data_9MIZ
# 
_entry.id   9MIZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MIZ         pdb_00009miz 10.2210/pdb9miz/pdb 
WWPDB D_1000291070 ?            ?                   
# 
_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       2025-06-11 
_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                        9MIZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-13 
_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           N 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              fuglestadb@vcu.edu 
_pdbx_contact_author.name_first         Brian 
_pdbx_contact_author.name_last          Fuglestad 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8304-8269 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Birchfield, A.B.' 1 0000-0001-9402-7615 
'Musayev, F.N.'    2 0000-0002-7969-1590 
'Fuglestad, B.'    3 0000-0001-8304-8269 
# 
_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            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Broad PFAS Binding with Fatty Acid Binding Protein 4 Is Enabled by Variable Binding Modes' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.5c00504 
_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 'Birchfield, A.S.' 1 ? 
primary 'Musayev, F.N.'    2 ? 
primary 'Castillo, A.J.'   3 ? 
primary 'Zorn, G.'         4 ? 
primary 'Fuglestad, B.'    5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Fatty acid-binding protein, adipocyte' 14935.098 1   ? ? ? ? 
2 non-polymer syn 'nonadecafluorodecanoic acid'           514.083   1   ? ? ? ? 
3 water       nat water                                   18.015    214 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Adipocyte lipid-binding protein,ALBP,Adipocyte-type fatty acid-binding protein,A-FABP,AFABP,Fatty acid-binding protein 4' 
# 
_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       
;GHMCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADD
RKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADD
RKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA
;
_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 'nonadecafluorodecanoic acid' A1BLY 
3 water                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   CYS n 
1 5   ASP n 
1 6   ALA n 
1 7   PHE n 
1 8   VAL n 
1 9   GLY n 
1 10  THR n 
1 11  TRP n 
1 12  LYS n 
1 13  LEU n 
1 14  VAL n 
1 15  SER n 
1 16  SER n 
1 17  GLU n 
1 18  ASN n 
1 19  PHE n 
1 20  ASP n 
1 21  ASP n 
1 22  TYR n 
1 23  MET n 
1 24  LYS n 
1 25  GLU n 
1 26  VAL n 
1 27  GLY n 
1 28  VAL n 
1 29  GLY n 
1 30  PHE n 
1 31  ALA n 
1 32  THR n 
1 33  ARG n 
1 34  LYS n 
1 35  VAL n 
1 36  ALA n 
1 37  GLY n 
1 38  MET n 
1 39  ALA n 
1 40  LYS n 
1 41  PRO n 
1 42  ASN n 
1 43  MET n 
1 44  ILE n 
1 45  ILE n 
1 46  SER n 
1 47  VAL n 
1 48  ASN n 
1 49  GLY n 
1 50  ASP n 
1 51  VAL n 
1 52  ILE n 
1 53  THR n 
1 54  ILE n 
1 55  LYS n 
1 56  SER n 
1 57  GLU n 
1 58  SER n 
1 59  THR n 
1 60  PHE n 
1 61  LYS n 
1 62  ASN n 
1 63  THR n 
1 64  GLU n 
1 65  ILE n 
1 66  SER n 
1 67  PHE n 
1 68  ILE n 
1 69  LEU n 
1 70  GLY n 
1 71  GLN n 
1 72  GLU n 
1 73  PHE n 
1 74  ASP n 
1 75  GLU n 
1 76  VAL n 
1 77  THR n 
1 78  ALA n 
1 79  ASP n 
1 80  ASP n 
1 81  ARG n 
1 82  LYS n 
1 83  VAL n 
1 84  LYS n 
1 85  SER n 
1 86  THR n 
1 87  ILE n 
1 88  THR n 
1 89  LEU n 
1 90  ASP n 
1 91  GLY n 
1 92  GLY n 
1 93  VAL n 
1 94  LEU n 
1 95  VAL n 
1 96  HIS n 
1 97  VAL n 
1 98  GLN n 
1 99  LYS n 
1 100 TRP n 
1 101 ASP n 
1 102 GLY n 
1 103 LYS n 
1 104 SER n 
1 105 THR n 
1 106 THR n 
1 107 ILE n 
1 108 LYS n 
1 109 ARG n 
1 110 LYS n 
1 111 ARG n 
1 112 GLU n 
1 113 ASP n 
1 114 ASP n 
1 115 LYS n 
1 116 LEU n 
1 117 VAL n 
1 118 VAL n 
1 119 GLU n 
1 120 CYS n 
1 121 VAL n 
1 122 MET n 
1 123 LYS n 
1 124 GLY n 
1 125 VAL n 
1 126 THR n 
1 127 SER n 
1 128 THR n 
1 129 ARG n 
1 130 VAL n 
1 131 TYR n 
1 132 GLU n 
1 133 ARG n 
1 134 ALA 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                   134 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FABP4 
_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 
A1BLY non-polymer         . 'nonadecafluorodecanoic acid' ? 'C10 H F19 O2'   514.083 
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 
THR   'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  -2  GLY GLY A . n 
A 1 2   HIS 2   -1  -1  HIS HIS A . n 
A 1 3   MET 3   0   0   MET MET A . n 
A 1 4   CYS 4   1   1   CYS CYS A . n 
A 1 5   ASP 5   2   2   ASP ASP A . n 
A 1 6   ALA 6   3   3   ALA ALA A . n 
A 1 7   PHE 7   4   4   PHE PHE A . n 
A 1 8   VAL 8   5   5   VAL VAL A . n 
A 1 9   GLY 9   6   6   GLY GLY A . n 
A 1 10  THR 10  7   7   THR THR A . n 
A 1 11  TRP 11  8   8   TRP TRP A . n 
A 1 12  LYS 12  9   9   LYS LYS A . n 
A 1 13  LEU 13  10  10  LEU LEU A . n 
A 1 14  VAL 14  11  11  VAL VAL A . n 
A 1 15  SER 15  12  12  SER SER A . n 
A 1 16  SER 16  13  13  SER SER A . n 
A 1 17  GLU 17  14  14  GLU GLU A . n 
A 1 18  ASN 18  15  15  ASN ASN A . n 
A 1 19  PHE 19  16  16  PHE PHE A . n 
A 1 20  ASP 20  17  17  ASP ASP A . n 
A 1 21  ASP 21  18  18  ASP ASP A . n 
A 1 22  TYR 22  19  19  TYR TYR A . n 
A 1 23  MET 23  20  20  MET MET A . n 
A 1 24  LYS 24  21  21  LYS LYS A . n 
A 1 25  GLU 25  22  22  GLU GLU A . n 
A 1 26  VAL 26  23  23  VAL VAL A . n 
A 1 27  GLY 27  24  24  GLY GLY A . n 
A 1 28  VAL 28  25  25  VAL VAL A . n 
A 1 29  GLY 29  26  26  GLY GLY A . n 
A 1 30  PHE 30  27  27  PHE PHE A . n 
A 1 31  ALA 31  28  28  ALA ALA A . n 
A 1 32  THR 32  29  29  THR THR A . n 
A 1 33  ARG 33  30  30  ARG ARG A . n 
A 1 34  LYS 34  31  31  LYS LYS A . n 
A 1 35  VAL 35  32  32  VAL VAL A . n 
A 1 36  ALA 36  33  33  ALA ALA A . n 
A 1 37  GLY 37  34  34  GLY GLY A . n 
A 1 38  MET 38  35  35  MET MET A . n 
A 1 39  ALA 39  36  36  ALA ALA A . n 
A 1 40  LYS 40  37  37  LYS LYS A . n 
A 1 41  PRO 41  38  38  PRO PRO A . n 
A 1 42  ASN 42  39  39  ASN ASN A . n 
A 1 43  MET 43  40  40  MET MET A . n 
A 1 44  ILE 44  41  41  ILE ILE A . n 
A 1 45  ILE 45  42  42  ILE ILE A . n 
A 1 46  SER 46  43  43  SER SER A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  ASN 48  45  45  ASN ASN A . n 
A 1 49  GLY 49  46  46  GLY GLY A . n 
A 1 50  ASP 50  47  47  ASP ASP A . n 
A 1 51  VAL 51  48  48  VAL VAL A . n 
A 1 52  ILE 52  49  49  ILE ILE A . n 
A 1 53  THR 53  50  50  THR THR A . n 
A 1 54  ILE 54  51  51  ILE ILE A . n 
A 1 55  LYS 55  52  52  LYS LYS A . n 
A 1 56  SER 56  53  53  SER SER A . n 
A 1 57  GLU 57  54  54  GLU GLU A . n 
A 1 58  SER 58  55  55  SER SER A . n 
A 1 59  THR 59  56  56  THR THR A . n 
A 1 60  PHE 60  57  57  PHE PHE A . n 
A 1 61  LYS 61  58  58  LYS LYS A . n 
A 1 62  ASN 62  59  59  ASN ASN A . n 
A 1 63  THR 63  60  60  THR THR A . n 
A 1 64  GLU 64  61  61  GLU GLU A . n 
A 1 65  ILE 65  62  62  ILE ILE A . n 
A 1 66  SER 66  63  63  SER SER A . n 
A 1 67  PHE 67  64  64  PHE PHE A . n 
A 1 68  ILE 68  65  65  ILE ILE A . n 
A 1 69  LEU 69  66  66  LEU LEU A . n 
A 1 70  GLY 70  67  67  GLY GLY A . n 
A 1 71  GLN 71  68  68  GLN GLN A . n 
A 1 72  GLU 72  69  69  GLU GLU A . n 
A 1 73  PHE 73  70  70  PHE PHE A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  GLU 75  72  72  GLU GLU A . n 
A 1 76  VAL 76  73  73  VAL VAL A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  ALA 78  75  75  ALA ALA A . n 
A 1 79  ASP 79  76  76  ASP ASP A . n 
A 1 80  ASP 80  77  77  ASP ASP A . n 
A 1 81  ARG 81  78  78  ARG ARG A . n 
A 1 82  LYS 82  79  79  LYS LYS A . n 
A 1 83  VAL 83  80  80  VAL VAL A . n 
A 1 84  LYS 84  81  81  LYS LYS A . n 
A 1 85  SER 85  82  82  SER SER A . n 
A 1 86  THR 86  83  83  THR THR A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  THR 88  85  85  THR THR A . n 
A 1 89  LEU 89  86  86  LEU LEU A . n 
A 1 90  ASP 90  87  87  ASP ASP A . n 
A 1 91  GLY 91  88  88  GLY GLY A . n 
A 1 92  GLY 92  89  89  GLY GLY A . n 
A 1 93  VAL 93  90  90  VAL VAL A . n 
A 1 94  LEU 94  91  91  LEU LEU A . n 
A 1 95  VAL 95  92  92  VAL VAL A . n 
A 1 96  HIS 96  93  93  HIS HIS A . n 
A 1 97  VAL 97  94  94  VAL VAL A . n 
A 1 98  GLN 98  95  95  GLN GLN A . n 
A 1 99  LYS 99  96  96  LYS LYS A . n 
A 1 100 TRP 100 97  97  TRP TRP A . n 
A 1 101 ASP 101 98  98  ASP ASP A . n 
A 1 102 GLY 102 99  99  GLY GLY A . n 
A 1 103 LYS 103 100 100 LYS LYS A . n 
A 1 104 SER 104 101 101 SER SER A . n 
A 1 105 THR 105 102 102 THR THR A . n 
A 1 106 THR 106 103 103 THR THR A . n 
A 1 107 ILE 107 104 104 ILE ILE A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 ARG 109 106 106 ARG ARG A . n 
A 1 110 LYS 110 107 107 LYS LYS A . n 
A 1 111 ARG 111 108 108 ARG ARG A . n 
A 1 112 GLU 112 109 109 GLU GLU A . n 
A 1 113 ASP 113 110 110 ASP ASP A . n 
A 1 114 ASP 114 111 111 ASP ASP A . n 
A 1 115 LYS 115 112 112 LYS LYS A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 VAL 118 115 115 VAL VAL A . n 
A 1 119 GLU 119 116 116 GLU GLU A . n 
A 1 120 CYS 120 117 117 CYS CYS A . n 
A 1 121 VAL 121 118 118 VAL VAL A . n 
A 1 122 MET 122 119 119 MET MET A . n 
A 1 123 LYS 123 120 120 LYS LYS A . n 
A 1 124 GLY 124 121 121 GLY GLY A . n 
A 1 125 VAL 125 122 122 VAL VAL A . n 
A 1 126 THR 126 123 123 THR THR A . n 
A 1 127 SER 127 124 124 SER SER A . n 
A 1 128 THR 128 125 125 THR THR A . n 
A 1 129 ARG 129 126 126 ARG ARG A . n 
A 1 130 VAL 130 127 127 VAL VAL A . n 
A 1 131 TYR 131 128 128 TYR TYR A . n 
A 1 132 GLU 132 129 129 GLU GLU A . n 
A 1 133 ARG 133 130 130 ARG ARG A . n 
A 1 134 ALA 134 131 131 ALA ALA A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BLY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BLY 
_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 A1BLY 1   201 135 A1BLY 9PF A . 
C 3 HOH   1   301 177 HOH   HOH A . 
C 3 HOH   2   302 162 HOH   HOH A . 
C 3 HOH   3   303 109 HOH   HOH A . 
C 3 HOH   4   304 172 HOH   HOH A . 
C 3 HOH   5   305 126 HOH   HOH A . 
C 3 HOH   6   306 116 HOH   HOH A . 
C 3 HOH   7   307 214 HOH   HOH A . 
C 3 HOH   8   308 211 HOH   HOH A . 
C 3 HOH   9   309 190 HOH   HOH A . 
C 3 HOH   10  310 161 HOH   HOH A . 
C 3 HOH   11  311 79  HOH   HOH A . 
C 3 HOH   12  312 173 HOH   HOH A . 
C 3 HOH   13  313 50  HOH   HOH A . 
C 3 HOH   14  314 145 HOH   HOH A . 
C 3 HOH   15  315 148 HOH   HOH A . 
C 3 HOH   16  316 122 HOH   HOH A . 
C 3 HOH   17  317 207 HOH   HOH A . 
C 3 HOH   18  318 144 HOH   HOH A . 
C 3 HOH   19  319 80  HOH   HOH A . 
C 3 HOH   20  320 45  HOH   HOH A . 
C 3 HOH   21  321 43  HOH   HOH A . 
C 3 HOH   22  322 137 HOH   HOH A . 
C 3 HOH   23  323 142 HOH   HOH A . 
C 3 HOH   24  324 97  HOH   HOH A . 
C 3 HOH   25  325 93  HOH   HOH A . 
C 3 HOH   26  326 55  HOH   HOH A . 
C 3 HOH   27  327 140 HOH   HOH A . 
C 3 HOH   28  328 160 HOH   HOH A . 
C 3 HOH   29  329 178 HOH   HOH A . 
C 3 HOH   30  330 68  HOH   HOH A . 
C 3 HOH   31  331 127 HOH   HOH A . 
C 3 HOH   32  332 51  HOH   HOH A . 
C 3 HOH   33  333 81  HOH   HOH A . 
C 3 HOH   34  334 181 HOH   HOH A . 
C 3 HOH   35  335 64  HOH   HOH A . 
C 3 HOH   36  336 36  HOH   HOH A . 
C 3 HOH   37  337 6   HOH   HOH A . 
C 3 HOH   38  338 38  HOH   HOH A . 
C 3 HOH   39  339 204 HOH   HOH A . 
C 3 HOH   40  340 29  HOH   HOH A . 
C 3 HOH   41  341 24  HOH   HOH A . 
C 3 HOH   42  342 95  HOH   HOH A . 
C 3 HOH   43  343 14  HOH   HOH A . 
C 3 HOH   44  344 54  HOH   HOH A . 
C 3 HOH   45  345 182 HOH   HOH A . 
C 3 HOH   46  346 69  HOH   HOH A . 
C 3 HOH   47  347 75  HOH   HOH A . 
C 3 HOH   48  348 15  HOH   HOH A . 
C 3 HOH   49  349 205 HOH   HOH A . 
C 3 HOH   50  350 125 HOH   HOH A . 
C 3 HOH   51  351 169 HOH   HOH A . 
C 3 HOH   52  352 28  HOH   HOH A . 
C 3 HOH   53  353 113 HOH   HOH A . 
C 3 HOH   54  354 158 HOH   HOH A . 
C 3 HOH   55  355 196 HOH   HOH A . 
C 3 HOH   56  356 7   HOH   HOH A . 
C 3 HOH   57  357 65  HOH   HOH A . 
C 3 HOH   58  358 62  HOH   HOH A . 
C 3 HOH   59  359 94  HOH   HOH A . 
C 3 HOH   60  360 8   HOH   HOH A . 
C 3 HOH   61  361 49  HOH   HOH A . 
C 3 HOH   62  362 130 HOH   HOH A . 
C 3 HOH   63  363 53  HOH   HOH A . 
C 3 HOH   64  364 85  HOH   HOH A . 
C 3 HOH   65  365 90  HOH   HOH A . 
C 3 HOH   66  366 73  HOH   HOH A . 
C 3 HOH   67  367 10  HOH   HOH A . 
C 3 HOH   68  368 189 HOH   HOH A . 
C 3 HOH   69  369 19  HOH   HOH A . 
C 3 HOH   70  370 40  HOH   HOH A . 
C 3 HOH   71  371 174 HOH   HOH A . 
C 3 HOH   72  372 23  HOH   HOH A . 
C 3 HOH   73  373 4   HOH   HOH A . 
C 3 HOH   74  374 18  HOH   HOH A . 
C 3 HOH   75  375 59  HOH   HOH A . 
C 3 HOH   76  376 180 HOH   HOH A . 
C 3 HOH   77  377 3   HOH   HOH A . 
C 3 HOH   78  378 1   HOH   HOH A . 
C 3 HOH   79  379 185 HOH   HOH A . 
C 3 HOH   80  380 186 HOH   HOH A . 
C 3 HOH   81  381 39  HOH   HOH A . 
C 3 HOH   82  382 2   HOH   HOH A . 
C 3 HOH   83  383 103 HOH   HOH A . 
C 3 HOH   84  384 33  HOH   HOH A . 
C 3 HOH   85  385 21  HOH   HOH A . 
C 3 HOH   86  386 27  HOH   HOH A . 
C 3 HOH   87  387 52  HOH   HOH A . 
C 3 HOH   88  388 143 HOH   HOH A . 
C 3 HOH   89  389 119 HOH   HOH A . 
C 3 HOH   90  390 35  HOH   HOH A . 
C 3 HOH   91  391 11  HOH   HOH A . 
C 3 HOH   92  392 120 HOH   HOH A . 
C 3 HOH   93  393 12  HOH   HOH A . 
C 3 HOH   94  394 188 HOH   HOH A . 
C 3 HOH   95  395 104 HOH   HOH A . 
C 3 HOH   96  396 166 HOH   HOH A . 
C 3 HOH   97  397 98  HOH   HOH A . 
C 3 HOH   98  398 31  HOH   HOH A . 
C 3 HOH   99  399 84  HOH   HOH A . 
C 3 HOH   100 400 37  HOH   HOH A . 
C 3 HOH   101 401 118 HOH   HOH A . 
C 3 HOH   102 402 22  HOH   HOH A . 
C 3 HOH   103 403 121 HOH   HOH A . 
C 3 HOH   104 404 25  HOH   HOH A . 
C 3 HOH   105 405 20  HOH   HOH A . 
C 3 HOH   106 406 179 HOH   HOH A . 
C 3 HOH   107 407 107 HOH   HOH A . 
C 3 HOH   108 408 87  HOH   HOH A . 
C 3 HOH   109 409 92  HOH   HOH A . 
C 3 HOH   110 410 152 HOH   HOH A . 
C 3 HOH   111 411 129 HOH   HOH A . 
C 3 HOH   112 412 210 HOH   HOH A . 
C 3 HOH   113 413 96  HOH   HOH A . 
C 3 HOH   114 414 105 HOH   HOH A . 
C 3 HOH   115 415 70  HOH   HOH A . 
C 3 HOH   116 416 171 HOH   HOH A . 
C 3 HOH   117 417 9   HOH   HOH A . 
C 3 HOH   118 418 5   HOH   HOH A . 
C 3 HOH   119 419 42  HOH   HOH A . 
C 3 HOH   120 420 111 HOH   HOH A . 
C 3 HOH   121 421 30  HOH   HOH A . 
C 3 HOH   122 422 17  HOH   HOH A . 
C 3 HOH   123 423 46  HOH   HOH A . 
C 3 HOH   124 424 100 HOH   HOH A . 
C 3 HOH   125 425 58  HOH   HOH A . 
C 3 HOH   126 426 72  HOH   HOH A . 
C 3 HOH   127 427 184 HOH   HOH A . 
C 3 HOH   128 428 198 HOH   HOH A . 
C 3 HOH   129 429 183 HOH   HOH A . 
C 3 HOH   130 430 66  HOH   HOH A . 
C 3 HOH   131 431 57  HOH   HOH A . 
C 3 HOH   132 432 170 HOH   HOH A . 
C 3 HOH   133 433 195 HOH   HOH A . 
C 3 HOH   134 434 61  HOH   HOH A . 
C 3 HOH   135 435 44  HOH   HOH A . 
C 3 HOH   136 436 67  HOH   HOH A . 
C 3 HOH   137 437 60  HOH   HOH A . 
C 3 HOH   138 438 168 HOH   HOH A . 
C 3 HOH   139 439 83  HOH   HOH A . 
C 3 HOH   140 440 163 HOH   HOH A . 
C 3 HOH   141 441 74  HOH   HOH A . 
C 3 HOH   142 442 77  HOH   HOH A . 
C 3 HOH   143 443 63  HOH   HOH A . 
C 3 HOH   144 444 106 HOH   HOH A . 
C 3 HOH   145 445 201 HOH   HOH A . 
C 3 HOH   146 446 41  HOH   HOH A . 
C 3 HOH   147 447 102 HOH   HOH A . 
C 3 HOH   148 448 153 HOH   HOH A . 
C 3 HOH   149 449 132 HOH   HOH A . 
C 3 HOH   150 450 13  HOH   HOH A . 
C 3 HOH   151 451 193 HOH   HOH A . 
C 3 HOH   152 452 199 HOH   HOH A . 
C 3 HOH   153 453 48  HOH   HOH A . 
C 3 HOH   154 454 108 HOH   HOH A . 
C 3 HOH   155 455 175 HOH   HOH A . 
C 3 HOH   156 456 151 HOH   HOH A . 
C 3 HOH   157 457 71  HOH   HOH A . 
C 3 HOH   158 458 147 HOH   HOH A . 
C 3 HOH   159 459 138 HOH   HOH A . 
C 3 HOH   160 460 209 HOH   HOH A . 
C 3 HOH   161 461 197 HOH   HOH A . 
C 3 HOH   162 462 149 HOH   HOH A . 
C 3 HOH   163 463 202 HOH   HOH A . 
C 3 HOH   164 464 135 HOH   HOH A . 
C 3 HOH   165 465 89  HOH   HOH A . 
C 3 HOH   166 466 128 HOH   HOH A . 
C 3 HOH   167 467 47  HOH   HOH A . 
C 3 HOH   168 468 82  HOH   HOH A . 
C 3 HOH   169 469 154 HOH   HOH A . 
C 3 HOH   170 470 206 HOH   HOH A . 
C 3 HOH   171 471 16  HOH   HOH A . 
C 3 HOH   172 472 123 HOH   HOH A . 
C 3 HOH   173 473 131 HOH   HOH A . 
C 3 HOH   174 474 117 HOH   HOH A . 
C 3 HOH   175 475 34  HOH   HOH A . 
C 3 HOH   176 476 146 HOH   HOH A . 
C 3 HOH   177 477 88  HOH   HOH A . 
C 3 HOH   178 478 136 HOH   HOH A . 
C 3 HOH   179 479 150 HOH   HOH A . 
C 3 HOH   180 480 99  HOH   HOH A . 
C 3 HOH   181 481 134 HOH   HOH A . 
C 3 HOH   182 482 26  HOH   HOH A . 
C 3 HOH   183 483 141 HOH   HOH A . 
C 3 HOH   184 484 114 HOH   HOH A . 
C 3 HOH   185 485 157 HOH   HOH A . 
C 3 HOH   186 486 187 HOH   HOH A . 
C 3 HOH   187 487 86  HOH   HOH A . 
C 3 HOH   188 488 200 HOH   HOH A . 
C 3 HOH   189 489 156 HOH   HOH A . 
C 3 HOH   190 490 167 HOH   HOH A . 
C 3 HOH   191 491 155 HOH   HOH A . 
C 3 HOH   192 492 139 HOH   HOH A . 
C 3 HOH   193 493 76  HOH   HOH A . 
C 3 HOH   194 494 56  HOH   HOH A . 
C 3 HOH   195 495 110 HOH   HOH A . 
C 3 HOH   196 496 78  HOH   HOH A . 
C 3 HOH   197 497 112 HOH   HOH A . 
C 3 HOH   198 498 115 HOH   HOH A . 
C 3 HOH   199 499 191 HOH   HOH A . 
C 3 HOH   200 500 101 HOH   HOH A . 
C 3 HOH   201 501 165 HOH   HOH A . 
C 3 HOH   202 502 176 HOH   HOH A . 
C 3 HOH   203 503 194 HOH   HOH A . 
C 3 HOH   204 504 213 HOH   HOH A . 
C 3 HOH   205 505 203 HOH   HOH A . 
C 3 HOH   206 506 91  HOH   HOH A . 
C 3 HOH   207 507 124 HOH   HOH A . 
C 3 HOH   208 508 192 HOH   HOH A . 
C 3 HOH   209 509 32  HOH   HOH A . 
C 3 HOH   210 510 212 HOH   HOH A . 
C 3 HOH   211 511 164 HOH   HOH A . 
C 3 HOH   212 512 159 HOH   HOH A . 
C 3 HOH   213 513 133 HOH   HOH A . 
C 3 HOH   214 514 208 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   92.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MIZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.746 
_cell.length_a_esd                 ? 
_cell.length_b                     37.709 
_cell.length_b_esd                 ? 
_cell.length_c                     28.490 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MIZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9MIZ 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.35 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '1.55-1.6 M sodium citrate' 
_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 EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MIZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               27.29 
_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                                     24826 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.090 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       222985 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.085 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6098 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1205 
_reflns_shell.percent_possible_obs                          95.9 
_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                               5.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               0.925 
_reflns_shell.pdbx_Rpim_I_all                               0.380 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.675 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.836 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_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                                 9MIZ 
_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                            1.40 
_refine.ls_d_res_low                             22.46 
_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                     24819 
_refine.ls_number_reflns_R_free                  1259 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.26 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1425 
_refine.ls_R_factor_R_free                       0.1974 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1396 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          1.36 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.36 
_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                             ? 
_refine.overall_SU_ML                            0.17 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        1044 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.number_atoms_solvent             214 
_refine_hist.number_atoms_total               1289 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        22.46 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 1137 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.950 ? 1557 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.776 ? 232  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.097 ? 174  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 193  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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.pdbx_total_number_of_bins_used 
_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 
'X-RAY DIFFRACTION' 1.40 1.46  . . 123 2520 96.00  . . . . 0.2049 . . . . . . . . . . . 0.2922 
'X-RAY DIFFRACTION' 1.46 1.52  . . 135 2597 98.00  . . . . 0.1757 . . . . . . . . . . . 0.2584 
'X-RAY DIFFRACTION' 1.52 1.60  . . 143 2581 99.00  . . . . 0.1509 . . . . . . . . . . . 0.2287 
'X-RAY DIFFRACTION' 1.60 1.70  . . 129 2623 100.00 . . . . 0.1445 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 1.70 1.83  . . 157 2616 100.00 . . . . 0.1393 . . . . . . . . . . . 0.2299 
'X-RAY DIFFRACTION' 1.83 2.02  . . 135 2629 100.00 . . . . 0.1242 . . . . . . . . . . . 0.1747 
'X-RAY DIFFRACTION' 2.02 2.31  . . 145 2634 100.00 . . . . 0.1264 . . . . . . . . . . . 0.1759 
'X-RAY DIFFRACTION' 2.31 2.91  . . 157 2638 100.00 . . . . 0.1440 . . . . . . . . . . . 0.2049 
'X-RAY DIFFRACTION' 2.91 22.46 . . 135 2722 100.00 . . . . 0.1326 . . . . . . . . . . . 0.1733 
# 
_struct.entry_id                     9MIZ 
_struct.title                        'Fatty Acid Binding Protein 4 (FABP4) Complexed with Perfluorodecanoic Acid (PFDA)' 
_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        9MIZ 
_struct_keywords.text            'PFAS, hydrophobic, beta-barrel, adipocyte, LIPID BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'LIPID BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FABP4_HUMAN 
_struct_ref.pdbx_db_accession          P15090 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRK
VKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA
;
_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              9MIZ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 134 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P15090 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  132 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       131 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9MIZ GLY A 1 ? UNP P15090 ? ? 'expression tag' -2 1 
1 9MIZ HIS A 2 ? UNP P15090 ? ? 'expression tag' -1 2 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0    ? 
1 MORE         0    ? 
1 'SSA (A^2)'  7270 ? 
# 
_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 ASN A 18 ? GLY A 27 ? ASN A 15 GLY A 24 1 ? 10 
HELX_P HELX_P2 AA2 GLY A 29 ? ALA A 39 ? GLY A 26 ALA A 36 1 ? 11 
# 
_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   10 
_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  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  THR A 63  ? PHE A 67  ? THR A 60  PHE A 64  
AA1 2  VAL A 51  ? GLU A 57  ? VAL A 48  GLU A 54  
AA1 3  ASN A 42  ? ASN A 48  ? ASN A 39  ASN A 45  
AA1 4  GLY A 9   ? GLU A 17  ? GLY A 6   GLU A 14  
AA1 5  VAL A 125 ? ARG A 133 ? VAL A 122 ARG A 130 
AA1 6  LYS A 115 ? MET A 122 ? LYS A 112 MET A 119 
AA1 7  LYS A 103 ? GLU A 112 ? LYS A 100 GLU A 109 
AA1 8  VAL A 93  ? TRP A 100 ? VAL A 90  TRP A 97  
AA1 9  LYS A 82  ? ASP A 90  ? LYS A 79  ASP A 87  
AA1 10 PHE A 73  ? VAL A 76  ? PHE A 70  VAL A 73  
# 
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 PHE A 67  ? O PHE A 64  N ILE A 52  ? N ILE A 49  
AA1 2 3  O LYS A 55  ? O LYS A 52  N ILE A 44  ? N ILE A 41  
AA1 3 4  O MET A 43  ? O MET A 40  N TRP A 11  ? N TRP A 8   
AA1 4 5  N VAL A 14  ? N VAL A 11  O VAL A 130 ? O VAL A 127 
AA1 5 6  O ARG A 129 ? O ARG A 126 N VAL A 118 ? N VAL A 115 
AA1 6 7  O GLU A 119 ? O GLU A 116 N LYS A 108 ? N LYS A 105 
AA1 7 8  O ILE A 107 ? O ILE A 104 N HIS A 96  ? N HIS A 93  
AA1 8 9  O VAL A 95  ? O VAL A 92  N THR A 88  ? N THR A 85  
AA1 9 10 O SER A 85  ? O SER A 82  N PHE A 73  ? N PHE A 70  
# 
_pdbx_entry_details.entry_id                   9MIZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 307 ? ? O A HOH 446 ? ? 2.14 
2 1 O A HOH 424 ? ? O A HOH 503 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NZ A LYS 21  ? ? 1_555 NZ A LYS 21  ? ? 2_556 1.44 
2 1 CD A LYS 21  ? ? 1_555 CD A LYS 21  ? ? 2_556 1.48 
3 1 CE A LYS 21  ? ? 1_555 NZ A LYS 21  ? ? 2_556 1.50 
4 1 CD A LYS 21  ? ? 1_555 CE A LYS 21  ? ? 2_556 1.52 
5 1 O  A HOH 339 ? ? 1_555 O  A HOH 349 ? ? 1_565 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 37  ? ? -114.09 79.70   
2 1 ASP A 77  ? A 73.75   30.28   
3 1 ASP A 110 ? ? 53.88   -129.49 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    LYS 
_pdbx_struct_special_symmetry.auth_seq_id     21 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   A 
_pdbx_struct_special_symmetry.label_comp_id   LYS 
_pdbx_struct_special_symmetry.label_seq_id    24 
# 
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 
A1BLY C1   C N N 1   
A1BLY C10  C N N 2   
A1BLY C2   C N N 3   
A1BLY C3   C N N 4   
A1BLY C4   C N N 5   
A1BLY C5   C N N 6   
A1BLY C6   C N N 7   
A1BLY C7   C N N 8   
A1BLY C8   C N N 9   
A1BLY C9   C N N 10  
A1BLY F1   F N N 11  
A1BLY F10  F N N 12  
A1BLY F11  F N N 13  
A1BLY F12  F N N 14  
A1BLY F13  F N N 15  
A1BLY F14  F N N 16  
A1BLY F15  F N N 17  
A1BLY F16  F N N 18  
A1BLY F17  F N N 19  
A1BLY F18  F N N 20  
A1BLY F19  F N N 21  
A1BLY F2   F N N 22  
A1BLY F3   F N N 23  
A1BLY F4   F N N 24  
A1BLY F5   F N N 25  
A1BLY F6   F N N 26  
A1BLY F7   F N N 27  
A1BLY F8   F N N 28  
A1BLY F9   F N N 29  
A1BLY O1   O N N 30  
A1BLY O2   O N N 31  
A1BLY H1   H N N 32  
ALA   N    N N N 33  
ALA   CA   C N S 34  
ALA   C    C N N 35  
ALA   O    O N N 36  
ALA   CB   C N N 37  
ALA   OXT  O N N 38  
ALA   H    H N N 39  
ALA   H2   H N N 40  
ALA   HA   H N N 41  
ALA   HB1  H N N 42  
ALA   HB2  H N N 43  
ALA   HB3  H N N 44  
ALA   HXT  H N N 45  
ARG   N    N N N 46  
ARG   CA   C N S 47  
ARG   C    C N N 48  
ARG   O    O N N 49  
ARG   CB   C N N 50  
ARG   CG   C N N 51  
ARG   CD   C N N 52  
ARG   NE   N N N 53  
ARG   CZ   C N N 54  
ARG   NH1  N N N 55  
ARG   NH2  N N N 56  
ARG   OXT  O N N 57  
ARG   H    H N N 58  
ARG   H2   H N N 59  
ARG   HA   H N N 60  
ARG   HB2  H N N 61  
ARG   HB3  H N N 62  
ARG   HG2  H N N 63  
ARG   HG3  H N N 64  
ARG   HD2  H N N 65  
ARG   HD3  H N N 66  
ARG   HE   H N N 67  
ARG   HH11 H N N 68  
ARG   HH12 H N N 69  
ARG   HH21 H N N 70  
ARG   HH22 H N N 71  
ARG   HXT  H N N 72  
ASN   N    N N N 73  
ASN   CA   C N S 74  
ASN   C    C N N 75  
ASN   O    O N N 76  
ASN   CB   C N N 77  
ASN   CG   C N N 78  
ASN   OD1  O N N 79  
ASN   ND2  N N N 80  
ASN   OXT  O N N 81  
ASN   H    H N N 82  
ASN   H2   H N N 83  
ASN   HA   H N N 84  
ASN   HB2  H N N 85  
ASN   HB3  H N N 86  
ASN   HD21 H N N 87  
ASN   HD22 H N N 88  
ASN   HXT  H N N 89  
ASP   N    N N N 90  
ASP   CA   C N S 91  
ASP   C    C N N 92  
ASP   O    O N N 93  
ASP   CB   C N N 94  
ASP   CG   C N N 95  
ASP   OD1  O N N 96  
ASP   OD2  O N N 97  
ASP   OXT  O N N 98  
ASP   H    H N N 99  
ASP   H2   H N N 100 
ASP   HA   H N N 101 
ASP   HB2  H N N 102 
ASP   HB3  H N N 103 
ASP   HD2  H N N 104 
ASP   HXT  H N N 105 
CYS   N    N N N 106 
CYS   CA   C N R 107 
CYS   C    C N N 108 
CYS   O    O N N 109 
CYS   CB   C N N 110 
CYS   SG   S N N 111 
CYS   OXT  O N N 112 
CYS   H    H N N 113 
CYS   H2   H N N 114 
CYS   HA   H N N 115 
CYS   HB2  H N N 116 
CYS   HB3  H N N 117 
CYS   HG   H N N 118 
CYS   HXT  H N N 119 
GLN   N    N N N 120 
GLN   CA   C N S 121 
GLN   C    C N N 122 
GLN   O    O N N 123 
GLN   CB   C N N 124 
GLN   CG   C N N 125 
GLN   CD   C N N 126 
GLN   OE1  O N N 127 
GLN   NE2  N N N 128 
GLN   OXT  O N N 129 
GLN   H    H N N 130 
GLN   H2   H N N 131 
GLN   HA   H N N 132 
GLN   HB2  H N N 133 
GLN   HB3  H N N 134 
GLN   HG2  H N N 135 
GLN   HG3  H N N 136 
GLN   HE21 H N N 137 
GLN   HE22 H N N 138 
GLN   HXT  H N N 139 
GLU   N    N N N 140 
GLU   CA   C N S 141 
GLU   C    C N N 142 
GLU   O    O N N 143 
GLU   CB   C N N 144 
GLU   CG   C N N 145 
GLU   CD   C N N 146 
GLU   OE1  O N N 147 
GLU   OE2  O N N 148 
GLU   OXT  O N N 149 
GLU   H    H N N 150 
GLU   H2   H N N 151 
GLU   HA   H N N 152 
GLU   HB2  H N N 153 
GLU   HB3  H N N 154 
GLU   HG2  H N N 155 
GLU   HG3  H N N 156 
GLU   HE2  H N N 157 
GLU   HXT  H N N 158 
GLY   N    N N N 159 
GLY   CA   C N N 160 
GLY   C    C N N 161 
GLY   O    O N N 162 
GLY   OXT  O N N 163 
GLY   H    H N N 164 
GLY   H2   H N N 165 
GLY   HA2  H N N 166 
GLY   HA3  H N N 167 
GLY   HXT  H N N 168 
HIS   N    N N N 169 
HIS   CA   C N S 170 
HIS   C    C N N 171 
HIS   O    O N N 172 
HIS   CB   C N N 173 
HIS   CG   C Y N 174 
HIS   ND1  N Y N 175 
HIS   CD2  C Y N 176 
HIS   CE1  C Y N 177 
HIS   NE2  N Y N 178 
HIS   OXT  O N N 179 
HIS   H    H N N 180 
HIS   H2   H N N 181 
HIS   HA   H N N 182 
HIS   HB2  H N N 183 
HIS   HB3  H N N 184 
HIS   HD1  H N N 185 
HIS   HD2  H N N 186 
HIS   HE1  H N N 187 
HIS   HE2  H N N 188 
HIS   HXT  H N N 189 
HOH   O    O N N 190 
HOH   H1   H N N 191 
HOH   H2   H N N 192 
ILE   N    N N N 193 
ILE   CA   C N S 194 
ILE   C    C N N 195 
ILE   O    O N N 196 
ILE   CB   C N S 197 
ILE   CG1  C N N 198 
ILE   CG2  C N N 199 
ILE   CD1  C N N 200 
ILE   OXT  O N N 201 
ILE   H    H N N 202 
ILE   H2   H N N 203 
ILE   HA   H N N 204 
ILE   HB   H N N 205 
ILE   HG12 H N N 206 
ILE   HG13 H N N 207 
ILE   HG21 H N N 208 
ILE   HG22 H N N 209 
ILE   HG23 H N N 210 
ILE   HD11 H N N 211 
ILE   HD12 H N N 212 
ILE   HD13 H N N 213 
ILE   HXT  H N N 214 
LEU   N    N N N 215 
LEU   CA   C N S 216 
LEU   C    C N N 217 
LEU   O    O N N 218 
LEU   CB   C N N 219 
LEU   CG   C N N 220 
LEU   CD1  C N N 221 
LEU   CD2  C N N 222 
LEU   OXT  O N N 223 
LEU   H    H N N 224 
LEU   H2   H N N 225 
LEU   HA   H N N 226 
LEU   HB2  H N N 227 
LEU   HB3  H N N 228 
LEU   HG   H N N 229 
LEU   HD11 H N N 230 
LEU   HD12 H N N 231 
LEU   HD13 H N N 232 
LEU   HD21 H N N 233 
LEU   HD22 H N N 234 
LEU   HD23 H N N 235 
LEU   HXT  H N N 236 
LYS   N    N N N 237 
LYS   CA   C N S 238 
LYS   C    C N N 239 
LYS   O    O N N 240 
LYS   CB   C N N 241 
LYS   CG   C N N 242 
LYS   CD   C N N 243 
LYS   CE   C N N 244 
LYS   NZ   N N N 245 
LYS   OXT  O N N 246 
LYS   H    H N N 247 
LYS   H2   H N N 248 
LYS   HA   H N N 249 
LYS   HB2  H N N 250 
LYS   HB3  H N N 251 
LYS   HG2  H N N 252 
LYS   HG3  H N N 253 
LYS   HD2  H N N 254 
LYS   HD3  H N N 255 
LYS   HE2  H N N 256 
LYS   HE3  H N N 257 
LYS   HZ1  H N N 258 
LYS   HZ2  H N N 259 
LYS   HZ3  H N N 260 
LYS   HXT  H N N 261 
MET   N    N N N 262 
MET   CA   C N S 263 
MET   C    C N N 264 
MET   O    O N N 265 
MET   CB   C N N 266 
MET   CG   C N N 267 
MET   SD   S N N 268 
MET   CE   C N N 269 
MET   OXT  O N N 270 
MET   H    H N N 271 
MET   H2   H N N 272 
MET   HA   H N N 273 
MET   HB2  H N N 274 
MET   HB3  H N N 275 
MET   HG2  H N N 276 
MET   HG3  H N N 277 
MET   HE1  H N N 278 
MET   HE2  H N N 279 
