data_8Y1W
# 
_entry.id   8Y1W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8Y1W         pdb_00008y1w 10.2210/pdb8y1w/pdb 
WWPDB D_1300044695 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        8Y1W 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              takato.yano@ompu.ac.jp 
_pdbx_contact_author.name_first         Takato 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9720-8339 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fukui, K.'    1 0000-0003-2463-7578 
'Murakawa, T.' 2 0000-0001-5905-532X 
'Yano, T.'     3 0000-0002-9720-8339 
# 
_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            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                e5185 
_citation.page_last                 e5185 
_citation.title                     
;dUTP pyrophosphatases from hyperthermophilic eubacterium and archaeon: Structural and functional examinations on the suitability for PCR application.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.5185 
_citation.pdbx_database_id_PubMed   39440877 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fukui, K.'    1 0000-0003-2463-7578 
primary 'Kondo, N.'    2 0000-0002-6624-5989 
primary 'Murakawa, T.' 3 ?                   
primary 'Baba, S.'     4 ?                   
primary 'Kumasaka, T.' 5 ?                   
primary 'Yano, T.'     6 ?                   
# 
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 'dCTP deaminase'                   17716.566 1   3.5.4.13 ? ? ? 
2 non-polymer syn GLYCEROL                           92.094    1   ?        ? ? ? 
3 non-polymer nat 
;2'-DEOXYURIDINE 5'-MONOPHOSPHATE
;
308.182   1   ?        ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'                    94.971    2   ?        ? ? ? 
5 water       nat water                              18.015    100 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Deoxycytidine triphosphate deaminase' 
# 
_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       
;MMLPDWKIRKEILIEPFNEKSLQPAGYDLRVGKEAYINGRLINVEKEGKVVIPPKTHALILTLERVKLPDDVMGDMKLRS
SLAREGLLGSFAWVDPGWDGNLTLMLFNASEEPVELNYGERFVQIAFIRLEGPAKNPYRGNYQGSQHLVLSKRRK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMLPDWKIRKEILIEPFNEKSLQPAGYDLRVGKEAYINGRLINVEKEGKVVIPPKTHALILTLERVKLPDDVMGDMKLRS
SLAREGLLGSFAWVDPGWDGNLTLMLFNASEEPVELNYGERFVQIAFIRLEGPAKNPYRGNYQGSQHLVLSKRRK
;
_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 GLYCEROL                           GOL 
3 
;2'-DEOXYURIDINE 5'-MONOPHOSPHATE
;
UMP 
4 'PHOSPHATE ION'                    PO4 
5 water                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   LEU n 
1 4   PRO n 
1 5   ASP n 
1 6   TRP n 
1 7   LYS n 
1 8   ILE n 
1 9   ARG n 
1 10  LYS n 
1 11  GLU n 
1 12  ILE n 
1 13  LEU n 
1 14  ILE n 
1 15  GLU n 
1 16  PRO n 
1 17  PHE n 
1 18  ASN n 
1 19  GLU n 
1 20  LYS n 
1 21  SER n 
1 22  LEU n 
1 23  GLN n 
1 24  PRO n 
1 25  ALA n 
1 26  GLY n 
1 27  TYR n 
1 28  ASP n 
1 29  LEU n 
1 30  ARG n 
1 31  VAL n 
1 32  GLY n 
1 33  LYS n 
1 34  GLU n 
1 35  ALA n 
1 36  TYR n 
1 37  ILE n 
1 38  ASN n 
1 39  GLY n 
1 40  ARG n 
1 41  LEU n 
1 42  ILE n 
1 43  ASN n 
1 44  VAL n 
1 45  GLU n 
1 46  LYS n 
1 47  GLU n 
1 48  GLY n 
1 49  LYS n 
1 50  VAL n 
1 51  VAL n 
1 52  ILE n 
1 53  PRO n 
1 54  PRO n 
1 55  LYS n 
1 56  THR n 
1 57  HIS n 
1 58  ALA n 
1 59  LEU n 
1 60  ILE n 
1 61  LEU n 
1 62  THR n 
1 63  LEU n 
1 64  GLU n 
1 65  ARG n 
1 66  VAL n 
1 67  LYS n 
1 68  LEU n 
1 69  PRO n 
1 70  ASP n 
1 71  ASP n 
1 72  VAL n 
1 73  MET n 
1 74  GLY n 
1 75  ASP n 
1 76  MET n 
1 77  LYS n 
1 78  LEU n 
1 79  ARG n 
1 80  SER n 
1 81  SER n 
1 82  LEU n 
1 83  ALA n 
1 84  ARG n 
1 85  GLU n 
1 86  GLY n 
1 87  LEU n 
1 88  LEU n 
1 89  GLY n 
1 90  SER n 
1 91  PHE n 
1 92  ALA n 
1 93  TRP n 
1 94  VAL n 
1 95  ASP n 
1 96  PRO n 
1 97  GLY n 
1 98  TRP n 
1 99  ASP n 
1 100 GLY n 
1 101 ASN n 
1 102 LEU n 
1 103 THR n 
1 104 LEU n 
1 105 MET n 
1 106 LEU n 
1 107 PHE n 
1 108 ASN n 
1 109 ALA n 
1 110 SER n 
1 111 GLU n 
1 112 GLU n 
1 113 PRO n 
1 114 VAL n 
1 115 GLU n 
1 116 LEU n 
1 117 ASN n 
1 118 TYR n 
1 119 GLY n 
1 120 GLU n 
1 121 ARG n 
1 122 PHE n 
1 123 VAL n 
1 124 GLN n 
1 125 ILE n 
1 126 ALA n 
1 127 PHE n 
1 128 ILE n 
1 129 ARG n 
1 130 LEU n 
1 131 GLU n 
1 132 GLY n 
1 133 PRO n 
1 134 ALA n 
1 135 LYS n 
1 136 ASN n 
1 137 PRO n 
1 138 TYR n 
1 139 ARG n 
1 140 GLY n 
1 141 ASN n 
1 142 TYR n 
1 143 GLN n 
1 144 GLY n 
1 145 SER n 
1 146 GLN n 
1 147 HIS n 
1 148 LEU n 
1 149 VAL n 
1 150 LEU n 
1 151 SER n 
1 152 LYS n 
1 153 ARG n 
1 154 ARG n 
1 155 LYS 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                   155 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'dut, dcd, A3L08_04840' 
_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      'Thermococcus pacificus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     71998 
_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               'Rosetta2(DE3) pLysS' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET11a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                            ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ?                               'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE                          ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                           'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                          ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                         ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                            ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                             ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                         ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                      ?                               'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                    ?                               'O4 P -3'        94.971  
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 
UMP non-polymer         . 
;2'-DEOXYURIDINE 5'-MONOPHOSPHATE
;
DUMP                            'C9 H13 N2 O8 P' 308.182 
VAL 'L-peptide linking' y VALINE                             ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   MET 2   2   2   MET MET A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   TRP 6   6   6   TRP TRP A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  TRP 93  93  93  TRP TRP A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 ARG 139 139 ?   ?   ?   A . n 
A 1 140 GLY 140 140 ?   ?   ?   A . n 
A 1 141 ASN 141 141 ?   ?   ?   A . n 
A 1 142 TYR 142 142 ?   ?   ?   A . n 
A 1 143 GLN 143 143 ?   ?   ?   A . n 
A 1 144 GLY 144 144 ?   ?   ?   A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLN 146 146 146 GLN GLN A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 ARG 154 154 ?   ?   ?   A . n 
A 1 155 LYS 155 155 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UMP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UMP 
_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 GOL 1   201 202 GOL GOL A . 
C 3 UMP 1   202 1   UMP DU  A . 
D 4 PO4 1   203 1   PO4 PO4 A . 
E 4 PO4 1   204 2   PO4 PO4 A . 
F 5 HOH 1   301 25  HOH HOH A . 
F 5 HOH 2   302 58  HOH HOH A . 
F 5 HOH 3   303 83  HOH HOH A . 
F 5 HOH 4   304 32  HOH HOH A . 
F 5 HOH 5   305 57  HOH HOH A . 
F 5 HOH 6   306 67  HOH HOH A . 
F 5 HOH 7   307 87  HOH HOH A . 
F 5 HOH 8   308 47  HOH HOH A . 
F 5 HOH 9   309 59  HOH HOH A . 
F 5 HOH 10  310 41  HOH HOH A . 
F 5 HOH 11  311 91  HOH HOH A . 
F 5 HOH 12  312 65  HOH HOH A . 
F 5 HOH 13  313 29  HOH HOH A . 
F 5 HOH 14  314 86  HOH HOH A . 
F 5 HOH 15  315 88  HOH HOH A . 
F 5 HOH 16  316 72  HOH HOH A . 
F 5 HOH 17  317 28  HOH HOH A . 
F 5 HOH 18  318 99  HOH HOH A . 
F 5 HOH 19  319 19  HOH HOH A . 
F 5 HOH 20  320 22  HOH HOH A . 
F 5 HOH 21  321 42  HOH HOH A . 
F 5 HOH 22  322 33  HOH HOH A . 
F 5 HOH 23  323 11  HOH HOH A . 
F 5 HOH 24  324 36  HOH HOH A . 
F 5 HOH 25  325 4   HOH HOH A . 
F 5 HOH 26  326 23  HOH HOH A . 
F 5 HOH 27  327 95  HOH HOH A . 
F 5 HOH 28  328 5   HOH HOH A . 
F 5 HOH 29  329 17  HOH HOH A . 
F 5 HOH 30  330 79  HOH HOH A . 
F 5 HOH 31  331 55  HOH HOH A . 
F 5 HOH 32  332 89  HOH HOH A . 
F 5 HOH 33  333 24  HOH HOH A . 
F 5 HOH 34  334 35  HOH HOH A . 
F 5 HOH 35  335 66  HOH HOH A . 
F 5 HOH 36  336 8   HOH HOH A . 
F 5 HOH 37  337 7   HOH HOH A . 
F 5 HOH 38  338 81  HOH HOH A . 
F 5 HOH 39  339 2   HOH HOH A . 
F 5 HOH 40  340 37  HOH HOH A . 
F 5 HOH 41  341 20  HOH HOH A . 
F 5 HOH 42  342 50  HOH HOH A . 
F 5 HOH 43  343 85  HOH HOH A . 
F 5 HOH 44  344 64  HOH HOH A . 
F 5 HOH 45  345 31  HOH HOH A . 
F 5 HOH 46  346 54  HOH HOH A . 
F 5 HOH 47  347 78  HOH HOH A . 
F 5 HOH 48  348 48  HOH HOH A . 
F 5 HOH 49  349 16  HOH HOH A . 
F 5 HOH 50  350 102 HOH HOH A . 
F 5 HOH 51  351 53  HOH HOH A . 
F 5 HOH 52  352 82  HOH HOH A . 
F 5 HOH 53  353 63  HOH HOH A . 
F 5 HOH 54  354 56  HOH HOH A . 
F 5 HOH 55  355 21  HOH HOH A . 
F 5 HOH 56  356 90  HOH HOH A . 
F 5 HOH 57  357 27  HOH HOH A . 
F 5 HOH 58  358 93  HOH HOH A . 
F 5 HOH 59  359 98  HOH HOH A . 
F 5 HOH 60  360 100 HOH HOH A . 
F 5 HOH 61  361 101 HOH HOH A . 
F 5 HOH 62  362 77  HOH HOH A . 
F 5 HOH 63  363 69  HOH HOH A . 
F 5 HOH 64  364 3   HOH HOH A . 
F 5 HOH 65  365 14  HOH HOH A . 
F 5 HOH 66  366 40  HOH HOH A . 
F 5 HOH 67  367 6   HOH HOH A . 
F 5 HOH 68  368 80  HOH HOH A . 
F 5 HOH 69  369 39  HOH HOH A . 
F 5 HOH 70  370 76  HOH HOH A . 
F 5 HOH 71  371 1   HOH HOH A . 
F 5 HOH 72  372 51  HOH HOH A . 
F 5 HOH 73  373 49  HOH HOH A . 
F 5 HOH 74  374 10  HOH HOH A . 
F 5 HOH 75  375 92  HOH HOH A . 
F 5 HOH 76  376 9   HOH HOH A . 
F 5 HOH 77  377 18  HOH HOH A . 
F 5 HOH 78  378 30  HOH HOH A . 
F 5 HOH 79  379 34  HOH HOH A . 
F 5 HOH 80  380 26  HOH HOH A . 
F 5 HOH 81  381 84  HOH HOH A . 
F 5 HOH 82  382 70  HOH HOH A . 
F 5 HOH 83  383 45  HOH HOH A . 
F 5 HOH 84  384 52  HOH HOH A . 
F 5 HOH 85  385 60  HOH HOH A . 
F 5 HOH 86  386 15  HOH HOH A . 
F 5 HOH 87  387 12  HOH HOH A . 
F 5 HOH 88  388 73  HOH HOH A . 
F 5 HOH 89  389 94  HOH HOH A . 
F 5 HOH 90  390 62  HOH HOH A . 
F 5 HOH 91  391 44  HOH HOH A . 
F 5 HOH 92  392 97  HOH HOH A . 
F 5 HOH 93  393 38  HOH HOH A . 
F 5 HOH 94  394 13  HOH HOH A . 
F 5 HOH 95  395 75  HOH HOH A . 
F 5 HOH 96  396 61  HOH HOH A . 
F 5 HOH 97  397 46  HOH HOH A . 
F 5 HOH 98  398 74  HOH HOH A . 
F 5 HOH 99  399 96  HOH HOH A . 
F 5 HOH 100 400 68  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 10  ? NZ  ? A LYS 10  NZ  
2  1 Y 1 A LYS 20  ? CG  ? A LYS 20  CG  
3  1 Y 1 A LYS 20  ? CD  ? A LYS 20  CD  
4  1 Y 1 A LYS 20  ? CE  ? A LYS 20  CE  
5  1 Y 1 A LYS 20  ? NZ  ? A LYS 20  NZ  
6  1 Y 1 A LEU 41  ? CD1 ? A LEU 41  CD1 
7  1 Y 1 A LEU 41  ? CD2 ? A LEU 41  CD2 
8  1 Y 1 A LYS 67  ? CE  ? A LYS 67  CE  
9  1 Y 1 A LYS 67  ? NZ  ? A LYS 67  NZ  
10 1 Y 1 A ASP 70  ? CG  ? A ASP 70  CG  
11 1 Y 1 A ASP 70  ? OD1 ? A ASP 70  OD1 
12 1 Y 1 A ASP 70  ? OD2 ? A ASP 70  OD2 
13 1 Y 1 A LYS 152 ? CE  ? A LYS 152 CE  
14 1 Y 1 A LYS 152 ? NZ  ? A LYS 152 NZ  
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21-5207   3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.92    4 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y1W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.616 
_cell.length_a_esd                 ? 
_cell.length_b                     52.616 
_cell.length_b_esd                 ? 
_cell.length_c                     87.519 
_cell.length_c_esd                 ? 
_cell.volume                       209830.510 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8Y1W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            'P 6c' 
_symmetry.space_group_name_H-M             'P 63' 
_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                   8Y1W 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.9 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.2 
_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    '56 mM sodium phosphate, 1.34 M potassium phosphate (pH 8.2)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          18.06 
_reflns.entry_id                                       8Y1W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.36 
_reflns.d_resolution_low                               43.76 
_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                                     29438 
_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                           99.24 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.5 
_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                                0.1 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1 
_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                                    1.36 
_reflns_shell.d_res_low                                     1.40 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2280 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.81 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.95 
_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                                  0.79 
_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                               24.45 
_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                                 8Y1W 
_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                            1.36 
_refine.ls_d_res_low                             43.76 
_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                     29437 
_refine.ls_number_reflns_R_free                  1710 
_refine.ls_number_reflns_R_work                  27727 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1515 
_refine.ls_R_factor_R_free                       0.1794 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1498 
_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                          1.44 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 17.9944 
_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                            0.1558 
_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.details                          ? 
_refine_hist.d_res_high                       1.36 
_refine_hist.d_res_low                        43.76 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               1300 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1164 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0149  ? 1236 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.3672  ? 1676 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1125  ? 182  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0099  ? 211  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.7971 ? 474  ? f_dihedral_angle_d ? ? 
# 
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' 1.36 1.40  . . 138 2280 98.94  . . . . 0.1753 . . . . . . . . . . . 0.2211 
'X-RAY DIFFRACTION' 1.40 1.45  . . 144 2286 99.79  . . . . 0.1450 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 1.45 1.50  . . 147 2317 99.88  . . . . 0.1308 . . . . . . . . . . . 0.1623 
'X-RAY DIFFRACTION' 1.50 1.56  . . 140 2298 99.96  . . . . 0.1380 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 1.56 1.63  . . 139 2326 99.92  . . . . 0.1664 . . . . . . . . . . . 0.2514 
'X-RAY DIFFRACTION' 1.63 1.71  . . 142 2293 100.00 . . . . 0.1509 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 1.71 1.82  . . 144 2321 100.00 . . . . 0.1326 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 1.82 1.96  . . 145 2309 100.00 . . . . 0.1432 . . . . . . . . . . . 0.1381 
'X-RAY DIFFRACTION' 1.96 2.16  . . 139 2287 100.00 . . . . 0.1432 . . . . . . . . . . . 0.1769 
'X-RAY DIFFRACTION' 2.16 2.47  . . 150 2325 100.00 . . . . 0.1545 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.47 3.11  . . 140 2336 100.00 . . . . 0.1726 . . . . . . . . . . . 0.1756 
'X-RAY DIFFRACTION' 3.11 43.76 . . 142 2349 99.92  . . . . 0.1412 . . . . . . . . . . . 0.1674 
# 
_struct.entry_id                     8Y1W 
_struct.title                        'Crystal structure of Thermococcus pacificus dUTPase complexed with dUMP.' 
_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        8Y1W 
_struct_keywords.text            'dUTPase, dUTP, dUMP, hyperthermophile, Thermococcus pacificus, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    K7PBY4_9EURY 
_struct_ref.pdbx_db_accession          K7PBY4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MMLPDWKIRKEILIEPFNEKSLQPAGYDLRVGKEAYINGRLINVEKEGKVVIPPKTHALILTLERVKLPDDVMGDMKLRS
SLAREGLLGSFAWVDPGWDGNLTLMLFNASEEPVELNYGERFVQIAFIRLEGPAKNPYRGNYQGSQHLVLSKRRK
;
_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              8Y1W 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 155 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             K7PBY4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  155 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       155 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 PRO A 4  ? ILE A 12 ? PRO A 4  ILE A 12 1 ? 9 
HELX_P HELX_P2 AA2 ASN A 18 ? LYS A 20 ? ASN A 18 LYS A 20 5 ? 3 
HELX_P HELX_P3 AA3 VAL A 44 ? GLY A 48 ? VAL A 44 GLY A 48 1 ? 5 
HELX_P HELX_P4 AA4 ARG A 79 ? GLU A 85 ? ARG A 79 GLU A 85 1 ? 7 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           15 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            15 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    16 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     16 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
# 
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 5 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 3 5 ? anti-parallel 
AA1 3 9 ? anti-parallel 
AA1 5 8 ? anti-parallel 
AA1 6 9 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? 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 LEU A 13  ? GLU A 15  ? LEU A 13  GLU A 15  
AA1 2 LEU A 22  ? GLN A 23  ? LEU A 22  GLN A 23  
AA1 3 GLY A 26  ? ILE A 37  ? GLY A 26  ILE A 37  
AA1 4 ARG A 40  ? ASN A 43  ? ARG A 40  ASN A 43  
AA1 5 THR A 56  ? LYS A 67  ? THR A 56  LYS A 67  
AA1 6 VAL A 72  ? LEU A 78  ? VAL A 72  LEU A 78  
AA1 7 LEU A 87  ? SER A 90  ? LEU A 87  SER A 90  
AA1 8 ASP A 99  ? ASN A 108 ? ASP A 99  ASN A 108 
AA1 9 ARG A 121 ? ARG A 129 ? ARG A 121 ARG A 129 
AA2 1 LYS A 49  ? ILE A 52  ? LYS A 49  ILE A 52  
AA2 2 VAL A 114 ? ASN A 117 ? VAL A 114 ASN A 117 
# 
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 5 N GLU A 15 ? N GLU A 15 O ARG A 65  ? O ARG A 65  
AA1 2 3 N GLN A 23 ? N GLN A 23 O GLY A 26  ? O GLY A 26  
AA1 3 4 N ALA A 35 ? N ALA A 35 O ILE A 42  ? O ILE A 42  
AA1 3 5 N ARG A 30 ? N ARG A 30 O LEU A 63  ? O LEU A 63  
AA1 3 9 N LEU A 29 ? N LEU A 29 O PHE A 122 ? O PHE A 122 
AA1 5 8 N THR A 56 ? N THR A 56 O ASN A 108 ? O ASN A 108 
AA1 6 9 N MET A 73 ? N MET A 73 O ILE A 128 ? O ILE A 128 
AA1 7 8 N LEU A 88 ? N LEU A 88 O PHE A 107 ? O PHE A 107 
AA2 1 2 N ILE A 52 ? N ILE A 52 O VAL A 114 ? O VAL A 114 
# 
_pdbx_entry_details.entry_id                   8Y1W 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     25 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -140.14 
_pdbx_validate_torsion.psi             42.01 
# 
_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    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     311 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z        
2 x-y,x,z+1/2  
3 y,-x+y,z+1/2 
4 -y,x-y,z     
5 -x+y,-x,z    
6 -x,-y,z+1/2  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ARG 139 ? A ARG 139 
2 1 Y 1 A GLY 140 ? A GLY 140 
3 1 Y 1 A ASN 141 ? A ASN 141 
4 1 Y 1 A TYR 142 ? A TYR 142 
5 1 Y 1 A GLN 143 ? A GLN 143 
6 1 Y 1 A GLY 144 ? A GLY 144 
7 1 Y 1 A ARG 154 ? A ARG 154 
8 1 Y 1 A LYS 155 ? A LYS 155 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
GLN N      N N N 74  
GLN CA     C N S 75  
GLN C      C N N 76  
GLN O      O N N 77  
GLN CB     C N N 78  
GLN CG     C N N 79  
GLN CD     C N N 80  
GLN OE1    O N N 81  
GLN NE2    N N N 82  
GLN OXT    O N N 83  
GLN H      H N N 84  
GLN H2     H N N 85  
GLN HA     H N N 86  
GLN HB2    H N N 87  
GLN HB3    H N N 88  
GLN HG2    H N N 89  
GLN HG3    H N N 90  
GLN HE21   H N N 91  
GLN HE22   H N N 92  
GLN HXT    H N N 93  
GLU N      N N N 94  
GLU CA     C N S 95  
GLU C      C N N 96  
GLU O      O N N 97  
GLU CB     C N N 98  
GLU CG     C N N 99  
GLU CD     C N N 100 
GLU OE1    O N N 101 
GLU OE2    O N N 102 
GLU OXT    O N N 103 
GLU H      H N N 104 
GLU H2     H N N 105 
GLU HA     H N N 106 
GLU HB2    H N N 107 
GLU HB3    H N N 108 
GLU HG2    H N N 109 
GLU HG3    H N N 110 
GLU HE2    H N N 111 
GLU HXT    H N N 112 
GLY N      N N N 113 
GLY CA     C N N 114 
GLY C      C N N 115 
GLY O      O N N 116 
GLY OXT    O N N 117 
GLY H      H N N 118 
GLY H2     H N N 119 
GLY HA2    H N N 120 
GLY HA3    H N N 121 
GLY HXT    H N N 122 
GOL C1     C N N 123 
GOL O1     O N N 124 
GOL C2     C N N 125 
GOL O2     O N N 126 
GOL C3     C N N 127 
GOL O3     O N N 128 
GOL H11    H N N 129 
GOL H12    H N N 130 
GOL HO1    H N N 131 
GOL H2     H N N 132 
GOL HO2    H N N 133 
GOL H31    H N N 134 
GOL H32    H N N 135 
GOL HO3    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LYS N      N N N 205 
LYS CA     C N S 206 
LYS C      C N N 207 
LYS O      O N N 208 
LYS CB     C N N 209 
LYS CG     C N N 210 
LYS CD     C N N 211 
LYS CE     C N N 212 
LYS NZ     N N N 213 
LYS OXT    O N N 214 
LYS H      H N N 215 
LYS H2     H N N 216 
LYS HA     H N N 217 
LYS HB2    H N N 218 
LYS HB3    H N N 219 
LYS HG2    H N N 220 
LYS HG3    H N N 221 
LYS HD2    H N N 222 
LYS HD3    H N N 223 
LYS HE2    H N N 224 
LYS HE3    H N N 225 
LYS HZ1    H N N 226 
LYS HZ2    H N N 227 
LYS HZ3    H N N 228 
LYS HXT    H N N 229 
MET N      N N N 230 
MET CA     C N S 231 
MET C      C N N 232 
MET O      O N N 233 
MET CB     C N N 234 
MET CG     C N N 235 
MET SD     S N N 236 
MET CE     C N N 237 
MET OXT    O N N 238 
MET H      H N N 239 
MET H2     H N N 240 
MET HA     H N N 241 
MET HB2    H N N 242 
MET HB3    H N N 243 
MET HG2    H N N 244 
MET HG3    H N N 245 
MET HE1    H N N 246 
MET HE2    H N N 247 
MET HE3    H N N 248 
MET HXT    H N N 249 
PHE N      N N N 250 
PHE CA     C N S 251 
PHE C      C N N 252 
PHE O      O N N 253 
PHE CB     C N N 254 
PHE CG     C Y N 255 
PHE CD1    C Y N 256 
PHE CD2    C Y N 257 
PHE CE1    C Y N 258 
PHE CE2    C Y N 259 
PHE CZ     C Y N 260 
PHE OXT    O N N 261 
PHE H      H N N 262 
PHE H2     H N N 263 
PHE HA     H N N 264 
PHE HB2    H N N 265 
PHE HB3    H N N 266 
PHE HD1    H N N 267 
PHE HD2    H N N 268 
PHE HE1    H N N 269 
PHE HE2    H N N 270 
PHE HZ     H N N 271 
PHE HXT    H N N 272 
PO4 P      P N N 273 
PO4 O1     O N N 274 
PO4 O2     O N N 275 
PO4 O3     O N N 276 
PO4 O4     O N N 277 
PRO N      N N N 278 
PRO CA     C N S 279 
PRO C      C N N 280 
PRO O      O N N 281 
PRO CB     C N N 282 
PRO CG     C N N 283 
PRO CD     C N N 284 
PRO OXT    O N N 285 
PRO H      H N N 286 
PRO HA     H N N 287 
PRO HB2    H N N 288 
PRO HB3    H N N 289 
PRO HG2    H N N 290 
PRO HG3    H N N 291 
PRO HD2    H N N 292 
PRO HD3    H N N 293 
PRO HXT    H N N 294 
SER N      N N N 295 
SER CA     C N S 296 
SER C      C N N 297 
SER O      O N N 298 
SER CB     C N N 299 
SER OG     O N N 300 
SER OXT    O N N 301 
SER H      H N N 302 
SER H2     H N N 303 
SER HA     H N N 304 
SER HB2    H N N 305 
SER HB3    H N N 306 
SER HG     H N N 307 
SER HXT    H N N 308 
THR N      N N N 309 
THR CA     C N S 310 
THR C      C N N 311 
THR O      O N N 312 
THR CB     C N R 313 
THR OG1    O N N 314 
THR CG2    C N N 315 
THR OXT    O N N 316 
THR H      H N N 317 
THR H2     H N N 318 
THR HA     H N N 319 
THR HB     H N N 320 
THR HG1    H N N 321 
THR HG21   H N N 322 
THR HG22   H N N 323 
THR HG23   H N N 324 
THR HXT    H N N 325 
TRP N      N N N 326 
TRP CA     C N S 327 
TRP C      C N N 328 
TRP O      O N N 329 
TRP CB     C N N 330 
TRP CG     C Y N 331 
TRP CD1    C Y N 332 
TRP CD2    C Y N 333 
TRP NE1    N Y N 334 
TRP CE2    C Y N 335 
TRP CE3    C Y N 336 
TRP CZ2    C Y N 337 
TRP CZ3    C Y N 338 
TRP CH2    C Y N 339 
TRP OXT    O N N 340 
TRP H      H N N 341 
TRP H2     H N N 342 
TRP HA     H N N 343 
TRP HB2    H N N 344 
TRP HB3    H N N 345 
TRP HD1    H N N 346 
TRP HE1    H N N 347 
TRP HE3    H N N 348 
TRP HZ2    H N N 349 
TRP HZ3    H N N 350 
TRP HH2    H N N 351 
TRP HXT    H N N 352 
TYR N      N N N 353 
TYR CA     C N S 354 
TYR C      C N N 355 
TYR O      O N N 356 
TYR CB     C N N 357 
TYR CG     C Y N 358 
TYR CD1    C Y N 359 
TYR CD2    C Y N 360 
TYR CE1    C Y N 361 
TYR CE2    C Y N 362 
TYR CZ     C Y N 363 
TYR OH     O N N 364 
TYR OXT    O N N 365 
TYR H      H N N 366 
TYR H2     H N N 367 
TYR HA     H N N 368 
TYR HB2    H N N 369 
TYR HB3    H N N 370 
TYR HD1    H N N 371 
TYR HD2    H N N 372 
TYR HE1    H N N 373 
TYR HE2    H N N 374 
TYR HH     H N N 375 
TYR HXT    H N N 376 
UMP N1     N N N 377 
UMP C2     C N N 378 
UMP N3     N N N 379 
UMP C4     C N N 380 
UMP C5     C N N 381 
UMP C6     C N N 382 
UMP O2     O N N 383 
UMP O4     O N N 384 
UMP "C1'"  C N R 385 
UMP "C2'"  C N N 386 
UMP "C3'"  C N S 387 
UMP "C4'"  C N R 388 
UMP "O3'"  O N N 389 
UMP "O4'"  O N N 390 
UMP "C5'"  C N N 391 
UMP "O5'"  O N N 392 
UMP P      P N N 393 
UMP OP1    O N N 394 
UMP OP2    O N N 395 
UMP OP3    O N N 396 
UMP HN3    H N N 397 
UMP H5     H N N 398 
UMP H6     H N N 399 
UMP "H1'"  H N N 400 
UMP "H2'"  H N N 401 
UMP "H2''" H N N 402 
UMP "H3'"  H N N 403 
UMP "H4'"  H N N 404 
UMP "HO3'" H N N 405 
UMP "H5'"  H N N 406 
UMP "H5''" H N N 407 
UMP HOP2   H N N 408 
UMP HOP3   H N N 409 
VAL N      N N N 410 
VAL CA     C N S 411 
VAL C      C N N 412 
VAL O      O N N 413 
VAL CB     C N N 414 
VAL CG1    C N N 415 
VAL CG2    C N N 416 
VAL OXT    O N N 417 
VAL H      H N N 418 
VAL H2     H N N 419 
VAL HA     H N N 420 
VAL HB     H N N 421 
VAL HG11   H N N 422 
VAL HG12   H N N 423 
VAL HG13   H N N 424 
VAL HG21   H N N 425 
VAL HG22   H N N 426 
VAL HG23   H N N 427 
VAL HXT    H N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
GLN N     CA     sing N N 70  
GLN N     H      sing N N 71  
GLN N     H2     sing N N 72  
GLN CA    C      sing N N 73  
GLN CA    CB     sing N N 74  
GLN CA    HA     sing N N 75  
GLN C     O      doub N N 76  
GLN C     OXT    sing N N 77  
GLN CB    CG     sing N N 78  
GLN CB    HB2    sing N N 79  
GLN CB    HB3    sing N N 80  
GLN CG    CD     sing N N 81  
GLN CG    HG2    sing N N 82  
GLN CG    HG3    sing N N 83  
GLN CD    OE1    doub N N 84  
GLN CD    NE2    sing N N 85  
GLN NE2   HE21   sing N N 86  
GLN NE2   HE22   sing N N 87  
GLN OXT   HXT    sing N N 88  
GLU N     CA     sing N N 89  
GLU N     H      sing N N 90  
GLU N     H2     sing N N 91  
GLU CA    C      sing N N 92  
GLU CA    CB     sing N N 93  
GLU CA    HA     sing N N 94  
GLU C     O      doub N N 95  
GLU C     OXT    sing N N 96  
GLU CB    CG     sing N N 97  
GLU CB    HB2    sing N N 98  
GLU CB    HB3    sing N N 99  
GLU CG    CD     sing N N 100 
GLU CG    HG2    sing N N 101 
GLU CG    HG3    sing N N 102 
GLU CD    OE1    doub N N 103 
GLU CD    OE2    sing N N 104 
GLU OE2   HE2    sing N N 105 
GLU OXT   HXT    sing N N 106 
GLY N     CA     sing N N 107 
GLY N     H      sing N N 108 
GLY N     H2     sing N N 109 
GLY CA    C      sing N N 110 
GLY CA    HA2    sing N N 111 
GLY CA    HA3    sing N N 112 
GLY C     O      doub N N 113 
GLY C     OXT    sing N N 114 
GLY OXT   HXT    sing N N 115 
GOL C1    O1     sing N N 116 
GOL C1    C2     sing N N 117 
GOL C1    H11    sing N N 118 
GOL C1    H12    sing N N 119 
GOL O1    HO1    sing N N 120 
GOL C2    O2     sing N N 121 
GOL C2    C3     sing N N 122 
GOL C2    H2     sing N N 123 
GOL O2    HO2    sing N N 124 
GOL C3    O3     sing N N 125 
GOL C3    H31    sing N N 126 
GOL C3    H32    sing N N 127 
GOL O3    HO3    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PO4 P     O1     doub N N 260 
PO4 P     O2     sing N N 261 
PO4 P     O3     sing N N 262 
PO4 P     O4     sing N N 263 
PRO N     CA     sing N N 264 
PRO N     CD     sing N N 265 
PRO N     H      sing N N 266 
PRO CA    C      sing N N 267 
PRO CA    CB     sing N N 268 
PRO CA    HA     sing N N 269 
PRO C     O      doub N N 270 
PRO C     OXT    sing N N 271 
PRO CB    CG     sing N N 272 
PRO CB    HB2    sing N N 273 
PRO CB    HB3    sing N N 274 
PRO CG    CD     sing N N 275 
PRO CG    HG2    sing N N 276 
PRO CG    HG3    sing N N 277 
PRO CD    HD2    sing N N 278 
PRO CD    HD3    sing N N 279 
PRO OXT   HXT    sing N N 280 
SER N     CA     sing N N 281 
SER N     H      sing N N 282 
SER N     H2     sing N N 283 
SER CA    C      sing N N 284 
SER CA    CB     sing N N 285 
SER CA    HA     sing N N 286 
SER C     O      doub N N 287 
SER C     OXT    sing N N 288 
SER CB    OG     sing N N 289 
SER CB    HB2    sing N N 290 
SER CB    HB3    sing N N 291 
SER OG    HG     sing N N 292 
SER OXT   HXT    sing N N 293 
THR N     CA     sing N N 294 
THR N     H      sing N N 295 
THR N     H2     sing N N 296 
THR CA    C      sing N N 297 
THR CA    CB     sing N N 298 
THR CA    HA     sing N N 299 
THR C     O      doub N N 300 
THR C     OXT    sing N N 301 
THR CB    OG1    sing N N 302 
THR CB    CG2    sing N N 303 
THR CB    HB     sing N N 304 
THR OG1   HG1    sing N N 305 
THR CG2   HG21   sing N N 306 
THR CG2   HG22   sing N N 307 
THR CG2   HG23   sing N N 308 
THR OXT   HXT    sing N N 309 
TRP N     CA     sing N N 310 
TRP N     H      sing N N 311 
TRP N     H2     sing N N 312 
TRP CA    C      sing N N 313 
TRP CA    CB     sing N N 314 
TRP CA    HA     sing N N 315 
TRP C     O      doub N N 316 
TRP C     OXT    sing N N 317 
TRP CB    CG     sing N N 318 
TRP CB    HB2    sing N N 319 
TRP CB    HB3    sing N N 320 
TRP CG    CD1    doub Y N 321 
TRP CG    CD2    sing Y N 322 
TRP CD1   NE1    sing Y N 323 
TRP CD1   HD1    sing N N 324 
TRP CD2   CE2    doub Y N 325 
TRP CD2   CE3    sing Y N 326 
TRP NE1   CE2    sing Y N 327 
TRP NE1   HE1    sing N N 328 
TRP CE2   CZ2    sing Y N 329 
TRP CE3   CZ3    doub Y N 330 
TRP CE3   HE3    sing N N 331 
TRP CZ2   CH2    doub Y N 332 
TRP CZ2   HZ2    sing N N 333 
TRP CZ3   CH2    sing Y N 334 
TRP CZ3   HZ3    sing N N 335 
TRP CH2   HH2    sing N N 336 
TRP OXT   HXT    sing N N 337 
TYR N     CA     sing N N 338 
TYR N     H      sing N N 339 
TYR N     H2     sing N N 340 
TYR CA    C      sing N N 341 
TYR CA    CB     sing N N 342 
TYR CA    HA     sing N N 343 
TYR C     O      doub N N 344 
TYR C     OXT    sing N N 345 
TYR CB    CG     sing N N 346 
TYR CB    HB2    sing N N 347 
TYR CB    HB3    sing N N 348 
TYR CG    CD1    doub Y N 349 
TYR CG    CD2    sing Y N 350 
TYR CD1   CE1    sing Y N 351 
TYR CD1   HD1    sing N N 352 
TYR CD2   CE2    doub Y N 353 
TYR CD2   HD2    sing N N 354 
TYR CE1   CZ     doub Y N 355 
TYR CE1   HE1    sing N N 356 
TYR CE2   CZ     sing Y N 357 
TYR CE2   HE2    sing N N 358 
TYR CZ    OH     sing N N 359 
TYR OH    HH     sing N N 360 
TYR OXT   HXT    sing N N 361 
UMP N1    C2     sing N N 362 
UMP N1    C6     sing N N 363 
UMP N1    "C1'"  sing N N 364 
UMP C2    N3     sing N N 365 
UMP C2    O2     doub N N 366 
UMP N3    C4     sing N N 367 
UMP N3    HN3    sing N N 368 
UMP C4    C5     sing N N 369 
UMP C4    O4     doub N N 370 
UMP C5    C6     doub N N 371 
UMP C5    H5     sing N N 372 
UMP C6    H6     sing N N 373 
UMP "C1'" "C2'"  sing N N 374 
UMP "C1'" "O4'"  sing N N 375 
UMP "C1'" "H1'"  sing N N 376 
UMP "C2'" "C3'"  sing N N 377 
UMP "C2'" "H2'"  sing N N 378 
UMP "C2'" "H2''" sing N N 379 
UMP "C3'" "C4'"  sing N N 380 
UMP "C3'" "O3'"  sing N N 381 
UMP "C3'" "H3'"  sing N N 382 
UMP "C4'" "O4'"  sing N N 383 
UMP "C4'" "C5'"  sing N N 384 
UMP "C4'" "H4'"  sing N N 385 
UMP "O3'" "HO3'" sing N N 386 
UMP "C5'" "O5'"  sing N N 387 
UMP "C5'" "H5'"  sing N N 388 
UMP "C5'" "H5''" sing N N 389 
UMP "O5'" P      sing N N 390 
UMP P     OP1    doub N N 391 
UMP P     OP2    sing N N 392 
UMP P     OP3    sing N N 393 
UMP OP2   HOP2   sing N N 394 
UMP OP3   HOP3   sing N N 395 
VAL N     CA     sing N N 396 
VAL N     H      sing N N 397 
VAL N     H2     sing N N 398 
VAL CA    C      sing N N 399 
VAL CA    CB     sing N N 400 
VAL CA    HA     sing N N 401 
VAL C     O      doub N N 402 
VAL C     OXT    sing N N 403 
VAL CB    CG1    sing N N 404 
VAL CB    CG2    sing N N 405 
VAL CB    HB     sing N N 406 
VAL CG1   HG11   sing N N 407 
VAL CG1   HG12   sing N N 408 
VAL CG1   HG13   sing N N 409 
VAL CG2   HG21   sing N N 410 
VAL CG2   HG22   sing N N 411 
VAL CG2   HG23   sing N N 412 
VAL OXT   HXT    sing N N 413 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 63' 
_space_group.name_Hall        'P 6c' 
_space_group.IT_number        173 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Y1W 
_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]   0.019006 
_atom_sites.fract_transf_matrix[1][2]   0.010973 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021946 
_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]   0.011426 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . MET A 1 1   ? 0.71500   28.67300 25.99100  1.000 34.43431 ? 1   MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? 2.15000   28.81800 25.82600  1.000 31.87957 ? 1   MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? 2.63600   27.71600 24.88900  1.000 26.78940 ? 1   MET A C     1 
ATOM   4    O O     . MET A 1 1   ? 1.98600   26.67900 24.72800  1.000 28.61933 ? 1   MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? 2.82200   28.68600 27.17700  1.000 36.89677 ? 1   MET A CB    1 
ATOM   6    C CG    . MET A 1 1   ? 2.58800   29.92700 28.09200  1.000 41.02561 ? 1   MET A CG    1 
ATOM   7    S SD    . MET A 1 1   ? 3.67800   30.02900 29.48500  1.000 45.66232 ? 1   MET A SD    1 
ATOM   8    C CE    . MET A 1 1   ? 3.15300   28.60600 30.43300  1.000 46.22456 ? 1   MET A CE    1 
ATOM   9    N N     . MET A 1 2   ? 3.75700   27.95300 24.24100  1.000 21.02940 ? 2   MET A N     1 
ATOM   10   C CA    A MET A 1 2   ? 4.36300   26.99800 23.32800  0.510 18.95238 ? 2   MET A CA    1 
ATOM   11   C CA    B MET A 1 2   ? 4.32600   26.97500 23.33200  0.490 21.45415 ? 2   MET A CA    1 
ATOM   12   C C     . MET A 1 2   ? 5.34400   26.07500 24.04900  1.000 19.78230 ? 2   MET A C     1 
ATOM   13   O O     . MET A 1 2   ? 6.09600   26.50500 24.93800  1.000 21.29519 ? 2   MET A O     1 
ATOM   14   C CB    A MET A 1 2   ? 5.11200   27.76700 22.24900  0.510 18.59935 ? 2   MET A CB    1 
ATOM   15   C CB    B MET A 1 2   ? 4.89800   27.65600 22.07400  0.490 25.62299 ? 2   MET A CB    1 
ATOM   16   C CG    A MET A 1 2   ? 5.65100   26.89600 21.14700  0.510 18.41035 ? 2   MET A CG    1 
ATOM   17   C CG    B MET A 1 2   ? 3.82600   28.13800 20.97400  0.490 29.69132 ? 2   MET A CG    1 
ATOM   18   S SD    A MET A 1 2   ? 6.00800   27.96400 19.76600  0.510 19.66734 ? 2   MET A SD    1 
ATOM   19   S SD    B MET A 1 2   ? 4.49600   28.17200 19.30300  0.490 34.07821 ? 2   MET A SD    1 
ATOM   20   C CE    A MET A 1 2   ? 4.38100   28.28300 19.08800  0.510 23.07340 ? 2   MET A CE    1 
ATOM   21   C CE    B MET A 1 2   ? 6.20800   27.90100 19.70200  0.490 33.62984 ? 2   MET A CE    1 
ATOM   22   N N     . LEU A 1 3   ? 5.36900   24.80200 23.64200  1.000 19.32338 ? 3   LEU A N     1 
ATOM   23   C CA    . LEU A 1 3   ? 6.28600   23.85900 24.31000  1.000 19.89330 ? 3   LEU A CA    1 
ATOM   24   C C     . LEU A 1 3   ? 7.70200   24.08200 23.80100  1.000 19.40280 ? 3   LEU A C     1 
ATOM   25   O O     . LEU A 1 3   ? 7.92500   24.10200 22.59000  1.000 20.11882 ? 3   LEU A O     1 
ATOM   26   C CB    . LEU A 1 3   ? 5.86200   22.43000 23.93200  1.000 20.42304 ? 3   LEU A CB    1 
ATOM   27   C CG    . LEU A 1 3   ? 4.74400   21.83600 24.79500  1.000 22.17862 ? 3   LEU A CG    1 
ATOM   28   C CD1   . LEU A 1 3   ? 3.41900   22.60300 24.65600  1.000 22.29486 ? 3   LEU A CD1   1 
ATOM   29   C CD2   . LEU A 1 3   ? 4.52100   20.33800 24.46800  1.000 22.36770 ? 3   LEU A CD2   1 
