data_9D10
# 
_entry.id   9D10 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9D10         pdb_00009d10 10.2210/pdb9d10/pdb 
WWPDB D_1000287151 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9D10 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              smarius@uwm.edu 
_pdbx_contact_author.name_first         Marius 
_pdbx_contact_author.name_last          Schmidt 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0962-9468 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Malla, T.N.' 1 0000-0002-1387-0801 
'Schmidt, M.' 2 0000-0002-0962-9468 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Iucrj 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                36 
_citation.page_last                 48 
_citation.title                     
'Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2052252524010868 
_citation.pdbx_database_id_PubMed   39575537 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Malla, T.N.'      1  ? 
primary 'Muniyappan, S.'   2  ? 
primary 'Menendez, D.'     3  ? 
primary 'Ogukwe, F.'       4  ? 
primary 'Dale, A.N.'       5  ? 
primary 'Clayton, J.D.'    6  ? 
primary 'Weatherall, D.D.' 7  ? 
primary 'Karki, P.'        8  ? 
primary 'Dangi, S.'        9  ? 
primary 'Mandella, V.'     10 ? 
primary 'Pacheco, A.A.'    11 ? 
primary 'Stojkovic, E.A.'  12 ? 
primary 'Rose, S.L.'       13 ? 
primary 'Orlans, J.'       14 ? 
primary 'Basu, S.'         15 ? 
primary 'de Sanctis, D.'   16 ? 
primary 'Schmidt, M.'      17 ? 
# 
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 'Photoactive yellow protein' 13888.575 1  ? ? ? ? 
2 non-polymer syn 
;4'-HYDROXYCINNAMIC ACID
;
164.158   1  ? ? ? ? 
3 water       nat water                        18.015    52 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PYP 
# 
_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       
;MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGKNFFKDVAPCTDSPEFYGKFK
EGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGKNFFKDVAPCTDSPEFYGKFK
EGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV
;
_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 
;4'-HYDROXYCINNAMIC ACID
;
HC4 
3 water                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   HIS n 
1 4   VAL n 
1 5   ALA n 
1 6   PHE n 
1 7   GLY n 
1 8   SER n 
1 9   GLU n 
1 10  ASP n 
1 11  ILE n 
1 12  GLU n 
1 13  ASN n 
1 14  THR n 
1 15  LEU n 
1 16  ALA n 
1 17  LYS n 
1 18  MET n 
1 19  ASP n 
1 20  ASP n 
1 21  GLY n 
1 22  GLN n 
1 23  LEU n 
1 24  ASP n 
1 25  GLY n 
1 26  LEU n 
1 27  ALA n 
1 28  PHE n 
1 29  GLY n 
1 30  ALA n 
1 31  ILE n 
1 32  GLN n 
1 33  LEU n 
1 34  ASP n 
1 35  GLY n 
1 36  ASP n 
1 37  GLY n 
1 38  ASN n 
1 39  ILE n 
1 40  LEU n 
1 41  GLN n 
1 42  TYR n 
1 43  ASN n 
1 44  ALA n 
1 45  ALA n 
1 46  GLU n 
1 47  GLY n 
1 48  ASP n 
1 49  ILE n 
1 50  THR n 
1 51  GLY n 
1 52  ARG n 
1 53  ASP n 
1 54  PRO n 
1 55  LYS n 
1 56  GLN n 
1 57  VAL n 
1 58  ILE n 
1 59  GLY n 
1 60  LYS n 
1 61  ASN n 
1 62  PHE n 
1 63  PHE n 
1 64  LYS n 
1 65  ASP n 
1 66  VAL n 
1 67  ALA n 
1 68  PRO n 
1 69  CYS n 
1 70  THR n 
1 71  ASP n 
1 72  SER n 
1 73  PRO n 
1 74  GLU n 
1 75  PHE n 
1 76  TYR n 
1 77  GLY n 
1 78  LYS n 
1 79  PHE n 
1 80  LYS n 
1 81  GLU n 
1 82  GLY n 
1 83  VAL n 
1 84  ALA n 
1 85  SER n 
1 86  GLY n 
1 87  ASN n 
1 88  LEU n 
1 89  ASN n 
1 90  THR n 
1 91  MET n 
1 92  PHE n 
1 93  GLU n 
1 94  TYR n 
1 95  THR n 
1 96  PHE n 
1 97  ASP n 
1 98  TYR n 
1 99  GLN n 
1 100 MET n 
1 101 THR n 
1 102 PRO n 
1 103 THR n 
1 104 LYS n 
1 105 VAL n 
1 106 LYS n 
1 107 VAL n 
1 108 HIS n 
1 109 MET n 
1 110 LYS n 
1 111 LYS n 
1 112 ALA n 
1 113 LEU n 
1 114 SER n 
1 115 GLY n 
1 116 ASP n 
1 117 SER n 
1 118 TYR n 
1 119 TRP n 
1 120 VAL n 
1 121 PHE n 
1 122 VAL n 
1 123 LYS n 
1 124 ARG n 
1 125 VAL 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                   125 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 pyp 
_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      'Halorhodospira halophila' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1053 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ?                    'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                  ?                    'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                ?                    'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ?                    'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                  ?                    'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                 ?                    'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ?                    'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                   ?                    'C2 H5 N O2'     75.067  
HC4 non-polymer         . 
;4'-HYDROXYCINNAMIC ACID
;
'PARA-COUMARIC ACID' 'C9 H8 O3'       164.158 
HIS 'L-peptide linking' y HISTIDINE                 ?                    'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                     ?                    'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ?                    'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                   ?                    'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                    ?                    'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                ?                    'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ?                    'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                   ?                    'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                    ?                    'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                 ?                    'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                ?                    'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                  ?                    'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                    ?                    'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  ASP 53  53  53  ASP ASP 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  GLN 56  56  56  GLN GLN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  CYS 69  69  69  CYS CYS A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  PHE 96  96  96  PHE PHE A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 HIS 108 108 108 HIS HIS A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 TRP 119 119 119 TRP TRP A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HC4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HC4 
_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 HC4 1  201 126 HC4 HC4 A . 
C 3 HOH 1  301 63  HOH HOH A . 
C 3 HOH 2  302 46  HOH HOH A . 
C 3 HOH 3  303 196 HOH HOH A . 
C 3 HOH 4  304 45  HOH HOH A . 
C 3 HOH 5  305 19  HOH HOH A . 
C 3 HOH 6  306 5   HOH HOH A . 
C 3 HOH 7  307 83  HOH HOH A . 
C 3 HOH 8  308 70  HOH HOH A . 
C 3 HOH 9  309 13  HOH HOH A . 
C 3 HOH 10 310 248 HOH HOH A . 
C 3 HOH 11 311 162 HOH HOH A . 
C 3 HOH 12 312 40  HOH HOH A . 
C 3 HOH 13 313 289 HOH HOH A . 
C 3 HOH 14 314 215 HOH HOH A . 
C 3 HOH 15 315 33  HOH HOH A . 
C 3 HOH 16 316 76  HOH HOH A . 
C 3 HOH 17 317 1   HOH HOH A . 
C 3 HOH 18 318 208 HOH HOH A . 
C 3 HOH 19 319 64  HOH HOH A . 
C 3 HOH 20 320 2   HOH HOH A . 
C 3 HOH 21 321 98  HOH HOH A . 
C 3 HOH 22 322 7   HOH HOH A . 
C 3 HOH 23 323 65  HOH HOH A . 
C 3 HOH 24 324 59  HOH HOH A . 
C 3 HOH 25 325 21  HOH HOH A . 
C 3 HOH 26 326 72  HOH HOH A . 
C 3 HOH 27 327 89  HOH HOH A . 
C 3 HOH 28 328 4   HOH HOH A . 
C 3 HOH 29 329 101 HOH HOH A . 
C 3 HOH 30 330 12  HOH HOH A . 
C 3 HOH 31 331 68  HOH HOH A . 
C 3 HOH 32 332 302 HOH HOH A . 
C 3 HOH 33 333 211 HOH HOH A . 
C 3 HOH 34 334 117 HOH HOH A . 
C 3 HOH 35 335 9   HOH HOH A . 
C 3 HOH 36 336 97  HOH HOH A . 
C 3 HOH 37 337 57  HOH HOH A . 
C 3 HOH 38 338 22  HOH HOH A . 
C 3 HOH 39 339 209 HOH HOH A . 
C 3 HOH 40 340 52  HOH HOH A . 
C 3 HOH 41 341 198 HOH HOH A . 
C 3 HOH 42 342 226 HOH HOH A . 
C 3 HOH 43 343 41  HOH HOH A . 
C 3 HOH 44 344 37  HOH HOH A . 
C 3 HOH 45 345 252 HOH HOH A . 
C 3 HOH 46 346 71  HOH HOH A . 
C 3 HOH 47 347 55  HOH HOH A . 
C 3 HOH 48 348 264 HOH HOH A . 
C 3 HOH 49 349 192 HOH HOH A . 
C 3 HOH 50 350 82  HOH HOH A . 
C 3 HOH 51 351 305 HOH HOH A . 
C 3 HOH 52 352 242 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .         4 
# 
_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                     9D10 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.360 
_cell.length_a_esd                 ? 
_cell.length_b                     41.360 
_cell.length_b_esd                 ? 
_cell.length_c                     118.870 
_cell.length_c_esd                 ? 
_cell.volume                       176101.865 
_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                         9D10 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            'P 65' 
_symmetry.space_group_name_H-M             'P 65' 
_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                   9D10 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.80 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM MES, 40% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             'room temperature' 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI JUNGFRAU 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-03 
_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                    multilayer 
_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   1.1 
_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                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          27.83 
_reflns.entry_id                                       9D10 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               118 
_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                                     2377266 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                135 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          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                                ? 
_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                                   0.1 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             513 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.65 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  3.0 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                               36.75 
_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                                 9D10 
_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                            1.80 
_refine.ls_d_res_low                             35.82 
_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                     9689 
_refine.ls_number_reflns_R_free                  500 
_refine.ls_number_reflns_R_work                  9189 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.13 
_refine.ls_percent_reflns_R_free                 5.16 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1548 
_refine.ls_R_factor_R_free                       0.1980 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1525 
_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                          0.02 
_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                 26.1160 
_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                            0.2234 
_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                       1.80 
_refine_hist.d_res_low                        35.82 
_refine_hist.number_atoms_solvent             52 
_refine_hist.number_atoms_total               1039 
_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        976 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_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' ? 0.0063  ? 1035 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8187  ? 1395 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0524  ? 147  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0040  ? 185  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.7657 ? 380  ? 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' 1.80 1.98  . . 85  1867 73.69 . . . . 0.3350 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 1.98 2.27  . . 147 2290 92.63 . . . . 0.1973 . . . . . . . . . . . 0.3008 
'X-RAY DIFFRACTION' 2.27 2.86  . . 142 2473 98.38 . . . . 0.1912 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 2.86 35.82 . . 126 2559 99.67 . . . . 0.1097 . . . . . . . . . . . 0.1571 
# 
_struct.entry_id                     9D10 
_struct.title                        'Photoactive Yellow Protein, crystals from PEG, room temperature' 
_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        9D10 
_struct_keywords.text            'photoactive yellow protein, phototaxis, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PYP_HALHA 
_struct_ref.pdbx_db_accession          P16113 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGKNFFKDVAPCTDSPEFYGKFK
EGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV
;
_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              9D10 
_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                 125 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P16113 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  125 
_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       125 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10 ? LYS A 17 ? ASP A 10 LYS A 17 1 ? 8  
HELX_P HELX_P2 AA2 ASP A 19 ? ASP A 24 ? ASP A 19 ASP A 24 1 ? 6  
HELX_P HELX_P3 AA3 ASN A 43 ? GLY A 51 ? ASN A 43 GLY A 51 1 ? 9  
HELX_P HELX_P4 AA4 ASP A 53 ? ILE A 58 ? ASP A 53 ILE A 58 1 ? 6  
HELX_P HELX_P5 AA5 ALA A 67 ? ASP A 71 ? ALA A 67 ASP A 71 5 ? 5  
HELX_P HELX_P6 AA6 PHE A 75 ? GLY A 86 ? PHE A 75 GLY A 86 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            69 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           HC4 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C1 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             69 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            HC4 
_struct_conn.ptnr2_auth_seq_id             201 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.764 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      HC4 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      69 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       HC4 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        201 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       69 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C1 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        HC4 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
# 
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 ILE A 39  ? TYR A 42  ? ILE A 39  TYR A 42  
AA1 2 GLY A 29  ? LEU A 33  ? GLY A 29  LEU A 33  
AA1 3 TYR A 118 ? ARG A 124 ? TYR A 118 ARG A 124 
AA1 4 THR A 103 ? LYS A 111 ? THR A 103 LYS A 111 
AA1 5 ASN A 89  ? PHE A 96  ? ASN A 89  PHE A 96  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 40  ? O LEU A 40  N GLN A 32  ? N GLN A 32  
AA1 2 3 N LEU A 33  ? N LEU A 33  O TYR A 118 ? O TYR A 118 
AA1 3 4 O TRP A 119 ? O TRP A 119 N LYS A 110 ? N LYS A 110 
AA1 4 5 O VAL A 107 ? O VAL A 107 N PHE A 92  ? N PHE A 92  
# 
_pdbx_entry_details.entry_id                   9D10 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    65 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 42 ? ? -161.42 109.26 
2 1 PHE A 75 ? ? -126.34 -76.24 
3 1 ASN A 89 ? ? -163.04 93.19  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 x-y,x,z+5/6   
3 y,-x+y,z+1/6  
4 -y,x-y,z+2/3  
5 -x+y,-x,z+1/3 
6 -x,-y,z+1/2   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         16.9965698696 
_pdbx_refine_tls.origin_y         -13.3318236835 
_pdbx_refine_tls.origin_z         -8.8799260354 
_pdbx_refine_tls.T[1][1]          0.238428327064 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0172101737317 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          8.32913196561e-06 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.209479672901 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0176057458537 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.196047766574 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.48322434133 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.116006978683 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.673750179311 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.91564528199 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0809794688821 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.1859526439 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.093162239783 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0687028177422 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0828415304816 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.030649792494 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0916300773002 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.18122940492 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0489000848857 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0440871906535 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.00588948793938 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     305 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HC4 C1     C N N 137 
HC4 O1     O N N 138 
HC4 O2     O N N 139 
HC4 C2     C N N 140 
HC4 C3     C N N 141 
HC4 "C1'"  C Y N 142 
HC4 "C2'"  C Y N 143 
HC4 "C3'"  C Y N 144 
HC4 "C4'"  C Y N 145 
HC4 "C5'"  C Y N 146 
HC4 "C6'"  C Y N 147 
HC4 "O4'"  O N N 148 
HC4 HO2    H N N 149 
HC4 H2     H N N 150 
HC4 H3     H N N 151 
HC4 "H2'"  H N N 152 
HC4 "H3'"  H N N 153 
HC4 "H5'"  H N N 154 
HC4 "H6'"  H N N 155 
HC4 "HO4'" H N N 156 
HIS N      N N N 157 
HIS CA     C N S 158 
HIS C      C N N 159 
HIS O      O N N 160 
HIS CB     C N N 161 
HIS CG     C Y N 162 
HIS ND1    N Y N 163 
HIS CD2    C Y N 164 
HIS CE1    C Y N 165 
HIS NE2    N Y N 166 
HIS OXT    O N N 167 
HIS H      H N N 168 
HIS H2     H N N 169 
HIS HA     H N N 170 
HIS HB2    H N N 171 
HIS HB3    H N N 172 
HIS HD1    H N N 173 
HIS HD2    H N N 174 
HIS HE1    H N N 175 
HIS HE2    H N N 176 
HIS HXT    H N N 177 
HOH O      O N N 178 
HOH H1     H N N 179 
HOH H2     H N N 180 
ILE N      N N N 181 
ILE CA     C N S 182 
ILE C      C N N 183 
ILE O      O N N 184 
ILE CB     C N S 185 
ILE CG1    C N N 186 
ILE CG2    C N N 187 
ILE CD1    C N N 188 
ILE OXT    O N N 189 
ILE H      H N N 190 
ILE H2     H N N 191 
ILE HA     H N N 192 
ILE HB     H N N 193 
ILE HG12   H N N 194 
ILE HG13   H N N 195 
ILE HG21   H N N 196 
ILE HG22   H N N 197 
ILE HG23   H N N 198 
ILE HD11   H N N 199 
ILE HD12   H N N 200 
ILE HD13   H N N 201 
ILE HXT    H N N 202 
LEU N      N N N 203 
LEU CA     C N S 204 
LEU C      C N N 205 
LEU O      O N N 206 
LEU CB     C N N 207 
LEU CG     C N N 208 
LEU CD1    C N N 209 
LEU CD2    C N N 210 
LEU OXT    O N N 211 
LEU H      H N N 212 
LEU H2     H N N 213 
LEU HA     H N N 214 
LEU HB2    H N N 215 
LEU HB3    H N N 216 
LEU HG     H N N 217 
LEU HD11   H N N 218 
LEU HD12   H N N 219 
LEU HD13   H N N 220 
LEU HD21   H N N 221 
LEU HD22   H N N 222 
LEU HD23   H N N 223 
LEU HXT    H N N 224 
LYS N      N N N 225 
LYS CA     C N S 226 
LYS C      C N N 227 
LYS O      O N N 228 
LYS CB     C N N 229 
LYS CG     C N N 230 
LYS CD     C N N 231 
LYS CE     C N N 232 
LYS NZ     N N N 233 
LYS OXT    O N N 234 
LYS H      H N N 235 
LYS H2     H N N 236 
LYS HA     H N N 237 
LYS HB2    H N N 238 
LYS HB3    H N N 239 
LYS HG2    H N N 240 
LYS HG3    H N N 241 
LYS HD2    H N N 242 
LYS HD3    H N N 243 
LYS HE2    H N N 244 
LYS HE3    H N N 245 
LYS HZ1    H N N 246 
LYS HZ2    H N N 247 
LYS HZ3    H N N 248 
LYS HXT    H N N 249 
MET N      N N N 250 
MET CA     C N S 251 
MET C      C N N 252 
MET O      O N N 253 
MET CB     C N N 254 
MET CG     C N N 255 
MET SD     S N N 256 
MET CE     C N N 257 
MET OXT    O N N 258 
MET H      H N N 259 
MET H2     H N N 260 
MET HA     H N N 261 
MET HB2    H N N 262 
MET HB3    H N N 263 
MET HG2    H N N 264 
MET HG3    H N N 265 
MET HE1    H N N 266 
MET HE2    H N N 267 
MET HE3    H N N 268 
MET HXT    H N N 269 
PHE N      N N N 270 
PHE CA     C N S 271 
PHE C      C N N 272 
PHE O      O N N 273 
PHE CB     C N N 274 
PHE CG     C Y N 275 
PHE CD1    C Y N 276 
PHE CD2    C Y N 277 
PHE CE1    C Y N 278 
PHE CE2    C Y N 279 
PHE CZ     C Y N 280 
PHE OXT    O N N 281 
PHE H      H N N 282 
PHE H2     H N N 283 
PHE HA     H N N 284 
PHE HB2    H N N 285 
PHE HB3    H N N 286 
PHE HD1    H N N 287 
PHE HD2    H N N 288 
PHE HE1    H N N 289 
PHE HE2    H N N 290 
PHE HZ     H N N 291 
PHE HXT    H N N 292 
PRO N      N N N 293 
PRO CA     C N S 294 
PRO C      C N N 295 
PRO O      O N N 296 
PRO CB     C N N 297 
PRO CG     C N N 298 
PRO CD     C N N 299 
PRO OXT    O N N 300 
PRO H      H N N 301 
PRO HA     H N N 302 
PRO HB2    H N N 303 
PRO HB3    H N N 304 
PRO HG2    H N N 305 
PRO HG3    H N N 306 
PRO HD2    H N N 307 
PRO HD3    H N N 308 
PRO HXT    H N N 309 
SER N      N N N 310 
SER CA     C N S 311 
SER C      C N N 312 
SER O      O N N 313 
SER CB     C N N 314 
SER OG     O N N 315 
SER OXT    O N N 316 
SER H      H N N 317 
SER H2     H N N 318 
SER HA     H N N 319 
SER HB2    H N N 320 
SER HB3    H N N 321 
SER HG     H N N 322 
SER HXT    H N N 323 
THR N      N N N 324 
THR CA     C N S 325 
THR C      C N N 326 
THR O      O N N 327 
THR CB     C N R 328 
THR OG1    O N N 329 
THR CG2    C N N 330 
THR OXT    O N N 331 
THR H      H N N 332 
THR H2     H N N 333 
THR HA     H N N 334 
THR HB     H N N 335 
THR HG1    H N N 336 
THR HG21   H N N 337 
THR HG22   H N N 338 
THR HG23   H N N 339 
THR HXT    H N N 340 
TRP N      N N N 341 
TRP CA     C N S 342 
TRP C      C N N 343 
TRP O      O N N 344 
TRP CB     C N N 345 
TRP CG     C Y N 346 
TRP CD1    C Y N 347 
TRP CD2    C Y N 348 
TRP NE1    N Y N 349 
TRP CE2    C Y N 350 
TRP CE3    C Y N 351 
TRP CZ2    C Y N 352 
TRP CZ3    C Y N 353 
TRP CH2    C Y N 354 
TRP OXT    O N N 355 
TRP H      H N N 356 
TRP H2     H N N 357 
TRP HA     H N N 358 
TRP HB2    H N N 359 
TRP HB3    H N N 360 
TRP HD1    H N N 361 
TRP HE1    H N N 362 
TRP HE3    H N N 363 
TRP HZ2    H N N 364 
TRP HZ3    H N N 365 
TRP HH2    H N N 366 
TRP HXT    H N N 367 
TYR N      N N N 368 
TYR CA     C N S 369 
TYR C      C N N 370 
TYR O      O N N 371 
TYR CB     C N N 372 
TYR CG     C Y N 373 
TYR CD1    C Y N 374 
TYR CD2    C Y N 375 
TYR CE1    C Y N 376 
TYR CE2    C Y N 377 
TYR CZ     C Y N 378 
TYR OH     O N N 379 
TYR OXT    O N N 380 
TYR H      H N N 381 
TYR H2     H N N 382 
TYR HA     H N N 383 
TYR HB2    H N N 384 
TYR HB3    H N N 385 
TYR HD1    H N N 386 
TYR HD2    H N N 387 
TYR HE1    H N N 388 
TYR HE2    H N N 389 
TYR HH     H N N 390 
TYR HXT    H N N 391 
VAL N      N N N 392 
VAL CA     C N S 393 
VAL C      C N N 394 
VAL O      O N N 395 
VAL CB     C N N 396 
VAL CG1    C N N 397 
VAL CG2    C N N 398 
VAL OXT    O N N 399 
VAL H      H N N 400 
VAL H2     H N N 401 
VAL HA     H N N 402 
VAL HB     H N N 403 
VAL HG11   H N N 404 
VAL HG12   H N N 405 
VAL HG13   H N N 406 
VAL HG21   H N N 407 
VAL HG22   H N N 408 
VAL HG23   H N N 409 
VAL HXT    H N N 410 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HC4 C1    O1     doub N N 129 
HC4 C1    O2     sing N N 130 
HC4 C1    C2     sing N N 131 
HC4 O2    HO2    sing N N 132 
HC4 C2    C3     doub N E 133 
HC4 C2    H2     sing N N 134 
HC4 C3    "C1'"  sing N N 135 
HC4 C3    H3     sing N N 136 
HC4 "C1'" "C2'"  doub Y N 137 
HC4 "C1'" "C6'"  sing Y N 138 
HC4 "C2'" "C3'"  sing Y N 139 
HC4 "C2'" "H2'"  sing N N 140 
HC4 "C3'" "C4'"  doub Y N 141 
HC4 "C3'" "H3'"  sing N N 142 
HC4 "C4'" "C5'"  sing Y N 143 
HC4 "C4'" "O4'"  sing N N 144 
HC4 "C5'" "C6'"  doub Y N 145 
HC4 "C5'" "H5'"  sing N N 146 
HC4 "C6'" "H6'"  sing N N 147 
HC4 "O4'" "HO4'" sing N N 148 
HIS N     CA     sing N N 149 
HIS N     H      sing N N 150 
HIS N     H2     sing N N 151 
HIS CA    C      sing N N 152 
HIS CA    CB     sing N N 153 
HIS CA    HA     sing N N 154 
HIS C     O      doub N N 155 
HIS C     OXT    sing N N 156 
HIS CB    CG     sing N N 157 
HIS CB    HB2    sing N N 158 
HIS CB    HB3    sing N N 159 
HIS CG    ND1    sing Y N 160 
HIS CG    CD2    doub Y N 161 
HIS ND1   CE1    doub Y N 162 
HIS ND1   HD1    sing N N 163 
HIS CD2   NE2    sing Y N 164 
HIS CD2   HD2    sing N N 165 
HIS CE1   NE2    sing Y N 166 
HIS CE1   HE1    sing N N 167 
HIS NE2   HE2    sing N N 168 
HIS OXT   HXT    sing N N 169 
HOH O     H1     sing N N 170 
HOH O     H2     sing N N 171 
ILE N     CA     sing N N 172 
ILE N     H      sing N N 173 
ILE N     H2     sing N N 174 
ILE CA    C      sing N N 175 
ILE CA    CB     sing N N 176 
ILE CA    HA     sing N N 177 
ILE C     O      doub N N 178 
ILE C     OXT    sing N N 179 
ILE CB    CG1    sing N N 180 
ILE CB    CG2    sing N N 181 
ILE CB    HB     sing N N 182 
ILE CG1   CD1    sing N N 183 
ILE CG1   HG12   sing N N 184 
ILE CG1   HG13   sing N N 185 
ILE CG2   HG21   sing N N 186 
ILE CG2   HG22   sing N N 187 
ILE CG2   HG23   sing N N 188 
ILE CD1   HD11   sing N N 189 
ILE CD1   HD12   sing N N 190 
ILE CD1   HD13   sing N N 191 
ILE OXT   HXT    sing N N 192 
LEU N     CA     sing N N 193 
LEU N     H      sing N N 194 
LEU N     H2     sing N N 195 
LEU CA    C      sing N N 196 
LEU CA    CB     sing N N 197 
LEU CA    HA     sing N N 198 
LEU C     O      doub N N 199 
LEU C     OXT    sing N N 200 
LEU CB    CG     sing N N 201 
LEU CB    HB2    sing N N 202 
LEU CB    HB3    sing N N 203 
LEU CG    CD1    sing N N 204 
LEU CG    CD2    sing N N 205 
LEU CG    HG     sing N N 206 
LEU CD1   HD11   sing N N 207 
LEU CD1   HD12   sing N N 208 
LEU CD1   HD13   sing N N 209 
LEU CD2   HD21   sing N N 210 
LEU CD2   HD22   sing N N 211 
LEU CD2   HD23   sing N N 212 
LEU OXT   HXT    sing N N 213 
LYS N     CA     sing N N 214 
LYS N     H      sing N N 215 
LYS N     H2     sing N N 216 
LYS CA    C      sing N N 217 
LYS CA    CB     sing N N 218 
LYS CA    HA     sing N N 219 
LYS C     O      doub N N 220 
LYS C     OXT    sing N N 221 
LYS CB    CG     sing N N 222 
LYS CB    HB2    sing N N 223 
LYS CB    HB3    sing N N 224 
LYS CG    CD     sing N N 225 
LYS CG    HG2    sing N N 226 
LYS CG    HG3    sing N N 227 
LYS CD    CE     sing N N 228 
LYS CD    HD2    sing N N 229 
LYS CD    HD3    sing N N 230 
LYS CE    NZ     sing N N 231 
LYS CE    HE2    sing N N 232 
LYS CE    HE3    sing N N 233 
LYS NZ    HZ1    sing N N 234 
LYS NZ    HZ2    sing N N 235 
LYS NZ    HZ3    sing N N 236 
LYS OXT   HXT    sing N N 237 
MET N     CA     sing N N 238 
MET N     H      sing N N 239 
MET N     H2     sing N N 240 
MET CA    C      sing N N 241 
MET CA    CB     sing N N 242 
MET CA    HA     sing N N 243 
MET C     O      doub N N 244 
MET C     OXT    sing N N 245 
MET CB    CG     sing N N 246 
MET CB    HB2    sing N N 247 
MET CB    HB3    sing N N 248 
MET CG    SD     sing N N 249 
MET CG    HG2    sing N N 250 
MET CG    HG3    sing N N 251 
MET SD    CE     sing N N 252 
MET CE    HE1    sing N N 253 
MET CE    HE2    sing N N 254 
MET CE    HE3    sing N N 255 
MET OXT   HXT    sing N N 256 
PHE N     CA     sing N N 257 
PHE N     H      sing N N 258 
PHE N     H2     sing N N 259 
PHE CA    C      sing N N 260 
PHE CA    CB     sing N N 261 
PHE CA    HA     sing N N 262 
PHE C     O      doub N N 263 
PHE C     OXT    sing N N 264 
PHE CB    CG     sing N N 265 
PHE CB    HB2    sing N N 266 
PHE CB    HB3    sing N N 267 
PHE CG    CD1    doub Y N 268 
PHE CG    CD2    sing Y N 269 
PHE CD1   CE1    sing Y N 270 
PHE CD1   HD1    sing N N 271 
PHE CD2   CE2    doub Y N 272 
PHE CD2   HD2    sing N N 273 
PHE CE1   CZ     doub Y N 274 
PHE CE1   HE1    sing N N 275 
PHE CE2   CZ     sing Y N 276 
PHE CE2   HE2    sing N N 277 
PHE CZ    HZ     sing N N 278 
PHE OXT   HXT    sing N N 279 
PRO N     CA     sing N N 280 
PRO N     CD     sing N N 281 
PRO N     H      sing N N 282 
PRO CA    C      sing N N 283 
PRO CA    CB     sing N N 284 
PRO CA    HA     sing N N 285 
PRO C     O      doub N N 286 
PRO C     OXT    sing N N 287 
PRO CB    CG     sing N N 288 
PRO CB    HB2    sing N N 289 
PRO CB    HB3    sing N N 290 
PRO CG    CD     sing N N 291 
PRO CG    HG2    sing N N 292 
PRO CG    HG3    sing N N 293 
PRO CD    HD2    sing N N 294 
PRO CD    HD3    sing N N 295 
PRO OXT   HXT    sing N N 296 
SER N     CA     sing N N 297 
SER N     H      sing N N 298 
SER N     H2     sing N N 299 
SER CA    C      sing N N 300 
SER CA    CB     sing N N 301 
SER CA    HA     sing N N 302 
SER C     O      doub N N 303 
SER C     OXT    sing N N 304 
SER CB    OG     sing N N 305 
SER CB    HB2    sing N N 306 
SER CB    HB3    sing N N 307 
SER OG    HG     sing N N 308 
SER OXT   HXT    sing N N 309 
THR N     CA     sing N N 310 
THR N     H      sing N N 311 
THR N     H2     sing N N 312 
THR CA    C      sing N N 313 
THR CA    CB     sing N N 314 
THR CA    HA     sing N N 315 
THR C     O      doub N N 316 
THR C     OXT    sing N N 317 
THR CB    OG1    sing N N 318 
THR CB    CG2    sing N N 319 
THR CB    HB     sing N N 320 
THR OG1   HG1    sing N N 321 
THR CG2   HG21   sing N N 322 
THR CG2   HG22   sing N N 323 
THR CG2   HG23   sing N N 324 
THR OXT   HXT    sing N N 325 
TRP N     CA     sing N N 326 
TRP N     H      sing N N 327 
TRP N     H2     sing N N 328 
TRP CA    C      sing N N 329 
TRP CA    CB     sing N N 330 
TRP CA    HA     sing N N 331 
TRP C     O      doub N N 332 
TRP C     OXT    sing N N 333 
TRP CB    CG     sing N N 334 
TRP CB    HB2    sing N N 335 
TRP CB    HB3    sing N N 336 
TRP CG    CD1    doub Y N 337 
TRP CG    CD2    sing Y N 338 
TRP CD1   NE1    sing Y N 339 
TRP CD1   HD1    sing N N 340 
TRP CD2   CE2    doub Y N 341 
TRP CD2   CE3    sing Y N 342 
TRP NE1   CE2    sing Y N 343 
TRP NE1   HE1    sing N N 344 
TRP CE2   CZ2    sing Y N 345 
TRP CE3   CZ3    doub Y N 346 
TRP CE3   HE3    sing N N 347 
TRP CZ2   CH2    doub Y N 348 
TRP CZ2   HZ2    sing N N 349 
TRP CZ3   CH2    sing Y N 350 
TRP CZ3   HZ3    sing N N 351 
TRP CH2   HH2    sing N N 352 
TRP OXT   HXT    sing N N 353 
TYR N     CA     sing N N 354 
TYR N     H      sing N N 355 
TYR N     H2     sing N N 356 
TYR CA    C      sing N N 357 
TYR CA    CB     sing N N 358 
TYR CA    HA     sing N N 359 
TYR C     O      doub N N 360 
TYR C     OXT    sing N N 361 
TYR CB    CG     sing N N 362 
TYR CB    HB2    sing N N 363 
TYR CB    HB3    sing N N 364 
TYR CG    CD1    doub Y N 365 
TYR CG    CD2    sing Y N 366 
TYR CD1   CE1    sing Y N 367 
TYR CD1   HD1    sing N N 368 
TYR CD2   CE2    doub Y N 369 
TYR CD2   HD2    sing N N 370 
TYR CE1   CZ     doub Y N 371 
TYR CE1   HE1    sing N N 372 
TYR CE2   CZ     sing Y N 373 
TYR CE2   HE2    sing N N 374 
TYR CZ    OH     sing N N 375 
TYR OH    HH     sing N N 376 
TYR OXT   HXT    sing N N 377 
VAL N     CA     sing N N 378 
VAL N     H      sing N N 379 
VAL N     H2     sing N N 380 
VAL CA    C      sing N N 381 
VAL CA    CB     sing N N 382 
VAL CA    HA     sing N N 383 
VAL C     O      doub N N 384 
VAL C     OXT    sing N N 385 
VAL CB    CG1    sing N N 386 
VAL CB    CG2    sing N N 387 
VAL CB    HB     sing N N 388 
VAL CG1   HG11   sing N N 389 
VAL CG1   HG12   sing N N 390 
VAL CG1   HG13   sing N N 391 
VAL CG2   HG21   sing N N 392 
VAL CG2   HG22   sing N N 393 
VAL CG2   HG23   sing N N 394 
VAL OXT   HXT    sing N N 395 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' 1231306 1 
'National Science Foundation (NSF, United States)' 'United States' 2423601 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4wla 
_pdbx_initial_refinement_model.details          'model from XFEL data' 
# 
_pdbx_serial_crystallography_data_reduction.diffrn_id             1 
_pdbx_serial_crystallography_data_reduction.frames_total          ? 
_pdbx_serial_crystallography_data_reduction.xfel_pulse_events     ? 
_pdbx_serial_crystallography_data_reduction.frame_hits            ? 
_pdbx_serial_crystallography_data_reduction.crystal_hits          36668 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        ? 
_pdbx_serial_crystallography_data_reduction.lattices_indexed      37078 
_pdbx_serial_crystallography_data_reduction.xfel_run_numbers      ? 
_pdbx_serial_crystallography_data_reduction.lattices_merged       ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               ? 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   ? 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          ? 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  4 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              ? 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   'fixed target scan' 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_space_group.name_H-M_alt     'P 65' 
_space_group.name_Hall        'P 65' 
_space_group.IT_number        170 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9D10 
_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]   0.024178 
_atom_sites.fract_transf_matrix[1][2]   0.013959 
_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]   0.027918 
_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]   0.008413 
_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.
;
? 
