data_9DFO
# 
_entry.id   9DFO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DFO         pdb_00009dfo 10.2210/pdb9dfo/pdb 
WWPDB D_1000287969 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DFO 
_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                ? 
_citation.page_last                 ? 
_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      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Frigon, L.'   1 0009-0004-7020-5295 
primary 'Pascal, J.M.' 2 0000-0002-2714-4317 
# 
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' 11710.606 1   2.4.2.- K31Q ? ? 
2 non-polymer syn 'SULFATE ION'                               96.063    1   ?       ?    ? ? 
3 water       nat water                                       18.015    133 ?       ?    ? ? 
# 
_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       
;MVMGIFANCIFCLKVKYLPQQQKKKLQTDIQENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKS
IREKRLLDVKNYDPYKPLDI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVMGIFANCIFCLKVKYLPQQQKKKLQTDIQENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKS
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  GLN 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  PHE 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  GLN 31  31  31 GLN GLN 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  PHE 39  39  39 PHE PHE 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  ?  ?   ?   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 3   SO4 SO4 A . 
C 3 HOH 1   301 101 HOH HOH A . 
C 3 HOH 2   302 35  HOH HOH A . 
C 3 HOH 3   303 107 HOH HOH A . 
C 3 HOH 4   304 1   HOH HOH A . 
C 3 HOH 5   305 135 HOH HOH A . 
C 3 HOH 6   306 33  HOH HOH A . 
C 3 HOH 7   307 132 HOH HOH A . 
C 3 HOH 8   308 82  HOH HOH A . 
C 3 HOH 9   309 65  HOH HOH A . 
C 3 HOH 10  310 68  HOH HOH A . 
C 3 HOH 11  311 151 HOH HOH A . 
C 3 HOH 12  312 96  HOH HOH A . 
C 3 HOH 13  313 38  HOH HOH A . 
C 3 HOH 14  314 28  HOH HOH A . 
C 3 HOH 15  315 5   HOH HOH A . 
C 3 HOH 16  316 75  HOH HOH A . 
C 3 HOH 17  317 147 HOH HOH A . 
C 3 HOH 18  318 20  HOH HOH A . 
C 3 HOH 19  319 51  HOH HOH A . 
C 3 HOH 20  320 2   HOH HOH A . 
C 3 HOH 21  321 37  HOH HOH A . 
C 3 HOH 22  322 66  HOH HOH A . 
C 3 HOH 23  323 12  HOH HOH A . 
C 3 HOH 24  324 30  HOH HOH A . 
C 3 HOH 25  325 140 HOH HOH A . 
C 3 HOH 26  326 79  HOH HOH A . 
C 3 HOH 27  327 100 HOH HOH A . 
C 3 HOH 28  328 52  HOH HOH A . 
C 3 HOH 29  329 15  HOH HOH A . 
C 3 HOH 30  330 24  HOH HOH A . 
C 3 HOH 31  331 84  HOH HOH A . 
C 3 HOH 32  332 122 HOH HOH A . 
C 3 HOH 33  333 117 HOH HOH A . 
C 3 HOH 34  334 26  HOH HOH A . 
C 3 HOH 35  335 43  HOH HOH A . 
C 3 HOH 36  336 34  HOH HOH A . 
C 3 HOH 37  337 69  HOH HOH A . 
C 3 HOH 38  338 124 HOH HOH A . 
C 3 HOH 39  339 94  HOH HOH A . 
C 3 HOH 40  340 83  HOH HOH A . 
C 3 HOH 41  341 16  HOH HOH A . 
C 3 HOH 42  342 129 HOH HOH A . 
C 3 HOH 43  343 44  HOH HOH A . 
C 3 HOH 44  344 21  HOH HOH A . 
C 3 HOH 45  345 115 HOH HOH A . 
C 3 HOH 46  346 85  HOH HOH A . 
C 3 HOH 47  347 4   HOH HOH A . 
C 3 HOH 48  348 3   HOH HOH A . 
C 3 HOH 49  349 54  HOH HOH A . 
C 3 HOH 50  350 49  HOH HOH A . 
C 3 HOH 51  351 31  HOH HOH A . 
C 3 HOH 52  352 78  HOH HOH A . 
C 3 HOH 53  353 46  HOH HOH A . 
C 3 HOH 54  354 148 HOH HOH A . 
C 3 HOH 55  355 40  HOH HOH A . 
C 3 HOH 56  356 123 HOH HOH A . 
C 3 HOH 57  357 22  HOH HOH A . 
C 3 HOH 58  358 53  HOH HOH A . 
C 3 HOH 59  359 50  HOH HOH A . 
C 3 HOH 60  360 10  HOH HOH A . 
C 3 HOH 61  361 39  HOH HOH A . 
C 3 HOH 62  362 23  HOH HOH A . 
C 3 HOH 63  363 36  HOH HOH A . 
C 3 HOH 64  364 47  HOH HOH A . 
C 3 HOH 65  365 109 HOH HOH A . 
C 3 HOH 66  366 114 HOH HOH A . 
C 3 HOH 67  367 27  HOH HOH A . 
C 3 HOH 68  368 42  HOH HOH A . 
C 3 HOH 69  369 72  HOH HOH A . 
C 3 HOH 70  370 141 HOH HOH A . 
C 3 HOH 71  371 80  HOH HOH A . 
C 3 HOH 72  372 77  HOH HOH A . 
C 3 HOH 73  373 137 HOH HOH A . 
C 3 HOH 74  374 120 HOH HOH A . 
C 3 HOH 75  375 91  HOH HOH A . 
C 3 HOH 76  376 67  HOH HOH A . 
C 3 HOH 77  377 126 HOH HOH A . 
C 3 HOH 78  378 134 HOH HOH A . 
C 3 HOH 79  379 6   HOH HOH A . 
C 3 HOH 80  380 105 HOH HOH A . 
C 3 HOH 81  381 113 HOH HOH A . 
C 3 HOH 82  382 32  HOH HOH A . 
C 3 HOH 83  383 41  HOH HOH A . 
C 3 HOH 84  384 138 HOH HOH A . 
C 3 HOH 85  385 9   HOH HOH A . 
C 3 HOH 86  386 29  HOH HOH A . 
C 3 HOH 87  387 149 HOH HOH A . 
C 3 HOH 88  388 8   HOH HOH A . 
C 3 HOH 89  389 130 HOH HOH A . 
C 3 HOH 90  390 56  HOH HOH A . 
C 3 HOH 91  391 133 HOH HOH A . 
C 3 HOH 92  392 146 HOH HOH A . 
C 3 HOH 93  393 108 HOH HOH A . 
C 3 HOH 94  394 95  HOH HOH A . 
C 3 HOH 95  395 98  HOH HOH A . 
C 3 HOH 96  396 45  HOH HOH A . 
C 3 HOH 97  397 89  HOH HOH A . 
C 3 HOH 98  398 136 HOH HOH A . 
C 3 HOH 99  399 103 HOH HOH A . 
C 3 HOH 100 400 13  HOH HOH A . 
C 3 HOH 101 401 102 HOH HOH A . 
C 3 HOH 102 402 110 HOH HOH A . 
C 3 HOH 103 403 127 HOH HOH A . 
C 3 HOH 104 404 125 HOH HOH A . 
C 3 HOH 105 405 97  HOH HOH A . 
C 3 HOH 106 406 48  HOH HOH A . 
C 3 HOH 107 407 81  HOH HOH A . 
C 3 HOH 108 408 119 HOH HOH A . 
C 3 HOH 109 409 25  HOH HOH A . 
C 3 HOH 110 410 139 HOH HOH A . 
C 3 HOH 111 411 14  HOH HOH A . 
C 3 HOH 112 412 18  HOH HOH A . 
C 3 HOH 113 413 111 HOH HOH A . 
C 3 HOH 114 414 106 HOH HOH A . 
C 3 HOH 115 415 150 HOH HOH A . 
C 3 HOH 116 416 17  HOH HOH A . 
C 3 HOH 117 417 7   HOH HOH A . 
C 3 HOH 118 418 58  HOH HOH A . 
C 3 HOH 119 419 62  HOH HOH A . 
C 3 HOH 120 420 99  HOH HOH A . 
C 3 HOH 121 421 118 HOH HOH A . 
C 3 HOH 122 422 145 HOH HOH A . 
C 3 HOH 123 423 19  HOH HOH A . 
C 3 HOH 124 424 131 HOH HOH A . 
C 3 HOH 125 425 112 HOH HOH A . 
C 3 HOH 126 426 92  HOH HOH A . 
C 3 HOH 127 427 70  HOH HOH A . 
C 3 HOH 128 428 63  HOH HOH A . 
C 3 HOH 129 429 76  HOH HOH A . 
C 3 HOH 130 430 121 HOH HOH A . 
C 3 HOH 131 431 93  HOH HOH A . 
C 3 HOH 132 432 142 HOH HOH A . 
C 3 HOH 133 433 128 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                     9DFO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.769 
_cell.length_a_esd                 ? 
_cell.length_b                     114.769 
_cell.length_b_esd                 ? 
_cell.length_c                     114.769 
_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                         9DFO 
_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                   9DFO 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.26 
_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    '31% PEG3350, 0.2M ammonium sulfate and 0.1M 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                                       9DFO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_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                                     9972 
_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                                8.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          36.9 
_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                                    1.90 
_reflns_shell.d_res_low                                     1.94 
_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                             653 
_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                               8.1 
_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                                  0.837 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_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                               34.530 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_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                                 9DFO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.90 
_refine.ls_d_res_low                             19.41 
_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                     9453 
_refine.ls_number_reflns_R_free                  516 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17215 
_refine.ls_R_factor_R_free                       0.20843 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17025 
_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                       0.134 
_refine.pdbx_overall_ESU_R_Free                  0.127 
_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                             6.287 
_refine.overall_SU_ML                            0.097 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        19.41 
_refine_hist.number_atoms_solvent             133 
_refine_hist.number_atoms_total               913 
_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        775 
_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  826  ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  799  ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.259  1.813  1122 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.434  1.793  1850 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 6.138  5.000  101  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 1.649  5.000  2    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 10.604 10.000 156  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.062  0.200  122  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  959  ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  191  ? 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' ? 1.350  2.424  389  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 1.349  2.424  389  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 2.104  4.335  489  ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 2.103  4.348  490  ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 2.056  2.781  437  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.023  2.726  434  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.278  4.894  626  ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 8.220  25.97  995  ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 8.112  24.88  941  ? 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                          1.901 
_refine_ls_shell.d_res_low                           1.950 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                26 
_refine_ls_shell.number_reflns_R_work                716 
_refine_ls_shell.percent_reflns_obs                  99.73 
_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                     0.238 
_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                     0.285 
# 
_struct.entry_id                     9DFO 
_struct.title                        'PARP4 BRCT domain K31Q 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        9DFO 
_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              9DFO 
_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             9DFO 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      31 
_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                    LYS 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          31 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            31 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 PRO A 19 ? GLU A 32 ? PRO A 19 GLU A 32 1 ? 14 
HELX_P HELX_P2 AA2 SER A 57 ? ASN A 67 ? SER A 57 ASN A 67 1 ? 11 
HELX_P HELX_P3 AA3 ASN A 73 ? LYS A 84 ? ASN A 73 LYS A 84 1 ? 12 
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 CYS A 12 ? N CYS A 12 O ILE A 49 ? O ILE A 49 
AA1 3 4 N ILE A 48 ? N ILE A 48 O ALA A 72 ? O ALA A 72 
# 
_pdbx_entry_details.entry_id                   9DFO 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    LYS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -114.11 
_pdbx_validate_torsion.psi             76.35 
# 
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 330 ? C HOH . 
2 1 A HOH 362 ? C HOH . 
3 1 A HOH 397 ? C HOH . 
4 1 A HOH 409 ? C HOH . 
5 1 A HOH 410 ? C HOH . 
6 1 A HOH 417 ? C HOH . 
7 1 A HOH 420 ? C HOH . 
8 1 A HOH 431 ? 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         13.2937 
_pdbx_refine_tls.origin_y         3.3899 
_pdbx_refine_tls.origin_z         25.4318 
_pdbx_refine_tls.T[1][1]          0.0130 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0062 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0183 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0492 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0280 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0433 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          6.2233 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0787 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -1.8406 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.9701 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2914 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          4.4243 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.1039 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.4480 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0652 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0079 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0148 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0633 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0677 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0654 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1186 
_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     97 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       433 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.59 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A 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 LEU 98  ? A LEU 98  
5 1 Y 1 A ASP 99  ? A ASP 99  
6 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                    9DFO 
_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]   0.008713 
_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]   0.008713 
_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]   0.008713 
_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  ? 25.532 -8.108  25.075 1.00 48.27  ? 4   GLY A N   1 
ATOM   2   C CA  . GLY A 1 4  ? 25.501 -6.797  24.393 1.00 44.32  ? 4   GLY A CA  1 
ATOM   3   C C   . GLY A 1 4  ? 25.276 -5.635  25.363 1.00 41.95  ? 4   GLY A C   1 
ATOM   4   O O   . GLY A 1 4  ? 25.046 -5.833  26.552 1.00 42.53  ? 4   GLY A O   1 
ATOM   5   N N   . ILE A 1 5  ? 25.304 -4.414  24.820 1.00 40.44  ? 5   ILE A N   1 
ATOM   6   C CA  . ILE A 1 5  ? 25.292 -3.194  25.616 1.00 39.79  ? 5   ILE A CA  1 
ATOM   7   C C   . ILE A 1 5  ? 23.969 -3.021  26.362 1.00 38.68  ? 5   ILE A C   1 
ATOM   8   O O   . ILE A 1 5  ? 23.914 -2.272  27.337 1.00 36.94  ? 5   ILE A O   1 
ATOM   9   C CB  . ILE A 1 5  ? 25.603 -1.960  24.746 1.00 39.21  ? 5   ILE A CB  1 
ATOM   10  C CG1 . ILE A 1 5  ? 24.613 -1.796  23.591 1.00 36.10  ? 5   ILE A CG1 1 
ATOM   11  C CG2 . ILE A 1 5  ? 27.047 -2.008  24.254 1.00 41.70  ? 5   ILE A CG2 1 
ATOM   12  C CD1 . ILE A 1 5  ? 24.817 -0.538  22.775 1.00 35.46  ? 5   ILE A CD1 1 
ATOM   13  N N   . PHE A 1 6  ? 22.905 -3.700  25.910 1.00 37.60  ? 6   PHE A N   1 
ATOM   14  C CA  . PHE A 1 6  ? 21.607 -3.563  26.547 1.00 36.71  ? 6   PHE A CA  1 
ATOM   15  C C   . PHE A 1 6  ? 21.290 -4.774  27.417 1.00 39.22  ? 6   PHE A C   1 
ATOM   16  O O   . PHE A 1 6  ? 20.129 -5.002  27.752 1.00 38.93  ? 6   PHE A O   1 
ATOM   17  C CB  . PHE A 1 6  ? 20.527 -3.361  25.481 1.00 34.63  ? 6   PHE A CB  1 
ATOM   18  C CG  . PHE A 1 6  ? 20.670 -2.106  24.637 1.00 32.51  ? 6   PHE A CG  1 
ATOM   19  C CD1 . PHE A 1 6  ? 20.919 -0.867  25.222 1.00 32.47  ? 6   PHE A CD1 1 
ATOM   20  C CD2 . PHE A 1 6  ? 20.516 -2.167  23.257 1.00 32.71  ? 6   PHE A CD2 1 
ATOM   21  C CE1 . PHE A 1 6  ? 21.014 0.281   24.441 1.00 31.83  ? 6   PHE A CE1 1 
ATOM   22  C CE2 . PHE A 1 6  ? 20.622 -1.024  22.480 1.00 30.72  ? 6   PHE A CE2 1 
ATOM   23  C CZ  . PHE A 1 6  ? 20.875 0.200   23.072 1.00 30.35  ? 6   PHE A CZ  1 
ATOM   24  N N   . ALA A 1 7  ? 22.317 -5.525  27.827 1.00 41.91  ? 7   ALA A N   1 
ATOM   25  C CA  . ALA A 1 7  ? 22.118 -6.629  28.751 1.00 44.86  ? 7   ALA A CA  1 
ATOM   26  C C   . ALA A 1 7  ? 21.342 -6.145  29.975 1.00 44.12  ? 7   ALA A C   1 
ATOM   27  O O   . ALA A 1 7  ? 21.636 -5.081  30.517 1.00 44.21  ? 7   ALA A O   1 
ATOM   28  C CB  . ALA A 1 7  ? 23.449 -7.221  29.151 1.00 48.25  ? 7   ALA A CB  1 
ATOM   29  N N   . ASN A 1 8  ? 20.332 -6.929  30.375 1.00 43.42  ? 8   ASN A N   1 
ATOM   30  C CA  . ASN A 1 8  ? 19.534 -6.673  31.567 1.00 44.90  ? 8   ASN A CA  1 
ATOM   31  C C   . ASN A 1 8  ? 18.660 -5.422  31.443 1.00 41.23  ? 8   ASN A C   1 
ATOM   32  O O   . ASN A 1 8  ? 18.099 -4.974  32.438 1.00 41.54  ? 8   ASN A O   1 
ATOM   33  C CB  . ASN A 1 8  ? 20.400 -6.616  32.821 1.00 47.64  ? 8   ASN A CB  1 
ATOM   34  C CG  . ASN A 1 8  ? 21.026 -7.953  33.115 1.00 52.64  ? 8   ASN A CG  1 
ATOM   35  O OD1 . ASN A 1 8  ? 20.313 -8.922  33.397 1.00 55.57  ? 8   ASN A OD1 1 
ATOM   36  N ND2 . ASN A 1 8  ? 22.346 -8.024  33.074 1.00 53.55  ? 8   ASN A ND2 1 
ATOM   37  N N   . CYS A 1 9  ? 18.513 -4.867  30.237 1.00 39.44  ? 9   CYS A N   1 
ATOM   38  C CA  . CYS A 1 9  ? 17.594 -3.755  30.029 1.00 36.12  ? 9   CYS A CA  1 
ATOM   39  C C   . CYS A 1 9  ? 16.292 -4.297  29.463 1.00 35.45  ? 9   CYS A C   1 
ATOM   40  O O   . CYS A 1 9  ? 16.301 -5.172  28.593 1.00 35.15  ? 9   CYS A O   1 
ATOM   41  C CB  . CYS A 1 9  ? 18.159 -2.690  29.102 1.00 35.55  ? 9   CYS A CB  1 
ATOM   42  S SG  . CYS A 1 9  ? 19.702 -1.960  29.708 1.00 40.13  ? 9   CYS A SG  1 
ATOM   43  N N   . ILE A 1 10 ? 15.188 -3.786  30.012 1.00 36.12  ? 10  ILE A N   1 
ATOM   44  C CA  . ILE A 1 10 ? 13.851 -4.108  29.548 1.00 36.81  ? 10  ILE A CA  1 
ATOM   45  C C   . ILE A 1 10 ? 13.190 -2.784  29.187 1.00 34.73  ? 10  ILE A C   1 
ATOM   46  O O   . ILE A 1 10 ? 12.972 -1.942  30.060 1.00 33.53  ? 10  ILE A O   1 
ATOM   47  C CB  . ILE A 1 10 ? 13.068 -4.895  30.620 1.00 39.19  ? 10  ILE A CB  1 
ATOM   48  C CG1 . ILE A 1 10 ? 13.822 -6.160  31.045 1.00 42.98  ? 10  ILE A CG1 1 
ATOM   49  C CG2 . ILE A 1 10 ? 11.647 -5.218  30.153 1.00 40.71  ? 10  ILE A CG2 1 
ATOM   50  C CD1 . ILE A 1 10 ? 13.026 -7.057  31.970 1.00 46.89  ? 10  ILE A CD1 1 
ATOM   51  N N   . PHE A 1 11 ? 12.916 -2.613  27.889 1.00 33.81  ? 11  PHE A N   1 
ATOM   52  C CA  . PHE A 1 11 ? 12.439 -1.355  27.348 1.00 31.58  ? 11  PHE A CA  1 
ATOM   53  C C   . PHE A 1 11 ? 10.941 -1.446  27.079 1.00 32.57  ? 11  PHE A C   1 
ATOM   54  O O   . PHE A 1 11 ? 10.503 -2.329  26.338 1.00 34.57  ? 11  PHE A O   1 
ATOM   55  C CB  . PHE A 1 11 ? 13.155 -1.041  26.033 1.00 31.79  ? 11  PHE A CB  1 
ATOM   56  C CG  . PHE A 1 11 ? 14.647 -0.775  26.158 1.00 32.02  ? 11  PHE A CG  1 
ATOM   57  C CD1 . PHE A 1 11 ? 15.120 0.502   26.422 1.00 31.39  ? 11  PHE A CD1 1 
ATOM   58  C CD2 . PHE A 1 11 ? 15.570 -1.803  25.995 1.00 33.20  ? 11  PHE A CD2 1 
ATOM   59  C CE1 . PHE A 1 11 ? 16.479 0.745   26.525 1.00 32.06  ? 11  PHE A CE1 1 
ATOM   60  C CE2 . PHE A 1 11 ? 16.925 -1.550  26.090 1.00 34.96  ? 11  PHE A CE2 1 
ATOM   61  C CZ  . PHE A 1 11 ? 17.378 -0.278  26.350 1.00 31.80  ? 11  PHE A CZ  1 
ATOM   62  N N   . CYS A 1 12 ? 10.174 -0.522  27.675 1.00 30.59  ? 12  CYS A N   1 
ATOM   63  C CA  . CYS A 1 12 ? 8.823  -0.244  27.208 1.00 30.49  ? 12  CYS A CA  1 
ATOM   64  C C   . CYS A 1 12 ? 8.909  0.705   26.015 1.00 27.59  ? 12  CYS A C   1 
ATOM   65  O O   . CYS A 1 12 ? 9.523  1.768   26.119 1.00 28.08  ? 12  CYS A O   1 
ATOM   66  C CB  . CYS A 1 12 ? 7.957  0.355   28.311 1.00 32.24  ? 12  CYS A CB  1 
ATOM   67  S SG  . CYS A 1 12 ? 6.289  0.787   27.735 1.00 32.72  ? 12  CYS A SG  1 
ATOM   68  N N   . LEU A 1 13 ? 8.343  0.301   24.868 1.00 27.44  ? 13  LEU A N   1 
ATOM   69  C CA  . LEU A 1 13 ? 8.380  1.127   23.669 1.00 26.14  ? 13  LEU A CA  1 
ATOM   70  C C   . LEU A 1 13 ? 7.025  1.803   23.458 1.00 25.93  ? 13  LEU A C   1 
