data_9JPK
# 
_entry.id   9JPK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JPK         pdb_00009jpk 10.2210/pdb9jpk/pdb 
WWPDB D_1300051878 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JPK 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sunpengkai@sxtcm.edu.cn 
_pdbx_contact_author.name_first         Pengkai 
_pdbx_contact_author.name_last          Sun 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2478-9109 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sun, P.'  1 ? 
'Wang, B.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of DhdR inducer binding domain' 
_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 'Sun, P.'  1 ? 
primary 'Wang, B.' 2 ? 
# 
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 'Pyruvate dehydrogenase complex repressor' 25587.777 2   ? ? ? ? 
2 non-polymer syn 'ZINC ION'                                 65.409    2   ? ? ? ? 
3 water       nat water                                      18.015    115 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        DhdR 
# 
_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       
;MLSKSLTLTEQVARQIAGDIAEGVHSVGAKLPPGRVLAEQYGVSAAVIREATERLRAQGLIQSRQGSGSVVVSRTGAQGF
QVSAGLDDREQLASVYELRMELEGGAAALAARRRNATDLAAMAEALAALEANLDHPEQGVEHDIAFHVAIAAATHNRYYQ
DLLQYLNLQLRLAVSTARTNSRRQEGLTAVVHQEHVAVYDAILAGDPDRARLAATRHLQQAASRLRLDLLSPAARQTS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLSKSLTLTEQVARQIAGDIAEGVHSVGAKLPPGRVLAEQYGVSAAVIREATERLRAQGLIQSRQGSGSVVVSRTGAQGF
QVSAGLDDREQLASVYELRMELEGGAAALAARRRNATDLAAMAEALAALEANLDHPEQGVEHDIAFHVAIAAATHNRYYQ
DLLQYLNLQLRLAVSTARTNSRRQEGLTAVVHQEHVAVYDAILAGDPDRARLAATRHLQQAASRLRLDLLSPAARQTS
;
_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 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LEU n 
1 3   SER n 
1 4   LYS n 
1 5   SER n 
1 6   LEU n 
1 7   THR n 
1 8   LEU n 
1 9   THR n 
1 10  GLU n 
1 11  GLN n 
1 12  VAL n 
1 13  ALA n 
1 14  ARG n 
1 15  GLN n 
1 16  ILE n 
1 17  ALA n 
1 18  GLY n 
1 19  ASP n 
1 20  ILE n 
1 21  ALA n 
1 22  GLU n 
1 23  GLY n 
1 24  VAL n 
1 25  HIS n 
1 26  SER n 
1 27  VAL n 
1 28  GLY n 
1 29  ALA n 
1 30  LYS n 
1 31  LEU n 
1 32  PRO n 
1 33  PRO n 
1 34  GLY n 
1 35  ARG n 
1 36  VAL n 
1 37  LEU n 
1 38  ALA n 
1 39  GLU n 
1 40  GLN n 
1 41  TYR n 
1 42  GLY n 
1 43  VAL n 
1 44  SER n 
1 45  ALA n 
1 46  ALA n 
1 47  VAL n 
1 48  ILE n 
1 49  ARG n 
1 50  GLU n 
1 51  ALA n 
1 52  THR n 
1 53  GLU n 
1 54  ARG n 
1 55  LEU n 
1 56  ARG n 
1 57  ALA n 
1 58  GLN n 
1 59  GLY n 
1 60  LEU n 
1 61  ILE n 
1 62  GLN n 
1 63  SER n 
1 64  ARG n 
1 65  GLN n 
1 66  GLY n 
1 67  SER n 
1 68  GLY n 
1 69  SER n 
1 70  VAL n 
1 71  VAL n 
1 72  VAL n 
1 73  SER n 
1 74  ARG n 
1 75  THR n 
1 76  GLY n 
1 77  ALA n 
1 78  GLN n 
1 79  GLY n 
1 80  PHE n 
1 81  GLN n 
1 82  VAL n 
1 83  SER n 
1 84  ALA n 
1 85  GLY n 
1 86  LEU n 
1 87  ASP n 
1 88  ASP n 
1 89  ARG n 
1 90  GLU n 
1 91  GLN n 
1 92  LEU n 
1 93  ALA n 
1 94  SER n 
1 95  VAL n 
1 96  TYR n 
1 97  GLU n 
1 98  LEU n 
1 99  ARG n 
1 100 MET n 
1 101 GLU n 
1 102 LEU n 
1 103 GLU n 
1 104 GLY n 
1 105 GLY n 
1 106 ALA n 
1 107 ALA n 
1 108 ALA n 
1 109 LEU n 
1 110 ALA n 
1 111 ALA n 
1 112 ARG n 
1 113 ARG n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 THR n 
1 118 ASP n 
1 119 LEU n 
1 120 ALA n 
1 121 ALA n 
1 122 MET n 
1 123 ALA n 
1 124 GLU n 
1 125 ALA n 
1 126 LEU n 
1 127 ALA n 
1 128 ALA n 
1 129 LEU n 
1 130 GLU n 
1 131 ALA n 
1 132 ASN n 
1 133 LEU n 
1 134 ASP n 
1 135 HIS n 
1 136 PRO n 
1 137 GLU n 
1 138 GLN n 
1 139 GLY n 
1 140 VAL n 
1 141 GLU n 
1 142 HIS n 
1 143 ASP n 
1 144 ILE n 
1 145 ALA n 
1 146 PHE n 
1 147 HIS n 
1 148 VAL n 
1 149 ALA n 
1 150 ILE n 
1 151 ALA n 
1 152 ALA n 
1 153 ALA n 
1 154 THR n 
1 155 HIS n 
1 156 ASN n 
1 157 ARG n 
1 158 TYR n 
1 159 TYR n 
1 160 GLN n 
1 161 ASP n 
1 162 LEU n 
1 163 LEU n 
1 164 GLN n 
1 165 TYR n 
1 166 LEU n 
1 167 ASN n 
1 168 LEU n 
1 169 GLN n 
1 170 LEU n 
1 171 ARG n 
1 172 LEU n 
1 173 ALA n 
1 174 VAL n 
1 175 SER n 
1 176 THR n 
1 177 ALA n 
1 178 ARG n 
1 179 THR n 
1 180 ASN n 
1 181 SER n 
1 182 ARG n 
1 183 ARG n 
1 184 GLN n 
1 185 GLU n 
1 186 GLY n 
1 187 LEU n 
1 188 THR n 
1 189 ALA n 
1 190 VAL n 
1 191 VAL n 
1 192 HIS n 
1 193 GLN n 
1 194 GLU n 
1 195 HIS n 
1 196 VAL n 
1 197 ALA n 
1 198 VAL n 
1 199 TYR n 
1 200 ASP n 
1 201 ALA n 
1 202 ILE n 
1 203 LEU n 
1 204 ALA n 
1 205 GLY n 
1 206 ASP n 
1 207 PRO n 
1 208 ASP n 
1 209 ARG n 
1 210 ALA n 
1 211 ARG n 
1 212 LEU n 
1 213 ALA n 
1 214 ALA n 
1 215 THR n 
1 216 ARG n 
1 217 HIS n 
1 218 LEU n 
1 219 GLN n 
1 220 GLN n 
1 221 ALA n 
1 222 ALA n 
1 223 SER n 
1 224 ARG n 
1 225 LEU n 
1 226 ARG n 
1 227 LEU n 
1 228 ASP n 
1 229 LEU n 
1 230 LEU n 
1 231 SER n 
1 232 PRO n 
1 233 ALA n 
1 234 ALA n 
1 235 ARG n 
1 236 GLN n 
1 237 THR n 
1 238 SER 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                   238 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FOC81_30220 
_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      'Achromobacter denitrificans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32002 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   THR 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   THR 9   9   ?   ?   ?   A . n 
A 1 10  GLU 10  10  ?   ?   ?   A . n 
A 1 11  GLN 11  11  ?   ?   ?   A . n 
A 1 12  VAL 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  ARG 14  14  ?   ?   ?   A . n 
A 1 15  GLN 15  15  ?   ?   ?   A . n 
A 1 16  ILE 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  ASP 19  19  ?   ?   ?   A . n 
A 1 20  ILE 20  20  ?   ?   ?   A . n 
A 1 21  ALA 21  21  ?   ?   ?   A . n 
A 1 22  GLU 22  22  ?   ?   ?   A . n 
A 1 23  GLY 23  23  ?   ?   ?   A . n 
A 1 24  VAL 24  24  ?   ?   ?   A . n 
A 1 25  HIS 25  25  ?   ?   ?   A . n 
A 1 26  SER 26  26  ?   ?   ?   A . n 
A 1 27  VAL 27  27  ?   ?   ?   A . n 
A 1 28  GLY 28  28  ?   ?   ?   A . n 
A 1 29  ALA 29  29  ?   ?   ?   A . n 
A 1 30  LYS 30  30  ?   ?   ?   A . n 
A 1 31  LEU 31  31  ?   ?   ?   A . n 
A 1 32  PRO 32  32  ?   ?   ?   A . n 
A 1 33  PRO 33  33  ?   ?   ?   A . n 
A 1 34  GLY 34  34  ?   ?   ?   A . n 
A 1 35  ARG 35  35  ?   ?   ?   A . n 
A 1 36  VAL 36  36  ?   ?   ?   A . n 
A 1 37  LEU 37  37  ?   ?   ?   A . n 
A 1 38  ALA 38  38  ?   ?   ?   A . n 
A 1 39  GLU 39  39  ?   ?   ?   A . n 
A 1 40  GLN 40  40  ?   ?   ?   A . n 
A 1 41  TYR 41  41  ?   ?   ?   A . n 
A 1 42  GLY 42  42  ?   ?   ?   A . n 
A 1 43  VAL 43  43  ?   ?   ?   A . n 
A 1 44  SER 44  44  ?   ?   ?   A . n 
A 1 45  ALA 45  45  ?   ?   ?   A . n 
A 1 46  ALA 46  46  ?   ?   ?   A . n 
A 1 47  VAL 47  47  ?   ?   ?   A . n 
A 1 48  ILE 48  48  ?   ?   ?   A . n 
A 1 49  ARG 49  49  ?   ?   ?   A . n 
A 1 50  GLU 50  50  ?   ?   ?   A . n 
A 1 51  ALA 51  51  ?   ?   ?   A . n 
A 1 52  THR 52  52  ?   ?   ?   A . n 
A 1 53  GLU 53  53  ?   ?   ?   A . n 
A 1 54  ARG 54  54  ?   ?   ?   A . n 
A 1 55  LEU 55  55  ?   ?   ?   A . n 
A 1 56  ARG 56  56  ?   ?   ?   A . n 
A 1 57  ALA 57  57  ?   ?   ?   A . n 
A 1 58  GLN 58  58  ?   ?   ?   A . n 
A 1 59  GLY 59  59  ?   ?   ?   A . n 
A 1 60  LEU 60  60  ?   ?   ?   A . n 
A 1 61  ILE 61  61  ?   ?   ?   A . n 
A 1 62  GLN 62  62  ?   ?   ?   A . n 
A 1 63  SER 63  63  ?   ?   ?   A . n 
A 1 64  ARG 64  64  ?   ?   ?   A . n 
A 1 65  GLN 65  65  ?   ?   ?   A . n 
A 1 66  GLY 66  66  ?   ?   ?   A . n 
A 1 67  SER 67  67  ?   ?   ?   A . n 
A 1 68  GLY 68  68  ?   ?   ?   A . n 
A 1 69  SER 69  69  ?   ?   ?   A . n 
A 1 70  VAL 70  70  ?   ?   ?   A . n 
A 1 71  VAL 71  71  ?   ?   ?   A . n 
A 1 72  VAL 72  72  ?   ?   ?   A . n 
A 1 73  SER 73  73  ?   ?   ?   A . n 
A 1 74  ARG 74  74  ?   ?   ?   A . n 
A 1 75  THR 75  75  ?   ?   ?   A . n 
A 1 76  GLY 76  76  ?   ?   ?   A . n 
A 1 77  ALA 77  77  ?   ?   ?   A . n 
A 1 78  GLN 78  78  ?   ?   ?   A . n 
A 1 79  GLY 79  79  ?   ?   ?   A . n 
A 1 80  PHE 80  80  ?   ?   ?   A . n 
A 1 81  GLN 81  81  ?   ?   ?   A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 TYR 158 158 158 TYR TYR A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 GLN 160 160 160 GLN GLN A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 HIS 195 195 195 HIS HIS A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 ALA 233 233 ?   ?   ?   A . n 
A 1 234 ALA 234 234 ?   ?   ?   A . n 
A 1 235 ARG 235 235 ?   ?   ?   A . n 
A 1 236 GLN 236 236 ?   ?   ?   A . n 
A 1 237 THR 237 237 ?   ?   ?   A . n 
A 1 238 SER 238 238 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LEU 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   ?   ?   ?   B . n 
B 1 7   THR 7   7   ?   ?   ?   B . n 
B 1 8   LEU 8   8   ?   ?   ?   B . n 
B 1 9   THR 9   9   ?   ?   ?   B . n 
B 1 10  GLU 10  10  ?   ?   ?   B . n 
B 1 11  GLN 11  11  ?   ?   ?   B . n 
B 1 12  VAL 12  12  ?   ?   ?   B . n 
B 1 13  ALA 13  13  ?   ?   ?   B . n 
B 1 14  ARG 14  14  ?   ?   ?   B . n 
B 1 15  GLN 15  15  ?   ?   ?   B . n 
B 1 16  ILE 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  GLY 18  18  ?   ?   ?   B . n 
B 1 19  ASP 19  19  ?   ?   ?   B . n 
B 1 20  ILE 20  20  ?   ?   ?   B . n 