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   ? 31.46818 -1.41719  -16.08698 1.000 71.47344 ? 1   MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? 30.19481 -2.12368  -16.19109 1.000 68.15734 ? 1   MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? 30.25036 -3.31238  -17.16642 1.000 70.26454 ? 1   MET A C     1 
ATOM   4    O O     . MET A 1 1   ? 30.97519 -3.27712  -18.16838 1.000 70.88347 ? 1   MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? 29.09372 -1.14782  -16.60674 1.000 67.98010 ? 1   MET A CB    1 
ATOM   6    C CG    . MET A 1 1   ? 27.77009 -1.81556  -16.94789 1.000 71.45914 ? 1   MET A CG    1 
ATOM   7    S SD    . MET A 1 1   ? 26.31678 -0.83743  -16.52151 1.000 81.55059 ? 1   MET A SD    1 
ATOM   8    C CE    . MET A 1 1   ? 25.23342 -1.25749  -17.89027 1.000 57.09313 ? 1   MET A CE    1 
ATOM   9    N N     . GLU A 1 2   ? 29.48585 -4.36244  -16.84462 1.000 61.21025 ? 2   GLU A N     1 
ATOM   10   C CA    . GLU A 1 2   ? 29.41882 -5.59368  -17.63109 1.000 62.95730 ? 2   GLU A CA    1 
ATOM   11   C C     . GLU A 1 2   ? 28.33347 -5.48821  -18.70118 1.000 57.28074 ? 2   GLU A C     1 
ATOM   12   O O     . GLU A 1 2   ? 27.20413 -5.08861  -18.40135 1.000 54.51605 ? 2   GLU A O     1 
ATOM   13   C CB    . GLU A 1 2   ? 29.13141 -6.78697  -16.70980 1.000 59.44926 ? 2   GLU A CB    1 
ATOM   14   C CG    . GLU A 1 2   ? 30.21563 -7.06094  -15.67330 1.000 50.47366 ? 2   GLU A CG    1 
ATOM   15   C CD    . GLU A 1 2   ? 31.50939 -7.54632  -16.31474 1.000 71.88808 ? 2   GLU A CD    1 
ATOM   16   O OE1   . GLU A 1 2   ? 31.45627 -8.48021  -17.15307 1.000 67.51721 ? 2   GLU A OE1   1 
ATOM   17   O OE2   . GLU A 1 2   ? 32.57509 -6.97679  -15.99510 1.000 73.04457 ? 2   GLU A OE2   1 
ATOM   18   N N     . HIS A 1 3   ? 28.66304 -5.86717  -19.94236 1.000 51.91697 ? 3   HIS A N     1 
ATOM   19   C CA    . HIS A 1 3   ? 27.70464 -5.75800  -21.05019 1.000 54.24702 ? 3   HIS A CA    1 
ATOM   20   C C     . HIS A 1 3   ? 26.97304 -7.09066  -21.23865 1.000 50.02014 ? 3   HIS A C     1 
ATOM   21   O O     . HIS A 1 3   ? 27.33211 -7.92840  -22.06886 1.000 51.90163 ? 3   HIS A O     1 
ATOM   22   C CB    . HIS A 1 3   ? 28.40073 -5.33145  -22.33912 1.000 60.67007 ? 3   HIS A CB    1 
ATOM   23   C CG    . HIS A 1 3   ? 29.25206 -4.10551  -22.20703 1.000 75.67101 ? 3   HIS A CG    1 
ATOM   24   N ND1   . HIS A 1 3   ? 28.73978 -2.86871  -21.87211 1.000 73.71562 ? 3   HIS A ND1   1 
ATOM   25   C CD2   . HIS A 1 3   ? 30.58208 -3.92378  -22.39880 1.000 76.24660 ? 3   HIS A CD2   1 
ATOM   26   C CE1   . HIS A 1 3   ? 29.72186 -1.98216  -21.84686 1.000 72.01032 ? 3   HIS A CE1   1 
ATOM   27   N NE2   . HIS A 1 3   ? 30.84856 -2.59585  -22.16427 1.000 79.04358 ? 3   HIS A NE2   1 
ATOM   28   N N     . VAL A 1 4   ? 25.92512 -7.29263  -20.44315 1.000 35.36925 ? 4   VAL A N     1 
ATOM   29   C CA    . VAL A 1 4   ? 24.99188 -8.39624  -20.64249 1.000 33.30081 ? 4   VAL A CA    1 
ATOM   30   C C     . VAL A 1 4   ? 23.58815 -7.83739  -20.47519 1.000 42.61247 ? 4   VAL A C     1 
ATOM   31   O O     . VAL A 1 4   ? 23.32328 -7.08038  -19.53447 1.000 35.73249 ? 4   VAL A O     1 
ATOM   32   C CB    A VAL A 1 4   ? 25.26402 -9.58028  -19.69069 0.450 38.18581 ? 4   VAL A CB    1 
ATOM   33   C CB    B VAL A 1 4   ? 25.21696 -9.55028  -19.64300 0.550 38.19648 ? 4   VAL A CB    1 
ATOM   34   C CG1   A VAL A 1 4   ? 26.27499 -9.19877  -18.64272 0.450 37.31436 ? 4   VAL A CG1   1 
ATOM   35   C CG1   B VAL A 1 4   ? 24.60325 -10.84928 -20.17549 0.550 39.24784 ? 4   VAL A CG1   1 
ATOM   36   C CG2   A VAL A 1 4   ? 23.98242 -10.09962 -19.06252 0.450 32.84041 ? 4   VAL A CG2   1 
ATOM   37   C CG2   B VAL A 1 4   ? 26.69291 -9.73207  -19.33268 0.550 38.53509 ? 4   VAL A CG2   1 
ATOM   38   N N     . ALA A 1 5   ? 22.69964 -8.16880  -21.40526 1.000 35.15609 ? 5   ALA A N     1 
ATOM   39   C CA    . ALA A 1 5   ? 21.36485 -7.59429  -21.40496 1.000 32.28689 ? 5   ALA A CA    1 
ATOM   40   C C     . ALA A 1 5   ? 20.40930 -8.48477  -20.62387 1.000 33.91285 ? 5   ALA A C     1 
ATOM   41   O O     . ALA A 1 5   ? 20.47208 -9.71738  -20.70337 1.000 33.72005 ? 5   ALA A O     1 
ATOM   42   C CB    . ALA A 1 5   ? 20.85922 -7.38723  -22.83528 1.000 31.60309 ? 5   ALA A CB    1 
ATOM   43   N N     . PHE A 1 6   ? 19.54488 -7.84805  -19.83903 1.000 29.78457 ? 6   PHE A N     1 
ATOM   44   C CA    . PHE A 1 6   ? 18.47812 -8.56418  -19.15257 1.000 30.64973 ? 6   PHE A CA    1 
ATOM   45   C C     . PHE A 1 6   ? 17.69144 -9.40312  -20.15494 1.000 32.28308 ? 6   PHE A C     1 
ATOM   46   O O     . PHE A 1 6   ? 17.26375 -8.89941  -21.19869 1.000 33.93335 ? 6   PHE A O     1 
ATOM   47   C CB    . PHE A 1 6   ? 17.56279 -7.55690  -18.45481 1.000 27.77576 ? 6   PHE A CB    1 
ATOM   48   C CG    . PHE A 1 6   ? 16.43753 -8.18511  -17.67366 1.000 30.19602 ? 6   PHE A CG    1 
ATOM   49   C CD1   . PHE A 1 6   ? 15.21842 -8.46825  -18.28726 1.000 35.74316 ? 6   PHE A CD1   1 
ATOM   50   C CD2   . PHE A 1 6   ? 16.58364 -8.46747  -16.32175 1.000 33.11076 ? 6   PHE A CD2   1 
ATOM   51   C CE1   . PHE A 1 6   ? 14.17853 -9.04128  -17.57542 1.000 32.84560 ? 6   PHE A CE1   1 
ATOM   52   C CE2   . PHE A 1 6   ? 15.53390 -9.04157  -15.59471 1.000 26.71400 ? 6   PHE A CE2   1 
ATOM   53   C CZ    . PHE A 1 6   ? 14.33486 -9.32746  -16.23160 1.000 27.25488 ? 6   PHE A CZ    1 
ATOM   54   N N     . GLY A 1 7   ? 17.53175 -10.69050 -19.85607 1.000 33.19223 ? 7   GLY A N     1 
ATOM   55   C CA    . GLY A 1 7   ? 16.72048 -11.55254 -20.69901 1.000 30.57014 ? 7   GLY A CA    1 
ATOM   56   C C     . GLY A 1 7   ? 17.43411 -12.20021 -21.86487 1.000 36.41088 ? 7   GLY A C     1 
ATOM   57   O O     . GLY A 1 7   ? 16.77236 -12.85578 -22.68679 1.000 34.84398 ? 7   GLY A O     1 
ATOM   58   N N     . SER A 1 8   ? 18.75533 -12.03583 -21.97050 1.000 31.23428 ? 8   SER A N     1 
ATOM   59   C CA    . SER A 1 8   ? 19.52701 -12.69159 -23.01915 1.000 35.12544 ? 8   SER A CA    1 
ATOM   60   C C     . SER A 1 8   ? 19.38183 -14.21236 -22.95231 1.000 32.54453 ? 8   SER A C     1 
ATOM   61   O O     . SER A 1 8   ? 19.38170 -14.80896 -21.87282 1.000 31.07897 ? 8   SER A O     1 
ATOM   62   C CB    . SER A 1 8   ? 20.99588 -12.30446 -22.88994 1.000 40.36480 ? 8   SER A CB    1 
ATOM   63   O OG    . SER A 1 8   ? 21.17152 -10.94563 -23.21777 1.000 46.88865 ? 8   SER A OG    1 
ATOM   64   N N     . GLU A 1 9   ? 19.27901 -14.85132 -24.12047 1.000 39.94615 ? 9   GLU A N     1 
ATOM   65   C CA    . GLU A 1 9   ? 18.97681 -16.27985 -24.11541 1.000 47.40609 ? 9   GLU A CA    1 
ATOM   66   C C     . GLU A 1 9   ? 20.14220 -17.12396 -23.61341 1.000 36.30849 ? 9   GLU A C     1 
ATOM   67   O O     . GLU A 1 9   ? 19.91229 -18.23168 -23.11404 1.000 43.56172 ? 9   GLU A O     1 
ATOM   68   C CB    . GLU A 1 9   ? 18.54060 -16.74002 -25.50526 1.000 50.20776 ? 9   GLU A CB    1 
ATOM   69   C CG    . GLU A 1 9   ? 19.46437 -16.33229 -26.62500 1.000 55.90601 ? 9   GLU A CG    1 
ATOM   70   C CD    . GLU A 1 9   ? 18.69917 -16.11541 -27.91783 1.000 79.44297 ? 9   GLU A CD    1 
ATOM   71   O OE1   . GLU A 1 9   ? 17.44990 -16.19899 -27.87062 1.000 84.72020 ? 9   GLU A OE1   1 
ATOM   72   O OE2   . GLU A 1 9   ? 19.33321 -15.85888 -28.96865 1.000 74.76580 ? 9   GLU A OE2   1 
ATOM   73   N N     . ASP A 1 10  ? 21.37583 -16.62467 -23.69953 1.000 38.14886 ? 10  ASP A N     1 
ATOM   74   C CA    . ASP A 1 10  ? 22.52939 -17.34919 -23.17893 1.000 40.23032 ? 10  ASP A CA    1 
ATOM   75   C C     . ASP A 1 10  ? 23.02956 -16.78031 -21.84904 1.000 35.90126 ? 10  ASP A C     1 
ATOM   76   O O     . ASP A 1 10  ? 24.19633 -16.98282 -21.50545 1.000 34.56569 ? 10  ASP A O     1 
ATOM   77   C CB    A ASP A 1 10  ? 23.65889 -17.37757 -24.21424 0.250 41.63157 ? 10  ASP A CB    1 
ATOM   78   C CB    B ASP A 1 10  ? 23.66211 -17.33485 -24.20941 0.750 41.63111 ? 10  ASP A CB    1 
ATOM   79   C CG    A ASP A 1 10  ? 23.86259 -18.76549 -24.82709 0.250 43.38454 ? 10  ASP A CG    1 
ATOM   80   C CG    B ASP A 1 10  ? 24.13119 -15.92294 -24.55032 0.750 45.09842 ? 10  ASP A CG    1 
ATOM   81   O OD1   A ASP A 1 10  ? 23.04501 -19.67082 -24.54254 0.250 43.90356 ? 10  ASP A OD1   1 
ATOM   82   O OD1   B ASP A 1 10  ? 23.45440 -14.95068 -24.15246 0.750 41.30659 ? 10  ASP A OD1   1 
ATOM   83   O OD2   A ASP A 1 10  ? 24.84467 -18.95528 -25.58562 0.250 37.76377 ? 10  ASP A OD2   1 
ATOM   84   O OD2   B ASP A 1 10  ? 25.17906 -15.78008 -25.21563 0.750 43.07877 ? 10  ASP A OD2   1 
ATOM   85   N N     . ILE A 1 11  ? 22.17070 -16.09040 -21.09140 1.000 31.74899 ? 11  ILE A N     1 
ATOM   86   C CA    . ILE A 1 11  ? 22.62668 -15.33072 -19.92332 1.000 32.82620 ? 11  ILE A CA    1 
ATOM   87   C C     . ILE A 1 11  ? 23.36746 -16.22668 -18.92676 1.000 39.83243 ? 11  ILE A C     1 
ATOM   88   O O     . ILE A 1 11  ? 24.35503 -15.80544 -18.30699 1.000 34.93376 ? 11  ILE A O     1 
ATOM   89   C CB    . ILE A 1 11  ? 21.43953 -14.59005 -19.26774 1.000 31.88104 ? 11  ILE A CB    1 
ATOM   90   C CG1   . ILE A 1 11  ? 21.95069 -13.58182 -18.23111 1.000 34.10810 ? 11  ILE A CG1   1 
ATOM   91   C CG2   . ILE A 1 11  ? 20.44450 -15.54465 -18.63029 1.000 26.70640 ? 11  ILE A CG2   1 
ATOM   92   C CD1   . ILE A 1 11  ? 20.89496 -12.61359 -17.76820 1.000 38.67807 ? 11  ILE A CD1   1 
ATOM   93   N N     . GLU A 1 12  ? 22.92064 -17.47717 -18.76696 1.000 39.65576 ? 12  GLU A N     1 
ATOM   94   C CA    . GLU A 1 12  ? 23.54559 -18.35755 -17.78555 1.000 33.22297 ? 12  GLU A CA    1 
ATOM   95   C C     . GLU A 1 12  ? 24.94299 -18.79371 -18.20683 1.000 35.85485 ? 12  GLU A C     1 
ATOM   96   O O     . GLU A 1 12  ? 25.74740 -19.15219 -17.34001 1.000 34.83674 ? 12  GLU A O     1 
ATOM   97   C CB    . GLU A 1 12  ? 22.67579 -19.59211 -17.54093 1.000 32.87021 ? 12  GLU A CB    1 
ATOM   98   C CG    . GLU A 1 12  ? 22.69686 -20.60789 -18.67716 1.000 37.56656 ? 12  GLU A CG    1 
ATOM   99   C CD    . GLU A 1 12  ? 21.68098 -20.30321 -19.77427 1.000 40.18965 ? 12  GLU A CD    1 
ATOM   100  O OE1   . GLU A 1 12  ? 21.23158 -19.13583 -19.90637 1.000 34.59803 ? 12  GLU A OE1   1 
ATOM   101  O OE2   . GLU A 1 12  ? 21.31334 -21.25196 -20.49612 1.000 41.00198 ? 12  GLU A OE2   1 
ATOM   102  N N     . ASN A 1 13  ? 25.23826 -18.80558 -19.51405 1.000 30.54277 ? 13  ASN A N     1 
ATOM   103  C CA    . ASN A 1 13  ? 26.60874 -19.02337 -19.96139 1.000 32.44079 ? 13  ASN A CA    1 
ATOM   104  C C     . ASN A 1 13  ? 27.50767 -17.86730 -19.53966 1.000 38.06821 ? 13  ASN A C     1 
ATOM   105  O O     . ASN A 1 13  ? 28.62851 -18.07632 -19.05821 1.000 39.27859 ? 13  ASN A O     1 
ATOM   106  C CB    . ASN A 1 13  ? 26.64785 -19.18910 -21.48371 1.000 38.20381 ? 13  ASN A CB    1 
ATOM   107  C CG    . ASN A 1 13  ? 26.39051 -20.62112 -21.93120 1.000 55.97678 ? 13  ASN A CG    1 
ATOM   108  O OD1   . ASN A 1 13  ? 27.28204 -21.27367 -22.47615 1.000 46.61673 ? 13  ASN A OD1   1 
ATOM   109  N ND2   . ASN A 1 13  ? 25.16522 -21.11336 -21.71223 1.000 48.78654 ? 13  ASN A ND2   1 
ATOM   110  N N     . THR A 1 14  ? 27.03749 -16.63914 -19.72820 1.000 31.75995 ? 14  THR A N     1 
ATOM   111  C CA    . THR A 1 14  ? 27.87678 -15.48358 -19.44178 1.000 35.55572 ? 14  THR A CA    1 
ATOM   112  C C     . THR A 1 14  ? 28.13985 -15.34713 -17.94735 1.000 42.02447 ? 14  THR A C     1 
ATOM   113  O O     . THR A 1 14  ? 29.28400 -15.11874 -17.53031 1.000 40.11496 ? 14  THR A O     1 
ATOM   114  C CB    . THR A 1 14  ? 27.21698 -14.22640 -19.99846 1.000 38.78798 ? 14  THR A CB    1 
ATOM   115  O OG1   . THR A 1 14  ? 27.06161 -14.38752 -21.41206 1.000 42.68807 ? 14  THR A OG1   1 
ATOM   116  C CG2   . THR A 1 14  ? 28.07701 -13.00171 -19.71817 1.000 40.40673 ? 14  THR A CG2   1 
ATOM   117  N N     . LEU A 1 15  ? 27.09885 -15.50412 -17.12379 1.000 33.78322 ? 15  LEU A N     1 
ATOM   118  C CA    . LEU A 1 15  ? 27.27242 -15.37350 -15.68135 1.000 33.49670 ? 15  LEU A CA    1 
ATOM   119  C C     . LEU A 1 15  ? 28.06566 -16.52437 -15.06819 1.000 34.78491 ? 15  LEU A C     1 
ATOM   120  O O     . LEU A 1 15  ? 28.63567 -16.35190 -13.98861 1.000 38.01820 ? 15  LEU A O     1 
ATOM   121  C CB    . LEU A 1 15  ? 25.91619 -15.26825 -14.99186 1.000 32.15960 ? 15  LEU A CB    1 
ATOM   122  C CG    . LEU A 1 15  ? 25.03021 -14.08352 -15.35878 1.000 35.47460 ? 15  LEU A CG    1 
ATOM   123  C CD1   . LEU A 1 15  ? 24.08166 -13.80379 -14.21782 1.000 31.35365 ? 15  LEU A CD1   1 
ATOM   124  C CD2   . LEU A 1 15  ? 25.83516 -12.83845 -15.69872 1.000 35.79650 ? 15  LEU A CD2   1 
ATOM   125  N N     . ALA A 1 16  ? 28.11151 -17.69610 -15.70802 1.000 34.17477 ? 16  ALA A N     1 
ATOM   126  C CA    . ALA A 1 16  ? 28.92491 -18.77307 -15.15756 1.000 34.47952 ? 16  ALA A CA    1 
ATOM   127  C C     . ALA A 1 16  ? 30.40067 -18.39302 -15.08170 1.000 40.49960 ? 16  ALA A C     1 
ATOM   128  O O     . ALA A 1 16  ? 31.13685 -18.95302 -14.26153 1.000 46.76878 ? 16  ALA A O     1 
ATOM   129  C CB    . ALA A 1 16  ? 28.75559 -20.04932 -15.98755 1.000 33.15902 ? 16  ALA A CB    1 
ATOM   130  N N     . LYS A 1 17  ? 30.84595 -17.45033 -15.90589 1.000 38.29730 ? 17  LYS A N     1 
ATOM   131  C CA    . LYS A 1 17  ? 32.25210 -17.08687 -15.99939 1.000 41.04463 ? 17  LYS A CA    1 
ATOM   132  C C     . LYS A 1 17  ? 32.64150 -15.93828 -15.07493 1.000 46.31832 ? 17  LYS A C     1 
ATOM   133  O O     . LYS A 1 17  ? 33.80906 -15.53210 -15.08596 1.000 47.82964 ? 17  LYS A O     1 
ATOM   134  C CB    . LYS A 1 17  ? 32.59479 -16.71882 -17.45104 1.000 45.17079 ? 17  LYS A CB    1 
ATOM   135  C CG    . LYS A 1 17  ? 32.33528 -17.84460 -18.44678 1.000 41.17610 ? 17  LYS A CG    1 
ATOM   136  C CD    . LYS A 1 17  ? 32.76221 -17.47650 -19.85401 1.000 35.17445 ? 17  LYS A CD    1 
ATOM   137  C CE    . LYS A 1 17  ? 31.73624 -16.60134 -20.53086 1.000 45.08754 ? 17  LYS A CE    1 
ATOM   138  N NZ    . LYS A 1 17  ? 32.21820 -16.18630 -21.87542 1.000 47.96531 ? 17  LYS A NZ    1 
ATOM   139  N N     . MET A 1 18  ? 31.70857 -15.42331 -14.26862 1.000 45.72353 ? 18  MET A N     1 
ATOM   140  C CA    . MET A 1 18  ? 31.91722 -14.21374 -13.47911 1.000 48.99761 ? 18  MET A CA    1 
ATOM   141  C C     . MET A 1 18  ? 32.16484 -14.52247 -12.00669 1.000 53.37483 ? 18  MET A C     1 
ATOM   142  O O     . MET A 1 18  ? 31.55130 -15.43082 -11.43673 1.000 53.38063 ? 18  MET A O     1 
ATOM   143  C CB    . MET A 1 18  ? 30.71117 -13.27968 -13.59616 1.000 44.59770 ? 18  MET A CB    1 
ATOM   144  C CG    . MET A 1 18  ? 30.55527 -12.67809 -14.97344 1.000 45.32605 ? 18  MET A CG    1 
ATOM   145  S SD    . MET A 1 18  ? 29.14637 -11.56262 -15.08802 1.000 48.74167 ? 18  MET A SD    1 
ATOM   146  C CE    . MET A 1 18  ? 29.46240 -10.86167 -16.71107 1.000 50.07419 ? 18  MET A CE    1 
ATOM   147  N N     . ASP A 1 19  ? 33.05187 -13.73500 -11.39078 1.000 53.97954 ? 19  ASP A N     1 
ATOM   148  C CA    . ASP A 1 19  ? 33.25564 -13.75132 -9.94932  1.000 60.12375 ? 19  ASP A CA    1 
ATOM   149  C C     . ASP A 1 19  ? 32.33682 -12.73453 -9.26402  1.000 61.02825 ? 19  ASP A C     1 
ATOM   150  O O     . ASP A 1 19  ? 31.55671 -12.02406 -9.90670  1.000 50.65841 ? 19  ASP A O     1 
ATOM   151  C CB    . ASP A 1 19  ? 34.72088 -13.47452 -9.60735  1.000 57.04215 ? 19  ASP A CB    1 
ATOM   152  C CG    . ASP A 1 19  ? 35.21175 -12.13111 -10.13871 1.000 61.34824 ? 19  ASP A CG    1 
ATOM   153  O OD1   . ASP A 1 19  ? 34.41230 -11.36298 -10.71762 1.000 60.57907 ? 19  ASP A OD1   1 
ATOM   154  O OD2   . ASP A 1 19  ? 36.41643 -11.84263 -9.98172  1.000 67.09912 ? 19  ASP A OD2   1 
ATOM   155  N N     . ASP A 1 20  ? 32.44894 -12.66432 -7.93232  1.000 64.89646 ? 20  ASP A N     1 
ATOM   156  C CA    . ASP A 1 20  ? 31.63212 -11.75284 -7.13463  1.000 56.71470 ? 20  ASP A CA    1 
ATOM   157  C C     . ASP A 1 20  ? 31.74276 -10.31890 -7.62753  1.000 51.31129 ? 20  ASP A C     1 
ATOM   158  O O     . ASP A 1 20  ? 30.73379 -9.60970  -7.74120  1.000 52.60026 ? 20  ASP A O     1 
ATOM   159  C CB    . ASP A 1 20  ? 32.05693 -11.83805 -5.66891  1.000 70.20819 ? 20  ASP A CB    1 
ATOM   160  C CG    . ASP A 1 20  ? 31.43078 -13.00947 -4.95240  1.000 77.02601 ? 20  ASP A CG    1 
ATOM   161  O OD1   . ASP A 1 20  ? 30.44765 -12.78587 -4.21273  1.000 83.33464 ? 20  ASP A OD1   1 
ATOM   162  O OD2   . ASP A 1 20  ? 31.90263 -14.15440 -5.14691  1.000 82.04428 ? 20  ASP A OD2   1 
ATOM   163  N N     . GLY A 1 21  ? 32.96428 -9.87497  -7.92269  1.000 56.21727 ? 21  GLY A N     1 
ATOM   164  C CA    . GLY A 1 21  ? 33.14816 -8.51777  -8.40728  1.000 51.57415 ? 21  GLY A CA    1 
ATOM   165  C C     . GLY A 1 21  ? 32.33650 -8.22705  -9.65573  1.000 53.64103 ? 21  GLY A C     1 
ATOM   166  O O     . GLY A 1 21  ? 31.64578 -7.20902  -9.73615  1.000 49.62706 ? 21  GLY A O     1 
ATOM   167  N N     . GLN A 1 22  ? 32.38754 -9.13621  -10.63936 1.000 54.19044 ? 22  GLN A N     1 
ATOM   168  C CA    . GLN A 1 22  ? 31.74514 -8.87673  -11.92864 1.000 46.13783 ? 22  GLN A CA    1 
ATOM   169  C C     . GLN A 1 22  ? 30.22394 -8.86871  -11.82715 1.000 41.45526 ? 22  GLN A C     1 
ATOM   170  O O     . GLN A 1 22  ? 29.57157 -8.11863  -12.56226 1.000 39.33461 ? 22  GLN A O     1 
ATOM   171  C CB    . GLN A 1 22  ? 32.19189 -9.90699  -12.96763 1.000 46.81570 ? 22  GLN A CB    1 
ATOM   172  C CG    . GLN A 1 22  ? 33.63312 -9.75431  -13.43049 1.000 51.55274 ? 22  GLN A CG    1 
ATOM   173  C CD    . GLN A 1 22  ? 34.11193 -10.94280 -14.24523 1.000 57.58000 ? 22  GLN A CD    1 
ATOM   174  O OE1   . GLN A 1 22  ? 34.30777 -12.04277 -13.71367 1.000 53.87988 ? 22  GLN A OE1   1 
ATOM   175  N NE2   . GLN A 1 22  ? 34.30174 -10.72866 -15.54354 1.000 61.13289 ? 22  GLN A NE2   1 
ATOM   176  N N     . LEU A 1 23  ? 29.64287 -9.69951  -10.94931 1.000 37.11255 ? 23  LEU A N     1 
ATOM   177  C CA    . LEU A 1 23  ? 28.19643 -9.66441  -10.73888 1.000 34.44388 ? 23  LEU A CA    1 
ATOM   178  C C     . LEU A 1 23  ? 27.72807 -8.27306  -10.34287 1.000 33.60000 ? 23  LEU A C     1 
ATOM   179  O O     . LEU A 1 23  ? 26.64232 -7.83674  -10.73933 1.000 32.04998 ? 23  LEU A O     1 
ATOM   180  C CB    . LEU A 1 23  ? 27.78359 -10.66169 -9.66103  1.000 34.14398 ? 23  LEU A CB    1 
ATOM   181  C CG    . LEU A 1 23  ? 27.60045 -12.12294 -10.04761 1.000 48.10253 ? 23  LEU A CG    1 
ATOM   182  C CD1   . LEU A 1 23  ? 26.65024 -12.78929 -9.04818  1.000 52.71369 ? 23  LEU A CD1   1 
ATOM   183  C CD2   . LEU A 1 23  ? 27.09805 -12.25930 -11.47959 1.000 39.35132 ? 23  LEU A CD2   1 
ATOM   184  N N     . ASP A 1 24  ? 28.53280 -7.56255  -9.55450  1.000 36.98583 ? 24  ASP A N     1 
ATOM   185  C CA    . ASP A 1 24  ? 28.15533 -6.22724  -9.11640  1.000 38.97702 ? 24  ASP A CA    1 
ATOM   186  C C     . ASP A 1 24  ? 28.15865 -5.21158  -10.24601 1.000 36.48303 ? 24  ASP A C     1 
ATOM   187  O O     . ASP A 1 24  ? 27.61966 -4.11989  -10.05970 1.000 37.40455 ? 24  ASP A O     1 
ATOM   188  C CB    . ASP A 1 24  ? 29.08807 -5.76913  -7.99094  1.000 34.35463 ? 24  ASP A CB    1 
ATOM   189  C CG    . ASP A 1 24  ? 28.76560 -6.43949  -6.67716  1.000 42.41154 ? 24  ASP A CG    1 
ATOM   190  O OD1   . ASP A 1 24  ? 27.71639 -7.11427  -6.60611  1.000 34.48457 ? 24  ASP A OD1   1 
ATOM   191  O OD2   . ASP A 1 24  ? 29.55972 -6.30145  -5.72389  1.000 38.96376 ? 24  ASP A OD2   1 
ATOM   192  N N     . GLY A 1 25  ? 28.75216 -5.53897  -11.39498 1.000 33.14069 ? 25  GLY A N     1 
ATOM   193  C CA    . GLY A 1 25  ? 28.74615 -4.65660  -12.55076 1.000 34.70966 ? 25  GLY A CA    1 
ATOM   194  C C     . GLY A 1 25  ? 27.54202 -4.77489  -13.47064 1.000 34.91719 ? 25  GLY A C     1 
ATOM   195  O O     . GLY A 1 25  ? 27.43807 -4.00214  -14.42496 1.000 37.59612 ? 25  GLY A O     1 
ATOM   196  N N     . LEU A 1 26  ? 26.63167 -5.70841  -13.21043 1.000 31.22640 ? 26  LEU A N     1 
ATOM   197  C CA    . LEU A 1 26  ? 25.46587 -5.88222  -14.06799 1.000 30.19410 ? 26  LEU A CA    1 
ATOM   198  C C     . LEU A 1 26  ? 24.50847 -4.69061  -13.97851 1.000 33.48469 ? 26  LEU A C     1 
ATOM   199  O O     . LEU A 1 26  ? 24.39400 -4.01675  -12.94803 1.000 32.25461 ? 26  LEU A O     1 
ATOM   200  C CB    . LEU A 1 26  ? 24.72339 -7.16642  -13.69358 1.000 29.55424 ? 26  LEU A CB    1 
ATOM   201  C CG    . LEU A 1 26  ? 25.56055 -8.42623  -13.90400 1.000 32.05260 ? 26  LEU A CG    1 
ATOM   202  C CD1   . LEU A 1 26  ? 24.79797 -9.66274  -13.46665 1.000 34.02528 ? 26  LEU A CD1   1 
ATOM   203  C CD2   . LEU A 1 26  ? 25.92040 -8.52276  -15.34745 1.000 30.08408 ? 26  LEU A CD2   1 
ATOM   204  N N     . ALA A 1 27  ? 23.79235 -4.45137  -15.07392 1.000 26.01619 ? 27  ALA A N     1 
ATOM   205  C CA    . ALA A 1 27  ? 22.79229 -3.39134  -15.11651 1.000 25.41977 ? 27  ALA A CA    1 
ATOM   206  C C     . ALA A 1 27  ? 21.49912 -3.74891  -14.38132 1.000 30.52644 ? 27  ALA A C     1 
ATOM   207  O O     . ALA A 1 27  ? 20.60620 -2.89868  -14.28649 1.000 35.56948 ? 27  ALA A O     1 
ATOM   208  C CB    . ALA A 1 27  ? 22.47258 -3.03511  -16.57073 1.000 28.92581 ? 27  ALA A CB    1 
ATOM   209  N N     . PHE A 1 28  ? 21.37170 -4.96240  -13.85156 1.000 27.50795 ? 28  PHE A N     1 
ATOM   210  C CA    . PHE A 1 28  ? 20.11258 -5.43329  -13.28209 1.000 25.29804 ? 28  PHE A CA    1 
ATOM   211  C C     . PHE A 1 28  ? 20.40510 -6.26156  -12.03608 1.000 25.67850 ? 28  PHE A C     1 
ATOM   212  O O     . PHE A 1 28  ? 21.53940 -6.69097  -11.80758 1.000 28.43961 ? 28  PHE A O     1 
ATOM   213  C CB    . PHE A 1 28  ? 19.32651 -6.25726  -14.31075 1.000 24.96196 ? 28  PHE A CB    1 
ATOM   214  C CG    . PHE A 1 28  ? 20.14325 -7.33652  -14.97633 1.000 31.52066 ? 28  PHE A CG    1 
ATOM   215  C CD1   . PHE A 1 28  ? 20.24749 -8.59809  -14.40654 1.000 31.98904 ? 28  PHE A CD1   1 
ATOM   216  C CD2   . PHE A 1 28  ? 20.81230 -7.08986  -16.17167 1.000 29.14156 ? 28  PHE A CD2   1 
ATOM   217  C CE1   . PHE A 1 28  ? 21.01373 -9.60522  -15.00787 1.000 29.16214 ? 28  PHE A CE1   1 
ATOM   218  C CE2   . PHE A 1 28  ? 21.57548 -8.09051  -16.78188 1.000 31.10768 ? 28  PHE A CE2   1 
ATOM   219  C CZ    . PHE A 1 28  ? 21.67316 -9.34746  -16.19862 1.000 30.26098 ? 28  PHE A CZ    1 
ATOM   220  N N     . GLY A 1 29  ? 19.37391 -6.49382  -11.22647 1.000 22.87018 ? 29  GLY A N     1 
ATOM   221  C CA    . GLY A 1 29  ? 19.55526 -7.32753  -10.03712 1.000 24.76859 ? 29  GLY A CA    1 
ATOM   222  C C     . GLY A 1 29  ? 19.80439 -8.78754  -10.40351 1.000 27.49762 ? 29  GLY A C     1 
ATOM   223  O O     . GLY A 1 29  ? 19.18621 -9.33612  -11.31227 1.000 25.80328 ? 29  GLY A O     1 
ATOM   224  N N     . ALA A 1 30  ? 20.72898 -9.42230  -9.68032  1.000 24.82908 ? 30  ALA A N     1 
ATOM   225  C CA    . ALA A 1 30  ? 21.03696 -10.83537 -9.86436  1.000 25.15241 ? 30  ALA A CA    1 
ATOM   226  C C     . ALA A 1 30  ? 21.13658 -11.48416 -8.49555  1.000 29.37269 ? 30  ALA A C     1 
ATOM   227  O O     . ALA A 1 30  ? 21.87982 -11.00458 -7.63027  1.000 27.20497 ? 30  ALA A O     1 
ATOM   228  C CB    . ALA A 1 30  ? 22.34418 -11.05343 -10.63955 1.000 25.25409 ? 30  ALA A CB    1 
ATOM   229  N N     . ILE A 1 31  ? 20.37389 -12.56251 -8.31160  1.000 29.12166 ? 31  ILE A N     1 
ATOM   230  C CA    . ILE A 1 31  ? 20.39680 -13.38885 -7.11054  1.000 25.86078 ? 31  ILE A CA    1 
ATOM   231  C C     . ILE A 1 31  ? 20.59264 -14.83000 -7.55088  1.000 29.34036 ? 31  ILE A C     1 
ATOM   232  O O     . ILE A 1 31  ? 19.93364 -15.28624 -8.49042  1.000 26.55458 ? 31  ILE A O     1 
ATOM   233  C CB    . ILE A 1 31  ? 19.09160 -13.25495 -6.30077  1.000 31.98348 ? 31  ILE A CB    1 
ATOM   234  C CG1   . ILE A 1 31  ? 18.70951 -11.77736 -6.13555  1.000 31.51352 ? 31  ILE A CG1   1 
ATOM   235  C CG2   . ILE A 1 31  ? 19.20151 -13.98030 -4.94815  1.000 27.64817 ? 31  ILE A CG2   1 
ATOM   236  C CD1   . ILE A 1 31  ? 17.28472 -11.57513 -5.63213  1.000 34.90051 ? 31  ILE A CD1   1 
ATOM   237  N N     . GLN A 1 32  ? 21.49963 -15.54491 -6.89147  1.000 23.15494 ? 32  GLN A N     1 
ATOM   238  C CA    . GLN A 1 32  ? 21.68588 -16.96404 -7.15614  1.000 26.36039 ? 32  GLN A CA    1 
ATOM   239  C C     . GLN A 1 32  ? 21.18874 -17.73288 -5.94269  1.000 29.23139 ? 32  GLN A C     1 
ATOM   240  O O     . GLN A 1 32  ? 21.56987 -17.41253 -4.80787  1.000 24.46561 ? 32  GLN A O     1 
ATOM   241  C CB    . GLN A 1 32  ? 23.14831 -17.30266 -7.46005  1.000 30.96226 ? 32  GLN A CB    1 
ATOM   242  C CG    . GLN A 1 32  ? 23.30637 -18.62349 -8.23540  1.000 31.53672 ? 32  GLN A CG    1 
ATOM   243  C CD    . GLN A 1 32  ? 24.75406 -19.08555 -8.32181  1.000 45.03320 ? 32  GLN A CD    1 
ATOM   244  O OE1   . GLN A 1 32  ? 25.61763 -18.59707 -7.58645  1.000 47.18286 ? 32  GLN A OE1   1 
ATOM   245  N NE2   . GLN A 1 32  ? 25.02842 -20.02575 -9.22734  1.000 44.04858 ? 32  GLN A NE2   1 
ATOM   246  N N     . LEU A 1 33  ? 20.31013 -18.71941 -6.18803  1.000 29.33707 ? 33  LEU A N     1 
ATOM   247  C CA    . LEU A 1 33  ? 19.71324 -19.55721 -5.15371  1.000 28.09860 ? 33  LEU A CA    1 
ATOM   248  C C     . LEU A 1 33  ? 20.11704 -21.01714 -5.33548  1.000 33.08510 ? 33  LEU A C     1 
ATOM   249  O O     . LEU A 1 33  ? 20.34186 -21.47990 -6.46244  1.000 29.67333 ? 33  LEU A O     1 
ATOM   250  C CB    . LEU A 1 33  ? 18.18065 -19.45768 -5.18678  1.000 27.83020 ? 33  LEU A CB    1 
ATOM   251  C CG    . LEU A 1 33  ? 17.52393 -18.08337 -5.02015  1.000 33.79294 ? 33  LEU A CG    1 
ATOM   252  C CD1   . LEU A 1 33  ? 16.02798 -18.23345 -5.12481  1.000 29.75879 ? 33  LEU A CD1   1 
ATOM   253  C CD2   . LEU A 1 33  ? 17.89838 -17.44563 -3.69915  1.000 28.78433 ? 33  LEU A CD2   1 
ATOM   254  N N     . ASP A 1 34  ? 20.19254 -21.75932 -4.22366  1.000 28.93778 ? 34  ASP A N     1 
ATOM   255  C CA    . ASP A 1 34  ? 20.25255 -23.20752 -4.35837  1.000 31.91893 ? 34  ASP A CA    1 
ATOM   256  C C     . ASP A 1 34  ? 18.82674 -23.74791 -4.43932  1.000 28.02133 ? 34  ASP A C     1 
ATOM   257  O O     . ASP A 1 34  ? 17.85539 -22.99254 -4.41909  1.000 27.31141 ? 34  ASP A O     1 
ATOM   258  C CB    . ASP A 1 34  ? 21.07154 -23.85380 -3.23570  1.000 29.51203 ? 34  ASP A CB    1 
ATOM   259  C CG    . ASP A 1 34  ? 20.42067 -23.75650 -1.86468  1.000 27.43957 ? 34  ASP A CG    1 
ATOM   260  O OD1   . ASP A 1 34  ? 19.22854 -23.38515 -1.74401  1.000 26.49821 ? 34  ASP A OD1   1 
ATOM   261  O OD2   . ASP A 1 34  ? 21.13598 -24.06878 -0.88980  1.000 28.36122 ? 34  ASP A OD2   1 
ATOM   262  N N     . GLY A 1 35  ? 18.69597 -25.07164 -4.52694  1.000 30.21101 ? 35  GLY A N     1 
ATOM   263  C CA    . GLY A 1 35  ? 17.38681 -25.67720 -4.70794  1.000 36.53649 ? 35  GLY A CA    1 
ATOM   264  C C     . GLY A 1 35  ? 16.41363 -25.44597 -3.56695  1.000 39.74177 ? 35  GLY A C     1 
ATOM   265  O O     . GLY A 1 35  ? 15.20074 -25.57914 -3.76636  1.000 38.75838 ? 35  GLY A O     1 
ATOM   266  N N     . ASP A 1 36  ? 16.91176 -25.11091 -2.37465  1.000 29.40105 ? 36  ASP A N     1 
ATOM   267  C CA    . ASP A 1 36  ? 16.05909 -24.78289 -1.23265  1.000 29.25473 ? 36  ASP A CA    1 
ATOM   268  C C     . ASP A 1 36  ? 15.71716 -23.30269 -1.12203  1.000 36.84539 ? 36  ASP A C     1 
ATOM   269  O O     . ASP A 1 36  ? 14.91501 -22.93529 -0.25593  1.000 38.76551 ? 36  ASP A O     1 
ATOM   270  C CB    . ASP A 1 36  ? 16.72651 -25.22520 0.07775   1.000 35.07694 ? 36  ASP A CB    1 
ATOM   271  C CG    . ASP A 1 36  ? 16.82274 -26.72082 0.19729   1.000 46.13301 ? 36  ASP A CG    1 
ATOM   272  O OD1   . ASP A 1 36  ? 15.88004 -27.40328 -0.25004  1.000 52.72428 ? 36  ASP A OD1   1 
ATOM   273  O OD2   . ASP A 1 36  ? 17.83987 -27.21179 0.73287   1.000 54.51602 ? 36  ASP A OD2   1 
ATOM   274  N N     . GLY A 1 37  ? 16.29626 -22.44546 -1.95508  1.000 27.63868 ? 37  GLY A N     1 
ATOM   275  C CA    . GLY A 1 37  ? 16.04365 -21.02652 -1.86137  1.000 27.12540 ? 37  GLY A CA    1 
ATOM   276  C C     . GLY A 1 37  ? 17.02108 -20.26416 -0.99837  1.000 29.05195 ? 37  GLY A C     1 
ATOM   277  O O     . GLY A 1 37  ? 16.76548 -19.09680 -0.68445  1.000 30.56760 ? 37  GLY A O     1 
ATOM   278  N N     . ASN A 1 38  ? 18.12462 -20.88649 -0.59046  1.000 26.21147 ? 38  ASN A N     1 
ATOM   279  C CA    . ASN A 1 38  ? 19.15678 -20.17495 0.14633   1.000 28.72213 ? 38  ASN A CA    1 
ATOM   280  C C     . ASN A 1 38  ? 19.94263 -19.29222 -0.81232  1.000 30.21730 ? 38  ASN A C     1 
ATOM   281  O O     . ASN A 1 38  ? 20.23573 -19.68779 -1.94451  1.000 30.20270 ? 38  ASN A O     1 
ATOM   282  C CB    . ASN A 1 38  ? 20.07780 -21.16400 0.85166   1.000 30.73912 ? 38  ASN A CB    1 
ATOM   283  C CG    . ASN A 1 38  ? 19.31889 -22.07527 1.79667   1.000 36.92589 ? 38  ASN A CG    1 
ATOM   284  O OD1   . ASN A 1 38  ? 18.54896 -21.60663 2.63304   1.000 36.09930 ? 38  ASN A OD1   1 
ATOM   285  N ND2   . ASN A 1 38  ? 19.50769 -23.38242 1.64884   1.000 32.07050 ? 38  ASN A ND2   1 
ATOM   286  N N     . ILE A 1 39  ? 20.25097 -18.08105 -0.36475  1.000 29.72087 ? 39  ILE A N     1 
ATOM   287  C CA    . ILE A 1 39  ? 20.89778 -17.09057 -1.21575  1.000 24.15603 ? 39  ILE A CA    1 
ATOM   288  C C     . ILE A 1 39  ? 22.39491 -17.39408 -1.26628  1.000 27.49399 ? 39  ILE A C     1 
ATOM   289  O O     . ILE A 1 39  ? 23.06810 -17.40696 -0.23561  1.000 26.72187 ? 39  ILE A O     1 
ATOM   290  C CB    . ILE A 1 39  ? 20.63314 -15.67089 -0.69643  1.000 28.26583 ? 39  ILE A CB    1 
ATOM   291  C CG1   . ILE A 1 39  ? 19.13805 -15.35153 -0.80421  1.000 25.34137 ? 39  ILE A CG1   1 
ATOM   292  C CG2   . ILE A 1 39  ? 21.45932 -14.66990 -1.47264  1.000 24.70926 ? 39  ILE A CG2   1 
ATOM   293  C CD1   . ILE A 1 39  ? 18.67909 -14.16841 0.05782   1.000 25.32950 ? 39  ILE A CD1   1 
ATOM   294  N N     . LEU A 1 40  ? 22.90404 -17.65394 -2.47445  1.000 30.26644 ? 40  LEU A N     1 
ATOM   295  C CA    . LEU A 1 40  ? 24.32820 -17.90010 -2.72443  1.000 27.58898 ? 40  LEU A CA    1 
