data_9BL0
# 
_entry.id   9BL0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BL0         pdb_00009bl0 10.2210/pdb9bl0/pdb 
WWPDB D_1000283236 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BL0 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-29 
_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                 5 
_pdbx_contact_author.email              rac1@cornell.edu 
_pdbx_contact_author.name_first         Richard 
_pdbx_contact_author.name_last          Cerione 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4512-5897 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, M.'        1 ? 
'Deck, S.L.'    2 ? 
'Milano, S.K.'  3 ? 
'Aplin, C.'     4 ? 
'Cerione, R.A.' 5 ? 
# 
_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                     'Room Temperature Structures of Oncogenic KRAS-G12D bound to MRTX-1133' 
_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 'Xu, M.'        1 ? 
primary 'Deck, S.L.'    2 ? 
primary 'Milano, S.K.'  3 ? 
primary 'Aplin, C.'     4 ? 
primary 'Cerione, R.A.' 5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Isoform 2B of GTPase KRas' 19307.680 2   3.6.5.2 'G12D, C51S, C80L, C118S' ? ? 
2 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE" 443.201   2   ?       ?                         ? ? 
3 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ?                         ? ? 
4 non-polymer nat 
;4-(4-[(1R,5S)-3,8-diazabicyclo[3.2.1]octan-3-yl]-8-fluoro-2-{[(2R,4R,7aS)-2-fluorotetrahydro-1H-pyrrolizin-7a(5H)-yl]methoxy}pyrido[4,3-d]pyrimidin-7-yl)-5-ethynyl-6-fluoronaphthalen-2-ol
;
600.633   2   ?       ?                         ? ? 
5 water       nat water 18.015    142 ?       ?                         ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras' 
# 
_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       
;MTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFLL
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFLL
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
_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 "GUANOSINE-5'-DIPHOSPHATE" GDP 
3 'MAGNESIUM ION' MG  
4 
;4-(4-[(1R,5S)-3,8-diazabicyclo[3.2.1]octan-3-yl]-8-fluoro-2-{[(2R,4R,7aS)-2-fluorotetrahydro-1H-pyrrolizin-7a(5H)-yl]methoxy}pyrido[4,3-d]pyrimidin-7-yl)-5-ethynyl-6-fluoronaphthalen-2-ol
;
6IC 
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   GLU n 
1 4   TYR n 
1 5   LYS n 
1 6   LEU n 
1 7   VAL n 
1 8   VAL n 
1 9   VAL n 
1 10  GLY n 
1 11  ALA n 
1 12  ASP n 
1 13  GLY n 
1 14  VAL n 
1 15  GLY n 
1 16  LYS n 
1 17  SER n 
1 18  ALA n 
1 19  LEU n 
1 20  THR n 
1 21  ILE n 
1 22  GLN n 
1 23  LEU n 
1 24  ILE n 
1 25  GLN n 
1 26  ASN n 
1 27  HIS n 
1 28  PHE n 
1 29  VAL n 
1 30  ASP n 
1 31  GLU n 
1 32  TYR n 
1 33  ASP n 
1 34  PRO n 
1 35  THR n 
1 36  ILE n 
1 37  GLU n 
1 38  ASP n 
1 39  SER n 
1 40  TYR n 
1 41  ARG n 
1 42  LYS n 
1 43  GLN n 
1 44  VAL n 
1 45  VAL n 
1 46  ILE n 
1 47  ASP n 
1 48  GLY n 
1 49  GLU n 
1 50  THR n 
1 51  SER n 
1 52  LEU n 
1 53  LEU n 
1 54  ASP n 
1 55  ILE n 
1 56  LEU n 
1 57  ASP n 
1 58  THR n 
1 59  ALA n 
1 60  GLY n 
1 61  GLN n 
1 62  GLU n 
1 63  GLU n 
1 64  TYR n 
1 65  SER n 
1 66  ALA n 
1 67  MET n 
1 68  ARG n 
1 69  ASP n 
1 70  GLN n 
1 71  TYR n 
1 72  MET n 
1 73  ARG n 
1 74  THR n 
1 75  GLY n 
1 76  GLU n 
1 77  GLY n 
1 78  PHE n 
1 79  LEU n 
1 80  LEU n 
1 81  VAL n 
1 82  PHE n 
1 83  ALA n 
1 84  ILE n 
1 85  ASN n 
1 86  ASN n 
1 87  THR n 
1 88  LYS n 
1 89  SER n 
1 90  PHE n 
1 91  GLU n 
1 92  ASP n 
1 93  ILE n 
1 94  HIS n 
1 95  HIS n 
1 96  TYR n 
1 97  ARG n 
1 98  GLU n 
1 99  GLN n 
1 100 ILE n 
1 101 LYS n 
1 102 ARG n 
1 103 VAL n 
1 104 LYS n 
1 105 ASP n 
1 106 SER n 
1 107 GLU n 
1 108 ASP n 
1 109 VAL n 
1 110 PRO n 
1 111 MET n 
1 112 VAL n 
1 113 LEU n 
1 114 VAL n 
1 115 GLY n 
1 116 ASN n 
1 117 LYS n 
1 118 SER n 
1 119 ASP n 
1 120 LEU n 
1 121 PRO n 
1 122 SER n 
1 123 ARG n 
1 124 THR n 
1 125 VAL n 
1 126 ASP n 
1 127 THR n 
1 128 LYS n 
1 129 GLN n 
1 130 ALA n 
1 131 GLN n 
1 132 ASP n 
1 133 LEU n 
1 134 ALA n 
1 135 ARG n 
1 136 SER n 
1 137 TYR n 
1 138 GLY n 
1 139 ILE n 
1 140 PRO n 
1 141 PHE n 
1 142 ILE n 
1 143 GLU n 
1 144 THR n 
1 145 SER n 
1 146 ALA n 
1 147 LYS n 
1 148 THR n 
1 149 ARG n 
1 150 GLN n 
1 151 GLY n 
1 152 VAL n 
1 153 ASP n 
1 154 ASP n 
1 155 ALA n 
1 156 PHE n 
1 157 TYR n 
1 158 THR n 
1 159 LEU n 
1 160 VAL n 
1 161 ARG n 
1 162 GLU n 
1 163 ILE n 
1 164 ARG n 
1 165 LYS n 
1 166 HIS n 
1 167 LYS n 
1 168 GLU n 
1 169 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KRAS, KRAS2, RASK2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
6IC non-polymer         . 
;4-(4-[(1R,5S)-3,8-diazabicyclo[3.2.1]octan-3-yl]-8-fluoro-2-{[(2R,4R,7aS)-2-fluorotetrahydro-1H-pyrrolizin-7a(5H)-yl]methoxy}pyrido[4,3-d]pyrimidin-7-yl)-5-ethynyl-6-fluoronaphthalen-2-ol
;
MRTX-1133 'C33 H31 F3 N6 O2'  600.633 
ALA 'L-peptide linking' y ALANINE ?         'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?         'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?         'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?         'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?         'C3 H7 N O2 S'      121.158 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ?         'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE ?         'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?         'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?         'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?         'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?         'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?         'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?         'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?         'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?         'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?         'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?         'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?         'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?         'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?         'C4 H9 N O3'        119.119 
TYR 'L-peptide linking' y TYROSINE ?         'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?         'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  MET 67  67  67  MET MET A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  MET 72  72  72  MET MET A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  HIS 95  95  95  HIS HIS A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 HIS 166 166 166 HIS HIS A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   GLU 3   3   3   GLU GLU B . n 
B 1 4   TYR 4   4   4   TYR TYR B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  THR 20  20  20  THR THR B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  HIS 27  27  27  HIS HIS B . n 
B 1 28  PHE 28  28  28  PHE PHE B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  TYR 32  32  32  TYR TYR B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ARG 41  41  41  ARG ARG B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  SER 51  51  51  SER SER B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  GLN 61  61  61  GLN GLN B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  MET 67  67  67  MET MET B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  MET 72  72  72  MET MET B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  PHE 78  78  78  PHE PHE B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  PHE 82  82  82  PHE PHE B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  HIS 95  95  95  HIS HIS B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  ARG 97  97  97  ARG ARG B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 PRO 110 110 110 PRO PRO B . n 
B 1 111 MET 111 111 111 MET MET B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 ASP 119 119 119 ASP ASP B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 SER 122 122 122 SER SER B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ASP 126 126 126 ASP ASP B . n 
B 1 127 THR 127 127 127 THR THR B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 PRO 140 140 140 PRO PRO B . n 
B 1 141 PHE 141 141 141 PHE PHE B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 LYS 165 165 165 LYS LYS B . n 
B 1 166 HIS 166 166 166 HIS HIS B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 GLU 168 168 168 GLU GLU B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        6IC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   6IC 
_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 GDP 1  201 201 GDP GDP A . 
D 3 MG  1  202 203 MG  MG  A . 
E 4 6IC 1  203 2   6IC 6IC A . 
F 2 GDP 1  201 201 GDP GDP B . 
G 3 MG  1  202 203 MG  MG  B . 
H 4 6IC 1  203 1   6IC 6IC B . 
I 5 HOH 1  301 48  HOH HOH A . 
I 5 HOH 2  302 195 HOH HOH A . 
I 5 HOH 3  303 137 HOH HOH A . 
I 5 HOH 4  304 98  HOH HOH A . 
I 5 HOH 5  305 92  HOH HOH A . 
I 5 HOH 6  306 28  HOH HOH A . 
I 5 HOH 7  307 82  HOH HOH A . 
I 5 HOH 8  308 76  HOH HOH A . 
I 5 HOH 9  309 19  HOH HOH A . 
I 5 HOH 10 310 100 HOH HOH A . 
I 5 HOH 11 311 189 HOH HOH A . 
I 5 HOH 12 312 69  HOH HOH A . 
I 5 HOH 13 313 27  HOH HOH A . 
I 5 HOH 14 314 61  HOH HOH A . 
I 5 HOH 15 315 51  HOH HOH A . 
I 5 HOH 16 316 5   HOH HOH A . 
I 5 HOH 17 317 8   HOH HOH A . 
I 5 HOH 18 318 170 HOH HOH A . 
I 5 HOH 19 319 14  HOH HOH A . 
I 5 HOH 20 320 199 HOH HOH A . 
I 5 HOH 21 321 52  HOH HOH A . 
I 5 HOH 22 322 34  HOH HOH A . 
I 5 HOH 23 323 165 HOH HOH A . 
I 5 HOH 24 324 1   HOH HOH A . 
I 5 HOH 25 325 29  HOH HOH A . 
I 5 HOH 26 326 11  HOH HOH A . 
I 5 HOH 27 327 102 HOH HOH A . 
I 5 HOH 28 328 16  HOH HOH A . 
I 5 HOH 29 329 103 HOH HOH A . 
I 5 HOH 30 330 174 HOH HOH A . 
I 5 HOH 31 331 60  HOH HOH A . 
I 5 HOH 32 332 56  HOH HOH A . 
I 5 HOH 33 333 47  HOH HOH A . 
I 5 HOH 34 334 25  HOH HOH A . 
I 5 HOH 35 335 9   HOH HOH A . 
I 5 HOH 36 336 84  HOH HOH A . 
I 5 HOH 37 337 10  HOH HOH A . 
I 5 HOH 38 338 23  HOH HOH A . 
I 5 HOH 39 339 104 HOH HOH A . 
I 5 HOH 40 340 109 HOH HOH A . 
I 5 HOH 41 341 38  HOH HOH A . 
I 5 HOH 42 342 214 HOH HOH A . 
I 5 HOH 43 343 50  HOH HOH A . 
I 5 HOH 44 344 136 HOH HOH A . 
I 5 HOH 45 345 40  HOH HOH A . 
I 5 HOH 46 346 144 HOH HOH A . 
I 5 HOH 47 347 44  HOH HOH A . 
I 5 HOH 48 348 39  HOH HOH A . 
I 5 HOH 49 349 70  HOH HOH A . 
I 5 HOH 50 350 59  HOH HOH A . 
I 5 HOH 51 351 72  HOH HOH A . 
I 5 HOH 52 352 37  HOH HOH A . 
I 5 HOH 53 353 30  HOH HOH A . 
I 5 HOH 54 354 111 HOH HOH A . 
I 5 HOH 55 355 160 HOH HOH A . 
I 5 HOH 56 356 148 HOH HOH A . 
I 5 HOH 57 357 188 HOH HOH A . 
I 5 HOH 58 358 85  HOH HOH A . 
I 5 HOH 59 359 90  HOH HOH A . 
I 5 HOH 60 360 97  HOH HOH A . 
I 5 HOH 61 361 149 HOH HOH A . 
I 5 HOH 62 362 63  HOH HOH A . 
I 5 HOH 63 363 126 HOH HOH A . 
I 5 HOH 64 364 21  HOH HOH A . 
I 5 HOH 65 365 62  HOH HOH A . 
I 5 HOH 66 366 91  HOH HOH A . 
I 5 HOH 67 367 119 HOH HOH A . 
J 5 HOH 1  301 101 HOH HOH B . 
J 5 HOH 2  302 58  HOH HOH B . 
J 5 HOH 3  303 200 HOH HOH B . 
J 5 HOH 4  304 114 HOH HOH B . 
J 5 HOH 5  305 74  HOH HOH B . 
J 5 HOH 6  306 93  HOH HOH B . 
J 5 HOH 7  307 152 HOH HOH B . 
J 5 HOH 8  308 120 HOH HOH B . 
J 5 HOH 9  309 53  HOH HOH B . 
J 5 HOH 10 310 18  HOH HOH B . 
J 5 HOH 11 311 73  HOH HOH B . 
J 5 HOH 12 312 141 HOH HOH B . 
J 5 HOH 13 313 222 HOH HOH B . 
J 5 HOH 14 314 2   HOH HOH B . 
J 5 HOH 15 315 67  HOH HOH B . 
J 5 HOH 16 316 77  HOH HOH B . 
J 5 HOH 17 317 151 HOH HOH B . 
J 5 HOH 18 318 133 HOH HOH B . 
J 5 HOH 19 319 12  HOH HOH B . 
J 5 HOH 20 320 15  HOH HOH B . 
J 5 HOH 21 321 4   HOH HOH B . 
J 5 HOH 22 322 45  HOH HOH B . 
J 5 HOH 23 323 13  HOH HOH B . 
J 5 HOH 24 324 33  HOH HOH B . 
J 5 HOH 25 325 32  HOH HOH B . 
J 5 HOH 26 326 88  HOH HOH B . 
J 5 HOH 27 327 65  HOH HOH B . 
J 5 HOH 28 328 43  HOH HOH B . 
J 5 HOH 29 329 95  HOH HOH B . 
J 5 HOH 30 330 86  HOH HOH B . 
J 5 HOH 31 331 108 HOH HOH B . 
J 5 HOH 32 332 116 HOH HOH B . 
J 5 HOH 33 333 7   HOH HOH B . 
J 5 HOH 34 334 80  HOH HOH B . 
J 5 HOH 35 335 49  HOH HOH B . 
J 5 HOH 36 336 110 HOH HOH B . 
J 5 HOH 37 337 22  HOH HOH B . 
J 5 HOH 38 338 31  HOH HOH B . 
J 5 HOH 39 339 57  HOH HOH B . 
J 5 HOH 40 340 24  HOH HOH B . 
J 5 HOH 41 341 55  HOH HOH B . 
J 5 HOH 42 342 54  HOH HOH B . 
J 5 HOH 43 343 81  HOH HOH B . 
J 5 HOH 44 344 87  HOH HOH B . 
J 5 HOH 45 345 6   HOH HOH B . 
J 5 HOH 46 346 20  HOH HOH B . 
J 5 HOH 47 347 46  HOH HOH B . 
J 5 HOH 48 348 36  HOH HOH B . 
J 5 HOH 49 349 89  HOH HOH B . 
J 5 HOH 50 350 146 HOH HOH B . 
J 5 HOH 51 351 26  HOH HOH B . 
J 5 HOH 52 352 35  HOH HOH B . 
J 5 HOH 53 353 129 HOH HOH B . 
J 5 HOH 54 354 96  HOH HOH B . 
J 5 HOH 55 355 125 HOH HOH B . 
J 5 HOH 56 356 64  HOH HOH B . 
J 5 HOH 57 357 163 HOH HOH B . 
J 5 HOH 58 358 147 HOH HOH B . 
J 5 HOH 59 359 66  HOH HOH B . 
J 5 HOH 60 360 68  HOH HOH B . 
J 5 HOH 61 361 164 HOH HOH B . 
J 5 HOH 62 362 124 HOH HOH B . 
J 5 HOH 63 363 135 HOH HOH B . 
J 5 HOH 64 364 41  HOH HOH B . 
J 5 HOH 65 365 127 HOH HOH B . 
J 5 HOH 66 366 75  HOH HOH B . 
J 5 HOH 67 367 3   HOH HOH B . 
J 5 HOH 68 368 83  HOH HOH B . 
J 5 HOH 69 369 122 HOH HOH B . 
J 5 HOH 70 370 105 HOH HOH B . 
J 5 HOH 71 371 17  HOH HOH B . 
J 5 HOH 72 372 183 HOH HOH B . 
J 5 HOH 73 373 185 HOH HOH B . 
J 5 HOH 74 374 157 HOH HOH B . 
J 5 HOH 75 375 78  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   ? ? ? '(1.21.1_5286: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BL0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.361 
_cell.length_a_esd                 ? 
_cell.length_b                     75.361 
_cell.length_b_esd                 ? 
_cell.length_c                     203.864 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9BL0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BL0 
_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             2.82 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '24% PEG 8000,100 mM Sodium Citrate, 100 mM Ammonium Acetate pH 5.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-25 
_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   0.9686 
_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                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          23.44 
_reflns.entry_id                                       9BL0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               50 
_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                                     49291 
_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                           95.66 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.7 
_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                                0.111 
_reflns.pdbx_Rpim_I_all                                0.049 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.66 
_reflns_shell.d_res_low                                     1.68 
_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                             4322 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.205 
_reflns_shell.pdbx_Rpim_I_all                               0.770 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .204 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BL0 
_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                            1.66 
_refine.ls_d_res_low                             40.17 
_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                     49223 
_refine.ls_number_reflns_R_free                  2017 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.66 
_refine.ls_percent_reflns_R_free                 4.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1794 
_refine.ls_R_factor_R_free                       0.1947 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1788 
_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                          1.96 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.16 
_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                            0.23 
_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                       1.66 
_refine_hist.d_res_low                        40.17 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               3001 
_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        2713 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         146 
_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' ? 0.009  ? 2925 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.445  ? 3980 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.544 ? 1119 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 436  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 493  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.66 1.70  . . 125 2936 83.00  . . . . 0.4009 . . . . . . . . . . . 0.3807 
'X-RAY DIFFRACTION' 1.70 1.74  . . 140 3151 89.00  . . . . 0.3547 . . . . . . . . . . . 0.3522 
'X-RAY DIFFRACTION' 1.74 1.79  . . 137 3255 92.00  . . . . 0.2802 . . . . . . . . . . . 0.2556 
'X-RAY DIFFRACTION' 1.79 1.85  . . 136 3250 93.00  . . . . 0.2246 . . . . . . . . . . . 0.2647 
'X-RAY DIFFRACTION' 1.85 1.92  . . 148 3366 95.00  . . . . 0.2054 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 1.92 1.99  . . 145 3370 96.00  . . . . 0.2084 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 2.00 2.09  . . 145 3433 97.00  . . . . 0.2010 . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 2.09 2.20  . . 152 3426 98.00  . . . . 0.1855 . . . . . . . . . . . 0.1842 
'X-RAY DIFFRACTION' 2.20 2.33  . . 145 3496 99.00  . . . . 0.1709 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.33 2.51  . . 148 3499 99.00  . . . . 0.1897 . . . . . . . . . . . 0.2538 
'X-RAY DIFFRACTION' 2.51 2.77  . . 148 3489 99.00  . . . . 0.1906 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 2.77 3.17  . . 150 3512 100.00 . . . . 0.1827 . . . . . . . . . . . 0.2117 
'X-RAY DIFFRACTION' 3.17 3.99  . . 151 3492 100.00 . . . . 0.1560 . . . . . . . . . . . 0.1657 
'X-RAY DIFFRACTION' 3.99 40.17 . . 147 3531 100.00 . . . . 0.1282 . . . . . . . . . . . 0.1390 
# 
_struct.entry_id                     9BL0 
_struct.title                        'KRAS G12D Mutant KRAS 1-169 at 298 K bound to MRTX-1133' 
_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        9BL0 
_struct_keywords.text            'GTPase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASK_HUMAN 
_struct_ref.pdbx_db_accession          P01116 
_struct_ref.pdbx_db_isoform            P01116-2 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
_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 9BL0 A 1 ? 169 ? P01116 1 ? 169 ? 1 169 
2 1 9BL0 B 1 ? 169 ? P01116 1 ? 169 ? 1 169 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BL0 ASP A 12  ? UNP P01116 GLY 12  'engineered mutation' 12  1 
1 9BL0 SER A 51  ? UNP P01116 CYS 51  'engineered mutation' 51  2 
1 9BL0 LEU A 80  ? UNP P01116 CYS 80  'engineered mutation' 80  3 
1 9BL0 SER A 118 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
2 9BL0 ASP B 12  ? UNP P01116 GLY 12  'engineered mutation' 12  5 
2 9BL0 SER B 51  ? UNP P01116 CYS 51  'engineered mutation' 51  6 
2 9BL0 LEU B 80  ? UNP P01116 CYS 80  'engineered mutation' 80  7 
2 9BL0 SER B 118 ? UNP P01116 CYS 118 'engineered mutation' 118 8 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? 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,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 15  ? ASN A 26  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 SER A 65  ? THR A 74  ? SER A 65  THR A 74  1 ? 10 
HELX_P HELX_P3  AA3 ASN A 86  ? ASP A 92  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P4  AA4 ASP A 92  ? ASP A 105 ? ASP A 92  ASP A 105 1 ? 14 
HELX_P HELX_P5  AA5 ASP A 126 ? GLY A 138 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 151 ? GLU A 168 ? GLY A 151 GLU A 168 1 ? 18 
HELX_P HELX_P7  AA7 GLY B 15  ? ASN B 26  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P8  AA8 SER B 65  ? THR B 74  ? SER B 65  THR B 74  1 ? 10 
HELX_P HELX_P9  AA9 ASN B 86  ? ASP B 92  ? ASN B 86  ASP B 92  1 ? 7  
HELX_P HELX_P10 AB1 ASP B 92  ? ASP B 105 ? ASP B 92  ASP B 105 1 ? 14 
HELX_P HELX_P11 AB2 ASP B 126 ? GLY B 138 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P12 AB3 GLY B 151 ? GLU B 168 ? GLY B 151 GLU B 168 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 17 OG  ? ? ? 1_555 D MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc2  metalc ? ? C GDP .  O3B ? ? ? 1_555 D MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc3  metalc ? ? D MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  202 A HOH 316 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc4  metalc ? ? D MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  202 A HOH 317 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc5  metalc ? ? D MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  202 A HOH 324 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc6  metalc ? ? D MG  .  MG  ? ? ? 1_555 I HOH . O  ? ? A MG  202 A HOH 335 1_555 ? ? ? ? ? ? ? 2.174 ? ? 
metalc7  metalc ? ? B SER 17 OG  ? ? ? 1_555 G MG  . MG ? ? B SER 17  B MG  202 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc8  metalc ? ? F GDP .  O3B ? ? ? 1_555 G MG  . MG ? ? B GDP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc9  metalc ? ? G MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? B MG  202 B HOH 314 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc10 metalc ? ? G MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? B MG  202 B HOH 321 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc11 metalc ? ? G MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? B MG  202 B HOH 333 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O3B ? C GDP . ? A GDP 201 ? 1_555 92.1  ? 
2  OG  ? A SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 316 ? 1_555 82.7  ? 
3  O3B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 316 ? 1_555 92.2  ? 
4  OG  ? A SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 317 ? 1_555 92.5  ? 
5  O3B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 317 ? 1_555 89.3  ? 
6  O   ? I HOH .  ? A HOH 316 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 317 ? 1_555 175.0 ? 
7  OG  ? A SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 324 ? 1_555 170.9 ? 
8  O3B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 324 ? 1_555 89.9  ? 
9  O   ? I HOH .  ? A HOH 316 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 324 ? 1_555 88.4  ? 
10 O   ? I HOH .  ? A HOH 317 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 324 ? 1_555 96.4  ? 
11 OG  ? A SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 335 ? 1_555 90.3  ? 
12 O3B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 335 ? 1_555 174.4 ? 
13 O   ? I HOH .  ? A HOH 316 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 335 ? 1_555 93.1  ? 
14 O   ? I HOH .  ? A HOH 317 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 335 ? 1_555 85.5  ? 
15 O   ? I HOH .  ? A HOH 324 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? I HOH . ? A HOH 335 ? 1_555 88.6  ? 
16 OG  ? B SER 17 ? B SER 17  ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O3B ? F GDP . ? B GDP 201 ? 1_555 92.2  ? 
17 OG  ? B SER 17 ? B SER 17  ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 314 ? 1_555 83.6  ? 
18 O3B ? F GDP .  ? B GDP 201 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 314 ? 1_555 94.4  ? 
19 OG  ? B SER 17 ? B SER 17  ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 321 ? 1_555 174.7 ? 
20 O3B ? F GDP .  ? B GDP 201 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 321 ? 1_555 88.4  ? 
21 O   ? J HOH .  ? B HOH 314 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 321 ? 1_555 91.1  ? 
22 OG  ? B SER 17 ? B SER 17  ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 333 ? 1_555 91.2  ? 
23 O3B ? F GDP .  ? B GDP 201 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 333 ? 1_555 172.3 ? 
24 O   ? J HOH .  ? B HOH 314 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 333 ? 1_555 92.8  ? 
25 O   ? J HOH .  ? B HOH 321 ? 1_555 MG ? G MG . ? B MG 202 ? 1_555 O   ? J HOH . ? B HOH 333 ? 1_555 88.8  ? 
# 
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 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? 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 ASP A 38  ? ILE A 46  ? ASP A 38  ILE A 46  
AA1 2 GLU A 49  ? ASP A 57  ? GLU A 49  ASP A 57  
AA1 3 THR A 2   ? VAL A 9   ? THR A 2   VAL A 9   
AA1 4 GLY A 77  ? ALA A 83  ? GLY A 77  ALA A 83  
AA1 5 MET A 111 ? ASN A 116 ? MET A 111 ASN A 116 
AA1 6 PHE A 141 ? GLU A 143 ? PHE A 141 GLU A 143 
AA2 1 ASP B 38  ? ILE B 46  ? ASP B 38  ILE B 46  
AA2 2 GLU B 49  ? ASP B 57  ? GLU B 49  ASP B 57  
AA2 3 THR B 2   ? VAL B 9   ? THR B 2   VAL B 9   
AA2 4 GLY B 77  ? ALA B 83  ? GLY B 77  ALA B 83  
AA2 5 MET B 111 ? ASN B 116 ? MET B 111 ASN B 116 
AA2 6 PHE B 141 ? GLU B 143 ? PHE B 141 GLU B 143 
# 
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 N LYS A 42  ? N LYS A 42  O LEU A 53  ? O LEU A 53  
AA1 2 3 O LEU A 56  ? O LEU A 56  N LEU A 6   ? N LEU A 6   
AA1 3 4 N VAL A 9   ? N VAL A 9   O LEU A 79  ? O LEU A 79  
AA1 4 5 N LEU A 80  ? N LEU A 80  O VAL A 114 ? O VAL A 114 
AA1 5 6 N LEU A 113 ? N LEU A 113 O ILE A 142 ? O ILE A 142 
AA2 1 2 N LYS B 42  ? N LYS B 42  O LEU B 53  ? O LEU B 53  
AA2 2 3 O LEU B 56  ? O LEU B 56  N VAL B 8   ? N VAL B 8   
AA2 3 4 N VAL B 9   ? N VAL B 9   O LEU B 79  ? O LEU B 79  
AA2 4 5 N LEU B 80  ? N LEU B 80  O VAL B 114 ? O VAL B 114 
AA2 5 6 N LEU B 113 ? N LEU B 113 O ILE B 142 ? O ILE B 142 
# 
_pdbx_entry_details.entry_id                   9BL0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 31  ? ? -116.13 68.34  
2 1 ASP A 33  ? ? -36.46  113.34 
3 1 ASP A 108 ? ? -117.60 77.79  
4 1 LYS A 117 ? ? 73.36   39.10  
5 1 GLU A 168 ? ? -104.12 58.27  
6 1 ASP B 33  ? ? -37.25  112.66 
7 1 ASP B 108 ? ? -117.52 77.24  
8 1 LYS B 117 ? ? 73.32   37.94  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 341 ? I HOH . 
2 1 A HOH 366 ? I HOH . 
3 1 B HOH 341 ? J HOH . 
4 1 B HOH 374 ? J HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z                 
2 -y,x-y,z              
3 -x+y,-x,z             
4 x+1/3,y+2/3,z+2/3     
5 -y+1/3,x-y+2/3,z+2/3  
6 -x+y+1/3,-x+2/3,z+2/3 
7 x+2/3,y+1/3,z+1/3     
8 -y+2/3,x-y+1/3,z+1/3  
9 -x+y+2/3,-x+1/3,z+1/3 
# 
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 
6IC C22    C  Y N 1   
6IC C21    C  Y N 2   
6IC C23    C  Y N 3   
6IC C20    C  Y N 4   
6IC C24    C  Y N 5   
6IC C19    C  Y N 6   
6IC C17    C  Y N 7   
6IC C14    C  N N 8   
6IC C13    C  N N 9   
6IC C18    C  Y N 10  
6IC C01    C  Y N 11  
6IC C02    C  Y N 12  
6IC C03    C  Y N 13  
6IC C04    C  Y N 14  
6IC C05    C  Y N 15  
6IC C06    C  Y N 16  
6IC C07    C  Y N 17  
6IC C08    C  Y N 18  
6IC C09    C  N N 19  
6IC C10    C  N N 20  
6IC C11    C  N S 21  
6IC C12    C  N R 22  
6IC C15    C  N N 23  
6IC C16    C  Y N 24  
6IC C25    C  N S 25  
6IC C26    C  N N 26  
6IC C27    C  N R 27  
6IC C28    C  N N 28  
6IC C29    C  N N 29  
6IC C30    C  N N 30  
6IC C31    C  N N 31  
6IC C32    C  N N 32  
6IC C33    C  N N 33  
6IC F01    F  N N 34  
6IC F02    F  N N 35  
6IC F23    F  N N 36  
6IC N01    N  Y N 37  
6IC N02    N  Y N 38  
6IC N03    N  Y N 39  
6IC N04    N  N N 40  
6IC N05    N  N N 41  
6IC N06    N  N N 42  
6IC O01    O  N N 43  
6IC O02    O  N N 44  
6IC H1     H  N N 45  
6IC H2     H  N N 46  
6IC H3     H  N N 47  
6IC H4     H  N N 48  
6IC H5     H  N N 49  
6IC H6     H  N N 50  
6IC H7     H  N N 51  
6IC H8     H  N N 52  
6IC H9     H  N N 53  
6IC H10    H  N N 54  
6IC H11    H  N N 55  
6IC H12    H  N N 56  
6IC H13    H  N N 57  
6IC H14    H  N N 58  
6IC H15    H  N N 59  
6IC H16    H  N N 60  
6IC H17    H  N N 61  
6IC H18    H  N N 62  
6IC H19    H  N N 63  
6IC H20    H  N N 64  
6IC H21    H  N N 65  
6IC H22    H  N N 66  
6IC H23    H  N N 67  
6IC H24    H  N N 68  
6IC H25    H  N N 69  
6IC H26    H  N N 70  
6IC H27    H  N N 71  
6IC H28    H  N N 72  
6IC H29    H  N N 73  
6IC H30    H  N N 74  
6IC H33    H  N N 75  
ALA N      N  N N 76  
ALA CA     C  N S 77  
ALA C      C  N N 78  
ALA O      O  N N 79  
ALA CB     C  N N 80  
ALA OXT    O  N N 81  
ALA H      H  N N 82  
ALA H2     H  N N 83  
ALA HA     H  N N 84  
ALA HB1    H  N N 85  
ALA HB2    H  N N 86  
ALA HB3    H  N N 87  
ALA HXT    H  N N 88  
ARG N      N  N N 89  
ARG CA     C  N S 90  
ARG C      C  N N 91  
ARG O      O  N N 92  
ARG CB     C  N N 93  
ARG CG     C  N N 94  
ARG CD     C  N N 95  
ARG NE     N  N N 96  
ARG CZ     C  N N 97  
ARG NH1    N  N N 98  
ARG NH2    N  N N 99  
ARG OXT    O  N N 100 
ARG H      H  N N 101 
ARG H2     H  N N 102 
ARG HA     H  N N 103 
ARG HB2    H  N N 104 
ARG HB3    H  N N 105 
ARG HG2    H  N N 106 
ARG HG3    H  N N 107 
ARG HD2    H  N N 108 
ARG HD3    H  N N 109 
ARG HE     H  N N 110 
ARG HH11   H  N N 111 
ARG HH12   H  N N 112 
ARG HH21   H  N N 113 
ARG HH22   H  N N 114 
ARG HXT    H  N N 115 
ASN N      N  N N 116 
ASN CA     C  N S 117 
ASN C      C  N N 118 
ASN O      O  N N 119 
ASN CB     C  N N 120 
ASN CG     C  N N 121 
ASN OD1    O  N N 122 
ASN ND2    N  N N 123 
ASN OXT    O  N N 124 
ASN H      H  N N 125 
ASN H2     H  N N 126 
ASN HA     H  N N 127 
ASN HB2    H  N N 128 
ASN HB3    H  N N 129 
ASN HD21   H  N N 130 
ASN HD22   H  N N 131 
ASN HXT    H  N N 132 
ASP N      N  N N 133 
ASP CA     C  N S 134 
ASP C      C  N N 135 
ASP O      O  N N 136 
ASP CB     C  N N 137 
ASP CG     C  N N 138 
ASP OD1    O  N N 139 
ASP OD2    O  N N 140 
ASP OXT    O  N N 141 
ASP H      H  N N 142 
ASP H2     H  N N 143 
ASP HA     H  N N 144 
ASP HB2    H  N N 145 
ASP HB3    H  N N 146 
ASP HD2    H  N N 147 
ASP HXT    H  N N 148 
CYS N      N  N N 149 
CYS CA     C  N R 150 
CYS C      C  N N 151 
CYS O      O  N N 152 
CYS CB     C  N N 153 
CYS SG     S  N N 154 
CYS OXT    O  N N 155 
CYS H      H  N N 156 
CYS H2     H  N N 157 
CYS HA     H  N N 158 
CYS HB2    H  N N 159 
CYS HB3    H  N N 160 
CYS HG     H  N N 161 
CYS HXT    H  N N 162 
GDP PB     P  N N 163 
GDP O1B    O  N N 164 
GDP O2B    O  N N 165 
GDP O3B    O  N N 166 
GDP O3A    O  N N 167 
GDP PA     P  N N 168 
GDP O1A    O  N N 169 
GDP O2A    O  N N 170 
GDP "O5'"  O  N N 171 
GDP "C5'"  C  N N 172 
GDP "C4'"  C  N R 173 
GDP "O4'"  O  N N 174 
GDP "C3'"  C  N S 175 
GDP "O3'"  O  N N 176 
GDP "C2'"  C  N R 177 
GDP "O2'"  O  N N 178 
GDP "C1'"  C  N R 179 
GDP N9     N  Y N 180 
GDP C8     C  Y N 181 
GDP N7     N  Y N 182 
GDP C5     C  Y N 183 
GDP C6     C  N N 184 
GDP O6     O  N N 185 
GDP N1     N  N N 186 
GDP C2     C  N N 187 
GDP N2     N  N N 188 
GDP N3     N  N N 189 
GDP C4     C  Y N 190 
GDP HOB2   H  N N 191 
GDP HOB3   H  N N 192 
GDP HOA2   H  N N 193 
GDP "H5'"  H  N N 194 
GDP "H5''" H  N N 195 
GDP "H4'"  H  N N 196 
GDP "H3'"  H  N N 197 
GDP "HO3'" H  N N 198 
GDP "H2'"  H  N N 199 
GDP "HO2'" H  N N 200 
GDP "H1'"  H  N N 201 
GDP H8     H  N N 202 
GDP HN1    H  N N 203 
GDP HN21   H  N N 204 
GDP HN22   H  N N 205 
GLN N      N  N N 206 
GLN CA     C  N S 207 
GLN C      C  N N 208 
GLN O      O  N N 209 
GLN CB     C  N N 210 
GLN CG     C  N N 211 
GLN CD     C  N N 212 
GLN OE1    O  N N 213 
GLN NE2    N  N N 214 
GLN OXT    O  N N 215 
GLN H      H  N N 216 
GLN H2     H  N N 217 
GLN HA     H  N N 218 
GLN HB2    H  N N 219 
GLN HB3    H  N N 220 
GLN HG2    H  N N 221 
GLN HG3    H  N N 222 
GLN HE21   H  N N 223 
GLN HE22   H  N N 224 
GLN HXT    H  N N 225 
GLU N      N  N N 226 
GLU CA     C  N S 227 
GLU C      C  N N 228 
GLU O      O  N N 229 
GLU CB     C  N N 230 
GLU CG     C  N N 231 
GLU CD     C  N N 232 
GLU OE1    O  N N 233 
GLU OE2    O  N N 234 
GLU OXT    O  N N 235 
GLU H      H  N N 236 
GLU H2     H  N N 237 
GLU HA     H  N N 238 
GLU HB2    H  N N 239 
GLU HB3    H  N N 240 
GLU HG2    H  N N 241 
GLU HG3    H  N N 242 
GLU HE2    H  N N 243 
GLU HXT    H  N N 244 
GLY N      N  N N 245 
GLY CA     C  N N 246 
GLY C      C  N N 247 
GLY O      O  N N 248 
GLY OXT    O  N N 249 
GLY H      H  N N 250 
GLY H2     H  N N 251 
GLY HA2    H  N N 252 
GLY HA3    H  N N 253 
GLY HXT    H  N N 254 
HIS N      N  N N 255 
HIS CA     C  N S 256 
HIS C      C  N N 257 
HIS O      O  N N 258 
HIS CB     C  N N 259 
HIS CG     C  Y N 260 
HIS ND1    N  Y N 261 
HIS CD2    C  Y N 262 
HIS CE1    C  Y N 263 
HIS NE2    N  Y N 264 
HIS OXT    O  N N 265 
HIS H      H  N N 266 
HIS H2     H  N N 267 
HIS HA     H  N N 268 
HIS HB2    H  N N 269 
HIS HB3    H  N N 270 
HIS HD1    H  N N 271 
HIS HD2    H  N N 272 
HIS HE1    H  N N 273 
HIS HE2    H  N N 274 
HIS HXT    H  N N 275 
HOH O      O  N N 276 
HOH H1     H  N N 277 
HOH H2     H  N N 278 
ILE N      N  N N 279 
ILE CA     C  N S 280 
ILE C      C  N N 281 
ILE O      O  N N 282 
ILE CB     C  N S 283 
ILE CG1    C  N N 284 
ILE CG2    C  N N 285 
ILE CD1    C  N N 286 
ILE OXT    O  N N 287 
ILE H      H  N N 288 
ILE H2     H  N N 289 
ILE HA     H  N N 290 
ILE HB     H  N N 291 
ILE HG12   H  N N 292 
ILE HG13   H  N N 293 
ILE HG21   H  N N 294 
ILE HG22   H  N N 295 
ILE HG23   H  N N 296 
ILE HD11   H  N N 297 
ILE HD12   H  N N 298 
ILE HD13   H  N N 299 
ILE HXT    H  N N 300 
LEU N      N  N N 301 
LEU CA     C  N S 302 
LEU C      C  N N 303 
LEU O      O  N N 304 
LEU CB     C  N N 305 
LEU CG     C  N N 306 
LEU CD1    C  N N 307 
LEU CD2    C  N N 308 
LEU OXT    O  N N 309 
LEU H      H  N N 310 
LEU H2     H  N N 311 
LEU HA     H  N N 312 
LEU HB2    H  N N 313 
LEU HB3    H  N N 314 
LEU HG     H  N N 315 
LEU HD11   H  N N 316 
LEU HD12   H  N N 317 
LEU HD13   H  N N 318 
LEU HD21   H  N N 319 
LEU HD22   H  N N 320 
LEU HD23   H  N N 321 
LEU HXT    H  N N 322 
LYS N      N  N N 323 
LYS CA     C  N S 324 
LYS C      C  N N 325 
LYS O      O  N N 326 
LYS CB     C  N N 327 
LYS CG     C  N N 328 
LYS CD     C  N N 329 
LYS CE     C  N N 330 
LYS NZ     N  N N 331 
LYS OXT    O  N N 332 
LYS H      H  N N 333 
LYS H2     H  N N 334 
LYS HA     H  N N 335 
LYS HB2    H  N N 336 
LYS HB3    H  N N 337 
LYS HG2    H  N N 338 
LYS HG3    H  N N 339 
LYS HD2    H  N N 340 
LYS HD3    H  N N 341 
LYS HE2    H  N N 342 
LYS HE3    H  N N 343 
LYS HZ1    H  N N 344 
LYS HZ2    H  N N 345 
LYS HZ3    H  N N 346 
LYS HXT    H  N N 347 
MET N      N  N N 348 
MET CA     C  N S 349 
MET C      C  N N 350 
MET O      O  N N 351 
MET CB     C  N N 352 
MET CG     C  N N 353 
MET SD     S  N N 354 
MET CE     C  N N 355 
MET OXT    O  N N 356 
MET H      H  N N 357 
MET H2     H  N N 358 
MET HA     H  N N 359 
MET HB2    H  N N 360 
MET HB3    H  N N 361 
MET HG2    H  N N 362 
MET HG3    H  N N 363 
MET HE1    H  N N 364 
MET HE2    H  N N 365 
MET HE3    H  N N 366 
MET HXT    H  N N 367 
MG  MG     MG N N 368 
PHE N      N  N N 369 
PHE CA     C  N S 370 
PHE C      C  N N 371 
PHE O      O  N N 372 
PHE CB     C  N N 373 
PHE CG     C  Y N 374 
PHE CD1    C  Y N 375 
PHE CD2    C  Y N 376 
PHE CE1    C  Y N 377 
PHE CE2    C  Y N 378 
PHE CZ     C  Y N 379 
PHE OXT    O  N N 380 
PHE H      H  N N 381 
PHE H2     H  N N 382 
PHE HA     H  N N 383 
PHE HB2    H  N N 384 
PHE HB3    H  N N 385 
PHE HD1    H  N N 386 
PHE HD2    H  N N 387 
PHE HE1    H  N N 388 
PHE HE2    H  N N 389 
PHE HZ     H  N N 390 
PHE HXT    H  N N 391 
PRO N      N  N N 392 
PRO CA     C  N S 393 
PRO C      C  N N 394 
PRO O      O  N N 395 
PRO CB     C  N N 396 
PRO CG     C  N N 397 
PRO CD     C  N N 398 
PRO OXT    O  N N 399 
PRO H      H  N N 400 
PRO HA     H  N N 401 
PRO HB2    H  N N 402 
PRO HB3    H  N N 403 
PRO HG2    H  N N 404 
PRO HG3    H  N N 405 
PRO HD2    H  N N 406 
PRO HD3    H  N N 407 
PRO HXT    H  N N 408 
SER N      N  N N 409 
SER CA     C  N S 410 
SER C      C  N N 411 
SER O      O  N N 412 
SER CB     C  N N 413 
SER OG     O  N N 414 
SER OXT    O  N N 415 
SER H      H  N N 416 
SER H2     H  N N 417 
SER HA     H  N N 418 
SER HB2    H  N N 419 
SER HB3    H  N N 420 
SER HG     H  N N 421 
SER HXT    H  N N 422 
THR N      N  N N 423 
THR CA     C  N S 424 
THR C      C  N N 425 
THR O      O  N N 426 
THR CB     C  N R 427 
THR OG1    O  N N 428 
THR CG2    C  N N 429 
THR OXT    O  N N 430 
THR H      H  N N 431 
THR H2     H  N N 432 
THR HA     H  N N 433 
THR HB     H  N N 434 
THR HG1    H  N N 435 
THR HG21   H  N N 436 
THR HG22   H  N N 437 
THR HG23   H  N N 438 
THR HXT    H  N N 439 
TYR N      N  N N 440 
TYR CA     C  N S 441 
TYR C      C  N N 442 
TYR O      O  N N 443 
TYR CB     C  N N 444 
TYR CG     C  Y N 445 
TYR CD1    C  Y N 446 
TYR CD2    C  Y N 447 
TYR CE1    C  Y N 448 
TYR CE2    C  Y N 449 
TYR CZ     C  Y N 450 
TYR OH     O  N N 451 
TYR OXT    O  N N 452 
TYR H      H  N N 453 
TYR H2     H  N N 454 
TYR HA     H  N N 455 
TYR HB2    H  N N 456 
TYR HB3    H  N N 457 
TYR HD1    H  N N 458 
TYR HD2    H  N N 459 
TYR HE1    H  N N 460 
TYR HE2    H  N N 461 
TYR HH     H  N N 462 
TYR HXT    H  N N 463 
VAL N      N  N N 464 
VAL CA     C  N S 465 
VAL C      C  N N 466 
VAL O      O  N N 467 
VAL CB     C  N N 468 
VAL CG1    C  N N 469 
VAL CG2    C  N N 470 
VAL OXT    O  N N 471 
VAL H      H  N N 472 
VAL H2     H  N N 473 
VAL HA     H  N N 474 
VAL HB     H  N N 475 
VAL HG11   H  N N 476 
VAL HG12   H  N N 477 
VAL HG13   H  N N 478 
VAL HG21   H  N N 479 
VAL HG22   H  N N 480 
VAL HG23   H  N N 481 
VAL HXT    H  N N 482 
# 
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 
6IC O02   C17    sing N N 1   
6IC C17   C16    doub Y N 2   
6IC C17   C18    sing Y N 3   
6IC C16   C08    sing Y N 4   
6IC C18   C19    doub Y N 5   
6IC N03   C05    doub Y N 6   
6IC N03   C06    sing Y N 7   
6IC C08   C06    sing N N 8   
6IC C08   C20    doub Y N 9   
6IC C05   C01    sing Y N 10  
6IC C06   C07    doub Y N 11  
6IC C19   C20    sing Y N 12  
6IC C19   C21    sing Y N 13  
6IC C20   C24    sing Y N 14  
6IC C01   C02    doub Y N 15  
6IC C01   C04    sing Y N 16  
6IC C07   C02    sing Y N 17  
6IC C07   F01    sing N N 18  
6IC C13   N04    sing N N 19  
6IC C13   C12    sing N N 20  
6IC C29   N06    sing N N 21  
6IC C29   C30    sing N N 22  
6IC N04   C04    sing N N 23  
6IC N04   C10    sing N N 24  
6IC C02   N01    sing Y N 25  
6IC C04   N02    doub Y N 26  
6IC C21   C22    doub Y N 27  
6IC N06   C28    sing N N 28  
6IC N06   C25    sing N N 29  
6IC C10   C11    sing N N 30  
6IC C30   C31    sing N N 31  
6IC N02   C03    sing Y N 32  
6IC C28   C27    sing N N 33  
6IC N01   C03    doub Y N 34  
6IC C03   O01    sing N N 35  
6IC C12   N05    sing N N 36  
6IC C12   C14    sing N N 37  
6IC N05   C11    sing N N 38  
6IC C24   C32    sing N N 39  
6IC C24   C23    doub Y N 40  
6IC O01   C09    sing N N 41  
6IC C09   C25    sing N N 42  
6IC C11   C15    sing N N 43  
6IC C22   C23    sing Y N 44  
6IC C25   C31    sing N N 45  
6IC C25   C26    sing N N 46  
6IC C32   C33    trip N N 47  
6IC C23   F23    sing N N 48  
6IC C27   F02    sing N N 49  
6IC C27   C26    sing N N 50  
6IC C14   C15    sing N N 51  
6IC C22   H1     sing N N 52  
6IC C21   H2     sing N N 53  
6IC C14   H3     sing N N 54  
6IC C14   H4     sing N N 55  
6IC C13   H5     sing N N 56  
6IC C13   H6     sing N N 57  
6IC C18   H7     sing N N 58  
6IC C05   H8     sing N N 59  
6IC C09   H9     sing N N 60  
6IC C09   H10    sing N N 61  
6IC C10   H11    sing N N 62  
6IC C10   H12    sing N N 63  
6IC C11   H13    sing N N 64  
6IC C12   H14    sing N N 65  
6IC C15   H15    sing N N 66  
6IC C15   H16    sing N N 67  
6IC C16   H17    sing N N 68  
6IC C26   H18    sing N N 69  
6IC C26   H19    sing N N 70  
6IC C27   H20    sing N N 71  
6IC C28   H21    sing N N 72  
6IC C28   H22    sing N N 73  
6IC C29   H23    sing N N 74  
6IC C29   H24    sing N N 75  
6IC C30   H25    sing N N 76  
6IC C30   H26    sing N N 77  
6IC C31   H27    sing N N 78  
6IC C31   H28    sing N N 79  
6IC C33   H29    sing N N 80  
6IC N05   H30    sing N N 81  
6IC O02   H33    sing N N 82  
ALA N     CA     sing N N 83  
ALA N     H      sing N N 84  
ALA N     H2     sing N N 85  
ALA CA    C      sing N N 86  
ALA CA    CB     sing N N 87  
ALA CA    HA     sing N N 88  
ALA C     O      doub N N 89  
ALA C     OXT    sing N N 90  
ALA CB    HB1    sing N N 91  
ALA CB    HB2    sing N N 92  
ALA CB    HB3    sing N N 93  
ALA OXT   HXT    sing N N 94  
ARG N     CA     sing N N 95  
ARG N     H      sing N N 96  
ARG N     H2     sing N N 97  
ARG CA    C      sing N N 98  
ARG CA    CB     sing N N 99  
ARG CA    HA     sing N N 100 
ARG C     O      doub N N 101 
ARG C     OXT    sing N N 102 
ARG CB    CG     sing N N 103 
ARG CB    HB2    sing N N 104 
ARG CB    HB3    sing N N 105 
ARG CG    CD     sing N N 106 
ARG CG    HG2    sing N N 107 
ARG CG    HG3    sing N N 108 
ARG CD    NE     sing N N 109 
ARG CD    HD2    sing N N 110 
ARG CD    HD3    sing N N 111 
ARG NE    CZ     sing N N 112 
ARG NE    HE     sing N N 113 
ARG CZ    NH1    sing N N 114 
ARG CZ    NH2    doub N N 115 
ARG NH1   HH11   sing N N 116 