ATOM   71  O O   . LEU A 1 13 ? 6.007  1.143   23.252 1.00 26.22  ? 13  LEU A O   1 
ATOM   72  C CB  . LEU A 1 13 ? 8.774  0.262   22.477 1.00 27.38  ? 13  LEU A CB  1 
ATOM   73  C CG  . LEU A 1 13 ? 10.118 -0.460  22.605 1.00 28.92  ? 13  LEU A CG  1 
ATOM   74  C CD1 . LEU A 1 13 ? 10.364 -1.282  21.339 1.00 30.65  ? 13  LEU A CD1 1 
ATOM   75  C CD2 . LEU A 1 13 ? 11.247 0.512   22.883 1.00 27.73  ? 13  LEU A CD2 1 
ATOM   76  N N   . LYS A 1 14 ? 7.024  3.127   23.609 1.00 25.60  ? 14  LYS A N   1 
ATOM   77  C CA  . LYS A 1 14 ? 5.900  3.972   23.249 1.00 27.34  ? 14  LYS A CA  1 
ATOM   78  C C   . LYS A 1 14 ? 6.329  4.866   22.089 1.00 26.09  ? 14  LYS A C   1 
ATOM   79  O O   . LYS A 1 14 ? 6.639  6.039   22.294 1.00 25.35  ? 14  LYS A O   1 
ATOM   80  C CB  . LYS A 1 14 ? 5.522  4.837   24.455 1.00 32.06  ? 14  LYS A CB  1 
ATOM   81  C CG  . LYS A 1 14 ? 5.017  4.080   25.675 1.00 36.86  ? 14  LYS A CG  1 
ATOM   82  C CD  . LYS A 1 14 ? 3.762  3.241   25.442 1.00 41.76  ? 14  LYS A CD  1 
ATOM   83  C CE  . LYS A 1 14 ? 3.246  2.648   26.722 1.00 42.70  ? 14  LYS A CE  1 
ATOM   84  N NZ  . LYS A 1 14 ? 2.168  1.684   26.514 1.00 42.91  ? 14  LYS A NZ  1 
ATOM   85  N N   . VAL A 1 15 ? 6.385  4.279   20.889 1.00 26.42  ? 15  VAL A N   1 
ATOM   86  C CA  . VAL A 1 15 ? 6.930  4.955   19.720 1.00 27.69  ? 15  VAL A CA  1 
ATOM   87  C C   . VAL A 1 15 ? 5.971  4.820   18.534 1.00 28.95  ? 15  VAL A C   1 
ATOM   88  O O   . VAL A 1 15 ? 6.394  4.666   17.381 1.00 29.36  ? 15  VAL A O   1 
ATOM   89  C CB  . VAL A 1 15 ? 8.323  4.364   19.424 1.00 27.66  ? 15  VAL A CB  1 
ATOM   90  C CG1 . VAL A 1 15 ? 9.311  4.693   20.529 1.00 27.66  ? 15  VAL A CG1 1 
ATOM   91  C CG2 . VAL A 1 15 ? 8.277  2.861   19.177 1.00 27.68  ? 15  VAL A CG2 1 
ATOM   92  N N   . LYS A 1 16 ? 4.672  4.979   18.830 1.00 29.15  ? 16  LYS A N   1 
ATOM   93  C CA  . LYS A 1 16 ? 3.593  4.724   17.892 1.00 30.63  ? 16  LYS A CA  1 
ATOM   94  C C   . LYS A 1 16 ? 3.726  5.519   16.594 1.00 31.01  ? 16  LYS A C   1 
ATOM   95  O O   . LYS A 1 16 ? 3.200  5.093   15.562 1.00 32.72  ? 16  LYS A O   1 
ATOM   96  C CB  . LYS A 1 16 ? 2.276  5.106   18.587 1.00 33.55  ? 16  LYS A CB  1 
ATOM   97  C CG  . LYS A 1 16 ? 1.010  5.062   17.743 1.00 38.43  ? 16  LYS A CG  1 
ATOM   98  C CD  . LYS A 1 16 ? -0.286 5.254   18.534 1.00 41.84  ? 16  LYS A CD  1 
ATOM   99  C CE  . LYS A 1 16 ? -1.529 5.235   17.684 1.00 46.77  ? 16  LYS A CE  1 
ATOM   100 N NZ  . LYS A 1 16 ? -2.742 5.163   18.512 1.00 49.40  ? 16  LYS A NZ  1 
ATOM   101 N N   . TYR A 1 17 ? 4.333  6.711   16.657 1.00 29.97  ? 17  TYR A N   1 
ATOM   102 C CA  . TYR A 1 17 ? 4.304  7.640   15.537 1.00 33.40  ? 17  TYR A CA  1 
ATOM   103 C C   . TYR A 1 17 ? 5.595  7.571   14.727 1.00 33.05  ? 17  TYR A C   1 
ATOM   104 O O   . TYR A 1 17 ? 5.726  8.279   13.734 1.00 35.72  ? 17  TYR A O   1 
ATOM   105 C CB  . TYR A 1 17 ? 3.958  9.052   16.025 1.00 34.19  ? 17  TYR A CB  1 
ATOM   106 C CG  . TYR A 1 17 ? 2.552  9.090   16.596 1.00 35.56  ? 17  TYR A CG  1 
ATOM   107 C CD1 . TYR A 1 17 ? 1.445  9.115   15.761 1.00 37.61  ? 17  TYR A CD1 1 
ATOM   108 C CD2 . TYR A 1 17 ? 2.335  9.010   17.969 1.00 34.56  ? 17  TYR A CD2 1 
ATOM   109 C CE1 . TYR A 1 17 ? 0.159  9.103   16.271 1.00 39.63  ? 17  TYR A CE1 1 
ATOM   110 C CE2 . TYR A 1 17 ? 1.053  8.991   18.490 1.00 35.99  ? 17  TYR A CE2 1 
ATOM   111 C CZ  . TYR A 1 17 ? -0.033 9.038   17.639 1.00 38.89  ? 17  TYR A CZ  1 
ATOM   112 O OH  . TYR A 1 17 ? -1.278 9.024   18.183 1.00 43.36  ? 17  TYR A OH  1 
ATOM   113 N N   . LEU A 1 18 ? 6.508  6.668   15.090 1.00 30.79  ? 18  LEU A N   1 
ATOM   114 C CA  . LEU A 1 18 ? 7.678  6.437   14.259 1.00 31.88  ? 18  LEU A CA  1 
ATOM   115 C C   . LEU A 1 18 ? 7.265  5.656   13.018 1.00 33.58  ? 18  LEU A C   1 
ATOM   116 O O   . LEU A 1 18 ? 6.403  4.788   13.095 1.00 34.14  ? 18  LEU A O   1 
ATOM   117 C CB  . LEU A 1 18 ? 8.749  5.659   15.016 1.00 29.84  ? 18  LEU A CB  1 
ATOM   118 C CG  . LEU A 1 18 ? 9.467  6.396   16.148 1.00 30.68  ? 18  LEU A CG  1 
ATOM   119 C CD1 . LEU A 1 18 ? 10.530 5.441   16.645 1.00 30.63  ? 18  LEU A CD1 1 
ATOM   120 C CD2 . LEU A 1 18 ? 10.051 7.745   15.752 1.00 31.96  ? 18  LEU A CD2 1 
ATOM   121 N N   . PRO A 1 19 ? 7.926  5.866   11.863 1.00 35.14  ? 19  PRO A N   1 
ATOM   122 C CA  . PRO A 1 19 ? 7.746  4.964   10.728 1.00 37.57  ? 19  PRO A CA  1 
ATOM   123 C C   . PRO A 1 19 ? 7.980  3.507   11.123 1.00 37.23  ? 19  PRO A C   1 
ATOM   124 O O   . PRO A 1 19 ? 8.794  3.229   12.006 1.00 32.18  ? 19  PRO A O   1 
ATOM   125 C CB  . PRO A 1 19 ? 8.741  5.471   9.690  1.00 39.11  ? 19  PRO A CB  1 
ATOM   126 C CG  . PRO A 1 19 ? 9.065  6.897   10.115 1.00 37.96  ? 19  PRO A CG  1 
ATOM   127 C CD  . PRO A 1 19 ? 8.877  6.959   11.607 1.00 35.18  ? 19  PRO A CD  1 
ATOM   128 N N   . GLN A 1 20 ? 7.249  2.586   10.482 1.00 39.22  ? 20  GLN A N   1 
ATOM   129 C CA  . GLN A 1 20 ? 7.292  1.174   10.842 1.00 40.87  ? 20  GLN A CA  1 
ATOM   130 C C   . GLN A 1 20 ? 8.726  0.629   10.776 1.00 38.38  ? 20  GLN A C   1 
ATOM   131 O O   . GLN A 1 20 ? 9.143  -0.151  11.625 1.00 36.72  ? 20  GLN A O   1 
ATOM   132 C CB  . GLN A 1 20 ? 6.352  0.383   9.928  1.00 46.08  ? 20  GLN A CB  1 
ATOM   133 C CG  . GLN A 1 20 ? 6.111  -1.052  10.383 1.00 50.20  ? 20  GLN A CG  1 
ATOM   134 C CD  . GLN A 1 20 ? 5.499  -1.130  11.765 1.00 54.51  ? 20  GLN A CD  1 
ATOM   135 O OE1 . GLN A 1 20 ? 6.056  -1.728  12.695 1.00 57.75  ? 20  GLN A OE1 1 
ATOM   136 N NE2 . GLN A 1 20 ? 4.349  -0.491  11.923 1.00 57.94  ? 20  GLN A NE2 1 
ATOM   137 N N   . GLN A 1 21 ? 9.479  1.032   9.753  1.00 39.84  ? 21  GLN A N   1 
ATOM   138 C CA  . GLN A 1 21 ? 10.842 0.563   9.562  1.00 40.47  ? 21  GLN A CA  1 
ATOM   139 C C   . GLN A 1 21 ? 11.723 0.951   10.751 1.00 37.19  ? 21  GLN A C   1 
ATOM   140 O O   . GLN A 1 21 ? 12.627 0.212   11.140 1.00 36.77  ? 21  GLN A O   1 
ATOM   141 C CB  . GLN A 1 21 ? 11.353 1.165   8.254  1.00 44.83  ? 21  GLN A CB  1 
ATOM   142 C CG  . GLN A 1 21 ? 12.531 0.411   7.656  1.00 50.22  ? 21  GLN A CG  1 
ATOM   143 C CD  . GLN A 1 21 ? 13.135 1.104   6.453  1.00 56.19  ? 21  GLN A CD  1 
ATOM   144 O OE1 . GLN A 1 21 ? 12.783 2.244   6.121  1.00 62.18  ? 21  GLN A OE1 1 
ATOM   145 N NE2 . GLN A 1 21 ? 14.053 0.415   5.786  1.00 58.29  ? 21  GLN A NE2 1 
ATOM   146 N N   . GLN A 1 22 ? 11.469 2.137   11.316 1.00 35.01  ? 22  GLN A N   1 
ATOM   147 C CA  . GLN A 1 22 ? 12.225 2.624   12.457 1.00 32.67  ? 22  GLN A CA  1 
ATOM   148 C C   . GLN A 1 22 ? 11.794 1.899   13.725 1.00 30.85  ? 22  GLN A C   1 
ATOM   149 O O   . GLN A 1 22 ? 12.644 1.594   14.551 1.00 28.27  ? 22  GLN A O   1 
ATOM   150 C CB  . GLN A 1 22 ? 12.095 4.139   12.636 1.00 33.09  ? 22  GLN A CB  1 
ATOM   151 C CG  . GLN A 1 22 ? 12.772 4.931   11.524 1.00 35.20  ? 22  GLN A CG  1 
ATOM   152 C CD  . GLN A 1 22 ? 12.681 6.432   11.704 1.00 35.71  ? 22  GLN A CD  1 
ATOM   153 O OE1 . GLN A 1 22 ? 12.410 6.946   12.795 1.00 37.95  ? 22  GLN A OE1 1 
ATOM   154 N NE2 . GLN A 1 22 ? 12.917 7.144   10.620 1.00 37.10  ? 22  GLN A NE2 1 
ATOM   155 N N   . LYS A 1 23 ? 10.491 1.621   13.877 1.00 31.03  ? 23  LYS A N   1 
ATOM   156 C CA  . LYS A 1 23 ? 10.017 0.856   15.020 1.00 31.27  ? 23  LYS A CA  1 
ATOM   157 C C   . LYS A 1 23 ? 10.717 -0.498  15.039 1.00 31.15  ? 23  LYS A C   1 
ATOM   158 O O   . LYS A 1 23 ? 11.196 -0.940  16.084 1.00 32.08  ? 23  LYS A O   1 
ATOM   159 C CB  . LYS A 1 23 ? 8.503  0.603   14.998 1.00 34.20  ? 23  LYS A CB  1 
ATOM   160 C CG  . LYS A 1 23 ? 7.610  1.839   15.077 1.00 35.90  ? 23  LYS A CG  1 
ATOM   161 C CD  . LYS A 1 23 ? 6.130  1.517   14.853 1.00 38.42  ? 23  LYS A CD  1 
ATOM   162 C CE  . LYS A 1 23 ? 5.205  2.620   15.247 1.00 38.60  ? 23  LYS A CE  1 
ATOM   163 N NZ  . LYS A 1 23 ? 3.809  2.306   14.916 1.00 41.52  ? 23  LYS A NZ  1 
ATOM   164 N N   . LYS A 1 24 ? 10.746 -1.149  13.873 1.00 35.78  ? 24  LYS A N   1 
ATOM   165 C CA  . LYS A 1 24 ? 11.355 -2.461  13.739 1.00 38.62  ? 24  LYS A CA  1 
ATOM   166 C C   . LYS A 1 24 ? 12.859 -2.388  14.012 1.00 35.86  ? 24  LYS A C   1 
ATOM   167 O O   . LYS A 1 24 ? 13.406 -3.272  14.662 1.00 34.23  ? 24  LYS A O   1 
ATOM   168 C CB  . LYS A 1 24 ? 11.094 -3.057  12.353 1.00 43.53  ? 24  LYS A CB  1 
ATOM   169 C CG  . LYS A 1 24 ? 11.381 -4.551  12.286 1.00 51.54  ? 24  LYS A CG  1 
ATOM   170 C CD  . LYS A 1 24 ? 12.086 -5.026  11.023 1.00 59.07  ? 24  LYS A CD  1 
ATOM   171 C CE  . LYS A 1 24 ? 12.621 -6.425  11.151 1.00 64.36  ? 24  LYS A CE  1 
ATOM   172 N NZ  . LYS A 1 24 ? 13.725 -6.652  10.212 1.00 67.68  ? 24  LYS A NZ  1 
ATOM   173 N N   . LYS A 1 25 ? 13.529 -1.337  13.516 1.00 34.43  ? 25  LYS A N   1 
ATOM   174 C CA  . LYS A 1 25 ? 14.963 -1.173  13.724 1.00 31.28  ? 25  LYS A CA  1 
ATOM   175 C C   . LYS A 1 25 ? 15.290 -0.965  15.204 1.00 29.46  ? 25  LYS A C   1 
ATOM   176 O O   . LYS A 1 25 ? 16.323 -1.436  15.668 1.00 30.08  ? 25  LYS A O   1 
ATOM   177 C CB  . LYS A 1 25 ? 15.543 -0.042  12.867 1.00 30.78  ? 25  LYS A CB  1 
ATOM   178 C CG  . LYS A 1 25 ? 17.064 0.066   12.897 1.00 30.09  ? 25  LYS A CG  1 
ATOM   179 C CD  . LYS A 1 25 ? 17.777 -1.214  12.473 1.00 32.55  ? 25  LYS A CD  1 
ATOM   180 C CE  . LYS A 1 25 ? 19.233 -0.983  12.236 1.00 33.29  ? 25  LYS A CE  1 
ATOM   181 N NZ  . LYS A 1 25 ? 19.896 -2.221  11.847 1.00 35.89  ? 25  LYS A NZ  1 
ATOM   182 N N   . LEU A 1 26 ? 14.438 -0.242  15.939 1.00 27.29  ? 26  LEU A N   1 
ATOM   183 C CA  A LEU A 1 26 ? 14.618 -0.052  17.365 0.50 27.71  ? 26  LEU A CA  1 
ATOM   184 C CA  B LEU A 1 26 ? 14.613 -0.052  17.376 0.50 27.00  ? 26  LEU A CA  1 
ATOM   185 C C   . LEU A 1 26 ? 14.561 -1.407  18.069 1.00 28.04  ? 26  LEU A C   1 
ATOM   186 O O   . LEU A 1 26 ? 15.377 -1.696  18.931 1.00 28.44  ? 26  LEU A O   1 
ATOM   187 C CB  A LEU A 1 26 ? 13.504 0.887   17.820 0.50 27.35  ? 26  LEU A CB  1 
ATOM   188 C CB  B LEU A 1 26 ? 13.570 0.853   18.031 0.50 25.38  ? 26  LEU A CB  1 
ATOM   189 C CG  A LEU A 1 26 ? 13.759 1.710   19.081 0.50 25.87  ? 26  LEU A CG  1 
ATOM   190 C CG  B LEU A 1 26 ? 13.769 2.364   17.913 0.50 23.85  ? 26  LEU A CG  1 
ATOM   191 C CD1 A LEU A 1 26 ? 14.805 2.790   18.876 0.50 25.89  ? 26  LEU A CD1 1 
ATOM   192 C CD1 B LEU A 1 26 ? 12.546 3.059   18.460 0.50 23.85  ? 26  LEU A CD1 1 
ATOM   193 C CD2 A LEU A 1 26 ? 12.439 2.309   19.512 0.50 26.17  ? 26  LEU A CD2 1 
ATOM   194 C CD2 B LEU A 1 26 ? 15.019 2.832   18.637 0.50 23.63  ? 26  LEU A CD2 1 
ATOM   195 N N   . GLN A 1 27 ? 13.566 -2.215  17.699 1.00 29.84  ? 27  GLN A N   1 
ATOM   196 C CA  . GLN A 1 27 ? 13.363 -3.531  18.287 1.00 31.62  ? 27  GLN A CA  1 
ATOM   197 C C   . GLN A 1 27 ? 14.576 -4.423  18.028 1.00 33.22  ? 27  GLN A C   1 
ATOM   198 O O   . GLN A 1 27 ? 15.084 -5.056  18.954 1.00 34.84  ? 27  GLN A O   1 
ATOM   199 C CB  . GLN A 1 27 ? 12.087 -4.177  17.741 1.00 32.79  ? 27  GLN A CB  1 
ATOM   200 C CG  . GLN A 1 27 ? 10.793 -3.513  18.200 1.00 31.77  ? 27  GLN A CG  1 
ATOM   201 C CD  . GLN A 1 27 ? 9.582  -3.969  17.410 1.00 35.29  ? 27  GLN A CD  1 
ATOM   202 O OE1 . GLN A 1 27 ? 9.575  -5.038  16.789 1.00 37.64  ? 27  GLN A OE1 1 
ATOM   203 N NE2 . GLN A 1 27 ? 8.538  -3.157  17.410 1.00 35.06  ? 27  GLN A NE2 1 
ATOM   204 N N   . THR A 1 28 ? 15.040 -4.489  16.773 1.00 33.05  ? 28  THR A N   1 
ATOM   205 C CA  . THR A 1 28 ? 16.140 -5.382  16.437 1.00 34.58  ? 28  THR A CA  1 
ATOM   206 C C   . THR A 1 28 ? 17.439 -4.884  17.079 1.00 34.33  ? 28  THR A C   1 
ATOM   207 O O   . THR A 1 28 ? 18.259 -5.689  17.517 1.00 33.89  ? 28  THR A O   1 
ATOM   208 C CB  . THR A 1 28 ? 16.263 -5.571  14.925 1.00 36.90  ? 28  THR A CB  1 
ATOM   209 O OG1 . THR A 1 28 ? 16.419 -4.318  14.263 1.00 37.27  ? 28  THR A OG1 1 
ATOM   210 C CG2 . THR A 1 28 ? 15.058 -6.301  14.354 1.00 38.92  ? 28  THR A CG2 1 
ATOM   211 N N   . ASP A 1 29 ? 17.627 -3.558  17.153 1.00 31.49  ? 29  ASP A N   1 
ATOM   212 C CA  . ASP A 1 29 ? 18.795 -2.987  17.809 1.00 30.65  ? 29  ASP A CA  1 
ATOM   213 C C   . ASP A 1 29 ? 18.835 -3.399  19.278 1.00 31.63  ? 29  ASP A C   1 
ATOM   214 O O   . ASP A 1 29 ? 19.905 -3.665  19.823 1.00 31.51  ? 29  ASP A O   1 
ATOM   215 C CB  . ASP A 1 29 ? 18.814 -1.470  17.719 1.00 28.32  ? 29  ASP A CB  1 
ATOM   216 C CG  . ASP A 1 29 ? 19.354 -0.863  16.435 1.00 28.24  ? 29  ASP A CG  1 
ATOM   217 O OD1 . ASP A 1 29 ? 19.776 -1.626  15.544 1.00 30.55  ? 29  ASP A OD1 1 
ATOM   218 O OD2 . ASP A 1 29 ? 19.395 0.384   16.372 1.00 27.86  ? 29  ASP A OD2 1 
ATOM   219 N N   . ILE A 1 30 ? 17.658 -3.411  19.913 1.00 30.85  ? 30  ILE A N   1 
ATOM   220 C CA  . ILE A 1 30 ? 17.521 -3.805  21.303 1.00 32.72  ? 30  ILE A CA  1 
ATOM   221 C C   . ILE A 1 30 ? 17.792 -5.306  21.440 1.00 33.93  ? 30  ILE A C   1 
ATOM   222 O O   . ILE A 1 30 ? 18.645 -5.694  22.226 1.00 36.08  ? 30  ILE A O   1 
ATOM   223 C CB  . ILE A 1 30 ? 16.136 -3.389  21.836 1.00 32.58  ? 30  ILE A CB  1 
ATOM   224 C CG1 . ILE A 1 30 ? 16.057 -1.865  22.051 1.00 30.03  ? 30  ILE A CG1 1 
ATOM   225 C CG2 . ILE A 1 30 ? 15.784 -4.164  23.106 1.00 35.13  ? 30  ILE A CG2 1 
ATOM   226 C CD1 . ILE A 1 30 ? 14.655 -1.322  22.266 1.00 29.87  ? 30  ILE A CD1 1 
ATOM   227 N N   . GLN A 1 31 ? 17.091 -6.134  20.654 1.00 36.49  ? 31  GLN A N   1 
ATOM   228 C CA  . GLN A 1 31 ? 17.191 -7.588  20.748 1.00 42.05  ? 31  GLN A CA  1 
ATOM   229 C C   . GLN A 1 31 ? 18.600 -8.093  20.444 1.00 41.73  ? 31  GLN A C   1 
ATOM   230 O O   . GLN A 1 31 ? 19.069 -9.035  21.080 1.00 45.61  ? 31  GLN A O   1 
ATOM   231 C CB  . GLN A 1 31 ? 16.299 -8.305  19.734 1.00 48.72  ? 31  GLN A CB  1 
ATOM   232 C CG  . GLN A 1 31 ? 14.810 -8.160  20.015 1.00 53.98  ? 31  GLN A CG  1 
ATOM   233 C CD  . GLN A 1 31 ? 13.921 -8.768  18.946 1.00 61.45  ? 31  GLN A CD  1 
ATOM   234 O OE1 . GLN A 1 31 ? 13.841 -8.285  17.806 1.00 63.71  ? 31  GLN A OE1 1 
ATOM   235 N NE2 . GLN A 1 31 ? 13.209 -9.820  19.327 1.00 62.45  ? 31  GLN A NE2 1 
ATOM   236 N N   . GLU A 1 32 ? 19.231 -7.526  19.414 1.00 40.11  ? 32  GLU A N   1 
ATOM   237 C CA  . GLU A 1 32 ? 20.522 -8.003  18.940 1.00 43.55  ? 32  GLU A CA  1 
ATOM   238 C C   . GLU A 1 32 ? 21.654 -7.628  19.901 1.00 42.73  ? 32  GLU A C   1 
ATOM   239 O O   . GLU A 1 32 ? 22.775 -8.112  19.753 1.00 43.70  ? 32  GLU A O   1 
ATOM   240 C CB  . GLU A 1 32 ? 20.835 -7.433  17.558 1.00 43.32  ? 32  GLU A CB  1 
ATOM   241 C CG  . GLU A 1 32 ? 20.007 -8.039  16.427 1.00 46.18  ? 32  GLU A CG  1 
ATOM   242 C CD  . GLU A 1 32 ? 20.027 -7.209  15.150 1.00 47.53  ? 32  GLU A CD  1 
ATOM   243 O OE1 . GLU A 1 32 ? 20.701 -6.156  15.106 1.00 46.35  ? 32  GLU A OE1 1 
ATOM   244 O OE2 . GLU A 1 32 ? 19.341 -7.607  14.193 1.00 51.97  ? 32  GLU A OE2 1 
ATOM   245 N N   . ASN A 1 33 ? 21.378 -6.743  20.865 1.00 40.81  ? 33  ASN A N   1 
ATOM   246 C CA  . ASN A 1 33 ? 22.403 -6.261  21.777 1.00 40.68  ? 33  ASN A CA  1 
ATOM   247 C C   . ASN A 1 33 ? 22.000 -6.527  23.225 1.00 41.26  ? 33  ASN A C   1 
ATOM   248 O O   . ASN A 1 33 ? 22.367 -5.760  24.115 1.00 40.56  ? 33  ASN A O   1 
ATOM   249 C CB  . ASN A 1 33 ? 22.695 -4.789  21.525 1.00 39.29  ? 33  ASN A CB  1 
ATOM   250 C CG  . ASN A 1 33 ? 23.289 -4.561  20.160 1.00 41.11  ? 33  ASN A CG  1 
ATOM   251 O OD1 . ASN A 1 33 ? 24.508 -4.674  20.003 1.00 45.61  ? 33  ASN A OD1 1 
ATOM   252 N ND2 . ASN A 1 33 ? 22.466 -4.222  19.174 1.00 40.25  ? 33  ASN A ND2 1 
ATOM   253 N N   . GLY A 1 34 ? 21.262 -7.628  23.448 1.00 41.02  ? 34  GLY A N   1 
ATOM   254 C CA  . GLY A 1 34 ? 21.131 -8.222  24.766 1.00 42.41  ? 34  GLY A CA  1 
ATOM   255 C C   . GLY A 1 34 ? 19.874 -7.765  25.504 1.00 40.89  ? 34  GLY A C   1 
ATOM   256 O O   . GLY A 1 34 ? 19.588 -8.271  26.580 1.00 42.43  ? 34  GLY A O   1 
ATOM   257 N N   . GLY A 1 35 ? 19.120 -6.830  24.923 1.00 37.03  ? 35  GLY A N   1 
ATOM   258 C CA  . GLY A 1 35 ? 17.978 -6.235  25.606 1.00 37.65  ? 35  GLY A CA  1 
ATOM   259 C C   . GLY A 1 35 ? 16.679 -6.977  25.306 1.00 38.13  ? 35  GLY A C   1 
ATOM   260 O O   . GLY A 1 35 ? 16.653 -7.877  24.468 1.00 38.10  ? 35  GLY A O   1 
ATOM   261 N N   . LYS A 1 36 ? 15.614 -6.599  26.026 1.00 38.42  ? 36  LYS A N   1 
ATOM   262 C CA  . LYS A 1 36 ? 14.267 -7.074  25.754 1.00 40.09  ? 36  LYS A CA  1 
ATOM   263 C C   . LYS A 1 36 ? 13.344 -5.863  25.670 1.00 36.40  ? 36  LYS A C   1 
ATOM   264 O O   . LYS A 1 36 ? 13.669 -4.790  26.181 1.00 34.16  ? 36  LYS A O   1 
ATOM   265 C CB  . LYS A 1 36 ? 13.782 -8.048  26.835 1.00 44.16  ? 36  LYS A CB  1 
ATOM   266 C CG  . LYS A 1 36 ? 14.622 -9.305  26.972 1.00 49.88  ? 36  LYS A CG  1 
ATOM   267 C CD  . LYS A 1 36 ? 14.056 -10.285 27.986 1.00 57.19  ? 36  LYS A CD  1 
ATOM   268 C CE  . LYS A 1 36 ? 14.893 -11.526 28.074 1.00 62.88  ? 36  LYS A CE  1 
ATOM   269 N NZ  . LYS A 1 36 ? 14.187 -12.584 28.796 1.00 69.19  ? 36  LYS A NZ  1 
ATOM   270 N N   . PHE A 1 37 ? 12.199 -6.030  24.998 1.00 35.80  ? 37  PHE A N   1 
ATOM   271 C CA  . PHE A 1 37 ? 11.270 -4.920  24.856 1.00 32.85  ? 37  PHE A CA  1 
ATOM   272 C C   . PHE A 1 37 ? 9.846  -5.420  25.074 1.00 34.64  ? 37  PHE A C   1 
ATOM   273 O O   . PHE A 1 37 ? 9.562  -6.607  24.905 1.00 35.63  ? 37  PHE A O   1 
ATOM   274 C CB  . PHE A 1 37 ? 11.413 -4.193  23.512 1.00 31.48  ? 37  PHE A CB  1 
ATOM   275 C CG  . PHE A 1 37 ? 11.133 -5.043  22.278 1.00 34.27  ? 37  PHE A CG  1 
ATOM   276 C CD1 . PHE A 1 37 ? 9.830  -5.221  21.810 1.00 35.63  ? 37  PHE A CD1 1 
ATOM   277 C CD2 . PHE A 1 37 ? 12.168 -5.651  21.581 1.00 35.16  ? 37  PHE A CD2 1 
ATOM   278 C CE1 . PHE A 1 37 ? 9.572  -6.011  20.693 1.00 37.57  ? 37  PHE A CE1 1 
ATOM   279 C CE2 . PHE A 1 37 ? 11.903 -6.439  20.465 1.00 37.71  ? 37  PHE A CE2 1 
ATOM   280 C CZ  . PHE A 1 37 ? 10.609 -6.616  20.022 1.00 38.21  ? 37  PHE A CZ  1 
ATOM   281 N N   A SER A 1 38 ? 8.988  -4.496  25.513 0.50 33.74  ? 38  SER A N   1 
ATOM   282 N N   B SER A 1 38 ? 8.969  -4.465  25.403 0.50 32.95  ? 38  SER A N   1 
ATOM   283 C CA  A SER A 1 38 ? 7.559  -4.711  25.643 0.50 35.97  ? 38  SER A CA  1 
ATOM   284 C CA  B SER A 1 38 ? 7.568  -4.691  25.708 0.50 34.74  ? 38  SER A CA  1 
ATOM   285 C C   A SER A 1 38 ? 6.847  -3.487  25.079 0.50 34.12  ? 38  SER A C   1 
ATOM   286 C C   B SER A 1 38 ? 6.783  -3.444  25.305 0.50 33.72  ? 38  SER A C   1 
ATOM   287 O O   A SER A 1 38 ? 7.470  -2.448  24.870 0.50 32.53  ? 38  SER A O   1 
ATOM   288 O O   B SER A 1 38 ? 7.289  -2.328  25.440 0.50 32.15  ? 38  SER A O   1 
ATOM   289 C CB  A SER A 1 38 ? 7.165  -4.938  27.074 0.50 37.64  ? 38  SER A CB  1 
ATOM   290 C CB  B SER A 1 38 ? 7.394  -5.007  27.172 0.50 35.74  ? 38  SER A CB  1 
ATOM   291 O OG  A SER A 1 38 ? 7.465  -3.792  27.860 0.50 36.86  ? 38  SER A OG  1 
ATOM   292 O OG  B SER A 1 38 ? 6.061  -4.791  27.615 0.50 34.81  ? 38  SER A OG  1 
ATOM   293 N N   . PHE A 1 39 ? 5.547  -3.627  24.829 1.00 34.09  ? 39  PHE A N   1 
ATOM   294 C CA  . PHE A 1 39 ? 4.710  -2.490  24.471 1.00 34.93  ? 39  PHE A CA  1 
ATOM   295 C C   . PHE A 1 39 ? 3.952  -1.990  25.700 1.00 35.94  ? 39  PHE A C   1 
ATOM   296 O O   . PHE A 1 39 ? 3.367  -0.916  25.661 1.00 37.91  ? 39  PHE A O   1 
ATOM   297 C CB  . PHE A 1 39 ? 3.836  -2.907  23.284 1.00 37.66  ? 39  PHE A CB  1 
ATOM   298 C CG  . PHE A 1 39 ? 4.699  -3.226  22.073 1.00 38.34  ? 39  PHE A CG  1 
ATOM   299 C CD1 . PHE A 1 39 ? 5.426  -2.224  21.437 1.00 39.48  ? 39  PHE A CD1 1 
ATOM   300 C CD2 . PHE A 1 39 ? 4.810  -4.529  21.595 1.00 43.03  ? 39  PHE A CD2 1 
ATOM   301 C CE1 . PHE A 1 39 ? 6.234  -2.519  20.348 1.00 40.26  ? 39  PHE A CE1 1 
ATOM   302 C CE2 . PHE A 1 39 ? 5.613  -4.812  20.498 1.00 42.97  ? 39  PHE A CE2 1 
ATOM   303 C CZ  . PHE A 1 39 ? 6.317  -3.809  19.880 1.00 40.84  ? 39  PHE A CZ  1 
ATOM   304 N N   . SER A 1 40 ? 4.006  -2.755  26.797 1.00 35.50  ? 40  SER A N   1 
ATOM   305 C CA  . SER A 1 40 ? 3.339  -2.399  28.039 1.00 35.59  ? 40  SER A CA  1 
