data_9LYG
# 
_entry.id   9LYG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9LYG         pdb_00009lyg 10.2210/pdb9lyg/pdb 
WWPDB D_1300056829 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LYG 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ssugiyama@kochi-u.ac.jp 
_pdbx_contact_author.name_first         Shigeru 
_pdbx_contact_author.name_last          Sugiyama 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0563-6799 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kato, S.'       1 ? 
'Tsuchikawa, H.' 2 ? 
'Katoh, A.'      3 ? 
'Matsuoka, S.'   4 ? 
'Sugiyama, S.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kato, S.'       1 ? 
primary 'Tsuchikawa, H.' 2 ? 
primary 'Katoh, A.'      3 ? 
primary 'Matsuoka, S.'   4 ? 
primary 'Sugiyama, S.'   5 ? 
# 
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 'Peptidyl-prolyl cis-trans isomerase FKBP1A'                                                        12249.980 1 
5.2.1.8 ? ? ? 
2 non-polymer syn '5-[(2~{S})-1-cyclohexylsulfonylpiperidin-2-yl]-3-[3-(3,4-dimethoxyphenyl)propyl]-1,2,4-oxadiazole' 477.617   1 
?       ? ? ? 
3 non-polymer syn GLYCEROL                                                                                            92.094    2 
?       ? ? ? 
4 water       nat water                                                                                               18.015    
120 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;PPIase FKBP1A,12 kDa FK506-binding protein,12 kDa FKBP,FKBP-12,Calstabin-1,FK506-binding protein 1A,FKBP-1A,Immunophilin FKBP12,Rotamase
;
# 
_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       
;GSHMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTI
SPDYAYGATGHPGIIPPHATLVFDVELLKLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTI
SPDYAYGATGHPGIIPPHATLVFDVELLKLE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '5-[(2~{S})-1-cyclohexylsulfonylpiperidin-2-yl]-3-[3-(3,4-dimethoxyphenyl)propyl]-1,2,4-oxadiazole' A1L7S 
3 GLYCEROL                                                                                            GOL   
4 water                                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   GLY n 
1 6   VAL n 
1 7   GLN n 
1 8   VAL n 
1 9   GLU n 
1 10  THR n 
1 11  ILE n 
1 12  SER n 
1 13  PRO n 
1 14  GLY n 
1 15  ASP n 
1 16  GLY n 
1 17  ARG n 
1 18  THR n 
1 19  PHE n 
1 20  PRO n 
1 21  LYS n 
1 22  ARG n 
1 23  GLY n 
1 24  GLN n 
1 25  THR n 
1 26  CYS n 
1 27  VAL n 
1 28  VAL n 
1 29  HIS n 
1 30  TYR n 
1 31  THR n 
1 32  GLY n 
1 33  MET n 
1 34  LEU n 
1 35  GLU n 
1 36  ASP n 
1 37  GLY n 
1 38  LYS n 
1 39  LYS n 
1 40  PHE n 
1 41  ASP n 
1 42  SER n 
1 43  SER n 
1 44  ARG n 
1 45  ASP n 
1 46  ARG n 
1 47  ASN n 
1 48  LYS n 
1 49  PRO n 
1 50  PHE n 
1 51  LYS n 
1 52  PHE n 
1 53  MET n 
1 54  LEU n 
1 55  GLY n 
1 56  LYS n 
1 57  GLN n 
1 58  GLU n 
1 59  VAL n 
1 60  ILE n 
1 61  ARG n 
1 62  GLY n 
1 63  TRP n 
1 64  GLU n 
1 65  GLU n 
1 66  GLY n 
1 67  VAL n 
1 68  ALA n 
1 69  GLN n 
1 70  MET n 
1 71  SER n 
1 72  VAL n 
1 73  GLY n 
1 74  GLN n 
1 75  ARG n 
1 76  ALA n 
1 77  LYS n 
1 78  LEU n 
1 79  THR n 
1 80  ILE n 
1 81  SER n 
1 82  PRO n 
1 83  ASP n 
1 84  TYR n 
1 85  ALA n 
1 86  TYR n 
1 87  GLY n 
1 88  ALA n 
1 89  THR n 
1 90  GLY n 
1 91  HIS n 
1 92  PRO n 
1 93  GLY n 
1 94  ILE n 
1 95  ILE n 
1 96  PRO n 
1 97  PRO n 
1 98  HIS n 
1 99  ALA n 
1 100 THR n 
1 101 LEU n 
1 102 VAL n 
1 103 PHE n 
1 104 ASP n 
1 105 VAL n 
1 106 GLU n 
1 107 LEU n 
1 108 LEU n 
1 109 LYS n 
1 110 LEU n 
1 111 GLU 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                   111 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FKBP1A, FKBP1, FKBP12' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
A1L7S non-polymer         . '5-[(2~{S})-1-cyclohexylsulfonylpiperidin-2-yl]-3-[3-(3,4-dimethoxyphenyl)propyl]-1,2,4-oxadiazole' ? 
'C24 H35 N3 O5 S' 477.617 
ALA   'L-peptide linking' y ALANINE                                                                                             ? 
'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                                            ? 
'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                          ? 
'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                     ? 
'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                            ? 
'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                           ? 
'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                     ? 
'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                                             ? 
'C2 H5 N O2'      75.067  
GOL   non-polymer         . GLYCEROL                                                                                            
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
HIS   'L-peptide linking' y HISTIDINE                                                                                           ? 
'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                                               ? 
'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                          ? 
'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                             ? 
'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                              ? 
'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                          ? 
'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                       ? 
'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                             ? 
'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                              ? 
'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                           ? 
'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                          ? 
'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                            ? 
'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                              ? 
'C5 H11 N O2'     117.146 
# 
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   GLY 1   -3  ?   ?   ?   A . n 
A 1 2   SER 2   -2  ?   ?   ?   A . n 
A 1 3   HIS 3   -1  ?   ?   ?   A . n 
A 1 4   MET 4   0   ?   ?   ?   A . n 
A 1 5   GLY 5   1   1   GLY GLY A . n 
A 1 6   VAL 6   2   2   VAL VAL A . n 
A 1 7   GLN 7   3   3   GLN GLN A . n 
A 1 8   VAL 8   4   4   VAL VAL A . n 
A 1 9   GLU 9   5   5   GLU GLU A . n 
A 1 10  THR 10  6   6   THR THR A . n 
A 1 11  ILE 11  7   7   ILE ILE A . n 
A 1 12  SER 12  8   8   SER SER A . n 
A 1 13  PRO 13  9   9   PRO PRO A . n 
A 1 14  GLY 14  10  10  GLY GLY A . n 
A 1 15  ASP 15  11  11  ASP ASP A . n 
A 1 16  GLY 16  12  12  GLY GLY A . n 
A 1 17  ARG 17  13  13  ARG ARG A . n 
A 1 18  THR 18  14  14  THR THR A . n 
A 1 19  PHE 19  15  15  PHE PHE A . n 
A 1 20  PRO 20  16  16  PRO PRO A . n 
A 1 21  LYS 21  17  17  LYS LYS A . n 
A 1 22  ARG 22  18  18  ARG ARG A . n 
A 1 23  GLY 23  19  19  GLY GLY A . n 
A 1 24  GLN 24  20  20  GLN GLN A . n 
A 1 25  THR 25  21  21  THR THR A . n 
A 1 26  CYS 26  22  22  CYS CYS A . n 
A 1 27  VAL 27  23  23  VAL VAL A . n 
A 1 28  VAL 28  24  24  VAL VAL A . n 
A 1 29  HIS 29  25  25  HIS HIS A . n 
A 1 30  TYR 30  26  26  TYR TYR A . n 
A 1 31  THR 31  27  27  THR THR A . n 
A 1 32  GLY 32  28  28  GLY GLY A . n 
A 1 33  MET 33  29  29  MET MET A . n 
A 1 34  LEU 34  30  30  LEU LEU A . n 
A 1 35  GLU 35  31  31  GLU GLU A . n 
A 1 36  ASP 36  32  32  ASP ASP A . n 
A 1 37  GLY 37  33  33  GLY GLY A . n 
A 1 38  LYS 38  34  34  LYS LYS A . n 
A 1 39  LYS 39  35  35  LYS LYS A . n 
A 1 40  PHE 40  36  36  PHE PHE A . n 
A 1 41  ASP 41  37  37  ASP ASP A . n 
A 1 42  SER 42  38  38  SER SER A . n 
A 1 43  SER 43  39  39  SER SER A . n 
A 1 44  ARG 44  40  40  ARG ARG A . n 
A 1 45  ASP 45  41  41  ASP ASP A . n 
A 1 46  ARG 46  42  42  ARG ARG A . n 
A 1 47  ASN 47  43  43  ASN ASN A . n 
A 1 48  LYS 48  44  44  LYS LYS A . n 
A 1 49  PRO 49  45  45  PRO PRO A . n 
A 1 50  PHE 50  46  46  PHE PHE A . n 
A 1 51  LYS 51  47  47  LYS LYS A . n 
A 1 52  PHE 52  48  48  PHE PHE A . n 
A 1 53  MET 53  49  49  MET MET A . n 
A 1 54  LEU 54  50  50  LEU LEU A . n 
A 1 55  GLY 55  51  51  GLY GLY A . n 
A 1 56  LYS 56  52  52  LYS LYS A . n 
A 1 57  GLN 57  53  53  GLN GLN A . n 
A 1 58  GLU 58  54  54  GLU GLU A . n 
A 1 59  VAL 59  55  55  VAL VAL A . n 
A 1 60  ILE 60  56  56  ILE ILE A . n 
A 1 61  ARG 61  57  57  ARG ARG A . n 
A 1 62  GLY 62  58  58  GLY GLY A . n 
A 1 63  TRP 63  59  59  TRP TRP A . n 
A 1 64  GLU 64  60  60  GLU GLU A . n 
A 1 65  GLU 65  61  61  GLU GLU A . n 
A 1 66  GLY 66  62  62  GLY GLY A . n 
A 1 67  VAL 67  63  63  VAL VAL A . n 
A 1 68  ALA 68  64  64  ALA ALA A . n 
A 1 69  GLN 69  65  65  GLN GLN A . n 
A 1 70  MET 70  66  66  MET MET A . n 
A 1 71  SER 71  67  67  SER SER A . n 
A 1 72  VAL 72  68  68  VAL VAL A . n 
A 1 73  GLY 73  69  69  GLY GLY A . n 
A 1 74  GLN 74  70  70  GLN GLN A . n 
A 1 75  ARG 75  71  71  ARG ARG A . n 
A 1 76  ALA 76  72  72  ALA ALA A . n 
A 1 77  LYS 77  73  73  LYS LYS A . n 
A 1 78  LEU 78  74  74  LEU LEU A . n 
A 1 79  THR 79  75  75  THR THR A . n 
A 1 80  ILE 80  76  76  ILE ILE A . n 
A 1 81  SER 81  77  77  SER SER A . n 
A 1 82  PRO 82  78  78  PRO PRO A . n 
A 1 83  ASP 83  79  79  ASP ASP A . n 
A 1 84  TYR 84  80  80  TYR TYR A . n 
A 1 85  ALA 85  81  81  ALA ALA A . n 
A 1 86  TYR 86  82  82  TYR TYR A . n 
A 1 87  GLY 87  83  83  GLY GLY A . n 
A 1 88  ALA 88  84  84  ALA ALA A . n 
A 1 89  THR 89  85  85  THR THR A . n 
A 1 90  GLY 90  86  86  GLY GLY A . n 
A 1 91  HIS 91  87  87  HIS HIS A . n 
A 1 92  PRO 92  88  88  PRO PRO A . n 
A 1 93  GLY 93  89  89  GLY GLY A . n 
A 1 94  ILE 94  90  90  ILE ILE A . n 
A 1 95  ILE 95  91  91  ILE ILE A . n 
A 1 96  PRO 96  92  92  PRO PRO A . n 
A 1 97  PRO 97  93  93  PRO PRO A . n 
A 1 98  HIS 98  94  94  HIS HIS A . n 
A 1 99  ALA 99  95  95  ALA ALA A . n 
A 1 100 THR 100 96  96  THR THR A . n 
A 1 101 LEU 101 97  97  LEU LEU A . n 
A 1 102 VAL 102 98  98  VAL VAL A . n 
A 1 103 PHE 103 99  99  PHE PHE A . n 
A 1 104 ASP 104 100 100 ASP ASP A . n 
A 1 105 VAL 105 101 101 VAL VAL A . n 
A 1 106 GLU 106 102 102 GLU GLU A . n 
A 1 107 LEU 107 103 103 LEU LEU A . n 
A 1 108 LEU 108 104 104 LEU LEU A . n 
A 1 109 LYS 109 105 105 LYS LYS A . n 
A 1 110 LEU 110 106 106 LEU LEU A . n 
A 1 111 GLU 111 107 107 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L7S 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L7S 
_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 
B 2 A1L7S 1   201 201 A1L7S S20 A . 
C 3 GOL   1   202 301 GOL   GOL A . 
D 3 GOL   1   203 302 GOL   GOL A . 
E 4 HOH   1   301 13  HOH   HOH A . 
E 4 HOH   2   302 117 HOH   HOH A . 
E 4 HOH   3   303 116 HOH   HOH A . 
E 4 HOH   4   304 108 HOH   HOH A . 
E 4 HOH   5   305 75  HOH   HOH A . 
E 4 HOH   6   306 124 HOH   HOH A . 
E 4 HOH   7   307 14  HOH   HOH A . 
E 4 HOH   8   308 58  HOH   HOH A . 
E 4 HOH   9   309 63  HOH   HOH A . 
E 4 HOH   10  310 81  HOH   HOH A . 
E 4 HOH   11  311 92  HOH   HOH A . 
E 4 HOH   12  312 82  HOH   HOH A . 
E 4 HOH   13  313 94  HOH   HOH A . 
E 4 HOH   14  314 2   HOH   HOH A . 
E 4 HOH   15  315 4   HOH   HOH A . 
E 4 HOH   16  316 110 HOH   HOH A . 
E 4 HOH   17  317 7   HOH   HOH A . 
E 4 HOH   18  318 37  HOH   HOH A . 
E 4 HOH   19  319 73  HOH   HOH A . 
E 4 HOH   20  320 19  HOH   HOH A . 
E 4 HOH   21  321 62  HOH   HOH A . 
E 4 HOH   22  322 20  HOH   HOH A . 
E 4 HOH   23  323 68  HOH   HOH A . 
E 4 HOH   24  324 114 HOH   HOH A . 
E 4 HOH   25  325 55  HOH   HOH A . 
E 4 HOH   26  326 31  HOH   HOH A . 
E 4 HOH   27  327 64  HOH   HOH A . 
E 4 HOH   28  328 101 HOH   HOH A . 
E 4 HOH   29  329 39  HOH   HOH A . 
E 4 HOH   30  330 49  HOH   HOH A . 
E 4 HOH   31  331 9   HOH   HOH A . 
E 4 HOH   32  332 24  HOH   HOH A . 
E 4 HOH   33  333 27  HOH   HOH A . 
E 4 HOH   34  334 50  HOH   HOH A . 
E 4 HOH   35  335 12  HOH   HOH A . 
E 4 HOH   36  336 33  HOH   HOH A . 
E 4 HOH   37  337 47  HOH   HOH A . 
E 4 HOH   38  338 56  HOH   HOH A . 
E 4 HOH   39  339 25  HOH   HOH A . 
E 4 HOH   40  340 41  HOH   HOH A . 
E 4 HOH   41  341 8   HOH   HOH A . 
E 4 HOH   42  342 16  HOH   HOH A . 
E 4 HOH   43  343 30  HOH   HOH A . 
E 4 HOH   44  344 85  HOH   HOH A . 
E 4 HOH   45  345 77  HOH   HOH A . 
E 4 HOH   46  346 23  HOH   HOH A . 
E 4 HOH   47  347 91  HOH   HOH A . 
E 4 HOH   48  348 115 HOH   HOH A . 
E 4 HOH   49  349 57  HOH   HOH A . 
E 4 HOH   50  350 119 HOH   HOH A . 
E 4 HOH   51  351 34  HOH   HOH A . 
E 4 HOH   52  352 52  HOH   HOH A . 
E 4 HOH   53  353 84  HOH   HOH A . 
E 4 HOH   54  354 99  HOH   HOH A . 
E 4 HOH   55  355 60  HOH   HOH A . 
E 4 HOH   56  356 71  HOH   HOH A . 
E 4 HOH   57  357 21  HOH   HOH A . 
E 4 HOH   58  358 32  HOH   HOH A . 
E 4 HOH   59  359 29  HOH   HOH A . 
E 4 HOH   60  360 26  HOH   HOH A . 
E 4 HOH   61  361 69  HOH   HOH A . 
E 4 HOH   62  362 93  HOH   HOH A . 
E 4 HOH   63  363 44  HOH   HOH A . 
E 4 HOH   64  364 109 HOH   HOH A . 
E 4 HOH   65  365 15  HOH   HOH A . 
E 4 HOH   66  366 103 HOH   HOH A . 
E 4 HOH   67  367 70  HOH   HOH A . 
E 4 HOH   68  368 53  HOH   HOH A . 
E 4 HOH   69  369 48  HOH   HOH A . 
E 4 HOH   70  370 80  HOH   HOH A . 
E 4 HOH   71  371 66  HOH   HOH A . 
E 4 HOH   72  372 67  HOH   HOH A . 
E 4 HOH   73  373 86  HOH   HOH A . 
E 4 HOH   74  374 42  HOH   HOH A . 
E 4 HOH   75  375 76  HOH   HOH A . 
E 4 HOH   76  376 5   HOH   HOH A . 
E 4 HOH   77  377 104 HOH   HOH A . 
E 4 HOH   78  378 1   HOH   HOH A . 
E 4 HOH   79  379 122 HOH   HOH A . 
E 4 HOH   80  380 74  HOH   HOH A . 
E 4 HOH   81  381 102 HOH   HOH A . 
E 4 HOH   82  382 3   HOH   HOH A . 
E 4 HOH   83  383 28  HOH   HOH A . 
E 4 HOH   84  384 61  HOH   HOH A . 
E 4 HOH   85  385 95  HOH   HOH A . 
E 4 HOH   86  386 59  HOH   HOH A . 
E 4 HOH   87  387 106 HOH   HOH A . 
E 4 HOH   88  388 65  HOH   HOH A . 
E 4 HOH   89  389 36  HOH   HOH A . 
E 4 HOH   90  390 6   HOH   HOH A . 
E 4 HOH   91  391 54  HOH   HOH A . 
E 4 HOH   92  392 113 HOH   HOH A . 
E 4 HOH   93  393 40  HOH   HOH A . 
E 4 HOH   94  394 46  HOH   HOH A . 
E 4 HOH   95  395 120 HOH   HOH A . 
E 4 HOH   96  396 79  HOH   HOH A . 
E 4 HOH   97  397 17  HOH   HOH A . 
E 4 HOH   98  398 118 HOH   HOH A . 
E 4 HOH   99  399 35  HOH   HOH A . 
E 4 HOH   100 400 97  HOH   HOH A . 
E 4 HOH   101 401 123 HOH   HOH A . 
E 4 HOH   102 402 100 HOH   HOH A . 
E 4 HOH   103 403 72  HOH   HOH A . 
E 4 HOH   104 404 11  HOH   HOH A . 
E 4 HOH   105 405 88  HOH   HOH A . 
E 4 HOH   106 406 107 HOH   HOH A . 
E 4 HOH   107 407 90  HOH   HOH A . 
E 4 HOH   108 408 78  HOH   HOH A . 
E 4 HOH   109 409 121 HOH   HOH A . 
E 4 HOH   110 410 51  HOH   HOH A . 
E 4 HOH   111 411 18  HOH   HOH A . 
E 4 HOH   112 412 96  HOH   HOH A . 
E 4 HOH   113 413 87  HOH   HOH A . 
E 4 HOH   114 414 83  HOH   HOH A . 
E 4 HOH   115 415 111 HOH   HOH A . 
E 4 HOH   116 416 22  HOH   HOH A . 
E 4 HOH   117 417 89  HOH   HOH A . 
E 4 HOH   118 418 38  HOH   HOH A . 
E 4 HOH   119 419 105 HOH   HOH A . 
E 4 HOH   120 420 112 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0238 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LYG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     31.577 
_cell.length_a_esd                 ? 
_cell.length_b                     48.039 
_cell.length_b_esd                 ? 
_cell.length_c                     65.306 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9LYG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9LYG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.16 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris-HCl (pH8.0), 3.0 M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2025-02-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LYG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.26 
_reflns.d_resolution_low                               38.70 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27488 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                17.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.161 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.26 
_reflns_shell.d_res_low                                     1.28 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1375 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.643 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.87 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.56 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.43 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               11.591 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LYG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.26 
_refine.ls_d_res_low                             38.70 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     26041 
_refine.ls_number_reflns_R_free                  1324 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.33 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14889 
_refine.ls_R_factor_R_free                       0.18808 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14698 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2PPN 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.052 
_refine.pdbx_overall_ESU_R_Free                  0.051 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.675 
_refine.overall_SU_ML                            0.034 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.26 
_refine_hist.d_res_low                        38.70 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               997 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        832 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.013  1070 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  1006 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.913  1.710  1465 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.427  1.643  2370 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.745  5.000  140  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 31.373 22.157 51   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.857 15.000 183  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.071 15.000 7    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.224  0.200  128  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  1244 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  216  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.341  0.917  518  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.318  0.913  517  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.909  1.386  672  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.912  1.389  673  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.099  1.177  552  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.097  1.178  553  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.715  1.655  794  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.857  12.632 1184 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.451  11.857 1149 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 2.769  3.000  2076 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.260 
_refine_ls_shell.d_res_low                           1.293 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                113 
_refine_ls_shell.number_reflns_R_work                1835 
_refine_ls_shell.percent_reflns_obs                  98.38 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.208 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.255 
# 
_struct.entry_id                     9LYG 
_struct.title                        'Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9LYG 
_struct_keywords.text            
'FK506-binding protein, FKBP12, complex, binding protein, PPIase, peptidyl-prolyl cis-trans isomerase, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FKB1A_HUMAN 
_struct_ref.pdbx_db_accession          P62942 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPD
YAYGATGHPGIIPPHATLVFDVELLKLE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9LYG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 111 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P62942 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       107 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9LYG GLY A 1 ? UNP P62942 ? ? 'expression tag' -3 1 
1 9LYG SER A 2 ? UNP P62942 ? ? 'expression tag' -2 2 
1 9LYG HIS A 3 ? UNP P62942 ? ? 'expression tag' -1 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 410  ? 
1 MORE         -1   ? 
1 'SSA (A^2)'  6060 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ARG A 44 ? ASN A 47 ? ARG A 40 ASN A 43 5 ? 4  
HELX_P HELX_P2 AA2 ILE A 60 ? GLN A 69 ? ILE A 56 GLN A 65 1 ? 10 
HELX_P HELX_P3 AA3 PRO A 82 ? ALA A 85 ? PRO A 78 ALA A 81 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
# 
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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? 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 VAL A 6   ? SER A 12  ? VAL A 2  SER A 8   
AA1 2 ARG A 75  ? ILE A 80  ? ARG A 71 ILE A 76  
AA1 3 LEU A 101 ? GLU A 111 ? LEU A 97 GLU A 107 
AA1 4 THR A 25  ? LEU A 34  ? THR A 21 LEU A 30  
AA1 5 LYS A 39  ? SER A 42  ? LYS A 35 SER A 38  
AA2 1 VAL A 6   ? SER A 12  ? VAL A 2  SER A 8   
AA2 2 ARG A 75  ? ILE A 80  ? ARG A 71 ILE A 76  
AA2 3 LEU A 101 ? GLU A 111 ? LEU A 97 GLU A 107 
AA2 4 THR A 25  ? LEU A 34  ? THR A 21 LEU A 30  
AA2 5 PHE A 50  ? MET A 53  ? PHE A 46 MET A 49  
# 
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 11  ? N ILE A 7  O ARG A 75  ? O ARG A 71  
AA1 2 3 N ALA A 76  ? N ALA A 72 O VAL A 105 ? O VAL A 101 
AA1 3 4 O VAL A 102 ? O VAL A 98 N MET A 33  ? N MET A 29  
AA1 4 5 N GLY A 32  ? N GLY A 28 O ASP A 41  ? O ASP A 37  
AA2 1 2 N ILE A 11  ? N ILE A 7  O ARG A 75  ? O ARG A 71  
AA2 2 3 N ALA A 76  ? N ALA A 72 O VAL A 105 ? O VAL A 101 
AA2 3 4 O VAL A 102 ? O VAL A 98 N MET A 33  ? N MET A 29  
AA2 4 5 N CYS A 26  ? N CYS A 22 O PHE A 52  ? O PHE A 48  
# 
_pdbx_entry_details.entry_id                   9LYG 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 13 ? A -140.46 -29.01  
2 1 ALA A 81 ? ? -127.30 -121.02 
3 1 PRO A 88 ? B -35.45  125.07  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             HIS 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              87 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   13.25 
# 
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 GLY -3 ? A GLY 1 
2 1 Y 1 A SER -2 ? A SER 2 
3 1 Y 1 A HIS -1 ? A HIS 3 
4 1 Y 1 A MET 0  ? A MET 4 
# 
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 
A1L7S C1   C N S 1   
A1L7S C3   C Y N 2   
A1L7S C12  C Y N 3   
A1L7S C13  C N N 4   
A1L7S C14  C N N 5   
A1L7S C15  C N N 6   
A1L7S C16  C N N 7   
A1L7S C17  C Y N 8   
A1L7S C18  C Y N 9   
A1L7S C19  C Y N 10  
A1L7S C25  C N N 11  
A1L7S C26  C N N 12  
A1L7S C27  C N N 13  
A1L7S C28  C N N 14  
A1L7S C29  C N N 15  
A1L7S O24  O N N 16  
A1L7S S22  S N N 17  
A1L7S O23  O N N 18  
A1L7S C30  C N N 19  
A1L7S N2   N N N 20  
A1L7S O6   O Y N 21  
A1L7S N7   N Y N 22  
A1L7S C8   C Y N 23  
A1L7S N5   N Y N 24  
A1L7S C9   C N N 25  
A1L7S C10  C N N 26  
A1L7S C11  C N N 27  
A1L7S C21  C Y N 28  
A1L7S C20  C Y N 29  
A1L7S O33  O N N 30  
A1L7S C34  C N N 31  
A1L7S O31  O N N 32  
A1L7S C32  C N N 33  
A1L7S H1   H N N 34  
A1L7S H2   H N N 35  
A1L7S H3   H N N 36  
A1L7S H4   H N N 37  
A1L7S H5   H N N 38  
A1L7S H6   H N N 39  
A1L7S H7   H N N 40  
A1L7S H8   H N N 41  
A1L7S H9   H N N 42  
A1L7S H10  H N N 43  
A1L7S H11  H N N 44  
A1L7S H12  H N N 45  
A1L7S H13  H N N 46  
A1L7S H14  H N N 47  
A1L7S H15  H N N 48  
A1L7S H16  H N N 49  
A1L7S H17  H N N 50  
A1L7S H18  H N N 51  
A1L7S H19  H N N 52  
A1L7S H20  H N N 53  
A1L7S H21  H N N 54  
A1L7S H22  H N N 55  
A1L7S H23  H N N 56  
A1L7S H24  H N N 57  
A1L7S H25  H N N 58  
A1L7S H26  H N N 59  
A1L7S H27  H N N 60  
A1L7S H28  H N N 61  
A1L7S H29  H N N 62  
A1L7S H30  H N N 63  
A1L7S H31  H N N 64  
A1L7S H32  H N N 65  
A1L7S H33  H N N 66  
A1L7S H34  H N N 67  
A1L7S H35  H N N 68  
ALA   N    N N N 69  
ALA   CA   C N S 70  
ALA   C    C N N 71  
ALA   O    O N N 72  
ALA   CB   C N N 73  
ALA   OXT  O N N 74  
ALA   H    H N N 75  
ALA   H2   H N N 76  
ALA   HA   H N N 77  
ALA   HB1  H N N 78  
ALA   HB2  H N N 79  
ALA   HB3  H N N 80  
ALA   HXT  H N N 81  
ARG   N    N N N 82  
ARG   CA   C N S 83  
ARG   C    C N N 84  
ARG   O    O N N 85  
ARG   CB   C N N 86  
ARG   CG   C N N 87  
ARG   CD   C N N 88  
ARG   NE   N N N 89  
ARG   CZ   C N N 90  
ARG   NH1  N N N 91  
ARG   NH2  N N N 92  
ARG   OXT  O N N 93  
ARG   H    H N N 94  
ARG   H2   H N N 95  
ARG   HA   H N N 96  
ARG   HB2  H N N 97  
ARG   HB3  H N N 98  
ARG   HG2  H N N 99  
ARG   HG3  H N N 100 
ARG   HD2  H N N 101 
ARG   HD3  H N N 102 
ARG   HE   H N N 103 
ARG   HH11 H N N 104 
ARG   HH12 H N N 105 
ARG   HH21 H N N 106 
ARG   HH22 H N N 107 
ARG   HXT  H N N 108 
ASN   N    N N N 109 
ASN   CA   C N S 110 
ASN   C    C N N 111 
ASN   O    O N N 112 
ASN   CB   C N N 113 
ASN   CG   C N N 114 
ASN   OD1  O N N 115 
ASN   ND2  N N N 116 
ASN   OXT  O N N 117 
ASN   H    H N N 118 
ASN   H2   H N N 119 
ASN   HA   H N N 120 
ASN   HB2  H N N 121 
ASN   HB3  H N N 122 
ASN   HD21 H N N 123 
ASN   HD22 H N N 124 
ASN   HXT  H N N 125 
ASP   N    N N N 126 
ASP   CA   C N S 127 
ASP   C    C N N 128 
ASP   O    O N N 129 
ASP   CB   C N N 130 
ASP   CG   C N N 131 
ASP   OD1  O N N 132 
ASP   OD2  O N N 133 
ASP   OXT  O N N 134 
ASP   H    H N N 135 
ASP   H2   H N N 136 
ASP   HA   H N N 137 
ASP   HB2  H N N 138 
ASP   HB3  H N N 139 
ASP   HD2  H N N 140 
ASP   HXT  H N N 141 
CYS   N    N N N 142 
CYS   CA   C N R 143 
CYS   C    C N N 144 
CYS   O    O N N 145 
CYS   CB   C N N 146 
CYS   SG   S N N 147 
CYS   OXT  O N N 148 
CYS   H    H N N 149 
CYS   H2   H N N 150 
CYS   HA   H N N 151 
CYS   HB2  H N N 152 
CYS   HB3  H N N 153 
CYS   HG   H N N 154 
CYS   HXT  H N N 155 
GLN   N    N N N 156 
GLN   CA   C N S 157 
GLN   C    C N N 158 
GLN   O    O N N 159 
GLN   CB   C N N 160 
GLN   CG   C N N 161 
GLN   CD   C N N 162 
GLN   OE1  O N N 163 
GLN   NE2  N N N 164 
GLN   OXT  O N N 165 
GLN   H    H N N 166 
GLN   H2   H N N 167 
GLN   HA   H N N 168 
GLN   HB2  H N N 169 
GLN   HB3  H N N 170 
GLN   HG2  H N N 171 
GLN   HG3  H N N 172 
GLN   HE21 H N N 173 
GLN   HE22 H N N 174 
GLN   HXT  H N N 175 
GLU   N    N N N 176 
GLU   CA   C N S 177 
GLU   C    C N N 178 
GLU   O    O N N 179 
GLU   CB   C N N 180 
GLU   CG   C N N 181 
GLU   CD   C N N 182 
GLU   OE1  O N N 183 
GLU   OE2  O N N 184 
GLU   OXT  O N N 185 
GLU   H    H N N 186 
GLU   H2   H N N 187 
GLU   HA   H N N 188 
GLU   HB2  H N N 189 
GLU   HB3  H N N 190 
GLU   HG2  H N N 191 
GLU   HG3  H N N 192 
GLU   HE2  H N N 193 
GLU   HXT  H N N 194 
GLY   N    N N N 195 
GLY   CA   C N N 196 
GLY   C    C N N 197 
GLY   O    O N N 198 
GLY   OXT  O N N 199 
GLY   H    H N N 200 
GLY   H2   H N N 201 
GLY   HA2  H N N 202 
GLY   HA3  H N N 203 
GLY   HXT  H N N 204 
GOL   C1   C N N 205 
GOL   O1   O N N 206 
GOL   C2   C N N 207 
GOL   O2   O N N 208 
GOL   C3   C N N 209 
GOL   O3   O N N 210 
GOL   H11  H N N 211 
GOL   H12  H N N 212 
GOL   HO1  H N N 213 
GOL   H2   H N N 214 
GOL   HO2  H N N 215 
GOL   H31  H N N 216 
GOL   H32  H N N 217 
GOL   HO3  H N N 218 
HIS   N    N N N 219 
HIS   CA   C N S 220 
HIS   C    C N N 221 
HIS   O    O N N 222 
HIS   CB   C N N 223 
HIS   CG   C Y N 224 
HIS   ND1  N Y N 225 
HIS   CD2  C Y N 226 
HIS   CE1  C Y N 227 
HIS   NE2  N Y N 228 
HIS   OXT  O N N 229 
HIS   H    H N N 230 
HIS   H2   H N N 231 
HIS   HA   H N N 232 
HIS   HB2  H N N 233 
HIS   HB3  H N N 234 
HIS   HD1  H N N 235 
HIS   HD2  H N N 236 
HIS   HE1  H N N 237 
HIS   HE2  H N N 238 
HIS   HXT  H N N 239 
HOH   O    O N N 240 
HOH   H1   H N N 241 
HOH   H2   H N N 242 
ILE   N    N N N 243 
ILE   CA   C N S 244 
ILE   C    C N N 245 
ILE   O    O N N 246 
ILE   CB   C N S 247 
ILE   CG1  C N N 248 
ILE   CG2  C N N 249 
ILE   CD1  C N N 250 
ILE   OXT  O N N 251 
ILE   H    H N N 252 
ILE   H2   H N N 253 
ILE   HA   H N N 254 
ILE   HB   H N N 255 
ILE   HG12 H N N 256 
ILE   HG13 H N N 257 
ILE   HG21 H N N 258 
ILE   HG22 H N N 259 
ILE   HG23 H N N 260 
ILE   HD11 H N N 261 
ILE   HD12 H N N 262 
ILE   HD13 H N N 263 
ILE   HXT  H N N 264 
LEU   N    N N N 265 
LEU   CA   C N S 266 
LEU   C    C N N 267 
LEU   O    O N N 268 
LEU   CB   C N N 269 
LEU   CG   C N N 270 
LEU   CD1  C N N 271 
LEU   CD2  C N N 272 
LEU   OXT  O N N 273 
LEU   H    H N N 274 
LEU   H2   H N N 275 
LEU   HA   H N N 276 
LEU   HB2  H N N 277 
LEU   HB3  H N N 278 
LEU   HG   H N N 279 
LEU   HD11 H N N 280 
LEU   HD12 H N N 281 
LEU   HD13 H N N 282 
LEU   HD21 H N N 283 
LEU   HD22 H N N 284 
LEU   HD23 H N N 285 
LEU   HXT  H N N 286 
LYS   N    N N N 287 
LYS   CA   C N S 288 
LYS   C    C N N 289 
LYS   O    O N N 290 
LYS   CB   C N N 291 
LYS   CG   C N N 292 
LYS   CD   C N N 293 
LYS   CE   C N N 294 
LYS   NZ   N N N 295 
LYS   OXT  O N N 296 
LYS   H    H N N 297 
LYS   H2   H N N 298 
LYS   HA   H N N 299 
LYS   HB2  H N N 300 
LYS   HB3  H N N 301 
LYS   HG2  H N N 302 
LYS   HG3  H N N 303 
LYS   HD2  H N N 304 
LYS   HD3  H N N 305 
LYS   HE2  H N N 306 
LYS   HE3  H N N 307 
LYS   HZ1  H N N 308 
LYS   HZ2  H N N 309 
LYS   HZ3  H N N 310 
LYS   HXT  H N N 311 
MET   N    N N N 312 
MET   CA   C N S 313 
MET   C    C N N 314 
MET   O    O N N 315 
MET   CB   C N N 316 
MET   CG   C N N 317 
MET   SD   S N N 318 
MET   CE   C N N 319 
MET   OXT  O N N 320 
MET   H    H N N 321 
MET   H2   H N N 322 
MET   HA   H N N 323 
MET   HB2  H N N 324 
MET   HB3  H N N 325 
MET   HG2  H N N 326 
MET   HG3  H N N 327 
MET   HE1  H N N 328 
MET   HE2  H N N 329 
MET   HE3  H N N 330 
MET   HXT  H N N 331 
PHE   N    N N N 332 
PHE   CA   C N S 333 
PHE   C    C N N 334 
PHE   O    O N N 335 
PHE   CB   C N N 336 
PHE   CG   C Y N 337 
PHE   CD1  C Y N 338 
PHE   CD2  C Y N 339 
PHE   CE1  C Y N 340 
PHE   CE2  C Y N 341 
PHE   CZ   C Y N 342 
PHE   OXT  O N N 343 
PHE   H    H N N 344 
PHE   H2   H N N 345 
PHE   HA   H N N 346 
PHE   HB2  H N N 347 
PHE   HB3  H N N 348 
PHE   HD1  H N N 349 
PHE   HD2  H N N 350 
PHE   HE1  H N N 351 
PHE   HE2  H N N 352 
PHE   HZ   H N N 353 
PHE   HXT  H N N 354 
PRO   N    N N N 355 
PRO   CA   C N S 356 
PRO   C    C N N 357 
PRO   O    O N N 358 
PRO   CB   C N N 359 
PRO   CG   C N N 360 
PRO   CD   C N N 361 
PRO   OXT  O N N 362 
PRO   H    H N N 363 
PRO   HA   H N N 364 
PRO   HB2  H N N 365 
PRO   HB3  H N N 366 
PRO   HG2  H N N 367 
PRO   HG3  H N N 368 
PRO   HD2  H N N 369 
PRO   HD3  H N N 370 
PRO   HXT  H N N 371 
SER   N    N N N 372 
SER   CA   C N S 373 
SER   C    C N N 374 
SER   O    O N N 375 
SER   CB   C N N 376 
SER   OG   O N N 377 
SER   OXT  O N N 378 
SER   H    H N N 379 
SER   H2   H N N 380 
SER   HA   H N N 381 
SER   HB2  H N N 382 
SER   HB3  H N N 383 
SER   HG   H N N 384 
SER   HXT  H N N 385 
THR   N    N N N 386 
THR   CA   C N S 387 
THR   C    C N N 388 
THR   O    O N N 389 
THR   CB   C N R 390 
THR   OG1  O N N 391 
THR   CG2  C N N 392 
THR   OXT  O N N 393 
THR   H    H N N 394 
THR   H2   H N N 395 
THR   HA   H N N 396 
THR   HB   H N N 397 
THR   HG1  H N N 398 
THR   HG21 H N N 399 
THR   HG22 H N N 400 
THR   HG23 H N N 401 
THR   HXT  H N N 402 
TRP   N    N N N 403 
TRP   CA   C N S 404 
TRP   C    C N N 405 
TRP   O    O N N 406 
TRP   CB   C N N 407 
TRP   CG   C Y N 408 
TRP   CD1  C Y N 409 
TRP   CD2  C Y N 410 
TRP   NE1  N Y N 411 
TRP   CE2  C Y N 412 
TRP   CE3  C Y N 413 
TRP   CZ2  C Y N 414 
TRP   CZ3  C Y N 415 
TRP   CH2  C Y N 416 
TRP   OXT  O N N 417 
TRP   H    H N N 418 
TRP   H2   H N N 419 
TRP   HA   H N N 420 
TRP   HB2  H N N 421 
TRP   HB3  H N N 422 
TRP   HD1  H N N 423 
TRP   HE1  H N N 424 
TRP   HE3  H N N 425 
TRP   HZ2  H N N 426 
TRP   HZ3  H N N 427 
TRP   HH2  H N N 428 
TRP   HXT  H N N 429 
TYR   N    N N N 430 