ATOM   296  C C     . LEU A 1 40  ? 25.08081 -16.65408 -3.16851  1.000 30.96580 ? 40  LEU A C     1 
ATOM   297  O O     . LEU A 1 40  ? 26.23968 -16.45269 -2.77513  1.000 30.74348 ? 40  LEU A O     1 
ATOM   298  C CB    . LEU A 1 40  ? 24.50168 -18.97698 -3.80305  1.000 31.04315 ? 40  LEU A CB    1 
ATOM   299  C CG    . LEU A 1 40  ? 23.79889 -20.30514 -3.56993  1.000 29.35269 ? 40  LEU A CG    1 
ATOM   300  C CD1   . LEU A 1 40  ? 23.99344 -21.22398 -4.76986  1.000 31.05166 ? 40  LEU A CD1   1 
ATOM   301  C CD2   . LEU A 1 40  ? 24.28674 -20.94753 -2.27922  1.000 33.03866 ? 40  LEU A CD2   1 
ATOM   302  N N     . GLN A 1 41  ? 24.45534 -15.83847 -4.01129  1.000 32.68253 ? 41  GLN A N     1 
ATOM   303  C CA    . GLN A 1 41  ? 25.02131 -14.58213 -4.46387  1.000 33.06757 ? 41  GLN A CA    1 
ATOM   304  C C     . GLN A 1 41  ? 23.89807 -13.56441 -4.54365  1.000 26.70506 ? 41  GLN A C     1 
ATOM   305  O O     . GLN A 1 41  ? 22.72965 -13.91801 -4.69926  1.000 26.23766 ? 41  GLN A O     1 
ATOM   306  C CB    . GLN A 1 41  ? 25.71921 -14.73259 -5.82218  1.000 32.24118 ? 41  GLN A CB    1 
ATOM   307  C CG    . GLN A 1 41  ? 26.94472 -15.61430 -5.74936  1.000 36.67101 ? 41  GLN A CG    1 
ATOM   308  C CD    . GLN A 1 41  ? 27.87557 -15.37926 -6.90521  1.000 61.76869 ? 41  GLN A CD    1 
ATOM   309  O OE1   . GLN A 1 41  ? 27.82744 -16.09321 -7.90995  1.000 70.54914 ? 41  GLN A OE1   1 
ATOM   310  N NE2   . GLN A 1 41  ? 28.72802 -14.36316 -6.78256  1.000 68.56591 ? 41  GLN A NE2   1 
ATOM   311  N N     . TYR A 1 42  ? 24.26543 -12.29066 -4.43985  1.000 30.47287 ? 42  TYR A N     1 
ATOM   312  C CA    . TYR A 1 42  ? 23.27440 -11.21561 -4.36566  1.000 34.94967 ? 42  TYR A CA    1 
ATOM   313  C C     . TYR A 1 42  ? 24.02172 -9.93810  -4.72617  1.000 34.68038 ? 42  TYR A C     1 
ATOM   314  O O     . TYR A 1 42  ? 24.87917 -9.49475  -3.95612  1.000 31.29491 ? 42  TYR A O     1 
ATOM   315  C CB    . TYR A 1 42  ? 22.66770 -11.15625 -2.95840  1.000 29.29215 ? 42  TYR A CB    1 
ATOM   316  C CG    . TYR A 1 42  ? 21.47426 -10.24077 -2.75304  1.000 27.76661 ? 42  TYR A CG    1 
ATOM   317  C CD1   . TYR A 1 42  ? 21.65132 -8.87720  -2.53238  1.000 29.71241 ? 42  TYR A CD1   1 
ATOM   318  C CD2   . TYR A 1 42  ? 20.17500 -10.74650 -2.72799  1.000 26.56937 ? 42  TYR A CD2   1 
ATOM   319  C CE1   . TYR A 1 42  ? 20.56423 -8.02241  -2.31927  1.000 30.96896 ? 42  TYR A CE1   1 
ATOM   320  C CE2   . TYR A 1 42  ? 19.07812 -9.90240  -2.51948  1.000 29.19098 ? 42  TYR A CE2   1 
ATOM   321  C CZ    . TYR A 1 42  ? 19.28064 -8.54052  -2.30341  1.000 27.26569 ? 42  TYR A CZ    1 
ATOM   322  O OH    . TYR A 1 42  ? 18.19474 -7.69356  -2.10226  1.000 29.27409 ? 42  TYR A OH    1 
ATOM   323  N N     . ASN A 1 43  ? 23.74517 -9.37442  -5.89959  1.000 25.44538 ? 43  ASN A N     1 
ATOM   324  C CA    . ASN A 1 43  ? 24.64882 -8.34183  -6.37854  1.000 32.07101 ? 43  ASN A CA    1 
ATOM   325  C C     . ASN A 1 43  ? 24.19413 -6.94639  -5.94259  1.000 29.34225 ? 43  ASN A C     1 
ATOM   326  O O     . ASN A 1 43  ? 23.09480 -6.74279  -5.41205  1.000 27.69275 ? 43  ASN A O     1 
ATOM   327  C CB    . ASN A 1 43  ? 24.80732 -8.42815  -7.89974  1.000 30.09066 ? 43  ASN A CB    1 
ATOM   328  C CG    . ASN A 1 43  ? 23.59445 -7.90816  -8.65102  1.000 28.75848 ? 43  ASN A CG    1 
ATOM   329  O OD1   . ASN A 1 43  ? 22.49063 -7.79172  -8.09661  1.000 27.12569 ? 43  ASN A OD1   1 
ATOM   330  N ND2   . ASN A 1 43  ? 23.79029 -7.61354  -9.93649  1.000 27.96387 ? 43  ASN A ND2   1 
ATOM   331  N N     . ALA A 1 44  ? 25.07187 -5.97326  -6.19867  1.000 29.61495 ? 44  ALA A N     1 
ATOM   332  C CA    . ALA A 1 44  ? 24.87590 -4.61628  -5.70063  1.000 32.50546 ? 44  ALA A CA    1 
ATOM   333  C C     . ALA A 1 44  ? 23.65632 -3.94927  -6.32091  1.000 35.30856 ? 44  ALA A C     1 
ATOM   334  O O     . ALA A 1 44  ? 22.97967 -3.15968  -5.64782  1.000 35.14835 ? 44  ALA A O     1 
ATOM   335  C CB    . ALA A 1 44  ? 26.12917 -3.77567  -5.96306  1.000 32.06773 ? 44  ALA A CB    1 
ATOM   336  N N     . ALA A 1 45  ? 23.36585 -4.23855  -7.59613  1.000 29.50405 ? 45  ALA A N     1 
ATOM   337  C CA    . ALA A 1 45  ? 22.21110 -3.62440  -8.24624  1.000 28.67001 ? 45  ALA A CA    1 
ATOM   338  C C     . ALA A 1 45  ? 20.91201 -4.08044  -7.61063  1.000 31.72975 ? 45  ALA A C     1 
ATOM   339  O O     . ALA A 1 45  ? 19.94310 -3.31529  -7.57069  1.000 29.29610 ? 45  ALA A O     1 
ATOM   340  C CB    . ALA A 1 45  ? 22.20298 -3.94163  -9.74347  1.000 33.10017 ? 45  ALA A CB    1 
ATOM   341  N N     . GLU A 1 46  ? 20.86869 -5.31609  -7.10124  1.000 29.98538 ? 46  GLU A N     1 
ATOM   342  C CA    . GLU A 1 46  ? 19.66002 -5.77277  -6.42821  1.000 25.53150 ? 46  GLU A CA    1 
ATOM   343  C C     . GLU A 1 46  ? 19.46814 -5.04240  -5.10493  1.000 31.21611 ? 46  GLU A C     1 
ATOM   344  O O     . GLU A 1 46  ? 18.34917 -4.63001  -4.77657  1.000 32.93457 ? 46  GLU A O     1 
ATOM   345  C CB    . GLU A 1 46  ? 19.71504 -7.28485  -6.21798  1.000 26.49359 ? 46  GLU A CB    1 
ATOM   346  C CG    . GLU A 1 46  ? 18.51620 -7.83678  -5.46534  1.000 27.16099 ? 46  GLU A CG    1 
ATOM   347  C CD    . GLU A 1 46  ? 17.24557 -7.85462  -6.29779  1.000 35.49450 ? 46  GLU A CD    1 
ATOM   348  O OE1   . GLU A 1 46  ? 17.32537 -7.60502  -7.51716  1.000 34.41958 ? 46  GLU A OE1   1 
ATOM   349  O OE2   . GLU A 1 46  ? 16.16438 -8.12577  -5.73282  1.000 27.02473 ? 46  GLU A OE2   1 
ATOM   350  N N     . GLY A 1 47  ? 20.54913 -4.85303  -4.33955  1.000 27.79197 ? 47  GLY A N     1 
ATOM   351  C CA    . GLY A 1 47  ? 20.44210 -4.07277  -3.11752  1.000 28.96866 ? 47  GLY A CA    1 
ATOM   352  C C     . GLY A 1 47  ? 20.01048 -2.63627  -3.37583  1.000 30.11484 ? 47  GLY A C     1 
ATOM   353  O O     . GLY A 1 47  ? 19.28197 -2.04670  -2.57400  1.000 33.16174 ? 47  GLY A O     1 
ATOM   354  N N     . ASP A 1 48  ? 20.47569 -2.05172  -4.48831  1.000 30.41644 ? 48  ASP A N     1 
ATOM   355  C CA    . ASP A 1 48  ? 20.03819 -0.70777  -4.87839  1.000 36.41088 ? 48  ASP A CA    1 
ATOM   356  C C     . ASP A 1 48  ? 18.53278 -0.63434  -5.07431  1.000 37.99243 ? 48  ASP A C     1 
ATOM   357  O O     . ASP A 1 48  ? 17.93127 0.42814   -4.86489  1.000 44.46605 ? 48  ASP A O     1 
ATOM   358  C CB    . ASP A 1 48  ? 20.70822 -0.27361  -6.18154  1.000 36.25826 ? 48  ASP A CB    1 
ATOM   359  C CG    . ASP A 1 48  ? 22.12186 0.19320   -5.98660  1.000 48.19434 ? 48  ASP A CG    1 
ATOM   360  O OD1   . ASP A 1 48  ? 22.52238 0.41468   -4.81970  1.000 42.01772 ? 48  ASP A OD1   1 
ATOM   361  O OD2   . ASP A 1 48  ? 22.82664 0.34401   -7.01284  1.000 54.27076 ? 48  ASP A OD2   1 
ATOM   362  N N     . ILE A 1 49  ? 17.92022 -1.73554  -5.51539  1.000 34.32729 ? 49  ILE A N     1 
ATOM   363  C CA    . ILE A 1 49  ? 16.48660 -1.76776  -5.78519  1.000 33.54270 ? 49  ILE A CA    1 
ATOM   364  C C     . ILE A 1 49  ? 15.69790 -1.98808  -4.50496  1.000 34.75352 ? 49  ILE A C     1 
ATOM   365  O O     . ILE A 1 49  ? 14.63049 -1.39243  -4.31710  1.000 37.49089 ? 49  ILE A O     1 
ATOM   366  C CB    . ILE A 1 49  ? 16.17520 -2.86077  -6.82411  1.000 33.55284 ? 49  ILE A CB    1 
ATOM   367  C CG1   . ILE A 1 49  ? 16.74335 -2.48835  -8.18769  1.000 35.15899 ? 49  ILE A CG1   1 
ATOM   368  C CG2   . ILE A 1 49  ? 14.66560 -3.14949  -6.90851  1.000 32.37069 ? 49  ILE A CG2   1 
ATOM   369  C CD1   . ILE A 1 49  ? 16.69096 -3.63730  -9.17301  1.000 37.95876 ? 49  ILE A CD1   1 
ATOM   370  N N     . THR A 1 50  ? 16.20370 -2.84180  -3.60708  1.000 26.48509 ? 50  THR A N     1 
ATOM   371  C CA    . THR A 1 50  ? 15.43852 -3.29803  -2.44869  1.000 29.89156 ? 50  THR A CA    1 
ATOM   372  C C     . THR A 1 50  ? 15.88088 -2.70778  -1.11573  1.000 36.54741 ? 50  THR A C     1 
ATOM   373  O O     . THR A 1 50  ? 15.15388 -2.85477  -0.12263  1.000 32.17344 ? 50  THR A O     1 
ATOM   374  C CB    . THR A 1 50  ? 15.50548 -4.82510  -2.32650  1.000 32.43829 ? 50  THR A CB    1 
ATOM   375  O OG1   . THR A 1 50  ? 16.86281 -5.22324  -2.04839  1.000 31.17979 ? 50  THR A OG1   1 
ATOM   376  C CG2   . THR A 1 50  ? 15.01690 -5.47036  -3.60191  1.000 28.88565 ? 50  THR A CG2   1 
ATOM   377  N N     . GLY A 1 51  ? 17.04392 -2.07261  -1.04954  1.000 28.43702 ? 51  GLY A N     1 
ATOM   378  C CA    . GLY A 1 51  ? 17.50812 -1.55665  0.21965   1.000 28.04011 ? 51  GLY A CA    1 
ATOM   379  C C     . GLY A 1 51  ? 18.12169 -2.58980  1.13403   1.000 33.33566 ? 51  GLY A C     1 
ATOM   380  O O     . GLY A 1 51  ? 18.29850 -2.31086  2.32484   1.000 33.62905 ? 51  GLY A O     1 
ATOM   381  N N     . ARG A 1 52  ? 18.45725 -3.76879  0.61601   1.000 35.25088 ? 52  ARG A N     1 
ATOM   382  C CA    . ARG A 1 52  ? 19.10467 -4.81713  1.39493   1.000 30.75513 ? 52  ARG A CA    1 
ATOM   383  C C     . ARG A 1 52  ? 20.61177 -4.75210  1.18556   1.000 34.35721 ? 52  ARG A C     1 
ATOM   384  O O     . ARG A 1 52  ? 21.09213 -4.49113  0.07584   1.000 36.59427 ? 52  ARG A O     1 
ATOM   385  C CB    . ARG A 1 52  ? 18.58858 -6.21355  1.00934   1.000 33.26672 ? 52  ARG A CB    1 
ATOM   386  C CG    . ARG A 1 52  ? 17.37054 -6.69065  1.79365   1.000 32.37533 ? 52  ARG A CG    1 
ATOM   387  C CD    . ARG A 1 52  ? 16.15308 -5.82702  1.50824   1.000 35.71816 ? 52  ARG A CD    1 
ATOM   388  N NE    . ARG A 1 52  ? 14.94931 -6.34364  2.14662   1.000 41.11524 ? 52  ARG A NE    1 
ATOM   389  C CZ    . ARG A 1 52  ? 13.73152 -5.84823  1.96456   1.000 41.94709 ? 52  ARG A CZ    1 
ATOM   390  N NH1   . ARG A 1 52  ? 13.51578 -4.81296  1.16370   1.000 35.10268 ? 52  ARG A NH1   1 
ATOM   391  N NH2   . ARG A 1 52  ? 12.70317 -6.41059  2.59549   1.000 39.44433 ? 52  ARG A NH2   1 
ATOM   392  N N     . ASP A 1 53  ? 21.34269 -4.98463  2.25680   1.000 30.43906 ? 53  ASP A N     1 
ATOM   393  C CA    . ASP A 1 53  ? 22.78658 -5.09361  2.18527   1.000 34.26301 ? 53  ASP A CA    1 
ATOM   394  C C     . ASP A 1 53  ? 23.14889 -6.50390  1.71868   1.000 36.55078 ? 53  ASP A C     1 
ATOM   395  O O     . ASP A 1 53  ? 22.82110 -7.47060  2.41200   1.000 35.88465 ? 53  ASP A O     1 
ATOM   396  C CB    . ASP A 1 53  ? 23.39557 -4.80518  3.55110   1.000 30.06862 ? 53  ASP A CB    1 
ATOM   397  C CG    . ASP A 1 53  ? 24.90983 -4.93778  3.55682   1.000 48.81394 ? 53  ASP A CG    1 
ATOM   398  O OD1   . ASP A 1 53  ? 25.52775 -4.76225  2.48683   1.000 50.07342 ? 53  ASP A OD1   1 
ATOM   399  O OD2   . ASP A 1 53  ? 25.47934 -5.22589  4.62987   1.000 60.31985 ? 53  ASP A OD2   1 
ATOM   400  N N     . PRO A 1 54  ? 23.79309 -6.65833  0.55435   1.000 38.94070 ? 54  PRO A N     1 
ATOM   401  C CA    . PRO A 1 54  ? 24.11938 -8.01879  0.07581   1.000 35.03866 ? 54  PRO A CA    1 
ATOM   402  C C     . PRO A 1 54  ? 24.85736 -8.87117  1.09181   1.000 36.65591 ? 54  PRO A C     1 
ATOM   403  O O     . PRO A 1 54  ? 24.62027 -10.08265 1.15971   1.000 37.07811 ? 54  PRO A O     1 
ATOM   404  C CB    . PRO A 1 54  ? 24.98196 -7.74828  -1.16614  1.000 29.12325 ? 54  PRO A CB    1 
ATOM   405  C CG    . PRO A 1 54  ? 24.49355 -6.44081  -1.66012  1.000 32.12197 ? 54  PRO A CG    1 
ATOM   406  C CD    . PRO A 1 54  ? 24.18877 -5.62749  -0.41713  1.000 32.54754 ? 54  PRO A CD    1 
ATOM   407  N N     . LYS A 1 55  ? 25.71891 -8.27330  1.91179   1.000 33.17827 ? 55  LYS A N     1 
ATOM   408  C CA    . LYS A 1 55  ? 26.49543 -9.05597  2.86118   1.000 34.08674 ? 55  LYS A CA    1 
ATOM   409  C C     . LYS A 1 55  ? 25.64737 -9.59786  4.00140   1.000 42.66367 ? 55  LYS A C     1 
ATOM   410  O O     . LYS A 1 55  ? 26.04348 -10.57501 4.64444   1.000 47.97070 ? 55  LYS A O     1 
ATOM   411  C CB    . LYS A 1 55  ? 27.63936 -8.19845  3.39004   1.000 43.55952 ? 55  LYS A CB    1 
ATOM   412  C CG    . LYS A 1 55  ? 28.63799 -7.82396  2.29195   1.000 55.77856 ? 55  LYS A CG    1 
ATOM   413  C CD    . LYS A 1 55  ? 29.02929 -6.34620  2.32665   1.000 73.27481 ? 55  LYS A CD    1 
ATOM   414  C CE    . LYS A 1 55  ? 30.12741 -6.05372  3.35883   1.000 73.04397 ? 55  LYS A CE    1 
ATOM   415  N NZ    . LYS A 1 55  ? 29.68042 -6.24347  4.77249   1.000 68.57564 ? 55  LYS A NZ    1 
ATOM   416  N N     . GLN A 1 56  ? 24.48828 -9.00325  4.26352   1.000 41.64210 ? 56  GLN A N     1 
ATOM   417  C CA    . GLN A 1 56  ? 23.61531 -9.52331  5.30982   1.000 46.12516 ? 56  GLN A CA    1 
ATOM   418  C C     . GLN A 1 56  ? 22.64417 -10.58810 4.80960   1.000 44.98254 ? 56  GLN A C     1 
ATOM   419  O O     . GLN A 1 56  ? 22.23870 -11.46100 5.58846   1.000 48.17899 ? 56  GLN A O     1 
ATOM   420  C CB    . GLN A 1 56  ? 22.82162 -8.38548  5.96174   1.000 51.28040 ? 56  GLN A CB    1 
ATOM   421  C CG    . GLN A 1 56  ? 23.63752 -7.52868  6.92243   1.000 60.37416 ? 56  GLN A CG    1 
ATOM   422  C CD    . GLN A 1 56  ? 22.87171 -6.31106  7.40876   1.000 68.06358 ? 56  GLN A CD    1 
ATOM   423  O OE1   . GLN A 1 56  ? 23.28979 -5.16671  7.18182   1.000 61.00957 ? 56  GLN A OE1   1 
ATOM   424  N NE2   . GLN A 1 56  ? 21.74452 -6.54933  8.08763   1.000 68.27219 ? 56  GLN A NE2   1 
ATOM   425  N N     . VAL A 1 57  ? 22.24814 -10.54144 3.54048   1.000 34.86500 ? 57  VAL A N     1 
ATOM   426  C CA    . VAL A 1 57  ? 21.26559 -11.50374 3.04720   1.000 35.34458 ? 57  VAL A CA    1 
ATOM   427  C C     . VAL A 1 57  ? 21.88510 -12.80266 2.53460   1.000 33.48629 ? 57  VAL A C     1 
ATOM   428  O O     . VAL A 1 57  ? 21.18619 -13.82258 2.46017   1.000 32.36510 ? 57  VAL A O     1 
ATOM   429  C CB    . VAL A 1 57  ? 20.39601 -10.87541 1.94686   1.000 33.02626 ? 57  VAL A CB    1 
ATOM   430  C CG1   . VAL A 1 57  ? 19.56964 -9.74065  2.52494   1.000 31.62837 ? 57  VAL A CG1   1 
ATOM   431  C CG2   . VAL A 1 57  ? 21.26328 -10.38261 0.80114   1.000 31.68635 ? 57  VAL A CG2   1 
ATOM   432  N N     . ILE A 1 58  ? 23.17201 -12.80820 2.19236   1.000 35.29980 ? 58  ILE A N     1 
ATOM   433  C CA    . ILE A 1 58  ? 23.78143 -14.02833 1.67007   1.000 41.19559 ? 58  ILE A CA    1 
ATOM   434  C C     . ILE A 1 58  ? 23.75920 -15.10862 2.74546   1.000 32.94889 ? 58  ILE A C     1 
ATOM   435  O O     . ILE A 1 58  ? 24.10023 -14.86027 3.90965   1.000 34.26953 ? 58  ILE A O     1 
ATOM   436  C CB    . ILE A 1 58  ? 25.20317 -13.73714 1.16463   1.000 41.40536 ? 58  ILE A CB    1 
ATOM   437  C CG1   . ILE A 1 58  ? 25.12574 -13.08506 -0.22985  1.000 42.57777 ? 58  ILE A CG1   1 
ATOM   438  C CG2   . ILE A 1 58  ? 26.03885 -15.01030 1.13594   1.000 39.91466 ? 58  ILE A CG2   1 
ATOM   439  C CD1   . ILE A 1 58  ? 26.46214 -12.59054 -0.78006  1.000 50.47192 ? 58  ILE A CD1   1 
ATOM   440  N N     . GLY A 1 59  ? 23.31948 -16.31663 2.36290   1.000 33.19422 ? 59  GLY A N     1 
ATOM   441  C CA    . GLY A 1 59  ? 23.14553 -17.41080 3.29779   1.000 31.80974 ? 59  GLY A CA    1 
ATOM   442  C C     . GLY A 1 59  ? 21.74758 -17.54499 3.87101   1.000 40.82332 ? 59  GLY A C     1 
ATOM   443  O O     . GLY A 1 59  ? 21.40893 -18.60964 4.39840   1.000 33.36010 ? 59  GLY A O     1 
ATOM   444  N N     . LYS A 1 60  ? 20.92890 -16.49728 3.79190   1.000 33.73448 ? 60  LYS A N     1 
ATOM   445  C CA    . LYS A 1 60  ? 19.57769 -16.57080 4.30720   1.000 31.45479 ? 60  LYS A CA    1 
ATOM   446  C C     . LYS A 1 60  ? 18.67835 -17.19666 3.25858   1.000 34.65060 ? 60  LYS A C     1 
ATOM   447  O O     . LYS A 1 60  ? 19.03798 -17.30669 2.08057   1.000 31.16801 ? 60  LYS A O     1 
ATOM   448  C CB    . LYS A 1 60  ? 19.05685 -15.18526 4.69612   1.000 31.64247 ? 60  LYS A CB    1 
ATOM   449  C CG    . LYS A 1 60  ? 19.80488 -14.52843 5.84024   1.000 30.80104 ? 60  LYS A CG    1 
ATOM   450  C CD    . LYS A 1 60  ? 18.89152 -13.60310 6.61960   1.000 42.23059 ? 60  LYS A CD    1 
ATOM   451  C CE    . LYS A 1 60  ? 19.67589 -12.67332 7.53217   1.000 46.79838 ? 60  LYS A CE    1 
ATOM   452  N NZ    . LYS A 1 60  ? 21.10693 -13.08341 7.68442   1.000 55.02554 ? 60  LYS A NZ    1 
ATOM   453  N N     . ASN A 1 61  ? 17.49275 -17.62047 3.69114   1.000 30.46459 ? 61  ASN A N     1 
ATOM   454  C CA    . ASN A 1 61  ? 16.54776 -18.22839 2.76799   1.000 30.08999 ? 61  ASN A CA    1 
ATOM   455  C C     . ASN A 1 61  ? 15.65637 -17.15077 2.16373   1.000 34.05624 ? 61  ASN A C     1 
ATOM   456  O O     . ASN A 1 61  ? 14.96436 -16.41968 2.88902   1.000 31.23425 ? 61  ASN A O     1 
ATOM   457  C CB    . ASN A 1 61  ? 15.70250 -19.30062 3.44249   1.000 31.09102 ? 61  ASN A CB    1 
ATOM   458  C CG    . ASN A 1 61  ? 14.91181 -20.10081 2.43126   1.000 36.75100 ? 61  ASN A CG    1 
ATOM   459  O OD1   . ASN A 1 61  ? 13.85593 -19.66786 1.97579   1.000 29.00663 ? 61  ASN A OD1   1 
ATOM   460  N ND2   . ASN A 1 61  ? 15.44149 -21.25541 2.04393   1.000 31.36331 ? 61  ASN A ND2   1 
ATOM   461  N N     . PHE A 1 62  ? 15.67128 -17.07646 0.83219   1.000 29.80305 ? 62  PHE A N     1 
ATOM   462  C CA    . PHE A 1 62  ? 14.95507 -16.03462 0.11121   1.000 28.65640 ? 62  PHE A CA    1 
ATOM   463  C C     . PHE A 1 62  ? 13.45315 -16.09408 0.38049   1.000 33.34233 ? 62  PHE A C     1 
ATOM   464  O O     . PHE A 1 62  ? 12.82713 -15.06361 0.65697   1.000 29.19143 ? 62  PHE A O     1 
ATOM   465  C CB    . PHE A 1 62  ? 15.24753 -16.16976 -1.38247  1.000 26.94359 ? 62  PHE A CB    1 
ATOM   466  C CG    . PHE A 1 62  ? 14.72159 -15.03524 -2.21421  1.000 29.08947 ? 62  PHE A CG    1 
ATOM   467  C CD1   . PHE A 1 62  ? 15.31857 -13.78113 -2.15263  1.000 35.50484 ? 62  PHE A CD1   1 
ATOM   468  C CD2   . PHE A 1 62  ? 13.65139 -15.22548 -3.07960  1.000 27.95319 ? 62  PHE A CD2   1 
ATOM   469  C CE1   . PHE A 1 62  ? 14.84752 -12.72269 -2.92684  1.000 28.65085 ? 62  PHE A CE1   1 
ATOM   470  C CE2   . PHE A 1 62  ? 13.17101 -14.17747 -3.86669  1.000 32.18183 ? 62  PHE A CE2   1 
ATOM   471  C CZ    . PHE A 1 62  ? 13.76689 -12.92347 -3.79282  1.000 29.90328 ? 62  PHE A CZ    1 
ATOM   472  N N     . PHE A 1 63  ? 12.85991 -17.29188 0.34369   1.000 30.36955 ? 63  PHE A N     1 
ATOM   473  C CA    . PHE A 1 63  ? 11.40453 -17.37475 0.41443   1.000 30.69854 ? 63  PHE A CA    1 
ATOM   474  C C     . PHE A 1 63  ? 10.88164 -17.33168 1.83731   1.000 30.41448 ? 63  PHE A C     1 
ATOM   475  O O     . PHE A 1 63  ? 9.76078  -16.85431 2.05589   1.000 30.57512 ? 63  PHE A O     1 
ATOM   476  C CB    . PHE A 1 63  ? 10.91029 -18.63704 -0.28455  1.000 26.04419 ? 63  PHE A CB    1 
ATOM   477  C CG    . PHE A 1 63  ? 11.29820 -18.69440 -1.72249  1.000 32.76605 ? 63  PHE A CG    1 
ATOM   478  C CD1   . PHE A 1 63  ? 10.69530 -17.84817 -2.64209  1.000 27.65733 ? 63  PHE A CD1   1 
ATOM   479  C CD2   . PHE A 1 63  ? 12.29898 -19.55336 -2.14992  1.000 26.40185 ? 63  PHE A CD2   1 
ATOM   480  C CE1   . PHE A 1 63  ? 11.06508 -17.87816 -3.97432  1.000 30.29424 ? 63  PHE A CE1   1 
ATOM   481  C CE2   . PHE A 1 63  ? 12.68332 -19.58838 -3.47612  1.000 28.30088 ? 63  PHE A CE2   1 
ATOM   482  C CZ    . PHE A 1 63  ? 12.06724 -18.75145 -4.39380  1.000 30.67031 ? 63  PHE A CZ    1 
ATOM   483  N N     . LYS A 1 64  ? 11.65967 -17.81463 2.80664   1.000 28.53812 ? 64  LYS A N     1 
ATOM   484  C CA    . LYS A 1 64  ? 11.19534 -17.83466 4.18847   1.000 25.67418 ? 64  LYS A CA    1 
ATOM   485  C C     . LYS A 1 64  ? 11.51424 -16.55080 4.93850   1.000 34.44246 ? 64  LYS A C     1 
ATOM   486  O O     . LYS A 1 64  ? 10.67780 -16.07407 5.70982   1.000 37.23638 ? 64  LYS A O     1 
ATOM   487  C CB    . LYS A 1 64  ? 11.80000 -19.01333 4.95000   1.000 33.57699 ? 64  LYS A CB    1 
ATOM   488  C CG    . LYS A 1 64  ? 11.36899 -19.04080 6.40447   1.000 31.05452 ? 64  LYS A CG    1 
ATOM   489  C CD    . LYS A 1 64  ? 11.95267 -20.21361 7.20404   1.000 34.58728 ? 64  LYS A CD    1 
ATOM   490  C CE    . LYS A 1 64  ? 11.49478 -20.09096 8.65602   1.000 48.66666 ? 64  LYS A CE    1 
ATOM   491  N NZ    . LYS A 1 64  ? 12.05624 -21.10383 9.59964   1.000 59.27617 ? 64  LYS A NZ    1 
ATOM   492  N N     . ASP A 1 65  ? 12.70071 -15.97521 4.72732   1.000 29.84146 ? 65  ASP A N     1 
ATOM   493  C CA    . ASP A 1 65  ? 13.18961 -14.88447 5.56302   1.000 33.22194 ? 65  ASP A CA    1 
ATOM   494  C C     . ASP A 1 65  ? 13.29492 -13.55207 4.84370   1.000 27.23842 ? 65  ASP A C     1 
ATOM   495  O O     . ASP A 1 65  ? 12.84669 -12.53501 5.37981   1.000 34.03530 ? 65  ASP A O     1 
ATOM   496  C CB    . ASP A 1 65  ? 14.55413 -15.25151 6.14249   1.000 35.19283 ? 65  ASP A CB    1 
ATOM   497  C CG    . ASP A 1 65  ? 14.49615 -16.50785 6.97230   1.000 46.49464 ? 65  ASP A CG    1 
ATOM   498  O OD1   . ASP A 1 65  ? 13.75599 -16.53778 7.98522   1.000 46.52386 ? 65  ASP A OD1   1 
ATOM   499  O OD2   . ASP A 1 65  ? 15.16233 -17.48296 6.57847   1.000 49.37854 ? 65  ASP A OD2   1 
ATOM   500  N N     . VAL A 1 66  ? 13.89350 -13.51891 3.65885   1.000 27.89769 ? 66  VAL A N     1 
ATOM   501  C CA    . VAL A 1 66  ? 14.18237 -12.23972 3.02096   1.000 29.32417 ? 66  VAL A CA    1 
ATOM   502  C C     . VAL A 1 66  ? 12.97772 -11.70095 2.24998   1.000 35.34786 ? 66  VAL A C     1 
ATOM   503  O O     . VAL A 1 66  ? 12.69788 -10.49941 2.30752   1.000 33.00023 ? 66  VAL A O     1 
ATOM   504  C CB    . VAL A 1 66  ? 15.43277 -12.36895 2.12423   1.000 28.60770 ? 66  VAL A CB    1 
ATOM   505  C CG1   . VAL A 1 66  ? 15.73580 -11.04433 1.41630   1.000 28.71523 ? 66  VAL A CG1   1 
ATOM   506  C CG2   . VAL A 1 66  ? 16.63629 -12.75396 2.95196   1.000 28.51741 ? 66  VAL A CG2   1 
ATOM   507  N N     . ALA A 1 67  ? 12.21718 -12.54644 1.54883   1.000 29.27299 ? 67  ALA A N     1 
ATOM   508  C CA    . ALA A 1 67  ? 11.21729 -12.07732 0.58298   1.000 26.93806 ? 67  ALA A CA    1 
ATOM   509  C C     . ALA A 1 67  ? 9.89211  -12.82426 0.73271   1.000 27.26618 ? 67  ALA A C     1 
ATOM   510  O O     . ALA A 1 67  ? 9.43910  -13.48305 -0.20370  1.000 26.65580 ? 67  ALA A O     1 
ATOM   511  C CB    . ALA A 1 67  ? 11.75124 -12.23236 -0.83898  1.000 24.85220 ? 67  ALA A CB    1 
ATOM   512  N N     . PRO A 1 68  ? 9.22840  -12.70786 1.88844   1.000 30.93699 ? 68  PRO A N     1 
ATOM   513  C CA    . PRO A 1 68  ? 7.96891  -13.45245 2.06927   1.000 30.98801 ? 68  PRO A CA    1 
ATOM   514  C C     . PRO A 1 68  ? 6.89968  -13.08200 1.05805   1.000 28.57421 ? 68  PRO A C     1 
ATOM   515  O O     . PRO A 1 68  ? 6.01181  -13.90409 0.79043   1.000 28.62002 ? 68  PRO A O     1 
ATOM   516  C CB    . PRO A 1 68  ? 7.54203  -13.09541 3.50083   1.000 27.88537 ? 68  PRO A CB    1 
ATOM   517  C CG    . PRO A 1 68  ? 8.23812  -11.81762 3.79896   1.000 30.83914 ? 68  PRO A CG    1 
ATOM   518  C CD    . PRO A 1 68  ? 9.54801  -11.88219 3.06510   1.000 27.13506 ? 68  PRO A CD    1 
ATOM   519  N N     . CYS A 1 69  ? 6.95331  -11.88571 0.47048   1.000 28.96376 ? 69  CYS A N     1 
ATOM   520  C CA    . CYS A 1 69  ? 5.94098  -11.56334 -0.52278  1.000 24.97325 ? 69  CYS A CA    1 
ATOM   521  C C     . CYS A 1 69  ? 6.07864  -12.41221 -1.77845  1.000 27.11976 ? 69  CYS A C     1 
ATOM   522  O O     . CYS A 1 69  ? 5.14581  -12.43687 -2.58426  1.000 28.32937 ? 69  CYS A O     1 
ATOM   523  C CB    . CYS A 1 69  ? 5.99168  -10.07791 -0.88475  1.000 28.75189 ? 69  CYS A CB    1 
ATOM   524  S SG    . CYS A 1 69  ? 7.30083  -9.63259  -2.03519  1.000 28.76665 ? 69  CYS A SG    1 
ATOM   525  N N     . THR A 1 70  ? 7.19743  -13.11843 -1.95292  1.000 25.21850 ? 70  THR A N     1 
ATOM   526  C CA    . THR A 1 70  ? 7.37434  -14.02891 -3.08110  1.000 22.10080 ? 70  THR A CA    1 
ATOM   527  C C     . THR A 1 70  ? 6.99310  -15.46059 -2.74991  1.000 27.29866 ? 70  THR A C     1 
ATOM   528  O O     . THR A 1 70  ? 7.03532  -16.32526 -3.63573  1.000 31.22250 ? 70  THR A O     1 
ATOM   529  C CB    . THR A 1 70  ? 8.82529  -14.02634 -3.57587  1.000 25.14942 ? 70  THR A CB    1 
ATOM   530  O OG1   . THR A 1 70  ? 9.66552  -14.65160 -2.59826  1.000 27.77445 ? 70  THR A OG1   1 
ATOM   531  C CG2   . THR A 1 70  ? 9.29576  -12.62199 -3.83922  1.000 25.24385 ? 70  THR A CG2   1 
ATOM   532  N N     . ASP A 1 71  ? 6.65761  -15.73519 -1.49936  1.000 23.37691 ? 71  ASP A N     1 
ATOM   533  C CA    . ASP A 1 71  ? 6.13028  -17.02981 -1.08611  1.000 26.57087 ? 71  ASP A CA    1 
ATOM   534  C C     . ASP A 1 71  ? 4.66517  -17.06631 -1.51338  1.000 31.90597 ? 71  ASP A C     1 
ATOM   535  O O     . ASP A 1 71  ? 3.76201  -16.67795 -0.76818  1.000 29.52508 ? 71  ASP A O     1 
ATOM   536  C CB    . ASP A 1 71  ? 6.30670  -17.18634 0.41303   1.000 27.46808 ? 71  ASP A CB    1 
ATOM   537  C CG    . ASP A 1 71  ? 5.86663  -18.52750 0.92405   1.000 31.98513 ? 71  ASP A CG    1 
ATOM   538  O OD1   . ASP A 1 71  ? 5.43215  -19.37582 0.11455   1.000 31.85692 ? 71  ASP A OD1   1 
ATOM   539  O OD2   . ASP A 1 71  ? 5.96183  -18.71148 2.15789   1.000 32.49604 ? 71  ASP A OD2   1 
ATOM   540  N N     . SER A 1 72  ? 4.44088  -17.51556 -2.74476  1.000 30.81922 ? 72  SER A N     1 
ATOM   541  C CA    . SER A 1 72  ? 3.13356  -17.49769 -3.38989  1.000 23.97811 ? 72  SER A CA    1 
ATOM   542  C C     . SER A 1 72  ? 3.19664  -18.42271 -4.59162  1.000 28.21870 ? 72  SER A C     1 
ATOM   543  O O     . SER A 1 72  ? 4.28127  -18.66227 -5.13046  1.000 26.81371 ? 72  SER A O     1 
ATOM   544  C CB    . SER A 1 72  ? 2.75454  -16.08185 -3.84324  1.000 32.17032 ? 72  SER A CB    1 
ATOM   545  O OG    . SER A 1 72  ? 3.48485  -15.74377 -5.01498  1.000 31.03246 ? 72  SER A OG    1 
ATOM   546  N N     . PRO A 1 73  ? 2.05361  -18.94839 -5.04269  1.000 27.59570 ? 73  PRO A N     1 
ATOM   547  C CA    . PRO A 1 73  ? 2.08188  -19.81563 -6.23203  1.000 32.88284 ? 73  PRO A CA    1 
ATOM   548  C C     . PRO A 1 73  ? 2.70304  -19.15795 -7.45912  1.000 31.63211 ? 73  PRO A C     1 
ATOM   549  O O     . PRO A 1 73  ? 3.28709  -19.85607 -8.30028  1.000 30.90915 ? 73  PRO A O     1 
ATOM   550  C CB    . PRO A 1 73  ? 0.59474  -20.13449 -6.45413  1.000 28.73672 ? 73  PRO A CB    1 
ATOM   551  C CG    . PRO A 1 73  ? -0.03451 -19.99215 -5.10167  1.000 29.71004 ? 73  PRO A CG    1 
ATOM   552  C CD    . PRO A 1 73  ? 0.68639  -18.79993 -4.51402  1.000 33.77699 ? 73  PRO A CD    1 
ATOM   553  N N     . GLU A 1 74  ? 2.60378  -17.83240 -7.58821  1.000 32.81886 ? 74  GLU A N     1 
ATOM   554  C CA    . GLU A 1 74  ? 3.02401  -17.17717 -8.82199  1.000 34.48090 ? 74  GLU A CA    1 
ATOM   555  C C     . GLU A 1 74  ? 4.52000  -16.91228 -8.86987  1.000 28.59421 ? 74  GLU A C     1 
ATOM   556  O O     . GLU A 1 74  ? 5.03341  -16.54600 -9.93332  1.000 31.74555 ? 74  GLU A O     1 
ATOM   557  C CB    A GLU A 1 74  ? 2.25937  -15.85883 -9.00817  0.620 38.24920 ? 74  GLU A CB    1 
ATOM   558  C CB    B GLU A 1 74  ? 2.27243  -15.85519 -9.02042  0.380 38.14003 ? 74  GLU A CB    1 
ATOM   559  C CG    A GLU A 1 74  ? 1.74822  -15.21257 -7.72659  0.620 37.06355 ? 74  GLU A CG    1 
ATOM   560  C CG    B GLU A 1 74  ? 1.33698  -15.82621 -10.24062 0.380 43.09778 ? 74  GLU A CG    1 
ATOM   561  C CD    A GLU A 1 74  ? 0.46070  -15.83619 -7.22400  0.620 31.97447 ? 74  GLU A CD    1 
ATOM   562  C CD    B GLU A 1 74  ? 2.04660  -16.09699 -11.56836 0.380 43.10928 ? 74  GLU A CD    1 
ATOM   563  O OE1   A GLU A 1 74  ? -0.40584 -16.20119 -8.04598  0.620 36.83946 ? 74  GLU A OE1   1 
ATOM   564  O OE1   B GLU A 1 74  ? 3.18333  -15.60361 -11.77731 0.380 36.99008 ? 74  GLU A OE1   1 
ATOM   565  O OE2   A GLU A 1 74  ? 0.32259  -15.96960 -5.99975  0.620 41.78209 ? 74  GLU A OE2   1 
ATOM   566  O OE2   B GLU A 1 74  ? 1.45361  -16.81351 -12.40536 0.380 41.56428 ? 74  GLU A OE2   1 
ATOM   567  N N     . PHE A 1 75  ? 5.22255  -17.08280 -7.75358  1.000 27.42015 ? 75  PHE A N     1 
ATOM   568  C CA    . PHE A 1 75  ? 6.65532  -16.83685 -7.71566  1.000 21.13491 ? 75  PHE A CA    1 
ATOM   569  C C     . PHE A 1 75  ? 7.35124  -18.08164 -7.16799  1.000 29.15529 ? 75  PHE A C     1 
ATOM   570  O O     . PHE A 1 75  ? 7.93618  -18.85448 -7.93734  1.000 27.65675 ? 75  PHE A O     1 
ATOM   571  C CB    . PHE A 1 75  ? 6.93814  -15.58067 -6.88011  1.000 24.36664 ? 75  PHE A CB    1 
ATOM   572  C CG    . PHE A 1 75  ? 8.31132  -14.97763 -7.09470  1.000 25.76358 ? 75  PHE A CG    1 
ATOM   573  C CD1   . PHE A 1 75  ? 9.46231  -15.75737 -7.00450  1.000 27.04089 ? 75  PHE A CD1   1 
ATOM   574  C CD2   . PHE A 1 75  ? 8.44433  -13.61721 -7.35989  1.000 24.74424 ? 75  PHE A CD2   1 
ATOM   575  C CE1   . PHE A 1 75  ? 10.72486 -15.19917 -7.18811  1.000 27.89685 ? 75  PHE A CE1   1 
ATOM   576  C CE2   . PHE A 1 75  ? 9.70772  -13.04719 -7.55200  1.000 23.73126 ? 75  PHE A CE2   1 
ATOM   577  C CZ    . PHE A 1 75  ? 10.85047 -13.84491 -7.46592  1.000 25.92538 ? 75  PHE A CZ    1 
ATOM   578  N N     . TYR A 1 76  ? 7.27869  -18.29226 -5.84540  1.000 26.27176 ? 76  TYR A N     1 
ATOM   579  C CA    . TYR A 1 76  ? 7.85328  -19.49258 -5.23280  1.000 26.16989 ? 76  TYR A CA    1 
ATOM   580  C C     . TYR A 1 76  ? 7.33610  -20.77152 -5.89786  1.000 26.18741 ? 76  TYR A C     1 
ATOM   581  O O     . TYR A 1 76  ? 8.09541  -21.72927 -6.10675  1.000 25.64039 ? 76  TYR A O     1 
ATOM   582  C CB    . TYR A 1 76  ? 7.54395  -19.49548 -3.72859  1.000 27.47399 ? 76  TYR A CB    1 
ATOM   583  C CG    . TYR A 1 76  ? 8.17816  -20.61768 -2.92668  1.000 28.88033 ? 76  TYR A CG    1 
ATOM   584  C CD1   . TYR A 1 76  ? 9.30059  -21.30571 -3.39676  1.000 34.72769 ? 76  TYR A CD1   1 
ATOM   585  C CD2   . TYR A 1 76  ? 7.64585  -20.99397 -1.68928  1.000 34.41963 ? 76  TYR A CD2   1 
ATOM   586  C CE1   . TYR A 1 76  ? 9.87276  -22.34212 -2.64870  1.000 38.69211 ? 76  TYR A CE1   1 
ATOM   587  C CE2   . TYR A 1 76  ? 8.20935  -22.02633 -0.93708  1.000 39.36050 ? 76  TYR A CE2   1 
ATOM   588  C CZ    . TYR A 1 76  ? 9.32058  -22.69574 -1.42349  1.000 43.52412 ? 76  TYR A CZ    1 
ATOM   589  O OH    . TYR A 1 76  ? 9.87749  -23.71371 -0.67697  1.000 53.52651 ? 76  TYR A OH    1 
ATOM   590  N N     . GLY A 1 77  ? 6.05004  -20.80080 -6.25354  1.000 26.18396 ? 77  GLY A N     1 
ATOM   591  C CA    . GLY A 1 77  ? 5.48856  -22.00116 -6.85942  1.000 30.06374 ? 77  GLY A CA    1 
