data_8UQF
# 
_entry.id   8UQF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8UQF         pdb_00008uqf 10.2210/pdb8uqf/pdb 
WWPDB D_1000278575 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8UQF 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-23 
_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              dabaker@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Baker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7896-6217 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pellock, S.J.' 1 0000-0002-7557-7985 
'Bera, A.'      2 ?                   
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small molecule binding and sensing with a designed protein family' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, G.R.'      1  ? 
primary 'Pellock, S.J.'  2  ? 
primary 'Norn, C.'       3  ? 
primary 'Tischer, D.'    4  ? 
primary 'Dauparas, J.'   5  ? 
primary 'Anischenko, I.' 6  ? 
primary 'Mercer, J.A.M.' 7  ? 
primary 'Kang, A.'       8  ? 
primary 'Bera, A.'       9  ? 
primary 'Nguyen, H.'     10 ? 
primary 'Goreshnik, I.'  11 ? 
primary 'Vafeados, D.'   12 ? 
primary 'Roullier, N.'   13 ? 
primary 'Han, H.L.'      14 ? 
primary 'Coventry, B.'   15 ? 
primary 'Liu, D.R.'      16 ? 
primary 'Yeh, A.H.W.'    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 'designed cortisol-binding protein hcy129_mpnn5'             15406.424 2  ? ? ? ? 
2 non-polymer syn '(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione' 362.460   2  ? ? ? ? 
3 non-polymer syn 'SULFATE ION'                                                96.063    1  ? ? ? ? 
4 water       nat water                                                        18.015    76 ? ? ? ? 
# 
_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       
;MSGTSSEEAKEAIIAMLKEWYDAMNEGDMEKLRSLVDPDASFVDARTNQVYDKDQFLQMIKEALEQDLKVEVKSIDIEQQ
PDGDVVIVKVKVRATMVRNGQEHVFEVVDTYEFRRKGDSWKIVKLVSEITQLGSG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSGTSSEEAKEAIIAMLKEWYDAMNEGDMEKLRSLVDPDASFVDARTNQVYDKDQFLQMIKEALEQDLKVEVKSIDIEQQ
PDGDVVIVKVKVRATMVRNGQEHVFEVVDTYEFRRKGDSWKIVKLVSEITQLGSG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione' HCY 
3 'SULFATE ION'                                                SO4 
4 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   SER n 
1 3   GLY n 
1 4   THR n 
1 5   SER n 
1 6   SER n 
1 7   GLU n 
1 8   GLU n 
1 9   ALA n 
1 10  LYS n 
1 11  GLU n 
1 12  ALA n 
1 13  ILE n 
1 14  ILE n 
1 15  ALA n 
1 16  MET n 
1 17  LEU n 
1 18  LYS n 
1 19  GLU n 
1 20  TRP n 
1 21  TYR n 
1 22  ASP n 
1 23  ALA n 
1 24  MET n 
1 25  ASN n 
1 26  GLU n 
1 27  GLY n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  LYS n 
1 32  LEU n 
1 33  ARG n 
1 34  SER n 
1 35  LEU n 
1 36  VAL n 
1 37  ASP n 
1 38  PRO n 
1 39  ASP n 
1 40  ALA n 
1 41  SER n 
1 42  PHE n 
1 43  VAL n 
1 44  ASP n 
1 45  ALA n 
1 46  ARG n 
1 47  THR n 
1 48  ASN n 
1 49  GLN n 
1 50  VAL n 
1 51  TYR n 
1 52  ASP n 
1 53  LYS n 
1 54  ASP n 
1 55  GLN n 
1 56  PHE n 
1 57  LEU n 
1 58  GLN n 
1 59  MET n 
1 60  ILE n 
1 61  LYS n 
1 62  GLU n 
1 63  ALA n 
1 64  LEU n 
1 65  GLU n 
1 66  GLN n 
1 67  ASP n 
1 68  LEU n 
1 69  LYS n 
1 70  VAL n 
1 71  GLU n 
1 72  VAL n 
1 73  LYS n 
1 74  SER n 
1 75  ILE n 
1 76  ASP n 
1 77  ILE n 
1 78  GLU n 
1 79  GLN n 
1 80  GLN n 
1 81  PRO n 
1 82  ASP n 
1 83  GLY n 
1 84  ASP n 
1 85  VAL n 
1 86  VAL n 
1 87  ILE n 
1 88  VAL n 
1 89  LYS n 
1 90  VAL n 
1 91  LYS n 
1 92  VAL n 
1 93  ARG n 
1 94  ALA n 
1 95  THR n 
1 96  MET n 
1 97  VAL n 
1 98  ARG n 
1 99  ASN n 
1 100 GLY n 
1 101 GLN n 
1 102 GLU n 
1 103 HIS n 
1 104 VAL n 
1 105 PHE n 
1 106 GLU n 
1 107 VAL n 
1 108 VAL n 
1 109 ASP n 
1 110 THR n 
1 111 TYR n 
1 112 GLU n 
1 113 PHE n 
1 114 ARG n 
1 115 ARG n 
1 116 LYS n 
1 117 GLY n 
1 118 ASP n 
1 119 SER n 
1 120 TRP n 
1 121 LYS n 
1 122 ILE n 
1 123 VAL n 
1 124 LYS n 
1 125 LEU n 
1 126 VAL n 
1 127 SER n 
1 128 GLU n 
1 129 ILE n 
1 130 THR n 
1 131 GLN n 
1 132 LEU n 
1 133 GLY n 
1 134 SER n 
1 135 GLY 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                   135 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_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 
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  
HCY non-polymer         . '(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione' CORTISOL 'C21 H30 O5'     362.460 
HIS 'L-peptide linking' y HISTIDINE                                                    ?        'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                        ?        'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                   ?        'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ?        'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                       ?        'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                   ?        'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                ?        'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                      ?        'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                       ?        'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                                ?        'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                                    ?        'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                   ?        'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                     ?        'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                       ?        'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -2  ?   ?   ?   A . n 
A 1 2   SER 2   -1  ?   ?   ?   A . n 
A 1 3   GLY 3   0   ?   ?   ?   A . n 
A 1 4   THR 4   1   ?   ?   ?   A . n 
A 1 5   SER 5   2   ?   ?   ?   A . n 
A 1 6   SER 6   3   3   SER SER A . n 
A 1 7   GLU 7   4   4   GLU GLU A . n 
A 1 8   GLU 8   5   5   GLU GLU A . n 
A 1 9   ALA 9   6   6   ALA ALA A . n 
A 1 10  LYS 10  7   7   LYS LYS A . n 
A 1 11  GLU 11  8   8   GLU GLU A . n 
A 1 12  ALA 12  9   9   ALA ALA A . n 
A 1 13  ILE 13  10  10  ILE ILE A . n 
A 1 14  ILE 14  11  11  ILE ILE A . n 
A 1 15  ALA 15  12  12  ALA ALA A . n 
A 1 16  MET 16  13  13  MET MET A . n 
A 1 17  LEU 17  14  14  LEU LEU A . n 
A 1 18  LYS 18  15  15  LYS LYS A . n 
A 1 19  GLU 19  16  16  GLU GLU A . n 
A 1 20  TRP 20  17  17  TRP TRP A . n 
A 1 21  TYR 21  18  18  TYR TYR A . n 
A 1 22  ASP 22  19  19  ASP ASP A . n 
A 1 23  ALA 23  20  20  ALA ALA A . n 
A 1 24  MET 24  21  21  MET MET A . n 
A 1 25  ASN 25  22  22  ASN ASN A . n 
A 1 26  GLU 26  23  23  GLU GLU A . n 
A 1 27  GLY 27  24  24  GLY GLY A . n 
A 1 28  ASP 28  25  25  ASP ASP A . n 
A 1 29  MET 29  26  26  MET MET A . n 
A 1 30  GLU 30  27  27  GLU GLU A . n 
A 1 31  LYS 31  28  28  LYS LYS A . n 
A 1 32  LEU 32  29  29  LEU LEU A . n 
A 1 33  ARG 33  30  30  ARG ARG A . n 
A 1 34  SER 34  31  31  SER SER A . n 
A 1 35  LEU 35  32  32  LEU LEU A . n 
A 1 36  VAL 36  33  33  VAL VAL A . n 
A 1 37  ASP 37  34  34  ASP ASP A . n 
A 1 38  PRO 38  35  35  PRO PRO A . n 
A 1 39  ASP 39  36  36  ASP ASP A . n 
A 1 40  ALA 40  37  37  ALA ALA A . n 
A 1 41  SER 41  38  38  SER SER A . n 
A 1 42  PHE 42  39  39  PHE PHE A . n 
A 1 43  VAL 43  40  40  VAL VAL A . n 
A 1 44  ASP 44  41  41  ASP ASP A . n 
A 1 45  ALA 45  42  42  ALA ALA A . n 
A 1 46  ARG 46  43  43  ARG ARG A . n 
A 1 47  THR 47  44  44  THR THR A . n 
A 1 48  ASN 48  45  45  ASN ASN A . n 
A 1 49  GLN 49  46  46  GLN GLN A . n 
A 1 50  VAL 50  47  47  VAL VAL A . n 
A 1 51  TYR 51  48  48  TYR TYR A . n 
A 1 52  ASP 52  49  49  ASP ASP A . n 
A 1 53  LYS 53  50  50  LYS LYS A . n 
A 1 54  ASP 54  51  51  ASP ASP A . n 
A 1 55  GLN 55  52  52  GLN GLN A . n 
A 1 56  PHE 56  53  53  PHE PHE A . n 
A 1 57  LEU 57  54  54  LEU LEU A . n 
A 1 58  GLN 58  55  55  GLN GLN A . n 
A 1 59  MET 59  56  56  MET MET A . n 
A 1 60  ILE 60  57  57  ILE ILE A . n 
A 1 61  LYS 61  58  58  LYS LYS A . n 
A 1 62  GLU 62  59  59  GLU GLU A . n 
A 1 63  ALA 63  60  60  ALA ALA A . n 
A 1 64  LEU 64  61  61  LEU LEU A . n 
A 1 65  GLU 65  62  62  GLU GLU A . n 
A 1 66  GLN 66  63  63  GLN GLN A . n 
A 1 67  ASP 67  64  64  ASP ASP A . n 
A 1 68  LEU 68  65  65  LEU LEU A . n 
A 1 69  LYS 69  66  66  LYS LYS A . n 
A 1 70  VAL 70  67  67  VAL VAL A . n 
A 1 71  GLU 71  68  68  GLU GLU A . n 
A 1 72  VAL 72  69  69  VAL VAL A . n 
A 1 73  LYS 73  70  70  LYS LYS A . n 
A 1 74  SER 74  71  71  SER SER A . n 
A 1 75  ILE 75  72  72  ILE ILE A . n 
A 1 76  ASP 76  73  73  ASP ASP A . n 
A 1 77  ILE 77  74  74  ILE ILE A . n 
A 1 78  GLU 78  75  75  GLU GLU A . n 
A 1 79  GLN 79  76  ?   ?   ?   A . n 
A 1 80  GLN 80  77  ?   ?   ?   A . n 
A 1 81  PRO 81  78  ?   ?   ?   A . n 
A 1 82  ASP 82  79  ?   ?   ?   A . n 
A 1 83  GLY 83  80  ?   ?   ?   A . n 
A 1 84  ASP 84  81  ?   ?   ?   A . n 
A 1 85  VAL 85  82  82  VAL VAL A . n 
A 1 86  VAL 86  83  83  VAL VAL A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  VAL 88  85  85  VAL VAL A . n 
A 1 89  LYS 89  86  86  LYS LYS A . n 
A 1 90  VAL 90  87  87  VAL VAL A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  VAL 92  89  89  VAL VAL A . n 
A 1 93  ARG 93  90  90  ARG ARG A . n 
A 1 94  ALA 94  91  91  ALA ALA A . n 
A 1 95  THR 95  92  92  THR THR A . n 
A 1 96  MET 96  93  93  MET MET A . n 
A 1 97  VAL 97  94  94  VAL VAL A . n 
A 1 98  ARG 98  95  95  ARG ARG A . n 
A 1 99  ASN 99  96  96  ASN ASN A . n 
A 1 100 GLY 100 97  97  GLY GLY A . n 
A 1 101 GLN 101 98  98  GLN GLN A . n 
A 1 102 GLU 102 99  99  GLU GLU A . n 
A 1 103 HIS 103 100 100 HIS HIS A . n 
A 1 104 VAL 104 101 101 VAL VAL A . n 
A 1 105 PHE 105 102 102 PHE PHE A . n 
A 1 106 GLU 106 103 103 GLU GLU A . n 
A 1 107 VAL 107 104 104 VAL VAL A . n 
A 1 108 VAL 108 105 105 VAL VAL A . n 
A 1 109 ASP 109 106 106 ASP ASP A . n 
A 1 110 THR 110 107 107 THR THR A . n 
A 1 111 TYR 111 108 108 TYR TYR A . n 
A 1 112 GLU 112 109 109 GLU GLU A . n 
A 1 113 PHE 113 110 110 PHE PHE A . n 
A 1 114 ARG 114 111 111 ARG ARG A . n 
A 1 115 ARG 115 112 112 ARG ARG A . n 
A 1 116 LYS 116 113 ?   ?   ?   A . n 
A 1 117 GLY 117 114 ?   ?   ?   A . n 
A 1 118 ASP 118 115 ?   ?   ?   A . n 
A 1 119 SER 119 116 116 SER SER A . n 
A 1 120 TRP 120 117 117 TRP TRP A . n 
A 1 121 LYS 121 118 118 LYS LYS A . n 
A 1 122 ILE 122 119 119 ILE ILE A . n 
A 1 123 VAL 123 120 120 VAL VAL A . n 
A 1 124 LYS 124 121 121 LYS LYS A . n 
A 1 125 LEU 125 122 122 LEU LEU A . n 
A 1 126 VAL 126 123 123 VAL VAL A . n 
A 1 127 SER 127 124 124 SER SER A . n 
A 1 128 GLU 128 125 125 GLU GLU A . n 
A 1 129 ILE 129 126 126 ILE ILE A . n 
A 1 130 THR 130 127 127 THR THR A . n 
A 1 131 GLN 131 128 128 GLN GLN A . n 
A 1 132 LEU 132 129 129 LEU LEU A . n 
A 1 133 GLY 133 130 130 GLY GLY A . n 
A 1 134 SER 134 131 131 SER SER A . n 
A 1 135 GLY 135 132 ?   ?   ?   A . n 
B 1 1   MET 1   -2  ?   ?   ?   B . n 
B 1 2   SER 2   -1  ?   ?   ?   B . n 
B 1 3   GLY 3   0   ?   ?   ?   B . n 
B 1 4   THR 4   1   ?   ?   ?   B . n 
B 1 5   SER 5   2   ?   ?   ?   B . n 
B 1 6   SER 6   3   ?   ?   ?   B . n 
B 1 7   GLU 7   4   4   GLU GLU B . n 
B 1 8   GLU 8   5   5   GLU GLU B . n 
B 1 9   ALA 9   6   6   ALA ALA B . n 
B 1 10  LYS 10  7   7   LYS LYS B . n 
B 1 11  GLU 11  8   8   GLU GLU B . n 
B 1 12  ALA 12  9   9   ALA ALA B . n 
B 1 13  ILE 13  10  10  ILE ILE B . n 
B 1 14  ILE 14  11  11  ILE ILE B . n 
B 1 15  ALA 15  12  12  ALA ALA B . n 
B 1 16  MET 16  13  13  MET MET B . n 
B 1 17  LEU 17  14  14  LEU LEU B . n 
B 1 18  LYS 18  15  15  LYS LYS B . n 
B 1 19  GLU 19  16  16  GLU GLU B . n 
B 1 20  TRP 20  17  17  TRP TRP B . n 
B 1 21  TYR 21  18  18  TYR TYR B . n 
B 1 22  ASP 22  19  19  ASP ASP B . n 
B 1 23  ALA 23  20  20  ALA ALA B . n 
B 1 24  MET 24  21  21  MET MET B . n 
B 1 25  ASN 25  22  22  ASN ASN B . n 
B 1 26  GLU 26  23  23  GLU GLU B . n 
B 1 27  GLY 27  24  24  GLY GLY B . n 
B 1 28  ASP 28  25  25  ASP ASP B . n 
B 1 29  MET 29  26  26  MET MET B . n 
B 1 30  GLU 30  27  27  GLU GLU B . n 
B 1 31  LYS 31  28  28  LYS LYS B . n 
B 1 32  LEU 32  29  29  LEU LEU B . n 
B 1 33  ARG 33  30  30  ARG ARG B . n 
B 1 34  SER 34  31  31  SER SER B . n 
B 1 35  LEU 35  32  32  LEU LEU B . n 
B 1 36  VAL 36  33  33  VAL VAL B . n 
B 1 37  ASP 37  34  34  ASP ASP B . n 
B 1 38  PRO 38  35  35  PRO PRO B . n 
B 1 39  ASP 39  36  36  ASP ASP B . n 
B 1 40  ALA 40  37  37  ALA ALA B . n 
B 1 41  SER 41  38  38  SER SER B . n 
B 1 42  PHE 42  39  39  PHE PHE B . n 
B 1 43  VAL 43  40  40  VAL VAL B . n 
B 1 44  ASP 44  41  41  ASP ASP B . n 
B 1 45  ALA 45  42  42  ALA ALA B . n 
B 1 46  ARG 46  43  43  ARG ARG B . n 
B 1 47  THR 47  44  44  THR THR B . n 
B 1 48  ASN 48  45  45  ASN ASN B . n 
B 1 49  GLN 49  46  46  GLN GLN B . n 
B 1 50  VAL 50  47  47  VAL VAL B . n 
B 1 51  TYR 51  48  48  TYR TYR B . n 
B 1 52  ASP 52  49  49  ASP ASP B . n 
B 1 53  LYS 53  50  50  LYS LYS B . n 
B 1 54  ASP 54  51  51  ASP ASP B . n 
B 1 55  GLN 55  52  52  GLN GLN B . n 
B 1 56  PHE 56  53  53  PHE PHE B . n 
B 1 57  LEU 57  54  54  LEU LEU B . n 
B 1 58  GLN 58  55  55  GLN GLN B . n 
B 1 59  MET 59  56  56  MET MET B . n 
B 1 60  ILE 60  57  57  ILE ILE B . n 
B 1 61  LYS 61  58  58  LYS LYS B . n 
B 1 62  GLU 62  59  59  GLU GLU B . n 
B 1 63  ALA 63  60  60  ALA ALA B . n 
B 1 64  LEU 64  61  61  LEU LEU B . n 
B 1 65  GLU 65  62  62  GLU GLU B . n 
B 1 66  GLN 66  63  63  GLN GLN B . n 
B 1 67  ASP 67  64  64  ASP ASP B . n 
B 1 68  LEU 68  65  65  LEU LEU B . n 
B 1 69  LYS 69  66  66  LYS LYS B . n 
B 1 70  VAL 70  67  67  VAL VAL B . n 
B 1 71  GLU 71  68  68  GLU GLU B . n 
B 1 72  VAL 72  69  69  VAL VAL B . n 
B 1 73  LYS 73  70  70  LYS LYS B . n 
B 1 74  SER 74  71  71  SER SER B . n 
B 1 75  ILE 75  72  72  ILE ILE B . n 
B 1 76  ASP 76  73  73  ASP ASP B . n 
B 1 77  ILE 77  74  74  ILE ILE B . n 
B 1 78  GLU 78  75  75  GLU GLU B . n 
B 1 79  GLN 79  76  76  GLN GLN B . n 
B 1 80  GLN 80  77  77  GLN GLN B . n 
B 1 81  PRO 81  78  78  PRO PRO B . n 
B 1 82  ASP 82  79  79  ASP ASP B . n 
B 1 83  GLY 83  80  80  GLY GLY B . n 
B 1 84  ASP 84  81  81  ASP ASP B . n 
B 1 85  VAL 85  82  82  VAL VAL B . n 
B 1 86  VAL 86  83  83  VAL VAL B . n 
B 1 87  ILE 87  84  84  ILE ILE B . n 
B 1 88  VAL 88  85  85  VAL VAL B . n 
B 1 89  LYS 89  86  86  LYS LYS B . n 
B 1 90  VAL 90  87  87  VAL VAL B . n 
B 1 91  LYS 91  88  88  LYS LYS B . n 
B 1 92  VAL 92  89  89  VAL VAL B . n 
B 1 93  ARG 93  90  90  ARG ARG B . n 
B 1 94  ALA 94  91  91  ALA ALA B . n 
B 1 95  THR 95  92  92  THR THR B . n 
B 1 96  MET 96  93  93  MET MET B . n 
B 1 97  VAL 97  94  94  VAL VAL B . n 
B 1 98  ARG 98  95  95  ARG ARG B . n 
B 1 99  ASN 99  96  ?   ?   ?   B . n 
B 1 100 GLY 100 97  ?   ?   ?   B . n 
B 1 101 GLN 101 98  98  GLN GLN B . n 
B 1 102 GLU 102 99  99  GLU GLU B . n 
B 1 103 HIS 103 100 100 HIS HIS B . n 
B 1 104 VAL 104 101 101 VAL VAL B . n 
B 1 105 PHE 105 102 102 PHE PHE B . n 
B 1 106 GLU 106 103 103 GLU GLU B . n 
B 1 107 VAL 107 104 104 VAL VAL B . n 
B 1 108 VAL 108 105 105 VAL VAL B . n 
B 1 109 ASP 109 106 106 ASP ASP B . n 
B 1 110 THR 110 107 107 THR THR B . n 
B 1 111 TYR 111 108 108 TYR TYR B . n 
B 1 112 GLU 112 109 109 GLU GLU B . n 
B 1 113 PHE 113 110 110 PHE PHE B . n 
B 1 114 ARG 114 111 111 ARG ARG B . n 
B 1 115 ARG 115 112 112 ARG ARG B . n 
B 1 116 LYS 116 113 113 LYS LYS B . n 
B 1 117 GLY 117 114 114 GLY GLY B . n 
B 1 118 ASP 118 115 115 ASP ASP B . n 
B 1 119 SER 119 116 116 SER SER B . n 
B 1 120 TRP 120 117 117 TRP TRP B . n 
B 1 121 LYS 121 118 118 LYS LYS B . n 
B 1 122 ILE 122 119 119 ILE ILE B . n 
B 1 123 VAL 123 120 120 VAL VAL B . n 
B 1 124 LYS 124 121 121 LYS LYS B . n 
B 1 125 LEU 125 122 122 LEU LEU B . n 
B 1 126 VAL 126 123 123 VAL VAL B . n 
B 1 127 SER 127 124 124 SER SER B . n 
B 1 128 GLU 128 125 125 GLU GLU B . n 
B 1 129 ILE 129 126 126 ILE ILE B . n 
B 1 130 THR 130 127 127 THR THR B . n 
B 1 131 GLN 131 128 128 GLN GLN B . n 
B 1 132 LEU 132 129 129 LEU LEU B . n 
B 1 133 GLY 133 130 130 GLY GLY B . n 
B 1 134 SER 134 131 131 SER SER B . n 
B 1 135 GLY 135 132 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HCY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HCY 
_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 
C 2 HCY 1  201 201 HCY HCY A . 
D 2 HCY 1  201 201 HCY HCY B . 
E 3 SO4 1  202 101 SO4 SO4 B . 
F 4 HOH 1  301 74  HOH HOH A . 
F 4 HOH 2  302 85  HOH HOH A . 
F 4 HOH 3  303 62  HOH HOH A . 
F 4 HOH 4  304 7   HOH HOH A . 
F 4 HOH 5  305 54  HOH HOH A . 
F 4 HOH 6  306 8   HOH HOH A . 
F 4 HOH 7  307 18  HOH HOH A . 
F 4 HOH 8  308 4   HOH HOH A . 
F 4 HOH 9  309 3   HOH HOH A . 
F 4 HOH 10 310 76  HOH HOH A . 
F 4 HOH 11 311 6   HOH HOH A . 
F 4 HOH 12 312 17  HOH HOH A . 
F 4 HOH 13 313 100 HOH HOH A . 
F 4 HOH 14 314 60  HOH HOH A . 
F 4 HOH 15 315 26  HOH HOH A . 
F 4 HOH 16 316 27  HOH HOH A . 
F 4 HOH 17 317 40  HOH HOH A . 
F 4 HOH 18 318 10  HOH HOH A . 
F 4 HOH 19 319 39  HOH HOH A . 
F 4 HOH 20 320 46  HOH HOH A . 
F 4 HOH 21 321 5   HOH HOH A . 
F 4 HOH 22 322 28  HOH HOH A . 
F 4 HOH 23 323 1   HOH HOH A . 
F 4 HOH 24 324 2   HOH HOH A . 
F 4 HOH 25 325 56  HOH HOH A . 
F 4 HOH 26 326 81  HOH HOH A . 
F 4 HOH 27 327 24  HOH HOH A . 
F 4 HOH 28 328 88  HOH HOH A . 
F 4 HOH 29 329 25  HOH HOH A . 
F 4 HOH 30 330 63  HOH HOH A . 
F 4 HOH 31 331 68  HOH HOH A . 
F 4 HOH 32 332 73  HOH HOH A . 
G 4 HOH 1  301 67  HOH HOH B . 
G 4 HOH 2  302 22  HOH HOH B . 
G 4 HOH 3  303 20  HOH HOH B . 
G 4 HOH 4  304 55  HOH HOH B . 
G 4 HOH 5  305 30  HOH HOH B . 
G 4 HOH 6  306 14  HOH HOH B . 
G 4 HOH 7  307 11  HOH HOH B . 
G 4 HOH 8  308 15  HOH HOH B . 
G 4 HOH 9  309 82  HOH HOH B . 
G 4 HOH 10 310 31  HOH HOH B . 
G 4 HOH 11 311 13  HOH HOH B . 
G 4 HOH 12 312 32  HOH HOH B . 
G 4 HOH 13 313 89  HOH HOH B . 
G 4 HOH 14 314 47  HOH HOH B . 
G 4 HOH 15 315 23  HOH HOH B . 
G 4 HOH 16 316 41  HOH HOH B . 
G 4 HOH 17 317 16  HOH HOH B . 
G 4 HOH 18 318 29  HOH HOH B . 
G 4 HOH 19 319 53  HOH HOH B . 
G 4 HOH 20 320 34  HOH HOH B . 
G 4 HOH 21 321 19  HOH HOH B . 
G 4 HOH 22 322 37  HOH HOH B . 
G 4 HOH 23 323 57  HOH HOH B . 
G 4 HOH 24 324 33  HOH HOH B . 
G 4 HOH 25 325 48  HOH HOH B . 
G 4 HOH 26 326 36  HOH HOH B . 
G 4 HOH 27 327 9   HOH HOH B . 
G 4 HOH 28 328 38  HOH HOH B . 
G 4 HOH 29 329 64  HOH HOH B . 
G 4 HOH 30 330 77  HOH HOH B . 
G 4 HOH 31 331 35  HOH HOH B . 
G 4 HOH 32 332 51  HOH HOH B . 
G 4 HOH 33 333 12  HOH HOH B . 
G 4 HOH 34 334 21  HOH HOH B . 
G 4 HOH 35 335 84  HOH HOH B . 
G 4 HOH 36 336 49  HOH HOH B . 
G 4 HOH 37 337 79  HOH HOH B . 
G 4 HOH 38 338 50  HOH HOH B . 
G 4 HOH 39 339 44  HOH HOH B . 
G 4 HOH 40 340 59  HOH HOH B . 
G 4 HOH 41 341 80  HOH HOH B . 
G 4 HOH 42 342 42  HOH HOH B . 
G 4 HOH 43 343 43  HOH HOH B . 
G 4 HOH 44 344 52  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.990 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UQF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.016 
_cell.length_a_esd                 ? 
_cell.length_b                     48.609 
_cell.length_b_esd                 ? 
_cell.length_c                     56.438 
_cell.length_c_esd                 ? 
_cell.volume                       131407.564 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8UQF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8UQF 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.32 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium sulfate, 30% w/v PEG 8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97926 
_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                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97926 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          25.10 
_reflns.entry_id                                       8UQF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               47.9 
_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                                     59774 
_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                           90.28 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.73 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.07593 
_reflns.pdbx_Rpim_I_all                                0.04351 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .993 
_reflns.pdbx_CC_star                                   .998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0617 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.574 
_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                             3628 
_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                               2.4 
_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                               1.024 
_reflns_shell.pdbx_Rpim_I_all                               .5868 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .613 
_reflns_shell.pdbx_CC_star                                  .872 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          91.52 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  .8317 
_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                               33.11 
_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                                 8UQF 
_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                            1.52 
_refine.ls_d_res_low                             47.90 
_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                     59774 
_refine.ls_number_reflns_R_free                  3305 
_refine.ls_number_reflns_R_work                  56469 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    76.29 
_refine.ls_percent_reflns_R_free                 5.53 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2277 
_refine.ls_R_factor_R_free                       0.2427 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2268 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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                 28.0434 
_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                            0.2328 
_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                       1.52 
_refine_hist.d_res_low                        47.90 
_refine_hist.number_atoms_solvent             76 
_refine_hist.number_atoms_total               2133 
_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        2000 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         57 
_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' ? 0.0237  ? 2110 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.9725  ? 2859 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.3318  ? 332  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0103  ? 357  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.8095 ? 809  ? 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' 1.52 1.54  . . 126 2270 75.87 . . . . 0.3473 . . . . . . . . . . . 0.3734 
'X-RAY DIFFRACTION' 1.54 1.56  . . 127 2389 75.56 . . . . 0.3330 . . . . . . . . . . . 0.3362 
'X-RAY DIFFRACTION' 1.56 1.59  . . 144 2349 76.40 . . . . 0.3225 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 1.59 1.61  . . 144 2333 75.36 . . . . 0.3140 . . . . . . . . . . . 0.3405 
'X-RAY DIFFRACTION' 1.61 1.64  . . 144 2292 76.41 . . . . 0.3155 . . . . . . . . . . . 0.3404 
'X-RAY DIFFRACTION' 1.64 1.67  . . 153 2424 77.71 . . . . 0.3164 . . . . . . . . . . . 0.3412 
'X-RAY DIFFRACTION' 1.67 1.70  . . 142 2370 77.36 . . . . 0.2964 . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 1.70 1.74  . . 167 2346 76.85 . . . . 0.2899 . . . . . . . . . . . 0.3663 
'X-RAY DIFFRACTION' 1.74 1.78  . . 93  2348 74.19 . . . . 0.2685 . . . . . . . . . . . 0.2891 
'X-RAY DIFFRACTION' 1.78 1.82  . . 154 2338 76.14 . . . . 0.2695 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 1.82 1.86  . . 123 2462 79.78 . . . . 0.2515 . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 1.86 1.91  . . 145 2477 80.36 . . . . 0.2264 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 1.91 1.97  . . 140 2437 78.88 . . . . 0.2400 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 1.97 2.03  . . 156 2373 77.86 . . . . 0.2373 . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 2.03 2.11  . . 126 2440 77.38 . . . . 0.2323 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 2.11 2.19  . . 141 2342 76.12 . . . . 0.2171 . . . . . . . . . . . 0.2427 
'X-RAY DIFFRACTION' 2.19 2.29  . . 136 2349 76.27 . . . . 0.2150 . . . . . . . . . . . 0.2764 
'X-RAY DIFFRACTION' 2.29 2.41  . . 122 2295 73.82 . . . . 0.2227 . . . . . . . . . . . 0.3327 
'X-RAY DIFFRACTION' 2.41 2.56  . . 137 2271 73.30 . . . . 0.2413 . . . . . . . . . . . 0.2320 
'X-RAY DIFFRACTION' 2.56 2.76  . . 133 2354 76.81 . . . . 0.2336 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 2.76 3.04  . . 127 2356 76.05 . . . . 0.2281 . . . . . . . . . . . 0.2386 
'X-RAY DIFFRACTION' 3.04 3.48  . . 130 2321 74.66 . . . . 0.2101 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 3.48 4.38  . . 165 2245 73.99 . . . . 0.1975 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 4.38 47.90 . . 130 2288 74.01 . . . . 0.2073 . . . . . . . . . . . 0.2237 
# 
_struct.entry_id                     8UQF 
_struct.title                        'Crystal structure of designed cortisol-binding protein hcy129_mpnn5' 
_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        8UQF 
_struct_keywords.text            'NTF2, cortisol binding, DE NOVO PROTEIN' 
_struct_keywords.pdbx_keywords   'DE NOVO 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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8UQF 
_struct_ref.pdbx_db_accession          8UQF 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8UQF A 1 ? 135 ? 8UQF -2 ? 132 ? -2 132 
2 1 8UQF B 1 ? 135 ? 8UQF -2 ? 132 ? -2 132 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,F   
2 1 B,D,E,G 
# 
_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 SER A 6  ? GLY A 27 ? SER A 3  GLY A 24 1 ? 22 
HELX_P HELX_P2 AA2 ASP A 28 ? LEU A 35 ? ASP A 25 LEU A 32 1 ? 8  
HELX_P HELX_P3 AA3 ASP A 52 ? GLN A 66 ? ASP A 49 GLN A 63 1 ? 15 
HELX_P HELX_P4 AA4 GLU B 8  ? GLY B 27 ? GLU B 5  GLY B 24 1 ? 20 
HELX_P HELX_P5 AA5 ASP B 28 ? SER B 34 ? ASP B 25 SER B 31 1 ? 7  
HELX_P HELX_P6 AA6 LYS B 53 ? GLN B 66 ? LYS B 50 GLN B 63 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? 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 GLN A 49  ? TYR A 51  ? GLN A 46  TYR A 48  
AA1 2 VAL A 36  ? ASP A 44  ? VAL A 33  ASP A 41  
AA1 3 LYS A 121 ? GLN A 131 ? LYS A 118 GLN A 128 
AA1 4 GLN A 101 ? ARG A 114 ? GLN A 98  ARG A 111 
AA1 5 VAL A 86  ? ARG A 98  ? VAL A 83  ARG A 95  
AA1 6 LYS A 69  ? GLU A 78  ? LYS A 66  GLU A 75  
AA2 1 GLN B 49  ? ASP B 52  ? GLN B 46  ASP B 49  
AA2 2 VAL B 36  ? ASP B 44  ? VAL B 33  ASP B 41  
AA2 3 SER B 119 ? GLY B 133 ? SER B 116 GLY B 130 
AA2 4 HIS B 103 ? LYS B 116 ? HIS B 100 LYS B 113 
AA2 5 VAL B 85  ? MET B 96  ? VAL B 82  MET B 93  
AA2 6 LYS B 69  ? GLU B 78  ? LYS B 66  GLU B 75  
# 
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 GLN A 49  ? O GLN A 46  N ASP A 44  ? N ASP A 41  
AA1 2 3 N VAL A 43  ? N VAL A 40  O LEU A 125 ? O LEU A 122 
AA1 3 4 O VAL A 126 ? O VAL A 123 N THR A 110 ? N THR A 107 
AA1 4 5 O ASP A 109 ? O ASP A 106 N VAL A 90  ? N VAL A 87  
AA1 5 6 O ILE A 87  ? O ILE A 84  N GLU A 78  ? N GLU A 75  
AA2 1 2 O TYR B 51  ? O TYR B 48  N PHE B 42  ? N PHE B 39  
AA2 2 3 N VAL B 43  ? N VAL B 40  O LEU B 125 ? O LEU B 122 
AA2 3 4 O SER B 119 ? O SER B 116 N LYS B 116 ? N LYS B 113 
AA2 4 5 O ASP B 109 ? O ASP B 106 N VAL B 90  ? N VAL B 87  
AA2 5 6 O ILE B 87  ? O ILE B 84  N GLU B 78  ? N GLU B 75  
# 
_pdbx_entry_details.entry_id                   8UQF 
_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   N 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CE1 A TYR 18 ? ? CZ A TYR 18 ? ? 1.285 1.381 -0.096 0.013 N 
2 1 N   B SER 38 ? ? CA B SER 38 ? A 1.581 1.459 0.122  0.020 N 
3 1 N   B SER 38 ? ? CA B SER 38 ? B 1.580 1.459 0.121  0.020 N 
4 1 CG  B GLU 75 ? ? CD B GLU 75 ? ? 1.423 1.515 -0.092 0.015 N 
5 1 C   B PRO 78 ? ? O  B PRO 78 ? ? 1.413 1.228 0.185  0.020 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 OE1 B GLU 75 ? ? CD B GLU 75 ? ? OE2 B GLU 75 ? ? 131.24 123.30 7.94  1.20 N 
2 1 CA  B PRO 78 ? ? C  B PRO 78 ? ? O   B PRO 78 ? ? 136.49 120.20 16.29 2.40 N 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -2  ? A MET 1   
2  1 Y 1 A SER -1  ? A SER 2   
3  1 Y 1 A GLY 0   ? A GLY 3   
4  1 Y 1 A THR 1   ? A THR 4   
5  1 Y 1 A SER 2   ? A SER 5   
6  1 Y 1 A GLN 76  ? A GLN 79  
7  1 Y 1 A GLN 77  ? A GLN 80  
8  1 Y 1 A PRO 78  ? A PRO 81  
9  1 Y 1 A ASP 79  ? A ASP 82  
10 1 Y 1 A GLY 80  ? A GLY 83  
11 1 Y 1 A ASP 81  ? A ASP 84  
12 1 Y 1 A LYS 113 ? A LYS 116 
13 1 Y 1 A GLY 114 ? A GLY 117 
14 1 Y 1 A ASP 115 ? A ASP 118 
15 1 Y 1 A GLY 132 ? A GLY 135 
16 1 Y 1 B MET -2  ? B MET 1   
17 1 Y 1 B SER -1  ? B SER 2   
18 1 Y 1 B GLY 0   ? B GLY 3   
19 1 Y 1 B THR 1   ? B THR 4   
20 1 Y 1 B SER 2   ? B SER 5   
21 1 Y 1 B SER 3   ? B SER 6   
22 1 Y 1 B ASN 96  ? B ASN 99  
23 1 Y 1 B GLY 97  ? B GLY 100 
24 1 Y 1 B GLY 132 ? B GLY 135 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HCY C1   C N N 123 
HCY C2   C N N 124 
HCY C3   C N N 125 
HCY C4   C N N 126 
HCY C5   C N N 127 
HCY C6   C N N 128 
HCY C7   C N N 129 
HCY C8   C N S 130 
HCY C9   C N S 131 
HCY C10  C N R 132 
HCY C12  C N N 133 
HCY C11  C N S 134 
HCY C13  C N S 135 
HCY C14  C N S 136 
HCY C15  C N N 137 
HCY C16  C N N 138 
HCY C17  C N R 139 
HCY C18  C N N 140 
HCY C19  C N N 141 
HCY C20  C N N 142 
HCY C21  C N N 143 
HCY O1   O N N 144 
HCY O2   O N N 145 
HCY O3   O N N 146 
HCY O4   O N N 147 
HCY O5   O N N 148 
HCY H4   H N N 149 
HCY H2C1 H N N 150 
HCY H2C2 H N N 151 
HCY H6C1 H N N 152 
HCY H6C2 H N N 153 
HCY H7C1 H N N 154 
HCY H7C2 H N N 155 
HCY H8   H N N 156 
HCY H1C1 H N N 157 
HCY H1C2 H N N 158 
HCY H191 H N N 159 
HCY H192 H N N 160 
HCY H193 H N N 161 
HCY H9   H N N 162 
HCY H11  H N N 163 
HCY H14  H N N 164 
HCY H2   H N N 165 
HCY H121 H N N 166 
HCY H122 H N N 167 
HCY H181 H N N 168 
HCY H182 H N N 169 
HCY H183 H N N 170 
HCY H151 H N N 171 
HCY H152 H N N 172 
HCY H161 H N N 173 
HCY H162 H N N 174 
HCY H3   H N N 175 
HCY H211 H N N 176 
HCY H212 H N N 177 
HCY H5   H N N 178 
HIS N    N N N 179 
HIS CA   C N S 180 
HIS C    C N N 181 
HIS O    O N N 182 
HIS CB   C N N 183 
HIS CG   C Y N 184 
HIS ND1  N Y N 185 
HIS CD2  C Y N 186 
HIS CE1  C Y N 187 
HIS NE2  N Y N 188 
HIS OXT  O N N 189 
HIS H    H N N 190 
HIS H2   H N N 191 
HIS HA   H N N 192 
HIS HB2  H N N 193 
HIS HB3  H N N 194 
HIS HD1  H N N 195 
HIS HD2  H N N 196 
HIS HE1  H N N 197 
HIS HE2  H N N 198 
HIS HXT  H N N 199 
HOH O    O N N 200 
HOH H1   H N N 201 
HOH H2   H N N 202 
ILE N    N N N 203 
ILE CA   C N S 204 
ILE C    C N N 205 
ILE O    O N N 206 
ILE CB   C N S 207 
ILE CG1  C N N 208 
ILE CG2  C N N 209 
ILE CD1  C N N 210 
ILE OXT  O N N 211 
ILE H    H N N 212 
ILE H2   H N N 213 
ILE HA   H N N 214 
ILE HB   H N N 215 
ILE HG12 H N N 216 
ILE HG13 H N N 217 
ILE HG21 H N N 218 
ILE HG22 H N N 219 
ILE HG23 H N N 220 
ILE HD11 H N N 221 
ILE HD12 H N N 222 
ILE HD13 H N N 223 
ILE HXT  H N N 224 
LEU N    N N N 225 
LEU CA   C N S 226 
LEU C    C N N 227 
LEU O    O N N 228 
LEU CB   C N N 229 
LEU CG   C N N 230 
LEU CD1  C N N 231 
LEU CD2  C N N 232 
LEU OXT  O N N 233 
LEU H    H N N 234 
LEU H2   H N N 235 
LEU HA   H N N 236 
LEU HB2  H N N 237 
LEU HB3  H N N 238 
LEU HG   H N N 239 
LEU HD11 H N N 240 