TYR   CA   C N S 431 
TYR   C    C N N 432 
TYR   O    O N N 433 
TYR   CB   C N N 434 
TYR   CG   C Y N 435 
TYR   CD1  C Y N 436 
TYR   CD2  C Y N 437 
TYR   CE1  C Y N 438 
TYR   CE2  C Y N 439 
TYR   CZ   C Y N 440 
TYR   OH   O N N 441 
TYR   OXT  O N N 442 
TYR   H    H N N 443 
TYR   H2   H N N 444 
TYR   HA   H N N 445 
TYR   HB2  H N N 446 
TYR   HB3  H N N 447 
TYR   HD1  H N N 448 
TYR   HD2  H N N 449 
TYR   HE1  H N N 450 
TYR   HE2  H N N 451 
TYR   HH   H N N 452 
TYR   HXT  H N N 453 
VAL   N    N N N 454 
VAL   CA   C N S 455 
VAL   C    C N N 456 
VAL   O    O N N 457 
VAL   CB   C N N 458 
VAL   CG1  C N N 459 
VAL   CG2  C N N 460 
VAL   OXT  O N N 461 
VAL   H    H N N 462 
VAL   H2   H N N 463 
VAL   HA   H N N 464 
VAL   HB   H N N 465 
VAL   HG11 H N N 466 
VAL   HG12 H N N 467 
VAL   HG13 H N N 468 
VAL   HG21 H N N 469 
VAL   HG22 H N N 470 
VAL   HG23 H N N 471 
VAL   HXT  H N N 472 
# 
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 
A1L7S C17 C18  doub Y N 1   
A1L7S C17 C12  sing Y N 2   
A1L7S C9  C8   sing N N 3   
A1L7S C9  C10  sing N N 4   
A1L7S C11 C10  sing N N 5   
A1L7S C11 C12  sing N N 6   
A1L7S C18 C19  sing Y N 7   
A1L7S C14 C15  sing N N 8   
A1L7S C14 C13  sing N N 9   
A1L7S N7  C8   doub Y N 10  
A1L7S N7  O6   sing Y N 11  
A1L7S C8  N5   sing Y N 12  
A1L7S C15 C16  sing N N 13  
A1L7S C12 C21  doub Y N 14  
A1L7S O6  C3   sing Y N 15  
A1L7S C16 N2   sing N N 16  
A1L7S N5  C3   doub Y N 17  
A1L7S C32 O31  sing N N 18  
A1L7S C3  C1   sing N N 19  
A1L7S C19 O31  sing N N 20  
A1L7S C19 C20  doub Y N 21  
A1L7S C13 C1   sing N N 22  
A1L7S C21 C20  sing Y N 23  
A1L7S C1  N2   sing N N 24  
A1L7S N2  S22  sing N N 25  
A1L7S C20 O33  sing N N 26  
A1L7S C30 C29  sing N N 27  
A1L7S C30 C25  sing N N 28  
A1L7S C29 C28  sing N N 29  
A1L7S S22 C25  sing N N 30  
A1L7S S22 O23  doub N N 31  
A1L7S S22 O24  doub N N 32  
A1L7S O33 C34  sing N N 33  
A1L7S C25 C26  sing N N 34  
A1L7S C28 C27  sing N N 35  
A1L7S C26 C27  sing N N 36  
A1L7S C1  H1   sing N N 37  
A1L7S C13 H2   sing N N 38  
A1L7S C13 H3   sing N N 39  
A1L7S C14 H4   sing N N 40  
A1L7S C14 H5   sing N N 41  
A1L7S C15 H6   sing N N 42  
A1L7S C15 H7   sing N N 43  
A1L7S C16 H8   sing N N 44  
A1L7S C16 H9   sing N N 45  
A1L7S C17 H10  sing N N 46  
A1L7S C18 H11  sing N N 47  
A1L7S C25 H12  sing N N 48  
A1L7S C26 H13  sing N N 49  
A1L7S C26 H14  sing N N 50  
A1L7S C27 H15  sing N N 51  
A1L7S C27 H16  sing N N 52  
A1L7S C28 H17  sing N N 53  
A1L7S C28 H18  sing N N 54  
A1L7S C29 H19  sing N N 55  
A1L7S C29 H20  sing N N 56  
A1L7S C30 H21  sing N N 57  
A1L7S C30 H22  sing N N 58  
A1L7S C9  H23  sing N N 59  
A1L7S C9  H24  sing N N 60  
A1L7S C10 H25  sing N N 61  
A1L7S C10 H26  sing N N 62  
A1L7S C11 H27  sing N N 63  
A1L7S C11 H28  sing N N 64  
A1L7S C21 H29  sing N N 65  
A1L7S C34 H30  sing N N 66  
A1L7S C34 H31  sing N N 67  
A1L7S C34 H32  sing N N 68  
A1L7S C32 H33  sing N N 69  
A1L7S C32 H34  sing N N 70  
A1L7S C32 H35  sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
GOL   C1  O1   sing N N 200 
GOL   C1  C2   sing N N 201 
GOL   C1  H11  sing N N 202 
GOL   C1  H12  sing N N 203 
GOL   O1  HO1  sing N N 204 
GOL   C2  O2   sing N N 205 
GOL   C2  C3   sing N N 206 
GOL   C2  H2   sing N N 207 
GOL   O2  HO2  sing N N 208 
GOL   C3  O3   sing N N 209 
GOL   C3  H31  sing N N 210 
GOL   C3  H32  sing N N 211 
GOL   O3  HO3  sing N N 212 
HIS   N   CA   sing N N 213 
HIS   N   H    sing N N 214 
HIS   N   H2   sing N N 215 
HIS   CA  C    sing N N 216 
HIS   CA  CB   sing N N 217 
HIS   CA  HA   sing N N 218 
HIS   C   O    doub N N 219 
HIS   C   OXT  sing N N 220 
HIS   CB  CG   sing N N 221 
HIS   CB  HB2  sing N N 222 
HIS   CB  HB3  sing N N 223 
HIS   CG  ND1  sing Y N 224 
HIS   CG  CD2  doub Y N 225 
HIS   ND1 CE1  doub Y N 226 
HIS   ND1 HD1  sing N N 227 
HIS   CD2 NE2  sing Y N 228 
HIS   CD2 HD2  sing N N 229 
HIS   CE1 NE2  sing Y N 230 
HIS   CE1 HE1  sing N N 231 
HIS   NE2 HE2  sing N N 232 
HIS   OXT HXT  sing N N 233 
HOH   O   H1   sing N N 234 
HOH   O   H2   sing N N 235 
ILE   N   CA   sing N N 236 
ILE   N   H    sing N N 237 
ILE   N   H2   sing N N 238 
ILE   CA  C    sing N N 239 
ILE   CA  CB   sing N N 240 
ILE   CA  HA   sing N N 241 
ILE   C   O    doub N N 242 
ILE   C   OXT  sing N N 243 
ILE   CB  CG1  sing N N 244 
ILE   CB  CG2  sing N N 245 
ILE   CB  HB   sing N N 246 
ILE   CG1 CD1  sing N N 247 
ILE   CG1 HG12 sing N N 248 
ILE   CG1 HG13 sing N N 249 
ILE   CG2 HG21 sing N N 250 
ILE   CG2 HG22 sing N N 251 
ILE   CG2 HG23 sing N N 252 
ILE   CD1 HD11 sing N N 253 
ILE   CD1 HD12 sing N N 254 
ILE   CD1 HD13 sing N N 255 
ILE   OXT HXT  sing N N 256 
LEU   N   CA   sing N N 257 
LEU   N   H    sing N N 258 
LEU   N   H2   sing N N 259 
LEU   CA  C    sing N N 260 
LEU   CA  CB   sing N N 261 
LEU   CA  HA   sing N N 262 
LEU   C   O    doub N N 263 
LEU   C   OXT  sing N N 264 
LEU   CB  CG   sing N N 265 
LEU   CB  HB2  sing N N 266 
LEU   CB  HB3  sing N N 267 
LEU   CG  CD1  sing N N 268 
LEU   CG  CD2  sing N N 269 
LEU   CG  HG   sing N N 270 
LEU   CD1 HD11 sing N N 271 
LEU   CD1 HD12 sing N N 272 
LEU   CD1 HD13 sing N N 273 
LEU   CD2 HD21 sing N N 274 
LEU   CD2 HD22 sing N N 275 
LEU   CD2 HD23 sing N N 276 
LEU   OXT HXT  sing N N 277 
LYS   N   CA   sing N N 278 
LYS   N   H    sing N N 279 
LYS   N   H2   sing N N 280 
LYS   CA  C    sing N N 281 
LYS   CA  CB   sing N N 282 
LYS   CA  HA   sing N N 283 
LYS   C   O    doub N N 284 
LYS   C   OXT  sing N N 285 
LYS   CB  CG   sing N N 286 
LYS   CB  HB2  sing N N 287 
LYS   CB  HB3  sing N N 288 
LYS   CG  CD   sing N N 289 
LYS   CG  HG2  sing N N 290 
LYS   CG  HG3  sing N N 291 
LYS   CD  CE   sing N N 292 
LYS   CD  HD2  sing N N 293 
LYS   CD  HD3  sing N N 294 
LYS   CE  NZ   sing N N 295 
LYS   CE  HE2  sing N N 296 
LYS   CE  HE3  sing N N 297 
LYS   NZ  HZ1  sing N N 298 
LYS   NZ  HZ2  sing N N 299 
LYS   NZ  HZ3  sing N N 300 
LYS   OXT HXT  sing N N 301 
MET   N   CA   sing N N 302 
MET   N   H    sing N N 303 
MET   N   H2   sing N N 304 
MET   CA  C    sing N N 305 
MET   CA  CB   sing N N 306 
MET   CA  HA   sing N N 307 
MET   C   O    doub N N 308 
MET   C   OXT  sing N N 309 
MET   CB  CG   sing N N 310 
MET   CB  HB2  sing N N 311 
MET   CB  HB3  sing N N 312 
MET   CG  SD   sing N N 313 
MET   CG  HG2  sing N N 314 
MET   CG  HG3  sing N N 315 
MET   SD  CE   sing N N 316 
MET   CE  HE1  sing N N 317 
MET   CE  HE2  sing N N 318 
MET   CE  HE3  sing N N 319 
MET   OXT HXT  sing N N 320 
PHE   N   CA   sing N N 321 
PHE   N   H    sing N N 322 
PHE   N   H2   sing N N 323 
PHE   CA  C    sing N N 324 
PHE   CA  CB   sing N N 325 
PHE   CA  HA   sing N N 326 
PHE   C   O    doub N N 327 
PHE   C   OXT  sing N N 328 
PHE   CB  CG   sing N N 329 
PHE   CB  HB2  sing N N 330 
PHE   CB  HB3  sing N N 331 
PHE   CG  CD1  doub Y N 332 
PHE   CG  CD2  sing Y N 333 
PHE   CD1 CE1  sing Y N 334 
PHE   CD1 HD1  sing N N 335 
PHE   CD2 CE2  doub Y N 336 
PHE   CD2 HD2  sing N N 337 
PHE   CE1 CZ   doub Y N 338 
PHE   CE1 HE1  sing N N 339 
PHE   CE2 CZ   sing Y N 340 
PHE   CE2 HE2  sing N N 341 
PHE   CZ  HZ   sing N N 342 
PHE   OXT HXT  sing N N 343 
PRO   N   CA   sing N N 344 
PRO   N   CD   sing N N 345 
PRO   N   H    sing N N 346 
PRO   CA  C    sing N N 347 
PRO   CA  CB   sing N N 348 
PRO   CA  HA   sing N N 349 
PRO   C   O    doub N N 350 
PRO   C   OXT  sing N N 351 
PRO   CB  CG   sing N N 352 
PRO   CB  HB2  sing N N 353 
PRO   CB  HB3  sing N N 354 
PRO   CG  CD   sing N N 355 
PRO   CG  HG2  sing N N 356 
PRO   CG  HG3  sing N N 357 
PRO   CD  HD2  sing N N 358 
PRO   CD  HD3  sing N N 359 
PRO   OXT HXT  sing N N 360 
SER   N   CA   sing N N 361 
SER   N   H    sing N N 362 
SER   N   H2   sing N N 363 
SER   CA  C    sing N N 364 
SER   CA  CB   sing N N 365 
SER   CA  HA   sing N N 366 
SER   C   O    doub N N 367 
SER   C   OXT  sing N N 368 
SER   CB  OG   sing N N 369 
SER   CB  HB2  sing N N 370 
SER   CB  HB3  sing N N 371 
SER   OG  HG   sing N N 372 
SER   OXT HXT  sing N N 373 
THR   N   CA   sing N N 374 
THR   N   H    sing N N 375 
THR   N   H2   sing N N 376 
THR   CA  C    sing N N 377 
THR   CA  CB   sing N N 378 
THR   CA  HA   sing N N 379 
THR   C   O    doub N N 380 
THR   C   OXT  sing N N 381 
THR   CB  OG1  sing N N 382 
THR   CB  CG2  sing N N 383 
THR   CB  HB   sing N N 384 
THR   OG1 HG1  sing N N 385 
THR   CG2 HG21 sing N N 386 
THR   CG2 HG22 sing N N 387 
THR   CG2 HG23 sing N N 388 
THR   OXT HXT  sing N N 389 
TRP   N   CA   sing N N 390 
TRP   N   H    sing N N 391 
TRP   N   H2   sing N N 392 
TRP   CA  C    sing N N 393 
TRP   CA  CB   sing N N 394 
TRP   CA  HA   sing N N 395 
TRP   C   O    doub N N 396 
TRP   C   OXT  sing N N 397 
TRP   CB  CG   sing N N 398 
TRP   CB  HB2  sing N N 399 
TRP   CB  HB3  sing N N 400 
TRP   CG  CD1  doub Y N 401 
TRP   CG  CD2  sing Y N 402 
TRP   CD1 NE1  sing Y N 403 
TRP   CD1 HD1  sing N N 404 
TRP   CD2 CE2  doub Y N 405 
TRP   CD2 CE3  sing Y N 406 
TRP   NE1 CE2  sing Y N 407 
TRP   NE1 HE1  sing N N 408 
TRP   CE2 CZ2  sing Y N 409 
TRP   CE3 CZ3  doub Y N 410 
TRP   CE3 HE3  sing N N 411 
TRP   CZ2 CH2  doub Y N 412 
TRP   CZ2 HZ2  sing N N 413 
TRP   CZ3 CH2  sing Y N 414 
TRP   CZ3 HZ3  sing N N 415 
TRP   CH2 HH2  sing N N 416 
TRP   OXT HXT  sing N N 417 
TYR   N   CA   sing N N 418 
TYR   N   H    sing N N 419 
TYR   N   H2   sing N N 420 
TYR   CA  C    sing N N 421 
TYR   CA  CB   sing N N 422 
TYR   CA  HA   sing N N 423 
TYR   C   O    doub N N 424 
TYR   C   OXT  sing N N 425 
TYR   CB  CG   sing N N 426 
TYR   CB  HB2  sing N N 427 
TYR   CB  HB3  sing N N 428 
TYR   CG  CD1  doub Y N 429 
TYR   CG  CD2  sing Y N 430 
TYR   CD1 CE1  sing Y N 431 
TYR   CD1 HD1  sing N N 432 
TYR   CD2 CE2  doub Y N 433 
TYR   CD2 HD2  sing N N 434 
TYR   CE1 CZ   doub Y N 435 
TYR   CE1 HE1  sing N N 436 
TYR   CE2 CZ   sing Y N 437 
TYR   CE2 HE2  sing N N 438 
TYR   CZ  OH   sing N N 439 
TYR   OH  HH   sing N N 440 
TYR   OXT HXT  sing N N 441 
VAL   N   CA   sing N N 442 
VAL   N   H    sing N N 443 
VAL   N   H2   sing N N 444 
VAL   CA  C    sing N N 445 
VAL   CA  CB   sing N N 446 
VAL   CA  HA   sing N N 447 
VAL   C   O    doub N N 448 
VAL   C   OXT  sing N N 449 
VAL   CB  CG1  sing N N 450 
VAL   CB  CG2  sing N N 451 
VAL   CB  HB   sing N N 452 
VAL   CG1 HG11 sing N N 453 
VAL   CG1 HG12 sing N N 454 
VAL   CG1 HG13 sing N N 455 
VAL   CG2 HG21 sing N N 456 
VAL   CG2 HG22 sing N N 457 
VAL   CG2 HG23 sing N N 458 
VAL   OXT HXT  sing N N 459 
# 
_pdbx_audit_support.funding_organization   'Japan Agency for Medical Research and Development (AMED)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           23ak0101198h0001 
_pdbx_audit_support.ordinal                1 
# 
_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   2PPN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LYG 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.031669 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020816 
_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]   0.015313 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   A GLY   A 1 5   ? -13.748 -1.242  24.639 0.60 22.96  ? 1   GLY   A N   1 
ATOM   2    N N   B GLY   A 1 5   ? -12.766 -0.338  24.175 0.40 16.12  ? 1   GLY   A N   1 
ATOM   3    C CA  A GLY   A 1 5   ? -13.551 -1.460  23.190 0.60 17.14  ? 1   GLY   A CA  1 
ATOM   4    C CA  B GLY   A 1 5   ? -13.446 -1.496  23.513 0.40 14.97  ? 1   GLY   A CA  1 
ATOM   5    C C   A GLY   A 1 5   ? -12.525 -2.537  22.914 0.60 12.67  ? 1   GLY   A C   1 
ATOM   6    C C   B GLY   A 1 5   ? -12.475 -2.546  23.008 0.40 12.14  ? 1   GLY   A C   1 
ATOM   7    O O   A GLY   A 1 5   ? -12.798 -3.698  23.156 0.60 11.69  ? 1   GLY   A O   1 
ATOM   8    O O   B GLY   A 1 5   ? -12.756 -3.723  23.197 0.40 11.94  ? 1   GLY   A O   1 
ATOM   9    N N   . VAL   A 1 6   ? -11.425 -2.143  22.296 1.00 12.38  ? 2   VAL   A N   1 
ATOM   10   C CA  . VAL   A 1 6   ? -10.390 -3.086  21.828 1.00 9.93   ? 2   VAL   A CA  1 
ATOM   11   C C   . VAL   A 1 6   ? -9.059  -2.412  22.125 1.00 8.73   ? 2   VAL   A C   1 
ATOM   12   O O   . VAL   A 1 6   ? -8.845  -1.262  21.782 1.00 12.22  ? 2   VAL   A O   1 
ATOM   13   C CB  . VAL   A 1 6   ? -10.479 -3.644  20.370 1.00 11.03  ? 2   VAL   A CB  1 
ATOM   14   C CG1 . VAL   A 1 6   ? -10.537 -2.575  19.313 1.00 15.24  ? 2   VAL   A CG1 1 
ATOM   15   C CG2 . VAL   A 1 6   ? -9.347  -4.627  20.068 1.00 11.26  ? 2   VAL   A CG2 1 
ATOM   16   N N   A GLN   A 1 7   ? -8.176  -3.194  22.713 0.80 9.18   ? 3   GLN   A N   1 
ATOM   17   N N   B GLN   A 1 7   ? -8.176  -3.168  22.760 0.20 8.59   ? 3   GLN   A N   1 
ATOM   18   C CA  A GLN   A 1 7   ? -6.767  -2.849  22.918 0.80 10.82  ? 3   GLN   A CA  1 
ATOM   19   C CA  B GLN   A 1 7   ? -6.763  -2.782  22.919 0.20 9.18   ? 3   GLN   A CA  1 
ATOM   20   C C   A GLN   A 1 7   ? -5.943  -3.721  21.981 0.80 9.79   ? 3   GLN   A C   1 
ATOM   21   C C   B GLN   A 1 7   ? -5.921  -3.709  22.048 0.20 9.40   ? 3   GLN   A C   1 
ATOM   22   O O   A GLN   A 1 7   ? -6.195  -4.907  21.894 0.80 10.46  ? 3   GLN   A O   1 
ATOM   23   O O   B GLN   A 1 7   ? -6.196  -4.916  22.016 0.20 9.76   ? 3   GLN   A O   1 
ATOM   24   C CB  A GLN   A 1 7   ? -6.415  -3.113  24.375 0.80 13.38  ? 3   GLN   A CB  1 
ATOM   25   C CB  B GLN   A 1 7   ? -6.364  -2.848  24.387 0.20 8.79   ? 3   GLN   A CB  1 
ATOM   26   C CG  A GLN   A 1 7   ? -7.208  -2.314  25.394 0.80 19.89  ? 3   GLN   A CG  1 
ATOM   27   C CG  B GLN   A 1 7   ? -4.898  -2.511  24.589 0.20 9.03   ? 3   GLN   A CG  1 
ATOM   28   C CD  A GLN   A 1 7   ? -6.895  -2.792  26.794 0.80 24.11  ? 3   GLN   A CD  1 
ATOM   29   C CD  B GLN   A 1 7   ? -4.368  -3.005  25.907 0.20 9.57   ? 3   GLN   A CD  1 
ATOM   30   O OE1 A GLN   A 1 7   ? -7.725  -3.407  27.478 0.80 32.46  ? 3   GLN   A OE1 1 
ATOM   31   O OE1 B GLN   A 1 7   ? -5.033  -3.753  26.619 0.20 13.67  ? 3   GLN   A OE1 1 
ATOM   32   N NE2 A GLN   A 1 7   ? -5.667  -2.540  27.221 0.80 30.32  ? 3   GLN   A NE2 1 
ATOM   33   N NE2 B GLN   A 1 7   ? -3.174  -2.550  26.248 0.20 10.80  ? 3   GLN   A NE2 1 
ATOM   34   N N   . VAL   A 1 8   ? -4.926  -3.133  21.386 1.00 9.90   ? 4   VAL   A N   1 
ATOM   35   C CA  . VAL   A 1 8   ? -4.018  -3.847  20.458 1.00 9.94   ? 4   VAL   A CA  1 
ATOM   36   C C   . VAL   A 1 8   ? -2.611  -3.728  21.023 1.00 9.56   ? 4   VAL   A C   1 
ATOM   37   O O   . VAL   A 1 8   ? -2.147  -2.599  21.221 1.00 13.98  ? 4   VAL   A O   1 
ATOM   38   C CB  . VAL   A 1 8   ? -4.113  -3.259  19.039 1.00 11.51  ? 4   VAL   A CB  1 
ATOM   39   C CG1 . VAL   A 1 8   ? -3.184  -3.990  18.088 1.00 11.64  ? 4   VAL   A CG1 1 
ATOM   40   C CG2 . VAL   A 1 8   ? -5.553  -3.271  18.523 1.00 12.76  ? 4   VAL   A CG2 1 
ATOM   41   N N   A GLU   A 1 9   ? -1.945  -4.861  21.202 0.65 7.67   ? 5   GLU   A N   1 
ATOM   42   N N   B GLU   A 1 9   ? -2.007  -4.866  21.391 0.35 8.44   ? 5   GLU   A N   1 
ATOM   43   C CA  A GLU   A 1 9   ? -0.547  -4.908  21.653 0.65 8.77   ? 5   GLU   A CA  1 
ATOM   44   C CA  B GLU   A 1 9   ? -0.579  -5.030  21.784 0.35 8.51   ? 5   GLU   A CA  1 
ATOM   45   C C   A GLU   A 1 9   ? 0.252   -5.785  20.696 0.65 8.35   ? 5   GLU   A C   1 
ATOM   46   C C   B GLU   A 1 9   ? 0.122   -5.685  20.589 0.35 8.40   ? 5   GLU   A C   1 
ATOM   47   O O   A GLU   A 1 9   ? -0.046  -6.939  20.469 0.65 6.66   ? 5   GLU   A O   1 
ATOM   48   O O   B GLU   A 1 9   ? -0.479  -6.594  20.013 0.35 8.51   ? 5   GLU   A O   1 
ATOM   49   C CB  A GLU   A 1 9   ? -0.523  -5.443  23.068 0.65 11.13  ? 5   GLU   A CB  1 
ATOM   50   C CB  B GLU   A 1 9   ? -0.489  -5.896  23.053 0.35 7.94   ? 5   GLU   A CB  1 
ATOM   51   C CG  A GLU   A 1 9   ? -1.188  -4.516  24.051 0.65 13.34  ? 5   GLU   A CG  1 
ATOM   52   C CG  B GLU   A 1 9   ? 0.930   -6.151  23.589 0.35 8.11   ? 5   GLU   A CG  1 
ATOM   53   C CD  A GLU   A 1 9   ? -1.329  -5.137  25.418 0.65 16.02  ? 5   GLU   A CD  1 
ATOM   54   C CD  B GLU   A 1 9   ? 1.033   -7.098  24.784 0.35 10.47  ? 5   GLU   A CD  1 
ATOM   55   O OE1 A GLU   A 1 9   ? -2.239  -5.999  25.612 0.65 16.55  ? 5   GLU   A OE1 1 
ATOM   56   O OE1 B GLU   A 1 9   ? 2.076   -7.782  24.959 0.35 11.33  ? 5   GLU   A OE1 1 
ATOM   57   O OE2 A GLU   A 1 9   ? -0.541  -4.737  26.292 0.65 20.38  ? 5   GLU   A OE2 1 
ATOM   58   O OE2 B GLU   A 1 9   ? 0.081   -7.115  25.572 0.35 13.03  ? 5   GLU   A OE2 1 
ATOM   59   N N   . THR   A 1 10  ? 1.305   -5.214  20.201 1.00 7.01   ? 6   THR   A N   1 
ATOM   60   C CA  . THR   A 1 10  ? 2.083   -5.849  19.133 1.00 6.44   ? 6   THR   A CA  1 
ATOM   61   C C   . THR   A 1 10  ? 2.947   -6.952  19.700 1.00 6.69   ? 6   THR   A C   1 
ATOM   62   O O   . THR   A 1 10  ? 3.686   -6.739  20.666 1.00 7.49   ? 6   THR   A O   1 
ATOM   63   C CB  . THR   A 1 10  ? 2.893   -4.811  18.362 1.00 7.43   ? 6   THR   A CB  1 
ATOM   64   O OG1 . THR   A 1 10  ? 1.972   -3.974  17.664 1.00 8.55   ? 6   THR   A OG1 1 
ATOM   65   C CG2 . THR   A 1 10  ? 3.818   -5.460  17.365 1.00 8.65   ? 6   THR   A CG2 1 
ATOM   66   N N   . ILE   A 1 11  ? 2.879   -8.119  19.103 1.00 6.09   ? 7   ILE   A N   1 
ATOM   67   C CA  . ILE   A 1 11  ? 3.766   -9.268  19.388 1.00 6.66   ? 7   ILE   A CA  1 
ATOM   68   C C   . ILE   A 1 11  ? 4.937   -9.279  18.414 1.00 6.23   ? 7   ILE   A C   1 
ATOM   69   O O   . ILE   A 1 11  ? 6.080   -9.477  18.790 1.00 8.04   ? 7   ILE   A O   1 
ATOM   70   C CB  . ILE   A 1 11  ? 2.973   -10.593 19.366 1.00 7.64   ? 7   ILE   A CB  1 
ATOM   71   C CG1 . ILE   A 1 11  ? 1.865   -10.590 20.429 1.00 8.24   ? 7   ILE   A CG1 1 
ATOM   72   C CG2 . ILE   A 1 11  ? 3.910   -11.824 19.491 1.00 8.48   ? 7   ILE   A CG2 1 
ATOM   73   C CD1 . ILE   A 1 11  ? 0.875   -11.707 20.285 1.00 10.79  ? 7   ILE   A CD1 1 
ATOM   74   N N   . SER   A 1 12  ? 4.671   -9.034  17.146 1.00 6.28   ? 8   SER   A N   1 
ATOM   75   C CA  . SER   A 1 12  ? 5.752   -8.837  16.152 1.00 7.62   ? 8   SER   A CA  1 
ATOM   76   C C   . SER   A 1 12  ? 5.250   -7.854  15.119 1.00 5.97   ? 8   SER   A C   1 
ATOM   77   O O   . SER   A 1 12  ? 4.065   -7.871  14.732 1.00 6.79   ? 8   SER   A O   1 
ATOM   78   C CB  . SER   A 1 12  ? 6.234   -10.099 15.611 1.00 9.20   ? 8   SER   A CB  1 
ATOM   79   O OG  . SER   A 1 12  ? 5.231   -10.813 14.980 1.00 11.36  ? 8   SER   A OG  1 
ATOM   80   N N   A PRO   A 1 13  ? 6.085   -6.908  14.684 0.90 6.75   ? 9   PRO   A N   1 
ATOM   81   N N   B PRO   A 1 13  ? 6.099   -6.874  14.743 0.10 5.75   ? 9   PRO   A N   1 
ATOM   82   C CA  A PRO   A 1 13  ? 5.592   -5.833  13.847 0.90 7.01   ? 9   PRO   A CA  1 
ATOM   83   C CA  B PRO   A 1 13  ? 5.689   -5.768  13.876 0.10 5.79   ? 9   PRO   A CA  1 
ATOM   84   C C   A PRO   A 1 13  ? 5.285   -6.264  12.418 0.90 6.56   ? 9   PRO   A C   1 
ATOM   85   C C   B PRO   A 1 13  ? 5.387   -6.149  12.418 0.10 6.34   ? 9   PRO   A C   1 
ATOM   86   O O   A PRO   A 1 13  ? 5.880   -7.181  11.868 0.90 9.21   ? 9   PRO   A O   1 
ATOM   87   O O   B PRO   A 1 13  ? 6.096   -6.977  11.871 0.10 6.54   ? 9   PRO   A O   1 
ATOM   88   C CB  A PRO   A 1 13  ? 6.723   -4.815  13.855 0.90 9.16   ? 9   PRO   A CB  1 
ATOM   89   C CB  B PRO   A 1 13  ? 6.919   -4.847  13.934 0.10 5.44   ? 9   PRO   A CB  1 
ATOM   90   C CG  A PRO   A 1 13  ? 7.912   -5.610  14.106 0.90 12.43  ? 9   PRO   A CG  1 
ATOM   91   C CG  B PRO   A 1 13  ? 7.578   -5.205  15.248 0.10 5.01   ? 9   PRO   A CG  1 
ATOM   92   C CD  A PRO   A 1 13  ? 7.485   -6.732  15.045 0.90 8.01   ? 9   PRO   A CD  1 
ATOM   93   C CD  B PRO   A 1 13  ? 7.474   -6.708  15.240 0.10 5.37   ? 9   PRO   A CD  1 
ATOM   94   N N   . GLY   A 1 14  ? 4.365   -5.515  11.824 1.00 7.02   ? 10  GLY   A N   1 
ATOM   95   C CA  . GLY   A 1 14  ? 4.104   -5.581  10.381 1.00 7.41   ? 10  GLY   A CA  1 
ATOM   96   C C   . GLY   A 1 14  ? 4.871   -4.506  9.644  1.00 6.93   ? 10  GLY   A C   1 
ATOM   97   O O   . GLY   A 1 14  ? 5.743   -3.822  10.206 1.00 6.68   ? 10  GLY   A O   1 
ATOM   98   N N   . ASP   A 1 15  ? 4.571   -4.380  8.353  1.00 7.42   ? 11  ASP   A N   1 
ATOM   99   C CA  . ASP   A 1 15  ? 5.357   -3.452  7.519  1.00 7.78   ? 11  ASP   A CA  1 
ATOM   100  C C   . ASP   A 1 15  ? 5.025   -1.989  7.798  1.00 7.34   ? 11  ASP   A C   1 
ATOM   101  O O   . ASP   A 1 15  ? 5.794   -1.100  7.369  1.00 8.17   ? 11  ASP   A O   1 
ATOM   102  C CB  . ASP   A 1 15  ? 5.206   -3.755  6.033  1.00 8.61   ? 11  ASP   A CB  1 
ATOM   103  C CG  . ASP   A 1 15  ? 3.856   -3.491  5.395  1.00 8.91   ? 11  ASP   A CG  1 
ATOM   104  O OD1 . ASP   A 1 15  ? 2.982   -2.935  6.026  1.00 9.12   ? 11  ASP   A OD1 1 
ATOM   105  O OD2 . ASP   A 1 15  ? 3.728   -3.791  4.173  1.00 12.61  ? 11  ASP   A OD2 1 
ATOM   106  N N   . GLY   A 1 16  ? 3.988   -1.675  8.548  1.00 7.46   ? 12  GLY   A N   1 
ATOM   107  C CA  . GLY   A 1 16  ? 3.660   -0.267  8.817  1.00 9.02   ? 12  GLY   A CA  1 
ATOM   108  C C   . GLY   A 1 16  ? 3.231   0.532   7.627  1.00 9.90   ? 12  GLY   A C   1 
ATOM   109  O O   . GLY   A 1 16  ? 3.238   1.764   7.738  1.00 11.05  ? 12  GLY   A O   1 
ATOM   110  N N   A ARG   A 1 17  ? 2.845   -0.124  6.533  0.50 9.72   ? 13  ARG   A N   1 
ATOM   111  N N   B ARG   A 1 17  ? 2.906   -0.153  6.526  0.50 9.34   ? 13  ARG   A N   1 
ATOM   112  C CA  A ARG   A 1 17  ? 2.538   0.582   5.255  0.50 11.92  ? 13  ARG   A CA  1 
ATOM   113  C CA  B ARG   A 1 17  ? 2.604   0.471   5.201  0.50 11.16  ? 13  ARG   A CA  1 
ATOM   114  C C   A ARG   A 1 17  ? 1.323   -0.032  4.557  0.50 10.80  ? 13  ARG   A C   1 
ATOM   115  C C   B ARG   A 1 17  ? 1.265   -0.018  4.671  0.50 10.76  ? 13  ARG   A C   1 
ATOM   116  O O   A ARG   A 1 17  ? 0.643   0.706   3.831  0.50 13.89  ? 13  ARG   A O   1 
ATOM   117  O O   B ARG   A 1 17  ? 0.476   0.800   4.178  0.50 13.90  ? 13  ARG   A O   1 
ATOM   118  C CB  A ARG   A 1 17  ? 3.758   0.621   4.313  0.50 16.20  ? 13  ARG   A CB  1 
ATOM   119  C CB  B ARG   A 1 17  ? 3.621   0.148   4.092  0.50 14.17  ? 13  ARG   A CB  1 
ATOM   120  C CG  A ARG   A 1 17  ? 3.658   1.612   3.159  0.50 18.14  ? 13  ARG   A CG  1 
ATOM   121  C CG  B ARG   A 1 17  ? 5.007   0.711   4.353  0.50 16.63  ? 13  ARG   A CG  1 
ATOM   122  C CD  A ARG   A 1 17  ? 4.045   1.046   1.798  0.50 24.28  ? 13  ARG   A CD  1 
ATOM   123  C CD  B ARG   A 1 17  ? 5.796   0.665   3.064  0.50 20.41  ? 13  ARG   A CD  1 
ATOM   124  N NE  A ARG   A 1 17  ? 5.451   0.677   1.697  0.50 28.78  ? 13  ARG   A NE  1 
ATOM   125  N NE  B ARG   A 1 17  ? 6.040   -0.686  2.574  0.50 22.79  ? 13  ARG   A NE  1 
ATOM   126  C CZ  A ARG   A 1 17  ? 6.370   1.378   1.041  0.50 29.27  ? 13  ARG   A CZ  1 
ATOM   127  C CZ  B ARG   A 1 17  ? 5.611   -1.179  1.418  0.50 26.01  ? 13  ARG   A CZ  1 
ATOM   128  N NH1 A ARG   A 1 17  ? 7.614   0.942   0.991  0.50 31.04  ? 13  ARG   A NH1 1 
ATOM   129  N NH1 B ARG   A 1 17  ? 5.914   -2.425  1.092  0.50 25.91  ? 13  ARG   A NH1 1 
ATOM   130  N NH2 A ARG   A 1 17  ? 6.046   2.510   0.439  0.50 32.58  ? 13  ARG   A NH2 1 
ATOM   131  N NH2 B ARG   A 1 17  ? 4.911   -0.435  0.576  0.50 29.33  ? 13  ARG   A NH2 1 
ATOM   132  N N   . THR   A 1 18  ? 1.063   -1.325  4.743  1.00 9.76   ? 14  THR   A N   1 
ATOM   133  C CA  . THR   A 1 18  ? -0.029  -2.027  4.043  1.00 9.68   ? 14  THR   A CA  1 
ATOM   134  C C   . THR   A 1 18  ? -1.132  -2.297  5.065  1.00 9.19   ? 14  THR   A C   1 
ATOM   135  O O   . THR   A 1 18  ? -1.053  -3.269  5.811  1.00 10.51  ? 14  THR   A O   1 
ATOM   136  C CB  . THR   A 1 18  ? 0.500   -3.299  3.385  1.00 11.38  ? 14  THR   A CB  1 
ATOM   137  O OG1 . THR   A 1 18  ? 1.703   -2.982  2.685  1.00 12.18  ? 14  THR   A OG1 1 
ATOM   138  C CG2 . THR   A 1 18  ? -0.539  -3.871  2.450  1.00 11.68  ? 14  THR   A CG2 1 
ATOM   139  N N   . PHE   A 1 19  ? -2.115  -1.426  5.125  1.00 10.18  ? 15  PHE   A N   1 
ATOM   140  C CA  . PHE   A 1 19  ? -3.237  -1.496  6.093  1.00 9.74   ? 15  PHE   A CA  1 
ATOM   141  C C   . PHE   A 1 19  ? -4.528  -1.807  5.368  1.00 9.99   ? 15  PHE   A C   1 
ATOM   142  O O   . PHE   A 1 19  ? -4.723  -1.380  4.230  1.00 12.73  ? 15  PHE   A O   1 
ATOM   143  C CB  . PHE   A 1 19  ? -3.360  -0.174  6.824  1.00 11.79  ? 15  PHE   A CB  1 
ATOM   144  C CG  . PHE   A 1 19  ? -2.209  0.135   7.740  1.00 11.75  ? 15  PHE   A CG  1 
ATOM   145  C CD1 . PHE   A 1 19  ? -2.230  -0.219  9.092  1.00 11.25  ? 15  PHE   A CD1 1 
ATOM   146  C CD2 . PHE   A 1 19  ? -1.142  0.884   7.293  1.00 12.88  ? 15  PHE   A CD2 1 
ATOM   147  C CE1 . PHE   A 1 19  ? -1.179  0.089   9.940  1.00 12.07  ? 15  PHE   A CE1 1 
ATOM   148  C CE2 . PHE   A 1 19  ? -0.113  1.227   8.154  1.00 13.02  ? 15  PHE   A CE2 1 
ATOM   149  C CZ  . PHE   A 1 19  ? -0.139  0.833   9.472  1.00 12.76  ? 15  PHE   A CZ  1 
ATOM   150  N N   . PRO   A 1 20  ? -5.425  -2.588  5.986  1.00 10.05  ? 16  PRO   A N   1 
ATOM   151  C CA  . PRO   A 1 20  ? -6.673  -2.986  5.373  1.00 11.52  ? 16  PRO   A CA  1 
ATOM   152  C C   . PRO   A 1 20  ? -7.580  -1.797  5.085  1.00 12.66  ? 16  PRO   A C   1 
ATOM   153  O O   . PRO   A 1 20  ? -7.802  -0.984  5.946  1.00 13.90  ? 16  PRO   A O   1 
ATOM   154  C CB  . PRO   A 1 20  ? -7.357  -3.899  6.395  1.00 15.22  ? 16  PRO   A CB  1 
ATOM   155  C CG  . PRO   A 1 20  ? -6.328  -4.238  7.408  1.00 13.26  ? 16  PRO   A CG  1 
ATOM   156  C CD  . PRO   A 1 20  ? -5.242  -3.205  7.300  1.00 10.55  ? 16  PRO   A CD  1 
ATOM   157  N N   A LYS   A 1 21  ? -8.120  -1.770  3.878  0.80 14.08  ? 17  LYS   A N   1 
ATOM   158  N N   B LYS   A 1 21  ? -8.109  -1.744  3.865  0.20 14.70  ? 17  LYS   A N   1 
ATOM   159  C CA  A LYS   A 1 21  ? -9.115  -0.761  3.468  0.80 18.18  ? 17  LYS   A CA  1 
ATOM   160  C CA  B LYS   A 1 21  ? -9.088  -0.718  3.428  0.20 17.99  ? 17  LYS   A CA  1 
ATOM   161  C C   A LYS   A 1 21  ? -10.514 -1.370  3.519  0.80 17.41  ? 17  LYS   A C   1 
ATOM   162  C C   B LYS   A 1 21  ? -10.490 -1.334  3.480  0.20 20.42  ? 17  LYS   A C   1 
ATOM   163  O O   A LYS   A 1 21  ? -10.666 -2.605  3.348  0.80 19.04  ? 17  LYS   A O   1 
ATOM   164  O O   B LYS   A 1 21  ? -10.600 -2.570  3.345  0.20 21.82  ? 17  LYS   A O   1 
ATOM   165  C CB  A LYS   A 1 21  ? -8.787  -0.243  2.070  0.80 20.57  ? 17  LYS   A CB  1 
ATOM   166  C CB  B LYS   A 1 21  ? -8.705  -0.214  2.035  0.20 18.87  ? 17  LYS   A CB  1 
ATOM   167  C CG  A LYS   A 1 21  ? -7.467  0.510   1.974  0.80 25.14  ? 17  LYS   A CG  1 
ATOM   168  C CG  B LYS   A 1 21  ? -7.345  0.474   1.969  0.20 18.94  ? 17  LYS   A CG  1 
ATOM   169  C CD  A LYS   A 1 21  ? -7.377  1.458   0.802  0.80 30.90  ? 17  LYS   A CD  1 
ATOM   170  C CD  B LYS   A 1 21  ? -6.655  0.366   0.625  0.20 19.30  ? 17  LYS   A CD  1 
ATOM   171  C CE  A LYS   A 1 21  ? -6.075  2.235   0.774  0.80 36.26  ? 17  LYS   A CE  1 
ATOM   172  C CE  B LYS   A 1 21  ? -5.359  1.146   0.561  0.20 19.45  ? 17  LYS   A CE  1 
ATOM   173  N NZ  A LYS   A 1 21  ? -5.840  2.882   -0.539 0.80 41.85  ? 17  LYS   A NZ  1 
ATOM   174  N NZ  B LYS   A 1 21  ? -5.023  1.540   -0.827 0.20 18.94  ? 17  LYS   A NZ  1 
ATOM   175  N N   . ARG   A 1 22  ? -11.508 -0.498  3.710  1.00 23.61  ? 18  ARG   A N   1 
ATOM   176  C CA  . ARG   A 1 22  ? -12.935 -0.884  3.625  1.00 24.87  ? 18  ARG   A CA  1 
ATOM   177  C C   . ARG   A 1 22  ? -13.085 -1.707  2.343  1.00 24.73  ? 18  ARG   A C   1 
ATOM   178  O O   . ARG   A 1 22  ? -12.574 -1.256  1.279  1.00 26.03  ? 18  ARG   A O   1 
ATOM   179  C CB  . ARG   A 1 22  ? -13.848 0.352   3.611  1.00 30.11  ? 18  ARG   A CB  1 
ATOM   180  C CG  . ARG   A 1 22  ? -14.951 0.342   4.664  1.00 33.57  ? 18  ARG   A CG  1 
ATOM   181  C CD  . ARG   A 1 22  ? -15.728 1.644   4.780  1.00 34.00  ? 18  ARG   A CD  1 
ATOM   182  N NE  . ARG   A 1 22  ? -17.105 1.405   5.207  1.00 36.32  ? 18  ARG   A NE  1 
ATOM   183  C CZ  . ARG   A 1 22  ? -17.542 1.305   6.468  1.00 39.46  ? 18  ARG   A CZ  1 
ATOM   184  N NH1 . ARG   A 1 22  ? -18.827 1.069   6.675  1.00 44.16  ? 18  ARG   A NH1 1 
ATOM   185  N NH2 . ARG   A 1 22  ? -16.730 1.435   7.513  1.00 29.02  ? 18  ARG   A NH2 1 
ATOM   186  N N   . GLY   A 1 23  ? -13.737 -2.865  2.426  1.00 27.04  ? 19  GLY   A N   1 
ATOM   187  C CA  . GLY   A 1 23  ? -14.067 -3.681  1.246  1.00 30.22  ? 19  GLY   A CA  1 
ATOM   188  C C   . GLY   A 1 23  ? -12.951 -4.618  0.811  1.00 26.65  ? 19  GLY   A C   1 
ATOM   189  O O   . GLY   A 1 23  ? -13.148 -5.348  -0.171 1.00 34.05  ? 19  GLY   A O   1 
ATOM   190  N N   . GLN   A 1 24  ? -11.785 -4.588  1.470  1.00 25.52  ? 20  GLN   A N   1 
ATOM   191  C CA  . GLN   A 1 24  ? -10.707 -5.590  1.229  1.00 23.01  ? 20  GLN   A CA  1 
ATOM   192  C C   . GLN   A 1 24  ? -10.929 -6.836  2.094  1.00 20.39  ? 20  GLN   A C   1 
ATOM   193  O O   . GLN   A 1 24  ? -11.475 -6.715  3.227  1.00 21.42  ? 20  GLN   A O   1 
ATOM   194  C CB  . GLN   A 1 24  ? -9.312  -5.032  1.494  1.00 22.47  ? 20  GLN   A CB  1 
ATOM   195  C CG  . GLN   A 1 24  ? -8.794  -4.145  0.378  1.00 22.87  ? 20  GLN   A CG  1 
ATOM   196  C CD  . GLN   A 1 24  ? -7.353  -3.821  0.676  1.00 24.00  ? 20  GLN   A CD  1 
ATOM   197  O OE1 . GLN   A 1 24  ? -7.027  -3.348  1.749  1.00 19.45  ? 20  GLN   A OE1 1 
ATOM   198  N NE2 . GLN   A 1 24  ? -6.479  -4.088  -0.282 1.00 29.42  ? 20  GLN   A NE2 1 
ATOM   199  N N   . THR   A 1 25  ? -10.425 -7.976  1.607  1.00 19.76  ? 21  THR   A N   1 
ATOM   200  C CA  . THR   A 1 25  ? -10.457 -9.258  2.348  1.00 16.42  ? 21  THR   A CA  1 
ATOM   201  C C   . THR   A 1 25  ? -9.162  -9.386  3.153  1.00 13.21  ? 21  THR   A C   1 
ATOM   202  O O   . THR   A 1 25  ? -8.054  -9.376  2.578  1.00 16.85  ? 21  THR   A O   1 
ATOM   203  C CB  . THR   A 1 25  ? -10.689 -10.449 1.419  1.00 17.22  ? 21  THR   A CB  1 
ATOM   204  O OG1 . THR   A 1 25  ? -11.991 -10.285 0.846  1.00 20.99  ? 21  THR   A OG1 1 
ATOM   205  C CG2 . THR   A 1 25  ? -10.608 -11.770 2.146  1.00 16.97  ? 21  THR   A CG2 1 
ATOM   206  N N   . CYS   A 1 26  ? -9.311  -9.467  4.468  1.00 11.20  ? 22  CYS   A N   1 
ATOM   207  C CA  . CYS   A 1 26  ? -8.218  -9.719  5.416  1.00 9.55   ? 22  CYS   A CA  1 
ATOM   208  C C   . CYS   A 1 26  ? -8.095  -11.219 5.596  1.00 8.49   ? 22  CYS   A C   1 
ATOM   209  O O   . CYS   A 1 26  ? -9.097  -11.894 5.854  1.00 10.19  ? 22  CYS   A O   1 
ATOM   210  C CB  . CYS   A 1 26  ? -8.499  -9.070  6.763  1.00 11.42  ? 22  CYS   A CB  1 
ATOM   211  S SG  . CYS   A 1 26  ? -8.667  -7.276  6.685  1.00 15.56  ? 22  CYS   A SG  1 
ATOM   212  N N   . VAL   A 1 27  ? -6.870  -11.680 5.448  1.00 7.07   ? 23  VAL   A N   1 
ATOM   213  C CA  . VAL   A 1 27  ? -6.514  -13.096 5.676  1.00 7.19   ? 23  VAL   A CA  1 
ATOM   214  C C   . VAL   A 1 27  ? -5.704  -13.151 6.965  1.00 6.94   ? 23  VAL   A C   1 
ATOM   215  O O   . VAL   A 1 27  ? -4.623  -12.580 7.022  1.00 7.93   ? 23  VAL   A O   1 
ATOM   216  C CB  . VAL   A 1 27  ? -5.738  -13.704 4.505  1.00 8.65   ? 23  VAL   A CB  1 
ATOM   217  C CG1 . VAL   A 1 27  ? -5.525  -15.189 4.726  1.00 9.27   ? 23  VAL   A CG1 1 
ATOM   218  C CG2 . VAL   A 1 27  ? -6.442  -13.443 3.196  1.00 8.90   ? 23  VAL   A CG2 1 
ATOM   219  N N   A VAL   A 1 28  ? -6.199  -13.908 7.921  0.50 6.76   ? 24  VAL   A N   1 
ATOM   220  N N   B VAL   A 1 28  ? -6.239  -13.837 7.984  0.50 7.10   ? 24  VAL   A N   1 
ATOM   221  C CA  A VAL   A 1 28  ? -5.489  -13.971 9.211  0.50 6.83   ? 24  VAL   A CA  1 
ATOM   222  C CA  B VAL   A 1 28  ? -5.773  -13.765 9.404  0.50 7.56   ? 24  VAL   A CA  1 
ATOM   223  C C   A VAL   A 1 28  ? -5.347  -15.404 9.665  0.50 6.97   ? 24  VAL   A C   1 
ATOM   224  C C   B VAL   A 1 28  ? -5.624  -15.182 9.967  0.50 7.50   ? 24  VAL   A C   1 
ATOM   225  O O   A VAL   A 1 28  ? -6.004  -16.329 9.184  0.50 8.95   ? 24  VAL   A O   1 
ATOM   226  O O   B VAL   A 1 28  ? -6.577  -15.946 9.820  0.50 10.25  ? 24  VAL   A O   1 
ATOM   227  C CB  A VAL   A 1 28  ? -6.171  -13.116 10.294 0.50 6.87   ? 24  VAL   A CB  1 
ATOM   228  C CB  B VAL   A 1 28  ? -6.732  -12.902 10.266 0.50 9.13   ? 24  VAL   A CB  1 