MET   HE3  H N N 280 
MET   HXT  H N N 281 
PHE   N    N N N 282 
PHE   CA   C N S 283 
PHE   C    C N N 284 
PHE   O    O N N 285 
PHE   CB   C N N 286 
PHE   CG   C Y N 287 
PHE   CD1  C Y N 288 
PHE   CD2  C Y N 289 
PHE   CE1  C Y N 290 
PHE   CE2  C Y N 291 
PHE   CZ   C Y N 292 
PHE   OXT  O N N 293 
PHE   H    H N N 294 
PHE   H2   H N N 295 
PHE   HA   H N N 296 
PHE   HB2  H N N 297 
PHE   HB3  H N N 298 
PHE   HD1  H N N 299 
PHE   HD2  H N N 300 
PHE   HE1  H N N 301 
PHE   HE2  H N N 302 
PHE   HZ   H N N 303 
PHE   HXT  H N N 304 
PRO   N    N N N 305 
PRO   CA   C N S 306 
PRO   C    C N N 307 
PRO   O    O N N 308 
PRO   CB   C N N 309 
PRO   CG   C N N 310 
PRO   CD   C N N 311 
PRO   OXT  O N N 312 
PRO   H    H N N 313 
PRO   HA   H N N 314 
PRO   HB2  H N N 315 
PRO   HB3  H N N 316 
PRO   HG2  H N N 317 
PRO   HG3  H N N 318 
PRO   HD2  H N N 319 
PRO   HD3  H N N 320 
PRO   HXT  H N N 321 
SER   N    N N N 322 
SER   CA   C N S 323 
SER   C    C N N 324 
SER   O    O N N 325 
SER   CB   C N N 326 
SER   OG   O N N 327 
SER   OXT  O N N 328 
SER   H    H N N 329 
SER   H2   H N N 330 
SER   HA   H N N 331 
SER   HB2  H N N 332 
SER   HB3  H N N 333 
SER   HG   H N N 334 
SER   HXT  H N N 335 
THR   N    N N N 336 
THR   CA   C N S 337 
THR   C    C N N 338 
THR   O    O N N 339 
THR   CB   C N R 340 
THR   OG1  O N N 341 
THR   CG2  C N N 342 
THR   OXT  O N N 343 
THR   H    H N N 344 
THR   H2   H N N 345 
THR   HA   H N N 346 
THR   HB   H N N 347 
THR   HG1  H N N 348 
THR   HG21 H N N 349 
THR   HG22 H N N 350 
THR   HG23 H N N 351 
THR   HXT  H N N 352 
TRP   N    N N N 353 
TRP   CA   C N S 354 
TRP   C    C N N 355 
TRP   O    O N N 356 
TRP   CB   C N N 357 
TRP   CG   C Y N 358 
TRP   CD1  C Y N 359 
TRP   CD2  C Y N 360 
TRP   NE1  N Y N 361 
TRP   CE2  C Y N 362 
TRP   CE3  C Y N 363 
TRP   CZ2  C Y N 364 
TRP   CZ3  C Y N 365 
TRP   CH2  C Y N 366 
TRP   OXT  O N N 367 
TRP   H    H N N 368 
TRP   H2   H N N 369 
TRP   HA   H N N 370 
TRP   HB2  H N N 371 
TRP   HB3  H N N 372 
TRP   HD1  H N N 373 
TRP   HE1  H N N 374 
TRP   HE3  H N N 375 
TRP   HZ2  H N N 376 
TRP   HZ3  H N N 377 
TRP   HH2  H N N 378 
TRP   HXT  H N N 379 
TYR   N    N N N 380 
TYR   CA   C N S 381 
TYR   C    C N N 382 
TYR   O    O N N 383 
TYR   CB   C N N 384 
TYR   CG   C Y N 385 
TYR   CD1  C Y N 386 
TYR   CD2  C Y N 387 
TYR   CE1  C Y N 388 
TYR   CE2  C Y N 389 
TYR   CZ   C Y N 390 
TYR   OH   O N N 391 
TYR   OXT  O N N 392 
TYR   H    H N N 393 
TYR   H2   H N N 394 
TYR   HA   H N N 395 
TYR   HB2  H N N 396 
TYR   HB3  H N N 397 
TYR   HD1  H N N 398 
TYR   HD2  H N N 399 
TYR   HE1  H N N 400 
TYR   HE2  H N N 401 
TYR   HH   H N N 402 
TYR   HXT  H N N 403 
VAL   N    N N N 404 
VAL   CA   C N S 405 
VAL   C    C N N 406 
VAL   O    O N N 407 
VAL   CB   C N N 408 
VAL   CG1  C N N 409 
VAL   CG2  C N N 410 
VAL   OXT  O N N 411 
VAL   H    H N N 412 
VAL   H2   H N N 413 
VAL   HA   H N N 414 
VAL   HB   H N N 415 
VAL   HG11 H N N 416 
VAL   HG12 H N N 417 
VAL   HG13 H N N 418 
VAL   HG21 H N N 419 
VAL   HG22 H N N 420 
VAL   HG23 H N N 421 
VAL   HXT  H N N 422 
# 
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 
A1BLY F17 C10  sing N N 1   
A1BLY F19 C10  sing N N 2   
A1BLY F16 C9   sing N N 3   
A1BLY C10 F18  sing N N 4   
A1BLY C10 C9   sing N N 5   
A1BLY F14 C8   sing N N 6   
A1BLY C9  C8   sing N N 7   
A1BLY C9  F15  sing N N 8   
A1BLY F9  C6   sing N N 9   
A1BLY C8  F13  sing N N 10  
A1BLY C8  C7   sing N N 11  
A1BLY F3  C3   sing N N 12  
A1BLY F10 C6   sing N N 13  
A1BLY O1  C1   doub N N 14  
A1BLY C6  C7   sing N N 15  
A1BLY C6  C5   sing N N 16  
A1BLY F5  C4   sing N N 17  
A1BLY C7  F12  sing N N 18  
A1BLY C7  F11  sing N N 19  
A1BLY C1  O2   sing N N 20  
A1BLY C1  C2   sing N N 21  
A1BLY C3  C4   sing N N 22  
A1BLY C3  F4   sing N N 23  
A1BLY C3  C2   sing N N 24  
A1BLY C4  C5   sing N N 25  
A1BLY C4  F6   sing N N 26  
A1BLY C5  F8   sing N N 27  
A1BLY C5  F7   sing N N 28  
A1BLY C2  F2   sing N N 29  
A1BLY C2  F1   sing N N 30  
A1BLY O2  H1   sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
THR   N   CA   sing N N 321 
THR   N   H    sing N N 322 
THR   N   H2   sing N N 323 
THR   CA  C    sing N N 324 
THR   CA  CB   sing N N 325 
THR   CA  HA   sing N N 326 
THR   C   O    doub N N 327 
THR   C   OXT  sing N N 328 
THR   CB  OG1  sing N N 329 
THR   CB  CG2  sing N N 330 
THR   CB  HB   sing N N 331 
THR   OG1 HG1  sing N N 332 
THR   CG2 HG21 sing N N 333 
THR   CG2 HG22 sing N N 334 
THR   CG2 HG23 sing N N 335 
THR   OXT HXT  sing N N 336 
TRP   N   CA   sing N N 337 
TRP   N   H    sing N N 338 
TRP   N   H2   sing N N 339 
TRP   CA  C    sing N N 340 
TRP   CA  CB   sing N N 341 
TRP   CA  HA   sing N N 342 
TRP   C   O    doub N N 343 
TRP   C   OXT  sing N N 344 
TRP   CB  CG   sing N N 345 
TRP   CB  HB2  sing N N 346 
TRP   CB  HB3  sing N N 347 
TRP   CG  CD1  doub Y N 348 
TRP   CG  CD2  sing Y N 349 
TRP   CD1 NE1  sing Y N 350 
TRP   CD1 HD1  sing N N 351 
TRP   CD2 CE2  doub Y N 352 
TRP   CD2 CE3  sing Y N 353 
TRP   NE1 CE2  sing Y N 354 
TRP   NE1 HE1  sing N N 355 
TRP   CE2 CZ2  sing Y N 356 
TRP   CE3 CZ3  doub Y N 357 
TRP   CE3 HE3  sing N N 358 
TRP   CZ2 CH2  doub Y N 359 
TRP   CZ2 HZ2  sing N N 360 
TRP   CZ3 CH2  sing Y N 361 
TRP   CZ3 HZ3  sing N N 362 
TRP   CH2 HH2  sing N N 363 
TRP   OXT HXT  sing N N 364 
TYR   N   CA   sing N N 365 
TYR   N   H    sing N N 366 
TYR   N   H2   sing N N 367 
TYR   CA  C    sing N N 368 
TYR   CA  CB   sing N N 369 
TYR   CA  HA   sing N N 370 
TYR   C   O    doub N N 371 
TYR   C   OXT  sing N N 372 
TYR   CB  CG   sing N N 373 
TYR   CB  HB2  sing N N 374 
TYR   CB  HB3  sing N N 375 
TYR   CG  CD1  doub Y N 376 
TYR   CG  CD2  sing Y N 377 
TYR   CD1 CE1  sing Y N 378 
TYR   CD1 HD1  sing N N 379 
TYR   CD2 CE2  doub Y N 380 
TYR   CD2 HD2  sing N N 381 
TYR   CE1 CZ   doub Y N 382 
TYR   CE1 HE1  sing N N 383 
TYR   CE2 CZ   sing Y N 384 
TYR   CE2 HE2  sing N N 385 
TYR   CZ  OH   sing N N 386 
TYR   OH  HH   sing N N 387 
TYR   OXT HXT  sing N N 388 
VAL   N   CA   sing N N 389 
VAL   N   H    sing N N 390 
VAL   N   H2   sing N N 391 
VAL   CA  C    sing N N 392 
VAL   CA  CB   sing N N 393 
VAL   CA  HA   sing N N 394 
VAL   C   O    doub N N 395 
VAL   C   OXT  sing N N 396 
VAL   CB  CG1  sing N N 397 
VAL   CB  CG2  sing N N 398 
VAL   CB  HB   sing N N 399 
VAL   CG1 HG11 sing N N 400 
VAL   CG1 HG12 sing N N 401 
VAL   CG1 HG13 sing N N 402 
VAL   CG2 HG21 sing N N 403 
VAL   CG2 HG22 sing N N 404 
VAL   CG2 HG23 sing N N 405 
VAL   OXT HXT  sing N N 406 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R35 GM147221' 
_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   7WC3 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MIZ 
_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]   0.008421 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000368 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.026519 
_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]   0.035133 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY   A 1 1   ? 38.981 -13.818 5.497  1.00 46.93  ? -2  GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 1   ? 37.619 -14.016 5.039  1.00 42.96  ? -2  GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 1   ? 36.976 -15.264 5.615  1.00 39.50  ? -2  GLY   A C   1 
ATOM   4    O O   . GLY   A 1 1   ? 36.101 -15.872 4.991  1.00 41.11  ? -2  GLY   A O   1 
ATOM   5    N N   . HIS   A 1 2   ? 37.402 -15.643 6.820  1.00 36.43  ? -1  HIS   A N   1 
ATOM   6    C CA  . HIS   A 1 2   ? 36.897 -16.840 7.483  1.00 33.86  ? -1  HIS   A CA  1 
ATOM   7    C C   . HIS   A 1 2   ? 35.893 -16.537 8.590  1.00 25.70  ? -1  HIS   A C   1 
ATOM   8    O O   . HIS   A 1 2   ? 35.332 -17.476 9.166  1.00 24.36  ? -1  HIS   A O   1 
ATOM   9    C CB  . HIS   A 1 2   ? 38.065 -17.652 8.050  1.00 41.34  ? -1  HIS   A CB  1 
ATOM   10   C CG  . HIS   A 1 2   ? 38.936 -18.262 6.998  1.00 48.17  ? -1  HIS   A CG  1 
ATOM   11   N ND1 . HIS   A 1 2   ? 38.456 -19.148 6.058  1.00 50.85  ? -1  HIS   A ND1 1 
ATOM   12   C CD2 . HIS   A 1 2   ? 40.252 -18.097 6.724  1.00 51.72  ? -1  HIS   A CD2 1 
ATOM   13   C CE1 . HIS   A 1 2   ? 39.443 -19.513 5.258  1.00 52.52  ? -1  HIS   A CE1 1 
ATOM   14   N NE2 . HIS   A 1 2   ? 40.543 -18.889 5.640  1.00 52.76  ? -1  HIS   A NE2 1 
ATOM   15   N N   . MET   A 1 3   ? 35.656 -15.253 8.885  1.00 20.58  ? 0   MET   A N   1 
ATOM   16   C CA  . MET   A 1 3   ? 34.776 -14.838 9.978  1.00 20.50  ? 0   MET   A CA  1 
ATOM   17   C C   . MET   A 1 3   ? 33.423 -15.541 9.936  1.00 16.21  ? 0   MET   A C   1 
ATOM   18   O O   . MET   A 1 3   ? 32.836 -15.836 10.986 1.00 16.21  ? 0   MET   A O   1 
ATOM   19   C CB  . MET   A 1 3   ? 34.561 -13.321 9.870  1.00 20.21  ? 0   MET   A CB  1 
ATOM   20   C CG  . MET   A 1 3   ? 35.727 -12.427 10.330 1.00 20.22  ? 0   MET   A CG  1 
ATOM   21   S SD  . MET   A 1 3   ? 36.233 -12.591 12.052 1.00 16.24  ? 0   MET   A SD  1 
ATOM   22   C CE  . MET   A 1 3   ? 37.997 -12.309 11.947 1.00 15.41  ? 0   MET   A CE  1 
ATOM   23   N N   . CYS   A 1 4   ? 32.923 -15.838 8.742  1.00 13.11  ? 1   CYS   A N   1 
ATOM   24   C CA  . CYS   A 1 4   ? 31.532 -16.235 8.572  1.00 12.78  ? 1   CYS   A CA  1 
ATOM   25   C C   . CYS   A 1 4   ? 31.407 -17.712 8.199  1.00 11.95  ? 1   CYS   A C   1 
ATOM   26   O O   . CYS   A 1 4   ? 30.331 -18.144 7.768  1.00 12.54  ? 1   CYS   A O   1 
ATOM   27   C CB  . CYS   A 1 4   ? 30.960 -15.389 7.436  1.00 15.61  ? 1   CYS   A CB  1 
ATOM   28   S SG  . CYS   A 1 4   ? 30.419 -13.769 7.970  1.00 21.18  ? 1   CYS   A SG  1 
ATOM   29   N N   . ASP   A 1 5   ? 32.479 -18.500 8.367  1.00 11.78  ? 2   ASP   A N   1 
ATOM   30   C CA  . ASP   A 1 5   ? 32.502 -19.872 7.860  1.00 13.19  ? 2   ASP   A CA  1 
ATOM   31   C C   . ASP   A 1 5   ? 31.372 -20.744 8.411  1.00 11.68  ? 2   ASP   A C   1 
ATOM   32   O O   . ASP   A 1 5   ? 30.919 -21.661 7.720  1.00 13.19  ? 2   ASP   A O   1 
ATOM   33   C CB  . ASP   A 1 5   ? 33.856 -20.529 8.125  1.00 16.10  ? 2   ASP   A CB  1 
ATOM   34   C CG  . ASP   A 1 5   ? 34.919 -20.085 7.146  1.00 24.26  ? 2   ASP   A CG  1 
ATOM   35   O OD1 . ASP   A 1 5   ? 34.572 -19.413 6.151  1.00 27.20  ? 2   ASP   A OD1 1 
ATOM   36   O OD2 . ASP   A 1 5   ? 36.099 -20.414 7.372  1.00 28.46  ? 2   ASP   A OD2 1 
ATOM   37   N N   . ALA   A 1 6   ? 30.924 -20.512 9.645  1.00 11.71  ? 3   ALA   A N   1 
ATOM   38   C CA  . ALA   A 1 6   ? 29.858 -21.343 10.200 1.00 12.49  ? 3   ALA   A CA  1 
ATOM   39   C C   . ALA   A 1 6   ? 28.484 -21.019 9.627  1.00 8.86   ? 3   ALA   A C   1 
ATOM   40   O O   . ALA   A 1 6   ? 27.535 -21.764 9.888  1.00 10.15  ? 3   ALA   A O   1 
ATOM   41   C CB  . ALA   A 1 6   ? 29.815 -21.201 11.718 1.00 14.18  ? 3   ALA   A CB  1 
ATOM   42   N N   . PHE   A 1 7   ? 28.353 -19.942 8.853  1.00 9.01   ? 4   PHE   A N   1 
ATOM   43   C CA  . PHE   A 1 7   ? 27.067 -19.544 8.298  1.00 8.43   ? 4   PHE   A CA  1 
ATOM   44   C C   . PHE   A 1 7   ? 26.919 -19.903 6.829  1.00 7.38   ? 4   PHE   A C   1 
ATOM   45   O O   . PHE   A 1 7   ? 25.787 -19.992 6.345  1.00 10.34  ? 4   PHE   A O   1 
ATOM   46   C CB  . PHE   A 1 7   ? 26.872 -18.031 8.465  1.00 8.83   ? 4   PHE   A CB  1 
ATOM   47   C CG  . PHE   A 1 7   ? 26.753 -17.604 9.895  1.00 10.32  ? 4   PHE   A CG  1 
ATOM   48   C CD1 . PHE   A 1 7   ? 25.538 -17.677 10.548 1.00 9.40   ? 4   PHE   A CD1 1 
ATOM   49   C CD2 . PHE   A 1 7   ? 27.857 -17.148 10.587 1.00 10.87  ? 4   PHE   A CD2 1 
ATOM   50   C CE1 . PHE   A 1 7   ? 25.415 -17.304 11.860 1.00 12.49  ? 4   PHE   A CE1 1 
ATOM   51   C CE2 . PHE   A 1 7   ? 27.740 -16.769 11.912 1.00 11.48  ? 4   PHE   A CE2 1 
ATOM   52   C CZ  . PHE   A 1 7   ? 26.511 -16.849 12.547 1.00 12.43  ? 4   PHE   A CZ  1 
ATOM   53   N N   . VAL   A 1 8   ? 28.026 -20.107 6.112  1.00 8.16   ? 5   VAL   A N   1 
ATOM   54   C CA  . VAL   A 1 8   ? 27.965 -20.279 4.665  1.00 8.23   ? 5   VAL   A CA  1 
ATOM   55   C C   . VAL   A 1 8   ? 27.268 -21.588 4.308  1.00 7.66   ? 5   VAL   A C   1 
ATOM   56   O O   . VAL   A 1 8   ? 27.438 -22.626 4.977  1.00 9.83   ? 5   VAL   A O   1 
ATOM   57   C CB  . VAL   A 1 8   ? 29.362 -20.175 4.024  1.00 11.18  ? 5   VAL   A CB  1 
ATOM   58   C CG1 . VAL   A 1 8   ? 29.924 -18.773 4.223  1.00 11.71  ? 5   VAL   A CG1 1 
ATOM   59   C CG2 . VAL   A 1 8   ? 30.310 -21.217 4.583  1.00 15.22  ? 5   VAL   A CG2 1 
ATOM   60   N N   . GLY   A 1 9   ? 26.464 -21.537 3.254  1.00 8.90   ? 6   GLY   A N   1 
ATOM   61   C CA  . GLY   A 1 9   ? 25.750 -22.683 2.739  1.00 9.90   ? 6   GLY   A CA  1 
ATOM   62   C C   . GLY   A 1 9   ? 24.323 -22.303 2.403  1.00 8.72   ? 6   GLY   A C   1 
ATOM   63   O O   . GLY   A 1 9   ? 23.967 -21.125 2.322  1.00 10.42  ? 6   GLY   A O   1 
ATOM   64   N N   . THR   A 1 10  ? 23.493 -23.319 2.199  1.00 10.06  ? 7   THR   A N   1 
ATOM   65   C CA  . THR   A 1 10  ? 22.079 -23.111 1.942  1.00 9.49   ? 7   THR   A CA  1 
ATOM   66   C C   . THR   A 1 10  ? 21.265 -23.712 3.080  1.00 8.72   ? 7   THR   A C   1 
ATOM   67   O O   . THR   A 1 10  ? 21.650 -24.728 3.677  1.00 9.03   ? 7   THR   A O   1 
ATOM   68   C CB  . THR   A 1 10  ? 21.653 -23.687 0.583  1.00 8.64   ? 7   THR   A CB  1 
ATOM   69   O OG1 . THR   A 1 10  ? 21.880 -25.100 0.570  1.00 10.79  ? 7   THR   A OG1 1 
ATOM   70   C CG2 . THR   A 1 10  ? 22.447 -23.065 -0.532 1.00 10.79  ? 7   THR   A CG2 1 
ATOM   71   N N   . TRP   A 1 11  ? 20.129 -23.074 3.366  1.00 8.57   ? 8   TRP   A N   1 
ATOM   72   C CA  . TRP   A 1 11  ? 19.329 -23.335 4.553  1.00 8.14   ? 8   TRP   A CA  1 
ATOM   73   C C   . TRP   A 1 11  ? 17.854 -23.256 4.181  1.00 9.86   ? 8   TRP   A C   1 
ATOM   74   O O   . TRP   A 1 11  ? 17.468 -22.501 3.282  1.00 12.11  ? 8   TRP   A O   1 
ATOM   75   C CB  . TRP   A 1 11  ? 19.602 -22.282 5.631  1.00 8.85   ? 8   TRP   A CB  1 
ATOM   76   C CG  . TRP   A 1 11  ? 21.056 -22.166 6.038  1.00 9.09   ? 8   TRP   A CG  1 
ATOM   77   C CD1 . TRP   A 1 11  ? 22.027 -21.395 5.456  1.00 9.95   ? 8   TRP   A CD1 1 
ATOM   78   C CD2 . TRP   A 1 11  ? 21.685 -22.837 7.139  1.00 8.94   ? 8   TRP   A CD2 1 
ATOM   79   N NE1 . TRP   A 1 11  ? 23.223 -21.553 6.136  1.00 10.75  ? 8   TRP   A NE1 1 
ATOM   80   C CE2 . TRP   A 1 11  ? 23.035 -22.434 7.167  1.00 8.89   ? 8   TRP   A CE2 1 
ATOM   81   C CE3 . TRP   A 1 11  ? 21.236 -23.758 8.094  1.00 9.05   ? 8   TRP   A CE3 1 
ATOM   82   C CZ2 . TRP   A 1 11  ? 23.933 -22.908 8.120  1.00 8.16   ? 8   TRP   A CZ2 1 
ATOM   83   C CZ3 . TRP   A 1 11  ? 22.117 -24.210 9.048  1.00 9.53   ? 8   TRP   A CZ3 1 
ATOM   84   C CH2 . TRP   A 1 11  ? 23.459 -23.796 9.050  1.00 9.60   ? 8   TRP   A CH2 1 
ATOM   85   N N   . LYS   A 1 12  ? 17.027 -24.035 4.885  1.00 9.36   ? 9   LYS   A N   1 
ATOM   86   C CA  . LYS   A 1 12  ? 15.584 -24.056 4.653  1.00 9.32   ? 9   LYS   A CA  1 
ATOM   87   C C   . LYS   A 1 12  ? 14.851 -23.968 5.987  1.00 9.32   ? 9   LYS   A C   1 
ATOM   88   O O   . LYS   A 1 12  ? 15.342 -24.445 7.013  1.00 11.36  ? 9   LYS   A O   1 
ATOM   89   C CB  . LYS   A 1 12  ? 15.131 -25.291 3.841  1.00 10.47  ? 9   LYS   A CB  1 
ATOM   90   C CG  . LYS   A 1 12  ? 15.513 -26.624 4.464  1.00 11.27  ? 9   LYS   A CG  1 
ATOM   91   C CD  . LYS   A 1 12  ? 15.210 -27.799 3.537  1.00 12.88  ? 9   LYS   A CD  1 
ATOM   92   C CE  . LYS   A 1 12  ? 15.679 -29.111 4.143  1.00 14.56  ? 9   LYS   A CE  1 
ATOM   93   N NZ  . LYS   A 1 12  ? 15.458 -30.260 3.197  1.00 15.75  ? 9   LYS   A NZ  1 
ATOM   94   N N   . LEU   A 1 13  ? 13.665 -23.362 5.963  1.00 11.08  ? 10  LEU   A N   1 
ATOM   95   C CA  . LEU   A 1 13  ? 12.964 -23.023 7.200  1.00 12.28  ? 10  LEU   A CA  1 
ATOM   96   C C   . LEU   A 1 13  ? 12.371 -24.265 7.867  1.00 13.43  ? 10  LEU   A C   1 
ATOM   97   O O   . LEU   A 1 13  ? 11.720 -25.084 7.211  1.00 15.18  ? 10  LEU   A O   1 
ATOM   98   C CB  . LEU   A 1 13  ? 11.858 -22.009 6.896  1.00 13.15  ? 10  LEU   A CB  1 
ATOM   99   C CG  . LEU   A 1 13  ? 11.072 -21.478 8.093  1.00 11.78  ? 10  LEU   A CG  1 
ATOM   100  C CD1 . LEU   A 1 13  ? 11.924 -20.619 9.002  1.00 10.24  ? 10  LEU   A CD1 1 
ATOM   101  C CD2 . LEU   A 1 13  ? 9.866  -20.689 7.602  1.00 14.50  ? 10  LEU   A CD2 1 
ATOM   102  N N   . VAL   A 1 14  ? 12.597 -24.400 9.170  1.00 12.33  ? 11  VAL   A N   1 
ATOM   103  C CA  . VAL   A 1 14  ? 11.975 -25.448 9.982  1.00 11.92  ? 11  VAL   A CA  1 
ATOM   104  C C   . VAL   A 1 14  ? 10.756 -24.928 10.731 1.00 11.73  ? 11  VAL   A C   1 
ATOM   105  O O   . VAL   A 1 14  ? 9.690  -25.549 10.707 1.00 16.23  ? 11  VAL   A O   1 
ATOM   106  C CB  . VAL   A 1 14  ? 12.994 -26.072 10.964 1.00 14.60  ? 11  VAL   A CB  1 
ATOM   107  C CG1 . VAL   A 1 14  ? 12.287 -27.054 11.923 1.00 15.03  ? 11  VAL   A CG1 1 
ATOM   108  C CG2 . VAL   A 1 14  ? 14.110 -26.747 10.226 1.00 16.37  ? 11  VAL   A CG2 1 
ATOM   109  N N   . SER   A 1 15  ? 10.906 -23.805 11.435 1.00 10.80  ? 12  SER   A N   1 
ATOM   110  C CA  . SER   A 1 15  ? 9.856  -23.330 12.318 1.00 10.64  ? 12  SER   A CA  1 
ATOM   111  C C   . SER   A 1 15  ? 9.940  -21.816 12.437 1.00 10.60  ? 12  SER   A C   1 
ATOM   112  O O   . SER   A 1 15  ? 10.997 -21.206 12.224 1.00 10.01  ? 12  SER   A O   1 
ATOM   113  C CB  . SER   A 1 15  ? 9.974  -23.954 13.709 1.00 12.18  ? 12  SER   A CB  1 
ATOM   114  O OG  . SER   A 1 15  ? 11.150 -23.523 14.363 1.00 13.47  ? 12  SER   A OG  1 
ATOM   115  N N   . SER   A 1 16  ? 8.805  -21.216 12.793 1.00 12.69  ? 13  SER   A N   1 
ATOM   116  C CA  . SER   A 1 16  ? 8.702  -19.776 12.987 1.00 12.59  ? 13  SER   A CA  1 
ATOM   117  C C   . SER   A 1 16  ? 7.817  -19.500 14.194 1.00 11.90  ? 13  SER   A C   1 
ATOM   118  O O   . SER   A 1 16  ? 6.748  -20.100 14.341 1.00 15.04  ? 13  SER   A O   1 
ATOM   119  C CB  . SER   A 1 16  ? 8.103  -19.127 11.736 1.00 13.29  ? 13  SER   A CB  1 
ATOM   120  O OG  . SER   A 1 16  ? 8.088  -17.722 11.850 1.00 14.71  ? 13  SER   A OG  1 
ATOM   121  N N   . GLU   A 1 17  ? 8.264  -18.595 15.052 1.00 11.54  ? 14  GLU   A N   1 
ATOM   122  C CA  . GLU   A 1 17  ? 7.517  -18.180 16.232 1.00 11.83  ? 14  GLU   A CA  1 
ATOM   123  C C   . GLU   A 1 17  ? 7.418  -16.660 16.247 1.00 10.40  ? 14  GLU   A C   1 
ATOM   124  O O   . GLU   A 1 17  ? 8.430  -15.969 16.106 1.00 11.24  ? 14  GLU   A O   1 
ATOM   125  C CB  . GLU   A 1 17  ? 8.228  -18.698 17.490 1.00 15.56  ? 14  GLU   A CB  1 
ATOM   126  C CG  . GLU   A 1 17  ? 7.733  -18.140 18.818 1.00 23.96  ? 14  GLU   A CG  1 
ATOM   127  C CD  . GLU   A 1 17  ? 8.579  -18.636 19.991 1.00 28.89  ? 14  GLU   A CD  1 
ATOM   128  O OE1 . GLU   A 1 17  ? 8.702  -19.870 20.145 1.00 33.98  ? 14  GLU   A OE1 1 
ATOM   129  O OE2 . GLU   A 1 17  ? 9.176  -17.800 20.719 1.00 26.23  ? 14  GLU   A OE2 1 
ATOM   130  N N   . ASN   A 1 18  ? 6.197  -16.143 16.395 1.00 10.52  ? 15  ASN   A N   1 
ATOM   131  C CA  . ASN   A 1 18  ? 5.924  -14.705 16.549 1.00 10.97  ? 15  ASN   A CA  1 
ATOM   132  C C   . ASN   A 1 18  ? 6.327  -13.851 15.342 1.00 9.68   ? 15  ASN   A C   1 
ATOM   133  O O   . ASN   A 1 18  ? 6.471  -12.626 15.473 1.00 11.44  ? 15  ASN   A O   1 
ATOM   134  C CB  . ASN   A 1 18  ? 6.516  -14.097 17.832 1.00 11.22  ? 15  ASN   A CB  1 
ATOM   135  C CG  . ASN   A 1 18  ? 6.141  -14.862 19.083 1.00 14.32  ? 15  ASN   A CG  1 
ATOM   136  O OD1 . ASN   A 1 18  ? 5.036  -15.406 19.197 1.00 15.61  ? 15  ASN   A OD1 1 
ATOM   137  N ND2 . ASN   A 1 18  ? 7.035  -14.856 20.064 1.00 17.11  ? 15  ASN   A ND2 1 
ATOM   138  N N   . PHE   A 1 19  ? 6.517  -14.452 14.168 1.00 10.71  ? 16  PHE   A N   1 
ATOM   139  C CA  . PHE   A 1 19  ? 6.960  -13.679 13.014 1.00 13.47  ? 16  PHE   A CA  1 
ATOM   140  C C   . PHE   A 1 19  ? 5.913  -12.657 12.614 1.00 12.59  ? 16  PHE   A C   1 
ATOM   141  O O   . PHE   A 1 19  ? 6.243  -11.512 12.273 1.00 11.04  ? 16  PHE   A O   1 
ATOM   142  C CB  . PHE   A 1 19  ? 7.269  -14.614 11.849 1.00 15.66  ? 16  PHE   A CB  1 
ATOM   143  C CG  . PHE   A 1 19  ? 7.936  -13.946 10.682 1.00 18.41  ? 16  PHE   A CG  1 
ATOM   144  C CD1 . PHE   A 1 19  ? 9.000  -13.073 10.870 1.00 19.99  ? 16  PHE   A CD1 1 
ATOM   145  C CD2 . PHE   A 1 19  ? 7.505  -14.203 9.391  1.00 19.09  ? 16  PHE   A CD2 1 
ATOM   146  C CE1 . PHE   A 1 19  ? 9.630  -12.474 9.778  1.00 22.65  ? 16  PHE   A CE1 1 
ATOM   147  C CE2 . PHE   A 1 19  ? 8.120  -13.606 8.301  1.00 22.09  ? 16  PHE   A CE2 1 
ATOM   148  C CZ  . PHE   A 1 19  ? 9.179  -12.741 8.494  1.00 22.90  ? 16  PHE   A CZ  1 
ATOM   149  N N   . ASP   A 1 20  ? 4.640  -13.041 12.663 1.00 12.31  ? 17  ASP   A N   1 
ATOM   150  C CA  . ASP   A 1 20  ? 3.614  -12.085 12.284 1.00 11.85  ? 17  ASP   A CA  1 
ATOM   151  C C   . ASP   A 1 20  ? 3.554  -10.926 13.274 1.00 12.16  ? 17  ASP   A C   1 
ATOM   152  O O   . ASP   A 1 20  ? 3.417  -9.765  12.869 1.00 13.08  ? 17  ASP   A O   1 
ATOM   153  C CB  . ASP   A 1 20  ? 2.261  -12.774 12.117 1.00 15.27  ? 17  ASP   A CB  1 
ATOM   154  C CG  . ASP   A 1 20  ? 1.267  -11.885 11.420 1.00 19.59  ? 17  ASP   A CG  1 
ATOM   155  O OD1 . ASP   A 1 20  ? 0.657  -11.013 12.077 1.00 21.86  ? 17  ASP   A OD1 1 
ATOM   156  O OD2 . ASP   A 1 20  ? 1.160  -12.009 10.188 1.00 22.44  ? 17  ASP   A OD2 1 
ATOM   157  N N   . ASP   A 1 21  ? 3.684  -11.216 14.572 1.00 11.89  ? 18  ASP   A N   1 
ATOM   158  C CA  . ASP   A 1 21  ? 3.713  -10.150 15.573 1.00 12.69  ? 18  ASP   A CA  1 
ATOM   159  C C   . ASP   A 1 21  ? 4.883  -9.208  15.332 1.00 12.05  ? 18  ASP   A C   1 
ATOM   160  O O   . ASP   A 1 21  ? 4.734  -7.988  15.441 1.00 11.84  ? 18  ASP   A O   1 
ATOM   161  C CB  . ASP   A 1 21  ? 3.798  -10.745 16.976 1.00 13.32  ? 18  ASP   A CB  1 
ATOM   162  C CG  . ASP   A 1 21  ? 2.483  -11.350 17.438 1.00 14.76  ? 18  ASP   A CG  1 
ATOM   163  O OD1 . ASP   A 1 21  ? 1.412  -10.873 17.002 1.00 15.15  ? 18  ASP   A OD1 1 
ATOM   164  O OD2 . ASP   A 1 21  ? 2.524  -12.302 18.244 1.00 21.75  ? 18  ASP   A OD2 1 
ATOM   165  N N   . TYR   A 1 22  ? 6.058  -9.761  15.008 1.00 12.04  ? 19  TYR   A N   1 
ATOM   166  C CA  . TYR   A 1 22  ? 7.208  -8.932  14.680 1.00 12.45  ? 19  TYR   A CA  1 
ATOM   167  C C   . TYR   A 1 22  ? 6.903  -8.015  13.498 1.00 10.46  ? 19  TYR   A C   1 
ATOM   168  O O   . TYR   A 1 22  ? 7.131  -6.803  13.580 1.00 12.07  ? 19  TYR   A O   1 
ATOM   169  C CB  . TYR   A 1 22  ? 8.440  -9.803  14.407 1.00 10.33  ? 19  TYR   A CB  1 
ATOM   170  C CG  . TYR   A 1 22  ? 9.593  -9.014  13.816 1.00 9.47   ? 19  TYR   A CG  1 
ATOM   171  C CD1 . TYR   A 1 22  ? 10.410 -8.216  14.616 1.00 11.96  ? 19  TYR   A CD1 1 
ATOM   172  C CD2 . TYR   A 1 22  ? 9.831  -9.030  12.442 1.00 10.33  ? 19  TYR   A CD2 1 
ATOM   173  C CE1 . TYR   A 1 22  ? 11.457 -7.477  14.057 1.00 11.66  ? 19  TYR   A CE1 1 
ATOM   174  C CE2 . TYR   A 1 22  ? 10.872 -8.306  11.876 1.00 10.22  ? 19  TYR   A CE2 1 
ATOM   175  C CZ  . TYR   A 1 22  ? 11.671 -7.521  12.683 1.00 9.74   ? 19  TYR   A CZ  1 
ATOM   176  O OH  . TYR   A 1 22  ? 12.695 -6.792  12.112 1.00 11.89  ? 19  TYR   A OH  1 
ATOM   177  N N   . MET   A 1 23  ? 6.401  -8.568  12.380 1.00 11.14  ? 20  MET   A N   1 
ATOM   178  C CA  . MET   A 1 23  ? 6.039  -7.691  11.269 1.00 11.71  ? 20  MET   A CA  1 
ATOM   179  C C   . MET   A 1 23  ? 4.978  -6.673  11.620 1.00 13.16  ? 20  MET   A C   1 
ATOM   180  O O   . MET   A 1 23  ? 5.013  -5.555  11.092 1.00 14.71  ? 20  MET   A O   1 
ATOM   181  C CB  . MET   A 1 23  ? 5.811  -8.327  9.885  1.00 17.02  ? 20  MET   A CB  1 
ATOM   182  C CG  . MET   A 1 23  ? 6.765  -9.388  9.373  1.00 13.28  ? 20  MET   A CG  1 
ATOM   183  S SD  . MET   A 1 23  ? 6.108  -10.364 7.977  1.00 14.20  ? 20  MET   A SD  1 
ATOM   184  C CE  . MET   A 1 23  ? 4.990  -11.553 8.739  1.00 16.61  ? 20  MET   A CE  1 
ATOM   185  N N   . LYS   A 1 24  ? 4.038  -7.020  12.497 1.00 13.89  ? 21  LYS   A N   1 
ATOM   186  C CA  . LYS   A 1 24  ? 3.058  -6.033  12.933 1.00 16.35  ? 21  LYS   A CA  1 
ATOM   187  C C   . LYS   A 1 24  ? 3.738  -4.842  13.598 1.00 15.72  ? 21  LYS   A C   1 
ATOM   188  O O   . LYS   A 1 24  ? 3.423  -3.682  13.297 1.00 17.68  ? 21  LYS   A O   1 
ATOM   189  C CB  . LYS   A 1 24  ? 2.077  -6.664  13.913 1.00 23.17  ? 21  LYS   A CB  1 
ATOM   190  C CG  . LYS   A 1 24  ? 1.003  -7.492  13.297 1.00 31.72  ? 21  LYS   A CG  1 
ATOM   191  C CD  . LYS   A 1 24  ? 0.089  -7.960  14.436 1.00 38.29  ? 21  LYS   A CD  1 
ATOM   192  C CE  . LYS   A 1 24  ? -0.621 -9.291  14.231 0.50 52.11  ? 21  LYS   A CE  1 
ATOM   193  N NZ  . LYS   A 1 24  ? 0.040  -10.601 14.519 1.00 50.29  ? 21  LYS   A NZ  1 
ATOM   194  N N   . GLU   A 1 25  ? 4.678  -5.106  14.513 1.00 14.50  ? 22  GLU   A N   1 
ATOM   195  C CA  . GLU   A 1 25  ? 5.370  -4.010  15.196 1.00 15.17  ? 22  GLU   A CA  1 
ATOM   196  C C   . GLU   A 1 25  ? 6.188  -3.170  14.227 1.00 15.57  ? 22  GLU   A C   1 
ATOM   197  O O   . GLU   A 1 25  ? 6.302  -1.952  14.402 1.00 16.67  ? 22  GLU   A O   1 
ATOM   198  C CB  . GLU   A 1 25  ? 6.278  -4.556  16.297 1.00 18.39  ? 22  GLU   A CB  1 
ATOM   199  C CG  . GLU   A 1 25  ? 5.527  -5.239  17.409 1.00 24.22  ? 22  GLU   A CG  1 
ATOM   200  C CD  . GLU   A 1 25  ? 4.565  -4.312  18.134 1.00 26.43  ? 22  GLU   A CD  1 
ATOM   201  O OE1 . GLU   A 1 25  ? 4.815  -3.091  18.185 1.00 30.64  ? 22  GLU   A OE1 1 
ATOM   202  O OE2 . GLU   A 1 25  ? 3.532  -4.807  18.631 1.00 29.23  ? 22  GLU   A OE2 1 
ATOM   203  N N   . VAL   A 1 26  ? 6.761  -3.802  13.207 1.00 14.75  ? 23  VAL   A N   1 
ATOM   204  C CA  . VAL   A 1 26  ? 7.520  -3.076  12.200 1.00 14.57  ? 23  VAL   A CA  1 
ATOM   205  C C   . VAL   A 1 26  ? 6.599  -2.195  11.364 1.00 17.25  ? 23  VAL   A C   1 
ATOM   206  O O   . VAL   A 1 26  ? 7.006  -1.123  10.900 1.00 20.93  ? 23  VAL   A O   1 
ATOM   207  C CB  . VAL   A 1 26  ? 8.322  -4.088  11.356 1.00 15.70  ? 23  VAL   A CB  1 
ATOM   208  C CG1 . VAL   A 1 26  ? 8.892  -3.422  10.128 1.00 17.12  ? 23  VAL   A CG1 1 
ATOM   209  C CG2 . VAL   A 1 26  ? 9.433  -4.723  12.197 1.00 16.43  ? 23  VAL   A CG2 1 
ATOM   210  N N   . GLY   A 1 27  ? 5.346  -2.607  11.183 1.00 15.25  ? 24  GLY   A N   1 
ATOM   211  C CA  . GLY   A 1 27  ? 4.379  -1.853  10.409 1.00 17.29  ? 24  GLY   A CA  1 
ATOM   212  C C   . GLY   A 1 27  ? 3.987  -2.464  9.079  1.00 16.10  ? 24  GLY   A C   1 
ATOM   213  O O   . GLY   A 1 27  ? 3.360  -1.773  8.260  1.00 18.86  ? 24  GLY   A O   1 
ATOM   214  N N   . VAL   A 1 28  ? 4.325  -3.734  8.846  1.00 15.54  ? 25  VAL   A N   1 
ATOM   215  C CA  . VAL   A 1 28  ? 4.020  -4.393  7.585  1.00 17.14  ? 25  VAL   A CA  1 
ATOM   216  C C   . VAL   A 1 28  ? 2.512  -4.551  7.434  1.00 21.96  ? 25  VAL   A C   1 
ATOM   217  O O   . VAL   A 1 28  ? 1.807  -4.923  8.383  1.00 22.52  ? 25  VAL   A O   1 
ATOM   218  C CB  . VAL   A 1 28  ? 4.740  -5.753  7.535  1.00 14.40  ? 25  VAL   A CB  1 
ATOM   219  C CG1 . VAL   A 1 28  ? 4.543  -6.418  6.194  1.00 17.99  ? 25  VAL   A CG1 1 
ATOM   220  C CG2 . VAL   A 1 28  ? 6.244  -5.584  7.845  1.00 14.14  ? 25  VAL   A CG2 1 
ATOM   221  N N   . GLY   A 1 29  ? 2.011  -4.267  6.231  1.00 24.55  ? 26  GLY   A N   1 
ATOM   222  C CA  . GLY   A 1 29  ? 0.591  -4.392  5.972  1.00 25.86  ? 26  GLY   A CA  1 
ATOM   223  C C   . GLY   A 1 29  ? 0.117  -5.834  5.961  1.00 25.95  ? 26  GLY   A C   1 
ATOM   224  O O   . GLY   A 1 29  ? 0.898  -6.780  5.854  1.00 24.29  ? 26  GLY   A O   1 
ATOM   225  N N   . PHE   A 1 30  ? -1.209 -5.989  6.054  1.00 27.87  ? 27  PHE   A N   1 
ATOM   226  C CA  . PHE   A 1 30  ? -1.815 -7.311  6.217  1.00 25.62  ? 27  PHE   A CA  1 
ATOM   227  C C   . PHE   A 1 30  ? -1.446 -8.252  5.072  1.00 25.22  ? 27  PHE   A C   1 
ATOM   228  O O   . PHE   A 1 30  ? -0.962 -9.368  5.304  1.00 24.28  ? 27  PHE   A O   1 
ATOM   229  C CB  . PHE   A 1 30  ? -3.336 -7.164  6.393  1.00 24.70  ? 27  PHE   A CB  1 
ATOM   230  C CG  . PHE   A 1 30  ? -4.081 -8.474  6.448  1.00 26.77  ? 27  PHE   A CG  1 
ATOM   231  C CD1 . PHE   A 1 30  ? -4.160 -9.192  7.629  1.00 26.16  ? 27  PHE   A CD1 1 
ATOM   232  C CD2 . PHE   A 1 30  ? -4.752 -8.955  5.331  1.00 27.49  ? 27  PHE   A CD2 1 
ATOM   233  C CE1 . PHE   A 1 30  ? -4.855 -10.394 7.685  1.00 26.15  ? 27  PHE   A CE1 1 
ATOM   234  C CE2 . PHE   A 1 30  ? -5.454 -10.148 5.380  1.00 27.35  ? 27  PHE   A CE2 1 
ATOM   235  C CZ  . PHE   A 1 30  ? -5.508 -10.869 6.559  1.00 26.16  ? 27  PHE   A CZ  1 
ATOM   236  N N   . ALA   A 1 31  ? -1.650 -7.814  3.825  1.00 26.24  ? 28  ALA   A N   1 
ATOM   237  C CA  . ALA   A 1 31  ? -1.412 -8.697  2.683  1.00 25.97  ? 28  ALA   A CA  1 
ATOM   238  C C   . ALA   A 1 31  ? 0.049  -9.133  2.604  1.00 24.10  ? 28  ALA   A C   1 
ATOM   239  O O   . ALA   A 1 31  ? 0.342  -10.311 2.365  1.00 22.64  ? 28  ALA   A O   1 
ATOM   240  C CB  . ALA   A 1 31  ? -1.855 -8.018  1.384  1.00 28.15  ? 28  ALA   A CB  1 
ATOM   241  N N   . THR   A 1 32  ? 0.980  -8.196  2.798  1.00 22.78  ? 29  THR   A N   1 
ATOM   242  C CA  . THR   A 1 32  ? 2.394  -8.556  2.796  1.00 20.84  ? 29  THR   A CA  1 
ATOM   243  C C   . THR   A 1 32  ? 2.724  -9.528  3.921  1.00 18.46  ? 29  THR   A C   1 
ATOM   244  O O   . THR   A 1 32  ? 3.480  -10.485 3.714  1.00 18.81  ? 29  THR   A O   1 
ATOM   245  C CB  . THR   A 1 32  ? 3.258  -7.298  2.871  1.00 22.78  ? 29  THR   A CB  1 
ATOM   246  O OG1 . THR   A 1 32  ? 2.833  -6.374  1.860  1.00 24.89  ? 29  THR   A OG1 1 
ATOM   247  C CG2 . THR   A 1 32  ? 4.726  -7.640  2.691  1.00 23.76  ? 29  THR   A CG2 1 
ATOM   248  N N   . ARG   A 1 33  ? 2.172  -9.297  5.118  1.00 17.43  ? 30  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 33  ? 2.353  -10.238 6.224  1.00 15.84  ? 30  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 33  ? 1.868  -11.635 5.853  1.00 15.84  ? 30  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 33  ? 2.522  -12.636 6.178  1.00 16.39  ? 30  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 33  ? 1.603  -9.744  7.462  1.00 16.40  ? 30  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 33  ? 2.176  -8.501  8.136  1.00 15.97  ? 30  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 33  ? 1.950  -8.518  9.640  1.00 20.94  ? 30  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 33  ? 0.552  -8.779  9.991  1.00 25.94  ? 30  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 33  ? -0.424 -7.883  9.941  1.00 28.36  ? 30  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 33  ? -0.214 -6.654  9.502  1.00 31.12  ? 30  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 33  ? -1.644 -8.227  10.345 1.00 28.51  ? 30  ARG   A NH2 1 
ATOM   259  N N   . LYS   A 1 34  ? 0.720  -11.725 5.172  1.00 17.45  ? 31  LYS   A N   1 
ATOM   260  C CA  . LYS   A 1 34  ? 0.166  -13.036 4.851  1.00 18.83  ? 31  LYS   A CA  1 
ATOM   261  C C   . LYS   A 1 34  ? 1.022  -13.757 3.809  1.00 20.18  ? 31  LYS   A C   1 
ATOM   262  O O   . LYS   A 1 34  ? 1.258  -14.968 3.927  1.00 20.78  ? 31  LYS   A O   1 
ATOM   263  C CB  . LYS   A 1 34  ? -1.303 -12.914 4.427  1.00 22.26  ? 31  LYS   A CB  1 
ATOM   264  C CG  . LYS   A 1 34  ? -2.262 -12.387 5.525  1.00 22.48  ? 31  LYS   A CG  1 
ATOM   265  C CD  . LYS   A 1 34  ? -2.133 -13.132 6.861  1.00 21.33  ? 31  LYS   A CD  1 
ATOM   266  C CE  . LYS   A 1 34  ? -1.426 -12.293 7.935  1.00 20.25  ? 31  LYS   A CE  1 
ATOM   267  N NZ  . LYS   A 1 34  ? -1.276 -13.010 9.240  1.00 19.77  ? 31  LYS   A NZ  1 