ATOM   306 C C   . SER A 1 40 ? 4.360  -1.919  29.067 1.00 35.01  ? 40  SER A C   1 
ATOM   307 O O   . SER A 1 40 ? 5.504  -2.382  29.073 1.00 33.33  ? 40  SER A O   1 
ATOM   308 C CB  . SER A 1 40 ? 2.572  -3.584  28.580 1.00 37.60  ? 40  SER A CB  1 
ATOM   309 O OG  . SER A 1 40 ? 1.705  -4.111  27.585 1.00 40.70  ? 40  SER A OG  1 
ATOM   310 N N   . LEU A 1 41 ? 3.916  -0.997  29.934 1.00 33.26  ? 41  LEU A N   1 
ATOM   311 C CA  . LEU A 1 41 ? 4.718  -0.513  31.048 1.00 33.91  ? 41  LEU A CA  1 
ATOM   312 C C   . LEU A 1 41 ? 4.353  -1.319  32.292 1.00 34.34  ? 41  LEU A C   1 
ATOM   313 O O   . LEU A 1 41 ? 3.191  -1.377  32.675 1.00 33.26  ? 41  LEU A O   1 
ATOM   314 C CB  . LEU A 1 41 ? 4.455  0.985   31.231 1.00 33.60  ? 41  LEU A CB  1 
ATOM   315 C CG  . LEU A 1 41 ? 5.068  1.643   32.471 1.00 35.56  ? 41  LEU A CG  1 
ATOM   316 C CD1 . LEU A 1 41 ? 6.595  1.600   32.413 1.00 34.42  ? 41  LEU A CD1 1 
ATOM   317 C CD2 . LEU A 1 41 ? 4.554  3.062   32.633 1.00 35.70  ? 41  LEU A CD2 1 
ATOM   318 N N   . ASN A 1 42 ? 5.354  -1.946  32.916 1.00 34.11  ? 42  ASN A N   1 
ATOM   319 C CA  . ASN A 1 42 ? 5.142  -2.734  34.119 1.00 37.98  ? 42  ASN A CA  1 
ATOM   320 C C   . ASN A 1 42 ? 6.358  -2.577  35.036 1.00 37.58  ? 42  ASN A C   1 
ATOM   321 O O   . ASN A 1 42 ? 7.369  -2.018  34.616 1.00 34.94  ? 42  ASN A O   1 
ATOM   322 C CB  . ASN A 1 42 ? 4.846  -4.192  33.777 1.00 40.96  ? 42  ASN A CB  1 
ATOM   323 C CG  . ASN A 1 42 ? 5.936  -4.811  32.935 1.00 44.22  ? 42  ASN A CG  1 
ATOM   324 O OD1 . ASN A 1 42 ? 7.124  -4.727  33.275 1.00 44.69  ? 42  ASN A OD1 1 
ATOM   325 N ND2 . ASN A 1 42 ? 5.552  -5.422  31.824 1.00 46.72  ? 42  ASN A ND2 1 
ATOM   326 N N   . PRO A 1 43 ? 6.293  -3.044  36.302 1.00 40.97  ? 43  PRO A N   1 
ATOM   327 C CA  . PRO A 1 43 ? 7.402  -2.901  37.244 1.00 42.64  ? 43  PRO A CA  1 
ATOM   328 C C   . PRO A 1 43 ? 8.759  -3.439  36.783 1.00 44.03  ? 43  PRO A C   1 
ATOM   329 O O   . PRO A 1 43 ? 9.787  -2.999  37.299 1.00 43.72  ? 43  PRO A O   1 
ATOM   330 C CB  . PRO A 1 43 ? 6.917  -3.651  38.487 1.00 46.21  ? 43  PRO A CB  1 
ATOM   331 C CG  . PRO A 1 43 ? 5.408  -3.565  38.392 1.00 46.16  ? 43  PRO A CG  1 
ATOM   332 C CD  . PRO A 1 43 ? 5.101  -3.642  36.928 1.00 43.29  ? 43  PRO A CD  1 
ATOM   333 N N   . GLN A 1 44 ? 8.770  -4.388  35.833 1.00 45.41  ? 44  GLN A N   1 
ATOM   334 C CA  . GLN A 1 44 ? 10.009 -4.993  35.355 1.00 45.31  ? 44  GLN A CA  1 
ATOM   335 C C   . GLN A 1 44 ? 10.713 -4.129  34.306 1.00 41.51  ? 44  GLN A C   1 
ATOM   336 O O   . GLN A 1 44 ? 11.868 -4.400  33.984 1.00 40.90  ? 44  GLN A O   1 
ATOM   337 C CB  . GLN A 1 44 ? 9.792  -6.385  34.756 1.00 48.20  ? 44  GLN A CB  1 
ATOM   338 C CG  . GLN A 1 44 ? 9.593  -7.488  35.789 1.00 54.22  ? 44  GLN A CG  1 
ATOM   339 C CD  . GLN A 1 44 ? 8.319  -7.319  36.586 1.00 58.00  ? 44  GLN A CD  1 
ATOM   340 O OE1 . GLN A 1 44 ? 7.224  -7.168  36.030 1.00 58.33  ? 44  GLN A OE1 1 
ATOM   341 N NE2 . GLN A 1 44 ? 8.454  -7.326  37.904 1.00 61.97  ? 44  GLN A NE2 1 
ATOM   342 N N   . CYS A 1 45 ? 10.042 -3.109  33.747 1.00 37.62  ? 45  CYS A N   1 
ATOM   343 C CA  . CYS A 1 45 ? 10.698 -2.234  32.777 1.00 33.23  ? 45  CYS A CA  1 
ATOM   344 C C   . CYS A 1 45 ? 11.838 -1.478  33.472 1.00 35.15  ? 45  CYS A C   1 
ATOM   345 O O   . CYS A 1 45 ? 11.693 -1.073  34.621 1.00 37.29  ? 45  CYS A O   1 
ATOM   346 C CB  . CYS A 1 45 ? 9.709  -1.299  32.082 1.00 31.02  ? 45  CYS A CB  1 
ATOM   347 S SG  . CYS A 1 45 ? 8.478  -2.158  31.064 0.47 25.00  ? 45  CYS A SG  1 
ATOM   348 N N   . THR A 1 46 ? 12.988 -1.350  32.796 1.00 33.90  ? 46  THR A N   1 
ATOM   349 C CA  . THR A 1 46 ? 14.086 -0.525  33.284 1.00 34.94  ? 46  THR A CA  1 
ATOM   350 C C   . THR A 1 46 ? 14.045 0.849   32.623 1.00 32.93  ? 46  THR A C   1 
ATOM   351 O O   . THR A 1 46 ? 14.525 1.836   33.193 1.00 31.63  ? 46  THR A O   1 
ATOM   352 C CB  . THR A 1 46 ? 15.425 -1.229  33.050 1.00 35.90  ? 46  THR A CB  1 
ATOM   353 O OG1 . THR A 1 46 ? 15.605 -1.523  31.667 1.00 35.29  ? 46  THR A OG1 1 
ATOM   354 C CG2 . THR A 1 46 ? 15.528 -2.499  33.876 1.00 39.57  ? 46  THR A CG2 1 
ATOM   355 N N   . HIS A 1 47 ? 13.482 0.885   31.406 1.00 30.17  ? 47  HIS A N   1 
ATOM   356 C CA  . HIS A 1 47 ? 13.481 2.066   30.565 1.00 29.99  ? 47  HIS A CA  1 
ATOM   357 C C   . HIS A 1 47 ? 12.138 2.154   29.848 1.00 29.52  ? 47  HIS A C   1 
ATOM   358 O O   . HIS A 1 47 ? 11.493 1.127   29.609 1.00 29.65  ? 47  HIS A O   1 
ATOM   359 C CB  . HIS A 1 47 ? 14.530 1.950   29.457 1.00 30.10  ? 47  HIS A CB  1 
ATOM   360 C CG  . HIS A 1 47 ? 15.948 1.915   29.916 1.00 31.71  ? 47  HIS A CG  1 
ATOM   361 N ND1 . HIS A 1 47 ? 16.492 0.852   30.602 1.00 31.75  ? 47  HIS A ND1 1 
ATOM   362 C CD2 . HIS A 1 47 ? 16.920 2.823   29.790 1.00 32.19  ? 47  HIS A CD2 1 
ATOM   363 C CE1 . HIS A 1 47 ? 17.767 1.114   30.864 1.00 34.33  ? 47  HIS A CE1 1 
ATOM   364 N NE2 . HIS A 1 47 ? 18.053 2.306   30.371 1.00 33.02  ? 47  HIS A NE2 1 
ATOM   365 N N   . ILE A 1 48 ? 11.729 3.384   29.526 1.00 30.78  ? 48  ILE A N   1 
ATOM   366 C CA  . ILE A 1 48 ? 10.638 3.602   28.588 1.00 28.55  ? 48  ILE A CA  1 
ATOM   367 C C   . ILE A 1 48 ? 11.133 4.553   27.501 1.00 27.18  ? 48  ILE A C   1 
ATOM   368 O O   . ILE A 1 48 ? 11.624 5.644   27.796 1.00 27.10  ? 48  ILE A O   1 
ATOM   369 C CB  . ILE A 1 48 ? 9.352  4.107   29.284 1.00 29.82  ? 48  ILE A CB  1 
ATOM   370 C CG1 . ILE A 1 48 ? 8.212  4.293   28.275 1.00 30.33  ? 48  ILE A CG1 1 
ATOM   371 C CG2 . ILE A 1 48 ? 9.575  5.383   30.084 1.00 30.10  ? 48  ILE A CG2 1 
ATOM   372 C CD1 . ILE A 1 48 ? 6.854  4.531   28.923 1.00 31.87  ? 48  ILE A CD1 1 
ATOM   373 N N   . ILE A 1 49 ? 10.992 4.116   26.242 1.00 26.81  ? 49  ILE A N   1 
ATOM   374 C CA  . ILE A 1 49 ? 11.386 4.904   25.083 1.00 25.42  ? 49  ILE A CA  1 
ATOM   375 C C   . ILE A 1 49 ? 10.135 5.587   24.540 1.00 25.93  ? 49  ILE A C   1 
ATOM   376 O O   . ILE A 1 49 ? 9.169  4.906   24.198 1.00 25.25  ? 49  ILE A O   1 
ATOM   377 C CB  . ILE A 1 49 ? 12.045 4.036   23.995 1.00 24.66  ? 49  ILE A CB  1 
ATOM   378 C CG1 . ILE A 1 49 ? 13.232 3.212   24.527 1.00 26.18  ? 49  ILE A CG1 1 
ATOM   379 C CG2 . ILE A 1 49 ? 12.425 4.883   22.773 1.00 24.13  ? 49  ILE A CG2 1 
ATOM   380 C CD1 . ILE A 1 49 ? 14.341 4.013   25.187 1.00 25.03  ? 49  ILE A CD1 1 
ATOM   381 N N   A LEU A 1 50 ? 10.201 6.912   24.405 0.50 24.82  ? 50  LEU A N   1 
ATOM   382 N N   B LEU A 1 50 ? 10.162 6.930   24.550 0.50 26.32  ? 50  LEU A N   1 
ATOM   383 C CA  A LEU A 1 50 ? 9.047  7.724   24.080 0.50 25.01  ? 50  LEU A CA  1 
ATOM   384 C CA  B LEU A 1 50 ? 9.083  7.793   24.094 0.50 27.27  ? 50  LEU A CA  1 
ATOM   385 C C   A LEU A 1 50 ? 9.404  8.641   22.920 0.50 25.82  ? 50  LEU A C   1 
ATOM   386 C C   B LEU A 1 50 ? 9.531  8.516   22.833 0.50 27.04  ? 50  LEU A C   1 
ATOM   387 O O   A LEU A 1 50 ? 10.272 9.500   23.070 0.50 24.94  ? 50  LEU A O   1 
ATOM   388 O O   B LEU A 1 50 ? 10.574 9.160   22.837 0.50 26.87  ? 50  LEU A O   1 
ATOM   389 C CB  A LEU A 1 50 ? 8.685  8.510   25.339 0.50 25.23  ? 50  LEU A CB  1 
ATOM   390 C CB  B LEU A 1 50 ? 8.743  8.855   25.139 0.50 29.26  ? 50  LEU A CB  1 
ATOM   391 C CG  A LEU A 1 50 ? 7.503  9.474   25.225 0.50 25.54  ? 50  LEU A CG  1 
ATOM   392 C CG  B LEU A 1 50 ? 7.643  8.549   26.156 0.50 30.46  ? 50  LEU A CG  1 
ATOM   393 C CD1 A LEU A 1 50 ? 6.185  8.726   25.279 0.50 25.79  ? 50  LEU A CD1 1 
ATOM   394 C CD1 B LEU A 1 50 ? 7.315  9.843   26.876 0.50 32.17  ? 50  LEU A CD1 1 
ATOM   395 C CD2 A LEU A 1 50 ? 7.568  10.525  26.314 0.50 26.92  ? 50  LEU A CD2 1 
ATOM   396 C CD2 B LEU A 1 50 ? 6.397  7.963   25.531 0.50 30.65  ? 50  LEU A CD2 1 
ATOM   397 N N   . ASP A 1 51 ? 8.706  8.479   21.785 1.00 28.21  ? 51  ASP A N   1 
ATOM   398 C CA  . ASP A 1 51 ? 8.920  9.352   20.637 1.00 27.91  ? 51  ASP A CA  1 
ATOM   399 C C   . ASP A 1 51 ? 8.262  10.688  20.954 1.00 28.79  ? 51  ASP A C   1 
ATOM   400 O O   . ASP A 1 51 ? 7.507  10.791  21.916 1.00 28.41  ? 51  ASP A O   1 
ATOM   401 C CB  . ASP A 1 51 ? 8.492  8.700   19.330 1.00 27.85  ? 51  ASP A CB  1 
ATOM   402 C CG  . ASP A 1 51 ? 7.004  8.468   19.167 1.00 29.16  ? 51  ASP A CG  1 
ATOM   403 O OD1 . ASP A 1 51 ? 6.276  8.624   20.162 1.00 29.66  ? 51  ASP A OD1 1 
ATOM   404 O OD2 . ASP A 1 51 ? 6.590  8.145   18.041 1.00 31.96  ? 51  ASP A OD2 1 
ATOM   405 N N   . ASN A 1 52 ? 8.528  11.711  20.134 1.00 31.35  ? 52  ASN A N   1 
ATOM   406 C CA  . ASN A 1 52 ? 8.165  13.076  20.497 1.00 33.21  ? 52  ASN A CA  1 
ATOM   407 C C   . ASN A 1 52 ? 6.644  13.283  20.492 1.00 31.57  ? 52  ASN A C   1 
ATOM   408 O O   . ASN A 1 52 ? 6.159  14.088  21.275 1.00 30.51  ? 52  ASN A O   1 
ATOM   409 C CB  . ASN A 1 52 ? 8.851  14.128  19.626 1.00 39.36  ? 52  ASN A CB  1 
ATOM   410 C CG  . ASN A 1 52 ? 10.272 14.446  20.049 1.00 43.95  ? 52  ASN A CG  1 
ATOM   411 O OD1 . ASN A 1 52 ? 10.837 13.833  20.968 1.00 45.26  ? 52  ASN A OD1 1 
ATOM   412 N ND2 . ASN A 1 52 ? 10.881 15.406  19.372 1.00 49.76  ? 52  ASN A ND2 1 
ATOM   413 N N   . ALA A 1 53 ? 5.906  12.564  19.628 1.00 30.38  ? 53  ALA A N   1 
ATOM   414 C CA  . ALA A 1 53 ? 4.461  12.725  19.503 1.00 32.20  ? 53  ALA A CA  1 
ATOM   415 C C   . ALA A 1 53 ? 3.672  11.939  20.559 1.00 31.24  ? 53  ALA A C   1 
ATOM   416 O O   . ALA A 1 53 ? 2.466  12.138  20.683 1.00 31.87  ? 53  ALA A O   1 
ATOM   417 C CB  . ALA A 1 53 ? 4.029  12.341  18.096 1.00 32.82  ? 53  ALA A CB  1 
ATOM   418 N N   . ASP A 1 54 ? 4.311  11.042  21.316 0.76 29.90  ? 54  ASP A N   1 
ATOM   419 C CA  . ASP A 1 54 ? 3.610  10.306  22.361 1.00 30.83  ? 54  ASP A CA  1 
ATOM   420 C C   . ASP A 1 54 ? 3.711  11.047  23.697 0.76 32.27  ? 54  ASP A C   1 
ATOM   421 O O   . ASP A 1 54 ? 4.679  11.753  23.948 0.76 30.13  ? 54  ASP A O   1 
ATOM   422 C CB  . ASP A 1 54 ? 4.104  8.873   22.451 1.00 31.90  ? 54  ASP A CB  1 
ATOM   423 C CG  . ASP A 1 54 ? 3.499  7.940   21.411 1.00 35.99  ? 54  ASP A CG  1 
ATOM   424 O OD1 . ASP A 1 54 ? 2.265  7.735   21.478 1.00 44.79  ? 54  ASP A OD1 1 
ATOM   425 O OD2 . ASP A 1 54 ? 4.226  7.505   20.502 1.00 31.36  ? 54  ASP A OD2 1 
ATOM   426 N N   . VAL A 1 55 ? 2.702  10.869  24.560 1.00 34.80  ? 55  VAL A N   1 
ATOM   427 C CA  . VAL A 1 55 ? 2.701  11.450  25.899 1.00 36.53  ? 55  VAL A CA  1 
ATOM   428 C C   . VAL A 1 55 ? 2.393  10.346  26.908 1.00 36.50  ? 55  VAL A C   1 
ATOM   429 O O   . VAL A 1 55 ? 1.970  9.257   26.530 1.00 36.70  ? 55  VAL A O   1 
ATOM   430 C CB  . VAL A 1 55 ? 1.715  12.621  26.068 1.00 41.84  ? 55  VAL A CB  1 
ATOM   431 C CG1 . VAL A 1 55 ? 1.992  13.731  25.061 1.00 43.58  ? 55  VAL A CG1 1 
ATOM   432 C CG2 . VAL A 1 55 ? 0.249  12.184  25.986 1.00 43.26  ? 55  VAL A CG2 1 
ATOM   433 N N   . LEU A 1 56 ? 2.639  10.655  28.184 1.00 35.50  ? 56  LEU A N   1 
ATOM   434 C CA  . LEU A 1 56 ? 2.404  9.744   29.288 1.00 36.05  ? 56  LEU A CA  1 
ATOM   435 C C   . LEU A 1 56 ? 1.411  10.383  30.251 1.00 39.18  ? 56  LEU A C   1 
ATOM   436 O O   . LEU A 1 56 ? 1.472  11.585  30.505 1.00 39.98  ? 56  LEU A O   1 
ATOM   437 C CB  . LEU A 1 56 ? 3.738  9.442   29.968 1.00 37.35  ? 56  LEU A CB  1 
ATOM   438 C CG  . LEU A 1 56 ? 4.757  8.667   29.132 1.00 36.30  ? 56  LEU A CG  1 
ATOM   439 C CD1 . LEU A 1 56 ? 6.098  8.602   29.854 1.00 37.65  ? 56  LEU A CD1 1 
ATOM   440 C CD2 . LEU A 1 56 ? 4.260  7.265   28.798 1.00 36.18  ? 56  LEU A CD2 1 
ATOM   441 N N   . SER A 1 57 ? 0.481  9.562   30.753 1.00 37.51  ? 57  SER A N   1 
ATOM   442 C CA  . SER A 1 57 ? -0.467 9.976   31.769 1.00 38.53  ? 57  SER A CA  1 
ATOM   443 C C   . SER A 1 57 ? 0.259  10.165  33.097 1.00 38.62  ? 57  SER A C   1 
ATOM   444 O O   . SER A 1 57 ? 1.389  9.708   33.279 1.00 36.64  ? 57  SER A O   1 
ATOM   445 C CB  . SER A 1 57 ? -1.595 8.964   31.909 1.00 37.61  ? 57  SER A CB  1 
ATOM   446 O OG  . SER A 1 57 ? -1.088 7.736   32.416 1.00 35.20  ? 57  SER A OG  1 
ATOM   447 N N   . GLN A 1 58 ? -0.428 10.818  34.035 1.00 40.62  ? 58  GLN A N   1 
ATOM   448 C CA  . GLN A 1 58 ? 0.095  10.978  35.378 1.00 43.75  ? 58  GLN A CA  1 
ATOM   449 C C   . GLN A 1 58 ? 0.255  9.599   36.018 1.00 43.21  ? 58  GLN A C   1 
ATOM   450 O O   . GLN A 1 58 ? 1.216  9.373   36.753 1.00 43.33  ? 58  GLN A O   1 
ATOM   451 C CB  . GLN A 1 58 ? -0.805 11.883  36.226 1.00 47.47  ? 58  GLN A CB  1 
ATOM   452 C CG  . GLN A 1 58 ? -0.180 12.269  37.563 1.00 51.21  ? 58  GLN A CG  1 
ATOM   453 C CD  . GLN A 1 58 ? 1.194  12.888  37.411 1.00 53.00  ? 58  GLN A CD  1 
ATOM   454 O OE1 . GLN A 1 58 ? 1.357  13.937  36.781 1.00 54.45  ? 58  GLN A OE1 1 
ATOM   455 N NE2 . GLN A 1 58 ? 2.208  12.216  37.937 1.00 54.16  ? 58  GLN A NE2 1 
ATOM   456 N N   . TYR A 1 59 ? -0.696 8.693   35.729 1.00 42.18  ? 59  TYR A N   1 
ATOM   457 C CA  . TYR A 1 59 ? -0.644 7.327   36.229 1.00 40.99  ? 59  TYR A CA  1 
ATOM   458 C C   . TYR A 1 59 ? 0.670  6.690   35.780 1.00 38.01  ? 59  TYR A C   1 
ATOM   459 O O   . TYR A 1 59 ? 1.386  6.084   36.573 1.00 38.17  ? 59  TYR A O   1 
ATOM   460 C CB  . TYR A 1 59 ? -1.859 6.489   35.796 1.00 41.46  ? 59  TYR A CB  1 
ATOM   461 C CG  . TYR A 1 59 ? -1.706 5.019   36.168 1.00 41.31  ? 59  TYR A CG  1 
ATOM   462 C CD1 . TYR A 1 59 ? -1.877 4.601   37.483 1.00 44.18  ? 59  TYR A CD1 1 
ATOM   463 C CD2 . TYR A 1 59 ? -1.319 4.061   35.236 1.00 39.21  ? 59  TYR A CD2 1 
ATOM   464 C CE1 . TYR A 1 59 ? -1.706 3.277   37.854 1.00 45.36  ? 59  TYR A CE1 1 
ATOM   465 C CE2 . TYR A 1 59 ? -1.136 2.732   35.594 1.00 39.78  ? 59  TYR A CE2 1 
ATOM   466 C CZ  . TYR A 1 59 ? -1.322 2.339   36.911 1.00 43.99  ? 59  TYR A CZ  1 
ATOM   467 O OH  . TYR A 1 59 ? -1.145 1.041   37.318 1.00 46.54  ? 59  TYR A OH  1 
ATOM   468 N N   . GLN A 1 60 ? 0.982  6.817   34.491 1.00 35.48  ? 60  GLN A N   1 
ATOM   469 C CA  . GLN A 1 60 ? 2.192  6.230   33.953 1.00 33.07  ? 60  GLN A CA  1 
ATOM   470 C C   . GLN A 1 60 ? 3.436  6.846   34.595 1.00 34.15  ? 60  GLN A C   1 
ATOM   471 O O   . GLN A 1 60 ? 4.397  6.136   34.865 1.00 34.78  ? 60  GLN A O   1 
ATOM   472 C CB  . GLN A 1 60 ? 2.200  6.421   32.440 1.00 31.59  ? 60  GLN A CB  1 
ATOM   473 C CG  . GLN A 1 60 ? 1.250  5.478   31.710 1.00 31.35  ? 60  GLN A CG  1 
ATOM   474 C CD  . GLN A 1 60 ? 1.104  5.796   30.238 1.00 30.56  ? 60  GLN A CD  1 
ATOM   475 O OE1 . GLN A 1 60 ? 0.903  6.950   29.850 1.00 33.72  ? 60  GLN A OE1 1 
ATOM   476 N NE2 . GLN A 1 60 ? 1.184  4.779   29.398 1.00 30.07  ? 60  GLN A NE2 1 
ATOM   477 N N   . LEU A 1 61 ? 3.427  8.168   34.788 1.00 35.41  ? 61  LEU A N   1 
ATOM   478 C CA  . LEU A 1 61 ? 4.565  8.867   35.365 1.00 37.84  ? 61  LEU A CA  1 
ATOM   479 C C   . LEU A 1 61 ? 4.783  8.425   36.813 1.00 39.05  ? 61  LEU A C   1 
ATOM   480 O O   . LEU A 1 61 ? 5.931  8.297   37.255 1.00 39.99  ? 61  LEU A O   1 
ATOM   481 C CB  . LEU A 1 61 ? 4.341  10.375  35.250 1.00 39.87  ? 61  LEU A CB  1 
ATOM   482 C CG  . LEU A 1 61 ? 4.411  10.962  33.835 1.00 38.93  ? 61  LEU A CG  1 
ATOM   483 C CD1 . LEU A 1 61 ? 4.014  12.433  33.861 1.00 41.05  ? 61  LEU A CD1 1 
ATOM   484 C CD2 . LEU A 1 61 ? 5.771  10.788  33.176 1.00 37.56  ? 61  LEU A CD2 1 
ATOM   485 N N   . ASN A 1 62 ? 3.684  8.188   37.544 1.00 39.94  ? 62  ASN A N   1 
ATOM   486 C CA  . ASN A 1 62 ? 3.761  7.718   38.921 1.00 42.79  ? 62  ASN A CA  1 
ATOM   487 C C   . ASN A 1 62 ? 4.377  6.324   38.963 1.00 41.83  ? 62  ASN A C   1 
ATOM   488 O O   . ASN A 1 62 ? 5.231  6.054   39.803 1.00 41.31  ? 62  ASN A O   1 
ATOM   489 C CB  . ASN A 1 62 ? 2.402  7.728   39.608 1.00 46.28  ? 62  ASN A CB  1 
ATOM   490 C CG  . ASN A 1 62 ? 1.876  9.129   39.807 1.00 48.19  ? 62  ASN A CG  1 
ATOM   491 O OD1 . ASN A 1 62 ? 2.620  10.103  39.662 1.00 48.83  ? 62  ASN A OD1 1 
ATOM   492 N ND2 . ASN A 1 62 ? 0.600  9.252   40.127 1.00 50.21  ? 62  ASN A ND2 1 
ATOM   493 N N   . SER A 1 63 ? 3.956  5.451   38.038 1.00 39.70  ? 63  SER A N   1 
ATOM   494 C CA  . SER A 1 63 ? 4.526  4.116   37.921 1.00 38.87  ? 63  SER A CA  1 
ATOM   495 C C   . SER A 1 63 ? 6.030  4.189   37.675 1.00 38.30  ? 63  SER A C   1 
ATOM   496 O O   . SER A 1 63 ? 6.796  3.467   38.311 1.00 39.05  ? 63  SER A O   1 
ATOM   497 C CB  . SER A 1 63 ? 3.849  3.324   36.840 1.00 37.16  ? 63  SER A CB  1 
ATOM   498 O OG  . SER A 1 63 ? 2.465  3.186   37.140 1.00 40.16  ? 63  SER A OG  1 
ATOM   499 N N   . ILE A 1 64 ? 6.423  5.042   36.718 1.00 36.96  ? 64  ILE A N   1 
ATOM   500 C CA  . ILE A 1 64 ? 7.810  5.217   36.312 1.00 36.90  ? 64  ILE A CA  1 
ATOM   501 C C   . ILE A 1 64 ? 8.663  5.634   37.510 1.00 39.67  ? 64  ILE A C   1 
ATOM   502 O O   . ILE A 1 64 ? 9.746  5.079   37.722 1.00 40.90  ? 64  ILE A O   1 
ATOM   503 C CB  . ILE A 1 64 ? 7.882  6.226   35.151 1.00 35.11  ? 64  ILE A CB  1 
ATOM   504 C CG1 . ILE A 1 64 ? 7.320  5.608   33.871 1.00 34.49  ? 64  ILE A CG1 1 
ATOM   505 C CG2 . ILE A 1 64 ? 9.304  6.752   34.933 1.00 35.31  ? 64  ILE A CG2 1 
ATOM   506 C CD1 . ILE A 1 64 ? 6.936  6.612   32.808 1.00 33.74  ? 64  ILE A CD1 1 
ATOM   507 N N   . GLN A 1 65 ? 8.178  6.619   38.274 1.00 42.82  ? 65  GLN A N   1 
ATOM   508 C CA  . GLN A 1 65 ? 8.875  7.087   39.465 1.00 47.04  ? 65  GLN A CA  1 
ATOM   509 C C   . GLN A 1 65 ? 8.969  5.955   40.487 1.00 48.48  ? 65  GLN A C   1 
ATOM   510 O O   . GLN A 1 65 ? 10.042 5.643   40.987 1.00 49.58  ? 65  GLN A O   1 
ATOM   511 C CB  . GLN A 1 65 ? 8.121  8.293   40.021 1.00 51.93  ? 65  GLN A CB  1 
ATOM   512 C CG  . GLN A 1 65 ? 8.774  8.947   41.235 1.00 58.65  ? 65  GLN A CG  1 
ATOM   513 C CD  . GLN A 1 65 ? 7.782  9.680   42.114 1.00 66.09  ? 65  GLN A CD  1 
ATOM   514 O OE1 . GLN A 1 65 ? 6.577  9.735   41.837 1.00 70.38  ? 65  GLN A OE1 1 
ATOM   515 N NE2 . GLN A 1 65 ? 8.278  10.230  43.214 1.00 75.04  ? 65  GLN A NE2 1 
ATOM   516 N N   . LYS A 1 66 ? 7.828  5.329   40.783 1.00 49.22  ? 66  LYS A N   1 
ATOM   517 C CA  . LYS A 1 66 ? 7.755  4.240   41.744 1.00 52.26  ? 66  LYS A CA  1 
ATOM   518 C C   . LYS A 1 66 ? 8.760  3.134   41.408 1.00 51.07  ? 66  LYS A C   1 
ATOM   519 O O   . LYS A 1 66 ? 9.403  2.600   42.306 1.00 52.45  ? 66  LYS A O   1 
ATOM   520 C CB  . LYS A 1 66 ? 6.311  3.723   41.797 1.00 54.08  ? 66  LYS A CB  1 
ATOM   521 C CG  . LYS A 1 66 ? 6.042  2.733   42.918 1.00 59.26  ? 66  LYS A CG  1 
ATOM   522 C CD  . LYS A 1 66 ? 4.650  2.117   42.915 1.00 62.04  ? 66  LYS A CD  1 
ATOM   523 C CE  . LYS A 1 66 ? 4.513  1.139   44.036 1.00 66.77  ? 66  LYS A CE  1 
ATOM   524 N NZ  . LYS A 1 66 ? 3.163  0.576   44.108 1.00 70.50  ? 66  LYS A NZ  1 
ATOM   525 N N   . ASN A 1 67 ? 8.903  2.779   40.126 1.00 45.84  ? 67  ASN A N   1 
ATOM   526 C CA  . ASN A 1 67 ? 9.672  1.599   39.746 1.00 45.97  ? 67  ASN A CA  1 
ATOM   527 C C   . ASN A 1 67 ? 11.061 1.989   39.223 1.00 45.05  ? 67  ASN A C   1 
ATOM   528 O O   . ASN A 1 67 ? 11.799 1.140   38.707 1.00 45.22  ? 67  ASN A O   1 
ATOM   529 C CB  . ASN A 1 67 ? 8.870  0.735   38.773 1.00 44.20  ? 67  ASN A CB  1 
ATOM   530 C CG  . ASN A 1 67 ? 7.627  0.163   39.418 1.00 45.95  ? 67  ASN A CG  1 
ATOM   531 O OD1 . ASN A 1 67 ? 6.496  0.467   39.012 1.00 46.43  ? 67  ASN A OD1 1 
ATOM   532 N ND2 . ASN A 1 67 ? 7.811  -0.647  40.446 1.00 47.02  ? 67  ASN A ND2 1 
ATOM   533 N N   . HIS A 1 68 ? 11.428 3.269   39.388 1.00 45.17  ? 68  HIS A N   1 
ATOM   534 C CA  . HIS A 1 68 ? 12.730 3.782   38.986 1.00 45.91  ? 68  HIS A CA  1 
ATOM   535 C C   . HIS A 1 68 ? 13.000 3.521   37.506 1.00 42.03  ? 68  HIS A C   1 
ATOM   536 O O   . HIS A 1 68 ? 14.113 3.170   37.122 1.00 43.32  ? 68  HIS A O   1 
ATOM   537 C CB  . HIS A 1 68 ? 13.830 3.198   39.881 1.00 50.81  ? 68  HIS A CB  1 
ATOM   538 C CG  . HIS A 1 68 ? 13.536 3.386   41.328 1.00 56.04  ? 68  HIS A CG  1 
ATOM   539 N ND1 . HIS A 1 68 ? 13.856 4.543   42.002 1.00 61.01  ? 68  HIS A ND1 1 