LEU HD12 H N N 241 
LEU HD13 H N N 242 
LEU HD21 H N N 243 
LEU HD22 H N N 244 
LEU HD23 H N N 245 
LEU HXT  H N N 246 
LYS N    N N N 247 
LYS CA   C N S 248 
LYS C    C N N 249 
LYS O    O N N 250 
LYS CB   C N N 251 
LYS CG   C N N 252 
LYS CD   C N N 253 
LYS CE   C N N 254 
LYS NZ   N N N 255 
LYS OXT  O N N 256 
LYS H    H N N 257 
LYS H2   H N N 258 
LYS HA   H N N 259 
LYS HB2  H N N 260 
LYS HB3  H N N 261 
LYS HG2  H N N 262 
LYS HG3  H N N 263 
LYS HD2  H N N 264 
LYS HD3  H N N 265 
LYS HE2  H N N 266 
LYS HE3  H N N 267 
LYS HZ1  H N N 268 
LYS HZ2  H N N 269 
LYS HZ3  H N N 270 
LYS HXT  H N N 271 
MET N    N N N 272 
MET CA   C N S 273 
MET C    C N N 274 
MET O    O N N 275 
MET CB   C N N 276 
MET CG   C N N 277 
MET SD   S N N 278 
MET CE   C N N 279 
MET OXT  O N N 280 
MET H    H N N 281 
MET H2   H N N 282 
MET HA   H N N 283 
MET HB2  H N N 284 
MET HB3  H N N 285 
MET HG2  H N N 286 
MET HG3  H N N 287 
MET HE1  H N N 288 
MET HE2  H N N 289 
MET HE3  H N N 290 
MET HXT  H N N 291 
PHE N    N N N 292 
PHE CA   C N S 293 
PHE C    C N N 294 
PHE O    O N N 295 
PHE CB   C N N 296 
PHE CG   C Y N 297 
PHE CD1  C Y N 298 
PHE CD2  C Y N 299 
PHE CE1  C Y N 300 
PHE CE2  C Y N 301 
PHE CZ   C Y N 302 
PHE OXT  O N N 303 
PHE H    H N N 304 
PHE H2   H N N 305 
PHE HA   H N N 306 
PHE HB2  H N N 307 
PHE HB3  H N N 308 
PHE HD1  H N N 309 
PHE HD2  H N N 310 
PHE HE1  H N N 311 
PHE HE2  H N N 312 
PHE HZ   H N N 313 
PHE HXT  H N N 314 
PRO N    N N N 315 
PRO CA   C N S 316 
PRO C    C N N 317 
PRO O    O N N 318 
PRO CB   C N N 319 
PRO CG   C N N 320 
PRO CD   C N N 321 
PRO OXT  O N N 322 
PRO H    H N N 323 
PRO HA   H N N 324 
PRO HB2  H N N 325 
PRO HB3  H N N 326 
PRO HG2  H N N 327 
PRO HG3  H N N 328 
PRO HD2  H N N 329 
PRO HD3  H N N 330 
PRO HXT  H N N 331 
SER N    N N N 332 
SER CA   C N S 333 
SER C    C N N 334 
SER O    O N N 335 
SER CB   C N N 336 
SER OG   O N N 337 
SER OXT  O N N 338 
SER H    H N N 339 
SER H2   H N N 340 
SER HA   H N N 341 
SER HB2  H N N 342 
SER HB3  H N N 343 
SER HG   H N N 344 
SER HXT  H N N 345 
SO4 S    S N N 346 
SO4 O1   O N N 347 
SO4 O2   O N N 348 
SO4 O3   O N N 349 
SO4 O4   O N N 350 
THR N    N N N 351 
THR CA   C N S 352 
THR C    C N N 353 
THR O    O N N 354 
THR CB   C N R 355 
THR OG1  O N N 356 
THR CG2  C N N 357 
THR OXT  O N N 358 
THR H    H N N 359 
THR H2   H N N 360 
THR HA   H N N 361 
THR HB   H N N 362 
THR HG1  H N N 363 
THR HG21 H N N 364 
THR HG22 H N N 365 
THR HG23 H N N 366 
THR HXT  H N N 367 
TRP N    N N N 368 
TRP CA   C N S 369 
TRP C    C N N 370 
TRP O    O N N 371 
TRP CB   C N N 372 
TRP CG   C Y N 373 
TRP CD1  C Y N 374 
TRP CD2  C Y N 375 
TRP NE1  N Y N 376 
TRP CE2  C Y N 377 
TRP CE3  C Y N 378 
TRP CZ2  C Y N 379 
TRP CZ3  C Y N 380 
TRP CH2  C Y N 381 
TRP OXT  O N N 382 
TRP H    H N N 383 
TRP H2   H N N 384 
TRP HA   H N N 385 
TRP HB2  H N N 386 
TRP HB3  H N N 387 
TRP HD1  H N N 388 
TRP HE1  H N N 389 
TRP HE3  H N N 390 
TRP HZ2  H N N 391 
TRP HZ3  H N N 392 
TRP HH2  H N N 393 
TRP HXT  H N N 394 
TYR N    N N N 395 
TYR CA   C N S 396 
TYR C    C N N 397 
TYR O    O N N 398 
TYR CB   C N N 399 
TYR CG   C Y N 400 
TYR CD1  C Y N 401 
TYR CD2  C Y N 402 
TYR CE1  C Y N 403 
TYR CE2  C Y N 404 
TYR CZ   C Y N 405 
TYR OH   O N N 406 
TYR OXT  O N N 407 
TYR H    H N N 408 
TYR H2   H N N 409 
TYR HA   H N N 410 
TYR HB2  H N N 411 
TYR HB3  H N N 412 
TYR HD1  H N N 413 
TYR HD2  H N N 414 
TYR HE1  H N N 415 
TYR HE2  H N N 416 
TYR HH   H N N 417 
TYR HXT  H N N 418 
VAL N    N N N 419 
VAL CA   C N S 420 
VAL C    C N N 421 
VAL O    O N N 422 
VAL CB   C N N 423 
VAL CG1  C N N 424 
VAL CG2  C N N 425 
VAL OXT  O N N 426 
VAL H    H N N 427 
VAL H2   H N N 428 
VAL HA   H N N 429 
VAL HB   H N N 430 
VAL HG11 H N N 431 
VAL HG12 H N N 432 
VAL HG13 H N N 433 
VAL HG21 H N N 434 
VAL HG22 H N N 435 
VAL HG23 H N N 436 
VAL HXT  H N N 437 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HCY O1  C3   doub N N 116 
HCY C3  C4   sing N N 117 
HCY C3  C2   sing N N 118 
HCY C4  C5   doub N N 119 
HCY C5  C6   sing N N 120 
HCY C5  C10  sing N N 121 
HCY C6  C7   sing N N 122 
HCY C7  C8   sing N N 123 
HCY C2  C1   sing N N 124 
HCY C1  C10  sing N N 125 
HCY C10 C19  sing N N 126 
HCY C10 C9   sing N N 127 
HCY C9  C8   sing N N 128 
HCY C9  C11  sing N N 129 
HCY C8  C14  sing N N 130 
HCY C11 O2   sing N N 131 
HCY C11 C12  sing N N 132 
HCY C12 C13  sing N N 133 
HCY C13 C18  sing N N 134 
HCY C13 C14  sing N N 135 
HCY C13 C17  sing N N 136 
HCY C14 C15  sing N N 137 
HCY C15 C16  sing N N 138 
HCY C16 C17  sing N N 139 
HCY C17 O3   sing N N 140 
HCY C17 C20  sing N N 141 
HCY C20 O4   doub N N 142 
HCY C20 C21  sing N N 143 
HCY C21 O5   sing N N 144 
HCY C4  H4   sing N N 145 
HCY C2  H2C1 sing N N 146 
HCY C2  H2C2 sing N N 147 
HCY C6  H6C1 sing N N 148 
HCY C6  H6C2 sing N N 149 
HCY C7  H7C1 sing N N 150 
HCY C7  H7C2 sing N N 151 
HCY C8  H8   sing N N 152 
HCY C1  H1C1 sing N N 153 
HCY C1  H1C2 sing N N 154 
HCY C19 H191 sing N N 155 
HCY C19 H192 sing N N 156 
HCY C19 H193 sing N N 157 
HCY C9  H9   sing N N 158 
HCY C11 H11  sing N N 159 
HCY C14 H14  sing N N 160 
HCY O2  H2   sing N N 161 
HCY C12 H121 sing N N 162 
HCY C12 H122 sing N N 163 
HCY C18 H181 sing N N 164 
HCY C18 H182 sing N N 165 
HCY C18 H183 sing N N 166 
HCY C15 H151 sing N N 167 
HCY C15 H152 sing N N 168 
HCY C16 H161 sing N N 169 
HCY C16 H162 sing N N 170 
HCY O3  H3   sing N N 171 
HCY C21 H211 sing N N 172 
HCY C21 H212 sing N N 173 
HCY O5  H5   sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PHE N   CA   sing N N 283 
PHE N   H    sing N N 284 
PHE N   H2   sing N N 285 
PHE CA  C    sing N N 286 
PHE CA  CB   sing N N 287 
PHE CA  HA   sing N N 288 
PHE C   O    doub N N 289 
PHE C   OXT  sing N N 290 
PHE CB  CG   sing N N 291 
PHE CB  HB2  sing N N 292 
PHE CB  HB3  sing N N 293 
PHE CG  CD1  doub Y N 294 
PHE CG  CD2  sing Y N 295 
PHE CD1 CE1  sing Y N 296 
PHE CD1 HD1  sing N N 297 
PHE CD2 CE2  doub Y N 298 
PHE CD2 HD2  sing N N 299 
PHE CE1 CZ   doub Y N 300 
PHE CE1 HE1  sing N N 301 
PHE CE2 CZ   sing Y N 302 
PHE CE2 HE2  sing N N 303 
PHE CZ  HZ   sing N N 304 
PHE OXT HXT  sing N N 305 
PRO N   CA   sing N N 306 
PRO N   CD   sing N N 307 
PRO N   H    sing N N 308 
PRO CA  C    sing N N 309 
PRO CA  CB   sing N N 310 
PRO CA  HA   sing N N 311 
PRO C   O    doub N N 312 
PRO C   OXT  sing N N 313 
PRO CB  CG   sing N N 314 
PRO CB  HB2  sing N N 315 
PRO CB  HB3  sing N N 316 
PRO CG  CD   sing N N 317 
PRO CG  HG2  sing N N 318 
PRO CG  HG3  sing N N 319 
PRO CD  HD2  sing N N 320 
PRO CD  HD3  sing N N 321 
PRO OXT HXT  sing N N 322 
SER N   CA   sing N N 323 
SER N   H    sing N N 324 
SER N   H2   sing N N 325 
SER CA  C    sing N N 326 
SER CA  CB   sing N N 327 
SER CA  HA   sing N N 328 
SER C   O    doub N N 329 
SER C   OXT  sing N N 330 
SER CB  OG   sing N N 331 
SER CB  HB2  sing N N 332 
SER CB  HB3  sing N N 333 
SER OG  HG   sing N N 334 
SER OXT HXT  sing N N 335 
SO4 S   O1   doub N N 336 
SO4 S   O2   doub N N 337 
SO4 S   O3   sing N N 338 
SO4 S   O4   sing N N 339 
THR N   CA   sing N N 340 
THR N   H    sing N N 341 
THR N   H2   sing N N 342 
THR CA  C    sing N N 343 
THR CA  CB   sing N N 344 
THR CA  HA   sing N N 345 
THR C   O    doub N N 346 
THR C   OXT  sing N N 347 
THR CB  OG1  sing N N 348 
THR CB  CG2  sing N N 349 
THR CB  HB   sing N N 350 
THR OG1 HG1  sing N N 351 
THR CG2 HG21 sing N N 352 
THR CG2 HG22 sing N N 353 
THR CG2 HG23 sing N N 354 
THR OXT HXT  sing N N 355 
TRP N   CA   sing N N 356 
TRP N   H    sing N N 357 
TRP N   H2   sing N N 358 
TRP CA  C    sing N N 359 
TRP CA  CB   sing N N 360 
TRP CA  HA   sing N N 361 
TRP C   O    doub N N 362 
TRP C   OXT  sing N N 363 
TRP CB  CG   sing N N 364 
TRP CB  HB2  sing N N 365 
TRP CB  HB3  sing N N 366 
TRP CG  CD1  doub Y N 367 
TRP CG  CD2  sing Y N 368 
TRP CD1 NE1  sing Y N 369 
TRP CD1 HD1  sing N N 370 
TRP CD2 CE2  doub Y N 371 
TRP CD2 CE3  sing Y N 372 
TRP NE1 CE2  sing Y N 373 
TRP NE1 HE1  sing N N 374 
TRP CE2 CZ2  sing Y N 375 
TRP CE3 CZ3  doub Y N 376 
TRP CE3 HE3  sing N N 377 
TRP CZ2 CH2  doub Y N 378 
TRP CZ2 HZ2  sing N N 379 
TRP CZ3 CH2  sing Y N 380 
TRP CZ3 HZ3  sing N N 381 
TRP CH2 HH2  sing N N 382 
TRP OXT HXT  sing N N 383 
TYR N   CA   sing N N 384 
TYR N   H    sing N N 385 
TYR N   H2   sing N N 386 
TYR CA  C    sing N N 387 
TYR CA  CB   sing N N 388 
TYR CA  HA   sing N N 389 
TYR C   O    doub N N 390 
TYR C   OXT  sing N N 391 
TYR CB  CG   sing N N 392 
TYR CB  HB2  sing N N 393 
TYR CB  HB3  sing N N 394 
TYR CG  CD1  doub Y N 395 
TYR CG  CD2  sing Y N 396 
TYR CD1 CE1  sing Y N 397 
TYR CD1 HD1  sing N N 398 
TYR CD2 CE2  doub Y N 399 
TYR CD2 HD2  sing N N 400 
TYR CE1 CZ   doub Y N 401 
TYR CE1 HE1  sing N N 402 
TYR CE2 CZ   sing Y N 403 
TYR CE2 HE2  sing N N 404 
TYR CZ  OH   sing N N 405 
TYR OH  HH   sing N N 406 
TYR OXT HXT  sing N N 407 
VAL N   CA   sing N N 408 
VAL N   H    sing N N 409 
VAL N   H2   sing N N 410 
VAL CA  C    sing N N 411 
VAL CA  CB   sing N N 412 
VAL CA  HA   sing N N 413 
VAL C   O    doub N N 414 
VAL C   OXT  sing N N 415 
VAL CB  CG1  sing N N 416 
VAL CB  CG2  sing N N 417 
VAL CB  HB   sing N N 418 
VAL CG1 HG11 sing N N 419 
VAL CG1 HG12 sing N N 420 
VAL CG1 HG13 sing N N 421 
VAL CG2 HG21 sing N N 422 
VAL CG2 HG22 sing N N 423 
VAL CG2 HG23 sing N N 424 
VAL OXT HXT  sing N N 425 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other private'                          ?               ? 1 
'Howard Hughes Medical Institute (HHMI)' 'United States' ? 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8UQF 
_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]   0.020826 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001453 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020572 
_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]   0.017762 
_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   . SER A 1 6   ? -7.21400  0.41800   8.74400   1.000 68.85167 ? 3   SER A N   1 
ATOM   2    C CA  . SER A 1 6   ? -6.09000  1.21100   8.27500   1.000 66.18239 ? 3   SER A CA  1 
ATOM   3    C C   . SER A 1 6   ? -4.89200  0.88000   9.11100   1.000 66.71175 ? 3   SER A C   1 
ATOM   4    O O   . SER A 1 6   ? -3.77700  0.82400   8.62000   1.000 68.41059 ? 3   SER A O   1 
ATOM   5    C CB  . SER A 1 6   ? -6.39900  2.70400   8.34100   1.000 73.37319 ? 3   SER A CB  1 
ATOM   6    O OG  . SER A 1 6   ? -5.74300  3.34600   9.41600   1.000 69.32962 ? 3   SER A OG  1 
ATOM   7    N N   . GLU A 1 7   ? -5.12100  0.60800   10.38200  1.000 66.84015 ? 4   GLU A N   1 
ATOM   8    C CA  . GLU A 1 7   ? -4.03800  0.25000   11.24500  1.000 66.03084 ? 4   GLU A CA  1 
ATOM   9    C C   . GLU A 1 7   ? -3.58400  -1.11400  10.79300  1.000 61.87250 ? 4   GLU A C   1 
ATOM   10   O O   . GLU A 1 7   ? -2.43200  -1.32700  10.71600  1.000 58.81240 ? 4   GLU A O   1 
ATOM   11   C CB  . GLU A 1 7   ? -4.42600  0.27700   12.71300  1.000 66.93018 ? 4   GLU A CB  1 
ATOM   12   C CG  . GLU A 1 7   ? -3.33200  0.83000   13.59700  1.000 69.85856 ? 4   GLU A CG  1 
ATOM   13   C CD  . GLU A 1 7   ? -3.79400  1.08600   15.02200  1.000 76.44594 ? 4   GLU A CD  1 
ATOM   14   O OE1 . GLU A 1 7   ? -4.82400  1.77500   15.19100  1.000 78.11742 ? 4   GLU A OE1 1 
ATOM   15   O OE2 . GLU A 1 7   ? -3.11800  0.62700   15.97300  1.000 68.93189 ? 4   GLU A OE2 1 
ATOM   16   N N   . GLU A 1 8   ? -4.49700  -2.01300  10.44900  1.000 62.18047 ? 5   GLU A N   1 
ATOM   17   C CA  . GLU A 1 8   ? -4.14400  -3.30500  9.92200   1.000 62.44084 ? 5   GLU A CA  1 
ATOM   18   C C   . GLU A 1 8   ? -3.32300  -3.15400  8.63600   1.000 59.57417 ? 5   GLU A C   1 
ATOM   19   O O   . GLU A 1 8   ? -2.35200  -3.82600  8.45000   1.000 58.66274 ? 5   GLU A O   1 
ATOM   20   C CB  . GLU A 1 8   ? -5.40100  -4.10900  9.66900   1.000 60.64866 ? 5   GLU A CB  1 
ATOM   21   C CG  . GLU A 1 8   ? -6.29600  -4.24100  10.88400  1.000 63.96413 ? 5   GLU A CG  1 
ATOM   22   C CD  . GLU A 1 8   ? -7.54700  -5.03700  10.57200  1.000 70.55294 ? 5   GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 8   ? -8.35700  -4.55400  9.75600   1.000 70.70077 ? 5   GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 8   ? -7.71400  -6.14600  11.13500  1.000 71.59241 ? 5   GLU A OE2 1 
ATOM   25   N N   . ALA A 1 9   ? -3.71900  -2.25500  7.76200   1.000 62.29183 ? 6   ALA A N   1 
ATOM   26   C CA  . ALA A 1 9   ? -2.98700  -2.00200  6.55000   1.000 57.51823 ? 6   ALA A CA  1 
ATOM   27   C C   . ALA A 1 9   ? -1.56700  -1.59600  6.88200   1.000 56.01931 ? 6   ALA A C   1 
ATOM   28   O O   . ALA A 1 9   ? -0.62200  -2.14500  6.34200   1.000 50.62959 ? 6   ALA A O   1 
ATOM   29   C CB  . ALA A 1 9   ? -3.65800  -0.91500  5.72900   1.000 62.04564 ? 6   ALA A CB  1 
ATOM   30   N N   . LYS A 1 10  ? -1.42500  -0.63600  7.77400   1.000 57.82107 ? 7   LYS A N   1 
ATOM   31   C CA  . LYS A 1 10  ? -0.12800  -0.16100  8.18000   1.000 52.92965 ? 7   LYS A CA  1 
ATOM   32   C C   . LYS A 1 10  ? 0.70300   -1.26700  8.78800   1.000 50.90346 ? 7   LYS A C   1 
ATOM   33   O O   . LYS A 1 10  ? 1.84000   -1.44700  8.48200   1.000 40.12512 ? 7   LYS A O   1 
ATOM   34   C CB  . LYS A 1 10  ? -0.26000  0.93600   9.22500   1.000 55.35036 ? 7   LYS A CB  1 
ATOM   35   C CG  . LYS A 1 10  ? -0.17800  2.37000   8.71300   1.000 53.98815 ? 7   LYS A CG  1 
ATOM   36   C CD  . LYS A 1 10  ? -0.14400  3.37300   9.88700   1.000 62.68751 ? 7   LYS A CD  1 
ATOM   37   C CE  . LYS A 1 10  ? -0.23100  4.86000   9.50900   1.000 59.85792 ? 7   LYS A CE  1 
ATOM   38   N NZ  . LYS A 1 10  ? 0.79100   5.73600   10.16900  1.000 54.75712 ? 7   LYS A NZ  1 
ATOM   39   N N   . GLU A 1 11  ? 0.08500   -2.04100  9.63400   1.000 48.03684 ? 8   GLU A N   1 
ATOM   40   C CA  . GLU A 1 11  ? 0.75800   -3.08000  10.33800  1.000 47.53756 ? 8   GLU A CA  1 
ATOM   41   C C   . GLU A 1 11  ? 1.23500   -4.14400  9.42100   1.000 42.57617 ? 8   GLU A C   1 
ATOM   42   O O   . GLU A 1 11  ? 2.21700   -4.73600  9.65900   1.000 40.44356 ? 8   GLU A O   1 
ATOM   43   C CB  . GLU A 1 11  ? -0.17000  -3.66000  11.39900  1.000 47.44482 ? 8   GLU A CB  1 
ATOM   44   C CG  . GLU A 1 11  ? -0.28000  -2.78100  12.60500  1.000 52.37775 ? 8   GLU A CG  1 
ATOM   45   C CD  . GLU A 1 11  ? -1.18100  -3.37500  13.64400  1.000 59.40918 ? 8   GLU A CD  1 
ATOM   46   O OE1 . GLU A 1 11  ? -0.71600  -4.28600  14.33300  1.000 58.78338 ? 8   GLU A OE1 1 
ATOM   47   O OE2 . GLU A 1 11  ? -2.33400  -2.94100  13.75600  1.000 59.67422 ? 8   GLU A OE2 1 
ATOM   48   N N   . ALA A 1 12  ? 0.49800   -4.38000  8.37000   1.000 40.93405 ? 9   ALA A N   1 
ATOM   49   C CA  . ALA A 1 12  ? 0.89700   -5.38000  7.38700   1.000 45.01239 ? 9   ALA A CA  1 
ATOM   50   C C   . ALA A 1 12  ? 2.09400   -4.90300  6.56600   1.000 41.85071 ? 9   ALA A C   1 
ATOM   51   O O   . ALA A 1 12  ? 3.01700   -5.68600  6.29100   1.000 38.83615 ? 9   ALA A O   1 
ATOM   52   C CB  . ALA A 1 12  ? -0.27900  -5.72500  6.47700   1.000 44.29924 ? 9   ALA A CB  1 
ATOM   53   N N   . ILE A 1 13  ? 2.10900   -3.64000  6.19700   1.000 37.72116 ? 10  ILE A N   1 
ATOM   54   C CA  . ILE A 1 13  ? 3.21000   -3.10300  5.44300   1.000 34.61332 ? 10  ILE A CA  1 
ATOM   55   C C   . ILE A 1 13  ? 4.47400   -3.15500  6.27500   1.000 37.65846 ? 10  ILE A C   1 
ATOM   56   O O   . ILE A 1 13  ? 5.51900   -3.50300  5.79200   1.000 33.54417 ? 10  ILE A O   1 
ATOM   57   C CB  . ILE A 1 13  ? 2.95900   -1.65700  5.02400   1.000 40.38032 ? 10  ILE A CB  1 
ATOM   58   C CG1 . ILE A 1 13  ? 1.73800   -1.54700  4.13700   1.000 44.39290 ? 10  ILE A CG1 1 
ATOM   59   C CG2 . ILE A 1 13  ? 4.13000   -1.11600  4.26200   1.000 38.43096 ? 10  ILE A CG2 1 
ATOM   60   C CD1 . ILE A 1 13  ? 1.99100   -1.92300  2.71300   1.000 40.86389 ? 10  ILE A CD1 1 
ATOM   61   N N   . ILE A 1 14  ? 4.37200   -2.78900  7.53400   1.000 34.11028 ? 11  ILE A N   1 
ATOM   62   C CA  . ILE A 1 14  ? 5.52800   -2.81800  8.38500   1.000 32.93165 ? 11  ILE A CA  1 
ATOM   63   C C   . ILE A 1 14  ? 6.05000   -4.20500  8.51700   1.000 35.16809 ? 11  ILE A C   1 
ATOM   64   O O   . ILE A 1 14  ? 7.21100   -4.41700  8.46300   1.000 33.71443 ? 11  ILE A O   1 
ATOM   65   C CB  . ILE A 1 14  ? 5.21500   -2.30200  9.79100   1.000 36.43218 ? 11  ILE A CB  1 
ATOM   66   C CG1 . ILE A 1 14  ? 4.97000   -0.82800  9.70100   1.000 40.79369 ? 11  ILE A CG1 1 
ATOM   67   C CG2 . ILE A 1 14  ? 6.34800   -2.54100  10.75100  1.000 37.25008 ? 11  ILE A CG2 1 
ATOM   68   C CD1 . ILE A 1 14  ? 4.89900   -0.12400  11.02300  1.000 41.94048 ? 11  ILE A CD1 1 
ATOM   69   N N   . ALA A 1 15  ? 5.16300   -5.14000  8.75100   1.000 33.45867 ? 12  ALA A N   1 
ATOM   70   C CA  . ALA A 1 15  ? 5.59200   -6.52100  8.89200   1.000 33.63702 ? 12  ALA A CA  1 
ATOM   71   C C   . ALA A 1 15  ? 6.33100   -6.98200  7.64500   1.000 32.15283 ? 12  ALA A C   1 
ATOM   72   O O   . ALA A 1 15  ? 7.33700   -7.69900  7.74400   1.000 32.96945 ? 12  ALA A O   1 
ATOM   73   C CB  . ALA A 1 15  ? 4.39000   -7.42600  9.16100   1.000 35.23091 ? 12  ALA A CB  1 
ATOM   74   N N   . MET A 1 16  ? 5.84700   -6.60600  6.47500   1.000 30.59841 ? 13  MET A N   1 
ATOM   75   C CA  . MET A 1 16  ? 6.48400   -6.97900  5.22400   1.000 30.82653 ? 13  MET A CA  1 
ATOM   76   C C   . MET A 1 16  ? 7.86800   -6.38000  5.10300   1.000 29.70445 ? 13  MET A C   1 
ATOM   77   O O   . MET A 1 16  ? 8.73100   -7.02000  4.62500   1.000 29.54123 ? 13  MET A O   1 
ATOM   78   C CB  . MET A 1 16  ? 5.64300   -6.62400  4.00200   1.000 28.55336 ? 13  MET A CB  1 
ATOM   79   C CG  . MET A 1 16  ? 4.44000   -7.53500  3.80600   1.000 42.94367 ? 13  MET A CG  1 
ATOM   80   S SD  . MET A 1 16  ? 3.44800   -7.17800  2.34600   1.000 52.09298 ? 13  MET A SD  1 
ATOM   81   C CE  . MET A 1 16  ? 4.32500   -8.07600  1.09600   1.000 43.57152 ? 13  MET A CE  1 
ATOM   82   N N   . LEU A 1 17  ? 8.05400   -5.14700  5.52600   1.000 24.84346 ? 14  LEU A N   1 
ATOM   83   C CA  . LEU A 1 17  ? 9.38800   -4.55100  5.48400   1.000 23.61970 ? 14  LEU A CA  1 
ATOM   84   C C   . LEU A 1 17  ? 10.32800  -5.23800  6.46000   1.000 27.35959 ? 14  LEU A C   1 
ATOM   85   O O   . LEU A 1 17  ? 11.51300  -5.40600  6.16700   1.000 24.76208 ? 14  LEU A O   1 
ATOM   86   C CB  . LEU A 1 17  ? 9.32300   -3.05400  5.78800   1.000 28.94726 ? 14  LEU A CB  1 
ATOM   87   C CG  . LEU A 1 17  ? 8.67300   -2.26700  4.66100   1.000 30.64207 ? 14  LEU A CG  1 
ATOM   88   C CD1 . LEU A 1 17  ? 8.47400   -0.82700  5.11600   1.000 35.37322 ? 14  LEU A CD1 1 
ATOM   89   C CD2 . LEU A 1 17  ? 9.51000   -2.32800  3.37000   1.000 30.62908 ? 14  LEU A CD2 1 
ATOM   90   N N   . LYS A 1 18  ? 9.81900   -5.64000  7.63200   1.000 28.87502 ? 15  LYS A N   1 
ATOM   91   C CA  . LYS A 1 18  ? 10.60200  -6.50100  8.51500   1.000 29.06621 ? 15  LYS A CA  1 
ATOM   92   C C   . LYS A 1 18  ? 11.02100  -7.77900  7.79400   1.000 29.84701 ? 15  LYS A C   1 
ATOM   93   O O   . LYS A 1 18  ? 12.17600  -8.20500  7.88500   1.000 28.29011 ? 15  LYS A O   1 
ATOM   94   C CB  . LYS A 1 18  ? 9.78000   -6.84900  9.76300   1.000 33.10702 ? 15  LYS A CB  1 
ATOM   95   C CG  . LYS A 1 18  ? 10.46700  -7.81300  10.72500  1.000 39.28597 ? 15  LYS A CG  1 
ATOM   96   C CD  . LYS A 1 18  ? 9.47000   -8.58600  11.57000  1.000 44.78035 ? 15  LYS A CD  1 
ATOM   97   C CE  . LYS A 1 18  ? 10.05500  -9.92000  12.01300  1.000 50.33142 ? 15  LYS A CE  1 
ATOM   98   N NZ  . LYS A 1 18  ? 10.31200  -10.82400 10.84800  1.000 52.03616 ? 15  LYS A NZ  1 
ATOM   99   N N   . GLU A 1 19  ? 10.07300  -8.42800  7.11300   1.000 27.08336 ? 16  GLU A N   1 
ATOM   100  C CA  . GLU A 1 19  ? 10.39800  -9.63800  6.37100   1.000 27.82882 ? 16  GLU A CA  1 
ATOM   101  C C   . GLU A 1 19  ? 11.46400  -9.36100  5.31900   1.000 26.16287 ? 16  GLU A C   1 
ATOM   102  O O   . GLU A 1 19  ? 12.37600  -10.18400 5.10800   1.000 24.97265 ? 16  GLU A O   1 
ATOM   103  C CB  . GLU A 1 19  ? 9.14500   -10.19900 5.70700   1.000 29.54630 ? 16  GLU A CB  1 
ATOM   104  C CG  . GLU A 1 19  ? 9.36000   -11.58800 5.13000   1.000 39.70162 ? 16  GLU A CG  1 
ATOM   105  C CD  . GLU A 1 19  ? 8.27200   -12.00600 4.16700   1.000 39.05342 ? 16  GLU A CD  1 
ATOM   106  O OE1 . GLU A 1 19  ? 7.14800   -11.45200 4.24600   1.000 43.38151 ? 16  GLU A OE1 1 
ATOM   107  O OE2 . GLU A 1 19  ? 8.55100   -12.88700 3.32200   1.000 48.65476 ? 16  GLU A OE2 1 
ATOM   108  N N   . TRP A 1 20  ? 11.36100  -8.21200  4.64300   1.000 24.20865 ? 17  TRP A N   1 
ATOM   109  C CA  . TRP A 1 20  ? 12.27900  -7.87300  3.56000   1.000 22.53693 ? 17  TRP A CA  1 
ATOM   110  C C   . TRP A 1 20  ? 13.70700  -7.81100  4.08700   1.000 21.03451 ? 17  TRP A C   1 
ATOM   111  O O   . TRP A 1 20  ? 14.61400  -8.48100  3.58200   1.000 20.37964 ? 17  TRP A O   1 
ATOM   112  C CB  . TRP A 1 20  ? 11.87800  -6.51600  2.94200   1.000 20.71019 ? 17  TRP A CB  1 
ATOM   113  C CG  . TRP A 1 20  ? 12.81700  -6.04500  1.86100   1.000 20.89742 ? 17  TRP A CG  1 
ATOM   114  C CD1 . TRP A 1 20  ? 13.94100  -5.28500  2.02600   1.000 22.29681 ? 17  TRP A CD1 1 
ATOM   115  C CD2 . TRP A 1 20  ? 12.74600  -6.35900  0.45600   1.000 18.83986 ? 17  TRP A CD2 1 
ATOM   116  N NE1 . TRP A 1 20  ? 14.59300  -5.12600  0.81700   1.000 22.63218 ? 17  TRP A NE1 1 
ATOM   117  C CE2 . TRP A 1 20  ? 13.86900  -5.77500  -0.16300  1.000 19.64538 ? 17  TRP A CE2 1 
ATOM   118  C CE3 . TRP A 1 20  ? 11.86300  -7.10700  -0.32600  1.000 20.60071 ? 17  TRP A CE3 1 
ATOM   119  C CZ2 . TRP A 1 20  ? 14.11600  -5.89100  -1.50900  1.000 26.79772 ? 17  TRP A CZ2 1 
ATOM   120  C CZ3 . TRP A 1 20  ? 12.10200  -7.20800  -1.66600  1.000 22.40067 ? 17  TRP A CZ3 1 
ATOM   121  C CH2 . TRP A 1 20  ? 13.19700  -6.58900  -2.26200  1.000 25.98284 ? 17  TRP A CH2 1 
ATOM   122  N N   . TYR A 1 21  ? 13.90400  -6.99900  5.08400   1.000 22.93757 ? 18  TYR A N   1 
ATOM   123  C CA  . TYR A 1 21  ? 15.20900  -6.84300  5.59500   1.000 19.91000 ? 18  TYR A CA  1 
ATOM   124  C C   . TYR A 1 21  ? 15.69800  -8.10500  6.30300   1.000 20.02549 ? 18  TYR A C   1 
ATOM   125  O O   . TYR A 1 21  ? 16.84000  -8.38300  6.26000   1.000 23.72861 ? 18  TYR A O   1 
ATOM   126  C CB  . TYR A 1 21  ? 15.31200  -5.55200  6.42800   1.000 24.46508 ? 18  TYR A CB  1 
ATOM   127  C CG  . TYR A 1 21  ? 15.18000  -4.29100  5.56100   1.000 22.87860 ? 18  TYR A CG  1 
ATOM   128  C CD1 . TYR A 1 21  ? 16.17900  -3.88000  4.73800   1.000 19.85776 ? 18  TYR A CD1 1 
ATOM   129  C CD2 . TYR A 1 21  ? 14.04200  -3.57100  5.54000   1.000 21.83890 ? 18  TYR A CD2 1 
ATOM   130  C CE1 . TYR A 1 21  ? 16.05800  -2.78200  3.94900   1.000 23.11181 ? 18  TYR A CE1 1 
ATOM   131  C CE2 . TYR A 1 21  ? 13.91800  -2.50200  4.74500   1.000 20.38591 ? 18  TYR A CE2 1 
ATOM   132  C CZ  . TYR A 1 21  ? 14.96900  -2.10400  4.02800   1.000 19.12203 ? 18  TYR A CZ  1 
ATOM   133  O OH  . TYR A 1 21  ? 14.79500  -1.05000  3.16600   1.000 22.80178 ? 18  TYR A OH  1 
ATOM   134  N N   . ASP A 1 22  ? 14.81100  -8.86100  6.91900   1.000 24.15663 ? 19  ASP A N   1 
ATOM   135  C CA  . ASP A 1 22  ? 15.22600  -10.09100 7.55300   1.000 27.73699 ? 19  ASP A CA  1 
ATOM   136  C C   . ASP A 1 22  ? 15.65900  -11.07200 6.48000   1.000 27.11164 ? 19  ASP A C   1 
ATOM   137  O O   . ASP A 1 22  ? 16.63700  -11.71100 6.63100   1.000 25.42673 ? 19  ASP A O   1 
ATOM   138  C CB  . ASP A 1 22  ? 14.12200  -10.70600 8.38800   1.000 29.46973 ? 19  ASP A CB  1 
ATOM   139  C CG  . ASP A 1 22  ? 13.95800  -10.04700 9.74900   1.000 33.79039 ? 19  ASP A CG  1 
ATOM   140  O OD1 . ASP A 1 22  ? 14.72200  -9.19800  10.14900  1.000 36.21224 ? 19  ASP A OD1 1 
ATOM   141  O OD2 . ASP A 1 22  ? 12.93400  -10.31300 10.36700  1.000 35.73480 ? 19  ASP A OD2 1 
ATOM   142  N N   . ALA A 1 23  ? 14.91800  -11.17100 5.40000   1.000 23.37502 ? 20  ALA A N   1 
ATOM   143  C CA  . ALA A 1 23  ? 15.28700  -12.06900 4.31200   1.000 24.59995 ? 20  ALA A CA  1 
ATOM   144  C C   . ALA A 1 23  ? 16.62700  -11.68400 3.70500   1.000 25.00573 ? 20  ALA A C   1 
ATOM   145  O O   . ALA A 1 23  ? 17.37900  -12.51000 3.27300   1.000 23.84625 ? 20  ALA A O   1 
ATOM   146  C CB  . ALA A 1 23  ? 14.22300  -12.07700 3.24100   1.000 27.47975 ? 20  ALA A CB  1 
ATOM   147  N N   . MET A 1 24  ? 16.89400  -10.39600 3.68900   1.000 21.33713 ? 21  MET A N   1 
ATOM   148  C CA  . MET A 1 24  ? 18.13500  -9.91800  3.18700   1.000 21.75842 ? 21  MET A CA  1 
ATOM   149  C C   . MET A 1 24  ? 19.26700  -10.42600 4.05500   1.000 21.42436 ? 21  MET A C   1 
ATOM   150  O O   . MET A 1 24  ? 20.17900  -10.96600 3.56600   1.000 22.06166 ? 21  MET A O   1 
ATOM   151  C CB  . MET A 1 24  ? 18.14600  -8.39500  3.14500   1.000 22.68689 ? 21  MET A CB  1 
ATOM   152  C CG  . MET A 1 24  ? 19.18400  -7.81300  2.22800   1.000 23.94605 ? 21  MET A CG  1 
ATOM   153  S SD  . MET A 1 24  ? 18.84700  -8.06600  0.47100   1.000 25.14586 ? 21  MET A SD  1 
ATOM   154  C CE  . MET A 1 24  ? 17.46300  -6.96100  0.28300   1.000 28.50548 ? 21  MET A CE  1 
ATOM   155  N N   . ASN A 1 25  ? 19.16800  -10.30600 5.34900   1.000 23.06334 ? 22  ASN A N   1 
ATOM   156  C CA  . ASN A 1 25  ? 20.22100  -10.81900 6.20800   1.000 21.37770 ? 22  ASN A CA  1 
ATOM   157  C C   . ASN A 1 25  ? 20.31500  -12.34200 6.16200   1.000 24.96673 ? 22  ASN A C   1 
ATOM   158  O O   . ASN A 1 25  ? 21.36500  -12.87500 6.23700   1.000 27.34869 ? 22  ASN A O   1 
ATOM   159  C CB  . ASN A 1 25  ? 20.01500  -10.38600 7.63000   1.000 23.25556 ? 22  ASN A CB  1 
ATOM   160  C CG  . ASN A 1 25  ? 20.38500  -8.96700  7.85600   1.000 26.00943 ? 22  ASN A CG  1 
ATOM   161  O OD1 . ASN A 1 25  ? 21.25400  -8.46400  7.24000   1.000 25.99090 ? 22  ASN A OD1 1 
ATOM   162  N ND2 . ASN A 1 25  ? 19.69900  -8.33800  8.72800   1.000 27.69002 ? 22  ASN A ND2 1 
ATOM   163  N N   . GLU A 1 26  ? 19.19300  -13.01200 5.90300   1.000 23.62227 ? 23  GLU A N   1 
ATOM   164  C CA  . GLU A 1 26  ? 19.20800  -14.46500 5.77800   1.000 24.32521 ? 23  GLU A CA  1 
ATOM   165  C C   . GLU A 1 26  ? 19.77600  -14.91700 4.44000   1.000 29.43115 ? 23  GLU A C   1 
ATOM   166  O O   . GLU A 1 26  ? 20.10900  -16.10500 4.28500   1.000 27.13728 ? 23  GLU A O   1 
ATOM   167  C CB  . GLU A 1 26  ? 17.79600  -15.01300 5.95700   1.000 28.06192 ? 23  GLU A CB  1 
ATOM   168  C CG  . GLU A 1 26  ? 17.19600  -14.77200 7.31500   1.000 32.90014 ? 23  GLU A CG  1 
ATOM   169  C CD  . GLU A 1 26  ? 15.68900  -14.87400 7.30600   1.000 35.01611 ? 23  GLU A CD  1 
ATOM   170  O OE1 . GLU A 1 26  ? 15.11100  -15.20800 6.24600   1.000 39.04560 ? 23  GLU A OE1 1 
ATOM   171  O OE2 . GLU A 1 26  ? 15.08200  -14.61300 8.36300   1.000 43.98340 ? 23  GLU A OE2 1 
ATOM   172  N N   . GLY A 1 27  ? 19.84800  -14.01600 3.45000   1.000 21.10274 ? 24  GLY A N   1 
ATOM   173  C CA  . GLY A 1 27  ? 20.20500  -14.40000 2.10900   1.000 22.57362 ? 24  GLY A CA  1 
ATOM   174  C C   . GLY A 1 27  ? 19.12300  -15.14400 1.36100   1.000 27.52709 ? 24  GLY A C   1 
ATOM   175  O O   . GLY A 1 27  ? 19.42800  -15.89100 0.43000   1.000 26.69983 ? 24  GLY A O   1 
ATOM   176  N N   . ASP A 1 28  ? 17.86600  -14.96700 1.75900   1.000 24.17266 ? 25  ASP A N   1 
ATOM   177  C CA  . ASP A 1 28  ? 16.74100  -15.72600 1.22000   1.000 25.24532 ? 25  ASP A CA  1 
ATOM   178  C C   . ASP A 1 28  ? 16.04000  -14.93100 0.11900   1.000 23.81750 ? 25  ASP A C   1 
ATOM   179  O O   . ASP A 1 28  ? 15.07600  -14.20200 0.36300   1.000 23.46471 ? 25  ASP A O   1 
ATOM   180  C CB  . ASP A 1 28  ? 15.76900  -16.08400 2.32700   1.000 27.18734 ? 25  ASP A CB  1 
ATOM   181  C CG  . ASP A 1 28  ? 14.72000  -17.05000 1.84800   1.000 37.88249 ? 25  ASP A CG  1 
ATOM   182  O OD1 . ASP A 1 28  ? 14.63200  -17.22700 0.60700   1.000 35.19722 ? 25  ASP A OD1 1 
ATOM   183  O OD2 . ASP A 1 28  ? 14.01300  -17.64400 2.69100   1.000 41.02061 ? 25  ASP A OD2 1 
ATOM   184  N N   . MET A 1 29  ? 16.51900  -15.09100 -1.10400  1.000 21.79300 ? 26  MET A N   1 
ATOM   185  C CA  . MET A 1 29  ? 15.93500  -14.33400 -2.20400  1.000 25.03667 ? 26  MET A CA  1 
ATOM   186  C C   . MET A 1 29  ? 14.57600  -14.86900 -2.61100  1.000 28.57159 ? 26  MET A C   1 
ATOM   187  O O   . MET A 1 29  ? 13.81400  -14.12900 -3.23400  1.000 25.22513 ? 26  MET A O   1 
ATOM   188  C CB  . MET A 1 29  ? 16.86600  -14.33100 -3.41100  1.000 22.51152 ? 26  MET A CB  1 
ATOM   189  C CG  . MET A 1 29  ? 18.13200  -13.61800 -3.15700  1.000 23.10531 ? 26  MET A CG  1 
ATOM   190  S SD  . MET A 1 29  ? 19.13000  -13.40300 -4.57100  1.000 25.93751 ? 26  MET A SD  1 
ATOM   191  C CE  . MET A 1 29  ? 18.01700  -12.41400 -5.60200  1.000 28.72690 ? 26  MET A CE  1 
ATOM   192  N N   . GLU A 1 30  ? 14.18100  -16.06000 -2.20400  1.000 26.65471 ? 27  GLU A N   1 
ATOM   193  C CA  . GLU A 1 30  ? 12.84600  -16.50700 -2.51000  1.000 27.00079 ? 27  GLU A CA  1 
ATOM   194  C C   . GLU A 1 30  ? 11.85600  -15.62100 -1.83800  1.000 29.33555 ? 27  GLU A C   1 
ATOM   195  O O   . GLU A 1 30  ? 10.81700  -15.34500 -2.35800  1.000 30.51309 ? 27  GLU A O   1 
ATOM   196  C CB  . GLU A 1 30  ? 12.63200  -17.92500 -2.01700  1.000 33.98390 ? 27  GLU A CB  1 
ATOM   197  C CG  . GLU A 1 30  ? 11.29100  -18.27400 -1.37400  1.000 44.45502 ? 27  GLU A CG  1 
ATOM   198  C CD  . GLU A 1 30  ? 11.47100  -19.28500 -0.27500  1.000 47.91114 ? 27  GLU A CD  1 
ATOM   199  O OE1 . GLU A 1 30  ? 11.97300  -20.35900 -0.62600  1.000 53.74438 ? 27  GLU A OE1 1 
ATOM   200  O OE2 . GLU A 1 30  ? 11.15100  -19.00600 0.90000   1.000 46.98166 ? 27  GLU A OE2 1 
ATOM   201  N N   . LYS A 1 31  ? 12.17000  -15.21500 -0.63400  1.000 25.22095 ? 28  LYS A N   1 
ATOM   202  C CA  . LYS A 1 31  ? 11.26400  -14.36100 0.10400   1.000 30.67809 ? 28  LYS A CA  1 
ATOM   203  C C   . LYS A 1 31  ? 11.24300  -12.97400 -0.51200  1.000 28.92171 ? 28  LYS A C   1 
ATOM   204  O O   . LYS A 1 31  ? 10.22200  -12.40200 -0.62500  1.000 27.75020 ? 28  LYS A O   1 
ATOM   205  C CB  . LYS A 1 31  ? 11.63700  -14.28600 1.56500   1.000 28.37173 ? 28  LYS A CB  1 
ATOM   206  C CG  . LYS A 1 31  ? 11.31200  -15.52600 2.36800   1.000 38.23345 ? 28  LYS A CG  1 
ATOM   207  C CD  . LYS A 1 31  ? 11.76800  -15.41800 3.81100   1.000 42.50564 ? 28  LYS A CD  1 
ATOM   208  C CE  . LYS A 1 31  ? 11.66900  -16.74600 4.54300   1.000 45.81683 ? 28  LYS A CE  1 
ATOM   209  N NZ  . LYS A 1 31  ? 12.31100  -16.73100 5.89000   1.000 53.33980 ? 28  LYS A NZ  1 
ATOM   210  N N   . LEU A 1 32  ? 12.35700  -12.45800 -0.94800  1.000 20.53597 ? 29  LEU A N   1 
ATOM   211  C CA  . LEU A 1 32  ? 12.37200  -11.12900 -1.58100  1.000 19.40688 ? 29  LEU A CA  1 
ATOM   212  C C   . LEU A 1 32  ? 11.54600  -11.11200 -2.86300  1.000 23.38803 ? 29  LEU A C   1 
ATOM   213  O O   . LEU A 1 32  ? 10.76800  -10.18400 -3.11200  1.000 25.11698 ? 29  LEU A O   1 
ATOM   214  C CB  . LEU A 1 32  ? 13.80800  -10.71100 -1.90500  1.000 22.54931 ? 29  LEU A CB  1 
ATOM   215  C CG  . LEU A 1 32  ? 14.80800  -10.61100 -0.77600  1.000 25.38040 ? 29  LEU A CG  1 
ATOM   216  C CD1 . LEU A 1 32  ? 16.13700  -10.19700 -1.33100  1.000 21.92058 ? 29  LEU A CD1 1 
ATOM   217  C CD2 . LEU A 1 32  ? 14.37500  -9.58600  0.21700   1.000 21.90631 ? 29  LEU A CD2 1 
ATOM   218  N N   . ARG A 1 33  ? 11.66900  -12.14700 -3.65600  1.000 25.99608 ? 30  ARG A N   1 
ATOM   219  C CA  . ARG A 1 33  ? 10.97900  -12.19200 -4.91700  1.000 26.32559 ? 30  ARG A CA  1 
ATOM   220  C C   . ARG A 1 33  ? 9.49800   -12.11300 -4.75000  1.000 28.23096 ? 30  ARG A C   1 