B 1 21  ALA 21  21  ?   ?   ?   B . n 
B 1 22  GLU 22  22  ?   ?   ?   B . n 
B 1 23  GLY 23  23  ?   ?   ?   B . n 
B 1 24  VAL 24  24  ?   ?   ?   B . n 
B 1 25  HIS 25  25  ?   ?   ?   B . n 
B 1 26  SER 26  26  ?   ?   ?   B . n 
B 1 27  VAL 27  27  ?   ?   ?   B . n 
B 1 28  GLY 28  28  ?   ?   ?   B . n 
B 1 29  ALA 29  29  ?   ?   ?   B . n 
B 1 30  LYS 30  30  ?   ?   ?   B . n 
B 1 31  LEU 31  31  ?   ?   ?   B . n 
B 1 32  PRO 32  32  ?   ?   ?   B . n 
B 1 33  PRO 33  33  ?   ?   ?   B . n 
B 1 34  GLY 34  34  ?   ?   ?   B . n 
B 1 35  ARG 35  35  ?   ?   ?   B . n 
B 1 36  VAL 36  36  ?   ?   ?   B . n 
B 1 37  LEU 37  37  ?   ?   ?   B . n 
B 1 38  ALA 38  38  ?   ?   ?   B . n 
B 1 39  GLU 39  39  ?   ?   ?   B . n 
B 1 40  GLN 40  40  ?   ?   ?   B . n 
B 1 41  TYR 41  41  ?   ?   ?   B . n 
B 1 42  GLY 42  42  ?   ?   ?   B . n 
B 1 43  VAL 43  43  ?   ?   ?   B . n 
B 1 44  SER 44  44  ?   ?   ?   B . n 
B 1 45  ALA 45  45  ?   ?   ?   B . n 
B 1 46  ALA 46  46  ?   ?   ?   B . n 
B 1 47  VAL 47  47  ?   ?   ?   B . n 
B 1 48  ILE 48  48  ?   ?   ?   B . n 
B 1 49  ARG 49  49  ?   ?   ?   B . n 
B 1 50  GLU 50  50  ?   ?   ?   B . n 
B 1 51  ALA 51  51  ?   ?   ?   B . n 
B 1 52  THR 52  52  ?   ?   ?   B . n 
B 1 53  GLU 53  53  ?   ?   ?   B . n 
B 1 54  ARG 54  54  ?   ?   ?   B . n 
B 1 55  LEU 55  55  ?   ?   ?   B . n 
B 1 56  ARG 56  56  ?   ?   ?   B . n 
B 1 57  ALA 57  57  ?   ?   ?   B . n 
B 1 58  GLN 58  58  ?   ?   ?   B . n 
B 1 59  GLY 59  59  ?   ?   ?   B . n 
B 1 60  LEU 60  60  ?   ?   ?   B . n 
B 1 61  ILE 61  61  ?   ?   ?   B . n 
B 1 62  GLN 62  62  ?   ?   ?   B . n 
B 1 63  SER 63  63  ?   ?   ?   B . n 
B 1 64  ARG 64  64  ?   ?   ?   B . n 
B 1 65  GLN 65  65  ?   ?   ?   B . n 
B 1 66  GLY 66  66  ?   ?   ?   B . n 
B 1 67  SER 67  67  ?   ?   ?   B . n 
B 1 68  GLY 68  68  ?   ?   ?   B . n 
B 1 69  SER 69  69  ?   ?   ?   B . n 
B 1 70  VAL 70  70  ?   ?   ?   B . n 
B 1 71  VAL 71  71  ?   ?   ?   B . n 
B 1 72  VAL 72  72  ?   ?   ?   B . n 
B 1 73  SER 73  73  ?   ?   ?   B . n 
B 1 74  ARG 74  74  ?   ?   ?   B . n 
B 1 75  THR 75  75  ?   ?   ?   B . n 
B 1 76  GLY 76  76  ?   ?   ?   B . n 
B 1 77  ALA 77  77  ?   ?   ?   B . n 
B 1 78  GLN 78  78  ?   ?   ?   B . n 
B 1 79  GLY 79  79  ?   ?   ?   B . n 
B 1 80  PHE 80  80  ?   ?   ?   B . n 
B 1 81  GLN 81  81  ?   ?   ?   B . n 
B 1 82  VAL 82  82  ?   ?   ?   B . n 
B 1 83  SER 83  83  ?   ?   ?   B . n 
B 1 84  ALA 84  84  ?   ?   ?   B . n 
B 1 85  GLY 85  85  ?   ?   ?   B . n 
B 1 86  LEU 86  86  ?   ?   ?   B . n 
B 1 87  ASP 87  87  ?   ?   ?   B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLN 91  91  91  GLN GLN B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  ARG 99  99  99  ARG ARG B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 GLU 101 101 101 GLU GLU B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 THR 117 117 117 THR THR B . n 
B 1 118 ASP 118 118 118 ASP ASP B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 MET 122 122 122 MET MET B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 GLU 124 124 124 GLU GLU B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 ASN 132 132 132 ASN ASN B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 HIS 135 135 135 HIS HIS B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 HIS 142 142 142 HIS HIS B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 HIS 147 147 147 HIS HIS B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 HIS 155 155 155 HIS HIS B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 ARG 157 157 157 ARG ARG B . n 
B 1 158 TYR 158 158 158 TYR TYR B . n 
B 1 159 TYR 159 159 159 TYR TYR B . n 
B 1 160 GLN 160 160 160 GLN GLN B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 GLN 164 164 164 GLN GLN B . n 
B 1 165 TYR 165 165 165 TYR TYR B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 ARG 171 171 171 ARG ARG B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ALA 177 177 ?   ?   ?   B . n 
B 1 178 ARG 178 178 ?   ?   ?   B . n 
B 1 179 THR 179 179 ?   ?   ?   B . n 
B 1 180 ASN 180 180 ?   ?   ?   B . n 
B 1 181 SER 181 181 ?   ?   ?   B . n 
B 1 182 ARG 182 182 ?   ?   ?   B . n 
B 1 183 ARG 183 183 ?   ?   ?   B . n 
B 1 184 GLN 184 184 ?   ?   ?   B . n 
B 1 185 GLU 185 185 ?   ?   ?   B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 HIS 192 192 192 HIS HIS B . n 
B 1 193 GLN 193 193 193 GLN GLN B . n 
B 1 194 GLU 194 194 194 GLU GLU B . n 
B 1 195 HIS 195 195 195 HIS HIS B . n 
B 1 196 VAL 196 196 196 VAL VAL B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 TYR 199 199 199 TYR TYR B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 ALA 201 201 201 ALA ALA B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 ASP 206 206 206 ASP ASP B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ALA 213 213 213 ALA ALA B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 THR 215 215 215 THR THR B . n 
B 1 216 ARG 216 216 216 ARG ARG B . n 
B 1 217 HIS 217 217 217 HIS HIS B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 ARG 224 224 224 ARG ARG B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 PRO 232 232 ?   ?   ?   B . n 
B 1 233 ALA 233 233 ?   ?   ?   B . n 
B 1 234 ALA 234 234 ?   ?   ?   B . n 
B 1 235 ARG 235 235 ?   ?   ?   B . n 
B 1 236 GLN 236 236 ?   ?   ?   B . n 
B 1 237 THR 237 237 ?   ?   ?   B . n 
B 1 238 SER 238 238 ?   ?   ?   B . n 
# 
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 ZN  1  301 1   ZN  ZN  A . 
D 2 ZN  1  301 2   ZN  ZN  B . 
E 3 HOH 1  401 113 HOH HOH A . 
E 3 HOH 2  402 34  HOH HOH A . 
E 3 HOH 3  403 58  HOH HOH A . 
E 3 HOH 4  404 15  HOH HOH A . 
E 3 HOH 5  405 103 HOH HOH A . 
E 3 HOH 6  406 2   HOH HOH A . 
E 3 HOH 7  407 1   HOH HOH A . 
E 3 HOH 8  408 5   HOH HOH A . 
E 3 HOH 9  409 6   HOH HOH A . 
E 3 HOH 10 410 28  HOH HOH A . 
E 3 HOH 11 411 102 HOH HOH A . 
E 3 HOH 12 412 35  HOH HOH A . 
E 3 HOH 13 413 7   HOH HOH A . 
E 3 HOH 14 414 26  HOH HOH A . 
E 3 HOH 15 415 12  HOH HOH A . 
E 3 HOH 16 416 29  HOH HOH A . 
E 3 HOH 17 417 14  HOH HOH A . 
E 3 HOH 18 418 110 HOH HOH A . 
E 3 HOH 19 419 83  HOH HOH A . 
E 3 HOH 20 420 86  HOH HOH A . 
E 3 HOH 21 421 51  HOH HOH A . 
E 3 HOH 22 422 108 HOH HOH A . 
E 3 HOH 23 423 18  HOH HOH A . 
E 3 HOH 24 424 106 HOH HOH A . 
E 3 HOH 25 425 117 HOH HOH A . 
E 3 HOH 26 426 107 HOH HOH A . 
E 3 HOH 27 427 43  HOH HOH A . 
E 3 HOH 28 428 39  HOH HOH A . 
E 3 HOH 29 429 63  HOH HOH A . 
E 3 HOH 30 430 62  HOH HOH A . 
E 3 HOH 31 431 24  HOH HOH A . 
E 3 HOH 32 432 10  HOH HOH A . 
E 3 HOH 33 433 77  HOH HOH A . 
E 3 HOH 34 434 55  HOH HOH A . 
E 3 HOH 35 435 60  HOH HOH A . 
E 3 HOH 36 436 8   HOH HOH A . 
E 3 HOH 37 437 30  HOH HOH A . 
E 3 HOH 38 438 47  HOH HOH A . 
E 3 HOH 39 439 38  HOH HOH A . 
E 3 HOH 40 440 3   HOH HOH A . 
E 3 HOH 41 441 79  HOH HOH A . 
E 3 HOH 42 442 52  HOH HOH A . 
E 3 HOH 43 443 17  HOH HOH A . 
E 3 HOH 44 444 109 HOH HOH A . 
E 3 HOH 45 445 93  HOH HOH A . 
E 3 HOH 46 446 112 HOH HOH A . 
E 3 HOH 47 447 84  HOH HOH A . 
E 3 HOH 48 448 71  HOH HOH A . 
E 3 HOH 49 449 56  HOH HOH A . 
E 3 HOH 50 450 46  HOH HOH A . 
E 3 HOH 51 451 37  HOH HOH A . 
E 3 HOH 52 452 61  HOH HOH A . 
E 3 HOH 53 453 98  HOH HOH A . 
E 3 HOH 54 454 116 HOH HOH A . 
E 3 HOH 55 455 20  HOH HOH A . 
E 3 HOH 56 456 75  HOH HOH A . 
E 3 HOH 57 457 105 HOH HOH A . 
E 3 HOH 58 458 99  HOH HOH A . 
E 3 HOH 59 459 36  HOH HOH A . 
E 3 HOH 60 460 78  HOH HOH A . 
E 3 HOH 61 461 59  HOH HOH A . 
E 3 HOH 62 462 33  HOH HOH A . 
E 3 HOH 63 463 74  HOH HOH A . 
E 3 HOH 64 464 76  HOH HOH A . 
E 3 HOH 65 465 32  HOH HOH A . 
E 3 HOH 66 466 104 HOH HOH A . 
E 3 HOH 67 467 73  HOH HOH A . 
E 3 HOH 68 468 53  HOH HOH A . 
E 3 HOH 69 469 41  HOH HOH A . 
E 3 HOH 70 470 85  HOH HOH A . 
E 3 HOH 71 471 66  HOH HOH A . 
E 3 HOH 72 472 72  HOH HOH A . 
E 3 HOH 73 473 80  HOH HOH A . 
F 3 HOH 1  401 101 HOH HOH B . 
F 3 HOH 2  402 25  HOH HOH B . 
F 3 HOH 3  403 11  HOH HOH B . 
F 3 HOH 4  404 65  HOH HOH B . 
F 3 HOH 5  405 13  HOH HOH B . 
F 3 HOH 6  406 19  HOH HOH B . 
F 3 HOH 7  407 21  HOH HOH B . 
F 3 HOH 8  408 22  HOH HOH B . 
F 3 HOH 9  409 23  HOH HOH B . 
F 3 HOH 10 410 40  HOH HOH B . 
F 3 HOH 11 411 16  HOH HOH B . 
F 3 HOH 12 412 9   HOH HOH B . 
F 3 HOH 13 413 45  HOH HOH B . 
F 3 HOH 14 414 70  HOH HOH B . 
F 3 HOH 15 415 4   HOH HOH B . 
F 3 HOH 16 416 114 HOH HOH B . 
F 3 HOH 17 417 64  HOH HOH B . 
F 3 HOH 18 418 54  HOH HOH B . 
F 3 HOH 19 419 42  HOH HOH B . 
F 3 HOH 20 420 50  HOH HOH B . 
F 3 HOH 21 421 57  HOH HOH B . 
F 3 HOH 22 422 92  HOH HOH B . 
F 3 HOH 23 423 31  HOH HOH B . 
F 3 HOH 24 424 68  HOH HOH B . 
F 3 HOH 25 425 94  HOH HOH B . 
F 3 HOH 26 426 111 HOH HOH B . 
F 3 HOH 27 427 81  HOH HOH B . 
F 3 HOH 28 428 89  HOH HOH B . 
F 3 HOH 29 429 48  HOH HOH B . 
F 3 HOH 30 430 97  HOH HOH B . 
F 3 HOH 31 431 96  HOH HOH B . 
F 3 HOH 32 432 44  HOH HOH B . 
F 3 HOH 33 433 49  HOH HOH B . 
F 3 HOH 34 434 100 HOH HOH B . 
F 3 HOH 35 435 27  HOH HOH B . 
F 3 HOH 36 436 67  HOH HOH B . 
F 3 HOH 37 437 82  HOH HOH B . 
F 3 HOH 38 438 69  HOH HOH B . 
F 3 HOH 39 439 115 HOH HOH B . 
F 3 HOH 40 440 88  HOH HOH B . 
F 3 HOH 41 441 95  HOH HOH B . 