ATOM   540 C CD2 . HIS A 1 68 ? 12.918 2.597   42.211 1.00 59.98  ? 68  HIS A CD2 1 
ATOM   541 C CE1 . HIS A 1 68 ? 13.469 4.433   43.264 1.00 64.94  ? 68  HIS A CE1 1 
ATOM   542 N NE2 . HIS A 1 68 ? 12.893 3.258   43.412 1.00 64.31  ? 68  HIS A NE2 1 
ATOM   543 N N   . VAL A 1 69 ? 11.991 3.742   36.661 1.00 39.06  ? 69  VAL A N   1 
ATOM   544 C CA  . VAL A 1 69 ? 12.144 3.557   35.227 1.00 34.91  ? 69  VAL A CA  1 
ATOM   545 C C   . VAL A 1 69 ? 12.765 4.818   34.624 1.00 34.01  ? 69  VAL A C   1 
ATOM   546 O O   . VAL A 1 69 ? 12.389 5.926   34.987 1.00 34.74  ? 69  VAL A O   1 
ATOM   547 C CB  . VAL A 1 69 ? 10.786 3.208   34.583 1.00 34.48  ? 69  VAL A CB  1 
ATOM   548 C CG1 . VAL A 1 69 ? 10.890 3.012   33.076 1.00 32.49  ? 69  VAL A CG1 1 
ATOM   549 C CG2 . VAL A 1 69 ? 10.167 1.977   35.229 1.00 35.96  ? 69  VAL A CG2 1 
ATOM   550 N N   . HIS A 1 70 ? 13.743 4.630   33.725 1.00 32.30  ? 70  HIS A N   1 
ATOM   551 C CA  . HIS A 1 70 ? 14.385 5.713   32.990 1.00 33.76  ? 70  HIS A CA  1 
ATOM   552 C C   . HIS A 1 70 ? 13.567 6.074   31.745 1.00 31.68  ? 70  HIS A C   1 
ATOM   553 O O   . HIS A 1 70 ? 13.288 5.205   30.926 1.00 31.49  ? 70  HIS A O   1 
ATOM   554 C CB  . HIS A 1 70 ? 15.781 5.287   32.517 1.00 34.91  ? 70  HIS A CB  1 
ATOM   555 C CG  . HIS A 1 70 ? 16.734 4.984   33.627 1.00 40.68  ? 70  HIS A CG  1 
ATOM   556 N ND1 . HIS A 1 70 ? 16.964 5.865   34.661 1.00 43.19  ? 70  HIS A ND1 1 
ATOM   557 C CD2 . HIS A 1 70 ? 17.516 3.921   33.860 1.00 43.84  ? 70  HIS A CD2 1 
ATOM   558 C CE1 . HIS A 1 70 ? 17.848 5.334   35.497 1.00 46.26  ? 70  HIS A CE1 1 
ATOM   559 N NE2 . HIS A 1 70 ? 18.193 4.152   35.031 1.00 45.21  ? 70  HIS A NE2 1 
ATOM   560 N N   . ILE A 1 71 ? 13.188 7.353   31.596 1.00 31.83  ? 71  ILE A N   1 
ATOM   561 C CA  . ILE A 1 71 ? 12.480 7.808   30.399 1.00 31.23  ? 71  ILE A CA  1 
ATOM   562 C C   . ILE A 1 71 ? 13.511 8.333   29.402 1.00 29.25  ? 71  ILE A C   1 
ATOM   563 O O   . ILE A 1 71 ? 14.323 9.180   29.771 1.00 29.59  ? 71  ILE A O   1 
ATOM   564 C CB  . ILE A 1 71 ? 11.436 8.896   30.721 1.00 33.16  ? 71  ILE A CB  1 
ATOM   565 C CG1 . ILE A 1 71 ? 10.494 8.475   31.854 1.00 34.44  ? 71  ILE A CG1 1 
ATOM   566 C CG2 . ILE A 1 71 ? 10.657 9.288   29.460 1.00 33.07  ? 71  ILE A CG2 1 
ATOM   567 C CD1 . ILE A 1 71 ? 9.537  9.568   32.305 1.00 37.63  ? 71  ILE A CD1 1 
ATOM   568 N N   . ALA A 1 72 ? 13.462 7.833   28.156 1.00 27.02  ? 72  ALA A N   1 
ATOM   569 C CA  . ALA A 1 72 ? 14.423 8.221   27.133 1.00 27.96  ? 72  ALA A CA  1 
ATOM   570 C C   . ALA A 1 72 ? 13.744 8.366   25.766 1.00 29.24  ? 72  ALA A C   1 
ATOM   571 O O   . ALA A 1 72 ? 12.723 7.742   25.507 1.00 29.87  ? 72  ALA A O   1 
ATOM   572 C CB  . ALA A 1 72 ? 15.565 7.223   27.080 1.00 28.18  ? 72  ALA A CB  1 
ATOM   573 N N   . ASN A 1 73 ? 14.316 9.221   24.905 1.00 30.76  ? 73  ASN A N   1 
ATOM   574 C CA  . ASN A 1 73 ? 13.911 9.301   23.504 1.00 28.85  ? 73  ASN A CA  1 
ATOM   575 C C   . ASN A 1 73 ? 14.617 8.208   22.693 1.00 28.28  ? 73  ASN A C   1 
ATOM   576 O O   . ASN A 1 73 ? 15.515 7.515   23.186 1.00 27.26  ? 73  ASN A O   1 
ATOM   577 C CB  . ASN A 1 73 ? 14.092 10.710  22.949 1.00 30.77  ? 73  ASN A CB  1 
ATOM   578 C CG  . ASN A 1 73 ? 15.544 11.123  22.887 1.00 30.71  ? 73  ASN A CG  1 
ATOM   579 O OD1 . ASN A 1 73 ? 16.408 10.298  22.579 1.00 31.92  ? 73  ASN A OD1 1 
ATOM   580 N ND2 . ASN A 1 73 ? 15.840 12.353  23.267 1.00 32.29  ? 73  ASN A ND2 1 
ATOM   581 N N   . PRO A 1 74 ? 14.205 7.964   21.427 1.00 26.19  ? 74  PRO A N   1 
ATOM   582 C CA  . PRO A 1 74 ? 14.829 6.930   20.601 1.00 23.98  ? 74  PRO A CA  1 
ATOM   583 C C   . PRO A 1 74 ? 16.319 7.117   20.328 1.00 24.32  ? 74  PRO A C   1 
ATOM   584 O O   . PRO A 1 74 ? 17.028 6.138   20.079 1.00 25.03  ? 74  PRO A O   1 
ATOM   585 C CB  . PRO A 1 74 ? 14.005 6.965   19.306 1.00 26.60  ? 74  PRO A CB  1 
ATOM   586 C CG  . PRO A 1 74 ? 12.677 7.545   19.750 1.00 27.78  ? 74  PRO A CG  1 
ATOM   587 C CD  . PRO A 1 74 ? 13.019 8.560   20.784 1.00 28.98  ? 74  PRO A CD  1 
ATOM   588 N N   . ASP A 1 75 ? 16.794 8.365   20.378 1.00 25.59  ? 75  ASP A N   1 
ATOM   589 C CA  . ASP A 1 75 ? 18.211 8.651   20.176 1.00 27.54  ? 75  ASP A CA  1 
ATOM   590 C C   . ASP A 1 75 ? 19.088 7.962   21.214 1.00 26.21  ? 75  ASP A C   1 
ATOM   591 O O   . ASP A 1 75 ? 20.249 7.698   20.933 1.00 26.43  ? 75  ASP A O   1 
ATOM   592 C CB  . ASP A 1 75 ? 18.499 10.141  20.220 1.00 30.21  ? 75  ASP A CB  1 
ATOM   593 C CG  . ASP A 1 75 ? 18.085 10.881  18.961 1.00 35.19  ? 75  ASP A CG  1 
ATOM   594 O OD1 . ASP A 1 75 ? 17.905 10.216  17.921 1.00 34.98  ? 75  ASP A OD1 1 
ATOM   595 O OD2 . ASP A 1 75 ? 17.967 12.099  19.038 1.00 41.20  ? 75  ASP A OD2 1 
ATOM   596 N N   . PHE A 1 76 ? 18.543 7.697   22.409 1.00 25.41  ? 76  PHE A N   1 
ATOM   597 C CA  . PHE A 1 76 ? 19.271 6.908   23.399 1.00 25.97  ? 76  PHE A CA  1 
ATOM   598 C C   . PHE A 1 76 ? 19.696 5.561   22.798 1.00 26.04  ? 76  PHE A C   1 
ATOM   599 O O   . PHE A 1 76 ? 20.850 5.150   22.941 1.00 26.62  ? 76  PHE A O   1 
ATOM   600 C CB  . PHE A 1 76 ? 18.455 6.755   24.683 1.00 26.14  ? 76  PHE A CB  1 
ATOM   601 C CG  . PHE A 1 76 ? 19.172 5.879   25.701 1.00 27.59  ? 76  PHE A CG  1 
ATOM   602 C CD1 . PHE A 1 76 ? 20.382 6.289   26.253 1.00 29.62  ? 76  PHE A CD1 1 
ATOM   603 C CD2 . PHE A 1 76 ? 18.658 4.639   26.063 1.00 28.29  ? 76  PHE A CD2 1 
ATOM   604 C CE1 . PHE A 1 76 ? 21.043 5.485   27.171 1.00 30.66  ? 76  PHE A CE1 1 
ATOM   605 C CE2 . PHE A 1 76 ? 19.329 3.828   26.972 1.00 29.97  ? 76  PHE A CE2 1 
ATOM   606 C CZ  . PHE A 1 76 ? 20.514 4.262   27.530 1.00 30.38  ? 76  PHE A CZ  1 
ATOM   607 N N   . ILE A 1 77 ? 18.779 4.893   22.091 1.00 23.47  ? 77  ILE A N   1 
ATOM   608 C CA  . ILE A 1 77 ? 19.074 3.627   21.438 1.00 25.33  ? 77  ILE A CA  1 
ATOM   609 C C   . ILE A 1 77 ? 20.010 3.840   20.251 1.00 25.55  ? 77  ILE A C   1 
ATOM   610 O O   . ILE A 1 77 ? 21.035 3.172   20.142 1.00 27.80  ? 77  ILE A O   1 
ATOM   611 C CB  . ILE A 1 77 ? 17.782 2.908   20.999 1.00 26.54  ? 77  ILE A CB  1 
ATOM   612 C CG1 . ILE A 1 77 ? 16.799 2.707   22.153 1.00 29.12  ? 77  ILE A CG1 1 
ATOM   613 C CG2 . ILE A 1 77 ? 18.107 1.592   20.288 1.00 26.65  ? 77  ILE A CG2 1 
ATOM   614 C CD1 . ILE A 1 77 ? 17.327 1.864   23.297 1.00 29.70  ? 77  ILE A CD1 1 
ATOM   615 N N   . TRP A 1 78 ? 19.647 4.762   19.354 1.00 25.20  ? 78  TRP A N   1 
ATOM   616 C CA  . TRP A 1 78 ? 20.394 4.972   18.122 1.00 27.23  ? 78  TRP A CA  1 
ATOM   617 C C   . TRP A 1 78 ? 21.858 5.295   18.437 1.00 26.61  ? 78  TRP A C   1 
ATOM   618 O O   . TRP A 1 78 ? 22.773 4.747   17.832 1.00 25.55  ? 78  TRP A O   1 
ATOM   619 C CB  . TRP A 1 78 ? 19.809 6.137   17.312 1.00 28.45  ? 78  TRP A CB  1 
ATOM   620 C CG  . TRP A 1 78 ? 18.364 6.051   16.886 1.00 29.37  ? 78  TRP A CG  1 
ATOM   621 C CD1 . TRP A 1 78 ? 17.494 7.098   16.834 1.00 30.64  ? 78  TRP A CD1 1 
ATOM   622 C CD2 . TRP A 1 78 ? 17.654 4.924   16.335 1.00 29.20  ? 78  TRP A CD2 1 
ATOM   623 N NE1 . TRP A 1 78 ? 16.275 6.693   16.356 1.00 29.01  ? 78  TRP A NE1 1 
ATOM   624 C CE2 . TRP A 1 78 ? 16.347 5.371   16.024 1.00 30.42  ? 78  TRP A CE2 1 
ATOM   625 C CE3 . TRP A 1 78 ? 17.986 3.589   16.093 1.00 28.93  ? 78  TRP A CE3 1 
ATOM   626 C CZ2 . TRP A 1 78 ? 15.374 4.531   15.476 1.00 29.35  ? 78  TRP A CZ2 1 
ATOM   627 C CZ3 . TRP A 1 78 ? 17.024 2.760   15.558 1.00 30.33  ? 78  TRP A CZ3 1 
ATOM   628 C CH2 . TRP A 1 78 ? 15.746 3.230   15.244 1.00 30.15  ? 78  TRP A CH2 1 
ATOM   629 N N   . LYS A 1 79 ? 22.072 6.229   19.369 1.00 28.23  ? 79  LYS A N   1 
ATOM   630 C CA  . LYS A 1 79 ? 23.412 6.740   19.626 1.00 30.67  ? 79  LYS A CA  1 
ATOM   631 C C   . LYS A 1 79 ? 24.227 5.751   20.463 1.00 29.25  ? 79  LYS A C   1 
ATOM   632 O O   . LYS A 1 79 ? 25.445 5.676   20.303 1.00 30.54  ? 79  LYS A O   1 
ATOM   633 C CB  . LYS A 1 79 ? 23.352 8.144   20.235 1.00 34.40  ? 79  LYS A CB  1 
ATOM   634 C CG  . LYS A 1 79 ? 22.709 9.138   19.284 1.00 42.28  ? 79  LYS A CG  1 
ATOM   635 C CD  . LYS A 1 79 ? 23.097 10.604  19.445 1.00 49.93  ? 79  LYS A CD  1 
ATOM   636 C CE  . LYS A 1 79 ? 22.438 11.428  18.378 1.00 51.55  ? 79  LYS A CE  1 
ATOM   637 N NZ  . LYS A 1 79 ? 22.860 12.824  18.439 1.00 59.63  ? 79  LYS A NZ  1 
ATOM   638 N N   . SER A 1 80 ? 23.582 5.008   21.369 1.00 27.54  ? 80  SER A N   1 
ATOM   639 C CA  . SER A 1 80 ? 24.284 3.960   22.104 1.00 29.83  ? 80  SER A CA  1 
ATOM   640 C C   . SER A 1 80 ? 24.819 2.907   21.122 1.00 32.02  ? 80  SER A C   1 
ATOM   641 O O   . SER A 1 80 ? 25.971 2.481   21.212 1.00 33.44  ? 80  SER A O   1 
ATOM   642 C CB  . SER A 1 80 ? 23.415 3.346   23.201 1.00 28.94  ? 80  SER A CB  1 
ATOM   643 O OG  . SER A 1 80 ? 23.133 4.270   24.250 1.00 27.70  ? 80  SER A OG  1 
ATOM   644 N N   . ILE A 1 81 ? 23.973 2.499   20.170 1.00 30.36  ? 81  ILE A N   1 
ATOM   645 C CA  . ILE A 1 81 ? 24.339 1.519   19.157 1.00 32.99  ? 81  ILE A CA  1 
ATOM   646 C C   . ILE A 1 81 ? 25.497 2.053   18.316 1.00 32.88  ? 81  ILE A C   1 
ATOM   647 O O   . ILE A 1 81 ? 26.443 1.329   18.016 1.00 34.43  ? 81  ILE A O   1 
ATOM   648 C CB  . ILE A 1 81 ? 23.124 1.189   18.266 1.00 33.30  ? 81  ILE A CB  1 
ATOM   649 C CG1 . ILE A 1 81 ? 22.068 0.357   19.000 1.00 34.19  ? 81  ILE A CG1 1 
ATOM   650 C CG2 . ILE A 1 81 ? 23.553 0.534   16.953 1.00 35.10  ? 81  ILE A CG2 1 
ATOM   651 C CD1 . ILE A 1 81 ? 22.495 -1.052  19.354 1.00 37.16  ? 81  ILE A CD1 1 
ATOM   652 N N   . ARG A 1 82 ? 25.406 3.327   17.940 1.00 32.17  ? 82  ARG A N   1 
ATOM   653 C CA  . ARG A 1 82 ? 26.406 3.973   17.105 1.00 35.20  ? 82  ARG A CA  1 
ATOM   654 C C   . ARG A 1 82 ? 27.760 4.024   17.815 1.00 36.28  ? 82  ARG A C   1 
ATOM   655 O O   . ARG A 1 82 ? 28.792 3.741   17.199 1.00 36.64  ? 82  ARG A O   1 
ATOM   656 C CB  . ARG A 1 82 ? 25.956 5.385   16.711 1.00 35.29  ? 82  ARG A CB  1 
ATOM   657 C CG  . ARG A 1 82 ? 27.079 6.161   16.040 1.00 41.71  ? 82  ARG A CG  1 
ATOM   658 C CD  . ARG A 1 82 ? 26.626 7.424   15.353 1.00 46.06  ? 82  ARG A CD  1 
ATOM   659 N NE  . ARG A 1 82 ? 25.879 7.087   14.138 1.00 47.72  ? 82  ARG A NE  1 
ATOM   660 C CZ  . ARG A 1 82 ? 24.744 7.659   13.783 1.00 50.30  ? 82  ARG A CZ  1 
ATOM   661 N NH1 . ARG A 1 82 ? 24.225 8.607   14.552 1.00 54.65  ? 82  ARG A NH1 1 
ATOM   662 N NH2 . ARG A 1 82 ? 24.138 7.293   12.665 1.00 44.72  ? 82  ARG A NH2 1 
ATOM   663 N N   . GLU A 1 83 ? 27.746 4.380   19.107 1.00 35.43  ? 83  GLU A N   1 
ATOM   664 C CA  A GLU A 1 83 ? 28.974 4.551   19.867 0.50 38.06  ? 83  GLU A CA  1 
ATOM   665 C CA  B GLU A 1 83 ? 28.955 4.552   19.896 0.50 37.86  ? 83  GLU A CA  1 
ATOM   666 C C   . GLU A 1 83 ? 29.454 3.198   20.398 1.00 39.44  ? 83  GLU A C   1 
ATOM   667 O O   . GLU A 1 83 ? 30.554 3.103   20.951 1.00 38.93  ? 83  GLU A O   1 
ATOM   668 C CB  A GLU A 1 83 ? 28.732 5.643   20.911 0.50 38.86  ? 83  GLU A CB  1 
ATOM   669 C CB  B GLU A 1 83 ? 28.660 5.490   21.067 0.50 38.24  ? 83  GLU A CB  1 
ATOM   670 C CG  A GLU A 1 83 ? 28.564 7.021   20.272 0.50 39.81  ? 83  GLU A CG  1 
ATOM   671 C CG  B GLU A 1 83 ? 28.387 6.932   20.647 0.50 38.85  ? 83  GLU A CG  1 
ATOM   672 C CD  A GLU A 1 83 ? 28.419 8.209   21.208 0.50 40.86  ? 83  GLU A CD  1 
ATOM   673 C CD  B GLU A 1 83 ? 29.470 7.552   19.777 0.50 41.08  ? 83  GLU A CD  1 
ATOM   674 O OE1 A GLU A 1 83 ? 29.243 8.334   22.131 0.50 42.78  ? 83  GLU A OE1 1 
ATOM   675 O OE1 B GLU A 1 83 ? 30.656 7.334   20.073 0.50 43.06  ? 83  GLU A OE1 1 
ATOM   676 O OE2 A GLU A 1 83 ? 27.507 9.033   20.988 0.50 41.16  ? 83  GLU A OE2 1 
ATOM   677 O OE2 B GLU A 1 83 ? 29.132 8.267   18.812 0.50 42.28  ? 83  GLU A OE2 1 
ATOM   678 N N   . LYS A 1 84 ? 28.627 2.154   20.212 1.00 38.01  ? 84  LYS A N   1 
ATOM   679 C CA  . LYS A 1 84 ? 28.938 0.796   20.638 1.00 40.27  ? 84  LYS A CA  1 
ATOM   680 C C   . LYS A 1 84 ? 29.152 0.775   22.148 1.00 39.95  ? 84  LYS A C   1 
ATOM   681 O O   . LYS A 1 84 ? 30.038 0.077   22.648 1.00 39.55  ? 84  LYS A O   1 
ATOM   682 C CB  . LYS A 1 84 ? 30.146 0.200   19.902 1.00 43.74  ? 84  LYS A CB  1 
ATOM   683 C CG  . LYS A 1 84 ? 29.908 -0.011  18.414 1.00 46.23  ? 84  LYS A CG  1 
ATOM   684 C CD  . LYS A 1 84 ? 31.027 -0.756  17.696 1.00 51.00  ? 84  LYS A CD  1 
ATOM   685 C CE  . LYS A 1 84 ? 30.678 -0.985  16.263 1.00 54.26  ? 84  LYS A CE  1 
ATOM   686 N NZ  . LYS A 1 84 ? 31.864 -1.343  15.475 1.00 59.11  ? 84  LYS A NZ  1 
ATOM   687 N N   . ARG A 1 85 ? 28.299 1.523   22.860 1.00 35.83  ? 85  ARG A N   1 
ATOM   688 C CA  . ARG A 1 85 ? 28.463 1.739   24.286 1.00 36.46  ? 85  ARG A CA  1 
ATOM   689 C C   . ARG A 1 85 ? 27.165 2.302   24.854 1.00 35.86  ? 85  ARG A C   1 
ATOM   690 O O   . ARG A 1 85 ? 26.563 3.199   24.259 1.00 32.31  ? 85  ARG A O   1 
ATOM   691 C CB  . ARG A 1 85 ? 29.639 2.698   24.479 1.00 37.88  ? 85  ARG A CB  1 
ATOM   692 C CG  . ARG A 1 85 ? 30.006 3.002   25.923 1.00 38.62  ? 85  ARG A CG  1 
ATOM   693 C CD  . ARG A 1 85 ? 31.303 3.797   25.985 1.00 40.49  ? 85  ARG A CD  1 
ATOM   694 N NE  . ARG A 1 85 ? 31.185 5.161   25.452 1.00 39.47  ? 85  ARG A NE  1 
ATOM   695 C CZ  . ARG A 1 85 ? 30.541 6.172   26.032 1.00 39.52  ? 85  ARG A CZ  1 
ATOM   696 N NH1 . ARG A 1 85 ? 29.988 6.022   27.221 1.00 38.47  ? 85  ARG A NH1 1 
ATOM   697 N NH2 . ARG A 1 85 ? 30.463 7.347   25.436 1.00 39.64  ? 85  ARG A NH2 1 
ATOM   698 N N   . LEU A 1 86 ? 26.723 1.752   25.989 1.00 36.49  ? 86  LEU A N   1 
ATOM   699 C CA  . LEU A 1 86 ? 25.534 2.264   26.650 1.00 35.12  ? 86  LEU A CA  1 
ATOM   700 C C   . LEU A 1 86 ? 25.837 3.686   27.126 1.00 34.81  ? 86  LEU A C   1 
ATOM   701 O O   . LEU A 1 86 ? 26.765 3.877   27.905 1.00 34.23  ? 86  LEU A O   1 
ATOM   702 C CB  . LEU A 1 86 ? 25.161 1.345   27.811 1.00 36.77  ? 86  LEU A CB  1 
ATOM   703 C CG  . LEU A 1 86 ? 23.823 1.632   28.496 1.00 37.24  ? 86  LEU A CG  1 
ATOM   704 C CD1 . LEU A 1 86 ? 22.675 1.414   27.530 1.00 34.52  ? 86  LEU A CD1 1 
ATOM   705 C CD2 . LEU A 1 86 ? 23.641 0.778   29.737 1.00 39.36  ? 86  LEU A CD2 1 
ATOM   706 N N   . LEU A 1 87 ? 25.071 4.678   26.636 1.00 33.15  ? 87  LEU A N   1 
ATOM   707 C CA  . LEU A 1 87 ? 25.319 6.075   26.972 1.00 32.86  ? 87  LEU A CA  1 
ATOM   708 C C   . LEU A 1 87 ? 24.588 6.463   28.261 1.00 33.17  ? 87  LEU A C   1 
ATOM   709 O O   . LEU A 1 87 ? 24.002 5.619   28.928 1.00 32.98  ? 87  LEU A O   1 
ATOM   710 C CB  . LEU A 1 87 ? 24.949 6.981   25.798 1.00 32.46  ? 87  LEU A CB  1 
ATOM   711 C CG  . LEU A 1 87 ? 25.626 6.650   24.465 1.00 32.06  ? 87  LEU A CG  1 
ATOM   712 C CD1 . LEU A 1 87 ? 25.190 7.600   23.356 1.00 32.96  ? 87  LEU A CD1 1 
ATOM   713 C CD2 . LEU A 1 87 ? 27.133 6.633   24.621 1.00 34.68  ? 87  LEU A CD2 1 
ATOM   714 N N   . ASP A 1 88 ? 24.697 7.745   28.632 1.00 33.41  ? 88  ASP A N   1 
ATOM   715 C CA  . ASP A 1 88 ? 24.073 8.271   29.829 1.00 35.85  ? 88  ASP A CA  1 
ATOM   716 C C   . ASP A 1 88 ? 22.614 8.595   29.519 1.00 34.24  ? 88  ASP A C   1 
ATOM   717 O O   . ASP A 1 88 ? 22.326 9.602   28.884 1.00 36.11  ? 88  ASP A O   1 
ATOM   718 C CB  . ASP A 1 88 ? 24.775 9.522   30.330 1.00 38.17  ? 88  ASP A CB  1 
ATOM   719 C CG  . ASP A 1 88 ? 24.328 10.004  31.700 1.00 40.79  ? 88  ASP A CG  1 
ATOM   720 O OD1 . ASP A 1 88 ? 23.296 9.496   32.200 1.00 41.31  ? 88  ASP A OD1 1 
ATOM   721 O OD2 . ASP A 1 88 ? 25.041 10.842  32.275 1.00 45.55  ? 88  ASP A OD2 1 
ATOM   722 N N   . VAL A 1 89 ? 21.716 7.750   30.018 1.00 33.88  ? 89  VAL A N   1 
ATOM   723 C CA  . VAL A 1 89 ? 20.296 7.855   29.742 1.00 31.82  ? 89  VAL A CA  1 
ATOM   724 C C   . VAL A 1 89 ? 19.739 9.194   30.233 1.00 34.92  ? 89  VAL A C   1 
ATOM   725 O O   . VAL A 1 89 ? 18.707 9.658   29.734 1.00 33.15  ? 89  VAL A O   1 
ATOM   726 C CB  . VAL A 1 89 ? 19.570 6.655   30.377 1.00 31.93  ? 89  VAL A CB  1 
ATOM   727 C CG1 . VAL A 1 89 ? 19.557 6.706   31.908 1.00 34.06  ? 89  VAL A CG1 1 
ATOM   728 C CG2 . VAL A 1 89 ? 18.150 6.527   29.839 1.00 29.51  ? 89  VAL A CG2 1 
ATOM   729 N N   . LYS A 1 90 ? 20.402 9.802   31.227 1.00 37.80  ? 90  LYS A N   1 
ATOM   730 C CA  . LYS A 1 90 ? 20.027 11.114  31.736 1.00 42.27  ? 90  LYS A CA  1 
ATOM   731 C C   . LYS A 1 90 ? 20.176 12.205  30.674 1.00 41.01  ? 90  LYS A C   1 
ATOM   732 O O   . LYS A 1 90 ? 19.604 13.273  30.840 1.00 43.88  ? 90  LYS A O   1 
ATOM   733 C CB  . LYS A 1 90 ? 20.890 11.559  32.926 1.00 50.65  ? 90  LYS A CB  1 
ATOM   734 C CG  . LYS A 1 90 ? 20.875 10.650  34.143 1.00 56.52  ? 90  LYS A CG  1 
ATOM   735 C CD  . LYS A 1 90 ? 19.501 10.453  34.768 1.00 62.20  ? 90  LYS A CD  1 
ATOM   736 C CE  . LYS A 1 90 ? 19.575 9.617   36.010 1.00 68.28  ? 90  LYS A CE  1 
ATOM   737 N NZ  . LYS A 1 90 ? 18.248 9.133   36.398 1.00 69.51  ? 90  LYS A NZ  1 
ATOM   738 N N   . ASN A 1 91 ? 20.960 11.972  29.612 1.00 38.35  ? 91  ASN A N   1 
ATOM   739 C CA  . ASN A 1 91 ? 21.106 12.953  28.545 1.00 40.62  ? 91  ASN A CA  1 
ATOM   740 C C   . ASN A 1 91 ? 19.983 12.846  27.502 1.00 37.32  ? 91  ASN A C   1 
ATOM   741 O O   . ASN A 1 91 ? 19.983 13.599  26.528 1.00 37.23  ? 91  ASN A O   1 
ATOM   742 C CB  . ASN A 1 91 ? 22.447 12.801  27.832 1.00 43.34  ? 91  ASN A CB  1 
ATOM   743 C CG  . ASN A 1 91 ? 23.622 13.137  28.715 1.00 48.22  ? 91  ASN A CG  1 
ATOM   744 O OD1 . ASN A 1 91 ? 23.462 13.797  29.745 1.00 50.49  ? 91  ASN A OD1 1 
ATOM   745 N ND2 . ASN A 1 91 ? 24.814 12.720  28.314 1.00 50.47  ? 91  ASN A ND2 1 
ATOM   746 N N   . TYR A 1 92 ? 19.029 11.929  27.690 1.00 33.87  ? 92  TYR A N   1 
ATOM   747 C CA  . TYR A 1 92 ? 18.034 11.650  26.654 1.00 31.98  ? 92  TYR A CA  1 
ATOM   748 C C   . TYR A 1 92 ? 16.624 11.677  27.236 1.00 31.96  ? 92  TYR A C   1 
ATOM   749 O O   . TYR A 1 92 ? 15.725 11.038  26.688 1.00 29.74  ? 92  TYR A O   1 
ATOM   750 C CB  . TYR A 1 92 ? 18.348 10.298  25.999 1.00 29.61  ? 92  TYR A CB  1 
ATOM   751 C CG  . TYR A 1 92 ? 19.694 10.307  25.298 1.00 31.27  ? 92  TYR A CG  1 
ATOM   752 C CD1 . TYR A 1 92 ? 19.820 10.757  23.989 1.00 31.52  ? 92  TYR A CD1 1 
ATOM   753 C CD2 . TYR A 1 92 ? 20.859 9.961   25.976 1.00 32.73  ? 92  TYR A CD2 1 
ATOM   754 C CE1 . TYR A 1 92 ? 21.054 10.829  23.362 1.00 32.94  ? 92  TYR A CE1 1 
ATOM   755 C CE2 . TYR A 1 92 ? 22.099 10.033  25.364 1.00 33.15  ? 92  TYR A CE2 1 
ATOM   756 C CZ  . TYR A 1 92 ? 22.199 10.471  24.058 1.00 34.27  ? 92  TYR A CZ  1 
ATOM   757 O OH  . TYR A 1 92 ? 23.423 10.552  23.465 1.00 35.47  ? 92  TYR A OH  1 
ATOM   758 N N   . ASP A 1 93 ? 16.429 12.403  28.346 1.00 35.52  ? 93  ASP A N   1 
ATOM   759 C CA  . ASP A 1 93 ? 15.138 12.432  29.019 1.00 39.19  ? 93  ASP A CA  1 
ATOM   760 C C   . ASP A 1 93 ? 14.279 13.539  28.413 1.00 41.48  ? 93  ASP A C   1 
ATOM   761 O O   . ASP A 1 93 ? 14.607 14.713  28.565 1.00 45.63  ? 93  ASP A O   1 
ATOM   762 C CB  . ASP A 1 93 ? 15.262 12.600  30.530 1.00 43.02  ? 93  ASP A CB  1 
ATOM   763 C CG  . ASP A 1 93 ? 13.964 12.404  31.317 1.00 46.00  ? 93  ASP A CG  1 
ATOM   764 O OD1 . ASP A 1 93 ? 12.879 12.344  30.691 1.00 43.23  ? 93  ASP A OD1 1 
ATOM   765 O OD2 . ASP A 1 93 ? 14.033 12.282  32.558 1.00 50.41  ? 93  ASP A OD2 1 
ATOM   766 N N   . PRO A 1 94 ? 13.141 13.207  27.751 1.00 42.26  ? 94  PRO A N   1 
ATOM   767 C CA  . PRO A 1 94 ? 12.265 14.238  27.198 1.00 46.33  ? 94  PRO A CA  1 
ATOM   768 C C   . PRO A 1 94 ? 11.573 15.111  28.244 1.00 52.47  ? 94  PRO A C   1 
ATOM   769 O O   . PRO A 1 94 ? 10.887 16.061  27.878 1.00 56.80  ? 94  PRO A O   1 
ATOM   770 C CB  . PRO A 1 94 ? 11.251 13.476  26.354 1.00 43.03  ? 94  PRO A CB  1 
ATOM   771 C CG  . PRO A 1 94 ? 11.421 12.012  26.693 1.00 42.98  ? 94  PRO A CG  1 
ATOM   772 C CD  . PRO A 1 94 ? 12.679 11.837  27.495 1.00 40.74  ? 94  PRO A CD  1 
ATOM   773 N N   . TYR A 1 95 ? 11.742 14.786  29.535 1.00 57.41  ? 95  TYR A N   1 
