data_9DFQ
# 
_entry.id   9DFQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9DFQ         pdb_00009dfq 10.2210/pdb9dfq/pdb 
WWPDB D_1000287978 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-28 ? 
2 'Structure model' 1 1 2025-06-18 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_DOI'    
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DFQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              john.pascal@umontreal.ca 
_pdbx_contact_author.name_first         Pascal 
_pdbx_contact_author.name_last          John 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2714-4317 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Frigon, L.'   1 0009-0004-7020-5295 
'Pascal, J.M.' 2 0000-0002-2714-4317 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                110277 
_citation.page_last                 110277 
_citation.title                     'Crystal structure and mutagenesis of a nucleic acid-binding BRCT domain in human PARP4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.110277 
_citation.pdbx_database_id_PubMed   40412520 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Frigon, L.'   1 ? 
primary 'Pascal, J.M.' 2 ? 
# 
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 'Protein mono-ADP-ribosyltransferase PARP4' 11692.612 1  2.4.2.- F39Q ? ? 
2 non-polymer syn 'SULFATE ION'                               96.063    1  ?       ?    ? ? 
3 water       nat water                                       18.015    73 ?       ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;193 kDa vault protein,ADP-ribosyltransferase diphtheria toxin-like 4,ARTD4,PARP-related/IalphaI-related H5/proline-rich,PH5P,Poly [ADP-ribose] polymerase 4,PARP-4,Vault poly(ADP-ribose) polymerase,VPARP
;
# 
_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       
;MVMGIFANCIFCLKVKYLPQQQKKKLQTDIKENGGKFSQSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKS
IREKRLLDVKNYDPYKPLDI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVMGIFANCIFCLKVKYLPQQQKKKLQTDIKENGGKFSQSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKS
IREKRLLDVKNYDPYKPLDI
;
_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 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   MET n 
1 4   GLY n 
1 5   ILE n 
1 6   PHE n 
1 7   ALA n 
1 8   ASN n 
1 9   CYS n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  LYS n 
1 15  VAL n 
1 16  LYS n 
1 17  TYR n 
1 18  LEU n 
1 19  PRO n 
1 20  GLN n 
1 21  GLN n 
1 22  GLN n 
1 23  LYS n 
1 24  LYS n 
1 25  LYS n 
1 26  LEU n 
1 27  GLN n 
1 28  THR n 
1 29  ASP n 
1 30  ILE n 
1 31  LYS n 
1 32  GLU n 
1 33  ASN n 
1 34  GLY n 
1 35  GLY n 
1 36  LYS n 
1 37  PHE n 
1 38  SER n 
1 39  GLN n 
1 40  SER n 
1 41  LEU n 
1 42  ASN n 
1 43  PRO n 
1 44  GLN n 
1 45  CYS n 
1 46  THR n 
1 47  HIS n 
1 48  ILE n 
1 49  ILE n 
1 50  LEU n 
1 51  ASP n 
1 52  ASN n 
1 53  ALA n 
1 54  ASP n 
1 55  VAL n 
1 56  LEU n 
1 57  SER n 
1 58  GLN n 
1 59  TYR n 
1 60  GLN n 
1 61  LEU n 
1 62  ASN n 
1 63  SER n 
1 64  ILE n 
1 65  GLN n 
1 66  LYS n 
1 67  ASN n 
1 68  HIS n 
1 69  VAL n 
1 70  HIS n 
1 71  ILE n 
1 72  ALA n 
1 73  ASN n 
1 74  PRO n 
1 75  ASP n 
1 76  PHE n 
1 77  ILE n 
1 78  TRP n 
1 79  LYS n 
1 80  SER n 
1 81  ILE n 
1 82  ARG n 
1 83  GLU n 
1 84  LYS n 
1 85  ARG n 
1 86  LEU n 
1 87  LEU n 
1 88  ASP n 
1 89  VAL n 
1 90  LYS n 
1 91  ASN n 
1 92  TYR n 
1 93  ASP n 
1 94  PRO n 
1 95  TYR n 
1 96  LYS n 
1 97  PRO n 
1 98  LEU n 
1 99  ASP n 
1 100 ILE 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                   100 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PARP4, ADPRTL1, KIAA0177, PARPL' 
_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 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   MET 1   1   ?  ?   ?   A . n 
A 1 2   VAL 2   2   ?  ?   ?   A . n 
A 1 3   MET 3   3   ?  ?   ?   A . n 
A 1 4   GLY 4   4   4  GLY GLY A . n 
A 1 5   ILE 5   5   5  ILE ILE A . n 
A 1 6   PHE 6   6   6  PHE PHE A . n 
A 1 7   ALA 7   7   7  ALA ALA A . n 
A 1 8   ASN 8   8   8  ASN ASN A . n 
A 1 9   CYS 9   9   9  CYS CYS A . n 
A 1 10  ILE 10  10  10 ILE ILE A . n 
A 1 11  PHE 11  11  11 PHE PHE A . n 
A 1 12  CYS 12  12  12 CYS CYS A . n 
A 1 13  LEU 13  13  13 LEU LEU A . n 
A 1 14  LYS 14  14  14 LYS LYS A . n 
A 1 15  VAL 15  15  15 VAL VAL A . n 
A 1 16  LYS 16  16  16 LYS LYS A . n 
A 1 17  TYR 17  17  17 TYR TYR A . n 
A 1 18  LEU 18  18  18 LEU LEU A . n 
A 1 19  PRO 19  19  19 PRO PRO A . n 
A 1 20  GLN 20  20  20 GLN GLN A . n 
A 1 21  GLN 21  21  21 GLN GLN A . n 
A 1 22  GLN 22  22  22 GLN GLN A . n 
A 1 23  LYS 23  23  23 LYS LYS A . n 
A 1 24  LYS 24  24  24 LYS LYS A . n 
A 1 25  LYS 25  25  25 LYS LYS A . n 
A 1 26  LEU 26  26  26 LEU LEU A . n 
A 1 27  GLN 27  27  27 GLN GLN A . n 
A 1 28  THR 28  28  28 THR THR A . n 
A 1 29  ASP 29  29  29 ASP ASP A . n 
A 1 30  ILE 30  30  30 ILE ILE A . n 
A 1 31  LYS 31  31  31 LYS LYS A . n 
A 1 32  GLU 32  32  32 GLU GLU A . n 
A 1 33  ASN 33  33  33 ASN ASN A . n 
A 1 34  GLY 34  34  34 GLY GLY A . n 
A 1 35  GLY 35  35  35 GLY GLY A . n 
A 1 36  LYS 36  36  36 LYS LYS A . n 
A 1 37  PHE 37  37  37 PHE PHE A . n 
A 1 38  SER 38  38  38 SER SER A . n 
A 1 39  GLN 39  39  39 GLN GLN A . n 
A 1 40  SER 40  40  40 SER SER A . n 
A 1 41  LEU 41  41  41 LEU LEU A . n 
A 1 42  ASN 42  42  42 ASN ASN A . n 
A 1 43  PRO 43  43  43 PRO PRO A . n 
A 1 44  GLN 44  44  44 GLN GLN A . n 
A 1 45  CYS 45  45  45 CYS CYS A . n 
A 1 46  THR 46  46  46 THR THR A . n 
A 1 47  HIS 47  47  47 HIS HIS A . n 
A 1 48  ILE 48  48  48 ILE ILE A . n 
A 1 49  ILE 49  49  49 ILE ILE A . n 
A 1 50  LEU 50  50  50 LEU LEU A . n 
A 1 51  ASP 51  51  51 ASP ASP A . n 
A 1 52  ASN 52  52  52 ASN ASN A . n 
A 1 53  ALA 53  53  53 ALA ALA A . n 
A 1 54  ASP 54  54  54 ASP ASP A . n 
A 1 55  VAL 55  55  55 VAL VAL A . n 
A 1 56  LEU 56  56  56 LEU LEU A . n 
A 1 57  SER 57  57  57 SER SER A . n 
A 1 58  GLN 58  58  58 GLN GLN A . n 
A 1 59  TYR 59  59  59 TYR TYR A . n 
A 1 60  GLN 60  60  60 GLN GLN A . n 
A 1 61  LEU 61  61  61 LEU LEU A . n 
A 1 62  ASN 62  62  62 ASN ASN A . n 
A 1 63  SER 63  63  63 SER SER A . n 
A 1 64  ILE 64  64  64 ILE ILE A . n 
A 1 65  GLN 65  65  65 GLN GLN A . n 
A 1 66  LYS 66  66  66 LYS LYS A . n 
A 1 67  ASN 67  67  67 ASN ASN A . n 
A 1 68  HIS 68  68  68 HIS HIS A . n 
A 1 69  VAL 69  69  69 VAL VAL A . n 
A 1 70  HIS 70  70  70 HIS HIS A . n 
A 1 71  ILE 71  71  71 ILE ILE A . n 
A 1 72  ALA 72  72  72 ALA ALA A . n 
A 1 73  ASN 73  73  73 ASN ASN A . n 
A 1 74  PRO 74  74  74 PRO PRO A . n 
A 1 75  ASP 75  75  75 ASP ASP A . n 
A 1 76  PHE 76  76  76 PHE PHE A . n 
A 1 77  ILE 77  77  77 ILE ILE A . n 
A 1 78  TRP 78  78  78 TRP TRP A . n 
A 1 79  LYS 79  79  79 LYS LYS A . n 
A 1 80  SER 80  80  80 SER SER A . n 
A 1 81  ILE 81  81  81 ILE ILE A . n 
A 1 82  ARG 82  82  82 ARG ARG A . n 
A 1 83  GLU 83  83  83 GLU GLU A . n 
A 1 84  LYS 84  84  84 LYS LYS A . n 
A 1 85  ARG 85  85  85 ARG ARG A . n 
A 1 86  LEU 86  86  86 LEU LEU A . n 
A 1 87  LEU 87  87  87 LEU LEU A . n 
A 1 88  ASP 88  88  88 ASP ASP A . n 
A 1 89  VAL 89  89  89 VAL VAL A . n 
A 1 90  LYS 90  90  90 LYS LYS A . n 
A 1 91  ASN 91  91  91 ASN ASN A . n 
A 1 92  TYR 92  92  92 TYR TYR A . n 
A 1 93  ASP 93  93  93 ASP ASP A . n 
A 1 94  PRO 94  94  94 PRO PRO A . n 
A 1 95  TYR 95  95  95 TYR TYR A . n 
A 1 96  LYS 96  96  96 LYS LYS A . n 
A 1 97  PRO 97  97  97 PRO PRO A . n 
A 1 98  LEU 98  98  98 LEU LEU A . n 
A 1 99  ASP 99  99  ?  ?   ?   A . n 
A 1 100 ILE 100 100 ?  ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SO4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SO4 
_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 SO4 1  201 1  SO4 SO4 A . 
C 3 HOH 1  301 70 HOH HOH A . 
C 3 HOH 2  302 32 HOH HOH A . 
C 3 HOH 3  303 41 HOH HOH A . 
C 3 HOH 4  304 55 HOH HOH A . 
C 3 HOH 5  305 73 HOH HOH A . 
C 3 HOH 6  306 62 HOH HOH A . 
C 3 HOH 7  307 30 HOH HOH A . 
C 3 HOH 8  308 47 HOH HOH A . 
C 3 HOH 9  309 19 HOH HOH A . 
C 3 HOH 10 310 27 HOH HOH A . 
C 3 HOH 11 311 49 HOH HOH A . 
C 3 HOH 12 312 16 HOH HOH A . 
C 3 HOH 13 313 7  HOH HOH A . 
C 3 HOH 14 314 44 HOH HOH A . 
C 3 HOH 15 315 36 HOH HOH A . 
C 3 HOH 16 316 11 HOH HOH A . 
C 3 HOH 17 317 9  HOH HOH A . 
C 3 HOH 18 318 6  HOH HOH A . 
C 3 HOH 19 319 45 HOH HOH A . 
C 3 HOH 20 320 37 HOH HOH A . 
C 3 HOH 21 321 66 HOH HOH A . 
C 3 HOH 22 322 3  HOH HOH A . 
C 3 HOH 23 323 5  HOH HOH A . 
C 3 HOH 24 324 31 HOH HOH A . 
C 3 HOH 25 325 21 HOH HOH A . 
C 3 HOH 26 326 2  HOH HOH A . 
C 3 HOH 27 327 35 HOH HOH A . 
C 3 HOH 28 328 10 HOH HOH A . 
C 3 HOH 29 329 33 HOH HOH A . 
C 3 HOH 30 330 50 HOH HOH A . 
C 3 HOH 31 331 67 HOH HOH A . 
C 3 HOH 32 332 15 HOH HOH A . 
C 3 HOH 33 333 22 HOH HOH A . 
C 3 HOH 34 334 54 HOH HOH A . 
C 3 HOH 35 335 1  HOH HOH A . 
C 3 HOH 36 336 28 HOH HOH A . 
C 3 HOH 37 337 20 HOH HOH A . 
C 3 HOH 38 338 69 HOH HOH A . 
C 3 HOH 39 339 52 HOH HOH A . 
C 3 HOH 40 340 56 HOH HOH A . 
C 3 HOH 41 341 58 HOH HOH A . 
C 3 HOH 42 342 24 HOH HOH A . 
C 3 HOH 43 343 25 HOH HOH A . 
C 3 HOH 44 344 34 HOH HOH A . 
C 3 HOH 45 345 38 HOH HOH A . 
C 3 HOH 46 346 40 HOH HOH A . 
C 3 HOH 47 347 60 HOH HOH A . 
C 3 HOH 48 348 68 HOH HOH A . 
C 3 HOH 49 349 46 HOH HOH A . 
C 3 HOH 50 350 4  HOH HOH A . 
C 3 HOH 51 351 59 HOH HOH A . 
C 3 HOH 52 352 42 HOH HOH A . 
C 3 HOH 53 353 39 HOH HOH A . 
C 3 HOH 54 354 64 HOH HOH A . 
C 3 HOH 55 355 8  HOH HOH A . 
C 3 HOH 56 356 61 HOH HOH A . 
C 3 HOH 57 357 29 HOH HOH A . 
C 3 HOH 58 358 53 HOH HOH A . 
C 3 HOH 59 359 18 HOH HOH A . 
C 3 HOH 60 360 57 HOH HOH A . 
C 3 HOH 61 361 65 HOH HOH A . 
C 3 HOH 62 362 63 HOH HOH A . 
C 3 HOH 63 363 71 HOH HOH A . 
C 3 HOH 64 364 13 HOH HOH A . 
C 3 HOH 65 365 12 HOH HOH A . 
C 3 HOH 66 366 14 HOH HOH A . 
C 3 HOH 67 367 23 HOH HOH A . 
C 3 HOH 68 368 51 HOH HOH A . 
C 3 HOH 69 369 48 HOH HOH A . 
C 3 HOH 70 370 43 HOH HOH A . 
C 3 HOH 71 371 17 HOH HOH A . 
C 3 HOH 72 372 72 HOH HOH A . 
C 3 HOH 73 373 26 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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0430 ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .        ? 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                     9DFQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.210 
_cell.length_a_esd                 ? 
_cell.length_b                     115.210 
_cell.length_b_esd                 ? 
_cell.length_c                     115.210 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9DFQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                196 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 2 3' 
_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                   9DFQ 
_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             2.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.86 
_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              ? 
_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    '2 M ammonium sulfate and 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 PILATUS3 S 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         2024-04-02 
_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   1.2 
_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                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.2 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DFQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               20 
_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                                     7499 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          32.1 
_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                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_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                             610 
_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                               9.0 
_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                                  0.815 
_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]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.239 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.details                                  ? 
_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                                 9DFQ 
_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                            2.10 
_refine.ls_d_res_low                             19.48 
_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                     7112 
_refine.ls_number_reflns_R_free                  379 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18303 
_refine.ls_R_factor_R_free                       0.22996 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18078 
_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                      ? 
_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                       0.193 
_refine.pdbx_overall_ESU_R_Free                  0.174 
_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                             9.905 
_refine.overall_SU_ML                            0.135 
_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                       2.10 
_refine_hist.d_res_low                        19.48 
_refine_hist.number_atoms_solvent             73 
_refine_hist.number_atoms_total               859 
_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        781 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  0.012  834  ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  822  ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.283  1.818  1131 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.425  1.802  1904 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 6.171  5.000  102  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 7.172  5.000  2    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 11.686 10.000 163  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.058  0.200  124  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  962  ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  188  ? 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' ? 1.993  3.463  396  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 1.983  3.464  396  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 3.075  6.213  499  ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.074  6.224  500  ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 2.886  3.903  438  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.827  3.854  435  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 4.611  6.922  626  ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 7.817  33.99  962  ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 7.625  33.55  942  ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? 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                          2.102 
_refine_ls_shell.d_res_low                           2.156 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                22 
_refine_ls_shell.number_reflns_R_work                521 
_refine_ls_shell.percent_reflns_obs                  100.00 
_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                     0.260 
_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                     0.290 
# 
_struct.entry_id                     9DFQ 
_struct.title                        'PARP4 BRCT domain F39Q mutant' 
_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        9DFQ 
_struct_keywords.text            'PARP family, ADP-ribosyltransferase, marylation, vault, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARP4_HUMAN 
_struct_ref.pdbx_db_accession          Q9UKK3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVMGIFANCIFCLKVKYLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKS
IREKRLLDVKNYDPYKPLDI
;
_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              9DFQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 100 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9UKK3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  100 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       100 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9DFQ 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      39 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q9UKK3 
_struct_ref_seq_dif.db_mon_id                    PHE 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          39 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            39 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 PRO A 19 ? ASN A 33 ? PRO A 19 ASN A 33 1 ? 15 
HELX_P HELX_P2 AA2 SER A 57 ? HIS A 68 ? SER A 57 HIS A 68 1 ? 12 
HELX_P HELX_P3 AA3 PRO A 74 ? LYS A 84 ? PRO A 74 LYS A 84 1 ? 11 
HELX_P HELX_P4 AA4 ASP A 88 ? ASP A 93 ? ASP A 88 ASP A 93 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? 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 LYS A 36 ? SER A 38 ? LYS A 36 SER A 38 
AA1 2 ILE A 10 ? LYS A 14 ? ILE A 10 LYS A 14 
AA1 3 HIS A 47 ? LEU A 50 ? HIS A 47 LEU A 50 
AA1 4 HIS A 70 ? ALA A 72 ? HIS A 70 ALA A 72 
# 
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 O LYS A 36 ? O LYS A 36 N PHE A 11 ? N PHE A 11 
AA1 2 3 N LYS A 14 ? N LYS A 14 O ILE A 49 ? O ILE A 49 
AA1 3 4 N ILE A 48 ? N ILE A 48 O HIS A 70 ? O HIS A 70 
# 
_pdbx_entry_details.entry_id                   9DFQ 
_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 LYS A 14 ? ? -118.99 76.65 
2 1 LYS A 96 ? ? -159.82 70.01 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 311 ? C HOH . 
2 1 A HOH 343 ? C HOH . 
3 1 A HOH 369 ? C HOH . 
4 1 A HOH 370 ? C HOH . 
5 1 A HOH 372 ? C HOH . 
6 1 A HOH 373 ? C HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         13.3794 
_pdbx_refine_tls.origin_y         3.4467 
_pdbx_refine_tls.origin_z         25.5701 
_pdbx_refine_tls.T[1][1]          0.0288 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0143 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0270 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0395 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0348 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0763 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          6.5787 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2351 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -2.9258 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.6219 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0570 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          4.9245 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.1279 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2818 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.3633 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0169 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0883 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0263 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1657 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0779 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.2161 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     4 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     98 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 MET 1   ? A MET 1   
2 1 Y 1 A VAL 2   ? A VAL 2   
3 1 Y 1 A MET 3   ? A MET 3   
4 1 Y 1 A ASP 99  ? A ASP 99  
5 1 Y 1 A ILE 100 ? A ILE 100 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Canadian Institutes of Health Research (CIHR)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           PJT153295 
_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   9DEV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DFQ 
_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]   0.008680 
_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]   0.008680 
_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]   0.008680 
_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  
NA 
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   . GLY A 1 4  ? 25.887 -8.027  25.301 1.00 59.93  ? 4   GLY A N   1 
ATOM   2   C CA  . GLY A 1 4  ? 25.582 -6.787  24.560 1.00 57.76  ? 4   GLY A CA  1 