ATOM   229  C CG1 A VAL   A 1 28  ? -6.405  -11.690 9.826  0.50 6.89   ? 24  VAL   A CG1 1 
ATOM   230  C CG1 B VAL   A 1 28  ? -6.354  -12.785 11.734 0.50 9.85   ? 24  VAL   A CG1 1 
ATOM   231  C CG2 A VAL   A 1 28  ? -7.484  -13.736 10.720 0.50 6.90   ? 24  VAL   A CG2 1 
ATOM   232  C CG2 B VAL   A 1 28  ? -6.892  -11.506 9.680  0.50 9.77   ? 24  VAL   A CG2 1 
ATOM   233  N N   . HIS   A 1 29  ? -4.529  -15.502 10.677 1.00 6.10   ? 25  HIS   A N   1 
ATOM   234  C CA  . HIS   A 1 29  ? -4.527  -16.646 11.606 1.00 6.28   ? 25  HIS   A CA  1 
ATOM   235  C C   . HIS   A 1 29  ? -4.847  -16.122 12.997 1.00 5.89   ? 25  HIS   A C   1 
ATOM   236  O O   . HIS   A 1 29  ? -4.340  -15.058 13.390 1.00 7.11   ? 25  HIS   A O   1 
ATOM   237  C CB  . HIS   A 1 29  ? -3.238  -17.473 11.586 1.00 6.73   ? 25  HIS   A CB  1 
ATOM   238  C CG  . HIS   A 1 29  ? -3.306  -18.701 10.744 1.00 6.81   ? 25  HIS   A CG  1 
ATOM   239  N ND1 . HIS   A 1 29  ? -4.351  -19.603 10.862 1.00 7.08   ? 25  HIS   A ND1 1 
ATOM   240  C CD2 . HIS   A 1 29  ? -2.441  -19.187 9.838  1.00 8.58   ? 25  HIS   A CD2 1 
ATOM   241  C CE1 . HIS   A 1 29  ? -4.114  -20.603 10.043 1.00 7.81   ? 25  HIS   A CE1 1 
ATOM   242  N NE2 . HIS   A 1 29  ? -2.946  -20.361 9.406  1.00 9.71   ? 25  HIS   A NE2 1 
ATOM   243  N N   . TYR   A 1 30  ? -5.637  -16.874 13.768 1.00 5.88   ? 26  TYR   A N   1 
ATOM   244  C CA  . TYR   A 1 30  ? -5.943  -16.423 15.134 1.00 5.51   ? 26  TYR   A CA  1 
ATOM   245  C C   . TYR   A 1 30  ? -6.020  -17.619 16.050 1.00 5.50   ? 26  TYR   A C   1 
ATOM   246  O O   . TYR   A 1 30  ? -6.350  -18.747 15.693 1.00 5.85   ? 26  TYR   A O   1 
ATOM   247  C CB  . TYR   A 1 30  ? -7.278  -15.654 15.177 1.00 5.88   ? 26  TYR   A CB  1 
ATOM   248  C CG  . TYR   A 1 30  ? -8.512  -16.484 14.930 1.00 5.80   ? 26  TYR   A CG  1 
ATOM   249  C CD1 . TYR   A 1 30  ? -9.023  -16.725 13.663 1.00 6.02   ? 26  TYR   A CD1 1 
ATOM   250  C CD2 . TYR   A 1 30  ? -9.188  -17.038 15.997 1.00 6.36   ? 26  TYR   A CD2 1 
ATOM   251  C CE1 . TYR   A 1 30  ? -10.131 -17.514 13.464 1.00 5.91   ? 26  TYR   A CE1 1 
ATOM   252  C CE2 . TYR   A 1 30  ? -10.303 -17.824 15.825 1.00 6.29   ? 26  TYR   A CE2 1 
ATOM   253  C CZ  . TYR   A 1 30  ? -10.798 -18.053 14.550 1.00 5.35   ? 26  TYR   A CZ  1 
ATOM   254  O OH  . TYR   A 1 30  ? -11.912 -18.799 14.301 1.00 7.04   ? 26  TYR   A OH  1 
ATOM   255  N N   . THR   A 1 31  ? -5.884  -17.293 17.334 1.00 5.78   ? 27  THR   A N   1 
ATOM   256  C CA  . THR   A 1 31  ? -6.303  -18.139 18.466 1.00 5.53   ? 27  THR   A CA  1 
ATOM   257  C C   . THR   A 1 31  ? -7.052  -17.224 19.423 1.00 6.01   ? 27  THR   A C   1 
ATOM   258  O O   . THR   A 1 31  ? -6.540  -16.138 19.750 1.00 6.76   ? 27  THR   A O   1 
ATOM   259  C CB  . THR   A 1 31  ? -5.099  -18.813 19.134 1.00 7.06   ? 27  THR   A CB  1 
ATOM   260  O OG1 . THR   A 1 31  ? -4.453  -19.626 18.147 1.00 8.76   ? 27  THR   A OG1 1 
ATOM   261  C CG2 . THR   A 1 31  ? -5.497  -19.631 20.346 1.00 7.67   ? 27  THR   A CG2 1 
ATOM   262  N N   . GLY   A 1 32  ? -8.231  -17.658 19.821 1.00 6.17   ? 28  GLY   A N   1 
ATOM   263  C CA  . GLY   A 1 32  ? -9.072  -16.925 20.783 1.00 6.36   ? 28  GLY   A CA  1 
ATOM   264  C C   . GLY   A 1 32  ? -9.047  -17.610 22.135 1.00 5.82   ? 28  GLY   A C   1 
ATOM   265  O O   . GLY   A 1 32  ? -9.279  -18.828 22.227 1.00 6.51   ? 28  GLY   A O   1 
ATOM   266  N N   . MET   A 1 33  ? -8.874  -16.795 23.173 1.00 5.91   ? 29  MET   A N   1 
ATOM   267  C CA  . MET   A 1 33  ? -8.826  -17.251 24.561 1.00 7.22   ? 29  MET   A CA  1 
ATOM   268  C C   . MET   A 1 33  ? -9.734  -16.396 25.444 1.00 6.79   ? 29  MET   A C   1 
ATOM   269  O O   . MET   A 1 33  ? -9.882  -15.197 25.227 1.00 7.62   ? 29  MET   A O   1 
ATOM   270  C CB  . MET   A 1 33  ? -7.395  -17.156 25.089 1.00 9.29   ? 29  MET   A CB  1 
ATOM   271  C CG  . MET   A 1 33  ? -6.449  -18.111 24.401 1.00 11.05  ? 29  MET   A CG  1 
ATOM   272  S SD  . MET   A 1 33  ? -4.755  -17.525 24.337 1.00 14.51  ? 29  MET   A SD  1 
ATOM   273  C CE  . MET   A 1 33  ? -4.940  -16.227 23.129 1.00 15.29  ? 29  MET   A CE  1 
ATOM   274  N N   . LEU   A 1 34  ? -10.293 -17.042 26.457 1.00 6.90   ? 30  LEU   A N   1 
ATOM   275  C CA  . LEU   A 1 34  ? -10.912 -16.291 27.562 1.00 7.73   ? 30  LEU   A CA  1 
ATOM   276  C C   . LEU   A 1 34  ? -9.789  -15.655 28.400 1.00 8.73   ? 30  LEU   A C   1 
ATOM   277  O O   . LEU   A 1 34  ? -8.608  -15.956 28.245 1.00 9.95   ? 30  LEU   A O   1 
ATOM   278  C CB  . LEU   A 1 34  ? -11.787 -17.247 28.379 1.00 8.08   ? 30  LEU   A CB  1 
ATOM   279  C CG  . LEU   A 1 34  ? -12.877 -17.950 27.580 1.00 9.35   ? 30  LEU   A CG  1 
ATOM   280  C CD1 . LEU   A 1 34  ? -13.652 -18.877 28.500 1.00 11.74  ? 30  LEU   A CD1 1 
ATOM   281  C CD2 . LEU   A 1 34  ? -13.807 -16.994 26.865 1.00 10.35  ? 30  LEU   A CD2 1 
ATOM   282  N N   . GLU   A 1 35  ? -10.151 -14.774 29.322 1.00 9.64   ? 31  GLU   A N   1 
ATOM   283  C CA  . GLU   A 1 35  ? -9.123  -14.030 30.085 1.00 12.82  ? 31  GLU   A CA  1 
ATOM   284  C C   . GLU   A 1 35  ? -8.229  -14.946 30.896 1.00 12.79  ? 31  GLU   A C   1 
ATOM   285  O O   . GLU   A 1 35  ? -7.067  -14.562 31.131 1.00 17.07  ? 31  GLU   A O   1 
ATOM   286  C CB  . GLU   A 1 35  ? -9.770  -13.062 31.044 1.00 14.93  ? 31  GLU   A CB  1 
ATOM   287  C CG  . GLU   A 1 35  ? -10.357 -11.843 30.395 1.00 18.00  ? 31  GLU   A CG  1 
ATOM   288  C CD  . GLU   A 1 35  ? -10.766 -10.793 31.418 1.00 20.05  ? 31  GLU   A CD  1 
ATOM   289  O OE1 . GLU   A 1 35  ? -9.912  -9.972  31.778 1.00 29.57  ? 31  GLU   A OE1 1 
ATOM   290  O OE2 . GLU   A 1 35  ? -11.932 -10.841 31.882 1.00 21.23  ? 31  GLU   A OE2 1 
ATOM   291  N N   . ASP   A 1 36  ? -8.743  -16.083 31.347 1.00 12.60  ? 32  ASP   A N   1 
ATOM   292  C CA  . ASP   A 1 36  ? -7.921  -17.034 32.137 1.00 15.60  ? 32  ASP   A CA  1 
ATOM   293  C C   . ASP   A 1 36  ? -7.028  -17.909 31.251 1.00 15.65  ? 32  ASP   A C   1 
ATOM   294  O O   . ASP   A 1 36  ? -6.399  -18.821 31.787 1.00 19.66  ? 32  ASP   A O   1 
ATOM   295  C CB  . ASP   A 1 36  ? -8.852  -17.873 33.000 1.00 17.56  ? 32  ASP   A CB  1 
ATOM   296  C CG  . ASP   A 1 36  ? -9.778  -18.778 32.218 1.00 18.71  ? 32  ASP   A CG  1 
ATOM   297  O OD1 . ASP   A 1 36  ? -9.708  -18.784 30.959 1.00 15.44  ? 32  ASP   A OD1 1 
ATOM   298  O OD2 . ASP   A 1 36  ? -10.576 -19.459 32.864 1.00 24.41  ? 32  ASP   A OD2 1 
ATOM   299  N N   . GLY   A 1 37  ? -6.985  -17.671 29.935 1.00 13.31  ? 33  GLY   A N   1 
ATOM   300  C CA  . GLY   A 1 37  ? -6.127  -18.405 28.983 1.00 13.66  ? 33  GLY   A CA  1 
ATOM   301  C C   . GLY   A 1 37  ? -6.787  -19.609 28.358 1.00 11.97  ? 33  GLY   A C   1 
ATOM   302  O O   . GLY   A 1 37  ? -6.191  -20.205 27.495 1.00 13.27  ? 33  GLY   A O   1 
ATOM   303  N N   A LYS   A 1 38  ? -7.998  -19.974 28.764 0.50 10.49  ? 34  LYS   A N   1 
ATOM   304  N N   B LYS   A 1 38  ? -8.014  -19.934 28.731 0.50 10.30  ? 34  LYS   A N   1 
ATOM   305  C CA  A LYS   A 1 38  ? -8.704  -21.123 28.140 0.50 10.14  ? 34  LYS   A CA  1 
ATOM   306  C CA  B LYS   A 1 38  ? -8.711  -21.090 28.114 0.50 10.34  ? 34  LYS   A CA  1 
ATOM   307  C C   A LYS   A 1 38  ? -8.968  -20.808 26.661 0.50 8.18   ? 34  LYS   A C   1 
ATOM   308  C C   B LYS   A 1 38  ? -8.966  -20.791 26.637 0.50 8.24   ? 34  LYS   A C   1 
ATOM   309  O O   A LYS   A 1 38  ? -9.546  -19.761 26.319 0.50 8.55   ? 34  LYS   A O   1 
ATOM   310  O O   B LYS   A 1 38  ? -9.537  -19.747 26.277 0.50 8.87   ? 34  LYS   A O   1 
ATOM   311  C CB  A LYS   A 1 38  ? -10.023 -21.460 28.837 0.50 12.81  ? 34  LYS   A CB  1 
ATOM   312  C CB  B LYS   A 1 38  ? -10.031 -21.421 28.803 0.50 13.22  ? 34  LYS   A CB  1 
ATOM   313  C CG  A LYS   A 1 38  ? -9.849  -22.186 30.169 0.50 15.48  ? 34  LYS   A CG  1 
ATOM   314  C CG  B LYS   A 1 38  ? -9.836  -21.853 30.247 0.50 16.88  ? 34  LYS   A CG  1 
ATOM   315  C CD  A LYS   A 1 38  ? -9.251  -23.573 30.023 0.50 21.03  ? 34  LYS   A CD  1 
ATOM   316  C CD  B LYS   A 1 38  ? -11.098 -22.309 30.935 0.50 18.22  ? 34  LYS   A CD  1 
ATOM   317  C CE  A LYS   A 1 38  ? -8.874  -24.234 31.334 0.50 22.23  ? 34  LYS   A CE  1 
ATOM   318  C CE  B LYS   A 1 38  ? -10.846 -22.796 32.347 0.50 22.46  ? 34  LYS   A CE  1 
ATOM   319  N NZ  A LYS   A 1 38  ? -7.752  -25.196 31.180 0.50 22.06  ? 34  LYS   A NZ  1 
ATOM   320  N NZ  B LYS   A 1 38  ? -9.548  -23.507 32.471 0.50 25.45  ? 34  LYS   A NZ  1 
ATOM   321  N N   . LYS   A 1 39  ? -8.571  -21.725 25.794 1.00 8.09   ? 35  LYS   A N   1 
ATOM   322  C CA  . LYS   A 1 39  ? -8.731  -21.561 24.332 1.00 6.81   ? 35  LYS   A CA  1 
ATOM   323  C C   . LYS   A 1 39  ? -10.165 -21.885 23.922 1.00 6.82   ? 35  LYS   A C   1 
ATOM   324  O O   . LYS   A 1 39  ? -10.694 -22.951 24.286 1.00 9.33   ? 35  LYS   A O   1 
ATOM   325  C CB  . LYS   A 1 39  ? -7.785  -22.489 23.590 1.00 7.32   ? 35  LYS   A CB  1 
ATOM   326  C CG  . LYS   A 1 39  ? -7.956  -22.456 22.084 1.00 6.87   ? 35  LYS   A CG  1 
ATOM   327  C CD  . LYS   A 1 39  ? -6.837  -23.164 21.318 1.00 7.43   ? 35  LYS   A CD  1 
ATOM   328  C CE  . LYS   A 1 39  ? -6.730  -24.635 21.683 1.00 7.17   ? 35  LYS   A CE  1 
ATOM   329  N NZ  . LYS   A 1 39  ? -5.683  -25.304 20.886 1.00 7.61   ? 35  LYS   A NZ  1 
ATOM   330  N N   . PHE   A 1 40  ? -10.823 -20.986 23.214 1.00 6.47   ? 36  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 40  ? -12.177 -21.268 22.711 1.00 6.53   ? 36  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 40  ? -12.189 -21.496 21.193 1.00 6.36   ? 36  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 40  ? -13.171 -22.072 20.739 1.00 7.36   ? 36  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 40  ? -13.190 -20.186 23.118 1.00 6.61   ? 36  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 40  ? -12.909 -18.794 22.619 1.00 6.54   ? 36  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 40  ? -13.130 -18.404 21.305 1.00 6.63   ? 36  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 40  ? -12.445 -17.841 23.503 1.00 6.75   ? 36  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 40  ? -12.841 -17.129 20.865 1.00 6.94   ? 36  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 40  ? -12.180 -16.555 23.080 1.00 6.71   ? 36  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 40  ? -12.389 -16.207 21.761 1.00 6.82   ? 36  PHE   A CZ  1 
ATOM   341  N N   . ASP   A 1 41  ? -11.175 -21.103 20.440 1.00 5.71   ? 37  ASP   A N   1 
ATOM   342  C CA  . ASP   A 1 41  ? -11.138 -21.388 18.984 1.00 6.13   ? 37  ASP   A CA  1 
ATOM   343  C C   . ASP   A 1 41  ? -9.755  -21.051 18.480 1.00 6.01   ? 37  ASP   A C   1 
ATOM   344  O O   . ASP   A 1 41  ? -9.083  -20.202 19.024 1.00 7.08   ? 37  ASP   A O   1 
ATOM   345  C CB  . ASP   A 1 41  ? -12.214 -20.655 18.173 1.00 6.33   ? 37  ASP   A CB  1 
ATOM   346  C CG  . ASP   A 1 41  ? -12.472 -21.357 16.836 1.00 7.03   ? 37  ASP   A CG  1 
ATOM   347  O OD1 . ASP   A 1 41  ? -12.279 -22.571 16.755 1.00 8.65   ? 37  ASP   A OD1 1 
ATOM   348  O OD2 . ASP   A 1 41  ? -12.845 -20.670 15.878 1.00 7.70   ? 37  ASP   A OD2 1 
ATOM   349  N N   . SER   A 1 42  ? -9.397  -21.656 17.352 1.00 6.40   ? 38  SER   A N   1 
ATOM   350  C CA  . SER   A 1 42  ? -8.124  -21.352 16.659 1.00 6.55   ? 38  SER   A CA  1 
ATOM   351  C C   . SER   A 1 42  ? -8.193  -21.769 15.207 1.00 5.43   ? 38  SER   A C   1 
ATOM   352  O O   . SER   A 1 42  ? -8.422  -22.919 14.923 1.00 6.59   ? 38  SER   A O   1 
ATOM   353  C CB  . SER   A 1 42  ? -6.963  -22.025 17.340 1.00 7.21   ? 38  SER   A CB  1 
ATOM   354  O OG  . SER   A 1 42  ? -5.761  -21.745 16.635 1.00 7.66   ? 38  SER   A OG  1 
ATOM   355  N N   . SER   A 1 43  ? -7.912  -20.830 14.299 1.00 5.79   ? 39  SER   A N   1 
ATOM   356  C CA  . SER   A 1 43  ? -7.740  -21.174 12.876 1.00 5.82   ? 39  SER   A CA  1 
ATOM   357  C C   . SER   A 1 43  ? -6.467  -21.969 12.677 1.00 6.19   ? 39  SER   A C   1 
ATOM   358  O O   . SER   A 1 43  ? -6.421  -22.793 11.745 1.00 6.43   ? 39  SER   A O   1 
ATOM   359  C CB  . SER   A 1 43  ? -7.733  -19.955 11.998 1.00 5.80   ? 39  SER   A CB  1 
ATOM   360  O OG  . SER   A 1 43  ? -6.623  -19.103 12.279 1.00 6.59   ? 39  SER   A OG  1 
ATOM   361  N N   . ARG   A 1 44  ? -5.448  -21.725 13.501 1.00 6.77   ? 40  ARG   A N   1 
ATOM   362  C CA  . ARG   A 1 44  ? -4.169  -22.433 13.372 1.00 7.36   ? 40  ARG   A CA  1 
ATOM   363  C C   . ARG   A 1 44  ? -4.382  -23.937 13.583 1.00 7.00   ? 40  ARG   A C   1 
ATOM   364  O O   . ARG   A 1 44  ? -3.752  -24.758 12.908 1.00 7.94   ? 40  ARG   A O   1 
ATOM   365  C CB  . ARG   A 1 44  ? -3.122  -21.871 14.333 1.00 8.42   ? 40  ARG   A CB  1 
ATOM   366  C CG  . ARG   A 1 44  ? -2.774  -20.392 14.128 1.00 12.33  ? 40  ARG   A CG  1 
ATOM   367  C CD  . ARG   A 1 44  ? -1.816  -19.854 15.219 0.80 13.88  ? 40  ARG   A CD  1 
ATOM   368  N NE  . ARG   A 1 44  ? -1.429  -18.449 15.005 1.00 15.18  ? 40  ARG   A NE  1 
ATOM   369  C CZ  . ARG   A 1 44  ? -1.902  -17.363 15.704 0.80 15.60  ? 40  ARG   A CZ  1 
ATOM   370  N NH1 . ARG   A 1 44  ? -2.691  -17.527 16.768 1.00 18.18  ? 40  ARG   A NH1 1 
ATOM   371  N NH2 . ARG   A 1 44  ? -1.510  -16.113 15.398 1.00 18.87  ? 40  ARG   A NH2 1 
ATOM   372  N N   . ASP   A 1 45  ? -5.287  -24.301 14.484 1.00 6.99   ? 41  ASP   A N   1 
ATOM   373  C CA  . ASP   A 1 45  ? -5.611  -25.705 14.792 1.00 6.90   ? 41  ASP   A CA  1 
ATOM   374  C C   . ASP   A 1 45  ? -6.196  -26.403 13.557 1.00 6.95   ? 41  ASP   A C   1 
ATOM   375  O O   . ASP   A 1 45  ? -6.085  -27.612 13.524 1.00 9.40   ? 41  ASP   A O   1 
ATOM   376  C CB  . ASP   A 1 45  ? -6.589  -25.810 15.977 1.00 7.78   ? 41  ASP   A CB  1 
ATOM   377  C CG  . ASP   A 1 45  ? -5.954  -25.655 17.364 1.00 8.07   ? 41  ASP   A CG  1 
ATOM   378  O OD1 . ASP   A 1 45  ? -4.695  -25.851 17.444 1.00 10.10  ? 41  ASP   A OD1 1 
ATOM   379  O OD2 . ASP   A 1 45  ? -6.685  -25.406 18.332 1.00 9.73   ? 41  ASP   A OD2 1 
ATOM   380  N N   . ARG   A 1 46  ? -6.804  -25.653 12.651 1.00 5.64   ? 42  ARG   A N   1 
ATOM   381  C CA  . ARG   A 1 46  ? -7.390  -26.220 11.443 1.00 6.60   ? 42  ARG   A CA  1 
ATOM   382  C C   . ARG   A 1 46  ? -6.464  -26.012 10.253 1.00 7.42   ? 42  ARG   A C   1 
ATOM   383  O O   . ARG   A 1 46  ? -6.867  -26.340 9.119  1.00 8.25   ? 42  ARG   A O   1 
ATOM   384  C CB  . ARG   A 1 46  ? -8.747  -25.578 11.193 1.00 7.37   ? 42  ARG   A CB  1 
ATOM   385  C CG  . ARG   A 1 46  ? -9.791  -25.922 12.236 1.00 7.89   ? 42  ARG   A CG  1 
ATOM   386  C CD  . ARG   A 1 46  ? -11.116 -25.271 11.986 1.00 7.34   ? 42  ARG   A CD  1 
ATOM   387  N NE  . ARG   A 1 46  ? -11.084 -23.828 12.178 1.00 6.95   ? 42  ARG   A NE  1 
ATOM   388  C CZ  . ARG   A 1 46  ? -11.440 -23.206 13.285 1.00 6.12   ? 42  ARG   A CZ  1 
ATOM   389  N NH1 . ARG   A 1 46  ? -11.416 -21.887 13.317 1.00 7.36   ? 42  ARG   A NH1 1 
ATOM   390  N NH2 . ARG   A 1 46  ? -11.782 -23.913 14.339 1.00 7.00   ? 42  ARG   A NH2 1 
ATOM   391  N N   . ASN   A 1 47  ? -5.266  -25.478 10.433 1.00 7.25   ? 43  ASN   A N   1 
ATOM   392  C CA  . ASN   A 1 47  ? -4.286  -25.331 9.337  1.00 7.90   ? 43  ASN   A CA  1 
ATOM   393  C C   . ASN   A 1 47  ? -4.854  -24.511 8.190  1.00 8.62   ? 43  ASN   A C   1 
ATOM   394  O O   . ASN   A 1 47  ? -4.483  -24.743 7.047  1.00 10.72  ? 43  ASN   A O   1 
ATOM   395  C CB  . ASN   A 1 47  ? -3.801  -26.673 8.804  1.00 9.02   ? 43  ASN   A CB  1 
ATOM   396  C CG  . ASN   A 1 47  ? -3.403  -27.552 9.941  1.00 8.11   ? 43  ASN   A CG  1 
ATOM   397  O OD1 . ASN   A 1 47  ? -2.437  -27.225 10.664 1.00 9.83   ? 43  ASN   A OD1 1 
ATOM   398  N ND2 . ASN   A 1 47  ? -4.135  -28.646 10.138 1.00 9.66   ? 43  ASN   A ND2 1 
ATOM   399  N N   A LYS   A 1 48  ? -5.697  -23.526 8.470  0.50 7.59   ? 44  LYS   A N   1 
ATOM   400  N N   B LYS   A 1 48  ? -5.718  -23.559 8.475  0.50 7.41   ? 44  LYS   A N   1 
ATOM   401  C CA  A LYS   A 1 48  ? -6.440  -22.816 7.409  0.50 9.03   ? 44  LYS   A CA  1 
ATOM   402  C CA  B LYS   A 1 48  ? -6.455  -22.880 7.402  0.50 8.70   ? 44  LYS   A CA  1 
ATOM   403  C C   A LYS   A 1 48  ? -6.751  -21.424 7.924  0.50 7.61   ? 44  LYS   A C   1 
ATOM   404  C C   B LYS   A 1 48  ? -6.813  -21.512 7.938  0.50 7.26   ? 44  LYS   A C   1 
ATOM   405  O O   A LYS   A 1 48  ? -7.490  -21.266 8.888  0.50 7.63   ? 44  LYS   A O   1 
ATOM   406  O O   B LYS   A 1 48  ? -7.462  -21.380 8.967  0.50 7.76   ? 44  LYS   A O   1 
ATOM   407  C CB  A LYS   A 1 48  ? -7.721  -23.565 7.047  0.50 10.76  ? 44  LYS   A CB  1 
ATOM   408  C CB  B LYS   A 1 48  ? -7.693  -23.663 6.986  0.50 10.32  ? 44  LYS   A CB  1 
ATOM   409  C CG  A LYS   A 1 48  ? -8.462  -22.980 5.860  0.50 13.42  ? 44  LYS   A CG  1 
ATOM   410  C CG  B LYS   A 1 48  ? -8.527  -22.925 5.966  0.50 12.43  ? 44  LYS   A CG  1 
ATOM   411  C CD  A LYS   A 1 48  ? -9.666  -23.789 5.405  0.50 17.75  ? 44  LYS   A CD  1 
ATOM   412  C CD  B LYS   A 1 48  ? -9.603  -23.773 5.337  0.50 15.67  ? 44  LYS   A CD  1 
ATOM   413  C CE  A LYS   A 1 48  ? -10.578 -23.015 4.473  0.50 20.46  ? 44  LYS   A CE  1 
ATOM   414  C CE  B LYS   A 1 48  ? -9.063  -24.858 4.426  0.50 17.85  ? 44  LYS   A CE  1 
ATOM   415  N NZ  A LYS   A 1 48  ? -10.961 -23.792 3.269  0.50 24.89  ? 44  LYS   A NZ  1 
ATOM   416  N NZ  B LYS   A 1 48  ? -10.149 -25.510 3.658  0.50 21.09  ? 44  LYS   A NZ  1 
ATOM   417  N N   A PRO   A 1 49  ? -6.176  -20.366 7.341  0.80 8.22   ? 45  PRO   A N   1 
ATOM   418  N N   B PRO   A 1 49  ? -6.389  -20.429 7.273  0.20 6.80   ? 45  PRO   A N   1 
ATOM   419  C CA  A PRO   A 1 49  ? -6.514  -19.009 7.751  0.80 9.09   ? 45  PRO   A CA  1 
ATOM   420  C CA  B PRO   A 1 49  ? -6.537  -19.104 7.849  0.20 7.03   ? 45  PRO   A CA  1 
ATOM   421  C C   A PRO   A 1 49  ? -8.014  -18.689 7.669  0.80 7.79   ? 45  PRO   A C   1 
ATOM   422  C C   B PRO   A 1 49  ? -7.984  -18.657 7.640  0.20 7.14   ? 45  PRO   A C   1 
ATOM   423  O O   A PRO   A 1 49  ? -8.746  -19.244 6.851  0.80 9.13   ? 45  PRO   A O   1 
ATOM   424  O O   B PRO   A 1 49  ? -8.651  -19.164 6.756  0.20 8.23   ? 45  PRO   A O   1 
ATOM   425  C CB  A PRO   A 1 49  ? -5.747  -18.172 6.701  0.80 12.16  ? 45  PRO   A CB  1 
ATOM   426  C CB  B PRO   A 1 49  ? -5.537  -18.294 7.019  0.20 7.26   ? 45  PRO   A CB  1 
ATOM   427  C CG  A PRO   A 1 49  ? -4.588  -19.021 6.250  0.80 13.90  ? 45  PRO   A CG  1 
ATOM   428  C CG  B PRO   A 1 49  ? -5.682  -18.902 5.644  0.20 7.05   ? 45  PRO   A CG  1 
ATOM   429  C CD  A PRO   A 1 49  ? -5.184  -20.403 6.252  0.80 10.77  ? 45  PRO   A CD  1 
ATOM   430  C CD  B PRO   A 1 49  ? -5.851  -20.387 5.907  0.20 6.66   ? 45  PRO   A CD  1 
ATOM   431  N N   . PHE   A 1 50  ? -8.401  -17.695 8.447  1.00 7.43   ? 46  PHE   A N   1 
ATOM   432  C CA  . PHE   A 1 50  ? -9.729  -17.087 8.422  1.00 7.19   ? 46  PHE   A CA  1 
ATOM   433  C C   . PHE   A 1 50  ? -9.685  -15.875 7.483  1.00 6.77   ? 46  PHE   A C   1 
ATOM   434  O O   . PHE   A 1 50  ? -8.719  -15.129 7.500  1.00 8.18   ? 46  PHE   A O   1 
ATOM   435  C CB  . PHE   A 1 50  ? -10.118 -16.706 9.841  1.00 7.30   ? 46  PHE   A CB  1 
ATOM   436  C CG  . PHE   A 1 50  ? -11.418 -15.989 9.983  1.00 7.87   ? 46  PHE   A CG  1 
ATOM   437  C CD1 . PHE   A 1 50  ? -12.602 -16.687 9.903  1.00 11.70  ? 46  PHE   A CD1 1 
ATOM   438  C CD2 . PHE   A 1 50  ? -11.468 -14.639 10.237 1.00 8.90   ? 46  PHE   A CD2 1 
ATOM   439  C CE1 . PHE   A 1 50  ? -13.803 -16.025 10.005 1.00 13.65  ? 46  PHE   A CE1 1 
ATOM   440  C CE2 . PHE   A 1 50  ? -12.675 -13.989 10.365 1.00 10.01  ? 46  PHE   A CE2 1 
ATOM   441  C CZ  . PHE   A 1 50  ? -13.831 -14.679 10.248 1.00 10.13  ? 46  PHE   A CZ  1 
ATOM   442  N N   . LYS   A 1 51  ? -10.776 -15.691 6.745  1.00 7.19   ? 47  LYS   A N   1 
ATOM   443  C CA  . LYS   A 1 51  ? -10.915 -14.526 5.863  1.00 7.96   ? 47  LYS   A CA  1 
ATOM   444  C C   . LYS   A 1 51  ? -12.178 -13.750 6.197  1.00 8.36   ? 47  LYS   A C   1 
ATOM   445  O O   . LYS   A 1 51  ? -13.224 -14.374 6.407  1.00 9.93   ? 47  LYS   A O   1 
ATOM   446  C CB  . LYS   A 1 51  ? -10.938 -14.944 4.394  1.00 9.19   ? 47  LYS   A CB  1 
ATOM   447  C CG  . LYS   A 1 51  ? -9.744  -15.783 3.986  1.00 10.73  ? 47  LYS   A CG  1 
ATOM   448  C CD  . LYS   A 1 51  ? -9.663  -15.971 2.494  1.00 13.63  ? 47  LYS   A CD  1 
ATOM   449  C CE  . LYS   A 1 51  ? -8.518  -16.866 2.098  1.00 17.28  ? 47  LYS   A CE  1 
ATOM   450  N NZ  . LYS   A 1 51  ? -8.382  -16.909 0.630  1.00 23.01  ? 47  LYS   A NZ  1 
ATOM   451  N N   . PHE   A 1 52  ? -12.097 -12.436 6.124  1.00 7.59   ? 48  PHE   A N   1 
ATOM   452  C CA  . PHE   A 1 52  ? -13.307 -11.608 6.253  1.00 7.85   ? 48  PHE   A CA  1 
ATOM   453  C C   . PHE   A 1 52  ? -13.067 -10.305 5.498  1.00 8.69   ? 48  PHE   A C   1 
ATOM   454  O O   . PHE   A 1 52  ? -11.928 -9.895  5.306  1.00 9.75   ? 48  PHE   A O   1 
ATOM   455  C CB  . PHE   A 1 52  ? -13.665 -11.372 7.720  1.00 8.24   ? 48  PHE   A CB  1 
ATOM   456  C CG  . PHE   A 1 52  ? -12.769 -10.379 8.397  1.00 9.35   ? 48  PHE   A CG  1 
ATOM   457  C CD1 . PHE   A 1 52  ? -11.534 -10.765 8.909  1.00 9.17   ? 48  PHE   A CD1 1 
ATOM   458  C CD2 . PHE   A 1 52  ? -13.207 -9.078  8.586  1.00 9.67   ? 48  PHE   A CD2 1 
ATOM   459  C CE1 . PHE   A 1 52  ? -10.734 -9.835  9.551  1.00 10.48  ? 48  PHE   A CE1 1 
ATOM   460  C CE2 . PHE   A 1 52  ? -12.375 -8.150  9.193  1.00 11.95  ? 48  PHE   A CE2 1 
ATOM   461  C CZ  . PHE   A 1 52  ? -11.158 -8.545  9.694  1.00 11.97  ? 48  PHE   A CZ  1 
ATOM   462  N N   A MET   A 1 53  ? -14.163 -9.625  5.201  0.80 10.16  ? 49  MET   A N   1 
ATOM   463  N N   B MET   A 1 53  ? -14.162 -9.640  5.134  0.20 9.91   ? 49  MET   A N   1 
ATOM   464  C CA  A MET   A 1 53  ? -14.138 -8.313  4.528  0.80 12.09  ? 49  MET   A CA  1 
ATOM   465  C CA  B MET   A 1 53  ? -14.145 -8.286  4.529  0.20 11.94  ? 49  MET   A CA  1 
ATOM   466  C C   A MET   A 1 53  ? -14.571 -7.217  5.497  0.80 11.89  ? 49  MET   A C   1 
ATOM   467  C C   B MET   A 1 53  ? -14.514 -7.249  5.586  0.20 12.48  ? 49  MET   A C   1 
ATOM   468  O O   A MET   A 1 53  ? -15.626 -7.396  6.102  0.80 11.75  ? 49  MET   A O   1 
ATOM   469  O O   B MET   A 1 53  ? -15.456 -7.507  6.351  0.20 14.31  ? 49  MET   A O   1 
ATOM   470  C CB  A MET   A 1 53  ? -15.102 -8.369  3.333  0.80 14.82  ? 49  MET   A CB  1 
ATOM   471  C CB  B MET   A 1 53  ? -15.152 -8.188  3.382  0.20 12.41  ? 49  MET   A CB  1 
ATOM   472  C CG  A MET   A 1 53  ? -15.118 -7.134  2.455  0.80 15.32  ? 49  MET   A CG  1 
ATOM   473  C CG  B MET   A 1 53  ? -15.307 -6.786  2.833  0.20 13.35  ? 49  MET   A CG  1 
ATOM   474  S SD  A MET   A 1 53  ? -16.076 -7.319  0.933  0.80 20.06  ? 49  MET   A SD  1 
ATOM   475  S SD  B MET   A 1 53  ? -15.722 -6.861  1.086  0.20 13.23  ? 49  MET   A SD  1 
ATOM   476  C CE  A MET   A 1 53  ? -14.792 -8.018  -0.099 0.80 20.72  ? 49  MET   A CE  1 
ATOM   477  C CE  B MET   A 1 53  ? -15.331 -8.590  0.829  0.20 9.60   ? 49  MET   A CE  1 
ATOM   478  N N   . LEU   A 1 54  ? -13.791 -6.124  5.618  1.00 14.17  ? 50  LEU   A N   1 
ATOM   479  C CA  . LEU   A 1 54  ? -14.169 -4.942  6.444  1.00 15.78  ? 50  LEU   A CA  1 
ATOM   480  C C   . LEU   A 1 54  ? -15.435 -4.300  5.904  1.00 15.03  ? 50  LEU   A C   1 
ATOM   481  O O   . LEU   A 1 54  ? -15.588 -4.233  4.665  1.00 19.58  ? 50  LEU   A O   1 
ATOM   482  C CB  . LEU   A 1 54  ? -13.073 -3.882  6.446  1.00 17.16  ? 50  LEU   A CB  1 
ATOM   483  C CG  . LEU   A 1 54  ? -11.874 -4.171  7.322  1.00 16.25  ? 50  LEU   A CG  1 
ATOM   484  C CD1 . LEU   A 1 54  ? -10.801 -3.133  7.051  1.00 21.01  ? 50  LEU   A CD1 1 
ATOM   485  C CD2 . LEU   A 1 54  ? -12.210 -4.251  8.786  1.00 14.59  ? 50  LEU   A CD2 1 
ATOM   486  N N   . GLY   A 1 55  ? -16.256 -3.784  6.808  1.00 15.83  ? 51  GLY   A N   1 
ATOM   487  C CA  . GLY   A 1 55  ? -17.429 -2.943  6.533  1.00 16.78  ? 51  GLY   A CA  1 
ATOM   488  C C   . GLY   A 1 55  ? -18.677 -3.738  6.198  1.00 15.57  ? 51  GLY   A C   1 
ATOM   489  O O   . GLY   A 1 55  ? -19.641 -3.143  5.737  1.00 19.60  ? 51  GLY   A O   1 
ATOM   490  N N   A LYS   A 1 56  ? -18.690 -5.031  6.500  0.50 15.06  ? 52  LYS   A N   1 
ATOM   491  N N   B LYS   A 1 56  ? -18.671 -5.042  6.454  0.50 13.90  ? 52  LYS   A N   1 
ATOM   492  C CA  A LYS   A 1 56  ? -19.808 -5.931  6.115  0.50 15.62  ? 52  LYS   A CA  1 
ATOM   493  C CA  B LYS   A 1 56  ? -19.722 -5.982  5.972  0.50 13.60  ? 52  LYS   A CA  1 
ATOM   494  C C   A LYS   A 1 56  ? -20.346 -6.701  7.327  0.50 13.70  ? 52  LYS   A C   1 
ATOM   495  C C   B LYS   A 1 56  ? -20.391 -6.702  7.133  0.50 12.65  ? 52  LYS   A C   1 
ATOM   496  O O   A LYS   A 1 56  ? -20.971 -7.745  7.129  0.50 13.14  ? 52  LYS   A O   1 
ATOM   497  O O   B LYS   A 1 56  ? -21.184 -7.636  6.921  0.50 14.43  ? 52  LYS   A O   1 
ATOM   498  C CB  A LYS   A 1 56  ? -19.342 -6.868  5.002  0.50 16.77  ? 52  LYS   A CB  1 
ATOM   499  C CB  B LYS   A 1 56  ? -19.097 -6.990  5.024  0.50 13.13  ? 52  LYS   A CB  1 
ATOM   500  C CG  A LYS   A 1 56  ? -20.435 -7.720  4.378  0.30 18.92  ? 52  LYS   A CG  1 
ATOM   501  C CG  B LYS   A 1 56  ? -18.587 -6.318  3.767  0.30 12.16  ? 52  LYS   A CG  1 
ATOM   502  C CD  A LYS   A 1 56  ? -21.640 -6.945  3.901  0.30 20.83  ? 52  LYS   A CD  1 
ATOM   503  C CD  B LYS   A 1 56  ? -19.673 -5.610  2.991  0.30 13.07  ? 52  LYS   A CD  1 
ATOM   504  C CE  A LYS   A 1 56  ? -22.910 -7.754  4.052  0.30 21.03  ? 52  LYS   A CE  1 
ATOM   505  C CE  B LYS   A 1 56  ? -19.180 -5.228  1.622  0.30 16.36  ? 52  LYS   A CE  1 
ATOM   506  N NZ  A LYS   A 1 56  ? -22.775 -8.757  5.135  0.30 18.90  ? 52  LYS   A NZ  1 
ATOM   507  N NZ  B LYS   A 1 56  ? -18.761 -6.447  0.908  0.30 14.47  ? 52  LYS   A NZ  1 
ATOM   508  N N   A GLN   A 1 57  ? -20.124 -6.220  8.552  0.80 12.26  ? 53  GLN   A N   1 
ATOM   509  N N   B GLN   A 1 57  ? -20.034 -6.280  8.344  0.20 11.42  ? 53  GLN   A N   1 
ATOM   510  C CA  A GLN   A 1 57  ? -20.662 -6.880  9.763  0.80 12.80  ? 53  GLN   A CA  1 
ATOM   511  C CA  B GLN   A 1 57  ? -20.609 -6.823  9.595  0.20 10.93  ? 53  GLN   A CA  1 
ATOM   512  C C   A GLN   A 1 57  ? -20.303 -8.365  9.705  0.80 11.44  ? 53  GLN   A C   1 
ATOM   513  C C   B GLN   A 1 57  ? -20.318 -8.320  9.649  0.20 9.91   ? 53  GLN   A C   1 
ATOM   514  O O   A GLN   A 1 57  ? -21.072 -9.165  10.187 0.80 12.43  ? 53  GLN   A O   1 
ATOM   515  O O   B GLN   A 1 57  ? -21.216 -9.075  10.050 0.20 11.06  ? 53  GLN   A O   1 
ATOM   516  C CB  A GLN   A 1 57  ? -22.181 -6.708  9.938  0.80 13.57  ? 53  GLN   A CB  1 
ATOM   517  C CB  B GLN   A 1 57  ? -22.106 -6.531  9.634  0.20 11.16  ? 53  GLN   A CB  1 
ATOM   518  C CG  A GLN   A 1 57  ? -22.672 -5.279  10.114 0.80 15.39  ? 53  GLN   A CG  1 
ATOM   519  C CG  B GLN   A 1 57  ? -22.413 -5.050  9.558  0.20 10.74  ? 53  GLN   A CG  1 
ATOM   520  C CD  A GLN   A 1 57  ? -22.689 -4.466  8.845  0.80 14.09  ? 53  GLN   A CD  1 
ATOM   521  C CD  B GLN   A 1 57  ? -22.261 -4.391  10.910 0.20 10.58  ? 53  GLN   A CD  1 
ATOM   522  O OE1 A GLN   A 1 57  ? -22.312 -3.280  8.825  0.80 20.26  ? 53  GLN   A OE1 1 
ATOM   523  O OE1 B GLN   A 1 57  ? -21.405 -4.733  11.734 0.20 11.00  ? 53  GLN   A OE1 1 
ATOM   524  N NE2 A GLN   A 1 57  ? -23.191 -5.059  7.781  0.80 15.98  ? 53  GLN   A NE2 1 
ATOM   525  N NE2 B GLN   A 1 57  ? -23.157 -3.465  11.184 0.20 8.88   ? 53  GLN   A NE2 1 
ATOM   526  N N   . GLU   A 1 58  ? -19.088 -8.709  9.305  1.00 9.08   ? 54  GLU   A N   1 
ATOM   527  C CA  . GLU   A 1 58  ? -18.691 -10.137 9.201  1.00 10.14  ? 54  GLU   A CA  1 
ATOM   528  C C   . GLU   A 1 58  ? -18.033 -10.676 10.471 1.00 9.19   ? 54  GLU   A C   1 
ATOM   529  O O   . GLU   A 1 58  ? -17.893 -11.870 10.622 1.00 12.05  ? 54  GLU   A O   1 
ATOM   530  C CB  . GLU   A 1 58  ? -17.764 -10.361 8.014  1.00 10.29  ? 54  GLU   A CB  1 
ATOM   531  C CG  . GLU   A 1 58  ? -18.555 -10.337 6.707  1.00 11.75  ? 54  GLU   A CG  1 
ATOM   532  C CD  . GLU   A 1 58  ? -17.767 -10.623 5.438  1.00 11.65  ? 54  GLU   A CD  1 
ATOM   533  O OE1 . GLU   A 1 58  ? -18.326 -10.460 4.355  1.00 15.22  ? 54  GLU   A OE1 1 
ATOM   534  O OE2 . GLU   A 1 58  ? -16.612 -11.067 5.540  1.00 12.44  ? 54  GLU   A OE2 1 
ATOM   535  N N   . VAL   A 1 59  ? -17.588 -9.775  11.323 1.00 7.49   ? 55  VAL   A N   1 
ATOM   536  C CA  . VAL   A 1 59  ? -16.839 -10.132 12.540 1.00 6.97   ? 55  VAL   A CA  1 
ATOM   537  C C   . VAL   A 1 59  ? -17.313 -9.271  13.690 1.00 5.55   ? 55  VAL   A C   1 
ATOM   538  O O   . VAL   A 1 59  ? -17.790 -8.173  13.511 1.00 6.63   ? 55  VAL   A O   1 
ATOM   539  C CB  . VAL   A 1 59  ? -15.322 -9.995  12.327 1.00 7.43   ? 55  VAL   A CB  1 
ATOM   540  C CG1 . VAL   A 1 59  ? -14.821 -11.016 11.321 1.00 9.26   ? 55  VAL   A CG1 1 
ATOM   541  C CG2 . VAL   A 1 59  ? -14.906 -8.595  11.932 1.00 7.49   ? 55  VAL   A CG2 1 
ATOM   542  N N   . ILE   A 1 60  ? -17.096 -9.784  14.906 1.00 6.03   ? 56  ILE   A N   1 
ATOM   543  C CA  . ILE   A 1 60  ? -17.395 -8.965  16.109 1.00 5.86   ? 56  ILE   A CA  1 
ATOM   544  C C   . ILE   A 1 60  ? -16.652 -7.627  16.017 1.00 5.82   ? 56  ILE   A C   1 
ATOM   545  O O   . ILE   A 1 60  ? -15.567 -7.539  15.405 1.00 6.03   ? 56  ILE   A O   1 
ATOM   546  C CB  . ILE   A 1 60  ? -17.068 -9.728  17.390 1.00 6.01   ? 56  ILE   A CB  1 
ATOM   547  C CG1 . ILE   A 1 60  ? -15.626 -10.223 17.432 1.00 6.42   ? 56  ILE   A CG1 1 
ATOM   548  C CG2 . ILE   A 1 60  ? -18.060 -10.847 17.606 1.00 6.90   ? 56  ILE   A CG2 1 
ATOM   549  C CD1 . ILE   A 1 60  ? -15.178 -10.753 18.770 1.00 6.77   ? 56  ILE   A CD1 1 
ATOM   550  N N   . ARG   A 1 61  ? -17.221 -6.615  16.649 1.00 5.99   ? 57  ARG   A N   1 
ATOM   551  C CA  . ARG   A 1 61  ? -16.750 -5.236  16.429 1.00 6.01   ? 57  ARG   A CA  1 
ATOM   552  C C   . ARG   A 1 61  ? -15.287 -5.047  16.813 1.00 6.86   ? 57  ARG   A C   1 
ATOM   553  O O   . ARG   A 1 61  ? -14.582 -4.279  16.159 1.00 7.17   ? 57  ARG   A O   1 
ATOM   554  C CB  . ARG   A 1 61  ? -17.650 -4.240  17.143 1.00 6.10   ? 57  ARG   A CB  1 
ATOM   555  C CG  . ARG   A 1 61  ? -17.268 -2.804  16.830 1.00 6.54   ? 57  ARG   A CG  1 
ATOM   556  C CD  . ARG   A 1 61  ? -17.535 -2.407  15.397 1.00 7.37   ? 57  ARG   A CD  1 
ATOM   557  N NE  . ARG   A 1 61  ? -17.064 -1.057  15.160 1.00 6.83   ? 57  ARG   A NE  1 
ATOM   558  C CZ  . ARG   A 1 61  ? -17.209 -0.411  14.020 1.00 7.26   ? 57  ARG   A CZ  1 
ATOM   559  N NH1 . ARG   A 1 61  ? -17.871 -0.962  13.006 1.00 9.25   ? 57  ARG   A NH1 1 
ATOM   560  N NH2 . ARG   A 1 61  ? -16.678 0.805   13.894 1.00 7.83   ? 57  ARG   A NH2 1 
ATOM   561  N N   . GLY   A 1 62  ? -14.842 -5.665  17.883 1.00 6.33   ? 58  GLY   A N   1 
ATOM   562  C CA  . GLY   A 1 62  ? -13.444 -5.540  18.318 1.00 6.83   ? 58  GLY   A CA  1 
ATOM   563  C C   . GLY   A 1 62  ? -12.472 -6.047  17.277 1.00 6.65   ? 58  GLY   A C   1 
ATOM   564  O O   . GLY   A 1 62  ? -11.342 -5.563  17.184 1.00 7.27   ? 58  GLY   A O   1 
ATOM   565  N N   . TRP   A 1 63  ? -12.856 -7.063  16.506 1.00 6.98   ? 59  TRP   A N   1 
ATOM   566  C CA  . TRP   A 1 63  ? -12.054 -7.470  15.314 1.00 7.41   ? 59  TRP   A CA  1 
ATOM   567  C C   . TRP   A 1 63  ? -12.079 -6.418  14.214 1.00 7.11   ? 59  TRP   A C   1 
ATOM   568  O O   . TRP   A 1 63  ? -11.018 -6.126  13.610 1.00 8.41   ? 59  TRP   A O   1 
ATOM   569  C CB  . TRP   A 1 63  ? -12.553 -8.800  14.748 1.00 7.64   ? 59  TRP   A CB  1 
ATOM   570  C CG  . TRP   A 1 63  ? -11.840 -10.004 15.276 1.00 6.59   ? 59  TRP   A CG  1 
ATOM   571  C CD1 . TRP   A 1 63  ? -11.775 -10.444 16.561 1.00 7.73   ? 59  TRP   A CD1 1 
ATOM   572  C CD2 . TRP   A 1 63  ? -11.097 -10.927 14.488 1.00 6.02   ? 59  TRP   A CD2 1 
ATOM   573  N NE1 . TRP   A 1 63  ? -11.008 -11.576 16.634 1.00 8.05   ? 59  TRP   A NE1 1 
ATOM   574  C CE2 . TRP   A 1 63  ? -10.601 -11.920 15.362 1.00 6.73   ? 59  TRP   A CE2 1 
ATOM   575  C CE3 . TRP   A 1 63  ? -10.845 -11.067 13.116 1.00 6.92   ? 59  TRP   A CE3 1 
ATOM   576  C CZ2 . TRP   A 1 63  ? -9.834  -12.993 14.915 1.00 7.11   ? 59  TRP   A CZ2 1 
ATOM   577  C CZ3 . TRP   A 1 63  ? -10.063 -12.117 12.666 1.00 7.01   ? 59  TRP   A CZ3 1 