ATOM   30   N N     . PRO A 1 4   ? 8.69300   24.17600 24.67900  1.000 21.24128 ? 4   PRO A N     1 
ATOM   31   C CA    . PRO A 1 4   ? 10.08000  24.18500 24.21800  1.000 20.48734 ? 4   PRO A CA    1 
ATOM   32   C C     . PRO A 1 4   ? 10.52600  22.78000 23.82000  1.000 19.96523 ? 4   PRO A C     1 
ATOM   33   O O     . PRO A 1 4   ? 9.91300   21.77100 24.17800  1.000 19.96479 ? 4   PRO A O     1 
ATOM   34   C CB    . PRO A 1 4   ? 10.84900  24.65600 25.45800  1.000 21.20893 ? 4   PRO A CB    1 
ATOM   35   C CG    . PRO A 1 4   ? 10.03900  24.11800 26.60000  1.000 21.48969 ? 4   PRO A CG    1 
ATOM   36   C CD    . PRO A 1 4   ? 8.59000   24.30700 26.15200  1.000 20.87715 ? 4   PRO A CD    1 
ATOM   37   N N     . ASP A 1 5   ? 11.68500  22.73500 23.18200  1.000 20.35780 ? 5   ASP A N     1 
ATOM   38   C CA    . ASP A 1 5   ? 12.29600  21.45700 22.74200  1.000 21.24821 ? 5   ASP A CA    1 
ATOM   39   C C     . ASP A 1 5   ? 12.24500  20.36500 23.80900  1.000 20.35870 ? 5   ASP A C     1 
ATOM   40   O O     . ASP A 1 5   ? 11.84800  19.26200 23.48300  1.000 22.20503 ? 5   ASP A O     1 
ATOM   41   C CB    . ASP A 1 5   ? 13.75300  21.69200 22.34700  1.000 22.05387 ? 5   ASP A CB    1 
ATOM   42   C CG    . ASP A 1 5   ? 14.58600  22.55900 23.28200  1.000 24.38919 ? 5   ASP A CG    1 
ATOM   43   O OD1   . ASP A 1 5   ? 14.12000  22.86700 24.38900  1.000 23.89316 ? 5   ASP A OD1   1 
ATOM   44   O OD2   . ASP A 1 5   ? 15.70700  22.90800 22.89000  1.000 26.53956 ? 5   ASP A OD2   1 
ATOM   45   N N     . TRP A 1 6   ? 12.67100  20.67800 25.04000  1.000 20.64392 ? 6   TRP A N     1 
ATOM   46   C CA    . TRP A 1 6   ? 12.75100  19.60500 26.01700  1.000 21.83828 ? 6   TRP A CA    1 
ATOM   47   C C     . TRP A 1 6   ? 11.37300  19.09700 26.43600  1.000 22.81793 ? 6   TRP A C     1 
ATOM   48   O O     . TRP A 1 6   ? 11.25500  17.96500 26.90900  1.000 24.67946 ? 6   TRP A O     1 
ATOM   49   C CB    . TRP A 1 6   ? 13.55900  20.10900 27.20300  1.000 23.01491 ? 6   TRP A CB    1 
ATOM   50   C CG    . TRP A 1 6   ? 13.01900  21.37500 27.87200  1.000 22.64141 ? 6   TRP A CG    1 
ATOM   51   C CD1   . TRP A 1 6   ? 13.34400  22.66200 27.55000  1.000 22.66685 ? 6   TRP A CD1   1 
ATOM   52   C CD2   . TRP A 1 6   ? 12.07200  21.45100 28.94500  1.000 24.42519 ? 6   TRP A CD2   1 
ATOM   53   N NE1   . TRP A 1 6   ? 12.69800  23.52600 28.40400  1.000 23.48914 ? 6   TRP A NE1   1 
ATOM   54   C CE2   . TRP A 1 6   ? 11.88000  22.81600 29.23400  1.000 24.08406 ? 6   TRP A CE2   1 
ATOM   55   C CE3   . TRP A 1 6   ? 11.36300  20.50200 29.68500  1.000 25.24894 ? 6   TRP A CE3   1 
ATOM   56   C CZ2   . TRP A 1 6   ? 11.01900  23.26300 30.24400  1.000 26.01760 ? 6   TRP A CZ2   1 
ATOM   57   C CZ3   . TRP A 1 6   ? 10.52500  20.94100 30.70600  1.000 26.63139 ? 6   TRP A CZ3   1 
ATOM   58   C CH2   . TRP A 1 6   ? 10.36600  22.31400 30.97600  1.000 28.58607 ? 6   TRP A CH2   1 
ATOM   59   N N     . LYS A 1 7   ? 10.33500  19.91400 26.34700  1.000 21.54813 ? 7   LYS A N     1 
ATOM   60   C CA    . LYS A 1 7   ? 8.99000   19.39900 26.60000  1.000 22.95981 ? 7   LYS A CA    1 
ATOM   61   C C     . LYS A 1 7   ? 8.43600   18.64700 25.40100  1.000 22.94269 ? 7   LYS A C     1 
ATOM   62   O O     . LYS A 1 7   ? 7.70600   17.66000 25.57600  1.000 24.03822 ? 7   LYS A O     1 
ATOM   63   C CB    . LYS A 1 7   ? 8.02400   20.53000 26.95400  1.000 27.18563 ? 7   LYS A CB    1 
ATOM   64   C CG    . LYS A 1 7   ? 7.92500   20.76600 28.42100  1.000 31.62289 ? 7   LYS A CG    1 
ATOM   65   C CD    . LYS A 1 7   ? 6.67700   21.51900 28.76600  1.000 34.04772 ? 7   LYS A CD    1 
ATOM   66   C CE    . LYS A 1 7   ? 6.58000   21.80500 30.25500  1.000 35.80486 ? 7   LYS A CE    1 
ATOM   67   N NZ    . LYS A 1 7   ? 7.32900   20.77900 31.02500  1.000 37.43062 ? 7   LYS A NZ    1 
ATOM   68   N N     . ILE A 1 8   ? 8.74400   19.10200 24.18100  1.000 22.42955 ? 8   ILE A N     1 
ATOM   69   C CA    . ILE A 1 8   ? 8.36700   18.31600 23.01200  1.000 21.88560 ? 8   ILE A CA    1 
ATOM   70   C C     . ILE A 1 8   ? 8.92600   16.90600 23.12000  1.000 23.54044 ? 8   ILE A C     1 
ATOM   71   O O     . ILE A 1 8   ? 8.22400   15.91700 22.88300  1.000 23.91604 ? 8   ILE A O     1 
ATOM   72   C CB    . ILE A 1 8   ? 8.87100   18.99800 21.73600  1.000 20.43630 ? 8   ILE A CB    1 
ATOM   73   C CG1   . ILE A 1 8   ? 8.21600   20.36100 21.56900  1.000 20.38775 ? 8   ILE A CG1   1 
ATOM   74   C CG2   . ILE A 1 8   ? 8.54500   18.08800 20.53100  1.000 21.99196 ? 8   ILE A CG2   1 
ATOM   75   C CD1   . ILE A 1 8   ? 8.86900   21.19100 20.45000  1.000 20.11319 ? 8   ILE A CD1   1 
ATOM   76   N N     . ARG A 1 9   ? 10.21000  16.79700 23.43100  1.000 25.81461 ? 9   ARG A N     1 
ATOM   77   C CA    . ARG A 1 9   ? 10.84300  15.49300 23.54900  1.000 29.10617 ? 9   ARG A CA    1 
ATOM   78   C C     . ARG A 1 9   ? 10.09500  14.59600 24.53100  1.000 32.01016 ? 9   ARG A C     1 
ATOM   79   O O     . ARG A 1 9   ? 9.94400   13.39500 24.28900  1.000 33.14943 ? 9   ARG A O     1 
ATOM   80   C CB    . ARG A 1 9   ? 12.28600  15.70600 24.02300  1.000 29.87511 ? 9   ARG A CB    1 
ATOM   81   C CG    . ARG A 1 9   ? 13.18600  14.50700 23.87300  1.000 31.89910 ? 9   ARG A CG    1 
ATOM   82   C CD    . ARG A 1 9   ? 14.53400  14.77800 24.50700  1.000 32.14631 ? 9   ARG A CD    1 
ATOM   83   N NE    . ARG A 1 9   ? 15.40300  15.60300 23.66500  1.000 32.66109 ? 9   ARG A NE    1 
ATOM   84   C CZ    . ARG A 1 9   ? 16.14200  15.11000 22.67900  1.000 33.38378 ? 9   ARG A CZ    1 
ATOM   85   N NH1   . ARG A 1 9   ? 16.02700  13.84800 22.30400  1.000 33.65053 ? 9   ARG A NH1   1 
ATOM   86   N NH2   . ARG A 1 9   ? 17.00300  15.90100 22.04900  1.000 33.22373 ? 9   ARG A NH2   1 
ATOM   87   N N     . LYS A 1 10  ? 9.60800   15.16500 25.63800  1.000 32.86224 ? 10  LYS A N     1 
ATOM   88   C CA    . LYS A 1 10  ? 8.93000   14.38500 26.67500  1.000 34.61163 ? 10  LYS A CA    1 
ATOM   89   C C     . LYS A 1 10  ? 7.48800   14.03500 26.30900  1.000 34.72504 ? 10  LYS A C     1 
ATOM   90   O O     . LYS A 1 10  ? 7.05500   12.90200 26.54300  1.000 35.24811 ? 10  LYS A O     1 
ATOM   91   C CB    . LYS A 1 10  ? 8.91900   15.15000 27.99600  1.000 37.87596 ? 10  LYS A CB    1 
ATOM   92   C CG    . LYS A 1 10  ? 8.86900   14.25800 29.19400  1.000 40.43597 ? 10  LYS A CG    1 
ATOM   93   C CD    . LYS A 1 10  ? 8.98100   15.00800 30.49400  1.000 42.20690 ? 10  LYS A CD    1 
ATOM   94   C CE    . LYS A 1 10  ? 8.31200   16.37100 30.42600  1.000 43.05568 ? 10  LYS A CE    1 
ATOM   95   N N     . GLU A 1 11  ? 6.71800   14.99300 25.78500  1.000 33.67500 ? 11  GLU A N     1 
ATOM   96   C CA    . GLU A 1 11  ? 5.26000   14.90400 25.72000  1.000 33.34020 ? 11  GLU A CA    1 
ATOM   97   C C     . GLU A 1 11  ? 4.68900   14.49500 24.37200  1.000 31.39731 ? 11  GLU A C     1 
ATOM   98   O O     . GLU A 1 11  ? 3.53000   14.06100 24.31500  1.000 31.89003 ? 11  GLU A O     1 
ATOM   99   C CB    . GLU A 1 11  ? 4.64500   16.25900 26.05500  1.000 35.83046 ? 11  GLU A CB    1 
ATOM   100  C CG    . GLU A 1 11  ? 4.80200   16.66100 27.47600  1.000 37.78910 ? 11  GLU A CG    1 
ATOM   101  C CD    . GLU A 1 11  ? 3.84400   17.77900 27.82200  1.000 39.65430 ? 11  GLU A CD    1 
ATOM   102  O OE1   . GLU A 1 11  ? 2.69800   17.76900 27.30700  1.000 41.66566 ? 11  GLU A OE1   1 
ATOM   103  O OE2   . GLU A 1 11  ? 4.23700   18.67000 28.59200  1.000 40.64477 ? 11  GLU A OE2   1 
ATOM   104  N N     . ILE A 1 12  ? 5.39200   14.71400 23.26800  1.000 28.35454 ? 12  ILE A N     1 
ATOM   105  C CA    . ILE A 1 12  ? 4.83900   14.42900 21.95700  1.000 27.69005 ? 12  ILE A CA    1 
ATOM   106  C C     . ILE A 1 12  ? 5.50100   13.17800 21.43000  1.000 26.65147 ? 12  ILE A C     1 
ATOM   107  O O     . ILE A 1 12  ? 6.72700   13.11600 21.32500  1.000 27.89521 ? 12  ILE A O     1 
ATOM   108  C CB    . ILE A 1 12  ? 5.02700   15.60000 20.97900  1.000 26.57125 ? 12  ILE A CB    1 
ATOM   109  C CG1   . ILE A 1 12  ? 4.77600   16.93800 21.70200  1.000 26.97948 ? 12  ILE A CG1   1 
ATOM   110  C CG2   . ILE A 1 12  ? 4.16900   15.33600 19.71600  1.000 26.75535 ? 12  ILE A CG2   1 
ATOM   111  C CD1   . ILE A 1 12  ? 3.30500   17.18200 22.04300  1.000 27.31145 ? 12  ILE A CD1   1 
ATOM   112  N N     . LEU A 1 13  ? 4.69600   12.18900 21.06900  1.000 26.84684 ? 13  LEU A N     1 
ATOM   113  C CA    . LEU A 1 13  ? 5.23100   11.04200 20.37400  1.000 26.01921 ? 13  LEU A CA    1 
ATOM   114  C C     . LEU A 1 13  ? 5.51400   11.45800 18.93700  1.000 25.58500 ? 13  LEU A C     1 
ATOM   115  O O     . LEU A 1 13  ? 4.60600   11.91300 18.24300  1.000 25.81363 ? 13  LEU A O     1 
ATOM   116  C CB    . LEU A 1 13  ? 4.22800   9.90300  20.48200  1.000 29.45008 ? 13  LEU A CB    1 
ATOM   117  C CG    . LEU A 1 13  ? 4.66900   8.58400  19.89200  1.000 30.68322 ? 13  LEU A CG    1 
ATOM   118  C CD1   . LEU A 1 13  ? 3.75200   7.49400  20.40700  1.000 31.05676 ? 13  LEU A CD1   1 
ATOM   119  C CD2   . LEU A 1 13  ? 4.54300   8.59500  18.37200  1.000 31.93306 ? 13  LEU A CD2   1 
ATOM   120  N N     . ILE A 1 14  ? 6.77000   11.33300 18.51000  1.000 25.78569 ? 14  ILE A N     1 
ATOM   121  C CA    . ILE A 1 14  ? 7.23900   11.71800 17.18000  1.000 25.73626 ? 14  ILE A CA    1 
ATOM   122  C C     . ILE A 1 14  ? 8.15800   10.59000 16.75100  1.000 26.56575 ? 14  ILE A C     1 
ATOM   123  O O     . ILE A 1 14  ? 9.25800   10.44700 17.29600  1.000 28.50089 ? 14  ILE A O     1 
ATOM   124  C CB    . ILE A 1 14  ? 7.98500   13.07300 17.15200  1.000 26.05994 ? 14  ILE A CB    1 
ATOM   125  C CG1   . ILE A 1 14  ? 7.09400   14.16700 17.71300  1.000 25.81447 ? 14  ILE A CG1   1 
ATOM   126  C CG2   . ILE A 1 14  ? 8.44500   13.40100 15.72300  1.000 26.15448 ? 14  ILE A CG2   1 
ATOM   127  C CD1   . ILE A 1 14  ? 7.79100   15.54600 17.82500  1.000 26.97675 ? 14  ILE A CD1   1 
ATOM   128  N N     . GLU A 1 15  ? 7.69700   9.75200  15.82300  1.000 24.77714 ? 15  GLU A N     1 
ATOM   129  C CA    . GLU A 1 15  ? 8.43200   8.52000  15.46100  1.000 27.02289 ? 15  GLU A CA    1 
ATOM   130  C C     . GLU A 1 15  ? 8.42900   8.28200  13.96100  1.000 25.35043 ? 15  GLU A C     1 
ATOM   131  O O     . GLU A 1 15  ? 7.35300   8.33700  13.33600  1.000 24.67152 ? 15  GLU A O     1 
ATOM   132  C CB    . GLU A 1 15  ? 7.81700   7.29700  16.15100  1.000 31.76463 ? 15  GLU A CB    1 
ATOM   133  C CG    . GLU A 1 15  ? 7.86400   7.34500  17.65100  1.000 37.12606 ? 15  GLU A CG    1 
ATOM   134  C CD    . GLU A 1 15  ? 7.33800   6.06100  18.27300  1.000 42.11494 ? 15  GLU A CD    1 
ATOM   135  O OE1   . GLU A 1 15  ? 6.81100   5.20300  17.52300  1.000 44.21658 ? 15  GLU A OE1   1 
ATOM   136  O OE2   . GLU A 1 15  ? 7.40500   5.94000  19.51300  1.000 44.29410 ? 15  GLU A OE2   1 
ATOM   137  N N     . PRO A 1 16  ? 9.58300   8.05000  13.34700  1.000 25.41752 ? 16  PRO A N     1 
ATOM   138  C CA    . PRO A 1 16  ? 10.92100  7.96700  13.97900  1.000 25.10812 ? 16  PRO A CA    1 
ATOM   139  C C     . PRO A 1 16  ? 11.47800  9.34500  14.35300  1.000 24.16795 ? 16  PRO A C     1 
ATOM   140  O O     . PRO A 1 16  ? 11.37100  10.28000 13.58100  1.000 25.36905 ? 16  PRO A O     1 
ATOM   141  C CB    . PRO A 1 16  ? 11.76500  7.26800  12.89700  1.000 25.85261 ? 16  PRO A CB    1 
ATOM   142  C CG    . PRO A 1 16  ? 11.13100  7.71100  11.60000  1.000 26.10082 ? 16  PRO A CG    1 
ATOM   143  C CD    . PRO A 1 16  ? 9.63900   7.77100  11.89700  1.000 25.39035 ? 16  PRO A CD    1 
ATOM   144  N N     . PHE A 1 17  ? 12.07400  9.46500  15.54100  1.000 24.96755 ? 17  PHE A N     1 
ATOM   145  C CA    . PHE A 1 17  ? 12.54000  10.74600 16.06300  1.000 25.03059 ? 17  PHE A CA    1 
ATOM   146  C C     . PHE A 1 17  ? 13.93800  11.01500 15.53400  1.000 24.40499 ? 17  PHE A C     1 
ATOM   147  O O     . PHE A 1 17  ? 14.83200  10.16300 15.64900  1.000 26.48302 ? 17  PHE A O     1 
ATOM   148  C CB    . PHE A 1 17  ? 12.54100  10.71900 17.59200  1.000 25.80581 ? 17  PHE A CB    1 
ATOM   149  C CG    . PHE A 1 17  ? 12.90000  12.00800 18.22100  1.000 28.07574 ? 17  PHE A CG    1 
ATOM   150  C CD1   . PHE A 1 17  ? 11.93400  12.94800 18.49000  1.000 27.90722 ? 17  PHE A CD1   1 
ATOM   151  C CD2   . PHE A 1 17  ? 14.21300  12.28700 18.54000  1.000 29.51073 ? 17  PHE A CD2   1 
ATOM   152  C CE1   . PHE A 1 17  ? 12.25100  14.15300 19.07200  1.000 29.63878 ? 17  PHE A CE1   1 
ATOM   153  C CE2   . PHE A 1 17  ? 14.53100  13.49300 19.09600  1.000 31.11452 ? 17  PHE A CE2   1 
ATOM   154  C CZ    . PHE A 1 17  ? 13.55100  14.41600 19.36100  1.000 30.01523 ? 17  PHE A CZ    1 
ATOM   155  N N     . ASN A 1 18  ? 14.12500  12.20200 14.97400  1.000 23.24307 ? 18  ASN A N     1 
ATOM   156  C CA    . ASN A 1 18  ? 15.38800  12.62400 14.38600  1.000 23.02167 ? 18  ASN A CA    1 
ATOM   157  C C     . ASN A 1 18  ? 15.96000  13.72600 15.26200  1.000 23.52628 ? 18  ASN A C     1 
ATOM   158  O O     . ASN A 1 18  ? 15.36700  14.80100 15.36600  1.000 22.39291 ? 18  ASN A O     1 
ATOM   159  C CB    . ASN A 1 18  ? 15.08100  13.15100 12.97800  1.000 23.52872 ? 18  ASN A CB    1 
ATOM   160  C CG    . ASN A 1 18  ? 16.31300  13.50200 12.20000  1.000 25.21305 ? 18  ASN A CG    1 
ATOM   161  O OD1   . ASN A 1 18  ? 17.24600  12.70900 12.12100  1.000 26.52683 ? 18  ASN A OD1   1 
ATOM   162  N ND2   . ASN A 1 18  ? 16.30800  14.68500 11.56600  1.000 25.45931 ? 18  ASN A ND2   1 
ATOM   163  N N     . GLU A 1 19  ? 17.12600  13.48100 15.86100  1.000 25.15696 ? 19  GLU A N     1 
ATOM   164  C CA    . GLU A 1 19  ? 17.70900  14.46600 16.76900  1.000 24.27774 ? 19  GLU A CA    1 
ATOM   165  C C     . GLU A 1 19  ? 17.89200  15.82600 16.10200  1.000 24.00538 ? 19  GLU A C     1 
ATOM   166  O O     . GLU A 1 19  ? 17.55800  16.86900 16.69600  1.000 24.37494 ? 19  GLU A O     1 
ATOM   167  C CB    . GLU A 1 19  ? 19.05600  13.95600 17.25000  1.000 26.47631 ? 19  GLU A CB    1 
ATOM   168  C CG    . GLU A 1 19  ? 18.92100  12.88900 18.32400  1.000 32.46390 ? 19  GLU A CG    1 
ATOM   169  C CD    . GLU A 1 19  ? 18.35200  13.44400 19.61700  1.000 36.10657 ? 19  GLU A CD    1 
ATOM   170  O OE1   . GLU A 1 19  ? 18.52600  14.65400 19.85700  1.000 37.28610 ? 19  GLU A OE1   1 
ATOM   171  O OE2   . GLU A 1 19  ? 17.75700  12.66700 20.39200  1.000 38.61212 ? 19  GLU A OE2   1 
ATOM   172  N N     . LYS A 1 20  ? 18.39900  15.84000 14.86400  1.000 23.08822 ? 20  LYS A N     1 
ATOM   173  C CA    . LYS A 1 20  ? 18.65700  17.08800 14.16400  1.000 23.34446 ? 20  LYS A CA    1 
ATOM   174  C C     . LYS A 1 20  ? 17.36900  17.85800 13.87500  1.000 21.90723 ? 20  LYS A C     1 
ATOM   175  O O     . LYS A 1 20  ? 17.41400  19.06700 13.60300  1.000 23.64246 ? 20  LYS A O     1 
ATOM   176  C CB    . LYS A 1 20  ? 19.38500  16.81000 12.85700  1.000 25.54209 ? 20  LYS A CB    1 
ATOM   177  N N     . SER A 1 21  ? 16.22600  17.20000 13.90800  1.000 20.39974 ? 21  SER A N     1 
ATOM   178  C CA    . SER A 1 21  ? 14.96100  17.89300 13.67000  1.000 19.93967 ? 21  SER A CA    1 
ATOM   179  C C     . SER A 1 21  ? 14.46600  18.70600 14.86300  1.000 19.42535 ? 21  SER A C     1 
ATOM   180  O O     . SER A 1 21  ? 13.54500  19.52200 14.71400  1.000 19.73258 ? 21  SER A O     1 
ATOM   181  C CB    . SER A 1 21  ? 13.89800  16.85100 13.27200  1.000 19.16992 ? 21  SER A CB    1 
ATOM   182  O OG    . SER A 1 21  ? 14.04300  16.40700 11.92200  1.000 19.54694 ? 21  SER A OG    1 
ATOM   183  N N     . LEU A 1 22  ? 14.96900  18.46200 16.07300  1.000 19.67244 ? 22  LEU A N     1 
ATOM   184  C CA    . LEU A 1 22  ? 14.42200  19.19100 17.20600  1.000 20.38459 ? 22  LEU A CA    1 
ATOM   185  C C     . LEU A 1 22  ? 14.96500  20.61400 17.19000  1.000 22.10640 ? 22  LEU A C     1 
ATOM   186  O O     . LEU A 1 22  ? 16.17900  20.81500 17.09500  1.000 24.87705 ? 22  LEU A O     1 
ATOM   187  C CB    . LEU A 1 22  ? 14.78900  18.48600 18.50000  1.000 22.29922 ? 22  LEU A CB    1 
ATOM   188  C CG    . LEU A 1 22  ? 14.00800  18.90200 19.75000  1.000 23.84845 ? 22  LEU A CG    1 
ATOM   189  C CD1   . LEU A 1 22  ? 12.51900  18.66500 19.62700  1.000 25.04128 ? 22  LEU A CD1   1 
ATOM   190  C CD2   . LEU A 1 22  ? 14.58700  18.17200 21.00200  1.000 23.37932 ? 22  LEU A CD2   1 
ATOM   191  N N     . GLN A 1 23  ? 14.05700  21.58100 17.20600  1.000 21.20848 ? 23  GLN A N     1 
ATOM   192  C CA    . GLN A 1 23  ? 14.36600  22.99000 17.17800  1.000 21.70734 ? 23  GLN A CA    1 
ATOM   193  C C     . GLN A 1 23  ? 14.01600  23.58200 18.52400  1.000 21.85835 ? 23  GLN A C     1 
ATOM   194  O O     . GLN A 1 23  ? 13.39300  22.91600 19.36300  1.000 22.06013 ? 23  GLN A O     1 
ATOM   195  C CB    . GLN A 1 23  ? 13.55800  23.63600 16.04800  1.000 21.90429 ? 23  GLN A CB    1 
ATOM   196  C CG    . GLN A 1 23  ? 13.93300  23.09500 14.62500  1.000 23.51556 ? 23  GLN A CG    1 
ATOM   197  C CD    . GLN A 1 23  ? 15.37500  23.41500 14.21200  1.000 27.38577 ? 23  GLN A CD    1 
ATOM   198  O OE1   . GLN A 1 23  ? 16.05400  24.22000 14.84600  1.000 29.97879 ? 23  GLN A OE1   1 
ATOM   199  N NE2   . GLN A 1 23  ? 15.83800  22.78700 13.14000  1.000 30.55860 ? 23  GLN A NE2   1 
ATOM   200  N N     . PRO A 1 24  ? 14.37200  24.84300 18.76900  1.000 23.11620 ? 24  PRO A N     1 
ATOM   201  C CA    . PRO A 1 24  ? 14.14800  25.41800 20.11100  1.000 22.68093 ? 24  PRO A CA    1 
ATOM   202  C C     . PRO A 1 24  ? 12.71000  25.31900 20.60000  1.000 21.90920 ? 24  PRO A C     1 
ATOM   203  O O     . PRO A 1 24  ? 12.47600  25.11600 21.81300  1.000 22.58198 ? 24  PRO A O     1 
ATOM   204  C CB    . PRO A 1 24  ? 14.55800  26.88700 19.89600  1.000 24.54348 ? 24  PRO A CB    1 
ATOM   205  C CG    . PRO A 1 24  ? 15.60800  26.81800 18.84700  1.000 25.05602 ? 24  PRO A CG    1 
ATOM   206  C CD    . PRO A 1 24  ? 15.14000  25.77300 17.90800  1.000 24.59057 ? 24  PRO A CD    1 
ATOM   207  N N     . ALA A 1 25  ? 11.75300  25.49200 19.68300  1.000 19.73329 ? 25  ALA A N     1 
ATOM   208  C CA    . ALA A 1 25  ? 10.35100  25.41000 20.02900  1.000 20.29384 ? 25  ALA A CA    1 
ATOM   209  C C     . ALA A 1 25  ? 9.56600   24.68500 18.93500  1.000 18.41451 ? 25  ALA A C     1 
ATOM   210  O O     . ALA A 1 25  ? 8.43700   25.05300 18.60000  1.000 17.70478 ? 25  ALA A O     1 
ATOM   211  C CB    . ALA A 1 25  ? 9.74600   26.77800 20.27400  1.000 22.16770 ? 25  ALA A CB    1 
ATOM   212  N N     . GLY A 1 26  ? 10.11300  23.60600 18.39800  1.000 17.32952 ? 26  GLY A N     1 
ATOM   213  C CA    . GLY A 1 26  ? 9.37400   22.86800 17.39200  1.000 17.71410 ? 26  GLY A CA    1 
ATOM   214  C C     . GLY A 1 26  ? 10.16600  21.68000 16.90100  1.000 18.65026 ? 26  GLY A C     1 
ATOM   215  O O     . GLY A 1 26  ? 11.26100  21.39600 17.41100  1.000 20.16348 ? 26  GLY A O     1 
ATOM   216  N N     . TYR A 1 27  ? 9.62200   20.99500 15.89200  1.000 16.34714 ? 27  TYR A N     1 
ATOM   217  C CA    . TYR A 1 27  ? 10.24400  19.79000 15.34200  1.000 16.83746 ? 27  TYR A CA    1 
ATOM   218  C C     . TYR A 1 27  ? 10.14600  19.85200 13.83200  1.000 15.75608 ? 27  TYR A C     1 
ATOM   219  O O     . TYR A 1 27  ? 9.04800   20.06900 13.31300  1.000 15.51101 ? 27  TYR A O     1 
ATOM   220  C CB    . TYR A 1 27  ? 9.56600   18.52200 15.90600  1.000 17.68125 ? 27  TYR A CB    1 
ATOM   221  C CG    . TYR A 1 27  ? 10.18900  17.27200 15.37400  1.000 16.67620 ? 27  TYR A CG    1 
ATOM   222  C CD1   . TYR A 1 27  ? 9.78600   16.72600 14.16700  1.000 18.30621 ? 27  TYR A CD1   1 
ATOM   223  C CD2   . TYR A 1 27  ? 11.16200  16.59100 16.11000  1.000 18.38158 ? 27  TYR A CD2   1 
ATOM   224  C CE1   . TYR A 1 27  ? 10.36000  15.56500 13.65400  1.000 18.73371 ? 27  TYR A CE1   1 
ATOM   225  C CE2   . TYR A 1 27  ? 11.75800  15.41500 15.61300  1.000 18.82572 ? 27  TYR A CE2   1 
ATOM   226  C CZ    . TYR A 1 27  ? 11.31800  14.92800 14.36800  1.000 18.91192 ? 27  TYR A CZ    1 
ATOM   227  O OH    . TYR A 1 27  ? 11.87100  13.75400 13.88300  1.000 20.70909 ? 27  TYR A OH    1 
ATOM   228  N N     . ASP A 1 28  ? 11.25700  19.62500 13.12900  1.000 15.63943 ? 28  ASP A N     1 
ATOM   229  C CA    . ASP A 1 28  ? 11.28500  19.60700 11.65300  1.000 15.61158 ? 28  ASP A CA    1 
ATOM   230  C C     . ASP A 1 28  ? 10.83600  18.23400 11.12300  1.000 15.05873 ? 28  ASP A C     1 
ATOM   231  O O     . ASP A 1 28  ? 11.60800  17.25800 11.07000  1.000 16.53132 ? 28  ASP A O     1 
ATOM   232  C CB    . ASP A 1 28  ? 12.68300  19.89600 11.12300  1.000 17.55175 ? 28  ASP A CB    1 
ATOM   233  C CG    . ASP A 1 28  ? 13.15600  21.29700 11.32000  1.000 19.97356 ? 28  ASP A CG    1 
ATOM   234  O OD1   . ASP A 1 28  ? 12.32400  22.18100 11.60200  1.000 19.02906 ? 28  ASP A OD1   1 
ATOM   235  O OD2   . ASP A 1 28  ? 14.40500  21.48200 11.19500  1.000 22.61879 ? 28  ASP A OD2   1 
ATOM   236  N N     . LEU A 1 29  ? 9.56400   18.16000 10.75700  1.000 14.19568 ? 29  LEU A N     1 
ATOM   237  C CA    . LEU A 1 29  ? 9.01300   17.00000 10.06100  1.000 14.34054 ? 29  LEU A CA    1 
ATOM   238  C C     . LEU A 1 29  ? 9.76700   16.79800 8.76000   1.000 15.04491 ? 29  LEU A C     1 
ATOM   239  O O     . LEU A 1 29  ? 10.24500  17.75100 8.11900   1.000 15.16042 ? 29  LEU A O     1 
ATOM   240  C CB    . LEU A 1 29  ? 7.52400   17.20600 9.78000   1.000 16.34900 ? 29  LEU A CB    1 
ATOM   241  C CG    . LEU A 1 29  ? 6.65800   17.39900 11.02600  1.000 16.33232 ? 29  LEU A CG    1 
ATOM   242  C CD1   . LEU A 1 29  ? 5.27400   17.92000 10.62200  1.000 17.23777 ? 29  LEU A CD1   1 
ATOM   243  C CD2   . LEU A 1 29  ? 6.48000   16.07000 11.73600  1.000 18.76137 ? 29  LEU A CD2   1 
ATOM   244  N N     . ARG A 1 30  ? 9.94200   15.53400 8.37700   1.000 15.57007 ? 30  ARG A N     1 
ATOM   245  C CA    . ARG A 1 30  ? 10.71800  15.17100 7.20800   1.000 16.23200 ? 30  ARG A CA    1 
ATOM   246  C C     . ARG A 1 30  ? 9.81700   14.63500 6.09600   1.000 14.55186 ? 30  ARG A C     1 
ATOM   247  O O     . ARG A 1 30  ? 8.72200   14.07400 6.34400   1.000 15.46166 ? 30  ARG A O     1 
ATOM   248  C CB    . ARG A 1 30  ? 11.80900  14.14600 7.56300   1.000 17.21419 ? 30  ARG A CB    1 
ATOM   249  C CG    . ARG A 1 30  ? 12.92000  14.76700 8.46800   1.000 19.01887 ? 30  ARG A CG    1 
ATOM   250  C CD    . ARG A 1 30  ? 13.85100  13.66700 8.95800   1.000 19.82108 ? 30  ARG A CD    1 
ATOM   251  N NE    . ARG A 1 30  ? 13.20800  12.74200 9.91200   1.000 21.35698 ? 30  ARG A NE    1 
ATOM   252  C CZ    . ARG A 1 30  ? 13.69900  11.56700 10.26700  1.000 23.34684 ? 30  ARG A CZ    1 
ATOM   253  N NH1   . ARG A 1 30  ? 14.84000  11.12900 9.77800   1.000 23.26757 ? 30  ARG A NH1   1 
ATOM   254  N NH2   . ARG A 1 30  ? 13.03400  10.83300 11.14800  1.000 23.45023 ? 30  ARG A NH2   1 
ATOM   255  N N     . VAL A 1 31  ? 10.29900  14.79100 4.86400   1.000 15.27106 ? 31  VAL A N     1 
ATOM   256  C CA    . VAL A 1 31  ? 9.63500   14.17900 3.70500   1.000 15.46749 ? 31  VAL A CA    1 
ATOM   257  C C     . VAL A 1 31  ? 9.58100   12.66200 3.88500   1.000 16.54439 ? 31  VAL A C     1 
ATOM   258  O O     . VAL A 1 31  ? 10.60900  11.99300 4.04100   1.000 16.86353 ? 31  VAL A O     1 
ATOM   259  C CB    . VAL A 1 31  ? 10.36400  14.56300 2.41000   1.000 15.86039 ? 31  VAL A CB    1 
ATOM   260  C CG1   . VAL A 1 31  ? 9.79900   13.82100 1.17400   1.000 16.78931 ? 31  VAL A CG1   1 
ATOM   261  C CG2   . VAL A 1 31  ? 10.34500  16.09000 2.22900   1.000 17.22543 ? 31  VAL A CG2   1 
ATOM   262  N N     . GLY A 1 32  ? 8.38200   12.08100 3.79600   1.000 15.93980 ? 32  GLY A N     1 
ATOM   263  C CA    . GLY A 1 32  ? 8.12100   10.65800 3.99800   1.000 17.13265 ? 32  GLY A CA    1 
ATOM   264  C C     . GLY A 1 32  ? 8.05300   9.85700  2.70400   1.000 17.31290 ? 32  GLY A C     1 
ATOM   265  O O     . GLY A 1 32  ? 8.61600   10.22500 1.64300   1.000 18.01632 ? 32  GLY A O     1 
ATOM   266  N N     . LYS A 1 33  ? 7.30500   8.74800  2.77500   1.000 17.69636 ? 33  LYS A N     1 
ATOM   267  C CA    . LYS A 1 33  ? 7.45300   7.68500  1.79300   1.000 18.60603 ? 33  LYS A CA    1 
ATOM   268  C C     . LYS A 1 33  ? 6.62300   7.86700  0.55500   1.000 18.08225 ? 33  LYS A C     1 
ATOM   269  O O     . LYS A 1 33  ? 6.85600   7.16900  -0.43500  1.000 19.34246 ? 33  LYS A O     1 
ATOM   270  C CB    . LYS A 1 33  ? 7.09400   6.34700  2.44100   1.000 21.58069 ? 33  LYS A CB    1 
ATOM   271  C CG    . LYS A 1 33  ? 8.04100   5.99400  3.57900   1.000 25.05127 ? 33  LYS A CG    1 
ATOM   272  C CD    . LYS A 1 33  ? 7.64300   4.68600  4.20000   1.000 29.77165 ? 33  LYS A CD    1 
ATOM   273  C CE    . LYS A 1 33  ? 8.59900   4.30900  5.31600   1.000 34.10503 ? 33  LYS A CE    1 
ATOM   274  N NZ    . LYS A 1 33  ? 8.29500   2.93200  5.81200   1.000 38.50983 ? 33  LYS A NZ    1 
ATOM   275  N N     . GLU A 1 34  ? 5.65400   8.78100  0.58300   1.000 17.73220 ? 34  GLU A N     1 
ATOM   276  C CA    . GLU A 1 34  ? 4.64300   8.89100  -0.45900  1.000 17.68095 ? 34  GLU A CA    1 
ATOM   277  C C     . GLU A 1 34  ? 4.34700   10.35400 -0.79100  1.000 16.69533 ? 34  GLU A C     1 
ATOM   278  O O     . GLU A 1 34  ? 4.36400   11.22800 0.08400   1.000 17.06503 ? 34  GLU A O     1 
ATOM   279  C CB    . GLU A 1 34  ? 3.32600   8.31400  0.10800   1.000 21.13874 ? 34  GLU A CB    1 
ATOM   280  C CG    . GLU A 1 34  ? 3.35200   6.83200  0.35000   1.000 23.65090 ? 34  GLU A CG    1 
ATOM   281  C CD    . GLU A 1 34  ? 2.12200   6.33500  1.12100   1.000 26.44726 ? 34  GLU A CD    1 
ATOM   282  O OE1   . GLU A 1 34  ? 1.05800   7.00400  1.10400   1.000 26.14597 ? 34  GLU A OE1   1 
ATOM   283  O OE2   . GLU A 1 34  ? 2.19300   5.18700  1.64300   1.000 30.46266 ? 34  GLU A OE2   1 
ATOM   284  N N     . ALA A 1 35  ? 4.07700   10.61400 -2.07500  1.000 17.03087 ? 35  ALA A N     1 
ATOM   285  C CA    . ALA A 1 35  ? 3.61000   11.92300 -2.51600  1.000 16.31905 ? 35  ALA A CA    1 
ATOM   286  C C     . ALA A 1 35  ? 2.56700   11.67900 -3.58300  1.000 16.59685 ? 35  ALA A C     1 
ATOM   287  O O     . ALA A 1 35  ? 2.45700   10.58800 -4.14900  1.000 17.96764 ? 35  ALA A O     1 
ATOM   288  C CB    . ALA A 1 35  ? 4.76900   12.79400 -3.02900  1.000 16.33918 ? 35  ALA A CB    1 
ATOM   289  N N     . TYR A 1 36  ? 1.82300   12.71500 -3.92700  1.000 16.03854 ? 36  TYR A N     1 
ATOM   290  C CA    . TYR A 1 36  ? 0.75700   12.61700 -4.92200  1.000 16.36785 ? 36  TYR A CA    1 
ATOM   291  C C     . TYR A 1 36  ? 0.71800   13.93500 -5.69800  1.000 16.36577 ? 36  TYR A C     1 
ATOM   292  O O     . TYR A 1 36  ? 0.51300   15.00900 -5.09900  1.000 16.44164 ? 36  TYR A O     1 
ATOM   293  C CB    . TYR A 1 36  ? -0.57700  12.33400 -4.21200  1.000 20.18283 ? 36  TYR A CB    1 
ATOM   294  C CG    . TYR A 1 36  ? -1.71600  12.11600 -5.15000  1.000 22.52429 ? 36  TYR A CG    1 
ATOM   295  C CD1   . TYR A 1 36  ? -1.85700  10.90400 -5.82700  1.000 25.90959 ? 36  TYR A CD1   1 
ATOM   296  C CD2   . TYR A 1 36  ? -2.69300  13.11600 -5.34800  1.000 25.18846 ? 36  TYR A CD2   1 
ATOM   297  C CE1   . TYR A 1 36  ? -2.95400  10.69300 -6.69000  1.000 27.83559 ? 36  TYR A CE1   1 
ATOM   298  C CE2   . TYR A 1 36  ? -3.75900  12.90700 -6.21100  1.000 28.10461 ? 36  TYR A CE2   1 
ATOM   299  C CZ    . TYR A 1 36  ? -3.87400  11.71100 -6.87200  1.000 28.43591 ? 36  TYR A CZ    1 
ATOM   300  O OH    . TYR A 1 36  ? -4.94000  11.49600 -7.74800  1.000 31.59608 ? 36  TYR A OH    1 
ATOM   301  N N     . ILE A 1 37  ? 0.95700   13.87600 -7.00600  1.000 16.67395 ? 37  ILE A N     1 
ATOM   302  C CA    . ILE A 1 37  ? 1.07300   15.07500 -7.84200  1.000 17.38105 ? 37  ILE A CA    1 
ATOM   303  C C     . ILE A 1 37  ? 0.39200   14.75900 -9.16100  1.000 19.28396 ? 37  ILE A C     1 
ATOM   304  O O     . ILE A 1 37  ? 0.65200   13.70400 -9.75900  1.000 20.67323 ? 37  ILE A O     1 
ATOM   305  C CB    . ILE A 1 37  ? 2.54100   15.46500 -8.13700  1.000 17.55062 ? 37  ILE A CB    1 
ATOM   306  C CG1   . ILE A 1 37  ? 3.31300   15.58700 -6.83400  1.000 18.12068 ? 37  ILE A CG1   1 
ATOM   307  C CG2   . ILE A 1 37  ? 2.56900   16.67600 -9.05500  1.000 19.83403 ? 37  ILE A CG2   1 
ATOM   308  C CD1   . ILE A 1 37  ? 4.71400   16.05500 -7.05200  1.000 19.15204 ? 37  ILE A CD1   1 
ATOM   309  N N     . ASN A 1 38  ? -0.51600  15.62800 -9.59700  1.000 21.18668 ? 38  ASN A N     1 
ATOM   310  C CA    . ASN A 1 38  ? -1.14700  15.48200 -10.92600 1.000 24.08957 ? 38  ASN A CA    1 
ATOM   311  C C     . ASN A 1 38  ? -1.75100  14.09300 -11.12400 1.000 25.51539 ? 38  ASN A C     1 
ATOM   312  O O     . ASN A 1 38  ? -1.61200  13.49400 -12.18600 1.000 27.36958 ? 38  ASN A O     1 
ATOM   313  C CB    . ASN A 1 38  ? -0.15000  15.82500 -12.04600 1.000 25.64679 ? 38  ASN A CB    1 
ATOM   314  C CG    . ASN A 1 38  ? 0.10000   17.31500 -12.17900 1.000 27.78967 ? 38  ASN A CG    1 
ATOM   315  O OD1   . ASN A 1 38  ? -0.74400  18.12700 -11.77800 1.000 28.50815 ? 38  ASN A OD1   1 
ATOM   316  N ND2   . ASN A 1 38  ? 1.23600   17.68100 -12.73700 1.000 29.34809 ? 38  ASN A ND2   1 
ATOM   317  N N     . GLY A 1 39  ? -2.43400  13.58300 -10.10200 1.000 25.07204 ? 39  GLY A N     1 
ATOM   318  C CA    . GLY A 1 39  ? -3.19200  12.33600 -10.23000 1.000 25.13102 ? 39  GLY A CA    1 
ATOM   319  C C     . GLY A 1 39  ? -2.38100  11.08200 -10.01800 1.000 26.04862 ? 39  GLY A C     1 
ATOM   320  O O     . GLY A 1 39  ? -2.94300  9.97100  -10.15600 1.000 27.96380 ? 39  GLY A O     1 
ATOM   321  N N     . ARG A 1 40  ? -1.08600  11.21100 -9.71400  1.000 26.56163 ? 40  ARG A N     1 
ATOM   322  C CA    . ARG A 1 40  ? -0.16100  10.07900 -9.68300  1.000 27.26331 ? 40  ARG A CA    1 
ATOM   323  C C     . ARG A 1 40  ? 0.51400   9.96800  -8.32300  1.000 24.60732 ? 40  ARG A C     1 
ATOM   324  O O     . ARG A 1 40  ? 1.02200   10.96700 -7.77800  1.000 23.03460 ? 40  ARG A O     1 
ATOM   325  C CB    . ARG A 1 40  ? 0.90000   10.19000 -10.78700 1.000 32.05786 ? 40  ARG A CB    1 
ATOM   326  C CG    . ARG A 1 40  ? 0.36300   10.53500 -12.17700 1.000 38.27332 ? 40  ARG A CG    1 
ATOM   327  C CD    . ARG A 1 40  ? 1.10500   9.83200  -13.30900 1.000 43.34226 ? 40  ARG A CD    1 
ATOM   328  N NE    . ARG A 1 40  ? 1.08700   8.38300  -13.14400 1.000 47.66182 ? 40  ARG A NE    1 
ATOM   329  C CZ    . ARG A 1 40  ? 0.57400   7.53100  -14.02200 1.000 50.57037 ? 40  ARG A CZ    1 
ATOM   330  N NH1   . ARG A 1 40  ? 0.04600   7.94800  -15.16300 1.000 51.72529 ? 40  ARG A NH1   1 
ATOM   331  N NH2   . ARG A 1 40  ? 0.59300   6.22800  -13.75000 1.000 51.73392 ? 40  ARG A NH2   1 
ATOM   332  N N     . LEU A 1 41  ? 0.52800   8.75200  -7.78000  1.000 24.14997 ? 41  LEU A N     1 
ATOM   333  C CA    . LEU A 1 41  ? 1.22300   8.44300  -6.54800  1.000 24.18227 ? 41  LEU A CA    1 
ATOM   334  C C     . LEU A 1 41  ? 2.68900   8.26800  -6.88500  1.000 23.77589 ? 41  LEU A C     1 
ATOM   335  O O     . LEU A 1 41  ? 3.03500   7.65500  -7.91400  1.000 27.11355 ? 41  LEU A O     1 
ATOM   336  C CB    . LEU A 1 41  ? 0.68600   7.12500  -5.97200  1.000 27.33992 ? 41  LEU A CB    1 
ATOM   337  C CG    . LEU A 1 41  ? -0.68600  7.27300  -5.32300  1.000 29.69426 ? 41  LEU A CG    1 
ATOM   338  N N     . ILE A 1 42  ? 3.53800   8.80100  -6.02200  1.000 22.10172 ? 42  ILE A N     1 
ATOM   339  C CA    . ILE A 1 42  ? 4.97900   8.73100  -6.17200  1.000 21.32241 ? 42  ILE A CA    1 
ATOM   340  C C     . ILE A 1 42  ? 5.51900   8.02200  -4.95000  1.000 20.94922 ? 42  ILE A C     1 
ATOM   341  O O     . ILE A 1 42  ? 5.23800   8.42500  -3.80500  1.000 21.89380 ? 42  ILE A O     1 
ATOM   342  C CB    . ILE A 1 42  ? 5.55900   10.15200 -6.29800  1.000 22.91155 ? 42  ILE A CB    1 
ATOM   343  C CG1   . ILE A 1 42  ? 4.99400   10.86000 -7.53300  1.000 24.30308 ? 42  ILE A CG1   1 
ATOM   344  C CG2   . ILE A 1 42  ? 7.09200   10.11700 -6.27000  1.000 23.54826 ? 42  ILE A CG2   1 
ATOM   345  C CD1   . ILE A 1 42  ? 5.06300   12.39600 -7.47100  1.000 25.29524 ? 42  ILE A CD1   1 
ATOM   346  N N     . ASN A 1 43  ? 6.31500   6.97300  -5.19200  1.000 20.06724 ? 43  ASN A N     1 
ATOM   347  C CA    . ASN A 1 43  ? 7.00000   6.29700  -4.09700  1.000 20.68188 ? 43  ASN A CA    1 
ATOM   348  C C     . ASN A 1 43  ? 8.29700   7.05800  -3.80500  1.000 20.34780 ? 43  ASN A C     1 
ATOM   349  O O     . ASN A 1 43  ? 9.33300   6.81100  -4.40400  1.000 21.80237 ? 43  ASN A O     1 
ATOM   350  C CB    . ASN A 1 43  ? 7.26500   4.82700  -4.43200  1.000 21.12588 ? 43  ASN A CB    1 
ATOM   351  C CG    . ASN A 1 43  ? 7.77600   4.09000  -3.24600  1.000 21.61141 ? 43  ASN A CG    1 
ATOM   352  O OD1   . ASN A 1 43  ? 8.41000   4.71100  -2.39900  1.000 23.31692 ? 43  ASN A OD1   1 
ATOM   353  N ND2   . ASN A 1 43  ? 7.57500   2.78600  -3.17800  1.000 24.02633 ? 43  ASN A ND2   1 
ATOM   354  N N     . VAL A 1 44  ? 8.24200   8.00800  -2.86600  1.000 19.41401 ? 44  VAL A N     1 
ATOM   355  C CA    . VAL A 1 44  ? 9.37300   8.88000  -2.56400  1.000 19.29437 ? 44  VAL A CA    1 
ATOM   356  C C     . VAL A 1 44  ? 10.47900  8.07400  -1.90300  1.000 20.51100 ? 44  VAL A C     1 
ATOM   357  O O     . VAL A 1 44  ? 11.67000  8.33600  -2.14000  1.000 20.38797 ? 44  VAL A O     1 
ATOM   358  C CB    . VAL A 1 44  ? 8.90700   10.05600 -1.68200  1.000 18.96081 ? 44  VAL A CB    1 
ATOM   359  C CG1   . VAL A 1 44  ? 10.10300  10.94800 -1.34500  1.000 19.54534 ? 44  VAL A CG1   1 
ATOM   360  C CG2   . VAL A 1 44  ? 7.87400   10.85800 -2.42500  1.000 20.01225 ? 44  VAL A CG2   1 
ATOM   361  N N     . GLU A 1 45  ? 10.12200  7.07900  -1.06600  1.000 21.13036 ? 45  GLU A N     1 
ATOM   362  C CA    . GLU A 1 45  ? 11.13600  6.21900  -0.45600  1.000 22.46633 ? 45  GLU A CA    1 
ATOM   363  C C     . GLU A 1 45  ? 11.98000  5.54000  -1.53300  1.000 22.19409 ? 45  GLU A C     1 
ATOM   364  O O     . GLU A 1 45  ? 13.22000  5.46100  -1.43600  1.000 23.13723 ? 45  GLU A O     1 
ATOM   365  C CB    . GLU A 1 45  ? 10.46000  5.15600  0.42000   1.000 23.71295 ? 45  GLU A CB    1 
ATOM   366  C CG    . GLU A 1 45  ? 11.40900  4.25600  1.16400   1.000 25.91807 ? 45  GLU A CG    1 
ATOM   367  C CD    . GLU A 1 45  ? 10.72100  3.00700  1.64100   1.000 30.77484 ? 45  GLU A CD    1 
ATOM   368  O OE1   . GLU A 1 45  ? 10.54600  2.07800  0.84000   1.000 32.06409 ? 45  GLU A OE1   1 
ATOM   369  O OE2   . GLU A 1 45  ? 10.30300  3.02700  2.81100   1.000 34.48291 ? 45  GLU A OE2   1 
ATOM   370  N N     . LYS A 1 46  ? 11.32400  5.00800  -2.56500  1.000 20.57688 ? 46  LYS A N     1 
ATOM   371  C CA    . LYS A 1 46  ? 12.02600  4.27500  -3.59500  1.000 22.10098 ? 46  LYS A CA    1 
ATOM   372  C C     . LYS A 1 46  ? 12.80200  5.21900  -4.50000  1.000 23.18376 ? 46  LYS A C     1 
ATOM   373  O O     . LYS A 1 46  ? 13.96300  4.96800  -4.82400  1.000 24.20905 ? 46  LYS A O     1 
ATOM   374  C CB    . LYS A 1 46  ? 10.99200  3.45900  -4.38500  1.000 23.83266 ? 46  LYS A CB    1 
ATOM   375  C CG    . LYS A 1 46  ? 11.50400  2.80400  -5.67500  1.000 28.16195 ? 46  LYS A CG    1 
ATOM   376  C CD    . LYS A 1 46  ? 10.39700  1.93100  -6.25500  1.000 31.87882 ? 46  LYS A CD    1 
ATOM   377  C CE    . LYS A 1 46  ? 10.87800  0.91300  -7.22300  1.000 35.05358 ? 46  LYS A CE    1 
ATOM   378  N NZ    . LYS A 1 46  ? 11.61300  1.54900  -8.34200  1.000 36.39705 ? 46  LYS A NZ    1 
ATOM   379  N N     . GLU A 1 47  ? 12.17300  6.31200  -4.93900  1.000 22.93045 ? 47  GLU A N     1 
ATOM   380  C CA    A GLU A 1 47  ? 12.81300  7.23200  -5.88000  0.430 22.99512 ? 47  GLU A CA    1 
ATOM   381  C CA    B GLU A 1 47  ? 12.81300  7.23500  -5.87900  0.570 23.80518 ? 47  GLU A CA    1 
ATOM   382  C C     . GLU A 1 47  ? 13.84700  8.12700  -5.21400  1.000 22.49092 ? 47  GLU A C     1 
ATOM   383  O O     . GLU A 1 47  ? 14.72200  8.65700  -5.90600  1.000 23.01065 ? 47  GLU A O     1 
ATOM   384  C CB    A GLU A 1 47  ? 11.74600  8.04500  -6.63800  0.430 23.70698 ? 47  GLU A CB    1 
ATOM   385  C CB    B GLU A 1 47  ? 11.76500  8.06000  -6.65500  0.570 26.24327 ? 47  GLU A CB    1 
ATOM   386  C CG    A GLU A 1 47  ? 10.64600  7.15000  -7.23600  0.430 25.96851 ? 47  GLU A CG    1 
ATOM   387  C CG    B GLU A 1 47  ? 10.57700  7.21400  -7.12900  0.570 30.28795 ? 47  GLU A CG    1 
ATOM   388  C CD    A GLU A 1 47  ? 9.86500   7.81100  -8.35400  0.430 28.38998 ? 47  GLU A CD    1 
ATOM   389  C CD    B GLU A 1 47  ? 10.79200  6.55600  -8.46700  0.570 33.60704 ? 47  GLU A CD    1 