ATOM   221  O O   . ARG A 1 33  ? 8.82300   -11.46100 -5.47600  1.000 27.53619 ? 30  ARG A O   1 
ATOM   222  C CB  . ARG A 1 33  ? 11.32200  -13.46400 -5.67000  1.000 27.56592 ? 30  ARG A CB  1 
ATOM   223  C CG  . ARG A 1 33  ? 10.98000  -13.38300 -7.14500  1.000 35.77544 ? 30  ARG A CG  1 
ATOM   224  C CD  . ARG A 1 33  ? 11.37600  -14.63900 -7.91500  1.000 40.46936 ? 30  ARG A CD  1 
ATOM   225  N NE  . ARG A 1 33  ? 12.76400  -14.60500 -8.35800  1.000 52.08818 ? 30  ARG A NE  1 
ATOM   226  C CZ  . ARG A 1 33  ? 13.79000  -15.10600 -7.68400  1.000 51.35616 ? 30  ARG A CZ  1 
ATOM   227  N NH1 . ARG A 1 33  ? 13.62500  -15.73500 -6.53700  1.000 48.83937 ? 30  ARG A NH1 1 
ATOM   228  N NH2 . ARG A 1 33  ? 14.98600  -15.00200 -8.18400  1.000 51.01895 ? 30  ARG A NH2 1 
ATOM   229  N N   . SER A 1 34  ? 9.00600   -12.70000 -3.69200  1.000 25.27116 ? 31  SER A N   1 
ATOM   230  C CA  . SER A 1 34  ? 7.59100   -12.72100 -3.47100  1.000 31.55018 ? 31  SER A CA  1 
ATOM   231  C C   . SER A 1 34  ? 6.96200   -11.42700 -2.97500  1.000 30.66003 ? 31  SER A C   1 
ATOM   232  O O   . SER A 1 34  ? 5.77600   -11.29000 -3.00700  1.000 32.95580 ? 31  SER A O   1 
ATOM   233  C CB  . SER A 1 34  ? 7.28300   -13.83900 -2.48600  1.000 35.72255 ? 31  SER A CB  1 
ATOM   234  O OG  . SER A 1 34  ? 7.68100   -13.49800 -1.20600  1.000 34.03528 ? 31  SER A OG  1 
ATOM   235  N N   . LEU A 1 35  ? 7.77500   -10.50300 -2.50500  1.000 23.27190 ? 32  LEU A N   1 
ATOM   236  C CA  . LEU A 1 35  ? 7.31000   -9.24000  -1.94100  1.000 26.47782 ? 32  LEU A CA  1 
ATOM   237  C C   . LEU A 1 35  ? 7.20000   -8.11800  -2.97000  1.000 25.81166 ? 32  LEU A C   1 
ATOM   238  O O   . LEU A 1 35  ? 6.65300   -7.05200  -2.65800  1.000 28.14505 ? 32  LEU A O   1 
ATOM   239  C CB  . LEU A 1 35  ? 8.26300   -8.81900  -0.80100  1.000 24.50235 ? 32  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 35  ? 8.16700   -9.68900  0.46400   1.000 24.76874 ? 32  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 35  ? 9.36600   -9.47600  1.41500   1.000 29.11584 ? 32  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 35  ? 6.86700   -9.44000  1.21800   1.000 32.22904 ? 32  LEU A CD2 1 
ATOM   243  N N   . VAL A 1 36  ? 7.62900   -8.36100  -4.20300  1.000 26.13617 ? 33  VAL A N   1 
ATOM   244  C CA  . VAL A 1 36  ? 7.76900   -7.34900  -5.24400  1.000 25.17406 ? 33  VAL A CA  1 
ATOM   245  C C   . VAL A 1 36  ? 6.80200   -7.66600  -6.36800  1.000 26.80228 ? 33  VAL A C   1 
ATOM   246  O O   . VAL A 1 36  ? 6.77500   -8.79800  -6.86300  1.000 28.22872 ? 33  VAL A O   1 
ATOM   247  C CB  . VAL A 1 36  ? 9.20400   -7.31500  -5.78400  1.000 24.02319 ? 33  VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 36  ? 9.34600   -6.28100  -6.85400  1.000 27.39700 ? 33  VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 36  ? 10.17700  -7.03200  -4.62900  1.000 22.96714 ? 33  VAL A CG2 1 
ATOM   250  N N   . ASP A 1 37  ? 6.08400   -6.66500  -6.84600  1.000 25.65483 ? 34  ASP A N   1 
ATOM   251  C CA  . ASP A 1 37  ? 5.20400   -6.84000  -7.96200  1.000 29.35809 ? 34  ASP A CA  1 
ATOM   252  C C   . ASP A 1 37  ? 6.07200   -7.12300  -9.17500  1.000 32.64797 ? 34  ASP A C   1 
ATOM   253  O O   . ASP A 1 37  ? 7.07300   -6.50200  -9.35500  1.000 25.49235 ? 34  ASP A O   1 
ATOM   254  C CB  . ASP A 1 37  ? 4.46100   -5.53500  -8.18400  1.000 24.15849 ? 34  ASP A CB  1 
ATOM   255  C CG  . ASP A 1 37  ? 3.32100   -5.66400  -9.15400  1.000 34.84533 ? 34  ASP A CG  1 
ATOM   256  O OD1 . ASP A 1 37  ? 2.32200   -6.24800  -8.77600  1.000 37.90992 ? 34  ASP A OD1 1 
ATOM   257  O OD2 . ASP A 1 37  ? 3.45400   -5.16900  -10.25200 1.000 37.73684 ? 34  ASP A OD2 1 
ATOM   258  N N   . PRO A 1 38  ? 5.62800   -7.97900  -10.10700 1.000 28.08756 ? 35  PRO A N   1 
ATOM   259  C CA  . PRO A 1 38  ? 6.46000   -8.19600  -11.28900 1.000 26.64954 ? 35  PRO A CA  1 
ATOM   260  C C   . PRO A 1 38  ? 6.81800   -6.95900  -12.14400 1.000 25.82256 ? 35  PRO A C   1 
ATOM   261  O O   . PRO A 1 38  ? 7.80200   -6.95800  -12.78500 1.000 27.99872 ? 35  PRO A O   1 
ATOM   262  C CB  . PRO A 1 38  ? 5.61900   -9.18000  -12.11600 1.000 32.05778 ? 35  PRO A CB  1 
ATOM   263  C CG  . PRO A 1 38  ? 4.83300   -9.89000  -11.12900 1.000 33.79215 ? 35  PRO A CG  1 
ATOM   264  C CD  . PRO A 1 38  ? 4.49700   -8.91600  -10.06600 1.000 37.47214 ? 35  PRO A CD  1 
ATOM   265  N N   . ASP A 1 39  ? 5.99600   -5.92900  -12.13500 1.000 28.41848 ? 36  ASP A N   1 
ATOM   266  C CA  . ASP A 1 39  ? 6.23000   -4.74100  -12.87300 1.000 29.56850 ? 36  ASP A CA  1 
ATOM   267  C C   . ASP A 1 39  ? 6.77900   -3.59900  -12.04600 1.000 29.03196 ? 36  ASP A C   1 
ATOM   268  O O   . ASP A 1 39  ? 6.68200   -2.48400  -12.44300 1.000 34.01773 ? 36  ASP A O   1 
ATOM   269  C CB  . ASP A 1 39  ? 4.92500   -4.30200  -13.51300 1.000 37.25096 ? 36  ASP A CB  1 
ATOM   270  C CG  . ASP A 1 39  ? 4.47200   -5.23800  -14.57400 1.000 42.32566 ? 36  ASP A CG  1 
ATOM   271  O OD1 . ASP A 1 39  ? 5.25200   -6.04300  -15.06000 1.000 46.98477 ? 36  ASP A OD1 1 
ATOM   272  O OD2 . ASP A 1 39  ? 3.30300   -5.18700  -14.95600 1.000 53.66958 ? 36  ASP A OD2 1 
ATOM   273  N N   . ALA A 1 40  ? 7.38400   -3.91700  -10.91900 1.000 27.68748 ? 37  ALA A N   1 
ATOM   274  C CA  . ALA A 1 40  ? 7.89600   -2.88100  -10.07200 1.000 26.06026 ? 37  ALA A CA  1 
ATOM   275  C C   . ALA A 1 40  ? 9.10000   -2.16500  -10.65500 1.000 22.79598 ? 37  ALA A C   1 
ATOM   276  O O   . ALA A 1 40  ? 9.80500   -2.71600  -11.43600 1.000 27.21519 ? 37  ALA A O   1 
ATOM   277  C CB  . ALA A 1 40  ? 8.29800   -3.45500  -8.73700  1.000 25.73027 ? 37  ALA A CB  1 
ATOM   278  N N   . SER A 1 41  ? 9.32800   -0.92500  -10.28700 1.000 23.05237 ? 38  SER A N   1 
ATOM   279  C CA  A SER A 1 41  ? 10.63500  -0.25800  -10.84100 0.527 22.88624 ? 38  SER A CA  1 
ATOM   280  C CA  B SER A 1 41  ? 10.63500  -0.23600  -10.83100 0.473 22.90264 ? 38  SER A CA  1 
ATOM   281  C C   . SER A 1 41  ? 11.54200  0.13800   -9.50700  1.000 19.20724 ? 38  SER A C   1 
ATOM   282  O O   . SER A 1 41  ? 11.07700  0.42200   -8.32800  1.000 25.20163 ? 38  SER A O   1 
ATOM   283  C CB  A SER A 1 41  ? 10.30400  0.99000   -11.61200 0.527 27.77132 ? 38  SER A CB  1 
ATOM   284  C CB  B SER A 1 41  ? 10.30500  1.10000   -11.44000 0.473 27.33256 ? 38  SER A CB  1 
ATOM   285  O OG  A SER A 1 41  ? 9.92200   2.00300   -10.74800 0.527 29.86042 ? 38  SER A OG  1 
ATOM   286  O OG  B SER A 1 41  ? 9.44500   0.94500   -12.52700 0.473 31.07424 ? 38  SER A OG  1 
ATOM   287  N N   . PHE A 1 42  ? 12.82600  0.01400   -9.72700  1.000 19.15664 ? 39  PHE A N   1 
ATOM   288  C CA  . PHE A 1 42  ? 13.80000  0.25500   -8.70400  1.000 20.72150 ? 39  PHE A CA  1 
ATOM   289  C C   . PHE A 1 42  ? 14.72500  1.36800   -9.10500  1.000 23.58257 ? 39  PHE A C   1 
ATOM   290  O O   . PHE A 1 42  ? 15.39800  1.23700   -10.07400 1.000 21.76343 ? 39  PHE A O   1 
ATOM   291  C CB  . PHE A 1 42  ? 14.54600  -1.03600  -8.49500  1.000 19.91785 ? 39  PHE A CB  1 
ATOM   292  C CG  . PHE A 1 42  ? 13.68800  -2.07200  -7.90800  1.000 20.47860 ? 39  PHE A CG  1 
ATOM   293  C CD1 . PHE A 1 42  ? 12.89900  -2.90500  -8.65000  1.000 21.42579 ? 39  PHE A CD1 1 
ATOM   294  C CD2 . PHE A 1 42  ? 13.60400  -2.10700  -6.60900  1.000 20.75639 ? 39  PHE A CD2 1 
ATOM   295  C CE1 . PHE A 1 42  ? 12.07800  -3.79900  -8.02200  1.000 24.79860 ? 39  PHE A CE1 1 
ATOM   296  C CE2 . PHE A 1 42  ? 12.81400  -2.97700  -5.95100  1.000 26.84886 ? 39  PHE A CE2 1 
ATOM   297  C CZ  . PHE A 1 42  ? 12.05000  -3.83900  -6.66100  1.000 23.83420 ? 39  PHE A CZ  1 
ATOM   298  N N   . VAL A 1 43  ? 14.78800  2.43100   -8.31500  1.000 21.36949 ? 40  VAL A N   1 
ATOM   299  C CA  . VAL A 1 43  ? 15.56800  3.54600   -8.69500  1.000 23.59223 ? 40  VAL A CA  1 
ATOM   300  C C   . VAL A 1 43  ? 16.75600  3.79400   -7.76300  1.000 22.20344 ? 40  VAL A C   1 
ATOM   301  O O   . VAL A 1 43  ? 16.58200  3.77100   -6.58900  1.000 23.77185 ? 40  VAL A O   1 
ATOM   302  C CB  . VAL A 1 43  ? 14.68900  4.81200   -8.66100  1.000 21.27211 ? 40  VAL A CB  1 
ATOM   303  C CG1 . VAL A 1 43  ? 15.46700  6.04300   -9.06200  1.000 23.69351 ? 40  VAL A CG1 1 
ATOM   304  C CG2 . VAL A 1 43  ? 13.48200  4.62700   -9.53900  1.000 22.81776 ? 40  VAL A CG2 1 
ATOM   305  N N   . ASP A 1 44  ? 17.93400  3.99400   -8.33400  1.000 21.48227 ? 41  ASP A N   1 
ATOM   306  C CA  . ASP A 1 44  ? 19.13900  4.43100   -7.62500  1.000 18.53253 ? 41  ASP A CA  1 
ATOM   307  C C   . ASP A 1 44  ? 19.12800  5.93900   -7.74100  1.000 20.99365 ? 41  ASP A C   1 
ATOM   308  O O   . ASP A 1 44  ? 19.43900  6.47700   -8.80000  1.000 23.75209 ? 41  ASP A O   1 
ATOM   309  C CB  . ASP A 1 44  ? 20.39100  3.85300   -8.27100  1.000 20.93263 ? 41  ASP A CB  1 
ATOM   310  C CG  . ASP A 1 44  ? 21.65800  4.12700   -7.49100  1.000 27.12582 ? 41  ASP A CG  1 
ATOM   311  O OD1 . ASP A 1 44  ? 21.74600  5.21400   -6.88900  1.000 32.35069 ? 41  ASP A OD1 1 
ATOM   312  O OD2 . ASP A 1 44  ? 22.58100  3.26000   -7.56000  1.000 31.31432 ? 41  ASP A OD2 1 
ATOM   313  N N   . ALA A 1 45  ? 18.73100  6.64100   -6.66500  1.000 22.92861 ? 42  ALA A N   1 
ATOM   314  C CA  . ALA A 1 45  ? 18.50000  8.08000   -6.81200  1.000 27.44019 ? 42  ALA A CA  1 
ATOM   315  C C   . ALA A 1 45  ? 19.78300  8.81600   -7.17400  1.000 26.56026 ? 42  ALA A C   1 
ATOM   316  O O   . ALA A 1 45  ? 19.75600  9.77000   -7.97500  1.000 27.82088 ? 42  ALA A O   1 
ATOM   317  C CB  . ALA A 1 45  ? 17.90900  8.62700   -5.51100  1.000 29.16289 ? 42  ALA A CB  1 
ATOM   318  N N   . ARG A 1 46  ? 20.91100  8.39900   -6.60900  1.000 24.46111 ? 43  ARG A N   1 
ATOM   319  C CA  . ARG A 1 46  ? 22.14600  9.14800   -6.77300  1.000 25.86514 ? 43  ARG A CA  1 
ATOM   320  C C   . ARG A 1 46  ? 22.71700  9.01200   -8.17900  1.000 31.78936 ? 43  ARG A C   1 
ATOM   321  O O   . ARG A 1 46  ? 23.31900  9.96900   -8.69400  1.000 34.25966 ? 43  ARG A O   1 
ATOM   322  C CB  . ARG A 1 46  ? 23.14700  8.69900   -5.71900  1.000 32.08316 ? 43  ARG A CB  1 
ATOM   323  C CG  . ARG A 1 46  ? 24.32900  9.57900   -5.62000  1.000 30.87986 ? 43  ARG A CG  1 
ATOM   324  C CD  . ARG A 1 46  ? 24.84300  9.71400   -4.16700  1.000 27.60776 ? 43  ARG A CD  1 
ATOM   325  N NE  . ARG A 1 46  ? 24.02100  10.55600  -3.31300  1.000 25.90355 ? 43  ARG A NE  1 
ATOM   326  C CZ  . ARG A 1 46  ? 23.96800  11.89000  -3.38000  1.000 21.10531 ? 43  ARG A CZ  1 
ATOM   327  N NH1 . ARG A 1 46  ? 24.64500  12.55500  -4.28200  1.000 25.63851 ? 43  ARG A NH1 1 
ATOM   328  N NH2 . ARG A 1 46  ? 23.22100  12.54200  -2.50100  1.000 23.33241 ? 43  ARG A NH2 1 
ATOM   329  N N   . THR A 1 47  ? 22.48900  7.87200   -8.83900  1.000 26.24845 ? 44  THR A N   1 
ATOM   330  C CA  . THR A 1 47  ? 22.97300  7.66200   -10.19800 1.000 25.21762 ? 44  THR A CA  1 
ATOM   331  C C   . THR A 1 47  ? 21.89100  7.89100   -11.25100 1.000 23.62727 ? 44  THR A C   1 
ATOM   332  O O   . THR A 1 47  ? 22.22100  7.90100   -12.45400 1.000 27.27154 ? 44  THR A O   1 
ATOM   333  C CB  . THR A 1 47  ? 23.50800  6.23600   -10.37800 1.000 27.19326 ? 44  THR A CB  1 
ATOM   334  O OG1 . THR A 1 47  ? 22.43000  5.30400   -10.15400 1.000 25.48168 ? 44  THR A OG1 1 
ATOM   335  C CG2 . THR A 1 47  ? 24.63500  5.94600   -9.41000  1.000 27.52419 ? 44  THR A CG2 1 
ATOM   336  N N   . ASN A 1 48  ? 20.62500  8.05100   -10.84400 1.000 20.22722 ? 45  ASN A N   1 
ATOM   337  C CA  . ASN A 1 48  ? 19.46100  8.18300   -11.71100 1.000 24.00741 ? 45  ASN A CA  1 
ATOM   338  C C   . ASN A 1 48  ? 19.18600  6.90800   -12.50300 1.000 25.88686 ? 45  ASN A C   1 
ATOM   339  O O   . ASN A 1 48  ? 18.41200  6.91700   -13.47600 1.000 22.53133 ? 45  ASN A O   1 
ATOM   340  C CB  . ASN A 1 48  ? 19.59600  9.37300   -12.67200 1.000 25.10481 ? 45  ASN A CB  1 
ATOM   341  C CG  . ASN A 1 48  ? 19.63200  10.69400  -11.94200 1.000 32.64574 ? 45  ASN A CG  1 
ATOM   342  O OD1 . ASN A 1 48  ? 18.60700  11.19000  -11.49300 1.000 35.88712 ? 45  ASN A OD1 1 
ATOM   343  N ND2 . ASN A 1 48  ? 20.81200  11.25700  -11.81300 1.000 35.68210 ? 45  ASN A ND2 1 
ATOM   344  N N   . GLN A 1 49  ? 19.77700  5.81000   -12.07800 1.000 21.47718 ? 46  GLN A N   1 
ATOM   345  C CA  . GLN A 1 49  ? 19.56100  4.52300   -12.74300 1.000 21.46719 ? 46  GLN A CA  1 
ATOM   346  C C   . GLN A 1 49  ? 18.25600  3.88000   -12.30900 1.000 22.20974 ? 46  GLN A C   1 
ATOM   347  O O   . GLN A 1 49  ? 17.90700  3.87000   -11.12600 1.000 23.79594 ? 46  GLN A O   1 
ATOM   348  C CB  . GLN A 1 49  ? 20.73300  3.59600   -12.46000 1.000 22.77726 ? 46  GLN A CB  1 
ATOM   349  C CG  . GLN A 1 49  ? 21.92400  3.96500   -13.30200 1.000 26.26171 ? 46  GLN A CG  1 
ATOM   350  C CD  . GLN A 1 49  ? 23.18300  3.30400   -12.87200 1.000 28.82096 ? 46  GLN A CD  1 
ATOM   351  O OE1 . GLN A 1 49  ? 23.53400  3.31100   -11.67800 1.000 24.39950 ? 46  GLN A OE1 1 
ATOM   352  N NE2 . GLN A 1 49  ? 23.92600  2.78100   -13.83600 1.000 24.72967 ? 46  GLN A NE2 1 
ATOM   353  N N   . VAL A 1 50  ? 17.55500  3.27700   -13.27700 1.000 20.35112 ? 47  VAL A N   1 
ATOM   354  C CA  . VAL A 1 50  ? 16.27000  2.63600   -13.05600 1.000 21.85866 ? 47  VAL A CA  1 
ATOM   355  C C   . VAL A 1 50  ? 16.35300  1.19500   -13.53800 1.000 20.13300 ? 47  VAL A C   1 
ATOM   356  O O   . VAL A 1 50  ? 16.86200  0.93700   -14.63700 1.000 24.53719 ? 47  VAL A O   1 
ATOM   357  C CB  . VAL A 1 50  ? 15.15100  3.37900   -13.80200 1.000 22.72272 ? 47  VAL A CB  1 
ATOM   358  C CG1 . VAL A 1 50  ? 13.81000  2.74800   -13.51700 1.000 26.02891 ? 47  VAL A CG1 1 
ATOM   359  C CG2 . VAL A 1 50  ? 15.22200  4.85700   -13.45000 1.000 23.07601 ? 47  VAL A CG2 1 
ATOM   360  N N   . TYR A 1 51  ? 15.87600  0.26900   -12.70600 1.000 19.59304 ? 48  TYR A N   1 
ATOM   361  C CA  . TYR A 1 51  ? 15.91700  -1.17000  -12.96100 1.000 20.60020 ? 48  TYR A CA  1 
ATOM   362  C C   . TYR A 1 51  ? 14.54500  -1.81500  -12.81700 1.000 17.81134 ? 48  TYR A C   1 
ATOM   363  O O   . TYR A 1 51  ? 13.69400  -1.37600  -12.04300 1.000 20.02653 ? 48  TYR A O   1 
ATOM   364  C CB  . TYR A 1 51  ? 16.90200  -1.80400  -11.97500 1.000 19.05128 ? 48  TYR A CB  1 
ATOM   365  C CG  . TYR A 1 51  ? 18.26600  -1.21500  -12.09000 1.000 23.44740 ? 48  TYR A CG  1 
ATOM   366  C CD1 . TYR A 1 51  ? 19.09500  -1.51900  -13.15300 1.000 23.67022 ? 48  TYR A CD1 1 
ATOM   367  C CD2 . TYR A 1 51  ? 18.74900  -0.34500  -11.11700 1.000 27.53665 ? 48  TYR A CD2 1 
ATOM   368  C CE1 . TYR A 1 51  ? 20.34800  -0.98500  -13.27100 1.000 23.45371 ? 48  TYR A CE1 1 
ATOM   369  C CE2 . TYR A 1 51  ? 20.01900  0.20300   -11.23000 1.000 29.37045 ? 48  TYR A CE2 1 
ATOM   370  C CZ  . TYR A 1 51  ? 20.80600  -0.11400  -12.30200 1.000 25.75834 ? 48  TYR A CZ  1 
ATOM   371  O OH  . TYR A 1 51  ? 22.07200  0.39500   -12.44200 1.000 27.00726 ? 48  TYR A OH  1 
ATOM   372  N N   . ASP A 1 52  ? 14.31300  -2.87700  -13.60500 1.000 21.47242 ? 49  ASP A N   1 
ATOM   373  C CA  . ASP A 1 52  ? 13.11900  -3.68200  -13.37800 1.000 18.77053 ? 49  ASP A CA  1 
ATOM   374  C C   . ASP A 1 52  ? 13.41000  -4.73100  -12.29600 1.000 21.11884 ? 49  ASP A C   1 
ATOM   375  O O   . ASP A 1 52  ? 14.51300  -4.76100  -11.71900 1.000 21.02548 ? 49  ASP A O   1 
ATOM   376  C CB  . ASP A 1 52  ? 12.63200  -4.32300  -14.68900 1.000 22.70887 ? 49  ASP A CB  1 
ATOM   377  C CG  . ASP A 1 52  ? 13.60000  -5.34400  -15.27500 1.000 29.61056 ? 49  ASP A CG  1 
ATOM   378  O OD1 . ASP A 1 52  ? 14.47200  -5.90000  -14.56000 1.000 25.46898 ? 49  ASP A OD1 1 
ATOM   379  O OD2 . ASP A 1 52  ? 13.44100  -5.65300  -16.49600 1.000 30.80858 ? 49  ASP A OD2 1 
ATOM   380  N N   . LYS A 1 53  ? 12.40600  -5.57200  -11.97800 1.000 23.05042 ? 50  LYS A N   1 
ATOM   381  C CA  . LYS A 1 53  ? 12.53000  -6.47800  -10.83800 1.000 22.69078 ? 50  LYS A CA  1 
ATOM   382  C C   . LYS A 1 53  ? 13.67400  -7.46900  -11.05000 1.000 23.40887 ? 50  LYS A C   1 
ATOM   383  O O   . LYS A 1 53  ? 14.47700  -7.71100  -10.13900 1.000 22.92166 ? 50  LYS A O   1 
ATOM   384  C CB  . LYS A 1 53  ? 11.21000  -7.21600  -10.57400 1.000 23.26333 ? 50  LYS A CB  1 
ATOM   385  C CG  . LYS A 1 53  ? 11.27800  -8.25800  -9.45600  1.000 23.77260 ? 50  LYS A CG  1 
ATOM   386  C CD  . LYS A 1 53  ? 9.91900   -8.91800  -9.30100  1.000 23.74042 ? 50  LYS A CD  1 
ATOM   387  C CE  . LYS A 1 53  ? 9.96600   -10.09800 -8.36300  1.000 24.98721 ? 50  LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 53  ? 8.55800   -10.63100 -8.13700  1.000 24.32104 ? 50  LYS A NZ  1 
ATOM   389  N N   . ASP A 1 54  ? 13.75300  -8.09100  -12.23700 1.000 22.87929 ? 51  ASP A N   1 
ATOM   390  C CA  . ASP A 1 54  ? 14.80000  -9.08000  -12.45100 1.000 26.66599 ? 51  ASP A CA  1 
ATOM   391  C C   . ASP A 1 54  ? 16.18700  -8.46100  -12.36700 1.000 22.55298 ? 51  ASP A C   1 
ATOM   392  O O   . ASP A 1 54  ? 17.11400  -9.09500  -11.86200 1.000 24.87393 ? 51  ASP A O   1 
ATOM   393  C CB  . ASP A 1 54  ? 14.61600  -9.78300  -13.79100 1.000 28.45901 ? 51  ASP A CB  1 
ATOM   394  C CG  . ASP A 1 54  ? 13.41500  -10.70400 -13.79200 1.000 39.19377 ? 51  ASP A CG  1 
ATOM   395  O OD1 . ASP A 1 54  ? 12.78800  -10.90000 -12.71600 1.000 36.77615 ? 51  ASP A OD1 1 
ATOM   396  O OD2 . ASP A 1 54  ? 13.10300  -11.22600 -14.87600 1.000 42.44999 ? 51  ASP A OD2 1 
ATOM   397  N N   . GLN A 1 55  ? 16.35600  -7.22000  -12.85300 1.000 21.89342 ? 52  GLN A N   1 
ATOM   398  C CA  . GLN A 1 55  ? 17.66100  -6.55900  -12.82000 1.000 21.70054 ? 52  GLN A CA  1 
ATOM   399  C C   . GLN A 1 55  ? 18.02900  -6.20200  -11.39500 1.000 22.06839 ? 52  GLN A C   1 
ATOM   400  O O   . GLN A 1 55  ? 19.18900  -6.34400  -10.97400 1.000 20.72668 ? 52  GLN A O   1 
ATOM   401  C CB  . GLN A 1 55  ? 17.62300  -5.28800  -13.67400 1.000 22.38230 ? 52  GLN A CB  1 
ATOM   402  C CG  . GLN A 1 55  ? 17.52800  -5.54800  -15.14800 1.000 26.37296 ? 52  GLN A CG  1 
ATOM   403  C CD  . GLN A 1 55  ? 17.14300  -4.30100  -15.93500 1.000 28.73965 ? 52  GLN A CD  1 
ATOM   404  O OE1 . GLN A 1 55  ? 16.54200  -3.33500  -15.41200 1.000 27.09462 ? 52  GLN A OE1 1 
ATOM   405  N NE2 . GLN A 1 55  ? 17.49200  -4.31000  -17.22400 1.000 35.38184 ? 52  GLN A NE2 1 
ATOM   406  N N   . PHE A 1 56  ? 17.02200  -5.74000  -10.64300 1.000 19.75740 ? 53  PHE A N   1 
ATOM   407  C CA  . PHE A 1 56  ? 17.22100  -5.40900  -9.23900  1.000 21.38977 ? 53  PHE A CA  1 
ATOM   408  C C   . PHE A 1 56  ? 17.63700  -6.63900  -8.45400  1.000 19.82658 ? 53  PHE A C   1 
ATOM   409  O O   . PHE A 1 56  ? 18.61900  -6.61000  -7.69900  1.000 20.82532 ? 53  PHE A O   1 
ATOM   410  C CB  . PHE A 1 56  ? 15.94100  -4.82600  -8.65800  1.000 20.00014 ? 53  PHE A CB  1 
ATOM   411  C CG  . PHE A 1 56  ? 16.02000  -4.54900  -7.15700  1.000 19.90201 ? 53  PHE A CG  1 
ATOM   412  C CD1 . PHE A 1 56  ? 16.75800  -3.47000  -6.66700  1.000 22.74684 ? 53  PHE A CD1 1 
ATOM   413  C CD2 . PHE A 1 56  ? 15.32200  -5.34400  -6.26500  1.000 23.88343 ? 53  PHE A CD2 1 
ATOM   414  C CE1 . PHE A 1 56  ? 16.82900  -3.24500  -5.29200  1.000 25.04097 ? 53  PHE A CE1 1 
ATOM   415  C CE2 . PHE A 1 56  ? 15.37000  -5.09900  -4.89900  1.000 27.49128 ? 53  PHE A CE2 1 
ATOM   416  C CZ  . PHE A 1 56  ? 16.09600  -4.02600  -4.41900  1.000 23.97271 ? 53  PHE A CZ  1 
ATOM   417  N N   . LEU A 1 57  ? 16.93800  -7.74100  -8.64100  1.000 21.53187 ? 54  LEU A N   1 
ATOM   418  C CA  . LEU A 1 57  ? 17.24700  -8.96700  -7.92000  1.000 20.34884 ? 54  LEU A CA  1 
ATOM   419  C C   . LEU A 1 57  ? 18.60000  -9.53300  -8.29700  1.000 23.10270 ? 54  LEU A C   1 
ATOM   420  O O   . LEU A 1 57  ? 19.24200  -10.15000 -7.52300  1.000 23.74603 ? 54  LEU A O   1 
ATOM   421  C CB  . LEU A 1 57  ? 16.15400  -10.00600 -8.11500  1.000 21.43538 ? 54  LEU A CB  1 
ATOM   422  C CG  . LEU A 1 57  ? 14.86700  -9.67200  -7.37500  1.000 24.29324 ? 54  LEU A CG  1 
ATOM   423  C CD1 . LEU A 1 57  ? 13.78200  -10.68600 -7.63400  1.000 31.91922 ? 54  LEU A CD1 1 
ATOM   424  C CD2 . LEU A 1 57  ? 15.04300  -9.50800  -5.90300  1.000 26.06728 ? 54  LEU A CD2 1 
ATOM   425  N N   . GLN A 1 58  ? 19.02500  -9.28500  -9.50800  1.000 23.02819 ? 55  GLN A N   1 
ATOM   426  C CA  . GLN A 1 58  ? 20.31900  -9.72100  -9.93000  1.000 25.03965 ? 55  GLN A CA  1 
ATOM   427  C C   . GLN A 1 58  ? 21.38700  -8.98400  -9.13800  1.000 24.85351 ? 55  GLN A C   1 
ATOM   428  O O   . GLN A 1 58  ? 22.36700  -9.54500  -8.75000  1.000 23.95310 ? 55  GLN A O   1 
ATOM   429  C CB  . GLN A 1 58  ? 20.47700  -9.40500  -11.39200 1.000 29.04093 ? 55  GLN A CB  1 
ATOM   430  C CG  . GLN A 1 58  ? 21.68700  -9.99300  -12.00800 1.000 33.81857 ? 55  GLN A CG  1 
ATOM   431  C CD  . GLN A 1 58  ? 21.48400  -11.45800 -12.21900 1.000 47.60197 ? 55  GLN A CD  1 
ATOM   432  O OE1 . GLN A 1 58  ? 22.05300  -12.26700 -11.51300 1.000 42.42292 ? 55  GLN A OE1 1 
ATOM   433  N NE2 . GLN A 1 58  ? 20.61800  -11.80400 -13.14700 1.000 49.64428 ? 55  GLN A NE2 1 
ATOM   434  N N   . MET A 1 59  ? 21.17700  -7.68600  -8.96900  1.000 23.30082 ? 56  MET A N   1 
ATOM   435  C CA  . MET A 1 59  ? 22.08300  -6.85900  -8.20400  1.000 24.41371 ? 56  MET A CA  1 
ATOM   436  C C   . MET A 1 59  ? 22.05800  -7.26500  -6.76000  1.000 22.34523 ? 56  MET A C   1 
ATOM   437  O O   . MET A 1 59  ? 23.04700  -7.26100  -6.14500  1.000 20.29277 ? 56  MET A O   1 
ATOM   438  C CB  . MET A 1 59  ? 21.76600  -5.39300  -8.37600  1.000 25.83049 ? 56  MET A CB  1 
ATOM   439  C CG  . MET A 1 59  ? 22.12900  -4.91600  -9.74900  1.000 27.71282 ? 56  MET A CG  1 
ATOM   440  S SD  . MET A 1 59  ? 21.90800  -3.16000  -9.96700  1.000 37.80155 ? 56  MET A SD  1 
ATOM   441  C CE  . MET A 1 59  ? 22.66700  -2.62200  -8.48600  1.000 30.24147 ? 56  MET A CE  1 
ATOM   442  N N   . ILE A 1 60  ? 20.89000  -7.56700  -6.24000  1.000 20.39854 ? 57  ILE A N   1 
ATOM   443  C CA  . ILE A 1 60  ? 20.81900  -8.09200  -4.87200  1.000 19.87333 ? 57  ILE A CA  1 
ATOM   444  C C   . ILE A 1 60  ? 21.63300  -9.36600  -4.75100  1.000 22.07527 ? 57  ILE A C   1 
ATOM   445  O O   . ILE A 1 60  ? 22.38000  -9.54600  -3.79600  1.000 21.66811 ? 57  ILE A O   1 
ATOM   446  C CB  . ILE A 1 60  ? 19.36000  -8.31500  -4.45900  1.000 23.30996 ? 57  ILE A CB  1 
ATOM   447  C CG1 . ILE A 1 60  ? 18.64900  -6.97100  -4.33400  1.000 21.61194 ? 57  ILE A CG1 1 
ATOM   448  C CG2 . ILE A 1 60  ? 19.25200  -9.15000  -3.15000  1.000 25.06856 ? 57  ILE A CG2 1 
ATOM   449  C CD1 . ILE A 1 60  ? 19.23100  -6.02800  -3.25700  1.000 24.80743 ? 57  ILE A CD1 1 
ATOM   450  N N   . LYS A 1 61  ? 21.49700  -10.26800 -5.69200  1.000 20.62739 ? 58  LYS A N   1 
ATOM   451  C CA  . LYS A 1 61  ? 22.25600  -11.51100 -5.63700  1.000 22.27628 ? 58  LYS A CA  1 
ATOM   452  C C   . LYS A 1 61  ? 23.76700  -11.27100 -5.53500  1.000 25.21950 ? 58  LYS A C   1 
ATOM   453  O O   . LYS A 1 61  ? 24.40700  -11.85600 -4.70400  1.000 20.84307 ? 58  LYS A O   1 
ATOM   454  C CB  . LYS A 1 61  ? 21.94500  -12.35700 -6.85800  1.000 21.46435 ? 58  LYS A CB  1 
ATOM   455  C CG  . LYS A 1 61  ? 22.63900  -13.70500 -6.92200  1.000 27.45946 ? 58  LYS A CG  1 
ATOM   456  C CD  . LYS A 1 61  ? 22.33900  -14.38000 -8.23300  1.000 29.10345 ? 58  LYS A CD  1 
ATOM   457  C CE  . LYS A 1 61  ? 23.50000  -15.17300 -8.75100  1.000 38.49710 ? 58  LYS A CE  1 
ATOM   458  N NZ  . LYS A 1 61  ? 23.11000  -15.99900 -9.88900  1.000 43.46444 ? 58  LYS A NZ  1 
ATOM   459  N N   . GLU A 1 62  ? 24.28000  -10.36200 -6.36300  1.000 21.07612 ? 59  GLU A N   1 
ATOM   460  C CA  . GLU A 1 62  ? 25.69000  -10.00700 -6.33800  1.000 21.15784 ? 59  GLU A CA  1 
ATOM   461  C C   . GLU A 1 62  ? 26.08300  -9.42300  -5.00200  1.000 25.24920 ? 59  GLU A C   1 
ATOM   462  O O   . GLU A 1 62  ? 27.17700  -9.69800  -4.50500  1.000 23.85211 ? 59  GLU A O   1 
ATOM   463  C CB  . GLU A 1 62  ? 26.03800  -9.01900  -7.45900  1.000 25.36638 ? 59  GLU A CB  1 
ATOM   464  C CG  . GLU A 1 62  ? 25.76600  -9.55400  -8.85900  1.000 29.16639 ? 59  GLU A CG  1 
ATOM   465  C CD  . GLU A 1 62  ? 25.58000  -8.47400  -9.91400  1.000 41.18823 ? 59  GLU A CD  1 
ATOM   466  O OE1 . GLU A 1 62  ? 25.41000  -7.28300  -9.55700  1.000 51.32811 ? 59  GLU A OE1 1 
ATOM   467  O OE2 . GLU A 1 62  ? 25.58000  -8.82600  -11.11300 1.000 42.95803 ? 59  GLU A OE2 1 
ATOM   468  N N   . ALA A 1 63  ? 25.21600  -8.56800  -4.41200  1.000 19.39145 ? 60  ALA A N   1 
ATOM   469  C CA  . ALA A 1 63  ? 25.53400  -7.98500  -3.12100  1.000 22.89582 ? 60  ALA A CA  1 
ATOM   470  C C   . ALA A 1 63  ? 25.53100  -9.02700  -2.02200  1.000 24.23355 ? 60  ALA A C   1 
ATOM   471  O O   . ALA A 1 63  ? 26.35200  -8.97400  -1.09300  1.000 23.43502 ? 60  ALA A O   1 
ATOM   472  C CB  . ALA A 1 63  ? 24.52700  -6.88700  -2.78000  1.000 21.97172 ? 60  ALA A CB  1 
ATOM   473  N N   . LEU A 1 64  ? 24.59100  -9.97400  -2.09200  1.000 20.18271 ? 61  LEU A N   1 
ATOM   474  C CA  . LEU A 1 64  ? 24.56800  -11.04100 -1.09600  1.000 21.09829 ? 61  LEU A CA  1 
ATOM   475  C C   . LEU A 1 64  ? 25.81600  -11.91500 -1.19000  1.000 23.94187 ? 61  LEU A C   1 
ATOM   476  O O   . LEU A 1 64  ? 26.30100  -12.39600 -0.14800  1.000 26.87874 ? 61  LEU A O   1 
ATOM   477  C CB  . LEU A 1 64  ? 23.30400  -11.87500 -1.26800  1.000 20.51629 ? 61  LEU A CB  1 
ATOM   478  C CG  . LEU A 1 64  ? 22.01900  -11.16300 -0.84500  1.000 22.49676 ? 61  LEU A CG  1 
ATOM   479  C CD1 . LEU A 1 64  ? 20.84500  -12.02900 -1.20600  1.000 23.80938 ? 61  LEU A CD1 1 
ATOM   480  C CD2 . LEU A 1 64  ? 21.96300  -10.83900 0.63500   1.000 22.04240 ? 61  LEU A CD2 1 
ATOM   481  N N   . GLU A 1 65  ? 26.36100  -12.08400 -2.39600  1.000 21.91554 ? 62  GLU A N   1 
ATOM   482  C CA  . GLU A 1 65  ? 27.62500  -12.81100 -2.56600  1.000 27.48136 ? 62  GLU A CA  1 
ATOM   483  C C   . GLU A 1 65  ? 28.78800  -12.07000 -1.92700  1.000 27.89375 ? 62  GLU A C   1 
ATOM   484  O O   . GLU A 1 65  ? 29.82700  -12.69300 -1.64900  1.000 28.85548 ? 62  GLU A O   1 
ATOM   485  C CB  . GLU A 1 65  ? 27.95200  -13.03400 -4.03500  1.000 24.19884 ? 62  GLU A CB  1 
ATOM   486  C CG  . GLU A 1 65  ? 27.01200  -13.98700 -4.74700  1.000 26.22717 ? 62  GLU A CG  1 
ATOM   487  C CD  . GLU A 1 65  ? 27.28900  -14.12000 -6.23900  1.000 29.55631 ? 62  GLU A CD  1 
ATOM   488  O OE1 . GLU A 1 65  ? 28.34900  -13.70900 -6.72000  1.000 32.15797 ? 62  GLU A OE1 1 
ATOM   489  O OE2 . GLU A 1 65  ? 26.42800  -14.70000 -6.93800  1.000 35.99253 ? 62  GLU A OE2 1 
ATOM   490  N N   . GLN A 1 66  ? 28.65200  -10.75100 -1.72900  1.000 24.62125 ? 63  GLN A N   1 
ATOM   491  C CA  . GLN A 1 66  ? 29.62700  -9.93100  -1.02600  1.000 27.84917 ? 63  GLN A CA  1 
ATOM   492  C C   . GLN A 1 66  ? 29.26900  -9.73200  0.44800   1.000 29.95512 ? 63  GLN A C   1 
ATOM   493  O O   . GLN A 1 66  ? 29.66300  -8.73400  1.05800   1.000 27.13563 ? 63  GLN A O   1 
ATOM   494  C CB  . GLN A 1 66  ? 29.76500  -8.57900  -1.73800  1.000 27.77130 ? 63  GLN A CB  1 
ATOM   495  C CG  . GLN A 1 66  ? 30.21500  -8.73000  -3.18600  1.000 31.12132 ? 63  GLN A CG  1 
ATOM   496  C CD  . GLN A 1 66  ? 30.40000  -7.40100  -3.90200  1.000 48.62752 ? 63  GLN A CD  1 
ATOM   497  O OE1 . GLN A 1 66  ? 30.30100  -6.33200  -3.29600  1.000 52.96645 ? 63  GLN A OE1 1 
ATOM   498  N NE2 . GLN A 1 66  ? 30.67000  -7.46600  -5.20100  1.000 46.96448 ? 63  GLN A NE2 1 
ATOM   499  N N   . ASP A 1 67  ? 28.53400  -10.65500 1.01400   1.000 23.35828 ? 64  ASP A N   1 
ATOM   500  C CA  . ASP A 1 67  ? 28.15100  -10.61900 2.39900   1.000 22.71275 ? 64  ASP A CA  1 
ATOM   501  C C   . ASP A 1 67  ? 27.35300  -9.39300  2.83500   1.000 23.15616 ? 64  ASP A C   1 
ATOM   502  O O   . ASP A 1 67  ? 27.49900  -8.92000  3.90800   1.000 23.87818 ? 64  ASP A O   1 
ATOM   503  C CB  . ASP A 1 67  ? 29.33900  -10.92600 3.33800   1.000 28.36486 ? 64  ASP A CB  1 
ATOM   504  C CG  . ASP A 1 67  ? 28.91900  -11.47700 4.65400   1.000 33.60483 ? 64  ASP A CG  1 
ATOM   505  O OD1 . ASP A 1 67  ? 28.04800  -12.29200 4.71000   1.000 29.06646 ? 64  ASP A OD1 1 
ATOM   506  O OD2 . ASP A 1 67  ? 29.48400  -11.06400 5.64800   1.000 37.92159 ? 64  ASP A OD2 1 
ATOM   507  N N   . LEU A 1 68  ? 26.46200  -8.92400  1.98100   1.000 22.32625 ? 65  LEU A N   1 
ATOM   508  C CA  . LEU A 1 68  ? 25.62000  -7.82100  2.36600   1.000 24.36524 ? 65  LEU A CA  1 
ATOM   509  C C   . LEU A 1 68  ? 24.81600  -8.10500  3.61200   1.000 23.27583 ? 65  LEU A C   1 
ATOM   510  O O   . LEU A 1 68  ? 24.18300  -9.09500  3.70300   1.000 24.64180 ? 65  LEU A O   1 
ATOM   511  C CB  . LEU A 1 68  ? 24.65300  -7.47400  1.23200   1.000 20.53424 ? 65  LEU A CB  1 
ATOM   512  C CG  . LEU A 1 68  ? 23.55100  -6.47400  1.54000   1.000 21.21815 ? 65  LEU A CG  1 
ATOM   513  C CD1 . LEU A 1 68  ? 24.16800  -5.10200  1.62600   1.000 23.17488 ? 65  LEU A CD1 1 
ATOM   514  C CD2 . LEU A 1 68  ? 22.45900  -6.51100  0.49200   1.000 22.09370 ? 65  LEU A CD2 1 
ATOM   515  N N   . LYS A 1 69  ? 24.89000  -7.21800  4.58000   1.000 20.80490 ? 66  LYS A N   1 
ATOM   516  C CA  . LYS A 1 69  ? 24.08600  -7.29100  5.78600   1.000 23.27319 ? 66  LYS A CA  1 
ATOM   517  C C   . LYS A 1 69  ? 23.45200  -5.92700  6.03500   1.000 23.20275 ? 66  LYS A C   1 
ATOM   518  O O   . LYS A 1 69  ? 23.99300  -4.92900  5.67700   1.000 23.76943 ? 66  LYS A O   1 
ATOM   519  C CB  . LYS A 1 69  ? 24.86900  -7.77800  7.00200   1.000 27.57446 ? 66  LYS A CB  1 
ATOM   520  C CG  . LYS A 1 69  ? 25.19400  -9.27100  6.96100   1.000 30.52668 ? 66  LYS A CG  1 
ATOM   521  C CD  . LYS A 1 69  ? 26.23100  -9.72700  7.97400   1.000 36.00812 ? 66  LYS A CD  1 
ATOM   522  C CE  . LYS A 1 69  ? 26.79300  -11.11300 7.62000   1.000 34.10464 ? 66  LYS A CE  1 
ATOM   523  N NZ  . LYS A 1 69  ? 27.84400  -11.65100 8.53100   1.000 38.11567 ? 66  LYS A NZ  1 
ATOM   524  N N   . VAL A 1 70  ? 22.28600  -5.92400  6.63700   1.000 21.43695 ? 67  VAL A N   1 
ATOM   525  C CA  . VAL A 1 70  ? 21.56500  -4.70000  6.86100   1.000 20.97862 ? 67  VAL A CA  1 
ATOM   526  C C   . VAL A 1 70  ? 20.91200  -4.60300  8.25500   1.000 27.28398 ? 67  VAL A C   1 
ATOM   527  O O   . VAL A 1 70  ? 20.62900  -5.58800  8.85700   1.000 29.62932 ? 67  VAL A O   1 
ATOM   528  C CB  . VAL A 1 70  ? 20.43200  -4.55600  5.82700   1.000 23.44032 ? 67  VAL A CB  1 
ATOM   529  C CG1 . VAL A 1 70  ? 20.93400  -4.37600  4.39600   1.000 23.35904 ? 67  VAL A CG1 1 
ATOM   530  C CG2 . VAL A 1 70  ? 19.49700  -5.74300  5.92700   1.000 25.03079 ? 67  VAL A CG2 1 
ATOM   531  N N   . GLU A 1 71  ? 20.69300  -3.39200  8.74500   1.000 23.58301 ? 68  GLU A N   1 
ATOM   532  C CA  . GLU A 1 71  ? 19.99100  -3.21500  9.96300   1.000 26.68598 ? 68  GLU A CA  1 
ATOM   533  C C   . GLU A 1 71  ? 19.06600  -2.00500  9.78000   1.000 27.23587 ? 68  GLU A C   1 
ATOM   534  O O   . GLU A 1 71  ? 19.49200  -0.96500  9.36500   1.000 26.95585 ? 68  GLU A O   1 
ATOM   535  C CB  . GLU A 1 71  ? 20.86800  -3.08400  11.19500  1.000 32.11235 ? 68  GLU A CB  1 
ATOM   536  C CG  . GLU A 1 71  ? 21.87400  -2.03400  11.12100  1.000 40.40820 ? 68  GLU A CG  1 
ATOM   537  C CD  . GLU A 1 71  ? 22.51100  -1.60100  12.44900  1.000 47.22509 ? 68  GLU A CD  1 
ATOM   538  O OE1 . GLU A 1 71  ? 21.82200  -1.36800  13.45900  1.000 43.11019 ? 68  GLU A OE1 1 
ATOM   539  O OE2 . GLU A 1 71  ? 23.74200  -1.47300  12.41900  1.000 45.42612 ? 68  GLU A OE2 1 
ATOM   540  N N   . VAL A 1 72  ? 17.80000  -2.16600  10.06500  1.000 24.99797 ? 69  VAL A N   1 
ATOM   541  C CA  . VAL A 1 72  ? 16.88800  -1.09000  9.90700   1.000 27.31618 ? 69  VAL A CA  1 
ATOM   542  C C   . VAL A 1 72  ? 17.03500  -0.11500  11.09800  1.000 30.59079 ? 69  VAL A C   1 