ATOM   3   C C   . GLY A 1 4  ? 25.325 -5.612  25.503 1.00 54.01  ? 4   GLY A C   1 
ATOM   4   O O   . GLY A 1 4  ? 25.084 -5.802  26.688 1.00 56.67  ? 4   GLY A O   1 
ATOM   5   N N   . ILE A 1 5  ? 25.359 -4.395  24.955 1.00 53.78  ? 5   ILE A N   1 
ATOM   6   C CA  . ILE A 1 5  ? 25.375 -3.180  25.758 1.00 51.92  ? 5   ILE A CA  1 
ATOM   7   C C   . ILE A 1 5  ? 24.050 -3.003  26.502 1.00 50.33  ? 5   ILE A C   1 
ATOM   8   O O   . ILE A 1 5  ? 24.014 -2.327  27.524 1.00 49.51  ? 5   ILE A O   1 
ATOM   9   C CB  . ILE A 1 5  ? 25.722 -1.951  24.895 1.00 51.11  ? 5   ILE A CB  1 
ATOM   10  C CG1 . ILE A 1 5  ? 24.747 -1.749  23.763 1.00 50.24  ? 5   ILE A CG1 1 
ATOM   11  C CG2 . ILE A 1 5  ? 27.155 -2.049  24.378 1.00 55.07  ? 5   ILE A CG2 1 
ATOM   12  C CD1 . ILE A 1 5  ? 24.885 -0.411  23.059 1.00 50.92  ? 5   ILE A CD1 1 
ATOM   13  N N   . PHE A 1 6  ? 22.974 -3.622  25.997 1.00 47.39  ? 6   PHE A N   1 
ATOM   14  C CA  . PHE A 1 6  ? 21.665 -3.509  26.617 1.00 47.34  ? 6   PHE A CA  1 
ATOM   15  C C   . PHE A 1 6  ? 21.303 -4.721  27.480 1.00 51.17  ? 6   PHE A C   1 
ATOM   16  O O   . PHE A 1 6  ? 20.125 -4.928  27.777 1.00 50.90  ? 6   PHE A O   1 
ATOM   17  C CB  . PHE A 1 6  ? 20.656 -3.326  25.482 1.00 46.63  ? 6   PHE A CB  1 
ATOM   18  C CG  . PHE A 1 6  ? 20.781 -2.034  24.690 1.00 42.54  ? 6   PHE A CG  1 
ATOM   19  C CD1 . PHE A 1 6  ? 20.972 -0.811  25.330 1.00 42.84  ? 6   PHE A CD1 1 
ATOM   20  C CD2 . PHE A 1 6  ? 20.683 -2.042  23.302 1.00 44.01  ? 6   PHE A CD2 1 
ATOM   21  C CE1 . PHE A 1 6  ? 21.054 0.372   24.597 1.00 41.67  ? 6   PHE A CE1 1 
ATOM   22  C CE2 . PHE A 1 6  ? 20.766 -0.856  22.575 1.00 41.51  ? 6   PHE A CE2 1 
ATOM   23  C CZ  . PHE A 1 6  ? 20.967 0.343   23.224 1.00 39.48  ? 6   PHE A CZ  1 
ATOM   24  N N   . ALA A 1 7  ? 22.293 -5.503  27.927 1.00 53.88  ? 7   ALA A N   1 
ATOM   25  C CA  . ALA A 1 7  ? 22.005 -6.642  28.785 1.00 56.72  ? 7   ALA A CA  1 
ATOM   26  C C   . ALA A 1 7  ? 21.342 -6.172  30.079 1.00 57.89  ? 7   ALA A C   1 
ATOM   27  O O   . ALA A 1 7  ? 21.741 -5.155  30.639 1.00 56.19  ? 7   ALA A O   1 
ATOM   28  C CB  . ALA A 1 7  ? 23.266 -7.414  29.074 1.00 59.38  ? 7   ALA A CB  1 
ATOM   29  N N   . ASN A 1 8  ? 20.338 -6.941  30.529 1.00 58.58  ? 8   ASN A N   1 
ATOM   30  C CA  . ASN A 1 8  ? 19.583 -6.696  31.752 1.00 61.31  ? 8   ASN A CA  1 
ATOM   31  C C   . ASN A 1 8  ? 18.706 -5.449  31.627 1.00 55.57  ? 8   ASN A C   1 
ATOM   32  O O   . ASN A 1 8  ? 18.232 -4.929  32.632 1.00 55.48  ? 8   ASN A O   1 
ATOM   33  C CB  . ASN A 1 8  ? 20.475 -6.616  32.987 1.00 63.87  ? 8   ASN A CB  1 
ATOM   34  C CG  . ASN A 1 8  ? 21.284 -7.873  33.200 1.00 71.27  ? 8   ASN A CG  1 
ATOM   35  O OD1 . ASN A 1 8  ? 20.721 -8.965  33.325 1.00 72.18  ? 8   ASN A OD1 1 
ATOM   36  N ND2 . ASN A 1 8  ? 22.601 -7.743  33.253 1.00 73.84  ? 8   ASN A ND2 1 
ATOM   37  N N   . CYS A 1 9  ? 18.483 -4.973  30.397 1.00 53.63  ? 9   CYS A N   1 
ATOM   38  C CA  . CYS A 1 9  ? 17.575 -3.860  30.171 1.00 52.87  ? 9   CYS A CA  1 
ATOM   39  C C   . CYS A 1 9  ? 16.269 -4.393  29.604 1.00 51.61  ? 9   CYS A C   1 
ATOM   40  O O   . CYS A 1 9  ? 16.284 -5.254  28.722 1.00 52.36  ? 9   CYS A O   1 
ATOM   41  C CB  . CYS A 1 9  ? 18.127 -2.837  29.186 1.00 51.52  ? 9   CYS A CB  1 
ATOM   42  S SG  . CYS A 1 9  ? 19.586 -1.959  29.798 1.00 52.60  ? 9   CYS A SG  1 
ATOM   43  N N   . ILE A 1 10 ? 15.162 -3.863  30.131 1.00 50.61  ? 10  ILE A N   1 
ATOM   44  C CA  . ILE A 1 10 ? 13.829 -4.224  29.681 1.00 50.38  ? 10  ILE A CA  1 
ATOM   45  C C   . ILE A 1 10 ? 13.141 -2.940  29.238 1.00 47.00  ? 10  ILE A C   1 
ATOM   46  O O   . ILE A 1 10 ? 12.896 -2.060  30.064 1.00 41.71  ? 10  ILE A O   1 
ATOM   47  C CB  . ILE A 1 10 ? 13.055 -4.964  30.789 1.00 53.01  ? 10  ILE A CB  1 
ATOM   48  C CG1 . ILE A 1 10 ? 13.835 -6.200  31.277 1.00 56.89  ? 10  ILE A CG1 1 
ATOM   49  C CG2 . ILE A 1 10 ? 11.636 -5.326  30.345 1.00 54.54  ? 10  ILE A CG2 1 
ATOM   50  C CD1 . ILE A 1 10 ? 13.037 -7.163  32.142 1.00 59.07  ? 10  ILE A CD1 1 
ATOM   51  N N   . PHE A 1 11 ? 12.830 -2.874  27.934 1.00 46.55  ? 11  PHE A N   1 
ATOM   52  C CA  . PHE A 1 11 ? 12.323 -1.666  27.299 1.00 46.03  ? 11  PHE A CA  1 
ATOM   53  C C   . PHE A 1 11 ? 10.829 -1.787  27.005 1.00 46.83  ? 11  PHE A C   1 
ATOM   54  O O   . PHE A 1 11 ? 10.405 -2.738  26.347 1.00 48.55  ? 11  PHE A O   1 
ATOM   55  C CB  . PHE A 1 11 ? 13.066 -1.408  25.985 1.00 45.72  ? 11  PHE A CB  1 
ATOM   56  C CG  . PHE A 1 11 ? 14.542 -1.068  26.146 1.00 45.62  ? 11  PHE A CG  1 
ATOM   57  C CD1 . PHE A 1 11 ? 15.503 -2.070  26.209 1.00 49.11  ? 11  PHE A CD1 1 
ATOM   58  C CD2 . PHE A 1 11 ? 14.963 0.252   26.243 1.00 45.55  ? 11  PHE A CD2 1 
ATOM   59  C CE1 . PHE A 1 11 ? 16.846 -1.755  26.357 1.00 48.12  ? 11  PHE A CE1 1 
ATOM   60  C CE2 . PHE A 1 11 ? 16.304 0.561   26.404 1.00 45.52  ? 11  PHE A CE2 1 
ATOM   61  C CZ  . PHE A 1 11 ? 17.244 -0.448  26.463 1.00 45.29  ? 11  PHE A CZ  1 
ATOM   62  N N   . CYS A 1 12 ? 10.048 -0.806  27.490 1.00 46.71  ? 12  CYS A N   1 
ATOM   63  C CA  . CYS A 1 12 ? 8.696  -0.565  27.001 1.00 46.34  ? 12  CYS A CA  1 
ATOM   64  C C   . CYS A 1 12 ? 8.760  0.493   25.905 1.00 41.71  ? 12  CYS A C   1 
ATOM   65  O O   . CYS A 1 12 ? 9.232  1.596   26.150 1.00 43.17  ? 12  CYS A O   1 
ATOM   66  C CB  . CYS A 1 12 ? 7.762  -0.105  28.115 1.00 47.12  ? 12  CYS A CB  1 
ATOM   67  S SG  . CYS A 1 12 ? 6.106  0.355   27.527 1.00 53.23  ? 12  CYS A SG  1 
ATOM   68  N N   . LEU A 1 13 ? 8.322  0.142   24.691 1.00 42.59  ? 13  LEU A N   1 
ATOM   69  C CA  . LEU A 1 13 ? 8.395  1.051   23.555 1.00 40.63  ? 13  LEU A CA  1 
ATOM   70  C C   . LEU A 1 13 ? 7.040  1.729   23.355 1.00 40.87  ? 13  LEU A C   1 
ATOM   71  O O   . LEU A 1 13 ? 6.008  1.066   23.199 1.00 39.34  ? 13  LEU A O   1 
ATOM   72  C CB  . LEU A 1 13 ? 8.847  0.329   22.286 1.00 43.74  ? 13  LEU A CB  1 
ATOM   73  C CG  . LEU A 1 13 ? 10.170 -0.436  22.380 1.00 45.00  ? 13  LEU A CG  1 
ATOM   74  C CD1 . LEU A 1 13 ? 10.457 -1.122  21.066 1.00 48.29  ? 13  LEU A CD1 1 
ATOM   75  C CD2 . LEU A 1 13 ? 11.318 0.459   22.781 1.00 45.41  ? 13  LEU A CD2 1 
ATOM   76  N N   . LYS A 1 14 ? 7.067  3.062   23.419 1.00 36.72  ? 14  LYS A N   1 
ATOM   77  C CA  . LYS A 1 14 ? 5.944  3.905   23.062 1.00 38.56  ? 14  LYS A CA  1 
ATOM   78  C C   . LYS A 1 14 ? 6.386  4.791   21.908 1.00 38.51  ? 14  LYS A C   1 
ATOM   79  O O   . LYS A 1 14 ? 6.728  5.949   22.118 1.00 38.38  ? 14  LYS A O   1 
ATOM   80  C CB  . LYS A 1 14 ? 5.587  4.797   24.250 1.00 40.62  ? 14  LYS A CB  1 
ATOM   81  C CG  . LYS A 1 14 ? 5.110  4.076   25.487 1.00 44.64  ? 14  LYS A CG  1 
ATOM   82  C CD  . LYS A 1 14 ? 3.883  3.218   25.226 1.00 48.75  ? 14  LYS A CD  1 
ATOM   83  C CE  . LYS A 1 14 ? 3.327  2.613   26.475 1.00 51.77  ? 14  LYS A CE  1 
ATOM   84  N NZ  . LYS A 1 14 ? 2.089  1.887   26.169 1.00 53.48  ? 14  LYS A NZ  1 
ATOM   85  N N   . VAL A 1 15 ? 6.441  4.205   20.712 1.00 39.83  ? 15  VAL A N   1 
ATOM   86  C CA  . VAL A 1 15 ? 7.008  4.862   19.546 1.00 40.70  ? 15  VAL A CA  1 
ATOM   87  C C   . VAL A 1 15 ? 6.030  4.716   18.383 1.00 43.68  ? 15  VAL A C   1 
ATOM   88  O O   . VAL A 1 15 ? 6.432  4.543   17.229 1.00 44.99  ? 15  VAL A O   1 
ATOM   89  C CB  . VAL A 1 15 ? 8.407  4.297   19.230 1.00 40.06  ? 15  VAL A CB  1 
ATOM   90  C CG1 . VAL A 1 15 ? 9.408  4.663   20.321 1.00 38.86  ? 15  VAL A CG1 1 
ATOM   91  C CG2 . VAL A 1 15 ? 8.400  2.791   19.008 1.00 40.72  ? 15  VAL A CG2 1 
ATOM   92  N N   . LYS A 1 16 ? 4.746  4.875   18.724 1.00 42.84  ? 16  LYS A N   1 
ATOM   93  C CA  . LYS A 1 16 ? 3.613  4.685   17.833 1.00 49.52  ? 16  LYS A CA  1 
ATOM   94  C C   . LYS A 1 16 ? 3.714  5.520   16.559 1.00 48.80  ? 16  LYS A C   1 
ATOM   95  O O   . LYS A 1 16 ? 3.109  5.159   15.560 1.00 49.92  ? 16  LYS A O   1 
ATOM   96  C CB  . LYS A 1 16 ? 2.361  5.112   18.610 1.00 53.70  ? 16  LYS A CB  1 
ATOM   97  C CG  . LYS A 1 16 ? 1.007  4.846   17.984 1.00 63.72  ? 16  LYS A CG  1 
ATOM   98  C CD  . LYS A 1 16 ? -0.126 4.989   18.998 1.00 67.69  ? 16  LYS A CD  1 
ATOM   99  C CE  . LYS A 1 16 ? -1.464 4.463   18.545 1.00 75.41  ? 16  LYS A CE  1 
ATOM   100 N NZ  . LYS A 1 16 ? -2.209 5.417   17.720 1.00 80.50  ? 16  LYS A NZ  1 
ATOM   101 N N   . TYR A 1 17 ? 4.418  6.658   16.594 1.00 44.60  ? 17  TYR A N   1 
ATOM   102 C CA  . TYR A 1 17 ? 4.325  7.613   15.500 1.00 46.78  ? 17  TYR A CA  1 
ATOM   103 C C   . TYR A 1 17 ? 5.588  7.601   14.649 1.00 45.18  ? 17  TYR A C   1 
ATOM   104 O O   . TYR A 1 17 ? 5.683  8.361   13.696 1.00 45.33  ? 17  TYR A O   1 
ATOM   105 C CB  . TYR A 1 17 ? 3.997  8.997   16.067 1.00 47.92  ? 17  TYR A CB  1 
ATOM   106 C CG  . TYR A 1 17 ? 2.628  9.014   16.725 1.00 48.86  ? 17  TYR A CG  1 
ATOM   107 C CD1 . TYR A 1 17 ? 1.474  8.987   15.965 1.00 51.72  ? 17  TYR A CD1 1 
ATOM   108 C CD2 . TYR A 1 17 ? 2.499  9.002   18.106 1.00 49.76  ? 17  TYR A CD2 1 
ATOM   109 C CE1 . TYR A 1 17 ? 0.225  8.963   16.558 1.00 55.47  ? 17  TYR A CE1 1 
ATOM   110 C CE2 . TYR A 1 17 ? 1.257  8.987   18.713 1.00 50.76  ? 17  TYR A CE2 1 
ATOM   111 C CZ  . TYR A 1 17 ? 0.119  8.959   17.936 1.00 53.21  ? 17  TYR A CZ  1 
ATOM   112 O OH  . TYR A 1 17 ? -1.095 8.943   18.550 1.00 58.77  ? 17  TYR A OH  1 
ATOM   113 N N   . LEU A 1 18 ? 6.549  6.738   14.990 1.00 44.10  ? 18  LEU A N   1 
ATOM   114 C CA  . LEU A 1 18 ? 7.728  6.558   14.164 1.00 44.73  ? 18  LEU A CA  1 
ATOM   115 C C   . LEU A 1 18 ? 7.315  5.808   12.911 1.00 47.84  ? 18  LEU A C   1 
ATOM   116 O O   . LEU A 1 18 ? 6.419  4.975   12.980 1.00 48.50  ? 18  LEU A O   1 
ATOM   117 C CB  . LEU A 1 18 ? 8.821  5.769   14.880 1.00 44.35  ? 18  LEU A CB  1 
ATOM   118 C CG  . LEU A 1 18 ? 9.538  6.473   16.031 1.00 44.38  ? 18  LEU A CG  1 
ATOM   119 C CD1 . LEU A 1 18 ? 10.646 5.572   16.541 1.00 43.08  ? 18  LEU A CD1 1 
ATOM   120 C CD2 . LEU A 1 18 ? 10.071 7.827   15.586 1.00 45.88  ? 18  LEU A CD2 1 
ATOM   121 N N   . PRO A 1 19 ? 8.005  6.018   11.767 1.00 50.74  ? 19  PRO A N   1 
ATOM   122 C CA  . PRO A 1 19 ? 7.843  5.116   10.632 1.00 54.34  ? 19  PRO A CA  1 
ATOM   123 C C   . PRO A 1 19 ? 8.159  3.679   11.046 1.00 55.65  ? 19  PRO A C   1 
ATOM   124 O O   . PRO A 1 19 ? 9.037  3.466   11.885 1.00 49.77  ? 19  PRO A O   1 
ATOM   125 C CB  . PRO A 1 19 ? 8.784  5.666   9.560  1.00 54.38  ? 19  PRO A CB  1 
ATOM   126 C CG  . PRO A 1 19 ? 9.358  6.965   10.107 1.00 52.91  ? 19  PRO A CG  1 
ATOM   127 C CD  . PRO A 1 19 ? 9.025  7.062   11.570 1.00 49.08  ? 19  PRO A CD  1 
ATOM   128 N N   . GLN A 1 20 ? 7.410  2.713   10.489 1.00 59.91  ? 20  GLN A N   1 
ATOM   129 C CA  . GLN A 1 20 ? 7.476  1.310   10.890 1.00 62.06  ? 20  GLN A CA  1 
ATOM   130 C C   . GLN A 1 20 ? 8.907  0.770   10.790 1.00 56.08  ? 20  GLN A C   1 
ATOM   131 O O   . GLN A 1 20 ? 9.340  -0.014  11.627 1.00 53.58  ? 20  GLN A O   1 
ATOM   132 C CB  . GLN A 1 20 ? 6.509  0.497   10.021 1.00 70.18  ? 20  GLN A CB  1 
ATOM   133 C CG  . GLN A 1 20 ? 6.535  -1.009  10.271 1.00 75.73  ? 20  GLN A CG  1 
ATOM   134 C CD  . GLN A 1 20 ? 6.036  -1.413  11.644 1.00 81.11  ? 20  GLN A CD  1 
ATOM   135 O OE1 . GLN A 1 20 ? 6.629  -1.088  12.679 1.00 83.26  ? 20  GLN A OE1 1 
ATOM   136 N NE2 . GLN A 1 20 ? 4.941  -2.162  11.664 1.00 88.08  ? 20  GLN A NE2 1 
ATOM   137 N N   . GLN A 1 21 ? 9.629  1.199   9.754  1.00 57.78  ? 21  GLN A N   1 
ATOM   138 C CA  . GLN A 1 21 ? 11.007 0.801   9.529  1.00 60.81  ? 21  GLN A CA  1 
ATOM   139 C C   . GLN A 1 21 ? 11.888 1.190   10.723 1.00 55.50  ? 21  GLN A C   1 
ATOM   140 O O   . GLN A 1 21 ? 12.772 0.436   11.119 1.00 53.84  ? 21  GLN A O   1 
ATOM   141 C CB  . GLN A 1 21 ? 11.441 1.477   8.230  1.00 68.10  ? 21  GLN A CB  1 
ATOM   142 C CG  . GLN A 1 21 ? 12.560 0.749   7.502  1.00 76.78  ? 21  GLN A CG  1 
ATOM   143 C CD  . GLN A 1 21 ? 13.029 1.490   6.269  1.00 87.70  ? 21  GLN A CD  1 
ATOM   144 O OE1 . GLN A 1 21 ? 12.533 2.580   5.954  1.00 95.28  ? 21  GLN A OE1 1 
ATOM   145 N NE2 . GLN A 1 21 ? 13.991 0.908   5.561  1.00 88.71  ? 21  GLN A NE2 1 
ATOM   146 N N   . GLN A 1 22 ? 11.634 2.364   11.311 1.00 51.14  ? 22  GLN A N   1 
ATOM   147 C CA  . GLN A 1 22 ? 12.430 2.847   12.427 1.00 48.79  ? 22  GLN A CA  1 
ATOM   148 C C   . GLN A 1 22 ? 12.063 2.081   13.690 1.00 47.47  ? 22  GLN A C   1 
ATOM   149 O O   . GLN A 1 22 ? 12.948 1.742   14.474 1.00 41.54  ? 22  GLN A O   1 
ATOM   150 C CB  . GLN A 1 22 ? 12.273 4.353   12.650 1.00 47.35  ? 22  GLN A CB  1 
ATOM   151 C CG  . GLN A 1 22 ? 12.877 5.194   11.531 1.00 51.13  ? 22  GLN A CG  1 
ATOM   152 C CD  . GLN A 1 22 ? 12.816 6.682   11.794 1.00 51.08  ? 22  GLN A CD  1 
ATOM   153 O OE1 . GLN A 1 22 ? 12.771 7.136   12.942 1.00 53.58  ? 22  GLN A OE1 1 
ATOM   154 N NE2 . GLN A 1 22 ? 12.839 7.453   10.721 1.00 50.49  ? 22  GLN A NE2 1 
ATOM   155 N N   . LYS A 1 23 ? 10.763 1.801   13.869 1.00 48.17  ? 23  LYS A N   1 
ATOM   156 C CA  . LYS A 1 23 ? 10.333 1.019   15.017 1.00 50.08  ? 23  LYS A CA  1 
ATOM   157 C C   . LYS A 1 23 ? 11.039 -0.335  14.997 1.00 46.26  ? 23  LYS A C   1 
ATOM   158 O O   . LYS A 1 23 ? 11.563 -0.774  16.010 1.00 47.29  ? 23  LYS A O   1 
ATOM   159 C CB  . LYS A 1 23 ? 8.818  0.801   15.096 1.00 54.42  ? 23  LYS A CB  1 
ATOM   160 C CG  . LYS A 1 23 ? 8.397  0.087   16.380 1.00 59.51  ? 23  LYS A CG  1 
ATOM   161 C CD  . LYS A 1 23 ? 6.906  -0.210  16.507 1.00 69.44  ? 23  LYS A CD  1 
ATOM   162 C CE  . LYS A 1 23 ? 6.531  -0.818  17.831 1.00 72.66  ? 23  LYS A CE  1 
ATOM   163 N NZ  . LYS A 1 23 ? 5.198  -1.432  17.798 1.00 76.68  ? 23  LYS A NZ  1 
ATOM   164 N N   . LYS A 1 24 ? 11.062 -0.987  13.837 1.00 51.56  ? 24  LYS A N   1 
ATOM   165 C CA  . LYS A 1 24 ? 11.653 -2.311  13.725 1.00 54.92  ? 24  LYS A CA  1 
ATOM   166 C C   . LYS A 1 24 ? 13.165 -2.247  13.938 1.00 51.99  ? 24  LYS A C   1 
ATOM   167 O O   . LYS A 1 24 ? 13.744 -3.144  14.551 1.00 49.40  ? 24  LYS A O   1 
ATOM   168 C CB  . LYS A 1 24 ? 11.258 -2.960  12.393 1.00 61.59  ? 24  LYS A CB  1 
ATOM   169 C CG  . LYS A 1 24 ? 9.810  -3.415  12.378 1.00 69.68  ? 24  LYS A CG  1 
ATOM   170 C CD  . LYS A 1 24 ? 9.259  -3.977  11.071 1.00 78.09  ? 24  LYS A CD  1 
ATOM   171 C CE  . LYS A 1 24 ? 7.850  -4.461  11.275 1.00 81.90  ? 24  LYS A CE  1 
ATOM   172 N NZ  . LYS A 1 24 ? 7.180  -4.813  10.021 1.00 88.32  ? 24  LYS A NZ  1 
ATOM   173 N N   . LYS A 1 25 ? 13.814 -1.179  13.451 1.00 49.49  ? 25  LYS A N   1 
ATOM   174 C CA  . LYS A 1 25 ? 15.245 -1.042  13.664 1.00 45.37  ? 25  LYS A CA  1 
ATOM   175 C C   . LYS A 1 25 ? 15.526 -0.823  15.151 1.00 41.86  ? 25  LYS A C   1 
ATOM   176 O O   . LYS A 1 25 ? 16.538 -1.300  15.658 1.00 42.63  ? 25  LYS A O   1 
ATOM   177 C CB  . LYS A 1 25 ? 15.851 0.056   12.784 1.00 46.84  ? 25  LYS A CB  1 
ATOM   178 C CG  . LYS A 1 25 ? 17.369 0.113   12.818 1.00 46.57  ? 25  LYS A CG  1 
ATOM   179 C CD  . LYS A 1 25 ? 18.019 -1.151  12.274 1.00 48.13  ? 25  LYS A CD  1 
ATOM   180 C CE  . LYS A 1 25 ? 19.495 -1.016  12.175 1.00 47.45  ? 25  LYS A CE  1 
ATOM   181 N NZ  . LYS A 1 25 ? 20.067 -2.279  11.714 1.00 51.06  ? 25  LYS A NZ  1 
ATOM   182 N N   . LEU A 1 26 ? 14.649 -0.081  15.844 1.00 41.47  ? 26  LEU A N   1 
ATOM   183 C CA  A LEU A 1 26 ? 14.775 0.101   17.278 0.50 39.95  ? 26  LEU A CA  1 
ATOM   184 C CA  B LEU A 1 26 ? 14.773 0.101   17.285 0.50 40.13  ? 26  LEU A CA  1 
ATOM   185 C C   . LEU A 1 26 ? 14.733 -1.269  17.956 1.00 42.09  ? 26  LEU A C   1 
ATOM   186 O O   . LEU A 1 26 ? 15.607 -1.609  18.740 1.00 44.11  ? 26  LEU A O   1 
ATOM   187 C CB  A LEU A 1 26 ? 13.640 1.020   17.730 0.50 39.65  ? 26  LEU A CB  1 
ATOM   188 C CB  B LEU A 1 26 ? 13.686 1.002   17.876 0.50 39.89  ? 26  LEU A CB  1 
ATOM   189 C CG  A LEU A 1 26 ? 13.860 1.797   19.028 0.50 36.84  ? 26  LEU A CG  1 
ATOM   190 C CG  B LEU A 1 26 ? 13.905 2.514   17.798 0.50 38.18  ? 26  LEU A CG  1 
ATOM   191 C CD1 A LEU A 1 26 ? 14.903 2.891   18.852 0.50 36.72  ? 26  LEU A CD1 1 
ATOM   192 C CD1 B LEU A 1 26 ? 12.736 3.221   18.461 0.50 38.66  ? 26  LEU A CD1 1 
ATOM   193 C CD2 A LEU A 1 26 ? 12.543 2.381   19.500 0.50 37.82  ? 26  LEU A CD2 1 
ATOM   194 C CD2 B LEU A 1 26 ? 15.215 2.945   18.440 0.50 37.82  ? 26  LEU A CD2 1 
ATOM   195 N N   . GLN A 1 27 ? 13.708 -2.062  17.622 1.00 43.56  ? 27  GLN A N   1 
ATOM   196 C CA  . GLN A 1 27 ? 13.530 -3.394  18.176 1.00 46.38  ? 27  GLN A CA  1 
ATOM   197 C C   . GLN A 1 27 ? 14.754 -4.265  17.903 1.00 45.37  ? 27  GLN A C   1 
ATOM   198 O O   . GLN A 1 27 ? 15.298 -4.860  18.826 1.00 46.42  ? 27  GLN A O   1 
ATOM   199 C CB  . GLN A 1 27 ? 12.252 -4.040  17.625 1.00 47.92  ? 27  GLN A CB  1 
ATOM   200 C CG  . GLN A 1 27 ? 10.972 -3.434  18.193 1.00 49.11  ? 27  GLN A CG  1 
ATOM   201 C CD  . GLN A 1 27 ? 9.719  -3.764  17.410 1.00 55.52  ? 27  GLN A CD  1 
ATOM   202 O OE1 . GLN A 1 27 ? 9.756  -4.210  16.259 1.00 60.59  ? 27  GLN A OE1 1 
ATOM   203 N NE2 . GLN A 1 27 ? 8.577  -3.524  18.028 1.00 58.52  ? 27  GLN A NE2 1 
ATOM   204 N N   . THR A 1 28 ? 15.189 -4.353  16.642 1.00 48.30  ? 28  THR A N   1 
ATOM   205 C CA  . THR A 1 28 ? 16.281 -5.254  16.299 1.00 50.10  ? 28  THR A CA  1 
ATOM   206 C C   . THR A 1 28 ? 17.583 -4.780  16.939 1.00 47.09  ? 28  THR A C   1 
ATOM   207 O O   . THR A 1 28 ? 18.376 -5.608  17.370 1.00 47.34  ? 28  THR A O   1 
ATOM   208 C CB  . THR A 1 28 ? 16.406 -5.419  14.785 1.00 56.87  ? 28  THR A CB  1 
ATOM   209 O OG1 . THR A 1 28 ? 16.608 -4.123  14.231 1.00 60.37  ? 28  THR A OG1 1 
ATOM   210 C CG2 . THR A 1 28 ? 15.179 -6.092  14.192 1.00 59.94  ? 28  THR A CG2 1 
ATOM   211 N N   . ASP A 1 29 ? 17.789 -3.457  17.022 1.00 44.48  ? 29  ASP A N   1 
ATOM   212 C CA  . ASP A 1 29 ? 18.940 -2.891  17.711 1.00 42.05  ? 29  ASP A CA  1 
ATOM   213 C C   . ASP A 1 29 ? 18.937 -3.325  19.172 1.00 40.43  ? 29  ASP A C   1 
ATOM   214 O O   . ASP A 1 29 ? 19.978 -3.675  19.712 1.00 41.44  ? 29  ASP A O   1 
ATOM   215 C CB  . ASP A 1 29 ? 18.964 -1.368  17.677 1.00 42.16  ? 29  ASP A CB  1 
ATOM   216 C CG  . ASP A 1 29 ? 19.534 -0.695  16.434 1.00 41.63  ? 29  ASP A CG  1 
ATOM   217 O OD1 . ASP A 1 29 ? 19.966 -1.414  15.524 1.00 41.33  ? 29  ASP A OD1 1 
ATOM   218 O OD2 . ASP A 1 29 ? 19.557 0.570   16.400 1.00 40.83  ? 29  ASP A OD2 1 
ATOM   219 N N   . ILE A 1 30 ? 17.776 -3.248  19.829 1.00 41.48  ? 30  ILE A N   1 
ATOM   220 C CA  . ILE A 1 30 ? 17.677 -3.645  21.226 1.00 43.65  ? 30  ILE A CA  1 
ATOM   221 C C   . ILE A 1 30 ? 17.932 -5.153  21.349 1.00 48.02  ? 30  ILE A C   1 
ATOM   222 O O   . ILE A 1 30 ? 18.768 -5.584  22.144 1.00 49.96  ? 30  ILE A O   1 
ATOM   223 C CB  . ILE A 1 30 ? 16.322 -3.218  21.822 1.00 44.91  ? 30  ILE A CB  1 
ATOM   224 C CG1 . ILE A 1 30 ? 16.240 -1.691  21.987 1.00 42.54  ? 30  ILE A CG1 1 
ATOM   225 C CG2 . ILE A 1 30 ? 16.064 -3.931  23.150 1.00 47.03  ? 30  ILE A CG2 1 
ATOM   226 C CD1 . ILE A 1 30 ? 14.838 -1.155  22.206 1.00 41.47  ? 30  ILE A CD1 1 
ATOM   227 N N   . LYS A 1 31 ? 17.242 -5.954  20.529 1.00 50.29  ? 31  LYS A N   1 
ATOM   228 C CA  . LYS A 1 31 ? 17.277 -7.405  20.668 1.00 56.29  ? 31  LYS A CA  1 
ATOM   229 C C   . LYS A 1 31 ? 18.665 -7.944  20.322 1.00 56.66  ? 31  LYS A C   1 
ATOM   230 O O   . LYS A 1 31 ? 19.193 -8.796  21.026 1.00 60.71  ? 31  LYS A O   1 
ATOM   231 C CB  . LYS A 1 31 ? 16.199 -8.049  19.787 1.00 62.70  ? 31  LYS A CB  1 
ATOM   232 C CG  . LYS A 1 31 ? 15.871 -9.512  20.103 1.00 72.43  ? 31  LYS A CG  1 
ATOM   233 C CD  . LYS A 1 31 ? 14.603 -10.016 19.413 1.00 77.05  ? 31  LYS A CD  1 
ATOM   234 C CE  . LYS A 1 31 ? 13.930 -11.167 20.102 1.00 82.15  ? 31  LYS A CE  1 
ATOM   235 N NZ  . LYS A 1 31 ? 14.680 -12.414 19.952 1.00 87.65  ? 31  LYS A NZ  1 
ATOM   236 N N   . GLU A 1 32 ? 19.275 -7.429  19.249 1.00 55.52  ? 32  GLU A N   1 
ATOM   237 C CA  . GLU A 1 32 ? 20.595 -7.874  18.834 1.00 57.67  ? 32  GLU A CA  1 
ATOM   238 C C   . GLU A 1 32 ? 21.688 -7.528  19.853 1.00 56.21  ? 32  GLU A C   1 
ATOM   239 O O   . GLU A 1 32 ? 22.785 -8.056  19.752 1.00 59.24  ? 32  GLU A O   1 
ATOM   240 C CB  . GLU A 1 32 ? 20.960 -7.246  17.493 1.00 60.58  ? 32  GLU A CB  1 