ARG NH1   HH12   sing N N 117 
ARG NH2   HH21   sing N N 118 
ARG NH2   HH22   sing N N 119 
ARG OXT   HXT    sing N N 120 
ASN N     CA     sing N N 121 
ASN N     H      sing N N 122 
ASN N     H2     sing N N 123 
ASN CA    C      sing N N 124 
ASN CA    CB     sing N N 125 
ASN CA    HA     sing N N 126 
ASN C     O      doub N N 127 
ASN C     OXT    sing N N 128 
ASN CB    CG     sing N N 129 
ASN CB    HB2    sing N N 130 
ASN CB    HB3    sing N N 131 
ASN CG    OD1    doub N N 132 
ASN CG    ND2    sing N N 133 
ASN ND2   HD21   sing N N 134 
ASN ND2   HD22   sing N N 135 
ASN OXT   HXT    sing N N 136 
ASP N     CA     sing N N 137 
ASP N     H      sing N N 138 
ASP N     H2     sing N N 139 
ASP CA    C      sing N N 140 
ASP CA    CB     sing N N 141 
ASP CA    HA     sing N N 142 
ASP C     O      doub N N 143 
ASP C     OXT    sing N N 144 
ASP CB    CG     sing N N 145 
ASP CB    HB2    sing N N 146 
ASP CB    HB3    sing N N 147 
ASP CG    OD1    doub N N 148 
ASP CG    OD2    sing N N 149 
ASP OD2   HD2    sing N N 150 
ASP OXT   HXT    sing N N 151 
CYS N     CA     sing N N 152 
CYS N     H      sing N N 153 
CYS N     H2     sing N N 154 
CYS CA    C      sing N N 155 
CYS CA    CB     sing N N 156 
CYS CA    HA     sing N N 157 
CYS C     O      doub N N 158 
CYS C     OXT    sing N N 159 
CYS CB    SG     sing N N 160 
CYS CB    HB2    sing N N 161 
CYS CB    HB3    sing N N 162 
CYS SG    HG     sing N N 163 
CYS OXT   HXT    sing N N 164 
GDP PB    O1B    doub N N 165 
GDP PB    O2B    sing N N 166 
GDP PB    O3B    sing N N 167 
GDP PB    O3A    sing N N 168 
GDP O2B   HOB2   sing N N 169 
GDP O3B   HOB3   sing N N 170 
GDP O3A   PA     sing N N 171 
GDP PA    O1A    doub N N 172 
GDP PA    O2A    sing N N 173 
GDP PA    "O5'"  sing N N 174 
GDP O2A   HOA2   sing N N 175 
GDP "O5'" "C5'"  sing N N 176 
GDP "C5'" "C4'"  sing N N 177 
GDP "C5'" "H5'"  sing N N 178 
GDP "C5'" "H5''" sing N N 179 
GDP "C4'" "O4'"  sing N N 180 
GDP "C4'" "C3'"  sing N N 181 
GDP "C4'" "H4'"  sing N N 182 
GDP "O4'" "C1'"  sing N N 183 
GDP "C3'" "O3'"  sing N N 184 
GDP "C3'" "C2'"  sing N N 185 
GDP "C3'" "H3'"  sing N N 186 
GDP "O3'" "HO3'" sing N N 187 
GDP "C2'" "O2'"  sing N N 188 
GDP "C2'" "C1'"  sing N N 189 
GDP "C2'" "H2'"  sing N N 190 
GDP "O2'" "HO2'" sing N N 191 
GDP "C1'" N9     sing N N 192 
GDP "C1'" "H1'"  sing N N 193 
GDP N9    C8     sing Y N 194 
GDP N9    C4     sing Y N 195 
GDP C8    N7     doub Y N 196 
GDP C8    H8     sing N N 197 
GDP N7    C5     sing Y N 198 
GDP C5    C6     sing N N 199 
GDP C5    C4     doub Y N 200 
GDP C6    O6     doub N N 201 
GDP C6    N1     sing N N 202 
GDP N1    C2     sing N N 203 
GDP N1    HN1    sing N N 204 
GDP C2    N2     sing N N 205 
GDP C2    N3     doub N N 206 
GDP N2    HN21   sing N N 207 
GDP N2    HN22   sing N N 208 
GDP N3    C4     sing N N 209 
GLN N     CA     sing N N 210 
GLN N     H      sing N N 211 
GLN N     H2     sing N N 212 
GLN CA    C      sing N N 213 
GLN CA    CB     sing N N 214 
GLN CA    HA     sing N N 215 
GLN C     O      doub N N 216 
GLN C     OXT    sing N N 217 
GLN CB    CG     sing N N 218 
GLN CB    HB2    sing N N 219 
GLN CB    HB3    sing N N 220 
GLN CG    CD     sing N N 221 
GLN CG    HG2    sing N N 222 
GLN CG    HG3    sing N N 223 
GLN CD    OE1    doub N N 224 
GLN CD    NE2    sing N N 225 
GLN NE2   HE21   sing N N 226 
GLN NE2   HE22   sing N N 227 
GLN OXT   HXT    sing N N 228 
GLU N     CA     sing N N 229 
GLU N     H      sing N N 230 
GLU N     H2     sing N N 231 
GLU CA    C      sing N N 232 
GLU CA    CB     sing N N 233 
GLU CA    HA     sing N N 234 
GLU C     O      doub N N 235 
GLU C     OXT    sing N N 236 
GLU CB    CG     sing N N 237 
GLU CB    HB2    sing N N 238 
GLU CB    HB3    sing N N 239 
GLU CG    CD     sing N N 240 
GLU CG    HG2    sing N N 241 
GLU CG    HG3    sing N N 242 
GLU CD    OE1    doub N N 243 
GLU CD    OE2    sing N N 244 
GLU OE2   HE2    sing N N 245 
GLU OXT   HXT    sing N N 246 
GLY N     CA     sing N N 247 
GLY N     H      sing N N 248 
GLY N     H2     sing N N 249 
GLY CA    C      sing N N 250 
GLY CA    HA2    sing N N 251 
GLY CA    HA3    sing N N 252 
GLY C     O      doub N N 253 
GLY C     OXT    sing N N 254 
GLY OXT   HXT    sing N N 255 
HIS N     CA     sing N N 256 
HIS N     H      sing N N 257 
HIS N     H2     sing N N 258 
HIS CA    C      sing N N 259 
HIS CA    CB     sing N N 260 
HIS CA    HA     sing N N 261 
HIS C     O      doub N N 262 
HIS C     OXT    sing N N 263 
HIS CB    CG     sing N N 264 
HIS CB    HB2    sing N N 265 
HIS CB    HB3    sing N N 266 
HIS CG    ND1    sing Y N 267 
HIS CG    CD2    doub Y N 268 
HIS ND1   CE1    doub Y N 269 
HIS ND1   HD1    sing N N 270 
HIS CD2   NE2    sing Y N 271 
HIS CD2   HD2    sing N N 272 
HIS CE1   NE2    sing Y N 273 
HIS CE1   HE1    sing N N 274 
HIS NE2   HE2    sing N N 275 
HIS OXT   HXT    sing N N 276 
HOH O     H1     sing N N 277 
HOH O     H2     sing N N 278 
ILE N     CA     sing N N 279 
ILE N     H      sing N N 280 
ILE N     H2     sing N N 281 
ILE CA    C      sing N N 282 
ILE CA    CB     sing N N 283 
ILE CA    HA     sing N N 284 
ILE C     O      doub N N 285 
ILE C     OXT    sing N N 286 
ILE CB    CG1    sing N N 287 
ILE CB    CG2    sing N N 288 
ILE CB    HB     sing N N 289 
ILE CG1   CD1    sing N N 290 
ILE CG1   HG12   sing N N 291 
ILE CG1   HG13   sing N N 292 
ILE CG2   HG21   sing N N 293 
ILE CG2   HG22   sing N N 294 
ILE CG2   HG23   sing N N 295 
ILE CD1   HD11   sing N N 296 
ILE CD1   HD12   sing N N 297 
ILE CD1   HD13   sing N N 298 
ILE OXT   HXT    sing N N 299 
LEU N     CA     sing N N 300 
LEU N     H      sing N N 301 
LEU N     H2     sing N N 302 
LEU CA    C      sing N N 303 
LEU CA    CB     sing N N 304 
LEU CA    HA     sing N N 305 
LEU C     O      doub N N 306 
LEU C     OXT    sing N N 307 
LEU CB    CG     sing N N 308 
LEU CB    HB2    sing N N 309 
LEU CB    HB3    sing N N 310 
LEU CG    CD1    sing N N 311 
LEU CG    CD2    sing N N 312 
LEU CG    HG     sing N N 313 
LEU CD1   HD11   sing N N 314 
LEU CD1   HD12   sing N N 315 
LEU CD1   HD13   sing N N 316 
LEU CD2   HD21   sing N N 317 
LEU CD2   HD22   sing N N 318 
LEU CD2   HD23   sing N N 319 
LEU OXT   HXT    sing N N 320 
LYS N     CA     sing N N 321 
LYS N     H      sing N N 322 
LYS N     H2     sing N N 323 
LYS CA    C      sing N N 324 
LYS CA    CB     sing N N 325 
LYS CA    HA     sing N N 326 
LYS C     O      doub N N 327 
LYS C     OXT    sing N N 328 
LYS CB    CG     sing N N 329 
LYS CB    HB2    sing N N 330 
LYS CB    HB3    sing N N 331 
LYS CG    CD     sing N N 332 
LYS CG    HG2    sing N N 333 
LYS CG    HG3    sing N N 334 
LYS CD    CE     sing N N 335 
LYS CD    HD2    sing N N 336 
LYS CD    HD3    sing N N 337 
LYS CE    NZ     sing N N 338 
LYS CE    HE2    sing N N 339 
LYS CE    HE3    sing N N 340 
LYS NZ    HZ1    sing N N 341 
LYS NZ    HZ2    sing N N 342 
LYS NZ    HZ3    sing N N 343 
LYS OXT   HXT    sing N N 344 
MET N     CA     sing N N 345 
MET N     H      sing N N 346 
MET N     H2     sing N N 347 
MET CA    C      sing N N 348 
MET CA    CB     sing N N 349 
MET CA    HA     sing N N 350 
MET C     O      doub N N 351 
MET C     OXT    sing N N 352 
MET CB    CG     sing N N 353 
MET CB    HB2    sing N N 354 
MET CB    HB3    sing N N 355 
MET CG    SD     sing N N 356 
MET CG    HG2    sing N N 357 
MET CG    HG3    sing N N 358 
MET SD    CE     sing N N 359 
MET CE    HE1    sing N N 360 
MET CE    HE2    sing N N 361 
MET CE    HE3    sing N N 362 
MET OXT   HXT    sing N N 363 
PHE N     CA     sing N N 364 
PHE N     H      sing N N 365 
PHE N     H2     sing N N 366 
PHE CA    C      sing N N 367 
PHE CA    CB     sing N N 368 
PHE CA    HA     sing N N 369 
PHE C     O      doub N N 370 
PHE C     OXT    sing N N 371 
PHE CB    CG     sing N N 372 
PHE CB    HB2    sing N N 373 
PHE CB    HB3    sing N N 374 
PHE CG    CD1    doub Y N 375 
PHE CG    CD2    sing Y N 376 
PHE CD1   CE1    sing Y N 377 
PHE CD1   HD1    sing N N 378 
PHE CD2   CE2    doub Y N 379 
PHE CD2   HD2    sing N N 380 
PHE CE1   CZ     doub Y N 381 
PHE CE1   HE1    sing N N 382 
PHE CE2   CZ     sing Y N 383 
PHE CE2   HE2    sing N N 384 
PHE CZ    HZ     sing N N 385 
PHE OXT   HXT    sing N N 386 
PRO N     CA     sing N N 387 
PRO N     CD     sing N N 388 
PRO N     H      sing N N 389 
PRO CA    C      sing N N 390 
PRO CA    CB     sing N N 391 
PRO CA    HA     sing N N 392 
PRO C     O      doub N N 393 
PRO C     OXT    sing N N 394 
PRO CB    CG     sing N N 395 
PRO CB    HB2    sing N N 396 
PRO CB    HB3    sing N N 397 
PRO CG    CD     sing N N 398 
PRO CG    HG2    sing N N 399 
PRO CG    HG3    sing N N 400 
PRO CD    HD2    sing N N 401 
PRO CD    HD3    sing N N 402 
PRO OXT   HXT    sing N N 403 
SER N     CA     sing N N 404 
SER N     H      sing N N 405 
SER N     H2     sing N N 406 
SER CA    C      sing N N 407 
SER CA    CB     sing N N 408 
SER CA    HA     sing N N 409 
SER C     O      doub N N 410 
SER C     OXT    sing N N 411 
SER CB    OG     sing N N 412 
SER CB    HB2    sing N N 413 
SER CB    HB3    sing N N 414 
SER OG    HG     sing N N 415 
SER OXT   HXT    sing N N 416 
THR N     CA     sing N N 417 
THR N     H      sing N N 418 
THR N     H2     sing N N 419 
THR CA    C      sing N N 420 
THR CA    CB     sing N N 421 
THR CA    HA     sing N N 422 
THR C     O      doub N N 423 
THR C     OXT    sing N N 424 
THR CB    OG1    sing N N 425 
THR CB    CG2    sing N N 426 
THR CB    HB     sing N N 427 
THR OG1   HG1    sing N N 428 
THR CG2   HG21   sing N N 429 
THR CG2   HG22   sing N N 430 
THR CG2   HG23   sing N N 431 
THR OXT   HXT    sing N N 432 
TYR N     CA     sing N N 433 
TYR N     H      sing N N 434 
TYR N     H2     sing N N 435 
TYR CA    C      sing N N 436 
TYR CA    CB     sing N N 437 
TYR CA    HA     sing N N 438 
TYR C     O      doub N N 439 
TYR C     OXT    sing N N 440 
TYR CB    CG     sing N N 441 
TYR CB    HB2    sing N N 442 
TYR CB    HB3    sing N N 443 
TYR CG    CD1    doub Y N 444 
TYR CG    CD2    sing Y N 445 
TYR CD1   CE1    sing Y N 446 
TYR CD1   HD1    sing N N 447 
TYR CD2   CE2    doub Y N 448 
TYR CD2   HD2    sing N N 449 
TYR CE1   CZ     doub Y N 450 
TYR CE1   HE1    sing N N 451 
TYR CE2   CZ     sing Y N 452 
TYR CE2   HE2    sing N N 453 
TYR CZ    OH     sing N N 454 
TYR OH    HH     sing N N 455 
TYR OXT   HXT    sing N N 456 
VAL N     CA     sing N N 457 
VAL N     H      sing N N 458 
VAL N     H2     sing N N 459 
VAL CA    C      sing N N 460 
VAL CA    CB     sing N N 461 
VAL CA    HA     sing N N 462 
VAL C     O      doub N N 463 
VAL C     OXT    sing N N 464 
VAL CB    CG1    sing N N 465 
VAL CB    CG2    sing N N 466 
VAL CB    HB     sing N N 467 
VAL CG1   HG11   sing N N 468 
VAL CG1   HG12   sing N N 469 
VAL CG1   HG13   sing N N 470 
VAL CG2   HG21   sing N N 471 
VAL CG2   HG22   sing N N 472 
VAL CG2   HG23   sing N N 473 
VAL OXT   HXT    sing N N 474 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' CA201402    1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' P30GM124166 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7RPZ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 :H' 
_space_group.name_Hall        'R 3' 
_space_group.IT_number        146 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BL0 
_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]   0.013269 
_atom_sites.fract_transf_matrix[1][2]   0.007661 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015322 
_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]   0.004905 
_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.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? 38.145 15.007  -23.807 1.00 48.19 ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 37.069 14.860  -22.796 1.00 47.44 ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 36.637 13.390  -22.716 1.00 44.26 ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 36.470 12.747  -23.754 1.00 43.37 ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 35.844 15.692  -23.182 1.00 49.54 ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 34.910 16.033  -22.057 1.00 44.27 ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 33.930 17.443  -22.599 1.00 74.28 ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 33.560 16.980  -24.295 1.00 48.48 ? 1   MET A CE    1 
ATOM   9    N  N     . THR A 1 2   ? 36.418 12.911  -21.503 1.00 44.32 ? 2   THR A N     1 
ATOM   10   C  CA    . THR A 1 2   ? 35.920 11.541  -21.394 1.00 40.75 ? 2   THR A CA    1 
ATOM   11   C  C     . THR A 1 2   ? 34.393 11.521  -21.320 1.00 35.14 ? 2   THR A C     1 
ATOM   12   O  O     . THR A 1 2   ? 33.792 12.282  -20.552 1.00 31.67 ? 2   THR A O     1 
ATOM   13   C  CB    . THR A 1 2   ? 36.555 10.806  -20.216 1.00 41.15 ? 2   THR A CB    1 
ATOM   14   O  OG1   . THR A 1 2   ? 35.875 11.141  -19.013 1.00 47.61 ? 2   THR A OG1   1 
ATOM   15   C  CG2   . THR A 1 2   ? 38.010 11.195  -20.089 1.00 38.14 ? 2   THR A CG2   1 
ATOM   16   N  N     . GLU A 1 3   ? 33.773 10.644  -22.121 1.00 32.09 ? 3   GLU A N     1 
ATOM   17   C  CA    . GLU A 1 3   ? 32.319 10.509  -22.201 1.00 31.77 ? 3   GLU A CA    1 
ATOM   18   C  C     . GLU A 1 3   ? 31.830 9.343   -21.337 1.00 30.11 ? 3   GLU A C     1 
ATOM   19   O  O     . GLU A 1 3   ? 32.484 8.299   -21.257 1.00 29.73 ? 3   GLU A O     1 
ATOM   20   C  CB    . GLU A 1 3   ? 31.897 10.304  -23.664 1.00 35.61 ? 3   GLU A CB    1 
ATOM   21   C  CG    . GLU A 1 3   ? 30.412 10.012  -23.880 1.00 40.70 ? 3   GLU A CG    1 
ATOM   22   C  CD    . GLU A 1 3   ? 29.936 10.402  -25.284 1.00 53.06 ? 3   GLU A CD    1 
ATOM   23   O  OE1   . GLU A 1 3   ? 30.651 11.192  -25.949 1.00 56.58 ? 3   GLU A OE1   1 
ATOM   24   O  OE2   . GLU A 1 3   ? 28.840 9.960   -25.702 1.00 53.63 ? 3   GLU A OE2   1 
ATOM   25   N  N     . TYR A 1 4   ? 30.703 9.543   -20.638 1.00 22.22 ? 4   TYR A N     1 
ATOM   26   C  CA    . TYR A 1 4   ? 30.089 8.501   -19.813 1.00 21.90 ? 4   TYR A CA    1 
ATOM   27   C  C     . TYR A 1 4   ? 28.629 8.337   -20.215 1.00 26.61 ? 4   TYR A C     1 
ATOM   28   O  O     . TYR A 1 4   ? 27.882 9.323   -20.217 1.00 25.13 ? 4   TYR A O     1 
ATOM   29   C  CB    . TYR A 1 4   ? 30.149 8.854   -18.325 1.00 23.55 ? 4   TYR A CB    1 
ATOM   30   C  CG    . TYR A 1 4   ? 31.542 8.925   -17.720 1.00 26.60 ? 4   TYR A CG    1 
ATOM   31   C  CD1   . TYR A 1 4   ? 32.175 7.777   -17.252 1.00 26.81 ? 4   TYR A CD1   1 
ATOM   32   C  CD2   . TYR A 1 4   ? 32.213 10.147  -17.597 1.00 28.35 ? 4   TYR A CD2   1 
ATOM   33   C  CE1   . TYR A 1 4   ? 33.442 7.836   -16.684 1.00 27.73 ? 4   TYR A CE1   1 
ATOM   34   C  CE2   . TYR A 1 4   ? 33.481 10.209  -17.036 1.00 32.29 ? 4   TYR A CE2   1 
ATOM   35   C  CZ    . TYR A 1 4   ? 34.087 9.051   -16.581 1.00 32.84 ? 4   TYR A CZ    1 
ATOM   36   O  OH    . TYR A 1 4   ? 35.341 9.107   -16.016 1.00 32.87 ? 4   TYR A OH    1 
ATOM   37   N  N     . LYS A 1 5   ? 28.206 7.091   -20.494 1.00 21.71 ? 5   LYS A N     1 
ATOM   38   C  CA    . LYS A 1 5   ? 26.819 6.787   -20.872 1.00 23.67 ? 5   LYS A CA    1 
ATOM   39   C  C     . LYS A 1 5   ? 26.080 6.291   -19.628 1.00 18.89 ? 5   LYS A C     1 
ATOM   40   O  O     . LYS A 1 5   ? 26.360 5.187   -19.122 1.00 19.10 ? 5   LYS A O     1 
ATOM   41   C  CB    . LYS A 1 5   ? 26.774 5.736   -21.986 1.00 23.88 ? 5   LYS A CB    1 
ATOM   42   C  CG    . LYS A 1 5   ? 27.623 6.058   -23.216 1.00 36.28 ? 5   LYS A CG    1 
ATOM   43   C  CD    . LYS A 1 5   ? 27.133 7.289   -23.950 1.00 38.30 ? 5   LYS A CD    1 
ATOM   44   C  CE    . LYS A 1 5   ? 26.513 6.908   -25.303 1.00 47.85 ? 5   LYS A CE    1 
ATOM   45   N  NZ    . LYS A 1 5   ? 27.530 6.851   -26.407 1.00 53.41 ? 5   LYS A NZ    1 
ATOM   46   N  N     . LEU A 1 6   ? 25.159 7.127   -19.105 1.00 16.07 ? 6   LEU A N     1 
ATOM   47   C  CA    . LEU A 1 6   ? 24.379 6.785   -17.929 1.00 15.97 ? 6   LEU A CA    1 
ATOM   48   C  C     . LEU A 1 6   ? 22.943 6.523   -18.350 1.00 20.00 ? 6   LEU A C     1 
ATOM   49   O  O     . LEU A 1 6   ? 22.434 7.167   -19.273 1.00 18.79 ? 6   LEU A O     1 
ATOM   50   C  CB    . LEU A 1 6   ? 24.389 7.899   -16.874 1.00 18.95 ? 6   LEU A CB    1 
ATOM   51   C  CG    . LEU A 1 6   ? 25.721 8.552   -16.499 1.00 21.09 ? 6   LEU A CG    1 
ATOM   52   C  CD1   . LEU A 1 6   ? 25.526 9.500   -15.317 1.00 21.81 ? 6   LEU A CD1   1 
ATOM   53   C  CD2   . LEU A 1 6   ? 26.742 7.508   -16.178 1.00 24.89 ? 6   LEU A CD2   1 
ATOM   54   N  N     . VAL A 1 7   ? 22.297 5.569   -17.683 1.00 16.31 ? 7   VAL A N     1 
ATOM   55   C  CA    . VAL A 1 7   ? 20.899 5.267   -17.973 1.00 16.17 ? 7   VAL A CA    1 
ATOM   56   C  C     . VAL A 1 7   ? 20.105 5.320   -16.676 1.00 17.64 ? 7   VAL A C     1 
ATOM   57   O  O     . VAL A 1 7   ? 20.511 4.720   -15.678 1.00 16.04 ? 7   VAL A O     1 
ATOM   58   C  CB    . VAL A 1 7   ? 20.757 3.884   -18.626 1.00 17.04 ? 7   VAL A CB    1 
ATOM   59   C  CG1   . VAL A 1 7   ? 19.273 3.591   -18.935 1.00 18.53 ? 7   VAL A CG1   1 
ATOM   60   C  CG2   . VAL A 1 7   ? 21.614 3.794   -19.864 1.00 18.68 ? 7   VAL A CG2   1 
ATOM   61   N  N     . VAL A 1 8   ? 18.955 6.003   -16.694 1.00 14.57 ? 8   VAL A N     1 
ATOM   62   C  CA    . VAL A 1 8   ? 18.119 6.153   -15.508 1.00 15.17 ? 8   VAL A CA    1 
ATOM   63   C  C     . VAL A 1 8   ? 16.904 5.256   -15.707 1.00 15.52 ? 8   VAL A C     1 
ATOM   64   O  O     . VAL A 1 8   ? 16.142 5.460   -16.657 1.00 14.07 ? 8   VAL A O     1 
ATOM   65   C  CB    . VAL A 1 8   ? 17.697 7.619   -15.286 1.00 16.03 ? 8   VAL A CB    1 
ATOM   66   C  CG1   . VAL A 1 8   ? 16.851 7.742   -13.993 1.00 16.11 ? 8   VAL A CG1   1 
ATOM   67   C  CG2   . VAL A 1 8   ? 18.915 8.554   -15.223 1.00 17.85 ? 8   VAL A CG2   1 
ATOM   68   N  N     . VAL A 1 9   ? 16.719 4.257   -14.826 1.00 16.19 ? 9   VAL A N     1 
ATOM   69   C  CA    . VAL A 1 9   ? 15.624 3.298   -14.970 1.00 14.42 ? 9   VAL A CA    1 
ATOM   70   C  C     . VAL A 1 9   ? 14.805 3.229   -13.685 1.00 15.86 ? 9   VAL A C     1 
ATOM   71   O  O     . VAL A 1 9   ? 15.240 3.657   -12.616 1.00 15.56 ? 9   VAL A O     1 
ATOM   72   C  CB    . VAL A 1 9   ? 16.110 1.892   -15.358 1.00 16.93 ? 9   VAL A CB    1 
ATOM   73   C  CG1   . VAL A 1 9   ? 16.879 1.949   -16.675 1.00 18.15 ? 9   VAL A CG1   1 
ATOM   74   C  CG2   . VAL A 1 9   ? 16.932 1.251   -14.245 1.00 18.08 ? 9   VAL A CG2   1 
ATOM   75   N  N     . GLY A 1 10  ? 13.607 2.665   -13.810 1.00 14.99 ? 10  GLY A N     1 
ATOM   76   C  CA    . GLY A 1 10  ? 12.698 2.511   -12.697 1.00 11.98 ? 10  GLY A CA    1 
ATOM   77   C  C     . GLY A 1 10  ? 11.263 2.723   -13.144 1.00 16.29 ? 10  GLY A C     1 
ATOM   78   O  O     . GLY A 1 10  ? 11.010 3.144   -14.279 1.00 15.61 ? 10  GLY A O     1 
ATOM   79   N  N     . ALA A 1 11  ? 10.322 2.470   -12.235 1.00 14.88 ? 11  ALA A N     1 
ATOM   80   C  CA    . ALA A 1 11  ? 8.890  2.549   -12.536 1.00 17.30 ? 11  ALA A CA    1 
ATOM   81   C  C     . ALA A 1 11  ? 8.465  3.959   -12.961 1.00 19.77 ? 11  ALA A C     1 
ATOM   82   O  O     . ALA A 1 11  ? 9.151  4.949   -12.713 1.00 17.65 ? 11  ALA A O     1 
ATOM   83   C  CB    . ALA A 1 11  ? 8.085  2.109   -11.306 1.00 16.22 ? 11  ALA A CB    1 
ATOM   84   N  N     . ASP A 1 12  ? 7.290  4.044   -13.593 1.00 14.74 ? 12  ASP A N     1 
ATOM   85   C  CA    . ASP A 1 12  ? 6.749  5.349   -13.958 1.00 18.90 ? 12  ASP A CA    1 
ATOM   86   C  C     . ASP A 1 12  ? 6.456  6.167   -12.709 1.00 22.11 ? 12  ASP A C     1 
ATOM   87   O  O     . ASP A 1 12  ? 6.014  5.627   -11.689 1.00 18.31 ? 12  ASP A O     1 
ATOM   88   C  CB    . ASP A 1 12  ? 5.434  5.227   -14.734 1.00 17.81 ? 12  ASP A CB    1 
ATOM   89   C  CG    . ASP A 1 12  ? 5.590  4.656   -16.110 1.00 22.12 ? 12  ASP A CG    1 
ATOM   90   O  OD1   . ASP A 1 12  ? 6.640  4.863   -16.759 1.00 19.18 ? 12  ASP A OD1   1 
ATOM   91   O  OD2   . ASP A 1 12  ? 4.597  4.030   -16.568 1.00 21.19 ? 12  ASP A OD2   1 
ATOM   92   N  N     . GLY A 1 13  ? 6.695  7.474   -12.787 1.00 14.54 ? 13  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 13  ? 6.260  8.368   -11.714 1.00 15.87 ? 13  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 13  ? 7.202  8.492   -10.533 1.00 23.66 ? 13  GLY A C     1 
ATOM   95   O  O     . GLY A 1 13  ? 6.834  9.113   -9.524  1.00 18.28 ? 13  GLY A O     1 
ATOM   96   N  N     . VAL A 1 14  ? 8.393  7.904   -10.603 1.00 18.39 ? 14  VAL A N     1 
ATOM   97   C  CA    . VAL A 1 14  ? 9.254  7.919   -9.432  1.00 16.29 ? 14  VAL A CA    1 
ATOM   98   C  C     . VAL A 1 14  ? 10.124 9.161   -9.413  1.00 16.74 ? 14  VAL A C     1 
ATOM   99   O  O     . VAL A 1 14  ? 10.750 9.441   -8.379  1.00 17.39 ? 14  VAL A O     1 
ATOM   100  C  CB    . VAL A 1 14  ? 10.131 6.660   -9.324  1.00 15.43 ? 14  VAL A CB    1 
ATOM   101  C  CG1   . VAL A 1 14  ? 9.253  5.407   -9.254  1.00 18.78 ? 14  VAL A CG1   1 
ATOM   102  C  CG2   . VAL A 1 14  ? 11.140 6.542   -10.491 1.00 15.55 ? 14  VAL A CG2   1 
ATOM   103  N  N     . GLY A 1 15  ? 10.200 9.889   -10.524 1.00 14.89 ? 15  GLY A N     1 
ATOM   104  C  CA    . GLY A 1 15  ? 11.002 11.084  -10.614 1.00 16.14 ? 15  GLY A CA    1 
ATOM   105  C  C     . GLY A 1 15  ? 12.264 10.958  -11.450 1.00 19.02 ? 15  GLY A C     1 
ATOM   106  O  O     . GLY A 1 15  ? 13.183 11.761  -11.261 1.00 17.85 ? 15  GLY A O     1 
ATOM   107  N  N     . LYS A 1 16  ? 12.343 9.978   -12.361 1.00 15.20 ? 16  LYS A N     1 
ATOM   108  C  CA    . LYS A 1 16  ? 13.515 9.872   -13.237 1.00 16.86 ? 16  LYS A CA    1 
ATOM   109  C  C     . LYS A 1 16  ? 13.755 11.156  -14.018 1.00 19.65 ? 16  LYS A C     1 
ATOM   110  O  O     . LYS A 1 16  ? 14.895 11.646  -14.115 1.00 18.65 ? 16  LYS A O     1 
ATOM   111  C  CB    . LYS A 1 16  ? 13.352 8.698   -14.211 1.00 17.56 ? 16  LYS A CB    1 
ATOM   112  C  CG    . LYS A 1 16  ? 13.243 7.326   -13.506 1.00 16.89 ? 16  LYS A CG    1 
ATOM   113  C  CD    . LYS A 1 16  ? 13.163 6.157   -14.506 1.00 16.10 ? 16  LYS A CD    1 
ATOM   114  C  CE    . LYS A 1 16  ? 11.936 6.249   -15.415 1.00 15.86 ? 16  LYS A CE    1 
ATOM   115  N  NZ    . LYS A 1 16  ? 10.630 6.297   -14.638 1.00 14.94 ? 16  LYS A NZ    1 
ATOM   116  N  N     . SER A 1 17  ? 12.697 11.699  -14.623 1.00 14.35 ? 17  SER A N     1 
ATOM   117  C  CA    . SER A 1 17  ? 12.870 12.882  -15.453 1.00 16.31 ? 17  SER A CA    1 
ATOM   118  C  C     . SER A 1 17  ? 13.179 14.103  -14.596 1.00 17.54 ? 17  SER A C     1 
ATOM   119  O  O     . SER A 1 17  ? 14.012 14.936  -14.967 1.00 18.73 ? 17  SER A O     1 
ATOM   120  C  CB    . SER A 1 17  ? 11.618 13.121  -16.306 1.00 17.38 ? 17  SER A CB    1 
ATOM   121  O  OG    . SER A 1 17  ? 11.411 12.057  -17.227 1.00 15.22 ? 17  SER A OG    1 
ATOM   122  N  N     . ALA A 1 18  ? 12.508 14.234  -13.458 1.00 16.28 ? 18  ALA A N     1 
ATOM   123  C  CA    . ALA A 1 18  ? 12.781 15.346  -12.549 1.00 20.18 ? 18  ALA A CA    1 
ATOM   124  C  C     . ALA A 1 18  ? 14.238 15.346  -12.090 1.00 20.64 ? 18  ALA A C     1 
ATOM   125  O  O     . ALA A 1 18  ? 14.889 16.394  -12.071 1.00 19.27 ? 18  ALA A O     1 
ATOM   126  C  CB    . ALA A 1 18  ? 11.843 15.265  -11.347 1.00 22.88 ? 18  ALA A CB    1 
ATOM   127  N  N     . LEU A 1 19  ? 14.757 14.177  -11.703 1.00 20.68 ? 19  LEU A N     1 
ATOM   128  C  CA    . LEU A 1 19  ? 16.173 14.055  -11.332 1.00 19.53 ? 19  LEU A CA    1 
ATOM   129  C  C     . LEU A 1 19  ? 17.078 14.482  -12.479 1.00 21.16 ? 19  LEU A C     1 
ATOM   130  O  O     . LEU A 1 19  ? 18.034 15.253  -12.287 1.00 21.27 ? 19  LEU A O     1 
ATOM   131  C  CB    . LEU A 1 19  ? 16.487 12.614  -10.928 1.00 17.99 ? 19  LEU A CB    1 
ATOM   132  C  CG    . LEU A 1 19  ? 15.989 12.209  -9.540  1.00 20.68 ? 19  LEU A CG    1 
ATOM   133  C  CD1   . LEU A 1 19  ? 16.139 10.698  -9.363  1.00 21.71 ? 19  LEU A CD1   1 
ATOM   134  C  CD2   . LEU A 1 19  ? 16.713 12.986  -8.413  1.00 22.70 ? 19  LEU A CD2   1 
ATOM   135  N  N     . THR A 1 20  ? 16.792 13.977  -13.687 1.00 18.07 ? 20  THR A N     1 
ATOM   136  C  CA    . THR A 1 20  ? 17.640 14.278  -14.840 1.00 19.78 ? 20  THR A CA    1 
ATOM   137  C  C     . THR A 1 20  ? 17.660 15.774  -15.139 1.00 23.93 ? 20  THR A C     1 
ATOM   138  O  O     . THR A 1 20  ? 18.730 16.373  -15.319 1.00 21.99 ? 20  THR A O     1 
ATOM   139  C  CB    . THR A 1 20  ? 17.164 13.492  -16.060 1.00 21.81 ? 20  THR A CB    1 
ATOM   140  O  OG1   . THR A 1 20  ? 17.319 12.097  -15.796 1.00 19.03 ? 20  THR A OG1   1 
ATOM   141  C  CG2   . THR A 1 20  ? 18.027 13.849  -17.286 1.00 23.04 ? 20  THR A CG2   1 
ATOM   142  N  N     . ILE A 1 21  ? 16.484 16.396  -15.186 1.00 19.44 ? 21  ILE A N     1 
ATOM   143  C  CA    . ILE A 1 21  ? 16.412 17.822  -15.497 1.00 22.04 ? 21  ILE A CA    1 
ATOM   144  C  C     . ILE A 1 21  ? 17.045 18.657  -14.397 1.00 24.51 ? 21  ILE A C     1 
ATOM   145  O  O     . ILE A 1 21  ? 17.613 19.719  -14.673 1.00 24.16 ? 21  ILE A O     1 
ATOM   146  C  CB    . ILE A 1 21  ? 14.953 18.251  -15.725 1.00 22.39 ? 21  ILE A CB    1 
ATOM   147  C  CG1   . ILE A 1 21  ? 14.333 17.445  -16.861 1.00 23.69 ? 21  ILE A CG1   1 
ATOM   148  C  CG2   . ILE A 1 21  ? 14.883 19.763  -15.996 1.00 26.36 ? 21  ILE A CG2   1 
ATOM   149  C  CD1   . ILE A 1 21  ? 14.993 17.650  -18.167 1.00 30.74 ? 21  ILE A CD1   1 
ATOM   150  N  N     . GLN A 1 22  ? 16.920 18.241  -13.133 1.00 22.73 ? 22  GLN A N     1 
ATOM   151  C  CA    . GLN A 1 22  ? 17.615 18.968  -12.077 1.00 25.43 ? 22  GLN A CA    1 
ATOM   152  C  C     . GLN A 1 22  ? 19.112 18.957  -12.320 1.00 29.22 ? 22  GLN A C     1 
ATOM   153  O  O     . GLN A 1 22  ? 19.785 19.980  -12.141 1.00 27.80 ? 22  GLN A O     1 
ATOM   154  C  CB    . GLN A 1 22  ? 17.314 18.363  -10.708 1.00 24.06 ? 22  GLN A CB    1 
ATOM   155  C  CG    . GLN A 1 22  ? 16.171 19.012  -9.937  1.00 30.35 ? 22  GLN A CG    1 
ATOM   156  C  CD    . GLN A 1 22  ? 16.510 20.383  -9.336  1.00 29.73 ? 22  GLN A CD    1 
ATOM   157  O  OE1   . GLN A 1 22  ? 17.511 21.008  -9.681  1.00 29.01 ? 22  GLN A OE1   1 
ATOM   158  N  NE2   . GLN A 1 22  ? 15.665 20.842  -8.422  1.00 28.89 ? 22  GLN A NE2   1 
ATOM   159  N  N     . LEU A 1 23  ? 19.661 17.802  -12.715 1.00 23.07 ? 23  LEU A N     1 
ATOM   160  C  CA    . LEU A 1 23  ? 21.096 17.766  -13.000 1.00 23.87 ? 23  LEU A CA    1 
ATOM   161  C  C     . LEU A 1 23  ? 21.453 18.640  -14.206 1.00 31.08 ? 23  LEU A C     1 
ATOM   162  O  O     . LEU A 1 23  ? 22.445 19.378  -14.174 1.00 30.80 ? 23  LEU A O     1 
ATOM   163  C  CB    . LEU A 1 23  ? 21.560 16.322  -13.214 1.00 23.57 ? 23  LEU A CB    1 
ATOM   164  C  CG    . LEU A 1 23  ? 23.078 16.159  -13.342 1.00 29.52 ? 23  LEU A CG    1 
ATOM   165  C  CD1   . LEU A 1 23  ? 23.764 16.246  -11.991 1.00 28.26 ? 23  LEU A CD1   1 
ATOM   166  C  CD2   . LEU A 1 23  ? 23.424 14.867  -14.035 1.00 30.91 ? 23  LEU A CD2   1 
ATOM   167  N  N     . ILE A 1 24  ? 20.653 18.581  -15.271 1.00 27.44 ? 24  ILE A N     1 
ATOM   168  C  CA    . ILE A 1 24  ? 21.008 19.239  -16.530 1.00 29.66 ? 24  ILE A CA    1 
ATOM   169  C  C     . ILE A 1 24  ? 20.808 20.748  -16.441 1.00 35.87 ? 24  ILE A C     1 
ATOM   170  O  O     . ILE A 1 24  ? 21.661 21.531  -16.875 1.00 36.39 ? 24  ILE A O     1 
ATOM   171  C  CB    . ILE A 1 24  ? 20.183 18.656  -17.696 1.00 33.64 ? 24  ILE A CB    1 
ATOM   172  C  CG1   . ILE A 1 24  ? 20.460 17.164  -17.886 1.00 32.73 ? 24  ILE A CG1   1 
ATOM   173  C  CG2   . ILE A 1 24  ? 20.475 19.411  -18.986 1.00 36.35 ? 24  ILE A CG2   1 
ATOM   174  C  CD1   . ILE A 1 24  ? 21.888 16.847  -18.200 1.00 31.84 ? 24  ILE A CD1   1 
ATOM   175  N  N     . GLN A 1 25  ? 19.646 21.173  -15.947 1.00 25.41 ? 25  GLN A N     1 
ATOM   176  C  CA    . GLN A 1 25  ? 19.190 22.556  -16.039 1.00 35.85 ? 25  GLN A CA    1 
ATOM   177  C  C     . GLN A 1 25  ? 19.080 23.257  -14.691 1.00 34.77 ? 25  GLN A C     1 
ATOM   178  O  O     . GLN A 1 25  ? 18.756 24.452  -14.656 1.00 37.22 ? 25  GLN A O     1 
ATOM   179  C  CB    . GLN A 1 25  ? 17.828 22.608  -16.746 1.00 34.37 ? 25  GLN A CB    1 
ATOM   180  C  CG    . GLN A 1 25  ? 17.850 21.977  -18.130 1.00 42.26 ? 25  GLN A CG    1 
ATOM   181  C  CD    . GLN A 1 25  ? 16.517 22.065  -18.861 1.00 45.89 ? 25  GLN A CD    1 
ATOM   182  O  OE1   . GLN A 1 25  ? 15.558 22.668  -18.376 1.00 51.03 ? 25  GLN A OE1   1 
ATOM   183  N  NE2   . GLN A 1 25  ? 16.443 21.421  -20.021 1.00 50.68 ? 25  GLN A NE2   1 
ATOM   184  N  N     . ASN A 1 26  ? 19.286 22.536  -13.589 1.00 31.86 ? 26  ASN A N     1 
ATOM   185  C  CA    . ASN A 1 26  ? 19.377 23.097  -12.243 1.00 35.66 ? 26  ASN A CA    1 
ATOM   186  C  C     . ASN A 1 26  ? 18.059 23.671  -11.746 1.00 38.06 ? 26  ASN A C     1 
ATOM   187  O  O     . ASN A 1 26  ? 18.046 24.639  -10.979 1.00 40.92 ? 26  ASN A O     1 
ATOM   188  C  CB    . ASN A 1 26  ? 20.481 24.151  -12.140 1.00 38.47 ? 26  ASN A CB    1 
ATOM   189  C  CG    . ASN A 1 26  ? 21.804 23.541  -11.801 1.00 42.68 ? 26  ASN A CG    1 
ATOM   190  O  OD1   . ASN A 1 26  ? 22.524 23.083  -12.688 1.00 48.23 ? 26  ASN A OD1   1 
ATOM   191  N  ND2   . ASN A 1 26  ? 22.129 23.494  -10.510 1.00 49.22 ? 26  ASN A ND2   1 
ATOM   192  N  N     . HIS A 1 27  ? 16.938 23.088  -12.154 1.00 35.55 ? 27  HIS A N     1 
ATOM   193  C  CA    . HIS A 1 27  ? 15.666 23.512  -11.595 1.00 34.69 ? 27  HIS A CA    1 
ATOM   194  C  C     . HIS A 1 27  ? 14.694 22.344  -11.648 1.00 31.19 ? 27  HIS A C     1 
ATOM   195  O  O     . HIS A 1 27  ? 14.911 21.365  -12.370 1.00 29.64 ? 27  HIS A O     1 
ATOM   196  C  CB    . HIS A 1 27  ? 15.128 24.764  -12.305 1.00 38.07 ? 27  HIS A CB    1 
ATOM   197  C  CG    . HIS A 1 27  ? 14.496 24.496  -13.632 1.00 37.89 ? 27  HIS A CG    1 
ATOM   198  N  ND1   . HIS A 1 27  ? 15.235 24.372  -14.790 1.00 46.43 ? 27  HIS A ND1   1 
ATOM   199  C  CD2   . HIS A 1 27  ? 13.198 24.384  -13.999 1.00 45.65 ? 27  HIS A CD2   1 
ATOM   200  C  CE1   . HIS A 1 27  ? 14.423 24.156  -15.810 1.00 42.98 ? 27  HIS A CE1   1 
ATOM   201  N  NE2   . HIS A 1 27  ? 13.181 24.165  -15.359 1.00 45.06 ? 27  HIS A NE2   1 
ATOM   202  N  N     . PHE A 1 28  ? 13.685 22.420  -10.787 1.00 29.67 ? 28  PHE A N     1 
ATOM   203  C  CA    . PHE A 1 28  ? 12.674 21.378  -10.667 1.00 28.29 ? 28  PHE A CA    1 
ATOM   204  C  C     . PHE A 1 28  ? 11.565 21.634  -11.682 1.00 31.87 ? 28  PHE A C     1 
ATOM   205  O  O     . PHE A 1 28  ? 10.905 22.678  -11.641 1.00 31.67 ? 28  PHE A O     1 
ATOM   206  C  CB    . PHE A 1 28  ? 12.129 21.359  -9.242  1.00 28.68 ? 28  PHE A CB    1 
ATOM   207  C  CG    . PHE A 1 28  ? 11.006 20.382  -9.017  1.00 27.20 ? 28  PHE A CG    1 
ATOM   208  C  CD1   . PHE A 1 28  ? 11.178 19.023  -9.247  1.00 28.22 ? 28  PHE A CD1   1 
ATOM   209  C  CD2   . PHE A 1 28  ? 9.787  20.822  -8.537  1.00 28.22 ? 28  PHE A CD2   1 
ATOM   210  C  CE1   . PHE A 1 28  ? 10.134 18.131  -9.019  1.00 26.74 ? 28  PHE A CE1   1 
ATOM   211  C  CE2   . PHE A 1 28  ? 8.747  19.940  -8.307  1.00 31.39 ? 28  PHE A CE2   1 
ATOM   212  C  CZ    . PHE A 1 28  ? 8.923  18.591  -8.546  1.00 30.50 ? 28  PHE A CZ    1 
ATOM   213  N  N     . VAL A 1 29  ? 11.391 20.709  -12.620 1.00 32.87 ? 29  VAL A N     1 
ATOM   214  C  CA    . VAL A 1 29  ? 10.272 20.738  -13.556 1.00 28.38 ? 29  VAL A CA    1 
ATOM   215  C  C     . VAL A 1 29  ? 9.225  19.758  -13.051 1.00 33.28 ? 29  VAL A C     1 
ATOM   216  O  O     . VAL A 1 29  ? 9.475  18.545  -12.992 1.00 31.63 ? 29  VAL A O     1 
ATOM   217  C  CB    . VAL A 1 29  ? 10.724 20.393  -14.979 1.00 29.74 ? 29  VAL A CB    1 
ATOM   218  C  CG1   . VAL A 1 29  ? 9.519  20.221  -15.901 1.00 33.10 ? 29  VAL A CG1   1 
ATOM   219  C  CG2   . VAL A 1 29  ? 11.621 21.492  -15.506 1.00 32.91 ? 29  VAL A CG2   1 
ATOM   220  N  N     . ASP A 1 30  ? 8.051  20.275  -12.693 1.00 29.04 ? 30  ASP A N     1 
ATOM   221  C  CA    . ASP A 1 30  ? 7.092  19.497  -11.923 1.00 30.89 ? 30  ASP A CA    1 
ATOM   222  C  C     . ASP A 1 30  ? 6.541  18.325  -12.729 1.00 35.38 ? 30  ASP A C     1 
ATOM   223  O  O     . ASP A 1 30  ? 6.783  17.169  -12.380 1.00 46.12 ? 30  ASP A O     1 
ATOM   224  C  CB    . ASP A 1 30  ? 5.969  20.418  -11.421 1.00 31.12 ? 30  ASP A CB    1 
ATOM   225  C  CG    . ASP A 1 30  ? 4.829  19.675  -10.730 1.00 33.86 ? 30  ASP A CG    1 
ATOM   226  O  OD1   . ASP A 1 30  ? 4.879  18.445  -10.516 1.00 31.22 ? 30  ASP A OD1   1 
ATOM   227  O  OD2   . ASP A 1 30  ? 3.839  20.356  -10.407 1.00 41.07 ? 30  ASP A OD2   1 
ATOM   228  N  N     . GLU A 1 31  ? 5.817  18.576  -13.798 1.00 35.23 ? 31  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 31  ? 5.068  17.508  -14.467 1.00 27.29 ? 31  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 31  ? 5.606  17.295  -15.879 1.00 24.32 ? 31  GLU A C     1 
ATOM   231  O  O     . GLU A 1 31  ? 4.896  17.496  -16.857 1.00 26.26 ? 31  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 31  ? 3.588  17.887  -14.486 1.00 21.77 ? 31  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 31  ? 2.752  17.327  -13.327 1.00 26.83 ? 31  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 31  ? 2.421  15.853  -13.498 1.00 24.27 ? 31  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 31  ? 1.867  15.509  -14.569 1.00 25.22 ? 31  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 31  ? 2.623  15.060  -12.551 1.00 24.94 ? 31  GLU A OE2   1 
ATOM   237  N  N     . TYR A 1 32  ? 6.823  16.787  -15.986 1.00 24.46 ? 32  TYR A N     1 
ATOM   238  C  CA    . TYR A 1 32  ? 7.429  16.581  -17.292 1.00 24.72 ? 32  TYR A CA    1 
ATOM   239  C  C     . TYR A 1 32  ? 6.758  15.394  -17.969 1.00 24.00 ? 32  TYR A C     1 
ATOM   240  O  O     . TYR A 1 32  ? 6.508  14.373  -17.327 1.00 22.05 ? 32  TYR A O     1 
ATOM   241  C  CB    . TYR A 1 32  ? 8.922  16.309  -17.121 1.00 25.81 ? 32  TYR A CB    1 
ATOM   242  C  CG    . TYR A 1 32  ? 9.718  16.298  -18.397 1.00 23.88 ? 32  TYR A CG    1 
ATOM   243  C  CD1   . TYR A 1 32  ? 10.158 17.489  -18.952 1.00 31.27 ? 32  TYR A CD1   1 
ATOM   244  C  CD2   . TYR A 1 32  ? 10.049 15.109  -19.039 1.00 24.20 ? 32  TYR A CD2   1 
ATOM   245  C  CE1   . TYR A 1 32  ? 10.894 17.513  -20.116 1.00 32.95 ? 32  TYR A CE1   1 
ATOM   246  C  CE2   . TYR A 1 32  ? 10.808 15.118  -20.226 1.00 27.98 ? 32  TYR A CE2   1 
ATOM   247  C  CZ    . TYR A 1 32  ? 11.222 16.337  -20.752 1.00 36.98 ? 32  TYR A CZ    1 
ATOM   248  O  OH    . TYR A 1 32  ? 11.964 16.407  -21.913 1.00 35.93 ? 32  TYR A OH    1 
ATOM   249  N  N     . ASP A 1 33  ? 6.447  15.544  -19.276 1.00 20.20 ? 33  ASP A N     1 
ATOM   250  C  CA    . ASP A 1 33  ? 5.736  14.540  -20.082 1.00 22.43 ? 33  ASP A CA    1 
ATOM   251  C  C     . ASP A 1 33  ? 6.151  13.122  -19.686 1.00 20.86 ? 33  ASP A C     1 
ATOM   252  O  O     . ASP A 1 33  ? 7.310  12.734  -19.872 1.00 22.30 ? 33  ASP A O     1 
ATOM   253  C  CB    . ASP A 1 33  ? 5.984  14.796  -21.572 1.00 23.02 ? 33  ASP A CB    1 
ATOM   254  C  CG    . ASP A 1 33  ? 5.153  13.890  -22.478 1.00 26.29 ? 33  ASP A CG    1 
ATOM   255  O  OD1   . ASP A 1 33  ? 4.957  12.704  -22.158 1.00 22.33 ? 33  ASP A OD1   1 
ATOM   256  O  OD2   . ASP A 1 33  ? 4.658  14.387  -23.519 1.00 28.68 ? 33  ASP A OD2   1 
ATOM   257  N  N     . PRO A 1 34  ? 5.234  12.335  -19.108 1.00 19.74 ? 34  PRO A N     1 
ATOM   258  C  CA    . PRO A 1 34  ? 5.607  10.999  -18.606 1.00 18.30 ? 34  PRO A CA    1 
ATOM   259  C  C     . PRO A 1 34  ? 6.021  10.010  -19.673 1.00 19.90 ? 34  PRO A C     1 
ATOM   260  O  O     . PRO A 1 34  ? 6.648  8.990   -19.327 1.00 18.50 ? 34  PRO A O     1 
ATOM   261  C  CB    . PRO A 1 34  ? 4.336  10.533  -17.858 1.00 23.38 ? 34  PRO A CB    1 
ATOM   262  C  CG    . PRO A 1 34  ? 3.302  11.574  -18.110 1.00 25.79 ? 34  PRO A CG    1 
ATOM   263  C  CD    . PRO A 1 34  ? 3.970  12.815  -18.517 1.00 21.15 ? 34  PRO A CD    1 
ATOM   264  N  N     . THR A 1 35  ? 5.734  10.280  -20.954 1.00 19.48 ? 35  THR A N     1 
ATOM   265  C  CA    . THR A 1 35  ? 6.000  9.332   -22.027 1.00 17.17 ? 35  THR A CA    1 
ATOM   266  C  C     . THR A 1 35  ? 7.291  9.600   -22.796 1.00 20.26 ? 35  THR A C     1 
ATOM   267  O  O     . THR A 1 35  ? 7.666  8.770   -23.634 1.00 24.66 ? 35  THR A O     1 
ATOM   268  C  CB    . THR A 1 35  ? 4.840  9.317   -23.037 1.00 21.46 ? 35  THR A CB    1 
ATOM   269  O  OG1   . THR A 1 35  ? 4.808  10.563  -23.753 1.00 23.72 ? 35  THR A OG1   1 
ATOM   270  C  CG2   . THR A 1 35  ? 3.515  9.093   -22.318 1.00 22.45 ? 35  THR A CG2   1 
ATOM   271  N  N     . ILE A 1 36  ? 7.974  10.719  -22.569 1.00 18.93 ? 36  ILE A N     1 
ATOM   272  C  CA    . ILE A 1 36  ? 9.133  11.061  -23.394 1.00 19.25 ? 36  ILE A CA    1 
ATOM   273  C  C     . ILE A 1 36  ? 10.370 10.331  -22.879 1.00 18.57 ? 36  ILE A C     1 
ATOM   274  O  O     . ILE A 1 36  ? 10.783 10.521  -21.729 1.00 20.14 ? 36  ILE A O     1 
ATOM   275  C  CB    . ILE A 1 36  ? 9.378  12.580  -23.427 1.00 24.71 ? 36  ILE A CB    1 
ATOM   276  C  CG1   . ILE A 1 36  ? 8.179  13.312  -24.036 1.00 26.18 ? 36  ILE A CG1   1 
ATOM   277  C  CG2   . ILE A 1 36  ? 10.674 12.886  -24.202 1.00 26.43 ? 36  ILE A CG2   1 
ATOM   278  C  CD1   . ILE A 1 36  ? 7.649  12.645  -25.306 1.00 32.96 ? 36  ILE A CD1   1 
ATOM   279  N  N     . GLU A 1 37  ? 10.973 9.520   -23.742 1.00 17.87 ? 37  GLU A N     1 
ATOM   280  C  CA    . GLU A 1 37  ? 12.266 8.896   -23.487 1.00 16.07 ? 37  GLU A CA    1 
ATOM   281  C  C     . GLU A 1 37  ? 13.286 9.631   -24.336 1.00 21.08 ? 37  GLU A C     1 
ATOM   282  O  O     . GLU A 1 37  ? 13.109 9.731   -25.551 1.00 20.71 ? 37  GLU A O     1 
ATOM   283  C  CB    . GLU A 1 37  ? 12.246 7.418   -23.860 1.00 17.37 ? 37  GLU A CB    1 
ATOM   284  C  CG    . GLU A 1 37  ? 13.593 6.734   -23.729 1.00 19.26 ? 37  GLU A CG    1 
ATOM   285  C  CD    . GLU A 1 37  ? 13.459 5.220   -23.762 1.00 23.04 ? 37  GLU A CD    1 
ATOM   286  O  OE1   . GLU A 1 37  ? 13.150 4.617   -22.713 1.00 18.69 ? 37  GLU A OE1   1 
ATOM   287  O  OE2   . GLU A 1 37  ? 13.662 4.641   -24.845 1.00 27.91 ? 37  GLU A OE2   1 
ATOM   288  N  N     . ASP A 1 38  ? 14.341 10.148  -23.714 1.00 19.81 ? 38  ASP A N     1 
ATOM   289  C  CA    . ASP A 1 38  ? 15.288 10.944  -24.498 1.00 20.15 ? 38  ASP A CA    1 
ATOM   290  C  C     . ASP A 1 38  ? 16.604 10.992  -23.745 1.00 23.02 ? 38  ASP A C     1 
ATOM   291  O  O     . ASP A 1 38  ? 16.680 10.633  -22.567 1.00 19.20 ? 38  ASP A O     1 
ATOM   292  C  CB    . ASP A 1 38  ? 14.756 12.366  -24.763 1.00 21.14 ? 38  ASP A CB    1 
ATOM   293  C  CG    . ASP A 1 38  ? 15.386 13.041  -26.002 1.00 28.31 ? 38  ASP A CG    1 
ATOM   294  O  OD1   . ASP A 1 38  ? 16.265 12.455  -26.678 1.00 24.97 ? 38  ASP A OD1   1 
ATOM   295  O  OD2   . ASP A 1 38  ? 14.990 14.191  -26.278 1.00 32.97 ? 38  ASP A OD2   1 
ATOM   296  N  N     . SER A 1 39  ? 17.638 11.474  -24.426 1.00 20.30 ? 39  SER A N     1 
ATOM   297  C  CA    . SER A 1 39  ? 18.953 11.588  -23.814 1.00 19.87 ? 39  SER A CA    1 
ATOM   298  C  C     . SER A 1 39  ? 19.376 13.049  -23.761 1.00 24.19 ? 39  SER A C     1 
ATOM   299  O  O     . SER A 1 39  ? 19.044 13.838  -24.649 1.00 25.29 ? 39  SER A O     1 
ATOM   300  C  CB    . SER A 1 39  ? 19.982 10.738  -24.575 1.00 25.61 ? 39  SER A CB    1 
ATOM   301  O  OG    . SER A 1 39  ? 20.148 11.239  -25.885 1.00 37.87 ? 39  SER A OG    1 
ATOM   302  N  N     . TYR A 1 40  ? 20.082 13.397  -22.685 1.00 20.01 ? 40  TYR A N     1 
ATOM   303  C  CA    . TYR A 1 40  ? 20.453 14.766  -22.337 1.00 22.98 ? 40  TYR A CA    1 
ATOM   304  C  C     . TYR A 1 40  ? 21.934 14.775  -22.007 1.00 25.54 ? 40  TYR A C     1 
ATOM   305  O  O     . TYR A 1 40  ? 22.442 13.822  -21.414 1.00 25.04 ? 40  TYR A O     1 
ATOM   306  C  CB    . TYR A 1 40  ? 19.649 15.283  -21.135 1.00 25.07 ? 40  TYR A CB    1 
ATOM   307  C  CG    . TYR A 1 40  ? 18.150 15.103  -21.314 1.00 25.14 ? 40  TYR A CG    1 
ATOM   308  C  CD1   . TYR A 1 40  ? 17.543 13.892  -21.023 1.00 23.08 ? 40  TYR A CD1   1 
ATOM   309  C  CD2   . TYR A 1 40  ? 17.361 16.129  -21.814 1.00 27.72 ? 40  TYR A CD2   1 
ATOM   310  C  CE1   . TYR A 1 40  ? 16.188 13.699  -21.223 1.00 24.66 ? 40  TYR A CE1   1 
ATOM   311  C  CE2   . TYR A 1 40  ? 15.995 15.952  -22.011 1.00 31.30 ? 40  TYR A CE2   1 
ATOM   312  C  CZ    . TYR A 1 40  ? 15.414 14.733  -21.710 1.00 27.88 ? 40  TYR A CZ    1 
ATOM   313  O  OH    . TYR A 1 40  ? 14.053 14.541  -21.900 1.00 29.05 ? 40  TYR A OH    1 
ATOM   314  N  N     . ARG A 1 41  ? 22.627 15.841  -22.380 1.00 24.78 ? 41  ARG A N     1 
ATOM   315  C  CA    . ARG A 1 41  ? 24.083 15.900  -22.255 1.00 24.60 ? 41  ARG A CA    1 
ATOM   316  C  C     . ARG A 1 41  ? 24.487 17.034  -21.325 1.00 29.77 ? 41  ARG A C     1 
ATOM   317  O  O     . ARG A 1 41  ? 23.867 18.100  -21.327 1.00 25.79 ? 41  ARG A O     1 
ATOM   318  C  CB    . ARG A 1 41  ? 24.747 16.082  -23.622 1.00 30.61 ? 41  ARG A CB    1 
ATOM   319  C  CG    . ARG A 1 41  ? 24.811 14.819  -24.465 1.00 35.35 ? 41  ARG A CG    1 