ATOM   543  O O   . VAL A 1 72  ? 17.05000  -0.53200  12.19000  1.000 29.60277 ? 69  VAL A O   1 
ATOM   544  C CB  . VAL A 1 72  ? 15.47200  -1.61700  9.85700   1.000 28.04009 ? 69  VAL A CB  1 
ATOM   545  C CG1 . VAL A 1 72  ? 14.47900  -0.49200  9.87000   1.000 27.87650 ? 69  VAL A CG1 1 
ATOM   546  C CG2 . VAL A 1 72  ? 15.30100  -2.48000  8.63600   1.000 29.92360 ? 69  VAL A CG2 1 
ATOM   547  N N   . LYS A 1 73  ? 17.17400  1.15700   10.83600  1.000 25.23968 ? 70  LYS A N   1 
ATOM   548  C CA  . LYS A 1 73  ? 17.30100  2.16600   11.85000  1.000 30.03643 ? 70  LYS A CA  1 
ATOM   549  C C   . LYS A 1 73  ? 16.03800  2.91700   12.15200  1.000 37.01277 ? 70  LYS A C   1 
ATOM   550  O O   . LYS A 1 73  ? 15.86300  3.31800   13.28800  1.000 40.98805 ? 70  LYS A O   1 
ATOM   551  C CB  . LYS A 1 73  ? 18.38100  3.15500   11.45200  1.000 30.60163 ? 70  LYS A CB  1 
ATOM   552  C CG  . LYS A 1 73  ? 19.76800  2.56200   11.45000  1.000 31.79247 ? 70  LYS A CG  1 
ATOM   553  C CD  . LYS A 1 73  ? 19.97600  1.55300   12.55600  1.000 41.75881 ? 70  LYS A CD  1 
ATOM   554  C CE  . LYS A 1 73  ? 21.21700  1.82600   13.35900  1.000 46.98338 ? 70  LYS A CE  1 
ATOM   555  N NZ  . LYS A 1 73  ? 21.12500  1.08100   14.63700  1.000 47.07044 ? 70  LYS A NZ  1 
ATOM   556  N N   . SER A 1 74  ? 15.16500  3.13800   11.17500  1.000 26.95397 ? 71  SER A N   1 
ATOM   557  C CA  . SER A 1 74  ? 13.92900  3.87200   11.38500  1.000 31.79350 ? 71  SER A CA  1 
ATOM   558  C C   . SER A 1 74  ? 12.99000  3.57500   10.22200  1.000 33.05140 ? 71  SER A C   1 
ATOM   559  O O   . SER A 1 74  ? 13.43900  3.32000   9.10300   1.000 28.74971 ? 71  SER A O   1 
ATOM   560  C CB  . SER A 1 74  ? 14.17200  5.38000   11.50500  1.000 34.65856 ? 71  SER A CB  1 
ATOM   561  O OG  . SER A 1 74  ? 14.62700  5.96000   10.29100  1.000 32.19754 ? 71  SER A OG  1 
ATOM   562  N N   . ILE A 1 75  ? 11.69500  3.60800   10.51100  1.000 32.20176 ? 72  ILE A N   1 
ATOM   563  C CA  . ILE A 1 75  ? 10.63700  3.36200   9.52900   1.000 31.70840 ? 72  ILE A CA  1 
ATOM   564  C C   . ILE A 1 75  ? 9.54800   4.40900   9.71500   1.000 39.52786 ? 72  ILE A C   1 
ATOM   565  O O   . ILE A 1 75  ? 8.95600   4.50800   10.80000  1.000 40.40333 ? 72  ILE A O   1 
ATOM   566  C CB  . ILE A 1 75  ? 10.04200  1.95800   9.68000   1.000 30.52284 ? 72  ILE A CB  1 
ATOM   567  C CG1 . ILE A 1 75  ? 11.08400  0.90100   9.32300   1.000 31.94994 ? 72  ILE A CG1 1 
ATOM   568  C CG2 . ILE A 1 75  ? 8.75200   1.83400   8.86900   1.000 31.71415 ? 72  ILE A CG2 1 
ATOM   569  C CD1 . ILE A 1 75  ? 10.74000  -0.48500  9.81000   1.000 38.02789 ? 72  ILE A CD1 1 
ATOM   570  N N   . ASP A 1 76  ? 9.25000   5.15800   8.65500   1.000 33.53623 ? 73  ASP A N   1 
ATOM   571  C CA  . ASP A 1 76  ? 8.27600   6.24300   8.71300   1.000 32.58991 ? 73  ASP A CA  1 
ATOM   572  C C   . ASP A 1 76  ? 7.25300   6.06100   7.60200   1.000 37.98915 ? 73  ASP A C   1 
ATOM   573  O O   . ASP A 1 76  ? 7.58300   6.16700   6.41600   1.000 34.42211 ? 73  ASP A O   1 
ATOM   574  C CB  . ASP A 1 76  ? 8.98000   7.59300   8.60800   1.000 41.01594 ? 73  ASP A CB  1 
ATOM   575  C CG  . ASP A 1 76  ? 8.07300   8.69800   8.11100   1.000 48.54014 ? 73  ASP A CG  1 
ATOM   576  O OD1 . ASP A 1 76  ? 6.92500   8.80700   8.59200   1.000 48.25194 ? 73  ASP A OD1 1 
ATOM   577  O OD2 . ASP A 1 76  ? 8.53100   9.47200   7.24400   1.000 50.29952 ? 73  ASP A OD2 1 
ATOM   578  N N   . ILE A 1 77  ? 5.99400   5.79000   7.96300   1.000 37.55597 ? 74  ILE A N   1 
ATOM   579  C CA  . ILE A 1 77  ? 4.96000   5.68700   7.00000   1.000 42.12719 ? 74  ILE A CA  1 
ATOM   580  C C   . ILE A 1 77  ? 4.47300   7.11200   6.69200   1.000 44.01069 ? 74  ILE A C   1 
ATOM   581  O O   . ILE A 1 77  ? 4.22600   7.88000   7.58900   1.000 41.77581 ? 74  ILE A O   1 
ATOM   582  C CB  . ILE A 1 77  ? 3.79800   4.85200   7.52000   1.000 43.63315 ? 74  ILE A CB  1 
ATOM   583  C CG1 . ILE A 1 77  ? 4.19300   3.39900   7.60200   1.000 48.81467 ? 74  ILE A CG1 1 
ATOM   584  C CG2 . ILE A 1 77  ? 2.63800   4.98300   6.60000   1.000 44.05211 ? 74  ILE A CG2 1 
ATOM   585  C CD1 . ILE A 1 77  ? 3.57700   2.65500   8.74800   1.000 50.80825 ? 74  ILE A CD1 1 
ATOM   586  N N   . GLU A 1 78  ? 4.37400   7.46700   5.43100   1.000 38.52194 ? 75  GLU A N   1 
ATOM   587  C CA  . GLU A 1 78  ? 3.94600   8.78500   5.03800   1.000 41.44048 ? 75  GLU A CA  1 
ATOM   588  C C   . GLU A 1 78  ? 2.60700   8.63100   4.38300   1.000 47.59479 ? 75  GLU A C   1 
ATOM   589  O O   . GLU A 1 78  ? 2.53100   8.55400   3.18600   1.000 48.63011 ? 75  GLU A O   1 
ATOM   590  C CB  . GLU A 1 78  ? 4.91300   9.36900   4.03000   1.000 44.44261 ? 75  GLU A CB  1 
ATOM   591  C CG  . GLU A 1 78  ? 6.36100   9.03000   4.31400   1.000 42.84518 ? 75  GLU A CG  1 
ATOM   592  C CD  . GLU A 1 78  ? 7.32000   10.16600  4.05500   1.000 52.55317 ? 75  GLU A CD  1 
ATOM   593  O OE1 . GLU A 1 78  ? 7.25800   11.17800  4.75900   1.000 52.90096 ? 75  GLU A OE1 1 
ATOM   594  O OE2 . GLU A 1 78  ? 8.15300   10.02700  3.16200   1.000 52.51618 ? 75  GLU A OE2 1 
ATOM   595  N N   . VAL A 1 85  ? -2.35200  3.15700   -2.13300  1.000 42.07744 ? 82  VAL A N   1 
ATOM   596  C CA  . VAL A 1 85  ? -0.92000  3.42500   -2.20300  1.000 38.72241 ? 82  VAL A CA  1 
ATOM   597  C C   . VAL A 1 85  ? -0.40900  3.87100   -0.83700  1.000 47.51881 ? 82  VAL A C   1 
ATOM   598  O O   . VAL A 1 85  ? -0.93800  4.82100   -0.24200  1.000 46.85022 ? 82  VAL A O   1 
ATOM   599  C CB  . VAL A 1 85  ? -0.59900  4.48500   -3.27200  1.000 49.02510 ? 82  VAL A CB  1 
ATOM   600  C CG1 . VAL A 1 85  ? 0.90500   4.72200   -3.36700  1.000 44.82194 ? 82  VAL A CG1 1 
ATOM   601  C CG2 . VAL A 1 85  ? -1.17400  4.06600   -4.61900  1.000 50.96817 ? 82  VAL A CG2 1 
ATOM   602  N N   . VAL A 1 86  ? 0.63000   3.20600   -0.36000  1.000 41.98797 ? 83  VAL A N   1 
ATOM   603  C CA  . VAL A 1 86  ? 1.26200   3.50100   0.91800   1.000 38.21516 ? 83  VAL A CA  1 
ATOM   604  C C   . VAL A 1 86  ? 2.73300   3.77600   0.64500   1.000 36.67349 ? 83  VAL A C   1 
ATOM   605  O O   . VAL A 1 86  ? 3.39600   2.96800   -0.01700  1.000 32.02156 ? 83  VAL A O   1 
ATOM   606  C CB  . VAL A 1 86  ? 1.08500   2.34100   1.91600   1.000 38.87460 ? 83  VAL A CB  1 
ATOM   607  C CG1 . VAL A 1 86  ? 1.83600   2.61300   3.20400   1.000 41.23914 ? 83  VAL A CG1 1 
ATOM   608  C CG2 . VAL A 1 86  ? -0.39500  2.12400   2.20300   1.000 43.92044 ? 83  VAL A CG2 1 
ATOM   609  N N   . ILE A 1 87  ? 3.25000   4.91000   1.13400   1.000 30.70974 ? 84  ILE A N   1 
ATOM   610  C CA  . ILE A 1 87  ? 4.61500   5.33900   0.94800   1.000 32.03453 ? 84  ILE A CA  1 
ATOM   611  C C   . ILE A 1 87  ? 5.34600   5.23200   2.28700   1.000 36.09363 ? 84  ILE A C   1 
ATOM   612  O O   . ILE A 1 87  ? 4.91300   5.78000   3.24200   1.000 33.39061 ? 84  ILE A O   1 
ATOM   613  C CB  . ILE A 1 87  ? 4.69200   6.81000   0.52600   1.000 34.67243 ? 84  ILE A CB  1 
ATOM   614  C CG1 . ILE A 1 87  ? 3.81500   7.08200   -0.66800  1.000 40.36134 ? 84  ILE A CG1 1 
ATOM   615  C CG2 . ILE A 1 87  ? 6.11600   7.21100   0.26700   1.000 35.73135 ? 84  ILE A CG2 1 
ATOM   616  C CD1 . ILE A 1 87  ? 4.22600   6.39000   -1.91600  1.000 37.89964 ? 84  ILE A CD1 1 
ATOM   617  N N   . VAL A 1 88  ? 6.45400   4.51200   2.34200   1.000 29.90832 ? 85  VAL A N   1 
ATOM   618  C CA  . VAL A 1 88  ? 7.17800   4.26000   3.58200   1.000 26.21342 ? 85  VAL A CA  1 
ATOM   619  C C   . VAL A 1 88  ? 8.64200   4.57000   3.35700   1.000 28.81947 ? 85  VAL A C   1 
ATOM   620  O O   . VAL A 1 88  ? 9.22600   4.11200   2.37300   1.000 24.35521 ? 85  VAL A O   1 
ATOM   621  C CB  . VAL A 1 88  ? 7.03600   2.80200   4.06300   1.000 31.44879 ? 85  VAL A CB  1 
ATOM   622  C CG1 . VAL A 1 88  ? 7.62100   2.65800   5.44400   1.000 27.05256 ? 85  VAL A CG1 1 
ATOM   623  C CG2 . VAL A 1 88  ? 5.59700   2.36100   4.06100   1.000 34.12141 ? 85  VAL A CG2 1 
ATOM   624  N N   . LYS A 1 89  ? 9.26900   5.37200   4.23000   1.000 26.29199 ? 86  LYS A N   1 
ATOM   625  C CA  . LYS A 1 89  ? 10.65200  5.70700   4.19600   1.000 26.90871 ? 86  LYS A CA  1 
ATOM   626  C C   . LYS A 1 89  ? 11.39800  4.87300   5.28300   1.000 29.33636 ? 86  LYS A C   1 
ATOM   627  O O   . LYS A 1 89  ? 11.06200  4.91400   6.41800   1.000 26.93276 ? 86  LYS A O   1 
ATOM   628  C CB  . LYS A 1 89  ? 10.78600  7.20100   4.46800   1.000 29.11004 ? 86  LYS A CB  1 
ATOM   629  C CG  . LYS A 1 89  ? 12.18700  7.77600   4.43300   1.000 34.04955 ? 86  LYS A CG  1 
ATOM   630  C CD  . LYS A 1 89  ? 12.20800  9.29500   4.64400   1.000 39.44725 ? 86  LYS A CD  1 
ATOM   631  C CE  . LYS A 1 89  ? 11.08300  9.96500   3.86500   1.000 48.03996 ? 86  LYS A CE  1 
ATOM   632  N NZ  . LYS A 1 89  ? 11.03500  11.46100  3.76300   1.000 53.00853 ? 86  LYS A NZ  1 
ATOM   633  N N   . VAL A 1 90  ? 12.42300  4.14300   4.90100   1.000 22.98981 ? 87  VAL A N   1 
ATOM   634  C CA  . VAL A 1 90  ? 13.21300  3.30800   5.79500   1.000 21.38712 ? 87  VAL A CA  1 
ATOM   635  C C   . VAL A 1 90  ? 14.64300  3.77700   5.72700   1.000 23.33922 ? 87  VAL A C   1 
ATOM   636  O O   . VAL A 1 90  ? 15.19600  3.91200   4.64600   1.000 23.42155 ? 87  VAL A O   1 
ATOM   637  C CB  . VAL A 1 90  ? 13.12600  1.82000   5.39200   1.000 20.99167 ? 87  VAL A CB  1 
ATOM   638  C CG1 . VAL A 1 90  ? 13.85100  0.94200   6.37100   1.000 22.96071 ? 87  VAL A CG1 1 
ATOM   639  C CG2 . VAL A 1 90  ? 11.65600  1.38500   5.25800   1.000 23.39971 ? 87  VAL A CG2 1 
ATOM   640  N N   . LYS A 1 91  ? 15.28900  3.98400   6.87300   1.000 24.96471 ? 88  LYS A N   1 
ATOM   641  C CA  . LYS A 1 91  ? 16.67300  4.31900   6.92400   1.000 24.71175 ? 88  LYS A CA  1 
ATOM   642  C C   . LYS A 1 91  ? 17.37800  3.05100   7.38600   1.000 24.28207 ? 88  LYS A C   1 
ATOM   643  O O   . LYS A 1 91  ? 16.96700  2.44000   8.30300   1.000 27.30355 ? 88  LYS A O   1 
ATOM   644  C CB  . LYS A 1 91  ? 16.94900  5.43900   7.89900   1.000 27.94655 ? 88  LYS A CB  1 
ATOM   645  C CG  . LYS A 1 91  ? 16.64300  6.79000   7.34500   1.000 31.03415 ? 88  LYS A CG  1 
ATOM   646  C CD  . LYS A 1 91  ? 17.23700  7.89300   8.19600   1.000 35.58701 ? 88  LYS A CD  1 
ATOM   647  C CE  . LYS A 1 91  ? 16.81800  9.26900   7.69200   1.000 40.82385 ? 88  LYS A CE  1 
ATOM   648  N NZ  . LYS A 1 91  ? 17.66600  10.38900  8.22000   1.000 47.81913 ? 88  LYS A NZ  1 
ATOM   649  N N   . VAL A 1 92  ? 18.44500  2.68500   6.69300   1.000 21.50937 ? 89  VAL A N   1 
ATOM   650  C CA  . VAL A 1 92  ? 19.14200  1.45300   6.93200   1.000 23.47323 ? 89  VAL A CA  1 
ATOM   651  C C   . VAL A 1 92  ? 20.66600  1.61900   6.96400   1.000 24.54165 ? 89  VAL A C   1 
ATOM   652  O O   . VAL A 1 92  ? 21.19700  2.41500   6.23700   1.000 24.23815 ? 89  VAL A O   1 
ATOM   653  C CB  . VAL A 1 92  ? 18.90000  0.48700   5.72800   1.000 24.04504 ? 89  VAL A CB  1 
ATOM   654  C CG1 . VAL A 1 92  ? 19.50100  -0.87400  5.92200   1.000 25.25590 ? 89  VAL A CG1 1 
ATOM   655  C CG2 . VAL A 1 92  ? 17.45700  0.34800   5.36600   1.000 25.29248 ? 89  VAL A CG2 1 
ATOM   656  N N   . ARG A 1 93  ? 21.33000  0.93600   7.88100   1.000 19.91329 ? 90  ARG A N   1 
ATOM   657  C CA  . ARG A 1 93  ? 22.77200  0.81800   7.80400   1.000 21.79309 ? 90  ARG A CA  1 
ATOM   658  C C   . ARG A 1 93  ? 23.10600  -0.51800  7.15700   1.000 25.15367 ? 90  ARG A C   1 
ATOM   659  O O   . ARG A 1 93  ? 22.47500  -1.53400  7.45900   1.000 26.58647 ? 90  ARG A O   1 
ATOM   660  C CB  . ARG A 1 93  ? 23.37800  0.92800   9.20900   1.000 27.76797 ? 90  ARG A CB  1 
ATOM   661  C CG  . ARG A 1 93  ? 24.91800  0.94600   9.19100   1.000 36.86516 ? 90  ARG A CG  1 
ATOM   662  C CD  . ARG A 1 93  ? 25.52200  0.53300   10.53300  1.000 40.29979 ? 90  ARG A CD  1 
ATOM   663  N NE  . ARG A 1 93  ? 26.95100  0.23500   10.44400  1.000 44.40605 ? 90  ARG A NE  1 
ATOM   664  C CZ  . ARG A 1 93  ? 27.46200  -0.97800  10.26000  1.000 43.51828 ? 90  ARG A CZ  1 
ATOM   665  N NH1 . ARG A 1 93  ? 26.69000  -2.05000  10.15200  1.000 51.12709 ? 90  ARG A NH1 1 
ATOM   666  N NH2 . ARG A 1 93  ? 28.78200  -1.12000  10.18700  1.000 46.86184 ? 90  ARG A NH2 1 
ATOM   667  N N   . ALA A 1 94  ? 24.05400  -0.51400  6.22400   1.000 21.76470 ? 91  ALA A N   1 
ATOM   668  C CA  . ALA A 1 94  ? 24.39900  -1.72200  5.50000   1.000 20.09154 ? 91  ALA A CA  1 
ATOM   669  C C   . ALA A 1 94  ? 25.89900  -1.87600  5.43900   1.000 27.36961 ? 91  ALA A C   1 
ATOM   670  O O   . ALA A 1 94  ? 26.64800  -0.89600  5.43100   1.000 25.02704 ? 91  ALA A O   1 
ATOM   671  C CB  . ALA A 1 94  ? 23.82700  -1.73500  4.10300   1.000 20.55467 ? 91  ALA A CB  1 
ATOM   672  N N   . THR A 1 95  ? 26.34800  -3.12700  5.33400   1.000 24.57625 ? 92  THR A N   1 
ATOM   673  C CA  . THR A 1 95  ? 27.73500  -3.41700  5.17300   1.000 22.64845 ? 92  THR A CA  1 
ATOM   674  C C   . THR A 1 95  ? 27.88400  -4.45200  4.08900   1.000 23.75335 ? 92  THR A C   1 
ATOM   675  O O   . THR A 1 95  ? 27.03900  -5.27800  3.93100   1.000 24.43265 ? 92  THR A O   1 
ATOM   676  C CB  . THR A 1 95  ? 28.38700  -4.01700  6.43100   1.000 31.97866 ? 92  THR A CB  1 
ATOM   677  O OG1 . THR A 1 95  ? 27.67200  -5.15900  6.87900   1.000 27.04343 ? 92  THR A OG1 1 
ATOM   678  C CG2 . THR A 1 95  ? 28.39100  -3.04600  7.47600   1.000 31.63561 ? 92  THR A CG2 1 
ATOM   679  N N   . MET A 1 96  ? 28.99100  -4.39800  3.37000   1.000 21.59598 ? 93  MET A N   1 
ATOM   680  C CA  . MET A 1 96  ? 29.33000  -5.33200  2.34000   1.000 25.38493 ? 93  MET A CA  1 
ATOM   681  C C   . MET A 1 96  ? 30.82200  -5.55300  2.42900   1.000 32.23422 ? 93  MET A C   1 
ATOM   682  O O   . MET A 1 96  ? 31.52200  -4.64000  2.71800   1.000 38.25812 ? 93  MET A O   1 
ATOM   683  C CB  . MET A 1 96  ? 29.03200  -4.77400  0.97000   1.000 34.88949 ? 93  MET A CB  1 
ATOM   684  C CG  . MET A 1 96  ? 27.80400  -5.32800  0.37100   1.000 36.25484 ? 93  MET A CG  1 
ATOM   685  S SD  . MET A 1 96  ? 27.57300  -4.89100  -1.32700  1.000 33.25127 ? 93  MET A SD  1 
ATOM   686  C CE  . MET A 1 96  ? 28.23200  -3.28000  -1.29900  1.000 27.22758 ? 93  MET A CE  1 
ATOM   687  N N   . VAL A 1 97  ? 31.29000  -6.75300  2.17700   1.000 30.21538 ? 94  VAL A N   1 
ATOM   688  C CA  . VAL A 1 97  ? 32.71500  -7.05100  2.22300   1.000 34.75512 ? 94  VAL A CA  1 
ATOM   689  C C   . VAL A 1 97  ? 33.15300  -7.33400  0.78900   1.000 39.74735 ? 94  VAL A C   1 
ATOM   690  O O   . VAL A 1 97  ? 32.74100  -8.29600  0.22600   1.000 42.00404 ? 94  VAL A O   1 
ATOM   691  C CB  . VAL A 1 97  ? 33.02400  -8.25400  3.08800   1.000 31.68286 ? 94  VAL A CB  1 
ATOM   692  C CG1 . VAL A 1 97  ? 34.48600  -8.58200  3.02300   1.000 39.91174 ? 94  VAL A CG1 1 
ATOM   693  C CG2 . VAL A 1 97  ? 32.62500  -7.97800  4.51800   1.000 34.47314 ? 94  VAL A CG2 1 
ATOM   694  N N   . ARG A 1 98  ? 34.03800  -6.51400  0.25000   1.000 43.49203 ? 95  ARG A N   1 
ATOM   695  C CA  . ARG A 1 98  ? 34.47700  -6.53100  -1.14200  1.000 42.76855 ? 95  ARG A CA  1 
ATOM   696  C C   . ARG A 1 98  ? 35.98500  -6.73600  -1.15900  1.000 52.79622 ? 95  ARG A C   1 
ATOM   697  O O   . ARG A 1 98  ? 36.73600  -5.83800  -0.76400  1.000 51.14195 ? 95  ARG A O   1 
ATOM   698  C CB  . ARG A 1 98  ? 34.09800  -5.22600  -1.84800  1.000 50.68603 ? 95  ARG A CB  1 
ATOM   699  C CG  . ARG A 1 98  ? 34.71400  -5.03600  -3.23200  1.000 57.52764 ? 95  ARG A CG  1 
ATOM   700  C CD  . ARG A 1 98  ? 34.09800  -5.97100  -4.26800  1.000 58.75838 ? 95  ARG A CD  1 
ATOM   701  N NE  . ARG A 1 98  ? 35.06100  -6.41900  -5.27200  1.000 65.46840 ? 95  ARG A NE  1 
ATOM   702  C CZ  . ARG A 1 98  ? 34.76000  -7.19500  -6.30800  1.000 67.86400 ? 95  ARG A CZ  1 
ATOM   703  N NH1 . ARG A 1 98  ? 33.51600  -7.59200  -6.53900  1.000 62.79150 ? 95  ARG A NH1 1 
ATOM   704  N NH2 . ARG A 1 98  ? 35.73100  -7.58300  -7.13300  1.000 68.77718 ? 95  ARG A NH2 1 
ATOM   705  N N   . ASN A 1 99  ? 36.42700  -7.90400  -1.62300  1.000 57.83189 ? 96  ASN A N   1 
ATOM   706  C CA  . ASN A 1 99  ? 37.84900  -8.22500  -1.68000  1.000 54.60642 ? 96  ASN A CA  1 
ATOM   707  C C   . ASN A 1 99  ? 38.51200  -7.98000  -0.32600  1.000 53.64218 ? 96  ASN A C   1 
ATOM   708  O O   . ASN A 1 99  ? 39.54400  -7.31800  -0.22100  1.000 56.25901 ? 96  ASN A O   1 
ATOM   709  C CB  . ASN A 1 99  ? 38.54800  -7.41700  -2.77600  1.000 56.32454 ? 96  ASN A CB  1 
ATOM   710  C CG  . ASN A 1 99  ? 38.33000  -8.00200  -4.15700  1.000 62.81654 ? 96  ASN A CG  1 
ATOM   711  O OD1 . ASN A 1 99  ? 38.33300  -9.22200  -4.33600  1.000 62.15311 ? 96  ASN A OD1 1 
ATOM   712  N ND2 . ASN A 1 99  ? 38.13600  -7.13300  -5.14300  1.000 64.91899 ? 96  ASN A ND2 1 
ATOM   713  N N   . GLY A 1 100 ? 37.87500  -8.41800  0.72300   1.000 55.68254 ? 97  GLY A N   1 
ATOM   714  C CA  . GLY A 1 100 ? 38.42900  -8.28600  2.03700   1.000 52.12871 ? 97  GLY A CA  1 
ATOM   715  C C   . GLY A 1 100 ? 38.34700  -6.94200  2.66900   1.000 53.23670 ? 97  GLY A C   1 
ATOM   716  O O   . GLY A 1 100 ? 38.79300  -6.84000  3.78300   1.000 55.91451 ? 97  GLY A O   1 
ATOM   717  N N   . GLN A 1 101 ? 37.74400  -5.94100  2.02400   1.000 41.36613 ? 98  GLN A N   1 
ATOM   718  C CA  . GLN A 1 101 ? 37.66600  -4.63000  2.60200   1.000 46.94876 ? 98  GLN A CA  1 
ATOM   719  C C   . GLN A 1 101 ? 36.18700  -4.41000  2.85500   1.000 40.71527 ? 98  GLN A C   1 
ATOM   720  O O   . GLN A 1 101 ? 35.40900  -4.52000  1.95300   1.000 39.23396 ? 98  GLN A O   1 
ATOM   721  C CB  . GLN A 1 101 ? 38.21300  -3.59600  1.62600   1.000 46.16267 ? 98  GLN A CB  1 
ATOM   722  C CG  . GLN A 1 101 ? 38.14100  -2.14800  2.13600   1.000 55.51943 ? 98  GLN A CG  1 
ATOM   723  C CD  . GLN A 1 101 ? 38.55700  -1.08200  1.09600   1.000 62.54364 ? 98  GLN A CD  1 
ATOM   724  O OE1 . GLN A 1 101 ? 38.67100  -1.37200  -0.09300  1.000 66.47238 ? 98  GLN A OE1 1 
ATOM   725  N NE2 . GLN A 1 101 ? 38.75600  0.15000   1.54400   1.000 60.68255 ? 98  GLN A NE2 1 
ATOM   726  N N   . GLU A 1 102 ? 35.80500  -4.13300  4.08200   1.000 40.00511 ? 99  GLU A N   1 
ATOM   727  C CA  . GLU A 1 102 ? 34.43700  -3.91000  4.39600   1.000 38.19058 ? 99  GLU A CA  1 
ATOM   728  C C   . GLU A 1 102 ? 34.06000  -2.48800  3.99100   1.000 41.53849 ? 99  GLU A C   1 
ATOM   729  O O   . GLU A 1 102 ? 34.87900  -1.60000  4.07100   1.000 43.07540 ? 99  GLU A O   1 
ATOM   730  C CB  . GLU A 1 102 ? 34.24400  -4.11000  5.89200   1.000 40.32243 ? 99  GLU A CB  1 
ATOM   731  C CG  . GLU A 1 102 ? 32.81200  -4.22500  6.36100   1.000 42.21361 ? 99  GLU A CG  1 
ATOM   732  C CD  . GLU A 1 102 ? 32.62000  -3.83800  7.79900   1.000 50.90976 ? 99  GLU A CD  1 
ATOM   733  O OE1 . GLU A 1 102 ? 33.41100  -4.27200  8.64800   1.000 51.06900 ? 99  GLU A OE1 1 
ATOM   734  O OE2 . GLU A 1 102 ? 31.68900  -3.09300  8.08700   1.000 47.78123 ? 99  GLU A OE2 1 
ATOM   735  N N   . HIS A 1 103 ? 32.83000  -2.28400  3.54600   1.000 29.22671 ? 100 HIS A N   1 
ATOM   736  C CA  . HIS A 1 103 ? 32.34600  -0.97600  3.16400   1.000 27.99541 ? 100 HIS A CA  1 
ATOM   737  C C   . HIS A 1 103 ? 31.06900  -0.76800  3.96200   1.000 28.01731 ? 100 HIS A C   1 
ATOM   738  O O   . HIS A 1 103 ? 30.33600  -1.69400  4.16400   1.000 30.09280 ? 100 HIS A O   1 
ATOM   739  C CB  . HIS A 1 103 ? 32.04600  -0.91600  1.67700   1.000 33.64027 ? 100 HIS A CB  1 
ATOM   740  C CG  . HIS A 1 103 ? 33.24400  -1.04300  0.78700   1.000 41.34136 ? 100 HIS A CG  1 
ATOM   741  N ND1 . HIS A 1 103 ? 33.89700  0.04100   0.26400   1.000 41.77243 ? 100 HIS A ND1 1 
ATOM   742  C CD2 . HIS A 1 103 ? 33.85800  -2.12800  0.26800   1.000 45.01558 ? 100 HIS A CD2 1 
ATOM   743  C CE1 . HIS A 1 103 ? 34.87600  -0.36600  -0.51100  1.000 48.53293 ? 100 HIS A CE1 1 
ATOM   744  N NE2 . HIS A 1 103 ? 34.87400  -1.67900  -0.52800  1.000 45.89360 ? 100 HIS A NE2 1 
ATOM   745  N N   . VAL A 1 104 ? 30.81700  0.43800   4.41800   1.000 23.26403 ? 101 VAL A N   1 
ATOM   746  C CA  . VAL A 1 104 ? 29.66100  0.70100   5.23200   1.000 22.36445 ? 101 VAL A CA  1 
ATOM   747  C C   . VAL A 1 104 ? 28.80600  1.75200   4.58800   1.000 25.68691 ? 101 VAL A C   1 
ATOM   748  O O   . VAL A 1 104 ? 29.32600  2.70800   4.11300   1.000 25.85007 ? 101 VAL A O   1 
ATOM   749  C CB  . VAL A 1 104 ? 30.06800  1.20100   6.60300   1.000 24.81757 ? 101 VAL A CB  1 
ATOM   750  C CG1 . VAL A 1 104 ? 28.89200  1.27900   7.50200   1.000 23.81945 ? 101 VAL A CG1 1 
ATOM   751  C CG2 . VAL A 1 104 ? 31.09400  0.27100   7.19600   1.000 35.76175 ? 101 VAL A CG2 1 
ATOM   752  N N   . PHE A 1 105 ? 27.50000  1.54600   4.57900   1.000 21.04083 ? 102 PHE A N   1 
ATOM   753  C CA  . PHE A 1 105 ? 26.59800  2.44200   3.93700   1.000 20.93771 ? 102 PHE A CA  1 
ATOM   754  C C   . PHE A 1 105 ? 25.41200  2.88600   4.77100   1.000 23.38268 ? 102 PHE A C   1 
ATOM   755  O O   . PHE A 1 105 ? 25.00100  2.19800   5.64400   1.000 24.36533 ? 102 PHE A O   1 
ATOM   756  C CB  . PHE A 1 105 ? 25.99100  1.76500   2.70100   1.000 21.52369 ? 102 PHE A CB  1 
ATOM   757  C CG  . PHE A 1 105 ? 26.98800  1.19300   1.77300   1.000 23.17206 ? 102 PHE A CG  1 
ATOM   758  C CD1 . PHE A 1 105 ? 27.52400  -0.03900  2.00400   1.000 23.36678 ? 102 PHE A CD1 1 
ATOM   759  C CD2 . PHE A 1 105 ? 27.37600  1.87500   0.66500   1.000 23.24591 ? 102 PHE A CD2 1 
ATOM   760  C CE1 . PHE A 1 105 ? 28.45300  -0.57300  1.16800   1.000 23.62453 ? 102 PHE A CE1 1 
ATOM   761  C CE2 . PHE A 1 105 ? 28.31200  1.35300   -0.17200  1.000 24.27432 ? 102 PHE A CE2 1 
ATOM   762  C CZ  . PHE A 1 105 ? 28.83800  0.11100   0.06700   1.000 26.67916 ? 102 PHE A CZ  1 
ATOM   763  N N   . GLU A 1 106 ? 24.86100  4.04800   4.48000   1.000 20.83645 ? 103 GLU A N   1 
ATOM   764  C CA  . GLU A 1 106 ? 23.64600  4.48000   5.11600   1.000 20.47028 ? 103 GLU A CA  1 
ATOM   765  C C   . GLU A 1 106 ? 22.70700  4.67300   3.93100   1.000 23.67867 ? 103 GLU A C   1 
ATOM   766  O O   . GLU A 1 106 ? 23.07200  5.29100   2.99600   1.000 25.21597 ? 103 GLU A O   1 
ATOM   767  C CB  . GLU A 1 106 ? 23.81400  5.76600   5.87000   1.000 25.61677 ? 103 GLU A CB  1 
ATOM   768  C CG  . GLU A 1 106 ? 22.50900  6.34800   6.32100   1.000 27.41247 ? 103 GLU A CG  1 
ATOM   769  C CD  . GLU A 1 106 ? 22.04600  5.89700   7.65500   1.000 43.20335 ? 103 GLU A CD  1 
ATOM   770  O OE1 . GLU A 1 106 ? 22.80700  5.31000   8.44400   1.000 45.08442 ? 103 GLU A OE1 1 
ATOM   771  O OE2 . GLU A 1 106 ? 20.86100  6.12300   7.93400   1.000 49.93551 ? 103 GLU A OE2 1 
ATOM   772  N N   . VAL A 1 107 ? 21.56000  4.00700   3.90800   1.000 20.19585 ? 104 VAL A N   1 
ATOM   773  C CA  . VAL A 1 107 ? 20.65000  4.00600   2.77600   1.000 19.31992 ? 104 VAL A CA  1 
ATOM   774  C C   . VAL A 1 107 ? 19.28900  4.50500   3.23100   1.000 20.01390 ? 104 VAL A C   1 
ATOM   775  O O   . VAL A 1 107 ? 18.78000  4.08700   4.26600   1.000 22.82925 ? 104 VAL A O   1 
ATOM   776  C CB  . VAL A 1 107 ? 20.53000  2.59000   2.17000   1.000 17.64528 ? 104 VAL A CB  1 
ATOM   777  C CG1 . VAL A 1 107 ? 19.60200  2.67800   0.98000   1.000 22.66359 ? 104 VAL A CG1 1 
ATOM   778  C CG2 . VAL A 1 107 ? 21.94800  2.08900   1.74100   1.000 22.19535 ? 104 VAL A CG2 1 
ATOM   779  N N   . VAL A 1 108 ? 18.67200  5.38000   2.44100   1.000 19.03771 ? 105 VAL A N   1 
ATOM   780  C CA  . VAL A 1 108 ? 17.30500  5.77300   2.68700   1.000 17.42252 ? 105 VAL A CA  1 
ATOM   781  C C   . VAL A 1 108 ? 16.50400  5.14900   1.57600   1.000 22.36360 ? 105 VAL A C   1 
ATOM   782  O O   . VAL A 1 108 ? 16.73300  5.45400   0.40900   1.000 21.84848 ? 105 VAL A O   1 
ATOM   783  C CB  . VAL A 1 108 ? 17.10600  7.29700   2.72200   1.000 21.92762 ? 105 VAL A CB  1 
ATOM   784  C CG1 . VAL A 1 108 ? 15.68300  7.60200   3.04400   1.000 24.16638 ? 105 VAL A CG1 1 
ATOM   785  C CG2 . VAL A 1 108 ? 18.09200  7.89400   3.72900   1.000 22.34032 ? 105 VAL A CG2 1 
ATOM   786  N N   . ASP A 1 109 ? 15.63300  4.21800   1.95400   1.000 18.96655 ? 106 ASP A N   1 
ATOM   787  C CA  . ASP A 1 109 ? 14.78300  3.47000   1.02100   1.000 18.00900 ? 106 ASP A CA  1 
ATOM   788  C C   . ASP A 1 109 ? 13.37200  4.01200   1.13300   1.000 20.01607 ? 106 ASP A C   1 
ATOM   789  O O   . ASP A 1 109 ? 12.76100  3.95200   2.19700   1.000 24.73885 ? 106 ASP A O   1 
ATOM   790  C CB  . ASP A 1 109 ? 14.78500  1.98600   1.37600   1.000 19.08225 ? 106 ASP A CB  1 
ATOM   791  C CG  . ASP A 1 109 ? 16.02800  1.27900   0.91300   1.000 20.25565 ? 106 ASP A CG  1 
ATOM   792  O OD1 . ASP A 1 109 ? 16.60300  1.67900   -0.11000  1.000 21.92961 ? 106 ASP A OD1 1 
ATOM   793  O OD2 . ASP A 1 109 ? 16.42800  0.27500   1.58600   1.000 22.50161 ? 106 ASP A OD2 1 
ATOM   794  N N   . THR A 1 110 ? 12.84500  4.55400   0.04200   1.000 22.93544 ? 107 THR A N   1 
ATOM   795  C CA  . THR A 1 110 ? 11.47000  4.96900   0.03100   1.000 23.14260 ? 107 THR A CA  1 
ATOM   796  C C   . THR A 1 110 ? 10.67700  4.06400   -0.89000  1.000 21.69603 ? 107 THR A C   1 
ATOM   797  O O   . THR A 1 110 ? 10.93000  4.03000   -2.10000  1.000 24.70800 ? 107 THR A O   1 
ATOM   798  C CB  . THR A 1 110 ? 11.36700  6.42800   -0.40400  1.000 23.59688 ? 107 THR A CB  1 
ATOM   799  O OG1 . THR A 1 110 ? 12.19200  7.21800   0.46300   1.000 27.00035 ? 107 THR A OG1 1 
ATOM   800  C CG2 . THR A 1 110 ? 9.94100   6.86900   -0.31400  1.000 30.02224 ? 107 THR A CG2 1 
ATOM   801  N N   . TYR A 1 111 ? 9.73700   3.34100   -0.30200  1.000 19.43954 ? 108 TYR A N   1 
ATOM   802  C CA  . TYR A 1 111 ? 8.92100   2.34000   -0.96300  1.000 22.24138 ? 108 TYR A CA  1 
ATOM   803  C C   . TYR A 1 111 ? 7.55100   2.89900   -1.27200  1.000 28.58107 ? 108 TYR A C   1 
ATOM   804  O O   . TYR A 1 111 ? 6.96800   3.58500   -0.43200  1.000 28.45147 ? 108 TYR A O   1 
ATOM   805  C CB  . TYR A 1 111 ? 8.68800   1.11300   -0.06600  1.000 24.62640 ? 108 TYR A CB  1 
ATOM   806  C CG  . TYR A 1 111 ? 9.94400   0.31100   0.21700   1.000 21.45365 ? 108 TYR A CG  1 
ATOM   807  C CD1 . TYR A 1 111 ? 10.78300  0.64200   1.25700   1.000 22.96624 ? 108 TYR A CD1 1 
ATOM   808  C CD2 . TYR A 1 111 ? 10.29600  -0.75400  -0.59100  1.000 22.62748 ? 108 TYR A CD2 1 
ATOM   809  C CE1 . TYR A 1 111 ? 11.94900  -0.10600  1.50200   1.000 22.76612 ? 108 TYR A CE1 1 
ATOM   810  C CE2 . TYR A 1 111 ? 11.46200  -1.48900  -0.35000  1.000 25.17914 ? 108 TYR A CE2 1 
ATOM   811  C CZ  . TYR A 1 111 ? 12.26100  -1.14800  0.70500   1.000 25.15144 ? 108 TYR A CZ  1 
ATOM   812  O OH  . TYR A 1 111 ? 13.40800  -1.85300  0.95800   1.000 22.09259 ? 108 TYR A OH  1 
ATOM   813  N N   . GLU A 1 112 ? 6.97500   2.41900   -2.37400  1.000 24.10182 ? 109 GLU A N   1 
ATOM   814  C CA  . GLU A 1 112 ? 5.59700   2.65000   -2.72100  1.000 29.98396 ? 109 GLU A CA  1 
ATOM   815  C C   . GLU A 1 112 ? 4.96500   1.24700   -2.76200  1.000 28.94267 ? 109 GLU A C   1 
ATOM   816  O O   . GLU A 1 112 ? 5.37200   0.44800   -3.53500  1.000 27.66851 ? 109 GLU A O   1 
ATOM   817  C CB  . GLU A 1 112 ? 5.42300   3.31100   -4.07500  1.000 25.80434 ? 109 GLU A CB  1 
ATOM   818  C CG  . GLU A 1 112 ? 3.96300   3.66000   -4.38100  1.000 37.59840 ? 109 GLU A CG  1 
ATOM   819  C CD  . GLU A 1 112 ? 3.65800   4.01600   -5.84000  1.000 47.84510 ? 109 GLU A CD  1 
ATOM   820  O OE1 . GLU A 1 112 ? 4.57400   4.22700   -6.64800  1.000 37.61041 ? 109 GLU A OE1 1 
ATOM   821  O OE2 . GLU A 1 112 ? 2.48400   4.07800   -6.19200  1.000 46.37245 ? 109 GLU A OE2 1 
ATOM   822  N N   . PHE A 1 113 ? 4.01300   0.95500   -1.87700  1.000 29.34800 ? 110 PHE A N   1 
ATOM   823  C CA  . PHE A 1 113 ? 3.31500   -0.31400  -1.85000  1.000 30.25659 ? 110 PHE A CA  1 
ATOM   824  C C   . PHE A 1 113 ? 1.93500   -0.10500  -2.48300  1.000 42.91953 ? 110 PHE A C   1 
ATOM   825  O O   . PHE A 1 113 ? 1.34100   0.91000   -2.29500  1.000 35.56623 ? 110 PHE A O   1 
ATOM   826  C CB  . PHE A 1 113 ? 3.10600   -0.80400  -0.42500  1.000 33.41189 ? 110 PHE A CB  1 
ATOM   827  C CG  . PHE A 1 113 ? 4.29600   -1.46800  0.21000   1.000 31.37636 ? 110 PHE A CG  1 
ATOM   828  C CD1 . PHE A 1 113 ? 5.28900   -0.74200  0.75600   1.000 27.32010 ? 110 PHE A CD1 1 
ATOM   829  C CD2 . PHE A 1 113 ? 4.36900   -2.82900  0.31300   1.000 32.91159 ? 110 PHE A CD2 1 
ATOM   830  C CE1 . PHE A 1 113 ? 6.34400   -1.33400  1.35500   1.000 28.89068 ? 110 PHE A CE1 1 
ATOM   831  C CE2 . PHE A 1 113 ? 5.43500   -3.43500  0.91200   1.000 31.49907 ? 110 PHE A CE2 1 
ATOM   832  C CZ  . PHE A 1 113 ? 6.41100   -2.67600  1.45100   1.000 29.78476 ? 110 PHE A CZ  1 
ATOM   833  N N   . ARG A 1 114 ? 1.43000   -1.06900  -3.22000  1.000 35.96335 ? 111 ARG A N   1 
ATOM   834  C CA  . ARG A 1 114 ? 0.11800   -0.92800  -3.83700  1.000 40.38534 ? 111 ARG A CA  1 
ATOM   835  C C   . ARG A 1 114 ? -0.62700  -2.23300  -3.63600  1.000 41.39351 ? 111 ARG A C   1 
ATOM   836  O O   . ARG A 1 114 ? -0.05100  -3.26600  -3.74000  1.000 40.29455 ? 111 ARG A O   1 
ATOM   837  C CB  . ARG A 1 114 ? 0.24900   -0.60700  -5.32200  1.000 43.85062 ? 111 ARG A CB  1 
ATOM   838  C CG  . ARG A 1 114 ? -0.97400  0.01100   -5.98200  1.000 50.15858 ? 111 ARG A CG  1 
ATOM   839  C CD  . ARG A 1 114 ? -0.76100  0.16300   -7.47200  1.000 52.39006 ? 111 ARG A CD  1 
ATOM   840  N NE  . ARG A 1 114 ? -0.49900  1.53700   -7.88100  1.000 55.14160 ? 111 ARG A NE  1 
ATOM   841  C CZ  . ARG A 1 114 ? 0.51800   1.94200   -8.65300  1.000 60.17835 ? 111 ARG A CZ  1 
ATOM   842  N NH1 . ARG A 1 114 ? 1.42000   1.07900   -9.12500  1.000 58.54517 ? 111 ARG A NH1 1 
ATOM   843  N NH2 . ARG A 1 114 ? 0.62800   3.23100   -8.97200  1.000 55.86323 ? 111 ARG A NH2 1 
ATOM   844  N N   . ARG A 1 115 ? -1.92600  -2.17900  -3.36500  1.000 42.12564 ? 112 ARG A N   1 
ATOM   845  C CA  . ARG A 1 115 ? -2.65400  -3.40700  -3.12100  1.000 47.96949 ? 112 ARG A CA  1 
ATOM   846  C C   . ARG A 1 115 ? -2.98300  -4.11300  -4.45300  1.000 48.87865 ? 112 ARG A C   1 
ATOM   847  O O   . ARG A 1 115 ? -3.57800  -3.53500  -5.32200  1.000 56.91224 ? 112 ARG A O   1 
ATOM   848  C CB  . ARG A 1 115 ? -3.90400  -3.20700  -2.23500  1.000 53.81247 ? 112 ARG A CB  1 
ATOM   849  C CG  . ARG A 1 115 ? -4.67100  -4.47200  -1.85800  1.000 59.14815 ? 112 ARG A CG  1 
ATOM   850  C CD  . ARG A 1 115 ? -5.46000  -4.32800  -0.56000  1.000 63.95223 ? 112 ARG A CD  1 
ATOM   851  N NE  . ARG A 1 115 ? -5.88200  -5.60700  0.03200   1.000 62.31154 ? 112 ARG A NE  1 
ATOM   852  C CZ  . ARG A 1 115 ? -5.72700  -5.93400  1.31600   1.000 63.30286 ? 112 ARG A CZ  1 
ATOM   853  N NH1 . ARG A 1 115 ? -5.25600  -5.04200  2.14300   1.000 64.29499 ? 112 ARG A NH1 1 
ATOM   854  N NH2 . ARG A 1 115 ? -6.08100  -7.11900  1.81300   1.000 61.78894 ? 112 ARG A NH2 1 
ATOM   855  N N   . SER A 1 119 ? -3.43700  -8.41400  -1.21200  1.000 57.80404 ? 116 SER A N   1 
ATOM   856  C CA  . SER A 1 119 ? -2.11800  -8.30600  -0.60300  1.000 59.18842 ? 116 SER A CA  1 
ATOM   857  C C   . SER A 1 119 ? -1.44000  -7.03300  -1.08600  1.000 47.87038 ? 116 SER A C   1 
ATOM   858  O O   . SER A 1 119 ? -1.68300  -6.56300  -2.20000  1.000 49.45963 ? 116 SER A O   1 
ATOM   859  C CB  . SER A 1 119 ? -1.23300  -9.50800  -0.94600  1.000 52.78657 ? 116 SER A CB  1 
ATOM   860  O OG  . SER A 1 119 ? -0.59200  -9.31300  -2.19400  1.000 58.38898 ? 116 SER A OG  1 
ATOM   861  N N   . TRP A 1 120 ? -0.58200  -6.48400  -0.23600  1.000 48.44383 ? 117 TRP A N   1 
ATOM   862  C CA  . TRP A 1 120 ? 0.24500   -5.34600  -0.60700  1.000 49.10784 ? 117 TRP A CA  1 
ATOM   863  C C   . TRP A 1 120 ? 1.54900   -5.81800  -1.24300  1.000 41.62708 ? 117 TRP A C   1 
ATOM   864  O O   . TRP A 1 120 ? 2.17900   -6.77600  -0.77500  1.000 45.07258 ? 117 TRP A O   1 
ATOM   865  C CB  . TRP A 1 120 ? 0.53400   -4.47600  0.61600   1.000 44.91603 ? 117 TRP A CB  1 