ATOM   592  C C     . GLY A 1 77  ? 6.11637  -22.32924 -8.19987  1.000 31.58208 ? 77  GLY A C     1 
ATOM   593  O O     . GLY A 1 77  ? 6.37359  -23.49656 -8.50873  1.000 31.91704 ? 77  GLY A O     1 
ATOM   594  N N     . LYS A 1 78  ? 6.37267  -21.30511 -9.02189  1.000 24.70042 ? 78  LYS A N     1 
ATOM   595  C CA    . LYS A 1 78  ? 7.01785  -21.54103 -10.30829 1.000 29.66080 ? 78  LYS A CA    1 
ATOM   596  C C     . LYS A 1 78  ? 8.46906  -21.97497 -10.12045 1.000 34.17202 ? 78  LYS A C     1 
ATOM   597  O O     . LYS A 1 78  ? 8.96088  -22.86058 -10.83422 1.000 33.53315 ? 78  LYS A O     1 
ATOM   598  C CB    . LYS A 1 78  ? 6.92013  -20.28059 -11.17237 1.000 32.16065 ? 78  LYS A CB    1 
ATOM   599  C CG    . LYS A 1 78  ? 5.46779  -19.97415 -11.59803 1.000 39.04103 ? 78  LYS A CG    1 
ATOM   600  C CD    . LYS A 1 78  ? 5.36387  -18.70915 -12.45650 1.000 48.44894 ? 78  LYS A CD    1 
ATOM   601  C CE    . LYS A 1 78  ? 4.00160  -18.61282 -13.14223 1.000 56.41364 ? 78  LYS A CE    1 
ATOM   602  N NZ    . LYS A 1 78  ? 3.81432  -19.68775 -14.17635 1.000 54.42807 ? 78  LYS A NZ    1 
ATOM   603  N N     . PHE A 1 79  ? 9.16034  -21.37304 -9.15058  1.000 30.97796 ? 79  PHE A N     1 
ATOM   604  C CA    . PHE A 1 79  ? 10.50950 -21.80553 -8.79442  1.000 24.77751 ? 79  PHE A CA    1 
ATOM   605  C C     . PHE A 1 79  ? 10.54405 -23.29215 -8.44713  1.000 31.72406 ? 79  PHE A C     1 
ATOM   606  O O     . PHE A 1 79  ? 11.37062 -24.04692 -8.97899  1.000 33.66211 ? 79  PHE A O     1 
ATOM   607  C CB    . PHE A 1 79  ? 11.01761 -20.96382 -7.62500  1.000 26.71878 ? 79  PHE A CB    1 
ATOM   608  C CG    . PHE A 1 79  ? 12.37578 -21.36590 -7.13279  1.000 30.30389 ? 79  PHE A CG    1 
ATOM   609  C CD1   . PHE A 1 79  ? 13.51688 -20.86829 -7.73346  1.000 31.36873 ? 79  PHE A CD1   1 
ATOM   610  C CD2   . PHE A 1 79  ? 12.51090 -22.22809 -6.05399  1.000 34.13114 ? 79  PHE A CD2   1 
ATOM   611  C CE1   . PHE A 1 79  ? 14.77079 -21.24203 -7.26789  1.000 36.71782 ? 79  PHE A CE1   1 
ATOM   612  C CE2   . PHE A 1 79  ? 13.76010 -22.60006 -5.58374  1.000 34.61466 ? 79  PHE A CE2   1 
ATOM   613  C CZ    . PHE A 1 79  ? 14.88505 -22.11472 -6.19442  1.000 35.44602 ? 79  PHE A CZ    1 
ATOM   614  N N     . LYS A 1 80  ? 9.63678  -23.74051 -7.57101  1.000 29.42828 ? 80  LYS A N     1 
ATOM   615  C CA    . LYS A 1 80  ? 9.65052  -25.14639 -7.16051  1.000 34.32732 ? 80  LYS A CA    1 
ATOM   616  C C     . LYS A 1 80  ? 9.31792  -26.09120 -8.32048  1.000 30.65400 ? 80  LYS A C     1 
ATOM   617  O O     . LYS A 1 80  ? 9.89308  -27.18269 -8.41217  1.000 34.54311 ? 80  LYS A O     1 
ATOM   618  C CB    . LYS A 1 80  ? 8.69541  -25.36695 -5.98231  1.000 37.96086 ? 80  LYS A CB    1 
ATOM   619  C CG    . LYS A 1 80  ? 7.28787  -25.77860 -6.36087  1.000 46.68300 ? 80  LYS A CG    1 
ATOM   620  C CD    . LYS A 1 80  ? 6.74002  -26.78414 -5.38478  1.000 45.41595 ? 80  LYS A CD    1 
ATOM   621  C CE    . LYS A 1 80  ? 5.32752  -27.22850 -5.77205  1.000 58.34421 ? 80  LYS A CE    1 
ATOM   622  N NZ    . LYS A 1 80  ? 5.30275  -28.31291 -6.80860  1.000 57.79954 ? 80  LYS A NZ    1 
ATOM   623  N N     . GLU A 1 81  ? 8.38506  -25.71029 -9.20655  1.000 33.55061 ? 81  GLU A N     1 
ATOM   624  C CA    . GLU A 1 81  ? 8.12777  -26.53551 -10.38685 1.000 37.05668 ? 81  GLU A CA    1 
ATOM   625  C C     . GLU A 1 81  ? 9.37633  -26.64821 -11.24337 1.000 35.20391 ? 81  GLU A C     1 
ATOM   626  O O     . GLU A 1 81  ? 9.68074  -27.72548 -11.77290 1.000 34.25388 ? 81  GLU A O     1 
ATOM   627  C CB    . GLU A 1 81  ? 7.00205  -25.95362 -11.23961 1.000 36.00479 ? 81  GLU A CB    1 
ATOM   628  C CG    . GLU A 1 81  ? 5.60674  -26.03818 -10.67305 1.000 48.86402 ? 81  GLU A CG    1 
ATOM   629  C CD    . GLU A 1 81  ? 4.67603  -25.04946 -11.36979 1.000 61.84272 ? 81  GLU A CD    1 
ATOM   630  O OE1   . GLU A 1 81  ? 3.50397  -24.92270 -10.94478 1.000 63.85068 ? 81  GLU A OE1   1 
ATOM   631  O OE2   . GLU A 1 81  ? 5.12669  -24.37646 -12.33645 1.000 56.79022 ? 81  GLU A OE2   1 
ATOM   632  N N     . GLY A 1 82  ? 10.08798 -25.52872 -11.41894 1.000 32.28901 ? 82  GLY A N     1 
ATOM   633  C CA    . GLY A 1 82  ? 11.28117 -25.53223 -12.25048 1.000 38.84834 ? 82  GLY A CA    1 
ATOM   634  C C     . GLY A 1 82  ? 12.40412 -26.36850 -11.66452 1.000 41.36770 ? 82  GLY A C     1 
ATOM   635  O O     . GLY A 1 82  ? 13.08228 -27.10863 -12.38766 1.000 37.11295 ? 82  GLY A O     1 
ATOM   636  N N     . VAL A 1 83  ? 12.62809 -26.25402 -10.35268 1.000 36.78042 ? 83  VAL A N     1 
ATOM   637  C CA    . VAL A 1 83  ? 13.64099 -27.07870 -9.70135  1.000 35.09331 ? 83  VAL A CA    1 
ATOM   638  C C     . VAL A 1 83  ? 13.31964 -28.55137 -9.90650  1.000 36.05811 ? 83  VAL A C     1 
ATOM   639  O O     . VAL A 1 83  ? 14.19632 -29.35099 -10.26584 1.000 39.30583 ? 83  VAL A O     1 
ATOM   640  C CB    . VAL A 1 83  ? 13.75336 -26.70556 -8.20677  1.000 31.53849 ? 83  VAL A CB    1 
ATOM   641  C CG1   . VAL A 1 83  ? 14.55009 -27.74843 -7.43473  1.000 29.22125 ? 83  VAL A CG1   1 
ATOM   642  C CG2   . VAL A 1 83  ? 14.37686 -25.30666 -8.04533  1.000 31.41308 ? 83  VAL A CG2   1 
ATOM   643  N N     . ALA A 1 84  ? 12.04326 -28.92015 -9.74489  1.000 34.90019 ? 84  ALA A N     1 
ATOM   644  C CA    . ALA A 1 84  ? 11.64771 -30.32239 -9.83112  1.000 33.68983 ? 84  ALA A CA    1 
ATOM   645  C C     . ALA A 1 84  ? 11.69279 -30.83180 -11.26434 1.000 39.68959 ? 84  ALA A C     1 
ATOM   646  O O     . ALA A 1 84  ? 12.09032 -31.97966 -11.50418 1.000 46.83183 ? 84  ALA A O     1 
ATOM   647  C CB    . ALA A 1 84  ? 10.24992 -30.51396 -9.24569  1.000 37.89864 ? 84  ALA A CB    1 
ATOM   648  N N     . SER A 1 85  ? 11.27796 -30.00685 -12.23510 1.000 39.23896 ? 85  SER A N     1 
ATOM   649  C CA    . SER A 1 85  ? 11.23578 -30.48539 -13.61384 1.000 34.62325 ? 85  SER A CA    1 
ATOM   650  C C     . SER A 1 85  ? 12.59233 -30.41527 -14.29399 1.000 34.61689 ? 85  SER A C     1 
ATOM   651  O O     . SER A 1 85  ? 12.78032 -31.05713 -15.33379 1.000 34.24458 ? 85  SER A O     1 
ATOM   652  C CB    . SER A 1 85  ? 10.20874 -29.69376 -14.42984 1.000 35.97700 ? 85  SER A CB    1 
ATOM   653  O OG    . SER A 1 85  ? 10.62541 -28.35398 -14.62593 1.000 36.46201 ? 85  SER A OG    1 
ATOM   654  N N     . GLY A 1 86  ? 13.53587 -29.65246 -13.73485 1.000 35.78535 ? 86  GLY A N     1 
ATOM   655  C CA    . GLY A 1 86  ? 14.83867 -29.47413 -14.34650 1.000 36.46900 ? 86  GLY A CA    1 
ATOM   656  C C     . GLY A 1 86  ? 14.86809 -28.45183 -15.45756 1.000 43.19425 ? 86  GLY A C     1 
ATOM   657  O O     . GLY A 1 86  ? 15.89650 -28.29931 -16.12441 1.000 42.31559 ? 86  GLY A O     1 
ATOM   658  N N     . ASN A 1 87  ? 13.76577 -27.74750 -15.67346 1.000 42.57787 ? 87  ASN A N     1 
ATOM   659  C CA    . ASN A 1 87  ? 13.63695 -26.75885 -16.73151 1.000 41.86128 ? 87  ASN A CA    1 
ATOM   660  C C     . ASN A 1 87  ? 13.00352 -25.52616 -16.10803 1.000 45.12165 ? 87  ASN A C     1 
ATOM   661  O O     . ASN A 1 87  ? 11.83097 -25.54968 -15.71587 1.000 54.81746 ? 87  ASN A O     1 
ATOM   662  C CB    A ASN A 1 87  ? 12.79265 -27.31508 -17.87956 0.820 43.66831 ? 87  ASN A CB    1 
ATOM   663  C CB    B ASN A 1 87  ? 12.80890 -27.28631 -17.90584 0.180 43.67272 ? 87  ASN A CB    1 
ATOM   664  C CG    A ASN A 1 87  ? 12.22897 -26.23574 -18.76367 0.820 50.71345 ? 87  ASN A CG    1 
ATOM   665  C CG    B ASN A 1 87  ? 11.61363 -28.09836 -17.45925 0.180 43.37985 ? 87  ASN A CG    1 
ATOM   666  O OD1   A ASN A 1 87  ? 11.06080 -25.85584 -18.62878 0.820 56.11378 ? 87  ASN A OD1   1 
ATOM   667  O OD1   B ASN A 1 87  ? 10.52555 -27.56139 -17.24878 0.180 44.58532 ? 87  ASN A OD1   1 
ATOM   668  N ND2   A ASN A 1 87  ? 13.05405 -25.72556 -19.67624 0.820 49.99714 ? 87  ASN A ND2   1 
ATOM   669  N ND2   B ASN A 1 87  ? 11.80853 -29.40440 -17.31507 0.180 41.07621 ? 87  ASN A ND2   1 
ATOM   670  N N     . LEU A 1 88  ? 13.79131 -24.47519 -15.95014 1.000 36.37871 ? 88  LEU A N     1 
ATOM   671  C CA    . LEU A 1 88  ? 13.31983 -23.24515 -15.32352 1.000 36.57560 ? 88  LEU A CA    1 
ATOM   672  C C     . LEU A 1 88  ? 13.75949 -22.09463 -16.20704 1.000 32.20510 ? 88  LEU A C     1 
ATOM   673  O O     . LEU A 1 88  ? 14.96032 -21.84949 -16.36360 1.000 33.30970 ? 88  LEU A O     1 
ATOM   674  C CB    . LEU A 1 88  ? 13.86290 -23.08644 -13.90382 1.000 36.11934 ? 88  LEU A CB    1 
ATOM   675  C CG    . LEU A 1 88  ? 13.58162 -21.74155 -13.23074 1.000 31.25126 ? 88  LEU A CG    1 
ATOM   676  C CD1   . LEU A 1 88  ? 12.08272 -21.52951 -13.11729 1.000 33.75448 ? 88  LEU A CD1   1 
ATOM   677  C CD2   . LEU A 1 88  ? 14.25722 -21.65994 -11.85975 1.000 27.76284 ? 88  LEU A CD2   1 
ATOM   678  N N     . ASN A 1 89  ? 12.79249 -21.41751 -16.80521 1.000 32.08925 ? 89  ASN A N     1 
ATOM   679  C CA    . ASN A 1 89  ? 13.08428 -20.28824 -17.67166 1.000 31.57091 ? 89  ASN A CA    1 
ATOM   680  C C     . ASN A 1 89  ? 11.80388 -19.49840 -17.84401 1.000 27.70749 ? 89  ASN A C     1 
ATOM   681  O O     . ASN A 1 89  ? 11.00344 -19.81183 -18.72731 1.000 33.36792 ? 89  ASN A O     1 
ATOM   682  C CB    A ASN A 1 89  ? 13.62217 -20.75602 -19.03311 0.910 32.54863 ? 89  ASN A CB    1 
ATOM   683  C CB    B ASN A 1 89  ? 13.63408 -20.75646 -19.02545 0.090 32.22560 ? 89  ASN A CB    1 
ATOM   684  C CG    A ASN A 1 89  ? 14.11639 -19.61230 -19.88802 0.910 26.84047 ? 89  ASN A CG    1 
ATOM   685  C CG    B ASN A 1 89  ? 12.80039 -21.86728 -19.64841 0.090 35.23782 ? 89  ASN A CG    1 
ATOM   686  O OD1   A ASN A 1 89  ? 14.33273 -18.52350 -19.38944 0.910 32.03671 ? 89  ASN A OD1   1 
ATOM   687  O OD1   B ASN A 1 89  ? 13.10130 -23.05044 -19.49173 0.090 39.48969 ? 89  ASN A OD1   1 
ATOM   688  N ND2   A ASN A 1 89  ? 14.30480 -19.85793 -21.18069 0.910 29.97364 ? 89  ASN A ND2   1 
ATOM   689  N ND2   B ASN A 1 89  ? 11.75204 -21.48534 -20.37027 0.090 32.46105 ? 89  ASN A ND2   1 
ATOM   690  N N     . THR A 1 90  ? 11.57788 -18.48306 -17.01971 1.000 28.48744 ? 90  THR A N     1 
ATOM   691  C CA    . THR A 1 90  ? 10.27791 -17.83613 -17.07556 1.000 29.86555 ? 90  THR A CA    1 
ATOM   692  C C     . THR A 1 90  ? 10.43134 -16.38506 -16.65682 1.000 33.38440 ? 90  THR A C     1 
ATOM   693  O O     . THR A 1 90  ? 11.28791 -16.04069 -15.83902 1.000 29.82918 ? 90  THR A O     1 
ATOM   694  C CB    . THR A 1 90  ? 9.23850  -18.57750 -16.20376 1.000 32.00635 ? 90  THR A CB    1 
ATOM   695  O OG1   . THR A 1 90  ? 7.93798  -18.03941 -16.45436 1.000 42.31070 ? 90  THR A OG1   1 
ATOM   696  C CG2   . THR A 1 90  ? 9.55630  -18.45908 -14.71177 1.000 30.03192 ? 90  THR A CG2   1 
ATOM   697  N N     . MET A 1 91  ? 9.59498  -15.54114 -17.23969 1.000 30.17452 ? 91  MET A N     1 
ATOM   698  C CA    . MET A 1 91  ? 9.62497  -14.10790 -16.99906 1.000 31.46711 ? 91  MET A CA    1 
ATOM   699  C C     . MET A 1 91  ? 8.22028  -13.64791 -16.64926 1.000 33.62489 ? 91  MET A C     1 
ATOM   700  O O     . MET A 1 91  ? 7.24716  -14.11107 -17.24640 1.000 32.52877 ? 91  MET A O     1 
ATOM   701  C CB    . MET A 1 91  ? 10.12766 -13.36456 -18.23307 1.000 36.04980 ? 91  MET A CB    1 
ATOM   702  C CG    . MET A 1 91  ? 11.05094 -12.19343 -17.97114 1.000 41.76292 ? 91  MET A CG    1 
ATOM   703  S SD    . MET A 1 91  ? 11.68177 -11.69393 -19.58863 1.000 52.23681 ? 91  MET A SD    1 
ATOM   704  C CE    . MET A 1 91  ? 12.57897 -13.17467 -20.04612 1.000 43.68728 ? 91  MET A CE    1 
ATOM   705  N N     . PHE A 1 92  ? 8.11531  -12.76739 -15.66089 1.000 26.98145 ? 92  PHE A N     1 
ATOM   706  C CA    . PHE A 1 92  ? 6.82196  -12.26879 -15.21960 1.000 29.69146 ? 92  PHE A CA    1 
ATOM   707  C C     . PHE A 1 92  ? 7.05494  -10.98031 -14.44639 1.000 31.82441 ? 92  PHE A C     1 
ATOM   708  O O     . PHE A 1 92  ? 8.17450  -10.68955 -14.00624 1.000 31.23957 ? 92  PHE A O     1 
ATOM   709  C CB    . PHE A 1 92  ? 6.07379  -13.30270 -14.35836 1.000 32.96844 ? 92  PHE A CB    1 
ATOM   710  C CG    . PHE A 1 92  ? 6.85622  -13.80236 -13.16029 1.000 32.14579 ? 92  PHE A CG    1 
ATOM   711  C CD1   . PHE A 1 92  ? 7.66189  -14.93071 -13.25381 1.000 37.47096 ? 92  PHE A CD1   1 
ATOM   712  C CD2   . PHE A 1 92  ? 6.75289  -13.16874 -11.93324 1.000 25.30608 ? 92  PHE A CD2   1 
ATOM   713  C CE1   . PHE A 1 92  ? 8.36736  -15.39972 -12.14257 1.000 37.54115 ? 92  PHE A CE1   1 
ATOM   714  C CE2   . PHE A 1 92  ? 7.45624  -13.62999 -10.82202 1.000 29.43562 ? 92  PHE A CE2   1 
ATOM   715  C CZ    . PHE A 1 92  ? 8.26386  -14.74483 -10.92564 1.000 31.98447 ? 92  PHE A CZ    1 
ATOM   716  N N     . GLU A 1 93  ? 5.99030  -10.20369 -14.30034 1.000 29.77561 ? 93  GLU A N     1 
ATOM   717  C CA    . GLU A 1 93  ? 6.04536  -9.00280  -13.48158 1.000 25.57808 ? 93  GLU A CA    1 
ATOM   718  C C     . GLU A 1 93  ? 5.55889  -9.31032  -12.07108 1.000 30.65541 ? 93  GLU A C     1 
ATOM   719  O O     . GLU A 1 93  ? 4.78075  -10.24182 -11.84484 1.000 26.57778 ? 93  GLU A O     1 
ATOM   720  C CB    . GLU A 1 93  ? 5.20917  -7.87950  -14.09753 1.000 31.91961 ? 93  GLU A CB    1 
ATOM   721  C CG    . GLU A 1 93  ? 5.75355  -7.45615  -15.44582 1.000 43.12912 ? 93  GLU A CG    1 
ATOM   722  C CD    . GLU A 1 93  ? 5.07278  -6.22582  -16.01643 1.000 58.19848 ? 93  GLU A CD    1 
ATOM   723  O OE1   . GLU A 1 93  ? 4.06662  -5.75054  -15.42541 1.000 64.28777 ? 93  GLU A OE1   1 
ATOM   724  O OE2   . GLU A 1 93  ? 5.55974  -5.72388  -17.06361 1.000 51.67137 ? 93  GLU A OE2   1 
ATOM   725  N N     . TYR A 1 94  ? 6.03849  -8.51556  -11.11938 1.000 33.73082 ? 94  TYR A N     1 
ATOM   726  C CA    . TYR A 1 94  ? 5.76781  -8.75724  -9.71246  1.000 28.74273 ? 94  TYR A CA    1 
ATOM   727  C C     . TYR A 1 94  ? 5.91728  -7.43529  -8.98379  1.000 29.32745 ? 94  TYR A C     1 
ATOM   728  O O     . TYR A 1 94  ? 6.46635  -6.47428  -9.52907  1.000 29.48388 ? 94  TYR A O     1 
ATOM   729  C CB    . TYR A 1 94  ? 6.72068  -9.80947  -9.14819  1.000 24.97254 ? 94  TYR A CB    1 
ATOM   730  C CG    . TYR A 1 94  ? 6.10875  -10.65383 -8.06742  1.000 24.24898 ? 94  TYR A CG    1 
ATOM   731  C CD1   . TYR A 1 94  ? 5.17118  -11.63585 -8.37614  1.000 27.63177 ? 94  TYR A CD1   1 
ATOM   732  C CD2   . TYR A 1 94  ? 6.45954  -10.47167 -6.73490  1.000 27.87099 ? 94  TYR A CD2   1 
ATOM   733  C CE1   . TYR A 1 94  ? 4.59672  -12.41694 -7.38660  1.000 27.43520 ? 94  TYR A CE1   1 
ATOM   734  C CE2   . TYR A 1 94  ? 5.89691  -11.25716 -5.73500  1.000 29.79224 ? 94  TYR A CE2   1 
ATOM   735  C CZ    . TYR A 1 94  ? 4.96551  -12.22584 -6.07499  1.000 25.40905 ? 94  TYR A CZ    1 
ATOM   736  O OH    . TYR A 1 94  ? 4.40399  -13.00083 -5.09412  1.000 31.38243 ? 94  TYR A OH    1 
ATOM   737  N N     . THR A 1 95  ? 5.39226  -7.38416  -7.75974  1.000 25.40790 ? 95  THR A N     1 
ATOM   738  C CA    . THR A 1 95  ? 5.54401  -6.21929  -6.89170  1.000 31.22703 ? 95  THR A CA    1 
ATOM   739  C C     . THR A 1 95  ? 6.26732  -6.63919  -5.61954  1.000 27.46705 ? 95  THR A C     1 
ATOM   740  O O     . THR A 1 95  ? 5.80334  -7.53299  -4.90481  1.000 29.89447 ? 95  THR A O     1 
ATOM   741  C CB    . THR A 1 95  ? 4.19059  -5.58544  -6.55821  1.000 30.28502 ? 95  THR A CB    1 
ATOM   742  O OG1   . THR A 1 95  ? 3.57430  -5.12668  -7.76079  1.000 34.74466 ? 95  THR A OG1   1 
ATOM   743  C CG2   . THR A 1 95  ? 4.37161  -4.39025  -5.64142  1.000 31.05311 ? 95  THR A CG2   1 
ATOM   744  N N     . PHE A 1 96  ? 7.40362  -6.00438  -5.35022  1.000 26.93676 ? 96  PHE A N     1 
ATOM   745  C CA    . PHE A 1 96  ? 8.14208  -6.19571  -4.10653  1.000 29.60306 ? 96  PHE A CA    1 
ATOM   746  C C     . PHE A 1 96  ? 7.65435  -5.16430  -3.09272  1.000 32.06600 ? 96  PHE A C     1 
ATOM   747  O O     . PHE A 1 96  ? 7.81613  -3.95436  -3.30885  1.000 29.41419 ? 96  PHE A O     1 
ATOM   748  C CB    . PHE A 1 96  ? 9.64628  -6.02756  -4.33218  1.000 25.33792 ? 96  PHE A CB    1 
ATOM   749  C CG    . PHE A 1 96  ? 10.28831 -7.11308  -5.17520  1.000 29.64181 ? 96  PHE A CG    1 
ATOM   750  C CD1   . PHE A 1 96  ? 9.65931  -8.32282  -5.40251  1.000 25.40802 ? 96  PHE A CD1   1 
ATOM   751  C CD2   . PHE A 1 96  ? 11.55586 -6.91245  -5.71789  1.000 26.38124 ? 96  PHE A CD2   1 
ATOM   752  C CE1   . PHE A 1 96  ? 10.28145 -9.31251  -6.16649  1.000 25.21389 ? 96  PHE A CE1   1 
ATOM   753  C CE2   . PHE A 1 96  ? 12.18553 -7.89583  -6.47553  1.000 28.44668 ? 96  PHE A CE2   1 
ATOM   754  C CZ    . PHE A 1 96  ? 11.54975 -9.09687  -6.69954  1.000 24.95006 ? 96  PHE A CZ    1 
ATOM   755  N N     . ASP A 1 97  ? 7.06644  -5.62957  -1.97853  1.000 31.34513 ? 97  ASP A N     1 
ATOM   756  C CA    . ASP A 1 97  ? 6.51780  -4.65729  -1.03806  1.000 27.91059 ? 97  ASP A CA    1 
ATOM   757  C C     . ASP A 1 97  ? 6.76149  -4.98350  0.43501   1.000 33.49353 ? 97  ASP A C     1 
ATOM   758  O O     . ASP A 1 97  ? 6.03070  -4.46758  1.29189   1.000 30.91462 ? 97  ASP A O     1 
ATOM   759  C CB    . ASP A 1 97  ? 5.00946  -4.48998  -1.25716  1.000 29.29870 ? 97  ASP A CB    1 
ATOM   760  C CG    . ASP A 1 97  ? 4.25643  -5.78660  -1.07774  1.000 32.40233 ? 97  ASP A CG    1 
ATOM   761  O OD1   . ASP A 1 97  ? 4.91015  -6.83316  -0.87399  1.000 31.97009 ? 97  ASP A OD1   1 
ATOM   762  O OD2   . ASP A 1 97  ? 3.01552  -5.75583  -1.13112  1.000 37.73978 ? 97  ASP A OD2   1 
ATOM   763  N N     . TYR A 1 98  ? 7.76296  -5.79401  0.77112   1.000 30.14571 ? 98  TYR A N     1 
ATOM   764  C CA    . TYR A 1 98  ? 8.03230  -6.15884  2.16300   1.000 32.25647 ? 98  TYR A CA    1 
ATOM   765  C C     . TYR A 1 98  ? 9.12073  -5.25062  2.72529   1.000 31.68899 ? 98  TYR A C     1 
ATOM   766  O O     . TYR A 1 98  ? 10.28101 -5.33390  2.30920   1.000 28.96676 ? 98  TYR A O     1 
ATOM   767  C CB    . TYR A 1 98  ? 8.45088  -7.62471  2.27947   1.000 29.46219 ? 98  TYR A CB    1 
ATOM   768  C CG    . TYR A 1 98  ? 8.72318  -8.06205  3.70530   1.000 36.06716 ? 98  TYR A CG    1 
ATOM   769  C CD1   . TYR A 1 98  ? 7.70453  -8.07286  4.64987   1.000 26.60302 ? 98  TYR A CD1   1 
ATOM   770  C CD2   . TYR A 1 98  ? 9.99110  -8.45941  4.10801   1.000 38.80287 ? 98  TYR A CD2   1 
ATOM   771  C CE1   . TYR A 1 98  ? 7.93155  -8.46742  5.95538   1.000 31.12979 ? 98  TYR A CE1   1 
ATOM   772  C CE2   . TYR A 1 98  ? 10.23407 -8.84586  5.42833   1.000 36.08677 ? 98  TYR A CE2   1 
ATOM   773  C CZ    . TYR A 1 98  ? 9.19781  -8.84946  6.33809   1.000 33.32059 ? 98  TYR A CZ    1 
ATOM   774  O OH    . TYR A 1 98  ? 9.41568  -9.24057  7.63647   1.000 38.56217 ? 98  TYR A OH    1 
ATOM   775  N N     . GLN A 1 99  ? 8.75144  -4.41315  3.69198   1.000 34.62212 ? 99  GLN A N     1 
ATOM   776  C CA    . GLN A 1 99  ? 9.68611  -3.49517  4.34227   1.000 34.99886 ? 99  GLN A CA    1 
ATOM   777  C C     . GLN A 1 99  ? 10.33744 -2.56000  3.32581   1.000 41.15035 ? 99  GLN A C     1 
ATOM   778  O O     . GLN A 1 99  ? 11.53785 -2.27450  3.38421   1.000 38.99091 ? 99  GLN A O     1 
ATOM   779  C CB    . GLN A 1 99  ? 10.73840 -4.26255  5.14438   1.000 41.34414 ? 99  GLN A CB    1 
ATOM   780  C CG    . GLN A 1 99  ? 10.19703 -4.88268  6.42613   1.000 38.08041 ? 99  GLN A CG    1 
ATOM   781  C CD    . GLN A 1 99  ? 11.25952 -5.65140  7.17835   1.000 55.00434 ? 99  GLN A CD    1 
ATOM   782  O OE1   . GLN A 1 99  ? 12.37972 -5.84145  6.68607   1.000 54.80161 ? 99  GLN A OE1   1 
ATOM   783  N NE2   . GLN A 1 99  ? 10.92036 -6.09809  8.38236   1.000 71.96559 ? 99  GLN A NE2   1 
ATOM   784  N N     . MET A 1 100 ? 9.53352  -2.07773  2.38420   1.000 30.43946 ? 100 MET A N     1 
ATOM   785  C CA    . MET A 1 100 ? 10.02067 -1.20206  1.32872   1.000 34.66260 ? 100 MET A CA    1 
ATOM   786  C C     . MET A 1 100 ? 8.81413  -0.58261  0.65100   1.000 38.25254 ? 100 MET A C     1 
ATOM   787  O O     . MET A 1 100 ? 7.71562  -1.13875  0.70753   1.000 40.08923 ? 100 MET A O     1 
ATOM   788  C CB    . MET A 1 100 ? 10.87518 -1.96470  0.30717   1.000 30.04769 ? 100 MET A CB    1 
ATOM   789  C CG    . MET A 1 100 ? 10.12506 -3.08381  -0.37048  1.000 30.48150 ? 100 MET A CG    1 
ATOM   790  S SD    . MET A 1 100 ? 11.20453 -4.12440  -1.32716  1.000 33.45442 ? 100 MET A SD    1 
ATOM   791  C CE    . MET A 1 100 ? 11.47701 -3.05053  -2.73960  1.000 30.61178 ? 100 MET A CE    1 
ATOM   792  N N     . THR A 1 101 ? 9.01766  0.59135   0.05652   1.000 38.84504 ? 101 THR A N     1 
ATOM   793  C CA    . THR A 1 101 ? 8.00923  1.18193   -0.80443  1.000 33.26585 ? 101 THR A CA    1 
ATOM   794  C C     . THR A 1 101 ? 7.61078  0.16750   -1.87986  1.000 35.05936 ? 101 THR A C     1 
ATOM   795  O O     . THR A 1 101 ? 8.50307  -0.43893  -2.49547  1.000 32.45806 ? 101 THR A O     1 
ATOM   796  C CB    . THR A 1 101 ? 8.56585  2.45264   -1.44955  1.000 38.00721 ? 101 THR A CB    1 
ATOM   797  O OG1   . THR A 1 101 ? 8.91002  3.37993   -0.41452  1.000 46.22701 ? 101 THR A OG1   1 
ATOM   798  C CG2   . THR A 1 101 ? 7.55042  3.10078   -2.38565  1.000 36.85844 ? 101 THR A CG2   1 
ATOM   799  N N     . PRO A 1 102 ? 6.32227  -0.06050  -2.11451  1.000 33.19410 ? 102 PRO A N     1 
ATOM   800  C CA    . PRO A 1 102 ? 5.93533  -1.05169  -3.13201  1.000 33.48941 ? 102 PRO A CA    1 
ATOM   801  C C     . PRO A 1 102 ? 6.57435  -0.71507  -4.47520  1.000 36.24755 ? 102 PRO A C     1 
ATOM   802  O O     . PRO A 1 102 ? 6.46141  0.41004   -4.97631  1.000 33.82676 ? 102 PRO A O     1 
ATOM   803  C CB    . PRO A 1 102 ? 4.40965  -0.94514  -3.17891  1.000 33.22537 ? 102 PRO A CB    1 
ATOM   804  C CG    . PRO A 1 102 ? 4.02315  -0.29035  -1.88979  1.000 37.76017 ? 102 PRO A CG    1 
ATOM   805  C CD    . PRO A 1 102 ? 5.15053  0.63733   -1.55168  1.000 39.86132 ? 102 PRO A CD    1 
ATOM   806  N N     . THR A 1 103 ? 7.27442  -1.69219  -5.04420  1.000 32.18781 ? 103 THR A N     1 
ATOM   807  C CA    . THR A 1 103 ? 8.08681  -1.46917  -6.23716  1.000 31.63148 ? 103 THR A CA    1 
ATOM   808  C C     . THR A 1 103 ? 7.78197  -2.52764  -7.28114  1.000 31.45981 ? 103 THR A C     1 
ATOM   809  O O     . THR A 1 103 ? 7.98084  -3.71963  -7.03235  1.000 28.79936 ? 103 THR A O     1 
ATOM   810  C CB    . THR A 1 103 ? 9.57680  -1.48440  -5.90061  1.000 34.13762 ? 103 THR A CB    1 
ATOM   811  O OG1   . THR A 1 103 ? 9.85900  -0.42549  -4.97747  1.000 36.70918 ? 103 THR A OG1   1 
ATOM   812  C CG2   . THR A 1 103 ? 10.39393 -1.29002  -7.16478  1.000 34.28990 ? 103 THR A CG2   1 
ATOM   813  N N     . LYS A 1 104 ? 7.31926  -2.08624  -8.45154  1.000 32.40449 ? 104 LYS A N     1 
ATOM   814  C CA    . LYS A 1 104 ? 7.01332  -2.99360  -9.55073  1.000 33.99882 ? 104 LYS A CA    1 
ATOM   815  C C     . LYS A 1 104 ? 8.29587  -3.39557  -10.28097 1.000 30.09937 ? 104 LYS A C     1 
ATOM   816  O O     . LYS A 1 104 ? 9.14752  -2.54887  -10.58246 1.000 27.34882 ? 104 LYS A O     1 
ATOM   817  C CB    . LYS A 1 104 ? 6.01808  -2.33442  -10.51349 1.000 41.61786 ? 104 LYS A CB    1 
ATOM   818  C CG    . LYS A 1 104 ? 5.18277  -3.33314  -11.32673 1.000 56.47702 ? 104 LYS A CG    1 
ATOM   819  C CD    . LYS A 1 104 ? 4.07843  -2.65286  -12.13295 1.000 73.07651 ? 104 LYS A CD    1 
ATOM   820  C CE    . LYS A 1 104 ? 4.21484  -2.99329  -13.63788 1.000 80.01865 ? 104 LYS A CE    1 
ATOM   821  N NZ    . LYS A 1 104 ? 3.08746  -2.42385  -14.45729 1.000 80.72590 ? 104 LYS A NZ    1 
ATOM   822  N N     . VAL A 1 105 ? 8.43918  -4.69306  -10.56956 1.000 24.41232 ? 105 VAL A N     1 
ATOM   823  C CA    . VAL A 1 105 ? 9.65080  -5.20709  -11.20245 1.000 29.90163 ? 105 VAL A CA    1 
ATOM   824  C C     . VAL A 1 105 ? 9.29086  -6.23957  -12.26476 1.000 29.02275 ? 105 VAL A C     1 
ATOM   825  O O     . VAL A 1 105 ? 8.19628  -6.80806  -12.27528 1.000 30.35125 ? 105 VAL A O     1 
ATOM   826  C CB    . VAL A 1 105 ? 10.62809 -5.84390  -10.18795 1.000 25.31400 ? 105 VAL A CB    1 
ATOM   827  C CG1   . VAL A 1 105 ? 11.11138 -4.81247  -9.16953  1.000 28.40540 ? 105 VAL A CG1   1 
ATOM   828  C CG2   . VAL A 1 105 ? 9.97951  -7.05744  -9.49527  1.000 27.24803 ? 105 VAL A CG2   1 
ATOM   829  N N     . LYS A 1 106 ? 10.23351 -6.47690  -13.17019 1.000 27.95584 ? 106 LYS A N     1 
ATOM   830  C CA    . LYS A 1 106 ? 10.16173 -7.62449  -14.06269 1.000 27.38906 ? 106 LYS A CA    1 
ATOM   831  C C     . LYS A 1 106 ? 11.15986 -8.66224  -13.57279 1.000 27.60721 ? 106 LYS A C     1 
ATOM   832  O O     . LYS A 1 106 ? 12.30592 -8.32934  -13.25233 1.000 26.23965 ? 106 LYS A O     1 
ATOM   833  C CB    . LYS A 1 106 ? 10.44547 -7.24137  -15.51760 1.000 32.47831 ? 106 LYS A CB    1 
ATOM   834  C CG    . LYS A 1 106 ? 10.39069 -8.45175  -16.44600 1.000 43.00153 ? 106 LYS A CG    1 
ATOM   835  C CD    . LYS A 1 106 ? 10.32908 -8.04441  -17.90476 1.000 53.90018 ? 106 LYS A CD    1 
ATOM   836  C CE    . LYS A 1 106 ? 9.02064  -7.35247  -18.22297 1.000 54.08927 ? 106 LYS A CE    1 
ATOM   837  N NZ    . LYS A 1 106 ? 9.10178  -6.64767  -19.53386 1.000 55.39936 ? 106 LYS A NZ    1 
ATOM   838  N N     . VAL A 1 107 ? 10.71365 -9.90715  -13.47297 1.000 26.67853 ? 107 VAL A N     1 
ATOM   839  C CA    . VAL A 1 107 ? 11.52639 -10.97867 -12.91824 1.000 23.54614 ? 107 VAL A CA    1 
ATOM   840  C C     . VAL A 1 107 ? 11.79277 -12.01209 -14.00028 1.000 26.49695 ? 107 VAL A C     1 
ATOM   841  O O     . VAL A 1 107 ? 10.88403 -12.39385 -14.74692 1.000 28.57459 ? 107 VAL A O     1 
ATOM   842  C CB    . VAL A 1 107 ? 10.83933 -11.63630 -11.70707 1.000 26.01916 ? 107 VAL A CB    1 
ATOM   843  C CG1   . VAL A 1 107 ? 11.69274 -12.79262 -11.19225 1.000 25.07644 ? 107 VAL A CG1   1 
ATOM   844  C CG2   . VAL A 1 107 ? 10.60992 -10.61171 -10.61691 1.000 28.35243 ? 107 VAL A CG2   1 
ATOM   845  N N     . HIS A 1 108 ? 13.04262 -12.46629 -14.08268 1.000 24.16923 ? 108 HIS A N     1 
ATOM   846  C CA    . HIS A 1 108 ? 13.43869 -13.56616 -14.95764 1.000 25.86559 ? 108 HIS A CA    1 
ATOM   847  C C     . HIS A 1 108 ? 14.11725 -14.62031 -14.09209 1.000 26.31381 ? 108 HIS A C     1 
ATOM   848  O O     . HIS A 1 108 ? 15.18211 -14.36474 -13.51836 1.000 29.09313 ? 108 HIS A O     1 
ATOM   849  C CB    . HIS A 1 108 ? 14.38011 -13.09091 -16.05812 1.000 28.46259 ? 108 HIS A CB    1 
ATOM   850  C CG    . HIS A 1 108 ? 14.76650 -14.16483 -17.02625 1.000 29.56012 ? 108 HIS A CG    1 
ATOM   851  N ND1   . HIS A 1 108 ? 15.90059 -14.08959 -17.80779 1.000 31.98537 ? 108 HIS A ND1   1 
ATOM   852  C CD2   . HIS A 1 108 ? 14.16684 -15.33650 -17.35017 1.000 26.62613 ? 108 HIS A CD2   1 
ATOM   853  C CE1   . HIS A 1 108 ? 15.97999 -15.16358 -18.57331 1.000 29.54814 ? 108 HIS A CE1   1 
ATOM   854  N NE2   . HIS A 1 108 ? 14.94137 -15.93826 -18.31318 1.000 30.24537 ? 108 HIS A NE2   1 
ATOM   855  N N     . MET A 1 109 ? 13.50391 -15.79382 -13.98241 1.000 25.73618 ? 109 MET A N     1 
ATOM   856  C CA    . MET A 1 109 ? 14.10585 -16.92797 -13.29079 1.000 26.47810 ? 109 MET A CA    1 
ATOM   857  C C     . MET A 1 109 ? 14.63935 -17.93243 -14.30762 1.000 25.82699 ? 109 MET A C     1 
ATOM   858  O O     . MET A 1 109 ? 13.93073 -18.30335 -15.25025 1.000 26.89490 ? 109 MET A O     1 
ATOM   859  C CB    . MET A 1 109 ? 13.09026 -17.60480 -12.36771 1.000 27.11069 ? 109 MET A CB    1 
ATOM   860  C CG    . MET A 1 109 ? 12.78473 -16.83566 -11.09353 1.000 37.39031 ? 109 MET A CG    1 
ATOM   861  S SD    . MET A 1 109 ? 11.81092 -17.85380 -9.95380  1.000 44.12994 ? 109 MET A SD    1 
ATOM   862  C CE    . MET A 1 109 ? 10.40381 -18.24986 -10.98633 1.000 30.69550 ? 109 MET A CE    1 
ATOM   863  N N     . LYS A 1 110 ? 15.87525 -18.39100 -14.10410 1.000 23.91787 ? 110 LYS A N     1 
ATOM   864  C CA    . LYS A 1 110 ? 16.47655 -19.33229 -15.03690 1.000 25.98289 ? 110 LYS A CA    1 
ATOM   865  C C     . LYS A 1 110 ? 17.45741 -20.23081 -14.30164 1.000 26.54603 ? 110 LYS A C     1 
ATOM   866  O O     . LYS A 1 110 ? 18.16493 -19.78112 -13.39809 1.000 29.47212 ? 110 LYS A O     1 
ATOM   867  C CB    . LYS A 1 110 ? 17.18030 -18.59526 -16.19156 1.000 20.87565 ? 110 LYS A CB    1 
ATOM   868  C CG    . LYS A 1 110 ? 17.60806 -19.50962 -17.35540 1.000 27.61432 ? 110 LYS A CG    1 
ATOM   869  C CD    . LYS A 1 110 ? 17.93367 -18.72793 -18.60535 1.000 33.86840 ? 110 LYS A CD    1 
ATOM   870  C CE    . LYS A 1 110 ? 18.15900 -19.67800 -19.77319 1.000 32.28828 ? 110 LYS A CE    1 
ATOM   871  N NZ    . LYS A 1 110 ? 18.57924 -18.91693 -20.98358 1.000 28.82883 ? 110 LYS A NZ    1 
ATOM   872  N N     . LYS A 1 111 ? 17.49479 -21.50095 -14.70332 1.000 30.07385 ? 111 LYS A N     1 
ATOM   873  C CA    . LYS A 1 111 ? 18.44785 -22.45699 -14.14781 1.000 26.58969 ? 111 LYS A CA    1 
ATOM   874  C C     . LYS A 1 111 ? 19.87620 -22.08031 -14.52729 1.000 28.02655 ? 111 LYS A C     1 
ATOM   875  O O     . LYS A 1 111 ? 20.13582 -21.62123 -15.64268 1.000 30.73702 ? 111 LYS A O     1 
ATOM   876  C CB    . LYS A 1 111 ? 18.12743 -23.86166 -14.66260 1.000 30.84603 ? 111 LYS A CB    1 
ATOM   877  C CG    . LYS A 1 111 ? 18.89384 -24.98295 -13.98413 1.000 35.88983 ? 111 LYS A CG    1 
ATOM   878  C CD    . LYS A 1 111 ? 18.44187 -26.35945 -14.50448 1.000 45.13660 ? 111 LYS A CD    1 
ATOM   879  C CE    . LYS A 1 111 ? 18.51719 -26.44261 -16.03296 1.000 43.15336 ? 111 LYS A CE    1 
ATOM   880  N NZ    . LYS A 1 111 ? 18.47276 -27.87004 -16.52919 1.000 50.21899 ? 111 LYS A NZ    1 
ATOM   881  N N     . ALA A 1 112 ? 20.81050 -22.28073 -13.59487 1.000 27.74896 ? 112 ALA A N     1 
ATOM   882  C CA    . ALA A 1 112 ? 22.21736 -22.01124 -13.87887 1.000 31.96080 ? 112 ALA A CA    1 
ATOM   883  C C     . ALA A 1 112 ? 22.77990 -23.05274 -14.84732 1.000 38.91040 ? 112 ALA A C     1 
ATOM   884  O O     . ALA A 1 112 ? 22.22979 -24.14653 -15.01434 1.000 33.74264 ? 112 ALA A O     1 
ATOM   885  C CB    . ALA A 1 112 ? 23.03646 -21.99554 -12.58680 1.000 29.44572 ? 112 ALA A CB    1 
ATOM   886  N N     . LEU A 1 113 ? 23.90345 -22.70221 -15.48746 1.000 38.42620 ? 113 LEU A N     1 