ATOM   241 C CG  . GLU A 1 32 ? 20.109 -7.748  16.330 1.00 66.86  ? 32  GLU A CG  1 
ATOM   242 C CD  . GLU A 1 32 ? 20.334 -6.942  15.060 1.00 70.11  ? 32  GLU A CD  1 
ATOM   243 O OE1 . GLU A 1 32 ? 21.131 -5.984  15.124 1.00 71.46  ? 32  GLU A OE1 1 
ATOM   244 O OE2 . GLU A 1 32 ? 19.736 -7.261  14.011 1.00 74.62  ? 32  GLU A OE2 1 
ATOM   245 N N   . ASN A 1 33 ? 21.418 -6.647  20.825 1.00 54.69  ? 33  ASN A N   1 
ATOM   246 C CA  . ASN A 1 33 ? 22.440 -6.213  21.768 1.00 52.80  ? 33  ASN A CA  1 
ATOM   247 C C   . ASN A 1 33 ? 22.029 -6.495  23.206 1.00 54.38  ? 33  ASN A C   1 
ATOM   248 O O   . ASN A 1 33 ? 22.377 -5.724  24.093 1.00 50.77  ? 33  ASN A O   1 
ATOM   249 C CB  . ASN A 1 33 ? 22.726 -4.727  21.618 1.00 49.81  ? 33  ASN A CB  1 
ATOM   250 C CG  . ASN A 1 33 ? 23.348 -4.451  20.276 1.00 50.51  ? 33  ASN A CG  1 
ATOM   251 O OD1 . ASN A 1 33 ? 24.542 -4.690  20.104 1.00 52.85  ? 33  ASN A OD1 1 
ATOM   252 N ND2 . ASN A 1 33 ? 22.560 -3.988  19.318 1.00 49.39  ? 33  ASN A ND2 1 
ATOM   253 N N   . GLY A 1 34 ? 21.286 -7.594  23.417 1.00 58.04  ? 34  GLY A N   1 
ATOM   254 C CA  . GLY A 1 34 ? 21.075 -8.157  24.743 1.00 57.72  ? 34  GLY A CA  1 
ATOM   255 C C   . GLY A 1 34 ? 19.853 -7.593  25.469 1.00 55.66  ? 34  GLY A C   1 
ATOM   256 O O   . GLY A 1 34 ? 19.654 -7.875  26.646 1.00 57.24  ? 34  GLY A O   1 
ATOM   257 N N   . GLY A 1 35 ? 19.031 -6.795  24.787 1.00 54.28  ? 35  GLY A N   1 
ATOM   258 C CA  . GLY A 1 35 ? 17.924 -6.119  25.453 1.00 54.40  ? 35  GLY A CA  1 
ATOM   259 C C   . GLY A 1 35 ? 16.641 -6.944  25.386 1.00 55.23  ? 35  GLY A C   1 
ATOM   260 O O   . GLY A 1 35 ? 16.528 -7.841  24.558 1.00 57.42  ? 35  GLY A O   1 
ATOM   261 N N   . LYS A 1 36 ? 15.672 -6.611  26.243 1.00 56.75  ? 36  LYS A N   1 
ATOM   262 C CA  . LYS A 1 36 ? 14.389 -7.297  26.263 1.00 62.58  ? 36  LYS A CA  1 
ATOM   263 C C   . LYS A 1 36 ? 13.266 -6.291  26.018 1.00 58.96  ? 36  LYS A C   1 
ATOM   264 O O   . LYS A 1 36 ? 13.502 -5.091  26.046 1.00 52.77  ? 36  LYS A O   1 
ATOM   265 C CB  . LYS A 1 36 ? 14.192 -7.982  27.618 1.00 68.68  ? 36  LYS A CB  1 
ATOM   266 C CG  . LYS A 1 36 ? 15.215 -9.042  27.979 1.00 74.04  ? 36  LYS A CG  1 
ATOM   267 C CD  . LYS A 1 36 ? 15.125 -10.285 27.109 1.00 78.52  ? 36  LYS A CD  1 
ATOM   268 C CE  . LYS A 1 36 ? 15.751 -11.453 27.785 1.00 85.51  ? 36  LYS A CE  1 
ATOM   269 N NZ  . LYS A 1 36 ? 15.760 -12.610 26.891 1.00 91.44  ? 36  LYS A NZ  1 
ATOM   270 N N   . PHE A 1 37 ? 12.042 -6.803  25.826 1.00 65.78  ? 37  PHE A N   1 
ATOM   271 C CA  . PHE A 1 37 ? 10.878 -5.982  25.528 1.00 66.55  ? 37  PHE A CA  1 
ATOM   272 C C   . PHE A 1 37 ? 9.727  -6.254  26.489 1.00 70.67  ? 37  PHE A C   1 
ATOM   273 O O   . PHE A 1 37 ? 9.522  -7.389  26.917 1.00 71.42  ? 37  PHE A O   1 
ATOM   274 C CB  . PHE A 1 37 ? 10.283 -6.266  24.151 1.00 64.88  ? 37  PHE A CB  1 
ATOM   275 C CG  . PHE A 1 37 ? 11.281 -5.966  23.051 1.00 69.21  ? 37  PHE A CG  1 
ATOM   276 C CD1 . PHE A 1 37 ? 11.587 -4.653  22.725 1.00 61.81  ? 37  PHE A CD1 1 
ATOM   277 C CD2 . PHE A 1 37 ? 11.941 -6.996  22.393 1.00 71.59  ? 37  PHE A CD2 1 
ATOM   278 C CE1 . PHE A 1 37 ? 12.508 -4.383  21.735 1.00 65.79  ? 37  PHE A CE1 1 
ATOM   279 C CE2 . PHE A 1 37 ? 12.861 -6.716  21.402 1.00 72.36  ? 37  PHE A CE2 1 
ATOM   280 C CZ  . PHE A 1 37 ? 13.147 -5.411  21.082 1.00 68.44  ? 37  PHE A CZ  1 
ATOM   281 N N   A SER A 1 38 ? 8.976  -5.188  26.793 0.50 70.19  ? 38  SER A N   1 
ATOM   282 N N   B SER A 1 38 ? 8.976  -5.188  26.793 0.50 70.19  ? 38  SER A N   1 
ATOM   283 C CA  A SER A 1 38 ? 7.709  -5.284  27.495 0.50 71.61  ? 38  SER A CA  1 
ATOM   284 C CA  B SER A 1 38 ? 7.709  -5.284  27.495 0.50 71.61  ? 38  SER A CA  1 
ATOM   285 C C   A SER A 1 38 ? 6.671  -4.465  26.732 0.50 69.73  ? 38  SER A C   1 
ATOM   286 C C   B SER A 1 38 ? 6.671  -4.465  26.732 0.50 69.73  ? 38  SER A C   1 
ATOM   287 O O   A SER A 1 38 ? 6.873  -3.276  26.509 0.50 66.00  ? 38  SER A O   1 
ATOM   288 O O   B SER A 1 38 ? 6.873  -3.276  26.509 0.50 66.00  ? 38  SER A O   1 
ATOM   289 C CB  A SER A 1 38 ? 7.836  -4.821  28.928 0.50 71.64  ? 38  SER A CB  1 
ATOM   290 C CB  B SER A 1 38 ? 7.836  -4.821  28.928 0.50 71.64  ? 38  SER A CB  1 
ATOM   291 O OG  A SER A 1 38 ? 6.622  -5.029  29.641 0.50 70.77  ? 38  SER A OG  1 
ATOM   292 O OG  B SER A 1 38 ? 6.622  -5.029  29.641 0.50 70.77  ? 38  SER A OG  1 
ATOM   293 N N   . GLN A 1 39 ? 5.577  -5.122  26.323 1.00 73.16  ? 39  GLN A N   1 
ATOM   294 C CA  . GLN A 1 39 ? 4.520  -4.498  25.536 1.00 70.71  ? 39  GLN A CA  1 
ATOM   295 C C   . GLN A 1 39 ? 3.974  -3.261  26.248 1.00 62.79  ? 39  GLN A C   1 
ATOM   296 O O   . GLN A 1 39 ? 3.991  -2.154  25.703 1.00 56.41  ? 39  GLN A O   1 
ATOM   297 C CB  . GLN A 1 39 ? 3.414  -5.521  25.263 1.00 75.05  ? 39  GLN A CB  1 
ATOM   298 C CG  . GLN A 1 39 ? 2.081  -4.910  24.844 1.00 80.17  ? 39  GLN A CG  1 
ATOM   299 C CD  . GLN A 1 39 ? 1.171  -5.888  24.128 1.00 94.76  ? 39  GLN A CD  1 
ATOM   300 O OE1 . GLN A 1 39 ? 0.635  -6.840  24.712 1.00 98.36  ? 39  GLN A OE1 1 
ATOM   301 N NE2 . GLN A 1 39 ? 0.985  -5.653  22.837 1.00 100.21 ? 39  GLN A NE2 1 
ATOM   302 N N   . SER A 1 40 ? 3.461  -3.481  27.461 1.00 65.53  ? 40  SER A N   1 
ATOM   303 C CA  . SER A 1 40 ? 2.938  -2.402  28.277 1.00 64.51  ? 40  SER A CA  1 
ATOM   304 C C   . SER A 1 40 ? 3.925  -2.098  29.399 1.00 62.67  ? 40  SER A C   1 
ATOM   305 O O   . SER A 1 40 ? 4.811  -2.898  29.696 1.00 61.15  ? 40  SER A O   1 
ATOM   306 C CB  . SER A 1 40 ? 1.568  -2.743  28.810 1.00 69.89  ? 40  SER A CB  1 
ATOM   307 O OG  . SER A 1 40 ? 0.560  -2.561  27.824 1.00 67.01  ? 40  SER A OG  1 
ATOM   308 N N   . LEU A 1 41 ? 3.765  -0.915  29.995 1.00 58.14  ? 41  LEU A N   1 
ATOM   309 C CA  . LEU A 1 41 ? 4.602  -0.472  31.096 1.00 51.47  ? 41  LEU A CA  1 
ATOM   310 C C   . LEU A 1 41 ? 4.288  -1.321  32.323 1.00 49.74  ? 41  LEU A C   1 
ATOM   311 O O   . LEU A 1 41 ? 3.128  -1.494  32.680 1.00 51.39  ? 41  LEU A O   1 
ATOM   312 C CB  . LEU A 1 41 ? 4.323  1.014   31.332 1.00 48.78  ? 41  LEU A CB  1 
ATOM   313 C CG  . LEU A 1 41 ? 5.046  1.674   32.509 1.00 47.19  ? 41  LEU A CG  1 
ATOM   314 C CD1 . LEU A 1 41 ? 6.536  1.711   32.220 1.00 45.12  ? 41  LEU A CD1 1 
ATOM   315 C CD2 . LEU A 1 41 ? 4.477  3.065   32.791 1.00 45.54  ? 41  LEU A CD2 1 
ATOM   316 N N   . ASN A 1 42 ? 5.323  -1.866  32.959 1.00 48.69  ? 42  ASN A N   1 
ATOM   317 C CA  . ASN A 1 42 ? 5.124  -2.622  34.186 1.00 52.53  ? 42  ASN A CA  1 
ATOM   318 C C   . ASN A 1 42 ? 6.369  -2.464  35.056 1.00 52.82  ? 42  ASN A C   1 
ATOM   319 O O   . ASN A 1 42 ? 7.360  -1.909  34.598 1.00 48.90  ? 42  ASN A O   1 
ATOM   320 C CB  . ASN A 1 42 ? 4.751  -4.074  33.895 1.00 56.32  ? 42  ASN A CB  1 
ATOM   321 C CG  . ASN A 1 42 ? 5.821  -4.835  33.145 1.00 57.48  ? 42  ASN A CG  1 
ATOM   322 O OD1 . ASN A 1 42 ? 7.014  -4.771  33.470 1.00 55.71  ? 42  ASN A OD1 1 
ATOM   323 N ND2 . ASN A 1 42 ? 5.397  -5.586  32.142 1.00 59.54  ? 42  ASN A ND2 1 
ATOM   324 N N   . PRO A 1 43 ? 6.363  -2.940  36.321 1.00 54.85  ? 43  PRO A N   1 
ATOM   325 C CA  . PRO A 1 43 ? 7.498  -2.747  37.217 1.00 56.68  ? 43  PRO A CA  1 
ATOM   326 C C   . PRO A 1 43 ? 8.815  -3.380  36.764 1.00 59.16  ? 43  PRO A C   1 
ATOM   327 O O   . PRO A 1 43 ? 9.862  -2.973  37.247 1.00 63.63  ? 43  PRO A O   1 
ATOM   328 C CB  . PRO A 1 43 ? 7.026  -3.351  38.543 1.00 60.48  ? 43  PRO A CB  1 
ATOM   329 C CG  . PRO A 1 43 ? 5.507  -3.356  38.424 1.00 61.95  ? 43  PRO A CG  1 
ATOM   330 C CD  . PRO A 1 43 ? 5.239  -3.625  36.973 1.00 59.04  ? 43  PRO A CD  1 
ATOM   331 N N   . GLN A 1 44 ? 8.778  -4.382  35.872 1.00 61.87  ? 44  GLN A N   1 
ATOM   332 C CA  . GLN A 1 44 ? 9.994  -5.057  35.427 1.00 61.63  ? 44  GLN A CA  1 
ATOM   333 C C   . GLN A 1 44 ? 10.759 -4.220  34.395 1.00 54.78  ? 44  GLN A C   1 
ATOM   334 O O   . GLN A 1 44 ? 11.920 -4.513  34.131 1.00 52.50  ? 44  GLN A O   1 
ATOM   335 C CB  . GLN A 1 44 ? 9.733  -6.446  34.835 1.00 66.08  ? 44  GLN A CB  1 
ATOM   336 C CG  . GLN A 1 44 ? 9.449  -7.543  35.860 1.00 72.82  ? 44  GLN A CG  1 
ATOM   337 C CD  . GLN A 1 44 ? 8.129  -7.369  36.577 1.00 75.81  ? 44  GLN A CD  1 
ATOM   338 O OE1 . GLN A 1 44 ? 7.070  -7.219  35.957 1.00 77.63  ? 44  GLN A OE1 1 
ATOM   339 N NE2 . GLN A 1 44 ? 8.180  -7.372  37.902 1.00 79.09  ? 44  GLN A NE2 1 
ATOM   340 N N   . CYS A 1 45 ? 10.106 -3.210  33.791 1.00 49.60  ? 45  CYS A N   1 
ATOM   341 C CA  . CYS A 1 45 ? 10.746 -2.335  32.816 1.00 44.16  ? 45  CYS A CA  1 
ATOM   342 C C   . CYS A 1 45 ? 11.850 -1.505  33.487 1.00 44.66  ? 45  CYS A C   1 
ATOM   343 O O   . CYS A 1 45 ? 11.637 -0.930  34.547 1.00 45.05  ? 45  CYS A O   1 
ATOM   344 C CB  . CYS A 1 45 ? 9.738  -1.421  32.112 1.00 39.83  ? 45  CYS A CB  1 
ATOM   345 S SG  . CYS A 1 45 ? 8.436  -2.283  31.175 0.47 33.86  ? 45  CYS A SG  1 
ATOM   346 N N   . THR A 1 46 ? 13.021 -1.439  32.845 1.00 43.18  ? 46  THR A N   1 
ATOM   347 C CA  . THR A 1 46 ? 14.117 -0.580  33.274 1.00 44.69  ? 46  THR A CA  1 
ATOM   348 C C   . THR A 1 46 ? 14.058 0.745   32.516 1.00 44.25  ? 46  THR A C   1 
ATOM   349 O O   . THR A 1 46 ? 14.540 1.769   33.004 1.00 44.29  ? 46  THR A O   1 
ATOM   350 C CB  . THR A 1 46 ? 15.457 -1.288  33.050 1.00 44.29  ? 46  THR A CB  1 
ATOM   351 O OG1 . THR A 1 46 ? 15.520 -1.620  31.666 1.00 42.94  ? 46  THR A OG1 1 
ATOM   352 C CG2 . THR A 1 46 ? 15.600 -2.551  33.891 1.00 48.45  ? 46  THR A CG2 1 
ATOM   353 N N   . HIS A 1 47 ? 13.453 0.706   31.320 1.00 43.44  ? 47  HIS A N   1 
ATOM   354 C CA  . HIS A 1 47 ? 13.449 1.826   30.400 1.00 42.26  ? 47  HIS A CA  1 
ATOM   355 C C   . HIS A 1 47 ? 12.093 1.933   29.699 1.00 41.54  ? 47  HIS A C   1 
ATOM   356 O O   . HIS A 1 47 ? 11.476 0.922   29.382 1.00 39.14  ? 47  HIS A O   1 
ATOM   357 C CB  . HIS A 1 47 ? 14.525 1.613   29.329 1.00 42.90  ? 47  HIS A CB  1 
ATOM   358 C CG  . HIS A 1 47 ? 15.935 1.707   29.811 1.00 43.31  ? 47  HIS A CG  1 
ATOM   359 N ND1 . HIS A 1 47 ? 16.578 0.691   30.485 1.00 42.84  ? 47  HIS A ND1 1 
ATOM   360 C CD2 . HIS A 1 47 ? 16.832 2.708   29.693 1.00 43.12  ? 47  HIS A CD2 1 
ATOM   361 C CE1 . HIS A 1 47 ? 17.824 1.073   30.760 1.00 46.08  ? 47  HIS A CE1 1 
ATOM   362 N NE2 . HIS A 1 47 ? 18.000 2.299   30.282 1.00 43.79  ? 47  HIS A NE2 1 
ATOM   363 N N   . ILE A 1 48 ? 11.664 3.172   29.425 1.00 41.71  ? 48  ILE A N   1 
ATOM   364 C CA  . ILE A 1 48 ? 10.573 3.422   28.499 1.00 40.79  ? 48  ILE A CA  1 
ATOM   365 C C   . ILE A 1 48 ? 11.065 4.427   27.467 1.00 40.22  ? 48  ILE A C   1 
ATOM   366 O O   . ILE A 1 48 ? 11.551 5.501   27.836 1.00 36.69  ? 48  ILE A O   1 
ATOM   367 C CB  . ILE A 1 48 ? 9.279  3.884   29.199 1.00 42.71  ? 48  ILE A CB  1 
ATOM   368 C CG1 . ILE A 1 48 ? 8.133  4.052   28.195 1.00 48.54  ? 48  ILE A CG1 1 
ATOM   369 C CG2 . ILE A 1 48 ? 9.476  5.154   30.018 1.00 41.24  ? 48  ILE A CG2 1 
ATOM   370 C CD1 . ILE A 1 48 ? 6.775  4.290   28.844 1.00 50.25  ? 48  ILE A CD1 1 
ATOM   371 N N   . ILE A 1 49 ? 10.937 4.025   26.189 1.00 38.48  ? 49  ILE A N   1 
ATOM   372 C CA  . ILE A 1 49 ? 11.353 4.820   25.049 1.00 36.91  ? 49  ILE A CA  1 
ATOM   373 C C   . ILE A 1 49 ? 10.124 5.519   24.469 1.00 36.43  ? 49  ILE A C   1 
ATOM   374 O O   . ILE A 1 49 ? 9.190  4.857   24.019 1.00 37.28  ? 49  ILE A O   1 
ATOM   375 C CB  . ILE A 1 49 ? 12.049 3.957   23.981 1.00 35.98  ? 49  ILE A CB  1 
ATOM   376 C CG1 . ILE A 1 49 ? 13.209 3.120   24.558 1.00 37.31  ? 49  ILE A CG1 1 
ATOM   377 C CG2 . ILE A 1 49 ? 12.482 4.818   22.791 1.00 34.79  ? 49  ILE A CG2 1 
ATOM   378 C CD1 . ILE A 1 49 ? 14.315 3.916   25.236 1.00 36.93  ? 49  ILE A CD1 1 
ATOM   379 N N   A LEU A 1 50 ? 10.195 6.849   24.399 0.50 35.52  ? 50  LEU A N   1 
ATOM   380 N N   B LEU A 1 50 ? 10.124 6.860   24.541 0.50 35.21  ? 50  LEU A N   1 
ATOM   381 C CA  A LEU A 1 50 ? 9.080  7.679   23.986 0.50 36.20  ? 50  LEU A CA  1 
ATOM   382 C CA  B LEU A 1 50 ? 9.085  7.698   23.959 0.50 35.50  ? 50  LEU A CA  1 
ATOM   383 C C   A LEU A 1 50 ? 9.503  8.513   22.783 0.50 37.28  ? 50  LEU A C   1 
ATOM   384 C C   B LEU A 1 50 ? 9.632  8.357   22.703 0.50 36.43  ? 50  LEU A C   1 
ATOM   385 O O   A LEU A 1 50 ? 10.416 9.330   22.910 0.50 36.14  ? 50  LEU A O   1 
ATOM   386 O O   B LEU A 1 50 ? 10.722 8.921   22.728 0.50 34.87  ? 50  LEU A O   1 
ATOM   387 C CB  A LEU A 1 50 ? 8.749  8.549   25.198 0.50 36.46  ? 50  LEU A CB  1 
ATOM   388 C CB  B LEU A 1 50 ? 8.607  8.811   24.891 0.50 35.53  ? 50  LEU A CB  1 
ATOM   389 C CG  A LEU A 1 50 ? 7.386  9.239   25.209 0.50 37.63  ? 50  LEU A CG  1 
ATOM   390 C CG  B LEU A 1 50 ? 8.009  8.393   26.232 0.50 35.96  ? 50  LEU A CG  1 
ATOM   391 C CD1 A LEU A 1 50 ? 6.270  8.232   25.423 0.50 38.41  ? 50  LEU A CD1 1 
ATOM   392 C CD1 B LEU A 1 50 ? 7.646  9.639   27.017 0.50 39.33  ? 50  LEU A CD1 1 
ATOM   393 C CD2 A LEU A 1 50 ? 7.371  10.322  26.279 0.50 39.15  ? 50  LEU A CD2 1 
ATOM   394 C CD2 B LEU A 1 50 ? 6.804  7.500   26.034 0.50 37.20  ? 50  LEU A CD2 1 
ATOM   395 N N   . ASP A 1 51 ? 8.832  8.315   21.635 1.00 39.03  ? 51  ASP A N   1 
ATOM   396 C CA  . ASP A 1 51 ? 8.997  9.214   20.505 1.00 36.63  ? 51  ASP A CA  1 
ATOM   397 C C   . ASP A 1 51 ? 8.358  10.556  20.871 1.00 37.82  ? 51  ASP A C   1 
ATOM   398 O O   . ASP A 1 51 ? 7.680  10.686  21.899 1.00 33.45  ? 51  ASP A O   1 
ATOM   399 C CB  . ASP A 1 51 ? 8.498  8.596   19.207 1.00 36.35  ? 51  ASP A CB  1 
ATOM   400 C CG  . ASP A 1 51 ? 7.000  8.378   19.105 1.00 39.03  ? 51  ASP A CG  1 
ATOM   401 O OD1 . ASP A 1 51 ? 6.290  8.726   20.056 1.00 41.50  ? 51  ASP A OD1 1 
ATOM   402 O OD2 . ASP A 1 51 ? 6.554  7.848   18.076 1.00 39.91  ? 51  ASP A OD2 1 
ATOM   403 N N   . ASN A 1 52 ? 8.569  11.545  19.994 1.00 40.22  ? 52  ASN A N   1 
ATOM   404 C CA  . ASN A 1 52 ? 8.227  12.940  20.238 1.00 43.74  ? 52  ASN A CA  1 
ATOM   405 C C   . ASN A 1 52 ? 6.730  13.169  20.442 1.00 40.61  ? 52  ASN A C   1 
ATOM   406 O O   . ASN A 1 52 ? 6.337  14.001  21.254 1.00 40.68  ? 52  ASN A O   1 
ATOM   407 C CB  . ASN A 1 52 ? 8.676  13.815  19.071 1.00 52.80  ? 52  ASN A CB  1 
ATOM   408 C CG  . ASN A 1 52 ? 9.990  14.506  19.343 1.00 62.99  ? 52  ASN A CG  1 
ATOM   409 O OD1 . ASN A 1 52 ? 10.054 15.413  20.182 1.00 72.89  ? 52  ASN A OD1 1 
ATOM   410 N ND2 . ASN A 1 52 ? 11.035 14.118  18.629 1.00 66.05  ? 52  ASN A ND2 1 
ATOM   411 N N   . ALA A 1 53 ? 5.899  12.482  19.655 1.00 40.31  ? 53  ALA A N   1 
ATOM   412 C CA  . ALA A 1 53 ? 4.465  12.734  19.637 1.00 40.52  ? 53  ALA A CA  1 
ATOM   413 C C   . ALA A 1 53 ? 3.726  11.916  20.698 1.00 40.53  ? 53  ALA A C   1 
ATOM   414 O O   . ALA A 1 53 ? 2.550  12.181  20.963 1.00 45.43  ? 53  ALA A O   1 
ATOM   415 C CB  . ALA A 1 53 ? 3.937  12.458  18.249 1.00 43.80  ? 53  ALA A CB  1 
ATOM   416 N N   . ASP A 1 54 ? 4.414  10.957  21.337 0.76 36.99  ? 54  ASP A N   1 
ATOM   417 C CA  . ASP A 1 54 ? 3.804  10.156  22.383 1.00 38.31  ? 54  ASP A CA  1 
ATOM   418 C C   . ASP A 1 54 ? 3.889  10.859  23.740 0.76 40.39  ? 54  ASP A C   1 
ATOM   419 O O   . ASP A 1 54 ? 4.919  11.426  24.082 0.76 37.07  ? 54  ASP A O   1 
ATOM   420 C CB  . ASP A 1 54 ? 4.473  8.800   22.520 1.00 39.67  ? 54  ASP A CB  1 
ATOM   421 C CG  . ASP A 1 54 ? 3.826  7.693   21.709 1.00 44.51  ? 54  ASP A CG  1 
ATOM   422 O OD1 . ASP A 1 54 ? 4.070  7.631   20.485 1.00 43.77  ? 54  ASP A OD1 1 
ATOM   423 O OD2 . ASP A 1 54 ? 3.033  6.947   22.319 1.00 49.34  ? 54  ASP A OD2 1 
ATOM   424 N N   . VAL A 1 55 ? 2.824  10.748  24.543 1.00 43.93  ? 55  VAL A N   1 
ATOM   425 C CA  . VAL A 1 55 ? 2.789  11.334  25.879 1.00 46.14  ? 55  VAL A CA  1 
ATOM   426 C C   . VAL A 1 55 ? 2.489  10.236  26.895 1.00 45.99  ? 55  VAL A C   1 
ATOM   427 O O   . VAL A 1 55 ? 2.042  9.146   26.536 1.00 45.61  ? 55  VAL A O   1 
ATOM   428 C CB  . VAL A 1 55 ? 1.778  12.485  26.008 1.00 49.14  ? 55  VAL A CB  1 
ATOM   429 C CG1 . VAL A 1 55 ? 2.095  13.617  25.043 1.00 52.17  ? 55  VAL A CG1 1 
ATOM   430 C CG2 . VAL A 1 55 ? 0.336  12.018  25.826 1.00 51.81  ? 55  VAL A CG2 1 
ATOM   431 N N   . LEU A 1 56 ? 2.784  10.533  28.162 1.00 43.95  ? 56  LEU A N   1 
ATOM   432 C CA  . LEU A 1 56 ? 2.489  9.631   29.258 1.00 43.92  ? 56  LEU A CA  1 
ATOM   433 C C   . LEU A 1 56 ? 1.489  10.308  30.180 1.00 46.95  ? 56  LEU A C   1 
ATOM   434 O O   . LEU A 1 56 ? 1.538  11.524  30.346 1.00 51.46  ? 56  LEU A O   1 
ATOM   435 C CB  . LEU A 1 56 ? 3.774  9.270   29.991 1.00 43.86  ? 56  LEU A CB  1 
ATOM   436 C CG  . LEU A 1 56 ? 4.809  8.498   29.172 1.00 41.84  ? 56  LEU A CG  1 
ATOM   437 C CD1 . LEU A 1 56 ? 6.113  8.422   29.937 1.00 44.56  ? 56  LEU A CD1 1 
ATOM   438 C CD2 . LEU A 1 56 ? 4.330  7.108   28.803 1.00 40.12  ? 56  LEU A CD2 1 
ATOM   439 N N   . SER A 1 57 ? 0.572  9.506   30.734 1.00 44.63  ? 57  SER A N   1 
ATOM   440 C CA  . SER A 1 57 ? -0.401 9.961   31.714 1.00 43.80  ? 57  SER A CA  1 
ATOM   441 C C   . SER A 1 57 ? 0.259  10.147  33.080 1.00 43.09  ? 57  SER A C   1 
ATOM   442 O O   . SER A 1 57 ? 1.359  9.646   33.337 1.00 41.46  ? 57  SER A O   1 
ATOM   443 C CB  . SER A 1 57 ? -1.577 8.984   31.839 1.00 43.45  ? 57  SER A CB  1 
ATOM   444 O OG  . SER A 1 57 ? -1.145 7.792   32.482 1.00 41.07  ? 57  SER A OG  1 
ATOM   445 N N   . GLN A 1 58 ? -0.470 10.816  33.982 1.00 44.21  ? 58  GLN A N   1 
ATOM   446 C CA  . GLN A 1 58 ? 0.001  10.981  35.346 1.00 46.95  ? 58  GLN A CA  1 
ATOM   447 C C   . GLN A 1 58 ? 0.182  9.593   35.956 1.00 45.37  ? 58  GLN A C   1 
ATOM   448 O O   . GLN A 1 58 ? 1.186  9.336   36.615 1.00 47.18  ? 58  GLN A O   1 
ATOM   449 C CB  . GLN A 1 58 ? -0.954 11.873  36.149 1.00 51.73  ? 58  GLN A CB  1 
ATOM   450 C CG  . GLN A 1 58 ? -0.347 12.395  37.448 1.00 55.92  ? 58  GLN A CG  1 
ATOM   451 C CD  . GLN A 1 58 ? 0.964  13.112  37.224 1.00 57.57  ? 58  GLN A CD  1 
ATOM   452 O OE1 . GLN A 1 58 ? 1.005  14.195  36.635 1.00 61.40  ? 58  GLN A OE1 1 
ATOM   453 N NE2 . GLN A 1 58 ? 2.056  12.488  37.641 1.00 58.61  ? 58  GLN A NE2 1 
ATOM   454 N N   . TYR A 1 59 ? -0.779 8.691   35.702 1.00 44.17  ? 59  TYR A N   1 
ATOM   455 C CA  . TYR A 1 59 ? -0.690 7.331   36.213 1.00 44.00  ? 59  TYR A CA  1 
ATOM   456 C C   . TYR A 1 59 ? 0.615  6.692   35.730 1.00 39.76  ? 59  TYR A C   1 
ATOM   457 O O   . TYR A 1 59 ? 1.333  6.078   36.504 1.00 39.25  ? 59  TYR A O   1 
ATOM   458 C CB  . TYR A 1 59 ? -1.924 6.502   35.836 1.00 45.97  ? 59  TYR A CB  1 
ATOM   459 C CG  . TYR A 1 59 ? -1.794 5.041   36.244 1.00 48.29  ? 59  TYR A CG  1 
ATOM   460 C CD1 . TYR A 1 59 ? -2.014 4.645   37.557 1.00 52.21  ? 59  TYR A CD1 1 
ATOM   461 C CD2 . TYR A 1 59 ? -1.387 4.068   35.335 1.00 48.10  ? 59  TYR A CD2 1 
ATOM   462 C CE1 . TYR A 1 59 ? -1.878 3.321   37.946 1.00 55.23  ? 59  TYR A CE1 1 
ATOM   463 C CE2 . TYR A 1 59 ? -1.240 2.743   35.710 1.00 50.99  ? 59  TYR A CE2 1 
ATOM   464 C CZ  . TYR A 1 59 ? -1.489 2.368   37.020 1.00 57.15  ? 59  TYR A CZ  1 
ATOM   465 O OH  . TYR A 1 59 ? -1.346 1.071   37.423 1.00 63.44  ? 59  TYR A OH  1 
ATOM   466 N N   . GLN A 1 60 ? 0.930  6.819   34.442 1.00 39.64  ? 60  GLN A N   1 
ATOM   467 C CA  . GLN A 1 60 ? 2.157  6.227   33.916 1.00 38.90  ? 60  GLN A CA  1 
ATOM   468 C C   . GLN A 1 60 ? 3.398  6.839   34.559 1.00 40.34  ? 60  GLN A C   1 
ATOM   469 O O   . GLN A 1 60 ? 4.348  6.122   34.838 1.00 41.43  ? 60  GLN A O   1 
ATOM   470 C CB  . GLN A 1 60 ? 2.223  6.370   32.401 1.00 37.30  ? 60  GLN A CB  1 
ATOM   471 C CG  . GLN A 1 60 ? 1.198  5.476   31.714 1.00 39.53  ? 60  GLN A CG  1 
ATOM   472 C CD  . GLN A 1 60 ? 1.057  5.738   30.233 1.00 38.78  ? 60  GLN A CD  1 
ATOM   473 O OE1 . GLN A 1 60 ? 0.834  6.870   29.786 1.00 40.05  ? 60  GLN A OE1 1 
ATOM   474 N NE2 . GLN A 1 60 ? 1.151  4.670   29.463 1.00 37.97  ? 60  GLN A NE2 1 
ATOM   475 N N   . LEU A 1 61 ? 3.393  8.166   34.727 1.00 43.48  ? 61  LEU A N   1 
ATOM   476 C CA  . LEU A 1 61 ? 4.518  8.885   35.303 1.00 45.11  ? 61  LEU A CA  1 
ATOM   477 C C   . LEU A 1 61 ? 4.734  8.461   36.757 1.00 44.60  ? 61  LEU A C   1 
ATOM   478 O O   . LEU A 1 61 ? 5.867  8.227   37.159 1.00 44.26  ? 61  LEU A O   1 