ATOM   578  C CH2 . TRP   A 1 63  ? -9.632  -13.091 13.558 1.00 8.23   ? 59  TRP   A CH2 1 
ATOM   579  N N   A GLU   A 1 64  ? -13.272 -5.914  13.893 0.10 7.56   ? 60  GLU   A N   1 
ATOM   580  N N   B GLU   A 1 64  ? -13.237 -5.899  13.908 0.90 7.46   ? 60  GLU   A N   1 
ATOM   581  C CA  A GLU   A 1 64  ? -13.468 -4.835  12.891 0.10 8.09   ? 60  GLU   A CA  1 
ATOM   582  C CA  B GLU   A 1 64  ? -13.358 -4.891  12.846 0.90 8.37   ? 60  GLU   A CA  1 
ATOM   583  C C   A GLU   A 1 64  ? -12.451 -3.726  13.148 0.10 8.56   ? 60  GLU   A C   1 
ATOM   584  C C   B GLU   A 1 64  ? -12.385 -3.752  13.165 0.90 9.33   ? 60  GLU   A C   1 
ATOM   585  O O   A GLU   A 1 64  ? -11.709 -3.362  12.217 0.10 9.18   ? 60  GLU   A O   1 
ATOM   586  O O   B GLU   A 1 64  ? -11.593 -3.354  12.302 0.90 11.67  ? 60  GLU   A O   1 
ATOM   587  C CB  A GLU   A 1 64  ? -14.867 -4.234  12.991 0.10 8.29   ? 60  GLU   A CB  1 
ATOM   588  C CB  B GLU   A 1 64  ? -14.815 -4.443  12.745 0.90 8.89   ? 60  GLU   A CB  1 
ATOM   589  C CG  A GLU   A 1 64  ? -15.843 -4.845  12.021 0.10 8.43   ? 60  GLU   A CG  1 
ATOM   590  C CG  B GLU   A 1 64  ? -15.092 -3.508  11.591 0.90 9.98   ? 60  GLU   A CG  1 
ATOM   591  C CD  A GLU   A 1 64  ? -15.566 -4.514  10.567 0.10 8.19   ? 60  GLU   A CD  1 
ATOM   592  C CD  B GLU   A 1 64  ? -15.479 -4.188  10.311 0.90 11.87  ? 60  GLU   A CD  1 
ATOM   593  O OE1 A GLU   A 1 64  ? -15.899 -3.385  10.145 0.10 7.48   ? 60  GLU   A OE1 1 
ATOM   594  O OE1 B GLU   A 1 64  ? -15.644 -3.461  9.311  0.90 15.79  ? 60  GLU   A OE1 1 
ATOM   595  O OE2 A GLU   A 1 64  ? -15.019 -5.386  9.863  0.10 7.84   ? 60  GLU   A OE2 1 
ATOM   596  O OE2 B GLU   A 1 64  ? -15.697 -5.416  10.314 0.90 15.25  ? 60  GLU   A OE2 1 
ATOM   597  N N   . GLU   A 1 65  ? -12.441 -3.213  14.378 1.00 8.44   ? 61  GLU   A N   1 
ATOM   598  C CA  . GLU   A 1 65  ? -11.595 -2.059  14.751 1.00 8.70   ? 61  GLU   A CA  1 
ATOM   599  C C   . GLU   A 1 65  ? -10.153 -2.505  15.012 1.00 7.88   ? 61  GLU   A C   1 
ATOM   600  O O   . GLU   A 1 65  ? -9.243  -1.750  14.704 1.00 11.01  ? 61  GLU   A O   1 
ATOM   601  C CB  . GLU   A 1 65  ? -12.214 -1.339  15.936 1.00 9.71   ? 61  GLU   A CB  1 
ATOM   602  C CG  . GLU   A 1 65  ? -13.503 -0.637  15.586 1.00 10.39  ? 61  GLU   A CG  1 
ATOM   603  C CD  . GLU   A 1 65  ? -14.056 0.302   16.640 1.00 10.38  ? 61  GLU   A CD  1 
ATOM   604  O OE1 . GLU   A 1 65  ? -13.261 0.827   17.443 1.00 13.77  ? 61  GLU   A OE1 1 
ATOM   605  O OE2 . GLU   A 1 65  ? -15.281 0.533   16.646 1.00 8.83   ? 61  GLU   A OE2 1 
ATOM   606  N N   . GLY   A 1 66  ? -9.937  -3.669  15.580 1.00 7.53   ? 62  GLY   A N   1 
ATOM   607  C CA  . GLY   A 1 66  ? -8.583  -4.092  15.973 1.00 7.86   ? 62  GLY   A CA  1 
ATOM   608  C C   . GLY   A 1 66  ? -7.746  -4.493  14.774 1.00 6.35   ? 62  GLY   A C   1 
ATOM   609  O O   . GLY   A 1 66  ? -6.612  -4.040  14.638 1.00 7.33   ? 62  GLY   A O   1 
ATOM   610  N N   . VAL   A 1 67  ? -8.310  -5.339  13.908 1.00 6.20   ? 63  VAL   A N   1 
ATOM   611  C CA  . VAL   A 1 67  ? -7.540  -5.773  12.709 1.00 7.09   ? 63  VAL   A CA  1 
ATOM   612  C C   . VAL   A 1 67  ? -7.317  -4.579  11.764 1.00 7.02   ? 63  VAL   A C   1 
ATOM   613  O O   . VAL   A 1 67  ? -6.263  -4.512  11.116 1.00 8.60   ? 63  VAL   A O   1 
ATOM   614  C CB  . VAL   A 1 67  ? -8.197  -6.988  12.034 1.00 8.41   ? 63  VAL   A CB  1 
ATOM   615  C CG1 . VAL   A 1 67  ? -7.462  -7.343  10.762 1.00 10.48  ? 63  VAL   A CG1 1 
ATOM   616  C CG2 . VAL   A 1 67  ? -8.268  -8.183  12.983 1.00 9.52   ? 63  VAL   A CG2 1 
ATOM   617  N N   . ALA   A 1 68  ? -8.249  -3.659  11.716 1.00 7.41   ? 64  ALA   A N   1 
ATOM   618  C CA  . ALA   A 1 68  ? -8.089  -2.462  10.875 1.00 9.51   ? 64  ALA   A CA  1 
ATOM   619  C C   . ALA   A 1 68  ? -6.840  -1.653  11.256 1.00 9.14   ? 64  ALA   A C   1 
ATOM   620  O O   . ALA   A 1 68  ? -6.303  -0.897  10.422 1.00 11.56  ? 64  ALA   A O   1 
ATOM   621  C CB  . ALA   A 1 68  ? -9.345  -1.647  10.893 1.00 11.69  ? 64  ALA   A CB  1 
ATOM   622  N N   A GLN   A 1 69  ? -6.382  -1.735  12.502 0.90 8.75   ? 65  GLN   A N   1 
ATOM   623  N N   B GLN   A 1 69  ? -6.412  -1.782  12.518 0.10 7.57   ? 65  GLN   A N   1 
ATOM   624  C CA  A GLN   A 1 69  ? -5.186  -0.997  12.970 0.90 10.99  ? 65  GLN   A CA  1 
ATOM   625  C CA  B GLN   A 1 69  ? -5.243  -1.080  13.118 0.10 7.18   ? 65  GLN   A CA  1 
ATOM   626  C C   A GLN   A 1 69  ? -3.883  -1.724  12.648 0.90 10.38  ? 65  GLN   A C   1 
ATOM   627  C C   B GLN   A 1 69  ? -3.922  -1.716  12.669 0.10 7.56   ? 65  GLN   A C   1 
ATOM   628  O O   A GLN   A 1 69  ? -2.823  -1.144  12.866 0.90 11.59  ? 65  GLN   A O   1 
ATOM   629  O O   B GLN   A 1 69  ? -2.873  -1.067  12.852 0.10 7.72   ? 65  GLN   A O   1 
ATOM   630  C CB  A GLN   A 1 69  ? -5.181  -0.835  14.486 0.90 13.12  ? 65  GLN   A CB  1 
ATOM   631  C CB  B GLN   A 1 69  ? -5.322  -1.124  14.647 0.10 5.75   ? 65  GLN   A CB  1 
ATOM   632  C CG  A GLN   A 1 69  ? -6.265  0.070   15.024 0.90 15.75  ? 65  GLN   A CG  1 
ATOM   633  C CG  B GLN   A 1 69  ? -6.388  -0.209  15.232 0.10 5.05   ? 65  GLN   A CG  1 
ATOM   634  C CD  A GLN   A 1 69  ? -6.243  0.029   16.529 0.90 18.99  ? 65  GLN   A CD  1 
ATOM   635  C CD  B GLN   A 1 69  ? -6.066  1.247   14.997 0.10 4.85   ? 65  GLN   A CD  1 
ATOM   636  O OE1 A GLN   A 1 69  ? -5.207  0.218   17.175 0.90 22.06  ? 65  GLN   A OE1 1 
ATOM   637  O OE1 B GLN   A 1 69  ? -4.918  1.665   15.083 0.10 5.58   ? 65  GLN   A OE1 1 
ATOM   638  N NE2 A GLN   A 1 69  ? -7.403  -0.273  17.076 0.90 18.63  ? 65  GLN   A NE2 1 
ATOM   639  N NE2 B GLN   A 1 69  ? -7.080  2.020   14.653 0.10 4.22   ? 65  GLN   A NE2 1 
ATOM   640  N N   . MET   A 1 70  ? -3.974  -2.926  12.102 1.00 7.16   ? 66  MET   A N   1 
ATOM   641  C CA  . MET   A 1 70  ? -2.788  -3.762  11.841 1.00 7.78   ? 66  MET   A CA  1 
ATOM   642  C C   . MET   A 1 70  ? -2.321  -3.608  10.395 1.00 6.84   ? 66  MET   A C   1 
ATOM   643  O O   . MET   A 1 70  ? -3.130  -3.346  9.484  1.00 8.36   ? 66  MET   A O   1 
ATOM   644  C CB  . MET   A 1 70  ? -3.117  -5.221  12.132 1.00 7.51   ? 66  MET   A CB  1 
ATOM   645  C CG  . MET   A 1 70  ? -3.415  -5.444  13.588 1.00 7.87   ? 66  MET   A CG  1 
ATOM   646  S SD  . MET   A 1 70  ? -3.947  -7.152  13.983 1.00 9.34   ? 66  MET   A SD  1 
ATOM   647  C CE  . MET   A 1 70  ? -2.430  -8.040  13.630 1.00 8.99   ? 66  MET   A CE  1 
ATOM   648  N N   . SER   A 1 71  ? -1.033  -3.800  10.214 1.00 6.44   ? 67  SER   A N   1 
ATOM   649  C CA  . SER   A 1 71  ? -0.477  -3.858  8.857  1.00 6.95   ? 67  SER   A CA  1 
ATOM   650  C C   . SER   A 1 71  ? -0.009  -5.270  8.525  1.00 6.71   ? 67  SER   A C   1 
ATOM   651  O O   . SER   A 1 71  ? 0.139   -6.149  9.422  1.00 7.00   ? 67  SER   A O   1 
ATOM   652  C CB  . SER   A 1 71  ? 0.672   -2.879  8.683  1.00 7.43   ? 67  SER   A CB  1 
ATOM   653  O OG  . SER   A 1 71  ? 1.729   -3.129  9.630  1.00 7.69   ? 67  SER   A OG  1 
ATOM   654  N N   . VAL   A 1 72  ? 0.121   -5.554  7.240  1.00 7.17   ? 68  VAL   A N   1 
ATOM   655  C CA  . VAL   A 1 72  ? 0.442   -6.928  6.796  1.00 7.82   ? 68  VAL   A CA  1 
ATOM   656  C C   . VAL   A 1 72  ? 1.755   -7.364  7.446  1.00 7.28   ? 68  VAL   A C   1 
ATOM   657  O O   . VAL   A 1 72  ? 2.768   -6.619  7.445  1.00 8.10   ? 68  VAL   A O   1 
ATOM   658  C CB  . VAL   A 1 72  ? 0.474   -7.016  5.273  1.00 8.85   ? 68  VAL   A CB  1 
ATOM   659  C CG1 . VAL   A 1 72  ? 0.997   -8.373  4.816  1.00 10.21  ? 68  VAL   A CG1 1 
ATOM   660  C CG2 . VAL   A 1 72  ? -0.911  -6.730  4.733  1.00 9.93   ? 68  VAL   A CG2 1 
ATOM   661  N N   . GLY   A 1 73  ? 1.738   -8.580  7.983  1.00 6.85   ? 69  GLY   A N   1 
ATOM   662  C CA  . GLY   A 1 73  ? 2.876   -9.165  8.693  1.00 7.99   ? 69  GLY   A CA  1 
ATOM   663  C C   . GLY   A 1 73  ? 2.753   -9.017  10.192 1.00 8.47   ? 69  GLY   A C   1 
ATOM   664  O O   . GLY   A 1 73  ? 3.480   -9.697  10.919 1.00 10.74  ? 69  GLY   A O   1 
ATOM   665  N N   . GLN   A 1 74  ? 1.912   -8.123  10.682 1.00 6.35   ? 70  GLN   A N   1 
ATOM   666  C CA  . GLN   A 1 74  ? 1.834   -7.879  12.145 1.00 5.70   ? 70  GLN   A CA  1 
ATOM   667  C C   . GLN   A 1 74  ? 1.149   -9.036  12.844 1.00 6.25   ? 70  GLN   A C   1 
ATOM   668  O O   . GLN   A 1 74  ? 0.143   -9.555  12.349 1.00 6.47   ? 70  GLN   A O   1 
ATOM   669  C CB  . GLN   A 1 74  ? 1.093   -6.569  12.383 1.00 6.08   ? 70  GLN   A CB  1 
ATOM   670  C CG  . GLN   A 1 74  ? 1.166   -6.052  13.800 1.00 6.52   ? 70  GLN   A CG  1 
ATOM   671  C CD  . GLN   A 1 74  ? 0.523   -4.692  13.920 1.00 7.27   ? 70  GLN   A CD  1 
ATOM   672  O OE1 . GLN   A 1 74  ? 0.046   -4.111  12.945 1.00 8.36   ? 70  GLN   A OE1 1 
ATOM   673  N NE2 . GLN   A 1 74  ? 0.489   -4.147  15.131 1.00 8.03   ? 70  GLN   A NE2 1 
ATOM   674  N N   . ARG   A 1 75  ? 1.643   -9.343  14.026 1.00 6.18   ? 71  ARG   A N   1 
ATOM   675  C CA  . ARG   A 1 75  ? 1.014   -10.256 14.973 1.00 5.73   ? 71  ARG   A CA  1 
ATOM   676  C C   . ARG   A 1 75  ? 0.727   -9.433  16.222 1.00 6.46   ? 71  ARG   A C   1 
ATOM   677  O O   . ARG   A 1 75  ? 1.617   -8.729  16.702 1.00 6.58   ? 71  ARG   A O   1 
ATOM   678  C CB  . ARG   A 1 75  ? 1.920   -11.421 15.319 1.00 6.64   ? 71  ARG   A CB  1 
ATOM   679  C CG  . ARG   A 1 75  ? 1.269   -12.461 16.213 1.00 7.68   ? 71  ARG   A CG  1 
ATOM   680  C CD  . ARG   A 1 75  ? 2.168   -13.656 16.354 1.00 11.14  ? 71  ARG   A CD  1 
ATOM   681  N NE  . ARG   A 1 75  ? 1.795   -14.438 17.516 1.00 13.94  ? 71  ARG   A NE  1 
ATOM   682  C CZ  . ARG   A 1 75  ? 2.635   -15.146 18.272 1.00 14.10  ? 71  ARG   A CZ  1 
ATOM   683  N NH1 . ARG   A 1 75  ? 3.925   -15.222 17.962 1.00 16.45  ? 71  ARG   A NH1 1 
ATOM   684  N NH2 . ARG   A 1 75  ? 2.191   -15.806 19.326 1.00 17.09  ? 71  ARG   A NH2 1 
ATOM   685  N N   . ALA   A 1 76  ? -0.489  -9.508  16.729 1.00 6.17   ? 72  ALA   A N   1 
ATOM   686  C CA  . ALA   A 1 76  ? -0.921  -8.681  17.869 1.00 6.94   ? 72  ALA   A CA  1 
ATOM   687  C C   . ALA   A 1 76  ? -1.833  -9.470  18.770 1.00 6.91   ? 72  ALA   A C   1 
ATOM   688  O O   . ALA   A 1 76  ? -2.501  -10.396 18.339 1.00 7.42   ? 72  ALA   A O   1 
ATOM   689  C CB  . ALA   A 1 76  ? -1.601  -7.420  17.334 1.00 8.23   ? 72  ALA   A CB  1 
ATOM   690  N N   . LYS   A 1 77  ? -1.849  -9.019  20.012 1.00 6.70   ? 73  LYS   A N   1 
ATOM   691  C CA  . LYS   A 1 77  ? -2.849  -9.406  21.020 1.00 7.22   ? 73  LYS   A CA  1 
ATOM   692  C C   . LYS   A 1 77  ? -3.959  -8.368  20.997 1.00 6.84   ? 73  LYS   A C   1 
ATOM   693  O O   . LYS   A 1 77  ? -3.701  -7.198  21.305 1.00 7.66   ? 73  LYS   A O   1 
ATOM   694  C CB  . LYS   A 1 77  ? -2.166  -9.489  22.384 1.00 9.35   ? 73  LYS   A CB  1 
ATOM   695  C CG  . LYS   A 1 77  ? -3.053  -9.975  23.534 1.00 12.37  ? 73  LYS   A CG  1 
ATOM   696  C CD  . LYS   A 1 77  ? -2.372  -9.853  24.926 1.00 18.46  ? 73  LYS   A CD  1 
ATOM   697  C CE  . LYS   A 1 77  ? -3.250  -10.268 26.073 1.00 20.26  ? 73  LYS   A CE  1 
ATOM   698  N NZ  . LYS   A 1 77  ? -2.617  -9.998  27.378 1.00 28.80  ? 73  LYS   A NZ  1 
ATOM   699  N N   . LEU   A 1 78  ? -5.162  -8.826  20.757 1.00 5.21   ? 74  LEU   A N   1 
ATOM   700  C CA  . LEU   A 1 78  ? -6.377  -7.989  20.802 1.00 6.90   ? 74  LEU   A CA  1 
ATOM   701  C C   . LEU   A 1 78  ? -7.140  -8.371  22.050 1.00 6.90   ? 74  LEU   A C   1 
ATOM   702  O O   . LEU   A 1 78  ? -7.532  -9.527  22.189 1.00 9.81   ? 74  LEU   A O   1 
ATOM   703  C CB  . LEU   A 1 78  ? -7.300  -8.249  19.625 1.00 9.47   ? 74  LEU   A CB  1 
ATOM   704  C CG  . LEU   A 1 78  ? -6.815  -7.987  18.219 1.00 13.48  ? 74  LEU   A CG  1 
ATOM   705  C CD1 . LEU   A 1 78  ? -7.982  -8.092  17.248 1.00 15.59  ? 74  LEU   A CD1 1 
ATOM   706  C CD2 . LEU   A 1 78  ? -6.100  -6.686  18.066 1.00 17.08  ? 74  LEU   A CD2 1 
ATOM   707  N N   . THR   A 1 79  ? -7.388  -7.393  22.923 1.00 6.44   ? 75  THR   A N   1 
ATOM   708  C CA  . THR   A 1 79  ? -8.222  -7.614  24.114 1.00 7.32   ? 75  THR   A CA  1 
ATOM   709  C C   . THR   A 1 79  ? -9.499  -6.832  23.921 1.00 6.99   ? 75  THR   A C   1 
ATOM   710  O O   . THR   A 1 79  ? -9.457  -5.627  23.683 1.00 8.01   ? 75  THR   A O   1 
ATOM   711  C CB  . THR   A 1 79  ? -7.536  -7.174  25.398 1.00 8.30   ? 75  THR   A CB  1 
ATOM   712  O OG1 . THR   A 1 79  ? -6.286  -7.848  25.484 1.00 9.54   ? 75  THR   A OG1 1 
ATOM   713  C CG2 . THR   A 1 79  ? -8.358  -7.463  26.635 1.00 9.91   ? 75  THR   A CG2 1 
ATOM   714  N N   . ILE   A 1 80  ? -10.626 -7.524  23.943 1.00 5.83   ? 76  ILE   A N   1 
ATOM   715  C CA  . ILE   A 1 80  ? -11.930 -7.001  23.470 1.00 5.71   ? 76  ILE   A CA  1 
ATOM   716  C C   . ILE   A 1 80  ? -12.955 -7.099  24.580 1.00 5.90   ? 76  ILE   A C   1 
ATOM   717  O O   . ILE   A 1 80  ? -13.205 -8.185  25.107 1.00 6.80   ? 76  ILE   A O   1 
ATOM   718  C CB  . ILE   A 1 80  ? -12.414 -7.741  22.221 1.00 6.04   ? 76  ILE   A CB  1 
ATOM   719  C CG1 . ILE   A 1 80  ? -11.369 -7.722  21.091 1.00 7.37   ? 76  ILE   A CG1 1 
ATOM   720  C CG2 . ILE   A 1 80  ? -13.732 -7.153  21.782 1.00 6.74   ? 76  ILE   A CG2 1 
ATOM   721  C CD1 . ILE   A 1 80  ? -11.685 -8.619  19.921 1.00 6.76   ? 76  ILE   A CD1 1 
ATOM   722  N N   . SER   A 1 81  ? -13.573 -5.969  24.907 1.00 6.78   ? 77  SER   A N   1 
ATOM   723  C CA  . SER   A 1 81  ? -14.624 -5.940  25.936 1.00 7.41   ? 77  SER   A CA  1 
ATOM   724  C C   . SER   A 1 81  ? -15.891 -6.606  25.444 1.00 6.86   ? 77  SER   A C   1 
ATOM   725  O O   . SER   A 1 81  ? -16.106 -6.699  24.227 1.00 6.73   ? 77  SER   A O   1 
ATOM   726  C CB  . SER   A 1 81  ? -14.892 -4.524  26.363 1.00 9.93   ? 77  SER   A CB  1 
ATOM   727  O OG  . SER   A 1 81  ? -15.499 -3.831  25.323 1.00 15.60  ? 77  SER   A OG  1 
ATOM   728  N N   A PRO   A 1 82  ? -16.777 -7.093  26.329 0.75 6.96   ? 78  PRO   A N   1 
ATOM   729  N N   B PRO   A 1 82  ? -16.711 -7.142  26.373 0.25 6.99   ? 78  PRO   A N   1 
ATOM   730  C CA  A PRO   A 1 82  ? -17.942 -7.830  25.812 0.75 7.08   ? 78  PRO   A CA  1 
ATOM   731  C CA  B PRO   A 1 82  ? -17.899 -7.917  26.001 0.25 7.28   ? 78  PRO   A CA  1 
ATOM   732  C C   A PRO   A 1 82  ? -18.853 -6.965  24.935 0.75 7.24   ? 78  PRO   A C   1 
ATOM   733  C C   B PRO   A 1 82  ? -18.794 -7.204  24.980 0.25 7.03   ? 78  PRO   A C   1 
ATOM   734  O O   A PRO   A 1 82  ? -19.499 -7.522  24.064 0.75 6.58   ? 78  PRO   A O   1 
ATOM   735  O O   B PRO   A 1 82  ? -19.322 -7.843  24.081 0.25 7.04   ? 78  PRO   A O   1 
ATOM   736  C CB  A PRO   A 1 82  ? -18.643 -8.365  27.063 0.75 8.75   ? 78  PRO   A CB  1 
ATOM   737  C CB  B PRO   A 1 82  ? -18.615 -8.071  27.351 0.25 7.40   ? 78  PRO   A CB  1 
ATOM   738  C CG  A PRO   A 1 82  ? -18.088 -7.508  28.171 0.75 9.31   ? 78  PRO   A CG  1 
ATOM   739  C CG  B PRO   A 1 82  ? -17.491 -8.094  28.360 0.25 7.25   ? 78  PRO   A CG  1 
ATOM   740  C CD  A PRO   A 1 82  ? -16.670 -7.144  27.803 0.75 8.85   ? 78  PRO   A CD  1 
ATOM   741  C CD  B PRO   A 1 82  ? -16.506 -7.076  27.835 0.25 7.38   ? 78  PRO   A CD  1 
ATOM   742  N N   A ASP   A 1 83  ? -18.959 -5.667  25.183 0.80 7.17   ? 79  ASP   A N   1 
ATOM   743  N N   B ASP   A 1 83  ? -18.954 -5.884  25.141 0.20 6.77   ? 79  ASP   A N   1 
ATOM   744  C CA  A ASP   A 1 83  ? -19.775 -4.793  24.294 0.80 8.47   ? 79  ASP   A CA  1 
ATOM   745  C CA  B ASP   A 1 83  ? -19.861 -5.046  24.301 0.20 6.58   ? 79  ASP   A CA  1 
ATOM   746  C C   A ASP   A 1 83  ? -19.291 -4.842  22.839 0.80 7.22   ? 79  ASP   A C   1 
ATOM   747  C C   B ASP   A 1 83  ? -19.318 -4.904  22.867 0.20 6.24   ? 79  ASP   A C   1 
ATOM   748  O O   A ASP   A 1 83  ? -20.078 -4.554  21.957 0.80 8.87   ? 79  ASP   A O   1 
ATOM   749  O O   B ASP   A 1 83  ? -20.125 -4.579  21.985 0.20 6.95   ? 79  ASP   A O   1 
ATOM   750  C CB  A ASP   A 1 83  ? -19.794 -3.379  24.873 0.80 9.86   ? 79  ASP   A CB  1 
ATOM   751  C CB  B ASP   A 1 83  ? -20.170 -3.689  24.964 0.20 6.68   ? 79  ASP   A CB  1 
ATOM   752  C CG  A ASP   A 1 83  ? -20.521 -3.213  26.185 0.80 15.79  ? 79  ASP   A CG  1 
ATOM   753  C CG  B ASP   A 1 83  ? -19.045 -3.086  25.791 0.20 7.62   ? 79  ASP   A CG  1 
ATOM   754  O OD1 A ASP   A 1 83  ? -21.529 -3.897  26.376 0.80 20.06  ? 79  ASP   A OD1 1 
ATOM   755  O OD1 B ASP   A 1 83  ? -17.885 -3.412  25.517 0.20 7.10   ? 79  ASP   A OD1 1 
ATOM   756  O OD2 A ASP   A 1 83  ? -20.066 -2.375  27.002 0.70 22.75  ? 79  ASP   A OD2 1 
ATOM   757  O OD2 B ASP   A 1 83  ? -19.352 -2.316  26.744 0.20 8.78   ? 79  ASP   A OD2 1 
ATOM   758  N N   . TYR   A 1 84  ? -18.018 -5.133  22.654 1.00 5.85   ? 80  TYR   A N   1 
ATOM   759  C CA  . TYR   A 1 84  ? -17.372 -5.185  21.319 1.00 6.04   ? 80  TYR   A CA  1 
ATOM   760  C C   . TYR   A 1 84  ? -17.145 -6.625  20.878 1.00 5.93   ? 80  TYR   A C   1 
ATOM   761  O O   . TYR   A 1 84  ? -16.498 -6.875  19.843 1.00 6.98   ? 80  TYR   A O   1 
ATOM   762  C CB  . TYR   A 1 84  ? -16.075 -4.376  21.362 1.00 6.45   ? 80  TYR   A CB  1 
ATOM   763  C CG  . TYR   A 1 84  ? -16.318 -2.891  21.253 1.00 6.94   ? 80  TYR   A CG  1 
ATOM   764  C CD1 . TYR   A 1 84  ? -16.794 -2.128  22.310 1.00 7.83   ? 80  TYR   A CD1 1 
ATOM   765  C CD2 . TYR   A 1 84  ? -16.078 -2.242  20.056 1.00 7.33   ? 80  TYR   A CD2 1 
ATOM   766  C CE1 . TYR   A 1 84  ? -17.049 -0.773  22.149 1.00 7.53   ? 80  TYR   A CE1 1 
ATOM   767  C CE2 . TYR   A 1 84  ? -16.342 -0.912  19.886 1.00 7.83   ? 80  TYR   A CE2 1 
ATOM   768  C CZ  . TYR   A 1 84  ? -16.816 -0.170  20.937 1.00 7.44   ? 80  TYR   A CZ  1 
ATOM   769  O OH  . TYR   A 1 84  ? -17.098 1.148   20.764 1.00 8.87   ? 80  TYR   A OH  1 
ATOM   770  N N   . ALA   A 1 85  ? -17.716 -7.566  21.638 1.00 6.20   ? 81  ALA   A N   1 
ATOM   771  C CA  . ALA   A 1 85  ? -17.615 -9.003  21.347 1.00 6.30   ? 81  ALA   A CA  1 
ATOM   772  C C   . ALA   A 1 85  ? -19.014 -9.599  21.317 1.00 5.89   ? 81  ALA   A C   1 
ATOM   773  O O   . ALA   A 1 85  ? -19.858 -9.110  20.534 1.00 6.56   ? 81  ALA   A O   1 
ATOM   774  C CB  . ALA   A 1 85  ? -16.626 -9.683  22.266 1.00 5.71   ? 81  ALA   A CB  1 
ATOM   775  N N   . TYR   A 1 86  ? -19.299 -10.588 22.169 1.00 5.62   ? 82  TYR   A N   1 
ATOM   776  C CA  . TYR   A 1 86  ? -20.584 -11.295 22.123 1.00 6.55   ? 82  TYR   A CA  1 
ATOM   777  C C   . TYR   A 1 86  ? -21.542 -10.883 23.242 1.00 6.03   ? 82  TYR   A C   1 
ATOM   778  O O   . TYR   A 1 86  ? -22.606 -11.485 23.305 1.00 6.95   ? 82  TYR   A O   1 
ATOM   779  C CB  . TYR   A 1 86  ? -20.341 -12.797 22.112 1.00 6.27   ? 82  TYR   A CB  1 
ATOM   780  C CG  . TYR   A 1 86  ? -19.711 -13.311 20.843 1.00 6.74   ? 82  TYR   A CG  1 
ATOM   781  C CD1 . TYR   A 1 86  ? -20.497 -13.528 19.734 1.00 7.13   ? 82  TYR   A CD1 1 
ATOM   782  C CD2 . TYR   A 1 86  ? -18.374 -13.601 20.730 1.00 7.48   ? 82  TYR   A CD2 1 
ATOM   783  C CE1 . TYR   A 1 86  ? -19.994 -14.028 18.549 1.00 7.39   ? 82  TYR   A CE1 1 
ATOM   784  C CE2 . TYR   A 1 86  ? -17.834 -14.081 19.543 1.00 8.04   ? 82  TYR   A CE2 1 
ATOM   785  C CZ  . TYR   A 1 86  ? -18.654 -14.325 18.457 1.00 7.49   ? 82  TYR   A CZ  1 
ATOM   786  O OH  . TYR   A 1 86  ? -18.162 -14.843 17.292 1.00 9.89   ? 82  TYR   A OH  1 
ATOM   787  N N   . GLY   A 1 87  ? -21.205 -9.879  24.039 1.00 6.46   ? 83  GLY   A N   1 
ATOM   788  C CA  . GLY   A 1 87  ? -22.216 -9.263  24.888 1.00 7.30   ? 83  GLY   A CA  1 
ATOM   789  C C   . GLY   A 1 87  ? -22.843 -10.223 25.879 1.00 7.29   ? 83  GLY   A C   1 
ATOM   790  O O   . GLY   A 1 87  ? -22.216 -11.186 26.358 1.00 7.71   ? 83  GLY   A O   1 
ATOM   791  N N   . ALA   A 1 88  ? -24.107 -9.960  26.161 1.00 8.42   ? 84  ALA   A N   1 
ATOM   792  C CA  . ALA   A 1 88  ? -24.853 -10.758 27.146 1.00 9.24   ? 84  ALA   A CA  1 
ATOM   793  C C   . ALA   A 1 88  ? -25.113 -12.179 26.638 1.00 9.48   ? 84  ALA   A C   1 
ATOM   794  O O   . ALA   A 1 88  ? -25.229 -13.108 27.454 1.00 12.12  ? 84  ALA   A O   1 
ATOM   795  C CB  . ALA   A 1 88  ? -26.153 -10.086 27.504 1.00 10.64  ? 84  ALA   A CB  1 
ATOM   796  N N   . THR   A 1 89  ? -25.334 -12.330 25.326 1.00 9.34   ? 85  THR   A N   1 
ATOM   797  C CA  . THR   A 1 89  ? -25.686 -13.644 24.765 1.00 10.26  ? 85  THR   A CA  1 
ATOM   798  C C   . THR   A 1 89  ? -24.479 -14.583 24.825 1.00 10.01  ? 85  THR   A C   1 
ATOM   799  O O   . THR   A 1 89  ? -24.670 -15.802 25.029 1.00 13.26  ? 85  THR   A O   1 
ATOM   800  C CB  . THR   A 1 89  ? -26.215 -13.468 23.341 1.00 12.42  ? 85  THR   A CB  1 
ATOM   801  O OG1 . THR   A 1 89  ? -27.356 -12.625 23.427 1.00 13.58  ? 85  THR   A OG1 1 
ATOM   802  C CG2 . THR   A 1 89  ? -26.609 -14.772 22.695 1.00 14.60  ? 85  THR   A CG2 1 
ATOM   803  N N   . GLY   A 1 90  ? -23.277 -14.067 24.602 1.00 8.69   ? 86  GLY   A N   1 
ATOM   804  C CA  . GLY   A 1 90  ? -22.145 -14.968 24.374 1.00 8.38   ? 86  GLY   A CA  1 
ATOM   805  C C   . GLY   A 1 90  ? -22.318 -15.725 23.063 1.00 8.15   ? 86  GLY   A C   1 
ATOM   806  O O   . GLY   A 1 90  ? -23.022 -15.291 22.167 1.00 9.02   ? 86  GLY   A O   1 
ATOM   807  N N   . HIS   A 1 91  ? -21.642 -16.851 22.964 1.00 9.46   ? 87  HIS   A N   1 
ATOM   808  C CA  . HIS   A 1 91  ? -21.753 -17.803 21.847 1.00 9.90   ? 87  HIS   A CA  1 
ATOM   809  C C   . HIS   A 1 91  ? -22.030 -19.136 22.514 1.00 10.33  ? 87  HIS   A C   1 
ATOM   810  O O   . HIS   A 1 91  ? -21.098 -19.693 23.096 1.00 9.41   ? 87  HIS   A O   1 
ATOM   811  C CB  . HIS   A 1 91  ? -20.528 -17.834 20.905 1.00 10.52  ? 87  HIS   A CB  1 
ATOM   812  C CG  . HIS   A 1 91  ? -20.723 -18.722 19.711 1.00 11.65  ? 87  HIS   A CG  1 
ATOM   813  N ND1 . HIS   A 1 91  ? -20.734 -18.303 18.374 1.00 16.64  ? 87  HIS   A ND1 1 
ATOM   814  C CD2 . HIS   A 1 91  ? -20.909 -20.054 19.675 1.00 12.21  ? 87  HIS   A CD2 1 
ATOM   815  C CE1 . HIS   A 1 91  ? -20.960 -19.361 17.632 1.00 16.43  ? 87  HIS   A CE1 1 
ATOM   816  N NE2 . HIS   A 1 91  ? -21.030 -20.430 18.375 1.00 15.32  ? 87  HIS   A NE2 1 
ATOM   817  N N   A PRO   A 1 92  ? -23.184 -19.795 22.193 0.75 13.41  ? 88  PRO   A N   1 
ATOM   818  N N   B PRO   A 1 92  ? -23.304 -19.382 22.865 0.25 8.27   ? 88  PRO   A N   1 
ATOM   819  C CA  A PRO   A 1 92  ? -23.665 -20.977 22.918 0.75 16.42  ? 88  PRO   A CA  1 
ATOM   820  C CA  B PRO   A 1 92  ? -23.663 -20.517 23.702 0.25 8.83   ? 88  PRO   A CA  1 
ATOM   821  C C   A PRO   A 1 92  ? -22.568 -21.982 23.271 0.75 16.60  ? 88  PRO   A C   1 
ATOM   822  C C   B PRO   A 1 92  ? -22.820 -21.782 23.466 0.25 11.45  ? 88  PRO   A C   1 
ATOM   823  O O   A PRO   A 1 92  ? -21.996 -22.459 22.300 0.75 15.69  ? 88  PRO   A O   1 
ATOM   824  O O   B PRO   A 1 92  ? -22.738 -22.263 22.388 0.25 9.91   ? 88  PRO   A O   1 
ATOM   825  C CB  A PRO   A 1 92  ? -24.675 -21.604 21.934 0.75 18.10  ? 88  PRO   A CB  1 
ATOM   826  C CB  B PRO   A 1 92  ? -25.082 -20.811 23.207 0.25 8.26   ? 88  PRO   A CB  1 
ATOM   827  C CG  A PRO   A 1 92  ? -25.247 -20.432 21.184 0.75 17.11  ? 88  PRO   A CG  1 
ATOM   828  C CG  B PRO   A 1 92  ? -25.660 -19.450 22.874 0.25 8.46   ? 88  PRO   A CG  1 
ATOM   829  C CD  A PRO   A 1 92  ? -24.124 -19.412 21.119 0.75 14.29  ? 88  PRO   A CD  1 
ATOM   830  C CD  B PRO   A 1 92  ? -24.478 -18.638 22.391 0.25 7.81   ? 88  PRO   A CD  1 
ATOM   831  N N   . GLY   A 1 93  ? -22.250 -22.244 24.568 1.00 14.90  ? 89  GLY   A N   1 
ATOM   832  C CA  . GLY   A 1 93  ? -21.396 -23.412 24.824 1.00 12.85  ? 89  GLY   A CA  1 
ATOM   833  C C   . GLY   A 1 93  ? -19.923 -23.144 24.586 1.00 12.12  ? 89  GLY   A C   1 
ATOM   834  O O   . GLY   A 1 93  ? -19.134 -24.018 24.908 1.00 12.79  ? 89  GLY   A O   1 
ATOM   835  N N   . ILE   A 1 94  ? -19.553 -21.995 24.020 1.00 10.85  ? 90  ILE   A N   1 
ATOM   836  C CA  . ILE   A 1 94  ? -18.161 -21.674 23.562 1.00 10.27  ? 90  ILE   A CA  1 
ATOM   837  C C   . ILE   A 1 94  ? -17.675 -20.412 24.284 1.00 9.15   ? 90  ILE   A C   1 
ATOM   838  O O   . ILE   A 1 94  ? -16.577 -20.417 24.852 1.00 12.10  ? 90  ILE   A O   1 
ATOM   839  C CB  . ILE   A 1 94  ? -18.081 -21.526 22.029 1.00 12.36  ? 90  ILE   A CB  1 
ATOM   840  C CG1 . ILE   A 1 94  ? -18.695 -22.730 21.298 1.00 14.87  ? 90  ILE   A CG1 1 
ATOM   841  C CG2 . ILE   A 1 94  ? -16.633 -21.281 21.609 1.00 11.76  ? 90  ILE   A CG2 1 
ATOM   842  C CD1 . ILE   A 1 94  ? -17.895 -24.004 21.402 1.00 16.66  ? 90  ILE   A CD1 1 
ATOM   843  N N   . ILE   A 1 95  ? -18.470 -19.354 24.280 1.00 8.46   ? 91  ILE   A N   1 
ATOM   844  C CA  . ILE   A 1 95  ? -18.101 -18.089 24.960 1.00 9.09   ? 91  ILE   A CA  1 
ATOM   845  C C   . ILE   A 1 95  ? -19.215 -17.746 25.925 1.00 8.12   ? 91  ILE   A C   1 
ATOM   846  O O   . ILE   A 1 95  ? -20.370 -17.620 25.533 1.00 8.85   ? 91  ILE   A O   1 
ATOM   847  C CB  . ILE   A 1 95  ? -17.852 -16.979 23.940 1.00 10.36  ? 91  ILE   A CB  1 
ATOM   848  C CG1 . ILE   A 1 95  ? -16.603 -17.331 23.110 1.00 12.92  ? 91  ILE   A CG1 1 
ATOM   849  C CG2 . ILE   A 1 95  ? -17.725 -15.625 24.650 1.00 9.79   ? 91  ILE   A CG2 1 
ATOM   850  C CD1 . ILE   A 1 95  ? -16.384 -16.385 21.995 1.00 14.74  ? 91  ILE   A CD1 1 
ATOM   851  N N   . PRO   A 1 96  ? -18.912 -17.561 27.227 1.00 9.74   ? 92  PRO   A N   1 
ATOM   852  C CA  . PRO   A 1 96  ? -19.940 -17.258 28.216 1.00 10.98  ? 92  PRO   A CA  1 
ATOM   853  C C   . PRO   A 1 96  ? -20.504 -15.851 28.037 1.00 9.26   ? 92  PRO   A C   1 
ATOM   854  O O   . PRO   A 1 96  ? -19.895 -14.997 27.422 1.00 8.90   ? 92  PRO   A O   1 
ATOM   855  C CB  . PRO   A 1 96  ? -19.233 -17.436 29.572 1.00 13.82  ? 92  PRO   A CB  1 
ATOM   856  C CG  . PRO   A 1 96  ? -17.779 -17.283 29.294 1.00 15.88  ? 92  PRO   A CG  1 
ATOM   857  C CD  . PRO   A 1 96  ? -17.576 -17.648 27.831 1.00 11.53  ? 92  PRO   A CD  1 
ATOM   858  N N   . PRO   A 1 97  ? -21.653 -15.559 28.659 1.00 9.88   ? 93  PRO   A N   1 
ATOM   859  C CA  . PRO   A 1 97  ? -22.156 -14.192 28.754 1.00 9.26   ? 93  PRO   A CA  1 
ATOM   860  C C   . PRO   A 1 97  ? -21.106 -13.238 29.327 1.00 8.43   ? 93  PRO   A C   1 
ATOM   861  O O   . PRO   A 1 97  ? -20.376 -13.575 30.231 1.00 10.14  ? 93  PRO   A O   1 
ATOM   862  C CB  . PRO   A 1 97  ? -23.370 -14.330 29.677 1.00 12.45  ? 93  PRO   A CB  1 
ATOM   863  C CG  . PRO   A 1 97  ? -23.836 -15.731 29.416 1.00 14.45  ? 93  PRO   A CG  1 
ATOM   864  C CD  . PRO   A 1 97  ? -22.560 -16.533 29.262 1.00 12.91  ? 93  PRO   A CD  1 
ATOM   865  N N   . HIS   A 1 98  ? -21.046 -12.023 28.805 1.00 8.24   ? 94  HIS   A N   1 
ATOM   866  C CA  . HIS   A 1 98  ? -20.296 -10.882 29.377 1.00 8.24   ? 94  HIS   A CA  1 
ATOM   867  C C   . HIS   A 1 98  ? -18.789 -11.141 29.437 1.00 7.49   ? 94  HIS   A C   1 
ATOM   868  O O   . HIS   A 1 98  ? -18.123 -10.620 30.315 1.00 10.81  ? 94  HIS   A O   1 
ATOM   869  C CB  . HIS   A 1 98  ? -20.872 -10.541 30.743 1.00 11.18  ? 94  HIS   A CB  1 
ATOM   870  C CG  . HIS   A 1 98  ? -22.335 -10.256 30.702 1.00 13.07  ? 94  HIS   A CG  1 
ATOM   871  N ND1 . HIS   A 1 98  ? -22.817 -9.110  30.123 1.00 15.59  ? 94  HIS   A ND1 1 
ATOM   872  C CD2 . HIS   A 1 98  ? -23.413 -10.955 31.138 1.00 16.41  ? 94  HIS   A CD2 1 
ATOM   873  C CE1 . HIS   A 1 98  ? -24.142 -9.105  30.210 1.00 14.50  ? 94  HIS   A CE1 1 
ATOM   874  N NE2 . HIS   A 1 98  ? -24.522 -10.220 30.833 1.00 18.47  ? 94  HIS   A NE2 1 
ATOM   875  N N   . ALA   A 1 99  ? -18.281 -11.851 28.449 1.00 7.46   ? 95  ALA   A N   1 
ATOM   876  C CA  . ALA   A 1 99  ? -16.874 -12.289 28.373 1.00 7.46   ? 95  ALA   A CA  1 
ATOM   877  C C   . ALA   A 1 99  ? -15.999 -11.243 27.675 1.00 6.62   ? 95  ALA   A C   1 
ATOM   878  O O   . ALA   A 1 99  ? -16.277 -10.830 26.554 1.00 7.22   ? 95  ALA   A O   1 
ATOM   879  C CB  . ALA   A 1 99  ? -16.755 -13.597 27.627 1.00 8.05   ? 95  ALA   A CB  1 
ATOM   880  N N   . THR   A 1 100 ? -14.886 -10.890 28.290 1.00 6.23   ? 96  THR   A N   1 
ATOM   881  C CA  . THR   A 1 100 ? -13.758 -10.226 27.659 1.00 6.31   ? 96  THR   A CA  1 
ATOM   882  C C   . THR   A 1 100 ? -12.969 -11.293 26.926 1.00 6.67   ? 96  THR   A C   1 
ATOM   883  O O   . THR   A 1 100 ? -12.696 -12.355 27.489 1.00 7.99   ? 96  THR   A O   1 
ATOM   884  C CB  . THR   A 1 100 ? -12.898 -9.521  28.706 1.00 7.75   ? 96  THR   A CB  1 
ATOM   885  O OG1 . THR   A 1 100 ? -13.686 -8.498  29.323 1.00 10.81  ? 96  THR   A OG1 1 
ATOM   886  C CG2 . THR   A 1 100 ? -11.654 -8.922  28.124 1.00 8.56   ? 96  THR   A CG2 1 
ATOM   887  N N   . LEU   A 1 101 ? -12.617 -11.017 25.660 1.00 6.31   ? 97  LEU   A N   1 
ATOM   888  C CA  . LEU   A 1 101 ? -11.902 -12.007 24.817 1.00 5.90   ? 97  LEU   A CA  1 
ATOM   889  C C   . LEU   A 1 101 ? -10.495 -11.509 24.539 1.00 5.57   ? 97  LEU   A C   1 
ATOM   890  O O   . LEU   A 1 101 ? -10.274 -10.325 24.387 1.00 7.16   ? 97  LEU   A O   1 
ATOM   891  C CB  . LEU   A 1 101 ? -12.643 -12.218 23.508 1.00 6.25   ? 97  LEU   A CB  1 
ATOM   892  C CG  . LEU   A 1 101 ? -14.126 -12.530 23.629 1.00 7.17   ? 97  LEU   A CG  1 
ATOM   893  C CD1 . LEU   A 1 101 ? -14.678 -12.814 22.241 1.00 7.73   ? 97  LEU   A CD1 1 
ATOM   894  C CD2 . LEU   A 1 101 ? -14.397 -13.712 24.550 1.00 7.05   ? 97  LEU   A CD2 1 
ATOM   895  N N   . VAL   A 1 102 ? -9.583  -12.446 24.411 1.00 5.85   ? 98  VAL   A N   1 
ATOM   896  C CA  . VAL   A 1 102 ? -8.190  -12.164 24.028 1.00 5.96   ? 98  VAL   A CA  1 
ATOM   897  C C   . VAL   A 1 102 ? -7.889  -12.998 22.785 1.00 6.35   ? 98  VAL   A C   1 
ATOM   898  O O   . VAL   A 1 102 ? -8.025  -14.202 22.788 1.00 9.38   ? 98  VAL   A O   1 
ATOM   899  C CB  . VAL   A 1 102 ? -7.219  -12.499 25.168 1.00 7.64   ? 98  VAL   A CB  1 
ATOM   900  C CG1 . VAL   A 1 102 ? -5.782  -12.217 24.740 1.00 10.51  ? 98  VAL   A CG1 1 
ATOM   901  C CG2 . VAL   A 1 102 ? -7.585  -11.796 26.473 1.00 9.17   ? 98  VAL   A CG2 1 
ATOM   902  N N   . PHE   A 1 103 ? -7.474  -12.309 21.754 1.00 5.59   ? 99  PHE   A N   1 
ATOM   903  C CA  . PHE   A 1 103 ? -7.060  -12.995 20.516 1.00 6.00   ? 99  PHE   A CA  1 
ATOM   904  C C   . PHE   A 1 103 ? -5.593  -12.724 20.224 1.00 6.48   ? 99  PHE   A C   1 
ATOM   905  O O   . PHE   A 1 103 ? -5.122  -11.611 20.299 1.00 9.04   ? 99  PHE   A O   1 
ATOM   906  C CB  . PHE   A 1 103 ? -7.861  -12.550 19.294 1.00 6.20   ? 99  PHE   A CB  1 
ATOM   907  C CG  . PHE   A 1 103 ? -9.293  -12.959 19.326 1.00 6.08   ? 99  PHE   A CG  1 
ATOM   908  C CD1 . PHE   A 1 103 ? -10.266 -12.191 19.955 1.00 6.64   ? 99  PHE   A CD1 1 
ATOM   909  C CD2 . PHE   A 1 103 ? -9.703  -14.105 18.647 1.00 6.19   ? 99  PHE   A CD2 1 
ATOM   910  C CE1 . PHE   A 1 103 ? -11.599 -12.566 19.921 1.00 6.63   ? 99  PHE   A CE1 1 
ATOM   911  C CE2 . PHE   A 1 103 ? -11.031 -14.463 18.612 1.00 6.48   ? 99  PHE   A CE2 1 
ATOM   912  C CZ  . PHE   A 1 103 ? -11.975 -13.687 19.215 1.00 6.46   ? 99  PHE   A CZ  1 
ATOM   913  N N   . ASP   A 1 104 ? -4.914  -13.768 19.788 1.00 5.33   ? 100 ASP   A N   1 
ATOM   914  C CA  . ASP   A 1 104 ? -3.577  -13.688 19.162 1.00 5.68   ? 100 ASP   A CA  1 
ATOM   915  C C   . ASP   A 1 104 ? -3.840  -13.765 17.666 1.00 5.39   ? 100 ASP   A C   1 
ATOM   916  O O   . ASP   A 1 104 ? -4.266  -14.808 17.187 1.00 6.95   ? 100 ASP   A O   1 
ATOM   917  C CB  . ASP   A 1 104 ? -2.699  -14.811 19.685 1.00 7.32   ? 100 ASP   A CB  1 
ATOM   918  C CG  . ASP   A 1 104 ? -1.293  -14.886 19.149 1.00 9.75   ? 100 ASP   A CG  1 
ATOM   919  O OD1 . ASP   A 1 104 ? -1.022  -14.325 18.077 1.00 11.93  ? 100 ASP   A OD1 1 
ATOM   920  O OD2 . ASP   A 1 104 ? -0.484  -15.580 19.806 1.00 16.44  ? 100 ASP   A OD2 1 
ATOM   921  N N   A VAL   A 1 105 ? -3.649  -12.645 16.976 0.50 5.51   ? 101 VAL   A N   1 
ATOM   922  N N   B VAL   A 1 105 ? -3.594  -12.669 16.972 0.50 5.72   ? 101 VAL   A N   1 
ATOM   923  C CA  A VAL   A 1 105 ? -3.996  -12.511 15.538 0.50 5.96   ? 101 VAL   A CA  1 
ATOM   924  C CA  B VAL   A 1 105 ? -3.985  -12.552 15.550 0.50 6.45   ? 101 VAL   A CA  1 
ATOM   925  C C   A VAL   A 1 105 ? -2.753  -12.149 14.735 0.50 5.82   ? 101 VAL   A C   1 
ATOM   926  C C   B VAL   A 1 105 ? -2.774  -12.134 14.724 0.50 6.05   ? 101 VAL   A C   1 