ATOM   866  C CG  . TRP A 1 120 ? -0.69100  -3.86100  1.21700   1.000 50.33843 ? 117 TRP A CG  1 
ATOM   867  C CD1 . TRP A 1 120 ? -1.45500  -4.37000  2.22800   1.000 52.61818 ? 117 TRP A CD1 1 
ATOM   868  C CD2 . TRP A 1 120 ? -1.30000  -2.61900  0.84100   1.000 51.21026 ? 117 TRP A CD2 1 
ATOM   869  N NE1 . TRP A 1 120 ? -2.49900  -3.51900  2.50800   1.000 56.03710 ? 117 TRP A NE1 1 
ATOM   870  C CE2 . TRP A 1 120 ? -2.42700  -2.43800  1.66900   1.000 55.52884 ? 117 TRP A CE2 1 
ATOM   871  C CE3 . TRP A 1 120 ? -1.00000  -1.64200  -0.11300  1.000 50.83408 ? 117 TRP A CE3 1 
ATOM   872  C CZ2 . TRP A 1 120 ? -3.25100  -1.31900  1.57400   1.000 56.62835 ? 117 TRP A CZ2 1 
ATOM   873  C CZ3 . TRP A 1 120 ? -1.81700  -0.53100  -0.20500  1.000 46.91185 ? 117 TRP A CZ3 1 
ATOM   874  C CH2 . TRP A 1 120 ? -2.93400  -0.38100  0.63100   1.000 51.49521 ? 117 TRP A CH2 1 
ATOM   875  N N   . LYS A 1 121 ? 1.95700   -5.14200  -2.31200  1.000 36.97828 ? 118 LYS A N   1 
ATOM   876  C CA  . LYS A 1 121 ? 3.19800   -5.46600  -2.99300  1.000 35.08204 ? 118 LYS A CA  1 
ATOM   877  C C   . LYS A 1 121 ? 3.98600   -4.19700  -3.25700  1.000 32.64239 ? 118 LYS A C   1 
ATOM   878  O O   . LYS A 1 121 ? 3.41400   -3.11600  -3.45300  1.000 32.08153 ? 118 LYS A O   1 
ATOM   879  C CB  . LYS A 1 121 ? 2.94300   -6.19900  -4.31000  1.000 39.89599 ? 118 LYS A CB  1 
ATOM   880  C CG  . LYS A 1 121 ? 2.35800   -7.60000  -4.11600  1.000 43.00093 ? 118 LYS A CG  1 
ATOM   881  C CD  . LYS A 1 121 ? 3.40100   -8.56400  -3.57700  1.000 40.63799 ? 118 LYS A CD  1 
ATOM   882  C CE  . LYS A 1 121 ? 2.82000   -9.55300  -2.56400  1.000 52.69922 ? 118 LYS A CE  1 
ATOM   883  N NZ  . LYS A 1 121 ? 1.74300   -10.40700 -3.14600  1.000 54.60095 ? 118 LYS A NZ  1 
ATOM   884  N N   . ILE A 1 122 ? 5.31000   -4.32800  -3.30100  1.000 27.52405 ? 119 ILE A N   1 
ATOM   885  C CA  . ILE A 1 122 ? 6.15600   -3.20600  -3.60200  1.000 25.93562 ? 119 ILE A CA  1 
ATOM   886  C C   . ILE A 1 122 ? 6.00700   -2.91600  -5.07800  1.000 27.40162 ? 119 ILE A C   1 
ATOM   887  O O   . ILE A 1 122 ? 6.10300   -3.81200  -5.85900  1.000 26.18360 ? 119 ILE A O   1 
ATOM   888  C CB  . ILE A 1 122 ? 7.62100   -3.52800  -3.33000  1.000 24.86244 ? 119 ILE A CB  1 
ATOM   889  C CG1 . ILE A 1 122 ? 7.82500   -3.67300  -1.84700  1.000 23.24560 ? 119 ILE A CG1 1 
ATOM   890  C CG2 . ILE A 1 122 ? 8.52400   -2.42900  -3.81300  1.000 27.77836 ? 119 ILE A CG2 1 
ATOM   891  C CD1 . ILE A 1 122 ? 9.14500   -4.25400  -1.47500  1.000 26.83700 ? 119 ILE A CD1 1 
ATOM   892  N N   . VAL A 1 123 ? 5.66300   -1.70200  -5.45300  1.000 26.50255 ? 120 VAL A N   1 
ATOM   893  C CA  . VAL A 1 123 ? 5.64300   -1.38500  -6.85000  1.000 29.83290 ? 120 VAL A CA  1 
ATOM   894  C C   . VAL A 1 123 ? 6.74600   -0.41900  -7.24800  1.000 30.29617 ? 120 VAL A C   1 
ATOM   895  O O   . VAL A 1 123 ? 7.03400   -0.25400  -8.40000  1.000 26.76225 ? 120 VAL A O   1 
ATOM   896  C CB  . VAL A 1 123 ? 4.28700   -0.86800  -7.32100  1.000 29.87775 ? 120 VAL A CB  1 
ATOM   897  C CG1 . VAL A 1 123 ? 3.22200   -1.86600  -6.98700  1.000 32.27109 ? 120 VAL A CG1 1 
ATOM   898  C CG2 . VAL A 1 123 ? 3.98100   0.41300   -6.64800  1.000 33.39058 ? 120 VAL A CG2 1 
ATOM   899  N N   . LYS A 1 124 ? 7.38000   0.20100   -6.27700  1.000 21.69540 ? 121 LYS A N   1 
ATOM   900  C CA  . LYS A 1 124 ? 8.42800   1.10400   -6.58100  1.000 24.06337 ? 121 LYS A CA  1 
ATOM   901  C C   . LYS A 1 124 ? 9.36800   1.29600   -5.40400  1.000 22.37305 ? 121 LYS A C   1 
ATOM   902  O O   . LYS A 1 124 ? 8.93100   1.37700   -4.32400  1.000 23.10465 ? 121 LYS A O   1 
ATOM   903  C CB  . LYS A 1 124 ? 7.88600   2.49700   -6.95400  1.000 26.47634 ? 121 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 124 ? 8.94300   3.38500   -7.54900  1.000 26.04832 ? 121 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 124 ? 8.33100   4.49900   -8.37300  1.000 33.34788 ? 121 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 124 ? 9.36000   5.49700   -8.81400  1.000 33.95195 ? 121 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 124 ? 8.81100   6.39300   -9.85700  1.000 42.98789 ? 121 LYS A NZ  1 
ATOM   908  N N   . LEU A 1 125 ? 10.65200  1.33500   -5.63800  1.000 21.18437 ? 122 LEU A N   1 
ATOM   909  C CA  . LEU A 1 125 ? 11.58200  1.70500   -4.56800  1.000 24.47439 ? 122 LEU A CA  1 
ATOM   910  C C   . LEU A 1 125 ? 12.54800  2.75100   -5.08600  1.000 24.28272 ? 122 LEU A C   1 
ATOM   911  O O   . LEU A 1 125 ? 13.13300  2.57100   -6.15400  1.000 23.58580 ? 122 LEU A O   1 
ATOM   912  C CB  . LEU A 1 125 ? 12.35600  0.49300   -4.09400  1.000 21.61389 ? 122 LEU A CB  1 
ATOM   913  C CG  . LEU A 1 125 ? 13.62400  0.77300   -3.29100  1.000 25.57043 ? 122 LEU A CG  1 
ATOM   914  C CD1 . LEU A 1 125 ? 13.31800  1.47000   -1.97000  1.000 24.43757 ? 122 LEU A CD1 1 
ATOM   915  C CD2 . LEU A 1 125 ? 14.37400  -0.53100  -3.10300  1.000 27.08594 ? 122 LEU A CD2 1 
ATOM   916  N N   . VAL A 1 126 ? 12.78200  3.82100   -4.31900  1.000 21.45937 ? 123 VAL A N   1 
ATOM   917  C CA  . VAL A 1 126 ? 13.85500  4.75000   -4.59800  1.000 21.64567 ? 123 VAL A CA  1 
ATOM   918  C C   . VAL A 1 126 ? 14.85800  4.63800   -3.45200  1.000 23.54426 ? 123 VAL A C   1 
ATOM   919  O O   . VAL A 1 126 ? 14.47300  4.79900   -2.28600  1.000 26.32613 ? 123 VAL A O   1 
ATOM   920  C CB  . VAL A 1 126 ? 13.34200  6.18800   -4.74400  1.000 25.33646 ? 123 VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 126 ? 14.48700  7.14300   -4.98400  1.000 28.40321 ? 123 VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 126 ? 12.34400  6.25000   -5.89800  1.000 25.23075 ? 123 VAL A CG2 1 
ATOM   923  N N   . SER A 1 127 ? 16.13000  4.37700   -3.77100  1.000 21.80198 ? 124 SER A N   1 
ATOM   924  C CA  . SER A 1 127 ? 17.17700  4.21900   -2.76000  1.000 19.82166 ? 124 SER A CA  1 
ATOM   925  C C   . SER A 1 127 ? 18.26500  5.30300   -2.87300  1.000 27.22896 ? 124 SER A C   1 
ATOM   926  O O   . SER A 1 127 ? 18.85200  5.44200   -3.90100  1.000 24.62162 ? 124 SER A O   1 
ATOM   927  C CB  . SER A 1 127 ? 17.89300  2.88300   -2.91000  1.000 27.28862 ? 124 SER A CB  1 
ATOM   928  O OG  . SER A 1 127 ? 17.01600  1.80600   -2.92600  1.000 28.34405 ? 124 SER A OG  1 
ATOM   929  N N   . GLU A 1 128 ? 18.50100  6.04900   -1.80700  1.000 21.32299 ? 125 GLU A N   1 
ATOM   930  C CA  . GLU A 1 128 ? 19.55000  6.98800   -1.74300  1.000 20.40797 ? 125 GLU A CA  1 
ATOM   931  C C   . GLU A 1 128 ? 20.64700  6.28600   -0.96000  1.000 19.94637 ? 125 GLU A C   1 
ATOM   932  O O   . GLU A 1 128 ? 20.46800  6.03000   0.16600   1.000 21.86119 ? 125 GLU A O   1 
ATOM   933  C CB  . GLU A 1 128 ? 19.03000  8.23000   -1.04800  1.000 26.06763 ? 125 GLU A CB  1 
ATOM   934  C CG  . GLU A 1 128 ? 20.03300  9.22300   -0.55600  1.000 31.23872 ? 125 GLU A CG  1 
ATOM   935  C CD  . GLU A 1 128 ? 21.25600  9.41400   -1.37500  1.000 44.29717 ? 125 GLU A CD  1 
ATOM   936  O OE1 . GLU A 1 128 ? 21.03600  9.85500   -2.52200  1.000 44.50031 ? 125 GLU A OE1 1 
ATOM   937  O OE2 . GLU A 1 128 ? 22.41200  9.23800   -0.82800  1.000 39.66628 ? 125 GLU A OE2 1 
ATOM   938  N N   . ILE A 1 129 ? 21.77700  6.01800   -1.59800  1.000 20.17255 ? 126 ILE A N   1 
ATOM   939  C CA  . ILE A 1 129 ? 22.86400  5.22600   -1.02900  1.000 22.08664 ? 126 ILE A CA  1 
ATOM   940  C C   . ILE A 1 129 ? 24.07700  6.12000   -0.80300  1.000 24.34792 ? 126 ILE A C   1 
ATOM   941  O O   . ILE A 1 129 ? 24.59200  6.70600   -1.74800  1.000 25.96499 ? 126 ILE A O   1 
ATOM   942  C CB  . ILE A 1 129 ? 23.23400  4.06600   -1.95500  1.000 24.07080 ? 126 ILE A CB  1 
ATOM   943  C CG1 . ILE A 1 129 ? 22.02000  3.14600   -2.09700  1.000 27.52832 ? 126 ILE A CG1 1 
ATOM   944  C CG2 . ILE A 1 129 ? 24.45800  3.34000   -1.39300  1.000 27.02334 ? 126 ILE A CG2 1 
ATOM   945  C CD1 . ILE A 1 129 ? 22.00200  2.34500   -3.36000  1.000 26.80859 ? 126 ILE A CD1 1 
ATOM   946  N N   . THR A 1 130 ? 24.56300  6.17500   0.43400   1.000 20.64528 ? 127 THR A N   1 
ATOM   947  C CA  . THR A 1 130 ? 25.70800  6.92900   0.78500   1.000 24.50639 ? 127 THR A CA  1 
ATOM   948  C C   . THR A 1 130 ? 26.72100  5.96800   1.38000   1.000 24.61778 ? 127 THR A C   1 
ATOM   949  O O   . THR A 1 130 ? 26.37000  5.20500   2.20100   1.000 24.48263 ? 127 THR A O   1 
ATOM   950  C CB  . THR A 1 130 ? 25.37400  7.93300   1.89700   1.000 24.85268 ? 127 THR A CB  1 
ATOM   951  O OG1 . THR A 1 130 ? 24.36600  8.82000   1.46400   1.000 27.20182 ? 127 THR A OG1 1 
ATOM   952  C CG2 . THR A 1 130 ? 26.58800  8.65400   2.27400   1.000 30.33674 ? 127 THR A CG2 1 
ATOM   953  N N   . GLN A 1 131 ? 27.95300  6.00100   0.93300   1.000 21.90794 ? 128 GLN A N   1 
ATOM   954  C CA  . GLN A 1 131 ? 28.98300  5.16300   1.48700   1.000 21.80547 ? 128 GLN A CA  1 
ATOM   955  C C   . GLN A 1 131 ? 29.64700  5.96600   2.59700   1.000 24.70671 ? 128 GLN A C   1 
ATOM   956  O O   . GLN A 1 131 ? 30.12600  7.01300   2.36800   1.000 25.63154 ? 128 GLN A O   1 
ATOM   957  C CB  . GLN A 1 131 ? 30.00200  4.73600   0.45700   1.000 23.57944 ? 128 GLN A CB  1 
ATOM   958  C CG  . GLN A 1 131 ? 30.95900  3.73500   1.03600   1.000 29.45911 ? 128 GLN A CG  1 
ATOM   959  C CD  . GLN A 1 131 ? 31.99700  3.28000   0.07900   1.000 34.69863 ? 128 GLN A CD  1 
ATOM   960  O OE1 . GLN A 1 131 ? 33.00900  2.81200   0.48000   1.000 48.68629 ? 128 GLN A OE1 1 
ATOM   961  N NE2 . GLN A 1 131 ? 31.72900  3.39600   -1.19000  1.000 38.24969 ? 128 GLN A NE2 1 
ATOM   962  N N   . LEU A 1 132 ? 29.61700  5.44600   3.79500   1.000 22.62925 ? 129 LEU A N   1 
ATOM   963  C CA  . LEU A 1 132 ? 30.13000  6.16200   4.93600   1.000 31.65488 ? 129 LEU A CA  1 
ATOM   964  C C   . LEU A 1 132 ? 31.58400  6.03500   5.15600   1.000 36.33960 ? 129 LEU A C   1 
ATOM   965  O O   . LEU A 1 132 ? 32.21800  6.92800   5.66800   1.000 38.06056 ? 129 LEU A O   1 
ATOM   966  C CB  . LEU A 1 132 ? 29.45000  5.67600   6.18800   1.000 26.75906 ? 129 LEU A CB  1 
ATOM   967  C CG  . LEU A 1 132 ? 27.96100  5.85800   6.22500   1.000 25.45875 ? 129 LEU A CG  1 
ATOM   968  C CD1 . LEU A 1 132 ? 27.42300  5.44700   7.56300   1.000 28.27111 ? 129 LEU A CD1 1 
ATOM   969  C CD2 . LEU A 1 132 ? 27.60400  7.29300   5.93300   1.000 29.52621 ? 129 LEU A CD2 1 
ATOM   970  N N   . GLY A 1 133 ? 32.12500  4.91500   4.77500   1.000 32.44451 ? 130 GLY A N   1 
ATOM   971  C CA  . GLY A 1 133 ? 33.50100  4.65200   5.06500   1.000 41.90670 ? 130 GLY A CA  1 
ATOM   972  C C   . GLY A 1 133 ? 33.53900  3.76800   6.30500   1.000 45.53726 ? 130 GLY A C   1 
ATOM   973  O O   . GLY A 1 133 ? 32.87800  4.02900   7.29100   1.000 48.71033 ? 130 GLY A O   1 
ATOM   974  N N   . SER A 1 134 ? 34.31100  2.69200   6.23600   1.000 47.06794 ? 131 SER A N   1 
ATOM   975  C CA  . SER A 1 134 ? 34.40500  1.74100   7.32700   1.000 48.83915 ? 131 SER A CA  1 
ATOM   976  C C   . SER A 1 134 ? 35.08500  2.28600   8.54700   1.000 51.58249 ? 131 SER A C   1 
ATOM   977  O O   . SER A 1 134 ? 35.76000  1.55500   9.23300   1.000 60.13213 ? 131 SER A O   1 
ATOM   978  C CB  . SER A 1 134 ? 35.12100  0.47500   6.88600   1.000 45.29724 ? 131 SER A CB  1 
ATOM   979  O OG  . SER A 1 134 ? 35.01500  -0.48400  7.89600   1.000 51.80390 ? 131 SER A OG  1 
ATOM   980  N N   . GLU B 1 7   ? -5.96900  10.52700  13.16900  1.000 52.49336 ? 4   GLU B N   1 
ATOM   981  C CA  . GLU B 1 7   ? -4.60000  10.87900  13.38800  1.000 50.66779 ? 4   GLU B CA  1 
ATOM   982  C C   . GLU B 1 7   ? -4.44800  12.12700  14.26200  1.000 48.39496 ? 4   GLU B C   1 
ATOM   983  O O   . GLU B 1 7   ? -3.37500  12.57600  14.43600  1.000 42.33323 ? 4   GLU B O   1 
ATOM   984  C CB  . GLU B 1 7   ? -3.93600  11.14100  12.02700  1.000 58.67417 ? 4   GLU B CB  1 
ATOM   985  C CG  . GLU B 1 7   ? -3.24100  9.95800   11.37000  1.000 61.22073 ? 4   GLU B CG  1 
ATOM   986  C CD  . GLU B 1 7   ? -2.46400  10.31700  10.11400  1.000 66.93807 ? 4   GLU B CD  1 
ATOM   987  O OE1 . GLU B 1 7   ? -2.65300  11.44800  9.60100   1.000 67.08593 ? 4   GLU B OE1 1 
ATOM   988  O OE2 . GLU B 1 7   ? -1.65700  9.47600   9.63900   1.000 68.82568 ? 4   GLU B OE2 1 
ATOM   989  N N   . GLU B 1 8   ? -5.50000  12.67200  14.82900  1.000 46.07160 ? 5   GLU B N   1 
ATOM   990  C CA  . GLU B 1 8   ? -5.33900  13.90700  15.58700  1.000 43.60670 ? 5   GLU B CA  1 
ATOM   991  C C   . GLU B 1 8   ? -4.40000  13.82600  16.76700  1.000 48.56722 ? 5   GLU B C   1 
ATOM   992  O O   . GLU B 1 8   ? -3.52800  14.65300  16.92800  1.000 49.03393 ? 5   GLU B O   1 
ATOM   993  C CB  . GLU B 1 8   ? -6.65600  14.46300  16.06200  1.000 46.45490 ? 5   GLU B CB  1 
ATOM   994  C CG  . GLU B 1 8   ? -6.83600  15.87600  15.58800  1.000 47.10552 ? 5   GLU B CG  1 
ATOM   995  C CD  . GLU B 1 8   ? -6.74000  16.91800  16.68200  1.000 52.12392 ? 5   GLU B CD  1 
ATOM   996  O OE1 . GLU B 1 8   ? -5.83900  16.81900  17.54600  1.000 58.13825 ? 5   GLU B OE1 1 
ATOM   997  O OE2 . GLU B 1 8   ? -7.57400  17.84900  16.64600  1.000 53.33327 ? 5   GLU B OE2 1 
ATOM   998  N N   . ALA B 1 9   ? -4.59000  12.82900  17.60100  1.000 45.35785 ? 6   ALA B N   1 
ATOM   999  C CA  . ALA B 1 9   ? -3.70700  12.69700  18.74900  1.000 42.00348 ? 6   ALA B CA  1 
ATOM   1000 C C   . ALA B 1 9   ? -2.29200  12.41500  18.35000  1.000 41.86345 ? 6   ALA B C   1 
ATOM   1001 O O   . ALA B 1 9   ? -1.38400  12.90600  18.95800  1.000 42.10764 ? 6   ALA B O   1 
ATOM   1002 C CB  . ALA B 1 9   ? -4.20200  11.62100  19.67900  1.000 49.99718 ? 6   ALA B CB  1 
ATOM   1003 N N   . LYS B 1 10  ? -2.10200  11.59300  17.35300  1.000 37.83029 ? 7   LYS B N   1 
ATOM   1004 C CA  . LYS B 1 10  ? -0.78900  11.29700  16.92800  1.000 38.80370 ? 7   LYS B CA  1 
ATOM   1005 C C   . LYS B 1 10  ? -0.08500  12.54200  16.43100  1.000 45.68666 ? 7   LYS B C   1 
ATOM   1006 O O   . LYS B 1 10  ? 0.98100   12.84500  16.85500  1.000 43.03620 ? 7   LYS B O   1 
ATOM   1007 C CB  . LYS B 1 10  ? -0.83900  10.26900  15.84000  1.000 41.20628 ? 7   LYS B CB  1 
ATOM   1008 C CG  . LYS B 1 10  ? -1.21500  8.89900   16.34600  1.000 49.39861 ? 7   LYS B CG  1 
ATOM   1009 C CD  . LYS B 1 10  ? -0.78200  7.79100   15.40100  1.000 54.15531 ? 7   LYS B CD  1 
ATOM   1010 C CE  . LYS B 1 10  ? -1.39100  6.44300   15.74800  1.000 51.33926 ? 7   LYS B CE  1 
ATOM   1011 N NZ  . LYS B 1 10  ? -1.49900  5.61000   14.52500  1.000 55.10236 ? 7   LYS B NZ  1 
ATOM   1012 N N   . GLU B 1 11  ? -0.77800  13.34300  15.64800  1.000 40.34682 ? 8   GLU B N   1 
ATOM   1013 C CA  . GLU B 1 11  ? -0.22100  14.54700  15.10800  1.000 38.71175 ? 8   GLU B CA  1 
ATOM   1014 C C   . GLU B 1 11  ? 0.19700   15.48700  16.20600  1.000 36.89104 ? 8   GLU B C   1 
ATOM   1015 O O   . GLU B 1 11  ? 1.24500   16.06100  16.09600  1.000 35.44509 ? 8   GLU B O   1 
ATOM   1016 C CB  . GLU B 1 11  ? -1.27200  15.25200  14.21500  1.000 36.40243 ? 8   GLU B CB  1 
ATOM   1017 C CG  . GLU B 1 11  ? -0.74500  16.28300  13.21700  1.000 34.33433 ? 8   GLU B CG  1 
ATOM   1018 C CD  . GLU B 1 11  ? -1.84400  17.13600  12.61800  1.000 44.31835 ? 8   GLU B CD  1 
ATOM   1019 O OE1 . GLU B 1 11  ? -3.01000  16.91000  12.90100  1.000 39.96703 ? 8   GLU B OE1 1 
ATOM   1020 O OE2 . GLU B 1 11  ? -1.53800  18.04500  11.89400  1.000 36.76041 ? 8   GLU B OE2 1 
ATOM   1021 N N   . ALA B 1 12  ? -0.57500  15.63800  17.24700  1.000 34.04284 ? 9   ALA B N   1 
ATOM   1022 C CA  . ALA B 1 12  ? -0.22000  16.55500  18.29000  1.000 41.06452 ? 9   ALA B CA  1 
ATOM   1023 C C   . ALA B 1 12  ? 0.99300   16.05200  19.05900  1.000 42.85114 ? 9   ALA B C   1 
ATOM   1024 O O   . ALA B 1 12  ? 1.88400   16.80200  19.37000  1.000 35.93250 ? 9   ALA B O   1 
ATOM   1025 C CB  . ALA B 1 12  ? -1.38700  16.77900  19.20700  1.000 40.07098 ? 9   ALA B CB  1 
ATOM   1026 N N   . ILE B 1 13  ? 1.02000   14.76500  19.31200  1.000 35.97123 ? 10  ILE B N   1 
ATOM   1027 C CA  . ILE B 1 13  ? 2.12200   14.19700  20.06100  1.000 37.27351 ? 10  ILE B CA  1 
ATOM   1028 C C   . ILE B 1 13  ? 3.45400   14.22000  19.32800  1.000 33.87849 ? 10  ILE B C   1 
ATOM   1029 O O   . ILE B 1 13  ? 4.47000   14.53800  19.89900  1.000 32.07794 ? 10  ILE B O   1 
ATOM   1030 C CB  . ILE B 1 13  ? 1.72500   12.83400  20.57700  1.000 38.70573 ? 10  ILE B CB  1 
ATOM   1031 C CG1 . ILE B 1 13  ? 0.54200   13.04000  21.51600  1.000 40.34400 ? 10  ILE B CG1 1 
ATOM   1032 C CG2 . ILE B 1 13  ? 2.86800   12.18500  21.27900  1.000 41.12568 ? 10  ILE B CG2 1 
ATOM   1033 C CD1 . ILE B 1 13  ? 0.53600   12.19600  22.74800  1.000 42.70040 ? 10  ILE B CD1 1 
ATOM   1034 N N   . ILE B 1 14  ? 3.44800   13.94800  18.04800  1.000 30.02763 ? 11  ILE B N   1 
ATOM   1035 C CA  . ILE B 1 14  ? 4.65900   14.00500  17.30700  1.000 30.01001 ? 11  ILE B CA  1 
ATOM   1036 C C   . ILE B 1 14  ? 5.14300   15.46400  17.27000  1.000 35.38220 ? 11  ILE B C   1 
ATOM   1037 O O   . ILE B 1 14  ? 6.28400   15.73300  17.47100  1.000 29.46502 ? 11  ILE B O   1 
ATOM   1038 C CB  . ILE B 1 14  ? 4.45300   13.38700  15.94600  1.000 38.26614 ? 11  ILE B CB  1 
ATOM   1039 C CG1 . ILE B 1 14  ? 4.49600   11.88000  16.07800  1.000 40.86161 ? 11  ILE B CG1 1 
ATOM   1040 C CG2 . ILE B 1 14  ? 5.49700   13.81400  14.96500  1.000 38.23538 ? 11  ILE B CG2 1 
ATOM   1041 C CD1 . ILE B 1 14  ? 3.41900   11.19100  15.29300  1.000 45.61237 ? 11  ILE B CD1 1 
ATOM   1042 N N   . ALA B 1 15  ? 4.23700   16.38900  17.04900  1.000 32.51358 ? 12  ALA B N   1 
ATOM   1043 C CA  . ALA B 1 15  ? 4.56300   17.79200  17.07100  1.000 30.88060 ? 12  ALA B CA  1 
ATOM   1044 C C   . ALA B 1 15  ? 5.14100   18.20100  18.40400  1.000 35.50319 ? 12  ALA B C   1 
ATOM   1045 O O   . ALA B 1 15  ? 6.03900   18.98200  18.43700  1.000 33.13744 ? 12  ALA B O   1 
ATOM   1046 C CB  . ALA B 1 15  ? 3.33400   18.61400  16.81600  1.000 32.56479 ? 12  ALA B CB  1 
ATOM   1047 N N   . MET B 1 16  ? 4.57300   17.71100  19.48900  1.000 30.05531 ? 13  MET B N   1 
ATOM   1048 C CA  . MET B 1 16  ? 5.08900   18.01500  20.82100  1.000 31.31676 ? 13  MET B CA  1 
ATOM   1049 C C   . MET B 1 16  ? 6.46900   17.40300  21.03400  1.000 26.65547 ? 13  MET B C   1 
ATOM   1050 O O   . MET B 1 16  ? 7.34300   18.02800  21.65500  1.000 25.31257 ? 13  MET B O   1 
ATOM   1051 C CB  . MET B 1 16  ? 4.12900   17.51200  21.89200  1.000 33.58244 ? 13  MET B CB  1 
ATOM   1052 C CG  . MET B 1 16  ? 2.87300   18.33000  22.04900  1.000 42.78647 ? 13  MET B CG  1 
ATOM   1053 S SD  . MET B 1 16  ? 1.75000   17.51900  23.20900  1.000 49.87461 ? 13  MET B SD  1 
ATOM   1054 C CE  . MET B 1 16  ? 0.34900   18.63400  23.15500  1.000 45.99013 ? 13  MET B CE  1 
ATOM   1055 N N   . LEU B 1 17  ? 6.69400   16.19400  20.54500  1.000 24.90440 ? 14  LEU B N   1 
ATOM   1056 C CA  . LEU B 1 17  ? 8.03100   15.61600  20.70800  1.000 25.49817 ? 14  LEU B CA  1 
ATOM   1057 C C   . LEU B 1 17  ? 9.05100   16.39600  19.89700  1.000 28.14891 ? 14  LEU B C   1 
ATOM   1058 O O   . LEU B 1 17  ? 10.15600  16.65500  20.37300  1.000 26.05201 ? 14  LEU B O   1 
ATOM   1059 C CB  . LEU B 1 17  ? 8.04300   14.14200  20.32500  1.000 26.78707 ? 14  LEU B CB  1 
ATOM   1060 C CG  . LEU B 1 17  ? 7.39000   13.24300  21.37100  1.000 32.34758 ? 14  LEU B CG  1 
ATOM   1061 C CD1 . LEU B 1 17  ? 7.11500   11.91100  20.71900  1.000 32.88229 ? 14  LEU B CD1 1 
ATOM   1062 C CD2 . LEU B 1 17  ? 8.24900   13.09500  22.64500  1.000 30.05968 ? 14  LEU B CD2 1 
ATOM   1063 N N   . LYS B 1 18  ? 8.66000   16.90600  18.74800  1.000 26.96992 ? 15  LYS B N   1 
ATOM   1064 C CA  . LYS B 1 18  ? 9.56600   17.72000  17.96500  1.000 28.65120 ? 15  LYS B CA  1 
ATOM   1065 C C   . LYS B 1 18  ? 9.90000   18.97700  18.75700  1.000 28.97376 ? 15  LYS B C   1 
ATOM   1066 O O   . LYS B 1 18  ? 11.01000  19.39800  18.78900  1.000 28.12273 ? 15  LYS B O   1 
ATOM   1067 C CB  . LYS B 1 18  ? 8.93000   18.08800  16.62900  1.000 28.65525 ? 15  LYS B CB  1 
ATOM   1068 C CG  . LYS B 1 18  ? 9.70500   19.09000  15.78000  1.000 41.55262 ? 15  LYS B CG  1 
ATOM   1069 C CD  . LYS B 1 18  ? 8.92900   19.60000  14.56800  1.000 39.85607 ? 15  LYS B CD  1 
ATOM   1070 C CE  . LYS B 1 18  ? 9.73200   20.56800  13.70700  1.000 41.41960 ? 15  LYS B CE  1 
ATOM   1071 N NZ  . LYS B 1 18  ? 11.07300  20.88500  14.24000  1.000 40.71331 ? 15  LYS B NZ  1 
ATOM   1072 N N   . GLU B 1 19  ? 8.90700   19.55600  19.39500  1.000 23.12283 ? 16  GLU B N   1 
ATOM   1073 C CA  . GLU B 1 19  ? 9.13100   20.72900  20.19100  1.000 24.99768 ? 16  GLU B CA  1 
ATOM   1074 C C   . GLU B 1 19  ? 10.05100  20.43800  21.35600  1.000 26.59253 ? 16  GLU B C   1 
ATOM   1075 O O   . GLU B 1 19  ? 10.90400  21.20300  21.65800  1.000 26.81673 ? 16  GLU B O   1 
ATOM   1076 C CB  . GLU B 1 19  ? 7.84600   21.25400  20.75600  1.000 30.41775 ? 16  GLU B CB  1 
ATOM   1077 C CG  . GLU B 1 19  ? 6.90700   21.83800  19.73200  1.000 35.80413 ? 16  GLU B CG  1 
ATOM   1078 C CD  . GLU B 1 19  ? 5.59600   22.21500  20.35400  1.000 41.16489 ? 16  GLU B CD  1 
ATOM   1079 O OE1 . GLU B 1 19  ? 5.60800   22.77900  21.44400  1.000 51.79640 ? 16  GLU B OE1 1 
ATOM   1080 O OE2 . GLU B 1 19  ? 4.55700   21.92900  19.78200  1.000 52.15510 ? 16  GLU B OE2 1 
ATOM   1081 N N   . TRP B 1 20  ? 9.82300   19.31100  22.00500  1.000 25.30485 ? 17  TRP B N   1 
ATOM   1082 C CA  . TRP B 1 20  ? 10.61800  18.93000  23.17000  1.000 20.84392 ? 17  TRP B CA  1 
ATOM   1083 C C   . TRP B 1 20  ? 12.10200  18.89700  22.83400  1.000 18.14039 ? 17  TRP B C   1 
ATOM   1084 O O   . TRP B 1 20  ? 12.92400  19.55900  23.49000  1.000 19.07973 ? 17  TRP B O   1 
ATOM   1085 C CB  . TRP B 1 20  ? 10.14300  17.55100  23.67500  1.000 22.51991 ? 17  TRP B CB  1 
ATOM   1086 C CG  . TRP B 1 20  ? 10.94700  17.04000  24.82700  1.000 22.16363 ? 17  TRP B CG  1 
ATOM   1087 C CD1 . TRP B 1 20  ? 12.08800  16.28300  24.77400  1.000 21.77930 ? 17  TRP B CD1 1 
ATOM   1088 C CD2 . TRP B 1 20  ? 10.70000  17.30800  26.21100  1.000 21.42868 ? 17  TRP B CD2 1 
ATOM   1089 N NE1 . TRP B 1 20  ? 12.56900  16.06400  26.05700  1.000 24.30062 ? 17  TRP B NE1 1 
ATOM   1090 C CE2 . TRP B 1 20  ? 11.72300  16.68500  26.94900  1.000 24.05108 ? 17  TRP B CE2 1 
ATOM   1091 C CE3 . TRP B 1 20  ? 9.70900   18.02100  26.89300  1.000 20.84362 ? 17  TRP B CE3 1 
ATOM   1092 C CZ2 . TRP B 1 20  ? 11.76300  16.73300  28.34400  1.000 27.20750 ? 17  TRP B CZ2 1 
ATOM   1093 C CZ3 . TRP B 1 20  ? 9.75800   18.08800  28.26500  1.000 24.80824 ? 17  TRP B CZ3 1 
ATOM   1094 C CH2 . TRP B 1 20  ? 10.76100  17.42400  28.98500  1.000 29.39306 ? 17  TRP B CH2 1 
ATOM   1095 N N   . TYR B 1 21  ? 12.46500  18.13600  21.81000  1.000 21.82890 ? 18  TYR B N   1 
ATOM   1096 C CA  . TYR B 1 21  ? 13.88100  18.00100  21.49100  1.000 19.56926 ? 18  TYR B CA  1 
ATOM   1097 C C   . TYR B 1 21  ? 14.40700  19.30600  20.88200  1.000 19.54470 ? 18  TYR B C   1 
ATOM   1098 O O   . TYR B 1 21  ? 15.54900  19.67200  21.13900  1.000 24.24535 ? 18  TYR B O   1 
ATOM   1099 C CB  . TYR B 1 21  ? 14.13900  16.78000  20.61300  1.000 19.32369 ? 18  TYR B CB  1 
ATOM   1100 C CG  . TYR B 1 21  ? 13.88400  15.48400  21.38400  1.000 18.55276 ? 18  TYR B CG  1 
ATOM   1101 C CD1 . TYR B 1 21  ? 14.82100  15.00200  22.27600  1.000 20.70276 ? 18  TYR B CD1 1 
ATOM   1102 C CD2 . TYR B 1 21  ? 12.68300  14.80800  21.24600  1.000 19.88006 ? 18  TYR B CD2 1 
ATOM   1103 C CE1 . TYR B 1 21  ? 14.59400  13.81900  23.02800  1.000 20.08697 ? 18  TYR B CE1 1 
ATOM   1104 C CE2 . TYR B 1 21  ? 12.44400  13.64300  21.96800  1.000 21.11013 ? 18  TYR B CE2 1 
ATOM   1105 C CZ  . TYR B 1 21  ? 13.39700  13.17900  22.87700  1.000 20.31362 ? 18  TYR B CZ  1 
ATOM   1106 O OH  . TYR B 1 21  ? 13.15400  11.99300  23.60400  1.000 23.10840 ? 18  TYR B OH  1 
ATOM   1107 N N   . ASP B 1 22  ? 13.57200  20.04500  20.13500  1.000 22.28277 ? 19  ASP B N   1 
ATOM   1108 C CA  . ASP B 1 22  ? 14.02100  21.35100  19.63600  1.000 22.62880 ? 19  ASP B CA  1 
ATOM   1109 C C   . ASP B 1 22  ? 14.29500  22.30700  20.79300  1.000 24.76740 ? 19  ASP B C   1 
ATOM   1110 O O   . ASP B 1 22  ? 15.31900  23.00300  20.80300  1.000 28.06653 ? 19  ASP B O   1 
ATOM   1111 C CB  . ASP B 1 22  ? 12.97300  21.93800  18.68100  1.000 29.56139 ? 19  ASP B CB  1 
ATOM   1112 C CG  . ASP B 1 22  ? 12.94400  21.25100  17.33800  1.000 31.32657 ? 19  ASP B CG  1 
ATOM   1113 O OD1 . ASP B 1 22  ? 13.86100  20.48000  16.99800  1.000 32.34666 ? 19  ASP B OD1 1 
ATOM   1114 O OD2 . ASP B 1 22  ? 11.97500  21.49300  16.58000  1.000 37.72854 ? 19  ASP B OD2 1 
ATOM   1115 N N   . ALA B 1 23  ? 13.41300  22.33300  21.79300  1.000 21.18409 ? 20  ALA B N   1 
ATOM   1116 C CA  . ALA B 1 23  ? 13.60500  23.21400  22.95100  1.000 22.54339 ? 20  ALA B CA  1 
ATOM   1117 C C   . ALA B 1 23  ? 14.82700  22.80300  23.74400  1.000 23.83349 ? 20  ALA B C   1 
ATOM   1118 O O   . ALA B 1 23  ? 15.54600  23.65000  24.27900  1.000 24.83498 ? 20  ALA B O   1 
ATOM   1119 C CB  . ALA B 1 23  ? 12.37400  23.18900  23.85300  1.000 24.59761 ? 20  ALA B CB  1 
ATOM   1120 N N   . MET B 1 24  ? 15.12000  21.52100  23.77700  1.000 21.67068 ? 21  MET B N   1 
ATOM   1121 C CA  . MET B 1 24  ? 16.30600  21.05400  24.43500  1.000 19.56786 ? 21  MET B CA  1 
ATOM   1122 C C   . MET B 1 24  ? 17.53400  21.59900  23.73900  1.000 22.48371 ? 21  MET B C   1 
ATOM   1123 O O   . MET B 1 24  ? 18.39300  22.11200  24.35500  1.000 23.37831 ? 21  MET B O   1 
ATOM   1124 C CB  . MET B 1 24  ? 16.34900  19.53100  24.44700  1.000 23.37708 ? 21  MET B CB  1 
ATOM   1125 C CG  . MET B 1 24  ? 17.38300  18.97200  25.35900  1.000 24.24248 ? 21  MET B CG  1 
ATOM   1126 S SD  . MET B 1 24  ? 16.87200  19.06800  27.06700  1.000 26.41879 ? 21  MET B SD  1 
ATOM   1127 C CE  . MET B 1 24  ? 15.48300  17.94800  27.20500  1.000 29.11181 ? 21  MET B CE  1 
ATOM   1128 N N   . ASN B 1 25  ? 17.59800  21.47400  22.43800  1.000 21.92990 ? 22  ASN B N   1 
ATOM   1129 C CA  . ASN B 1 25  ? 18.74300  21.98400  21.72200  1.000 22.13658 ? 22  ASN B CA  1 
ATOM   1130 C C   . ASN B 1 25  ? 18.84800  23.50800  21.84800  1.000 23.76127 ? 22  ASN B C   1 
ATOM   1131 O O   . ASN B 1 25  ? 19.91500  24.01900  21.83500  1.000 24.30731 ? 22  ASN B O   1 
ATOM   1132 C CB  . ASN B 1 25  ? 18.71100  21.59300  20.26600  1.000 25.51710 ? 22  ASN B CB  1 
ATOM   1133 C CG  . ASN B 1 25  ? 19.22800  20.20600  20.02500  1.000 24.92915 ? 22  ASN B CG  1 
ATOM   1134 O OD1 . ASN B 1 25  ? 20.13200  19.77300  20.65700  1.000 26.99499 ? 22  ASN B OD1 1 
ATOM   1135 N ND2 . ASN B 1 25  ? 18.63300  19.52500  19.10100  1.000 26.23264 ? 22  ASN B ND2 1 
ATOM   1136 N N   . GLU B 1 26  ? 17.71400  24.19100  21.91800  1.000 21.78218 ? 23  GLU B N   1 
ATOM   1137 C CA  . GLU B 1 26  ? 17.68300  25.64600  22.10400  1.000 23.52280 ? 23  GLU B CA  1 
ATOM   1138 C C   . GLU B 1 26  ? 18.04100  26.07200  23.52200  1.000 26.73582 ? 23  GLU B C   1 
ATOM   1139 O O   . GLU B 1 26  ? 18.32700  27.25900  23.75200  1.000 26.44953 ? 23  GLU B O   1 
ATOM   1140 C CB  . GLU B 1 26  ? 16.29700  26.18800  21.77300  1.000 24.56590 ? 23  GLU B CB  1 
ATOM   1141 C CG  . GLU B 1 26  ? 15.89400  25.98200  20.33000  1.000 31.05155 ? 23  GLU B CG  1 
ATOM   1142 C CD  . GLU B 1 26  ? 14.40800  26.13500  20.12300  1.000 38.13214 ? 23  GLU B CD  1 
ATOM   1143 O OE1 . GLU B 1 26  ? 13.69700  26.40900  21.10500  1.000 33.89947 ? 23  GLU B OE1 1 
ATOM   1144 O OE2 . GLU B 1 26  ? 13.95700  25.98200  18.96800  1.000 45.15721 ? 23  GLU B OE2 1 
ATOM   1145 N N   . GLY B 1 27  ? 18.04100  25.14000  24.47500  1.000 27.95298 ? 24  GLY B N   1 
ATOM   1146 C CA  . GLY B 1 27  ? 18.14100  25.48200  25.87900  1.000 24.60715 ? 24  GLY B CA  1 
ATOM   1147 C C   . GLY B 1 27  ? 16.94100  26.22300  26.43100  1.000 28.18730 ? 24  GLY B C   1 
ATOM   1148 O O   . GLY B 1 27  ? 17.08600  27.02000  27.36300  1.000 27.91603 ? 24  GLY B O   1 
ATOM   1149 N N   . ASP B 1 28  ? 15.74300  25.96700  25.90500  1.000 26.65629 ? 25  ASP B N   1 
ATOM   1150 C CA  . ASP B 1 28  ? 14.55500  26.74400  26.23500  1.000 24.44313 ? 25  ASP B CA  1 
ATOM   1151 C C   . ASP B 1 28  ? 13.73400  26.00500  27.28200  1.000 28.06659 ? 25  ASP B C   1 
ATOM   1152 O O   . ASP B 1 28  ? 12.82300  25.24800  26.95200  1.000 27.48642 ? 25  ASP B O   1 
ATOM   1153 C CB  . ASP B 1 28  ? 13.71600  26.99900  24.98800  1.000 25.85341 ? 25  ASP B CB  1 
ATOM   1154 C CG  . ASP B 1 28  ? 12.60600  28.00300  25.23100  1.000 39.58114 ? 25  ASP B CG  1 
ATOM   1155 O OD1 . ASP B 1 28  ? 12.09900  28.05700  26.37400  1.000 40.47924 ? 25  ASP B OD1 1 
ATOM   1156 O OD2 . ASP B 1 28  ? 12.24700  28.73500  24.28200  1.000 42.58154 ? 25  ASP B OD2 1 
ATOM   1157 N N   . MET B 1 29  ? 14.07200  26.21000  28.52500  1.000 26.98109 ? 26  MET B N   1 
ATOM   1158 C CA  . MET B 1 29  ? 13.37900  25.51300  29.55500  1.000 26.50970 ? 26  MET B CA  1 
ATOM   1159 C C   . MET B 1 29  ? 11.91600  25.85700  29.77000  1.000 29.39046 ? 26  MET B C   1 
ATOM   1160 O O   . MET B 1 29  ? 11.19000  25.03200  30.22900  1.000 30.02563 ? 26  MET B O   1 
ATOM   1161 C CB  . MET B 1 29  ? 14.18900  25.49900  30.81000  1.000 29.73181 ? 26  MET B CB  1 
ATOM   1162 C CG  . MET B 1 29  ? 15.43200  24.69600  30.57700  1.000 28.92576 ? 26  MET B CG  1 
ATOM   1163 S SD  . MET B 1 29  ? 16.21100  24.38900  32.10200  1.000 36.72582 ? 26  MET B SD  1 
ATOM   1164 C CE  . MET B 1 29  ? 15.02200  23.25500  32.76200  1.000 30.89730 ? 26  MET B CE  1 
ATOM   1165 N N   . GLU B 1 30  ? 11.47000  27.05200  29.41000  1.000 32.78281 ? 27  GLU B N   1 
ATOM   1166 C CA  . GLU B 1 30  ? 10.04500  27.31800  29.60100  1.000 34.96240 ? 27  GLU B CA  1 
ATOM   1167 C C   . GLU B 1 30  ? 9.21300   26.44000  28.67600  1.000 32.71341 ? 27  GLU B C   1 
ATOM   1168 O O   . GLU B 1 30  ? 8.19300   25.97900  29.07800  1.000 33.97758 ? 27  GLU B O   1 
ATOM   1169 C CB  . GLU B 1 30  ? 9.58400   28.79200  29.56200  1.000 48.02380 ? 27  GLU B CB  1 
ATOM   1170 C CG  . GLU B 1 30  ? 8.07500   28.95000  29.90600  1.000 48.54710 ? 27  GLU B CG  1 
ATOM   1171 C CD  . GLU B 1 30  ? 7.70700   29.45000  31.32800  1.000 56.63434 ? 27  GLU B CD  1 
ATOM   1172 O OE1 . GLU B 1 30  ? 7.81400   28.70400  32.31700  1.000 54.86597 ? 27  GLU B OE1 1 
ATOM   1173 O OE2 . GLU B 1 30  ? 7.20300   30.59300  31.46900  1.000 53.93424 ? 27  GLU B OE2 1 
ATOM   1174 N N   . LYS B 1 31  ? 9.67800   26.17600  27.47300  1.000 32.06586 ? 28  LYS B N   1 
ATOM   1175 C CA  . LYS B 1 31  ? 8.94900   25.27100  26.60900  1.000 26.74506 ? 28  LYS B CA  1 
ATOM   1176 C C   . LYS B 1 31  ? 8.93700   23.87100  27.16200  1.000 30.06069 ? 28  LYS B C   1 
ATOM   1177 O O   . LYS B 1 31  ? 7.95300   23.22300  27.06800  1.000 30.13647 ? 28  LYS B O   1 
ATOM   1178 C CB  . LYS B 1 31  ? 9.53200   25.19100  25.21700  1.000 30.96674 ? 28  LYS B CB  1 
ATOM   1179 C CG  . LYS B 1 31  ? 9.58300   26.47400  24.43400  1.000 38.90473 ? 28  LYS B CG  1 
ATOM   1180 C CD  . LYS B 1 31  ? 9.44300   26.23300  22.92700  1.000 50.58048 ? 28  LYS B CD  1 
ATOM   1181 C CE  . LYS B 1 31  ? 10.68800  25.85400  22.09800  1.000 46.01960 ? 28  LYS B CE  1 
ATOM   1182 N NZ  . LYS B 1 31  ? 10.43800  24.65600  21.17200  1.000 47.86870 ? 28  LYS B NZ  1 
ATOM   1183 N N   . LEU B 1 32  ? 10.04900  23.38700  27.69900  1.000 26.07370 ? 29  LEU B N   1 
ATOM   1184 C CA  . LEU B 1 32  ? 10.04500  22.04500  28.25100  1.000 25.37063 ? 29  LEU B CA  1 
ATOM   1185 C C   . LEU B 1 32  ? 9.01100   21.92100  29.35200  1.000 25.44286 ? 29  LEU B C   1 
ATOM   1186 O O   . LEU B 1 32  ? 8.26000   21.00800  29.38600  1.000 25.74515 ? 29  LEU B O   1 
ATOM   1187 C CB  . LEU B 1 32  ? 11.40000  21.68300  28.82400  1.000 21.09789 ? 29  LEU B CB  1 