ATOM   479 C CB  . LEU A 1 61 ? 4.258  10.384  35.146 1.00 47.39  ? 61  LEU A CB  1 
ATOM   480 C CG  . LEU A 1 61 ? 4.391  10.926  33.717 1.00 46.99  ? 61  LEU A CG  1 
ATOM   481 C CD1 . LEU A 1 61 ? 3.930  12.372  33.637 1.00 49.43  ? 61  LEU A CD1 1 
ATOM   482 C CD2 . LEU A 1 61 ? 5.829  10.794  33.217 1.00 47.49  ? 61  LEU A CD2 1 
ATOM   483 N N   . ASN A 1 62 ? 3.645  8.291   37.514 1.00 45.81  ? 62  ASN A N   1 
ATOM   484 C CA  . ASN A 1 62 ? 3.724  7.802   38.882 1.00 48.95  ? 62  ASN A CA  1 
ATOM   485 C C   . ASN A 1 62 ? 4.335  6.406   38.944 1.00 48.33  ? 62  ASN A C   1 
ATOM   486 O O   . ASN A 1 62 ? 5.178  6.150   39.798 1.00 48.67  ? 62  ASN A O   1 
ATOM   487 C CB  . ASN A 1 62 ? 2.349  7.795   39.533 1.00 52.97  ? 62  ASN A CB  1 
ATOM   488 C CG  . ASN A 1 62 ? 1.821  9.197   39.700 1.00 55.69  ? 62  ASN A CG  1 
ATOM   489 O OD1 . ASN A 1 62 ? 2.567  10.160  39.516 1.00 55.87  ? 62  ASN A OD1 1 
ATOM   490 N ND2 . ASN A 1 62 ? 0.550  9.336   40.045 1.00 60.71  ? 62  ASN A ND2 1 
ATOM   491 N N   . SER A 1 63 ? 3.906  5.504   38.050 1.00 46.15  ? 63  SER A N   1 
ATOM   492 C CA  . SER A 1 63 ? 4.457  4.154   38.011 1.00 45.35  ? 63  SER A CA  1 
ATOM   493 C C   . SER A 1 63 ? 5.950  4.214   37.714 1.00 44.95  ? 63  SER A C   1 
ATOM   494 O O   . SER A 1 63 ? 6.739  3.492   38.316 1.00 44.49  ? 63  SER A O   1 
ATOM   495 C CB  . SER A 1 63 ? 3.769  3.296   36.986 1.00 44.48  ? 63  SER A CB  1 
ATOM   496 O OG  . SER A 1 63 ? 2.389  3.150   37.297 1.00 46.34  ? 63  SER A OG  1 
ATOM   497 N N   . ILE A 1 64 ? 6.303  5.062   36.745 1.00 43.79  ? 64  ILE A N   1 
ATOM   498 C CA  . ILE A 1 64 ? 7.683  5.253   36.328 1.00 44.55  ? 64  ILE A CA  1 
ATOM   499 C C   . ILE A 1 64 ? 8.541  5.686   37.517 1.00 46.25  ? 64  ILE A C   1 
ATOM   500 O O   . ILE A 1 64 ? 9.620  5.135   37.741 1.00 48.68  ? 64  ILE A O   1 
ATOM   501 C CB  . ILE A 1 64 ? 7.747  6.250   35.154 1.00 42.23  ? 64  ILE A CB  1 
ATOM   502 C CG1 . ILE A 1 64 ? 7.385  5.547   33.838 1.00 45.16  ? 64  ILE A CG1 1 
ATOM   503 C CG2 . ILE A 1 64 ? 9.118  6.927   35.074 1.00 42.31  ? 64  ILE A CG2 1 
ATOM   504 C CD1 . ILE A 1 64 ? 6.840  6.457   32.753 1.00 44.81  ? 64  ILE A CD1 1 
ATOM   505 N N   . GLN A 1 65 ? 8.073  6.683   38.268 1.00 49.85  ? 65  GLN A N   1 
ATOM   506 C CA  . GLN A 1 65 ? 8.839  7.185   39.398 1.00 53.66  ? 65  GLN A CA  1 
ATOM   507 C C   . GLN A 1 65 ? 8.983  6.075   40.433 1.00 53.36  ? 65  GLN A C   1 
ATOM   508 O O   . GLN A 1 65 ? 10.079 5.787   40.899 1.00 52.35  ? 65  GLN A O   1 
ATOM   509 C CB  . GLN A 1 65 ? 8.186  8.410   40.032 1.00 60.26  ? 65  GLN A CB  1 
ATOM   510 C CG  . GLN A 1 65 ? 8.963  8.955   41.227 1.00 69.00  ? 65  GLN A CG  1 
ATOM   511 C CD  . GLN A 1 65 ? 8.237  10.051  41.977 1.00 80.42  ? 65  GLN A CD  1 
ATOM   512 O OE1 . GLN A 1 65 ? 7.051  9.935   42.310 1.00 84.12  ? 65  GLN A OE1 1 
ATOM   513 N NE2 . GLN A 1 65 ? 8.958  11.125  42.272 1.00 87.86  ? 65  GLN A NE2 1 
ATOM   514 N N   . LYS A 1 66 ? 7.860  5.429   40.745 1.00 53.91  ? 66  LYS A N   1 
ATOM   515 C CA  . LYS A 1 66 ? 7.807  4.403   41.767 1.00 56.48  ? 66  LYS A CA  1 
ATOM   516 C C   . LYS A 1 66 ? 8.777  3.269   41.453 1.00 54.67  ? 66  LYS A C   1 
ATOM   517 O O   . LYS A 1 66 ? 9.401  2.715   42.349 1.00 55.63  ? 66  LYS A O   1 
ATOM   518 C CB  . LYS A 1 66 ? 6.379  3.860   41.836 1.00 59.61  ? 66  LYS A CB  1 
ATOM   519 C CG  . LYS A 1 66 ? 6.167  2.842   42.927 1.00 64.51  ? 66  LYS A CG  1 
ATOM   520 C CD  . LYS A 1 66 ? 4.754  2.284   42.958 1.00 68.95  ? 66  LYS A CD  1 
ATOM   521 C CE  . LYS A 1 66 ? 4.661  1.221   43.997 1.00 75.52  ? 66  LYS A CE  1 
ATOM   522 N NZ  . LYS A 1 66 ? 3.275  0.779   44.158 1.00 79.46  ? 66  LYS A NZ  1 
ATOM   523 N N   . ASN A 1 67 ? 8.890  2.907   40.176 1.00 51.40  ? 67  ASN A N   1 
ATOM   524 C CA  . ASN A 1 67 ? 9.608  1.698   39.821 1.00 52.49  ? 67  ASN A CA  1 
ATOM   525 C C   . ASN A 1 67 ? 10.984 2.031   39.261 1.00 50.53  ? 67  ASN A C   1 
ATOM   526 O O   . ASN A 1 67 ? 11.661 1.129   38.788 1.00 50.46  ? 67  ASN A O   1 
ATOM   527 C CB  . ASN A 1 67 ? 8.787  0.848   38.859 1.00 53.48  ? 67  ASN A CB  1 
ATOM   528 C CG  . ASN A 1 67 ? 7.534  0.340   39.526 1.00 53.35  ? 67  ASN A CG  1 
ATOM   529 O OD1 . ASN A 1 67 ? 6.413  0.640   39.097 1.00 54.85  ? 67  ASN A OD1 1 
ATOM   530 N ND2 . ASN A 1 67 ? 7.712  -0.418  40.590 1.00 56.53  ? 67  ASN A ND2 1 
ATOM   531 N N   . HIS A 1 68 ? 11.382 3.308   39.338 1.00 51.53  ? 68  HIS A N   1 
ATOM   532 C CA  . HIS A 1 68 ? 12.699 3.776   38.910 1.00 52.79  ? 68  HIS A CA  1 
ATOM   533 C C   . HIS A 1 68 ? 12.948 3.477   37.434 1.00 49.11  ? 68  HIS A C   1 
ATOM   534 O O   . HIS A 1 68 ? 14.069 3.153   37.042 1.00 50.85  ? 68  HIS A O   1 
ATOM   535 C CB  . HIS A 1 68 ? 13.816 3.208   39.797 1.00 57.50  ? 68  HIS A CB  1 
ATOM   536 C CG  . HIS A 1 68 ? 13.510 3.292   41.253 1.00 64.30  ? 68  HIS A CG  1 
ATOM   537 N ND1 . HIS A 1 68 ? 13.662 4.449   41.986 1.00 67.72  ? 68  HIS A ND1 1 
ATOM   538 C CD2 . HIS A 1 68 ? 13.025 2.371   42.101 1.00 69.87  ? 68  HIS A CD2 1 
ATOM   539 C CE1 . HIS A 1 68 ? 13.296 4.221   43.237 1.00 71.24  ? 68  HIS A CE1 1 
ATOM   540 N NE2 . HIS A 1 68 ? 12.906 2.966   43.329 1.00 72.05  ? 68  HIS A NE2 1 
ATOM   541 N N   . VAL A 1 69 ? 11.912 3.660   36.609 1.00 45.66  ? 69  VAL A N   1 
ATOM   542 C CA  . VAL A 1 69 ? 12.027 3.455   35.174 1.00 43.88  ? 69  VAL A CA  1 
ATOM   543 C C   . VAL A 1 69 ? 12.703 4.686   34.565 1.00 39.95  ? 69  VAL A C   1 
ATOM   544 O O   . VAL A 1 69 ? 12.374 5.806   34.918 1.00 41.31  ? 69  VAL A O   1 
ATOM   545 C CB  . VAL A 1 69 ? 10.634 3.200   34.559 1.00 44.33  ? 69  VAL A CB  1 
ATOM   546 C CG1 . VAL A 1 69 ? 10.700 2.851   33.074 1.00 42.51  ? 69  VAL A CG1 1 
ATOM   547 C CG2 . VAL A 1 69 ? 9.870  2.122   35.320 1.00 46.26  ? 69  VAL A CG2 1 
ATOM   548 N N   . HIS A 1 70 ? 13.674 4.463   33.678 1.00 41.22  ? 70  HIS A N   1 
ATOM   549 C CA  . HIS A 1 70 ? 14.310 5.538   32.922 1.00 41.46  ? 70  HIS A CA  1 
ATOM   550 C C   . HIS A 1 70 ? 13.478 5.884   31.685 1.00 39.26  ? 70  HIS A C   1 
ATOM   551 O O   . HIS A 1 70 ? 13.173 5.009   30.876 1.00 38.77  ? 70  HIS A O   1 
ATOM   552 C CB  . HIS A 1 70 ? 15.712 5.105   32.487 1.00 42.50  ? 70  HIS A CB  1 
ATOM   553 C CG  . HIS A 1 70 ? 16.607 4.786   33.633 1.00 45.67  ? 70  HIS A CG  1 
ATOM   554 N ND1 . HIS A 1 70 ? 16.824 5.668   34.667 1.00 47.03  ? 70  HIS A ND1 1 
ATOM   555 C CD2 . HIS A 1 70 ? 17.357 3.711   33.888 1.00 47.45  ? 70  HIS A CD2 1 
ATOM   556 C CE1 . HIS A 1 70 ? 17.670 5.124   35.527 1.00 53.02  ? 70  HIS A CE1 1 
ATOM   557 N NE2 . HIS A 1 70 ? 18.005 3.936   35.072 1.00 52.09  ? 70  HIS A NE2 1 
ATOM   558 N N   . ILE A 1 71 ? 13.113 7.167   31.553 1.00 40.09  ? 71  ILE A N   1 
ATOM   559 C CA  . ILE A 1 71 ? 12.413 7.675   30.379 1.00 38.32  ? 71  ILE A CA  1 
ATOM   560 C C   . ILE A 1 71 ? 13.455 8.207   29.402 1.00 38.08  ? 71  ILE A C   1 
ATOM   561 O O   . ILE A 1 71 ? 14.208 9.102   29.764 1.00 34.22  ? 71  ILE A O   1 
ATOM   562 C CB  . ILE A 1 71 ? 11.420 8.803   30.723 1.00 41.29  ? 71  ILE A CB  1 
ATOM   563 C CG1 . ILE A 1 71 ? 10.481 8.447   31.861 1.00 42.47  ? 71  ILE A CG1 1 
ATOM   564 C CG2 . ILE A 1 71 ? 10.642 9.223   29.470 1.00 42.00  ? 71  ILE A CG2 1 
ATOM   565 C CD1 . ILE A 1 71 ? 9.480  9.532   32.208 1.00 43.83  ? 71  ILE A CD1 1 
ATOM   566 N N   . ALA A 1 72 ? 13.431 7.707   28.158 1.00 36.19  ? 72  ALA A N   1 
ATOM   567 C CA  . ALA A 1 72 ? 14.403 8.082   27.146 1.00 36.43  ? 72  ALA A CA  1 
ATOM   568 C C   . ALA A 1 72 ? 13.728 8.255   25.784 1.00 39.31  ? 72  ALA A C   1 
ATOM   569 O O   . ALA A 1 72 ? 12.652 7.711   25.542 1.00 40.60  ? 72  ALA A O   1 
ATOM   570 C CB  . ALA A 1 72 ? 15.503 7.040   27.079 1.00 34.21  ? 72  ALA A CB  1 
ATOM   571 N N   . ASN A 1 73 ? 14.372 9.033   24.904 1.00 39.50  ? 73  ASN A N   1 
ATOM   572 C CA  . ASN A 1 73 ? 13.947 9.157   23.517 1.00 36.40  ? 73  ASN A CA  1 
ATOM   573 C C   . ASN A 1 73 ? 14.685 8.105   22.688 1.00 34.39  ? 73  ASN A C   1 
ATOM   574 O O   . ASN A 1 73 ? 15.582 7.438   23.194 1.00 34.48  ? 73  ASN A O   1 
ATOM   575 C CB  . ASN A 1 73 ? 14.100 10.589  23.003 1.00 39.42  ? 73  ASN A CB  1 
ATOM   576 C CG  . ASN A 1 73 ? 15.536 11.064  22.978 1.00 41.45  ? 73  ASN A CG  1 
ATOM   577 O OD1 . ASN A 1 73 ? 16.461 10.296  22.696 1.00 43.67  ? 73  ASN A OD1 1 
ATOM   578 N ND2 . ASN A 1 73 ? 15.755 12.313  23.327 1.00 42.68  ? 73  ASN A ND2 1 
ATOM   579 N N   . PRO A 1 74 ? 14.299 7.875   21.410 1.00 32.18  ? 74  PRO A N   1 
ATOM   580 C CA  . PRO A 1 74 ? 14.979 6.911   20.549 1.00 31.40  ? 74  PRO A CA  1 
ATOM   581 C C   . PRO A 1 74 ? 16.474 7.154   20.339 1.00 30.90  ? 74  PRO A C   1 
ATOM   582 O O   . PRO A 1 74 ? 17.226 6.215   20.099 1.00 31.97  ? 74  PRO A O   1 
ATOM   583 C CB  . PRO A 1 74 ? 14.227 7.054   19.220 1.00 33.27  ? 74  PRO A CB  1 
ATOM   584 C CG  . PRO A 1 74 ? 12.843 7.479   19.663 1.00 33.92  ? 74  PRO A CG  1 
ATOM   585 C CD  . PRO A 1 74 ? 13.121 8.468   20.748 1.00 35.59  ? 74  PRO A CD  1 
ATOM   586 N N   . ASP A 1 75 ? 16.897 8.420   20.409 1.00 32.11  ? 75  ASP A N   1 
ATOM   587 C CA  . ASP A 1 75 ? 18.305 8.783   20.281 1.00 34.69  ? 75  ASP A CA  1 
ATOM   588 C C   . ASP A 1 75 ? 19.191 8.059   21.287 1.00 32.39  ? 75  ASP A C   1 
ATOM   589 O O   . ASP A 1 75 ? 20.340 7.760   20.977 1.00 31.77  ? 75  ASP A O   1 
ATOM   590 C CB  . ASP A 1 75 ? 18.508 10.285  20.378 1.00 39.88  ? 75  ASP A CB  1 
ATOM   591 C CG  . ASP A 1 75 ? 18.258 11.018  19.071 1.00 42.90  ? 75  ASP A CG  1 
ATOM   592 O OD1 . ASP A 1 75 ? 18.304 10.355  18.022 1.00 43.47  ? 75  ASP A OD1 1 
ATOM   593 O OD2 . ASP A 1 75 ? 18.017 12.231  19.122 1.00 52.42  ? 75  ASP A OD2 1 
ATOM   594 N N   . PHE A 1 76 ? 18.671 7.782   22.488 1.00 31.12  ? 76  PHE A N   1 
ATOM   595 C CA  . PHE A 1 76 ? 19.417 7.001   23.460 1.00 32.26  ? 76  PHE A CA  1 
ATOM   596 C C   . PHE A 1 76 ? 19.888 5.675   22.855 1.00 33.53  ? 76  PHE A C   1 
ATOM   597 O O   . PHE A 1 76 ? 21.014 5.236   23.099 1.00 34.29  ? 76  PHE A O   1 
ATOM   598 C CB  . PHE A 1 76 ? 18.550 6.769   24.696 1.00 33.22  ? 76  PHE A CB  1 
ATOM   599 C CG  . PHE A 1 76 ? 19.202 5.844   25.710 1.00 34.30  ? 76  PHE A CG  1 
ATOM   600 C CD1 . PHE A 1 76 ? 20.402 6.194   26.312 1.00 37.01  ? 76  PHE A CD1 1 
ATOM   601 C CD2 . PHE A 1 76 ? 18.604 4.642   26.077 1.00 35.62  ? 76  PHE A CD2 1 
ATOM   602 C CE1 . PHE A 1 76 ? 20.999 5.358   27.242 1.00 39.11  ? 76  PHE A CE1 1 
ATOM   603 C CE2 . PHE A 1 76 ? 19.208 3.809   27.011 1.00 37.88  ? 76  PHE A CE2 1 
ATOM   604 C CZ  . PHE A 1 76 ? 20.408 4.163   27.581 1.00 39.73  ? 76  PHE A CZ  1 
ATOM   605 N N   . ILE A 1 77 ? 18.985 5.004   22.128 1.00 33.51  ? 77  ILE A N   1 
ATOM   606 C CA  . ILE A 1 77 ? 19.269 3.734   21.484 1.00 32.89  ? 77  ILE A CA  1 
ATOM   607 C C   . ILE A 1 77 ? 20.195 3.953   20.286 1.00 31.61  ? 77  ILE A C   1 
ATOM   608 O O   . ILE A 1 77 ? 21.225 3.295   20.171 1.00 35.08  ? 77  ILE A O   1 
ATOM   609 C CB  . ILE A 1 77 ? 17.958 3.044   21.047 1.00 36.05  ? 77  ILE A CB  1 
ATOM   610 C CG1 . ILE A 1 77 ? 16.973 2.813   22.218 1.00 36.23  ? 77  ILE A CG1 1 
ATOM   611 C CG2 . ILE A 1 77 ? 18.263 1.756   20.280 1.00 35.20  ? 77  ILE A CG2 1 
ATOM   612 C CD1 . ILE A 1 77 ? 17.510 1.955   23.345 1.00 37.14  ? 77  ILE A CD1 1 
ATOM   613 N N   . TRP A 1 78 ? 19.805 4.832   19.359 1.00 32.64  ? 78  TRP A N   1 
ATOM   614 C CA  . TRP A 1 78 ? 20.587 5.074   18.148 1.00 34.92  ? 78  TRP A CA  1 
ATOM   615 C C   . TRP A 1 78 ? 22.045 5.394   18.483 1.00 36.95  ? 78  TRP A C   1 
ATOM   616 O O   . TRP A 1 78 ? 22.966 4.834   17.880 1.00 36.82  ? 78  TRP A O   1 
ATOM   617 C CB  . TRP A 1 78 ? 20.035 6.254   17.333 1.00 35.58  ? 78  TRP A CB  1 
ATOM   618 C CG  . TRP A 1 78 ? 18.606 6.179   16.855 1.00 38.35  ? 78  TRP A CG  1 
ATOM   619 C CD1 . TRP A 1 78 ? 17.738 7.230   16.784 1.00 39.34  ? 78  TRP A CD1 1 
ATOM   620 C CD2 . TRP A 1 78 ? 17.891 5.041   16.330 1.00 38.66  ? 78  TRP A CD2 1 
ATOM   621 N NE1 . TRP A 1 78 ? 16.532 6.827   16.279 1.00 39.82  ? 78  TRP A NE1 1 
ATOM   622 C CE2 . TRP A 1 78 ? 16.591 5.491   15.995 1.00 38.94  ? 78  TRP A CE2 1 
ATOM   623 C CE3 . TRP A 1 78 ? 18.209 3.691   16.131 1.00 39.69  ? 78  TRP A CE3 1 
ATOM   624 C CZ2 . TRP A 1 78 ? 15.618 4.647   15.459 1.00 40.71  ? 78  TRP A CZ2 1 
ATOM   625 C CZ3 . TRP A 1 78 ? 17.244 2.856   15.607 1.00 40.90  ? 78  TRP A CZ3 1 
ATOM   626 C CH2 . TRP A 1 78 ? 15.972 3.330   15.270 1.00 42.48  ? 78  TRP A CH2 1 
ATOM   627 N N   A LYS A 1 79 ? 22.255 6.322   19.429 0.50 36.30  ? 79  LYS A N   1 
ATOM   628 N N   B LYS A 1 79 ? 22.233 6.313   19.442 0.50 35.45  ? 79  LYS A N   1 
ATOM   629 C CA  A LYS A 1 79 ? 23.597 6.817   19.709 0.50 37.58  ? 79  LYS A CA  1 
ATOM   630 C CA  B LYS A 1 79 ? 23.552 6.844   19.752 0.50 36.24  ? 79  LYS A CA  1 
ATOM   631 C C   A LYS A 1 79 ? 24.388 5.815   20.549 0.50 35.95  ? 79  LYS A C   1 
ATOM   632 C C   B LYS A 1 79 ? 24.369 5.818   20.538 0.50 35.25  ? 79  LYS A C   1 
ATOM   633 O O   A LYS A 1 79 ? 25.597 5.723   20.388 0.50 36.59  ? 79  LYS A O   1 
ATOM   634 O O   B LYS A 1 79 ? 25.570 5.716   20.331 0.50 35.84  ? 79  LYS A O   1 
ATOM   635 C CB  A LYS A 1 79 ? 23.611 8.230   20.305 0.50 38.42  ? 79  LYS A CB  1 
ATOM   636 C CB  B LYS A 1 79 ? 23.435 8.183   20.489 0.50 35.93  ? 79  LYS A CB  1 
ATOM   637 C CG  A LYS A 1 79 ? 23.929 9.315   19.274 0.50 43.73  ? 79  LYS A CG  1 
ATOM   638 C CG  B LYS A 1 79 ? 22.730 9.294   19.709 0.50 39.07  ? 79  LYS A CG  1 
ATOM   639 C CD  A LYS A 1 79 ? 23.755 10.762  19.731 0.50 46.85  ? 79  LYS A CD  1 
ATOM   640 C CD  B LYS A 1 79 ? 22.650 10.617  20.471 0.50 41.70  ? 79  LYS A CD  1 
ATOM   641 C CE  A LYS A 1 79 ? 24.642 11.132  20.874 0.50 47.86  ? 79  LYS A CE  1 
ATOM   642 C CE  B LYS A 1 79 ? 22.013 11.751  19.721 0.50 43.74  ? 79  LYS A CE  1 
ATOM   643 N NZ  A LYS A 1 79 ? 24.144 12.330  21.552 0.50 49.44  ? 79  LYS A NZ  1 
ATOM   644 N NZ  B LYS A 1 79 ? 22.537 11.863  18.360 0.50 44.89  ? 79  LYS A NZ  1 
ATOM   645 N N   . SER A 1 80 ? 23.729 5.065   21.443 1.00 34.25  ? 80  SER A N   1 
ATOM   646 C CA  . SER A 1 80 ? 24.434 4.029   22.189 1.00 37.64  ? 80  SER A CA  1 
ATOM   647 C C   . SER A 1 80 ? 24.942 2.953   21.220 1.00 40.19  ? 80  SER A C   1 
ATOM   648 O O   . SER A 1 80 ? 26.057 2.449   21.364 1.00 40.33  ? 80  SER A O   1 
ATOM   649 C CB  . SER A 1 80 ? 23.589 3.413   23.299 1.00 38.70  ? 80  SER A CB  1 
ATOM   650 O OG  . SER A 1 80 ? 23.255 4.337   24.331 1.00 37.32  ? 80  SER A OG  1 
ATOM   651 N N   . ILE A 1 81 ? 24.103 2.584   20.243 1.00 36.25  ? 81  ILE A N   1 
ATOM   652 C CA  . ILE A 1 81 ? 24.489 1.641   19.206 1.00 38.02  ? 81  ILE A CA  1 
ATOM   653 C C   . ILE A 1 81 ? 25.650 2.228   18.404 1.00 37.82  ? 81  ILE A C   1 
ATOM   654 O O   . ILE A 1 81 ? 26.629 1.552   18.110 1.00 38.43  ? 81  ILE A O   1 
ATOM   655 C CB  . ILE A 1 81 ? 23.298 1.301   18.284 1.00 37.82  ? 81  ILE A CB  1 
ATOM   656 C CG1 . ILE A 1 81 ? 22.227 0.493   19.011 1.00 41.57  ? 81  ILE A CG1 1 
ATOM   657 C CG2 . ILE A 1 81 ? 23.761 0.585   17.014 1.00 39.27  ? 81  ILE A CG2 1 
ATOM   658 C CD1 . ILE A 1 81 ? 22.686 -0.872  19.479 1.00 44.41  ? 81  ILE A CD1 1 
ATOM   659 N N   . ARG A 1 82 ? 25.506 3.487   18.014 1.00 38.23  ? 82  ARG A N   1 
ATOM   660 C CA  . ARG A 1 82 ? 26.487 4.120   17.159 1.00 41.00  ? 82  ARG A CA  1 
ATOM   661 C C   . ARG A 1 82 ? 27.835 4.149   17.874 1.00 41.96  ? 82  ARG A C   1 
ATOM   662 O O   . ARG A 1 82 ? 28.853 3.863   17.257 1.00 40.90  ? 82  ARG A O   1 
ATOM   663 C CB  . ARG A 1 82 ? 26.022 5.513   16.744 1.00 41.51  ? 82  ARG A CB  1 
ATOM   664 C CG  . ARG A 1 82 ? 27.111 6.269   15.999 1.00 48.04  ? 82  ARG A CG  1 
ATOM   665 C CD  . ARG A 1 82 ? 26.590 7.562   15.444 1.00 51.49  ? 82  ARG A CD  1 
ATOM   666 N NE  . ARG A 1 82 ? 25.863 7.319   14.194 1.00 57.74  ? 82  ARG A NE  1 
ATOM   667 C CZ  . ARG A 1 82 ? 24.614 7.677   13.937 1.00 62.62  ? 82  ARG A CZ  1 
ATOM   668 N NH1 . ARG A 1 82 ? 23.850 8.133   14.922 1.00 69.59  ? 82  ARG A NH1 1 
ATOM   669 N NH2 . ARG A 1 82 ? 24.135 7.558   12.703 1.00 55.82  ? 82  ARG A NH2 1 
ATOM   670 N N   . GLU A 1 83 ? 27.822 4.441   19.177 1.00 41.99  ? 83  GLU A N   1 
ATOM   671 C CA  . GLU A 1 83 ? 29.057 4.584   19.930 1.00 47.15  ? 83  GLU A CA  1 
ATOM   672 C C   . GLU A 1 83 ? 29.494 3.248   20.522 1.00 46.64  ? 83  GLU A C   1 
ATOM   673 O O   . GLU A 1 83 ? 30.550 3.173   21.148 1.00 44.17  ? 83  GLU A O   1 
ATOM   674 C CB  . GLU A 1 83 ? 28.862 5.667   20.988 1.00 47.29  ? 83  GLU A CB  1 
ATOM   675 C CG  . GLU A 1 83 ? 28.971 7.056   20.374 1.00 53.79  ? 83  GLU A CG  1 
ATOM   676 C CD  . GLU A 1 83 ? 28.660 8.172   21.342 1.00 58.58  ? 83  GLU A CD  1 
ATOM   677 O OE1 . GLU A 1 83 ? 29.208 8.121   22.463 1.00 60.89  ? 83  GLU A OE1 1 
ATOM   678 O OE2 . GLU A 1 83 ? 27.888 9.084   20.968 1.00 64.37  ? 83  GLU A OE2 1 
ATOM   679 N N   . LYS A 1 84 ? 28.668 2.212   20.331 1.00 46.39  ? 84  LYS A N   1 
ATOM   680 C CA  . LYS A 1 84 ? 28.970 0.859   20.783 1.00 48.70  ? 84  LYS A CA  1 
ATOM   681 C C   . LYS A 1 84 ? 29.213 0.851   22.289 1.00 48.98  ? 84  LYS A C   1 
ATOM   682 O O   . LYS A 1 84 ? 30.075 0.126   22.784 1.00 50.99  ? 84  LYS A O   1 
ATOM   683 C CB  . LYS A 1 84 ? 30.171 0.267   20.038 1.00 52.54  ? 84  LYS A CB  1 
ATOM   684 C CG  . LYS A 1 84 ? 29.964 0.138   18.545 1.00 54.07  ? 84  LYS A CG  1 
ATOM   685 C CD  . LYS A 1 84 ? 31.136 -0.568  17.876 1.00 60.26  ? 84  LYS A CD  1 
ATOM   686 C CE  . LYS A 1 84 ? 30.832 -0.923  16.467 1.00 63.45  ? 84  LYS A CE  1 
ATOM   687 N NZ  . LYS A 1 84 ? 32.051 -1.381  15.800 1.00 69.58  ? 84  LYS A NZ  1 
ATOM   688 N N   . ARG A 1 85 ? 28.416 1.648   23.007 1.00 44.83  ? 85  ARG A N   1 
ATOM   689 C CA  . ARG A 1 85 ? 28.591 1.829   24.435 1.00 44.01  ? 85  ARG A CA  1 
ATOM   690 C C   . ARG A 1 85 ? 27.281 2.364   24.993 1.00 41.97  ? 85  ARG A C   1 
ATOM   691 O O   . ARG A 1 85 ? 26.645 3.223   24.381 1.00 39.35  ? 85  ARG A O   1 
ATOM   692 C CB  . ARG A 1 85 ? 29.766 2.791   24.652 1.00 45.71  ? 85  ARG A CB  1 
ATOM   693 C CG  . ARG A 1 85 ? 30.284 2.954   26.070 1.00 47.69  ? 85  ARG A CG  1 
ATOM   694 C CD  . ARG A 1 85 ? 31.557 3.802   26.082 1.00 48.69  ? 85  ARG A CD  1 
ATOM   695 N NE  . ARG A 1 85 ? 31.353 5.161   25.562 1.00 46.92  ? 85  ARG A NE  1 
ATOM   696 C CZ  . ARG A 1 85 ? 30.679 6.142   26.170 1.00 46.31  ? 85  ARG A CZ  1 
ATOM   697 N NH1 . ARG A 1 85 ? 30.209 5.999   27.406 1.00 46.38  ? 85  ARG A NH1 1 
ATOM   698 N NH2 . ARG A 1 85 ? 30.499 7.294   25.549 1.00 43.61  ? 85  ARG A NH2 1 
ATOM   699 N N   . LEU A 1 86 ? 26.886 1.842   26.157 1.00 43.23  ? 86  LEU A N   1 
ATOM   700 C CA  . LEU A 1 86 ? 25.714 2.338   26.859 1.00 43.72  ? 86  LEU A CA  1 
ATOM   701 C C   . LEU A 1 86 ? 26.005 3.744   27.382 1.00 42.35  ? 86  LEU A C   1 
ATOM   702 O O   . LEU A 1 86 ? 26.890 3.938   28.219 1.00 42.95  ? 86  LEU A O   1 
ATOM   703 C CB  . LEU A 1 86 ? 25.328 1.386   27.993 1.00 45.80  ? 86  LEU A CB  1 
ATOM   704 C CG  . LEU A 1 86 ? 23.981 1.669   28.673 1.00 45.13  ? 86  LEU A CG  1 
ATOM   705 C CD1 . LEU A 1 86 ? 22.817 1.387   27.757 1.00 42.20  ? 86  LEU A CD1 1 
ATOM   706 C CD2 . LEU A 1 86 ? 23.877 0.854   29.951 1.00 48.36  ? 86  LEU A CD2 1 
ATOM   707 N N   . LEU A 1 87 ? 25.229 4.708   26.880 1.00 42.37  ? 87  LEU A N   1 
ATOM   708 C CA  . LEU A 1 87 ? 25.401 6.112   27.215 1.00 40.10  ? 87  LEU A CA  1 
ATOM   709 C C   . LEU A 1 87 ? 24.607 6.441   28.475 1.00 40.23  ? 87  LEU A C   1 
ATOM   710 O O   . LEU A 1 87 ? 23.994 5.570   29.087 1.00 41.24  ? 87  LEU A O   1 
ATOM   711 C CB  . LEU A 1 87 ? 24.983 6.969   26.017 1.00 40.12  ? 87  LEU A CB  1 
ATOM   712 C CG  . LEU A 1 87 ? 25.732 6.706   24.706 1.00 39.95  ? 87  LEU A CG  1 
ATOM   713 C CD1 . LEU A 1 87 ? 25.249 7.622   23.597 1.00 39.34  ? 87  LEU A CD1 1 
ATOM   714 C CD2 . LEU A 1 87 ? 27.233 6.869   24.900 1.00 43.55  ? 87  LEU A CD2 1 
ATOM   715 N N   . ASP A 1 88 ? 24.685 7.715   28.868 1.00 40.55  ? 88  ASP A N   1 
ATOM   716 C CA  . ASP A 1 88 ? 24.014 8.242   30.036 1.00 41.86  ? 88  ASP A CA  1 