ATOM   320  C  CD    . ARG A 1 41  ? 25.297 15.136  -25.865 1.00 42.80 ? 41  ARG A CD    1 
ATOM   321  N  NE    . ARG A 1 41  ? 25.693 13.921  -26.564 1.00 52.39 ? 41  ARG A NE    1 
ATOM   322  C  CZ    . ARG A 1 41  ? 26.933 13.677  -26.965 1.00 52.32 ? 41  ARG A CZ    1 
ATOM   323  N  NH1   . ARG A 1 41  ? 27.904 14.562  -26.782 1.00 50.75 ? 41  ARG A NH1   1 
ATOM   324  N  NH2   . ARG A 1 41  ? 27.210 12.512  -27.546 1.00 55.74 ? 41  ARG A NH2   1 
ATOM   325  N  N     . LYS A 1 42  ? 25.501 16.790  -20.496 1.00 25.21 ? 42  LYS A N     1 
ATOM   326  C  CA    . LYS A 1 42  ? 26.021 17.839  -19.623 1.00 27.46 ? 42  LYS A CA    1 
ATOM   327  C  C     . LYS A 1 42  ? 27.533 17.696  -19.524 1.00 27.92 ? 42  LYS A C     1 
ATOM   328  O  O     . LYS A 1 42  ? 28.035 16.590  -19.316 1.00 24.57 ? 42  LYS A O     1 
ATOM   329  C  CB    . LYS A 1 42  ? 25.377 17.761  -18.235 1.00 28.91 ? 42  LYS A CB    1 
ATOM   330  C  CG    . LYS A 1 42  ? 25.974 18.695  -17.174 1.00 33.25 ? 42  LYS A CG    1 
ATOM   331  C  CD    . LYS A 1 42  ? 25.133 19.966  -17.030 1.00 34.91 ? 42  LYS A CD    1 
ATOM   332  C  CE    . LYS A 1 42  ? 25.386 20.700  -15.717 1.00 41.46 ? 42  LYS A CE    1 
ATOM   333  N  NZ    . LYS A 1 42  ? 25.459 19.758  -14.567 1.00 42.58 ? 42  LYS A NZ    1 
ATOM   334  N  N     . GLN A 1 43  ? 28.264 18.802  -19.653 1.00 27.95 ? 43  GLN A N     1 
ATOM   335  C  CA    . GLN A 1 43  ? 29.704 18.791  -19.420 1.00 24.57 ? 43  GLN A CA    1 
ATOM   336  C  C     . GLN A 1 43  ? 29.991 19.272  -17.998 1.00 26.09 ? 43  GLN A C     1 
ATOM   337  O  O     . GLN A 1 43  ? 29.506 20.329  -17.584 1.00 27.77 ? 43  GLN A O     1 
ATOM   338  C  CB    . GLN A 1 43  ? 30.427 19.671  -20.435 1.00 30.17 ? 43  GLN A CB    1 
ATOM   339  C  CG    . GLN A 1 43  ? 31.937 19.630  -20.281 1.00 37.01 ? 43  GLN A CG    1 
ATOM   340  C  CD    . GLN A 1 43  ? 32.645 20.516  -21.287 1.00 43.55 ? 43  GLN A CD    1 
ATOM   341  O  OE1   . GLN A 1 43  ? 32.431 20.407  -22.498 1.00 43.85 ? 43  GLN A OE1   1 
ATOM   342  N  NE2   . GLN A 1 43  ? 33.483 21.416  -20.782 1.00 36.87 ? 43  GLN A NE2   1 
ATOM   343  N  N     . VAL A 1 44  ? 30.767 18.490  -17.246 1.00 22.36 ? 44  VAL A N     1 
ATOM   344  C  CA    . VAL A 1 44  ? 31.060 18.813  -15.856 1.00 23.52 ? 44  VAL A CA    1 
ATOM   345  C  C     . VAL A 1 44  ? 32.462 18.320  -15.537 1.00 25.53 ? 44  VAL A C     1 
ATOM   346  O  O     . VAL A 1 44  ? 32.947 17.353  -16.125 1.00 26.76 ? 44  VAL A O     1 
ATOM   347  C  CB    . VAL A 1 44  ? 30.015 18.179  -14.910 1.00 28.13 ? 44  VAL A CB    1 
ATOM   348  C  CG1   . VAL A 1 44  ? 29.991 16.665  -15.094 1.00 29.24 ? 44  VAL A CG1   1 
ATOM   349  C  CG2   . VAL A 1 44  ? 30.265 18.575  -13.457 1.00 33.00 ? 44  VAL A CG2   1 
ATOM   350  N  N     . VAL A 1 45  ? 33.125 18.999  -14.609 1.00 22.51 ? 45  VAL A N     1 
ATOM   351  C  CA    . VAL A 1 45  ? 34.429 18.563  -14.127 1.00 20.60 ? 45  VAL A CA    1 
ATOM   352  C  C     . VAL A 1 45  ? 34.197 17.788  -12.839 1.00 24.66 ? 45  VAL A C     1 
ATOM   353  O  O     . VAL A 1 45  ? 33.633 18.327  -11.880 1.00 25.86 ? 45  VAL A O     1 
ATOM   354  C  CB    . VAL A 1 45  ? 35.378 19.749  -13.899 1.00 21.78 ? 45  VAL A CB    1 
ATOM   355  C  CG1   . VAL A 1 45  ? 36.726 19.248  -13.395 1.00 24.44 ? 45  VAL A CG1   1 
ATOM   356  C  CG2   . VAL A 1 45  ? 35.529 20.562  -15.179 1.00 24.11 ? 45  VAL A CG2   1 
ATOM   357  N  N     . ILE A 1 46  ? 34.611 16.520  -12.809 1.00 21.53 ? 46  ILE A N     1 
ATOM   358  C  CA    . ILE A 1 46  ? 34.434 15.670  -11.632 1.00 23.66 ? 46  ILE A CA    1 
ATOM   359  C  C     . ILE A 1 46  ? 35.806 15.152  -11.206 1.00 25.21 ? 46  ILE A C     1 
ATOM   360  O  O     . ILE A 1 46  ? 36.491 14.479  -11.992 1.00 23.73 ? 46  ILE A O     1 
ATOM   361  C  CB    . ILE A 1 46  ? 33.472 14.502  -11.909 1.00 26.68 ? 46  ILE A CB    1 
ATOM   362  C  CG1   . ILE A 1 46  ? 32.095 15.029  -12.306 1.00 27.01 ? 46  ILE A CG1   1 
ATOM   363  C  CG2   . ILE A 1 46  ? 33.339 13.619  -10.691 1.00 29.06 ? 46  ILE A CG2   1 
ATOM   364  C  CD1   . ILE A 1 46  ? 31.244 13.979  -13.010 1.00 29.92 ? 46  ILE A CD1   1 
ATOM   365  N  N     . ASP A 1 47  ? 36.189 15.439  -9.956  1.00 26.91 ? 47  ASP A N     1 
ATOM   366  C  CA    . ASP A 1 47  ? 37.505 15.068  -9.420  1.00 27.02 ? 47  ASP A CA    1 
ATOM   367  C  C     . ASP A 1 47  ? 38.624 15.443  -10.386 1.00 27.99 ? 47  ASP A C     1 
ATOM   368  O  O     . ASP A 1 47  ? 39.516 14.643  -10.685 1.00 29.05 ? 47  ASP A O     1 
ATOM   369  C  CB    . ASP A 1 47  ? 37.561 13.577  -9.097  1.00 32.07 ? 47  ASP A CB    1 
ATOM   370  C  CG    . ASP A 1 47  ? 36.415 13.137  -8.224  1.00 30.66 ? 47  ASP A CG    1 
ATOM   371  O  OD1   . ASP A 1 47  ? 36.003 13.939  -7.376  1.00 33.19 ? 47  ASP A OD1   1 
ATOM   372  O  OD2   . ASP A 1 47  ? 35.914 12.006  -8.396  1.00 34.82 ? 47  ASP A OD2   1 
ATOM   373  N  N     . GLY A 1 48  ? 38.549 16.660  -10.919 1.00 26.58 ? 48  GLY A N     1 
ATOM   374  C  CA    . GLY A 1 48  ? 39.604 17.146  -11.786 1.00 26.66 ? 48  GLY A CA    1 
ATOM   375  C  C     . GLY A 1 48  ? 39.577 16.657  -13.220 1.00 28.25 ? 48  GLY A C     1 
ATOM   376  O  O     . GLY A 1 48  ? 40.485 17.001  -13.985 1.00 24.41 ? 48  GLY A O     1 
ATOM   377  N  N     . GLU A 1 49  ? 38.592 15.846  -13.618 1.00 25.82 ? 49  GLU A N     1 
ATOM   378  C  CA    . GLU A 1 49  ? 38.547 15.305  -14.969 1.00 21.83 ? 49  GLU A CA    1 
ATOM   379  C  C     . GLU A 1 49  ? 37.354 15.895  -15.708 1.00 24.44 ? 49  GLU A C     1 
ATOM   380  O  O     . GLU A 1 49  ? 36.237 15.881  -15.179 1.00 23.86 ? 49  GLU A O     1 
ATOM   381  C  CB    . GLU A 1 49  ? 38.443 13.778  -14.943 1.00 28.00 ? 49  GLU A CB    1 
ATOM   382  C  CG    . GLU A 1 49  ? 37.899 13.187  -16.240 1.00 31.93 ? 49  GLU A CG    1 
ATOM   383  C  CD    . GLU A 1 49  ? 37.743 11.679  -16.174 1.00 44.31 ? 49  GLU A CD    1 
ATOM   384  O  OE1   . GLU A 1 49  ? 36.631 11.202  -15.845 1.00 43.52 ? 49  GLU A OE1   1 
ATOM   385  O  OE2   . GLU A 1 49  ? 38.753 10.980  -16.416 1.00 46.66 ? 49  GLU A OE2   1 
ATOM   386  N  N     . THR A 1 50  ? 37.596 16.456  -16.898 1.00 23.50 ? 50  THR A N     1 
ATOM   387  C  CA    . THR A 1 50  ? 36.500 16.993  -17.702 1.00 23.33 ? 50  THR A CA    1 
ATOM   388  C  C     . THR A 1 50  ? 35.718 15.858  -18.364 1.00 28.62 ? 50  THR A C     1 
ATOM   389  O  O     . THR A 1 50  ? 36.263 15.081  -19.169 1.00 33.13 ? 50  THR A O     1 
ATOM   390  C  CB    . THR A 1 50  ? 37.019 17.960  -18.756 1.00 30.77 ? 50  THR A CB    1 
ATOM   391  O  OG1   . THR A 1 50  ? 37.819 18.970  -18.119 1.00 27.97 ? 50  THR A OG1   1 
ATOM   392  C  CG2   . THR A 1 50  ? 35.847 18.630  -19.444 1.00 32.14 ? 50  THR A CG2   1 
ATOM   393  N  N     . SER A 1 51  ? 34.421 15.803  -18.065 1.00 25.31 ? 51  SER A N     1 
ATOM   394  C  CA    . SER A 1 51  ? 33.584 14.664  -18.383 1.00 28.01 ? 51  SER A CA    1 
ATOM   395  C  C     . SER A 1 51  ? 32.347 15.151  -19.117 1.00 27.47 ? 51  SER A C     1 
ATOM   396  O  O     . SER A 1 51  ? 31.788 16.210  -18.793 1.00 27.32 ? 51  SER A O     1 
ATOM   397  C  CB    . SER A 1 51  ? 33.168 13.936  -17.097 1.00 29.41 ? 51  SER A CB    1 
ATOM   398  O  OG    . SER A 1 51  ? 34.284 13.759  -16.229 1.00 35.15 ? 51  SER A OG    1 
ATOM   399  N  N     . LEU A 1 52  ? 31.919 14.365  -20.091 1.00 24.20 ? 52  LEU A N     1 
ATOM   400  C  CA    . LEU A 1 52  ? 30.675 14.595  -20.816 1.00 25.65 ? 52  LEU A CA    1 
ATOM   401  C  C     . LEU A 1 52  ? 29.725 13.489  -20.380 1.00 24.99 ? 52  LEU A C     1 
ATOM   402  O  O     . LEU A 1 52  ? 29.980 12.316  -20.651 1.00 30.19 ? 52  LEU A O     1 
ATOM   403  C  CB    . LEU A 1 52  ? 30.912 14.573  -22.327 1.00 32.04 ? 52  LEU A CB    1 
ATOM   404  C  CG    . LEU A 1 52  ? 29.803 15.035  -23.279 1.00 36.20 ? 52  LEU A CG    1 
ATOM   405  C  CD1   . LEU A 1 52  ? 28.824 13.918  -23.607 1.00 40.58 ? 52  LEU A CD1   1 
ATOM   406  C  CD2   . LEU A 1 52  ? 29.062 16.241  -22.702 1.00 34.04 ? 52  LEU A CD2   1 
ATOM   407  N  N     . LEU A 1 53  ? 28.654 13.851  -19.683 1.00 23.91 ? 53  LEU A N     1 
ATOM   408  C  CA    . LEU A 1 53  ? 27.644 12.888  -19.263 1.00 23.72 ? 53  LEU A CA    1 
ATOM   409  C  C     . LEU A 1 53  ? 26.538 12.848  -20.309 1.00 25.50 ? 53  LEU A C     1 
ATOM   410  O  O     . LEU A 1 53  ? 25.982 13.891  -20.667 1.00 25.05 ? 53  LEU A O     1 
ATOM   411  C  CB    . LEU A 1 53  ? 27.079 13.250  -17.897 1.00 22.97 ? 53  LEU A CB    1 
ATOM   412  C  CG    . LEU A 1 53  ? 28.090 13.557  -16.790 1.00 26.29 ? 53  LEU A CG    1 
ATOM   413  C  CD1   . LEU A 1 53  ? 27.375 13.653  -15.456 1.00 28.89 ? 53  LEU A CD1   1 
ATOM   414  C  CD2   . LEU A 1 53  ? 29.184 12.499  -16.758 1.00 24.70 ? 53  LEU A CD2   1 
ATOM   415  N  N     . ASP A 1 54  ? 26.271 11.658  -20.842 1.00 21.73 ? 54  ASP A N     1 
ATOM   416  C  CA    . ASP A 1 54  ? 25.175 11.415  -21.774 1.00 20.93 ? 54  ASP A CA    1 
ATOM   417  C  C     . ASP A 1 54  ? 24.160 10.566  -21.014 1.00 22.35 ? 54  ASP A C     1 
ATOM   418  O  O     . ASP A 1 54  ? 24.433 9.409   -20.700 1.00 22.10 ? 54  ASP A O     1 
ATOM   419  C  CB    . ASP A 1 54  ? 25.708 10.708  -23.022 1.00 25.62 ? 54  ASP A CB    1 
ATOM   420  C  CG    . ASP A 1 54  ? 24.664 10.543  -24.119 1.00 36.59 ? 54  ASP A CG    1 
ATOM   421  O  OD1   . ASP A 1 54  ? 23.450 10.610  -23.846 1.00 36.34 ? 54  ASP A OD1   1 
ATOM   422  O  OD2   . ASP A 1 54  ? 25.069 10.336  -25.278 1.00 41.67 ? 54  ASP A OD2   1 
ATOM   423  N  N     . ILE A 1 55  ? 23.000 11.133  -20.703 1.00 19.80 ? 55  ILE A N     1 
ATOM   424  C  CA    . ILE A 1 55  ? 22.076 10.542  -19.743 1.00 17.24 ? 55  ILE A CA    1 
ATOM   425  C  C     . ILE A 1 55  ? 20.814 10.150  -20.484 1.00 19.20 ? 55  ILE A C     1 
ATOM   426  O  O     . ILE A 1 55  ? 20.118 11.013  -21.025 1.00 17.85 ? 55  ILE A O     1 
ATOM   427  C  CB    . ILE A 1 55  ? 21.738 11.523  -18.618 1.00 19.24 ? 55  ILE A CB    1 
ATOM   428  C  CG1   . ILE A 1 55  ? 23.012 11.952  -17.898 1.00 22.95 ? 55  ILE A CG1   1 
ATOM   429  C  CG2   . ILE A 1 55  ? 20.748 10.868  -17.632 1.00 21.54 ? 55  ILE A CG2   1 
ATOM   430  C  CD1   . ILE A 1 55  ? 22.755 13.035  -16.883 1.00 26.45 ? 55  ILE A CD1   1 
ATOM   431  N  N     . LEU A 1 56  ? 20.505 8.863   -20.488 1.00 19.13 ? 56  LEU A N     1 
ATOM   432  C  CA    . LEU A 1 56  ? 19.279 8.368   -21.099 1.00 16.66 ? 56  LEU A CA    1 
ATOM   433  C  C     . LEU A 1 56  ? 18.194 8.293   -20.029 1.00 15.75 ? 56  LEU A C     1 
ATOM   434  O  O     . LEU A 1 56  ? 18.316 7.524   -19.074 1.00 15.20 ? 56  LEU A O     1 
ATOM   435  C  CB    . LEU A 1 56  ? 19.532 7.002   -21.723 1.00 15.65 ? 56  LEU A CB    1 
ATOM   436  C  CG    . LEU A 1 56  ? 18.320 6.253   -22.291 1.00 22.65 ? 56  LEU A CG    1 
ATOM   437  C  CD1   . LEU A 1 56  ? 17.552 7.109   -23.255 1.00 23.04 ? 56  LEU A CD1   1 
ATOM   438  C  CD2   . LEU A 1 56  ? 18.803 4.993   -22.974 1.00 26.53 ? 56  LEU A CD2   1 
ATOM   439  N  N     . ASP A 1 57  ? 17.137 9.085   -20.200 1.00 16.08 ? 57  ASP A N     1 
ATOM   440  C  CA    . ASP A 1 57  ? 15.998 9.132   -19.295 1.00 16.01 ? 57  ASP A CA    1 
ATOM   441  C  C     . ASP A 1 57  ? 14.900 8.253   -19.900 1.00 19.84 ? 57  ASP A C     1 
ATOM   442  O  O     . ASP A 1 57  ? 14.321 8.620   -20.936 1.00 17.12 ? 57  ASP A O     1 
ATOM   443  C  CB    . ASP A 1 57  ? 15.545 10.583  -19.153 1.00 18.79 ? 57  ASP A CB    1 
ATOM   444  C  CG    . ASP A 1 57  ? 14.292 10.734  -18.344 1.00 19.86 ? 57  ASP A CG    1 
ATOM   445  O  OD1   . ASP A 1 57  ? 14.002 9.851   -17.508 1.00 16.14 ? 57  ASP A OD1   1 
ATOM   446  O  OD2   . ASP A 1 57  ? 13.577 11.747  -18.554 1.00 19.20 ? 57  ASP A OD2   1 
ATOM   447  N  N     . THR A 1 58  ? 14.675 7.063   -19.301 1.00 18.58 ? 58  THR A N     1 
ATOM   448  C  CA    . THR A 1 58  ? 13.828 6.043   -19.931 1.00 16.99 ? 58  THR A CA    1 
ATOM   449  C  C     . THR A 1 58  ? 12.346 6.322   -19.681 1.00 20.04 ? 58  THR A C     1 
ATOM   450  O  O     . THR A 1 58  ? 11.962 6.914   -18.666 1.00 17.32 ? 58  THR A O     1 
ATOM   451  C  CB    . THR A 1 58  ? 14.197 4.619   -19.460 1.00 17.53 ? 58  THR A CB    1 
ATOM   452  O  OG1   . THR A 1 58  ? 14.067 4.472   -18.037 1.00 14.28 ? 58  THR A OG1   1 
ATOM   453  C  CG2   . THR A 1 58  ? 15.648 4.258   -19.858 1.00 17.37 ? 58  THR A CG2   1 
ATOM   454  N  N     . ALA A 1 59  ? 11.506 5.873   -20.618 1.00 15.60 ? 59  ALA A N     1 
ATOM   455  C  CA    . ALA A 1 59  ? 10.058 6.038   -20.501 1.00 16.43 ? 59  ALA A CA    1 
ATOM   456  C  C     . ALA A 1 59  ? 9.390  5.108   -21.495 1.00 21.64 ? 59  ALA A C     1 
ATOM   457  O  O     . ALA A 1 59  ? 10.053 4.396   -22.254 1.00 22.60 ? 59  ALA A O     1 
ATOM   458  C  CB    . ALA A 1 59  ? 9.618  7.484   -20.770 1.00 17.96 ? 59  ALA A CB    1 
ATOM   459  N  N     . GLY A 1 60  ? 8.062  5.146   -21.510 1.00 18.70 ? 60  GLY A N     1 
ATOM   460  C  CA    . GLY A 1 60  ? 7.314  4.542   -22.596 1.00 20.33 ? 60  GLY A CA    1 
ATOM   461  C  C     . GLY A 1 60  ? 6.813  3.137   -22.331 1.00 25.11 ? 60  GLY A C     1 
ATOM   462  O  O     . GLY A 1 60  ? 6.624  2.732   -21.180 1.00 22.54 ? 60  GLY A O     1 
ATOM   463  N  N     . GLN A 1 61  ? 6.612  2.387   -23.414 1.00 25.28 ? 61  GLN A N     1 
ATOM   464  C  CA    . GLN A 1 61  ? 5.954  1.087   -23.371 1.00 30.11 ? 61  GLN A CA    1 
ATOM   465  C  C     . GLN A 1 61  ? 6.913  0.008   -22.886 1.00 24.18 ? 61  GLN A C     1 
ATOM   466  O  O     . GLN A 1 61  ? 8.120  0.084   -23.106 1.00 26.53 ? 61  GLN A O     1 
ATOM   467  C  CB    . GLN A 1 61  ? 5.471  0.702   -24.776 1.00 29.56 ? 61  GLN A CB    1 
ATOM   468  C  CG    . GLN A 1 61  ? 4.578  1.708   -25.516 1.00 40.98 ? 61  GLN A CG    1 
ATOM   469  C  CD    . GLN A 1 61  ? 3.121  1.676   -25.103 1.00 51.20 ? 61  GLN A CD    1 
ATOM   470  O  OE1   . GLN A 1 61  ? 2.248  1.326   -25.905 1.00 59.67 ? 61  GLN A OE1   1 
ATOM   471  N  NE2   . GLN A 1 61  ? 2.844  2.055   -23.859 1.00 52.09 ? 61  GLN A NE2   1 
ATOM   472  N  N     . GLU A 1 62  ? 6.365  -1.013  -22.227 1.00 22.10 ? 62  GLU A N     1 
ATOM   473  C  CA    . GLU A 1 62  ? 7.161  -2.166  -21.813 1.00 19.46 ? 62  GLU A CA    1 
ATOM   474  C  C     . GLU A 1 62  ? 7.273  -3.109  -23.000 1.00 24.63 ? 62  GLU A C     1 
ATOM   475  O  O     . GLU A 1 62  ? 6.270  -3.693  -23.423 1.00 23.51 ? 62  GLU A O     1 
ATOM   476  C  CB    . GLU A 1 62  ? 6.532  -2.886  -20.622 1.00 18.77 ? 62  GLU A CB    1 
ATOM   477  C  CG    . GLU A 1 62  ? 7.341  -4.112  -20.212 1.00 19.84 ? 62  GLU A CG    1 
ATOM   478  C  CD    . GLU A 1 62  ? 6.829  -4.729  -18.916 1.00 21.39 ? 62  GLU A CD    1 
ATOM   479  O  OE1   . GLU A 1 62  ? 5.682  -4.428  -18.539 1.00 23.14 ? 62  GLU A OE1   1 
ATOM   480  O  OE2   . GLU A 1 62  ? 7.593  -5.461  -18.280 1.00 20.44 ? 62  GLU A OE2   1 
ATOM   481  N  N     . GLU A 1 63  ? 8.485  -3.258  -23.538 1.00 22.50 ? 63  GLU A N     1 
ATOM   482  C  CA    . GLU A 1 63  ? 8.757  -4.134  -24.672 1.00 23.80 ? 63  GLU A CA    1 
ATOM   483  C  C     . GLU A 1 63  ? 10.199 -4.625  -24.594 1.00 25.90 ? 63  GLU A C     1 
ATOM   484  O  O     . GLU A 1 63  ? 11.078 -3.903  -24.106 1.00 26.31 ? 63  GLU A O     1 
ATOM   485  C  CB    . GLU A 1 63  ? 8.450  -3.383  -25.980 1.00 30.21 ? 63  GLU A CB    1 
ATOM   486  C  CG    . GLU A 1 63  ? 9.127  -2.006  -26.081 1.00 37.45 ? 63  GLU A CG    1 
ATOM   487  C  CD    . GLU A 1 63  ? 10.187 -1.866  -27.168 1.00 46.60 ? 63  GLU A CD    1 
ATOM   488  O  OE1   . GLU A 1 63  ? 10.660 -2.885  -27.728 1.00 47.09 ? 63  GLU A OE1   1 
ATOM   489  O  OE2   . GLU A 1 63  ? 10.536 -0.698  -27.469 1.00 52.57 ? 63  GLU A OE2   1 
ATOM   490  N  N     . TYR A 1 64  ? 10.428 -5.869  -25.036 1.00 21.66 ? 64  TYR A N     1 
ATOM   491  C  CA    . TYR A 1 64  ? 11.731 -6.532  -24.897 1.00 19.51 ? 64  TYR A CA    1 
ATOM   492  C  C     . TYR A 1 64  ? 12.342 -7.017  -26.209 1.00 30.86 ? 64  TYR A C     1 
ATOM   493  O  O     . TYR A 1 64  ? 12.628 -8.211  -26.354 1.00 40.79 ? 64  TYR A O     1 
ATOM   494  C  CB    . TYR A 1 64  ? 11.637 -7.725  -23.930 1.00 23.19 ? 64  TYR A CB    1 
ATOM   495  C  CG    . TYR A 1 64  ? 11.259 -7.247  -22.567 1.00 20.89 ? 64  TYR A CG    1 
ATOM   496  C  CD1   . TYR A 1 64  ? 12.222 -6.710  -21.715 1.00 23.83 ? 64  TYR A CD1   1 
ATOM   497  C  CD2   . TYR A 1 64  ? 9.942  -7.262  -22.154 1.00 20.92 ? 64  TYR A CD2   1 
ATOM   498  C  CE1   . TYR A 1 64  ? 11.884 -6.224  -20.482 1.00 20.84 ? 64  TYR A CE1   1 
ATOM   499  C  CE2   . TYR A 1 64  ? 9.581  -6.783  -20.901 1.00 17.70 ? 64  TYR A CE2   1 
ATOM   500  C  CZ    . TYR A 1 64  ? 10.567 -6.259  -20.071 1.00 23.01 ? 64  TYR A CZ    1 
ATOM   501  O  OH    . TYR A 1 64  ? 10.247 -5.754  -18.839 1.00 21.27 ? 64  TYR A OH    1 
ATOM   502  N  N     . SER A 1 65  ? 12.560 -6.123  -27.156 1.00 27.54 ? 65  SER A N     1 
ATOM   503  C  CA    . SER A 1 65  ? 13.125 -6.481  -28.452 1.00 29.29 ? 65  SER A CA    1 
ATOM   504  C  C     . SER A 1 65  ? 14.658 -6.554  -28.427 1.00 26.59 ? 65  SER A C     1 
ATOM   505  O  O     . SER A 1 65  ? 15.328 -5.995  -27.557 1.00 23.88 ? 65  SER A O     1 
ATOM   506  C  CB    . SER A 1 65  ? 12.684 -5.463  -29.481 1.00 27.59 ? 65  SER A CB    1 
ATOM   507  O  OG    . SER A 1 65  ? 13.087 -4.176  -29.038 1.00 29.03 ? 65  SER A OG    1 
ATOM   508  N  N     . ALA A 1 66  ? 15.226 -7.186  -29.461 1.00 25.65 ? 66  ALA A N     1 
ATOM   509  C  CA    . ALA A 1 66  ? 16.676 -7.097  -29.652 1.00 23.99 ? 66  ALA A CA    1 
ATOM   510  C  C     . ALA A 1 66  ? 17.111 -5.643  -29.825 1.00 20.72 ? 66  ALA A C     1 
ATOM   511  O  O     . ALA A 1 66  ? 18.172 -5.233  -29.338 1.00 22.68 ? 66  ALA A O     1 
ATOM   512  C  CB    . ALA A 1 66  ? 17.104 -7.935  -30.863 1.00 30.06 ? 66  ALA A CB    1 
ATOM   513  N  N     . MET A 1 67  ? 16.282 -4.841  -30.485 1.00 20.95 ? 67  MET A N     1 
ATOM   514  C  CA    . MET A 1 67  ? 16.577 -3.424  -30.679 1.00 23.10 ? 67  MET A CA    1 
ATOM   515  C  C     . MET A 1 67  ? 16.709 -2.694  -29.338 1.00 22.36 ? 67  MET A C     1 
ATOM   516  O  O     . MET A 1 67  ? 17.689 -1.962  -29.094 1.00 20.55 ? 67  MET A O     1 
ATOM   517  C  CB    . MET A 1 67  ? 15.464 -2.823  -31.547 1.00 25.52 ? 67  MET A CB    1 
ATOM   518  C  CG    . MET A 1 67  ? 15.432 -1.337  -31.691 1.00 26.76 ? 67  MET A CG    1 
ATOM   519  S  SD    . MET A 1 67  ? 14.103 -0.881  -32.864 1.00 29.37 ? 67  MET A SD    1 
ATOM   520  C  CE    . MET A 1 67  ? 12.622 -1.266  -31.914 1.00 34.87 ? 67  MET A CE    1 
ATOM   521  N  N     . ARG A 1 68  ? 15.744 -2.908  -28.436 1.00 19.38 ? 68  ARG A N     1 
ATOM   522  C  CA    . ARG A 1 68  ? 15.824 -2.243  -27.139 1.00 21.32 ? 68  ARG A CA    1 
ATOM   523  C  C     . ARG A 1 68  ? 16.939 -2.826  -26.287 1.00 19.58 ? 68  ARG A C     1 
ATOM   524  O  O     . ARG A 1 68  ? 17.588 -2.092  -25.533 1.00 19.99 ? 68  ARG A O     1 
ATOM   525  C  CB    . ARG A 1 68  ? 14.482 -2.319  -26.407 1.00 16.82 ? 68  ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 68  ? 14.428 -1.349  -25.197 1.00 22.04 ? 68  ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 68  ? 12.997 -0.993  -24.800 1.00 25.52 ? 68  ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 68  ? 12.951 -0.114  -23.629 1.00 24.85 ? 68  ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 68  ? 13.122 1.202   -23.663 1.00 24.79 ? 68  ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 68  ? 13.445 1.832   -24.782 1.00 24.40 ? 68  ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 68  ? 12.976 1.906   -22.539 1.00 22.44 ? 68  ARG A NH2   1 
ATOM   532  N  N     . ASP A 1 69  ? 17.180 -4.136  -26.389 1.00 17.28 ? 69  ASP A N     1 
ATOM   533  C  CA    . ASP A 1 69  ? 18.280 -4.729  -25.637 1.00 19.04 ? 69  ASP A CA    1 
ATOM   534  C  C     . ASP A 1 69  ? 19.604 -4.075  -26.012 1.00 23.08 ? 69  ASP A C     1 
ATOM   535  O  O     . ASP A 1 69  ? 20.401 -3.714  -25.142 1.00 22.22 ? 69  ASP A O     1 
ATOM   536  C  CB    . ASP A 1 69  ? 18.360 -6.236  -25.888 1.00 19.87 ? 69  ASP A CB    1 
ATOM   537  C  CG    . ASP A 1 69  ? 17.351 -7.035  -25.108 1.00 23.96 ? 69  ASP A CG    1 
ATOM   538  O  OD1   . ASP A 1 69  ? 16.600 -6.484  -24.259 1.00 21.03 ? 69  ASP A OD1   1 
ATOM   539  O  OD2   . ASP A 1 69  ? 17.332 -8.265  -25.339 1.00 23.50 ? 69  ASP A OD2   1 
ATOM   540  N  N     . GLN A 1 70  ? 19.872 -3.936  -27.309 1.00 20.49 ? 70  GLN A N     1 
ATOM   541  C  CA    . GLN A 1 70  ? 21.126 -3.308  -27.726 1.00 21.72 ? 70  GLN A CA    1 
ATOM   542  C  C     . GLN A 1 70  ? 21.202 -1.853  -27.276 1.00 26.02 ? 70  GLN A C     1 
ATOM   543  O  O     . GLN A 1 70  ? 22.279 -1.358  -26.879 1.00 27.06 ? 70  GLN A O     1 
ATOM   544  C  CB    . GLN A 1 70  ? 21.272 -3.414  -29.239 1.00 25.22 ? 70  GLN A CB    1 
ATOM   545  C  CG    . GLN A 1 70  ? 22.654 -3.062  -29.722 1.00 33.50 ? 70  GLN A CG    1 
ATOM   546  C  CD    . GLN A 1 70  ? 22.731 -3.205  -31.202 1.00 47.34 ? 70  GLN A CD    1 
ATOM   547  O  OE1   . GLN A 1 70  ? 22.503 -4.292  -31.748 1.00 48.62 ? 70  GLN A OE1   1 
ATOM   548  N  NE2   . GLN A 1 70  ? 22.989 -2.094  -31.883 1.00 42.27 ? 70  GLN A NE2   1 
ATOM   549  N  N     . TYR A 1 71  ? 20.065 -1.153  -27.351 1.00 20.88 ? 71  TYR A N     1 
ATOM   550  C  CA    . TYR A 1 71  ? 19.995 0.234   -26.904 1.00 22.74 ? 71  TYR A CA    1 
ATOM   551  C  C     . TYR A 1 71  ? 20.433 0.351   -25.451 1.00 25.80 ? 71  TYR A C     1 
ATOM   552  O  O     . TYR A 1 71  ? 21.287 1.179   -25.108 1.00 23.93 ? 71  TYR A O     1 
ATOM   553  C  CB    . TYR A 1 71  ? 18.560 0.740   -27.085 1.00 23.31 ? 71  TYR A CB    1 
ATOM   554  C  CG    . TYR A 1 71  ? 18.361 2.239   -26.991 1.00 26.13 ? 71  TYR A CG    1 
ATOM   555  C  CD1   . TYR A 1 71  ? 19.211 3.110   -27.654 1.00 28.77 ? 71  TYR A CD1   1 
ATOM   556  C  CD2   . TYR A 1 71  ? 17.280 2.776   -26.296 1.00 29.09 ? 71  TYR A CD2   1 
ATOM   557  C  CE1   . TYR A 1 71  ? 19.020 4.475   -27.596 1.00 29.08 ? 71  TYR A CE1   1 
ATOM   558  C  CE2   . TYR A 1 71  ? 17.070 4.156   -26.243 1.00 27.65 ? 71  TYR A CE2   1 
ATOM   559  C  CZ    . TYR A 1 71  ? 17.956 4.990   -26.899 1.00 30.40 ? 71  TYR A CZ    1 
ATOM   560  O  OH    . TYR A 1 71  ? 17.765 6.350   -26.865 1.00 36.52 ? 71  TYR A OH    1 
ATOM   561  N  N     . MET A 1 72  ? 19.858 -0.488  -24.583 1.00 23.32 ? 72  MET A N     1 
ATOM   562  C  CA    . MET A 1 72  ? 20.200 -0.457  -23.159 1.00 21.19 ? 72  MET A CA    1 
ATOM   563  C  C     . MET A 1 72  ? 21.622 -0.920  -22.897 1.00 22.99 ? 72  MET A C     1 
ATOM   564  O  O     . MET A 1 72  ? 22.265 -0.422  -21.964 1.00 22.00 ? 72  MET A O     1 
ATOM   565  C  CB    . MET A 1 72  ? 19.235 -1.329  -22.361 1.00 19.78 ? 72  MET A CB    1 
ATOM   566  C  CG    . MET A 1 72  ? 17.816 -0.860  -22.439 1.00 23.40 ? 72  MET A CG    1 
ATOM   567  S  SD    . MET A 1 72  ? 17.601 0.731   -21.605 1.00 28.60 ? 72  MET A SD    1 
ATOM   568  C  CE    . MET A 1 72  ? 16.061 1.269   -22.273 1.00 30.98 ? 72  MET A CE    1 
ATOM   569  N  N     . ARG A 1 73  ? 22.108 -1.891  -23.677 1.00 20.82 ? 73  ARG A N     1 
ATOM   570  C  CA    . ARG A 1 73  ? 23.461 -2.411  -23.521 1.00 24.48 ? 73  ARG A CA    1 
ATOM   571  C  C     . ARG A 1 73  ? 24.515 -1.326  -23.713 1.00 24.32 ? 73  ARG A C     1 
ATOM   572  O  O     . ARG A 1 73  ? 25.625 -1.444  -23.178 1.00 23.31 ? 73  ARG A O     1 
ATOM   573  C  CB    . ARG A 1 73  ? 23.678 -3.557  -24.517 1.00 28.25 ? 73  ARG A CB    1 
ATOM   574  C  CG    . ARG A 1 73  ? 25.033 -4.241  -24.478 1.00 34.96 ? 73  ARG A CG    1 
ATOM   575  C  CD    . ARG A 1 73  ? 25.054 -5.476  -25.390 1.00 32.80 ? 73  ARG A CD    1 
ATOM   576  N  NE    . ARG A 1 73  ? 23.993 -6.420  -25.058 1.00 41.05 ? 73  ARG A NE    1 
ATOM   577  C  CZ    . ARG A 1 73  ? 23.060 -6.845  -25.902 1.00 39.90 ? 73  ARG A CZ    1 
ATOM   578  N  NH1   . ARG A 1 73  ? 23.032 -6.443  -27.166 1.00 39.21 ? 73  ARG A NH1   1 
ATOM   579  N  NH2   . ARG A 1 73  ? 22.126 -7.688  -25.464 1.00 38.09 ? 73  ARG A NH2   1 
ATOM   580  N  N     . THR A 1 74  ? 24.211 -0.283  -24.485 1.00 23.66 ? 74  THR A N     1 
ATOM   581  C  CA    . THR A 1 74  ? 25.206 0.788   -24.615 1.00 27.35 ? 74  THR A CA    1 
ATOM   582  C  C     . THR A 1 74  ? 25.463 1.556   -23.309 1.00 26.50 ? 74  THR A C     1 
ATOM   583  O  O     . THR A 1 74  ? 26.479 2.262   -23.208 1.00 24.37 ? 74  THR A O     1 
ATOM   584  C  CB    . THR A 1 74  ? 24.797 1.783   -25.709 1.00 27.42 ? 74  THR A CB    1 
ATOM   585  O  OG1   . THR A 1 74  ? 23.681 2.572   -25.264 1.00 36.97 ? 74  THR A OG1   1 
ATOM   586  C  CG2   . THR A 1 74  ? 24.426 1.044   -26.970 1.00 32.00 ? 74  THR A CG2   1 
ATOM   587  N  N     . GLY A 1 75  ? 24.581 1.452   -22.316 1.00 20.27 ? 75  GLY A N     1 
ATOM   588  C  CA    . GLY A 1 75  ? 24.800 2.168   -21.064 1.00 20.69 ? 75  GLY A CA    1 
ATOM   589  C  C     . GLY A 1 75  ? 25.987 1.609   -20.294 1.00 23.56 ? 75  GLY A C     1 
ATOM   590  O  O     . GLY A 1 75  ? 26.202 0.397   -20.233 1.00 23.16 ? 75  GLY A O     1 
ATOM   591  N  N     . GLU A 1 76  ? 26.779 2.509   -19.700 1.00 18.17 ? 76  GLU A N     1 
ATOM   592  C  CA    . GLU A 1 76  ? 27.931 2.089   -18.911 1.00 20.88 ? 76  GLU A CA    1 
ATOM   593  C  C     . GLU A 1 76  ? 27.654 2.069   -17.422 1.00 22.29 ? 76  GLU A C     1 
ATOM   594  O  O     . GLU A 1 76  ? 28.367 1.377   -16.681 1.00 21.63 ? 76  GLU A O     1 
ATOM   595  C  CB    . GLU A 1 76  ? 29.122 3.016   -19.141 1.00 22.36 ? 76  GLU A CB    1 
ATOM   596  C  CG    . GLU A 1 76  ? 29.629 3.047   -20.555 1.00 25.22 ? 76  GLU A CG    1 
ATOM   597  C  CD    . GLU A 1 76  ? 30.693 4.108   -20.719 1.00 32.71 ? 76  GLU A CD    1 
ATOM   598  O  OE1   . GLU A 1 76  ? 30.328 5.297   -20.804 1.00 23.95 ? 76  GLU A OE1   1 
ATOM   599  O  OE2   . GLU A 1 76  ? 31.894 3.755   -20.711 1.00 38.72 ? 76  GLU A OE2   1 
ATOM   600  N  N     . GLY A 1 77  ? 26.666 2.827   -16.968 1.00 21.08 ? 77  GLY A N     1 
ATOM   601  C  CA    . GLY A 1 77  ? 26.255 2.735   -15.576 1.00 18.87 ? 77  GLY A CA    1 
ATOM   602  C  C     . GLY A 1 77  ? 24.784 3.061   -15.472 1.00 18.39 ? 77  GLY A C     1 
ATOM   603  O  O     . GLY A 1 77  ? 24.237 3.774   -16.315 1.00 15.73 ? 77  GLY A O     1 
ATOM   604  N  N     . PHE A 1 78  ? 24.142 2.544   -14.428 1.00 16.98 ? 78  PHE A N     1 
ATOM   605  C  CA    . PHE A 1 78  ? 22.686 2.626   -14.312 1.00 17.64 ? 78  PHE A CA    1 
ATOM   606  C  C     . PHE A 1 78  ? 22.272 3.197   -12.964 1.00 18.98 ? 78  PHE A C     1 
ATOM   607  O  O     . PHE A 1 78  ? 22.767 2.759   -11.914 1.00 17.61 ? 78  PHE A O     1 
ATOM   608  C  CB    . PHE A 1 78  ? 22.056 1.238   -14.511 1.00 16.14 ? 78  PHE A CB    1 
ATOM   609  C  CG    . PHE A 1 78  ? 22.255 0.699   -15.890 1.00 17.93 ? 78  PHE A CG    1 
ATOM   610  C  CD1   . PHE A 1 78  ? 23.474 0.138   -16.246 1.00 22.40 ? 78  PHE A CD1   1 
ATOM   611  C  CD2   . PHE A 1 78  ? 21.244 0.789   -16.849 1.00 19.76 ? 78  PHE A CD2   1 
ATOM   612  C  CE1   . PHE A 1 78  ? 23.686 -0.342  -17.526 1.00 22.61 ? 78  PHE A CE1   1 
ATOM   613  C  CE2   . PHE A 1 78  ? 21.456 0.311   -18.124 1.00 20.91 ? 78  PHE A CE2   1 
ATOM   614  C  CZ    . PHE A 1 78  ? 22.684 -0.243  -18.464 1.00 19.55 ? 78  PHE A CZ    1 
ATOM   615  N  N     . LEU A 1 79  ? 21.349 4.160   -12.998 1.00 15.43 ? 79  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 79  ? 20.680 4.639   -11.796 1.00 17.06 ? 79  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 79  ? 19.372 3.879   -11.649 1.00 20.03 ? 79  LEU A C     1 
ATOM   618  O  O     . LEU A 1 79  ? 18.494 3.995   -12.515 1.00 16.68 ? 79  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 79  ? 20.378 6.135   -11.874 1.00 17.97 ? 79  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 79  ? 21.383 7.220   -11.561 1.00 26.85 ? 79  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 79  ? 20.574 8.531   -11.290 1.00 23.96 ? 79  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 79  ? 22.188 6.807   -10.349 1.00 24.02 ? 79  LEU A CD2   1 
ATOM   623  N  N     . LEU A 1 80  ? 19.233 3.119   -10.566 1.00 16.57 ? 80  LEU A N     1 
ATOM   624  C  CA    . LEU A 1 80  ? 17.997 2.396   -10.274 1.00 17.42 ? 80  LEU A CA    1 
ATOM   625  C  C     . LEU A 1 80  ? 17.182 3.260   -9.333  1.00 16.27 ? 80  LEU A C     1 
ATOM   626  O  O     . LEU A 1 80  ? 17.548 3.397   -8.164  1.00 17.01 ? 80  LEU A O     1 
ATOM   627  C  CB    . LEU A 1 80  ? 18.285 1.051   -9.612  1.00 15.04 ? 80  LEU A CB    1 
ATOM   628  C  CG    . LEU A 1 80  ? 19.307 0.155   -10.302 1.00 20.99 ? 80  LEU A CG    1 
ATOM   629  C  CD1   . LEU A 1 80  ? 19.773 -0.911  -9.310  1.00 26.05 ? 80  LEU A CD1   1 
ATOM   630  C  CD2   . LEU A 1 80  ? 18.675 -0.475  -11.513 1.00 27.45 ? 80  LEU A CD2   1 
ATOM   631  N  N     . VAL A 1 81  ? 16.072 3.823   -9.814  1.00 14.36 ? 81  VAL A N     1 
ATOM   632  C  CA    . VAL A 1 81  ? 15.311 4.807   -9.048  1.00 15.83 ? 81  VAL A CA    1 
ATOM   633  C  C     . VAL A 1 81  ? 13.996 4.198   -8.587  1.00 19.78 ? 81  VAL A C     1 
ATOM   634  O  O     . VAL A 1 81  ? 13.256 3.622   -9.394  1.00 16.64 ? 81  VAL A O     1 
ATOM   635  C  CB    . VAL A 1 81  ? 15.064 6.076   -9.876  1.00 15.23 ? 81  VAL A CB    1 
ATOM   636  C  CG1   . VAL A 1 81  ? 14.404 7.162   -9.023  1.00 17.78 ? 81  VAL A CG1   1 
ATOM   637  C  CG2   . VAL A 1 81  ? 16.386 6.574   -10.469 1.00 16.47 ? 81  VAL A CG2   1 
ATOM   638  N  N     . PHE A 1 82  ? 13.704 4.328   -7.286  1.00 17.99 ? 82  PHE A N     1 
ATOM   639  C  CA    . PHE A 1 82  ? 12.355 4.093   -6.772  1.00 18.32 ? 82  PHE A CA    1 
ATOM   640  C  C     . PHE A 1 82  ? 11.918 5.326   -5.983  1.00 18.91 ? 82  PHE A C     1 
ATOM   641  O  O     . PHE A 1 82  ? 12.722 6.222   -5.712  1.00 17.90 ? 82  PHE A O     1 
ATOM   642  C  CB    . PHE A 1 82  ? 12.275 2.821   -5.909  1.00 18.24 ? 82  PHE A CB    1 
ATOM   643  C  CG    . PHE A 1 82  ? 12.999 2.932   -4.594  1.00 17.68 ? 82  PHE A CG    1 
ATOM   644  C  CD1   . PHE A 1 82  ? 14.368 2.720   -4.518  1.00 16.65 ? 82  PHE A CD1   1 
ATOM   645  C  CD2   . PHE A 1 82  ? 12.308 3.268   -3.438  1.00 18.71 ? 82  PHE A CD2   1 
ATOM   646  C  CE1   . PHE A 1 82  ? 15.032 2.831   -3.306  1.00 16.47 ? 82  PHE A CE1   1 
ATOM   647  C  CE2   . PHE A 1 82  ? 12.965 3.390   -2.224  1.00 20.74 ? 82  PHE A CE2   1 
ATOM   648  C  CZ    . PHE A 1 82  ? 14.322 3.171   -2.154  1.00 20.86 ? 82  PHE A CZ    1 
ATOM   649  N  N     . ALA A 1 83  ? 10.628 5.403   -5.653  1.00 16.97 ? 83  ALA A N     1 
ATOM   650  C  CA    . ALA A 1 83  ? 10.088 6.489   -4.834  1.00 18.28 ? 83  ALA A CA    1 
ATOM   651  C  C     . ALA A 1 83  ? 9.830  5.983   -3.417  1.00 19.59 ? 83  ALA A C     1 
ATOM   652  O  O     . ALA A 1 83  ? 9.234  4.917   -3.232  1.00 21.75 ? 83  ALA A O     1 
ATOM   653  C  CB    . ALA A 1 83  ? 8.791  7.054   -5.426  1.00 21.40 ? 83  ALA A CB    1 
ATOM   654  N  N     . ILE A 1 84  ? 10.274 6.748   -2.413  1.00 20.41 ? 84  ILE A N     1 
ATOM   655  C  CA    . ILE A 1 84  ? 10.208 6.236   -1.046  1.00 20.49 ? 84  ILE A CA    1 
ATOM   656  C  C     . ILE A 1 84  ? 8.786  6.126   -0.527  1.00 21.24 ? 84  ILE A C     1 
ATOM   657  O  O     . ILE A 1 84  ? 8.577  5.538   0.537   1.00 24.44 ? 84  ILE A O     1 
ATOM   658  C  CB    . ILE A 1 84  ? 11.063 7.090   -0.077  1.00 24.85 ? 84  ILE A CB    1 
ATOM   659  C  CG1   . ILE A 1 84  ? 10.553 8.538   0.009   1.00 25.84 ? 84  ILE A CG1   1 
ATOM   660  C  CG2   . ILE A 1 84  ? 12.521 7.055   -0.506  1.00 22.42 ? 84  ILE A CG2   1 
ATOM   661  C  CD1   . ILE A 1 84  ? 9.504  8.796   1.096   1.00 36.79 ? 84  ILE A CD1   1 
ATOM   662  N  N     . ASN A 1 85  ? 7.805  6.700   -1.227  1.00 20.64 ? 85  ASN A N     1 
ATOM   663  C  CA    . ASN A 1 85  ? 6.407  6.570   -0.829  1.00 25.63 ? 85  ASN A CA    1 
ATOM   664  C  C     . ASN A 1 85  ? 5.641  5.617   -1.733  1.00 24.64 ? 85  ASN A C     1 
ATOM   665  O  O     . ASN A 1 85  ? 4.402  5.647   -1.762  1.00 26.04 ? 85  ASN A O     1 
ATOM   666  C  CB    . ASN A 1 85  ? 5.718  7.937   -0.813  1.00 26.97 ? 85  ASN A CB    1 
ATOM   667  C  CG    . ASN A 1 85  ? 5.564  8.524   -2.194  1.00 30.39 ? 85  ASN A CG    1 
ATOM   668  O  OD1   . ASN A 1 85  ? 6.316  8.192   -3.115  1.00 27.10 ? 85  ASN A OD1   1 
ATOM   669  N  ND2   . ASN A 1 85  ? 4.573  9.392   -2.358  1.00 32.42 ? 85  ASN A ND2   1 
ATOM   670  N  N     . ASN A 1 86  ? 6.345  4.759   -2.470  1.00 24.52 ? 86  ASN A N     1 
ATOM   671  C  CA    . ASN A 1 86  ? 5.676  3.805   -3.355  1.00 24.39 ? 86  ASN A CA    1 
ATOM   672  C  C     . ASN A 1 86  ? 6.359  2.447   -3.238  1.00 21.36 ? 86  ASN A C     1 
ATOM   673  O  O     . ASN A 1 86  ? 7.394  2.211   -3.867  1.00 19.88 ? 86  ASN A O     1 
ATOM   674  C  CB    . ASN A 1 86  ? 5.683  4.290   -4.799  1.00 22.35 ? 86  ASN A CB    1 
ATOM   675  C  CG    . ASN A 1 86  ? 4.803  3.445   -5.673  1.00 24.40 ? 86  ASN A CG    1 
ATOM   676  O  OD1   . ASN A 1 86  ? 5.112  2.294   -5.932  1.00 30.35 ? 86  ASN A OD1   1 
ATOM   677  N  ND2   . ASN A 1 86  ? 3.659  3.994   -6.081  1.00 34.85 ? 86  ASN A ND2   1 
ATOM   678  N  N     . THR A 1 87  ? 5.761  1.541   -2.461  1.00 19.10 ? 87  THR A N     1 
ATOM   679  C  CA    . THR A 1 87  ? 6.401  0.251   -2.218  1.00 23.40 ? 87  THR A CA    1 
ATOM   680  C  C     . THR A 1 87  ? 6.547  -0.566  -3.498  1.00 21.48 ? 87  THR A C     1 
ATOM   681  O  O     . THR A 1 87  ? 7.523  -1.317  -3.662  1.00 21.19 ? 87  THR A O     1 
ATOM   682  C  CB    . THR A 1 87  ? 5.612  -0.514  -1.153  1.00 23.39 ? 87  THR A CB    1 
ATOM   683  O  OG1   . THR A 1 87  ? 5.726  0.207   0.084   1.00 27.15 ? 87  THR A OG1   1 
ATOM   684  C  CG2   . THR A 1 87  ? 6.173  -1.915  -0.977  1.00 31.86 ? 87  THR A CG2   1 
ATOM   685  N  N     . LYS A 1 88  ? 5.566  -0.478  -4.400  1.00 20.41 ? 88  LYS A N     1 
ATOM   686  C  CA    . LYS A 1 88  ? 5.670  -1.255  -5.630  1.00 21.25 ? 88  LYS A CA    1 
ATOM   687  C  C     . LYS A 1 88  ? 6.910  -0.854  -6.423  1.00 19.51 ? 88  LYS A C     1 
ATOM   688  O  O     . LYS A 1 88  ? 7.606  -1.713  -6.979  1.00 18.04 ? 88  LYS A O     1 
ATOM   689  C  CB    . LYS A 1 88  ? 4.397  -1.096  -6.467  1.00 22.80 ? 88  LYS A CB    1 
ATOM   690  C  CG    . LYS A 1 88  ? 4.447  -1.779  -7.829  1.00 25.66 ? 88  LYS A CG    1 
ATOM   691  C  CD    . LYS A 1 88  ? 4.587  -3.304  -7.733  1.00 28.20 ? 88  LYS A CD    1 
ATOM   692  C  CE    . LYS A 1 88  ? 3.913  -3.992  -8.928  1.00 32.09 ? 88  LYS A CE    1 
ATOM   693  N  NZ    . LYS A 1 88  ? 4.559  -3.611  -10.230 1.00 32.62 ? 88  LYS A NZ    1 
ATOM   694  N  N     . SER A 1 89  ? 7.202  0.450   -6.502  1.00 20.25 ? 89  SER A N     1 
ATOM   695  C  CA    . SER A 1 89  ? 8.363  0.868   -7.287  1.00 18.74 ? 89  SER A CA    1 
ATOM   696  C  C     . SER A 1 89  ? 9.661  0.335   -6.686  1.00 19.88 ? 89  SER A C     1 
ATOM   697  O  O     . SER A 1 89  ? 10.627 0.080   -7.415  1.00 18.68 ? 89  SER A O     1 
ATOM   698  C  CB    . SER A 1 89  ? 8.387  2.393   -7.405  1.00 18.59 ? 89  SER A CB    1 
ATOM   699  O  OG    . SER A 1 89  ? 8.726  3.015   -6.175  1.00 19.19 ? 89  SER A OG    1 
ATOM   700  N  N     . PHE A 1 90  ? 9.694  0.148   -5.355  1.00 17.43 ? 90  PHE A N     1 
ATOM   701  C  CA    . PHE A 1 90  ? 10.840 -0.470  -4.701  1.00 18.42 ? 90  PHE A CA    1 
ATOM   702  C  C     . PHE A 1 90  ? 10.931 -1.953  -5.024  1.00 19.13 ? 90  PHE A C     1 
ATOM   703  O  O     . PHE A 1 90  ? 12.026 -2.473  -5.284  1.00 18.54 ? 90  PHE A O     1 
ATOM   704  C  CB    . PHE A 1 90  ? 10.742 -0.257  -3.187  1.00 20.34 ? 90  PHE A CB    1 
ATOM   705  C  CG    . PHE A 1 90  ? 11.838 -0.924  -2.410  1.00 20.59 ? 90  PHE A CG    1 
ATOM   706  C  CD1   . PHE A 1 90  ? 13.156 -0.510  -2.556  1.00 20.32 ? 90  PHE A CD1   1 
ATOM   707  C  CD2   . PHE A 1 90  ? 11.550 -1.950  -1.518  1.00 21.64 ? 90  PHE A CD2   1 
ATOM   708  C  CE1   . PHE A 1 90  ? 14.184 -1.114  -1.825  1.00 20.80 ? 90  PHE A CE1   1 
ATOM   709  C  CE2   . PHE A 1 90  ? 12.573 -2.562  -0.772  1.00 26.26 ? 90  PHE A CE2   1 
ATOM   710  C  CZ    . PHE A 1 90  ? 13.895 -2.138  -0.939  1.00 23.99 ? 90  PHE A CZ    1 
ATOM   711  N  N     . GLU A 1 91  ? 9.793  -2.658  -4.987  1.00 18.18 ? 91  GLU A N     1 
ATOM   712  C  CA    . GLU A 1 91  ? 9.811  -4.083  -5.298  1.00 21.34 ? 91  GLU A CA    1 
ATOM   713  C  C     . GLU A 1 91  ? 10.196 -4.341  -6.754  1.00 21.00 ? 91  GLU A C     1 
ATOM   714  O  O     . GLU A 1 91  ? 10.772 -5.391  -7.064  1.00 22.55 ? 91  GLU A O     1 
ATOM   715  C  CB    . GLU A 1 91  ? 8.444  -4.684  -4.979  1.00 21.95 ? 91  GLU A CB    1 
ATOM   716  C  CG    . GLU A 1 91  ? 8.293  -5.049  -3.491  1.00 34.60 ? 91  GLU A CG    1 
ATOM   717  C  CD    . GLU A 1 91  ? 6.837  -5.073  -3.029  1.00 39.43 ? 91  GLU A CD    1 
ATOM   718  O  OE1   . GLU A 1 91  ? 5.933  -4.843  -3.867  1.00 40.16 ? 91  GLU A OE1   1 
ATOM   719  O  OE2   . GLU A 1 91  ? 6.598  -5.311  -1.821  1.00 41.88 ? 91  GLU A OE2   1 
ATOM   720  N  N     . ASP A 1 92  ? 9.915  -3.389  -7.649  1.00 19.56 ? 92  ASP A N     1 
ATOM   721  C  CA    . ASP A 1 92  ? 10.286 -3.508  -9.069  1.00 18.95 ? 92  ASP A CA    1 
ATOM   722  C  C     . ASP A 1 92  ? 11.793 -3.398  -9.318  1.00 17.86 ? 92  ASP A C     1 
ATOM   723  O  O     . ASP A 1 92  ? 12.262 -3.754  -10.421 1.00 16.68 ? 92  ASP A O     1 
ATOM   724  C  CB    . ASP A 1 92  ? 9.574  -2.438  -9.915  1.00 17.20 ? 92  ASP A CB    1 
ATOM   725  C  CG    . ASP A 1 92  ? 8.083  -2.708  -10.118 1.00 24.82 ? 92  ASP A CG    1 
ATOM   726  O  OD1   . ASP A 1 92  ? 7.584  -3.804  -9.757  1.00 24.08 ? 92  ASP A OD1   1 
ATOM   727  O  OD2   . ASP A 1 92  ? 7.420  -1.789  -10.639 1.00 21.78 ? 92  ASP A OD2   1 
ATOM   728  N  N     . ILE A 1 93  ? 12.562 -2.922  -8.333  1.00 17.42 ? 93  ILE A N     1 
ATOM   729  C  CA    . ILE A 1 93  ? 13.999 -2.744  -8.541  1.00 17.38 ? 93  ILE A CA    1 
ATOM   730  C  C     . ILE A 1 93  ? 14.659 -4.063  -8.940  1.00 17.20 ? 93  ILE A C     1 
ATOM   731  O  O     . ILE A 1 93  ? 15.586 -4.085  -9.761  1.00 16.13 ? 93  ILE A O     1 
ATOM   732  C  CB    . ILE A 1 93  ? 14.644 -2.140  -7.275  1.00 18.09 ? 93  ILE A CB    1 
ATOM   733  C  CG1   . ILE A 1 93  ? 14.182 -0.691  -7.077  1.00 16.50 ? 93  ILE A CG1   1 
ATOM   734  C  CG2   . ILE A 1 93  ? 16.160 -2.204  -7.369  1.00 20.75 ? 93  ILE A CG2   1 
ATOM   735  C  CD1   . ILE A 1 93  ? 14.446 0.253   -8.258  1.00 20.56 ? 93  ILE A CD1   1 
ATOM   736  N  N     . HIS A 1 94  ? 14.210 -5.177  -8.355  1.00 16.62 ? 94  HIS A N     1 
ATOM   737  C  CA    . HIS A 1 94  ? 14.772 -6.480  -8.704  1.00 19.97 ? 94  HIS A CA    1 
ATOM   738  C  C     . HIS A 1 94  ? 14.653 -6.746  -10.198 1.00 18.41 ? 94  HIS A C     1 
ATOM   739  O  O     . HIS A 1 94  ? 15.616 -7.178  -10.850 1.00 17.14 ? 94  HIS A O     1 
ATOM   740  C  CB    . HIS A 1 94  ? 14.067 -7.595  -7.916  1.00 23.08 ? 94  HIS A CB    1 
ATOM   741  C  CG    . HIS A 1 94  ? 14.404 -8.977  -8.392  1.00 23.56 ? 94  HIS A CG    1 
ATOM   742  N  ND1   . HIS A 1 94  ? 15.561 -9.630  -8.016  1.00 25.79 ? 94  HIS A ND1   1 
ATOM   743  C  CD2   . HIS A 1 94  ? 13.734 -9.839  -9.197  1.00 26.18 ? 94  HIS A CD2   1 
ATOM   744  C  CE1   . HIS A 1 94  ? 15.600 -10.821 -8.588  1.00 28.28 ? 94  HIS A CE1   1 
ATOM   745  N  NE2   . HIS A 1 94  ? 14.500 -10.977 -9.304  1.00 25.33 ? 94  HIS A NE2   1 
ATOM   746  N  N     . HIS A 1 95  ? 13.464 -6.502  -10.750 1.00 18.47 ? 95  HIS A N     1 
ATOM   747  C  CA    . HIS A 1 95  ? 13.243 -6.646  -12.182 1.00 22.10 ? 95  HIS A CA    1 
ATOM   748  C  C     . HIS A 1 95  ? 14.226 -5.810  -12.988 1.00 17.98 ? 95  HIS A C     1 
ATOM   749  O  O     . HIS A 1 95  ? 14.853 -6.305  -13.939 1.00 16.20 ? 95  HIS A O     1 
ATOM   750  C  CB    . HIS A 1 95  ? 11.794 -6.259  -12.519 1.00 19.34 ? 95  HIS A CB    1 
ATOM   751  C  CG    . HIS A 1 95  ? 11.562 -5.977  -13.980 1.00 19.46 ? 95  HIS A CG    1 
ATOM   752  N  ND1   . HIS A 1 95  ? 11.479 -6.975  -14.927 1.00 19.10 ? 95  HIS A ND1   1 
ATOM   753  C  CD2   . HIS A 1 95  ? 11.363 -4.810  -14.642 1.00 17.77 ? 95  HIS A CD2   1 
ATOM   754  C  CE1   . HIS A 1 95  ? 11.281 -6.434  -16.119 1.00 20.59 ? 95  HIS A CE1   1 
ATOM   755  N  NE2   . HIS A 1 95  ? 11.190 -5.122  -15.972 1.00 19.05 ? 95  HIS A NE2   1 
ATOM   756  N  N     . TYR A 1 96  ? 14.339 -4.518  -12.655 1.00 16.64 ? 96  TYR A N     1 
ATOM   757  C  CA    . TYR A 1 96  ? 15.215 -3.667  -13.460 1.00 15.83 ? 96  TYR A CA    1 
ATOM   758  C  C     . TYR A 1 96  ? 16.667 -4.135  -13.377 1.00 16.45 ? 96  TYR A C     1 
ATOM   759  O  O     . TYR A 1 96  ? 17.371 -4.188  -14.394 1.00 16.07 ? 96  TYR A O     1 
ATOM   760  C  CB    . TYR A 1 96  ? 15.064 -2.200  -13.044 1.00 15.02 ? 96  TYR A CB    1 
ATOM   761  C  CG    . TYR A 1 96  ? 13.735 -1.669  -13.521 1.00 18.09 ? 96  TYR A CG    1 
ATOM   762  C  CD1   . TYR A 1 96  ? 13.513 -1.410  -14.870 1.00 18.13 ? 96  TYR A CD1   1 
ATOM   763  C  CD2   . TYR A 1 96  ? 12.667 -1.505  -12.634 1.00 16.18 ? 96  TYR A CD2   1 
ATOM   764  C  CE1   . TYR A 1 96  ? 12.265 -0.939  -15.312 1.00 18.82 ? 96  TYR A CE1   1 
ATOM   765  C  CE2   . TYR A 1 96  ? 11.415 -1.051  -13.078 1.00 16.36 ? 96  TYR A CE2   1 
ATOM   766  C  CZ    . TYR A 1 96  ? 11.230 -0.778  -14.424 1.00 20.07 ? 96  TYR A CZ    1 