ATOM   927  O O   A VAL   A 1 105 ? -2.005  -11.257 15.114 0.50 6.83   ? 101 VAL   A O   1 
ATOM   928  O O   B VAL   A 1 105 ? -2.042  -11.229 15.103 0.50 6.94   ? 101 VAL   A O   1 
ATOM   929  C CB  A VAL   A 1 105 ? -5.081  -11.451 15.265 0.50 6.71   ? 101 VAL   A CB  1 
ATOM   930  C CB  B VAL   A 1 105 ? -5.151  -11.567 15.352 0.50 7.95   ? 101 VAL   A CB  1 
ATOM   931  C CG1 A VAL   A 1 105 ? -5.463  -11.439 13.771 0.50 6.87   ? 101 VAL   A CG1 1 
ATOM   932  C CG1 B VAL   A 1 105 ? -6.438  -12.072 15.947 0.50 9.55   ? 101 VAL   A CG1 1 
ATOM   933  C CG2 A VAL   A 1 105 ? -6.296  -11.626 16.152 0.50 6.93   ? 101 VAL   A CG2 1 
ATOM   934  C CG2 B VAL   A 1 105 ? -4.836  -10.190 15.890 0.50 9.67   ? 101 VAL   A CG2 1 
ATOM   935  N N   . GLU   A 1 106 ? -2.637  -12.767 13.566 1.00 6.48   ? 102 GLU   A N   1 
ATOM   936  C CA  . GLU   A 1 106 ? -1.582  -12.415 12.597 1.00 6.82   ? 102 GLU   A CA  1 
ATOM   937  C C   . GLU   A 1 106 ? -2.270  -12.038 11.281 1.00 6.10   ? 102 GLU   A C   1 
ATOM   938  O O   . GLU   A 1 106 ? -2.989  -12.867 10.721 1.00 6.46   ? 102 GLU   A O   1 
ATOM   939  C CB  . GLU   A 1 106 ? -0.570  -13.537 12.381 1.00 8.79   ? 102 GLU   A CB  1 
ATOM   940  C CG  . GLU   A 1 106 ? 0.599   -13.118 11.500 1.00 11.42  ? 102 GLU   A CG  1 
ATOM   941  C CD  . GLU   A 1 106 ? 1.642   -14.203 11.336 1.00 17.40  ? 102 GLU   A CD  1 
ATOM   942  O OE1 . GLU   A 1 106 ? 2.539   -14.003 10.470 1.00 20.05  ? 102 GLU   A OE1 1 
ATOM   943  O OE2 . GLU   A 1 106 ? 1.512   -15.243 12.024 1.00 24.27  ? 102 GLU   A OE2 1 
ATOM   944  N N   . LEU   A 1 107 ? -1.988  -10.834 10.789 1.00 6.82   ? 103 LEU   A N   1 
ATOM   945  C CA  . LEU   A 1 107 ? -2.542  -10.363 9.505  1.00 7.64   ? 103 LEU   A CA  1 
ATOM   946  C C   . LEU   A 1 107 ? -1.592  -10.828 8.403  1.00 7.43   ? 103 LEU   A C   1 
ATOM   947  O O   . LEU   A 1 107 ? -0.483  -10.301 8.266  1.00 8.49   ? 103 LEU   A O   1 
ATOM   948  C CB  . LEU   A 1 107 ? -2.730  -8.857  9.499  1.00 7.38   ? 103 LEU   A CB  1 
ATOM   949  C CG  . LEU   A 1 107 ? -3.263  -8.275  8.195  1.00 8.03   ? 103 LEU   A CG  1 
ATOM   950  C CD1 . LEU   A 1 107 ? -4.599  -8.878  7.799  1.00 8.43   ? 103 LEU   A CD1 1 
ATOM   951  C CD2 . LEU   A 1 107 ? -3.371  -6.766  8.321  1.00 9.41   ? 103 LEU   A CD2 1 
ATOM   952  N N   . LEU   A 1 108 ? -1.979  -11.861 7.694  1.00 7.47   ? 104 LEU   A N   1 
ATOM   953  C CA  . LEU   A 1 108 ? -1.099  -12.563 6.761  1.00 8.17   ? 104 LEU   A CA  1 
ATOM   954  C C   . LEU   A 1 108 ? -1.079  -11.873 5.388  1.00 8.55   ? 104 LEU   A C   1 
ATOM   955  O O   . LEU   A 1 108 ? -0.040  -11.886 4.700  1.00 9.98   ? 104 LEU   A O   1 
ATOM   956  C CB  . LEU   A 1 108 ? -1.624  -13.985 6.561  1.00 8.04   ? 104 LEU   A CB  1 
ATOM   957  C CG  . LEU   A 1 108 ? -1.638  -14.862 7.804  1.00 9.10   ? 104 LEU   A CG  1 
ATOM   958  C CD1 . LEU   A 1 108 ? -2.401  -16.144 7.552  1.00 11.00  ? 104 LEU   A CD1 1 
ATOM   959  C CD2 . LEU   A 1 108 ? -0.231  -15.128 8.323  1.00 13.22  ? 104 LEU   A CD2 1 
ATOM   960  N N   . LYS   A 1 109 ? -2.212  -11.371 4.921  1.00 8.05   ? 105 LYS   A N   1 
ATOM   961  C CA  . LYS   A 1 109 ? -2.386  -11.001 3.489  1.00 8.72   ? 105 LYS   A CA  1 
ATOM   962  C C   . LYS   A 1 109 ? -3.661  -10.180 3.359  1.00 8.14   ? 105 LYS   A C   1 
ATOM   963  O O   . LYS   A 1 109 ? -4.621  -10.371 4.155  1.00 9.28   ? 105 LYS   A O   1 
ATOM   964  C CB  . LYS   A 1 109 ? -2.491  -12.269 2.615  1.00 10.11  ? 105 LYS   A CB  1 
ATOM   965  C CG  . LYS   A 1 109 ? -2.500  -12.102 1.105  1.00 12.65  ? 105 LYS   A CG  1 
ATOM   966  C CD  . LYS   A 1 109 ? -2.523  -13.457 0.391  1.00 14.30  ? 105 LYS   A CD  1 
ATOM   967  C CE  . LYS   A 1 109 ? -2.669  -13.437 -1.128 1.00 20.33  ? 105 LYS   A CE  1 
ATOM   968  N NZ  . LYS   A 1 109 ? -1.760  -12.484 -1.780 1.00 25.23  ? 105 LYS   A NZ  1 
ATOM   969  N N   . LEU   A 1 110 ? -3.680  -9.293  2.373  1.00 10.30  ? 106 LEU   A N   1 
ATOM   970  C CA  . LEU   A 1 110 ? -4.904  -8.568  1.965  1.00 11.02  ? 106 LEU   A CA  1 
ATOM   971  C C   . LEU   A 1 110 ? -5.198  -9.007  0.531  1.00 13.27  ? 106 LEU   A C   1 
ATOM   972  O O   . LEU   A 1 110 ? -4.257  -8.965  -0.321 1.00 16.61  ? 106 LEU   A O   1 
ATOM   973  C CB  . LEU   A 1 110 ? -4.680  -7.065  1.989  1.00 12.33  ? 106 LEU   A CB  1 
ATOM   974  C CG  . LEU   A 1 110 ? -4.437  -6.497  3.365  1.00 13.27  ? 106 LEU   A CG  1 
ATOM   975  C CD1 . LEU   A 1 110 ? -4.168  -5.001  3.267  1.00 16.42  ? 106 LEU   A CD1 1 
ATOM   976  C CD2 . LEU   A 1 110 ? -5.600  -6.745  4.306  1.00 16.07  ? 106 LEU   A CD2 1 
ATOM   977  N N   . GLU   A 1 111 ? -6.446  -9.369  0.271  1.00 15.48  ? 107 GLU   A N   1 
ATOM   978  C CA  . GLU   A 1 111 ? -6.927  -9.832  -1.065 1.00 20.39  ? 107 GLU   A CA  1 
ATOM   979  C C   . GLU   A 1 111 ? -8.141  -9.001  -1.492 1.00 24.10  ? 107 GLU   A C   1 
ATOM   980  O O   . GLU   A 1 111 ? -8.719  -8.221  -0.705 1.00 24.33  ? 107 GLU   A O   1 
ATOM   981  C CB  . GLU   A 1 111 ? -7.354  -11.310 -1.022 1.00 25.30  ? 107 GLU   A CB  1 
ATOM   982  C CG  . GLU   A 1 111 ? -6.204  -12.283 -0.707 1.00 28.00  ? 107 GLU   A CG  1 
ATOM   983  C CD  . GLU   A 1 111 ? -6.530  -13.777 -0.665 1.00 32.09  ? 107 GLU   A CD  1 
ATOM   984  O OE1 . GLU   A 1 111 ? -7.700  -14.173 -0.328 1.00 28.47  ? 107 GLU   A OE1 1 
ATOM   985  O OE2 . GLU   A 1 111 ? -5.584  -14.560 -0.940 1.00 39.99  ? 107 GLU   A OE2 1 
ATOM   986  O OXT . GLU   A 1 111 ? -8.528  -9.186  -2.650 1.00 35.58  ? 107 GLU   A OXT 1 
HETATM 987  C C1  . A1L7S B 2 .   ? -15.057 -14.129 15.729 1.00 7.80   ? 201 A1L7S A C1  1 
HETATM 988  C C3  . A1L7S B 2 .   ? -16.310 -14.123 14.981 1.00 10.98  ? 201 A1L7S A C3  1 
HETATM 989  C C12 . A1L7S B 2 .   ? -21.586 -11.177 14.140 1.00 11.23  ? 201 A1L7S A C12 1 
HETATM 990  C C13 . A1L7S B 2 .   ? -14.038 -13.141 15.206 1.00 8.65   ? 201 A1L7S A C13 1 
HETATM 991  C C14 . A1L7S B 2 .   ? -13.473 -13.662 13.871 1.00 8.14   ? 201 A1L7S A C14 1 
HETATM 992  C C15 . A1L7S B 2 .   ? -12.811 -15.008 14.086 1.00 7.80   ? 201 A1L7S A C15 1 
HETATM 993  C C16 . A1L7S B 2 .   ? -13.824 -16.031 14.587 1.00 8.39   ? 201 A1L7S A C16 1 
HETATM 994  C C17 . A1L7S B 2 .   ? -21.204 -10.181 13.260 1.00 10.75  ? 201 A1L7S A C17 1 
HETATM 995  C C18 . A1L7S B 2 .   ? -20.967 -8.893  13.710 1.00 10.40  ? 201 A1L7S A C18 1 
HETATM 996  C C19 . A1L7S B 2 .   ? -21.113 -8.613  15.075 1.00 9.74   ? 201 A1L7S A C19 1 
HETATM 997  C C25 . A1L7S B 2 .   ? -15.825 -17.332 17.291 1.00 7.71   ? 201 A1L7S A C25 1 
HETATM 998  C C26 . A1L7S B 2 .   ? -15.965 -17.994 18.675 1.00 10.66  ? 201 A1L7S A C26 1 
HETATM 999  C C27 . A1L7S B 2 .   ? -17.230 -18.837 18.696 1.00 12.44  ? 201 A1L7S A C27 1 
HETATM 1000 C C28 . A1L7S B 2 .   ? -17.094 -19.933 17.653 1.00 12.75  ? 201 A1L7S A C28 1 
HETATM 1001 C C29 . A1L7S B 2 .   ? -17.009 -19.334 16.248 1.00 10.89  ? 201 A1L7S A C29 1 
HETATM 1002 O O24 . A1L7S B 2 .   ? -14.653 -15.283 18.306 1.00 7.91   ? 201 A1L7S A O24 1 
HETATM 1003 S S22 . A1L7S B 2 .   ? -14.489 -16.276 17.231 1.00 7.35   ? 201 A1L7S A S22 1 
HETATM 1004 O O23 . A1L7S B 2 .   ? -13.258 -17.014 17.337 1.00 9.38   ? 201 A1L7S A O23 1 
HETATM 1005 C C30 . A1L7S B 2 .   ? -15.801 -18.396 16.170 1.00 8.58   ? 201 A1L7S A C30 1 
HETATM 1006 N N2  . A1L7S B 2 .   ? -14.460 -15.459 15.799 1.00 8.27   ? 201 A1L7S A N2  1 
HETATM 1007 O O6  . A1L7S B 2 .   ? -16.839 -15.297 14.567 1.00 13.21  ? 201 A1L7S A O6  1 
HETATM 1008 N N7  . A1L7S B 2 .   ? -18.008 -15.043 13.967 1.00 17.18  ? 201 A1L7S A N7  1 
HETATM 1009 C C8  . A1L7S B 2 .   ? -18.160 -13.709 14.009 1.00 15.37  ? 201 A1L7S A C8  1 
HETATM 1010 N N5  . A1L7S B 2 .   ? -17.111 -13.137 14.651 1.00 12.55  ? 201 A1L7S A N5  1 
HETATM 1011 C C9  . A1L7S B 2 .   ? -19.327 -12.937 13.460 1.00 13.34  ? 201 A1L7S A C9  1 
HETATM 1012 C C10 . A1L7S B 2 .   ? -20.648 -13.474 14.014 1.00 13.52  ? 201 A1L7S A C10 1 
HETATM 1013 C C11 . A1L7S B 2 .   ? -21.811 -12.581 13.608 1.00 13.29  ? 201 A1L7S A C11 1 
HETATM 1014 C C21 . A1L7S B 2 .   ? -21.734 -10.886 15.500 1.00 11.26  ? 201 A1L7S A C21 1 
HETATM 1015 C C20 . A1L7S B 2 .   ? -21.513 -9.594  15.948 1.00 9.65   ? 201 A1L7S A C20 1 
HETATM 1016 O O33 . A1L7S B 2 .   ? -21.647 -9.250  17.270 1.00 10.37  ? 201 A1L7S A O33 1 
HETATM 1017 C C34 . A1L7S B 2 .   ? -22.117 -10.225 18.195 1.00 11.86  ? 201 A1L7S A C34 1 
HETATM 1018 O O31 . A1L7S B 2 .   ? -20.891 -7.371  15.582 1.00 9.99   ? 201 A1L7S A O31 1 
HETATM 1019 C C32 . A1L7S B 2 .   ? -20.371 -6.321  14.787 1.00 10.68  ? 201 A1L7S A C32 1 
HETATM 1020 C C1  . GOL   C 3 .   ? -23.878 -6.585  19.952 1.00 11.00  ? 202 GOL   A C1  1 
HETATM 1021 O O1  . GOL   C 3 .   ? -23.863 -5.701  18.830 1.00 12.45  ? 202 GOL   A O1  1 
HETATM 1022 C C2  . GOL   C 3 .   ? -22.712 -6.398  20.893 1.00 10.70  ? 202 GOL   A C2  1 
HETATM 1023 O O2  . GOL   C 3 .   ? -22.841 -5.176  21.610 1.00 12.13  ? 202 GOL   A O2  1 
HETATM 1024 C C3  . GOL   C 3 .   ? -22.664 -7.466  21.937 1.00 11.63  ? 202 GOL   A C3  1 
HETATM 1025 O O3  . GOL   C 3 .   ? -22.448 -8.719  21.341 1.00 10.57  ? 202 GOL   A O3  1 
HETATM 1026 C C1  . GOL   D 3 .   ? -11.870 -22.600 8.916  1.00 16.12  ? 203 GOL   A C1  1 
HETATM 1027 O O1  . GOL   D 3 .   ? -12.752 -22.050 7.946  1.00 23.86  ? 203 GOL   A O1  1 
HETATM 1028 C C2  . GOL   D 3 .   ? -10.629 -21.761 9.037  1.00 12.45  ? 203 GOL   A C2  1 
HETATM 1029 O O2  . GOL   D 3 .   ? -9.768  -22.412 9.945  1.00 10.15  ? 203 GOL   A O2  1 
HETATM 1030 C C3  . GOL   D 3 .   ? -10.902 -20.353 9.498  1.00 12.70  ? 203 GOL   A C3  1 
HETATM 1031 O O3  . GOL   D 3 .   ? -11.431 -20.353 10.829 1.00 13.69  ? 203 GOL   A O3  1 
HETATM 1032 O O   . HOH   E 4 .   ? -18.036 -4.009  27.380 0.80 26.86  ? 301 HOH   A O   1 
HETATM 1033 O O   . HOH   E 4 .   ? -21.506 -2.198  11.337 0.80 21.11  ? 302 HOH   A O   1 
HETATM 1034 O O   . HOH   E 4 .   ? -23.044 -4.729  5.478  1.00 40.30  ? 303 HOH   A O   1 
HETATM 1035 O O   . HOH   E 4 .   ? 0.035   -16.636 13.684 1.00 33.34  ? 304 HOH   A O   1 
HETATM 1036 O O   . HOH   E 4 .   ? -2.611  -10.128 -1.962 1.00 32.32  ? 305 HOH   A O   1 
HETATM 1037 O O   . HOH   E 4 .   ? -11.447 -1.555  26.030 1.00 45.19  ? 306 HOH   A O   1 
HETATM 1038 O O   . HOH   E 4 .   ? -23.350 -4.308  24.584 0.20 112.33 ? 307 HOH   A O   1 
HETATM 1039 O O   A HOH   E 4 .   ? 0.064   -19.137 13.004 0.70 19.83  ? 308 HOH   A O   1 
HETATM 1040 O O   B HOH   E 4 .   ? 0.352   -18.666 11.931 0.30 22.39  ? 308 HOH   A O   1 
HETATM 1041 O O   . HOH   E 4 .   ? -16.948 -6.828  8.358  1.00 13.64  ? 309 HOH   A O   1 
HETATM 1042 O O   . HOH   E 4 .   ? -20.918 -10.462 4.120  1.00 27.04  ? 310 HOH   A O   1 
HETATM 1043 O O   . HOH   E 4 .   ? -21.323 -7.111  29.329 1.00 34.75  ? 311 HOH   A O   1 
HETATM 1044 O O   . HOH   E 4 .   ? -2.356  1.511   12.931 1.00 36.11  ? 312 HOH   A O   1 
HETATM 1045 O O   . HOH   E 4 .   ? -14.057 -20.413 10.655 1.00 29.37  ? 313 HOH   A O   1 
HETATM 1046 O O   . HOH   E 4 .   ? -7.660  0.261   19.964 1.00 32.44  ? 314 HOH   A O   1 
HETATM 1047 O O   . HOH   E 4 .   ? -4.339  -6.518  24.077 1.00 10.40  ? 315 HOH   A O   1 
HETATM 1048 O O   . HOH   E 4 .   ? -29.872 -13.188 24.052 1.00 44.77  ? 316 HOH   A O   1 
HETATM 1049 O O   A HOH   E 4 .   ? -12.976 -14.171 29.414 0.90 12.03  ? 317 HOH   A O   1 
HETATM 1050 O O   B HOH   E 4 .   ? -14.053 -14.377 30.179 0.10 22.52  ? 317 HOH   A O   1 
HETATM 1051 O O   A HOH   E 4 .   ? 1.313   -1.806  19.064 0.50 12.31  ? 318 HOH   A O   1 
HETATM 1052 O O   B HOH   E 4 .   ? 1.469   -2.112  19.850 0.50 29.51  ? 318 HOH   A O   1 
HETATM 1053 O O   . HOH   E 4 .   ? -1.538  -17.982 20.280 1.00 33.67  ? 319 HOH   A O   1 
HETATM 1054 O O   . HOH   E 4 .   ? -26.047 -10.300 23.315 1.00 13.28  ? 320 HOH   A O   1 
HETATM 1055 O O   . HOH   E 4 .   ? -8.716  -19.839 4.160  1.00 29.63  ? 321 HOH   A O   1 
HETATM 1056 O O   . HOH   E 4 .   ? -24.476 -10.467 21.120 1.00 10.03  ? 322 HOH   A O   1 
HETATM 1057 O O   . HOH   E 4 .   ? -17.881 -6.114  11.720 1.00 16.65  ? 323 HOH   A O   1 
HETATM 1058 O O   . HOH   E 4 .   ? 2.415   -12.386 8.321  1.00 37.82  ? 324 HOH   A O   1 
HETATM 1059 O O   . HOH   E 4 .   ? -14.223 -11.723 1.294  1.00 30.48  ? 325 HOH   A O   1 
HETATM 1060 O O   . HOH   E 4 .   ? -6.537  0.265   7.970  1.00 13.67  ? 326 HOH   A O   1 
HETATM 1061 O O   . HOH   E 4 .   ? -15.010 -1.087  8.164  1.00 19.64  ? 327 HOH   A O   1 
HETATM 1062 O O   . HOH   E 4 .   ? -27.094 -13.741 29.320 1.00 33.42  ? 328 HOH   A O   1 
HETATM 1063 O O   . HOH   E 4 .   ? -20.096 -16.470 16.275 1.00 16.97  ? 329 HOH   A O   1 
HETATM 1064 O O   A HOH   E 4 .   ? 7.836   -0.368  5.714  0.50 11.90  ? 330 HOH   A O   1 
HETATM 1065 O O   B HOH   E 4 .   ? 7.749   -0.422  5.858  0.50 14.79  ? 330 HOH   A O   1 
HETATM 1066 O O   . HOH   E 4 .   ? -15.839 -9.107  30.888 1.00 16.32  ? 331 HOH   A O   1 
HETATM 1067 O O   . HOH   E 4 .   ? -26.905 -16.815 26.227 1.00 37.60  ? 332 HOH   A O   1 
HETATM 1068 O O   . HOH   E 4 .   ? -16.665 2.254   18.303 1.00 9.09   ? 333 HOH   A O   1 
HETATM 1069 O O   . HOH   E 4 .   ? 3.095   2.603   10.339 1.00 14.10  ? 334 HOH   A O   1 
HETATM 1070 O O   . HOH   E 4 .   ? -13.266 -5.793  29.237 1.00 23.80  ? 335 HOH   A O   1 
HETATM 1071 O O   . HOH   E 4 .   ? 1.287   -1.830  12.006 1.00 10.60  ? 336 HOH   A O   1 
HETATM 1072 O O   . HOH   E 4 .   ? 4.724   -7.468  5.715  1.00 18.20  ? 337 HOH   A O   1 
HETATM 1073 O O   . HOH   E 4 .   ? -15.786 -12.483 3.337  1.00 27.31  ? 338 HOH   A O   1 
HETATM 1074 O O   . HOH   E 4 .   ? -19.999 -12.742 25.844 1.00 7.87   ? 339 HOH   A O   1 
HETATM 1075 O O   . HOH   E 4 .   ? -17.430 -14.191 9.205  1.00 29.76  ? 340 HOH   A O   1 
HETATM 1076 O O   A HOH   E 4 .   ? -14.227 -12.062 30.935 0.90 14.00  ? 341 HOH   A O   1 
HETATM 1077 O O   B HOH   E 4 .   ? -15.370 -15.263 29.625 0.10 37.48  ? 341 HOH   A O   1 
HETATM 1078 O O   A HOH   E 4 .   ? -25.287 -7.703  25.068 0.70 12.07  ? 342 HOH   A O   1 
HETATM 1079 O O   B HOH   E 4 .   ? -25.023 -6.821  25.787 0.30 11.65  ? 342 HOH   A O   1 
HETATM 1080 O O   . HOH   E 4 .   ? -10.743 1.809   16.824 1.00 21.48  ? 343 HOH   A O   1 
HETATM 1081 O O   A HOH   E 4 .   ? 2.360   -11.747 6.098  0.50 21.66  ? 344 HOH   A O   1 
HETATM 1082 O O   B HOH   E 4 .   ? 2.340   -12.646 5.613  0.50 32.11  ? 344 HOH   A O   1 
HETATM 1083 O O   . HOH   E 4 .   ? -2.141  0.824   3.212  1.00 25.64  ? 345 HOH   A O   1 
HETATM 1084 O O   . HOH   E 4 .   ? -23.032 -18.097 26.247 1.00 20.94  ? 346 HOH   A O   1 
HETATM 1085 O O   . HOH   E 4 .   ? -21.854 -6.629  26.906 1.00 25.50  ? 347 HOH   A O   1 
HETATM 1086 O O   . HOH   E 4 .   ? -8.568  -26.049 28.638 1.00 52.26  ? 348 HOH   A O   1 
HETATM 1087 O O   . HOH   E 4 .   ? -2.013  -22.307 7.612  1.00 30.00  ? 349 HOH   A O   1 
HETATM 1088 O O   . HOH   E 4 .   ? -14.779 -16.647 5.859  1.00 47.45  ? 350 HOH   A O   1 
HETATM 1089 O O   . HOH   E 4 .   ? 3.551   -3.098  13.003 1.00 8.55   ? 351 HOH   A O   1 
HETATM 1090 O O   . HOH   E 4 .   ? 3.676   4.009   6.088  1.00 17.34  ? 352 HOH   A O   1 
HETATM 1091 O O   A HOH   E 4 .   ? 1.075   -11.191 2.190  0.50 23.21  ? 353 HOH   A O   1 
HETATM 1092 O O   B HOH   E 4 .   ? 1.226   -10.124 0.930  0.50 30.38  ? 353 HOH   A O   1 
HETATM 1093 O O   . HOH   E 4 .   ? -20.841 -15.559 32.208 1.00 30.79  ? 354 HOH   A O   1 
HETATM 1094 O O   A HOH   E 4 .   ? -9.929  -25.209 25.847 0.50 17.05  ? 355 HOH   A O   1 
HETATM 1095 O O   B HOH   E 4 .   ? -9.283  -26.120 25.487 0.50 27.53  ? 355 HOH   A O   1 
HETATM 1096 O O   A HOH   E 4 .   ? -21.280 -4.895  17.934 0.50 7.34   ? 356 HOH   A O   1 
HETATM 1097 O O   B HOH   E 4 .   ? -20.196 -4.685  19.147 0.50 12.66  ? 356 HOH   A O   1 
HETATM 1098 O O   . HOH   E 4 .   ? -23.926 -13.129 20.537 1.00 12.38  ? 357 HOH   A O   1 
HETATM 1099 O O   . HOH   E 4 .   ? -0.960  -1.508  15.000 1.00 18.86  ? 358 HOH   A O   1 
HETATM 1100 O O   A HOH   E 4 .   ? -9.451  0.878   13.598 0.50 16.28  ? 359 HOH   A O   1 
HETATM 1101 O O   B HOH   E 4 .   ? -9.777  0.826   14.582 0.50 22.55  ? 359 HOH   A O   1 
HETATM 1102 O O   . HOH   E 4 .   ? -17.887 -11.765 24.378 1.00 6.86   ? 360 HOH   A O   1 
HETATM 1103 O O   . HOH   E 4 .   ? -15.972 -13.778 6.972  1.00 22.60  ? 361 HOH   A O   1 
HETATM 1104 O O   . HOH   E 4 .   ? -17.247 -0.554  25.896 1.00 32.37  ? 362 HOH   A O   1 
HETATM 1105 O O   . HOH   E 4 .   ? 5.610   -13.451 16.057 1.00 20.13  ? 363 HOH   A O   1 
HETATM 1106 O O   . HOH   E 4 .   ? -14.203 -9.560  33.096 1.00 42.17  ? 364 HOH   A O   1 
HETATM 1107 O O   A HOH   E 4 .   ? -24.858 -5.388  23.650 0.80 11.55  ? 365 HOH   A O   1 
HETATM 1108 O O   B HOH   E 4 .   ? -24.226 -5.692  24.945 0.20 9.78   ? 365 HOH   A O   1 
HETATM 1109 O O   A HOH   E 4 .   ? -27.221 -9.230  30.952 0.50 23.38  ? 366 HOH   A O   1 
HETATM 1110 O O   B HOH   E 4 .   ? -26.696 -7.120  29.187 0.50 31.85  ? 366 HOH   A O   1 
HETATM 1111 O O   . HOH   E 4 .   ? -19.640 -7.286  18.318 1.00 7.97   ? 367 HOH   A O   1 
HETATM 1112 O O   . HOH   E 4 .   ? -4.305  -1.787  1.410  1.00 25.74  ? 368 HOH   A O   1 
HETATM 1113 O O   . HOH   E 4 .   ? 4.878   -6.304  3.353  1.00 28.24  ? 369 HOH   A O   1 
HETATM 1114 O O   . HOH   E 4 .   ? -11.309 -19.782 5.646  1.00 49.34  ? 370 HOH   A O   1 
HETATM 1115 O O   . HOH   E 4 .   ? -18.781 -3.808  9.401  1.00 17.65  ? 371 HOH   A O   1 
HETATM 1116 O O   A HOH   E 4 .   ? -19.123 -3.548  12.702 0.50 8.95   ? 372 HOH   A O   1 
HETATM 1117 O O   B HOH   E 4 .   ? -21.000 -3.065  12.845 0.50 26.58  ? 372 HOH   A O   1 
HETATM 1118 O O   . HOH   E 4 .   ? 5.779   -16.915 19.441 1.00 38.57  ? 373 HOH   A O   1 
HETATM 1119 O O   . HOH   E 4 .   ? -12.607 -17.952 6.524  1.00 16.96  ? 374 HOH   A O   1 
HETATM 1120 O O   . HOH   E 4 .   ? -2.331  -0.293  17.190 1.00 32.98  ? 375 HOH   A O   1 
HETATM 1121 O O   A HOH   E 4 .   ? -5.355  -8.842  28.073 0.50 18.23  ? 376 HOH   A O   1 
HETATM 1122 O O   B HOH   E 4 .   ? -4.989  -8.203  27.811 0.50 28.98  ? 376 HOH   A O   1 
HETATM 1123 O O   . HOH   E 4 .   ? -11.414 0.706   21.632 1.00 34.15  ? 377 HOH   A O   1 
HETATM 1124 O O   A HOH   E 4 .   ? -10.396 -4.009  25.934 0.50 14.52  ? 378 HOH   A O   1 
HETATM 1125 O O   B HOH   E 4 .   ? -10.822 -4.689  27.643 0.50 44.96  ? 378 HOH   A O   1 
HETATM 1126 O O   . HOH   E 4 .   ? -18.580 -10.773 33.212 1.00 40.58  ? 379 HOH   A O   1 
HETATM 1127 O O   . HOH   E 4 .   ? -1.058  -8.652  1.172  1.00 15.93  ? 380 HOH   A O   1 
HETATM 1128 O O   . HOH   E 4 .   ? -27.159 -11.532 31.077 1.00 33.69  ? 381 HOH   A O   1 
HETATM 1129 O O   A HOH   E 4 .   ? -4.938  0.274   20.144 0.20 34.03  ? 382 HOH   A O   1 
HETATM 1130 O O   B HOH   E 4 .   ? -4.746  -0.329  21.691 0.80 24.11  ? 382 HOH   A O   1 
HETATM 1131 O O   A HOH   E 4 .   ? -13.441 1.474   20.375 0.50 21.84  ? 383 HOH   A O   1 
HETATM 1132 O O   B HOH   E 4 .   ? -13.493 2.190   19.481 0.50 19.88  ? 383 HOH   A O   1 
HETATM 1133 O O   . HOH   E 4 .   ? -12.078 -25.064 22.573 1.00 21.04  ? 384 HOH   A O   1 
HETATM 1134 O O   A HOH   E 4 .   ? -14.458 -19.237 12.668 0.50 22.18  ? 385 HOH   A O   1 
HETATM 1135 O O   B HOH   E 4 .   ? -16.657 -18.107 12.364 0.50 31.81  ? 385 HOH   A O   1 
HETATM 1136 O O   . HOH   E 4 .   ? -11.754 -16.087 31.911 1.00 28.53  ? 386 HOH   A O   1 
HETATM 1137 O O   A HOH   E 4 .   ? 4.631   -15.628 15.006 0.50 23.99  ? 387 HOH   A O   1 
HETATM 1138 O O   B HOH   E 4 .   ? 4.561   -15.282 13.770 0.50 29.18  ? 387 HOH   A O   1 
HETATM 1139 O O   . HOH   E 4 .   ? -17.118 -0.395  9.980  1.00 21.10  ? 388 HOH   A O   1 
HETATM 1140 O O   . HOH   E 4 .   ? 2.414   -1.128  16.419 1.00 20.32  ? 389 HOH   A O   1 
HETATM 1141 O O   A HOH   E 4 .   ? -5.589  -14.831 27.872 0.50 21.83  ? 390 HOH   A O   1 
HETATM 1142 O O   B HOH   E 4 .   ? -3.940  -15.677 28.711 0.50 32.38  ? 390 HOH   A O   1 
HETATM 1143 O O   . HOH   E 4 .   ? -10.857 2.719   4.127  1.00 23.27  ? 391 HOH   A O   1 
HETATM 1144 O O   . HOH   E 4 .   ? 0.822   -1.179  22.686 1.00 42.61  ? 392 HOH   A O   1 
HETATM 1145 O O   . HOH   E 4 .   ? -19.948 -18.107 14.111 1.00 37.72  ? 393 HOH   A O   1 
HETATM 1146 O O   . HOH   E 4 .   ? 6.832   -7.051  7.264  1.00 31.29  ? 394 HOH   A O   1 
HETATM 1147 O O   . HOH   E 4 .   ? -18.911 -4.612  30.013 1.00 54.17  ? 395 HOH   A O   1 
HETATM 1148 O O   . HOH   E 4 .   ? -5.763  2.356   6.614  1.00 43.02  ? 396 HOH   A O   1 
HETATM 1149 O O   . HOH   E 4 .   ? -30.019 -9.840  24.618 0.80 67.16  ? 397 HOH   A O   1 
HETATM 1150 O O   A HOH   E 4 .   ? -21.161 -1.531  15.365 0.50 39.57  ? 398 HOH   A O   1 
HETATM 1151 O O   B HOH   E 4 .   ? -21.968 -0.749  15.310 0.50 23.54  ? 398 HOH   A O   1 
HETATM 1152 O O   A HOH   E 4 .   ? 3.393   0.484   11.998 0.80 8.76   ? 399 HOH   A O   1 
HETATM 1153 O O   B HOH   E 4 .   ? 3.392   0.880   13.304 0.20 8.22   ? 399 HOH   A O   1 
HETATM 1154 O O   A HOH   E 4 .   ? -15.980 -13.657 32.174 0.50 34.90  ? 400 HOH   A O   1 
HETATM 1155 O O   B HOH   E 4 .   ? -17.747 -13.951 31.184 0.50 19.28  ? 400 HOH   A O   1 
HETATM 1156 O O   . HOH   E 4 .   ? -17.612 -16.619 10.046 1.00 56.14  ? 401 HOH   A O   1 
HETATM 1157 O O   . HOH   E 4 .   ? -23.194 -14.118 33.470 1.00 34.69  ? 402 HOH   A O   1 
HETATM 1158 O O   A HOH   E 4 .   ? -20.634 -2.440  17.193 0.50 5.63   ? 403 HOH   A O   1 
HETATM 1159 O O   B HOH   E 4 .   ? -20.832 -2.283  17.101 0.50 26.85  ? 403 HOH   A O   1 
HETATM 1160 O O   . HOH   E 4 .   ? -16.854 -6.524  31.558 1.00 27.91  ? 404 HOH   A O   1 
HETATM 1161 O O   . HOH   E 4 .   ? 7.870   -13.395 17.721 1.00 22.27  ? 405 HOH   A O   1 
HETATM 1162 O O   . HOH   E 4 .   ? 1.776   5.703   6.595  1.00 49.33  ? 406 HOH   A O   1 
HETATM 1163 O O   A HOH   E 4 .   ? -15.520 -4.597  30.344 0.50 35.18  ? 407 HOH   A O   1 
HETATM 1164 O O   B HOH   E 4 .   ? -16.448 -3.520  29.753 0.50 32.53  ? 407 HOH   A O   1 
HETATM 1165 O O   . HOH   E 4 .   ? -8.374  3.396   5.390  1.00 29.67  ? 408 HOH   A O   1 
HETATM 1166 O O   . HOH   E 4 .   ? -20.243 -8.296  33.675 1.00 28.06  ? 409 HOH   A O   1 
HETATM 1167 O O   . HOH   E 4 .   ? 0.790   4.381   10.678 1.00 29.03  ? 410 HOH   A O   1 
HETATM 1168 O O   . HOH   E 4 .   ? -27.455 -7.992  23.216 1.00 14.78  ? 411 HOH   A O   1 
HETATM 1169 O O   A HOH   E 4 .   ? -22.543 -1.986  13.389 0.50 15.89  ? 412 HOH   A O   1 
HETATM 1170 O O   B HOH   E 4 .   ? -21.563 -1.088  13.600 0.50 10.96  ? 412 HOH   A O   1 
HETATM 1171 O O   . HOH   E 4 .   ? 6.661   -19.225 17.419 1.00 39.39  ? 413 HOH   A O   1 
HETATM 1172 O O   . HOH   E 4 .   ? -2.273  3.491   10.999 1.00 44.74  ? 414 HOH   A O   1 
HETATM 1173 O O   . HOH   E 4 .   ? -32.040 -14.472 22.904 1.00 51.79  ? 415 HOH   A O   1 
HETATM 1174 O O   . HOH   E 4 .   ? -27.694 -17.648 20.732 1.00 27.65  ? 416 HOH   A O   1 
HETATM 1175 O O   A HOH   E 4 .   ? 8.855   -15.574 16.345 0.50 19.59  ? 417 HOH   A O   1 
HETATM 1176 O O   B HOH   E 4 .   ? 8.046   -16.118 18.134 0.50 34.44  ? 417 HOH   A O   1 
HETATM 1177 O O   A HOH   E 4 .   ? 1.823   1.525   13.586 0.50 21.22  ? 418 HOH   A O   1 
HETATM 1178 O O   B HOH   E 4 .   ? 0.974   0.639   13.238 0.50 20.53  ? 418 HOH   A O   1 
HETATM 1179 O O   A HOH   E 4 .   ? 0.102   2.362   20.370 0.70 31.48  ? 419 HOH   A O   1 
HETATM 1180 O O   B HOH   E 4 .   ? -0.302  3.754   21.244 0.30 23.32  ? 419 HOH   A O   1 
HETATM 1181 O O   . HOH   E 4 .   ? -3.255  3.516   8.381  1.00 60.97  ? 420 HOH   A 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   A GLY   A 5   ? 0.2497 0.3553 0.2673 0.0138  0.0161  -0.0186 1   GLY   A N   
2    N N   B GLY   A 5   ? 0.1557 0.0943 0.3623 -0.0103 0.0781  -0.0352 1   GLY   A N   
3    C CA  A GLY   A 5   ? 0.1512 0.2245 0.2755 0.0283  0.0209  -0.0327 1   GLY   A CA  
4    C CA  B GLY   A 5   ? 0.1349 0.1420 0.2918 -0.0047 0.0364  -0.0304 1   GLY   A CA  
5    C C   A GLY   A 5   ? 0.1891 0.1263 0.1660 0.0056  0.0281  0.0115  1   GLY   A C   
6    C C   B GLY   A 5   ? 0.1656 0.0933 0.2023 0.0018  0.0160  0.0069  1   GLY   A C   
7    O O   A GLY   A 5   ? 0.1716 0.1260 0.1463 0.0073  0.0226  0.0140  1   GLY   A O   
8    O O   B GLY   A 5   ? 0.1669 0.1013 0.1854 -0.0034 0.0108  0.0256  1   GLY   A O   
9    N N   . VAL   A 6   ? 0.1605 0.1070 0.2029 -0.0122 -0.0070 0.0371  2   VAL   A N   
10   C CA  . VAL   A 6   ? 0.1601 0.1276 0.0895 -0.0145 -0.0136 0.0116  2   VAL   A CA  
11   C C   . VAL   A 6   ? 0.1595 0.0903 0.0816 0.0016  -0.0002 -0.0382 2   VAL   A C   
12   O O   . VAL   A 6   ? 0.1784 0.1059 0.1800 -0.0088 0.0086  0.0014  2   VAL   A O   
13   C CB  . VAL   A 6   ? 0.1540 0.1610 0.1039 -0.0147 -0.0229 -0.0042 2   VAL   A CB  
14   C CG1 . VAL   A 6   ? 0.2339 0.2184 0.1266 -0.0424 -0.0282 0.0358  2   VAL   A CG1 
15   C CG2 . VAL   A 6   ? 0.1755 0.1670 0.0850 -0.0042 -0.0018 -0.0005 2   VAL   A CG2 
16   N N   A GLN   A 7   ? 0.1383 0.1017 0.1085 -0.0060 0.0021  -0.0238 3   GLN   A N   
17   N N   B GLN   A 7   ? 0.1437 0.1059 0.0767 -0.0012 -0.0013 -0.0420 3   GLN   A N   
18   C CA  A GLN   A 7   ? 0.1431 0.1298 0.1379 -0.0179 0.0044  -0.0347 3   GLN   A CA  
19   C CA  B GLN   A 7   ? 0.1433 0.1175 0.0877 -0.0032 -0.0015 -0.0473 3   GLN   A CA  
20   C C   A GLN   A 7   ? 0.1352 0.1099 0.1269 -0.0032 -0.0132 -0.0164 3   GLN   A C   
21   C C   B GLN   A 7   ? 0.1406 0.1129 0.1037 0.0014  0.0056  -0.0382 3   GLN   A C   
22   O O   A GLN   A 7   ? 0.1638 0.0997 0.1337 0.0025  0.0247  -0.0128 3   GLN   A O   
23   O O   B GLN   A 7   ? 0.1523 0.1110 0.1072 0.0029  0.0167  -0.0411 3   GLN   A O   
24   C CB  A GLN   A 7   ? 0.1818 0.1907 0.1357 -0.0540 -0.0121 -0.0425 3   GLN   A CB  
25   C CB  B GLN   A 7   ? 0.1254 0.1225 0.0860 -0.0046 -0.0015 -0.0658 3   GLN   A CB  
26   C CG  A GLN   A 7   ? 0.2710 0.3206 0.1641 -0.0121 0.0170  -0.0696 3   GLN   A CG  
27   C CG  B GLN   A 7   ? 0.1270 0.1423 0.0737 -0.0038 -0.0174 -0.0761 3   GLN   A CG  
28   C CD  A GLN   A 7   ? 0.3526 0.4084 0.1549 -0.0611 -0.0073 -0.0705 3   GLN   A CD  
29   C CD  B GLN   A 7   ? 0.1352 0.1605 0.0680 -0.0017 -0.0112 -0.0754 3   GLN   A CD  
30   O OE1 A GLN   A 7   ? 0.4936 0.5359 0.2036 -0.1356 -0.0019 0.0341  3   GLN   A OE1 
31   O OE1 B GLN   A 7   ? 0.1833 0.1913 0.1447 -0.0291 -0.0180 -0.0282 3   GLN   A OE1 
32   N NE2 A GLN   A 7   ? 0.4412 0.4825 0.2282 -0.0226 -0.1931 -0.0391 3   GLN   A NE2 
33   N NE2 B GLN   A 7   ? 0.1576 0.1671 0.0857 -0.0058 -0.0387 -0.1041 3   GLN   A NE2 
34   N N   . VAL   A 8   ? 0.1487 0.1007 0.1268 -0.0103 0.0038  -0.0301 4   VAL   A N   
35   C CA  . VAL   A 8   ? 0.1341 0.1071 0.1362 -0.0029 0.0134  -0.0100 4   VAL   A CA  
36   C C   . VAL   A 8   ? 0.1277 0.1161 0.1192 -0.0218 0.0202  -0.0363 4   VAL   A C   
37   O O   . VAL   A 8   ? 0.1635 0.1289 0.2385 -0.0479 0.0309  -0.0447 4   VAL   A O   
38   C CB  . VAL   A 8   ? 0.1815 0.1130 0.1428 -0.0066 0.0182  0.0035  4   VAL   A CB  
39   C CG1 . VAL   A 8   ? 0.1904 0.1596 0.0920 -0.0139 0.0334  0.0228  4   VAL   A CG1 
40   C CG2 . VAL   A 8   ? 0.2038 0.1253 0.1557 -0.0040 -0.0201 0.0403  4   VAL   A CG2 
41   N N   A GLU   A 9   ? 0.1266 0.1106 0.0543 -0.0316 0.0265  -0.0491 5   GLU   A N   
42   N N   B GLU   A 9   ? 0.1180 0.1362 0.0662 -0.0239 -0.0030 -0.0358 5   GLU   A N   
43   C CA  A GLU   A 9   ? 0.1370 0.1114 0.0846 -0.0382 0.0072  -0.0495 5   GLU   A CA  
44   C CA  B GLU   A 9   ? 0.1201 0.1474 0.0557 -0.0106 -0.0012 -0.0331 5   GLU   A CA  
45   C C   A GLU   A 9   ? 0.1254 0.1213 0.0703 -0.0329 -0.0022 -0.0434 5   GLU   A C   
46   C C   B GLU   A 9   ? 0.1150 0.1511 0.0529 -0.0226 -0.0010 -0.0370 5   GLU   A C   
47   O O   A GLU   A 9   ? 0.1083 0.1082 0.0363 -0.0246 -0.0098 -0.0274 5   GLU   A O   
48   O O   B GLU   A 9   ? 0.1095 0.1373 0.0764 -0.0137 -0.0075 -0.0379 5   GLU   A O   
49   C CB  A GLU   A 9   ? 0.1509 0.2015 0.0705 -0.0434 0.0044  -0.0532 5   GLU   A CB  
50   C CB  B GLU   A 9   ? 0.0931 0.1853 0.0233 -0.0010 -0.0072 -0.0436 5   GLU   A CB  
51   C CG  A GLU   A 9   ? 0.1858 0.2268 0.0942 -0.0497 0.0401  -0.0569 5   GLU   A CG  
52   C CG  B GLU   A 9   ? 0.0902 0.1918 0.0258 0.0084  0.0003  -0.0283 5   GLU   A CG  
53   C CD  A GLU   A 9   ? 0.2220 0.2887 0.0979 -0.0706 0.0270  -0.0434 5   GLU   A CD  
54   C CD  B GLU   A 9   ? 0.1198 0.2301 0.0478 0.0258  0.0111  -0.0011 5   GLU   A CD  
55   O OE1 A GLU   A 9   ? 0.2105 0.3404 0.0778 -0.0951 -0.0173 -0.0181 5   GLU   A OE1 
56   O OE1 B GLU   A 9   ? 0.1610 0.2402 0.0293 0.0587  0.0263  0.0304  5   GLU   A OE1 
57   O OE2 A GLU   A 9   ? 0.2820 0.3208 0.1715 -0.1004 -0.0022 -0.1005 5   GLU   A OE2 
58   O OE2 B GLU   A 9   ? 0.1595 0.3037 0.0319 0.0249  0.0268  0.0368  5   GLU   A OE2 
59   N N   . THR   A 10  ? 0.1088 0.1144 0.0428 -0.0206 -0.0130 -0.0378 6   THR   A N   
60   C CA  . THR   A 10  ? 0.1273 0.0980 0.0192 -0.0233 -0.0125 -0.0294 6   THR   A CA  
61   C C   . THR   A 10  ? 0.1166 0.1155 0.0219 -0.0214 -0.0101 -0.0104 6   THR   A C   
62   O O   . THR   A 10  ? 0.1385 0.1208 0.0250 -0.0206 -0.0193 -0.0182 6   THR   A O   
63   C CB  . THR   A 10  ? 0.1550 0.1090 0.0180 -0.0194 0.0004  -0.0113 6   THR   A CB  
64   O OG1 . THR   A 10  ? 0.1770 0.1119 0.0359 -0.0164 -0.0053 -0.0014 6   THR   A OG1 
65   C CG2 . THR   A 10  ? 0.1595 0.1320 0.0372 -0.0289 0.0156  -0.0196 6   THR   A CG2 
66   N N   . ILE   A 11  ? 0.1082 0.1150 0.0081 -0.0142 -0.0116 -0.0053 7   ILE   A N   
67   C CA  . ILE   A 11  ? 0.1095 0.1338 0.0094 -0.0015 -0.0178 -0.0027 7   ILE   A CA  
68   C C   . ILE   A 11  ? 0.1165 0.1104 0.0095 0.0043  -0.0112 -0.0093 7   ILE   A C   
69   O O   . ILE   A 11  ? 0.1258 0.1522 0.0275 0.0044  -0.0152 0.0083  7   ILE   A O   
70   C CB  . ILE   A 11  ? 0.1338 0.1361 0.0201 -0.0048 -0.0002 -0.0005 7   ILE   A CB  
71   C CG1 . ILE   A 11  ? 0.1447 0.1382 0.0301 0.0003  0.0085  0.0167  7   ILE   A CG1 
72   C CG2 . ILE   A 11  ? 0.1230 0.1530 0.0459 -0.0033 0.0011  0.0099  7   ILE   A CG2 
73   C CD1 . ILE   A 11  ? 0.1654 0.1529 0.0914 -0.0137 0.0263  0.0188  7   ILE   A CD1 
74   N N   . SER   A 12  ? 0.0949 0.1267 0.0169 0.0028  -0.0071 0.0140  8   SER   A N   
75   C CA  . SER   A 12  ? 0.1168 0.1424 0.0302 -0.0027 0.0089  0.0142  8   SER   A CA  
76   C C   . SER   A 12  ? 0.1002 0.1074 0.0191 -0.0134 0.0074  -0.0082 8   SER   A C   
77   O O   . SER   A 12  ? 0.1003 0.1252 0.0322 -0.0274 -0.0016 0.0132  8   SER   A O   
78   C CB  . SER   A 12  ? 0.1435 0.1493 0.0567 0.0027  0.0314  0.0213  8   SER   A CB  
79   O OG  . SER   A 12  ? 0.1454 0.1764 0.1097 0.0137  0.0168  -0.0248 8   SER   A OG  
80   N N   A PRO   A 13  ? 0.0956 0.1037 0.0571 -0.0131 -0.0079 0.0025  9   PRO   A N   
81   N N   B PRO   A 13  ? 0.0977 0.1072 0.0135 -0.0127 0.0051  -0.0055 9   PRO   A N   
82   C CA  A PRO   A 13  ? 0.1230 0.1100 0.0331 -0.0112 -0.0028 0.0047  9   PRO   A CA  
83   C CA  B PRO   A 13  ? 0.1015 0.1023 0.0159 -0.0151 0.0074  -0.0052 9   PRO   A CA  
84   C C   A PRO   A 13  ? 0.1226 0.1107 0.0158 -0.0143 0.0287  0.0117  9   PRO   A C   
85   C C   B PRO   A 13  ? 0.1182 0.1065 0.0159 -0.0179 0.0097  -0.0082 9   PRO   A C   
86   O O   A PRO   A 13  ? 0.1680 0.1266 0.0553 -0.0089 0.0205  -0.0261 9   PRO   A O   
87   O O   B PRO   A 13  ? 0.1144 0.1075 0.0265 -0.0145 0.0036  -0.0112 9   PRO   A O   
88   C CB  A PRO   A 13  ? 0.1353 0.1336 0.0790 -0.0292 0.0023  -0.0060 9   PRO   A CB  
89   C CB  B PRO   A 13  ? 0.0955 0.1016 0.0094 -0.0123 0.0095  -0.0079 9   PRO   A CB  
90   C CG  A PRO   A 13  ? 0.1476 0.1549 0.1697 -0.0361 -0.0058 0.0467  9   PRO   A CG  
91   C CG  B PRO   A 13  ? 0.0845 0.0964 0.0091 -0.0150 0.0112  -0.0094 9   PRO   A CG  
92   C CD  A PRO   A 13  ? 0.0912 0.1059 0.1072 -0.0148 -0.0109 0.0062  9   PRO   A CD  
93   C CD  B PRO   A 13  ? 0.0933 0.0976 0.0131 -0.0138 0.0096  -0.0061 9   PRO   A CD  
94   N N   . GLY   A 14  ? 0.1313 0.0982 0.0370 -0.0169 0.0047  -0.0015 10  GLY   A N   
95   C CA  . GLY   A 14  ? 0.1319 0.1089 0.0406 -0.0236 -0.0051 -0.0104 10  GLY   A CA  
96   C C   . GLY   A 14  ? 0.1190 0.1053 0.0390 -0.0174 -0.0093 -0.0132 10  GLY   A C   
97   O O   . GLY   A 14  ? 0.1160 0.1058 0.0320 -0.0236 -0.0111 0.0018  10  GLY   A O   
98   N N   . ASP   A 15  ? 0.1345 0.1087 0.0386 -0.0193 -0.0056 -0.0073 11  ASP   A N   