ATOM   1188 C CG  . LEU B 1 32  ? 12.53300  21.66000  27.84600  1.000 23.27974 ? 29  LEU B CG  1 
ATOM   1189 C CD1 . LEU B 1 32  ? 13.83200  21.40800  28.57300  1.000 22.77071 ? 29  LEU B CD1 1 
ATOM   1190 C CD2 . LEU B 1 32  ? 12.28100  20.62700  26.77000  1.000 23.29647 ? 29  LEU B CD2 1 
ATOM   1191 N N   . ARG B 1 33  ? 8.99900   22.88400  30.24300  1.000 25.91649 ? 30  ARG B N   1 
ATOM   1192 C CA  . ARG B 1 33  ? 8.09200   22.93900  31.38200  1.000 25.65514 ? 30  ARG B CA  1 
ATOM   1193 C C   . ARG B 1 33  ? 6.61300   22.86200  31.04100  1.000 27.90796 ? 30  ARG B C   1 
ATOM   1194 O O   . ARG B 1 33  ? 5.84600   22.15900  31.63100  1.000 27.20551 ? 30  ARG B O   1 
ATOM   1195 C CB  . ARG B 1 33  ? 8.35600   24.23800  32.10800  1.000 30.92788 ? 30  ARG B CB  1 
ATOM   1196 C CG  . ARG B 1 33  ? 7.80000   24.34400  33.48100  1.000 43.04651 ? 30  ARG B CG  1 
ATOM   1197 C CD  . ARG B 1 33  ? 8.24000   25.68200  34.06200  1.000 52.24366 ? 30  ARG B CD  1 
ATOM   1198 N NE  . ARG B 1 33  ? 9.44300   25.62900  34.88000  1.000 54.79673 ? 30  ARG B NE  1 
ATOM   1199 C CZ  . ARG B 1 33  ? 10.56300  26.32000  34.65400  1.000 56.04258 ? 30  ARG B CZ  1 
ATOM   1200 N NH1 . ARG B 1 33  ? 10.68800  27.10900  33.60400  1.000 52.37752 ? 30  ARG B NH1 1 
ATOM   1201 N NH2 . ARG B 1 33  ? 11.57700  26.21000  35.49100  1.000 60.20684 ? 30  ARG B NH2 1 
ATOM   1202 N N   . SER B 1 34  ? 6.25100   23.49100  29.94600  1.000 26.59663 ? 31  SER B N   1 
ATOM   1203 C CA  . SER B 1 34  ? 4.89400   23.49400  29.47000  1.000 28.85476 ? 31  SER B CA  1 
ATOM   1204 C C   . SER B 1 34  ? 4.41300   22.18800  28.84600  1.000 34.11191 ? 31  SER B C   1 
ATOM   1205 O O   . SER B 1 34  ? 3.25600   22.07500  28.60300  1.000 33.91328 ? 31  SER B O   1 
ATOM   1206 C CB  . SER B 1 34  ? 4.74900   24.60100  28.43800  1.000 30.37084 ? 31  SER B CB  1 
ATOM   1207 O OG  . SER B 1 34  ? 5.21300   24.17800  27.19900  1.000 34.21668 ? 31  SER B OG  1 
ATOM   1208 N N   . LEU B 1 35  ? 5.29400   21.22300  28.56700  1.000 28.61584 ? 32  LEU B N   1 
ATOM   1209 C CA  . LEU B 1 35  ? 4.92300   19.94700  27.97200  1.000 31.12103 ? 32  LEU B CA  1 
ATOM   1210 C C   . LEU B 1 35  ? 4.72500   18.82100  28.98700  1.000 28.77057 ? 32  LEU B C   1 
ATOM   1211 O O   . LEU B 1 35  ? 4.35600   17.71400  28.59000  1.000 28.89723 ? 32  LEU B O   1 
ATOM   1212 C CB  . LEU B 1 35  ? 5.98800   19.54100  26.94700  1.000 31.88338 ? 32  LEU B CB  1 
ATOM   1213 C CG  . LEU B 1 35  ? 6.16200   20.54700  25.80000  1.000 30.02593 ? 32  LEU B CG  1 
ATOM   1214 C CD1 . LEU B 1 35  ? 7.36000   20.23300  24.91700  1.000 33.42149 ? 32  LEU B CD1 1 
ATOM   1215 C CD2 . LEU B 1 35  ? 4.87100   20.58800  24.97800  1.000 37.12222 ? 32  LEU B CD2 1 
ATOM   1216 N N   . VAL B 1 36  ? 4.91900   19.08400  30.27900  1.000 28.97529 ? 33  VAL B N   1 
ATOM   1217 C CA  . VAL B 1 36  ? 4.96100   18.04100  31.30200  1.000 25.43565 ? 33  VAL B CA  1 
ATOM   1218 C C   . VAL B 1 36  ? 3.87900   18.28100  32.34900  1.000 27.46529 ? 33  VAL B C   1 
ATOM   1219 O O   . VAL B 1 36  ? 3.80800   19.36600  32.93600  1.000 30.14110 ? 33  VAL B O   1 
ATOM   1220 C CB  . VAL B 1 36  ? 6.34900   18.00400  31.96200  1.000 26.66054 ? 33  VAL B CB  1 
ATOM   1221 C CG1 . VAL B 1 36  ? 6.39600   16.96000  33.04900  1.000 26.02407 ? 33  VAL B CG1 1 
ATOM   1222 C CG2 . VAL B 1 36  ? 7.42400   17.74500  30.90700  1.000 26.34719 ? 33  VAL B CG2 1 
ATOM   1223 N N   . ASP B 1 37  ? 3.06800   17.25900  32.60400  1.000 27.63208 ? 34  ASP B N   1 
ATOM   1224 C CA  . ASP B 1 37  ? 2.07200   17.34100  33.66300  1.000 32.35269 ? 34  ASP B CA  1 
ATOM   1225 C C   . ASP B 1 37  ? 2.76100   17.54200  35.00800  1.000 32.78624 ? 34  ASP B C   1 
ATOM   1226 O O   . ASP B 1 37  ? 3.83900   16.98200  35.24700  1.000 28.80620 ? 34  ASP B O   1 
ATOM   1227 C CB  . ASP B 1 37  ? 1.23700   16.07000  33.68200  1.000 34.26500 ? 34  ASP B CB  1 
ATOM   1228 C CG  . ASP B 1 37  ? 0.05100   16.17400  34.61400  1.000 39.86533 ? 34  ASP B CG  1 
ATOM   1229 O OD1 . ASP B 1 37  ? 0.21300   15.86400  35.80500  1.000 43.43042 ? 34  ASP B OD1 1 
ATOM   1230 O OD2 . ASP B 1 37  ? -1.03500  16.58000  34.15900  1.000 49.63789 ? 34  ASP B OD2 1 
ATOM   1231 N N   . PRO B 1 38  ? 2.18900   18.32100  35.92800  1.000 35.92958 ? 35  PRO B N   1 
ATOM   1232 C CA  . PRO B 1 38  ? 2.90200   18.54100  37.19500  1.000 37.75770 ? 35  PRO B CA  1 
ATOM   1233 C C   . PRO B 1 38  ? 3.19300   17.26100  37.96400  1.000 32.46752 ? 35  PRO B C   1 
ATOM   1234 O O   . PRO B 1 38  ? 4.16500   17.22600  38.72500  1.000 35.72390 ? 35  PRO B O   1 
ATOM   1235 C CB  . PRO B 1 38  ? 1.96600   19.48100  37.97400  1.000 41.81445 ? 35  PRO B CB  1 
ATOM   1236 C CG  . PRO B 1 38  ? 1.12300   20.13100  36.92700  1.000 37.11517 ? 35  PRO B CG  1 
ATOM   1237 C CD  . PRO B 1 38  ? 0.93200   19.10100  35.86400  1.000 35.11446 ? 35  PRO B CD  1 
ATOM   1238 N N   . ASP B 1 39  ? 2.39700   16.20800  37.79200  1.000 31.31397 ? 36  ASP B N   1 
ATOM   1239 C CA  . ASP B 1 39  ? 2.58700   14.96300  38.52500  1.000 34.20088 ? 36  ASP B CA  1 
ATOM   1240 C C   . ASP B 1 39  ? 3.30200   13.89700  37.70100  1.000 27.64653 ? 36  ASP B C   1 
ATOM   1241 O O   . ASP B 1 39  ? 3.21600   12.71800  38.02600  1.000 31.54559 ? 36  ASP B O   1 
ATOM   1242 C CB  . ASP B 1 39  ? 1.23800   14.44000  39.02100  1.000 38.97366 ? 36  ASP B CB  1 
ATOM   1243 C CG  . ASP B 1 39  ? 0.55700   15.41300  39.97000  1.000 46.16188 ? 36  ASP B CG  1 
ATOM   1244 O OD1 . ASP B 1 39  ? 0.52200   16.62000  39.65500  1.000 49.19679 ? 36  ASP B OD1 1 
ATOM   1245 O OD2 . ASP B 1 39  ? 0.05700   14.97600  41.02700  1.000 51.08505 ? 36  ASP B OD2 1 
ATOM   1246 N N   . ALA B 1 40  ? 4.02100   14.29700  36.65000  1.000 29.30884 ? 37  ALA B N   1 
ATOM   1247 C CA  . ALA B 1 40  ? 4.76400   13.32400  35.85300  1.000 26.73382 ? 37  ALA B CA  1 
ATOM   1248 C C   . ALA B 1 40  ? 5.87300   12.66700  36.66600  1.000 21.45617 ? 37  ALA B C   1 
ATOM   1249 O O   . ALA B 1 40  ? 6.42200   13.24000  37.61300  1.000 28.66829 ? 37  ALA B O   1 
ATOM   1250 C CB  . ALA B 1 40  ? 5.35900   14.00800  34.61700  1.000 25.65017 ? 37  ALA B CB  1 
ATOM   1251 N N   . SER B 1 41  ? 6.20900   11.45600  36.23800  1.000 26.83664 ? 38  SER B N   1 
ATOM   1252 C CA  A SER B 1 41  ? 7.38000   10.69300  36.97700  0.466 22.63356 ? 38  SER B CA  1 
ATOM   1253 C CA  B SER B 1 41  ? 7.37500   10.67800  36.96700  0.534 22.61947 ? 38  SER B CA  1 
ATOM   1254 C C   . SER B 1 41  ? 8.43700   10.37600  35.73200  1.000 22.36258 ? 38  SER B C   1 
ATOM   1255 O O   . SER B 1 41  ? 8.15100   10.13000  34.51600  1.000 25.30782 ? 38  SER B O   1 
ATOM   1256 C CB  A SER B 1 41  ? 6.88800   9.39800   37.57900  0.466 25.06451 ? 38  SER B CB  1 
ATOM   1257 C CB  B SER B 1 41  ? 6.86000   9.33500   37.40800  0.534 24.82057 ? 38  SER B CB  1 
ATOM   1258 O OG  A SER B 1 41  ? 6.23400   8.61700   36.63600  0.466 29.65160 ? 38  SER B OG  1 
ATOM   1259 O OG  B SER B 1 41  ? 6.28100   9.43600   38.67700  0.534 28.92888 ? 38  SER B OG  1 
ATOM   1260 N N   . PHE B 1 42  ? 9.64600   10.64500  36.06900  1.000 22.63233 ? 39  PHE B N   1 
ATOM   1261 C CA  . PHE B 1 42  ? 10.75500  10.50700  35.13300  1.000 24.70122 ? 39  PHE B CA  1 
ATOM   1262 C C   . PHE B 1 42  ? 11.66500  9.41500   35.65300  1.000 23.06900 ? 39  PHE B C   1 
ATOM   1263 O O   . PHE B 1 42  ? 12.21900  9.55100   36.75100  1.000 25.12227 ? 39  PHE B O   1 
ATOM   1264 C CB  . PHE B 1 42  ? 11.48900  11.84700  35.00200  1.000 23.44332 ? 39  PHE B CB  1 
ATOM   1265 C CG  . PHE B 1 42  ? 10.67400  12.86700  34.30000  1.000 25.06351 ? 39  PHE B CG  1 
ATOM   1266 C CD1 . PHE B 1 42  ? 9.74300   13.62000  34.98600  1.000 23.28626 ? 39  PHE B CD1 1 
ATOM   1267 C CD2 . PHE B 1 42  ? 10.80200  13.02400  32.93300  1.000 21.70891 ? 39  PHE B CD2 1 
ATOM   1268 C CE1 . PHE B 1 42  ? 8.96200   14.54200  34.31400  1.000 22.98476 ? 39  PHE B CE1 1 
ATOM   1269 C CE2 . PHE B 1 42  ? 9.99600   13.92900  32.26700  1.000 25.95167 ? 39  PHE B CE2 1 
ATOM   1270 C CZ  . PHE B 1 42  ? 9.09500   14.68500  32.96800  1.000 21.59791 ? 39  PHE B CZ  1 
ATOM   1271 N N   . VAL B 1 43  ? 11.81100  8.33500   34.89400  1.000 21.89506 ? 40  VAL B N   1 
ATOM   1272 C CA  . VAL B 1 43  ? 12.54900  7.21700   35.33600  1.000 22.03856 ? 40  VAL B CA  1 
ATOM   1273 C C   . VAL B 1 43  ? 13.85300  7.00300   34.57600  1.000 23.89084 ? 40  VAL B C   1 
ATOM   1274 O O   . VAL B 1 43  ? 13.86400  7.00900   33.38900  1.000 23.72798 ? 40  VAL B O   1 
ATOM   1275 C CB  . VAL B 1 43  ? 11.73500  5.94700   35.11200  1.000 24.12414 ? 40  VAL B CB  1 
ATOM   1276 C CG1 . VAL B 1 43  ? 12.47200  4.74600   35.66100  1.000 23.83576 ? 40  VAL B CG1 1 
ATOM   1277 C CG2 . VAL B 1 43  ? 10.35800  6.07300   35.69700  1.000 24.49367 ? 40  VAL B CG2 1 
ATOM   1278 N N   . ASP B 1 44  ? 14.93600  6.85000   35.30200  1.000 21.65852 ? 41  ASP B N   1 
ATOM   1279 C CA  . ASP B 1 44  ? 16.24900  6.50300   34.75200  1.000 22.52438 ? 41  ASP B CA  1 
ATOM   1280 C C   . ASP B 1 44  ? 16.30100  4.98600   34.86300  1.000 23.54441 ? 41  ASP B C   1 
ATOM   1281 O O   . ASP B 1 44  ? 16.52200  4.44800   35.94500  1.000 22.97165 ? 41  ASP B O   1 
ATOM   1282 C CB  . ASP B 1 44  ? 17.35900  7.19100   35.54200  1.000 22.64268 ? 41  ASP B CB  1 
ATOM   1283 C CG  . ASP B 1 44  ? 18.76300  6.90600   35.00500  1.000 28.57645 ? 41  ASP B CG  1 
ATOM   1284 O OD1 . ASP B 1 44  ? 18.97400  5.80700   34.45600  1.000 28.60828 ? 41  ASP B OD1 1 
ATOM   1285 O OD2 . ASP B 1 44  ? 19.66900  7.77900   35.18200  1.000 31.43811 ? 41  ASP B OD2 1 
ATOM   1286 N N   . ALA B 1 45  ? 16.06300  4.28400   33.74100  1.000 23.37118 ? 42  ALA B N   1 
ATOM   1287 C CA  . ALA B 1 45  ? 15.90300  2.82900   33.81100  1.000 25.42283 ? 42  ALA B CA  1 
ATOM   1288 C C   . ALA B 1 45  ? 17.13500  2.14900   34.37600  1.000 24.74943 ? 42  ALA B C   1 
ATOM   1289 O O   . ALA B 1 45  ? 17.01400  1.21100   35.17800  1.000 27.69038 ? 42  ALA B O   1 
ATOM   1290 C CB  . ALA B 1 45  ? 15.59500  2.26200   32.42100  1.000 29.69877 ? 42  ALA B CB  1 
ATOM   1291 N N   . ARG B 1 46  ? 18.30200  2.53600   33.93900  1.000 24.74617 ? 43  ARG B N   1 
ATOM   1292 C CA  . ARG B 1 46  ? 19.52200  1.89800   34.34400  1.000 25.16606 ? 43  ARG B CA  1 
ATOM   1293 C C   . ARG B 1 46  ? 19.81500  1.94700   35.83100  1.000 25.84077 ? 43  ARG B C   1 
ATOM   1294 O O   . ARG B 1 46  ? 20.27200  1.00400   36.37400  1.000 30.26435 ? 43  ARG B O   1 
ATOM   1295 C CB  . ARG B 1 46  ? 20.66600  2.46900   33.53000  1.000 31.80784 ? 43  ARG B CB  1 
ATOM   1296 C CG  . ARG B 1 46  ? 21.82900  1.53200   33.36100  1.000 33.13246 ? 43  ARG B CG  1 
ATOM   1297 C CD  . ARG B 1 46  ? 22.47600  1.57500   31.99800  1.000 30.47288 ? 43  ARG B CD  1 
ATOM   1298 N NE  . ARG B 1 46  ? 21.90000  0.65700   31.05500  1.000 27.19153 ? 43  ARG B NE  1 
ATOM   1299 C CZ  . ARG B 1 46  ? 21.82200  -0.65000  31.21600  1.000 26.49508 ? 43  ARG B CZ  1 
ATOM   1300 N NH1 . ARG B 1 46  ? 22.29300  -1.23100  32.27200  1.000 26.39533 ? 43  ARG B NH1 1 
ATOM   1301 N NH2 . ARG B 1 46  ? 21.24900  -1.35100  30.29400  1.000 25.90559 ? 43  ARG B NH2 1 
ATOM   1302 N N   . THR B 1 47  ? 19.50500  3.05700   36.46700  1.000 27.81140 ? 44  THR B N   1 
ATOM   1303 C CA  . THR B 1 47  ? 19.74300  3.24900   37.89200  1.000 22.14432 ? 44  THR B CA  1 
ATOM   1304 C C   . THR B 1 47  ? 18.51100  3.01200   38.75700  1.000 22.99739 ? 44  THR B C   1 
ATOM   1305 O O   . THR B 1 47  ? 18.63100  3.00800   39.99300  1.000 25.11063 ? 44  THR B O   1 
ATOM   1306 C CB  . THR B 1 47  ? 20.22800  4.67300   38.15800  1.000 28.16951 ? 44  THR B CB  1 
ATOM   1307 O OG1 . THR B 1 47  ? 19.17300  5.58500   37.79100  1.000 26.85468 ? 44  THR B OG1 1 
ATOM   1308 C CG2 . THR B 1 47  ? 21.49800  5.01100   37.36500  1.000 33.02621 ? 44  THR B CG2 1 
ATOM   1309 N N   . ASN B 1 48  ? 17.34300  2.81700   38.16300  1.000 23.41122 ? 45  ASN B N   1 
ATOM   1310 C CA  . ASN B 1 48  ? 16.07000  2.63900   38.85800  1.000 25.34509 ? 45  ASN B CA  1 
ATOM   1311 C C   . ASN B 1 48  ? 15.64600  3.89400   39.60200  1.000 21.64687 ? 45  ASN B C   1 
ATOM   1312 O O   . ASN B 1 48  ? 14.76100  3.83400   40.45700  1.000 23.02083 ? 45  ASN B O   1 
ATOM   1313 C CB  . ASN B 1 48  ? 16.07600  1.46900   39.84900  1.000 22.35294 ? 45  ASN B CB  1 
ATOM   1314 C CG  . ASN B 1 48  ? 16.44700  0.15200   39.20900  1.000 31.62361 ? 45  ASN B CG  1 
ATOM   1315 O OD1 . ASN B 1 48  ? 17.58800  -0.31000  39.32300  1.000 35.50084 ? 45  ASN B OD1 1 
ATOM   1316 N ND2 . ASN B 1 48  ? 15.49600  -0.45600  38.53600  1.000 34.95457 ? 45  ASN B ND2 1 
ATOM   1317 N N   . GLN B 1 49  ? 16.08300  5.05400   39.19000  1.000 22.72041 ? 46  GLN B N   1 
ATOM   1318 C CA  . GLN B 1 49  ? 15.82800  6.27200   39.94600  1.000 23.12696 ? 46  GLN B CA  1 
ATOM   1319 C C   . GLN B 1 49  ? 14.59700  6.87500   39.36100  1.000 25.53165 ? 46  GLN B C   1 
ATOM   1320 O O   . GLN B 1 49  ? 14.43000  6.85200   38.19700  1.000 25.55260 ? 46  GLN B O   1 
ATOM   1321 C CB  . GLN B 1 49  ? 16.95100  7.32800   39.95500  1.000 23.77614 ? 46  GLN B CB  1 
ATOM   1322 C CG  . GLN B 1 49  ? 18.11200  6.96300   40.85500  1.000 24.83851 ? 46  GLN B CG  1 
ATOM   1323 C CD  . GLN B 1 49  ? 19.40600  7.66900   40.54200  1.000 31.17312 ? 46  GLN B CD  1 
ATOM   1324 O OE1 . GLN B 1 49  ? 19.89200  7.64900   39.43800  1.000 25.39470 ? 46  GLN B OE1 1 
ATOM   1325 N NE2 . GLN B 1 49  ? 19.99100  8.25200   41.55000  1.000 29.75438 ? 46  GLN B NE2 1 
ATOM   1326 N N   . VAL B 1 50  ? 13.76600  7.43800   40.20700  1.000 23.14753 ? 47  VAL B N   1 
ATOM   1327 C CA  . VAL B 1 50  ? 12.51500  8.03100   39.75900  1.000 20.09061 ? 47  VAL B CA  1 
ATOM   1328 C C   . VAL B 1 50  ? 12.46400  9.46400   40.28600  1.000 22.01029 ? 47  VAL B C   1 
ATOM   1329 O O   . VAL B 1 50  ? 12.71500  9.71700   41.46900  1.000 25.35204 ? 47  VAL B O   1 
ATOM   1330 C CB  . VAL B 1 50  ? 11.27900  7.21600   40.19000  1.000 22.46839 ? 47  VAL B CB  1 
ATOM   1331 C CG1 . VAL B 1 50  ? 9.98100   7.89500   39.66800  1.000 24.07645 ? 47  VAL B CG1 1 
ATOM   1332 C CG2 . VAL B 1 50  ? 11.39100  5.77600   39.67100  1.000 24.96868 ? 47  VAL B CG2 1 
ATOM   1333 N N   . TYR B 1 51  ? 12.13800  10.40300  39.39700  1.000 22.47114 ? 48  TYR B N   1 
ATOM   1334 C CA  . TYR B 1 51  ? 12.13600  11.82300  39.72900  1.000 20.77833 ? 48  TYR B CA  1 
ATOM   1335 C C   . TYR B 1 51  ? 10.78900  12.44900  39.41500  1.000 21.95492 ? 48  TYR B C   1 
ATOM   1336 O O   . TYR B 1 51  ? 10.08500  12.02100  38.50200  1.000 23.36050 ? 48  TYR B O   1 
ATOM   1337 C CB  . TYR B 1 51  ? 13.21900  12.53900  38.93600  1.000 18.64692 ? 48  TYR B CB  1 
ATOM   1338 C CG  . TYR B 1 51  ? 14.59800  12.01000  39.22200  1.000 23.27171 ? 48  TYR B CG  1 
ATOM   1339 C CD1 . TYR B 1 51  ? 15.25900  12.35300  40.37900  1.000 26.23021 ? 48  TYR B CD1 1 
ATOM   1340 C CD2 . TYR B 1 51  ? 15.22300  11.14700  38.34100  1.000 24.36692 ? 48  TYR B CD2 1 
ATOM   1341 C CE1 . TYR B 1 51  ? 16.51800  11.85500  40.65600  1.000 26.00591 ? 48  TYR B CE1 1 
ATOM   1342 C CE2 . TYR B 1 51  ? 16.49100  10.63400  38.60600  1.000 26.01244 ? 48  TYR B CE2 1 
ATOM   1343 C CZ  . TYR B 1 51  ? 17.12500  10.98800  39.75500  1.000 24.59189 ? 48  TYR B CZ  1 
ATOM   1344 O OH  . TYR B 1 51  ? 18.37900  10.47900  39.99100  1.000 28.14276 ? 48  TYR B OH  1 
ATOM   1345 N N   . ASP B 1 52  ? 10.45300  13.50600  40.14800  1.000 22.35729 ? 49  ASP B N   1 
ATOM   1346 C CA  . ASP B 1 52  ? 9.26900   14.26500  39.79900  1.000 22.23218 ? 49  ASP B CA  1 
ATOM   1347 C C   . ASP B 1 52  ? 9.68400   15.35200  38.80600  1.000 23.31732 ? 49  ASP B C   1 
ATOM   1348 O O   . ASP B 1 52  ? 10.85800  15.48000  38.43400  1.000 22.72476 ? 49  ASP B O   1 
ATOM   1349 C CB  . ASP B 1 52  ? 8.57500   14.84200  41.04900  1.000 28.86634 ? 49  ASP B CB  1 
ATOM   1350 C CG  . ASP B 1 52  ? 9.44700   15.79100  41.87300  1.000 31.62043 ? 49  ASP B CG  1 
ATOM   1351 O OD1 . ASP B 1 52  ? 10.39800  16.40300  41.37200  1.000 26.17215 ? 49  ASP B OD1 1 
ATOM   1352 O OD2 . ASP B 1 52  ? 9.13900   15.95000  43.07200  1.000 34.36426 ? 49  ASP B OD2 1 
ATOM   1353 N N   . LYS B 1 53  ? 8.69300   16.16200  38.39100  1.000 23.42824 ? 50  LYS B N   1 
ATOM   1354 C CA  . LYS B 1 53  ? 8.91700   17.15800  37.34600  1.000 23.50964 ? 50  LYS B CA  1 
ATOM   1355 C C   . LYS B 1 53  ? 10.02100  18.14500  37.70900  1.000 24.27698 ? 50  LYS B C   1 
ATOM   1356 O O   . LYS B 1 53  ? 10.90800  18.41500  36.89800  1.000 24.99070 ? 50  LYS B O   1 
ATOM   1357 C CB  . LYS B 1 53  ? 7.60000   17.88800  37.04900  1.000 27.17405 ? 50  LYS B CB  1 
ATOM   1358 C CG  . LYS B 1 53  ? 7.70200   18.91300  35.96300  1.000 25.16950 ? 50  LYS B CG  1 
ATOM   1359 C CD  . LYS B 1 53  ? 6.34000   19.55600  35.66500  1.000 27.54873 ? 50  LYS B CD  1 
ATOM   1360 C CE  . LYS B 1 53  ? 6.53400   20.77800  34.78300  1.000 26.46537 ? 50  LYS B CE  1 
ATOM   1361 N NZ  . LYS B 1 53  ? 5.19300   21.30900  34.33500  1.000 27.93075 ? 50  LYS B NZ  1 
ATOM   1362 N N   . ASP B 1 54  ? 9.95700   18.75700  38.90200  1.000 26.92437 ? 51  ASP B N   1 
ATOM   1363 C CA  . ASP B 1 54  ? 10.95800  19.76300  39.25200  1.000 26.46473 ? 51  ASP B CA  1 
ATOM   1364 C C   . ASP B 1 54  ? 12.35100  19.16000  39.36300  1.000 23.07325 ? 51  ASP B C   1 
ATOM   1365 O O   . ASP B 1 54  ? 13.33500  19.80400  38.99500  1.000 26.19456 ? 51  ASP B O   1 
ATOM   1366 C CB  . ASP B 1 54  ? 10.58600  20.46700  40.56500  1.000 27.97950 ? 51  ASP B CB  1 
ATOM   1367 C CG  . ASP B 1 54  ? 9.39100   21.38600  40.39800  1.000 38.71550 ? 51  ASP B CG  1 
ATOM   1368 O OD1 . ASP B 1 54  ? 8.95400   21.57600  39.24200  1.000 35.64496 ? 51  ASP B OD1 1 
ATOM   1369 O OD2 . ASP B 1 54  ? 8.87600   21.89800  41.40900  1.000 41.59357 ? 51  ASP B OD2 1 
ATOM   1370 N N   . GLN B 1 55  ? 12.44500  17.94400  39.86200  1.000 25.78403 ? 52  GLN B N   1 
ATOM   1371 C CA  . GLN B 1 55  ? 13.72400  17.28700  40.01400  1.000 25.42423 ? 52  GLN B CA  1 
ATOM   1372 C C   . GLN B 1 55  ? 14.31700  16.98700  38.64600  1.000 23.85172 ? 52  GLN B C   1 
ATOM   1373 O O   . GLN B 1 55  ? 15.45200  17.13300  38.41600  1.000 25.63401 ? 52  GLN B O   1 
ATOM   1374 C CB  . GLN B 1 55  ? 13.56700  15.97100  40.77600  1.000 28.79056 ? 52  GLN B CB  1 
ATOM   1375 C CG  . GLN B 1 55  ? 13.30000  16.10600  42.25900  1.000 29.43448 ? 52  GLN B CG  1 
ATOM   1376 C CD  . GLN B 1 55  ? 12.83700  14.81900  42.90700  1.000 31.23267 ? 52  GLN B CD  1 
ATOM   1377 O OE1 . GLN B 1 55  ? 12.34700  13.96100  42.29500  1.000 27.60254 ? 52  GLN B OE1 1 
ATOM   1378 N NE2 . GLN B 1 55  ? 12.97900  14.75300  44.19500  1.000 39.54216 ? 52  GLN B NE2 1 
ATOM   1379 N N   . PHE B 1 56  ? 13.48400  16.55700  37.74400  1.000 21.47406 ? 53  PHE B N   1 
ATOM   1380 C CA  . PHE B 1 56  ? 13.95500  16.23400  36.39500  1.000 20.73819 ? 53  PHE B CA  1 
ATOM   1381 C C   . PHE B 1 56  ? 14.41200  17.49100  35.67400  1.000 23.06839 ? 53  PHE B C   1 
ATOM   1382 O O   . PHE B 1 56  ? 15.47200  17.50700  35.03100  1.000 23.28754 ? 53  PHE B O   1 
ATOM   1383 C CB  . PHE B 1 56  ? 12.84000  15.55400  35.62600  1.000 20.78370 ? 53  PHE B CB  1 
ATOM   1384 C CG  . PHE B 1 56  ? 13.13900  15.33200  34.18800  1.000 20.97448 ? 53  PHE B CG  1 
ATOM   1385 C CD1 . PHE B 1 56  ? 13.99100  14.32000  33.78400  1.000 26.45454 ? 53  PHE B CD1 1 
ATOM   1386 C CD2 . PHE B 1 56  ? 12.56500  16.12300  33.23700  1.000 22.32953 ? 53  PHE B CD2 1 
ATOM   1387 C CE1 . PHE B 1 56  ? 14.26400  14.10800  32.44900  1.000 26.83087 ? 53  PHE B CE1 1 
ATOM   1388 C CE2 . PHE B 1 56  ? 12.80500  15.91400  31.89500  1.000 28.56263 ? 53  PHE B CE2 1 
ATOM   1389 C CZ  . PHE B 1 56  ? 13.66400  14.89800  31.49800  1.000 25.26801 ? 53  PHE B CZ  1 
ATOM   1390 N N   . LEU B 1 57  ? 13.62100  18.55800  35.75700  1.000 25.49471 ? 54  LEU B N   1 
ATOM   1391 C CA  . LEU B 1 57  ? 14.01400  19.80100  35.09800  1.000 23.20973 ? 54  LEU B CA  1 
ATOM   1392 C C   . LEU B 1 57  ? 15.26900  20.39200  35.71300  1.000 23.24556 ? 54  LEU B C   1 
ATOM   1393 O O   . LEU B 1 57  ? 16.05500  21.02300  35.00600  1.000 24.30541 ? 54  LEU B O   1 
ATOM   1394 C CB  . LEU B 1 57  ? 12.85700  20.79200  35.16300  1.000 23.09132 ? 54  LEU B CB  1 
ATOM   1395 C CG  . LEU B 1 57  ? 11.66300  20.33200  34.33000  1.000 27.48332 ? 54  LEU B CG  1 
ATOM   1396 C CD1 . LEU B 1 57  ? 10.41800  21.16300  34.70300  1.000 33.75940 ? 54  LEU B CD1 1 
ATOM   1397 C CD2 . LEU B 1 57  ? 11.97100  20.42400  32.85300  1.000 30.63136 ? 54  LEU B CD2 1 
ATOM   1398 N N   . GLN B 1 58  ? 15.49800  20.15900  36.99500  1.000 23.94464 ? 55  GLN B N   1 
ATOM   1399 C CA  . GLN B 1 58  ? 16.72100  20.57700  37.64100  1.000 25.01994 ? 55  GLN B CA  1 
ATOM   1400 C C   . GLN B 1 58  ? 17.89400  19.86500  36.97100  1.000 26.05149 ? 55  GLN B C   1 
ATOM   1401 O O   . GLN B 1 58  ? 18.88800  20.47300  36.70000  1.000 24.93370 ? 55  GLN B O   1 
ATOM   1402 C CB  . GLN B 1 58  ? 16.74900  20.15000  39.11000  1.000 31.83781 ? 55  GLN B CB  1 
ATOM   1403 C CG  . GLN B 1 58  ? 16.07000  20.98900  40.17400  1.000 48.65372 ? 55  GLN B CG  1 
ATOM   1404 C CD  . GLN B 1 58  ? 15.73800  20.20500  41.49300  1.000 43.96826 ? 55  GLN B CD  1 
ATOM   1405 O OE1 . GLN B 1 58  ? 16.60800  19.58600  42.11500  1.000 47.29698 ? 55  GLN B OE1 1 
ATOM   1406 N NE2 . GLN B 1 58  ? 14.46800  20.23100  41.90000  1.000 39.56738 ? 55  GLN B NE2 1 
ATOM   1407 N N   . MET B 1 59  ? 17.80300  18.54500  36.80100  1.000 21.22224 ? 56  MET B N   1 
ATOM   1408 C CA  . MET B 1 59  ? 18.83800  17.79800  36.11800  1.000 24.95516 ? 56  MET B CA  1 
ATOM   1409 C C   . MET B 1 59  ? 19.02800  18.26500  34.68100  1.000 22.72446 ? 56  MET B C   1 
ATOM   1410 O O   . MET B 1 59  ? 20.16000  18.28500  34.17700  1.000 23.10067 ? 56  MET B O   1 
ATOM   1411 C CB  . MET B 1 59  ? 18.51200  16.30400  36.16200  1.000 25.22951 ? 56  MET B CB  1 
ATOM   1412 C CG  . MET B 1 59  ? 18.82800  15.70200  37.51800  1.000 34.19690 ? 56  MET B CG  1 
ATOM   1413 S SD  . MET B 1 59  ? 18.46400  13.93700  37.63400  1.000 42.91958 ? 56  MET B SD  1 
ATOM   1414 C CE  . MET B 1 59  ? 19.30300  13.34400  36.15900  1.000 43.00063 ? 56  MET B CE  1 
ATOM   1415 N N   . ILE B 1 60  ? 17.93900  18.59000  33.97000  1.000 21.53911 ? 57  ILE B N   1 
ATOM   1416 C CA  A ILE B 1 60  ? 18.08100  19.09900  32.60200  0.116 20.15142 ? 57  ILE B CA  1 
ATOM   1417 C CA  B ILE B 1 60  ? 18.09500  19.09000  32.59600  0.884 19.93251 ? 57  ILE B CA  1 
ATOM   1418 C C   . ILE B 1 60  ? 18.89000  20.37900  32.59000  1.000 22.10532 ? 57  ILE B C   1 
ATOM   1419 O O   . ILE B 1 60  ? 19.76200  20.59300  31.73200  1.000 22.07990 ? 57  ILE B O   1 
ATOM   1420 C CB  A ILE B 1 60  ? 16.69700  19.31900  31.96100  0.116 22.67464 ? 57  ILE B CB  1 
ATOM   1421 C CB  B ILE B 1 60  ? 16.72500  19.27700  31.93100  0.884 22.67185 ? 57  ILE B CB  1 
ATOM   1422 C CG1 A ILE B 1 60  ? 16.14900  18.00300  31.41000  0.116 23.01771 ? 57  ILE B CG1 1 
ATOM   1423 C CG1 B ILE B 1 60  ? 16.02600  17.93000  31.77000  0.884 22.25215 ? 57  ILE B CG1 1 
ATOM   1424 C CG2 A ILE B 1 60  ? 16.77800  20.41400  30.87900  0.116 23.84826 ? 57  ILE B CG2 1 
ATOM   1425 C CG2 B ILE B 1 60  ? 16.87200  20.03200  30.58600  0.884 24.68023 ? 57  ILE B CG2 1 
ATOM   1426 C CD1 A ILE B 1 60  ? 14.73800  18.09200  30.87000  0.116 23.88509 ? 57  ILE B CD1 1 
ATOM   1427 C CD1 B ILE B 1 60  ? 16.72500  17.00000  30.76200  0.884 22.37377 ? 57  ILE B CD1 1 
ATOM   1428 N N   . LYS B 1 61  ? 18.55800  21.30600  33.49900  1.000 22.41782 ? 58  LYS B N   1 
ATOM   1429 C CA  . LYS B 1 61  ? 19.30900  22.56000  33.61600  1.000 20.96041 ? 58  LYS B CA  1 
ATOM   1430 C C   . LYS B 1 61  ? 20.80000  22.29700  33.72400  1.000 24.60010 ? 58  LYS B C   1 
ATOM   1431 O O   . LYS B 1 61  ? 21.60600  22.88300  32.98800  1.000 24.44723 ? 58  LYS B O   1 
ATOM   1432 C CB  . LYS B 1 61  ? 18.82400  23.35800  34.82400  1.000 26.02478 ? 58  LYS B CB  1 
ATOM   1433 C CG  . LYS B 1 61  ? 19.48500  24.70800  34.93700  1.000 27.00133 ? 58  LYS B CG  1 
ATOM   1434 C CD  . LYS B 1 61  ? 18.96900  25.45400  36.16100  1.000 36.12788 ? 58  LYS B CD  1 
ATOM   1435 C CE  . LYS B 1 61  ? 20.08000  25.79600  37.13200  1.000 41.83346 ? 58  LYS B CE  1 
ATOM   1436 N NZ  . LYS B 1 61  ? 19.79500  27.09800  37.80000  1.000 44.08134 ? 58  LYS B NZ  1 
ATOM   1437 N N   . GLU B 1 62  ? 21.18500  21.38300  34.61100  1.000 23.36818 ? 59  GLU B N   1 
ATOM   1438 C CA  . GLU B 1 62  ? 22.59900  21.05500  34.75800  1.000 25.07053 ? 59  GLU B CA  1 
ATOM   1439 C C   . GLU B 1 62  ? 23.16700  20.47800  33.47100  1.000 26.27797 ? 59  GLU B C   1 
ATOM   1440 O O   . GLU B 1 62  ? 24.27500  20.82500  33.05400  1.000 23.78170 ? 59  GLU B O   1 
ATOM   1441 C CB  . GLU B 1 62  ? 22.79000  20.09000  35.92900  1.000 28.43436 ? 59  GLU B CB  1 
ATOM   1442 C CG  . GLU B 1 62  ? 22.19300  20.60500  37.24700  1.000 26.94415 ? 59  GLU B CG  1 
ATOM   1443 C CD  . GLU B 1 62  ? 22.16200  19.54500  38.33400  1.000 46.83724 ? 59  GLU B CD  1 
ATOM   1444 O OE1 . GLU B 1 62  ? 22.16800  18.33300  38.00200  1.000 44.64890 ? 59  GLU B OE1 1 
ATOM   1445 O OE2 . GLU B 1 62  ? 22.12500  19.93500  39.51900  1.000 49.13717 ? 59  GLU B OE2 1 
ATOM   1446 N N   . ALA B 1 63  ? 22.42900  19.58500  32.80500  1.000 20.86956 ? 60  ALA B N   1 
ATOM   1447 C CA  . ALA B 1 63  ? 22.96100  19.02700  31.57600  1.000 22.78310 ? 60  ALA B CA  1 
ATOM   1448 C C   . ALA B 1 63  ? 23.11500  20.08900  30.50800  1.000 24.34691 ? 60  ALA B C   1 
ATOM   1449 O O   . ALA B 1 63  ? 24.05900  20.05000  29.72000  1.000 23.42551 ? 60  ALA B O   1 
ATOM   1450 C CB  . ALA B 1 63  ? 22.06900  17.90700  31.06000  1.000 23.34738 ? 60  ALA B CB  1 
ATOM   1451 N N   . LEU B 1 64  ? 22.17000  21.01200  30.46100  1.000 22.63136 ? 61  LEU B N   1 
ATOM   1452 C CA  . LEU B 1 64  ? 22.24500  22.10700  29.48800  1.000 22.65385 ? 61  LEU B CA  1 
ATOM   1453 C C   . LEU B 1 64  ? 23.47400  23.00900  29.73200  1.000 24.67587 ? 61  LEU B C   1 
ATOM   1454 O O   . LEU B 1 64  ? 24.07600  23.47400  28.82900  1.000 24.24116 ? 61  LEU B O   1 
ATOM   1455 C CB  . LEU B 1 64  ? 20.95600  22.91400  29.44900  1.000 19.14696 ? 61  LEU B CB  1 
ATOM   1456 C CG  . LEU B 1 64  ? 19.74800  22.25600  28.80600  1.000 22.57677 ? 61  LEU B CG  1 
ATOM   1457 C CD1 . LEU B 1 64  ? 18.50900  23.07000  29.01200  1.000 26.11217 ? 61  LEU B CD1 1 
ATOM   1458 C CD2 . LEU B 1 64  ? 19.90900  21.93900  27.34100  1.000 25.52463 ? 61  LEU B CD2 1 
ATOM   1459 N N   . GLU B 1 65  ? 23.81800  23.18500  30.98200  1.000 24.76774 ? 62  GLU B N   1 
ATOM   1460 C CA  . GLU B 1 65  ? 24.99000  23.95800  31.35300  1.000 27.08417 ? 62  GLU B CA  1 
ATOM   1461 C C   . GLU B 1 65  ? 26.25600  23.26800  30.82000  1.000 29.48754 ? 62  GLU B C   1 
ATOM   1462 O O   . GLU B 1 65  ? 27.25400  23.88800  30.54400  1.000 31.94306 ? 62  GLU B O   1 
ATOM   1463 C CB  . GLU B 1 65  ? 25.07700  24.12500  32.87300  1.000 26.19945 ? 62  GLU B CB  1 
ATOM   1464 C CG  . GLU B 1 65  ? 24.03500  25.08200  33.45100  1.000 30.00335 ? 62  GLU B CG  1 
ATOM   1465 C CD  . GLU B 1 65  ? 24.06500  25.23500  34.97000  1.000 37.28961 ? 62  GLU B CD  1 
ATOM   1466 O OE1 . GLU B 1 65  ? 25.07000  24.99100  35.60800  1.000 42.57343 ? 62  GLU B OE1 1 
ATOM   1467 O OE2 . GLU B 1 65  ? 23.06700  25.62300  35.51500  1.000 36.38214 ? 62  GLU B OE2 1 
ATOM   1468 N N   . GLN B 1 66  ? 26.17300  21.95200  30.65600  1.000 25.52913 ? 63  GLN B N   1 
ATOM   1469 C CA  . GLN B 1 66  ? 27.21600  21.15900  30.08200  1.000 27.11139 ? 63  GLN B CA  1 
ATOM   1470 C C   . GLN B 1 66  ? 27.07500  20.89000  28.58200  1.000 28.65652 ? 63  GLN B C   1 
ATOM   1471 O O   . GLN B 1 66  ? 27.50800  19.86300  28.14900  1.000 30.67233 ? 63  GLN B O   1 
ATOM   1472 C CB  . GLN B 1 66  ? 27.31400  19.82900  30.81800  1.000 37.09732 ? 63  GLN B CB  1 
ATOM   1473 C CG  . GLN B 1 66  ? 27.70700  19.95800  32.25100  1.000 34.97991 ? 63  GLN B CG  1 
ATOM   1474 C CD  . GLN B 1 66  ? 27.55200  18.67900  33.02600  1.000 46.23733 ? 63  GLN B CD  1 
ATOM   1475 O OE1 . GLN B 1 66  ? 26.46800  18.34700  33.47200  1.000 54.35968 ? 63  GLN B OE1 1 
ATOM   1476 N NE2 . GLN B 1 66  ? 28.64500  17.96000  33.21700  1.000 53.37345 ? 63  GLN B NE2 1 
ATOM   1477 N N   . ASP B 1 67  ? 26.44500  21.79400  27.83800  1.000 26.44117 ? 64  ASP B N   1 
ATOM   1478 C CA  . ASP B 1 67  ? 26.29500  21.75000  26.41600  1.000 25.70751 ? 64  ASP B CA  1 
ATOM   1479 C C   . ASP B 1 67  ? 25.55100  20.53900  25.88300  1.000 26.94931 ? 64  ASP B C   1 
ATOM   1480 O O   . ASP B 1 67  ? 25.85500  20.09300  24.81800  1.000 25.06345 ? 64  ASP B O   1 
ATOM   1481 C CB  . ASP B 1 67  ? 27.64800  21.92700  25.74000  1.000 30.17257 ? 64  ASP B CB  1 
ATOM   1482 C CG  . ASP B 1 67  ? 27.55300  22.38300  24.34800  1.000 33.17371 ? 64  ASP B CG  1 
ATOM   1483 O OD1 . ASP B 1 67  ? 26.70000  23.17000  24.04500  1.000 31.73294 ? 64  ASP B OD1 1 
ATOM   1484 O OD2 . ASP B 1 67  ? 28.37600  21.96800  23.56900  1.000 35.91254 ? 64  ASP B OD2 1 
ATOM   1485 N N   . LEU B 1 68  ? 24.57700  20.05500  26.63900  1.000 24.36808 ? 65  LEU B N   1 
ATOM   1486 C CA  . LEU B 1 68  ? 23.73500  18.97200  26.13100  1.000 22.38427 ? 65  LEU B CA  1 
ATOM   1487 C C   . LEU B 1 68  ? 23.14100  19.33400  24.77000  1.000 25.01376 ? 65  LEU B C   1 
ATOM   1488 O O   . LEU B 1 68  ? 22.55300  20.40500  24.59200  1.000 25.08558 ? 65  LEU B O   1 
ATOM   1489 C CB  . LEU B 1 68  ? 22.61100  18.67800  27.12200  1.000 20.13117 ? 65  LEU B CB  1 
ATOM   1490 C CG  . LEU B 1 68  ? 21.60300  17.64000  26.62900  1.000 21.17730 ? 65  LEU B CG  1 
ATOM   1491 C CD1 . LEU B 1 68  ? 22.24200  16.24100  26.58800  1.000 22.13408 ? 65  LEU B CD1 1 
ATOM   1492 C CD2 . LEU B 1 68  ? 20.36100  17.62100  27.47800  1.000 24.00706 ? 65  LEU B CD2 1 
ATOM   1493 N N   . LYS B 1 69  ? 23.21200  18.40000  23.81300  1.000 22.71991 ? 66  LYS B N   1 
ATOM   1494 C CA  . LYS B 1 69  ? 22.66500  18.52700  22.47900  1.000 22.25746 ? 66  LYS B CA  1 
ATOM   1495 C C   . LYS B 1 69  ? 22.08800  17.16300  22.12100  1.000 22.34065 ? 66  LYS B C   1 
ATOM   1496 O O   . LYS B 1 69  ? 22.59800  16.18500  22.53400  1.000 25.18953 ? 66  LYS B O   1 
ATOM   1497 C CB  . LYS B 1 69  ? 23.72200  18.92100  21.48900  1.000 23.65775 ? 66  LYS B CB  1 
ATOM   1498 C CG  . LYS B 1 69  ? 24.20800  20.33500  21.71600  1.000 30.64369 ? 66  LYS B CG  1 
ATOM   1499 C CD  . LYS B 1 69  ? 25.13600  20.77500  20.62200  1.000 38.74479 ? 66  LYS B CD  1 
ATOM   1500 C CE  . LYS B 1 69  ? 25.22400  22.29900  20.52200  1.000 36.19869 ? 66  LYS B CE  1 
ATOM   1501 N NZ  . LYS B 1 69  ? 26.62000  22.70300  20.74700  1.000 38.68754 ? 66  LYS B NZ  1 
ATOM   1502 N N   . VAL B 1 70  ? 20.98400  17.15600  21.41300  1.000 20.77232 ? 67  VAL B N   1 
ATOM   1503 C CA  . VAL B 1 70  ? 20.31300  15.92800  21.06500  1.000 17.76771 ? 67  VAL B CA  1 
ATOM   1504 C C   . VAL B 1 70  ? 19.93200  15.86500  19.58300  1.000 29.50333 ? 67  VAL B C   1 
ATOM   1505 O O   . VAL B 1 70  ? 19.70800  16.86900  18.98900  1.000 27.06543 ? 67  VAL B O   1 
ATOM   1506 C CB  . VAL B 1 70  ? 19.01700  15.76900  21.87600  1.000 22.33442 ? 67  VAL B CB  1 
ATOM   1507 C CG1 . VAL B 1 70  ? 19.31000  15.64600  23.34700  1.000 21.56710 ? 67  VAL B CG1 1 
ATOM   1508 C CG2 . VAL B 1 70  ? 18.09200  16.93900  21.61600  1.000 24.88441 ? 67  VAL B CG2 1 
ATOM   1509 N N   . GLU B 1 71  ? 19.87700  14.65500  19.03700  1.000 22.51497 ? 68  GLU B N   1 
ATOM   1510 C CA  . GLU B 1 71  ? 19.51100  14.42500  17.69000  1.000 26.51847 ? 68  GLU B CA  1 