ATOM   767  O  OH    . TYR A 1 96  ? 9.991  -0.341  -14.886 1.00 17.31 ? 96  TYR A OH    1 
ATOM   768  N  N     . ARG A 1 97  ? 17.131 -4.500  -12.173 1.00 16.66 ? 97  ARG A N     1 
ATOM   769  C  CA    . ARG A 1 97  ? 18.500 -4.998  -12.038 1.00 16.15 ? 97  ARG A CA    1 
ATOM   770  C  C     . ARG A 1 97  ? 18.729 -6.272  -12.847 1.00 20.23 ? 97  ARG A C     1 
ATOM   771  O  O     . ARG A 1 97  ? 19.785 -6.436  -13.470 1.00 18.41 ? 97  ARG A O     1 
ATOM   772  C  CB    . ARG A 1 97  ? 18.842 -5.235  -10.567 1.00 22.04 ? 97  ARG A CB    1 
ATOM   773  C  CG    . ARG A 1 97  ? 20.232 -5.841  -10.391 1.00 24.61 ? 97  ARG A CG    1 
ATOM   774  C  CD    . ARG A 1 97  ? 20.712 -5.736  -8.957  1.00 26.90 ? 97  ARG A CD    1 
ATOM   775  N  NE    . ARG A 1 97  ? 22.084 -6.206  -8.797  1.00 27.79 ? 97  ARG A NE    1 
ATOM   776  C  CZ    . ARG A 1 97  ? 22.414 -7.448  -8.483  1.00 33.62 ? 97  ARG A CZ    1 
ATOM   777  N  NH1   . ARG A 1 97  ? 21.496 -8.399  -8.364  1.00 37.31 ? 97  ARG A NH1   1 
ATOM   778  N  NH2   . ARG A 1 97  ? 23.695 -7.742  -8.262  1.00 34.31 ? 97  ARG A NH2   1 
ATOM   779  N  N     . GLU A 1 98  ? 17.754 -7.191  -12.860 1.00 16.85 ? 98  GLU A N     1 
ATOM   780  C  CA    . GLU A 1 98  ? 17.938 -8.416  -13.633 1.00 20.16 ? 98  GLU A CA    1 
ATOM   781  C  C     . GLU A 1 98  ? 17.946 -8.159  -15.134 1.00 20.90 ? 98  GLU A C     1 
ATOM   782  O  O     . GLU A 1 98  ? 18.662 -8.847  -15.875 1.00 18.19 ? 98  GLU A O     1 
ATOM   783  C  CB    . GLU A 1 98  ? 16.851 -9.433  -13.283 1.00 20.45 ? 98  GLU A CB    1 
ATOM   784  C  CG    . GLU A 1 98  ? 16.996 -9.986  -11.855 1.00 25.04 ? 98  GLU A CG    1 
ATOM   785  C  CD    . GLU A 1 98  ? 18.308 -10.727 -11.624 1.00 31.51 ? 98  GLU A CD    1 
ATOM   786  O  OE1   . GLU A 1 98  ? 18.730 -11.515 -12.499 1.00 32.00 ? 98  GLU A OE1   1 
ATOM   787  O  OE2   . GLU A 1 98  ? 18.916 -10.524 -10.548 1.00 31.52 ? 98  GLU A OE2   1 
ATOM   788  N  N     . GLN A 1 99  ? 17.175 -7.179  -15.613 1.00 16.80 ? 99  GLN A N     1 
ATOM   789  C  CA    . GLN A 1 99  ? 17.215 -6.894  -17.047 1.00 17.92 ? 99  GLN A CA    1 
ATOM   790  C  C     . GLN A 1 99  ? 18.555 -6.275  -17.440 1.00 19.78 ? 99  GLN A C     1 
ATOM   791  O  O     . GLN A 1 99  ? 19.099 -6.565  -18.523 1.00 20.68 ? 99  GLN A O     1 
ATOM   792  C  CB    . GLN A 1 99  ? 16.052 -5.977  -17.440 1.00 19.28 ? 99  GLN A CB    1 
ATOM   793  C  CG    . GLN A 1 99  ? 14.667 -6.605  -17.255 1.00 19.14 ? 99  GLN A CG    1 
ATOM   794  C  CD    . GLN A 1 99  ? 14.548 -7.920  -18.002 1.00 22.69 ? 99  GLN A CD    1 
ATOM   795  O  OE1   . GLN A 1 99  ? 14.946 -8.014  -19.168 1.00 20.57 ? 99  GLN A OE1   1 
ATOM   796  N  NE2   . GLN A 1 99  ? 14.040 -8.959  -17.320 1.00 25.05 ? 99  GLN A NE2   1 
ATOM   797  N  N     . ILE A 1 100 ? 19.109 -5.426  -16.568 1.00 17.43 ? 100 ILE A N     1 
ATOM   798  C  CA    . ILE A 1 100 ? 20.452 -4.900  -16.815 1.00 16.23 ? 100 ILE A CA    1 
ATOM   799  C  C     . ILE A 1 100 ? 21.467 -6.037  -16.890 1.00 21.60 ? 100 ILE A C     1 
ATOM   800  O  O     . ILE A 1 100 ? 22.263 -6.123  -17.836 1.00 22.78 ? 100 ILE A O     1 
ATOM   801  C  CB    . ILE A 1 100 ? 20.842 -3.870  -15.736 1.00 22.52 ? 100 ILE A CB    1 
ATOM   802  C  CG1   . ILE A 1 100 ? 19.955 -2.638  -15.833 1.00 19.07 ? 100 ILE A CG1   1 
ATOM   803  C  CG2   . ILE A 1 100 ? 22.314 -3.473  -15.894 1.00 20.96 ? 100 ILE A CG2   1 
ATOM   804  C  CD1   . ILE A 1 100 ? 19.922 -1.815  -14.549 1.00 16.37 ? 100 ILE A CD1   1 
ATOM   805  N  N     . LYS A 1 101 ? 21.485 -6.899  -15.860 1.00 21.41 ? 101 LYS A N     1 
ATOM   806  C  CA    . LYS A 1 101 ? 22.408 -8.036  -15.850 1.00 21.08 ? 101 LYS A CA    1 
ATOM   807  C  C     . LYS A 1 101 ? 22.256 -8.881  -17.103 1.00 26.92 ? 101 LYS A C     1 
ATOM   808  O  O     . LYS A 1 101 ? 23.254 -9.352  -17.667 1.00 26.22 ? 101 LYS A O     1 
ATOM   809  C  CB    . LYS A 1 101 ? 22.172 -8.897  -14.612 1.00 23.36 ? 101 LYS A CB    1 
ATOM   810  C  CG    . LYS A 1 101 ? 22.752 -8.315  -13.338 1.00 27.78 ? 101 LYS A CG    1 
ATOM   811  C  CD    . LYS A 1 101 ? 22.177 -9.036  -12.118 1.00 36.00 ? 101 LYS A CD    1 
ATOM   812  C  CE    . LYS A 1 101 ? 22.203 -10.556 -12.298 1.00 40.57 ? 101 LYS A CE    1 
ATOM   813  N  NZ    . LYS A 1 101 ? 21.780 -11.284 -11.054 1.00 35.55 ? 101 LYS A NZ    1 
ATOM   814  N  N     . ARG A 1 102 ? 21.012 -9.072  -17.565 1.00 22.39 ? 102 ARG A N     1 
ATOM   815  C  CA    . ARG A 1 102 ? 20.786 -9.892  -18.752 1.00 22.78 ? 102 ARG A CA    1 
ATOM   816  C  C     . ARG A 1 102 ? 21.417 -9.268  -19.996 1.00 26.56 ? 102 ARG A C     1 
ATOM   817  O  O     . ARG A 1 102 ? 22.111 -9.953  -20.759 1.00 25.66 ? 102 ARG A O     1 
ATOM   818  C  CB    . ARG A 1 102 ? 19.286 -10.106 -18.959 1.00 20.69 ? 102 ARG A CB    1 
ATOM   819  C  CG    . ARG A 1 102 ? 18.924 -10.942 -20.182 1.00 22.54 ? 102 ARG A CG    1 
ATOM   820  C  CD    . ARG A 1 102 ? 17.416 -11.109 -20.333 1.00 21.31 ? 102 ARG A CD    1 
ATOM   821  N  NE    . ARG A 1 102 ? 16.709 -9.857  -20.616 1.00 22.76 ? 102 ARG A NE    1 
ATOM   822  C  CZ    . ARG A 1 102 ? 16.678 -9.258  -21.799 1.00 25.09 ? 102 ARG A CZ    1 
ATOM   823  N  NH1   . ARG A 1 102 ? 17.267 -9.788  -22.865 1.00 24.91 ? 102 ARG A NH1   1 
ATOM   824  N  NH2   . ARG A 1 102 ? 16.042 -8.095  -21.921 1.00 20.80 ? 102 ARG A NH2   1 
ATOM   825  N  N     . VAL A 1 103 ? 21.161 -7.978  -20.247 1.00 20.58 ? 103 VAL A N     1 
ATOM   826  C  CA    . VAL A 1 103 ? 21.660 -7.432  -21.511 1.00 23.50 ? 103 VAL A CA    1 
ATOM   827  C  C     . VAL A 1 103 ? 23.162 -7.155  -21.459 1.00 28.33 ? 103 VAL A C     1 
ATOM   828  O  O     . VAL A 1 103 ? 23.829 -7.158  -22.503 1.00 25.99 ? 103 VAL A O     1 
ATOM   829  C  CB    . VAL A 1 103 ? 20.877 -6.176  -21.925 1.00 23.65 ? 103 VAL A CB    1 
ATOM   830  C  CG1   . VAL A 1 103 ? 19.403 -6.520  -22.031 1.00 22.82 ? 103 VAL A CG1   1 
ATOM   831  C  CG2   . VAL A 1 103 ? 21.133 -5.008  -20.950 1.00 23.57 ? 103 VAL A CG2   1 
ATOM   832  N  N     . LYS A 1 104 ? 23.719 -6.892  -20.272 1.00 24.35 ? 104 LYS A N     1 
ATOM   833  C  CA    . LYS A 1 104 ? 25.158 -6.667  -20.170 1.00 27.91 ? 104 LYS A CA    1 
ATOM   834  C  C     . LYS A 1 104 ? 25.939 -7.967  -20.046 1.00 32.94 ? 104 LYS A C     1 
ATOM   835  O  O     . LYS A 1 104 ? 27.168 -7.951  -20.196 1.00 36.58 ? 104 LYS A O     1 
ATOM   836  C  CB    . LYS A 1 104 ? 25.476 -5.740  -18.988 1.00 26.40 ? 104 LYS A CB    1 
ATOM   837  C  CG    . LYS A 1 104 ? 24.801 -4.381  -19.114 1.00 24.45 ? 104 LYS A CG    1 
ATOM   838  C  CD    . LYS A 1 104 ? 25.470 -3.497  -20.166 1.00 24.72 ? 104 LYS A CD    1 
ATOM   839  C  CE    . LYS A 1 104 ? 26.781 -2.922  -19.694 1.00 28.04 ? 104 LYS A CE    1 
ATOM   840  N  NZ    . LYS A 1 104 ? 27.401 -2.083  -20.754 1.00 25.16 ? 104 LYS A NZ    1 
ATOM   841  N  N     . ASP A 1 105 ? 25.258 -9.080  -19.752 1.00 30.10 ? 105 ASP A N     1 
ATOM   842  C  CA    . ASP A 1 105 ? 25.906 -10.389 -19.650 1.00 37.54 ? 105 ASP A CA    1 
ATOM   843  C  C     . ASP A 1 105 ? 26.959 -10.394 -18.539 1.00 40.13 ? 105 ASP A C     1 
ATOM   844  O  O     . ASP A 1 105 ? 28.060 -10.928 -18.697 1.00 42.27 ? 105 ASP A O     1 
ATOM   845  C  CB    . ASP A 1 105 ? 26.508 -10.792 -21.004 1.00 35.64 ? 105 ASP A CB    1 
ATOM   846  C  CG    . ASP A 1 105 ? 26.919 -12.255 -21.066 1.00 49.13 ? 105 ASP A CG    1 
ATOM   847  O  OD1   . ASP A 1 105 ? 27.947 -12.539 -21.723 1.00 48.55 ? 105 ASP A OD1   1 
ATOM   848  O  OD2   . ASP A 1 105 ? 26.266 -13.101 -20.415 1.00 53.08 ? 105 ASP A OD2   1 
ATOM   849  N  N     . SER A 1 106 ? 26.625 -9.787  -17.404 1.00 35.50 ? 106 SER A N     1 
ATOM   850  C  CA    . SER A 1 106 ? 27.596 -9.609  -16.334 1.00 41.18 ? 106 SER A CA    1 
ATOM   851  C  C     . SER A 1 106 ? 26.862 -9.281  -15.044 1.00 40.26 ? 106 SER A C     1 
ATOM   852  O  O     . SER A 1 106 ? 25.803 -8.646  -15.065 1.00 41.95 ? 106 SER A O     1 
ATOM   853  C  CB    . SER A 1 106 ? 28.600 -8.500  -16.668 1.00 42.73 ? 106 SER A CB    1 
ATOM   854  O  OG    . SER A 1 106 ? 29.484 -8.267  -15.585 1.00 45.16 ? 106 SER A OG    1 
ATOM   855  N  N     . GLU A 1 107 ? 27.412 -9.750  -13.925 1.00 43.51 ? 107 GLU A N     1 
ATOM   856  C  CA    . GLU A 1 107 ? 26.902 -9.365  -12.614 1.00 45.09 ? 107 GLU A CA    1 
ATOM   857  C  C     . GLU A 1 107 ? 27.619 -8.150  -12.046 1.00 45.79 ? 107 GLU A C     1 
ATOM   858  O  O     . GLU A 1 107 ? 27.233 -7.668  -10.976 1.00 53.09 ? 107 GLU A O     1 
ATOM   859  C  CB    . GLU A 1 107 ? 27.015 -10.523 -11.610 1.00 49.49 ? 107 GLU A CB    1 
ATOM   860  C  CG    . GLU A 1 107 ? 26.059 -11.686 -11.834 1.00 52.24 ? 107 GLU A CG    1 
ATOM   861  C  CD    . GLU A 1 107 ? 26.636 -12.749 -12.751 1.00 61.36 ? 107 GLU A CD    1 
ATOM   862  O  OE1   . GLU A 1 107 ? 27.880 -12.783 -12.915 1.00 59.79 ? 107 GLU A OE1   1 
ATOM   863  O  OE2   . GLU A 1 107 ? 25.844 -13.550 -13.306 1.00 59.38 ? 107 GLU A OE2   1 
ATOM   864  N  N     . ASP A 1 108 ? 28.630 -7.631  -12.739 1.00 41.22 ? 108 ASP A N     1 
ATOM   865  C  CA    . ASP A 1 108 ? 29.453 -6.536  -12.230 1.00 47.04 ? 108 ASP A CA    1 
ATOM   866  C  C     . ASP A 1 108 ? 29.276 -5.342  -13.170 1.00 40.74 ? 108 ASP A C     1 
ATOM   867  O  O     . ASP A 1 108 ? 30.142 -5.027  -13.992 1.00 44.46 ? 108 ASP A O     1 
ATOM   868  C  CB    . ASP A 1 108 ? 30.924 -6.994  -12.112 1.00 49.95 ? 108 ASP A CB    1 
ATOM   869  C  CG    . ASP A 1 108 ? 31.733 -6.129  -11.168 1.00 58.46 ? 108 ASP A CG    1 
ATOM   870  O  OD1   . ASP A 1 108 ? 31.659 -6.372  -9.940  1.00 65.43 ? 108 ASP A OD1   1 
ATOM   871  O  OD2   . ASP A 1 108 ? 32.452 -5.222  -11.642 1.00 61.60 ? 108 ASP A OD2   1 
ATOM   872  N  N     . VAL A 1 109 ? 28.153 -4.660  -13.015 1.00 30.26 ? 109 VAL A N     1 
ATOM   873  C  CA    . VAL A 1 109 ? 27.794 -3.501  -13.823 1.00 22.90 ? 109 VAL A CA    1 
ATOM   874  C  C     . VAL A 1 109 ? 27.658 -2.323  -12.858 1.00 19.55 ? 109 VAL A C     1 
ATOM   875  O  O     . VAL A 1 109 ? 27.000 -2.467  -11.828 1.00 19.47 ? 109 VAL A O     1 
ATOM   876  C  CB    . VAL A 1 109 ? 26.486 -3.706  -14.600 1.00 24.84 ? 109 VAL A CB    1 
ATOM   877  C  CG1   . VAL A 1 109 ? 26.140 -2.476  -15.445 1.00 25.66 ? 109 VAL A CG1   1 
ATOM   878  C  CG2   . VAL A 1 109 ? 26.561 -4.963  -15.470 1.00 29.93 ? 109 VAL A CG2   1 
ATOM   879  N  N     . PRO A 1 110 ? 28.271 -1.176  -13.137 1.00 20.12 ? 110 PRO A N     1 
ATOM   880  C  CA    . PRO A 1 110 ? 28.123 -0.032  -12.231 1.00 20.51 ? 110 PRO A CA    1 
ATOM   881  C  C     . PRO A 1 110 ? 26.663 0.384   -12.089 1.00 21.09 ? 110 PRO A C     1 
ATOM   882  O  O     . PRO A 1 110 ? 25.967 0.638   -13.086 1.00 19.26 ? 110 PRO A O     1 
ATOM   883  C  CB    . PRO A 1 110 ? 28.964 1.062   -12.903 1.00 21.65 ? 110 PRO A CB    1 
ATOM   884  C  CG    . PRO A 1 110 ? 29.982 0.295   -13.701 1.00 23.73 ? 110 PRO A CG    1 
ATOM   885  C  CD    . PRO A 1 110 ? 29.233 -0.906  -14.219 1.00 24.17 ? 110 PRO A CD    1 
ATOM   886  N  N     . MET A 1 111 ? 26.199 0.444   -10.833 1.00 21.65 ? 111 MET A N     1 
ATOM   887  C  CA    . MET A 1 111 ? 24.829 0.840   -10.519 1.00 18.26 ? 111 MET A CA    1 
ATOM   888  C  C     . MET A 1 111 ? 24.783 1.578   -9.195  1.00 23.67 ? 111 MET A C     1 
ATOM   889  O  O     . MET A 1 111 ? 25.632 1.381   -8.316  1.00 21.68 ? 111 MET A O     1 
ATOM   890  C  CB    . MET A 1 111 ? 23.844 -0.336  -10.415 1.00 21.94 ? 111 MET A CB    1 
ATOM   891  C  CG    . MET A 1 111 ? 23.854 -1.326  -11.541 1.00 23.33 ? 111 MET A CG    1 
ATOM   892  S  SD    . MET A 1 111 ? 22.652 -2.645  -11.209 1.00 26.78 ? 111 MET A SD    1 
ATOM   893  C  CE    . MET A 1 111 ? 23.346 -3.947  -12.192 1.00 29.64 ? 111 MET A CE    1 
ATOM   894  N  N     . VAL A 1 112 ? 23.773 2.433   -9.062  1.00 18.47 ? 112 VAL A N     1 
ATOM   895  C  CA    . VAL A 1 112 ? 23.512 3.142   -7.811  1.00 17.82 ? 112 VAL A CA    1 
ATOM   896  C  C     . VAL A 1 112 ? 22.019 3.055   -7.545  1.00 19.27 ? 112 VAL A C     1 
ATOM   897  O  O     . VAL A 1 112 ? 21.214 3.274   -8.457  1.00 17.20 ? 112 VAL A O     1 
ATOM   898  C  CB    . VAL A 1 112 ? 23.983 4.614   -7.868  1.00 19.67 ? 112 VAL A CB    1 
ATOM   899  C  CG1   . VAL A 1 112 ? 23.436 5.402   -6.680  1.00 23.72 ? 112 VAL A CG1   1 
ATOM   900  C  CG2   . VAL A 1 112 ? 25.508 4.675   -7.908  1.00 21.82 ? 112 VAL A CG2   1 
ATOM   901  N  N     . LEU A 1 113 ? 21.640 2.693   -6.319  1.00 17.47 ? 113 LEU A N     1 
ATOM   902  C  CA    . LEU A 1 113 ? 20.231 2.657   -5.935  1.00 17.45 ? 113 LEU A CA    1 
ATOM   903  C  C     . LEU A 1 113 ? 19.815 4.012   -5.361  1.00 18.53 ? 113 LEU A C     1 
ATOM   904  O  O     . LEU A 1 113 ? 20.431 4.507   -4.413  1.00 17.97 ? 113 LEU A O     1 
ATOM   905  C  CB    . LEU A 1 113 ? 19.987 1.536   -4.916  1.00 17.25 ? 113 LEU A CB    1 
ATOM   906  C  CG    . LEU A 1 113 ? 18.559 1.385   -4.384  1.00 17.47 ? 113 LEU A CG    1 
ATOM   907  C  CD1   . LEU A 1 113 ? 17.612 1.013   -5.531  1.00 21.65 ? 113 LEU A CD1   1 
ATOM   908  C  CD2   . LEU A 1 113 ? 18.472 0.351   -3.235  1.00 21.17 ? 113 LEU A CD2   1 
ATOM   909  N  N     . VAL A 1 114 ? 18.760 4.602   -5.922  1.00 17.38 ? 114 VAL A N     1 
ATOM   910  C  CA    . VAL A 1 114 ? 18.301 5.940   -5.551  1.00 17.79 ? 114 VAL A CA    1 
ATOM   911  C  C     . VAL A 1 114 ? 16.892 5.837   -4.999  1.00 18.50 ? 114 VAL A C     1 
ATOM   912  O  O     . VAL A 1 114 ? 15.979 5.392   -5.708  1.00 18.09 ? 114 VAL A O     1 
ATOM   913  C  CB    . VAL A 1 114 ? 18.333 6.906   -6.747  1.00 20.72 ? 114 VAL A CB    1 
ATOM   914  C  CG1   . VAL A 1 114 ? 17.781 8.276   -6.353  1.00 21.24 ? 114 VAL A CG1   1 
ATOM   915  C  CG2   . VAL A 1 114 ? 19.770 6.994   -7.296  1.00 22.84 ? 114 VAL A CG2   1 
ATOM   916  N  N     . GLY A 1 115 ? 16.709 6.300   -3.765  1.00 16.15 ? 115 GLY A N     1 
ATOM   917  C  CA    . GLY A 1 115 ? 15.361 6.496   -3.254  1.00 20.72 ? 115 GLY A CA    1 
ATOM   918  C  C     . GLY A 1 115 ? 14.957 7.951   -3.340  1.00 22.62 ? 115 GLY A C     1 
ATOM   919  O  O     . GLY A 1 115 ? 15.433 8.777   -2.550  1.00 22.67 ? 115 GLY A O     1 
ATOM   920  N  N     . ASN A 1 116 ? 14.078 8.281   -4.286  1.00 19.27 ? 116 ASN A N     1 
ATOM   921  C  CA    . ASN A 1 116 ? 13.704 9.661   -4.535  1.00 19.15 ? 116 ASN A CA    1 
ATOM   922  C  C     . ASN A 1 116 ? 12.445 10.060  -3.762  1.00 21.63 ? 116 ASN A C     1 
ATOM   923  O  O     . ASN A 1 116 ? 11.700 9.217   -3.245  1.00 20.85 ? 116 ASN A O     1 
ATOM   924  C  CB    . ASN A 1 116 ? 13.502 9.872   -6.032  1.00 17.57 ? 116 ASN A CB    1 
ATOM   925  C  CG    . ASN A 1 116 ? 13.383 11.310  -6.404  1.00 19.97 ? 116 ASN A CG    1 
ATOM   926  O  OD1   . ASN A 1 116 ? 14.139 12.166  -5.926  1.00 22.35 ? 116 ASN A OD1   1 
ATOM   927  N  ND2   . ASN A 1 116 ? 12.423 11.604  -7.274  1.00 20.54 ? 116 ASN A ND2   1 
ATOM   928  N  N     . LYS A 1 117 ? 12.209 11.383  -3.729  1.00 18.88 ? 117 LYS A N     1 
ATOM   929  C  CA    . LYS A 1 117 ? 11.088 12.037  -3.033  1.00 20.56 ? 117 LYS A CA    1 
ATOM   930  C  C     . LYS A 1 117 ? 11.277 12.037  -1.511  1.00 25.23 ? 117 LYS A C     1 
ATOM   931  O  O     . LYS A 1 117 ? 10.314 11.880  -0.755  1.00 23.94 ? 117 LYS A O     1 
ATOM   932  C  CB    . LYS A 1 117 ? 9.737  11.421  -3.408  1.00 21.11 ? 117 LYS A CB    1 
ATOM   933  C  CG    . LYS A 1 117 ? 9.536  11.252  -4.918  1.00 20.32 ? 117 LYS A CG    1 
ATOM   934  C  CD    . LYS A 1 117 ? 8.061  11.035  -5.244  1.00 20.81 ? 117 LYS A CD    1 
ATOM   935  C  CE    . LYS A 1 117 ? 7.880  10.837  -6.744  1.00 22.68 ? 117 LYS A CE    1 
ATOM   936  N  NZ    . LYS A 1 117 ? 6.462  10.694  -7.106  1.00 23.37 ? 117 LYS A NZ    1 
ATOM   937  N  N     . SER A 1 118 ? 12.516 12.254  -1.058  1.00 22.80 ? 118 SER A N     1 
ATOM   938  C  CA    A SER A 1 118 ? 12.802 12.294  0.372   0.75 29.04 ? 118 SER A CA    1 
ATOM   939  C  CA    B SER A 1 118 ? 12.763 12.271  0.378   0.25 29.78 ? 118 SER A CA    1 
ATOM   940  C  C     . SER A 1 118 ? 12.175 13.498  1.059   1.00 31.44 ? 118 SER A C     1 
ATOM   941  O  O     . SER A 1 118 ? 12.121 13.526  2.293   1.00 32.98 ? 118 SER A O     1 
ATOM   942  C  CB    A SER A 1 118 ? 14.309 12.326  0.618   0.75 25.51 ? 118 SER A CB    1 
ATOM   943  C  CB    B SER A 1 118 ? 14.262 12.188  0.664   0.25 24.53 ? 118 SER A CB    1 
ATOM   944  O  OG    A SER A 1 118 ? 14.854 13.545  0.139   0.75 26.45 ? 118 SER A OG    1 
ATOM   945  O  OG    B SER A 1 118 ? 14.762 10.907  0.327   0.25 30.07 ? 118 SER A OG    1 
ATOM   946  N  N     . ASP A 1 119 ? 11.731 14.497  0.296   1.00 28.18 ? 119 ASP A N     1 
ATOM   947  C  CA    . ASP A 1 119 ? 11.045 15.648  0.875   1.00 28.14 ? 119 ASP A CA    1 
ATOM   948  C  C     . ASP A 1 119 ? 9.656  15.301  1.396   1.00 37.11 ? 119 ASP A C     1 
ATOM   949  O  O     . ASP A 1 119 ? 9.037  16.136  2.064   1.00 36.74 ? 119 ASP A O     1 
ATOM   950  C  CB    . ASP A 1 119 ? 10.921 16.760  -0.159  1.00 25.65 ? 119 ASP A CB    1 
ATOM   951  C  CG    . ASP A 1 119 ? 10.212 16.296  -1.412  1.00 30.74 ? 119 ASP A CG    1 
ATOM   952  O  OD1   . ASP A 1 119 ? 10.798 15.471  -2.141  1.00 25.26 ? 119 ASP A OD1   1 
ATOM   953  O  OD2   . ASP A 1 119 ? 9.065  16.726  -1.658  1.00 29.69 ? 119 ASP A OD2   1 
ATOM   954  N  N     . LEU A 1 120 ? 9.150  14.103  1.113   1.00 30.62 ? 120 LEU A N     1 
ATOM   955  C  CA    . LEU A 1 120 ? 7.782  13.793  1.519   1.00 34.61 ? 120 LEU A CA    1 
ATOM   956  C  C     . LEU A 1 120 ? 7.764  13.154  2.905   1.00 42.94 ? 120 LEU A C     1 
ATOM   957  O  O     . LEU A 1 120 ? 8.691  12.421  3.261   1.00 46.53 ? 120 LEU A O     1 
ATOM   958  C  CB    . LEU A 1 120 ? 7.128  12.838  0.525   1.00 34.75 ? 120 LEU A CB    1 
ATOM   959  C  CG    . LEU A 1 120 ? 6.900  13.369  -0.886  1.00 30.47 ? 120 LEU A CG    1 
ATOM   960  C  CD1   . LEU A 1 120 ? 6.300  12.268  -1.751  1.00 34.05 ? 120 LEU A CD1   1 
ATOM   961  C  CD2   . LEU A 1 120 ? 5.995  14.598  -0.868  1.00 34.02 ? 120 LEU A CD2   1 
ATOM   962  N  N     . PRO A 1 121 ? 6.733  13.425  3.712   1.00 45.40 ? 121 PRO A N     1 
ATOM   963  C  CA    . PRO A 1 121 ? 6.610  12.735  5.005   1.00 45.70 ? 121 PRO A CA    1 
ATOM   964  C  C     . PRO A 1 121 ? 5.935  11.372  4.920   1.00 43.95 ? 121 PRO A C     1 
ATOM   965  O  O     . PRO A 1 121 ? 6.052  10.586  5.868   1.00 51.99 ? 121 PRO A O     1 
ATOM   966  C  CB    . PRO A 1 121 ? 5.767  13.713  5.830   1.00 49.61 ? 121 PRO A CB    1 
ATOM   967  C  CG    . PRO A 1 121 ? 4.866  14.333  4.804   1.00 47.71 ? 121 PRO A CG    1 
ATOM   968  C  CD    . PRO A 1 121 ? 5.730  14.495  3.561   1.00 45.62 ? 121 PRO A CD    1 
ATOM   969  N  N     . SER A 1 122 ? 5.256  11.056  3.818   1.00 47.46 ? 122 SER A N     1 
ATOM   970  C  CA    . SER A 1 122 ? 4.439  9.846   3.723   1.00 47.73 ? 122 SER A CA    1 
ATOM   971  C  C     . SER A 1 122 ? 5.237  8.601   3.337   1.00 46.34 ? 122 SER A C     1 
ATOM   972  O  O     . SER A 1 122 ? 4.832  7.868   2.426   1.00 44.56 ? 122 SER A O     1 
ATOM   973  C  CB    . SER A 1 122 ? 3.313  10.051  2.702   1.00 49.01 ? 122 SER A CB    1 
ATOM   974  O  OG    . SER A 1 122 ? 3.765  10.785  1.567   1.00 49.92 ? 122 SER A OG    1 
ATOM   975  N  N     . ARG A 1 123 ? 6.340  8.331   4.034   1.00 39.22 ? 123 ARG A N     1 
ATOM   976  C  CA    . ARG A 1 123 ? 7.266  7.278   3.626   1.00 33.75 ? 123 ARG A CA    1 
ATOM   977  C  C     . ARG A 1 123 ? 6.687  5.880   3.849   1.00 37.08 ? 123 ARG A C     1 
ATOM   978  O  O     . ARG A 1 123 ? 6.143  5.587   4.916   1.00 35.69 ? 123 ARG A O     1 
ATOM   979  C  CB    . ARG A 1 123 ? 8.564  7.417   4.406   1.00 35.09 ? 123 ARG A CB    1 
ATOM   980  C  CG    . ARG A 1 123 ? 9.451  6.234   4.259   1.00 36.78 ? 123 ARG A CG    1 
ATOM   981  C  CD    . ARG A 1 123 ? 10.706 6.368   5.074   1.00 37.17 ? 123 ARG A CD    1 
ATOM   982  N  NE    . ARG A 1 123 ? 11.571 7.450   4.633   1.00 42.30 ? 123 ARG A NE    1 
ATOM   983  C  CZ    . ARG A 1 123 ? 12.685 7.280   3.932   1.00 40.53 ? 123 ARG A CZ    1 
ATOM   984  N  NH1   . ARG A 1 123 ? 13.029 6.092   3.449   1.00 34.63 ? 123 ARG A NH1   1 
ATOM   985  N  NH2   . ARG A 1 123 ? 13.487 8.322   3.732   1.00 36.88 ? 123 ARG A NH2   1 
ATOM   986  N  N     . THR A 1 124 ? 6.821  5.001   2.842   1.00 27.51 ? 124 THR A N     1 
ATOM   987  C  CA    . THR A 1 124 ? 6.420  3.608   2.973   1.00 25.92 ? 124 THR A CA    1 
ATOM   988  C  C     . THR A 1 124 ? 7.574  2.621   2.836   1.00 26.62 ? 124 THR A C     1 
ATOM   989  O  O     . THR A 1 124 ? 7.434  1.465   3.250   1.00 28.98 ? 124 THR A O     1 
ATOM   990  C  CB    . THR A 1 124 ? 5.320  3.268   1.947   1.00 28.37 ? 124 THR A CB    1 
ATOM   991  O  OG1   . THR A 1 124 ? 5.845  3.362   0.619   1.00 26.42 ? 124 THR A OG1   1 
ATOM   992  C  CG2   . THR A 1 124 ? 4.159  4.224   2.075   1.00 30.36 ? 124 THR A CG2   1 
ATOM   993  N  N     . VAL A 1 125 ? 8.721  3.040   2.325   1.00 26.87 ? 125 VAL A N     1 
ATOM   994  C  CA    . VAL A 1 125 ? 9.882  2.171   2.214   1.00 27.88 ? 125 VAL A CA    1 
ATOM   995  C  C     . VAL A 1 125 ? 10.887 2.608   3.263   1.00 30.62 ? 125 VAL A C     1 
ATOM   996  O  O     . VAL A 1 125 ? 11.378 3.744   3.228   1.00 30.65 ? 125 VAL A O     1 
ATOM   997  C  CB    . VAL A 1 125 ? 10.502 2.199   0.806   1.00 25.78 ? 125 VAL A CB    1 
ATOM   998  C  CG1   . VAL A 1 125 ? 11.696 1.248   0.741   1.00 25.20 ? 125 VAL A CG1   1 
ATOM   999  C  CG2   . VAL A 1 125 ? 9.452  1.828   -0.240  1.00 23.64 ? 125 VAL A CG2   1 
ATOM   1000 N  N     . ASP A 1 126 ? 11.174 1.711   4.199   1.00 28.91 ? 126 ASP A N     1 
ATOM   1001 C  CA    . ASP A 1 126 ? 12.108 2.000   5.276   1.00 36.82 ? 126 ASP A CA    1 
ATOM   1002 C  C     . ASP A 1 126 ? 13.507 2.230   4.717   1.00 33.84 ? 126 ASP A C     1 
ATOM   1003 O  O     . ASP A 1 126 ? 13.944 1.524   3.809   1.00 34.63 ? 126 ASP A O     1 
ATOM   1004 C  CB    . ASP A 1 126 ? 12.164 0.800   6.227   1.00 38.06 ? 126 ASP A CB    1 
ATOM   1005 C  CG    . ASP A 1 126 ? 11.517 1.067   7.554   1.00 48.18 ? 126 ASP A CG    1 
ATOM   1006 O  OD1   . ASP A 1 126 ? 10.629 1.950   7.620   1.00 51.17 ? 126 ASP A OD1   1 
ATOM   1007 O  OD2   . ASP A 1 126 ? 11.916 0.392   8.533   1.00 52.00 ? 126 ASP A OD2   1 
ATOM   1008 N  N     . THR A 1 127 ? 14.233 3.191   5.297   1.00 33.16 ? 127 THR A N     1 
ATOM   1009 C  CA    . THR A 1 127 ? 15.622 3.381   4.890   1.00 31.33 ? 127 THR A CA    1 
ATOM   1010 C  C     . THR A 1 127 ? 16.453 2.131   5.150   1.00 31.82 ? 127 THR A C     1 
ATOM   1011 O  O     . THR A 1 127 ? 17.354 1.805   4.368   1.00 28.56 ? 127 THR A O     1 
ATOM   1012 C  CB    . THR A 1 127 ? 16.237 4.587   5.596   1.00 35.15 ? 127 THR A CB    1 
ATOM   1013 O  OG1   . THR A 1 127 ? 15.453 5.749   5.312   1.00 45.19 ? 127 THR A OG1   1 
ATOM   1014 C  CG2   . THR A 1 127 ? 17.624 4.829   5.094   1.00 34.16 ? 127 THR A CG2   1 
ATOM   1015 N  N     . LYS A 1 128 ? 16.172 1.409   6.243   1.00 28.18 ? 128 LYS A N     1 
ATOM   1016 C  CA    . LYS A 1 128 ? 16.960 0.207   6.498   1.00 29.99 ? 128 LYS A CA    1 
ATOM   1017 C  C     . LYS A 1 128 ? 16.664 -0.860  5.451   1.00 25.66 ? 128 LYS A C     1 
ATOM   1018 O  O     . LYS A 1 128 ? 17.585 -1.528  4.973   1.00 27.73 ? 128 LYS A O     1 
ATOM   1019 C  CB    . LYS A 1 128 ? 16.724 -0.342  7.912   1.00 32.94 ? 128 LYS A CB    1 
ATOM   1020 C  CG    . LYS A 1 128 ? 17.348 -1.732  8.092   1.00 33.82 ? 128 LYS A CG    1 
ATOM   1021 C  CD    . LYS A 1 128 ? 18.009 -1.937  9.430   1.00 36.36 ? 128 LYS A CD    1 
ATOM   1022 C  CE    . LYS A 1 128 ? 18.903 -3.182  9.419   1.00 33.68 ? 128 LYS A CE    1 
ATOM   1023 N  NZ    . LYS A 1 128 ? 18.242 -4.401  8.883   1.00 36.04 ? 128 LYS A NZ    1 
ATOM   1024 N  N     . GLN A 1 129 ? 15.385 -1.030  5.081   1.00 27.43 ? 129 GLN A N     1 
ATOM   1025 C  CA    . GLN A 1 129 ? 15.017 -1.977  4.026   1.00 27.21 ? 129 GLN A CA    1 
ATOM   1026 C  C     . GLN A 1 129 ? 15.810 -1.704  2.746   1.00 21.90 ? 129 GLN A C     1 
ATOM   1027 O  O     . GLN A 1 129 ? 16.419 -2.611  2.143   1.00 26.87 ? 129 GLN A O     1 
ATOM   1028 C  CB    . GLN A 1 129 ? 13.512 -1.880  3.747   1.00 32.16 ? 129 GLN A CB    1 
ATOM   1029 C  CG    . GLN A 1 129 ? 12.931 -3.092  3.048   1.00 46.13 ? 129 GLN A CG    1 
ATOM   1030 C  CD    . GLN A 1 129 ? 11.407 -3.074  3.029   1.00 50.93 ? 129 GLN A CD    1 
ATOM   1031 O  OE1   . GLN A 1 129 ? 10.791 -2.023  3.260   1.00 51.42 ? 129 GLN A OE1   1 
ATOM   1032 N  NE2   . GLN A 1 129 ? 10.792 -4.218  2.718   1.00 49.12 ? 129 GLN A NE2   1 
ATOM   1033 N  N     . ALA A 1 130 ? 15.823 -0.439  2.332   1.00 26.93 ? 130 ALA A N     1 
ATOM   1034 C  CA    . ALA A 1 130 ? 16.482 -0.057  1.093   1.00 23.11 ? 130 ALA A CA    1 
ATOM   1035 C  C     . ALA A 1 130 ? 17.987 -0.258  1.196   1.00 23.46 ? 130 ALA A C     1 
ATOM   1036 O  O     . ALA A 1 130 ? 18.618 -0.794  0.275   1.00 22.21 ? 130 ALA A O     1 
ATOM   1037 C  CB    . ALA A 1 130 ? 16.142 1.395   0.772   1.00 24.29 ? 130 ALA A CB    1 
ATOM   1038 N  N     . GLN A 1 131 ? 18.585 0.182   2.314   1.00 21.49 ? 131 GLN A N     1 
ATOM   1039 C  CA    . GLN A 1 131 ? 20.019 -0.006  2.512   1.00 21.80 ? 131 GLN A CA    1 
ATOM   1040 C  C     . GLN A 1 131 ? 20.397 -1.464  2.437   1.00 23.98 ? 131 GLN A C     1 
ATOM   1041 O  O     . GLN A 1 131 ? 21.436 -1.817  1.881   1.00 25.01 ? 131 GLN A O     1 
ATOM   1042 C  CB    . GLN A 1 131 ? 20.455 0.479   3.896   1.00 27.26 ? 131 GLN A CB    1 
ATOM   1043 C  CG    . GLN A 1 131 ? 20.655 1.902   4.137   1.00 40.58 ? 131 GLN A CG    1 
ATOM   1044 C  CD    . GLN A 1 131 ? 20.591 2.133   5.631   1.00 34.11 ? 131 GLN A CD    1 
ATOM   1045 O  OE1   . GLN A 1 131 ? 19.879 3.021   6.088   1.00 45.69 ? 131 GLN A OE1   1 
ATOM   1046 N  NE2   . GLN A 1 131 ? 21.258 1.262   6.409   1.00 29.94 ? 131 GLN A NE2   1 
ATOM   1047 N  N     . ASP A 1 132 ? 19.599 -2.319  3.073   1.00 26.51 ? 132 ASP A N     1 
ATOM   1048 C  CA    . ASP A 1 132 ? 19.915 -3.738  3.096   1.00 25.09 ? 132 ASP A CA    1 
ATOM   1049 C  C     . ASP A 1 132 ? 19.886 -4.320  1.693   1.00 23.81 ? 132 ASP A C     1 
ATOM   1050 O  O     . ASP A 1 132 ? 20.710 -5.175  1.354   1.00 26.66 ? 132 ASP A O     1 
ATOM   1051 C  CB    . ASP A 1 132 ? 18.958 -4.478  4.024   1.00 26.30 ? 132 ASP A CB    1 
ATOM   1052 C  CG    . ASP A 1 132 ? 19.262 -4.226  5.496   1.00 32.84 ? 132 ASP A CG    1 
ATOM   1053 O  OD1   . ASP A 1 132 ? 20.337 -3.643  5.798   1.00 30.59 ? 132 ASP A OD1   1 
ATOM   1054 O  OD2   . ASP A 1 132 ? 18.423 -4.599  6.334   1.00 31.34 ? 132 ASP A OD2   1 
ATOM   1055 N  N     . LEU A 1 133 ? 18.897 -3.930  0.891   1.00 24.66 ? 133 LEU A N     1 
ATOM   1056 C  CA    . LEU A 1 133 ? 18.899 -4.363  -0.511  1.00 24.57 ? 133 LEU A CA    1 
ATOM   1057 C  C     . LEU A 1 133 ? 20.189 -3.941  -1.214  1.00 23.74 ? 133 LEU A C     1 
ATOM   1058 O  O     . LEU A 1 133 ? 20.853 -4.755  -1.868  1.00 24.14 ? 133 LEU A O     1 
ATOM   1059 C  CB    . LEU A 1 133 ? 17.683 -3.795  -1.246  1.00 21.80 ? 133 LEU A CB    1 
ATOM   1060 C  CG    . LEU A 1 133 ? 17.514 -4.345  -2.669  1.00 25.59 ? 133 LEU A CG    1 
ATOM   1061 C  CD1   . LEU A 1 133 ? 17.314 -5.861  -2.622  1.00 30.34 ? 133 LEU A CD1   1 
ATOM   1062 C  CD2   . LEU A 1 133 ? 16.352 -3.679  -3.368  1.00 26.98 ? 133 LEU A CD2   1 
ATOM   1063 N  N     . ALA A 1 134 ? 20.559 -2.658  -1.088  1.00 23.19 ? 134 ALA A N     1 
ATOM   1064 C  CA    . ALA A 1 134 ? 21.781 -2.170  -1.732  1.00 21.20 ? 134 ALA A CA    1 
ATOM   1065 C  C     . ALA A 1 134 ? 23.022 -2.912  -1.231  1.00 22.74 ? 134 ALA A C     1 
ATOM   1066 O  O     . ALA A 1 134 ? 23.962 -3.152  -1.994  1.00 23.11 ? 134 ALA A O     1 
ATOM   1067 C  CB    . ALA A 1 134 ? 21.932 -0.661  -1.507  1.00 22.43 ? 134 ALA A CB    1 
ATOM   1068 N  N     . ARG A 1 135 ? 23.063 -3.254  0.060   1.00 23.56 ? 135 ARG A N     1 
ATOM   1069 C  CA    . ARG A 1 135 ? 24.215 -3.997  0.581   1.00 23.95 ? 135 ARG A CA    1 
ATOM   1070 C  C     . ARG A 1 135 ? 24.260 -5.415  0.012   1.00 20.97 ? 135 ARG A C     1 
ATOM   1071 O  O     . ARG A 1 135 ? 25.341 -5.940  -0.283  1.00 24.91 ? 135 ARG A O     1 
ATOM   1072 C  CB    . ARG A 1 135 ? 24.190 -4.024  2.114   1.00 25.64 ? 135 ARG A CB    1 
ATOM   1073 C  CG    . ARG A 1 135 ? 24.361 -2.638  2.742   1.00 26.01 ? 135 ARG A CG    1 
ATOM   1074 C  CD    . ARG A 1 135 ? 24.352 -2.646  4.269   1.00 28.64 ? 135 ARG A CD    1 
ATOM   1075 N  NE    . ARG A 1 135 ? 24.429 -1.274  4.769   1.00 29.51 ? 135 ARG A NE    1 
ATOM   1076 C  CZ    . ARG A 1 135 ? 24.741 -0.943  6.016   1.00 27.75 ? 135 ARG A CZ    1 
ATOM   1077 N  NH1   . ARG A 1 135 ? 25.008 -1.864  6.926   1.00 28.50 ? 135 ARG A NH1   1 
ATOM   1078 N  NH2   . ARG A 1 135 ? 24.820 0.346   6.345   1.00 26.22 ? 135 ARG A NH2   1 
ATOM   1079 N  N     . SER A 1 136 ? 23.101 -6.057  -0.151  1.00 25.93 ? 136 SER A N     1 
ATOM   1080 C  CA    . SER A 1 136 ? 23.111 -7.375  -0.786  1.00 26.90 ? 136 SER A CA    1 
ATOM   1081 C  C     . SER A 1 136 ? 23.539 -7.287  -2.251  1.00 27.39 ? 136 SER A C     1 
ATOM   1082 O  O     . SER A 1 136 ? 24.202 -8.202  -2.762  1.00 30.17 ? 136 SER A O     1 
ATOM   1083 C  CB    . SER A 1 136 ? 21.743 -8.041  -0.649  1.00 30.65 ? 136 SER A CB    1 
ATOM   1084 O  OG    . SER A 1 136 ? 20.794 -7.422  -1.484  1.00 34.12 ? 136 SER A OG    1 
ATOM   1085 N  N     . TYR A 1 137 ? 23.198 -6.193  -2.934  1.00 25.70 ? 137 TYR A N     1 
ATOM   1086 C  CA    . TYR A 1 137 ? 23.679 -5.971  -4.295  1.00 21.17 ? 137 TYR A CA    1 
ATOM   1087 C  C     . TYR A 1 137 ? 25.125 -5.497  -4.356  1.00 27.42 ? 137 TYR A C     1 
ATOM   1088 O  O     . TYR A 1 137 ? 25.734 -5.560  -5.432  1.00 29.03 ? 137 TYR A O     1 
ATOM   1089 C  CB    . TYR A 1 137 ? 22.816 -4.923  -5.009  1.00 25.01 ? 137 TYR A CB    1 
ATOM   1090 C  CG    . TYR A 1 137 ? 21.384 -5.306  -5.313  1.00 25.81 ? 137 TYR A CG    1 
ATOM   1091 C  CD1   . TYR A 1 137 ? 20.939 -6.624  -5.238  1.00 28.97 ? 137 TYR A CD1   1 
ATOM   1092 C  CD2   . TYR A 1 137 ? 20.475 -4.326  -5.707  1.00 26.33 ? 137 TYR A CD2   1 
ATOM   1093 C  CE1   . TYR A 1 137 ? 19.605 -6.955  -5.551  1.00 25.91 ? 137 TYR A CE1   1 
ATOM   1094 C  CE2   . TYR A 1 137 ? 19.166 -4.646  -6.015  1.00 25.39 ? 137 TYR A CE2   1 
ATOM   1095 C  CZ    . TYR A 1 137 ? 18.739 -5.951  -5.939  1.00 30.61 ? 137 TYR A CZ    1 
ATOM   1096 O  OH    . TYR A 1 137 ? 17.421 -6.206  -6.262  1.00 30.70 ? 137 TYR A OH    1 
ATOM   1097 N  N     . GLY A 1 138 ? 25.672 -4.993  -3.250  1.00 25.85 ? 138 GLY A N     1 
ATOM   1098 C  CA    . GLY A 1 138 ? 27.015 -4.439  -3.246  1.00 23.56 ? 138 GLY A CA    1 
ATOM   1099 C  C     . GLY A 1 138 ? 27.164 -3.083  -3.916  1.00 25.15 ? 138 GLY A C     1 
ATOM   1100 O  O     . GLY A 1 138 ? 28.218 -2.810  -4.501  1.00 25.10 ? 138 GLY A O     1 
ATOM   1101 N  N     . ILE A 1 139 ? 26.150 -2.224  -3.851  1.00 22.44 ? 139 ILE A N     1 
ATOM   1102 C  CA    . ILE A 1 139 ? 26.178 -0.962  -4.594  1.00 19.93 ? 139 ILE A CA    1 
ATOM   1103 C  C     . ILE A 1 139 ? 25.794 0.163   -3.642  1.00 21.32 ? 139 ILE A C     1 
ATOM   1104 O  O     . ILE A 1 139 ? 25.193 -0.079  -2.586  1.00 23.38 ? 139 ILE A O     1 
ATOM   1105 C  CB    . ILE A 1 139 ? 25.207 -0.982  -5.800  1.00 23.72 ? 139 ILE A CB    1 
ATOM   1106 C  CG1   . ILE A 1 139 ? 23.775 -1.159  -5.308  1.00 20.72 ? 139 ILE A CG1   1 
ATOM   1107 C  CG2   . ILE A 1 139 ? 25.546 -2.091  -6.770  1.00 26.37 ? 139 ILE A CG2   1 
ATOM   1108 C  CD1   . ILE A 1 139 ? 22.699 -0.962  -6.409  1.00 22.04 ? 139 ILE A CD1   1 
ATOM   1109 N  N     . PRO A 1 140 ? 26.108 1.407   -4.000  1.00 22.50 ? 140 PRO A N     1 
ATOM   1110 C  CA    . PRO A 1 140 ? 25.729 2.534   -3.143  1.00 22.64 ? 140 PRO A CA    1 
ATOM   1111 C  C     . PRO A 1 140 ? 24.230 2.782   -3.147  1.00 21.73 ? 140 PRO A C     1 
ATOM   1112 O  O     . PRO A 1 140 ? 23.508 2.442   -4.088  1.00 23.02 ? 140 PRO A O     1 
ATOM   1113 C  CB    . PRO A 1 140 ? 26.476 3.722   -3.768  1.00 22.48 ? 140 PRO A CB    1 
ATOM   1114 C  CG    . PRO A 1 140 ? 27.564 3.116   -4.563  1.00 23.13 ? 140 PRO A CG    1 
ATOM   1115 C  CD    . PRO A 1 140 ? 27.032 1.818   -5.069  1.00 21.76 ? 140 PRO A CD    1 
ATOM   1116 N  N     . PHE A 1 141 ? 23.770 3.401   -2.058  1.00 21.61 ? 141 PHE A N     1 
ATOM   1117 C  CA    . PHE A 1 141 ? 22.380 3.790   -1.866  1.00 19.04 ? 141 PHE A CA    1 
ATOM   1118 C  C     . PHE A 1 141 ? 22.342 5.248   -1.437  1.00 26.16 ? 141 PHE A C     1 
ATOM   1119 O  O     . PHE A 1 141 ? 22.991 5.627   -0.452  1.00 24.27 ? 141 PHE A O     1 
ATOM   1120 C  CB    . PHE A 1 141 ? 21.689 2.929   -0.807  1.00 21.35 ? 141 PHE A CB    1 
ATOM   1121 C  CG    . PHE A 1 141 ? 20.342 3.447   -0.409  1.00 26.25 ? 141 PHE A CG    1 
ATOM   1122 C  CD1   . PHE A 1 141 ? 19.345 3.613   -1.355  1.00 24.87 ? 141 PHE A CD1   1 
ATOM   1123 C  CD2   . PHE A 1 141 ? 20.074 3.790   0.911   1.00 25.58 ? 141 PHE A CD2   1 
ATOM   1124 C  CE1   . PHE A 1 141 ? 18.099 4.109   -0.988  1.00 22.18 ? 141 PHE A CE1   1 
ATOM   1125 C  CE2   . PHE A 1 141 ? 18.828 4.280   1.284   1.00 25.69 ? 141 PHE A CE2   1 
ATOM   1126 C  CZ    . PHE A 1 141 ? 17.843 4.444   0.338   1.00 26.72 ? 141 PHE A CZ    1 
ATOM   1127 N  N     . ILE A 1 142 ? 21.581 6.058   -2.164  1.00 21.64 ? 142 ILE A N     1 
ATOM   1128 C  CA    . ILE A 1 142 ? 21.455 7.482   -1.874  1.00 23.16 ? 142 ILE A CA    1 
ATOM   1129 C  C     . ILE A 1 142 ? 19.988 7.876   -1.939  1.00 25.79 ? 142 ILE A C     1 
ATOM   1130 O  O     . ILE A 1 142 ? 19.275 7.485   -2.871  1.00 21.98 ? 142 ILE A O     1 
ATOM   1131 C  CB    . ILE A 1 142 ? 22.291 8.322   -2.857  1.00 22.22 ? 142 ILE A CB    1 
ATOM   1132 C  CG1   . ILE A 1 142 ? 23.749 7.856   -2.824  1.00 31.33 ? 142 ILE A CG1   1 
ATOM   1133 C  CG2   . ILE A 1 142 ? 22.161 9.827   -2.564  1.00 27.85 ? 142 ILE A CG2   1 
ATOM   1134 C  CD1   . ILE A 1 142 ? 24.596 8.467   -3.893  1.00 34.81 ? 142 ILE A CD1   1 
ATOM   1135 N  N     . GLU A 1 143 ? 19.530 8.652   -0.955  1.00 21.14 ? 143 GLU A N     1 
ATOM   1136 C  CA    . GLU A 1 143 ? 18.174 9.191   -0.984  1.00 20.97 ? 143 GLU A CA    1 
ATOM   1137 C  C     . GLU A 1 143 ? 18.239 10.608  -1.527  1.00 23.89 ? 143 GLU A C     1 
ATOM   1138 O  O     . GLU A 1 143 ? 19.128 11.378  -1.153  1.00 26.44 ? 143 GLU A O     1 
ATOM   1139 C  CB    . GLU A 1 143 ? 17.502 9.176   0.398   1.00 25.03 ? 143 GLU A CB    1 
ATOM   1140 C  CG    . GLU A 1 143 ? 17.334 7.787   0.993   1.00 27.46 ? 143 GLU A CG    1 
ATOM   1141 C  CD    . GLU A 1 143 ? 16.237 7.686   2.055   1.00 36.06 ? 143 GLU A CD    1 
ATOM   1142 O  OE1   . GLU A 1 143 ? 15.876 8.719   2.653   1.00 37.16 ? 143 GLU A OE1   1 
ATOM   1143 O  OE2   . GLU A 1 143 ? 15.766 6.552   2.325   1.00 39.66 ? 143 GLU A OE2   1 
ATOM   1144 N  N     . THR A 1 144 ? 17.307 10.946  -2.422  1.00 22.03 ? 144 THR A N     1 
ATOM   1145 C  CA    . THR A 1 144 ? 17.316 12.217  -3.140  1.00 16.67 ? 144 THR A CA    1 
ATOM   1146 C  C     . THR A 1 144 ? 15.959 12.897  -3.053  1.00 22.88 ? 144 THR A C     1 
ATOM   1147 O  O     . THR A 1 144 ? 14.936 12.276  -2.751  1.00 21.15 ? 144 THR A O     1 
ATOM   1148 C  CB    . THR A 1 144 ? 17.648 12.040  -4.632  1.00 22.68 ? 144 THR A CB    1 
ATOM   1149 O  OG1   . THR A 1 144 ? 16.619 11.240  -5.257  1.00 19.30 ? 144 THR A OG1   1 
ATOM   1150 C  CG2   . THR A 1 144 ? 19.018 11.378  -4.821  1.00 21.83 ? 144 THR A CG2   1 
ATOM   1151 N  N     . SER A 1 145 ? 15.969 14.189  -3.361  1.00 21.99 ? 145 SER A N     1 
ATOM   1152 C  CA    . SER A 1 145 ? 14.760 14.924  -3.702  1.00 22.35 ? 145 SER A CA    1 
ATOM   1153 C  C     . SER A 1 145 ? 15.061 15.757  -4.930  1.00 23.95 ? 145 SER A C     1 
ATOM   1154 O  O     . SER A 1 145 ? 15.873 16.687  -4.867  1.00 23.44 ? 145 SER A O     1 
ATOM   1155 C  CB    . SER A 1 145 ? 14.287 15.819  -2.548  1.00 24.23 ? 145 SER A CB    1 
ATOM   1156 O  OG    . SER A 1 145 ? 13.193 16.616  -2.972  1.00 22.63 ? 145 SER A OG    1 
ATOM   1157 N  N     . ALA A 1 146 ? 14.405 15.441  -6.052  1.00 20.01 ? 146 ALA A N     1 
ATOM   1158 C  CA    . ALA A 1 146 ? 14.518 16.328  -7.193  1.00 20.70 ? 146 ALA A CA    1 
ATOM   1159 C  C     . ALA A 1 146 ? 13.854 17.671  -6.909  1.00 23.46 ? 146 ALA A C     1 
ATOM   1160 O  O     . ALA A 1 146 ? 14.221 18.676  -7.523  1.00 28.19 ? 146 ALA A O     1 
ATOM   1161 C  CB    . ALA A 1 146 ? 13.904 15.674  -8.437  1.00 24.78 ? 146 ALA A CB    1 
ATOM   1162 N  N     . LYS A 1 147 ? 12.915 17.712  -5.962  1.00 24.03 ? 147 LYS A N     1 
ATOM   1163 C  CA    . LYS A 1 147 ? 12.198 18.955  -5.692  1.00 23.92 ? 147 LYS A CA    1 
ATOM   1164 C  C     . LYS A 1 147 ? 13.084 19.959  -4.965  1.00 28.27 ? 147 LYS A C     1 
ATOM   1165 O  O     . LYS A 1 147 ? 13.126 21.137  -5.337  1.00 28.68 ? 147 LYS A O     1 
ATOM   1166 C  CB    . LYS A 1 147 ? 10.940 18.665  -4.879  1.00 28.08 ? 147 LYS A CB    1 
ATOM   1167 C  CG    . LYS A 1 147 ? 10.185 19.915  -4.454  1.00 32.01 ? 147 LYS A CG    1 
ATOM   1168 C  CD    . LYS A 1 147 ? 8.685  19.657  -4.363  1.00 36.02 ? 147 LYS A CD    1 
ATOM   1169 C  CE    . LYS A 1 147 ? 7.993  20.746  -3.544  1.00 44.33 ? 147 LYS A CE    1 
ATOM   1170 N  NZ    . LYS A 1 147 ? 7.724  21.945  -4.377  1.00 50.01 ? 147 LYS A NZ    1 
ATOM   1171 N  N     . THR A 1 148 ? 13.825 19.508  -3.954  1.00 26.58 ? 148 THR A N     1 
ATOM   1172 C  CA    . THR A 1 148 ? 14.711 20.393  -3.198  1.00 28.58 ? 148 THR A CA    1 
ATOM   1173 C  C     . THR A 1 148 ? 16.154 20.336  -3.676  1.00 34.32 ? 148 THR A C     1 
ATOM   1174 O  O     . THR A 1 148 ? 16.980 21.115  -3.180  1.00 32.63 ? 148 THR A O     1 
ATOM   1175 C  CB    . THR A 1 148 ? 14.697 20.045  -1.703  1.00 27.28 ? 148 THR A CB    1 
ATOM   1176 O  OG1   . THR A 1 148 ? 15.373 18.794  -1.502  1.00 30.20 ? 148 THR A OG1   1 
ATOM   1177 C  CG2   . THR A 1 148 ? 13.283 19.970  -1.146  1.00 33.00 ? 148 THR A CG2   1 
ATOM   1178 N  N     . ARG A 1 149 ? 16.478 19.418  -4.596  1.00 26.97 ? 149 ARG A N     1 
ATOM   1179 C  CA    . ARG A 1 149 ? 17.808 19.128  -5.129  1.00 28.30 ? 149 ARG A CA    1 
ATOM   1180 C  C     . ARG A 1 149 ? 18.720 18.387  -4.148  1.00 30.43 ? 149 ARG A C     1 
ATOM   1181 O  O     . ARG A 1 149 ? 19.875 18.097  -4.503  1.00 30.99 ? 149 ARG A O     1 
ATOM   1182 C  CB    . ARG A 1 149 ? 18.559 20.381  -5.623  1.00 32.70 ? 149 ARG A CB    1 
ATOM   1183 C  CG    . ARG A 1 149 ? 19.671 20.023  -6.618  1.00 34.75 ? 149 ARG A CG    1 
ATOM   1184 C  CD    . ARG A 1 149 ? 20.668 21.144  -6.922  1.00 44.24 ? 149 ARG A CD    1 
ATOM   1185 N  NE    . ARG A 1 149 ? 21.664 20.646  -7.871  1.00 41.43 ? 149 ARG A NE    1 
ATOM   1186 C  CZ    . ARG A 1 149 ? 21.481 20.605  -9.182  1.00 39.07 ? 149 ARG A CZ    1 
ATOM   1187 N  NH1   . ARG A 1 149 ? 20.373 21.068  -9.732  1.00 39.98 ? 149 ARG A NH1   1 
ATOM   1188 N  NH2   . ARG A 1 149 ? 22.421 20.065  -9.956  1.00 36.77 ? 149 ARG A NH2   1 
ATOM   1189 N  N     . GLN A 1 150 ? 18.252 18.023  -2.955  1.00 24.99 ? 150 GLN A N     1 
ATOM   1190 C  CA    . GLN A 1 150 ? 19.100 17.251  -2.049  1.00 25.00 ? 150 GLN A CA    1 
ATOM   1191 C  C     . GLN A 1 150 ? 19.529 15.928  -2.683  1.00 28.95 ? 150 GLN A C     1 
ATOM   1192 O  O     . GLN A 1 150 ? 18.695 15.155  -3.171  1.00 24.40 ? 150 GLN A O     1 
ATOM   1193 C  CB    . GLN A 1 150 ? 18.400 17.009  -0.706  1.00 31.59 ? 150 GLN A CB    1 
ATOM   1194 C  CG    . GLN A 1 150 ? 19.102 15.929  0.146   1.00 43.75 ? 150 GLN A CG    1 
ATOM   1195 C  CD    . GLN A 1 150 ? 18.403 15.610  1.477   1.00 52.04 ? 150 GLN A CD    1 
ATOM   1196 O  OE1   . GLN A 1 150 ? 17.626 16.413  2.006   1.00 51.05 ? 150 GLN A OE1   1 
ATOM   1197 N  NE2   . GLN A 1 150 ? 18.699 14.432  2.028   1.00 51.11 ? 150 GLN A NE2   1 
ATOM   1198 N  N     . GLY A 1 151 ? 20.847 15.688  -2.709  1.00 23.51 ? 151 GLY A N     1 
ATOM   1199 C  CA    . GLY A 1 151 ? 21.422 14.424  -3.134  1.00 24.65 ? 151 GLY A CA    1 
ATOM   1200 C  C     . GLY A 1 151 ? 21.529 14.193  -4.630  1.00 23.56 ? 151 GLY A C     1 
ATOM   1201 O  O     . GLY A 1 151 ? 22.098 13.169  -5.033  1.00 23.92 ? 151 GLY A O     1 
ATOM   1202 N  N     . VAL A 1 152 ? 21.022 15.106  -5.467  1.00 22.44 ? 152 VAL A N     1 
ATOM   1203 C  CA    . VAL A 1 152 ? 20.970 14.873  -6.914  1.00 21.18 ? 152 VAL A CA    1 
ATOM   1204 C  C     . VAL A 1 152 ? 22.380 14.751  -7.503  1.00 25.79 ? 152 VAL A C     1 
ATOM   1205 O  O     . VAL A 1 152 ? 22.739 13.736  -8.135  1.00 20.94 ? 152 VAL A O     1 
ATOM   1206 C  CB    . VAL A 1 152 ? 20.152 15.982  -7.600  1.00 25.15 ? 152 VAL A CB    1 
ATOM   1207 C  CG1   . VAL A 1 152 ? 20.200 15.836  -9.124  1.00 22.51 ? 152 VAL A CG1   1 
ATOM   1208 C  CG2   . VAL A 1 152 ? 18.701 15.938  -7.120  1.00 23.51 ? 152 VAL A CG2   1 
ATOM   1209 N  N     . ASP A 1 153 ? 23.195 15.807  -7.325  1.00 26.11 ? 153 ASP A N     1 
ATOM   1210 C  CA    . ASP A 1 153 ? 24.585 15.750  -7.776  1.00 25.13 ? 153 ASP A CA    1 
ATOM   1211 C  C     . ASP A 1 153 ? 25.281 14.512  -7.234  1.00 25.27 ? 153 ASP A C     1 
ATOM   1212 O  O     . ASP A 1 153 ? 26.039 13.853  -7.955  1.00 23.80 ? 153 ASP A O     1 
ATOM   1213 C  CB    . ASP A 1 153 ? 25.363 17.004  -7.344  1.00 29.66 ? 153 ASP A CB    1 
ATOM   1214 C  CG    . ASP A 1 153 ? 24.912 18.266  -8.059  1.00 35.40 ? 153 ASP A CG    1 
ATOM   1215 O  OD1   . ASP A 1 153 ? 24.246 18.168  -9.105  1.00 37.81 ? 153 ASP A OD1   1 