ATOM   887  C CA    . LEU A 1 113 ? 24.47811 -23.58028 -16.50436 1.000 36.52133 ? 113 LEU A CA    1 
ATOM   888  C C     . LEU A 1 113 ? 24.74801 -24.97189 -15.94567 1.000 37.56741 ? 113 LEU A C     1 
ATOM   889  O O     . LEU A 1 113 ? 24.47243 -25.97756 -16.60970 1.000 40.51872 ? 113 LEU A O     1 
ATOM   890  C CB    . LEU A 1 113 ? 25.76176 -22.95945 -17.07154 1.000 35.26960 ? 113 LEU A CB    1 
ATOM   891  C CG    . LEU A 1 113 ? 26.50976 -23.71368 -18.17270 1.000 37.56822 ? 113 LEU A CG    1 
ATOM   892  C CD1   . LEU A 1 113 ? 25.60513 -24.05074 -19.35385 1.000 38.21663 ? 113 LEU A CD1   1 
ATOM   893  C CD2   . LEU A 1 113 ? 27.70345 -22.88949 -18.62858 1.000 37.61478 ? 113 LEU A CD2   1 
ATOM   894  N N     . SER A 1 114 ? 25.26386 -25.05362 -14.71672 1.000 40.50282 ? 114 SER A N     1 
ATOM   895  C CA    . SER A 1 114 ? 25.57143 -26.35084 -14.12100 1.000 44.54423 ? 114 SER A CA    1 
ATOM   896  C C     . SER A 1 114 ? 24.32109 -27.11635 -13.69597 1.000 49.31953 ? 114 SER A C     1 
ATOM   897  O O     . SER A 1 114 ? 24.42693 -28.29647 -13.34834 1.000 51.28313 ? 114 SER A O     1 
ATOM   898  C CB    . SER A 1 114 ? 26.50362 -26.17046 -12.91781 1.000 42.54447 ? 114 SER A CB    1 
ATOM   899  O OG    . SER A 1 114 ? 25.93665 -25.26589 -11.97990 1.000 50.94333 ? 114 SER A OG    1 
ATOM   900  N N     . GLY A 1 115 ? 23.15240 -26.47819 -13.70147 1.000 40.50943 ? 115 GLY A N     1 
ATOM   901  C CA    . GLY A 1 115 ? 21.90062 -27.14647 -13.41550 1.000 46.17402 ? 115 GLY A CA    1 
ATOM   902  C C     . GLY A 1 115 ? 21.61403 -27.43173 -11.95551 1.000 47.18394 ? 115 GLY A C     1 
ATOM   903  O O     . GLY A 1 115 ? 20.58155 -28.04719 -11.65893 1.000 60.53001 ? 115 GLY A O     1 
ATOM   904  N N     . ASP A 1 116 ? 22.47452 -27.00374 -11.03143 1.000 40.08579 ? 116 ASP A N     1 
ATOM   905  C CA    . ASP A 1 116 ? 22.26984 -27.27300 -9.61470  1.000 44.50412 ? 116 ASP A CA    1 
ATOM   906  C C     . ASP A 1 116 ? 22.03122 -26.01655 -8.78891  1.000 45.93011 ? 116 ASP A C     1 
ATOM   907  O O     . ASP A 1 116 ? 21.93055 -26.11252 -7.55971  1.000 42.21262 ? 116 ASP A O     1 
ATOM   908  C CB    . ASP A 1 116 ? 23.46736 -28.04557 -9.04353  1.000 48.12602 ? 116 ASP A CB    1 
ATOM   909  C CG    . ASP A 1 116 ? 24.78833 -27.33981 -9.29667  1.000 69.43424 ? 116 ASP A CG    1 
ATOM   910  O OD1   . ASP A 1 116 ? 24.82090 -26.42650 -10.15937 1.000 70.70197 ? 116 ASP A OD1   1 
ATOM   911  O OD2   . ASP A 1 116 ? 25.79646 -27.70342 -8.64560  1.000 76.41062 ? 116 ASP A OD2   1 
ATOM   912  N N     . SER A 1 117 ? 21.96507 -24.84485 -9.41687  1.000 37.97987 ? 117 SER A N     1 
ATOM   913  C CA    . SER A 1 117 ? 21.54014 -23.61776 -8.75517  1.000 27.93965 ? 117 SER A CA    1 
ATOM   914  C C     . SER A 1 117 ? 20.71496 -22.82493 -9.75469  1.000 29.82152 ? 117 SER A C     1 
ATOM   915  O O     . SER A 1 117 ? 20.57760 -23.21131 -10.91863 1.000 31.78068 ? 117 SER A O     1 
ATOM   916  C CB    . SER A 1 117 ? 22.72533 -22.79564 -8.23946  1.000 34.39730 ? 117 SER A CB    1 
ATOM   917  O OG    . SER A 1 117 ? 23.58892 -22.42866 -9.30040  1.000 39.80513 ? 117 SER A OG    1 
ATOM   918  N N     . TYR A 1 118 ? 20.14598 -21.71514 -9.29453  1.000 26.97348 ? 118 TYR A N     1 
ATOM   919  C CA    . TYR A 1 118 ? 19.10048 -21.03602 -10.04745 1.000 27.57553 ? 118 TYR A CA    1 
ATOM   920  C C     . TYR A 1 118 ? 19.24969 -19.52921 -9.89158  1.000 28.18877 ? 118 TYR A C     1 
ATOM   921  O O     . TYR A 1 118 ? 19.53331 -19.03154 -8.79803  1.000 30.87835 ? 118 TYR A O     1 
ATOM   922  C CB    . TYR A 1 118 ? 17.71275 -21.51635 -9.57694  1.000 29.99657 ? 118 TYR A CB    1 
ATOM   923  C CG    . TYR A 1 118 ? 17.64954 -23.03189 -9.53302  1.000 29.42034 ? 118 TYR A CG    1 
ATOM   924  C CD1   . TYR A 1 118 ? 18.05332 -23.74236 -8.39194  1.000 31.53796 ? 118 TYR A CD1   1 
ATOM   925  C CD2   . TYR A 1 118 ? 17.24693 -23.76049 -10.64457 1.000 33.62694 ? 118 TYR A CD2   1 
ATOM   926  C CE1   . TYR A 1 118 ? 18.04929 -25.14573 -8.36232  1.000 29.09960 ? 118 TYR A CE1   1 
ATOM   927  C CE2   . TYR A 1 118 ? 17.23081 -25.16403 -10.61901 1.000 32.34652 ? 118 TYR A CE2   1 
ATOM   928  C CZ    . TYR A 1 118 ? 17.63090 -25.84321 -9.47993  1.000 32.91730 ? 118 TYR A CZ    1 
ATOM   929  O OH    . TYR A 1 118 ? 17.61577 -27.22263 -9.47639  1.000 35.94478 ? 118 TYR A OH    1 
ATOM   930  N N     . TRP A 1 119 ? 19.06161 -18.80446 -10.98718 1.000 26.00374 ? 119 TRP A N     1 
ATOM   931  C CA    . TRP A 1 119 ? 19.17201 -17.35317 -10.97536 1.000 28.32562 ? 119 TRP A CA    1 
ATOM   932  C C     . TRP A 1 119 ? 17.78819 -16.71473 -10.90876 1.000 26.82718 ? 119 TRP A C     1 
ATOM   933  O O     . TRP A 1 119 ? 16.83574 -17.20129 -11.52672 1.000 25.51049 ? 119 TRP A O     1 
ATOM   934  C CB    . TRP A 1 119 ? 19.90191 -16.84978 -12.22305 1.000 30.14092 ? 119 TRP A CB    1 
ATOM   935  C CG    . TRP A 1 119 ? 21.34263 -17.24703 -12.31923 1.000 31.03516 ? 119 TRP A CG    1 
ATOM   936  C CD1   . TRP A 1 119 ? 21.85853 -18.29001 -13.03447 1.000 28.70089 ? 119 TRP A CD1   1 
ATOM   937  C CD2   . TRP A 1 119 ? 22.46093 -16.59866 -11.68754 1.000 26.92623 ? 119 TRP A CD2   1 
ATOM   938  N NE1   . TRP A 1 119 ? 23.22581 -18.33958 -12.87997 1.000 36.01481 ? 119 TRP A NE1   1 
ATOM   939  C CE2   . TRP A 1 119 ? 23.62108 -17.31531 -12.05637 1.000 31.36321 ? 119 TRP A CE2   1 
ATOM   940  C CE3   . TRP A 1 119 ? 22.59164 -15.49180 -10.83274 1.000 31.55324 ? 119 TRP A CE3   1 
ATOM   941  C CZ2   . TRP A 1 119 ? 24.90729 -16.94846 -11.61690 1.000 37.23204 ? 119 TRP A CZ2   1 
ATOM   942  C CZ3   . TRP A 1 119 ? 23.87608 -15.13002 -10.38931 1.000 29.05532 ? 119 TRP A CZ3   1 
ATOM   943  C CH2   . TRP A 1 119 ? 25.00966 -15.85704 -10.78650 1.000 31.03639 ? 119 TRP A CH2   1 
ATOM   944  N N     . VAL A 1 120 ? 17.68727 -15.62330 -10.15815 1.000 24.19061 ? 120 VAL A N     1 
ATOM   945  C CA    . VAL A 1 120 ? 16.54230 -14.72117 -10.20771 1.000 28.38773 ? 120 VAL A CA    1 
ATOM   946  C C     . VAL A 1 120 ? 17.07398 -13.35270 -10.60917 1.000 29.73580 ? 120 VAL A C     1 
ATOM   947  O O     . VAL A 1 120 ? 17.90571 -12.77687 -9.89589  1.000 28.88468 ? 120 VAL A O     1 
ATOM   948  C CB    . VAL A 1 120 ? 15.80191 -14.65565 -8.86161  1.000 30.04000 ? 120 VAL A CB    1 
ATOM   949  C CG1   . VAL A 1 120 ? 14.62317 -13.72282 -8.95806  1.000 27.49928 ? 120 VAL A CG1   1 
ATOM   950  C CG2   . VAL A 1 120 ? 15.35784 -16.04259 -8.44060  1.000 26.33863 ? 120 VAL A CG2   1 
ATOM   951  N N     . PHE A 1 121 ? 16.61809 -12.84738 -11.75831 1.000 27.26059 ? 121 PHE A N     1 
ATOM   952  C CA    . PHE A 1 121 ? 17.02832 -11.54464 -12.28047 1.000 31.44202 ? 121 PHE A CA    1 
ATOM   953  C C     . PHE A 1 121 ? 15.88366 -10.54684 -12.15247 1.000 30.52353 ? 121 PHE A C     1 
ATOM   954  O O     . PHE A 1 121 ? 14.71600 -10.89868 -12.36942 1.000 24.30051 ? 121 PHE A O     1 
ATOM   955  C CB    . PHE A 1 121 ? 17.45951 -11.64856 -13.74479 1.000 23.06331 ? 121 PHE A CB    1 
ATOM   956  C CG    . PHE A 1 121 ? 18.51835 -12.68869 -13.99197 1.000 27.30694 ? 121 PHE A CG    1 
ATOM   957  C CD1   . PHE A 1 121 ? 19.78720 -12.53362 -13.45221 1.000 23.26992 ? 121 PHE A CD1   1 
ATOM   958  C CD2   . PHE A 1 121 ? 18.24932 -13.80816 -14.76638 1.000 26.77205 ? 121 PHE A CD2   1 
ATOM   959  C CE1   . PHE A 1 121 ? 20.78203 -13.47757 -13.67513 1.000 28.58532 ? 121 PHE A CE1   1 
ATOM   960  C CE2   . PHE A 1 121 ? 19.23265 -14.75434 -15.00296 1.000 32.37654 ? 121 PHE A CE2   1 
ATOM   961  C CZ    . PHE A 1 121 ? 20.51392 -14.58148 -14.45890 1.000 31.82763 ? 121 PHE A CZ    1 
ATOM   962  N N     . VAL A 1 122 ? 16.22718 -9.29943  -11.81845 1.000 24.20844 ? 122 VAL A N     1 
ATOM   963  C CA    . VAL A 1 122 ? 15.24958 -8.27760  -11.44479 1.000 30.54553 ? 122 VAL A CA    1 
ATOM   964  C C     . VAL A 1 122 ? 15.62103 -6.96187  -12.11315 1.000 24.55822 ? 122 VAL A C     1 
ATOM   965  O O     . VAL A 1 122 ? 16.78607 -6.55162  -12.07397 1.000 29.10935 ? 122 VAL A O     1 
ATOM   966  C CB    . VAL A 1 122 ? 15.19465 -8.06160  -9.91935  1.000 29.42486 ? 122 VAL A CB    1 
ATOM   967  C CG1   . VAL A 1 122 ? 14.19062 -6.98052  -9.58586  1.000 25.42936 ? 122 VAL A CG1   1 
ATOM   968  C CG2   . VAL A 1 122 ? 14.91158 -9.36220  -9.16381  1.000 28.17560 ? 122 VAL A CG2   1 
ATOM   969  N N     . LYS A 1 123 ? 14.63519 -6.28290  -12.70358 1.000 25.47192 ? 123 LYS A N     1 
ATOM   970  C CA    . LYS A 1 123 ? 14.82752 -4.90561  -13.13173 1.000 28.66888 ? 123 LYS A CA    1 
ATOM   971  C C     . LYS A 1 123 ? 13.53639 -4.13090  -12.89790 1.000 30.98183 ? 123 LYS A C     1 
ATOM   972  O O     . LYS A 1 123 ? 12.44532 -4.70823  -12.83065 1.000 27.76706 ? 123 LYS A O     1 
ATOM   973  C CB    . LYS A 1 123 ? 15.25696 -4.80506  -14.59969 1.000 27.55146 ? 123 LYS A CB    1 
ATOM   974  C CG    . LYS A 1 123 ? 14.16752 -5.12235  -15.60115 1.000 32.40676 ? 123 LYS A CG    1 
ATOM   975  C CD    . LYS A 1 123 ? 14.60943 -4.74081  -17.00788 1.000 31.99128 ? 123 LYS A CD    1 
ATOM   976  C CE    . LYS A 1 123 ? 13.51008 -5.01331  -18.04550 1.000 31.09471 ? 123 LYS A CE    1 
ATOM   977  N NZ    . LYS A 1 123 ? 13.77744 -4.28658  -19.31978 1.000 32.75403 ? 123 LYS A NZ    1 
ATOM   978  N N     . ARG A 1 124 ? 13.67299 -2.81211  -12.75290 1.000 27.11277 ? 124 ARG A N     1 
ATOM   979  C CA    . ARG A 1 124 ? 12.50569 -1.96752  -12.53112 1.000 27.71402 ? 124 ARG A CA    1 
ATOM   980  C C     . ARG A 1 124 ? 11.69403 -1.86868  -13.82089 1.000 31.66920 ? 124 ARG A C     1 
ATOM   981  O O     . ARG A 1 124 ? 12.22910 -2.01924  -14.92363 1.000 33.75928 ? 124 ARG A O     1 
ATOM   982  C CB    A ARG A 1 124 ? 12.91195 -0.56545  -12.05012 0.620 28.84763 ? 124 ARG A CB    1 
ATOM   983  C CB    B ARG A 1 124 ? 12.94049 -0.57573  -12.05946 0.380 28.74890 ? 124 ARG A CB    1 
ATOM   984  C CG    A ARG A 1 124 ? 13.52316 -0.50536  -10.62872 0.620 35.07490 ? 124 ARG A CG    1 
ATOM   985  C CG    B ARG A 1 124 ? 14.01785 -0.59337  -10.95760 0.380 35.48332 ? 124 ARG A CG    1 
ATOM   986  C CD    A ARG A 1 124 ? 13.66573 0.94946   -10.13376 0.620 41.47659 ? 124 ARG A CD    1 
ATOM   987  C CD    B ARG A 1 124 ? 14.57346 0.80970   -10.68868 0.380 40.21725 ? 124 ARG A CD    1 
ATOM   988  N NE    A ARG A 1 124 ? 14.48614 1.10247   -8.93187  0.620 40.64615 ? 124 ARG A NE    1 
ATOM   989  N NE    B ARG A 1 124 ? 15.52030 0.86292   -9.57691  0.380 41.10645 ? 124 ARG A NE    1 
ATOM   990  C CZ    A ARG A 1 124 ? 14.01570 1.32907   -7.71031  0.620 45.97124 ? 124 ARG A CZ    1 
ATOM   991  C CZ    B ARG A 1 124 ? 16.83023 1.03631   -9.70471  0.380 38.77786 ? 124 ARG A CZ    1 
ATOM   992  N NH1   A ARG A 1 124 ? 12.71980 1.42985   -7.47535  0.620 48.12377 ? 124 ARG A NH1   1 
ATOM   993  N NH1   B ARG A 1 124 ? 17.39957 1.15519   -10.89148 0.380 41.39111 ? 124 ARG A NH1   1 
ATOM   994  N NH2   A ARG A 1 124 ? 14.87035 1.46797   -6.69833  0.620 48.14049 ? 124 ARG A NH2   1 
ATOM   995  N NH2   B ARG A 1 124 ? 17.58637 1.10276   -8.61186  0.380 36.08235 ? 124 ARG A NH2   1 
ATOM   996  N N     . VAL A 1 125 ? 10.38866 -1.63686  -13.67939 1.000 28.61234 ? 125 VAL A N     1 
ATOM   997  C CA    . VAL A 1 125 ? 9.52571  -1.38748  -14.84122 1.000 25.99232 ? 125 VAL A CA    1 
ATOM   998  C C     . VAL A 1 125 ? 8.66405  -0.15869  -14.57700 1.000 37.73837 ? 125 VAL A C     1 
ATOM   999  O O     . VAL A 1 125 ? 8.54328  0.25969   -13.41825 1.000 36.92437 ? 125 VAL A O     1 
ATOM   1000 C CB    . VAL A 1 125 ? 8.64326  -2.60389  -15.17855 1.000 32.14623 ? 125 VAL A CB    1 
ATOM   1001 C CG1   . VAL A 1 125 ? 9.49346  -3.79559  -15.51538 1.000 37.30661 ? 125 VAL A CG1   1 
ATOM   1002 C CG2   . VAL A 1 125 ? 7.70753  -2.92857  -14.03129 1.000 34.64800 ? 125 VAL A CG2   1 
ATOM   1003 O OXT   . VAL A 1 125 ? 8.08314  0.45238   -15.48782 1.000 34.41696 ? 125 VAL A OXT   1 
HETATM 1004 C C1    . HC4 B 2 .   ? 8.66495  -9.30134  -0.96699  1.000 28.57639 ? 201 HC4 A C1    1 
HETATM 1005 O O1    . HC4 B 2 .   ? 8.75962  -9.76346  0.18149   1.000 29.66238 ? 201 HC4 A O1    1 
HETATM 1006 C C2    . HC4 B 2 .   ? 9.94490  -9.20720  -1.73819  1.000 24.82882 ? 201 HC4 A C2    1 
HETATM 1007 C C3    . HC4 B 2 .   ? 11.08009 -8.98085  -1.08598  1.000 26.06507 ? 201 HC4 A C3    1 
HETATM 1008 C "C1'" . HC4 B 2 .   ? 12.39846 -8.90302  -1.69409  1.000 27.43575 ? 201 HC4 A "C1'" 1 
HETATM 1009 C "C2'" . HC4 B 2 .   ? 13.47276 -8.64357  -0.85013  1.000 35.93981 ? 201 HC4 A "C2'" 1 
HETATM 1010 C "C3'" . HC4 B 2 .   ? 14.76633 -8.57268  -1.34302  1.000 35.95333 ? 201 HC4 A "C3'" 1 
HETATM 1011 C "C4'" . HC4 B 2 .   ? 15.02221 -8.77528  -2.69998  1.000 33.51384 ? 201 HC4 A "C4'" 1 
HETATM 1012 C "C5'" . HC4 B 2 .   ? 13.95226 -9.04781  -3.57163  1.000 25.51896 ? 201 HC4 A "C5'" 1 
HETATM 1013 C "C6'" . HC4 B 2 .   ? 12.65874 -9.11512  -3.06713  1.000 28.22305 ? 201 HC4 A "C6'" 1 
HETATM 1014 O "O4'" . HC4 B 2 .   ? 16.28015 -8.68859  -3.19142  1.000 29.48044 ? 201 HC4 A "O4'" 1 
HETATM 1015 O O     . HOH C 3 .   ? 17.30878 -17.13288 6.46393   1.000 45.07462 ? 301 HOH A O     1 
HETATM 1016 O O     . HOH C 3 .   ? 8.93346  -26.71925 -15.84731 1.000 48.13999 ? 302 HOH A O     1 
HETATM 1017 O O     . HOH C 3 .   ? 12.17678 -24.32245 -0.85689  1.000 56.61169 ? 303 HOH A O     1 
HETATM 1018 O O     . HOH C 3 .   ? 24.17237 -13.38991 -22.46262 1.000 44.79872 ? 304 HOH A O     1 
HETATM 1019 O O     . HOH C 3 .   ? 16.49535 1.22866   -13.20830 1.000 54.18073 ? 305 HOH A O     1 
HETATM 1020 O O     . HOH C 3 .   ? 7.41436  -17.11817 3.43108   1.000 32.74408 ? 306 HOH A O     1 
HETATM 1021 O O     . HOH C 3 .   ? 19.58129 -20.09407 5.25747   1.000 39.31728 ? 307 HOH A O     1 
HETATM 1022 O O     . HOH C 3 .   ? 27.85673 -19.59283 -6.78247  1.000 51.68586 ? 308 HOH A O     1 
HETATM 1023 O O     . HOH C 3 .   ? 17.24200 -16.67831 -21.13410 1.000 35.80003 ? 309 HOH A O     1 
HETATM 1024 O O     . HOH C 3 .   ? 32.71486 -4.52878  -19.68092 1.000 69.96926 ? 310 HOH A O     1 
HETATM 1025 O O     . HOH C 3 .   ? 11.22200 2.54568   -9.32952  1.000 49.87552 ? 311 HOH A O     1 
HETATM 1026 O O     . HOH C 3 .   ? 17.63292 -12.15763 -17.35142 1.000 33.63847 ? 312 HOH A O     1 
HETATM 1027 O O     . HOH C 3 .   ? 5.78887  2.88618   -5.62923  1.000 46.62440 ? 313 HOH A O     1 
HETATM 1028 O O     . HOH C 3 .   ? 3.79550  -22.25097 -13.25095 1.000 51.10632 ? 314 HOH A O     1 
HETATM 1029 O O     . HOH C 3 .   ? 16.73488 -28.76224 -11.49286 1.000 42.49442 ? 315 HOH A O     1 
HETATM 1030 O O     . HOH C 3 .   ? 7.03388  2.89745   -15.03778 1.000 38.41224 ? 316 HOH A O     1 
HETATM 1031 O O     . HOH C 3 .   ? 14.04288 -8.46165  3.74524   1.000 40.40303 ? 317 HOH A O     1 
HETATM 1032 O O     . HOH C 3 .   ? 26.72433 -22.90411 -13.06731 1.000 49.01451 ? 318 HOH A O     1 
HETATM 1033 O O     . HOH C 3 .   ? 24.71752 -5.65376  -17.34476 1.000 38.03445 ? 319 HOH A O     1 
HETATM 1034 O O     . HOH C 3 .   ? 9.34361  0.18561   -10.75347 1.000 36.58214 ? 320 HOH A O     1 
HETATM 1035 O O     . HOH C 3 .   ? 31.13167 -13.47370 -18.75872 1.000 58.57095 ? 321 HOH A O     1 
HETATM 1036 O O     . HOH C 3 .   ? 25.00279 -20.00193 -14.80637 1.000 30.34726 ? 322 HOH A O     1 
HETATM 1037 O O     . HOH C 3 .   ? 15.85186 -24.64863 -17.81462 1.000 47.47049 ? 323 HOH A O     1 
HETATM 1038 O O     . HOH C 3 .   ? 28.24995 -9.82421  -6.10497  1.000 46.90545 ? 324 HOH A O     1 
HETATM 1039 O O     . HOH C 3 .   ? 34.89011 -16.42894 -22.73986 1.000 40.86349 ? 325 HOH A O     1 
HETATM 1040 O O     . HOH C 3 .   ? 11.89909 -4.63455  -21.41156 1.000 49.27018 ? 326 HOH A O     1 
HETATM 1041 O O     . HOH C 3 .   ? 10.86613 -28.43745 -6.06058  1.000 46.14954 ? 327 HOH A O     1 
HETATM 1042 O O     . HOH C 3 .   ? 11.59406 -1.68838  -17.67186 1.000 38.67970 ? 328 HOH A O     1 
HETATM 1043 O O     . HOH C 3 .   ? 19.24951 -13.08531 -26.39501 1.000 48.16769 ? 329 HOH A O     1 
HETATM 1044 O O     . HOH C 3 .   ? 18.61186 -2.45398  -12.23157 1.000 48.87007 ? 330 HOH A O     1 
HETATM 1045 O O     . HOH C 3 .   ? 9.48410  -0.08595  -18.01136 1.000 41.77015 ? 331 HOH A O     1 
HETATM 1046 O O     . HOH C 3 .   ? 27.28462 -7.85354  -3.55970  1.000 46.87451 ? 332 HOH A O     1 
HETATM 1047 O O     . HOH C 3 .   ? 20.62386 -27.24146 -5.11499  1.000 45.74670 ? 333 HOH A O     1 
HETATM 1048 O O     . HOH C 3 .   ? 28.87552 -17.32528 -11.20076 1.000 51.19173 ? 334 HOH A O     1 
HETATM 1049 O O     . HOH C 3 .   ? 18.25113 -25.65868 3.22539   1.000 47.77410 ? 335 HOH A O     1 
HETATM 1050 O O     . HOH C 3 .   ? 3.05050  -9.03710  -6.99270  1.000 40.43598 ? 336 HOH A O     1 
HETATM 1051 O O     . HOH C 3 .   ? 27.23009 -11.95911 -4.06962  1.000 43.15436 ? 337 HOH A O     1 
HETATM 1052 O O     . HOH C 3 .   ? 16.42498 -1.60697  -13.01609 1.000 38.60323 ? 338 HOH A O     1 
HETATM 1053 O O     . HOH C 3 .   ? 21.54919 -9.82464  -25.99622 1.000 42.98327 ? 339 HOH A O     1 
HETATM 1054 O O     . HOH C 3 .   ? 8.14118  -23.26084 -13.71744 1.000 43.85622 ? 340 HOH A O     1 
HETATM 1055 O O     . HOH C 3 .   ? 25.25841 -19.33545 0.76538   1.000 44.80872 ? 341 HOH A O     1 
HETATM 1056 O O     . HOH C 3 .   ? 3.27204  -11.37866 -15.26139 1.000 46.88344 ? 342 HOH A O     1 
HETATM 1057 O O     . HOH C 3 .   ? 9.96778  -22.63580 -16.31308 1.000 42.48068 ? 343 HOH A O     1 
HETATM 1058 O O     . HOH C 3 .   ? 7.33872  1.03265   -8.82499  1.000 39.40736 ? 344 HOH A O     1 
HETATM 1059 O O     . HOH C 3 .   ? 19.83760 -0.98892  -9.74164  1.000 52.86170 ? 345 HOH A O     1 
HETATM 1060 O O     . HOH C 3 .   ? 12.52395 -6.83041  -20.90757 1.000 49.32542 ? 346 HOH A O     1 
HETATM 1061 O O     . HOH C 3 .   ? 14.01199 -8.56842  -21.78398 1.000 43.31388 ? 347 HOH A O     1 
HETATM 1062 O O     . HOH C 3 .   ? 28.22335 -21.01419 -9.23044  1.000 56.53496 ? 348 HOH A O     1 
HETATM 1063 O O     . HOH C 3 .   ? 26.67371 -20.40088 -12.31892 1.000 48.53263 ? 349 HOH A O     1 
HETATM 1064 O O     . HOH C 3 .   ? 15.55449 -16.83749 -22.88016 1.000 49.27883 ? 350 HOH A O     1 
HETATM 1065 O O     . HOH C 3 .   ? 21.32712 -1.80714  7.72403   1.000 60.41985 ? 351 HOH A O     1 
HETATM 1066 O O     . HOH C 3 .   ? 34.93168 -5.76378  -20.73796 1.000 70.52056 ? 352 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   ? 0.80917 0.83192 1.07457 -0.04914 0.17079  0.10349  1   MET A N     
2    C CA    . MET A 1   ? 0.78726 0.79720 1.00520 -0.03398 0.15945  0.10170  1   MET A CA    
3    C C     . MET A 1   ? 0.81793 0.83759 1.01421 -0.01871 0.16767  0.10621  1   MET A C     
4    O O     . MET A 1   ? 0.82182 0.84663 1.02479 -0.01681 0.18938  0.11628  1   MET A O     
5    C CB    . MET A 1   ? 0.80594 0.78368 0.99331 -0.03133 0.16423  0.11029  1   MET A CB    
6    C CG    . MET A 1   ? 0.86902 0.83634 1.00976 -0.01554 0.15497  0.11077  1   MET A CG    
7    S SD    . MET A 1   ? 1.01393 0.95247 1.13215 -0.01393 0.14561  0.11127  1   MET A SD    
8    C CE    . MET A 1   ? 0.72377 0.65238 0.79313 0.00481  0.15010  0.12424  1   MET A CE    
9    N N     . GLU A 2   ? 0.71155 0.73234 0.88182 -0.00858 0.15133  0.09793  2   GLU A N     
10   C CA    . GLU A 2   ? 0.73952 0.76603 0.88654 0.00536  0.15598  0.09822  2   GLU A CA    
11   C C     . GLU A 2   ? 0.69081 0.69575 0.78985 0.01528  0.16215  0.10616  2   GLU A C     
12   O O     . GLU A 2   ? 0.66793 0.65758 0.74584 0.01597  0.15017  0.10541  2   GLU A O     
13   C CB    . GLU A 2   ? 0.69269 0.72897 0.83715 0.00993  0.13511  0.08531  2   GLU A CB    
14   C CG    . GLU A 2   ? 0.55626 0.61671 0.74480 0.00297  0.12622  0.07843  2   GLU A CG    
15   C CD    . GLU A 2   ? 0.81088 0.89253 1.02802 0.00666  0.14300  0.08243  2   GLU A CD    
16   O OE1   . GLU A 2   ? 0.76294 0.84293 0.95947 0.01939  0.15270  0.08347  2   GLU A OE1   
17   O OE2   . GLU A 2   ? 0.80467 0.90477 1.06592 -0.00356 0.14724  0.08380  2   GLU A OE2   
18   N N     . HIS A 3   ? 0.62876 0.63371 0.71014 0.02357  0.18041  0.11341  3   HIS A N     
19   C CA    . HIS A 3   ? 0.68063 0.66695 0.71356 0.03314  0.18552  0.12164  3   HIS A CA    
20   C C     . HIS A 3   ? 0.63765 0.62454 0.63834 0.04359  0.17344  0.11103  3   HIS A C     
21   O O     . HIS A 3   ? 0.66592 0.65596 0.65015 0.05136  0.18439  0.10930  3   HIS A O     
22   C CB    . HIS A 3   ? 0.76610 0.74866 0.79043 0.03573  0.21292  0.13595  3   HIS A CB    
23   C CG    . HIS A 3   ? 0.94403 0.92635 1.00477 0.02380  0.22806  0.14649  3   HIS A CG    
24   N ND1   . HIS A 3   ? 0.92395 0.88897 0.98794 0.01690  0.22443  0.15381  3   HIS A ND1   
25   C CD2   . HIS A 3   ? 0.93433 0.93108 1.03162 0.01715  0.24821  0.15082  3   HIS A CD2   
26   C CE1   . HIS A 3   ? 0.88978 0.85645 0.98984 0.00520  0.24122  0.16148  3   HIS A CE1   
27   N NE2   . HIS A 3   ? 0.96454 0.95215 1.08661 0.00464  0.25564  0.16007  3   HIS A NE2   
28   N N     . VAL A 4   ? 0.45635 0.43906 0.44846 0.04318  0.15166  0.10298  4   VAL A N     
29   C CA    . VAL A 4   ? 0.44181 0.42160 0.40187 0.05102  0.13925  0.09382  4   VAL A CA    
30   C C     . VAL A 4   ? 0.57014 0.53901 0.50993 0.05160  0.12473  0.09586  4   VAL A C     
31   O O     . VAL A 4   ? 0.47714 0.44405 0.43648 0.04517  0.11669  0.09609  4   VAL A O     
32   C CB    A VAL A 4   ? 0.49410 0.48470 0.47208 0.05025  0.12776  0.07989  4   VAL A CB    
33   C CB    B VAL A 4   ? 0.49427 0.48463 0.47240 0.04996  0.12689  0.07983  4   VAL A CB    
34   C CG1   A VAL A 4   ? 0.46376 0.46732 0.48670 0.04178  0.12712  0.07924  4   VAL A CG1   
35   C CG1   B VAL A 4   ? 0.51970 0.50543 0.46611 0.05803  0.12201  0.07068  4   VAL A CG1   
36   C CG2   A VAL A 4   ? 0.43381 0.41896 0.39501 0.05066  0.10722  0.07117  4   VAL A CG2   
37   C CG2   B VAL A 4   ? 0.48068 0.48652 0.49697 0.04727  0.13735  0.07948  4   VAL A CG2   
38   N N     . ALA A 5   ? 0.49070 0.45309 0.39198 0.05947  0.12168  0.09708  5   ALA A N     
39   C CA    . ALA A 5   ? 0.46240 0.41781 0.34655 0.06187  0.10872  0.10108  5   ALA A CA    
40   C C     . ALA A 5   ? 0.48172 0.44220 0.36461 0.06080  0.08901  0.08713  5   ALA A C     
41   O O     . ALA A 5   ? 0.48081 0.44526 0.35514 0.06189  0.08562  0.07600  5   ALA A O     
42   C CB    . ALA A 5   ? 0.46957 0.41797 0.31323 0.07089  0.11353  0.11130  5   ALA A CB    
43   N N     . PHE A 6   ? 0.42660 0.38547 0.31961 0.05847  0.07785  0.08777  6   PHE A N     
44   C CA    . PHE A 6   ? 0.43657 0.40028 0.32770 0.05739  0.06091  0.07669  6   PHE A CA    
45   C C     . PHE A 6   ? 0.46707 0.43315 0.32639 0.06310  0.05416  0.07295  6   PHE A C     
46   O O     . PHE A 6   ? 0.49642 0.46013 0.33277 0.06962  0.05530  0.08233  6   PHE A O     
47   C CB    . PHE A 6   ? 0.39736 0.35829 0.29971 0.05668  0.05367  0.08062  6   PHE A CB    
48   C CG    . PHE A 6   ? 0.42522 0.39251 0.32958 0.05495  0.03877  0.07027  6   PHE A CG    
49   C CD1   . PHE A 6   ? 0.49949 0.47243 0.38616 0.06015  0.02868  0.07011  6   PHE A CD1   
50   C CD2   . PHE A 6   ? 0.45506 0.42377 0.37923 0.04776  0.03482  0.06124  6   PHE A CD2   
51   C CE1   . PHE A 6   ? 0.45822 0.43878 0.35099 0.05732  0.01673  0.06092  6   PHE A CE1   
52   C CE2   . PHE A 6   ? 0.37196 0.34568 0.29737 0.04576  0.02378  0.05294  6   PHE A CE2   
53   C CZ    . PHE A 6   ? 0.38128 0.36124 0.29305 0.05013  0.01567  0.05279  6   PHE A CZ    
54   N N     . GLY A 7   ? 0.47822 0.44788 0.33505 0.06045  0.04702  0.05934  7   GLY A N     
55   C CA    . GLY A 7   ? 0.45385 0.42513 0.28255 0.06322  0.03869  0.05229  7   GLY A CA    
56   C C     . GLY A 7   ? 0.53803 0.50439 0.34102 0.06738  0.04900  0.04964  7   GLY A C     
57   O O     . GLY A 7   ? 0.52767 0.49389 0.30236 0.06926  0.04188  0.04267  7   GLY A O     
58   N N     . SER A 8   ? 0.47042 0.43353 0.28282 0.06852  0.06583  0.05411  8   SER A N     
59   C CA    . SER A 8   ? 0.52873 0.48697 0.31890 0.07321  0.07928  0.05073  8   SER A CA    
60   C C     . SER A 8   ? 0.49992 0.45463 0.28200 0.07199  0.07393  0.03303  8   SER A C     
61   O O     . SER A 8   ? 0.47295 0.42884 0.27908 0.06742  0.06732  0.02581  8   SER A O     
62   C CB    . SER A 8   ? 0.58689 0.54627 0.40052 0.07355  0.09855  0.05780  8   SER A CB    
63   O OG    . SER A 8   ? 0.66921 0.62766 0.48468 0.07431  0.10683  0.07414  8   SER A OG    
64   N N     . GLU A 9   ? 0.60791 0.55604 0.35383 0.07610  0.07756  0.02596  9   GLU A N     
65   C CA    . GLU A 9   ? 0.70816 0.64912 0.44394 0.07392  0.07152  0.00760  9   GLU A CA    
66   C C     . GLU A 9   ? 0.56197 0.49760 0.31998 0.07562  0.08446  0.00137  9   GLU A C     
67   O O     . GLU A 9   ? 0.65431 0.58290 0.41794 0.07276  0.07817  -0.01125 9   GLU A O     
68   C CB    . GLU A 9   ? 0.76181 0.69561 0.45025 0.07705  0.07110  -0.00083 9   GLU A CB    
69   C CG    . GLU A 9   ? 0.84368 0.77296 0.50753 0.08507  0.09154  0.00649  9   GLU A CG    
70   C CD    . GLU A 9   ? 1.15917 1.08649 0.77281 0.08809  0.08516  0.00657  9   GLU A CD    
71   O OE1   . GLU A 9   ? 1.22705 1.16006 0.83187 0.08370  0.06302  0.00173  9   GLU A OE1   
72   O OE2   . GLU A 9   ? 1.11197 1.03344 0.69534 0.09487  0.10198  0.01190  9   GLU A OE2   
73   N N     . ASP A 10  ? 0.57873 0.51816 0.35259 0.08023  0.10228  0.01078  10  ASP A N     
74   C CA    . ASP A 10  ? 0.59599 0.53509 0.39749 0.08333  0.11365  0.00682  10  ASP A CA    
75   C C     . ASP A 10  ? 0.52206 0.47357 0.36845 0.07939  0.10942  0.01581  10  ASP A C     
76   O O     . ASP A 10  ? 0.49373 0.45146 0.36814 0.08280  0.12025  0.01782  10  ASP A O     
77   C CB    A ASP A 10  ? 0.61750 0.55496 0.40935 0.09151  0.13796  0.00871  10  ASP A CB    
78   C CB    B ASP A 10  ? 0.61723 0.55506 0.40950 0.09142  0.13798  0.00922  10  ASP A CB    
79   C CG    A ASP A 10  ? 0.65170 0.57424 0.42247 0.09743  0.14631  -0.00791 10  ASP A CG    
80   C CG    B ASP A 10  ? 0.65581 0.60342 0.45430 0.09125  0.14881  0.02666  10  ASP A CG    
81   O OD1   A ASP A 10  ? 0.66522 0.57707 0.42584 0.09393  0.13213  -0.02082 10  ASP A OD1   
82   O OD1   B ASP A 10  ? 0.60484 0.55695 0.40768 0.08579  0.13661  0.03586  10  ASP A OD1   
83   O OD2   A ASP A 10  ? 0.58297 0.50343 0.34845 0.10532  0.16846  -0.00849 10  ASP A OD2   
84   O OD2   B ASP A 10  ? 0.62893 0.57869 0.42918 0.09662  0.17104  0.03139  10  ASP A OD2   
85   N N     . ILE A 11  ? 0.46544 0.42148 0.31939 0.07255  0.09368  0.02043  11  ILE A N     
86   C CA    . ILE A 11  ? 0.46332 0.43006 0.35386 0.06798  0.09019  0.02862  11  ILE A CA    
87   C C     . ILE A 11  ? 0.54182 0.51152 0.46010 0.06874  0.08841  0.02373  11  ILE A C     
88   O O     . ILE A 11  ? 0.46534 0.44666 0.41532 0.06798  0.09217  0.02972  11  ILE A O     
89   C CB    . ILE A 11  ? 0.45129 0.41912 0.34092 0.06146  0.07415  0.03148  11  ILE A CB    
90   C CG1   . ILE A 11  ? 0.46596 0.44228 0.38770 0.05637  0.07293  0.03935  11  ILE A CG1   
91   C CG2   . ILE A 11  ? 0.38938 0.35218 0.27316 0.05814  0.05933  0.02120  11  ILE A CG2   
92   C CD1   . ILE A 11  ? 0.52469 0.50024 0.44466 0.05174  0.06243  0.04330  11  ILE A CD1   
93   N N     . GLU A 12  ? 0.54664 0.50585 0.45424 0.07018  0.08230  0.01322  12  GLU A N     
94   C CA    . GLU A 12  ? 0.45699 0.41652 0.38881 0.07236  0.07959  0.01077  12  GLU A CA    
95   C C     . GLU A 12  ? 0.48315 0.44728 0.43189 0.08162  0.09595  0.01159  12  GLU A C     
96   O O     . GLU A 12  ? 0.45766 0.42967 0.43631 0.08461  0.09405  0.01433  12  GLU A O     
97   C CB    . GLU A 12  ? 0.46327 0.40651 0.37914 0.07122  0.07079  0.00037  12  GLU A CB    
98   C CG    . GLU A 12  ? 0.53598 0.46370 0.42768 0.07703  0.08099  -0.01063 12  GLU A CG    
99   C CD    . GLU A 12  ? 0.58277 0.50552 0.43873 0.07332  0.07887  -0.01604 12  GLU A CD    
100  O OE1   . GLU A 12  ? 0.50969 0.44317 0.36171 0.06953  0.07429  -0.00802 12  GLU A OE1   
101  O OE2   . GLU A 12  ? 0.60634 0.51369 0.43785 0.07434  0.08097  -0.02865 12  GLU A OE2   
102  N N     . ASN A 13  ? 0.42356 0.38361 0.35331 0.08701  0.11205  0.00938  13  ASN A N     
103  C CA    . ASN A 13  ? 0.43849 0.40628 0.38784 0.09599  0.13117  0.01148  13  ASN A CA    
104  C C     . ASN A 13  ? 0.49036 0.48053 0.47553 0.09265  0.13506  0.02401  13  ASN A C     
105  O O     . ASN A 13  ? 0.48838 0.49323 0.51079 0.09703  0.14001  0.02724  13  ASN A O     
106  C CB    . ASN A 13  ? 0.52629 0.48362 0.44166 0.10171  0.14922  0.00634  13  ASN A CB    
107  C CG    . ASN A 13  ? 0.76620 0.70253 0.65813 0.10804  0.15239  -0.00889 13  ASN A CG    
108  O OD1   . ASN A 13  ? 0.64749 0.58024 0.54350 0.11816  0.17074  -0.01345 13  ASN A OD1   
109  N ND2   . ASN A 13  ? 0.68765 0.60950 0.55651 0.10179  0.13567  -0.01746 13  ASN A ND2   
110  N N     . THR A 14  ? 0.41246 0.40560 0.38868 0.08491  0.13277  0.03113  14  THR A N     
111  C CA    . THR A 14  ? 0.44370 0.45461 0.45266 0.07992  0.13847  0.04200  14  THR A CA    
112  C C     . THR A 14  ? 0.50962 0.53320 0.55391 0.07412  0.12180  0.04324  14  THR A C     
113  O O     . THR A 14  ? 0.46605 0.50861 0.54953 0.07369  0.12604  0.04759  14  THR A O     
114  C CB    . THR A 14  ? 0.49332 0.49895 0.48150 0.07370  0.14013  0.04963  14  THR A CB    
115  O OG1   . THR A 14  ? 0.55825 0.55324 0.51046 0.08005  0.15534  0.04942  14  THR A OG1   
116  C CG2   . THR A 14  ? 0.49744 0.51759 0.52024 0.06678  0.14748  0.06032  14  THR A CG2   
117  N N     . LEU A 15  ? 0.41266 0.42730 0.44365 0.06949  0.10274  0.03922  15  LEU A N     
118  C CA    . LEU A 15  ? 0.39712 0.42161 0.45399 0.06397  0.08660  0.04003  15  LEU A CA    
119  C C     . LEU A 15  ? 0.40385 0.43537 0.48245 0.07159  0.08333  0.03788  15  LEU A C     
120  O O     . LEU A 15  ? 0.43059 0.47672 0.53721 0.06857  0.07241  0.04066  15  LEU A O     
121  C CB    . LEU A 15  ? 0.39170 0.40389 0.42632 0.05776  0.07011  0.03663  15  LEU A CB    
122  C CG    . LEU A 15  ? 0.44140 0.44760 0.45887 0.05133  0.06988  0.03969  15  LEU A CG    
123  C CD1   . LEU A 15  ? 0.39189 0.39401 0.40539 0.04449  0.05353  0.03725  15  LEU A CD1   