ATOM   268  N N   . VAL   A 1 35  ? 1.506  -13.028 2.791  1.00 21.66  ? 32  VAL   A N   1 
ATOM   269  C CA  . VAL   A 1 35  ? 2.461  -13.596 1.833  1.00 22.70  ? 32  VAL   A CA  1 
ATOM   270  C C   . VAL   A 1 35  ? 3.711  -14.085 2.548  1.00 20.20  ? 32  VAL   A C   1 
ATOM   271  O O   . VAL   A 1 35  ? 4.187  -15.205 2.318  1.00 20.47  ? 32  VAL   A O   1 
ATOM   272  C CB  . VAL   A 1 35  ? 2.838  -12.565 0.750  1.00 27.61  ? 32  VAL   A CB  1 
ATOM   273  C CG1 . VAL   A 1 35  ? 3.874  -13.159 -0.203 1.00 30.17  ? 32  VAL   A CG1 1 
ATOM   274  C CG2 . VAL   A 1 35  ? 1.646  -12.127 -0.017 1.00 30.55  ? 32  VAL   A CG2 1 
ATOM   275  N N   . ALA   A 1 36  ? 4.285  -13.228 3.394  1.00 18.84  ? 33  ALA   A N   1 
ATOM   276  C CA  . ALA   A 1 36  ? 5.509  -13.586 4.102  1.00 19.51  ? 33  ALA   A CA  1 
ATOM   277  C C   . ALA   A 1 36  ? 5.321  -14.848 4.931  1.00 19.74  ? 33  ALA   A C   1 
ATOM   278  O O   . ALA   A 1 36  ? 6.209  -15.707 4.971  1.00 21.77  ? 33  ALA   A O   1 
ATOM   279  C CB  . ALA   A 1 36  ? 5.955  -12.424 4.992  1.00 20.75  ? 33  ALA   A CB  1 
ATOM   280  N N   . GLY   A 1 37  ? 4.172  -14.974 5.601  1.00 19.88  ? 34  GLY   A N   1 
ATOM   281  C CA  . GLY   A 1 37  ? 3.927  -16.137 6.436  1.00 20.34  ? 34  GLY   A CA  1 
ATOM   282  C C   . GLY   A 1 37  ? 3.777  -17.421 5.649  1.00 23.18  ? 34  GLY   A C   1 
ATOM   283  O O   . GLY   A 1 37  ? 4.135  -18.496 6.139  1.00 27.25  ? 34  GLY   A O   1 
ATOM   284  N N   A MET   A 1 38  ? 3.251  -17.333 4.427  0.45 23.81  ? 35  MET   A N   1 
ATOM   285  N N   B MET   A 1 38  ? 3.259  -17.331 4.423  0.55 23.01  ? 35  MET   A N   1 
ATOM   286  C CA  A MET   A 1 38  ? 3.091  -18.501 3.569  0.45 24.64  ? 35  MET   A CA  1 
ATOM   287  C CA  B MET   A 1 38  ? 3.098  -18.503 3.571  0.55 22.95  ? 35  MET   A CA  1 
ATOM   288  C C   A MET   A 1 38  ? 4.400  -18.962 2.943  0.45 24.91  ? 35  MET   A C   1 
ATOM   289  C C   B MET   A 1 38  ? 4.414  -18.979 2.975  0.55 24.21  ? 35  MET   A C   1 
ATOM   290  O O   A MET   A 1 38  ? 4.458  -20.082 2.426  0.45 25.89  ? 35  MET   A O   1 
ATOM   291  O O   B MET   A 1 38  ? 4.492  -20.121 2.512  0.55 25.37  ? 35  MET   A O   1 
ATOM   292  C CB  A MET   A 1 38  ? 2.089  -18.197 2.449  0.45 26.03  ? 35  MET   A CB  1 
ATOM   293  C CB  B MET   A 1 38  ? 2.134  -18.185 2.425  0.55 22.89  ? 35  MET   A CB  1 
ATOM   294  C CG  A MET   A 1 38  ? 0.615  -18.447 2.785  0.45 37.86  ? 35  MET   A CG  1 
ATOM   295  C CG  B MET   A 1 38  ? 0.697  -17.956 2.860  0.55 56.39  ? 35  MET   A CG  1 
ATOM   296  S SD  A MET   A 1 38  ? 0.257  -20.006 3.625  0.45 78.82  ? 35  MET   A SD  1 
ATOM   297  S SD  B MET   A 1 38  ? -0.357 -17.440 1.492  0.55 71.43  ? 35  MET   A SD  1 
ATOM   298  C CE  A MET   A 1 38  ? 0.226  -19.499 5.344  0.45 23.19  ? 35  MET   A CE  1 
ATOM   299  C CE  B MET   A 1 38  ? -0.473 -18.970 0.570  0.55 54.06  ? 35  MET   A CE  1 
ATOM   300  N N   . ALA   A 1 39  ? 5.441  -18.135 2.977  1.00 22.99  ? 36  ALA   A N   1 
ATOM   301  C CA  . ALA   A 1 39  ? 6.671  -18.447 2.268  1.00 23.24  ? 36  ALA   A CA  1 
ATOM   302  C C   . ALA   A 1 39  ? 7.453  -19.554 2.967  1.00 27.21  ? 36  ALA   A C   1 
ATOM   303  O O   . ALA   A 1 39  ? 7.464  -19.654 4.197  1.00 29.07  ? 36  ALA   A O   1 
ATOM   304  C CB  . ALA   A 1 39  ? 7.526  -17.187 2.147  1.00 22.00  ? 36  ALA   A CB  1 
ATOM   305  N N   . LYS   A 1 40  ? 8.099  -20.396 2.161  1.00 27.45  ? 37  LYS   A N   1 
ATOM   306  C CA  . LYS   A 1 40  ? 9.022  -21.424 2.624  1.00 29.51  ? 37  LYS   A CA  1 
ATOM   307  C C   . LYS   A 1 40  ? 10.401 -21.038 2.106  1.00 26.57  ? 37  LYS   A C   1 
ATOM   308  O O   . LYS   A 1 40  ? 10.858 -21.582 1.093  1.00 29.67  ? 37  LYS   A O   1 
ATOM   309  C CB  . LYS   A 1 40  ? 8.640  -22.782 2.038  1.00 34.02  ? 37  LYS   A CB  1 
ATOM   310  C CG  . LYS   A 1 40  ? 7.377  -23.389 2.615  1.00 39.96  ? 37  LYS   A CG  1 
ATOM   311  C CD  . LYS   A 1 40  ? 6.586  -24.103 1.525  1.00 45.38  ? 37  LYS   A CD  1 
ATOM   312  C CE  . LYS   A 1 40  ? 6.329  -23.193 0.329  1.00 48.44  ? 37  LYS   A CE  1 
ATOM   313  N NZ  . LYS   A 1 40  ? 5.611  -21.943 0.714  1.00 50.56  ? 37  LYS   A NZ  1 
ATOM   314  N N   . PRO   A 1 41  ? 11.090 -20.105 2.754  1.00 21.47  ? 38  PRO   A N   1 
ATOM   315  C CA  . PRO   A 1 41  ? 12.291 -19.525 2.140  1.00 20.50  ? 38  PRO   A CA  1 
ATOM   316  C C   . PRO   A 1 41  ? 13.496 -20.451 2.162  1.00 21.40  ? 38  PRO   A C   1 
ATOM   317  O O   . PRO   A 1 41  ? 13.708 -21.219 3.105  1.00 23.19  ? 38  PRO   A O   1 
ATOM   318  C CB  . PRO   A 1 41  ? 12.550 -18.258 2.969  1.00 22.67  ? 38  PRO   A CB  1 
ATOM   319  C CG  . PRO   A 1 41  ? 11.610 -18.304 4.138  1.00 24.95  ? 38  PRO   A CG  1 
ATOM   320  C CD  . PRO   A 1 41  ? 10.788 -19.542 4.080  1.00 23.68  ? 38  PRO   A CD  1 
ATOM   321  N N   . ASN   A 1 42  ? 14.283 -20.364 1.091  1.00 18.82  ? 39  ASN   A N   1 
ATOM   322  C CA  . ASN   A 1 42  ? 15.593 -20.999 0.975  1.00 18.58  ? 39  ASN   A CA  1 
ATOM   323  C C   . ASN   A 1 42  ? 16.597 -19.865 1.105  1.00 19.72  ? 39  ASN   A C   1 
ATOM   324  O O   . ASN   A 1 42  ? 16.525 -18.891 0.347  1.00 23.43  ? 39  ASN   A O   1 
ATOM   325  C CB  . ASN   A 1 42  ? 15.718 -21.649 -0.408 1.00 24.02  ? 39  ASN   A CB  1 
ATOM   326  C CG  . ASN   A 1 42  ? 17.073 -22.333 -0.654 1.00 29.28  ? 39  ASN   A CG  1 
ATOM   327  O OD1 . ASN   A 1 42  ? 17.415 -23.344 -0.021 1.00 28.83  ? 39  ASN   A OD1 1 
ATOM   328  N ND2 . ASN   A 1 42  ? 17.840 -21.791 -1.600 1.00 30.33  ? 39  ASN   A ND2 1 
ATOM   329  N N   . MET   A 1 43  ? 17.501 -19.967 2.074  1.00 15.26  ? 40  MET   A N   1 
ATOM   330  C CA  . MET   A 1 43  ? 18.472 -18.921 2.359  1.00 12.72  ? 40  MET   A CA  1 
ATOM   331  C C   . MET   A 1 43  ? 19.862 -19.382 1.940  1.00 12.74  ? 40  MET   A C   1 
ATOM   332  O O   . MET   A 1 43  ? 20.275 -20.499 2.264  1.00 13.98  ? 40  MET   A O   1 
ATOM   333  C CB  . MET   A 1 43  ? 18.431 -18.527 3.841  1.00 14.85  ? 40  MET   A CB  1 
ATOM   334  C CG  . MET   A 1 43  ? 19.324 -17.354 4.169  1.00 17.79  ? 40  MET   A CG  1 
ATOM   335  S SD  . MET   A 1 43  ? 19.588 -17.046 5.930  1.00 21.53  ? 40  MET   A SD  1 
ATOM   336  C CE  . MET   A 1 43  ? 18.152 -17.796 6.684  1.00 21.78  ? 40  MET   A CE  1 
ATOM   337  N N   . ILE   A 1 44  ? 20.569 -18.533 1.204  1.00 11.24  ? 41  ILE   A N   1 
ATOM   338  C CA  . ILE   A 1 44  ? 21.929 -18.805 0.744  1.00 10.98  ? 41  ILE   A CA  1 
ATOM   339  C C   . ILE   A 1 44  ? 22.837 -17.753 1.341  1.00 10.06  ? 41  ILE   A C   1 
ATOM   340  O O   . ILE   A 1 44  ? 22.629 -16.555 1.121  1.00 11.52  ? 41  ILE   A O   1 
ATOM   341  C CB  . ILE   A 1 44  ? 22.027 -18.776 -0.788 1.00 13.14  ? 41  ILE   A CB  1 
ATOM   342  C CG1 . ILE   A 1 44  ? 20.868 -19.554 -1.416 1.00 15.10  ? 41  ILE   A CG1 1 
ATOM   343  C CG2 . ILE   A 1 44  ? 23.423 -19.199 -1.256 1.00 12.26  ? 41  ILE   A CG2 1 
ATOM   344  C CD1 . ILE   A 1 44  ? 20.608 -19.203 -2.855 1.00 23.31  ? 41  ILE   A CD1 1 
ATOM   345  N N   . ILE   A 1 45  ? 23.863 -18.192 2.060  1.00 10.08  ? 42  ILE   A N   1 
ATOM   346  C CA  . ILE   A 1 45  ? 24.851 -17.285 2.633  1.00 8.88   ? 42  ILE   A CA  1 
ATOM   347  C C   . ILE   A 1 45  ? 26.202 -17.639 2.035  1.00 9.43   ? 42  ILE   A C   1 
ATOM   348  O O   . ILE   A 1 45  ? 26.599 -18.816 2.027  1.00 10.63  ? 42  ILE   A O   1 
ATOM   349  C CB  . ILE   A 1 45  ? 24.886 -17.371 4.172  1.00 8.08   ? 42  ILE   A CB  1 
ATOM   350  C CG1 . ILE   A 1 45  ? 23.501 -17.048 4.759  1.00 10.27  ? 42  ILE   A CG1 1 
ATOM   351  C CG2 . ILE   A 1 45  ? 25.999 -16.483 4.759  1.00 10.92  ? 42  ILE   A CG2 1 
ATOM   352  C CD1 . ILE   A 1 45  ? 23.461 -17.119 6.275  1.00 12.37  ? 42  ILE   A CD1 1 
ATOM   353  N N   . SER   A 1 46  ? 26.907 -16.625 1.538  1.00 9.34   ? 43  SER   A N   1 
ATOM   354  C CA  . SER   A 1 46  ? 28.150 -16.862 0.818  1.00 9.40   ? 43  SER   A CA  1 
ATOM   355  C C   . SER   A 1 46  ? 29.106 -15.713 1.098  1.00 8.32   ? 43  SER   A C   1 
ATOM   356  O O   . SER   A 1 46  ? 28.697 -14.617 1.495  1.00 11.09  ? 43  SER   A O   1 
ATOM   357  C CB  . SER   A 1 46  ? 27.900 -17.024 -0.687 1.00 10.40  ? 43  SER   A CB  1 
ATOM   358  O OG  . SER   A 1 46  ? 27.312 -15.857 -1.249 1.00 10.80  ? 43  SER   A OG  1 
ATOM   359  N N   . VAL   A 1 47  ? 30.393 -15.979 0.900  1.00 9.15   ? 44  VAL   A N   1 
ATOM   360  C CA  . VAL   A 1 47  ? 31.448 -15.007 1.168  1.00 9.52   ? 44  VAL   A CA  1 
ATOM   361  C C   . VAL   A 1 47  ? 32.320 -14.893 -0.079 1.00 9.09   ? 44  VAL   A C   1 
ATOM   362  O O   . VAL   A 1 47  ? 32.740 -15.913 -0.650 1.00 10.50  ? 44  VAL   A O   1 
ATOM   363  C CB  . VAL   A 1 47  ? 32.305 -15.410 2.388  1.00 11.54  ? 44  VAL   A CB  1 
ATOM   364  C CG1 . VAL   A 1 47  ? 33.516 -14.486 2.529  1.00 17.37  ? 44  VAL   A CG1 1 
ATOM   365  C CG2 . VAL   A 1 47  ? 31.478 -15.448 3.676  1.00 13.69  ? 44  VAL   A CG2 1 
ATOM   366  N N   . ASN   A 1 48  ? 32.610 -13.659 -0.486 1.00 9.63   ? 45  ASN   A N   1 
ATOM   367  C CA  . ASN   A 1 48  ? 33.528 -13.395 -1.586 1.00 8.71   ? 45  ASN   A CA  1 
ATOM   368  C C   . ASN   A 1 48  ? 34.493 -12.323 -1.094 1.00 9.72   ? 45  ASN   A C   1 
ATOM   369  O O   . ASN   A 1 48  ? 34.167 -11.130 -1.114 1.00 9.28   ? 45  ASN   A O   1 
ATOM   370  C CB  . ASN   A 1 48  ? 32.780 -12.945 -2.832 1.00 9.41   ? 45  ASN   A CB  1 
ATOM   371  C CG  . ASN   A 1 48  ? 33.650 -12.983 -4.070 1.00 8.62   ? 45  ASN   A CG  1 
ATOM   372  O OD1 . ASN   A 1 48  ? 34.689 -12.303 -4.144 1.00 13.00  ? 45  ASN   A OD1 1 
ATOM   373  N ND2 . ASN   A 1 48  ? 33.257 -13.795 -5.039 1.00 10.21  ? 45  ASN   A ND2 1 
ATOM   374  N N   . GLY   A 1 49  ? 35.669 -12.754 -0.642 1.00 10.37  ? 46  GLY   A N   1 
ATOM   375  C CA  . GLY   A 1 49  ? 36.602 -11.832 -0.009 1.00 9.58   ? 46  GLY   A CA  1 
ATOM   376  C C   . GLY   A 1 49  ? 35.981 -11.196 1.222  1.00 10.66  ? 46  GLY   A C   1 
ATOM   377  O O   . GLY   A 1 49  ? 35.587 -11.883 2.175  1.00 11.54  ? 46  GLY   A O   1 
ATOM   378  N N   . ASP   A 1 50  ? 35.907 -9.863  1.217  1.00 10.15  ? 47  ASP   A N   1 
ATOM   379  C CA  . ASP   A 1 50  ? 35.322 -9.115  2.326  1.00 8.99   ? 47  ASP   A CA  1 
ATOM   380  C C   . ASP   A 1 50  ? 33.816 -8.976  2.229  1.00 9.56   ? 47  ASP   A C   1 
ATOM   381  O O   . ASP   A 1 50  ? 33.197 -8.472  3.172  1.00 11.47  ? 47  ASP   A O   1 
ATOM   382  C CB  . ASP   A 1 50  ? 35.930 -7.714  2.412  1.00 9.84   ? 47  ASP   A CB  1 
ATOM   383  C CG  . ASP   A 1 50  ? 37.410 -7.759  2.669  1.00 12.38  ? 47  ASP   A CG  1 
ATOM   384  O OD1 . ASP   A 1 50  ? 37.784 -8.254  3.746  1.00 17.21  ? 47  ASP   A OD1 1 
ATOM   385  O OD2 . ASP   A 1 50  ? 38.197 -7.332  1.800  1.00 12.88  ? 47  ASP   A OD2 1 
ATOM   386  N N   . VAL   A 1 51  ? 33.220 -9.395  1.123  1.00 8.54   ? 48  VAL   A N   1 
ATOM   387  C CA  . VAL   A 1 51  ? 31.807 -9.137  0.852  1.00 9.16   ? 48  VAL   A CA  1 
ATOM   388  C C   . VAL   A 1 51  ? 30.993 -10.391 1.152  1.00 8.48   ? 48  VAL   A C   1 
ATOM   389  O O   . VAL   A 1 51  ? 31.167 -11.427 0.501  1.00 10.05  ? 48  VAL   A O   1 
ATOM   390  C CB  . VAL   A 1 51  ? 31.584 -8.654  -0.588 1.00 9.92   ? 48  VAL   A CB  1 
ATOM   391  C CG1 . VAL   A 1 51  ? 30.090 -8.387  -0.833 1.00 10.42  ? 48  VAL   A CG1 1 
ATOM   392  C CG2 . VAL   A 1 51  ? 32.438 -7.417  -0.871 1.00 10.85  ? 48  VAL   A CG2 1 
ATOM   393  N N   . ILE   A 1 52  ? 30.086 -10.287 2.128  1.00 8.76   ? 49  ILE   A N   1 
ATOM   394  C CA  . ILE   A 1 52  ? 29.163 -11.358 2.497  1.00 9.27   ? 49  ILE   A CA  1 
ATOM   395  C C   . ILE   A 1 52  ? 27.824 -11.105 1.827  1.00 10.04  ? 49  ILE   A C   1 
ATOM   396  O O   . ILE   A 1 52  ? 27.363 -9.962  1.759  1.00 9.81   ? 49  ILE   A O   1 
ATOM   397  C CB  . ILE   A 1 52  ? 29.009 -11.444 4.029  1.00 11.07  ? 49  ILE   A CB  1 
ATOM   398  C CG1 . ILE   A 1 52  ? 30.383 -11.539 4.684  1.00 17.85  ? 49  ILE   A CG1 1 
ATOM   399  C CG2 . ILE   A 1 52  ? 28.086 -12.590 4.449  1.00 11.55  ? 49  ILE   A CG2 1 
ATOM   400  C CD1 . ILE   A 1 52  ? 30.450 -10.826 5.967  1.00 21.14  ? 49  ILE   A CD1 1 
ATOM   401  N N   . THR   A 1 53  ? 27.199 -12.167 1.324  1.00 8.92   ? 50  THR   A N   1 
ATOM   402  C CA  . THR   A 1 53  ? 25.884 -12.074 0.708  1.00 10.55  ? 50  THR   A CA  1 
ATOM   403  C C   . THR   A 1 53  ? 24.915 -12.989 1.444  1.00 9.79   ? 50  THR   A C   1 
ATOM   404  O O   . THR   A 1 53  ? 25.215 -14.170 1.677  1.00 11.71  ? 50  THR   A O   1 
ATOM   405  C CB  . THR   A 1 53  ? 25.932 -12.433 -0.781 1.00 11.53  ? 50  THR   A CB  1 
ATOM   406  O OG1 . THR   A 1 53  ? 26.755 -11.484 -1.471 1.00 11.22  ? 50  THR   A OG1 1 
ATOM   407  C CG2 . THR   A 1 53  ? 24.542 -12.392 -1.383 1.00 10.70  ? 50  THR   A CG2 1 
ATOM   408  N N   . ILE   A 1 54  ? 23.762 -12.441 1.813  1.00 9.58   ? 51  ILE   A N   1 
ATOM   409  C CA  . ILE   A 1 54  ? 22.650 -13.222 2.340  1.00 9.32   ? 51  ILE   A CA  1 
ATOM   410  C C   . ILE   A 1 54  ? 21.500 -13.087 1.355  1.00 9.53   ? 51  ILE   A C   1 
ATOM   411  O O   . ILE   A 1 54  ? 20.983 -11.979 1.143  1.00 10.57  ? 51  ILE   A O   1 
ATOM   412  C CB  . ILE   A 1 54  ? 22.224 -12.766 3.744  1.00 10.50  ? 51  ILE   A CB  1 
ATOM   413  C CG1 . ILE   A 1 54  ? 23.384 -12.877 4.728  1.00 10.99  ? 51  ILE   A CG1 1 
ATOM   414  C CG2 . ILE   A 1 54  ? 21.007 -13.556 4.214  1.00 13.07  ? 51  ILE   A CG2 1 
ATOM   415  C CD1 . ILE   A 1 54  ? 23.092 -12.269 6.095  1.00 11.80  ? 51  ILE   A CD1 1 
ATOM   416  N N   . LYS   A 1 55  ? 21.098 -14.204 0.761  1.00 11.36  ? 52  LYS   A N   1 
ATOM   417  C CA  . LYS   A 1 55  ? 20.008 -14.228 -0.200 1.00 12.06  ? 52  LYS   A CA  1 
ATOM   418  C C   . LYS   A 1 55  ? 18.872 -15.050 0.380  1.00 12.89  ? 52  LYS   A C   1 
ATOM   419  O O   . LYS   A 1 55  ? 19.104 -16.117 0.957  1.00 15.12  ? 52  LYS   A O   1 
ATOM   420  C CB  . LYS   A 1 55  ? 20.473 -14.828 -1.529 1.00 15.12  ? 52  LYS   A CB  1 
ATOM   421  C CG  . LYS   A 1 55  ? 19.466 -14.702 -2.641 1.00 19.51  ? 52  LYS   A CG  1 
ATOM   422  C CD  . LYS   A 1 55  ? 19.998 -15.273 -3.928 1.00 24.24  ? 52  LYS   A CD  1 
ATOM   423  C CE  . LYS   A 1 55  ? 19.045 -14.959 -5.071 1.00 25.99  ? 52  LYS   A CE  1 
ATOM   424  N NZ  . LYS   A 1 55  ? 19.033 -16.050 -6.071 1.00 29.88  ? 52  LYS   A NZ  1 
ATOM   425  N N   . SER   A 1 56  ? 17.656 -14.531 0.272  1.00 13.32  ? 53  SER   A N   1 
ATOM   426  C CA  . SER   A 1 56  ? 16.445 -15.238 0.675  1.00 15.02  ? 53  SER   A CA  1 
ATOM   427  C C   . SER   A 1 56  ? 15.618 -15.467 -0.577 1.00 13.82  ? 53  SER   A C   1 
ATOM   428  O O   . SER   A 1 56  ? 15.304 -14.513 -1.290 1.00 16.46  ? 53  SER   A O   1 
ATOM   429  C CB  . SER   A 1 56  ? 15.649 -14.391 1.668  1.00 19.33  ? 53  SER   A CB  1 
ATOM   430  O OG  . SER   A 1 56  ? 14.735 -15.179 2.415  1.00 27.63  ? 53  SER   A OG  1 
ATOM   431  N N   . GLU   A 1 57  ? 15.282 -16.716 -0.866 1.00 13.31  ? 54  GLU   A N   1 
ATOM   432  C CA  . GLU   A 1 57  ? 14.531 -17.052 -2.065 1.00 14.55  ? 54  GLU   A CA  1 
ATOM   433  C C   . GLU   A 1 57  ? 13.198 -17.647 -1.653 1.00 14.30  ? 54  GLU   A C   1 
ATOM   434  O O   . GLU   A 1 57  ? 13.160 -18.588 -0.856 1.00 15.21  ? 54  GLU   A O   1 
ATOM   435  C CB  . GLU   A 1 57  ? 15.268 -18.085 -2.920 1.00 17.36  ? 54  GLU   A CB  1 
ATOM   436  C CG  . GLU   A 1 57  ? 16.600 -17.626 -3.471 1.00 17.03  ? 54  GLU   A CG  1 
ATOM   437  C CD  . GLU   A 1 57  ? 17.276 -18.704 -4.294 1.00 22.15  ? 54  GLU   A CD  1 
ATOM   438  O OE1 . GLU   A 1 57  ? 16.991 -19.905 -4.064 1.00 24.27  ? 54  GLU   A OE1 1 
ATOM   439  O OE2 . GLU   A 1 57  ? 18.060 -18.347 -5.194 1.00 23.76  ? 54  GLU   A OE2 1 
ATOM   440  N N   . SER   A 1 58  ? 12.113 -17.118 -2.215 1.00 12.98  ? 55  SER   A N   1 
ATOM   441  C CA  . SER   A 1 58  ? 10.809 -17.728 -2.022 1.00 13.51  ? 55  SER   A CA  1 
ATOM   442  C C   . SER   A 1 58  ? 10.001 -17.497 -3.284 1.00 13.71  ? 55  SER   A C   1 
ATOM   443  O O   . SER   A 1 58  ? 10.358 -16.679 -4.137 1.00 16.40  ? 55  SER   A O   1 
ATOM   444  C CB  . SER   A 1 58  ? 10.075 -17.155 -0.805 1.00 15.96  ? 55  SER   A CB  1 
ATOM   445  O OG  . SER   A 1 58  ? 9.605  -15.844 -1.066 1.00 20.51  ? 55  SER   A OG  1 
ATOM   446  N N   . THR   A 1 59  ? 8.889  -18.221 -3.384 1.00 17.05  ? 56  THR   A N   1 
ATOM   447  C CA  . THR   A 1 59  ? 8.113  -18.203 -4.614 1.00 23.57  ? 56  THR   A CA  1 
ATOM   448  C C   . THR   A 1 59  ? 7.747  -16.783 -5.019 1.00 26.29  ? 56  THR   A C   1 
ATOM   449  O O   . THR   A 1 59  ? 7.859  -16.419 -6.195 1.00 31.18  ? 56  THR   A O   1 
ATOM   450  C CB  . THR   A 1 59  ? 6.874  -19.072 -4.442 1.00 28.64  ? 56  THR   A CB  1 
ATOM   451  O OG1 . THR   A 1 59  ? 7.261  -20.444 -4.557 1.00 34.10  ? 56  THR   A OG1 1 
ATOM   452  C CG2 . THR   A 1 59  ? 5.860  -18.761 -5.516 1.00 32.86  ? 56  THR   A CG2 1 
ATOM   453  N N   . PHE   A 1 60  ? 7.354  -15.947 -4.062 1.00 21.55  ? 57  PHE   A N   1 
ATOM   454  C CA  . PHE   A 1 60  ? 6.849  -14.637 -4.428 1.00 25.90  ? 57  PHE   A CA  1 
ATOM   455  C C   . PHE   A 1 60  ? 7.769  -13.469 -4.100 1.00 25.98  ? 57  PHE   A C   1 
ATOM   456  O O   . PHE   A 1 60  ? 7.536  -12.366 -4.604 1.00 24.63  ? 57  PHE   A O   1 
ATOM   457  C CB  . PHE   A 1 60  ? 5.430  -14.425 -3.885 1.00 29.49  ? 57  PHE   A CB  1 
ATOM   458  C CG  . PHE   A 1 60  ? 4.427  -15.357 -4.506 1.00 32.79  ? 57  PHE   A CG  1 
ATOM   459  C CD1 . PHE   A 1 60  ? 4.333  -15.465 -5.889 1.00 32.71  ? 57  PHE   A CD1 1 
ATOM   460  C CD2 . PHE   A 1 60  ? 3.622  -16.162 -3.716 1.00 34.24  ? 57  PHE   A CD2 1 
ATOM   461  C CE1 . PHE   A 1 60  ? 3.424  -16.337 -6.475 1.00 34.09  ? 57  PHE   A CE1 1 
ATOM   462  C CE2 . PHE   A 1 60  ? 2.717  -17.038 -4.295 1.00 36.68  ? 57  PHE   A CE2 1 
ATOM   463  C CZ  . PHE   A 1 60  ? 2.618  -17.124 -5.676 1.00 36.10  ? 57  PHE   A CZ  1 
ATOM   464  N N   . LYS   A 1 61  ? 8.822  -13.666 -3.314 1.00 24.93  ? 58  LYS   A N   1 
ATOM   465  C CA  . LYS   A 1 61  ? 9.796  -12.592 -3.176 1.00 26.81  ? 58  LYS   A CA  1 
ATOM   466  C C   . LYS   A 1 61  ? 11.178 -13.134 -2.854 1.00 22.86  ? 58  LYS   A C   1 
ATOM   467  O O   . LYS   A 1 61  ? 11.322 -14.029 -2.013 1.00 21.91  ? 58  LYS   A O   1 
ATOM   468  C CB  . LYS   A 1 61  ? 9.361  -11.517 -2.166 1.00 32.80  ? 58  LYS   A CB  1 
ATOM   469  C CG  . LYS   A 1 61  ? 9.819  -10.114 -2.589 1.00 32.56  ? 58  LYS   A CG  1 
ATOM   470  C CD  . LYS   A 1 61  ? 9.125  -9.004  -1.826 1.00 33.89  ? 58  LYS   A CD  1 
ATOM   471  C CE  . LYS   A 1 61  ? 9.088  -7.721  -2.647 1.00 35.79  ? 58  LYS   A CE  1 
ATOM   472  N NZ  . LYS   A 1 61  ? 7.727  -7.420  -3.194 1.00 37.47  ? 58  LYS   A NZ  1 
ATOM   473  N N   . ASN   A 1 62  ? 12.176 -12.608 -3.561 1.00 19.47  ? 59  ASN   A N   1 
ATOM   474  C CA  . ASN   A 1 62  ? 13.579 -12.802 -3.242 1.00 18.52  ? 59  ASN   A CA  1 
ATOM   475  C C   . ASN   A 1 62  ? 14.140 -11.500 -2.690 1.00 18.98  ? 59  ASN   A C   1 
ATOM   476  O O   . ASN   A 1 62  ? 13.744 -10.409 -3.109 1.00 20.66  ? 59  ASN   A O   1 
ATOM   477  C CB  . ASN   A 1 62  ? 14.410 -13.156 -4.487 1.00 17.69  ? 59  ASN   A CB  1 
ATOM   478  C CG  . ASN   A 1 62  ? 14.151 -14.567 -5.015 1.00 17.62  ? 59  ASN   A CG  1 
ATOM   479  O OD1 . ASN   A 1 62  ? 13.246 -15.280 -4.560 1.00 16.13  ? 59  ASN   A OD1 1 
ATOM   480  N ND2 . ASN   A 1 62  ? 14.980 -14.985 -5.963 1.00 22.25  ? 59  ASN   A ND2 1 
ATOM   481  N N   . THR   A 1 63  ? 15.071 -11.615 -1.750 1.00 14.43  ? 60  THR   A N   1 
ATOM   482  C CA  . THR   A 1 63  ? 15.904 -10.493 -1.349 1.00 13.87  ? 60  THR   A CA  1 
ATOM   483  C C   . THR   A 1 63  ? 17.357 -10.928 -1.402 1.00 14.42  ? 60  THR   A C   1 
ATOM   484  O O   . THR   A 1 63  ? 17.686 -12.111 -1.276 1.00 14.36  ? 60  THR   A O   1 
ATOM   485  C CB  . THR   A 1 63  ? 15.599 -9.962  0.066  1.00 17.95  ? 60  THR   A CB  1 
ATOM   486  O OG1 . THR   A 1 63  ? 15.806 -10.999 1.035  1.00 17.57  ? 60  THR   A OG1 1 
ATOM   487  C CG2 . THR   A 1 63  ? 14.168 -9.442  0.153  1.00 21.17  ? 60  THR   A CG2 1 
ATOM   488  N N   . GLU   A 1 64  ? 18.229 -9.948  -1.574 1.00 14.48  ? 61  GLU   A N   1 
ATOM   489  C CA  . GLU   A 1 64  ? 19.660 -10.205 -1.605 1.00 12.25  ? 61  GLU   A CA  1 
ATOM   490  C C   . GLU   A 1 64  ? 20.338 -8.977  -1.036 1.00 12.73  ? 61  GLU   A C   1 
ATOM   491  O O   . GLU   A 1 64  ? 20.127 -7.867  -1.536 1.00 15.93  ? 61  GLU   A O   1 
ATOM   492  C CB  . GLU   A 1 64  ? 20.112 -10.455 -3.046 1.00 13.64  ? 61  GLU   A CB  1 
ATOM   493  C CG  . GLU   A 1 64  ? 21.583 -10.789 -3.194 1.00 22.35  ? 61  GLU   A CG  1 
ATOM   494  C CD  . GLU   A 1 64  ? 22.009 -10.929 -4.647 1.00 31.02  ? 61  GLU   A CD  1 
ATOM   495  O OE1 . GLU   A 1 64  ? 21.170 -10.704 -5.549 1.00 37.06  ? 61  GLU   A OE1 1 
ATOM   496  O OE2 . GLU   A 1 64  ? 23.183 -11.269 -4.885 1.00 34.61  ? 61  GLU   A OE2 1 
ATOM   497  N N   . ILE   A 1 65  ? 21.110 -9.164  0.025  1.00 11.14  ? 62  ILE   A N   1 
ATOM   498  C CA  . ILE   A 1 65  ? 21.931 -8.100  0.583  1.00 8.85   ? 62  ILE   A CA  1 
ATOM   499  C C   . ILE   A 1 65  ? 23.388 -8.540  0.526  1.00 8.53   ? 62  ILE   A C   1 
ATOM   500  O O   . ILE   A 1 65  ? 23.720 -9.687  0.852  1.00 12.79  ? 62  ILE   A O   1 
ATOM   501  C CB  . ILE   A 1 65  ? 21.502 -7.689  2.010  1.00 9.04   ? 62  ILE   A CB  1 
ATOM   502  C CG1 . ILE   A 1 65  ? 21.536 -8.883  2.972  1.00 10.69  ? 62  ILE   A CG1 1 
ATOM   503  C CG2 . ILE   A 1 65  ? 20.111 -7.050  1.984  1.00 15.32  ? 62  ILE   A CG2 1 
ATOM   504  C CD1 . ILE   A 1 65  ? 21.346 -8.490  4.440  1.00 15.40  ? 62  ILE   A CD1 1 
ATOM   505  N N   . SER   A 1 66  ? 24.255 -7.638  0.104  1.00 10.16  ? 63  SER   A N   1 
ATOM   506  C CA  . SER   A 1 66  ? 25.689 -7.873  0.104  1.00 9.65   ? 63  SER   A CA  1 
ATOM   507  C C   . SER   A 1 66  ? 26.335 -6.750  0.896  1.00 9.94   ? 63  SER   A C   1 
ATOM   508  O O   . SER   A 1 66  ? 25.981 -5.577  0.720  1.00 13.35  ? 63  SER   A O   1 
ATOM   509  C CB  . SER   A 1 66  ? 26.248 -7.882  -1.312 1.00 10.47  ? 63  SER   A CB  1 
ATOM   510  O OG  . SER   A 1 66  ? 25.712 -8.968  -2.060 1.00 13.18  ? 63  SER   A OG  1 
ATOM   511  N N   . PHE   A 1 67  ? 27.279 -7.101  1.766  1.00 8.99   ? 64  PHE   A N   1 
ATOM   512  C CA  . PHE   A 1 67  ? 27.777 -6.127  2.727  1.00 8.13   ? 64  PHE   A CA  1 
ATOM   513  C C   . PHE   A 1 67  ? 29.167 -6.525  3.196  1.00 8.82   ? 64  PHE   A C   1 
ATOM   514  O O   . PHE   A 1 67  ? 29.575 -7.687  3.094  1.00 10.88  ? 64  PHE   A O   1 
ATOM   515  C CB  . PHE   A 1 67  ? 26.828 -6.029  3.927  1.00 9.86   ? 64  PHE   A CB  1 
ATOM   516  C CG  . PHE   A 1 67  ? 26.543 -7.359  4.563  1.00 10.83  ? 64  PHE   A CG  1 
ATOM   517  C CD1 . PHE   A 1 67  ? 25.528 -8.170  4.073  1.00 10.68  ? 64  PHE   A CD1 1 
ATOM   518  C CD2 . PHE   A 1 67  ? 27.306 -7.814  5.631  1.00 10.80  ? 64  PHE   A CD2 1 
ATOM   519  C CE1 . PHE   A 1 67  ? 25.271 -9.405  4.647  1.00 12.08  ? 64  PHE   A CE1 1 
ATOM   520  C CE2 . PHE   A 1 67  ? 27.062 -9.052  6.208  1.00 10.73  ? 64  PHE   A CE2 1 
ATOM   521  C CZ  . PHE   A 1 67  ? 26.035 -9.843  5.717  1.00 11.52  ? 64  PHE   A CZ  1 
ATOM   522  N N   . ILE   A 1 68  ? 29.863 -5.543  3.755  1.00 8.16   ? 65  ILE   A N   1 
ATOM   523  C CA  . ILE   A 1 68  ? 31.123 -5.744  4.459  1.00 9.10   ? 65  ILE   A CA  1 
ATOM   524  C C   . ILE   A 1 68  ? 30.831 -5.557  5.943  1.00 7.21   ? 65  ILE   A C   1 
ATOM   525  O O   . ILE   A 1 68  ? 30.115 -4.625  6.322  1.00 9.88   ? 65  ILE   A O   1 
ATOM   526  C CB  . ILE   A 1 68  ? 32.188 -4.746  3.962  1.00 11.27  ? 65  ILE   A CB  1 
ATOM   527  C CG1 . ILE   A 1 68  ? 32.454 -4.980  2.466  1.00 11.40  ? 65  ILE   A CG1 1 
ATOM   528  C CG2 . ILE   A 1 68  ? 33.458 -4.805  4.833  1.00 12.62  ? 65  ILE   A CG2 1 
ATOM   529  C CD1 . ILE   A 1 68  ? 33.452 -4.029  1.866  1.00 15.30  ? 65  ILE   A CD1 1 
ATOM   530  N N   . LEU   A 1 69  ? 31.341 -6.454  6.777  1.00 9.27   ? 66  LEU   A N   1 
ATOM   531  C CA  . LEU   A 1 69  ? 31.052 -6.359  8.205  1.00 8.25   ? 66  LEU   A CA  1 
ATOM   532  C C   . LEU   A 1 69  ? 31.513 -5.009  8.739  1.00 9.31   ? 66  LEU   A C   1 
ATOM   533  O O   . LEU   A 1 69  ? 32.650 -4.586  8.501  1.00 11.50  ? 66  LEU   A O   1 
ATOM   534  C CB  . LEU   A 1 69  ? 31.727 -7.498  8.981  1.00 9.82   ? 66  LEU   A CB  1 
ATOM   535  C CG  . LEU   A 1 69  ? 31.167 -8.909  8.717  1.00 10.56  ? 66  LEU   A CG  1 
ATOM   536  C CD1 . LEU   A 1 69  ? 32.095 -9.992  9.284  1.00 13.07  ? 66  LEU   A CD1 1 
ATOM   537  C CD2 . LEU   A 1 69  ? 29.731 -9.083  9.276  1.00 12.50  ? 66  LEU   A CD2 1 
ATOM   538  N N   . GLY   A 1 70  ? 30.615 -4.324  9.442  1.00 9.43   ? 67  GLY   A N   1 
ATOM   539  C CA  . GLY   A 1 70  ? 30.925 -3.040  10.049 1.00 8.99   ? 67  GLY   A CA  1 
ATOM   540  C C   . GLY   A 1 70  ? 30.679 -1.834  9.171  1.00 9.64   ? 67  GLY   A C   1 
ATOM   541  O O   . GLY   A 1 70  ? 30.778 -0.702  9.663  1.00 11.27  ? 67  GLY   A O   1 
ATOM   542  N N   . GLN   A 1 71  ? 30.324 -2.032  7.907  1.00 9.42   ? 68  GLN   A N   1 
ATOM   543  C CA  . GLN   A 1 71  ? 30.165 -0.943  6.956  1.00 9.05   ? 68  GLN   A CA  1 
ATOM   544  C C   . GLN   A 1 71  ? 28.684 -0.740  6.678  1.00 8.69   ? 68  GLN   A C   1 
ATOM   545  O O   . GLN   A 1 71  ? 28.023 -1.638  6.155  1.00 9.58   ? 68  GLN   A O   1 
ATOM   546  C CB  . GLN   A 1 71  ? 30.929 -1.266  5.675  1.00 10.11  ? 68  GLN   A CB  1 
ATOM   547  C CG  . GLN   A 1 71  ? 30.798 -0.202  4.626  1.00 11.12  ? 68  GLN   A CG  1 
ATOM   548  C CD  . GLN   A 1 71  ? 31.404 -0.640  3.318  1.00 13.35  ? 68  GLN   A CD  1 
ATOM   549  O OE1 . GLN   A 1 71  ? 30.774 -1.354  2.529  1.00 15.89  ? 68  GLN   A OE1 1 
ATOM   550  N NE2 . GLN   A 1 71  ? 32.645 -0.249  3.095  1.00 13.39  ? 68  GLN   A NE2 1 
ATOM   551  N N   . GLU   A 1 72  ? 28.169 0.442   7.004  1.00 9.01   ? 69  GLU   A N   1 
ATOM   552  C CA  . GLU   A 1 72  ? 26.748 0.687   6.810  1.00 7.76   ? 69  GLU   A CA  1 
ATOM   553  C C   . GLU   A 1 72  ? 26.428 0.686   5.322  1.00 7.79   ? 69  GLU   A C   1 
ATOM   554  O O   . GLU   A 1 72  ? 27.244 1.108   4.493  1.00 9.84   ? 69  GLU   A O   1 
ATOM   555  C CB  . GLU   A 1 72  ? 26.364 2.043   7.407  1.00 10.34  ? 69  GLU   A CB  1 
ATOM   556  C CG  . GLU   A 1 72  ? 24.848 2.279   7.410  1.00 8.66   ? 69  GLU   A CG  1 
ATOM   557  C CD  . GLU   A 1 72  ? 24.466 3.565   8.093  1.00 7.99   ? 69  GLU   A CD  1 
ATOM   558  O OE1 . GLU   A 1 72  ? 24.666 4.654   7.515  1.00 9.57   ? 69  GLU   A OE1 1 
ATOM   559  O OE2 . GLU   A 1 72  ? 24.096 3.500   9.288  1.00 11.52  ? 69  GLU   A OE2 1 
ATOM   560  N N   . PHE   A 1 73  ? 25.239 0.192   4.983  1.00 9.05   ? 70  PHE   A N   1 
ATOM   561  C CA  . PHE   A 1 73  ? 24.808 0.134   3.591  1.00 8.28   ? 70  PHE   A CA  1 
ATOM   562  C C   . PHE   A 1 73  ? 23.306 0.369   3.503  1.00 8.45   ? 70  PHE   A C   1 
ATOM   563  O O   . PHE   A 1 73  ? 22.576 0.265   4.494  1.00 11.40  ? 70  PHE   A O   1 
ATOM   564  C CB  . PHE   A 1 73  ? 25.180 -1.207  2.922  1.00 8.89   ? 70  PHE   A CB  1 
ATOM   565  C CG  . PHE   A 1 73  ? 24.517 -2.412  3.536  1.00 8.90   ? 70  PHE   A CG  1 
ATOM   566  C CD1 . PHE   A 1 73  ? 24.989 -2.937  4.727  1.00 9.27   ? 70  PHE   A CD1 1 
ATOM   567  C CD2 . PHE   A 1 73  ? 23.424 -3.013  2.923  1.00 10.63  ? 70  PHE   A CD2 1 
ATOM   568  C CE1 . PHE   A 1 73  ? 24.392 -4.056  5.305  1.00 10.69  ? 70  PHE   A CE1 1 
ATOM   569  C CE2 . PHE   A 1 73  ? 22.814 -4.127  3.497  1.00 11.02  ? 70  PHE   A CE2 1 
ATOM   570  C CZ  . PHE   A 1 73  ? 23.305 -4.657  4.675  1.00 12.04  ? 70  PHE   A CZ  1 
ATOM   571  N N   . ASP   A 1 74  ? 22.846 0.680   2.292  1.00 8.78   ? 71  ASP   A N   1 
ATOM   572  C CA  . ASP   A 1 74  ? 21.425 0.885   2.044  1.00 9.93   ? 71  ASP   A CA  1 
ATOM   573  C C   . ASP   A 1 74  ? 20.758 -0.438  1.714  1.00 10.60  ? 71  ASP   A C   1 
ATOM   574  O O   . ASP   A 1 74  ? 21.238 -1.184  0.859  1.00 13.64  ? 71  ASP   A O   1 
ATOM   575  C CB  . ASP   A 1 74  ? 21.232 1.842   0.877  1.00 8.75   ? 71  ASP   A CB  1 
ATOM   576  C CG  . ASP   A 1 74  ? 21.828 3.182   1.147  1.00 9.94   ? 71  ASP   A CG  1 
ATOM   577  O OD1 . ASP   A 1 74  ? 21.363 3.824   2.107  1.00 13.39  ? 71  ASP   A OD1 1 
ATOM   578  O OD2 . ASP   A 1 74  ? 22.776 3.571   0.427  1.00 13.00  ? 71  ASP   A OD2 1 
ATOM   579  N N   . GLU   A 1 75  ? 19.641 -0.710  2.384  1.00 10.11  ? 72  GLU   A N   1 
ATOM   580  C CA  . GLU   A 1 75  ? 18.862 -1.923  2.180  1.00 10.18  ? 72  GLU   A CA  1 
ATOM   581  C C   . GLU   A 1 75  ? 17.419 -1.517  1.935  1.00 11.86  ? 72  GLU   A C   1 
ATOM   582  O O   . GLU   A 1 75  ? 16.885 -0.656  2.642  1.00 12.12  ? 72  GLU   A O   1 
ATOM   583  C CB  . GLU   A 1 75  ? 18.951 -2.822  3.426  1.00 9.76   ? 72  GLU   A CB  1 
ATOM   584  C CG  . GLU   A 1 75  ? 18.101 -4.093  3.341  1.00 10.16  ? 72  GLU   A CG  1 
ATOM   585  C CD  . GLU   A 1 75  ? 18.203 -4.969  4.576  1.00 11.33  ? 72  GLU   A CD  1 
ATOM   586  O OE1 . GLU   A 1 75  ? 18.826 -4.560  5.575  1.00 11.23  ? 72  GLU   A OE1 1 
ATOM   587  O OE2 . GLU   A 1 75  ? 17.646 -6.080  4.546  1.00 13.53  ? 72  GLU   A OE2 1 
ATOM   588  N N   . VAL   A 1 76  ? 16.809 -2.095  0.908  1.00 12.57  ? 73  VAL   A N   1 
ATOM   589  C CA  . VAL   A 1 76  ? 15.373 -1.977  0.693  1.00 12.43  ? 73  VAL   A CA  1 
ATOM   590  C C   . VAL   A 1 76  ? 14.773 -3.309  1.118  1.00 14.00  ? 73  VAL   A C   1 
ATOM   591  O O   . VAL   A 1 76  ? 14.972 -4.331  0.448  1.00 16.48  ? 73  VAL   A O   1 
ATOM   592  C CB  . VAL   A 1 76  ? 15.031 -1.647  -0.765 1.00 15.63  ? 73  VAL   A CB  1 
ATOM   593  C CG1 . VAL   A 1 76  ? 13.516 -1.539  -0.948 1.00 18.16  ? 73  VAL   A CG1 1 
ATOM   594  C CG2 . VAL   A 1 76  ? 15.709 -0.359  -1.189 1.00 15.36  ? 73  VAL   A CG2 1 
ATOM   595  N N   . THR   A 1 77  ? 14.051 -3.305  2.237  1.00 12.42  ? 74  THR   A N   1 
ATOM   596  C CA  . THR   A 1 77  ? 13.573 -4.557  2.806  1.00 13.13  ? 74  THR   A CA  1 
ATOM   597  C C   . THR   A 1 77  ? 12.434 -5.135  1.964  1.00 13.97  ? 74  THR   A C   1 
ATOM   598  O O   . THR   A 1 77  ? 11.895 -4.491  1.058  1.00 15.08  ? 74  THR   A O   1 
ATOM   599  C CB  . THR   A 1 77  ? 13.110 -4.345  4.243  1.00 12.17  ? 74  THR   A CB  1 
ATOM   600  O OG1 . THR   A 1 77  ? 11.979 -3.467  4.254  1.00 13.08  ? 74  THR   A OG1 1 
ATOM   601  C CG2 . THR   A 1 77  ? 14.227 -3.735  5.093  1.00 12.74  ? 74  THR   A CG2 1 
ATOM   602  N N   . ALA   A 1 78  ? 12.056 -6.375  2.294  1.00 14.95  ? 75  ALA   A N   1 
ATOM   603  C CA  . ALA   A 1 78  ? 11.009 -7.060  1.545  1.00 18.18  ? 75  ALA   A CA  1 
ATOM   604  C C   . ALA   A 1 78  ? 9.674  -6.335  1.661  1.00 18.53  ? 75  ALA   A C   1 
ATOM   605  O O   . ALA   A 1 78  ? 8.829  -6.442  0.768  1.00 19.56  ? 75  ALA   A O   1 
ATOM   606  C CB  . ALA   A 1 78  ? 10.890 -8.510  2.018  1.00 20.43  ? 75  ALA   A CB  1 
ATOM   607  N N   . ASP   A 1 79  ? 9.464  -5.596  2.747  1.00 18.38  ? 76  ASP   A N   1 
ATOM   608  C CA  . ASP   A 1 79  ? 8.268  -4.787  2.930  1.00 15.60  ? 76  ASP   A CA  1 
ATOM   609  C C   . ASP   A 1 79  ? 8.456  -3.345  2.464  1.00 17.74  ? 76  ASP   A C   1 
ATOM   610  O O   . ASP   A 1 79  ? 7.625  -2.488  2.790  1.00 18.87  ? 76  ASP   A O   1 
ATOM   611  C CB  . ASP   A 1 79  ? 7.799  -4.848  4.386  1.00 16.01  ? 76  ASP   A CB  1 
ATOM   612  C CG  . ASP   A 1 79  ? 8.865  -4.374  5.365  1.00 13.21  ? 76  ASP   A CG  1 
ATOM   613  O OD1 . ASP   A 1 79  ? 10.014 -4.864  5.300  1.00 16.02  ? 76  ASP   A OD1 1 