F 3 HOH 42 442 90  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 112 ? CG  ? A ARG 112 CG  
2  1 Y 1 A ARG 112 ? CD  ? A ARG 112 CD  
3  1 Y 1 A ARG 112 ? NE  ? A ARG 112 NE  
4  1 Y 1 A ARG 112 ? CZ  ? A ARG 112 CZ  
5  1 Y 1 A ARG 112 ? NH1 ? A ARG 112 NH1 
6  1 Y 1 A ARG 112 ? NH2 ? A ARG 112 NH2 
7  1 Y 1 A ARG 171 ? CG  ? A ARG 171 CG  
8  1 Y 1 A ARG 171 ? CD  ? A ARG 171 CD  
9  1 Y 1 A ARG 171 ? NE  ? A ARG 171 NE  
10 1 Y 1 A ARG 171 ? CZ  ? A ARG 171 CZ  
11 1 Y 1 A ARG 171 ? NH1 ? A ARG 171 NH1 
12 1 Y 1 A ARG 171 ? NH2 ? A ARG 171 NH2 
13 1 Y 1 A VAL 174 ? CG1 ? A VAL 174 CG1 
14 1 Y 1 A VAL 174 ? CG2 ? A VAL 174 CG2 
15 1 Y 1 A SER 175 ? OG  ? A SER 175 OG  
16 1 Y 1 A THR 176 ? OG1 ? A THR 176 OG1 
17 1 Y 1 A THR 176 ? CG2 ? A THR 176 CG2 
18 1 Y 1 A ASN 180 ? CG  ? A ASN 180 CG  
19 1 Y 1 A ASN 180 ? OD1 ? A ASN 180 OD1 
20 1 Y 1 A ASN 180 ? ND2 ? A ASN 180 ND2 
21 1 Y 1 A ARG 183 ? CG  ? A ARG 183 CG  
22 1 Y 1 A ARG 183 ? CD  ? A ARG 183 CD  
23 1 Y 1 A ARG 183 ? NE  ? A ARG 183 NE  
24 1 Y 1 A ARG 183 ? CZ  ? A ARG 183 CZ  
25 1 Y 1 A ARG 183 ? NH1 ? A ARG 183 NH1 
26 1 Y 1 A ARG 183 ? NH2 ? A ARG 183 NH2 
27 1 Y 1 B ARG 89  ? CG  ? B ARG 89  CG  
28 1 Y 1 B ARG 89  ? CD  ? B ARG 89  CD  
29 1 Y 1 B ARG 89  ? NE  ? B ARG 89  NE  
30 1 Y 1 B ARG 89  ? CZ  ? B ARG 89  CZ  
31 1 Y 1 B ARG 89  ? NH1 ? B ARG 89  NH1 
32 1 Y 1 B ARG 89  ? NH2 ? B ARG 89  NH2 
33 1 Y 1 B GLN 91  ? CG  ? B GLN 91  CG  
34 1 Y 1 B GLN 91  ? CD  ? B GLN 91  CD  
35 1 Y 1 B GLN 91  ? OE1 ? B GLN 91  OE1 
36 1 Y 1 B GLN 91  ? NE2 ? B GLN 91  NE2 
37 1 Y 1 B ARG 112 ? NE  ? B ARG 112 NE  
38 1 Y 1 B ARG 112 ? CZ  ? B ARG 112 CZ  
39 1 Y 1 B ARG 112 ? NH1 ? B ARG 112 NH1 
40 1 Y 1 B ARG 112 ? NH2 ? B ARG 112 NH2 
41 1 Y 1 B GLU 130 ? CG  ? B GLU 130 CG  
42 1 Y 1 B GLU 130 ? CD  ? B GLU 130 CD  
43 1 Y 1 B GLU 130 ? OE1 ? B GLU 130 OE1 
44 1 Y 1 B GLU 130 ? OE2 ? B GLU 130 OE2 
45 1 Y 1 B LEU 133 ? CG  ? B LEU 133 CG  
46 1 Y 1 B LEU 133 ? CD1 ? B LEU 133 CD1 
47 1 Y 1 B LEU 133 ? CD2 ? B LEU 133 CD2 
48 1 Y 1 B GLU 137 ? CG  ? B GLU 137 CG  
49 1 Y 1 B GLU 137 ? CD  ? B GLU 137 CD  
50 1 Y 1 B GLU 137 ? OE1 ? B GLU 137 OE1 
51 1 Y 1 B GLU 137 ? OE2 ? B GLU 137 OE2 
52 1 Y 1 B GLU 141 ? CG  ? B GLU 141 CG  
53 1 Y 1 B GLU 141 ? CD  ? B GLU 141 CD  
54 1 Y 1 B GLU 141 ? OE1 ? B GLU 141 OE1 
55 1 Y 1 B GLU 141 ? OE2 ? B GLU 141 OE2 
56 1 Y 1 B THR 176 ? OG1 ? B THR 176 OG1 
57 1 Y 1 B THR 176 ? CG2 ? B THR 176 CG2 
58 1 Y 1 B LEU 187 ? CG  ? B LEU 187 CG  
59 1 Y 1 B LEU 187 ? CD1 ? B LEU 187 CD1 
60 1 Y 1 B LEU 187 ? CD2 ? B LEU 187 CD2 
61 1 Y 1 B THR 188 ? OG1 ? B THR 188 OG1 
62 1 Y 1 B THR 188 ? CG2 ? B THR 188 CG2 
63 1 Y 1 B ARG 216 ? CG  ? B ARG 216 CG  
64 1 Y 1 B ARG 216 ? CD  ? B ARG 216 CD  
65 1 Y 1 B ARG 216 ? NE  ? B ARG 216 NE  
66 1 Y 1 B ARG 216 ? CZ  ? B ARG 216 CZ  
67 1 Y 1 B ARG 216 ? NH1 ? B ARG 216 NH1 
68 1 Y 1 B ARG 216 ? NH2 ? B ARG 216 NH2 
69 1 Y 1 B ASP 228 ? CG  ? B ASP 228 CG  
70 1 Y 1 B ASP 228 ? OD1 ? B ASP 228 OD1 
71 1 Y 1 B ASP 228 ? OD2 ? B ASP 228 OD2 
# 
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 ? ? ? 1.14_3260 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   124.207 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JPK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     93.745 
_cell.length_a_esd                 ? 
_cell.length_b                     64.641 
_cell.length_b_esd                 ? 
_cell.length_c                     65.432 
_cell.length_c_esd                 ? 
_cell.volume                       327914.697 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9JPK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JPK 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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    '0.2 M Sodium chloride, 20% w/v Polyethylene glycol 3,350, pH 7.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     177 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-24 
_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   0.979145 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979145 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          27.56 
_reflns.entry_id                                       9JPK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.28 
_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                                     14804 
_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                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.895 
_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                                    2.28 
_reflns_shell.d_res_low                                     10 
_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                             14840 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.883 
_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                               32.80 
_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                                 9JPK 
_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                            2.28 
_refine.ls_d_res_low                             31.39 
_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                     14804 
_refine.ls_number_reflns_R_free                  741 
_refine.ls_number_reflns_R_work                  14063 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.60 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2327 
_refine.ls_R_factor_R_free                       0.2706 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2308 
_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                          1.34 
_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                      AlphaFold 
_refine.pdbx_stereochemistry_target_values       'CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.8243 
_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                            0.2965 
_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                       2.28 
_refine_hist.d_res_low                        31.39 
_refine_hist.number_atoms_solvent             115 
_refine_hist.number_atoms_total               2248 
_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        2131 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_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' ? 0.0257  ? 2159 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 2.2339  ? 2938 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1692  ? 348  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0130  ? 393  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 28.6920 ? 758  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.28 2.46  . . 139 2752 98.77  . . . . 0.2846 . . . . . . . . . . . 0.3905 
'X-RAY DIFFRACTION' 2.46 2.70  . . 136 2834 99.87  . . . . 0.2645 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 2.70 3.09  . . 161 2784 100.00 . . . . 0.2589 . . . . . . . . . . . 0.2928 
'X-RAY DIFFRACTION' 3.09 3.90  . . 153 2816 99.56  . . . . 0.2262 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 3.90 31.39 . . 152 2877 99.80  . . . . 0.1964 . . . . . . . . . . . 0.2281 
# 
_struct.entry_id                     9JPK 
_struct.title                        'Crystal structure of DhdR inducer binding domain' 
_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        9JPK 
_struct_keywords.text            'transcriptional regulator, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A6N0JVZ6_ACHDE 
_struct_ref.pdbx_db_accession          A0A6N0JVZ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLSKSLTLTEQVARQIAGDIAEGVHSVGAKLPPGRVLAEQYGVSAAVIREATERLRAQGLIQSRQGSGSVVVSRTGAQGF
QVSAGLDDREQLASVYELRMELEGGAAALAARRRNATDLVAMAEALAALEANLEHPEQGVEHDIAFHVAIAAATHNRYYQ
DLLQYLNLQLRLAVSTARTNSRRQEGLTAVVHQEHVAVYDAILAGDPDRARLAATRHLQQAASRLRLDLLSPAARQTS
;
_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 9JPK A 1 ? 238 ? A0A6N0JVZ6 1 ? 238 ? 1 238 
2 1 9JPK B 1 ? 238 ? A0A6N0JVZ6 1 ? 238 ? 1 238 
# 
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 9JPK ALA A 120 ? UNP A0A6N0JVZ6 VAL 120 conflict 120 1 
1 9JPK ASP A 134 ? UNP A0A6N0JVZ6 GLU 134 conflict 134 2 
2 9JPK ALA B 120 ? UNP A0A6N0JVZ6 VAL 120 conflict 120 3 
2 9JPK ASP B 134 ? UNP A0A6N0JVZ6 GLU 134 conflict 134 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1650  ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  15100 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 85  ? ARG A 114 ? GLY A 85  ARG A 114 1 ? 30 
HELX_P HELX_P2  AA2 ASN A 115 ? ASN A 132 ? ASN A 115 ASN A 132 1 ? 18 
HELX_P HELX_P3  AA3 HIS A 135 ? ALA A 153 ? HIS A 135 ALA A 153 1 ? 19 
HELX_P HELX_P4  AA4 ASN A 156 ? ASN A 167 ? ASN A 156 ASN A 167 1 ? 12 
HELX_P HELX_P5  AA5 SER A 175 ? GLY A 186 ? SER A 175 GLY A 186 1 ? 12 
HELX_P HELX_P6  AA6 GLY A 186 ? ALA A 204 ? GLY A 186 ALA A 204 1 ? 19 
HELX_P HELX_P7  AA7 ASP A 206 ? SER A 231 ? ASP A 206 SER A 231 1 ? 26 
HELX_P HELX_P8  AA8 ARG B 89  ? ARG B 114 ? ARG B 89  ARG B 114 1 ? 26 
HELX_P HELX_P9  AA9 ASN B 115 ? ASN B 132 ? ASN B 115 ASN B 132 1 ? 18 
HELX_P HELX_P10 AB1 HIS B 135 ? ALA B 153 ? HIS B 135 ALA B 153 1 ? 19 
HELX_P HELX_P11 AB2 ASN B 156 ? VAL B 174 ? ASN B 156 VAL B 174 1 ? 19 
HELX_P HELX_P12 AB3 LEU B 187 ? GLY B 205 ? LEU B 187 GLY B 205 1 ? 19 
HELX_P HELX_P13 AB4 ASP B 206 ? SER B 231 ? ASP B 206 SER B 231 1 ? 26 
# 
_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 ASP 143 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 143 A ZN 301 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc2 metalc ? ? A HIS 147 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 147 A ZN 301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc3 metalc ? ? A HIS 195 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 195 A ZN 301 1_555 ? ? ? ? ? ? ? 1.843 ? ? 
metalc4 metalc ? ? A HIS 217 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 217 A ZN 301 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc5 metalc ? ? B ASP 143 OD1 ? ? ? 1_555 D ZN . ZN ? ? B ASP 143 B ZN 301 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc6 metalc ? ? B HIS 147 NE2 ? ? ? 1_555 D ZN . ZN ? ? B HIS 147 B ZN 301 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc7 metalc ? ? B HIS 195 NE2 ? ? ? 1_555 D ZN . ZN ? ? B HIS 195 B ZN 301 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
metalc8 metalc ? ? B HIS 217 NE2 ? ? ? 1_555 D ZN . ZN ? ? B HIS 217 B ZN 301 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
# 
_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  OD1 ? A ASP 143 ? A ASP 143 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 147 ? A HIS 147 ? 1_555 88.0  ? 