99   C CA  . ASP   A 15  ? 0.1385 0.1296 0.0272 -0.0235 -0.0045 0.0100  11  ASP   A CA  
100  C C   . ASP   A 15  ? 0.1099 0.1242 0.0445 -0.0292 -0.0019 0.0171  11  ASP   A C   
101  O O   . ASP   A 15  ? 0.1203 0.1363 0.0535 -0.0335 0.0151  0.0164  11  ASP   A O   
102  C CB  . ASP   A 15  ? 0.1596 0.1397 0.0279 -0.0110 0.0007  0.0038  11  ASP   A CB  
103  C CG  . ASP   A 15  ? 0.1521 0.1498 0.0364 -0.0125 0.0039  0.0061  11  ASP   A CG  
104  O OD1 . ASP   A 15  ? 0.1613 0.1285 0.0565 -0.0109 0.0050  0.0013  11  ASP   A OD1 
105  O OD2 . ASP   A 15  ? 0.1886 0.2515 0.0389 0.0048  0.0069  -0.0166 11  ASP   A OD2 
106  N N   . GLY   A 16  ? 0.1221 0.1220 0.0393 -0.0293 0.0016  0.0210  12  GLY   A N   
107  C CA  . GLY   A 16  ? 0.1462 0.1307 0.0656 -0.0326 0.0071  0.0078  12  GLY   A CA  
108  C C   . GLY   A 16  ? 0.1736 0.1187 0.0837 -0.0108 -0.0035 0.0082  12  GLY   A C   
109  O O   . GLY   A 16  ? 0.1860 0.1169 0.1166 -0.0117 -0.0102 0.0177  12  GLY   A O   
110  N N   A ARG   A 17  ? 0.1628 0.1283 0.0781 -0.0284 -0.0051 0.0200  13  ARG   A N   
111  N N   B ARG   A 17  ? 0.1823 0.1198 0.0525 -0.0163 -0.0035 0.0334  13  ARG   A N   
112  C CA  A ARG   A 17  ? 0.1827 0.1709 0.0990 -0.0415 -0.0213 0.0466  13  ARG   A CA  
113  C CA  B ARG   A 17  ? 0.2128 0.1538 0.0572 -0.0252 -0.0199 0.0417  13  ARG   A CA  
114  C C   A ARG   A 17  ? 0.1829 0.1723 0.0548 -0.0226 -0.0159 0.0269  13  ARG   A C   
115  C C   B ARG   A 17  ? 0.2013 0.1668 0.0407 -0.0068 -0.0168 0.0312  13  ARG   A C   
116  O O   A ARG   A 17  ? 0.2313 0.1852 0.1110 -0.0022 -0.0276 0.0552  13  ARG   A O   
117  O O   B ARG   A 17  ? 0.2514 0.2114 0.0651 0.0115  -0.0461 0.0636  13  ARG   A O   
118  C CB  A ARG   A 17  ? 0.2151 0.2772 0.1230 -0.0963 0.0076  0.0824  13  ARG   A CB  
119  C CB  B ARG   A 17  ? 0.2736 0.2175 0.0472 -0.0429 0.0122  0.0887  13  ARG   A CB  
120  C CG  A ARG   A 17  ? 0.2666 0.3072 0.1154 -0.0747 -0.0321 0.0795  13  ARG   A CG  
121  C CG  B ARG   A 17  ? 0.2927 0.2732 0.0658 -0.0479 -0.0219 0.0600  13  ARG   A CG  
122  C CD  A ARG   A 17  ? 0.3059 0.4106 0.2060 -0.0682 0.0326  0.0146  13  ARG   A CD  
123  C CD  B ARG   A 17  ? 0.3176 0.3378 0.1200 -0.0612 0.0234  0.0152  13  ARG   A CD  
124  N NE  A ARG   A 17  ? 0.3223 0.5032 0.2677 -0.0410 0.0594  0.0010  13  ARG   A NE  
125  N NE  B ARG   A 17  ? 0.2843 0.3137 0.2677 -0.0872 0.0696  0.0547  13  ARG   A NE  
126  C CZ  A ARG   A 17  ? 0.2801 0.4264 0.4056 -0.1114 -0.0743 0.0647  13  ARG   A CZ  
127  C CZ  B ARG   A 17  ? 0.4041 0.3303 0.2539 -0.0500 0.0450  0.0632  13  ARG   A CZ  
128  N NH1 A ARG   A 17  ? 0.3233 0.4670 0.3888 -0.0637 0.0368  0.0952  13  ARG   A NH1 
129  N NH1 B ARG   A 17  ? 0.4546 0.3635 0.1662 -0.0144 0.0057  0.0015  13  ARG   A NH1 
130  N NH2 A ARG   A 17  ? 0.3625 0.4557 0.4196 -0.1054 -0.1167 0.0847  13  ARG   A NH2 
131  N NH2 B ARG   A 17  ? 0.4204 0.4410 0.2529 -0.0232 -0.0284 0.0226  13  ARG   A NH2 
132  N N   . THR   A 18  ? 0.1617 0.1648 0.0443 -0.0167 -0.0019 0.0240  14  THR   A N   
133  C CA  . THR   A 18  ? 0.1494 0.1814 0.0367 -0.0191 0.0056  0.0325  14  THR   A CA  
134  C C   . THR   A 18  ? 0.1310 0.1773 0.0407 -0.0163 -0.0029 0.0245  14  THR   A C   
135  O O   . THR   A 18  ? 0.1721 0.1808 0.0463 0.0021  0.0102  0.0312  14  THR   A O   
136  C CB  . THR   A 18  ? 0.1634 0.2079 0.0609 -0.0272 0.0132  -0.0023 14  THR   A CB  
137  O OG1 . THR   A 18  ? 0.1793 0.2281 0.0554 -0.0342 0.0178  0.0079  14  THR   A OG1 
138  C CG2 . THR   A 18  ? 0.1749 0.2299 0.0389 -0.0151 0.0140  -0.0066 14  THR   A CG2 
139  N N   . PHE   A 19  ? 0.1441 0.1671 0.0755 -0.0076 0.0034  0.0144  15  PHE   A N   
140  C CA  . PHE   A 19  ? 0.1256 0.1642 0.0801 0.0072  0.0004  -0.0035 15  PHE   A CA  
141  C C   . PHE   A 19  ? 0.1288 0.1662 0.0845 0.0196  -0.0136 0.0081  15  PHE   A C   
142  O O   . PHE   A 19  ? 0.1783 0.2103 0.0949 0.0341  -0.0204 0.0300  15  PHE   A O   
143  C CB  . PHE   A 19  ? 0.1593 0.1713 0.1172 0.0148  0.0054  -0.0238 15  PHE   A CB  
144  C CG  . PHE   A 19  ? 0.1878 0.1425 0.1159 -0.0077 -0.0127 -0.0154 15  PHE   A CG  
145  C CD1 . PHE   A 19  ? 0.1706 0.1370 0.1197 -0.0207 -0.0104 -0.0082 15  PHE   A CD1 
146  C CD2 . PHE   A 19  ? 0.2047 0.1220 0.1623 -0.0026 0.0070  -0.0066 15  PHE   A CD2 
147  C CE1 . PHE   A 19  ? 0.1921 0.1492 0.1169 -0.0213 -0.0169 -0.0101 15  PHE   A CE1 
148  C CE2 . PHE   A 19  ? 0.1616 0.1432 0.1900 -0.0290 0.0242  -0.0043 15  PHE   A CE2 
149  C CZ  . PHE   A 19  ? 0.1670 0.1402 0.1773 -0.0120 -0.0038 -0.0250 15  PHE   A CZ  
150  N N   . PRO   A 20  ? 0.1437 0.1788 0.0593 0.0065  -0.0151 -0.0032 16  PRO   A N   
151  C CA  . PRO   A 20  ? 0.1471 0.2124 0.0782 0.0040  -0.0217 -0.0145 16  PRO   A CA  
152  C C   . PRO   A 20  ? 0.1586 0.2207 0.1016 0.0187  -0.0154 0.0058  16  PRO   A C   
153  O O   . PRO   A 20  ? 0.1845 0.2056 0.1379 0.0630  -0.0260 0.0019  16  PRO   A O   
154  C CB  . PRO   A 20  ? 0.1951 0.1807 0.2022 -0.0140 -0.0232 0.0333  16  PRO   A CB  
155  C CG  . PRO   A 20  ? 0.2219 0.2407 0.0410 -0.0494 0.0062  -0.0345 16  PRO   A CG  
156  C CD  . PRO   A 20  ? 0.1461 0.1910 0.0636 0.0059  -0.0187 0.0020  16  PRO   A CD  
157  N N   A LYS   A 21  ? 0.1711 0.2666 0.0969 0.0258  -0.0099 0.0171  17  LYS   A N   
158  N N   B LYS   A 21  ? 0.1887 0.2620 0.1077 0.0222  -0.0245 0.0200  17  LYS   A N   
159  C CA  A LYS   A 21  ? 0.1878 0.3372 0.1658 0.0166  -0.0871 0.0715  17  LYS   A CA  
160  C CA  B LYS   A 21  ? 0.2063 0.2908 0.1865 0.0331  -0.0303 0.0515  17  LYS   A CA  
161  C C   A LYS   A 21  ? 0.1999 0.2864 0.1751 0.0234  -0.0521 0.1646  17  LYS   A C   
162  C C   B LYS   A 21  ? 0.2116 0.3166 0.2476 0.0253  -0.0246 0.0998  17  LYS   A C   
163  O O   A LYS   A 21  ? 0.1628 0.3087 0.2518 0.0181  -0.0382 0.1943  17  LYS   A O   
164  O O   B LYS   A 21  ? 0.2183 0.3218 0.2890 0.0223  -0.0330 0.1206  17  LYS   A O   
165  C CB  A LYS   A 21  ? 0.2469 0.3037 0.2307 0.0065  -0.0435 0.1448  17  LYS   A CB  
166  C CB  B LYS   A 21  ? 0.2292 0.2884 0.1992 0.0327  -0.0062 0.0574  17  LYS   A CB  
167  C CG  A LYS   A 21  ? 0.2701 0.3804 0.3047 -0.0225 0.0283  0.1263  17  LYS   A CG  
168  C CG  B LYS   A 21  ? 0.2310 0.2799 0.2087 0.0386  0.0327  0.0526  17  LYS   A CG  
169  C CD  A LYS   A 21  ? 0.4262 0.4168 0.3310 -0.0220 0.0345  0.1484  17  LYS   A CD  
170  C CD  B LYS   A 21  ? 0.2600 0.2588 0.2144 0.0496  0.0416  0.0309  17  LYS   A CD  
171  C CE  A LYS   A 21  ? 0.4702 0.4476 0.4597 -0.0551 0.0339  0.1277  17  LYS   A CE  
172  C CE  B LYS   A 21  ? 0.2516 0.2462 0.2410 0.0645  0.0765  0.0001  17  LYS   A CE  
173  N NZ  A LYS   A 21  ? 0.6702 0.4543 0.4653 0.0119  0.0591  0.1331  17  LYS   A NZ  
174  N NZ  B LYS   A 21  ? 0.2518 0.2200 0.2476 0.0818  0.0923  -0.0046 17  LYS   A NZ  
175  N N   . ARG   A 22  ? 0.2035 0.3298 0.3638 0.0497  -0.0370 0.1843  18  ARG   A N   
176  C CA  . ARG   A 22  ? 0.2124 0.3304 0.4020 0.0260  -0.0084 0.2160  18  ARG   A CA  
177  C C   . ARG   A 22  ? 0.2021 0.3086 0.4289 -0.0019 -0.0735 0.2190  18  ARG   A C   
178  O O   . ARG   A 22  ? 0.1978 0.3807 0.4102 -0.0697 -0.1259 0.2421  18  ARG   A O   
179  C CB  . ARG   A 22  ? 0.2156 0.4128 0.5155 0.0873  -0.0069 0.1904  18  ARG   A CB  
180  C CG  . ARG   A 22  ? 0.3283 0.4119 0.5353 0.1089  0.0499  0.1127  18  ARG   A CG  
181  C CD  . ARG   A 22  ? 0.4885 0.3696 0.4334 0.0918  0.1496  0.0089  18  ARG   A CD  
182  N NE  . ARG   A 22  ? 0.4626 0.4058 0.5115 0.1059  0.1379  -0.0487 18  ARG   A NE  
183  C CZ  . ARG   A 22  ? 0.4985 0.5203 0.4802 -0.0008 0.1044  -0.0671 18  ARG   A CZ  
184  N NH1 . ARG   A 22  ? 0.4893 0.6720 0.5164 -0.0106 0.0517  -0.0896 18  ARG   A NH1 
185  N NH2 . ARG   A 22  ? 0.3125 0.2340 0.5559 -0.0549 0.1653  -0.1403 18  ARG   A NH2 
186  N N   . GLY   A 23  ? 0.2179 0.3378 0.4715 -0.0366 -0.0645 0.2055  19  GLY   A N   
187  C CA  . GLY   A 23  ? 0.2804 0.3888 0.4790 -0.0231 -0.1918 0.2069  19  GLY   A CA  
188  C C   . GLY   A 23  ? 0.2392 0.3481 0.4253 -0.0926 -0.1468 0.2324  19  GLY   A C   
189  O O   . GLY   A 23  ? 0.4172 0.3531 0.5234 -0.0814 -0.2543 0.1812  19  GLY   A O   
190  N N   . GLN   A 24  ? 0.2616 0.3279 0.3801 -0.0727 -0.1552 0.2163  20  GLN   A N   
191  C CA  . GLN   A 24  ? 0.2738 0.3363 0.2642 -0.0768 -0.1185 0.2099  20  GLN   A CA  
192  C C   . GLN   A 24  ? 0.2551 0.2939 0.2256 -0.0685 -0.1049 0.1729  20  GLN   A C   
193  O O   . GLN   A 24  ? 0.2146 0.2849 0.3142 -0.0452 -0.0620 0.1583  20  GLN   A O   
194  C CB  . GLN   A 24  ? 0.3242 0.3578 0.1718 -0.1096 -0.1302 0.1527  20  GLN   A CB  
195  C CG  . GLN   A 24  ? 0.3192 0.3769 0.1727 -0.1280 -0.1122 0.1375  20  GLN   A CG  
196  C CD  . GLN   A 24  ? 0.2933 0.4769 0.1414 -0.1155 -0.0527 0.0192  20  GLN   A CD  
197  O OE1 . GLN   A 24  ? 0.2071 0.3653 0.1666 -0.0910 -0.0114 -0.0136 20  GLN   A OE1 
198  N NE2 . GLN   A 24  ? 0.3661 0.5347 0.2166 -0.0831 0.0071  -0.0417 20  GLN   A NE2 
199  N N   . THR   A 25  ? 0.2474 0.3285 0.1748 -0.0745 -0.0785 0.1798  21  THR   A N   
200  C CA  . THR   A 25  ? 0.2164 0.2741 0.1334 -0.0544 -0.0534 0.1222  21  THR   A CA  
201  C C   . THR   A 25  ? 0.1833 0.2384 0.0802 -0.0388 -0.0103 0.0731  21  THR   A C   
202  O O   . THR   A 25  ? 0.2014 0.3516 0.0869 -0.0586 0.0033  0.1055  21  THR   A O   
203  C CB  . THR   A 25  ? 0.2120 0.2970 0.1453 -0.0484 -0.0558 0.0800  21  THR   A CB  
204  O OG1 . THR   A 25  ? 0.2323 0.3694 0.1956 -0.0770 -0.0862 0.1335  21  THR   A OG1 
205  C CG2 . THR   A 25  ? 0.2524 0.2334 0.1589 -0.0320 -0.0550 0.0164  21  THR   A CG2 
206  N N   . CYS   A 26  ? 0.1570 0.1925 0.0757 -0.0258 -0.0117 0.0530  22  CYS   A N   
207  C CA  . CYS   A 26  ? 0.1319 0.1428 0.0879 -0.0109 -0.0070 0.0240  22  CYS   A CA  
208  C C   . CYS   A 26  ? 0.1406 0.1353 0.0466 -0.0252 0.0032  0.0121  22  CYS   A C   
209  O O   . CYS   A 26  ? 0.1378 0.1409 0.1082 -0.0211 -0.0065 0.0252  22  CYS   A O   
210  C CB  . CYS   A 26  ? 0.1785 0.1569 0.0984 -0.0267 0.0220  0.0106  22  CYS   A CB  
211  S SG  . CYS   A 26  ? 0.2638 0.1532 0.1741 -0.0165 0.0672  0.0084  22  CYS   A SG  
212  N N   . VAL   A 27  ? 0.1324 0.1207 0.0153 -0.0353 0.0081  0.0094  23  VAL   A N   
213  C CA  . VAL   A 27  ? 0.1402 0.1212 0.0116 -0.0368 -0.0149 0.0067  23  VAL   A CA  
214  C C   . VAL   A 27  ? 0.1302 0.1216 0.0115 -0.0233 -0.0102 0.0106  23  VAL   A C   
215  O O   . VAL   A 27  ? 0.1332 0.1434 0.0248 -0.0302 -0.0107 0.0078  23  VAL   A O   
216  C CB  . VAL   A 27  ? 0.1834 0.1378 0.0071 -0.0317 -0.0109 -0.0028 23  VAL   A CB  
217  C CG1 . VAL   A 27  ? 0.1726 0.1547 0.0247 -0.0019 -0.0150 0.0038  23  VAL   A CG1 
218  C CG2 . VAL   A 27  ? 0.1940 0.1364 0.0075 -0.0372 -0.0104 0.0109  23  VAL   A CG2 
219  N N   A VAL   A 28  ? 0.1441 0.1038 0.0089 -0.0386 -0.0135 -0.0067 24  VAL   A N   
220  N N   B VAL   A 28  ? 0.1485 0.1086 0.0126 -0.0395 -0.0280 0.0157  24  VAL   A N   
221  C CA  A VAL   A 28  ? 0.1438 0.1046 0.0108 -0.0309 -0.0096 -0.0165 24  VAL   A CA  
222  C CA  B VAL   A 28  ? 0.1438 0.1180 0.0253 -0.0254 -0.0475 0.0253  24  VAL   A CA  
223  C C   A VAL   A 28  ? 0.1303 0.1275 0.0068 -0.0114 -0.0034 0.0070  24  VAL   A C   
224  C C   B VAL   A 28  ? 0.1436 0.1109 0.0301 -0.0442 -0.0429 0.0221  24  VAL   A C   
225  O O   A VAL   A 28  ? 0.1653 0.1576 0.0168 -0.0171 0.0237  -0.0348 24  VAL   A O   
226  O O   B VAL   A 28  ? 0.1790 0.1407 0.0695 -0.0776 -0.0958 0.0648  24  VAL   A O   
227  C CB  A VAL   A 28  ? 0.1347 0.1081 0.0182 -0.0191 -0.0149 -0.0294 24  VAL   A CB  
228  C CB  B VAL   A 28  ? 0.1547 0.1342 0.0578 -0.0145 -0.0386 0.0216  24  VAL   A CB  
229  C CG1 A VAL   A 28  ? 0.1290 0.1162 0.0165 -0.0279 -0.0108 -0.0154 24  VAL   A CG1 
230  C CG1 B VAL   A 28  ? 0.1715 0.1495 0.0530 0.0010  -0.0233 -0.0048 24  VAL   A CG1 
231  C CG2 A VAL   A 28  ? 0.1339 0.0991 0.0290 -0.0039 0.0073  -0.0299 24  VAL   A CG2 
232  C CG2 B VAL   A 28  ? 0.1610 0.1338 0.0761 -0.0187 -0.0284 0.0305  24  VAL   A CG2 
233  N N   . HIS   A 29  ? 0.1170 0.1051 0.0095 -0.0209 -0.0127 0.0020  25  HIS   A N   
234  C CA  . HIS   A 29  ? 0.1321 0.1001 0.0064 -0.0115 -0.0029 -0.0021 25  HIS   A CA  
235  C C   . HIS   A 29  ? 0.1219 0.0937 0.0081 -0.0179 -0.0030 -0.0106 25  HIS   A C   
236  O O   . HIS   A 29  ? 0.1497 0.1037 0.0167 -0.0386 0.0057  -0.0125 25  HIS   A O   
237  C CB  . HIS   A 29  ? 0.1262 0.1216 0.0077 -0.0142 0.0109  0.0056  25  HIS   A CB  
238  C CG  . HIS   A 29  ? 0.1233 0.1182 0.0171 -0.0058 -0.0022 0.0029  25  HIS   A CG  
239  N ND1 . HIS   A 29  ? 0.1248 0.1303 0.0138 -0.0103 0.0035  -0.0269 25  HIS   A ND1 
240  C CD2 . HIS   A 29  ? 0.1331 0.1233 0.0696 -0.0040 0.0201  -0.0069 25  HIS   A CD2 
241  C CE1 . HIS   A 29  ? 0.1676 0.1139 0.0153 -0.0211 -0.0112 -0.0244 25  HIS   A CE1 
242  N NE2 . HIS   A 29  ? 0.1606 0.1422 0.0661 -0.0061 0.0019  -0.0254 25  HIS   A NE2 
243  N N   . TYR   A 30  ? 0.1324 0.0821 0.0088 -0.0044 0.0039  -0.0134 26  TYR   A N   
244  C CA  . TYR   A 30  ? 0.1270 0.0731 0.0092 -0.0043 0.0031  -0.0138 26  TYR   A CA  
245  C C   . TYR   A 30  ? 0.1164 0.0850 0.0072 0.0038  -0.0008 -0.0086 26  TYR   A C   
246  O O   . TYR   A 30  ? 0.1324 0.0830 0.0069 -0.0110 0.0024  0.0061  26  TYR   A O   
247  C CB  . TYR   A 30  ? 0.1328 0.0840 0.0063 0.0060  -0.0002 -0.0015 26  TYR   A CB  
248  C CG  . TYR   A 30  ? 0.1115 0.0987 0.0099 0.0134  0.0051  0.0022  26  TYR   A CG  
249  C CD1 . TYR   A 30  ? 0.1138 0.1065 0.0083 0.0127  0.0081  -0.0013 26  TYR   A CD1 
250  C CD2 . TYR   A 30  ? 0.1199 0.1151 0.0063 0.0098  0.0017  0.0001  26  TYR   A CD2 
251  C CE1 . TYR   A 30  ? 0.1152 0.1003 0.0090 0.0108  0.0167  0.0047  26  TYR   A CE1 
252  C CE2 . TYR   A 30  ? 0.1230 0.1063 0.0095 0.0038  0.0117  0.0146  26  TYR   A CE2 
253  C CZ  . TYR   A 30  ? 0.1004 0.0921 0.0107 0.0136  0.0114  0.0075  26  TYR   A CZ  
254  O OH  . TYR   A 30  ? 0.1173 0.1110 0.0389 -0.0013 -0.0126 0.0086  26  TYR   A OH  
255  N N   . THR   A 31  ? 0.1238 0.0881 0.0078 0.0005  0.0064  -0.0097 27  THR   A N   
256  C CA  . THR   A 31  ? 0.1197 0.0830 0.0073 -0.0069 0.0043  -0.0082 27  THR   A CA  
257  C C   . THR   A 31  ? 0.1374 0.0831 0.0076 0.0016  -0.0038 -0.0096 27  THR   A C   
258  O O   . THR   A 31  ? 0.1409 0.0863 0.0295 -0.0095 0.0094  -0.0034 27  THR   A O   
259  C CB  . THR   A 31  ? 0.1295 0.1016 0.0368 0.0070  -0.0024 -0.0025 27  THR   A CB  
260  O OG1 . THR   A 31  ? 0.1487 0.1158 0.0682 0.0226  0.0101  -0.0130 27  THR   A OG1 
261  C CG2 . THR   A 31  ? 0.1667 0.0892 0.0354 0.0073  -0.0054 -0.0029 27  THR   A CG2 
262  N N   . GLY   A 32  ? 0.1402 0.0814 0.0127 -0.0091 0.0035  -0.0220 28  GLY   A N   
263  C CA  . GLY   A 32  ? 0.1407 0.0729 0.0279 0.0047  0.0180  -0.0065 28  GLY   A CA  
264  C C   . GLY   A 32  ? 0.1221 0.0804 0.0185 -0.0040 0.0170  -0.0154 28  GLY   A C   
265  O O   . GLY   A 32  ? 0.1530 0.0794 0.0149 -0.0051 0.0223  -0.0117 28  GLY   A O   
266  N N   . MET   A 33  ? 0.1300 0.0853 0.0090 0.0056  0.0137  -0.0091 29  MET   A N   
267  C CA  . MET   A 33  ? 0.1602 0.1055 0.0084 0.0096  0.0169  -0.0043 29  MET   A CA  
268  C C   . MET   A 33  ? 0.1596 0.0906 0.0077 0.0008  0.0120  -0.0060 29  MET   A C   
269  O O   . MET   A 33  ? 0.1816 0.0934 0.0144 0.0098  0.0211  -0.0077 29  MET   A O   
270  C CB  . MET   A 33  ? 0.1688 0.1693 0.0148 0.0210  0.0059  0.0070  29  MET   A CB  
271  C CG  . MET   A 33  ? 0.1701 0.1845 0.0651 0.0364  -0.0131 -0.0032 29  MET   A CG  
272  S SD  . MET   A 33  ? 0.1885 0.2521 0.1107 0.0253  -0.0160 0.0101  29  MET   A SD  
273  C CE  . MET   A 33  ? 0.1849 0.3023 0.0935 0.0913  0.0213  0.0337  29  MET   A CE  
274  N N   . LEU   A 34  ? 0.1640 0.0895 0.0084 0.0130  0.0179  0.0044  30  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1643 0.1178 0.0114 0.0166  0.0201  -0.0064 30  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1696 0.1504 0.0114 0.0428  -0.0039 -0.0232 30  LEU   A C   
277  O O   . LEU   A 34  ? 0.1823 0.1590 0.0364 0.0313  -0.0021 -0.0514 30  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1774 0.1104 0.0191 0.0320  0.0222  0.0165  30  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1765 0.1260 0.0527 0.0097  0.0198  0.0140  30  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1951 0.1639 0.0869 0.0009  0.0276  0.0418  30  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1744 0.1553 0.0632 0.0267  0.0228  0.0082  30  LEU   A CD2 
282  N N   . GLU   A 35  ? 0.2001 0.1415 0.0246 0.0244  0.0174  -0.0259 31  GLU   A N   
283  C CA  . GLU   A 35  ? 0.2302 0.1615 0.0951 0.0006  0.0162  -0.0569 31  GLU   A CA  
284  C C   . GLU   A 35  ? 0.2210 0.2037 0.0612 0.0103  0.0180  -0.0876 31  GLU   A C   
285  O O   . GLU   A 35  ? 0.2428 0.2775 0.1282 -0.0221 -0.0464 -0.0724 31  GLU   A O   
286  C CB  . GLU   A 35  ? 0.2821 0.1848 0.1001 0.0402  -0.0077 -0.0718 31  GLU   A CB  
287  C CG  . GLU   A 35  ? 0.3006 0.2223 0.1610 0.0558  -0.0457 -0.0514 31  GLU   A CG  
288  C CD  . GLU   A 35  ? 0.2954 0.2428 0.2236 0.0814  -0.0575 -0.0897 31  GLU   A CD  
289  O OE1 . GLU   A 35  ? 0.3379 0.3522 0.4331 0.0148  -0.0526 -0.1283 31  GLU   A OE1 
290  O OE2 . GLU   A 35  ? 0.3059 0.3522 0.1485 0.0830  -0.0783 -0.0707 31  GLU   A OE2 
291  N N   . ASP   A 36  ? 0.2290 0.2021 0.0474 0.0177  -0.0152 -0.0633 32  ASP   A N   
292  C CA  . ASP   A 36  ? 0.2966 0.2330 0.0630 0.0446  -0.0407 -0.0550 32  ASP   A CA  
293  C C   . ASP   A 36  ? 0.3231 0.2062 0.0652 0.0738  -0.0530 -0.0436 32  ASP   A C   
294  O O   . ASP   A 36  ? 0.3356 0.2757 0.1355 0.1246  -0.1014 -0.0576 32  ASP   A O   
295  C CB  . ASP   A 36  ? 0.3709 0.2308 0.0652 0.0808  -0.0154 0.0118  32  ASP   A CB  
296  C CG  . ASP   A 36  ? 0.3494 0.2863 0.0751 0.0556  0.0450  -0.0468 32  ASP   A CG  
297  O OD1 . ASP   A 36  ? 0.2694 0.2487 0.0685 0.0459  -0.0100 -0.0311 32  ASP   A OD1 
298  O OD2 . ASP   A 36  ? 0.4637 0.3463 0.1174 0.0394  0.0832  0.0157  32  ASP   A OD2 
299  N N   . GLY   A 37  ? 0.2396 0.2032 0.0630 0.0536  -0.0452 -0.0574 33  GLY   A N   
300  C CA  . GLY   A 37  ? 0.2273 0.1969 0.0946 0.0486  -0.0333 -0.0519 33  GLY   A CA  
301  C C   . GLY   A 37  ? 0.1909 0.1846 0.0792 0.0672  -0.0287 -0.0409 33  GLY   A C   
302  O O   . GLY   A 37  ? 0.2118 0.2080 0.0844 0.0641  -0.0113 -0.0545 33  GLY   A O   
303  N N   A LYS   A 38  ? 0.1942 0.1656 0.0385 0.0618  -0.0258 -0.0409 34  LYS   A N   
304  N N   B LYS   A 38  ? 0.2041 0.1677 0.0193 0.0496  -0.0110 -0.0457 34  LYS   A N   
305  C CA  A LYS   A 38  ? 0.2327 0.1351 0.0172 0.0539  -0.0204 -0.0092 34  LYS   A CA  
306  C CA  B LYS   A 38  ? 0.2403 0.1437 0.0088 0.0342  0.0013  -0.0179 34  LYS   A CA  
307  C C   A LYS   A 38  ? 0.1868 0.1081 0.0158 0.0332  -0.0146 -0.0103 34  LYS   A C   
308  C C   B LYS   A 38  ? 0.1901 0.1127 0.0103 0.0268  -0.0078 -0.0103 34  LYS   A C   
309  O O   A LYS   A 38  ? 0.2217 0.0958 0.0071 0.0316  0.0024  -0.0025 34  LYS   A O   
310  O O   B LYS   A 38  ? 0.2270 0.1028 0.0072 0.0300  0.0028  -0.0086 34  LYS   A O   
311  C CB  A LYS   A 38  ? 0.2751 0.1839 0.0276 0.0452  0.0128  -0.0038 34  LYS   A CB  
312  C CB  B LYS   A 38  ? 0.3019 0.1868 0.0136 0.0111  0.0416  -0.0147 34  LYS   A CB  
313  C CG  A LYS   A 38  ? 0.3252 0.2340 0.0290 0.0592  0.0102  0.0076  34  LYS   A CG  
314  C CG  B LYS   A 38  ? 0.3723 0.2430 0.0260 -0.0069 0.0768  -0.0304 34  LYS   A CG  
315  C CD  A LYS   A 38  ? 0.3862 0.2475 0.1652 0.0614  0.0249  -0.0461 34  LYS   A CD  
316  C CD  B LYS   A 38  ? 0.3877 0.2587 0.0455 -0.0441 0.1129  0.0240  34  LYS   A CD  
317  C CE  A LYS   A 38  ? 0.3711 0.3294 0.1439 0.0852  0.0424  -0.0539 34  LYS   A CE  
318  C CE  B LYS   A 38  ? 0.4589 0.3083 0.0859 -0.0509 0.0888  0.0818  34  LYS   A CE  
319  N NZ  A LYS   A 38  ? 0.3859 0.3440 0.1081 0.1082  0.0376  0.0052  34  LYS   A NZ  
320  N NZ  B LYS   A 38  ? 0.4694 0.3989 0.0984 -0.0569 0.1301  0.1303  34  LYS   A NZ  
321  N N   . LYS   A 39  ? 0.1793 0.1214 0.0065 0.0428  0.0019  0.0045  35  LYS   A N   
322  C CA  . LYS   A 39  ? 0.1637 0.0881 0.0068 0.0266  -0.0047 0.0045  35  LYS   A CA  
323  C C   . LYS   A 39  ? 0.1567 0.0903 0.0119 0.0254  0.0123  0.0048  35  LYS   A C   
324  O O   . LYS   A 39  ? 0.1546 0.1207 0.0789 0.0097  0.0011  0.0381  35  LYS   A O   
325  C CB  . LYS   A 39  ? 0.1516 0.1188 0.0075 0.0308  -0.0121 -0.0075 35  LYS   A CB  
326  C CG  . LYS   A 39  ? 0.1525 0.1004 0.0078 0.0065  -0.0046 -0.0116 35  LYS   A CG  
327  C CD  . LYS   A 39  ? 0.1657 0.1070 0.0097 0.0068  0.0226  -0.0036 35  LYS   A CD  
328  C CE  . LYS   A 39  ? 0.1462 0.1044 0.0218 0.0172  0.0140  -0.0094 35  LYS   A CE  
329  N NZ  . LYS   A 39  ? 0.1570 0.1076 0.0244 0.0295  0.0127  -0.0004 35  LYS   A NZ  
330  N N   . PHE   A 40  ? 0.1504 0.0867 0.0085 0.0132  -0.0007 0.0040  36  PHE   A N   
331  C CA  . PHE   A 40  ? 0.1325 0.0923 0.0233 -0.0043 0.0232  0.0010  36  PHE   A CA  
332  C C   . PHE   A 40  ? 0.1360 0.0840 0.0215 -0.0101 0.0122  0.0093  36  PHE   A C   
333  O O   . PHE   A 40  ? 0.1439 0.1068 0.0289 -0.0171 0.0095  -0.0021 36  PHE   A O   
334  C CB  . PHE   A 40  ? 0.1309 0.1107 0.0092 0.0004  0.0184  -0.0046 36  PHE   A CB  
335  C CG  . PHE   A 40  ? 0.1344 0.1009 0.0132 0.0162  0.0044  -0.0059 36  PHE   A CG  
336  C CD1 . PHE   A 40  ? 0.1452 0.0976 0.0090 0.0233  0.0068  -0.0132 36  PHE   A CD1 
337  C CD2 . PHE   A 40  ? 0.1348 0.1035 0.0182 0.0194  -0.0055 -0.0078 36  PHE   A CD2 
338  C CE1 . PHE   A 40  ? 0.1229 0.1150 0.0257 0.0159  -0.0111 0.0100  36  PHE   A CE1 
339  C CE2 . PHE   A 40  ? 0.1434 0.1008 0.0105 0.0196  0.0071  -0.0177 36  PHE   A CE2 
340  C CZ  . PHE   A 40  ? 0.1257 0.1099 0.0236 0.0137  0.0021  0.0098  36  PHE   A CZ  
341  N N   . ASP   A 41  ? 0.1234 0.0862 0.0071 -0.0102 0.0004  -0.0081 37  ASP   A N   
342  C CA  . ASP   A 41  ? 0.1387 0.0874 0.0065 0.0015  -0.0017 -0.0039 37  ASP   A CA  
343  C C   . ASP   A 41  ? 0.1285 0.0755 0.0240 0.0031  -0.0049 -0.0129 37  ASP   A C   
344  O O   . ASP   A 41  ? 0.1221 0.1036 0.0431 -0.0206 0.0162  -0.0277 37  ASP   A O   
345  C CB  . ASP   A 41  ? 0.1302 0.0999 0.0104 0.0107  0.0096  0.0098  37  ASP   A CB  
346  C CG  . ASP   A 41  ? 0.1315 0.1136 0.0220 0.0048  0.0032  -0.0012 37  ASP   A CG  
347  O OD1 . ASP   A 41  ? 0.1783 0.1100 0.0402 -0.0037 -0.0149 -0.0109 37  ASP   A OD1 
348  O OD2 . ASP   A 41  ? 0.1518 0.1151 0.0256 -0.0093 -0.0036 0.0048  37  ASP   A OD2 
349  N N   . SER   A 42  ? 0.1213 0.0907 0.0311 -0.0041 -0.0029 -0.0240 38  SER   A N   
350  C CA  . SER   A 42  ? 0.1272 0.1006 0.0208 -0.0101 -0.0017 -0.0267 38  SER   A CA  
351  C C   . SER   A 42  ? 0.1088 0.0807 0.0167 -0.0055 0.0137  -0.0195 38  SER   A C   
352  O O   . SER   A 42  ? 0.1486 0.0865 0.0150 -0.0169 0.0069  -0.0246 38  SER   A O   
353  C CB  . SER   A 42  ? 0.1351 0.1131 0.0256 0.0017  0.0010  -0.0237 38  SER   A CB  
354  O OG  . SER   A 42  ? 0.1331 0.1400 0.0178 0.0146  0.0041  0.0013  38  SER   A OG  
355  N N   . SER   A 43  ? 0.1244 0.0820 0.0136 -0.0035 0.0025  -0.0148 39  SER   A N   
356  C CA  . SER   A 43  ? 0.1239 0.0836 0.0133 -0.0138 -0.0115 -0.0197 39  SER   A CA  
357  C C   . SER   A 43  ? 0.1139 0.1130 0.0082 -0.0126 -0.0039 -0.0131 39  SER   A C   
358  O O   . SER   A 43  ? 0.1252 0.1089 0.0101 0.0081  -0.0070 -0.0191 39  SER   A O   
359  C CB  . SER   A 43  ? 0.1241 0.0865 0.0095 -0.0027 0.0008  -0.0161 39  SER   A CB  
360  O OG  . SER   A 43  ? 0.1442 0.0802 0.0258 -0.0214 0.0088  -0.0115 39  SER   A OG  
361  N N   . ARG   A 44  ? 0.1191 0.1294 0.0085 -0.0033 -0.0093 -0.0130 40  ARG   A N   
362  C CA  . ARG   A 44  ? 0.1321 0.1319 0.0154 0.0061  0.0021  -0.0071 40  ARG   A CA  
363  C C   . ARG   A 44  ? 0.1174 0.1233 0.0250 0.0197  -0.0055 -0.0058 40  ARG   A C   
364  O O   . ARG   A 44  ? 0.1308 0.1346 0.0360 0.0208  -0.0024 -0.0233 40  ARG   A O   
365  C CB  . ARG   A 44  ? 0.1390 0.1450 0.0360 0.0028  -0.0145 -0.0040 40  ARG   A CB  
366  C CG  . ARG   A 44  ? 0.1468 0.1722 0.1495 -0.0214 -0.0205 0.0392  40  ARG   A CG  
367  C CD  . ARG   A 44  ? 0.1806 0.1825 0.1641 -0.0019 -0.0360 0.0055  40  ARG   A CD  
368  N NE  . ARG   A 44  ? 0.2339 0.1781 0.1645 -0.0094 -0.0061 0.0004  40  ARG   A NE  
369  C CZ  . ARG   A 44  ? 0.2565 0.1620 0.1742 -0.0299 0.0202  -0.0108 40  ARG   A CZ  
370  N NH1 . ARG   A 44  ? 0.2612 0.2445 0.1849 -0.0706 0.0211  -0.0551 40  ARG   A NH1 
371  N NH2 . ARG   A 44  ? 0.3696 0.2184 0.1287 -0.0671 0.0049  0.0450  40  ARG   A NH2 
372  N N   . ASP   A 45  ? 0.1185 0.1136 0.0332 0.0131  -0.0009 -0.0172 41  ASP   A N   
373  C CA  . ASP   A 45  ? 0.1362 0.1132 0.0127 0.0182  -0.0137 0.0021  41  ASP   A CA  
374  C C   . ASP   A 45  ? 0.1333 0.1066 0.0241 0.0305  -0.0210 -0.0048 41  ASP   A C   
375  O O   . ASP   A 45  ? 0.1893 0.1060 0.0616 0.0374  -0.0312 -0.0011 41  ASP   A O   
376  C CB  . ASP   A 45  ? 0.1642 0.1028 0.0284 0.0126  0.0040  -0.0031 41  ASP   A CB  
377  C CG  . ASP   A 45  ? 0.1714 0.1114 0.0235 0.0179  0.0029  0.0268  41  ASP   A CG  
378  O OD1 . ASP   A 45  ? 0.1749 0.1694 0.0392 0.0261  -0.0146 0.0118  41  ASP   A OD1 
379  O OD2 . ASP   A 45  ? 0.2084 0.1276 0.0335 0.0236  0.0113  0.0018  41  ASP   A OD2 
380  N N   . ARG   A 46  ? 0.1204 0.0744 0.0192 0.0142  -0.0134 -0.0065 42  ARG   A N   
381  C CA  . ARG   A 46  ? 0.1149 0.1063 0.0295 0.0052  -0.0105 -0.0228 42  ARG   A CA  
382  C C   . ARG   A 46  ? 0.1275 0.1133 0.0410 0.0095  0.0003  -0.0194 42  ARG   A C   
383  O O   . ARG   A 46  ? 0.1439 0.1261 0.0432 0.0025  -0.0070 -0.0161 42  ARG   A O   
384  C CB  . ARG   A 46  ? 0.1308 0.1138 0.0354 0.0178  -0.0178 -0.0330 42  ARG   A CB  
385  C CG  . ARG   A 46  ? 0.1337 0.1189 0.0470 0.0122  -0.0156 -0.0353 42  ARG   A CG  
386  C CD  . ARG   A 46  ? 0.1305 0.1095 0.0386 0.0136  -0.0050 -0.0306 42  ARG   A CD  
387  N NE  . ARG   A 46  ? 0.1259 0.1037 0.0343 0.0085  -0.0017 -0.0213 42  ARG   A NE  
388  C CZ  . ARG   A 46  ? 0.1068 0.1007 0.0249 0.0004  -0.0143 -0.0183 42  ARG   A CZ  
389  N NH1 . ARG   A 46  ? 0.1383 0.0990 0.0422 -0.0076 -0.0026 -0.0065 42  ARG   A NH1 
390  N NH2 . ARG   A 46  ? 0.1314 0.0993 0.0349 0.0006  -0.0015 -0.0148 42  ARG   A NH2 
391  N N   . ASN   A 47  ? 0.1265 0.1282 0.0206 0.0073  0.0054  -0.0208 43  ASN   A N   
392  C CA  . ASN   A 47  ? 0.1334 0.1257 0.0408 0.0053  0.0189  -0.0156 43  ASN   A CA  
393  C C   . ASN   A 47  ? 0.1605 0.1309 0.0358 0.0139  0.0175  -0.0190 43  ASN   A C   
394  O O   . ASN   A 47  ? 0.2055 0.1694 0.0324 0.0307  0.0276  -0.0056 43  ASN   A O   
395  C CB  . ASN   A 47  ? 0.1757 0.1237 0.0431 0.0279  0.0129  -0.0033 43  ASN   A CB  
396  C CG  . ASN   A 47  ? 0.1626 0.1036 0.0418 0.0198  -0.0024 -0.0129 43  ASN   A CG  
397  O OD1 . ASN   A 47  ? 0.1572 0.1475 0.0684 0.0049  -0.0110 0.0079  43  ASN   A OD1 
398  N ND2 . ASN   A 47  ? 0.1569 0.1224 0.0876 0.0075  0.0040  -0.0184 43  ASN   A ND2 
399  N N   A LYS   A 48  ? 0.1470 0.1143 0.0269 0.0036  0.0032  -0.0086 44  LYS   A N   
400  N N   B LYS   A 48  ? 0.1437 0.1191 0.0188 0.0070  -0.0033 -0.0062 44  LYS   A N   
401  C CA  A LYS   A 48  ? 0.1922 0.1153 0.0353 0.0089  -0.0065 -0.0016 44  LYS   A CA  
402  C CA  B LYS   A 48  ? 0.1889 0.1208 0.0208 0.0108  -0.0147 -0.0028 44  LYS   A CA  
403  C C   A LYS   A 48  ? 0.1556 0.1108 0.0228 -0.0057 0.0104  -0.0021 44  LYS   A C   
404  C C   B LYS   A 48  ? 0.1490 0.1078 0.0188 -0.0025 -0.0045 0.0043  44  LYS   A C   
405  O O   A LYS   A 48  ? 0.1741 0.1077 0.0078 -0.0221 0.0071  -0.0118 44  LYS   A O   
406  O O   B LYS   A 48  ? 0.1662 0.1113 0.0171 -0.0197 0.0003  -0.0064 44  LYS   A O   
407  C CB  A LYS   A 48  ? 0.1931 0.1159 0.0996 0.0056  -0.0018 -0.0061 44  LYS   A CB  
408  C CB  B LYS   A 48  ? 0.1897 0.1400 0.0624 0.0063  -0.0201 -0.0001 44  LYS   A CB  
409  C CG  A LYS   A 48  ? 0.2328 0.1474 0.1297 0.0190  -0.0310 -0.0059 44  LYS   A CG  
410  C CG  B LYS   A 48  ? 0.2251 0.1689 0.0780 0.0253  -0.0542 -0.0221 44  LYS   A CG  
411  C CD  A LYS   A 48  ? 0.2673 0.2306 0.1762 -0.0021 -0.0591 -0.0364 44  LYS   A CD  
412  C CD  B LYS   A 48  ? 0.2714 0.2501 0.0737 0.0160  -0.0953 -0.0485 44  LYS   A CD  
413  C CE  A LYS   A 48  ? 0.2611 0.3054 0.2107 0.0061  -0.0768 -0.0180 44  LYS   A CE  
414  C CE  B LYS   A 48  ? 0.2936 0.2763 0.1082 0.0572  -0.0465 -0.0304 44  LYS   A CE  
415  N NZ  A LYS   A 48  ? 0.3644 0.3476 0.2335 0.0065  -0.0272 -0.0712 44  LYS   A NZ  
416  N NZ  B LYS   A 48  ? 0.3234 0.3412 0.1364 0.0237  -0.0687 -0.0149 44  LYS   A NZ  
417  N N   A PRO   A 49  ? 0.1588 0.1244 0.0289 -0.0038 0.0126  0.0135  45  PRO   A N   
418  N N   B PRO   A 49  ? 0.1410 0.1050 0.0122 -0.0031 -0.0092 0.0011  45  PRO   A N   
419  C CA  A PRO   A 49  ? 0.1612 0.1248 0.0592 -0.0102 0.0109  0.0018  45  PRO   A CA  
420  C CA  B PRO   A 49  ? 0.1429 0.1039 0.0201 -0.0074 -0.0099 0.0000  45  PRO   A CA  
421  C C   A PRO   A 49  ? 0.1590 0.1115 0.0252 -0.0254 -0.0037 -0.0050 45  PRO   A C   
422  C C   B PRO   A 49  ? 0.1442 0.1155 0.0113 -0.0123 -0.0171 -0.0029 45  PRO   A C   
423  O O   A PRO   A 49  ? 0.1885 0.1278 0.0304 -0.0047 -0.0311 -0.0149 45  PRO   A O   
424  O O   B PRO   A 49  ? 0.1763 0.1255 0.0107 0.0019  -0.0243 -0.0106 45  PRO   A O   
425  C CB  A PRO   A 49  ? 0.1748 0.1491 0.1378 -0.0358 0.0096  0.0483  45  PRO   A CB  
426  C CB  B PRO   A 49  ? 0.1292 0.1017 0.0446 -0.0030 -0.0116 0.0095  45  PRO   A CB  
427  C CG  A PRO   A 49  ? 0.2283 0.1945 0.1053 -0.0226 0.0252  0.0155  45  PRO   A CG  
428  C CG  B PRO   A 49  ? 0.1248 0.1007 0.0424 -0.0007 -0.0085 0.0108  45  PRO   A CG  
429  C CD  A PRO   A 49  ? 0.1916 0.1686 0.0490 0.0000  0.0374  0.0037  45  PRO   A CD  
430  C CD  B PRO   A 49  ? 0.1372 0.1002 0.0154 0.0024  -0.0065 0.0090  45  PRO   A CD  
431  N N   . PHE   A 50  ? 0.1461 0.1148 0.0211 -0.0169 -0.0052 -0.0031 46  PHE   A N   
432  C CA  . PHE   A 50  ? 0.1439 0.1116 0.0175 -0.0201 -0.0041 -0.0096 46  PHE   A CA  
433  C C   . PHE   A 50  ? 0.1116 0.1205 0.0249 -0.0196 -0.0052 0.0000  46  PHE   A C   
434  O O   . PHE   A 50  ? 0.1385 0.1423 0.0299 -0.0417 -0.0124 0.0104  46  PHE   A O   
435  C CB  . PHE   A 50  ? 0.1515 0.1136 0.0123 -0.0164 0.0019  0.0051  46  PHE   A CB  
436  C CG  . PHE   A 50  ? 0.1465 0.1196 0.0327 -0.0126 0.0124  0.0070  46  PHE   A CG  
437  C CD1 . PHE   A 50  ? 0.1660 0.1104 0.1682 -0.0159 0.0011  -0.0263 46  PHE   A CD1 
438  C CD2 . PHE   A 50  ? 0.1659 0.1280 0.0443 -0.0211 0.0097  -0.0031 46  PHE   A CD2 
439  C CE1 . PHE   A 50  ? 0.1535 0.1684 0.1965 -0.0125 0.0018  -0.0342 46  PHE   A CE1 
440  C CE2 . PHE   A 50  ? 0.1814 0.1399 0.0590 -0.0073 0.0279  0.0062  46  PHE   A CE2 
441  C CZ  . PHE   A 50  ? 0.1584 0.1597 0.0667 0.0068  0.0049  -0.0023 46  PHE   A CZ  
442  N N   . LYS   A 51  ? 0.1197 0.1276 0.0257 -0.0292 -0.0143 -0.0001 47  LYS   A N   
443  C CA  . LYS   A 51  ? 0.1611 0.1220 0.0190 -0.0235 0.0001  -0.0046 47  LYS   A CA  
444  C C   . LYS   A 51  ? 0.1494 0.1391 0.0292 -0.0250 -0.0052 0.0114  47  LYS   A C   
445  O O   . LYS   A 51  ? 0.1455 0.1653 0.0661 -0.0336 -0.0172 0.0160  47  LYS   A O   
446  C CB  . LYS   A 51  ? 0.1785 0.1527 0.0180 -0.0107 -0.0190 -0.0063 47  LYS   A CB  
447  C CG  . LYS   A 51  ? 0.1890 0.1693 0.0494 -0.0118 -0.0105 -0.0380 47  LYS   A CG  
448  C CD  . LYS   A 51  ? 0.2346 0.2282 0.0548 -0.0136 0.0205  -0.0461 47  LYS   A CD  
449  C CE  . LYS   A 51  ? 0.2744 0.2735 0.1085 -0.0008 0.0549  -0.0929 47  LYS   A CE  
450  N NZ  . LYS   A 51  ? 0.3572 0.4093 0.1077 0.0014  0.0289  -0.0785 47  LYS   A NZ  
451  N N   . PHE   A 52  ? 0.1369 0.1357 0.0158 -0.0128 -0.0081 0.0099  48  PHE   A N   
452  C CA  . PHE   A 52  ? 0.1232 0.1559 0.0189 -0.0109 -0.0101 0.0366  48  PHE   A CA  
453  C C   . PHE   A 52  ? 0.1366 0.1767 0.0165 0.0071  -0.0015 0.0415  48  PHE   A C   
454  O O   . PHE   A 52  ? 0.1395 0.1682 0.0625 -0.0032 -0.0119 0.0300  48  PHE   A O   
455  C CB  . PHE   A 52  ? 0.1275 0.1569 0.0287 -0.0114 0.0031  0.0223  48  PHE   A CB  
456  C CG  . PHE   A 52  ? 0.1497 0.1565 0.0487 -0.0306 0.0093  0.0321  48  PHE   A CG  
457  C CD1 . PHE   A 52  ? 0.1661 0.1498 0.0323 -0.0381 -0.0060 0.0231  48  PHE   A CD1 
458  C CD2 . PHE   A 52  ? 0.1876 0.1699 0.0098 -0.0205 -0.0021 0.0238  48  PHE   A CD2 