ATOM   614  O OD2 . ASP   A 1 79  ? 8.552  -3.508  6.205  1.00 16.36  ? 76  ASP   A OD2 1 
ATOM   615  N N   A ASP   A 1 80  ? 9.535  -3.061  1.729  0.48 16.65  ? 77  ASP   A N   1 
ATOM   616  N N   B ASP   A 1 80  ? 9.541  -3.062  1.736  0.52 16.24  ? 77  ASP   A N   1 
ATOM   617  C CA  A ASP   A 1 80  ? 9.738  -1.783  1.041  0.48 17.81  ? 77  ASP   A CA  1 
ATOM   618  C CA  B ASP   A 1 80  ? 9.752  -1.787  1.042  0.52 17.15  ? 77  ASP   A CA  1 
ATOM   619  C C   A ASP   A 1 80  ? 10.092 -0.640  1.991  0.48 16.22  ? 77  ASP   A C   1 
ATOM   620  C C   B ASP   A 1 80  ? 10.109 -0.638  1.983  0.52 15.93  ? 77  ASP   A C   1 
ATOM   621  O O   A ASP   A 1 80  ? 9.755  0.518   1.731  0.48 18.91  ? 77  ASP   A O   1 
ATOM   622  O O   B ASP   A 1 80  ? 9.799  0.523   1.703  0.52 18.77  ? 77  ASP   A O   1 
ATOM   623  C CB  A ASP   A 1 80  ? 8.559  -1.405  0.133  0.48 21.06  ? 77  ASP   A CB  1 
ATOM   624  C CB  B ASP   A 1 80  ? 8.591  -1.414  0.111  0.52 20.05  ? 77  ASP   A CB  1 
ATOM   625  C CG  A ASP   A 1 80  ? 8.971  -0.507  -1.019 0.48 24.22  ? 77  ASP   A CG  1 
ATOM   626  C CG  B ASP   A 1 80  ? 8.471  -2.351  -1.074 0.52 23.35  ? 77  ASP   A CG  1 
ATOM   627  O OD1 A ASP   A 1 80  ? 10.178 -0.443  -1.329 0.48 24.86  ? 77  ASP   A OD1 1 
ATOM   628  O OD1 B ASP   A 1 80  ? 9.515  -2.693  -1.671 0.52 24.88  ? 77  ASP   A OD1 1 
ATOM   629  O OD2 A ASP   A 1 80  ? 8.087  0.150   -1.603 0.48 27.04  ? 77  ASP   A OD2 1 
ATOM   630  O OD2 B ASP   A 1 80  ? 7.334  -2.756  -1.399 0.52 25.54  ? 77  ASP   A OD2 1 
ATOM   631  N N   . ARG   A 1 81  ? 10.758 -0.937  3.100  1.00 13.28  ? 78  ARG   A N   1 
ATOM   632  C CA  . ARG   A 1 81  ? 11.364 0.108   3.912  1.00 11.43  ? 78  ARG   A CA  1 
ATOM   633  C C   . ARG   A 1 81  ? 12.743 0.401   3.349  1.00 12.88  ? 78  ARG   A C   1 
ATOM   634  O O   . ARG   A 1 81  ? 13.481 -0.516  2.977  1.00 13.96  ? 78  ARG   A O   1 
ATOM   635  C CB  . ARG   A 1 81  ? 11.527 -0.333  5.363  1.00 13.30  ? 78  ARG   A CB  1 
ATOM   636  C CG  . ARG   A 1 81  ? 10.257 -0.284  6.208  1.00 14.21  ? 78  ARG   A CG  1 
ATOM   637  C CD  . ARG   A 1 81  ? 10.481 -0.938  7.575  1.00 12.89  ? 78  ARG   A CD  1 
ATOM   638  N NE  . ARG   A 1 81  ? 10.652 -2.383  7.456  1.00 12.58  ? 78  ARG   A NE  1 
ATOM   639  C CZ  . ARG   A 1 81  ? 11.642 -3.099  7.974  1.00 11.25  ? 78  ARG   A CZ  1 
ATOM   640  N NH1 . ARG   A 1 81  ? 12.581 -2.550  8.740  1.00 12.18  ? 78  ARG   A NH1 1 
ATOM   641  N NH2 . ARG   A 1 81  ? 11.691 -4.406  7.714  1.00 12.03  ? 78  ARG   A NH2 1 
ATOM   642  N N   . LYS   A 1 82  ? 13.085 1.682   3.276  1.00 13.61  ? 79  LYS   A N   1 
ATOM   643  C CA  . LYS   A 1 82  ? 14.444 2.099   2.939  1.00 13.44  ? 79  LYS   A CA  1 
ATOM   644  C C   . LYS   A 1 82  ? 15.213 2.321   4.236  1.00 12.86  ? 79  LYS   A C   1 
ATOM   645  O O   . LYS   A 1 82  ? 14.982 3.311   4.940  1.00 15.03  ? 79  LYS   A O   1 
ATOM   646  C CB  . LYS   A 1 82  ? 14.436 3.368   2.090  1.00 16.02  ? 79  LYS   A CB  1 
ATOM   647  C CG  . LYS   A 1 82  ? 13.899 3.162   0.705  1.00 20.69  ? 79  LYS   A CG  1 
ATOM   648  C CD  . LYS   A 1 82  ? 13.839 4.474   -0.052 1.00 27.35  ? 79  LYS   A CD  1 
ATOM   649  C CE  . LYS   A 1 82  ? 13.578 4.233   -1.528 1.00 34.45  ? 79  LYS   A CE  1 
ATOM   650  N NZ  . LYS   A 1 82  ? 12.313 3.478   -1.744 1.00 39.73  ? 79  LYS   A NZ  1 
ATOM   651  N N   . VAL   A 1 83  ? 16.132 1.408   4.547  1.00 11.44  ? 80  VAL   A N   1 
ATOM   652  C CA  . VAL   A 1 83  ? 16.795 1.406   5.843  1.00 10.00  ? 80  VAL   A CA  1 
ATOM   653  C C   . VAL   A 1 83  ? 18.301 1.535   5.660  1.00 8.84   ? 80  VAL   A C   1 
ATOM   654  O O   . VAL   A 1 83  ? 18.858 1.223   4.603  1.00 11.00  ? 80  VAL   A O   1 
ATOM   655  C CB  . VAL   A 1 83  ? 16.428 0.165   6.690  1.00 9.73   ? 80  VAL   A CB  1 
ATOM   656  C CG1 . VAL   A 1 83  ? 14.909 0.004   6.738  1.00 11.44  ? 80  VAL   A CG1 1 
ATOM   657  C CG2 . VAL   A 1 83  ? 17.084 -1.104  6.138  1.00 9.85   ? 80  VAL   A CG2 1 
ATOM   658  N N   . LYS   A 1 84  ? 18.951 2.037   6.710  1.00 9.88   ? 81  LYS   A N   1 
ATOM   659  C CA  . LYS   A 1 84  ? 20.406 2.033   6.821  1.00 8.79   ? 81  LYS   A CA  1 
ATOM   660  C C   . LYS   A 1 84  ? 20.792 0.830   7.682  1.00 7.31   ? 81  LYS   A C   1 
ATOM   661  O O   . LYS   A 1 84  ? 20.407 0.741   8.862  1.00 9.36   ? 81  LYS   A O   1 
ATOM   662  C CB  . LYS   A 1 84  ? 20.897 3.340   7.453  1.00 9.20   ? 81  LYS   A CB  1 
ATOM   663  C CG  . LYS   A 1 84  ? 20.568 4.590   6.637  1.00 9.19   ? 81  LYS   A CG  1 
ATOM   664  C CD  . LYS   A 1 84  ? 21.433 4.707   5.399  1.00 9.49   ? 81  LYS   A CD  1 
ATOM   665  C CE  . LYS   A 1 84  ? 21.108 5.991   4.641  1.00 9.48   ? 81  LYS   A CE  1 
ATOM   666  N NZ  . LYS   A 1 84  ? 21.948 6.141   3.435  1.00 9.98   ? 81  LYS   A NZ  1 
ATOM   667  N N   . SER   A 1 85  ? 21.563 -0.084  7.101  1.00 9.61   ? 82  SER   A N   1 
ATOM   668  C CA  . SER   A 1 85  ? 21.878 -1.355  7.736  1.00 8.43   ? 82  SER   A CA  1 
ATOM   669  C C   . SER   A 1 85  ? 23.363 -1.470  8.058  1.00 9.47   ? 82  SER   A C   1 
ATOM   670  O O   . SER   A 1 85  ? 24.220 -1.131  7.235  1.00 10.09  ? 82  SER   A O   1 
ATOM   671  C CB  . SER   A 1 85  ? 21.471 -2.513  6.821  1.00 9.02   ? 82  SER   A CB  1 
ATOM   672  O OG  . SER   A 1 85  ? 20.060 -2.670  6.865  1.00 10.07  ? 82  SER   A OG  1 
ATOM   673  N N   . THR   A 1 86  ? 23.672 -2.010  9.240  1.00 7.49   ? 83  THR   A N   1 
ATOM   674  C CA  . THR   A 1 86  ? 25.042 -2.381  9.579  1.00 8.41   ? 83  THR   A CA  1 
ATOM   675  C C   . THR   A 1 86  ? 25.020 -3.765  10.200 1.00 8.68   ? 83  THR   A C   1 
ATOM   676  O O   . THR   A 1 86  ? 24.209 -4.034  11.094 1.00 10.05  ? 83  THR   A O   1 
ATOM   677  C CB  . THR   A 1 86  ? 25.675 -1.376  10.551 1.00 11.12  ? 83  THR   A CB  1 
ATOM   678  O OG1 . THR   A 1 86  ? 25.608 -0.066  9.976  1.00 14.18  ? 83  THR   A OG1 1 
ATOM   679  C CG2 . THR   A 1 86  ? 27.150 -1.718  10.800 1.00 13.88  ? 83  THR   A CG2 1 
ATOM   680  N N   . ILE   A 1 87  ? 25.904 -4.641  9.724  1.00 8.75   ? 84  ILE   A N   1 
ATOM   681  C CA  . ILE   A 1 87  ? 26.024 -6.009  10.225 1.00 7.13   ? 84  ILE   A CA  1 
ATOM   682  C C   . ILE   A 1 87  ? 27.439 -6.205  10.737 1.00 8.06   ? 84  ILE   A C   1 
ATOM   683  O O   . ILE   A 1 87  ? 28.409 -5.947  10.013 1.00 9.31   ? 84  ILE   A O   1 
ATOM   684  C CB  . ILE   A 1 87  ? 25.679 -7.055  9.146  1.00 9.27   ? 84  ILE   A CB  1 
ATOM   685  C CG1 . ILE   A 1 87  ? 24.290 -6.746  8.572  1.00 10.82  ? 84  ILE   A CG1 1 
ATOM   686  C CG2 . ILE   A 1 87  ? 25.747 -8.469  9.731  1.00 10.85  ? 84  ILE   A CG2 1 
ATOM   687  C CD1 . ILE   A 1 87  ? 23.835 -7.699  7.507  1.00 12.49  ? 84  ILE   A CD1 1 
ATOM   688  N N   . THR   A 1 88  ? 27.553 -6.653  11.981 1.00 8.24   ? 85  THR   A N   1 
ATOM   689  C CA  . THR   A 1 88  ? 28.836 -6.896  12.618 1.00 8.70   ? 85  THR   A CA  1 
ATOM   690  C C   . THR   A 1 88  ? 28.879 -8.333  13.118 1.00 10.76  ? 85  THR   A C   1 
ATOM   691  O O   . THR   A 1 88  ? 27.848 -8.991  13.268 1.00 10.89  ? 85  THR   A O   1 
ATOM   692  C CB  . THR   A 1 88  ? 29.060 -5.905  13.775 1.00 9.83   ? 85  THR   A CB  1 
ATOM   693  O OG1 . THR   A 1 88  ? 27.930 -5.932  14.662 1.00 11.36  ? 85  THR   A OG1 1 
ATOM   694  C CG2 . THR   A 1 88  ? 29.239 -4.472  13.237 1.00 11.26  ? 85  THR   A CG2 1 
ATOM   695  N N   A LEU   A 1 89  ? 30.088 -8.827  13.366 0.52 8.78   ? 86  LEU   A N   1 
ATOM   696  N N   B LEU   A 1 89  ? 30.089 -8.815  13.368 0.48 8.72   ? 86  LEU   A N   1 
ATOM   697  C CA  A LEU   A 1 89  ? 30.281 -10.163 13.929 0.52 9.63   ? 86  LEU   A CA  1 
ATOM   698  C CA  B LEU   A 1 89  ? 30.289 -10.142 13.936 0.48 9.61   ? 86  LEU   A CA  1 
ATOM   699  C C   A LEU   A 1 89  ? 30.666 -9.969  15.391 0.52 9.63   ? 86  LEU   A C   1 
ATOM   700  C C   B LEU   A 1 89  ? 30.668 -9.963  15.399 0.48 10.24  ? 86  LEU   A C   1 
ATOM   701  O O   A LEU   A 1 89  ? 31.717 -9.389  15.692 0.52 9.59   ? 86  LEU   A O   1 
ATOM   702  O O   B LEU   A 1 89  ? 31.718 -9.388  15.712 0.48 10.76  ? 86  LEU   A O   1 
ATOM   703  C CB  A LEU   A 1 89  ? 31.339 -10.938 13.140 0.52 11.01  ? 86  LEU   A CB  1 
ATOM   704  C CB  B LEU   A 1 89  ? 31.358 -10.907 13.162 0.48 10.04  ? 86  LEU   A CB  1 
ATOM   705  C CG  A LEU   A 1 89  ? 31.472 -12.468 13.253 0.52 12.91  ? 86  LEU   A CG  1 
ATOM   706  C CG  B LEU   A 1 89  ? 31.640 -12.281 13.758 0.48 10.72  ? 86  LEU   A CG  1 
ATOM   707  C CD1 A LEU   A 1 89  ? 31.774 -12.951 14.661 0.52 13.41  ? 86  LEU   A CD1 1 
ATOM   708  C CD1 B LEU   A 1 89  ? 30.383 -13.129 13.718 0.48 13.26  ? 86  LEU   A CD1 1 
ATOM   709  C CD2 A LEU   A 1 89  ? 30.233 -13.180 12.700 0.52 11.86  ? 86  LEU   A CD2 1 
ATOM   710  C CD2 B LEU   A 1 89  ? 32.752 -12.953 12.985 0.48 11.90  ? 86  LEU   A CD2 1 
ATOM   711  N N   . ASP   A 1 90  ? 29.791 -10.421 16.291 1.00 9.18   ? 87  ASP   A N   1 
ATOM   712  C CA  . ASP   A 1 90  ? 29.935 -10.221 17.726 1.00 9.43   ? 87  ASP   A CA  1 
ATOM   713  C C   . ASP   A 1 90  ? 29.681 -11.556 18.406 1.00 10.63  ? 87  ASP   A C   1 
ATOM   714  O O   . ASP   A 1 90  ? 28.565 -12.086 18.340 1.00 11.23  ? 87  ASP   A O   1 
ATOM   715  C CB  . ASP   A 1 90  ? 28.939 -9.168  18.212 1.00 10.43  ? 87  ASP   A CB  1 
ATOM   716  C CG  . ASP   A 1 90  ? 29.103 -7.848  17.487 1.00 14.08  ? 87  ASP   A CG  1 
ATOM   717  O OD1 . ASP   A 1 90  ? 30.231 -7.334  17.499 1.00 13.28  ? 87  ASP   A OD1 1 
ATOM   718  O OD2 . ASP   A 1 90  ? 28.124 -7.344  16.892 1.00 17.10  ? 87  ASP   A OD2 1 
ATOM   719  N N   . GLY   A 1 91  ? 30.716 -12.107 19.031 1.00 10.81  ? 88  GLY   A N   1 
ATOM   720  C CA  . GLY   A 1 91  ? 30.581 -13.369 19.735 1.00 9.75   ? 88  GLY   A CA  1 
ATOM   721  C C   . GLY   A 1 91  ? 30.064 -14.483 18.854 1.00 10.59  ? 88  GLY   A C   1 
ATOM   722  O O   . GLY   A 1 91  ? 29.182 -15.245 19.271 1.00 12.64  ? 88  GLY   A O   1 
ATOM   723  N N   . GLY   A 1 92  ? 30.565 -14.576 17.626 1.00 10.53  ? 89  GLY   A N   1 
ATOM   724  C CA  . GLY   A 1 92  ? 30.137 -15.632 16.732 1.00 12.02  ? 89  GLY   A CA  1 
ATOM   725  C C   . GLY   A 1 92  ? 28.750 -15.461 16.149 1.00 11.36  ? 89  GLY   A C   1 
ATOM   726  O O   . GLY   A 1 92  ? 28.258 -16.391 15.498 1.00 14.30  ? 89  GLY   A O   1 
ATOM   727  N N   . VAL   A 1 93  ? 28.118 -14.300 16.344 1.00 12.28  ? 90  VAL   A N   1 
ATOM   728  C CA  . VAL   A 1 93  ? 26.763 -14.012 15.879 1.00 12.88  ? 90  VAL   A CA  1 
ATOM   729  C C   . VAL   A 1 93  ? 26.818 -12.850 14.894 1.00 12.03  ? 90  VAL   A C   1 
ATOM   730  O O   . VAL   A 1 93  ? 27.548 -11.876 15.111 1.00 11.37  ? 90  VAL   A O   1 
ATOM   731  C CB  . VAL   A 1 93  ? 25.845 -13.674 17.075 1.00 12.31  ? 90  VAL   A CB  1 
ATOM   732  C CG1 . VAL   A 1 93  ? 24.451 -13.243 16.608 1.00 13.47  ? 90  VAL   A CG1 1 
ATOM   733  C CG2 . VAL   A 1 93  ? 25.748 -14.870 18.040 1.00 13.17  ? 90  VAL   A CG2 1 
ATOM   734  N N   . LEU   A 1 94  ? 26.060 -12.952 13.804 1.00 10.50  ? 91  LEU   A N   1 
ATOM   735  C CA  . LEU   A 1 94  ? 25.895 -11.818 12.898 1.00 9.23   ? 91  LEU   A CA  1 
ATOM   736  C C   . LEU   A 1 94  ? 24.792 -10.919 13.446 1.00 8.70   ? 91  LEU   A C   1 
ATOM   737  O O   . LEU   A 1 94  ? 23.633 -11.341 13.532 1.00 10.31  ? 91  LEU   A O   1 
ATOM   738  C CB  . LEU   A 1 94  ? 25.536 -12.301 11.493 1.00 9.60   ? 91  LEU   A CB  1 
ATOM   739  C CG  . LEU   A 1 94  ? 26.701 -12.987 10.779 1.00 10.02  ? 91  LEU   A CG  1 
ATOM   740  C CD1 . LEU   A 1 94  ? 26.216 -13.761 9.570  1.00 12.18  ? 91  LEU   A CD1 1 
ATOM   741  C CD2 . LEU   A 1 94  ? 27.785 -12.005 10.369 1.00 11.52  ? 91  LEU   A CD2 1 
ATOM   742  N N   . VAL   A 1 95  ? 25.154 -9.694  13.838 1.00 8.30   ? 92  VAL   A N   1 
ATOM   743  C CA  . VAL   A 1 95  ? 24.211 -8.748  14.430 1.00 7.92   ? 92  VAL   A CA  1 
ATOM   744  C C   . VAL   A 1 95  ? 23.915 -7.666  13.400 1.00 9.52   ? 92  VAL   A C   1 
ATOM   745  O O   . VAL   A 1 95  ? 24.811 -6.907  13.013 1.00 9.48   ? 92  VAL   A O   1 
ATOM   746  C CB  . VAL   A 1 95  ? 24.754 -8.143  15.736 1.00 9.00   ? 92  VAL   A CB  1 
ATOM   747  C CG1 . VAL   A 1 95  ? 23.714 -7.206  16.360 1.00 9.77   ? 92  VAL   A CG1 1 
ATOM   748  C CG2 . VAL   A 1 95  ? 25.146 -9.237  16.715 1.00 10.87  ? 92  VAL   A CG2 1 
ATOM   749  N N   . HIS   A 1 96  ? 22.662 -7.604  12.955 1.00 9.36   ? 93  HIS   A N   1 
ATOM   750  C CA  . HIS   A 1 96  ? 22.215 -6.730  11.871 1.00 8.33   ? 93  HIS   A CA  1 
ATOM   751  C C   . HIS   A 1 96  ? 21.239 -5.720  12.466 1.00 8.48   ? 93  HIS   A C   1 
ATOM   752  O O   . HIS   A 1 96  ? 20.174 -6.103  12.962 1.00 10.22  ? 93  HIS   A O   1 
ATOM   753  C CB  . HIS   A 1 96  ? 21.532 -7.606  10.804 1.00 7.73   ? 93  HIS   A CB  1 
ATOM   754  C CG  . HIS   A 1 96  ? 20.972 -6.871  9.623  1.00 8.64   ? 93  HIS   A CG  1 
ATOM   755  N ND1 . HIS   A 1 96  ? 20.347 -7.534  8.585  1.00 9.97   ? 93  HIS   A ND1 1 
ATOM   756  C CD2 . HIS   A 1 96  ? 20.939 -5.552  9.300  1.00 9.51   ? 93  HIS   A CD2 1 
ATOM   757  C CE1 . HIS   A 1 96  ? 19.930 -6.653  7.692  1.00 9.20   ? 93  HIS   A CE1 1 
ATOM   758  N NE2 . HIS   A 1 96  ? 20.286 -5.445  8.095  1.00 10.74  ? 93  HIS   A NE2 1 
ATOM   759  N N   A VAL   A 1 97  ? 21.593 -4.437  12.417 0.63 8.73   ? 94  VAL   A N   1 
ATOM   760  N N   B VAL   A 1 97  ? 21.596 -4.439  12.427 0.37 8.81   ? 94  VAL   A N   1 
ATOM   761  C CA  A VAL   A 1 97  ? 20.711 -3.356  12.854 0.63 8.76   ? 94  VAL   A CA  1 
ATOM   762  C CA  B VAL   A 1 97  ? 20.692 -3.371  12.846 0.37 8.83   ? 94  VAL   A CA  1 
ATOM   763  C C   A VAL   A 1 97  ? 20.233 -2.582  11.633 0.63 9.16   ? 94  VAL   A C   1 
ATOM   764  C C   B VAL   A 1 97  ? 20.223 -2.607  11.616 0.37 8.98   ? 94  VAL   A C   1 
ATOM   765  O O   A VAL   A 1 97  ? 21.042 -2.203  10.776 0.63 9.97   ? 94  VAL   A O   1 
ATOM   766  O O   B VAL   A 1 97  ? 21.025 -2.280  10.731 0.37 9.31   ? 94  VAL   A O   1 
ATOM   767  C CB  A VAL   A 1 97  ? 21.407 -2.414  13.854 0.63 9.45   ? 94  VAL   A CB  1 
ATOM   768  C CB  B VAL   A 1 97  ? 21.318 -2.434  13.896 0.37 9.25   ? 94  VAL   A CB  1 
ATOM   769  C CG1 A VAL   A 1 97  ? 20.468 -1.264  14.234 0.63 12.42  ? 94  VAL   A CG1 1 
ATOM   770  C CG1 B VAL   A 1 97  ? 22.542 -1.717  13.341 0.37 10.34  ? 94  VAL   A CG1 1 
ATOM   771  C CG2 A VAL   A 1 97  ? 21.873 -3.176  15.092 0.63 10.36  ? 94  VAL   A CG2 1 
ATOM   772  C CG2 B VAL   A 1 97  ? 20.274 -1.424  14.378 0.37 10.85  ? 94  VAL   A CG2 1 
ATOM   773  N N   . GLN   A 1 98  ? 18.919 -2.354  11.550 1.00 7.44   ? 95  GLN   A N   1 
ATOM   774  C CA  . GLN   A 1 98  ? 18.315 -1.535  10.511 1.00 8.35   ? 95  GLN   A CA  1 
ATOM   775  C C   . GLN   A 1 98  ? 17.770 -0.282  11.175 1.00 8.40   ? 95  GLN   A C   1 
ATOM   776  O O   . GLN   A 1 98  ? 17.022 -0.379  12.153 1.00 10.38  ? 95  GLN   A O   1 
ATOM   777  C CB  . GLN   A 1 98  ? 17.152 -2.271  9.847  1.00 9.89   ? 95  GLN   A CB  1 
ATOM   778  C CG  . GLN   A 1 98  ? 17.552 -3.525  9.061  1.00 9.84   ? 95  GLN   A CG  1 
ATOM   779  C CD  . GLN   A 1 98  ? 16.354 -4.286  8.532  1.00 10.50  ? 95  GLN   A CD  1 
ATOM   780  O OE1 . GLN   A 1 98  ? 15.248 -4.180  9.068  1.00 10.45  ? 95  GLN   A OE1 1 
ATOM   781  N NE2 . GLN   A 1 98  ? 16.567 -5.063  7.484  1.00 10.68  ? 95  GLN   A NE2 1 
ATOM   782  N N   . LYS   A 1 99  ? 18.130 0.884   10.636 1.00 9.49   ? 96  LYS   A N   1 
ATOM   783  C CA  . LYS   A 1 99  ? 17.705 2.175   11.167 1.00 10.61  ? 96  LYS   A CA  1 
ATOM   784  C C   . LYS   A 1 99  ? 16.957 2.945   10.084 1.00 9.32   ? 96  LYS   A C   1 
ATOM   785  O O   . LYS   A 1 99  ? 17.449 3.087   8.958  1.00 10.68  ? 96  LYS   A O   1 
ATOM   786  C CB  . LYS   A 1 99  ? 18.918 2.994   11.626 1.00 11.54  ? 96  LYS   A CB  1 
ATOM   787  C CG  . LYS   A 1 99  ? 19.693 2.334   12.757 1.00 9.78   ? 96  LYS   A CG  1 
ATOM   788  C CD  . LYS   A 1 99  ? 20.710 3.291   13.377 1.00 9.31   ? 96  LYS   A CD  1 
ATOM   789  C CE  . LYS   A 1 99  ? 21.870 3.627   12.453 1.00 8.52   ? 96  LYS   A CE  1 
ATOM   790  N NZ  . LYS   A 1 99  ? 22.817 4.575   13.123 1.00 10.23  ? 96  LYS   A NZ  1 
ATOM   791  N N   . TRP   A 1 100 ? 15.761 3.424   10.416 1.00 9.57   ? 97  TRP   A N   1 
ATOM   792  C CA  . TRP   A 1 100 ? 14.973 4.204   9.468  1.00 9.02   ? 97  TRP   A CA  1 
ATOM   793  C C   . TRP   A 1 100 ? 13.891 4.973   10.221 1.00 9.68   ? 97  TRP   A C   1 
ATOM   794  O O   . TRP   A 1 100 ? 13.324 4.467   11.194 1.00 11.43  ? 97  TRP   A O   1 
ATOM   795  C CB  . TRP   A 1 100 ? 14.328 3.276   8.417  1.00 11.33  ? 97  TRP   A CB  1 
ATOM   796  C CG  . TRP   A 1 100 ? 13.065 2.603   8.904  1.00 11.26  ? 97  TRP   A CG  1 
ATOM   797  C CD1 . TRP   A 1 100 ? 11.789 2.900   8.530  1.00 13.82  ? 97  TRP   A CD1 1 
ATOM   798  C CD2 . TRP   A 1 100 ? 12.963 1.531   9.862  1.00 9.74   ? 97  TRP   A CD2 1 
ATOM   799  N NE1 . TRP   A 1 100 ? 10.897 2.093   9.193  1.00 12.72  ? 97  TRP   A NE1 1 
ATOM   800  C CE2 . TRP   A 1 100 ? 11.586 1.238   10.016 1.00 11.76  ? 97  TRP   A CE2 1 
ATOM   801  C CE3 . TRP   A 1 100 ? 13.896 0.792   10.602 1.00 10.60  ? 97  TRP   A CE3 1 
ATOM   802  C CZ2 . TRP   A 1 100 ? 11.120 0.231   10.882 1.00 13.69  ? 97  TRP   A CZ2 1 
ATOM   803  C CZ3 . TRP   A 1 100 ? 13.434 -0.208  11.462 1.00 12.00  ? 97  TRP   A CZ3 1 
ATOM   804  C CH2 . TRP   A 1 100 ? 12.057 -0.478  11.592 1.00 12.24  ? 97  TRP   A CH2 1 
ATOM   805  N N   . ASP   A 1 101 ? 13.613 6.202   9.770  1.00 10.11  ? 98  ASP   A N   1 
ATOM   806  C CA  . ASP   A 1 101 ? 12.436 6.944   10.231 1.00 14.11  ? 98  ASP   A CA  1 
ATOM   807  C C   . ASP   A 1 101 ? 12.401 7.071   11.755 1.00 12.27  ? 98  ASP   A C   1 
ATOM   808  O O   . ASP   A 1 101 ? 11.335 6.995   12.371 1.00 14.14  ? 98  ASP   A O   1 
ATOM   809  C CB  . ASP   A 1 101 ? 11.143 6.309   9.698  1.00 16.71  ? 98  ASP   A CB  1 
ATOM   810  C CG  . ASP   A 1 101 ? 9.937  7.204   9.863  1.00 18.93  ? 98  ASP   A CG  1 
ATOM   811  O OD1 . ASP   A 1 101 ? 10.090 8.435   9.731  1.00 20.95  ? 98  ASP   A OD1 1 
ATOM   812  O OD2 . ASP   A 1 101 ? 8.836  6.675   10.134 1.00 23.11  ? 98  ASP   A OD2 1 
ATOM   813  N N   . GLY   A 1 102 ? 13.571 7.239   12.372 1.00 11.31  ? 99  GLY   A N   1 
ATOM   814  C CA  . GLY   A 1 102 ? 13.636 7.361   13.816 1.00 12.84  ? 99  GLY   A CA  1 
ATOM   815  C C   . GLY   A 1 102 ? 13.401 6.074   14.571 1.00 14.04  ? 99  GLY   A C   1 
ATOM   816  O O   . GLY   A 1 102 ? 13.113 6.113   15.777 1.00 14.34  ? 99  GLY   A O   1 
ATOM   817  N N   . LYS   A 1 103 ? 13.504 4.933   13.891 1.00 12.22  ? 100 LYS   A N   1 
ATOM   818  C CA  . LYS   A 1 103 ? 13.197 3.628   14.449 1.00 12.62  ? 100 LYS   A CA  1 
ATOM   819  C C   . LYS   A 1 103 ? 14.382 2.709   14.212 1.00 10.35  ? 100 LYS   A C   1 
ATOM   820  O O   . LYS   A 1 103 ? 15.289 3.006   13.428 1.00 11.44  ? 100 LYS   A O   1 
ATOM   821  C CB  . LYS   A 1 103 ? 11.957 3.002   13.788 1.00 14.57  ? 100 LYS   A CB  1 
ATOM   822  C CG  . LYS   A 1 103 ? 10.636 3.764   13.992 1.00 18.87  ? 100 LYS   A CG  1 
ATOM   823  C CD  . LYS   A 1 103 ? 9.581  3.235   13.001 1.00 23.18  ? 100 LYS   A CD  1 
ATOM   824  C CE  . LYS   A 1 103 ? 8.416  4.188   12.756 1.00 26.75  ? 100 LYS   A CE  1 
ATOM   825  N NZ  . LYS   A 1 103 ? 8.603  5.535   13.370 1.00 32.20  ? 100 LYS   A NZ  1 
ATOM   826  N N   A SER   A 1 104 ? 14.384 1.583   14.919 0.63 9.63   ? 101 SER   A N   1 
ATOM   827  N N   B SER   A 1 104 ? 14.351 1.553   14.872 0.37 10.82  ? 101 SER   A N   1 
ATOM   828  C CA  A SER   A 1 104 ? 15.406 0.579   14.679 0.63 11.31  ? 101 SER   A CA  1 
ATOM   829  C CA  B SER   A 1 104 ? 15.434 0.588   14.750 0.37 11.57  ? 101 SER   A CA  1 
ATOM   830  C C   A SER   A 1 104 ? 14.831 -0.801  14.949 0.63 9.73   ? 101 SER   A C   1 
ATOM   831  C C   B SER   A 1 104 ? 14.902 -0.810  15.032 0.37 10.71  ? 101 SER   A C   1 
ATOM   832  O O   A SER   A 1 104 ? 13.885 -0.960  15.723 0.63 12.63  ? 101 SER   A O   1 
ATOM   833  O O   B SER   A 1 104 ? 14.045 -0.991  15.901 0.37 12.09  ? 101 SER   A O   1 
ATOM   834  C CB  A SER   A 1 104 ? 16.663 0.806   15.530 0.63 15.01  ? 101 SER   A CB  1 
ATOM   835  C CB  B SER   A 1 104 ? 16.564 0.926   15.730 0.37 13.43  ? 101 SER   A CB  1 
ATOM   836  O OG  A SER   A 1 104 ? 16.449 0.432   16.876 0.63 15.31  ? 101 SER   A OG  1 
ATOM   837  O OG  B SER   A 1 104 ? 17.635 0.010   15.615 0.37 14.69  ? 101 SER   A OG  1 
ATOM   838  N N   . THR   A 1 105 ? 15.414 -1.795  14.295 1.00 10.24  ? 102 THR   A N   1 
ATOM   839  C CA  . THR   A 1 105 ? 15.108 -3.195  14.554 1.00 10.89  ? 102 THR   A CA  1 
ATOM   840  C C   . THR   A 1 105 ? 16.415 -3.966  14.436 1.00 10.10  ? 102 THR   A C   1 
ATOM   841  O O   . THR   A 1 105 ? 17.303 -3.580  13.675 1.00 10.10  ? 102 THR   A O   1 
ATOM   842  C CB  . THR   A 1 105 ? 14.014 -3.743  13.598 1.00 11.98  ? 102 THR   A CB  1 
ATOM   843  O OG1 . THR   A 1 105 ? 13.642 -5.072  13.992 1.00 12.61  ? 102 THR   A OG1 1 
ATOM   844  C CG2 . THR   A 1 105 ? 14.487 -3.787  12.164 1.00 11.08  ? 102 THR   A CG2 1 
ATOM   845  N N   . THR   A 1 106 ? 16.550 -5.040  15.213 1.00 10.23  ? 103 THR   A N   1 
ATOM   846  C CA  . THR   A 1 106 ? 17.766 -5.843  15.200 1.00 11.35  ? 103 THR   A CA  1 
ATOM   847  C C   . THR   A 1 106 ? 17.435 -7.264  14.764 1.00 11.02  ? 103 THR   A C   1 
ATOM   848  O O   . THR   A 1 106 ? 16.468 -7.857  15.246 1.00 13.53  ? 103 THR   A O   1 
ATOM   849  C CB  . THR   A 1 106 ? 18.444 -5.824  16.574 1.00 15.37  ? 103 THR   A CB  1 
ATOM   850  O OG1 . THR   A 1 106 ? 18.851 -4.486  16.890 1.00 17.35  ? 103 THR   A OG1 1 
ATOM   851  C CG2 . THR   A 1 106 ? 19.683 -6.679  16.573 1.00 17.54  ? 103 THR   A CG2 1 
ATOM   852  N N   . ILE   A 1 107 ? 18.228 -7.795  13.842 1.00 10.51  ? 104 ILE   A N   1 
ATOM   853  C CA  . ILE   A 1 107 ? 18.104 -9.164  13.344 1.00 9.14   ? 104 ILE   A CA  1 
ATOM   854  C C   . ILE   A 1 107 ? 19.404 -9.863  13.699 1.00 8.76   ? 104 ILE   A C   1 
ATOM   855  O O   . ILE   A 1 107 ? 20.470 -9.484  13.201 1.00 10.30  ? 104 ILE   A O   1 
ATOM   856  C CB  . ILE   A 1 107 ? 17.881 -9.189  11.826 1.00 9.20   ? 104 ILE   A CB  1 
ATOM   857  C CG1 . ILE   A 1 107 ? 16.629 -8.379  11.464 1.00 10.49  ? 104 ILE   A CG1 1 
ATOM   858  C CG2 . ILE   A 1 107 ? 17.789 -10.630 11.318 1.00 11.18  ? 104 ILE   A CG2 1 
ATOM   859  C CD1 . ILE   A 1 107 ? 16.506 -8.089  9.982  1.00 14.35  ? 104 ILE   A CD1 1 
ATOM   860  N N   . LYS   A 1 108 ? 19.334 -10.872 14.560 1.00 9.81   ? 105 LYS   A N   1 
ATOM   861  C CA  . LYS   A 1 108 ? 20.512 -11.653 14.917 1.00 10.71  ? 105 LYS   A CA  1 
ATOM   862  C C   . LYS   A 1 108 ? 20.447 -12.999 14.212 1.00 9.43   ? 105 LYS   A C   1 
ATOM   863  O O   . LYS   A 1 108 ? 19.442 -13.707 14.305 1.00 12.00  ? 105 LYS   A O   1 
ATOM   864  C CB  . LYS   A 1 108 ? 20.586 -11.853 16.429 1.00 11.82  ? 105 LYS   A CB  1 
ATOM   865  C CG  . LYS   A 1 108 ? 21.017 -10.601 17.191 1.00 13.92  ? 105 LYS   A CG  1 
ATOM   866  C CD  . LYS   A 1 108 ? 21.281 -10.865 18.655 1.00 18.10  ? 105 LYS   A CD  1 
ATOM   867  C CE  . LYS   A 1 108 ? 21.562 -9.551  19.373 1.00 23.54  ? 105 LYS   A CE  1 
ATOM   868  N NZ  . LYS   A 1 108 ? 21.837 -9.713  20.832 1.00 27.42  ? 105 LYS   A NZ  1 
ATOM   869  N N   . ARG   A 1 109 ? 21.506 -13.337 13.494 1.00 8.72   ? 106 ARG   A N   1 
ATOM   870  C CA  . ARG   A 1 109 ? 21.631 -14.622 12.824 1.00 8.82   ? 106 ARG   A CA  1 
ATOM   871  C C   . ARG   A 1 109 ? 22.716 -15.399 13.558 1.00 9.84   ? 106 ARG   A C   1 
ATOM   872  O O   . ARG   A 1 109 ? 23.876 -14.973 13.596 1.00 9.66   ? 106 ARG   A O   1 
ATOM   873  C CB  . ARG   A 1 109 ? 21.953 -14.425 11.338 1.00 9.60   ? 106 ARG   A CB  1 
ATOM   874  C CG  . ARG   A 1 109 ? 20.798 -13.741 10.556 1.00 9.80   ? 106 ARG   A CG  1 
ATOM   875  C CD  . ARG   A 1 109 ? 21.197 -13.305 9.148  1.00 10.45  ? 106 ARG   A CD  1 
ATOM   876  N NE  . ARG   A 1 109 ? 20.112 -12.697 8.378  1.00 12.70  ? 106 ARG   A NE  1 
ATOM   877  C CZ  . ARG   A 1 109 ? 19.937 -11.389 8.224  1.00 10.82  ? 106 ARG   A CZ  1 
ATOM   878  N NH1 . ARG   A 1 109 ? 20.693 -10.510 8.861  1.00 11.11  ? 106 ARG   A NH1 1 
ATOM   879  N NH2 . ARG   A 1 109 ? 18.972 -10.955 7.414  1.00 13.03  ? 106 ARG   A NH2 1 
ATOM   880  N N   . LYS   A 1 110 ? 22.332 -16.506 14.177 1.00 10.52  ? 107 LYS   A N   1 
ATOM   881  C CA  . LYS   A 1 110 ? 23.220 -17.237 15.063 1.00 11.60  ? 107 LYS   A CA  1 
ATOM   882  C C   . LYS   A 1 110 ? 23.174 -18.723 14.744 1.00 11.77  ? 107 LYS   A C   1 
ATOM   883  O O   . LYS   A 1 110 ? 22.267 -19.219 14.071 1.00 13.15  ? 107 LYS   A O   1 
ATOM   884  C CB  . LYS   A 1 110 ? 22.838 -17.035 16.533 1.00 16.50  ? 107 LYS   A CB  1 
ATOM   885  C CG  . LYS   A 1 110 ? 21.450 -17.538 16.876 1.00 19.64  ? 107 LYS   A CG  1 
ATOM   886  C CD  . LYS   A 1 110 ? 20.907 -16.921 18.182 1.00 26.87  ? 107 LYS   A CD  1 
ATOM   887  C CE  . LYS   A 1 110 ? 21.874 -17.084 19.350 1.00 31.48  ? 107 LYS   A CE  1 
ATOM   888  N NZ  . LYS   A 1 110 ? 21.564 -18.258 20.228 1.00 32.22  ? 107 LYS   A NZ  1 
ATOM   889  N N   . ARG   A 1 111 ? 24.174 -19.433 15.244 1.00 9.59   ? 108 ARG   A N   1 
ATOM   890  C CA  . ARG   A 1 111 ? 24.190 -20.883 15.165 1.00 7.71   ? 108 ARG   A CA  1 
ATOM   891  C C   . ARG   A 1 111 ? 23.755 -21.457 16.507 1.00 10.00  ? 108 ARG   A C   1 
ATOM   892  O O   . ARG   A 1 111 ? 24.183 -20.979 17.567 1.00 11.49  ? 108 ARG   A O   1 
ATOM   893  C CB  . ARG   A 1 111 ? 25.593 -21.366 14.808 1.00 9.00   ? 108 ARG   A CB  1 
ATOM   894  C CG  . ARG   A 1 111 ? 26.054 -21.004 13.387 1.00 10.11  ? 108 ARG   A CG  1 
ATOM   895  C CD  . ARG   A 1 111 ? 25.157 -21.670 12.328 1.00 10.28  ? 108 ARG   A CD  1 
ATOM   896  N NE  . ARG   A 1 111 ? 24.934 -23.078 12.644 1.00 11.38  ? 108 ARG   A NE  1 
ATOM   897  C CZ  . ARG   A 1 111 ? 25.806 -24.047 12.402 1.00 10.12  ? 108 ARG   A CZ  1 
ATOM   898  N NH1 . ARG   A 1 111 ? 26.911 -23.825 11.711 1.00 10.89  ? 108 ARG   A NH1 1 
ATOM   899  N NH2 . ARG   A 1 111 ? 25.579 -25.264 12.894 1.00 10.31  ? 108 ARG   A NH2 1 
ATOM   900  N N   . GLU   A 1 112 ? 22.872 -22.451 16.457 1.00 10.82  ? 109 GLU   A N   1 
ATOM   901  C CA  . GLU   A 1 112 ? 22.506 -23.242 17.624 1.00 10.97  ? 109 GLU   A CA  1 
ATOM   902  C C   . GLU   A 1 112 ? 22.408 -24.678 17.148 1.00 12.15  ? 109 GLU   A C   1 
ATOM   903  O O   . GLU   A 1 112 ? 21.748 -24.936 16.139 1.00 12.69  ? 109 GLU   A O   1 
ATOM   904  C CB  . GLU   A 1 112 ? 21.151 -22.821 18.223 1.00 13.15  ? 109 GLU   A CB  1 
ATOM   905  C CG  . GLU   A 1 112 ? 21.044 -21.353 18.625 1.00 18.00  ? 109 GLU   A CG  1 
ATOM   906  C CD  . GLU   A 1 112 ? 19.709 -21.017 19.271 1.00 24.23  ? 109 GLU   A CD  1 
ATOM   907  O OE1 . GLU   A 1 112 ? 18.830 -21.908 19.359 1.00 24.45  ? 109 GLU   A OE1 1 
ATOM   908  O OE2 . GLU   A 1 112 ? 19.535 -19.846 19.677 1.00 28.40  ? 109 GLU   A OE2 1 
ATOM   909  N N   . ASP   A 1 113 ? 23.077 -25.601 17.843 1.00 11.15  ? 110 ASP   A N   1 
ATOM   910  C CA  . ASP   A 1 113 ? 23.094 -27.012 17.425 1.00 12.73  ? 110 ASP   A CA  1 
ATOM   911  C C   . ASP   A 1 113 ? 23.559 -27.066 15.971 1.00 12.05  ? 110 ASP   A C   1 
ATOM   912  O O   . ASP   A 1 113 ? 24.589 -26.462 15.632 1.00 13.14  ? 110 ASP   A O   1 
ATOM   913  C CB  . ASP   A 1 113 ? 21.727 -27.632 17.669 1.00 14.27  ? 110 ASP   A CB  1 
ATOM   914  C CG  . ASP   A 1 113 ? 21.377 -27.753 19.119 1.00 16.10  ? 110 ASP   A CG  1 
ATOM   915  O OD1 . ASP   A 1 113 ? 22.279 -27.769 19.973 1.00 19.60  ? 110 ASP   A OD1 1 
ATOM   916  O OD2 . ASP   A 1 113 ? 20.168 -27.831 19.394 1.00 18.89  ? 110 ASP   A OD2 1 
ATOM   917  N N   . ASP   A 1 114 ? 22.835 -27.757 15.092 1.00 10.48  ? 111 ASP   A N   1 
ATOM   918  C CA  . ASP   A 1 114 ? 23.116 -27.804 13.668 1.00 9.48   ? 111 ASP   A CA  1 
ATOM   919  C C   . ASP   A 1 114 ? 22.292 -26.785 12.884 1.00 9.50   ? 111 ASP   A C   1 
ATOM   920  O O   . ASP   A 1 114 ? 22.286 -26.824 11.650 1.00 9.68   ? 111 ASP   A O   1 
ATOM   921  C CB  . ASP   A 1 114 ? 22.886 -29.223 13.126 1.00 9.95   ? 111 ASP   A CB  1 
ATOM   922  C CG  . ASP   A 1 114 ? 21.482 -29.743 13.386 1.00 10.88  ? 111 ASP   A CG  1 
ATOM   923  O OD1 . ASP   A 1 114 ? 20.663 -29.043 14.015 1.00 11.43  ? 111 ASP   A OD1 1 
ATOM   924  O OD2 . ASP   A 1 114 ? 21.195 -30.877 12.950 1.00 10.96  ? 111 ASP   A OD2 1 
ATOM   925  N N   . LYS   A 1 115 ? 21.624 -25.860 13.577 1.00 9.27   ? 112 LYS   A N   1 
ATOM   926  C CA  . LYS   A 1 115 ? 20.665 -24.944 12.978 1.00 8.30   ? 112 LYS   A CA  1 
ATOM   927  C C   . LYS   A 1 115 ? 21.252 -23.548 12.798 1.00 7.78   ? 112 LYS   A C   1 
ATOM   928  O O   . LYS   A 1 115 ? 22.229 -23.151 13.447 1.00 9.06   ? 112 LYS   A O   1 
ATOM   929  C CB  . LYS   A 1 115 ? 19.416 -24.780 13.861 1.00 10.70  ? 112 LYS   A CB  1 
ATOM   930  C CG  . LYS   A 1 115 ? 18.755 -26.058 14.339 1.00 10.43  ? 112 LYS   A CG  1 
ATOM   931  C CD  . LYS   A 1 115 ? 18.174 -26.830 13.174 1.00 10.13  ? 112 LYS   A CD  1 
ATOM   932  C CE  . LYS   A 1 115 ? 17.242 -27.933 13.661 1.00 12.27  ? 112 LYS   A CE  1 
ATOM   933  N NZ  . LYS   A 1 115 ? 17.946 -28.799 14.656 1.00 11.66  ? 112 LYS   A NZ  1 
ATOM   934  N N   A LEU   A 1 116 ? 20.626 -22.793 11.903 0.56 8.50   ? 113 LEU   A N   1 
ATOM   935  N N   B LEU   A 1 116 ? 20.621 -22.801 11.893 0.44 7.29   ? 113 LEU   A N   1 
ATOM   936  C CA  A LEU   A 1 116 ? 20.807 -21.351 11.826 0.56 9.45   ? 113 LEU   A CA  1 
ATOM   937  C CA  B LEU   A 1 116 ? 20.762 -21.355 11.783 0.44 7.38   ? 113 LEU   A CA  1 
ATOM   938  C C   A LEU   A 1 116 ? 19.510 -20.737 12.331 0.56 8.69   ? 113 LEU   A C   1 
ATOM   939  C C   B LEU   A 1 116 ? 19.483 -20.757 12.350 0.44 8.14   ? 113 LEU   A C   1 
ATOM   940  O O   A LEU   A 1 116 ? 18.432 -21.023 11.793 0.56 10.42  ? 113 LEU   A O   1 
ATOM   941  O O   B LEU   A 1 116 ? 18.386 -21.074 11.875 0.44 11.23  ? 113 LEU   A O   1 
ATOM   942  C CB  A LEU   A 1 116 ? 21.109 -20.914 10.392 0.56 12.03  ? 113 LEU   A CB  1 
ATOM   943  C CB  B LEU   A 1 116 ? 20.912 -20.952 10.318 0.44 8.38   ? 113 LEU   A CB  1 
ATOM   944  C CG  A LEU   A 1 116 ? 21.668 -19.495 10.210 0.56 10.28  ? 113 LEU   A CG  1 
ATOM   945  C CG  B LEU   A 1 116 ? 20.911 -19.445 10.051 0.44 7.34   ? 113 LEU   A CG  1 
ATOM   946  C CD1 A LEU   A 1 116 ? 22.299 -19.346 8.840  0.56 12.25  ? 113 LEU   A CD1 1 
ATOM   947  C CD1 B LEU   A 1 116 ? 22.107 -18.787 10.712 0.44 10.28  ? 113 LEU   A CD1 1 
ATOM   948  C CD2 A LEU   A 1 116 ? 20.602 -18.434 10.394 0.56 11.91  ? 113 LEU   A CD2 1 
ATOM   949  C CD2 B LEU   A 1 116 ? 20.895 -19.178 8.547  0.44 9.41   ? 113 LEU   A CD2 1 
ATOM   950  N N   . VAL   A 1 117 ? 19.616 -19.909 13.369 1.00 8.94   ? 114 VAL   A N   1 
ATOM   951  C CA  . VAL   A 1 117 ? 18.472 -19.290 14.029 1.00 8.46   ? 114 VAL   A CA  1 
ATOM   952  C C   . VAL   A 1 117 ? 18.491 -17.795 13.741 1.00 9.40   ? 114 VAL   A C   1 
ATOM   953  O O   . VAL   A 1 117 ? 19.520 -17.125 13.921 1.00 10.82  ? 114 VAL   A O   1 
ATOM   954  C CB  . VAL   A 1 117 ? 18.464 -19.566 15.542 1.00 9.14   ? 114 VAL   A CB  1 
ATOM   955  C CG1 . VAL   A 1 117 ? 17.268 -18.878 16.188 1.00 12.35  ? 114 VAL   A CG1 1 
ATOM   956  C CG2 . VAL   A 1 117 ? 18.418 -21.066 15.817 1.00 11.09  ? 114 VAL   A CG2 1 
ATOM   957  N N   . VAL   A 1 118 ? 17.353 -17.268 13.307 1.00 9.77   ? 115 VAL   A N   1 
ATOM   958  C CA  . VAL   A 1 118 ? 17.199 -15.846 13.028 1.00 11.50  ? 115 VAL   A CA  1 
ATOM   959  C C   . VAL   A 1 118 ? 16.254 -15.273 14.072 1.00 10.32  ? 115 VAL   A C   1 