2  OD1 ? A ASP 143 ? A ASP 143 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 195 ? A HIS 195 ? 1_555 72.1  ? 
3  NE2 ? A HIS 147 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 195 ? A HIS 195 ? 1_555 89.1  ? 
4  OD1 ? A ASP 143 ? A ASP 143 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 161.1 ? 
5  NE2 ? A HIS 147 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 102.5 ? 
6  NE2 ? A HIS 195 ? A HIS 195 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 92.1  ? 
7  OD1 ? B ASP 143 ? B ASP 143 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 147 ? B HIS 147 ? 1_555 89.8  ? 
8  OD1 ? B ASP 143 ? B ASP 143 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 195 ? B HIS 195 ? 1_555 72.1  ? 
9  NE2 ? B HIS 147 ? B HIS 147 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 195 ? B HIS 195 ? 1_555 93.4  ? 
10 OD1 ? B ASP 143 ? B ASP 143 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 167.9 ? 
11 NE2 ? B HIS 147 ? B HIS 147 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 100.9 ? 
12 NE2 ? B HIS 195 ? B HIS 195 ? 1_555 ZN ? D ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 101.3 ? 
# 
_pdbx_entry_details.entry_id                   9JPK 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE  A ARG 182 ? ? O   A HOH 401 ? ? 1.52 
2 1 OE1 B GLU 90  ? ? O   B HOH 401 ? ? 1.69 
3 1 CB  B ASP 228 ? ? O   B HOH 428 ? ? 1.80 
4 1 OE2 A GLU 141 ? ? O   A HOH 402 ? ? 2.06 
5 1 CB  A THR 179 ? ? O   A HOH 411 ? ? 2.07 
6 1 O   A HOH 461 ? ? O   A HOH 465 ? ? 2.12 
7 1 OD2 A ASP 206 ? ? O   A HOH 403 ? ? 2.17 
8 1 OE2 A GLU 97  ? ? NH1 B ARG 113 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OD2 B ASP 161 ? ? 1_555 OD2 B ASP 161 ? ? 2_556 1.89 
2 1 NH2 B ARG 157 ? ? 1_555 OD1 B ASP 161 ? ? 2_556 2.09 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 130 ? ? OE1 A GLU 130 ? ? 1.181 1.252 -0.071 0.011 N 
2 1 CD A GLU 194 ? ? OE1 A GLU 194 ? ? 1.182 1.252 -0.070 0.011 N 
3 1 CD B GLU 97  ? ? OE2 B GLU 97  ? ? 1.181 1.252 -0.071 0.011 N 
4 1 CD B GLU 194 ? ? OE2 B GLU 194 ? ? 1.184 1.252 -0.068 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASN 167 ? ? CA A ASN 167 ? ? C A ASN 167 ? ? 123.39 110.40 12.99  2.00 N 
2 1 CB B ASN 115 ? ? CA B ASN 115 ? ? C B ASN 115 ? ? 91.76  110.40 -18.64 2.00 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    VAL 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     174 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -115.51 
_pdbx_validate_torsion.psi             65.60 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             THR 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              179 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.51 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A LEU 2   ? A LEU 2   
3   1 Y 1 A SER 3   ? A SER 3   
4   1 Y 1 A LYS 4   ? A LYS 4   
5   1 Y 1 A SER 5   ? A SER 5   
6   1 Y 1 A LEU 6   ? A LEU 6   
7   1 Y 1 A THR 7   ? A THR 7   
8   1 Y 1 A LEU 8   ? A LEU 8   
9   1 Y 1 A THR 9   ? A THR 9   
10  1 Y 1 A GLU 10  ? A GLU 10  
11  1 Y 1 A GLN 11  ? A GLN 11  
12  1 Y 1 A VAL 12  ? A VAL 12  
13  1 Y 1 A ALA 13  ? A ALA 13  
14  1 Y 1 A ARG 14  ? A ARG 14  
15  1 Y 1 A GLN 15  ? A GLN 15  
16  1 Y 1 A ILE 16  ? A ILE 16  
17  1 Y 1 A ALA 17  ? A ALA 17  
18  1 Y 1 A GLY 18  ? A GLY 18  
19  1 Y 1 A ASP 19  ? A ASP 19  
20  1 Y 1 A ILE 20  ? A ILE 20  
21  1 Y 1 A ALA 21  ? A ALA 21  
22  1 Y 1 A GLU 22  ? A GLU 22  
23  1 Y 1 A GLY 23  ? A GLY 23  
24  1 Y 1 A VAL 24  ? A VAL 24  
25  1 Y 1 A HIS 25  ? A HIS 25  
26  1 Y 1 A SER 26  ? A SER 26  
27  1 Y 1 A VAL 27  ? A VAL 27  
28  1 Y 1 A GLY 28  ? A GLY 28  
29  1 Y 1 A ALA 29  ? A ALA 29  
30  1 Y 1 A LYS 30  ? A LYS 30  
31  1 Y 1 A LEU 31  ? A LEU 31  
32  1 Y 1 A PRO 32  ? A PRO 32  
33  1 Y 1 A PRO 33  ? A PRO 33  
34  1 Y 1 A GLY 34  ? A GLY 34  
35  1 Y 1 A ARG 35  ? A ARG 35  
36  1 Y 1 A VAL 36  ? A VAL 36  
37  1 Y 1 A LEU 37  ? A LEU 37  
38  1 Y 1 A ALA 38  ? A ALA 38  
39  1 Y 1 A GLU 39  ? A GLU 39  
40  1 Y 1 A GLN 40  ? A GLN 40  
41  1 Y 1 A TYR 41  ? A TYR 41  
42  1 Y 1 A GLY 42  ? A GLY 42  
43  1 Y 1 A VAL 43  ? A VAL 43  
44  1 Y 1 A SER 44  ? A SER 44  
45  1 Y 1 A ALA 45  ? A ALA 45  
46  1 Y 1 A ALA 46  ? A ALA 46  
47  1 Y 1 A VAL 47  ? A VAL 47  
48  1 Y 1 A ILE 48  ? A ILE 48  
49  1 Y 1 A ARG 49  ? A ARG 49  
50  1 Y 1 A GLU 50  ? A GLU 50  
51  1 Y 1 A ALA 51  ? A ALA 51  
52  1 Y 1 A THR 52  ? A THR 52  
53  1 Y 1 A GLU 53  ? A GLU 53  
54  1 Y 1 A ARG 54  ? A ARG 54  
55  1 Y 1 A LEU 55  ? A LEU 55  
56  1 Y 1 A ARG 56  ? A ARG 56  
57  1 Y 1 A ALA 57  ? A ALA 57  
58  1 Y 1 A GLN 58  ? A GLN 58  
59  1 Y 1 A GLY 59  ? A GLY 59  
60  1 Y 1 A LEU 60  ? A LEU 60  
61  1 Y 1 A ILE 61  ? A ILE 61  
62  1 Y 1 A GLN 62  ? A GLN 62  
63  1 Y 1 A SER 63  ? A SER 63  
64  1 Y 1 A ARG 64  ? A ARG 64  
65  1 Y 1 A GLN 65  ? A GLN 65  
66  1 Y 1 A GLY 66  ? A GLY 66  
67  1 Y 1 A SER 67  ? A SER 67  
68  1 Y 1 A GLY 68  ? A GLY 68  
69  1 Y 1 A SER 69  ? A SER 69  
70  1 Y 1 A VAL 70  ? A VAL 70  
71  1 Y 1 A VAL 71  ? A VAL 71  
72  1 Y 1 A VAL 72  ? A VAL 72  
73  1 Y 1 A SER 73  ? A SER 73  
74  1 Y 1 A ARG 74  ? A ARG 74  
75  1 Y 1 A THR 75  ? A THR 75  
76  1 Y 1 A GLY 76  ? A GLY 76  
77  1 Y 1 A ALA 77  ? A ALA 77  
78  1 Y 1 A GLN 78  ? A GLN 78  
79  1 Y 1 A GLY 79  ? A GLY 79  
80  1 Y 1 A PHE 80  ? A PHE 80  
81  1 Y 1 A GLN 81  ? A GLN 81  
82  1 Y 1 A ALA 233 ? A ALA 233 
83  1 Y 1 A ALA 234 ? A ALA 234 
84  1 Y 1 A ARG 235 ? A ARG 235 
85  1 Y 1 A GLN 236 ? A GLN 236 
86  1 Y 1 A THR 237 ? A THR 237 
87  1 Y 1 A SER 238 ? A SER 238 
88  1 Y 1 B MET 1   ? B MET 1   
89  1 Y 1 B LEU 2   ? B LEU 2   
90  1 Y 1 B SER 3   ? B SER 3   
91  1 Y 1 B LYS 4   ? B LYS 4   
92  1 Y 1 B SER 5   ? B SER 5   
93  1 Y 1 B LEU 6   ? B LEU 6   
94  1 Y 1 B THR 7   ? B THR 7   
95  1 Y 1 B LEU 8   ? B LEU 8   
96  1 Y 1 B THR 9   ? B THR 9   
97  1 Y 1 B GLU 10  ? B GLU 10  
98  1 Y 1 B GLN 11  ? B GLN 11  
99  1 Y 1 B VAL 12  ? B VAL 12  
100 1 Y 1 B ALA 13  ? B ALA 13  
101 1 Y 1 B ARG 14  ? B ARG 14  
102 1 Y 1 B GLN 15  ? B GLN 15  
103 1 Y 1 B ILE 16  ? B ILE 16  
104 1 Y 1 B ALA 17  ? B ALA 17  
105 1 Y 1 B GLY 18  ? B GLY 18  
106 1 Y 1 B ASP 19  ? B ASP 19  
107 1 Y 1 B ILE 20  ? B ILE 20  
108 1 Y 1 B ALA 21  ? B ALA 21  
109 1 Y 1 B GLU 22  ? B GLU 22  
110 1 Y 1 B GLY 23  ? B GLY 23  
111 1 Y 1 B VAL 24  ? B VAL 24  
112 1 Y 1 B HIS 25  ? B HIS 25  
113 1 Y 1 B SER 26  ? B SER 26  
114 1 Y 1 B VAL 27  ? B VAL 27  
115 1 Y 1 B GLY 28  ? B GLY 28  
116 1 Y 1 B ALA 29  ? B ALA 29  
117 1 Y 1 B LYS 30  ? B LYS 30  
118 1 Y 1 B LEU 31  ? B LEU 31  
119 1 Y 1 B PRO 32  ? B PRO 32  
120 1 Y 1 B PRO 33  ? B PRO 33  
121 1 Y 1 B GLY 34  ? B GLY 34  
122 1 Y 1 B ARG 35  ? B ARG 35  
123 1 Y 1 B VAL 36  ? B VAL 36  
124 1 Y 1 B LEU 37  ? B LEU 37  
125 1 Y 1 B ALA 38  ? B ALA 38  
126 1 Y 1 B GLU 39  ? B GLU 39  
127 1 Y 1 B GLN 40  ? B GLN 40  
128 1 Y 1 B TYR 41  ? B TYR 41  
129 1 Y 1 B GLY 42  ? B GLY 42  
130 1 Y 1 B VAL 43  ? B VAL 43  
131 1 Y 1 B SER 44  ? B SER 44  
132 1 Y 1 B ALA 45  ? B ALA 45  
133 1 Y 1 B ALA 46  ? B ALA 46  
134 1 Y 1 B VAL 47  ? B VAL 47  
135 1 Y 1 B ILE 48  ? B ILE 48  
136 1 Y 1 B ARG 49  ? B ARG 49  
137 1 Y 1 B GLU 50  ? B GLU 50  
138 1 Y 1 B ALA 51  ? B ALA 51  
139 1 Y 1 B THR 52  ? B THR 52  
140 1 Y 1 B GLU 53  ? B GLU 53  
141 1 Y 1 B ARG 54  ? B ARG 54  
142 1 Y 1 B LEU 55  ? B LEU 55  
143 1 Y 1 B ARG 56  ? B ARG 56  
144 1 Y 1 B ALA 57  ? B ALA 57  
145 1 Y 1 B GLN 58  ? B GLN 58  
146 1 Y 1 B GLY 59  ? B GLY 59  
147 1 Y 1 B LEU 60  ? B LEU 60  
148 1 Y 1 B ILE 61  ? B ILE 61  
149 1 Y 1 B GLN 62  ? B GLN 62  
150 1 Y 1 B SER 63  ? B SER 63  
151 1 Y 1 B ARG 64  ? B ARG 64  
152 1 Y 1 B GLN 65  ? B GLN 65  
153 1 Y 1 B GLY 66  ? B GLY 66  
154 1 Y 1 B SER 67  ? B SER 67  
155 1 Y 1 B GLY 68  ? B GLY 68  
156 1 Y 1 B SER 69  ? B SER 69  
157 1 Y 1 B VAL 70  ? B VAL 70  
158 1 Y 1 B VAL 71  ? B VAL 71  
159 1 Y 1 B VAL 72  ? B VAL 72  
160 1 Y 1 B SER 73  ? B SER 73  
161 1 Y 1 B ARG 74  ? B ARG 74  
162 1 Y 1 B THR 75  ? B THR 75  
163 1 Y 1 B GLY 76  ? B GLY 76  
164 1 Y 1 B ALA 77  ? B ALA 77  
165 1 Y 1 B GLN 78  ? B GLN 78  
166 1 Y 1 B GLY 79  ? B GLY 79  
167 1 Y 1 B PHE 80  ? B PHE 80  
168 1 Y 1 B GLN 81  ? B GLN 81  
169 1 Y 1 B VAL 82  ? B VAL 82  
170 1 Y 1 B SER 83  ? B SER 83  
171 1 Y 1 B ALA 84  ? B ALA 84  
172 1 Y 1 B GLY 85  ? B GLY 85  
173 1 Y 1 B LEU 86  ? B LEU 86  
174 1 Y 1 B ASP 87  ? B ASP 87  
175 1 Y 1 B ALA 177 ? B ALA 177 
176 1 Y 1 B ARG 178 ? B ARG 178 
177 1 Y 1 B THR 179 ? B THR 179 
178 1 Y 1 B ASN 180 ? B ASN 180 
179 1 Y 1 B SER 181 ? B SER 181 
180 1 Y 1 B ARG 182 ? B ARG 182 
181 1 Y 1 B ARG 183 ? B ARG 183 
182 1 Y 1 B GLN 184 ? B GLN 184 
183 1 Y 1 B GLU 185 ? B GLU 185 
184 1 Y 1 B PRO 232 ? B PRO 232 
185 1 Y 1 B ALA 233 ? B ALA 233 
186 1 Y 1 B ALA 234 ? B ALA 234 
187 1 Y 1 B ARG 235 ? B ARG 235 
188 1 Y 1 B GLN 236 ? B GLN 236 
189 1 Y 1 B THR 237 ? B THR 237 
190 1 Y 1 B SER 238 ? B SER 238 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
HIS N    N  N N 123 
HIS CA   C  N S 124 
HIS C    C  N N 125 
HIS O    O  N N 126 
HIS CB   C  N N 127 
HIS CG   C  Y N 128 
HIS ND1  N  Y N 129 
HIS CD2  C  Y N 130 
HIS CE1  C  Y N 131 
HIS NE2  N  Y N 132 
HIS OXT  O  N N 133 
HIS H    H  N N 134 
HIS H2   H  N N 135 
HIS HA   H  N N 136 
HIS HB2  H  N N 137 
HIS HB3  H  N N 138 
HIS HD1  H  N N 139 
HIS HD2  H  N N 140 
HIS HE1  H  N N 141 
HIS HE2  H  N N 142 
HIS HXT  H  N N 143 
HOH O    O  N N 144 
HOH H1   H  N N 145 
HOH H2   H  N N 146 
ILE N    N  N N 147 
ILE CA   C  N S 148 
ILE C    C  N N 149 
ILE O    O  N N 150 
ILE CB   C  N S 151 
ILE CG1  C  N N 152 
ILE CG2  C  N N 153 
ILE CD1  C  N N 154 
ILE OXT  O  N N 155 
ILE H    H  N N 156 
ILE H2   H  N N 157 