ATOM   1216 O  OD2   . ASP A 1 153 ? 25.242 19.372  -7.574  1.00 39.79 ? 153 ASP A OD2   1 
ATOM   1217 N  N     . ASP A 1 154 ? 25.066 14.205  -5.952  1.00 24.15 ? 154 ASP A N     1 
ATOM   1218 C  CA    . ASP A 1 154 ? 25.746 13.074  -5.324  1.00 25.91 ? 154 ASP A CA    1 
ATOM   1219 C  C     . ASP A 1 154 ? 25.401 11.760  -6.013  1.00 29.50 ? 154 ASP A C     1 
ATOM   1220 O  O     . ASP A 1 154 ? 26.278 10.925  -6.249  1.00 24.42 ? 154 ASP A O     1 
ATOM   1221 C  CB    . ASP A 1 154 ? 25.399 12.993  -3.841  1.00 31.53 ? 154 ASP A CB    1 
ATOM   1222 C  CG    . ASP A 1 154 ? 26.009 14.127  -3.039  1.00 40.72 ? 154 ASP A CG    1 
ATOM   1223 O  OD1   . ASP A 1 154 ? 27.053 14.664  -3.478  1.00 40.69 ? 154 ASP A OD1   1 
ATOM   1224 O  OD2   . ASP A 1 154 ? 25.457 14.461  -1.968  1.00 41.63 ? 154 ASP A OD2   1 
ATOM   1225 N  N     . ALA A 1 155 ? 24.119 11.534  -6.293  1.00 25.45 ? 155 ALA A N     1 
ATOM   1226 C  CA    . ALA A 1 155 ? 23.728 10.288  -6.947  1.00 22.27 ? 155 ALA A CA    1 
ATOM   1227 C  C     . ALA A 1 155 ? 24.423 10.147  -8.300  1.00 21.17 ? 155 ALA A C     1 
ATOM   1228 O  O     . ALA A 1 155 ? 25.055 9.114   -8.593  1.00 22.93 ? 155 ALA A O     1 
ATOM   1229 C  CB    . ALA A 1 155 ? 22.202 10.223  -7.075  1.00 24.32 ? 155 ALA A CB    1 
ATOM   1230 N  N     . PHE A 1 156 ? 24.349 11.190  -9.136  1.00 20.47 ? 156 PHE A N     1 
ATOM   1231 C  CA    . PHE A 1 156 ? 24.955 11.058  -10.465 1.00 21.90 ? 156 PHE A CA    1 
ATOM   1232 C  C     . PHE A 1 156 ? 26.480 10.952  -10.396 1.00 21.67 ? 156 PHE A C     1 
ATOM   1233 O  O     . PHE A 1 156 ? 27.089 10.161  -11.135 1.00 18.87 ? 156 PHE A O     1 
ATOM   1234 C  CB    . PHE A 1 156 ? 24.542 12.223  -11.361 1.00 19.56 ? 156 PHE A CB    1 
ATOM   1235 C  CG    . PHE A 1 156 ? 23.161 12.061  -11.930 1.00 18.73 ? 156 PHE A CG    1 
ATOM   1236 C  CD1   . PHE A 1 156 ? 22.957 11.295  -13.067 1.00 23.03 ? 156 PHE A CD1   1 
ATOM   1237 C  CD2   . PHE A 1 156 ? 22.078 12.644  -11.306 1.00 19.74 ? 156 PHE A CD2   1 
ATOM   1238 C  CE1   . PHE A 1 156 ? 21.675 11.125  -13.592 1.00 20.67 ? 156 PHE A CE1   1 
ATOM   1239 C  CE2   . PHE A 1 156 ? 20.792 12.484  -11.825 1.00 22.38 ? 156 PHE A CE2   1 
ATOM   1240 C  CZ    . PHE A 1 156 ? 20.599 11.721  -12.966 1.00 21.32 ? 156 PHE A CZ    1 
ATOM   1241 N  N     . TYR A 1 157 ? 27.125 11.753  -9.543  1.00 21.57 ? 157 TYR A N     1 
ATOM   1242 C  CA    . TYR A 1 157 ? 28.587 11.718  -9.493  1.00 24.32 ? 157 TYR A CA    1 
ATOM   1243 C  C     . TYR A 1 157 ? 29.098 10.428  -8.868  1.00 22.73 ? 157 TYR A C     1 
ATOM   1244 O  O     . TYR A 1 157 ? 30.165 9.928   -9.259  1.00 22.25 ? 157 TYR A O     1 
ATOM   1245 C  CB    . TYR A 1 157 ? 29.139 12.930  -8.740  1.00 23.78 ? 157 TYR A CB    1 
ATOM   1246 C  CG    . TYR A 1 157 ? 28.845 14.266  -9.402  1.00 29.71 ? 157 TYR A CG    1 
ATOM   1247 C  CD1   . TYR A 1 157 ? 28.219 14.337  -10.639 1.00 29.75 ? 157 TYR A CD1   1 
ATOM   1248 C  CD2   . TYR A 1 157 ? 29.194 15.456  -8.778  1.00 37.72 ? 157 TYR A CD2   1 
ATOM   1249 C  CE1   . TYR A 1 157 ? 27.934 15.564  -11.237 1.00 33.64 ? 157 TYR A CE1   1 
ATOM   1250 C  CE2   . TYR A 1 157 ? 28.920 16.680  -9.366  1.00 37.59 ? 157 TYR A CE2   1 
ATOM   1251 C  CZ    . TYR A 1 157 ? 28.290 16.729  -10.590 1.00 39.82 ? 157 TYR A CZ    1 
ATOM   1252 O  OH    . TYR A 1 157 ? 28.023 17.958  -11.167 1.00 48.08 ? 157 TYR A OH    1 
ATOM   1253 N  N     . THR A 1 158 ? 28.375 9.883   -7.877  1.00 20.63 ? 158 THR A N     1 
ATOM   1254 C  CA    . THR A 1 158 ? 28.743 8.583   -7.328  1.00 19.62 ? 158 THR A CA    1 
ATOM   1255 C  C     . THR A 1 158 ? 28.698 7.522   -8.421  1.00 25.22 ? 158 THR A C     1 
ATOM   1256 O  O     . THR A 1 158 ? 29.585 6.667   -8.494  1.00 21.64 ? 158 THR A O     1 
ATOM   1257 C  CB    . THR A 1 158 ? 27.810 8.209   -6.164  1.00 20.90 ? 158 THR A CB    1 
ATOM   1258 O  OG1   . THR A 1 158 ? 27.900 9.192   -5.118  1.00 23.69 ? 158 THR A OG1   1 
ATOM   1259 C  CG2   . THR A 1 158 ? 28.191 6.849   -5.588  1.00 24.73 ? 158 THR A CG2   1 
ATOM   1260 N  N     . LEU A 1 159 ? 27.686 7.582   -9.310  1.00 20.81 ? 159 LEU A N     1 
ATOM   1261 C  CA    . LEU A 1 159 ? 27.650 6.628   -10.428 1.00 18.73 ? 159 LEU A CA    1 
ATOM   1262 C  C     . LEU A 1 159 ? 28.850 6.800   -11.362 1.00 20.05 ? 159 LEU A C     1 
ATOM   1263 O  O     . LEU A 1 159 ? 29.460 5.811   -11.806 1.00 19.73 ? 159 LEU A O     1 
ATOM   1264 C  CB    . LEU A 1 159 ? 26.335 6.775   -11.208 1.00 20.98 ? 159 LEU A CB    1 
ATOM   1265 C  CG    . LEU A 1 159 ? 26.122 5.772   -12.359 1.00 20.72 ? 159 LEU A CG    1 
ATOM   1266 C  CD1   . LEU A 1 159 ? 26.236 4.332   -11.832 1.00 21.38 ? 159 LEU A CD1   1 
ATOM   1267 C  CD2   . LEU A 1 159 ? 24.788 6.006   -13.043 1.00 22.02 ? 159 LEU A CD2   1 
ATOM   1268 N  N     . VAL A 1 160 ? 29.200 8.044   -11.687 1.00 18.07 ? 160 VAL A N     1 
ATOM   1269 C  CA    . VAL A 1 160 ? 30.393 8.274   -12.512 1.00 20.18 ? 160 VAL A CA    1 
ATOM   1270 C  C     . VAL A 1 160 ? 31.631 7.658   -11.857 1.00 22.26 ? 160 VAL A C     1 
ATOM   1271 O  O     . VAL A 1 160 ? 32.463 7.013   -12.518 1.00 23.74 ? 160 VAL A O     1 
ATOM   1272 C  CB    . VAL A 1 160 ? 30.582 9.778   -12.784 1.00 23.21 ? 160 VAL A CB    1 
ATOM   1273 C  CG1   . VAL A 1 160 ? 31.918 10.013  -13.496 1.00 25.48 ? 160 VAL A CG1   1 
ATOM   1274 C  CG2   . VAL A 1 160 ? 29.448 10.289  -13.669 1.00 23.01 ? 160 VAL A CG2   1 
ATOM   1275 N  N     . ARG A 1 161 ? 31.793 7.873   -10.554 1.00 20.69 ? 161 ARG A N     1 
ATOM   1276 C  CA    . ARG A 1 161 ? 32.960 7.313   -9.878  1.00 23.56 ? 161 ARG A CA    1 
ATOM   1277 C  C     . ARG A 1 161 ? 32.941 5.784   -9.896  1.00 26.16 ? 161 ARG A C     1 
ATOM   1278 O  O     . ARG A 1 161 ? 33.998 5.146   -10.000 1.00 31.07 ? 161 ARG A O     1 
ATOM   1279 C  CB    . ARG A 1 161 ? 33.046 7.844   -8.454  1.00 25.19 ? 161 ARG A CB    1 
ATOM   1280 C  CG    . ARG A 1 161 ? 33.439 9.303   -8.407  1.00 24.89 ? 161 ARG A CG    1 
ATOM   1281 C  CD    . ARG A 1 161 ? 33.126 9.922   -7.071  1.00 28.54 ? 161 ARG A CD    1 
ATOM   1282 N  NE    . ARG A 1 161 ? 33.480 11.336  -7.097  1.00 28.19 ? 161 ARG A NE    1 
ATOM   1283 C  CZ    . ARG A 1 161 ? 32.755 12.289  -6.537  1.00 31.73 ? 161 ARG A CZ    1 
ATOM   1284 N  NH1   . ARG A 1 161 ? 31.613 12.015  -5.923  1.00 32.74 ? 161 ARG A NH1   1 
ATOM   1285 N  NH2   . ARG A 1 161 ? 33.163 13.550  -6.630  1.00 33.27 ? 161 ARG A NH2   1 
ATOM   1286 N  N     . GLU A 1 162 ? 31.755 5.172   -9.784  1.00 25.14 ? 162 GLU A N     1 
ATOM   1287 C  CA    . GLU A 1 162 ? 31.683 3.709   -9.892  1.00 24.43 ? 162 GLU A CA    1 
ATOM   1288 C  C     . GLU A 1 162 ? 32.137 3.233   -11.269 1.00 23.99 ? 162 GLU A C     1 
ATOM   1289 O  O     . GLU A 1 162 ? 32.819 2.204   -11.393 1.00 29.31 ? 162 GLU A O     1 
ATOM   1290 C  CB    . GLU A 1 162 ? 30.260 3.207   -9.607  1.00 27.72 ? 162 GLU A CB    1 
ATOM   1291 C  CG    . GLU A 1 162 ? 29.774 3.394   -8.169  1.00 27.63 ? 162 GLU A CG    1 
ATOM   1292 C  CD    . GLU A 1 162 ? 30.460 2.450   -7.219  1.00 31.17 ? 162 GLU A CD    1 
ATOM   1293 O  OE1   . GLU A 1 162 ? 30.231 1.233   -7.339  1.00 32.02 ? 162 GLU A OE1   1 
ATOM   1294 O  OE2   . GLU A 1 162 ? 31.261 2.920   -6.382  1.00 33.30 ? 162 GLU A OE2   1 
ATOM   1295 N  N     . ILE A 1 163 ? 31.748 3.957   -12.319 1.00 23.88 ? 163 ILE A N     1 
ATOM   1296 C  CA    . ILE A 1 163 ? 32.186 3.586   -13.666 1.00 24.06 ? 163 ILE A CA    1 
ATOM   1297 C  C     . ILE A 1 163 ? 33.701 3.694   -13.779 1.00 31.02 ? 163 ILE A C     1 
ATOM   1298 O  O     . ILE A 1 163 ? 34.361 2.817   -14.348 1.00 30.24 ? 163 ILE A O     1 
ATOM   1299 C  CB    . ILE A 1 163 ? 31.487 4.450   -14.726 1.00 24.24 ? 163 ILE A CB    1 
ATOM   1300 C  CG1   . ILE A 1 163 ? 29.971 4.212   -14.714 1.00 21.29 ? 163 ILE A CG1   1 
ATOM   1301 C  CG2   . ILE A 1 163 ? 32.024 4.129   -16.108 1.00 27.43 ? 163 ILE A CG2   1 
ATOM   1302 C  CD1   . ILE A 1 163 ? 29.219 5.229   -15.536 1.00 24.75 ? 163 ILE A CD1   1 
ATOM   1303 N  N     . ARG A 1 164 ? 34.275 4.784   -13.262 1.00 27.99 ? 164 ARG A N     1 
ATOM   1304 C  CA    . ARG A 1 164 ? 35.734 4.900   -13.294 1.00 34.27 ? 164 ARG A CA    1 
ATOM   1305 C  C     . ARG A 1 164 ? 36.400 3.721   -12.602 1.00 38.34 ? 164 ARG A C     1 
ATOM   1306 O  O     . ARG A 1 164 ? 37.355 3.141   -13.133 1.00 40.93 ? 164 ARG A O     1 
ATOM   1307 C  CB    . ARG A 1 164 ? 36.218 6.193   -12.654 1.00 30.10 ? 164 ARG A CB    1 
ATOM   1308 C  CG    . ARG A 1 164 ? 35.907 7.426   -13.405 1.00 33.83 ? 164 ARG A CG    1 
ATOM   1309 C  CD    . ARG A 1 164 ? 36.708 8.535   -12.763 1.00 40.47 ? 164 ARG A CD    1 
ATOM   1310 N  NE    . ARG A 1 164 ? 36.373 9.829   -13.325 1.00 40.57 ? 164 ARG A NE    1 
ATOM   1311 C  CZ    . ARG A 1 164 ? 36.144 10.909  -12.595 1.00 37.57 ? 164 ARG A CZ    1 
ATOM   1312 N  NH1   . ARG A 1 164 ? 36.198 10.872  -11.272 1.00 39.83 ? 164 ARG A NH1   1 
ATOM   1313 N  NH2   . ARG A 1 164 ? 35.823 12.044  -13.204 1.00 35.52 ? 164 ARG A NH2   1 
ATOM   1314 N  N     . LYS A 1 165 ? 35.942 3.385   -11.389 1.00 37.57 ? 165 LYS A N     1 
ATOM   1315 C  CA    . LYS A 1 165 ? 36.476 2.214   -10.692 1.00 42.31 ? 165 LYS A CA    1 
ATOM   1316 C  C     . LYS A 1 165 ? 36.416 0.971   -11.573 1.00 46.40 ? 165 LYS A C     1 
ATOM   1317 O  O     . LYS A 1 165 ? 37.409 0.248   -11.714 1.00 52.41 ? 165 LYS A O     1 
ATOM   1318 C  CB    . LYS A 1 165 ? 35.709 1.964   -9.390  1.00 40.96 ? 165 LYS A CB    1 
ATOM   1319 C  CG    . LYS A 1 165 ? 36.196 2.738   -8.178  1.00 47.15 ? 165 LYS A CG    1 
ATOM   1320 C  CD    . LYS A 1 165 ? 35.678 2.071   -6.901  1.00 46.90 ? 165 LYS A CD    1 
ATOM   1321 C  CE    . LYS A 1 165 ? 35.186 3.094   -5.877  1.00 50.30 ? 165 LYS A CE    1 
ATOM   1322 N  NZ    . LYS A 1 165 ? 35.754 2.857   -4.511  1.00 51.94 ? 165 LYS A NZ    1 
ATOM   1323 N  N     . HIS A 1 166 ? 35.243 0.708   -12.165 1.00 42.97 ? 166 HIS A N     1 
ATOM   1324 C  CA    . HIS A 1 166 ? 35.040 -0.502  -12.965 1.00 45.46 ? 166 HIS A CA    1 
ATOM   1325 C  C     . HIS A 1 166 ? 35.952 -0.531  -14.189 1.00 49.65 ? 166 HIS A C     1 
ATOM   1326 O  O     . HIS A 1 166 ? 36.382 -1.603  -14.622 1.00 53.75 ? 166 HIS A O     1 
ATOM   1327 C  CB    . HIS A 1 166 ? 33.566 -0.606  -13.372 1.00 42.51 ? 166 HIS A CB    1 
ATOM   1328 C  CG    . HIS A 1 166 ? 33.290 -1.573  -14.487 1.00 49.13 ? 166 HIS A CG    1 
ATOM   1329 N  ND1   . HIS A 1 166 ? 33.023 -2.911  -14.274 1.00 53.39 ? 166 HIS A ND1   1 
ATOM   1330 C  CD2   . HIS A 1 166 ? 33.220 -1.386  -15.828 1.00 51.23 ? 166 HIS A CD2   1 
ATOM   1331 C  CE1   . HIS A 1 166 ? 32.804 -3.506  -15.435 1.00 53.87 ? 166 HIS A CE1   1 
ATOM   1332 N  NE2   . HIS A 1 166 ? 32.922 -2.603  -16.394 1.00 57.20 ? 166 HIS A NE2   1 
ATOM   1333 N  N     . LYS A 1 167 ? 36.221 0.628   -14.797 1.00 48.89 ? 167 LYS A N     1 
ATOM   1334 C  CA    . LYS A 1 167 ? 37.186 0.656   -15.895 1.00 50.31 ? 167 LYS A CA    1 
ATOM   1335 C  C     . LYS A 1 167 ? 38.613 0.396   -15.431 1.00 55.20 ? 167 LYS A C     1 
ATOM   1336 O  O     . LYS A 1 167 ? 39.454 -0.003  -16.244 1.00 61.21 ? 167 LYS A O     1 
ATOM   1337 C  CB    . LYS A 1 167 ? 37.191 2.009   -16.592 1.00 47.99 ? 167 LYS A CB    1 
ATOM   1338 C  CG    . LYS A 1 167 ? 36.010 2.326   -17.437 1.00 46.52 ? 167 LYS A CG    1 
ATOM   1339 C  CD    . LYS A 1 167 ? 36.126 3.783   -17.788 1.00 49.75 ? 167 LYS A CD    1 
ATOM   1340 C  CE    . LYS A 1 167 ? 35.159 4.193   -18.864 1.00 54.85 ? 167 LYS A CE    1 
ATOM   1341 N  NZ    . LYS A 1 167 ? 35.451 5.605   -19.249 1.00 50.60 ? 167 LYS A NZ    1 
ATOM   1342 N  N     . GLU A 1 168 ? 38.898 0.619   -14.153 1.00 58.28 ? 168 GLU A N     1 
ATOM   1343 C  CA    . GLU A 1 168 ? 40.243 0.466   -13.593 1.00 62.34 ? 168 GLU A CA    1 
ATOM   1344 C  C     . GLU A 1 168 ? 40.341 -0.826  -12.781 1.00 62.79 ? 168 GLU A C     1 
ATOM   1345 O  O     . GLU A 1 168 ? 40.640 -0.809  -11.587 1.00 67.00 ? 168 GLU A O     1 
ATOM   1346 C  CB    . GLU A 1 168 ? 40.589 1.678   -12.726 1.00 55.50 ? 168 GLU A CB    1 
ATOM   1347 C  CG    . GLU A 1 168 ? 40.499 3.042   -13.419 1.00 51.51 ? 168 GLU A CG    1 
ATOM   1348 C  CD    . GLU A 1 168 ? 40.808 4.190   -12.462 1.00 58.88 ? 168 GLU A CD    1 
ATOM   1349 O  OE1   . GLU A 1 168 ? 41.260 3.906   -11.327 1.00 63.82 ? 168 GLU A OE1   1 
ATOM   1350 O  OE2   . GLU A 1 168 ? 40.553 5.365   -12.820 1.00 55.13 ? 168 GLU A OE2   1 
ATOM   1351 N  N     . LYS A 1 169 ? 40.070 -1.961  -13.425 1.00 65.70 ? 169 LYS A N     1 
ATOM   1352 C  CA    . LYS A 1 169 ? 40.090 -3.237  -12.702 1.00 69.39 ? 169 LYS A CA    1 
ATOM   1353 C  C     . LYS A 1 169 ? 41.010 -4.245  -13.389 1.00 72.43 ? 169 LYS A C     1 
ATOM   1354 O  O     . LYS A 1 169 ? 41.655 -3.939  -14.398 1.00 74.94 ? 169 LYS A O     1 
ATOM   1355 C  CB    . LYS A 1 169 ? 38.676 -3.830  -12.578 1.00 66.45 ? 169 LYS A CB    1 
ATOM   1356 C  CG    . LYS A 1 169 ? 37.985 -4.131  -13.911 1.00 68.10 ? 169 LYS A CG    1 
ATOM   1357 C  CD    . LYS A 1 169 ? 36.494 -4.457  -13.725 1.00 64.37 ? 169 LYS A CD    1 
ATOM   1358 C  CE    . LYS A 1 169 ? 36.214 -5.945  -13.547 1.00 67.66 ? 169 LYS A CE    1 
ATOM   1359 N  NZ    . LYS A 1 169 ? 34.746 -6.195  -13.392 1.00 61.88 ? 169 LYS A NZ    1 
ATOM   1360 O  OXT   . LYS A 1 169 ? 41.141 -5.386  -12.935 1.00 72.07 ? 169 LYS A OXT   1 
ATOM   1361 N  N     . MET B 1 1   ? 5.730  -4.490  30.255  1.00 50.34 ? 1   MET B N     1 
ATOM   1362 C  CA    . MET B 1 1   ? 6.318  -3.315  29.619  1.00 49.52 ? 1   MET B CA    1 
ATOM   1363 C  C     . MET B 1 1   ? 7.819  -3.463  29.386  1.00 44.32 ? 1   MET B C     1 
ATOM   1364 O  O     . MET B 1 1   ? 8.565  -3.635  30.343  1.00 44.04 ? 1   MET B O     1 
ATOM   1365 C  CB    . MET B 1 1   ? 6.064  -2.073  30.463  1.00 51.72 ? 1   MET B CB    1 
ATOM   1366 C  CG    . MET B 1 1   ? 6.737  -0.875  29.857  1.00 47.40 ? 1   MET B CG    1 
ATOM   1367 S  SD    . MET B 1 1   ? 5.615  0.336   29.155  1.00 60.35 ? 1   MET B SD    1 
ATOM   1368 C  CE    . MET B 1 1   ? 5.423  1.440   30.540  1.00 42.59 ? 1   MET B CE    1 
ATOM   1369 N  N     . THR B 1 2   ? 8.295  -3.348  28.145  1.00 42.85 ? 2   THR B N     1 
ATOM   1370 C  CA    . THR B 1 2   ? 9.723  -3.577  27.924  1.00 40.72 ? 2   THR B CA    1 
ATOM   1371 C  C     . THR B 1 2   ? 10.500 -2.267  27.986  1.00 36.02 ? 2   THR B C     1 
ATOM   1372 O  O     . THR B 1 2   ? 10.146 -1.302  27.308  1.00 31.91 ? 2   THR B O     1 
ATOM   1373 C  CB    . THR B 1 2   ? 9.958  -4.266  26.582  1.00 41.39 ? 2   THR B CB    1 
ATOM   1374 O  OG1   . THR B 1 2   ? 9.103  -5.410  26.486  1.00 42.47 ? 2   THR B OG1   1 
ATOM   1375 C  CG2   . THR B 1 2   ? 11.401 -4.726  26.491  1.00 39.80 ? 2   THR B CG2   1 
ATOM   1376 N  N     . GLU B 1 3   ? 11.570 -2.237  28.778  1.00 31.01 ? 3   GLU B N     1 
ATOM   1377 C  CA    . GLU B 1 3   ? 12.392 -1.040  28.912  1.00 31.02 ? 3   GLU B CA    1 
ATOM   1378 C  C     . GLU B 1 3   ? 13.671 -1.181  28.079  1.00 29.42 ? 3   GLU B C     1 
ATOM   1379 O  O     . GLU B 1 3   ? 14.274 -2.259  28.018  1.00 28.81 ? 3   GLU B O     1 
ATOM   1380 C  CB    . GLU B 1 3   ? 12.687 -0.805  30.395  1.00 38.98 ? 3   GLU B CB    1 
ATOM   1381 C  CG    . GLU B 1 3   ? 13.615 0.338   30.772  1.00 46.08 ? 3   GLU B CG    1 
ATOM   1382 C  CD    . GLU B 1 3   ? 13.359 0.781   32.218  1.00 60.13 ? 3   GLU B CD    1 
ATOM   1383 O  OE1   . GLU B 1 3   ? 12.271 0.468   32.759  1.00 60.03 ? 3   GLU B OE1   1 
ATOM   1384 O  OE2   . GLU B 1 3   ? 14.244 1.418   32.824  1.00 60.02 ? 3   GLU B OE2   1 
ATOM   1385 N  N     . TYR B 1 4   ? 14.059 -0.099  27.391  1.00 21.64 ? 4   TYR B N     1 
ATOM   1386 C  CA    . TYR B 1 4   ? 15.277 -0.068  26.578  1.00 22.96 ? 4   TYR B CA    1 
ATOM   1387 C  C     . TYR B 1 4   ? 16.135 1.118   26.993  1.00 27.07 ? 4   TYR B C     1 
ATOM   1388 O  O     . TYR B 1 4   ? 15.633 2.247   27.047  1.00 26.67 ? 4   TYR B O     1 
ATOM   1389 C  CB    . TYR B 1 4   ? 14.951 0.070   25.087  1.00 23.25 ? 4   TYR B CB    1 
ATOM   1390 C  CG    . TYR B 1 4   ? 14.205 -1.098  24.477  1.00 27.26 ? 4   TYR B CG    1 
ATOM   1391 C  CD1   . TYR B 1 4   ? 14.884 -2.219  24.012  1.00 28.86 ? 4   TYR B CD1   1 
ATOM   1392 C  CD2   . TYR B 1 4   ? 12.817 -1.077  24.368  1.00 27.06 ? 4   TYR B CD2   1 
ATOM   1393 C  CE1   . TYR B 1 4   ? 14.193 -3.293  23.449  1.00 30.85 ? 4   TYR B CE1   1 
ATOM   1394 C  CE2   . TYR B 1 4   ? 12.125 -2.143  23.816  1.00 30.03 ? 4   TYR B CE2   1 
ATOM   1395 C  CZ    . TYR B 1 4   ? 12.816 -3.244  23.355  1.00 34.67 ? 4   TYR B CZ    1 
ATOM   1396 O  OH    . TYR B 1 4   ? 12.127 -4.301  22.799  1.00 33.76 ? 4   TYR B OH    1 
ATOM   1397 N  N     . LYS B 1 5   ? 17.428 0.872   27.246  1.00 20.89 ? 5   LYS B N     1 
ATOM   1398 C  CA    . LYS B 1 5   ? 18.390 1.927   27.592  1.00 25.07 ? 5   LYS B CA    1 
ATOM   1399 C  C     . LYS B 1 5   ? 19.176 2.313   26.348  1.00 20.55 ? 5   LYS B C     1 
ATOM   1400 O  O     . LYS B 1 5   ? 20.007 1.530   25.862  1.00 18.75 ? 5   LYS B O     1 
ATOM   1401 C  CB    . LYS B 1 5   ? 19.353 1.477   28.688  1.00 24.28 ? 5   LYS B CB    1 
ATOM   1402 C  CG    . LYS B 1 5   ? 18.662 0.994   29.911  1.00 35.43 ? 5   LYS B CG    1 
ATOM   1403 C  CD    . LYS B 1 5   ? 17.868 2.127   30.470  1.00 41.24 ? 5   LYS B CD    1 
ATOM   1404 C  CE    . LYS B 1 5   ? 16.947 1.622   31.532  1.00 50.94 ? 5   LYS B CE    1 
ATOM   1405 N  NZ    . LYS B 1 5   ? 15.893 2.622   31.836  1.00 53.43 ? 5   LYS B NZ    1 
ATOM   1406 N  N     . LEU B 1 6   ? 18.917 3.527   25.833  1.00 16.77 ? 6   LEU B N     1 
ATOM   1407 C  CA    . LEU B 1 6   ? 19.606 4.034   24.662  1.00 18.07 ? 6   LEU B CA    1 
ATOM   1408 C  C     . LEU B 1 6   ? 20.550 5.145   25.099  1.00 20.07 ? 6   LEU B C     1 
ATOM   1409 O  O     . LEU B 1 6   ? 20.237 5.901   26.028  1.00 19.23 ? 6   LEU B O     1 
ATOM   1410 C  CB    . LEU B 1 6   ? 18.621 4.584   23.630  1.00 18.65 ? 6   LEU B CB    1 
ATOM   1411 C  CG    . LEU B 1 6   ? 17.386 3.752   23.293  1.00 22.76 ? 6   LEU B CG    1 
ATOM   1412 C  CD1   . LEU B 1 6   ? 16.617 4.404   22.166  1.00 22.73 ? 6   LEU B CD1   1 
ATOM   1413 C  CD2   . LEU B 1 6   ? 17.792 2.371   22.891  1.00 24.23 ? 6   LEU B CD2   1 
ATOM   1414 N  N     . VAL B 1 7   ? 21.702 5.237   24.439  1.00 17.14 ? 7   VAL B N     1 
ATOM   1415 C  CA    . VAL B 1 7   ? 22.662 6.299   24.724  1.00 15.24 ? 7   VAL B CA    1 
ATOM   1416 C  C     . VAL B 1 7   ? 23.009 7.009   23.420  1.00 17.38 ? 7   VAL B C     1 
ATOM   1417 O  O     . VAL B 1 7   ? 23.318 6.354   22.425  1.00 15.83 ? 7   VAL B O     1 
ATOM   1418 C  CB    . VAL B 1 7   ? 23.932 5.727   25.375  1.00 17.04 ? 7   VAL B CB    1 
ATOM   1419 C  CG1   . VAL B 1 7   ? 24.924 6.869   25.679  1.00 18.82 ? 7   VAL B CG1   1 
ATOM   1420 C  CG2   . VAL B 1 7   ? 23.589 4.926   26.618  1.00 18.20 ? 7   VAL B CG2   1 
ATOM   1421 N  N     . VAL B 1 8   ? 22.993 8.344   23.428  1.00 14.74 ? 8   VAL B N     1 
ATOM   1422 C  CA    . VAL B 1 8   ? 23.283 9.134   22.236  1.00 14.67 ? 8   VAL B CA    1 
ATOM   1423 C  C     . VAL B 1 8   ? 24.667 9.735   22.437  1.00 16.82 ? 8   VAL B C     1 
ATOM   1424 O  O     . VAL B 1 8   ? 24.873 10.495  23.389  1.00 15.28 ? 8   VAL B O     1 
ATOM   1425 C  CB    . VAL B 1 8   ? 22.229 10.237  22.004  1.00 18.00 ? 8   VAL B CB    1 
ATOM   1426 C  CG1   . VAL B 1 8   ? 22.537 11.015  20.708  1.00 17.25 ? 8   VAL B CG1   1 
ATOM   1427 C  CG2   . VAL B 1 8   ? 20.791 9.670   21.983  1.00 18.66 ? 8   VAL B CG2   1 
ATOM   1428 N  N     . VAL B 1 9   ? 25.624 9.391   21.560  1.00 15.39 ? 9   VAL B N     1 
ATOM   1429 C  CA    . VAL B 1 9   ? 27.002 9.859   21.713  1.00 13.93 ? 9   VAL B CA    1 
ATOM   1430 C  C     . VAL B 1 9   ? 27.477 10.539  20.433  1.00 16.78 ? 9   VAL B C     1 
ATOM   1431 O  O     . VAL B 1 9   ? 26.907 10.365  19.354  1.00 16.23 ? 9   VAL B O     1 
ATOM   1432 C  CB    . VAL B 1 9   ? 27.964 8.730   22.116  1.00 16.67 ? 9   VAL B CB    1 
ATOM   1433 C  CG1   . VAL B 1 9   ? 27.474 8.105   23.429  1.00 17.02 ? 9   VAL B CG1   1 
ATOM   1434 C  CG2   . VAL B 1 9   ? 28.120 7.684   21.019  1.00 20.12 ? 9   VAL B CG2   1 
ATOM   1435 N  N     . GLY B 1 10  ? 28.560 11.300  20.569  1.00 14.37 ? 10  GLY B N     1 
ATOM   1436 C  CA    . GLY B 1 10  ? 29.154 12.016  19.457  1.00 12.57 ? 10  GLY B CA    1 
ATOM   1437 C  C     . GLY B 1 10  ? 29.699 13.356  19.912  1.00 16.05 ? 10  GLY B C     1 
ATOM   1438 O  O     . GLY B 1 10  ? 29.500 13.757  21.065  1.00 15.49 ? 10  GLY B O     1 
ATOM   1439 N  N     . ALA B 1 11  ? 30.386 14.052  19.001  1.00 14.72 ? 11  ALA B N     1 
ATOM   1440 C  CA    . ALA B 1 11  ? 31.029 15.333  19.296  1.00 17.14 ? 11  ALA B CA    1 
ATOM   1441 C  C     . ALA B 1 11  ? 30.019 16.406  19.722  1.00 18.63 ? 11  ALA B C     1 
ATOM   1442 O  O     . ALA B 1 11  ? 28.810 16.301  19.489  1.00 15.43 ? 11  ALA B O     1 
ATOM   1443 C  CB    . ALA B 1 11  ? 31.796 15.812  18.054  1.00 17.19 ? 11  ALA B CB    1 
ATOM   1444 N  N     . ASP B 1 12  ? 30.532 17.471  20.343  1.00 15.18 ? 12  ASP B N     1 
ATOM   1445 C  CA    . ASP B 1 12  ? 29.666 18.587  20.694  1.00 17.25 ? 12  ASP B CA    1 
ATOM   1446 C  C     . ASP B 1 12  ? 29.116 19.236  19.436  1.00 19.37 ? 12  ASP B C     1 
ATOM   1447 O  O     . ASP B 1 12  ? 29.819 19.345  18.426  1.00 16.85 ? 12  ASP B O     1 
ATOM   1448 C  CB    . ASP B 1 12  ? 30.423 19.673  21.460  1.00 17.91 ? 12  ASP B CB    1 
ATOM   1449 C  CG    . ASP B 1 12  ? 30.863 19.240  22.833  1.00 24.59 ? 12  ASP B CG    1 
ATOM   1450 O  OD1   . ASP B 1 12  ? 30.162 18.426  23.481  1.00 17.95 ? 12  ASP B OD1   1 
ATOM   1451 O  OD2   . ASP B 1 12  ? 31.922 19.751  23.290  1.00 21.50 ? 12  ASP B OD2   1 
ATOM   1452 N  N     . GLY B 1 13  ? 27.862 19.673  19.500  1.00 15.03 ? 13  GLY B N     1 
ATOM   1453 C  CA    . GLY B 1 13  ? 27.315 20.503  18.433  1.00 16.49 ? 13  GLY B CA    1 
ATOM   1454 C  C     . GLY B 1 13  ? 26.744 19.761  17.245  1.00 22.47 ? 13  GLY B C     1 
ATOM   1455 O  O     . GLY B 1 13  ? 26.420 20.400  16.235  1.00 17.23 ? 13  GLY B O     1 
ATOM   1456 N  N     . VAL B 1 14  ? 26.640 18.433  17.313  1.00 16.86 ? 14  VAL B N     1 
ATOM   1457 C  CA    . VAL B 1 14  ? 26.188 17.683  16.152  1.00 16.19 ? 14  VAL B CA    1 
ATOM   1458 C  C     . VAL B 1 14  ? 24.679 17.546  16.140  1.00 18.53 ? 14  VAL B C     1 
ATOM   1459 O  O     . VAL B 1 14  ? 24.121 17.132  15.115  1.00 17.38 ? 14  VAL B O     1 
ATOM   1460 C  CB    . VAL B 1 14  ? 26.844 16.296  16.058  1.00 15.09 ? 14  VAL B CB    1 
ATOM   1461 C  CG1   . VAL B 1 14  ? 28.357 16.463  15.994  1.00 20.23 ? 14  VAL B CG1   1 
ATOM   1462 C  CG2   . VAL B 1 14  ? 26.446 15.383  17.241  1.00 15.45 ? 14  VAL B CG2   1 
ATOM   1463 N  N     . GLY B 1 15  ? 24.016 17.852  17.247  1.00 16.63 ? 15  GLY B N     1 
ATOM   1464 C  CA    . GLY B 1 15  ? 22.580 17.763  17.334  1.00 17.69 ? 15  GLY B CA    1 
ATOM   1465 C  C     . GLY B 1 15  ? 22.054 16.617  18.171  1.00 17.11 ? 15  GLY B C     1 
ATOM   1466 O  O     . GLY B 1 15  ? 20.909 16.213  17.966  1.00 16.78 ? 15  GLY B O     1 
ATOM   1467 N  N     . LYS B 1 16  ? 22.857 16.063  19.091  1.00 13.77 ? 16  LYS B N     1 
ATOM   1468 C  CA    . LYS B 1 16  ? 22.364 14.988  19.966  1.00 15.65 ? 16  LYS B CA    1 
ATOM   1469 C  C     . LYS B 1 16  ? 21.136 15.412  20.763  1.00 20.17 ? 16  LYS B C     1 
ATOM   1470 O  O     . LYS B 1 16  ? 20.151 14.658  20.876  1.00 18.13 ? 16  LYS B O     1 
ATOM   1471 C  CB    . LYS B 1 16  ? 23.464 14.532  20.928  1.00 17.46 ? 16  LYS B CB    1 
ATOM   1472 C  CG    . LYS B 1 16  ? 24.697 13.940  20.216  1.00 16.28 ? 16  LYS B CG    1 
ATOM   1473 C  CD    . LYS B 1 16  ? 25.733 13.418  21.221  1.00 15.05 ? 16  LYS B CD    1 
ATOM   1474 C  CE    . LYS B 1 16  ? 26.265 14.525  22.147  1.00 15.41 ? 16  LYS B CE    1 
ATOM   1475 N  NZ    . LYS B 1 16  ? 26.903 15.683  21.401  1.00 14.24 ? 16  LYS B NZ    1 
ATOM   1476 N  N     . SER B 1 17  ? 21.196 16.601  21.369  1.00 13.86 ? 17  SER B N     1 
ATOM   1477 C  CA    . SER B 1 17  ? 20.090 17.048  22.203  1.00 15.07 ? 17  SER B CA    1 
ATOM   1478 C  C     . SER B 1 17  ? 18.872 17.387  21.350  1.00 18.56 ? 17  SER B C     1 
ATOM   1479 O  O     . SER B 1 17  ? 17.737 17.099  21.739  1.00 17.95 ? 17  SER B O     1 
ATOM   1480 C  CB    . SER B 1 17  ? 20.521 18.266  23.036  1.00 18.73 ? 17  SER B CB    1 
ATOM   1481 O  OG    . SER B 1 17  ? 21.540 17.916  23.966  1.00 15.80 ? 17  SER B OG    1 
ATOM   1482 N  N     . ALA B 1 18  ? 19.084 18.035  20.211  1.00 17.64 ? 18  ALA B N     1 
ATOM   1483 C  CA    . ALA B 1 18  ? 17.977 18.349  19.315  1.00 19.22 ? 18  ALA B CA    1 
ATOM   1484 C  C     . ALA B 1 18  ? 17.261 17.086  18.850  1.00 19.94 ? 18  ALA B C     1 
ATOM   1485 O  O     . ALA B 1 18  ? 16.028 17.047  18.812  1.00 20.86 ? 18  ALA B O     1 
ATOM   1486 C  CB    . ALA B 1 18  ? 18.490 19.143  18.118  1.00 22.90 ? 18  ALA B CB    1 
ATOM   1487 N  N     . LEU B 1 19  ? 18.021 16.058  18.465  1.00 18.58 ? 19  LEU B N     1 
ATOM   1488 C  CA    . LEU B 1 19  ? 17.428 14.769  18.094  1.00 17.40 ? 19  LEU B CA    1 
ATOM   1489 C  C     . LEU B 1 19  ? 16.604 14.186  19.236  1.00 20.85 ? 19  LEU B C     1 
ATOM   1490 O  O     . LEU B 1 19  ? 15.462 13.737  19.040  1.00 19.68 ? 19  LEU B O     1 
ATOM   1491 C  CB    . LEU B 1 19  ? 18.528 13.791  17.690  1.00 18.05 ? 19  LEU B CB    1 
ATOM   1492 C  CG    . LEU B 1 19  ? 19.118 14.001  16.287  1.00 17.43 ? 19  LEU B CG    1 
ATOM   1493 C  CD1   . LEU B 1 19  ? 20.370 13.145  16.097  1.00 22.08 ? 19  LEU B CD1   1 
ATOM   1494 C  CD2   . LEU B 1 19  ? 18.062 13.692  15.210  1.00 22.11 ? 19  LEU B CD2   1 
ATOM   1495 N  N     . THR B 1 20  ? 17.183 14.170  20.439  1.00 17.55 ? 20  THR B N     1 
ATOM   1496 C  CA    . THR B 1 20  ? 16.496 13.588  21.588  1.00 17.70 ? 20  THR B CA    1 
ATOM   1497 C  C     . THR B 1 20  ? 15.193 14.325  21.878  1.00 23.90 ? 20  THR B C     1 
ATOM   1498 O  O     . THR B 1 20  ? 14.128 13.706  22.034  1.00 22.89 ? 20  THR B O     1 
ATOM   1499 C  CB    . THR B 1 20  ? 17.419 13.620  22.802  1.00 21.26 ? 20  THR B CB    1 
ATOM   1500 O  OG1   . THR B 1 20  ? 18.559 12.793  22.519  1.00 19.78 ? 20  THR B OG1   1 
ATOM   1501 C  CG2   . THR B 1 20  ? 16.682 13.062  24.025  1.00 23.05 ? 20  THR B CG2   1 
ATOM   1502 N  N     . ILE B 1 21  ? 15.255 15.654  21.915  1.00 18.33 ? 21  ILE B N     1 
ATOM   1503 C  CA    . ILE B 1 21  ? 14.071 16.446  22.234  1.00 23.04 ? 21  ILE B CA    1 
ATOM   1504 C  C     . ILE B 1 21  ? 13.019 16.309  21.147  1.00 26.52 ? 21  ILE B C     1 
ATOM   1505 O  O     . ILE B 1 21  ? 11.819 16.306  21.436  1.00 27.92 ? 21  ILE B O     1 
ATOM   1506 C  CB    . ILE B 1 21  ? 14.463 17.919  22.459  1.00 24.69 ? 21  ILE B CB    1 
ATOM   1507 C  CG1   . ILE B 1 21  ? 15.456 18.043  23.611  1.00 24.49 ? 21  ILE B CG1   1 
ATOM   1508 C  CG2   . ILE B 1 21  ? 13.217 18.795  22.677  1.00 27.27 ? 21  ILE B CG2   1 
ATOM   1509 C  CD1   . ILE B 1 21  ? 14.920 17.604  24.915  1.00 32.86 ? 21  ILE B CD1   1 
ATOM   1510 N  N     . GLN B 1 22  ? 13.433 16.210  19.881  1.00 25.01 ? 22  GLN B N     1 
ATOM   1511 C  CA    . GLN B 1 22  ? 12.451 15.971  18.828  1.00 25.83 ? 22  GLN B CA    1 
ATOM   1512 C  C     . GLN B 1 22  ? 11.713 14.665  19.066  1.00 29.35 ? 22  GLN B C     1 
ATOM   1513 O  O     . GLN B 1 22  ? 10.494 14.592  18.869  1.00 27.78 ? 22  GLN B O     1 
ATOM   1514 C  CB    . GLN B 1 22  ? 13.122 15.937  17.458  1.00 24.11 ? 22  GLN B CB    1 
ATOM   1515 C  CG    . GLN B 1 22  ? 13.145 17.246  16.698  1.00 32.09 ? 22  GLN B CG    1 
ATOM   1516 C  CD    . GLN B 1 22  ? 11.790 17.645  16.109  1.00 29.32 ? 22  GLN B CD    1 
ATOM   1517 O  OE1   . GLN B 1 22  ? 10.744 17.110  16.479  1.00 29.81 ? 22  GLN B OE1   1 
ATOM   1518 N  NE2   . GLN B 1 22  ? 11.819 18.564  15.157  1.00 27.62 ? 22  GLN B NE2   1 
ATOM   1519 N  N     . LEU B 1 23  ? 12.435 13.609  19.462  1.00 25.12 ? 23  LEU B N     1 
ATOM   1520 C  CA    . LEU B 1 23  ? 11.740 12.353  19.745  1.00 26.74 ? 23  LEU B CA    1 
ATOM   1521 C  C     . LEU B 1 23  ? 10.798 12.494  20.944  1.00 33.20 ? 23  LEU B C     1 
ATOM   1522 O  O     . LEU B 1 23  ? 9.665  11.997  20.915  1.00 33.62 ? 23  LEU B O     1 
ATOM   1523 C  CB    . LEU B 1 23  ? 12.741 11.220  19.986  1.00 24.52 ? 23  LEU B CB    1 
ATOM   1524 C  CG    . LEU B 1 23  ? 12.078 9.841   20.083  1.00 30.66 ? 23  LEU B CG    1 
ATOM   1525 C  CD1   . LEU B 1 23  ? 11.714 9.302   18.707  1.00 30.01 ? 23  LEU B CD1   1 
ATOM   1526 C  CD2   . LEU B 1 23  ? 12.961 8.873   20.830  1.00 28.66 ? 23  LEU B CD2   1 
ATOM   1527 N  N     . ILE B 1 24  ? 11.245 13.166  22.005  1.00 28.11 ? 24  ILE B N     1 
ATOM   1528 C  CA    . ILE B 1 24  ? 10.478 13.199  23.252  1.00 33.05 ? 24  ILE B CA    1 
ATOM   1529 C  C     . ILE B 1 24  ? 9.268  14.124  23.130  1.00 37.78 ? 24  ILE B C     1 
ATOM   1530 O  O     . ILE B 1 24  ? 8.148  13.760  23.503  1.00 39.18 ? 24  ILE B O     1 
ATOM   1531 C  CB    . ILE B 1 24  ? 11.372 13.637  24.428  1.00 36.02 ? 24  ILE B CB    1 
ATOM   1532 C  CG1   . ILE B 1 24  ? 12.544 12.672  24.647  1.00 31.70 ? 24  ILE B CG1   1 
ATOM   1533 C  CG2   . ILE B 1 24  ? 10.534 13.749  25.690  1.00 37.48 ? 24  ILE B CG2   1 
ATOM   1534 C  CD1   . ILE B 1 24  ? 12.144 11.262  24.980  1.00 32.23 ? 24  ILE B CD1   1 
ATOM   1535 N  N     . GLN B 1 25  ? 9.486  15.344  22.643  1.00 31.24 ? 25  GLN B N     1 
ATOM   1536 C  CA    . GLN B 1 25  ? 8.505  16.424  22.679  1.00 40.65 ? 25  GLN B CA    1 
ATOM   1537 C  C     . GLN B 1 25  ? 7.990  16.856  21.313  1.00 40.03 ? 25  GLN B C     1 
ATOM   1538 O  O     . GLN B 1 25  ? 7.131  17.742  21.252  1.00 42.21 ? 25  GLN B O     1 
ATOM   1539 C  CB    . GLN B 1 25  ? 9.102  17.641  23.397  1.00 36.37 ? 25  GLN B CB    1 
ATOM   1540 C  CG    . GLN B 1 25  ? 9.490  17.331  24.815  1.00 42.46 ? 25  GLN B CG    1 
ATOM   1541 C  CD    . GLN B 1 25  ? 10.077 18.516  25.533  1.00 48.93 ? 25  GLN B CD    1 
ATOM   1542 O  OE1   . GLN B 1 25  ? 10.174 19.616  24.979  1.00 53.30 ? 25  GLN B OE1   1 
ATOM   1543 N  NE2   . GLN B 1 25  ? 10.480 18.304  26.778  1.00 52.87 ? 25  GLN B NE2   1 
ATOM   1544 N  N     . ASN B 1 26  ? 8.530  16.310  20.225  1.00 34.80 ? 26  ASN B N     1 
ATOM   1545 C  CA    . ASN B 1 26  ? 8.006  16.502  18.872  1.00 40.25 ? 26  ASN B CA    1 
ATOM   1546 C  C     . ASN B 1 26  ? 8.151  17.933  18.377  1.00 42.08 ? 26  ASN B C     1 
ATOM   1547 O  O     . ASN B 1 26  ? 7.317  18.421  17.610  1.00 42.39 ? 26  ASN B O     1 
ATOM   1548 C  CB    . ASN B 1 26  ? 6.550  16.053  18.760  1.00 42.95 ? 26  ASN B CB    1 
ATOM   1549 C  CG    . ASN B 1 26  ? 6.435  14.597  18.421  1.00 50.03 ? 26  ASN B CG    1 
ATOM   1550 O  OD1   . ASN B 1 26  ? 6.480  13.751  19.304  1.00 54.53 ? 26  ASN B OD1   1 
ATOM   1551 N  ND2   . ASN B 1 26  ? 6.325  14.287  17.130  1.00 50.72 ? 26  ASN B ND2   1 
ATOM   1552 N  N     . HIS B 1 27  ? 9.201  18.624  18.799  1.00 37.69 ? 27  HIS B N     1 
ATOM   1553 C  CA    . HIS B 1 27  ? 9.474  19.937  18.243  1.00 37.96 ? 27  HIS B CA    1 
ATOM   1554 C  C     . HIS B 1 27  ? 10.965 20.212  18.351  1.00 34.67 ? 27  HIS B C     1 
ATOM   1555 O  O     . HIS B 1 27  ? 11.677 19.597  19.150  1.00 30.44 ? 27  HIS B O     1 
ATOM   1556 C  CB    . HIS B 1 27  ? 8.635  21.028  18.913  1.00 41.72 ? 27  HIS B CB    1 
ATOM   1557 C  CG    . HIS B 1 27  ? 9.142  21.450  20.252  1.00 43.30 ? 27  HIS B CG    1 
ATOM   1558 N  ND1   . HIS B 1 27  ? 8.813  20.782  21.413  1.00 51.68 ? 27  HIS B ND1   1 
ATOM   1559 C  CD2   . HIS B 1 27  ? 9.949  22.473  20.620  1.00 49.68 ? 27  HIS B CD2   1 
ATOM   1560 C  CE1   . HIS B 1 27  ? 9.399  21.374  22.439  1.00 48.67 ? 27  HIS B CE1   1 
ATOM   1561 N  NE2   . HIS B 1 27  ? 10.095 22.403  21.985  1.00 48.67 ? 27  HIS B NE2   1 
ATOM   1562 N  N     . PHE B 1 28  ? 11.426 21.120  17.497  1.00 31.41 ? 28  PHE B N     1 
ATOM   1563 C  CA    . PHE B 1 28  ? 12.839 21.467  17.381  1.00 33.71 ? 28  PHE B CA    1 
ATOM   1564 C  C     . PHE B 1 28  ? 13.175 22.548  18.404  1.00 36.93 ? 28  PHE B C     1 
ATOM   1565 O  O     . PHE B 1 28  ? 12.622 23.650  18.355  1.00 35.90 ? 28  PHE B O     1 
ATOM   1566 C  CB    . PHE B 1 28  ? 13.140 21.929  15.957  1.00 32.88 ? 28  PHE B CB    1 
ATOM   1567 C  CG    . PHE B 1 28  ? 14.555 22.390  15.745  1.00 30.81 ? 28  PHE B CG    1 
ATOM   1568 C  CD1   . PHE B 1 28  ? 15.622 21.537  15.996  1.00 32.27 ? 28  PHE B CD1   1 
ATOM   1569 C  CD2   . PHE B 1 28  ? 14.819 23.665  15.267  1.00 32.04 ? 28  PHE B CD2   1 
ATOM   1570 C  CE1   . PHE B 1 28  ? 16.926 21.957  15.793  1.00 31.64 ? 28  PHE B CE1   1 
ATOM   1571 C  CE2   . PHE B 1 28  ? 16.124 24.088  15.056  1.00 36.88 ? 28  PHE B CE2   1 
ATOM   1572 C  CZ    . PHE B 1 28  ? 17.179 23.228  15.319  1.00 35.58 ? 28  PHE B CZ    1 
ATOM   1573 N  N     . VAL B 1 29  ? 14.054 22.226  19.352  1.00 36.26 ? 29  VAL B N     1 
ATOM   1574 C  CA    . VAL B 1 29  ? 14.583 23.206  20.296  1.00 34.17 ? 29  VAL B CA    1 
ATOM   1575 C  C     . VAL B 1 29  ? 15.958 23.635  19.802  1.00 38.46 ? 29  VAL B C     1 
ATOM   1576 O  O     . VAL B 1 29  ? 16.897 22.827  19.774  1.00 35.09 ? 29  VAL B O     1 
ATOM   1577 C  CB    . VAL B 1 29  ? 14.647 22.639  21.720  1.00 36.11 ? 29  VAL B CB    1 
ATOM   1578 C  CG1   . VAL B 1 29  ? 15.382 23.603  22.643  1.00 35.72 ? 29  VAL B CG1   1 
ATOM   1579 C  CG2   . VAL B 1 29  ? 13.247 22.383  22.237  1.00 37.33 ? 29  VAL B CG2   1 
ATOM   1580 N  N     . ASP B 1 30  ? 16.096 24.911  19.446  1.00 37.77 ? 30  ASP B N     1 
ATOM   1581 C  CA    . ASP B 1 30  ? 17.424 25.412  18.998  1.00 36.42 ? 30  ASP B CA    1 
ATOM   1582 C  C     . ASP B 1 30  ? 18.251 25.874  20.201  1.00 40.95 ? 30  ASP B C     1 
ATOM   1583 O  O     . ASP B 1 30  ? 17.645 26.447  21.135  1.00 49.49 ? 30  ASP B O     1 
ATOM   1584 C  CB    . ASP B 1 30  ? 17.288 26.510  17.955  1.00 34.08 ? 30  ASP B CB    1 
ATOM   1585 C  CG    . ASP B 1 30  ? 18.546 27.334  17.717  1.00 38.75 ? 30  ASP B CG    1 
ATOM   1586 O  OD1   . ASP B 1 30  ? 19.565 26.743  17.302  1.00 32.82 ? 30  ASP B OD1   1 
ATOM   1587 O  OD2   . ASP B 1 30  ? 18.499 28.557  17.962  1.00 43.48 ? 30  ASP B OD2   1 
ATOM   1588 N  N     . GLU B 1 31  ? 19.559 25.596  20.199  1.00 38.17 ? 31  GLU B N     1 
ATOM   1589 C  CA    . GLU B 1 31  ? 20.482 26.101  21.257  1.00 32.76 ? 31  GLU B CA    1 
ATOM   1590 C  C     . GLU B 1 31  ? 20.199 25.500  22.645  1.00 29.91 ? 31  GLU B C     1 
ATOM   1591 O  O     . GLU B 1 31  ? 20.428 26.220  23.640  1.00 35.34 ? 31  GLU B O     1 
ATOM   1592 C  CB    . GLU B 1 31  ? 20.470 27.631  21.300  1.00 26.43 ? 31  GLU B CB    1 
ATOM   1593 C  CG    . GLU B 1 31  ? 21.435 28.260  20.299  1.00 30.03 ? 31  GLU B CG    1 
ATOM   1594 C  CD    . GLU B 1 31  ? 22.782 27.563  20.224  1.00 26.49 ? 31  GLU B CD    1 
ATOM   1595 O  OE1   . GLU B 1 31  ? 23.486 27.514  21.255  1.00 26.91 ? 31  GLU B OE1   1 
ATOM   1596 O  OE2   . GLU B 1 31  ? 23.131 27.074  19.130  1.00 24.30 ? 31  GLU B OE2   1 
ATOM   1597 N  N     . TYR B 1 32  ? 19.736 24.249  22.728  1.00 26.51 ? 32  TYR B N     1 
ATOM   1598 C  CA    . TYR B 1 32  ? 19.607 23.613  24.033  1.00 22.85 ? 32  TYR B CA    1 
ATOM   1599 C  C     . TYR B 1 32  ? 20.965 23.606  24.725  1.00 24.44 ? 32  TYR B C     1 
ATOM   1600 O  O     . TYR B 1 32  ? 21.980 23.298  24.094  1.00 24.14 ? 32  TYR B O     1 
ATOM   1601 C  CB    . TYR B 1 32  ? 19.097 22.183  23.860  1.00 26.94 ? 32  TYR B CB    1 
ATOM   1602 C  CG    . TYR B 1 32  ? 18.717 21.480  25.141  1.00 25.33 ? 32  TYR B CG    1 
ATOM   1603 C  CD1   . TYR B 1 32  ? 17.474 21.692  25.715  1.00 32.22 ? 32  TYR B CD1   1 
ATOM   1604 C  CD2   . TYR B 1 32  ? 19.586 20.587  25.763  1.00 24.62 ? 32  TYR B CD2   1 
ATOM   1605 C  CE1   . TYR B 1 32  ? 17.103 21.056  26.880  1.00 35.21 ? 32  TYR B CE1   1 
ATOM   1606 C  CE2   . TYR B 1 32  ? 19.221 19.929  26.945  1.00 28.11 ? 32  TYR B CE2   1 
ATOM   1607 C  CZ    . TYR B 1 32  ? 17.967 20.180  27.494  1.00 35.60 ? 32  TYR B CZ    1 
ATOM   1608 O  OH    . TYR B 1 32  ? 17.555 19.559  28.654  1.00 36.41 ? 32  TYR B OH    1 
ATOM   1609 N  N     . ASP B 1 33  ? 20.977 23.945  26.034  1.00 20.15 ? 33  ASP B N     1 
ATOM   1610 C  CA    . ASP B 1 33  ? 22.209 24.049  26.829  1.00 22.00 ? 33  ASP B CA    1 
ATOM   1611 C  C     . ASP B 1 33  ? 23.226 22.971  26.442  1.00 22.60 ? 33  ASP B C     1 
ATOM   1612 O  O     . ASP B 1 33  ? 22.979 21.775  26.639  1.00 23.78 ? 33  ASP B O     1 
ATOM   1613 C  CB    . ASP B 1 33  ? 21.862 23.993  28.324  1.00 21.14 ? 33  ASP B CB    1 
ATOM   1614 C  CG    . ASP B 1 33  ? 23.068 24.252  29.226  1.00 24.88 ? 33  ASP B CG    1 
ATOM   1615 O  OD1   . ASP B 1 33  ? 24.180 23.810  28.909  1.00 20.75 ? 33  ASP B OD1   1 
ATOM   1616 O  OD2   . ASP B 1 33  ? 22.900 24.924  30.271  1.00 28.15 ? 33  ASP B OD2   1 
ATOM   1617 N  N     . PRO B 1 34  ? 24.360 23.364  25.846  1.00 18.79 ? 34  PRO B N     1 
ATOM   1618 C  CA    . PRO B 1 34  ? 25.330 22.375  25.346  1.00 17.72 ? 34  PRO B CA    1 
ATOM   1619 C  C     . PRO B 1 34  ? 25.998 21.545  26.415  1.00 19.35 ? 34  PRO B C     1 
ATOM   1620 O  O     . PRO B 1 34  ? 26.626 20.531  26.062  1.00 19.61 ? 34  PRO B O     1 
ATOM   1621 C  CB    . PRO B 1 34  ? 26.356 23.235  24.572  1.00 20.97 ? 34  PRO B CB    1 
ATOM   1622 C  CG    . PRO B 1 34  ? 25.977 24.640  24.819  1.00 25.08 ? 34  PRO B CG    1 
ATOM   1623 C  CD    . PRO B 1 34  ? 24.576 24.699  25.254  1.00 21.89 ? 34  PRO B CD    1 
ATOM   1624 N  N     . THR B 1 35  ? 25.898 21.926  27.700  1.00 20.07 ? 35  THR B N     1 
ATOM   1625 C  CA    . THR B 1 35  ? 26.595 21.217  28.768  1.00 17.98 ? 35  THR B CA    1 
ATOM   1626 C  C     . THR B 1 35  ? 25.724 20.236  29.544  1.00 20.26 ? 35  THR B C     1 
ATOM   1627 O  O     . THR B 1 35  ? 26.262 19.487  30.364  1.00 21.87 ? 35  THR B O     1 
ATOM   1628 C  CB    . THR B 1 35  ? 27.207 22.210  29.769  1.00 21.79 ? 35  THR B CB    1 
ATOM   1629 O  OG1   . THR B 1 35  ? 26.149 22.889  30.470  1.00 23.59 ? 35  THR B OG1   1 
ATOM   1630 C  CG2   . THR B 1 35  ? 28.083 23.214  29.040  1.00 22.19 ? 35  THR B CG2   1 
ATOM   1631 N  N     . ILE B 1 36  ? 24.414 20.207  29.322  1.00 18.55 ? 36  ILE B N     1 
ATOM   1632 C  CA    . ILE B 1 36  ? 23.538 19.376  30.148  1.00 20.43 ? 36  ILE B CA    1 
ATOM   1633 C  C     . ILE B 1 36  ? 23.544 17.941  29.629  1.00 19.03 ? 36  ILE B C     1 
ATOM   1634 O  O     . ILE B 1 36  ? 23.188 17.684  28.475  1.00 19.46 ? 36  ILE B O     1 
ATOM   1635 C  CB    . ILE B 1 36  ? 22.105 19.930  30.189  1.00 23.88 ? 36  ILE B CB    1 
ATOM   1636 C  CG1   . ILE B 1 36  ? 22.073 21.338  30.801  1.00 25.48 ? 36  ILE B CG1   1 
ATOM   1637 C  CG2   . ILE B 1 36  ? 21.182 18.952  30.943  1.00 24.12 ? 36  ILE B CG2   1 
ATOM   1638 C  CD1   . ILE B 1 36  ? 22.901 21.480  32.070  1.00 32.76 ? 36  ILE B CD1   1 
ATOM   1639 N  N     . GLU B 1 37  ? 23.929 17.007  30.488  1.00 18.38 ? 37  GLU B N     1 
ATOM   1640 C  CA    . GLU B 1 37  ? 23.813 15.574  30.221  1.00 17.97 ? 37  GLU B CA    1 
ATOM   1641 C  C     . GLU B 1 37  ? 22.670 15.061  31.070  1.00 20.06 ? 37  GLU B C     1 
ATOM   1642 O  O     . GLU B 1 37  ? 22.666 15.294  32.280  1.00 20.82 ? 37  GLU B O     1 
ATOM   1643 C  CB    . GLU B 1 37  ? 25.101 14.843  30.585  1.00 18.32 ? 37  GLU B CB    1 
ATOM   1644 C  CG    . GLU B 1 37  ? 25.021 13.338  30.455  1.00 18.41 ? 37  GLU B CG    1 
ATOM   1645 C  CD    . GLU B 1 37  ? 26.403 12.719  30.504  1.00 23.07 ? 37  GLU B CD    1 
ATOM   1646 O  OE1   . GLU B 1 37  ? 27.073 12.676  29.456  1.00 18.97 ? 37  GLU B OE1   1 
ATOM   1647 O  OE2   . GLU B 1 37  ? 26.824 12.304  31.604  1.00 25.80 ? 37  GLU B OE2   1 
ATOM   1648 N  N     . ASP B 1 38  ? 21.693 14.396  30.453  1.00 20.27 ? 38  ASP B N     1 
ATOM   1649 C  CA    . ASP B 1 38  ? 20.535 13.974  31.249  1.00 19.38 ? 38  ASP B CA    1 
ATOM   1650 C  C     . ASP B 1 38  ? 19.848 12.846  30.507  1.00 22.81 ? 38  ASP B C     1 
ATOM   1651 O  O     . ASP B 1 38  ? 20.138 12.584  29.338  1.00 19.12 ? 38  ASP B O     1 
ATOM   1652 C  CB    . ASP B 1 38  ? 19.553 15.136  31.498  1.00 20.52 ? 38  ASP B CB    1 
ATOM   1653 C  CG    . ASP B 1 38  ? 18.681 14.950  32.765  1.00 27.10 ? 38  ASP B CG    1 
ATOM   1654 O  OD1   . ASP B 1 38  ? 18.782 13.914  33.461  1.00 26.30 ? 38  ASP B OD1   1 
ATOM   1655 O  OD2   . ASP B 1 38  ? 17.895 15.874  33.066  1.00 33.73 ? 38  ASP B OD2   1 
ATOM   1656 N  N     . SER B 1 39  ? 18.902 12.201  31.185  1.00 19.23 ? 39  SER B N     1 
ATOM   1657 C  CA    . SER B 1 39  ? 18.150 11.119  30.569  1.00 19.84 ? 39  SER B CA    1 
ATOM   1658 C  C     . SER B 1 39  ? 16.677 11.488  30.491  1.00 24.44 ? 39  SER B C     1 
ATOM   1659 O  O     . SER B 1 39  ? 16.151 12.191  31.358  1.00 24.59 ? 39  SER B O     1 
ATOM   1660 C  CB    . SER B 1 39  ? 18.367 9.798   31.337  1.00 26.58 ? 39  SER B CB    1 
ATOM   1661 O  OG    . SER B 1 39  ? 17.869 9.889   32.652  1.00 38.20 ? 39  SER B OG    1 
ATOM   1662 N  N     . TYR B 1 40  ? 16.035 11.045  29.418  1.00 21.13 ? 40  TYR B N     1 
ATOM   1663 C  CA    . TYR B 1 40  ? 14.664 11.413  29.074  1.00 24.90 ? 40  TYR B CA    1 