ATOM   774 C CA  . TYR A 1 95 ? 11.130 15.547  30.615 1.00 63.11  ? 95  TYR A CA  1 
ATOM   775 C C   . TYR A 1 95 ? 12.174 16.366  31.375 1.00 73.83  ? 95  TYR A C   1 
ATOM   776 O O   . TYR A 1 95 ? 11.827 17.376  31.986 1.00 77.96  ? 95  TYR A O   1 
ATOM   777 C CB  . TYR A 1 95 ? 10.354 14.603  31.538 1.00 60.99  ? 95  TYR A CB  1 
ATOM   778 C CG  . TYR A 1 95 ? 9.046  14.102  30.938 1.00 54.24  ? 95  TYR A CG  1 
ATOM   779 C CD1 . TYR A 1 95 ? 7.875  14.847  31.048 1.00 54.13  ? 95  TYR A CD1 1 
ATOM   780 C CD2 . TYR A 1 95 ? 8.983  12.897  30.248 1.00 49.93  ? 95  TYR A CD2 1 
ATOM   781 C CE1 . TYR A 1 95 ? 6.682  14.404  30.502 1.00 50.05  ? 95  TYR A CE1 1 
ATOM   782 C CE2 . TYR A 1 95 ? 7.798  12.446  29.691 1.00 47.92  ? 95  TYR A CE2 1 
ATOM   783 C CZ  . TYR A 1 95 ? 6.642  13.198  29.825 1.00 49.55  ? 95  TYR A CZ  1 
ATOM   784 O OH  . TYR A 1 95 ? 5.468  12.769  29.282 1.00 49.13  ? 95  TYR A OH  1 
ATOM   785 N N   . LYS A 1 96 ? 13.446 15.946  31.338 1.00 78.70  ? 96  LYS A N   1 
ATOM   786 C CA  . LYS A 1 96 ? 14.521 16.759  31.887 1.00 86.61  ? 96  LYS A CA  1 
ATOM   787 C C   . LYS A 1 96 ? 15.615 16.957  30.837 1.00 90.78  ? 96  LYS A C   1 
ATOM   788 O O   . LYS A 1 96 ? 16.673 16.333  30.915 1.00 88.80  ? 96  LYS A O   1 
ATOM   789 C CB  . LYS A 1 96 ? 15.087 16.175  33.188 1.00 90.12  ? 96  LYS A CB  1 
ATOM   790 C CG  . LYS A 1 96 ? 16.141 17.060  33.854 1.00 96.90  ? 96  LYS A CG  1 
ATOM   791 C CD  . LYS A 1 96 ? 16.505 16.711  35.293 1.00 99.48  ? 96  LYS A CD  1 
ATOM   792 C CE  . LYS A 1 96 ? 17.540 17.649  35.834 1.00 102.62 ? 96  LYS A CE  1 
ATOM   793 N NZ  . LYS A 1 96 ? 17.954 17.289  37.192 1.00 106.35 ? 96  LYS A NZ  1 
ATOM   794 N N   . PRO A 1 97 ? 15.386 17.812  29.810 1.00 94.53  ? 97  PRO A N   1 
ATOM   795 C CA  . PRO A 1 97 ? 16.478 18.364  29.017 1.00 95.81  ? 97  PRO A CA  1 
ATOM   796 C C   . PRO A 1 97 ? 17.411 19.253  29.835 1.00 97.82  ? 97  PRO A C   1 
ATOM   797 O O   . PRO A 1 97 ? 18.637 19.188  29.590 1.00 97.62  ? 97  PRO A O   1 
ATOM   798 C CB  . PRO A 1 97 ? 15.769 19.152  27.915 1.00 97.53  ? 97  PRO A CB  1 
ATOM   799 C CG  . PRO A 1 97 ? 14.350 18.608  27.903 1.00 94.62  ? 97  PRO A CG  1 
ATOM   800 C CD  . PRO A 1 97 ? 14.063 18.227  29.317 1.00 94.46  ? 97  PRO A CD  1 
HETATM 801 S S   . SO4 B 2 .  ? -3.219 12.706  32.867 1.00 97.71  ? 201 SO4 A S   1 
HETATM 802 O O1  . SO4 B 2 .  ? -3.444 12.754  31.446 1.00 103.25 ? 201 SO4 A O1  1 
HETATM 803 O O2  . SO4 B 2 .  ? -3.832 11.523  33.407 1.00 92.63  ? 201 SO4 A O2  1 
HETATM 804 O O3  . SO4 B 2 .  ? -1.805 12.677  33.124 1.00 101.23 ? 201 SO4 A O3  1 
HETATM 805 O O4  . SO4 B 2 .  ? -3.790 13.873  33.488 1.00 98.99  ? 201 SO4 A O4  1 
HETATM 806 O O   . HOH C 3 .  ? 22.507 7.965   15.927 1.00 38.87  ? 301 HOH A O   1 
HETATM 807 O O   . HOH C 3 .  ? 18.028 14.545  29.463 1.00 43.81  ? 302 HOH A O   1 
HETATM 808 O O   . HOH C 3 .  ? -0.573 7.889   28.122 1.00 48.85  ? 303 HOH A O   1 
HETATM 809 O O   . HOH C 3 .  ? -3.503 9.517   34.831 1.00 45.64  ? 304 HOH A O   1 
HETATM 810 O O   . HOH C 3 .  ? 16.335 10.402  15.982 1.00 46.46  ? 305 HOH A O   1 
HETATM 811 O O   . HOH C 3 .  ? 20.879 1.496   14.685 1.00 29.37  ? 306 HOH A O   1 
HETATM 812 O O   . HOH C 3 .  ? 31.500 7.366   22.698 1.00 46.51  ? 307 HOH A O   1 
HETATM 813 O O   . HOH C 3 .  ? 18.184 -9.694  23.605 1.00 40.09  ? 308 HOH A O   1 
HETATM 814 O O   . HOH C 3 .  ? 15.326 1.372   35.558 1.00 55.11  ? 309 HOH A O   1 
HETATM 815 O O   . HOH C 3 .  ? 13.836 -5.538  35.159 1.00 51.98  ? 310 HOH A O   1 
HETATM 816 O O   . HOH C 3 .  ? 22.592 -4.716  16.067 1.00 52.56  ? 311 HOH A O   1 
HETATM 817 O O   . HOH C 3 .  ? 12.323 7.116   37.258 1.00 47.11  ? 312 HOH A O   1 
HETATM 818 O O   . HOH C 3 .  ? 29.062 2.830   14.815 1.00 49.71  ? 313 HOH A O   1 
HETATM 819 O O   . HOH C 3 .  ? 25.381 10.999  25.089 1.00 38.45  ? 314 HOH A O   1 
HETATM 820 O O   . HOH C 3 .  ? -1.944 -0.754  35.640 1.00 36.41  ? 315 HOH A O   1 
HETATM 821 O O   . HOH C 3 .  ? 31.932 0.729   13.931 1.00 59.11  ? 316 HOH A O   1 
HETATM 822 O O   . HOH C 3 .  ? 9.602  17.379  20.448 1.00 68.55  ? 317 HOH A O   1 
HETATM 823 O O   . HOH C 3 .  ? 23.219 -3.105  29.985 1.00 36.73  ? 318 HOH A O   1 
HETATM 824 O O   . HOH C 3 .  ? 26.255 -4.776  21.929 1.00 38.73  ? 319 HOH A O   1 
HETATM 825 O O   . HOH C 3 .  ? -2.441 5.767   31.363 1.00 34.46  ? 320 HOH A O   1 
HETATM 826 O O   . HOH C 3 .  ? 13.605 -2.025  10.209 1.00 38.10  ? 321 HOH A O   1 
HETATM 827 O O   . HOH C 3 .  ? 12.278 -1.332  37.159 1.00 41.60  ? 322 HOH A O   1 
HETATM 828 O O   . HOH C 3 .  ? 16.437 9.371   31.314 1.00 36.12  ? 323 HOH A O   1 
HETATM 829 O O   . HOH C 3 .  ? 10.390 12.129  23.205 1.00 35.18  ? 324 HOH A O   1 
HETATM 830 O O   . HOH C 3 .  ? -2.714 2.522   18.660 1.00 51.79  ? 325 HOH A O   1 
HETATM 831 O O   . HOH C 3 .  ? 19.315 -3.048  33.791 1.00 46.84  ? 326 HOH A O   1 
HETATM 832 O O   . HOH C 3 .  ? 10.286 16.428  25.321 1.00 70.64  ? 327 HOH A O   1 
HETATM 833 O O   . HOH C 3 .  ? 19.403 -3.997  14.257 1.00 31.81  ? 328 HOH A O   1 
HETATM 834 O O   . HOH C 3 .  ? 22.589 4.953   31.083 1.00 30.89  ? 329 HOH A O   1 
HETATM 835 O O   . HOH C 3 .  ? 28.692 7.828   28.692 0.50 42.55  ? 330 HOH A O   1 
HETATM 836 O O   . HOH C 3 .  ? 0.188  1.843   28.298 1.00 37.65  ? 331 HOH A O   1 
HETATM 837 O O   . HOH C 3 .  ? 18.003 14.027  32.849 1.00 47.88  ? 332 HOH A O   1 
HETATM 838 O O   . HOH C 3 .  ? 6.202  -3.568  16.152 1.00 60.07  ? 333 HOH A O   1 
HETATM 839 O O   . HOH C 3 .  ? 28.965 9.338   26.458 1.00 42.04  ? 334 HOH A O   1 
HETATM 840 O O   . HOH C 3 .  ? 7.828  10.066  36.490 1.00 46.77  ? 335 HOH A O   1 
HETATM 841 O O   . HOH C 3 .  ? 22.322 3.706   15.377 1.00 27.60  ? 336 HOH A O   1 
HETATM 842 O O   . HOH C 3 .  ? 16.308 -6.071  34.150 1.00 52.66  ? 337 HOH A O   1 
HETATM 843 O O   . HOH C 3 .  ? 11.059 18.617  29.680 1.00 58.65  ? 338 HOH A O   1 
HETATM 844 O O   . HOH C 3 .  ? 4.525  7.650   11.360 1.00 49.53  ? 339 HOH A O   1 
HETATM 845 O O   . HOH C 3 .  ? 19.940 13.199  20.586 1.00 58.71  ? 340 HOH A O   1 
HETATM 846 O O   . HOH C 3 .  ? 20.639 2.969   31.014 1.00 36.88  ? 341 HOH A O   1 
HETATM 847 O O   . HOH C 3 .  ? 12.474 9.554   13.654 1.00 47.17  ? 342 HOH A O   1 
HETATM 848 O O   . HOH C 3 .  ? 16.492 8.549   34.239 1.00 46.62  ? 343 HOH A O   1 
HETATM 849 O O   . HOH C 3 .  ? 26.371 -2.031  28.566 1.00 43.83  ? 344 HOH A O   1 
HETATM 850 O O   . HOH C 3 .  ? 11.348 -7.153  16.558 1.00 50.99  ? 345 HOH A O   1 
HETATM 851 O O   . HOH C 3 .  ? 0.588  9.474   23.411 1.00 37.82  ? 346 HOH A O   1 
HETATM 852 O O   . HOH C 3 .  ? 1.217  0.522   33.163 1.00 31.83  ? 347 HOH A O   1 
HETATM 853 O O   . HOH C 3 .  ? 1.364  -3.325  31.886 1.00 31.30  ? 348 HOH A O   1 
HETATM 854 O O   . HOH C 3 .  ? -4.749 5.498   16.602 1.00 54.88  ? 349 HOH A O   1 
HETATM 855 O O   . HOH C 3 .  ? 31.914 0.129   24.718 1.00 49.24  ? 350 HOH A O   1 
HETATM 856 O O   . HOH C 3 .  ? 10.608 11.101  18.357 1.00 34.01  ? 351 HOH A O   1 
HETATM 857 O O   . HOH C 3 .  ? 17.111 -7.830  29.015 1.00 45.29  ? 352 HOH A O   1 
HETATM 858 O O   . HOH C 3 .  ? 31.895 5.045   22.553 1.00 48.82  ? 353 HOH A O   1 
HETATM 859 O O   . HOH C 3 .  ? 3.736  -0.190  39.312 1.00 48.77  ? 354 HOH A O   1 
HETATM 860 O O   . HOH C 3 .  ? 0.891  4.855   26.560 1.00 39.36  ? 355 HOH A O   1 
HETATM 861 O O   . HOH C 3 .  ? 16.632 12.336  33.745 1.00 53.52  ? 356 HOH A O   1 
HETATM 862 O O   . HOH C 3 .  ? 28.209 -0.387  27.184 1.00 39.16  ? 357 HOH A O   1 
HETATM 863 O O   . HOH C 3 .  ? 15.384 -4.169  11.586 1.00 46.19  ? 358 HOH A O   1 
HETATM 864 O O   . HOH C 3 .  ? 30.322 -2.781  22.509 1.00 47.17  ? 359 HOH A O   1 
HETATM 865 O O   . HOH C 3 .  ? 13.712 9.290   33.662 1.00 36.13  ? 360 HOH A O   1 
HETATM 866 O O   . HOH C 3 .  ? 27.543 0.231   15.565 1.00 56.84  ? 361 HOH A O   1 
HETATM 867 O O   . HOH C 3 .  ? 28.692 1.844   28.692 0.50 33.15  ? 362 HOH A O   1 
HETATM 868 O O   . HOH C 3 .  ? 5.297  1.648   20.284 1.00 33.29  ? 363 HOH A O   1 
HETATM 869 O O   . HOH C 3 .  ? 33.202 2.155   20.190 1.00 68.31  ? 364 HOH A O   1 
HETATM 870 O O   . HOH C 3 .  ? 2.852  -5.680  25.363 1.00 44.93  ? 365 HOH A O   1 
HETATM 871 O O   . HOH C 3 .  ? 10.382 -9.908  18.473 1.00 65.25  ? 366 HOH A O   1 
HETATM 872 O O   . HOH C 3 .  ? 26.531 9.730   27.438 1.00 47.50  ? 367 HOH A O   1 
HETATM 873 O O   . HOH C 3 .  ? 11.651 12.535  34.293 1.00 52.00  ? 368 HOH A O   1 
HETATM 874 O O   . HOH C 3 .  ? -0.679 6.596   40.371 1.00 45.72  ? 369 HOH A O   1 
HETATM 875 O O   . HOH C 3 .  ? 26.641 -1.602  18.423 1.00 55.93  ? 370 HOH A O   1 
HETATM 876 O O   . HOH C 3 .  ? 23.533 -5.390  33.756 1.00 51.70  ? 371 HOH A O   1 
HETATM 877 O O   . HOH C 3 .  ? 9.698  -8.052  27.520 1.00 62.04  ? 372 HOH A O   1 
HETATM 878 O O   . HOH C 3 .  ? 18.411 13.583  22.321 1.00 52.38  ? 373 HOH A O   1 
HETATM 879 O O   . HOH C 3 .  ? 15.011 0.765   2.955  1.00 58.97  ? 374 HOH A O   1 
HETATM 880 O O   . HOH C 3 .  ? 5.297  3.539   8.367  1.00 48.39  ? 375 HOH A O   1 
HETATM 881 O O   . HOH C 3 .  ? 12.446 -0.397  41.256 1.00 71.22  ? 376 HOH A O   1 
HETATM 882 O O   . HOH C 3 .  ? 4.937  13.569  37.847 1.00 50.49  ? 377 HOH A O   1 
HETATM 883 O O   . HOH C 3 .  ? -0.241 2.664   24.901 1.00 50.97  ? 378 HOH A O   1 
HETATM 884 O O   . HOH C 3 .  ? 0.729  2.037   30.731 1.00 34.20  ? 379 HOH A O   1 
HETATM 885 O O   . HOH C 3 .  ? -2.701 7.481   20.544 1.00 44.85  ? 380 HOH A O   1 
HETATM 886 O O   . HOH C 3 .  ? 11.935 -8.800  23.620 1.00 36.83  ? 381 HOH A O   1 
HETATM 887 O O   . HOH C 3 .  ? 7.109  11.214  17.088 1.00 35.69  ? 382 HOH A O   1 
HETATM 888 O O   . HOH C 3 .  ? 2.459  6.424   25.181 1.00 45.15  ? 383 HOH A O   1 
HETATM 889 O O   . HOH C 3 .  ? 27.405 12.553  30.160 1.00 56.60  ? 384 HOH A O   1 
HETATM 890 O O   . HOH C 3 .  ? 6.627  0.865   35.841 1.00 39.36  ? 385 HOH A O   1 
HETATM 891 O O   . HOH C 3 .  ? 14.952 10.905  19.700 1.00 39.73  ? 386 HOH A O   1 
HETATM 892 O O   . HOH C 3 .  ? 2.255  1.401   39.825 1.00 53.48  ? 387 HOH A O   1 
HETATM 893 O O   . HOH C 3 .  ? -4.206 0.456   36.372 1.00 38.82  ? 388 HOH A O   1 
HETATM 894 O O   . HOH C 3 .  ? 18.966 7.280   38.998 1.00 66.09  ? 389 HOH A O   1 
HETATM 895 O O   . HOH C 3 .  ? 1.920  1.014   17.258 1.00 63.70  ? 390 HOH A O   1 
HETATM 896 O O   . HOH C 3 .  ? 28.239 -5.720  25.549 1.00 53.28  ? 391 HOH A O   1 
HETATM 897 O O   . HOH C 3 .  ? 4.685  -7.627  38.114 1.00 66.97  ? 392 HOH A O   1 
HETATM 898 O O   . HOH C 3 .  ? 4.918  -6.867  24.491 1.00 42.69  ? 393 HOH A O   1 
HETATM 899 O O   . HOH C 3 .  ? 7.900  2.649   7.185  1.00 47.05  ? 394 HOH A O   1 
HETATM 900 O O   . HOH C 3 .  ? 13.746 9.008   16.298 1.00 43.55  ? 395 HOH A O   1 
HETATM 901 O O   . HOH C 3 .  ? 34.119 4.787   23.660 1.00 46.99  ? 396 HOH A O   1 
HETATM 902 O O   . HOH C 3 .  ? -0.000 -0.000  40.474 0.50 46.21  ? 397 HOH A O   1 
HETATM 903 O O   . HOH C 3 .  ? 16.203 8.463   13.199 1.00 46.35  ? 398 HOH A O   1 
HETATM 904 O O   . HOH C 3 .  ? 14.693 -0.736  39.875 1.00 57.73  ? 399 HOH A O   1 
HETATM 905 O O   . HOH C 3 .  ? 21.106 6.408   35.239 1.00 45.04  ? 400 HOH A O   1 
HETATM 906 O O   . HOH C 3 .  ? 14.859 -0.446  37.237 1.00 59.39  ? 401 HOH A O   1 
HETATM 907 O O   . HOH C 3 .  ? 23.199 -11.470 34.140 1.00 65.35  ? 402 HOH A O   1 
HETATM 908 O O   . HOH C 3 .  ? 6.869  11.946  37.951 1.00 59.62  ? 403 HOH A O   1 
HETATM 909 O O   . HOH C 3 .  ? 10.554 9.522   37.481 1.00 51.30  ? 404 HOH A O   1 
HETATM 910 O O   . HOH C 3 .  ? 20.524 5.915   37.624 1.00 59.42  ? 405 HOH A O   1 
HETATM 911 O O   . HOH C 3 .  ? 30.497 -1.530  26.198 1.00 44.94  ? 406 HOH A O   1 
HETATM 912 O O   . HOH C 3 .  ? 22.186 -3.237  33.991 1.00 53.48  ? 407 HOH A O   1 
HETATM 913 O O   . HOH C 3 .  ? 6.521  0.179   18.173 1.00 53.66  ? 408 HOH A O   1 
HETATM 914 O O   . HOH C 3 .  ? 28.692 9.485   28.692 0.50 41.22  ? 409 HOH A O   1 
HETATM 915 O O   . HOH C 3 .  ? 28.692 11.784  28.692 0.50 47.62  ? 410 HOH A O   1 
HETATM 916 O O   . HOH C 3 .  ? 33.767 1.817   22.974 1.00 65.62  ? 411 HOH A O   1 
HETATM 917 O O   . HOH C 3 .  ? 18.975 -0.580  33.653 1.00 42.15  ? 412 HOH A O   1 
HETATM 918 O O   . HOH C 3 .  ? 26.100 -8.821  31.859 1.00 57.62  ? 413 HOH A O   1 
HETATM 919 O O   . HOH C 3 .  ? -1.332 6.018   22.185 1.00 51.08  ? 414 HOH A O   1 
HETATM 920 O O   . HOH C 3 .  ? 3.253  -1.939  40.954 1.00 50.63  ? 415 HOH A O   1 
HETATM 921 O O   . HOH C 3 .  ? 21.040 0.628   32.505 1.00 44.45  ? 416 HOH A O   1 
HETATM 922 O O   . HOH C 3 .  ? -0.000 -0.000  29.740 0.50 54.18  ? 417 HOH A O   1 
HETATM 923 O O   . HOH C 3 .  ? -1.432 2.072   20.804 1.00 52.44  ? 418 HOH A O   1 
HETATM 924 O O   . HOH C 3 .  ? 21.092 10.248  39.127 1.00 67.08  ? 419 HOH A O   1 
HETATM 925 O O   . HOH C 3 .  ? 10.339 10.339  10.339 0.33 65.05  ? 420 HOH A O   1 
HETATM 926 O O   . HOH C 3 .  ? 4.717  -1.632  17.015 1.00 56.94  ? 421 HOH A O   1 
HETATM 927 O O   . HOH C 3 .  ? -4.128 9.976   37.651 1.00 47.51  ? 422 HOH A O   1 
HETATM 928 O O   . HOH C 3 .  ? 22.967 -1.418  32.079 1.00 37.55  ? 423 HOH A O   1 
HETATM 929 O O   . HOH C 3 .  ? 17.950 4.135   39.286 1.00 60.96  ? 424 HOH A O   1 
HETATM 930 O O   . HOH C 3 .  ? 11.755 -3.051  8.369  1.00 52.25  ? 425 HOH A O   1 
HETATM 931 O O   . HOH C 3 .  ? 5.017  6.222   8.619  1.00 51.52  ? 426 HOH A O   1 
HETATM 932 O O   . HOH C 3 .  ? 12.888 -8.256  35.807 1.00 49.17  ? 427 HOH A O   1 
HETATM 933 O O   . HOH C 3 .  ? 11.634 16.287  36.252 1.00 61.23  ? 428 HOH A O   1 
HETATM 934 O O   . HOH C 3 .  ? 30.141 -3.855  24.729 1.00 49.63  ? 429 HOH A O   1 
HETATM 935 O O   . HOH C 3 .  ? -0.664 1.450   16.683 1.00 61.10  ? 430 HOH A O   1 
HETATM 936 O O   . HOH C 3 .  ? 6.961  6.961   6.961  0.33 39.28  ? 431 HOH A O   1 
HETATM 937 O O   . HOH C 3 .  ? 26.965 14.699  22.696 1.00 57.64  ? 432 HOH A O   1 
HETATM 938 O O   . HOH C 3 .  ? -4.965 12.263  41.957 1.00 61.03  ? 433 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  ? 0.5199 0.5695 0.7444 0.2085  0.1177  0.2302  4  GLY A N   
2   C CA  . GLY A 4  ? 0.4694 0.5393 0.6753 0.1809  0.1011  0.1974  4  GLY A CA  
3   C C   . GLY A 4  ? 0.4260 0.5499 0.6178 0.1636  0.0742  0.1985  4  GLY A C   
4   O O   . GLY A 4  ? 0.4251 0.5740 0.6167 0.1706  0.0670  0.2216  4  GLY A O   
5   N N   . ILE A 5  ? 0.4059 0.5452 0.5853 0.1402  0.0613  0.1723  5  ILE A N   
6   C CA  . ILE A 5  ? 0.3839 0.5733 0.5544 0.1227  0.0386  0.1670  5  ILE A CA  
7   C C   . ILE A 5  ? 0.3832 0.5550 0.5315 0.1098  0.0300  0.1640  5  ILE A C   
8   O O   . ILE A 5  ? 0.3487 0.5643 0.4904 0.1009  0.0139  0.1637  5  ILE A O   
9   C CB  . ILE A 5  ? 0.3757 0.5727 0.5414 0.1008  0.0319  0.1408  5  ILE A CB  
10  C CG1 . ILE A 5  ? 0.3633 0.4996 0.5084 0.0857  0.0384  0.1184  5  ILE A CG1 
11  C CG2 . ILE A 5  ? 0.3863 0.6207 0.5773 0.1122  0.0386  0.1468  5  ILE A CG2 
12  C CD1 . ILE A 5  ? 0.3553 0.4975 0.4942 0.0654  0.0327  0.0991  5  ILE A CD1 
13  N N   . PHE A 6  ? 0.3929 0.5048 0.5307 0.1073  0.0414  0.1592  6  PHE A N   
14  C CA  . PHE A 6  ? 0.3923 0.4902 0.5120 0.0946  0.0350  0.1564  6  PHE A CA  
15  C C   . PHE A 6  ? 0.4250 0.5139 0.5513 0.1112  0.0455  0.1860  6  PHE A C   
16  O O   . PHE A 6  ? 0.4330 0.4982 0.5479 0.1017  0.0472  0.1857  6  PHE A O   
17  C CB  . PHE A 6  ? 0.3879 0.4351 0.4924 0.0760  0.0385  0.1303  6  PHE A CB  
18  C CG  . PHE A 6  ? 0.3619 0.4154 0.4578 0.0602  0.0290  0.1063  6  PHE A CG  
19  C CD1 . PHE A 6  ? 0.3494 0.4418 0.4424 0.0507  0.0135  0.1003  6  PHE A CD1 
20  C CD2 . PHE A 6  ? 0.3774 0.3975 0.4678 0.0538  0.0372  0.0895  6  PHE A CD2 
21  C CE1 . PHE A 6  ? 0.3437 0.4339 0.4316 0.0362  0.0081  0.0818  6  PHE A CE1 
22  C CE2 . PHE A 6  ? 0.3528 0.3792 0.4350 0.0409  0.0301  0.0738  6  PHE A CE2 
23  C CZ  . PHE A 6  ? 0.3374 0.3955 0.4201 0.0325  0.0164  0.0718  6  PHE A CZ  
24  N N   . ALA A 7  ? 0.4445 0.5566 0.5913 0.1366  0.0531  0.2147  7  ALA A N   
25  C CA  . ALA A 7  ? 0.4803 0.5886 0.6354 0.1557  0.0639  0.2508  7  ALA A CA  
26  C C   . ALA A 7  ? 0.4651 0.6098 0.6013 0.1452  0.0496  0.2582  7  ALA A C   
27  O O   . ALA A 7  ? 0.4505 0.6526 0.5766 0.1362  0.0301  0.2478  7  ALA A O   
28  C CB  . ALA A 7  ? 0.5015 0.6496 0.6819 0.1873  0.0692  0.2840  7  ALA A CB  
29  N N   . ASN A 8  ? 0.4693 0.5789 0.6016 0.1443  0.0613  0.2733  8  ASN A N   
30  C CA  . ASN A 8  ? 0.4826 0.6256 0.5977 0.1371  0.0527  0.2847  8  ASN A CA  
31  C C   . ASN A 8  ? 0.4412 0.5911 0.5340 0.1092  0.0371  0.2464  8  ASN A C   
32  O O   . ASN A 8  ? 0.4378 0.6253 0.5150 0.1027  0.0282  0.2489  8  ASN A O   
33  C CB  . ASN A 8  ? 0.4905 0.7128 0.6066 0.1564  0.0425  0.3169  8  ASN A CB  
34  C CG  . ASN A 8  ? 0.5486 0.7637 0.6877 0.1882  0.0604  0.3645  8  ASN A CG  
35  O OD1 . ASN A 8  ? 0.5980 0.7724 0.7411 0.1935  0.0784  0.3896  8  ASN A OD1 
36  N ND2 . ASN A 8  ? 0.5407 0.7958 0.6980 0.2100  0.0574  0.3791  8  ASN A ND2 
37  N N   . CYS A 9  ? 0.4306 0.5457 0.5220 0.0943  0.0352  0.2125  9  CYS A N   
38  C CA  . CYS A 9  ? 0.3948 0.5086 0.4689 0.0717  0.0236  0.1806  9  CYS A CA  
39  C C   . CYS A 9  ? 0.4044 0.4661 0.4764 0.0593  0.0346  0.1723  9  CYS A C   
40  O O   . CYS A 9  ? 0.4126 0.4276 0.4953 0.0608  0.0488  0.1722  9  CYS A O   
41  C CB  . CYS A 9  ? 0.3874 0.5023 0.4607 0.0626  0.0140  0.1524  9  CYS A CB  
42  S SG  . CYS A 9  ? 0.4210 0.6025 0.5012 0.0702  0.0007  0.1564  9  CYS A SG  
43  N N   . ILE A 10 ? 0.4127 0.4874 0.4721 0.0468  0.0288  0.1641  10 ILE A N   
44  C CA  . ILE A 10 ? 0.4333 0.4732 0.4918 0.0317  0.0361  0.1534  10 ILE A CA  
45  C C   . ILE A 10 ? 0.4068 0.4586 0.4539 0.0183  0.0225  0.1238  10 ILE A C   
46  O O   . ILE A 10 ? 0.3825 0.4714 0.4200 0.0178  0.0133  0.1199  10 ILE A O   
47  C CB  . ILE A 10 ? 0.4607 0.5081 0.5202 0.0320  0.0461  0.1785  10 ILE A CB  
48  C CG1 . ILE A 10 ? 0.5081 0.5434 0.5813 0.0498  0.0611  0.2147  10 ILE A CG1 
49  C CG2 . ILE A 10 ? 0.4885 0.5070 0.5511 0.0128  0.0536  0.1659  10 ILE A CG2 
50  C CD1 . ILE A 10 ? 0.5571 0.5906 0.6338 0.0492  0.0753  0.2443  10 ILE A CD1 
51  N N   . PHE A 11 ? 0.4050 0.4263 0.4533 0.0091  0.0224  0.1035  11 PHE A N   
52  C CA  . PHE A 11 ? 0.3768 0.4056 0.4173 0.0008  0.0109  0.0802  11 PHE A CA  
53  C C   . PHE A 11 ? 0.3915 0.4137 0.4320 -0.0114 0.0125  0.0712  11 PHE A C   
54  O O   . PHE A 11 ? 0.4236 0.4199 0.4697 -0.0199 0.0208  0.0687  11 PHE A O   
55  C CB  . PHE A 11 ? 0.3858 0.3952 0.4266 0.0002  0.0091  0.0676  11 PHE A CB  
56  C CG  . PHE A 11 ? 0.3832 0.4057 0.4274 0.0104  0.0068  0.0735  11 PHE A CG  
57  C CD1 . PHE A 11 ? 0.3684 0.4148 0.4095 0.0093  -0.0039 0.0646  11 PHE A CD1 
58  C CD2 . PHE A 11 ? 0.3987 0.4099 0.4526 0.0207  0.0168  0.0871  11 PHE A CD2 
59  C CE1 . PHE A 11 ? 0.3685 0.4334 0.4160 0.0149  -0.0062 0.0684  11 PHE A CE1 
60  C CE2 . PHE A 11 ? 0.4119 0.4439 0.4724 0.0305  0.0144  0.0932  11 PHE A CE2 
61  C CZ  . PHE A 11 ? 0.3629 0.4247 0.4204 0.0259  0.0020  0.0835  11 PHE A CZ  
62  N N   . CYS A 12 ? 0.3593 0.4076 0.3952 -0.0129 0.0054  0.0643  12 CYS A N   
63  C CA  . CYS A 12 ? 0.3563 0.4075 0.3946 -0.0222 0.0038  0.0527  12 CYS A CA  
64  C C   . CYS A 12 ? 0.3231 0.3664 0.3587 -0.0221 -0.0046 0.0374  12 CYS A C   
65  O O   . CYS A 12 ? 0.3290 0.3773 0.3606 -0.0151 -0.0108 0.0325  12 CYS A O   
66  C CB  . CYS A 12 ? 0.3680 0.4517 0.4050 -0.0203 0.0023  0.0521  12 CYS A CB  
67  S SG  . CYS A 12 ? 0.3667 0.4643 0.4121 -0.0278 0.0000  0.0397  12 CYS A SG  
68  N N   . LEU A 13 ? 0.3243 0.3564 0.3620 -0.0312 -0.0040 0.0303  13 LEU A N   
69  C CA  . LEU A 13 ? 0.3100 0.3403 0.3429 -0.0302 -0.0114 0.0207  13 LEU A CA  
70  C C   . LEU A 13 ? 0.2976 0.3523 0.3350 -0.0312 -0.0176 0.0158  13 LEU A C   
71  O O   . LEU A 13 ? 0.2951 0.3626 0.3386 -0.0419 -0.0162 0.0127  13 LEU A O   
72  C CB  . LEU A 13 ? 0.3334 0.3439 0.3627 -0.0382 -0.0070 0.0152  13 LEU A CB  