459  C CE1 . PHE   A 52  ? 0.1642 0.1952 0.0386 -0.0540 -0.0009 0.0107  48  PHE   A CE1 
460  C CE2 . PHE   A 52  ? 0.2317 0.1844 0.0379 -0.0412 0.0014  -0.0004 48  PHE   A CE2 
461  C CZ  . PHE   A 52  ? 0.2106 0.1777 0.0665 -0.0733 -0.0051 -0.0055 48  PHE   A CZ  
462  N N   A MET   A 53  ? 0.1380 0.1726 0.0752 0.0038  -0.0230 0.0544  49  MET   A N   
463  N N   B MET   A 53  ? 0.1466 0.1808 0.0490 0.0046  -0.0198 0.0613  49  MET   A N   
464  C CA  A MET   A 53  ? 0.1758 0.1971 0.0865 0.0183  -0.0266 0.0855  49  MET   A CA  
465  C CA  B MET   A 53  ? 0.1825 0.1963 0.0748 -0.0035 -0.0239 0.0853  49  MET   A CA  
466  C C   A MET   A 53  ? 0.1777 0.1765 0.0973 -0.0165 -0.0524 0.0704  49  MET   A C   
467  C C   B MET   A 53  ? 0.1925 0.1851 0.0964 -0.0243 -0.0393 0.0726  49  MET   A C   
468  O O   A MET   A 53  ? 0.1846 0.1548 0.1067 -0.0237 -0.0291 0.0323  49  MET   A O   
469  O O   B MET   A 53  ? 0.1923 0.2168 0.1346 -0.0284 -0.0197 0.0595  49  MET   A O   
470  C CB  A MET   A 53  ? 0.2122 0.2348 0.1159 0.0078  -0.0594 0.0756  49  MET   A CB  
471  C CB  B MET   A 53  ? 0.2023 0.1955 0.0735 0.0031  -0.0295 0.0996  49  MET   A CB  
472  C CG  A MET   A 53  ? 0.2432 0.2455 0.0931 -0.0016 -0.0578 0.0738  49  MET   A CG  
473  C CG  B MET   A 53  ? 0.2167 0.1964 0.0940 -0.0098 -0.0180 0.1093  49  MET   A CG  
474  S SD  A MET   A 53  ? 0.2985 0.3632 0.1002 -0.0389 -0.0685 0.0475  49  MET   A SD  
475  S SD  B MET   A 53  ? 0.2384 0.1765 0.0876 0.0052  -0.0094 0.1150  49  MET   A SD  
476  C CE  A MET   A 53  ? 0.3436 0.2977 0.1459 -0.0172 -0.0467 0.0657  49  MET   A CE  
477  C CE  B MET   A 53  ? 0.1394 0.1926 0.0327 -0.0023 -0.0215 0.0656  49  MET   A CE  
478  N N   . LEU   A 54  ? 0.2215 0.2109 0.1058 -0.0561 -0.0498 0.0892  50  LEU   A N   
479  C CA  . LEU   A 54  ? 0.2729 0.1954 0.1312 -0.0618 -0.0843 0.0631  50  LEU   A CA  
480  C C   . LEU   A 54  ? 0.3214 0.1283 0.1213 -0.0154 -0.1008 0.0085  50  LEU   A C   
481  O O   . LEU   A 54  ? 0.4027 0.2013 0.1396 -0.0427 -0.1638 0.0469  50  LEU   A O   
482  C CB  . LEU   A 54  ? 0.2749 0.2252 0.1518 -0.0745 -0.0241 0.0321  50  LEU   A CB  
483  C CG  . LEU   A 54  ? 0.1963 0.2835 0.1376 -0.0514 0.0107  -0.0709 50  LEU   A CG  
484  C CD1 . LEU   A 54  ? 0.2189 0.3469 0.2326 -0.1061 0.0018  -0.0723 50  LEU   A CD1 
485  C CD2 . LEU   A 54  ? 0.2247 0.2148 0.1147 -0.0196 -0.0408 -0.0179 50  LEU   A CD2 
486  N N   . GLY   A 55  ? 0.3176 0.1576 0.1262 -0.0419 -0.0788 0.0512  51  GLY   A N   
487  C CA  . GLY   A 55  ? 0.3424 0.1882 0.1068 -0.0125 -0.1289 0.0141  51  GLY   A CA  
488  C C   . GLY   A 55  ? 0.2994 0.1741 0.1177 0.0127  -0.1063 0.0420  51  GLY   A C   
489  O O   . GLY   A 55  ? 0.3311 0.2316 0.1817 0.0585  -0.1329 0.0412  51  GLY   A O   
490  N N   A LYS   A 56  ? 0.2863 0.1654 0.1204 0.0130  -0.0718 0.0268  52  LYS   A N   
491  N N   B LYS   A 56  ? 0.2925 0.1663 0.0693 0.0050  -0.0842 0.0301  52  LYS   A N   
492  C CA  A LYS   A 56  ? 0.2614 0.2134 0.1185 0.0173  -0.0828 0.0046  52  LYS   A CA  
493  C CA  B LYS   A 56  ? 0.2822 0.1739 0.0603 0.0165  -0.0983 0.0089  52  LYS   A CA  
494  C C   A LYS   A 56  ? 0.2178 0.1955 0.1073 0.0280  -0.0736 -0.0153 52  LYS   A C   
495  C C   B LYS   A 56  ? 0.2375 0.1719 0.0710 0.0223  -0.0943 0.0025  52  LYS   A C   
496  O O   A LYS   A 56  ? 0.2077 0.1996 0.0918 0.0209  -0.0929 0.0020  52  LYS   A O   
497  O O   B LYS   A 56  ? 0.2736 0.1443 0.1302 0.0214  -0.0837 0.0125  52  LYS   A O   
498  C CB  A LYS   A 56  ? 0.2457 0.2230 0.1684 0.0003  -0.0591 -0.0178 52  LYS   A CB  
499  C CB  B LYS   A 56  ? 0.2581 0.1727 0.0680 -0.0118 -0.0761 0.0066  52  LYS   A CB  
500  C CG  A LYS   A 56  ? 0.2250 0.2712 0.2226 -0.0133 -0.0633 -0.0152 52  LYS   A CG  
501  C CG  B LYS   A 56  ? 0.2515 0.1595 0.0510 -0.0315 -0.0826 -0.0394 52  LYS   A CG  
502  C CD  A LYS   A 56  ? 0.2322 0.3014 0.2576 -0.0096 -0.0716 0.0019  52  LYS   A CD  
503  C CD  B LYS   A 56  ? 0.2186 0.1743 0.1036 -0.0161 -0.1015 -0.0525 52  LYS   A CD  
504  C CE  A LYS   A 56  ? 0.2308 0.3105 0.2576 -0.0129 -0.0519 0.0119  52  LYS   A CE  
505  C CE  B LYS   A 56  ? 0.2501 0.2262 0.1451 -0.0238 -0.0726 -0.0203 52  LYS   A CE  
506  N NZ  A LYS   A 56  ? 0.2120 0.2817 0.2243 -0.0435 -0.0306 -0.0125 52  LYS   A NZ  
507  N NZ  B LYS   A 56  ? 0.2211 0.2461 0.0824 -0.0475 -0.0768 -0.0335 52  LYS   A NZ  
508  N N   A GLN   A 57  ? 0.1808 0.1820 0.1031 0.0169  -0.0582 -0.0143 53  GLN   A N   
509  N N   B GLN   A 57  ? 0.1975 0.1709 0.0654 -0.0012 -0.0714 0.0023  53  GLN   A N   
510  C CA  A GLN   A 57  ? 0.1888 0.2133 0.0840 0.0223  -0.0469 -0.0061 53  GLN   A CA  
511  C CA  B GLN   A 57  ? 0.1796 0.1766 0.0590 -0.0074 -0.0762 0.0027  53  GLN   A CA  
512  C C   A GLN   A 57  ? 0.1595 0.2037 0.0712 -0.0010 -0.0484 -0.0203 53  GLN   A C   
513  C C   B GLN   A 57  ? 0.1622 0.1775 0.0366 -0.0056 -0.0553 -0.0022 53  GLN   A C   
514  O O   A GLN   A 57  ? 0.1736 0.1934 0.1053 0.0195  -0.0268 0.0105  53  GLN   A O   
515  O O   B GLN   A 57  ? 0.1935 0.1962 0.0304 -0.0195 -0.0344 -0.0032 53  GLN   A O   
516  C CB  A GLN   A 57  ? 0.1950 0.2424 0.0782 0.0222  -0.0289 -0.0182 53  GLN   A CB  
517  C CB  B GLN   A 57  ? 0.1718 0.1799 0.0720 -0.0257 -0.0908 0.0096  53  GLN   A CB  
518  C CG  A GLN   A 57  ? 0.2242 0.2689 0.0914 0.0581  0.0002  -0.0105 53  GLN   A CG  
519  C CG  B GLN   A 57  ? 0.1648 0.1839 0.0591 -0.0257 -0.0902 0.0303  53  GLN   A CG  
520  C CD  A GLN   A 57  ? 0.2331 0.2095 0.0928 0.0275  -0.0098 -0.0290 53  GLN   A CD  
521  C CD  B GLN   A 57  ? 0.1500 0.1915 0.0603 -0.0454 -0.0880 0.0234  53  GLN   A CD  
522  O OE1 A GLN   A 57  ? 0.2947 0.1890 0.2859 0.0397  -0.0224 -0.0166 53  GLN   A OE1 
523  O OE1 B GLN   A 57  ? 0.1495 0.2149 0.0535 -0.0354 -0.0638 0.0721  53  GLN   A OE1 
524  N NE2 A GLN   A 57  ? 0.2672 0.2858 0.0539 0.0486  -0.0240 -0.0169 53  GLN   A NE2 
525  N NE2 B GLN   A 57  ? 0.1280 0.1881 0.0211 -0.0622 -0.0419 0.0291  53  GLN   A NE2 
526  N N   . GLU   A 58  ? 0.1641 0.1545 0.0262 -0.0055 -0.0402 0.0106  54  GLU   A N   
527  C CA  . GLU   A 58  ? 0.1773 0.1524 0.0556 0.0061  -0.0189 0.0004  54  GLU   A CA  
528  C C   . GLU   A 58  ? 0.1737 0.1061 0.0693 -0.0053 -0.0297 -0.0024 54  GLU   A C   
529  O O   . GLU   A 58  ? 0.2924 0.1140 0.0514 -0.0111 -0.0262 -0.0181 54  GLU   A O   
530  C CB  . GLU   A 58  ? 0.1686 0.1666 0.0556 -0.0036 -0.0128 0.0108  54  GLU   A CB  
531  C CG  . GLU   A 58  ? 0.1920 0.1924 0.0620 0.0138  -0.0229 0.0088  54  GLU   A CG  
532  C CD  . GLU   A 58  ? 0.2051 0.1896 0.0480 -0.0115 -0.0294 -0.0213 54  GLU   A CD  
533  O OE1 . GLU   A 58  ? 0.2400 0.2922 0.0461 0.0109  -0.0333 -0.0192 54  GLU   A OE1 
534  O OE2 . GLU   A 58  ? 0.1918 0.2247 0.0559 -0.0110 -0.0211 -0.0211 54  GLU   A OE2 
535  N N   . VAL   A 59  ? 0.1352 0.0930 0.0562 0.0044  -0.0328 0.0102  55  VAL   A N   
536  C CA  . VAL   A 59  ? 0.1420 0.0881 0.0347 0.0203  -0.0149 0.0090  55  VAL   A CA  
537  C C   . VAL   A 59  ? 0.0980 0.0845 0.0283 0.0082  -0.0185 0.0123  55  VAL   A C   
538  O O   . VAL   A 59  ? 0.1249 0.0880 0.0389 0.0163  -0.0026 0.0169  55  VAL   A O   
539  C CB  . VAL   A 59  ? 0.1453 0.1145 0.0223 0.0324  -0.0151 0.0070  55  VAL   A CB  
540  C CG1 . VAL   A 59  ? 0.1831 0.1454 0.0230 0.0275  0.0026  -0.0068 55  VAL   A CG1 
541  C CG2 . VAL   A 59  ? 0.1438 0.1139 0.0267 0.0232  -0.0080 -0.0033 55  VAL   A CG2 
542  N N   . ILE   A 60  ? 0.1193 0.0912 0.0187 0.0155  -0.0128 0.0046  56  ILE   A N   
543  C CA  . ILE   A 60  ? 0.1141 0.0938 0.0147 0.0118  -0.0099 0.0064  56  ILE   A CA  
544  C C   . ILE   A 60  ? 0.1134 0.0980 0.0096 0.0099  0.0071  -0.0066 56  ILE   A C   
545  O O   . ILE   A 60  ? 0.1073 0.1077 0.0142 0.0026  -0.0023 0.0017  56  ILE   A O   
546  C CB  . ILE   A 60  ? 0.1165 0.0979 0.0136 0.0167  -0.0022 0.0099  56  ILE   A CB  
547  C CG1 . ILE   A 60  ? 0.1195 0.0928 0.0312 0.0127  -0.0123 0.0144  56  ILE   A CG1 
548  C CG2 . ILE   A 60  ? 0.1250 0.1029 0.0342 0.0111  -0.0129 0.0082  56  ILE   A CG2 
549  C CD1 . ILE   A 60  ? 0.1264 0.1007 0.0300 0.0248  -0.0214 0.0035  56  ILE   A CD1 
550  N N   . ARG   A 61  ? 0.1029 0.0917 0.0328 0.0049  0.0218  -0.0022 57  ARG   A N   
551  C CA  . ARG   A 61  ? 0.1130 0.0932 0.0221 -0.0006 0.0229  0.0078  57  ARG   A CA  
552  C C   . ARG   A 61  ? 0.1196 0.0859 0.0549 0.0011  0.0062  0.0153  57  ARG   A C   
553  O O   . ARG   A 61  ? 0.1144 0.0862 0.0717 0.0065  0.0175  0.0180  57  ARG   A O   
554  C CB  . ARG   A 61  ? 0.1139 0.0954 0.0223 0.0041  0.0114  0.0025  57  ARG   A CB  
555  C CG  . ARG   A 61  ? 0.1077 0.0976 0.0431 0.0124  0.0017  0.0165  57  ARG   A CG  
556  C CD  . ARG   A 61  ? 0.1207 0.1092 0.0501 -0.0029 -0.0017 0.0316  57  ARG   A CD  
557  N NE  . ARG   A 61  ? 0.1121 0.1006 0.0468 -0.0032 -0.0110 0.0173  57  ARG   A NE  
558  C CZ  . ARG   A 61  ? 0.1109 0.1106 0.0542 -0.0091 0.0066  0.0325  57  ARG   A CZ  
559  N NH1 . ARG   A 61  ? 0.1461 0.1324 0.0730 -0.0161 -0.0125 0.0356  57  ARG   A NH1 
560  N NH2 . ARG   A 61  ? 0.1433 0.0983 0.0557 0.0026  0.0086  0.0194  57  ARG   A NH2 
561  N N   . GLY   A 62  ? 0.1158 0.0890 0.0356 -0.0043 0.0005  -0.0005 58  GLY   A N   
562  C CA  . GLY   A 62  ? 0.1135 0.0995 0.0464 -0.0088 0.0012  0.0103  58  GLY   A CA  
563  C C   . GLY   A 62  ? 0.1265 0.0949 0.0313 0.0007  -0.0095 0.0093  58  GLY   A C   
564  O O   . GLY   A 62  ? 0.1240 0.1042 0.0479 -0.0098 -0.0045 0.0018  58  GLY   A O   
565  N N   . TRP   A 63  ? 0.1219 0.0844 0.0589 -0.0052 -0.0049 0.0053  59  TRP   A N   
566  C CA  . TRP   A 63  ? 0.1051 0.1064 0.0700 0.0108  -0.0092 -0.0106 59  TRP   A CA  
567  C C   . TRP   A 63  ? 0.1010 0.1148 0.0544 0.0024  -0.0005 -0.0188 59  TRP   A C   
568  O O   . TRP   A 63  ? 0.1124 0.1312 0.0757 -0.0001 0.0135  -0.0013 59  TRP   A O   
569  C CB  . TRP   A 63  ? 0.1300 0.1082 0.0519 0.0103  -0.0210 -0.0115 59  TRP   A CB  
570  C CG  . TRP   A 63  ? 0.1256 0.0963 0.0285 0.0058  -0.0041 -0.0100 59  TRP   A CG  
571  C CD1 . TRP   A 63  ? 0.1265 0.1372 0.0299 0.0096  0.0003  -0.0007 59  TRP   A CD1 
572  C CD2 . TRP   A 63  ? 0.1120 0.0880 0.0285 -0.0033 -0.0049 -0.0129 59  TRP   A CD2 
573  N NE1 . TRP   A 63  ? 0.1329 0.1464 0.0263 0.0168  -0.0073 0.0029  59  TRP   A NE1 
574  C CE2 . TRP   A 63  ? 0.1280 0.0973 0.0303 0.0050  -0.0088 -0.0074 59  TRP   A CE2 
575  C CE3 . TRP   A 63  ? 0.1214 0.1056 0.0357 -0.0018 0.0205  -0.0036 59  TRP   A CE3 
576  C CZ2 . TRP   A 63  ? 0.1353 0.1055 0.0290 0.0167  -0.0115 0.0161  59  TRP   A CZ2 
577  C CZ3 . TRP   A 63  ? 0.1380 0.1148 0.0133 0.0011  0.0296  -0.0055 59  TRP   A CZ3 
578  C CH2 . TRP   A 63  ? 0.1472 0.1303 0.0350 -0.0010 0.0055  0.0067  59  TRP   A CH2 
579  N N   A GLU   A 64  ? 0.1062 0.1244 0.0565 0.0064  0.0019  -0.0104 60  GLU   A N   
580  N N   B GLU   A 64  ? 0.1098 0.1247 0.0487 0.0032  -0.0022 0.0022  60  GLU   A N   
581  C CA  A GLU   A 64  ? 0.1213 0.1292 0.0568 0.0014  0.0063  -0.0057 60  GLU   A CA  
582  C CA  B GLU   A 64  ? 0.1431 0.1488 0.0260 -0.0032 -0.0092 0.0051  60  GLU   A CA  
583  C C   A GLU   A 64  ? 0.1220 0.1324 0.0708 -0.0033 0.0121  -0.0036 60  GLU   A C   
584  C C   B GLU   A 64  ? 0.1453 0.1456 0.0634 -0.0100 0.0076  -0.0016 60  GLU   A C   
585  O O   A GLU   A 64  ? 0.1429 0.1350 0.0706 -0.0037 0.0183  0.0007  60  GLU   A O   
586  O O   B GLU   A 64  ? 0.1758 0.1669 0.1006 -0.0204 0.0358  -0.0014 60  GLU   A O   
587  C CB  A GLU   A 64  ? 0.1235 0.1311 0.0602 0.0046  0.0069  -0.0031 60  GLU   A CB  
588  C CB  B GLU   A 64  ? 0.1394 0.1510 0.0471 -0.0058 -0.0073 0.0303  60  GLU   A CB  
589  C CG  A GLU   A 64  ? 0.1293 0.1339 0.0568 0.0019  0.0064  -0.0028 60  GLU   A CG  
590  C CG  B GLU   A 64  ? 0.1600 0.1461 0.0731 -0.0161 -0.0176 0.0436  60  GLU   A CG  
591  C CD  A GLU   A 64  ? 0.1322 0.1253 0.0534 0.0004  -0.0023 -0.0035 60  GLU   A CD  
592  C CD  B GLU   A 64  ? 0.1937 0.1807 0.0767 -0.0338 -0.0683 0.0630  60  GLU   A CD  
593  O OE1 A GLU   A 64  ? 0.1226 0.1048 0.0566 -0.0001 0.0022  -0.0285 60  GLU   A OE1 
594  O OE1 B GLU   A 64  ? 0.2451 0.2740 0.0807 -0.0920 -0.0656 0.1119  60  GLU   A OE1 
595  O OE2 A GLU   A 64  ? 0.1325 0.1224 0.0430 -0.0042 -0.0079 -0.0041 60  GLU   A OE2 
596  O OE2 B GLU   A 64  ? 0.2779 0.1942 0.1073 -0.0843 -0.0405 0.0547  60  GLU   A OE2 
597  N N   . GLU   A 65  ? 0.1070 0.1343 0.0794 -0.0112 0.0172  -0.0133 61  GLU   A N   
598  C CA  . GLU   A 65  ? 0.1184 0.1213 0.0908 -0.0126 0.0165  0.0047  61  GLU   A CA  
599  C C   . GLU   A 65  ? 0.1216 0.1075 0.0701 -0.0135 0.0102  -0.0132 61  GLU   A C   
600  O O   . GLU   A 65  ? 0.1128 0.1231 0.1823 -0.0110 0.0152  0.0212  61  GLU   A O   
601  C CB  . GLU   A 65  ? 0.1207 0.1313 0.1166 0.0049  0.0063  -0.0197 61  GLU   A CB  
602  C CG  . GLU   A 65  ? 0.1481 0.1590 0.0873 0.0161  -0.0281 -0.0192 61  GLU   A CG  
603  C CD  . GLU   A 65  ? 0.1265 0.1654 0.1024 0.0136  -0.0163 -0.0181 61  GLU   A CD  
604  O OE1 . GLU   A 65  ? 0.1346 0.2254 0.1630 0.0156  -0.0309 -0.0667 61  GLU   A OE1 
605  O OE2 . GLU   A 65  ? 0.1216 0.1421 0.0714 0.0000  0.0010  -0.0063 61  GLU   A OE2 
606  N N   . GLY   A 66  ? 0.1258 0.1082 0.0518 -0.0133 0.0233  -0.0108 62  GLY   A N   
607  C CA  . GLY   A 66  ? 0.1346 0.1184 0.0457 -0.0012 0.0205  0.0186  62  GLY   A CA  
608  C C   . GLY   A 66  ? 0.1093 0.0843 0.0474 -0.0086 0.0026  -0.0004 62  GLY   A C   
609  O O   . GLY   A 66  ? 0.1144 0.1078 0.0560 -0.0134 0.0063  0.0059  62  GLY   A O   
610  N N   . VAL   A 67  ? 0.1050 0.0953 0.0352 -0.0089 0.0038  0.0005  63  VAL   A N   
611  C CA  . VAL   A 67  ? 0.0969 0.1154 0.0568 0.0023  0.0103  -0.0144 63  VAL   A CA  
612  C C   . VAL   A 67  ? 0.1132 0.1235 0.0299 -0.0140 0.0043  -0.0225 63  VAL   A C   
613  O O   . VAL   A 67  ? 0.1271 0.1493 0.0503 -0.0200 0.0181  -0.0322 63  VAL   A O   
614  C CB  . VAL   A 67  ? 0.1115 0.1289 0.0789 -0.0056 0.0113  -0.0288 63  VAL   A CB  
615  C CG1 . VAL   A 67  ? 0.1450 0.1606 0.0927 -0.0311 0.0329  -0.0447 63  VAL   A CG1 
616  C CG2 . VAL   A 67  ? 0.1272 0.1359 0.0984 0.0052  0.0111  -0.0214 63  VAL   A CG2 
617  N N   . ALA   A 68  ? 0.1287 0.1287 0.0239 -0.0147 0.0247  0.0008  64  ALA   A N   
618  C CA  . ALA   A 68  ? 0.1856 0.1591 0.0166 -0.0195 -0.0011 0.0259  64  ALA   A CA  
619  C C   . ALA   A 68  ? 0.1676 0.1318 0.0479 -0.0094 0.0143  0.0196  64  ALA   A C   
620  O O   . ALA   A 68  ? 0.2264 0.1508 0.0619 -0.0362 0.0141  0.0326  64  ALA   A O   
621  C CB  . ALA   A 68  ? 0.1772 0.1866 0.0803 -0.0198 -0.0301 0.0399  64  ALA   A CB  
622  N N   A GLN   A 69  ? 0.1646 0.1207 0.0470 -0.0095 0.0102  -0.0052 65  GLN   A N   
623  N N   B GLN   A 69  ? 0.1368 0.1065 0.0441 -0.0277 0.0159  -0.0014 65  GLN   A N   
624  C CA  A GLN   A 69  ? 0.1744 0.1641 0.0791 -0.0263 -0.0033 -0.0196 65  GLN   A CA  
625  C CA  B GLN   A 69  ? 0.1337 0.0981 0.0407 -0.0276 0.0214  -0.0067 65  GLN   A CA  
626  C C   A GLN   A 69  ? 0.1623 0.1405 0.0912 -0.0444 0.0025  -0.0240 65  GLN   A C   
627  C C   B GLN   A 69  ? 0.1276 0.1180 0.0416 -0.0265 0.0179  -0.0017 65  GLN   A C   
628  O O   A GLN   A 69  ? 0.1473 0.1357 0.1573 -0.0338 0.0056  -0.0455 65  GLN   A O   
629  O O   B GLN   A 69  ? 0.1328 0.1164 0.0438 -0.0291 0.0154  -0.0023 65  GLN   A O   
630  C CB  A GLN   A 69  ? 0.1709 0.2396 0.0878 -0.0460 0.0074  -0.0614 65  GLN   A CB  
631  C CB  B GLN   A 69  ? 0.1110 0.0670 0.0404 -0.0285 0.0246  -0.0187 65  GLN   A CB  
632  C CG  A GLN   A 69  ? 0.1828 0.2419 0.1737 -0.0257 0.0083  -0.0281 65  GLN   A CG  
633  C CG  B GLN   A 69  ? 0.1098 0.0485 0.0333 -0.0417 0.0277  -0.0253 65  GLN   A CG  
634  C CD  A GLN   A 69  ? 0.2749 0.2753 0.1714 -0.0688 0.0081  -0.0541 65  GLN   A CD  
635  C CD  B GLN   A 69  ? 0.1030 0.0482 0.0331 -0.0391 0.0285  -0.0334 65  GLN   A CD  
636  O OE1 A GLN   A 69  ? 0.2777 0.3975 0.1626 -0.0538 0.0131  -0.0326 65  GLN   A OE1 
637  O OE1 B GLN   A 69  ? 0.1003 0.0480 0.0637 -0.0367 0.0289  -0.0382 65  GLN   A OE1 
638  N NE2 A GLN   A 69  ? 0.2463 0.3151 0.1463 -0.0339 -0.0130 0.0138  65  GLN   A NE2 
639  N NE2 B GLN   A 69  ? 0.0978 0.0365 0.0259 -0.0462 0.0348  -0.0241 65  GLN   A NE2 
640  N N   . MET   A 70  ? 0.1145 0.1264 0.0310 -0.0295 0.0155  -0.0056 66  MET   A N   
641  C CA  . MET   A 70  ? 0.1221 0.1372 0.0362 -0.0181 0.0035  0.0045  66  MET   A CA  
642  C C   . MET   A 70  ? 0.1188 0.1110 0.0298 -0.0120 -0.0050 -0.0006 66  MET   A C   
643  O O   . MET   A 70  ? 0.1208 0.1589 0.0379 -0.0008 0.0010  0.0131  66  MET   A O   
644  C CB  . MET   A 70  ? 0.1254 0.1349 0.0250 -0.0126 0.0137  -0.0032 66  MET   A CB  
645  C CG  . MET   A 70  ? 0.1239 0.1392 0.0359 -0.0118 0.0297  0.0104  66  MET   A CG  
646  S SD  . MET   A 70  ? 0.1341 0.1551 0.0656 -0.0149 0.0140  0.0332  66  MET   A SD  
647  C CE  . MET   A 70  ? 0.1424 0.1507 0.0482 -0.0127 -0.0061 -0.0001 66  MET   A CE  
648  N N   . SER   A 71  ? 0.1159 0.1176 0.0111 -0.0134 -0.0151 0.0112  67  SER   A N   
649  C CA  . SER   A 71  ? 0.1301 0.1193 0.0145 -0.0175 -0.0059 0.0193  67  SER   A CA  
650  C C   . SER   A 71  ? 0.1218 0.1196 0.0134 -0.0322 0.0035  0.0043  67  SER   A C   
651  O O   . SER   A 71  ? 0.1326 0.1179 0.0154 -0.0241 -0.0012 0.0008  67  SER   A O   
652  C CB  . SER   A 71  ? 0.1199 0.1225 0.0396 -0.0064 0.0182  0.0319  67  SER   A CB  
653  O OG  . SER   A 71  ? 0.1231 0.1090 0.0601 -0.0260 -0.0004 0.0151  67  SER   A OG  
654  N N   . VAL   A 72  ? 0.1421 0.1205 0.0097 -0.0126 -0.0081 0.0189  68  VAL   A N   
655  C CA  . VAL   A 72  ? 0.1586 0.1320 0.0065 -0.0217 0.0033  0.0034  68  VAL   A CA  
656  C C   . VAL   A 72  ? 0.1503 0.1180 0.0083 -0.0183 0.0155  -0.0085 68  VAL   A C   
657  O O   . VAL   A 72  ? 0.1505 0.1226 0.0346 -0.0245 0.0334  -0.0213 68  VAL   A O   
658  C CB  . VAL   A 72  ? 0.1750 0.1548 0.0064 -0.0128 -0.0035 0.0031  68  VAL   A CB  
659  C CG1 . VAL   A 72  ? 0.1976 0.1802 0.0099 0.0022  0.0048  -0.0125 68  VAL   A CG1 
660  C CG2 . VAL   A 72  ? 0.1818 0.1676 0.0276 -0.0025 -0.0144 -0.0103 68  VAL   A CG2 
661  N N   . GLY   A 73  ? 0.1344 0.1012 0.0247 -0.0205 0.0121  -0.0163 69  GLY   A N   
662  C CA  . GLY   A 73  ? 0.1395 0.1220 0.0418 0.0055  0.0166  -0.0220 69  GLY   A CA  
663  C C   . GLY   A 73  ? 0.1510 0.1308 0.0399 0.0041  0.0029  -0.0224 69  GLY   A C   
664  O O   . GLY   A 73  ? 0.1806 0.1701 0.0574 0.0405  -0.0088 -0.0198 69  GLY   A O   
665  N N   . GLN   A 74  ? 0.1249 0.1086 0.0076 -0.0155 -0.0024 -0.0110 70  GLN   A N   
666  C CA  . GLN   A 74  ? 0.1107 0.0974 0.0083 -0.0265 -0.0047 -0.0112 70  GLN   A CA  
667  C C   . GLN   A 74  ? 0.1147 0.1082 0.0143 -0.0260 -0.0143 0.0053  70  GLN   A C   
668  O O   . GLN   A 74  ? 0.1130 0.1199 0.0127 -0.0347 -0.0050 -0.0022 70  GLN   A O   
669  C CB  . GLN   A 74  ? 0.1199 0.1044 0.0063 -0.0169 0.0024  0.0001  70  GLN   A CB  
670  C CG  . GLN   A 74  ? 0.1197 0.1118 0.0159 -0.0222 -0.0013 -0.0147 70  GLN   A CG  
671  C CD  . GLN   A 74  ? 0.1227 0.1201 0.0332 -0.0055 -0.0083 -0.0108 70  GLN   A CD  
672  O OE1 . GLN   A 74  ? 0.1516 0.1268 0.0392 -0.0026 -0.0154 -0.0045 70  GLN   A OE1 
673  N NE2 . GLN   A 74  ? 0.1324 0.1396 0.0329 0.0055  -0.0113 -0.0156 70  GLN   A NE2 
674  N N   . ARG   A 75  ? 0.1107 0.1166 0.0073 -0.0215 -0.0073 0.0011  71  ARG   A N   
675  C CA  . ARG   A 75  ? 0.0908 0.1099 0.0169 -0.0218 -0.0008 -0.0065 71  ARG   A CA  
676  C C   . ARG   A 75  ? 0.1044 0.1307 0.0101 -0.0175 -0.0180 -0.0046 71  ARG   A C   
677  O O   . ARG   A 75  ? 0.1066 0.1153 0.0282 -0.0196 -0.0113 -0.0151 71  ARG   A O   
678  C CB  . ARG   A 75  ? 0.1154 0.1144 0.0221 -0.0114 -0.0051 0.0003  71  ARG   A CB  
679  C CG  . ARG   A 75  ? 0.1003 0.1182 0.0731 -0.0091 0.0023  0.0162  71  ARG   A CG  
680  C CD  . ARG   A 75  ? 0.1358 0.1468 0.1407 0.0124  0.0227  0.0586  71  ARG   A CD  
681  N NE  . ARG   A 75  ? 0.1593 0.1737 0.1964 0.0290  0.0586  0.1015  71  ARG   A NE  
682  C CZ  . ARG   A 75  ? 0.1770 0.1770 0.1817 0.0282  0.0029  0.0499  71  ARG   A CZ  
683  N NH1 . ARG   A 75  ? 0.1731 0.2522 0.1996 0.0380  -0.0077 0.0536  71  ARG   A NH1 
684  N NH2 . ARG   A 75  ? 0.1848 0.2527 0.2118 0.0372  -0.0039 0.1009  71  ARG   A NH2 
685  N N   . ALA   A 76  ? 0.1014 0.1010 0.0320 -0.0275 -0.0115 -0.0160 72  ALA   A N   
686  C CA  . ALA   A 76  ? 0.1172 0.1141 0.0322 -0.0216 -0.0119 -0.0235 72  ALA   A CA  
687  C C   . ALA   A 76  ? 0.1052 0.1145 0.0425 -0.0162 -0.0088 -0.0223 72  ALA   A C   
688  O O   . ALA   A 76  ? 0.1303 0.1095 0.0420 -0.0276 0.0053  -0.0247 72  ALA   A O   
689  C CB  . ALA   A 76  ? 0.1644 0.1315 0.0168 -0.0030 0.0151  -0.0170 72  ALA   A CB  
690  N N   . LYS   A 77  ? 0.1034 0.1080 0.0429 -0.0107 0.0010  -0.0204 73  LYS   A N   
691  C CA  . LYS   A 77  ? 0.1063 0.1071 0.0607 -0.0125 0.0029  -0.0056 73  LYS   A CA  
692  C C   . LYS   A 77  ? 0.1133 0.1043 0.0421 -0.0102 -0.0075 -0.0006 73  LYS   A C   
693  O O   . LYS   A 77  ? 0.1248 0.1058 0.0605 -0.0127 0.0035  -0.0165 73  LYS   A O   
694  C CB  . LYS   A 77  ? 0.1481 0.1483 0.0588 0.0100  -0.0065 -0.0001 73  LYS   A CB  
695  C CG  . LYS   A 77  ? 0.1943 0.1762 0.0992 -0.0058 0.0228  0.0154  73  LYS   A CG  
696  C CD  . LYS   A 77  ? 0.2877 0.3138 0.0998 -0.0020 -0.0030 0.0565  73  LYS   A CD  
697  C CE  . LYS   A 77  ? 0.2927 0.3492 0.1278 -0.0300 0.0146  0.0164  73  LYS   A CE  
698  N NZ  . LYS   A 77  ? 0.4567 0.4462 0.1912 0.0076  -0.0895 -0.0239 73  LYS   A NZ  
699  N N   . LEU   A 78  ? 0.1093 0.0782 0.0102 -0.0088 0.0034  -0.0103 74  LEU   A N   
700  C CA  . LEU   A 78  ? 0.1206 0.0865 0.0550 -0.0022 0.0055  -0.0102 74  LEU   A CA  
701  C C   . LEU   A 78  ? 0.1253 0.0814 0.0554 -0.0003 0.0120  -0.0166 74  LEU   A C   
702  O O   . LEU   A 78  ? 0.1805 0.0839 0.1079 -0.0095 0.0439  -0.0211 74  LEU   A O   
703  C CB  . LEU   A 78  ? 0.1575 0.0996 0.1026 0.0030  -0.0399 -0.0183 74  LEU   A CB  
704  C CG  . LEU   A 78  ? 0.1746 0.2298 0.1076 0.0100  -0.0206 -0.0488 74  LEU   A CG  
705  C CD1 . LEU   A 78  ? 0.2663 0.2524 0.0735 0.0116  -0.0697 -0.0559 74  LEU   A CD1 
706  C CD2 . LEU   A 78  ? 0.2710 0.2715 0.1063 -0.0292 -0.0587 0.0037  74  LEU   A CD2 
707  N N   . THR   A 79  ? 0.1210 0.0904 0.0330 -0.0068 -0.0058 -0.0190 75  THR   A N   
708  C CA  . THR   A 79  ? 0.1260 0.1089 0.0431 -0.0064 -0.0015 -0.0080 75  THR   A CA  
709  C C   . THR   A 79  ? 0.1248 0.0955 0.0451 -0.0076 -0.0018 -0.0138 75  THR   A C   
710  O O   . THR   A 79  ? 0.1189 0.0953 0.0902 -0.0034 0.0157  -0.0055 75  THR   A O   
711  C CB  . THR   A 79  ? 0.1423 0.1277 0.0454 0.0005  -0.0127 -0.0119 75  THR   A CB  
712  O OG1 . THR   A 79  ? 0.1320 0.1777 0.0526 0.0082  -0.0201 -0.0060 75  THR   A OG1 
713  C CG2 . THR   A 79  ? 0.1367 0.1813 0.0583 -0.0041 -0.0093 -0.0109 75  THR   A CG2 
714  N N   . ILE   A 80  ? 0.1085 0.0774 0.0355 0.0045  0.0066  -0.0121 76  ILE   A N   
715  C CA  . ILE   A 80  ? 0.1129 0.0777 0.0261 0.0041  0.0035  -0.0067 76  ILE   A CA  
716  C C   . ILE   A 80  ? 0.0936 0.0908 0.0396 0.0065  0.0025  -0.0001 76  ILE   A C   
717  O O   . ILE   A 80  ? 0.1364 0.0969 0.0250 0.0070  -0.0024 -0.0012 76  ILE   A O   
718  C CB  . ILE   A 80  ? 0.1059 0.0868 0.0367 -0.0067 -0.0012 -0.0096 76  ILE   A CB  
719  C CG1 . ILE   A 80  ? 0.1320 0.1135 0.0342 0.0156  0.0049  -0.0169 76  ILE   A CG1 
720  C CG2 . ILE   A 80  ? 0.1147 0.0965 0.0449 0.0012  -0.0069 -0.0117 76  ILE   A CG2 
721  C CD1 . ILE   A 80  ? 0.1176 0.0971 0.0419 0.0278  0.0062  -0.0197 76  ILE   A CD1 
722  N N   . SER   A 81  ? 0.1184 0.0987 0.0404 0.0095  0.0037  -0.0103 77  SER   A N   
723  C CA  . SER   A 81  ? 0.1365 0.1188 0.0262 0.0102  0.0061  -0.0070 77  SER   A CA  
724  C C   . SER   A 81  ? 0.1370 0.1075 0.0159 0.0078  0.0051  0.0039  77  SER   A C   
725  O O   . SER   A 81  ? 0.1340 0.1028 0.0185 0.0180  0.0010  -0.0039 77  SER   A O   
726  C CB  . SER   A 81  ? 0.1453 0.1393 0.0924 0.0064  0.0415  -0.0514 77  SER   A CB  
727  O OG  . SER   A 81  ? 0.2418 0.1894 0.1615 0.0276  0.0353  0.0135  77  SER   A OG  
728  N N   A PRO   A 82  ? 0.1401 0.1120 0.0121 0.0044  0.0004  0.0099  78  PRO   A N   
729  N N   B PRO   A 82  ? 0.1417 0.1116 0.0121 0.0120  0.0061  0.0056  78  PRO   A N   
730  C CA  A PRO   A 82  ? 0.1287 0.1171 0.0230 0.0018  0.0133  0.0174  78  PRO   A CA  
731  C CA  B PRO   A 82  ? 0.1408 0.1169 0.0188 0.0126  0.0057  0.0084  78  PRO   A CA  
732  C C   A PRO   A 82  ? 0.1327 0.1004 0.0418 -0.0023 -0.0009 0.0095  78  PRO   A C   
733  C C   B PRO   A 82  ? 0.1468 0.1083 0.0118 0.0199  0.0005  -0.0098 78  PRO   A C   
734  O O   A PRO   A 82  ? 0.1247 0.0967 0.0287 0.0145  0.0062  -0.0022 78  PRO   A O   
735  O O   B PRO   A 82  ? 0.1439 0.1169 0.0064 0.0188  -0.0022 0.0029  78  PRO   A O   
736  C CB  A PRO   A 82  ? 0.1563 0.1457 0.0305 0.0083  0.0344  0.0194  78  PRO   A CB  
737  C CB  B PRO   A 82  ? 0.1429 0.1173 0.0207 0.0202  0.0097  0.0046  78  PRO   A CB  
738  C CG  A PRO   A 82  ? 0.1676 0.1591 0.0269 0.0186  0.0447  -0.0025 78  PRO   A CG  
739  C CG  B PRO   A 82  ? 0.1456 0.1098 0.0200 0.0277  0.0076  0.0081  78  PRO   A CG  
740  C CD  A PRO   A 82  ? 0.1643 0.1612 0.0107 0.0105  0.0161  0.0217  78  PRO   A CD  
741  C CD  B PRO   A 82  ? 0.1473 0.1212 0.0118 0.0226  0.0057  0.0096  78  PRO   A CD  
742  N N   A ASP   A 83  ? 0.1389 0.1109 0.0225 0.0017  0.0018  -0.0136 79  ASP   A N   
743  N N   B ASP   A 83  ? 0.1369 0.1101 0.0099 0.0197  0.0056  -0.0176 79  ASP   A N   
744  C CA  A ASP   A 83  ? 0.1459 0.1342 0.0416 0.0245  0.0166  0.0058  79  ASP   A CA  
745  C CA  B ASP   A 83  ? 0.1322 0.1058 0.0120 0.0236  0.0070  -0.0212 79  ASP   A CA  
746  C C   A ASP   A 83  ? 0.1315 0.1057 0.0371 0.0328  0.0046  -0.0117 79  ASP   A C   
747  C C   B ASP   A 83  ? 0.1281 0.1007 0.0080 0.0246  0.0017  -0.0117 79  ASP   A C   
748  O O   A ASP   A 83  ? 0.1327 0.1193 0.0848 0.0413  -0.0058 0.0258  79  ASP   A O   
749  O O   B ASP   A 83  ? 0.1485 0.1090 0.0065 0.0258  0.0021  0.0042  79  ASP   A O   
750  C CB  A ASP   A 83  ? 0.1889 0.1098 0.0760 0.0283  0.0111  0.0288  79  ASP   A CB  
751  C CB  B ASP   A 83  ? 0.1281 0.1068 0.0188 0.0184  0.0148  -0.0272 79  ASP   A CB  
752  C CG  A ASP   A 83  ? 0.2290 0.2350 0.1358 0.0208  0.0671  -0.0044 79  ASP   A CG  
753  C CG  B ASP   A 83  ? 0.1306 0.1202 0.0386 0.0194  0.0159  -0.0479 79  ASP   A CG  
754  O OD1 A ASP   A 83  ? 0.3176 0.2284 0.2160 -0.0304 0.1019  -0.0143 79  ASP   A OD1 
755  O OD1 B ASP   A 83  ? 0.1149 0.1135 0.0413 0.0035  0.0053  -0.0335 79  ASP   A OD1 
756  O OD2 A ASP   A 83  ? 0.3039 0.3248 0.2356 -0.0236 0.0538  -0.0574 79  ASP   A OD2 
757  O OD2 B ASP   A 83  ? 0.1284 0.1655 0.0396 0.0256  0.0351  -0.0523 79  ASP   A OD2 
758  N N   . TYR   A 84  ? 0.1209 0.0931 0.0081 0.0211  -0.0056 0.0017  80  TYR   A N   
759  C CA  . TYR   A 84  ? 0.1293 0.0855 0.0146 0.0093  0.0035  0.0081  80  TYR   A CA  
760  C C   . TYR   A 84  ? 0.1143 0.0875 0.0235 -0.0011 0.0097  0.0028  80  TYR   A C   
761  O O   . TYR   A 84  ? 0.1419 0.1027 0.0205 0.0010  0.0107  -0.0102 80  TYR   A O   
762  C CB  . TYR   A 84  ? 0.1122 0.1022 0.0307 0.0113  -0.0037 0.0033  80  TYR   A CB  
763  C CG  . TYR   A 84  ? 0.1313 0.0992 0.0330 0.0066  -0.0034 0.0011  80  TYR   A CG  
764  C CD1 . TYR   A 84  ? 0.1521 0.0966 0.0485 0.0149  -0.0041 -0.0065 80  TYR   A CD1 
765  C CD2 . TYR   A 84  ? 0.1565 0.0961 0.0258 0.0044  -0.0060 -0.0055 80  TYR   A CD2 
766  C CE1 . TYR   A 84  ? 0.1326 0.0960 0.0574 0.0064  -0.0001 -0.0069 80  TYR   A CE1 
767  C CE2 . TYR   A 84  ? 0.1571 0.0978 0.0425 0.0014  -0.0063 0.0096  80  TYR   A CE2 
768  C CZ  . TYR   A 84  ? 0.1313 0.0902 0.0608 -0.0001 -0.0086 -0.0018 80  TYR   A CZ  
769  O OH  . TYR   A 84  ? 0.1590 0.0912 0.0865 0.0015  -0.0136 0.0034  80  TYR   A OH  
770  N N   . ALA   A 85  ? 0.1211 0.0862 0.0283 0.0020  0.0289  -0.0019 81  ALA   A N   
771  C CA  . ALA   A 85  ? 0.1300 0.0866 0.0227 0.0049  0.0226  -0.0026 81  ALA   A CA  
772  C C   . ALA   A 85  ? 0.1256 0.0815 0.0164 0.0136  0.0140  -0.0026 81  ALA   A C   
773  O O   . ALA   A 85  ? 0.1289 0.0916 0.0285 0.0057  0.0089  0.0184  81  ALA   A O   
774  C CB  . ALA   A 85  ? 0.1011 0.0694 0.0464 0.0015  0.0324  -0.0032 81  ALA   A CB  
775  N N   . TYR   A 86  ? 0.1164 0.0809 0.0160 0.0035  -0.0027 0.0000  82  TYR   A N   
776  C CA  . TYR   A 86  ? 0.1308 0.0949 0.0231 -0.0098 -0.0010 -0.0006 82  TYR   A CA  
777  C C   . TYR   A 86  ? 0.1173 0.1030 0.0089 -0.0064 -0.0168 -0.0006 82  TYR   A C   
778  O O   . TYR   A 86  ? 0.1215 0.1264 0.0162 -0.0193 0.0024  -0.0116 82  TYR   A O   
779  C CB  . TYR   A 86  ? 0.1234 0.0965 0.0180 -0.0029 0.0049  0.0018  82  TYR   A CB  
780  C CG  . TYR   A 86  ? 0.1280 0.0915 0.0364 0.0070  0.0118  -0.0052 82  TYR   A CG  
781  C CD1 . TYR   A 86  ? 0.1261 0.1121 0.0326 0.0146  0.0165  -0.0176 82  TYR   A CD1 
782  C CD2 . TYR   A 86  ? 0.1281 0.0874 0.0685 0.0087  0.0142  0.0023  82  TYR   A CD2 
783  C CE1 . TYR   A 86  ? 0.1292 0.1189 0.0324 0.0048  0.0177  -0.0229 82  TYR   A CE1 
784  C CE2 . TYR   A 86  ? 0.1216 0.1034 0.0802 0.0138  0.0332  0.0076  82  TYR   A CE2 
785  C CZ  . TYR   A 86  ? 0.1351 0.1011 0.0483 0.0060  0.0494  0.0151  82  TYR   A CZ  
786  O OH  . TYR   A 86  ? 0.1793 0.1388 0.0575 0.0449  0.0568  0.0116  82  TYR   A OH  
787  N N   . GLY   A 87  ? 0.0971 0.1090 0.0393 0.0008  -0.0098 -0.0200 83  GLY   A N   
788  C CA  . GLY   A 87  ? 0.0997 0.1229 0.0545 0.0117  -0.0038 -0.0204 83  GLY   A CA  
789  C C   . GLY   A 87  ? 0.1282 0.1236 0.0249 0.0193  -0.0057 -0.0279 83  GLY   A C   
790  O O   . GLY   A 87  ? 0.1258 0.1421 0.0249 0.0285  0.0028  -0.0234 83  GLY   A O   
791  N N   . ALA   A 88  ? 0.1301 0.1466 0.0431 0.0229  0.0043  -0.0112 84  ALA   A N   
792  C CA  . ALA   A 88  ? 0.1388 0.1811 0.0311 0.0210  0.0046  0.0058  84  ALA   A CA  
793  C C   . ALA   A 88  ? 0.1482 0.1793 0.0326 0.0006  0.0283  0.0086  84  ALA   A C   
794  O O   . ALA   A 88  ? 0.1915 0.2063 0.0624 0.0061  0.0371  0.0334  84  ALA   A O   
795  C CB  . ALA   A 88  ? 0.1485 0.1777 0.0780 0.0252  0.0181  0.0012  84  ALA   A CB  
796  N N   . THR   A 89  ? 0.1346 0.1791 0.0411 0.0000  0.0172  -0.0099 85  THR   A N   
797  C CA  . THR   A 89  ? 0.1162 0.1889 0.0846 -0.0115 0.0211  -0.0183 85  THR   A CA  
798  C C   . THR   A 89  ? 0.1540 0.1363 0.0900 -0.0089 0.0368  -0.0013 85  THR   A C   
799  O O   . THR   A 89  ? 0.1976 0.1384 0.1676 -0.0244 0.0417  0.0275  85  THR   A O   
800  C CB  . THR   A 89  ? 0.1652 0.1998 0.1068 0.0044  -0.0187 -0.0390 85  THR   A CB  
801  O OG1 . THR   A 89  ? 0.1621 0.2543 0.0993 0.0182  -0.0232 -0.0564 85  THR   A OG1 
802  C CG2 . THR   A 89  ? 0.2065 0.2307 0.1176 -0.0091 -0.0107 -0.0700 85  THR   A CG2 
803  N N   . GLY   A 90  ? 0.1474 0.1022 0.0803 -0.0087 0.0201  0.0080  86  GLY   A N   
804  C CA  . GLY   A 90  ? 0.1355 0.1156 0.0670 -0.0066 0.0060  0.0107  86  GLY   A CA  
805  C C   . GLY   A 90  ? 0.1215 0.1084 0.0795 -0.0056 0.0000  0.0088  86  GLY   A C   
806  O O   . GLY   A 90  ? 0.1439 0.1165 0.0821 0.0045  -0.0007 0.0130  86  GLY   A O   
807  N N   . HIS   A 91  ? 0.1574 0.1082 0.0937 0.0092  -0.0126 0.0042  87  HIS   A N   
808  C CA  . HIS   A 91  ? 0.1579 0.1133 0.1047 -0.0226 0.0103  -0.0029 87  HIS   A CA  
809  C C   . HIS   A 91  ? 0.1388 0.1142 0.1393 -0.0030 0.0069  0.0151  87  HIS   A C   
810  O O   . HIS   A 91  ? 0.1545 0.1118 0.0910 0.0012  0.0008  -0.0034 87  HIS   A O   
811  C CB  . HIS   A 91  ? 0.1585 0.1044 0.1368 -0.0199 0.0233  0.0035  87  HIS   A CB  
812  C CG  . HIS   A 91  ? 0.1774 0.1931 0.0719 -0.0030 0.0215  0.0085  87  HIS   A CG  
813  N ND1 . HIS   A 91  ? 0.2591 0.2875 0.0856 -0.0076 0.0256  0.0326  87  HIS   A ND1 
814  C CD2 . HIS   A 91  ? 0.1837 0.1918 0.0883 -0.0038 0.0155  0.0207  87  HIS   A CD2 
815  C CE1 . HIS   A 91  ? 0.2762 0.3272 0.0205 0.0173  0.0100  0.0200  87  HIS   A CE1 
816  N NE2 . HIS   A 91  ? 0.2314 0.2379 0.1126 0.0075  0.0063  -0.0182 87  HIS   A NE2 
817  N N   A PRO   A 92  ? 0.1385 0.1554 0.2153 -0.0014 -0.0315 0.0783  88  PRO   A N   
818  N N   B PRO   A 92  ? 0.1333 0.0880 0.0927 0.0038  0.0084  -0.0041 88  PRO   A N   
819  C CA  A PRO   A 92  ? 0.1685 0.1904 0.2650 -0.0350 -0.0349 0.1030  88  PRO   A CA  
820  C CA  B PRO   A 92  ? 0.1047 0.1143 0.1165 -0.0136 -0.0011 0.0164  88  PRO   A CA  