ATOM   1664 C  C     . TYR B 1 40  ? 13.911 10.136  28.762  1.00 25.75 ? 40  TYR B C     1 
ATOM   1665 O  O     . TYR B 1 40  ? 14.479 9.210   28.183  1.00 26.42 ? 40  TYR B O     1 
ATOM   1666 C  CB    . TYR B 1 40  ? 14.605 12.367  27.868  1.00 26.21 ? 40  TYR B CB    1 
ATOM   1667 C  CG    . TYR B 1 40  ? 15.501 13.582  28.055  1.00 27.11 ? 40  TYR B CG    1 
ATOM   1668 C  CD1   . TYR B 1 40  ? 16.857 13.524  27.749  1.00 22.18 ? 40  TYR B CD1   1 
ATOM   1669 C  CD2   . TYR B 1 40  ? 14.999 14.761  28.582  1.00 30.11 ? 40  TYR B CD2   1 
ATOM   1670 C  CE1   . TYR B 1 40  ? 17.684 14.616  27.947  1.00 24.83 ? 40  TYR B CE1   1 
ATOM   1671 C  CE2   . TYR B 1 40  ? 15.821 15.869  28.782  1.00 29.99 ? 40  TYR B CE2   1 
ATOM   1672 C  CZ    . TYR B 1 40  ? 17.159 15.791  28.462  1.00 28.57 ? 40  TYR B CZ    1 
ATOM   1673 O  OH    . TYR B 1 40  ? 17.994 16.883  28.661  1.00 28.61 ? 40  TYR B OH    1 
ATOM   1674 N  N     . ARG B 1 41  ? 12.643 10.087  29.142  1.00 26.60 ? 41  ARG B N     1 
ATOM   1675 C  CA    . ARG B 1 41  ? 11.857 8.865   29.046  1.00 26.49 ? 41  ARG B CA    1 
ATOM   1676 C  C     . ARG B 1 41  ? 10.687 9.077   28.105  1.00 28.96 ? 41  ARG B C     1 
ATOM   1677 O  O     . ARG B 1 41  ? 10.089 10.159  28.060  1.00 27.73 ? 41  ARG B O     1 
ATOM   1678 C  CB    . ARG B 1 41  ? 11.358 8.419   30.398  1.00 30.14 ? 41  ARG B CB    1 
ATOM   1679 C  CG    . ARG B 1 41  ? 12.459 7.818   31.209  1.00 36.23 ? 41  ARG B CG    1 
ATOM   1680 C  CD    . ARG B 1 41  ? 11.980 7.522   32.597  1.00 43.45 ? 41  ARG B CD    1 
ATOM   1681 N  NE    . ARG B 1 41  ? 12.997 6.759   33.303  1.00 52.86 ? 41  ARG B NE    1 
ATOM   1682 C  CZ    . ARG B 1 41  ? 12.878 5.489   33.662  1.00 52.74 ? 41  ARG B CZ    1 
ATOM   1683 N  NH1   . ARG B 1 41  ? 11.786 4.792   33.390  1.00 53.80 ? 41  ARG B NH1   1 
ATOM   1684 N  NH2   . ARG B 1 41  ? 13.887 4.900   34.298  1.00 54.77 ? 41  ARG B NH2   1 
ATOM   1685 N  N     . LYS B 1 42  ? 10.402 8.044   27.321  1.00 27.10 ? 42  LYS B N     1 
ATOM   1686 C  CA    . LYS B 1 42  ? 9.309  8.075   26.363  1.00 28.58 ? 42  LYS B CA    1 
ATOM   1687 C  C     . LYS B 1 42  ? 8.636  6.715   26.305  1.00 26.93 ? 42  LYS B C     1 
ATOM   1688 O  O     . LYS B 1 42  ? 9.321  5.711   26.115  1.00 26.46 ? 42  LYS B O     1 
ATOM   1689 C  CB    . LYS B 1 42  ? 9.867  8.434   24.990  1.00 28.42 ? 42  LYS B CB    1 
ATOM   1690 C  CG    . LYS B 1 42  ? 8.911  8.256   23.861  1.00 35.18 ? 42  LYS B CG    1 
ATOM   1691 C  CD    . LYS B 1 42  ? 8.265  9.569   23.491  1.00 37.50 ? 42  LYS B CD    1 
ATOM   1692 C  CE    . LYS B 1 42  ? 7.697  9.482   22.087  1.00 43.69 ? 42  LYS B CE    1 
ATOM   1693 N  NZ    . LYS B 1 42  ? 6.452  10.296  21.951  1.00 46.74 ? 42  LYS B NZ    1 
ATOM   1694 N  N     . GLN B 1 43  ? 7.306  6.670   26.402  1.00 27.54 ? 43  GLN B N     1 
ATOM   1695 C  CA    . GLN B 1 43  ? 6.576  5.422   26.176  1.00 25.73 ? 43  GLN B CA    1 
ATOM   1696 C  C     . GLN B 1 43  ? 6.010  5.409   24.757  1.00 27.62 ? 43  GLN B C     1 
ATOM   1697 O  O     . GLN B 1 43  ? 5.308  6.343   24.362  1.00 26.81 ? 43  GLN B O     1 
ATOM   1698 C  CB    . GLN B 1 43  ? 5.452  5.242   27.192  1.00 31.53 ? 43  GLN B CB    1 
ATOM   1699 C  CG    . GLN B 1 43  ? 4.703  3.929   27.016  1.00 36.84 ? 43  GLN B CG    1 
ATOM   1700 C  CD    . GLN B 1 43  ? 3.610  3.755   28.043  1.00 42.62 ? 43  GLN B CD    1 
ATOM   1701 O  OE1   . GLN B 1 43  ? 2.483  3.384   27.704  1.00 43.36 ? 43  GLN B OE1   1 
ATOM   1702 N  NE2   . GLN B 1 43  ? 3.930  4.034   29.307  1.00 40.54 ? 43  GLN B NE2   1 
ATOM   1703 N  N     . VAL B 1 44  ? 6.296  4.348   23.999  1.00 23.72 ? 44  VAL B N     1 
ATOM   1704 C  CA    . VAL B 1 44  ? 5.845  4.257   22.612  1.00 24.14 ? 44  VAL B CA    1 
ATOM   1705 C  C     . VAL B 1 44  ? 5.590  2.795   22.268  1.00 26.95 ? 44  VAL B C     1 
ATOM   1706 O  O     . VAL B 1 44  ? 6.212  1.891   22.826  1.00 27.04 ? 44  VAL B O     1 
ATOM   1707 C  CB    . VAL B 1 44  ? 6.884  4.894   21.658  1.00 30.15 ? 44  VAL B CB    1 
ATOM   1708 C  CG1   . VAL B 1 44  ? 8.232  4.201   21.821  1.00 30.23 ? 44  VAL B CG1   1 
ATOM   1709 C  CG2   . VAL B 1 44  ? 6.401  4.873   20.208  1.00 34.00 ? 44  VAL B CG2   1 
ATOM   1710 N  N     . VAL B 1 45  ? 4.660  2.558   21.348  1.00 23.63 ? 45  VAL B N     1 
ATOM   1711 C  CA    . VAL B 1 45  ? 4.378  1.210   20.864  1.00 22.28 ? 45  VAL B CA    1 
ATOM   1712 C  C     . VAL B 1 45  ? 5.159  1.011   19.574  1.00 26.63 ? 45  VAL B C     1 
ATOM   1713 O  O     . VAL B 1 45  ? 4.957  1.746   18.604  1.00 24.62 ? 45  VAL B O     1 
ATOM   1714 C  CB    . VAL B 1 45  ? 2.872  0.991   20.639  1.00 23.70 ? 45  VAL B CB    1 
ATOM   1715 C  CG1   . VAL B 1 45  ? 2.625  -0.419  20.125  1.00 24.76 ? 45  VAL B CG1   1 
ATOM   1716 C  CG2   . VAL B 1 45  ? 2.099  1.256   21.929  1.00 25.44 ? 45  VAL B CG2   1 
ATOM   1717 N  N     . ILE B 1 46  ? 6.052  0.020   19.554  1.00 22.09 ? 46  ILE B N     1 
ATOM   1718 C  CA    . ILE B 1 46  ? 6.896  -0.257  18.392  1.00 26.08 ? 46  ILE B CA    1 
ATOM   1719 C  C     . ILE B 1 46  ? 6.662  -1.703  17.969  1.00 26.23 ? 46  ILE B C     1 
ATOM   1720 O  O     . ILE B 1 46  ? 6.887  -2.627  18.762  1.00 24.75 ? 46  ILE B O     1 
ATOM   1721 C  CB    . ILE B 1 46  ? 8.386  -0.009  18.699  1.00 26.77 ? 46  ILE B CB    1 
ATOM   1722 C  CG1   . ILE B 1 46  ? 8.615  1.456   19.078  1.00 28.33 ? 46  ILE B CG1   1 
ATOM   1723 C  CG2   . ILE B 1 46  ? 9.244  -0.395  17.512  1.00 28.21 ? 46  ILE B CG2   1 
ATOM   1724 C  CD1   . ILE B 1 46  ? 9.929  1.694   19.836  1.00 30.31 ? 46  ILE B CD1   1 
ATOM   1725 N  N     . ASP B 1 47  ? 6.233  -1.897  16.715  1.00 26.23 ? 47  ASP B N     1 
ATOM   1726 C  CA    . ASP B 1 47  ? 5.905  -3.224  16.175  1.00 28.50 ? 47  ASP B CA    1 
ATOM   1727 C  C     . ASP B 1 47  ? 5.028  -4.014  17.142  1.00 28.04 ? 47  ASP B C     1 
ATOM   1728 O  O     . ASP B 1 47  ? 5.260  -5.196  17.405  1.00 30.19 ? 47  ASP B O     1 
ATOM   1729 C  CB    . ASP B 1 47  ? 7.166  -4.019  15.840  1.00 30.74 ? 47  ASP B CB    1 
ATOM   1730 C  CG    . ASP B 1 47  ? 8.111  -3.251  14.963  1.00 30.33 ? 47  ASP B CG    1 
ATOM   1731 O  OD1   . ASP B 1 47  ? 7.619  -2.495  14.113  1.00 32.45 ? 47  ASP B OD1   1 
ATOM   1732 O  OD2   . ASP B 1 47  ? 9.339  -3.380  15.142  1.00 33.10 ? 47  ASP B OD2   1 
ATOM   1733 N  N     . GLY B 1 48  ? 4.016  -3.341  17.688  1.00 27.64 ? 48  GLY B N     1 
ATOM   1734 C  CA    . GLY B 1 48  ? 3.054  -3.991  18.562  1.00 27.90 ? 48  GLY B CA    1 
ATOM   1735 C  C     . GLY B 1 48  ? 3.486  -4.200  19.996  1.00 29.56 ? 48  GLY B C     1 
ATOM   1736 O  O     . GLY B 1 48  ? 2.725  -4.789  20.770  1.00 25.70 ? 48  GLY B O     1 
ATOM   1737 N  N     . GLU B 1 49  ? 4.682  -3.757  20.386  1.00 25.64 ? 49  GLU B N     1 
ATOM   1738 C  CA    . GLU B 1 49  ? 5.172  -3.986  21.736  1.00 24.06 ? 49  GLU B CA    1 
ATOM   1739 C  C     . GLU B 1 49  ? 5.265  -2.649  22.453  1.00 26.37 ? 49  GLU B C     1 
ATOM   1740 O  O     . GLU B 1 49  ? 5.837  -1.698  21.911  1.00 24.59 ? 49  GLU B O     1 
ATOM   1741 C  CB    . GLU B 1 49  ? 6.535  -4.684  21.714  1.00 29.40 ? 49  GLU B CB    1 
ATOM   1742 C  CG    . GLU B 1 49  ? 7.338  -4.545  23.007  1.00 34.08 ? 49  GLU B CG    1 
ATOM   1743 C  CD    . GLU B 1 49  ? 8.709  -5.208  22.911  1.00 48.93 ? 49  GLU B CD    1 
ATOM   1744 O  OE1   . GLU B 1 49  ? 8.788  -6.441  23.112  1.00 52.85 ? 49  GLU B OE1   1 
ATOM   1745 O  OE2   . GLU B 1 49  ? 9.698  -4.497  22.613  1.00 45.13 ? 49  GLU B OE2   1 
ATOM   1746 N  N     . THR B 1 50  ? 4.653  -2.565  23.635  1.00 22.46 ? 50  THR B N     1 
ATOM   1747 C  CA    . THR B 1 50  ? 4.702  -1.346  24.433  1.00 21.51 ? 50  THR B CA    1 
ATOM   1748 C  C     . THR B 1 50  ? 6.067  -1.233  25.104  1.00 27.87 ? 50  THR B C     1 
ATOM   1749 O  O     . THR B 1 50  ? 6.458  -2.094  25.912  1.00 30.06 ? 50  THR B O     1 
ATOM   1750 C  CB    . THR B 1 50  ? 3.583  -1.331  25.470  1.00 31.60 ? 50  THR B CB    1 
ATOM   1751 O  OG1   . THR B 1 50  ? 2.324  -1.535  24.808  1.00 30.18 ? 50  THR B OG1   1 
ATOM   1752 C  CG2   . THR B 1 50  ? 3.549  0.003   26.172  1.00 33.79 ? 50  THR B CG2   1 
ATOM   1753 N  N     . SER B 1 51  ? 6.767  -0.141  24.801  1.00 23.59 ? 51  SER B N     1 
ATOM   1754 C  CA    . SER B 1 51  ? 8.169  0.016   25.129  1.00 27.57 ? 51  SER B CA    1 
ATOM   1755 C  C     . SER B 1 51  ? 8.371  1.333   25.858  1.00 28.07 ? 51  SER B C     1 
ATOM   1756 O  O     . SER B 1 51  ? 7.726  2.343   25.553  1.00 28.04 ? 51  SER B O     1 
ATOM   1757 C  CB    . SER B 1 51  ? 9.029  -0.002  23.860  1.00 28.51 ? 51  SER B CB    1 
ATOM   1758 O  OG    . SER B 1 51  ? 8.663  -1.079  23.004  1.00 33.34 ? 51  SER B OG    1 
ATOM   1759 N  N     . LEU B 1 52  ? 9.271  1.302   26.817  1.00 24.75 ? 52  LEU B N     1 
ATOM   1760 C  CA    . LEU B 1 52  ? 9.741  2.476   27.538  1.00 23.71 ? 52  LEU B CA    1 
ATOM   1761 C  C     . LEU B 1 52  ? 11.168 2.738   27.093  1.00 24.51 ? 52  LEU B C     1 
ATOM   1762 O  O     . LEU B 1 52  ? 12.056 1.933   27.367  1.00 26.66 ? 52  LEU B O     1 
ATOM   1763 C  CB    . LEU B 1 52  ? 9.681  2.243   29.043  1.00 29.59 ? 52  LEU B CB    1 
ATOM   1764 C  CG    . LEU B 1 52  ? 10.052 3.444   29.901  1.00 33.76 ? 52  LEU B CG    1 
ATOM   1765 C  CD1   . LEU B 1 52  ? 9.106  4.617   29.690  1.00 35.41 ? 52  LEU B CD1   1 
ATOM   1766 C  CD2   . LEU B 1 52  ? 10.103 2.996   31.352  1.00 46.76 ? 52  LEU B CD2   1 
ATOM   1767 N  N     . LEU B 1 53  ? 11.386 3.852   26.407  1.00 24.72 ? 53  LEU B N     1 
ATOM   1768 C  CA    . LEU B 1 53  ? 12.722 4.257   25.994  1.00 20.60 ? 53  LEU B CA    1 
ATOM   1769 C  C     . LEU B 1 53  ? 13.287 5.202   27.047  1.00 26.22 ? 53  LEU B C     1 
ATOM   1770 O  O     . LEU B 1 53  ? 12.639 6.186   27.417  1.00 25.26 ? 53  LEU B O     1 
ATOM   1771 C  CB    . LEU B 1 53  ? 12.689 4.921   24.627  1.00 24.11 ? 53  LEU B CB    1 
ATOM   1772 C  CG    . LEU B 1 53  ? 11.934 4.172   23.520  1.00 26.05 ? 53  LEU B CG    1 
ATOM   1773 C  CD1   . LEU B 1 53  ? 12.225 4.847   22.201  1.00 29.38 ? 53  LEU B CD1   1 
ATOM   1774 C  CD2   . LEU B 1 53  ? 12.283 2.683   23.477  1.00 26.00 ? 53  LEU B CD2   1 
ATOM   1775 N  N     . ASP B 1 54  ? 14.446 4.851   27.589  1.00 22.69 ? 54  ASP B N     1 
ATOM   1776 C  CA    . ASP B 1 54  ? 15.195 5.690   28.513  1.00 20.91 ? 54  ASP B CA    1 
ATOM   1777 C  C     . ASP B 1 54  ? 16.443 6.130   27.757  1.00 21.39 ? 54  ASP B C     1 
ATOM   1778 O  O     . ASP B 1 54  ? 17.311 5.306   27.459  1.00 21.77 ? 54  ASP B O     1 
ATOM   1779 C  CB    . ASP B 1 54  ? 15.528 4.893   29.770  1.00 27.25 ? 54  ASP B CB    1 
ATOM   1780 C  CG    . ASP B 1 54  ? 16.166 5.731   30.859  1.00 38.66 ? 54  ASP B CG    1 
ATOM   1781 O  OD1   . ASP B 1 54  ? 16.703 6.818   30.574  1.00 39.54 ? 54  ASP B OD1   1 
ATOM   1782 O  OD2   . ASP B 1 54  ? 16.134 5.286   32.024  1.00 44.69 ? 54  ASP B OD2   1 
ATOM   1783 N  N     . ILE B 1 55  ? 16.534 7.413   27.427  1.00 20.52 ? 55  ILE B N     1 
ATOM   1784 C  CA    . ILE B 1 55  ? 17.507 7.913   26.462  1.00 15.77 ? 55  ILE B CA    1 
ATOM   1785 C  C     . ILE B 1 55  ? 18.476 8.811   27.203  1.00 20.20 ? 55  ILE B C     1 
ATOM   1786 O  O     . ILE B 1 55  ? 18.066 9.836   27.751  1.00 18.24 ? 55  ILE B O     1 
ATOM   1787 C  CB    . ILE B 1 55  ? 16.817 8.702   25.342  1.00 19.73 ? 55  ILE B CB    1 
ATOM   1788 C  CG1   . ILE B 1 55  ? 15.786 7.811   24.643  1.00 23.98 ? 55  ILE B CG1   1 
ATOM   1789 C  CG2   . ILE B 1 55  ? 17.878 9.261   24.381  1.00 21.63 ? 55  ILE B CG2   1 
ATOM   1790 C  CD1   . ILE B 1 55  ? 14.941 8.546   23.634  1.00 25.38 ? 55  ILE B CD1   1 
ATOM   1791 N  N     . LEU B 1 56  ? 19.749 8.440   27.216  1.00 17.01 ? 56  LEU B N     1 
ATOM   1792 C  CA    . LEU B 1 56  ? 20.794 9.254   27.827  1.00 16.99 ? 56  LEU B CA    1 
ATOM   1793 C  C     . LEU B 1 56  ? 21.409 10.147  26.758  1.00 16.90 ? 56  LEU B C     1 
ATOM   1794 O  O     . LEU B 1 56  ? 22.001 9.652   25.795  1.00 15.18 ? 56  LEU B O     1 
ATOM   1795 C  CB    . LEU B 1 56  ? 21.854 8.365   28.470  1.00 18.02 ? 56  LEU B CB    1 
ATOM   1796 C  CG    . LEU B 1 56  ? 23.127 9.014   29.040  1.00 20.39 ? 56  LEU B CG    1 
ATOM   1797 C  CD1   . LEU B 1 56  ? 22.798 10.100  29.994  1.00 24.66 ? 56  LEU B CD1   1 
ATOM   1798 C  CD2   . LEU B 1 56  ? 23.980 7.969   29.721  1.00 26.25 ? 56  LEU B CD2   1 
ATOM   1799 N  N     . ASP B 1 57  ? 21.266 11.458  26.938  1.00 15.40 ? 57  ASP B N     1 
ATOM   1800 C  CA    . ASP B 1 57  ? 21.792 12.475  26.035  1.00 15.22 ? 57  ASP B CA    1 
ATOM   1801 C  C     . ASP B 1 57  ? 23.097 12.990  26.644  1.00 18.39 ? 57  ASP B C     1 
ATOM   1802 O  O     . ASP B 1 57  ? 23.067 13.699  27.663  1.00 17.63 ? 57  ASP B O     1 
ATOM   1803 C  CB    . ASP B 1 57  ? 20.749 13.583  25.888  1.00 19.65 ? 57  ASP B CB    1 
ATOM   1804 C  CG    . ASP B 1 57  ? 21.241 14.752  25.075  1.00 18.73 ? 57  ASP B CG    1 
ATOM   1805 O  OD1   . ASP B 1 57  ? 22.158 14.560  24.240  1.00 15.91 ? 57  ASP B OD1   1 
ATOM   1806 O  OD2   . ASP B 1 57  ? 20.712 15.869  25.272  1.00 19.86 ? 57  ASP B OD2   1 
ATOM   1807 N  N     . THR B 1 58  ? 24.234 12.584  26.056  1.00 17.86 ? 58  THR B N     1 
ATOM   1808 C  CA    . THR B 1 58  ? 25.545 12.808  26.674  1.00 16.21 ? 58  THR B CA    1 
ATOM   1809 C  C     . THR B 1 58  ? 26.040 14.235  26.412  1.00 19.72 ? 58  THR B C     1 
ATOM   1810 O  O     . THR B 1 58  ? 25.683 14.869  25.408  1.00 17.36 ? 58  THR B O     1 
ATOM   1811 C  CB    . THR B 1 58  ? 26.585 11.774  26.187  1.00 15.80 ? 58  THR B CB    1 
ATOM   1812 O  OG1   . THR B 1 58  ? 26.758 11.816  24.763  1.00 15.94 ? 58  THR B OG1   1 
ATOM   1813 C  CG2   . THR B 1 58  ? 26.160 10.332  26.603  1.00 17.93 ? 58  THR B CG2   1 
ATOM   1814 N  N     . ALA B 1 59  ? 26.868 14.742  27.336  1.00 14.60 ? 59  ALA B N     1 
ATOM   1815 C  CA    . ALA B 1 59  ? 27.449 16.080  27.226  1.00 16.11 ? 59  ALA B CA    1 
ATOM   1816 C  C     . ALA B 1 59  ? 28.580 16.181  28.235  1.00 23.53 ? 59  ALA B C     1 
ATOM   1817 O  O     . ALA B 1 59  ? 28.885 15.223  28.950  1.00 24.25 ? 59  ALA B O     1 
ATOM   1818 C  CB    . ALA B 1 59  ? 26.414 17.190  27.468  1.00 17.60 ? 59  ALA B CB    1 
ATOM   1819 N  N     . GLY B 1 60  ? 29.201 17.353  28.291  1.00 20.27 ? 60  GLY B N     1 
ATOM   1820 C  CA    . GLY B 1 60  ? 30.101 17.693  29.378  1.00 22.48 ? 60  GLY B CA    1 
ATOM   1821 C  C     . GLY B 1 60  ? 31.565 17.436  29.064  1.00 24.68 ? 60  GLY B C     1 
ATOM   1822 O  O     . GLY B 1 60  ? 32.003 17.402  27.913  1.00 22.57 ? 60  GLY B O     1 
ATOM   1823 N  N     . GLN B 1 61  ? 32.335 17.254  30.135  1.00 25.97 ? 61  GLN B N     1 
ATOM   1824 C  CA    . GLN B 1 61  ? 33.786 17.158  30.034  1.00 29.00 ? 61  GLN B CA    1 
ATOM   1825 C  C     . GLN B 1 61  ? 34.232 15.770  29.618  1.00 25.86 ? 61  GLN B C     1 
ATOM   1826 O  O     . GLN B 1 61  ? 33.558 14.773  29.880  1.00 26.84 ? 61  GLN B O     1 
ATOM   1827 C  CB    . GLN B 1 61  ? 34.444 17.515  31.362  1.00 30.77 ? 61  GLN B CB    1 
ATOM   1828 C  CG    . GLN B 1 61  ? 34.061 18.886  31.817  1.00 40.55 ? 61  GLN B CG    1 
ATOM   1829 C  CD    . GLN B 1 61  ? 34.768 19.946  31.012  1.00 54.40 ? 61  GLN B CD    1 
ATOM   1830 O  OE1   . GLN B 1 61  ? 35.980 19.869  30.786  1.00 60.64 ? 61  GLN B OE1   1 
ATOM   1831 N  NE2   . GLN B 1 61  ? 34.012 20.932  30.545  1.00 54.56 ? 61  GLN B NE2   1 
ATOM   1832 N  N     . GLU B 1 62  ? 35.383 15.712  28.953  1.00 19.06 ? 62  GLU B N     1 
ATOM   1833 C  CA    . GLU B 1 62  ? 35.965 14.436  28.560  1.00 20.25 ? 62  GLU B CA    1 
ATOM   1834 C  C     . GLU B 1 62  ? 36.722 13.865  29.749  1.00 23.94 ? 62  GLU B C     1 
ATOM   1835 O  O     . GLU B 1 62  ? 37.731 14.438  30.169  1.00 26.79 ? 62  GLU B O     1 
ATOM   1836 C  CB    . GLU B 1 62  ? 36.907 14.611  27.367  1.00 19.05 ? 62  GLU B CB    1 
ATOM   1837 C  CG    . GLU B 1 62  ? 37.559 13.306  26.955  1.00 19.40 ? 62  GLU B CG    1 
ATOM   1838 C  CD    . GLU B 1 62  ? 38.353 13.439  25.660  1.00 23.08 ? 62  GLU B CD    1 
ATOM   1839 O  OE1   . GLU B 1 62  ? 38.666 14.585  25.292  1.00 23.24 ? 62  GLU B OE1   1 
ATOM   1840 O  OE2   . GLU B 1 62  ? 38.595 12.412  25.000  1.00 23.51 ? 62  GLU B OE2   1 
ATOM   1841 N  N     . GLU B 1 63  ? 36.240 12.754  30.307  1.00 23.57 ? 63  GLU B N     1 
ATOM   1842 C  CA    . GLU B 1 63  ? 36.953 12.089  31.389  1.00 22.70 ? 63  GLU B CA    1 
ATOM   1843 C  C     . GLU B 1 63  ? 36.629 10.599  31.336  1.00 27.43 ? 63  GLU B C     1 
ATOM   1844 O  O     . GLU B 1 63  ? 35.552 10.201  30.870  1.00 25.00 ? 63  GLU B O     1 
ATOM   1845 C  CB    . GLU B 1 63  ? 36.598 12.645  32.772  1.00 30.77 ? 63  GLU B CB    1 
ATOM   1846 C  CG    . GLU B 1 63  ? 35.177 12.434  33.218  1.00 39.25 ? 63  GLU B CG    1 
ATOM   1847 C  CD    . GLU B 1 63  ? 35.132 11.353  34.302  1.00 48.58 ? 63  GLU B CD    1 
ATOM   1848 O  OE1   . GLU B 1 63  ? 36.143 10.612  34.420  1.00 48.37 ? 63  GLU B OE1   1 
ATOM   1849 O  OE2   . GLU B 1 63  ? 34.132 11.261  35.050  1.00 51.51 ? 63  GLU B OE2   1 
ATOM   1850 N  N     . TYR B 1 64  ? 37.593 9.774   31.765  1.00 21.04 ? 64  TYR B N     1 
ATOM   1851 C  CA    . TYR B 1 64  ? 37.501 8.316   31.645  1.00 22.34 ? 64  TYR B CA    1 
ATOM   1852 C  C     . TYR B 1 64  ? 37.625 7.553   32.964  1.00 29.32 ? 64  TYR B C     1 
ATOM   1853 O  O     . TYR B 1 64  ? 38.535 6.733   33.127  1.00 42.96 ? 64  TYR B O     1 
ATOM   1854 C  CB    . TYR B 1 64  ? 38.567 7.801   30.669  1.00 23.50 ? 64  TYR B CB    1 
ATOM   1855 C  CG    . TYR B 1 64  ? 38.329 8.367   29.301  1.00 20.46 ? 64  TYR B CG    1 
ATOM   1856 C  CD1   . TYR B 1 64  ? 37.384 7.799   28.457  1.00 21.15 ? 64  TYR B CD1   1 
ATOM   1857 C  CD2   . TYR B 1 64  ? 39.001 9.510   28.884  1.00 20.84 ? 64  TYR B CD2   1 
ATOM   1858 C  CE1   . TYR B 1 64  ? 37.125 8.331   27.219  1.00 21.88 ? 64  TYR B CE1   1 
ATOM   1859 C  CE2   . TYR B 1 64  ? 38.760 10.056  27.631  1.00 19.12 ? 64  TYR B CE2   1 
ATOM   1860 C  CZ    . TYR B 1 64  ? 37.818 9.452   26.805  1.00 23.57 ? 64  TYR B CZ    1 
ATOM   1861 O  OH    . TYR B 1 64  ? 37.552 10.007  25.586  1.00 19.83 ? 64  TYR B OH    1 
ATOM   1862 N  N     . SER B 1 65  ? 36.737 7.806   33.906  1.00 30.03 ? 65  SER B N     1 
ATOM   1863 C  CA    . SER B 1 65  ? 36.763 7.131   35.200  1.00 30.34 ? 65  SER B CA    1 
ATOM   1864 C  C     . SER B 1 65  ? 36.069 5.762   35.169  1.00 28.87 ? 65  SER B C     1 
ATOM   1865 O  O     . SER B 1 65  ? 35.261 5.460   34.291  1.00 24.49 ? 65  SER B O     1 
ATOM   1866 C  CB    . SER B 1 65  ? 36.084 8.013   36.230  1.00 26.97 ? 65  SER B CB    1 
ATOM   1867 O  OG    . SER B 1 65  ? 34.764 8.296   35.793  1.00 28.97 ? 65  SER B OG    1 
ATOM   1868 N  N     . ALA B 1 66  ? 36.325 4.958   36.207  1.00 27.19 ? 66  ALA B N     1 
ATOM   1869 C  CA    . ALA B 1 66  ? 35.518 3.752   36.398  1.00 25.77 ? 66  ALA B CA    1 
ATOM   1870 C  C     . ALA B 1 66  ? 34.039 4.105   36.554  1.00 23.36 ? 66  ALA B C     1 
ATOM   1871 O  O     . ALA B 1 66  ? 33.158 3.396   36.049  1.00 24.75 ? 66  ALA B O     1 
ATOM   1872 C  CB    . ALA B 1 66  ? 36.021 2.975   37.621  1.00 30.58 ? 66  ALA B CB    1 
ATOM   1873 N  N     . MET B 1 67  ? 33.750 5.222   37.218  1.00 21.92 ? 67  MET B N     1 
ATOM   1874 C  CA    . MET B 1 67  ? 32.374 5.671   37.416  1.00 22.98 ? 67  MET B CA    1 
ATOM   1875 C  C     . MET B 1 67  ? 31.666 5.946   36.082  1.00 23.08 ? 67  MET B C     1 
ATOM   1876 O  O     . MET B 1 67  ? 30.539 5.471   35.837  1.00 21.62 ? 67  MET B O     1 
ATOM   1877 C  CB    . MET B 1 67  ? 32.412 6.919   38.301  1.00 26.73 ? 67  MET B CB    1 
ATOM   1878 C  CG    . MET B 1 67  ? 31.136 7.684   38.435  1.00 30.30 ? 67  MET B CG    1 
ATOM   1879 S  SD    . MET B 1 67  ? 31.372 9.080   39.576  1.00 46.32 ? 67  MET B SD    1 
ATOM   1880 C  CE    . MET B 1 67  ? 32.437 10.164  38.628  1.00 39.74 ? 67  MET B CE    1 
ATOM   1881 N  N     . ARG B 1 68  ? 32.328 6.688   35.190  1.00 20.67 ? 68  ARG B N     1 
ATOM   1882 C  CA    . ARG B 1 68  ? 31.708 6.944   33.894  1.00 21.14 ? 68  ARG B CA    1 
ATOM   1883 C  C     . ARG B 1 68  ? 31.657 5.675   33.051  1.00 19.60 ? 68  ARG B C     1 
ATOM   1884 O  O     . ARG B 1 68  ? 30.692 5.466   32.309  1.00 20.14 ? 68  ARG B O     1 
ATOM   1885 C  CB    . ARG B 1 68  ? 32.445 8.072   33.163  1.00 19.01 ? 68  ARG B CB    1 
ATOM   1886 C  CG    . ARG B 1 68  ? 31.632 8.606   31.952  1.00 21.02 ? 68  ARG B CG    1 
ATOM   1887 C  CD    . ARG B 1 68  ? 32.050 10.003  31.518  1.00 25.26 ? 68  ARG B CD    1 
ATOM   1888 N  NE    . ARG B 1 68  ? 31.288 10.452  30.351  1.00 23.75 ? 68  ARG B NE    1 
ATOM   1889 C  CZ    . ARG B 1 68  ? 30.064 10.963  30.401  1.00 23.23 ? 68  ARG B CZ    1 
ATOM   1890 N  NH1   . ARG B 1 68  ? 29.386 11.028  31.534  1.00 23.91 ? 68  ARG B NH1   1 
ATOM   1891 N  NH2   . ARG B 1 68  ? 29.498 11.411  29.280  1.00 23.58 ? 68  ARG B NH2   1 
ATOM   1892 N  N     . ASP B 1 69  ? 32.666 4.808   33.159  1.00 18.55 ? 69  ASP B N     1 
ATOM   1893 C  CA    . ASP B 1 69  ? 32.625 3.554   32.414  1.00 19.85 ? 69  ASP B CA    1 
ATOM   1894 C  C     . ASP B 1 69  ? 31.396 2.728   32.787  1.00 23.44 ? 69  ASP B C     1 
ATOM   1895 O  O     . ASP B 1 69  ? 30.699 2.209   31.909  1.00 22.13 ? 69  ASP B O     1 
ATOM   1896 C  CB    . ASP B 1 69  ? 33.897 2.738   32.652  1.00 18.43 ? 69  ASP B CB    1 
ATOM   1897 C  CG    . ASP B 1 69  ? 35.090 3.232   31.854  1.00 25.16 ? 69  ASP B CG    1 
ATOM   1898 O  OD1   . ASP B 1 69  ? 34.965 4.161   31.017  1.00 22.63 ? 69  ASP B OD1   1 
ATOM   1899 O  OD2   . ASP B 1 69  ? 36.182 2.659   32.073  1.00 24.34 ? 69  ASP B OD2   1 
ATOM   1900 N  N     . GLN B 1 70  ? 31.130 2.557   34.087  1.00 22.68 ? 70  GLN B N     1 
ATOM   1901 C  CA    . GLN B 1 70  ? 29.947 1.791   34.501  1.00 24.20 ? 70  GLN B CA    1 
ATOM   1902 C  C     . GLN B 1 70  ? 28.658 2.454   34.033  1.00 26.73 ? 70  GLN B C     1 
ATOM   1903 O  O     . GLN B 1 70  ? 27.695 1.771   33.619  1.00 29.29 ? 70  GLN B O     1 
ATOM   1904 C  CB    . GLN B 1 70  ? 29.919 1.630   36.021  1.00 29.42 ? 70  GLN B CB    1 
ATOM   1905 C  CG    . GLN B 1 70  ? 30.728 0.469   36.513  1.00 42.27 ? 70  GLN B CG    1 
ATOM   1906 C  CD    . GLN B 1 70  ? 30.720 0.370   38.026  1.00 52.01 ? 70  GLN B CD    1 
ATOM   1907 O  OE1   . GLN B 1 70  ? 31.779 0.327   38.664  1.00 51.99 ? 70  GLN B OE1   1 
ATOM   1908 N  NE2   . GLN B 1 70  ? 29.520 0.328   38.611  1.00 50.16 ? 70  GLN B NE2   1 
ATOM   1909 N  N     . TYR B 1 71  ? 28.622 3.791   34.113  1.00 22.14 ? 71  TYR B N     1 
ATOM   1910 C  CA    . TYR B 1 71  ? 27.466 4.546   33.646  1.00 22.13 ? 71  TYR B CA    1 
ATOM   1911 C  C     . TYR B 1 71  ? 27.170 4.223   32.186  1.00 26.30 ? 71  TYR B C     1 
ATOM   1912 O  O     . TYR B 1 71  ? 26.027 3.928   31.816  1.00 23.24 ? 71  TYR B O     1 
ATOM   1913 C  CB    . TYR B 1 71  ? 27.749 6.039   33.830  1.00 23.86 ? 71  TYR B CB    1 
ATOM   1914 C  CG    . TYR B 1 71  ? 26.566 6.970   33.727  1.00 27.52 ? 71  TYR B CG    1 
ATOM   1915 C  CD1   . TYR B 1 71  ? 25.383 6.685   34.387  1.00 28.70 ? 71  TYR B CD1   1 
ATOM   1916 C  CD2   . TYR B 1 71  ? 26.663 8.174   33.032  1.00 29.75 ? 71  TYR B CD2   1 
ATOM   1917 C  CE1   . TYR B 1 71  ? 24.309 7.542   34.321  1.00 27.88 ? 71  TYR B CE1   1 
ATOM   1918 C  CE2   . TYR B 1 71  ? 25.584 9.059   32.975  1.00 28.73 ? 71  TYR B CE2   1 
ATOM   1919 C  CZ    . TYR B 1 71  ? 24.412 8.722   33.626  1.00 31.81 ? 71  TYR B CZ    1 
ATOM   1920 O  OH    . TYR B 1 71  ? 23.332 9.571   33.593  1.00 35.86 ? 71  TYR B OH    1 
ATOM   1921 N  N     . MET B 1 72  ? 28.200 4.282   31.338  1.00 21.55 ? 72  MET B N     1 
ATOM   1922 C  CA    . MET B 1 72  ? 28.016 4.006   29.912  1.00 24.06 ? 72  MET B CA    1 
ATOM   1923 C  C     . MET B 1 72  ? 27.713 2.538   29.641  1.00 23.91 ? 72  MET B C     1 
ATOM   1924 O  O     . MET B 1 72  ? 26.971 2.229   28.705  1.00 23.36 ? 72  MET B O     1 
ATOM   1925 C  CB    . MET B 1 72  ? 29.254 4.449   29.132  1.00 21.57 ? 72  MET B CB    1 
ATOM   1926 C  CG    . MET B 1 72  ? 29.511 5.938   29.240  1.00 21.80 ? 72  MET B CG    1 
ATOM   1927 S  SD    . MET B 1 72  ? 28.239 6.903   28.378  1.00 28.11 ? 72  MET B SD    1 
ATOM   1928 C  CE    . MET B 1 72  ? 28.422 8.496   29.126  1.00 33.24 ? 72  MET B CE    1 
ATOM   1929 N  N     . ARG B 1 73  ? 28.296 1.630   30.430  1.00 23.36 ? 73  ARG B N     1 
ATOM   1930 C  CA    . ARG B 1 73  ? 28.072 0.197   30.277  1.00 25.15 ? 73  ARG B CA    1 
ATOM   1931 C  C     . ARG B 1 73  ? 26.601 -0.171  30.447  1.00 25.82 ? 73  ARG B C     1 
ATOM   1932 O  O     . ARG B 1 73  ? 26.157 -1.197  29.917  1.00 24.46 ? 73  ARG B O     1 
ATOM   1933 C  CB    . ARG B 1 73  ? 28.934 -0.561  31.294  1.00 29.39 ? 73  ARG B CB    1 
ATOM   1934 C  CG    . ARG B 1 73  ? 28.842 -2.084  31.243  1.00 37.46 ? 73  ARG B CG    1 
ATOM   1935 C  CD    . ARG B 1 73  ? 29.864 -2.731  32.186  1.00 35.68 ? 73  ARG B CD    1 
ATOM   1936 N  NE    . ARG B 1 73  ? 31.216 -2.269  31.896  1.00 41.85 ? 73  ARG B NE    1 
ATOM   1937 C  CZ    . ARG B 1 73  ? 32.025 -1.685  32.774  1.00 42.93 ? 73  ARG B CZ    1 
ATOM   1938 N  NH1   . ARG B 1 73  ? 31.660 -1.493  34.034  1.00 42.07 ? 73  ARG B NH1   1 
ATOM   1939 N  NH2   . ARG B 1 73  ? 33.224 -1.268  32.373  1.00 38.33 ? 73  ARG B NH2   1 
ATOM   1940 N  N     . THR B 1 74  ? 25.837 0.623   31.200  1.00 23.66 ? 74  THR B N     1 
ATOM   1941 C  CA    . THR B 1 74  ? 24.406 0.302   31.313  1.00 25.85 ? 74  THR B CA    1 
ATOM   1942 C  C     . THR B 1 74  ? 23.617 0.465   30.007  1.00 25.92 ? 74  THR B C     1 
ATOM   1943 O  O     . THR B 1 74  ? 22.501 -0.071  29.898  1.00 24.12 ? 74  THR B O     1 
ATOM   1944 C  CB    . THR B 1 74  ? 23.749 1.156   32.398  1.00 29.51 ? 74  THR B CB    1 
ATOM   1945 O  OG1   . THR B 1 74  ? 23.650 2.519   31.957  1.00 34.23 ? 74  THR B OG1   1 
ATOM   1946 C  CG2   . THR B 1 74  ? 24.573 1.084   33.648  1.00 34.20 ? 74  THR B CG2   1 
ATOM   1947 N  N     . GLY B 1 75  ? 24.147 1.184   29.021  1.00 21.71 ? 75  GLY B N     1 
ATOM   1948 C  CA    . GLY B 1 75  ? 23.414 1.352   27.776  1.00 21.73 ? 75  GLY B CA    1 
ATOM   1949 C  C     . GLY B 1 75  ? 23.300 0.035   27.025  1.00 23.89 ? 75  GLY B C     1 
ATOM   1950 O  O     . GLY B 1 75  ? 24.237 -0.761  26.977  1.00 21.74 ? 75  GLY B O     1 
ATOM   1951 N  N     . GLU B 1 76  ? 22.121 -0.206  26.447  1.00 18.94 ? 76  GLU B N     1 
ATOM   1952 C  CA    . GLU B 1 76  ? 21.912 -1.411  25.658  1.00 22.26 ? 76  GLU B CA    1 
ATOM   1953 C  C     . GLU B 1 76  ? 22.058 -1.165  24.168  1.00 23.32 ? 76  GLU B C     1 
ATOM   1954 O  O     . GLU B 1 76  ? 22.301 -2.118  23.410  1.00 21.31 ? 76  GLU B O     1 
ATOM   1955 C  CB    . GLU B 1 76  ? 20.519 -1.984  25.904  1.00 21.71 ? 76  GLU B CB    1 
ATOM   1956 C  CG    . GLU B 1 76  ? 20.262 -2.402  27.321  1.00 25.10 ? 76  GLU B CG    1 
ATOM   1957 C  CD    . GLU B 1 76  ? 18.812 -2.795  27.494  1.00 33.23 ? 76  GLU B CD    1 
ATOM   1958 O  OE1   . GLU B 1 76  ? 17.964 -1.887  27.579  1.00 26.71 ? 76  GLU B OE1   1 
ATOM   1959 O  OE2   . GLU B 1 76  ? 18.519 -4.011  27.498  1.00 41.89 ? 76  GLU B OE2   1 
ATOM   1960 N  N     . GLY B 1 77  ? 21.900 0.075   23.731  1.00 21.40 ? 77  GLY B N     1 
ATOM   1961 C  CA    . GLY B 1 77  ? 22.168 0.398   22.339  1.00 19.71 ? 77  GLY B CA    1 
ATOM   1962 C  C     . GLY B 1 77  ? 22.625 1.834   22.246  1.00 18.79 ? 77  GLY B C     1 
ATOM   1963 O  O     . GLY B 1 77  ? 22.287 2.659   23.101  1.00 14.89 ? 77  GLY B O     1 
ATOM   1964 N  N     . PHE B 1 78  ? 23.392 2.136   21.195  1.00 17.47 ? 78  PHE B N     1 
ATOM   1965 C  CA    . PHE B 1 78  ? 24.054 3.435   21.073  1.00 16.79 ? 78  PHE B CA    1 
ATOM   1966 C  C     . PHE B 1 78  ? 23.759 4.081   19.727  1.00 18.44 ? 78  PHE B C     1 
ATOM   1967 O  O     . PHE B 1 78  ? 23.876 3.435   18.675  1.00 17.88 ? 78  PHE B O     1 
ATOM   1968 C  CB    . PHE B 1 78  ? 25.576 3.284   21.264  1.00 16.71 ? 78  PHE B CB    1 
ATOM   1969 C  CG    . PHE B 1 78  ? 25.953 2.838   22.639  1.00 17.65 ? 78  PHE B CG    1 
ATOM   1970 C  CD1   . PHE B 1 78  ? 25.845 1.497   22.993  1.00 21.25 ? 78  PHE B CD1   1 
ATOM   1971 C  CD2   . PHE B 1 78  ? 26.362 3.767   23.604  1.00 18.89 ? 78  PHE B CD2   1 
ATOM   1972 C  CE1   . PHE B 1 78  ? 26.163 1.078   24.275  1.00 23.61 ? 78  PHE B CE1   1 
ATOM   1973 C  CE2   . PHE B 1 78  ? 26.671 3.350   24.883  1.00 22.68 ? 78  PHE B CE2   1 
ATOM   1974 C  CZ    . PHE B 1 78  ? 26.568 2.005   25.216  1.00 18.87 ? 78  PHE B CZ    1 
ATOM   1975 N  N     . LEU B 1 79  ? 23.400 5.364   19.757  1.00 13.90 ? 79  LEU B N     1 
ATOM   1976 C  CA    . LEU B 1 79  ? 23.328 6.175   18.548  1.00 14.92 ? 79  LEU B CA    1 
ATOM   1977 C  C     . LEU B 1 79  ? 24.643 6.921   18.395  1.00 19.24 ? 79  LEU B C     1 
ATOM   1978 O  O     . LEU B 1 79  ? 24.980 7.747   19.252  1.00 17.68 ? 79  LEU B O     1 
ATOM   1979 C  CB    . LEU B 1 79  ? 22.193 7.199   18.602  1.00 18.39 ? 79  LEU B CB    1 
ATOM   1980 C  CG    . LEU B 1 79  ? 20.739 6.912   18.293  1.00 26.51 ? 79  LEU B CG    1 
ATOM   1981 C  CD1   . LEU B 1 79  ? 20.067 8.289   17.994  1.00 25.02 ? 79  LEU B CD1   1 
ATOM   1982 C  CD2   . LEU B 1 79  ? 20.619 5.953   17.102  1.00 23.62 ? 79  LEU B CD2   1 
ATOM   1983 N  N     . LEU B 1 80  ? 25.367 6.662   17.306  1.00 17.36 ? 80  LEU B N     1 
ATOM   1984 C  CA    . LEU B 1 80  ? 26.608 7.378   17.001  1.00 17.29 ? 80  LEU B CA    1 
ATOM   1985 C  C     . LEU B 1 80  ? 26.258 8.516   16.059  1.00 18.24 ? 80  LEU B C     1 
ATOM   1986 O  O     . LEU B 1 80  ? 25.961 8.265   14.889  1.00 18.90 ? 80  LEU B O     1 
ATOM   1987 C  CB    . LEU B 1 80  ? 27.624 6.452   16.337  1.00 15.72 ? 80  LEU B CB    1 
ATOM   1988 C  CG    . LEU B 1 80  ? 27.922 5.122   17.031  1.00 22.01 ? 80  LEU B CG    1 
ATOM   1989 C  CD1   . LEU B 1 80  ? 28.577 4.140   16.041  1.00 23.99 ? 80  LEU B CD1   1 
ATOM   1990 C  CD2   . LEU B 1 80  ? 28.831 5.394   18.179  1.00 27.50 ? 80  LEU B CD2   1 
ATOM   1991 N  N     . VAL B 1 81  ? 26.327 9.758   16.536  1.00 15.31 ? 81  VAL B N     1 
ATOM   1992 C  CA    . VAL B 1 81  ? 25.869 10.916  15.769  1.00 16.34 ? 81  VAL B CA    1 
ATOM   1993 C  C     . VAL B 1 81  ? 27.064 11.737  15.310  1.00 19.80 ? 81  VAL B C     1 
ATOM   1994 O  O     . VAL B 1 81  ? 27.931 12.087  16.123  1.00 16.42 ? 81  VAL B O     1 
ATOM   1995 C  CB    . VAL B 1 81  ? 24.915 11.783  16.598  1.00 17.46 ? 81  VAL B CB    1 
ATOM   1996 C  CG1   . VAL B 1 81  ? 24.310 12.899  15.747  1.00 18.28 ? 81  VAL B CG1   1 
ATOM   1997 C  CG2   . VAL B 1 81  ? 23.814 10.896  17.208  1.00 18.06 ? 81  VAL B CG2   1 
ATOM   1998 N  N     . PHE B 1 82  ? 27.101 12.058  14.010  1.00 18.53 ? 82  PHE B N     1 
ATOM   1999 C  CA    . PHE B 1 82  ? 27.975 13.114  13.498  1.00 16.26 ? 82  PHE B CA    1 
ATOM   2000 C  C     . PHE B 1 82  ? 27.117 14.101  12.710  1.00 20.67 ? 82  PHE B C     1 
ATOM   2001 O  O     . PHE B 1 82  ? 25.940 13.845  12.446  1.00 18.50 ? 82  PHE B O     1 
ATOM   2002 C  CB    . PHE B 1 82  ? 29.118 12.557  12.632  1.00 15.80 ? 82  PHE B CB    1 
ATOM   2003 C  CG    . PHE B 1 82  ? 28.660 11.982  11.325  1.00 20.46 ? 82  PHE B CG    1 
ATOM   2004 C  CD1   . PHE B 1 82  ? 28.162 10.689  11.268  1.00 17.34 ? 82  PHE B CD1   1 
ATOM   2005 C  CD2   . PHE B 1 82  ? 28.706 12.739  10.161  1.00 18.54 ? 82  PHE B CD2   1 
ATOM   2006 C  CE1   . PHE B 1 82  ? 27.731 10.150  10.067  1.00 19.66 ? 82  PHE B CE1   1 
ATOM   2007 C  CE2   . PHE B 1 82  ? 28.266 12.215  8.960   1.00 20.20 ? 82  PHE B CE2   1 
ATOM   2008 C  CZ    . PHE B 1 82  ? 27.779 10.919  8.910   1.00 20.94 ? 82  PHE B CZ    1 
ATOM   2009 N  N     . ALA B 1 83  ? 27.691 15.255  12.375  1.00 17.84 ? 83  ALA B N     1 
ATOM   2010 C  CA    . ALA B 1 83  ? 27.022 16.267  11.556  1.00 18.54 ? 83  ALA B CA    1 
ATOM   2011 C  C     . ALA B 1 83  ? 27.602 16.230  10.149  1.00 18.46 ? 83  ALA B C     1 
ATOM   2012 O  O     . ALA B 1 83  ? 28.827 16.215  9.982   1.00 22.81 ? 83  ALA B O     1 
ATOM   2013 C  CB    . ALA B 1 83  ? 27.174 17.678  12.143  1.00 21.99 ? 83  ALA B CB    1 
ATOM   2014 N  N     . ILE B 1 84  ? 26.732 16.219  9.134   1.00 21.51 ? 84  ILE B N     1 
ATOM   2015 C  CA    . ILE B 1 84  ? 27.226 16.025  7.775   1.00 21.53 ? 84  ILE B CA    1 
ATOM   2016 C  C     . ILE B 1 84  ? 28.008 17.217  7.258   1.00 21.45 ? 84  ILE B C     1 
ATOM   2017 O  O     . ILE B 1 84  ? 28.624 17.119  6.194   1.00 25.27 ? 84  ILE B O     1 
ATOM   2018 C  CB    . ILE B 1 84  ? 26.097 15.713  6.774   1.00 24.99 ? 84  ILE B CB    1 
ATOM   2019 C  CG1   . ILE B 1 84  ? 25.156 16.906  6.655   1.00 26.27 ? 84  ILE B CG1   1 
ATOM   2020 C  CG2   . ILE B 1 84  ? 25.349 14.462  7.207   1.00 23.10 ? 84  ILE B CG2   1 
ATOM   2021 C  CD1   . ILE B 1 84  ? 24.165 16.766  5.541   1.00 33.37 ? 84  ILE B CD1   1 
ATOM   2022 N  N     . ASN B 1 85  ? 27.985 18.348  7.965   1.00 19.98 ? 85  ASN B N     1 
ATOM   2023 C  CA    . ASN B 1 85  ? 28.796 19.492  7.567   1.00 24.99 ? 85  ASN B CA    1 
ATOM   2024 C  C     . ASN B 1 85  ? 30.007 19.670  8.467   1.00 24.62 ? 85  ASN B C     1 
ATOM   2025 O  O     . ASN B 1 85  ? 30.645 20.732  8.443   1.00 28.09 ? 85  ASN B O     1 
ATOM   2026 C  CB    . ASN B 1 85  ? 27.956 20.773  7.552   1.00 27.90 ? 85  ASN B CB    1 
ATOM   2027 C  CG    . ASN B 1 85  ? 27.522 21.212  8.938   1.00 31.32 ? 85  ASN B CG    1 
ATOM   2028 O  OD1   . ASN B 1 85  ? 27.437 20.402  9.870   1.00 27.38 ? 85  ASN B OD1   1 
ATOM   2029 N  ND2   . ASN B 1 85  ? 27.241 22.506  9.083   1.00 32.43 ? 85  ASN B ND2   1 
ATOM   2030 N  N     . ASN B 1 86  ? 30.386 18.632  9.212   1.00 25.24 ? 86  ASN B N     1 
ATOM   2031 C  CA    . ASN B 1 86  ? 31.553 18.717  10.094  1.00 24.31 ? 86  ASN B CA    1 
ATOM   2032 C  C     . ASN B 1 86  ? 32.386 17.443  9.978   1.00 24.16 ? 86  ASN B C     1 
ATOM   2033 O  O     . ASN B 1 86  ? 32.065 16.420  10.586  1.00 19.79 ? 86  ASN B O     1 
ATOM   2034 C  CB    . ASN B 1 86  ? 31.132 18.963  11.534  1.00 23.96 ? 86  ASN B CB    1 
ATOM   2035 C  CG    . ASN B 1 86  ? 32.303 19.313  12.408  1.00 26.38 ? 86  ASN B CG    1 
ATOM   2036 O  OD1   . ASN B 1 86  ? 33.152 18.480  12.679  1.00 28.31 ? 86  ASN B OD1   1 
ATOM   2037 N  ND2   . ASN B 1 86  ? 32.388 20.584  12.801  1.00 36.10 ? 86  ASN B ND2   1 
ATOM   2038 N  N     . THR B 1 87  ? 33.473 17.512  9.210   1.00 19.67 ? 87  THR B N     1 
ATOM   2039 C  CA    . THR B 1 87  ? 34.277 16.319  8.965   1.00 22.85 ? 87  THR B CA    1 
ATOM   2040 C  C     . THR B 1 87  ? 34.900 15.771  10.243  1.00 21.25 ? 87  THR B C     1 
ATOM   2041 O  O     . THR B 1 87  ? 35.043 14.549  10.402  1.00 22.14 ? 87  THR B O     1 
ATOM   2042 C  CB    . THR B 1 87  ? 35.351 16.644  7.926   1.00 24.57 ? 87  THR B CB    1 
ATOM   2043 O  OG1   . THR B 1 87  ? 34.691 16.895  6.681   1.00 26.82 ? 87  THR B OG1   1 
ATOM   2044 C  CG2   . THR B 1 87  ? 36.322 15.488  7.789   1.00 30.94 ? 87  THR B CG2   1 
ATOM   2045 N  N     . LYS B 1 88  ? 35.319 16.656  11.150  1.00 20.79 ? 88  LYS B N     1 
ATOM   2046 C  CA    . LYS B 1 88  ? 35.937 16.173  12.381  1.00 21.18 ? 88  LYS B CA    1 
ATOM   2047 C  C     . LYS B 1 88  ? 34.958 15.315  13.177  1.00 21.48 ? 88  LYS B C     1 
ATOM   2048 O  O     . LYS B 1 88  ? 35.342 14.295  13.757  1.00 19.41 ? 88  LYS B O     1 
ATOM   2049 C  CB    . LYS B 1 88  ? 36.443 17.354  13.213  1.00 24.80 ? 88  LYS B CB    1 
ATOM   2050 C  CG    . LYS B 1 88  ? 37.015 16.963  14.566  1.00 26.30 ? 88  LYS B CG    1 
ATOM   2051 C  CD    . LYS B 1 88  ? 38.261 16.094  14.436  1.00 28.87 ? 88  LYS B CD    1 
ATOM   2052 C  CE    . LYS B 1 88  ? 39.215 16.317  15.614  1.00 31.72 ? 88  LYS B CE    1 
ATOM   2053 N  NZ    . LYS B 1 88  ? 38.611 15.927  16.928  1.00 33.76 ? 88  LYS B NZ    1 
ATOM   2054 N  N     . SER B 1 89  ? 33.687 15.724  13.242  1.00 21.00 ? 89  SER B N     1 
ATOM   2055 C  CA    . SER B 1 89  ? 32.741 14.941  14.032  1.00 18.15 ? 89  SER B CA    1 
ATOM   2056 C  C     . SER B 1 89  ? 32.556 13.544  13.441  1.00 19.55 ? 89  SER B C     1 
ATOM   2057 O  O     . SER B 1 89  ? 32.321 12.582  14.180  1.00 18.83 ? 89  SER B O     1 
ATOM   2058 C  CB    . SER B 1 89  ? 31.416 15.693  14.146  1.00 18.97 ? 89  SER B CB    1 
ATOM   2059 O  OG    . SER B 1 89  ? 30.707 15.719  12.914  1.00 20.76 ? 89  SER B OG    1 
ATOM   2060 N  N     . PHE B 1 90  ? 32.700 13.413  12.113  1.00 16.70 ? 90  PHE B N     1 
ATOM   2061 C  CA    . PHE B 1 90  ? 32.671 12.109  11.462  1.00 17.89 ? 90  PHE B CA    1 
ATOM   2062 C  C     . PHE B 1 90  ? 33.917 11.300  11.790  1.00 18.28 ? 90  PHE B C     1 
ATOM   2063 O  O     . PHE B 1 90  ? 33.833 10.091  12.043  1.00 17.35 ? 90  PHE B O     1 
ATOM   2064 C  CB    . PHE B 1 90  ? 32.529 12.300  9.946   1.00 19.37 ? 90  PHE B CB    1 
ATOM   2065 C  CG    . PHE B 1 90  ? 32.557 11.018  9.159   1.00 20.74 ? 90  PHE B CG    1 
ATOM   2066 C  CD1   . PHE B 1 90  ? 31.535 10.093  9.266   1.00 21.43 ? 90  PHE B CD1   1 
ATOM   2067 C  CD2   . PHE B 1 90  ? 33.610 10.750  8.297   1.00 22.51 ? 90  PHE B CD2   1 
ATOM   2068 C  CE1   . PHE B 1 90  ? 31.566 8.907   8.524   1.00 21.24 ? 90  PHE B CE1   1 
ATOM   2069 C  CE2   . PHE B 1 90  ? 33.651 9.575   7.551   1.00 25.67 ? 90  PHE B CE2   1 
ATOM   2070 C  CZ    . PHE B 1 90  ? 32.619 8.655   7.664   1.00 23.51 ? 90  PHE B CZ    1 
ATOM   2071 N  N     . GLU B 1 91  ? 35.092 11.938  11.755  1.00 18.42 ? 91  GLU B N     1 
ATOM   2072 C  CA    . GLU B 1 91  ? 36.319 11.212  12.067  1.00 20.05 ? 91  GLU B CA    1 
ATOM   2073 C  C     . GLU B 1 91  ? 36.355 10.758  13.526  1.00 21.27 ? 91  GLU B C     1 
ATOM   2074 O  O     . GLU B 1 91  ? 36.975 9.729   13.834  1.00 23.38 ? 91  GLU B O     1 
ATOM   2075 C  CB    . GLU B 1 91  ? 37.521 12.091  11.724  1.00 23.05 ? 91  GLU B CB    1 
ATOM   2076 C  CG    . GLU B 1 91  ? 37.908 12.009  10.226  1.00 34.21 ? 91  GLU B CG    1 
ATOM   2077 C  CD    . GLU B 1 91  ? 38.623 13.264  9.728   1.00 40.41 ? 91  GLU B CD    1 
ATOM   2078 O  OE1   . GLU B 1 91  ? 38.860 14.178  10.547  1.00 40.85 ? 91  GLU B OE1   1 
ATOM   2079 O  OE2   . GLU B 1 91  ? 38.929 13.348  8.514   1.00 42.69 ? 91  GLU B OE2   1 
ATOM   2080 N  N     . ASP B 1 92  ? 35.675 11.484  14.423  1.00 18.61 ? 92  ASP B N     1 
ATOM   2081 C  CA    . ASP B 1 92  ? 35.585 11.096  15.840  1.00 19.93 ? 92  ASP B CA    1 
ATOM   2082 C  C     . ASP B 1 92  ? 34.732 9.843   16.080  1.00 18.39 ? 92  ASP B C     1 
ATOM   2083 O  O     . ASP B 1 92  ? 34.789 9.266   17.185  1.00 15.96 ? 92  ASP B O     1 
ATOM   2084 C  CB    . ASP B 1 92  ? 35.015 12.251  16.687  1.00 17.75 ? 92  ASP B CB    1 
ATOM   2085 C  CG    . ASP B 1 92  ? 36.005 13.390  16.915  1.00 24.31 ? 92  ASP B CG    1 
ATOM   2086 O  OD1   . ASP B 1 92  ? 37.201 13.238  16.579  1.00 23.34 ? 92  ASP B OD1   1 
ATOM   2087 O  OD2   . ASP B 1 92  ? 35.551 14.435  17.428  1.00 22.40 ? 92  ASP B OD2   1 
ATOM   2088 N  N     . ILE B 1 93  ? 33.941 9.412   15.089  1.00 16.26 ? 93  ILE B N     1 
ATOM   2089 C  CA    . ILE B 1 93  ? 33.064 8.255   15.288  1.00 17.49 ? 93  ILE B CA    1 
ATOM   2090 C  C     . ILE B 1 93  ? 33.874 7.025   15.682  1.00 16.99 ? 93  ILE B C     1 
ATOM   2091 O  O     . ILE B 1 93  ? 33.436 6.215   16.512  1.00 17.02 ? 93  ILE B O     1 
ATOM   2092 C  CB    . ILE B 1 93  ? 32.222 7.996   14.020  1.00 18.50 ? 93  ILE B CB    1 
ATOM   2093 C  CG1   . ILE B 1 93  ? 31.180 9.102   13.841  1.00 17.10 ? 93  ILE B CG1   1 
ATOM   2094 C  CG2   . ILE B 1 93  ? 31.499 6.657   14.114  1.00 18.92 ? 93  ILE B CG2   1 
ATOM   2095 C  CD1   . ILE B 1 93  ? 30.240 9.297   15.030  1.00 20.04 ? 93  ILE B CD1   1 
ATOM   2096 N  N     . HIS B 1 94  ? 35.058 6.857   15.090  1.00 17.07 ? 94  HIS B N     1 
ATOM   2097 C  CA    . HIS B 1 94  ? 35.904 5.714   15.434  1.00 19.68 ? 94  HIS B CA    1 
ATOM   2098 C  C     . HIS B 1 94  ? 36.191 5.678   16.929  1.00 18.64 ? 94  HIS B C     1 
ATOM   2099 O  O     . HIS B 1 94  ? 36.078 4.624   17.579  1.00 17.57 ? 94  HIS B O     1 
ATOM   2100 C  CB    . HIS B 1 94  ? 37.220 5.772   14.645  1.00 22.23 ? 94  HIS B CB    1 
ATOM   2101 C  CG    . HIS B 1 94  ? 38.257 4.804   15.130  1.00 23.79 ? 94  HIS B CG    1 
ATOM   2102 N  ND1   . HIS B 1 94  ? 38.269 3.476   14.754  1.00 27.00 ? 94  HIS B ND1   1 
ATOM   2103 C  CD2   . HIS B 1 94  ? 39.321 4.969   15.957  1.00 28.10 ? 94  HIS B CD2   1 
ATOM   2104 C  CE1   . HIS B 1 94  ? 39.285 2.863   15.338  1.00 27.51 ? 94  HIS B CE1   1 
ATOM   2105 N  NE2   . HIS B 1 94  ? 39.941 3.746   16.071  1.00 26.55 ? 94  HIS B NE2   1 
ATOM   2106 N  N     . HIS B 1 95  ? 36.577 6.829   17.484  1.00 18.49 ? 95  HIS B N     1 
ATOM   2107 C  CA    . HIS B 1 95  ? 36.813 6.947   18.918  1.00 19.10 ? 95  HIS B CA    1 
ATOM   2108 C  C     . HIS B 1 95  ? 35.591 6.527   19.729  1.00 17.81 ? 95  HIS B C     1 
ATOM   2109 O  O     . HIS B 1 95  ? 35.700 5.762   20.702  1.00 15.92 ? 95  HIS B O     1 
ATOM   2110 C  CB    . HIS B 1 95  ? 37.217 8.397   19.246  1.00 19.63 ? 95  HIS B CB    1 
ATOM   2111 C  CG    . HIS B 1 95  ? 37.101 8.747   20.702  1.00 20.99 ? 95  HIS B CG    1 