ATOM   390  O OE1   A GLU A 1 47  ? 10.11600  8.99700  -8.63900  0.430 30.22429 ? 47  GLU A OE1   1 
ATOM   391  O OE1   B GLU A 1 47  ? 11.83200  5.90100  -8.65500  0.570 34.44620 ? 47  GLU A OE1   1 
ATOM   392  O OE2   A GLU A 1 47  ? 8.96900   7.14600  -8.92300  0.430 29.10996 ? 47  GLU A OE2   1 
ATOM   393  O OE2   B GLU A 1 47  ? 9.90100   6.66500  -9.34000  0.570 35.51523 ? 47  GLU A OE2   1 
ATOM   394  N N     . GLY A 1 48  ? 13.77900  8.28300  -3.90300  1.000 21.61501 ? 48  GLY A N     1 
ATOM   395  C CA    . GLY A 1 48  ? 14.70000  9.08000  -3.15800  1.000 20.71450 ? 48  GLY A CA    1 
ATOM   396  C C     . GLY A 1 48  ? 14.36700  10.54500 -3.10900  1.000 19.47573 ? 48  GLY A C     1 
ATOM   397  O O     . GLY A 1 48  ? 15.07200  11.29000 -2.42800  1.000 21.16813 ? 48  GLY A O     1 
ATOM   398  N N     . LYS A 1 49  ? 13.30400  10.99000 -3.77500  1.000 19.33940 ? 49  LYS A N     1 
ATOM   399  C CA    . LYS A 1 49  ? 12.96400  12.40000 -3.80900  1.000 19.49006 ? 49  LYS A CA    1 
ATOM   400  C C     . LYS A 1 49  ? 11.58900  12.52700 -4.43400  1.000 18.93941 ? 49  LYS A C     1 
ATOM   401  O O     . LYS A 1 49  ? 11.04900  11.60000 -5.06200  1.000 19.72276 ? 49  LYS A O     1 
ATOM   402  C CB    . LYS A 1 49  ? 14.00300  13.17500 -4.62800  1.000 21.92165 ? 49  LYS A CB    1 
ATOM   403  C CG    . LYS A 1 49  ? 14.01900  12.77600 -6.06900  1.000 24.90279 ? 49  LYS A CG    1 
ATOM   404  C CD    . LYS A 1 49  ? 15.00000  13.70400 -6.80700  1.000 29.74747 ? 49  LYS A CD    1 
ATOM   405  C CE    . LYS A 1 49  ? 15.57200  13.05400 -8.04500  1.000 33.03263 ? 49  LYS A CE    1 
ATOM   406  N NZ    . LYS A 1 49  ? 16.56600  13.98500 -8.66100  1.000 34.73420 ? 49  LYS A NZ    1 
ATOM   407  N N     . VAL A 1 50  ? 11.02800  13.71200 -4.24100  1.000 20.19220 ? 50  VAL A N     1 
ATOM   408  C CA    . VAL A 1 50  ? 9.83700   14.16300 -4.95800  1.000 19.47542 ? 50  VAL A CA    1 
ATOM   409  C C     . VAL A 1 50  ? 10.19700  15.47500 -5.65800  1.000 18.78311 ? 50  VAL A C     1 
ATOM   410  O O     . VAL A 1 50  ? 10.86100  16.32900 -5.05900  1.000 18.76421 ? 50  VAL A O     1 
ATOM   411  C CB    . VAL A 1 50  ? 8.63000   14.30300 -3.99400  1.000 21.58941 ? 50  VAL A CB    1 
ATOM   412  C CG1   . VAL A 1 50  ? 8.91600   15.18400 -2.78000  1.000 22.30761 ? 50  VAL A CG1   1 
ATOM   413  C CG2   . VAL A 1 50  ? 7.34600   14.77700 -4.73300  1.000 23.14310 ? 50  VAL A CG2   1 
ATOM   414  N N     . VAL A 1 51  ? 9.74300   15.64800 -6.90200  1.000 18.56698 ? 51  VAL A N     1 
ATOM   415  C CA    . VAL A 1 51  ? 9.94300   16.87500 -7.68100  1.000 19.05744 ? 51  VAL A CA    1 
ATOM   416  C C     . VAL A 1 51  ? 8.58200   17.51900 -7.84600  1.000 17.49985 ? 51  VAL A C     1 
ATOM   417  O O     . VAL A 1 51  ? 7.65400   16.91800 -8.41800  1.000 19.31617 ? 51  VAL A O     1 
ATOM   418  C CB    . VAL A 1 51  ? 10.56900  16.57800 -9.05100  1.000 22.86287 ? 51  VAL A CB    1 
ATOM   419  C CG1   . VAL A 1 51  ? 10.85200  17.86700 -9.74700  1.000 23.54796 ? 51  VAL A CG1   1 
ATOM   420  C CG2   . VAL A 1 51  ? 11.87200  15.77100 -8.87400  1.000 26.29585 ? 51  VAL A CG2   1 
ATOM   421  N N     . ILE A 1 52  ? 8.44100   18.72900 -7.33700  1.000 17.06188 ? 52  ILE A N     1 
ATOM   422  C CA    . ILE A 1 52  ? 7.19100   19.47900 -7.47900  1.000 16.65274 ? 52  ILE A CA    1 
ATOM   423  C C     . ILE A 1 52  ? 7.31100   20.32900 -8.74400  1.000 15.39594 ? 52  ILE A C     1 
ATOM   424  O O     . ILE A 1 52  ? 8.19900   21.19000 -8.81200  1.000 17.05575 ? 52  ILE A O     1 
ATOM   425  C CB    . ILE A 1 52  ? 6.85000   20.34600 -6.25700  1.000 16.90475 ? 52  ILE A CB    1 
ATOM   426  C CG1   . ILE A 1 52  ? 6.94500   19.48300 -4.96700  1.000 18.03922 ? 52  ILE A CG1   1 
ATOM   427  C CG2   . ILE A 1 52  ? 5.43800   20.95000 -6.48200  1.000 17.66952 ? 52  ILE A CG2   1 
ATOM   428  C CD1   . ILE A 1 52  ? 6.69700   20.30400 -3.66700  1.000 18.61530 ? 52  ILE A CD1   1 
ATOM   429  N N     . PRO A 1 53  ? 6.51200   20.08900 -9.77300  1.000 17.25557 ? 53  PRO A N     1 
ATOM   430  C CA    . PRO A 1 53  ? 6.66300   20.85000 -11.03200 1.000 18.25718 ? 53  PRO A CA    1 
ATOM   431  C C     . PRO A 1 53  ? 6.35400   22.32700 -10.82700 1.000 18.01218 ? 53  PRO A C     1 
ATOM   432  O O     . PRO A 1 53  ? 5.64100   22.70500 -9.86500  1.000 17.35677 ? 53  PRO A O     1 
ATOM   433  C CB    . PRO A 1 53  ? 5.62300   20.20400 -11.97600 1.000 19.64049 ? 53  PRO A CB    1 
ATOM   434  C CG    . PRO A 1 53  ? 5.40400   18.84200 -11.38200 1.000 20.45416 ? 53  PRO A CG    1 
ATOM   435  C CD    . PRO A 1 53  ? 5.47500   19.04700 -9.87700  1.000 18.55441 ? 53  PRO A CD    1 
ATOM   436  N N     . PRO A 1 54  ? 6.80900   23.19100 -11.74200 1.000 19.46659 ? 54  PRO A N     1 
ATOM   437  C CA    . PRO A 1 54  ? 6.48000   24.62200 -11.64200 1.000 19.45595 ? 54  PRO A CA    1 
ATOM   438  C C     . PRO A 1 54  ? 4.96900   24.83500 -11.56100 1.000 18.26386 ? 54  PRO A C     1 
ATOM   439  O O     . PRO A 1 54  ? 4.19900   24.14500 -12.22800 1.000 18.98341 ? 54  PRO A O     1 
ATOM   440  C CB    . PRO A 1 54  ? 7.04700   25.20600 -12.95000 1.000 21.31415 ? 54  PRO A CB    1 
ATOM   441  C CG    . PRO A 1 54  ? 8.14900   24.27500 -13.33700 1.000 22.76351 ? 54  PRO A CG    1 
ATOM   442  C CD    . PRO A 1 54  ? 7.68200   22.88700 -12.90900 1.000 21.54064 ? 54  PRO A CD    1 
ATOM   443  N N     . LYS A 1 55  ? 4.55200   25.77700 -10.72400 1.000 17.57660 ? 55  LYS A N     1 
ATOM   444  C CA    . LYS A 1 55  ? 3.15500   26.19600 -10.66500 1.000 17.91130 ? 55  LYS A CA    1 
ATOM   445  C C     . LYS A 1 55  ? 2.20400   25.03700 -10.42000 1.000 16.63204 ? 55  LYS A C     1 
ATOM   446  O O     . LYS A 1 55  ? 1.10000   25.03000 -10.95200 1.000 18.38445 ? 55  LYS A O     1 
ATOM   447  C CB    . LYS A 1 55  ? 2.76500   27.01800 -11.90000 1.000 19.55256 ? 55  LYS A CB    1 
ATOM   448  C CG    . LYS A 1 55  ? 3.49900   28.40500 -12.05200 1.000 22.39198 ? 55  LYS A CG    1 
ATOM   449  C CD    . LYS A 1 55  ? 3.20200   29.33900 -10.84300 1.000 23.76258 ? 55  LYS A CD    1 
ATOM   450  C CE    . LYS A 1 55  ? 3.40500   30.82800 -11.11000 1.000 26.56796 ? 55  LYS A CE    1 
ATOM   451  N NZ    . LYS A 1 55  ? 4.86500   31.09800 -11.29300 1.000 28.32845 ? 55  LYS A NZ    1 
ATOM   452  N N     . THR A 1 56  ? 2.60900   24.10400 -9.56800  1.000 16.46222 ? 56  THR A N     1 
ATOM   453  C CA    . THR A 1 56  ? 1.83500   22.90300 -9.29700  1.000 15.84392 ? 56  THR A CA    1 
ATOM   454  C C     . THR A 1 56  ? 1.87500   22.64500 -7.80300  1.000 14.15957 ? 56  THR A C     1 
ATOM   455  O O     . THR A 1 56  ? 2.88800   22.91200 -7.12500  1.000 15.27828 ? 56  THR A O     1 
ATOM   456  C CB    . THR A 1 56  ? 2.46500   21.73400 -10.05900 1.000 17.48767 ? 56  THR A CB    1 
ATOM   457  O OG1   . THR A 1 56  ? 2.52300   22.06400 -11.44200 1.000 19.33914 ? 56  THR A OG1   1 
ATOM   458  C CG2   . THR A 1 56  ? 1.63500   20.50400 -9.96400  1.000 19.15258 ? 56  THR A CG2   1 
ATOM   459  N N     . HIS A 1 57  ? 0.79900   22.07200 -7.26400  1.000 14.77354 ? 57  HIS A N     1 
ATOM   460  C CA    . HIS A 1 57  ? 0.76600   21.62100 -5.87600  1.000 14.66826 ? 57  HIS A CA    1 
ATOM   461  C C     . HIS A 1 57  ? 1.00400   20.12900 -5.77300  1.000 15.34052 ? 57  HIS A C     1 
ATOM   462  O O     . HIS A 1 57  ? 0.86200   19.38200 -6.74700  1.000 16.94356 ? 57  HIS A O     1 
ATOM   463  C CB    . HIS A 1 57  ? -0.53300  22.03200 -5.17900  1.000 17.65859 ? 57  HIS A CB    1 
ATOM   464  C CG    . HIS A 1 57  ? -1.75400  21.30100 -5.63800  1.000 18.25099 ? 57  HIS A CG    1 
ATOM   465  N ND1   . HIS A 1 57  ? -2.46500  20.42000 -4.84900  1.000 22.94497 ? 57  HIS A ND1   1 
ATOM   466  C CD2   . HIS A 1 57  ? -2.44300  21.41000 -6.79400  1.000 19.12243 ? 57  HIS A CD2   1 
ATOM   467  C CE1   . HIS A 1 57  ? -3.49800  19.95600 -5.53900  1.000 21.62944 ? 57  HIS A CE1   1 
ATOM   468  N NE2   . HIS A 1 57  ? -3.51100  20.55100 -6.71100  1.000 22.90776 ? 57  HIS A NE2   1 
ATOM   469  N N     . ALA A 1 58  ? 1.35200   19.69400 -4.58400  1.000 15.46259 ? 58  ALA A N     1 
ATOM   470  C CA    . ALA A 1 58  ? 1.72700   18.31000 -4.31300  1.000 15.63490 ? 58  ALA A CA    1 
ATOM   471  C C     . ALA A 1 58  ? 1.23100   17.98700 -2.92500  1.000 13.93779 ? 58  ALA A C     1 
ATOM   472  O O     . ALA A 1 58  ? 1.18900   18.86200 -2.07300  1.000 14.76374 ? 58  ALA A O     1 
ATOM   473  C CB    . ALA A 1 58  ? 3.23800   18.11100 -4.32700  1.000 16.44155 ? 58  ALA A CB    1 
ATOM   474  N N     . LEU A 1 59  ? 0.85000   16.73600 -2.68400  1.000 13.86325 ? 59  LEU A N     1 
ATOM   475  C CA    . LEU A 1 59  ? 0.63300   16.19700 -1.34300  1.000 13.79498 ? 59  LEU A CA    1 
ATOM   476  C C     . LEU A 1 59  ? 1.83800   15.37900 -0.95700  1.000 14.39541 ? 59  LEU A C     1 
ATOM   477  O O     . LEU A 1 59  ? 2.28400   14.53500 -1.74300  1.000 15.91947 ? 59  LEU A O     1 
ATOM   478  C CB    . LEU A 1 59  ? -0.60900  15.29400 -1.23700  1.000 15.60705 ? 59  LEU A CB    1 
ATOM   479  C CG    . LEU A 1 59  ? -1.89100  15.97600 -1.74100  1.000 16.83214 ? 59  LEU A CG    1 
ATOM   480  C CD1   . LEU A 1 59  ? -3.10000  15.01800 -1.52300  1.000 19.32541 ? 59  LEU A CD1   1 
ATOM   481  C CD2   . LEU A 1 59  ? -2.15800  17.27500 -1.05300  1.000 18.19545 ? 59  LEU A CD2   1 
ATOM   482  N N     . ILE A 1 60  ? 2.35400   15.59200 0.22700   1.000 14.08612 ? 60  ILE A N     1 
ATOM   483  C CA    . ILE A 1 60  ? 3.53300   14.87300 0.71000   1.000 15.30163 ? 60  ILE A CA    1 
ATOM   484  C C     . ILE A 1 60  ? 3.20400   14.30600 2.07900   1.000 14.19478 ? 60  ILE A C     1 
ATOM   485  O O     . ILE A 1 60  ? 2.72700   15.05700 2.94800   1.000 15.44976 ? 60  ILE A O     1 
ATOM   486  C CB    . ILE A 1 60  ? 4.76800   15.80200 0.78600   1.000 16.04198 ? 60  ILE A CB    1 
ATOM   487  C CG1   . ILE A 1 60  ? 5.10800   16.36600 -0.62000  1.000 19.38163 ? 60  ILE A CG1   1 
ATOM   488  C CG2   . ILE A 1 60  ? 5.94400   15.01400 1.38900   1.000 17.91276 ? 60  ILE A CG2   1 
ATOM   489  C CD1   . ILE A 1 60  ? 6.26500   17.34500 -0.63900  1.000 21.64128 ? 60  ILE A CD1   1 
ATOM   490  N N     . LEU A 1 61  ? 3.50900   13.03100 2.30200   1.000 13.64521 ? 61  LEU A N     1 
ATOM   491  C CA    . LEU A 1 61  ? 3.30500   12.39600 3.60000   1.000 14.91034 ? 61  LEU A CA    1 
ATOM   492  C C     . LEU A 1 61  ? 4.51600   12.64100 4.48200   1.000 15.71973 ? 61  LEU A C     1 
ATOM   493  O O     . LEU A 1 61  ? 5.65300   12.50500 4.01200   1.000 17.24556 ? 61  LEU A O     1 
ATOM   494  C CB    . LEU A 1 61  ? 3.15200   10.88900 3.37400   1.000 16.63064 ? 61  LEU A CB    1 
ATOM   495  C CG    . LEU A 1 61  ? 2.74300   10.06300 4.61000   1.000 17.84018 ? 61  LEU A CG    1 
ATOM   496  C CD1   . LEU A 1 61  ? 1.34500   10.49500 5.10900   1.000 18.33835 ? 61  LEU A CD1   1 
ATOM   497  C CD2   . LEU A 1 61  ? 2.72700   8.60400  4.24900   1.000 18.73303 ? 61  LEU A CD2   1 
ATOM   498  N N     . THR A 1 62  ? 4.31400   12.98300 5.75100   1.000 16.03028 ? 62  THR A N     1 
ATOM   499  C CA    . THR A 1 62  ? 5.47900   13.12800 6.62000   1.000 16.26976 ? 62  THR A CA    1 
ATOM   500  C C     . THR A 1 62  ? 6.07100   11.75300 6.91100   1.000 16.43955 ? 62  THR A C     1 
ATOM   501  O O     . THR A 1 62  ? 5.34800   10.75100 7.02400   1.000 16.98801 ? 62  THR A O     1 
ATOM   502  C CB    . THR A 1 62  ? 5.10500   13.82400 7.94800   1.000 16.01722 ? 62  THR A CB    1 
ATOM   503  O OG1   . THR A 1 62  ? 4.10300   13.07700 8.66000   1.000 16.41339 ? 62  THR A OG1   1 
ATOM   504  C CG2   . THR A 1 62  ? 4.59100   15.26300 7.68800   1.000 15.86289 ? 62  THR A CG2   1 
ATOM   505  N N     . LEU A 1 63  ? 7.40200   11.71600 7.09700   1.000 16.76131 ? 63  LEU A N     1 
ATOM   506  C CA    . LEU A 1 63  ? 8.03200   10.48900 7.57400   1.000 17.49880 ? 63  LEU A CA    1 
ATOM   507  C C     . LEU A 1 63  ? 7.54700   10.13100 8.97200   1.000 17.97779 ? 63  LEU A C     1 
ATOM   508  O O     . LEU A 1 63  ? 7.30300   8.95900  9.28200   1.000 21.00442 ? 63  LEU A O     1 
ATOM   509  C CB    . LEU A 1 63  ? 9.54900   10.75400 7.60700   1.000 19.40109 ? 63  LEU A CB    1 
ATOM   510  C CG    . LEU A 1 63  ? 10.39200  9.50500  7.87000   1.000 21.39625 ? 63  LEU A CG    1 
ATOM   511  C CD1   . LEU A 1 63  ? 10.11500  8.34700  6.87800   1.000 24.04334 ? 63  LEU A CD1   1 
ATOM   512  C CD2   . LEU A 1 63  ? 11.90800  9.81200  7.85700   1.000 22.67424 ? 63  LEU A CD2   1 
ATOM   513  N N     . GLU A 1 64  ? 7.36700   11.12200 9.83500   1.000 18.31070 ? 64  GLU A N     1 
ATOM   514  C CA    . GLU A 1 64  ? 7.03800   10.90300 11.23100  1.000 18.61870 ? 64  GLU A CA    1 
ATOM   515  C C     . GLU A 1 64  ? 5.54300   10.75000 11.43500  1.000 19.13575 ? 64  GLU A C     1 
ATOM   516  O O     . GLU A 1 64  ? 4.73900   11.47400 10.82000  1.000 18.75072 ? 64  GLU A O     1 
ATOM   517  C CB    . GLU A 1 64  ? 7.43900   12.12500 12.06200  1.000 19.09982 ? 64  GLU A CB    1 
ATOM   518  C CG    . GLU A 1 64  ? 8.94300   12.21500 12.25100  1.000 20.92289 ? 64  GLU A CG    1 
ATOM   519  C CD    . GLU A 1 64  ? 9.67500   13.00400 11.18900  1.000 21.36033 ? 64  GLU A CD    1 
ATOM   520  O OE1   . GLU A 1 64  ? 9.06500   13.39200 10.15400  1.000 19.79956 ? 64  GLU A OE1   1 
ATOM   521  O OE2   . GLU A 1 64  ? 10.92100  13.18200 11.43100  1.000 22.06309 ? 64  GLU A OE2   1 
ATOM   522  N N     . ARG A 1 65  ? 5.18700   9.80700  12.32200  1.000 20.34530 ? 65  ARG A N     1 
ATOM   523  C CA    . ARG A 1 65  ? 3.91800   9.84500  13.01600  1.000 21.34457 ? 65  ARG A CA    1 
ATOM   524  C C     . ARG A 1 65  ? 4.04500   10.84300 14.16600  1.000 22.08738 ? 65  ARG A C     1 
ATOM   525  O O     . ARG A 1 65  ? 5.04200   10.83800 14.89100  1.000 23.04230 ? 65  ARG A O     1 
ATOM   526  C CB    . ARG A 1 65  ? 3.61000   8.44000  13.57200  1.000 23.60704 ? 65  ARG A CB    1 
ATOM   527  C CG    . ARG A 1 65  ? 2.63900   8.37100  14.74100  1.000 25.54394 ? 65  ARG A CG    1 
ATOM   528  C CD    . ARG A 1 65  ? 2.70300   7.00400  15.40600  1.000 29.30082 ? 65  ARG A CD    1 
ATOM   529  N NE    . ARG A 1 65  ? 1.66300   6.89700  16.41300  1.000 31.30321 ? 65  ARG A NE    1 
ATOM   530  C CZ    . ARG A 1 65  ? 1.65900   6.02400  17.40500  1.000 32.89206 ? 65  ARG A CZ    1 
ATOM   531  N NH1   . ARG A 1 65  ? 2.65000   5.15100  17.56600  1.000 33.57947 ? 65  ARG A NH1   1 
ATOM   532  N NH2   . ARG A 1 65  ? 0.63300   6.03000  18.24800  1.000 34.13438 ? 65  ARG A NH2   1 
ATOM   533  N N     . VAL A 1 66  ? 3.00900   11.64600 14.36900  1.000 21.64906 ? 66  VAL A N     1 
ATOM   534  C CA    . VAL A 1 66  ? 2.90300   12.59000 15.47500  1.000 21.68880 ? 66  VAL A CA    1 
ATOM   535  C C     . VAL A 1 66  ? 1.62300   12.28500 16.25300  1.000 22.14910 ? 66  VAL A C     1 
ATOM   536  O O     . VAL A 1 66  ? 0.54300   12.17200 15.66000  1.000 21.85394 ? 66  VAL A O     1 
ATOM   537  C CB    . VAL A 1 66  ? 2.88500   14.04600 14.95300  1.000 22.93263 ? 66  VAL A CB    1 
ATOM   538  C CG1   . VAL A 1 66  ? 2.79500   15.04000 16.07200  1.000 23.87788 ? 66  VAL A CG1   1 
ATOM   539  C CG2   . VAL A 1 66  ? 4.17300   14.31600 14.16800  1.000 24.39014 ? 66  VAL A CG2   1 
ATOM   540  N N     . LYS A 1 67  ? 1.72900   12.19500 17.57900  1.000 23.01663 ? 67  LYS A N     1 
ATOM   541  C CA    . LYS A 1 67  ? 0.57200   11.96900 18.43700  1.000 23.47958 ? 67  LYS A CA    1 
ATOM   542  C C     . LYS A 1 67  ? 0.50200   13.12800 19.42300  1.000 24.60847 ? 67  LYS A C     1 
ATOM   543  O O     . LYS A 1 67  ? 1.44300   13.33200 20.20300  1.000 26.63190 ? 67  LYS A O     1 
ATOM   544  C CB    . LYS A 1 67  ? 0.65900   10.63700 19.17800  1.000 26.96734 ? 67  LYS A CB    1 
ATOM   545  C CG    . LYS A 1 67  ? -0.50200  10.43000 20.13000  1.000 28.42175 ? 67  LYS A CG    1 
ATOM   546  C CD    . LYS A 1 67  ? -0.42000  9.04400  20.81200  1.000 28.85578 ? 67  LYS A CD    1 
ATOM   547  N N     . LEU A 1 68  ? -0.60300  13.88200 19.39200  1.000 23.64395 ? 68  LEU A N     1 
ATOM   548  C CA    . LEU A 1 68  ? -0.79800  15.02900 20.26800  1.000 25.95270 ? 68  LEU A CA    1 
ATOM   549  C C     . LEU A 1 68  ? -1.67800  14.67300 21.45900  1.000 28.06865 ? 68  LEU A C     1 
ATOM   550  O O     . LEU A 1 68  ? -2.74400  14.06900 21.28300  1.000 29.43124 ? 68  LEU A O     1 
ATOM   551  C CB    . LEU A 1 68  ? -1.46300  16.15300 19.48200  1.000 26.22626 ? 68  LEU A CB    1 
ATOM   552  C CG    . LEU A 1 68  ? -0.47900  16.99400 18.66400  1.000 28.04225 ? 68  LEU A CG    1 
ATOM   553  C CD1   . LEU A 1 68  ? 0.07500   16.24300 17.51000  1.000 31.17278 ? 68  LEU A CD1   1 
ATOM   554  C CD2   . LEU A 1 68  ? -1.23800  18.19300 18.17000  1.000 28.49098 ? 68  LEU A CD2   1 
ATOM   555  N N     . PRO A 1 69  ? -1.27100  15.09500 22.66100  1.000 27.98437 ? 69  PRO A N     1 
ATOM   556  C CA    . PRO A 1 69  ? -2.14500  15.02900 23.84400  1.000 28.89323 ? 69  PRO A CA    1 
ATOM   557  C C     . PRO A 1 69  ? -3.43400  15.80000 23.61800  1.000 29.40747 ? 69  PRO A C     1 
ATOM   558  O O     . PRO A 1 69  ? -3.53700  16.62800 22.70500  1.000 28.63707 ? 69  PRO A O     1 
ATOM   559  C CB    . PRO A 1 69  ? -1.30500  15.76100 24.90300  1.000 31.18249 ? 69  PRO A CB    1 
ATOM   560  C CG    . PRO A 1 69  ? 0.06800   15.51100 24.49500  1.000 31.17414 ? 69  PRO A CG    1 
ATOM   561  C CD    . PRO A 1 69  ? 0.06800   15.61100 22.98600  1.000 28.95751 ? 69  PRO A CD    1 
ATOM   562  N N     . ASP A 1 70  ? -4.41200  15.58800 24.50100  1.000 30.76081 ? 70  ASP A N     1 
ATOM   563  C CA    . ASP A 1 70  ? -5.69100  16.27100 24.38000  1.000 30.55595 ? 70  ASP A CA    1 
ATOM   564  C C     . ASP A 1 70  ? -5.63700  17.74900 24.79000  1.000 29.31343 ? 70  ASP A C     1 
ATOM   565  O O     . ASP A 1 70  ? -6.65900  18.44700 24.72100  1.000 29.64988 ? 70  ASP A O     1 
ATOM   566  C CB    . ASP A 1 70  ? -6.75900  15.51800 25.18300  1.000 32.29759 ? 70  ASP A CB    1 
ATOM   567  N N     . ASP A 1 71  ? -4.47600  18.24000 25.23200  1.000 27.57841 ? 71  ASP A N     1 
ATOM   568  C CA    . ASP A 1 71  ? -4.32700  19.64400 25.59900  1.000 26.79494 ? 71  ASP A CA    1 
ATOM   569  C C     . ASP A 1 71  ? -3.21200  20.34200 24.81100  1.000 23.02477 ? 71  ASP A C     1 
ATOM   570  O O     . ASP A 1 71  ? -2.62200  21.31700 25.29100  1.000 23.54264 ? 71  ASP A O     1 
ATOM   571  C CB    . ASP A 1 71  ? -4.14200  19.81300 27.11100  1.000 28.31016 ? 71  ASP A CB    1 
ATOM   572  C CG    . ASP A 1 71  ? -2.82000  19.25600 27.61200  1.000 29.77050 ? 71  ASP A CG    1 
ATOM   573  O OD1   . ASP A 1 71  ? -2.20800  18.43200 26.90900  1.000 29.97139 ? 71  ASP A OD1   1 
ATOM   574  O OD2   . ASP A 1 71  ? -2.43000  19.60100 28.74900  1.000 31.66439 ? 71  ASP A OD2   1 
ATOM   575  N N     . VAL A 1 72  ? -2.88800  19.84400 23.61800  1.000 21.32900 ? 72  VAL A N     1 
ATOM   576  C CA    . VAL A 1 72  ? -1.89800  20.49700 22.77000  1.000 20.35294 ? 72  VAL A CA    1 
ATOM   577  C C     . VAL A 1 72  ? -2.41800  20.56600 21.34600  1.000 20.26995 ? 72  VAL A C     1 
ATOM   578  O O     . VAL A 1 72  ? -2.91300  19.56500 20.80700  1.000 22.10569 ? 72  VAL A O     1 
ATOM   579  C CB    . VAL A 1 72  ? -0.58400  19.70300 22.81800  1.000 22.12294 ? 72  VAL A CB    1 
ATOM   580  C CG1   . VAL A 1 72  ? 0.43200   20.17400 21.81100  1.000 23.19133 ? 72  VAL A CG1   1 
ATOM   581  C CG2   . VAL A 1 72  ? 0.00300   19.77300 24.25300  1.000 23.09244 ? 72  VAL A CG2   1 
ATOM   582  N N     . MET A 1 73  ? -2.20300  21.73900 20.73400  1.000 18.63492 ? 73  MET A N     1 
ATOM   583  C CA    . MET A 1 73  ? -2.53800  21.97100 19.30600  1.000 18.11662 ? 73  MET A CA    1 
ATOM   584  C C     . MET A 1 73  ? -1.23000  22.08400 18.50300  1.000 17.57333 ? 73  MET A C     1 
ATOM   585  O O     . MET A 1 73  ? -0.31000  22.71700 18.99000  1.000 19.06560 ? 73  MET A O     1 
ATOM   586  C CB    . MET A 1 73  ? -3.30700  23.28900 19.20600  1.000 18.36379 ? 73  MET A CB    1 
ATOM   587  C CG    . MET A 1 73  ? -3.57800  23.73500 17.77600  1.000 19.36552 ? 73  MET A CG    1 
ATOM   588  S SD    . MET A 1 73  ? -5.04400  22.97300 17.03200  1.000 20.23768 ? 73  MET A SD    1 
ATOM   589  C CE    . MET A 1 73  ? -6.19100  24.34900 17.03600  1.000 21.97309 ? 73  MET A CE    1 
ATOM   590  N N     . GLY A 1 74  ? -1.17600  21.46800 17.31300  1.000 15.83954 ? 74  GLY A N     1 
ATOM   591  C CA    . GLY A 1 74  ? 0.01100   21.55500 16.45700  1.000 16.06624 ? 74  GLY A CA    1 
ATOM   592  C C     . GLY A 1 74  ? -0.12600  22.59900 15.35900  1.000 14.45837 ? 74  GLY A C     1 
ATOM   593  O O     . GLY A 1 74  ? -1.17300  22.71300 14.70200  1.000 15.40980 ? 74  GLY A O     1 
ATOM   594  N N     . ASP A 1 75  ? 0.96000   23.31500 15.12000  1.000 13.97361 ? 75  ASP A N     1 
ATOM   595  C CA    . ASP A 1 75  ? 0.95300   24.52000 14.27800  1.000 13.91884 ? 75  ASP A CA    1 
ATOM   596  C C     . ASP A 1 75  ? 2.16500   24.47100 13.34100  1.000 13.55895 ? 75  ASP A C     1 
ATOM   597  O O     . ASP A 1 75  ? 3.29600   24.61200 13.80700  1.000 14.97506 ? 75  ASP A O     1 
ATOM   598  C CB    . ASP A 1 75  ? 1.05200   25.74600 15.21400  1.000 16.58306 ? 75  ASP A CB    1 
ATOM   599  C CG    . ASP A 1 75  ? 0.73300   27.05500 14.54100  1.000 18.23750 ? 75  ASP A CG    1 
ATOM   600  O OD1   . ASP A 1 75  ? 0.70100   27.03800 13.32600  1.000 18.49398 ? 75  ASP A OD1   1 
ATOM   601  O OD2   . ASP A 1 75  ? 0.57400   28.09700 15.26200  1.000 18.60239 ? 75  ASP A OD2   1 
ATOM   602  N N     . MET A 1 76  ? 1.95600   24.23200 12.03300  1.000 13.19060 ? 76  MET A N     1 
ATOM   603  C CA    . MET A 1 76  ? 3.03900   23.98100 11.08800  1.000 13.16711 ? 76  MET A CA    1 
ATOM   604  C C     . MET A 1 76  ? 3.35900   25.17400 10.21200  1.000 14.06367 ? 76  MET A C     1 
ATOM   605  O O     . MET A 1 76  ? 2.45800   25.91400 9.79200   1.000 14.26007 ? 76  MET A O     1 
ATOM   606  C CB    . MET A 1 76  ? 2.62700   22.82700 10.18000  1.000 14.14116 ? 76  MET A CB    1 
ATOM   607  C CG    . MET A 1 76  ? 2.40700   21.52000 10.94800  1.000 15.57838 ? 76  MET A CG    1 
ATOM   608  S SD    . MET A 1 76  ? 2.06800   20.12400 9.90400   1.000 16.84673 ? 76  MET A SD    1 
ATOM   609  C CE    . MET A 1 76  ? 0.35800   20.49600 9.44200   1.000 17.39775 ? 76  MET A CE    1 
ATOM   610  N N     . LYS A 1 77  ? 4.65800   25.34100 9.91300   1.000 13.81717 ? 77  LYS A N     1 
ATOM   611  C CA    . LYS A 1 77  ? 5.13200   26.29700 8.91500   1.000 12.77885 ? 77  LYS A CA    1 
ATOM   612  C C     . LYS A 1 77  ? 6.23100   25.65400 8.12400   1.000 12.34017 ? 77  LYS A C     1 
ATOM   613  O O     . LYS A 1 77  ? 6.97900   24.81000 8.63600   1.000 13.99947 ? 77  LYS A O     1 
ATOM   614  C CB    . LYS A 1 77  ? 5.68000   27.59600 9.55500   1.000 14.63412 ? 77  LYS A CB    1 
ATOM   615  C CG    . LYS A 1 77  ? 4.60300   28.46400 10.23300  1.000 17.27313 ? 77  LYS A CG    1 
ATOM   616  C CD    . LYS A 1 77  ? 5.17300   29.79800 10.61900  1.000 17.67141 ? 77  LYS A CD    1 
ATOM   617  C CE    . LYS A 1 77  ? 4.11900   30.85900 10.95700  1.000 23.13418 ? 77  LYS A CE    1 
ATOM   618  N NZ    . LYS A 1 77  ? 3.39000   30.36200 12.07200  1.000 25.12192 ? 77  LYS A NZ    1 
ATOM   619  N N     . LEU A 1 78  ? 6.35200   26.04900 6.86500   1.000 12.90647 ? 78  LEU A N     1 
ATOM   620  C CA    . LEU A 1 78  ? 7.42300   25.57800 6.02900   1.000 13.81076 ? 78  LEU A CA    1 
ATOM   621  C C     . LEU A 1 78  ? 8.75700   26.05600 6.56600   1.000 13.49558 ? 78  LEU A C     1 
ATOM   622  O O     . LEU A 1 78  ? 8.84300   27.09700 7.21900   1.000 15.96526 ? 78  LEU A O     1 
ATOM   623  C CB    . LEU A 1 78  ? 7.16100   26.23800 4.64400   1.000 17.50877 ? 78  LEU A CB    1 
ATOM   624  C CG    . LEU A 1 78  ? 7.80800   25.68500 3.41900   1.000 19.76035 ? 78  LEU A CG    1 
ATOM   625  C CD1   . LEU A 1 78  ? 7.38900   24.22100 3.25500   1.000 19.16166 ? 78  LEU A CD1   1 
ATOM   626  C CD2   . LEU A 1 78  ? 7.30500   26.49200 2.24600   1.000 17.87569 ? 78  LEU A CD2   1 
ATOM   627  N N     . ARG A 1 79  ? 9.82300   25.29700 6.31100   1.000 15.49914 ? 79  ARG A N     1 
ATOM   628  C CA    . ARG A 1 79  ? 11.16500  25.78400 6.61200   1.000 18.19450 ? 79  ARG A CA    1 
ATOM   629  C C     . ARG A 1 79  ? 11.56600  26.92800 5.69900   1.000 17.40561 ? 79  ARG A C     1 
ATOM   630  O O     . ARG A 1 79  ? 11.15900  26.99800 4.53700   1.000 17.07010 ? 79  ARG A O     1 
ATOM   631  C CB    . ARG A 1 79  ? 12.22900  24.67700 6.53500   1.000 21.76539 ? 79  ARG A CB    1 
ATOM   632  C CG    . ARG A 1 79  ? 11.97500  23.71900 7.71000   1.000 26.50924 ? 79  ARG A CG    1 
ATOM   633  C CD    . ARG A 1 79  ? 13.13200  22.86900 8.04600   1.000 32.19198 ? 79  ARG A CD    1 
ATOM   634  N NE    . ARG A 1 79  ? 14.33600  23.63300 8.33700   1.000 35.32785 ? 79  ARG A NE    1 
ATOM   635  C CZ    . ARG A 1 79  ? 15.51100  23.38500 7.77900   1.000 38.41228 ? 79  ARG A CZ    1 
ATOM   636  N NH1   . ARG A 1 79  ? 15.65500  22.41500 6.88900   1.000 39.29205 ? 79  ARG A NH1   1 
ATOM   637  N NH2   . ARG A 1 79  ? 16.56100  24.13400 8.11300   1.000 39.49489 ? 79  ARG A NH2   1 
ATOM   638  N N     . SER A 1 80  ? 12.41200  27.82300 6.21700   1.000 19.14219 ? 80  SER A N     1 
ATOM   639  C CA    . SER A 1 80  ? 12.67600  29.08400 5.52800   1.000 20.00321 ? 80  SER A CA    1 
ATOM   640  C C     . SER A 1 80  ? 13.31400  28.89400 4.15300   1.000 18.05802 ? 80  SER A C     1 
ATOM   641  O O     . SER A 1 80  ? 12.96800  29.60900 3.20500   1.000 18.15088 ? 80  SER A O     1 
ATOM   642  C CB    . SER A 1 80  ? 13.51400  30.02600 6.42500   1.000 23.75607 ? 80  SER A CB    1 
ATOM   643  O OG    . SER A 1 80  ? 14.85500  29.54400 6.49800   1.000 30.44985 ? 80  SER A OG    1 
ATOM   644  N N     . SER A 1 81  ? 14.26300  27.94300 4.00100   1.000 18.31826 ? 81  SER A N     1 
ATOM   645  C CA    . SER A 1 81  ? 14.91400  27.82400 2.69000   1.000 19.94107 ? 81  SER A CA    1 
ATOM   646  C C     . SER A 1 81  ? 13.92000  27.39800 1.59900   1.000 19.06569 ? 81  SER A C     1 
ATOM   647  O O     . SER A 1 81  ? 13.99600  27.83700 0.45900   1.000 21.39295 ? 81  SER A O     1 
ATOM   648  C CB    . SER A 1 81  ? 16.10900  26.84300 2.74600   1.000 24.02438 ? 81  SER A CB    1 
ATOM   649  O OG    . SER A 1 81  ? 15.65700  25.64800 3.35500   1.000 30.47515 ? 81  SER A OG    1 
ATOM   650  N N     . LEU A 1 82  ? 12.92700  26.57100 1.95100   1.000 17.66303 ? 82  LEU A N     1 
ATOM   651  C CA    . LEU A 1 82  ? 11.95500  26.11300 0.96200   1.000 17.40031 ? 82  LEU A CA    1 
ATOM   652  C C     . LEU A 1 82  ? 10.99700  27.22800 0.57200   1.000 16.08742 ? 82  LEU A C     1 
ATOM   653  O O     . LEU A 1 82  ? 10.70000  27.39400 -0.62300  1.000 16.62147 ? 82  LEU A O     1 
ATOM   654  C CB    . LEU A 1 82  ? 11.17800  24.93100 1.53300   1.000 17.65359 ? 82  LEU A CB    1 
ATOM   655  C CG    . LEU A 1 82  ? 12.07000  23.68400 1.65200   1.000 19.70869 ? 82  LEU A CG    1 
ATOM   656  C CD1   . LEU A 1 82  ? 11.29500  22.55400 2.31500   1.000 20.93738 ? 82  LEU A CD1   1 
ATOM   657  C CD2   . LEU A 1 82  ? 12.49400  23.22600 0.28400   1.000 24.00083 ? 82  LEU A CD2   1 
ATOM   658  N N     . ALA A 1 83  ? 10.68300  28.11700 1.52000   1.000 15.05591 ? 83  ALA A N     1 
ATOM   659  C CA    . ALA A 1 83  ? 9.87900   29.28200 1.16600   1.000 16.29538 ? 83  ALA A CA    1 
ATOM   660  C C     . ALA A 1 83  ? 10.64100  30.16500 0.20200   1.000 17.60713 ? 83  ALA A C     1 
ATOM   661  O O     . ALA A 1 83  ? 10.09400  30.63300 -0.79700  1.000 18.67454 ? 83  ALA A O     1 
ATOM   662  C CB    . ALA A 1 83  ? 9.52000   30.09400 2.40300   1.000 18.82536 ? 83  ALA A CB    1 
ATOM   663  N N     . ARG A 1 84  ? 11.96100  30.37200 0.44500   1.000 16.57670 ? 84  ARG A N     1 
ATOM   664  C CA    . ARG A 1 84  ? 12.73600  31.23600 -0.43400  1.000 19.24082 ? 84  ARG A CA    1 
ATOM   665  C C     . ARG A 1 84  ? 12.78800  30.70300 -1.85200  1.000 19.72214 ? 84  ARG A C     1 
ATOM   666  O O     . ARG A 1 84  ? 12.93100  31.50400 -2.81000  1.000 23.57785 ? 84  ARG A O     1 
ATOM   667  C CB    . ARG A 1 84  ? 14.13500  31.46800 0.15100   1.000 21.95696 ? 84  ARG A CB    1 
ATOM   668  C CG    . ARG A 1 84  ? 14.11200  32.33000 1.41800   1.000 22.69748 ? 84  ARG A CG    1 
ATOM   669  C CD    . ARG A 1 84  ? 15.55600  32.83100 1.69200   1.000 26.24110 ? 84  ARG A CD    1 
ATOM   670  N NE    . ARG A 1 84  ? 16.52900  31.72300 1.65400   1.000 28.07266 ? 84  ARG A NE    1 
ATOM   671  C CZ    . ARG A 1 84  ? 16.85300  31.01600 2.72400   1.000 31.29735 ? 84  ARG A CZ    1 
ATOM   672  N NH1   . ARG A 1 84  ? 16.31900  31.27900 3.89700   1.000 31.05355 ? 84  ARG A NH1   1 
ATOM   673  N NH2   . ARG A 1 84  ? 17.73600  30.02600 2.61600   1.000 31.30470 ? 84  ARG A NH2   1 
ATOM   674  N N     . GLU A 1 85  ? 12.72700  29.38600 -2.01800  1.000 18.10798 ? 85  GLU A N     1 
ATOM   675  C CA    . GLU A 1 85  ? 12.80600  28.75700 -3.32000  1.000 18.70398 ? 85  GLU A CA    1 
ATOM   676  C C     . GLU A 1 85  ? 11.47000  28.73900 -4.03200  1.000 19.83701 ? 85  GLU A C     1 
ATOM   677  O O     . GLU A 1 85  ? 11.36700  28.22400 -5.15000  1.000 21.82769 ? 85  GLU A O     1 
ATOM   678  C CB    . GLU A 1 85  ? 13.39000  27.35200 -3.18400  1.000 21.46493 ? 85  GLU A CB    1 
ATOM   679  C CG    . GLU A 1 85  ? 14.87800  27.37400 -2.68700  1.000 23.94345 ? 85  GLU A CG    1 
ATOM   680  C CD    . GLU A 1 85  ? 15.53000  25.99900 -2.56200  1.000 27.36203 ? 85  GLU A CD    1 
ATOM   681  O OE1   . GLU A 1 85  ? 15.28100  25.15200 -3.42900  1.000 28.09733 ? 85  GLU A OE1   1 
ATOM   682  O OE2   . GLU A 1 85  ? 16.30700  25.78400 -1.59200  1.000 27.55863 ? 85  GLU A OE2   1 
ATOM   683  N N     . GLY A 1 86  ? 10.43800  29.26000 -3.39900  1.000 16.75008 ? 86  GLY A N     1 
ATOM   684  C CA    . GLY A 1 86  ? 9.17400   29.46200 -4.07700  1.000 17.90938 ? 86  GLY A CA    1 
ATOM   685  C C     . GLY A 1 86  ? 8.07400   28.54700 -3.60200  1.000 14.98349 ? 86  GLY A C     1 
ATOM   686  O O     . GLY A 1 86  ? 6.98000   28.61700 -4.17500  1.000 15.74780 ? 86  GLY A O     1 
ATOM   687  N N     . LEU A 1 87  ? 8.27700   27.71100 -2.57100  1.000 14.79484 ? 87  LEU A N     1 
ATOM   688  C CA    . LEU A 1 87  ? 7.18200   26.88400 -2.06600  1.000 13.42743 ? 87  LEU A CA    1 
ATOM   689  C C     . LEU A 1 87  ? 6.32500   27.61300 -1.05500  1.000 12.90261 ? 87  LEU A C     1 
ATOM   690  O O     . LEU A 1 87  ? 6.80500   28.48400 -0.28600  1.000 13.38764 ? 87  LEU A O     1 
ATOM   691  C CB    . LEU A 1 87  ? 7.75800   25.64600 -1.34800  1.000 14.67257 ? 87  LEU A CB    1 
ATOM   692  C CG    . LEU A 1 87  ? 8.55000   24.70300 -2.28000  1.000 16.29681 ? 87  LEU A CG    1 
ATOM   693  C CD1   . LEU A 1 87  ? 8.73900   23.34900 -1.52500  1.000 18.60768 ? 87  LEU A CD1   1 
ATOM   694  C CD2   . LEU A 1 87  ? 7.93900   24.50400 -3.65800  1.000 17.45102 ? 87  LEU A CD2   1 
ATOM   695  N N     . LEU A 1 88  ? 5.02400   27.29100 -1.08400  1.000 13.06242 ? 88  LEU A N     1 
ATOM   696  C CA    . LEU A 1 88  ? 4.05000   27.74200 -0.08600  1.000 12.76521 ? 88  LEU A CA    1 
ATOM   697  C C     . LEU A 1 88  ? 3.35200   26.51500 0.47300   1.000 13.25793 ? 88  LEU A C     1 
ATOM   698  O O     . LEU A 1 88  ? 2.87000   25.64800 -0.27900  1.000 16.60299 ? 88  LEU A O     1 
ATOM   699  C CB    . LEU A 1 88  ? 2.95800   28.62500 -0.70600  1.000 15.69614 ? 88  LEU A CB    1 
ATOM   700  C CG    . LEU A 1 88  ? 3.50400   29.96300 -1.16500  1.000 16.40409 ? 88  LEU A CG    1 
ATOM   701  C CD1   . LEU A 1 88  ? 3.49900   29.89700 -2.66300  1.000 20.14929 ? 88  LEU A CD1   1 
ATOM   702  C CD2   . LEU A 1 88  ? 2.66600   31.13700 -0.69400  1.000 20.39295 ? 88  LEU A CD2   1 
ATOM   703  N N     . GLY A 1 89  ? 3.26900   26.39400 1.77700   1.000 13.39651 ? 89  GLY A N     1 
ATOM   704  C CA    . GLY A 1 89  ? 2.50300   25.29400 2.38100   1.000 13.14672 ? 89  GLY A CA    1 
ATOM   705  C C     . GLY A 1 89  ? 1.06900   25.72200 2.62800   1.000 13.29062 ? 89  GLY A C     1 
ATOM   706  O O     . GLY A 1 89  ? 0.80400   26.86800 2.95800   1.000 15.84221 ? 89  GLY A O     1 
ATOM   707  N N     . SER A 1 90  ? 0.15400   24.80000 2.45100   1.000 12.71575 ? 90  SER A N     1 
ATOM   708  C CA    . SER A 1 90  ? -1.24100  25.06800 2.77600   1.000 12.72063 ? 90  SER A CA    1 
ATOM   709  C C     . SER A 1 90  ? -1.63200  24.12300 3.88200   1.000 12.70085 ? 90  SER A C     1 
ATOM   710  O O     . SER A 1 90  ? -1.99200  22.99000 3.60500   1.000 14.01667 ? 90  SER A O     1 
ATOM   711  C CB    . SER A 1 90  ? -2.10700  24.88800 1.54200   1.000 13.05281 ? 90  SER A CB    1 
ATOM   712  O OG    . SER A 1 90  ? -3.40700  25.29400 1.91000   1.000 13.76104 ? 90  SER A OG    1 
ATOM   713  N N     . PHE A 1 91  ? -1.52200  24.57400 5.11000   1.000 13.57724 ? 91  PHE A N     1 
ATOM   714  C CA    . PHE A 1 91  ? -1.60200  23.68600 6.25400   1.000 14.46680 ? 91  PHE A CA    1 
ATOM   715  C C     . PHE A 1 91  ? -2.83800  23.92600 7.09400   1.000 14.09207 ? 91  PHE A C     1 
ATOM   716  O O     . PHE A 1 91  ? -3.24200  25.08200 7.30000   1.000 16.33946 ? 91  PHE A O     1 
ATOM   717  C CB    . PHE A 1 91  ? -0.37500  23.78700 7.15100   1.000 18.47119 ? 91  PHE A CB    1 
ATOM   718  C CG    . PHE A 1 91  ? 0.93600   23.49300 6.43500   1.000 18.82418 ? 91  PHE A CG    1 
ATOM   719  C CD1   . PHE A 1 91  ? 1.07600   22.48200 5.49700   1.000 19.62683 ? 91  PHE A CD1   1 
ATOM   720  C CD2   . PHE A 1 91  ? 1.98800   24.28400 6.71500   1.000 21.31598 ? 91  PHE A CD2   1 
ATOM   721  C CE1   . PHE A 1 91  ? 2.32600   22.30600 4.83600   1.000 18.89934 ? 91  PHE A CE1   1 
ATOM   722  C CE2   . PHE A 1 91  ? 3.22500   24.09800 6.04500   1.000 20.76922 ? 91  PHE A CE2   1 
ATOM   723  C CZ    . PHE A 1 91  ? 3.37600   23.14100 5.16200   1.000 20.01366 ? 91  PHE A CZ    1 
ATOM   724  N N     . ALA A 1 92  ? -3.44800  22.85900 7.59600   1.000 13.45236 ? 92  ALA A N     1 
ATOM   725  C CA    . ALA A 1 92  ? -4.56200  22.93200 8.55800   1.000 13.75538 ? 92  ALA A CA    1 
ATOM   726  C C     . ALA A 1 92  ? -3.99700  22.83900 9.96300   1.000 13.60290 ? 92  ALA A C     1 
ATOM   727  O O     . ALA A 1 92  ? -2.85700  22.44900 10.16000  1.000 14.20910 ? 92  ALA A O     1 
ATOM   728  C CB    . ALA A 1 92  ? -5.54500  21.77400 8.32800   1.000 14.76320 ? 92  ALA A CB    1 
ATOM   729  N N     . TRP A 1 93  ? -4.82900  23.17900 10.94200  1.000 13.81066 ? 93  TRP A N     1 
ATOM   730  C CA    . TRP A 1 93  ? -4.44300  22.91600 12.32700  1.000 13.82315 ? 93  TRP A CA    1 
ATOM   731  C C     . TRP A 1 93  ? -4.27800  21.41300 12.55700  1.000 14.30713 ? 93  TRP A C     1 
ATOM   732  O O     . TRP A 1 93  ? -4.92200  20.60200 11.90800  1.000 14.89671 ? 93  TRP A O     1 
ATOM   733  C CB    . TRP A 1 93  ? -5.54500  23.41500 13.26700  1.000 12.81019 ? 93  TRP A CB    1 
ATOM   734  C CG    . TRP A 1 93  ? -5.57300  24.89200 13.34800  1.000 13.22425 ? 93  TRP A CG    1 
ATOM   735  C CD1   . TRP A 1 93  ? -6.52000  25.72400 12.86700  1.000 14.39146 ? 93  TRP A CD1   1 
ATOM   736  C CD2   . TRP A 1 93  ? -4.60900  25.71700 14.01700  1.000 14.47146 ? 93  TRP A CD2   1 
ATOM   737  N NE1   . TRP A 1 93  ? -6.21300  27.03100 13.19800  1.000 14.71238 ? 93  TRP A NE1   1 
ATOM   738  C CE2   . TRP A 1 93  ? -5.04600  27.05500 13.91700  1.000 14.20335 ? 93  TRP A CE2   1 
ATOM   739  C CE3   . TRP A 1 93  ? -3.43600  25.44400 14.72400  1.000 14.66252 ? 93  TRP A CE3   1 
ATOM   740  C CZ2   . TRP A 1 93  ? -4.31600  28.14100 14.44900  1.000 16.65900 ? 93  TRP A CZ2   1 
ATOM   741  C CZ3   . TRP A 1 93  ? -2.72400  26.52100 15.29400  1.000 16.57136 ? 93  TRP A CZ3   1 
ATOM   742  C CH2   . TRP A 1 93  ? -3.18900  27.84300 15.16700  1.000 16.48189 ? 93  TRP A CH2   1 
ATOM   743  N N     . VAL A 1 94  ? -3.36000  21.03000 13.45500  1.000 14.33118 ? 94  VAL A N     1 
ATOM   744  C CA    . VAL A 1 94  ? -3.23900  19.63000 13.90400  1.000 14.76439 ? 94  VAL A CA    1 
ATOM   745  C C     . VAL A 1 94  ? -3.94400  19.53200 15.26100  1.000 14.89642 ? 94  VAL A C     1 
ATOM   746  O O     . VAL A 1 94  ? -3.47900  20.09400 16.26300  1.000 16.59438 ? 94  VAL A O     1 
ATOM   747  C CB    . VAL A 1 94  ? -1.76500  19.19500 13.99100  1.000 16.24312 ? 94  VAL A CB    1 
ATOM   748  C CG1   . VAL A 1 94  ? -1.67800  17.71000 14.32700  1.000 17.25332 ? 94  VAL A CG1   1 