821  C C   A PRO   A 92  ? 0.1639 0.2177 0.2489 -0.0301 -0.0626 0.0798  88  PRO   A C   
822  C C   B PRO   A 92  ? 0.1187 0.1282 0.1879 0.0030  -0.0152 0.0268  88  PRO   A C   
823  O O   A PRO   A 92  ? 0.2114 0.1270 0.2578 -0.0373 -0.1383 0.0511  88  PRO   A O   
824  O O   B PRO   A 92  ? 0.0722 0.1324 0.1716 -0.0192 -0.0649 0.0309  88  PRO   A O   
825  C CB  A PRO   A 92  ? 0.2097 0.2144 0.2633 -0.0422 -0.0533 0.1007  88  PRO   A CB  
826  C CB  B PRO   A 92  ? 0.0896 0.1007 0.1232 -0.0030 0.0114  0.0044  88  PRO   A CB  
827  C CG  A PRO   A 92  ? 0.1831 0.2290 0.2378 -0.0355 -0.0691 0.0871  88  PRO   A CG  
828  C CG  B PRO   A 92  ? 0.1127 0.0957 0.1129 -0.0009 0.0013  -0.0066 88  PRO   A CG  
829  C CD  A PRO   A 92  ? 0.1888 0.1850 0.1690 -0.0210 -0.0356 0.0694  88  PRO   A CD  
830  C CD  B PRO   A 92  ? 0.1181 0.0956 0.0830 0.0020  0.0114  -0.0164 88  PRO   A CD  
831  N N   . GLY   A 93  ? 0.1615 0.1799 0.2247 -0.0186 -0.0432 0.0646  89  GLY   A N   
832  C CA  . GLY   A 93  ? 0.1752 0.1382 0.1747 -0.0332 -0.0457 0.0167  89  GLY   A CA  
833  C C   . GLY   A 93  ? 0.1709 0.1452 0.1442 -0.0034 -0.0109 0.0132  89  GLY   A C   
834  O O   . GLY   A 93  ? 0.2098 0.1383 0.1380 0.0113  -0.0528 -0.0197 89  GLY   A O   
835  N N   . ILE   A 94  ? 0.1460 0.1239 0.1422 0.0172  -0.0059 0.0068  90  ILE   A N   
836  C CA  . ILE   A 94  ? 0.1296 0.1089 0.1514 0.0212  -0.0186 -0.0179 90  ILE   A CA  
837  C C   . ILE   A 94  ? 0.1222 0.1077 0.1175 0.0015  0.0213  -0.0076 90  ILE   A C   
838  O O   . ILE   A 94  ? 0.1362 0.1614 0.1621 0.0084  -0.0052 -0.0172 90  ILE   A O   
839  C CB  . ILE   A 94  ? 0.1561 0.1627 0.1506 0.0225  -0.0363 -0.0297 90  ILE   A CB  
840  C CG1 . ILE   A 94  ? 0.1901 0.1894 0.1851 0.0059  -0.0642 -0.0370 90  ILE   A CG1 
841  C CG2 . ILE   A 94  ? 0.1783 0.1873 0.0811 -0.0074 -0.0211 -0.0230 90  ILE   A CG2 
842  C CD1 . ILE   A 94  ? 0.2403 0.1877 0.2049 0.0119  -0.0446 -0.0252 90  ILE   A CD1 
843  N N   . ILE   A 95  ? 0.1276 0.0978 0.0960 -0.0020 0.0126  -0.0214 91  ILE   A N   
844  C CA  . ILE   A 95  ? 0.1535 0.1075 0.0840 -0.0110 0.0150  -0.0265 91  ILE   A CA  
845  C C   . ILE   A 95  ? 0.1334 0.0844 0.0905 -0.0170 0.0095  -0.0122 91  ILE   A C   
846  O O   . ILE   A 95  ? 0.1321 0.1175 0.0866 0.0011  0.0018  -0.0165 91  ILE   A O   
847  C CB  . ILE   A 95  ? 0.2021 0.1313 0.0602 -0.0336 0.0177  -0.0301 91  ILE   A CB  
848  C CG1 . ILE   A 95  ? 0.2397 0.1427 0.1085 -0.0085 0.0212  -0.0802 91  ILE   A CG1 
849  C CG2 . ILE   A 95  ? 0.1660 0.1164 0.0893 -0.0378 0.0456  -0.0228 91  ILE   A CG2 
850  C CD1 . ILE   A 95  ? 0.2559 0.1860 0.1180 -0.0026 0.0399  -0.0697 91  ILE   A CD1 
851  N N   . PRO   A 96  ? 0.1594 0.1277 0.0827 0.0010  0.0000  0.0038  92  PRO   A N   
852  C CA  . PRO   A 96  ? 0.1798 0.1596 0.0775 0.0059  0.0161  0.0015  92  PRO   A CA  
853  C C   . PRO   A 96  ? 0.1536 0.1529 0.0452 -0.0138 0.0137  0.0015  92  PRO   A C   
854  O O   . PRO   A 96  ? 0.1461 0.1514 0.0406 0.0001  0.0085  0.0179  92  PRO   A O   
855  C CB  . PRO   A 96  ? 0.2336 0.1963 0.0950 0.0285  0.0006  0.0336  92  PRO   A CB  
856  C CG  . PRO   A 96  ? 0.2498 0.2681 0.0852 -0.0048 -0.0022 0.0572  92  PRO   A CG  
857  C CD  . PRO   A 96  ? 0.1725 0.1669 0.0986 0.0055  -0.0059 0.0483  92  PRO   A CD  
858  N N   . PRO   A 97  ? 0.1542 0.1561 0.0648 -0.0060 0.0228  0.0032  93  PRO   A N   
859  C CA  . PRO   A 97  ? 0.1434 0.1695 0.0389 0.0050  0.0157  -0.0012 93  PRO   A CA  
860  C C   . PRO   A 97  ? 0.1306 0.1648 0.0245 0.0077  0.0167  0.0044  93  PRO   A C   
861  O O   . PRO   A 97  ? 0.1681 0.1845 0.0327 0.0120  -0.0022 0.0150  93  PRO   A O   
862  C CB  . PRO   A 97  ? 0.1395 0.1919 0.1414 0.0160  0.0507  0.0035  93  PRO   A CB  
863  C CG  . PRO   A 97  ? 0.1599 0.2026 0.1863 -0.0046 0.0357  0.0291  93  PRO   A CG  
864  C CD  . PRO   A 97  ? 0.1657 0.1687 0.1561 -0.0144 0.0284  0.0256  93  PRO   A CD  
865  N N   . HIS   A 98  ? 0.1470 0.1570 0.0088 0.0118  0.0163  -0.0083 94  HIS   A N   
866  C CA  . HIS   A 98  ? 0.1465 0.1489 0.0175 0.0166  0.0113  -0.0151 94  HIS   A CA  
867  C C   . HIS   A 98  ? 0.1445 0.1124 0.0277 0.0044  0.0103  -0.0280 94  HIS   A C   
868  O O   . HIS   A 98  ? 0.1551 0.2036 0.0520 0.0008  -0.0084 -0.0550 94  HIS   A O   
869  C CB  . HIS   A 98  ? 0.1825 0.1953 0.0469 0.0190  0.0372  -0.0470 94  HIS   A CB  
870  C CG  . HIS   A 98  ? 0.1894 0.2733 0.0338 0.0266  0.0214  -0.0603 94  HIS   A CG  
871  N ND1 . HIS   A 98  ? 0.2044 0.2626 0.1251 0.0539  -0.0045 -0.1100 94  HIS   A ND1 
872  C CD2 . HIS   A 98  ? 0.2384 0.3193 0.0656 0.0017  0.0482  -0.1003 94  HIS   A CD2 
873  C CE1 . HIS   A 98  ? 0.1903 0.2760 0.0846 0.0707  -0.0459 -0.1018 94  HIS   A CE1 
874  N NE2 . HIS   A 98  ? 0.2550 0.3390 0.1076 0.0291  0.0543  -0.1045 94  HIS   A NE2 
875  N N   . ALA   A 99  ? 0.1316 0.1390 0.0128 -0.0094 0.0146  -0.0262 95  ALA   A N   
876  C CA  . ALA   A 99  ? 0.1305 0.1325 0.0201 -0.0045 0.0073  -0.0094 95  ALA   A CA  
877  C C   . ALA   A 99  ? 0.1127 0.1199 0.0187 0.0043  0.0000  -0.0074 95  ALA   A C   
878  O O   . ALA   A 99  ? 0.1257 0.1296 0.0189 0.0006  -0.0033 -0.0058 95  ALA   A O   
879  C CB  . ALA   A 99  ? 0.1388 0.1281 0.0388 0.0023  -0.0001 -0.0119 95  ALA   A CB  
880  N N   . THR   A 100 ? 0.1091 0.1202 0.0074 0.0022  0.0050  -0.0068 96  THR   A N   
881  C CA  . THR   A 100 ? 0.0954 0.1289 0.0152 0.0098  -0.0025 -0.0008 96  THR   A CA  
882  C C   . THR   A 100 ? 0.1101 0.1141 0.0290 0.0123  0.0010  0.0033  96  THR   A C   
883  O O   . THR   A 100 ? 0.1473 0.1202 0.0358 0.0205  0.0040  0.0036  96  THR   A O   
884  C CB  . THR   A 100 ? 0.1266 0.1346 0.0330 -0.0024 -0.0054 -0.0157 96  THR   A CB  
885  O OG1 . THR   A 100 ? 0.1614 0.1556 0.0936 0.0146  -0.0074 -0.0540 96  THR   A OG1 
886  C CG2 . THR   A 100 ? 0.1071 0.1396 0.0784 -0.0003 -0.0081 -0.0251 96  THR   A CG2 
887  N N   . LEU   A 101 ? 0.1137 0.0931 0.0329 0.0001  0.0103  -0.0026 97  LEU   A N   
888  C CA  . LEU   A 101 ? 0.1289 0.0883 0.0069 0.0031  0.0003  -0.0033 97  LEU   A CA  
889  C C   . LEU   A 101 ? 0.1198 0.0783 0.0132 0.0091  -0.0066 -0.0032 97  LEU   A C   
890  O O   . LEU   A 101 ? 0.1227 0.0796 0.0695 0.0083  0.0024  -0.0047 97  LEU   A O   
891  C CB  . LEU   A 101 ? 0.1112 0.0908 0.0355 0.0065  -0.0132 -0.0238 97  LEU   A CB  
892  C CG  . LEU   A 101 ? 0.1067 0.1073 0.0582 0.0127  -0.0046 -0.0227 97  LEU   A CG  
893  C CD1 . LEU   A 101 ? 0.1102 0.1197 0.0635 -0.0022 -0.0100 -0.0183 97  LEU   A CD1 
894  C CD2 . LEU   A 101 ? 0.1036 0.1079 0.0561 0.0070  0.0063  -0.0274 97  LEU   A CD2 
895  N N   . VAL   A 102 ? 0.1157 0.0868 0.0197 0.0080  -0.0067 0.0025  98  VAL   A N   
896  C CA  . VAL   A 102 ? 0.1256 0.0854 0.0150 0.0015  -0.0007 0.0013  98  VAL   A CA  
897  C C   . VAL   A 102 ? 0.1266 0.0775 0.0370 0.0071  0.0166  -0.0049 98  VAL   A C   
898  O O   . VAL   A 102 ? 0.2287 0.0808 0.0469 0.0024  0.0475  -0.0065 98  VAL   A O   
899  C CB  . VAL   A 102 ? 0.1442 0.1244 0.0215 0.0164  -0.0061 0.0042  98  VAL   A CB  
900  C CG1 . VAL   A 102 ? 0.1495 0.1570 0.0928 -0.0021 -0.0064 0.0147  98  VAL   A CG1 
901  C CG2 . VAL   A 102 ? 0.1702 0.1639 0.0143 0.0133  -0.0234 -0.0127 98  VAL   A CG2 
902  N N   . PHE   A 103 ? 0.1118 0.0847 0.0159 0.0052  -0.0009 -0.0093 99  PHE   A N   
903  C CA  . PHE   A 103 ? 0.1230 0.0822 0.0225 0.0024  0.0064  -0.0122 99  PHE   A CA  
904  C C   . PHE   A 103 ? 0.1191 0.0868 0.0403 0.0008  0.0038  -0.0092 99  PHE   A C   
905  O O   . PHE   A 103 ? 0.1362 0.0983 0.1089 -0.0120 0.0289  -0.0390 99  PHE   A O   
906  C CB  . PHE   A 103 ? 0.1366 0.0746 0.0241 -0.0013 0.0041  -0.0026 99  PHE   A CB  
907  C CG  . PHE   A 103 ? 0.1329 0.0890 0.0088 -0.0023 0.0051  0.0060  99  PHE   A CG  
908  C CD1 . PHE   A 103 ? 0.1330 0.0963 0.0229 0.0010  0.0140  0.0174  99  PHE   A CD1 
909  C CD2 . PHE   A 103 ? 0.1252 0.0971 0.0127 0.0059  -0.0257 0.0076  99  PHE   A CD2 
910  C CE1 . PHE   A 103 ? 0.1265 0.1025 0.0230 0.0122  0.0050  0.0052  99  PHE   A CE1 
911  C CE2 . PHE   A 103 ? 0.1331 0.0876 0.0252 0.0068  -0.0131 0.0091  99  PHE   A CE2 
912  C CZ  . PHE   A 103 ? 0.1247 0.1026 0.0178 0.0009  0.0012  0.0181  99  PHE   A CZ  
913  N N   . ASP   A 104 ? 0.1091 0.0819 0.0113 -0.0010 -0.0003 0.0006  100 ASP   A N   
914  C CA  . ASP   A 104 ? 0.1193 0.0899 0.0066 -0.0139 0.0030  -0.0045 100 ASP   A CA  
915  C C   . ASP   A 104 ? 0.1178 0.0793 0.0076 -0.0108 0.0050  -0.0092 100 ASP   A C   
916  O O   . ASP   A 104 ? 0.1523 0.0874 0.0242 -0.0268 -0.0171 -0.0040 100 ASP   A O   
917  C CB  . ASP   A 104 ? 0.1240 0.1227 0.0311 -0.0021 -0.0057 0.0183  100 ASP   A CB  
918  C CG  . ASP   A 104 ? 0.1401 0.1230 0.1073 0.0058  0.0206  0.0398  100 ASP   A CG  
919  O OD1 . ASP   A 104 ? 0.1507 0.1754 0.1270 0.0141  0.0366  0.0676  100 ASP   A OD1 
920  O OD2 . ASP   A 104 ? 0.1432 0.2740 0.2072 0.0381  0.0263  0.1230  100 ASP   A OD2 
921  N N   A VAL   A 105 ? 0.1204 0.0817 0.0073 -0.0177 -0.0020 -0.0080 101 VAL   A N   
922  N N   B VAL   A 105 ? 0.1272 0.0825 0.0074 -0.0219 0.0000  -0.0090 101 VAL   A N   
923  C CA  A VAL   A 105 ? 0.1171 0.1004 0.0088 -0.0123 -0.0024 -0.0149 101 VAL   A CA  
924  C CA  B VAL   A 105 ? 0.1286 0.1070 0.0095 -0.0202 -0.0009 -0.0174 101 VAL   A CA  
925  C C   A VAL   A 105 ? 0.1242 0.0899 0.0067 -0.0135 -0.0004 -0.0059 101 VAL   A C   
926  C C   B VAL   A 105 ? 0.1311 0.0918 0.0068 -0.0160 -0.0005 -0.0066 101 VAL   A C   
927  O O   A VAL   A 105 ? 0.1292 0.1053 0.0248 -0.0231 0.0031  -0.0144 101 VAL   A O   
928  O O   B VAL   A 105 ? 0.1342 0.1092 0.0201 -0.0274 0.0036  -0.0128 101 VAL   A O   
929  C CB  A VAL   A 105 ? 0.1298 0.1156 0.0093 -0.0001 -0.0095 -0.0024 101 VAL   A CB  
930  C CB  B VAL   A 105 ? 0.1522 0.1320 0.0177 -0.0016 -0.0108 0.0042  101 VAL   A CB  
931  C CG1 A VAL   A 105 ? 0.1322 0.1195 0.0092 0.0135  -0.0094 -0.0005 101 VAL   A CG1 
932  C CG1 B VAL   A 105 ? 0.1646 0.1400 0.0580 -0.0260 -0.0134 0.0035  101 VAL   A CG1 
933  C CG2 A VAL   A 105 ? 0.1300 0.0856 0.0477 -0.0111 -0.0030 0.0073  101 VAL   A CG2 
934  C CG2 B VAL   A 105 ? 0.1800 0.1176 0.0696 0.0050  -0.0209 0.0134  101 VAL   A CG2 
935  N N   . GLU   A 106 ? 0.1268 0.1096 0.0096 -0.0231 -0.0011 -0.0179 102 GLU   A N   
936  C CA  . GLU   A 106 ? 0.1299 0.1177 0.0112 -0.0240 -0.0013 -0.0009 102 GLU   A CA  
937  C C   . GLU   A 106 ? 0.1202 0.0968 0.0144 -0.0134 -0.0003 -0.0040 102 GLU   A C   
938  O O   . GLU   A 106 ? 0.1238 0.1139 0.0076 -0.0212 0.0019  -0.0052 102 GLU   A O   
939  C CB  . GLU   A 106 ? 0.1354 0.1696 0.0288 0.0018  -0.0101 0.0108  102 GLU   A CB  
940  C CG  . GLU   A 106 ? 0.1355 0.2381 0.0601 -0.0068 -0.0015 -0.0066 102 GLU   A CG  
941  C CD  . GLU   A 106 ? 0.1945 0.2757 0.1909 0.0271  0.0233  -0.0009 102 GLU   A CD  
942  O OE1 . GLU   A 106 ? 0.1794 0.3517 0.2307 0.0006  0.0328  -0.0332 102 GLU   A OE1 
943  O OE2 . GLU   A 106 ? 0.2937 0.3351 0.2931 0.1223  0.0186  0.0583  102 GLU   A OE2 
944  N N   . LEU   A 107 ? 0.1420 0.1105 0.0063 -0.0284 0.0009  -0.0008 103 LEU   A N   
945  C CA  . LEU   A 107 ? 0.1570 0.1264 0.0066 -0.0189 -0.0069 0.0026  103 LEU   A CA  
946  C C   . LEU   A 107 ? 0.1377 0.1230 0.0215 -0.0389 -0.0035 -0.0101 103 LEU   A C   
947  O O   . LEU   A 107 ? 0.1427 0.1420 0.0376 -0.0489 -0.0043 -0.0059 103 LEU   A O   
948  C CB  . LEU   A 107 ? 0.1467 0.1151 0.0187 -0.0303 0.0025  -0.0049 103 LEU   A CB  
949  C CG  . LEU   A 107 ? 0.1435 0.1245 0.0370 -0.0241 0.0073  0.0191  103 LEU   A CG  
950  C CD1 . LEU   A 107 ? 0.1469 0.1166 0.0566 -0.0174 -0.0026 0.0098  103 LEU   A CD1 
951  C CD2 . LEU   A 107 ? 0.1568 0.1228 0.0779 -0.0239 0.0012  0.0353  103 LEU   A CD2 
952  N N   . LEU   A 108 ? 0.1232 0.1165 0.0441 -0.0198 -0.0057 -0.0227 104 LEU   A N   
953  C CA  . LEU   A 108 ? 0.1575 0.1263 0.0265 -0.0107 0.0106  -0.0113 104 LEU   A CA  
954  C C   . LEU   A 108 ? 0.1601 0.1320 0.0326 -0.0068 0.0250  -0.0062 104 LEU   A C   
955  O O   . LEU   A 108 ? 0.1639 0.1591 0.0562 0.0006  0.0349  -0.0173 104 LEU   A O   
956  C CB  . LEU   A 108 ? 0.1546 0.1249 0.0258 -0.0129 0.0037  -0.0032 104 LEU   A CB  
957  C CG  . LEU   A 108 ? 0.2008 0.1179 0.0269 0.0001  -0.0136 -0.0044 104 LEU   A CG  
958  C CD1 . LEU   A 108 ? 0.2134 0.1519 0.0527 -0.0296 -0.0223 -0.0066 104 LEU   A CD1 
959  C CD2 . LEU   A 108 ? 0.2207 0.1766 0.1047 -0.0016 -0.0325 0.0361  104 LEU   A CD2 
960  N N   . LYS   A 109 ? 0.1545 0.1390 0.0122 -0.0057 0.0279  -0.0105 105 LYS   A N   
961  C CA  . LYS   A 109 ? 0.1701 0.1485 0.0127 -0.0100 0.0322  -0.0002 105 LYS   A CA  
962  C C   . LYS   A 109 ? 0.1691 0.1314 0.0087 -0.0113 0.0179  0.0065  105 LYS   A C   
963  O O   . LYS   A 109 ? 0.1698 0.1424 0.0403 -0.0201 0.0330  0.0070  105 LYS   A O   
964  C CB  . LYS   A 109 ? 0.2131 0.1484 0.0224 -0.0066 0.0303  -0.0027 105 LYS   A CB  
965  C CG  . LYS   A 109 ? 0.2646 0.1961 0.0197 -0.0334 0.0344  -0.0110 105 LYS   A CG  
966  C CD  . LYS   A 109 ? 0.3005 0.1941 0.0486 -0.0340 0.0566  -0.0244 105 LYS   A CD  
967  C CE  . LYS   A 109 ? 0.4350 0.2791 0.0582 -0.0068 0.0163  -0.0312 105 LYS   A CE  
968  N NZ  . LYS   A 109 ? 0.4795 0.3056 0.1732 0.0047  0.0530  -0.0178 105 LYS   A NZ  
969  N N   . LEU   A 110 ? 0.1977 0.1792 0.0143 -0.0165 0.0279  0.0235  106 LEU   A N   
970  C CA  . LEU   A 110 ? 0.1902 0.1811 0.0474 -0.0187 0.0284  0.0101  106 LEU   A CA  
971  C C   . LEU   A 110 ? 0.2459 0.2291 0.0289 -0.0174 0.0241  0.0236  106 LEU   A C   
972  O O   . LEU   A 110 ? 0.2740 0.3072 0.0497 0.0075  0.0402  0.0165  106 LEU   A O   
973  C CB  . LEU   A 110 ? 0.1858 0.1761 0.1067 -0.0135 0.0595  0.0201  106 LEU   A CB  
974  C CG  . LEU   A 110 ? 0.1774 0.1656 0.1611 -0.0036 -0.0047 -0.0126 106 LEU   A CG  
975  C CD1 . LEU   A 110 ? 0.2006 0.1795 0.2436 -0.0367 0.0321  -0.0352 106 LEU   A CD1 
976  C CD2 . LEU   A 110 ? 0.3314 0.1801 0.0991 -0.0302 0.0641  -0.0141 106 LEU   A CD2 
977  N N   . GLU   A 111 ? 0.2665 0.2930 0.0286 -0.0362 0.0316  0.0315  107 GLU   A N   
978  C CA  . GLU   A 111 ? 0.3968 0.3504 0.0275 0.0008  -0.0013 0.0134  107 GLU   A CA  
979  C C   . GLU   A 111 ? 0.3946 0.4330 0.0878 -0.0229 -0.0511 0.0547  107 GLU   A C   
980  O O   . GLU   A 111 ? 0.3106 0.4474 0.1664 -0.0377 -0.0087 0.1158  107 GLU   A O   
981  C CB  . GLU   A 111 ? 0.4989 0.3620 0.1001 -0.0370 -0.0037 -0.0371 107 GLU   A CB  
982  C CG  . GLU   A 111 ? 0.5986 0.4182 0.0467 0.0030  -0.0645 -0.0848 107 GLU   A CG  
983  C CD  . GLU   A 111 ? 0.6510 0.4227 0.1452 -0.0726 0.0287  -0.0875 107 GLU   A CD  
984  O OE1 . GLU   A 111 ? 0.6571 0.3501 0.0743 -0.0704 0.0300  -0.0576 107 GLU   A OE1 
985  O OE2 . GLU   A 111 ? 0.7094 0.5578 0.2520 0.0343  0.1229  0.0848  107 GLU   A OE2 
986  O OXT . GLU   A 111 ? 0.6137 0.5826 0.1556 -0.0472 -0.1500 -0.0276 107 GLU   A OXT 
987  C C1  . A1L7S B .   ? 0.1427 0.1171 0.0362 -0.0003 0.0325  -0.0146 201 A1L7S A C1  
988  C C3  . A1L7S B .   ? 0.1557 0.1826 0.0786 0.0109  0.0182  -0.0019 201 A1L7S A C3  
989  C C12 . A1L7S B .   ? 0.1417 0.1849 0.1000 0.0042  0.0001  -0.0163 201 A1L7S A C12 
990  C C13 . A1L7S B .   ? 0.1602 0.1133 0.0551 -0.0141 0.0235  -0.0072 201 A1L7S A C13 
991  C C14 . A1L7S B .   ? 0.1279 0.1118 0.0694 -0.0069 0.0396  0.0028  201 A1L7S A C14 
992  C C15 . A1L7S B .   ? 0.1216 0.1266 0.0482 0.0112  0.0214  -0.0051 201 A1L7S A C15 
993  C C16 . A1L7S B .   ? 0.1588 0.1289 0.0310 0.0083  0.0303  0.0062  201 A1L7S A C16 
994  C C17 . A1L7S B .   ? 0.1576 0.1714 0.0792 0.0032  -0.0135 -0.0199 201 A1L7S A C17 
995  C C18 . A1L7S B .   ? 0.1294 0.1726 0.0930 0.0100  -0.0474 -0.0173 201 A1L7S A C18 
996  C C19 . A1L7S B .   ? 0.1273 0.1479 0.0949 0.0165  -0.0267 -0.0026 201 A1L7S A C19 
997  C C25 . A1L7S B .   ? 0.1322 0.0965 0.0643 0.0134  0.0028  0.0094  201 A1L7S A C25 
998  C C26 . A1L7S B .   ? 0.1780 0.1436 0.0834 -0.0150 0.0030  0.0355  201 A1L7S A C26 
999  C C27 . A1L7S B .   ? 0.1938 0.1532 0.1254 -0.0236 0.0378  0.0347  201 A1L7S A C27 
1000 C C28 . A1L7S B .   ? 0.2067 0.1285 0.1491 -0.0231 0.0302  0.0380  201 A1L7S A C28 
1001 C C29 . A1L7S B .   ? 0.1917 0.1059 0.1160 -0.0184 0.0043  -0.0038 201 A1L7S A C29 
1002 O O24 . A1L7S B .   ? 0.1381 0.1324 0.0300 -0.0067 0.0075  -0.0090 201 A1L7S A O24 
1003 S S22 . A1L7S B .   ? 0.1211 0.1191 0.0390 0.0058  0.0102  0.0000  201 A1L7S A S22 
1004 O O23 . A1L7S B .   ? 0.1308 0.1368 0.0886 0.0139  0.0088  0.0110  201 A1L7S A O23 
1005 C C30 . A1L7S B .   ? 0.1566 0.0983 0.0708 0.0069  0.0168  0.0039  201 A1L7S A C30 
1006 N N2  . A1L7S B .   ? 0.1542 0.1206 0.0393 0.0136  0.0307  0.0059  201 A1L7S A N2  
1007 O O6  . A1L7S B .   ? 0.1717 0.2396 0.0904 -0.0217 -0.0051 -0.0116 201 A1L7S A O6  
1008 N N7  . A1L7S B .   ? 0.2150 0.2462 0.1912 0.0408  -0.0143 -0.0272 201 A1L7S A N7  
1009 C C8  . A1L7S B .   ? 0.1609 0.2274 0.1956 0.0151  0.0267  0.0029  201 A1L7S A C8  
1010 N N5  . A1L7S B .   ? 0.1844 0.2488 0.0436 0.0666  0.0064  0.0081  201 A1L7S A N5  
1011 C C9  . A1L7S B .   ? 0.1595 0.2155 0.1317 0.0061  -0.0035 -0.0507 201 A1L7S A C9  
1012 C C10 . A1L7S B .   ? 0.1720 0.2018 0.1399 -0.0324 -0.0330 -0.0617 201 A1L7S A C10 
1013 C C11 . A1L7S B .   ? 0.1613 0.2102 0.1332 -0.0300 -0.0208 -0.0482 201 A1L7S A C11 
1014 C C21 . A1L7S B .   ? 0.1379 0.1782 0.1115 -0.0016 0.0001  -0.0376 201 A1L7S A C21 
1015 C C20 . A1L7S B .   ? 0.1241 0.1657 0.0768 0.0012  -0.0147 -0.0154 201 A1L7S A C20 
1016 O O33 . A1L7S B .   ? 0.1338 0.1756 0.0845 0.0058  0.0006  -0.0212 201 A1L7S A O33 
1017 C C34 . A1L7S B .   ? 0.1296 0.2367 0.0844 -0.0217 0.0018  -0.0117 201 A1L7S A C34 
1018 O O31 . A1L7S B .   ? 0.1338 0.1582 0.0874 0.0066  -0.0073 -0.0063 201 A1L7S A O31 
1019 C C32 . A1L7S B .   ? 0.1157 0.1517 0.1382 0.0153  -0.0133 0.0220  201 A1L7S A C32 
1020 C C1  . GOL   C .   ? 0.1528 0.1325 0.1324 0.0201  -0.0188 0.0215  202 GOL   A C1  
1021 O O1  . GOL   C .   ? 0.2137 0.1888 0.0705 0.0387  -0.0075 0.0089  202 GOL   A O1  
1022 C C2  . GOL   C .   ? 0.1703 0.1487 0.0873 -0.0031 -0.0045 -0.0081 202 GOL   A C2  
1023 O O2  . GOL   C .   ? 0.2020 0.1357 0.1229 0.0253  -0.0057 0.0027  202 GOL   A O2  
1024 C C3  . GOL   C .   ? 0.1910 0.1713 0.0793 0.0244  -0.0153 -0.0030 202 GOL   A C3  
1025 O O3  . GOL   C .   ? 0.1506 0.1394 0.1115 0.0005  -0.0156 0.0082  202 GOL   A O3  
1026 C C1  . GOL   D .   ? 0.2320 0.2149 0.1655 -0.0566 -0.0481 0.0474  203 GOL   A C1  
1027 O O1  . GOL   D .   ? 0.3403 0.3199 0.2464 -0.0399 -0.1439 0.0614  203 GOL   A O1  
1028 C C2  . GOL   D .   ? 0.2415 0.1669 0.0643 -0.0478 -0.0296 0.0607  203 GOL   A C2  
1029 O O2  . GOL   D .   ? 0.1946 0.1388 0.0520 -0.0107 0.0010  0.0170  203 GOL   A O2  
1030 C C3  . GOL   D .   ? 0.2456 0.1607 0.0761 -0.0263 -0.0028 0.0696  203 GOL   A C3  
1031 O O3  . GOL   D .   ? 0.2279 0.1951 0.0971 0.0238  0.0171  0.0605  203 GOL   A O3  
1032 O O   . HOH   E .   ? 0.3698 0.3322 0.3185 0.0700  -0.1527 -0.1797 301 HOH   A O   
1033 O O   . HOH   E .   ? 0.2278 0.1952 0.3790 0.0314  -0.0271 0.0284  302 HOH   A O   
1034 O O   . HOH   E .   ? 0.1997 0.7682 0.5632 0.0567  0.0128  0.0482  303 HOH   A O   
1035 O O   . HOH   E .   ? 0.7345 0.3278 0.2042 0.0654  -0.0808 -0.0199 304 HOH   A O   
1036 O O   . HOH   E .   ? 0.6233 0.2386 0.3658 0.0540  0.2923  0.0500  305 HOH   A O   
1037 O O   . HOH   E .   ? 0.8070 0.5932 0.3168 -0.1309 0.0467  -0.2223 306 HOH   A O   
1038 O O   . HOH   E .   ? 0.6538 1.1725 2.4415 0.5306  -0.2592 1.0934  307 HOH   A O   
1039 O O   A HOH   E .   ? 0.2845 0.3460 0.1228 -0.0228 -0.1070 0.0290  308 HOH   A O   
1040 O O   B HOH   E .   ? 0.3504 0.3513 0.1488 0.0855  -0.2213 -0.0592 308 HOH   A O   
1041 O O   . HOH   E .   ? 0.2130 0.1889 0.1161 -0.0121 -0.0582 -0.0128 309 HOH   A O   
1042 O O   . HOH   E .   ? 0.3243 0.4764 0.2265 -0.0529 -0.0743 0.0674  310 HOH   A O   
1043 O O   . HOH   E .   ? 0.2898 0.6825 0.3480 0.1063  0.0200  -0.0578 311 HOH   A O   
1044 O O   . HOH   E .   ? 0.6163 0.2502 0.5055 -0.1374 0.2156  -0.1537 312 HOH   A O   
1045 O O   . HOH   E .   ? 0.2552 0.4393 0.4211 -0.0597 0.1122  -0.0141 313 HOH   A O   
1046 O O   . HOH   E .   ? 0.5219 0.3137 0.3968 -0.1150 0.1494  0.0387  314 HOH   A O   
1047 O O   . HOH   E .   ? 0.1438 0.1815 0.0698 -0.0265 -0.0040 -0.0320 315 HOH   A O   
1048 O O   . HOH   E .   ? 0.5323 0.4140 0.7544 -0.0784 0.2997  0.0109  316 HOH   A O   
1049 O O   A HOH   E .   ? 0.2283 0.1662 0.0626 0.0588  0.0369  0.0396  317 HOH   A O   
1050 O O   B HOH   E .   ? 0.0666 0.3018 0.4871 0.0165  0.1643  0.1424  317 HOH   A O   
1051 O O   A HOH   E .   ? 0.1250 0.1876 0.1550 -0.0280 -0.0522 -0.0025 318 HOH   A O   
1052 O O   B HOH   E .   ? 0.5881 0.0846 0.4483 0.0936  0.1466  -0.0081 318 HOH   A O   
1053 O O   . HOH   E .   ? 0.3355 0.3793 0.5643 -0.0522 -0.0996 0.0158  319 HOH   A O   
1054 O O   . HOH   E .   ? 0.2185 0.2206 0.0654 0.0382  -0.0120 0.0148  320 HOH   A O   
1055 O O   . HOH   E .   ? 0.7321 0.3095 0.0841 -0.0235 -0.0407 -0.0233 321 HOH   A O   
1056 O O   . HOH   E .   ? 0.1646 0.1740 0.0422 0.0103  -0.0103 0.0126  322 HOH   A O   
1057 O O   . HOH   E .   ? 0.2290 0.2271 0.1764 -0.0376 -0.0622 0.0893  323 HOH   A O   
1058 O O   . HOH   E .   ? 0.6456 0.4917 0.2994 -0.2810 -0.0868 0.0754  324 HOH   A O   
1059 O O   . HOH   E .   ? 0.4679 0.4148 0.2754 -0.1019 0.1339  -0.0262 325 HOH   A O   
1060 O O   . HOH   E .   ? 0.2104 0.1745 0.1344 0.0238  0.0347  0.0016  326 HOH   A O   
1061 O O   . HOH   E .   ? 0.3409 0.1841 0.2212 -0.0340 0.0258  -0.0144 327 HOH   A O   
1062 O O   . HOH   E .   ? 0.3723 0.5613 0.3360 -0.1098 0.1709  0.1113  328 HOH   A O   
1063 O O   . HOH   E .   ? 0.2538 0.1994 0.1916 -0.0140 0.0096  -0.0706 329 HOH   A O   
1064 O O   A HOH   E .   ? 0.2342 0.1473 0.0706 -0.1080 0.0674  -0.0139 330 HOH   A O   
1065 O O   B HOH   E .   ? 0.2674 0.1970 0.0972 -0.0194 0.0766  -0.0678 330 HOH   A O   
1066 O O   . HOH   E .   ? 0.2275 0.2927 0.0999 0.0096  0.0271  -0.0486 331 HOH   A O   
1067 O O   . HOH   E .   ? 0.3553 0.3536 0.7197 -0.0564 0.2161  0.2083  332 HOH   A O   
1068 O O   . HOH   E .   ? 0.1629 0.1047 0.0777 -0.0036 -0.0089 0.0169  333 HOH   A O   
1069 O O   . HOH   E .   ? 0.2438 0.1490 0.1426 -0.0194 -0.0581 0.0142  334 HOH   A O   
1070 O O   . HOH   E .   ? 0.3416 0.2519 0.3108 0.0049  -0.0321 -0.0208 335 HOH   A O   
1071 O O   . HOH   E .   ? 0.1928 0.1494 0.0603 0.0213  -0.0410 -0.0248 336 HOH   A O   
1072 O O   . HOH   E .   ? 0.2483 0.2541 0.1889 -0.0278 0.0368  -0.0204 337 HOH   A O   
1073 O O   . HOH   E .   ? 0.4134 0.4949 0.1290 -0.0560 0.0432  -0.1137 338 HOH   A O   
1074 O O   . HOH   E .   ? 0.1516 0.1037 0.0435 -0.0024 0.0314  -0.0021 339 HOH   A O   
1075 O O   . HOH   E .   ? 0.4152 0.3069 0.4083 -0.0145 0.0695  -0.1108 340 HOH   A O   
1076 O O   A HOH   E .   ? 0.2847 0.2239 0.0231 0.0265  -0.0020 0.0101  341 HOH   A O   
1077 O O   B HOH   E .   ? 0.6388 0.6002 0.1848 0.3799  0.1384  0.2450  341 HOH   A O   
1078 O O   A HOH   E .   ? 0.1675 0.1886 0.1022 0.0621  -0.0057 -0.0295 342 HOH   A O   
1079 O O   B HOH   E .   ? 0.2305 0.0890 0.1231 0.0044  0.1195  -0.0133 342 HOH   A O   
1080 O O   . HOH   E .   ? 0.3816 0.2942 0.1401 -0.0804 0.0271  0.0420  343 HOH   A O   
1081 O O   A HOH   E .   ? 0.3144 0.3934 0.1152 0.0225  0.0323  -0.0146 344 HOH   A O   
1082 O O   B HOH   E .   ? 0.3019 0.6307 0.2874 0.1612  0.0518  -0.0128 344 HOH   A O   
1083 O O   . HOH   E .   ? 0.3630 0.2996 0.3114 0.0112  -0.0513 0.1988  345 HOH   A O   
1084 O O   . HOH   E .   ? 0.2432 0.2981 0.2540 -0.0343 0.0407  0.0777  346 HOH   A O   
1085 O O   . HOH   E .   ? 0.3420 0.3636 0.2632 -0.0963 0.0881  -0.1604 347 HOH   A O   
1086 O O   . HOH   E .   ? 0.6599 0.5700 0.7554 -0.1933 0.1383  0.1410  348 HOH   A O   
1087 O O   . HOH   E .   ? 0.3532 0.4371 0.3494 0.0443  0.0838  -0.2897 349 HOH   A O   
1088 O O   . HOH   E .   ? 0.4045 0.5052 0.8930 -0.0733 -0.1031 0.1121  350 HOH   A O   
1089 O O   . HOH   E .   ? 0.1341 0.1348 0.0559 0.0023  -0.0130 -0.0088 351 HOH   A O   
1090 O O   . HOH   E .   ? 0.3110 0.1918 0.1560 -0.0250 -0.0163 0.0479  352 HOH   A O   
1091 O O   A HOH   E .   ? 0.3887 0.4601 0.0329 -0.1046 0.0959  0.0070  353 HOH   A O   
1092 O O   B HOH   E .   ? 0.3007 0.3126 0.5406 0.0114  0.1462  -0.2094 353 HOH   A O   
1093 O O   . HOH   E .   ? 0.6063 0.3231 0.2405 0.0942  0.1259  -0.0058 354 HOH   A O   
1094 O O   A HOH   E .   ? 0.2901 0.1426 0.2150 0.0150  0.0719  -0.0137 355 HOH   A O   
1095 O O   B HOH   E .   ? 0.4083 0.2907 0.3469 0.0035  0.0265  -0.0661 355 HOH   A O   
1096 O O   A HOH   E .   ? 0.1658 0.0699 0.0432 0.0092  0.0281  0.0350  356 HOH   A O   
1097 O O   B HOH   E .   ? 0.2065 0.1768 0.0974 0.0513  0.0437  -0.0107 356 HOH   A O   
1098 O O   . HOH   E .   ? 0.1698 0.1744 0.1262 0.0178  -0.0128 -0.0183 357 HOH   A O   
1099 O O   . HOH   E .   ? 0.2819 0.2305 0.2041 0.0373  -0.0296 -0.0475 358 HOH   A O   
1100 O O   A HOH   E .   ? 0.2296 0.0714 0.3175 -0.0045 -0.0495 0.0429  359 HOH   A O   
1101 O O   B HOH   E .   ? 0.3215 0.1922 0.3430 -0.0107 -0.0194 -0.0313 359 HOH   A O   
1102 O O   . HOH   E .   ? 0.1283 0.1121 0.0203 0.0001  -0.0130 0.0121  360 HOH   A O   
1103 O O   . HOH   E .   ? 0.3029 0.3359 0.2198 -0.0031 0.0426  0.0164  361 HOH   A O   
1104 O O   . HOH   E .   ? 0.6734 0.3716 0.1846 -0.0691 0.0662  -0.0251 362 HOH   A O   
1105 O O   . HOH   E .   ? 0.2115 0.2378 0.3154 0.0207  0.0249  0.0352  363 HOH   A O   
1106 O O   . HOH   E .   ? 0.5535 0.6746 0.3738 0.2978  -0.1570 -0.1801 364 HOH   A O   
1107 O O   A HOH   E .   ? 0.2046 0.1438 0.0902 0.0328  -0.0057 0.0093  365 HOH   A O   
1108 O O   B HOH   E .   ? 0.2426 0.1103 0.0184 0.0568  -0.0401 -0.0314 365 HOH   A O   
1109 O O   A HOH   E .   ? 0.2165 0.5863 0.0854 0.0154  0.0196  -0.1398 366 HOH   A O   
1110 O O   B HOH   E .   ? 0.5479 0.3649 0.2974 0.2363  -0.1594 -0.2450 366 HOH   A O   
1111 O O   . HOH   E .   ? 0.1441 0.1001 0.0586 0.0132  0.0328  0.0226  367 HOH   A O   
1112 O O   . HOH   E .   ? 0.3054 0.4301 0.2423 -0.0278 0.0368  0.0390  368 HOH   A O   
1113 O O   . HOH   E .   ? 0.4550 0.4475 0.1703 0.0243  0.0229  -0.1111 369 HOH   A O   
1114 O O   . HOH   E .   ? 0.4375 0.9467 0.4903 0.2022  -0.1384 0.2071  370 HOH   A O   
1115 O O   . HOH   E .   ? 0.2221 0.2454 0.2029 0.0352  -0.0408 -0.0570 371 HOH   A O   
1116 O O   A HOH   E .   ? 0.1848 0.1385 0.0165 -0.0804 -0.0399 0.0187  372 HOH   A O   
1117 O O   B HOH   E .   ? 0.4995 0.4464 0.0640 -0.2528 0.1169  -0.0849 372 HOH   A O   
1118 O O   . HOH   E .   ? 0.5283 0.7296 0.2074 0.3234  0.0360  0.2093  373 HOH   A O   
1119 O O   . HOH   E .   ? 0.1982 0.2672 0.1789 -0.0810 -0.0346 -0.0009 374 HOH   A O   
1120 O O   . HOH   E .   ? 0.4803 0.4859 0.2868 -0.2281 -0.0408 -0.0348 375 HOH   A O   
1121 O O   A HOH   E .   ? 0.2035 0.4143 0.0746 0.0369  -0.0275 -0.0292 376 HOH   A O   
1122 O O   B HOH   E .   ? 0.5079 0.5158 0.0774 -0.0550 -0.1024 0.1540  376 HOH   A O   
1123 O O   . HOH   E .   ? 0.6936 0.2063 0.3973 0.0516  -0.0161 0.0886  377 HOH   A O   
1124 O O   A HOH   E .   ? 0.2923 0.1886 0.0707 0.0085  -0.0129 -0.0722 378 HOH   A O   
1125 O O   B HOH   E .   ? 0.3203 0.3871 1.0006 0.0645  -0.2749 -0.2622 378 HOH   A O   
1126 O O   . HOH   E .   ? 0.4661 0.9027 0.1728 0.0367  0.0674  -0.1334 379 HOH   A O   
1127 O O   . HOH   E .   ? 0.2414 0.2515 0.1121 -0.0483 0.0724  0.0198  380 HOH   A O   
1128 O O   . HOH   E .   ? 0.3924 0.6371 0.2504 -0.1485 0.1039  -0.1170 381 HOH   A O   
1129 O O   A HOH   E .   ? 0.4058 0.5667 0.3205 0.1298  0.3146  -0.0314 382 HOH   A O   
1130 O O   B HOH   E .   ? 0.2936 0.1400 0.4822 -0.0350 0.1423  -0.0482 382 HOH   A O   
1131 O O   A HOH   E .   ? 0.3736 0.3985 0.0577 -0.1579 -0.0066 -0.1215 383 HOH   A O   
1132 O O   B HOH   E .   ? 0.3596 0.3586 0.0369 0.0548  0.0083  -0.0642 383 HOH   A O   
1133 O O   . HOH   E .   ? 0.3379 0.2344 0.2269 -0.0102 -0.0460 -0.0178 384 HOH   A O   
1134 O O   A HOH   E .   ? 0.4413 0.1775 0.2237 -0.0453 -0.1452 0.0002  385 HOH   A O   
1135 O O   B HOH   E .   ? 0.3341 0.7161 0.1583 -0.1496 0.0604  -0.2102 385 HOH   A O   
1136 O O   . HOH   E .   ? 0.5343 0.4605 0.0889 -0.0775 -0.0321 0.0243  386 HOH   A O   
1137 O O   A HOH   E .   ? 0.3984 0.3067 0.2061 0.0631  0.0471  0.0483  387 HOH   A O   
1138 O O   B HOH   E .   ? 0.7071 0.2493 0.1521 0.0420  0.0321  -0.0174 387 HOH   A O   
1139 O O   . HOH   E .   ? 0.3061 0.3206 0.1746 -0.0107 0.0352  -0.0672 388 HOH   A O   
1140 O O   . HOH   E .   ? 0.2738 0.3451 0.1530 -0.1016 0.0385  -0.0587 389 HOH   A O   
1141 O O   A HOH   E .   ? 0.3871 0.2929 0.1493 0.0919  0.0221  0.0831  390 HOH   A O   
1142 O O   B HOH   E .   ? 0.3905 0.7428 0.0970 -0.0407 -0.0765 -0.0387 390 HOH   A O   
1143 O O   . HOH   E .   ? 0.2204 0.2871 0.3764 0.0107  0.0033  -0.0237 391 HOH   A O   
1144 O O   . HOH   E .   ? 0.3267 0.6119 0.6801 0.2147  0.0157  0.0380  392 HOH   A O   
1145 O O   . HOH   E .   ? 0.6105 0.4736 0.3489 0.1433  -0.1182 -0.3045 393 HOH   A O   
1146 O O   . HOH   E .   ? 0.3923 0.3211 0.4754 0.0600  -0.2225 -0.0102 394 HOH   A O   
1147 O O   . HOH   E .   ? 1.1925 0.6605 0.2050 0.2771  0.0226  -0.0447 395 HOH   A O   
1148 O O   . HOH   E .   ? 0.4578 0.2231 0.9535 0.0818  0.2838  0.1431  396 HOH   A O   
1149 O O   . HOH   E .   ? 0.4821 1.3107 0.7590 0.2210  -0.1003 -0.3103 397 HOH   A O   
1150 O O   A HOH   E .   ? 0.3403 0.8161 0.3468 0.1004  -0.2434 -0.2277 398 HOH   A O   
1151 O O   B HOH   E .   ? 0.1273 0.4047 0.3623 -0.0119 0.0307  0.3689  398 HOH   A O   
1152 O O   A HOH   E .   ? 0.1364 0.1243 0.0718 -0.0112 0.0188  -0.0273 399 HOH   A O   
1153 O O   B HOH   E .   ? 0.0495 0.2518 0.0110 0.0318  -0.0064 -0.0335 399 HOH   A O   
1154 O O   A HOH   E .   ? 0.5009 0.4826 0.3424 0.0430  0.0676  0.3146  400 HOH   A O   
1155 O O   B HOH   E .   ? 0.3063 0.3143 0.1118 -0.0759 -0.0455 0.0679  400 HOH   A O   
1156 O O   . HOH   E .   ? 0.5268 0.7001 0.9059 0.0542  0.0641  -0.4678 401 HOH   A O   
1157 O O   . HOH   E .   ? 0.5238 0.6414 0.1528 0.0001  0.0096  0.0667  402 HOH   A O   
1158 O O   A HOH   E .   ? 0.0794 0.0608 0.0734 0.0359  0.0325  -0.0189 403 HOH   A O   
1159 O O   B HOH   E .   ? 0.5061 0.3596 0.1545 -0.3112 0.0425  0.0039  403 HOH   A O   
1160 O O   . HOH   E .   ? 0.3558 0.3626 0.3419 -0.0184 -0.0728 -0.0536 404 HOH   A O   
1161 O O   . HOH   E .   ? 0.2602 0.3580 0.2280 0.0169  0.0002  -0.0169 405 HOH   A O   
1162 O O   . HOH   E .   ? 0.4238 0.6318 0.8185 0.0053  -0.2597 -0.0811 406 HOH   A O   
1163 O O   A HOH   E .   ? 0.7174 0.2898 0.3295 0.0114  -0.1893 -0.1533 407 HOH   A O   
1164 O O   B HOH   E .   ? 0.6343 0.3830 0.2186 0.0602  0.2295  -0.0883 407 HOH   A O   
1165 O O   . HOH   E .   ? 0.3563 0.3554 0.4156 0.0657  0.0325  -0.1746 408 HOH   A O   
1166 O O   . HOH   E .   ? 0.3334 0.4296 0.3031 -0.0142 0.0507  -0.1579 409 HOH   A O   
1167 O O   . HOH   E .   ? 0.3186 0.3693 0.4149 0.0154  -0.0354 -0.0276 410 HOH   A O   
1168 O O   . HOH   E .   ? 0.2263 0.2075 0.1277 0.0034  -0.0285 -0.0062 411 HOH   A O   
1169 O O   A HOH   E .   ? 0.3045 0.1623 0.1368 0.0008  -0.1189 -0.0661 412 HOH   A O   
1170 O O   B HOH   E .   ? 0.1351 0.1431 0.1379 -0.0654 -0.0327 0.0011  412 HOH   A O   
1171 O O   . HOH   E .   ? 0.4649 0.4335 0.5979 0.1543  0.0262  0.0587  413 HOH   A O   
1172 O O   . HOH   E .   ? 0.3872 0.4249 0.8874 0.0368  -0.0541 -0.2551 414 HOH   A O   
1173 O O   . HOH   E .   ? 0.9154 0.8064 0.2457 -0.1492 -0.0471 0.1808  415 HOH   A O   
1174 O O   . HOH   E .   ? 0.4455 0.2171 0.3878 0.0436  -0.2326 0.0399  416 HOH   A O   
1175 O O   A HOH   E .   ? 0.1587 0.2145 0.3710 -0.0250 -0.0444 -0.0711 417 HOH   A O   
1176 O O   B HOH   E .   ? 0.1432 0.3668 0.7982 -0.0104 -0.0512 0.1365  417 HOH   A O   
1177 O O   A HOH   E .   ? 0.3237 0.2883 0.1941 -0.2347 0.0444  -0.0833 418 HOH   A O   
1178 O O   B HOH   E .   ? 0.1611 0.2056 0.4132 -0.0391 0.1316  -0.1826 418 HOH   A O   
1179 O O   A HOH   E .   ? 0.2621 0.3322 0.6016 0.0399  0.0739  0.1321  419 HOH   A O   
1180 O O   B HOH   E .   ? 0.2411 0.3672 0.2778 0.1150  -0.1493 -0.2127 419 HOH   A O   
1181 O O   . HOH   E .   ? 0.4120 0.5007 1.4036 -0.1342 0.3863  -0.4781 420 HOH   A O   
# 