ATOM   2112 N  ND1   . HIS B 1 95  ? 38.008 8.312   21.646  1.00 20.79 ? 95  HIS B ND1   1 
ATOM   2113 C  CD2   . HIS B 1 95  ? 36.199 9.513   21.369  1.00 18.93 ? 95  HIS B CD2   1 
ATOM   2114 C  CE1   . HIS B 1 95  ? 37.653 8.764   22.838  1.00 19.55 ? 95  HIS B CE1   1 
ATOM   2115 N  NE2   . HIS B 1 95  ? 36.564 9.503   22.696  1.00 18.57 ? 95  HIS B NE2   1 
ATOM   2116 N  N     . TYR B 1 96  ? 34.418 7.076   19.393  1.00 16.78 ? 96  TYR B N     1 
ATOM   2117 C  CA    . TYR B 1 96  ? 33.247 6.743   20.206  1.00 16.68 ? 96  TYR B CA    1 
ATOM   2118 C  C     . TYR B 1 96  ? 32.926 5.252   20.124  1.00 15.57 ? 96  TYR B C     1 
ATOM   2119 O  O     . TYR B 1 96  ? 32.638 4.610   21.143  1.00 16.42 ? 96  TYR B O     1 
ATOM   2120 C  CB    . TYR B 1 96  ? 32.045 7.603   19.801  1.00 15.95 ? 96  TYR B CB    1 
ATOM   2121 C  CG    . TYR B 1 96  ? 32.259 9.021   20.271  1.00 17.91 ? 96  TYR B CG    1 
ATOM   2122 C  CD1   . TYR B 1 96  ? 32.176 9.340   21.616  1.00 19.89 ? 96  TYR B CD1   1 
ATOM   2123 C  CD2   . TYR B 1 96  ? 32.614 10.033  19.374  1.00 17.22 ? 96  TYR B CD2   1 
ATOM   2124 C  CE1   . TYR B 1 96  ? 32.399 10.663  22.061  1.00 18.72 ? 96  TYR B CE1   1 
ATOM   2125 C  CE2   . TYR B 1 96  ? 32.855 11.348  19.813  1.00 16.24 ? 96  TYR B CE2   1 
ATOM   2126 C  CZ    . TYR B 1 96  ? 32.743 11.647  21.161  1.00 16.92 ? 96  TYR B CZ    1 
ATOM   2127 O  OH    . TYR B 1 96  ? 32.995 12.937  21.599  1.00 18.46 ? 96  TYR B OH    1 
ATOM   2128 N  N     . ARG B 1 97  ? 33.004 4.676   18.921  1.00 17.07 ? 97  ARG B N     1 
ATOM   2129 C  CA    . ARG B 1 97  ? 32.751 3.243   18.781  1.00 17.66 ? 97  ARG B CA    1 
ATOM   2130 C  C     . ARG B 1 97  ? 33.738 2.402   19.590  1.00 20.85 ? 97  ARG B C     1 
ATOM   2131 O  O     . ARG B 1 97  ? 33.349 1.402   20.210  1.00 19.08 ? 97  ARG B O     1 
ATOM   2132 C  CB    . ARG B 1 97  ? 32.788 2.845   17.310  1.00 22.66 ? 97  ARG B CB    1 
ATOM   2133 C  CG    . ARG B 1 97  ? 32.641 1.338   17.111  1.00 26.11 ? 97  ARG B CG    1 
ATOM   2134 C  CD    . ARG B 1 97  ? 32.323 0.988   15.674  1.00 27.92 ? 97  ARG B CD    1 
ATOM   2135 N  NE    . ARG B 1 97  ? 32.113 -0.447  15.500  1.00 28.09 ? 97  ARG B NE    1 
ATOM   2136 C  CZ    . ARG B 1 97  ? 33.070 -1.302  15.170  1.00 35.20 ? 97  ARG B CZ    1 
ATOM   2137 N  NH1   . ARG B 1 97  ? 34.334 -0.916  15.046  1.00 36.55 ? 97  ARG B NH1   1 
ATOM   2138 N  NH2   . ARG B 1 97  ? 32.749 -2.575  14.931  1.00 35.83 ? 97  ARG B NH2   1 
ATOM   2139 N  N     . GLU B 1 98  ? 35.021 2.782   19.600  1.00 17.62 ? 98  GLU B N     1 
ATOM   2140 C  CA    . GLU B 1 98  ? 35.996 2.004   20.365  1.00 21.46 ? 98  GLU B CA    1 
ATOM   2141 C  C     . GLU B 1 98  ? 35.774 2.127   21.867  1.00 19.82 ? 98  GLU B C     1 
ATOM   2142 O  O     . GLU B 1 98  ? 36.018 1.168   22.610  1.00 17.96 ? 98  GLU B O     1 
ATOM   2143 C  CB    . GLU B 1 98  ? 37.416 2.434   20.007  1.00 19.82 ? 98  GLU B CB    1 
ATOM   2144 C  CG    . GLU B 1 98  ? 37.820 2.045   18.573  1.00 25.29 ? 98  GLU B CG    1 
ATOM   2145 C  CD    . GLU B 1 98  ? 37.814 0.537   18.346  1.00 30.53 ? 98  GLU B CD    1 
ATOM   2146 O  OE1   . GLU B 1 98  ? 38.294 -0.209  19.224  1.00 29.04 ? 98  GLU B OE1   1 
ATOM   2147 O  OE2   . GLU B 1 98  ? 37.333 0.098   17.281  1.00 32.59 ? 98  GLU B OE2   1 
ATOM   2148 N  N     . GLN B 1 99  ? 35.305 3.283   22.343  1.00 15.52 ? 99  GLN B N     1 
ATOM   2149 C  CA    . GLN B 1 99  ? 35.035 3.393   23.774  1.00 17.59 ? 99  GLN B CA    1 
ATOM   2150 C  C     . GLN B 1 99  ? 33.833 2.534   24.166  1.00 20.66 ? 99  GLN B C     1 
ATOM   2151 O  O     . GLN B 1 99  ? 33.817 1.917   25.249  1.00 20.15 ? 99  GLN B O     1 
ATOM   2152 C  CB    . GLN B 1 99  ? 34.810 4.856   24.155  1.00 19.72 ? 99  GLN B CB    1 
ATOM   2153 C  CG    . GLN B 1 99  ? 36.042 5.753   23.976  1.00 17.33 ? 99  GLN B CG    1 
ATOM   2154 C  CD    . GLN B 1 99  ? 37.242 5.219   24.734  1.00 23.06 ? 99  GLN B CD    1 
ATOM   2155 O  OE1   . GLN B 1 99  ? 37.123 4.833   25.901  1.00 22.62 ? 99  GLN B OE1   1 
ATOM   2156 N  NE2   . GLN B 1 99  ? 38.401 5.158   24.064  1.00 27.68 ? 99  GLN B NE2   1 
ATOM   2157 N  N     . ILE B 1 100 ? 32.822 2.471   23.292  1.00 17.95 ? 100 ILE B N     1 
ATOM   2158 C  CA    . ILE B 1 100 ? 31.686 1.580   23.545  1.00 16.28 ? 100 ILE B CA    1 
ATOM   2159 C  C     . ILE B 1 100 ? 32.164 0.137   23.638  1.00 20.58 ? 100 ILE B C     1 
ATOM   2160 O  O     . ILE B 1 100 ? 31.864 -0.579  24.607  1.00 21.11 ? 100 ILE B O     1 
ATOM   2161 C  CB    . ILE B 1 100 ? 30.605 1.747   22.457  1.00 20.63 ? 100 ILE B CB    1 
ATOM   2162 C  CG1   . ILE B 1 100 ? 29.977 3.133   22.539  1.00 19.46 ? 100 ILE B CG1   1 
ATOM   2163 C  CG2   . ILE B 1 100 ? 29.509 0.676   22.613  1.00 20.25 ? 100 ILE B CG2   1 
ATOM   2164 C  CD1   . ILE B 1 100 ? 29.266 3.574   21.265  1.00 16.30 ? 100 ILE B CD1   1 
ATOM   2165 N  N     . LYS B 1 101 ? 32.899 -0.313  22.611  1.00 20.05 ? 101 LYS B N     1 
ATOM   2166 C  CA    . LYS B 1 101 ? 33.434 -1.675  22.598  1.00 22.56 ? 101 LYS B CA    1 
ATOM   2167 C  C     . LYS B 1 101 ? 34.247 -1.965  23.853  1.00 27.44 ? 101 LYS B C     1 
ATOM   2168 O  O     . LYS B 1 101 ? 34.154 -3.060  24.424  1.00 24.48 ? 101 LYS B O     1 
ATOM   2169 C  CB    . LYS B 1 101 ? 34.292 -1.886  21.351  1.00 25.31 ? 101 LYS B CB    1 
ATOM   2170 C  CG    . LYS B 1 101 ? 33.499 -2.126  20.089  1.00 29.86 ? 101 LYS B CG    1 
ATOM   2171 C  CD    . LYS B 1 101 ? 34.398 -1.997  18.852  1.00 34.99 ? 101 LYS B CD    1 
ATOM   2172 C  CE    . LYS B 1 101 ? 35.714 -2.759  19.037  1.00 40.72 ? 101 LYS B CE    1 
ATOM   2173 N  NZ    . LYS B 1 101 ? 36.557 -2.782  17.799  1.00 35.62 ? 101 LYS B NZ    1 
ATOM   2174 N  N     . ARG B 1 102 ? 35.030 -0.985  24.315  1.00 21.66 ? 102 ARG B N     1 
ATOM   2175 C  CA    . ARG B 1 102 ? 35.848 -1.201  25.502  1.00 21.15 ? 102 ARG B CA    1 
ATOM   2176 C  C     . ARG B 1 102 ? 34.992 -1.435  26.746  1.00 25.41 ? 102 ARG B C     1 
ATOM   2177 O  O     . ARG B 1 102 ? 35.234 -2.383  27.503  1.00 26.93 ? 102 ARG B O     1 
ATOM   2178 C  CB    . ARG B 1 102 ? 36.784 -0.015  25.708  1.00 21.94 ? 102 ARG B CB    1 
ATOM   2179 C  CG    . ARG B 1 102 ? 37.674 -0.130  26.946  1.00 24.82 ? 102 ARG B CG    1 
ATOM   2180 C  CD    . ARG B 1 102 ? 38.586 1.074   27.087  1.00 22.94 ? 102 ARG B CD    1 
ATOM   2181 N  NE    . ARG B 1 102 ? 37.859 2.316   27.350  1.00 22.40 ? 102 ARG B NE    1 
ATOM   2182 C  CZ    . ARG B 1 102 ? 37.363 2.662   28.533  1.00 24.30 ? 102 ARG B CZ    1 
ATOM   2183 N  NH1   . ARG B 1 102 ? 37.550 1.912   29.613  1.00 24.56 ? 102 ARG B NH1   1 
ATOM   2184 N  NH2   . ARG B 1 102 ? 36.665 3.786   28.640  1.00 21.49 ? 102 ARG B NH2   1 
ATOM   2185 N  N     . VAL B 1 103 ? 34.010 -0.565  27.002  1.00 20.88 ? 103 VAL B N     1 
ATOM   2186 C  CA    . VAL B 1 103 ? 33.288 -0.724  28.268  1.00 23.32 ? 103 VAL B CA    1 
ATOM   2187 C  C     . VAL B 1 103 ? 32.299 -1.886  28.215  1.00 28.29 ? 103 VAL B C     1 
ATOM   2188 O  O     . VAL B 1 103 ? 31.955 -2.453  29.262  1.00 24.93 ? 103 VAL B O     1 
ATOM   2189 C  CB    . VAL B 1 103 ? 32.588 0.574   28.694  1.00 22.60 ? 103 VAL B CB    1 
ATOM   2190 C  CG1   . VAL B 1 103 ? 33.612 1.686   28.823  1.00 23.86 ? 103 VAL B CG1   1 
ATOM   2191 C  CG2   . VAL B 1 103 ? 31.465 0.956   27.712  1.00 21.65 ? 103 VAL B CG2   1 
ATOM   2192 N  N     . LYS B 1 104 ? 31.801 -2.241  27.026  1.00 23.35 ? 104 LYS B N     1 
ATOM   2193 C  CA    . LYS B 1 104 ? 30.894 -3.381  26.921  1.00 27.34 ? 104 LYS B CA    1 
ATOM   2194 C  C     . LYS B 1 104 ? 31.637 -4.701  26.803  1.00 34.75 ? 104 LYS B C     1 
ATOM   2195 O  O     . LYS B 1 104 ? 31.013 -5.760  26.954  1.00 36.39 ? 104 LYS B O     1 
ATOM   2196 C  CB    . LYS B 1 104 ? 29.938 -3.204  25.725  1.00 26.92 ? 104 LYS B CB    1 
ATOM   2197 C  CG    . LYS B 1 104 ? 29.074 -1.939  25.814  1.00 26.72 ? 104 LYS B CG    1 
ATOM   2198 C  CD    . LYS B 1 104 ? 27.955 -2.063  26.868  1.00 25.97 ? 104 LYS B CD    1 
ATOM   2199 C  CE    . LYS B 1 104 ? 26.809 -2.947  26.420  1.00 28.19 ? 104 LYS B CE    1 
ATOM   2200 N  NZ    . LYS B 1 104 ? 25.736 -3.042  27.454  1.00 26.65 ? 104 LYS B NZ    1 
ATOM   2201 N  N     . ASP B 1 105 ? 32.938 -4.659  26.504  1.00 30.02 ? 105 ASP B N     1 
ATOM   2202 C  CA    . ASP B 1 105 ? 33.772 -5.858  26.399  1.00 41.03 ? 105 ASP B CA    1 
ATOM   2203 C  C     . ASP B 1 105 ? 33.254 -6.786  25.301  1.00 46.08 ? 105 ASP B C     1 
ATOM   2204 O  O     . ASP B 1 105 ? 33.176 -8.005  25.470  1.00 47.07 ? 105 ASP B O     1 
ATOM   2205 C  CB    . ASP B 1 105 ? 33.869 -6.587  27.744  1.00 43.00 ? 105 ASP B CB    1 
ATOM   2206 C  CG    . ASP B 1 105 ? 34.974 -7.632  27.770  1.00 56.63 ? 105 ASP B CG    1 
ATOM   2207 O  OD1   . ASP B 1 105 ? 35.993 -7.464  27.059  1.00 54.10 ? 105 ASP B OD1   1 
ATOM   2208 O  OD2   . ASP B 1 105 ? 34.810 -8.634  28.503  1.00 65.91 ? 105 ASP B OD2   1 
ATOM   2209 N  N     . SER B 1 106 ? 32.881 -6.203  24.166  1.00 40.52 ? 106 SER B N     1 
ATOM   2210 C  CA    . SER B 1 106 ? 32.242 -6.960  23.101  1.00 50.27 ? 106 SER B CA    1 
ATOM   2211 C  C     . SER B 1 106 ? 32.317 -6.162  21.812  1.00 48.89 ? 106 SER B C     1 
ATOM   2212 O  O     . SER B 1 106 ? 32.268 -4.930  21.827  1.00 45.37 ? 106 SER B O     1 
ATOM   2213 C  CB    . SER B 1 106 ? 30.781 -7.279  23.438  1.00 48.73 ? 106 SER B CB    1 
ATOM   2214 O  OG    . SER B 1 106 ? 30.142 -7.928  22.357  1.00 50.10 ? 106 SER B OG    1 
ATOM   2215 N  N     . GLU B 1 107 ? 32.457 -6.880  20.702  1.00 53.35 ? 107 GLU B N     1 
ATOM   2216 C  CA    . GLU B 1 107 ? 32.386 -6.286  19.373  1.00 59.25 ? 107 GLU B CA    1 
ATOM   2217 C  C     . GLU B 1 107 ? 30.972 -6.319  18.812  1.00 57.11 ? 107 GLU B C     1 
ATOM   2218 O  O     . GLU B 1 107 ? 30.741 -5.824  17.705  1.00 61.04 ? 107 GLU B O     1 
ATOM   2219 C  CB    . GLU B 1 107 ? 33.353 -6.997  18.418  1.00 67.09 ? 107 GLU B CB    1 
ATOM   2220 C  CG    . GLU B 1 107 ? 34.825 -6.720  18.711  1.00 69.53 ? 107 GLU B CG    1 
ATOM   2221 C  CD    . GLU B 1 107 ? 35.411 -7.690  19.722  1.00 81.80 ? 107 GLU B CD    1 
ATOM   2222 O  OE1   . GLU B 1 107 ? 34.822 -8.777  19.913  1.00 82.25 ? 107 GLU B OE1   1 
ATOM   2223 O  OE2   . GLU B 1 107 ? 36.452 -7.360  20.334  1.00 82.47 ? 107 GLU B OE2   1 
ATOM   2224 N  N     . ASP B 1 108 ? 30.027 -6.882  19.560  1.00 50.74 ? 108 ASP B N     1 
ATOM   2225 C  CA    . ASP B 1 108 ? 28.643 -7.082  19.134  1.00 54.66 ? 108 ASP B CA    1 
ATOM   2226 C  C     . ASP B 1 108 ? 27.713 -6.284  20.045  1.00 47.02 ? 108 ASP B C     1 
ATOM   2227 O  O     . ASP B 1 108 ? 27.034 -6.836  20.916  1.00 49.91 ? 108 ASP B O     1 
ATOM   2228 C  CB    . ASP B 1 108 ? 28.331 -8.556  19.167  1.00 58.32 ? 108 ASP B CB    1 
ATOM   2229 C  CG    . ASP B 1 108 ? 27.081 -8.898  18.406  1.00 66.40 ? 108 ASP B CG    1 
ATOM   2230 O  OD1   . ASP B 1 108 ? 27.159 -9.035  17.167  1.00 70.58 ? 108 ASP B OD1   1 
ATOM   2231 O  OD2   . ASP B 1 108 ? 26.019 -9.043  19.052  1.00 70.15 ? 108 ASP B OD2   1 
ATOM   2232 N  N     . VAL B 1 109 ? 27.654 -4.979  19.816  1.00 32.12 ? 109 VAL B N     1 
ATOM   2233 C  CA    . VAL B 1 109 ? 26.821 -4.069  20.590  1.00 25.86 ? 109 VAL B CA    1 
ATOM   2234 C  C     . VAL B 1 109 ? 25.886 -3.380  19.630  1.00 21.21 ? 109 VAL B C     1 
ATOM   2235 O  O     . VAL B 1 109 ? 26.327 -2.902  18.580  1.00 21.92 ? 109 VAL B O     1 
ATOM   2236 C  CB    . VAL B 1 109 ? 27.671 -3.025  21.357  1.00 26.85 ? 109 VAL B CB    1 
ATOM   2237 C  CG1   . VAL B 1 109 ? 26.768 -2.097  22.165  1.00 28.09 ? 109 VAL B CG1   1 
ATOM   2238 C  CG2   . VAL B 1 109 ? 28.676 -3.731  22.252  1.00 30.64 ? 109 VAL B CG2   1 
ATOM   2239 N  N     . PRO B 1 110 ? 24.575 -3.323  19.898  1.00 20.91 ? 110 PRO B N     1 
ATOM   2240 C  CA    . PRO B 1 110 ? 23.670 -2.614  18.984  1.00 20.16 ? 110 PRO B CA    1 
ATOM   2241 C  C     . PRO B 1 110 ? 24.040 -1.138  18.840  1.00 21.60 ? 110 PRO B C     1 
ATOM   2242 O  O     . PRO B 1 110 ? 24.191 -0.407  19.833  1.00 19.51 ? 110 PRO B O     1 
ATOM   2243 C  CB    . PRO B 1 110 ? 22.292 -2.800  19.631  1.00 21.62 ? 110 PRO B CB    1 
ATOM   2244 C  CG    . PRO B 1 110 ? 22.437 -4.094  20.387  1.00 25.81 ? 110 PRO B CG    1 
ATOM   2245 C  CD    . PRO B 1 110 ? 23.841 -4.074  20.931  1.00 26.11 ? 110 PRO B CD    1 
ATOM   2246 N  N     . MET B 1 111 ? 24.211 -0.710  17.584  1.00 21.27 ? 111 MET B N     1 
ATOM   2247 C  CA    . MET B 1 111 ? 24.564 0.674   17.274  1.00 19.34 ? 111 MET B CA    1 
ATOM   2248 C  C     . MET B 1 111 ? 23.948 1.076   15.946  1.00 23.83 ? 111 MET B C     1 
ATOM   2249 O  O     . MET B 1 111 ? 23.709 0.236   15.069  1.00 21.40 ? 111 MET B O     1 
ATOM   2250 C  CB    . MET B 1 111 ? 26.077 0.928   17.171  1.00 21.34 ? 111 MET B CB    1 
ATOM   2251 C  CG    . MET B 1 111 ? 26.915 0.396   18.284  1.00 25.69 ? 111 MET B CG    1 
ATOM   2252 S  SD    . MET B 1 111 ? 28.652 0.786   17.959  1.00 27.92 ? 111 MET B SD    1 
ATOM   2253 C  CE    . MET B 1 111 ? 29.462 -0.517  18.846  1.00 31.06 ? 111 MET B CE    1 
ATOM   2254 N  N     . VAL B 1 112 ? 23.704 2.376   15.807  1.00 18.74 ? 112 VAL B N     1 
ATOM   2255 C  CA    . VAL B 1 112 ? 23.223 2.958   14.556  1.00 17.37 ? 112 VAL B CA    1 
ATOM   2256 C  C     . VAL B 1 112 ? 24.043 4.215   14.289  1.00 21.03 ? 112 VAL B C     1 
ATOM   2257 O  O     . VAL B 1 112 ? 24.257 5.019   15.202  1.00 17.64 ? 112 VAL B O     1 
ATOM   2258 C  CB    . VAL B 1 112 ? 21.714 3.289   14.610  1.00 19.80 ? 112 VAL B CB    1 
ATOM   2259 C  CG1   . VAL B 1 112 ? 21.315 4.153   13.401  1.00 23.22 ? 112 VAL B CG1   1 
ATOM   2260 C  CG2   . VAL B 1 112 ? 20.879 2.018   14.666  1.00 23.03 ? 112 VAL B CG2   1 
ATOM   2261 N  N     . LEU B 1 113 ? 24.539 4.369   13.060  1.00 17.25 ? 113 LEU B N     1 
ATOM   2262 C  CA    . LEU B 1 113 ? 25.274 5.571   12.671  1.00 16.73 ? 113 LEU B CA    1 
ATOM   2263 C  C     . LEU B 1 113 ? 24.306 6.610   12.102  1.00 18.99 ? 113 LEU B C     1 
ATOM   2264 O  O     . LEU B 1 113 ? 23.579 6.327   11.150  1.00 17.05 ? 113 LEU B O     1 
ATOM   2265 C  CB    . LEU B 1 113 ? 26.351 5.218   11.639  1.00 16.41 ? 113 LEU B CB    1 
ATOM   2266 C  CG    . LEU B 1 113 ? 27.205 6.376   11.125  1.00 17.07 ? 113 LEU B CG    1 
ATOM   2267 C  CD1   . LEU B 1 113 ? 28.021 6.947   12.292  1.00 21.01 ? 113 LEU B CD1   1 
ATOM   2268 C  CD2   . LEU B 1 113 ? 28.114 5.938   9.943   1.00 22.11 ? 113 LEU B CD2   1 
ATOM   2269 N  N     . VAL B 1 114 ? 24.312 7.817   12.668  1.00 17.16 ? 114 VAL B N     1 
ATOM   2270 C  CA    . VAL B 1 114 ? 23.375 8.879   12.307  1.00 17.94 ? 114 VAL B CA    1 
ATOM   2271 C  C     . VAL B 1 114 ? 24.173 10.052  11.764  1.00 18.24 ? 114 VAL B C     1 
ATOM   2272 O  O     . VAL B 1 114 ? 25.022 10.610  12.473  1.00 17.26 ? 114 VAL B O     1 
ATOM   2273 C  CB    . VAL B 1 114 ? 22.524 9.322   13.510  1.00 19.93 ? 114 VAL B CB    1 
ATOM   2274 C  CG1   . VAL B 1 114 ? 21.607 10.481  13.134  1.00 21.82 ? 114 VAL B CG1   1 
ATOM   2275 C  CG2   . VAL B 1 114 ? 21.709 8.129   14.037  1.00 23.76 ? 114 VAL B CG2   1 
ATOM   2276 N  N     . GLY B 1 115 ? 23.877 10.444  10.529  1.00 17.18 ? 115 GLY B N     1 
ATOM   2277 C  CA    . GLY B 1 115 ? 24.388 11.706  10.019  1.00 21.12 ? 115 GLY B CA    1 
ATOM   2278 C  C     . GLY B 1 115 ? 23.324 12.780  10.089  1.00 21.70 ? 115 GLY B C     1 
ATOM   2279 O  O     . GLY B 1 115 ? 22.367 12.762  9.302   1.00 23.04 ? 115 GLY B O     1 
ATOM   2280 N  N     . ASN B 1 116 ? 23.469 13.714  11.025  1.00 17.60 ? 116 ASN B N     1 
ATOM   2281 C  CA    . ASN B 1 116 ? 22.460 14.726  11.280  1.00 19.13 ? 116 ASN B CA    1 
ATOM   2282 C  C     . ASN B 1 116 ? 22.733 16.009  10.498  1.00 23.35 ? 116 ASN B C     1 
ATOM   2283 O  O     . ASN B 1 116 ? 23.825 16.221  9.961   1.00 20.14 ? 116 ASN B O     1 
ATOM   2284 C  CB    . ASN B 1 116 ? 22.389 15.012  12.778  1.00 17.26 ? 116 ASN B CB    1 
ATOM   2285 C  CG    . ASN B 1 116 ? 21.194 15.836  13.161  1.00 20.40 ? 116 ASN B CG    1 
ATOM   2286 O  OD1   . ASN B 1 116 ? 20.076 15.617  12.675  1.00 21.79 ? 116 ASN B OD1   1 
ATOM   2287 N  ND2   . ASN B 1 116 ? 21.410 16.784  14.061  1.00 21.25 ? 116 ASN B ND2   1 
ATOM   2288 N  N     . LYS B 1 117 ? 21.709 16.881  10.482  1.00 16.69 ? 117 LYS B N     1 
ATOM   2289 C  CA    . LYS B 1 117 ? 21.687 18.172  9.784   1.00 20.84 ? 117 LYS B CA    1 
ATOM   2290 C  C     . LYS B 1 117 ? 21.557 18.017  8.265   1.00 25.89 ? 117 LYS B C     1 
ATOM   2291 O  O     . LYS B 1 117 ? 22.138 18.798  7.505   1.00 24.49 ? 117 LYS B O     1 
ATOM   2292 C  CB    . LYS B 1 117 ? 22.908 19.029  10.134  1.00 23.18 ? 117 LYS B CB    1 
ATOM   2293 C  CG    . LYS B 1 117 ? 23.182 19.105  11.647  1.00 19.56 ? 117 LYS B CG    1 
ATOM   2294 C  CD    . LYS B 1 117 ? 24.088 20.294  11.987  1.00 21.21 ? 117 LYS B CD    1 
ATOM   2295 C  CE    . LYS B 1 117 ? 24.358 20.328  13.490  1.00 24.17 ? 117 LYS B CE    1 
ATOM   2296 N  NZ    . LYS B 1 117 ? 25.153 21.524  13.856  1.00 26.33 ? 117 LYS B NZ    1 
ATOM   2297 N  N     . SER B 1 118 ? 20.760 17.044  7.806   1.00 23.25 ? 118 SER B N     1 
ATOM   2298 C  CA    A SER B 1 118 ? 20.615 16.826  6.368   0.80 28.64 ? 118 SER B CA    1 
ATOM   2299 C  CA    B SER B 1 118 ? 20.618 16.826  6.370   0.20 29.29 ? 118 SER B CA    1 
ATOM   2300 C  C     . SER B 1 118 ? 19.912 17.983  5.675   1.00 31.61 ? 118 SER B C     1 
ATOM   2301 O  O     . SER B 1 118 ? 19.985 18.082  4.443   1.00 33.46 ? 118 SER B O     1 
ATOM   2302 C  CB    A SER B 1 118 ? 19.849 15.531  6.084   0.80 27.50 ? 118 SER B CB    1 
ATOM   2303 C  CB    B SER B 1 118 ? 19.871 15.519  6.105   0.20 28.06 ? 118 SER B CB    1 
ATOM   2304 O  OG    A SER B 1 118 ? 18.532 15.605  6.607   0.80 29.10 ? 118 SER B OG    1 
ATOM   2305 O  OG    B SER B 1 118 ? 20.609 14.412  6.590   0.20 28.28 ? 118 SER B OG    1 
ATOM   2306 N  N     . ASP B 1 119 ? 19.239 18.855  6.429   1.00 27.16 ? 119 ASP B N     1 
ATOM   2307 C  CA    . ASP B 1 119 ? 18.608 20.040  5.854   1.00 26.32 ? 119 ASP B CA    1 
ATOM   2308 C  C     . ASP B 1 119 ? 19.622 21.058  5.345   1.00 36.71 ? 119 ASP B C     1 
ATOM   2309 O  O     . ASP B 1 119 ? 19.225 22.016  4.672   1.00 34.71 ? 119 ASP B O     1 
ATOM   2310 C  CB    . ASP B 1 119 ? 17.714 20.726  6.889   1.00 27.63 ? 119 ASP B CB    1 
ATOM   2311 C  CG    . ASP B 1 119 ? 18.477 21.111  8.154   1.00 30.91 ? 119 ASP B CG    1 
ATOM   2312 O  OD1   . ASP B 1 119 ? 18.895 20.198  8.895   1.00 27.74 ? 119 ASP B OD1   1 
ATOM   2313 O  OD2   . ASP B 1 119 ? 18.670 22.321  8.409   1.00 29.09 ? 119 ASP B OD2   1 
ATOM   2314 N  N     . LEU B 1 120 ? 20.908 20.882  5.644   1.00 30.70 ? 120 LEU B N     1 
ATOM   2315 C  CA    . LEU B 1 120 ? 21.855 21.923  5.252   1.00 34.92 ? 120 LEU B CA    1 
ATOM   2316 C  C     . LEU B 1 120 ? 22.423 21.635  3.866   1.00 42.89 ? 120 LEU B C     1 
ATOM   2317 O  O     . LEU B 1 120 ? 22.619 20.470  3.505   1.00 45.70 ? 120 LEU B O     1 
ATOM   2318 C  CB    . LEU B 1 120 ? 23.004 22.011  6.252   1.00 34.70 ? 120 LEU B CB    1 
ATOM   2319 C  CG    . LEU B 1 120 ? 22.685 22.442  7.683   1.00 31.26 ? 120 LEU B CG    1 
ATOM   2320 C  CD1   . LEU B 1 120 ? 23.955 22.398  8.534   1.00 33.10 ? 120 LEU B CD1   1 
ATOM   2321 C  CD2   . LEU B 1 120 ? 22.051 23.835  7.721   1.00 33.98 ? 120 LEU B CD2   1 
ATOM   2322 N  N     . PRO B 1 121 ? 22.693 22.670  3.064   1.00 46.00 ? 121 PRO B N     1 
ATOM   2323 C  CA    . PRO B 1 121 ? 23.337 22.433  1.761   1.00 49.47 ? 121 PRO B CA    1 
ATOM   2324 C  C     . PRO B 1 121 ? 24.858 22.332  1.816   1.00 46.22 ? 121 PRO B C     1 
ATOM   2325 O  O     . PRO B 1 121 ? 25.454 21.817  0.863   1.00 54.79 ? 121 PRO B O     1 
ATOM   2326 C  CB    . PRO B 1 121 ? 22.896 23.650  0.939   1.00 54.23 ? 121 PRO B CB    1 
ATOM   2327 C  CG    . PRO B 1 121 ? 22.813 24.744  1.976   1.00 49.06 ? 121 PRO B CG    1 
ATOM   2328 C  CD    . PRO B 1 121 ? 22.258 24.071  3.221   1.00 44.02 ? 121 PRO B CD    1 
ATOM   2329 N  N     . SER B 1 122 ? 25.501 22.773  2.900   1.00 48.85 ? 122 SER B N     1 
ATOM   2330 C  CA    . SER B 1 122 ? 26.958 22.881  2.970   1.00 48.64 ? 122 SER B CA    1 
ATOM   2331 C  C     . SER B 1 122 ? 27.634 21.571  3.370   1.00 48.39 ? 122 SER B C     1 
ATOM   2332 O  O     . SER B 1 122 ? 28.485 21.555  4.269   1.00 46.60 ? 122 SER B O     1 
ATOM   2333 C  CB    . SER B 1 122 ? 27.359 23.968  3.970   1.00 51.77 ? 122 SER B CB    1 
ATOM   2334 O  OG    . SER B 1 122 ? 26.521 23.937  5.119   1.00 51.22 ? 122 SER B OG    1 
ATOM   2335 N  N     . ARG B 1 123 ? 27.295 20.481  2.693   1.00 40.57 ? 123 ARG B N     1 
ATOM   2336 C  CA    . ARG B 1 123 ? 27.711 19.151  3.121   1.00 35.31 ? 123 ARG B CA    1 
ATOM   2337 C  C     . ARG B 1 123 ? 29.206 18.913  2.894   1.00 36.29 ? 123 ARG B C     1 
ATOM   2338 O  O     . ARG B 1 123 ? 29.739 19.248  1.834   1.00 34.26 ? 123 ARG B O     1 
ATOM   2339 C  CB    . ARG B 1 123 ? 26.867 18.134  2.369   1.00 36.10 ? 123 ARG B CB    1 
ATOM   2340 C  CG    . ARG B 1 123 ? 27.309 16.739  2.480   1.00 36.41 ? 123 ARG B CG    1 
ATOM   2341 C  CD    . ARG B 1 123 ? 26.346 15.830  1.751   1.00 35.02 ? 123 ARG B CD    1 
ATOM   2342 N  NE    . ARG B 1 123 ? 26.387 14.523  2.383   1.00 41.96 ? 123 ARG B NE    1 
ATOM   2343 C  CZ    . ARG B 1 123 ? 25.362 13.933  2.980   1.00 37.35 ? 123 ARG B CZ    1 
ATOM   2344 N  NH1   . ARG B 1 123 ? 24.138 14.441  2.929   1.00 35.54 ? 123 ARG B NH1   1 
ATOM   2345 N  NH2   . ARG B 1 123 ? 25.572 12.801  3.642   1.00 37.75 ? 123 ARG B NH2   1 
ATOM   2346 N  N     . THR B 1 124 ? 29.900 18.354  3.908   1.00 27.49 ? 124 THR B N     1 
ATOM   2347 C  CA    . THR B 1 124 ? 31.307 17.997  3.765   1.00 25.54 ? 124 THR B CA    1 
ATOM   2348 C  C     . THR B 1 124 ? 31.593 16.505  3.913   1.00 28.42 ? 124 THR B C     1 
ATOM   2349 O  O     . THR B 1 124 ? 32.675 16.055  3.513   1.00 30.75 ? 124 THR B O     1 
ATOM   2350 C  CB    . THR B 1 124 ? 32.175 18.791  4.764   1.00 28.67 ? 124 THR B CB    1 
ATOM   2351 O  OG1   . THR B 1 124 ? 31.880 18.387  6.102   1.00 28.47 ? 124 THR B OG1   1 
ATOM   2352 C  CG2   . THR B 1 124 ? 31.897 20.280  4.644   1.00 29.84 ? 124 THR B CG2   1 
ATOM   2353 N  N     . VAL B 1 125 ? 30.667 15.716  4.436   1.00 24.31 ? 125 VAL B N     1 
ATOM   2354 C  CA    . VAL B 1 125 ? 30.840 14.272  4.507   1.00 25.07 ? 125 VAL B CA    1 
ATOM   2355 C  C     . VAL B 1 125 ? 29.898 13.689  3.468   1.00 30.70 ? 125 VAL B C     1 
ATOM   2356 O  O     . VAL B 1 125 ? 28.675 13.827  3.592   1.00 28.84 ? 125 VAL B O     1 
ATOM   2357 C  CB    . VAL B 1 125 ? 30.536 13.720  5.911   1.00 22.82 ? 125 VAL B CB    1 
ATOM   2358 C  CG1   . VAL B 1 125 ? 30.770 12.225  5.961   1.00 25.11 ? 125 VAL B CG1   1 
ATOM   2359 C  CG2   . VAL B 1 125 ? 31.365 14.460  6.974   1.00 23.69 ? 125 VAL B CG2   1 
ATOM   2360 N  N     . ASP B 1 126 ? 30.446 13.099  2.410   1.00 31.04 ? 126 ASP B N     1 
ATOM   2361 C  CA    . ASP B 1 126 ? 29.565 12.560  1.383   1.00 36.65 ? 126 ASP B CA    1 
ATOM   2362 C  C     . ASP B 1 126 ? 28.886 11.286  1.884   1.00 35.20 ? 126 ASP B C     1 
ATOM   2363 O  O     . ASP B 1 126 ? 29.448 10.516  2.672   1.00 33.02 ? 126 ASP B O     1 
ATOM   2364 C  CB    . ASP B 1 126 ? 30.305 12.361  0.049   1.00 43.62 ? 126 ASP B CB    1 
ATOM   2365 C  CG    . ASP B 1 126 ? 31.200 11.163  0.031   1.00 45.33 ? 126 ASP B CG    1 
ATOM   2366 O  OD1   . ASP B 1 126 ? 32.134 11.109  0.856   1.00 50.65 ? 126 ASP B OD1   1 
ATOM   2367 O  OD2   . ASP B 1 126 ? 30.983 10.292  -0.837  1.00 47.24 ? 126 ASP B OD2   1 
ATOM   2368 N  N     . THR B 1 127 ? 27.654 11.078  1.417   1.00 34.04 ? 127 THR B N     1 
ATOM   2369 C  CA    . THR B 1 127 ? 26.869 9.922   1.835   1.00 32.12 ? 127 THR B CA    1 
ATOM   2370 C  C     . THR B 1 127 ? 27.590 8.604   1.580   1.00 33.07 ? 127 THR B C     1 
ATOM   2371 O  O     . THR B 1 127 ? 27.431 7.655   2.358   1.00 28.25 ? 127 THR B O     1 
ATOM   2372 C  CB    . THR B 1 127 ? 25.517 9.932   1.119   1.00 37.81 ? 127 THR B CB    1 
ATOM   2373 O  OG1   . THR B 1 127 ? 24.861 11.182  1.359   1.00 45.44 ? 127 THR B OG1   1 
ATOM   2374 C  CG2   . THR B 1 127 ? 24.632 8.839   1.646   1.00 34.70 ? 127 THR B CG2   1 
ATOM   2375 N  N     . LYS B 1 128 ? 28.384 8.518   0.505   1.00 29.06 ? 128 LYS B N     1 
ATOM   2376 C  CA    . LYS B 1 128 ? 29.060 7.260   0.196   1.00 29.39 ? 128 LYS B CA    1 
ATOM   2377 C  C     . LYS B 1 128 ? 30.117 6.917   1.245   1.00 27.83 ? 128 LYS B C     1 
ATOM   2378 O  O     . LYS B 1 128 ? 30.170 5.777   1.715   1.00 28.31 ? 128 LYS B O     1 
ATOM   2379 C  CB    . LYS B 1 128 ? 29.682 7.341   -1.202  1.00 34.67 ? 128 LYS B CB    1 
ATOM   2380 C  CG    . LYS B 1 128 ? 30.658 6.230   -1.529  1.00 37.13 ? 128 LYS B CG    1 
ATOM   2381 C  CD    . LYS B 1 128 ? 29.956 4.955   -1.895  1.00 35.15 ? 128 LYS B CD    1 
ATOM   2382 C  CE    . LYS B 1 128 ? 30.825 4.098   -2.808  1.00 35.31 ? 128 LYS B CE    1 
ATOM   2383 N  NZ    . LYS B 1 128 ? 32.121 3.719   -2.201  1.00 34.08 ? 128 LYS B NZ    1 
ATOM   2384 N  N     . GLN B 1 129 ? 30.942 7.900   1.635   1.00 27.63 ? 129 GLN B N     1 
ATOM   2385 C  CA    . GLN B 1 129 ? 31.917 7.747   2.720   1.00 30.16 ? 129 GLN B CA    1 
ATOM   2386 C  C     . GLN B 1 129 ? 31.270 7.208   3.987   1.00 22.12 ? 129 GLN B C     1 
ATOM   2387 O  O     . GLN B 1 129 ? 31.752 6.245   4.612   1.00 26.33 ? 129 GLN B O     1 
ATOM   2388 C  CB    . GLN B 1 129 ? 32.531 9.120   3.020   1.00 34.92 ? 129 GLN B CB    1 
ATOM   2389 C  CG    . GLN B 1 129 ? 33.765 9.197   3.914   1.00 46.92 ? 129 GLN B CG    1 
ATOM   2390 C  CD    . GLN B 1 129 ? 34.445 10.576  3.819   1.00 51.51 ? 129 GLN B CD    1 
ATOM   2391 O  OE1   . GLN B 1 129 ? 33.845 11.553  3.344   1.00 49.05 ? 129 GLN B OE1   1 
ATOM   2392 N  NE2   . GLN B 1 129 ? 35.690 10.657  4.284   1.00 54.13 ? 129 GLN B NE2   1 
ATOM   2393 N  N     . ALA B 1 130 ? 30.184 7.853   4.395   1.00 24.41 ? 130 ALA B N     1 
ATOM   2394 C  CA    . ALA B 1 130 ? 29.541 7.491   5.647   1.00 24.35 ? 130 ALA B CA    1 
ATOM   2395 C  C     . ALA B 1 130 ? 28.928 6.103   5.563   1.00 25.37 ? 130 ALA B C     1 
ATOM   2396 O  O     . ALA B 1 130 ? 29.091 5.278   6.475   1.00 23.41 ? 130 ALA B O     1 
ATOM   2397 C  CB    . ALA B 1 130 ? 28.488 8.536   5.999   1.00 25.18 ? 130 ALA B CB    1 
ATOM   2398 N  N     . GLN B 1 131 ? 28.196 5.819   4.478   1.00 24.20 ? 131 GLN B N     1 
ATOM   2399 C  CA    . GLN B 1 131 ? 27.610 4.490   4.357   1.00 22.53 ? 131 GLN B CA    1 
ATOM   2400 C  C     . GLN B 1 131 ? 28.689 3.409   4.326   1.00 21.69 ? 131 GLN B C     1 
ATOM   2401 O  O     . GLN B 1 131 ? 28.484 2.320   4.866   1.00 25.67 ? 131 GLN B O     1 
ATOM   2402 C  CB    . GLN B 1 131 ? 26.654 4.427   3.161   1.00 27.42 ? 131 GLN B CB    1 
ATOM   2403 C  CG    . GLN B 1 131 ? 27.241 4.107   1.824   1.00 36.46 ? 131 GLN B CG    1 
ATOM   2404 C  CD    . GLN B 1 131 ? 26.163 4.144   0.753   1.00 30.93 ? 131 GLN B CD    1 
ATOM   2405 O  OE1   . GLN B 1 131 ? 26.370 3.697   -0.361  1.00 35.79 ? 131 GLN B OE1   1 
ATOM   2406 N  NE2   . GLN B 1 131 ? 25.003 4.680   1.101   1.00 35.79 ? 131 GLN B NE2   1 
ATOM   2407 N  N     . ASP B 1 132 ? 29.833 3.674   3.675   1.00 24.39 ? 132 ASP B N     1 
ATOM   2408 C  CA    . ASP B 1 132 ? 30.922 2.691   3.635   1.00 23.08 ? 132 ASP B CA    1 
ATOM   2409 C  C     . ASP B 1 132 ? 31.461 2.408   5.035   1.00 22.87 ? 132 ASP B C     1 
ATOM   2410 O  O     . ASP B 1 132 ? 31.812 1.263   5.365   1.00 25.10 ? 132 ASP B O     1 
ATOM   2411 C  CB    . ASP B 1 132 ? 32.050 3.158   2.714   1.00 26.98 ? 132 ASP B CB    1 
ATOM   2412 C  CG    . ASP B 1 132 ? 31.717 2.986   1.240   1.00 33.40 ? 132 ASP B CG    1 
ATOM   2413 O  OD1   . ASP B 1 132 ? 30.699 2.318   0.923   1.00 31.31 ? 132 ASP B OD1   1 
ATOM   2414 O  OD2   . ASP B 1 132 ? 32.480 3.526   0.414   1.00 32.66 ? 132 ASP B OD2   1 
ATOM   2415 N  N     . LEU B 1 133 ? 31.623 3.456   5.842   1.00 23.95 ? 133 LEU B N     1 
ATOM   2416 C  CA    . LEU B 1 133 ? 32.004 3.225   7.239   1.00 23.80 ? 133 LEU B CA    1 
ATOM   2417 C  C     . LEU B 1 133 ? 30.996 2.315   7.944   1.00 23.33 ? 133 LEU B C     1 
ATOM   2418 O  O     . LEU B 1 133 ? 31.371 1.322   8.584   1.00 23.05 ? 133 LEU B O     1 
ATOM   2419 C  CB    . LEU B 1 133 ? 32.137 4.553   7.979   1.00 22.27 ? 133 LEU B CB    1 
ATOM   2420 C  CG    . LEU B 1 133 ? 32.679 4.426   9.410   1.00 26.70 ? 133 LEU B CG    1 
ATOM   2421 C  CD1   . LEU B 1 133 ? 34.064 3.792   9.399   1.00 31.13 ? 133 LEU B CD1   1 
ATOM   2422 C  CD2   . LEU B 1 133 ? 32.717 5.797   10.068  1.00 28.64 ? 133 LEU B CD2   1 
ATOM   2423 N  N     . ALA B 1 134 ? 29.700 2.637   7.828   1.00 21.75 ? 134 ALA B N     1 
ATOM   2424 C  CA    . ALA B 1 134 ? 28.677 1.809   8.478   1.00 20.34 ? 134 ALA B CA    1 
ATOM   2425 C  C     . ALA B 1 134 ? 28.713 0.369   7.971   1.00 22.72 ? 134 ALA B C     1 
ATOM   2426 O  O     . ALA B 1 134 ? 28.474 -0.573  8.735   1.00 24.14 ? 134 ALA B O     1 
ATOM   2427 C  CB    . ALA B 1 134 ? 27.278 2.404   8.268   1.00 20.11 ? 134 ALA B CB    1 
ATOM   2428 N  N     . ARG B 1 135 ? 28.977 0.174   6.676   1.00 21.80 ? 135 ARG B N     1 
ATOM   2429 C  CA    . ARG B 1 135 ? 29.051 -1.189  6.155   1.00 22.57 ? 135 ARG B CA    1 
ATOM   2430 C  C     . ARG B 1 135 ? 30.258 -1.933  6.725   1.00 21.02 ? 135 ARG B C     1 
ATOM   2431 O  O     . ARG B 1 135 ? 30.173 -3.132  7.016   1.00 25.65 ? 135 ARG B O     1 
ATOM   2432 C  CB    . ARG B 1 135 ? 29.080 -1.170  4.623   1.00 24.08 ? 135 ARG B CB    1 
ATOM   2433 C  CG    . ARG B 1 135 ? 27.776 -0.651  4.013   1.00 23.33 ? 135 ARG B CG    1 
ATOM   2434 C  CD    . ARG B 1 135 ? 27.795 -0.612  2.486   1.00 28.30 ? 135 ARG B CD    1 
ATOM   2435 N  NE    . ARG B 1 135 ? 26.553 -0.018  1.990   1.00 27.16 ? 135 ARG B NE    1 
ATOM   2436 C  CZ    . ARG B 1 135 ? 26.123 -0.108  0.738   1.00 28.01 ? 135 ARG B CZ    1 
ATOM   2437 N  NH1   . ARG B 1 135 ? 26.816 -0.753  -0.186  1.00 25.10 ? 135 ARG B NH1   1 
ATOM   2438 N  NH2   . ARG B 1 135 ? 24.958 0.444   0.412   1.00 23.51 ? 135 ARG B NH2   1 
ATOM   2439 N  N     . SER B 1 136 ? 31.392 -1.249  6.900   1.00 24.89 ? 136 SER B N     1 
ATOM   2440 C  CA    . SER B 1 136 ? 32.523 -1.930  7.538   1.00 25.67 ? 136 SER B CA    1 
ATOM   2441 C  C     . SER B 1 136 ? 32.219 -2.279  8.996   1.00 28.17 ? 136 SER B C     1 
ATOM   2442 O  O     . SER B 1 136 ? 32.660 -3.326  9.489   1.00 29.29 ? 136 SER B O     1 
ATOM   2443 C  CB    . SER B 1 136 ? 33.790 -1.082  7.438   1.00 30.28 ? 136 SER B CB    1 
ATOM   2444 O  OG    . SER B 1 136 ? 33.708 0.036   8.289   1.00 34.07 ? 136 SER B OG    1 
ATOM   2445 N  N     . TYR B 1 137 ? 31.445 -1.438  9.690   1.00 24.19 ? 137 TYR B N     1 
ATOM   2446 C  CA    . TYR B 1 137 ? 31.009 -1.753  11.050  1.00 24.76 ? 137 TYR B CA    1 
ATOM   2447 C  C     . TYR B 1 137 ? 29.879 -2.771  11.107  1.00 27.80 ? 137 TYR B C     1 
ATOM   2448 O  O     . TYR B 1 137 ? 29.631 -3.344  12.178  1.00 27.25 ? 137 TYR B O     1 
ATOM   2449 C  CB    . TYR B 1 137 ? 30.518 -0.491  11.772  1.00 25.05 ? 137 TYR B CB    1 
ATOM   2450 C  CG    . TYR B 1 137 ? 31.553 0.567   12.078  1.00 25.75 ? 137 TYR B CG    1 
ATOM   2451 C  CD1   . TYR B 1 137 ? 32.925 0.305   12.007  1.00 29.34 ? 137 TYR B CD1   1 
ATOM   2452 C  CD2   . TYR B 1 137 ? 31.146 1.846   12.460  1.00 24.50 ? 137 TYR B CD2   1 
ATOM   2453 C  CE1   . TYR B 1 137 ? 33.868 1.303   12.319  1.00 26.44 ? 137 TYR B CE1   1 
ATOM   2454 C  CE2   . TYR B 1 137 ? 32.069 2.832   12.766  1.00 27.53 ? 137 TYR B CE2   1 
ATOM   2455 C  CZ    . TYR B 1 137 ? 33.423 2.560   12.695  1.00 30.73 ? 137 TYR B CZ    1 
ATOM   2456 O  OH    . TYR B 1 137 ? 34.303 3.582   13.001  1.00 32.08 ? 137 TYR B OH    1 
ATOM   2457 N  N     . GLY B 1 138 ? 29.174 -2.983  10.000  1.00 26.50 ? 138 GLY B N     1 
ATOM   2458 C  CA    . GLY B 1 138 ? 28.025 -3.866  9.993   1.00 24.50 ? 138 GLY B CA    1 
ATOM   2459 C  C     . GLY B 1 138 ? 26.779 -3.313  10.650  1.00 25.84 ? 138 GLY B C     1 
ATOM   2460 O  O     . GLY B 1 138 ? 25.998 -4.091  11.212  1.00 24.60 ? 138 GLY B O     1 
ATOM   2461 N  N     . ILE B 1 139 ? 26.549 -1.998  10.580  1.00 21.65 ? 139 ILE B N     1 
ATOM   2462 C  CA    . ILE B 1 139 ? 25.435 -1.390  11.306  1.00 21.02 ? 139 ILE B CA    1 
ATOM   2463 C  C     . ILE B 1 139 ? 24.654 -0.494  10.353  1.00 19.59 ? 139 ILE B C     1 
ATOM   2464 O  O     . ILE B 1 139 ? 25.157 -0.097  9.291   1.00 22.03 ? 139 ILE B O     1 
ATOM   2465 C  CB    . ILE B 1 139 ? 25.919 -0.566  12.531  1.00 22.93 ? 139 ILE B CB    1 
ATOM   2466 C  CG1   . ILE B 1 139 ? 26.800 0.594   12.084  1.00 19.86 ? 139 ILE B CG1   1 
ATOM   2467 C  CG2   . ILE B 1 139 ? 26.684 -1.436  13.523  1.00 25.47 ? 139 ILE B CG2   1 
ATOM   2468 C  CD1   . ILE B 1 139 ? 27.120 1.622   13.210  1.00 19.64 ? 139 ILE B CD1   1 
ATOM   2469 N  N     . PRO B 1 140 ? 23.420 -0.141  10.709  1.00 21.40 ? 140 PRO B N     1 
ATOM   2470 C  CA    . PRO B 1 140 ? 22.636 0.746   9.843   1.00 21.37 ? 140 PRO B CA    1 
ATOM   2471 C  C     . PRO B 1 140 ? 23.166 2.172   9.863   1.00 22.27 ? 140 PRO B C     1 
ATOM   2472 O  O     . PRO B 1 140 ? 23.830 2.618   10.802  1.00 22.41 ? 140 PRO B O     1 
ATOM   2473 C  CB    . PRO B 1 140 ? 21.224 0.690   10.444  1.00 21.39 ? 140 PRO B CB    1 
ATOM   2474 C  CG    . PRO B 1 140 ? 21.208 -0.565  11.273  1.00 24.56 ? 140 PRO B CG    1 
ATOM   2475 C  CD    . PRO B 1 140 ? 22.601 -0.716  11.791  1.00 22.68 ? 140 PRO B CD    1 
ATOM   2476 N  N     . PHE B 1 141 ? 22.864 2.885   8.783   1.00 21.23 ? 141 PHE B N     1 
ATOM   2477 C  CA    . PHE B 1 141 ? 23.226 4.283   8.602   1.00 18.10 ? 141 PHE B CA    1 
ATOM   2478 C  C     . PHE B 1 141 ? 21.988 5.057   8.176   1.00 24.83 ? 141 PHE B C     1 
ATOM   2479 O  O     . PHE B 1 141 ? 21.350 4.712   7.174   1.00 24.93 ? 141 PHE B O     1 
ATOM   2480 C  CB    . PHE B 1 141 ? 24.319 4.445   7.544   1.00 21.85 ? 141 PHE B CB    1 
ATOM   2481 C  CG    . PHE B 1 141 ? 24.545 5.869   7.140   1.00 26.65 ? 141 PHE B CG    1 
ATOM   2482 C  CD1   . PHE B 1 141 ? 24.899 6.818   8.083   1.00 25.02 ? 141 PHE B CD1   1 
ATOM   2483 C  CD2   . PHE B 1 141 ? 24.374 6.272   5.819   1.00 27.40 ? 141 PHE B CD2   1 
ATOM   2484 C  CE1   . PHE B 1 141 ? 25.102 8.141   7.712   1.00 22.36 ? 141 PHE B CE1   1 
ATOM   2485 C  CE2   . PHE B 1 141 ? 24.576 7.599   5.448   1.00 27.86 ? 141 PHE B CE2   1 
ATOM   2486 C  CZ    . PHE B 1 141 ? 24.933 8.530   6.396   1.00 28.64 ? 141 PHE B CZ    1 
ATOM   2487 N  N     . ILE B 1 142 ? 21.661 6.111   8.909   1.00 21.60 ? 142 ILE B N     1 
ATOM   2488 C  CA    . ILE B 1 142 ? 20.489 6.926   8.618   1.00 22.67 ? 142 ILE B CA    1 
ATOM   2489 C  C     . ILE B 1 142 ? 20.869 8.396   8.696   1.00 26.11 ? 142 ILE B C     1 
ATOM   2490 O  O     . ILE B 1 142 ? 21.543 8.824   9.642   1.00 21.14 ? 142 ILE B O     1 
ATOM   2491 C  CB    . ILE B 1 142 ? 19.338 6.603   9.589   1.00 23.67 ? 142 ILE B CB    1 
ATOM   2492 C  CG1   . ILE B 1 142 ? 19.018 5.105   9.529   1.00 31.07 ? 142 ILE B CG1   1 
ATOM   2493 C  CG2   . ILE B 1 142 ? 18.107 7.465   9.300   1.00 28.30 ? 142 ILE B CG2   1 
ATOM   2494 C  CD1   . ILE B 1 142 ? 18.058 4.622   10.581  1.00 35.42 ? 142 ILE B CD1   1 
ATOM   2495 N  N     . GLU B 1 143 ? 20.421 9.176   7.712   1.00 19.61 ? 143 GLU B N     1 
ATOM   2496 C  CA    . GLU B 1 143 ? 20.606 10.623  7.733   1.00 20.91 ? 143 GLU B CA    1 
ATOM   2497 C  C     . GLU B 1 143 ? 19.346 11.264  8.285   1.00 24.61 ? 143 GLU B C     1 
ATOM   2498 O  O     . GLU B 1 143 ? 18.233 10.876  7.919   1.00 28.06 ? 143 GLU B O     1 
ATOM   2499 C  CB    . GLU B 1 143 ? 20.917 11.188  6.341   1.00 26.82 ? 143 GLU B CB    1 
ATOM   2500 C  CG    . GLU B 1 143 ? 22.200 10.665  5.749   1.00 27.57 ? 143 GLU B CG    1 
ATOM   2501 C  CD    . GLU B 1 143 ? 22.773 11.546  4.646   1.00 37.93 ? 143 GLU B CD    1 
ATOM   2502 O  OE1   . GLU B 1 143 ? 22.009 12.310  4.012   1.00 40.75 ? 143 GLU B OE1   1 
ATOM   2503 O  OE2   . GLU B 1 143 ? 23.995 11.435  4.389   1.00 39.81 ? 143 GLU B OE2   1 
ATOM   2504 N  N     . THR B 1 144 ? 19.524 12.239  9.172   1.00 21.11 ? 144 THR B N     1 
ATOM   2505 C  CA    . THR B 1 144 ? 18.428 12.862  9.895   1.00 17.49 ? 144 THR B CA    1 
ATOM   2506 C  C     . THR B 1 144 ? 18.530 14.375  9.799   1.00 23.38 ? 144 THR B C     1 
ATOM   2507 O  O     . THR B 1 144 ? 19.584 14.938  9.489   1.00 21.82 ? 144 THR B O     1 
ATOM   2508 C  CB    . THR B 1 144 ? 18.426 12.493  11.377  1.00 25.14 ? 144 THR B CB    1 
ATOM   2509 O  OG1   . THR B 1 144 ? 19.626 13.001  11.992  1.00 19.63 ? 144 THR B OG1   1 
ATOM   2510 C  CG2   . THR B 1 144 ? 18.351 10.985  11.561  1.00 23.52 ? 144 THR B CG2   1 
ATOM   2511 N  N     . SER B 1 145 ? 17.412 15.022  10.106  1.00 21.94 ? 145 SER B N     1 
ATOM   2512 C  CA    . SER B 1 145 ? 17.390 16.438  10.440  1.00 23.06 ? 145 SER B CA    1 
ATOM   2513 C  C     . SER B 1 145 ? 16.515 16.597  11.669  1.00 24.41 ? 145 SER B C     1 
ATOM   2514 O  O     . SER B 1 145 ? 15.311 16.327  11.609  1.00 23.30 ? 145 SER B O     1 
ATOM   2515 C  CB    . SER B 1 145 ? 16.855 17.289  9.283   1.00 24.16 ? 145 SER B CB    1 
ATOM   2516 O  OG    . SER B 1 145 ? 16.703 18.636  9.699   1.00 23.02 ? 145 SER B OG    1 
ATOM   2517 N  N     . ALA B 1 146 ? 17.112 17.020  12.791  1.00 19.92 ? 146 ALA B N     1 
ATOM   2518 C  CA    . ALA B 1 146 ? 16.278 17.361  13.931  1.00 22.60 ? 146 ALA B CA    1 
ATOM   2519 C  C     . ALA B 1 146 ? 15.445 18.610  13.654  1.00 21.99 ? 146 ALA B C     1 
ATOM   2520 O  O     . ALA B 1 146 ? 14.386 18.786  14.265  1.00 27.70 ? 146 ALA B O     1 
ATOM   2521 C  CB    . ALA B 1 146 ? 17.136 17.532  15.188  1.00 25.64 ? 146 ALA B CB    1 
ATOM   2522 N  N     . LYS B 1 147 ? 15.875 19.451  12.709  1.00 24.75 ? 147 LYS B N     1 
ATOM   2523 C  CA    . LYS B 1 147 ? 15.144 20.684  12.430  1.00 27.07 ? 147 LYS B CA    1 
ATOM   2524 C  C     . LYS B 1 147 ? 13.828 20.403  11.706  1.00 30.86 ? 147 LYS B C     1 
ATOM   2525 O  O     . LYS B 1 147 ? 12.778 20.925  12.098  1.00 30.61 ? 147 LYS B O     1 
ATOM   2526 C  CB    . LYS B 1 147 ? 16.022 21.628  11.609  1.00 28.86 ? 147 LYS B CB    1 
ATOM   2527 C  CG    . LYS B 1 147 ? 15.319 22.906  11.152  1.00 33.48 ? 147 LYS B CG    1 
ATOM   2528 C  CD    . LYS B 1 147 ? 16.286 24.089  11.059  1.00 38.29 ? 147 LYS B CD    1 
ATOM   2529 C  CE    . LYS B 1 147 ? 15.694 25.220  10.210  1.00 48.17 ? 147 LYS B CE    1 
ATOM   2530 N  NZ    . LYS B 1 147 ? 14.750 26.059  10.999  1.00 52.73 ? 147 LYS B NZ    1 
ATOM   2531 N  N     . THR B 1 148 ? 13.852 19.545  10.682  1.00 26.50 ? 148 THR B N     1 
ATOM   2532 C  CA    . THR B 1 148 ? 12.645 19.209  9.921   1.00 28.41 ? 148 THR B CA    1 
ATOM   2533 C  C     . THR B 1 148 ? 12.002 17.913  10.385  1.00 33.81 ? 148 THR B C     1 
ATOM   2534 O  O     . THR B 1 148 ? 10.920 17.564  9.894   1.00 32.06 ? 148 THR B O     1 
ATOM   2535 C  CB    . THR B 1 148 ? 12.955 19.074  8.431   1.00 28.52 ? 148 THR B CB    1 
ATOM   2536 O  OG1   . THR B 1 148 ? 13.713 17.871  8.220   1.00 34.65 ? 148 THR B OG1   1 
ATOM   2537 C  CG2   . THR B 1 148 ? 13.740 20.275  7.926   1.00 32.10 ? 148 THR B CG2   1 
ATOM   2538 N  N     . ARG B 1 149 ? 12.668 17.183  11.283  1.00 27.52 ? 149 ARG B N     1 
ATOM   2539 C  CA    . ARG B 1 149 ? 12.254 15.915  11.865  1.00 27.91 ? 149 ARG B CA    1 
ATOM   2540 C  C     . ARG B 1 149 ? 12.389 14.742  10.892  1.00 31.21 ? 149 ARG B C     1 
ATOM   2541 O  O     . ARG B 1 149 ? 12.028 13.611  11.249  1.00 30.61 ? 149 ARG B O     1 
ATOM   2542 C  CB    . ARG B 1 149 ? 10.833 16.012  12.440  1.00 29.62 ? 149 ARG B CB    1 
ATOM   2543 C  CG    . ARG B 1 149 ? 10.656 15.159  13.691  1.00 34.12 ? 149 ARG B CG    1 
ATOM   2544 C  CD    . ARG B 1 149 ? 9.220  15.097  14.195  1.00 41.86 ? 149 ARG B CD    1 
ATOM   2545 N  NE    . ARG B 1 149 ? 9.187  14.433  15.495  1.00 37.95 ? 149 ARG B NE    1 
ATOM   2546 C  CZ    . ARG B 1 149 ? 9.150  13.118  15.656  1.00 41.89 ? 149 ARG B CZ    1 
ATOM   2547 N  NH1   . ARG B 1 149 ? 9.137  12.297  14.617  1.00 40.56 ? 149 ARG B NH1   1 
ATOM   2548 N  NH2   . ARG B 1 149 ? 9.160  12.613  16.888  1.00 39.64 ? 149 ARG B NH2   1 
ATOM   2549 N  N     . GLN B 1 150 ? 12.955 14.962  9.698   1.00 25.60 ? 150 GLN B N     1 
ATOM   2550 C  CA    . GLN B 1 150 ? 13.278 13.869  8.781   1.00 24.14 ? 150 GLN B CA    1 
ATOM   2551 C  C     . GLN B 1 150 ? 14.141 12.807  9.453   1.00 28.67 ? 150 GLN B C     1 
ATOM   2552 O  O     . GLN B 1 150 ? 15.250 13.102  9.916   1.00 25.11 ? 150 GLN B O     1 
ATOM   2553 C  CB    . GLN B 1 150 ? 14.054 14.401  7.570   1.00 29.59 ? 150 GLN B CB    1 
ATOM   2554 C  CG    . GLN B 1 150 ? 14.802 13.231  6.875   1.00 40.21 ? 150 GLN B CG    1 
ATOM   2555 C  CD    . GLN B 1 150 ? 15.826 13.635  5.825   1.00 47.90 ? 150 GLN B CD    1 
ATOM   2556 O  OE1   . GLN B 1 150 ? 17.028 13.365  5.989   1.00 41.80 ? 150 GLN B OE1   1 
ATOM   2557 N  NE2   . GLN B 1 150 ? 15.363 14.248  4.734   1.00 45.24 ? 150 GLN B NE2   1 
ATOM   2558 N  N     . GLY B 1 151 ? 13.659 11.557  9.448   1.00 23.43 ? 151 GLY B N     1 
ATOM   2559 C  CA    . GLY B 1 151 ? 14.455 10.421  9.879   1.00 21.50 ? 151 GLY B CA    1 