ATOM   960  O O   . VAL   A 1 118 ? 15.084 -15.665 14.135 1.00 12.80  ? 115 VAL   A O   1 
ATOM   961  C CB  . VAL   A 1 118 ? 16.669 -15.592 11.610 1.00 13.73  ? 115 VAL   A CB  1 
ATOM   962  C CG1 . VAL   A 1 118 ? 16.681 -14.093 11.341 1.00 26.67  ? 115 VAL   A CG1 1 
ATOM   963  C CG2 . VAL   A 1 118 ? 17.499 -16.330 10.570 1.00 14.15  ? 115 VAL   A CG2 1 
ATOM   964  N N   . GLU   A 1 119 ? 16.764 -14.363 14.896 1.00 10.23  ? 116 GLU   A N   1 
ATOM   965  C CA  . GLU   A 1 119 ? 16.007 -13.696 15.949 1.00 10.73  ? 116 GLU   A CA  1 
ATOM   966  C C   . GLU   A 1 119 ? 15.816 -12.236 15.556 1.00 10.03  ? 116 GLU   A C   1 
ATOM   967  O O   . GLU   A 1 119 ? 16.796 -11.498 15.407 1.00 11.43  ? 116 GLU   A O   1 
ATOM   968  C CB  . GLU   A 1 119 ? 16.786 -13.737 17.257 1.00 16.58  ? 116 GLU   A CB  1 
ATOM   969  C CG  . GLU   A 1 119 ? 16.019 -14.201 18.457 1.00 27.94  ? 116 GLU   A CG  1 
ATOM   970  C CD  . GLU   A 1 119 ? 16.945 -14.509 19.618 1.00 33.81  ? 116 GLU   A CD  1 
ATOM   971  O OE1 . GLU   A 1 119 ? 17.635 -13.571 20.074 1.00 38.22  ? 116 GLU   A OE1 1 
ATOM   972  O OE2 . GLU   A 1 119 ? 16.994 -15.673 20.068 1.00 36.74  ? 116 GLU   A OE2 1 
ATOM   973  N N   . CYS   A 1 120 ? 14.562 -11.808 15.425 1.00 10.64  ? 117 CYS   A N   1 
ATOM   974  C CA  . CYS   A 1 120 ? 14.228 -10.450 15.006 1.00 11.59  ? 117 CYS   A CA  1 
ATOM   975  C C   . CYS   A 1 120 ? 13.507 -9.769  16.153 1.00 10.20  ? 117 CYS   A C   1 
ATOM   976  O O   . CYS   A 1 120 ? 12.562 -10.334 16.710 1.00 13.83  ? 117 CYS   A O   1 
ATOM   977  C CB  . CYS   A 1 120 ? 13.302 -10.474 13.789 1.00 14.41  ? 117 CYS   A CB  1 
ATOM   978  S SG  . CYS   A 1 120 ? 13.949 -11.321 12.362 1.00 17.09  ? 117 CYS   A SG  1 
ATOM   979  N N   . VAL   A 1 121 ? 13.923 -8.550  16.493 1.00 10.21  ? 118 VAL   A N   1 
ATOM   980  C CA  . VAL   A 1 121 ? 13.364 -7.831  17.635 1.00 11.45  ? 118 VAL   A CA  1 
ATOM   981  C C   . VAL   A 1 121 ? 12.922 -6.441  17.189 1.00 11.08  ? 118 VAL   A C   1 
ATOM   982  O O   . VAL   A 1 121 ? 13.691 -5.718  16.548 1.00 11.99  ? 118 VAL   A O   1 
ATOM   983  C CB  . VAL   A 1 121 ? 14.371 -7.751  18.803 1.00 13.33  ? 118 VAL   A CB  1 
ATOM   984  C CG1 . VAL   A 1 121 ? 13.746 -7.041  19.992 1.00 14.24  ? 118 VAL   A CG1 1 
ATOM   985  C CG2 . VAL   A 1 121 ? 14.851 -9.155  19.208 1.00 14.07  ? 118 VAL   A CG2 1 
ATOM   986  N N   . MET   A 1 122 ? 11.691 -6.064  17.538 1.00 12.61  ? 119 MET   A N   1 
ATOM   987  C CA  . MET   A 1 122 ? 11.173 -4.722  17.270 1.00 15.15  ? 119 MET   A CA  1 
ATOM   988  C C   . MET   A 1 122 ? 10.364 -4.344  18.501 1.00 16.76  ? 119 MET   A C   1 
ATOM   989  O O   . MET   A 1 122 ? 9.399  -5.041  18.834 1.00 17.13  ? 119 MET   A O   1 
ATOM   990  C CB  . MET   A 1 122 ? 10.235 -4.754  16.054 1.00 16.86  ? 119 MET   A CB  1 
ATOM   991  C CG  . MET   A 1 122 ? 9.618  -3.416  15.610 1.00 19.65  ? 119 MET   A CG  1 
ATOM   992  S SD  . MET   A 1 122 ? 10.877 -2.152  15.347 1.00 20.80  ? 119 MET   A SD  1 
ATOM   993  C CE  . MET   A 1 122 ? 9.931  -0.693  14.931 1.00 21.10  ? 119 MET   A CE  1 
ATOM   994  N N   . LYS   A 1 123 ? 10.768 -3.271  19.182 1.00 18.72  ? 120 LYS   A N   1 
ATOM   995  C CA  . LYS   A 1 123 ? 10.077 -2.748  20.370 1.00 23.11  ? 120 LYS   A CA  1 
ATOM   996  C C   . LYS   A 1 123 ? 9.604  -3.852  21.319 1.00 23.70  ? 120 LYS   A C   1 
ATOM   997  O O   . LYS   A 1 123 ? 8.438  -3.923  21.710 1.00 25.31  ? 120 LYS   A O   1 
ATOM   998  C CB  . LYS   A 1 123 ? 8.943  -1.784  20.006 1.00 29.38  ? 120 LYS   A CB  1 
ATOM   999  C CG  . LYS   A 1 123 ? 9.403  -0.493  19.327 1.00 34.97  ? 120 LYS   A CG  1 
ATOM   1000 C CD  . LYS   A 1 123 ? 10.770 -0.033  19.848 1.00 39.03  ? 120 LYS   A CD  1 
ATOM   1001 C CE  . LYS   A 1 123 ? 10.654 0.871   21.068 1.00 40.28  ? 120 LYS   A CE  1 
ATOM   1002 N NZ  . LYS   A 1 123 ? 10.251 2.259   20.706 1.00 41.75  ? 120 LYS   A NZ  1 
ATOM   1003 N N   . GLY   A 1 124 ? 10.529 -4.730  21.697 1.00 18.62  ? 121 GLY   A N   1 
ATOM   1004 C CA  . GLY   A 1 124 ? 10.227 -5.760  22.678 1.00 19.71  ? 121 GLY   A CA  1 
ATOM   1005 C C   . GLY   A 1 124 ? 9.473  -6.982  22.178 1.00 16.71  ? 121 GLY   A C   1 
ATOM   1006 O O   . GLY   A 1 124 ? 9.227  -7.897  22.976 1.00 20.88  ? 121 GLY   A O   1 
ATOM   1007 N N   . VAL   A 1 125 ? 9.075  -7.035  20.907 1.00 15.23  ? 122 VAL   A N   1 
ATOM   1008 C CA  . VAL   A 1 125 ? 8.501  -8.250  20.327 1.00 14.83  ? 122 VAL   A CA  1 
ATOM   1009 C C   . VAL   A 1 125 ? 9.606  -9.010  19.607 1.00 11.61  ? 122 VAL   A C   1 
ATOM   1010 O O   . VAL   A 1 125 ? 10.331 -8.433  18.787 1.00 12.76  ? 122 VAL   A O   1 
ATOM   1011 C CB  . VAL   A 1 125 ? 7.349  -7.915  19.367 1.00 17.50  ? 122 VAL   A CB  1 
ATOM   1012 C CG1 . VAL   A 1 125 ? 6.858  -9.178  18.687 1.00 20.36  ? 122 VAL   A CG1 1 
ATOM   1013 C CG2 . VAL   A 1 125 ? 6.216  -7.267  20.138 1.00 19.41  ? 122 VAL   A CG2 1 
ATOM   1014 N N   . THR   A 1 126 ? 9.737  -10.302 19.905 1.00 13.46  ? 123 THR   A N   1 
ATOM   1015 C CA  . THR   A 1 126 ? 10.819 -11.114 19.358 1.00 12.64  ? 123 THR   A CA  1 
ATOM   1016 C C   . THR   A 1 126 ? 10.248 -12.252 18.523 1.00 13.24  ? 123 THR   A C   1 
ATOM   1017 O O   . THR   A 1 126 ? 9.384  -13.005 18.992 1.00 15.72  ? 123 THR   A O   1 
ATOM   1018 C CB  . THR   A 1 126 ? 11.671 -11.719 20.478 1.00 14.34  ? 123 THR   A CB  1 
ATOM   1019 O OG1 . THR   A 1 126 ? 12.266 -10.672 21.255 1.00 16.48  ? 123 THR   A OG1 1 
ATOM   1020 C CG2 . THR   A 1 126 ? 12.785 -12.598 19.887 1.00 17.96  ? 123 THR   A CG2 1 
ATOM   1021 N N   . SER   A 1 127 ? 10.748 -12.392 17.303 1.00 11.31  ? 124 SER   A N   1 
ATOM   1022 C CA  . SER   A 1 127 ? 10.436 -13.529 16.450 1.00 10.91  ? 124 SER   A CA  1 
ATOM   1023 C C   . SER   A 1 127 ? 11.659 -14.430 16.358 1.00 11.35  ? 124 SER   A C   1 
ATOM   1024 O O   . SER   A 1 127 ? 12.788 -13.940 16.246 1.00 12.48  ? 124 SER   A O   1 
ATOM   1025 C CB  . SER   A 1 127 ? 10.070 -13.051 15.046 1.00 12.53  ? 124 SER   A CB  1 
ATOM   1026 O OG  . SER   A 1 127 ? 9.911  -14.140 14.157 1.00 18.08  ? 124 SER   A OG  1 
ATOM   1027 N N   . THR   A 1 128 ? 11.435 -15.746 16.385 1.00 11.02  ? 125 THR   A N   1 
ATOM   1028 C CA  . THR   A 1 128 ? 12.513 -16.723 16.280 1.00 10.48  ? 125 THR   A CA  1 
ATOM   1029 C C   . THR   A 1 128 ? 12.208 -17.667 15.129 1.00 9.02   ? 125 THR   A C   1 
ATOM   1030 O O   . THR   A 1 128 ? 11.177 -18.354 15.144 1.00 11.77  ? 125 THR   A O   1 
ATOM   1031 C CB  . THR   A 1 128 ? 12.647 -17.505 17.593 1.00 10.44  ? 125 THR   A CB  1 
ATOM   1032 O OG1 . THR   A 1 128 ? 12.835 -16.588 18.678 1.00 11.86  ? 125 THR   A OG1 1 
ATOM   1033 C CG2 . THR   A 1 128 ? 13.826 -18.483 17.537 1.00 12.46  ? 125 THR   A CG2 1 
ATOM   1034 N N   . ARG   A 1 129 ? 13.113 -17.734 14.152 1.00 8.18   ? 126 ARG   A N   1 
ATOM   1035 C CA  . ARG   A 1 129 ? 12.939 -18.598 12.991 1.00 8.06   ? 126 ARG   A CA  1 
ATOM   1036 C C   . ARG   A 1 129 ? 14.129 -19.541 12.901 1.00 9.01   ? 126 ARG   A C   1 
ATOM   1037 O O   . ARG   A 1 129 ? 15.281 -19.095 12.920 1.00 11.93  ? 126 ARG   A O   1 
ATOM   1038 C CB  . ARG   A 1 129 ? 12.774 -17.774 11.704 1.00 11.25  ? 126 ARG   A CB  1 
ATOM   1039 C CG  . ARG   A 1 129 ? 11.403 -17.093 11.657 1.00 13.65  ? 126 ARG   A CG  1 
ATOM   1040 C CD  . ARG   A 1 129 ? 11.331 -15.931 10.677 1.00 16.87  ? 126 ARG   A CD  1 
ATOM   1041 N NE  . ARG   A 1 129 ? 11.375 -16.335 9.275  1.00 16.99  ? 126 ARG   A NE  1 
ATOM   1042 C CZ  . ARG   A 1 129 ? 10.334 -16.795 8.590  1.00 18.72  ? 126 ARG   A CZ  1 
ATOM   1043 N NH1 . ARG   A 1 129 ? 9.182  -17.073 9.182  1.00 19.41  ? 126 ARG   A NH1 1 
ATOM   1044 N NH2 . ARG   A 1 129 ? 10.451 -16.980 7.278  1.00 19.97  ? 126 ARG   A NH2 1 
ATOM   1045 N N   . VAL   A 1 130 ? 13.851 -20.838 12.811 1.00 9.17   ? 127 VAL   A N   1 
ATOM   1046 C CA  . VAL   A 1 130 ? 14.878 -21.873 12.834 1.00 8.77   ? 127 VAL   A CA  1 
ATOM   1047 C C   . VAL   A 1 130 ? 15.021 -22.443 11.432 1.00 8.69   ? 127 VAL   A C   1 
ATOM   1048 O O   . VAL   A 1 130 ? 14.022 -22.831 10.810 1.00 10.21  ? 127 VAL   A O   1 
ATOM   1049 C CB  . VAL   A 1 130 ? 14.521 -22.989 13.830 1.00 8.88   ? 127 VAL   A CB  1 
ATOM   1050 C CG1 . VAL   A 1 130 ? 15.573 -24.096 13.778 1.00 12.12  ? 127 VAL   A CG1 1 
ATOM   1051 C CG2 . VAL   A 1 130 ? 14.390 -22.433 15.238 1.00 10.76  ? 127 VAL   A CG2 1 
ATOM   1052 N N   . TYR   A 1 131 ? 16.268 -22.515 10.950 1.00 8.60   ? 128 TYR   A N   1 
ATOM   1053 C CA  . TYR   A 1 131 ? 16.591 -23.082 9.649  1.00 8.35   ? 128 TYR   A CA  1 
ATOM   1054 C C   . TYR   A 1 131 ? 17.504 -24.291 9.841  1.00 8.53   ? 128 TYR   A C   1 
ATOM   1055 O O   . TYR   A 1 131 ? 18.378 -24.288 10.720 1.00 10.09  ? 128 TYR   A O   1 
ATOM   1056 C CB  . TYR   A 1 131 ? 17.329 -22.067 8.775  1.00 10.23  ? 128 TYR   A CB  1 
ATOM   1057 C CG  . TYR   A 1 131 ? 16.478 -20.938 8.236  1.00 9.87   ? 128 TYR   A CG  1 
ATOM   1058 C CD1 . TYR   A 1 131 ? 16.092 -19.874 9.048  1.00 12.00  ? 128 TYR   A CD1 1 
ATOM   1059 C CD2 . TYR   A 1 131 ? 16.080 -20.926 6.910  1.00 9.67   ? 128 TYR   A CD2 1 
ATOM   1060 C CE1 . TYR   A 1 131 ? 15.306 -18.829 8.548  1.00 12.31  ? 128 TYR   A CE1 1 
ATOM   1061 C CE2 . TYR   A 1 131 ? 15.302 -19.890 6.391  1.00 13.94  ? 128 TYR   A CE2 1 
ATOM   1062 C CZ  . TYR   A 1 131 ? 14.919 -18.845 7.215  1.00 12.90  ? 128 TYR   A CZ  1 
ATOM   1063 O OH  . TYR   A 1 131 ? 14.156 -17.820 6.696  1.00 15.77  ? 128 TYR   A OH  1 
ATOM   1064 N N   . GLU   A 1 132 ? 17.303 -25.315 9.010  1.00 9.22   ? 129 GLU   A N   1 
ATOM   1065 C CA  . GLU   A 1 132 ? 18.202 -26.457 8.908  1.00 9.40   ? 129 GLU   A CA  1 
ATOM   1066 C C   . GLU   A 1 132 ? 18.918 -26.394 7.565  1.00 8.26   ? 129 GLU   A C   1 
ATOM   1067 O O   . GLU   A 1 132 ? 18.503 -25.687 6.649  1.00 9.04   ? 129 GLU   A O   1 
ATOM   1068 C CB  . GLU   A 1 132 ? 17.423 -27.774 9.014  1.00 11.81  ? 129 GLU   A CB  1 
ATOM   1069 C CG  . GLU   A 1 132 ? 16.411 -27.989 7.889  1.00 14.56  ? 129 GLU   A CG  1 
ATOM   1070 C CD  . GLU   A 1 132 ? 15.589 -29.270 8.067  1.00 16.86  ? 129 GLU   A CD  1 
ATOM   1071 O OE1 . GLU   A 1 132 ? 16.120 -30.258 8.614  1.00 18.48  ? 129 GLU   A OE1 1 
ATOM   1072 O OE2 . GLU   A 1 132 ? 14.398 -29.271 7.694  1.00 20.40  ? 129 GLU   A OE2 1 
ATOM   1073 N N   . ARG   A 1 133 ? 20.029 -27.108 7.458  1.00 10.01  ? 130 ARG   A N   1 
ATOM   1074 C CA  . ARG   A 1 133 ? 20.750 -27.111 6.195  1.00 8.74   ? 130 ARG   A CA  1 
ATOM   1075 C C   . ARG   A 1 133 ? 19.888 -27.720 5.090  1.00 9.20   ? 130 ARG   A C   1 
ATOM   1076 O O   . ARG   A 1 133 ? 19.196 -28.728 5.290  1.00 10.85  ? 130 ARG   A O   1 
ATOM   1077 C CB  . ARG   A 1 133 ? 22.079 -27.855 6.349  1.00 10.69  ? 130 ARG   A CB  1 
ATOM   1078 C CG  . ARG   A 1 133 ? 23.075 -27.012 7.150  1.00 14.83  ? 130 ARG   A CG  1 
ATOM   1079 C CD  . ARG   A 1 133 ? 24.519 -27.418 6.972  1.00 14.85  ? 130 ARG   A CD  1 
ATOM   1080 N NE  . ARG   A 1 133 ? 25.371 -26.650 7.875  1.00 11.37  ? 130 ARG   A NE  1 
ATOM   1081 C CZ  . ARG   A 1 133 ? 26.059 -25.569 7.531  1.00 10.95  ? 130 ARG   A CZ  1 
ATOM   1082 N NH1 . ARG   A 1 133 ? 25.965 -25.044 6.317  1.00 12.20  ? 130 ARG   A NH1 1 
ATOM   1083 N NH2 . ARG   A 1 133 ? 26.865 -25.003 8.426  1.00 11.26  ? 130 ARG   A NH2 1 
ATOM   1084 N N   . ALA   A 1 134 ? 19.893 -27.074 3.923  1.00 10.80  ? 131 ALA   A N   1 
ATOM   1085 C CA  . ALA   A 1 134 ? 19.155 -27.586 2.768  1.00 11.11  ? 131 ALA   A CA  1 
ATOM   1086 C C   . ALA   A 1 134 ? 19.867 -28.784 2.139  1.00 12.98  ? 131 ALA   A C   1 
ATOM   1087 O O   . ALA   A 1 134 ? 21.032 -29.044 2.446  1.00 11.61  ? 131 ALA   A O   1 
ATOM   1088 C CB  . ALA   A 1 134 ? 18.935 -26.476 1.737  1.00 11.85  ? 131 ALA   A CB  1 
ATOM   1089 O OXT . ALA   A 1 134 ? 19.303 -29.517 1.315  1.00 16.11  ? 131 ALA   A OXT 1 
HETATM 1090 C C1  . A1BLY B 2 .   ? 14.581 -14.936 7.500  1.00 61.73  ? 201 A1BLY A C1  1 
HETATM 1091 C C10 . A1BLY B 2 .   ? 8.258  -9.106  4.515  1.00 59.77  ? 201 A1BLY A C10 1 
HETATM 1092 C C2  . A1BLY B 2 .   ? 14.637 -13.655 8.324  1.00 64.35  ? 201 A1BLY A C2  1 
HETATM 1093 C C3  . A1BLY B 2 .   ? 13.682 -12.625 7.728  1.00 63.47  ? 201 A1BLY A C3  1 
HETATM 1094 C C4  . A1BLY B 2 .   ? 14.093 -11.193 8.100  1.00 73.93  ? 201 A1BLY A C4  1 
HETATM 1095 C C5  . A1BLY B 2 .   ? 12.881 -10.262 8.281  1.00 56.63  ? 201 A1BLY A C5  1 
HETATM 1096 C C6  . A1BLY B 2 .   ? 12.050 -10.053 7.002  1.00 47.54  ? 201 A1BLY A C6  1 
HETATM 1097 C C7  . A1BLY B 2 .   ? 10.947 -9.027  7.319  1.00 42.22  ? 201 A1BLY A C7  1 
HETATM 1098 C C8  . A1BLY B 2 .   ? 10.098 -8.564  6.121  1.00 50.10  ? 201 A1BLY A C8  1 
HETATM 1099 C C9  . A1BLY B 2 .   ? 9.418  -9.688  5.329  1.00 79.81  ? 201 A1BLY A C9  1 
HETATM 1100 F F1  . A1BLY B 2 .   ? 14.221 -13.941 9.592  1.00 69.42  ? 201 A1BLY A F1  1 
HETATM 1101 F F10 . A1BLY B 2 .   ? 11.490 -11.231 6.592  1.00 61.19  ? 201 A1BLY A F10 1 
HETATM 1102 F F11 . A1BLY B 2 .   ? 10.113 -9.542  8.270  1.00 81.94  ? 201 A1BLY A F11 1 
HETATM 1103 F F12 . A1BLY B 2 .   ? 11.546 -7.919  7.846  1.00 52.68  ? 201 A1BLY A F12 1 
HETATM 1104 F F13 . A1BLY B 2 .   ? 9.090  -7.783  6.609  1.00 40.85  ? 201 A1BLY A F13 1 
HETATM 1105 F F14 . A1BLY B 2 .   ? 10.875 -7.805  5.292  1.00 46.38  ? 201 A1BLY A F14 1 
HETATM 1106 F F15 . A1BLY B 2 .   ? 8.919  -10.619 6.194  1.00 80.72  ? 201 A1BLY A F15 1 
HETATM 1107 F F16 . A1BLY B 2 .   ? 10.311 -10.293 4.490  1.00 70.40  ? 201 A1BLY A F16 1 
HETATM 1108 F F17 . A1BLY B 2 .   ? 7.959  -9.941  3.476  1.00 47.40  ? 201 A1BLY A F17 1 
HETATM 1109 F F18 . A1BLY B 2 .   ? 7.159  -8.967  5.316  1.00 75.97  ? 201 A1BLY A F18 1 
HETATM 1110 F F19 . A1BLY B 2 .   ? 8.600  -7.880  4.023  1.00 72.17  ? 201 A1BLY A F19 1 
HETATM 1111 F F2  . A1BLY B 2 .   ? 15.915 -13.170 8.325  1.00 76.52  ? 201 A1BLY A F2  1 
HETATM 1112 F F3  . A1BLY B 2 .   ? 13.673 -12.748 6.366  1.00 95.56  ? 201 A1BLY A F3  1 
HETATM 1113 F F4  . A1BLY B 2 .   ? 12.435 -12.897 8.215  1.00 70.09  ? 201 A1BLY A F4  1 
HETATM 1114 F F5  . A1BLY B 2 .   ? 14.922 -10.682 7.140  1.00 97.06  ? 201 A1BLY A F5  1 
HETATM 1115 F F6  . A1BLY B 2 .   ? 14.776 -11.236 9.283  1.00 87.51  ? 201 A1BLY A F6  1 
HETATM 1116 F F7  . A1BLY B 2 .   ? 12.086 -10.764 9.272  1.00 54.98  ? 201 A1BLY A F7  1 
HETATM 1117 F F8  . A1BLY B 2 .   ? 13.333 -9.034  8.681  1.00 47.14  ? 201 A1BLY A F8  1 
HETATM 1118 F F9  . A1BLY B 2 .   ? 12.865 -9.575  6.014  1.00 76.63  ? 201 A1BLY A F9  1 
HETATM 1119 O O1  . A1BLY B 2 .   ? 15.475 -15.175 6.645  1.00 107.22 ? 201 A1BLY A O1  1 
HETATM 1120 O O2  . A1BLY B 2 .   ? 13.640 -15.752 7.680  1.00 85.35  ? 201 A1BLY A O2  1 
HETATM 1121 O O   . HOH   C 3 .   ? 17.411 -18.026 19.871 1.00 44.66  ? 301 HOH   A O   1 
HETATM 1122 O O   . HOH   C 3 .   ? 33.976 -16.079 6.145  1.00 42.55  ? 302 HOH   A O   1 
HETATM 1123 O O   . HOH   C 3 .   ? 35.916 -18.920 11.055 1.00 36.14  ? 303 HOH   A O   1 
HETATM 1124 O O   . HOH   C 3 .   ? 7.902  4.506   9.479  1.00 48.83  ? 304 HOH   A O   1 
HETATM 1125 O O   . HOH   C 3 .   ? 15.353 -16.562 4.349  1.00 27.13  ? 305 HOH   A O   1 
HETATM 1126 O O   . HOH   C 3 .   ? 14.481 -16.700 20.513 1.00 36.29  ? 306 HOH   A O   1 
HETATM 1127 O O   . HOH   C 3 .   ? 28.661 -18.824 15.258 1.00 47.88  ? 307 HOH   A O   1 
HETATM 1128 O O   . HOH   C 3 .   ? 1.094  -4.655  19.145 1.00 33.36  ? 308 HOH   A O   1 
HETATM 1129 O O   . HOH   C 3 .   ? 6.346  1.676   -0.622 1.00 51.08  ? 309 HOH   A O   1 
HETATM 1130 O O   . HOH   C 3 .   ? 12.141 -23.161 3.428  1.00 29.67  ? 310 HOH   A O   1 
HETATM 1131 O O   . HOH   C 3 .   ? 34.097 1.047   4.757  1.00 22.76  ? 311 HOH   A O   1 
HETATM 1132 O O   . HOH   C 3 .   ? 5.999  -3.163  21.492 1.00 45.46  ? 312 HOH   A O   1 
HETATM 1133 O O   . HOH   C 3 .   ? 28.056 -16.198 21.385 1.00 16.58  ? 313 HOH   A O   1 
HETATM 1134 O O   . HOH   C 3 .   ? 16.932 -18.829 -7.466 1.00 23.57  ? 314 HOH   A O   1 
HETATM 1135 O O   . HOH   C 3 .   ? 18.806 -26.105 20.753 1.00 32.47  ? 315 HOH   A O   1 
HETATM 1136 O O   . HOH   C 3 .   ? 9.564  8.378   13.668 1.00 44.39  ? 316 HOH   A O   1 
HETATM 1137 O O   . HOH   C 3 .   ? 5.752  -22.244 15.411 1.00 43.85  ? 317 HOH   A O   1 
HETATM 1138 O O   . HOH   C 3 .   ? 10.500 -10.287 23.130 1.00 21.86  ? 318 HOH   A O   1 
HETATM 1139 O O   . HOH   C 3 .   ? 2.344  -13.782 8.681  1.00 23.67  ? 319 HOH   A O   1 
HETATM 1140 O O   . HOH   C 3 .   ? 10.352 -15.795 19.503 1.00 18.44  ? 320 HOH   A O   1 
HETATM 1141 O O   . HOH   C 3 .   ? 34.781 -5.985  7.853  1.00 17.70  ? 321 HOH   A O   1 
HETATM 1142 O O   . HOH   C 3 .   ? 10.152 8.996   7.160  1.00 47.54  ? 322 HOH   A O   1 
HETATM 1143 O O   . HOH   C 3 .   ? 20.035 -13.674 21.153 1.00 28.04  ? 323 HOH   A O   1 
HETATM 1144 O O   . HOH   C 3 .   ? 12.559 -27.801 6.508  1.00 27.81  ? 324 HOH   A O   1 
HETATM 1145 O O   . HOH   C 3 .   ? 40.657 -6.458  2.209  1.00 26.72  ? 325 HOH   A O   1 
HETATM 1146 O O   . HOH   C 3 .   ? 16.335 -7.280  2.582  1.00 17.11  ? 326 HOH   A O   1 
HETATM 1147 O O   . HOH   C 3 .   ? 21.834 -0.955  -1.717 1.00 36.00  ? 327 HOH   A O   1 
HETATM 1148 O O   . HOH   C 3 .   ? -0.121 -15.330 8.650  1.00 33.25  ? 328 HOH   A O   1 
HETATM 1149 O O   . HOH   C 3 .   ? 11.286 -20.508 20.242 1.00 40.54  ? 329 HOH   A O   1 
HETATM 1150 O O   . HOH   C 3 .   ? 16.673 -29.686 0.896  1.00 21.30  ? 330 HOH   A O   1 
HETATM 1151 O O   . HOH   C 3 .   ? 25.816 -24.282 16.552 1.00 60.80  ? 331 HOH   A O   1 
HETATM 1152 O O   . HOH   C 3 .   ? 27.108 -3.191  1.121  1.00 16.25  ? 332 HOH   A O   1 
HETATM 1153 O O   . HOH   C 3 .   ? 22.331 3.430   -2.201 1.00 27.32  ? 333 HOH   A O   1 
HETATM 1154 O O   . HOH   C 3 .   ? 17.978 -10.923 20.040 1.00 55.73  ? 334 HOH   A O   1 
HETATM 1155 O O   . HOH   C 3 .   ? 19.226 -32.030 0.411  1.00 21.89  ? 335 HOH   A O   1 
HETATM 1156 O O   . HOH   C 3 .   ? 29.019 -14.444 -2.744 1.00 15.17  ? 336 HOH   A O   1 
HETATM 1157 O O   . HOH   C 3 .   ? 24.817 5.283   11.154 1.00 10.68  ? 337 HOH   A O   1 
HETATM 1158 O O   . HOH   C 3 .   ? 18.720 3.899   2.569  1.00 16.60  ? 338 HOH   A O   1 
HETATM 1159 O O   . HOH   C 3 .   ? 8.134  10.210  9.252  1.00 30.01  ? 339 HOH   A O   1 
HETATM 1160 O O   . HOH   C 3 .   ? 28.193 1.095   1.980  1.00 14.42  ? 340 HOH   A O   1 
HETATM 1161 O O   . HOH   C 3 .   ? 28.972 -23.417 7.118  1.00 10.99  ? 341 HOH   A O   1 
HETATM 1162 O O   . HOH   C 3 .   ? 6.534  -0.069  8.469  1.00 27.01  ? 342 HOH   A O   1 
HETATM 1163 O O   . HOH   C 3 .   ? 29.395 -11.993 -1.596 1.00 11.22  ? 343 HOH   A O   1 
HETATM 1164 O O   . HOH   C 3 .   ? 12.177 -25.614 15.734 1.00 21.38  ? 344 HOH   A O   1 
HETATM 1165 O O   . HOH   C 3 .   ? 12.914 -7.882  -3.614 1.00 36.51  ? 345 HOH   A O   1 
HETATM 1166 O O   . HOH   C 3 .   ? 18.307 -11.400 2.014  1.00 19.61  ? 346 HOH   A O   1 
HETATM 1167 O O   . HOH   C 3 .   ? 2.592  -15.041 18.065 1.00 20.54  ? 347 HOH   A O   1 
HETATM 1168 O O   . HOH   C 3 .   ? 17.962 -30.847 6.467  1.00 14.42  ? 348 HOH   A O   1 
HETATM 1169 O O   . HOH   C 3 .   ? 8.295  -27.787 11.382 1.00 43.21  ? 349 HOH   A O   1 
HETATM 1170 O O   . HOH   C 3 .   ? 23.661 -8.318  -3.730 1.00 35.37  ? 350 HOH   A O   1 
HETATM 1171 O O   . HOH   C 3 .   ? 21.956 -26.235 22.211 1.00 34.95  ? 351 HOH   A O   1 
HETATM 1172 O O   . HOH   C 3 .   ? 13.388 -6.182  9.308  1.00 12.89  ? 352 HOH   A O   1 
HETATM 1173 O O   . HOH   C 3 .   ? 6.523  -1.661  6.203  1.00 25.84  ? 353 HOH   A O   1 
HETATM 1174 O O   . HOH   C 3 .   ? 23.898 -13.916 -5.070 1.00 61.16  ? 354 HOH   A O   1 
HETATM 1175 O O   . HOH   C 3 .   ? 25.355 -9.248  -4.772 1.00 47.25  ? 355 HOH   A O   1 
HETATM 1176 O O   . HOH   C 3 .   ? 23.050 -27.438 1.432  1.00 11.89  ? 356 HOH   A O   1 
HETATM 1177 O O   . HOH   C 3 .   ? 2.935  -7.268  17.550 1.00 18.62  ? 357 HOH   A O   1 
HETATM 1178 O O   . HOH   C 3 .   ? 16.937 -6.254  0.171  1.00 19.80  ? 358 HOH   A O   1 
HETATM 1179 O O   . HOH   C 3 .   ? 14.312 5.857   5.783  1.00 36.57  ? 359 HOH   A O   1 
HETATM 1180 O O   . HOH   C 3 .   ? 22.963 6.743   8.139  1.00 10.60  ? 360 HOH   A O   1 
HETATM 1181 O O   . HOH   C 3 .   ? 18.169 -27.999 17.487 1.00 16.04  ? 361 HOH   A O   1 
HETATM 1182 O O   . HOH   C 3 .   ? 7.952  -17.580 6.033  1.00 22.96  ? 362 HOH   A O   1 
HETATM 1183 O O   . HOH   C 3 .   ? 33.328 -8.370  5.939  1.00 14.29  ? 363 HOH   A O   1 
HETATM 1184 O O   . HOH   C 3 .   ? 18.284 -14.122 6.851  1.00 23.98  ? 364 HOH   A O   1 
HETATM 1185 O O   . HOH   C 3 .   ? 26.617 -5.502  18.327 1.00 20.03  ? 365 HOH   A O   1 
HETATM 1186 O O   . HOH   C 3 .   ? 26.587 -11.664 20.248 1.00 22.45  ? 366 HOH   A O   1 
HETATM 1187 O O   . HOH   C 3 .   ? 34.579 -17.915 -0.059 1.00 12.34  ? 367 HOH   A O   1 
HETATM 1188 O O   . HOH   C 3 .   ? 2.639  -1.138  14.106 1.00 38.95  ? 368 HOH   A O   1 
HETATM 1189 O O   . HOH   C 3 .   ? 18.433 -31.235 12.925 1.00 13.03  ? 369 HOH   A O   1 
HETATM 1190 O O   . HOH   C 3 .   ? 21.109 -3.925  0.380  1.00 17.21  ? 370 HOH   A O   1 
HETATM 1191 O O   . HOH   C 3 .   ? 23.825 -29.560 21.446 1.00 36.90  ? 371 HOH   A O   1 
HETATM 1192 O O   . HOH   C 3 .   ? 24.529 -15.785 -1.120 1.00 13.30  ? 372 HOH   A O   1 
HETATM 1193 O O   . HOH   C 3 .   ? 22.060 -10.808 11.294 1.00 10.42  ? 373 HOH   A O   1 
HETATM 1194 O O   . HOH   C 3 .   ? 25.686 -4.351  14.169 1.00 13.75  ? 374 HOH   A O   1 
HETATM 1195 O O   . HOH   C 3 .   ? 33.944 -2.269  7.638  1.00 22.43  ? 375 HOH   A O   1 
HETATM 1196 O O   . HOH   C 3 .   ? 20.781 -17.739 22.856 1.00 39.67  ? 376 HOH   A O   1 
HETATM 1197 O O   . HOH   C 3 .   ? 20.823 -28.370 9.839  1.00 12.98  ? 377 HOH   A O   1 
HETATM 1198 O O   . HOH   C 3 .   ? 27.413 -4.097  7.340  1.00 9.95   ? 378 HOH   A O   1 
HETATM 1199 O O   . HOH   C 3 .   ? 34.928 -12.077 4.887  1.00 35.79  ? 379 HOH   A O   1 
HETATM 1200 O O   . HOH   C 3 .   ? 13.104 -3.778  21.154 1.00 37.89  ? 380 HOH   A O   1 
HETATM 1201 O O   . HOH   C 3 .   ? 16.233 -30.482 11.403 1.00 15.55  ? 381 HOH   A O   1 
HETATM 1202 O O   . HOH   C 3 .   ? 24.810 -27.354 10.556 1.00 11.16  ? 382 HOH   A O   1 
HETATM 1203 O O   . HOH   C 3 .   ? 20.325 -19.796 -5.987 1.00 31.70  ? 383 HOH   A O   1 
HETATM 1204 O O   . HOH   C 3 .   ? 31.713 0.568   11.981 1.00 14.66  ? 384 HOH   A O   1 
HETATM 1205 O O   . HOH   C 3 .   ? 31.298 -18.118 11.521 1.00 14.84  ? 385 HOH   A O   1 
HETATM 1206 O O   . HOH   C 3 .   ? 17.404 4.439   14.584 1.00 13.82  ? 386 HOH   A O   1 
HETATM 1207 O O   . HOH   C 3 .   ? 34.170 -16.033 13.448 1.00 15.54  ? 387 HOH   A O   1 
HETATM 1208 O O   . HOH   C 3 .   ? 23.030 1.101   10.285 1.00 15.84  ? 388 HOH   A O   1 
HETATM 1209 O O   . HOH   C 3 .   ? 16.350 -20.825 20.110 1.00 31.09  ? 389 HOH   A O   1 
HETATM 1210 O O   . HOH   C 3 .   ? 10.881 -21.121 15.795 1.00 14.24  ? 390 HOH   A O   1 
HETATM 1211 O O   . HOH   C 3 .   ? 28.644 3.535   4.709  1.00 11.25  ? 391 HOH   A O   1 
HETATM 1212 O O   . HOH   C 3 .   ? 13.368 -1.927  18.466 1.00 30.47  ? 392 HOH   A O   1 
HETATM 1213 O O   . HOH   C 3 .   ? 24.307 -25.614 3.943  1.00 11.12  ? 393 HOH   A O   1 
HETATM 1214 O O   . HOH   C 3 .   ? -2.560 -3.522  6.149  1.00 47.77  ? 394 HOH   A O   1 
HETATM 1215 O O   . HOH   C 3 .   ? 32.564 -23.227 6.046  1.00 28.84  ? 395 HOH   A O   1 
HETATM 1216 O O   . HOH   C 3 .   ? 17.082 -2.280  17.335 1.00 29.61  ? 396 HOH   A O   1 
HETATM 1217 O O   . HOH   C 3 .   ? 9.585  -11.935 -6.507 1.00 20.44  ? 397 HOH   A O   1 
HETATM 1218 O O   . HOH   C 3 .   ? 16.441 -30.961 15.696 1.00 13.91  ? 398 HOH   A O   1 
HETATM 1219 O O   . HOH   C 3 .   ? 30.997 -1.807  -0.258 1.00 17.99  ? 399 HOH   A O   1 
HETATM 1220 O O   . HOH   C 3 .   ? 28.613 -24.934 3.829  1.00 15.74  ? 400 HOH   A O   1 
HETATM 1221 O O   . HOH   C 3 .   ? 0.352  -5.176  2.545  1.00 37.26  ? 401 HOH   A O   1 
HETATM 1222 O O   . HOH   C 3 .   ? 33.362 -11.132 18.683 1.00 10.73  ? 402 HOH   A O   1 
HETATM 1223 O O   . HOH   C 3 .   ? 40.279 -7.961  5.078  1.00 27.80  ? 403 HOH   A O   1 
HETATM 1224 O O   . HOH   C 3 .   ? 17.501 -8.461  6.102  1.00 15.14  ? 404 HOH   A O   1 
HETATM 1225 O O   . HOH   C 3 .   ? 5.690  -17.164 13.286 1.00 16.25  ? 405 HOH   A O   1 
HETATM 1226 O O   . HOH   C 3 .   ? 3.955  1.006   8.038  1.00 41.85  ? 406 HOH   A O   1 
HETATM 1227 O O   . HOH   C 3 .   ? 12.624 -30.447 2.920  1.00 31.00  ? 407 HOH   A O   1 
HETATM 1228 O O   . HOH   C 3 .   ? 3.847  -15.776 13.013 1.00 24.04  ? 408 HOH   A O   1 
HETATM 1229 O O   . HOH   C 3 .   ? 14.611 -10.871 3.644  1.00 27.97  ? 409 HOH   A O   1 
HETATM 1230 O O   . HOH   C 3 .   ? 4.312  -18.157 19.607 1.00 30.38  ? 410 HOH   A O   1 
HETATM 1231 O O   . HOH   C 3 .   ? 0.547  -16.434 6.297  1.00 26.50  ? 411 HOH   A O   1 
HETATM 1232 O O   . HOH   C 3 .   ? 8.101  2.354   8.553  1.00 31.50  ? 412 HOH   A O   1 
HETATM 1233 O O   . HOH   C 3 .   ? 12.814 -14.234 13.082 1.00 16.86  ? 413 HOH   A O   1 
HETATM 1234 O O   . HOH   C 3 .   ? 13.708 8.478   17.314 1.00 25.97  ? 414 HOH   A O   1 
HETATM 1235 O O   . HOH   C 3 .   ? 11.346 -17.794 22.619 1.00 19.82  ? 415 HOH   A O   1 
HETATM 1236 O O   . HOH   C 3 .   ? 19.277 -6.324  -3.822 1.00 39.00  ? 416 HOH   A O   1 
HETATM 1237 O O   . HOH   C 3 .   ? 20.870 -31.145 10.090 1.00 11.87  ? 417 HOH   A O   1 
HETATM 1238 O O   . HOH   C 3 .   ? 28.529 -2.861  3.567  1.00 11.42  ? 418 HOH   A O   1 
HETATM 1239 O O   . HOH   C 3 .   ? 17.036 -7.425  -2.374 1.00 18.96  ? 419 HOH   A O   1 
HETATM 1240 O O   . HOH   C 3 .   ? 19.610 -28.774 -1.480 1.00 24.84  ? 420 HOH   A O   1 
HETATM 1241 O O   . HOH   C 3 .   ? 18.515 5.792   9.043  1.00 12.89  ? 421 HOH   A O   1 
HETATM 1242 O O   . HOH   C 3 .   ? 34.352 -9.464  -3.495 1.00 11.75  ? 422 HOH   A O   1 
HETATM 1243 O O   . HOH   C 3 .   ? 23.356 -5.017  -0.809 1.00 18.40  ? 423 HOH   A O   1 
HETATM 1244 O O   . HOH   C 3 .   ? 3.907  -17.951 16.446 1.00 25.69  ? 424 HOH   A O   1 
HETATM 1245 O O   . HOH   C 3 .   ? 14.734 -7.149  6.574  1.00 16.89  ? 425 HOH   A O   1 
HETATM 1246 O O   . HOH   C 3 .   ? 11.022 3.579   4.134  1.00 23.65  ? 426 HOH   A O   1 
HETATM 1247 O O   . HOH   C 3 .   ? 7.205  0.217   3.843  1.00 37.99  ? 427 HOH   A O   1 
HETATM 1248 O O   . HOH   C 3 .   ? 17.803 -22.120 -5.808 1.00 51.58  ? 428 HOH   A O   1 
HETATM 1249 O O   . HOH   C 3 .   ? 6.957  0.771   13.527 1.00 40.21  ? 429 HOH   A O   1 
HETATM 1250 O O   . HOH   C 3 .   ? 17.156 5.235   4.463  1.00 17.82  ? 430 HOH   A O   1 
HETATM 1251 O O   . HOH   C 3 .   ? 14.028 -7.904  3.862  1.00 17.27  ? 431 HOH   A O   1 
HETATM 1252 O O   . HOH   C 3 .   ? 37.196 -21.079 10.031 1.00 37.35  ? 432 HOH   A O   1 
HETATM 1253 O O   . HOH   C 3 .   ? 8.773  -25.195 7.390  1.00 44.17  ? 433 HOH   A O   1 
HETATM 1254 O O   . HOH   C 3 .   ? 6.502  -23.069 12.860 1.00 19.96  ? 434 HOH   A O   1 
HETATM 1255 O O   . HOH   C 3 .   ? 17.434 1.907   1.244  1.00 18.63  ? 435 HOH   A O   1 
HETATM 1256 O O   . HOH   C 3 .   ? 18.372 -4.141  -0.576 1.00 19.04  ? 436 HOH   A O   1 
HETATM 1257 O O   . HOH   C 3 .   ? 2.981  -14.000 15.359 1.00 17.53  ? 437 HOH   A O   1 
HETATM 1258 O O   . HOH   C 3 .   ? 19.706 -30.313 20.975 1.00 32.87  ? 438 HOH   A O   1 
HETATM 1259 O O   . HOH   C 3 .   ? 0.143  -13.380 15.618 1.00 28.85  ? 439 HOH   A O   1 
HETATM 1260 O O   . HOH   C 3 .   ? -2.435 -5.014  3.125  1.00 45.22  ? 440 HOH   A O   1 
HETATM 1261 O O   . HOH   C 3 .   ? 35.869 -17.561 2.514  1.00 27.89  ? 441 HOH   A O   1 
HETATM 1262 O O   . HOH   C 3 .   ? 12.346 1.414   17.183 1.00 22.33  ? 442 HOH   A O   1 
HETATM 1263 O O   . HOH   C 3 .   ? 10.767 -14.515 -6.252 1.00 18.95  ? 443 HOH   A O   1 
HETATM 1264 O O   . HOH   C 3 .   ? 24.510 -18.558 19.465 1.00 27.41  ? 444 HOH   A O   1 
HETATM 1265 O O   . HOH   C 3 .   ? 8.035  -20.093 -0.899 1.00 27.95  ? 445 HOH   A O   1 
HETATM 1266 O O   . HOH   C 3 .   ? 30.266 -18.184 13.999 1.00 20.37  ? 446 HOH   A O   1 
HETATM 1267 O O   . HOH   C 3 .   ? 0.488  -0.700  7.934  1.00 49.50  ? 447 HOH   A O   1 
HETATM 1268 O O   . HOH   C 3 .   ? 16.815 -23.529 17.678 1.00 30.14  ? 448 HOH   A O   1 
HETATM 1269 O O   . HOH   C 3 .   ? 21.950 -6.221  -3.406 1.00 43.47  ? 449 HOH   A O   1 
HETATM 1270 O O   . HOH   C 3 .   ? 30.665 -19.008 0.327  1.00 13.33  ? 450 HOH   A O   1 
HETATM 1271 O O   . HOH   C 3 .   ? 26.281 -11.327 -4.675 1.00 49.46  ? 451 HOH   A O   1 
HETATM 1272 O O   . HOH   C 3 .   ? 12.665 -13.282 3.770  1.00 49.42  ? 452 HOH   A O   1 
HETATM 1273 O O   . HOH   C 3 .   ? 17.732 -9.419  17.642 1.00 22.16  ? 453 HOH   A O   1 
HETATM 1274 O O   . HOH   C 3 .   ? 4.539  -17.097 -0.152 1.00 29.60  ? 454 HOH   A O   1 
HETATM 1275 O O   . HOH   C 3 .   ? 33.977 -20.929 3.456  1.00 42.37  ? 455 HOH   A O   1 
HETATM 1276 O O   . HOH   C 3 .   ? 22.548 -20.277 22.442 1.00 35.21  ? 456 HOH   A O   1 
HETATM 1277 O O   . HOH   C 3 .   ? 27.712 -8.598  -4.475 1.00 23.15  ? 457 HOH   A O   1 
HETATM 1278 O O   . HOH   C 3 .   ? 33.831 -13.715 6.570  1.00 37.25  ? 458 HOH   A O   1 
HETATM 1279 O O   . HOH   C 3 .   ? 12.837 -24.083 1.193  1.00 34.31  ? 459 HOH   A O   1 
HETATM 1280 O O   . HOH   C 3 .   ? 3.729  -19.158 13.790 1.00 39.12  ? 460 HOH   A O   1 
HETATM 1281 O O   . HOH   C 3 .   ? 14.966 -9.964  22.860 1.00 36.10  ? 461 HOH   A O   1 
HETATM 1282 O O   . HOH   C 3 .   ? 20.145 -22.835 -3.662 1.00 27.54  ? 462 HOH   A O   1 
HETATM 1283 O O   . HOH   C 3 .   ? 9.772  -21.096 -2.008 1.00 41.41  ? 463 HOH   A O   1 
HETATM 1284 O O   . HOH   C 3 .   ? 25.284 1.230   13.007 1.00 31.42  ? 464 HOH   A O   1 
HETATM 1285 O O   . HOH   C 3 .   ? 28.141 -28.202 6.881  1.00 24.67  ? 465 HOH   A O   1 
HETATM 1286 O O   . HOH   C 3 .   ? 39.940 -19.163 2.304  1.00 43.30  ? 466 HOH   A O   1 
HETATM 1287 O O   . HOH   C 3 .   ? 33.519 -19.908 11.862 1.00 17.24  ? 467 HOH   A O   1 
HETATM 1288 O O   . HOH   C 3 .   ? 17.305 -10.441 4.387  1.00 32.34  ? 468 HOH   A O   1 
HETATM 1289 O O   . HOH   C 3 .   ? 9.829  2.586   17.232 1.00 31.61  ? 469 HOH   A O   1 
HETATM 1290 O O   . HOH   C 3 .   ? 8.042  -22.295 16.790 1.00 49.67  ? 470 HOH   A O   1 
HETATM 1291 O O   . HOH   C 3 .   ? 27.593 -27.517 4.356  1.00 14.18  ? 471 HOH   A O   1 
HETATM 1292 O O   . HOH   C 3 .   ? 9.385  -14.207 2.081  1.00 32.85  ? 472 HOH   A O   1 
HETATM 1293 O O   . HOH   C 3 .   ? 12.050 -20.031 -4.390 1.00 27.24  ? 473 HOH   A O   1 
HETATM 1294 O O   . HOH   C 3 .   ? 26.678 -13.578 -4.504 1.00 29.95  ? 474 HOH   A O   1 
HETATM 1295 O O   . HOH   C 3 .   ? 33.244 -22.656 11.592 1.00 17.69  ? 475 HOH   A O   1 
HETATM 1296 O O   . HOH   C 3 .   ? 29.312 -4.363  -0.443 1.00 26.53  ? 476 HOH   A O   1 
HETATM 1297 O O   . HOH   C 3 .   ? 30.038 -26.011 6.665  1.00 25.84  ? 477 HOH   A O   1 
HETATM 1298 O O   . HOH   C 3 .   ? 14.556 -19.167 -6.866 1.00 30.52  ? 478 HOH   A O   1 
HETATM 1299 O O   . HOH   C 3 .   ? 39.707 -14.456 1.771  1.00 31.61  ? 479 HOH   A O   1 
HETATM 1300 O O   . HOH   C 3 .   ? 35.522 -23.411 9.743  1.00 32.63  ? 480 HOH   A O   1 
HETATM 1301 O O   . HOH   C 3 .   ? 4.146  -15.902 10.052 1.00 37.88  ? 481 HOH   A O   1 
HETATM 1302 O O   . HOH   C 3 .   ? 29.741 -10.428 -3.762 1.00 13.83  ? 482 HOH   A O   1 
HETATM 1303 O O   . HOH   C 3 .   ? 9.737  -14.173 4.276  1.00 38.25  ? 483 HOH   A O   1 
HETATM 1304 O O   . HOH   C 3 .   ? 28.559 -11.885 22.345 1.00 26.98  ? 484 HOH   A O   1 
HETATM 1305 O O   . HOH   C 3 .   ? 11.776 -24.818 18.079 1.00 35.93  ? 485 HOH   A O   1 