124  C CD2   . LEU A 15  ? 0.43577 0.45148 0.47286 0.04728  0.08071  0.04766  15  LEU A CD2   
125  N N     . ALA A 16  ? 0.40406 0.42466 0.46976 0.08178  0.09180  0.03287  16  ALA A N     
126  C CA    . ALA A 16  ? 0.39836 0.42423 0.48748 0.09127  0.09023  0.03255  16  ALA A CA    
127  C C     . ALA A 16  ? 0.45059 0.50372 0.58449 0.09469  0.09808  0.03913  16  ALA A C     
128  O O     . ALA A 16  ? 0.51600 0.58192 0.67908 0.10058  0.09027  0.04193  16  ALA A O     
129  C CB    . ALA A 16  ? 0.39549 0.40132 0.46309 0.10199  0.10143  0.02478  16  ALA A CB    
130  N N     . LYS A 17  ? 0.41685 0.48007 0.55821 0.09105  0.11312  0.04259  17  LYS A N     
131  C CA    . LYS A 17  ? 0.42736 0.51794 0.61420 0.09321  0.12431  0.04850  17  LYS A CA    
132  C C     . LYS A 17  ? 0.47665 0.58838 0.69486 0.08013  0.11157  0.05366  17  LYS A C     
133  O O     . LYS A 17  ? 0.47276 0.61059 0.73396 0.07903  0.11909  0.05830  17  LYS A O     
134  C CB    . LYS A 17  ? 0.48299 0.57204 0.66126 0.09589  0.15124  0.05007  17  LYS A CB    
135  C CG    . LYS A 17  ? 0.45000 0.51835 0.59616 0.10871  0.16571  0.04269  17  LYS A CG    
136  C CD    . LYS A 17  ? 0.37789 0.44565 0.51293 0.11195  0.19350  0.04454  17  LYS A CD    
137  C CE    . LYS A 17  ? 0.52358 0.57451 0.61503 0.10319  0.19390  0.04621  17  LYS A CE    
138  N NZ    . LYS A 17  ? 0.56450 0.61495 0.64301 0.10648  0.22166  0.05047  17  LYS A NZ    
139  N N     . MET A 18  ? 0.47877 0.58034 0.67818 0.06991  0.09314  0.05195  18  MET A N     
140  C CA    . MET A 18  ? 0.50853 0.62372 0.72944 0.05583  0.08237  0.05421  18  MET A CA    
141  C C     . MET A 18  ? 0.55369 0.68153 0.79278 0.05393  0.05877  0.05279  18  MET A C     
142  O O     . MET A 18  ? 0.56520 0.68019 0.78283 0.05988  0.04693  0.05042  18  MET A O     
143  C CB    . MET A 18  ? 0.47110 0.56538 0.65803 0.04604  0.07979  0.05302  18  MET A CB    
144  C CG    . MET A 18  ? 0.48883 0.57348 0.65987 0.04620  0.10101  0.05717  18  MET A CG    
145  S SD    . MET A 18  ? 0.55168 0.61341 0.68687 0.03740  0.09656  0.05801  18  MET A SD    
146  C CE    . MET A 18  ? 0.57294 0.63001 0.69963 0.03925  0.12341  0.06709  18  MET A CE    
147  N N     . ASP A 19  ? 0.54032 0.69284 0.81782 0.04464  0.05183  0.05435  19  ASP A N     
148  C CA    . ASP A 19  ? 0.60945 0.77483 0.90014 0.03978  0.02703  0.05241  19  ASP A CA    
149  C C     . ASP A 19  ? 0.63400 0.78423 0.90057 0.02518  0.01550  0.04731  19  ASP A C     
150  O O     . ASP A 19  ? 0.51679 0.64766 0.76035 0.01994  0.02641  0.04642  19  ASP A O     
151  C CB    . ASP A 19  ? 0.53927 0.74213 0.88594 0.03679  0.02307  0.05500  19  ASP A CB    
152  C CG    . ASP A 19  ? 0.58189 0.79512 0.95394 0.02226  0.03589  0.05516  19  ASP A CG    
153  O OD1   . ASP A 19  ? 0.58929 0.77893 0.93351 0.01531  0.04689  0.05432  19  ASP A OD1   
154  O OD2   . ASP A 19  ? 0.62713 0.87286 1.04947 0.01784  0.03515  0.05689  19  ASP A OD2   
155  N N     . ASP A 20  ? 0.67834 0.83762 0.94981 0.01950  -0.00681 0.04411  20  ASP A N     
156  C CA    . ASP A 20  ? 0.58715 0.73202 0.83574 0.00638  -0.01792 0.03754  20  ASP A CA    
157  C C     . ASP A 20  ? 0.51494 0.65810 0.77655 -0.00732 -0.00685 0.03533  20  ASP A C     
158  O O     . ASP A 20  ? 0.54836 0.66787 0.78233 -0.01286 -0.00255 0.03243  20  ASP A O     
159  C CB    . ASP A 20  ? 0.75008 0.91039 1.00712 0.00176  -0.04284 0.03408  20  ASP A CB    
160  C CG    . ASP A 20  ? 0.85065 0.99909 1.07689 0.01240  -0.05465 0.03624  20  ASP A CG    
161  O OD1   . ASP A 20  ? 0.94827 1.07781 1.14026 0.00703  -0.06262 0.03147  20  ASP A OD1   
162  O OD2   . ASP A 20  ? 0.90820 1.06448 1.14463 0.02644  -0.05406 0.04302  20  ASP A OD2   
163  N N     . GLY A 21  ? 0.55397 0.72204 0.85999 -0.01269 -0.00137 0.03739  21  GLY A N     
164  C CA    . GLY A 21  ? 0.49113 0.65590 0.81255 -0.02666 0.01109  0.03658  21  GLY A CA    
165  C C     . GLY A 21  ? 0.53510 0.67407 0.82895 -0.02214 0.03323  0.04212  21  GLY A C     
166  O O     . GLY A 21  ? 0.49667 0.61480 0.77414 -0.03055 0.03748  0.04052  21  GLY A O     
167  N N     . GLN A 22  ? 0.54445 0.68354 0.83100 -0.00791 0.04707  0.04851  22  GLN A N     
168  C CA    . GLN A 22  ? 0.45827 0.57629 0.71847 -0.00332 0.06777  0.05429  22  GLN A CA    
169  C C     . GLN A 22  ? 0.42415 0.51384 0.63712 -0.00077 0.06150  0.05155  22  GLN A C     
170  O O     . GLN A 22  ? 0.40978 0.48133 0.60343 -0.00228 0.07276  0.05556  22  GLN A O     
171  C CB    . GLN A 22  ? 0.46445 0.58910 0.72524 0.01107  0.08351  0.05932  22  GLN A CB    
172  C CG    . GLN A 22  ? 0.49971 0.65130 0.80776 0.00964  0.09819  0.06424  22  GLN A CG    
173  C CD    . GLN A 22  ? 0.57300 0.73200 0.88278 0.02597  0.11226  0.06692  22  GLN A CD    
174  O OE1   . GLN A 22  ? 0.52141 0.68904 0.83674 0.03589  0.10102  0.06385  22  GLN A OE1   
175  N NE2   . GLN A 22  ? 0.62203 0.77558 0.92516 0.02945  0.13796  0.07291  22  GLN A NE2   
176  N N     . LEU A 23  ? 0.37624 0.46247 0.57140 0.00363  0.04441  0.04597  23  LEU A N     
177  C CA    . LEU A 23  ? 0.36322 0.42614 0.51936 0.00463  0.03842  0.04286  23  LEU A CA    
178  C C     . LEU A 23  ? 0.35704 0.40847 0.51115 -0.00697 0.03686  0.04051  23  LEU A C     
179  O O     . LEU A 23  ? 0.35234 0.38461 0.48080 -0.00542 0.04131  0.04183  23  LEU A O     
180  C CB    . LEU A 23  ? 0.36396 0.42651 0.50685 0.00836  0.02097  0.03773  23  LEU A CB    
181  C CG    . LEU A 23  ? 0.54640 0.60610 0.67518 0.02120  0.02240  0.03907  23  LEU A CG    
182  C CD1   . LEU A 23  ? 0.61683 0.66508 0.72098 0.02215  0.00798  0.03503  23  LEU A CD1   
183  C CD2   . LEU A 23  ? 0.44611 0.49364 0.55542 0.02764  0.03880  0.04187  23  LEU A CD2   
184  N N     . ASP A 24  ? 0.38675 0.44969 0.56886 -0.01852 0.03009  0.03648  24  ASP A N     
185  C CA    . ASP A 24  ? 0.41685 0.46581 0.59828 -0.03035 0.02927  0.03218  24  ASP A CA    
186  C C     . ASP A 24  ? 0.38772 0.42472 0.57375 -0.03274 0.04895  0.04027  24  ASP A C     
187  O O     . ASP A 24  ? 0.40754 0.42608 0.58759 -0.03958 0.05116  0.03843  24  ASP A O     
188  C CB    . ASP A 24  ? 0.34346 0.40810 0.55376 -0.04366 0.01586  0.02378  24  ASP A CB    
189  C CG    . ASP A 24  ? 0.44982 0.51768 0.64394 -0.04275 -0.00509 0.01556  24  ASP A CG    
190  O OD1   . ASP A 24  ? 0.36476 0.41930 0.52620 -0.03346 -0.00703 0.01623  24  ASP A OD1   
191  O OD2   . ASP A 24  ? 0.39415 0.47839 0.60791 -0.05165 -0.01967 0.00881  24  ASP A OD2   
192  N N     . GLY A 25  ? 0.33955 0.38491 0.53474 -0.02667 0.06429  0.04955  25  GLY A N     
193  C CA    . GLY A 25  ? 0.36398 0.39670 0.55813 -0.02740 0.08461  0.05989  25  GLY A CA    
194  C C     . GLY A 25  ? 0.38679 0.39935 0.54055 -0.01565 0.09150  0.06674  25  GLY A C     
195  O O     . GLY A 25  ? 0.42707 0.42685 0.57456 -0.01491 0.10726  0.07710  25  GLY A O     
196  N N     . LEU A 26  ? 0.34993 0.35972 0.47681 -0.00691 0.07980  0.06182  26  LEU A N     
197  C CA    . LEU A 26  ? 0.35377 0.34860 0.44487 0.00339  0.08349  0.06697  26  LEU A CA    
198  C C     . LEU A 26  ? 0.40576 0.38077 0.48573 0.00110  0.08373  0.06990  26  LEU A C     
199  O O     . LEU A 26  ? 0.38813 0.35787 0.47953 -0.00730 0.07640  0.06323  26  LEU A O     
200  C CB    . LEU A 26  ? 0.35169 0.34913 0.42211 0.01069  0.07027  0.05957  26  LEU A CB    
201  C CG    . LEU A 26  ? 0.37582 0.38814 0.45389 0.01599  0.07158  0.05757  26  LEU A CG    
202  C CD1   . LEU A 26  ? 0.40803 0.41837 0.46641 0.02186  0.05919  0.05053  26  LEU A CD1   
203  C CD2   . LEU A 26  ? 0.35400 0.36555 0.42351 0.02269  0.08923  0.06548  26  LEU A CD2   
204  N N     . ALA A 27  ? 0.32303 0.28655 0.37892 0.00965  0.09194  0.07975  27  ALA A N     
205  C CA    . ALA A 27  ? 0.32542 0.27031 0.37011 0.01125  0.09242  0.08483  27  ALA A CA    
206  C C     . ALA A 27  ? 0.39602 0.33846 0.42539 0.01519  0.07730  0.07653  27  ALA A C     
207  O O     . ALA A 27  ? 0.46640 0.39511 0.48996 0.01771  0.07702  0.07956  27  ALA A O     
208  C CB    . ALA A 27  ? 0.38020 0.31567 0.40318 0.02060  0.10485  0.10024  27  ALA A CB    
209  N N     . PHE A 28  ? 0.35534 0.30999 0.37984 0.01611  0.06617  0.06691  28  PHE A N     
210  C CA    . PHE A 28  ? 0.33271 0.28634 0.34217 0.01976  0.05426  0.06032  28  PHE A CA    
211  C C     . PHE A 28  ? 0.33205 0.29444 0.34918 0.01401  0.04351  0.04861  28  PHE A C     
212  O O     . PHE A 28  ? 0.35900 0.33101 0.39056 0.00995  0.04348  0.04644  28  PHE A O     
213  C CB    . PHE A 28  ? 0.33537 0.29240 0.32067 0.02953  0.05259  0.06387  28  PHE A CB    
214  C CG    . PHE A 28  ? 0.41699 0.38291 0.39774 0.03167  0.05612  0.06326  28  PHE A CG    
215  C CD1   . PHE A 28  ? 0.42042 0.39390 0.40112 0.03081  0.04815  0.05391  28  PHE A CD1   
216  C CD2   . PHE A 28  ? 0.38886 0.35370 0.36469 0.03523  0.06916  0.07252  28  PHE A CD2   
217  C CE1   . PHE A 28  ? 0.38356 0.36287 0.36160 0.03419  0.05285  0.05272  28  PHE A CE1   
218  C CE2   . PHE A 28  ? 0.41272 0.38489 0.38434 0.03819  0.07476  0.07072  28  PHE A CE2   
219  C CZ    . PHE A 28  ? 0.39898 0.37808 0.37272 0.03805  0.06647  0.06030  28  PHE A CZ    
220  N N     . GLY A 29  ? 0.30039 0.26029 0.30828 0.01435  0.03472  0.04207  29  GLY A N     
221  C CA    . GLY A 29  ? 0.32184 0.28792 0.33134 0.00982  0.02486  0.03287  29  GLY A CA    
222  C C     . GLY A 29  ? 0.35572 0.33065 0.35842 0.01414  0.02181  0.03264  29  GLY A C     
223  O O     . GLY A 29  ? 0.33902 0.31357 0.32781 0.02036  0.02361  0.03522  29  GLY A O     
224  N N     . ALA A 30  ? 0.31606 0.29854 0.32879 0.01099  0.01654  0.02914  30  ALA A N     
225  C CA    . ALA A 30  ? 0.31970 0.30762 0.32835 0.01583  0.01406  0.02871  30  ALA A CA    
226  C C     . ALA A 30  ? 0.37253 0.36234 0.38116 0.01281  0.00313  0.02404  30  ALA A C     
227  O O     . ALA A 30  ? 0.33896 0.33426 0.36045 0.00730  -0.00218 0.02211  30  ALA A O     
228  C CB    . ALA A 30  ? 0.31277 0.30979 0.33699 0.01875  0.02146  0.03286  30  ALA A CB    
229  N N     . ILE A 31  ? 0.37619 0.36092 0.36938 0.01581  -0.00037 0.02237  31  ILE A N     
230  C CA    . ILE A 31  ? 0.33692 0.32051 0.32516 0.01456  -0.00920 0.02051  31  ILE A CA    
231  C C     . ILE A 31  ? 0.38295 0.36416 0.36769 0.02109  -0.00833 0.02230  31  ILE A C     
232  O O     . ILE A 31  ? 0.35280 0.32821 0.32794 0.02392  -0.00295 0.02124  31  ILE A O     
233  C CB    . ILE A 31  ? 0.42267 0.39790 0.39465 0.01057  -0.01171 0.01700  31  ILE A CB    
234  C CG1   . ILE A 31  ? 0.41632 0.39008 0.39097 0.00613  -0.00908 0.01433  31  ILE A CG1   
235  C CG2   . ILE A 31  ? 0.37145 0.34417 0.33489 0.00872  -0.01981 0.01665  31  ILE A CG2   
236  C CD1   . ILE A 31  ? 0.46581 0.43270 0.42755 0.00447  -0.00762 0.01102  31  ILE A CD1   
237  N N     . GLN A 32  ? 0.30070 0.28587 0.29321 0.02380  -0.01408 0.02472  32  GLN A N     
238  C CA    . GLN A 32  ? 0.34436 0.32323 0.33398 0.03098  -0.01277 0.02662  32  GLN A CA    
239  C C     . GLN A 32  ? 0.38838 0.35783 0.36445 0.02964  -0.02036 0.02824  32  GLN A C     
240  O O     . GLN A 32  ? 0.32592 0.30075 0.30292 0.02708  -0.02924 0.03027  32  GLN A O     
241  C CB    . GLN A 32  ? 0.39156 0.38171 0.40315 0.03822  -0.01147 0.03037  32  GLN A CB    
242  C CG    . GLN A 32  ? 0.40283 0.38336 0.41206 0.04744  -0.00432 0.03052  32  GLN A CG    
243  C CD    . GLN A 32  ? 0.56157 0.55392 0.59557 0.05674  -0.00295 0.03502  32  GLN A CD    
244  O OE1   . GLN A 32  ? 0.57664 0.58597 0.63013 0.05585  -0.01103 0.03889  32  GLN A OE1   
245  N NE2   . GLN A 32  ? 0.55158 0.53587 0.58619 0.06573  0.00726  0.03368  32  GLN A NE2   
246  N N     . LEU A 33  ? 0.39927 0.35405 0.36135 0.03040  -0.01665 0.02705  33  LEU A N     
247  C CA    . LEU A 33  ? 0.39251 0.33475 0.34036 0.02856  -0.02041 0.02987  33  LEU A CA    
248  C C     . LEU A 33  ? 0.45979 0.38920 0.40809 0.03609  -0.01838 0.03355  33  LEU A C     
249  O O     . LEU A 33  ? 0.41597 0.34181 0.36967 0.04074  -0.01150 0.03009  33  LEU A O     
250  C CB    . LEU A 33  ? 0.39628 0.33085 0.33030 0.02087  -0.01637 0.02526  33  LEU A CB    
251  C CG    . LEU A 33  ? 0.46913 0.41269 0.40216 0.01478  -0.01624 0.02148  33  LEU A CG    
252  C CD1   . LEU A 33  ? 0.42254 0.36093 0.34723 0.00925  -0.01179 0.01788  33  LEU A CD1   
253  C CD2   . LEU A 33  ? 0.40576 0.35300 0.33491 0.01211  -0.02253 0.02334  33  LEU A CD2   
254  N N     . ASP A 34  ? 0.41302 0.33312 0.35336 0.03779  -0.02353 0.04073  34  ASP A N     
255  C CA    . ASP A 34  ? 0.45808 0.35895 0.39574 0.04394  -0.01956 0.04446  34  ASP A CA    
256  C C     . ASP A 34  ? 0.41974 0.30294 0.34201 0.03515  -0.01312 0.04027  34  ASP A C     
257  O O     . ASP A 34  ? 0.41065 0.30003 0.32702 0.02597  -0.01213 0.03511  34  ASP A O     
258  C CB    . ASP A 34  ? 0.42884 0.32622 0.36627 0.05188  -0.02760 0.05656  34  ASP A CB    
259  C CG    . ASP A 34  ? 0.41149 0.30313 0.32796 0.04545  -0.03314 0.06243  34  ASP A CG    
260  O OD1   . ASP A 34  ? 0.40538 0.29261 0.30882 0.03491  -0.02830 0.05717  34  ASP A OD1   
261  O OD2   . ASP A 34  ? 0.42402 0.31654 0.33704 0.05188  -0.04238 0.07296  34  ASP A OD2   
262  N N     . GLY A 35  ? 0.45615 0.31721 0.37452 0.03791  -0.00824 0.04247  35  GLY A N     
263  C CA    . GLY A 35  ? 0.54506 0.38963 0.45352 0.02794  -0.00161 0.03728  35  GLY A CA    
264  C C     . GLY A 35  ? 0.59026 0.43338 0.48637 0.01848  -0.00216 0.04184  35  GLY A C     
265  O O     . GLY A 35  ? 0.58021 0.41894 0.47349 0.00797  0.00324  0.03597  35  GLY A O     
266  N N     . ASP A 36  ? 0.46021 0.30798 0.34892 0.02179  -0.00843 0.05172  36  ASP A N     
267  C CA    . ASP A 36  ? 0.46390 0.31075 0.33690 0.01362  -0.00750 0.05566  36  ASP A CA    
268  C C     . ASP A 36  ? 0.55260 0.42106 0.42629 0.00852  -0.01006 0.04871  36  ASP A C     
269  O O     . ASP A 36  ? 0.58112 0.44951 0.44228 0.00177  -0.00695 0.04963  36  ASP A O     
270  C CB    . ASP A 36  ? 0.54563 0.38362 0.40352 0.01986  -0.01326 0.06998  36  ASP A CB    
271  C CG    . ASP A 36  ? 0.69598 0.50699 0.54988 0.02443  -0.00849 0.07967  36  ASP A CG    
272  O OD1   . ASP A 36  ? 0.78438 0.57944 0.63946 0.01658  0.00196  0.07550  36  ASP A OD1   
273  O OD2   . ASP A 36  ? 0.80479 0.61061 0.65596 0.03585  -0.01554 0.09145  36  ASP A OD2   
274  N N     . GLY A 37  ? 0.42583 0.31087 0.31345 0.01181  -0.01391 0.04218  37  GLY A N     
275  C CA    . GLY A 37  ? 0.41320 0.31493 0.30251 0.00779  -0.01560 0.03634  37  GLY A CA    
276  C C     . GLY A 37  ? 0.43542 0.34680 0.32162 0.01066  -0.02474 0.03929  37  GLY A C     
277  O O     . GLY A 37  ? 0.45220 0.37278 0.33644 0.00625  -0.02543 0.03401  37  GLY A O     
278  N N     . ASN A 38  ? 0.39989 0.30949 0.28653 0.01798  -0.03226 0.04716  38  ASN A N     
279  C CA    . ASN A 38  ? 0.42695 0.34990 0.31445 0.02013  -0.04386 0.04893  38  ASN A CA    
280  C C     . ASN A 38  ? 0.43201 0.37238 0.34373 0.02157  -0.04547 0.04278  38  ASN A C     
281  O O     . ASN A 38  ? 0.42639 0.36751 0.35367 0.02640  -0.04030 0.04209  38  ASN A O     
282  C CB    . ASN A 38  ? 0.45531 0.37388 0.33875 0.02880  -0.05282 0.06077  38  ASN A CB    
283  C CG    . ASN A 38  ? 0.54929 0.44726 0.40646 0.02758  -0.04950 0.06937  38  ASN A CG    
284  O OD1   . ASN A 38  ? 0.54696 0.44157 0.38308 0.02012  -0.04739 0.06761  38  ASN A OD1   
285  N ND2   . ASN A 38  ? 0.49269 0.37487 0.35097 0.03492  -0.04695 0.07873  38  ASN A ND2   
286  N N     . ILE A 39  ? 0.42111 0.37361 0.33454 0.01665  -0.05121 0.03776  39  ILE A N     
287  C CA    . ILE A 39  ? 0.33815 0.30529 0.27438 0.01573  -0.05064 0.03227  39  ILE A CA    
288  C C     . ILE A 39  ? 0.36868 0.35017 0.32579 0.02237  -0.05938 0.03738  39  ILE A C     
289  O O     . ILE A 39  ? 0.35734 0.34622 0.31174 0.02270  -0.07217 0.04055  39  ILE A O     
290  C CB    . ILE A 39  ? 0.39032 0.36161 0.32205 0.00695  -0.05222 0.02419  39  ILE A CB    
291  C CG1   . ILE A 39  ? 0.36183 0.32165 0.27937 0.00265  -0.04157 0.01960  39  ILE A CG1   
292  C CG2   . ILE A 39  ? 0.33244 0.31714 0.28925 0.00529  -0.05174 0.02036  39  ILE A CG2   
293  C CD1   . ILE A 39  ? 0.36625 0.32403 0.27213 -0.00461 -0.04166 0.01181  39  ILE A CD1   
294  N N     . LEU A 40  ? 0.39522 0.38177 0.37300 0.02812  -0.05240 0.03816  40  LEU A N     
295  C CA    . LEU A 40  ? 0.34683 0.35001 0.35141 0.03543  -0.05707 0.04263  40  LEU A CA    
296  C C     . LEU A 40  ? 0.37529 0.39728 0.40399 0.03004  -0.05663 0.03792  40  LEU A C     
297  O O     . LEU A 40  ? 0.35861 0.40005 0.40945 0.03085  -0.06625 0.04002  40  LEU A O     
298  C CB    . LEU A 40  ? 0.39011 0.38627 0.40312 0.04565  -0.04661 0.04572  40  LEU A CB    
299  C CG    . LEU A 40  ? 0.38271 0.35665 0.37591 0.05055  -0.04430 0.04987  40  LEU A CG    
300  C CD1   . LEU A 40  ? 0.40428 0.36947 0.40608 0.05931  -0.03254 0.04926  40  LEU A CD1   
301  C CD2   . LEU A 40  ? 0.43115 0.40492 0.41925 0.05564  -0.05725 0.05942  40  LEU A CD2   
302  N N     . GLN A 41  ? 0.39935 0.41639 0.42605 0.02470  -0.04561 0.03245  41  GLN A N     
303  C CA    . GLN A 41  ? 0.39333 0.42282 0.44027 0.01841  -0.04244 0.02891  41  GLN A CA    
304  C C     . GLN A 41  ? 0.32241 0.33946 0.35280 0.01050  -0.03689 0.02312  41  GLN A C     
305  O O     . GLN A 41  ? 0.32834 0.33098 0.33759 0.01184  -0.03216 0.02238  41  GLN A O     
306  C CB    . GLN A 41  ? 0.37310 0.41040 0.44152 0.02456  -0.03015 0.03190  41  GLN A CB    
307  C CG    . GLN A 41  ? 0.41631 0.46889 0.50813 0.03352  -0.03412 0.03739  41  GLN A CG    
308  C CD    . GLN A 41  ? 0.72031 0.78651 0.84011 0.03697  -0.02133 0.03919  41  GLN A CD    
309  O OE1   . GLN A 41  ? 0.83498 0.89405 0.95152 0.04569  -0.00876 0.04061  41  GLN A OE1   
310  N NE2   . GLN A 41  ? 0.79102 0.87614 0.93803 0.02930  -0.02331 0.03843  41  GLN A NE2   
311  N N     . TYR A 42  ? 0.36396 0.38696 0.40692 0.00220  -0.03722 0.01898  42  TYR A N     
312  C CA    . TYR A 42  ? 0.42940 0.43946 0.45907 -0.00441 -0.03233 0.01351  42  TYR A CA    
313  C C     . TYR A 42  ? 0.41623 0.43258 0.46889 -0.01168 -0.02840 0.01135  42  TYR A C     
314  O O     . TYR A 42  ? 0.36530 0.39187 0.43189 -0.01901 -0.03787 0.00715  42  TYR A O     
315  C CB    . TYR A 42  ? 0.36754 0.36996 0.37546 -0.00917 -0.04171 0.00790  42  TYR A CB    
316  C CG    . TYR A 42  ? 0.35849 0.34594 0.35058 -0.01356 -0.03528 0.00185  42  TYR A CG    
317  C CD1   . TYR A 42  ? 0.38175 0.36577 0.38142 -0.02163 -0.03390 -0.00506 42  TYR A CD1   
318  C CD2   . TYR A 42  ? 0.35361 0.33033 0.32557 -0.00979 -0.03024 0.00265  42  TYR A CD2   
319  C CE1   . TYR A 42  ? 0.40700 0.37581 0.39387 -0.02381 -0.02676 -0.01065 42  TYR A CE1   
320  C CE2   . TYR A 42  ? 0.39387 0.35961 0.35564 -0.01229 -0.02362 -0.00253 42  TYR A CE2   
321  C CZ    . TYR A 42  ? 0.36873 0.32985 0.33739 -0.01833 -0.02167 -0.00905 42  TYR A CZ    
322  O OH    . TYR A 42  ? 0.40108 0.34979 0.36141 -0.01888 -0.01368 -0.01409 42  TYR A OH    
323  N N     . ASN A 43  ? 0.29973 0.31037 0.35671 -0.01007 -0.01499 0.01466  43  ASN A N     
324  C CA    . ASN A 43  ? 0.37309 0.38994 0.45553 -0.01641 -0.00884 0.01550  43  ASN A CA    
325  C C     . ASN A 43  ? 0.34392 0.34701 0.42394 -0.02570 -0.00708 0.00924  43  ASN A C     
326  O O     . ASN A 43  ? 0.33503 0.32393 0.39323 -0.02538 -0.00848 0.00472  43  ASN A O     
327  C CB    . ASN A 43  ? 0.34572 0.36325 0.43433 -0.00970 0.00621  0.02409  43  ASN A CB    
328  C CG    . ASN A 43  ? 0.34143 0.34154 0.40972 -0.00619 0.01555  0.02689  43  ASN A CG    
329  O OD1   . ASN A 43  ? 0.33064 0.31970 0.38031 -0.00613 0.01120  0.02282  43  ASN A OD1   
330  N ND2   . ASN A 43  ? 0.33063 0.32947 0.40240 -0.00240 0.02878  0.03466  43  ASN A ND2   
331  N N     . ALA A 44  ? 0.33778 0.34459 0.44286 -0.03411 -0.00227 0.00897  44  ALA A N     
332  C CA    . ALA A 44  ? 0.37847 0.37065 0.48594 -0.04470 -0.00076 0.00144  44  ALA A CA    
333  C C     . ALA A 44  ? 0.42712 0.39690 0.51754 -0.03930 0.01152  0.00513  44  ALA A C     
334  O O     . ALA A 44  ? 0.43400 0.38721 0.51427 -0.04332 0.01120  -0.00262 44  ALA A O     
335  C CB    . ALA A 44  ? 0.35856 0.35927 0.50060 -0.05595 0.00341  0.00133  44  ALA A CB    
336  N N     . ALA A 45  ? 0.35505 0.32424 0.44173 -0.02960 0.02225  0.01666  45  ALA A N     
337  C CA    . ALA A 45  ? 0.35555 0.30671 0.42707 -0.02289 0.03178  0.02204  45  ALA A CA    
338  C C     . ALA A 45  ? 0.40391 0.34956 0.45212 -0.01726 0.02522  0.01691  45  ALA A C     
339  O O     . ALA A 45  ? 0.38068 0.31131 0.42112 -0.01458 0.02997  0.01646  45  ALA A O     
340  C CB    . ALA A 45  ? 0.41185 0.36588 0.47992 -0.01354 0.04221  0.03523  45  ALA A CB    
341  N N     . GLU A 46  ? 0.38113 0.33836 0.41982 -0.01504 0.01550  0.01371  46  GLU A N     
342  C CA    . GLU A 46  ? 0.33305 0.28549 0.35154 -0.01140 0.01095  0.00911  46  GLU A CA    
343  C C     . GLU A 46  ? 0.40968 0.35239 0.42399 -0.01903 0.00730  -0.00208 46  GLU A C     
344  O O     . GLU A 46  ? 0.43885 0.37048 0.44203 -0.01627 0.01119  -0.00534 46  GLU A O     
345  C CB    . GLU A 46  ? 0.34446 0.30830 0.35388 -0.00789 0.00314  0.00966  46  GLU A CB    
346  C CG    . GLU A 46  ? 0.36080 0.32014 0.35105 -0.00586 -0.00018 0.00561  46  GLU A CG    
347  C CD    . GLU A 46  ? 0.46971 0.42582 0.45310 0.00129  0.00608  0.00983  46  GLU A CD    
348  O OE1   . GLU A 46  ? 0.45394 0.41125 0.44260 0.00589  0.01135  0.01672  46  GLU A OE1   
349  O OE2   . GLU A 46  ? 0.36676 0.32047 0.33959 0.00228  0.00563  0.00659  46  GLU A OE2   
350  N N     . GLY A 47  ? 0.36163 0.30913 0.38521 -0.02855 -0.00011 -0.00877 47  GLY A N     
351  C CA    . GLY A 47  ? 0.38254 0.31900 0.39914 -0.03707 -0.00378 -0.02152 47  GLY A CA    
352  C C     . GLY A 47  ? 0.40172 0.31814 0.42437 -0.03909 0.00776  -0.02430 47  GLY A C     
353  O O     . GLY A 47  ? 0.44960 0.35090 0.45949 -0.04059 0.01012  -0.03389 47  GLY A O     
354  N N     . ASP A 48  ? 0.39986 0.31430 0.44153 -0.03866 0.01645  -0.01551 48  ASP A N     
355  C CA    . ASP A 48  ? 0.48107 0.37347 0.52891 -0.03848 0.02901  -0.01455 48  ASP A CA    
356  C C     . ASP A 48  ? 0.50952 0.39187 0.54215 -0.02606 0.03549  -0.01096 48  ASP A C     
357  O O     . ASP A 48  ? 0.59826 0.46010 0.63115 -0.02496 0.04381  -0.01477 48  ASP A O     
358  C CB    . ASP A 48  ? 0.47273 0.36525 0.53967 -0.03787 0.03870  -0.00142 48  ASP A CB    
359  C CG    . ASP A 48  ? 0.61449 0.51141 0.70526 -0.05241 0.03723  -0.00600 48  ASP A CG    
360  O OD1   . ASP A 48  ? 0.53591 0.43232 0.62825 -0.06375 0.02785  -0.02094 48  ASP A OD1   
361  O OD2   . ASP A 48  ? 0.68417 0.58590 0.79197 -0.05284 0.04567  0.00525  48  ASP A OD2   
362  N N     . ILE A 49  ? 0.46183 0.35851 0.48393 -0.01659 0.03222  -0.00370 49  ILE A N     
363  C CA    . ILE A 49  ? 0.45620 0.34954 0.46873 -0.00515 0.03679  0.00040  49  ILE A CA    
364  C C     . ILE A 49  ? 0.47694 0.36768 0.47585 -0.00630 0.03429  -0.01143 49  ILE A C     
365  O O     . ILE A 49  ? 0.51555 0.39623 0.51270 -0.00008 0.04166  -0.01329 49  ILE A O     
366  C CB    . ILE A 49  ? 0.45231 0.36236 0.46019 0.00332  0.03383  0.01146  49  ILE A CB    
367  C CG1   . ILE A 49  ? 0.47002 0.37951 0.48635 0.00673  0.03969  0.02410  49  ILE A CG1   
368  C CG2   . ILE A 49  ? 0.43887 0.35229 0.43878 0.01296  0.03459  0.01328  49  ILE A CG2   
369  C CD1   . ILE A 49  ? 0.50290 0.42806 0.51130 0.01299  0.03618  0.03193  49  ILE A CD1   
370  N N     . THR A 50  ? 0.37251 0.27229 0.36151 -0.01327 0.02479  -0.01866 50  THR A N     
371  C CA    . THR A 50  ? 0.42188 0.32095 0.39291 -0.01371 0.02308  -0.02730 50  THR A CA    
372  C C     . THR A 50  ? 0.51359 0.40085 0.47419 -0.02365 0.02065  -0.04226 50  THR A C     
373  O O     . THR A 50  ? 0.46587 0.34825 0.40833 -0.02354 0.02273  -0.05018 50  THR A O     
374  C CB    . THR A 50  ? 0.45200 0.36745 0.41306 -0.01298 0.01441  -0.02318 50  THR A CB    
375  O OG1   . THR A 50  ? 0.43301 0.35559 0.39609 -0.02015 0.00410  -0.02441 50  THR A OG1   
376  C CG2   . THR A 50  ? 0.40119 0.32706 0.36928 -0.00446 0.01613  -0.01144 50  THR A CG2   
377  N N     . GLY A 51  ? 0.40881 0.29207 0.37960 -0.03296 0.01643  -0.04695 51  GLY A N     
378  C CA    . GLY A 51  ? 0.41095 0.28437 0.37008 -0.04395 0.01135  -0.06307 51  GLY A CA    
379  C C     . GLY A 51  ? 0.47859 0.36652 0.42149 -0.04925 -0.00373 -0.06644 51  GLY A C     
380  O O     . GLY A 51  ? 0.49090 0.37150 0.41535 -0.05712 -0.00927 -0.08016 51  GLY A O     
381  N N     . ARG A 52  ? 0.49497 0.40184 0.44256 -0.04462 -0.01054 -0.05436 52  ARG A N     
382  C CA    . ARG A 52  ? 0.43774 0.35827 0.37254 -0.04739 -0.02518 -0.05424 52  ARG A CA    
383  C C     . ARG A 52  ? 0.47119 0.40610 0.42813 -0.05447 -0.03674 -0.05363 52  ARG A C     
384  O O     . ARG A 52  ? 0.48900 0.42926 0.47216 -0.05341 -0.03174 -0.04651 52  ARG A O     
385  C CB    . ARG A 52  ? 0.46837 0.39894 0.39668 -0.03773 -0.02501 -0.04172 52  ARG A CB    
386  C CG    . ARG A 52  ? 0.46864 0.39128 0.37020 -0.03428 -0.01964 -0.04354 52  ARG A CG    
387  C CD    . ARG A 52  ? 0.51452 0.42459 0.41802 -0.03054 -0.00415 -0.04709 52  ARG A CD    
388  N NE    . ARG A 52  ? 0.59062 0.49700 0.47457 -0.02691 0.00329  -0.04763 52  ARG A NE    
389  C CZ    . ARG A 52  ? 0.60209 0.50227 0.48944 -0.02167 0.01701  -0.04909 52  ARG A CZ    
390  N NH1   . ARG A 52  ? 0.51067 0.40545 0.41762 -0.01810 0.02411  -0.04928 52  ARG A NH1   
391  N NH2   . ARG A 52  ? 0.57550 0.47540 0.44780 -0.01944 0.02437  -0.04922 52  ARG A NH2   
392  N N     . ASP A 53  ? 0.42263 0.36496 0.36896 -0.06147 -0.05197 -0.06066 53  ASP A N     
393  C CA    . ASP A 53  ? 0.45656 0.41869 0.42658 -0.06760 -0.06565 -0.05959 53  ASP A CA    
394  C C     . ASP A 53  ? 0.47712 0.45777 0.45387 -0.05744 -0.07088 -0.04459 53  ASP A C     
395  O O     . ASP A 53  ? 0.47638 0.45805 0.42902 -0.05218 -0.07745 -0.04109 53  ASP A O     
396  C CB    . ASP A 53  ? 0.40756 0.37242 0.36250 -0.07857 -0.08262 -0.07326 53  ASP A CB    
397  C CG    . ASP A 53  ? 0.62675 0.61744 0.61051 -0.08522 -0.09950 -0.07240 53  ASP A CG    
398  O OD1   . ASP A 53  ? 0.62708 0.62834 0.64714 -0.08526 -0.09352 -0.06546 53  ASP A OD1   
399  O OD2   . ASP A 53  ? 0.77330 0.77505 0.74353 -0.09000 -0.11865 -0.07809 53  ASP A OD2   
400  N N     . PRO A 54  ? 0.49303 0.48600 0.50054 -0.05411 -0.06632 -0.03541 54  PRO A N     
401  C CA    . PRO A 54  ? 0.43682 0.44427 0.45022 -0.04339 -0.06920 -0.02253 54  PRO A CA    
402  C C     . PRO A 54  ? 0.45443 0.47672 0.46161 -0.04257 -0.08793 -0.02119 54  PRO A C     
403  O O     . PRO A 54  ? 0.46363 0.48682 0.45835 -0.03268 -0.08988 -0.01206 54  PRO A O     
404  C CB    . PRO A 54  ? 0.34573 0.36538 0.39544 -0.04310 -0.06182 -0.01663 54  PRO A CB    
405  C CG    . PRO A 54  ? 0.38782 0.39128 0.44139 -0.04908 -0.04879 -0.02154 54  PRO A CG    
406  C CD    . PRO A 54  ? 0.40312 0.39440 0.43913 -0.05912 -0.05573 -0.03565 54  PRO A CD    
407  N N     . LYS A 55  ? 0.40438 0.43738 0.41886 -0.05283 -0.10247 -0.03001 55  LYS A N     
408  C CA    . LYS A 55  ? 0.41168 0.46210 0.42136 -0.05107 -0.12306 -0.02733 55  LYS A CA    
409  C C     . LYS A 55  ? 0.54059 0.57628 0.50416 -0.04809 -0.12854 -0.02804 55  LYS A C     
410  O O     . LYS A 55  ? 0.60812 0.65357 0.56098 -0.04162 -0.14242 -0.02004 55  LYS A O     
411  C CB    . LYS A 55  ? 0.51831 0.58674 0.55001 -0.06444 -0.13877 -0.03792 55  LYS A CB    
412  C CG    . LYS A 55  ? 0.64985 0.73733 0.73215 -0.06725 -0.13304 -0.03459 55  LYS A CG    
413  C CD    . LYS A 55  ? 0.86575 0.95121 0.96715 -0.08497 -0.13205 -0.04896 55  LYS A CD    
414  C CE    . LYS A 55  ? 0.85068 0.95948 0.96518 -0.09725 -0.15702 -0.05913 55  LYS A CE    
415  N NZ    . LYS A 55  ? 0.81236 0.91231 0.88089 -0.09887 -0.17380 -0.06749 55  LYS A NZ    
416  N N     . GLN A 56  ? 0.54446 0.55672 0.48104 -0.05171 -0.11682 -0.03621 56  GLN A N     
417  C CA    . GLN A 56  ? 0.62070 0.61846 0.51339 -0.04891 -0.11801 -0.03623 56  GLN A CA    
418  C C     . GLN A 56  ? 0.61302 0.60068 0.49543 -0.03754 -0.10457 -0.02355 56  GLN A C     
419  O O     . GLN A 56  ? 0.66542 0.64671 0.51845 -0.03298 -0.10770 -0.01732 56  GLN A O     
420  C CB    . GLN A 56  ? 0.70077 0.67866 0.56899 -0.05809 -0.11071 -0.05242 56  GLN A CB    
421  C CG    . GLN A 56  ? 0.81643 0.79922 0.67829 -0.07080 -0.12732 -0.06774 56  GLN A CG    
422  C CD    . GLN A 56  ? 0.92852 0.88782 0.76977 -0.07963 -0.11670 -0.08579 56  GLN A CD    
423  O OE1   . GLN A 56  ? 0.83344 0.78980 0.69485 -0.09001 -0.11593 -0.09827 56  GLN A OE1   
424  N NE2   . GLN A 56  ? 0.95023 0.89148 0.75232 -0.07556 -0.10688 -0.08728 56  GLN A NE2   
425  N N     . VAL A 57  ? 0.47831 0.46363 0.38278 -0.03354 -0.08978 -0.01960 57  VAL A N     
426  C CA    . VAL A 57  ? 0.49054 0.46644 0.38595 -0.02492 -0.07791 -0.01018 57  VAL A CA    
427  C C     . VAL A 57  ? 0.45941 0.44490 0.36802 -0.01557 -0.08239 0.00294  57  VAL A C     
428  O O     . VAL A 57  ? 0.45275 0.42871 0.34827 -0.00953 -0.07633 0.01060  57  VAL A O     
429  C CB    . VAL A 57  ? 0.45958 0.42771 0.36756 -0.02448 -0.06096 -0.01260 57  VAL A CB    
430  C CG1   . VAL A 57  ? 0.45142 0.40612 0.34419 -0.03083 -0.05385 -0.02428 57  VAL A CG1   
431  C CG2   . VAL A 57  ? 0.42763 0.40695 0.36936 -0.02459 -0.05968 -0.01134 57  VAL A CG2   
432  N N     . ILE A 58  ? 0.46725 0.47084 0.40314 -0.01433 -0.09180 0.00541  58  ILE A N     
433  C CA    . ILE A 58  ? 0.53427 0.54597 0.48500 -0.00367 -0.09398 0.01732  58  ILE A CA    
434  C C     . ILE A 58  ? 0.43979 0.44661 0.36550 0.00193  -0.10423 0.02574  58  ILE A C     
435  O O     . ILE A 58  ? 0.46059 0.47174 0.36975 -0.00202 -0.11843 0.02350  58  ILE A O     
436  C CB    . ILE A 58  ? 0.51649 0.55162 0.50510 -0.00329 -0.10100 0.01801  58  ILE A CB    
437  C CG1   . ILE A 58  ? 0.52356 0.55892 0.53528 -0.00480 -0.08516 0.01530  58  ILE A CG1   