ATOM   1511 C C   . GLU B 1 71  ? 18.51800  13.22600  17.69000  1.000 25.71443 ? 68  GLU B C   1 
ATOM   1512 O O   . GLU B 1 71  ? 18.85700  12.16100  18.05600  1.000 26.01830 ? 68  GLU B O   1 
ATOM   1513 C CB  . GLU B 1 71  ? 20.71600  14.10300  16.84400  1.000 29.08334 ? 68  GLU B CB  1 
ATOM   1514 C CG  . GLU B 1 71  ? 20.35300  13.77500  15.41600  1.000 36.21215 ? 68  GLU B CG  1 
ATOM   1515 C CD  . GLU B 1 71  ? 21.56900  13.71600  14.53100  1.000 47.78341 ? 68  GLU B CD  1 
ATOM   1516 O OE1 . GLU B 1 71  ? 22.29700  14.70200  14.42700  1.000 59.21918 ? 68  GLU B OE1 1 
ATOM   1517 O OE2 . GLU B 1 71  ? 21.81000  12.63700  13.97900  1.000 48.34452 ? 68  GLU B OE2 1 
ATOM   1518 N N   . VAL B 1 72  ? 17.29500  13.43600  17.28200  1.000 25.17319 ? 69  VAL B N   1 
ATOM   1519 C CA  . VAL B 1 72  ? 16.31700  12.34300  17.23700  1.000 24.58764 ? 69  VAL B CA  1 
ATOM   1520 C C   . VAL B 1 72  ? 16.59800  11.43700  16.03700  1.000 29.84724 ? 69  VAL B C   1 
ATOM   1521 O O   . VAL B 1 72  ? 16.75400  11.91400  14.90100  1.000 27.28920 ? 69  VAL B O   1 
ATOM   1522 C CB  . VAL B 1 72  ? 14.89200  12.89700  17.18100  1.000 23.22687 ? 69  VAL B CB  1 
ATOM   1523 C CG1 . VAL B 1 72  ? 13.91000  11.76000  16.94300  1.000 26.37008 ? 69  VAL B CG1 1 
ATOM   1524 C CG2 . VAL B 1 72  ? 14.55400  13.64300  18.47100  1.000 27.99351 ? 69  VAL B CG2 1 
ATOM   1525 N N   . LYS B 1 73  ? 16.72500  10.13200  16.28100  1.000 26.58662 ? 70  LYS B N   1 
ATOM   1526 C CA  . LYS B 1 73  ? 16.96900  9.17700   15.23900  1.000 25.75193 ? 70  LYS B CA  1 
ATOM   1527 C C   . LYS B 1 73  ? 15.71500  8.47000   14.79400  1.000 36.10518 ? 70  LYS B C   1 
ATOM   1528 O O   . LYS B 1 73  ? 15.65600  8.11100   13.64900  1.000 38.04902 ? 70  LYS B O   1 
ATOM   1529 C CB  . LYS B 1 73  ? 17.94300  8.10400   15.70800  1.000 30.23674 ? 70  LYS B CB  1 
ATOM   1530 C CG  . LYS B 1 73  ? 19.24400  8.57900   16.29500  1.000 27.37822 ? 70  LYS B CG  1 
ATOM   1531 C CD  . LYS B 1 73  ? 19.93200  9.64500   15.48000  1.000 44.08297 ? 70  LYS B CD  1 
ATOM   1532 C CE  . LYS B 1 73  ? 20.83200  9.07600   14.39800  1.000 51.57311 ? 70  LYS B CE  1 
ATOM   1533 N NZ  . LYS B 1 73  ? 21.37500  10.10100  13.44800  1.000 52.81648 ? 70  LYS B NZ  1 
ATOM   1534 N N   . SER B 1 74  ? 14.74300  8.21800   15.67500  1.000 28.22184 ? 71  SER B N   1 
ATOM   1535 C CA  . SER B 1 74  ? 13.53500  7.49600   15.30100  1.000 34.32865 ? 71  SER B CA  1 
ATOM   1536 C C   . SER B 1 74  ? 12.46800  7.76700   16.34700  1.000 32.21444 ? 71  SER B C   1 
ATOM   1537 O O   . SER B 1 74  ? 12.78300  8.06300   17.50500  1.000 27.95777 ? 71  SER B O   1 
ATOM   1538 C CB  . SER B 1 74  ? 13.79500  5.99900   15.19100  1.000 34.68044 ? 71  SER B CB  1 
ATOM   1539 O OG  . SER B 1 74  ? 14.09900  5.45300   16.45500  1.000 34.18774 ? 71  SER B OG  1 
ATOM   1540 N N   . ILE B 1 75  ? 11.20700  7.69500   15.93400  1.000 27.55075 ? 72  ILE B N   1 
ATOM   1541 C CA  . ILE B 1 75  ? 10.03000  7.92400   16.77300  1.000 29.19723 ? 72  ILE B CA  1 
ATOM   1542 C C   . ILE B 1 75  ? 8.95400   6.89800   16.41100  1.000 36.97269 ? 72  ILE B C   1 
ATOM   1543 O O   . ILE B 1 75  ? 8.46900   6.89600   15.29700  1.000 39.53979 ? 72  ILE B O   1 
ATOM   1544 C CB  . ILE B 1 75  ? 9.38800   9.25000   16.46700  1.000 30.20792 ? 72  ILE B CB  1 
ATOM   1545 C CG1 . ILE B 1 75  ? 10.35300  10.40300  16.69400  1.000 30.87344 ? 72  ILE B CG1 1 
ATOM   1546 C CG2 . ILE B 1 75  ? 8.12400   9.42800   17.28800  1.000 29.96956 ? 72  ILE B CG2 1 
ATOM   1547 C CD1 . ILE B 1 75  ? 9.77400   11.73900  16.38700  1.000 37.78617 ? 72  ILE B CD1 1 
ATOM   1548 N N   . ASP B 1 76  ? 8.60900   6.00700   17.31700  1.000 31.35101 ? 73  ASP B N   1 
ATOM   1549 C CA  . ASP B 1 76  ? 7.64800   4.98800   17.03500  1.000 33.29716 ? 73  ASP B CA  1 
ATOM   1550 C C   . ASP B 1 76  ? 6.50300   5.02400   18.02200  1.000 37.81015 ? 73  ASP B C   1 
ATOM   1551 O O   . ASP B 1 76  ? 6.71600   4.71300   19.14900  1.000 33.84601 ? 73  ASP B O   1 
ATOM   1552 C CB  . ASP B 1 76  ? 8.36300   3.66800   17.18300  1.000 37.66119 ? 73  ASP B CB  1 
ATOM   1553 C CG  . ASP B 1 76  ? 7.61900   2.50400   16.52000  1.000 50.94577 ? 73  ASP B CG  1 
ATOM   1554 O OD1 . ASP B 1 76  ? 6.68300   1.98800   17.12200  1.000 48.31445 ? 73  ASP B OD1 1 
ATOM   1555 O OD2 . ASP B 1 76  ? 8.00200   2.09400   15.40700  1.000 55.36947 ? 73  ASP B OD2 1 
ATOM   1556 N N   . ILE B 1 77  ? 5.30400   5.40900   17.59800  1.000 32.21556 ? 74  ILE B N   1 
ATOM   1557 C CA  . ILE B 1 77  ? 4.15200   5.41800   18.48600  1.000 33.81253 ? 74  ILE B CA  1 
ATOM   1558 C C   . ILE B 1 77  ? 3.76000   3.97500   18.66500  1.000 39.30089 ? 74  ILE B C   1 
ATOM   1559 O O   . ILE B 1 77  ? 3.54100   3.30000   17.69300  1.000 40.02546 ? 74  ILE B O   1 
ATOM   1560 C CB  . ILE B 1 77  ? 2.95700   6.15600   17.90900  1.000 33.81235 ? 74  ILE B CB  1 
ATOM   1561 C CG1 . ILE B 1 77  ? 3.28700   7.63600   17.77900  1.000 44.10009 ? 74  ILE B CG1 1 
ATOM   1562 C CG2 . ILE B 1 77  ? 1.73900   5.95100   18.78400  1.000 38.11935 ? 74  ILE B CG2 1 
ATOM   1563 C CD1 . ILE B 1 77  ? 2.09500   8.53200   17.55900  1.000 40.80971 ? 74  ILE B CD1 1 
ATOM   1564 N N   . GLU B 1 78  ? 3.63500   3.50700   19.88500  1.000 33.47699 ? 75  GLU B N   1 
ATOM   1565 C CA  . GLU B 1 78  ? 3.37200   2.12800   20.05300  1.000 38.17034 ? 75  GLU B CA  1 
ATOM   1566 C C   . GLU B 1 78  ? 1.91600   1.75700   20.20500  1.000 40.11836 ? 75  GLU B C   1 
ATOM   1567 O O   . GLU B 1 78  ? 1.24000   2.33200   20.97400  1.000 38.53887 ? 75  GLU B O   1 
ATOM   1568 C CB  . GLU B 1 78  ? 4.12000   1.60400   21.17600  1.000 42.57229 ? 75  GLU B CB  1 
ATOM   1569 C CG  . GLU B 1 78  ? 5.53100   1.60100   20.79000  1.000 46.80093 ? 75  GLU B CG  1 
ATOM   1570 C CD  . GLU B 1 78  ? 6.27400   1.19400   21.93300  1.000 49.98560 ? 75  GLU B CD  1 
ATOM   1571 O OE1 . GLU B 1 78  ? 6.01500   0.05400   22.27900  1.000 56.89596 ? 75  GLU B OE1 1 
ATOM   1572 O OE2 . GLU B 1 78  ? 6.96000   2.05600   22.45500  1.000 51.23957 ? 75  GLU B OE2 1 
ATOM   1573 N N   . GLN B 1 79  ? 1.50100   0.77700   19.42300  1.000 38.90756 ? 76  GLN B N   1 
ATOM   1574 C CA  . GLN B 1 79  ? 0.13600   0.28300   19.28400  1.000 42.94729 ? 76  GLN B CA  1 
ATOM   1575 C C   . GLN B 1 79  ? -0.27500  -0.35000  20.59000  1.000 38.59094 ? 76  GLN B C   1 
ATOM   1576 O O   . GLN B 1 79  ? 0.37700   -1.26200  21.02500  1.000 42.21062 ? 76  GLN B O   1 
ATOM   1577 C CB  . GLN B 1 79  ? 0.14900   -0.79900  18.20300  1.000 49.10640 ? 76  GLN B CB  1 
ATOM   1578 C CG  . GLN B 1 79  ? 1.45500   -1.60800  18.22900  1.000 51.54769 ? 76  GLN B CG  1 
ATOM   1579 C CD  . GLN B 1 79  ? 1.58600   -2.70900  17.17400  1.000 55.04601 ? 76  GLN B CD  1 
ATOM   1580 O OE1 . GLN B 1 79  ? 1.72500   -3.87400  17.52200  1.000 58.18434 ? 76  GLN B OE1 1 
ATOM   1581 N NE2 . GLN B 1 79  ? 1.57800   -2.34200  15.90200  1.000 52.66930 ? 76  GLN B NE2 1 
ATOM   1582 N N   . GLN B 1 80  ? -1.31600  0.18000   21.22000  1.000 34.89835 ? 77  GLN B N   1 
ATOM   1583 C CA  . GLN B 1 80  ? -1.83200  -0.34100  22.47100  1.000 39.99238 ? 77  GLN B CA  1 
ATOM   1584 C C   . GLN B 1 80  ? -3.31500  0.10600   22.58600  1.000 37.79716 ? 77  GLN B C   1 
ATOM   1585 O O   . GLN B 1 80  ? -3.69000  1.10000   22.00000  1.000 34.23198 ? 77  GLN B O   1 
ATOM   1586 C CB  . GLN B 1 80  ? -0.94700  0.02900   23.65600  1.000 39.86612 ? 77  GLN B CB  1 
ATOM   1587 C CG  . GLN B 1 80  ? -0.73900  1.50700   23.83100  1.000 35.68986 ? 77  GLN B CG  1 
ATOM   1588 C CD  . GLN B 1 80  ? -1.90100  2.15900   24.53000  1.000 36.92054 ? 77  GLN B CD  1 
ATOM   1589 O OE1 . GLN B 1 80  ? -2.58500  1.53300   25.30700  1.000 37.49511 ? 77  GLN B OE1 1 
ATOM   1590 N NE2 . GLN B 1 80  ? -2.11100  3.42600   24.26400  1.000 34.72498 ? 77  GLN B NE2 1 
ATOM   1591 N N   . PRO B 1 81  ? -4.22900  -0.58400  23.35700  1.000 32.84023 ? 78  PRO B N   1 
ATOM   1592 C CA  . PRO B 1 81  ? -5.72100  -0.26000  23.40100  1.000 34.43799 ? 78  PRO B CA  1 
ATOM   1593 C C   . PRO B 1 81  ? -6.37000  0.85400   24.38400  1.000 41.10970 ? 78  PRO B C   1 
ATOM   1594 O O   . PRO B 1 81  ? -7.52800  1.66400   24.39200  1.000 49.97735 ? 78  PRO B O   1 
ATOM   1595 C CB  . PRO B 1 81  ? -6.32900  -1.63700  23.64300  1.000 37.92884 ? 78  PRO B CB  1 
ATOM   1596 C CG  . PRO B 1 81  ? -5.29700  -2.37700  24.41400  1.000 36.62118 ? 78  PRO B CG  1 
ATOM   1597 C CD  . PRO B 1 81  ? -3.94200  -1.83100  24.07200  1.000 35.49813 ? 78  PRO B CD  1 
ATOM   1598 N N   . ASP B 1 82  ? -5.45000  1.19400   25.27200  1.000 34.85638 ? 79  ASP B N   1 
ATOM   1599 C CA  . ASP B 1 82  ? -5.79500  2.22900   26.20300  1.000 38.86268 ? 79  ASP B CA  1 
ATOM   1600 C C   . ASP B 1 82  ? -5.62400  3.44800   25.24500  1.000 41.13002 ? 79  ASP B C   1 
ATOM   1601 O O   . ASP B 1 82  ? -4.60700  3.83800   24.96600  1.000 42.37266 ? 79  ASP B O   1 
ATOM   1602 C CB  . ASP B 1 82  ? -4.94000  2.27300   27.42800  1.000 39.04826 ? 79  ASP B CB  1 
ATOM   1603 C CG  . ASP B 1 82  ? -5.52500  3.15100   28.48100  1.000 37.18422 ? 79  ASP B CG  1 
ATOM   1604 O OD1 . ASP B 1 82  ? -6.43100  3.90400   28.17400  1.000 34.82416 ? 79  ASP B OD1 1 
ATOM   1605 O OD2 . ASP B 1 82  ? -5.04600  3.11500   29.59800  1.000 46.77485 ? 79  ASP B OD2 1 
ATOM   1606 N N   . GLY B 1 83  ? -6.78400  3.95600   24.73500  1.000 41.03548 ? 80  GLY B N   1 
ATOM   1607 C CA  . GLY B 1 83  ? -7.11000  5.06500   23.90100  1.000 36.14427 ? 80  GLY B CA  1 
ATOM   1608 C C   . GLY B 1 83  ? -7.13700  6.22400   24.82100  1.000 42.60904 ? 80  GLY B C   1 
ATOM   1609 O O   . GLY B 1 83  ? -7.08800  7.34700   24.39500  1.000 44.05505 ? 80  GLY B O   1 
ATOM   1610 N N   . ASP B 1 84  ? -7.16800  5.97800   26.13300  1.000 40.89428 ? 81  ASP B N   1 
ATOM   1611 C CA  . ASP B 1 84  ? -6.82700  7.23400   27.00400  1.000 39.04105 ? 81  ASP B CA  1 
ATOM   1612 C C   . ASP B 1 84  ? -5.27300  7.74200   27.19700  1.000 36.68309 ? 81  ASP B C   1 
ATOM   1613 O O   . ASP B 1 84  ? -4.94100  8.72000   27.85300  1.000 37.02162 ? 81  ASP B O   1 
ATOM   1614 C CB  . ASP B 1 84  ? -7.29000  7.06000   28.44300  1.000 43.76401 ? 81  ASP B CB  1 
ATOM   1615 C CG  . ASP B 1 84  ? -8.76900  7.21400   28.62600  1.000 50.83491 ? 81  ASP B CG  1 
ATOM   1616 O OD1 . ASP B 1 84  ? -9.44600  7.62300   27.68100  1.000 54.88545 ? 81  ASP B OD1 1 
ATOM   1617 O OD2 . ASP B 1 84  ? -9.24000  6.92900   29.75100  1.000 51.75422 ? 81  ASP B OD2 1 
ATOM   1618 N N   . VAL B 1 85  ? -4.35900  7.02800   26.61500  1.000 33.96243 ? 82  VAL B N   1 
ATOM   1619 C CA  . VAL B 1 85  ? -2.90300  7.06000   26.76500  1.000 32.11081 ? 82  VAL B CA  1 
ATOM   1620 C C   . VAL B 1 85  ? -2.26600  6.89400   25.39400  1.000 32.23168 ? 82  VAL B C   1 
ATOM   1621 O O   . VAL B 1 85  ? -2.77600  6.15100   24.55200  1.000 34.83140 ? 82  VAL B O   1 
ATOM   1622 C CB  . VAL B 1 85  ? -2.44000  5.93200   27.71500  1.000 32.44167 ? 82  VAL B CB  1 
ATOM   1623 C CG1 . VAL B 1 85  ? -0.95000  5.69300   27.58900  1.000 39.61000 ? 82  VAL B CG1 1 
ATOM   1624 C CG2 . VAL B 1 85  ? -2.81400  6.24900   29.15600  1.000 42.56003 ? 82  VAL B CG2 1 
ATOM   1625 N N   . VAL B 1 86  ? -1.19000  7.64100   25.08200  1.000 30.98600 ? 83  VAL B N   1 
ATOM   1626 C CA  . VAL B 1 86  ? -0.39800  7.39600   23.92300  1.000 26.57611 ? 83  VAL B CA  1 
ATOM   1627 C C   . VAL B 1 86  ? 1.07800   7.04200   24.34300  1.000 28.81991 ? 83  VAL B C   1 
ATOM   1628 O O   . VAL B 1 86  ? 1.66900   7.79000   25.08100  1.000 25.89411 ? 83  VAL B O   1 
ATOM   1629 C CB  . VAL B 1 86  ? -0.42900  8.63700   23.09200  1.000 36.08764 ? 83  VAL B CB  1 
ATOM   1630 C CG1 . VAL B 1 86  ? 0.65900   8.58300   22.11800  1.000 36.95771 ? 83  VAL B CG1 1 
ATOM   1631 C CG2 . VAL B 1 86  ? -1.78700  8.81900   22.47600  1.000 39.74455 ? 83  VAL B CG2 1 
ATOM   1632 N N   . ILE B 1 87  ? 1.62000   5.90000   23.90300  1.000 24.57592 ? 84  ILE B N   1 
ATOM   1633 C CA  . ILE B 1 87  ? 2.99000   5.46800   24.23100  1.000 25.28907 ? 84  ILE B CA  1 
ATOM   1634 C C   . ILE B 1 87  ? 3.93500   5.66400   23.08200  1.000 33.60263 ? 84  ILE B C   1 
ATOM   1635 O O   . ILE B 1 87  ? 3.68700   5.16400   22.03600  1.000 29.22466 ? 84  ILE B O   1 
ATOM   1636 C CB  . ILE B 1 87  ? 3.10800   3.97200   24.47300  1.000 28.17640 ? 84  ILE B CB  1 
ATOM   1637 C CG1 . ILE B 1 87  ? 2.03300   3.50400   25.39000  1.000 34.70610 ? 84  ILE B CG1 1 
ATOM   1638 C CG2 . ILE B 1 87  ? 4.45700   3.63100   25.06100  1.000 31.62172 ? 84  ILE B CG2 1 
ATOM   1639 C CD1 . ILE B 1 87  ? 2.03200   4.18800   26.67500  1.000 35.34981 ? 84  ILE B CD1 1 
ATOM   1640 N N   . VAL B 1 88  ? 5.02800   6.39200   23.27200  1.000 28.52689 ? 85  VAL B N   1 
ATOM   1641 C CA  . VAL B 1 88  ? 5.92800   6.65400   22.17000  1.000 26.98053 ? 85  VAL B CA  1 
ATOM   1642 C C   . VAL B 1 88  ? 7.39800   6.38100   22.50400  1.000 26.64917 ? 85  VAL B C   1 
ATOM   1643 O O   . VAL B 1 88  ? 7.87600   6.85300   23.48100  1.000 25.37124 ? 85  VAL B O   1 
ATOM   1644 C CB  . VAL B 1 88  ? 5.83700   8.11200   21.65100  1.000 25.63541 ? 85  VAL B CB  1 
ATOM   1645 C CG1 . VAL B 1 88  ? 6.49500   8.24200   20.30400  1.000 27.61383 ? 85  VAL B CG1 1 
ATOM   1646 C CG2 . VAL B 1 88  ? 4.43200   8.61600   21.52700  1.000 33.44211 ? 85  VAL B CG2 1 
ATOM   1647 N N   . LYS B 1 89  ? 8.08500   5.63600   21.64800  1.000 23.88240 ? 86  LYS B N   1 
ATOM   1648 C CA  . LYS B 1 89  ? 9.47100   5.29600   21.84500  1.000 27.03413 ? 86  LYS B CA  1 
ATOM   1649 C C   . LYS B 1 89  ? 10.37500  6.14300   20.92200  1.000 30.93305 ? 86  LYS B C   1 
ATOM   1650 O O   . LYS B 1 89  ? 10.23200  6.11200   19.73400  1.000 28.59303 ? 86  LYS B O   1 
ATOM   1651 C CB  . LYS B 1 89  ? 9.72400   3.83500   21.56700  1.000 26.51268 ? 86  LYS B CB  1 
ATOM   1652 C CG  . LYS B 1 89  ? 11.11800  3.44200   21.93600  1.000 27.70539 ? 86  LYS B CG  1 
ATOM   1653 C CD  . LYS B 1 89  ? 11.52800  2.16900   21.22400  1.000 45.34358 ? 86  LYS B CD  1 
ATOM   1654 C CE  . LYS B 1 89  ? 11.64400  0.99300   22.15800  1.000 45.97387 ? 86  LYS B CE  1 
ATOM   1655 N NZ  . LYS B 1 89  ? 12.47900  -0.10100  21.56600  1.000 46.88127 ? 86  LYS B NZ  1 
ATOM   1656 N N   . VAL B 1 90  ? 11.31700  6.85900   21.49700  1.000 21.11507 ? 87  VAL B N   1 
ATOM   1657 C CA  . VAL B 1 90  ? 12.16800  7.76200   20.74600  1.000 21.69113 ? 87  VAL B CA  1 
ATOM   1658 C C   . VAL B 1 90  ? 13.60300  7.33800   20.96900  1.000 22.31841 ? 87  VAL B C   1 
ATOM   1659 O O   . VAL B 1 90  ? 14.04400  7.21600   22.11500  1.000 26.03008 ? 87  VAL B O   1 
ATOM   1660 C CB  . VAL B 1 90  ? 11.96500  9.23200   21.17900  1.000 20.67495 ? 87  VAL B CB  1 
ATOM   1661 C CG1 . VAL B 1 90  ? 12.79400  10.15400  20.28900  1.000 22.19938 ? 87  VAL B CG1 1 
ATOM   1662 C CG2 . VAL B 1 90  ? 10.49900  9.66500   21.14000  1.000 21.84594 ? 87  VAL B CG2 1 
ATOM   1663 N N   . LYS B 1 91  ? 14.36300  7.17200   19.89700  1.000 20.39534 ? 88  LYS B N   1 
ATOM   1664 C CA  . LYS B 1 91  ? 15.74700  6.86600   20.01300  1.000 22.69612 ? 88  LYS B CA  1 
ATOM   1665 C C   . LYS B 1 91  ? 16.52000  8.14000   19.68100  1.000 23.34331 ? 88  LYS B C   1 
ATOM   1666 O O   . LYS B 1 91  ? 16.21100  8.80800   18.75000  1.000 26.55435 ? 88  LYS B O   1 
ATOM   1667 C CB  . LYS B 1 91  ? 16.15700  5.74600   19.07800  1.000 29.37716 ? 88  LYS B CB  1 
ATOM   1668 C CG  . LYS B 1 91  ? 15.76500  4.40100   19.62100  1.000 33.42287 ? 88  LYS B CG  1 
ATOM   1669 C CD  . LYS B 1 91  ? 16.64400  3.28700   19.06700  1.000 37.03731 ? 88  LYS B CD  1 
ATOM   1670 C CE  . LYS B 1 91  ? 15.84800  2.03400   18.77300  1.000 50.24042 ? 88  LYS B CE  1 
ATOM   1671 N NZ  . LYS B 1 91  ? 16.70000  0.89200   18.30100  1.000 49.36575 ? 88  LYS B NZ  1 
ATOM   1672 N N   . VAL B 1 92  ? 17.50000  8.47100   20.50200  1.000 21.47783 ? 89  VAL B N   1 
ATOM   1673 C CA  . VAL B 1 92  ? 18.16800  9.71300   20.40500  1.000 21.51521 ? 89  VAL B CA  1 
ATOM   1674 C C   . VAL B 1 92  ? 19.67100  9.56200   20.60100  1.000 22.83761 ? 89  VAL B C   1 
ATOM   1675 O O   . VAL B 1 92  ? 20.10800  8.72500   21.31100  1.000 23.15587 ? 89  VAL B O   1 
ATOM   1676 C CB  . VAL B 1 92  ? 17.64100  10.64900  21.56400  1.000 21.34205 ? 89  VAL B CB  1 
ATOM   1677 C CG1 . VAL B 1 92  ? 18.25100  12.02200  21.57800  1.000 26.32697 ? 89  VAL B CG1 1 
ATOM   1678 C CG2 . VAL B 1 92  ? 16.16800  10.92000  21.51100  1.000 23.94472 ? 89  VAL B CG2 1 
ATOM   1679 N N   . ARG B 1 93  ? 20.49000  10.32700  19.87400  1.000 22.65040 ? 90  ARG B N   1 
ATOM   1680 C CA  . ARG B 1 93  ? 21.90500  10.45100  20.10000  1.000 22.08069 ? 90  ARG B CA  1 
ATOM   1681 C C   . ARG B 1 93  ? 22.05800  11.77500  20.84500  1.000 22.44714 ? 90  ARG B C   1 
ATOM   1682 O O   . ARG B 1 93  ? 21.45300  12.73400  20.48000  1.000 25.77755 ? 90  ARG B O   1 
ATOM   1683 C CB  . ARG B 1 93  ? 22.69800  10.52500  18.80600  1.000 28.82732 ? 90  ARG B CB  1 
ATOM   1684 C CG  . ARG B 1 93  ? 24.20500  10.53900  19.01800  1.000 32.79397 ? 90  ARG B CG  1 
ATOM   1685 C CD  . ARG B 1 93  ? 25.06300  10.68300  17.73400  1.000 39.10172 ? 90  ARG B CD  1 
ATOM   1686 N NE  . ARG B 1 93  ? 26.39500  11.18200  18.12300  1.000 41.41916 ? 90  ARG B NE  1 
ATOM   1687 C CZ  . ARG B 1 93  ? 27.40100  11.57500  17.33400  1.000 54.90842 ? 90  ARG B CZ  1 
ATOM   1688 N NH1 . ARG B 1 93  ? 27.33500  11.49600  16.00800  1.000 57.99621 ? 90  ARG B NH1 1 
ATOM   1689 N NH2 . ARG B 1 93  ? 28.53200  12.00900  17.89400  1.000 49.31973 ? 90  ARG B NH2 1 
ATOM   1690 N N   . ALA B 1 94  ? 22.88800  11.81600  21.85600  1.000 21.16829 ? 91  ALA B N   1 
ATOM   1691 C CA  . ALA B 1 94  ? 23.04900  12.99300  22.71200  1.000 22.98723 ? 91  ALA B CA  1 
ATOM   1692 C C   . ALA B 1 94  ? 24.52800  13.17600  23.00700  1.000 23.55872 ? 91  ALA B C   1 
ATOM   1693 O O   . ALA B 1 94  ? 25.27000  12.19800  23.15500  1.000 25.48456 ? 91  ALA B O   1 
ATOM   1694 C CB  . ALA B 1 94  ? 22.27600  12.85000  24.02800  1.000 23.60472 ? 91  ALA B CB  1 
ATOM   1695 N N   . THR B 1 95  ? 24.95700  14.42500  23.11800  1.000 23.81216 ? 92  THR B N   1 
ATOM   1696 C CA  . THR B 1 95  ? 26.31900  14.71500  23.43800  1.000 24.37602 ? 92  THR B CA  1 
ATOM   1697 C C   . THR B 1 95  ? 26.32700  15.67500  24.61000  1.000 26.39949 ? 92  THR B C   1 
ATOM   1698 O O   . THR B 1 95  ? 25.45200  16.46300  24.73500  1.000 25.33161 ? 92  THR B O   1 
ATOM   1699 C CB  . THR B 1 95  ? 27.08500  15.36800  22.26300  1.000 29.99243 ? 92  THR B CB  1 
ATOM   1700 O OG1 . THR B 1 95  ? 26.46200  16.57900  21.88900  1.000 28.08597 ? 92  THR B OG1 1 
ATOM   1701 C CG2 . THR B 1 95  ? 27.12900  14.47900  21.06900  1.000 32.65241 ? 92  THR B CG2 1 
ATOM   1702 N N   . MET B 1 96  ? 27.31600  15.56000  25.47700  1.000 25.40067 ? 93  MET B N   1 
ATOM   1703 C CA  . MET B 1 96  ? 27.46200  16.43900  26.61200  1.000 24.86670 ? 93  MET B CA  1 
ATOM   1704 C C   . MET B 1 96  ? 28.95200  16.72000  26.78300  1.000 34.90325 ? 93  MET B C   1 
ATOM   1705 O O   . MET B 1 96  ? 29.74500  15.91900  26.42200  1.000 37.97219 ? 93  MET B O   1 
ATOM   1706 C CB  . MET B 1 96  ? 26.88500  15.82000  27.86400  1.000 36.22535 ? 93  MET B CB  1 
ATOM   1707 C CG  . MET B 1 96  ? 25.86200  16.66300  28.54600  1.000 33.81587 ? 93  MET B CG  1 
ATOM   1708 S SD  . MET B 1 96  ? 25.12700  16.02300  30.04000  1.000 34.75387 ? 93  MET B SD  1 
ATOM   1709 C CE  . MET B 1 96  ? 25.91700  14.48000  30.23200  1.000 28.18309 ? 93  MET B CE  1 
ATOM   1710 N N   . VAL B 1 97  ? 29.31100  17.84600  27.35700  1.000 31.51137 ? 94  VAL B N   1 
ATOM   1711 C CA  . VAL B 1 97  ? 30.70800  18.20300  27.52700  1.000 41.04549 ? 94  VAL B CA  1 
ATOM   1712 C C   . VAL B 1 97  ? 31.07900  18.58100  28.94700  1.000 42.90587 ? 94  VAL B C   1 
ATOM   1713 O O   . VAL B 1 97  ? 30.60500  19.57500  29.40900  1.000 41.99786 ? 94  VAL B O   1 
ATOM   1714 C CB  . VAL B 1 97  ? 31.03400  19.43100  26.70300  1.000 34.09686 ? 94  VAL B CB  1 
ATOM   1715 C CG1 . VAL B 1 97  ? 32.46000  19.86500  26.93600  1.000 48.86709 ? 94  VAL B CG1 1 
ATOM   1716 C CG2 . VAL B 1 97  ? 30.80800  19.16600  25.24900  1.000 42.09372 ? 94  VAL B CG2 1 
ATOM   1717 N N   . ARG B 1 98  ? 31.88900  17.76300  29.63000  1.000 46.70835 ? 95  ARG B N   1 
ATOM   1718 C CA  . ARG B 1 98  ? 32.33600  17.99300  30.98000  1.000 49.23399 ? 95  ARG B CA  1 
ATOM   1719 C C   . ARG B 1 98  ? 33.84200  18.15100  30.95400  1.000 50.33010 ? 95  ARG B C   1 
ATOM   1720 O O   . ARG B 1 98  ? 34.54700  17.16900  30.87300  1.000 53.61964 ? 95  ARG B O   1 
ATOM   1721 C CB  . ARG B 1 98  ? 31.94700  16.81700  31.89800  1.000 55.61489 ? 95  ARG B CB  1 
ATOM   1722 C CG  . ARG B 1 98  ? 32.40600  16.90200  33.37600  1.000 67.39015 ? 95  ARG B CG  1 
ATOM   1723 C CD  . ARG B 1 98  ? 31.69700  17.99700  34.16900  1.000 62.80256 ? 95  ARG B CD  1 
ATOM   1724 N NE  . ARG B 1 98  ? 32.02800  18.09500  35.60400  1.000 65.59468 ? 95  ARG B NE  1 
ATOM   1725 C CZ  . ARG B 1 98  ? 33.14800  18.62300  36.12000  1.000 74.84717 ? 95  ARG B CZ  1 
ATOM   1726 N NH1 . ARG B 1 98  ? 34.13700  19.07200  35.33900  1.000 73.83914 ? 95  ARG B NH1 1 
ATOM   1727 N NH2 . ARG B 1 98  ? 33.30800  18.69800  37.43800  1.000 69.42907 ? 95  ARG B NH2 1 
ATOM   1728 N N   . GLN B 1 101 ? 35.79900  17.93700  27.30400  1.000 49.32975 ? 98  GLN B N   1 
ATOM   1729 C CA  . GLN B 1 101 ? 35.66800  16.51700  27.01100  1.000 42.67262 ? 98  GLN B CA  1 
ATOM   1730 C C   . GLN B 1 101 ? 34.25900  16.09400  26.68900  1.000 43.27046 ? 98  GLN B C   1 
ATOM   1731 O O   . GLN B 1 101 ? 33.49100  15.84000  27.56200  1.000 42.20631 ? 98  GLN B O   1 
ATOM   1732 C CB  . GLN B 1 101 ? 36.12500  15.70400  28.19100  1.000 51.83071 ? 98  GLN B CB  1 
ATOM   1733 C CG  . GLN B 1 101 ? 37.59300  15.89700  28.49200  1.000 58.44676 ? 98  GLN B CG  1 
ATOM   1734 C CD  . GLN B 1 101 ? 38.16400  14.79600  29.32000  1.000 59.35216 ? 98  GLN B CD  1 
ATOM   1735 O OE1 . GLN B 1 101 ? 38.22400  13.66300  28.88800  1.000 58.33192 ? 98  GLN B OE1 1 
ATOM   1736 N NE2 . GLN B 1 101 ? 38.59800  15.13100  30.50900  1.000 59.80251 ? 98  GLN B NE2 1 
ATOM   1737 N N   . GLU B 1 102 ? 33.97200  15.99300  25.41600  1.000 39.99432 ? 99  GLU B N   1 
ATOM   1738 C CA  . GLU B 1 102 ? 32.68200  15.59900  24.94800  1.000 41.29959 ? 99  GLU B CA  1 
ATOM   1739 C C   . GLU B 1 102 ? 32.40600  14.13100  25.23500  1.000 45.69987 ? 99  GLU B C   1 
ATOM   1740 O O   . GLU B 1 102 ? 33.27600  13.34100  25.09700  1.000 44.70986 ? 99  GLU B O   1 
ATOM   1741 C CB  . GLU B 1 102 ? 32.61400  15.84300  23.45400  1.000 39.30344 ? 99  GLU B CB  1 
ATOM   1742 C CG  . GLU B 1 102 ? 31.22400  16.03800  22.88900  1.000 43.95143 ? 99  GLU B CG  1 
ATOM   1743 C CD  . GLU B 1 102 ? 31.06700  15.45000  21.51800  1.000 52.40502 ? 99  GLU B CD  1 
ATOM   1744 O OE1 . GLU B 1 102 ? 31.77600  14.46800  21.21100  1.000 59.18589 ? 99  GLU B OE1 1 
ATOM   1745 O OE2 . GLU B 1 102 ? 30.25800  15.97400  20.74100  1.000 52.77225 ? 99  GLU B OE2 1 
ATOM   1746 N N   . HIS B 1 103 ? 31.19300  13.79500  25.66400  1.000 33.00449 ? 100 HIS B N   1 
ATOM   1747 C CA  . HIS B 1 103 ? 30.76800  12.42300  25.91600  1.000 33.61148 ? 100 HIS B CA  1 
ATOM   1748 C C   . HIS B 1 103 ? 29.56300  12.21300  25.03200  1.000 36.28075 ? 100 HIS B C   1 
ATOM   1749 O O   . HIS B 1 103 ? 28.79100  13.11600  24.82300  1.000 28.37131 ? 100 HIS B O   1 
ATOM   1750 C CB  . HIS B 1 103 ? 30.31700  12.21000  27.33000  1.000 34.53163 ? 100 HIS B CB  1 
ATOM   1751 C CG  . HIS B 1 103 ? 31.40800  12.22100  28.33200  1.000 45.53996 ? 100 HIS B CG  1 
ATOM   1752 N ND1 . HIS B 1 103 ? 31.86400  11.08200  28.93600  1.000 43.32686 ? 100 HIS B ND1 1 
ATOM   1753 C CD2 . HIS B 1 103 ? 32.11900  13.23600  28.85700  1.000 45.08575 ? 100 HIS B CD2 1 
ATOM   1754 C CE1 . HIS B 1 103 ? 32.82600  11.39100  29.77700  1.000 45.85770 ? 100 HIS B CE1 1 
ATOM   1755 N NE2 . HIS B 1 103 ? 33.00600  12.69100  29.74000  1.000 47.12405 ? 100 HIS B NE2 1 
ATOM   1756 N N   . VAL B 1 104 ? 29.40500  10.99100  24.55400  1.000 27.49117 ? 101 VAL B N   1 
ATOM   1757 C CA  . VAL B 1 104 ? 28.36500  10.66100  23.60500  1.000 26.35803 ? 101 VAL B CA  1 
ATOM   1758 C C   . VAL B 1 104 ? 27.46100  9.57000   24.12400  1.000 24.79076 ? 101 VAL B C   1 
ATOM   1759 O O   . VAL B 1 104 ? 27.93300  8.61100   24.64700  1.000 27.94554 ? 101 VAL B O   1 
ATOM   1760 C CB  . VAL B 1 104 ? 28.96900  10.18600  22.30100  1.000 31.20121 ? 101 VAL B CB  1 
ATOM   1761 C CG1 . VAL B 1 104 ? 27.93200  10.02500  21.22800  1.000 33.01625 ? 101 VAL B CG1 1 
ATOM   1762 C CG2 . VAL B 1 104 ? 30.01600  11.16800  21.84900  1.000 40.27696 ? 101 VAL B CG2 1 
ATOM   1763 N N   . PHE B 1 105 ? 26.16100  9.73900   23.98000  1.000 23.11115 ? 102 PHE B N   1 
ATOM   1764 C CA  . PHE B 1 105 ? 25.20300  8.78300   24.46500  1.000 20.70329 ? 102 PHE B CA  1 
ATOM   1765 C C   . PHE B 1 105 ? 24.16700  8.34600   23.47100  1.000 23.04473 ? 102 PHE B C   1 
ATOM   1766 O O   . PHE B 1 105 ? 23.90200  9.02100   22.55500  1.000 23.72109 ? 102 PHE B O   1 
ATOM   1767 C CB  . PHE B 1 105 ? 24.43200  9.37700   25.66200  1.000 24.15762 ? 102 PHE B CB  1 
ATOM   1768 C CG  . PHE B 1 105 ? 25.31200  9.96300   26.72300  1.000 21.27541 ? 102 PHE B CG  1 
ATOM   1769 C CD1 . PHE B 1 105 ? 25.82500  11.21800  26.58600  1.000 26.51547 ? 102 PHE B CD1 1 
ATOM   1770 C CD2 . PHE B 1 105 ? 25.61700  9.25300   27.83200  1.000 26.50726 ? 102 PHE B CD2 1 
ATOM   1771 C CE1 . PHE B 1 105 ? 26.64000  11.75000  27.52900  1.000 27.60301 ? 102 PHE B CE1 1 
ATOM   1772 C CE2 . PHE B 1 105 ? 26.42700  9.77300   28.78500  1.000 24.81282 ? 102 PHE B CE2 1 
ATOM   1773 C CZ  . PHE B 1 105 ? 26.93900  11.02800  28.63600  1.000 29.35427 ? 102 PHE B CZ  1 
ATOM   1774 N N   . GLU B 1 106 ? 23.63300  7.15900   23.68500  1.000 20.17054 ? 103 GLU B N   1 
ATOM   1775 C CA  . GLU B 1 106 ? 22.50400  6.66100   22.93900  1.000 21.14329 ? 103 GLU B CA  1 
ATOM   1776 C C   . GLU B 1 106 ? 21.45000  6.52300   23.98800  1.000 23.68212 ? 103 GLU B C   1 
ATOM   1777 O O   . GLU B 1 106 ? 21.68500  5.94300   24.98600  1.000 23.69176 ? 103 GLU B O   1 
ATOM   1778 C CB  . GLU B 1 106 ? 22.71000  5.28700   22.30700  1.000 25.01874 ? 103 GLU B CB  1 
ATOM   1779 C CG  . GLU B 1 106 ? 21.69400  4.96400   21.21200  1.000 29.39056 ? 103 GLU B CG  1 
ATOM   1780 C CD  . GLU B 1 106 ? 20.30100  4.61000   21.69700  1.000 36.79261 ? 103 GLU B CD  1 
ATOM   1781 O OE1 . GLU B 1 106 ? 20.15300  4.18600   22.82200  1.000 38.57042 ? 103 GLU B OE1 1 
ATOM   1782 O OE2 . GLU B 1 106 ? 19.33700  4.73900   20.94300  1.000 38.16264 ? 103 GLU B OE2 1 
ATOM   1783 N N   . VAL B 1 107 ? 20.30300  7.11700   23.76300  1.000 20.44249 ? 104 VAL B N   1 
ATOM   1784 C CA  . VAL B 1 107 ? 19.21800  7.04300   24.69700  1.000 17.54002 ? 104 VAL B CA  1 
ATOM   1785 C C   . VAL B 1 107 ? 17.92100  6.57600   24.06100  1.000 21.05254 ? 104 VAL B C   1 
ATOM   1786 O O   . VAL B 1 107 ? 17.58600  6.99500   23.01700  1.000 23.41113 ? 104 VAL B O   1 
ATOM   1787 C CB  . VAL B 1 107 ? 18.91700  8.43300   25.31600  1.000 21.41418 ? 104 VAL B CB  1 
ATOM   1788 C CG1 . VAL B 1 107 ? 17.94800  8.31100   26.46900  1.000 24.90527 ? 104 VAL B CG1 1 
ATOM   1789 C CG2 . VAL B 1 107 ? 20.19000  9.07100   25.82400  1.000 25.50600 ? 104 VAL B CG2 1 
ATOM   1790 N N   . VAL B 1 108 ? 17.21600  5.68600   24.72500  1.000 21.12613 ? 105 VAL B N   1 
ATOM   1791 C CA  . VAL B 1 108 ? 15.89000  5.30200   24.27000  1.000 18.66216 ? 105 VAL B CA  1 
ATOM   1792 C C   . VAL B 1 108 ? 14.89900  5.86100   25.26600  1.000 22.44906 ? 105 VAL B C   1 
ATOM   1793 O O   . VAL B 1 108 ? 14.91000  5.49900   26.45300  1.000 23.29315 ? 105 VAL B O   1 
ATOM   1794 C CB  . VAL B 1 108 ? 15.73200  3.78000   24.12900  1.000 24.18203 ? 105 VAL B CB  1 
ATOM   1795 C CG1 . VAL B 1 108 ? 14.36200  3.49400   23.54400  1.000 27.45216 ? 105 VAL B CG1 1 
ATOM   1796 C CG2 . VAL B 1 108 ? 16.87200  3.22700   23.28100  1.000 22.25447 ? 105 VAL B CG2 1 
ATOM   1797 N N   . ASP B 1 109 ? 14.12000  6.81400   24.79600  1.000 17.75709 ? 106 ASP B N   1 
ATOM   1798 C CA  . ASP B 1 109 ? 13.13000  7.52800   25.61000  1.000 19.43515 ? 106 ASP B CA  1 
ATOM   1799 C C   . ASP B 1 109 ? 11.75200  6.96800   25.30000  1.000 21.96197 ? 106 ASP B C   1 
ATOM   1800 O O   . ASP B 1 109 ? 11.29100  7.04700   24.14600  1.000 23.19163 ? 106 ASP B O   1 
ATOM   1801 C CB  . ASP B 1 109 ? 13.17200  9.01100   25.26900  1.000 19.80963 ? 106 ASP B CB  1 
ATOM   1802 C CG  . ASP B 1 109 ? 14.32000  9.74600   25.91100  1.000 22.09723 ? 106 ASP B CG  1 
ATOM   1803 O OD1 . ASP B 1 109 ? 14.79600  9.31300   26.99200  1.000 24.17754 ? 106 ASP B OD1 1 
ATOM   1804 O OD2 . ASP B 1 109 ? 14.67700  10.82900  25.36300  1.000 23.23988 ? 106 ASP B OD2 1 
ATOM   1805 N N   . THR B 1 110 ? 11.09900  6.37900   26.29400  1.000 20.51203 ? 107 THR B N   1 
ATOM   1806 C CA  . THR B 1 110 ? 9.72200   5.91800   26.11000  1.000 20.32977 ? 107 THR B CA  1 
ATOM   1807 C C   . THR B 1 110 ? 8.78600   6.80300   26.91300  1.000 21.65772 ? 107 THR B C   1 
ATOM   1808 O O   . THR B 1 110 ? 8.89100   6.85500   28.13700  1.000 23.94583 ? 107 THR B O   1 
ATOM   1809 C CB  . THR B 1 110 ? 9.59100   4.44700   26.50100  1.000 21.29178 ? 107 THR B CB  1 
ATOM   1810 O OG1 . THR B 1 110 ? 10.49300  3.65700   25.69900  1.000 25.00575 ? 107 THR B OG1 1 
ATOM   1811 C CG2 . THR B 1 110 ? 8.15200   3.97500   26.29200  1.000 27.97243 ? 107 THR B CG2 1 
ATOM   1812 N N   . TYR B 1 111 ? 7.87500   7.50000   26.21600  1.000 20.94093 ? 108 TYR B N   1 
ATOM   1813 C CA  . TYR B 1 111 ? 6.98000   8.47200   26.82100  1.000 21.28650 ? 108 TYR B CA  1 
ATOM   1814 C C   . TYR B 1 111 ? 5.59100   7.89600   26.95900  1.000 22.50010 ? 108 TYR B C   1 
ATOM   1815 O O   . TYR B 1 111 ? 5.11700   7.21800   26.05000  1.000 24.65939 ? 108 TYR B O   1 
ATOM   1816 C CB  . TYR B 1 111 ? 6.84100   9.74400   25.98100  1.000 21.65512 ? 108 TYR B CB  1 
ATOM   1817 C CG  . TYR B 1 111 ? 8.10500   10.56000  25.84700  1.000 20.31893 ? 108 TYR B CG  1 
ATOM   1818 C CD1 . TYR B 1 111 ? 9.09000   10.22300  24.93900  1.000 21.60325 ? 108 TYR B CD1 1 
ATOM   1819 C CD2 . TYR B 1 111 ? 8.30900   11.63200  26.67200  1.000 23.15712 ? 108 TYR B CD2 1 
ATOM   1820 C CE1 . TYR B 1 111 ? 10.27200  11.00000  24.82700  1.000 22.07670 ? 108 TYR B CE1 1 
ATOM   1821 C CE2 . TYR B 1 111 ? 9.46300   12.39400  26.59200  1.000 22.07246 ? 108 TYR B CE2 1 
ATOM   1822 C CZ  . TYR B 1 111 ? 10.42600  12.08000  25.66900  1.000 24.38657 ? 108 TYR B CZ  1 
ATOM   1823 O OH  . TYR B 1 111 ? 11.54600  12.84200  25.63900  1.000 25.81661 ? 108 TYR B OH  1 
ATOM   1824 N N   . GLU B 1 112 ? 4.89700   8.30300   28.00800  1.000 23.77002 ? 109 GLU B N   1 
ATOM   1825 C CA  . GLU B 1 112 ? 3.50900   8.04700   28.11500  1.000 25.64848 ? 109 GLU B CA  1 
ATOM   1826 C C   . GLU B 1 112 ? 2.82100   9.42700   28.12700  1.000 25.05576 ? 109 GLU B C   1 
ATOM   1827 O O   . GLU B 1 112 ? 3.10800   10.24200  28.95300  1.000 28.16316 ? 109 GLU B O   1 
ATOM   1828 C CB  . GLU B 1 112 ? 3.15200   7.30700   29.37600  1.000 26.35977 ? 109 GLU B CB  1 
ATOM   1829 C CG  . GLU B 1 112 ? 1.74000   6.84100   29.32400  1.000 36.19977 ? 109 GLU B CG  1 
ATOM   1830 C CD  . GLU B 1 112 ? 1.23400   6.21200   30.58400  1.000 40.71791 ? 109 GLU B CD  1 
ATOM   1831 O OE1 . GLU B 1 112 ? 2.01100   5.98000   31.49400  1.000 43.13473 ? 109 GLU B OE1 1 
ATOM   1832 O OE2 . GLU B 1 112 ? 0.05000   5.96200   30.62900  1.000 43.87217 ? 109 GLU B OE2 1 