HETATM 1306 O O   . HOH   C 3 .   ? 36.889 -5.208  6.192  1.00 39.09  ? 486 HOH   A O   1 
HETATM 1307 O O   . HOH   C 3 .   ? 14.451 -27.174 15.765 1.00 19.95  ? 487 HOH   A O   1 
HETATM 1308 O O   . HOH   C 3 .   ? 11.385 -12.989 1.979  1.00 47.22  ? 488 HOH   A O   1 
HETATM 1309 O O   . HOH   C 3 .   ? 16.500 -30.325 18.138 1.00 30.94  ? 489 HOH   A O   1 
HETATM 1310 O O   . HOH   C 3 .   ? 41.160 -21.895 2.937  1.00 45.25  ? 490 HOH   A O   1 
HETATM 1311 O O   . HOH   C 3 .   ? 14.765 -22.210 18.801 1.00 33.35  ? 491 HOH   A O   1 
HETATM 1312 O O   . HOH   C 3 .   ? 25.619 -6.954  20.199 1.00 40.03  ? 492 HOH   A O   1 
HETATM 1313 O O   . HOH   C 3 .   ? 25.620 -1.436  14.068 1.00 21.27  ? 493 HOH   A O   1 
HETATM 1314 O O   . HOH   C 3 .   ? 25.311 -16.722 21.320 1.00 20.94  ? 494 HOH   A O   1 
HETATM 1315 O O   . HOH   C 3 .   ? 16.379 -26.053 17.429 1.00 24.26  ? 495 HOH   A O   1 
HETATM 1316 O O   . HOH   C 3 .   ? 12.100 -21.802 18.081 1.00 24.47  ? 496 HOH   A O   1 
HETATM 1317 O O   . HOH   C 3 .   ? 10.170 -27.573 15.358 1.00 32.02  ? 497 HOH   A O   1 
HETATM 1318 O O   . HOH   C 3 .   ? 11.527 5.626   6.052  1.00 37.33  ? 498 HOH   A O   1 
HETATM 1319 O O   . HOH   C 3 .   ? 11.621 -28.530 4.093  1.00 38.13  ? 499 HOH   A O   1 
HETATM 1320 O O   . HOH   C 3 .   ? 8.350  2.687   5.209  1.00 34.29  ? 500 HOH   A O   1 
HETATM 1321 O O   . HOH   C 3 .   ? 28.444 -5.782  -3.173 1.00 35.16  ? 501 HOH   A O   1 
HETATM 1322 O O   . HOH   C 3 .   ? 18.447 -24.174 -5.192 1.00 43.38  ? 502 HOH   A O   1 
HETATM 1323 O O   . HOH   C 3 .   ? 1.938  -17.095 16.003 1.00 57.64  ? 503 HOH   A O   1 
HETATM 1324 O O   . HOH   C 3 .   ? 25.798 -14.117 -6.995 1.00 52.96  ? 504 HOH   A O   1 
HETATM 1325 O O   . HOH   C 3 .   ? 26.527 -4.466  -3.508 1.00 49.18  ? 505 HOH   A O   1 
HETATM 1326 O O   . HOH   C 3 .   ? 35.755 2.824   3.668  1.00 26.64  ? 506 HOH   A O   1 
HETATM 1327 O O   . HOH   C 3 .   ? 15.536 -27.362 -0.206 1.00 32.15  ? 507 HOH   A O   1 
HETATM 1328 O O   . HOH   C 3 .   ? 10.786 5.364   2.248  1.00 37.82  ? 508 HOH   A O   1 
HETATM 1329 O O   . HOH   C 3 .   ? 33.076 -20.170 0.879  1.00 16.97  ? 509 HOH   A O   1 
HETATM 1330 O O   . HOH   C 3 .   ? 42.409 -8.880  2.500  1.00 42.16  ? 510 HOH   A O   1 
HETATM 1331 O O   . HOH   C 3 .   ? 42.102 -6.897  4.119  1.00 35.04  ? 511 HOH   A O   1 
HETATM 1332 O O   . HOH   C 3 .   ? 20.801 -22.008 23.645 1.00 34.00  ? 512 HOH   A O   1 
HETATM 1333 O O   . HOH   C 3 .   ? 41.330 -16.750 1.533  1.00 27.01  ? 513 HOH   A O   1 
HETATM 1334 O O   . HOH   C 3 .   ? 2.098  -17.277 13.091 1.00 47.87  ? 514 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 1   ? 0.3187 0.5939 0.8707 -0.1587 0.0329  0.0746  -2  GLY A N   
2    C CA  . GLY A 1   ? 0.3086 0.5344 0.7894 -0.1632 0.0478  0.1073  -2  GLY A CA  
3    C C   . GLY A 1   ? 0.3013 0.4778 0.7219 -0.1436 0.0355  0.1476  -2  GLY A C   
4    O O   . GLY A 1   ? 0.3074 0.5305 0.7243 -0.1351 -0.0073 0.1404  -2  GLY A O   
5    N N   . HIS A 2   ? 0.2804 0.4368 0.6671 -0.1205 0.0321  0.1278  -1  HIS A N   
6    C CA  . HIS A 2   ? 0.2655 0.3877 0.6334 -0.1002 0.0309  0.1191  -1  HIS A CA  
7    C C   . HIS A 2   ? 0.2344 0.2838 0.4585 -0.0721 -0.0254 0.1038  -1  HIS A C   
8    O O   . HIS A 2   ? 0.2183 0.2361 0.4712 -0.0803 -0.0349 0.1214  -1  HIS A O   
9    C CB  . HIS A 2   ? 0.2938 0.4989 0.7782 -0.0685 0.0409  0.0255  -1  HIS A CB  
10   C CG  . HIS A 2   ? 0.3167 0.5874 0.9259 -0.0512 0.0417  -0.0802 -1  HIS A CG  
11   N ND1 . HIS A 2   ? 0.3283 0.6254 0.9782 -0.0409 0.0433  -0.1185 -1  HIS A ND1 
12   C CD2 . HIS A 2   ? 0.3287 0.6277 1.0087 -0.0523 0.0422  -0.0893 -1  HIS A CD2 
13   C CE1 . HIS A 2   ? 0.3315 0.6491 1.0148 -0.0470 0.0378  -0.1247 -1  HIS A CE1 
14   N NE2 . HIS A 2   ? 0.3319 0.6459 1.0268 -0.0528 0.0409  -0.1201 -1  HIS A NE2 
15   N N   . MET A 3   ? 0.2284 0.2199 0.3336 -0.0612 -0.0412 0.0084  0   MET A N   
16   C CA  . MET A 3   ? 0.2416 0.2202 0.3171 -0.0730 -0.0119 -0.0445 0   MET A CA  
17   C C   . MET A 3   ? 0.2179 0.1926 0.2055 -0.0680 0.0257  -0.0726 0   MET A C   
18   O O   . MET A 3   ? 0.2145 0.1909 0.2103 -0.0704 0.0179  -0.0118 0   MET A O   
19   C CB  . MET A 3   ? 0.2726 0.1719 0.3232 -0.0645 0.0121  -0.0498 0   MET A CB  
20   C CG  . MET A 3   ? 0.2999 0.2178 0.2504 -0.0763 0.0243  0.0121  0   MET A CG  
21   S SD  . MET A 3   ? 0.3060 0.1495 0.1617 -0.0577 0.0198  -0.0003 0   MET A SD  
22   C CE  . MET A 3   ? 0.3008 0.1302 0.1544 -0.0592 0.0389  -0.0044 0   MET A CE  
23   N N   . CYS A 4   ? 0.1985 0.1579 0.1418 -0.0537 0.0044  -0.0619 1   CYS A N   
24   C CA  . CYS A 4   ? 0.1829 0.1516 0.1511 -0.0237 -0.0115 -0.0237 1   CYS A CA  
25   C C   . CYS A 4   ? 0.1530 0.1487 0.1522 -0.0173 -0.0113 0.0048  1   CYS A C   
26   O O   . CYS A 4   ? 0.1638 0.1567 0.1558 -0.0641 -0.0157 0.0454  1   CYS A O   
27   C CB  . CYS A 4   ? 0.2111 0.0840 0.2979 0.0246  -0.0388 -0.0025 1   CYS A CB  
28   S SG  . CYS A 4   ? 0.2535 0.2692 0.2823 0.0226  0.0149  0.0576  1   CYS A SG  
29   N N   . ASP A 5   ? 0.1351 0.1214 0.1911 -0.0027 0.0205  0.0066  2   ASP A N   
30   C CA  . ASP A 5   ? 0.1341 0.1324 0.2349 0.0018  0.0591  0.0245  2   ASP A CA  
31   C C   . ASP A 5   ? 0.1322 0.1454 0.1661 -0.0198 0.0550  -0.0094 2   ASP A C   
32   O O   . ASP A 5   ? 0.1445 0.1492 0.2073 -0.0619 0.0281  -0.0735 2   ASP A O   
33   C CB  . ASP A 5   ? 0.1649 0.1535 0.2933 0.0158  0.0834  -0.0425 2   ASP A CB  
34   C CG  . ASP A 5   ? 0.2106 0.2606 0.4507 0.0002  0.0976  -0.0592 2   ASP A CG  
35   O OD1 . ASP A 5   ? 0.2357 0.3112 0.4864 -0.0129 0.1406  -0.0609 2   ASP A OD1 
36   O OD2 . ASP A 5   ? 0.2287 0.3174 0.5352 0.0004  0.1064  -0.0832 2   ASP A OD2 
37   N N   . ALA A 6   ? 0.1290 0.1589 0.1570 0.0062  0.0050  0.0506  3   ALA A N   
38   C CA  . ALA A 6   ? 0.1244 0.1855 0.1648 -0.0143 -0.0060 0.0602  3   ALA A CA  
39   C C   . ALA A 6   ? 0.1184 0.0936 0.1246 -0.0190 0.0065  0.0202  3   ALA A C   
40   O O   . ALA A 6   ? 0.1143 0.1099 0.1615 -0.0070 -0.0011 0.0314  3   ALA A O   
41   C CB  . ALA A 6   ? 0.1456 0.2184 0.1748 -0.0386 0.0030  0.0703  3   ALA A CB  
42   N N   . PHE A 7   ? 0.1223 0.0751 0.1450 0.0275  0.0106  0.0046  4   PHE A N   
43   C CA  . PHE A 7   ? 0.1221 0.0493 0.1491 0.0103  -0.0138 -0.0101 4   PHE A CA  
44   C C   . PHE A 7   ? 0.1193 0.0532 0.1080 0.0048  0.0065  -0.0179 4   PHE A C   
45   O O   . PHE A 7   ? 0.1103 0.1110 0.1714 -0.0190 -0.0364 0.0176  4   PHE A O   
46   C CB  . PHE A 7   ? 0.1215 0.0713 0.1428 0.0051  0.0040  -0.0042 4   PHE A CB  
47   C CG  . PHE A 7   ? 0.1223 0.0896 0.1800 0.0036  -0.0148 -0.0088 4   PHE A CG  
48   C CD1 . PHE A 7   ? 0.1160 0.1359 0.1053 0.0099  0.0120  -0.0130 4   PHE A CD1 
49   C CD2 . PHE A 7   ? 0.1251 0.1046 0.1833 -0.0059 -0.0325 -0.0219 4   PHE A CD2 
50   C CE1 . PHE A 7   ? 0.1214 0.1486 0.2044 0.0236  0.0070  -0.0208 4   PHE A CE1 
51   C CE2 . PHE A 7   ? 0.1167 0.1391 0.1803 0.0104  0.0068  -0.0105 4   PHE A CE2 
52   C CZ  . PHE A 7   ? 0.1140 0.1270 0.2314 0.0167  0.0066  -0.0252 4   PHE A CZ  
53   N N   . VAL A 8   ? 0.1221 0.0807 0.1073 0.0031  0.0297  -0.0200 5   VAL A N   
54   C CA  . VAL A 8   ? 0.1334 0.0825 0.0968 -0.0178 -0.0032 -0.0037 5   VAL A CA  
55   C C   . VAL A 8   ? 0.1321 0.0370 0.1218 0.0023  0.0140  -0.0066 5   VAL A C   
56   O O   . VAL A 8   ? 0.1426 0.0666 0.1641 0.0320  0.0024  0.0039  5   VAL A O   
57   C CB  . VAL A 8   ? 0.1523 0.0751 0.1975 -0.0220 0.0238  0.0409  5   VAL A CB  
58   C CG1 . VAL A 8   ? 0.1575 0.0883 0.1993 -0.0287 0.0548  0.0246  5   VAL A CG1 
59   C CG2 . VAL A 8   ? 0.1673 0.1742 0.2369 -0.0095 0.0604  0.0150  5   VAL A CG2 
60   N N   . GLY A 9   ? 0.1231 0.0994 0.1158 -0.0213 -0.0105 -0.0158 6   GLY A N   
61   C CA  . GLY A 9   ? 0.1166 0.0873 0.1722 -0.0197 -0.0033 0.0048  6   GLY A CA  
62   C C   . GLY A 9   ? 0.1181 0.0710 0.1423 -0.0001 -0.0109 0.0177  6   GLY A C   
63   O O   . GLY A 9   ? 0.1212 0.0854 0.1892 -0.0066 -0.0050 0.0021  6   GLY A O   
64   N N   . THR A 10  ? 0.1242 0.1241 0.1340 -0.0162 -0.0168 -0.0183 7   THR A N   
65   C CA  . THR A 10  ? 0.1280 0.0561 0.1765 0.0013  -0.0052 0.0162  7   THR A CA  
66   C C   . THR A 10  ? 0.1206 0.0575 0.1533 0.0113  -0.0044 0.0293  7   THR A C   
67   O O   . THR A 10  ? 0.0997 0.0614 0.1821 0.0219  -0.0005 0.0176  7   THR A O   
68   C CB  . THR A 10  ? 0.1476 0.0593 0.1212 0.0089  0.0145  0.0108  7   THR A CB  
69   O OG1 . THR A 10  ? 0.1451 0.0673 0.1976 -0.0022 0.0018  0.0100  7   THR A OG1 
70   C CG2 . THR A 10  ? 0.1568 0.1179 0.1353 -0.0009 0.0333  0.0136  7   THR A CG2 
71   N N   . TRP A 11  ? 0.1116 0.0600 0.1542 0.0046  0.0090  -0.0122 8   TRP A N   
72   C CA  . TRP A 11  ? 0.1080 0.1339 0.0675 0.0028  0.0062  -0.0405 8   TRP A CA  
73   C C   . TRP A 11  ? 0.1208 0.1015 0.1522 0.0103  -0.0007 0.0402  8   TRP A C   
74   O O   . TRP A 11  ? 0.1341 0.1022 0.2238 -0.0075 -0.0020 0.0398  8   TRP A O   
75   C CB  . TRP A 11  ? 0.0947 0.1038 0.1376 -0.0165 -0.0075 0.0026  8   TRP A CB  
76   C CG  . TRP A 11  ? 0.0965 0.0744 0.1745 -0.0101 0.0042  0.0195  8   TRP A CG  
77   C CD1 . TRP A 11  ? 0.1122 0.1197 0.1460 0.0127  -0.0036 -0.0058 8   TRP A CD1 
78   C CD2 . TRP A 11  ? 0.1032 0.0715 0.1649 0.0016  0.0146  0.0147  8   TRP A CD2 
79   N NE1 . TRP A 11  ? 0.1171 0.1235 0.1679 0.0250  0.0140  0.0198  8   TRP A NE1 
80   C CE2 . TRP A 11  ? 0.1090 0.0673 0.1613 0.0256  0.0331  0.0394  8   TRP A CE2 
81   C CE3 . TRP A 11  ? 0.1276 0.0640 0.1524 0.0098  0.0116  0.0182  8   TRP A CE3 
82   C CZ2 . TRP A 11  ? 0.1060 0.0515 0.1525 0.0031  0.0205  0.0049  8   TRP A CZ2 
83   C CZ3 . TRP A 11  ? 0.1251 0.1129 0.1243 -0.0032 0.0112  -0.0085 8   TRP A CZ3 
84   C CH2 . TRP A 11  ? 0.1148 0.0780 0.1718 -0.0134 0.0291  -0.0172 8   TRP A CH2 
85   N N   . LYS A 12  ? 0.1219 0.0959 0.1379 0.0010  0.0010  -0.0034 9   LYS A N   
86   C CA  . LYS A 12  ? 0.1395 0.0692 0.1455 0.0015  0.0158  -0.0056 9   LYS A CA  
87   C C   . LYS A 12  ? 0.1254 0.0769 0.1518 -0.0019 0.0352  -0.0246 9   LYS A C   
88   O O   . LYS A 12  ? 0.1237 0.1339 0.1740 0.0105  0.0056  0.0064  9   LYS A O   
89   C CB  . LYS A 12  ? 0.1742 0.0702 0.1534 0.0178  -0.0094 -0.0460 9   LYS A CB  
90   C CG  . LYS A 12  ? 0.1898 0.0662 0.1722 -0.0126 -0.0183 -0.0384 9   LYS A CG  
91   C CD  . LYS A 12  ? 0.2136 0.0627 0.2129 -0.0261 -0.0121 -0.0093 9   LYS A CD  
92   C CE  . LYS A 12  ? 0.2237 0.0987 0.2310 -0.0196 -0.0164 0.0054  9   LYS A CE  
93   N NZ  . LYS A 12  ? 0.2371 0.1193 0.2423 -0.0228 -0.0138 -0.0604 9   LYS A NZ  
94   N N   . LEU A 13  ? 0.1269 0.1428 0.1513 -0.0033 0.0282  -0.0220 10  LEU A N   
95   C CA  . LEU A 13  ? 0.1236 0.1530 0.1902 0.0161  0.0267  -0.0108 10  LEU A CA  
96   C C   . LEU A 13  ? 0.1248 0.1587 0.2266 -0.0303 0.0341  -0.0366 10  LEU A C   
97   O O   . LEU A 13  ? 0.1272 0.2225 0.2271 -0.0439 0.0074  -0.0486 10  LEU A O   
98   C CB  . LEU A 13  ? 0.1265 0.1905 0.1825 0.0551  -0.0113 -0.0119 10  LEU A CB  
99   C CG  . LEU A 13  ? 0.1377 0.1229 0.1871 0.0437  -0.0249 -0.0282 10  LEU A CG  
100  C CD1 . LEU A 13  ? 0.1526 0.1115 0.1250 -0.0126 -0.0286 -0.0089 10  LEU A CD1 
101  C CD2 . LEU A 13  ? 0.1340 0.1717 0.2453 0.0450  -0.0644 -0.0333 10  LEU A CD2 
102  N N   . VAL A 14  ? 0.1228 0.1173 0.2282 -0.0216 0.0477  -0.0289 11  VAL A N   
103  C CA  . VAL A 14  ? 0.1185 0.1222 0.2123 -0.0329 0.0251  -0.0243 11  VAL A CA  
104  C C   . VAL A 14  ? 0.1118 0.0892 0.2446 -0.0304 0.0210  -0.0269 11  VAL A C   
105  O O   . VAL A 14  ? 0.1131 0.1982 0.3055 -0.0516 0.0427  -0.0590 11  VAL A O   
106  C CB  . VAL A 14  ? 0.1281 0.1270 0.2998 -0.0269 0.0333  0.0079  11  VAL A CB  
107  C CG1 . VAL A 14  ? 0.1407 0.1100 0.3205 -0.0274 -0.0073 0.0089  11  VAL A CG1 
108  C CG2 . VAL A 14  ? 0.1283 0.1878 0.3061 0.0086  0.0540  -0.0499 11  VAL A CG2 
109  N N   . SER A 15  ? 0.1068 0.0772 0.2262 -0.0040 0.0254  -0.0394 12  SER A N   
110  C CA  . SER A 15  ? 0.0979 0.0796 0.2268 -0.0162 0.0288  -0.0061 12  SER A CA  
111  C C   . SER A 15  ? 0.0980 0.0861 0.2185 -0.0276 0.0157  -0.0428 12  SER A C   
112  O O   . SER A 15  ? 0.0868 0.0877 0.2059 -0.0293 0.0040  -0.0336 12  SER A O   
113  C CB  . SER A 15  ? 0.1107 0.1321 0.2200 -0.0169 0.0180  0.0213  12  SER A CB  
114  O OG  . SER A 15  ? 0.1083 0.1844 0.2191 -0.0022 0.0129  0.0231  12  SER A OG  
115  N N   . SER A 16  ? 0.1232 0.1273 0.2318 -0.0249 0.0297  -0.0244 13  SER A N   
116  C CA  . SER A 16  ? 0.1431 0.1195 0.2156 0.0062  0.0392  -0.0395 13  SER A CA  
117  C C   . SER A 16  ? 0.1465 0.0816 0.2242 -0.0125 0.0402  -0.0383 13  SER A C   
118  O O   . SER A 16  ? 0.1436 0.1389 0.2891 -0.0586 0.0425  -0.0370 13  SER A O   
119  C CB  . SER A 16  ? 0.1520 0.1420 0.2110 0.0083  -0.0006 0.0320  13  SER A CB  
120  O OG  . SER A 16  ? 0.1569 0.1704 0.2315 0.0322  -0.0042 0.0117  13  SER A OG  
121  N N   . GLU A 17  ? 0.1448 0.1144 0.1792 0.0072  0.0251  -0.0395 14  GLU A N   
122  C CA  . GLU A 17  ? 0.1651 0.1364 0.1482 -0.0141 0.0523  0.0103  14  GLU A CA  
123  C C   . GLU A 17  ? 0.1449 0.0912 0.1592 -0.0113 0.0416  0.0158  14  GLU A C   
124  O O   . GLU A 17  ? 0.1481 0.0842 0.1949 -0.0297 0.0281  -0.0088 14  GLU A O   
125  C CB  . GLU A 17  ? 0.2108 0.2362 0.1442 -0.0184 0.0494  0.0225  14  GLU A CB  
126  C CG  . GLU A 17  ? 0.2597 0.3439 0.3068 -0.0133 0.0261  0.0463  14  GLU A CG  
127  C CD  . GLU A 17  ? 0.3005 0.3888 0.4083 -0.0487 -0.0196 0.0839  14  GLU A CD  
128  O OE1 . GLU A 17  ? 0.3305 0.4102 0.5503 -0.0606 -0.0259 0.1480  14  GLU A OE1 
129  O OE2 . GLU A 17  ? 0.2946 0.4012 0.3008 -0.0955 -0.0728 0.0972  14  GLU A OE2 
130  N N   . ASN A 18  ? 0.1237 0.1296 0.1464 0.0202  0.0119  0.0005  15  ASN A N   
131  C CA  . ASN A 18  ? 0.1290 0.1106 0.1771 0.0229  0.0081  0.0059  15  ASN A CA  
132  C C   . ASN A 18  ? 0.1228 0.0954 0.1495 0.0217  0.0133  -0.0060 15  ASN A C   
133  O O   . ASN A 18  ? 0.1175 0.1310 0.1861 0.0196  0.0253  -0.0096 15  ASN A O   
134  C CB  . ASN A 18  ? 0.1409 0.1322 0.1533 0.0123  0.0075  -0.0049 15  ASN A CB  
135  C CG  . ASN A 18  ? 0.1412 0.2104 0.1926 0.0001  0.0040  0.0572  15  ASN A CG  
136  O OD1 . ASN A 18  ? 0.1361 0.2494 0.2074 -0.0342 0.0112  0.0081  15  ASN A OD1 
137  N ND2 . ASN A 18  ? 0.1454 0.2600 0.2447 0.0057  -0.0147 0.0051  15  ASN A ND2 
138  N N   . PHE A 19  ? 0.1358 0.1259 0.1453 0.0225  0.0201  0.0165  16  PHE A N   
139  C CA  . PHE A 19  ? 0.1598 0.1477 0.2044 0.0657  0.0529  0.0062  16  PHE A CA  
140  C C   . PHE A 19  ? 0.1354 0.1636 0.1793 0.0266  0.0392  -0.0095 16  PHE A C   
141  O O   . PHE A 19  ? 0.1238 0.1579 0.1377 0.0078  0.0324  0.0069  16  PHE A O   
142  C CB  . PHE A 19  ? 0.2002 0.2082 0.1867 0.0662  0.0628  0.0200  16  PHE A CB  
143  C CG  . PHE A 19  ? 0.2306 0.2438 0.2250 0.0934  0.0989  0.0437  16  PHE A CG  
144  C CD1 . PHE A 19  ? 0.2497 0.2640 0.2461 0.0876  0.1315  0.0920  16  PHE A CD1 
145  C CD2 . PHE A 19  ? 0.2392 0.2520 0.2341 0.1300  0.0791  0.0824  16  PHE A CD2 
146  C CE1 . PHE A 19  ? 0.2672 0.2881 0.3052 0.1107  0.1149  0.0724  16  PHE A CE1 
147  C CE2 . PHE A 19  ? 0.2515 0.2995 0.2884 0.1245  0.0931  0.1018  16  PHE A CE2 
148  C CZ  . PHE A 19  ? 0.2646 0.3054 0.3002 0.1167  0.1095  0.1118  16  PHE A CZ  
149  N N   . ASP A 20  ? 0.1247 0.1774 0.1656 0.0147  0.0452  -0.0040 17  ASP A N   
150  C CA  . ASP A 20  ? 0.1154 0.1434 0.1915 -0.0214 0.0270  -0.0072 17  ASP A CA  
151  C C   . ASP A 20  ? 0.1035 0.1865 0.1718 -0.0109 0.0264  0.0031  17  ASP A C   
152  O O   . ASP A 20  ? 0.0995 0.1959 0.2016 -0.0162 0.0067  0.0415  17  ASP A O   
153  C CB  . ASP A 20  ? 0.1366 0.1895 0.2541 -0.0233 -0.0122 -0.0270 17  ASP A CB  
154  C CG  . ASP A 20  ? 0.1796 0.2681 0.2967 0.0093  -0.0231 -0.0280 17  ASP A CG  
155  O OD1 . ASP A 20  ? 0.1984 0.3033 0.3291 -0.0105 -0.0322 0.0015  17  ASP A OD1 
156  O OD2 . ASP A 20  ? 0.2029 0.3204 0.3291 0.0217  -0.0685 -0.0794 17  ASP A OD2 
157  N N   . ASP A 21  ? 0.1057 0.1855 0.1606 -0.0012 0.0340  0.0193  18  ASP A N   
158  C CA  . ASP A 21  ? 0.1141 0.1512 0.2168 -0.0148 0.0389  0.0064  18  ASP A CA  
159  C C   . ASP A 21  ? 0.1012 0.1107 0.2460 0.0116  0.0245  0.0185  18  ASP A C   
160  O O   . ASP A 21  ? 0.1152 0.1227 0.2120 0.0113  0.0174  0.0236  18  ASP A O   
161  C CB  . ASP A 21  ? 0.1361 0.1406 0.2295 0.0222  0.0309  0.0485  18  ASP A CB  
162  C CG  . ASP A 21  ? 0.1409 0.2018 0.2182 0.0307  0.0242  0.0882  18  ASP A CG  
163  O OD1 . ASP A 21  ? 0.1345 0.1930 0.2481 0.0182  0.0225  0.0550  18  ASP A OD1 
164  O OD2 . ASP A 21  ? 0.1619 0.3161 0.3485 0.0202  0.0286  0.0759  18  ASP A OD2 
165  N N   . TYR A 22  ? 0.0874 0.1278 0.2424 0.0086  0.0298  -0.0283 19  TYR A N   
166  C CA  . TYR A 22  ? 0.0931 0.1550 0.2249 0.0304  0.0244  0.0178  19  TYR A CA  
167  C C   . TYR A 22  ? 0.1031 0.0994 0.1949 0.0354  0.0273  -0.0098 19  TYR A C   
168  O O   . TYR A 22  ? 0.1037 0.1140 0.2408 0.0183  0.0165  -0.0146 19  TYR A O   
169  C CB  . TYR A 22  ? 0.0847 0.0993 0.2084 0.0297  0.0285  0.0386  19  TYR A CB  
170  C CG  . TYR A 22  ? 0.0814 0.1084 0.1700 -0.0057 0.0174  0.0174  19  TYR A CG  
171  C CD1 . TYR A 22  ? 0.0687 0.1594 0.2264 0.0177  0.0059  -0.0120 19  TYR A CD1 
172  C CD2 . TYR A 22  ? 0.0999 0.1546 0.1381 0.0066  0.0292  0.0468  19  TYR A CD2 
173  C CE1 . TYR A 22  ? 0.0821 0.1027 0.2582 0.0065  0.0374  -0.0077 19  TYR A CE1 
174  C CE2 . TYR A 22  ? 0.1043 0.1077 0.1764 0.0011  0.0085  0.0294  19  TYR A CE2 
175  C CZ  . TYR A 22  ? 0.0794 0.1307 0.1601 0.0081  0.0201  -0.0119 19  TYR A CZ  
176  O OH  . TYR A 22  ? 0.0981 0.1538 0.1997 0.0147  0.0338  0.0233  19  TYR A OH  
177  N N   . MET A 23  ? 0.1116 0.1715 0.1403 0.0337  -0.0016 -0.0073 20  MET A N   
178  C CA  . MET A 23  ? 0.1354 0.1706 0.1389 0.0513  0.0001  0.0022  20  MET A CA  
179  C C   . MET A 23  ? 0.1494 0.1336 0.2170 0.0466  -0.0105 -0.0075 20  MET A C   
180  O O   . MET A 23  ? 0.1653 0.1534 0.2403 0.0401  -0.0159 0.0299  20  MET A O   
181  C CB  . MET A 23  ? 0.1591 0.2568 0.2307 0.0756  -0.0479 -0.0684 20  MET A CB  
182  C CG  . MET A 23  ? 0.1595 0.2058 0.1393 0.0697  0.0149  -0.0638 20  MET A CG  
183  S SD  . MET A 23  ? 0.1682 0.1793 0.1920 0.0514  0.0284  0.0123  20  MET A SD  
184  C CE  . MET A 23  ? 0.1794 0.2245 0.2273 0.0095  0.0406  0.0010  20  MET A CE  
185  N N   . LYS A 24  ? 0.1624 0.1398 0.2255 0.0259  -0.0230 0.0227  21  LYS A N   
186  C CA  . LYS A 24  ? 0.1736 0.1470 0.3004 0.0476  -0.0206 -0.0405 21  LYS A CA  
187  C C   . LYS A 24  ? 0.1747 0.1270 0.2957 0.0466  0.0088  -0.0443 21  LYS A C   
188  O O   . LYS A 24  ? 0.1884 0.1320 0.3514 0.0345  -0.0460 -0.0366 21  LYS A O   
189  C CB  . LYS A 24  ? 0.1908 0.2397 0.4497 0.0622  -0.0207 -0.0484 21  LYS A CB  
190  C CG  . LYS A 24  ? 0.2137 0.3451 0.6463 0.0962  0.0107  -0.0059 21  LYS A CG  
191  C CD  . LYS A 24  ? 0.2303 0.4412 0.7834 0.0904  0.0023  0.0029  21  LYS A CD  
192  C CE  . LYS A 24  ? 0.3613 0.6143 1.0045 0.0000  -0.0544 0.0000  21  LYS A CE  
193  N NZ  . LYS A 24  ? 0.3181 0.5938 0.9988 0.0636  -0.0153 -0.0530 21  LYS A NZ  
194  N N   . GLU A 25  ? 0.1615 0.1149 0.2745 0.0472  0.0271  0.0302  22  GLU A N   
195  C CA  . GLU A 25  ? 0.1809 0.1261 0.2696 0.0341  0.0093  -0.0178 22  GLU A CA  
196  C C   . GLU A 25  ? 0.1799 0.1389 0.2728 0.0119  -0.0279 -0.0262 22  GLU A C   
197  O O   . GLU A 25  ? 0.1873 0.1389 0.3071 0.0231  -0.0207 -0.0119 22  GLU A O   
198  C CB  . GLU A 25  ? 0.1948 0.1825 0.3213 0.0523  0.0229  0.0240  22  GLU A CB  
199  C CG  . GLU A 25  ? 0.2299 0.2746 0.4156 0.0552  0.0224  0.0084  22  GLU A CG  
200  C CD  . GLU A 25  ? 0.2611 0.2895 0.4535 0.0500  0.0435  -0.0689 22  GLU A CD  
201  O OE1 . GLU A 25  ? 0.2743 0.3488 0.5413 0.0243  0.0381  -0.0704 22  GLU A OE1 
202  O OE2 . GLU A 25  ? 0.2756 0.3099 0.5251 0.0413  0.0324  -0.1495 22  GLU A OE2 
203  N N   . VAL A 26  ? 0.1708 0.1266 0.2632 0.0144  -0.0059 0.0108  23  VAL A N   
204  C CA  . VAL A 26  ? 0.1760 0.1124 0.2654 0.0105  -0.0188 0.0002  23  VAL A CA  
205  C C   . VAL A 26  ? 0.1864 0.1457 0.3234 -0.0052 -0.0313 -0.0010 23  VAL A C   
206  O O   . VAL A 26  ? 0.2014 0.1924 0.4015 -0.0154 -0.0576 0.0560  23  VAL A O   
207  C CB  . VAL A 26  ? 0.1813 0.1428 0.2726 0.0261  -0.0011 0.0667  23  VAL A CB  
208  C CG1 . VAL A 26  ? 0.1954 0.1228 0.3322 -0.0186 0.0234  0.0242  23  VAL A CG1 
209  C CG2 . VAL A 26  ? 0.1757 0.1922 0.2562 0.0099  0.0144  0.0437  23  VAL A CG2 
210  N N   . GLY A 27  ? 0.1802 0.1425 0.2567 0.0317  -0.0661 0.0277  24  GLY A N   
211  C CA  . GLY A 27  ? 0.1885 0.1917 0.2769 0.0295  -0.0876 0.0605  24  GLY A CA  
212  C C   . GLY A 27  ? 0.1986 0.1427 0.2705 0.0222  -0.0644 0.0793  24  GLY A C   
213  O O   . GLY A 27  ? 0.2196 0.1855 0.3114 0.0140  -0.0682 0.0666  24  GLY A O   
214  N N   . VAL A 28  ? 0.1853 0.1363 0.2688 0.0161  -0.0376 0.0535  25  VAL A N   
215  C CA  . VAL A 28  ? 0.1739 0.1690 0.3082 0.0103  -0.0753 -0.0017 25  VAL A CA  
216  C C   . VAL A 28  ? 0.1728 0.2169 0.4446 -0.0008 -0.0892 -0.0066 25  VAL A C   
217  O O   . VAL A 28  ? 0.1563 0.2170 0.4824 0.0458  -0.0637 -0.0734 25  VAL A O   
218  C CB  . VAL A 28  ? 0.1551 0.1275 0.2643 0.0069  -0.0482 0.0174  25  VAL A CB  
219  C CG1 . VAL A 28  ? 0.1682 0.1856 0.3296 -0.0170 -0.0718 0.0405  25  VAL A CG1 
220  C CG2 . VAL A 28  ? 0.1325 0.1756 0.2291 0.0017  -0.0106 0.0154  25  VAL A CG2 
221  N N   . GLY A 29  ? 0.1924 0.2311 0.5094 -0.0145 -0.1232 -0.0029 26  GLY A N   
222  C CA  . GLY A 29  ? 0.2072 0.2274 0.5480 -0.0258 -0.1407 0.0098  26  GLY A CA  
223  C C   . GLY A 29  ? 0.2135 0.2230 0.5495 -0.0143 -0.1419 -0.0354 26  GLY A C   
224  O O   . GLY A 29  ? 0.2247 0.2025 0.4958 -0.0053 -0.1484 0.0109  26  GLY A O   
225  N N   . PHE A 30  ? 0.2193 0.2558 0.5839 0.0098  -0.1521 -0.0582 27  PHE A N   
226  C CA  . PHE A 30  ? 0.2104 0.2429 0.5200 0.0358  -0.1485 -0.0623 27  PHE A CA  
227  C C   . PHE A 30  ? 0.2228 0.2264 0.5089 0.0126  -0.1517 -0.0233 27  PHE A C   
228  O O   . PHE A 30  ? 0.2096 0.2118 0.5013 0.0194  -0.1445 -0.0748 27  PHE A O   
229  C CB  . PHE A 30  ? 0.2148 0.2619 0.4619 0.0544  -0.1498 -0.0864 27  PHE A CB  
230  C CG  . PHE A 30  ? 0.2201 0.3037 0.4932 0.0712  -0.1151 -0.0991 27  PHE A CG  
231  C CD1 . PHE A 30  ? 0.2272 0.3324 0.4343 0.0520  -0.0780 -0.1540 27  PHE A CD1 
232  C CD2 . PHE A 30  ? 0.2352 0.3103 0.4990 0.0544  -0.1054 -0.1169 27  PHE A CD2 
233  C CE1 . PHE A 30  ? 0.2306 0.3646 0.3982 0.0447  -0.1018 -0.1847 27  PHE A CE1 
234  C CE2 . PHE A 30  ? 0.2311 0.3257 0.4826 0.0654  -0.0929 -0.1292 27  PHE A CE2 
235  C CZ  . PHE A 30  ? 0.2290 0.3209 0.4441 0.0525  -0.0930 -0.1870 27  PHE A CZ  
236  N N   . ALA A 31  ? 0.2519 0.2468 0.4984 0.0170  -0.1444 0.0255  28  ALA A N   
237  C CA  . ALA A 31  ? 0.2692 0.3098 0.4078 0.0121  -0.1695 0.0837  28  ALA A CA  
238  C C   . ALA A 31  ? 0.2745 0.2561 0.3850 0.0076  -0.1565 0.0780  28  ALA A C   
239  O O   . ALA A 31  ? 0.2881 0.2561 0.3160 -0.0085 -0.1603 0.0423  28  ALA A O   
240  C CB  . ALA A 31  ? 0.2694 0.3083 0.4918 0.0097  -0.1592 0.0872  28  ALA A CB  
241  N N   . THR A 32  ? 0.2679 0.2422 0.3554 -0.0132 -0.1623 0.0617  29  THR A N   
242  C CA  . THR A 32  ? 0.2625 0.2245 0.3048 -0.0366 -0.1084 0.0139  29  THR A CA  
243  C C   . THR A 32  ? 0.2340 0.2429 0.2245 0.0068  -0.0696 0.0494  29  THR A C   
244  O O   . THR A 32  ? 0.2525 0.2792 0.1828 0.0292  -0.0441 -0.0045 29  THR A O   
245  C CB  . THR A 32  ? 0.2957 0.2661 0.3036 -0.0574 -0.1058 0.0502  29  THR A CB  
246  O OG1 . THR A 32  ? 0.3146 0.2960 0.3351 -0.0739 -0.1129 0.0985  29  THR A OG1 
247  C CG2 . THR A 32  ? 0.2985 0.2905 0.3138 -0.0477 -0.0815 0.0304  29  THR A CG2 
248  N N   . ARG A 33  ? 0.1955 0.2540 0.2127 0.0476  -0.0536 0.0445  30  ARG A N   
249  C CA  . ARG A 33  ? 0.1729 0.2214 0.2075 0.0707  -0.0468 -0.0110 30  ARG A CA  
250  C C   . ARG A 33  ? 0.1638 0.2120 0.2260 0.0561  -0.0433 -0.0453 30  ARG A C   
251  O O   . ARG A 33  ? 0.1658 0.1997 0.2573 0.0348  0.0046  -0.0403 30  ARG A O   
252  C CB  . ARG A 33  ? 0.1703 0.2164 0.2363 0.0563  0.0114  -0.0524 30  ARG A CB  
253  C CG  . ARG A 33  ? 0.1822 0.2011 0.2235 0.0240  -0.0149 -0.0094 30  ARG A CG  
254  C CD  . ARG A 33  ? 0.2061 0.2879 0.3015 0.0287  -0.0079 -0.0501 30  ARG A CD  
255  N NE  . ARG A 33  ? 0.2487 0.3913 0.3455 0.0391  -0.0252 -0.0368 30  ARG A NE  
256  C CZ  . ARG A 33  ? 0.2725 0.4263 0.3788 0.0088  -0.0337 -0.0701 30  ARG A CZ  
257  N NH1 . ARG A 33  ? 0.2952 0.4170 0.4700 -0.0080 -0.0334 -0.0560 30  ARG A NH1 
258  N NH2 . ARG A 33  ? 0.2749 0.4398 0.3687 0.0176  -0.0226 -0.1318 30  ARG A NH2 
259  N N   . LYS A 34  ? 0.1673 0.2420 0.2536 0.0151  -0.0346 -0.0759 31  LYS A N   
260  C CA  . LYS A 34  ? 0.1854 0.2721 0.2580 -0.0021 -0.0427 -0.1025 31  LYS A CA  
261  C C   . LYS A 34  ? 0.2110 0.2691 0.2865 -0.0034 -0.0366 -0.0936 31  LYS A C   
262  O O   . LYS A 34  ? 0.2179 0.2365 0.3349 -0.0189 -0.0083 -0.0438 31  LYS A O   
263  C CB  . LYS A 34  ? 0.1874 0.3329 0.3256 0.0090  -0.0369 -0.0493 31  LYS A CB  
264  C CG  . LYS A 34  ? 0.1814 0.3226 0.3500 0.0016  -0.0580 -0.0311 31  LYS A CG  
265  C CD  . LYS A 34  ? 0.1715 0.2929 0.3459 0.0161  -0.0353 -0.0496 31  LYS A CD  
266  C CE  . LYS A 34  ? 0.1566 0.2897 0.3231 0.0266  -0.0223 -0.0233 31  LYS A CE  
267  N NZ  . LYS A 34  ? 0.1459 0.3064 0.2990 0.0100  -0.0077 -0.0544 31  LYS A NZ  
268  N N   . VAL A 35  ? 0.2289 0.3094 0.2848 -0.0173 -0.0535 0.0010  32  VAL A N   
269  C CA  . VAL A 35  ? 0.2563 0.3378 0.2684 0.0043  -0.0174 0.0472  32  VAL A CA  
270  C C   . VAL A 35  ? 0.2487 0.2811 0.2377 0.0052  -0.0131 0.0236  32  VAL A C   
271  O O   . VAL A 35  ? 0.2439 0.2810 0.2530 0.0257  0.0036  0.0077  32  VAL A O   
272  C CB  . VAL A 35  ? 0.2882 0.4261 0.3349 0.0156  0.0045  0.0931  32  VAL A CB  
273  C CG1 . VAL A 35  ? 0.3100 0.4676 0.3688 0.0169  -0.0029 0.0680  32  VAL A CG1 
274  C CG2 . VAL A 35  ? 0.3051 0.4475 0.4080 0.0078  0.0154  0.0501  32  VAL A CG2 
275  N N   . ALA A 36  ? 0.2480 0.2827 0.1851 -0.0144 -0.0338 0.0159  33  ALA A N   
276  C CA  . ALA A 36  ? 0.2522 0.2724 0.2167 0.0174  -0.0584 0.0035  33  ALA A CA  
277  C C   . ALA A 36  ? 0.2634 0.2495 0.2372 0.0388  -0.0202 0.0130  33  ALA A C   
278  O O   . ALA A 36  ? 0.2735 0.3023 0.2513 0.0636  -0.0041 -0.0364 33  ALA A O   
279  C CB  . ALA A 36  ? 0.2569 0.2716 0.2599 0.0100  -0.0810 -0.0478 33  ALA A CB  
280  N N   . GLY A 37  ? 0.2742 0.2415 0.2396 0.0312  -0.0132 0.0279  34  GLY A N   
281  C CA  . GLY A 37  ? 0.2836 0.2315 0.2577 0.0576  0.0054  0.0238  34  GLY A CA  
282  C C   . GLY A 37  ? 0.2886 0.2463 0.3457 0.0583  0.0696  0.0044  34  GLY A C   
283  O O   . GLY A 37  ? 0.3095 0.3027 0.4231 0.0418  0.0743  0.0228  34  GLY A O   
284  N N   A MET A 38  ? 0.2904 0.2726 0.3418 0.0556  0.0849  -0.0225 35  MET A N   
285  N N   B MET A 38  ? 0.2783 0.2641 0.3319 0.0577  0.0949  -0.0292 35  MET A N   
286  C CA  A MET A 38  ? 0.3000 0.2930 0.3430 0.0469  0.0872  -0.0511 35  MET A CA  
287  C CA  B MET A 38  ? 0.2787 0.2732 0.3201 0.0496  0.0985  -0.0641 35  MET A CA  
288  C C   A MET A 38  ? 0.2855 0.2849 0.3759 0.0346  0.0604  -0.0493 35  MET A C   
289  C C   B MET A 38  ? 0.2752 0.2787 0.3660 0.0359  0.0600  -0.0494 35  MET A C   
290  O O   A MET A 38  ? 0.2879 0.2868 0.4090 0.0258  0.0465  -0.0853 35  MET A O   
291  O O   B MET A 38  ? 0.2775 0.2906 0.3957 0.0267  0.0371  -0.0829 35  MET A O   
300  N N   . ALA A 39  ? 0.2651 0.2667 0.3418 0.0298  0.0503  -0.0238 36  ALA A N   
301  C CA  . ALA A 39  ? 0.2599 0.2525 0.3705 0.0383  0.0274  -0.0201 36  ALA A CA  
302  C C   . ALA A 39  ? 0.2590 0.3146 0.4604 0.0253  0.0034  -0.0496 36  ALA A C   
303  O O   . ALA A 39  ? 0.2722 0.3596 0.4727 0.0296  -0.0034 -0.0389 36  ALA A O   
304  C CB  . ALA A 39  ? 0.2641 0.2561 0.3158 0.0229  0.0431  0.0064  36  ALA A CB  
305  N N   . LYS A 40  ? 0.2447 0.2707 0.5274 0.0113  -0.0007 -0.1250 37  LYS A N   
306  C CA  . LYS A 40  ? 0.2556 0.2493 0.6165 -0.0009 0.0189  -0.0553 37  LYS A CA  
307  C C   . LYS A 40  ? 0.2385 0.2240 0.5468 -0.0020 0.0135  -0.0433 37  LYS A C   
308  O O   . LYS A 40  ? 0.2373 0.2236 0.6664 -0.0089 0.0070  -0.0917 37  LYS A O   
309  C CB  . LYS A 40  ? 0.2787 0.2880 0.7258 -0.0102 0.0230  -0.0407 37  LYS A CB  
310  C CG  . LYS A 40  ? 0.3039 0.3699 0.8445 -0.0066 0.0131  -0.0160 37  LYS A CG  
311  C CD  . LYS A 40  ? 0.3291 0.4498 0.9453 0.0222  0.0083  -0.0178 37  LYS A CD  
312  C CE  . LYS A 40  ? 0.3444 0.4718 1.0241 0.0464  0.0104  -0.0401 37  LYS A CE  
313  N NZ  . LYS A 40  ? 0.3533 0.4986 1.0692 0.0504  0.0100  -0.0750 37  LYS A NZ  
314  N N   . PRO A 41  ? 0.2333 0.2324 0.3500 0.0032  0.0056  0.0162  38  PRO A N   
315  C CA  . PRO A 41  ? 0.2331 0.2148 0.3309 -0.0238 -0.0154 0.0339  38  PRO A CA  
316  C C   . PRO A 41  ? 0.2225 0.2230 0.3676 -0.0219 -0.0674 0.0386  38  PRO A C   
317  O O   . PRO A 41  ? 0.2232 0.2602 0.3978 -0.0456 -0.0784 0.1077  38  PRO A O   
318  C CB  . PRO A 41  ? 0.2474 0.2734 0.3407 -0.0371 0.0006  -0.0657 38  PRO A CB  
319  C CG  . PRO A 41  ? 0.2474 0.3158 0.3848 -0.0103 0.0192  -0.0369 38  PRO A CG  
320  C CD  . PRO A 41  ? 0.2449 0.3023 0.3527 -0.0140 0.0019  0.0202  38  PRO A CD  
321  N N   . ASN A 42  ? 0.2043 0.1663 0.3444 0.0047  -0.0911 0.0100  39  ASN A N   
322  C CA  . ASN A 42  ? 0.2122 0.1360 0.3579 0.0007  -0.0979 0.0689  39  ASN A CA  
323  C C   . ASN A 42  ? 0.2151 0.1531 0.3812 -0.0020 -0.1003 0.0842  39  ASN A C   
324  O O   . ASN A 42  ? 0.2430 0.2088 0.4384 -0.0203 -0.1328 0.1205  39  ASN A O   
325  C CB  . ASN A 42  ? 0.2416 0.1737 0.4975 0.0084  -0.0867 0.0010  39  ASN A CB  
326  C CG  . ASN A 42  ? 0.2812 0.2439 0.5875 0.0120  -0.0666 0.0614  39  ASN A CG  
327  O OD1 . ASN A 42  ? 0.2986 0.2105 0.5863 0.0467  -0.0657 0.0306  39  ASN A OD1 
328  N ND2 . ASN A 42  ? 0.2858 0.2639 0.6025 -0.0123 -0.0546 0.0582  39  ASN A ND2 
329  N N   . MET A 43  ? 0.1927 0.1191 0.2682 -0.0237 -0.0413 0.0492  40  MET A N   
330  C CA  . MET A 43  ? 0.1819 0.0796 0.2218 0.0195  -0.0196 0.0181  40  MET A CA  
331  C C   . MET A 43  ? 0.1509 0.0996 0.2335 -0.0197 -0.0121 0.0677  40  MET A C   
332  O O   . MET A 43  ? 0.1430 0.0909 0.2972 0.0056  0.0092  0.0478  40  MET A O   
333  C CB  . MET A 43  ? 0.2036 0.1590 0.2018 0.0047  -0.0078 0.0590  40  MET A CB  
334  C CG  . MET A 43  ? 0.2283 0.2496 0.1979 -0.0208 0.0206  0.0249  40  MET A CG  
335  S SD  . MET A 43  ? 0.2409 0.2719 0.3053 -0.0521 0.0837  -0.0057 40  MET A SD  
336  C CE  . MET A 43  ? 0.2296 0.2951 0.3029 -0.0659 0.1059  -0.0088 40  MET A CE  
337  N N   . ILE A 44  ? 0.1317 0.1108 0.1846 -0.0224 0.0031  0.0371  41  ILE A N   
338  C CA  . ILE A 44  ? 0.1397 0.1021 0.1754 -0.0194 -0.0088 0.0266  41  ILE A CA  
339  C C   . ILE A 44  ? 0.1310 0.0689 0.1823 -0.0040 -0.0217 -0.0083 41  ILE A C   
340  O O   . ILE A 44  ? 0.1456 0.0637 0.2285 -0.0143 -0.0044 0.0214  41  ILE A O   
341  C CB  . ILE A 44  ? 0.1653 0.1510 0.1829 -0.0257 -0.0150 -0.0176 41  ILE A CB  
342  C CG1 . ILE A 44  ? 0.1886 0.1833 0.2019 -0.0302 -0.0669 0.0284  41  ILE A CG1 
343  C CG2 . ILE A 44  ? 0.1678 0.1250 0.1731 -0.0429 -0.0106 -0.0175 41  ILE A CG2 
344  C CD1 . ILE A 44  ? 0.2182 0.2840 0.3836 -0.0297 -0.0872 0.0065  41  ILE A CD1 
345  N N   . ILE A 45  ? 0.1249 0.1123 0.1459 -0.0099 -0.0269 -0.0152 42  ILE A N   
346  C CA  . ILE A 45  ? 0.1158 0.1305 0.0912 -0.0109 -0.0361 -0.0182 42  ILE A CA  
347  C C   . ILE A 45  ? 0.1289 0.0763 0.1533 0.0054  0.0258  0.0050  42  ILE A C   
348  O O   . ILE A 45  ? 0.1488 0.0603 0.1946 0.0083  -0.0106 0.0205  42  ILE A O   