ILE HA   H  N N 158 
ILE HB   H  N N 159 
ILE HG12 H  N N 160 
ILE HG13 H  N N 161 
ILE HG21 H  N N 162 
ILE HG22 H  N N 163 
ILE HG23 H  N N 164 
ILE HD11 H  N N 165 
ILE HD12 H  N N 166 
ILE HD13 H  N N 167 
ILE HXT  H  N N 168 
LEU N    N  N N 169 
LEU CA   C  N S 170 
LEU C    C  N N 171 
LEU O    O  N N 172 
LEU CB   C  N N 173 
LEU CG   C  N N 174 
LEU CD1  C  N N 175 
LEU CD2  C  N N 176 
LEU OXT  O  N N 177 
LEU H    H  N N 178 
LEU H2   H  N N 179 
LEU HA   H  N N 180 
LEU HB2  H  N N 181 
LEU HB3  H  N N 182 
LEU HG   H  N N 183 
LEU HD11 H  N N 184 
LEU HD12 H  N N 185 
LEU HD13 H  N N 186 
LEU HD21 H  N N 187 
LEU HD22 H  N N 188 
LEU HD23 H  N N 189 
LEU HXT  H  N N 190 
LYS N    N  N N 191 
LYS CA   C  N S 192 
LYS C    C  N N 193 
LYS O    O  N N 194 
LYS CB   C  N N 195 
LYS CG   C  N N 196 
LYS CD   C  N N 197 
LYS CE   C  N N 198 
LYS NZ   N  N N 199 
LYS OXT  O  N N 200 
LYS H    H  N N 201 
LYS H2   H  N N 202 
LYS HA   H  N N 203 
LYS HB2  H  N N 204 
LYS HB3  H  N N 205 
LYS HG2  H  N N 206 
LYS HG3  H  N N 207 
LYS HD2  H  N N 208 
LYS HD3  H  N N 209 
LYS HE2  H  N N 210 
LYS HE3  H  N N 211 
LYS HZ1  H  N N 212 
LYS HZ2  H  N N 213 
LYS HZ3  H  N N 214 
LYS HXT  H  N N 215 
MET N    N  N N 216 
MET CA   C  N S 217 
MET C    C  N N 218 
MET O    O  N N 219 
MET CB   C  N N 220 
MET CG   C  N N 221 
MET SD   S  N N 222 
MET CE   C  N N 223 
MET OXT  O  N N 224 
MET H    H  N N 225 
MET H2   H  N N 226 
MET HA   H  N N 227 
MET HB2  H  N N 228 
MET HB3  H  N N 229 
MET HG2  H  N N 230 
MET HG3  H  N N 231 
MET HE1  H  N N 232 
MET HE2  H  N N 233 
MET HE3  H  N N 234 
MET HXT  H  N N 235 
PHE N    N  N N 236 
PHE CA   C  N S 237 
PHE C    C  N N 238 
PHE O    O  N N 239 
PHE CB   C  N N 240 
PHE CG   C  Y N 241 
PHE CD1  C  Y N 242 
PHE CD2  C  Y N 243 
PHE CE1  C  Y N 244 
PHE CE2  C  Y N 245 
PHE CZ   C  Y N 246 
PHE OXT  O  N N 247 
PHE H    H  N N 248 
PHE H2   H  N N 249 
PHE HA   H  N N 250 
PHE HB2  H  N N 251 
PHE HB3  H  N N 252 
PHE HD1  H  N N 253 
PHE HD2  H  N N 254 
PHE HE1  H  N N 255 
PHE HE2  H  N N 256 
PHE HZ   H  N N 257 
PHE HXT  H  N N 258 
PRO N    N  N N 259 
PRO CA   C  N S 260 
PRO C    C  N N 261 
PRO O    O  N N 262 
PRO CB   C  N N 263 
PRO CG   C  N N 264 
PRO CD   C  N N 265 
PRO OXT  O  N N 266 
PRO H    H  N N 267 
PRO HA   H  N N 268 
PRO HB2  H  N N 269 
PRO HB3  H  N N 270 
PRO HG2  H  N N 271 
PRO HG3  H  N N 272 
PRO HD2  H  N N 273 
PRO HD3  H  N N 274 
PRO HXT  H  N N 275 
SER N    N  N N 276 
SER CA   C  N S 277 
SER C    C  N N 278 
SER O    O  N N 279 
SER CB   C  N N 280 
SER OG   O  N N 281 
SER OXT  O  N N 282 
SER H    H  N N 283 
SER H2   H  N N 284 
SER HA   H  N N 285 
SER HB2  H  N N 286 
SER HB3  H  N N 287 
SER HG   H  N N 288 
SER HXT  H  N N 289 
THR N    N  N N 290 
THR CA   C  N S 291 
THR C    C  N N 292 
THR O    O  N N 293 
THR CB   C  N R 294 
THR OG1  O  N N 295 
THR CG2  C  N N 296 
THR OXT  O  N N 297 
THR H    H  N N 298 
THR H2   H  N N 299 
THR HA   H  N N 300 
THR HB   H  N N 301 
THR HG1  H  N N 302 
THR HG21 H  N N 303 
THR HG22 H  N N 304 
THR HG23 H  N N 305 
THR HXT  H  N N 306 
TYR N    N  N N 307 
TYR CA   C  N S 308 
TYR C    C  N N 309 
TYR O    O  N N 310 
TYR CB   C  N N 311 
TYR CG   C  Y N 312 
TYR CD1  C  Y N 313 
TYR CD2  C  Y N 314 
TYR CE1  C  Y N 315 
TYR CE2  C  Y N 316 
TYR CZ   C  Y N 317 
TYR OH   O  N N 318 
TYR OXT  O  N N 319 
TYR H    H  N N 320 
TYR H2   H  N N 321 
TYR HA   H  N N 322 
TYR HB2  H  N N 323 
TYR HB3  H  N N 324 
TYR HD1  H  N N 325 
TYR HD2  H  N N 326 
TYR HE1  H  N N 327 
TYR HE2  H  N N 328 
TYR HH   H  N N 329 
TYR HXT  H  N N 330 
VAL N    N  N N 331 
VAL CA   C  N S 332 
VAL C    C  N N 333 
VAL O    O  N N 334 
VAL CB   C  N N 335 
VAL CG1  C  N N 336 
VAL CG2  C  N N 337 
VAL OXT  O  N N 338 
VAL H    H  N N 339 
VAL H2   H  N N 340 
VAL HA   H  N N 341 
VAL HB   H  N N 342 
VAL HG11 H  N N 343 
VAL HG12 H  N N 344 
VAL HG13 H  N N 345 
VAL HG21 H  N N 346 
VAL HG22 H  N N 347 
VAL HG23 H  N N 348 
VAL HXT  H  N N 349 
ZN  ZN   ZN N N 350 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TYR N   CA   sing N N 293 
TYR N   H    sing N N 294 
TYR N   H2   sing N N 295 
TYR CA  C    sing N N 296 
TYR CA  CB   sing N N 297 
TYR CA  HA   sing N N 298 
TYR C   O    doub N N 299 
TYR C   OXT  sing N N 300 
TYR CB  CG   sing N N 301 
TYR CB  HB2  sing N N 302 
TYR CB  HB3  sing N N 303 
TYR CG  CD1  doub Y N 304 
TYR CG  CD2  sing Y N 305 
TYR CD1 CE1  sing Y N 306 
TYR CD1 HD1  sing N N 307 
TYR CD2 CE2  doub Y N 308 
TYR CD2 HD2  sing N N 309 
TYR CE1 CZ   doub Y N 310 
TYR CE1 HE1  sing N N 311 
TYR CE2 CZ   sing Y N 312 
TYR CE2 HE2  sing N N 313 
TYR CZ  OH   sing N N 314 
TYR OH  HH   sing N N 315 
TYR OXT HXT  sing N N 316 
VAL N   CA   sing N N 317 
VAL N   H    sing N N 318 
VAL N   H2   sing N N 319 
VAL CA  C    sing N N 320 
VAL CA  CB   sing N N 321 
VAL CA  HA   sing N N 322 
VAL C   O    doub N N 323 
VAL C   OXT  sing N N 324 
VAL CB  CG1  sing N N 325 
VAL CB  CG2  sing N N 326 
VAL CB  HB   sing N N 327 
VAL CG1 HG11 sing N N 328 
VAL CG1 HG12 sing N N 329 
VAL CG1 HG13 sing N N 330 
VAL CG2 HG21 sing N N 331 
VAL CG2 HG22 sing N N 332 
VAL CG2 HG23 sing N N 333 
VAL OXT HXT  sing N N 334 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9JPK 
_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]   0.010667 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007251 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015470 
_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]   0.018480 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 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   . VAL A 1 82  ? 4.39300   -14.21600 41.86400 1.000 45.39000 ? 82  VAL A N   1 
ATOM   2    C  CA  . VAL A 1 82  ? 4.06700   -13.29300 40.74900 1.000 44.49000 ? 82  VAL A CA  1 
ATOM   3    C  C   . VAL A 1 82  ? 2.96500   -12.34600 41.23200 1.000 43.21000 ? 82  VAL A C   1 
ATOM   4    O  O   . VAL A 1 82  ? 2.26300   -12.69900 42.12900 1.000 50.39000 ? 82  VAL A O   1 
ATOM   5    C  CB  . VAL A 1 82  ? 3.66700   -14.08600 39.49000 1.000 41.36000 ? 82  VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 82  ? 4.81900   -14.87900 38.88600 1.000 38.84000 ? 82  VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 82  ? 2.49300   -14.99700 39.74900 1.000 42.31000 ? 82  VAL A CG2 1 
ATOM   8    N  N   . SER A 1 83  ? 2.88200   -11.14000 40.70500 1.000 44.53000 ? 83  SER A N   1 
ATOM   9    C  CA  . SER A 1 83  ? 1.80900   -10.16200 41.02900 1.000 48.61000 ? 83  SER A CA  1 
ATOM   10   C  C   . SER A 1 83  ? 0.44100   -10.69200 40.58000 1.000 45.45000 ? 83  SER A C   1 
ATOM   11   O  O   . SER A 1 83  ? -0.57900  -10.27600 41.12900 1.000 48.22000 ? 83  SER A O   1 
ATOM   12   C  CB  . SER A 1 83  ? 2.11900   -8.79100  40.56300 1.000 46.79000 ? 83  SER A CB  1 
ATOM   13   O  OG  . SER A 1 83  ? 2.49700   -8.81100  39.22700 1.000 46.75000 ? 83  SER A OG  1 
ATOM   14   N  N   . ALA A 1 84  ? 0.45800   -11.35300 39.43700 1.000 42.71000 ? 84  ALA A N   1 
ATOM   15   C  CA  . ALA A 1 84  ? -0.74500  -11.97800 38.86700 1.000 39.03000 ? 84  ALA A CA  1 
ATOM   16   C  C   . ALA A 1 84  ? -0.33300  -13.32900 38.30100 1.000 39.89000 ? 84  ALA A C   1 
ATOM   17   O  O   . ALA A 1 84  ? 0.69100   -13.36700 37.64100 1.000 35.10000 ? 84  ALA A O   1 
ATOM   18   C  CB  . ALA A 1 84  ? -1.27000  -11.09600 37.78000 1.000 39.26000 ? 84  ALA A CB  1 
ATOM   19   N  N   . GLY A 1 85  ? -1.18300  -14.33300 38.52000 1.000 40.68000 ? 85  GLY A N   1 
ATOM   20   C  CA  . GLY A 1 85  ? -1.09000  -15.72500 38.05000 1.000 33.28000 ? 85  GLY A CA  1 
ATOM   21   C  C   . GLY A 1 85  ? -1.45900  -15.86600 36.58900 1.000 32.60000 ? 85  GLY A C   1 
ATOM   22   O  O   . GLY A 1 85  ? -2.00600  -14.95300 36.06200 1.000 28.36000 ? 85  GLY A O   1 
ATOM   23   N  N   . LEU A 1 86  ? -1.22100  -17.03800 36.00300 1.000 31.44000 ? 86  LEU A N   1 
ATOM   24   C  CA  . LEU A 1 86  ? -1.38300  -17.27200 34.54900 1.000 27.84000 ? 86  LEU A CA  1 
ATOM   25   C  C   . LEU A 1 86  ? -2.78800  -16.95400 34.03100 1.000 25.97000 ? 86  LEU A C   1 
ATOM   26   O  O   . LEU A 1 86  ? -2.87400  -16.45500 32.98300 1.000 24.88000 ? 86  LEU A O   1 
ATOM   27   C  CB  . LEU A 1 86  ? -1.03200  -18.72000 34.24100 1.000 31.10000 ? 86  LEU A CB  1 
ATOM   28   C  CG  . LEU A 1 86  ? -1.01000  -19.07800 32.76200 1.000 27.23000 ? 86  LEU A CG  1 
ATOM   29   C  CD1 . LEU A 1 86  ? 0.06900   -18.29700 32.06500 1.000 27.29000 ? 86  LEU A CD1 1 
ATOM   30   C  CD2 . LEU A 1 86  ? -0.81900  -20.54800 32.54600 1.000 19.83000 ? 86  LEU A CD2 1 
ATOM   31   N  N   . ASP A 1 87  ? -3.83800  -17.30000 34.73300 1.000 31.29000 ? 87  ASP A N   1 
ATOM   32   C  CA  . ASP A 1 87  ? -5.18200  -17.00600 34.17100 1.000 29.91000 ? 87  ASP A CA  1 
ATOM   33   C  C   . ASP A 1 87  ? -5.46600  -15.49400 34.11700 1.000 28.55000 ? 87  ASP A C   1 
ATOM   34   O  O   . ASP A 1 87  ? -6.06800  -15.08300 33.17900 1.000 25.70000 ? 87  ASP A O   1 
ATOM   35   C  CB  . ASP A 1 87  ? -6.24500  -17.96100 34.70400 1.000 31.52000 ? 87  ASP A CB  1 
ATOM   36   C  CG  . ASP A 1 87  ? -7.62900  -17.74500 34.10400 1.000 53.39000 ? 87  ASP A CG  1 
ATOM   37   O  OD1 . ASP A 1 87  ? -7.78500  -18.01800 32.92200 1.000 50.60000 ? 87  ASP A OD1 1 
ATOM   38   O  OD2 . ASP A 1 87  ? -8.53900  -17.31100 34.83700 1.000 57.50000 ? 87  ASP A OD2 1 
ATOM   39   N  N   . ASP A 1 88  ? -5.01500  -14.71200 35.09300 1.000 28.62000 ? 88  ASP A N   1 
ATOM   40   C  CA  . ASP A 1 88  ? -5.13200  -13.23000 35.08100 1.000 27.72000 ? 88  ASP A CA  1 
ATOM   41   C  C   . ASP A 1 88  ? -4.28800  -12.66700 33.93500 1.000 25.54000 ? 88  ASP A C   1 
ATOM   42   O  O   . ASP A 1 88  ? -4.81800  -11.84400 33.20000 1.000 23.51000 ? 88  ASP A O   1 