ATOM   717 C C   . ASP A 1 88 ? 22.568 8.567   29.676 1.00 41.24  ? 88  ASP A C   1 
ATOM   718 O O   . ASP A 1 88 ? 22.302 9.598   29.058 1.00 41.16  ? 88  ASP A O   1 
ATOM   719 C CB  . ASP A 1 88 ? 24.726 9.490   30.533 1.00 45.76  ? 88  ASP A CB  1 
ATOM   720 C CG  . ASP A 1 88 ? 24.275 9.976   31.897 1.00 46.92  ? 88  ASP A CG  1 
ATOM   721 O OD1 . ASP A 1 88 ? 23.333 9.378   32.446 1.00 46.74  ? 88  ASP A OD1 1 
ATOM   722 O OD2 . ASP A 1 88 ? 24.877 10.947  32.385 1.00 54.20  ? 88  ASP A OD2 1 
ATOM   723 N N   . VAL A 1 89 ? 21.658 7.679   30.102 1.00 40.12  ? 89  VAL A N   1 
ATOM   724 C CA  . VAL A 1 89 ? 20.243 7.764   29.793 1.00 40.83  ? 89  VAL A CA  1 
ATOM   725 C C   . VAL A 1 89 ? 19.630 9.069   30.314 1.00 42.61  ? 89  VAL A C   1 
ATOM   726 O O   . VAL A 1 89 ? 18.584 9.488   29.817 1.00 41.21  ? 89  VAL A O   1 
ATOM   727 C CB  . VAL A 1 89 ? 19.486 6.532   30.339 1.00 41.85  ? 89  VAL A CB  1 
ATOM   728 C CG1 . VAL A 1 89 ? 19.501 6.453   31.867 1.00 44.75  ? 89  VAL A CG1 1 
ATOM   729 C CG2 . VAL A 1 89 ? 18.057 6.494   29.818 1.00 40.41  ? 89  VAL A CG2 1 
ATOM   730 N N   . LYS A 1 90 ? 20.269 9.704   31.306 1.00 46.12  ? 90  LYS A N   1 
ATOM   731 C CA  . LYS A 1 90 ? 19.793 10.966  31.857 1.00 48.88  ? 90  LYS A CA  1 
ATOM   732 C C   . LYS A 1 90 ? 19.941 12.101  30.846 1.00 46.17  ? 90  LYS A C   1 
ATOM   733 O O   . LYS A 1 90 ? 19.263 13.109  30.962 1.00 45.89  ? 90  LYS A O   1 
ATOM   734 C CB  . LYS A 1 90 ? 20.569 11.406  33.103 1.00 56.71  ? 90  LYS A CB  1 
ATOM   735 C CG  . LYS A 1 90 ? 20.669 10.398  34.236 1.00 64.28  ? 90  LYS A CG  1 
ATOM   736 C CD  . LYS A 1 90 ? 19.355 10.057  34.925 1.00 71.74  ? 90  LYS A CD  1 
ATOM   737 C CE  . LYS A 1 90 ? 19.567 9.114   36.071 1.00 79.61  ? 90  LYS A CE  1 
ATOM   738 N NZ  . LYS A 1 90 ? 18.323 8.852   36.800 1.00 81.95  ? 90  LYS A NZ  1 
ATOM   739 N N   . ASN A 1 91 ? 20.832 11.951  29.861 1.00 44.34  ? 91  ASN A N   1 
ATOM   740 C CA  . ASN A 1 91 ? 20.974 12.939  28.807 1.00 45.23  ? 91  ASN A CA  1 
ATOM   741 C C   . ASN A 1 91 ? 19.892 12.813  27.725 1.00 43.32  ? 91  ASN A C   1 
ATOM   742 O O   . ASN A 1 91 ? 19.931 13.555  26.746 1.00 44.34  ? 91  ASN A O   1 
ATOM   743 C CB  . ASN A 1 91 ? 22.338 12.818  28.142 1.00 45.57  ? 91  ASN A CB  1 
ATOM   744 C CG  . ASN A 1 91 ? 23.459 13.165  29.086 1.00 50.13  ? 91  ASN A CG  1 
ATOM   745 O OD1 . ASN A 1 91 ? 23.225 13.782  30.129 1.00 53.59  ? 91  ASN A OD1 1 
ATOM   746 N ND2 . ASN A 1 91 ? 24.678 12.809  28.720 1.00 51.51  ? 91  ASN A ND2 1 
ATOM   747 N N   . TYR A 1 92 ? 18.934 11.890  27.869 1.00 40.19  ? 92  TYR A N   1 
ATOM   748 C CA  . TYR A 1 92 ? 17.984 11.621  26.796 1.00 37.65  ? 92  TYR A CA  1 
ATOM   749 C C   . TYR A 1 92 ? 16.555 11.555  27.313 1.00 37.25  ? 92  TYR A C   1 
ATOM   750 O O   . TYR A 1 92 ? 15.748 10.839  26.738 1.00 37.22  ? 92  TYR A O   1 
ATOM   751 C CB  . TYR A 1 92 ? 18.362 10.298  26.123 1.00 37.91  ? 92  TYR A CB  1 
ATOM   752 C CG  . TYR A 1 92 ? 19.724 10.378  25.465 1.00 38.10  ? 92  TYR A CG  1 
ATOM   753 C CD1 . TYR A 1 92 ? 19.864 10.962  24.213 1.00 40.43  ? 92  TYR A CD1 1 
ATOM   754 C CD2 . TYR A 1 92 ? 20.873 9.958   26.128 1.00 40.30  ? 92  TYR A CD2 1 
ATOM   755 C CE1 . TYR A 1 92 ? 21.110 11.093  23.623 1.00 43.33  ? 92  TYR A CE1 1 
ATOM   756 C CE2 . TYR A 1 92 ? 22.128 10.095  25.552 1.00 41.20  ? 92  TYR A CE2 1 
ATOM   757 C CZ  . TYR A 1 92 ? 22.243 10.656  24.292 1.00 43.26  ? 92  TYR A CZ  1 
ATOM   758 O OH  . TYR A 1 92 ? 23.458 10.779  23.691 1.00 49.58  ? 92  TYR A OH  1 
ATOM   759 N N   . ASP A 1 93 ? 16.245 12.294  28.383 1.00 40.61  ? 93  ASP A N   1 
ATOM   760 C CA  . ASP A 1 93 ? 14.942 12.207  29.023 1.00 44.74  ? 93  ASP A CA  1 
ATOM   761 C C   . ASP A 1 93 ? 14.045 13.317  28.486 1.00 44.91  ? 93  ASP A C   1 
ATOM   762 O O   . ASP A 1 93 ? 14.316 14.484  28.755 1.00 45.16  ? 93  ASP A O   1 
ATOM   763 C CB  . ASP A 1 93 ? 15.063 12.299  30.541 1.00 50.44  ? 93  ASP A CB  1 
ATOM   764 C CG  . ASP A 1 93 ? 13.779 12.089  31.338 1.00 52.97  ? 93  ASP A CG  1 
ATOM   765 O OD1 . ASP A 1 93 ? 12.678 12.254  30.772 1.00 47.56  ? 93  ASP A OD1 1 
ATOM   766 O OD2 . ASP A 1 93 ? 13.885 11.721  32.528 1.00 57.26  ? 93  ASP A OD2 1 
ATOM   767 N N   . PRO A 1 94 ? 12.960 12.997  27.737 1.00 43.62  ? 94  PRO A N   1 
ATOM   768 C CA  . PRO A 1 94 ? 12.053 14.022  27.235 1.00 46.03  ? 94  PRO A CA  1 
ATOM   769 C C   . PRO A 1 94 ? 11.289 14.752  28.328 1.00 50.98  ? 94  PRO A C   1 
ATOM   770 O O   . PRO A 1 94 ? 10.934 15.908  28.143 1.00 54.76  ? 94  PRO A O   1 
ATOM   771 C CB  . PRO A 1 94 ? 11.111 13.278  26.300 1.00 46.54  ? 94  PRO A CB  1 
ATOM   772 C CG  . PRO A 1 94 ? 11.253 11.818  26.674 1.00 45.14  ? 94  PRO A CG  1 
ATOM   773 C CD  . PRO A 1 94 ? 12.623 11.650  27.251 1.00 45.09  ? 94  PRO A CD  1 
ATOM   774 N N   . TYR A 1 95 ? 11.036 14.061  29.449 1.00 52.11  ? 95  TYR A N   1 
ATOM   775 C CA  . TYR A 1 95 ? 10.294 14.630  30.565 1.00 54.33  ? 95  TYR A CA  1 
ATOM   776 C C   . TYR A 1 95 ? 11.230 15.331  31.548 1.00 60.15  ? 95  TYR A C   1 
ATOM   777 O O   . TYR A 1 95 ? 10.797 15.752  32.619 1.00 62.02  ? 95  TYR A O   1 
ATOM   778 C CB  . TYR A 1 95 ? 9.464  13.561  31.285 1.00 49.23  ? 95  TYR A CB  1 
ATOM   779 C CG  . TYR A 1 95 ? 8.099  13.393  30.648 1.00 47.28  ? 95  TYR A CG  1 
ATOM   780 C CD1 . TYR A 1 95 ? 7.067  14.258  30.965 1.00 48.47  ? 95  TYR A CD1 1 
ATOM   781 C CD2 . TYR A 1 95 ? 7.862  12.424  29.689 1.00 44.62  ? 95  TYR A CD2 1 
ATOM   782 C CE1 . TYR A 1 95 ? 5.818  14.131  30.382 1.00 50.49  ? 95  TYR A CE1 1 
ATOM   783 C CE2 . TYR A 1 95 ? 6.618  12.288  29.097 1.00 46.07  ? 95  TYR A CE2 1 
ATOM   784 C CZ  . TYR A 1 95 ? 5.592  13.144  29.440 1.00 48.25  ? 95  TYR A CZ  1 
ATOM   785 O OH  . TYR A 1 95 ? 4.359  13.038  28.853 1.00 53.53  ? 95  TYR A OH  1 
ATOM   786 N N   . LYS A 1 96 ? 12.513 15.447  31.206 1.00 67.94  ? 96  LYS A N   1 
ATOM   787 C CA  . LYS A 1 96 ? 13.393 16.312  31.972 1.00 78.76  ? 96  LYS A CA  1 
ATOM   788 C C   . LYS A 1 96 ? 14.604 16.648  31.105 1.00 86.39  ? 96  LYS A C   1 
ATOM   789 O O   . LYS A 1 96 ? 15.704 16.169  31.368 1.00 89.60  ? 96  LYS A O   1 
ATOM   790 C CB  . LYS A 1 96 ? 13.749 15.657  33.315 1.00 81.62  ? 96  LYS A CB  1 
ATOM   791 C CG  . LYS A 1 96 ? 13.994 16.638  34.463 1.00 91.39  ? 96  LYS A CG  1 
ATOM   792 C CD  . LYS A 1 96 ? 14.471 15.993  35.762 1.00 95.00  ? 96  LYS A CD  1 
ATOM   793 C CE  . LYS A 1 96 ? 14.864 16.985  36.817 1.00 99.25  ? 96  LYS A CE  1 
ATOM   794 N NZ  . LYS A 1 96 ? 15.587 16.346  37.920 1.00 101.12 ? 96  LYS A NZ  1 
ATOM   795 N N   . PRO A 1 97 ? 14.430 17.464  30.034 1.00 95.12  ? 97  PRO A N   1 
ATOM   796 C CA  . PRO A 1 97 ? 15.545 17.853  29.170 1.00 97.22  ? 97  PRO A CA  1 
ATOM   797 C C   . PRO A 1 97 ? 16.679 18.561  29.915 1.00 100.11 ? 97  PRO A C   1 
ATOM   798 O O   . PRO A 1 97 ? 16.453 19.138  30.976 1.00 102.46 ? 97  PRO A O   1 
ATOM   799 C CB  . PRO A 1 97 ? 14.887 18.760  28.123 1.00 98.42  ? 97  PRO A CB  1 
ATOM   800 C CG  . PRO A 1 97 ? 13.412 18.387  28.165 1.00 97.70  ? 97  PRO A CG  1 
ATOM   801 C CD  . PRO A 1 97 ? 13.144 18.038  29.599 1.00 95.55  ? 97  PRO A CD  1 
ATOM   802 N N   . LEU A 1 98 ? 17.901 18.497  29.362 1.00 99.99  ? 98  LEU A N   1 
ATOM   803 C CA  . LEU A 1 98 ? 19.042 19.217  29.912 1.00 100.28 ? 98  LEU A CA  1 
ATOM   804 C C   . LEU A 1 98 ? 19.731 19.997  28.779 1.00 99.19  ? 98  LEU A C   1 
ATOM   805 O O   . LEU A 1 98 ? 19.741 21.243  28.877 1.00 98.70  ? 98  LEU A O   1 
ATOM   806 C CB  . LEU A 1 98 ? 20.021 18.295  30.649 1.00 100.49 ? 98  LEU A CB  1 
ATOM   807 C CG  . LEU A 1 98 ? 20.785 17.246  29.828 1.00 100.40 ? 98  LEU A CG  1 
ATOM   808 C CD1 . LEU A 1 98 ? 21.876 17.824  28.929 1.00 102.11 ? 98  LEU A CD1 1 
ATOM   809 C CD2 . LEU A 1 98 ? 21.384 16.220  30.779 1.00 97.20  ? 98  LEU A CD2 1 
HETATM 810 S S   . SO4 B 2 .  ? -3.523 12.658  32.909 1.00 102.68 ? 201 SO4 A S   1 
HETATM 811 O O1  . SO4 B 2 .  ? -4.079 12.761  31.584 1.00 101.70 ? 201 SO4 A O1  1 
HETATM 812 O O2  . SO4 B 2 .  ? -2.100 12.511  32.812 1.00 94.23  ? 201 SO4 A O2  1 
HETATM 813 O O3  . SO4 B 2 .  ? -3.830 13.849  33.660 1.00 110.19 ? 201 SO4 A O3  1 
HETATM 814 O O4  . SO4 B 2 .  ? -4.084 11.514  33.579 1.00 96.05  ? 201 SO4 A O4  1 
HETATM 815 O O   . HOH C 3 .  ? 7.526  -2.703  24.332 1.00 65.60  ? 301 HOH A O   1 
HETATM 816 O O   . HOH C 3 .  ? 2.688  14.697  29.054 1.00 52.26  ? 302 HOH A O   1 
HETATM 817 O O   . HOH C 3 .  ? -0.588 7.282   27.921 1.00 57.01  ? 303 HOH A O   1 
HETATM 818 O O   . HOH C 3 .  ? 23.025 8.871   34.754 1.00 64.88  ? 304 HOH A O   1 
HETATM 819 O O   . HOH C 3 .  ? 20.744 10.046  17.870 1.00 65.81  ? 305 HOH A O   1 
HETATM 820 O O   . HOH C 3 .  ? 5.493  -3.338  16.264 1.00 65.14  ? 306 HOH A O   1 
HETATM 821 O O   . HOH C 3 .  ? -3.588 9.392   34.792 1.00 48.03  ? 307 HOH A O   1 
HETATM 822 O O   . HOH C 3 .  ? 29.307 9.259   26.554 1.00 51.86  ? 308 HOH A O   1 
HETATM 823 O O   . HOH C 3 .  ? 11.854 12.379  33.859 1.00 51.91  ? 309 HOH A O   1 
HETATM 824 O O   . HOH C 3 .  ? 10.582 11.871  22.866 1.00 43.92  ? 310 HOH A O   1 
HETATM 825 O O   . HOH C 3 .  ? 28.788 7.657   28.751 0.50 44.50  ? 311 HOH A O   1 
HETATM 826 O O   . HOH C 3 .  ? 22.566 4.856   31.124 1.00 37.17  ? 312 HOH A O   1 
HETATM 827 O O   . HOH C 3 .  ? 22.528 3.833   15.532 1.00 36.63  ? 313 HOH A O   1 
HETATM 828 O O   . HOH C 3 .  ? 17.850 14.638  29.416 1.00 51.66  ? 314 HOH A O   1 
HETATM 829 O O   . HOH C 3 .  ? 1.589  -3.509  32.126 1.00 44.88  ? 315 HOH A O   1 
HETATM 830 O O   . HOH C 3 .  ? 23.306 -3.211  29.921 1.00 47.71  ? 316 HOH A O   1 
HETATM 831 O O   . HOH C 3 .  ? 26.217 -4.666  22.106 1.00 49.12  ? 317 HOH A O   1 
HETATM 832 O O   . HOH C 3 .  ? 1.472  14.551  21.214 1.00 41.19  ? 318 HOH A O   1 
HETATM 833 O O   . HOH C 3 .  ? 25.405 10.988  25.473 1.00 48.85  ? 319 HOH A O   1 
HETATM 834 O O   . HOH C 3 .  ? -1.931 -0.866  35.699 1.00 42.90  ? 320 HOH A O   1 
HETATM 835 O O   . HOH C 3 .  ? 26.726 -1.058  18.651 1.00 58.75  ? 321 HOH A O   1 
HETATM 836 O O   . HOH C 3 .  ? 13.645 -1.785  9.899  1.00 52.54  ? 322 HOH A O   1 
HETATM 837 O O   . HOH C 3 .  ? 19.811 -3.791  14.279 1.00 49.90  ? 323 HOH A O   1 
HETATM 838 O O   . HOH C 3 .  ? 1.698  13.963  31.500 1.00 61.97  ? 324 HOH A O   1 
HETATM 839 O O   . HOH C 3 .  ? 16.387 9.115   31.364 1.00 42.80  ? 325 HOH A O   1 
HETATM 840 O O   . HOH C 3 .  ? 3.783  0.869   17.681 1.00 59.03  ? 326 HOH A O   1 
HETATM 841 O O   . HOH C 3 .  ? -2.529 5.649   31.564 1.00 38.63  ? 327 HOH A O   1 
HETATM 842 O O   . HOH C 3 .  ? 26.477 -2.026  28.621 1.00 48.07  ? 328 HOH A O   1 
HETATM 843 O O   . HOH C 3 .  ? 2.385  6.779   25.235 1.00 44.64  ? 329 HOH A O   1 
HETATM 844 O O   . HOH C 3 .  ? 32.024 5.267   22.899 1.00 50.33  ? 330 HOH A O   1 
HETATM 845 O O   . HOH C 3 .  ? 30.310 -2.617  22.679 1.00 55.46  ? 331 HOH A O   1 
HETATM 846 O O   . HOH C 3 .  ? 20.632 2.888   30.849 1.00 37.71  ? 332 HOH A O   1 
HETATM 847 O O   . HOH C 3 .  ? 13.434 8.840   33.721 1.00 54.82  ? 333 HOH A O   1 
HETATM 848 O O   . HOH C 3 .  ? 18.795 13.444  21.480 1.00 57.22  ? 334 HOH A O   1 
HETATM 849 O O   . HOH C 3 .  ? 5.375  1.730   19.993 1.00 44.67  ? 335 HOH A O   1 
HETATM 850 O O   . HOH C 3 .  ? 10.797 11.011  18.393 1.00 44.56  ? 336 HOH A O   1 
HETATM 851 O O   . HOH C 3 .  ? 16.251 12.194  33.961 1.00 52.93  ? 337 HOH A O   1 
HETATM 852 O O   . HOH C 3 .  ? 25.162 10.003  16.559 1.00 60.29  ? 338 HOH A O   1 
HETATM 853 O O   . HOH C 3 .  ? 14.118 8.074   15.526 1.00 58.18  ? 339 HOH A O   1 
HETATM 854 O O   . HOH C 3 .  ? 0.682  9.411   23.265 1.00 48.77  ? 340 HOH A O   1 
HETATM 855 O O   . HOH C 3 .  ? 6.030  2.779   15.025 1.00 57.03  ? 341 HOH A O   1 
HETATM 856 O O   . HOH C 3 .  ? 31.722 -0.262  25.090 1.00 51.54  ? 342 HOH A O   1 
HETATM 857 O O   . HOH C 3 .  ? 28.802 1.885   28.802 0.50 39.53  ? 343 HOH A O   1 
HETATM 858 O O   . HOH C 3 .  ? 0.898  4.967   26.623 1.00 45.12  ? 344 HOH A O   1 
HETATM 859 O O   . HOH C 3 .  ? 1.263  0.621   33.331 1.00 41.14  ? 345 HOH A O   1 
HETATM 860 O O   . HOH C 3 .  ? 1.481  0.654   29.104 1.00 42.67  ? 346 HOH A O   1 
HETATM 861 O O   . HOH C 3 .  ? 7.109  11.659  17.132 1.00 54.09  ? 347 HOH A O   1 
HETATM 862 O O   . HOH C 3 .  ? 28.277 -0.406  27.410 1.00 48.82  ? 348 HOH A O   1 
HETATM 863 O O   . HOH C 3 .  ? 26.505 9.678   27.687 1.00 51.57  ? 349 HOH A O   1 
HETATM 864 O O   . HOH C 3 .  ? 15.522 -4.006  11.438 1.00 67.71  ? 350 HOH A O   1 
HETATM 865 O O   . HOH C 3 .  ? 4.770  0.547   14.421 1.00 79.04  ? 351 HOH A O   1 
HETATM 866 O O   . HOH C 3 .  ? 6.497  0.654   35.975 1.00 50.64  ? 352 HOH A O   1 
HETATM 867 O O   . HOH C 3 .  ? 0.874  2.210   31.229 1.00 45.46  ? 353 HOH A O   1 
HETATM 868 O O   . HOH C 3 .  ? -4.144 0.298   36.481 1.00 55.60  ? 354 HOH A O   1 
HETATM 869 O O   . HOH C 3 .  ? 27.861 0.355   15.554 1.00 47.21  ? 355 HOH A O   1 
HETATM 870 O O   . HOH C 3 .  ? -5.344 5.357   17.603 1.00 74.40  ? 356 HOH A O   1 
HETATM 871 O O   . HOH C 3 .  ? 3.271  0.435   39.714 1.00 53.45  ? 357 HOH A O   1 
HETATM 872 O O   . HOH C 3 .  ? 15.078 11.102  19.783 1.00 48.21  ? 358 HOH A O   1 
HETATM 873 O O   . HOH C 3 .  ? 34.383 4.660   23.856 1.00 51.98  ? 359 HOH A O   1 
HETATM 874 O O   . HOH C 3 .  ? 22.985 -0.733  13.835 1.00 54.41  ? 360 HOH A O   1 
HETATM 875 O O   . HOH C 3 .  ? 26.919 -7.239  21.298 1.00 73.13  ? 361 HOH A O   1 
HETATM 876 O O   . HOH C 3 .  ? 10.157 -6.262  19.993 1.00 63.51  ? 362 HOH A O   1 
HETATM 877 O O   . HOH C 3 .  ? 11.689 15.542  37.429 1.00 63.14  ? 363 HOH A O   1 
HETATM 878 O O   . HOH C 3 .  ? 18.809 -0.179  33.726 1.00 51.96  ? 364 HOH A O   1 
HETATM 879 O O   . HOH C 3 .  ? 22.781 -1.492  32.034 1.00 55.60  ? 365 HOH A O   1 
HETATM 880 O O   . HOH C 3 .  ? 21.110 0.809   32.549 1.00 47.78  ? 366 HOH A O   1 
HETATM 881 O O   . HOH C 3 .  ? 30.816 -1.821  26.625 1.00 43.21  ? 367 HOH A O   1 
HETATM 882 O O   . HOH C 3 .  ? 33.735 -1.784  20.831 1.00 61.82  ? 368 HOH A O   1 
HETATM 883 O O   . HOH C 3 .  ? 28.803 10.442  28.802 0.50 41.32  ? 369 HOH A O   1 
HETATM 884 O O   . HOH C 3 .  ? 10.999 10.999  46.606 0.33 65.44  ? 370 HOH A O   1 
HETATM 885 O O   . HOH C 3 .  ? 34.896 2.085   23.171 1.00 58.12  ? 371 HOH A O   1 
HETATM 886 O O   . HOH C 3 .  ? 17.142 17.142  17.142 0.33 58.92  ? 372 HOH A O   1 
HETATM 887 O O   . HOH C 3 .  ? 13.817 13.817  13.817 0.33 69.88  ? 373 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   . GLY A 4  ? 0.7000 0.6389 0.9381 0.2185  0.1617  0.2751  4  GLY A N   
2   C CA  . GLY A 4  ? 0.6753 0.6293 0.8898 0.1843  0.1341  0.2324  4  GLY A CA  
3   C C   . GLY A 4  ? 0.6140 0.6287 0.8093 0.1696  0.1025  0.2351  4  GLY A C   
4   O O   . GLY A 4  ? 0.6395 0.6786 0.8350 0.1796  0.1011  0.2634  4  GLY A O   
5   N N   . ILE A 5  ? 0.6092 0.6462 0.7878 0.1457  0.0798  0.2051  5  ILE A N   
6   C CA  . ILE A 5  ? 0.5710 0.6667 0.7350 0.1319  0.0531  0.2029  5  ILE A CA  
7   C C   . ILE A 5  ? 0.5605 0.6418 0.7099 0.1172  0.0467  0.1998  5  ILE A C   
8   O O   . ILE A 5  ? 0.5366 0.6674 0.6769 0.1127  0.0309  0.2059  5  ILE A O   
9   C CB  . ILE A 5  ? 0.5596 0.6692 0.7129 0.1101  0.0374  0.1726  5  ILE A CB  
10  C CG1 . ILE A 5  ? 0.5721 0.6250 0.7116 0.0903  0.0392  0.1423  5  ILE A CG1 
11  C CG2 . ILE A 5  ? 0.5937 0.7352 0.7634 0.1248  0.0427  0.1796  5  ILE A CG2 
12  C CD1 . ILE A 5  ? 0.5810 0.6466 0.7068 0.0699  0.0245  0.1188  5  ILE A CD1 
13  N N   . PHE A 6  ? 0.5445 0.5633 0.6929 0.1086  0.0600  0.1878  6  PHE A N   
14  C CA  . PHE A 6  ? 0.5515 0.5577 0.6893 0.0941  0.0560  0.1838  6  PHE A CA  
15  C C   . PHE A 6  ? 0.6018 0.5897 0.7525 0.1103  0.0772  0.2159  6  PHE A C   
16  O O   . PHE A 6  ? 0.6079 0.5711 0.7550 0.0971  0.0818  0.2113  6  PHE A O   
17  C CB  . PHE A 6  ? 0.5605 0.5209 0.6902 0.0708  0.0561  0.1480  6  PHE A CB  
18  C CG  . PHE A 6  ? 0.5085 0.4850 0.6226 0.0555  0.0366  0.1214  6  PHE A CG  
19  C CD1 . PHE A 6  ? 0.5020 0.5211 0.6047 0.0492  0.0171  0.1204  6  PHE A CD1 
20  C CD2 . PHE A 6  ? 0.5374 0.4864 0.6484 0.0469  0.0405  0.0972  6  PHE A CD2 
21  C CE1 . PHE A 6  ? 0.4893 0.5136 0.5805 0.0357  0.0048  0.0990  6  PHE A CE1 
22  C CE2 . PHE A 6  ? 0.5058 0.4690 0.6022 0.0356  0.0256  0.0793  6  PHE A CE2 
23  C CZ  . PHE A 6  ? 0.4719 0.4683 0.5598 0.0307  0.0092  0.0821  6  PHE A CZ  
24  N N   . ALA A 7  ? 0.6255 0.6289 0.7926 0.1401  0.0916  0.2515  7  ALA A N   
25  C CA  . ALA A 7  ? 0.6631 0.6483 0.8435 0.1598  0.1154  0.2898  7  ALA A CA  
26  C C   . ALA A 7  ? 0.6683 0.6982 0.8328 0.1543  0.1017  0.3044  7  ALA A C   
27  O O   . ALA A 7  ? 0.6292 0.7271 0.7787 0.1510  0.0763  0.3008  7  ALA A O   
28  C CB  . ALA A 7  ? 0.6832 0.6894 0.8835 0.1984  0.1316  0.3307  7  ALA A CB  
29  N N   . ASN A 8  ? 0.6884 0.6794 0.8580 0.1518  0.1212  0.3186  8  ASN A N   
30  C CA  . ASN A 8  ? 0.7154 0.7423 0.8716 0.1478  0.1147  0.3351  8  ASN A CA  
31  C C   . ASN A 8  ? 0.6446 0.6873 0.7792 0.1154  0.0884  0.2926  8  ASN A C   
32  O O   . ASN A 8  ? 0.6338 0.7209 0.7532 0.1110  0.0771  0.2984  8  ASN A O   
33  C CB  . ASN A 8  ? 0.7226 0.8310 0.8732 0.1761  0.1073  0.3775  8  ASN A CB  
34  C CG  . ASN A 8  ? 0.8123 0.9095 0.9859 0.2148  0.1358  0.4282  8  ASN A CG  
35  O OD1 . ASN A 8  ? 0.8382 0.8767 1.0273 0.2231  0.1677  0.4530  8  ASN A OD1 
36  N ND2 . ASN A 8  ? 0.8244 0.9776 1.0033 0.2393  0.1274  0.4452  8  ASN A ND2 
37  N N   . CYS A 9  ? 0.6318 0.6407 0.7651 0.0951  0.0804  0.2514  9  CYS A N   
38  C CA  . CYS A 9  ? 0.6252 0.6417 0.7415 0.0688  0.0601  0.2151  9  CYS A CA  
39  C C   . CYS A 9  ? 0.6242 0.5883 0.7482 0.0497  0.0737  0.1968  9  CYS A C   
40  O O   . CYS A 9  ? 0.6450 0.5598 0.7845 0.0476  0.0920  0.1896  9  CYS A O   
41  C CB  . CYS A 9  ? 0.6086 0.6319 0.7167 0.0596  0.0416  0.1843  9  CYS A CB  
42  S SG  . CYS A 9  ? 0.6013 0.6948 0.7022 0.0716  0.0234  0.1943  9  CYS A SG  
43  N N   . ILE A 10 ? 0.6094 0.5899 0.7235 0.0349  0.0653  0.1869  10 ILE A N   
44  C CA  . ILE A 10 ? 0.6147 0.5624 0.7369 0.0139  0.0748  0.1671  10 ILE A CA  
45  C C   . ILE A 10 ? 0.5697 0.5392 0.6769 -0.0015 0.0514  0.1338  10 ILE A C   
46  O O   . ILE A 10 ? 0.4945 0.5022 0.5880 -0.0005 0.0379  0.1351  10 ILE A O   
47  C CB  . ILE A 10 ? 0.6454 0.5934 0.7754 0.0138  0.0929  0.1931  10 ILE A CB  
48  C CG1 . ILE A 10 ? 0.6968 0.6225 0.8421 0.0358  0.1192  0.2348  10 ILE A CG1 
49  C CG2 . ILE A 10 ? 0.6694 0.5911 0.8116 -0.0120 0.1033  0.1697  10 ILE A CG2 
50  C CD1 . ILE A 10 ? 0.7257 0.6345 0.8841 0.0345  0.1461  0.2634  10 ILE A CD1 
51  N N   . PHE A 11 ? 0.5705 0.5169 0.6810 -0.0143 0.0492  0.1048  11 PHE A N   
52  C CA  . PHE A 11 ? 0.5620 0.5275 0.6595 -0.0231 0.0291  0.0782  11 PHE A CA  
53  C C   . PHE A 11 ? 0.5692 0.5365 0.6736 -0.0410 0.0313  0.0593  11 PHE A C   
54  O O   . PHE A 11 ? 0.5939 0.5376 0.7131 -0.0540 0.0455  0.0475  11 PHE A O   
55  C CB  . PHE A 11 ? 0.5636 0.5162 0.6571 -0.0219 0.0235  0.0623  11 PHE A CB  
56  C CG  . PHE A 11 ? 0.5616 0.5221 0.6494 -0.0064 0.0186  0.0766  11 PHE A CG  
57  C CD1 . PHE A 11 ? 0.6076 0.5513 0.7071 0.0055  0.0335  0.0945  11 PHE A CD1 
58  C CD2 . PHE A 11 ? 0.5569 0.5428 0.6307 -0.0040 0.0016  0.0718  11 PHE A CD2 
59  C CE1 . PHE A 11 ? 0.5895 0.5520 0.6867 0.0200  0.0284  0.1076  11 PHE A CE1 
60  C CE2 . PHE A 11 ? 0.5523 0.5528 0.6243 0.0057  -0.0021 0.0818  11 PHE A CE2 
61  C CZ  . PHE A 11 ? 0.5477 0.5416 0.6314 0.0180  0.0097  0.1000  11 PHE A CZ  
62  N N   . CYS A 12 ? 0.5602 0.5588 0.6557 -0.0421 0.0185  0.0541  12 CYS A N   
63  C CA  . CYS A 12 ? 0.5483 0.5631 0.6490 -0.0553 0.0147  0.0335  12 CYS A CA  
64  C C   . CYS A 12 ? 0.4898 0.5158 0.5789 -0.0510 -0.0015 0.0164  12 CYS A C   
65  O O   . CYS A 12 ? 0.5101 0.5443 0.5856 -0.0389 -0.0123 0.0207  12 CYS A O   
66  C CB  . CYS A 12 ? 0.5487 0.5930 0.6486 -0.0552 0.0131  0.0393  12 CYS A CB  
67  S SG  . CYS A 12 ? 0.6118 0.6900 0.7205 -0.0664 0.0067  0.0159  12 CYS A SG  
68  N N   . LEU A 13 ? 0.4987 0.5261 0.5934 -0.0615 -0.0013 -0.0028 13 LEU A N   
69  C CA  . LEU A 13 ? 0.4730 0.5153 0.5554 -0.0551 -0.0149 -0.0141 13 LEU A CA  
70  C C   . LEU A 13 ? 0.4616 0.5449 0.5460 -0.0556 -0.0239 -0.0235 13 LEU A C   