ATOM   749  C CG2   . VAL A 1 94  ? -1.01700  19.49300 12.69000  1.000 17.25320 ? 94  VAL A CG2   1 
ATOM   750  N N     . ASP A 1 95  ? -5.12000  18.92000 15.24700  1.000 16.63951 ? 95  ASP A N     1 
ATOM   751  C CA    . ASP A 1 95  ? -6.03300  19.01300 16.38100  1.000 19.46447 ? 95  ASP A CA    1 
ATOM   752  C C     . ASP A 1 95  ? -5.53000  18.23300 17.59800  1.000 19.43188 ? 95  ASP A C     1 
ATOM   753  O O     . ASP A 1 95  ? -4.85500  17.20000 17.46300  1.000 20.12741 ? 95  ASP A O     1 
ATOM   754  C CB    . ASP A 1 95  ? -7.42300  18.51200 15.97000  1.000 22.33535 ? 95  ASP A CB    1 
ATOM   755  C CG    . ASP A 1 95  ? -8.00400  19.34500 14.83700  1.000 24.57570 ? 95  ASP A CG    1 
ATOM   756  O OD1   . ASP A 1 95  ? -8.35800  20.51700 15.07500  1.000 26.53150 ? 95  ASP A OD1   1 
ATOM   757  O OD2   . ASP A 1 95  ? -8.06400  18.84300 13.68500  1.000 23.82304 ? 95  ASP A OD2   1 
ATOM   758  N N     . PRO A 1 96  ? -5.83400  18.72200 18.80500  1.000 20.03541 ? 96  PRO A N     1 
ATOM   759  C CA    . PRO A 1 96  ? -5.57000  17.94700 20.01900  1.000 19.91383 ? 96  PRO A CA    1 
ATOM   760  C C     . PRO A 1 96  ? -6.16400  16.55900 19.87100  1.000 21.73288 ? 96  PRO A C     1 
ATOM   761  O O     . PRO A 1 96  ? -7.30400  16.41300 19.47100  1.000 24.80366 ? 96  PRO A O     1 
ATOM   762  C CB    . PRO A 1 96  ? -6.32000  18.74100 21.10600  1.000 20.99287 ? 96  PRO A CB    1 
ATOM   763  C CG    . PRO A 1 96  ? -6.29200  20.18700 20.61700  1.000 22.94920 ? 96  PRO A CG    1 
ATOM   764  C CD    . PRO A 1 96  ? -6.49600  20.00100 19.09900  1.000 21.40125 ? 96  PRO A CD    1 
ATOM   765  N N     . GLY A 1 97  ? -5.35300  15.55300 20.20100  1.000 23.00282 ? 97  GLY A N     1 
ATOM   766  C CA    . GLY A 1 97  ? -5.76300  14.15200 20.06800  1.000 23.01767 ? 97  GLY A CA    1 
ATOM   767  C C     . GLY A 1 97  ? -5.36800  13.51900 18.74900  1.000 23.12004 ? 97  GLY A C     1 
ATOM   768  O O     . GLY A 1 97  ? -5.49000  12.29800 18.61500  1.000 23.73490 ? 97  GLY A O     1 
ATOM   769  N N     . TRP A 1 98  ? -4.90500  14.29800 17.76700  1.000 21.83103 ? 98  TRP A N     1 
ATOM   770  C CA    . TRP A 1 98  ? -4.44700  13.70800 16.51600  1.000 19.66384 ? 98  TRP A CA    1 
ATOM   771  C C     . TRP A 1 98  ? -3.38600  12.64300 16.77000  1.000 21.30988 ? 98  TRP A C     1 
ATOM   772  O O     . TRP A 1 98  ? -2.47800  12.81800 17.57800  1.000 21.90364 ? 98  TRP A O     1 
ATOM   773  C CB    . TRP A 1 98  ? -3.84600  14.79800 15.62700  1.000 19.24972 ? 98  TRP A CB    1 
ATOM   774  C CG    . TRP A 1 98  ? -3.10800  14.20200 14.46000  1.000 18.54984 ? 98  TRP A CG    1 
ATOM   775  C CD1   . TRP A 1 98  ? -1.74700  14.04900 14.31400  1.000 19.48161 ? 98  TRP A CD1   1 
ATOM   776  C CD2   . TRP A 1 98  ? -3.69900  13.61800 13.29900  1.000 19.26354 ? 98  TRP A CD2   1 
ATOM   777  N NE1   . TRP A 1 98  ? -1.45700  13.44000 13.11500  1.000 18.95814 ? 98  TRP A NE1   1 
ATOM   778  C CE2   . TRP A 1 98  ? -2.64600  13.13800 12.49000  1.000 20.18148 ? 98  TRP A CE2   1 
ATOM   779  C CE3   . TRP A 1 98  ? -5.02100  13.40500 12.89700  1.000 20.81818 ? 98  TRP A CE3   1 
ATOM   780  C CZ2   . TRP A 1 98  ? -2.87800  12.52700 11.24800  1.000 21.54580 ? 98  TRP A CZ2   1 
ATOM   781  C CZ3   . TRP A 1 98  ? -5.26000  12.74600 11.68200  1.000 22.04801 ? 98  TRP A CZ3   1 
ATOM   782  C CH2   . TRP A 1 98  ? -4.17800  12.32300 10.87400  1.000 21.93381 ? 98  TRP A CH2   1 
ATOM   783  N N     . ASP A 1 99  ? -3.44500  11.57400 16.00300  1.000 21.33113 ? 99  ASP A N     1 
ATOM   784  C CA    . ASP A 1 99  ? -2.40300  10.55100 16.03100  1.000 22.53595 ? 99  ASP A CA    1 
ATOM   785  C C     . ASP A 1 99  ? -2.19200  10.04900 14.60100  1.000 21.80819 ? 99  ASP A C     1 
ATOM   786  O O     . ASP A 1 99  ? -3.03600  9.31900  14.09600  1.000 23.34736 ? 99  ASP A O     1 
ATOM   787  C CB    . ASP A 1 99  ? -2.83900  9.41400  16.97000  1.000 24.44333 ? 99  ASP A CB    1 
ATOM   788  C CG    . ASP A 1 99  ? -1.77900  8.37200  17.15100  1.000 27.71788 ? 99  ASP A CG    1 
ATOM   789  O OD1   . ASP A 1 99  ? -0.73800  8.40700  16.47400  1.000 29.09997 ? 99  ASP A OD1   1 
ATOM   790  O OD2   . ASP A 1 99  ? -1.96700  7.48600  18.02000  1.000 30.72335 ? 99  ASP A OD2   1 
ATOM   791  N N     . GLY A 1 100 ? -1.07600  10.36200 13.96300  1.000 20.30686 ? 100 GLY A N     1 
ATOM   792  C CA    . GLY A 1 100 ? -0.79300  9.79300  12.65100  1.000 19.09496 ? 100 GLY A CA    1 
ATOM   793  C C     . GLY A 1 100 ? 0.29100   10.54400 11.89400  1.000 17.79692 ? 100 GLY A C     1 
ATOM   794  O O     . GLY A 1 100 ? 0.76500   11.62100 12.29400  1.000 18.99506 ? 100 GLY A O     1 
ATOM   795  N N     . ASN A 1 101 ? 0.67000   9.98300  10.74700  1.000 17.75385 ? 101 ASN A N     1 
ATOM   796  C CA    . ASN A 1 101 ? 1.46200   10.74900 9.76900   1.000 16.57209 ? 101 ASN A CA    1 
ATOM   797  C C     . ASN A 1 101 ? 0.57600   11.77200 9.08200   1.000 17.05666 ? 101 ASN A C     1 
ATOM   798  O O     . ASN A 1 101 ? -0.59700  11.49600 8.84700   1.000 18.08480 ? 101 ASN A O     1 
ATOM   799  C CB    . ASN A 1 101 ? 2.01200   9.77800  8.69800   1.000 18.03424 ? 101 ASN A CB    1 
ATOM   800  C CG    . ASN A 1 101 ? 2.92700   8.72800  9.28000   1.000 19.39196 ? 101 ASN A CG    1 
ATOM   801  O OD1   . ASN A 1 101 ? 2.47900   7.86900  10.03000  1.000 20.85347 ? 101 ASN A OD1   1 
ATOM   802  N ND2   . ASN A 1 101 ? 4.21700   8.78800  8.94500   1.000 20.68768 ? 101 ASN A ND2   1 
ATOM   803  N N     . LEU A 1 102 ? 1.14500   12.92000 8.75600   1.000 15.70461 ? 102 LEU A N     1 
ATOM   804  C CA    . LEU A 1 102 ? 0.36900   14.04500 8.23800   1.000 14.95549 ? 102 LEU A CA    1 
ATOM   805  C C     . LEU A 1 102 ? 0.47300   14.10500 6.71800   1.000 14.20344 ? 102 LEU A C     1 
ATOM   806  O O     . LEU A 1 102 ? 1.56500   13.91200 6.15100   1.000 15.96517 ? 102 LEU A O     1 
ATOM   807  C CB    . LEU A 1 102 ? 0.86800   15.35800 8.87100   1.000 17.18476 ? 102 LEU A CB    1 
ATOM   808  C CG    . LEU A 1 102 ? 0.63000   15.45600 10.37400  1.000 16.77200 ? 102 LEU A CG    1 
ATOM   809  C CD1   . LEU A 1 102 ? 1.63600   16.38800 11.04400  1.000 19.52074 ? 102 LEU A CD1   1 
ATOM   810  C CD2   . LEU A 1 102 ? -0.79600  15.85100 10.62600  1.000 19.13069 ? 102 LEU A CD2   1 
ATOM   811  N N     . THR A 1 103 ? -0.65000  14.41300 6.05700   1.000 14.57182 ? 103 THR A N     1 
ATOM   812  C CA    . THR A 1 103 ? -0.66100  14.66200 4.62100   1.000 15.44267 ? 103 THR A CA    1 
ATOM   813  C C     . THR A 1 103 ? -0.60900  16.17100 4.42700   1.000 14.86542 ? 103 THR A C     1 
ATOM   814  O O     . THR A 1 103 ? -1.55300  16.90100 4.80300   1.000 15.49509 ? 103 THR A O     1 
ATOM   815  C CB    . THR A 1 103 ? -1.93200  14.08300 4.00700   1.000 16.45007 ? 103 THR A CB    1 
ATOM   816  O OG1   . THR A 1 103 ? -1.92700  12.64900 4.12700   1.000 18.24820 ? 103 THR A OG1   1 
ATOM   817  C CG2   . THR A 1 103 ? -2.01000  14.41300 2.54500   1.000 18.47454 ? 103 THR A CG2   1 
ATOM   818  N N     . LEU A 1 104 ? 0.46400   16.63700 3.85100   1.000 13.94584 ? 104 LEU A N     1 
ATOM   819  C CA    . LEU A 1 104 ? 0.76100   18.07100 3.74000   1.000 13.23701 ? 104 LEU A CA    1 
ATOM   820  C C     . LEU A 1 104 ? 0.72000   18.54300 2.28400   1.000 14.01513 ? 104 LEU A C     1 
ATOM   821  O O     . LEU A 1 104 ? 1.37600   17.96000 1.41300   1.000 16.16459 ? 104 LEU A O     1 
ATOM   822  C CB    . LEU A 1 104 ? 2.11800   18.38400 4.35000   1.000 13.92415 ? 104 LEU A CB    1 
ATOM   823  C CG    . LEU A 1 104 ? 2.26800   17.99200 5.82300   1.000 14.56615 ? 104 LEU A CG    1 
ATOM   824  C CD1   . LEU A 1 104 ? 3.56000   18.49700 6.36400   1.000 16.91944 ? 104 LEU A CD1   1 
ATOM   825  C CD2   . LEU A 1 104 ? 1.08600   18.49400 6.66800   1.000 15.35622 ? 104 LEU A CD2   1 
ATOM   826  N N     . MET A 1 105 ? 0.05600   19.66100 2.01500   1.000 12.96662 ? 105 MET A N     1 
ATOM   827  C CA    . MET A 1 105 ? 0.00200   20.19100 0.66600   1.000 12.56456 ? 105 MET A CA    1 
ATOM   828  C C     . MET A 1 105 ? 1.02400   21.31800 0.54500   1.000 11.57865 ? 105 MET A C     1 
ATOM   829  O O     . MET A 1 105 ? 1.10300   22.23400 1.40800   1.000 12.77474 ? 105 MET A O     1 
ATOM   830  C CB    . MET A 1 105 ? -1.42500  20.69200 0.35200   1.000 13.58039 ? 105 MET A CB    1 
ATOM   831  C CG    . MET A 1 105 ? -1.57400  21.28700 -1.03000  1.000 14.36464 ? 105 MET A CG    1 
ATOM   832  S SD    . MET A 1 105 ? -0.84900  22.89800 -1.39400  1.000 14.34449 ? 105 MET A SD    1 
ATOM   833  C CE    . MET A 1 105 ? -2.27200  23.78900 -1.97400  1.000 16.82889 ? 105 MET A CE    1 
ATOM   834  N N     . LEU A 1 106 ? 1.83700   21.24600 -0.49900  1.000 11.94786 ? 106 LEU A N     1 
ATOM   835  C CA    . LEU A 1 106 ? 2.80200   22.28800 -0.84100  1.000 12.60430 ? 106 LEU A CA    1 
ATOM   836  C C     . LEU A 1 106 ? 2.54200   22.74100 -2.25400  1.000 12.97508 ? 106 LEU A C     1 
ATOM   837  O O     . LEU A 1 106 ? 2.37600   21.88900 -3.14000  1.000 15.97874 ? 106 LEU A O     1 
ATOM   838  C CB    . LEU A 1 106 ? 4.24000   21.81900 -0.71400  1.000 16.44375 ? 106 LEU A CB    1 
ATOM   839  C CG    . LEU A 1 106 ? 4.75500   21.35000 0.62000   1.000 19.72485 ? 106 LEU A CG    1 
ATOM   840  C CD1   . LEU A 1 106 ? 6.29900   21.19400 0.52200   1.000 21.42845 ? 106 LEU A CD1   1 
ATOM   841  C CD2   . LEU A 1 106 ? 4.52300   22.27000 1.62300   1.000 22.57325 ? 106 LEU A CD2   1 
ATOM   842  N N     . PHE A 1 107 ? 2.59400   24.03700 -2.53200  1.000 12.42231 ? 107 PHE A N     1 
ATOM   843  C CA    . PHE A 1 107 ? 2.44200   24.57700 -3.88100  1.000 12.49527 ? 107 PHE A CA    1 
ATOM   844  C C     . PHE A 1 107 ? 3.76900   25.18000 -4.29800  1.000 12.36751 ? 107 PHE A C     1 
ATOM   845  O O     . PHE A 1 107 ? 4.35000   26.00200 -3.56400  1.000 13.09607 ? 107 PHE A O     1 
ATOM   846  C CB    . PHE A 1 107 ? 1.35800   25.66600 -3.87700  1.000 12.53434 ? 107 PHE A CB    1 
ATOM   847  C CG    . PHE A 1 107 ? 1.25100   26.38600 -5.14800  1.000 13.45878 ? 107 PHE A CG    1 
ATOM   848  C CD1   . PHE A 1 107 ? 0.97400   25.73700 -6.35600  1.000 15.28053 ? 107 PHE A CD1   1 
ATOM   849  C CD2   . PHE A 1 107 ? 1.35800   27.76900 -5.18400  1.000 15.60367 ? 107 PHE A CD2   1 
ATOM   850  C CE1   . PHE A 1 107 ? 0.81600   26.47500 -7.50800  1.000 16.88632 ? 107 PHE A CE1   1 
ATOM   851  C CE2   . PHE A 1 107 ? 1.25000   28.47200 -6.37700  1.000 16.08223 ? 107 PHE A CE2   1 
ATOM   852  C CZ    . PHE A 1 107 ? 0.99300   27.81000 -7.52500  1.000 16.14879 ? 107 PHE A CZ    1 
ATOM   853  N N     . ASN A 1 108 ? 4.25800   24.81500 -5.47500  1.000 13.91529 ? 108 ASN A N     1 
ATOM   854  C CA    . ASN A 1 108 ? 5.44800   25.46400 -6.02200  1.000 14.26457 ? 108 ASN A CA    1 
ATOM   855  C C     . ASN A 1 108 ? 5.02700   26.64000 -6.86600  1.000 14.06810 ? 108 ASN A C     1 
ATOM   856  O O     . ASN A 1 108 ? 4.54200   26.46700 -7.98400  1.000 16.53269 ? 108 ASN A O     1 
ATOM   857  C CB    . ASN A 1 108 ? 6.20000   24.44100 -6.87300  1.000 15.70755 ? 108 ASN A CB    1 
ATOM   858  C CG    . ASN A 1 108 ? 7.40800   25.01800 -7.54700  1.000 16.45081 ? 108 ASN A CG    1 
ATOM   859  O OD1   . ASN A 1 108 ? 7.79800   26.17100 -7.28400  1.000 16.86612 ? 108 ASN A OD1   1 
ATOM   860  N ND2   . ASN A 1 108 ? 8.08300   24.19300 -8.36300  1.000 17.02244 ? 108 ASN A ND2   1 
ATOM   861  N N     . ALA A 1 109 ? 5.20900   27.83800 -6.33400  1.000 14.19897 ? 109 ALA A N     1 
ATOM   862  C CA    . ALA A 1 109 ? 4.82000   29.05400 -7.05100  1.000 17.09087 ? 109 ALA A CA    1 
ATOM   863  C C     . ALA A 1 109 ? 5.85900   29.48900 -8.06500  1.000 17.72758 ? 109 ALA A C     1 
ATOM   864  O O     . ALA A 1 109 ? 5.63800   30.47200 -8.76400  1.000 21.40242 ? 109 ALA A O     1 
ATOM   865  C CB    . ALA A 1 109 ? 4.62800   30.20600 -6.04600  1.000 17.81044 ? 109 ALA A CB    1 
ATOM   866  N N     . SER A 1 110 ? 7.00800   28.82500 -8.13700  1.000 18.39506 ? 110 SER A N     1 
ATOM   867  C CA    . SER A 1 110 ? 8.05800   29.27800 -9.03200  1.000 19.41830 ? 110 SER A CA    1 
ATOM   868  C C     . SER A 1 110 ? 7.86100   28.67800 -10.43000 1.000 20.38269 ? 110 SER A C     1 
ATOM   869  O O     . SER A 1 110 ? 7.07500   27.74200 -10.62100 1.000 21.01495 ? 110 SER A O     1 
ATOM   870  C CB    . SER A 1 110 ? 9.38800   28.85900 -8.43200  1.000 21.25664 ? 110 SER A CB    1 
ATOM   871  O OG    . SER A 1 110 ? 9.68200   27.53900 -8.75100  1.000 24.47142 ? 110 SER A OG    1 
ATOM   872  N N     . GLU A 1 111 ? 8.61100   29.21400 -11.38400 1.000 21.70656 ? 111 GLU A N     1 
ATOM   873  C CA    . GLU A 1 111 ? 8.64600   28.73800 -12.76100 1.000 24.27073 ? 111 GLU A CA    1 
ATOM   874  C C     . GLU A 1 111 ? 9.60000   27.56300 -12.97100 1.000 23.79335 ? 111 GLU A C     1 
ATOM   875  O O     . GLU A 1 111 ? 9.74000   27.06600 -14.09500 1.000 23.67588 ? 111 GLU A O     1 
ATOM   876  C CB    . GLU A 1 111 ? 9.04900   29.91200 -13.66900 1.000 27.96189 ? 111 GLU A CB    1 
ATOM   877  C CG    . GLU A 1 111 ? 7.93600   30.98600 -13.76600 1.000 32.63674 ? 111 GLU A CG    1 
ATOM   878  C CD    . GLU A 1 111 ? 6.68500   30.49300 -14.49500 1.000 37.31987 ? 111 GLU A CD    1 
ATOM   879  O OE1   . GLU A 1 111 ? 6.76900   30.20800 -15.71200 1.000 41.67741 ? 111 GLU A OE1   1 
ATOM   880  O OE2   . GLU A 1 111 ? 5.60500   30.39300 -13.85700 1.000 39.07078 ? 111 GLU A OE2   1 
ATOM   881  N N     . GLU A 1 112 ? 10.23100  27.07600 -11.91600 1.000 24.51703 ? 112 GLU A N     1 
ATOM   882  C CA    . GLU A 1 112 ? 11.21700  26.01500 -12.01700 1.000 25.21442 ? 112 GLU A CA    1 
ATOM   883  C C     . GLU A 1 112 ? 10.83800  24.90200 -11.05600 1.000 22.96138 ? 112 GLU A C     1 
ATOM   884  O O     . GLU A 1 112 ? 10.27500  25.17200 -9.98400  1.000 21.71420 ? 112 GLU A O     1 
ATOM   885  C CB    . GLU A 1 112 ? 12.59000  26.54000 -11.58000 1.000 30.05353 ? 112 GLU A CB    1 
ATOM   886  C CG    . GLU A 1 112 ? 13.09600  27.79300 -12.34000 1.000 36.55303 ? 112 GLU A CG    1 
ATOM   887  C CD    . GLU A 1 112 ? 14.40600  28.28500 -11.75500 1.000 45.13026 ? 112 GLU A CD    1 
ATOM   888  O OE1   . GLU A 1 112 ? 14.79900  27.85000 -10.64400 1.000 48.11350 ? 112 GLU A OE1   1 
ATOM   889  O OE2   . GLU A 1 112 ? 15.03800  29.11600 -12.41400 1.000 50.51837 ? 112 GLU A OE2   1 
ATOM   890  N N     . PRO A 1 113 ? 11.14400  23.66300 -11.37500 1.000 21.66979 ? 113 PRO A N     1 
ATOM   891  C CA    . PRO A 1 113 ? 10.79300  22.56600 -10.44600 1.000 21.17901 ? 113 PRO A CA    1 
ATOM   892  C C     . PRO A 1 113 ? 11.57400  22.67700 -9.14900  1.000 20.68965 ? 113 PRO A C     1 
ATOM   893  O O     . PRO A 1 113 ? 12.70900  23.17600 -9.11300  1.000 21.21564 ? 113 PRO A O     1 
ATOM   894  C CB    . PRO A 1 113 ? 11.16400  21.29900 -11.24000 1.000 22.04096 ? 113 PRO A CB    1 
ATOM   895  C CG    . PRO A 1 113 ? 12.21900  21.76400 -12.21400 1.000 24.53375 ? 113 PRO A CG    1 
ATOM   896  C CD    . PRO A 1 113 ? 11.79600  23.18000 -12.60700 1.000 23.39408 ? 113 PRO A CD    1 
ATOM   897  N N     . VAL A 1 114 ? 10.97500  22.19800 -8.06500  1.000 19.58076 ? 114 VAL A N     1 
ATOM   898  C CA    . VAL A 1 114 ? 11.64300  22.18600 -6.77400  1.000 18.14308 ? 114 VAL A CA    1 
ATOM   899  C C     . VAL A 1 114 ? 11.67100  20.75100 -6.27500  1.000 18.32749 ? 114 VAL A C     1 
ATOM   900  O O     . VAL A 1 114 ? 10.60800  20.10900 -6.17700  1.000 18.40367 ? 114 VAL A O     1 
ATOM   901  C CB    . VAL A 1 114 ? 10.95100  23.11700 -5.76300  1.000 18.98158 ? 114 VAL A CB    1 
ATOM   902  C CG1   . VAL A 1 114 ? 11.59400  22.99900 -4.38800  1.000 20.05569 ? 114 VAL A CG1   1 
ATOM   903  C CG2   . VAL A 1 114 ? 11.00700  24.56200 -6.23800  1.000 20.84286 ? 114 VAL A CG2   1 
ATOM   904  N N     . GLU A 1 115 ? 12.85800  20.27100 -5.91200  1.000 19.51740 ? 115 GLU A N     1 
ATOM   905  C CA    . GLU A 1 115 ? 13.03200  18.87900 -5.48800  1.000 19.89481 ? 115 GLU A CA    1 
ATOM   906  C C     . GLU A 1 115 ? 13.18500  18.82200 -3.97700  1.000 20.10823 ? 115 GLU A C     1 
ATOM   907  O O     . GLU A 1 115 ? 13.84400  19.68400 -3.38200  1.000 22.34623 ? 115 GLU A O     1 
ATOM   908  C CB    . GLU A 1 115 ? 14.29300  18.25700 -6.12900  1.000 25.40864 ? 115 GLU A CB    1 
ATOM   909  C CG    . GLU A 1 115 ? 14.35400  18.43300 -7.62100  1.000 31.36604 ? 115 GLU A CG    1 
ATOM   910  C CD    . GLU A 1 115 ? 15.36000  17.49800 -8.27200  1.000 35.60600 ? 115 GLU A CD    1 
ATOM   911  O OE1   . GLU A 1 115 ? 16.14300  16.85800 -7.52700  1.000 36.34971 ? 115 GLU A OE1   1 
ATOM   912  O OE2   . GLU A 1 115 ? 15.34900  17.39700 -9.52000  1.000 37.15612 ? 115 GLU A OE2   1 
ATOM   913  N N     . LEU A 1 116 ? 12.61600  17.79600 -3.35000  1.000 19.16407 ? 116 LEU A N     1 
ATOM   914  C CA    . LEU A 1 116 ? 12.82300  17.54800 -1.92500  1.000 20.23728 ? 116 LEU A CA    1 
ATOM   915  C C     . LEU A 1 116 ? 13.21700  16.08800 -1.78900  1.000 19.32813 ? 116 LEU A C     1 
ATOM   916  O O     . LEU A 1 116 ? 12.61400  15.21800 -2.43200  1.000 20.41850 ? 116 LEU A O     1 
ATOM   917  C CB    . LEU A 1 116 ? 11.54000  17.77200 -1.11600  1.000 20.67932 ? 116 LEU A CB    1 
ATOM   918  C CG    . LEU A 1 116 ? 10.87700  19.19100 -1.14500  1.000 23.49192 ? 116 LEU A CG    1 
ATOM   919  C CD1   . LEU A 1 116 ? 10.07700  19.39800 -2.37600  1.000 26.39160 ? 116 LEU A CD1   1 
ATOM   920  C CD2   . LEU A 1 116 ? 9.88400   19.32500 0.01200   1.000 26.85385 ? 116 LEU A CD2   1 
ATOM   921  N N     . ASN A 1 117 ? 14.22300  15.80500 -0.99300  1.000 19.80514 ? 117 ASN A N     1 
ATOM   922  C CA    . ASN A 1 117 ? 14.72000  14.44700 -0.89700  1.000 19.02465 ? 117 ASN A CA    1 
ATOM   923  C C     . ASN A 1 117 ? 13.93800  13.68100 0.15600   1.000 17.83447 ? 117 ASN A C     1 
ATOM   924  O O     . ASN A 1 117 ? 13.41400  14.24800 1.12700   1.000 18.11907 ? 117 ASN A O     1 
ATOM   925  C CB    . ASN A 1 117 ? 16.18300  14.46000 -0.44300  1.000 22.88106 ? 117 ASN A CB    1 
ATOM   926  C CG    . ASN A 1 117 ? 17.13100  14.84000 -1.54800  1.000 27.96483 ? 117 ASN A CG    1 
ATOM   927  O OD1   . ASN A 1 117 ? 16.91400  14.53700 -2.71000  1.000 30.28793 ? 117 ASN A OD1   1 
ATOM   928  N ND2   . ASN A 1 117 ? 18.19400  15.53500 -1.17600  1.000 31.33753 ? 117 ASN A ND2   1 
ATOM   929  N N     . TYR A 1 118 ? 13.85900  12.36100 -0.03600  1.000 19.05031 ? 118 TYR A N     1 
ATOM   930  C CA    . TYR A 1 118 ? 13.30900  11.51100 1.00900   1.000 19.19866 ? 118 TYR A CA    1 
ATOM   931  C C     . TYR A 1 118 ? 14.06700  11.75700 2.30100   1.000 19.47178 ? 118 TYR A C     1 
ATOM   932  O O     . TYR A 1 118 ? 15.29700  11.79000 2.29300   1.000 20.65508 ? 118 TYR A O     1 
ATOM   933  C CB    . TYR A 1 118 ? 13.42400  10.04400 0.57500   1.000 20.54151 ? 118 TYR A CB    1 
ATOM   934  C CG    . TYR A 1 118 ? 12.98100  9.02900  1.59600   1.000 20.87317 ? 118 TYR A CG    1 
ATOM   935  C CD1   . TYR A 1 118 ? 11.68600  9.01900  2.06700   1.000 21.38063 ? 118 TYR A CD1   1 
ATOM   936  C CD2   . TYR A 1 118 ? 13.84600  8.05500  2.03300   1.000 22.93674 ? 118 TYR A CD2   1 
ATOM   937  C CE1   . TYR A 1 118 ? 11.25100  8.12800  2.98000   1.000 22.05972 ? 118 TYR A CE1   1 
ATOM   938  C CE2   . TYR A 1 118 ? 13.42000  7.11500  2.95100   1.000 23.71655 ? 118 TYR A CE2   1 
ATOM   939  C CZ    . TYR A 1 118 ? 12.10900  7.17600  3.42800   1.000 24.40229 ? 118 TYR A CZ    1 
ATOM   940  O OH    . TYR A 1 118 ? 11.66500  6.24100  4.34300   1.000 29.96284 ? 118 TYR A OH    1 
ATOM   941  N N     . GLY A 1 119 ? 13.35300  11.97400 3.40300   1.000 18.63597 ? 119 GLY A N     1 
ATOM   942  C CA    . GLY A 1 119 ? 13.98700  12.21300 4.68200   1.000 19.16661 ? 119 GLY A CA    1 
ATOM   943  C C     . GLY A 1 119 ? 14.43800  13.65000 4.92400   1.000 18.87562 ? 119 GLY A C     1 
ATOM   944  O O     . GLY A 1 119 ? 14.97800  13.93700 6.00100   1.000 20.81986 ? 119 GLY A O     1 
ATOM   945  N N     . GLU A 1 120 ? 14.22300  14.56900 3.97700   1.000 17.30948 ? 120 GLU A N     1 
ATOM   946  C CA    . GLU A 1 120 ? 14.65500  15.95600 4.15300   1.000 18.24308 ? 120 GLU A CA    1 
ATOM   947  C C     . GLU A 1 120 ? 13.73700  16.70100 5.10400   1.000 16.48339 ? 120 GLU A C     1 
ATOM   948  O O     . GLU A 1 120 ? 12.52400  16.57600 5.01600   1.000 16.87714 ? 120 GLU A O     1 
ATOM   949  C CB    . GLU A 1 120 ? 14.63300  16.61500 2.78200   1.000 19.15418 ? 120 GLU A CB    1 
ATOM   950  C CG    . GLU A 1 120 ? 15.14500  18.06400 2.83500   1.000 22.38694 ? 120 GLU A CG    1 
ATOM   951  C CD    . GLU A 1 120 ? 15.46100  18.68100 1.47800   1.000 24.45525 ? 120 GLU A CD    1 
ATOM   952  O OE1   . GLU A 1 120 ? 15.28100  18.04900 0.42200   1.000 24.62590 ? 120 GLU A OE1   1 
ATOM   953  O OE2   . GLU A 1 120 ? 15.94700  19.83900 1.48200   1.000 29.52202 ? 120 GLU A OE2   1 
ATOM   954  N N     . ARG A 1 121 ? 14.31900  17.45400 6.02800   1.000 17.18508 ? 121 ARG A N     1 
ATOM   955  C CA    . ARG A 1 121 ? 13.53600  18.30900 6.91300   1.000 16.84093 ? 121 ARG A CA    1 
ATOM   956  C C     . ARG A 1 121 ? 12.81900  19.38500 6.09800   1.000 17.15832 ? 121 ARG A C     1 
ATOM   957  O O     . ARG A 1 121 ? 13.48200  20.12600 5.36100   1.000 20.30167 ? 121 ARG A O     1 
ATOM   958  C CB    . ARG A 1 121 ? 14.51400  18.99700 7.87300   1.000 19.15821 ? 121 ARG A CB    1 
ATOM   959  C CG    . ARG A 1 121 ? 15.12400  17.98800 8.84400   1.000 20.39899 ? 121 ARG A CG    1 
ATOM   960  C CD    . ARG A 1 121 ? 16.00500  18.59800 9.90800   1.000 24.81256 ? 121 ARG A CD    1 
ATOM   961  N NE    . ARG A 1 121 ? 17.23700  19.10800 9.33600   1.000 27.40124 ? 121 ARG A NE    1 
ATOM   962  C CZ    . ARG A 1 121 ? 17.69500  20.32800 9.59100   1.000 30.66877 ? 121 ARG A CZ    1 
ATOM   963  N NH1   . ARG A 1 121 ? 17.06100  21.14800 10.42500  1.000 31.69918 ? 121 ARG A NH1   1 
ATOM   964  N NH2   . ARG A 1 121 ? 18.82000  20.73300 9.00800   1.000 32.31697 ? 121 ARG A NH2   1 
ATOM   965  N N     . PHE A 1 122 ? 11.51700  19.50200 6.24000   1.000 16.13328 ? 122 PHE A N     1 
ATOM   966  C CA    . PHE A 1 122 ? 10.78500  20.43900 5.37700   1.000 15.86448 ? 122 PHE A CA    1 
ATOM   967  C C     . PHE A 1 122 ? 9.73300   21.30900 6.06600   1.000 15.01660 ? 122 PHE A C     1 
ATOM   968  O O     . PHE A 1 122 ? 9.44500   22.40500 5.54500   1.000 15.15382 ? 122 PHE A O     1 
ATOM   969  C CB    . PHE A 1 122 ? 10.24300  19.74700 4.09300   1.000 16.55861 ? 122 PHE A CB    1 
ATOM   970  C CG    . PHE A 1 122 ? 8.97800   18.91500 4.23600   1.000 15.87771 ? 122 PHE A CG    1 
ATOM   971  C CD1   . PHE A 1 122 ? 8.81500   17.89400 5.17100   1.000 15.73107 ? 122 PHE A CD1   1 
ATOM   972  C CD2   . PHE A 1 122 ? 7.95800   19.10400 3.31600   1.000 18.39490 ? 122 PHE A CD2   1 
ATOM   973  C CE1   . PHE A 1 122 ? 7.66600   17.11400 5.20200   1.000 16.32999 ? 122 PHE A CE1   1 
ATOM   974  C CE2   . PHE A 1 122 ? 6.80900   18.32500 3.36700   1.000 18.24914 ? 122 PHE A CE2   1 
ATOM   975  C CZ    . PHE A 1 122 ? 6.67300   17.33800 4.29500   1.000 17.14433 ? 122 PHE A CZ    1 
ATOM   976  N N     . VAL A 1 123 ? 9.12900   20.87400 7.17600   1.000 14.68405 ? 123 VAL A N     1 
ATOM   977  C CA    . VAL A 1 123 ? 8.05900   21.63400 7.83200   1.000 14.33596 ? 123 VAL A CA    1 
ATOM   978  C C     . VAL A 1 123 ? 8.31300   21.60100 9.31000   1.000 13.58458 ? 123 VAL A C     1 
ATOM   979  O O     . VAL A 1 123 ? 8.49000   20.50300 9.86200   1.000 15.69452 ? 123 VAL A O     1 
ATOM   980  C CB    . VAL A 1 123 ? 6.69200   21.03100 7.47800   1.000 14.58524 ? 123 VAL A CB    1 
ATOM   981  C CG1   . VAL A 1 123 ? 5.57900   21.65600 8.34400   1.000 15.87111 ? 123 VAL A CG1   1 
ATOM   982  C CG2   . VAL A 1 123 ? 6.32600   21.24100 6.00300   1.000 15.09844 ? 123 VAL A CG2   1 
ATOM   983  N N     . GLN A 1 124 ? 8.33900   22.75600 9.95700   1.000 13.56138 ? 124 GLN A N     1 
ATOM   984  C CA    . GLN A 1 124 ? 8.52000   22.78200 11.40700  1.000 14.23262 ? 124 GLN A CA    1 
ATOM   985  C C     . GLN A 1 124 ? 7.16100   22.86500 12.07000  1.000 13.45092 ? 124 GLN A C     1 
ATOM   986  O O     . GLN A 1 124 ? 6.39900   23.83200 11.85700  1.000 13.82347 ? 124 GLN A O     1 
ATOM   987  C CB    . GLN A 1 124 ? 9.39400   23.95300 11.85200  1.000 15.85337 ? 124 GLN A CB    1 
ATOM   988  C CG    . GLN A 1 124 ? 9.59300   23.90300 13.34500  1.000 17.09003 ? 124 GLN A CG    1 
ATOM   989  C CD    . GLN A 1 124 ? 10.35600  24.99800 14.00700  1.000 19.64194 ? 124 GLN A CD    1 
ATOM   990  O OE1   . GLN A 1 124 ? 10.40400  25.01500 15.23000  1.000 23.68090 ? 124 GLN A OE1   1 
ATOM   991  N NE2   . GLN A 1 124 ? 10.91600  25.91200 13.28000  1.000 19.88467 ? 124 GLN A NE2   1 
ATOM   992  N N     . ILE A 1 125 ? 6.84900   21.86800 12.90300  1.000 13.91902 ? 125 ILE A N     1 
ATOM   993  C CA    . ILE A 1 125 ? 5.62700   21.85600 13.68500  1.000 14.95906 ? 125 ILE A CA    1 
ATOM   994  C C     . ILE A 1 125 ? 5.94900   22.34800 15.08100  1.000 15.26134 ? 125 ILE A C     1 
ATOM   995  O O     . ILE A 1 125 ? 6.90100   21.86500 15.72300  1.000 15.83473 ? 125 ILE A O     1 
ATOM   996  C CB    . ILE A 1 125 ? 4.96500   20.45800 13.69100  1.000 14.40659 ? 125 ILE A CB    1 
ATOM   997  C CG1   . ILE A 1 125 ? 3.61200   20.54100 14.40700  1.000 15.67305 ? 125 ILE A CG1   1 
ATOM   998  C CG2   . ILE A 1 125 ? 5.88100   19.35100 14.31100  1.000 16.22656 ? 125 ILE A CG2   1 
ATOM   999  C CD1   . ILE A 1 125 ? 2.70300   19.26800 14.19800  1.000 16.18043 ? 125 ILE A CD1   1 
ATOM   1000 N N     . ALA A 1 126 ? 5.16800   23.30100 15.55400  1.000 15.14182 ? 126 ALA A N     1 
ATOM   1001 C CA    . ALA A 1 126 ? 5.23300   23.81900 16.92100  1.000 15.92201 ? 126 ALA A CA    1 
ATOM   1002 C C     . ALA A 1 126 ? 3.99200   23.37700 17.68300  1.000 15.67893 ? 126 ALA A C     1 
ATOM   1003 O O     . ALA A 1 126 ? 2.98300   22.98100 17.05900  1.000 16.31777 ? 126 ALA A O     1 
ATOM   1004 C CB    . ALA A 1 126 ? 5.44500   25.33800 16.92300  1.000 16.78885 ? 126 ALA A CB    1 
ATOM   1005 N N     . PHE A 1 127 ? 4.02500   23.44700 19.00200  1.000 15.77901 ? 127 PHE A N     1 
ATOM   1006 C CA    . PHE A 1 127 ? 3.00300   22.82500 19.83300  1.000 16.72615 ? 127 PHE A CA    1 
ATOM   1007 C C     . PHE A 1 127 ? 2.55800   23.84100 20.86600  1.000 17.46475 ? 127 PHE A C     1 
ATOM   1008 O O     . PHE A 1 127 ? 3.38700   24.37000 21.61400  1.000 19.33113 ? 127 PHE A O     1 
ATOM   1009 C CB    . PHE A 1 127 ? 3.57200   21.56400 20.51800  1.000 17.82737 ? 127 PHE A CB    1 
ATOM   1010 C CG    . PHE A 1 127 ? 4.03900   20.53600 19.53700  1.000 16.98201 ? 127 PHE A CG    1 
ATOM   1011 C CD1   . PHE A 1 127 ? 3.14000   19.62500 18.99400  1.000 18.23388 ? 127 PHE A CD1   1 
ATOM   1012 C CD2   . PHE A 1 127 ? 5.36300   20.50200 19.09600  1.000 17.74037 ? 127 PHE A CD2   1 
ATOM   1013 C CE1   . PHE A 1 127 ? 3.58100   18.68000 18.09400  1.000 19.37625 ? 127 PHE A CE1   1 
ATOM   1014 C CE2   . PHE A 1 127 ? 5.77900   19.54800 18.19700  1.000 18.69839 ? 127 PHE A CE2   1 
ATOM   1015 C CZ    . PHE A 1 127 ? 4.89400   18.64800 17.70600  1.000 19.12186 ? 127 PHE A CZ    1 
ATOM   1016 N N     . ILE A 1 128 ? 1.26100   24.14200 20.87300  1.000 17.35355 ? 128 ILE A N     1 
ATOM   1017 C CA    . ILE A 1 128 ? 0.69100   25.16600 21.72700  1.000 18.11076 ? 128 ILE A CA    1 
ATOM   1018 C C     . ILE A 1 128 ? -0.20700  24.50600 22.76200  1.000 17.87910 ? 128 ILE A C     1 
ATOM   1019 O O     . ILE A 1 128 ? -1.14400  23.78300 22.40300  1.000 19.48383 ? 128 ILE A O     1 
ATOM   1020 C CB    . ILE A 1 128 ? -0.10300  26.21000 20.91400  1.000 21.81329 ? 128 ILE A CB    1 
ATOM   1021 C CG1   . ILE A 1 128 ? 0.74900   26.77500 19.75800  1.000 25.09673 ? 128 ILE A CG1   1 
ATOM   1022 C CG2   . ILE A 1 128 ? -0.55000  27.32300 21.82400  1.000 24.42569 ? 128 ILE A CG2   1 
ATOM   1023 C CD1   . ILE A 1 128 ? -0.06100  27.66900 18.74900  1.000 26.34070 ? 128 ILE A CD1   1 
ATOM   1024 N N     . ARG A 1 129 ? 0.04800   24.79600 24.02800  1.000 18.99546 ? 129 ARG A N     1 
ATOM   1025 C CA    . ARG A 1 129 ? -0.76500  24.23000 25.08200  1.000 20.31028 ? 129 ARG A CA    1 
ATOM   1026 C C     . ARG A 1 129 ? -2.14900  24.87200 25.12700  1.000 18.99215 ? 129 ARG A C     1 
ATOM   1027 O O     . ARG A 1 129 ? -2.28500  26.09700 25.03200  1.000 20.26768 ? 129 ARG A O     1 
ATOM   1028 C CB    . ARG A 1 129 ? -0.05300  24.44200 26.42000  1.000 23.18235 ? 129 ARG A CB    1 
ATOM   1029 C CG    . ARG A 1 129 ? -0.74900  23.82700 27.62200  1.000 25.96340 ? 129 ARG A CG    1 
ATOM   1030 C CD    . ARG A 1 129 ? -0.35600  22.36100 27.75300  1.000 27.19538 ? 129 ARG A CD    1 
ATOM   1031 N NE    . ARG A 1 129 ? 1.08500   22.18500 27.93400  1.000 27.79817 ? 129 ARG A NE    1 
ATOM   1032 C CZ    . ARG A 1 129 ? 1.71400   21.02000 27.85200  1.000 28.23338 ? 129 ARG A CZ    1 
ATOM   1033 N NH1   . ARG A 1 129 ? 1.06800   19.90100 27.57100  1.000 28.89186 ? 129 ARG A NH1   1 
ATOM   1034 N NH2   . ARG A 1 129 ? 3.02900   20.97800 28.05600  1.000 28.23680 ? 129 ARG A NH2   1 
ATOM   1035 N N     . LEU A 1 130 ? -3.17400  24.05500 25.39500  1.000 20.54389 ? 130 LEU A N     1 
ATOM   1036 C CA    . LEU A 1 130 ? -4.51500  24.57500 25.63200  1.000 21.16721 ? 130 LEU A CA    1 
ATOM   1037 C C     . LEU A 1 130 ? -4.69300  24.96300 27.10000  1.000 22.69443 ? 130 LEU A C     1 
ATOM   1038 O O     . LEU A 1 130 ? -4.01300  24.43300 27.98300  1.000 25.23097 ? 130 LEU A O     1 
ATOM   1039 C CB    . LEU A 1 130 ? -5.59000  23.53400 25.35300  1.000 23.15433 ? 130 LEU A CB    1 
ATOM   1040 C CG    . LEU A 1 130 ? -5.64400  22.79500 24.00900  1.000 26.39716 ? 130 LEU A CG    1 
ATOM   1041 C CD1   . LEU A 1 130 ? -7.01800  22.26500 23.76300  1.000 24.74706 ? 130 LEU A CD1   1 
ATOM   1042 C CD2   . LEU A 1 130 ? -5.03000  23.49100 22.84100  1.000 27.44385 ? 130 LEU A CD2   1 
ATOM   1043 N N     . GLU A 1 131 ? -5.65800  25.85900 27.37700  1.000 23.97224 ? 131 GLU A N     1 
ATOM   1044 C CA    . GLU A 1 131 ? -5.89200  26.33200 28.74900  1.000 26.86014 ? 131 GLU A CA    1 
ATOM   1045 C C     . GLU A 1 131 ? -6.46200  25.24000 29.62200  1.000 28.94117 ? 131 GLU A C     1 
ATOM   1046 O O     . GLU A 1 131 ? -6.31700  25.28700 30.85300  1.000 31.50773 ? 131 GLU A O     1 
ATOM   1047 C CB    . GLU A 1 131 ? -6.87100  27.50700 28.72600  1.000 28.58832 ? 131 GLU A CB    1 
ATOM   1048 C CG    . GLU A 1 131 ? -6.17800  28.80500 28.31200  1.000 30.16179 ? 131 GLU A CG    1 
ATOM   1049 C CD    . GLU A 1 131 ? -7.04500  30.03500 28.38700  1.000 33.02729 ? 131 GLU A CD    1 
ATOM   1050 O OE1   . GLU A 1 131 ? -8.27500  29.92800 28.20900  1.000 34.01685 ? 131 GLU A OE1   1 
ATOM   1051 O OE2   . GLU A 1 131 ? -6.48400  31.11300 28.65200  1.000 34.03726 ? 131 GLU A OE2   1 
ATOM   1052 N N     . GLY A 1 132 ? -7.15600  24.29800 29.01600  1.000 28.51947 ? 132 GLY A N     1 
ATOM   1053 C CA    . GLY A 1 132 ? -7.67100  23.13900 29.70100  1.000 29.13917 ? 132 GLY A CA    1 
ATOM   1054 C C     . GLY A 1 132 ? -7.87200  22.09900 28.61900  1.000 29.83015 ? 132 GLY A C     1 
ATOM   1055 O O     . GLY A 1 132 ? -7.84100  22.39100 27.41900  1.000 28.85852 ? 132 GLY A O     1 
ATOM   1056 N N     . PRO A 1 133 ? -8.09700  20.85900 29.00500  1.000 31.50665 ? 133 PRO A N     1 
ATOM   1057 C CA    . PRO A 1 133 ? -8.28500  19.82500 27.98600  1.000 30.57132 ? 133 PRO A CA    1 
ATOM   1058 C C     . PRO A 1 133 ? -9.59000  20.03600 27.21300  1.000 29.37654 ? 133 PRO A C     1 
ATOM   1059 O O     . PRO A 1 133 ? -10.60400 20.45700 27.76500  1.000 28.88431 ? 133 PRO A O     1 
ATOM   1060 C CB    . PRO A 1 133 ? -8.30100  18.52900 28.80800  1.000 32.55990 ? 133 PRO A CB    1 
ATOM   1061 C CG    . PRO A 1 133 ? -8.77500  18.97900 30.18500  1.000 33.82435 ? 133 PRO A CG    1 
ATOM   1062 C CD    . PRO A 1 133 ? -8.11700  20.32000 30.37600  1.000 32.46574 ? 133 PRO A CD    1 
ATOM   1063 N N     . ALA A 1 134 ? -9.55100  19.73700 25.92100  1.000 29.11931 ? 134 ALA A N     1 
ATOM   1064 C CA    . ALA A 1 134 ? -10.75300 19.82400 25.11300  1.000 28.40920 ? 134 ALA A CA    1 
ATOM   1065 C C     . ALA A 1 134 ? -11.81800 18.88600 25.65200  1.000 28.49594 ? 134 ALA A C     1 
ATOM   1066 O O     . ALA A 1 134 ? -11.52000 17.76800 26.09200  1.000 29.07313 ? 134 ALA A O     1 
ATOM   1067 C CB    . ALA A 1 134 ? -10.41300 19.47900 23.66300  1.000 28.47602 ? 134 ALA A CB    1 
ATOM   1068 N N     . LYS A 1 135 ? -13.06700 19.36600 25.68600  1.000 28.99213 ? 135 LYS A N     1 
ATOM   1069 C CA    . LYS A 1 135 ? -14.18000 18.49700 26.03200  1.000 31.06493 ? 135 LYS A CA    1 
ATOM   1070 C C     . LYS A 1 135 ? -14.32300 17.32800 25.05400  1.000 30.96761 ? 135 LYS A C     1 
ATOM   1071 O O     . LYS A 1 135 ? -14.63700 16.20400 25.46900  1.000 31.59894 ? 135 LYS A O     1 
ATOM   1072 C CB    . LYS A 1 135 ? -15.48200 19.29800 26.21500  1.000 31.78102 ? 135 LYS A CB    1 
ATOM   1073 C CG    . LYS A 1 135 ? -16.74700 18.47600 26.31800  1.000 34.13621 ? 135 LYS A CG    1 
ATOM   1074 C CD    . LYS A 1 135 ? -17.99700 19.35700 26.25900  1.000 37.03408 ? 135 LYS A CD    1 
ATOM   1075 C CE    . LYS A 1 135 ? -19.17000 18.75600 26.99300  1.000 39.21702 ? 135 LYS A CE    1 
ATOM   1076 N NZ    . LYS A 1 135 ? -20.17700 18.26100 26.03000  1.000 40.54741 ? 135 LYS A NZ    1 
ATOM   1077 N N     . ASN A 1 136 ? -14.07900 17.56900 23.76100  1.000 31.44936 ? 136 ASN A N     1 
ATOM   1078 C CA    . ASN A 1 136 ? -14.19300 16.57200 22.68800  1.000 31.87930 ? 136 ASN A CA    1 
ATOM   1079 C C     . ASN A 1 136 ? -12.96800 16.62500 21.78700  1.000 31.17302 ? 136 ASN A C     1 
ATOM   1080 O O     . ASN A 1 136 ? -12.99700 17.25800 20.72600  1.000 31.75394 ? 136 ASN A O     1 
ATOM   1081 C CB    . ASN A 1 136 ? -15.44100 16.83700 21.85000  1.000 34.66588 ? 136 ASN A CB    1 
ATOM   1082 C CG    . ASN A 1 136 ? -16.69700 16.48400 22.56600  1.000 36.77447 ? 136 ASN A CG    1 
ATOM   1083 O OD1   . ASN A 1 136 ? -17.54000 17.33900 22.83100  1.000 37.96063 ? 136 ASN A OD1   1 
ATOM   1084 N ND2   . ASN A 1 136 ? -16.85700 15.20400 22.86800  1.000 37.13071 ? 136 ASN A ND2   1 
ATOM   1085 N N     . PRO A 1 137 ? -11.88000 15.94200 22.16700  1.000 32.86765 ? 137 PRO A N     1 
ATOM   1086 C CA    . PRO A 1 137 ? -10.66100 15.92400 21.34700  1.000 32.98635 ? 137 PRO A CA    1 
ATOM   1087 C C     . PRO A 1 137 ? -10.90400 15.09900 20.09700  1.000 32.30496 ? 137 PRO A C     1 
ATOM   1088 O O     . PRO A 1 137 ? -11.91100 14.40600 19.96200  1.000 32.80138 ? 137 PRO A O     1 
ATOM   1089 C CB    . PRO A 1 137 ? -9.63000  15.21200 22.22900  1.000 35.10109 ? 137 PRO A CB    1 
ATOM   1090 C CG    . PRO A 1 137 ? -10.34200 14.96100 23.57900  1.000 35.21790 ? 137 PRO A CG    1 
ATOM   1091 C CD    . PRO A 1 137 ? -11.80000 15.03400 23.31900  1.000 34.43535 ? 137 PRO A CD    1 
ATOM   1092 N N     . TYR A 1 138 ? -9.95000  15.18100 19.18500  1.000 33.43224 ? 138 TYR A N     1 
ATOM   1093 C CA    . TYR A 1 138 ? -10.01500 14.46700 17.92000  1.000 32.33218 ? 138 TYR A CA    1 
ATOM   1094 C C     . TYR A 1 138 ? -9.76300  12.99600 18.26200  1.000 33.21810 ? 138 TYR A C     1 
ATOM   1095 O O     . TYR A 1 138 ? -10.59200 12.12500 17.99500  1.000 34.73274 ? 138 TYR A O     1 
ATOM   1096 C CB    . TYR A 1 138 ? -8.92600  14.99600 16.99600  1.000 33.53612 ? 138 TYR A CB    1 
ATOM   1097 C CG    . TYR A 1 138 ? -8.90200  14.40200 15.61500  1.000 35.45247 ? 138 TYR A CG    1 
ATOM   1098 C CD1   . TYR A 1 138 ? -8.31500  13.16000 15.38400  1.000 35.49191 ? 138 TYR A CD1   1 
ATOM   1099 C CD2   . TYR A 1 138 ? -9.37400  15.12800 14.51700  1.000 36.69040 ? 138 TYR A CD2   1 
ATOM   1100 C CE1   . TYR A 1 138 ? -8.28100  12.60800 14.11000  1.000 38.52508 ? 138 TYR A CE1   1 
ATOM   1101 C CE2   . TYR A 1 138 ? -9.31500  14.60000 13.22500  1.000 39.33757 ? 138 TYR A CE2   1 
ATOM   1102 C CZ    . TYR A 1 138 ? -8.77200  13.33700 13.03100  1.000 41.25374 ? 138 TYR A CZ    1 
ATOM   1103 O OH    . TYR A 1 138 ? -8.72800  12.80000 11.75500  1.000 44.41494 ? 138 TYR A OH    1 
ATOM   1104 N N     . SER A 1 145 ? -4.12900  6.54300  8.63500   1.000 46.66991 ? 145 SER A N     1 
ATOM   1105 C CA    . SER A 1 145 ? -3.32300  7.50200  9.39600   1.000 39.23485 ? 145 SER A CA    1 
ATOM   1106 C C     . SER A 1 145 ? -1.83100  7.26500  9.19000   1.000 32.32686 ? 145 SER A C     1 
ATOM   1107 O O     . SER A 1 145 ? -1.02900  8.00800  9.73500   1.000 31.15735 ? 145 SER A O     1 
ATOM   1108 C CB    . SER A 1 145 ? -3.63700  7.35600  10.88000  1.000 40.77655 ? 145 SER A CB    1 