73  C CG  . LEU A 13 ? 0.3608 0.3479 0.3899 -0.0335 0.0014  0.0210  13 LEU A CG  
74  C CD1 . LEU A 13 ? 0.3906 0.3579 0.4159 -0.0413 0.0082  0.0101  13 LEU A CD1 
75  C CD2 . LEU A 13 ? 0.3452 0.3369 0.3716 -0.0219 -0.0034 0.0260  13 LEU A CD2 
76  N N   . LYS A 14 ? 0.2909 0.3532 0.3283 -0.0197 -0.0230 0.0152  14 LYS A N   
77  C CA  . LYS A 14 ? 0.3036 0.3873 0.3476 -0.0140 -0.0283 0.0137  14 LYS A CA  
78  C C   . LYS A 14 ? 0.2925 0.3670 0.3316 -0.0070 -0.0332 0.0163  14 LYS A C   
79  O O   . LYS A 14 ? 0.2853 0.3506 0.3271 0.0043  -0.0332 0.0182  14 LYS A O   
80  C CB  . LYS A 14 ? 0.3574 0.4524 0.4080 -0.0033 -0.0263 0.0119  14 LYS A CB  
81  C CG  . LYS A 14 ? 0.4114 0.5238 0.4652 -0.0086 -0.0204 0.0124  14 LYS A CG  
82  C CD  . LYS A 14 ? 0.4621 0.5987 0.5258 -0.0191 -0.0191 0.0142  14 LYS A CD  
83  C CE  . LYS A 14 ? 0.4663 0.6215 0.5344 -0.0236 -0.0108 0.0181  14 LYS A CE  
84  N NZ  . LYS A 14 ? 0.4582 0.6334 0.5386 -0.0392 -0.0072 0.0201  14 LYS A NZ  
85  N N   . VAL A 15 ? 0.2986 0.3748 0.3302 -0.0151 -0.0356 0.0158  15 VAL A N   
86  C CA  . VAL A 15 ? 0.3195 0.3899 0.3425 -0.0099 -0.0387 0.0214  15 VAL A CA  
87  C C   . VAL A 15 ? 0.3259 0.4286 0.3452 -0.0131 -0.0457 0.0224  15 VAL A C   
88  O O   . VAL A 15 ? 0.3348 0.4402 0.3406 -0.0172 -0.0472 0.0227  15 VAL A O   
89  C CB  . VAL A 15 ? 0.3311 0.3760 0.3438 -0.0162 -0.0332 0.0186  15 VAL A CB  
90  C CG1 . VAL A 15 ? 0.3359 0.3614 0.3536 -0.0117 -0.0289 0.0198  15 VAL A CG1 
91  C CG2 . VAL A 15 ? 0.3333 0.3762 0.3419 -0.0304 -0.0288 0.0085  15 VAL A CG2 
92  N N   . LYS A 16 ? 0.3138 0.4480 0.3458 -0.0102 -0.0501 0.0234  16 LYS A N   
93  C CA  . LYS A 16 ? 0.3173 0.4964 0.3499 -0.0156 -0.0584 0.0228  16 LYS A CA  
94  C C   . LYS A 16 ? 0.3203 0.5157 0.3421 -0.0050 -0.0649 0.0362  16 LYS A C   
95  O O   . LYS A 16 ? 0.3317 0.5662 0.3453 -0.0140 -0.0724 0.0328  16 LYS A O   
96  C CB  . LYS A 16 ? 0.3360 0.5492 0.3896 -0.0075 -0.0611 0.0265  16 LYS A CB  
97  C CG  . LYS A 16 ? 0.3749 0.6491 0.4360 -0.0095 -0.0715 0.0290  16 LYS A CG  
98  C CD  . LYS A 16 ? 0.3970 0.7097 0.4831 -0.0032 -0.0721 0.0311  16 LYS A CD  
99  C CE  . LYS A 16 ? 0.4319 0.8160 0.5290 -0.0046 -0.0838 0.0349  16 LYS A CE  
100 N NZ  . LYS A 16 ? 0.4427 0.8674 0.5667 -0.0037 -0.0823 0.0335  16 LYS A NZ  
101 N N   . TYR A 17 ? 0.3151 0.4855 0.3381 0.0133  -0.0618 0.0520  17 TYR A N   
102 C CA  . TYR A 17 ? 0.3550 0.5420 0.3721 0.0277  -0.0659 0.0729  17 TYR A CA  
103 C C   . TYR A 17 ? 0.3653 0.5286 0.3619 0.0216  -0.0616 0.0752  17 TYR A C   
104 O O   . TYR A 17 ? 0.3976 0.5737 0.3857 0.0318  -0.0632 0.0951  17 TYR A O   
105 C CB  . TYR A 17 ? 0.3624 0.5379 0.3988 0.0528  -0.0624 0.0917  17 TYR A CB  
106 C CG  . TYR A 17 ? 0.3605 0.5733 0.4172 0.0613  -0.0666 0.0906  17 TYR A CG  
107 C CD1 . TYR A 17 ? 0.3647 0.6381 0.4259 0.0682  -0.0771 0.1028  17 TYR A CD1 
108 C CD2 . TYR A 17 ? 0.3486 0.5450 0.4195 0.0607  -0.0603 0.0766  17 TYR A CD2 
109 C CE1 . TYR A 17 ? 0.3690 0.6845 0.4523 0.0752  -0.0806 0.1017  17 TYR A CE1 
110 C CE2 . TYR A 17 ? 0.3473 0.5826 0.4375 0.0676  -0.0623 0.0752  17 TYR A CE2 
111 C CZ  . TYR A 17 ? 0.3616 0.6560 0.4599 0.0749  -0.0722 0.0878  17 TYR A CZ  
112 O OH  . TYR A 17 ? 0.3960 0.7342 0.5171 0.0817  -0.0734 0.0865  17 TYR A OH  
113 N N   . LEU A 18 ? 0.3485 0.4833 0.3377 0.0061  -0.0554 0.0572  18 LEU A N   
114 C CA  . LEU A 18 ? 0.3730 0.4939 0.3440 -0.0001 -0.0503 0.0567  18 LEU A CA  
115 C C   . LEU A 18 ? 0.3877 0.5486 0.3393 -0.0113 -0.0557 0.0481  18 LEU A C   
116 O O   . LEU A 18 ? 0.3863 0.5708 0.3399 -0.0236 -0.0605 0.0313  18 LEU A O   
117 C CB  . LEU A 18 ? 0.3590 0.4432 0.3314 -0.0100 -0.0414 0.0413  18 LEU A CB  
118 C CG  . LEU A 18 ? 0.3759 0.4268 0.3630 -0.0026 -0.0361 0.0464  18 LEU A CG  
119 C CD1 . LEU A 18 ? 0.3826 0.4126 0.3686 -0.0117 -0.0290 0.0341  18 LEU A CD1 
120 C CD2 . LEU A 18 ? 0.3957 0.4335 0.3852 0.0075  -0.0329 0.0648  18 LEU A CD2 
121 N N   . PRO A 19 ? 0.4109 0.5816 0.3426 -0.0106 -0.0535 0.0561  19 PRO A N   
122 C CA  . PRO A 19 ? 0.4371 0.6443 0.3459 -0.0251 -0.0562 0.0394  19 PRO A CA  
123 C C   . PRO A 19 ? 0.4399 0.6255 0.3490 -0.0447 -0.0492 0.0062  19 PRO A C   
124 O O   . PRO A 19 ? 0.3874 0.5276 0.3077 -0.0441 -0.0397 0.0022  19 PRO A O   
125 C CB  . PRO A 19 ? 0.4626 0.6722 0.3511 -0.0196 -0.0501 0.0541  19 PRO A CB  
126 C CG  . PRO A 19 ? 0.4512 0.6360 0.3552 -0.0003 -0.0475 0.0865  19 PRO A CG  
127 C CD  . PRO A 19 ? 0.4191 0.5677 0.3497 0.0019  -0.0467 0.0796  19 PRO A CD  
128 N N   . GLN A 20 ? 0.4573 0.6771 0.3558 -0.0623 -0.0535 -0.0169 20 GLN A N   
129 C CA  . GLN A 20 ? 0.4847 0.6800 0.3878 -0.0823 -0.0446 -0.0487 20 GLN A CA  
130 C C   . GLN A 20 ? 0.4706 0.6207 0.3666 -0.0820 -0.0280 -0.0580 20 GLN A C   
131 O O   . GLN A 20 ? 0.4590 0.5667 0.3695 -0.0854 -0.0173 -0.0677 20 GLN A O   
132 C CB  . GLN A 20 ? 0.5389 0.7821 0.4297 -0.1046 -0.0507 -0.0755 20 GLN A CB  
133 C CG  . GLN A 20 ? 0.5965 0.8120 0.4989 -0.1285 -0.0404 -0.1085 20 GLN A CG  
134 C CD  . GLN A 20 ? 0.6480 0.8431 0.5798 -0.1275 -0.0408 -0.0993 20 GLN A CD  
135 O OE1 . GLN A 20 ? 0.7021 0.8444 0.6476 -0.1272 -0.0277 -0.1008 20 GLN A OE1 
136 N NE2 . GLN A 20 ? 0.6724 0.9143 0.6147 -0.1246 -0.0554 -0.0867 20 GLN A NE2 
137 N N   . GLN A 21 ? 0.4918 0.6554 0.3664 -0.0764 -0.0250 -0.0527 21 GLN A N   
138 C CA  . GLN A 21 ? 0.5126 0.6434 0.3814 -0.0745 -0.0085 -0.0611 21 GLN A CA  
139 C C   . GLN A 21 ? 0.4780 0.5654 0.3695 -0.0605 -0.0028 -0.0425 21 GLN A C   
140 O O   . GLN A 21 ? 0.4811 0.5351 0.3808 -0.0596 0.0105  -0.0520 21 GLN A O   
141 C CB  . GLN A 21 ? 0.5655 0.7301 0.4075 -0.0699 -0.0076 -0.0524 21 GLN A CB  
142 C CG  . GLN A 21 ? 0.6432 0.7919 0.4728 -0.0728 0.0107  -0.0720 21 GLN A CG  
143 C CD  . GLN A 21 ? 0.7158 0.8996 0.5193 -0.0670 0.0136  -0.0585 21 GLN A CD  
144 O OE1 . GLN A 21 ? 0.7838 0.9978 0.5808 -0.0585 0.0027  -0.0282 21 GLN A OE1 
145 N NE2 . GLN A 21 ? 0.7482 0.9284 0.5378 -0.0701 0.0305  -0.0791 21 GLN A NE2 
146 N N   . GLN A 22 ? 0.4456 0.5364 0.3480 -0.0489 -0.0124 -0.0164 22 GLN A N   
147 C CA  . GLN A 22 ? 0.4202 0.4784 0.3427 -0.0387 -0.0089 -0.0021 22 GLN A CA  
148 C C   . GLN A 22 ? 0.3980 0.4352 0.3388 -0.0421 -0.0088 -0.0109 22 GLN A C   
149 O O   . GLN A 22 ? 0.3697 0.3812 0.3229 -0.0378 -0.0014 -0.0093 22 GLN A O   
150 C CB  . GLN A 22 ? 0.4215 0.4854 0.3504 -0.0270 -0.0162 0.0239  22 GLN A CB  
151 C CG  . GLN A 22 ? 0.4485 0.5256 0.3632 -0.0224 -0.0124 0.0401  22 GLN A CG  
152 C CD  . GLN A 22 ? 0.4530 0.5256 0.3781 -0.0111 -0.0157 0.0675  22 GLN A CD  
153 O OE1 . GLN A 22 ? 0.4813 0.5343 0.4262 -0.0063 -0.0186 0.0710  22 GLN A OE1 
154 N NE2 . GLN A 22 ? 0.4692 0.5593 0.3810 -0.0066 -0.0132 0.0872  22 GLN A NE2 
155 N N   . LYS A 23 ? 0.3939 0.4478 0.3371 -0.0496 -0.0166 -0.0179 23 LYS A N   
156 C CA  . LYS A 23 ? 0.3971 0.4341 0.3569 -0.0549 -0.0143 -0.0245 23 LYS A CA  
157 C C   . LYS A 23 ? 0.4050 0.4121 0.3662 -0.0621 0.0004  -0.0404 23 LYS A C   
158 O O   . LYS A 23 ? 0.4206 0.4018 0.3962 -0.0570 0.0074  -0.0346 23 LYS A O   
159 C CB  . LYS A 23 ? 0.4235 0.4886 0.3870 -0.0662 -0.0227 -0.0326 23 LYS A CB  
160 C CG  . LYS A 23 ? 0.4329 0.5301 0.4008 -0.0559 -0.0359 -0.0160 23 LYS A CG  
161 C CD  . LYS A 23 ? 0.4495 0.5876 0.4224 -0.0675 -0.0445 -0.0248 23 LYS A CD  
162 C CE  . LYS A 23 ? 0.4382 0.6048 0.4234 -0.0533 -0.0546 -0.0070 23 LYS A CE  
163 N NZ  . LYS A 23 ? 0.4559 0.6733 0.4480 -0.0642 -0.0636 -0.0146 23 LYS A NZ  
164 N N   . LYS A 24 ? 0.4665 0.4801 0.4128 -0.0728 0.0058  -0.0602 24 LYS A N   
165 C CA  . LYS A 24 ? 0.5124 0.4937 0.4610 -0.0789 0.0232  -0.0792 24 LYS A CA  
166 C C   . LYS A 24 ? 0.4834 0.4414 0.4375 -0.0618 0.0337  -0.0672 24 LYS A C   
167 O O   . LYS A 24 ? 0.4686 0.3943 0.4376 -0.0571 0.0468  -0.0675 24 LYS A O   
168 C CB  . LYS A 24 ? 0.5759 0.5732 0.5046 -0.0948 0.0276  -0.1082 24 LYS A CB  
169 C CG  . LYS A 24 ? 0.6883 0.6458 0.6239 -0.1052 0.0482  -0.1348 24 LYS A CG  
170 C CD  . LYS A 24 ? 0.7901 0.7479 0.7062 -0.1086 0.0614  -0.1604 24 LYS A CD  
171 C CE  . LYS A 24 ? 0.8702 0.7754 0.7997 -0.1112 0.0865  -0.1822 24 LYS A CE  
172 N NZ  . LYS A 24 ? 0.9181 0.8194 0.8338 -0.1027 0.1021  -0.1972 24 LYS A NZ  
173 N N   . LYS A 25 ? 0.4624 0.4392 0.4066 -0.0523 0.0289  -0.0542 25 LYS A N   
174 C CA  . LYS A 25 ? 0.4238 0.3887 0.3759 -0.0384 0.0379  -0.0430 25 LYS A CA  
175 C C   . LYS A 25 ? 0.3976 0.3500 0.3717 -0.0287 0.0349  -0.0246 25 LYS A C   
176 O O   . LYS A 25 ? 0.4053 0.3447 0.3926 -0.0186 0.0448  -0.0193 25 LYS A O   
177 C CB  . LYS A 25 ? 0.4136 0.4031 0.3526 -0.0342 0.0344  -0.0318 25 LYS A CB  
178 C CG  . LYS A 25 ? 0.4032 0.3882 0.3516 -0.0235 0.0456  -0.0233 25 LYS A CG  
179 C CD  . LYS A 25 ? 0.4390 0.4088 0.3886 -0.0203 0.0645  -0.0414 25 LYS A CD  
180 C CE  . LYS A 25 ? 0.4428 0.4216 0.4004 -0.0093 0.0755  -0.0326 25 LYS A CE  
181 N NZ  . LYS A 25 ? 0.4796 0.4428 0.4411 -0.0024 0.0960  -0.0502 25 LYS A NZ  
182 N N   . LEU A 26 ? 0.3657 0.3274 0.3436 -0.0304 0.0215  -0.0149 26 LEU A N   
183 C CA  A LEU A 26 ? 0.3672 0.3238 0.3617 -0.0233 0.0182  -0.0013 26 LEU A CA  
184 C CA  B LEU A 26 ? 0.3581 0.3147 0.3527 -0.0232 0.0182  -0.0013 26 LEU A CA  
185 C C   . LEU A 26 ? 0.3747 0.3100 0.3804 -0.0227 0.0285  -0.0035 26 LEU A C   
186 O O   . LEU A 26 ? 0.3771 0.3073 0.3958 -0.0121 0.0332  0.0085  26 LEU A O   
187 C CB  A LEU A 26 ? 0.3580 0.3292 0.3518 -0.0261 0.0048  0.0035  26 LEU A CB  
188 C CB  B LEU A 26 ? 0.3328 0.3027 0.3288 -0.0252 0.0051  0.0047  26 LEU A CB  
189 C CG  A LEU A 26 ? 0.3339 0.3098 0.3390 -0.0192 -0.0010 0.0151  26 LEU A CG  
190 C CG  B LEU A 26 ? 0.3098 0.2918 0.3044 -0.0208 -0.0029 0.0141  26 LEU A CG  
191 C CD1 A LEU A 26 ? 0.3321 0.3125 0.3390 -0.0150 -0.0022 0.0217  26 LEU A CD1 
192 C CD1 B LEU A 26 ? 0.3056 0.2974 0.3031 -0.0208 -0.0124 0.0165  26 LEU A CD1 
193 C CD2 A LEU A 26 ? 0.3339 0.3208 0.3395 -0.0213 -0.0099 0.0152  26 LEU A CD2 
194 C CD2 B LEU A 26 ? 0.3039 0.2842 0.3097 -0.0149 -0.0010 0.0219  26 LEU A CD2 
195 N N   . GLN A 27 ? 0.4019 0.3277 0.4039 -0.0350 0.0320  -0.0177 27 GLN A N   
196 C CA  . GLN A 27 ? 0.4293 0.3279 0.4441 -0.0375 0.0448  -0.0193 27 GLN A CA  
197 C C   . GLN A 27 ? 0.4557 0.3286 0.4779 -0.0266 0.0626  -0.0205 27 GLN A C   
198 O O   . GLN A 27 ? 0.4759 0.3331 0.5145 -0.0148 0.0715  -0.0044 27 GLN A O   
199 C CB  . GLN A 27 ? 0.4467 0.3415 0.4576 -0.0581 0.0465  -0.0395 27 GLN A CB  
200 C CG  . GLN A 27 ? 0.4245 0.3471 0.4355 -0.0666 0.0316  -0.0354 27 GLN A CG  
201 C CD  . GLN A 27 ? 0.4664 0.4010 0.4732 -0.0887 0.0301  -0.0575 27 GLN A CD  
202 O OE1 . GLN A 27 ? 0.5034 0.4165 0.5103 -0.1021 0.0429  -0.0782 27 GLN A OE1 
203 N NE2 . GLN A 27 ? 0.4518 0.4236 0.4565 -0.0931 0.0149  -0.0551 27 GLN A NE2 
204 N N   . THR A 28 ? 0.4576 0.3300 0.4681 -0.0287 0.0688  -0.0379 28 THR A N   
205 C CA  . THR A 28 ? 0.4821 0.3304 0.5012 -0.0170 0.0886  -0.0425 28 THR A CA  
206 C C   . THR A 28 ? 0.4697 0.3331 0.5015 0.0040  0.0874  -0.0182 28 THR A C   
207 O O   . THR A 28 ? 0.4635 0.3102 0.5136 0.0201  0.1019  -0.0081 28 THR A O   
208 C CB  . THR A 28 ? 0.5171 0.3668 0.5180 -0.0256 0.0968  -0.0705 28 THR A CB  
209 O OG1 . THR A 28 ? 0.5151 0.4029 0.4980 -0.0267 0.0828  -0.0668 28 THR A OG1 
210 C CG2 . THR A 28 ? 0.5501 0.3869 0.5418 -0.0486 0.1002  -0.0988 28 THR A CG2 
211 N N   . ASP A 29 ? 0.4249 0.3215 0.4498 0.0038  0.0710  -0.0083 29 ASP A N   
212 C CA  . ASP A 29 ? 0.4026 0.3207 0.4411 0.0180  0.0678  0.0111  29 ASP A CA  
213 C C   . ASP A 29 ? 0.4095 0.3271 0.4651 0.0279  0.0662  0.0307  29 ASP A C   
214 O O   . ASP A 29 ? 0.3983 0.3278 0.4709 0.0441  0.0714  0.0462  29 ASP A O   
215 C CB  . ASP A 29 ? 0.3664 0.3129 0.3965 0.0113  0.0519  0.0157  29 ASP A CB  
216 C CG  . ASP A 29 ? 0.3651 0.3240 0.3838 0.0079  0.0550  0.0089  29 ASP A CG  
217 O OD1 . ASP A 29 ? 0.3985 0.3491 0.4130 0.0111  0.0696  -0.0025 29 ASP A OD1 
218 O OD2 . ASP A 29 ? 0.3556 0.3321 0.3708 0.0027  0.0447  0.0160  29 ASP A OD2 
219 N N   . ILE A 30 ? 0.4031 0.3146 0.4543 0.0184  0.0587  0.0316  30 ILE A N   
220 C CA  . ILE A 30 ? 0.4217 0.3365 0.4847 0.0260  0.0576  0.0512  30 ILE A CA  
221 C C   . ILE A 30 ? 0.4429 0.3251 0.5210 0.0372  0.0779  0.0593  30 ILE A C   
222 O O   . ILE A 30 ? 0.4615 0.3538 0.5553 0.0559  0.0828  0.0819  30 ILE A O   
223 C CB  . ILE A 30 ? 0.4214 0.3409 0.4753 0.0121  0.0465  0.0485  30 ILE A CB  
224 C CG1 . ILE A 30 ? 0.3816 0.3322 0.4270 0.0079  0.0290  0.0465  30 ILE A CG1 
225 C CG2 . ILE A 30 ? 0.4515 0.3674 0.5155 0.0176  0.0515  0.0678  30 ILE A CG2 
226 C CD1 . ILE A 30 ? 0.3806 0.3365 0.4175 -0.0037 0.0196  0.0397  30 ILE A CD1 
227 N N   . GLN A 31 ? 0.4888 0.3336 0.5637 0.0260  0.0905  0.0406  31 GLN A N   
228 C CA  . GLN A 31 ? 0.5681 0.3696 0.6597 0.0335  0.1136  0.0449  31 GLN A CA  
229 C C   . GLN A 31 ? 0.5615 0.3560 0.6681 0.0571  0.1291  0.0518  31 GLN A C   
230 O O   . GLN A 31 ? 0.6102 0.3847 0.7380 0.0762  0.1448  0.0736  31 GLN A O   
231 C CB  . GLN A 31 ? 0.6674 0.4311 0.7525 0.0125  0.1255  0.0137  31 GLN A CB  
232 C CG  . GLN A 31 ? 0.7353 0.5025 0.8130 -0.0111 0.1155  0.0068  31 GLN A CG  
233 C CD  . GLN A 31 ? 0.8402 0.5832 0.9114 -0.0362 0.1240  -0.0281 31 GLN A CD  
234 O OE1 . GLN A 31 ? 0.8692 0.6293 0.9220 -0.0464 0.1171  -0.0534 31 GLN A OE1 
235 N NE2 . GLN A 31 ? 0.8598 0.5669 0.9460 -0.0483 0.1390  -0.0293 31 GLN A NE2 
236 N N   . GLU A 32 ? 0.5388 0.3492 0.6358 0.0567  0.1271  0.0343  32 GLU A N   
237 C CA  . GLU A 32 ? 0.5787 0.3856 0.6903 0.0779  0.1441  0.0359  32 GLU A CA  
238 C C   . GLU A 32 ? 0.5481 0.3970 0.6781 0.1009  0.1371  0.0685  32 GLU A C   
239 O O   . GLU A 32 ? 0.5526 0.4056 0.7020 0.1236  0.1516  0.0775  32 GLU A O   
240 C CB  . GLU A 32 ? 0.5774 0.3974 0.6712 0.0688  0.1440  0.0090  32 GLU A CB  
241 C CG  . GLU A 32 ? 0.6308 0.4158 0.7078 0.0498  0.1557  -0.0268 32 GLU A CG  
242 C CD  . GLU A 32 ? 0.6474 0.4601 0.6982 0.0365  0.1486  -0.0493 32 GLU A CD  
243 O OE1 . GLU A 32 ? 0.6203 0.4727 0.6681 0.0416  0.1368  -0.0360 32 GLU A OE1 
244 O OE2 . GLU A 32 ? 0.7147 0.5117 0.7480 0.0193  0.1551  -0.0801 32 GLU A OE2 
245 N N   . ASN A 33 ? 0.5135 0.3987 0.6382 0.0950  0.1153  0.0839  33 ASN A N   
246 C CA  . ASN A 33 ? 0.4900 0.4261 0.6294 0.1112  0.1053  0.1094  33 ASN A CA  
247 C C   . ASN A 33 ? 0.4916 0.4397 0.6364 0.1176  0.0986  0.1364  33 ASN A C   
248 O O   . ASN A 33 ? 0.4655 0.4648 0.6108 0.1190  0.0816  0.1498  33 ASN A O   
249 C CB  . ASN A 33 ? 0.4622 0.4403 0.5901 0.0967  0.0862  0.0988  33 ASN A CB  
250 C CG  . ASN A 33 ? 0.4873 0.4626 0.6118 0.0940  0.0949  0.0801  33 ASN A CG  
251 O OD1 . ASN A 33 ? 0.5299 0.5303 0.6728 0.1098  0.1026  0.0883  33 ASN A OD1 
252 N ND2 . ASN A 33 ? 0.4915 0.4443 0.5933 0.0751  0.0937  0.0566  33 ASN A ND2 
253 N N   . GLY A 34 ? 0.5024 0.4047 0.6514 0.1200  0.1136  0.1434  34 GLY A N   
254 C CA  . GLY A 34 ? 0.5135 0.4241 0.6734 0.1340  0.1156  0.1779  34 GLY A CA  
255 C C   . GLY A 34 ? 0.4981 0.4155 0.6398 0.1137  0.1018  0.1771  34 GLY A C   
256 O O   . GLY A 34 ? 0.5138 0.4375 0.6607 0.1220  0.1046  0.2053  34 GLY A O   
257 N N   . GLY A 35 ? 0.4556 0.3740 0.5771 0.0891  0.0884  0.1473  35 GLY A N   
258 C CA  . GLY A 35 ? 0.4637 0.3967 0.5699 0.0722  0.0749  0.1447  35 GLY A CA  
259 C C   . GLY A 35 ? 0.4857 0.3731 0.5897 0.0560  0.0862  0.1349  35 GLY A C   
260 O O   . GLY A 35 ? 0.4979 0.3397 0.6101 0.0543  0.1037  0.1243  35 GLY A O   
261 N N   . LYS A 36 ? 0.4873 0.3906 0.5819 0.0433  0.0771  0.1369  36 LYS A N   
262 C CA  . LYS A 36 ? 0.5187 0.3924 0.6120 0.0229  0.0841  0.1246  36 LYS A CA  
263 C C   . LYS A 36 ? 0.4675 0.3709 0.5445 0.0066  0.0653  0.1051  36 LYS A C   
264 O O   . LYS A 36 ? 0.4292 0.3711 0.4975 0.0122  0.0501  0.1069  36 LYS A O   
265 C CB  . LYS A 36 ? 0.5701 0.4329 0.6746 0.0260  0.0976  0.1537  36 LYS A CB  
266 C CG  . LYS A 36 ? 0.6475 0.4753 0.7722 0.0457  0.1196  0.1787  36 LYS A CG  
267 C CD  . LYS A 36 ? 0.7412 0.5532 0.8783 0.0475  0.1358  0.2117  36 LYS A CD  
268 C CE  . LYS A 36 ? 0.8191 0.5902 0.9798 0.0705  0.1603  0.2397  36 LYS A CE  
269 N NZ  . LYS A 36 ? 0.9048 0.6436 1.0803 0.0671  0.1813  0.2687  36 LYS A NZ  
270 N N   . PHE A 37 ? 0.4661 0.3528 0.5410 -0.0136 0.0672  0.0851  37 PHE A N   
271 C CA  . PHE A 37 ? 0.4228 0.3390 0.4862 -0.0254 0.0509  0.0694  37 PHE A CA  
272 C C   . PHE A 37 ? 0.4441 0.3584 0.5135 -0.0435 0.0559  0.0665  37 PHE A C   
273 O O   . PHE A 37 ? 0.4637 0.3451 0.5450 -0.0534 0.0722  0.0672  37 PHE A O   
274 C CB  . PHE A 37 ? 0.4086 0.3256 0.4617 -0.0305 0.0421  0.0455  37 PHE A CB  
275 C CG  . PHE A 37 ? 0.4534 0.3409 0.5075 -0.0443 0.0524  0.0252  37 PHE A CG  
276 C CD1 . PHE A 37 ? 0.4692 0.3614 0.5232 -0.0652 0.0508  0.0086  37 PHE A CD1 
277 C CD2 . PHE A 37 ? 0.4730 0.3336 0.5290 -0.0371 0.0640  0.0201  37 PHE A CD2 
278 C CE1 . PHE A 37 ? 0.5010 0.3717 0.5547 -0.0814 0.0598  -0.0150 37 PHE A CE1 
279 C CE2 . PHE A 37 ? 0.5144 0.3487 0.5694 -0.0513 0.0751  -0.0039 37 PHE A CE2 
280 C CZ  . PHE A 37 ? 0.5196 0.3594 0.5724 -0.0749 0.0724  -0.0228 37 PHE A CZ  
281 N N   A SER A 38 ? 0.4226 0.3726 0.4864 -0.0475 0.0436  0.0634  38 SER A N   
282 N N   B SER A 38 ? 0.4130 0.3625 0.4764 -0.0483 0.0431  0.0614  38 SER A N   
283 C CA  A SER A 38 ? 0.4446 0.4068 0.5153 -0.0649 0.0454  0.0582  38 SER A CA  
284 C CA  B SER A 38 ? 0.4286 0.3920 0.4992 -0.0642 0.0453  0.0592  38 SER A CA  
285 C C   A SER A 38 ? 0.4128 0.4070 0.4764 -0.0678 0.0291  0.0406  38 SER A C   
286 C C   B SER A 38 ? 0.4063 0.4045 0.4703 -0.0668 0.0292  0.0432  38 SER A C   
287 O O   A SER A 38 ? 0.3930 0.3965 0.4464 -0.0552 0.0183  0.0372  38 SER A O   
288 O O   B SER A 38 ? 0.3845 0.3981 0.4390 -0.0529 0.0183  0.0427  38 SER A O   
289 C CB  A SER A 38 ? 0.4580 0.4385 0.5334 -0.0616 0.0514  0.0810  38 SER A CB  
290 C CB  B SER A 38 ? 0.4351 0.4126 0.5100 -0.0586 0.0525  0.0846  38 SER A CB  
291 O OG  A SER A 38 ? 0.4403 0.4560 0.5039 -0.0466 0.0393  0.0855  38 SER A OG  
292 O OG  B SER A 38 ? 0.4119 0.4190 0.4917 -0.0704 0.0513  0.0825  38 SER A OG  
293 N N   . PHE A 39 ? 0.4038 0.4157 0.4757 -0.0843 0.0286  0.0310  39 PHE A N   
294 C CA  . PHE A 39 ? 0.4026 0.4522 0.4724 -0.0830 0.0145  0.0205  39 PHE A CA  
295 C C   . PHE A 39 ? 0.4025 0.4851 0.4778 -0.0773 0.0142  0.0308  39 PHE A C   
296 O O   . PHE A 39 ? 0.4175 0.5300 0.4929 -0.0695 0.0047  0.0253  39 PHE A O   
297 C CB  . PHE A 39 ? 0.4320 0.4911 0.5077 -0.1032 0.0123  0.0021  39 PHE A CB  
298 C CG  . PHE A 39 ? 0.4536 0.4847 0.5183 -0.1059 0.0126  -0.0109 39 PHE A CG  
299 C CD1 . PHE A 39 ? 0.4718 0.5061 0.5219 -0.0905 0.0022  -0.0120 39 PHE A CD1 
300 C CD2 . PHE A 39 ? 0.5217 0.5215 0.5917 -0.1239 0.0259  -0.0223 39 PHE A CD2 
301 C CE1 . PHE A 39 ? 0.4923 0.5061 0.5313 -0.0925 0.0043  -0.0230 39 PHE A CE1 
302 C CE2 . PHE A 39 ? 0.5324 0.5089 0.5911 -0.1251 0.0282  -0.0372 39 PHE A CE2 
303 C CZ  . PHE A 39 ? 0.5074 0.4944 0.5498 -0.1091 0.0171  -0.0369 39 PHE A CZ  
304 N N   . SER A 40 ? 0.3972 0.4745 0.4769 -0.0791 0.0262  0.0471  40 SER A N   
305 C CA  . SER A 40 ? 0.3859 0.4980 0.4681 -0.0743 0.0288  0.0574  40 SER A CA  
306 C C   . SER A 40 ? 0.3825 0.4973 0.4501 -0.0555 0.0276  0.0691  40 SER A C   
307 O O   . SER A 40 ? 0.3719 0.4606 0.4338 -0.0497 0.0302  0.0784  40 SER A O   
308 C CB  . SER A 40 ? 0.4060 0.5196 0.5029 -0.0917 0.0441  0.0701  40 SER A CB  
309 O OG  . SER A 40 ? 0.4407 0.5531 0.5527 -0.1139 0.0452  0.0552  40 SER A OG  
310 N N   . LEU A 41 ? 0.3498 0.5009 0.4129 -0.0463 0.0244  0.0667  41 LEU A N   
311 C CA  . LEU A 41 ? 0.3579 0.5241 0.4063 -0.0324 0.0234  0.0730  41 LEU A CA  
312 C C   . LEU A 41 ? 0.3558 0.5455 0.4034 -0.0350 0.0359  0.0950  41 LEU A C   
313 O O   . LEU A 41 ? 0.3306 0.5467 0.3862 -0.0417 0.0423  0.0957  41 LEU A O   
314 C CB  . LEU A 41 ? 0.3480 0.5368 0.3915 -0.0219 0.0151  0.0530  41 LEU A CB  