71  O O   . LEU A 13 ? 0.4302 0.5353 0.5291 -0.0711 -0.0195 -0.0368 13 LEU A O   
72  C CB  . LEU A 13 ? 0.5161 0.5463 0.5994 -0.0631 -0.0102 -0.0293 13 LEU A CB  
73  C CG  . LEU A 13 ? 0.5446 0.5352 0.6298 -0.0598 0.0016  -0.0202 13 LEU A CG  
74  C CD1 . LEU A 13 ? 0.5889 0.5705 0.6753 -0.0687 0.0084  -0.0410 13 LEU A CD1 
75  C CD2 . LEU A 13 ? 0.5559 0.5412 0.6282 -0.0422 -0.0062 -0.0018 13 LEU A CD2 
76  N N   . LYS A 14 ? 0.4095 0.5035 0.4821 -0.0383 -0.0340 -0.0159 14 LYS A N   
77  C CA  . LYS A 14 ? 0.4196 0.5523 0.4930 -0.0299 -0.0420 -0.0198 14 LYS A CA  
78  C C   . LYS A 14 ? 0.4226 0.5584 0.4820 -0.0153 -0.0496 -0.0166 14 LYS A C   
79  O O   . LYS A 14 ? 0.4282 0.5511 0.4790 0.0014  -0.0509 -0.0050 14 LYS A O   
80  C CB  . LYS A 14 ? 0.4450 0.5802 0.5180 -0.0182 -0.0414 -0.0104 14 LYS A CB  
81  C CG  . LYS A 14 ? 0.4909 0.6301 0.5748 -0.0295 -0.0332 -0.0092 14 LYS A CG  
82  C CD  . LYS A 14 ? 0.5256 0.6984 0.6280 -0.0455 -0.0300 -0.0206 14 LYS A CD  
83  C CE  . LYS A 14 ? 0.5582 0.7364 0.6722 -0.0558 -0.0191 -0.0158 14 LYS A CE  
84  N NZ  . LYS A 14 ? 0.5605 0.7752 0.6960 -0.0743 -0.0147 -0.0292 14 LYS A NZ  
85  N N   . VAL A 15 ? 0.4352 0.5855 0.4925 -0.0232 -0.0517 -0.0277 15 VAL A N   
86  C CA  . VAL A 15 ? 0.4502 0.6044 0.4918 -0.0105 -0.0568 -0.0225 15 VAL A CA  
87  C C   . VAL A 15 ? 0.4681 0.6817 0.5097 -0.0120 -0.0642 -0.0341 15 VAL A C   
88  O O   . VAL A 15 ? 0.4839 0.7115 0.5139 -0.0130 -0.0664 -0.0402 15 VAL A O   
89  C CB  . VAL A 15 ? 0.4573 0.5731 0.4917 -0.0173 -0.0510 -0.0241 15 VAL A CB  
90  C CG1 . VAL A 15 ? 0.4563 0.5301 0.4900 -0.0124 -0.0464 -0.0102 15 VAL A CG1 
91  C CG2 . VAL A 15 ? 0.4635 0.5755 0.5080 -0.0391 -0.0435 -0.0443 15 VAL A CG2 
92  N N   . LYS A 16 ? 0.4393 0.6949 0.4934 -0.0104 -0.0681 -0.0364 16 LYS A N   
93  C CA  . LYS A 16 ? 0.4974 0.8267 0.5570 -0.0139 -0.0763 -0.0493 16 LYS A CA  
94  C C   . LYS A 16 ? 0.4822 0.8482 0.5237 0.0083  -0.0845 -0.0364 16 LYS A C   
95  O O   . LYS A 16 ? 0.4748 0.9068 0.5150 0.0020  -0.0921 -0.0508 16 LYS A O   
96  C CB  . LYS A 16 ? 0.5329 0.8980 0.6093 -0.0060 -0.0782 -0.0440 16 LYS A CB  
97  C CG  . LYS A 16 ? 0.6257 1.0796 0.7158 -0.0122 -0.0866 -0.0585 16 LYS A CG  
98  C CD  . LYS A 16 ? 0.6596 1.1406 0.7717 -0.0108 -0.0845 -0.0568 16 LYS A CD  
99  C CE  . LYS A 16 ? 0.7199 1.2927 0.8524 -0.0263 -0.0909 -0.0771 16 LYS A CE  
100 N NZ  . LYS A 16 ? 0.7588 1.4108 0.8890 0.0042  -0.1033 -0.0620 16 LYS A NZ  
101 N N   . TYR A 17 ? 0.4456 0.7748 0.4739 0.0339  -0.0819 -0.0092 17 TYR A N   
102 C CA  . TYR A 17 ? 0.4661 0.8317 0.4795 0.0610  -0.0864 0.0120  17 TYR A CA  
103 C C   . TYR A 17 ? 0.4619 0.7994 0.4550 0.0602  -0.0831 0.0163  17 TYR A C   
104 O O   . TYR A 17 ? 0.4605 0.8232 0.4385 0.0823  -0.0842 0.0375  17 TYR A O   
105 C CB  . TYR A 17 ? 0.4849 0.8334 0.5022 0.0927  -0.0811 0.0416  17 TYR A CB  
106 C CG  . TYR A 17 ? 0.4754 0.8681 0.5129 0.0970  -0.0844 0.0374  17 TYR A CG  
107 C CD1 . TYR A 17 ? 0.4796 0.9625 0.5228 0.1071  -0.0946 0.0381  17 TYR A CD1 
108 C CD2 . TYR A 17 ? 0.4953 0.8486 0.5464 0.0896  -0.0776 0.0314  17 TYR A CD2 
109 C CE1 . TYR A 17 ? 0.5041 1.0347 0.5689 0.1099  -0.0972 0.0334  17 TYR A CE1 
110 C CE2 . TYR A 17 ? 0.4872 0.8837 0.5575 0.0928  -0.0790 0.0271  17 TYR A CE2 
111 C CZ  . TYR A 17 ? 0.4863 0.9705 0.5649 0.1026  -0.0886 0.0280  17 TYR A CZ  
112 O OH  . TYR A 17 ? 0.5335 1.0654 0.6339 0.1054  -0.0893 0.0236  17 TYR A OH  
113 N N   . LEU A 18 ? 0.4646 0.7529 0.4581 0.0371  -0.0775 -0.0009 18 LEU A N   
114 C CA  . LEU A 18 ? 0.4845 0.7532 0.4617 0.0341  -0.0735 -0.0012 18 LEU A CA  
115 C C   . LEU A 18 ? 0.5053 0.8388 0.4733 0.0235  -0.0797 -0.0227 18 LEU A C   
116 O O   . LEU A 18 ? 0.4969 0.8682 0.4774 0.0049  -0.0839 -0.0486 18 LEU A O   
117 C CB  . LEU A 18 ? 0.4982 0.7049 0.4817 0.0153  -0.0648 -0.0132 18 LEU A CB  
118 C CG  . LEU A 18 ? 0.5160 0.6653 0.5047 0.0224  -0.0587 0.0043  18 LEU A CG  
119 C CD1 . LEU A 18 ? 0.5118 0.6189 0.5060 0.0065  -0.0515 -0.0057 18 LEU A CD1 
120 C CD2 . LEU A 18 ? 0.5433 0.6798 0.5200 0.0436  -0.0551 0.0303  18 LEU A CD2 
121 N N   . PRO A 19 ? 0.5442 0.8926 0.4910 0.0314  -0.0787 -0.0162 19 PRO A N   
122 C CA  . PRO A 19 ? 0.5744 0.9794 0.5107 0.0151  -0.0822 -0.0457 19 PRO A CA  
123 C C   . PRO A 19 ? 0.5980 0.9672 0.5491 -0.0178 -0.0737 -0.0842 19 PRO A C   
124 O O   . PRO A 19 ? 0.5447 0.8416 0.5047 -0.0214 -0.0639 -0.0791 19 PRO A O   
125 C CB  . PRO A 19 ? 0.5817 0.9921 0.4923 0.0309  -0.0785 -0.0274 19 PRO A CB  
126 C CG  . PRO A 19 ? 0.5812 0.9377 0.4912 0.0560  -0.0723 0.0149  19 PRO A CG  
127 C CD  . PRO A 19 ? 0.5406 0.8499 0.4740 0.0521  -0.0714 0.0158  19 PRO A CD  
128 N N   . GLN A 20 ? 0.6327 1.0552 0.5884 -0.0415 -0.0759 -0.1221 20 GLN A N   
129 C CA  . GLN A 20 ? 0.6651 1.0529 0.6401 -0.0743 -0.0633 -0.1600 20 GLN A CA  
130 C C   . GLN A 20 ? 0.6130 0.9346 0.5830 -0.0774 -0.0478 -0.1645 20 GLN A C   
131 O O   . GLN A 20 ? 0.5962 0.8546 0.5848 -0.0893 -0.0341 -0.1715 20 GLN A O   
132 C CB  . GLN A 20 ? 0.7412 1.2063 0.7189 -0.1010 -0.0663 -0.2042 20 GLN A CB  
133 C CG  . GLN A 20 ? 0.8169 1.2439 0.8166 -0.1386 -0.0476 -0.2487 20 GLN A CG  
134 C CD  . GLN A 20 ? 0.8905 1.2709 0.9203 -0.1499 -0.0400 -0.2443 20 GLN A CD  
135 O OE1 . GLN A 20 ? 0.9383 1.2523 0.9729 -0.1334 -0.0359 -0.2119 20 GLN A OE1 
136 N NE2 . GLN A 20 ? 0.9587 1.3785 1.0094 -0.1805 -0.0368 -0.2787 20 GLN A NE2 
137 N N   . GLN A 21 ? 0.6361 0.9774 0.5816 -0.0644 -0.0490 -0.1576 21 GLN A N   
138 C CA  . GLN A 21 ? 0.6933 0.9837 0.6333 -0.0639 -0.0346 -0.1599 21 GLN A CA  
139 C C   . GLN A 21 ? 0.6468 0.8630 0.5989 -0.0506 -0.0293 -0.1279 21 GLN A C   
140 O O   . GLN A 21 ? 0.6394 0.8032 0.6030 -0.0565 -0.0150 -0.1347 21 GLN A O   
141 C CB  . GLN A 21 ? 0.7796 1.1184 0.6892 -0.0485 -0.0391 -0.1500 21 GLN A CB  
142 C CG  . GLN A 21 ? 0.8987 1.2187 0.7996 -0.0559 -0.0235 -0.1715 21 GLN A CG  
143 C CD  . GLN A 21 ? 1.0311 1.4006 0.9004 -0.0391 -0.0267 -0.1566 21 GLN A CD  
144 O OE1 . GLN A 21 ? 1.1171 1.5317 0.9711 -0.0198 -0.0397 -0.1257 21 GLN A OE1 
145 N NE2 . GLN A 21 ? 1.0498 1.4110 0.9096 -0.0442 -0.0125 -0.1758 21 GLN A NE2 
146 N N   . GLN A 22 ? 0.5923 0.8076 0.5429 -0.0322 -0.0398 -0.0940 22 GLN A N   
147 C CA  . GLN A 22 ? 0.5787 0.7357 0.5391 -0.0222 -0.0360 -0.0678 22 GLN A CA  
148 C C   . GLN A 22 ? 0.5652 0.6891 0.5492 -0.0349 -0.0317 -0.0760 22 GLN A C   
149 O O   . GLN A 22 ? 0.5021 0.5795 0.4967 -0.0345 -0.0230 -0.0683 22 GLN A O   
150 C CB  . GLN A 22 ? 0.5614 0.7234 0.5141 -0.0010 -0.0441 -0.0341 22 GLN A CB  
151 C CG  . GLN A 22 ? 0.6102 0.7911 0.5411 0.0143  -0.0430 -0.0160 22 GLN A CG  
152 C CD  . GLN A 22 ? 0.6142 0.7851 0.5416 0.0351  -0.0442 0.0189  22 GLN A CD  
153 O OE1 . GLN A 22 ? 0.6531 0.7881 0.5945 0.0366  -0.0434 0.0281  22 GLN A OE1 
154 N NE2 . GLN A 22 ? 0.6025 0.8046 0.5110 0.0515  -0.0434 0.0386  22 GLN A NE2 
155 N N   . LYS A 23 ? 0.5609 0.7154 0.5537 -0.0454 -0.0372 -0.0899 23 LYS A N   
156 C CA  . LYS A 23 ? 0.5870 0.7134 0.6023 -0.0590 -0.0304 -0.0967 23 LYS A CA  
157 C C   . LYS A 23 ? 0.5482 0.6342 0.5750 -0.0739 -0.0119 -0.1159 23 LYS A C   
158 O O   . LYS A 23 ? 0.5720 0.6122 0.6126 -0.0724 -0.0019 -0.1037 23 LYS A O   
159 C CB  . LYS A 23 ? 0.6235 0.7946 0.6495 -0.0724 -0.0363 -0.1129 23 LYS A CB  
160 C CG  . LYS A 23 ? 0.6906 0.8301 0.7401 -0.0853 -0.0269 -0.1139 23 LYS A CG  
161 C CD  . LYS A 23 ? 0.7961 0.9814 0.8609 -0.1023 -0.0300 -0.1315 23 LYS A CD  
162 C CE  . LYS A 23 ? 0.8403 0.9934 0.9270 -0.1132 -0.0187 -0.1264 23 LYS A CE  
163 N NZ  . LYS A 23 ? 0.8709 1.0652 0.9772 -0.1381 -0.0158 -0.1512 23 LYS A NZ  
164 N N   . LYS A 24 ? 0.6106 0.7164 0.6317 -0.0865 -0.0058 -0.1455 24 LYS A N   
165 C CA  . LYS A 24 ? 0.6628 0.7268 0.6972 -0.1005 0.0164  -0.1682 24 LYS A CA  
166 C C   . LYS A 24 ? 0.6412 0.6608 0.6733 -0.0818 0.0247  -0.1460 24 LYS A C   
167 O O   . LYS A 24 ? 0.6187 0.5891 0.6689 -0.0823 0.0431  -0.1438 24 LYS A O   
168 C CB  . LYS A 24 ? 0.7366 0.8388 0.7645 -0.1209 0.0218  -0.2118 24 LYS A CB  
169 C CG  . LYS A 24 ? 0.8216 0.9631 0.8626 -0.1471 0.0197  -0.2408 24 LYS A CG  
170 C CD  . LYS A 24 ? 0.9114 1.1097 0.9458 -0.1720 0.0221  -0.2900 24 LYS A CD  
171 C CE  . LYS A 24 ? 0.9403 1.1767 0.9948 -0.2012 0.0216  -0.3180 24 LYS A CE  
172 N NZ  . LYS A 24 ? 0.9981 1.3125 1.0448 -0.2264 0.0185  -0.3667 24 LYS A NZ  
173 N N   . LYS A 25 ? 0.6098 0.6487 0.6216 -0.0642 0.0130  -0.1271 25 LYS A N   
174 C CA  . LYS A 25 ? 0.5682 0.5751 0.5804 -0.0485 0.0200  -0.1068 25 LYS A CA  
175 C C   . LYS A 25 ? 0.5288 0.5056 0.5557 -0.0395 0.0184  -0.0783 25 LYS A C   
176 O O   . LYS A 25 ? 0.5447 0.4914 0.5834 -0.0313 0.0298  -0.0667 25 LYS A O   
177 C CB  . LYS A 25 ? 0.5850 0.6200 0.5744 -0.0354 0.0108  -0.0937 25 LYS A CB  
178 C CG  . LYS A 25 ? 0.5887 0.5999 0.5807 -0.0232 0.0201  -0.0784 25 LYS A CG  
179 C CD  . LYS A 25 ? 0.6119 0.6045 0.6121 -0.0272 0.0404  -0.1017 25 LYS A CD  
180 C CE  . LYS A 25 ? 0.6060 0.5879 0.6088 -0.0128 0.0489  -0.0859 25 LYS A CE  
181 N NZ  . LYS A 25 ? 0.6553 0.6156 0.6690 -0.0134 0.0716  -0.1083 25 LYS A NZ  
182 N N   . LEU A 26 ? 0.5196 0.5108 0.5453 -0.0394 0.0047  -0.0666 26 LEU A N   
183 C CA  A LEU A 26 ? 0.5030 0.4744 0.5403 -0.0335 0.0033  -0.0445 26 LEU A CA  
184 C CA  B LEU A 26 ? 0.5053 0.4766 0.5426 -0.0335 0.0033  -0.0444 26 LEU A CA  
185 C C   . LEU A 26 ? 0.5336 0.4738 0.5917 -0.0404 0.0204  -0.0486 26 LEU A C   
186 O O   . LEU A 26 ? 0.5632 0.4811 0.6314 -0.0302 0.0285  -0.0299 26 LEU A O   
187 C CB  A LEU A 26 ? 0.4928 0.4881 0.5254 -0.0338 -0.0110 -0.0390 26 LEU A CB  
188 C CB  B LEU A 26 ? 0.4963 0.4888 0.5302 -0.0334 -0.0105 -0.0372 26 LEU A CB  
189 C CG  A LEU A 26 ? 0.4590 0.4463 0.4942 -0.0250 -0.0167 -0.0167 26 LEU A CG  
190 C CG  B LEU A 26 ? 0.4748 0.4810 0.4946 -0.0208 -0.0225 -0.0209 26 LEU A CG  
191 C CD1 A LEU A 26 ? 0.4612 0.4475 0.4862 -0.0142 -0.0211 -0.0030 26 LEU A CD1 
192 C CD1 B LEU A 26 ? 0.4753 0.4974 0.4961 -0.0193 -0.0313 -0.0162 26 LEU A CD1 
193 C CD2 A LEU A 26 ? 0.4647 0.4725 0.4998 -0.0267 -0.0255 -0.0170 26 LEU A CD2 
194 C CD2 B LEU A 26 ? 0.4761 0.4629 0.4979 -0.0129 -0.0202 -0.0036 26 LEU A CD2 
195 N N   . GLN A 27 ? 0.5491 0.4911 0.6150 -0.0581 0.0277  -0.0727 27 GLN A N   
196 C CA  . GLN A 27 ? 0.5893 0.4951 0.6777 -0.0678 0.0493  -0.0780 27 GLN A CA  
197 C C   . GLN A 27 ? 0.5861 0.4542 0.6834 -0.0588 0.0700  -0.0769 27 GLN A C   
198 O O   . GLN A 27 ? 0.6047 0.4414 0.7175 -0.0476 0.0839  -0.0541 27 GLN A O   
199 C CB  . GLN A 27 ? 0.6018 0.5206 0.6982 -0.0942 0.0554  -0.1121 27 GLN A CB  
200 C CG  . GLN A 27 ? 0.6051 0.5589 0.7018 -0.1015 0.0403  -0.1087 27 GLN A CG  
201 C CD  . GLN A 27 ? 0.6720 0.6638 0.7735 -0.1270 0.0393  -0.1447 27 GLN A CD  
202 O OE1 . GLN A 27 ? 0.7333 0.7378 0.8311 -0.1399 0.0446  -0.1760 27 GLN A OE1 
203 N NE2 . GLN A 27 ? 0.6982 0.7170 0.8081 -0.1352 0.0322  -0.1424 27 GLN A NE2 
204 N N   . THR A 28 ? 0.6240 0.4992 0.7117 -0.0612 0.0732  -0.0997 28 THR A N   
205 C CA  . THR A 28 ? 0.6552 0.4947 0.7536 -0.0524 0.0964  -0.1031 28 THR A CA  
206 C C   . THR A 28 ? 0.6178 0.4547 0.7166 -0.0259 0.0922  -0.0663 28 THR A C   
207 O O   . THR A 28 ? 0.6256 0.4304 0.7427 -0.0120 0.1123  -0.0521 28 THR A O   
208 C CB  . THR A 28 ? 0.7399 0.5953 0.8255 -0.0622 0.1010  -0.1394 28 THR A CB  
209 O OG1 . THR A 28 ? 0.7773 0.6788 0.8373 -0.0543 0.0768  -0.1305 28 THR A OG1 
210 C CG2 . THR A 28 ? 0.7748 0.6379 0.8645 -0.0919 0.1087  -0.1816 28 THR A CG2 
211 N N   . ASP A 29 ? 0.5788 0.4513 0.6600 -0.0191 0.0682  -0.0507 29 ASP A N   
212 C CA  . ASP A 29 ? 0.5448 0.4250 0.6279 -0.0001 0.0623  -0.0201 29 ASP A CA  
213 C C   . ASP A 29 ? 0.5231 0.3903 0.6226 0.0083  0.0670  0.0057  29 ASP A C   
214 O O   . ASP A 29 ? 0.5328 0.3969 0.6448 0.0261  0.0755  0.0280  29 ASP A O   
215 C CB  . ASP A 29 ? 0.5409 0.4551 0.6056 0.0000  0.0392  -0.0114 29 ASP A CB  
216 C CG  . ASP A 29 ? 0.5333 0.4662 0.5820 0.0010  0.0354  -0.0198 29 ASP A CG  
217 O OD1 . ASP A 29 ? 0.5317 0.4574 0.5813 0.0017  0.0492  -0.0353 29 ASP A OD1 
218 O OD2 . ASP A 29 ? 0.5205 0.4740 0.5566 0.0015  0.0210  -0.0100 29 ASP A OD2 
219 N N   . ILE A 30 ? 0.5362 0.4043 0.6354 -0.0028 0.0610  0.0053  30 ILE A N   
220 C CA  . ILE A 30 ? 0.5618 0.4231 0.6736 0.0047  0.0661  0.0314  30 ILE A CA  
221 C C   . ILE A 30 ? 0.6238 0.4425 0.7583 0.0115  0.0962  0.0376  30 ILE A C   
222 O O   . ILE A 30 ? 0.6454 0.4606 0.7920 0.0326  0.1060  0.0682  30 ILE A O   
223 C CB  . ILE A 30 ? 0.5754 0.4493 0.6817 -0.0094 0.0551  0.0274  30 ILE A CB  
224 C CG1 . ILE A 30 ? 0.5394 0.4497 0.6271 -0.0090 0.0300  0.0293  30 ILE A CG1 
225 C CG2 . ILE A 30 ? 0.6013 0.4638 0.7216 -0.0041 0.0671  0.0521  30 ILE A CG2 
226 C CD1 . ILE A 30 ? 0.5228 0.4482 0.6044 -0.0216 0.0196  0.0191  30 ILE A CD1 
227 N N   . LYS A 31 ? 0.6603 0.4487 0.8018 -0.0056 0.1126  0.0081  31 LYS A N   
228 C CA  . LYS A 31 ? 0.7452 0.4816 0.9118 -0.0037 0.1469  0.0099  31 LYS A CA  
229 C C   . LYS A 31 ? 0.7528 0.4700 0.9299 0.0204  0.1646  0.0209  31 LYS A C   
230 O O   . LYS A 31 ? 0.8068 0.4954 1.0045 0.0409  0.1875  0.0503  31 LYS A O   
231 C CB  . LYS A 31 ? 0.8320 0.5457 1.0044 -0.0342 0.1607  -0.0336 31 LYS A CB  
232 C CG  . LYS A 31 ? 0.9657 0.6184 1.1678 -0.0412 0.1998  -0.0352 31 LYS A CG  
233 C CD  . LYS A 31 ? 1.0252 0.6676 1.2346 -0.0798 0.2104  -0.0824 31 LYS A CD  
234 C CE  . LYS A 31 ? 1.0972 0.6875 1.3364 -0.0934 0.2443  -0.0778 31 LYS A CE  
235 N NZ  . LYS A 31 ? 1.1819 0.7017 1.4464 -0.0823 0.2871  -0.0756 31 LYS A NZ  
236 N N   . GLU A 32 ? 0.7363 0.4731 0.8999 0.0207  0.1549  0.0009  32 GLU A N   
237 C CA  . GLU A 32 ? 0.7638 0.4896 0.9376 0.0435  0.1714  0.0086  32 GLU A CA  
238 C C   . GLU A 32 ? 0.7337 0.4884 0.9136 0.0732  0.1634  0.0543  32 GLU A C   
239 O O   . GLU A 32 ? 0.7692 0.5172 0.9644 0.0973  0.1805  0.0691  32 GLU A O   
240 C CB  . GLU A 32 ? 0.7987 0.5498 0.9533 0.0357  0.1603  -0.0210 32 GLU A CB  
241 C CG  . GLU A 32 ? 0.8860 0.6190 1.0352 0.0094  0.1716  -0.0694 32 GLU A CG  
242 C CD  . GLU A 32 ? 0.9223 0.6954 1.0460 0.0021  0.1558  -0.0938 32 GLU A CD  
243 O OE1 . GLU A 32 ? 0.9318 0.7385 1.0446 0.0163  0.1381  -0.0714 32 GLU A OE1 
244 O OE2 . GLU A 32 ? 0.9818 0.7565 1.0967 -0.0183 0.1623  -0.1348 32 GLU A OE2 
245 N N   . ASN A 33 ? 0.7053 0.4981 0.8744 0.0719  0.1386  0.0749  33 ASN A N   
246 C CA  . ASN A 33 ? 0.6659 0.5014 0.8386 0.0951  0.1279  0.1117  33 ASN A CA  
247 C C   . ASN A 33 ? 0.6817 0.5235 0.8609 0.1036  0.1292  0.1443  33 ASN A C   
248 O O   . ASN A 33 ? 0.6214 0.5146 0.7930 0.1098  0.1091  0.1642  33 ASN A O   
249 C CB  . ASN A 33 ? 0.6178 0.5043 0.7701 0.0851  0.0972  0.1040  33 ASN A CB  
250 C CG  . ASN A 33 ? 0.6282 0.5162 0.7748 0.0820  0.0982  0.0814  33 ASN A CG  
251 O OD1 . ASN A 33 ? 0.6491 0.5509 0.8079 0.1008  0.1070  0.0934  33 ASN A OD1 
252 N ND2 . ASN A 33 ? 0.6228 0.5022 0.7515 0.0606  0.0906  0.0508  33 ASN A ND2 
253 N N   . GLY A 34 ? 0.7401 0.5314 0.9335 0.1018  0.1545  0.1477  34 GLY A N   
254 C CA  . GLY A 34 ? 0.7326 0.5235 0.9368 0.1169  0.1654  0.1872  34 GLY A CA  
255 C C   . GLY A 34 ? 0.7060 0.5131 0.8955 0.0955  0.1488  0.1836  34 GLY A C   
256 O O   . GLY A 34 ? 0.7206 0.5401 0.9139 0.1068  0.1539  0.2171  34 GLY A O   
257 N N   . GLY A 35 ? 0.6925 0.5044 0.8653 0.0672  0.1299  0.1454  35 GLY A N   
258 C CA  . GLY A 35 ? 0.6910 0.5256 0.8503 0.0499  0.1127  0.1414  35 GLY A CA  
259 C C   . GLY A 35 ? 0.7116 0.5045 0.8825 0.0300  0.1320  0.1282  35 GLY A C   
260 O O   . GLY A 35 ? 0.7499 0.4962 0.9356 0.0219  0.1549  0.1094  35 GLY A O   
261 N N   . LYS A 36 ? 0.7261 0.5388 0.8911 0.0198  0.1238  0.1346  36 LYS A N   
262 C CA  . LYS A 36 ? 0.8056 0.5887 0.9832 -0.0025 0.1410  0.1218  36 LYS A CA  
263 C C   . LYS A 36 ? 0.7534 0.5706 0.9161 -0.0252 0.1165  0.0926  36 LYS A C   
264 O O   . LYS A 36 ? 0.6684 0.5254 0.8113 -0.0199 0.0897  0.0895  36 LYS A O   
265 C CB  . LYS A 36 ? 0.8812 0.6584 1.0698 0.0090  0.1599  0.1633  36 LYS A CB  
266 C CG  . LYS A 36 ? 0.9538 0.6990 1.1602 0.0374  0.1882  0.2015  36 LYS A CG  
267 C CD  . LYS A 36 ? 1.0262 0.6981 1.2589 0.0281  0.2245  0.1848  36 LYS A CD  
268 C CE  . LYS A 36 ? 1.1204 0.7526 1.3758 0.0567  0.2612  0.2318  36 LYS A CE  
269 N NZ  . LYS A 36 ? 1.2125 0.7669 1.4949 0.0481  0.2998  0.2110  36 LYS A NZ  
270 N N   . PHE A 37 ? 0.8406 0.6428 1.0159 -0.0501 0.1285  0.0727  37 PHE A N   
271 C CA  . PHE A 37 ? 0.8412 0.6800 1.0073 -0.0700 0.1084  0.0456  37 PHE A CA  
272 C C   . PHE A 37 ? 0.8868 0.7348 1.0635 -0.0825 0.1174  0.0552  37 PHE A C   
273 O O   . PHE A 37 ? 0.9014 0.7132 1.0991 -0.0888 0.1465  0.0682  37 PHE A O   
274 C CB  . PHE A 37 ? 0.8201 0.6525 0.9926 -0.0946 0.1112  0.0021  37 PHE A CB  
275 C CG  . PHE A 37 ? 0.8801 0.7093 1.0402 -0.0851 0.1027  -0.0116 37 PHE A CG  
276 C CD1 . PHE A 37 ? 0.7813 0.6489 0.9182 -0.0740 0.0743  -0.0124 37 PHE A CD1 
277 C CD2 . PHE A 37 ? 0.9205 0.7056 1.0937 -0.0861 0.1266  -0.0218 37 PHE A CD2 
278 C CE1 . PHE A 37 ? 0.8358 0.7020 0.9618 -0.0659 0.0689  -0.0221 37 PHE A CE1 
279 C CE2 . PHE A 37 ? 0.9336 0.7205 1.0950 -0.0768 0.1200  -0.0341 37 PHE A CE2 
280 C CZ  . PHE A 37 ? 0.8778 0.7072 1.0152 -0.0671 0.0906  -0.0329 37 PHE A CZ  
281 N N   A SER A 38 ? 0.8695 0.7645 1.0327 -0.0855 0.0946  0.0489  38 SER A N   
282 N N   B SER A 38 ? 0.8695 0.7645 1.0327 -0.0855 0.0946  0.0489  38 SER A N   
283 C CA  A SER A 38 ? 0.8775 0.7926 1.0505 -0.1004 0.1000  0.0495  38 SER A CA  
284 C CA  B SER A 38 ? 0.8775 0.7926 1.0505 -0.1004 0.1000  0.0495  38 SER A CA  
285 C C   A SER A 38 ? 0.8411 0.7979 1.0104 -0.1151 0.0803  0.0163  38 SER A C   
286 C C   B SER A 38 ? 0.8411 0.7979 1.0104 -0.1151 0.0803  0.0163  38 SER A C   
287 O O   A SER A 38 ? 0.7909 0.7761 0.9405 -0.1016 0.0564  0.0126  38 SER A O   
288 O O   B SER A 38 ? 0.7909 0.7761 0.9405 -0.1016 0.0564  0.0126  38 SER A O   
289 C CB  A SER A 38 ? 0.8738 0.8132 1.0350 -0.0827 0.0955  0.0828  38 SER A CB  
290 C CB  B SER A 38 ? 0.8738 0.8132 1.0350 -0.0827 0.0955  0.0828  38 SER A CB  
291 O OG  A SER A 38 ? 0.8529 0.8109 1.0250 -0.0970 0.1049  0.0856  38 SER A OG  
292 O OG  B SER A 38 ? 0.8529 0.8109 1.0250 -0.0970 0.1049  0.0856  38 SER A OG  
293 N N   . GLN A 39 ? 0.8759 0.8375 1.0663 -0.1425 0.0925  -0.0070 39 GLN A N   
294 C CA  . GLN A 39 ? 0.8278 0.8399 1.0189 -0.1565 0.0754  -0.0380 39 GLN A CA  
295 C C   . GLN A 39 ? 0.7163 0.7752 0.8941 -0.1408 0.0555  -0.0260 39 GLN A C   
296 O O   . GLN A 39 ? 0.6311 0.7193 0.7927 -0.1271 0.0335  -0.0335 39 GLN A O   
297 C CB  . GLN A 39 ? 0.8713 0.8881 1.0921 -0.1919 0.0953  -0.0631 39 GLN A CB  
298 C CG  . GLN A 39 ? 0.9104 0.9983 1.1372 -0.2056 0.0789  -0.0878 39 GLN A CG  
299 C CD  . GLN A 39 ? 1.0806 1.1834 1.3362 -0.2457 0.0948  -0.1257 39 GLN A CD  
300 O OE1 . GLN A 39 ? 1.1241 1.2069 1.4060 -0.2700 0.1212  -0.1259 39 GLN A OE1 
301 N NE2 . GLN A 39 ? 1.1381 1.2801 1.3890 -0.2546 0.0800  -0.1591 39 GLN A NE2 
302 N N   . SER A 40 ? 0.7465 0.8109 0.9324 -0.1425 0.0667  -0.0072 40 SER A N   
303 C CA  . SER A 40 ? 0.7234 0.8293 0.8981 -0.1280 0.0529  0.0026  40 SER A CA  
304 C C   . SER A 40 ? 0.7120 0.8011 0.8679 -0.1058 0.0530  0.0329  40 SER A C   
305 O O   . SER A 40 ? 0.7049 0.7568 0.8615 -0.1024 0.0666  0.0518  40 SER A O   
306 C CB  . SER A 40 ? 0.7734 0.9129 0.9691 -0.1463 0.0639  -0.0016 40 SER A CB  
307 O OG  . SER A 40 ? 0.7180 0.9004 0.9275 -0.1615 0.0551  -0.0317 40 SER A OG  
308 N N   . LEU A 41 ? 0.6494 0.7704 0.7893 -0.0900 0.0385  0.0359  41 LEU A N   
309 C CA  . LEU A 41 ? 0.5712 0.6922 0.6919 -0.0721 0.0363  0.0573  41 LEU A CA  
310 C C   . LEU A 41 ? 0.5452 0.6717 0.6728 -0.0765 0.0557  0.0815  41 LEU A C   
311 O O   . LEU A 41 ? 0.5538 0.7042 0.6943 -0.0880 0.0641  0.0783  41 LEU A O   
312 C CB  . LEU A 41 ? 0.5318 0.6839 0.6375 -0.0588 0.0200  0.0459  41 LEU A CB  
313 C CG  . LEU A 41 ? 0.5145 0.6786 0.5997 -0.0447 0.0169  0.0576  41 LEU A CG  
314 C CD1 . LEU A 41 ? 0.5002 0.6398 0.5740 -0.0369 0.0107  0.0641  41 LEU A CD1 
315 C CD2 . LEU A 41 ? 0.4876 0.6784 0.5640 -0.0355 0.0081  0.0408  41 LEU A CD2 
316 N N   . ASN A 42 ? 0.5404 0.6493 0.6603 -0.0660 0.0640  0.1086  42 ASN A N   