ATOM   1109 O OG    . SER A 1 145 ? -3.39000  6.00400  11.29800  1.000 42.05229 ? 145 SER A OG    1 
ATOM   1110 N N     . GLN A 1 146 ? -1.45600  6.20900  8.44700   1.000 29.12128 ? 146 GLN A N     1 
ATOM   1111 C CA    . GLN A 1 146 ? -0.07500  5.92200  8.05400   1.000 27.36499 ? 146 GLN A CA    1 
ATOM   1112 C C     . GLN A 1 146 ? 0.20100   6.15600  6.57100   1.000 26.30844 ? 146 GLN A C     1 
ATOM   1113 O O     . GLN A 1 146 ? 1.30300   5.86300  6.10400   1.000 26.86772 ? 146 GLN A O     1 
ATOM   1114 C CB    . GLN A 1 146 ? 0.29300   4.47600  8.39200   1.000 31.41952 ? 146 GLN A CB    1 
ATOM   1115 C CG    . GLN A 1 146 ? 0.24800   4.16700  9.88900   1.000 35.99974 ? 146 GLN A CG    1 
ATOM   1116 C CD    . GLN A 1 146 ? 0.18100   2.68100  10.20000  1.000 40.55109 ? 146 GLN A CD    1 
ATOM   1117 O OE1   . GLN A 1 146 ? 0.59000   1.84600  9.40400   1.000 41.79460 ? 146 GLN A OE1   1 
ATOM   1118 N NE2   . GLN A 1 146 ? -0.35800  2.35500  11.35700  1.000 42.59462 ? 146 GLN A NE2   1 
ATOM   1119 N N     . HIS A 1 147 ? -0.78200  6.60800  5.80000   1.000 24.22958 ? 147 HIS A N     1 
ATOM   1120 C CA    . HIS A 1 147 ? -0.62500  6.78400  4.36400   1.000 22.92397 ? 147 HIS A CA    1 
ATOM   1121 C C     . HIS A 1 147 ? -1.26200  8.09600  3.98000   1.000 20.89598 ? 147 HIS A C     1 
ATOM   1122 O O     . HIS A 1 147 ? -1.93800  8.73500  4.79300   1.000 21.08929 ? 147 HIS A O     1 
ATOM   1123 C CB    . HIS A 1 147 ? -1.29200  5.64500  3.59900   1.000 24.19513 ? 147 HIS A CB    1 
ATOM   1124 C CG    . HIS A 1 147 ? -0.70000  4.30900  3.92300   1.000 26.45680 ? 147 HIS A CG    1 
ATOM   1125 N ND1   . HIS A 1 147 ? 0.48700   3.87500  3.36500   1.000 28.80485 ? 147 HIS A ND1   1 
ATOM   1126 C CD2   . HIS A 1 147 ? -1.06700  3.36200  4.82100   1.000 27.89989 ? 147 HIS A CD2   1 
ATOM   1127 C CE1   . HIS A 1 147 ? 0.78700   2.68100  3.85700   1.000 30.12448 ? 147 HIS A CE1   1 
ATOM   1128 N NE2   . HIS A 1 147 ? -0.13600  2.35100  4.74700   1.000 29.74078 ? 147 HIS A NE2   1 
ATOM   1129 N N     . LEU A 1 148 ? -0.96600  8.53400  2.75400   1.000 20.10811 ? 148 LEU A N     1 
ATOM   1130 C CA    . LEU A 1 148 ? -1.56400  9.76800  2.24500   1.000 19.99683 ? 148 LEU A CA    1 
ATOM   1131 C C     . LEU A 1 148 ? -3.07500  9.68000  2.25800   1.000 19.47029 ? 148 LEU A C     1 
ATOM   1132 O O     . LEU A 1 148 ? -3.66200  8.64500  1.91100   1.000 21.69881 ? 148 LEU A O     1 
ATOM   1133 C CB    . LEU A 1 148 ? -1.19000  9.96100  0.78300   1.000 22.76489 ? 148 LEU A CB    1 
ATOM   1134 C CG    . LEU A 1 148 ? 0.16200   10.54100 0.44500   1.000 24.35873 ? 148 LEU A CG    1 
ATOM   1135 C CD1   . LEU A 1 148 ? 0.32100   10.48400 -1.04900  1.000 26.67480 ? 148 LEU A CD1   1 
ATOM   1136 C CD2   . LEU A 1 148 ? 0.30700   11.94600 0.95300   1.000 22.62883 ? 148 LEU A CD2   1 
ATOM   1137 N N     . VAL A 1 149 ? -3.71500  10.76500 2.63000   1.000 17.97998 ? 149 VAL A N     1 
ATOM   1138 C CA    . VAL A 1 149 ? -5.16700  10.88300 2.50800   1.000 18.60567 ? 149 VAL A CA    1 
ATOM   1139 C C     . VAL A 1 149 ? -5.46900  11.45500 1.13500   1.000 17.94436 ? 149 VAL A C     1 
ATOM   1140 O O     . VAL A 1 149 ? -5.04400  12.57200 0.80200   1.000 18.53806 ? 149 VAL A O     1 
ATOM   1141 C CB    . VAL A 1 149 ? -5.75300  11.78100 3.59400   1.000 21.39518 ? 149 VAL A CB    1 
ATOM   1142 C CG1   . VAL A 1 149 ? -7.22000  11.99600 3.35600   1.000 21.79205 ? 149 VAL A CG1   1 
ATOM   1143 C CG2   . VAL A 1 149 ? -5.48200  11.13700 4.94900   1.000 24.91463 ? 149 VAL A CG2   1 
ATOM   1144 N N     . LEU A 1 150 ? -6.16000  10.69200 0.33500   1.000 18.13389 ? 150 LEU A N     1 
ATOM   1145 C CA    . LEU A 1 150 ? -6.41800  11.01500 -1.05500  1.000 21.33184 ? 150 LEU A CA    1 
ATOM   1146 C C     . LEU A 1 150 ? -7.88900  11.28600 -1.35300  1.000 23.01574 ? 150 LEU A C     1 
ATOM   1147 O O     . LEU A 1 150 ? -8.24600  11.36700 -2.52000  1.000 24.80173 ? 150 LEU A O     1 
ATOM   1148 C CB    . LEU A 1 150 ? -5.91000  9.87800  -1.93100  1.000 23.24328 ? 150 LEU A CB    1 
ATOM   1149 C CG    . LEU A 1 150 ? -4.38900  9.69800  -1.87300  1.000 24.15295 ? 150 LEU A CG    1 
ATOM   1150 C CD1   . LEU A 1 150 ? -4.09100  8.59400  -2.85600  1.000 26.29880 ? 150 LEU A CD1   1 
ATOM   1151 C CD2   . LEU A 1 150 ? -3.66500  10.97600 -2.21700  1.000 25.76270 ? 150 LEU A CD2   1 
ATOM   1152 N N     . SER A 1 151 ? -8.74800  11.36900 -0.33900  1.000 22.06888 ? 151 SER A N     1 
ATOM   1153 C CA    . SER A 1 151 ? -10.15700 11.64500 -0.56100  1.000 22.91870 ? 151 SER A CA    1 
ATOM   1154 C C     . SER A 1 151 ? -10.33600 13.12800 -0.87900  1.000 23.87317 ? 151 SER A C     1 
ATOM   1155 O O     . SER A 1 151 ? -9.48000  13.97500 -0.58700  1.000 26.48589 ? 151 SER A O     1 
ATOM   1156 C CB    . SER A 1 151 ? -10.91600 11.31100 0.71600   1.000 26.09512 ? 151 SER A CB    1 
ATOM   1157 O OG    . SER A 1 151 ? -10.37600 12.16100 1.72200   1.000 29.64187 ? 151 SER A OG    1 
ATOM   1158 N N     . LYS A 1 152 ? -11.45500 13.43100 -1.51300  1.000 24.34498 ? 152 LYS A N     1 
ATOM   1159 C CA    . LYS A 1 152 ? -11.89000 14.80700 -1.69100  1.000 27.05968 ? 152 LYS A CA    1 
ATOM   1160 C C     . LYS A 1 152 ? -13.34000 14.90200 -1.25600  1.000 27.18787 ? 152 LYS A C     1 
ATOM   1161 O O     . LYS A 1 152 ? -14.04000 13.89300 -1.11700  1.000 26.72422 ? 152 LYS A O     1 
ATOM   1162 C CB    . LYS A 1 152 ? -11.67000 15.31100 -3.13400  1.000 30.57160 ? 152 LYS A CB    1 
ATOM   1163 C CG    . LYS A 1 152 ? -12.50300 14.64100 -4.18800  1.000 32.83086 ? 152 LYS A CG    1 
ATOM   1164 C CD    . LYS A 1 152 ? -12.24100 15.22500 -5.58100  1.000 34.19412 ? 152 LYS A CD    1 
ATOM   1165 N N     . ARG A 1 153 ? -13.80100 16.12100 -1.03200  1.000 29.22463 ? 153 ARG A N     1 
ATOM   1166 C CA    . ARG A 1 153 ? -15.21000 16.28800 -0.67300  1.000 30.94343 ? 153 ARG A CA    1 
ATOM   1167 C C     . ARG A 1 153 ? -16.15200 15.80100 -1.77800  1.000 33.94805 ? 153 ARG A C     1 
ATOM   1168 O O     . ARG A 1 153 ? -15.86700 15.99900 -2.95700  1.000 35.44311 ? 153 ARG A O     1 
ATOM   1169 C CB    . ARG A 1 153 ? -15.51700 17.75200 -0.35500  1.000 28.32898 ? 153 ARG A CB    1 
ATOM   1170 C CG    . ARG A 1 153 ? -14.66200 18.38400 0.68900   1.000 24.39812 ? 153 ARG A CG    1 
ATOM   1171 C CD    . ARG A 1 153 ? -14.75000 19.90900 0.53600   1.000 23.65375 ? 153 ARG A CD    1 
ATOM   1172 N NE    . ARG A 1 153 ? -14.22200 20.33100 -0.76100  1.000 23.32616 ? 153 ARG A NE    1 
ATOM   1173 C CZ    . ARG A 1 153 ? -14.77100 21.26500 -1.53600  1.000 21.82457 ? 153 ARG A CZ    1 
ATOM   1174 N NH1   . ARG A 1 153 ? -15.76400 22.00300 -1.10900  1.000 21.74413 ? 153 ARG A NH1   1 
ATOM   1175 N NH2   . ARG A 1 153 ? -14.25900 21.49400 -2.74400  1.000 22.25886 ? 153 ARG A NH2   1 
HETATM 1176 C C1    . GOL B 2 .   ? 17.63300  7.13900  -4.25800  1.000 52.19714 ? 201 GOL A C1    1 
HETATM 1177 O O1    . GOL B 2 .   ? 18.61100  8.03100  -3.78200  1.000 53.36914 ? 201 GOL A O1    1 
HETATM 1178 C C2    . GOL B 2 .   ? 17.56400  7.15900  -5.80400  1.000 53.32643 ? 201 GOL A C2    1 
HETATM 1179 O O2    . GOL B 2 .   ? 18.78100  7.00800  -6.40700  1.000 54.12950 ? 201 GOL A O2    1 
HETATM 1180 C C3    . GOL B 2 .   ? 16.58500  6.02800  -6.16800  1.000 51.88557 ? 201 GOL A C3    1 
HETATM 1181 O O3    . GOL B 2 .   ? 16.99400  5.55900  -7.41200  1.000 53.48871 ? 201 GOL A O3    1 
HETATM 1182 N N1    . UMP C 3 .   ? -3.59600  17.27500 9.29600   1.000 21.84959 ? 202 UMP A N1    1 
HETATM 1183 C C2    . UMP C 3 .   ? -3.02000  16.87500 8.10300   1.000 22.97778 ? 202 UMP A C2    1 
HETATM 1184 N N3    . UMP C 3 .   ? -2.48200  17.89800 7.35400   1.000 21.12188 ? 202 UMP A N3    1 
HETATM 1185 C C4    . UMP C 3 .   ? -2.45700  19.24700 7.68100   1.000 20.44569 ? 202 UMP A C4    1 
HETATM 1186 C C5    . UMP C 3 .   ? -3.05800  19.56500 8.93500   1.000 20.82323 ? 202 UMP A C5    1 
HETATM 1187 C C6    . UMP C 3 .   ? -3.61800  18.59900 9.66900   1.000 22.32159 ? 202 UMP A C6    1 
HETATM 1188 O O2    . UMP C 3 .   ? -2.97400  15.70600 7.74000   1.000 22.99076 ? 202 UMP A O2    1 
HETATM 1189 O O4    . UMP C 3 .   ? -1.98400  20.06300 6.88400   1.000 17.97659 ? 202 UMP A O4    1 
HETATM 1190 C "C1'" . UMP C 3 .   ? -4.26600  16.26700 10.13100  1.000 22.65026 ? 202 UMP A "C1'" 1 
HETATM 1191 C "C2'" . UMP C 3 .   ? -4.27800  16.59000 11.63100  1.000 22.38995 ? 202 UMP A "C2'" 1 
HETATM 1192 C "C3'" . UMP C 3 .   ? -5.65100  17.20300 11.84400  1.000 22.69732 ? 202 UMP A "C3'" 1 
HETATM 1193 C "C4'" . UMP C 3 .   ? -6.50300  16.42300 10.85300  1.000 25.89228 ? 202 UMP A "C4'" 1 
HETATM 1194 O "O3'" . UMP C 3 .   ? -6.14000  17.03900 13.17900  1.000 23.64497 ? 202 UMP A "O3'" 1 
HETATM 1195 O "O4'" . UMP C 3 .   ? -5.63300  16.22100 9.71700   1.000 23.61144 ? 202 UMP A "O4'" 1 
HETATM 1196 C "C5'" . UMP C 3 .   ? -7.77600  17.10800 10.41600  1.000 32.19391 ? 202 UMP A "C5'" 1 
HETATM 1197 O "O5'" . UMP C 3 .   ? -8.50500  16.23500 9.53400   1.000 34.61813 ? 202 UMP A "O5'" 1 
HETATM 1198 P P     . UMP C 3 .   ? -10.09100 16.32100 9.41300   1.000 40.41623 ? 202 UMP A P     1 
HETATM 1199 O OP1   . UMP C 3 .   ? -10.49300 15.41700 8.15200   1.000 42.68416 ? 202 UMP A OP1   1 
HETATM 1200 O OP2   . UMP C 3 .   ? -10.73700 16.01200 10.84600  1.000 44.30063 ? 202 UMP A OP2   1 
HETATM 1201 O OP3   . UMP C 3 .   ? -10.36700 17.85500 9.03500   1.000 41.95796 ? 202 UMP A OP3   1 
HETATM 1202 P P     . PO4 D 4 .   ? -7.11400  14.30100 -8.94300  1.000 73.60630 ? 203 PO4 A P     1 
HETATM 1203 O O1    . PO4 D 4 .   ? -5.92100  14.33800 -9.86400  1.000 73.04296 ? 203 PO4 A O1    1 
HETATM 1204 O O2    . PO4 D 4 .   ? -7.81700  15.63400 -9.04000  1.000 73.23377 ? 203 PO4 A O2    1 
HETATM 1205 O O3    . PO4 D 4 .   ? -8.03100  13.16600 -9.35900  1.000 73.41991 ? 203 PO4 A O3    1 
HETATM 1206 O O4    . PO4 D 4 .   ? -6.66700  14.08900 -7.51800  1.000 73.14582 ? 203 PO4 A O4    1 
HETATM 1207 P P     . PO4 E 4 .   ? 20.42400  17.61600 7.40500   1.000 78.29791 ? 204 PO4 A P     1 
HETATM 1208 O O1    . PO4 E 4 .   ? 21.55100  17.45100 8.39700   1.000 78.04333 ? 204 PO4 A O1    1 
HETATM 1209 O O2    . PO4 E 4 .   ? 20.47700  19.01500 6.82000   1.000 77.98150 ? 204 PO4 A O2    1 
HETATM 1210 O O3    . PO4 E 4 .   ? 20.58400  16.58700 6.30400   1.000 77.73273 ? 204 PO4 A O3    1 
HETATM 1211 O O4    . PO4 E 4 .   ? 19.10100  17.37100 8.10400   1.000 78.15807 ? 204 PO4 A O4    1 
HETATM 1212 O O     . HOH F 5 .   ? 10.49900  11.21800 -7.82400  1.000 24.73715 ? 301 HOH A O     1 
HETATM 1213 O O     . HOH F 5 .   ? 16.85600  27.48000 0.06500   1.000 49.46830 ? 302 HOH A O     1 
HETATM 1214 O O     . HOH F 5 .   ? 14.90700  24.76100 -5.80400  1.000 37.40579 ? 303 HOH A O     1 
HETATM 1215 O O     . HOH F 5 .   ? 18.36400  15.47900 9.46400   1.000 40.95842 ? 304 HOH A O     1 
HETATM 1216 O O     . HOH F 5 .   ? 8.61700   30.19000 -17.33000 1.000 41.74270 ? 305 HOH A O     1 
HETATM 1217 O O     . HOH F 5 .   ? 6.95800   6.16200  -7.84400  1.000 32.50057 ? 306 HOH A O     1 
HETATM 1218 O O     . HOH F 5 .   ? -3.40600  4.52000  7.24200   1.000 45.24255 ? 307 HOH A O     1 
HETATM 1219 O O     . HOH F 5 .   ? 1.41400   28.30100 11.20400  1.000 37.80175 ? 308 HOH A O     1 
HETATM 1220 O O     . HOH F 5 .   ? 15.25300  6.78200  -0.55800  1.000 42.25101 ? 309 HOH A O     1 
HETATM 1221 O O     . HOH F 5 .   ? 13.26400  24.56400 11.19600  1.000 27.21502 ? 310 HOH A O     1 
HETATM 1222 O O     . HOH F 5 .   ? 0.00000   30.37786 14.15900  0.33  23.20260 ? 311 HOH A O     1 
HETATM 1223 O O     . HOH F 5 .   ? -3.15000  11.78100 22.51000  1.000 39.97223 ? 312 HOH A O     1 
HETATM 1224 O O     . HOH F 5 .   ? -14.56500 17.99400 -4.08700  1.000 39.86432 ? 313 HOH A O     1 
HETATM 1225 O O     . HOH F 5 .   ? -5.13400  4.39400  10.14000  1.000 50.58904 ? 314 HOH A O     1 
HETATM 1226 O O     . HOH F 5 .   ? -3.32400  6.29600  0.72300   1.000 57.34363 ? 315 HOH A O     1 
HETATM 1227 O O     . HOH F 5 .   ? 15.18200  21.41800 3.76300   1.000 38.80297 ? 316 HOH A O     1 
HETATM 1228 O O     . HOH F 5 .   ? -0.29100  16.97400 28.06000  1.000 40.10074 ? 317 HOH A O     1 
HETATM 1229 O O     . HOH F 5 .   ? 17.54500  10.08400 12.55200  1.000 44.59427 ? 318 HOH A O     1 
HETATM 1230 O O     . HOH F 5 .   ? -7.57700  20.43600 11.52300  1.000 24.27912 ? 319 HOH A O     1 
HETATM 1231 O O     . HOH F 5 .   ? 1.99900   20.16400 -13.44100 1.000 27.10948 ? 320 HOH A O     1 
HETATM 1232 O O     . HOH F 5 .   ? 3.75000   5.57600  10.65400  1.000 35.98208 ? 321 HOH A O     1 
HETATM 1233 O O     . HOH F 5 .   ? 6.90300   15.30400 -10.44400 1.000 31.51199 ? 322 HOH A O     1 
HETATM 1234 O O     . HOH F 5 .   ? -2.17300  11.43900 6.53200   1.000 27.57529 ? 323 HOH A O     1 
HETATM 1235 O O     . HOH F 5 .   ? 17.30500  13.16300 3.47400   1.000 38.05289 ? 324 HOH A O     1 
HETATM 1236 O O     . HOH F 5 .   ? -1.97900  20.31900 4.09100   1.000 17.15948 ? 325 HOH A O     1 
HETATM 1237 O O     . HOH F 5 .   ? 15.20000  22.06600 -9.02500  1.000 34.09089 ? 326 HOH A O     1 
HETATM 1238 O O     . HOH F 5 .   ? 9.40900   13.43000 20.93300  1.000 44.73356 ? 327 HOH A O     1 
HETATM 1239 O O     . HOH F 5 .   ? 12.42400  27.83300 -7.63800  1.000 29.26689 ? 328 HOH A O     1 
HETATM 1240 O O     . HOH F 5 .   ? -0.84200  23.22100 11.83900  1.000 21.15877 ? 329 HOH A O     1 
HETATM 1241 O O     . HOH F 5 .   ? -6.13500  15.51800 7.11900   1.000 42.47959 ? 330 HOH A O     1 
HETATM 1242 O O     . HOH F 5 .   ? -10.67400 15.40600 27.19200  1.000 48.16706 ? 331 HOH A O     1 
HETATM 1243 O O     . HOH F 5 .   ? -3.99900  21.28000 30.25200  1.000 45.49652 ? 332 HOH A O     1 
HETATM 1244 O O     . HOH F 5 .   ? -5.19200  6.78800  3.24500   1.000 37.97493 ? 333 HOH A O     1 
HETATM 1245 O O     . HOH F 5 .   ? 15.55400  26.31500 6.02300   1.000 37.75580 ? 334 HOH A O     1 
HETATM 1246 O O     . HOH F 5 .   ? 2.35800   13.04900 26.59100  1.000 38.78789 ? 335 HOH A O     1 
HETATM 1247 O O     . HOH F 5 .   ? -1.13600  17.89300 -7.92700  1.000 22.99044 ? 336 HOH A O     1 
HETATM 1248 O O     . HOH F 5 .   ? 11.82700  26.56800 17.00900  1.000 21.87081 ? 337 HOH A O     1 
HETATM 1249 O O     . HOH F 5 .   ? 3.87800   19.78900 31.09000  1.000 52.21026 ? 338 HOH A O     1 
HETATM 1250 O O     . HOH F 5 .   ? 6.45500   24.05000 20.25000  1.000 22.70032 ? 339 HOH A O     1 
HETATM 1251 O O     . HOH F 5 .   ? 7.77500   6.25600  8.91800   1.000 41.73444 ? 340 HOH A O     1 
HETATM 1252 O O     . HOH F 5 .   ? 10.47800  28.07300 -16.57400 1.000 26.92443 ? 341 HOH A O     1 
HETATM 1253 O O     . HOH F 5 .   ? 8.10500   2.14400  -0.48900  1.000 32.51710 ? 342 HOH A O     1 
HETATM 1254 O O     . HOH F 5 .   ? 4.43600   23.16900 -14.82200 1.000 37.39821 ? 343 HOH A O     1 
HETATM 1255 O O     . HOH F 5 .   ? -4.67500  10.34700 20.42500  1.000 43.40245 ? 344 HOH A O     1 
HETATM 1256 O O     . HOH F 5 .   ? 1.79900   12.44600 22.83500  1.000 33.46687 ? 345 HOH A O     1 
HETATM 1257 O O     . HOH F 5 .   ? -9.95400  12.06600 -4.62500  1.000 46.63682 ? 346 HOH A O     1 
HETATM 1258 O O     . HOH F 5 .   ? 16.46800  11.97700 7.65600   1.000 38.49397 ? 347 HOH A O     1 
HETATM 1259 O O     . HOH F 5 .   ? 2.87300   13.18800 -11.39900 1.000 33.75911 ? 348 HOH A O     1 
HETATM 1260 O O     . HOH F 5 .   ? -1.82300  16.51100 -5.61000  1.000 27.89505 ? 349 HOH A O     1 
HETATM 1261 O O     . HOH F 5 .   ? 14.15500  11.76000 22.63900  1.000 56.74789 ? 350 HOH A O     1 
HETATM 1262 O O     . HOH F 5 .   ? -14.80300 15.52300 28.20500  1.000 36.09374 ? 351 HOH A O     1 
HETATM 1263 O O     . HOH F 5 .   ? -4.56400  13.40800 7.28400   1.000 43.01382 ? 352 HOH A O     1 
HETATM 1264 O O     A HOH F 5 .   ? -6.63900  10.15700 17.14000  0.600 27.20260 ? 353 HOH A O     1 
HETATM 1265 O O     B HOH F 5 .   ? -5.93300  10.41700 14.76800  0.400 27.24363 ? 353 HOH A O     1 
HETATM 1266 O O     . HOH F 5 .   ? -4.00500  13.35300 26.21300  1.000 44.90318 ? 354 HOH A O     1 
HETATM 1267 O O     . HOH F 5 .   ? 17.18600  17.67300 6.01500   1.000 28.00186 ? 355 HOH A O     1 
HETATM 1268 O O     . HOH F 5 .   ? -3.02400  23.95000 30.61200  1.000 44.01851 ? 356 HOH A O     1 
HETATM 1269 O O     . HOH F 5 .   ? 13.88000  25.57600 -8.09100  1.000 26.72477 ? 357 HOH A O     1 
HETATM 1270 O O     . HOH F 5 .   ? -3.58100  3.15100  11.44600  1.000 44.04012 ? 358 HOH A O     1 
HETATM 1271 O O     . HOH F 5 .   ? 8.00300   11.43200 23.52300  1.000 48.71876 ? 359 HOH A O     1 
HETATM 1272 O O     . HOH F 5 .   ? 18.76700  11.15900 15.44800  1.000 42.84770 ? 360 HOH A O     1 
HETATM 1273 O O     . HOH F 5 .   ? 19.27000  12.71400 22.84500  1.000 52.24997 ? 361 HOH A O     1 
HETATM 1274 O O     . HOH F 5 .   ? 0.81700   6.70800  12.08000  1.000 41.25640 ? 362 HOH A O     1 
HETATM 1275 O O     . HOH F 5 .   ? 4.52800   8.49600  -10.23300 1.000 41.90234 ? 363 HOH A O     1 
HETATM 1276 O O     . HOH F 5 .   ? 4.17900   28.61600 3.37900   1.000 15.09904 ? 364 HOH A O     1 
HETATM 1277 O O     . HOH F 5 .   ? 15.19800  21.95200 -6.19600  1.000 27.27854 ? 365 HOH A O     1 
HETATM 1278 O O     . HOH F 5 .   ? 15.46100  19.93800 -10.91800 1.000 39.14329 ? 366 HOH A O     1 
HETATM 1279 O O     . HOH F 5 .   ? 7.37200   32.79200 -9.01400  1.000 28.66259 ? 367 HOH A O     1 
HETATM 1280 O O     . HOH F 5 .   ? 14.72900  26.24200 13.22800  1.000 41.93712 ? 368 HOH A O     1 
HETATM 1281 O O     . HOH F 5 .   ? 8.77100   13.26100 -8.25300  1.000 33.36800 ? 369 HOH A O     1 
HETATM 1282 O O     . HOH F 5 .   ? 19.62600  13.52300 13.58700  1.000 35.41671 ? 370 HOH A O     1 
HETATM 1283 O O     . HOH F 5 .   ? 4.63500   28.28200 6.12500   1.000 15.37176 ? 371 HOH A O     1 
HETATM 1284 O O     . HOH F 5 .   ? -12.88900 11.06000 -2.41700  1.000 30.59947 ? 372 HOH A O     1 
HETATM 1285 O O     . HOH F 5 .   ? -3.62300  15.40300 -8.16000  1.000 34.32737 ? 373 HOH A O     1 
HETATM 1286 O O     . HOH F 5 .   ? -7.50400  23.95300 10.07500  1.000 17.21277 ? 374 HOH A O     1 
HETATM 1287 O O     . HOH F 5 .   ? 14.91400  8.69000  11.76600  1.000 39.63624 ? 375 HOH A O     1 
HETATM 1288 O O     . HOH F 5 .   ? 6.07500   8.33100  5.39500   1.000 19.74745 ? 376 HOH A O     1 
HETATM 1289 O O     . HOH F 5 .   ? 15.59500  18.38900 24.55100  1.000 29.32652 ? 377 HOH A O     1 
HETATM 1290 O O     . HOH F 5 .   ? 11.94100  32.07600 4.43700   1.000 34.77408 ? 378 HOH A O     1 
HETATM 1291 O O     . HOH F 5 .   ? 6.05800   4.33600  -0.40700  1.000 34.63244 ? 379 HOH A O     1 
HETATM 1292 O O     . HOH F 5 .   ? 8.89500   10.39400 20.32500  1.000 38.75327 ? 380 HOH A O     1 
HETATM 1293 O O     . HOH F 5 .   ? 16.99800  10.52200 -5.72100  1.000 38.01226 ? 381 HOH A O     1 
HETATM 1294 O O     . HOH F 5 .   ? -0.59700  6.66900  -9.54600  1.000 38.94496 ? 382 HOH A O     1 
HETATM 1295 O O     . HOH F 5 .   ? 11.73000  7.02900  17.18200  1.000 43.16036 ? 383 HOH A O     1 
HETATM 1296 O O     . HOH F 5 .   ? -4.48700  16.48200 4.92200   1.000 35.90715 ? 384 HOH A O     1 
HETATM 1297 O O     . HOH F 5 .   ? -0.08900  23.08900 -12.86600 1.000 46.04116 ? 385 HOH A O     1 
HETATM 1298 O O     . HOH F 5 .   ? -10.63800 11.01900 4.46800   1.000 45.73275 ? 386 HOH A O     1 
HETATM 1299 O O     . HOH F 5 .   ? -0.48900  27.33600 5.66100   1.000 27.59376 ? 387 HOH A O     1 
HETATM 1300 O O     . HOH F 5 .   ? -1.36100  29.29900 3.01900   1.000 39.60811 ? 388 HOH A O     1 
HETATM 1301 O O     . HOH F 5 .   ? -6.45500  6.68800  12.22200  1.000 49.49541 ? 389 HOH A O     1 
HETATM 1302 O O     . HOH F 5 .   ? 11.98300  26.82200 10.20900  1.000 45.23550 ? 390 HOH A O     1 
HETATM 1303 O O     . HOH F 5 .   ? 12.77600  11.25200 -9.19900  1.000 41.82972 ? 391 HOH A O     1 
HETATM 1304 O O     . HOH F 5 .   ? -7.44800  9.51200  12.12400  1.000 41.40562 ? 392 HOH A O     1 
HETATM 1305 O O     . HOH F 5 .   ? 4.50700   15.49000 -11.78200 1.000 35.60573 ? 393 HOH A O     1 
HETATM 1306 O O     . HOH F 5 .   ? 12.83500  29.10600 -15.99400 1.000 29.19492 ? 394 HOH A O     1 
HETATM 1307 O O     . HOH F 5 .   ? 17.45400  21.23100 -4.89200  1.000 42.36473 ? 395 HOH A O     1 
HETATM 1308 O O     . HOH F 5 .   ? 8.62500   16.03700 -12.46000 1.000 42.42533 ? 396 HOH A O     1 
HETATM 1309 O O     . HOH F 5 .   ? 2.09900   29.12500 6.63900   1.000 31.94348 ? 397 HOH A O     1 
HETATM 1310 O O     . HOH F 5 .   ? 17.41800  23.40600 -9.30300  1.000 41.93659 ? 398 HOH A O     1 
HETATM 1311 O O     . HOH F 5 .   ? 7.14600   12.53400 -10.50600 1.000 41.55868 ? 399 HOH A O     1 
HETATM 1312 O O     . HOH F 5 .   ? 4.66600   11.28400 -11.32100 1.000 41.41048 ? 400 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     . MET A 1   ? 0.46632 0.48178 0.36025 0.09658  0.02401  -0.04894 1   MET A N     
2    C CA    . MET A 1   ? 0.45350 0.42537 0.33240 0.06592  0.00481  -0.03485 1   MET A CA    
3    C C     . MET A 1   ? 0.39716 0.33617 0.28454 0.03555  -0.02299 -0.01584 1   MET A C     
4    O O     . MET A 1   ? 0.41216 0.37471 0.30053 0.01001  -0.02362 -0.03913 1   MET A O     
5    C CB    . MET A 1   ? 0.52447 0.53144 0.34599 0.10282  0.00448  -0.04822 1   MET A CB    
6    C CG    . MET A 1   ? 0.59339 0.60443 0.36096 0.13865  -0.00183 -0.04694 1   MET A CG    
7    S SD    . MET A 1   ? 0.65697 0.68368 0.39431 0.14779  -0.01978 -0.06249 1   MET A SD    
8    C CE    . MET A 1   ? 0.66249 0.69244 0.40139 0.12648  0.00657  -0.05191 1   MET A CE    
9    N N     . MET A 2   ? 0.32052 0.25107 0.22743 0.03715  -0.04210 0.00893  2   MET A N     
10   C CA    A MET A 2   ? 0.30729 0.22478 0.18804 0.00848  -0.05840 0.00648  2   MET A CA    
11   C CA    B MET A 2   ? 0.31956 0.27390 0.22170 0.04351  -0.05655 0.01590  2   MET A CA    
12   C C     . MET A 2   ? 0.30525 0.25980 0.18658 0.00698  -0.07136 0.00498  2   MET A C     
13   O O     . MET A 2   ? 0.35097 0.27091 0.18724 0.00607  -0.07561 0.00372  2   MET A O     
14   C CB    A MET A 2   ? 0.32226 0.21565 0.16879 -0.01937 -0.05232 0.00179  2   MET A CB    
15   C CB    B MET A 2   ? 0.35551 0.35180 0.26624 0.04341  -0.04959 0.02318  2   MET A CB    
16   C CG    A MET A 2   ? 0.33101 0.21369 0.15481 -0.03237 -0.02948 0.01309  2   MET A CG    
17   C CG    B MET A 2   ? 0.37790 0.44401 0.30623 0.04754  -0.04597 0.03451  2   MET A CG    
18   S SD    A MET A 2   ? 0.32176 0.26974 0.15577 -0.02778 -0.02247 0.01521  2   MET A SD    
19   S SD    B MET A 2   ? 0.40892 0.54434 0.34156 0.09165  -0.07757 0.07626  2   MET A SD    
20   C CE    A MET A 2   ? 0.33970 0.35164 0.18534 -0.02532 0.03254  0.03888  2   MET A CE    
21   C CE    B MET A 2   ? 0.41282 0.52175 0.34321 0.09254  -0.08807 0.08139  2   MET A CE    
22   N N     . LEU A 3   ? 0.29048 0.28182 0.16190 0.02064  -0.06452 0.02741  3   LEU A N     
23   C CA    . LEU A 3   ? 0.28247 0.30087 0.17251 0.02325  -0.07248 0.04519  3   LEU A CA    
24   C C     . LEU A 3   ? 0.28907 0.29169 0.15646 0.01964  -0.07635 0.03910  3   LEU A C     
25   O O     . LEU A 3   ? 0.30049 0.30863 0.15531 0.01596  -0.09327 0.02697  3   LEU A O     
26   C CB    . LEU A 3   ? 0.28639 0.29704 0.19256 -0.00493 -0.06313 0.04280  3   LEU A CB    
27   C CG    . LEU A 3   ? 0.31823 0.30747 0.21698 0.01521  -0.04290 0.04514  3   LEU A CG    
28   C CD1   . LEU A 3   ? 0.32537 0.31438 0.20735 0.01303  -0.05728 0.03933  3   LEU A CD1   
29   C CD2   . LEU A 3   ? 0.32645 0.29618 0.22724 0.02171  -0.04737 0.02557  3   LEU A CD2   
30   N N     . PRO A 4   ? 0.30948 0.33173 0.16586 0.03279  -0.07177 0.04516  4   PRO A N     
31   C CA    . PRO A 4   ? 0.28883 0.30640 0.18319 0.02460  -0.07530 0.00641  4   PRO A CA    
32   C C     . PRO A 4   ? 0.28483 0.27186 0.20190 0.02453  -0.07868 0.01665  4   PRO A C     
33   O O     . PRO A 4   ? 0.26614 0.27632 0.21611 0.01990  -0.06340 0.03569  4   PRO A O     
34   C CB    . PRO A 4   ? 0.30609 0.31743 0.18232 0.02880  -0.08389 -0.00698 4   PRO A CB    
35   C CG    . PRO A 4   ? 0.29171 0.34932 0.17548 0.04323  -0.08495 0.01516  4   PRO A CG    
36   C CD    . PRO A 4   ? 0.30308 0.32763 0.16252 0.04226  -0.08354 0.01837  4   PRO A CD    
37   N N     . ASP A 5   ? 0.28113 0.28613 0.20624 0.04019  -0.07056 0.01107  5   ASP A N     
38   C CA    . ASP A 5   ? 0.28294 0.30581 0.21858 0.02718  -0.07059 0.00927  5   ASP A CA    
39   C C     . ASP A 5   ? 0.28962 0.26972 0.21420 0.00317  -0.08100 -0.00001 5   ASP A C     
40   O O     . ASP A 5   ? 0.31378 0.29524 0.23467 0.00819  -0.07710 0.01019  5   ASP A O     
41   C CB    . ASP A 5   ? 0.26670 0.34544 0.22581 0.01662  -0.07014 0.03184  5   ASP A CB    
42   C CG    . ASP A 5   ? 0.29141 0.39111 0.24416 0.00210  -0.04706 0.00759  5   ASP A CG    
43   O OD1   . ASP A 5   ? 0.29463 0.37624 0.23696 -0.02443 -0.06566 -0.01566 5   ASP A OD1   
44   O OD2   . ASP A 5   ? 0.31799 0.44030 0.25009 -0.01547 -0.06126 -0.02161 5   ASP A OD2   
45   N N     . TRP A 6   ? 0.28962 0.30326 0.19150 0.04191  -0.09028 0.00998  6   TRP A N     
46   C CA    . TRP A 6   ? 0.33283 0.28930 0.20763 0.04833  -0.09288 0.02211  6   TRP A CA    
47   C C     . TRP A 6   ? 0.34116 0.29935 0.22647 0.03285  -0.08900 0.03265  6   TRP A C     
48   O O     . TRP A 6   ? 0.36756 0.30485 0.26530 0.04854  -0.07364 0.03780  6   TRP A O     
49   C CB    . TRP A 6   ? 0.35621 0.30708 0.21117 0.07303  -0.08342 0.00597  6   TRP A CB    
50   C CG    . TRP A 6   ? 0.31237 0.33862 0.20928 0.07697  -0.10940 0.01638  6   TRP A CG    
51   C CD1   . TRP A 6   ? 0.32877 0.32675 0.20572 0.06016  -0.10981 -0.00966 6   TRP A CD1   
52   C CD2   . TRP A 6   ? 0.30983 0.41216 0.20606 0.05863  -0.12358 0.01092  6   TRP A CD2   
53   N NE1   . TRP A 6   ? 0.31736 0.37024 0.20489 0.06861  -0.10583 0.01460  6   TRP A NE1   
54   C CE2   . TRP A 6   ? 0.30817 0.40156 0.20535 0.04666  -0.11491 0.01022  6   TRP A CE2   
55   C CE3   . TRP A 6   ? 0.30697 0.43474 0.21763 0.04852  -0.11783 0.00533  6   TRP A CE3   
56   C CZ2   . TRP A 6   ? 0.31586 0.43728 0.23542 0.03671  -0.09900 0.02247  6   TRP A CZ2   
57   C CZ3   . TRP A 6   ? 0.32157 0.44552 0.24478 0.05170  -0.10100 0.01823  6   TRP A CZ3   
58   C CH2   . TRP A 6   ? 0.34520 0.48293 0.25801 0.05025  -0.08908 0.01678  6   TRP A CH2   
59   N N     . LYS A 7   ? 0.31914 0.28235 0.21724 0.00850  -0.09608 0.02676  7   LYS A N     
60   C CA    . LYS A 7   ? 0.33895 0.30155 0.23187 0.01516  -0.08263 0.04218  7   LYS A CA    
61   C C     . LYS A 7   ? 0.34270 0.29837 0.23065 0.00295  -0.07814 0.04808  7   LYS A C     
62   O O     . LYS A 7   ? 0.34575 0.33535 0.23225 -0.00006 -0.05666 0.03639  7   LYS A O     
63   C CB    . LYS A 7   ? 0.39452 0.37699 0.26142 0.08231  -0.07630 0.03245  7   LYS A CB    
64   C CG    . LYS A 7   ? 0.44306 0.47039 0.28808 0.11999  -0.06484 0.00804  7   LYS A CG    
65   C CD    . LYS A 7   ? 0.47609 0.52370 0.29387 0.10902  -0.06513 0.03052  7   LYS A CD    
66   C CE    . LYS A 7   ? 0.50963 0.55428 0.29652 0.09130  -0.05981 0.04573  7   LYS A CE    
67   N NZ    . LYS A 7   ? 0.53646 0.56687 0.31887 0.11494  -0.03169 0.04643  7   LYS A NZ    
68   N N     . ILE A 8   ? 0.35114 0.29488 0.20620 -0.00029 -0.10298 0.04388  8   ILE A N     
69   C CA    . ILE A 8   ? 0.36645 0.25196 0.21314 -0.01448 -0.07710 0.04822  8   ILE A CA    
70   C C     . ILE A 8   ? 0.39105 0.27013 0.23325 -0.01425 -0.08641 0.03425  8   ILE A C     
71   O O     . ILE A 8   ? 0.42017 0.25181 0.23673 -0.02688 -0.07037 0.05605  8   ILE A O     
72   C CB    . ILE A 8   ? 0.32893 0.25382 0.19373 -0.02371 -0.07296 0.03702  8   ILE A CB    
73   C CG1   . ILE A 8   ? 0.30381 0.27357 0.19727 -0.01934 -0.05434 0.05071  8   ILE A CG1   
74   C CG2   . ILE A 8   ? 0.34726 0.28524 0.20310 -0.01791 -0.06651 0.01878  8   ILE A CG2   
75   C CD1   . ILE A 8   ? 0.30586 0.27987 0.17847 0.00829  -0.05297 0.03796  8   ILE A CD1   
76   N N     . ARG A 9   ? 0.42488 0.30536 0.25060 0.05363  -0.09425 0.02348  9   ARG A N     
77   C CA    . ARG A 9   ? 0.47112 0.34875 0.28604 0.08255  -0.10061 0.05213  9   ARG A CA    
78   C C     . ARG A 9   ? 0.51688 0.39114 0.30822 0.08925  -0.07409 0.08418  9   ARG A C     
79   O O     . ARG A 9   ? 0.52657 0.41668 0.31628 0.10187  -0.08019 0.07446  9   ARG A O     
80   C CB    . ARG A 9   ? 0.45070 0.37458 0.30984 0.07262  -0.11355 0.03230  9   ARG A CB    
81   C CG    . ARG A 9   ? 0.46638 0.42991 0.31573 0.10482  -0.11793 0.04587  9   ARG A CG    
82   C CD    . ARG A 9   ? 0.46858 0.44688 0.30596 0.09261  -0.12125 0.02457  9   ARG A CD    
83   N NE    . ARG A 9   ? 0.45789 0.47927 0.30380 0.09839  -0.13386 0.01677  9   ARG A NE    
84   C CZ    . ARG A 9   ? 0.44561 0.50330 0.31952 0.10419  -0.13346 0.02400  9   ARG A CZ    
85   N NH1   . ARG A 9   ? 0.46286 0.49497 0.32074 0.11526  -0.12787 -0.00068 9   ARG A NH1   
86   N NH2   . ARG A 9   ? 0.40981 0.52593 0.32662 0.08823  -0.14234 0.03217  9   ARG A NH2   
87   N N     . LYS A 10  ? 0.54849 0.38840 0.31173 0.08754  -0.04314 0.09164  10  LYS A N     
88   C CA    . LYS A 10  ? 0.57413 0.41812 0.32284 0.09321  -0.03831 0.09660  10  LYS A CA    
89   C C     . LYS A 10  ? 0.58378 0.40789 0.32772 0.05918  -0.02547 0.10484  10  LYS A C     
90   O O     . LYS A 10  ? 0.60535 0.38931 0.34460 0.06314  -0.02078 0.08691  10  LYS A O     
91   C CB    . LYS A 10  ? 0.60845 0.48318 0.34748 0.11342  -0.04839 0.07891  10  LYS A CB    
92   C CG    . LYS A 10  ? 0.63853 0.52239 0.37546 0.10552  -0.05090 0.05737  10  LYS A CG    
93   C CD    . LYS A 10  ? 0.65193 0.55347 0.39826 0.07041  -0.06413 0.03667  10  LYS A CD    
94   C CE    . LYS A 10  ? 0.66074 0.56865 0.40654 0.04648  -0.07525 0.04266  10  LYS A CE    
95   N N     . GLU A 11  ? 0.57095 0.39042 0.31813 0.03969  -0.03118 0.09388  11  GLU A N     
96   C CA    . GLU A 11  ? 0.55487 0.38932 0.32259 0.01103  -0.02085 0.11431  11  GLU A CA    
97   C C     . GLU A 11  ? 0.51173 0.35139 0.32983 -0.04486 -0.01809 0.10066  11  GLU A C     
98   O O     . GLU A 11  ? 0.51020 0.36520 0.33628 -0.03742 -0.01547 0.10086  11  GLU A O     
99   C CB    . GLU A 11  ? 0.58193 0.45079 0.32868 0.03757  -0.02548 0.10892  11  GLU A CB    
100  C CG    . GLU A 11  ? 0.61044 0.48612 0.33925 0.04263  -0.03483 0.11164  11  GLU A CG    
101  C CD    . GLU A 11  ? 0.63522 0.52293 0.34853 0.05739  -0.05183 0.08675  11  GLU A CD    
102  O OE1   . GLU A 11  ? 0.66189 0.56007 0.36114 0.05159  -0.05037 0.06058  11  GLU A OE1   
103  O OE2   . GLU A 11  ? 0.63878 0.55899 0.34655 0.06398  -0.06345 0.07535  11  GLU A OE2   
104  N N     . ILE A 12  ? 0.46589 0.29665 0.31480 -0.04049 -0.02388 0.11228  12  ILE A N     
105  C CA    . ILE A 12  ? 0.44147 0.29719 0.31344 -0.03267 -0.03953 0.10736  12  ILE A CA    
106  C C     . ILE A 12  ? 0.41963 0.27901 0.31399 -0.03794 -0.05517 0.10598  12  ILE A C     
107  O O     . ILE A 12  ? 0.43756 0.30852 0.31381 -0.00456 -0.07180 0.05365  12  ILE A O     
108  C CB    . ILE A 12  ? 0.42623 0.28120 0.30216 -0.03407 -0.06686 0.10030  12  ILE A CB    
109  C CG1   . ILE A 12  ? 0.42850 0.28879 0.30781 -0.03955 -0.05563 0.08520  12  ILE A CG1   
110  C CG2   . ILE A 12  ? 0.43068 0.28469 0.30122 -0.03936 -0.08741 0.12369  12  ILE A CG2   
111  C CD1   . ILE A 12  ? 0.43295 0.29340 0.31136 -0.03447 -0.05630 0.07237  12  ILE A CD1   
112  N N     . LEU A 13  ? 0.41320 0.29122 0.31564 -0.04472 -0.05251 0.13800  13  LEU A N     
113  C CA    . LEU A 13  ? 0.39902 0.27419 0.31540 -0.04691 -0.05856 0.13742  13  LEU A CA    
114  C C     . LEU A 13  ? 0.36831 0.29211 0.31169 -0.04654 -0.08603 0.11516  13  LEU A C     
115  O O     . LEU A 13  ? 0.35041 0.29632 0.33407 -0.03963 -0.09254 0.11967  13  LEU A O     
116  C CB    . LEU A 13  ? 0.42654 0.34328 0.34915 -0.02088 -0.04587 0.12684  13  LEU A CB    
117  C CG    . LEU A 13  ? 0.46434 0.33840 0.36308 -0.03364 -0.02556 0.11981  13  LEU A CG    
118  C CD1   . LEU A 13  ? 0.48043 0.33132 0.36827 -0.04908 -0.00590 0.15155  13  LEU A CD1   
119  C CD2   . LEU A 13  ? 0.48060 0.36461 0.36810 -0.02167 -0.01363 0.10719  13  LEU A CD2   
120  N N     . ILE A 14  ? 0.37482 0.28686 0.31806 -0.05415 -0.08121 0.11274  14  ILE A N     
121  C CA    . ILE A 14  ? 0.37123 0.28186 0.32476 -0.04110 -0.07630 0.09883  14  ILE A CA    
122  C C     . ILE A 14  ? 0.36497 0.30499 0.33942 -0.01570 -0.08079 0.09290  14  ILE A C     
123  O O     . ILE A 14  ? 0.37343 0.36881 0.34066 0.02298  -0.11012 0.03472  14  ILE A O     
124  C CB    . ILE A 14  ? 0.36219 0.30089 0.32709 -0.06591 -0.07589 0.09507  14  ILE A CB    
125  C CG1   . ILE A 14  ? 0.38616 0.27318 0.32149 -0.06256 -0.09900 0.08768  14  ILE A CG1   
126  C CG2   . ILE A 14  ? 0.34613 0.32087 0.32675 -0.07049 -0.07370 0.07378  14  ILE A CG2   
127  C CD1   . ILE A 14  ? 0.41622 0.29162 0.31715 -0.09549 -0.10776 0.07573  14  ILE A CD1   
128  N N     . GLU A 15  ? 0.34540 0.24662 0.34940 -0.03123 -0.07401 0.11030  15  GLU A N     
129  C CA    . GLU A 15  ? 0.38983 0.25579 0.38113 0.00394  -0.05480 0.12337  15  GLU A CA    
130  C C     . GLU A 15  ? 0.35288 0.22602 0.38430 0.03969  -0.06900 0.09991  15  GLU A C     
131  O O     . GLU A 15  ? 0.31884 0.22728 0.39128 0.02490  -0.07188 0.08244  15  GLU A O     
132  C CB    . GLU A 15  ? 0.47763 0.31914 0.41013 0.02801  -0.02968 0.16189  15  GLU A CB    
133  C CG    . GLU A 15  ? 0.56211 0.41179 0.43672 0.06279  0.00017  0.17847  15  GLU A CG    
134  C CD    . GLU A 15  ? 0.63432 0.49932 0.46653 0.10065  0.01883  0.14132  15  GLU A CD    
135  O OE1   . GLU A 15  ? 0.66384 0.53418 0.48201 0.09572  0.02800  0.12178  15  GLU A OE1   
136  O OE2   . GLU A 15  ? 0.65899 0.54544 0.47855 0.11222  0.02675  0.13463  15  GLU A OE2   
137  N N     . PRO A 16  ? 0.36234 0.22376 0.37965 0.04476  -0.07996 0.07777  16  PRO A N     
138  C CA    . PRO A 16  ? 0.35726 0.21484 0.38190 0.04866  -0.08884 0.05525  16  PRO A CA    
139  C C     . PRO A 16  ? 0.35313 0.19424 0.37091 0.04915  -0.09389 0.06045  16  PRO A C     
140  O O     . PRO A 16  ? 0.37478 0.21255 0.37658 0.03247  -0.06755 0.07137  16  PRO A O     
141  C CB    . PRO A 16  ? 0.34984 0.24313 0.38931 0.06676  -0.07072 0.04464  16  PRO A CB    
142  C CG    . PRO A 16  ? 0.33788 0.26526 0.38857 0.03751  -0.07018 0.03440  16  PRO A CG    
143  C CD    . PRO A 16  ? 0.34636 0.23289 0.38547 0.04703  -0.06823 0.04432  16  PRO A CD    
144  N N     . PHE A 17  ? 0.36511 0.22331 0.36023 0.02490  -0.10205 0.06609  17  PHE A N     
145  C CA    . PHE A 17  ? 0.36247 0.24186 0.34672 0.03679  -0.09041 0.07838  17  PHE A CA    
146  C C     . PHE A 17  ? 0.33038 0.24957 0.34733 0.03667  -0.09246 0.06674  17  PHE A C     
147  O O     . PHE A 17  ? 0.35819 0.27793 0.37012 0.05710  -0.07350 0.05531  17  PHE A O     
148  C CB    . PHE A 17  ? 0.38377 0.26616 0.33057 0.04146  -0.09822 0.07957  17  PHE A CB    
149  C CG    . PHE A 17  ? 0.41380 0.32409 0.32886 0.01024  -0.10689 0.07369  17  PHE A CG    
150  C CD1   . PHE A 17  ? 0.41921 0.31189 0.32925 0.00287  -0.11024 0.09258  17  PHE A CD1   
151  C CD2   . PHE A 17  ? 0.43754 0.34486 0.33888 0.00122  -0.09596 0.05654  17  PHE A CD2   
152  C CE1   . PHE A 17  ? 0.44312 0.34759 0.33543 0.01858  -0.11928 0.08505  17  PHE A CE1   
153  C CE2   . PHE A 17  ? 0.45724 0.39521 0.32976 0.02355  -0.10679 0.06133  17  PHE A CE2   
154  C CZ    . PHE A 17  ? 0.44302 0.37366 0.32376 0.02664  -0.12290 0.07820  17  PHE A CZ    
155  N N     . ASN A 18  ? 0.30093 0.25013 0.33207 0.02791  -0.06397 0.05258  18  ASN A N     
156  C CA    . ASN A 18  ? 0.30203 0.24762 0.32507 0.03276  -0.07380 0.02723  18  ASN A CA    
157  C C     . ASN A 18  ? 0.32289 0.25244 0.31856 0.06647  -0.08609 0.03245  18  ASN A C     
158  O O     . ASN A 18  ? 0.30165 0.24151 0.30767 0.01592  -0.08224 0.02280  18  ASN A O     
159  C CB    . ASN A 18  ? 0.28372 0.28282 0.32745 0.01338  -0.06522 0.01972  18  ASN A CB    
160  C CG    . ASN A 18  ? 0.30014 0.31529 0.34255 0.05777  -0.04904 0.00962  18  ASN A CG    
161  O OD1   . ASN A 18  ? 0.29580 0.35682 0.35528 0.09199  -0.03839 0.02908  18  ASN A OD1   
162  N ND2   . ASN A 18  ? 0.34628 0.28301 0.33804 0.03174  -0.03776 0.01749  18  ASN A ND2   
163  N N     . GLU A 19  ? 0.34071 0.28720 0.32794 0.07741  -0.08349 0.02064  19  GLU A N     
164  C CA    . GLU A 19  ? 0.30969 0.28640 0.32635 0.04820  -0.11084 0.02112  19  GLU A CA    
165  C C     . GLU A 19  ? 0.28535 0.29060 0.33614 0.03290  -0.10379 0.01221  19  GLU A C     