ATOM   43   C  CB  . ASP A 1 88  ? -4.75000  -12.56600 36.40600 1.000 31.15000 ? 88  ASP A CB  1 
ATOM   44   C  CG  . ASP A 1 88  ? -5.84500  -12.50600 37.46100 1.000 35.05000 ? 88  ASP A CG  1 
ATOM   45   O  OD1 . ASP A 1 88  ? -6.74300  -13.29500 37.38000 1.000 33.27000 ? 88  ASP A OD1 1 
ATOM   46   O  OD2 . ASP A 1 88  ? -5.74500  -11.68700 38.37100 1.000 32.27000 ? 88  ASP A OD2 1 
ATOM   47   N  N   . ARG A 1 89  ? -3.07600  -13.18800 33.73500 1.000 18.92000 ? 89  ARG A N   1 
ATOM   48   C  CA  . ARG A 1 89  ? -2.23300  -12.74300 32.59700 1.000 21.91000 ? 89  ARG A CA  1 
ATOM   49   C  C   . ARG A 1 89  ? -2.89800  -13.05800 31.24800 1.000 23.04000 ? 89  ARG A C   1 
ATOM   50   O  O   . ARG A 1 89  ? -2.78300  -12.23900 30.39600 1.000 20.36000 ? 89  ARG A O   1 
ATOM   51   C  CB  . ARG A 1 89  ? -0.81200  -13.30000 32.61200 1.000 19.27000 ? 89  ARG A CB  1 
ATOM   52   C  CG  . ARG A 1 89  ? 0.01100   -12.95800 33.82900 1.000 20.34000 ? 89  ARG A CG  1 
ATOM   53   C  CD  . ARG A 1 89  ? 1.45600   -13.31900 33.61400 1.000 28.72000 ? 89  ARG A CD  1 
ATOM   54   N  NE  . ARG A 1 89  ? 1.76600   -14.72600 33.57700 1.000 25.49000 ? 89  ARG A NE  1 
ATOM   55   C  CZ  . ARG A 1 89  ? 1.99300   -15.45900 34.62900 1.000 25.33000 ? 89  ARG A CZ  1 
ATOM   56   N  NH1 . ARG A 1 89  ? 1.97300   -14.92600 35.81600 1.000 30.25000 ? 89  ARG A NH1 1 
ATOM   57   N  NH2 . ARG A 1 89  ? 2.29900   -16.71300 34.50700 1.000 23.38000 ? 89  ARG A NH2 1 
ATOM   58   N  N   . GLU A 1 90  ? -3.51200  -14.23100 31.10200 1.000 17.44000 ? 90  GLU A N   1 
ATOM   59   C  CA  . GLU A 1 90  ? -4.19900  -14.61000 29.85300 1.000 21.57000 ? 90  GLU A CA  1 
ATOM   60   C  C   . GLU A 1 90  ? -5.42800  -13.72100 29.60100 1.000 20.71000 ? 90  GLU A C   1 
ATOM   61   O  O   . GLU A 1 90  ? -5.59300  -13.31900 28.52800 1.000 19.57000 ? 90  GLU A O   1 
ATOM   62   C  CB  . GLU A 1 90  ? -4.46400  -16.11200 29.78100 1.000 24.31000 ? 90  GLU A CB  1 
ATOM   63   C  CG  . GLU A 1 90  ? -3.32200  -16.88800 29.17900 1.000 33.58000 ? 90  GLU A CG  1 
ATOM   64   C  CD  . GLU A 1 90  ? -2.63500  -16.26100 27.97500 1.000 39.63000 ? 90  GLU A CD  1 
ATOM   65   O  OE1 . GLU A 1 90  ? -3.28600  -16.01100 26.98800 1.000 41.57000 ? 90  GLU A OE1 1 
ATOM   66   O  OE2 . GLU A 1 90  ? -1.45500  -16.03500 28.03900 1.000 39.51000 ? 90  GLU A OE2 1 
ATOM   67   N  N   . GLN A 1 91  ? -6.20500  -13.41300 30.61100 1.000 17.12000 ? 91  GLN A N   1 
ATOM   68   C  CA  . GLN A 1 91  ? -7.38200  -12.53300 30.46600 1.000 21.45000 ? 91  GLN A CA  1 
ATOM   69   C  C   . GLN A 1 91  ? -6.94800  -11.11800 30.07000 1.000 22.54000 ? 91  GLN A C   1 
ATOM   70   O  O   . GLN A 1 91  ? -7.48900  -10.61600 29.13300 1.000 20.69000 ? 91  GLN A O   1 
ATOM   71   C  CB  . GLN A 1 91  ? -8.21400  -12.63400 31.73200 1.000 23.37000 ? 91  GLN A CB  1 
ATOM   72   C  CG  . GLN A 1 91  ? -9.03300  -13.90100 31.73900 1.000 32.35000 ? 91  GLN A CG  1 
ATOM   73   C  CD  . GLN A 1 91  ? -9.50600  -14.35800 33.08800 1.000 38.45000 ? 91  GLN A CD  1 
ATOM   74   O  OE1 . GLN A 1 91  ? -9.27200  -13.74400 34.11100 1.000 37.32000 ? 91  GLN A OE1 1 
ATOM   75   N  NE2 . GLN A 1 91  ? -10.20100 -15.47200 33.08700 1.000 44.30000 ? 91  GLN A NE2 1 
ATOM   76   N  N   . LEU A 1 92  ? -5.90700  -10.61800 30.71500 1.000 19.18000 ? 92  LEU A N   1 
ATOM   77   C  CA  . LEU A 1 92  ? -5.34200  -9.28900  30.42900 1.000 20.24000 ? 92  LEU A CA  1 
ATOM   78   C  C   . LEU A 1 92  ? -4.80700  -9.20600  29.01100 1.000 21.61000 ? 92  LEU A C   1 
ATOM   79   O  O   . LEU A 1 92  ? -5.12200  -8.26400  28.35500 1.000 22.19000 ? 92  LEU A O   1 
ATOM   80   C  CB  . LEU A 1 92  ? -4.28100  -8.92700  31.46000 1.000 17.38000 ? 92  LEU A CB  1 
ATOM   81   C  CG  . LEU A 1 92  ? -4.89100  -8.43500  32.74700 1.000 22.43000 ? 92  LEU A CG  1 
ATOM   82   C  CD1 . LEU A 1 92  ? -4.02200  -8.68300  33.95700 1.000 24.16000 ? 92  LEU A CD1 1 
ATOM   83   C  CD2 . LEU A 1 92  ? -5.37100  -7.00600  32.63000 1.000 20.16000 ? 92  LEU A CD2 1 
ATOM   84   N  N   . ALA A 1 93  ? -4.10700  -10.22700 28.54800 1.000 19.17000 ? 93  ALA A N   1 
ATOM   85   C  CA  . ALA A 1 93  ? -3.59200  -10.23000 27.17400 1.000 18.89000 ? 93  ALA A CA  1 
ATOM   86   C  C   . ALA A 1 93  ? -4.75800  -10.21300 26.17500 1.000 22.83000 ? 93  ALA A C   1 
ATOM   87   O  O   . ALA A 1 93  ? -4.62100  -9.61900  25.17500 1.000 23.21000 ? 93  ALA A O   1 
ATOM   88   C  CB  . ALA A 1 93  ? -2.71400  -11.41400 26.99900 1.000 21.72000 ? 93  ALA A CB  1 
ATOM   89   N  N   . SER A 1 94  ? -5.83300  -10.91300 26.48000 1.000 16.67000 ? 94  SER A N   1 
ATOM   90   C  CA  . SER A 1 94  ? -7.05300  -10.92100 25.66300 1.000 21.75000 ? 94  SER A CA  1 
ATOM   91   C  C   . SER A 1 94  ? -7.66800  -9.51800  25.61800 1.000 19.03000 ? 94  SER A C   1 
ATOM   92   O  O   . SER A 1 94  ? -8.01500  -9.10800  24.58100 1.000 17.88000 ? 94  SER A O   1 
ATOM   93   C  CB  . SER A 1 94  ? -8.02000  -11.94100 26.17300 1.000 21.35000 ? 94  SER A CB  1 
ATOM   94   O  OG  . SER A 1 94  ? -7.85900  -13.12400 25.48200 1.000 22.34000 ? 94  SER A OG  1 
ATOM   95   N  N   . VAL A 1 95  ? -7.70400  -8.83000  26.73900 1.000 17.08000 ? 95  VAL A N   1 
ATOM   96   C  CA  . VAL A 1 95  ? -8.25700  -7.45500  26.80100 1.000 20.05000 ? 95  VAL A CA  1 
ATOM   97   C  C   . VAL A 1 95  ? -7.39500  -6.50000  25.95900 1.000 22.75000 ? 95  VAL A C   1 
ATOM   98   O  O   . VAL A 1 95  ? -7.95700  -5.76500  25.19700 1.000 17.20000 ? 95  VAL A O   1 
ATOM   99   C  CB  . VAL A 1 95  ? -8.46300  -6.97200  28.23900 1.000 19.37000 ? 95  VAL A CB  1 
ATOM   100  C  CG1 . VAL A 1 95  ? -8.66900  -5.48100  28.26100 1.000 22.60000 ? 95  VAL A CG1 1 
ATOM   101  C  CG2 . VAL A 1 95  ? -9.59200  -7.67800  28.94500 1.000 17.63000 ? 95  VAL A CG2 1 
ATOM   102  N  N   . TYR A 1 96  ? -6.07200  -6.61600  26.05100 1.000 20.03000 ? 96  TYR A N   1 
ATOM   103  C  CA  . TYR A 1 96  ? -5.14000  -5.80700  25.23300 1.000 18.73000 ? 96  TYR A CA  1 
ATOM   104  C  C   . TYR A 1 96  ? -5.28300  -6.14300  23.76100 1.000 17.91000 ? 96  TYR A C   1 
ATOM   105  O  O   . TYR A 1 96  ? -5.06300  -5.31200  23.01400 1.000 15.00000 ? 96  TYR A O   1 
ATOM   106  C  CB  . TYR A 1 96  ? -3.68800  -5.86100  25.70700 1.000 18.63000 ? 96  TYR A CB  1 
ATOM   107  C  CG  . TYR A 1 96  ? -3.36400  -4.89200  26.80100 1.000 22.78000 ? 96  TYR A CG  1 
ATOM   108  C  CD1 . TYR A 1 96  ? -4.01100  -4.97700  28.00200 1.000 24.88000 ? 96  TYR A CD1 1 
ATOM   109  C  CD2 . TYR A 1 96  ? -2.41800  -3.90500  26.64400 1.000 25.19000 ? 96  TYR A CD2 1 
ATOM   110  C  CE1 . TYR A 1 96  ? -3.76700  -4.10000  29.01900 1.000 26.18000 ? 96  TYR A CE1 1 
ATOM   111  C  CE2 . TYR A 1 96  ? -2.12100  -3.03300  27.66300 1.000 25.53000 ? 96  TYR A CE2 1 
ATOM   112  C  CZ  . TYR A 1 96  ? -2.80100  -3.14100  28.85700 1.000 34.04000 ? 96  TYR A CZ  1 
ATOM   113  O  OH  . TYR A 1 96  ? -2.56200  -2.31300  29.89800 1.000 44.60000 ? 96  TYR A OH  1 
ATOM   114  N  N   . GLU A 1 97  ? -5.53500  -7.40600  23.44200 1.000 24.45000 ? 97  GLU A N   1 
ATOM   115  C  CA  . GLU A 1 97  ? -5.68700  -7.89000  22.04200 1.000 22.42000 ? 97  GLU A CA  1 
ATOM   116  C  C   . GLU A 1 97  ? -6.88400  -7.19100  21.36600 1.000 20.40000 ? 97  GLU A C   1 
ATOM   117  O  O   . GLU A 1 97  ? -6.72300  -6.71900  20.30200 1.000 18.41000 ? 97  GLU A O   1 
ATOM   118  C  CB  . GLU A 1 97  ? -5.69800  -9.41200  22.06500 1.000 21.13000 ? 97  GLU A CB  1 
ATOM   119  C  CG  . GLU A 1 97  ? -6.05400  -10.07600 20.77500 1.000 24.76000 ? 97  GLU A CG  1 
ATOM   120  C  CD  . GLU A 1 97  ? -5.89300  -11.60000 20.70800 1.000 31.98000 ? 97  GLU A CD  1 
ATOM   121  O  OE1 . GLU A 1 97  ? -6.81600  -12.33600 21.07600 1.000 24.59000 ? 97  GLU A OE1 1 
ATOM   122  O  OE2 . GLU A 1 97  ? -4.82900  -12.02000 20.29600 1.000 29.85000 ? 97  GLU A OE2 1 
ATOM   123  N  N   . LEU A 1 98  ? -8.00800  -7.09600  22.05700 1.000 20.45000 ? 98  LEU A N   1 
ATOM   124  C  CA  . LEU A 1 98  ? -9.22200  -6.38600  21.59800 1.000 19.94000 ? 98  LEU A CA  1 
ATOM   125  C  C   . LEU A 1 98  ? -8.95400  -4.88400  21.51900 1.000 20.62000 ? 98  LEU A C   1 
ATOM   126  O  O   . LEU A 1 98  ? -9.33200  -4.28800  20.55000 1.000 21.02000 ? 98  LEU A O   1 
ATOM   127  C  CB  . LEU A 1 98  ? -10.37800 -6.67100  22.54500 1.000 17.92000 ? 98  LEU A CB  1 
ATOM   128  C  CG  . LEU A 1 98  ? -11.61300 -5.83700  22.26900 1.000 19.96000 ? 98  LEU A CG  1 
ATOM   129  C  CD1 . LEU A 1 98  ? -11.98200 -5.90500  20.82800 1.000 17.95000 ? 98  LEU A CD1 1 
ATOM   130  C  CD2 . LEU A 1 98  ? -12.77900 -6.21500  23.14200 1.000 20.41000 ? 98  LEU A CD2 1 
ATOM   131  N  N   . ARG A 1 99  ? -8.25500  -4.35200  22.50900 1.000 19.24000 ? 99  ARG A N   1 
ATOM   132  C  CA  . ARG A 1 99  ? -7.88500  -2.93000  22.56600 1.000 19.68000 ? 99  ARG A CA  1 
ATOM   133  C  C   . ARG A 1 99  ? -6.95800  -2.63900  21.40100 1.000 21.54000 ? 99  ARG A C   1 
ATOM   134  O  O   . ARG A 1 99  ? -7.17500  -1.63800  20.78900 1.000 21.52000 ? 99  ARG A O   1 
ATOM   135  C  CB  . ARG A 1 99  ? -7.36600  -2.51800  23.94500 1.000 20.72000 ? 99  ARG A CB  1 
ATOM   136  C  CG  . ARG A 1 99  ? -7.05800  -1.03700  24.12100 1.000 26.77000 ? 99  ARG A CG  1 
ATOM   137  C  CD  . ARG A 1 99  ? -8.18100  -0.03700  24.29700 1.000 26.07000 ? 99  ARG A CD  1 
ATOM   138  N  NE  . ARG A 1 99  ? -7.65600  1.31000   24.32300 1.000 31.69000 ? 99  ARG A NE  1 
ATOM   139  C  CZ  . ARG A 1 99  ? -7.19600  1.97600   25.37200 1.000 35.19000 ? 99  ARG A CZ  1 
ATOM   140  N  NH1 . ARG A 1 99  ? -7.21400  1.44700   26.56900 1.000 32.78000 ? 99  ARG A NH1 1 
ATOM   141  N  NH2 . ARG A 1 99  ? -6.70100  3.18800   25.20400 1.000 31.83000 ? 99  ARG A NH2 1 
ATOM   142  N  N   . MET A 1 100 ? -6.05900  -3.55700  21.06500 1.000 16.29000 ? 100 MET A N   1 