ATOM   2560 C  C     . GLY B 1 151 ? 14.594 10.205  11.376  1.00 24.92 ? 151 GLY B C     1 
ATOM   2561 O  O     . GLY B 1 151 ? 15.224 9.216   11.779  1.00 24.67 ? 151 GLY B O     1 
ATOM   2562 N  N     . VAL B 1 152 ? 14.053 11.095  12.214  1.00 24.25 ? 152 VAL B N     1 
ATOM   2563 C  CA    . VAL B 1 152 ? 14.284 11.017  13.663  1.00 24.51 ? 152 VAL B CA    1 
ATOM   2564 C  C     . VAL B 1 152 ? 13.694 9.730   14.247  1.00 28.63 ? 152 VAL B C     1 
ATOM   2565 O  O     . VAL B 1 152 ? 14.404 8.914   14.874  1.00 21.25 ? 152 VAL B O     1 
ATOM   2566 C  CB    . VAL B 1 152 ? 13.731 12.274  14.357  1.00 26.53 ? 152 VAL B CB    1 
ATOM   2567 C  CG1   . VAL B 1 152 ? 13.845 12.151  15.873  1.00 26.01 ? 152 VAL B CG1   1 
ATOM   2568 C  CG2   . VAL B 1 152 ? 14.494 13.510  13.876  1.00 25.06 ? 152 VAL B CG2   1 
ATOM   2569 N  N     . ASP B 1 153 ? 12.374 9.545   14.067  1.00 25.07 ? 153 ASP B N     1 
ATOM   2570 C  CA    . ASP B 1 153 ? 11.721 8.319   14.520  1.00 25.45 ? 153 ASP B CA    1 
ATOM   2571 C  C     . ASP B 1 153 ? 12.456 7.096   13.994  1.00 25.64 ? 153 ASP B C     1 
ATOM   2572 O  O     . ASP B 1 153 ? 12.691 6.139   14.737  1.00 26.03 ? 153 ASP B O     1 
ATOM   2573 C  CB    . ASP B 1 153 ? 10.254 8.271   14.064  1.00 29.10 ? 153 ASP B CB    1 
ATOM   2574 C  CG    . ASP B 1 153 ? 9.371  9.295   14.752  1.00 37.19 ? 153 ASP B CG    1 
ATOM   2575 O  OD1   . ASP B 1 153 ? 9.747  9.826   15.816  1.00 39.59 ? 153 ASP B OD1   1 
ATOM   2576 O  OD2   . ASP B 1 153 ? 8.279  9.580   14.208  1.00 45.34 ? 153 ASP B OD2   1 
ATOM   2577 N  N     . ASP B 1 154 ? 12.823 7.118   12.707  1.00 24.89 ? 154 ASP B N     1 
ATOM   2578 C  CA    . ASP B 1 154 ? 13.478 5.970   12.081  1.00 26.11 ? 154 ASP B CA    1 
ATOM   2579 C  C     . ASP B 1 154 ? 14.792 5.633   12.767  1.00 26.70 ? 154 ASP B C     1 
ATOM   2580 O  O     . ASP B 1 154 ? 15.085 4.460   13.018  1.00 24.21 ? 154 ASP B O     1 
ATOM   2581 C  CB    . ASP B 1 154 ? 13.737 6.228   10.600  1.00 29.64 ? 154 ASP B CB    1 
ATOM   2582 C  CG    . ASP B 1 154 ? 12.468 6.244   9.773   1.00 42.71 ? 154 ASP B CG    1 
ATOM   2583 O  OD1   . ASP B 1 154 ? 11.482 5.586   10.177  1.00 40.92 ? 154 ASP B OD1   1 
ATOM   2584 O  OD2   . ASP B 1 154 ? 12.472 6.908   8.711   1.00 44.24 ? 154 ASP B OD2   1 
ATOM   2585 N  N     . ALA B 1 155 ? 15.624 6.641   13.033  1.00 23.57 ? 155 ALA B N     1 
ATOM   2586 C  CA    . ALA B 1 155 ? 16.894 6.357   13.691  1.00 19.74 ? 155 ALA B CA    1 
ATOM   2587 C  C     . ALA B 1 155 ? 16.656 5.670   15.034  1.00 21.49 ? 155 ALA B C     1 
ATOM   2588 O  O     . ALA B 1 155 ? 17.230 4.600   15.317  1.00 22.68 ? 155 ALA B O     1 
ATOM   2589 C  CB    . ALA B 1 155 ? 17.703 7.652   13.850  1.00 23.72 ? 155 ALA B CB    1 
ATOM   2590 N  N     . PHE B 1 156 ? 15.787 6.250   15.875  1.00 20.58 ? 156 PHE B N     1 
ATOM   2591 C  CA    . PHE B 1 156 ? 15.613 5.655   17.206  1.00 20.46 ? 156 PHE B CA    1 
ATOM   2592 C  C     . PHE B 1 156 ? 14.952 4.280   17.140  1.00 20.79 ? 156 PHE B C     1 
ATOM   2593 O  O     . PHE B 1 156 ? 15.331 3.363   17.883  1.00 19.21 ? 156 PHE B O     1 
ATOM   2594 C  CB    . PHE B 1 156 ? 14.814 6.588   18.115  1.00 21.04 ? 156 PHE B CB    1 
ATOM   2595 C  CG    . PHE B 1 156 ? 15.640 7.699   18.691  1.00 18.94 ? 156 PHE B CG    1 
ATOM   2596 C  CD1   . PHE B 1 156 ? 16.398 7.495   19.839  1.00 24.54 ? 156 PHE B CD1   1 
ATOM   2597 C  CD2   . PHE B 1 156 ? 15.684 8.926   18.070  1.00 20.37 ? 156 PHE B CD2   1 
ATOM   2598 C  CE1   . PHE B 1 156 ? 17.176 8.521   20.371  1.00 21.72 ? 156 PHE B CE1   1 
ATOM   2599 C  CE2   . PHE B 1 156 ? 16.458 9.962   18.595  1.00 21.88 ? 156 PHE B CE2   1 
ATOM   2600 C  CZ    . PHE B 1 156 ? 17.207 9.747   19.742  1.00 20.19 ? 156 PHE B CZ    1 
ATOM   2601 N  N     . TYR B 1 157 ? 13.939 4.117   16.285  1.00 21.47 ? 157 TYR B N     1 
ATOM   2602 C  CA    . TYR B 1 157 ? 13.239 2.835   16.234  1.00 22.76 ? 157 TYR B CA    1 
ATOM   2603 C  C     . TYR B 1 157 ? 14.108 1.750   15.617  1.00 23.49 ? 157 TYR B C     1 
ATOM   2604 O  O     . TYR B 1 157 ? 14.010 0.579   16.006  1.00 23.19 ? 157 TYR B O     1 
ATOM   2605 C  CB    . TYR B 1 157 ? 11.931 2.960   15.461  1.00 23.85 ? 157 TYR B CB    1 
ATOM   2606 C  CG    . TYR B 1 157 ? 10.910 3.875   16.107  1.00 29.44 ? 157 TYR B CG    1 
ATOM   2607 C  CD1   . TYR B 1 157 ? 9.720  4.174   15.452  1.00 37.39 ? 157 TYR B CD1   1 
ATOM   2608 C  CD2   . TYR B 1 157 ? 11.136 4.450   17.353  1.00 32.37 ? 157 TYR B CD2   1 
ATOM   2609 C  CE1   . TYR B 1 157 ? 8.781  5.013   16.030  1.00 34.99 ? 157 TYR B CE1   1 
ATOM   2610 C  CE2   . TYR B 1 157 ? 10.205 5.298   17.933  1.00 34.62 ? 157 TYR B CE2   1 
ATOM   2611 C  CZ    . TYR B 1 157 ? 9.032  5.574   17.264  1.00 39.17 ? 157 TYR B CZ    1 
ATOM   2612 O  OH    . TYR B 1 157 ? 8.088  6.414   17.830  1.00 49.16 ? 157 TYR B OH    1 
ATOM   2613 N  N     . THR B 1 158 ? 14.941 2.106   14.631  1.00 19.60 ? 158 THR B N     1 
ATOM   2614 C  CA    . THR B 1 158 ? 15.879 1.136   14.083  1.00 20.51 ? 158 THR B CA    1 
ATOM   2615 C  C     . THR B 1 158 ? 16.819 0.638   15.172  1.00 25.19 ? 158 THR B C     1 
ATOM   2616 O  O     . THR B 1 158 ? 17.118 -0.562  15.244  1.00 22.27 ? 158 THR B O     1 
ATOM   2617 C  CB    . THR B 1 158 ? 16.664 1.767   12.925  1.00 21.61 ? 158 THR B CB    1 
ATOM   2618 O  OG1   . THR B 1 158 ? 15.762 2.173   11.878  1.00 23.30 ? 158 THR B OG1   1 
ATOM   2619 C  CG2   . THR B 1 158 ? 17.683 0.775   12.355  1.00 25.74 ? 158 THR B CG2   1 
ATOM   2620 N  N     . LEU B 1 159 ? 17.275 1.546   16.056  1.00 20.04 ? 159 LEU B N     1 
ATOM   2621 C  CA    . LEU B 1 159 ? 18.120 1.107   17.177  1.00 17.72 ? 159 LEU B CA    1 
ATOM   2622 C  C     . LEU B 1 159 ? 17.373 0.156   18.118  1.00 20.30 ? 159 LEU B C     1 
ATOM   2623 O  O     . LEU B 1 159 ? 17.927 -0.863  18.569  1.00 20.76 ? 159 LEU B O     1 
ATOM   2624 C  CB    . LEU B 1 159 ? 18.644 2.332   17.951  1.00 20.11 ? 159 LEU B CB    1 
ATOM   2625 C  CG    . LEU B 1 159 ? 19.612 2.031   19.111  1.00 21.00 ? 159 LEU B CG    1 
ATOM   2626 C  CD1   . LEU B 1 159 ? 20.813 1.211   18.582  1.00 20.46 ? 159 LEU B CD1   1 
ATOM   2627 C  CD2   . LEU B 1 159 ? 20.062 3.315   19.801  1.00 19.41 ? 159 LEU B CD2   1 
ATOM   2628 N  N     . VAL B 1 160 ? 16.121 0.477   18.443  1.00 18.50 ? 160 VAL B N     1 
ATOM   2629 C  CA    . VAL B 1 160 ? 15.315 -0.437  19.262  1.00 21.21 ? 160 VAL B CA    1 
ATOM   2630 C  C     . VAL B 1 160 ? 15.233 -1.819  18.606  1.00 22.52 ? 160 VAL B C     1 
ATOM   2631 O  O     . VAL B 1 160 ? 15.393 -2.861  19.263  1.00 23.30 ? 160 VAL B O     1 
ATOM   2632 C  CB    . VAL B 1 160 ? 13.914 0.155   19.506  1.00 21.83 ? 160 VAL B CB    1 
ATOM   2633 C  CG1   . VAL B 1 160 ? 13.038 -0.879  20.225  1.00 25.77 ? 160 VAL B CG1   1 
ATOM   2634 C  CG2   . VAL B 1 160 ? 14.019 1.412   20.351  1.00 21.79 ? 160 VAL B CG2   1 
ATOM   2635 N  N     . ARG B 1 161 ? 14.968 -1.851  17.303  1.00 23.12 ? 161 ARG B N     1 
ATOM   2636 C  CA    . ARG B 1 161 ? 14.869 -3.137  16.614  1.00 25.35 ? 161 ARG B CA    1 
ATOM   2637 C  C     . ARG B 1 161 ? 16.198 -3.896  16.636  1.00 25.82 ? 161 ARG B C     1 
ATOM   2638 O  O     . ARG B 1 161 ? 16.214 -5.134  16.736  1.00 31.75 ? 161 ARG B O     1 
ATOM   2639 C  CB    . ARG B 1 161 ? 14.375 -2.926  15.187  1.00 26.11 ? 161 ARG B CB    1 
ATOM   2640 C  CG    . ARG B 1 161 ? 12.909 -2.524  15.120  1.00 24.34 ? 161 ARG B CG    1 
ATOM   2641 C  CD    . ARG B 1 161 ? 12.534 -1.929  13.774  1.00 29.38 ? 161 ARG B CD    1 
ATOM   2642 N  NE    . ARG B 1 161 ? 11.135 -1.511  13.788  1.00 29.40 ? 161 ARG B NE    1 
ATOM   2643 C  CZ    . ARG B 1 161 ? 10.684 -0.398  13.229  1.00 31.71 ? 161 ARG B CZ    1 
ATOM   2644 N  NH1   . ARG B 1 161 ? 11.499 0.452   12.627  1.00 32.52 ? 161 ARG B NH1   1 
ATOM   2645 N  NH2   . ARG B 1 161 ? 9.387  -0.114  13.304  1.00 32.60 ? 161 ARG B NH2   1 
ATOM   2646 N  N     . GLU B 1 162 ? 17.325 -3.180  16.531  1.00 25.57 ? 162 GLU B N     1 
ATOM   2647 C  CA    . GLU B 1 162 ? 18.630 -3.842  16.645  1.00 25.42 ? 162 GLU B CA    1 
ATOM   2648 C  C     . GLU B 1 162 ? 18.811 -4.461  18.029  1.00 25.46 ? 162 GLU B C     1 
ATOM   2649 O  O     . GLU B 1 162 ? 19.359 -5.566  18.165  1.00 30.48 ? 162 GLU B O     1 
ATOM   2650 C  CB    . GLU B 1 162 ? 19.769 -2.852  16.354  1.00 28.19 ? 162 GLU B CB    1 
ATOM   2651 C  CG    . GLU B 1 162 ? 19.821 -2.331  14.915  1.00 28.05 ? 162 GLU B CG    1 
ATOM   2652 C  CD    . GLU B 1 162 ? 20.288 -3.388  13.933  1.00 30.66 ? 162 GLU B CD    1 
ATOM   2653 O  OE1   . GLU B 1 162 ? 21.470 -3.783  13.995  1.00 33.20 ? 162 GLU B OE1   1 
ATOM   2654 O  OE2   . GLU B 1 162 ? 19.455 -3.865  13.132  1.00 33.08 ? 162 GLU B OE2   1 
ATOM   2655 N  N     . ILE B 1 163 ? 18.372 -3.758  19.074  1.00 23.83 ? 163 ILE B N     1 
ATOM   2656 C  CA    . ILE B 1 163 ? 18.471 -4.328  20.420  1.00 24.79 ? 163 ILE B CA    1 
ATOM   2657 C  C     . ILE B 1 163 ? 17.630 -5.592  20.525  1.00 30.77 ? 163 ILE B C     1 
ATOM   2658 O  O     . ILE B 1 163 ? 18.059 -6.598  21.107  1.00 31.13 ? 163 ILE B O     1 
ATOM   2659 C  CB    . ILE B 1 163 ? 18.062 -3.300  21.484  1.00 24.48 ? 163 ILE B CB    1 
ATOM   2660 C  CG1   . ILE B 1 163 ? 19.018 -2.108  21.469  1.00 22.51 ? 163 ILE B CG1   1 
ATOM   2661 C  CG2   . ILE B 1 163 ? 18.102 -3.933  22.867  1.00 26.31 ? 163 ILE B CG2   1 
ATOM   2662 C  CD1   . ILE B 1 163 ? 18.503 -0.955  22.272  1.00 24.46 ? 163 ILE B CD1   1 
ATOM   2663 N  N     . ARG B 1 164 ? 16.412 -5.560  19.985  1.00 28.65 ? 164 ARG B N     1 
ATOM   2664 C  CA    . ARG B 1 164 ? 15.606 -6.780  20.001  1.00 36.91 ? 164 ARG B CA    1 
ATOM   2665 C  C     . ARG B 1 164 ? 16.338 -7.930  19.330  1.00 40.54 ? 164 ARG B C     1 
ATOM   2666 O  O     . ARG B 1 164 ? 16.371 -9.048  19.857  1.00 47.10 ? 164 ARG B O     1 
ATOM   2667 C  CB    . ARG B 1 164 ? 14.272 -6.573  19.312  1.00 34.34 ? 164 ARG B CB    1 
ATOM   2668 C  CG    . ARG B 1 164 ? 13.340 -5.678  20.000  1.00 36.16 ? 164 ARG B CG    1 
ATOM   2669 C  CD    . ARG B 1 164 ? 12.039 -5.870  19.273  1.00 43.22 ? 164 ARG B CD    1 
ATOM   2670 N  NE    . ARG B 1 164 ? 11.029 -4.922  19.699  1.00 44.44 ? 164 ARG B NE    1 
ATOM   2671 C  CZ    . ARG B 1 164 ? 10.276 -4.241  18.850  1.00 41.26 ? 164 ARG B CZ    1 
ATOM   2672 N  NH1   . ARG B 1 164 ? 10.419 -4.374  17.537  1.00 39.63 ? 164 ARG B NH1   1 
ATOM   2673 N  NH2   . ARG B 1 164 ? 9.371  -3.396  19.328  1.00 37.37 ? 164 ARG B NH2   1 
ATOM   2674 N  N     . LYS B 1 165 ? 16.884 -7.688  18.133  1.00 40.17 ? 165 LYS B N     1 
ATOM   2675 C  CA    . LYS B 1 165 ? 17.669 -8.717  17.450  1.00 45.59 ? 165 LYS B CA    1 
ATOM   2676 C  C     . LYS B 1 165 ? 18.774 -9.264  18.352  1.00 48.18 ? 165 LYS B C     1 
ATOM   2677 O  O     . LYS B 1 165 ? 18.950 -10.484 18.467  1.00 54.98 ? 165 LYS B O     1 
ATOM   2678 C  CB    . LYS B 1 165 ? 18.269 -8.162  16.155  1.00 42.45 ? 165 LYS B CB    1 
ATOM   2679 C  CG    . LYS B 1 165 ? 17.337 -8.195  14.952  1.00 50.06 ? 165 LYS B CG    1 
ATOM   2680 C  CD    . LYS B 1 165 ? 18.119 -8.088  13.642  1.00 53.28 ? 165 LYS B CD    1 
ATOM   2681 C  CE    . LYS B 1 165 ? 17.436 -7.145  12.648  1.00 56.90 ? 165 LYS B CE    1 
ATOM   2682 N  NZ    . LYS B 1 165 ? 17.269 -7.772  11.298  1.00 60.06 ? 165 LYS B NZ    1 
ATOM   2683 N  N     . HIS B 1 166 ? 19.544 -8.368  18.984  1.00 46.04 ? 166 HIS B N     1 
ATOM   2684 C  CA    . HIS B 1 166 ? 20.688 -8.786  19.799  1.00 48.42 ? 166 HIS B CA    1 
ATOM   2685 C  C     . HIS B 1 166 ? 20.249 -9.628  20.990  1.00 53.00 ? 166 HIS B C     1 
ATOM   2686 O  O     . HIS B 1 166 ? 20.924 -10.596 21.360  1.00 55.69 ? 166 HIS B O     1 
ATOM   2687 C  CB    . HIS B 1 166 ? 21.469 -7.558  20.282  1.00 47.73 ? 166 HIS B CB    1 
ATOM   2688 C  CG    . HIS B 1 166 ? 22.429 -7.839  21.403  1.00 52.23 ? 166 HIS B CG    1 
ATOM   2689 N  ND1   . HIS B 1 166 ? 23.721 -8.270  21.180  1.00 56.96 ? 166 HIS B ND1   1 
ATOM   2690 C  CD2   . HIS B 1 166 ? 22.300 -7.723  22.748  1.00 56.28 ? 166 HIS B CD2   1 
ATOM   2691 C  CE1   . HIS B 1 166 ? 24.339 -8.427  22.338  1.00 60.28 ? 166 HIS B CE1   1 
ATOM   2692 N  NE2   . HIS B 1 166 ? 23.499 -8.102  23.306  1.00 62.41 ? 166 HIS B NE2   1 
ATOM   2693 N  N     . LYS B 1 167 ? 19.114 -9.275  21.599  1.00 52.07 ? 167 LYS B N     1 
ATOM   2694 C  CA    . LYS B 1 167 ? 18.552 -10.075 22.681  1.00 55.42 ? 167 LYS B CA    1 
ATOM   2695 C  C     . LYS B 1 167 ? 18.086 -11.434 22.180  1.00 61.01 ? 167 LYS B C     1 
ATOM   2696 O  O     . LYS B 1 167 ? 17.838 -12.333 22.992  1.00 67.26 ? 167 LYS B O     1 
ATOM   2697 C  CB    . LYS B 1 167 ? 17.395 -9.322  23.347  1.00 53.99 ? 167 LYS B CB    1 
ATOM   2698 C  CG    . LYS B 1 167 ? 17.834 -8.116  24.180  1.00 52.70 ? 167 LYS B CG    1 
ATOM   2699 C  CD    . LYS B 1 167 ? 16.650 -7.235  24.598  1.00 56.42 ? 167 LYS B CD    1 
ATOM   2700 C  CE    . LYS B 1 167 ? 17.070 -6.195  25.646  1.00 59.58 ? 167 LYS B CE    1 
ATOM   2701 N  NZ    . LYS B 1 167 ? 15.925 -5.393  26.198  1.00 57.54 ? 167 LYS B NZ    1 
ATOM   2702 N  N     . GLU B 1 168 ? 17.940 -11.579 20.857  1.00 63.59 ? 168 GLU B N     1 
ATOM   2703 C  CA    . GLU B 1 168 ? 17.488 -12.806 20.191  1.00 68.25 ? 168 GLU B CA    1 
ATOM   2704 C  C     . GLU B 1 168 ? 16.026 -13.094 20.530  1.00 70.58 ? 168 GLU B C     1 
ATOM   2705 O  O     . GLU B 1 168 ? 15.662 -14.195 20.951  1.00 75.98 ? 168 GLU B O     1 
ATOM   2706 C  CB    . GLU B 1 168 ? 18.386 -14.002 20.528  1.00 65.16 ? 168 GLU B CB    1 
ATOM   2707 C  CG    . GLU B 1 168 ? 19.843 -13.813 20.135  1.00 68.17 ? 168 GLU B CG    1 
ATOM   2708 C  CD    . GLU B 1 168 ? 20.695 -15.006 20.517  1.00 75.35 ? 168 GLU B CD    1 
ATOM   2709 O  OE1   . GLU B 1 168 ? 20.120 -16.024 20.962  1.00 73.94 ? 168 GLU B OE1   1 
ATOM   2710 O  OE2   . GLU B 1 168 ? 21.934 -14.925 20.372  1.00 78.53 ? 168 GLU B OE2   1 
ATOM   2711 N  N     . LYS B 1 169 ? 15.190 -12.081 20.318  1.00 62.88 ? 169 LYS B N     1 
ATOM   2712 C  CA    . LYS B 1 169 ? 13.759 -12.145 20.566  1.00 63.37 ? 169 LYS B CA    1 
ATOM   2713 C  C     . LYS B 1 169 ? 13.034 -11.608 19.324  1.00 60.75 ? 169 LYS B C     1 
ATOM   2714 O  O     . LYS B 1 169 ? 12.362 -10.573 19.349  1.00 59.62 ? 169 LYS B O     1 
ATOM   2715 C  CB    . LYS B 1 169 ? 13.387 -11.369 21.840  1.00 64.62 ? 169 LYS B CB    1 
ATOM   2716 C  CG    . LYS B 1 169 ? 13.807 -9.897  21.850  1.00 61.61 ? 169 LYS B CG    1 
ATOM   2717 C  CD    . LYS B 1 169 ? 13.640 -9.259  23.224  1.00 59.65 ? 169 LYS B CD    1 
ATOM   2718 C  CE    . LYS B 1 169 ? 12.269 -8.612  23.371  1.00 62.82 ? 169 LYS B CE    1 
ATOM   2719 N  NZ    . LYS B 1 169 ? 12.099 -7.953  24.698  1.00 60.00 ? 169 LYS B NZ    1 
HETATM 2720 P  PB    . GDP C 2 .   ? 9.234  9.647   -14.149 1.00 16.65 ? 201 GDP A PB    1 
HETATM 2721 O  O1B   . GDP C 2 .   ? 7.947  9.009   -14.638 1.00 17.21 ? 201 GDP A O1B   1 
HETATM 2722 O  O2B   . GDP C 2 .   ? 10.044 8.629   -13.376 1.00 15.26 ? 201 GDP A O2B   1 
HETATM 2723 O  O3B   . GDP C 2 .   ? 10.022 10.377  -15.213 1.00 17.14 ? 201 GDP A O3B   1 
HETATM 2724 O  O3A   . GDP C 2 .   ? 8.857  10.726  -13.023 1.00 16.18 ? 201 GDP A O3A   1 
HETATM 2725 P  PA    . GDP C 2 .   ? 8.641  12.304  -13.155 1.00 17.50 ? 201 GDP A PA    1 
HETATM 2726 O  O1A   . GDP C 2 .   ? 7.731  12.682  -14.294 1.00 20.90 ? 201 GDP A O1A   1 
HETATM 2727 O  O2A   . GDP C 2 .   ? 9.942  13.059  -13.124 1.00 16.79 ? 201 GDP A O2A   1 
HETATM 2728 O  "O5'" . GDP C 2 .   ? 7.824  12.520  -11.744 1.00 18.25 ? 201 GDP A "O5'" 1 
HETATM 2729 C  "C5'" . GDP C 2 .   ? 6.482  12.050  -11.460 1.00 19.69 ? 201 GDP A "C5'" 1 
HETATM 2730 C  "C4'" . GDP C 2 .   ? 5.759  13.031  -10.518 1.00 19.21 ? 201 GDP A "C4'" 1 
HETATM 2731 O  "O4'" . GDP C 2 .   ? 6.562  13.110  -9.339  1.00 19.00 ? 201 GDP A "O4'" 1 
HETATM 2732 C  "C3'" . GDP C 2 .   ? 5.679  14.461  -11.032 1.00 22.60 ? 201 GDP A "C3'" 1 
HETATM 2733 O  "O3'" . GDP C 2 .   ? 4.475  15.147  -10.610 1.00 23.65 ? 201 GDP A "O3'" 1 
HETATM 2734 C  "C2'" . GDP C 2 .   ? 6.874  15.121  -10.363 1.00 22.46 ? 201 GDP A "C2'" 1 
HETATM 2735 O  "O2'" . GDP C 2 .   ? 6.724  16.548  -10.269 1.00 31.74 ? 201 GDP A "O2'" 1 
HETATM 2736 C  "C1'" . GDP C 2 .   ? 6.914  14.456  -9.005  1.00 22.58 ? 201 GDP A "C1'" 1 
HETATM 2737 N  N9    . GDP C 2 .   ? 8.275  14.426  -8.442  1.00 21.12 ? 201 GDP A N9    1 
HETATM 2738 C  C8    . GDP C 2 .   ? 9.402  13.970  -9.044  1.00 22.15 ? 201 GDP A C8    1 
HETATM 2739 N  N7    . GDP C 2 .   ? 10.462 14.020  -8.197  1.00 18.41 ? 201 GDP A N7    1 
HETATM 2740 C  C5    . GDP C 2 .   ? 9.984  14.436  -6.982  1.00 21.53 ? 201 GDP A C5    1 
HETATM 2741 C  C6    . GDP C 2 .   ? 10.546 14.693  -5.637  1.00 23.06 ? 201 GDP A C6    1 
HETATM 2742 O  O6    . GDP C 2 .   ? 11.766 14.515  -5.383  1.00 22.69 ? 201 GDP A O6    1 
HETATM 2743 N  N1    . GDP C 2 .   ? 9.701  15.118  -4.670  1.00 24.37 ? 201 GDP A N1    1 
HETATM 2744 C  C2    . GDP C 2 .   ? 8.384  15.309  -4.893  1.00 27.92 ? 201 GDP A C2    1 
HETATM 2745 N  N2    . GDP C 2 .   ? 7.612  15.740  -3.863  1.00 30.56 ? 201 GDP A N2    1 
HETATM 2746 N  N3    . GDP C 2 .   ? 7.803  15.111  -6.110  1.00 25.35 ? 201 GDP A N3    1 
HETATM 2747 C  C4    . GDP C 2 .   ? 8.551  14.671  -7.158  1.00 22.66 ? 201 GDP A C4    1 
HETATM 2748 MG MG    . MG  D 3 .   ? 9.852  10.663  -17.217 1.00 16.62 ? 202 MG  A MG    1 
HETATM 2749 C  C22   . 6IC E 4 .   ? 17.746 -2.828  -18.960 1.00 24.70 ? 203 6IC A C22   1 
HETATM 2750 C  C21   . 6IC E 4 .   ? 17.517 -3.581  -20.117 1.00 24.70 ? 203 6IC A C21   1 
HETATM 2751 C  C23   . 6IC E 4 .   ? 16.712 -2.034  -18.451 1.00 24.70 ? 203 6IC A C23   1 
HETATM 2752 C  C20   . 6IC E 4 .   ? 15.269 -2.782  -20.266 1.00 24.70 ? 203 6IC A C20   1 
HETATM 2753 C  C24   . 6IC E 4 .   ? 15.526 -2.055  -19.129 1.00 24.70 ? 203 6IC A C24   1 
HETATM 2754 C  C19   . 6IC E 4 .   ? 16.269 -3.562  -20.773 1.00 24.70 ? 203 6IC A C19   1 
HETATM 2755 C  C17   . 6IC E 4 .   ? 14.753 -4.222  -22.533 1.00 24.70 ? 203 6IC A C17   1 
HETATM 2756 C  C14   . 6IC E 4 .   ? 7.638  1.669   -16.564 1.00 24.70 ? 203 6IC A C14   1 
HETATM 2757 C  C13   . 6IC E 4 .   ? 6.788  0.451   -18.554 1.00 24.70 ? 203 6IC A C13   1 
HETATM 2758 C  C18   . 6IC E 4 .   ? 15.999 -4.300  -21.935 1.00 24.70 ? 203 6IC A C18   1 
HETATM 2759 C  C01   . 6IC E 4 .   ? 10.272 -1.263  -19.353 1.00 24.70 ? 203 6IC A C01   1 
HETATM 2760 C  C02   . 6IC E 4 .   ? 10.895 -2.285  -18.765 1.00 24.70 ? 203 6IC A C02   1 
HETATM 2761 C  C03   . 6IC E 4 .   ? 9.036  -2.339  -17.221 1.00 24.70 ? 203 6IC A C03   1 
HETATM 2762 C  C04   . 6IC E 4 .   ? 9.055  -0.776  -18.898 1.00 24.70 ? 203 6IC A C04   1 
HETATM 2763 C  C05   . 6IC E 4 .   ? 10.813 -0.623  -20.488 1.00 24.70 ? 203 6IC A C05   1 
HETATM 2764 C  C06   . 6IC E 4 .   ? 12.655 -2.000  -20.487 1.00 24.70 ? 203 6IC A C06   1 
HETATM 2765 C  C07   . 6IC E 4 .   ? 12.147 -2.681  -19.342 1.00 24.70 ? 203 6IC A C07   1 
HETATM 2766 C  C08   . 6IC E 4 .   ? 13.989 -2.714  -20.833 1.00 24.70 ? 203 6IC A C08   1 
HETATM 2767 C  C09   . 6IC E 4 .   ? 7.425  -3.005  -15.841 1.00 24.70 ? 203 6IC A C09   1 
HETATM 2768 C  C10   . 6IC E 4 .   ? 9.063  1.733   -19.383 1.00 24.70 ? 203 6IC A C10   1 
HETATM 2769 C  C11   . 6IC E 4 .   ? 8.502  2.788   -18.453 1.00 24.70 ? 203 6IC A C11   1 
HETATM 2770 C  C12   . 6IC E 4 .   ? 6.685  1.782   -17.831 1.00 24.70 ? 203 6IC A C12   1 
HETATM 2771 C  C15   . 6IC E 4 .   ? 8.849  2.296   -17.013 1.00 24.70 ? 203 6IC A C15   1 
HETATM 2772 C  C16   . 6IC E 4 .   ? 13.723 -3.429  -21.994 1.00 24.70 ? 203 6IC A C16   1 
HETATM 2773 C  C25   . 6IC E 4 .   ? 6.827  -4.011  -14.816 1.00 24.70 ? 203 6IC A C25   1 
HETATM 2774 C  C26   . 6IC E 4 .   ? 7.583  -4.149  -13.727 1.00 24.70 ? 203 6IC A C26   1 
HETATM 2775 C  C27   . 6IC E 4 .   ? 7.798  -5.614  -13.576 1.00 25.81 ? 203 6IC A C27   1 
HETATM 2776 C  C28   . 6IC E 4 .   ? 7.696  -6.110  -14.963 1.00 24.70 ? 203 6IC A C28   1 
HETATM 2777 C  C29   . 6IC E 4 .   ? 5.069  -5.589  -15.761 1.00 24.82 ? 203 6IC A C29   1 
HETATM 2778 C  C30   . 6IC E 4 .   ? 4.338  -4.392  -15.376 1.00 28.81 ? 203 6IC A C30   1 
HETATM 2779 C  C31   . 6IC E 4 .   ? 5.381  -3.561  -14.370 1.00 24.70 ? 203 6IC A C31   1 
HETATM 2780 C  C32   . 6IC E 4 .   ? 14.619 -1.122  -18.386 1.00 24.70 ? 203 6IC A C32   1 
HETATM 2781 C  C33   . 6IC E 4 .   ? 13.843 -0.396  -17.844 1.00 26.16 ? 203 6IC A C33   1 
HETATM 2782 F  F01   . 6IC E 4 .   ? 12.654 -3.717  -18.580 1.00 24.70 ? 203 6IC A F01   1 
HETATM 2783 F  F02   . 6IC E 4 .   ? 6.739  -6.138  -12.856 1.00 24.70 ? 203 6IC A F02   1 
HETATM 2784 F  F23   . 6IC E 4 .   ? 16.993 -1.324  -17.319 1.00 24.70 ? 203 6IC A F23   1 
HETATM 2785 N  N01   . 6IC E 4 .   ? 10.257 -2.842  -17.640 1.00 24.70 ? 203 6IC A N01   1 
HETATM 2786 N  N02   . 6IC E 4 .   ? 8.463  -1.304  -17.865 1.00 24.70 ? 203 6IC A N02   1 
HETATM 2787 N  N03   . 6IC E 4 .   ? 11.959 -1.008  -21.007 1.00 24.70 ? 203 6IC A N03   1 
HETATM 2788 N  N04   . 6IC E 4 .   ? 8.206  0.338   -19.345 1.00 24.70 ? 203 6IC A N04   1 
HETATM 2789 N  N05   . 6IC E 4 .   ? 7.158  2.802   -18.495 1.00 24.70 ? 203 6IC A N05   1 
HETATM 2790 N  N06   . 6IC E 4 .   ? 6.640  -5.403  -15.436 1.00 24.70 ? 203 6IC A N06   1 
HETATM 2791 O  O01   . 6IC E 4 .   ? 8.799  -3.235  -16.159 1.00 24.70 ? 203 6IC A O01   1 
HETATM 2792 O  O02   . 6IC E 4 .   ? 14.475 -4.925  -23.700 1.00 24.70 ? 203 6IC A O02   1 
HETATM 2793 P  PB    . GDP F 2 .   ? 24.729 18.591  20.853  1.00 17.43 ? 201 GDP B PB    1 
HETATM 2794 O  O1B   . GDP F 2 .   ? 25.862 19.422  21.372  1.00 17.79 ? 201 GDP B O1B   1 
HETATM 2795 O  O2B   . GDP F 2 .   ? 25.188 17.389  20.102  1.00 15.91 ? 201 GDP B O2B   1 
HETATM 2796 O  O3B   . GDP F 2 .   ? 23.711 18.277  21.888  1.00 18.38 ? 201 GDP B O3B   1 
HETATM 2797 O  O3A   . GDP F 2 .   ? 23.955 19.493  19.782  1.00 16.65 ? 201 GDP B O3A   1 
HETATM 2798 P  PA    . GDP F 2 .   ? 22.654 20.405  19.919  1.00 20.13 ? 201 GDP B PA    1 
HETATM 2799 O  O1A   . GDP F 2 .   ? 22.821 21.325  21.074  1.00 22.84 ? 201 GDP B O1A   1 
HETATM 2800 O  O2A   . GDP F 2 .   ? 21.435 19.558  19.869  1.00 18.20 ? 201 GDP B O2A   1 
HETATM 2801 O  "O5'" . GDP F 2 .   ? 22.749 21.232  18.561  1.00 28.47 ? 201 GDP B "O5'" 1 
HETATM 2802 C  "C5'" . GDP F 2 .   ? 23.917 22.013  18.251  1.00 28.56 ? 201 GDP B "C5'" 1 
HETATM 2803 C  "C4'" . GDP F 2 .   ? 23.517 23.110  17.297  1.00 26.58 ? 201 GDP B "C4'" 1 
HETATM 2804 O  "O4'" . GDP F 2 .   ? 23.117 22.516  16.036  1.00 25.34 ? 201 GDP B "O4'" 1 
HETATM 2805 C  "C3'" . GDP F 2 .   ? 22.326 23.970  17.741  1.00 29.91 ? 201 GDP B "C3'" 1 
HETATM 2806 O  "O3'" . GDP F 2 .   ? 22.468 25.323  17.334  1.00 30.75 ? 201 GDP B "O3'" 1 
HETATM 2807 C  "C2'" . GDP F 2 .   ? 21.149 23.302  17.028  1.00 29.86 ? 201 GDP B "C2'" 1 
HETATM 2808 O  "O2'" . GDP F 2 .   ? 20.073 24.182  16.802  1.00 33.77 ? 201 GDP B "O2'" 1 
HETATM 2809 C  "C1'" . GDP F 2 .   ? 21.793 22.871  15.721  1.00 27.73 ? 201 GDP B "C1'" 1 
HETATM 2810 N  N9    . GDP F 2 .   ? 21.149 21.717  15.114  1.00 25.18 ? 201 GDP B N9    1 
HETATM 2811 C  C8    . GDP F 2 .   ? 20.902 20.508  15.709  1.00 22.64 ? 201 GDP B C8    1 
HETATM 2812 N  N7    . GDP F 2 .   ? 20.327 19.647  14.909  1.00 21.37 ? 201 GDP B N7    1 
HETATM 2813 C  C5    . GDP F 2 .   ? 20.189 20.333  13.711  1.00 22.24 ? 201 GDP B C5    1 
HETATM 2814 C  C6    . GDP F 2 .   ? 19.635 19.913  12.478  1.00 24.10 ? 201 GDP B C6    1 
HETATM 2815 O  O6    . GDP F 2 .   ? 19.143 18.816  12.194  1.00 24.43 ? 201 GDP B O6    1 
HETATM 2816 N  N1    . GDP F 2 .   ? 19.702 20.925  11.522  1.00 23.24 ? 201 GDP B N1    1 
HETATM 2817 C  C2    . GDP F 2 .   ? 20.230 22.174  11.722  1.00 31.74 ? 201 GDP B C2    1 
HETATM 2818 N  N2    . GDP F 2 .   ? 20.201 23.010  10.677  1.00 29.83 ? 201 GDP B N2    1 
HETATM 2819 N  N3    . GDP F 2 .   ? 20.749 22.575  12.879  1.00 25.31 ? 201 GDP B N3    1 
HETATM 2820 C  C4    . GDP F 2 .   ? 20.697 21.608  13.823  1.00 24.84 ? 201 GDP B C4    1 
HETATM 2821 MG MG    . MG  G 3 .   ? 23.536 18.548  23.970  1.00 17.09 ? 202 MG  B MG    1 
HETATM 2822 C  C22   . 6IC H 4 .   ? 31.249 4.982   25.718  1.00 24.70 ? 203 6IC B C22   1 
HETATM 2823 C  C21   . 6IC H 4 .   ? 32.025 4.802   26.872  1.00 24.70 ? 203 6IC B C21   1 
HETATM 2824 C  C23   . 6IC H 4 .   ? 31.083 6.277   25.210  1.00 24.70 ? 203 6IC B C23   1 
HETATM 2825 C  C20   . 6IC H 4 .   ? 32.467 7.138   27.026  1.00 24.70 ? 203 6IC B C20   1 
HETATM 2826 C  C24   . 6IC H 4 .   ? 31.702 7.278   25.893  1.00 24.70 ? 203 6IC B C24   1 
HETATM 2827 C  C19   . 6IC H 4 .   ? 32.646 5.884   27.534  1.00 24.70 ? 203 6IC B C19   1 
HETATM 2828 C  C17   . 6IC H 4 .   ? 33.988 6.877   29.289  1.00 24.70 ? 203 6IC B C17   1 
HETATM 2829 C  C14   . 6IC H 4 .   ? 32.446 16.001  23.344  1.00 24.70 ? 203 6IC B C14   1 
HETATM 2830 C  C13   . 6IC H 4 .   ? 33.862 16.089  25.352  1.00 24.70 ? 203 6IC B C13   1 
HETATM 2831 C  C18   . 6IC H 4 .   ? 33.429 5.753   28.697  1.00 24.70 ? 203 6IC B C18   1 
HETATM 2832 C  C01   . 6IC H 4 .   ? 33.631 12.225  26.087  1.00 24.70 ? 203 6IC B C01   1 
HETATM 2833 C  C02   . 6IC H 4 .   ? 34.211 11.184  25.493  1.00 24.70 ? 203 6IC B C02   1 
HETATM 2834 C  C03   . 6IC H 4 .   ? 35.177 12.779  23.955  1.00 24.70 ? 203 6IC B C03   1 
HETATM 2835 C  C04   . 6IC H 4 .   ? 33.807 13.516  25.637  1.00 24.70 ? 203 6IC B C04   1 
HETATM 2836 C  C05   . 6IC H 4 .   ? 32.813 12.074  27.226  1.00 24.70 ? 203 6IC B C05   1 
HETATM 2837 C  C06   . 6IC H 4 .   ? 33.096 9.792   27.217  1.00 24.70 ? 203 6IC B C06   1 
HETATM 2838 C  C07   . 6IC H 4 .   ? 33.935 9.901   26.066  1.00 24.70 ? 203 6IC B C07   1 
HETATM 2839 C  C08   . 6IC H 4 .   ? 33.050 8.283   27.579  1.00 24.70 ? 203 6IC B C08   1 
HETATM 2840 C  C09   . 6IC H 4 .   ? 36.577 13.835  22.571  1.00 24.70 ? 203 6IC B C09   1 
HETATM 2841 C  C10   . 6IC H 4 .   ? 31.606 14.729  26.112  1.00 24.70 ? 203 6IC B C10   1 
HETATM 2842 C  C11   . 6IC H 4 .   ? 30.990 15.742  25.176  1.00 24.70 ? 203 6IC B C11   1 
HETATM 2843 C  C12   . 6IC H 4 .   ? 32.768 16.859  24.639  1.00 24.70 ? 203 6IC B C12   1 
HETATM 2844 C  C15   . 6IC H 4 .   ? 31.305 15.225  23.739  1.00 24.70 ? 203 6IC B C15   1 
HETATM 2845 C  C16   . 6IC H 4 .   ? 33.807 8.163   28.743  1.00 24.70 ? 203 6IC B C16   1 
HETATM 2846 C  C25   . 6IC H 4 .   ? 37.752 13.838  21.553  1.00 24.70 ? 203 6IC B C25   1 
HETATM 2847 C  C26   . 6IC H 4 .   ? 37.523 13.098  20.460  1.00 24.70 ? 203 6IC B C26   1 
HETATM 2848 C  C27   . 6IC H 4 .   ? 38.686 12.169  20.345  1.00 25.53 ? 203 6IC B C27   1 
HETATM 2849 C  C28   . 6IC H 4 .   ? 39.169 12.062  21.738  1.00 24.70 ? 203 6IC B C28   1 
HETATM 2850 C  C29   . 6IC H 4 .   ? 39.953 14.621  22.548  1.00 25.86 ? 203 6IC B C29   1 
HETATM 2851 C  C30   . 6IC H 4 .   ? 39.275 15.839  22.133  1.00 27.77 ? 203 6IC B C30   1 
HETATM 2852 C  C31   . 6IC H 4 .   ? 38.062 15.322  21.106  1.00 24.70 ? 203 6IC B C31   1 
HETATM 2853 C  C32   . 6IC H 4 .   ? 31.333 8.518   25.142  1.00 24.70 ? 203 6IC B C32   1 
HETATM 2854 C  C33   . 6IC H 4 .   ? 31.078 9.542   24.588  1.00 26.86 ? 203 6IC B C33   1 
HETATM 2855 F  F01   . 6IC H 4 .   ? 34.596 8.965   25.287  1.00 24.70 ? 203 6IC B F01   1 
HETATM 2856 F  F02   . 6IC H 4 .   ? 39.660 12.790  19.577  1.00 24.70 ? 203 6IC B F02   1 
HETATM 2857 F  F23   . 6IC H 4 .   ? 30.322 6.423   24.087  1.00 24.70 ? 203 6IC B F23   1 
HETATM 2858 N  N01   . 6IC H 4 .   ? 35.012 11.470  24.368  1.00 24.70 ? 203 6IC B N01   1 
HETATM 2859 N  N02   . 6IC H 4 .   ? 34.556 13.779  24.608  1.00 24.70 ? 203 6IC B N02   1 
HETATM 2860 N  N03   . 6IC H 4 .   ? 32.581 10.887  27.737  1.00 24.70 ? 203 6IC B N03   1 
HETATM 2861 N  N04   . 6IC H 4 .   ? 33.247 14.790  26.117  1.00 24.70 ? 203 6IC B N04   1 
HETATM 2862 N  N05   . 6IC H 4 .   ? 31.624 16.926  25.264  1.00 24.70 ? 203 6IC B N05   1 
HETATM 2863 N  N06   . 6IC H 4 .   ? 39.048 13.330  22.197  1.00 24.70 ? 203 6IC B N06   1 
HETATM 2864 O  O01   . 6IC H 4 .   ? 36.067 12.540  22.884  1.00 24.70 ? 203 6IC B O01   1 
HETATM 2865 O  O02   . 6IC H 4 .   ? 34.756 6.771   30.455  1.00 24.70 ? 203 6IC B O02   1 
HETATM 2866 O  O     . HOH I 5 .   ? 33.355 5.864   -20.162 1.00 42.75 ? 301 HOH A O     1 
HETATM 2867 O  O     . HOH I 5 .   ? 10.087 1.144   -25.983 1.00 54.55 ? 302 HOH A O     1 
HETATM 2868 O  O     . HOH I 5 .   ? 5.461  -0.235  -10.805 1.00 40.73 ? 303 HOH A O     1 
HETATM 2869 O  O     . HOH I 5 .   ? 31.688 5.377   -6.082  1.00 43.23 ? 304 HOH A O     1 
HETATM 2870 O  O     . HOH I 5 .   ? 16.541 -8.517  -5.624  1.00 37.83 ? 305 HOH A O     1 
HETATM 2871 O  O     . HOH I 5 .   ? 8.577  15.872  -13.655 1.00 26.14 ? 306 HOH A O     1 
HETATM 2872 O  O     . HOH I 5 .   ? 29.858 -1.451  -20.368 1.00 42.61 ? 307 HOH A O     1 
HETATM 2873 O  O     . HOH I 5 .   ? 28.138 0.151   -8.394  1.00 33.68 ? 308 HOH A O     1 
HETATM 2874 O  O     . HOH I 5 .   ? 13.119 12.233  -21.053 1.00 22.86 ? 309 HOH A O     1 
HETATM 2875 O  O     . HOH I 5 .   ? 18.609 -8.581  -8.858  1.00 43.09 ? 310 HOH A O     1 
HETATM 2876 O  O     . HOH I 5 .   ? 7.301  18.239  -0.419  1.00 40.37 ? 311 HOH A O     1 
HETATM 2877 O  O     . HOH I 5 .   ? 2.738  2.295   -15.822 1.00 40.37 ? 312 HOH A O     1 
HETATM 2878 O  O     . HOH I 5 .   ? 5.304  13.576  -14.875 1.00 21.67 ? 313 HOH A O     1 
HETATM 2879 O  O     . HOH I 5 .   ? 3.453  -5.410  -11.840 1.00 32.28 ? 314 HOH A O     1 
HETATM 2880 O  O     . HOH I 5 .   ? 6.118  -6.697  -5.760  1.00 36.21 ? 315 HOH A O     1 
HETATM 2881 O  O     . HOH I 5 .   ? 11.392 9.333   -17.617 1.00 16.22 ? 316 HOH A O     1 
HETATM 2882 O  O     . HOH I 5 .   ? 8.370  12.181  -16.849 1.00 15.07 ? 317 HOH A O     1 
HETATM 2883 O  O     . HOH I 5 .   ? 10.220 1.756   -23.342 1.00 43.27 ? 318 HOH A O     1 
HETATM 2884 O  O     . HOH I 5 .   ? 7.881  -0.655  -13.229 1.00 18.08 ? 319 HOH A O     1 
HETATM 2885 O  O     . HOH I 5 .   ? 13.298 15.670  -24.771 1.00 40.18 ? 320 HOH A O     1 
HETATM 2886 O  O     . HOH I 5 .   ? 21.448 -1.809  7.464   1.00 29.27 ? 321 HOH A O     1 
HETATM 2887 O  O     . HOH I 5 .   ? 5.537  8.512   -5.776  1.00 30.88 ? 322 HOH A O     1 
HETATM 2888 O  O     . HOH I 5 .   ? 14.468 7.686   6.952   1.00 45.50 ? 323 HOH A O     1 
HETATM 2889 O  O     . HOH I 5 .   ? 8.499  9.035   -17.329 1.00 15.41 ? 324 HOH A O     1 
HETATM 2890 O  O     . HOH I 5 .   ? 6.229  6.318   -19.675 1.00 26.35 ? 325 HOH A O     1 
HETATM 2891 O  O     . HOH I 5 .   ? 11.347 1.686   -9.654  1.00 18.54 ? 326 HOH A O     1 
HETATM 2892 O  O     . HOH I 5 .   ? 4.177  13.427  -26.040 1.00 39.96 ? 327 HOH A O     1 
HETATM 2893 O  O     . HOH I 5 .   ? 9.048  6.150   -16.993 1.00 19.00 ? 328 HOH A O     1 
HETATM 2894 O  O     . HOH I 5 .   ? 14.930 -9.604  -25.449 1.00 39.32 ? 329 HOH A O     1 
HETATM 2895 O  O     . HOH I 5 .   ? 15.493 -5.200  1.965   1.00 39.01 ? 330 HOH A O     1 
HETATM 2896 O  O     . HOH I 5 .   ? 10.844 -7.174  -9.166  1.00 28.60 ? 331 HOH A O     1 
HETATM 2897 O  O     . HOH I 5 .   ? 19.313 -11.488 -15.197 1.00 32.26 ? 332 HOH A O     1 
HETATM 2898 O  O     . HOH I 5 .   ? 22.562 17.961  -5.160  1.00 32.83 ? 333 HOH A O     1 
HETATM 2899 O  O     . HOH I 5 .   ? 13.565 18.804  -12.511 1.00 25.34 ? 334 HOH A O     1 
HETATM 2900 O  O     . HOH I 5 .   ? 9.478  11.049  -19.324 1.00 17.28 ? 335 HOH A O     1 
HETATM 2901 O  O     . HOH I 5 .   ? 30.511 -0.140  -17.645 1.00 37.32 ? 336 HOH A O     1 
HETATM 2902 O  O     . HOH I 5 .   ? 12.429 2.535   -16.818 1.00 17.99 ? 337 HOH A O     1 
HETATM 2903 O  O     . HOH I 5 .   ? 5.392  10.206  -14.626 1.00 25.95 ? 338 HOH A O     1 
HETATM 2904 O  O     . HOH I 5 .   ? 21.248 12.415  0.397   1.00 40.51 ? 339 HOH A O     1 
HETATM 2905 O  O     . HOH I 5 .   ? 2.095  6.164   -0.196  1.00 35.19 ? 340 HOH A O     1 
HETATM 2906 O  O     . HOH I 5 .   ? 37.680 21.755  -18.670 0.33 36.08 ? 341 HOH A O     1 
HETATM 2907 O  O     . HOH I 5 .   ? 34.532 16.889  -8.154  1.00 42.95 ? 342 HOH A O     1 
HETATM 2908 O  O     . HOH I 5 .   ? 6.814  18.003  -20.674 1.00 31.55 ? 343 HOH A O     1 
HETATM 2909 O  O     . HOH I 5 .   ? 13.533 -8.870  -31.059 1.00 36.50 ? 344 HOH A O     1 
HETATM 2910 O  O     . HOH I 5 .   ? 8.026  -7.383  -25.625 1.00 28.95 ? 345 HOH A O     1 
HETATM 2911 O  O     . HOH I 5 .   ? 3.682  -0.737  -21.125 1.00 36.09 ? 346 HOH A O     1 
HETATM 2912 O  O     . HOH I 5 .   ? 5.425  13.201  -6.038  1.00 33.04 ? 347 HOH A O     1 
HETATM 2913 O  O     . HOH I 5 .   ? 3.257  2.287   -1.160  1.00 30.50 ? 348 HOH A O     1 
HETATM 2914 O  O     . HOH I 5 .   ? 18.806 -12.182 -23.514 1.00 40.08 ? 349 HOH A O     1 
HETATM 2915 O  O     . HOH I 5 .   ? 3.349  14.152  -8.106  1.00 33.27 ? 350 HOH A O     1 
HETATM 2916 O  O     . HOH I 5 .   ? 4.072  -2.000  -18.142 1.00 35.59 ? 351 HOH A O     1 
HETATM 2917 O  O     . HOH I 5 .   ? 30.782 9.504   -4.510  1.00 32.25 ? 352 HOH A O     1 
HETATM 2918 O  O     . HOH I 5 .   ? 3.121  12.224  -13.250 1.00 29.50 ? 353 HOH A O     1 
HETATM 2919 O  O     . HOH I 5 .   ? 13.714 24.862  -9.098  1.00 42.88 ? 354 HOH A O     1 
HETATM 2920 O  O     . HOH I 5 .   ? 22.375 6.558   2.300   1.00 46.30 ? 355 HOH A O     1 
HETATM 2921 O  O     . HOH I 5 .   ? 2.823  0.606   -3.756  1.00 37.79 ? 356 HOH A O     1 
HETATM 2922 O  O     . HOH I 5 .   ? 15.005 3.056   8.556   1.00 44.27 ? 357 HOH A O     1 
HETATM 2923 O  O     . HOH I 5 .   ? 9.705  9.311   -26.532 1.00 36.42 ? 358 HOH A O     1 
HETATM 2924 O  O     . HOH I 5 .   ? 7.389  3.432   -26.312 1.00 45.92 ? 359 HOH A O     1 
HETATM 2925 O  O     . HOH I 5 .   ? 21.129 9.243   1.736   1.00 36.90 ? 360 HOH A O     1 
HETATM 2926 O  O     . HOH I 5 .   ? 3.665  10.980  -4.976  1.00 46.19 ? 361 HOH A O     1 
HETATM 2927 O  O     . HOH I 5 .   ? 14.436 -6.062  -32.808 1.00 35.64 ? 362 HOH A O     1 
HETATM 2928 O  O     . HOH I 5 .   ? 4.455  1.862   -9.065  1.00 34.45 ? 363 HOH A O     1 
HETATM 2929 O  O     . HOH I 5 .   ? 5.564  1.279   -13.617 1.00 21.81 ? 364 HOH A O     1 
HETATM 2930 O  O     . HOH I 5 .   ? 23.115 -3.386  9.371   1.00 33.66 ? 365 HOH A O     1 
HETATM 2931 O  O     . HOH I 5 .   ? 37.680 21.755  -21.382 0.33 34.09 ? 366 HOH A O     1 
HETATM 2932 O  O     . HOH I 5 .   ? 4.130  -0.255  -16.025 1.00 38.22 ? 367 HOH A O     1 
HETATM 2933 O  O     . HOH J 5 .   ? 21.102 9.299   33.863  1.00 42.75 ? 301 HOH B O     1 
HETATM 2934 O  O     . HOH J 5 .   ? 13.322 5.113   7.290   1.00 47.37 ? 302 HOH B O     1 
HETATM 2935 O  O     . HOH J 5 .   ? 18.034 24.285  7.104   1.00 41.05 ? 303 HOH B O     1 
HETATM 2936 O  O     . HOH J 5 .   ? 17.152 -2.985  12.857  1.00 43.74 ? 304 HOH B O     1 
HETATM 2937 O  O     . HOH J 5 .   ? 35.259 16.911  17.434  1.00 38.07 ? 305 HOH B O     1 
HETATM 2938 O  O     . HOH J 5 .   ? 35.946 1.321   15.606  1.00 40.30 ? 306 HOH B O     1 
HETATM 2939 O  O     . HOH J 5 .   ? 32.435 20.010  25.809  1.00 45.11 ? 307 HOH B O     1 
HETATM 2940 O  O     . HOH J 5 .   ? 30.163 -2.281  15.129  1.00 52.30 ? 308 HOH B O     1 
HETATM 2941 O  O     . HOH J 5 .   ? 28.483 2.200   -0.711  1.00 30.78 ? 309 HOH B O     1 
HETATM 2942 O  O     . HOH J 5 .   ? 20.514 16.532  27.799  1.00 22.32 ? 310 HOH B O     1 
HETATM 2943 O  O     . HOH J 5 .   ? 26.667 12.581  -0.500  1.00 48.67 ? 311 HOH B O     1 
HETATM 2944 O  O     . HOH J 5 .   ? 23.865 -4.882  27.123  1.00 44.19 ? 312 HOH B O     1 
HETATM 2945 O  O     . HOH J 5 .   ? 28.019 -3.406  16.600  1.00 44.09 ? 313 HOH B O     1 
HETATM 2946 O  O     . HOH J 5 .   ? 23.916 16.597  24.414  1.00 15.99 ? 314 HOH B O     1 
HETATM 2947 O  O     . HOH J 5 .   ? 36.794 2.835   12.370  1.00 37.90 ? 315 HOH B O     1 
HETATM 2948 O  O     . HOH J 5 .   ? 23.634 -2.732  15.176  1.00 32.35 ? 316 HOH B O     1 
HETATM 2949 O  O     . HOH J 5 .   ? 23.693 13.031  -0.199  1.00 46.58 ? 317 HOH B O     1 
HETATM 2950 O  O     . HOH J 5 .   ? 31.086 13.732  30.057  1.00 38.27 ? 318 HOH B O     1 
HETATM 2951 O  O     . HOH J 5 .   ? 30.496 12.867  16.412  1.00 19.42 ? 319 HOH B O     1 
HETATM 2952 O  O     . HOH J 5 .   ? 27.835 17.101  23.806  1.00 18.74 ? 320 HOH B O     1 
HETATM 2953 O  O     . HOH J 5 .   ? 25.596 19.004  24.024  1.00 15.22 ? 321 HOH B O     1 
HETATM 2954 O  O     . HOH J 5 .   ? 38.428 8.780   15.905  1.00 25.99 ? 322 HOH B O     1 
HETATM 2955 O  O     . HOH J 5 .   ? 34.223 14.636  19.887  1.00 18.55 ? 323 HOH B O     1 
HETATM 2956 O  O     . HOH J 5 .   ? 27.483 21.128  12.530  1.00 30.07 ? 324 HOH B O     1 
HETATM 2957 O  O     . HOH J 5 .   ? 29.133 19.543  26.439  1.00 25.47 ? 325 HOH B O     1 
HETATM 2958 O  O     . HOH J 5 .   ? 24.057 24.891  32.742  1.00 36.66 ? 326 HOH B O     1 
HETATM 2959 O  O     . HOH J 5 .   ? 37.932 -0.685  21.945  1.00 33.53 ? 327 HOH B O     1 
HETATM 2960 O  O     . HOH J 5 .   ? 40.425 13.078  12.535  1.00 37.88 ? 328 HOH B O     1 
HETATM 2961 O  O     . HOH J 5 .   ? 40.772 16.272  18.618  1.00 33.83 ? 329 HOH B O     1 
HETATM 2962 O  O     . HOH J 5 .   ? 16.230 9.664   6.443   1.00 38.56 ? 330 HOH B O     1 
HETATM 2963 O  O     . HOH J 5 .   ? 2.678  -4.355  24.406  1.00 40.76 ? 331 HOH B O     1 
HETATM 2964 O  O     . HOH J 5 .   ? 38.620 4.126   32.171  1.00 38.72 ? 332 HOH B O     1 
HETATM 2965 O  O     . HOH J 5 .   ? 23.406 19.098  26.021  1.00 16.66 ? 333 HOH B O     1 
HETATM 2966 O  O     . HOH J 5 .   ? 31.126 23.018  6.914   1.00 36.08 ? 334 HOH B O     1 
HETATM 2967 O  O     . HOH J 5 .   ? 34.436 20.723  22.557  1.00 39.67 ? 335 HOH B O     1 
HETATM 2968 O  O     . HOH J 5 .   ? 22.737 -4.704  24.397  1.00 38.69 ? 336 HOH B O     1 
HETATM 2969 O  O     . HOH J 5 .   ? 14.482 19.436  19.226  1.00 24.04 ? 337 HOH B O     1 
HETATM 2970 O  O     . HOH J 5 .   ? 23.261 24.033  21.689  1.00 24.33 ? 338 HOH B O     1 
HETATM 2971 O  O     . HOH J 5 .   ? 23.610 23.670  12.895  1.00 34.59 ? 339 HOH B O     1 
HETATM 2972 O  O     . HOH J 5 .   ? 26.167 22.220  21.415  1.00 24.10 ? 340 HOH B O     1 
HETATM 2973 O  O     . HOH J 5 .   ? 0.000  0.000   25.275  0.33 41.68 ? 341 HOH B O     1 
HETATM 2974 O  O     . HOH J 5 .   ? 18.712 24.976  27.375  1.00 32.04 ? 342 HOH B O     1 
HETATM 2975 O  O     . HOH J 5 .   ? 10.773 11.165  11.940  1.00 36.38 ? 343 HOH B O     1 
HETATM 2976 O  O     . HOH J 5 .   ? 9.448  22.360  15.883  1.00 42.92 ? 344 HOH B O     1 
HETATM 2977 O  O     . HOH J 5 .   ? 29.260 12.254  23.489  1.00 16.42 ? 345 HOH B O     1 
HETATM 2978 O  O     . HOH J 5 .   ? 19.617 22.252  20.399  1.00 27.08 ? 346 HOH B O     1 
HETATM 2979 O  O     . HOH J 5 .   ? 11.643 8.799   10.690  1.00 37.07 ? 347 HOH B O     1 
HETATM 2980 O  O     . HOH J 5 .   ? 40.059 11.097  32.395  1.00 29.35 ? 348 HOH B O     1 
HETATM 2981 O  O     . HOH J 5 .   ? 38.666 5.609   37.737  1.00 35.10 ? 349 HOH B O     1 
HETATM 2982 O  O     . HOH J 5 .   ? 35.416 7.695   11.819  1.00 46.44 ? 350 HOH B O     1 
HETATM 2983 O  O     . HOH J 5 .   ? 28.094 5.151   37.332  1.00 26.59 ? 351 HOH B O     1 
HETATM 2984 O  O     . HOH J 5 .   ? 13.998 -0.041  11.245  1.00 33.16 ? 352 HOH B O     1 
HETATM 2985 O  O     . HOH J 5 .   ? 36.471 18.173  27.768  1.00 36.52 ? 353 HOH B O     1 
HETATM 2986 O  O     . HOH J 5 .   ? 13.927 -6.721  15.776  1.00 43.51 ? 354 HOH B O     1 
HETATM 2987 O  O     . HOH J 5 .   ? 2.748  -0.995  16.438  1.00 36.21 ? 355 HOH B O     1 
HETATM 2988 O  O     . HOH J 5 .   ? 33.916 20.110  7.871   1.00 34.67 ? 356 HOH B O     1 
HETATM 2989 O  O     . HOH J 5 .   ? 27.550 10.095  -1.906  1.00 42.32 ? 357 HOH B O     1 
HETATM 2990 O  O     . HOH J 5 .   ? 38.852 -0.708  30.320  1.00 47.81 ? 358 HOH B O     1 
HETATM 2991 O  O     . HOH J 5 .   ? 23.870 25.956  14.734  1.00 35.76 ? 359 HOH B O     1 
HETATM 2992 O  O     . HOH J 5 .   ? 31.171 17.232  32.936  1.00 44.10 ? 360 HOH B O     1 
HETATM 2993 O  O     . HOH J 5 .   ? 27.051 -4.729  29.619  1.00 46.04 ? 361 HOH B O     1 
HETATM 2994 O  O     . HOH J 5 .   ? 36.022 19.543  10.383  1.00 33.92 ? 362 HOH B O     1 
HETATM 2995 O  O     . HOH J 5 .   ? 11.726 12.429  30.902  1.00 37.85 ? 363 HOH B O     1 
HETATM 2996 O  O     . HOH J 5 .   ? 25.541 25.253  19.934  1.00 31.63 ? 364 HOH B O     1 
HETATM 2997 O  O     . HOH J 5 .   ? 24.713 18.012  33.349  1.00 38.66 ? 365 HOH B O     1 
HETATM 2998 O  O     . HOH J 5 .   ? 19.193 8.128   5.004   1.00 37.61 ? 366 HOH B O     1 
HETATM 2999 O  O     . HOH J 5 .   ? 24.189 1.612   3.377   1.00 16.03 ? 367 HOH B O     1 
HETATM 3000 O  O     . HOH J 5 .   ? 28.875 0.224   -2.517  1.00 35.98 ? 368 HOH B O     1 
HETATM 3001 O  O     . HOH J 5 .   ? 33.691 18.715  15.887  1.00 33.99 ? 369 HOH B O     1 
HETATM 3002 O  O     . HOH J 5 .   ? 35.737 6.295   39.582  1.00 38.01 ? 370 HOH B O     1 
HETATM 3003 O  O     . HOH J 5 .   ? 33.807 17.566  20.341  1.00 22.12 ? 371 HOH B O     1 
HETATM 3004 O  O     . HOH J 5 .   ? 26.318 24.183  11.747  1.00 49.76 ? 372 HOH B O     1 
HETATM 3005 O  O     . HOH J 5 .   ? 24.214 -6.343  17.259  1.00 45.57 ? 373 HOH B O     1 
HETATM 3006 O  O     . HOH J 5 .   ? 0.000  0.000   28.016  0.33 36.87 ? 374 HOH B O     1 
HETATM 3007 O  O     . HOH J 5 .   ? 37.432 5.852   10.858  1.00 39.86 ? 375 HOH B O     1 
# 