166  O O     . GLU A 19  ? 0.29157 0.29804 0.33652 0.06064  -0.13670 -0.00812 19  GLU A O     
167  C CB    . GLU A 19  ? 0.34735 0.31353 0.34509 0.06901  -0.11061 0.04395  19  GLU A CB    
168  C CG    . GLU A 19  ? 0.43103 0.43513 0.36731 0.11588  -0.08842 0.06548  19  GLU A CG    
169  C CD    . GLU A 19  ? 0.47611 0.51401 0.38177 0.13336  -0.06450 0.05660  19  GLU A CD    
170  O OE1   . GLU A 19  ? 0.48922 0.53747 0.39001 0.13660  -0.06782 0.05153  19  GLU A OE1   
171  O OE2   . GLU A 19  ? 0.50548 0.56467 0.39694 0.13012  -0.03919 0.04029  19  GLU A OE2   
172  N N     . LYS A 20  ? 0.24688 0.28704 0.34333 0.04657  -0.09182 0.01089  20  LYS A N     
173  C CA    . LYS A 20  ? 0.23879 0.30122 0.34697 0.02576  -0.06620 0.03629  20  LYS A CA    
174  C C     . LYS A 20  ? 0.24287 0.26601 0.32349 0.02014  -0.06488 0.04734  20  LYS A C     
175  O O     . LYS A 20  ? 0.26134 0.28519 0.35177 0.01074  -0.06184 0.03714  20  LYS A O     
176  C CB    . LYS A 20  ? 0.26429 0.34221 0.36399 0.07317  -0.05158 0.03114  20  LYS A CB    
177  N N     . SER A 21  ? 0.25507 0.24516 0.27487 0.01961  -0.07774 0.02279  21  SER A N     
178  C CA    . SER A 21  ? 0.24995 0.24400 0.26366 0.02472  -0.07106 0.01267  21  SER A CA    
179  C C     . SER A 21  ? 0.24070 0.24363 0.25375 0.01635  -0.07701 0.01469  21  SER A C     
180  O O     . SER A 21  ? 0.25224 0.25431 0.24320 0.03958  -0.06074 -0.00656 21  SER A O     
181  C CB    . SER A 21  ? 0.25349 0.20653 0.26835 -0.00360 -0.04076 0.00534  21  SER A CB    
182  O OG    . SER A 21  ? 0.25824 0.21721 0.26725 0.02700  -0.04657 0.00620  21  SER A OG    
183  N N     . LEU A 22  ? 0.24480 0.24897 0.25370 0.02519  -0.08116 0.01492  22  LEU A N     
184  C CA    . LEU A 22  ? 0.26536 0.24698 0.26218 0.03295  -0.09138 0.03422  22  LEU A CA    
185  C C     . LEU A 22  ? 0.28174 0.27870 0.27950 0.01793  -0.08015 0.00328  22  LEU A C     
186  O O     . LEU A 22  ? 0.30950 0.32310 0.31262 0.00993  -0.03590 -0.00674 22  LEU A O     
187  C CB    . LEU A 22  ? 0.29252 0.29534 0.25941 0.04932  -0.09843 0.02386  22  LEU A CB    
188  C CG    . LEU A 22  ? 0.33466 0.31818 0.25329 0.07174  -0.09702 0.02894  22  LEU A CG    
189  C CD1   . LEU A 22  ? 0.35096 0.34598 0.25451 0.07923  -0.09990 0.01745  22  LEU A CD1   
190  C CD2   . LEU A 22  ? 0.33690 0.29611 0.25530 0.03092  -0.08523 0.06438  22  LEU A CD2   
191  N N     . GLN A 23  ? 0.27844 0.27316 0.25423 0.00879  -0.08619 0.01012  23  GLN A N     
192  C CA    . GLN A 23  ? 0.29763 0.27359 0.25356 0.00514  -0.07498 0.02748  23  GLN A CA    
193  C C     . GLN A 23  ? 0.31546 0.26862 0.24644 0.00346  -0.06582 0.03259  23  GLN A C     
194  O O     . GLN A 23  ? 0.32398 0.28152 0.23268 -0.00556 -0.06745 0.02846  23  GLN A O     
195  C CB    . GLN A 23  ? 0.29965 0.27414 0.25847 0.02135  -0.05882 0.00214  23  GLN A CB    
196  C CG    . GLN A 23  ? 0.32088 0.29382 0.27878 0.00822  -0.05614 -0.01600 23  GLN A CG    
197  C CD    . GLN A 23  ? 0.36771 0.36594 0.30688 -0.03492 -0.06636 -0.05328 23  GLN A CD    
198  O OE1   . GLN A 23  ? 0.41424 0.39248 0.33233 -0.05332 -0.04924 -0.03440 23  GLN A OE1   
199  N NE2   . GLN A 23  ? 0.37541 0.44901 0.33667 0.01811  -0.05653 -0.03963 23  GLN A NE2   
200  N N     . PRO A 24  ? 0.34264 0.28193 0.25374 0.01297  -0.06542 0.00960  24  PRO A N     
201  C CA    . PRO A 24  ? 0.33056 0.27547 0.25575 -0.01907 -0.06446 -0.02369 24  PRO A CA    
202  C C     . PRO A 24  ? 0.31495 0.29338 0.22412 -0.02913 -0.08145 -0.00814 24  PRO A C     
203  O O     . PRO A 24  ? 0.33197 0.31157 0.21447 -0.03176 -0.07831 -0.01563 24  PRO A O     
204  C CB    . PRO A 24  ? 0.34851 0.29870 0.28533 -0.02019 -0.04642 -0.02895 24  PRO A CB    
205  C CG    . PRO A 24  ? 0.38065 0.29070 0.28067 -0.00795 -0.04995 -0.03262 24  PRO A CG    
206  C CD    . PRO A 24  ? 0.36715 0.28994 0.27725 -0.00243 -0.04793 -0.01247 24  PRO A CD    
207  N N     . ALA A 25  ? 0.28553 0.25104 0.21320 -0.03253 -0.07639 0.00047  25  ALA A N     
208  C CA    . ALA A 25  ? 0.28274 0.28331 0.20503 -0.01371 -0.07241 0.01868  25  ALA A CA    
209  C C     . ALA A 25  ? 0.26437 0.25369 0.18161 -0.00676 -0.05938 0.01773  25  ALA A C     
210  O O     . ALA A 25  ? 0.26467 0.24528 0.16275 0.01585  -0.04375 0.02592  25  ALA A O     
211  C CB    . ALA A 25  ? 0.31142 0.30423 0.22662 0.02081  -0.07321 -0.00939 25  ALA A CB    
212  N N     . GLY A 26  ? 0.25805 0.21753 0.18286 -0.00265 -0.05995 0.00158  26  GLY A N     
213  C CA    . GLY A 26  ? 0.25509 0.21396 0.20400 -0.00631 -0.05837 0.00253  26  GLY A CA    
214  C C     . GLY A 26  ? 0.25886 0.22760 0.22216 0.02670  -0.05719 0.00441  26  GLY A C     
215  O O     . GLY A 26  ? 0.25940 0.26210 0.24462 0.04286  -0.06060 0.02215  26  GLY A O     
216  N N     . TYR A 27  ? 0.24075 0.17591 0.20446 0.00321  -0.05221 0.00367  27  TYR A N     
217  C CA    . TYR A 27  ? 0.26456 0.18001 0.19518 0.02819  -0.03824 0.03989  27  TYR A CA    
218  C C     . TYR A 27  ? 0.22152 0.17829 0.19885 0.03306  -0.04142 0.04000  27  TYR A C     
219  O O     . TYR A 27  ? 0.19851 0.19268 0.19816 0.02429  -0.05371 0.03415  27  TYR A O     
220  C CB    . TYR A 27  ? 0.28059 0.19914 0.19208 0.03154  -0.03474 0.05824  27  TYR A CB    
221  C CG    . TYR A 27  ? 0.25371 0.16654 0.21337 -0.00410 -0.04074 0.05612  27  TYR A CG    
222  C CD1   . TYR A 27  ? 0.27133 0.18960 0.23462 0.02299  -0.04526 0.02038  27  TYR A CD1   
223  C CD2   . TYR A 27  ? 0.26553 0.18955 0.24333 0.03396  -0.05966 0.06965  27  TYR A CD2   
224  C CE1   . TYR A 27  ? 0.28207 0.17132 0.25841 0.00931  -0.05073 0.04995  27  TYR A CE1   
225  C CE2   . TYR A 27  ? 0.26048 0.19968 0.25513 0.01996  -0.06628 0.05307  27  TYR A CE2   
226  C CZ    . TYR A 27  ? 0.27521 0.17766 0.26569 0.02024  -0.06277 0.03173  27  TYR A CZ    
227  O OH    . TYR A 27  ? 0.30353 0.19799 0.28534 0.03551  -0.04984 0.04049  27  TYR A OH    
228  N N     . ASP A 28  ? 0.21250 0.17435 0.20737 0.01836  -0.02999 0.02804  28  ASP A N     
229  C CA    . ASP A 28  ? 0.20136 0.18505 0.20675 0.01352  -0.02606 0.02802  28  ASP A CA    
230  C C     . ASP A 28  ? 0.21176 0.15923 0.20117 0.02066  -0.02742 0.01827  28  ASP A C     
231  O O     . ASP A 28  ? 0.22565 0.18191 0.22056 0.01723  -0.03637 0.00965  28  ASP A O     
232  C CB    . ASP A 28  ? 0.21015 0.20604 0.25069 -0.00228 -0.01792 0.00209  28  ASP A CB    
233  C CG    . ASP A 28  ? 0.24192 0.23494 0.28205 0.02033  -0.00412 -0.01320 28  ASP A CG    
234  O OD1   . ASP A 28  ? 0.24369 0.20766 0.27167 -0.00572 -0.00605 0.00055  28  ASP A OD1   
235  O OD2   . ASP A 28  ? 0.27643 0.25796 0.32502 -0.00549 0.00613  -0.05223 28  ASP A OD2   
236  N N     . LEU A 29  ? 0.19123 0.15205 0.19610 -0.00856 -0.04993 0.01564  29  LEU A N     
237  C CA    . LEU A 29  ? 0.18595 0.15153 0.20740 0.00212  -0.02355 0.01133  29  LEU A CA    
238  C C     . LEU A 29  ? 0.21584 0.15090 0.20490 0.02273  -0.01024 0.03427  29  LEU A C     
239  O O     . LEU A 29  ? 0.20428 0.15845 0.21329 0.01106  -0.01185 0.01950  29  LEU A O     
240  C CB    . LEU A 29  ? 0.19049 0.22472 0.20598 0.00582  -0.00888 0.03195  29  LEU A CB    
241  C CG    . LEU A 29  ? 0.21746 0.19700 0.20609 -0.00160 0.00521  0.05385  29  LEU A CG    
242  C CD1   . LEU A 29  ? 0.19467 0.23860 0.22169 -0.00081 -0.00530 0.03685  29  LEU A CD1   
243  C CD2   . LEU A 29  ? 0.28004 0.21161 0.22119 0.01920  0.00027  0.07391  29  LEU A CD2   
244  N N     . ARG A 30  ? 0.20907 0.16033 0.22220 0.01754  -0.01580 0.00239  30  ARG A N     
245  C CA    . ARG A 30  ? 0.20501 0.17377 0.23796 0.02406  -0.02332 -0.00839 30  ARG A CA    
246  C C     . ARG A 30  ? 0.18903 0.12969 0.23419 -0.01067 -0.00735 0.00398  30  ARG A C     
247  O O     . ARG A 30  ? 0.20618 0.15067 0.23062 -0.01088 -0.01328 0.01148  30  ARG A O     
248  C CB    . ARG A 30  ? 0.20636 0.19833 0.24937 0.01105  -0.04470 -0.01217 30  ARG A CB    
249  C CG    . ARG A 30  ? 0.22984 0.22637 0.26641 -0.00315 -0.05757 -0.01084 30  ARG A CG    
250  C CD    . ARG A 30  ? 0.24683 0.23407 0.27221 0.02948  -0.05097 0.04664  30  ARG A CD    
251  N NE    . ARG A 30  ? 0.28606 0.24544 0.27997 0.04005  -0.05471 0.04373  30  ARG A NE    
252  C CZ    . ARG A 30  ? 0.29925 0.28464 0.30318 0.03477  -0.06466 0.02501  30  ARG A CZ    
253  N NH1   . ARG A 30  ? 0.28190 0.28169 0.32047 0.03836  -0.05774 0.01579  30  ARG A NH1   
254  N NH2   . ARG A 30  ? 0.28809 0.28900 0.31391 0.01550  -0.06985 0.03323  30  ARG A NH2   
255  N N     . VAL A 31  ? 0.18710 0.15779 0.23533 0.01038  -0.00509 0.00607  31  VAL A N     
256  C CA    . VAL A 31  ? 0.20046 0.14720 0.24004 -0.01491 -0.00407 -0.00778 31  VAL A CA    
257  C C     . VAL A 31  ? 0.19481 0.17502 0.25878 0.00391  -0.00265 0.00416  31  VAL A C     
258  O O     . VAL A 31  ? 0.18848 0.16376 0.28850 0.01635  -0.01476 0.00720  31  VAL A O     
259  C CB    . VAL A 31  ? 0.21046 0.15539 0.23677 -0.00052 0.00895  -0.00280 31  VAL A CB    
260  C CG1   . VAL A 31  ? 0.22777 0.17614 0.23401 0.00261  -0.00065 -0.01666 31  VAL A CG1   
261  C CG2   . VAL A 31  ? 0.23014 0.17600 0.24835 -0.02995 -0.00934 0.02438  31  VAL A CG2   
262  N N     . GLY A 32  ? 0.19838 0.14933 0.25793 -0.00983 0.01291  0.00883  32  GLY A N     
263  C CA    . GLY A 32  ? 0.22838 0.15075 0.27183 0.00426  0.02080  -0.00912 32  GLY A CA    
264  C C     . GLY A 32  ? 0.22505 0.14107 0.29168 -0.01609 0.01957  -0.00505 32  GLY A C     
265  O O     . GLY A 32  ? 0.21533 0.17829 0.29093 0.00389  0.02021  -0.01015 32  GLY A O     
266  N N     . LYS A 33  ? 0.21734 0.13889 0.31615 0.00083  0.00165  -0.02118 33  LYS A N     
267  C CA    . LYS A 33  ? 0.25055 0.13607 0.32033 0.01331  -0.01147 -0.03582 33  LYS A CA    
268  C C     . LYS A 33  ? 0.21927 0.15656 0.31121 0.01197  0.00675  -0.03068 33  LYS A C     
269  O O     . LYS A 33  ? 0.25125 0.16448 0.31919 0.02590  0.00436  -0.02592 33  LYS A O     
270  C CB    . LYS A 33  ? 0.31610 0.15276 0.35111 0.00454  -0.03010 0.00429  33  LYS A CB    
271  C CG    . LYS A 33  ? 0.38610 0.17827 0.38746 -0.00270 -0.03081 0.02199  33  LYS A CG    
272  C CD    . LYS A 33  ? 0.47086 0.23351 0.42681 0.04223  -0.03441 0.03639  33  LYS A CD    
273  C CE    . LYS A 33  ? 0.52868 0.30571 0.46144 0.12078  -0.02547 0.05931  33  LYS A CE    
274  N NZ    . LYS A 33  ? 0.57612 0.37713 0.50994 0.15352  -0.02207 0.04237  33  LYS A NZ    
275  N N     . GLU A 34  ? 0.20102 0.16138 0.31134 -0.00128 -0.01442 -0.00044 34  GLU A N     
276  C CA    . GLU A 34  ? 0.18963 0.17679 0.30537 -0.03157 -0.03992 -0.00467 34  GLU A CA    
277  C C     . GLU A 34  ? 0.19744 0.16359 0.27332 -0.01604 -0.01210 -0.01435 34  GLU A C     
278  O O     . GLU A 34  ? 0.21032 0.18694 0.25114 0.00365  0.00189  -0.01732 34  GLU A O     
279  C CB    . GLU A 34  ? 0.25816 0.19888 0.34614 -0.02154 -0.04179 -0.00152 34  GLU A CB    
280  C CG    . GLU A 34  ? 0.32017 0.20016 0.37829 -0.00785 -0.02876 0.00471  34  GLU A CG    
281  C CD    . GLU A 34  ? 0.34852 0.24430 0.41205 0.00916  -0.01501 -0.00648 34  GLU A CD    
282  O OE1   . GLU A 34  ? 0.34239 0.23435 0.41669 -0.05253 -0.01662 -0.00419 34  GLU A OE1   
283  O OE2   . GLU A 34  ? 0.42833 0.28705 0.44206 0.05497  -0.01471 -0.02212 34  GLU A OE2   
284  N N     . ALA A 35  ? 0.20240 0.17990 0.26480 0.01359  0.00513  -0.01050 35  ALA A N     
285  C CA    . ALA A 35  ? 0.19318 0.16220 0.26467 -0.00452 0.02567  -0.02635 35  ALA A CA    
286  C C     . ALA A 35  ? 0.18943 0.18722 0.25396 0.02039  0.02109  -0.05667 35  ALA A C     
287  O O     . ALA A 35  ? 0.22203 0.19043 0.27023 0.00711  0.00319  -0.05796 35  ALA A O     
288  C CB    . ALA A 35  ? 0.17452 0.17491 0.27138 0.00627  0.04669  -0.02437 35  ALA A CB    
289  N N     . TYR A 36  ? 0.17845 0.17786 0.25309 -0.00086 0.00559  -0.04338 36  TYR A N     
290  C CA    . TYR A 36  ? 0.17343 0.19067 0.25781 -0.02227 0.00376  -0.03491 36  TYR A CA    
291  C C     . TYR A 36  ? 0.20453 0.18044 0.23685 -0.01802 0.02413  -0.03643 36  TYR A C     
292  O O     . TYR A 36  ? 0.21909 0.18794 0.21768 -0.00767 -0.00185 -0.04812 36  TYR A O     
293  C CB    . TYR A 36  ? 0.20511 0.25915 0.30260 -0.02766 -0.00583 -0.05914 36  TYR A CB    
294  C CG    . TYR A 36  ? 0.21435 0.30223 0.33924 -0.02162 -0.03258 -0.05151 36  TYR A CG    
295  C CD1   . TYR A 36  ? 0.25123 0.36107 0.37215 -0.05799 -0.03081 -0.07374 36  TYR A CD1   
296  C CD2   . TYR A 36  ? 0.20311 0.40066 0.35328 -0.01402 -0.04520 -0.04002 36  TYR A CD2   
297  C CE1   . TYR A 36  ? 0.25115 0.41217 0.39430 -0.06288 -0.04880 -0.07995 36  TYR A CE1   
298  C CE2   . TYR A 36  ? 0.25699 0.43618 0.37467 -0.00775 -0.04605 -0.02884 36  TYR A CE2   
299  C CZ    . TYR A 36  ? 0.23347 0.45055 0.39642 -0.05936 -0.06169 -0.06235 36  TYR A CZ    
300  O OH    . TYR A 36  ? 0.24845 0.52980 0.42226 -0.06651 -0.04932 -0.02497 36  TYR A OH    
301  N N     . ILE A 37  ? 0.21187 0.19054 0.23113 -0.00054 0.02410  -0.03418 37  ILE A N     
302  C CA    . ILE A 37  ? 0.22138 0.20264 0.23638 -0.03007 0.00680  -0.03037 37  ILE A CA    
303  C C     . ILE A 37  ? 0.25856 0.22348 0.25067 0.01798  -0.02316 -0.09503 37  ILE A C     
304  O O     . ILE A 37  ? 0.28577 0.23848 0.26124 0.01417  -0.01856 -0.10360 37  ILE A O     
305  C CB    . ILE A 37  ? 0.23111 0.19586 0.23987 -0.03635 0.00798  -0.02307 37  ILE A CB    
306  C CG1   . ILE A 37  ? 0.21497 0.23911 0.23443 -0.03233 0.01844  -0.03961 37  ILE A CG1   
307  C CG2   . ILE A 37  ? 0.30288 0.21530 0.23542 -0.01801 0.02569  -0.00229 37  ILE A CG2   
308  C CD1   . ILE A 37  ? 0.22576 0.24687 0.25506 -0.03637 0.01773  -0.02508 37  ILE A CD1   
309  N N     . ASN A 38  ? 0.28153 0.26071 0.26276 0.00833  -0.05863 -0.09679 38  ASN A N     
310  C CA    . ASN A 38  ? 0.32405 0.30526 0.28598 0.01605  -0.05471 -0.10262 38  ASN A CA    
311  C C     . ASN A 38  ? 0.34945 0.31071 0.30930 0.01742  -0.05338 -0.10289 38  ASN A C     
312  O O     . ASN A 38  ? 0.39474 0.32517 0.32001 0.03567  -0.06179 -0.12408 38  ASN A O     
313  C CB    . ASN A 38  ? 0.37233 0.32162 0.28050 0.03557  -0.03539 -0.11310 38  ASN A CB    
314  C CG    . ASN A 38  ? 0.41824 0.34595 0.29168 0.03722  -0.01701 -0.09680 38  ASN A CG    
315  O OD1   . ASN A 38  ? 0.43414 0.32732 0.32172 0.02172  -0.01591 -0.06553 38  ASN A OD1   
316  N ND2   . ASN A 38  ? 0.44489 0.38544 0.28477 0.02894  0.00214  -0.07970 38  ASN A ND2   
317  N N     . GLY A 39  ? 0.31193 0.30498 0.33571 -0.02276 -0.05805 -0.07272 39  GLY A N     
318  C CA    . GLY A 39  ? 0.31784 0.26980 0.36722 -0.02230 -0.06287 -0.07308 39  GLY A CA    
319  C C     . GLY A 39  ? 0.33560 0.26743 0.38670 -0.03788 -0.06440 -0.09349 39  GLY A C     
320  O O     . GLY A 39  ? 0.34295 0.31472 0.40482 -0.08071 -0.06579 -0.08034 39  GLY A O     
321  N N     . ARG A 40  ? 0.32988 0.29449 0.38485 -0.01380 -0.06475 -0.10937 40  ARG A N     
322  C CA    . ARG A 40  ? 0.33412 0.30171 0.40005 -0.01385 -0.05658 -0.11580 40  ARG A CA    
323  C C     . ARG A 40  ? 0.29244 0.25104 0.39149 -0.00094 -0.05038 -0.12754 40  ARG A C     
324  O O     . ARG A 40  ? 0.25918 0.23890 0.37713 0.00025  -0.04502 -0.12904 40  ARG A O     
325  C CB    . ARG A 40  ? 0.39162 0.39466 0.43178 0.00390  -0.05444 -0.13886 40  ARG A CB    
326  C CG    . ARG A 40  ? 0.47382 0.50526 0.47513 0.02355  -0.05295 -0.14553 40  ARG A CG    
327  C CD    . ARG A 40  ? 0.55514 0.57551 0.51616 0.07124  -0.04200 -0.15422 40  ARG A CD    
328  N NE    . ARG A 40  ? 0.62354 0.64165 0.54574 0.10490  -0.04176 -0.16904 40  ARG A NE    
329  C CZ    . ARG A 40  ? 0.66995 0.68155 0.56995 0.13756  -0.04621 -0.17663 40  ARG A CZ    
330  N NH1   . ARG A 40  ? 0.68346 0.70622 0.57564 0.13437  -0.04907 -0.18737 40  ARG A NH1   
331  N NH2   . ARG A 40  ? 0.67790 0.70812 0.57963 0.15050  -0.04603 -0.17944 40  ARG A NH2   
332  N N     . LEU A 41  ? 0.28201 0.23367 0.40191 -0.00564 -0.05350 -0.11126 41  LEU A N     
333  C CA    . LEU A 41  ? 0.29069 0.21521 0.41291 0.01235  -0.03151 -0.09469 41  LEU A CA    
334  C C     . LEU A 41  ? 0.27702 0.23259 0.39377 0.03105  -0.01845 -0.11609 41  LEU A C     
335  O O     . LEU A 41  ? 0.34017 0.28997 0.40004 0.04428  -0.03604 -0.15853 41  LEU A O     
336  C CB    . LEU A 41  ? 0.34082 0.25882 0.43915 0.02635  -0.03334 -0.07254 41  LEU A CB    
337  C CG    . LEU A 41  ? 0.36123 0.31091 0.45611 0.01567  -0.03934 -0.05593 41  LEU A CG    
338  N N     . ILE A 42  ? 0.25104 0.21916 0.36957 0.01723  0.00029  -0.09175 42  ILE A N     
339  C CA    . ILE A 42  ? 0.23830 0.21522 0.35663 0.01573  -0.00907 -0.08297 42  ILE A CA    
340  C C     . ILE A 42  ? 0.24226 0.20802 0.34570 0.03053  0.00193  -0.08161 42  ILE A C     
341  O O     . ILE A 42  ? 0.24451 0.24037 0.34699 0.02809  -0.00257 -0.07348 42  ILE A O     
342  C CB    . ILE A 42  ? 0.27053 0.24844 0.35156 0.01380  -0.00704 -0.07187 42  ILE A CB    
343  C CG1   . ILE A 42  ? 0.31842 0.24971 0.35528 0.02546  -0.01861 -0.05901 42  ILE A CG1   
344  C CG2   . ILE A 42  ? 0.24555 0.29879 0.35039 0.01819  -0.00258 -0.08389 42  ILE A CG2   
345  C CD1   . ILE A 42  ? 0.35691 0.24686 0.35734 0.06480  -0.00663 -0.06018 42  ILE A CD1   
346  N N     . ASN A 43  ? 0.22769 0.17922 0.35556 0.02689  0.00803  -0.07747 43  ASN A N     
347  C CA    . ASN A 43  ? 0.25620 0.17154 0.35807 0.03803  0.00336  -0.05707 43  ASN A CA    
348  C C     . ASN A 43  ? 0.22347 0.18897 0.36068 0.01399  0.01950  -0.04206 43  ASN A C     
349  O O     . ASN A 43  ? 0.23217 0.21922 0.37701 0.04653  0.03030  -0.07894 43  ASN A O     
350  C CB    . ASN A 43  ? 0.27685 0.14974 0.37609 0.03991  -0.00133 -0.05271 43  ASN A CB    
351  C CG    . ASN A 43  ? 0.27777 0.14966 0.39371 0.01504  0.00646  -0.04381 43  ASN A CG    
352  O OD1   . ASN A 43  ? 0.28327 0.18933 0.41334 0.02067  0.00533  -0.05907 43  ASN A OD1   
353  N ND2   . ASN A 43  ? 0.30708 0.20211 0.40371 -0.00165 0.04764  -0.02016 43  ASN A ND2   
354  N N     . VAL A 44  ? 0.22574 0.16291 0.34900 -0.00142 0.00377  -0.06615 44  VAL A N     
355  C CA    . VAL A 44  ? 0.21715 0.16063 0.35532 0.00918  0.02184  -0.05694 44  VAL A CA    
356  C C     . VAL A 44  ? 0.24206 0.16348 0.37378 0.02515  0.02753  -0.05037 44  VAL A C     
357  O O     . VAL A 44  ? 0.20214 0.19097 0.38154 0.03604  0.01491  -0.04913 44  VAL A O     
358  C CB    . VAL A 44  ? 0.19562 0.17303 0.35177 0.01919  0.02650  -0.05949 44  VAL A CB    
359  C CG1   . VAL A 44  ? 0.21130 0.17524 0.35610 0.00187  0.03808  -0.04539 44  VAL A CG1   
360  C CG2   . VAL A 44  ? 0.24260 0.16227 0.35550 0.02333  0.00134  -0.06826 44  VAL A CG2   
361  N N     . GLU A 45  ? 0.25349 0.17205 0.37732 0.02912  0.03875  -0.04786 45  GLU A N     
362  C CA    . GLU A 45  ? 0.27137 0.19775 0.38449 0.04514  0.03521  -0.02214 45  GLU A CA    
363  C C     . GLU A 45  ? 0.24962 0.21930 0.37435 0.04072  0.04133  -0.03256 45  GLU A C     
364  O O     . GLU A 45  ? 0.24036 0.25976 0.37899 0.03473  0.04530  -0.01200 45  GLU A O     
365  C CB    . GLU A 45  ? 0.31573 0.17851 0.40674 0.04719  0.05966  -0.00649 45  GLU A CB    
366  C CG    . GLU A 45  ? 0.36663 0.19231 0.42583 0.06622  0.08683  0.02253  45  GLU A CG    
367  C CD    . GLU A 45  ? 0.43634 0.28657 0.44640 0.05102  0.09217  0.04660  45  GLU A CD    
368  O OE1   . GLU A 45  ? 0.44373 0.30950 0.46507 0.11409  0.06794  0.06843  45  GLU A OE1   
369  O OE2   . GLU A 45  ? 0.50592 0.33634 0.46794 0.06043  0.08871  0.03334  45  GLU A OE2   
370  N N     . LYS A 46  ? 0.25098 0.17055 0.36030 0.03194  0.03743  -0.05767 46  LYS A N     
371  C CA    . LYS A 46  ? 0.28212 0.17973 0.37789 0.03620  0.01466  -0.05786 46  LYS A CA    
372  C C     . LYS A 46  ? 0.28205 0.21994 0.37889 0.03476  0.02364  -0.04449 46  LYS A C     
373  O O     . LYS A 46  ? 0.29698 0.22715 0.39571 0.04819  0.04902  -0.01594 46  LYS A O     
374  C CB    . LYS A 46  ? 0.30986 0.20336 0.39232 0.03850  0.03450  -0.05580 46  LYS A CB    
375  C CG    . LYS A 46  ? 0.38722 0.27308 0.40973 0.07251  0.03751  -0.05051 46  LYS A CG    
376  C CD    . LYS A 46  ? 0.45573 0.33305 0.42247 0.09946  0.03667  -0.03139 46  LYS A CD    
377  C CE    . LYS A 46  ? 0.51776 0.38122 0.43289 0.07675  0.04099  -0.01773 46  LYS A CE    
378  N NZ    . LYS A 46  ? 0.55090 0.39753 0.43449 0.06785  0.04756  0.00129  46  LYS A NZ    
379  N N     . GLU A 47  ? 0.29417 0.20940 0.36768 0.03630  0.02264  -0.05216 47  GLU A N     
380  C CA    A GLU A 47  ? 0.29476 0.21237 0.36658 0.02966  0.02117  -0.04235 47  GLU A CA    
381  C CA    B GLU A 47  ? 0.29418 0.24010 0.37021 0.04080  0.01439  -0.03470 47  GLU A CA    
382  C C     . GLU A 47  ? 0.28187 0.20838 0.36430 0.03691  0.03234  -0.03824 47  GLU A C     
383  O O     . GLU A 47  ? 0.25937 0.25664 0.35829 0.03823  0.04718  -0.02018 47  GLU A O     
384  C CB    A GLU A 47  ? 0.31923 0.21701 0.36451 0.03110  0.01085  -0.06432 47  GLU A CB    
385  C CB    B GLU A 47  ? 0.32348 0.29958 0.37406 0.07220  -0.00570 -0.04683 47  GLU A CB    
386  C CG    A GLU A 47  ? 0.35249 0.26973 0.36447 0.03117  -0.00797 -0.08046 47  GLU A CG    
387  C CG    B GLU A 47  ? 0.36707 0.40310 0.38064 0.10144  -0.02545 -0.04676 47  GLU A CG    
388  C CD    A GLU A 47  ? 0.40292 0.30741 0.36837 0.08168  -0.01432 -0.10877 47  GLU A CD    
389  C CD    B GLU A 47  ? 0.41937 0.46791 0.38964 0.14744  -0.02755 -0.04458 47  GLU A CD    
390  O OE1   A GLU A 47  ? 0.43706 0.33653 0.37480 0.12201  -0.02873 -0.10591 47  GLU A OE1   
391  O OE1   B GLU A 47  ? 0.43467 0.48632 0.38781 0.16354  -0.01115 -0.03570 47  GLU A OE1   
392  O OE2   A GLU A 47  ? 0.39859 0.33941 0.36805 0.10439  -0.00684 -0.10591 47  GLU A OE2   
393  O OE2   B GLU A 47  ? 0.45812 0.49057 0.40073 0.15591  -0.03115 -0.05820 47  GLU A OE2   
394  N N     . GLY A 48  ? 0.27971 0.18698 0.35458 0.04064  0.03253  -0.03789 48  GLY A N     
395  C CA    . GLY A 48  ? 0.23501 0.20771 0.34433 0.01646  0.03321  -0.03582 48  GLY A CA    
396  C C     . GLY A 48  ? 0.22442 0.18141 0.33416 0.01628  0.04148  -0.03669 48  GLY A C     
397  O O     . GLY A 48  ? 0.26431 0.21120 0.32878 0.01781  0.05537  -0.02172 48  GLY A O     
398  N N     . LYS A 49  ? 0.22106 0.18548 0.32827 0.01985  0.04108  -0.01600 49  LYS A N     
399  C CA    . LYS A 49  ? 0.21898 0.20135 0.32021 0.02085  0.03889  -0.01595 49  LYS A CA    
400  C C     . LYS A 49  ? 0.21878 0.17851 0.32232 -0.00329 0.01740  -0.02993 49  LYS A C     
401  O O     . LYS A 49  ? 0.22643 0.19949 0.32346 0.00691  0.00953  -0.02976 49  LYS A O     
402  C CB    . LYS A 49  ? 0.27322 0.23280 0.32690 0.02835  0.05614  -0.00290 49  LYS A CB    
403  C CG    . LYS A 49  ? 0.28773 0.31467 0.34379 0.01852  0.10265  0.02667  49  LYS A CG    
404  C CD    . LYS A 49  ? 0.37279 0.38709 0.37038 0.04689  0.11445  0.04050  49  LYS A CD    
405  C CE    . LYS A 49  ? 0.41084 0.45939 0.38485 0.08114  0.12960  0.06059  49  LYS A CE    
406  N NZ    . LYS A 49  ? 0.41575 0.50648 0.39752 0.06006  0.14567  0.07479  49  LYS A NZ    
407  N N     . VAL A 50  ? 0.23274 0.21220 0.32227 0.03155  0.00704  -0.01074 50  VAL A N     
408  C CA    . VAL A 50  ? 0.21390 0.21033 0.31575 0.01905  0.01090  0.00642  50  VAL A CA    
409  C C     . VAL A 50  ? 0.22424 0.20163 0.28780 -0.00498 0.03343  -0.02444 50  VAL A C     
410  O O     . VAL A 50  ? 0.23654 0.19578 0.28063 -0.02292 0.03198  -0.01590 50  VAL A O     
411  C CB    . VAL A 50  ? 0.24749 0.24131 0.33150 -0.00033 0.01985  0.04278  50  VAL A CB    
412  C CG1   . VAL A 50  ? 0.26200 0.26099 0.32461 0.00963  0.01458  0.00936  50  VAL A CG1   
413  C CG2   . VAL A 50  ? 0.26709 0.26688 0.34536 0.00621  0.00908  0.05128  50  VAL A CG2   
414  N N     . VAL A 51  ? 0.21867 0.22068 0.26611 0.02095  0.02658  -0.01929 51  VAL A N     
415  C CA    . VAL A 51  ? 0.24365 0.23080 0.24965 0.03720  0.05581  -0.00044 51  VAL A CA    
416  C C     . VAL A 51  ? 0.22962 0.19828 0.23701 0.00790  0.04575  -0.00733 51  VAL A C     
417  O O     . VAL A 51  ? 0.24455 0.23062 0.25876 0.02434  0.00459  -0.02595 51  VAL A O     
418  C CB    . VAL A 51  ? 0.28548 0.30463 0.27858 0.08085  0.08133  -0.00355 51  VAL A CB    
419  C CG1   . VAL A 51  ? 0.29111 0.32751 0.27610 0.04347  0.09633  0.00690  51  VAL A CG1   
420  C CG2   . VAL A 51  ? 0.32614 0.36059 0.31239 0.09727  0.06621  -0.01855 51  VAL A CG2   
421  N N     . ILE A 52  ? 0.21298 0.20994 0.22535 0.01308  0.06403  -0.00854 52  ILE A N     
422  C CA    . ILE A 52  ? 0.20778 0.21423 0.21072 0.01851  0.04861  -0.01306 52  ILE A CA    
423  C C     . ILE A 52  ? 0.18680 0.19820 0.19997 -0.01195 0.05195  -0.00599 52  ILE A C     
424  O O     . ILE A 52  ? 0.20596 0.22951 0.21256 0.00339  0.05708  0.00035  52  ILE A O     
425  C CB    . ILE A 52  ? 0.21153 0.22145 0.20933 0.00738  0.03710  0.00871  52  ILE A CB    
426  C CG1   . ILE A 52  ? 0.23842 0.24182 0.20517 0.00446  0.03612  -0.00299 52  ILE A CG1   
427  C CG2   . ILE A 52  ? 0.21014 0.23879 0.22243 0.00011  0.04326  0.02288  52  ILE A CG2   
428  C CD1   . ILE A 52  ? 0.26386 0.22497 0.21847 0.00858  0.05419  -0.00628 52  ILE A CD1   
429  N N     . PRO A 53  ? 0.23426 0.23065 0.19072 -0.00642 0.04224  -0.01794 53  PRO A N     
430  C CA    . PRO A 53  ? 0.27022 0.24345 0.18002 0.00684  0.04479  -0.02216 53  PRO A CA    
431  C C     . PRO A 53  ? 0.26208 0.24947 0.17283 -0.01149 0.05113  -0.02363 53  PRO A C     
432  O O     . PRO A 53  ? 0.25977 0.25068 0.14902 0.01928  0.04108  -0.00436 53  PRO A O     
433  C CB    . PRO A 53  ? 0.31105 0.24641 0.18879 0.02388  0.03878  -0.04118 53  PRO A CB    
434  C CG    . PRO A 53  ? 0.32200 0.25882 0.19635 0.02413  0.05695  -0.02450 53  PRO A CG    
435  C CD    . PRO A 53  ? 0.28264 0.23178 0.19057 -0.01730 0.04789  -0.03773 53  PRO A CD    
436  N N     . PRO A 54  ? 0.26763 0.28309 0.18893 -0.00550 0.05351  -0.00972 54  PRO A N     
437  C CA    . PRO A 54  ? 0.24134 0.30524 0.19265 -0.01831 0.05351  0.02396  54  PRO A CA    
438  C C     . PRO A 54  ? 0.24806 0.27202 0.17386 0.00286  0.03638  0.02307  54  PRO A C     
439  O O     . PRO A 54  ? 0.25934 0.29814 0.16381 -0.00059 0.02497  0.01738  54  PRO A O     
440  C CB    . PRO A 54  ? 0.26062 0.33791 0.21131 0.00365  0.06640  0.05534  54  PRO A CB    
441  C CG    . PRO A 54  ? 0.29668 0.35700 0.21123 0.02128  0.08463  0.05548  54  PRO A CG    
442  C CD    . PRO A 54  ? 0.28424 0.33445 0.19976 0.00897  0.09115  0.03059  54  PRO A CD    
443  N N     . LYS A 55  ? 0.24966 0.24647 0.17169 0.03735  0.04569  0.02429  55  LYS A N     
444  C CA    . LYS A 55  ? 0.26607 0.23029 0.18418 0.02030  0.02666  0.01560  55  LYS A CA    
445  C C     . LYS A 55  ? 0.24123 0.22178 0.16893 0.00949  0.00161  -0.00026 55  LYS A C     
446  O O     . LYS A 55  ? 0.24025 0.26981 0.18847 0.00771  0.01106  0.01228  55  LYS A O     
447  C CB    . LYS A 55  ? 0.27627 0.27106 0.19557 -0.02215 0.04733  0.05315  55  LYS A CB    
448  C CG    . LYS A 55  ? 0.32028 0.30516 0.22535 0.00052  0.03945  0.03575  55  LYS A CG    
449  C CD    . LYS A 55  ? 0.36157 0.29814 0.24316 0.01703  0.01512  0.01288  55  LYS A CD    
450  C CE    . LYS A 55  ? 0.37100 0.35480 0.28366 0.01356  0.00841  0.01484  55  LYS A CE    
451  N NZ    . LYS A 55  ? 0.38827 0.39802 0.29006 0.01514  0.00932  0.02630  55  LYS A NZ    
452  N N     . THR A 56  ? 0.24116 0.23000 0.15432 0.00875  0.01732  0.00937  56  THR A N     
453  C CA    . THR A 56  ? 0.24995 0.19930 0.15275 0.00323  0.01886  -0.01212 56  THR A CA    
454  C C     . THR A 56  ? 0.21283 0.18175 0.14342 -0.00729 0.00826  -0.00345 56  THR A C     
455  O O     . THR A 56  ? 0.21985 0.21197 0.14868 0.00057  -0.00914 -0.01656 56  THR A O     
456  C CB    . THR A 56  ? 0.27552 0.22810 0.16083 -0.01548 0.01755  -0.01219 56  THR A CB    
457  O OG1   . THR A 56  ? 0.29943 0.26782 0.16755 0.01110  0.01842  -0.03269 56  THR A OG1   
458  C CG2   . THR A 56  ? 0.28016 0.25056 0.19699 -0.01745 0.01233  -0.00465 56  THR A CG2   
459  N N     . HIS A 57  ? 0.23429 0.18161 0.14543 -0.02383 0.02614  0.00423  57  HIS A N     
460  C CA    . HIS A 57  ? 0.21366 0.18290 0.16077 -0.03800 0.01397  0.02408  57  HIS A CA    
461  C C     . HIS A 57  ? 0.23470 0.18600 0.16217 -0.01275 0.00255  -0.01099 57  HIS A C     
462  O O     . HIS A 57  ? 0.26701 0.21231 0.16446 -0.00361 -0.00518 -0.03896 57  HIS A O     
463  C CB    . HIS A 57  ? 0.25167 0.22877 0.19050 -0.00329 -0.00074 0.00391  57  HIS A CB    
464  C CG    . HIS A 57  ? 0.24631 0.22188 0.22526 -0.00640 -0.01667 -0.01262 57  HIS A CG    
465  N ND1   . HIS A 57  ? 0.29323 0.30562 0.27295 -0.00133 -0.04278 -0.01609 57  HIS A ND1   
466  C CD2   . HIS A 57  ? 0.23110 0.24441 0.25105 -0.00852 -0.04971 -0.02532 57  HIS A CD2   
467  C CE1   . HIS A 57  ? 0.26436 0.27412 0.28334 -0.02229 -0.03858 -0.00586 57  HIS A CE1   
468  N NE2   . HIS A 57  ? 0.26604 0.31812 0.28623 -0.00807 -0.03561 -0.04279 57  HIS A NE2   
469  N N     . ALA A 58  ? 0.24599 0.17095 0.17057 -0.00337 0.00455  -0.00365 58  ALA A N     
470  C CA    . ALA A 58  ? 0.20704 0.19797 0.18905 0.00801  0.03719  0.00492  58  ALA A CA    
471  C C     . ALA A 58  ? 0.18721 0.16956 0.17280 -0.01190 0.01801  -0.02341 58  ALA A C     
472  O O     . ALA A 58  ? 0.23569 0.15734 0.16792 -0.01118 0.01841  -0.01562 58  ALA A O     
473  C CB    . ALA A 58  ? 0.17204 0.25011 0.20256 -0.03364 0.03824  -0.01010 58  ALA A CB    
474  N N     . LEU A 59  ? 0.19602 0.15037 0.18035 -0.00908 0.01378  -0.00846 59  LEU A N     
475  C CA    . LEU A 59  ? 0.15926 0.17015 0.19474 -0.01875 0.02419  -0.00937 59  LEU A CA    
476  C C     . LEU A 59  ? 0.17436 0.16186 0.21074 0.00130  0.00557  -0.02813 59  LEU A C     
477  O O     . LEU A 59  ? 0.21989 0.16928 0.21570 0.00964  0.03014  -0.02098 59  LEU A O     
478  C CB    . LEU A 59  ? 0.18583 0.17209 0.23508 -0.01024 -0.00407 -0.02568 59  LEU A CB    
479  C CG    . LEU A 59  ? 0.18815 0.18148 0.26992 -0.00546 -0.00646 -0.03930 59  LEU A CG    
480  C CD1   . LEU A 59  ? 0.20561 0.23862 0.29004 -0.06083 0.00902  -0.04026 59  LEU A CD1   
481  C CD2   . LEU A 59  ? 0.19060 0.21254 0.28820 0.03844  -0.01362 -0.05110 59  LEU A CD2   
482  N N     . ILE A 60  ? 0.17021 0.16050 0.20449 -0.00273 0.00815  -0.00046 60  ILE A N     
483  C CA    . ILE A 60  ? 0.18367 0.18278 0.21494 0.00302  0.00338  0.01607  60  ILE A CA    
484  C C     . ILE A 60  ? 0.17972 0.15153 0.20809 0.02000  0.02550  0.01971  60  ILE A C     
485  O O     . ILE A 60  ? 0.20123 0.17403 0.21176 0.03181  0.02154  0.00514  60  ILE A O     
486  C CB    . ILE A 60  ? 0.20321 0.16103 0.24528 -0.02061 0.00505  0.01954  60  ILE A CB    
487  C CG1   . ILE A 60  ? 0.22406 0.22174 0.29061 -0.05778 0.01767  0.02940  60  ILE A CG1   
488  C CG2   . ILE A 60  ? 0.19575 0.22703 0.25783 0.01389  0.00508  -0.01917 60  ILE A CG2   
489  C CD1   . ILE A 60  ? 0.28884 0.22507 0.30836 -0.01569 0.00993  0.01083  60  ILE A CD1   
490  N N     . LEU A 61  ? 0.17111 0.14742 0.19992 -0.00718 0.01357  0.01424  61  LEU A N     
491  C CA    . LEU A 61  ? 0.21301 0.13220 0.22131 -0.00274 0.01198  0.01554  61  LEU A CA    
492  C C     . LEU A 61  ? 0.18739 0.16993 0.23996 0.00210  0.00679  0.00862  61  LEU A C     
493  O O     . LEU A 61  ? 0.19227 0.20798 0.25500 -0.00746 0.00869  0.01429  61  LEU A O     
494  C CB    . LEU A 61  ? 0.23612 0.14263 0.25314 -0.02176 0.01335  0.01406  61  LEU A CB    
495  C CG    . LEU A 61  ? 0.21789 0.19034 0.26962 -0.03123 0.01605  0.03042  61  LEU A CG    
496  C CD1   . LEU A 61  ? 0.23139 0.20908 0.25630 -0.03174 0.04205  0.00868  61  LEU A CD1   
497  C CD2   . LEU A 61  ? 0.26209 0.15592 0.29376 -0.01333 -0.01896 0.01244  61  LEU A CD2   
498  N N     . THR A 62  ? 0.19349 0.17011 0.24547 -0.01684 0.00078  0.00042  62  THR A N     
499  C CA    . THR A 62  ? 0.19302 0.17094 0.25421 -0.01173 -0.01931 0.00307  62  THR A CA    
500  C C     . THR A 62  ? 0.20831 0.14014 0.27618 -0.02063 -0.00720 0.04872  62  THR A C     
501  O O     . THR A 62  ? 0.20851 0.15393 0.28303 0.00146  -0.02813 0.02725  62  THR A O     
502  C CB    . THR A 62  ? 0.20015 0.16727 0.24116 -0.01842 0.00164  0.02667  62  THR A CB    
503  O OG1   . THR A 62  ? 0.20483 0.18462 0.23419 -0.00462 0.01991  0.01510  62  THR A OG1   
504  C CG2   . THR A 62  ? 0.21103 0.15389 0.23780 0.00555  -0.01188 0.02600  62  THR A CG2   
505  N N     . LEU A 63  ? 0.20701 0.13769 0.29216 0.00186  -0.00908 0.04216  63  LEU A N     
506  C CA    . LEU A 63  ? 0.21166 0.14496 0.30826 -0.01459 -0.03685 0.04569  63  LEU A CA    
507  C C     . LEU A 63  ? 0.23992 0.14114 0.30202 -0.00156 -0.04652 0.06635  63  LEU A C     
508  O O     . LEU A 63  ? 0.28782 0.18452 0.32573 -0.00996 -0.03371 0.07906  63  LEU A O     
509  C CB    . LEU A 63  ? 0.24657 0.14687 0.34372 0.01911  -0.04544 -0.01101 63  LEU A CB    
510  C CG    . LEU A 63  ? 0.26759 0.17142 0.37395 0.01477  -0.02653 -0.02848 63  LEU A CG    
511  C CD1   . LEU A 63  ? 0.31573 0.21050 0.38731 0.06235  -0.01679 -0.02169 63  LEU A CD1   
512  C CD2   . LEU A 63  ? 0.22710 0.24271 0.39171 0.00151  -0.01574 -0.02629 63  LEU A CD2   
513  N N     . GLU A 64  ? 0.24011 0.17129 0.28433 0.01106  -0.02495 0.04853  64  GLU A N     
514  C CA    . GLU A 64  ? 0.25322 0.17237 0.28183 -0.01242 -0.03969 0.04770  64  GLU A CA    
515  C C     . GLU A 64  ? 0.25427 0.19250 0.28030 -0.02661 -0.05523 0.05421  64  GLU A C     
516  O O     . GLU A 64  ? 0.26507 0.17528 0.27209 -0.01745 -0.03237 0.04153  64  GLU A O     
517  C CB    . GLU A 64  ? 0.24108 0.20199 0.28264 -0.01464 -0.04641 0.03528  64  GLU A CB    
518  C CG    . GLU A 64  ? 0.26498 0.22506 0.30493 -0.00074 -0.02773 0.04699  64  GLU A CG    
519  C CD    . GLU A 64  ? 0.27295 0.22454 0.31411 0.03673  -0.04093 0.03653  64  GLU A CD    
520  O OE1   . GLU A 64  ? 0.27570 0.17724 0.29935 -0.00726 -0.02194 0.04674  64  GLU A OE1   
521  O OE2   . GLU A 64  ? 0.29083 0.21080 0.33666 0.00948  -0.01812 0.02815  64  GLU A OE2   
522  N N     . ARG A 65  ? 0.28644 0.19528 0.29131 -0.02433 -0.02732 0.07798  65  ARG A N     
523  C CA    . ARG A 65  ? 0.31204 0.20041 0.29854 -0.04903 -0.02359 0.09136  65  ARG A CA    
524  C C     . ARG A 65  ? 0.31631 0.24079 0.28212 -0.02997 -0.03860 0.09316  65  ARG A C     
525  O O     . ARG A 65  ? 0.31869 0.26391 0.29290 -0.01661 -0.04949 0.08064  65  ARG A O     
526  C CB    . ARG A 65  ? 0.35732 0.21063 0.32901 -0.03650 -0.02187 0.11891  65  ARG A CB    
527  C CG    . ARG A 65  ? 0.40570 0.20070 0.36415 -0.04502 -0.00575 0.12788  65  ARG A CG    
528  C CD    . ARG A 65  ? 0.45830 0.26898 0.38602 -0.03111 -0.00003 0.14405  65  ARG A CD    
529  N NE    . ARG A 65  ? 0.50499 0.28939 0.39499 -0.00616 -0.00223 0.16625  65  ARG A NE    
530  C CZ    . ARG A 65  ? 0.52983 0.30920 0.41071 0.00702  0.00273  0.15698  65  ARG A CZ    
531  N NH1   . ARG A 65  ? 0.54896 0.30865 0.41825 0.02085  -0.00140 0.14408  65  ARG A NH1   
532  N NH2   . ARG A 65  ? 0.53174 0.35062 0.41458 0.00405  0.02335  0.16454  65  ARG A NH2   
533  N N     . VAL A 66  ? 0.31688 0.24255 0.26313 -0.04371 -0.03007 0.10833  66  VAL A N     
534  C CA    . VAL A 66  ? 0.32433 0.24510 0.25464 -0.08586 -0.02800 0.08852  66  VAL A CA    
535  C C     . VAL A 66  ? 0.32872 0.27350 0.23935 -0.08874 -0.02390 0.09192  66  VAL A C     
536  O O     . VAL A 66  ? 0.32425 0.27076 0.23534 -0.06570 -0.02844 0.07606  66  VAL A O     
537  C CB    . VAL A 66  ? 0.35099 0.24788 0.27247 -0.11609 0.00141  0.06451  66  VAL A CB    
538  C CG1   . VAL A 66  ? 0.39017 0.24505 0.27203 -0.05451 -0.01845 0.05873  66  VAL A CG1   
539  C CG2   . VAL A 66  ? 0.35310 0.27838 0.29523 -0.11224 0.01149  0.06922  66  VAL A CG2   
540  N N     . LYS A 67  ? 0.36531 0.27068 0.23854 -0.05961 -0.03029 0.09781  67  LYS A N     
541  C CA    . LYS A 67  ? 0.37944 0.26310 0.24957 -0.07333 -0.03412 0.09158  67  LYS A CA    
542  C C     . LYS A 67  ? 0.39992 0.29705 0.23804 -0.11191 -0.03692 0.07803  67  LYS A C     
543  O O     . LYS A 67  ? 0.41257 0.34596 0.25336 -0.07642 -0.04473 0.09244  67  LYS A O     
544  C CB    . LYS A 67  ? 0.40880 0.32640 0.28944 -0.03608 -0.02420 0.10762  67  LYS A CB    
545  C CG    . LYS A 67  ? 0.41800 0.35374 0.30815 -0.04588 -0.02090 0.11731  67  LYS A CG    
546  C CD    . LYS A 67  ? 0.43636 0.34660 0.31343 -0.01959 -0.02544 0.11963  67  LYS A CD    
547  N N     . LEU A 68  ? 0.42025 0.25976 0.21835 -0.09287 -0.01928 0.09677  68  LEU A N     