317 C CA  . ASN A 42 ? 0.5849 0.7032 0.7078 -0.0649 0.0835  0.1394  42 ASN A CA  
318 C C   . ASN A 42 ? 0.5914 0.7225 0.6930 -0.0429 0.0795  0.1661  42 ASN A C   
319 O O   . ASN A 42 ? 0.5472 0.6732 0.6375 -0.0331 0.0640  0.1578  42 ASN A O   
320 C CB  . ASN A 42 ? 0.6369 0.7156 0.7872 -0.0815 0.1109  0.1501  42 ASN A CB  
321 C CG  . ASN A 42 ? 0.6664 0.6939 0.8236 -0.0770 0.1190  0.1564  42 ASN A CG  
322 O OD1 . ASN A 42 ? 0.6496 0.6742 0.7927 -0.0554 0.1147  0.1778  42 ASN A OD1 
323 N ND2 . ASN A 42 ? 0.6967 0.6882 0.8772 -0.0981 0.1320  0.1358  42 ASN A ND2 
324 N N   . PRO A 43 ? 0.6108 0.7661 0.7069 -0.0348 0.0935  0.1992  43 PRO A N   
325 C CA  . PRO A 43 ? 0.6306 0.8175 0.7052 -0.0134 0.0876  0.2242  43 PRO A CA  
326 C C   . PRO A 43 ? 0.6705 0.8276 0.7495 0.0004  0.0906  0.2437  43 PRO A C   
327 O O   . PRO A 43 ? 0.7213 0.9130 0.7833 0.0168  0.0786  0.2545  43 PRO A O   
328 C CB  . PRO A 43 ? 0.6692 0.8885 0.7402 -0.0085 0.1069  0.2601  43 PRO A CB  
329 C CG  . PRO A 43 ? 0.6838 0.9001 0.7699 -0.0297 0.1159  0.2415  43 PRO A CG  
330 C CD  . PRO A 43 ? 0.6567 0.8200 0.7663 -0.0463 0.1155  0.2144  43 PRO A CD  
331 N N   . GLN A 44 ? 0.7165 0.8146 0.8195 -0.0065 0.1078  0.2467  44 GLN A N   
332 C CA  . GLN A 44 ? 0.7215 0.7880 0.8319 0.0090  0.1150  0.2656  44 GLN A CA  
333 C C   . GLN A 44 ? 0.6388 0.7005 0.7419 0.0091  0.0913  0.2337  44 GLN A C   
334 O O   . GLN A 44 ? 0.6126 0.6647 0.7175 0.0249  0.0920  0.2475  44 GLN A O   
335 C CB  . GLN A 44 ? 0.7905 0.7898 0.9304 0.0012  0.1467  0.2765  44 GLN A CB  
336 C CG  . GLN A 44 ? 0.8748 0.8658 1.0262 0.0093  0.1790  0.3239  44 GLN A CG  
337 C CD  . GLN A 44 ? 0.9038 0.9227 1.0539 -0.0079 0.1838  0.3214  44 GLN A CD  
338 O OE1 . GLN A 44 ? 0.9270 0.9328 1.0894 -0.0354 0.1828  0.2856  44 GLN A OE1 
339 N NE2 . GLN A 44 ? 0.9345 1.0010 1.0693 0.0087  0.1886  0.3599  44 GLN A NE2 
340 N N   . CYS A 45 ? 0.5731 0.6416 0.6697 -0.0066 0.0729  0.1942  45 CYS A N   
341 C CA  . CYS A 45 ? 0.5081 0.5722 0.5972 -0.0068 0.0527  0.1667  45 CYS A CA  
342 C C   . CYS A 45 ? 0.5065 0.6137 0.5765 0.0078  0.0367  0.1738  45 CYS A C   
343 O O   . CYS A 45 ? 0.5013 0.6533 0.5569 0.0100  0.0306  0.1769  45 CYS A O   
344 C CB  . CYS A 45 ? 0.4534 0.5194 0.5404 -0.0224 0.0396  0.1303  45 CYS A CB  
345 S SG  . CYS A 45 ? 0.3805 0.4143 0.4914 -0.0445 0.0542  0.1129  45 CYS A SG  
346 N N   . THR A 46 ? 0.4907 0.5883 0.5614 0.0158  0.0307  0.1728  46 THR A N   
347 C CA  . THR A 46 ? 0.5000 0.6409 0.5568 0.0241  0.0147  0.1717  46 THR A CA  
348 C C   . THR A 46 ? 0.4988 0.6348 0.5476 0.0118  -0.0018 0.1346  46 THR A C   
349 O O   . THR A 46 ? 0.4915 0.6630 0.5279 0.0100  -0.0140 0.1224  46 THR A O   
350 C CB  . THR A 46 ? 0.4925 0.6320 0.5583 0.0410  0.0201  0.1950  46 THR A CB  
351 O OG1 . THR A 46 ? 0.4891 0.5748 0.5673 0.0359  0.0253  0.1802  46 THR A OG1 
352 C CG2 . THR A 46 ? 0.5402 0.6860 0.6146 0.0594  0.0398  0.2393  46 THR A CG2 
353 N N   . HIS A 47 ? 0.5002 0.5936 0.5567 0.0028  -0.0002 0.1168  47 HIS A N   
354 C CA  . HIS A 47 ? 0.4905 0.5736 0.5414 -0.0041 -0.0122 0.0895  47 HIS A CA  
355 C C   . HIS A 47 ? 0.4865 0.5501 0.5417 -0.0134 -0.0111 0.0727  47 HIS A C   
356 O O   . HIS A 47 ? 0.4582 0.5037 0.5252 -0.0183 -0.0005 0.0767  47 HIS A O   
357 C CB  . HIS A 47 ? 0.5039 0.5658 0.5601 -0.0004 -0.0125 0.0890  47 HIS A CB  
358 C CG  . HIS A 47 ? 0.5005 0.5899 0.5551 0.0083  -0.0160 0.1016  47 HIS A CG  
359 N ND1 . HIS A 47 ? 0.4868 0.5921 0.5485 0.0219  -0.0073 0.1301  47 HIS A ND1 
360 C CD2 . HIS A 47 ? 0.4937 0.6017 0.5428 0.0055  -0.0259 0.0900  47 HIS A CD2 
361 C CE1 . HIS A 47 ? 0.5163 0.6579 0.5765 0.0280  -0.0146 0.1350  47 HIS A CE1 
362 N NE2 . HIS A 47 ? 0.4892 0.6320 0.5424 0.0155  -0.0258 0.1084  47 HIS A NE2 
363 N N   . ILE A 48 ? 0.4894 0.5583 0.5368 -0.0157 -0.0206 0.0535  48 ILE A N   
364 C CA  . ILE A 48 ? 0.4797 0.5385 0.5313 -0.0199 -0.0222 0.0391  48 ILE A CA  
365 C C   . ILE A 48 ? 0.4787 0.5254 0.5238 -0.0164 -0.0297 0.0282  48 ILE A C   
366 O O   . ILE A 48 ? 0.4355 0.4859 0.4727 -0.0134 -0.0333 0.0235  48 ILE A O   
367 C CB  . ILE A 48 ? 0.4966 0.5772 0.5487 -0.0210 -0.0217 0.0330  48 ILE A CB  
368 C CG1 . ILE A 48 ? 0.5673 0.6498 0.6269 -0.0232 -0.0239 0.0207  48 ILE A CG1 
369 C CG2 . ILE A 48 ? 0.4770 0.5722 0.5174 -0.0158 -0.0257 0.0255  48 ILE A CG2 
370 C CD1 . ILE A 48 ? 0.5780 0.6878 0.6435 -0.0236 -0.0214 0.0165  48 ILE A CD1 
371 N N   . ILE A 49 ? 0.4599 0.4934 0.5087 -0.0183 -0.0298 0.0234  49 ILE A N   
372 C CA  . ILE A 49 ? 0.4453 0.4696 0.4873 -0.0137 -0.0348 0.0177  49 ILE A CA  
373 C C   . ILE A 49 ? 0.4350 0.4727 0.4763 -0.0093 -0.0387 0.0104  49 ILE A C   
374 O O   . ILE A 49 ? 0.4385 0.4910 0.4867 -0.0144 -0.0387 0.0046  49 ILE A O   
375 C CB  . ILE A 49 ? 0.4374 0.4480 0.4813 -0.0165 -0.0319 0.0171  49 ILE A CB  
376 C CG1 . ILE A 49 ? 0.4560 0.4565 0.5049 -0.0162 -0.0255 0.0283  49 ILE A CG1 
377 C CG2 . ILE A 49 ? 0.4270 0.4334 0.4614 -0.0110 -0.0360 0.0141  49 ILE A CG2 
378 C CD1 . ILE A 49 ? 0.4504 0.4584 0.4941 -0.0116 -0.0292 0.0352  49 ILE A CD1 
379 N N   A LEU A 50 ? 0.4271 0.4604 0.4619 0.0002  -0.0402 0.0109  50 LEU A N   
380 N N   B LEU A 50 ? 0.4227 0.4571 0.4579 0.0001  -0.0400 0.0107  50 LEU A N   
381 C CA  A LEU A 50 ? 0.4310 0.4780 0.4664 0.0115  -0.0415 0.0099  50 LEU A CA  
382 C CA  B LEU A 50 ? 0.4222 0.4689 0.4574 0.0117  -0.0416 0.0100  50 LEU A CA  
383 C C   A LEU A 50 ? 0.4509 0.4869 0.4786 0.0222  -0.0415 0.0163  50 LEU A C   
384 C C   B LEU A 50 ? 0.4405 0.4759 0.4678 0.0205  -0.0419 0.0161  50 LEU A C   
385 O O   A LEU A 50 ? 0.4464 0.4569 0.4697 0.0240  -0.0365 0.0194  50 LEU A O   
386 O O   B LEU A 50 ? 0.4305 0.4412 0.4529 0.0199  -0.0380 0.0192  50 LEU A O   
387 C CB  A LEU A 50 ? 0.4345 0.4798 0.4710 0.0161  -0.0370 0.0071  50 LEU A CB  
388 C CB  B LEU A 50 ? 0.4229 0.4679 0.4591 0.0204  -0.0370 0.0082  50 LEU A CB  
389 C CG  A LEU A 50 ? 0.4410 0.5053 0.4834 0.0299  -0.0352 0.0065  50 LEU A CG  
390 C CG  B LEU A 50 ? 0.4210 0.4828 0.4623 0.0142  -0.0350 0.0029  50 LEU A CG  
391 C CD1 A LEU A 50 ? 0.4357 0.5352 0.4882 0.0232  -0.0384 0.0033  50 LEU A CD1 
392 C CD1 B LEU A 50 ? 0.4653 0.5230 0.5060 0.0238  -0.0281 -0.0032 50 LEU A CD1 
393 C CD2 A LEU A 50 ? 0.4650 0.5158 0.5066 0.0357  -0.0265 0.0002  50 LEU A CD2 
394 C CD2 B LEU A 50 ? 0.4232 0.5153 0.4749 0.0107  -0.0374 0.0023  50 LEU A CD2 
395 N N   . ASP A 51 ? 0.4653 0.5256 0.4917 0.0281  -0.0460 0.0182  51 ASP A N   
396 C CA  . ASP A 51 ? 0.4381 0.4975 0.4558 0.0435  -0.0448 0.0301  51 ASP A CA  
397 C C   . ASP A 51 ? 0.4543 0.5071 0.4754 0.0629  -0.0381 0.0400  51 ASP A C   
398 O O   . ASP A 51 ? 0.3948 0.4515 0.4244 0.0634  -0.0362 0.0336  51 ASP A O   
399 C CB  . ASP A 51 ? 0.4230 0.5217 0.4361 0.0445  -0.0520 0.0286  51 ASP A CB  
400 C CG  . ASP A 51 ? 0.4373 0.5866 0.4589 0.0488  -0.0583 0.0239  51 ASP A CG  
401 O OD1 . ASP A 51 ? 0.4646 0.6158 0.4964 0.0535  -0.0563 0.0242  51 ASP A OD1 
402 O OD2 . ASP A 51 ? 0.4352 0.6274 0.4537 0.0461  -0.0649 0.0177  51 ASP A OD2 
403 N N   . ASN A 52 ? 0.4904 0.5325 0.5052 0.0803  -0.0317 0.0569  52 ASN A N   
404 C CA  . ASN A 52 ? 0.5412 0.5600 0.5605 0.1010  -0.0183 0.0695  52 ASN A CA  
405 C C   . ASN A 52 ? 0.4863 0.5412 0.5153 0.1200  -0.0197 0.0734  52 ASN A C   
406 O O   . ASN A 52 ? 0.4913 0.5252 0.5291 0.1306  -0.0081 0.0726  52 ASN A O   
407 C CB  . ASN A 52 ? 0.6637 0.6672 0.6750 0.1184  -0.0088 0.0935  52 ASN A CB  
408 C CG  . ASN A 52 ? 0.8119 0.7584 0.8229 0.1073  0.0056  0.0926  52 ASN A CG  
409 O OD1 . ASN A 52 ? 0.9471 0.8552 0.9672 0.1082  0.0204  0.0873  52 ASN A OD1 
410 N ND2 . ASN A 52 ? 0.8548 0.7978 0.8569 0.0959  0.0034  0.0953  52 ASN A ND2 
411 N N   . ALA A 53 ? 0.4634 0.5763 0.4919 0.1245  -0.0325 0.0763  53 ALA A N   
412 C CA  . ALA A 53 ? 0.4459 0.6080 0.4856 0.1452  -0.0348 0.0831  53 ALA A CA  
413 C C   . ALA A 53 ? 0.4340 0.6196 0.4864 0.1278  -0.0406 0.0615  53 ALA A C   
414 O O   . ALA A 53 ? 0.4790 0.7027 0.5444 0.1432  -0.0401 0.0644  53 ALA A O   
415 C CB  . ALA A 53 ? 0.4682 0.6941 0.5018 0.1570  -0.0457 0.0954  53 ALA A CB  
416 N N   . ASP A 54 ? 0.3971 0.5611 0.4471 0.0983  -0.0439 0.0429  54 ASP A N   
417 C CA  . ASP A 54 ? 0.4043 0.5857 0.4655 0.0816  -0.0460 0.0270  54 ASP A CA  
418 C C   . ASP A 54 ? 0.4407 0.5892 0.5047 0.0852  -0.0349 0.0233  54 ASP A C   
419 O O   . ASP A 54 ? 0.4171 0.5187 0.4727 0.0832  -0.0278 0.0229  54 ASP A O   
420 C CB  . ASP A 54 ? 0.4256 0.5976 0.4841 0.0523  -0.0506 0.0136  54 ASP A CB  
421 C CG  . ASP A 54 ? 0.4691 0.6876 0.5342 0.0383  -0.0587 0.0034  54 ASP A CG  
422 O OD1 . ASP A 54 ? 0.4576 0.6912 0.5143 0.0410  -0.0640 0.0049  54 ASP A OD1 
423 O OD2 . ASP A 54 ? 0.5175 0.7604 0.5967 0.0241  -0.0580 -0.0071 54 ASP A OD2 
424 N N   . VAL A 55 ? 0.4713 0.6500 0.5476 0.0869  -0.0330 0.0173  55 VAL A N   
425 C CA  . VAL A 55 ? 0.5058 0.6635 0.5836 0.0890  -0.0218 0.0095  55 VAL A CA  
426 C C   . VAL A 55 ? 0.4952 0.6747 0.5773 0.0671  -0.0240 -0.0012 55 VAL A C   
427 O O   . VAL A 55 ? 0.4775 0.6882 0.5670 0.0532  -0.0312 -0.0022 55 VAL A O   
428 C CB  . VAL A 55 ? 0.5361 0.7060 0.6249 0.1184  -0.0112 0.0150  55 VAL A CB  
429 C CG1 . VAL A 55 ? 0.5851 0.7265 0.6707 0.1436  -0.0039 0.0318  55 VAL A CG1 
430 C CG2 . VAL A 55 ? 0.5417 0.7793 0.6473 0.1255  -0.0171 0.0174  55 VAL A CG2 
431 N N   . LEU A 56 ? 0.4768 0.6392 0.5539 0.0627  -0.0157 -0.0097 56 LEU A N   
432 C CA  . LEU A 56 ? 0.4681 0.6529 0.5474 0.0461  -0.0144 -0.0149 56 LEU A CA  
433 C C   . LEU A 56 ? 0.4965 0.7042 0.5828 0.0586  -0.0041 -0.0220 56 LEU A C   
434 O O   . LEU A 56 ? 0.5615 0.7483 0.6455 0.0754  0.0049  -0.0280 56 LEU A O   
435 C CB  . LEU A 56 ? 0.4809 0.6397 0.5455 0.0305  -0.0143 -0.0171 56 LEU A CB  
436 C CG  . LEU A 56 ? 0.4640 0.6018 0.5237 0.0194  -0.0222 -0.0096 56 LEU A CG  
437 C CD1 . LEU A 56 ? 0.5086 0.6285 0.5558 0.0101  -0.0214 -0.0105 56 LEU A CD1 
438 C CD2 . LEU A 56 ? 0.4324 0.5893 0.5025 0.0061  -0.0251 -0.0043 56 LEU A CD2 
439 N N   . SER A 57 ? 0.4500 0.6989 0.5469 0.0497  -0.0029 -0.0219 57 SER A N   
440 C CA  . SER A 57 ? 0.4272 0.7058 0.5311 0.0591  0.0079  -0.0289 57 SER A CA  
441 C C   . SER A 57 ? 0.4283 0.6939 0.5150 0.0514  0.0159  -0.0386 57 SER A C   
442 O O   . SER A 57 ? 0.4190 0.6647 0.4913 0.0363  0.0114  -0.0362 57 SER A O   
443 C CB  . SER A 57 ? 0.3988 0.7306 0.5214 0.0488  0.0080  -0.0250 57 SER A CB  
444 O OG  . SER A 57 ? 0.3712 0.7009 0.4882 0.0239  0.0090  -0.0203 57 SER A OG  
445 N N   . GLN A 58 ? 0.4348 0.7211 0.5238 0.0623  0.0283  -0.0499 58 GLN A N   
446 C CA  . GLN A 58 ? 0.4743 0.7639 0.5457 0.0541  0.0365  -0.0628 58 GLN A CA  
447 C C   . GLN A 58 ? 0.4474 0.7632 0.5131 0.0332  0.0324  -0.0485 58 GLN A C   
448 O O   . GLN A 58 ? 0.4782 0.7887 0.5254 0.0222  0.0307  -0.0482 58 GLN A O   
449 C CB  . GLN A 58 ? 0.5256 0.8378 0.6021 0.0701  0.0528  -0.0794 58 GLN A CB  
450 C CG  . GLN A 58 ? 0.5857 0.8979 0.6408 0.0631  0.0629  -0.1019 58 GLN A CG  
451 C CD  . GLN A 58 ? 0.6271 0.8911 0.6691 0.0578  0.0613  -0.1159 58 GLN A CD  
452 O OE1 . GLN A 58 ? 0.6867 0.9099 0.7364 0.0720  0.0697  -0.1262 58 GLN A OE1 
453 N NE2 . GLN A 58 ? 0.6443 0.9138 0.6686 0.0379  0.0517  -0.1131 58 GLN A NE2 
454 N N   . TYR A 59 ? 0.4163 0.7620 0.5000 0.0277  0.0323  -0.0354 59 TYR A N   
455 C CA  . TYR A 59 ? 0.4089 0.7711 0.4918 0.0083  0.0339  -0.0184 59 TYR A CA  
456 C C   . TYR A 59 ? 0.3710 0.6956 0.4438 -0.0018 0.0248  -0.0072 59 TYR A C   
457 O O   . TYR A 59 ? 0.3683 0.6950 0.4278 -0.0098 0.0273  0.0046  59 TYR A O   
458 C CB  . TYR A 59 ? 0.4142 0.8087 0.5235 -0.0002 0.0377  -0.0104 59 TYR A CB  
459 C CG  . TYR A 59 ? 0.4414 0.8393 0.5540 -0.0221 0.0445  0.0090  59 TYR A CG  
460 C CD1 . TYR A 59 ? 0.4841 0.9104 0.5892 -0.0269 0.0579  0.0198  59 TYR A CD1 
461 C CD2 . TYR A 59 ? 0.4451 0.8150 0.5673 -0.0367 0.0404  0.0177  59 TYR A CD2 
462 C CE1 . TYR A 59 ? 0.5216 0.9459 0.6308 -0.0438 0.0684  0.0437  59 TYR A CE1 
463 C CE2 . TYR A 59 ? 0.4822 0.8449 0.6102 -0.0548 0.0519  0.0369  59 TYR A CE2 
464 C CZ  . TYR A 59 ? 0.5536 0.9418 0.6758 -0.0574 0.0667  0.0525  59 TYR A CZ  
465 O OH  . TYR A 59 ? 0.6346 1.0120 0.7635 -0.0722 0.0823  0.0773  59 TYR A OH  
466 N N   . GLN A 60 ? 0.3772 0.6722 0.4566 0.0004  0.0150  -0.0090 60 GLN A N   
467 C CA  . GLN A 60 ? 0.3819 0.6426 0.4535 -0.0077 0.0078  0.0002  60 GLN A CA  
468 C C   . GLN A 60 ? 0.4121 0.6586 0.4620 -0.0044 0.0056  -0.0041 60 GLN A C   
469 O O   . GLN A 60 ? 0.4306 0.6710 0.4723 -0.0115 0.0041  0.0088  60 GLN A O   
470 C CB  . GLN A 60 ? 0.3662 0.6045 0.4465 -0.0047 -0.0013 -0.0031 60 GLN A CB  
471 C CG  . GLN A 60 ? 0.3799 0.6400 0.4818 -0.0151 -0.0005 -0.0011 60 GLN A CG  
472 C CD  . GLN A 60 ? 0.3692 0.6260 0.4782 -0.0101 -0.0103 -0.0071 60 GLN A CD  
473 O OE1 . GLN A 60 ? 0.3848 0.6449 0.4919 0.0089  -0.0144 -0.0115 60 GLN A OE1 
474 N NE2 . GLN A 60 ? 0.3577 0.6095 0.4754 -0.0268 -0.0118 -0.0069 60 GLN A NE2 
475 N N   . LEU A 61 ? 0.4555 0.6974 0.4988 0.0061  0.0070  -0.0231 61 LEU A N   
476 C CA  . LEU A 61 ? 0.4853 0.7176 0.5110 0.0046  0.0066  -0.0356 61 LEU A CA  
477 C C   . LEU A 61 ? 0.4702 0.7430 0.4812 -0.0024 0.0109  -0.0330 61 LEU A C   
478 O O   . LEU A 61 ? 0.4679 0.7474 0.4660 -0.0089 0.0062  -0.0288 61 LEU A O   
479 C CB  . LEU A 61 ? 0.5201 0.7332 0.5471 0.0161  0.0132  -0.0589 61 LEU A CB  
480 C CG  . LEU A 61 ? 0.5254 0.6978 0.5621 0.0255  0.0097  -0.0564 61 LEU A CG  
481 C CD1 . LEU A 61 ? 0.5616 0.7131 0.6035 0.0417  0.0224  -0.0733 61 LEU A CD1 
482 C CD2 . LEU A 61 ? 0.5435 0.6888 0.5722 0.0154  0.0018  -0.0529 61 LEU A CD2 
483 N N   . ASN A 62 ? 0.4734 0.7802 0.4868 -0.0002 0.0199  -0.0322 62 ASN A N   
484 C CA  . ASN A 62 ? 0.5029 0.8557 0.5011 -0.0052 0.0256  -0.0246 62 ASN A CA  
485 C C   . ASN A 62 ? 0.4939 0.8511 0.4911 -0.0115 0.0230  0.0087  62 ASN A C   
486 O O   . ASN A 62 ? 0.4945 0.8804 0.4743 -0.0130 0.0219  0.0180  62 ASN A O   
487 C CB  . ASN A 62 ? 0.5402 0.9277 0.5445 -0.0014 0.0378  -0.0266 62 ASN A CB  
488 C CG  . ASN A 62 ? 0.5750 0.9617 0.5791 0.0086  0.0447  -0.0595 62 ASN A CG  
489 O OD1 . ASN A 62 ? 0.5887 0.9489 0.5852 0.0099  0.0426  -0.0814 62 ASN A OD1 
490 N ND2 . ASN A 62 ? 0.6261 1.0398 0.6407 0.0157  0.0558  -0.0636 62 ASN A ND2 
491 N N   . SER A 63 ? 0.4681 0.8001 0.4851 -0.0148 0.0236  0.0263  63 SER A N   
492 C CA  . SER A 63 ? 0.4596 0.7832 0.4802 -0.0197 0.0264  0.0573  63 SER A CA  
493 C C   . SER A 63 ? 0.4638 0.7699 0.4742 -0.0170 0.0161  0.0604  63 SER A C   
494 O O   . SER A 63 ? 0.4552 0.7777 0.4575 -0.0145 0.0184  0.0845  63 SER A O   
495 C CB  . SER A 63 ? 0.4500 0.7446 0.4954 -0.0276 0.0307  0.0652  63 SER A CB  
496 O OG  . SER A 63 ? 0.4607 0.7807 0.5193 -0.0325 0.0410  0.0634  63 SER A OG  
497 N N   . ILE A 64 ? 0.4586 0.7338 0.4713 -0.0162 0.0063  0.0389  64 ILE A N   
498 C CA  . ILE A 64 ? 0.4758 0.7346 0.4821 -0.0155 -0.0029 0.0379  64 ILE A CA  
499 C C   . ILE A 64 ? 0.4894 0.7917 0.4758 -0.0153 -0.0054 0.0335  64 ILE A C   
500 O O   . ILE A 64 ? 0.5169 0.8342 0.4984 -0.0134 -0.0090 0.0511  64 ILE A O   
501 C CB  . ILE A 64 ? 0.4570 0.6784 0.4689 -0.0147 -0.0095 0.0153  64 ILE A CB  
502 C CG1 . ILE A 64 ? 0.4997 0.6878 0.5281 -0.0156 -0.0105 0.0243  64 ILE A CG1 
503 C CG2 . ILE A 64 ? 0.4630 0.6789 0.4654 -0.0167 -0.0165 0.0048  64 ILE A CG2 
504 C CD1 . ILE A 64 ? 0.5003 0.6666 0.5354 -0.0110 -0.0142 0.0076  64 ILE A CD1 
505 N N   . GLN A 65 ? 0.5301 0.8576 0.5061 -0.0169 -0.0027 0.0084  65 GLN A N   
506 C CA  . GLN A 65 ? 0.5684 0.9457 0.5245 -0.0207 -0.0049 -0.0043 65 GLN A CA  
507 C C   . GLN A 65 ? 0.5506 0.9805 0.4964 -0.0159 -0.0017 0.0291  65 GLN A C   
508 O O   . GLN A 65 ? 0.5287 0.9957 0.4643 -0.0144 -0.0077 0.0413  65 GLN A O   
509 C CB  . GLN A 65 ? 0.6499 1.0421 0.5976 -0.0241 0.0018  -0.0414 65 GLN A CB  
510 C CG  . GLN A 65 ? 0.7480 1.1994 0.6741 -0.0327 0.0004  -0.0630 65 GLN A CG  
511 C CD  . GLN A 65 ? 0.8901 1.3581 0.8073 -0.0366 0.0116  -0.1022 65 GLN A CD  
512 O OE1 . GLN A 65 ? 0.9340 1.4090 0.8529 -0.0291 0.0212  -0.0987 65 GLN A OE1 
513 N NE2 . GLN A 65 ? 0.9842 1.4603 0.8937 -0.0497 0.0125  -0.1423 65 GLN A NE2 
514 N N   . LYS A 66 ? 0.5543 0.9889 0.5049 -0.0124 0.0090  0.0468  66 LYS A N   
515 C CA  . LYS A 66 ? 0.5744 1.0556 0.5159 -0.0064 0.0173  0.0828  66 LYS A CA  
516 C C   . LYS A 66 ? 0.5530 1.0230 0.5012 0.0012  0.0164  0.1217  66 LYS A C   
517 O O   . LYS A 66 ? 0.5526 1.0735 0.4876 0.0103  0.0183  0.1501  66 LYS A O   
518 C CB  . LYS A 66 ? 0.6129 1.0847 0.5670 -0.0074 0.0318  0.0951  66 LYS A CB  
519 C CG  . LYS A 66 ? 0.6629 1.1794 0.6087 -0.0017 0.0455  0.1346  66 LYS A CG  
520 C CD  . LYS A 66 ? 0.7168 1.2236 0.6793 -0.0067 0.0624  0.1459  66 LYS A CD  
521 C CE  . LYS A 66 ? 0.7896 1.3348 0.7450 -0.0008 0.0793  0.1913  66 LYS A CE  
522 N NZ  . LYS A 66 ? 0.8345 1.3786 0.8060 -0.0090 0.0977  0.1991  66 LYS A NZ  
523 N N   . ASN A 67 ? 0.5258 0.9326 0.4945 -0.0003 0.0149  0.1242  67 ASN A N   
524 C CA  . ASN A 67 ? 0.5428 0.9289 0.5225 0.0082  0.0201  0.1613  67 ASN A CA  
525 C C   . ASN A 67 ? 0.5200 0.9012 0.4985 0.0113  0.0065  0.1538  67 ASN A C   
526 O O   . ASN A 67 ? 0.5228 0.8812 0.5130 0.0201  0.0107  0.1802  67 ASN A O   
527 C CB  . ASN A 67 ? 0.5675 0.8923 0.5720 0.0025  0.0322  0.1699  67 ASN A CB  
528 C CG  . ASN A 67 ? 0.5599 0.8980 0.5690 -0.0018 0.0487  0.1834  67 ASN A CG  
529 O OD1 . ASN A 67 ? 0.5805 0.9028 0.6007 -0.0129 0.0506  0.1619  67 ASN A OD1 
530 N ND2 . ASN A 67 ? 0.5912 0.9642 0.5925 0.0079  0.0613  0.2212  67 ASN A ND2 
531 N N   . HIS A 68 ? 0.5298 0.9317 0.4964 0.0036  -0.0066 0.1176  68 HIS A N   
532 C CA  . HIS A 68 ? 0.5443 0.9510 0.5105 0.0024  -0.0187 0.1061  68 HIS A CA  
533 C C   . HIS A 68 ? 0.5137 0.8531 0.4989 0.0023  -0.0193 0.1072  68 HIS A C   
534 O O   . HIS A 68 ? 0.5338 0.8738 0.5245 0.0081  -0.0233 0.1189  68 HIS A O   
535 C CB  . HIS A 68 ? 0.5847 1.0580 0.5418 0.0142  -0.0216 0.1349  68 HIS A CB  
536 C CG  . HIS A 68 ? 0.6531 1.2009 0.5892 0.0165  -0.0196 0.1404  68 HIS A CG  
537 N ND1 . HIS A 68 ? 0.6846 1.2857 0.6025 0.0035  -0.0279 0.1018  68 HIS A ND1 
538 C CD2 . HIS A 68 ? 0.7155 1.2934 0.6456 0.0293  -0.0078 0.1787  68 HIS A CD2 
539 C CE1 . HIS A 68 ? 0.7131 1.3810 0.6123 0.0089  -0.0232 0.1153  68 HIS A CE1 
540 N NE2 . HIS A 68 ? 0.7254 1.3806 0.6313 0.0256  -0.0110 0.1647  68 HIS A NE2 
541 N N   . VAL A 69 ? 0.4836 0.7729 0.4784 -0.0037 -0.0157 0.0926  69 VAL A N   
542 C CA  . VAL A 69 ? 0.4747 0.7081 0.4843 -0.0052 -0.0165 0.0891  69 VAL A CA  
543 C C   . VAL A 69 ? 0.4293 0.6529 0.4354 -0.0113 -0.0268 0.0609  69 VAL A C   
544 O O   . VAL A 69 ? 0.4458 0.6795 0.4440 -0.0175 -0.0291 0.0356  69 VAL A O   
545 C CB  . VAL A 69 ? 0.4879 0.6875 0.5087 -0.0100 -0.0097 0.0838  69 VAL A CB  
546 C CG1 . VAL A 69 ? 0.4761 0.6282 0.5106 -0.0123 -0.0101 0.0799  69 VAL A CG1 
547 C CG2 . VAL A 69 ? 0.5066 0.7187 0.5324 -0.0087 0.0039  0.1084  69 VAL A CG2 
548 N N   . HIS A 70 ? 0.4500 0.6527 0.4634 -0.0094 -0.0300 0.0658  70 HIS A N   
549 C CA  . HIS A 70 ? 0.4586 0.6446 0.4719 -0.0163 -0.0364 0.0430  70 HIS A CA  
550 C C   . HIS A 70 ? 0.4450 0.5824 0.4642 -0.0174 -0.0348 0.0319  70 HIS A C   
551 O O   . HIS A 70 ? 0.4441 0.5570 0.4717 -0.0139 -0.0318 0.0434  70 HIS A O   
552 C CB  . HIS A 70 ? 0.4679 0.6594 0.4873 -0.0128 -0.0393 0.0551  70 HIS A CB  
553 C CG  . HIS A 70 ? 0.4895 0.7411 0.5044 -0.0085 -0.0422 0.0689  70 HIS A CG  
554 N ND1 . HIS A 70 ? 0.4940 0.7950 0.4976 -0.0180 -0.0474 0.0500  70 HIS A ND1 
555 C CD2 . HIS A 70 ? 0.5022 0.7774 0.5230 0.0053  -0.0399 0.0993  70 HIS A CD2 
556 C CE1 . HIS A 70 ? 0.5504 0.9127 0.5513 -0.0105 -0.0508 0.0691  70 HIS A CE1 
557 N NE2 . HIS A 70 ? 0.5401 0.8867 0.5521 0.0060  -0.0459 0.1023  70 HIS A NE2 
558 N N   . ILE A 71 ? 0.4603 0.5870 0.4759 -0.0216 -0.0351 0.0093  71 ILE A N   
559 C CA  . ILE A 71 ? 0.4486 0.5384 0.4688 -0.0184 -0.0337 0.0025  71 ILE A CA  
560 C C   . ILE A 71 ? 0.4526 0.5199 0.4743 -0.0206 -0.0349 -0.0008 71 ILE A C   
561 O O   . ILE A 71 ? 0.4030 0.4745 0.4225 -0.0281 -0.0335 -0.0139 71 ILE A O   
562 C CB  . ILE A 71 ? 0.4881 0.5746 0.5062 -0.0162 -0.0289 -0.0145 71 ILE A CB  
563 C CG1 . ILE A 71 ? 0.4938 0.6103 0.5093 -0.0152 -0.0261 -0.0142 71 ILE A CG1 