438  C CG2   . ILE A 58  ? 0.48969 0.53585 0.49104 0.00878  -0.10850 0.02998  58  ILE A CG2   
439  C CD1   . ILE A 58  ? 0.60287 0.66083 0.65400 -0.00688 -0.08769 0.01519  58  ILE A CD1   
440  N N     . GLY A 59  ? 0.44844 0.44406 0.36873 0.01081  -0.09676 0.03545  59  GLY A N     
441  C CA    . GLY A 59  ? 0.44288 0.42801 0.33773 0.01661  -0.10268 0.04578  59  GLY A CA    
442  C C     . GLY A 59  ? 0.57571 0.53925 0.43614 0.01199  -0.09251 0.04475  59  GLY A C     
443  O O     . GLY A 59  ? 0.49238 0.44227 0.33288 0.01689  -0.09162 0.05522  59  GLY A O     
444  N N     . LYS A 60  ? 0.48912 0.44889 0.34374 0.00310  -0.08368 0.03319  60  LYS A N     
445  C CA    . LYS A 60  ? 0.47515 0.41775 0.30224 -0.00099 -0.07204 0.03170  60  LYS A CA    
446  C C     . LYS A 60  ? 0.51470 0.44884 0.35303 0.00113  -0.05712 0.03423  60  LYS A C     
447  O O     . LYS A 60  ? 0.45988 0.40049 0.32387 0.00470  -0.05503 0.03413  60  LYS A O     
448  C CB    . LYS A 60  ? 0.48075 0.42276 0.29876 -0.00986 -0.06805 0.01793  60  LYS A CB    
449  C CG    . LYS A 60  ? 0.47399 0.42136 0.27494 -0.01446 -0.08274 0.01205  60  LYS A CG    
450  C CD    . LYS A 60  ? 0.63125 0.56713 0.40619 -0.02198 -0.07436 0.00019  60  LYS A CD    
451  C CE    . LYS A 60  ? 0.69172 0.63275 0.45365 -0.02890 -0.08877 -0.01104 60  LYS A CE    
452  N NZ    . LYS A 60  ? 0.78614 0.74475 0.55982 -0.02640 -0.11040 -0.00489 60  LYS A NZ    
453  N N     . ASN A 61  ? 0.47296 0.39308 0.29148 -0.00170 -0.04638 0.03607  61  ASN A N     
454  C CA    . ASN A 61  ? 0.46675 0.38024 0.29629 -0.00181 -0.03364 0.03707  61  ASN A CA    
455  C C     . ASN A 61  ? 0.51144 0.43067 0.35187 -0.00669 -0.02445 0.02637  61  ASN A C     
456  O O     . ASN A 61  ? 0.48090 0.39805 0.30781 -0.01134 -0.01908 0.02084  61  ASN A O     
457  C CB    . ASN A 61  ? 0.49171 0.38869 0.30091 -0.00333 -0.02564 0.04525  61  ASN A CB    
458  C CG    . ASN A 61  ? 0.56031 0.45120 0.38486 -0.00442 -0.01537 0.04582  61  ASN A CG    
459  O OD1   . ASN A 61  ? 0.45822 0.35292 0.29098 -0.00974 -0.00602 0.03877  61  ASN A OD1   
460  N ND2   . ASN A 61  ? 0.49321 0.37522 0.32323 0.00094  -0.01774 0.05347  61  ASN A ND2   
461  N N     . PHE A 62  ? 0.44771 0.37335 0.31132 -0.00455 -0.02214 0.02398  62  PHE A N     
462  C CA    . PHE A 62  ? 0.42683 0.35911 0.30288 -0.00683 -0.01547 0.01616  62  PHE A CA    
463  C C     . PHE A 62  ? 0.48949 0.41785 0.35953 -0.01098 -0.00437 0.01414  62  PHE A C     
464  O O     . PHE A 62  ? 0.43610 0.36720 0.30584 -0.01300 0.00109  0.00803  62  PHE A O     
465  C CB    . PHE A 62  ? 0.39626 0.33476 0.29271 -0.00291 -0.01540 0.01623  62  PHE A CB    
466  C CG    . PHE A 62  ? 0.41691 0.36269 0.32567 -0.00323 -0.01074 0.01081  62  PHE A CG    
467  C CD1   . PHE A 62  ? 0.49477 0.44483 0.40943 -0.00358 -0.01276 0.00730  62  PHE A CD1   
468  C CD2   . PHE A 62  ? 0.39953 0.34771 0.31486 -0.00319 -0.00506 0.00966  62  PHE A CD2   
469  C CE1   . PHE A 62  ? 0.40314 0.35674 0.32872 -0.00260 -0.00762 0.00444  62  PHE A CE1   
470  C CE2   . PHE A 62  ? 0.44711 0.40247 0.37318 -0.00150 -0.00204 0.00691  62  PHE A CE2   
471  C CZ    . PHE A 62  ? 0.41633 0.37293 0.34693 -0.00050 -0.00255 0.00520  62  PHE A CZ    
472  N N     . PHE A 63  ? 0.45507 0.37663 0.32220 -0.01249 0.00007  0.01905  63  PHE A N     
473  C CA    . PHE A 63  ? 0.45818 0.38046 0.32776 -0.01744 0.01122  0.01692  63  PHE A CA    
474  C C     . PHE A 63  ? 0.46407 0.37898 0.31257 -0.02131 0.01863  0.01834  63  PHE A C     
475  O O     . PHE A 63  ? 0.46320 0.38285 0.31566 -0.02441 0.02928  0.01419  63  PHE A O     
476  C CB    . PHE A 63  ? 0.39770 0.31588 0.27598 -0.01986 0.01385  0.01988  63  PHE A CB    
477  C CG    . PHE A 63  ? 0.47530 0.39980 0.36986 -0.01627 0.00819  0.01687  63  PHE A CG    
478  C CD1   . PHE A 63  ? 0.40096 0.33931 0.31058 -0.01563 0.00883  0.01110  63  PHE A CD1   
479  C CD2   . PHE A 63  ? 0.39778 0.31409 0.29128 -0.01220 0.00271  0.02036  63  PHE A CD2   
480  C CE1   . PHE A 63  ? 0.42952 0.37282 0.34871 -0.01199 0.00401  0.00897  63  PHE A CE1   
481  C CE2   . PHE A 63  ? 0.41637 0.33751 0.32142 -0.00851 -0.00047 0.01683  63  PHE A CE2   
482  C CZ    . PHE A 63  ? 0.43841 0.37275 0.35417 -0.00884 0.00009  0.01116  63  PHE A CZ    
483  N N     . LYS A 64  ? 0.45141 0.35565 0.27725 -0.02040 0.01356  0.02457  64  LYS A N     
484  C CA    . LYS A 64  ? 0.42708 0.32235 0.22607 -0.02384 0.02106  0.02685  64  LYS A CA    
485  C C     . LYS A 64  ? 0.54214 0.43997 0.32654 -0.02357 0.01859  0.01859  64  LYS A C     
486  O O     . LYS A 64  ? 0.58298 0.47792 0.35391 -0.02666 0.03036  0.01424  64  LYS A O     
487  C CB    . LYS A 64  ? 0.53957 0.42022 0.31598 -0.02246 0.01660  0.03921  64  LYS A CB    
488  C CG    . LYS A 64  ? 0.52256 0.39252 0.26485 -0.02560 0.02459  0.04304  64  LYS A CG    
489  C CD    . LYS A 64  ? 0.58139 0.43506 0.29770 -0.02293 0.01989  0.05826  64  LYS A CD    
490  C CE    . LYS A 64  ? 0.77634 0.61956 0.45321 -0.02603 0.02876  0.06168  64  LYS A CE    
491  N NZ    . LYS A 64  ? 0.92730 0.75359 0.57134 -0.02240 0.02368  0.07839  64  LYS A NZ    
492  N N     . ASP A 65  ? 0.48099 0.38387 0.26898 -0.02050 0.00464  0.01541  65  ASP A N     
493  C CA    . ASP A 65  ? 0.52954 0.43200 0.30074 -0.02203 -0.00030 0.00693  65  ASP A CA    
494  C C     . ASP A 65  ? 0.44388 0.35421 0.23686 -0.02206 -0.00053 -0.00407 65  ASP A C     
495  O O     . ASP A 65  ? 0.53415 0.44064 0.31840 -0.02442 0.00637  -0.01398 65  ASP A O     
496  C CB    . ASP A 65  ? 0.55953 0.46174 0.31589 -0.02017 -0.01774 0.01204  65  ASP A CB    
497  C CG    . ASP A 65  ? 0.71494 0.60622 0.44542 -0.01870 -0.01786 0.02495  65  ASP A CG    
498  O OD1   . ASP A 65  ? 0.72838 0.60948 0.42983 -0.02190 -0.00806 0.02524  65  ASP A OD1   
499  O OD2   . ASP A 65  ? 0.74842 0.63984 0.48790 -0.01377 -0.02593 0.03546  65  ASP A OD2   
500  N N     . VAL A 66  ? 0.44041 0.35954 0.26003 -0.01912 -0.00699 -0.00236 66  VAL A N     
501  C CA    . VAL A 66  ? 0.45064 0.37485 0.28870 -0.01921 -0.00773 -0.01054 66  VAL A CA    
502  C C     . VAL A 66  ? 0.52066 0.44693 0.37547 -0.01725 0.00514  -0.01326 66  VAL A C     
503  O O     . VAL A 66  ? 0.49043 0.41402 0.34941 -0.01751 0.01054  -0.02125 66  VAL A O     
504  C CB    . VAL A 66  ? 0.43194 0.36508 0.28994 -0.01682 -0.01891 -0.00665 66  VAL A CB    
505  C CG1   . VAL A 66  ? 0.42568 0.36214 0.30323 -0.01768 -0.01761 -0.01325 66  VAL A CG1   
506  C CG2   . VAL A 66  ? 0.43410 0.36921 0.28022 -0.01791 -0.03304 -0.00435 66  VAL A CG2   
507  N N     . ALA A 67  ? 0.43874 0.36953 0.30397 -0.01522 0.00996  -0.00715 67  ALA A N     
508  C CA    . ALA A 67  ? 0.39977 0.33786 0.28590 -0.01230 0.01771  -0.00840 67  ALA A CA    
509  C C     . ALA A 67  ? 0.40240 0.34361 0.28998 -0.01390 0.02727  -0.00615 67  ALA A C     
510  O O     . ALA A 67  ? 0.38717 0.33605 0.28958 -0.01332 0.02653  -0.00252 67  ALA A O     
511  C CB    . ALA A 67  ? 0.36482 0.31025 0.26920 -0.00870 0.01112  -0.00428 67  ALA A CB    
512  N N     . PRO A 68  ? 0.45560 0.39144 0.32843 -0.01662 0.03708  -0.00907 68  PRO A N     
513  C CA    . PRO A 68  ? 0.45311 0.39347 0.33083 -0.01949 0.04816  -0.00629 68  PRO A CA    
514  C C     . PRO A 68  ? 0.40712 0.36338 0.31518 -0.01652 0.05269  -0.00764 68  PRO A C     
515  O O     . PRO A 68  ? 0.40064 0.36545 0.32134 -0.02004 0.05705  -0.00471 68  PRO A O     
516  C CB    . PRO A 68  ? 0.42429 0.35585 0.27938 -0.02178 0.06011  -0.01029 68  PRO A CB    
517  C CG    . PRO A 68  ? 0.46672 0.39189 0.31314 -0.01901 0.05647  -0.01867 68  PRO A CG    
518  C CD    . PRO A 68  ? 0.41812 0.34369 0.26919 -0.01791 0.03974  -0.01601 68  PRO A CD    
519  N N     . CYS A 69  ? 0.40621 0.36690 0.32738 -0.01033 0.05117  -0.01141 69  CYS A N     
520  C CA    . CYS A 69  ? 0.34067 0.31808 0.29012 -0.00581 0.05324  -0.01063 69  CYS A CA    
521  C C     . CYS A 69  ? 0.36117 0.34758 0.32167 -0.00668 0.04228  -0.00593 69  CYS A C     
522  O O     . CYS A 69  ? 0.36382 0.36666 0.34590 -0.00475 0.04173  -0.00504 69  CYS A O     
523  C CB    . CYS A 69  ? 0.38539 0.36221 0.34484 0.00246  0.05449  -0.01359 69  CYS A CB    
524  S SG    . CYS A 69  ? 0.38696 0.35913 0.34691 0.00599  0.04103  -0.01023 69  CYS A SG    
525  N N     . THR A 70  ? 0.34498 0.32176 0.29145 -0.00920 0.03350  -0.00348 70  THR A N     
526  C CA    . THR A 70  ? 0.30178 0.28333 0.25461 -0.01024 0.02500  -0.00081 70  THR A CA    
527  C C     . THR A 70  ? 0.37001 0.34803 0.31918 -0.01812 0.02708  0.00060  70  THR A C     
528  O O     . THR A 70  ? 0.41767 0.39713 0.37151 -0.02027 0.02120  0.00082  70  THR A O     
529  C CB    . THR A 70  ? 0.34638 0.31945 0.28973 -0.00730 0.01630  0.00106  70  THR A CB    
530  O OG1   . THR A 70  ? 0.38979 0.34990 0.31562 -0.01050 0.01535  0.00265  70  THR A OG1   
531  C CG2   . THR A 70  ? 0.34620 0.31961 0.29334 -0.00140 0.01571  0.00031  70  THR A CG2   
532  N N     . ASP A 71  ? 0.32617 0.29711 0.26494 -0.02267 0.03613  0.00145  71  ASP A N     
533  C CA    . ASP A 71  ? 0.36903 0.33487 0.30566 -0.03096 0.04148  0.00428  71  ASP A CA    
534  C C     . ASP A 71  ? 0.42147 0.40628 0.38453 -0.03506 0.04732  0.00140  71  ASP A C     
535  O O     . ASP A 71  ? 0.38668 0.37866 0.35648 -0.03662 0.05925  0.00061  71  ASP A O     
536  C CB    . ASP A 71  ? 0.39305 0.34454 0.30608 -0.03350 0.05005  0.00771  71  ASP A CB    
537  C CG    . ASP A 71  ? 0.45539 0.39700 0.36290 -0.04187 0.05728  0.01327  71  ASP A CG    
538  O OD1   . ASP A 71  ? 0.44707 0.39212 0.37122 -0.04698 0.05546  0.01292  71  ASP A OD1   
539  O OD2   . ASP A 71  ? 0.47374 0.40266 0.35831 -0.04370 0.06505  0.01788  71  ASP A OD2   
540  N N     . SER A 72  ? 0.39929 0.39374 0.37796 -0.03655 0.03859  -0.00078 72  SER A N     
541  C CA    . SER A 72  ? 0.29536 0.31300 0.30270 -0.03994 0.03888  -0.00425 72  SER A CA    
542  C C     . SER A 72  ? 0.34672 0.36606 0.35941 -0.04467 0.02757  -0.00752 72  SER A C     
543  O O     . SER A 72  ? 0.33898 0.34469 0.33512 -0.04099 0.01975  -0.00732 72  SER A O     
544  C CB    . SER A 72  ? 0.38821 0.42389 0.41023 -0.02964 0.03670  -0.00539 72  SER A CB    
545  O OG    . SER A 72  ? 0.37533 0.41108 0.39268 -0.02290 0.02367  -0.00541 72  SER A OG    
546  N N     . PRO A 73  ? 0.32514 0.36178 0.36160 -0.05313 0.02669  -0.01156 73  PRO A N     
547  C CA    . PRO A 73  ? 0.39098 0.42833 0.43009 -0.05872 0.01486  -0.01743 73  PRO A CA    
548  C C     . PRO A 73  ? 0.37615 0.41862 0.40711 -0.04827 0.00148  -0.01898 73  PRO A C     
549  O O     . PRO A 73  ? 0.37472 0.40646 0.39323 -0.04991 -0.00622 -0.02319 73  PRO A O     
550  C CB    . PRO A 73  ? 0.31903 0.38203 0.39080 -0.06910 0.01498  -0.02223 73  PRO A CB    
551  C CG    . PRO A 73  ? 0.32744 0.39245 0.40895 -0.07266 0.03229  -0.01744 73  PRO A CG    
552  C CD    . PRO A 73  ? 0.38746 0.44495 0.45096 -0.05864 0.03646  -0.01208 73  PRO A CD    
553  N N     . GLU A 74  ? 0.38471 0.44110 0.42116 -0.03720 0.00006  -0.01542 74  GLU A N     
554  C CA    . GLU A 74  ? 0.40574 0.46848 0.43589 -0.02765 -0.01157 -0.01508 74  GLU A CA    
555  C C     . GLU A 74  ? 0.34695 0.38774 0.35176 -0.02045 -0.01097 -0.01162 74  GLU A C     
556  O O     . GLU A 74  ? 0.38957 0.43140 0.38521 -0.01370 -0.01851 -0.01091 74  GLU A O     
557  C CB    A GLU A 74  ? 0.43975 0.52510 0.48845 -0.01792 -0.01294 -0.01101 74  GLU A CB    
558  C CB    B GLU A 74  ? 0.43850 0.52372 0.48693 -0.01783 -0.01305 -0.01099 74  GLU A CB    
559  C CG    A GLU A 74  ? 0.41957 0.50759 0.48109 -0.01625 0.00081  -0.00818 74  GLU A CG    
560  C CG    B GLU A 74  ? 0.48687 0.59885 0.55180 -0.01701 -0.02692 -0.01333 74  GLU A CG    
561  C CD    A GLU A 74  ? 0.34062 0.44625 0.42801 -0.02627 0.00652  -0.01144 74  GLU A CD    
562  C CD    B GLU A 74  ? 0.49645 0.60226 0.53924 -0.01454 -0.03947 -0.01535 74  GLU A CD    
563  O OE1   A GLU A 74  ? 0.38775 0.51626 0.49572 -0.03050 -0.00325 -0.01486 74  GLU A OE1   
564  O OE1   B GLU A 74  ? 0.43201 0.52038 0.45306 -0.00642 -0.03746 -0.01078 74  GLU A OE1   
565  O OE2   A GLU A 74  ? 0.46788 0.56501 0.55464 -0.03053 0.02088  -0.01067 74  GLU A OE2   
566  O OE2   B GLU A 74  ? 0.47100 0.58991 0.51835 -0.02147 -0.05086 -0.02228 74  GLU A OE2   
567  N N     . PHE A 75  ? 0.34186 0.36443 0.33555 -0.02175 -0.00233 -0.00902 75  PHE A N     
568  C CA    . PHE A 75  ? 0.27411 0.27983 0.24909 -0.01563 -0.00253 -0.00583 75  PHE A CA    
569  C C     . PHE A 75  ? 0.38649 0.37248 0.34879 -0.02121 0.00004  -0.00611 75  PHE A C     
570  O O     . PHE A 75  ? 0.37294 0.35036 0.32753 -0.02132 -0.00415 -0.00863 75  PHE A O     
571  C CB    . PHE A 75  ? 0.31565 0.32016 0.29001 -0.00960 0.00309  -0.00183 75  PHE A CB    
572  C CG    . PHE A 75  ? 0.34067 0.33497 0.30326 -0.00311 0.00107  0.00109  75  PHE A CG    
573  C CD1   . PHE A 75  ? 0.36554 0.34621 0.31569 -0.00416 -0.00050 0.00173  75  PHE A CD1   
574  C CD2   . PHE A 75  ? 0.32494 0.32335 0.29188 0.00409  0.00167  0.00371  75  PHE A CD2   
575  C CE1   . PHE A 75  ? 0.37995 0.35520 0.32480 0.00105  -0.00182 0.00439  75  PHE A CE1   
576  C CE2   . PHE A 75  ? 0.31744 0.30710 0.27714 0.00809  0.00103  0.00636  75  PHE A CE2   
577  C CZ    . PHE A 75  ? 0.35169 0.33171 0.30164 0.00613  -0.00088 0.00642  75  PHE A CZ    
578  N N     . TYR A 76  ? 0.35401 0.33153 0.31266 -0.02501 0.00760  -0.00315 76  TYR A N     
579  C CA    . TYR A 76  ? 0.36345 0.32113 0.30976 -0.02922 0.01021  -0.00076 76  TYR A CA    
580  C C     . TYR A 76  ? 0.36348 0.31639 0.31514 -0.03721 0.00907  -0.00547 76  TYR A C     
581  O O     . TYR A 76  ? 0.36569 0.30083 0.30770 -0.03698 0.00797  -0.00537 76  TYR A O     
582  C CB    . TYR A 76  ? 0.38419 0.33561 0.32409 -0.03287 0.01920  0.00389  76  TYR A CB    
583  C CG    . TYR A 76  ? 0.41468 0.34418 0.33846 -0.03524 0.02189  0.00979  76  TYR A CG    
584  C CD1   . TYR A 76  ? 0.49564 0.41193 0.41192 -0.03069 0.01593  0.01144  76  TYR A CD1   
585  C CD2   . TYR A 76  ? 0.49019 0.41166 0.40594 -0.04098 0.03154  0.01482  76  TYR A CD2   
586  C CE1   . TYR A 76  ? 0.55716 0.45276 0.46020 -0.03078 0.01808  0.01871  76  TYR A CE1   
587  C CE2   . TYR A 76  ? 0.56570 0.46537 0.46445 -0.04197 0.03387  0.02281  76  TYR A CE2   
588  C CZ    . TYR A 76  ? 0.62450 0.51133 0.51789 -0.03634 0.02637  0.02507  76  TYR A CZ    
589  O OH    . TYR A 76  ? 0.76363 0.62845 0.64168 -0.03525 0.02827  0.03467  76  TYR A OH    
590  N N     . GLY A 77  ? 0.35236 0.32123 0.32129 -0.04432 0.00916  -0.01033 77  GLY A N     
591  C CA    . GLY A 77  ? 0.40056 0.36534 0.37639 -0.05458 0.00737  -0.01694 77  GLY A CA    
592  C C     . GLY A 77  ? 0.42413 0.38430 0.39155 -0.05108 -0.00185 -0.02356 77  GLY A C     
593  O O     . GLY A 77  ? 0.43653 0.37829 0.39788 -0.05626 -0.00147 -0.02821 77  GLY A O     
594  N N     . LYS A 78  ? 0.33278 0.30744 0.29828 -0.04194 -0.00882 -0.02397 78  LYS A N     
595  C CA    . LYS A 78  ? 0.40127 0.37128 0.35442 -0.03762 -0.01564 -0.02959 78  LYS A CA    
596  C C     . LYS A 78  ? 0.47134 0.41845 0.40860 -0.03090 -0.01117 -0.02619 78  LYS A C     
597  O O     . LYS A 78  ? 0.47133 0.40390 0.39887 -0.03107 -0.01172 -0.03239 78  LYS A O     
598  C CB    . LYS A 78  ? 0.42609 0.41627 0.37960 -0.02893 -0.02251 -0.02799 78  LYS A CB    
599  C CG    . LYS A 78  ? 0.49881 0.51452 0.47005 -0.03396 -0.02984 -0.03176 78  LYS A CG    
600  C CD    . LYS A 78  ? 0.61214 0.64616 0.58253 -0.02322 -0.03703 -0.02748 78  LYS A CD    
601  C CE    . LYS A 78  ? 0.69866 0.75947 0.68534 -0.02711 -0.04815 -0.03190 78  LYS A CE    
602  N NZ    . LYS A 78  ? 0.67743 0.73649 0.65410 -0.03550 -0.05777 -0.04393 78  LYS A NZ    
603  N N     . PHE A 79  ? 0.43245 0.37666 0.36791 -0.02487 -0.00686 -0.01711 79  PHE A N     
604  C CA    . PHE A 79  ? 0.36314 0.28965 0.28864 -0.01852 -0.00384 -0.01256 79  PHE A CA    
605  C C     . PHE A 79  ? 0.45970 0.36395 0.38171 -0.02386 0.00013  -0.01391 79  PHE A C     
606  O O     . PHE A 79  ? 0.49154 0.38057 0.40689 -0.01940 0.00115  -0.01636 79  PHE A O     
607  C CB    . PHE A 79  ? 0.38682 0.31618 0.31219 -0.01425 -0.00194 -0.00374 79  PHE A CB    
608  C CG    . PHE A 79  ? 0.43885 0.35497 0.35758 -0.00772 -0.00127 0.00199  79  PHE A CG    
609  C CD1   . PHE A 79  ? 0.45084 0.37101 0.37002 0.00080  -0.00308 0.00303  79  PHE A CD1   
610  C CD2   . PHE A 79  ? 0.49419 0.39508 0.40755 -0.00970 0.00137  0.00757  79  PHE A CD2   
611  C CE1   . PHE A 79  ? 0.52139 0.43382 0.43991 0.00727  -0.00331 0.00857  79  PHE A CE1   
612  C CE2   . PHE A 79  ? 0.50491 0.39626 0.41402 -0.00211 -0.00002 0.01423  79  PHE A CE2   
613  C CZ    . PHE A 79  ? 0.51143 0.41016 0.42519 0.00639  -0.00289 0.01422  79  PHE A CZ    
614  N N     . LYS A 80  ? 0.43014 0.33078 0.35722 -0.03320 0.00411  -0.01208 80  LYS A N     
615  C CA    . LYS A 80  ? 0.50161 0.37732 0.42535 -0.03872 0.00956  -0.01127 80  LYS A CA    
616  C C     . LYS A 80  ? 0.45784 0.32396 0.38292 -0.04499 0.00811  -0.02368 80  LYS A C     
617  O O     . LYS A 80  ? 0.51770 0.35833 0.43645 -0.04380 0.01196  -0.02478 80  LYS A O     
618  C CB    . LYS A 80  ? 0.54659 0.42065 0.47509 -0.04844 0.01637  -0.00564 80  LYS A CB    
619  C CG    . LYS A 80  ? 0.64936 0.53116 0.59322 -0.06283 0.01792  -0.01412 80  LYS A CG    
620  C CD    . LYS A 80  ? 0.63891 0.50212 0.58457 -0.07337 0.02847  -0.00860 80  LYS A CD    
621  C CE    . LYS A 80  ? 0.79229 0.66558 0.75894 -0.08996 0.03034  -0.01787 80  LYS A CE    
622  N NZ    . LYS A 80  ? 0.78997 0.64734 0.75881 -0.09746 0.02679  -0.02999 80  LYS A NZ    
623  N N     . GLU A 81  ? 0.48551 0.37090 0.41836 -0.05144 0.00215  -0.03351 81  GLU A N     
624  C CA    . GLU A 81  ? 0.53351 0.41087 0.46361 -0.05765 -0.00147 -0.04761 81  GLU A CA    
625  C C     . GLU A 81  ? 0.51941 0.38483 0.43334 -0.04570 -0.00182 -0.05076 81  GLU A C     
626  O O     . GLU A 81  ? 0.51764 0.35992 0.42394 -0.04752 0.00111  -0.05951 81  GLU A O     
627  C CB    . GLU A 81  ? 0.50779 0.41296 0.44726 -0.06449 -0.01115 -0.05662 81  GLU A CB    
628  C CG    . GLU A 81  ? 0.65846 0.57839 0.61976 -0.07838 -0.01079 -0.05741 81  GLU A CG    
629  C CD    . GLU A 81  ? 0.80691 0.76229 0.78055 -0.07892 -0.02173 -0.06126 81  GLU A CD    
630  O OE1   . GLU A 81  ? 0.81821 0.79292 0.81491 -0.08831 -0.02171 -0.06122 81  GLU A OE1   
631  O OE2   . GLU A 81  ? 0.74409 0.70859 0.70509 -0.06899 -0.02965 -0.06306 81  GLU A OE2   
632  N N     . GLY A 82  ? 0.47888 0.35940 0.38855 -0.03378 -0.00403 -0.04437 82  GLY A N     
633  C CA    . GLY A 82  ? 0.56869 0.44162 0.46575 -0.02235 -0.00229 -0.04643 82  GLY A CA    
634  C C     . GLY A 82  ? 0.60924 0.45798 0.50456 -0.01506 0.00558  -0.04090 82  GLY A C     
635  O O     . GLY A 82  ? 0.56382 0.39544 0.45086 -0.00995 0.00996  -0.04773 82  GLY A O     
636  N N     . VAL A 83  ? 0.54938 0.39654 0.45156 -0.01340 0.00746  -0.02837 83  VAL A N     
637  C CA    . VAL A 83  ? 0.53540 0.36106 0.43692 -0.00550 0.01289  -0.02080 83  VAL A CA    
638  C C     . VAL A 83  ? 0.55845 0.35463 0.45696 -0.01143 0.01839  -0.02805 83  VAL A C     
639  O O     . VAL A 83  ? 0.60743 0.38326 0.50275 -0.00284 0.02375  -0.02995 83  VAL A O     
640  C CB    . VAL A 83  ? 0.48787 0.31761 0.39284 -0.00440 0.01194  -0.00626 83  VAL A CB    
641  C CG1   . VAL A 83  ? 0.46714 0.27279 0.37034 0.00251  0.01596  0.00318  83  VAL A CG1   
642  C CG2   . VAL A 83  ? 0.47715 0.33121 0.38519 0.00274  0.00713  -0.00071 83  VAL A CG2   
643  N N     . ALA A 84  ? 0.54365 0.33715 0.44525 -0.02649 0.01802  -0.03322 84  ALA A N     
644  C CA    . ALA A 84  ? 0.53866 0.30174 0.43966 -0.03514 0.02399  -0.04015 84  ALA A CA    
645  C C     . ALA A 84  ? 0.62048 0.37386 0.51369 -0.03664 0.02365  -0.05864 84  ALA A C     
646  O O     . ALA A 84  ? 0.72299 0.44459 0.61182 -0.03520 0.03081  -0.06433 84  ALA A O     
647  C CB    . ALA A 84  ? 0.58776 0.35400 0.49822 -0.05268 0.02448  -0.04059 84  ALA A CB    
648  N N     . SER A 85  ? 0.60768 0.38618 0.49705 -0.03907 0.01570  -0.06829 85  SER A N     
649  C CA    . SER A 85  ? 0.55650 0.32610 0.43292 -0.04159 0.01441  -0.08703 85  SER A CA    
650  C C     . SER A 85  ? 0.56308 0.32534 0.42686 -0.02458 0.02014  -0.08775 85  SER A C     
651  O O     . SER A 85  ? 0.56873 0.31427 0.41814 -0.02438 0.02330  -0.10334 85  SER A O     
652  C CB    . SER A 85  ? 0.56430 0.36369 0.43897 -0.05052 0.00243  -0.09634 85  SER A CB    
653  O OG    . SER A 85  ? 0.56241 0.38883 0.43416 -0.03932 -0.00166 -0.08735 85  SER A OG    
654  N N     . GLY A 86  ? 0.57183 0.34664 0.44121 -0.01098 0.02209  -0.07221 86  GLY A N     
655  C CA    . GLY A 86  ? 0.58296 0.35654 0.44615 0.00488  0.02849  -0.07144 86  GLY A CA    
656  C C     . GLY A 86  ? 0.66443 0.46107 0.51569 0.00758  0.02486  -0.07658 86  GLY A C     
657  O O     . GLY A 86  ? 0.65569 0.45177 0.50034 0.01959  0.03226  -0.07725 86  GLY A O     
658  N N     . ASN A 87  ? 0.65047 0.46764 0.49965 -0.00257 0.01449  -0.07909 87  ASN A N     
659  C CA    . ASN A 87  ? 0.63879 0.47715 0.47459 -0.00015 0.00959  -0.08208 87  ASN A CA    
660  C C     . ASN A 87  ? 0.66655 0.53246 0.51541 -0.00288 0.00115  -0.07014 87  ASN A C     
661  O O     . ASN A 87  ? 0.78380 0.65772 0.64130 -0.01414 -0.00656 -0.07200 87  ASN A O     
662  C CB    A ASN A 87  ? 0.66993 0.50282 0.48644 -0.00963 0.00375  -0.10092 87  ASN A CB    
663  C CB    B ASN A 87  ? 0.66998 0.50334 0.48605 -0.00933 0.00376  -0.10083 87  ASN A CB    
664  C CG    A ASN A 87  ? 0.75451 0.61376 0.55861 -0.00990 -0.00631 -0.10128 87  ASN A CG    
665  C CG    B ASN A 87  ? 0.66540 0.49147 0.49136 -0.02582 -0.00284 -0.10922 87  ASN A CG    
666  O OD1   A ASN A 87  ? 0.81400 0.69171 0.62636 -0.01941 -0.01838 -0.10144 87  ASN A OD1   
667  O OD1   B ASN A 87  ? 0.66990 0.51800 0.50614 -0.03499 -0.01352 -0.10739 87  ASN A OD1   
668  N ND2   A ASN A 87  ? 0.75091 0.61267 0.53609 0.00127  -0.00065 -0.10021 87  ASN A ND2   
669  N ND2   B ASN A 87  ? 0.64696 0.44161 0.47214 -0.02956 0.00465  -0.11818 87  ASN A ND2   
670  N N     . LEU A 88  ? 0.54987 0.42934 0.40301 0.00711  0.00393  -0.05805 88  LEU A N     
671  C CA    . LEU A 88  ? 0.54089 0.44259 0.40622 0.00598  -0.00199 -0.04705 88  LEU A CA    
672  C C     . LEU A 88  ? 0.48368 0.39987 0.34010 0.01407  -0.00130 -0.04237 88  LEU A C     
673  O O     . LEU A 88  ? 0.49865 0.41216 0.35481 0.02313  0.00719  -0.03720 88  LEU A O     
674  C CB    . LEU A 88  ? 0.53000 0.43015 0.41222 0.00834  0.00116  -0.03541 88  LEU A CB    
675  C CG    . LEU A 88  ? 0.45828 0.37798 0.35115 0.00847  -0.00264 -0.02537 88  LEU A CG    
676  C CD1   . LEU A 88  ? 0.48486 0.41578 0.38188 -0.00084 -0.00969 -0.02851 88  LEU A CD1   
677  C CD2   . LEU A 88  ? 0.41142 0.32777 0.31567 0.01072  -0.00025 -0.01594 88  LEU A CD2   
678  N N     . ASN A 89  ? 0.47901 0.41079 0.32944 0.01102  -0.00981 -0.04343 89  ASN A N     
679  C CA    . ASN A 89  ? 0.47204 0.41576 0.31175 0.01879  -0.00922 -0.03686 89  ASN A CA    
680  C C     . ASN A 89  ? 0.41584 0.37871 0.25822 0.01546  -0.02089 -0.03436 89  ASN A C     
681  O O     . ASN A 89  ? 0.49039 0.45850 0.31894 0.01186  -0.02977 -0.04279 89  ASN A O     
682  C CB    A ASN A 89  ? 0.49651 0.43082 0.30937 0.02343  -0.00435 -0.04501 89  ASN A CB    
683  C CB    B ASN A 89  ? 0.49239 0.42662 0.30541 0.02349  -0.00423 -0.04495 89  ASN A CB    
684  C CG    A ASN A 89  ? 0.42549 0.36891 0.22541 0.03235  -0.00005 -0.03546 89  ASN A CG    
685  C CG    B ASN A 89  ? 0.53835 0.46463 0.33589 0.01520  -0.01159 -0.06170 89  ASN A CG    
686  O OD1   A ASN A 89  ? 0.48320 0.43627 0.29778 0.03563  0.00164  -0.02254 89  ASN A OD1   
687  O OD1   B ASN A 89  ? 0.59903 0.50584 0.39556 0.01217  -0.00648 -0.07170 89  ASN A OD1   
688  N ND2   A ASN A 89  ? 0.47666 0.41493 0.24727 0.03596  0.00275  -0.04199 89  ASN A ND2   
689  N ND2   B ASN A 89  ? 0.50201 0.44311 0.28825 0.01154  -0.02417 -0.06490 89  ASN A ND2   
690  N N     . THR A 90  ? 0.41600 0.38992 0.27648 0.01686  -0.02156 -0.02360 90  THR A N     
691  C CA    . THR A 90  ? 0.42471 0.41710 0.29294 0.01466  -0.03190 -0.02148 90  THR A CA    
692  C C     . THR A 90  ? 0.46290 0.46328 0.34228 0.02170  -0.02872 -0.00795 90  THR A C     
693  O O     . THR A 90  ? 0.41744 0.41014 0.30580 0.02343  -0.02034 -0.00259 90  THR A O     
694  C CB    . THR A 90  ? 0.44474 0.44074 0.33061 0.00376  -0.03682 -0.02823 90  THR A CB    
695  O OG1   . THR A 90  ? 0.56467 0.58253 0.46041 0.00215  -0.04736 -0.02746 90  THR A OG1   
696  C CG2   . THR A 90  ? 0.41599 0.40580 0.31929 0.00221  -0.02914 -0.02243 90  THR A CG2   
697  N N     . MET A 91  ? 0.41734 0.43285 0.29631 0.02582  -0.03617 -0.00276 91  MET A N     
698  C CA    . MET A 91  ? 0.42883 0.44935 0.31742 0.03345  -0.03293 0.01011  91  MET A CA    
699  C C     . MET A 91  ? 0.44397 0.48243 0.35119 0.03312  -0.04133 0.01172  91  MET A C     
700  O O     . MET A 91  ? 0.42579 0.47844 0.33172 0.03054  -0.05277 0.00641  91  MET A O     
701  C CB    . MET A 91  ? 0.49414 0.51324 0.36236 0.04283  -0.03121 0.01890  91  MET A CB    
702  C CG    . MET A 91  ? 0.56758 0.57799 0.44123 0.04880  -0.01974 0.03095  91  MET A CG    
703  S SD    . MET A 91  ? 0.71164 0.71768 0.55544 0.05800  -0.01542 0.04044  91  MET A SD    
704  C CE    . MET A 91  ? 0.61286 0.60911 0.43795 0.05334  -0.01050 0.02720  91  MET A CE    
705  N N     . PHE A 92  ? 0.35360 0.39212 0.27946 0.03533  -0.03552 0.01786  92  PHE A N     
706  C CA    . PHE A 92  ? 0.37518 0.43050 0.32246 0.03657  -0.04018 0.01964  92  PHE A CA    
707  C C     . PHE A 92  ? 0.40042 0.44899 0.35977 0.04285  -0.03079 0.02802  92  PHE A C     
708  O O     . PHE A 92  ? 0.40044 0.43218 0.35435 0.04230  -0.02181 0.02967  92  PHE A O     
709  C CB    . PHE A 92  ? 0.40965 0.47127 0.37173 0.02536  -0.04159 0.00940  92  PHE A CB    
710  C CG    . PHE A 92  ? 0.40513 0.44909 0.36717 0.01871  -0.03135 0.00578  92  PHE A CG    
711  C CD1   . PHE A 92  ? 0.48196 0.51194 0.42983 0.01288  -0.03015 -0.00031 92  PHE A CD1   
712  C CD2   . PHE A 92  ? 0.31509 0.35620 0.29022 0.01896  -0.02326 0.00831  92  PHE A CD2   
713  C CE1   . PHE A 92  ? 0.48774 0.50288 0.43577 0.00837  -0.02251 -0.00165 92  PHE A CE1   
714  C CE2   . PHE A 92  ? 0.37362 0.39969 0.34511 0.01322  -0.01597 0.00562  92  PHE A CE2   
715  C CZ    . PHE A 92  ? 0.41421 0.42822 0.37283 0.00834  -0.01639 0.00167  92  PHE A CZ    
716  N N     . GLU A 93  ? 0.36391 0.42616 0.34127 0.04886  -0.03309 0.03266  93  GLU A N     
717  C CA    . GLU A 93  ? 0.30918 0.36313 0.29954 0.05454  -0.02318 0.03821  93  GLU A CA    
718  C C     . GLU A 93  ? 0.36775 0.42292 0.37409 0.04737  -0.01688 0.03014  93  GLU A C     
719  O O     . GLU A 93  ? 0.30881 0.37745 0.32357 0.04040  -0.02099 0.02347  93  GLU A O     
720  C CB    . GLU A 93  ? 0.38218 0.44712 0.38350 0.06786  -0.02671 0.04912  93  GLU A CB    
721  C CG    . GLU A 93  ? 0.53256 0.59277 0.51339 0.07588  -0.03101 0.05971  93  GLU A CG    
722  C CD    . GLU A 93  ? 0.71861 0.78469 0.70797 0.09111  -0.03338 0.07394  93  GLU A CD    
723  O OE1   . GLU A 93  ? 0.78347 0.86086 0.79831 0.09634  -0.03287 0.07462  93  GLU A OE1   
724  O OE2   . GLU A 93  ? 0.64480 0.70333 0.61515 0.09876  -0.03455 0.08545  93  GLU A OE2   
725  N N     . TYR A 94  ? 0.41088 0.45072 0.42002 0.04830  -0.00616 0.03047  94  TYR A N     
726  C CA    . TYR A 94  ? 0.34630 0.38294 0.36285 0.04157  0.00159  0.02284  94  TYR A CA    
727  C C     . TYR A 94  ? 0.35630 0.37959 0.37841 0.04715  0.01190  0.02426  94  TYR A C     
728  O O     . TYR A 94  ? 0.36267 0.37558 0.38200 0.05388  0.01328  0.03089  94  TYR A O     
729  C CB    . TYR A 94  ? 0.30772 0.33255 0.30858 0.03083  0.00221  0.01671  94  TYR A CB    
730  C CG    . TYR A 94  ? 0.29604 0.32416 0.30115 0.02245  0.00601  0.01010  94  TYR A CG    
731  C CD1   . TYR A 94  ? 0.33073 0.37449 0.34466 0.01752  0.00124  0.00745  94  TYR A CD1   
732  C CD2   . TYR A 94  ? 0.34819 0.36335 0.34743 0.01863  0.01459  0.00645  94  TYR A CD2   
733  C CE1   . TYR A 94  ? 0.32608 0.37149 0.34485 0.00892  0.00701  0.00279  94  TYR A CE1   
734  C CE2   . TYR A 94  ? 0.37201 0.38856 0.37140 0.01120  0.01978  0.00216  94  TYR A CE2   
735  C CZ    . TYR A 94  ? 0.30801 0.33923 0.31819 0.00638  0.01697  0.00110  94  TYR A CZ    
736  O OH    . TYR A 94  ? 0.38330 0.41450 0.39459 -0.00180 0.02427  -0.00177 94  TYR A OH    
737  N N     . THR A 95  ? 0.30467 0.32681 0.33391 0.04407  0.02036  0.01778  95  THR A N     
738  C CA    . THR A 95  ? 0.38312 0.38913 0.41423 0.04759  0.03146  0.01531  95  THR A CA    
739  C C     . THR A 95  ? 0.34576 0.33739 0.36048 0.03696  0.03628  0.00635  95  THR A C     
740  O O     . THR A 95  ? 0.37519 0.37319 0.38748 0.03052  0.03824  0.00176  95  THR A O     
741  C CB    . THR A 95  ? 0.36022 0.37714 0.41333 0.05612  0.03915  0.01525  95  THR A CB    
742  O OG1   . THR A 95  ? 0.40683 0.43809 0.47522 0.06770  0.03240  0.02535  95  THR A OG1   
743  C CG2   . THR A 95  ? 0.37719 0.37308 0.42961 0.05972  0.05227  0.01043  95  THR A CG2   
744  N N     . PHE A 96  ? 0.34899 0.32181 0.35268 0.03477  0.03773  0.00453  96  PHE A N     
745  C CA    . PHE A 96  ? 0.39262 0.35215 0.38001 0.02570  0.04031  -0.00403 96  PHE A CA    
746  C C     . PHE A 96  ? 0.42744 0.37513 0.41580 0.02791  0.05213  -0.01169 96  PHE A C     
747  O O     . PHE A 96  ? 0.39565 0.33109 0.39087 0.03315  0.05672  -0.01160 96  PHE A O     
748  C CB    . PHE A 96  ? 0.34520 0.29373 0.32379 0.02114  0.03455  -0.00336 96  PHE A CB    
749  C CG    . PHE A 96  ? 0.39794 0.35543 0.37288 0.01890  0.02520  0.00228  96  PHE A CG    
750  C CD1   . PHE A 96  ? 0.34055 0.31045 0.31439 0.01783  0.02146  0.00364  96  PHE A CD1   
751  C CD2   . PHE A 96  ? 0.35875 0.31108 0.33253 0.01730  0.02159  0.00533  96  PHE A CD2   
752  C CE1   . PHE A 96  ? 0.33823 0.31249 0.30729 0.01608  0.01426  0.00699  96  PHE A CE1   