548  C CA    . LEU A 68  ? 0.46733 0.29854 0.22021 -0.07822 -0.00029 0.08381  68  LEU A CA    
549  C C     . LEU A 68  ? 0.49776 0.34588 0.22283 -0.08264 -0.01758 0.08754  68  LEU A C     
550  O O     . LEU A 68  ? 0.50747 0.38324 0.22755 -0.10930 -0.01172 0.06824  68  LEU A O     
551  C CB    . LEU A 68  ? 0.47679 0.29907 0.22062 -0.06032 0.03549  0.10630  68  LEU A CB    
552  C CG    . LEU A 68  ? 0.49896 0.32988 0.23663 0.01388  0.07654  0.13336  68  LEU A CG    
553  C CD1   . LEU A 68  ? 0.52377 0.39224 0.26841 0.05395  0.05688  0.10589  68  LEU A CD1   
554  C CD2   . LEU A 68  ? 0.48853 0.35573 0.23827 0.04051  0.08478  0.12398  68  LEU A CD2   
555  N N     . PRO A 69  ? 0.50776 0.34259 0.21293 -0.09916 -0.02828 0.08521  69  PRO A N     
556  C CA    . PRO A 69  ? 0.51313 0.37462 0.21006 -0.09745 -0.02037 0.06912  69  PRO A CA    
557  C C     . PRO A 69  ? 0.50767 0.39077 0.21890 -0.10019 -0.00445 0.08097  69  PRO A C     
558  O O     . PRO A 69  ? 0.50998 0.36666 0.21144 -0.07546 -0.01368 0.08788  69  PRO A O     
559  C CB    . PRO A 69  ? 0.51678 0.44808 0.21993 -0.06141 -0.04018 0.05229  69  PRO A CB    
560  C CG    . PRO A 69  ? 0.51882 0.44265 0.22301 -0.06788 -0.02934 0.07321  69  PRO A CG    
561  C CD    . PRO A 69  ? 0.51181 0.37602 0.21243 -0.10018 -0.05043 0.07890  69  PRO A CD    
562  N N     . ASP A 70  ? 0.51246 0.41046 0.24585 -0.09694 0.01471  0.08483  70  ASP A N     
563  C CA    . ASP A 70  ? 0.48270 0.42135 0.25693 -0.14785 0.04458  0.10275  70  ASP A CA    
564  C C     . ASP A 70  ? 0.46177 0.41938 0.23263 -0.12657 0.04511  0.11022  70  ASP A C     
565  O O     . ASP A 70  ? 0.45674 0.43516 0.23466 -0.11712 0.03788  0.10758  70  ASP A O     
566  C CB    . ASP A 70  ? 0.49322 0.46477 0.26918 -0.17519 0.05107  0.09372  70  ASP A CB    
567  N N     . ASP A 71  ? 0.44686 0.39988 0.20112 -0.07240 0.03505  0.12596  71  ASP A N     
568  C CA    . ASP A 71  ? 0.43630 0.40073 0.18107 -0.03944 0.01353  0.09892  71  ASP A CA    
569  C C     . ASP A 71  ? 0.38221 0.32229 0.17033 -0.04746 -0.00255 0.08506  71  ASP A C     
570  O O     . ASP A 71  ? 0.39490 0.33476 0.16485 -0.01444 -0.01967 0.08640  71  ASP A O     
571  C CB    . ASP A 71  ? 0.46343 0.42444 0.18779 0.01059  0.00611  0.11101  71  ASP A CB    
572  C CG    . ASP A 71  ? 0.49323 0.42526 0.21266 0.02198  0.00244  0.10385  71  ASP A CG    
573  O OD1   . ASP A 71  ? 0.50547 0.41071 0.22260 0.02270  0.01064  0.10825  71  ASP A OD1   
574  O OD2   . ASP A 71  ? 0.51153 0.45543 0.23615 0.03351  -0.01023 0.08152  71  ASP A OD2   
575  N N     . VAL A 72  ? 0.32956 0.31987 0.16097 -0.05003 -0.00124 0.09294  72  VAL A N     
576  C CA    . VAL A 72  ? 0.30305 0.30725 0.16302 -0.06136 -0.00756 0.07827  72  VAL A CA    
577  C C     . VAL A 72  ? 0.30900 0.29369 0.16748 -0.05274 -0.01476 0.04615  72  VAL A C     
578  O O     . VAL A 72  ? 0.36132 0.29658 0.18202 -0.05805 -0.01558 0.06771  72  VAL A O     
579  C CB    . VAL A 72  ? 0.30776 0.34832 0.18448 -0.00338 -0.00370 0.09410  72  VAL A CB    
580  C CG1   . VAL A 72  ? 0.28521 0.39164 0.20432 -0.02128 0.01056  0.09492  72  VAL A CG1   
581  C CG2   . VAL A 72  ? 0.33032 0.35080 0.19629 0.03391  -0.03918 0.08950  72  VAL A CG2   
582  N N     . MET A 73  ? 0.27758 0.28847 0.14199 -0.04243 0.00662  0.07025  73  MET A N     
583  C CA    . MET A 73  ? 0.27534 0.26740 0.14560 0.01373  0.01855  0.05784  73  MET A CA    
584  C C     . MET A 73  ? 0.24224 0.27191 0.15355 0.00022  0.00394  0.04216  73  MET A C     
585  O O     . MET A 73  ? 0.25128 0.31431 0.15882 -0.01334 -0.00871 0.05025  73  MET A O     
586  C CB    . MET A 73  ? 0.25630 0.30731 0.13413 0.03016  0.02221  0.05395  73  MET A CB    
587  C CG    . MET A 73  ? 0.22463 0.34926 0.16191 -0.00905 0.01372  0.03496  73  MET A CG    
588  S SD    . MET A 73  ? 0.26639 0.31444 0.18812 0.01049  0.03219  0.04739  73  MET A SD    
589  C CE    . MET A 73  ? 0.26422 0.37417 0.19648 -0.02048 0.02997  0.03266  73  MET A CE    
590  N N     . GLY A 74  ? 0.22085 0.23656 0.14442 0.00568  0.02162  0.04530  74  GLY A N     
591  C CA    . GLY A 74  ? 0.23482 0.24138 0.13424 0.00851  0.01128  0.05933  74  GLY A CA    
592  C C     . GLY A 74  ? 0.20629 0.20646 0.13660 0.01993  -0.00026 0.04923  74  GLY A C     
593  O O     . GLY A 74  ? 0.21275 0.21368 0.15907 0.01284  -0.00693 0.02289  74  GLY A O     
594  N N     . ASP A 75  ? 0.20054 0.19266 0.13773 0.00194  0.01634  0.04595  75  ASP A N     
595  C CA    . ASP A 75  ? 0.20586 0.19963 0.12337 0.00048  0.01232  0.03230  75  ASP A CA    
596  C C     . ASP A 75  ? 0.19057 0.19713 0.12747 -0.00014 0.00136  0.04590  75  ASP A C     
597  O O     . ASP A 75  ? 0.20130 0.22551 0.14217 0.01941  -0.00922 0.02215  75  ASP A O     
598  C CB    . ASP A 75  ? 0.23183 0.22365 0.17460 0.01359  0.02947  0.00051  75  ASP A CB    
599  C CG    . ASP A 75  ? 0.24514 0.24176 0.20605 -0.00767 0.02068  0.00481  75  ASP A CG    
600  O OD1   . ASP A 75  ? 0.27469 0.22244 0.20556 0.02638  -0.02210 0.02421  75  ASP A OD1   
601  O OD2   . ASP A 75  ? 0.22635 0.26955 0.21091 -0.01361 0.03129  -0.00187 75  ASP A OD2   
602  N N     . MET A 76  ? 0.18719 0.18160 0.13238 0.02116  0.00368  0.01267  76  MET A N     
603  C CA    . MET A 76  ? 0.18659 0.17374 0.13996 0.00726  -0.00319 0.00685  76  MET A CA    
604  C C     . MET A 76  ? 0.18834 0.19493 0.15109 0.00113  -0.01618 0.01410  76  MET A C     
605  O O     . MET A 76  ? 0.18439 0.19854 0.15889 -0.01674 -0.01357 0.00905  76  MET A O     
606  C CB    . MET A 76  ? 0.22151 0.16629 0.14951 0.00978  -0.00994 0.00662  76  MET A CB    
607  C CG    . MET A 76  ? 0.23917 0.17446 0.17828 -0.02441 -0.02033 0.02340  76  MET A CG    
608  S SD    . MET A 76  ? 0.23347 0.19198 0.21465 0.00674  -0.01036 0.01566  76  MET A SD    
609  C CE    . MET A 76  ? 0.20291 0.24187 0.21626 -0.03598 -0.01405 0.02906  76  MET A CE    
610  N N     . LYS A 77  ? 0.20705 0.16703 0.15091 -0.01542 -0.02528 0.02466  77  LYS A N     
611  C CA    . LYS A 77  ? 0.17869 0.16332 0.14352 -0.01524 -0.02162 0.04285  77  LYS A CA    
612  C C     . LYS A 77  ? 0.17438 0.16008 0.13442 0.00990  -0.02690 0.03537  77  LYS A C     
613  O O     . LYS A 77  ? 0.22968 0.15659 0.14564 0.02764  -0.01373 0.03071  77  LYS A O     
614  C CB    . LYS A 77  ? 0.20363 0.18365 0.16875 -0.01915 -0.01307 0.01121  77  LYS A CB    
615  C CG    . LYS A 77  ? 0.23345 0.22412 0.19873 -0.01694 0.01979  -0.02509 77  LYS A CG    
616  C CD    . LYS A 77  ? 0.25924 0.19942 0.21277 -0.01918 0.00111  -0.05902 77  LYS A CD    
617  C CE    . LYS A 77  ? 0.35716 0.27666 0.24517 0.02620  0.01997  -0.04533 77  LYS A CE    
618  N NZ    . LYS A 77  ? 0.41798 0.26499 0.27155 0.00218  0.04137  -0.04552 77  LYS A NZ    
619  N N     . LEU A 78  ? 0.20183 0.16060 0.12795 0.01377  -0.00323 0.00865  78  LEU A N     
620  C CA    . LEU A 78  ? 0.22712 0.16039 0.13723 0.00022  0.00040  0.01748  78  LEU A CA    
621  C C     . LEU A 78  ? 0.21246 0.13680 0.16351 -0.00568 0.01832  -0.01006 78  LEU A C     
622  O O     . LEU A 78  ? 0.23171 0.18185 0.19304 -0.03553 0.02562  -0.02623 78  LEU A O     
623  C CB    . LEU A 78  ? 0.33071 0.16369 0.17086 0.03241  0.03221  0.04107  78  LEU A CB    
624  C CG    . LEU A 78  ? 0.36984 0.19260 0.18836 0.05914  0.01123  0.01489  78  LEU A CG    
625  C CD1   . LEU A 78  ? 0.36576 0.16416 0.19813 0.00955  0.00294  -0.00494 78  LEU A CD1   
626  C CD2   . LEU A 78  ? 0.34289 0.16239 0.17392 0.02369  0.01449  0.05304  78  LEU A CD2   
627  N N     . ARG A 79  ? 0.21348 0.17061 0.20481 0.00842  0.02716  0.00022  79  ARG A N     
628  C CA    . ARG A 79  ? 0.24514 0.20033 0.24584 0.01805  0.00037  -0.02366 79  ARG A CA    
629  C C     . ARG A 79  ? 0.22421 0.18922 0.24790 -0.01524 0.00284  -0.01895 79  ARG A C     
630  O O     . ARG A 79  ? 0.19700 0.20443 0.24716 -0.02210 0.00989  -0.00430 79  ARG A O     
631  C CB    . ARG A 79  ? 0.30645 0.23803 0.28251 0.00934  -0.01822 0.01438  79  ARG A CB    
632  C CG    . ARG A 79  ? 0.36339 0.31542 0.32842 0.03230  -0.05220 0.01512  79  ARG A CG    
633  C CD    . ARG A 79  ? 0.43377 0.40202 0.38736 0.04800  -0.05361 0.01685  79  ARG A CD    
634  N NE    . ARG A 79  ? 0.48135 0.42934 0.43161 0.04019  -0.04293 0.02563  79  ARG A NE    
635  C CZ    . ARG A 79  ? 0.51304 0.48759 0.45886 0.04402  -0.03141 0.01279  79  ARG A CZ    
636  N NH1   . ARG A 79  ? 0.51793 0.50504 0.46995 0.01298  -0.02871 0.01732  79  ARG A NH1   
637  N NH2   . ARG A 79  ? 0.52383 0.50151 0.47528 0.03020  -0.05008 -0.02200 79  ARG A NH2   
638  N N     . SER A 80  ? 0.24935 0.19969 0.27828 -0.00500 0.00683  -0.00289 80  SER A N     
639  C CA    . SER A 80  ? 0.23107 0.21790 0.31107 -0.02510 -0.01361 -0.01689 80  SER A CA    
640  C C     . SER A 80  ? 0.19152 0.18365 0.31095 -0.00228 0.00414  -0.00731 80  SER A C     
641  O O     . SER A 80  ? 0.20497 0.19205 0.29263 -0.00472 0.02224  -0.00092 80  SER A O     
642  C CB    . SER A 80  ? 0.24702 0.30591 0.34970 -0.06216 -0.04172 -0.04106 80  SER A CB    
643  O OG    . SER A 80  ? 0.35443 0.43079 0.37173 0.01285  -0.04035 -0.03348 80  SER A OG    
644  N N     . SER A 81  ? 0.16425 0.20123 0.33053 -0.02572 0.01188  -0.01340 81  SER A N     
645  C CA    . SER A 81  ? 0.18603 0.22554 0.34610 -0.00412 0.03488  0.01711  81  SER A CA    
646  C C     . SER A 81  ? 0.21070 0.18673 0.32698 -0.00755 0.03456  -0.00456 81  SER A C     
647  O O     . SER A 81  ? 0.26011 0.21062 0.34211 -0.02538 0.06034  -0.00746 81  SER A O     
648  C CB    . SER A 81  ? 0.24922 0.27954 0.38406 0.04950  0.02418  0.02940  81  SER A CB    
649  O OG    . SER A 81  ? 0.36583 0.37944 0.41265 0.15093  0.03876  0.04164  81  SER A OG    
650  N N     . LEU A 82  ? 0.18976 0.16734 0.31402 -0.00255 0.01768  -0.01289 82  LEU A N     
651  C CA    . LEU A 82  ? 0.19880 0.16532 0.29701 -0.00101 0.01696  -0.00240 82  LEU A CA    
652  C C     . LEU A 82  ? 0.19115 0.15114 0.26896 -0.00092 0.01518  -0.00746 82  LEU A C     
653  O O     . LEU A 82  ? 0.20067 0.17937 0.25149 -0.00340 0.04376  0.00508  82  LEU A O     
654  C CB    . LEU A 82  ? 0.20042 0.16483 0.30551 -0.00151 0.02412  0.01963  82  LEU A CB    
655  C CG    . LEU A 82  ? 0.22140 0.18546 0.34198 0.01159  0.06367  0.04522  82  LEU A CG    
656  C CD1   . LEU A 82  ? 0.25972 0.19727 0.33853 -0.02483 0.04388  0.03789  82  LEU A CD1   
657  C CD2   . LEU A 82  ? 0.31209 0.23176 0.36808 0.05701  0.09023  0.04617  82  LEU A CD2   
658  N N     . ALA A 83  ? 0.15300 0.15176 0.26730 0.00083  -0.00162 -0.01780 83  ALA A N     
659  C CA    . ALA A 83  ? 0.18540 0.15295 0.28080 0.00204  -0.02022 -0.02016 83  ALA A CA    
660  C C     . ALA A 83  ? 0.20473 0.18459 0.27967 -0.00398 -0.01815 -0.01879 83  ALA A C     
661  O O     . ALA A 83  ? 0.23719 0.19221 0.28014 0.00637  -0.00336 0.01353  83  ALA A O     
662  C CB    . ALA A 83  ? 0.22610 0.19040 0.29878 0.02647  -0.01984 -0.02860 83  ALA A CB    
663  N N     . ARG A 84  ? 0.18335 0.15560 0.29090 -0.02201 0.00766  0.01014  84  ARG A N     
664  C CA    . ARG A 84  ? 0.22813 0.19617 0.30676 -0.05589 0.01643  0.02060  84  ARG A CA    
665  C C     . ARG A 84  ? 0.24545 0.19846 0.30544 -0.05034 0.03511  0.02378  84  ARG A C     
666  O O     . ARG A 84  ? 0.33951 0.23325 0.32308 -0.04963 0.03472  0.02248  84  ARG A O     
667  C CB    . ARG A 84  ? 0.26462 0.23756 0.33209 -0.04552 0.00190  0.00921  84  ARG A CB    
668  C CG    . ARG A 84  ? 0.28957 0.19892 0.37392 -0.04309 -0.02987 -0.00350 84  ARG A CG    
669  C CD    . ARG A 84  ? 0.31476 0.27430 0.40799 -0.02312 -0.04034 -0.01160 84  ARG A CD    
670  N NE    . ARG A 84  ? 0.33491 0.29239 0.43933 -0.03372 -0.04413 0.00001  84  ARG A NE    
671  C CZ    . ARG A 84  ? 0.34298 0.38680 0.45938 -0.06239 -0.03370 -0.02466 84  ARG A CZ    
672  N NH1   . ARG A 84  ? 0.34513 0.38204 0.45273 -0.06325 -0.00777 -0.03093 84  ARG A NH1   
673  N NH2   . ARG A 84  ? 0.31766 0.39582 0.47596 -0.08640 -0.03190 -0.03007 84  ARG A NH2   
674  N N     . GLU A 85  ? 0.16935 0.22785 0.29082 -0.02903 0.04662  0.01284  85  GLU A N     
675  C CA    . GLU A 85  ? 0.20534 0.22992 0.27541 -0.02067 0.04842  0.03403  85  GLU A CA    
676  C C     . GLU A 85  ? 0.22558 0.26996 0.25818 -0.00803 0.04484  0.02173  85  GLU A C     
677  O O     . GLU A 85  ? 0.24965 0.31024 0.26946 0.00464  0.05200  -0.00497 85  GLU A O     
678  C CB    . GLU A 85  ? 0.24193 0.27280 0.30085 0.00104  0.03174  0.03006  85  GLU A CB    
679  C CG    . GLU A 85  ? 0.27054 0.31689 0.32231 -0.00290 0.02264  0.03185  85  GLU A CG    
680  C CD    . GLU A 85  ? 0.34010 0.35137 0.34816 -0.00332 0.00677  0.03790  85  GLU A CD    
681  O OE1   . GLU A 85  ? 0.38767 0.32565 0.35426 0.06218  0.01664  0.02237  85  GLU A OE1   
682  O OE2   . GLU A 85  ? 0.33786 0.34620 0.36304 -0.00365 -0.00840 0.05638  85  GLU A OE2   
683  N N     . GLY A 86  ? 0.18478 0.22586 0.22579 -0.01482 0.03513  0.04787  86  GLY A N     
684  C CA    . GLY A 86  ? 0.22299 0.25288 0.20460 0.01385  0.03508  0.03573  86  GLY A CA    
685  C C     . GLY A 86  ? 0.20305 0.19182 0.17443 -0.01496 0.04133  0.02109  86  GLY A C     
686  O O     . GLY A 86  ? 0.21236 0.20293 0.18306 -0.00175 0.02003  0.01250  86  GLY A O     
687  N N     . LEU A 87  ? 0.22546 0.15706 0.17962 -0.00289 0.05761  0.00422  87  LEU A N     
688  C CA    . LEU A 87  ? 0.17701 0.14736 0.18582 -0.00292 0.02795  0.00958  87  LEU A CA    
689  C C     . LEU A 87  ? 0.16693 0.15260 0.17072 0.00218  0.00422  0.00091  87  LEU A C     
690  O O     . LEU A 87  ? 0.17350 0.17315 0.16202 0.00069  0.02060  0.01104  87  LEU A O     
691  C CB    . LEU A 87  ? 0.19930 0.16324 0.19495 0.01551  0.03198  -0.00469 87  LEU A CB    
692  C CG    . LEU A 87  ? 0.22219 0.18803 0.20899 0.01510  0.01882  -0.00816 87  LEU A CG    
693  C CD1   . LEU A 87  ? 0.27514 0.18692 0.24494 0.02894  -0.01328 -0.01184 87  LEU A CD1   
694  C CD2   . LEU A 87  ? 0.24496 0.21165 0.20644 -0.00155 0.02362  -0.01715 87  LEU A CD2   
695  N N     . LEU A 88  ? 0.18114 0.15222 0.16295 0.00506  -0.00037 0.00287  88  LEU A N     
696  C CA    . LEU A 88  ? 0.14522 0.17413 0.16566 0.00396  0.01527  -0.00809 88  LEU A CA    
697  C C     . LEU A 88  ? 0.16440 0.17558 0.16376 -0.04476 0.01454  -0.01255 88  LEU A C     
698  O O     . LEU A 88  ? 0.24536 0.22255 0.16292 -0.07415 0.02792  -0.03291 88  LEU A O     
699  C CB    . LEU A 88  ? 0.20645 0.19033 0.19960 0.00355  0.00743  -0.01014 88  LEU A CB    
700  C CG    . LEU A 88  ? 0.23596 0.19122 0.19609 0.00444  0.00695  -0.01022 88  LEU A CG    
701  C CD1   . LEU A 88  ? 0.30730 0.25921 0.19907 -0.01123 -0.02771 -0.00907 88  LEU A CD1   
702  C CD2   . LEU A 88  ? 0.23974 0.27139 0.26370 0.02337  -0.00354 -0.04943 88  LEU A CD2   
703  N N     . GLY A 89  ? 0.16069 0.19804 0.15028 -0.01275 0.02225  0.01309  89  GLY A N     
704  C CA    . GLY A 89  ? 0.15403 0.20176 0.14372 -0.00256 0.03748  0.02138  89  GLY A CA    
705  C C     . GLY A 89  ? 0.15975 0.17747 0.16776 0.00804  0.03207  0.00523  89  GLY A C     
706  O O     . GLY A 89  ? 0.19008 0.19300 0.21885 0.01493  0.02278  -0.02614 89  GLY A O     
707  N N     . SER A 90  ? 0.15655 0.18772 0.13887 -0.00754 0.01695  -0.00027 90  SER A N     
708  C CA    . SER A 90  ? 0.17907 0.18204 0.12221 0.00040  0.01367  -0.00646 90  SER A CA    
709  C C     . SER A 90  ? 0.17358 0.15410 0.15490 -0.00583 0.00343  0.00368  90  SER A C     
710  O O     . SER A 90  ? 0.19382 0.17152 0.16723 -0.01786 0.00279  0.02248  90  SER A O     
711  C CB    . SER A 90  ? 0.16976 0.19546 0.13073 0.01664  0.01374  -0.02802 90  SER A CB    
712  O OG    . SER A 90  ? 0.19885 0.17771 0.14630 0.02851  0.01594  -0.01856 90  SER A OG    
713  N N     . PHE A 91  ? 0.16886 0.19350 0.15352 0.02752  0.00936  0.00861  91  PHE A N     
714  C CA    . PHE A 91  ? 0.16493 0.22934 0.15541 0.01755  0.00515  0.02342  91  PHE A CA    
715  C C     . PHE A 91  ? 0.16777 0.21869 0.14898 0.01791  0.03762  0.00547  91  PHE A C     
716  O O     . PHE A 91  ? 0.22623 0.24359 0.15101 0.02461  0.03891  0.01025  91  PHE A O     
717  C CB    . PHE A 91  ? 0.19595 0.33600 0.16987 0.00231  -0.00742 0.03706  91  PHE A CB    
718  C CG    . PHE A 91  ? 0.20287 0.32277 0.18960 -0.00932 0.01317  0.04761  91  PHE A CG    
719  C CD1   . PHE A 91  ? 0.22279 0.27584 0.24710 0.05228  0.02312  0.05229  91  PHE A CD1   
720  C CD2   . PHE A 91  ? 0.21804 0.39304 0.19883 -0.03169 0.01826  0.01308  91  PHE A CD2   
721  C CE1   . PHE A 91  ? 0.16545 0.28565 0.26699 0.01513  0.01301  0.03348  91  PHE A CE1   
722  C CE2   . PHE A 91  ? 0.17918 0.39381 0.21615 -0.01015 -0.02766 0.01320  91  PHE A CE2   
723  C CZ    . PHE A 91  ? 0.18723 0.32531 0.24790 0.02589  -0.03005 0.03431  91  PHE A CZ    
724  N N     . ALA A 92  ? 0.17311 0.20421 0.13381 0.01494  0.02558  0.01279  92  ALA A N     
725  C CA    . ALA A 92  ? 0.17564 0.20664 0.14037 -0.00375 0.01329  -0.00484 92  ALA A CA    
726  C C     . ALA A 92  ? 0.19256 0.17907 0.14522 -0.00550 0.01068  0.01292  92  ALA A C     
727  O O     . ALA A 92  ? 0.19729 0.20026 0.14233 -0.01578 0.02136  0.01988  92  ALA A O     
728  C CB    . ALA A 92  ? 0.18600 0.21958 0.15536 -0.01474 -0.01037 0.00250  92  ALA A CB    
729  N N     . TRP A 93  ? 0.20155 0.18643 0.13676 -0.00062 0.02741  0.02608  93  TRP A N     
730  C CA    . TRP A 93  ? 0.20154 0.19987 0.12381 0.03478  0.04008  0.04185  93  TRP A CA    
731  C C     . TRP A 93  ? 0.19698 0.20641 0.14022 -0.01121 0.01690  0.03625  93  TRP A C     
732  O O     . TRP A 93  ? 0.21182 0.20675 0.14745 -0.01331 -0.00372 0.02635  93  TRP A O     
733  C CB    . TRP A 93  ? 0.17537 0.19442 0.11694 0.01323  0.03122  0.02852  93  TRP A CB    
734  C CG    . TRP A 93  ? 0.18903 0.19745 0.11598 0.01446  0.01693  0.01759  93  TRP A CG    
735  C CD1   . TRP A 93  ? 0.18195 0.23243 0.13244 0.02287  0.02634  0.01735  93  TRP A CD1   
736  C CD2   . TRP A 93  ? 0.20478 0.20586 0.13921 -0.00408 0.02175  0.01216  93  TRP A CD2   
737  N NE1   . TRP A 93  ? 0.20670 0.21475 0.13756 0.00953  0.00914  -0.00799 93  TRP A NE1   
738  C CE2   . TRP A 93  ? 0.20487 0.19494 0.13986 -0.00963 0.02170  0.00559  93  TRP A CE2   
739  C CE3   . TRP A 93  ? 0.18109 0.23519 0.14083 -0.01342 0.02670  -0.00809 93  TRP A CE3   
740  C CZ2   . TRP A 93  ? 0.23031 0.24439 0.15827 0.00360  0.02484  0.01286  93  TRP A CZ2   
741  C CZ3   . TRP A 93  ? 0.23061 0.24563 0.15340 -0.00621 0.02691  -0.00843 93  TRP A CZ3   
742  C CH2   . TRP A 93  ? 0.24429 0.22629 0.15566 0.01065  0.02557  -0.00841 93  TRP A CH2   
743  N N     . VAL A 94  ? 0.20799 0.19560 0.14093 -0.00169 0.01935  0.05157  94  VAL A N     
744  C CA    . VAL A 94  ? 0.19241 0.20246 0.16611 -0.01147 0.04404  0.06048  94  VAL A CA    
745  C C     . VAL A 94  ? 0.20872 0.19315 0.16413 -0.01298 0.02159  0.03495  94  VAL A C     
746  O O     . VAL A 94  ? 0.23456 0.23187 0.16408 -0.01509 0.01039  0.03755  94  VAL A O     
747  C CB    . VAL A 94  ? 0.23096 0.19981 0.18640 0.00563  0.03250  0.04685  94  VAL A CB    
748  C CG1   . VAL A 94  ? 0.26516 0.20714 0.18325 0.02052  0.04446  0.06464  94  VAL A CG1   
749  C CG2   . VAL A 94  ? 0.25102 0.22801 0.17651 0.00872  0.04468  0.05686  94  VAL A CG2   
750  N N     . ASP A 95  ? 0.22267 0.23202 0.17754 -0.02958 0.04159  0.03615  95  ASP A N     
751  C CA    . ASP A 95  ? 0.24991 0.29496 0.19469 -0.03845 0.05335  0.02225  95  ASP A CA    
752  C C     . ASP A 95  ? 0.28170 0.26791 0.18872 -0.02860 0.03950  0.02430  95  ASP A C     
753  O O     . ASP A 95  ? 0.31144 0.25688 0.19643 -0.02005 0.06078  0.05229  95  ASP A O     
754  C CB    . ASP A 95  ? 0.27948 0.35596 0.21320 -0.04072 0.05140  0.01119  95  ASP A CB    
755  C CG    . ASP A 95  ? 0.31970 0.39697 0.21710 -0.04949 0.04089  0.01064  95  ASP A CG    
756  O OD1   . ASP A 95  ? 0.36540 0.41621 0.22647 0.06240  0.00427  0.00219  95  ASP A OD1   
757  O OD2   . ASP A 95  ? 0.33593 0.37233 0.19691 -0.04580 0.04075  0.03501  95  ASP A OD2   
758  N N     . PRO A 96  ? 0.30371 0.28173 0.17582 -0.04627 0.02579  0.04706  96  PRO A N     
759  C CA    . PRO A 96  ? 0.32205 0.27836 0.15623 -0.06412 0.03250  0.05535  96  PRO A CA    
760  C C     . PRO A 96  ? 0.36853 0.28548 0.17175 -0.11030 0.02733  0.05608  96  PRO A C     
761  O O     . PRO A 96  ? 0.41196 0.35119 0.17928 -0.09525 0.02183  0.06408  96  PRO A O     
762  C CB    . PRO A 96  ? 0.35487 0.29286 0.14990 -0.05817 0.05774  0.06815  96  PRO A CB    
763  C CG    . PRO A 96  ? 0.35793 0.33586 0.17817 -0.01800 0.02777  0.04866  96  PRO A CG    
764  C CD    . PRO A 96  ? 0.31628 0.31886 0.17801 -0.05046 0.03854  0.04010  96  PRO A CD    
765  N N     . GLY A 97  ? 0.42373 0.26490 0.18537 -0.07928 0.03577  0.06003  97  GLY A N     
766  C CA    . GLY A 97  ? 0.42700 0.25513 0.19244 -0.07403 0.03402  0.04001  97  GLY A CA    
767  C C     . GLY A 97  ? 0.41483 0.26294 0.20068 -0.07866 0.03653  0.05449  97  GLY A C     
768  O O     . GLY A 97  ? 0.44023 0.23210 0.22949 -0.05467 0.02096  0.04876  97  GLY A O     
769  N N     . TRP A 98  ? 0.36855 0.26940 0.19153 -0.07636 0.04110  0.04450  98  TRP A N     
770  C CA    . TRP A 98  ? 0.31403 0.23274 0.20036 -0.07440 0.01754  0.04424  98  TRP A CA    
771  C C     . TRP A 98  ? 0.32812 0.25402 0.22754 -0.04723 0.00238  0.07006  98  TRP A C     
772  O O     . TRP A 98  ? 0.34745 0.26104 0.22375 -0.03783 -0.02303 0.06836  98  TRP A O     
773  C CB    . TRP A 98  ? 0.29239 0.22754 0.21147 -0.06899 0.02123  0.04515  98  TRP A CB    
774  C CG    . TRP A 98  ? 0.27686 0.21022 0.21773 -0.05242 0.00707  0.04109  98  TRP A CG    
775  C CD1   . TRP A 98  ? 0.29611 0.21903 0.22507 -0.03090 0.00160  0.05614  98  TRP A CD1   
776  C CD2   . TRP A 98  ? 0.29101 0.22108 0.21984 -0.06594 0.01304  0.04371  98  TRP A CD2   
777  N NE1   . TRP A 98  ? 0.29760 0.19403 0.22869 -0.01639 -0.01052 0.04555  98  TRP A NE1   
778  C CE2   . TRP A 98  ? 0.30872 0.21611 0.24198 -0.04729 0.00799  0.03386  98  TRP A CE2   
779  C CE3   . TRP A 98  ? 0.30596 0.25593 0.22911 -0.06596 -0.00843 0.02942  98  TRP A CE3   
780  C CZ2   . TRP A 98  ? 0.31707 0.24940 0.25218 -0.06875 -0.00349 0.02342  98  TRP A CZ2   
781  C CZ3   . TRP A 98  ? 0.31900 0.27628 0.24244 -0.05151 -0.00347 0.03829  98  TRP A CZ3   
782  C CH2   . TRP A 98  ? 0.31635 0.26997 0.24706 -0.06988 -0.00065 0.04323  98  TRP A CH2   
783  N N     . ASP A 99  ? 0.33387 0.24412 0.23249 -0.03819 0.01714  0.09149  99  ASP A N     
784  C CA    . ASP A 99  ? 0.34076 0.25171 0.26379 -0.04096 0.02082  0.09793  99  ASP A CA    
785  C C     . ASP A 99  ? 0.30394 0.25598 0.26869 -0.05019 0.02902  0.07066  99  ASP A C     
786  O O     . ASP A 99  ? 0.33095 0.27228 0.28387 -0.04368 0.05905  0.06351  99  ASP A O     
787  C CB    . ASP A 99  ? 0.37087 0.26228 0.29559 -0.05839 0.00984  0.12700  99  ASP A CB    
788  C CG    . ASP A 99  ? 0.39742 0.31588 0.33985 -0.06344 0.00839  0.13863  99  ASP A CG    
789  O OD1   . ASP A 99  ? 0.41797 0.33423 0.35347 -0.03014 -0.01181 0.12814  99  ASP A OD1   
790  O OD2   . ASP A 99  ? 0.43437 0.36284 0.37014 -0.01513 0.01598  0.15975  99  ASP A OD2   
791  N N     . GLY A 100 ? 0.30181 0.21519 0.25457 -0.03411 0.00868  0.06545  100 GLY A N     
792  C CA    . GLY A 100 ? 0.27228 0.20813 0.24511 -0.03626 -0.01056 0.06030  100 GLY A CA    
793  C C     . GLY A 100 ? 0.25036 0.18231 0.24353 -0.05347 -0.01824 0.05961  100 GLY A C     
794  O O     . GLY A 100 ? 0.27733 0.19942 0.24498 -0.04825 -0.01968 0.06226  100 GLY A O     
795  N N     . ASN A 101 ? 0.25970 0.17857 0.23629 -0.02067 -0.02175 0.07107  101 ASN A N     
796  C CA    . ASN A 101 ? 0.24674 0.14315 0.23977 -0.00909 -0.00443 0.05889  101 ASN A CA    
797  C C     . ASN A 101 ? 0.24439 0.16852 0.23517 -0.00429 0.01189  0.04223  101 ASN A C     
798  O O     . ASN A 101 ? 0.24589 0.19568 0.24558 -0.01999 -0.00530 0.04684  101 ASN A O     
799  C CB    . ASN A 101 ? 0.23673 0.16401 0.28448 -0.01338 -0.00167 0.05524  101 ASN A CB    
800  C CG    . ASN A 101 ? 0.25244 0.17183 0.31254 -0.02694 -0.01350 0.05317  101 ASN A CG    
801  O OD1   . ASN A 101 ? 0.26989 0.18675 0.33570 0.00810  0.00037  0.06363  101 ASN A OD1   
802  N ND2   . ASN A 101 ? 0.28251 0.18527 0.31826 -0.02471 -0.01120 0.03170  101 ASN A ND2   
803  N N     . LEU A 102 ? 0.22332 0.15671 0.21668 -0.00877 0.00820  0.03499  102 LEU A N     
804  C CA    . LEU A 102 ? 0.22403 0.14191 0.20230 -0.00427 0.00463  0.05427  102 LEU A CA    
805  C C     . LEU A 102 ? 0.19228 0.15570 0.19169 -0.01615 0.02042  0.04036  102 LEU A C     
806  O O     . LEU A 102 ? 0.19961 0.21206 0.19494 -0.01702 0.01025  0.02692  102 LEU A O     
807  C CB    . LEU A 102 ? 0.24813 0.18707 0.21774 -0.01092 0.01497  0.02498  102 LEU A CB    
808  C CG    . LEU A 102 ? 0.26287 0.16237 0.21202 -0.01471 0.01580  0.02816  102 LEU A CG    
809  C CD1   . LEU A 102 ? 0.29945 0.20851 0.23373 0.00981  0.02991  -0.01052 102 LEU A CD1   
810  C CD2   . LEU A 102 ? 0.28433 0.22286 0.21969 0.01031  0.02174  0.03643  102 LEU A CD2   
811  N N     . THR A 103 ? 0.20374 0.15147 0.19845 -0.01843 -0.01398 0.04353  103 THR A N     
812  C CA    . THR A 103 ? 0.20489 0.16382 0.21804 -0.00855 -0.01252 0.03178  103 THR A CA    
813  C C     . THR A 103 ? 0.20320 0.16628 0.19535 -0.00523 0.00455  0.03535  103 THR A C     
814  O O     . THR A 103 ? 0.19002 0.18868 0.21005 0.00831  0.03005  0.02184  103 THR A O     
815  C CB    . THR A 103 ? 0.21364 0.17195 0.23944 -0.03022 -0.03685 0.02509  103 THR A CB    
816  O OG1   . THR A 103 ? 0.25116 0.18639 0.25580 -0.05113 -0.03976 0.01007  103 THR A OG1   
817  C CG2   . THR A 103 ? 0.23638 0.21829 0.24728 -0.06747 -0.03722 0.03641  103 THR A CG2   
818  N N     . LEU A 104 ? 0.22110 0.13755 0.17124 -0.01078 0.01656  0.02247  104 LEU A N     
819  C CA    . LEU A 104 ? 0.20462 0.13932 0.15901 0.00260  -0.00811 0.02660  104 LEU A CA    
820  C C     . LEU A 104 ? 0.22324 0.14384 0.16543 -0.00654 0.00357  0.00043  104 LEU A C     
821  O O     . LEU A 104 ? 0.26831 0.15973 0.18614 0.03941  0.03282  -0.01212 104 LEU A O     
822  C CB    . LEU A 104 ? 0.19936 0.15436 0.17534 0.01037  -0.00144 0.01540  104 LEU A CB    
823  C CG    . LEU A 104 ? 0.21477 0.16271 0.17596 -0.03352 0.00396  0.00958  104 LEU A CG    
824  C CD1   . LEU A 104 ? 0.24857 0.19929 0.19501 -0.00056 -0.00522 0.00515  104 LEU A CD1   
825  C CD2   . LEU A 104 ? 0.24699 0.17739 0.15908 -0.00875 0.01847  0.01081  104 LEU A CD2   
826  N N     . MET A 105 ? 0.18300 0.13713 0.17254 -0.01165 0.00005  0.02602  105 MET A N     
827  C CA    . MET A 105 ? 0.15169 0.16465 0.16106 -0.00666 0.00513  0.02393  105 MET A CA    
828  C C     . MET A 105 ? 0.15523 0.15010 0.13461 -0.00383 -0.00427 -0.00846 105 MET A C     
829  O O     . MET A 105 ? 0.20202 0.15235 0.13101 -0.00383 0.01150  0.00024  105 MET A O     
830  C CB    . MET A 105 ? 0.16279 0.17478 0.17842 -0.00857 0.01221  0.01773  105 MET A CB    
831  C CG    . MET A 105 ? 0.18035 0.17617 0.18927 -0.01929 0.01138  0.00752  105 MET A CG    
832  S SD    . MET A 105 ? 0.18597 0.18303 0.17602 0.00609  0.01799  0.00261  105 MET A SD    
833  C CE    . MET A 105 ? 0.21366 0.22583 0.19993 0.03269  -0.02050 -0.00163 105 MET A CE    
834  N N     . LEU A 106 ? 0.15670 0.15731 0.13996 -0.00025 0.01903  0.01205  106 LEU A N     
835  C CA    . LEU A 106 ? 0.16835 0.16412 0.14643 -0.02672 0.00427  0.03541  106 LEU A CA    
836  C C     . LEU A 106 ? 0.18070 0.16444 0.14785 -0.00656 0.01510  0.01477  106 LEU A C     
837  O O     . LEU A 106 ? 0.27732 0.18365 0.14614 -0.02647 0.01383  -0.02484 106 LEU A O     
838  C CB    . LEU A 106 ? 0.18482 0.24655 0.19341 -0.00526 -0.00918 0.01919  106 LEU A CB    
839  C CG    . LEU A 106 ? 0.20308 0.30915 0.23723 0.01490  -0.01077 0.05287  106 LEU A CG    
840  C CD1   . LEU A 106 ? 0.18676 0.36664 0.26078 0.00710  -0.00428 0.08658  106 LEU A CD1   
841  C CD2   . LEU A 106 ? 0.25921 0.34979 0.24868 0.00114  -0.04255 0.01318  106 LEU A CD2   
842  N N     . PHE A 107 ? 0.17335 0.15485 0.14380 0.00582  0.01587  0.01815  107 PHE A N     
843  C CA    . PHE A 107 ? 0.15932 0.17073 0.14471 0.00400  0.02027  0.01683  107 PHE A CA    
844  C C     . PHE A 107 ? 0.17496 0.15999 0.13497 -0.00547 0.00398  -0.01122 107 PHE A C     
845  O O     . PHE A 107 ? 0.18745 0.17368 0.13646 -0.02703 0.00825  0.00392  107 PHE A O     
846  C CB    . PHE A 107 ? 0.16728 0.16489 0.14407 0.00768  0.01882  0.00320  107 PHE A CB    
847  C CG    . PHE A 107 ? 0.19175 0.17557 0.14405 -0.02009 0.01803  -0.00150 107 PHE A CG    
848  C CD1   . PHE A 107 ? 0.21084 0.23518 0.13457 0.02363  -0.00292 -0.00150 107 PHE A CD1   
849  C CD2   . PHE A 107 ? 0.23998 0.18254 0.17034 0.00808  0.01290  0.00562  107 PHE A CD2   
850  C CE1   . PHE A 107 ? 0.22476 0.24448 0.17236 0.00865  -0.00192 0.01167  107 PHE A CE1   
851  C CE2   . PHE A 107 ? 0.24281 0.19499 0.17326 0.01296  0.01664  0.01986  107 PHE A CE2   
852  C CZ    . PHE A 107 ? 0.19984 0.23892 0.17483 -0.00182 0.02513  0.02138  107 PHE A CZ    
853  N N     . ASN A 108 ? 0.18065 0.20220 0.14587 0.02359  0.04270  -0.01739 108 ASN A N     
854  C CA    . ASN A 108 ? 0.20424 0.18113 0.15662 0.01153  0.05294  0.00534  108 ASN A CA    
855  C C     . ASN A 108 ? 0.18838 0.19304 0.15310 -0.00625 0.03131  0.00113  108 ASN A C     
856  O O     . ASN A 108 ? 0.23114 0.24770 0.14933 0.00663  0.01168  -0.00277 108 ASN A O     
857  C CB    . ASN A 108 ? 0.21866 0.19687 0.18128 0.02340  0.05310  0.00257  108 ASN A CB    
858  C CG    . ASN A 108 ? 0.21884 0.20664 0.19957 0.02107  0.04100  0.01159  108 ASN A CG    
859  O OD1   . ASN A 108 ? 0.19762 0.21357 0.22965 0.01111  0.02938  0.00198  108 ASN A OD1   
860  N ND2   . ASN A 108 ? 0.24103 0.22506 0.18069 0.01632  0.04949  -0.00363 108 ASN A ND2   
861  N N     . ALA A 109 ? 0.21003 0.17911 0.15036 -0.00003 0.04204  0.00777  109 ALA A N     
862  C CA    . ALA A 109 ? 0.25935 0.20419 0.18584 0.03026  0.04999  0.02820  109 ALA A CA    
863  C C     . ALA A 109 ? 0.24993 0.21765 0.20599 0.02432  0.04773  0.05218  109 ALA A C     
864  O O     . ALA A 109 ? 0.28409 0.29088 0.23823 0.04424  0.05559  0.05953  109 ALA A O     
865  C CB    . ALA A 109 ? 0.28125 0.18354 0.21192 0.00959  0.02971  0.00930  109 ALA A CB    
866  N N     . SER A 110 ? 0.23405 0.24589 0.21899 0.02240  0.06522  0.03049  110 SER A N     
867  C CA    . SER A 110 ? 0.24188 0.26689 0.22903 -0.01969 0.08937  0.00636  110 SER A CA    
868  C C     . SER A 110 ? 0.30010 0.25499 0.21936 0.02016  0.06697  0.00276  110 SER A C     
869  O O     . SER A 110 ? 0.31236 0.28013 0.20598 0.03408  0.06849  -0.00324 110 SER A O     
870  C CB    . SER A 110 ? 0.25814 0.28210 0.26741 -0.06410 0.08671  0.02396  110 SER A CB    
871  O OG    . SER A 110 ? 0.32622 0.30938 0.29420 -0.03394 0.08336  0.05061  110 SER A OG    
872  N N     . GLU A 111 ? 0.32825 0.26761 0.22889 0.03833  0.09481  0.03686  111 GLU A N     
873  C CA    . GLU A 111 ? 0.38419 0.30984 0.22815 0.06813  0.10704  0.06469  111 GLU A CA    
874  C C     . GLU A 111 ? 0.34324 0.32914 0.23165 0.01336  0.11907  0.06821  111 GLU A C     
875  O O     . GLU A 111 ? 0.36558 0.31950 0.21450 0.04672  0.11008  0.03528  111 GLU A O     
876  C CB    . GLU A 111 ? 0.44251 0.37786 0.24205 0.11534  0.11857  0.07354  111 GLU A CB    
877  C CG    . GLU A 111 ? 0.50139 0.45293 0.28573 0.16856  0.10940  0.04645  111 GLU A CG    
878  C CD    . GLU A 111 ? 0.54164 0.57032 0.30603 0.21056  0.11886  0.04400  111 GLU A CD    
879  O OE1   . GLU A 111 ? 0.58632 0.65319 0.34404 0.25378  0.09110  0.01078  111 GLU A OE1   
880  O OE2   . GLU A 111 ? 0.58183 0.59551 0.30717 0.21063  0.13298  0.04839  111 GLU A OE2   
881  N N     . GLU A 112 ? 0.31952 0.36089 0.25113 0.02338  0.11460  0.05667  112 GLU A N     
882  C CA    . GLU A 112 ? 0.32729 0.34164 0.28911 0.00238  0.12603  0.05262  112 GLU A CA    
883  C C     . GLU A 112 ? 0.28491 0.33247 0.25506 0.00103  0.12562  0.04769  112 GLU A C     
884  O O     . GLU A 112 ? 0.26841 0.31986 0.23677 0.01955  0.10730  0.04858  112 GLU A O     
885  C CB    . GLU A 112 ? 0.38864 0.39216 0.36109 0.00552  0.15627  0.09055  112 GLU A CB    
886  C CG    . GLU A 112 ? 0.48170 0.48578 0.42137 0.03195  0.18015  0.11179  112 GLU A CG    
887  C CD    . GLU A 112 ? 0.59489 0.63013 0.48972 0.08672  0.17407  0.07341  112 GLU A CD    
888  O OE1   . GLU A 112 ? 0.63287 0.67821 0.51702 0.12846  0.16775  0.02941  112 GLU A OE1   
889  O OE2   . GLU A 112 ? 0.67634 0.69959 0.54354 0.13675  0.16198  0.04545  112 GLU A OE2   
890  N N     . PRO A 113 ? 0.27043 0.31892 0.23400 0.00505  0.13577  0.04531  113 PRO A N     
891  C CA    . PRO A 113 ? 0.25358 0.30709 0.24403 -0.00348 0.09190  0.00447  113 PRO A CA    
892  C C     . PRO A 113 ? 0.23086 0.29918 0.25608 -0.02456 0.07104  0.01154  113 PRO A C     
893  O O     . PRO A 113 ? 0.23418 0.29107 0.28085 -0.00533 0.07041  0.01766  113 PRO A O     
894  C CB    . PRO A 113 ? 0.25416 0.33694 0.24635 -0.00671 0.10120  -0.01486 113 PRO A CB    
895  C CG    . PRO A 113 ? 0.32100 0.36478 0.24639 0.05169  0.11458  0.00900  113 PRO A CG    
896  C CD    . PRO A 113 ? 0.29654 0.36482 0.22751 0.06079  0.13716  0.03517  113 PRO A CD    
897  N N     . VAL A 114 ? 0.22783 0.26451 0.25164 0.00012  0.05549  0.02046  114 VAL A N     
898  C CA    . VAL A 114 ? 0.22018 0.22702 0.24216 -0.00938 0.04719  0.00929  114 VAL A CA    
899  C C     . VAL A 114 ? 0.22048 0.23266 0.24322 -0.01703 0.05280  0.00201  114 VAL A C     
900  O O     . VAL A 114 ? 0.22384 0.23666 0.23875 -0.02776 0.05526  0.00426  114 VAL A O     
901  C CB    . VAL A 114 ? 0.25114 0.22100 0.24908 -0.00609 0.02718  -0.00285 114 VAL A CB    
902  C CG1   . VAL A 114 ? 0.26002 0.25390 0.24811 0.01418  0.02992  -0.01774 114 VAL A CG1   
903  C CG2   . VAL A 114 ? 0.28597 0.22752 0.27844 -0.00860 0.02410  0.01534  114 VAL A CG2   
904  N N     . GLU A 115 ? 0.25378 0.22362 0.26417 0.00269  0.03684  0.02027  115 GLU A N     
905  C CA    . GLU A 115 ? 0.27383 0.20723 0.27486 0.00908  0.02500  0.01648  115 GLU A CA    
906  C C     . GLU A 115 ? 0.28448 0.19534 0.28420 0.01322  0.00584  -0.00521 115 GLU A C     
907  O O     . GLU A 115 ? 0.32833 0.23255 0.28818 -0.02846 -0.00282 -0.01506 115 GLU A O     
908  C CB    . GLU A 115 ? 0.36622 0.30151 0.29768 0.09281  0.06366  0.01911  115 GLU A CB    
909  C CG    . GLU A 115 ? 0.41880 0.42048 0.35249 0.12044  0.08591  0.04452  115 GLU A CG    
910  C CD    . GLU A 115 ? 0.46539 0.49100 0.39648 0.12288  0.09247  0.06167  115 GLU A CD    
911  O OE1   . GLU A 115 ? 0.45672 0.49845 0.42595 0.08346  0.10847  0.08041  115 GLU A OE1   
912  O OE2   . GLU A 115 ? 0.51100 0.48789 0.41288 0.14343  0.08445  0.07073  115 GLU A OE2   
913  N N     . LEU A 116 ? 0.23552 0.20911 0.28352 0.00869  0.03279  0.01245  116 LEU A N     
914  C CA    . LEU A 116 ? 0.25916 0.21094 0.29882 0.00256  0.02612  0.01238  116 LEU A CA    
915  C C     . LEU A 116 ? 0.24249 0.18368 0.30821 -0.00812 0.01419  -0.00288 116 LEU A C     
916  O O     . LEU A 116 ? 0.24814 0.21292 0.31475 0.01817  0.00274  -0.02482 116 LEU A O     
917  C CB    . LEU A 116 ? 0.27736 0.20180 0.30656 0.03472  0.04616  0.02252  116 LEU A CB    
918  C CG    . LEU A 116 ? 0.31511 0.25893 0.31855 0.10278  0.06865  0.04212  116 LEU A CG    
919  C CD1   . LEU A 116 ? 0.37124 0.30101 0.33051 0.11217  0.06225  0.03230  116 LEU A CD1   
920  C CD2   . LEU A 116 ? 0.34900 0.32939 0.34193 0.13102  0.10587  0.05494  116 LEU A CD2   
921  N N     . ASN A 117 ? 0.24926 0.18831 0.31493 0.00486  0.01541  -0.01895 117 ASN A N     
922  C CA    . ASN A 117 ? 0.20479 0.19004 0.32802 0.01581  -0.00607 -0.01288 117 ASN A CA    
923  C C     . ASN A 117 ? 0.18081 0.17675 0.32007 0.01788  -0.00045 -0.01499 117 ASN A C     
924  O O     . ASN A 117 ? 0.19504 0.17325 0.32015 0.03511  0.00572  0.00287  117 ASN A O     
925  C CB    . ASN A 117 ? 0.19742 0.31872 0.35324 0.00810  0.02817  -0.01516 117 ASN A CB    
926  C CG    . ASN A 117 ? 0.26719 0.40861 0.38674 0.00204  0.01828  -0.02778 117 ASN A CG    
927  O OD1   . ASN A 117 ? 0.31409 0.44670 0.39002 -0.00617 0.04168  -0.04360 117 ASN A OD1   
928  N ND2   . ASN A 117 ? 0.31211 0.46632 0.41225 0.02202  0.01077  -0.03428 117 ASN A ND2   
929  N N     . TYR A 118 ? 0.20508 0.18554 0.33320 0.01193  -0.00406 -0.03081 118 TYR A N     
930  C CA    . TYR A 118 ? 0.21477 0.17099 0.34370 0.00833  0.01766  -0.01711 118 TYR A CA    