349  C CB  . ILE A 45  ? 0.1254 0.1020 0.0797 0.0055  -0.0058 -0.0063 42  ILE A CB  
350  C CG1 . ILE A 45  ? 0.1232 0.1592 0.1077 0.0251  0.0325  -0.0115 42  ILE A CG1 
351  C CG2 . ILE A 45  ? 0.1503 0.1432 0.1213 -0.0202 0.0104  -0.0473 42  ILE A CG2 
352  C CD1 . ILE A 45  ? 0.1347 0.1360 0.1992 0.0071  0.0211  0.0154  42  ILE A CD1 
353  N N   . SER A 46  ? 0.1266 0.0853 0.1431 -0.0221 0.0226  0.0389  43  SER A N   
354  C CA  . SER A 46  ? 0.1384 0.0825 0.1364 -0.0126 0.0556  -0.0049 43  SER A CA  
355  C C   . SER A 46  ? 0.1486 0.0486 0.1189 -0.0024 0.0271  0.0203  43  SER A C   
356  O O   . SER A 46  ? 0.1446 0.0582 0.2185 0.0022  0.0269  -0.0061 43  SER A O   
357  C CB  . SER A 46  ? 0.1488 0.0889 0.1575 -0.0032 0.0288  -0.0169 43  SER A CB  
358  O OG  . SER A 46  ? 0.1506 0.0859 0.1739 0.0140  0.0241  0.0134  43  SER A OG  
359  N N   . VAL A 47  ? 0.1555 0.0744 0.1178 0.0017  0.0299  -0.0054 44  VAL A N   
360  C CA  . VAL A 47  ? 0.1580 0.1059 0.0978 -0.0428 0.0273  0.0332  44  VAL A CA  
361  C C   . VAL A 47  ? 0.1543 0.0668 0.1240 -0.0190 0.0200  0.0027  44  VAL A C   
362  O O   . VAL A 47  ? 0.1426 0.0689 0.1874 0.0075  0.0076  -0.0104 44  VAL A O   
363  C CB  . VAL A 47  ? 0.1767 0.1635 0.0983 -0.0761 0.0115  0.0301  44  VAL A CB  
364  C CG1 . VAL A 47  ? 0.1981 0.3249 0.1372 -0.1141 -0.0248 0.0466  44  VAL A CG1 
365  C CG2 . VAL A 47  ? 0.1852 0.1421 0.1930 -0.0060 0.0065  0.0514  44  VAL A CG2 
366  N N   . ASN A 48  ? 0.1232 0.1256 0.1172 -0.0150 0.0323  0.0083  45  ASN A N   
367  C CA  . ASN A 48  ? 0.1234 0.0678 0.1397 -0.0038 0.0259  0.0103  45  ASN A CA  
368  C C   . ASN A 48  ? 0.1271 0.0679 0.1741 -0.0142 0.0174  -0.0185 45  ASN A C   
369  O O   . ASN A 48  ? 0.1227 0.0686 0.1613 -0.0120 0.0159  -0.0009 45  ASN A O   
370  C CB  . ASN A 48  ? 0.1321 0.1310 0.0945 -0.0342 0.0230  0.0166  45  ASN A CB  
371  C CG  . ASN A 48  ? 0.1267 0.1025 0.0983 -0.0335 0.0414  -0.0304 45  ASN A CG  
372  O OD1 . ASN A 48  ? 0.1337 0.1874 0.1728 -0.0466 0.0523  -0.0145 45  ASN A OD1 
373  N ND2 . ASN A 48  ? 0.1371 0.1019 0.1488 0.0046  0.0195  -0.0460 45  ASN A ND2 
374  N N   . GLY A 49  ? 0.1184 0.1048 0.1710 -0.0196 0.0443  -0.0294 46  GLY A N   
375  C CA  . GLY A 49  ? 0.1219 0.0793 0.1628 -0.0080 0.0166  -0.0057 46  GLY A CA  
376  C C   . GLY A 49  ? 0.1348 0.0945 0.1757 -0.0261 0.0195  -0.0047 46  GLY A C   
377  O O   . GLY A 49  ? 0.1505 0.1197 0.1685 -0.0302 0.0117  -0.0050 46  GLY A O   
378  N N   . ASP A 50  ? 0.1301 0.0866 0.1689 0.0210  0.0457  -0.0193 47  ASP A N   
379  C CA  . ASP A 50  ? 0.1334 0.0840 0.1240 0.0229  0.0099  -0.0257 47  ASP A CA  
380  C C   . ASP A 50  ? 0.1275 0.1360 0.0998 0.0268  0.0413  -0.0300 47  ASP A C   
381  O O   . ASP A 50  ? 0.1364 0.1661 0.1333 -0.0141 0.0228  -0.0368 47  ASP A O   
382  C CB  . ASP A 50  ? 0.1384 0.0754 0.1603 0.0080  0.0062  -0.0377 47  ASP A CB  
383  C CG  . ASP A 50  ? 0.1546 0.1660 0.1496 -0.0175 -0.0438 0.0377  47  ASP A CG  
384  O OD1 . ASP A 50  ? 0.1863 0.2789 0.1889 -0.0425 -0.0941 0.0703  47  ASP A OD1 
385  O OD2 . ASP A 50  ? 0.1605 0.1723 0.1566 0.0285  0.0049  0.0265  47  ASP A OD2 
386  N N   . VAL A 51  ? 0.1229 0.1142 0.0876 -0.0042 -0.0013 -0.0066 48  VAL A N   
387  C CA  . VAL A 51  ? 0.1121 0.0938 0.1419 0.0163  0.0013  0.0003  48  VAL A CA  
388  C C   . VAL A 51  ? 0.1263 0.0640 0.1320 0.0192  0.0423  -0.0200 48  VAL A C   
389  O O   . VAL A 51  ? 0.1385 0.1016 0.1418 0.0139  0.0183  -0.0230 48  VAL A O   
390  C CB  . VAL A 51  ? 0.1249 0.0727 0.1791 0.0071  0.0244  0.0084  48  VAL A CB  
391  C CG1 . VAL A 51  ? 0.1276 0.0792 0.1893 0.0204  0.0100  -0.0030 48  VAL A CG1 
392  C CG2 . VAL A 51  ? 0.1486 0.0782 0.1856 -0.0291 0.0245  -0.0072 48  VAL A CG2 
393  N N   . ILE A 52  ? 0.1214 0.0894 0.1220 0.0201  0.0510  0.0076  49  ILE A N   
394  C CA  . ILE A 52  ? 0.1209 0.0644 0.1668 -0.0033 0.0279  0.0047  49  ILE A CA  
395  C C   . ILE A 52  ? 0.1131 0.1147 0.1538 0.0101  0.0192  -0.0433 49  ILE A C   
396  O O   . ILE A 52  ? 0.1176 0.0861 0.1688 0.0043  -0.0013 -0.0174 49  ILE A O   
397  C CB  . ILE A 52  ? 0.1376 0.1229 0.1599 -0.0065 0.0245  -0.0209 49  ILE A CB  
398  C CG1 . ILE A 52  ? 0.1697 0.2678 0.2406 0.0153  0.0102  -0.0279 49  ILE A CG1 
399  C CG2 . ILE A 52  ? 0.1497 0.1375 0.1518 -0.0475 0.0320  0.0229  49  ILE A CG2 
400  C CD1 . ILE A 52  ? 0.1903 0.3033 0.3094 0.0663  -0.0063 -0.1024 49  ILE A CD1 
401  N N   . THR A 53  ? 0.1053 0.0965 0.1372 0.0109  0.0400  0.0101  50  THR A N   
402  C CA  . THR A 53  ? 0.1186 0.0986 0.1836 0.0040  0.0067  0.0125  50  THR A CA  
403  C C   . THR A 53  ? 0.1253 0.0828 0.1639 0.0088  0.0338  -0.0416 50  THR A C   
404  O O   . THR A 53  ? 0.1262 0.0978 0.2208 -0.0038 0.0183  -0.0347 50  THR A O   
405  C CB  . THR A 53  ? 0.1291 0.1152 0.1935 -0.0066 0.0148  0.0150  50  THR A CB  
406  O OG1 . THR A 53  ? 0.1363 0.1025 0.1874 -0.0347 0.0143  0.0003  50  THR A OG1 
407  C CG2 . THR A 53  ? 0.1373 0.0911 0.1781 0.0297  -0.0108 0.0196  50  THR A CG2 
408  N N   . ILE A 54  ? 0.1401 0.0788 0.1452 -0.0035 0.0513  -0.0007 51  ILE A N   
409  C CA  . ILE A 54  ? 0.1371 0.0790 0.1380 -0.0201 0.0087  0.0138  51  ILE A CA  
410  C C   . ILE A 54  ? 0.1475 0.0670 0.1477 -0.0273 -0.0218 0.0392  51  ILE A C   
411  O O   . ILE A 54  ? 0.1556 0.0732 0.1726 -0.0107 -0.0085 0.0352  51  ILE A O   
412  C CB  . ILE A 54  ? 0.1410 0.1280 0.1299 -0.0055 0.0141  0.0479  51  ILE A CB  
413  C CG1 . ILE A 54  ? 0.1579 0.1581 0.1018 0.0202  0.0027  0.0202  51  ILE A CG1 
414  C CG2 . ILE A 54  ? 0.1322 0.1489 0.2157 -0.0139 0.0189  0.0607  51  ILE A CG2 
415  C CD1 . ILE A 54  ? 0.1529 0.1623 0.1332 0.0177  0.0303  0.0243  51  ILE A CD1 
416  N N   . LYS A 55  ? 0.1520 0.1140 0.1655 -0.0227 -0.0595 0.0093  52  LYS A N   
417  C CA  . LYS A 55  ? 0.1779 0.0647 0.2156 -0.0047 -0.0431 0.0036  52  LYS A CA  
418  C C   . LYS A 55  ? 0.1678 0.0843 0.2378 -0.0156 -0.0343 0.0270  52  LYS A C   
419  O O   . LYS A 55  ? 0.1732 0.1085 0.2930 -0.0100 -0.0406 0.0725  52  LYS A O   
420  C CB  . LYS A 55  ? 0.2257 0.1419 0.2067 0.0077  -0.0813 -0.0471 52  LYS A CB  
421  C CG  . LYS A 55  ? 0.2686 0.2166 0.2560 0.0102  -0.0808 -0.0372 52  LYS A CG  
422  C CD  . LYS A 55  ? 0.2929 0.3400 0.2879 -0.0114 -0.0950 -0.0199 52  LYS A CD  
423  C CE  . LYS A 55  ? 0.3071 0.4102 0.2703 -0.0082 -0.1073 -0.0248 52  LYS A CE  
424  N NZ  . LYS A 55  ? 0.3210 0.4559 0.3586 -0.0136 -0.0945 -0.0708 52  LYS A NZ  
425  N N   . SER A 56  ? 0.1649 0.1534 0.1879 -0.0204 -0.0373 0.0007  53  SER A N   
426  C CA  . SER A 56  ? 0.1820 0.1787 0.2101 -0.0188 -0.0162 0.0083  53  SER A CA  
427  C C   . SER A 56  ? 0.1860 0.1151 0.2240 -0.0249 -0.0542 -0.0048 53  SER A C   
428  O O   . SER A 56  ? 0.2095 0.1198 0.2961 -0.0051 -0.0691 0.0738  53  SER A O   
429  C CB  . SER A 56  ? 0.2090 0.2375 0.2881 -0.0223 0.0289  0.0466  53  SER A CB  
430  O OG  . SER A 56  ? 0.2276 0.3785 0.4438 -0.0234 0.0542  0.0654  53  SER A OG  
431  N N   . GLU A 57  ? 0.1711 0.1188 0.2160 -0.0142 -0.0535 0.0273  54  GLU A N   
432  C CA  . GLU A 57  ? 0.1565 0.1408 0.2557 -0.0329 -0.0148 -0.0044 54  GLU A CA  
433  C C   . GLU A 57  ? 0.1299 0.1426 0.2708 -0.0096 -0.0217 0.0664  54  GLU A C   
434  O O   . GLU A 57  ? 0.1290 0.1701 0.2790 -0.0029 -0.0271 0.0657  54  GLU A O   
435  C CB  . GLU A 57  ? 0.1765 0.1621 0.3211 -0.0204 0.0100  0.0259  54  GLU A CB  
436  C CG  . GLU A 57  ? 0.2083 0.1912 0.2476 -0.0126 0.0182  0.0329  54  GLU A CG  
437  C CD  . GLU A 57  ? 0.2340 0.2813 0.3263 0.0112  0.0326  0.0562  54  GLU A CD  
438  O OE1 . GLU A 57  ? 0.2520 0.3197 0.3505 0.0119  0.0348  0.0260  54  GLU A OE1 
439  O OE2 . GLU A 57  ? 0.2368 0.3244 0.3417 0.0415  0.0499  0.0840  54  GLU A OE2 
440  N N   . SER A 58  ? 0.1294 0.1212 0.2426 -0.0084 -0.0059 0.0343  55  SER A N   
441  C CA  . SER A 58  ? 0.1485 0.1446 0.2202 -0.0159 -0.0036 0.0309  55  SER A CA  
442  C C   . SER A 58  ? 0.1526 0.1815 0.1867 -0.0438 -0.0045 -0.0110 55  SER A C   
443  O O   . SER A 58  ? 0.1414 0.2647 0.2170 -0.0173 0.0074  0.0296  55  SER A O   
444  C CB  . SER A 58  ? 0.1792 0.1858 0.2413 -0.0146 0.0143  0.0148  55  SER A CB  
445  O OG  . SER A 58  ? 0.2035 0.2759 0.2998 0.0136  0.0178  -0.0230 55  SER A OG  
446  N N   . THR A 59  ? 0.1691 0.2479 0.2308 -0.0326 -0.0693 -0.0082 56  THR A N   
447  C CA  . THR A 59  ? 0.2029 0.2907 0.4019 -0.0444 -0.0759 0.0362  56  THR A CA  
448  C C   . THR A 59  ? 0.2154 0.3209 0.4625 -0.0568 -0.0535 0.0252  56  THR A C   
449  O O   . THR A 59  ? 0.2396 0.4243 0.5209 -0.0550 -0.0531 0.0021  56  THR A O   
450  C CB  . THR A 59  ? 0.2258 0.3195 0.5427 -0.0679 -0.1158 -0.0032 56  THR A CB  
451  O OG1 . THR A 59  ? 0.2464 0.4112 0.6380 -0.0623 -0.1053 -0.0367 56  THR A OG1 
452  C CG2 . THR A 59  ? 0.2351 0.3691 0.6442 -0.0454 -0.0990 0.0124  56  THR A CG2 
453  N N   . PHE A 60  ? 0.1990 0.2028 0.4169 -0.0360 -0.0250 0.0340  57  PHE A N   
454  C CA  . PHE A 60  ? 0.2013 0.2238 0.5590 0.0112  -0.0504 0.1141  57  PHE A CA  
455  C C   . PHE A 60  ? 0.1955 0.2799 0.5118 0.0333  -0.0196 0.0576  57  PHE A C   
456  O O   . PHE A 60  ? 0.1924 0.2678 0.4758 0.0213  0.0020  0.0401  57  PHE A O   
457  C CB  . PHE A 60  ? 0.2097 0.2403 0.6707 -0.0098 -0.0609 0.0252  57  PHE A CB  
458  C CG  . PHE A 60  ? 0.2156 0.2994 0.7309 0.0126  -0.1158 -0.0341 57  PHE A CG  
459  C CD1 . PHE A 60  ? 0.2224 0.3078 0.7124 0.0109  -0.1334 -0.0390 57  PHE A CD1 
460  C CD2 . PHE A 60  ? 0.2223 0.3279 0.7509 0.0029  -0.1209 -0.0331 57  PHE A CD2 
461  C CE1 . PHE A 60  ? 0.2290 0.3179 0.7485 0.0032  -0.1323 -0.0416 57  PHE A CE1 
462  C CE2 . PHE A 60  ? 0.2325 0.3615 0.7997 -0.0173 -0.1136 -0.0364 57  PHE A CE2 
463  C CZ  . PHE A 60  ? 0.2308 0.3597 0.7812 -0.0073 -0.1226 -0.0357 57  PHE A CZ  
464  N N   . LYS A 61  ? 0.1986 0.2636 0.4852 0.0476  -0.0073 0.0947  58  LYS A N   
465  C CA  . LYS A 61  ? 0.2191 0.2861 0.5134 0.0326  -0.0119 -0.0387 58  LYS A CA  
466  C C   . LYS A 61  ? 0.2027 0.2743 0.3915 0.0012  -0.0392 0.0055  58  LYS A C   
467  O O   . LYS A 61  ? 0.2038 0.2942 0.3345 -0.0149 -0.0118 -0.0516 58  LYS A O   
468  C CB  . LYS A 61  ? 0.2582 0.3751 0.6129 0.0350  0.0084  -0.0089 58  LYS A CB  
469  C CG  . LYS A 61  ? 0.2831 0.3567 0.5975 0.0474  0.0330  0.0420  58  LYS A CG  
470  C CD  . LYS A 61  ? 0.2980 0.4024 0.5872 0.0603  0.0314  0.0879  58  LYS A CD  
471  C CE  . LYS A 61  ? 0.3058 0.4309 0.6231 0.0577  0.0486  0.0852  58  LYS A CE  
472  N NZ  . LYS A 61  ? 0.3067 0.4508 0.6663 0.0432  0.0656  0.0803  58  LYS A NZ  
473  N N   . ASN A 62  ? 0.1839 0.1834 0.3724 -0.0428 -0.0734 0.0682  59  ASN A N   
474  C CA  . ASN A 62  ? 0.1901 0.2015 0.3120 -0.0108 -0.0512 0.1148  59  ASN A CA  
475  C C   . ASN A 62  ? 0.1933 0.1719 0.3559 -0.0095 -0.0474 0.1002  59  ASN A C   
476  O O   . ASN A 62  ? 0.2029 0.1821 0.4000 -0.0290 -0.0824 0.0958  59  ASN A O   
477  C CB  . ASN A 62  ? 0.1883 0.2149 0.2689 -0.0032 0.0146  0.0885  59  ASN A CB  
478  C CG  . ASN A 62  ? 0.1997 0.2062 0.2637 0.0153  0.0745  0.1075  59  ASN A CG  
479  O OD1 . ASN A 62  ? 0.1872 0.2059 0.2197 0.0051  0.0500  0.0667  59  ASN A OD1 
480  N ND2 . ASN A 62  ? 0.2233 0.2810 0.3412 0.0313  0.0738  0.1340  59  ASN A ND2 
481  N N   . THR A 63  ? 0.1750 0.1052 0.2683 0.0204  -0.0054 0.0704  60  THR A N   
482  C CA  . THR A 63  ? 0.1682 0.1244 0.2345 0.0279  -0.0043 0.0189  60  THR A CA  
483  C C   . THR A 63  ? 0.1677 0.1463 0.2340 0.0330  -0.0126 0.0826  60  THR A C   
484  O O   . THR A 63  ? 0.1652 0.1348 0.2456 0.0270  0.0026  0.0890  60  THR A O   
485  C CB  . THR A 63  ? 0.1663 0.2352 0.2803 0.0358  0.0163  0.0149  60  THR A CB  
486  O OG1 . THR A 63  ? 0.1668 0.2538 0.2468 -0.0204 -0.0121 0.0340  60  THR A OG1 
487  C CG2 . THR A 63  ? 0.1729 0.2932 0.3382 0.0661  0.0018  -0.0141 60  THR A CG2 
488  N N   . GLU A 64  ? 0.1731 0.1010 0.2760 0.0243  -0.0410 0.0327  61  GLU A N   
489  C CA  . GLU A 64  ? 0.1769 0.1188 0.1699 -0.0101 -0.0442 0.0149  61  GLU A CA  
490  C C   . GLU A 64  ? 0.1760 0.1225 0.1854 -0.0174 -0.0238 -0.0090 61  GLU A C   
491  O O   . GLU A 64  ? 0.2015 0.1110 0.2928 -0.0025 -0.0386 0.0148  61  GLU A O   
492  C CB  . GLU A 64  ? 0.1871 0.1887 0.1422 0.0331  -0.0237 -0.0545 61  GLU A CB  
493  C CG  . GLU A 64  ? 0.2125 0.3321 0.3045 0.0716  -0.0023 -0.0683 61  GLU A CG  
494  C CD  . GLU A 64  ? 0.2421 0.4883 0.4483 0.0812  0.0038  -0.0688 61  GLU A CD  
495  O OE1 . GLU A 64  ? 0.2750 0.5600 0.5730 0.0650  0.0271  -0.0831 61  GLU A OE1 
496  O OE2 . GLU A 64  ? 0.2538 0.5508 0.5103 0.0714  -0.0173 -0.0172 61  GLU A OE2 
497  N N   . ILE A 65  ? 0.1541 0.1047 0.1643 -0.0262 -0.0041 -0.0195 62  ILE A N   
498  C CA  . ILE A 65  ? 0.1349 0.0691 0.1321 -0.0011 0.0102  0.0408  62  ILE A CA  
499  C C   . ILE A 65  ? 0.1129 0.0627 0.1487 0.0319  0.0382  0.0232  62  ILE A C   
500  O O   . ILE A 65  ? 0.1122 0.1031 0.2707 0.0315  0.0417  0.0488  62  ILE A O   
501  C CB  . ILE A 65  ? 0.1362 0.0897 0.1177 0.0317  0.0306  0.0206  62  ILE A CB  
502  C CG1 . ILE A 65  ? 0.1261 0.1982 0.0819 0.0065  0.0305  -0.0036 62  ILE A CG1 
503  C CG2 . ILE A 65  ? 0.1510 0.1510 0.2801 0.0706  0.0302  0.0159  62  ILE A CG2 
504  C CD1 . ILE A 65  ? 0.1445 0.2264 0.2143 -0.0133 0.0320  0.0162  62  ILE A CD1 
505  N N   . SER A 66  ? 0.1245 0.0872 0.1745 0.0024  0.0175  0.0185  63  SER A N   
506  C CA  . SER A 66  ? 0.1394 0.1171 0.1103 0.0161  -0.0050 -0.0301 63  SER A CA  
507  C C   . SER A 66  ? 0.1445 0.0999 0.1332 0.0069  -0.0204 0.0003  63  SER A C   
508  O O   . SER A 66  ? 0.1761 0.0715 0.2595 0.0104  -0.0361 0.0115  63  SER A O   
509  C CB  . SER A 66  ? 0.1443 0.1374 0.1162 -0.0027 -0.0197 -0.0294 63  SER A CB  
510  O OG  . SER A 66  ? 0.1715 0.1544 0.1748 0.0093  -0.0007 -0.0389 63  SER A OG  
511  N N   . PHE A 67  ? 0.1154 0.0907 0.1353 0.0002  0.0024  -0.0007 64  PHE A N   
512  C CA  . PHE A 67  ? 0.1032 0.1046 0.1010 0.0082  -0.0026 -0.0209 64  PHE A CA  
513  C C   . PHE A 67  ? 0.0999 0.0745 0.1606 -0.0005 -0.0022 -0.0303 64  PHE A C   
514  O O   . PHE A 67  ? 0.1124 0.1081 0.1928 0.0116  0.0385  -0.0209 64  PHE A O   
515  C CB  . PHE A 67  ? 0.1081 0.1581 0.1084 -0.0225 0.0410  -0.0409 64  PHE A CB  
516  C CG  . PHE A 67  ? 0.1107 0.1449 0.1560 -0.0203 0.0426  -0.0016 64  PHE A CG  
517  C CD1 . PHE A 67  ? 0.1262 0.1102 0.1694 -0.0509 0.0537  -0.0440 64  PHE A CD1 
518  C CD2 . PHE A 67  ? 0.1053 0.1237 0.1812 -0.0402 0.0416  -0.0347 64  PHE A CD2 
519  C CE1 . PHE A 67  ? 0.1305 0.1212 0.2072 -0.0499 0.0626  -0.0723 64  PHE A CE1 
520  C CE2 . PHE A 67  ? 0.1181 0.0824 0.2072 -0.0099 0.0751  0.0074  64  PHE A CE2 
521  C CZ  . PHE A 67  ? 0.1247 0.1268 0.1862 -0.0444 0.0600  -0.0423 64  PHE A CZ  
522  N N   . ILE A 68  ? 0.0878 0.0994 0.1230 -0.0200 0.0056  -0.0256 65  ILE A N   
523  C CA  . ILE A 68  ? 0.0770 0.1483 0.1206 -0.0284 -0.0062 -0.0075 65  ILE A CA  
524  C C   . ILE A 68  ? 0.0891 0.1220 0.0629 -0.0118 -0.0047 0.0156  65  ILE A C   
525  O O   . ILE A 68  ? 0.1197 0.1019 0.1537 0.0103  0.0053  -0.0308 65  ILE A O   
526  C CB  . ILE A 68  ? 0.0884 0.2260 0.1139 -0.0275 0.0258  0.0048  65  ILE A CB  
527  C CG1 . ILE A 68  ? 0.0974 0.2132 0.1226 0.0111  0.0493  0.0322  65  ILE A CG1 
528  C CG2 . ILE A 68  ? 0.0916 0.2021 0.1856 -0.0442 0.0349  0.0254  65  ILE A CG2 
529  C CD1 . ILE A 68  ? 0.1002 0.3077 0.1736 -0.0112 0.0451  -0.0015 65  ILE A CD1 
530  N N   . LEU A 69  ? 0.1177 0.1443 0.0902 -0.0251 0.0148  0.0506  66  LEU A N   
531  C CA  . LEU A 69  ? 0.1144 0.0924 0.1065 -0.0214 0.0081  0.0326  66  LEU A CA  
532  C C   . LEU A 69  ? 0.1184 0.0947 0.1406 -0.0088 -0.0108 0.0041  66  LEU A C   
533  O O   . LEU A 69  ? 0.1119 0.1610 0.1639 -0.0413 0.0348  -0.0354 66  LEU A O   
534  C CB  . LEU A 69  ? 0.1242 0.1079 0.1411 -0.0129 -0.0169 0.0078  66  LEU A CB  
535  C CG  . LEU A 69  ? 0.1154 0.0868 0.1991 -0.0164 -0.0029 0.0089  66  LEU A CG  
536  C CD1 . LEU A 69  ? 0.1203 0.1288 0.2475 0.0189  -0.0216 0.0625  66  LEU A CD1 
537  C CD2 . LEU A 69  ? 0.1166 0.1280 0.2305 -0.0091 0.0462  -0.0056 66  LEU A CD2 
538  N N   . GLY A 70  ? 0.1468 0.0764 0.1352 -0.0039 -0.0042 -0.0268 67  GLY A N   
539  C CA  . GLY A 70  ? 0.1481 0.0972 0.0963 -0.0101 0.0106  -0.0007 67  GLY A CA  
540  C C   . GLY A 70  ? 0.1331 0.1060 0.1271 -0.0113 0.0064  0.0667  67  GLY A C   
541  O O   . GLY A 70  ? 0.1344 0.1015 0.1925 -0.0122 0.0251  -0.0143 67  GLY A O   
542  N N   . GLN A 71  ? 0.1207 0.0791 0.1581 0.0204  0.0153  0.0482  68  GLN A N   
543  C CA  . GLN A 71  ? 0.1006 0.1036 0.1396 0.0088  0.0133  -0.0011 68  GLN A CA  
544  C C   . GLN A 71  ? 0.1030 0.0799 0.1472 -0.0048 -0.0171 -0.0013 68  GLN A C   
545  O O   . GLN A 71  ? 0.1140 0.0888 0.1611 -0.0255 0.0057  -0.0273 68  GLN A O   
546  C CB  . GLN A 71  ? 0.1255 0.1307 0.1282 0.0321  -0.0007 0.0226  68  GLN A CB  
547  C CG  . GLN A 71  ? 0.1533 0.1430 0.1262 0.0152  0.0348  0.0000  68  GLN A CG  
548  C CD  . GLN A 71  ? 0.1647 0.1760 0.1664 0.0193  0.0414  0.0462  68  GLN A CD  
549  O OE1 . GLN A 71  ? 0.1836 0.2250 0.1950 0.0194  0.0283  -0.0175 68  GLN A OE1 
550  N NE2 . GLN A 71  ? 0.1517 0.1612 0.1957 0.0135  0.0739  0.0549  68  GLN A NE2 
551  N N   . GLU A 72  ? 0.0877 0.0748 0.1797 0.0173  -0.0104 -0.0125 69  GLU A N   
552  C CA  . GLU A 72  ? 0.1059 0.0805 0.1083 0.0117  0.0136  -0.0257 69  GLU A CA  
553  C C   . GLU A 72  ? 0.1117 0.0769 0.1075 -0.0099 -0.0042 0.0155  69  GLU A C   
554  O O   . GLU A 72  ? 0.1070 0.1185 0.1486 -0.0147 0.0167  -0.0087 69  GLU A O   
555  C CB  . GLU A 72  ? 0.1256 0.0844 0.1831 0.0327  0.0159  -0.0429 69  GLU A CB  
556  C CG  . GLU A 72  ? 0.1282 0.0766 0.1241 0.0039  0.0091  -0.0374 69  GLU A CG  
557  C CD  . GLU A 72  ? 0.1492 0.0894 0.0651 0.0043  0.0202  0.0069  69  GLU A CD  
558  O OE1 . GLU A 72  ? 0.1247 0.0965 0.1424 -0.0007 0.0441  0.0187  69  GLU A OE1 
559  O OE2 . GLU A 72  ? 0.2108 0.0943 0.1327 -0.0046 0.0211  -0.0016 69  GLU A OE2 
560  N N   . PHE A 73  ? 0.1078 0.1037 0.1323 -0.0082 -0.0151 0.0063  70  PHE A N   
561  C CA  . PHE A 73  ? 0.1142 0.0688 0.1316 -0.0050 -0.0077 -0.0430 70  PHE A CA  
562  C C   . PHE A 73  ? 0.1148 0.0685 0.1377 0.0046  -0.0106 0.0181  70  PHE A C   
563  O O   . PHE A 73  ? 0.1235 0.1200 0.1896 -0.0075 0.0173  -0.0145 70  PHE A O   
564  C CB  . PHE A 73  ? 0.1302 0.0630 0.1444 -0.0226 0.0425  -0.0254 70  PHE A CB  
565  C CG  . PHE A 73  ? 0.1237 0.0651 0.1495 -0.0164 0.0093  -0.0122 70  PHE A CG  
566  C CD1 . PHE A 73  ? 0.1347 0.0708 0.1469 0.0134  0.0506  0.0043  70  PHE A CD1 
567  C CD2 . PHE A 73  ? 0.1271 0.0617 0.2152 -0.0164 0.0146  -0.0200 70  PHE A CD2 
568  C CE1 . PHE A 73  ? 0.1281 0.0961 0.1822 0.0005  0.0275  -0.0191 70  PHE A CE1 
569  C CE2 . PHE A 73  ? 0.1355 0.0805 0.2026 0.0181  -0.0256 0.0008  70  PHE A CE2 
570  C CZ  . PHE A 73  ? 0.1397 0.1241 0.1938 -0.0256 0.0081  -0.0273 70  PHE A CZ  
571  N N   . ASP A 74  ? 0.1181 0.0941 0.1216 -0.0175 -0.0171 0.0198  71  ASP A N   
572  C CA  . ASP A 74  ? 0.1255 0.0957 0.1560 -0.0350 -0.0096 0.0216  71  ASP A CA  
573  C C   . ASP A 74  ? 0.1239 0.0802 0.1987 -0.0123 0.0110  0.0117  71  ASP A C   
574  O O   . ASP A 74  ? 0.1382 0.1241 0.2559 -0.0401 0.0002  -0.0115 71  ASP A O   
575  C CB  . ASP A 74  ? 0.1378 0.0600 0.1347 -0.0122 0.0111  -0.0046 71  ASP A CB  
576  C CG  . ASP A 74  ? 0.1493 0.0694 0.1589 -0.0051 0.0273  0.0107  71  ASP A CG  
577  O OD1 . ASP A 74  ? 0.1768 0.1136 0.2183 -0.0214 0.0437  -0.0419 71  ASP A OD1 
578  O OD2 . ASP A 74  ? 0.1550 0.1300 0.2088 -0.0143 0.0492  0.0133  71  ASP A OD2 
579  N N   . GLU A 75  ? 0.1264 0.0908 0.1668 -0.0480 0.0148  0.0193  72  GLU A N   
580  C CA  . GLU A 75  ? 0.1291 0.1574 0.1004 -0.0426 -0.0463 0.0234  72  GLU A CA  
581  C C   . GLU A 75  ? 0.1310 0.2188 0.1009 -0.0216 -0.0070 -0.0125 72  GLU A C   
582  O O   . GLU A 75  ? 0.1257 0.1807 0.1541 -0.0277 -0.0027 0.0248  72  GLU A O   
583  C CB  . GLU A 75  ? 0.1410 0.1074 0.1223 -0.0454 -0.0029 0.0281  72  GLU A CB  
584  C CG  . GLU A 75  ? 0.1315 0.0874 0.1673 -0.0357 -0.0235 0.0299  72  GLU A CG  
585  C CD  . GLU A 75  ? 0.1356 0.0945 0.2004 -0.0209 0.0003  -0.0177 72  GLU A CD  
586  O OE1 . GLU A 75  ? 0.1263 0.0991 0.2011 -0.0030 0.0173  0.0209  72  GLU A OE1 
587  O OE2 . GLU A 75  ? 0.1526 0.1231 0.2385 -0.0311 0.0190  -0.0121 72  GLU A OE2 
588  N N   . VAL A 76  ? 0.1232 0.2473 0.1069 -0.0682 -0.0006 0.0262  73  VAL A N   
589  C CA  . VAL A 76  ? 0.1295 0.2502 0.0925 -0.0778 -0.0081 -0.0004 73  VAL A CA  
590  C C   . VAL A 76  ? 0.1393 0.2070 0.1855 -0.0846 0.0074  -0.0089 73  VAL A C   
591  O O   . VAL A 76  ? 0.1494 0.2463 0.2305 -0.0891 0.0218  -0.0594 73  VAL A O   
592  C CB  . VAL A 76  ? 0.1507 0.2883 0.1550 -0.0636 -0.0359 0.0282  73  VAL A CB  
593  C CG1 . VAL A 76  ? 0.1671 0.3336 0.1894 -0.0299 -0.0232 0.0417  73  VAL A CG1 
594  C CG2 . VAL A 76  ? 0.1647 0.2356 0.1834 -0.0549 -0.0314 0.0503  73  VAL A CG2 
595  N N   . THR A 77  ? 0.1321 0.1833 0.1566 -0.0283 0.0054  -0.0202 74  THR A N   
596  C CA  . THR A 77  ? 0.1420 0.1775 0.1793 -0.0442 0.0128  -0.0075 74  THR A CA  
597  C C   . THR A 77  ? 0.1522 0.1705 0.2082 -0.0795 0.0024  -0.0115 74  THR A C   
598  O O   . THR A 77  ? 0.1495 0.2423 0.1812 -0.0564 -0.0337 -0.0121 74  THR A O   
599  C CB  . THR A 77  ? 0.1472 0.1822 0.1331 -0.0035 -0.0048 -0.0322 74  THR A CB  
600  O OG1 . THR A 77  ? 0.1438 0.1454 0.2076 0.0231  0.0096  -0.0073 74  THR A OG1 
601  C CG2 . THR A 77  ? 0.1504 0.1622 0.1714 -0.0221 -0.0299 -0.0058 74  THR A CG2 
602  N N   . ALA A 78  ? 0.1652 0.1895 0.2131 -0.0923 0.0147  -0.0609 75  ALA A N   
603  C CA  . ALA A 78  ? 0.1693 0.2344 0.2869 -0.0960 0.0291  -0.0644 75  ALA A CA  
604  C C   . ALA A 78  ? 0.1655 0.2666 0.2719 -0.1071 0.0044  -0.0494 75  ALA A C   
605  O O   . ALA A 78  ? 0.1987 0.3349 0.2095 -0.0814 0.0121  -0.0879 75  ALA A O   
606  C CB  . ALA A 78  ? 0.1750 0.2355 0.3657 -0.0510 0.0370  -0.0899 75  ALA A CB  
607  N N   . ASP A 79  ? 0.1527 0.2518 0.2940 -0.0668 0.0265  -0.0248 76  ASP A N   
608  C CA  . ASP A 79  ? 0.1507 0.2135 0.2283 -0.0268 0.0032  0.0159  76  ASP A CA  
609  C C   . ASP A 79  ? 0.1693 0.2091 0.2958 -0.0279 -0.0281 -0.0020 76  ASP A C   
610  O O   . ASP A 79  ? 0.1689 0.2267 0.3215 0.0073  -0.0557 -0.0063 76  ASP A O   
611  C CB  . ASP A 79  ? 0.1499 0.2274 0.2308 -0.0489 -0.0092 -0.0599 76  ASP A CB  
612  C CG  . ASP A 79  ? 0.1450 0.1916 0.1655 -0.0538 0.0097  -0.0422 76  ASP A CG  
613  O OD1 . ASP A 79  ? 0.1288 0.2037 0.2762 -0.0117 0.0086  -0.0427 76  ASP A OD1 
614  O OD2 . ASP A 79  ? 0.1572 0.2015 0.2630 -0.0490 0.0356  -0.0491 76  ASP A OD2 
615  N N   A ASP A 80  ? 0.1792 0.2127 0.2407 -0.0395 -0.0507 -0.0099 77  ASP A N   
616  N N   B ASP A 80  ? 0.1810 0.2099 0.2261 -0.0409 -0.0513 0.0076  77  ASP A N   
617  C CA  A ASP A 80  ? 0.1925 0.2318 0.2523 -0.0158 -0.0485 0.0325  77  ASP A CA  
618  C CA  B ASP A 80  ? 0.1969 0.2263 0.2284 -0.0148 -0.0480 0.0693  77  ASP A CA  
619  C C   A ASP A 80  ? 0.1973 0.1763 0.2429 -0.0092 -0.0587 0.0528  77  ASP A C   
620  C C   B ASP A 80  ? 0.1998 0.1705 0.2348 -0.0082 -0.0596 0.0715  77  ASP A C   
621  O O   A ASP A 80  ? 0.2261 0.1813 0.3110 0.0120  -0.0791 0.0437  77  ASP A O   
622  O O   B ASP A 80  ? 0.2303 0.1715 0.3112 0.0122  -0.0803 0.0641  77  ASP A O   
623  C CB  A ASP A 80  ? 0.2012 0.3039 0.2952 -0.0252 -0.0496 0.0169  77  ASP A CB  
624  C CB  B ASP A 80  ? 0.2106 0.2956 0.2557 -0.0223 -0.0480 0.0722  77  ASP A CB  
625  C CG  A ASP A 80  ? 0.2118 0.4147 0.2936 -0.0190 -0.0503 -0.0157 77  ASP A CG  
626  C CG  B ASP A 80  ? 0.2275 0.4095 0.2502 -0.0137 -0.0571 0.0388  77  ASP A CG  
627  O OD1 A ASP A 80  ? 0.2179 0.4587 0.2681 -0.0230 -0.0365 -0.0216 77  ASP A OD1 
628  O OD1 B ASP A 80  ? 0.2408 0.4356 0.2687 -0.0016 -0.0608 0.0540  77  ASP A OD1 
629  O OD2 A ASP A 80  ? 0.2168 0.4536 0.3570 -0.0153 -0.0438 -0.0496 77  ASP A OD2 
630  O OD2 B ASP A 80  ? 0.2352 0.4598 0.2755 -0.0243 -0.0489 -0.0009 77  ASP A OD2 
631  N N   . ARG A 81  ? 0.1744 0.1488 0.1813 -0.0243 -0.0486 0.0034  78  ARG A N   
632  C CA  . ARG A 81  ? 0.1579 0.1356 0.1408 -0.0198 0.0099  0.0196  78  ARG A CA  
633  C C   . ARG A 81  ? 0.1427 0.1483 0.1982 -0.0053 -0.0016 0.0061  78  ARG A C   
634  O O   . ARG A 81  ? 0.1389 0.1620 0.2294 -0.0211 0.0106  -0.0067 78  ARG A O   
635  C CB  . ARG A 81  ? 0.1509 0.1691 0.1853 0.0107  0.0306  0.0491  78  ARG A CB  
636  C CG  . ARG A 81  ? 0.1425 0.1453 0.2523 0.0074  0.0266  0.0798  78  ARG A CG  
637  C CD  . ARG A 81  ? 0.1571 0.1385 0.1941 0.0166  0.0027  0.0485  78  ARG A CD  
638  N NE  . ARG A 81  ? 0.1696 0.1206 0.1879 0.0141  0.0095  0.0232  78  ARG A NE  
639  C CZ  . ARG A 81  ? 0.1625 0.1019 0.1631 -0.0381 0.0005  -0.0136 78  ARG A CZ  
640  N NH1 . ARG A 81  ? 0.1468 0.1234 0.1926 -0.0259 0.0001  -0.0053 78  ARG A NH1 
641  N NH2 . ARG A 81  ? 0.1770 0.0856 0.1943 -0.0311 -0.0069 0.0274  78  ARG A NH2 
642  N N   . LYS A 82  ? 0.1484 0.1257 0.2428 -0.0292 -0.0277 0.0271  79  LYS A N   
643  C CA  . LYS A 82  ? 0.1611 0.1329 0.2167 -0.0130 -0.0352 0.0598  79  LYS A CA  
644  C C   . LYS A 82  ? 0.1530 0.1456 0.1900 -0.0049 -0.0511 0.0296  79  LYS A C   
645  O O   . LYS A 82  ? 0.1697 0.1676 0.2336 0.0030  -0.0472 0.0296  79  LYS A O   
646  C CB  . LYS A 82  ? 0.1980 0.1864 0.2244 -0.0368 -0.0602 0.1017  79  LYS A CB  
647  C CG  . LYS A 82  ? 0.2401 0.3076 0.2384 -0.0338 -0.0924 0.1304  79  LYS A CG  
648  C CD  . LYS A 82  ? 0.2830 0.4289 0.3271 -0.0376 -0.0833 0.1770  79  LYS A CD  
649  C CE  . LYS A 82  ? 0.3055 0.5647 0.4387 -0.0402 -0.1103 0.1314  79  LYS A CE  
650  N NZ  . LYS A 82  ? 0.3270 0.6534 0.5291 -0.0320 -0.1103 0.1202  79  LYS A NZ  
651  N N   . VAL A 83  ? 0.1324 0.1430 0.1591 -0.0131 -0.0214 0.0467  80  VAL A N   
652  C CA  . VAL A 83  ? 0.1107 0.1280 0.1410 -0.0116 0.0146  0.0163  80  VAL A CA  
653  C C   . VAL A 83  ? 0.1093 0.0674 0.1592 0.0236  0.0222  -0.0153 80  VAL A C   
654  O O   . VAL A 83  ? 0.1246 0.1319 0.1614 0.0026  -0.0071 -0.0026 80  VAL A O   
655  C CB  . VAL A 83  ? 0.1073 0.0820 0.1805 -0.0059 0.0565  -0.0037 80  VAL A CB  
656  C CG1 . VAL A 83  ? 0.1058 0.1373 0.1915 -0.0282 0.0339  0.0359  80  VAL A CG1 
657  C CG2 . VAL A 83  ? 0.1146 0.0974 0.1622 -0.0069 0.0230  0.0312  80  VAL A CG2 
658  N N   . LYS A 84  ? 0.1056 0.0655 0.2041 0.0047  -0.0119 -0.0140 81  LYS A N   
659  C CA  . LYS A 84  ? 0.1115 0.0461 0.1763 -0.0079 0.0011  0.0038  81  LYS A CA  
660  C C   . LYS A 84  ? 0.1268 0.0658 0.0852 -0.0024 0.0074  0.0187  81  LYS A C   
661  O O   . LYS A 84  ? 0.1365 0.0892 0.1298 0.0087  0.0158  0.0113  81  LYS A O   
662  C CB  . LYS A 84  ? 0.1202 0.0500 0.1795 0.0083  0.0292  -0.0020 81  LYS A CB  
663  C CG  . LYS A 84  ? 0.1301 0.0709 0.1483 0.0230  0.0189  0.0466  81  LYS A CG  
664  C CD  . LYS A 84  ? 0.1450 0.0610 0.1544 0.0001  0.0370  0.0324  81  LYS A CD  
665  C CE  . LYS A 84  ? 0.1435 0.0729 0.1437 0.0128  0.0732  0.0298  81  LYS A CE  
666  N NZ  . LYS A 84  ? 0.1466 0.0728 0.1597 0.0100  0.0456  0.0070  81  LYS A NZ  
667  N N   . SER A 85  ? 0.1328 0.0590 0.1733 0.0049  0.0206  0.0091  82  SER A N   
668  C CA  . SER A 85  ? 0.1206 0.0739 0.1256 -0.0060 0.0024  0.0072  82  SER A CA  
669  C C   . SER A 85  ? 0.1185 0.0826 0.1588 -0.0040 -0.0036 0.0328  82  SER A C   
670  O O   . SER A 85  ? 0.1418 0.0841 0.1574 -0.0050 0.0123  0.0009  82  SER A O   
671  C CB  . SER A 85  ? 0.1044 0.0705 0.1678 -0.0300 0.0057  -0.0350 82  SER A CB  
672  O OG  . SER A 85  ? 0.0875 0.1300 0.1649 0.0109  0.0217  0.0135  82  SER A OG  
673  N N   . THR A 86  ? 0.1052 0.0482 0.1312 -0.0117 0.0140  -0.0158 83  THR A N   
674  C CA  . THR A 86  ? 0.1042 0.0792 0.1361 -0.0043 -0.0244 -0.0058 83  THR A CA  
675  C C   . THR A 86  ? 0.0913 0.0594 0.1790 0.0136  0.0149  0.0314  83  THR A C   
676  O O   . THR A 86  ? 0.1026 0.1226 0.1567 -0.0032 0.0376  0.0277  83  THR A O   
677  C CB  . THR A 86  ? 0.1320 0.1229 0.1675 -0.0247 -0.0455 -0.0007 83  THR A CB  
678  O OG1 . THR A 86  ? 0.1747 0.1157 0.2483 -0.0465 -0.0336 0.0208  83  THR A OG1 
679  C CG2 . THR A 86  ? 0.1214 0.1990 0.2068 -0.0620 -0.0318 -0.0531 83  THR A CG2 
680  N N   . ILE A 87  ? 0.0957 0.0929 0.1438 0.0326  -0.0046 0.0041  84  ILE A N   
681  C CA  . ILE A 87  ? 0.0979 0.0691 0.1040 -0.0093 -0.0534 0.0267  84  ILE A CA  
682  C C   . ILE A 87  ? 0.1014 0.1000 0.1051 -0.0077 -0.0272 0.0096  84  ILE A C   
683  O O   . ILE A 87  ? 0.1105 0.1028 0.1407 0.0140  0.0089  0.0175  84  ILE A O   
684  C CB  . ILE A 87  ? 0.1107 0.0875 0.1538 0.0098  -0.0304 -0.0292 84  ILE A CB  
685  C CG1 . ILE A 87  ? 0.1144 0.1273 0.1695 -0.0064 -0.0256 -0.0596 84  ILE A CG1 
686  C CG2 . ILE A 87  ? 0.1113 0.0986 0.2023 0.0144  -0.0083 -0.0013 84  ILE A CG2 
687  C CD1 . ILE A 87  ? 0.1319 0.1953 0.1475 -0.0125 -0.0425 -0.0286 84  ILE A CD1 
688  N N   . THR A 88  ? 0.1060 0.1047 0.1025 -0.0270 -0.0377 0.0017  85  THR A N   
689  C CA  . THR A 88  ? 0.1187 0.0534 0.1584 -0.0261 -0.0152 -0.0125 85  THR A CA  
690  C C   . THR A 88  ? 0.1193 0.1004 0.1892 0.0146  -0.0152 -0.0040 85  THR A C   
691  O O   . THR A 88  ? 0.1316 0.0876 0.1944 -0.0083 -0.0073 0.0241  85  THR A O   
692  C CB  . THR A 88  ? 0.1316 0.0700 0.1719 -0.0059 0.0096  0.0216  85  THR A CB  
693  O OG1 . THR A 88  ? 0.1313 0.1134 0.1871 -0.0087 0.0125  -0.0089 85  THR A OG1 
694  C CG2 . THR A 88  ? 0.1427 0.0766 0.2086 -0.0111 -0.0192 0.0379  85  THR A CG2 
695  N N   A LEU A 89  ? 0.1142 0.0921 0.1272 0.0056  -0.0052 0.0179  86  LEU A N   
696  N N   B LEU A 89  ? 0.1151 0.0958 0.1206 0.0191  -0.0012 0.0328  86  LEU A N   
697  C CA  A LEU A 89  ? 0.1183 0.1170 0.1304 0.0079  -0.0216 0.0075  86  LEU A CA  
698  C CA  B LEU A 89  ? 0.1221 0.1198 0.1234 0.0340  -0.0076 0.0330  86  LEU A CA  
699  C C   A LEU A 89  ? 0.1071 0.1282 0.1303 -0.0155 -0.0067 -0.0120 86  LEU A C   
700  C C   B LEU A 89  ? 0.1111 0.1337 0.1442 0.0049  0.0040  0.0076  86  LEU A C   
701  O O   A LEU A 89  ? 0.0973 0.1068 0.1603 -0.0341 -0.0254 0.0220  86  LEU A O   
702  O O   B LEU A 89  ? 0.1022 0.1237 0.1831 -0.0007 -0.0093 0.0341  86  LEU A O   
703  C CB  A LEU A 89  ? 0.1305 0.0984 0.1893 -0.0056 -0.0265 -0.0119 86  LEU A CB  
704  C CB  B LEU A 89  ? 0.1379 0.0953 0.1482 0.0450  0.0106  0.0482  86  LEU A CB  
705  C CG  A LEU A 89  ? 0.1315 0.1401 0.2191 -0.0146 -0.0492 -0.0105 86  LEU A CG  
706  C CG  B LEU A 89  ? 0.1405 0.1158 0.1511 0.0704  0.0068  0.0289  86  LEU A CG  
707  C CD1 A LEU A 89  ? 0.1360 0.1492 0.2242 -0.0114 -0.0155 0.0426  86  LEU A CD1 
708  C CD1 B LEU A 89  ? 0.1479 0.1417 0.2141 0.0645  0.0194  0.0670  86  LEU A CD1 
709  C CD2 A LEU A 89  ? 0.1271 0.1212 0.2022 -0.0365 -0.0630 -0.0233 86  LEU A CD2 
710  C CD2 B LEU A 89  ? 0.1400 0.1394 0.1727 0.0663  0.0100  -0.0496 86  LEU A CD2 
711  N N   . ASP A 90  ? 0.1237 0.1024 0.1227 0.0062  0.0070  0.0018  87  ASP A N   
712  C CA  . ASP A 90  ? 0.1303 0.0966 0.1315 0.0175  0.0143  -0.0050 87  ASP A CA  
713  C C   . ASP A 90  ? 0.1296 0.1360 0.1381 0.0045  -0.0007 0.0214  87  ASP A C   
714  O O   . ASP A 90  ? 0.1150 0.1147 0.1971 -0.0104 0.0054  0.0325  87  ASP A O   
715  C CB  . ASP A 90  ? 0.1582 0.0894 0.1488 0.0099  0.0039  0.0052  87  ASP A CB  
716  C CG  . ASP A 90  ? 0.1735 0.1052 0.2563 -0.0117 0.0117  -0.0202 87  ASP A CG  
717  O OD1 . ASP A 90  ? 0.1840 0.1100 0.2106 -0.0198 0.0249  -0.0268 87  ASP A OD1 
718  O OD2 . ASP A 90  ? 0.1801 0.2117 0.2581 -0.0210 0.0588  0.0390  87  ASP A OD2 