315 C CG  . LEU A 41 ? 0.3697 0.5836 0.3976 -0.0114 0.0144  0.0503  41 LEU A CG  
316 C CD1 . LEU A 41 ? 0.3641 0.5610 0.3824 -0.0073 0.0085  0.0541  41 LEU A CD1 
317 C CD2 . LEU A 41 ? 0.3661 0.5960 0.3941 -0.0031 0.0113  0.0265  41 LEU A CD2 
318 N N   . ASN A 42 ? 0.3574 0.5416 0.3967 -0.0286 0.0399  0.1158  42 ASN A N   
319 C CA  . ASN A 42 ? 0.3994 0.6076 0.4357 -0.0283 0.0525  0.1438  42 ASN A CA  
320 C C   . ASN A 42 ? 0.3928 0.6238 0.4112 -0.0125 0.0481  0.1574  42 ASN A C   
321 O O   . ASN A 42 ? 0.3644 0.5855 0.3775 -0.0052 0.0367  0.1449  42 ASN A O   
322 C CB  . ASN A 42 ? 0.4431 0.6160 0.4971 -0.0407 0.0680  0.1657  42 ASN A CB  
323 C CG  . ASN A 42 ? 0.4991 0.6229 0.5581 -0.0371 0.0682  0.1697  42 ASN A CG  
324 O OD1 . ASN A 42 ? 0.5072 0.6343 0.5563 -0.0210 0.0637  0.1808  42 ASN A OD1 
325 N ND2 . ASN A 42 ? 0.5390 0.6221 0.6139 -0.0522 0.0736  0.1587  42 ASN A ND2 
326 N N   . PRO A 43 ? 0.4264 0.6949 0.4351 -0.0077 0.0569  0.1841  43 PRO A N   
327 C CA  . PRO A 43 ? 0.4415 0.7468 0.4317 0.0069  0.0511  0.1983  43 PRO A CA  
328 C C   . PRO A 43 ? 0.4663 0.7445 0.4620 0.0171  0.0474  0.2138  43 PRO A C   
329 O O   . PRO A 43 ? 0.4551 0.7679 0.4380 0.0280  0.0369  0.2145  43 PRO A O   
330 C CB  . PRO A 43 ? 0.4761 0.8206 0.4587 0.0089  0.0653  0.2337  43 PRO A CB  
331 C CG  . PRO A 43 ? 0.4720 0.8177 0.4642 -0.0057 0.0747  0.2219  43 PRO A CG  
332 C CD  . PRO A 43 ? 0.4475 0.7352 0.4619 -0.0170 0.0723  0.2016  43 PRO A CD  
333 N N   . GLN A 44 ? 0.4962 0.7171 0.5119 0.0130  0.0568  0.2244  44 GLN A N   
334 C CA  . GLN A 44 ? 0.5015 0.6939 0.5259 0.0249  0.0573  0.2395  44 GLN A CA  
335 C C   . GLN A 44 ? 0.4591 0.6339 0.4842 0.0245  0.0428  0.2064  44 GLN A C   
336 O O   . GLN A 44 ? 0.4529 0.6174 0.4836 0.0360  0.0410  0.2152  44 GLN A O   
337 C CB  . GLN A 44 ? 0.5504 0.6839 0.5968 0.0211  0.0768  0.2607  44 GLN A CB  
338 C CG  . GLN A 44 ? 0.6225 0.7644 0.6733 0.0277  0.0950  0.3074  44 GLN A CG  
339 C CD  . GLN A 44 ? 0.6614 0.8375 0.7046 0.0146  0.1002  0.3102  44 GLN A CD  
340 O OE1 . GLN A 44 ? 0.6686 0.8274 0.7201 -0.0054 0.1028  0.2863  44 GLN A OE1 
341 N NE2 . GLN A 44 ? 0.6983 0.9310 0.7252 0.0263  0.1016  0.3395  44 GLN A NE2 
342 N N   . CYS A 45 ? 0.4120 0.5840 0.4334 0.0128  0.0340  0.1715  45 CYS A N   
343 C CA  . CYS A 45 ? 0.3615 0.5178 0.3833 0.0124  0.0219  0.1445  45 CYS A CA  
344 C C   . CYS A 45 ? 0.3755 0.5734 0.3865 0.0220  0.0102  0.1419  45 CYS A C   
345 O O   . CYS A 45 ? 0.3913 0.6363 0.3889 0.0239  0.0070  0.1432  45 CYS A O   
346 C CB  . CYS A 45 ? 0.3367 0.4833 0.3585 0.0011  0.0164  0.1140  45 CYS A CB  
347 S SG  . CYS A 45 ? 0.2684 0.3762 0.3052 -0.0136 0.0267  0.1122  45 CYS A SG  
348 N N   . THR A 46 ? 0.3618 0.5472 0.3790 0.0268  0.0049  0.1380  46 THR A N   
349 C CA  . THR A 46 ? 0.3633 0.5896 0.3746 0.0307  -0.0072 0.1295  46 THR A CA  
350 C C   . THR A 46 ? 0.3421 0.5569 0.3520 0.0198  -0.0161 0.0936  46 THR A C   
351 O O   . THR A 46 ? 0.3166 0.5652 0.3200 0.0161  -0.0251 0.0760  46 THR A O   
352 C CB  . THR A 46 ? 0.3709 0.5993 0.3939 0.0435  -0.0062 0.1507  46 THR A CB  
353 O OG1 . THR A 46 ? 0.3764 0.5522 0.4122 0.0421  -0.0006 0.1441  46 THR A OG1 
354 C CG2 . THR A 46 ? 0.4112 0.6553 0.4369 0.0585  0.0036  0.1913  46 THR A CG2 
355 N N   . HIS A 47 ? 0.3205 0.4881 0.3374 0.0142  -0.0126 0.0834  47 HIS A N   
356 C CA  . HIS A 47 ? 0.3238 0.4732 0.3423 0.0069  -0.0185 0.0576  47 HIS A CA  
357 C C   . HIS A 47 ? 0.3269 0.4481 0.3466 0.0018  -0.0148 0.0495  47 HIS A C   
358 O O   . HIS A 47 ? 0.3323 0.4389 0.3554 0.0008  -0.0075 0.0619  47 HIS A O   
359 C CB  . HIS A 47 ? 0.3299 0.4565 0.3574 0.0079  -0.0187 0.0589  47 HIS A CB  
360 C CG  . HIS A 47 ? 0.3385 0.4958 0.3705 0.0130  -0.0229 0.0664  47 HIS A CG  
361 N ND1 . HIS A 47 ? 0.3303 0.5108 0.3653 0.0247  -0.0196 0.0918  47 HIS A ND1 
362 C CD2 . HIS A 47 ? 0.3378 0.5105 0.3745 0.0078  -0.0296 0.0531  47 HIS A CD2 
363 C CE1 . HIS A 47 ? 0.3492 0.5644 0.3906 0.0279  -0.0259 0.0938  47 HIS A CE1 
364 N NE2 . HIS A 47 ? 0.3335 0.5446 0.3764 0.0156  -0.0320 0.0687  47 HIS A NE2 
365 N N   . ILE A 48 ? 0.3447 0.4604 0.3641 -0.0015 -0.0191 0.0291  48 ILE A N   
366 C CA  . ILE A 48 ? 0.3224 0.4162 0.3460 -0.0037 -0.0178 0.0231  48 ILE A CA  
367 C C   . ILE A 48 ? 0.3114 0.3829 0.3382 -0.0045 -0.0216 0.0133  48 ILE A C   
368 O O   . ILE A 48 ? 0.3092 0.3834 0.3370 -0.0047 -0.0242 0.0012  48 ILE A O   
369 C CB  . ILE A 48 ? 0.3326 0.4448 0.3557 -0.0024 -0.0161 0.0149  48 ILE A CB  
370 C CG1 . ILE A 48 ? 0.3406 0.4401 0.3714 -0.0029 -0.0160 0.0119  48 ILE A CG1 
371 C CG2 . ILE A 48 ? 0.3323 0.4591 0.3521 0.0001  -0.0182 -0.0035 48 ILE A CG2 
372 C CD1 . ILE A 48 ? 0.3506 0.4744 0.3857 -0.0003 -0.0125 0.0077  48 ILE A CD1 
373 N N   . ILE A 49 ? 0.3130 0.3637 0.3416 -0.0064 -0.0207 0.0180  49 ILE A N   
374 C CA  . ILE A 49 ? 0.3011 0.3338 0.3308 -0.0066 -0.0229 0.0142  49 ILE A CA  
375 C C   . ILE A 49 ? 0.3071 0.3387 0.3393 -0.0036 -0.0247 0.0109  49 ILE A C   
376 O O   . ILE A 49 ? 0.2962 0.3348 0.3284 -0.0057 -0.0246 0.0137  49 ILE A O   
377 C CB  . ILE A 49 ? 0.2970 0.3155 0.3244 -0.0092 -0.0201 0.0207  49 ILE A CB  
378 C CG1 . ILE A 49 ? 0.3143 0.3366 0.3437 -0.0076 -0.0166 0.0278  49 ILE A CG1 
379 C CG2 . ILE A 49 ? 0.2949 0.3009 0.3209 -0.0094 -0.0214 0.0196  49 ILE A CG2 
380 C CD1 . ILE A 49 ? 0.2935 0.3305 0.3270 -0.0068 -0.0200 0.0252  49 ILE A CD1 
381 N N   A LEU A 50 ? 0.2944 0.3173 0.3310 0.0009  -0.0253 0.0059  50 LEU A N   
382 N N   B LEU A 50 ? 0.3129 0.3373 0.3497 0.0011  -0.0252 0.0050  50 LEU A N   
383 C CA  A LEU A 50 ? 0.2943 0.3185 0.3372 0.0092  -0.0256 0.0058  50 LEU A CA  
384 C CA  B LEU A 50 ? 0.3232 0.3464 0.3664 0.0094  -0.0255 0.0054  50 LEU A CA  
385 C C   A LEU A 50 ? 0.3103 0.3148 0.3556 0.0131  -0.0253 0.0130  50 LEU A C   
386 C C   B LEU A 50 ? 0.3264 0.3306 0.3703 0.0118  -0.0256 0.0137  50 LEU A C   
387 O O   A LEU A 50 ? 0.3039 0.2899 0.3535 0.0117  -0.0219 0.0091  50 LEU A O   
388 O O   B LEU A 50 ? 0.3292 0.3160 0.3754 0.0087  -0.0227 0.0115  50 LEU A O   
389 C CB  A LEU A 50 ? 0.2931 0.3233 0.3420 0.0143  -0.0221 -0.0068 50 LEU A CB  
390 C CB  B LEU A 50 ? 0.3456 0.3693 0.3965 0.0160  -0.0217 -0.0068 50 LEU A CB  
391 C CG  A LEU A 50 ? 0.2930 0.3241 0.3533 0.0277  -0.0193 -0.0081 50 LEU A CG  
392 C CG  B LEU A 50 ? 0.3516 0.4013 0.4043 0.0198  -0.0198 -0.0127 50 LEU A CG  
393 C CD1 A LEU A 50 ? 0.2852 0.3465 0.3481 0.0305  -0.0211 -0.0031 50 LEU A CD1 
394 C CD1 B LEU A 50 ? 0.3722 0.4165 0.4335 0.0290  -0.0136 -0.0278 50 LEU A CD1 
395 C CD2 A LEU A 50 ? 0.3107 0.3346 0.3772 0.0322  -0.0124 -0.0263 50 LEU A CD2 
396 C CD2 B LEU A 50 ? 0.3465 0.4145 0.4035 0.0228  -0.0221 -0.0027 50 LEU A CD2 
397 N N   . ASP A 51 ? 0.3387 0.3513 0.3816 0.0169  -0.0285 0.0238  51 ASP A N   
398 C CA  . ASP A 51 ? 0.3389 0.3392 0.3823 0.0231  -0.0277 0.0367  51 ASP A CA  
399 C C   . ASP A 51 ? 0.3483 0.3385 0.4069 0.0378  -0.0235 0.0394  51 ASP A C   
400 O O   . ASP A 51 ? 0.3377 0.3371 0.4043 0.0432  -0.0222 0.0294  51 ASP A O   
401 C CB  . ASP A 51 ? 0.3350 0.3557 0.3674 0.0215  -0.0331 0.0467  51 ASP A CB  
402 C CG  . ASP A 51 ? 0.3393 0.3927 0.3759 0.0272  -0.0390 0.0491  51 ASP A CG  
403 O OD1 . ASP A 51 ? 0.3393 0.3998 0.3876 0.0323  -0.0380 0.0428  51 ASP A OD1 
404 O OD2 . ASP A 51 ? 0.3696 0.4469 0.3979 0.0259  -0.0446 0.0564  51 ASP A OD2 
405 N N   . ASN A 52 ? 0.3856 0.3562 0.4492 0.0456  -0.0192 0.0542  52 ASN A N   
406 C CA  . ASN A 52 ? 0.4111 0.3575 0.4931 0.0599  -0.0105 0.0560  52 ASN A CA  
407 C C   . ASN A 52 ? 0.3788 0.3495 0.4713 0.0795  -0.0123 0.0637  52 ASN A C   
408 O O   . ASN A 52 ? 0.3644 0.3214 0.4732 0.0914  -0.0041 0.0553  52 ASN A O   
409 C CB  . ASN A 52 ? 0.4977 0.4117 0.5857 0.0633  -0.0022 0.0743  52 ASN A CB  
410 C CG  . ASN A 52 ? 0.5653 0.4490 0.6557 0.0454  0.0045  0.0611  52 ASN A CG  
411 O OD1 . ASN A 52 ? 0.5807 0.4725 0.6662 0.0312  0.0014  0.0390  52 ASN A OD1 
412 N ND2 . ASN A 52 ? 0.6461 0.4989 0.7453 0.0455  0.0143  0.0766  52 ASN A ND2 
413 N N   . ALA A 53 ? 0.3532 0.3632 0.4377 0.0821  -0.0223 0.0772  53 ALA A N   
414 C CA  . ALA A 53 ? 0.3601 0.4057 0.4574 0.1001  -0.0258 0.0869  53 ALA A CA  
415 C C   . ALA A 53 ? 0.3373 0.4112 0.4385 0.0945  -0.0283 0.0676  53 ALA A C   
416 O O   . ALA A 53 ? 0.3295 0.4353 0.4461 0.1094  -0.0290 0.0724  53 ALA A O   
417 C CB  . ALA A 53 ? 0.3583 0.4431 0.4457 0.1024  -0.0363 0.1082  53 ALA A CB  
418 N N   . ASP A 54 ? 0.3265 0.3936 0.4157 0.0746  -0.0287 0.0488  54 ASP A N   
419 C CA  . ASP A 54 ? 0.3286 0.4214 0.4211 0.0689  -0.0286 0.0346  54 ASP A CA  
420 C C   . ASP A 54 ? 0.3502 0.4247 0.4509 0.0758  -0.0183 0.0186  54 ASP A C   
421 O O   . ASP A 54 ? 0.3360 0.3739 0.4348 0.0746  -0.0126 0.0116  54 ASP A O   
422 C CB  . ASP A 54 ? 0.3453 0.4445 0.4221 0.0464  -0.0330 0.0276  54 ASP A CB  
423 C CG  . ASP A 54 ? 0.3881 0.5185 0.4607 0.0372  -0.0413 0.0341  54 ASP A CG  
424 O OD1 . ASP A 54 ? 0.4826 0.6517 0.5672 0.0396  -0.0440 0.0350  54 ASP A OD1 
425 O OD2 . ASP A 54 ? 0.3376 0.4576 0.3963 0.0278  -0.0445 0.0368  54 ASP A OD2 
426 N N   . VAL A 55 ? 0.3694 0.4736 0.4792 0.0809  -0.0151 0.0107  55 VAL A N   
427 C CA  . VAL A 55 ? 0.3925 0.4888 0.5065 0.0861  -0.0045 -0.0086 55 VAL A CA  
428 C C   . VAL A 55 ? 0.3840 0.5131 0.4895 0.0730  -0.0046 -0.0169 55 VAL A C   
429 O O   . VAL A 55 ? 0.3788 0.5334 0.4821 0.0624  -0.0110 -0.0069 55 VAL A O   
430 C CB  . VAL A 55 ? 0.4513 0.5501 0.5881 0.1119  0.0053  -0.0099 55 VAL A CB  
431 C CG1 . VAL A 55 ? 0.4818 0.5444 0.6295 0.1273  0.0081  0.0046  55 VAL A CG1 
432 C CG2 . VAL A 55 ? 0.4465 0.5990 0.5978 0.1217  0.0031  -0.0005 55 VAL A CG2 
433 N N   . LEU A 56 ? 0.3733 0.5014 0.4741 0.0727  0.0035  -0.0356 56 LEU A N   
434 C CA  . LEU A 56 ? 0.3725 0.5334 0.4637 0.0625  0.0058  -0.0408 56 LEU A CA  
435 C C   . LEU A 56 ? 0.4001 0.5866 0.5017 0.0768  0.0175  -0.0550 56 LEU A C   
436 O O   . LEU A 56 ? 0.4148 0.5807 0.5236 0.0903  0.0258  -0.0714 56 LEU A O   
437 C CB  . LEU A 56 ? 0.3999 0.5477 0.4714 0.0485  0.0042  -0.0489 56 LEU A CB  
438 C CG  . LEU A 56 ? 0.3963 0.5239 0.4587 0.0356  -0.0050 -0.0350 56 LEU A CG  
439 C CD1 . LEU A 56 ? 0.4204 0.5416 0.4684 0.0261  -0.0062 -0.0433 56 LEU A CD1 
440 C CD2 . LEU A 56 ? 0.3889 0.5353 0.4503 0.0262  -0.0082 -0.0181 56 LEU A CD2 
441 N N   . SER A 57 ? 0.3634 0.5939 0.4678 0.0734  0.0201  -0.0490 57 SER A N   
442 C CA  . SER A 57 ? 0.3622 0.6269 0.4746 0.0853  0.0329  -0.0619 57 SER A CA  
443 C C   . SER A 57 ? 0.3699 0.6363 0.4610 0.0799  0.0398  -0.0828 57 SER A C   
444 O O   . SER A 57 ? 0.3561 0.6084 0.4276 0.0651  0.0331  -0.0817 57 SER A O   
445 C CB  . SER A 57 ? 0.3305 0.6457 0.4527 0.0790  0.0343  -0.0474 57 SER A CB  
446 O OG  . SER A 57 ? 0.3035 0.6268 0.4072 0.0576  0.0322  -0.0381 57 SER A OG  
447 N N   . GLN A 58 ? 0.3857 0.6766 0.4810 0.0927  0.0538  -0.1023 58 GLN A N   
448 C CA  . GLN A 58 ? 0.4275 0.7345 0.5001 0.0869  0.0611  -0.1253 58 GLN A CA  
449 C C   . GLN A 58 ? 0.4144 0.7598 0.4674 0.0695  0.0573  -0.1063 58 GLN A C   
450 O O   . GLN A 58 ? 0.4218 0.7738 0.4507 0.0587  0.0544  -0.1122 58 GLN A O   
451 C CB  . GLN A 58 ? 0.4639 0.7944 0.5451 0.1049  0.0794  -0.1516 58 GLN A CB  
452 C CG  . GLN A 58 ? 0.5147 0.8609 0.5698 0.0984  0.0874  -0.1839 58 GLN A CG  
453 C CD  . GLN A 58 ? 0.5562 0.8568 0.6005 0.0877  0.0804  -0.2025 58 GLN A CD  
454 O OE1 . GLN A 58 ? 0.5854 0.8358 0.6474 0.0967  0.0842  -0.2163 58 GLN A OE1 
455 N NE2 . GLN A 58 ? 0.5737 0.8926 0.5914 0.0685  0.0702  -0.1994 58 GLN A NE2 
456 N N   . TYR A 59 ? 0.3880 0.7607 0.4538 0.0668  0.0579  -0.0823 59 TYR A N   
457 C CA  . TYR A 59 ? 0.3677 0.7689 0.4207 0.0503  0.0574  -0.0591 59 TYR A CA  
458 C C   . TYR A 59 ? 0.3464 0.7125 0.3852 0.0372  0.0447  -0.0458 59 TYR A C   
459 O O   . TYR A 59 ? 0.3504 0.7311 0.3685 0.0291  0.0445  -0.0376 59 TYR A O   
460 C CB  . TYR A 59 ? 0.3574 0.7851 0.4325 0.0451  0.0606  -0.0377 59 TYR A CB  
461 C CG  . TYR A 59 ? 0.3540 0.7960 0.4196 0.0255  0.0621  -0.0108 59 TYR A CG  
462 C CD1 . TYR A 59 ? 0.3811 0.8661 0.4314 0.0225  0.0741  -0.0044 59 TYR A CD1 
463 C CD2 . TYR A 59 ? 0.3362 0.7465 0.4069 0.0109  0.0535  0.0083  59 TYR A CD2 
464 C CE1 . TYR A 59 ? 0.3955 0.8893 0.4386 0.0068  0.0779  0.0252  59 TYR A CE1 
465 C CE2 . TYR A 59 ? 0.3441 0.7581 0.4092 -0.0051 0.0582  0.0333  59 TYR A CE2 
466 C CZ  . TYR A 59 ? 0.3883 0.8425 0.4406 -0.0066 0.0707  0.0443  59 TYR A CZ  
467 O OH  . TYR A 59 ? 0.4214 0.8773 0.4695 -0.0203 0.0781  0.0745  59 TYR A OH  
468 N N   . GLN A 60 ? 0.3242 0.6488 0.3748 0.0368  0.0346  -0.0416 60 GLN A N   
469 C CA  . GLN A 60 ? 0.3080 0.6001 0.3484 0.0262  0.0243  -0.0299 60 GLN A CA  
470 C C   . GLN A 60 ? 0.3304 0.6148 0.3522 0.0266  0.0214  -0.0460 60 GLN A C   
471 O O   . GLN A 60 ? 0.3424 0.6280 0.3507 0.0185  0.0167  -0.0338 60 GLN A O   
472 C CB  . GLN A 60 ? 0.2964 0.5522 0.3517 0.0272  0.0159  -0.0259 60 GLN A CB  
473 C CG  . GLN A 60 ? 0.2846 0.5517 0.3549 0.0192  0.0153  -0.0089 60 GLN A CG  
474 C CD  . GLN A 60 ? 0.2776 0.5229 0.3604 0.0218  0.0066  -0.0074 60 GLN A CD  
475 O OE1 . GLN A 60 ? 0.3175 0.5551 0.4086 0.0369  0.0055  -0.0164 60 GLN A OE1 
476 N NE2 . GLN A 60 ? 0.2742 0.5098 0.3584 0.0075  0.0017  0.0042  60 GLN A NE2 
477 N N   . LEU A 61 ? 0.3483 0.6246 0.3725 0.0357  0.0249  -0.0736 61 LEU A N   
478 C CA  . LEU A 61 ? 0.3857 0.6563 0.3956 0.0319  0.0226  -0.0955 61 LEU A CA  
479 C C   . LEU A 61 ? 0.3915 0.7138 0.3781 0.0268  0.0259  -0.0987 61 LEU A C   
480 O O   . LEU A 61 ? 0.4051 0.7381 0.3761 0.0184  0.0189  -0.1010 61 LEU A O   
481 C CB  . LEU A 61 ? 0.4161 0.6610 0.4377 0.0418  0.0297  -0.1262 61 LEU A CB  
482 C CG  . LEU A 61 ? 0.4146 0.6077 0.4566 0.0476  0.0262  -0.1200 61 LEU A CG  
483 C CD1 . LEU A 61 ? 0.4450 0.6122 0.5023 0.0611  0.0380  -0.1464 61 LEU A CD1 
484 C CD2 . LEU A 61 ? 0.4085 0.5730 0.4454 0.0351  0.0153  -0.1123 61 LEU A CD2 
485 N N   . ASN A 62 ? 0.3906 0.7516 0.3753 0.0321  0.0366  -0.0970 62 ASN A N   
486 C CA  . ASN A 62 ? 0.4158 0.8335 0.3763 0.0284  0.0414  -0.0953 62 ASN A CA  
487 C C   . ASN A 62 ? 0.4031 0.8317 0.3545 0.0202  0.0346  -0.0567 62 ASN A C   
488 O O   . ASN A 62 ? 0.3926 0.8543 0.3225 0.0163  0.0306  -0.0528 62 ASN A O   
489 C CB  . ASN A 62 ? 0.4458 0.9038 0.4086 0.0361  0.0565  -0.0984 62 ASN A CB  
490 C CG  . ASN A 62 ? 0.4693 0.9221 0.4396 0.0477  0.0667  -0.1391 62 ASN A CG  
491 O OD1 . ASN A 62 ? 0.4879 0.9100 0.4572 0.0472  0.0635  -0.1676 62 ASN A OD1 
492 N ND2 . ASN A 62 ? 0.4818 0.9629 0.4628 0.0583  0.0808  -0.1424 62 ASN A ND2 
493 N N   . SER A 63 ? 0.3793 0.7807 0.3482 0.0180  0.0338  -0.0290 63 SER A N   
494 C CA  . SER A 63 ? 0.3711 0.7684 0.3371 0.0115  0.0306  0.0066  63 SER A CA  
495 C C   . SER A 63 ? 0.3725 0.7519 0.3308 0.0099  0.0185  0.0059  63 SER A C   
496 O O   . SER A 63 ? 0.3780 0.7824 0.3232 0.0096  0.0165  0.0270  63 SER A O   
497 C CB  . SER A 63 ? 0.3531 0.7173 0.3413 0.0064  0.0326  0.0258  63 SER A CB  
498 O OG  . SER A 63 ? 0.3788 0.7700 0.3768 0.0057  0.0439  0.0283  63 SER A OG  
499 N N   . ILE A 64 ? 0.3655 0.7042 0.3345 0.0100  0.0113  -0.0147 64 ILE A N   
500 C CA  . ILE A 64 ? 0.3715 0.6917 0.3387 0.0069  0.0008  -0.0175 64 ILE A CA  
501 C C   . ILE A 64 ? 0.3976 0.7644 0.3450 0.0048  -0.0030 -0.0316 64 ILE A C   
502 O O   . ILE A 64 ? 0.4096 0.7936 0.3507 0.0034  -0.0101 -0.0154 64 ILE A O   
503 C CB  . ILE A 64 ? 0.3597 0.6321 0.3421 0.0069  -0.0027 -0.0380 64 ILE A CB  
504 C CG1 . ILE A 64 ? 0.3587 0.5947 0.3570 0.0074  -0.0024 -0.0197 64 ILE A CG1 
505 C CG2 . ILE A 64 ? 0.3664 0.6277 0.3474 0.0013  -0.0113 -0.0493 64 ILE A CG2 
506 C CD1 . ILE A 64 ? 0.3561 0.5570 0.3688 0.0112  -0.0034 -0.0347 64 ILE A CD1 
507 N N   . GLN A 65 ? 0.4325 0.8229 0.3712 0.0049  0.0019  -0.0631 65 GLN A N   
508 C CA  . GLN A 65 ? 0.4758 0.9183 0.3932 -0.0001 -0.0012 -0.0842 65 GLN A CA  
509 C C   . GLN A 65 ? 0.4808 0.9829 0.3784 0.0028  -0.0008 -0.0519 65 GLN A C   
510 O O   . GLN A 65 ? 0.4861 1.0258 0.3718 0.0004  -0.0099 -0.0421 65 GLN A O   
511 C CB  . GLN A 65 ? 0.5365 0.9867 0.4498 0.0004  0.0085  -0.1266 65 GLN A CB  
512 C CG  . GLN A 65 ? 0.6113 1.1156 0.5014 -0.0083 0.0065  -0.1603 65 GLN A CG  
513 C CD  . GLN A 65 ? 0.7004 1.2309 0.5796 -0.0045 0.0210  -0.1940 65 GLN A CD  
514 O OE1 . GLN A 65 ? 0.7573 1.2675 0.6491 0.0065  0.0329  -0.1907 65 GLN A OE1 
515 N NE2 . GLN A 65 ? 0.8041 1.3870 0.6599 -0.0139 0.0205  -0.2282 65 GLN A NE2 
516 N N   . LYS A 66 ? 0.4866 1.0004 0.3831 0.0083  0.0105  -0.0322 66 LYS A N   
517 C CA  . LYS A 66 ? 0.5132 1.0797 0.3927 0.0118  0.0149  0.0038  66 LYS A CA  
518 C C   . LYS A 66 ? 0.4994 1.0568 0.3839 0.0146  0.0077  0.0447  66 LYS A C   
519 O O   . LYS A 66 ? 0.5048 1.1160 0.3718 0.0186  0.0047  0.0675  66 LYS A O   
520 C CB  . LYS A 66 ? 0.5341 1.0991 0.4213 0.0144  0.0303  0.0202  66 LYS A CB  
521 C CG  . LYS A 66 ? 0.5866 1.2092 0.4558 0.0171  0.0395  0.0568  66 LYS A CG  
522 C CD  . LYS A 66 ? 0.6182 1.2389 0.4998 0.0159  0.0562  0.0767  66 LYS A CD  
523 C CE  . LYS A 66 ? 0.6655 1.3422 0.5292 0.0179  0.0668  0.1175  66 LYS A CE  
524 N NZ  . LYS A 66 ? 0.7069 1.3873 0.5843 0.0135  0.0847  0.1358  66 LYS A NZ  
525 N N   . ASN A 67 ? 0.4468 0.9399 0.3550 0.0141  0.0057  0.0549  67 ASN A N   
526 C CA  . ASN A 67 ? 0.4509 0.9277 0.3679 0.0191  0.0040  0.0946  67 ASN A CA  
527 C C   . ASN A 67 ? 0.4409 0.9076 0.3632 0.0189  -0.0095 0.0839  67 ASN A C   
528 O O   . ASN A 67 ? 0.4459 0.8923 0.3799 0.0249  -0.0107 0.1116  67 ASN A O   
529 C CB  . ASN A 67 ? 0.4403 0.8601 0.3788 0.0173  0.0141  0.1144  67 ASN A CB  
530 C CG  . ASN A 67 ? 0.4566 0.8966 0.3926 0.0155  0.0286  0.1321  67 ASN A CG  
531 O OD1 . ASN A 67 ? 0.4647 0.8878 0.4113 0.0094  0.0345  0.1164  67 ASN A OD1 
532 N ND2 . ASN A 67 ? 0.4603 0.9424 0.3837 0.0213  0.0351  0.1670  67 ASN A ND2 
533 N N   . HIS A 68 ? 0.4396 0.9215 0.3551 0.0117  -0.0179 0.0432  68 HIS A N   
534 C CA  . HIS A 68 ? 0.4473 0.9276 0.3692 0.0073  -0.0300 0.0288  68 HIS A CA  
535 C C   . HIS A 68 ? 0.4129 0.8256 0.3582 0.0080  -0.0300 0.0369  68 HIS A C   
536 O O   . HIS A 68 ? 0.4263 0.8390 0.3805 0.0107  -0.0360 0.0501  68 HIS A O   
537 C CB  . HIS A 68 ? 0.4908 1.0378 0.4017 0.0131  -0.0381 0.0526  68 HIS A CB  
538 C CG  . HIS A 68 ? 0.5413 1.1628 0.4249 0.0124  -0.0381 0.0468  68 HIS A CG  
539 N ND1 . HIS A 68 ? 0.5945 1.2599 0.4635 0.0000  -0.0454 0.0027  68 HIS A ND1 
540 C CD2 . HIS A 68 ? 0.5837 1.2436 0.4515 0.0212  -0.0300 0.0772  68 HIS A CD2 
541 C CE1 . HIS A 68 ? 0.6305 1.3641 0.4726 0.0019  -0.0428 0.0052  68 HIS A CE1 
542 N NE2 . HIS A 68 ? 0.6233 1.3558 0.4642 0.0155  -0.0334 0.0528  68 HIS A NE2 
543 N N   . VAL A 69 ? 0.3892 0.7503 0.3445 0.0059  -0.0232 0.0275  69 VAL A N   
544 C CA  . VAL A 69 ? 0.3499 0.6529 0.3234 0.0055  -0.0231 0.0319  69 VAL A CA  
545 C C   . VAL A 69 ? 0.3426 0.6266 0.3227 -0.0021 -0.0296 0.0014  69 VAL A C   
546 O O   . VAL A 69 ? 0.3515 0.6405 0.3277 -0.0072 -0.0292 -0.0278 69 VAL A O   
547 C CB  . VAL A 69 ? 0.3539 0.6211 0.3350 0.0056  -0.0143 0.0368  69 VAL A CB  
548 C CG1 . VAL A 69 ? 0.3412 0.5559 0.3372 0.0038  -0.0146 0.0390  69 VAL A CG1 
549 C CG2 . VAL A 69 ? 0.3680 0.6526 0.3456 0.0091  -0.0052 0.0667  69 VAL A CG2 
550 N N   . HIS A 70 ? 0.3246 0.5864 0.3161 -0.0026 -0.0333 0.0090  70 HIS A N   
551 C CA  . HIS A 70 ? 0.3475 0.5865 0.3486 -0.0111 -0.0372 -0.0134 70 HIS A CA  
552 C C   . HIS A 70 ? 0.3363 0.5210 0.3463 -0.0107 -0.0323 -0.0176 70 HIS A C   
553 O O   . HIS A 70 ? 0.3405 0.5014 0.3544 -0.0060 -0.0293 0.0011  70 HIS A O   
554 C CB  . HIS A 70 ? 0.3567 0.6018 0.3676 -0.0110 -0.0418 -0.0001 70 HIS A CB  
555 C CG  . HIS A 70 ? 0.4109 0.7180 0.4168 -0.0100 -0.0487 0.0067  70 HIS A CG  
556 N ND1 . HIS A 70 ? 0.4308 0.7823 0.4278 -0.0204 -0.0547 -0.0187 70 HIS A ND1 
557 C CD2 . HIS A 70 ? 0.4401 0.7762 0.4495 0.0008  -0.0503 0.0359  70 HIS A CD2 