ATOM   143  C  CA  . MET A 1 100 ? -5.09200  -3.34300  19.98700 1.000 16.05000 ? 100 MET A CA  1 
ATOM   144  C  C   . MET A 1 100 ? -5.79700  -3.11900  18.66200 1.000 18.67000 ? 100 MET A C   1 
ATOM   145  O  O   . MET A 1 100 ? -5.50200  -2.15500  18.04500 1.000 16.04000 ? 100 MET A O   1 
ATOM   146  C  CB  . MET A 1 100 ? -4.17000  -4.54600  19.90300 1.000 17.11000 ? 100 MET A CB  1 
ATOM   147  C  CG  . MET A 1 100 ? -3.21700  -4.56300  18.78000 1.000 18.14000 ? 100 MET A CG  1 
ATOM   148  S  SD  . MET A 1 100 ? -2.03400  -5.85900  19.08100 1.000 30.44000 ? 100 MET A SD  1 
ATOM   149  C  CE  . MET A 1 100 ? -2.67900  -7.15100  18.04700 1.000 25.38000 ? 100 MET A CE  1 
ATOM   150  N  N   . GLU A 1 101 ? -6.75800  -3.96500  18.33800 1.000 16.47000 ? 101 GLU A N   1 
ATOM   151  C  CA  . GLU A 1 101 ? -7.55500  -3.88300  17.10300 1.000 16.48000 ? 101 GLU A CA  1 
ATOM   152  C  C   . GLU A 1 101 ? -8.38000  -2.60800  17.06900 1.000 18.22000 ? 101 GLU A C   1 
ATOM   153  O  O   . GLU A 1 101 ? -8.38400  -2.02900  16.05300 1.000 20.44000 ? 101 GLU A O   1 
ATOM   154  C  CB  . GLU A 1 101 ? -8.51000  -5.06900  17.03600 1.000 24.57000 ? 101 GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 101 ? -8.93500  -5.40800  15.65500 1.000 29.85000 ? 101 GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 101 ? -7.82700  -5.48500  14.62500 1.000 36.08000 ? 101 GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 101 ? -8.02400  -4.94700  13.52200 1.000 40.52000 ? 101 GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 101 ? -6.81200  -6.07600  14.91900 1.000 30.97000 ? 101 GLU A OE2 1 
ATOM   159  N  N   . LEU A 1 102 ? -9.03300  -2.23300  18.16500 1.000 17.13000 ? 102 LEU A N   1 
ATOM   160  C  CA  . LEU A 1 102 ? -9.86300  -0.99700  18.22900 1.000 21.80000 ? 102 LEU A CA  1 
ATOM   161  C  C   . LEU A 1 102 ? -9.03000  0.28600   18.04100 1.000 20.01000 ? 102 LEU A C   1 
ATOM   162  O  O   . LEU A 1 102 ? -9.46700  1.12700   17.32100 1.000 16.60000 ? 102 LEU A O   1 
ATOM   163  C  CB  . LEU A 1 102 ? -10.70500 -0.97300  19.50800 1.000 24.40000 ? 102 LEU A CB  1 
ATOM   164  C  CG  . LEU A 1 102 ? -11.91300 -1.91000  19.54800 1.000 20.46000 ? 102 LEU A CG  1 
ATOM   165  C  CD1 . LEU A 1 102 ? -12.40900 -2.08800  20.94000 1.000 19.08000 ? 102 LEU A CD1 1 
ATOM   166  C  CD2 . LEU A 1 102 ? -13.04200 -1.47300  18.64400 1.000 16.67000 ? 102 LEU A CD2 1 
ATOM   167  N  N   . GLU A 1 103 ? -7.84200  0.35300   18.64200 1.000 19.27000 ? 103 GLU A N   1 
ATOM   168  C  CA  . GLU A 1 103 ? -6.88100  1.48800   18.55300 1.000 22.27000 ? 103 GLU A CA  1 
ATOM   169  C  C   . GLU A 1 103 ? -6.37100  1.66800   17.12300 1.000 21.80000 ? 103 GLU A C   1 
ATOM   170  O  O   . GLU A 1 103 ? -6.27900  2.76700   16.71200 1.000 19.69000 ? 103 GLU A O   1 
ATOM   171  C  CB  . GLU A 1 103 ? -5.73600  1.34300   19.55200 1.000 20.55000 ? 103 GLU A CB  1 
ATOM   172  C  CG  . GLU A 1 103 ? -6.13600  1.52400   20.98500 1.000 22.62000 ? 103 GLU A CG  1 
ATOM   173  C  CD  . GLU A 1 103 ? -6.21600  2.92500   21.55000 1.000 30.65000 ? 103 GLU A CD  1 
ATOM   174  O  OE1 . GLU A 1 103 ? -6.83800  3.07400   22.55600 1.000 28.34000 ? 103 GLU A OE1 1 
ATOM   175  O  OE2 . GLU A 1 103 ? -5.64000  3.82500   20.99300 1.000 30.76000 ? 103 GLU A OE2 1 
ATOM   176  N  N   . GLY A 1 104 ? -6.08900  0.56800   16.43000 1.000 18.94000 ? 104 GLY A N   1 
ATOM   177  C  CA  . GLY A 1 104 ? -5.66900  0.55800   15.02100 1.000 17.99000 ? 104 GLY A CA  1 
ATOM   178  C  C   . GLY A 1 104 ? -6.73500  1.12100   14.09500 1.000 24.52000 ? 104 GLY A C   1 
ATOM   179  O  O   . GLY A 1 104 ? -6.40000  1.85300   13.20200 1.000 18.83000 ? 104 GLY A O   1 
ATOM   180  N  N   . GLY A 1 105 ? -7.98900  0.72900   14.31500 1.000 24.16000 ? 105 GLY A N   1 
ATOM   181  C  CA  . GLY A 1 105 ? -9.12900  1.26400   13.56000 1.000 23.08000 ? 105 GLY A CA  1 
ATOM   182  C  C   . GLY A 1 105 ? -9.32700  2.73500   13.85400 1.000 23.58000 ? 105 GLY A C   1 
ATOM   183  O  O   . GLY A 1 105 ? -9.57300  3.44800   12.97000 1.000 24.75000 ? 105 GLY A O   1 
ATOM   184  N  N   . ALA A 1 106 ? -9.20300  3.12000   15.11000 1.000 24.53000 ? 106 ALA A N   1 
ATOM   185  C  CA  . ALA A 1 106 ? -9.35100  4.52600   15.52200 1.000 23.87000 ? 106 ALA A CA  1 
ATOM   186  C  C   . ALA A 1 106 ? -8.23000  5.36000   14.91200 1.000 24.08000 ? 106 ALA A C   1 
ATOM   187  O  O   . ALA A 1 106 ? -8.53800  6.34900   14.40800 1.000 25.60000 ? 106 ALA A O   1 
ATOM   188  C  CB  . ALA A 1 106 ? -9.41700  4.67000   17.00900 1.000 19.84000 ? 106 ALA A CB  1 
ATOM   189  N  N   . ALA A 1 107 ? -6.99800  4.88300   14.90000 1.000 23.54000 ? 107 ALA A N   1 
ATOM   190  C  CA  . ALA A 1 107 ? -5.91100  5.69500   14.32600 1.000 27.97000 ? 107 ALA A CA  1 
ATOM   191  C  C   . ALA A 1 107 ? -6.08900  5.91700   12.82500 1.000 25.92000 ? 107 ALA A C   1 
ATOM   192  O  O   . ALA A 1 107 ? -5.72100  6.95100   12.37700 1.000 24.79000 ? 107 ALA A O   1 
ATOM   193  C  CB  . ALA A 1 107 ? -4.55900  5.17100   14.68800 1.000 24.44000 ? 107 ALA A CB  1 
ATOM   194  N  N   . ALA A 1 108 ? -6.52200  4.89600   12.10500 1.000 25.34000 ? 108 ALA A N   1 
ATOM   195  C  CA  . ALA A 1 108 ? -6.79600  4.97400   10.66600 1.000 24.98000 ? 108 ALA A CA  1 
ATOM   196  C  C   . ALA A 1 108 ? -7.95200  5.92000   10.39900 1.000 25.64000 ? 108 ALA A C   1 
ATOM   197  O  O   . ALA A 1 108 ? -7.85500  6.68300   9.52800  1.000 29.62000 ? 108 ALA A O   1 
ATOM   198  C  CB  . ALA A 1 108 ? -7.09200  3.61200   10.12800 1.000 25.98000 ? 108 ALA A CB  1 
ATOM   199  N  N   . LEU A 1 109 ? -9.00900  5.82800   11.16800 1.000 24.93000 ? 109 LEU A N   1 
ATOM   200  C  CA  . LEU A 1 109 ? -10.13700 6.74700   10.95500 1.000 26.88000 ? 109 LEU A CA  1 
ATOM   201  C  C   . LEU A 1 109 ? -9.67900  8.16900   11.26600 1.000 27.33000 ? 109 LEU A C   1 
ATOM   202  O  O   . LEU A 1 109 ? -9.94800  9.03000   10.47400 1.000 31.08000 ? 109 LEU A O   1 
ATOM   203  C  CB  . LEU A 1 109 ? -11.34400 6.32900   11.79800 1.000 25.68000 ? 109 LEU A CB  1 
ATOM   204  C  CG  . LEU A 1 109 ? -11.99600 5.00300   11.42100 1.000 30.47000 ? 109 LEU A CG  1 
ATOM   205  C  CD1 . LEU A 1 109 ? -13.25800 4.80200   12.20100 1.000 30.28000 ? 109 LEU A CD1 1 
ATOM   206  C  CD2 . LEU A 1 109 ? -12.32300 4.93700   9.95100  1.000 28.38000 ? 109 LEU A CD2 1 
ATOM   207  N  N   . ALA A 1 110 ? -8.94200  8.33600   12.35100 1.000 25.71000 ? 110 ALA A N   1 
ATOM   208  C  CA  . ALA A 1 110 ? -8.46800  9.65300   12.78700 1.000 26.06000 ? 110 ALA A CA  1 
ATOM   209  C  C   . ALA A 1 110 ? -7.53100  10.22800  11.74200 1.000 26.86000 ? 110 ALA A C   1 
ATOM   210  O  O   . ALA A 1 110 ? -7.69300  11.33700  11.45100 1.000 30.51000 ? 110 ALA A O   1 
ATOM   211  C  CB  . ALA A 1 110 ? -7.80900  9.55800   14.11600 1.000 25.45000 ? 110 ALA A CB  1 
ATOM   212  N  N   . ALA A 1 111 ? -6.68400  9.42300   11.14300 1.000 25.36000 ? 111 ALA A N   1 
ATOM   213  C  CA  . ALA A 1 111 ? -5.72500  9.92500   10.14900 1.000 30.57000 ? 111 ALA A CA  1 
ATOM   214  C  C   . ALA A 1 111 ? -6.47000  10.55900  8.98400  1.000 31.31000 ? 111 ALA A C   1 
ATOM   215  O  O   . ALA A 1 111 ? -5.99300  11.52800  8.49700  1.000 29.26000 ? 111 ALA A O   1 
ATOM   216  C  CB  . ALA A 1 111 ? -4.85900  8.79400   9.65100  1.000 32.11000 ? 111 ALA A CB  1 
ATOM   217  N  N   . ARG A 1 112 ? -7.51300  9.90400   8.49500  1.000 34.41000 ? 112 ARG A N   1 
ATOM   218  C  CA  . ARG A 1 112 ? -8.37100  10.41700  7.40200  1.000 29.90000 ? 112 ARG A CA  1 
ATOM   219  C  C   . ARG A 1 112 ? -9.28600  11.57600  7.80200  1.000 29.66000 ? 112 ARG A C   1 
ATOM   220  O  O   . ARG A 1 112 ? -9.45100  12.43300  7.03200  1.000 35.84000 ? 112 ARG A O   1 
ATOM   221  C  CB  . ARG A 1 112 ? -9.26200  9.30600   6.86500  1.000 32.45000 ? 112 ARG A CB  1 
ATOM   222  N  N   . ARG A 1 113 ? -9.88000  11.57900  8.97200  1.000 31.14000 ? 113 ARG A N   1 
ATOM   223  C  CA  . ARG A 1 113 ? -10.92400 12.59600  9.21300  1.000 29.55000 ? 113 ARG A CA  1 
ATOM   224  C  C   . ARG A 1 113 ? -10.54200 13.65200  10.23600 1.000 33.29000 ? 113 ARG A C   1 
ATOM   225  O  O   . ARG A 1 113 ? -11.40900 14.41800  10.55400 1.000 33.37000 ? 113 ARG A O   1 
ATOM   226  C  CB  . ARG A 1 113 ? -12.20600 11.90900  9.69100  1.000 31.42000 ? 113 ARG A CB  1 
ATOM   227  C  CG  . ARG A 1 113 ? -12.58200 10.65700  8.91300  1.000 35.18000 ? 113 ARG A CG  1 
ATOM   228  C  CD  . ARG A 1 113 ? -13.84700 10.05700  9.49400  1.000 36.65000 ? 113 ARG A CD  1 
ATOM   229  N  NE  . ARG A 1 113 ? -14.47500 9.02700   8.69300  1.000 43.72000 ? 113 ARG A NE  1 
ATOM   230  C  CZ  . ARG A 1 113 ? -15.16200 8.00400   9.16500  1.000 35.71000 ? 113 ARG A CZ  1 
ATOM   231  N  NH1 . ARG A 1 113 ? -15.67800 7.14300   8.33200  1.000 37.62000 ? 113 ARG A NH1 1 
ATOM   232  N  NH2 . ARG A 1 113 ? -15.30700 7.81700   10.45000 1.000 30.61000 ? 113 ARG A NH2 1 
ATOM   233  N  N   . ARG A 1 114 ? -9.30500  13.69800  10.71800 1.000 30.02000 ? 114 ARG A N   1 
ATOM   234  C  CA  . ARG A 1 114 ? -8.97800  14.68800  11.77600 1.000 33.31000 ? 114 ARG A CA  1 
ATOM   235  C  C   . ARG A 1 114 ? -9.11200  16.11900  11.25500 1.000 26.31000 ? 114 ARG A C   1 
ATOM   236  O  O   . ARG A 1 114 ? -8.63000  16.40700  10.21900 1.000 28.11000 ? 114 ARG A O   1 
ATOM   237  C  CB  . ARG A 1 114 ? -7.59000  14.45100  12.35900 1.000 27.16000 ? 114 ARG A CB  1 
ATOM   238  C  CG  . ARG A 1 114 ? -6.54700  14.31900  11.27400 1.000 30.28000 ? 114 ARG A CG  1 
ATOM   239  C  CD  . ARG A 1 114 ? -5.53700  15.36500  11.43200 1.000 32.33000 ? 114 ARG A CD  1 
ATOM   240  N  NE  . ARG A 1 114 ? -4.61500  15.37500  10.32200 1.000 41.79000 ? 114 ARG A NE  1 
ATOM   241  C  CZ  . ARG A 1 114 ? -4.78700  16.11800  9.25800  1.000 40.25000 ? 114 ARG A CZ  1 