ATOM   1833 N N   . PHE B 1 113 ? 1.91100   9.67400   27.20900  1.000 26.03078 ? 110 PHE B N   1 
ATOM   1834 C CA  . PHE B 1 113 ? 1.19400   10.91500  27.19500  1.000 28.80698 ? 110 PHE B CA  1 
ATOM   1835 C C   . PHE B 1 113 ? -0.22300  10.62100  27.64300  1.000 34.05800 ? 110 PHE B C   1 
ATOM   1836 O O   . PHE B 1 113 ? -0.74100  9.58900   27.32900  1.000 31.88188 ? 110 PHE B O   1 
ATOM   1837 C CB  . PHE B 1 113 ? 1.10300   11.48800  25.80000  1.000 29.58948 ? 110 PHE B CB  1 
ATOM   1838 C CG  . PHE B 1 113 ? 2.33500   12.17700  25.33200  1.000 29.54364 ? 110 PHE B CG  1 
ATOM   1839 C CD1 . PHE B 1 113 ? 3.43400   11.45600  24.93900  1.000 29.49436 ? 110 PHE B CD1 1 
ATOM   1840 C CD2 . PHE B 1 113 ? 2.39100   13.53500  25.27000  1.000 29.43053 ? 110 PHE B CD2 1 
ATOM   1841 C CE1 . PHE B 1 113 ? 4.56500   12.07400  24.50900  1.000 30.36896 ? 110 PHE B CE1 1 
ATOM   1842 C CE2 . PHE B 1 113 ? 3.53500   14.15600  24.83400  1.000 29.99959 ? 110 PHE B CE2 1 
ATOM   1843 C CZ  . PHE B 1 113 ? 4.61500   13.42600  24.45100  1.000 27.51744 ? 110 PHE B CZ  1 
ATOM   1844 N N   . ARG B 1 114 ? -0.81800  11.53300  28.39200  1.000 37.69076 ? 111 ARG B N   1 
ATOM   1845 C CA  . ARG B 1 114 ? -2.16600  11.36400  28.86900  1.000 37.48357 ? 111 ARG B CA  1 
ATOM   1846 C C   . ARG B 1 114 ? -2.94500  12.65200  28.55600  1.000 43.92687 ? 111 ARG B C   1 
ATOM   1847 O O   . ARG B 1 114 ? -2.40600  13.71300  28.57000  1.000 37.05948 ? 111 ARG B O   1 
ATOM   1848 C CB  . ARG B 1 114 ? -2.14500  11.05000  30.35000  1.000 42.88528 ? 111 ARG B CB  1 
ATOM   1849 C CG  . ARG B 1 114 ? -3.43700  10.58300  30.96700  1.000 49.77229 ? 111 ARG B CG  1 
ATOM   1850 C CD  . ARG B 1 114 ? -3.17300  9.94200   32.32300  1.000 48.29540 ? 111 ARG B CD  1 
ATOM   1851 N NE  . ARG B 1 114 ? -3.11200  8.50700   32.19200  1.000 54.98249 ? 111 ARG B NE  1 
ATOM   1852 C CZ  . ARG B 1 114 ? -2.26500  7.71400   32.81100  1.000 55.29391 ? 111 ARG B CZ  1 
ATOM   1853 N NH1 . ARG B 1 114 ? -1.36700  8.19600   33.66300  1.000 56.83422 ? 111 ARG B NH1 1 
ATOM   1854 N NH2 . ARG B 1 114 ? -2.32600  6.41800   32.58700  1.000 56.07907 ? 111 ARG B NH2 1 
ATOM   1855 N N   . ARG B 1 115 ? -4.23600  12.51000  28.26700  1.000 47.06254 ? 112 ARG B N   1 
ATOM   1856 C CA  . ARG B 1 115 ? -5.10400  13.61200  27.91200  1.000 43.84005 ? 112 ARG B CA  1 
ATOM   1857 C C   . ARG B 1 115 ? -5.26800  14.56500  29.07200  1.000 47.24265 ? 112 ARG B C   1 
ATOM   1858 O O   . ARG B 1 115 ? -5.52900  14.12800  30.15100  1.000 47.41450 ? 112 ARG B O   1 
ATOM   1859 C CB  . ARG B 1 115 ? -6.47300  13.03300  27.51600  1.000 51.15293 ? 112 ARG B CB  1 
ATOM   1860 C CG  . ARG B 1 115 ? -6.59500  12.54600  26.09000  1.000 48.72457 ? 112 ARG B CG  1 
ATOM   1861 C CD  . ARG B 1 115 ? -7.95500  11.88500  25.82500  1.000 55.62773 ? 112 ARG B CD  1 
ATOM   1862 N NE  . ARG B 1 115 ? -8.65000  12.50700  24.71100  1.000 58.62473 ? 112 ARG B NE  1 
ATOM   1863 C CZ  . ARG B 1 115 ? -8.81900  11.94900  23.51800  1.000 59.33408 ? 112 ARG B CZ  1 
ATOM   1864 N NH1 . ARG B 1 115 ? -8.39200  10.72700  23.29300  1.000 48.76447 ? 112 ARG B NH1 1 
ATOM   1865 N NH2 . ARG B 1 115 ? -9.44500  12.62200  22.55800  1.000 58.36259 ? 112 ARG B NH2 1 
ATOM   1866 N N   . LYS B 1 116 ? -5.00400  15.84700  28.90300  1.000 51.41906 ? 113 LYS B N   1 
ATOM   1867 C CA  . LYS B 1 116 ? -5.21300  16.84400  29.95200  1.000 57.73028 ? 113 LYS B CA  1 
ATOM   1868 C C   . LYS B 1 116 ? -5.98900  17.99400  29.31100  1.000 57.94448 ? 113 LYS B C   1 
ATOM   1869 O O   . LYS B 1 116 ? -5.40700  19.01700  28.93700  1.000 64.41294 ? 113 LYS B O   1 
ATOM   1870 C CB  . LYS B 1 116 ? -3.88400  17.31000  30.56400  1.000 57.45382 ? 113 LYS B CB  1 
ATOM   1871 C CG  . LYS B 1 116 ? -3.70500  16.90500  32.02700  1.000 56.30190 ? 113 LYS B CG  1 
ATOM   1872 C CD  . LYS B 1 116 ? -3.38600  15.41800  32.17700  1.000 50.21120 ? 113 LYS B CD  1 
ATOM   1873 C CE  . LYS B 1 116 ? -3.59000  14.95200  33.60900  1.000 52.79014 ? 113 LYS B CE  1 
ATOM   1874 N NZ  . LYS B 1 116 ? -3.05800  13.57800  33.83400  1.000 48.51642 ? 113 LYS B NZ  1 
ATOM   1875 N N   . GLY B 1 117 ? -7.29600  17.81200  29.17600  1.000 61.96193 ? 114 GLY B N   1 
ATOM   1876 C CA  . GLY B 1 117 ? -8.15000  18.84300  28.58500  1.000 53.63447 ? 114 GLY B CA  1 
ATOM   1877 C C   . GLY B 1 117 ? -8.20700  18.73100  27.05900  1.000 54.34768 ? 114 GLY B C   1 
ATOM   1878 O O   . GLY B 1 117 ? -8.54700  17.67900  26.53400  1.000 60.84165 ? 114 GLY B O   1 
ATOM   1879 N N   . ASP B 1 118 ? -7.87900  19.83500  26.38800  1.000 62.23643 ? 115 ASP B N   1 
ATOM   1880 C CA  . ASP B 1 118 ? -7.91200  19.87800  24.92500  1.000 65.36482 ? 115 ASP B CA  1 
ATOM   1881 C C   . ASP B 1 118 ? -6.66100  19.28200  24.28700  1.000 65.59543 ? 115 ASP B C   1 
ATOM   1882 O O   . ASP B 1 118 ? -6.62800  19.10400  23.06200  1.000 68.46594 ? 115 ASP B O   1 
ATOM   1883 C CB  . ASP B 1 118 ? -8.09500  21.32600  24.45000  1.000 62.51664 ? 115 ASP B CB  1 
ATOM   1884 C CG  . ASP B 1 118 ? -9.51900  21.81600  24.61500  1.000 72.11455 ? 115 ASP B CG  1 
ATOM   1885 O OD1 . ASP B 1 118 ? -9.85600  22.31600  25.71000  1.000 72.39422 ? 115 ASP B OD1 1 
ATOM   1886 O OD2 . ASP B 1 118 ? -10.30300 21.70000  23.64700  1.000 69.33697 ? 115 ASP B OD2 1 
ATOM   1887 N N   . SER B 1 119 ? -5.64000  18.95800  25.07800  1.000 60.01524 ? 116 SER B N   1 
ATOM   1888 C CA  . SER B 1 119 ? -4.38100  18.47200  24.53700  1.000 55.40928 ? 116 SER B CA  1 
ATOM   1889 C C   . SER B 1 119 ? -3.80800  17.40100  25.45300  1.000 53.44216 ? 116 SER B C   1 
ATOM   1890 O O   . SER B 1 119 ? -4.41800  17.00500  26.45400  1.000 62.03629 ? 116 SER B O   1 
ATOM   1891 C CB  . SER B 1 119 ? -3.37300  19.61400  24.35600  1.000 58.77245 ? 116 SER B CB  1 
ATOM   1892 O OG  . SER B 1 119 ? -3.02100  20.18200  25.60800  1.000 57.28884 ? 116 SER B OG  1 
ATOM   1893 N N   . TRP B 1 120 ? -2.67200  16.82900  25.10000  1.000 43.28148 ? 117 TRP B N   1 
ATOM   1894 C CA  . TRP B 1 120 ? -2.00900  15.83200  25.86200  1.000 42.16632 ? 117 TRP B CA  1 
ATOM   1895 C C   . TRP B 1 120 ? -0.76900  16.40000  26.56600  1.000 36.79079 ? 117 TRP B C   1 
ATOM   1896 O O   . TRP B 1 120 ? -0.22200  17.36800  26.14000  1.000 37.56353 ? 117 TRP B O   1 
ATOM   1897 C CB  . TRP B 1 120 ? -1.54500  14.75600  24.89800  1.000 42.30155 ? 117 TRP B CB  1 
ATOM   1898 C CG  . TRP B 1 120 ? -2.60900  14.12800  24.06600  1.000 46.75196 ? 117 TRP B CG  1 
ATOM   1899 C CD1 . TRP B 1 120 ? -3.17900  14.63600  22.95500  1.000 49.48360 ? 117 TRP B CD1 1 
ATOM   1900 C CD2 . TRP B 1 120 ? -3.18000  12.83800  24.25600  1.000 42.94976 ? 117 TRP B CD2 1 
ATOM   1901 N NE1 . TRP B 1 120 ? -4.09200  13.76400  22.45000  1.000 49.64496 ? 117 TRP B NE1 1 
ATOM   1902 C CE2 . TRP B 1 120 ? -4.12200  12.65000  23.24200  1.000 45.66825 ? 117 TRP B CE2 1 
ATOM   1903 C CE3 . TRP B 1 120 ? -3.01100  11.83400  25.20700  1.000 40.05530 ? 117 TRP B CE3 1 
ATOM   1904 C CZ2 . TRP B 1 120 ? -4.88200  11.49400  23.14600  1.000 45.08272 ? 117 TRP B CZ2 1 
ATOM   1905 C CZ3 . TRP B 1 120 ? -3.76100  10.69900  25.11100  1.000 39.12346 ? 117 TRP B CZ3 1 
ATOM   1906 C CH2 . TRP B 1 120 ? -4.67700  10.53100  24.09000  1.000 45.18336 ? 117 TRP B CH2 1 
ATOM   1907 N N   . LYS B 1 121 ? -0.37800  15.78800  27.66500  1.000 33.79507 ? 118 LYS B N   1 
ATOM   1908 C CA  . LYS B 1 121 ? 0.82200   16.13800  28.40800  1.000 32.29053 ? 118 LYS B CA  1 
ATOM   1909 C C   . LYS B 1 121 ? 1.59900   14.87300  28.73100  1.000 31.59528 ? 118 LYS B C   1 
ATOM   1910 O O   . LYS B 1 121 ? 1.02400   13.79000  28.88500  1.000 27.78176 ? 118 LYS B O   1 
ATOM   1911 C CB  . LYS B 1 121 ? 0.52600   16.86700  29.72000  1.000 34.70249 ? 118 LYS B CB  1 
ATOM   1912 C CG  . LYS B 1 121 ? -0.29100  18.13700  29.56800  1.000 41.37651 ? 118 LYS B CG  1 
ATOM   1913 C CD  . LYS B 1 121 ? 0.47500   19.21900  28.84700  1.000 37.80380 ? 118 LYS B CD  1 
ATOM   1914 C CE  . LYS B 1 121 ? -0.29000  20.53800  28.89800  1.000 44.08163 ? 118 LYS B CE  1 
ATOM   1915 N NZ  . LYS B 1 121 ? 0.52100   21.68100  28.38700  1.000 42.24744 ? 118 LYS B NZ  1 
ATOM   1916 N N   . ILE B 1 122 ? 2.89800   15.00200  28.86500  1.000 25.78564 ? 119 ILE B N   1 
ATOM   1917 C CA  . ILE B 1 122 ? 3.70900   13.88900  29.23800  1.000 24.21331 ? 119 ILE B CA  1 
ATOM   1918 C C   . ILE B 1 122 ? 3.42000   13.55500  30.70200  1.000 27.50858 ? 119 ILE B C   1 
ATOM   1919 O O   . ILE B 1 122 ? 3.44100   14.43600  31.52000  1.000 27.59029 ? 119 ILE B O   1 
ATOM   1920 C CB  . ILE B 1 122 ? 5.19000   14.27600  29.11900  1.000 27.27847 ? 119 ILE B CB  1 
ATOM   1921 C CG1 . ILE B 1 122 ? 5.56500   14.42700  27.66500  1.000 23.76266 ? 119 ILE B CG1 1 
ATOM   1922 C CG2 . ILE B 1 122 ? 6.07600   13.27400  29.81900  1.000 24.47758 ? 119 ILE B CG2 1 
ATOM   1923 C CD1 . ILE B 1 122 ? 6.90700   15.08000  27.43800  1.000 27.46924 ? 119 ILE B CD1 1 
ATOM   1924 N N   . VAL B 1 123 ? 3.06900   12.32200  31.00900  1.000 26.12706 ? 120 VAL B N   1 
ATOM   1925 C CA  . VAL B 1 123 ? 2.90900   11.94000  32.38900  1.000 27.27267 ? 120 VAL B CA  1 
ATOM   1926 C C   . VAL B 1 123 ? 3.96600   10.96500  32.87200  1.000 27.95915 ? 120 VAL B C   1 
ATOM   1927 O O   . VAL B 1 123 ? 4.08000   10.74500  34.04100  1.000 27.89505 ? 120 VAL B O   1 
ATOM   1928 C CB  . VAL B 1 123 ? 1.52100   11.34800  32.69000  1.000 30.79508 ? 120 VAL B CB  1 
ATOM   1929 C CG1 . VAL B 1 123 ? 0.46000   12.39600  32.47800  1.000 31.68905 ? 120 VAL B CG1 1 
ATOM   1930 C CG2 . VAL B 1 123 ? 1.25500   10.12300  31.85700  1.000 30.90972 ? 120 VAL B CG2 1 
ATOM   1931 N N   . LYS B 1 124 ? 4.71200   10.38600  31.96100  1.000 24.22638 ? 121 LYS B N   1 
ATOM   1932 C CA  . LYS B 1 124 ? 5.76600   9.48500   32.32100  1.000 23.90764 ? 121 LYS B CA  1 
ATOM   1933 C C   . LYS B 1 124 ? 6.78200   9.35300   31.22500  1.000 24.00678 ? 121 LYS B C   1 
ATOM   1934 O O   . LYS B 1 124 ? 6.49100   9.36300   30.11100  1.000 26.02258 ? 121 LYS B O   1 
ATOM   1935 C CB  . LYS B 1 124 ? 5.24500   8.08400   32.67700  1.000 25.70666 ? 121 LYS B CB  1 
ATOM   1936 C CG  . LYS B 1 124 ? 6.27600   7.19100   33.34100  1.000 28.68725 ? 121 LYS B CG  1 
ATOM   1937 C CD  . LYS B 1 124 ? 5.77700   5.80400   33.62200  1.000 34.75461 ? 121 LYS B CD  1 
ATOM   1938 C CE  . LYS B 1 124 ? 6.59700   5.13100   34.68900  1.000 36.08308 ? 121 LYS B CE  1 
ATOM   1939 N NZ  . LYS B 1 124 ? 6.04100   3.83300   35.13700  1.000 45.50672 ? 121 LYS B NZ  1 
ATOM   1940 N N   . LEU B 1 125 ? 8.00000   9.33800   31.63600  1.000 21.29930 ? 122 LEU B N   1 
ATOM   1941 C CA  A LEU B 1 125 ? 9.14200   9.11400   30.71900  0.819 21.19966 ? 122 LEU B CA  1 
ATOM   1942 C CA  B LEU B 1 125 ? 9.14100   9.12700   30.72000  0.181 21.37258 ? 122 LEU B CA  1 
ATOM   1943 C C   . LEU B 1 125 ? 10.25500  8.09400   31.31500  1.000 26.13454 ? 122 LEU B C   1 
ATOM   1944 O O   . LEU B 1 125 ? 10.71700  8.09700   32.53100  1.000 27.19186 ? 122 LEU B O   1 
ATOM   1945 C CB  A LEU B 1 125 ? 9.87200   10.41100  30.38700  0.819 23.13203 ? 122 LEU B CB  1 
ATOM   1946 C CB  B LEU B 1 125 ? 9.81500   10.46300  30.41700  0.181 23.19774 ? 122 LEU B CB  1 
ATOM   1947 C CG  A LEU B 1 125 ? 11.27700  10.21000  29.80900  0.819 26.65660 ? 122 LEU B CG  1 
ATOM   1948 C CG  B LEU B 1 125 ? 11.00800  10.59000  29.46500  0.181 25.62323 ? 122 LEU B CG  1 
ATOM   1949 C CD1 A LEU B 1 125 ? 11.24600  9.44100   28.50700  0.819 24.30712 ? 122 LEU B CD1 1 
ATOM   1950 C CD1 B LEU B 1 125 ? 12.28100  11.05300  30.13700  0.181 27.00820 ? 122 LEU B CD1 1 
ATOM   1951 C CD2 A LEU B 1 125 ? 12.00400  11.51400  29.63200  0.819 28.87051 ? 122 LEU B CD2 1 
ATOM   1952 C CD2 B LEU B 1 125 ? 11.24400  9.41800   28.52900  0.181 24.30188 ? 122 LEU B CD2 1 
ATOM   1953 N N   . VAL B 1 126 ? 10.46800  7.02300   30.57500  1.000 21.49054 ? 123 VAL B N   1 
ATOM   1954 C CA  . VAL B 1 126 ? 11.46900  6.08000   30.99800  1.000 22.96306 ? 123 VAL B CA  1 
ATOM   1955 C C   . VAL B 1 126 ? 12.62900  6.18400   30.02800  1.000 24.97058 ? 123 VAL B C   1 
ATOM   1956 O O   . VAL B 1 126 ? 12.43600  5.96400   28.88400  1.000 26.90049 ? 123 VAL B O   1 
ATOM   1957 C CB  . VAL B 1 126 ? 10.99200  4.64300   30.95300  1.000 26.69329 ? 123 VAL B CB  1 
ATOM   1958 C CG1 . VAL B 1 126 ? 12.11900  3.72900   31.34200  1.000 26.25200 ? 123 VAL B CG1 1 
ATOM   1959 C CG2 . VAL B 1 126 ? 9.80800   4.46200   31.85500  1.000 30.78995 ? 123 VAL B CG2 1 
ATOM   1960 N N   . SER B 1 127 ? 13.79300  6.57100   30.51100  1.000 22.99040 ? 124 SER B N   1 
ATOM   1961 C CA  . SER B 1 127 ? 14.94800  6.70000   29.67400  1.000 24.64094 ? 124 SER B CA  1 
ATOM   1962 C C   . SER B 1 127 ? 15.98400  5.68700   29.95600  1.000 29.48525 ? 124 SER B C   1 
ATOM   1963 O O   . SER B 1 127 ? 16.39500  5.52100   31.03200  1.000 22.87727 ? 124 SER B O   1 
ATOM   1964 C CB  . SER B 1 127 ? 15.67000  8.02000   29.85100  1.000 28.96065 ? 124 SER B CB  1 
ATOM   1965 O OG  . SER B 1 127 ? 14.82900  9.12500   29.74900  1.000 29.20599 ? 124 SER B OG  1 
ATOM   1966 N N   . GLU B 1 128 ? 16.33400  4.99200   28.91100  1.000 21.88443 ? 125 GLU B N   1 
ATOM   1967 C CA  A GLU B 1 128 ? 17.45000  4.03000   28.91300  0.666 22.43944 ? 125 GLU B CA  1 
ATOM   1968 C CA  B GLU B 1 128 ? 17.47600  4.02900   28.94000  0.334 22.53821 ? 125 GLU B CA  1 
ATOM   1969 C C   . GLU B 1 128 ? 18.79800  4.65800   28.22500  1.000 19.40656 ? 125 GLU B C   1 
ATOM   1970 O O   . GLU B 1 128 ? 18.95000  5.06900   27.03600  1.000 22.63179 ? 125 GLU B O   1 
ATOM   1971 C CB  A GLU B 1 128 ? 17.05900  2.81600   28.11500  0.666 27.16811 ? 125 GLU B CB  1 
ATOM   1972 C CB  B GLU B 1 128 ? 17.15400  2.71300   28.25100  0.334 27.34329 ? 125 GLU B CB  1 
ATOM   1973 C CG  A GLU B 1 128 ? 17.93100  1.63600   28.39900  0.666 29.49868 ? 125 GLU B CG  1 
ATOM   1974 C CG  B GLU B 1 128 ? 18.04000  1.54400   28.68800  0.334 29.71924 ? 125 GLU B CG  1 
ATOM   1975 C CD  A GLU B 1 128 ? 17.51900  0.97500   29.67500  0.666 28.80547 ? 125 GLU B CD  1 
ATOM   1976 C CD  B GLU B 1 128 ? 19.55000  1.75900   28.49500  0.334 33.17631 ? 125 GLU B CD  1 
ATOM   1977 O OE1 A GLU B 1 128 ? 16.33700  0.66900   29.80200  0.666 32.11822 ? 125 GLU B OE1 1 
ATOM   1978 O OE1 B GLU B 1 128 ? 19.99900  2.03600   27.36100  0.334 31.97209 ? 125 GLU B OE1 1 
ATOM   1979 O OE2 A GLU B 1 128 ? 18.37200  0.79900   30.54500  0.666 32.99742 ? 125 GLU B OE2 1 
ATOM   1980 O OE2 B GLU B 1 128 ? 20.31800  1.61200   29.46400  0.334 27.73070 ? 125 GLU B OE2 1 
ATOM   1981 N N   . ILE B 1 129 ? 19.69300  5.00000   29.10800  1.000 19.76462 ? 126 ILE B N   1 
ATOM   1982 C CA  . ILE B 1 129 ? 20.90000  5.66400   28.73900  1.000 21.35092 ? 126 ILE B CA  1 
ATOM   1983 C C   . ILE B 1 129 ? 22.16400  4.84200   28.67500  1.000 24.38439 ? 126 ILE B C   1 
ATOM   1984 O O   . ILE B 1 129 ? 22.49000  4.21300   29.60600  1.000 25.77881 ? 126 ILE B O   1 
ATOM   1985 C CB  . ILE B 1 129 ? 21.14800  6.83400   29.70900  1.000 25.28516 ? 126 ILE B CB  1 
ATOM   1986 C CG1 . ILE B 1 129 ? 19.92100  7.73600   29.77400  1.000 33.15192 ? 126 ILE B CG1 1 
ATOM   1987 C CG2 . ILE B 1 129 ? 22.39400  7.59200   29.34200  1.000 25.53822 ? 126 ILE B CG2 1 
ATOM   1988 C CD1 . ILE B 1 129 ? 19.79400  8.52600   31.04400  1.000 33.11078 ? 126 ILE B CD1 1 
ATOM   1989 N N   . THR B 1 130 ? 22.83000  4.90200   27.53700  1.000 21.34102 ? 127 THR B N   1 
ATOM   1990 C CA  . THR B 1 130 ? 24.06700  4.22600   27.29000  1.000 23.34261 ? 127 THR B CA  1 
ATOM   1991 C C   . THR B 1 130 ? 25.14700  5.21500   26.89400  1.000 28.14850 ? 127 THR B C   1 
ATOM   1992 O O   . THR B 1 130 ? 24.94700  6.02200   26.02700  1.000 24.58914 ? 127 THR B O   1 
ATOM   1993 C CB  . THR B 1 130 ? 23.90700  3.22000   26.13800  1.000 29.83290 ? 127 THR B CB  1 
ATOM   1994 O OG1 . THR B 1 130 ? 22.94000  2.26600   26.50700  1.000 29.25434 ? 127 THR B OG1 1 
ATOM   1995 C CG2 . THR B 1 130 ? 25.22300  2.55700   25.79500  1.000 30.59014 ? 127 THR B CG2 1 
ATOM   1996 N N   . GLN B 1 131 ? 26.27400  5.14600   27.57800  1.000 22.26208 ? 128 GLN B N   1 
ATOM   1997 C CA  . GLN B 1 131 ? 27.40300  5.99100   27.25100  1.000 25.91034 ? 128 GLN B CA  1 
ATOM   1998 C C   . GLN B 1 131 ? 28.28100  5.28100   26.22600  1.000 30.79171 ? 128 GLN B C   1 
ATOM   1999 O O   . GLN B 1 131 ? 28.81600  4.19700   26.50500  1.000 28.37193 ? 128 GLN B O   1 
ATOM   2000 C CB  . GLN B 1 131 ? 28.21600  6.34200   28.48800  1.000 29.68244 ? 128 GLN B CB  1 
ATOM   2001 C CG  . GLN B 1 131 ? 29.44300  7.17800   28.13200  1.000 32.38752 ? 128 GLN B CG  1 
ATOM   2002 C CD  . GLN B 1 131 ? 29.95700  8.01600   29.27800  1.000 40.68822 ? 128 GLN B CD  1 
ATOM   2003 O OE1 . GLN B 1 131 ? 30.69700  8.97500   29.06300  1.000 47.98225 ? 128 GLN B OE1 1 
ATOM   2004 N NE2 . GLN B 1 131 ? 29.56100  7.67300   30.49900  1.000 41.66440 ? 128 GLN B NE2 1 
ATOM   2005 N N   . LEU B 1 132 ? 28.39000  5.83200   25.02100  1.000 26.73335 ? 129 LEU B N   1 
ATOM   2006 C CA  . LEU B 1 132 ? 29.10900  5.21300   23.94300  1.000 33.16589 ? 129 LEU B CA  1 
ATOM   2007 C C   . LEU B 1 132 ? 30.57600  5.44300   23.97000  1.000 39.89959 ? 129 LEU B C   1 
ATOM   2008 O O   . LEU B 1 132 ? 31.33200  4.56300   23.61300  1.000 46.19448 ? 129 LEU B O   1 
ATOM   2009 C CB  . LEU B 1 132 ? 28.56000  5.68300   22.60800  1.000 30.69146 ? 129 LEU B CB  1 
ATOM   2010 C CG  . LEU B 1 132 ? 27.12400  5.32300   22.32100  1.000 27.41334 ? 129 LEU B CG  1 
ATOM   2011 C CD1 . LEU B 1 132 ? 26.71600  5.77900   20.95700  1.000 33.82503 ? 129 LEU B CD1 1 
ATOM   2012 C CD2 . LEU B 1 132 ? 26.86400  3.85200   22.45400  1.000 34.01800 ? 129 LEU B CD2 1 
ATOM   2013 N N   . GLY B 1 133 ? 30.98100  6.61400   24.38600  1.000 32.81768 ? 130 GLY B N   1 
ATOM   2014 C CA  . GLY B 1 133 ? 32.37600  6.95800   24.46000  1.000 45.84099 ? 130 GLY B CA  1 
ATOM   2015 C C   . GLY B 1 133 ? 32.63100  8.38800   24.01000  1.000 47.64848 ? 130 GLY B C   1 
ATOM   2016 O O   . GLY B 1 133 ? 32.00000  9.31400   24.52200  1.000 48.39529 ? 130 GLY B O   1 
ATOM   2017 N N   . SER B 1 134 ? 33.58700  8.55600   23.11400  1.000 53.28575 ? 131 SER B N   1 
ATOM   2018 C CA  . SER B 1 134 ? 33.96900  9.79100   22.44800  1.000 50.69795 ? 131 SER B CA  1 
ATOM   2019 C C   . SER B 1 134 ? 33.63700  11.14000  22.98500  1.000 52.94985 ? 131 SER B C   1 
ATOM   2020 O O   . SER B 1 134 ? 33.94800  12.13200  22.32900  1.000 58.79028 ? 131 SER B O   1 
ATOM   2021 C CB  . SER B 1 134 ? 33.48900  9.67700   21.01400  1.000 51.60611 ? 131 SER B CB  1 
ATOM   2022 O OG  . SER B 1 134 ? 33.75500  8.37800   20.50500  1.000 62.93542 ? 131 SER B OG  1 
HETATM 2023 C C1  . HCY C 2 .   ? 23.73700  -1.19000  -4.51000  1.000 27.98124 ? 201 HCY A C1  1 
HETATM 2024 C C2  . HCY C 2 .   ? 24.75200  -0.92500  -5.06700  1.000 29.69453 ? 201 HCY A C2  1 
HETATM 2025 C C3  . HCY C 2 .   ? 25.80500  -0.03500  -4.15600  1.000 38.51518 ? 201 HCY A C3  1 
HETATM 2026 C C4  . HCY C 2 .   ? 25.83400  -0.25300  -2.70100  1.000 24.85001 ? 201 HCY A C4  1 
HETATM 2027 C C5  . HCY C 2 .   ? 24.87800  -1.17800  -2.14300  1.000 23.28823 ? 201 HCY A C5  1 
HETATM 2028 C C6  . HCY C 2 .   ? 24.82700  -1.49400  -0.54800  1.000 24.52542 ? 201 HCY A C6  1 
HETATM 2029 C C7  . HCY C 2 .   ? 23.54400  -1.26800  0.01400   1.000 23.76913 ? 201 HCY A C7  1 
HETATM 2030 C C8  . HCY C 2 .   ? 22.53200  -1.99400  -0.70700  1.000 21.56468 ? 201 HCY A C8  1 
HETATM 2031 C C9  . HCY C 2 .   ? 22.55500  -1.62900  -2.21700  1.000 23.58856 ? 201 HCY A C9  1 
HETATM 2032 C C10 . HCY C 2 .   ? 23.90800  -1.85500  -2.86400  1.000 21.77830 ? 201 HCY A C10 1 
HETATM 2033 C C12 . HCY C 2 .   ? 19.90800  -1.95100  -2.25000  1.000 22.01428 ? 201 HCY A C12 1 
HETATM 2034 C C11 . HCY C 2 .   ? 21.29400  -2.29000  -3.01300  1.000 20.44745 ? 201 HCY A C11 1 
HETATM 2035 C C13 . HCY C 2 .   ? 19.86500  -2.33900  -0.75600  1.000 17.75968 ? 201 HCY A C13 1 
HETATM 2036 C C14 . HCY C 2 .   ? 21.17600  -1.64400  -0.01500  1.000 21.14605 ? 201 HCY A C14 1 
HETATM 2037 C C15 . HCY C 2 .   ? 20.97600  -1.85600  1.30000   1.000 19.85305 ? 201 HCY A C15 1 
HETATM 2038 C C16 . HCY C 2 .   ? 19.38700  -1.91200  1.48500   1.000 23.96865 ? 201 HCY A C16 1 
HETATM 2039 C C17 . HCY C 2 .   ? 18.99100  -1.70300  0.00800   1.000 22.71269 ? 201 HCY A C17 1 
HETATM 2040 C C18 . HCY C 2 .   ? 19.90900  -3.88800  -0.55900  1.000 19.77369 ? 201 HCY A C18 1 
HETATM 2041 C C19 . HCY C 2 .   ? 24.25300  -3.35200  -2.95000  1.000 19.23073 ? 201 HCY A C19 1 
HETATM 2042 C C20 . HCY C 2 .   ? 17.63200  -2.52900  -0.00500  1.000 27.28124 ? 201 HCY A C20 1 
HETATM 2043 C C21 . HCY C 2 .   ? 16.58800  -2.17600  -1.06400  1.000 22.97763 ? 201 HCY A C21 1 
HETATM 2044 O O1  . HCY C 2 .   ? 26.52700  0.72900   -4.63400  1.000 43.79201 ? 201 HCY A O1  1 
HETATM 2045 O O2  . HCY C 2 .   ? 21.46100  -3.57500  -3.15600  1.000 24.04649 ? 201 HCY A O2  1 
HETATM 2046 O O3  . HCY C 2 .   ? 18.52700  -0.47400  -0.35600  1.000 21.12404 ? 201 HCY A O3  1 
HETATM 2047 O O4  . HCY C 2 .   ? 17.30400  -3.34400  0.74700   1.000 26.07431 ? 201 HCY A O4  1 
HETATM 2048 O O5  . HCY C 2 .   ? 15.39400  -2.96000  -0.96600  1.000 23.99802 ? 201 HCY A O5  1 
HETATM 2049 C C1  . HCY D 2 .   ? 21.00500  12.07100  32.44800  1.000 29.34482 ? 201 HCY B C1  1 
HETATM 2050 C C2  . HCY D 2 .   ? 21.95400  11.87600  33.11700  1.000 34.00020 ? 201 HCY B C2  1 
HETATM 2051 C C3  . HCY D 2 .   ? 23.07400  10.92700  32.37100  1.000 37.88209 ? 201 HCY B C3  1 
HETATM 2052 C C4  . HCY D 2 .   ? 23.42300  11.24900  30.96800  1.000 28.78580 ? 201 HCY B C4  1 
HETATM 2053 C C5  . HCY D 2 .   ? 22.55500  12.18700  30.29900  1.000 25.87339 ? 201 HCY B C5  1 
HETATM 2054 C C6  . HCY D 2 .   ? 22.76800  12.62900  28.75900  1.000 27.71595 ? 201 HCY B C6  1 
HETATM 2055 C C7  . HCY D 2 .   ? 21.58400  12.38800  28.01700  1.000 24.74864 ? 201 HCY B C7  1 
HETATM 2056 C C8  . HCY D 2 .   ? 20.41400  12.99300  28.61100  1.000 24.04983 ? 201 HCY B C8  1 
HETATM 2057 C C9  . HCY D 2 .   ? 20.21400  12.55600  30.06600  1.000 24.53947 ? 201 HCY B C9  1 
HETATM 2058 C C10 . HCY D 2 .   ? 21.44800  12.79000  30.89400  1.000 23.86319 ? 201 HCY B C10 1 
HETATM 2059 C C12 . HCY D 2 .   ? 17.57300  12.90700  29.75300  1.000 21.70780 ? 201 HCY B C12 1 
HETATM 2060 C C11 . HCY D 2 .   ? 18.84500  13.15600  30.71100  1.000 23.29010 ? 201 HCY B C11 1 
HETATM 2061 C C13 . HCY D 2 .   ? 17.72700  13.28600  28.27000  1.000 22.74285 ? 201 HCY B C13 1 
HETATM 2062 C C14 . HCY D 2 .   ? 19.15400  12.65800  27.72700  1.000 22.87960 ? 201 HCY B C14 1 
HETATM 2063 C C15 . HCY D 2 .   ? 19.11100  12.89700  26.40400  1.000 24.53825 ? 201 HCY B C15 1 
HETATM 2064 C C16 . HCY D 2 .   ? 17.56100  12.80800  26.00100  1.000 25.36190 ? 201 HCY B C16 1 
HETATM 2065 C C17 . HCY D 2 .   ? 16.99200  12.57800  27.42700  1.000 26.28741 ? 201 HCY B C17 1 
HETATM 2066 C C18 . HCY D 2 .   ? 17.74300  14.83300  28.05200  1.000 25.23483 ? 201 HCY B C18 1 
HETATM 2067 C C19 . HCY D 2 .   ? 21.75100  14.26500  31.16200  1.000 22.93955 ? 201 HCY B C19 1 
HETATM 2068 C C20 . HCY D 2 .   ? 15.61900  13.34400  27.32600  1.000 27.49392 ? 201 HCY B C20 1 
HETATM 2069 C C21 . HCY D 2 .   ? 14.45900  12.97000  28.27900  1.000 26.15937 ? 201 HCY B C21 1 
HETATM 2070 O O1  . HCY D 2 .   ? 23.56000  10.00500  32.87800  1.000 49.16417 ? 201 HCY B O1  1 
HETATM 2071 O O2  . HCY D 2 .   ? 18.98100  14.41500  30.95700  1.000 27.30494 ? 201 HCY B O2  1 
HETATM 2072 O O3  . HCY D 2 .   ? 16.46400  11.35400  27.74200  1.000 23.91829 ? 201 HCY B O3  1 
HETATM 2073 O O4  . HCY D 2 .   ? 15.38600  14.16900  26.54900  1.000 26.38655 ? 201 HCY B O4  1 
HETATM 2074 O O5  . HCY D 2 .   ? 13.31000  13.76600  28.10800  1.000 27.72107 ? 201 HCY B O5  1 
HETATM 2075 S S   . SO4 E 3 .   ? 4.13500   22.81800  37.11600  1.000 85.84612 ? 202 SO4 B S   1 
HETATM 2076 O O1  . SO4 E 3 .   ? 3.50500   21.98600  36.12800  1.000 48.72931 ? 202 SO4 B O1  1 
HETATM 2077 O O2  . SO4 E 3 .   ? 4.65900   24.02400  36.51300  1.000 62.55171 ? 202 SO4 B O2  1 
HETATM 2078 O O3  . SO4 E 3 .   ? 3.01400   23.12000  37.99300  1.000 71.65644 ? 202 SO4 B O3  1 
HETATM 2079 O O4  . SO4 E 3 .   ? 5.15200   22.19900  37.94100  1.000 60.03652 ? 202 SO4 B O4  1 
HETATM 2080 O O   . HOH F 4 .   ? 5.74800   0.55200   -10.36800 1.000 43.21655 ? 301 HOH A O   1 
HETATM 2081 O O   . HOH F 4 .   ? 14.73700  -7.54100  -17.63500 1.000 45.82368 ? 302 HOH A O   1 
HETATM 2082 O O   . HOH F 4 .   ? 26.07800  -5.41800  8.87900   1.000 45.35481 ? 303 HOH A O   1 
HETATM 2083 O O   . HOH F 4 .   ? 21.50600  6.22800   -4.45500  1.000 24.66138 ? 304 HOH A O   1 
HETATM 2084 O O   . HOH F 4 .   ? 24.92600  3.50900   -6.22300  1.000 43.19086 ? 305 HOH A O   1 
HETATM 2085 O O   . HOH F 4 .   ? 12.82700  6.57100   8.35100   1.000 35.50286 ? 306 HOH A O   1 
HETATM 2086 O O   . HOH F 4 .   ? 28.85500  -7.30100  5.66300   1.000 29.98703 ? 307 HOH A O   1 
HETATM 2087 O O   . HOH F 4 .   ? 9.44600   -9.05600  -13.41600 1.000 35.59139 ? 308 HOH A O   1 
HETATM 2088 O O   . HOH F 4 .   ? 9.74700   -5.03400  -12.96500 1.000 25.53639 ? 309 HOH A O   1 
HETATM 2089 O O   . HOH F 4 .   ? 30.78900  -4.39800  10.34000  1.000 54.62082 ? 310 HOH A O   1 
HETATM 2090 O O   . HOH F 4 .   ? 16.54900  0.84800   -5.46900  1.000 28.83094 ? 311 HOH A O   1 
HETATM 2091 O O   . HOH F 4 .   ? 21.19200  -6.25200  -12.88800 1.000 36.48382 ? 312 HOH A O   1 
HETATM 2092 O O   . HOH F 4 .   ? 32.89000  2.40700   3.80100   1.000 36.60346 ? 313 HOH A O   1 
HETATM 2093 O O   . HOH F 4 .   ? 1.02000   6.24200   2.68900   1.000 36.15416 ? 314 HOH A O   1 
HETATM 2094 O O   . HOH F 4 .   ? 17.03600  -11.87700 -11.41800 1.000 37.09210 ? 315 HOH A O   1 
HETATM 2095 O O   . HOH F 4 .   ? 20.02600  -3.79600  -5.58300  1.000 33.25717 ? 316 HOH A O   1 
HETATM 2096 O O   . HOH F 4 .   ? 21.96600  7.98100   2.72700   1.000 32.46352 ? 317 HOH A O   1 
HETATM 2097 O O   . HOH F 4 .   ? 14.77400  7.39400   -0.77200  1.000 29.82782 ? 318 HOH A O   1 
HETATM 2098 O O   . HOH F 4 .   ? 29.27400  -10.34800 -6.46900  1.000 45.10606 ? 319 HOH A O   1 
HETATM 2099 O O   . HOH F 4 .   ? 22.96600  0.84000   -9.26100  1.000 46.43829 ? 320 HOH A O   1 
HETATM 2100 O O   . HOH F 4 .   ? 11.79800  -7.99000  -14.49900 1.000 31.45142 ? 321 HOH A O   1 
HETATM 2101 O O   . HOH F 4 .   ? 25.23500  -5.20200  -6.67900  1.000 36.25943 ? 322 HOH A O   1 
HETATM 2102 O O   . HOH F 4 .   ? 17.04300  -12.44200 9.57500   1.000 39.16286 ? 323 HOH A O   1 
HETATM 2103 O O   . HOH F 4 .   ? 17.81400  -9.81800  10.64600  1.000 40.92099 ? 324 HOH A O   1 
HETATM 2104 O O   . HOH F 4 .   ? 11.09100  3.91700   13.54700  1.000 42.09948 ? 325 HOH A O   1 
HETATM 2105 O O   . HOH F 4 .   ? 5.12000   -11.49300 -6.78100  1.000 43.78070 ? 326 HOH A O   1 
HETATM 2106 O O   . HOH F 4 .   ? 11.37100  -0.49100  -14.66400 1.000 39.81752 ? 327 HOH A O   1 
HETATM 2107 O O   . HOH F 4 .   ? 25.20500  5.86100   -5.19700  1.000 38.31093 ? 328 HOH A O   1 
HETATM 2108 O O   . HOH F 4 .   ? 12.82800  -0.40100  -16.48900 1.000 48.02182 ? 329 HOH A O   1 
HETATM 2109 O O   . HOH F 4 .   ? 18.71600  -0.10400  -7.03200  1.000 44.56069 ? 330 HOH A O   1 
HETATM 2110 O O   . HOH F 4 .   ? -0.83900  5.86900   4.11500   1.000 50.87322 ? 331 HOH A O   1 
HETATM 2111 O O   . HOH F 4 .   ? 5.44700   3.64900   -10.98900 1.000 48.30947 ? 332 HOH A O   1 
HETATM 2112 O O   . HOH G 4 .   ? -2.99500  19.41300  27.78900  1.000 52.39909 ? 301 HOH B O   1 
HETATM 2113 O O   . HOH G 4 .   ? 20.32500  3.10000   25.25800  1.000 28.07659 ? 302 HOH B O   1 
HETATM 2114 O O   . HOH G 4 .   ? 22.12200  7.65500   34.68700  1.000 39.02309 ? 303 HOH B O   1 
HETATM 2115 O O   . HOH G 4 .   ? 16.43600  14.21900  13.87300  1.000 41.02489 ? 304 HOH B O   1 
HETATM 2116 O O   . HOH G 4 .   ? 10.07200  1.13400   25.39200  1.000 36.27360 ? 305 HOH B O   1 
HETATM 2117 O O   . HOH G 4 .   ? 27.56000  18.61900  23.49200  1.000 31.09759 ? 306 HOH B O   1 
HETATM 2118 O O   . HOH G 4 .   ? 6.05600   15.42200  39.10600  1.000 29.74720 ? 307 HOH B O   1 
HETATM 2119 O O   . HOH G 4 .   ? 12.10500  4.52000   18.02500  1.000 33.05864 ? 308 HOH B O   1 
HETATM 2120 O O   . HOH G 4 .   ? 27.47600  21.10800  18.70800  1.000 44.30153 ? 309 HOH B O   1 
HETATM 2121 O O   . HOH G 4 .   ? -4.01700  5.53400   22.19200  1.000 38.62993 ? 310 HOH B O   1 
HETATM 2122 O O   . HOH G 4 .   ? 18.89200  4.73800   31.90400  1.000 27.42377 ? 311 HOH B O   1 
HETATM 2123 O O   . HOH G 4 .   ? -0.14700  4.45800   22.07800  1.000 31.00626 ? 312 HOH B O   1 
HETATM 2124 O O   . HOH G 4 .   ? 9.56200   23.96400  18.61600  1.000 53.85441 ? 313 HOH B O   1 
HETATM 2125 O O   . HOH G 4 .   ? -5.43300  3.30000   21.88800  1.000 38.86660 ? 314 HOH B O   1 
HETATM 2126 O O   . HOH G 4 .   ? -8.980    20.101    15.709    1.000 43.69012 ? 315 HOH B O   1 
HETATM 2127 O O   . HOH G 4 .   ? 6.24500   21.09500  16.55300  1.000 42.24940 ? 316 HOH B O   1 
HETATM 2128 O O   . HOH G 4 .   ? 12.93900  3.56500   27.22200  1.000 27.73996 ? 317 HOH B O   1 
HETATM 2129 O O   . HOH G 4 .   ? 4.62400   5.47900   14.80400  1.000 45.33615 ? 318 HOH B O   1 
HETATM 2130 O O   . HOH G 4 .   ? 16.72600  20.86900  17.16600  1.000 40.09087 ? 319 HOH B O   1 
HETATM 2131 O O   . HOH G 4 .   ? 20.08600  9.78000   37.23600  1.000 49.49923 ? 320 HOH B O   1 
HETATM 2132 O O   . HOH G 4 .   ? 16.45200  16.09300  16.31600  1.000 35.23264 ? 321 HOH B O   1 
HETATM 2133 O O   . HOH G 4 .   ? 7.74100   0.24100   24.66600  1.000 43.32235 ? 322 HOH B O   1 
HETATM 2134 O O   . HOH G 4 .   ? 6.02900   7.03500   40.42700  1.000 49.49389 ? 323 HOH B O   1 
HETATM 2135 O O   . HOH G 4 .   ? 14.14800  10.08100  32.49800  1.000 32.03639 ? 324 HOH B O   1 
HETATM 2136 O O   . HOH G 4 .   ? 11.53700  8.63500   43.99900  1.000 43.85890 ? 325 HOH B O   1 
HETATM 2137 O O   . HOH G 4 .   ? 5.52600   19.60400  39.96100  1.000 42.44967 ? 326 HOH B O   1 
HETATM 2138 O O   . HOH G 4 .   ? 11.02300  7.54100   12.91600  1.000 35.89945 ? 327 HOH B O   1 
HETATM 2139 O O   . HOH G 4 .   ? 2.76700   16.61300  13.53000  1.000 37.00288 ? 328 HOH B O   1 
HETATM 2140 O O   . HOH G 4 .   ? 17.16100  14.67100  33.42000  1.000 33.53511 ? 329 HOH B O   1 
HETATM 2141 O O   . HOH G 4 .   ? 29.434    25.683    29.328    1.000 41.04142 ? 330 HOH B O   1 
HETATM 2142 O O   . HOH G 4 .   ? 20.369    28.660    21.827    1.000 40.19621 ? 331 HOH B O   1 
HETATM 2143 O O   . HOH G 4 .   ? 26.08100  21.28500  35.58100  1.000 41.26241 ? 332 HOH B O   1 
HETATM 2144 O O   . HOH G 4 .   ? 7.31600   18.46500  40.72600  1.000 31.79377 ? 333 HOH B O   1 
HETATM 2145 O O   . HOH G 4 .   ? 22.59900  5.33400   32.77200  1.000 41.67248 ? 334 HOH B O   1 
HETATM 2146 O O   . HOH G 4 .   ? 16.16600  23.57000  17.59700  1.000 45.55798 ? 335 HOH B O   1 
HETATM 2147 O O   . HOH G 4 .   ? 24.50300  16.37700  19.15600  1.000 43.14408 ? 336 HOH B O   1 
HETATM 2148 O O   . HOH G 4 .   ? 28.94000  19.90600  20.90900  1.000 47.08065 ? 337 HOH B O   1 
HETATM 2149 O O   . HOH G 4 .   ? 23.82200  14.20200  18.47900  1.000 43.22784 ? 338 HOH B O   1 
HETATM 2150 O O   . HOH G 4 .   ? -2.59300  3.14200   19.38400  1.000 53.65370 ? 339 HOH B O   1 
HETATM 2151 O O   . HOH G 4 .   ? 8.86100   12.95500  45.36500  1.000 53.87452 ? 340 HOH B O   1 
HETATM 2152 O O   . HOH G 4 .   ? 8.80900   10.88700  42.35300  1.000 41.36027 ? 341 HOH B O   1 
HETATM 2153 O O   . HOH G 4 .   ? 5.46600   17.57100  13.58700  1.000 44.50678 ? 342 HOH B O   1 
HETATM 2154 O O   . HOH G 4 .   ? -1.80300  4.94400   20.44300  1.000 42.23495 ? 343 HOH B O   1 
HETATM 2155 O O   . HOH G 4 .   ? 5.68000   20.50000  14.51300  1.000 45.84621 ? 344 HOH B O   1 
# 