558 C CE1 . HIS A 70 ? 0.4503 0.8638 0.4434 -0.0167 -0.0620 -0.0043 70 HIS A CE1 
559 N NE2 . HIS A 70 ? 0.4371 0.8415 0.4389 -0.0018 -0.0592 0.0316  70 HIS A NE2 
560 N N   . ILE A 71 ? 0.3431 0.5095 0.3567 -0.0152 -0.0307 -0.0423 71 ILE A N   
561 C CA  . ILE A 71 ? 0.3471 0.4691 0.3700 -0.0121 -0.0268 -0.0424 71 ILE A CA  
562 C C   . ILE A 71 ? 0.3273 0.4240 0.3601 -0.0183 -0.0283 -0.0434 71 ILE A C   
563 O O   . ILE A 71 ? 0.3281 0.4306 0.3654 -0.0278 -0.0292 -0.0607 71 ILE A O   
564 C CB  . ILE A 71 ? 0.3738 0.4868 0.3991 -0.0088 -0.0212 -0.0627 71 ILE A CB  
565 C CG1 . ILE A 71 ? 0.3819 0.5292 0.3973 -0.0038 -0.0181 -0.0646 71 ILE A CG1 
566 C CG2 . ILE A 71 ? 0.3815 0.4571 0.4176 -0.0016 -0.0181 -0.0556 71 ILE A CG2 
567 C CD1 . ILE A 71 ? 0.4223 0.5662 0.4413 0.0016  -0.0104 -0.0881 71 ILE A CD1 
568 N N   . ALA A 72 ? 0.3062 0.3781 0.3422 -0.0148 -0.0275 -0.0266 72 ALA A N   
569 C CA  . ALA A 72 ? 0.3222 0.3742 0.3660 -0.0199 -0.0271 -0.0237 72 ALA A CA  
570 C C   . ALA A 72 ? 0.3481 0.3694 0.3932 -0.0148 -0.0243 -0.0139 72 ALA A C   
571 O O   . ALA A 72 ? 0.3578 0.3790 0.3979 -0.0085 -0.0244 -0.0065 72 ALA A O   
572 C CB  . ALA A 72 ? 0.3187 0.3892 0.3628 -0.0210 -0.0293 -0.0111 72 ALA A CB  
573 N N   . ASN A 73 ? 0.3722 0.3721 0.4245 -0.0187 -0.0214 -0.0132 73 ASN A N   
574 C CA  . ASN A 73 ? 0.3552 0.3350 0.4058 -0.0137 -0.0193 0.0005  73 ASN A CA  
575 C C   . ASN A 73 ? 0.3480 0.3342 0.3922 -0.0154 -0.0195 0.0117  73 ASN A C   
576 O O   . ASN A 73 ? 0.3295 0.3311 0.3749 -0.0186 -0.0200 0.0110  73 ASN A O   
577 C CB  . ASN A 73 ? 0.3848 0.3383 0.4458 -0.0151 -0.0136 0.0009  73 ASN A CB  
578 C CG  . ASN A 73 ? 0.3819 0.3328 0.4518 -0.0284 -0.0102 -0.0022 73 ASN A CG  
579 O OD1 . ASN A 73 ? 0.3930 0.3601 0.4596 -0.0322 -0.0118 0.0039  73 ASN A OD1 
580 N ND2 . ASN A 73 ? 0.4035 0.3361 0.4871 -0.0363 -0.0045 -0.0142 73 ASN A ND2 
581 N N   . PRO A 74 ? 0.3265 0.3048 0.3636 -0.0119 -0.0184 0.0221  74 PRO A N   
582 C CA  . PRO A 74 ? 0.2996 0.2821 0.3293 -0.0135 -0.0159 0.0277  74 PRO A CA  
583 C C   . PRO A 74 ? 0.3012 0.2854 0.3374 -0.0186 -0.0111 0.0302  74 PRO A C   
584 O O   . PRO A 74 ? 0.3080 0.3001 0.3428 -0.0177 -0.0075 0.0319  74 PRO A O   
585 C CB  . PRO A 74 ? 0.3372 0.3171 0.3563 -0.0106 -0.0162 0.0347  74 PRO A CB  
586 C CG  . PRO A 74 ? 0.3505 0.3319 0.3729 -0.0049 -0.0210 0.0338  74 PRO A CG  
587 C CD  . PRO A 74 ? 0.3648 0.3364 0.3997 -0.0049 -0.0195 0.0280  74 PRO A CD  
588 N N   . ASP A 75 ? 0.3164 0.2929 0.3628 -0.0240 -0.0092 0.0300  75 ASP A N   
589 C CA  . ASP A 75 ? 0.3353 0.3186 0.3923 -0.0323 -0.0041 0.0317  75 ASP A CA  
590 C C   . ASP A 75 ? 0.3069 0.3163 0.3724 -0.0342 -0.0070 0.0250  75 ASP A C   
591 O O   . ASP A 75 ? 0.3016 0.3271 0.3755 -0.0371 -0.0030 0.0288  75 ASP A O   
592 C CB  . ASP A 75 ? 0.3700 0.3373 0.4405 -0.0417 -0.0001 0.0301  75 ASP A CB  
593 C CG  . ASP A 75 ? 0.4419 0.3872 0.5080 -0.0386 0.0061  0.0462  75 ASP A CG  
594 O OD1 . ASP A 75 ? 0.4417 0.3944 0.4928 -0.0321 0.0070  0.0573  75 ASP A OD1 
595 O OD2 . ASP A 75 ? 0.5218 0.4441 0.5995 -0.0425 0.0110  0.0474  75 ASP A OD2 
596 N N   . PHE A 76 ? 0.2941 0.3130 0.3581 -0.0316 -0.0133 0.0171  76 PHE A N   
597 C CA  . PHE A 76 ? 0.2889 0.3393 0.3582 -0.0296 -0.0167 0.0167  76 PHE A CA  
598 C C   . PHE A 76 ? 0.2893 0.3434 0.3566 -0.0194 -0.0115 0.0291  76 PHE A C   
599 O O   . PHE A 76 ? 0.2846 0.3631 0.3634 -0.0171 -0.0096 0.0344  76 PHE A O   
600 C CB  . PHE A 76 ? 0.2894 0.3510 0.3527 -0.0267 -0.0227 0.0101  76 PHE A CB  
601 C CG  . PHE A 76 ? 0.2938 0.3936 0.3607 -0.0219 -0.0262 0.0161  76 PHE A CG  
602 C CD1 . PHE A 76 ? 0.3033 0.4391 0.3827 -0.0294 -0.0300 0.0112  76 PHE A CD1 
603 C CD2 . PHE A 76 ? 0.3042 0.4066 0.3641 -0.0100 -0.0248 0.0287  76 PHE A CD2 
604 C CE1 . PHE A 76 ? 0.3005 0.4805 0.3838 -0.0219 -0.0342 0.0212  76 PHE A CE1 
605 C CE2 . PHE A 76 ? 0.3121 0.4499 0.3765 -0.0020 -0.0265 0.0410  76 PHE A CE2 
606 C CZ  . PHE A 76 ? 0.2997 0.4795 0.3751 -0.0063 -0.0321 0.0383  76 PHE A CZ  
607 N N   . ILE A 77 ? 0.2685 0.3000 0.3232 -0.0135 -0.0082 0.0323  77 ILE A N   
608 C CA  . ILE A 77 ? 0.2945 0.3209 0.3471 -0.0055 -0.0002 0.0384  77 ILE A CA  
609 C C   . ILE A 77 ? 0.2962 0.3231 0.3513 -0.0071 0.0072  0.0400  77 ILE A C   
610 O O   . ILE A 77 ? 0.3170 0.3571 0.3820 -0.0004 0.0142  0.0447  77 ILE A O   
611 C CB  . ILE A 77 ? 0.3215 0.3260 0.3606 -0.0042 0.0013  0.0356  77 ILE A CB  
612 C CG1 . ILE A 77 ? 0.3537 0.3608 0.3917 -0.0036 -0.0041 0.0356  77 ILE A CG1 
613 C CG2 . ILE A 77 ? 0.3272 0.3200 0.3651 0.0015  0.0126  0.0361  77 ILE A CG2 
614 C CD1 . ILE A 77 ? 0.3531 0.3754 0.3996 0.0041  -0.0023 0.0453  77 ILE A CD1 
615 N N   . TRP A 78 ? 0.2984 0.3136 0.3454 -0.0142 0.0072  0.0386  78 TRP A N   
616 C CA  . TRP A 78 ? 0.3239 0.3415 0.3691 -0.0163 0.0158  0.0426  78 TRP A CA  
617 C C   . TRP A 78 ? 0.3013 0.3428 0.3670 -0.0195 0.0194  0.0462  78 TRP A C   
618 O O   . TRP A 78 ? 0.2818 0.3364 0.3525 -0.0149 0.0290  0.0493  78 TRP A O   
619 C CB  . TRP A 78 ? 0.3464 0.3520 0.3823 -0.0227 0.0147  0.0471  78 TRP A CB  
620 C CG  . TRP A 78 ? 0.3681 0.3614 0.3863 -0.0198 0.0097  0.0460  78 TRP A CG  
621 C CD1 . TRP A 78 ? 0.3879 0.3719 0.4042 -0.0205 0.0046  0.0513  78 TRP A CD1 
622 C CD2 . TRP A 78 ? 0.3712 0.3640 0.3740 -0.0166 0.0105  0.0392  78 TRP A CD2 
623 N NE1 . TRP A 78 ? 0.3718 0.3572 0.3732 -0.0166 0.0000  0.0502  78 TRP A NE1 
624 C CE2 . TRP A 78 ? 0.3907 0.3820 0.3830 -0.0167 0.0032  0.0409  78 TRP A CE2 
625 C CE3 . TRP A 78 ? 0.3691 0.3617 0.3684 -0.0138 0.0180  0.0306  78 TRP A CE3 
626 C CZ2 . TRP A 78 ? 0.3802 0.3768 0.3582 -0.0179 0.0012  0.0326  78 TRP A CZ2 
627 C CZ3 . TRP A 78 ? 0.3931 0.3814 0.3779 -0.0158 0.0182  0.0202  78 TRP A CZ3 
628 C CH2 . TRP A 78 ? 0.3926 0.3862 0.3666 -0.0196 0.0089  0.0204  78 TRP A CH2 
629 N N   . LYS A 79 ? 0.3143 0.3649 0.3931 -0.0286 0.0124  0.0435  79 LYS A N   
630 C CA  . LYS A 79 ? 0.3286 0.4076 0.4291 -0.0374 0.0145  0.0442  79 LYS A CA  
631 C C   . LYS A 79 ? 0.2942 0.4087 0.4084 -0.0277 0.0126  0.0463  79 LYS A C   
632 O O   . LYS A 79 ? 0.2939 0.4400 0.4263 -0.0284 0.0177  0.0508  79 LYS A O   
633 C CB  . LYS A 79 ? 0.3740 0.4484 0.4845 -0.0544 0.0095  0.0360  79 LYS A CB  
634 C CG  . LYS A 79 ? 0.4884 0.5272 0.5907 -0.0601 0.0150  0.0410  79 LYS A CG  
635 C CD  . LYS A 79 ? 0.5830 0.6111 0.7029 -0.0789 0.0187  0.0369  79 LYS A CD  
636 C CE  . LYS A 79 ? 0.6184 0.6101 0.7299 -0.0782 0.0265  0.0505  79 LYS A CE  
637 N NZ  . LYS A 79 ? 0.7203 0.6929 0.8524 -0.0964 0.0345  0.0494  79 LYS A NZ  
638 N N   . SER A 80 ? 0.2750 0.3888 0.3825 -0.0176 0.0062  0.0461  80 SER A N   
639 C CA  . SER A 80 ? 0.2892 0.4350 0.4090 -0.0034 0.0061  0.0552  80 SER A CA  
640 C C   . SER A 80 ? 0.3179 0.4574 0.4410 0.0115  0.0203  0.0634  80 SER A C   
641 O O   . SER A 80 ? 0.3178 0.4916 0.4610 0.0209  0.0253  0.0719  80 SER A O   
642 C CB  . SER A 80 ? 0.2819 0.4249 0.3925 0.0047  -0.0006 0.0579  80 SER A CB  
643 O OG  . SER A 80 ? 0.2610 0.4213 0.3702 -0.0075 -0.0124 0.0480  80 SER A OG  
644 N N   . ILE A 81 ? 0.3166 0.4161 0.4209 0.0137  0.0275  0.0590  81 ILE A N   
645 C CA  . ILE A 81 ? 0.3540 0.4422 0.4573 0.0256  0.0430  0.0596  81 ILE A CA  
646 C C   . ILE A 81 ? 0.3408 0.4534 0.4551 0.0218  0.0512  0.0609  81 ILE A C   
647 O O   . ILE A 81 ? 0.3497 0.4796 0.4785 0.0354  0.0633  0.0654  81 ILE A O   
648 C CB  . ILE A 81 ? 0.3797 0.4277 0.4577 0.0221  0.0467  0.0490  81 ILE A CB  
649 C CG1 . ILE A 81 ? 0.4007 0.4257 0.4726 0.0265  0.0436  0.0482  81 ILE A CG1 
650 C CG2 . ILE A 81 ? 0.4072 0.4473 0.4792 0.0278  0.0635  0.0423  81 ILE A CG2 
651 C CD1 . ILE A 81 ? 0.4362 0.4541 0.5214 0.0442  0.0558  0.0551  81 ILE A CD1 
652 N N   . ARG A 82 ? 0.3332 0.4464 0.4426 0.0039  0.0464  0.0585  82 ARG A N   
653 C CA  . ARG A 82 ? 0.3611 0.4957 0.4804 -0.0038 0.0553  0.0620  82 ARG A CA  
654 C C   . ARG A 82 ? 0.3477 0.5313 0.4994 -0.0029 0.0550  0.0679  82 ARG A C   
655 O O   . ARG A 82 ? 0.3385 0.5488 0.5046 0.0028  0.0676  0.0726  82 ARG A O   
656 C CB  . ARG A 82 ? 0.3701 0.4897 0.4808 -0.0234 0.0511  0.0623  82 ARG A CB  
657 C CG  . ARG A 82 ? 0.4380 0.5823 0.5645 -0.0352 0.0611  0.0693  82 ARG A CG  
658 C CD  . ARG A 82 ? 0.5039 0.6256 0.6205 -0.0509 0.0630  0.0754  82 ARG A CD  
659 N NE  . ARG A 82 ? 0.5413 0.6437 0.6279 -0.0428 0.0693  0.0792  82 ARG A NE  
660 C CZ  . ARG A 82 ? 0.5900 0.6644 0.6565 -0.0450 0.0642  0.0832  82 ARG A CZ  
661 N NH1 . ARG A 82 ? 0.6488 0.7037 0.7237 -0.0534 0.0551  0.0836  82 ARG A NH1 
662 N NH2 . ARG A 82 ? 0.5300 0.5998 0.5690 -0.0384 0.0688  0.0860  82 ARG A NH2 
663 N N   . GLU A 83 ? 0.3272 0.5287 0.4901 -0.0087 0.0408  0.0668  83 GLU A N   
664 C CA  A GLU A 83 ? 0.3311 0.5903 0.5246 -0.0115 0.0368  0.0708  83 GLU A CA  
665 C CA  B GLU A 83 ? 0.3287 0.5877 0.5220 -0.0116 0.0364  0.0707  83 GLU A CA  
666 C C   . GLU A 83 ? 0.3355 0.6215 0.5416 0.0155  0.0393  0.0824  83 GLU A C   
667 O O   . GLU A 83 ? 0.3003 0.6445 0.5343 0.0198  0.0370  0.0902  83 GLU A O   
668 C CB  A GLU A 83 ? 0.3367 0.6060 0.5337 -0.0330 0.0214  0.0604  83 GLU A CB  
669 C CB  B GLU A 83 ? 0.3289 0.5992 0.5249 -0.0301 0.0201  0.0609  83 GLU A CB  
670 C CG  A GLU A 83 ? 0.3581 0.6017 0.5529 -0.0582 0.0247  0.0524  83 GLU A CG  
671 C CG  B GLU A 83 ? 0.3461 0.5909 0.5391 -0.0565 0.0205  0.0506  83 GLU A CG  
672 C CD  A GLU A 83 ? 0.3676 0.6147 0.5700 -0.0819 0.0141  0.0371  83 GLU A CD  
673 C CD  B GLU A 83 ? 0.3607 0.6261 0.5739 -0.0708 0.0320  0.0545  83 GLU A CD  
674 O OE1 A GLU A 83 ? 0.3673 0.6670 0.5910 -0.0908 0.0062  0.0307  83 GLU A OE1 
675 O OE1 B GLU A 83 ? 0.3580 0.6799 0.5982 -0.0714 0.0326  0.0576  83 GLU A OE1 
676 O OE2 A GLU A 83 ? 0.3919 0.5918 0.5803 -0.0916 0.0146  0.0308  83 GLU A OE2 
677 O OE2 B GLU A 83 ? 0.3912 0.6208 0.5944 -0.0811 0.0408  0.0568  83 GLU A OE2 
678 N N   . LYS A 84 ? 0.3372 0.5817 0.5252 0.0335  0.0450  0.0847  84 LYS A N   
679 C CA  . LYS A 84 ? 0.3587 0.6126 0.5586 0.0615  0.0518  0.0983  84 LYS A CA  
680 C C   . LYS A 84 ? 0.3357 0.6335 0.5486 0.0658  0.0366  0.1096  84 LYS A C   
681 O O   . LYS A 84 ? 0.3080 0.6496 0.5449 0.0865  0.0392  0.1270  84 LYS A O   
682 C CB  . LYS A 84 ? 0.3862 0.6665 0.6091 0.0788  0.0693  0.1055  84 LYS A CB  
683 C CG  . LYS A 84 ? 0.4370 0.6768 0.6427 0.0783  0.0869  0.0933  84 LYS A CG  
684 C CD  . LYS A 84 ? 0.4827 0.7452 0.7098 0.0992  0.1080  0.0979  84 LYS A CD  
685 C CE  . LYS A 84 ? 0.5444 0.7687 0.7482 0.0972  0.1253  0.0818  84 LYS A CE  
686 N NZ  . LYS A 84 ? 0.5885 0.8449 0.8123 0.1117  0.1460  0.0830  84 LYS A NZ  
687 N N   . ARG A 85 ? 0.2922 0.5806 0.4884 0.0479  0.0215  0.1002  85 ARG A N   
688 C CA  . ARG A 85 ? 0.2816 0.6187 0.4847 0.0460  0.0056  0.1053  85 ARG A CA  
689 C C   . ARG A 85 ? 0.2933 0.5986 0.4706 0.0312  -0.0047 0.0922  85 ARG A C   
690 O O   . ARG A 85 ? 0.2647 0.5337 0.4290 0.0124  -0.0048 0.0752  85 ARG A O   
691 C CB  . ARG A 85 ? 0.2709 0.6707 0.4974 0.0286  -0.0016 0.0987  85 ARG A CB  
692 C CG  . ARG A 85 ? 0.2549 0.7221 0.4902 0.0228  -0.0193 0.0994  85 ARG A CG  
693 C CD  . ARG A 85 ? 0.2460 0.7816 0.5105 0.0045  -0.0245 0.0918  85 ARG A CD  
694 N NE  . ARG A 85 ? 0.2427 0.7519 0.5050 -0.0298 -0.0240 0.0663  85 ARG A NE  
695 C CZ  . ARG A 85 ? 0.2529 0.7469 0.5017 -0.0546 -0.0334 0.0436  85 ARG A CZ  
696 N NH1 . ARG A 85 ? 0.2384 0.7506 0.4725 -0.0513 -0.0460 0.0401  85 ARG A NH1 
697 N NH2 . ARG A 85 ? 0.2647 0.7259 0.5155 -0.0820 -0.0286 0.0250  85 ARG A NH2 
698 N N   . LEU A 86 ? 0.2984 0.6187 0.4691 0.0418  -0.0117 0.1029  86 LEU A N   
699 C CA  . LEU A 86 ? 0.2953 0.5953 0.4435 0.0294  -0.0206 0.0906  86 LEU A CA  
700 C C   . LEU A 86 ? 0.2798 0.6118 0.4308 0.0036  -0.0326 0.0682  86 LEU A C   
701 O O   . LEU A 86 ? 0.2459 0.6428 0.4116 0.0003  -0.0414 0.0692  86 LEU A O   
702 C CB  . LEU A 86 ? 0.3114 0.6318 0.4539 0.0466  -0.0239 0.1103  86 LEU A CB  
703 C CG  . LEU A 86 ? 0.3322 0.6316 0.4509 0.0378  -0.0295 0.1009  86 LEU A CG  
704 C CD1 . LEU A 86 ? 0.3259 0.5542 0.4313 0.0358  -0.0197 0.0941  86 LEU A CD1 
705 C CD2 . LEU A 86 ? 0.3493 0.6826 0.4636 0.0540  -0.0322 0.1244  86 LEU A CD2 
706 N N   . LEU A 87 ? 0.2776 0.5652 0.4167 -0.0145 -0.0319 0.0478  87 LEU A N   
707 C CA  . LEU A 87 ? 0.2670 0.5699 0.4116 -0.0402 -0.0386 0.0240  87 LEU A CA  
708 C C   . LEU A 87 ? 0.2707 0.5889 0.4007 -0.0466 -0.0485 0.0096  87 LEU A C   
709 O O   . LEU A 87 ? 0.2701 0.5960 0.3869 -0.0308 -0.0509 0.0223  87 LEU A O   
710 C CB  . LEU A 87 ? 0.2810 0.5286 0.4237 -0.0535 -0.0300 0.0136  87 LEU A CB  
711 C CG  . LEU A 87 ? 0.2764 0.5122 0.4292 -0.0482 -0.0187 0.0267  87 LEU A CG  
712 C CD1 . LEU A 87 ? 0.3060 0.4927 0.4536 -0.0607 -0.0106 0.0208  87 LEU A CD1 
713 C CD2 . LEU A 87 ? 0.2809 0.5762 0.4605 -0.0528 -0.0195 0.0304  87 LEU A CD2 
714 N N   . ASP A 88 ? 0.2700 0.5949 0.4042 -0.0709 -0.0525 -0.0177 88 ASP A N   
715 C CA  . ASP A 88 ? 0.3000 0.6413 0.4206 -0.0798 -0.0598 -0.0388 88 ASP A CA  
716 C C   . ASP A 88 ? 0.3071 0.5832 0.4105 -0.0758 -0.0532 -0.0452 88 ASP A C   
717 O O   . ASP A 88 ? 0.3442 0.5752 0.4524 -0.0879 -0.0465 -0.0597 88 ASP A O   
718 C CB  . ASP A 88 ? 0.3151 0.6858 0.4493 -0.1093 -0.0641 -0.0710 88 ASP A CB  
719 C CG  . ASP A 88 ? 0.3423 0.7453 0.4619 -0.1196 -0.0718 -0.0979 88 ASP A CG  
720 O OD1 . ASP A 88 ? 0.3594 0.7532 0.4570 -0.1034 -0.0722 -0.0908 88 ASP A OD1 
721 O OD2 . ASP A 88 ? 0.3857 0.8282 0.5164 -0.1450 -0.0768 -0.1267 88 ASP A OD2 
722 N N   . VAL A 89 ? 0.3085 0.5843 0.3941 -0.0587 -0.0544 -0.0325 89 VAL A N   
723 C CA  . VAL A 89 ? 0.3040 0.5291 0.3757 -0.0523 -0.0486 -0.0346 89 VAL A CA  
724 C C   . VAL A 89 ? 0.3488 0.5600 0.4180 -0.0670 -0.0475 -0.0663 89 VAL A C   
725 O O   . VAL A 89 ? 0.3434 0.5071 0.4090 -0.0636 -0.0409 -0.0705 89 VAL A O   
726 C CB  . VAL A 89 ? 0.3056 0.5450 0.3624 -0.0348 -0.0496 -0.0151 89 VAL A CB  
727 C CG1 . VAL A 89 ? 0.3176 0.6131 0.3634 -0.0371 -0.0569 -0.0239 89 VAL A CG1 
728 C CG2 . VAL A 89 ? 0.2946 0.4847 0.3418 -0.0278 -0.0430 -0.0123 89 VAL A CG2 
729 N N   . LYS A 90 ? 0.3694 0.6251 0.4415 -0.0828 -0.0534 -0.0895 90 LYS A N   
730 C CA  . LYS A 90 ? 0.4307 0.6720 0.5032 -0.0993 -0.0498 -0.1260 90 LYS A CA  
731 C C   . LYS A 90 ? 0.4279 0.6111 0.5191 -0.1115 -0.0397 -0.1355 90 LYS A C   
732 O O   . LYS A 90 ? 0.4748 0.6235 0.5688 -0.1193 -0.0317 -0.1603 90 LYS A O   
733 C CB  . LYS A 90 ? 0.5151 0.8208 0.5886 -0.1192 -0.0580 -0.1540 90 LYS A CB  
734 C CG  . LYS A 90 ? 0.5721 0.9490 0.6262 -0.1093 -0.0685 -0.1453 90 LYS A CG  
735 C CD  . LYS A 90 ? 0.6550 1.0215 0.6865 -0.0957 -0.0643 -0.1469 90 LYS A CD  
736 C CE  . LYS A 90 ? 0.7134 1.1557 0.7252 -0.0876 -0.0733 -0.1357 90 LYS A CE  
737 N NZ  . LYS A 90 ? 0.7394 1.1692 0.7322 -0.0712 -0.0671 -0.1247 90 LYS A NZ  
738 N N   . ASN A 91 ? 0.3932 0.5659 0.4979 -0.1125 -0.0381 -0.1154 91 ASN A N   
739 C CA  . ASN A 91 ? 0.4340 0.5538 0.5553 -0.1228 -0.0270 -0.1173 91 ASN A CA  
740 C C   . ASN A 91 ? 0.4135 0.4777 0.5268 -0.1034 -0.0197 -0.0963 91 ASN A C   
741 O O   . ASN A 91 ? 0.4232 0.4439 0.5475 -0.1072 -0.0100 -0.0903 91 ASN A O   
742 C CB  . ASN A 91 ? 0.4560 0.5952 0.5952 -0.1332 -0.0268 -0.1047 91 ASN A CB  
743 C CG  . ASN A 91 ? 0.4935 0.6907 0.6476 -0.1569 -0.0336 -0.1273 91 ASN A CG  
744 O OD1 . ASN A 91 ? 0.5183 0.7297 0.6703 -0.1715 -0.0360 -0.1590 91 ASN A OD1 
745 N ND2 . ASN A 91 ? 0.5041 0.7394 0.6739 -0.1618 -0.0361 -0.1135 91 ASN A ND2 
746 N N   . TYR A 92 ? 0.3740 0.4433 0.4693 -0.0837 -0.0239 -0.0836 92 TYR A N   
747 C CA  . TYR A 92 ? 0.3653 0.3963 0.4535 -0.0671 -0.0195 -0.0631 92 TYR A CA  
748 C C   . TYR A 92 ? 0.3713 0.3942 0.4486 -0.0551 -0.0192 -0.0697 92 TYR A C   
749 O O   . TYR A 92 ? 0.3495 0.3622 0.4182 -0.0408 -0.0195 -0.0527 92 TYR A O   
750 C CB  . TYR A 92 ? 0.3325 0.3787 0.4137 -0.0567 -0.0230 -0.0383 92 TYR A CB  
751 C CG  . TYR A 92 ? 0.3463 0.4014 0.4402 -0.0658 -0.0207 -0.0308 92 TYR A CG  
752 C CD1 . TYR A 92 ? 0.3583 0.3822 0.4570 -0.0672 -0.0128 -0.0193 92 TYR A CD1 
753 C CD2 . TYR A 92 ? 0.3467 0.4477 0.4492 -0.0733 -0.0259 -0.0346 92 TYR A CD2 
754 C CE1 . TYR A 92 ? 0.3682 0.4037 0.4796 -0.0766 -0.0086 -0.0127 92 TYR A CE1 
755 C CE2 . TYR A 92 ? 0.3418 0.4573 0.4602 -0.0820 -0.0229 -0.0286 92 TYR A CE2 
756 C CZ  . TYR A 92 ? 0.3659 0.4471 0.4888 -0.0844 -0.0134 -0.0183 92 TYR A CZ  
757 O OH  . TYR A 92 ? 0.3697 0.4690 0.5089 -0.0936 -0.0086 -0.0120 92 TYR A OH  
758 N N   . ASP A 93 ? 0.4132 0.4447 0.4914 -0.0620 -0.0179 -0.0964 93 ASP A N   
759 C CA  . ASP A 93 ? 0.4629 0.4945 0.5316 -0.0503 -0.0159 -0.1047 93 ASP A CA  
760 C C   . ASP A 93 ? 0.5047 0.4865 0.5847 -0.0429 -0.0050 -0.1085 93 ASP A C   
761 O O   . ASP A 93 ? 0.5612 0.5176 0.6547 -0.0532 0.0033  -0.1292 93 ASP A O   
762 C CB  . ASP A 93 ? 0.5009 0.5720 0.5617 -0.0587 -0.0183 -0.1322 93 ASP A CB  
763 C CG  . ASP A 93 ? 0.5385 0.6222 0.5870 -0.0456 -0.0157 -0.1380 93 ASP A CG  
764 O OD1 . ASP A 93 ? 0.5113 0.5687 0.5622 -0.0306 -0.0112 -0.1242 93 ASP A OD1 
765 O OD2 . ASP A 93 ? 0.5839 0.7109 0.6202 -0.0504 -0.0185 -0.1553 93 ASP A OD2 
766 N N   . PRO A 94 ? 0.5199 0.4886 0.5971 -0.0248 -0.0040 -0.0888 94 PRO A N   
767 C CA  . PRO A 94 ? 0.5805 0.5095 0.6703 -0.0126 0.0059  -0.0872 94 PRO A CA  
768 C C   . PRO A 94 ? 0.6584 0.5810 0.7542 -0.0083 0.0153  -0.1155 94 PRO A C   
769 O O   . PRO A 94 ? 0.7202 0.6069 0.8308 0.0043  0.0264  -0.1152 94 PRO A O   
770 C CB  . PRO A 94 ? 0.5383 0.4742 0.6223 0.0039  0.0014  -0.0603 94 PRO A CB  
771 C CG  . PRO A 94 ? 0.5302 0.5046 0.5982 -0.0004 -0.0086 -0.0536 94 PRO A CG  
772 C CD  . PRO A 94 ? 0.4969 0.4899 0.5611 -0.0161 -0.0118 -0.0672 94 PRO A CD  
773 N N   . TYR A 95 ? 0.7126 0.6721 0.7966 -0.0169 0.0120  -0.1387 95 TYR A N   
774 C CA  . TYR A 95 ? 0.7838 0.7445 0.8696 -0.0141 0.0218  -0.1707 95 TYR A CA  
775 C C   . TYR A 95 ? 0.9191 0.8774 1.0086 -0.0370 0.0261  -0.2074 95 TYR A C   
776 O O   . TYR A 95 ? 0.9754 0.9135 1.0729 -0.0376 0.0393  -0.2396 95 TYR A O   
777 C CB  . TYR A 95 ? 0.7460 0.7574 0.8137 -0.0062 0.0168  -0.1705 95 TYR A CB  
778 C CG  . TYR A 95 ? 0.6595 0.6712 0.7301 0.0147  0.0172  -0.1446 95 TYR A CG  
779 C CD1 . TYR A 95 ? 0.6584 0.6567 0.7415 0.0325  0.0291  -0.1531 95 TYR A CD1 
780 C CD2 . TYR A 95 ? 0.6020 0.6294 0.6655 0.0161  0.0067  -0.1135 95 TYR A CD2 
781 C CE1 . TYR A 95 ? 0.6012 0.6102 0.6901 0.0504  0.0283  -0.1297 95 TYR A CE1 
782 C CE2 . TYR A 95 ? 0.5731 0.6066 0.6410 0.0306  0.0064  -0.0938 95 TYR A CE2 
783 C CZ  . TYR A 95 ? 0.5909 0.6197 0.6718 0.0474  0.0161  -0.1010 95 TYR A CZ  
784 O OH  . TYR A 95 ? 0.5779 0.6227 0.6660 0.0608  0.0147  -0.0817 95 TYR A OH  
785 N N   . LYS A 96 ? 0.9745 0.9554 1.0602 -0.0562 0.0158  -0.2047 96 LYS A N   
786 C CA  . LYS A 96 ? 1.0716 1.0537 1.1654 -0.0821 0.0188  -0.2388 96 LYS A CA  
787 C C   . LYS A 96 ? 1.1271 1.0848 1.2373 -0.0959 0.0179  -0.2224 96 LYS A C   
788 O O   . LYS A 96 ? 1.0896 1.0882 1.1960 -0.1095 0.0064  -0.2167 96 LYS A O   
789 C CB  . LYS A 96 ? 1.0985 1.1525 1.1728 -0.0958 0.0073  -0.2592 96 LYS A CB  
790 C CG  . LYS A 96 ? 1.1775 1.2440 1.2600 -0.1262 0.0093  -0.3015 96 LYS A CG  
791 C CD  . LYS A 96 ? 1.1912 1.3361 1.2522 -0.1387 -0.0006 -0.3288 96 LYS A CD  
792 C CE  . LYS A 96 ? 1.2227 1.3816 1.2946 -0.1725 0.0010  -0.3742 96 LYS A CE  
793 N NZ  . LYS A 96 ? 1.2482 1.4956 1.2970 -0.1854 -0.0110 -0.3994 96 LYS A NZ  
794 N N   . PRO A 97 ? 1.1892 1.0834 1.3191 -0.0907 0.0310  -0.2109 97 PRO A N   
795 C CA  . PRO A 97 ? 1.2080 1.0753 1.3570 -0.1096 0.0359  -0.2049 97 PRO A CA  
796 C C   . PRO A 97 ? 1.2279 1.0979 1.3909 -0.1418 0.0418  -0.2485 97 PRO A C   
797 O O   . PRO A 97 ? 1.2156 1.1053 1.3881 -0.1644 0.0371  -0.2471 97 PRO A O   
798 C CB  . PRO A 97 ? 1.2468 1.0468 1.4120 -0.0926 0.0511  -0.1820 97 PRO A CB  
799 C CG  . PRO A 97 ? 1.2121 1.0196 1.3632 -0.0616 0.0477  -0.1658 97 PRO A CG  
800 C CD  . PRO A 97 ? 1.2006 1.0523 1.3361 -0.0645 0.0418  -0.1974 97 PRO A CD  
# 