753  C CE2   . PHE A 96  ? 0.38372 0.34304 0.35408 0.01639  0.01534  0.00954  96  PHE A CE2   
754  C CZ    . PHE A 96  ? 0.33750 0.30636 0.30413 0.01620  0.01167  0.00987  96  PHE A CZ    
755  N N     . ASP A 97  ? 0.42062 0.36950 0.40085 0.02394  0.05865  -0.01841 97  ASP A N     
756  C CA    . ASP A 97  ? 0.38126 0.31840 0.36081 0.02707  0.07220  -0.02700 97  ASP A CA    
757  C C     . ASP A 97  ? 0.46428 0.39040 0.41792 0.01836  0.07721  -0.03728 97  ASP A C     
758  O O     . ASP A 97  ? 0.43478 0.35446 0.38538 0.02085  0.09102  -0.04506 97  ASP A O     
759  C CB    . ASP A 97  ? 0.38588 0.33858 0.38876 0.03664  0.08153  -0.02412 97  ASP A CB    
760  C CG    . ASP A 97  ? 0.41771 0.39011 0.42332 0.03190  0.08124  -0.02195 97  ASP A CG    
761  O OD1   . ASP A 97  ? 0.41842 0.38975 0.40655 0.02235  0.07367  -0.02140 97  ASP A OD1   
762  O OD2   . ASP A 97  ? 0.47257 0.46141 0.49997 0.03773  0.08908  -0.02052 97  ASP A OD2   
763  N N     . TYR A 98  ? 0.42939 0.35278 0.36322 0.00931  0.06695  -0.03732 98  TYR A N     
764  C CA    . TYR A 98  ? 0.46905 0.38252 0.37403 0.00173  0.06941  -0.04510 98  TYR A CA    
765  C C     . TYR A 98  ? 0.47305 0.36830 0.36269 -0.00301 0.06528  -0.05499 98  TYR A C     
766  O O     . TYR A 98  ? 0.43836 0.33355 0.32869 -0.00709 0.05227  -0.05244 98  TYR A O     
767  C CB    . TYR A 98  ? 0.43533 0.35640 0.32769 -0.00431 0.05991  -0.03812 98  TYR A CB    
768  C CG    . TYR A 98  ? 0.53344 0.44425 0.39270 -0.01091 0.06139  -0.04313 98  TYR A CG    
769  C CD1   . TYR A 98  ? 0.41868 0.32629 0.26582 -0.01090 0.07696  -0.04748 98  TYR A CD1   
770  C CD2   . TYR A 98  ? 0.57628 0.48179 0.41626 -0.01646 0.04752  -0.04278 98  TYR A CD2   
771  C CE1   . TYR A 98  ? 0.49146 0.38837 0.30296 -0.01647 0.07911  -0.05102 98  TYR A CE1   
772  C CE2   . TYR A 98  ? 0.55619 0.45268 0.36226 -0.02151 0.04710  -0.04612 98  TYR A CE2   
773  C CZ    . TYR A 98  ? 0.52851 0.41953 0.31800 -0.02159 0.06309  -0.05002 98  TYR A CZ    
774  O OH    . TYR A 98  ? 0.61113 0.49202 0.36203 -0.02616 0.06349  -0.05220 98  TYR A OH    
775  N N     . GLN A 99  ? 0.51960 0.39989 0.39600 -0.00314 0.07681  -0.06723 99  GLN A N     
776  C CA    . GLN A 99  ? 0.53617 0.39724 0.39638 -0.00949 0.07342  -0.08010 99  GLN A CA    
777  C C     . GLN A 99  ? 0.60788 0.46365 0.49199 -0.00808 0.06877  -0.07836 99  GLN A C     
778  O O     . GLN A 99  ? 0.58392 0.43360 0.46397 -0.01619 0.05782  -0.08254 99  GLN A O     
779  C CB    . GLN A 99  ? 0.62584 0.48721 0.45784 -0.01954 0.05903  -0.08213 99  GLN A CB    
780  C CG    . GLN A 99  ? 0.59669 0.45466 0.39554 -0.02190 0.06585  -0.08630 99  GLN A CG    
781  C CD    . GLN A 99  ? 0.82032 0.67909 0.59050 -0.02997 0.04950  -0.08561 99  GLN A CD    
782  O OE1   . GLN A 99  ? 0.81212 0.67784 0.59225 -0.03326 0.03276  -0.08121 99  GLN A OE1   
783  N NE2   . GLN A 99  ? 1.04915 0.90154 0.78367 -0.03246 0.05468  -0.08905 99  GLN A NE2   
784  N N     . MET A 100 ? 0.46240 0.32149 0.37267 0.00232  0.07724  -0.07123 100 MET A N     
785  C CA    . MET A 100 ? 0.51070 0.36353 0.44279 0.00537  0.07519  -0.06616 100 MET A CA    
786  C C     . MET A 100 ? 0.54822 0.40216 0.50304 0.01934  0.08746  -0.05985 100 MET A C     
787  O O     . MET A 100 ? 0.56487 0.43367 0.52467 0.02579  0.09307  -0.05616 100 MET A O     
788  C CB    . MET A 100 ? 0.44411 0.31250 0.38506 0.00288  0.06095  -0.05348 100 MET A CB    
789  C CG    . MET A 100 ? 0.43986 0.33020 0.38810 0.00901  0.05850  -0.04150 100 MET A CG    
790  S SD    . MET A 100 ? 0.47177 0.37657 0.42278 0.00516  0.04335  -0.03067 100 MET A SD    
791  C CE    . MET A 100 ? 0.43023 0.33008 0.40280 0.01178  0.04559  -0.02178 100 MET A CE    
792  N N     . THR A 101 ? 0.55599 0.39404 0.52590 0.02388  0.09194  -0.05839 101 THR A N     
793  C CA    . THR A 101 ? 0.47643 0.31705 0.47047 0.03922  0.10041  -0.04813 101 THR A CA    
794  C C     . THR A 101 ? 0.48570 0.35528 0.49112 0.04456  0.09070  -0.03207 101 THR A C     
795  O O     . THR A 101 ? 0.45165 0.32882 0.45278 0.03825  0.07865  -0.02562 101 THR A O     
796  C CB    . THR A 101 ? 0.54000 0.35781 0.54629 0.04194  0.10399  -0.04491 101 THR A CB    
797  O OG1   . THR A 101 ? 0.65730 0.44625 0.65286 0.03532  0.11298  -0.06256 101 THR A OG1   
798  C CG2   . THR A 101 ? 0.51684 0.33639 0.54723 0.06002  0.11153  -0.03143 101 THR A CG2   
799  N N     . PRO A 102 ? 0.45134 0.33812 0.47176 0.05537  0.09544  -0.02653 102 PRO A N     
800  C CA    . PRO A 102 ? 0.44260 0.35708 0.47276 0.05848  0.08448  -0.01362 102 PRO A CA    
801  C C     . PRO A 102 ? 0.47610 0.38899 0.51215 0.06237  0.07608  -0.00077 102 PRO A C     
802  O O     . PRO A 102 ? 0.44597 0.34571 0.49358 0.07200  0.08169  0.00520  102 PRO A O     
803  C CB    . PRO A 102 ? 0.42625 0.35762 0.47854 0.07079  0.09229  -0.01055 102 PRO A CB    
804  C CG    . PRO A 102 ? 0.49065 0.40538 0.53869 0.07147  0.10891  -0.02414 102 PRO A CG    
805  C CD    . PRO A 102 ? 0.53308 0.41576 0.56570 0.06593  0.11119  -0.03181 102 PRO A CD    
806  N N     . THR A 103 ? 0.42405 0.34819 0.45075 0.05521  0.06405  0.00383  103 THR A N     
807  C CA    . THR A 103 ? 0.41803 0.33913 0.44469 0.05673  0.05778  0.01477  103 THR A CA    
808  C C     . THR A 103 ? 0.40801 0.35277 0.43455 0.05908  0.04677  0.02374  103 THR A C     
809  O O     . THR A 103 ? 0.37379 0.32936 0.39109 0.05075  0.04049  0.01923  103 THR A O     
810  C CB    . THR A 103 ? 0.45862 0.36572 0.47273 0.04430  0.05556  0.00932  103 THR A CB    
811  O OG1   . THR A 103 ? 0.49899 0.38299 0.51280 0.04083  0.06460  -0.00074 103 THR A OG1   
812  C CG2   . THR A 103 ? 0.46054 0.36612 0.47620 0.04586  0.05200  0.02135  103 THR A CG2   
813  N N     . LYS A 104 ? 0.41505 0.36602 0.45016 0.07050  0.04421  0.03640  104 LYS A N     
814  C CA    . LYS A 104 ? 0.42907 0.40152 0.46120 0.07290  0.03265  0.04392  104 LYS A CA    
815  C C     . LYS A 104 ? 0.38709 0.35367 0.40287 0.06685  0.02827  0.04757  104 LYS A C     
816  O O     . LYS A 104 ? 0.35885 0.30810 0.37218 0.06760  0.03375  0.05296  104 LYS A O     
817  C CB    . LYS A 104 ? 0.51787 0.50058 0.56284 0.08838  0.02998  0.05660  104 LYS A CB    
818  C CG    . LYS A 104 ? 0.69575 0.70758 0.74254 0.09050  0.01658  0.05973  104 LYS A CG    
819  C CD    . LYS A 104 ? 0.89582 0.92230 0.95846 0.10679  0.01175  0.07202  104 LYS A CD    
820  C CE    . LYS A 104 ? 0.98533 1.02270 1.03231 0.11108  -0.00177 0.08299  104 LYS A CE    
821  N NZ    . LYS A 104 ? 0.98338 1.03939 1.04445 0.12763  -0.01035 0.09607  104 LYS A NZ    
822  N N     . VAL A 105 ? 0.31373 0.29395 0.31989 0.06067  0.01987  0.04446  105 VAL A N     
823  C CA    . VAL A 105 ? 0.38946 0.36536 0.38131 0.05556  0.01739  0.04641  105 VAL A CA    
824  C C     . VAL A 105 ? 0.37607 0.36829 0.35837 0.05717  0.00767  0.04881  105 VAL A C     
825  O O     . VAL A 105 ? 0.38575 0.39397 0.37350 0.05808  0.00122  0.04589  105 VAL A O     
826  C CB    . VAL A 105 ? 0.33521 0.30433 0.32227 0.04385  0.01875  0.03636  105 VAL A CB    
827  C CG1   . VAL A 105 ? 0.37791 0.33037 0.37100 0.04042  0.02656  0.03194  105 VAL A CG1   
828  C CG2   . VAL A 105 ? 0.35652 0.33679 0.34199 0.03839  0.01404  0.02800  105 VAL A CG2   
829  N N     . LYS A 106 ? 0.36852 0.35667 0.33700 0.05684  0.00735  0.05326  106 LYS A N     
830  C CA    . LYS A 106 ? 0.36242 0.36146 0.31679 0.05582  -0.00059 0.05148  106 LYS A CA    
831  C C     . LYS A 106 ? 0.36870 0.36257 0.31768 0.04652  0.00104  0.04285  106 LYS A C     
832  O O     . LYS A 106 ? 0.35444 0.33759 0.30496 0.04374  0.00787  0.04373  106 LYS A O     
833  C CB    . LYS A 106 ? 0.43244 0.43054 0.37104 0.06369  -0.00103 0.06249  106 LYS A CB    
834  C CG    . LYS A 106 ? 0.56894 0.57620 0.48873 0.06205  -0.00893 0.05787  106 LYS A CG    
835  C CD    . LYS A 106 ? 0.71307 0.72218 0.61271 0.07122  -0.01142 0.06881  106 LYS A CD    
836  C CE    . LYS A 106 ? 0.70903 0.73082 0.61529 0.08040  -0.02052 0.07672  106 LYS A CE    
837  N NZ    . LYS A 106 ? 0.73341 0.75271 0.61880 0.09138  -0.02118 0.09187  106 LYS A NZ    
838  N N     . VAL A 107 ? 0.35556 0.35720 0.30090 0.04162  -0.00530 0.03474  107 VAL A N     
839  C CA    . VAL A 107 ? 0.31911 0.31475 0.26078 0.03431  -0.00409 0.02745  107 VAL A CA    
840  C C     . VAL A 107 ? 0.36131 0.35809 0.28737 0.03450  -0.00730 0.02466  107 VAL A C     
841  O O     . VAL A 107 ? 0.38679 0.39258 0.30634 0.03547  -0.01449 0.02260  107 VAL A O     
842  C CB    . VAL A 107 ? 0.34698 0.34487 0.29676 0.02756  -0.00598 0.02013  107 VAL A CB    
843  C CG1   . VAL A 107 ? 0.33960 0.32941 0.28379 0.02177  -0.00534 0.01505  107 VAL A CG1   
844  C CG2   . VAL A 107 ? 0.37379 0.36859 0.33488 0.02764  -0.00116 0.02109  107 VAL A CG2   
845  N N     . HIS A 108 ? 0.33635 0.32471 0.25726 0.03360  -0.00209 0.02372  108 HIS A N     
846  C CA    . HIS A 108 ? 0.36374 0.34933 0.26971 0.03388  -0.00232 0.01882  108 HIS A CA    
847  C C     . HIS A 108 ? 0.37019 0.34820 0.28141 0.02930  -0.00049 0.01290  108 HIS A C     
848  O O     . HIS A 108 ? 0.40355 0.37807 0.32379 0.02974  0.00453  0.01600  108 HIS A O     
849  C CB    . HIS A 108 ? 0.40136 0.38386 0.29622 0.04008  0.00512  0.02510  108 HIS A CB    
850  C CG    . HIS A 108 ? 0.42287 0.40112 0.29917 0.04149  0.00693  0.01884  108 HIS A CG    
851  N ND1   . HIS A 108 ? 0.45802 0.43155 0.32572 0.04629  0.01758  0.02228  108 HIS A ND1   
852  C CD2   . HIS A 108 ? 0.39006 0.36679 0.25482 0.03834  0.00077  0.00834  108 HIS A CD2   
853  C CE1   . HIS A 108 ? 0.43493 0.40341 0.28435 0.04721  0.01836  0.01369  108 HIS A CE1   
854  N NE2   . HIS A 108 ? 0.44429 0.41357 0.29133 0.04194  0.00761  0.00461  108 HIS A NE2   
855  N N     . MET A 109 ? 0.36509 0.34069 0.27208 0.02476  -0.00503 0.00494  109 MET A N     
856  C CA    . MET A 109 ? 0.37718 0.34235 0.28652 0.02193  -0.00302 0.00075  109 MET A CA    
857  C C     . MET A 109 ? 0.37627 0.33280 0.27224 0.02462  0.00014  -0.00520 109 MET A C     
858  O O     . MET A 109 ? 0.39402 0.35124 0.27663 0.02327  -0.00347 -0.01151 109 MET A O     
859  C CB    . MET A 109 ? 0.38402 0.34766 0.29840 0.01433  -0.00740 -0.00342 109 MET A CB    
860  C CG    . MET A 109 ? 0.50901 0.47697 0.43468 0.01198  -0.00743 0.00119  109 MET A CG    
861  S SD    . MET A 109 ? 0.59492 0.55789 0.52392 0.00302  -0.00834 -0.00244 109 MET A SD    
862  C CE    . MET A 109 ? 0.42129 0.39404 0.35096 -0.00174 -0.01352 -0.00952 109 MET A CE    
863  N N     . LYS A 110 ? 0.35329 0.30222 0.25326 0.02861  0.00655  -0.00400 110 LYS A N     
864  C CA    . LYS A 110 ? 0.38665 0.32554 0.27503 0.03284  0.01245  -0.01020 110 LYS A CA    
865  C C     . LYS A 110 ? 0.39347 0.32236 0.29280 0.03594  0.01675  -0.00965 110 LYS A C     
866  O O     . LYS A 110 ? 0.42322 0.35798 0.33861 0.03763  0.01665  -0.00203 110 LYS A O     
867  C CB    . LYS A 110 ? 0.32306 0.26721 0.20291 0.03967  0.02008  -0.00671 110 LYS A CB    
868  C CG    . LYS A 110 ? 0.41823 0.35160 0.27938 0.04426  0.02761  -0.01523 110 LYS A CG    
869  C CD    . LYS A 110 ? 0.50115 0.43976 0.34594 0.04969  0.03469  -0.01165 110 LYS A CD    
870  C CE    . LYS A 110 ? 0.49361 0.41993 0.31327 0.05345  0.04185  -0.02272 110 LYS A CE    
871  N NZ    . LYS A 110 ? 0.45499 0.38542 0.25496 0.05956  0.05115  -0.01768 110 LYS A NZ    
872  N N     . LYS A 111 ? 0.44628 0.35962 0.33677 0.03692  0.01989  -0.01803 111 LYS A N     
873  C CA    . LYS A 111 ? 0.40271 0.30421 0.30337 0.04258  0.02487  -0.01676 111 LYS A CA    
874  C C     . LYS A 111 ? 0.41476 0.32405 0.32607 0.05278  0.03398  -0.01161 111 LYS A C     
875  O O     . LYS A 111 ? 0.45066 0.36468 0.35253 0.05604  0.04100  -0.01369 111 LYS A O     
876  C CB    . LYS A 111 ? 0.46826 0.34769 0.35606 0.04170  0.02821  -0.02823 111 LYS A CB    
877  C CG    . LYS A 111 ? 0.53423 0.39676 0.43266 0.04793  0.03282  -0.02602 111 LYS A CG    
878  C CD    . LYS A 111 ? 0.66473 0.50050 0.54975 0.04543  0.03697  -0.03883 111 LYS A CD    
879  C CE    . LYS A 111 ? 0.64748 0.47924 0.51291 0.04777  0.04390  -0.05179 111 LYS A CE    
880  N NZ    . LYS A 111 ? 0.75084 0.55239 0.60486 0.04814  0.05097  -0.06571 111 LYS A NZ    
881  N N     . ALA A 112 ? 0.40366 0.31554 0.33514 0.05785  0.03393  -0.00423 112 ALA A N     
882  C CA    . ALA A 112 ? 0.44758 0.37033 0.39646 0.06726  0.04249  0.00071  112 ALA A CA    
883  C C     . ALA A 112 ? 0.54219 0.45111 0.48511 0.07651  0.05529  -0.00662 112 ALA A C     
884  O O     . ALA A 112 ? 0.48856 0.37630 0.41721 0.07597  0.05591  -0.01502 112 ALA A O     
885  C CB    . ALA A 112 ? 0.40429 0.33650 0.37802 0.07028  0.03609  0.01021  112 ALA A CB    
886  N N     . LEU A 113 ? 0.52824 0.44847 0.48331 0.08468  0.06708  -0.00398 113 LEU A N     
887  C CA    . LEU A 113 ? 0.51069 0.41829 0.45867 0.09455  0.08254  -0.01187 113 LEU A CA    
888  C C     . LEU A 113 ? 0.52726 0.41643 0.48369 0.10189  0.08304  -0.01422 113 LEU A C     
889  O O     . LEU A 113 ? 0.57864 0.44420 0.51668 0.10468  0.09058  -0.02574 113 LEU A O     
890  C CB    . LEU A 113 ? 0.48222 0.40844 0.44943 0.10267  0.09678  -0.00622 113 LEU A CB    
891  C CG    . LEU A 113 ? 0.51641 0.43279 0.47822 0.11449  0.11700  -0.01380 113 LEU A CG    
892  C CD1   . LEU A 113 ? 0.54600 0.44175 0.46431 0.11109  0.12200  -0.02754 113 LEU A CD1   
893  C CD2   . LEU A 113 ? 0.50155 0.44126 0.48637 0.12010  0.13146  -0.00588 113 LEU A CD2   
894  N N     . SER A 114 ? 0.55287 0.45074 0.53531 0.10499  0.07455  -0.00348 114 SER A N     
895  C CA    . SER A 114 ? 0.60715 0.48680 0.59853 0.11386  0.07470  -0.00224 114 SER A CA    
896  C C     . SER A 114 ? 0.68369 0.53727 0.65295 0.10490  0.06685  -0.00737 114 SER A C     
897  O O     . SER A 114 ? 0.71537 0.54634 0.68682 0.11132  0.06921  -0.00742 114 SER A O     
898  C CB    . SER A 114 ? 0.56449 0.46358 0.58843 0.12039  0.06575  0.01242  114 SER A CB    
899  O OG    . SER A 114 ? 0.66706 0.57953 0.68902 0.10850  0.05004  0.01870  114 SER A OG    
900  N N     . GLY A 115 ? 0.57738 0.43365 0.52814 0.09056  0.05841  -0.01086 115 GLY A N     
901  C CA    . GLY A 115 ? 0.66220 0.49725 0.59495 0.08018  0.05253  -0.01680 115 GLY A CA    
902  C C     . GLY A 115 ? 0.67383 0.50461 0.61433 0.07706  0.04239  -0.00601 115 GLY A C     
903  O O     . GLY A 115 ? 0.85314 0.66552 0.78121 0.06781  0.03954  -0.00982 115 GLY A O     
904  N N     . ASP A 116 ? 0.57188 0.41950 0.53170 0.08363  0.03679  0.00721  116 ASP A N     
905  C CA    . ASP A 116 ? 0.62849 0.47177 0.59069 0.08177  0.02689  0.01841  116 ASP A CA    
906  C C     . ASP A 116 ? 0.63809 0.50510 0.60194 0.07373  0.01568  0.02477  116 ASP A C     
907  O O     . ASP A 116 ? 0.59179 0.45759 0.55451 0.07235  0.00724  0.03421  116 ASP A O     
908  C CB    . ASP A 116 ? 0.66955 0.50883 0.65019 0.09751  0.02731  0.02916  116 ASP A CB    
909  C CG    . ASP A 116 ? 0.92160 0.78941 0.92718 0.10755  0.02799  0.03326  116 ASP A CG    
910  O OD1   . ASP A 116 ? 0.93219 0.81606 0.93810 0.10318  0.03262  0.02628  116 ASP A OD1   
911  O OD2   . ASP A 116 ? 1.00079 0.87557 1.02689 0.11988  0.02402  0.04421  116 ASP A OD2   
912  N N     . SER A 117 ? 0.53057 0.41707 0.49543 0.06894  0.01610  0.02016  117 SER A N     
913  C CA    . SER A 117 ? 0.39794 0.30185 0.36179 0.05997  0.00745  0.02329  117 SER A CA    
914  C C     . SER A 117 ? 0.42353 0.33261 0.37694 0.05242  0.01104  0.01475  117 SER A C     
915  O O     . SER A 117 ? 0.45347 0.35488 0.39917 0.05419  0.01872  0.00694  117 SER A O     
916  C CB    . SER A 117 ? 0.46524 0.39207 0.44963 0.06459  0.00208  0.03073  117 SER A CB    
917  O OG    . SER A 117 ? 0.52505 0.46376 0.52360 0.07041  0.01062  0.02826  117 SER A OG    
918  N N     . TYR A 118 ? 0.38404 0.30526 0.33557 0.04459  0.00526  0.01619  118 TYR A N     
919  C CA    . TYR A 118 ? 0.39417 0.31865 0.33493 0.03776  0.00654  0.01008  118 TYR A CA    
920  C C     . TYR A 118 ? 0.39375 0.33546 0.34183 0.03527  0.00420  0.01351  118 TYR A C     
921  O O     . TYR A 118 ? 0.42339 0.37127 0.37858 0.03322  -0.00146 0.01811  118 TYR A O     
922  C CB    . TYR A 118 ? 0.43209 0.34639 0.36125 0.02913  0.00320  0.00684  118 TYR A CB    
923  C CG    . TYR A 118 ? 0.43339 0.32685 0.35760 0.03028  0.00601  0.00448  118 TYR A CG    
924  C CD1   . TYR A 118 ? 0.46267 0.34594 0.38969 0.03291  0.00406  0.01219  118 TYR A CD1   
925  C CD2   . TYR A 118 ? 0.49339 0.37549 0.40879 0.02922  0.01062  -0.00532 118 TYR A CD2   
926  C CE1   . TYR A 118 ? 0.44074 0.30085 0.36406 0.03506  0.00809  0.01153  118 TYR A CE1   
927  C CE2   . TYR A 118 ? 0.48620 0.34496 0.39786 0.02986  0.01452  -0.00868 118 TYR A CE2   
928  C CZ    . TYR A 118 ? 0.49568 0.34261 0.41242 0.03308  0.01396  0.00044  118 TYR A CZ    
929  O OH    . TYR A 118 ? 0.54400 0.36425 0.45750 0.03440  0.01912  -0.00169 118 TYR A OH    
930  N N     . TRP A 119 ? 0.36531 0.31295 0.30976 0.03540  0.00862  0.01119  119 TRP A N     
931  C CA    . TRP A 119 ? 0.38834 0.34818 0.33972 0.03328  0.00844  0.01493  119 TRP A CA    
932  C C     . TRP A 119 ? 0.37218 0.33263 0.31449 0.02759  0.00486  0.01316  119 TRP A C     
933  O O     . TRP A 119 ? 0.36070 0.31721 0.29137 0.02631  0.00422  0.00865  119 TRP A O     
934  C CB    . TRP A 119 ? 0.40876 0.37406 0.36239 0.03821  0.01733  0.01654  119 TRP A CB    
935  C CG    . TRP A 119 ? 0.41345 0.38308 0.38267 0.04438  0.02311  0.01902  119 TRP A CG    
936  C CD1   . TRP A 119 ? 0.38694 0.35032 0.35324 0.05151  0.03041  0.01598  119 TRP A CD1   
937  C CD2   . TRP A 119 ? 0.34918 0.33178 0.34211 0.04410  0.02235  0.02435  119 TRP A CD2   
938  N NE1   . TRP A 119 ? 0.46871 0.44193 0.45776 0.05712  0.03506  0.02027  119 TRP A NE1   
939  C CE2   . TRP A 119 ? 0.39939 0.38612 0.40616 0.05202  0.02917  0.02551  119 TRP A CE2   
940  C CE3   . TRP A 119 ? 0.40100 0.39211 0.40577 0.03753  0.01642  0.02709  119 TRP A CE3   
941  C CZ2   . TRP A 119 ? 0.45855 0.46184 0.49426 0.05339  0.02919  0.03036  119 TRP A CZ2   
942  C CZ3   . TRP A 119 ? 0.35606 0.36130 0.38661 0.03735  0.01559  0.03047  119 TRP A CZ3   
943  C CH2   . TRP A 119 ? 0.37292 0.38604 0.42028 0.04513  0.02136  0.03257  119 TRP A CH2   
944  N N     . VAL A 120 ? 0.33462 0.30062 0.28389 0.02422  0.00243  0.01594  120 VAL A N     
945  C CA    . VAL A 120 ? 0.38813 0.35665 0.33382 0.02142  0.00145  0.01560  120 VAL A CA    
946  C C     . VAL A 120 ? 0.40111 0.37409 0.35462 0.02297  0.00560  0.02018  120 VAL A C     
947  O O     . VAL A 120 ? 0.38605 0.36065 0.35079 0.02067  0.00552  0.02155  120 VAL A O     
948  C CB    . VAL A 120 ? 0.40972 0.37642 0.35525 0.01610  -0.00254 0.01384  120 VAL A CB    
949  C CG1   . VAL A 120 ? 0.37616 0.34672 0.32196 0.01511  -0.00182 0.01344  120 VAL A CG1   
950  C CG2   . VAL A 120 ? 0.36743 0.32738 0.30594 0.01379  -0.00466 0.01122  120 VAL A CG2   
951  N N     . PHE A 121 ? 0.37136 0.34584 0.31858 0.02647  0.00885  0.02281  121 PHE A N     
952  C CA    . PHE A 121 ? 0.42222 0.39749 0.37494 0.02845  0.01470  0.02930  121 PHE A CA    
953  C C     . PHE A 121 ? 0.41091 0.38554 0.36331 0.02890  0.01312  0.03136  121 PHE A C     
954  O O     . PHE A 121 ? 0.33345 0.31139 0.27847 0.03032  0.00843  0.02939  121 PHE A O     
955  C CB    . PHE A 121 ? 0.31920 0.29492 0.26217 0.03405  0.02128  0.03351  121 PHE A CB    
956  C CG    . PHE A 121 ? 0.37254 0.34861 0.31639 0.03564  0.02514  0.03078  121 PHE A CG    
957  C CD1   . PHE A 121 ? 0.31387 0.29361 0.27667 0.03404  0.02882  0.03251  121 PHE A CD1   
958  C CD2   . PHE A 121 ? 0.37218 0.34533 0.29970 0.03886  0.02502  0.02582  121 PHE A CD2   
959  C CE1   . PHE A 121 ? 0.37870 0.36071 0.34670 0.03750  0.03307  0.03090  121 PHE A CE1   
960  C CE2   . PHE A 121 ? 0.44321 0.41440 0.37255 0.04195  0.03057  0.02294  121 PHE A CE2   
961  C CZ    . PHE A 121 ? 0.42729 0.40373 0.37828 0.04225  0.03508  0.02633  121 PHE A CZ    
962  N N     . VAL A 122 ? 0.32879 0.29939 0.29164 0.02768  0.01738  0.03501  122 VAL A N     
963  C CA    . VAL A 122 ? 0.40910 0.37613 0.37536 0.02876  0.01748  0.03616  122 VAL A CA    
964  C C     . VAL A 122 ? 0.33402 0.29383 0.30524 0.03188  0.02535  0.04502  122 VAL A C     
965  O O     . VAL A 122 ? 0.38997 0.34593 0.37013 0.02785  0.03084  0.04667  122 VAL A O     
966  C CB    . VAL A 122 ? 0.39380 0.35702 0.36719 0.02241  0.01551  0.02870  122 VAL A CB    
967  C CG1   . VAL A 122 ? 0.34362 0.30148 0.32110 0.02496  0.01835  0.02900  122 VAL A CG1   
968  C CG2   . VAL A 122 ? 0.37860 0.34628 0.34566 0.01902  0.00930  0.02213  122 VAL A CG2   
969  N N     . LYS A 123 ? 0.34731 0.30557 0.31493 0.03901  0.02603  0.05150  123 LYS A N     
970  C CA    . LYS A 123 ? 0.38980 0.33657 0.36292 0.04252  0.03432  0.06109  123 LYS A CA    
971  C C     . LYS A 123 ? 0.41871 0.36248 0.39598 0.04915  0.03319  0.06331  123 LYS A C     
972  O O     . LYS A 123 ? 0.37510 0.33039 0.34953 0.05267  0.02579  0.06020  123 LYS A O     
973  C CB    . LYS A 123 ? 0.37975 0.32606 0.34103 0.04841  0.03944  0.07302  123 LYS A CB    
974  C CG    . LYS A 123 ? 0.44406 0.39873 0.38852 0.05807  0.03279  0.07875  123 LYS A CG    
975  C CD    . LYS A 123 ? 0.44564 0.39584 0.37404 0.06462  0.03953  0.09239  123 LYS A CD    
976  C CE    . LYS A 123 ? 0.43780 0.39769 0.34597 0.07454  0.03011  0.09815  123 LYS A CE    
977  N NZ    . LYS A 123 ? 0.46750 0.41942 0.35759 0.08297  0.03726  0.11496  123 LYS A NZ    
978  N N     . ARG A 124 ? 0.37175 0.29978 0.35863 0.05063  0.04145  0.06841  124 ARG A N     
979  C CA    . ARG A 124 ? 0.37880 0.30164 0.37257 0.05898  0.04260  0.07123  124 ARG A CA    
980  C C     . ARG A 124 ? 0.42917 0.35975 0.41436 0.07212  0.03895  0.08524  124 ARG A C     
981  O O     . ARG A 124 ? 0.45981 0.39117 0.43172 0.07445  0.03969  0.09474  124 ARG A O     
982  C CB    A ARG A 124 ? 0.39689 0.29623 0.40295 0.05719  0.05362  0.07234  124 ARG A CB    
983  C CB    B ARG A 124 ? 0.39567 0.29505 0.40161 0.05700  0.05363  0.07237  124 ARG A CB    
984  C CG    A ARG A 124 ? 0.47582 0.36743 0.48944 0.04424  0.05514  0.05625  124 ARG A CG    
985  C CG    B ARG A 124 ? 0.48120 0.37331 0.49370 0.04227  0.05572  0.05901  124 ARG A CG    
986  C CD    A ARG A 124 ? 0.56155 0.42749 0.58688 0.04272  0.06575  0.05474  124 ARG A CD    
987  C CD    B ARG A 124 ? 0.54540 0.41263 0.57004 0.03817  0.06671  0.05974  124 ARG A CD    
988  N NE    A ARG A 124 ? 0.55231 0.40975 0.58231 0.02841  0.06625  0.03920  124 ARG A NE    
989  N NE    B ARG A 124 ? 0.55608 0.41814 0.58764 0.02325  0.06619  0.04511  124 ARG A NE    
990  C CZ    A ARG A 124 ? 0.62226 0.47253 0.65190 0.02533  0.06663  0.02515  124 ARG A CZ    
991  C CZ    B ARG A 124 ? 0.52452 0.38404 0.56481 0.01272  0.06900  0.04522  124 ARG A CZ    
992  N NH1   A ARG A 124 ? 0.64955 0.50069 0.67824 0.03567  0.06856  0.02449  124 ARG A NH1   
993  N NH1   B ARG A 124 ? 0.55688 0.41688 0.59892 0.01515  0.07521  0.05940  124 ARG A NH1   
994  N NH2   A ARG A 124 ? 0.65186 0.49504 0.68222 0.01158  0.06514  0.01116  124 ARG A NH2   
995  N NH2   B ARG A 124 ? 0.48861 0.34621 0.53615 -0.00072 0.06561  0.03078  124 ARG A NH2   
996  N N     . VAL A 125 ? 0.38556 0.32354 0.37804 0.08106  0.03478  0.08645  125 VAL A N     
997  C CA    . VAL A 125 ? 0.35114 0.29828 0.33818 0.09506  0.02905  0.10078  125 VAL A CA    
998  C C     . VAL A 125 ? 0.49737 0.43525 0.50126 0.10681  0.03416  0.10787  125 VAL A C     
999  O O     . VAL A 125 ? 0.48547 0.41340 0.50409 0.10312  0.04116  0.09782  125 VAL A O     
1000 C CB    . VAL A 125 ? 0.42182 0.39623 0.40335 0.09578  0.01468  0.09581  125 VAL A CB    
1001 C CG1   . VAL A 125 ? 0.49136 0.47065 0.45547 0.08583  0.01119  0.08902  125 VAL A CG1   
1002 C CG2   . VAL A 125 ? 0.44369 0.42922 0.44355 0.09300  0.01252  0.08373  125 VAL A CG2   
1003 O OXT   . VAL A 125 ? 0.45547 0.39441 0.45781 0.12091  0.03186  0.12367  125 VAL A OXT   
1004 C C1    . HC4 B .   ? 0.39906 0.35218 0.33454 0.00113  0.03877  -0.01529 201 HC4 A C1    
1005 O O1    . HC4 B .   ? 0.42151 0.36759 0.33794 -0.00411 0.04132  -0.01828 201 HC4 A O1    
1006 C C2    . HC4 B .   ? 0.35206 0.30275 0.28857 0.00135  0.02836  -0.01217 201 HC4 A C2    
1007 C C3    . HC4 B .   ? 0.37511 0.31623 0.29901 -0.00286 0.02366  -0.01563 201 HC4 A C3    
1008 C "C1'" . HC4 B .   ? 0.39103 0.33210 0.31930 -0.00363 0.01489  -0.01291 201 HC4 A "C1'" 
1009 C "C2'" . HC4 B .   ? 0.50424 0.43887 0.42244 -0.00905 0.00919  -0.01770 201 HC4 A "C2'" 
1010 C "C3'" . HC4 B .   ? 0.50043 0.43824 0.42739 -0.01054 0.00141  -0.01533 201 HC4 A "C3'" 
1011 C "C4'" . HC4 B .   ? 0.46212 0.40704 0.40421 -0.00605 0.00126  -0.00790 201 HC4 A "C4'" 
1012 C "C5'" . HC4 B .   ? 0.35798 0.30709 0.30454 -0.00039 0.00631  -0.00345 201 HC4 A "C5'" 
1013 C "C6'" . HC4 B .   ? 0.39407 0.34260 0.33567 0.00048  0.01190  -0.00600 201 HC4 A "C6'" 
1014 O "O4'" . HC4 B .   ? 0.40613 0.35520 0.35879 -0.00728 -0.00350 -0.00532 201 HC4 A "O4'" 
1015 O O     . HOH C .   ? 0.68336 0.59230 0.43698 -0.00812 -0.05384 0.03555  301 HOH A O     
1016 O O     . HOH C .   ? 0.69219 0.57325 0.56366 -0.04759 -0.02346 -0.09414 302 HOH A O     
1017 O O     . HOH C .   ? 0.81136 0.66061 0.67902 -0.01827 0.01483  0.04302  303 HOH A O     
1018 O O     . HOH C .   ? 0.62072 0.59069 0.49074 0.07623  0.13326  0.05266  304 HOH A O     
1019 O O     . HOH C .   ? 0.72502 0.58643 0.74717 0.03794  0.08149  0.08964  305 HOH A O     
1020 O O     . HOH C .   ? 0.49309 0.41209 0.33895 -0.03409 0.05815  0.01445  306 HOH A O     
1021 O O     . HOH C .   ? 0.59591 0.50801 0.38996 0.01644  -0.07376 0.06790  307 HOH A O     
1022 O O     . HOH C .   ? 0.60922 0.64537 0.70924 0.07210  -0.02121 0.05014  308 HOH A O     
1023 O O     . HOH C .   ? 0.53747 0.48901 0.33376 0.05703  0.03691  0.00095  309 HOH A O     
1024 O O     . HOH C .   ? 0.79269 0.84985 1.01597 -0.00562 0.22377  0.12411  310 HOH A O     
1025 O O     . HOH C .   ? 0.66990 0.51549 0.70966 0.06397  0.07653  0.05316  311 HOH A O     
1026 O O     . HOH C .   ? 0.46979 0.44326 0.36506 0.04839  0.03449  0.03983  312 HOH A O     
1027 O O     . HOH C .   ? 0.60982 0.47654 0.68515 0.09617  0.09950  0.01654  313 HOH A O     
1028 O O     . HOH C .   ? 0.64612 0.66975 0.62594 -0.06025 -0.04717 -0.05892 314 HOH A O     
1029 O O     . HOH C .   ? 0.64395 0.43063 0.54002 0.02655  0.02937  -0.02888 315 HOH A O     
1030 O O     . HOH C .   ? 0.50587 0.41329 0.54033 0.14408  0.04807  0.13936  316 HOH A O     
1031 O O     . HOH C .   ? 0.59576 0.50449 0.43488 -0.02627 0.00271  -0.04148 317 HOH A O     
1032 O O     . HOH C .   ? 0.62241 0.57864 0.66128 0.10179  0.05850  0.02004  318 HOH A O     
1033 O O     . HOH C .   ? 0.47857 0.45324 0.51333 0.02320  0.11458  0.09197  319 HOH A O     
1034 O O     . HOH C .   ? 0.48412 0.39296 0.51287 0.08017  0.05239  0.06582  320 HOH A O     
1035 O O     . HOH C .   ? 0.67686 0.74533 0.80324 0.06919  0.16261  0.06316  321 HOH A O     
1036 O O     . HOH C .   ? 0.39697 0.36383 0.39226 0.07815  0.06321  0.01508  322 HOH A O     
1037 O O     . HOH C .   ? 0.70366 0.56978 0.53022 0.02695  0.02226  -0.06432 323 HOH A O     
1038 O O     . HOH C .   ? 0.51570 0.59383 0.67267 -0.01361 -0.02348 0.02205  324 HOH A O     
1039 O O     . HOH C .   ? 0.43766 0.52697 0.58800 0.12056  0.27039  0.05763  325 HOH A O     
1040 O O     . HOH C .   ? 0.68495 0.65749 0.52960 0.10245  0.01503  0.12806  326 HOH A O     
1041 O O     . HOH C .   ? 0.68211 0.48124 0.59012 -0.03771 0.02425  0.00052  327 HOH A O     
1042 O O     . HOH C .   ? 0.53137 0.46919 0.46910 0.09645  0.03498  0.12517  328 HOH A O     
1043 O O     . HOH C .   ? 0.73281 0.67796 0.41938 0.08776  0.09222  0.05144  329 HOH A O     
1044 O O     . HOH C .   ? 0.63962 0.55722 0.65999 0.01734  0.05940  0.06226  330 HOH A O     
1045 O O     . HOH C .   ? 0.56561 0.50373 0.51774 0.12240  0.02858  0.14576  331 HOH A O     
1046 O O     . HOH C .   ? 0.53211 0.58908 0.65983 -0.03924 -0.04714 -0.00028 332 HOH A O     
1047 O O     . HOH C .   ? 0.65592 0.49006 0.59218 0.06337  -0.00227 0.05100  333 HOH A O     
1048 O O     . HOH C .   ? 0.58617 0.64262 0.71626 0.06846  0.03570  0.04203  334 HOH A O     
1049 O O     . HOH C .   ? 0.72403 0.55405 0.53712 0.03445  -0.03463 0.10285  335 HOH A O     
1050 O O     . HOH C .   ? 0.47288 0.53285 0.53066 0.03491  0.02203  0.00999  336 HOH A O     
1051 O O     . HOH C .   ? 0.48816 0.55623 0.59528 -0.00173 -0.05138 0.02135  337 HOH A O     
1052 O O     . HOH C .   ? 0.51944 0.42491 0.52240 0.03600  0.06016  0.07473  338 HOH A O     
1053 O O     . HOH C .   ? 0.64692 0.59169 0.39456 0.08756  0.13584  0.09911  339 HOH A O     
1054 O O     . HOH C .   ? 0.60278 0.54838 0.51518 -0.03574 -0.02752 -0.05519 340 HOH A O     
1055 O O     . HOH C .   ? 0.57462 0.58009 0.54782 0.04401  -0.09611 0.06230  341 HOH A O     
1056 O O     . HOH C .   ? 0.55413 0.66996 0.55727 0.04426  -0.05982 0.02407  342 HOH A O     
1057 O O     . HOH C .   ? 0.60252 0.54276 0.46879 -0.01473 -0.02831 -0.06022 343 HOH A O     
1058 O O     . HOH C .   ? 0.51263 0.41772 0.56695 0.08997  0.06462  0.04976  344 HOH A O     
1059 O O     . HOH C .   ? 0.68426 0.58525 0.73900 -0.00816 0.05761  0.03925  345 HOH A O     
1060 O O     . HOH C .   ? 0.68319 0.66649 0.52446 0.08638  0.01078  0.09947  346 HOH A O     
1061 O O     . HOH C .   ? 0.61844 0.59790 0.42938 0.07963  0.02007  0.08555  347 HOH A O     
1062 O O     . HOH C .   ? 0.67521 0.69376 0.77910 0.09081  0.01207  0.04547  348 HOH A O     
1063 O O     . HOH C .   ? 0.59970 0.59081 0.65351 0.08380  0.04502  0.02846  349 HOH A O     
1064 O O     . HOH C .   ? 0.72449 0.67918 0.46870 0.05682  0.02046  -0.00745 350 HOH A O     
1065 O O     . HOH C .   ? 0.85962 0.74276 0.69331 -0.10605 -0.07574 -0.14284 351 HOH A O     
1066 O O     . HOH C .   ? 0.76809 0.87007 1.04130 0.00319  0.26008  0.12751  352 HOH A O     
# 