931  C C     . TYR A 118 ? 0.20725 0.20404 0.32855 0.03752  0.00652  0.00626  118 TYR A C     
932  O O     . TYR A 118 ? 0.19778 0.26091 0.32611 0.02653  0.00410  0.01281  118 TYR A O     
933  C CB    . TYR A 118 ? 0.23035 0.16949 0.38064 0.01886  0.03242  -0.01371 118 TYR A CB    
934  C CG    . TYR A 118 ? 0.24506 0.15192 0.39611 0.04116  0.03274  -0.01579 118 TYR A CG    
935  C CD1   . TYR A 118 ? 0.25687 0.17005 0.38544 -0.00175 0.05068  0.00136  118 TYR A CD1   
936  C CD2   . TYR A 118 ? 0.27595 0.18033 0.41521 0.04532  0.03178  0.01706  118 TYR A CD2   
937  C CE1   . TYR A 118 ? 0.28253 0.15891 0.39672 0.02436  0.05455  0.02695  118 TYR A CE1   
938  C CE2   . TYR A 118 ? 0.30252 0.18629 0.41231 0.02436  0.02989  0.04988  118 TYR A CE2   
939  C CZ    . TYR A 118 ? 0.31954 0.20135 0.40629 0.02894  0.03637  0.03342  118 TYR A CZ    
940  O OH    . TYR A 118 ? 0.39432 0.32458 0.41956 0.06606  0.02111  0.02647  118 TYR A OH    
941  N N     . GLY A 119 ? 0.22047 0.17905 0.30857 0.03071  -0.00959 0.00677  119 GLY A N     
942  C CA    . GLY A 119 ? 0.22874 0.18615 0.31335 0.03446  -0.01388 0.00527  119 GLY A CA    
943  C C     . GLY A 119 ? 0.22801 0.18283 0.30634 0.03601  -0.01320 0.01938  119 GLY A C     
944  O O     . GLY A 119 ? 0.23486 0.24122 0.31499 0.03058  -0.02329 0.02305  119 GLY A O     
945  N N     . GLU A 120 ? 0.19612 0.17047 0.29110 0.00576  -0.00465 0.01868  120 GLU A N     
946  C CA    . GLU A 120 ? 0.22335 0.18787 0.28193 -0.00048 -0.00985 0.00654  120 GLU A CA    
947  C C     . GLU A 120 ? 0.19603 0.15910 0.27116 -0.01174 -0.01889 0.00733  120 GLU A C     
948  O O     . GLU A 120 ? 0.18448 0.17033 0.28644 -0.01715 -0.01823 0.04003  120 GLU A O     
949  C CB    . GLU A 120 ? 0.26898 0.17519 0.28361 -0.02979 0.00215  0.01651  120 GLU A CB    
950  C CG    . GLU A 120 ? 0.34895 0.21380 0.28786 -0.05380 -0.00467 0.00826  120 GLU A CG    
951  C CD    . GLU A 120 ? 0.42710 0.20129 0.30079 -0.07519 -0.01062 0.00593  120 GLU A CD    
952  O OE1   . GLU A 120 ? 0.40289 0.23568 0.29711 -0.06724 -0.01758 -0.00829 120 GLU A OE1   
953  O OE2   . GLU A 120 ? 0.54078 0.25610 0.32482 -0.06544 -0.01038 0.01010  120 GLU A OE2   
954  N N     . ARG A 121 ? 0.20359 0.16621 0.28316 0.03146  -0.00138 0.01094  121 ARG A N     
955  C CA    . ARG A 121 ? 0.20387 0.14573 0.29028 0.00608  -0.00519 -0.00061 121 ARG A CA    
956  C C     . ARG A 121 ? 0.20916 0.14625 0.29654 -0.00334 0.01260  0.03083  121 ARG A C     
957  O O     . ARG A 121 ? 0.22880 0.19888 0.34370 0.03319  0.03765  0.08214  121 ARG A O     
958  C CB    . ARG A 121 ? 0.22608 0.18755 0.31429 0.00354  -0.02537 0.00208  121 ARG A CB    
959  C CG    . ARG A 121 ? 0.21509 0.22207 0.33791 -0.00482 -0.02832 -0.01311 121 ARG A CG    
960  C CD    . ARG A 121 ? 0.25676 0.31375 0.37225 -0.02832 -0.02275 -0.00840 121 ARG A CD    
961  N NE    . ARG A 121 ? 0.29077 0.35202 0.39834 -0.05613 -0.00858 -0.02647 121 ARG A NE    
962  C CZ    . ARG A 121 ? 0.31244 0.42778 0.42506 -0.04253 0.02720  -0.02008 121 ARG A CZ    
963  N NH1   . ARG A 121 ? 0.30741 0.46215 0.43486 -0.05684 0.06284  0.00611  121 ARG A NH1   
964  N NH2   . ARG A 121 ? 0.32975 0.46039 0.43776 -0.05136 0.04066  0.00331  121 ARG A NH2   
965  N N     . PHE A 122 ? 0.20413 0.16142 0.24745 0.01008  -0.00313 0.01596  122 PHE A N     
966  C CA    . PHE A 122 ? 0.21179 0.17608 0.21491 0.03067  0.01170  0.00501  122 PHE A CA    
967  C C     . PHE A 122 ? 0.20830 0.16279 0.19947 0.00283  0.00976  0.01394  122 PHE A C     
968  O O     . PHE A 122 ? 0.23760 0.13913 0.19904 0.01669  0.00171  0.00989  122 PHE A O     
969  C CB    . PHE A 122 ? 0.22079 0.19031 0.21806 -0.00157 0.02864  -0.00162 122 PHE A CB    
970  C CG    . PHE A 122 ? 0.21150 0.16472 0.22706 0.00735  0.01321  -0.01197 122 PHE A CG    
971  C CD1   . PHE A 122 ? 0.18643 0.17261 0.23867 0.00246  0.03253  0.01787  122 PHE A CD1   
972  C CD2   . PHE A 122 ? 0.23725 0.22451 0.23717 0.00597  -0.01171 -0.02016 122 PHE A CD2   
973  C CE1   . PHE A 122 ? 0.17434 0.20634 0.23979 0.01707  0.00467  -0.01170 122 PHE A CE1   
974  C CE2   . PHE A 122 ? 0.23428 0.21380 0.24530 -0.00455 -0.02398 0.01387  122 PHE A CE2   
975  C CZ    . PHE A 122 ? 0.19914 0.20981 0.24245 0.02498  -0.01518 -0.00271 122 PHE A CZ    
976  N N     . VAL A 123 ? 0.20294 0.16506 0.18993 0.01645  0.00382  0.00822  123 VAL A N     
977  C CA    . VAL A 123 ? 0.19566 0.18498 0.16406 0.00755  0.00073  -0.00446 123 VAL A CA    
978  C C     . VAL A 123 ? 0.20188 0.14921 0.16506 0.02292  -0.01134 0.01626  123 VAL A C     
979  O O     . VAL A 123 ? 0.24842 0.17082 0.17708 0.03810  -0.02028 0.04777  123 VAL A O     
980  C CB    . VAL A 123 ? 0.21633 0.17514 0.16270 -0.00270 0.00384  0.02021  123 VAL A CB    
981  C CG1   . VAL A 123 ? 0.24159 0.18794 0.17350 0.02624  0.02809  0.01285  123 VAL A CG1   
982  C CG2   . VAL A 123 ? 0.23671 0.18236 0.15460 0.01850  -0.01248 0.03052  123 VAL A CG2   
983  N N     . GLN A 124 ? 0.21034 0.16358 0.14135 0.01776  -0.01717 0.02221  124 GLN A N     
984  C CA    . GLN A 124 ? 0.21795 0.17887 0.14395 0.02594  -0.00698 0.01665  124 GLN A CA    
985  C C     . GLN A 124 ? 0.19521 0.16931 0.14655 0.02200  -0.01410 0.04031  124 GLN A C     
986  O O     . GLN A 124 ? 0.19747 0.18096 0.14680 0.03209  -0.01760 0.02879  124 GLN A O     
987  C CB    . GLN A 124 ? 0.24384 0.19979 0.15872 -0.00554 -0.01570 -0.00548 124 GLN A CB    
988  C CG    . GLN A 124 ? 0.22379 0.23416 0.19140 -0.00124 -0.05769 0.02752  124 GLN A CG    
989  C CD    . GLN A 124 ? 0.27799 0.25569 0.21263 -0.02680 -0.05714 0.03901  124 GLN A CD    
990  O OE1   . GLN A 124 ? 0.38893 0.29106 0.21978 -0.01854 -0.06599 0.01632  124 GLN A OE1   
991  N NE2   . GLN A 124 ? 0.26729 0.23937 0.24887 -0.02616 -0.04959 0.00925  124 GLN A NE2   
992  N N     . ILE A 125 ? 0.19401 0.17979 0.15506 0.00325  -0.01024 0.04639  125 ILE A N     
993  C CA    . ILE A 125 ? 0.20488 0.20550 0.15799 -0.00573 -0.00774 0.03734  125 ILE A CA    
994  C C     . ILE A 125 ? 0.20769 0.20265 0.16952 0.01331  -0.03495 0.02685  125 ILE A C     
995  O O     . ILE A 125 ? 0.20971 0.21463 0.17731 0.00772  -0.03462 0.03017  125 ILE A O     
996  C CB    . ILE A 125 ? 0.19466 0.18716 0.16557 0.00216  -0.00346 0.03481  125 ILE A CB    
997  C CG1   . ILE A 125 ? 0.20586 0.22029 0.16935 0.00112  0.00172  0.03344  125 ILE A CG1   
998  C CG2   . ILE A 125 ? 0.22145 0.20136 0.19373 0.01787  -0.02263 0.06125  125 ILE A CG2   
999  C CD1   . ILE A 125 ? 0.21551 0.20933 0.18994 -0.01884 0.00389  0.01431  125 ILE A CD1   
1000 N N     . ALA A 126 ? 0.21337 0.20847 0.15349 0.01933  -0.03340 0.02867  126 ALA A N     
1001 C CA    . ALA A 126 ? 0.23806 0.22084 0.14607 0.02243  -0.03162 0.01615  126 ALA A CA    
1002 C C     . ALA A 126 ? 0.20853 0.25683 0.13037 0.02456  -0.03095 0.02139  126 ALA A C     
1003 O O     . ALA A 126 ? 0.22105 0.26545 0.13351 -0.01042 -0.04307 0.03898  126 ALA A O     
1004 C CB    . ALA A 126 ? 0.26746 0.21302 0.15742 0.01742  -0.04392 0.02032  126 ALA A CB    
1005 N N     . PHE A 127 ? 0.22794 0.23270 0.13889 0.00744  -0.00746 0.04334  127 PHE A N     
1006 C CA    . PHE A 127 ? 0.25370 0.22390 0.15791 0.01326  -0.02759 0.04301  127 PHE A CA    
1007 C C     . PHE A 127 ? 0.26814 0.24321 0.15223 0.02633  -0.02515 0.00823  127 PHE A C     
1008 O O     . PHE A 127 ? 0.28452 0.29599 0.15398 0.03449  -0.03901 0.01478  127 PHE A O     
1009 C CB    . PHE A 127 ? 0.26256 0.24667 0.16813 0.01644  -0.04164 0.04449  127 PHE A CB    
1010 C CG    . PHE A 127 ? 0.25011 0.21620 0.17893 -0.01395 -0.02425 0.03839  127 PHE A CG    
1011 C CD1   . PHE A 127 ? 0.29312 0.21323 0.18646 -0.00947 -0.02540 0.04374  127 PHE A CD1   
1012 C CD2   . PHE A 127 ? 0.25658 0.24253 0.17494 0.02980  -0.02543 0.05290  127 PHE A CD2   
1013 C CE1   . PHE A 127 ? 0.31270 0.22740 0.19611 0.00335  -0.01224 0.04157  127 PHE A CE1   
1014 C CE2   . PHE A 127 ? 0.30801 0.22769 0.17475 0.04070  -0.02257 0.04371  127 PHE A CE2   
1015 C CZ    . PHE A 127 ? 0.31152 0.22444 0.19059 0.01350  -0.01797 0.04713  127 PHE A CZ    
1016 N N     . ILE A 128 ? 0.25206 0.26000 0.14730 0.01223  0.01503  0.03763  128 ILE A N     
1017 C CA    . ILE A 128 ? 0.26763 0.27952 0.14098 0.03295  0.00440  0.04540  128 ILE A CA    
1018 C C     . ILE A 128 ? 0.26946 0.27295 0.13691 0.00756  0.00425  0.02534  128 ILE A C     
1019 O O     . ILE A 128 ? 0.28790 0.30815 0.14424 -0.02955 0.00825  0.03810  128 ILE A O     
1020 C CB    . ILE A 128 ? 0.33259 0.32963 0.16658 0.06574  0.05199  0.07834  128 ILE A CB    
1021 C CG1   . ILE A 128 ? 0.37075 0.37988 0.20294 0.03809  0.05063  0.06731  128 ILE A CG1   
1022 C CG2   . ILE A 128 ? 0.38303 0.35412 0.19092 0.08381  0.07080  0.04605  128 ILE A CG2   
1023 C CD1   . ILE A 128 ? 0.38834 0.39905 0.21344 0.06607  0.04063  0.05883  128 ILE A CD1   
1024 N N     . ARG A 129 ? 0.27920 0.31049 0.13205 0.00755  -0.00694 0.02963  129 ARG A N     
1025 C CA    . ARG A 129 ? 0.28684 0.33557 0.14929 0.01324  0.00538  0.03798  129 ARG A CA    
1026 C C     . ARG A 129 ? 0.28138 0.29268 0.14756 -0.00691 0.02491  0.04646  129 ARG A C     
1027 O O     . ARG A 129 ? 0.32167 0.30268 0.14573 0.01725  0.01597  0.02802  129 ARG A O     
1028 C CB    . ARG A 129 ? 0.31916 0.39654 0.16513 0.02440  0.01509  0.03909  129 ARG A CB    
1029 C CG    . ARG A 129 ? 0.36599 0.42022 0.20029 0.05184  0.00368  0.06726  129 ARG A CG    
1030 C CD    . ARG A 129 ? 0.35976 0.44009 0.23345 0.03159  -0.00977 0.09931  129 ARG A CD    
1031 N NE    . ARG A 129 ? 0.36023 0.45557 0.24040 0.02697  -0.04051 0.09543  129 ARG A NE    
1032 C CZ    . ARG A 129 ? 0.37673 0.46556 0.23046 0.02925  -0.04177 0.11452  129 ARG A CZ    
1033 N NH1   . ARG A 129 ? 0.39202 0.47727 0.22848 0.02494  -0.02115 0.14127  129 ARG A NH1   
1034 N NH2   . ARG A 129 ? 0.38667 0.46524 0.22096 0.02659  -0.04984 0.12359  129 ARG A NH2   
1035 N N     . LEU A 130 ? 0.27404 0.35156 0.15497 -0.01280 0.01923  0.05619  130 LEU A N     
1036 C CA    . LEU A 130 ? 0.28466 0.36408 0.15551 -0.03237 0.03753  0.03780  130 LEU A CA    
1037 C C     . LEU A 130 ? 0.31361 0.38810 0.16058 -0.04209 0.04230  0.05819  130 LEU A C     
1038 O O     . LEU A 130 ? 0.35982 0.42733 0.17151 0.03218  0.01282  0.07449  130 LEU A O     
1039 C CB    . LEU A 130 ? 0.30836 0.40734 0.16407 -0.02275 0.01732  0.00253  130 LEU A CB    
1040 C CG    . LEU A 130 ? 0.34862 0.46381 0.19054 -0.01225 0.02393  -0.02574 130 LEU A CG    
1041 C CD1   . LEU A 130 ? 0.32094 0.42966 0.18968 -0.00297 0.00925  -0.02068 130 LEU A CD1   
1042 C CD2   . LEU A 130 ? 0.35248 0.49345 0.19680 -0.03072 0.03258  -0.02002 130 LEU A CD2   
1043 N N     . GLU A 131 ? 0.34188 0.40497 0.16399 -0.03484 0.04945  0.04441  131 GLU A N     
1044 C CA    . GLU A 131 ? 0.39744 0.44215 0.18098 -0.01802 0.06215  0.02366  131 GLU A CA    
1045 C C     . GLU A 131 ? 0.43860 0.47049 0.19054 -0.03260 0.05851  0.03844  131 GLU A C     
1046 O O     . GLU A 131 ? 0.50079 0.50372 0.19265 0.01034  0.03736  0.03564  131 GLU A O     
1047 C CB    . GLU A 131 ? 0.41290 0.46368 0.20965 0.01094  0.07551  -0.00012 131 GLU A CB    
1048 C CG    . GLU A 131 ? 0.41821 0.47165 0.25616 0.01798  0.08566  0.01131  131 GLU A CG    
1049 C CD    . GLU A 131 ? 0.44713 0.50854 0.29921 0.03739  0.06951  0.00301  131 GLU A CD    
1050 O OE1   . GLU A 131 ? 0.43774 0.54017 0.31457 0.05879  0.06968  0.01616  131 GLU A OE1   
1051 O OE2   . GLU A 131 ? 0.46465 0.51575 0.31286 0.02992  0.05474  0.00230  131 GLU A OE2   
1052 N N     . GLY A 132 ? 0.43231 0.45926 0.19204 -0.04597 0.05785  0.09550  132 GLY A N     
1053 C CA    . GLY A 132 ? 0.43829 0.45566 0.21321 -0.06098 0.04141  0.10158  132 GLY A CA    
1054 C C     . GLY A 132 ? 0.45710 0.44923 0.22708 -0.04153 0.03366  0.11787  132 GLY A C     
1055 O O     . GLY A 132 ? 0.42717 0.45587 0.21345 -0.06504 0.04047  0.12332  132 GLY A O     
1056 N N     . PRO A 133 ? 0.50651 0.44322 0.24738 -0.00168 0.04627  0.13498  133 PRO A N     
1057 C CA    . PRO A 133 ? 0.50339 0.40596 0.25222 0.00761  0.04743  0.11766  133 PRO A CA    
1058 C C     . PRO A 133 ? 0.47620 0.39591 0.24406 0.00813  0.04474  0.12581  133 PRO A C     
1059 O O     . PRO A 133 ? 0.44139 0.40805 0.24803 -0.01514 0.05109  0.09144  133 PRO A O     
1060 C CB    . PRO A 133 ? 0.54987 0.41389 0.27337 0.01853  0.04560  0.11835  133 PRO A CB    
1061 C CG    . PRO A 133 ? 0.56123 0.44076 0.28318 0.01276  0.05958  0.12951  133 PRO A CG    
1062 C CD    . PRO A 133 ? 0.54047 0.42949 0.26359 0.00279  0.06704  0.14068  133 PRO A CD    
1063 N N     . ALA A 134 ? 0.47363 0.39016 0.24261 0.01052  0.04554  0.11727  134 ALA A N     
1064 C CA    . ALA A 134 ? 0.47120 0.37071 0.23751 -0.01533 0.05482  0.11844  134 ALA A CA    
1065 C C     . ALA A 134 ? 0.48729 0.34946 0.24597 -0.02803 0.03594  0.11570  134 ALA A C     
1066 O O     . ALA A 134 ? 0.51485 0.32685 0.26295 -0.01667 0.04089  0.10689  134 ALA A O     
1067 C CB    . ALA A 134 ? 0.46481 0.38215 0.23500 0.00304  0.05004  0.10759  134 ALA A CB    
1068 N N     . LYS A 135 ? 0.48562 0.37511 0.24085 -0.03437 0.03130  0.09333  135 LYS A N     
1069 C CA    . LYS A 135 ? 0.49083 0.42140 0.26809 -0.03830 0.02886  0.08662  135 LYS A CA    
1070 C C     . LYS A 135 ? 0.49823 0.39994 0.27846 -0.03465 0.02977  0.08143  135 LYS A C     
1071 O O     . LYS A 135 ? 0.51340 0.40423 0.28299 -0.04531 0.00491  0.05479  135 LYS A O     
1072 C CB    . LYS A 135 ? 0.48743 0.43910 0.28100 -0.05955 0.01906  0.10271  135 LYS A CB    
1073 C CG    . LYS A 135 ? 0.49593 0.50443 0.29667 -0.06388 0.02378  0.14080  135 LYS A CG    
1074 C CD    . LYS A 135 ? 0.51042 0.57555 0.32115 -0.07513 0.01004  0.14165  135 LYS A CD    
1075 C CE    . LYS A 135 ? 0.52946 0.62538 0.33523 -0.06641 -0.00679 0.13932  135 LYS A CE    
1076 N NZ    . LYS A 135 ? 0.52777 0.65936 0.35349 -0.06545 -0.01918 0.14541  135 LYS A NZ    
1077 N N     . ASN A 136 ? 0.48596 0.42348 0.28550 -0.03411 0.04458  0.07813  136 ASN A N     
1078 C CA    . ASN A 136 ? 0.46500 0.44206 0.30420 -0.07017 0.07576  0.09592  136 ASN A CA    
1079 C C     . ASN A 136 ? 0.44572 0.42273 0.31599 -0.08421 0.10504  0.11800  136 ASN A C     
1080 O O     . ASN A 136 ? 0.44146 0.43589 0.32916 -0.02516 0.08696  0.08488  136 ASN A O     
1081 C CB    . ASN A 136 ? 0.49287 0.50138 0.32289 -0.06431 0.06774  0.07938  136 ASN A CB    
1082 C CG    . ASN A 136 ? 0.51505 0.53826 0.34396 -0.03789 0.05387  0.06647  136 ASN A CG    
1083 O OD1   . ASN A 136 ? 0.53045 0.54860 0.36328 -0.02406 0.04431  0.05021  136 ASN A OD1   
1084 N ND2   . ASN A 136 ? 0.52681 0.53984 0.34415 -0.04241 0.04829  0.08576  136 ASN A ND2   
1085 N N     . PRO A 137 ? 0.44473 0.46478 0.33931 -0.06322 0.12308  0.11719  137 PRO A N     
1086 C CA    . PRO A 137 ? 0.44633 0.45574 0.35126 -0.04433 0.11969  0.11025  137 PRO A CA    
1087 C C     . PRO A 137 ? 0.44136 0.41527 0.37080 -0.03818 0.11166  0.06103  137 PRO A C     
1088 O O     . PRO A 137 ? 0.47749 0.39501 0.37380 -0.00458 0.08390  0.03639  137 PRO A O     
1089 C CB    . PRO A 137 ? 0.46560 0.51673 0.35135 -0.00402 0.11980  0.11903  137 PRO A CB    
1090 C CG    . PRO A 137 ? 0.45779 0.53247 0.34786 -0.01344 0.12824  0.14278  137 PRO A CG    
1091 C CD    . PRO A 137 ? 0.45764 0.50337 0.34737 -0.00682 0.12953  0.15129  137 PRO A CD    
1092 N N     . TYR A 138 ? 0.43597 0.43282 0.40148 -0.01829 0.10873  0.02724  138 TYR A N     
1093 C CA    . TYR A 138 ? 0.41353 0.39189 0.42305 -0.11029 0.12348  -0.00203 138 TYR A CA    
1094 C C     . TYR A 138 ? 0.40963 0.41218 0.44032 -0.15714 0.14763  0.01184  138 TYR A C     
1095 O O     . TYR A 138 ? 0.41874 0.43787 0.46307 -0.12673 0.13596  -0.01413 138 TYR A O     
1096 C CB    . TYR A 138 ? 0.40480 0.42291 0.44650 -0.13522 0.11385  -0.01605 138 TYR A CB    
1097 C CG    . TYR A 138 ? 0.42582 0.43897 0.48224 -0.15728 0.09566  -0.02472 138 TYR A CG    
1098 C CD1   . TYR A 138 ? 0.43320 0.41940 0.49593 -0.17339 0.09890  -0.01668 138 TYR A CD1   
1099 C CD2   . TYR A 138 ? 0.43634 0.46004 0.49770 -0.15361 0.09876  -0.01074 138 TYR A CD2   
1100 C CE1   . TYR A 138 ? 0.45490 0.50722 0.50166 -0.13264 0.10456  -0.01447 138 TYR A CE1   
1101 C CE2   . TYR A 138 ? 0.46576 0.52331 0.50557 -0.10481 0.09258  -0.02634 138 TYR A CE2   
1102 C CZ    . TYR A 138 ? 0.48409 0.56660 0.51676 -0.07992 0.09991  -0.03376 138 TYR A CZ    
1103 O OH    . TYR A 138 ? 0.52191 0.63004 0.53562 -0.05272 0.09851  -0.05278 138 TYR A OH    
1104 N N     . SER A 145 ? 0.55144 0.65506 0.56674 0.08117  0.00698  -0.00303 145 SER A N     
1105 C CA    . SER A 145 ? 0.48487 0.48613 0.51975 -0.06692 -0.01453 -0.01917 145 SER A CA    
1106 C C     . SER A 145 ? 0.38365 0.37623 0.46840 -0.18344 -0.03410 -0.02274 145 SER A C     
1107 O O     . SER A 145 ? 0.41071 0.30896 0.46417 -0.11052 -0.05398 -0.05684 145 SER A O     
1108 C CB    . SER A 145 ? 0.52597 0.49049 0.53287 -0.02027 -0.01769 -0.01594 145 SER A CB    
1109 O OG    . SER A 145 ? 0.55833 0.48908 0.55038 -0.00004 -0.01827 0.00622  145 SER A OG    
1110 N N     . GLN A 146 ? 0.36322 0.30432 0.43894 -0.09896 -0.01193 0.01833  146 GLN A N     
1111 C CA    . GLN A 146 ? 0.36883 0.24208 0.42883 -0.03981 -0.00907 0.05556  146 GLN A CA    
1112 C C     . GLN A 146 ? 0.31534 0.27215 0.41212 -0.03557 0.00628  0.06441  146 GLN A C     
1113 O O     . GLN A 146 ? 0.28261 0.32550 0.41274 -0.04367 -0.01591 0.06974  146 GLN A O     
1114 C CB    . GLN A 146 ? 0.46929 0.28000 0.44450 0.04208  0.01564  0.11109  146 GLN A CB    
1115 C CG    . GLN A 146 ? 0.56444 0.33391 0.46948 0.10006  0.03477  0.11735  146 GLN A CG    
1116 C CD    . GLN A 146 ? 0.64175 0.40576 0.49325 0.17329  0.03915  0.11227  146 GLN A CD    
1117 O OE1   . GLN A 146 ? 0.67512 0.40569 0.50720 0.20086  0.03982  0.10833  146 GLN A OE1   
1118 N NE2   . GLN A 146 ? 0.67621 0.43981 0.50238 0.16693  0.04803  0.10423  146 GLN A NE2   
1119 N N     . HIS A 147 ? 0.31458 0.21351 0.39252 -0.02750 0.01183  0.04807  147 HIS A N     
1120 C CA    . HIS A 147 ? 0.29766 0.19799 0.37536 -0.02138 0.00675  0.03456  147 HIS A CA    
1121 C C     . HIS A 147 ? 0.24302 0.20294 0.34799 -0.03407 0.00750  0.04810  147 HIS A C     
1122 O O     . HIS A 147 ? 0.24823 0.21606 0.33700 -0.03288 0.00434  0.03127  147 HIS A O     
1123 C CB    . HIS A 147 ? 0.31718 0.19790 0.40422 -0.02971 -0.00143 -0.00515 147 HIS A CB    
1124 C CG    . HIS A 147 ? 0.38690 0.19177 0.42657 -0.01160 0.02133  -0.00722 147 HIS A CG    
1125 N ND1   . HIS A 147 ? 0.43030 0.22207 0.44208 0.02419  0.02929  -0.00878 147 HIS A ND1   
1126 C CD2   . HIS A 147 ? 0.42098 0.20655 0.43253 -0.01275 0.02027  0.00977  147 HIS A CD2   
1127 C CE1   . HIS A 147 ? 0.46409 0.23241 0.44809 0.02734  0.03134  -0.00480 147 HIS A CE1   
1128 N NE2   . HIS A 147 ? 0.45430 0.23281 0.44291 -0.00318 0.03969  0.00803  147 HIS A NE2   
1129 N N     . LEU A 148 ? 0.22744 0.21096 0.32562 -0.04194 0.00337  0.04883  148 LEU A N     
1130 C CA    . LEU A 148 ? 0.22645 0.21552 0.31781 -0.04631 0.01523  0.05599  148 LEU A CA    
1131 C C     . LEU A 148 ? 0.23425 0.18511 0.32043 -0.06415 -0.01901 0.03167  148 LEU A C     
1132 O O     . LEU A 148 ? 0.25280 0.22469 0.34697 -0.04111 -0.05450 -0.00582 148 LEU A O     
1133 C CB    . LEU A 148 ? 0.28119 0.26252 0.32126 -0.03755 0.03563  0.05834  148 LEU A CB    
1134 C CG    . LEU A 148 ? 0.28104 0.30588 0.33861 -0.02109 0.03684  0.06148  148 LEU A CG    
1135 C CD1   . LEU A 148 ? 0.32691 0.35014 0.33647 -0.00127 0.02666  0.06173  148 LEU A CD1   
1136 C CD2   . LEU A 148 ? 0.26125 0.24256 0.35597 -0.01639 0.02059  0.06011  148 LEU A CD2   
1137 N N     . VAL A 149 ? 0.21623 0.18830 0.27863 -0.05161 -0.02589 0.03205  149 VAL A N     
1138 C CA    . VAL A 149 ? 0.23179 0.22434 0.25081 -0.06195 -0.02889 0.01087  149 VAL A CA    
1139 C C     . VAL A 149 ? 0.21671 0.21502 0.25007 -0.04826 -0.03790 0.02807  149 VAL A C     
1140 O O     . VAL A 149 ? 0.24245 0.20583 0.25608 -0.05363 -0.01131 0.03888  149 VAL A O     
1141 C CB    . VAL A 149 ? 0.27034 0.29395 0.24864 -0.07183 -0.01042 0.00091  149 VAL A CB    
1142 C CG1   . VAL A 149 ? 0.29945 0.27689 0.25166 -0.03467 -0.00786 -0.00208 149 VAL A CG1   
1143 C CG2   . VAL A 149 ? 0.28598 0.40287 0.25779 -0.06133 -0.03396 0.01050  149 VAL A CG2   
1144 N N     . LEU A 150 ? 0.18179 0.24499 0.26222 -0.01879 -0.03876 -0.01099 150 LEU A N     
1145 C CA    . LEU A 150 ? 0.21408 0.31078 0.28565 -0.01642 -0.00956 0.01241  150 LEU A CA    
1146 C C     . LEU A 150 ? 0.22946 0.33395 0.31108 -0.03604 -0.02102 0.02255  150 LEU A C     
1147 O O     . LEU A 150 ? 0.23572 0.39836 0.30827 -0.02573 -0.03787 0.04330  150 LEU A O     
1148 C CB    . LEU A 150 ? 0.22326 0.36743 0.29245 -0.03396 -0.00618 -0.03430 150 LEU A CB    
1149 C CG    . LEU A 150 ? 0.22721 0.38786 0.30263 -0.05461 -0.00196 -0.05572 150 LEU A CG    
1150 C CD1   . LEU A 150 ? 0.27730 0.40805 0.31388 -0.04170 -0.00021 -0.06594 150 LEU A CD1   
1151 C CD2   . LEU A 150 ? 0.23025 0.43673 0.31188 -0.05815 0.01953  -0.02869 150 LEU A CD2   
1152 N N     . SER A 151 ? 0.19603 0.29519 0.34730 -0.03546 -0.01979 0.00916  151 SER A N     
1153 C CA    . SER A 151 ? 0.22246 0.26518 0.38317 -0.04154 -0.00281 0.00346  151 SER A CA    
1154 C C     . SER A 151 ? 0.26565 0.21571 0.42571 -0.03889 -0.00690 0.00436  151 SER A C     
1155 O O     . SER A 151 ? 0.28864 0.25775 0.45995 -0.03100 -0.00112 0.01212  151 SER A O     
1156 C CB    . SER A 151 ? 0.28917 0.32385 0.37847 0.03914  -0.01764 -0.02645 151 SER A CB    
1157 O OG    . SER A 151 ? 0.34660 0.40929 0.37037 0.02478  -0.03893 -0.04613 151 SER A OG    
1158 N N     . LYS A 152 ? 0.28812 0.20843 0.42845 -0.00824 -0.01416 0.01018  152 LYS A N     
1159 C CA    . LYS A 152 ? 0.32053 0.27339 0.43423 0.00757  -0.00903 0.01043  152 LYS A CA    
1160 C C     . LYS A 152 ? 0.28332 0.30728 0.44242 -0.02617 -0.00406 -0.00443 152 LYS A C     
1161 O O     . LYS A 152 ? 0.29870 0.26349 0.45321 -0.01139 -0.00749 -0.01148 152 LYS A O     
1162 C CB    . LYS A 152 ? 0.38483 0.34983 0.42692 0.01331  -0.01526 0.03880  152 LYS A CB    
1163 C CG    . LYS A 152 ? 0.42065 0.40071 0.42607 -0.00647 -0.00273 0.09400  152 LYS A CG    
1164 C CD    . LYS A 152 ? 0.43995 0.43494 0.42433 0.00329  0.01397  0.14884  152 LYS A CD    
1165 N N     . ARG A 153 ? 0.28774 0.38576 0.43691 0.01801  0.00072  -0.01967 153 ARG A N     
1166 C CA    . ARG A 153 ? 0.30921 0.45817 0.40833 0.04706  -0.01584 -0.05178 153 ARG A CA    
1167 C C     . ARG A 153 ? 0.37392 0.49390 0.42206 0.09915  -0.03660 -0.07339 153 ARG A C     
1168 O O     . ARG A 153 ? 0.39836 0.51838 0.42994 0.06373  -0.04521 -0.07019 153 ARG A O     
1169 C CB    . ARG A 153 ? 0.30469 0.39015 0.38154 0.07386  0.00780  -0.04314 153 ARG A CB    
1170 C CG    . ARG A 153 ? 0.28354 0.29232 0.35116 0.03530  0.01726  -0.00614 153 ARG A CG    
1171 C CD    . ARG A 153 ? 0.31623 0.25484 0.32766 0.06703  0.02436  0.02774  153 ARG A CD    
1172 N NE    . ARG A 153 ? 0.30467 0.27403 0.30759 0.04493  0.00460  0.02389  153 ARG A NE    
1173 C CZ    . ARG A 153 ? 0.27691 0.24524 0.30709 0.03928  -0.01056 0.00373  153 ARG A CZ    
1174 N NH1   . ARG A 153 ? 0.27402 0.24324 0.30891 0.04012  -0.02365 -0.00144 153 ARG A NH1   
1175 N NH2   . ARG A 153 ? 0.28885 0.25279 0.30410 -0.02409 -0.00566 -0.01150 153 ARG A NH2   
1176 C C1    . GOL B .   ? 0.62378 0.57168 0.78779 0.09329  0.10676  -0.02242 201 GOL A C1    
1177 O O1    . GOL B .   ? 0.64395 0.58494 0.79889 0.12548  0.10597  -0.01986 201 GOL A O1    
1178 C C2    . GOL B .   ? 0.62661 0.61561 0.78394 0.09259  0.10738  -0.03649 201 GOL A C2    
1179 O O2    . GOL B .   ? 0.64374 0.62611 0.78683 0.10940  0.12035  -0.03566 201 GOL A O2    
1180 C C3    . GOL B .   ? 0.62983 0.56762 0.77397 0.09504  0.10764  -0.03699 201 GOL A C3    
1181 O O3    . GOL B .   ? 0.65862 0.60536 0.76835 0.08631  0.09798  -0.03903 201 GOL A O3    
1182 N N1    . UMP C .   ? 0.32879 0.25885 0.24254 -0.00965 0.02547  0.02228  202 UMP A N1    
1183 C C2    . UMP C .   ? 0.33156 0.28807 0.25342 -0.00509 0.02795  0.00951  202 UMP A C2    
1184 N N3    . UMP C .   ? 0.31396 0.25126 0.23731 -0.03323 0.01053  0.02791  202 UMP A N3    
1185 C C4    . UMP C .   ? 0.31199 0.24846 0.21639 -0.01363 0.00583  0.00695  202 UMP A C4    
1186 C C5    . UMP C .   ? 0.34426 0.23788 0.20905 0.02177  0.01234  0.05222  202 UMP A C5    
1187 C C6    . UMP C .   ? 0.39939 0.21709 0.23163 0.07610  -0.00141 0.02208  202 UMP A C6    
1188 O O2    . UMP C .   ? 0.25405 0.35786 0.26163 -0.03025 0.03792  0.05774  202 UMP A O2    
1189 O O4    . UMP C .   ? 0.27939 0.22253 0.18111 -0.03690 0.01230  0.01351  202 UMP A O4    
1190 C "C1'" . UMP C .   ? 0.27434 0.33825 0.24802 -0.06816 0.01812  0.03692  202 UMP A "C1'" 
1191 C "C2'" . UMP C .   ? 0.25968 0.34309 0.24795 -0.06299 0.02306  0.00971  202 UMP A "C2'" 
1192 C "C3'" . UMP C .   ? 0.26894 0.33125 0.26221 -0.10340 0.05067  0.02332  202 UMP A "C3'" 
1193 C "C4'" . UMP C .   ? 0.25863 0.42713 0.29803 -0.10449 0.04106  0.02452  202 UMP A "C4'" 
1194 O "O3'" . UMP C .   ? 0.31007 0.35594 0.23239 -0.07695 0.07088  0.00678  202 UMP A "O3'" 
1195 O "O4'" . UMP C .   ? 0.28091 0.35173 0.26449 -0.05857 0.02980  0.04377  202 UMP A "O4'" 
1196 C "C5'" . UMP C .   ? 0.31841 0.53262 0.37220 -0.07126 0.00307  -0.00426 202 UMP A "C5'" 
1197 O "O5'" . UMP C .   ? 0.30668 0.55789 0.45077 -0.12302 -0.01703 -0.02346 202 UMP A "O5'" 
1198 P P     . UMP C .   ? 0.41622 0.61365 0.50576 -0.08810 -0.00661 -0.02891 202 UMP A P     
1199 O OP1   . UMP C .   ? 0.45370 0.64609 0.52201 -0.05458 -0.02986 -0.06595 202 UMP A OP1   
1200 O OP2   . UMP C .   ? 0.50469 0.65831 0.52022 -0.05157 0.04181  -0.00516 202 UMP A OP2   
1201 O OP3   . UMP C .   ? 0.42458 0.65156 0.51807 -0.04796 -0.01372 -0.04435 202 UMP A OP3   
1202 P P     . PO4 D .   ? 0.87079 0.98697 0.93894 0.10919  0.06448  0.00508  203 PO4 A P     
1203 O O1    . PO4 D .   ? 0.86353 0.97183 0.93995 0.10617  0.07093  0.00193  203 PO4 A O1    
1204 O O2    . PO4 D .   ? 0.87050 0.97347 0.93858 0.09875  0.07072  0.00348  203 PO4 A O2    
1205 O O3    . PO4 D .   ? 0.87541 0.97399 0.94023 0.06859  0.06409  0.00789  203 PO4 A O3    
1206 O O4    . PO4 D .   ? 0.86268 0.97936 0.93716 0.09800  0.05383  -0.00152 203 PO4 A O4    
1207 P P     . PO4 E .   ? 0.92888 0.98948 1.05661 0.04524  0.01075  -0.08373 204 PO4 A P     
1208 O O1    . PO4 E .   ? 0.93416 0.97287 1.05826 0.03715  0.00393  -0.07953 204 PO4 A O1    
1209 O O2    . PO4 E .   ? 0.92907 0.97750 1.05637 0.01947  0.01105  -0.08415 204 PO4 A O2    
1210 O O3    . PO4 E .   ? 0.92407 0.97141 1.05801 0.03090  0.00674  -0.07959 204 PO4 A O3    
1211 O O4    . PO4 E .   ? 0.93015 0.98305 1.05645 0.03690  0.02039  -0.08226 204 PO4 A O4    
1212 O O     . HOH F .   ? 0.34610 0.26234 0.33146 0.04137  0.07002  -0.04340 301 HOH A O     
1213 O O     . HOH F .   ? 0.29527 0.86679 0.71751 -0.17393 -0.00892 -0.07948 302 HOH A O     
1214 O O     . HOH F .   ? 0.53735 0.39524 0.48866 -0.07443 -0.05437 0.05822  303 HOH A O     
1215 O O     . HOH F .   ? 0.52437 0.48665 0.54521 0.04585  0.01247  -0.02287 304 HOH A O     
1216 O O     . HOH F .   ? 0.52431 0.76633 0.29539 0.19573  0.01814  0.13835  305 HOH A O     
1217 O O     . HOH F .   ? 0.45663 0.33391 0.44434 0.04982  0.03699  -0.18632 306 HOH A O     
1218 O O     . HOH F .   ? 0.59663 0.53651 0.58586 -0.15074 -0.07458 -0.08919 307 HOH A O     
1219 O O     . HOH F .   ? 0.35650 0.64296 0.43683 0.11102  0.11129  0.28626  308 HOH A O     
1220 O O     . HOH F .   ? 0.55409 0.58460 0.46666 0.00896  0.01407  -0.18785 309 HOH A O     
1221 O O     . HOH F .   ? 0.42499 0.27438 0.33468 0.02634  -0.00301 0.03371  310 HOH A O     
1222 O O     . HOH F .   ? 0.24729 0.24729 0.38701 0.00000  0.00000  0.00000  311 HOH A O     
1223 O O     . HOH F .   ? 0.62463 0.49546 0.39867 -0.18506 -0.01428 0.18375  312 HOH A O     
1224 O O     . HOH F .   ? 0.36743 0.44680 0.70044 0.00228  -0.02551 0.06067  313 HOH A O     
1225 O O     . HOH F .   ? 0.65200 0.40865 0.86150 -0.09732 -0.00825 -0.03515 314 HOH A O     
1226 O O     . HOH F .   ? 0.83386 0.52052 0.82442 -0.09246 0.01826  -0.18548 315 HOH A O     
1227 O O     . HOH F .   ? 0.68798 0.36468 0.42167 -0.16922 0.18830  -0.02104 316 HOH A O     
1228 O O     . HOH F .   ? 0.64059 0.53770 0.34536 -0.04754 -0.17748 -0.06259 317 HOH A O     
1229 O O     . HOH F .   ? 0.62636 0.52664 0.54138 0.19413  0.04319  -0.01216 318 HOH A O     
1230 O O     . HOH F .   ? 0.25334 0.38124 0.28791 -0.01041 -0.01925 0.02023  319 HOH A O     
1231 O O     . HOH F .   ? 0.39748 0.39723 0.23533 -0.05017 0.03365  -0.06309 320 HOH A O     
1232 O O     . HOH F .   ? 0.52045 0.23937 0.60733 0.05054  -0.14160 0.10572  321 HOH A O     
1233 O O     . HOH F .   ? 0.37017 0.45218 0.37497 -0.06782 0.07851  -0.15888 322 HOH A O     
1234 O O     . HOH F .   ? 0.32816 0.34215 0.37742 -0.12464 -0.10702 0.18414  323 HOH A O     
1235 O O     . HOH F .   ? 0.35075 0.57213 0.52295 -0.04004 -0.02513 -0.09854 324 HOH A O     
1236 O O     . HOH F .   ? 0.29469 0.17404 0.18325 0.04689  0.04057  0.01314  325 HOH A O     
1237 O O     . HOH F .   ? 0.35728 0.60683 0.33120 0.13781  0.05482  0.06324  326 HOH A O     
1238 O O     . HOH F .   ? 0.58832 0.72460 0.38675 0.05268  -0.10670 -0.09714 327 HOH A O     
1239 O O     . HOH F .   ? 0.35681 0.42037 0.33483 0.03257  0.13852  0.00121  328 HOH A O     
1240 O O     . HOH F .   ? 0.21406 0.25607 0.33381 -0.00649 0.04190  -0.00485 329 HOH A O     
1241 O O     . HOH F .   ? 0.70717 0.54009 0.36677 0.05642  0.06450  0.00914  330 HOH A O     
1242 O O     . HOH F .   ? 0.74375 0.46084 0.62555 -0.06025 0.15302  0.12480  331 HOH A O     
1243 O O     . HOH F .   ? 0.71879 0.60301 0.40685 -0.03309 0.05302  -0.09229 332 HOH A O     
1244 O O     . HOH F .   ? 0.38408 0.43279 0.62600 -0.12459 -0.00688 0.24241  333 HOH A O     
1245 O O     . HOH F .   ? 0.31199 0.45763 0.66493 0.03484  0.06661  0.21869  334 HOH A O     
1246 O O     . HOH F .   ? 0.55636 0.62122 0.29619 -0.15204 0.02379  0.08697  335 HOH A O     
1247 O O     . HOH F .   ? 0.30544 0.26389 0.30421 0.00327  -0.02982 -0.09742 336 HOH A O     
1248 O O     . HOH F .   ? 0.37360 0.26141 0.19598 -0.02192 -0.08239 0.02661  337 HOH A O     
1249 O O     . HOH F .   ? 0.72212 0.81017 0.45147 0.04020  0.10327  0.19543  338 HOH A O     
1250 O O     . HOH F .   ? 0.28473 0.39204 0.18574 -0.03940 -0.08244 0.06242  339 HOH A O     
1251 O O     . HOH F .   ? 0.51188 0.30833 0.76551 0.01928  0.11586  -0.01205 340 HOH A O     
1252 O O     . HOH F .   ? 0.34104 0.45616 0.22580 0.08787  0.05098  0.04536  341 HOH A O     
1253 O O     . HOH F .   ? 0.38659 0.38615 0.46276 -0.10320 -0.04612 0.04878  342 HOH A O     
1254 O O     . HOH F .   ? 0.51410 0.56618 0.34068 -0.05955 -0.00767 -0.00327 343 HOH A O     
1255 O O     . HOH F .   ? 0.74478 0.51623 0.38808 0.04152  0.09394  0.20349  344 HOH A O     
1256 O O     . HOH F .   ? 0.54322 0.43459 0.29378 0.05083  -0.01901 0.11174  345 HOH A O     
1257 O O     . HOH F .   ? 0.56693 0.67880 0.52626 -0.18777 -0.08140 0.15425  346 HOH A O     
1258 O O     . HOH F .   ? 0.60867 0.44483 0.40910 0.12869  -0.00383 0.10690  347 HOH A O     
1259 O O     . HOH F .   ? 0.52800 0.32919 0.42551 -0.08662 0.11711  -0.16177 348 HOH A O     
1260 O O     . HOH F .   ? 0.40065 0.35856 0.30067 0.14065  0.06441  0.02700  349 HOH A O     
1261 O O     . HOH F .   ? 0.95681 0.64195 0.55740 0.06194  0.18981  0.15277  350 HOH A O     
1262 O O     . HOH F .   ? 0.69298 0.42329 0.25513 -0.00779 0.07465  0.11334  351 HOH A O     
1263 O O     . HOH F .   ? 0.58292 0.63106 0.42035 -0.06018 -0.03878 -0.00195 352 HOH A O     
1264 O O     A HOH F .   ? 0.43955 0.25987 0.33415 -0.12660 0.02075  0.00100  353 HOH A O     
1265 O O     B HOH F .   ? 0.31268 0.33939 0.38306 -0.14929 -0.08420 0.11380  353 HOH A O     
1266 O O     . HOH F .   ? 0.76542 0.56738 0.37332 -0.04403 0.00373  0.25337  354 HOH A O     
1267 O O     . HOH F .   ? 0.19329 0.45068 0.41997 0.00285  -0.04652 -0.00003 355 HOH A O     
1268 O O     . HOH F .   ? 0.78583 0.57713 0.30954 0.16927  0.10265  0.10772  356 HOH A O     
1269 O O     . HOH F .   ? 0.26083 0.38803 0.36656 0.02789  0.02865  -0.01637 357 HOH A O     
1270 O O     . HOH F .   ? 0.51920 0.37588 0.77824 -0.05090 0.13881  0.06591  358 HOH A O     
1271 O O     . HOH F .   ? 0.71823 0.63971 0.49315 0.19860  -0.22142 0.13048  359 HOH A O     
1272 O O     . HOH F .   ? 0.56777 0.41125 0.64899 0.24666  -0.09455 0.02492  360 HOH A O     
1273 O O     . HOH F .   ? 0.65396 0.81165 0.51965 0.09943  -0.05647 0.09944  361 HOH A O     
1274 O O     . HOH F .   ? 0.60163 0.46173 0.50420 -0.20651 0.06295  0.00472  362 HOH A O     
1275 O O     . HOH F .   ? 0.54025 0.41288 0.63897 0.12932  -0.03234 -0.16407 363 HOH A O     
1276 O O     . HOH F .   ? 0.22555 0.19413 0.15401 -0.01075 -0.00542 -0.00159 364 HOH A O     
1277 O O     . HOH F .   ? 0.27669 0.36661 0.39317 -0.07694 0.05883  0.00631  365 HOH A O     
1278 O O     . HOH F .   ? 0.56844 0.52260 0.39622 0.11534  0.13159  -0.04445 366 HOH A O     
1279 O O     . HOH F .   ? 0.54974 0.29858 0.24073 0.11041  0.00252  -0.04511 367 HOH A O     
1280 O O     . HOH F .   ? 0.48225 0.57898 0.53219 0.19070  -0.10230 -0.11446 368 HOH A O     
1281 O O     . HOH F .   ? 0.38331 0.29241 0.59211 0.03741  -0.16158 -0.09000 369 HOH A O     
1282 O O     . HOH F .   ? 0.39876 0.54300 0.40391 0.12640  0.00439  -0.09503 370 HOH A O     
1283 O O     . HOH F .   ? 0.24042 0.18630 0.15734 0.02140  -0.02373 0.02900  371 HOH A O     
1284 O O     . HOH F .   ? 0.31527 0.24658 0.60079 0.00333  -0.09756 -0.05182 372 HOH A O     
1285 O O     . HOH F .   ? 0.40115 0.44100 0.46213 0.12471  0.01719  -0.10383 373 HOH A O     
1286 O O     . HOH F .   ? 0.21497 0.25076 0.18828 0.03972  0.01003  -0.02450 374 HOH A O     
1287 O O     . HOH F .   ? 0.48781 0.28889 0.72930 0.01779  -0.15714 0.17065  375 HOH A O     
1288 O O     . HOH F .   ? 0.25264 0.18427 0.31341 -0.00994 0.01136  0.00215  376 HOH A O     
1289 O O     . HOH F .   ? 0.35466 0.44034 0.31928 0.07499  -0.10111 -0.02660 377 HOH A O     
1290 O O     . HOH F .   ? 0.35224 0.43110 0.53792 0.05516  -0.07642 -0.18958 378 HOH A O     
1291 O O     . HOH F .   ? 0.56952 0.23061 0.51574 -0.09198 0.16152  -0.07778 379 HOH A O     
1292 O O     . HOH F .   ? 0.51058 0.49608 0.46578 0.06448  -0.23628 0.05850  380 HOH A O     
1293 O O     . HOH F .   ? 0.40598 0.37739 0.66092 0.01579  0.05111  0.14835  381 HOH A O     
1294 O O     . HOH F .   ? 0.59103 0.31160 0.57710 -0.03485 -0.13225 -0.15684 382 HOH A O     
1295 O O     . HOH F .   ? 0.71984 0.37359 0.54647 -0.05458 -0.18895 0.21076  383 HOH A O     
1296 O O     . HOH F .   ? 0.42721 0.42511 0.51199 0.12185  0.11045  0.09412  384 HOH A O     
1297 O O     . HOH F .   ? 0.41729 0.94897 0.38309 -0.00647 -0.12492 -0.16591 385 HOH A O     
1298 O O     . HOH F .   ? 0.58165 0.61564 0.54035 -0.19046 0.23079  -0.04847 386 HOH A O     
1299 O O     . HOH F .   ? 0.28392 0.37358 0.39093 -0.06919 0.04977  -0.13880 387 HOH A O     
1300 O O     . HOH F .   ? 0.24735 0.38200 0.87557 -0.01086 -0.00985 0.18737  388 HOH A O     
1301 O O     . HOH F .   ? 0.64057 0.78045 0.45958 -0.11890 0.05450  0.26430  389 HOH A O     
1302 O O     . HOH F .   ? 0.61913 0.52573 0.57388 0.28342  -0.20698 -0.14378 390 HOH A O     
1303 O O     . HOH F .   ? 0.49362 0.71320 0.38252 0.05025  0.16924  -0.08401 391 HOH A O     
1304 O O     . HOH F .   ? 0.58075 0.38507 0.60740 -0.04753 0.05443  -0.02781 392 HOH A O     
1305 O O     . HOH F .   ? 0.48138 0.39225 0.47922 -0.07740 0.16175  -0.10595 393 HOH A O     
1306 O O     . HOH F .   ? 0.41722 0.33763 0.35442 0.10026  0.14597  0.00490  394 HOH A O     
1307 O O     . HOH F .   ? 0.43173 0.56470 0.61323 -0.12601 -0.00662 -0.09649 395 HOH A O     
1308 O O     . HOH F .   ? 0.54212 0.53903 0.53082 -0.14333 0.06137  0.09865  396 HOH A O     
1309 O O     . HOH F .   ? 0.38573 0.37974 0.44823 0.02042  0.00181  0.14249  397 HOH A O     
1310 O O     . HOH F .   ? 0.38606 0.69707 0.51027 -0.02757 0.10449  -0.04964 398 HOH A O     
1311 O O     . HOH F .   ? 0.62633 0.49722 0.45550 -0.00919 0.07883  -0.10239 399 HOH A O     
1312 O O     . HOH F .   ? 0.42523 0.73803 0.41014 0.06179  0.07577  -0.25622 400 HOH A O     
# 