719  N N   . GLY A 91  ? 0.1275 0.1420 0.1411 0.0283  0.0118  0.0318  88  GLY A N   
720  C CA  . GLY A 91  ? 0.1402 0.1573 0.0731 0.0206  -0.0139 -0.0056 88  GLY A CA  
721  C C   . GLY A 91  ? 0.1391 0.1246 0.1389 -0.0157 -0.0180 -0.0045 88  GLY A C   
722  O O   . GLY A 91  ? 0.1257 0.1723 0.1820 -0.0366 0.0217  0.0252  88  GLY A O   
723  N N   . GLY A 92  ? 0.1498 0.1319 0.1183 -0.0255 -0.0339 0.0033  89  GLY A N   
724  C CA  . GLY A 92  ? 0.1567 0.1485 0.1514 -0.0195 -0.0734 -0.0271 89  GLY A CA  
725  C C   . GLY A 92  ? 0.1525 0.1179 0.1610 -0.0513 -0.0604 0.0075  89  GLY A C   
726  O O   . GLY A 92  ? 0.1757 0.1459 0.2216 -0.0489 -0.0526 0.0333  89  GLY A O   
727  N N   . VAL A 93  ? 0.1256 0.1208 0.2202 -0.0169 -0.0229 0.0451  90  VAL A N   
728  C CA  . VAL A 93  ? 0.1212 0.1402 0.2279 -0.0079 -0.0159 0.0131  90  VAL A CA  
729  C C   . VAL A 93  ? 0.1077 0.1580 0.1915 -0.0235 -0.0350 0.0488  90  VAL A C   
730  O O   . VAL A 93  ? 0.1092 0.1438 0.1789 -0.0322 -0.0214 0.0290  90  VAL A O   
731  C CB  . VAL A 93  ? 0.1262 0.1779 0.1638 -0.0142 -0.0318 0.0485  90  VAL A CB  
732  C CG1 . VAL A 93  ? 0.1207 0.2024 0.1886 -0.0399 -0.0466 0.0054  90  VAL A CG1 
733  C CG2 . VAL A 93  ? 0.1230 0.1816 0.1957 0.0105  -0.0245 0.0922  90  VAL A CG2 
734  N N   . LEU A 94  ? 0.1012 0.0986 0.1990 0.0029  -0.0061 0.0489  91  LEU A N   
735  C CA  . LEU A 94  ? 0.1061 0.1075 0.1372 0.0374  0.0164  0.0084  91  LEU A CA  
736  C C   . LEU A 94  ? 0.0944 0.0919 0.1444 -0.0118 0.0008  -0.0143 91  LEU A C   
737  O O   . LEU A 94  ? 0.0841 0.1037 0.2040 -0.0403 0.0030  0.0086  91  LEU A O   
738  C CB  . LEU A 94  ? 0.1137 0.1369 0.1140 0.0391  -0.0012 -0.0205 91  LEU A CB  
739  C CG  . LEU A 94  ? 0.1277 0.1089 0.1442 0.0005  0.0264  -0.0364 91  LEU A CG  
740  C CD1 . LEU A 94  ? 0.1545 0.1498 0.1584 -0.0182 0.0204  -0.0316 91  LEU A CD1 
741  C CD2 . LEU A 94  ? 0.1364 0.1206 0.1807 -0.0169 0.0476  0.0183  91  LEU A CD2 
742  N N   . VAL A 95  ? 0.1135 0.0626 0.1392 0.0101  -0.0119 -0.0139 92  VAL A N   
743  C CA  . VAL A 95  ? 0.1130 0.0863 0.1015 -0.0010 -0.0052 -0.0031 92  VAL A CA  
744  C C   . VAL A 95  ? 0.1156 0.1196 0.1266 0.0049  -0.0046 0.0295  92  VAL A C   
745  O O   . VAL A 95  ? 0.1288 0.1202 0.1111 -0.0385 0.0102  0.0109  92  VAL A O   
746  C CB  . VAL A 95  ? 0.1087 0.1579 0.0752 -0.0093 0.0218  0.0300  92  VAL A CB  
747  C CG1 . VAL A 95  ? 0.0932 0.1411 0.1370 -0.0064 0.0216  -0.0132 92  VAL A CG1 
748  C CG2 . VAL A 95  ? 0.1138 0.1827 0.1167 -0.0214 0.0122  0.0748  92  VAL A CG2 
749  N N   . HIS A 96  ? 0.1153 0.0934 0.1468 0.0373  0.0042  0.0113  93  HIS A N   
750  C CA  . HIS A 96  ? 0.1133 0.0678 0.1354 -0.0041 0.0016  0.0111  93  HIS A CA  
751  C C   . HIS A 96  ? 0.1227 0.0595 0.1400 -0.0106 0.0280  -0.0031 93  HIS A C   
752  O O   . HIS A 96  ? 0.1146 0.0881 0.1854 -0.0078 0.0149  0.0398  93  HIS A O   
753  C CB  . HIS A 96  ? 0.1157 0.0592 0.1187 -0.0005 0.0079  -0.0051 93  HIS A CB  
754  C CG  . HIS A 96  ? 0.0957 0.0946 0.1381 -0.0037 0.0518  0.0378  93  HIS A CG  
755  N ND1 . HIS A 96  ? 0.1012 0.1290 0.1485 0.0037  0.0259  0.0131  93  HIS A ND1 
756  C CD2 . HIS A 96  ? 0.1046 0.1520 0.1047 -0.0072 0.0278  0.0609  93  HIS A CD2 
757  C CE1 . HIS A 96  ? 0.0972 0.1128 0.1395 0.0128  -0.0192 0.0607  93  HIS A CE1 
758  N NE2 . HIS A 96  ? 0.0970 0.1434 0.1678 0.0091  0.0346  0.0004  93  HIS A NE2 
759  N N   A VAL A 97  ? 0.1258 0.0918 0.1140 -0.0033 0.0285  0.0004  94  VAL A N   
760  N N   B VAL A 97  ? 0.1210 0.0848 0.1291 0.0024  0.0133  -0.0112 94  VAL A N   
761  C CA  A VAL A 97  ? 0.1378 0.0780 0.1170 -0.0051 0.0027  0.0007  94  VAL A CA  
762  C CA  B VAL A 97  ? 0.1238 0.0855 0.1261 0.0085  -0.0043 -0.0261 94  VAL A CA  
763  C C   A VAL A 97  ? 0.1200 0.0995 0.1284 0.0002  0.0038  0.0156  94  VAL A C   
764  C C   B VAL A 97  ? 0.1151 0.0887 0.1372 0.0111  0.0053  0.0027  94  VAL A C   
765  O O   A VAL A 97  ? 0.1216 0.1023 0.1548 0.0017  0.0221  0.0212  94  VAL A O   
766  O O   B VAL A 97  ? 0.1165 0.0673 0.1701 0.0202  0.0259  0.0198  94  VAL A O   
767  C CB  A VAL A 97  ? 0.1513 0.0533 0.1544 -0.0139 -0.0022 0.0072  94  VAL A CB  
768  C CB  B VAL A 97  ? 0.1243 0.0914 0.1358 0.0160  -0.0225 -0.0485 94  VAL A CB  
769  C CG1 A VAL A 97  ? 0.1659 0.1239 0.1823 0.0173  -0.0014 -0.0224 94  VAL A CG1 
770  C CG1 B VAL A 97  ? 0.1224 0.1309 0.1396 0.0137  -0.0299 -0.0242 94  VAL A CG1 
771  C CG2 A VAL A 97  ? 0.1542 0.0971 0.1423 -0.0244 0.0204  0.0177  94  VAL A CG2 
772  C CG2 B VAL A 97  ? 0.1285 0.1264 0.1573 0.0293  -0.0309 -0.0795 94  VAL A CG2 
773  N N   . GLN A 98  ? 0.1103 0.0669 0.1057 0.0092  -0.0020 -0.0039 95  GLN A N   
774  C CA  . GLN A 98  ? 0.1141 0.0527 0.1506 -0.0207 0.0069  -0.0094 95  GLN A CA  
775  C C   . GLN A 98  ? 0.1221 0.0602 0.1370 -0.0222 0.0281  0.0122  95  GLN A C   
776  O O   . GLN A 98  ? 0.1353 0.0776 0.1815 -0.0120 0.0621  -0.0005 95  GLN A O   
777  C CB  . GLN A 98  ? 0.1191 0.0916 0.1652 -0.0114 -0.0200 -0.0381 95  GLN A CB  
778  C CG  . GLN A 98  ? 0.1312 0.0708 0.1718 -0.0175 -0.0157 -0.0442 95  GLN A CG  
779  C CD  . GLN A 98  ? 0.1264 0.1033 0.1692 0.0007  0.0395  -0.0190 95  GLN A CD  
780  O OE1 . GLN A 98  ? 0.1059 0.1115 0.1797 0.0057  0.0365  -0.0230 95  GLN A OE1 
781  N NE2 . GLN A 98  ? 0.1367 0.1281 0.1410 0.0155  0.0148  -0.0045 95  GLN A NE2 
782  N N   . LYS A 99  ? 0.1234 0.0641 0.1731 -0.0028 -0.0155 0.0251  96  LYS A N   
783  C CA  . LYS A 99  ? 0.1249 0.0659 0.2124 0.0098  -0.0250 0.0011  96  LYS A CA  
784  C C   . LYS A 99  ? 0.1180 0.0690 0.1671 0.0063  0.0031  0.0044  96  LYS A C   
785  O O   . LYS A 99  ? 0.1211 0.1145 0.1701 -0.0094 0.0364  0.0360  96  LYS A O   
786  C CB  . LYS A 99  ? 0.1236 0.1043 0.2105 -0.0075 -0.0249 0.0259  96  LYS A CB  
787  C CG  . LYS A 99  ? 0.1156 0.0769 0.1792 -0.0011 -0.0329 -0.0127 96  LYS A CG  
788  C CD  . LYS A 99  ? 0.0987 0.0982 0.1568 -0.0132 0.0030  0.0005  96  LYS A CD  
789  C CE  . LYS A 99  ? 0.1004 0.0571 0.1660 -0.0175 0.0215  -0.0306 96  LYS A CE  
790  N NZ  . LYS A 99  ? 0.0998 0.0743 0.2146 0.0107  0.0078  -0.0185 96  LYS A NZ  
791  N N   . TRP A 100 ? 0.1237 0.0616 0.1781 0.0329  -0.0161 0.0045  97  TRP A N   
792  C CA  . TRP A 100 ? 0.1385 0.0453 0.1590 0.0202  0.0051  0.0021  97  TRP A CA  
793  C C   . TRP A 100 ? 0.1444 0.0485 0.1748 -0.0036 0.0198  -0.0117 97  TRP A C   
794  O O   . TRP A 100 ? 0.1443 0.1010 0.1890 0.0133  0.0456  0.0134  97  TRP A O   
795  C CB  . TRP A 100 ? 0.1447 0.1132 0.1725 -0.0123 0.0271  -0.0336 97  TRP A CB  
796  C CG  . TRP A 100 ? 0.1416 0.0964 0.1897 -0.0093 0.0182  -0.0133 97  TRP A CG  
797  C CD1 . TRP A 100 ? 0.1523 0.1103 0.2624 -0.0065 0.0162  0.0195  97  TRP A CD1 
798  C CD2 . TRP A 100 ? 0.1486 0.0504 0.1709 -0.0094 -0.0190 0.0085  97  TRP A CD2 
799  N NE1 . TRP A 100 ? 0.1633 0.0872 0.2327 -0.0136 0.0301  0.0401  97  TRP A NE1 
800  C CE2 . TRP A 100 ? 0.1636 0.0713 0.2121 -0.0194 0.0076  0.0402  97  TRP A CE2 
801  C CE3 . TRP A 100 ? 0.1638 0.0559 0.1831 -0.0234 -0.0115 0.0091  97  TRP A CE3 
802  C CZ2 . TRP A 100 ? 0.1687 0.1232 0.2283 -0.0113 -0.0245 -0.0049 97  TRP A CZ2 
803  C CZ3 . TRP A 100 ? 0.1714 0.0784 0.2061 -0.0400 0.0087  -0.0204 97  TRP A CZ3 
804  C CH2 . TRP A 100 ? 0.1704 0.1255 0.1693 -0.0186 -0.0284 -0.0214 97  TRP A CH2 
805  N N   . ASP A 101 ? 0.1470 0.0567 0.1806 0.0071  0.0106  0.0014  98  ASP A N   
806  C CA  . ASP A 101 ? 0.1551 0.1068 0.2744 0.0039  0.0101  -0.0233 98  ASP A CA  
807  C C   . ASP A 101 ? 0.1610 0.0775 0.2276 0.0010  0.0138  0.0254  98  ASP A C   
808  O O   . ASP A 101 ? 0.1552 0.1355 0.2468 -0.0086 0.0433  0.0045  98  ASP A O   
809  C CB  . ASP A 101 ? 0.1557 0.1244 0.3549 0.0243  0.0061  -0.0397 98  ASP A CB  
810  C CG  . ASP A 101 ? 0.1682 0.1655 0.3855 0.0196  0.0074  -0.0432 98  ASP A CG  
811  O OD1 . ASP A 101 ? 0.1827 0.1796 0.4337 0.0381  0.0009  -0.0123 98  ASP A OD1 
812  O OD2 . ASP A 101 ? 0.1748 0.2167 0.4866 0.0281  0.0097  -0.0213 98  ASP A OD2 
813  N N   . GLY A 102 ? 0.1830 0.0666 0.1800 -0.0006 -0.0047 -0.0130 99  GLY A N   
814  C CA  . GLY A 102 ? 0.1818 0.0999 0.2060 -0.0117 -0.0007 0.0030  99  GLY A CA  
815  C C   . GLY A 102 ? 0.1664 0.1339 0.2332 -0.0012 0.0233  0.0103  99  GLY A C   
816  O O   . GLY A 102 ? 0.1627 0.1215 0.2605 0.0121  0.0343  0.0090  99  GLY A O   
817  N N   . LYS A 103 ? 0.1614 0.0765 0.2264 0.0071  0.0179  0.0311  100 LYS A N   
818  C CA  . LYS A 103 ? 0.1750 0.0703 0.2343 0.0158  0.0371  0.0264  100 LYS A CA  
819  C C   . LYS A 103 ? 0.1636 0.0532 0.1765 -0.0058 0.0366  0.0020  100 LYS A C   
820  O O   . LYS A 103 ? 0.1794 0.1003 0.1550 0.0064  0.0536  -0.0058 100 LYS A O   
821  C CB  . LYS A 103 ? 0.1854 0.0884 0.2798 0.0305  0.0516  -0.0098 100 LYS A CB  
822  C CG  . LYS A 103 ? 0.2033 0.1394 0.3743 0.0271  0.0413  0.0050  100 LYS A CG  
823  C CD  . LYS A 103 ? 0.2180 0.1835 0.4791 0.0299  0.0436  -0.0161 100 LYS A CD  
824  C CE  . LYS A 103 ? 0.2567 0.1875 0.5722 0.0204  0.0306  0.0560  100 LYS A CE  
825  N NZ  . LYS A 103 ? 0.2773 0.2979 0.6483 0.0276  0.0285  0.0357  100 LYS A NZ  
826  N N   A SER A 104 ? 0.1562 0.0445 0.1653 0.0107  0.0072  0.0039  101 SER A N   
827  N N   B SER A 104 ? 0.1548 0.0564 0.2000 0.0070  0.0191  0.0202  101 SER A N   
828  C CA  A SER A 104 ? 0.1490 0.0722 0.2084 0.0326  0.0255  -0.0191 101 SER A CA  
829  C CA  B SER A 104 ? 0.1453 0.0794 0.2150 0.0205  0.0260  -0.0067 101 SER A CA  
830  C C   A SER A 104 ? 0.1283 0.0576 0.1838 0.0234  0.0293  0.0077  101 SER A C   
831  C C   B SER A 104 ? 0.1331 0.0657 0.2083 0.0127  0.0306  0.0075  101 SER A C   
832  O O   A SER A 104 ? 0.1271 0.1315 0.2215 0.0053  0.0516  0.0138  101 SER A O   
833  O O   B SER A 104 ? 0.1333 0.1100 0.2160 -0.0033 0.0406  0.0209  101 SER A O   
834  C CB  A SER A 104 ? 0.1677 0.1268 0.2758 0.0013  -0.0041 -0.0055 101 SER A CB  
835  C CB  B SER A 104 ? 0.1483 0.1191 0.2429 0.0061  0.0123  0.0035  101 SER A CB  
836  O OG  A SER A 104 ? 0.1862 0.1381 0.2574 -0.0100 -0.0507 -0.0521 101 SER A OG  
837  O OG  B SER A 104 ? 0.1517 0.1339 0.2725 0.0080  -0.0085 -0.0345 101 SER A OG  
838  N N   . THR A 105 ? 0.1303 0.0705 0.1882 0.0039  0.0174  0.0108  102 THR A N   
839  C CA  . THR A 105 ? 0.1407 0.0559 0.2174 -0.0006 -0.0021 0.0087  102 THR A CA  
840  C C   . THR A 105 ? 0.1412 0.0972 0.1453 -0.0072 0.0299  0.0413  102 THR A C   
841  O O   . THR A 105 ? 0.1494 0.0966 0.1379 -0.0045 0.0450  0.0251  102 THR A O   
842  C CB  . THR A 105 ? 0.1468 0.0940 0.2142 -0.0353 0.0384  0.0371  102 THR A CB  
843  O OG1 . THR A 105 ? 0.1459 0.0882 0.2450 -0.0052 0.0335  0.0220  102 THR A OG1 
844  C CG2 . THR A 105 ? 0.1677 0.1240 0.1295 -0.0372 0.0173  0.0104  102 THR A CG2 
845  N N   . THR A 106 ? 0.1360 0.1114 0.1413 -0.0032 0.0257  0.0126  103 THR A N   
846  C CA  . THR A 106 ? 0.1558 0.0945 0.1809 0.0152  0.0335  -0.0003 103 THR A CA  
847  C C   . THR A 106 ? 0.1417 0.0641 0.2128 0.0145  0.0372  0.0244  103 THR A C   
848  O O   . THR A 106 ? 0.1567 0.0834 0.2739 0.0022  0.0795  0.0220  103 THR A O   
849  C CB  . THR A 106 ? 0.1807 0.1680 0.2352 0.0107  -0.0031 -0.0726 103 THR A CB  
850  O OG1 . THR A 106 ? 0.1918 0.1979 0.2696 -0.0096 -0.0146 -0.0607 103 THR A OG1 
851  C CG2 . THR A 106 ? 0.1881 0.2099 0.2686 0.0219  0.0185  -0.0182 103 THR A CG2 
852  N N   . ILE A 107 ? 0.1310 0.0618 0.2067 0.0210  0.0236  -0.0093 104 ILE A N   
853  C CA  . ILE A 107 ? 0.1192 0.0602 0.1680 0.0286  0.0281  0.0201  104 ILE A CA  
854  C C   . ILE A 107 ? 0.1049 0.0607 0.1674 0.0173  0.0275  0.0176  104 ILE A C   
855  O O   . ILE A 107 ? 0.1124 0.0851 0.1937 -0.0083 0.0469  0.0193  104 ILE A O   
856  C CB  . ILE A 107 ? 0.1142 0.0666 0.1688 0.0075  0.0204  0.0233  104 ILE A CB  
857  C CG1 . ILE A 107 ? 0.1174 0.1321 0.1491 0.0425  -0.0210 0.0384  104 ILE A CG1 
858  C CG2 . ILE A 107 ? 0.1286 0.1001 0.1963 -0.0154 0.0257  -0.0180 104 ILE A CG2 
859  C CD1 . ILE A 107 ? 0.1289 0.1801 0.2365 0.0204  -0.0331 0.0364  104 ILE A CD1 
860  N N   . LYS A 108 ? 0.1043 0.0627 0.2057 0.0190  0.0039  -0.0188 105 LYS A N   
861  C CA  . LYS A 108 ? 0.1117 0.1035 0.1917 0.0010  0.0126  -0.0748 105 LYS A CA  
862  C C   . LYS A 108 ? 0.1016 0.0724 0.1845 0.0114  0.0156  0.0011  105 LYS A C   
863  O O   . LYS A 108 ? 0.1130 0.0968 0.2463 -0.0284 0.0207  -0.0041 105 LYS A O   
864  C CB  . LYS A 108 ? 0.1352 0.1917 0.1221 -0.0105 -0.0182 -0.0465 105 LYS A CB  
865  C CG  . LYS A 108 ? 0.1580 0.2701 0.1008 -0.0317 -0.0122 -0.0619 105 LYS A CG  
866  C CD  . LYS A 108 ? 0.1872 0.3767 0.1240 -0.0569 -0.0037 -0.0665 105 LYS A CD  
867  C CE  . LYS A 108 ? 0.2184 0.4720 0.2041 -0.0701 0.0250  -0.1165 105 LYS A CE  
868  N NZ  . LYS A 108 ? 0.2440 0.5470 0.2507 -0.0811 0.0644  -0.1277 105 LYS A NZ  
869  N N   . ARG A 109 ? 0.0989 0.0505 0.1820 0.0116  0.0167  -0.0053 106 ARG A N   
870  C CA  . ARG A 109 ? 0.0904 0.0861 0.1586 0.0112  0.0125  -0.0036 106 ARG A CA  
871  C C   . ARG A 109 ? 0.0936 0.0745 0.2059 0.0018  0.0094  -0.0054 106 ARG A C   
872  O O   . ARG A 109 ? 0.0792 0.0948 0.1931 -0.0240 0.0023  0.0020  106 ARG A O   
873  C CB  . ARG A 109 ? 0.0944 0.1229 0.1475 -0.0025 0.0018  0.0052  106 ARG A CB  
874  C CG  . ARG A 109 ? 0.1104 0.0709 0.1911 -0.0064 -0.0023 -0.0089 106 ARG A CG  
875  C CD  . ARG A 109 ? 0.1185 0.1226 0.1561 0.0078  0.0126  0.0108  106 ARG A CD  
876  N NE  . ARG A 109 ? 0.1294 0.1256 0.2274 0.0044  0.0238  -0.0037 106 ARG A NE  
877  C CZ  . ARG A 109 ? 0.1260 0.1289 0.1563 -0.0125 -0.0114 -0.0365 106 ARG A CZ  
878  N NH1 . ARG A 109 ? 0.1444 0.1097 0.1680 0.0082  -0.0106 -0.0280 106 ARG A NH1 
879  N NH2 . ARG A 109 ? 0.1285 0.1778 0.1888 0.0012  -0.0069 0.0361  106 ARG A NH2 
880  N N   . LYS A 110 ? 0.1214 0.0847 0.1936 0.0498  -0.0018 -0.0036 107 LYS A N   
881  C CA  . LYS A 110 ? 0.1476 0.0877 0.2054 0.0576  -0.0062 -0.0009 107 LYS A CA  
882  C C   . LYS A 110 ? 0.1308 0.0952 0.2214 0.0337  -0.0244 0.0347  107 LYS A C   
883  O O   . LYS A 110 ? 0.1210 0.1064 0.2723 0.0111  -0.0502 0.0044  107 LYS A O   
884  C CB  . LYS A 110 ? 0.1762 0.1890 0.2617 0.0302  0.0292  -0.0539 107 LYS A CB  
885  C CG  . LYS A 110 ? 0.1985 0.2584 0.2894 0.0006  0.0522  -0.0540 107 LYS A CG  
886  C CD  . LYS A 110 ? 0.2208 0.3903 0.4098 -0.0278 0.0662  0.0016  107 LYS A CD  
887  C CE  . LYS A 110 ? 0.2432 0.4369 0.5158 -0.0561 0.0938  0.0539  107 LYS A CE  
888  N NZ  . LYS A 110 ? 0.2560 0.4183 0.5500 -0.0447 0.0806  0.0534  107 LYS A NZ  
889  N N   . ARG A 111 ? 0.1246 0.0674 0.1725 0.0247  -0.0176 0.0335  108 ARG A N   
890  C CA  . ARG A 111 ? 0.1027 0.0784 0.1117 0.0142  0.0130  0.0506  108 ARG A CA  
891  C C   . ARG A 111 ? 0.1147 0.1215 0.1437 0.0031  -0.0158 0.0114  108 ARG A C   
892  O O   . ARG A 111 ? 0.1141 0.1302 0.1922 -0.0108 0.0198  -0.0237 108 ARG A O   
893  C CB  . ARG A 111 ? 0.0872 0.1161 0.1387 0.0318  0.0178  0.0186  108 ARG A CB  
894  C CG  . ARG A 111 ? 0.1098 0.0931 0.1813 0.0063  0.0108  -0.0200 108 ARG A CG  
895  C CD  . ARG A 111 ? 0.1249 0.0722 0.1935 -0.0064 0.0003  0.0145  108 ARG A CD  
896  N NE  . ARG A 111 ? 0.1336 0.0842 0.2144 -0.0195 -0.0094 0.0132  108 ARG A NE  
897  C CZ  . ARG A 111 ? 0.1373 0.0714 0.1756 -0.0185 -0.0012 0.0138  108 ARG A CZ  
898  N NH1 . ARG A 111 ? 0.1258 0.1173 0.1707 -0.0330 0.0004  0.0433  108 ARG A NH1 
899  N NH2 . ARG A 111 ? 0.1523 0.0942 0.1450 0.0042  0.0106  -0.0066 108 ARG A NH2 
900  N N   . GLU A 112 ? 0.1197 0.1084 0.1832 0.0077  -0.0083 -0.0034 109 GLU A N   
901  C CA  . GLU A 112 ? 0.1363 0.0702 0.2104 0.0366  0.0046  0.0075  109 GLU A CA  
902  C C   . GLU A 112 ? 0.1516 0.0687 0.2413 0.0225  0.0036  0.0166  109 GLU A C   
903  O O   . GLU A 112 ? 0.1512 0.1140 0.2171 0.0084  0.0044  0.0207  109 GLU A O   
904  C CB  . GLU A 112 ? 0.1553 0.1156 0.2289 0.0320  -0.0085 -0.0774 109 GLU A CB  
905  C CG  . GLU A 112 ? 0.1677 0.2150 0.3013 0.0228  0.0214  -0.1359 109 GLU A CG  
906  C CD  . GLU A 112 ? 0.1931 0.3621 0.3656 0.0324  0.0287  -0.1897 109 GLU A CD  
907  O OE1 . GLU A 112 ? 0.1969 0.4484 0.2837 0.0056  0.0457  -0.0858 109 GLU A OE1 
908  O OE2 . GLU A 112 ? 0.2104 0.4227 0.4462 0.0234  0.0386  -0.1843 109 GLU A OE2 
909  N N   . ASP A 113 ? 0.1688 0.0775 0.1774 -0.0104 -0.0009 0.0073  110 ASP A N   
910  C CA  . ASP A 113 ? 0.1902 0.1032 0.1902 0.0017  0.0252  -0.0545 110 ASP A CA  
911  C C   . ASP A 113 ? 0.1715 0.0771 0.2094 0.0202  -0.0136 -0.0035 110 ASP A C   
912  O O   . ASP A 113 ? 0.1734 0.1146 0.2113 0.0292  -0.0317 -0.0057 110 ASP A O   
913  C CB  . ASP A 113 ? 0.2074 0.1385 0.1963 0.0018  0.0118  -0.0059 110 ASP A CB  
914  C CG  . ASP A 113 ? 0.2247 0.1526 0.2345 0.0064  0.0072  0.0048  110 ASP A CG  
915  O OD1 . ASP A 113 ? 0.2372 0.2329 0.2745 0.0095  -0.0322 0.0035  110 ASP A OD1 
916  O OD2 . ASP A 113 ? 0.2258 0.2691 0.2228 -0.0206 0.0368  0.0171  110 ASP A OD2 
917  N N   . ASP A 114 ? 0.1514 0.0638 0.1831 0.0004  -0.0332 0.0161  111 ASP A N   
918  C CA  . ASP A 114 ? 0.1378 0.0777 0.1445 0.0183  -0.0154 -0.0082 111 ASP A CA  
919  C C   . ASP A 114 ? 0.1310 0.0922 0.1375 0.0046  0.0025  0.0113  111 ASP A C   
920  O O   . ASP A 114 ? 0.1328 0.0739 0.1611 0.0105  0.0157  0.0234  111 ASP A O   
921  C CB  . ASP A 114 ? 0.1296 0.0728 0.1757 0.0159  0.0059  0.0134  111 ASP A CB  
922  C CG  . ASP A 114 ? 0.1540 0.0839 0.1756 0.0027  0.0126  -0.0089 111 ASP A CG  
923  O OD1 . ASP A 114 ? 0.1676 0.0809 0.1857 0.0088  -0.0094 0.0069  111 ASP A OD1 
924  O OD2 . ASP A 114 ? 0.1514 0.0852 0.1799 -0.0214 0.0254  -0.0107 111 ASP A OD2 
925  N N   . LYS A 115 ? 0.1241 0.0495 0.1787 -0.0075 -0.0006 -0.0183 112 LYS A N   
926  C CA  . LYS A 115 ? 0.1097 0.0698 0.1358 0.0089  0.0055  0.0116  112 LYS A CA  
927  C C   . LYS A 115 ? 0.1111 0.0440 0.1405 0.0072  -0.0263 0.0143  112 LYS A C   
928  O O   . LYS A 115 ? 0.1136 0.0995 0.1312 -0.0083 -0.0184 0.0139  112 LYS A O   
929  C CB  . LYS A 115 ? 0.1199 0.0885 0.1981 0.0167  0.0325  0.0101  112 LYS A CB  
930  C CG  . LYS A 115 ? 0.1313 0.0861 0.1787 -0.0068 0.0067  0.0450  112 LYS A CG  
931  C CD  . LYS A 115 ? 0.1345 0.0969 0.1533 -0.0323 -0.0055 0.0187  112 LYS A CD  
932  C CE  . LYS A 115 ? 0.1467 0.1214 0.1980 0.0055  0.0217  0.0856  112 LYS A CE  
933  N NZ  . LYS A 115 ? 0.1518 0.0781 0.2130 -0.0169 0.0356  0.0071  112 LYS A NZ  
934  N N   A LEU A 116 ? 0.1200 0.0471 0.1557 0.0040  0.0179  0.0041  113 LEU A N   
935  N N   B LEU A 116 ? 0.1201 0.0347 0.1222 -0.0024 0.0057  0.0011  113 LEU A N   
936  C CA  A LEU A 116 ? 0.1193 0.0899 0.1496 0.0044  0.0125  0.0137  113 LEU A CA  
937  C CA  B LEU A 116 ? 0.1248 0.0511 0.1046 -0.0085 -0.0024 0.0193  113 LEU A CA  
938  C C   A LEU A 116 ? 0.1083 0.0743 0.1475 0.0050  0.0189  0.0150  113 LEU A C   
939  C C   B LEU A 116 ? 0.1094 0.0528 0.1470 0.0054  -0.0012 0.0251  113 LEU A C   
940  O O   A LEU A 116 ? 0.1125 0.1178 0.1655 -0.0198 0.0322  -0.0230 113 LEU A O   
941  O O   B LEU A 116 ? 0.1129 0.1027 0.2111 -0.0030 -0.0155 0.0060  113 LEU A O   
942  C CB  A LEU A 116 ? 0.1293 0.1134 0.2145 -0.0028 0.0130  0.0239  113 LEU A CB  
943  C CB  B LEU A 116 ? 0.1332 0.0464 0.1388 -0.0294 0.0050  0.0041  113 LEU A CB  
944  C CG  A LEU A 116 ? 0.1252 0.1081 0.1572 0.0256  0.0029  0.0106  113 LEU A CG  
945  C CG  B LEU A 116 ? 0.1346 0.0442 0.1002 -0.0247 0.0177  -0.0049 113 LEU A CG  
946  C CD1 A LEU A 116 ? 0.1253 0.1621 0.1780 0.0027  0.0481  0.0015  113 LEU A CD1 
947  C CD1 B LEU A 116 ? 0.1420 0.0679 0.1806 -0.0157 0.0287  -0.0352 113 LEU A CD1 
948  C CD2 A LEU A 116 ? 0.1291 0.1254 0.1978 0.0684  0.0225  0.0262  113 LEU A CD2 
949  C CD2 B LEU A 116 ? 0.1586 0.0870 0.1118 0.0067  -0.0039 0.0567  113 LEU A CD2 
950  N N   . VAL A 117 ? 0.1010 0.0945 0.1442 0.0116  0.0189  -0.0044 114 VAL A N   
951  C CA  . VAL A 117 ? 0.0967 0.0813 0.1434 0.0125  0.0296  -0.0048 114 VAL A CA  
952  C C   . VAL A 117 ? 0.1140 0.0663 0.1769 -0.0078 0.0007  -0.0342 114 VAL A C   
953  O O   . VAL A 117 ? 0.0997 0.1023 0.2091 -0.0205 0.0136  -0.0281 114 VAL A O   
954  C CB  . VAL A 117 ? 0.1049 0.0835 0.1588 0.0165  0.0256  0.0110  114 VAL A CB  
955  C CG1 . VAL A 117 ? 0.1178 0.2044 0.1470 0.0243  0.0515  0.0206  114 VAL A CG1 
956  C CG2 . VAL A 117 ? 0.1214 0.1017 0.1984 0.0164  0.0222  0.0129  114 VAL A CG2 
957  N N   . VAL A 118 ? 0.1506 0.0510 0.1694 0.0288  0.0006  -0.0009 115 VAL A N   
958  C CA  . VAL A 118 ? 0.2085 0.0626 0.1658 0.0057  0.0308  -0.0221 115 VAL A CA  
959  C C   . VAL A 118 ? 0.1627 0.0744 0.1550 0.0151  0.0109  -0.0224 115 VAL A C   
960  O O   . VAL A 118 ? 0.1174 0.0919 0.2769 -0.0108 0.0040  -0.0037 115 VAL A O   
961  C CB  . VAL A 118 ? 0.3178 0.0976 0.1061 -0.0379 0.0459  -0.0168 115 VAL A CB  
962  C CG1 . VAL A 118 ? 0.5541 0.2465 0.2128 -0.0399 0.0474  -0.0180 115 VAL A CG1 
963  C CG2 . VAL A 118 ? 0.3159 0.1359 0.0859 -0.0647 0.0072  0.0018  115 VAL A CG2 
964  N N   . GLU A 119 ? 0.1597 0.0688 0.1602 0.0243  0.0086  -0.0326 116 GLU A N   
965  C CA  . GLU A 119 ? 0.1737 0.0781 0.1558 -0.0021 0.0331  -0.0491 116 GLU A CA  
966  C C   . GLU A 119 ? 0.1554 0.0652 0.1607 0.0116  0.0477  -0.0257 116 GLU A C   
967  O O   . GLU A 119 ? 0.1383 0.1135 0.1824 -0.0054 0.0210  0.0195  116 GLU A O   
968  C CB  . GLU A 119 ? 0.2216 0.2654 0.1430 -0.0355 -0.0110 -0.0291 116 GLU A CB  
969  C CG  . GLU A 119 ? 0.2765 0.5119 0.2733 -0.0489 -0.0788 -0.0057 116 GLU A CG  
970  C CD  . GLU A 119 ? 0.3073 0.6028 0.3746 -0.0879 -0.1174 -0.0070 116 GLU A CD  
971  O OE1 . GLU A 119 ? 0.3256 0.6631 0.4635 -0.0776 -0.1294 -0.0387 116 GLU A OE1 
972  O OE2 . GLU A 119 ? 0.3197 0.6410 0.4351 -0.0938 -0.0871 0.0296  116 GLU A OE2 
973  N N   . CYS A 120 ? 0.1505 0.0879 0.1658 0.0198  0.0359  0.0068  117 CYS A N   
974  C CA  . CYS A 120 ? 0.1597 0.1091 0.1714 0.0368  0.0277  0.0480  117 CYS A CA  
975  C C   . CYS A 120 ? 0.1524 0.0663 0.1688 0.0310  0.0319  0.0306  117 CYS A C   
976  O O   . CYS A 120 ? 0.1490 0.1180 0.2585 -0.0151 0.0840  0.0170  117 CYS A O   
977  C CB  . CYS A 120 ? 0.1944 0.1672 0.1858 0.0679  0.0525  0.0454  117 CYS A CB  
978  S SG  . CYS A 120 ? 0.2138 0.2484 0.1871 0.0816  0.0195  0.0036  117 CYS A SG  
979  N N   . VAL A 121 ? 0.1653 0.0672 0.1556 0.0122  -0.0059 0.0057  118 VAL A N   
980  C CA  . VAL A 121 ? 0.1820 0.0775 0.1754 -0.0137 -0.0215 -0.0053 118 VAL A CA  
981  C C   . VAL A 121 ? 0.1800 0.0886 0.1526 -0.0025 -0.0314 0.0097  118 VAL A C   
982  O O   . VAL A 121 ? 0.1764 0.0746 0.2044 -0.0241 0.0123  -0.0125 118 VAL A O   
983  C CB  . VAL A 121 ? 0.2018 0.1224 0.1822 0.0332  -0.0101 -0.0233 118 VAL A CB  
984  C CG1 . VAL A 121 ? 0.2163 0.1661 0.1588 0.0258  -0.0103 -0.0274 118 VAL A CG1 
985  C CG2 . VAL A 121 ? 0.2006 0.1170 0.2172 0.0369  -0.0030 0.0102  118 VAL A CG2 
986  N N   . MET A 122 ? 0.2031 0.0764 0.1997 0.0319  -0.0108 -0.0095 119 MET A N   
987  C CA  . MET A 122 ? 0.2349 0.0925 0.2481 0.0404  0.0205  -0.0477 119 MET A CA  
988  C C   . MET A 122 ? 0.2722 0.1092 0.2555 0.0341  0.0299  -0.0215 119 MET A C   
989  O O   . MET A 122 ? 0.2584 0.1945 0.1981 0.0759  0.0340  0.0175  119 MET A O   
990  C CB  . MET A 122 ? 0.2362 0.1457 0.2587 0.0605  0.0054  0.0091  119 MET A CB  
991  C CG  . MET A 122 ? 0.2391 0.2047 0.3029 0.0254  0.0782  0.0624  119 MET A CG  
992  S SD  . MET A 122 ? 0.2400 0.1257 0.4245 0.0136  0.1295  0.0176  119 MET A SD  
993  C CE  . MET A 122 ? 0.2401 0.1474 0.4141 -0.0010 0.1192  -0.0396 119 MET A CE  
994  N N   . LYS A 123 ? 0.3244 0.1492 0.2378 0.0353  0.0689  -0.0478 120 LYS A N   
995  C CA  . LYS A 123 ? 0.3557 0.1970 0.3256 0.0412  0.0696  -0.0333 120 LYS A CA  
996  C C   . LYS A 123 ? 0.3638 0.2351 0.3018 0.0075  0.0578  -0.0442 120 LYS A C   
997  O O   . LYS A 123 ? 0.3711 0.3257 0.2647 0.0285  0.1066  -0.0281 120 LYS A O   
998  C CB  . LYS A 123 ? 0.3723 0.2988 0.4451 0.0513  0.1164  -0.0821 120 LYS A CB  
999  C CG  . LYS A 123 ? 0.3945 0.3780 0.5560 0.0289  0.1160  -0.1110 120 LYS A CG  
1000 C CD  . LYS A 123 ? 0.4104 0.4272 0.6454 0.0194  0.1145  -0.0837 120 LYS A CD  
1001 C CE  . LYS A 123 ? 0.4226 0.4422 0.6658 0.0147  0.1091  -0.1104 120 LYS A CE  
1002 N NZ  . LYS A 123 ? 0.4327 0.4666 0.6870 0.0148  0.1020  -0.1262 120 LYS A NZ  
1003 N N   . GLY A 124 ? 0.3531 0.1205 0.2338 -0.0297 -0.0052 -0.0616 121 GLY A N   
1004 C CA  . GLY A 124 ? 0.3472 0.1374 0.2644 -0.0384 -0.0170 -0.0124 121 GLY A CA  
1005 C C   . GLY A 124 ? 0.3173 0.1192 0.1983 -0.0174 0.0086  -0.0158 121 GLY A C   
1006 O O   . GLY A 124 ? 0.3436 0.1533 0.2966 0.0348  -0.0113 -0.0036 121 GLY A O   
1007 N N   . VAL A 125 ? 0.2531 0.1560 0.1697 0.0009  0.0214  -0.0151 122 VAL A N   
1008 C CA  . VAL A 125 ? 0.2133 0.1888 0.1615 0.0370  0.0324  -0.0262 122 VAL A CA  
1009 C C   . VAL A 125 ? 0.1807 0.1521 0.1081 0.0203  0.0297  -0.0462 122 VAL A C   
1010 O O   . VAL A 125 ? 0.1814 0.1413 0.1622 -0.0172 0.0299  0.0268  122 VAL A O   
1011 C CB  . VAL A 125 ? 0.2208 0.2320 0.2122 0.0233  -0.0036 -0.0745 122 VAL A CB  
1012 C CG1 . VAL A 125 ? 0.2273 0.2890 0.2574 0.0167  -0.0396 -0.0674 122 VAL A CG1 
1013 C CG2 . VAL A 125 ? 0.2163 0.2637 0.2576 0.0387  0.0205  -0.0490 122 VAL A CG2 
1014 N N   . THR A 126 ? 0.1714 0.1779 0.1622 0.0255  0.0162  -0.0333 123 THR A N   
1015 C CA  . THR A 126 ? 0.1658 0.1524 0.1622 0.0067  0.0299  0.0100  123 THR A CA  
1016 C C   . THR A 126 ? 0.1650 0.1531 0.1850 -0.0373 0.0620  -0.0457 123 THR A C   
1017 O O   . THR A 126 ? 0.1898 0.2037 0.2039 -0.0857 0.0545  -0.0115 123 THR A O   
1018 C CB  . THR A 126 ? 0.1776 0.1381 0.2291 0.0155  -0.0066 0.0209  123 THR A CB  
1019 O OG1 . THR A 126 ? 0.1811 0.1713 0.2736 -0.0032 -0.0240 0.0437  123 THR A OG1 
1020 C CG2 . THR A 126 ? 0.1923 0.1973 0.2926 0.0075  0.0159  0.0064  123 THR A CG2 
1021 N N   . SER A 127 ? 0.1491 0.0912 0.1893 -0.0040 0.0464  -0.0339 124 SER A N   
1022 C CA  . SER A 127 ? 0.1421 0.1275 0.1449 -0.0080 0.0304  -0.0516 124 SER A CA  
1023 C C   . SER A 127 ? 0.1328 0.0772 0.2214 0.0056  0.0328  -0.0228 124 SER A C   
1024 O O   . SER A 127 ? 0.1203 0.0929 0.2609 -0.0206 0.0405  -0.0112 124 SER A O   
1025 C CB  . SER A 127 ? 0.1757 0.1874 0.1131 0.0446  -0.0254 -0.0686 124 SER A CB  
1026 O OG  . SER A 127 ? 0.1886 0.2412 0.2571 0.0304  0.0021  -0.0021 124 SER A OG  
1027 N N   . THR A 128 ? 0.1357 0.1072 0.1757 0.0284  0.0217  -0.0082 125 THR A N   
1028 C CA  . THR A 128 ? 0.1337 0.1049 0.1597 0.0027  -0.0088 -0.0114 125 THR A CA  
1029 C C   . THR A 128 ? 0.1178 0.0961 0.1290 0.0068  0.0434  0.0318  125 THR A C   
1030 O O   . THR A 128 ? 0.1197 0.1223 0.2052 -0.0310 0.0489  -0.0055 125 THR A O   
1031 C CB  . THR A 128 ? 0.1543 0.1060 0.1362 0.0036  -0.0246 0.0176  125 THR A CB  
1032 O OG1 . THR A 128 ? 0.1716 0.1143 0.1646 -0.0159 -0.0218 -0.0218 125 THR A OG1 
1033 C CG2 . THR A 128 ? 0.1417 0.1479 0.1838 0.0130  0.0013  0.0190  125 THR A CG2 
1034 N N   . ARG A 129 ? 0.1202 0.0822 0.1083 0.0158  0.0255  -0.0209 126 ARG A N   
1035 C CA  . ARG A 129 ? 0.1058 0.0970 0.1034 0.0302  -0.0026 -0.0105 126 ARG A CA  
1036 C C   . ARG A 129 ? 0.0894 0.0760 0.1770 0.0286  -0.0321 -0.0235 126 ARG A C   
1037 O O   . ARG A 129 ? 0.0702 0.1274 0.2558 0.0041  -0.0005 -0.0216 126 ARG A O   
1038 C CB  . ARG A 129 ? 0.1197 0.1509 0.1569 0.0532  -0.0412 -0.0257 126 ARG A CB  
1039 C CG  . ARG A 129 ? 0.1536 0.1690 0.1962 0.0802  -0.0239 0.0428  126 ARG A CG  
1040 C CD  . ARG A 129 ? 0.1871 0.2439 0.2100 0.0646  -0.0378 0.0434  126 ARG A CD  
1041 N NE  . ARG A 129 ? 0.1981 0.2423 0.2052 0.0716  -0.0345 -0.0219 126 ARG A NE  
1042 C CZ  . ARG A 129 ? 0.2071 0.2416 0.2624 0.0893  -0.0180 -0.0619 126 ARG A CZ  
1043 N NH1 . ARG A 129 ? 0.2075 0.2315 0.2984 0.1275  -0.0165 -0.0253 126 ARG A NH1 
1044 N NH2 . ARG A 129 ? 0.2255 0.2441 0.2892 0.0816  -0.0250 -0.0278 126 ARG A NH2 
1045 N N   . VAL A 130 ? 0.0990 0.0695 0.1801 0.0205  0.0007  -0.0125 127 VAL A N   
1046 C CA  . VAL A 130 ? 0.0969 0.0992 0.1371 0.0183  0.0003  0.0261  127 VAL A CA  
1047 C C   . VAL A 130 ? 0.1013 0.0761 0.1527 -0.0071 -0.0043 -0.0038 127 VAL A C   
1048 O O   . VAL A 130 ? 0.1239 0.1003 0.1635 -0.0196 0.0129  -0.0135 127 VAL A O   
1049 C CB  . VAL A 130 ? 0.1263 0.1027 0.1085 0.0329  0.0252  0.0277  127 VAL A CB  
1050 C CG1 . VAL A 130 ? 0.1448 0.0908 0.2249 0.0509  0.0005  0.0213  127 VAL A CG1 
1051 C CG2 . VAL A 130 ? 0.1325 0.1608 0.1155 0.0499  0.0471  -0.0091 127 VAL A CG2 
1052 N N   . TYR A 131 ? 0.1149 0.0822 0.1298 0.0086  0.0293  -0.0159 128 TYR A N   
1053 C CA  . TYR A 131 ? 0.1240 0.0438 0.1494 0.0170  0.0075  -0.0033 128 TYR A CA  
1054 C C   . TYR A 131 ? 0.1295 0.0808 0.1137 0.0237  -0.0017 -0.0054 128 TYR A C   
1055 O O   . TYR A 131 ? 0.1336 0.0760 0.1738 0.0008  -0.0058 0.0143  128 TYR A O   
1056 C CB  . TYR A 131 ? 0.1279 0.0898 0.1708 0.0093  -0.0092 0.0640  128 TYR A CB  
1057 C CG  . TYR A 131 ? 0.1315 0.0604 0.1830 0.0070  -0.0055 0.0370  128 TYR A CG  
1058 C CD1 . TYR A 131 ? 0.1403 0.0864 0.2292 0.0246  0.0000  -0.0253 128 TYR A CD1 
1059 C CD2 . TYR A 131 ? 0.1374 0.0881 0.1421 0.0103  -0.0225 0.0576  128 TYR A CD2 
1060 C CE1 . TYR A 131 ? 0.1432 0.0725 0.2520 0.0212  0.0342  0.0059  128 TYR A CE1 
1061 C CE2 . TYR A 131 ? 0.1371 0.1086 0.2841 0.0350  0.0153  0.0553  128 TYR A CE2 
1062 C CZ  . TYR A 131 ? 0.1429 0.0914 0.2560 0.0310  0.0055  0.0461  128 TYR A CZ  
1063 O OH  . TYR A 131 ? 0.1577 0.1525 0.2891 0.0425  0.0005  0.0833  128 TYR A OH  
1064 N N   . GLU A 132 ? 0.1178 0.0849 0.1477 0.0033  0.0260  -0.0287 129 GLU A N   
1065 C CA  . GLU A 132 ? 0.1182 0.0584 0.1808 0.0117  0.0212  0.0149  129 GLU A CA  
1066 C C   . GLU A 132 ? 0.1067 0.0775 0.1295 0.0142  -0.0001 0.0285  129 GLU A C   
1067 O O   . GLU A 132 ? 0.1035 0.1058 0.1341 0.0120  -0.0087 0.0280  129 GLU A O   
1068 C CB  . GLU A 132 ? 0.1443 0.1055 0.1989 -0.0247 -0.0102 0.0144  129 GLU A CB  
1069 C CG  . GLU A 132 ? 0.1712 0.1188 0.2633 -0.0682 0.0286  0.0095  129 GLU A CG  
1070 C CD  . GLU A 132 ? 0.1972 0.1571 0.2861 -0.0542 0.0683  0.0179  129 GLU A CD  
1071 O OE1 . GLU A 132 ? 0.2249 0.1392 0.3381 -0.0413 0.1030  -0.0120 129 GLU A OE1 
1072 O OE2 . GLU A 132 ? 0.2060 0.2581 0.3111 -0.0822 0.0138  -0.0110 129 GLU A OE2 
1073 N N   . ARG A 133 ? 0.1145 0.0782 0.1876 0.0271  0.0034  0.0011  130 ARG A N   
1074 C CA  . ARG A 133 ? 0.1243 0.0925 0.1152 0.0493  -0.0107 -0.0285 130 ARG A CA  
1075 C C   . ARG A 133 ? 0.1291 0.1100 0.1104 -0.0058 -0.0155 -0.0149 130 ARG A C   
1076 O O   . ARG A 133 ? 0.1498 0.0774 0.1851 0.0056  0.0065  -0.0010 130 ARG A O   
1077 C CB  . ARG A 133 ? 0.1379 0.0867 0.1815 0.0269  -0.0208 -0.0581 130 ARG A CB  
1078 C CG  . ARG A 133 ? 0.1271 0.1967 0.2398 0.0071  -0.0247 -0.1217 130 ARG A CG  
1079 C CD  . ARG A 133 ? 0.1338 0.1768 0.2536 -0.0588 0.0370  -0.0528 130 ARG A CD  
1080 N NE  . ARG A 133 ? 0.1311 0.1061 0.1949 -0.0478 0.0425  -0.0328 130 ARG A NE  
1081 C CZ  . ARG A 133 ? 0.1323 0.0806 0.2031 0.0143  0.0206  0.0131  130 ARG A CZ  
1082 N NH1 . ARG A 133 ? 0.1241 0.0884 0.2509 0.0051  0.0434  0.0132  130 ARG A NH1 
1083 N NH2 . ARG A 133 ? 0.1408 0.1225 0.1645 0.0073  0.0177  0.0009  130 ARG A NH2 
1084 N N   . ALA A 134 ? 0.1254 0.1468 0.1382 0.0054  -0.0150 -0.0050 131 ALA A N   
1085 C CA  . ALA A 134 ? 0.1533 0.1054 0.1633 -0.0004 -0.0110 -0.0152 131 ALA A CA  
1086 C C   . ALA A 134 ? 0.1747 0.1206 0.1980 -0.0515 0.0157  0.0296  131 ALA A C   
1087 O O   . ALA A 134 ? 0.1854 0.0831 0.1727 -0.0203 0.0089  -0.0123 131 ALA A O   
1088 C CB  . ALA A 134 ? 0.1593 0.1139 0.1770 -0.0002 -0.0208 0.0765  131 ALA A CB  
1089 O OXT . ALA A 134 ? 0.1929 0.1661 0.2530 -0.0354 0.0131  -0.0542 131 ALA A OXT 
# 