564 C CG2 . ILE A 71 ? 0.5045 0.5626 0.5285 -0.0071 -0.0275 -0.0138 71 ILE A CG2 
565 C CD1 . ILE A 71 ? 0.5117 0.6264 0.5271 -0.0103 -0.0190 -0.0319 71 ILE A CD1 
566 N N   . ALA A 72 ? 0.4345 0.4802 0.4603 -0.0162 -0.0360 0.0082  72 ALA A N   
567 C CA  . ALA A 72 ? 0.4434 0.4708 0.4699 -0.0173 -0.0358 0.0084  72 ALA A CA  
568 C C   . ALA A 72 ? 0.4873 0.4928 0.5134 -0.0100 -0.0350 0.0107  72 ALA A C   
569 O O   . ALA A 72 ? 0.5014 0.5120 0.5291 -0.0058 -0.0366 0.0127  72 ALA A O   
570 C CB  . ALA A 72 ? 0.4104 0.4485 0.4409 -0.0182 -0.0375 0.0199  72 ALA A CB  
571 N N   . ASN A 73 ? 0.4964 0.4838 0.5207 -0.0092 -0.0319 0.0109  73 ASN A N   
572 C CA  . ASN A 73 ? 0.4619 0.4382 0.4829 -0.0004 -0.0314 0.0173  73 ASN A CA  
573 C C   . ASN A 73 ? 0.4356 0.4150 0.4561 -0.0027 -0.0335 0.0222  73 ASN A C   
574 O O   . ASN A 73 ? 0.4331 0.4184 0.4582 -0.0085 -0.0337 0.0232  73 ASN A O   
575 C CB  . ASN A 73 ? 0.5084 0.4620 0.5273 0.0047  -0.0230 0.0194  73 ASN A CB  
576 C CG  . ASN A 73 ? 0.5374 0.4787 0.5587 -0.0061 -0.0170 0.0176  73 ASN A CG  
577 O OD1 . ASN A 73 ? 0.5616 0.5134 0.5839 -0.0117 -0.0205 0.0203  73 ASN A OD1 
578 N ND2 . ASN A 73 ? 0.5588 0.4789 0.5839 -0.0105 -0.0060 0.0109  73 ASN A ND2 
579 N N   . PRO A 74 ? 0.4087 0.3897 0.4241 0.0030  -0.0344 0.0250  74 PRO A N   
580 C CA  . PRO A 74 ? 0.3986 0.3816 0.4128 0.0004  -0.0335 0.0248  74 PRO A CA  
581 C C   . PRO A 74 ? 0.3947 0.3694 0.4098 -0.0021 -0.0288 0.0294  74 PRO A C   
582 O O   . PRO A 74 ? 0.4061 0.3832 0.4252 -0.0038 -0.0264 0.0290  74 PRO A O   
583 C CB  . PRO A 74 ? 0.4214 0.4165 0.4261 0.0073  -0.0353 0.0248  74 PRO A CB  
584 C CG  . PRO A 74 ? 0.4248 0.4323 0.4315 0.0125  -0.0394 0.0240  74 PRO A CG  
585 C CD  . PRO A 74 ? 0.4510 0.4399 0.4614 0.0136  -0.0358 0.0277  74 PRO A CD  
586 N N   . ASP A 75 ? 0.4138 0.3784 0.4278 -0.0026 -0.0249 0.0332  75 ASP A N   
587 C CA  . ASP A 75 ? 0.4460 0.4075 0.4643 -0.0091 -0.0192 0.0357  75 ASP A CA  
588 C C   . ASP A 75 ? 0.4076 0.3860 0.4369 -0.0158 -0.0217 0.0327  75 ASP A C   
589 O O   . ASP A 75 ? 0.3947 0.3825 0.4298 -0.0178 -0.0185 0.0358  75 ASP A O   
590 C CB  . ASP A 75 ? 0.5174 0.4609 0.5370 -0.0132 -0.0108 0.0368  75 ASP A CB  
591 C CG  . ASP A 75 ? 0.5636 0.4924 0.5739 -0.0034 -0.0030 0.0498  75 ASP A CG  
592 O OD1 . ASP A 75 ? 0.5695 0.5108 0.5713 0.0030  -0.0052 0.0555  75 ASP A OD1 
593 O OD2 . ASP A 75 ? 0.6914 0.5971 0.7031 -0.0015 0.0070  0.0543  75 ASP A OD2 
594 N N   . PHE A 76 ? 0.3874 0.3753 0.4197 -0.0173 -0.0266 0.0290  76 PHE A N   
595 C CA  . PHE A 76 ? 0.3907 0.4030 0.4318 -0.0188 -0.0290 0.0321  76 PHE A CA  
596 C C   . PHE A 76 ? 0.4048 0.4179 0.4510 -0.0104 -0.0258 0.0409  76 PHE A C   
597 O O   . PHE A 76 ? 0.4048 0.4374 0.4606 -0.0079 -0.0238 0.0479  76 PHE A O   
598 C CB  . PHE A 76 ? 0.3996 0.4229 0.4396 -0.0186 -0.0332 0.0307  76 PHE A CB  
599 C CG  . PHE A 76 ? 0.4006 0.4545 0.4479 -0.0153 -0.0346 0.0410  76 PHE A CG  
600 C CD1 . PHE A 76 ? 0.4215 0.5096 0.4748 -0.0203 -0.0366 0.0407  76 PHE A CD1 
601 C CD2 . PHE A 76 ? 0.4170 0.4696 0.4667 -0.0070 -0.0323 0.0524  76 PHE A CD2 
602 C CE1 . PHE A 76 ? 0.4330 0.5601 0.4926 -0.0127 -0.0384 0.0551  76 PHE A CE1 
603 C CE2 . PHE A 76 ? 0.4339 0.5148 0.4906 0.0007  -0.0307 0.0689  76 PHE A CE2 
604 C CZ  . PHE A 76 ? 0.4424 0.5638 0.5031 0.0001  -0.0347 0.0721  76 PHE A CZ  
605 N N   . ILE A 77 ? 0.4120 0.4074 0.4535 -0.0061 -0.0240 0.0388  77 ILE A N   
606 C CA  . ILE A 77 ? 0.4049 0.3928 0.4517 -0.0003 -0.0167 0.0407  77 ILE A CA  
607 C C   . ILE A 77 ? 0.3897 0.3769 0.4340 0.0010  -0.0121 0.0390  77 ILE A C   
608 O O   . ILE A 77 ? 0.4286 0.4216 0.4826 0.0068  -0.0053 0.0443  77 ILE A O   
609 C CB  . ILE A 77 ? 0.4506 0.4247 0.4942 -0.0024 -0.0150 0.0315  77 ILE A CB  
610 C CG1 . ILE A 77 ? 0.4507 0.4274 0.4981 -0.0049 -0.0175 0.0341  77 ILE A CG1 
611 C CG2 . ILE A 77 ? 0.4422 0.4028 0.4923 -0.0001 -0.0032 0.0263  77 ILE A CG2 
612 C CD1 . ILE A 77 ? 0.4569 0.4381 0.5159 0.0005  -0.0116 0.0491  77 ILE A CD1 
613 N N   . TRP A 78 ? 0.4087 0.3911 0.4404 -0.0017 -0.0140 0.0341  78 TRP A N   
614 C CA  . TRP A 78 ? 0.4385 0.4231 0.4649 -0.0001 -0.0081 0.0346  78 TRP A CA  
615 C C   . TRP A 78 ? 0.4561 0.4535 0.4941 -0.0019 -0.0043 0.0420  78 TRP A C   
616 O O   . TRP A 78 ? 0.4502 0.4552 0.4935 0.0025  0.0031  0.0433  78 TRP A O   
617 C CB  . TRP A 78 ? 0.4530 0.4345 0.4643 -0.0004 -0.0095 0.0369  78 TRP A CB  
618 C CG  . TRP A 78 ? 0.4911 0.4750 0.4908 0.0029  -0.0147 0.0316  78 TRP A CG  
619 C CD1 . TRP A 78 ? 0.5065 0.4898 0.4983 0.0071  -0.0180 0.0379  78 TRP A CD1 
620 C CD2 . TRP A 78 ? 0.4933 0.4855 0.4899 0.0022  -0.0153 0.0180  78 TRP A CD2 
621 N NE1 . TRP A 78 ? 0.5096 0.5093 0.4939 0.0106  -0.0234 0.0313  78 TRP A NE1 
622 C CE2 . TRP A 78 ? 0.4954 0.5015 0.4823 0.0047  -0.0222 0.0164  78 TRP A CE2 
623 C CE3 . TRP A 78 ? 0.5052 0.4939 0.5086 -0.0006 -0.0085 0.0058  78 TRP A CE3 
624 C CZ2 . TRP A 78 ? 0.5126 0.5377 0.4964 0.0005  -0.0247 0.0001  78 TRP A CZ2 
625 C CZ3 . TRP A 78 ? 0.5190 0.5152 0.5195 -0.0061 -0.0079 -0.0122 78 TRP A CZ3 
626 C CH2 . TRP A 78 ? 0.5350 0.5533 0.5257 -0.0075 -0.0171 -0.0165 78 TRP A CH2 
627 N N   A LYS A 79 ? 0.4439 0.4480 0.4873 -0.0097 -0.0084 0.0440  79 LYS A N   
628 N N   B LYS A 79 ? 0.4332 0.4371 0.4765 -0.0096 -0.0085 0.0439  79 LYS A N   
629 C CA  A LYS A 79 ? 0.4488 0.4742 0.5048 -0.0168 -0.0051 0.0467  79 LYS A CA  
630 C CA  B LYS A 79 ? 0.4321 0.4570 0.4879 -0.0170 -0.0054 0.0464  79 LYS A CA  
631 C C   A LYS A 79 ? 0.4132 0.4678 0.4849 -0.0103 -0.0066 0.0522  79 LYS A C   
632 C C   B LYS A 79 ? 0.4046 0.4587 0.4760 -0.0103 -0.0066 0.0521  79 LYS A C   
633 O O   A LYS A 79 ? 0.4086 0.4887 0.4928 -0.0098 -0.0021 0.0564  79 LYS A O   
634 O O   B LYS A 79 ? 0.3998 0.4783 0.4834 -0.0096 -0.0019 0.0563  79 LYS A O   
635 C CB  A LYS A 79 ? 0.4596 0.4829 0.5173 -0.0317 -0.0054 0.0411  79 LYS A CB  
636 C CB  B LYS A 79 ? 0.4283 0.4512 0.4854 -0.0313 -0.0069 0.0403  79 LYS A CB  
637 C CG  A LYS A 79 ? 0.5339 0.5397 0.5879 -0.0384 0.0052  0.0437  79 LYS A CG  
638 C CG  B LYS A 79 ? 0.4828 0.4736 0.5280 -0.0333 -0.0010 0.0409  79 LYS A CG  
639 C CD  A LYS A 79 ? 0.5786 0.5658 0.6354 -0.0527 0.0115  0.0373  79 LYS A CD  
640 C CD  B LYS A 79 ? 0.5182 0.4976 0.5685 -0.0473 0.0033  0.0323  79 LYS A CD  
641 C CE  A LYS A 79 ? 0.5764 0.5914 0.6504 -0.0715 0.0109  0.0238  79 LYS A CE  
642 C CE  B LYS A 79 ? 0.5590 0.5016 0.6011 -0.0447 0.0141  0.0384  79 LYS A CE  
643 N NZ  A LYS A 79 ? 0.6035 0.5959 0.6789 -0.0850 0.0169  0.0101  79 LYS A NZ  
644 N NZ  B LYS A 79 ? 0.5769 0.5144 0.6140 -0.0402 0.0233  0.0525  79 LYS A NZ  
645 N N   . SER A 80 ? 0.3912 0.4462 0.4636 -0.0036 -0.0113 0.0553  80 SER A N   
646 C CA  . SER A 80 ? 0.4202 0.5024 0.5073 0.0084  -0.0097 0.0679  80 SER A CA  
647 C C   . SER A 80 ? 0.4543 0.5245 0.5481 0.0226  0.0022  0.0731  80 SER A C   
648 O O   . SER A 80 ? 0.4414 0.5394 0.5512 0.0336  0.0075  0.0842  80 SER A O   
649 C CB  . SER A 80 ? 0.4341 0.5160 0.5201 0.0140  -0.0133 0.0748  80 SER A CB  
650 O OG  . SER A 80 ? 0.4118 0.5135 0.4924 0.0023  -0.0229 0.0685  80 SER A OG  
651 N N   . ILE A 81 ? 0.4204 0.4540 0.5028 0.0226  0.0073  0.0633  81 ILE A N   
652 C CA  . ILE A 81 ? 0.4463 0.4658 0.5324 0.0325  0.0209  0.0601  81 ILE A CA  
653 C C   . ILE A 81 ? 0.4360 0.4763 0.5243 0.0313  0.0245  0.0600  81 ILE A C   
654 O O   . ILE A 81 ? 0.4353 0.4875 0.5372 0.0436  0.0354  0.0652  81 ILE A O   
655 C CB  . ILE A 81 ? 0.4593 0.4472 0.5303 0.0269  0.0238  0.0429  81 ILE A CB  
656 C CG1 . ILE A 81 ? 0.5123 0.4800 0.5869 0.0267  0.0249  0.0419  81 ILE A CG1 
657 C CG2 . ILE A 81 ? 0.4807 0.4599 0.5512 0.0323  0.0382  0.0316  81 ILE A CG2 
658 C CD1 . ILE A 81 ? 0.5461 0.5009 0.6402 0.0410  0.0409  0.0525  81 ILE A CD1 
659 N N   . ARG A 82 ? 0.4446 0.4872 0.5207 0.0176  0.0182  0.0552  82 ARG A N   
660 C CA  . ARG A 82 ? 0.4741 0.5325 0.5511 0.0136  0.0244  0.0561  82 ARG A CA  
661 C C   . ARG A 82 ? 0.4650 0.5639 0.5653 0.0150  0.0255  0.0654  82 ARG A C   
662 O O   . ARG A 82 ? 0.4418 0.5600 0.5523 0.0214  0.0353  0.0684  82 ARG A O   
663 C CB  . ARG A 82 ? 0.4891 0.5368 0.5512 -0.0003 0.0210  0.0543  82 ARG A CB  
664 C CG  . ARG A 82 ? 0.5650 0.6289 0.6313 -0.0071 0.0303  0.0589  82 ARG A CG  
665 C CD  . ARG A 82 ? 0.6202 0.6646 0.6717 -0.0168 0.0326  0.0621  82 ARG A CD  
666 N NE  . ARG A 82 ? 0.7108 0.7434 0.7394 -0.0072 0.0357  0.0625  82 ARG A NE  
667 C CZ  . ARG A 82 ? 0.7843 0.7999 0.7951 -0.0040 0.0304  0.0633  82 ARG A CZ  
668 N NH1 . ARG A 82 ? 0.8766 0.8772 0.8904 -0.0079 0.0221  0.0622  82 ARG A NH1 
669 N NH2 . ARG A 82 ? 0.7033 0.7241 0.6934 0.0037  0.0336  0.0646  82 ARG A NH2 
670 N N   . GLU A 83 ? 0.4558 0.5747 0.5646 0.0098  0.0156  0.0690  83 GLU A N   
671 C CA  . GLU A 83 ? 0.4959 0.6688 0.6266 0.0084  0.0138  0.0757  83 GLU A CA  
672 C C   . GLU A 83 ? 0.4764 0.6725 0.6228 0.0328  0.0167  0.0915  83 GLU A C   
673 O O   . GLU A 83 ? 0.4197 0.6724 0.5861 0.0379  0.0151  0.1013  83 GLU A O   
674 C CB  . GLU A 83 ? 0.4918 0.6826 0.6222 -0.0118 0.0029  0.0677  83 GLU A CB  
675 C CG  . GLU A 83 ? 0.5806 0.7565 0.7066 -0.0350 0.0075  0.0559  83 GLU A CG  
676 C CD  . GLU A 83 ? 0.6399 0.8202 0.7657 -0.0569 0.0017  0.0421  83 GLU A CD  
677 O OE1 . GLU A 83 ? 0.6475 0.8793 0.7865 -0.0625 -0.0056 0.0385  83 GLU A OE1 
678 O OE2 . GLU A 83 ? 0.7322 0.8682 0.8451 -0.0670 0.0059  0.0351  83 GLU A OE2 
679 N N   . LYS A 84 ? 0.4895 0.6441 0.6286 0.0477  0.0226  0.0944  84 LYS A N   
680 C CA  . LYS A 84 ? 0.5117 0.6717 0.6667 0.0738  0.0322  0.1122  84 LYS A CA  
681 C C   . LYS A 84 ? 0.4957 0.7041 0.6610 0.0796  0.0221  0.1297  84 LYS A C   
682 O O   . LYS A 84 ? 0.5014 0.7492 0.6866 0.1022  0.0277  0.1515  84 LYS A O   
683 C CB  . LYS A 84 ? 0.5484 0.7264 0.7214 0.0911  0.0472  0.1186  84 LYS A CB  
684 C CG  . LYS A 84 ? 0.5855 0.7225 0.7464 0.0874  0.0592  0.1005  84 LYS A CG  
685 C CD  . LYS A 84 ? 0.6517 0.8064 0.8315 0.1075  0.0772  0.1060  84 LYS A CD  
686 C CE  . LYS A 84 ? 0.7101 0.8248 0.8759 0.1060  0.0915  0.0856  84 LYS A CE  
687 N NZ  . LYS A 84 ? 0.7738 0.9126 0.9573 0.1232  0.1090  0.0886  84 LYS A NZ  
688 N N   . ARG A 85 ? 0.4480 0.6564 0.5989 0.0612  0.0082  0.1209  85 ARG A N   
689 C CA  . ARG A 85 ? 0.4179 0.6805 0.5735 0.0617  -0.0029 0.1318  85 ARG A CA  
690 C C   . ARG A 85 ? 0.4080 0.6430 0.5436 0.0459  -0.0119 0.1196  85 ARG A C   
691 O O   . ARG A 85 ? 0.3914 0.5902 0.5134 0.0269  -0.0144 0.0990  85 ARG A O   
692 C CB  . ARG A 85 ? 0.4133 0.7427 0.5807 0.0469  -0.0110 0.1240  85 ARG A CB  
693 C CG  . ARG A 85 ? 0.4084 0.8193 0.5840 0.0471  -0.0228 0.1325  85 ARG A CG  
694 C CD  . ARG A 85 ? 0.3920 0.8732 0.5848 0.0294  -0.0278 0.1203  85 ARG A CD  
695 N NE  . ARG A 85 ? 0.3822 0.8338 0.5668 -0.0061 -0.0287 0.0887  85 ARG A NE  
696 C CZ  . ARG A 85 ? 0.3818 0.8244 0.5532 -0.0313 -0.0357 0.0664  85 ARG A CZ  
697 N NH1 . ARG A 85 ? 0.3748 0.8491 0.5382 -0.0287 -0.0455 0.0684  85 ARG A NH1 
698 N NH2 . ARG A 85 ? 0.3623 0.7653 0.5292 -0.0583 -0.0304 0.0430  85 ARG A NH2 
699 N N   . LEU A 86 ? 0.4175 0.6727 0.5521 0.0565  -0.0150 0.1356  86 LEU A N   
700 C CA  . LEU A 86 ? 0.4341 0.6754 0.5516 0.0429  -0.0229 0.1252  86 LEU A CA  
701 C C   . LEU A 86 ? 0.4049 0.6866 0.5175 0.0184  -0.0353 0.1030  86 LEU A C   
702 O O   . LEU A 86 ? 0.3862 0.7385 0.5072 0.0172  -0.0421 0.1066  86 LEU A O   
703 C CB  . LEU A 86 ? 0.4540 0.7136 0.5722 0.0614  -0.0205 0.1511  86 LEU A CB  
704 C CG  . LEU A 86 ? 0.4575 0.6983 0.5588 0.0505  -0.0251 0.1430  86 LEU A CG  
705 C CD1 . LEU A 86 ? 0.4470 0.6141 0.5422 0.0455  -0.0172 0.1322  86 LEU A CD1 
706 C CD2 . LEU A 86 ? 0.4855 0.7641 0.5879 0.0686  -0.0226 0.1728  86 LEU A CD2 
707 N N   . LEU A 87 ? 0.4239 0.6619 0.5241 -0.0008 -0.0365 0.0796  87 LEU A N   
708 C CA  . LEU A 87 ? 0.3900 0.6462 0.4874 -0.0261 -0.0418 0.0547  87 LEU A CA  
709 C C   . LEU A 87 ? 0.3893 0.6639 0.4753 -0.0327 -0.0484 0.0462  87 LEU A C   
710 O O   . LEU A 87 ? 0.4026 0.6811 0.4831 -0.0171 -0.0495 0.0633  87 LEU A O   
711 C CB  . LEU A 87 ? 0.4118 0.6090 0.5032 -0.0382 -0.0353 0.0396  87 LEU A CB  
712 C CG  . LEU A 87 ? 0.4122 0.5942 0.5114 -0.0327 -0.0276 0.0467  87 LEU A CG  
713 C CD1 . LEU A 87 ? 0.4246 0.5556 0.5145 -0.0427 -0.0208 0.0363  87 LEU A CD1 
714 C CD2 . LEU A 87 ? 0.4321 0.6724 0.5501 -0.0392 -0.0277 0.0469  87 LEU A CD2 
715 N N   . ASP A 88 ? 0.3899 0.6767 0.4739 -0.0570 -0.0500 0.0186  88 ASP A N   
716 C CA  . ASP A 88 ? 0.4036 0.7103 0.4765 -0.0672 -0.0541 0.0023  88 ASP A CA  
717 C C   . ASP A 88 ? 0.4226 0.6615 0.4828 -0.0653 -0.0490 -0.0037 88 ASP A C   
718 O O   . ASP A 88 ? 0.4360 0.6317 0.4960 -0.0777 -0.0418 -0.0214 88 ASP A O   
719 C CB  . ASP A 88 ? 0.4387 0.7822 0.5177 -0.0966 -0.0538 -0.0306 88 ASP A CB  
720 C CG  . ASP A 88 ? 0.4435 0.8272 0.5117 -0.1089 -0.0578 -0.0524 88 ASP A CG  
721 O OD1 . ASP A 88 ? 0.4469 0.8272 0.5016 -0.0930 -0.0608 -0.0388 88 ASP A OD1 
722 O OD2 . ASP A 88 ? 0.5220 0.9413 0.5960 -0.1363 -0.0562 -0.0849 88 ASP A OD2 
723 N N   . VAL A 89 ? 0.4127 0.6471 0.4645 -0.0489 -0.0511 0.0131  89 VAL A N   
724 C CA  . VAL A 89 ? 0.4418 0.6248 0.4845 -0.0445 -0.0474 0.0109  89 VAL A CA  
725 C C   . VAL A 89 ? 0.4694 0.6441 0.5053 -0.0596 -0.0444 -0.0171 89 VAL A C   
726 O O   . VAL A 89 ? 0.4682 0.5973 0.5000 -0.0564 -0.0394 -0.0218 89 VAL A O   
727 C CB  . VAL A 89 ? 0.4537 0.6438 0.4923 -0.0283 -0.0481 0.0332  89 VAL A CB  
728 C CG1 . VAL A 89 ? 0.4732 0.7222 0.5048 -0.0291 -0.0523 0.0347  89 VAL A CG1 
729 C CG2 . VAL A 89 ? 0.4532 0.5951 0.4869 -0.0249 -0.0441 0.0311  89 VAL A CG2 
730 N N   . LYS A 90 ? 0.4983 0.7201 0.5340 -0.0755 -0.0463 -0.0370 90 LYS A N   
731 C CA  . LYS A 90 ? 0.5377 0.7501 0.5690 -0.0921 -0.0394 -0.0695 90 LYS A CA  
732 C C   . LYS A 90 ? 0.5196 0.6751 0.5595 -0.1031 -0.0271 -0.0848 90 LYS A C   
733 O O   . LYS A 90 ? 0.5280 0.6490 0.5664 -0.1094 -0.0159 -0.1052 90 LYS A O   
734 C CB  . LYS A 90 ? 0.6139 0.8965 0.6440 -0.1117 -0.0427 -0.0943 90 LYS A CB  
735 C CG  . LYS A 90 ? 0.6882 1.0449 0.7090 -0.1009 -0.0541 -0.0770 90 LYS A CG  
736 C CD  . LYS A 90 ? 0.7892 1.1413 0.7953 -0.0886 -0.0529 -0.0704 90 LYS A CD  
737 C CE  . LYS A 90 ? 0.8661 1.2958 0.8627 -0.0780 -0.0614 -0.0494 90 LYS A CE  
738 N NZ  . LYS A 90 ? 0.9003 1.3303 0.8830 -0.0690 -0.0580 -0.0441 90 LYS A NZ  
739 N N   . ASN A 91 ? 0.4966 0.6419 0.5463 -0.1039 -0.0267 -0.0730 91 ASN A N   
740 C CA  . ASN A 91 ? 0.5235 0.6142 0.5805 -0.1115 -0.0130 -0.0796 91 ASN A CA  
741 C C   . ASN A 91 ? 0.5203 0.5547 0.5708 -0.0901 -0.0094 -0.0595 91 ASN A C   
742 O O   . ASN A 91 ? 0.5464 0.5373 0.6007 -0.0904 0.0023  -0.0567 91 ASN A O   
743 C CB  . ASN A 91 ? 0.5179 0.6258 0.5875 -0.1204 -0.0127 -0.0735 91 ASN A CB  
744 C CG  . ASN A 91 ? 0.5515 0.7214 0.6316 -0.1453 -0.0147 -0.0972 91 ASN A CG  
745 O OD1 . ASN A 91 ? 0.5897 0.7792 0.6672 -0.1609 -0.0125 -0.1248 91 ASN A OD1 
746 N ND2 . ASN A 91 ? 0.5525 0.7589 0.6454 -0.1503 -0.0181 -0.0894 91 ASN A ND2 
747 N N   . TYR A 92 ? 0.4821 0.5213 0.5235 -0.0722 -0.0183 -0.0447 92 TYR A N   
748 C CA  . TYR A 92 ? 0.4637 0.4662 0.5004 -0.0542 -0.0174 -0.0275 92 TYR A CA  
749 C C   . TYR A 92 ? 0.4620 0.4606 0.4925 -0.0437 -0.0186 -0.0290 92 TYR A C   
750 O O   . TYR A 92 ? 0.4646 0.4575 0.4920 -0.0303 -0.0230 -0.0147 92 TYR A O   
751 C CB  . TYR A 92 ? 0.4629 0.4777 0.4996 -0.0446 -0.0255 -0.0075 92 TYR A CB  
752 C CG  . TYR A 92 ? 0.4612 0.4808 0.5054 -0.0519 -0.0227 -0.0046 92 TYR A CG  
753 C CD1 . TYR A 92 ? 0.5015 0.4890 0.5453 -0.0502 -0.0145 0.0005  92 TYR A CD1 
754 C CD2 . TYR A 92 ? 0.4722 0.5347 0.5243 -0.0597 -0.0272 -0.0059 92 TYR A CD2 
755 C CE1 . TYR A 92 ? 0.5335 0.5275 0.5851 -0.0582 -0.0098 0.0031  92 TYR A CE1 
756 C CE2 . TYR A 92 ? 0.4766 0.5500 0.5386 -0.0671 -0.0238 -0.0044 92 TYR A CE2 
757 C CZ  . TYR A 92 ? 0.5149 0.5518 0.5768 -0.0674 -0.0145 -0.0007 92 TYR A CZ  
758 O OH  . TYR A 92 ? 0.5876 0.6365 0.6598 -0.0751 -0.0093 0.0016  92 TYR A OH  
759 N N   . ASP A 93 ? 0.5025 0.5080 0.5321 -0.0515 -0.0134 -0.0488 93 ASP A N   
760 C CA  . ASP A 93 ? 0.5549 0.5652 0.5795 -0.0420 -0.0136 -0.0513 93 ASP A CA  
761 C C   . ASP A 93 ? 0.5702 0.5384 0.5978 -0.0317 -0.0007 -0.0554 93 ASP A C   
762 O O   . ASP A 93 ? 0.5795 0.5251 0.6113 -0.0404 0.0132  -0.0742 93 ASP A O   
763 C CB  . ASP A 93 ? 0.6156 0.6652 0.6357 -0.0536 -0.0145 -0.0703 93 ASP A CB  
764 C CG  . ASP A 93 ? 0.6447 0.7087 0.6591 -0.0445 -0.0141 -0.0721 93 ASP A CG  
765 O OD1 . ASP A 93 ? 0.5839 0.6220 0.6011 -0.0304 -0.0101 -0.0653 93 ASP A OD1 
766 O OD2 . ASP A 93 ? 0.6864 0.7952 0.6938 -0.0508 -0.0180 -0.0784 93 ASP A OD2 
767 N N   . PRO A 94 ? 0.5569 0.5162 0.5840 -0.0131 -0.0032 -0.0385 94 PRO A N   
768 C CA  . PRO A 94 ? 0.5963 0.5249 0.6275 0.0029  0.0091  -0.0363 94 PRO A CA  
769 C C   . PRO A 94 ? 0.6585 0.5862 0.6921 0.0050  0.0199  -0.0555 94 PRO A C   
770 O O   . PRO A 94 ? 0.7162 0.6083 0.7561 0.0148  0.0373  -0.0599 94 PRO A O   
771 C CB  . PRO A 94 ? 0.5986 0.5408 0.6289 0.0200  -0.0002 -0.0154 94 PRO A CB  
772 C CG  . PRO A 94 ? 0.5707 0.5467 0.5977 0.0102  -0.0146 -0.0132 94 PRO A CG  
773 C CD  . PRO A 94 ? 0.5693 0.5494 0.5942 -0.0069 -0.0161 -0.0209 94 PRO A CD  
774 N N   . TYR A 95 ? 0.6617 0.6277 0.6903 -0.0024 0.0119  -0.0650 95 TYR A N   
775 C CA  . TYR A 95 ? 0.6870 0.6617 0.7155 -0.0010 0.0217  -0.0851 95 TYR A CA  
776 C C   . TYR A 95 ? 0.7611 0.7373 0.7867 -0.0228 0.0305  -0.1159 95 TYR A C   
777 O O   . TYR A 95 ? 0.7810 0.7718 0.8036 -0.0265 0.0388  -0.1390 95 TYR A O   
778 C CB  . TYR A 95 ? 0.6087 0.6291 0.6327 0.0019  0.0111  -0.0787 95 TYR A CB  
779 C CG  . TYR A 95 ? 0.5809 0.6027 0.6127 0.0226  0.0109  -0.0629 95 TYR A CG  
780 C CD1 . TYR A 95 ? 0.5956 0.6120 0.6340 0.0377  0.0243  -0.0720 95 TYR A CD1 
781 C CD2 . TYR A 95 ? 0.5429 0.5747 0.5774 0.0269  -0.0010 -0.0414 95 TYR A CD2 
782 C CE1 . TYR A 95 ? 0.6135 0.6432 0.6616 0.0580  0.0235  -0.0568 95 TYR A CE1 
783 C CE2 . TYR A 95 ? 0.5538 0.5995 0.5970 0.0429  -0.0022 -0.0305 95 TYR A CE2 
784 C CZ  . TYR A 95 ? 0.5782 0.6266 0.6286 0.0594  0.0090  -0.0365 95 TYR A CZ  
785 O OH  . TYR A 95 ? 0.6329 0.7065 0.6944 0.0769  0.0071  -0.0247 95 TYR A OH  
786 N N   . LYS A 96 ? 0.8621 0.8300 0.8890 -0.0390 0.0290  -0.1190 96 LYS A N   
787 C CA  . LYS A 96 ? 0.9985 0.9669 1.0270 -0.0630 0.0403  -0.1530 96 LYS A CA  
788 C C   . LYS A 96 ? 1.1008 1.0439 1.1376 -0.0760 0.0437  -0.1498 96 LYS A C   
789 O O   . LYS A 96 ? 1.1293 1.1103 1.1647 -0.0937 0.0328  -0.1538 96 LYS A O   
790 C CB  . LYS A 96 ? 1.0159 1.0524 1.0328 -0.0779 0.0281  -0.1679 96 LYS A CB  
791 C CG  . LYS A 96 ? 1.1355 1.1863 1.1507 -0.0993 0.0422  -0.2131 96 LYS A CG  
792 C CD  . LYS A 96 ? 1.1583 1.2917 1.1593 -0.1139 0.0285  -0.2257 96 LYS A CD  
793 C CE  . LYS A 96 ? 1.2053 1.3619 1.2038 -0.1403 0.0419  -0.2768 96 LYS A CE  
794 N NZ  . LYS A 96 ? 1.2025 1.4527 1.1868 -0.1551 0.0258  -0.2852 96 LYS A NZ  
795 N N   . PRO A 97 ? 1.2282 1.1111 1.2746 -0.0654 0.0598  -0.1391 97 PRO A N   
796 C CA  . PRO A 97 ? 1.2606 1.1173 1.3157 -0.0779 0.0667  -0.1341 97 PRO A CA  
797 C C   . PRO A 97 ? 1.2919 1.1563 1.3553 -0.1129 0.0779  -0.1717 97 PRO A C   
798 O O   . PRO A 97 ? 1.3193 1.1903 1.3831 -0.1258 0.0882  -0.2061 97 PRO A O   
799 C CB  . PRO A 97 ? 1.2951 1.0866 1.3578 -0.0562 0.0874  -0.1155 97 PRO A CB  
800 C CG  . PRO A 97 ? 1.2849 1.0858 1.3414 -0.0268 0.0806  -0.1001 97 PRO A CG  
801 C CD  . PRO A 97 ? 1.2456 1.0889 1.2959 -0.0384 0.0731  -0.1273 97 PRO A CD  
802 N N   . LEU A 98 ? 1.2861 1.1562 1.3567 -0.1297 0.0762  -0.1677 98 LEU A N   
803 C CA  . LEU A 98 ? 1.2818 1.1633 1.3648 -0.1666 0.0881  -0.2042 98 LEU A CA  
804 C C   . LEU A 98 ? 1.2811 1.1070 1.3803 -0.1751 0.1091  -0.1947 98 LEU A C   
805 O O   . LEU A 98 ? 1.2881 1.0606 1.4014 -0.1905 0.1392  -0.2190 98 LEU A O   
806 C CB  . LEU A 98 ? 1.2568 1.2254 1.3356 -0.1840 0.0643  -0.2129 98 LEU A CB  
807 C CG  . LEU A 98 ? 1.2463 1.2433 1.3251 -0.1749 0.0460  -0.1787 98 LEU A CG  
808 C CD1 . LEU A 98 ? 1.2700 1.2436 1.3659 -0.1928 0.0595  -0.1784 98 LEU A CD1 
809 C CD2 . LEU A 98 ? 1.1781 1.2642 1.2506 -0.1801 0.0229  -0.1810 98 LEU A CD2 
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