ATOM   242  N  NH1 . ARG A 1 114 ? -5.89100  16.82000  9.12300  1.000 30.98000 ? 114 ARG A NH1 1 
ATOM   243  N  NH2 . ARG A 1 114 ? -3.87300  16.13400  8.33100  1.000 36.81000 ? 114 ARG A NH2 1 
ATOM   244  N  N   . ASN A 1 115 ? -9.68500  16.97200  12.07000 1.000 26.50000 ? 115 ASN A N   1 
ATOM   245  C  CA  . ASN A 1 115 ? -9.89600  18.40400  11.74800 1.000 29.02000 ? 115 ASN A CA  1 
ATOM   246  C  C   . ASN A 1 115 ? -9.07500  19.25400  12.71900 1.000 30.16000 ? 115 ASN A C   1 
ATOM   247  O  O   . ASN A 1 115 ? -8.61100  18.72700  13.71400 1.000 31.80000 ? 115 ASN A O   1 
ATOM   248  C  CB  . ASN A 1 115 ? -11.37400 18.73700  11.59100 1.000 23.18000 ? 115 ASN A CB  1 
ATOM   249  C  CG  . ASN A 1 115 ? -12.10600 18.82800  12.89900 1.000 32.69000 ? 115 ASN A CG  1 
ATOM   250  O  OD1 . ASN A 1 115 ? -11.49100 18.95800  13.92600 1.000 35.74000 ? 115 ASN A OD1 1 
ATOM   251  N  ND2 . ASN A 1 115 ? -13.41500 18.77500  12.88000 1.000 29.20000 ? 115 ASN A ND2 1 
ATOM   252  N  N   . ALA A 1 116 ? -9.05400  20.56100  12.53600 1.000 30.75000 ? 116 ALA A N   1 
ATOM   253  C  CA  . ALA A 1 116 ? -8.18900  21.46300  13.32700 1.000 30.46000 ? 116 ALA A CA  1 
ATOM   254  C  C   . ALA A 1 116 ? -8.42600  21.31800  14.82200 1.000 28.29000 ? 116 ALA A C   1 
ATOM   255  O  O   . ALA A 1 116 ? -7.48300  21.33400  15.54500 1.000 31.05000 ? 116 ALA A O   1 
ATOM   256  C  CB  . ALA A 1 116 ? -8.39200  22.88100  12.88200 1.000 35.74000 ? 116 ALA A CB  1 
ATOM   257  N  N   . THR A 1 117 ? -9.65600  21.15400  15.23700 1.000 30.48000 ? 117 THR A N   1 
ATOM   258  C  CA  . THR A 1 117 ? -9.93500  20.96100  16.68200 1.000 32.26000 ? 117 THR A CA  1 
ATOM   259  C  C   . THR A 1 117 ? -9.33200  19.64500  17.21200 1.000 32.57000 ? 117 THR A C   1 
ATOM   260  O  O   . THR A 1 117 ? -8.82600  19.66400  18.32200 1.000 32.53000 ? 117 THR A O   1 
ATOM   261  C  CB  . THR A 1 117 ? -11.44500 21.02900  16.89600 1.000 31.06000 ? 117 THR A CB  1 
ATOM   262  O  OG1 . THR A 1 117 ? -11.82200 22.25300  16.28200 1.000 40.39000 ? 117 THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 117 ? -11.86100 21.02600  18.34000 1.000 26.31000 ? 117 THR A CG2 1 
ATOM   264  N  N   . ASP A 1 118 ? -9.33700  18.56300  16.44100 1.000 26.21000 ? 118 ASP A N   1 
ATOM   265  C  CA  . ASP A 1 118 ? -8.75900  17.26400  16.86500 1.000 28.39000 ? 118 ASP A CA  1 
ATOM   266  C  C   . ASP A 1 118 ? -7.23700  17.37600  17.01800 1.000 30.07000 ? 118 ASP A C   1 
ATOM   267  O  O   . ASP A 1 118 ? -6.70600  16.89100  17.97700 1.000 29.80000 ? 118 ASP A O   1 
ATOM   268  C  CB  . ASP A 1 118 ? -9.13800  16.15100  15.88800 1.000 23.86000 ? 118 ASP A CB  1 
ATOM   269  C  CG  . ASP A 1 118 ? -10.62000 15.84200  15.73700 1.000 29.22000 ? 118 ASP A CG  1 
ATOM   270  O  OD1 . ASP A 1 118 ? -11.24900 15.51900  16.71100 1.000 30.84000 ? 118 ASP A OD1 1 
ATOM   271  O  OD2 . ASP A 1 118 ? -11.10800 15.91000  14.64000 1.000 28.66000 ? 118 ASP A OD2 1 
ATOM   272  N  N   . LEU A 1 119 ? -6.58800  18.04600  16.08100 1.000 29.22000 ? 119 LEU A N   1 
ATOM   273  C  CA  . LEU A 1 119 ? -5.12800  18.23100  16.12000 1.000 30.58000 ? 119 LEU A CA  1 
ATOM   274  C  C   . LEU A 1 119 ? -4.74900  19.00200  17.38500 1.000 26.59000 ? 119 LEU A C   1 
ATOM   275  O  O   . LEU A 1 119 ? -3.88300  18.57600  18.03100 1.000 23.92000 ? 119 LEU A O   1 
ATOM   276  C  CB  . LEU A 1 119 ? -4.69200  18.93900  14.84400 1.000 33.55000 ? 119 LEU A CB  1 
ATOM   277  C  CG  . LEU A 1 119 ? -4.72200  18.08400  13.58800 1.000 34.38000 ? 119 LEU A CG  1 
ATOM   278  C  CD1 . LEU A 1 119 ? -4.31300  18.89200  12.38100 1.000 30.32000 ? 119 LEU A CD1 1 
ATOM   279  C  CD2 . LEU A 1 119 ? -3.83700  16.86700  13.72000 1.000 29.70000 ? 119 LEU A CD2 1 
ATOM   280  N  N   . ALA A 1 120 ? -5.49700  20.02000  17.76300 1.000 25.52000 ? 120 ALA A N   1 
ATOM   281  C  CA  . ALA A 1 120 ? -5.17400  20.75200  18.99700 1.000 28.49000 ? 120 ALA A CA  1 
ATOM   282  C  C   . ALA A 1 120 ? -5.26600  19.85900  20.24200 1.000 29.02000 ? 120 ALA A C   1 
ATOM   283  O  O   . ALA A 1 120 ? -4.41100  19.92900  21.06700 1.000 27.57000 ? 120 ALA A O   1 
ATOM   284  C  CB  . ALA A 1 120 ? -6.09100  21.93500  19.10600 1.000 31.00000 ? 120 ALA A CB  1 
ATOM   285  N  N   . ALA A 1 121 ? -6.31100  19.06100  20.35500 1.000 27.29000 ? 121 ALA A N   1 
ATOM   286  C  CA  . ALA A 1 121 ? -6.48600  18.17400  21.51200 1.000 28.34000 ? 121 ALA A CA  1 
ATOM   287  C  C   . ALA A 1 121 ? -5.37700  17.10600  21.58800 1.000 23.39000 ? 121 ALA A C   1 
ATOM   288  O  O   . ALA A 1 121 ? -4.94600  16.85000  22.62100 1.000 21.86000 ? 121 ALA A O   1 
ATOM   289  C  CB  . ALA A 1 121 ? -7.88500  17.62000  21.47500 1.000 29.75000 ? 121 ALA A CB  1 
ATOM   290  N  N   . MET A 1 122 ? -4.97200  16.50900  20.48700 1.000 24.76000 ? 122 MET A N   1 
ATOM   291  C  CA  . MET A 1 122 ? -3.86000  15.54100  20.51500 1.000 24.02000 ? 122 MET A CA  1 
ATOM   292  C  C   . MET A 1 122 ? -2.54400  16.23700  20.87800 1.000 24.77000 ? 122 MET A C   1 
ATOM   293  O  O   . MET A 1 122 ? -1.88500  15.76300  21.70900 1.000 22.95000 ? 122 MET A O   1 
ATOM   294  C  CB  . MET A 1 122 ? -3.68100  14.87300  19.16100 1.000 24.16000 ? 122 MET A CB  1 
ATOM   295  C  CG  . MET A 1 122 ? -4.87800  14.16200  18.65400 1.000 27.74000 ? 122 MET A CG  1 
ATOM   296  S  SD  . MET A 1 122 ? -4.56400  13.33500  17.12500 1.000 40.31000 ? 122 MET A SD  1 
ATOM   297  C  CE  . MET A 1 122 ? -2.93400  12.68500  17.44700 1.000 28.66000 ? 122 MET A CE  1 
ATOM   298  N  N   . ALA A 1 123 ? -2.25200  17.38500  20.28600 1.000 24.75000 ? 123 ALA A N   1 
ATOM   299  C  CA  . ALA A 1 123 ? -1.00000  18.11600  20.53900 1.000 22.28000 ? 123 ALA A CA  1 
ATOM   300  C  C   . ALA A 1 123 ? -0.88600  18.54500  21.99500 1.000 20.99000 ? 123 ALA A C   1 
ATOM   301  O  O   . ALA A 1 123 ? 0.13400   18.35600  22.56000 1.000 23.08000 ? 123 ALA A O   1 
ATOM   302  C  CB  . ALA A 1 123 ? -0.92700  19.27900  19.61500 1.000 22.13000 ? 123 ALA A CB  1 
ATOM   303  N  N   . GLU A 1 124 ? -1.95800  19.04900  22.57100 1.000 23.77000 ? 124 GLU A N   1 
ATOM   304  C  CA  . GLU A 1 124 ? -1.99300  19.49400  23.98100 1.000 24.80000 ? 124 GLU A CA  1 
ATOM   305  C  C   . GLU A 1 124 ? -1.75000  18.31900  24.93200 1.000 23.07000 ? 124 GLU A C   1 
ATOM   306  O  O   . GLU A 1 124 ? -1.00000  18.49100  25.83700 1.000 24.82000 ? 124 GLU A O   1 
ATOM   307  C  CB  . GLU A 1 124 ? -3.28800  20.26500  24.22000 1.000 23.32000 ? 124 GLU A CB  1 
ATOM   308  C  CG  . GLU A 1 124 ? -3.79300  20.25800  25.62700 1.000 28.31000 ? 124 GLU A CG  1 
ATOM   309  C  CD  . GLU A 1 124 ? -5.06500  21.04200  25.91200 1.000 40.95000 ? 124 GLU A CD  1 
ATOM   310  O  OE1 . GLU A 1 124 ? -5.96300  20.52000  26.54300 1.000 41.41000 ? 124 GLU A OE1 1 
ATOM   311  O  OE2 . GLU A 1 124 ? -5.11400  22.19300  25.54300 1.000 51.03000 ? 124 GLU A OE2 1 
ATOM   312  N  N   . ALA A 1 125 ? -2.39000  17.18000  24.71100 1.000 21.03000 ? 125 ALA A N   1 
ATOM   313  C  CA  . ALA A 1 125 ? -2.16600  16.01600  25.57900 1.000 21.28000 ? 125 ALA A CA  1 
ATOM   314  C  C   . ALA A 1 125 ? -0.73000  15.55800  25.40700 1.000 20.87000 ? 125 ALA A C   1 
ATOM   315  O  O   . ALA A 1 125 ? -0.15000  15.25500  26.35300 1.000 23.94000 ? 125 ALA A O   1 
ATOM   316  C  CB  . ALA A 1 125 ? -3.11200  14.90900  25.24300 1.000 21.42000 ? 125 ALA A CB  1 
ATOM   317  N  N   . LEU A 1 126 ? -0.23200  15.54500  24.18300 1.000 22.44000 ? 126 LEU A N   1 
ATOM   318  C  CA  . LEU A 1 126 ? 1.15000   15.08700  23.90800 1.000 23.70000 ? 126 LEU A CA  1 
ATOM   319  C  C   . LEU A 1 126 ? 2.15900   16.02100  24.57200 1.000 26.38000 ? 126 LEU A C   1 
ATOM   320  O  O   . LEU A 1 126 ? 3.06700   15.53400  25.15500 1.000 22.44000 ? 126 LEU A O   1 
ATOM   321  C  CB  . LEU A 1 126 ? 1.38600   14.92900  22.41400 1.000 22.41000 ? 126 LEU A CB  1 
ATOM   322  C  CG  . LEU A 1 126 ? 2.47700   13.93500  22.05900 1.000 25.02000 ? 126 LEU A CG  1 
ATOM   323  C  CD1 . LEU A 1 126 ? 2.07000   12.56100  22.45600 1.000 18.27000 ? 126 LEU A CD1 1 
ATOM   324  C  CD2 . LEU A 1 126 ? 2.82100   13.96000  20.59800 1.000 25.37000 ? 126 LEU A CD2 1 
ATOM   325  N  N   . ALA A 1 127 ? 1.91700   17.31800  24.52300 1.000 22.90000 ? 127 ALA A N   1 
ATOM   326  C  CA  . ALA A 1 127 ? 2.81400   18.28700  25.16100 1.000 23.46000 ? 127 ALA A CA  1 
ATOM   327  C  C   . ALA A 1 127 ? 2.84000   17.99600  26.64300 1.000 23.38000 ? 127 ALA A C   1 
ATOM   328  O  O   . ALA A 1 127 ? 3.88400   17.92700  27.12700 1.000 25.22000 ? 127 ALA A O   1 
ATOM   329  C  CB  . ALA A 1 127 ? 2.30800   19.67000  24.93300 1.000 17.34000 ? 127 ALA A CB  1 
ATOM   330  N  N   . ALA A 1 128 ? 1.69300   17.76300  27.26400 1.000 23.13000 ? 128 ALA A N   1 
ATOM   331  C  CA  . ALA A 1 128 ? 1.62200   17.44900  28.70000 1.000 22.90000 ? 128 ALA A CA  1 
ATOM   332  C  C   . ALA A 1 128 ? 2.35500   16.13900  29.05300 1.000 28.45000 ? 128 ALA A C   1 
ATOM   333  O  O   . ALA A 1 128 ? 2.98100   16.11700  30.07600 1.000 25.19000 ? 128 ALA A O   1 
ATOM   334  C  CB  . ALA A 1 128 ? 0.18900   17.42400  29.12600 1.000 26.97000 ? 128 ALA A CB  1 
ATOM   335  N  N   . LEU A 1 129 ? 2.21300   15.09900  28.23900 1.000 21.38000 ? 129 LEU A N   1 
ATOM   336  C  CA  . LEU A 1 129 ? 2.94700   13.82600  28.43200 1.000 26.22000 ? 129 LEU A CA  1 
ATOM   337  C  C   . LEU A 1 129 ? 4.46000   14.09000  28.30700 1.000 25.53000 ? 129 LEU A C   1 
ATOM   338  O  O   . LEU A 1 129 ? 5.18500   13.55700  29.09300 1.000 20.56000 ? 129 LEU A O   1 
ATOM   339  C  CB  . LEU A 1 129 ? 2.48900   12.81100  27.37600 1.000 18.64000 ? 129 LEU A CB  1 
ATOM   340  C  CG  . LEU A 1 129 ? 1.15400   12.11300  27.60700 1.000 23.19000 ? 129 LEU A CG  1 
ATOM   341  C  CD1 . LEU A 1 129 ? 0.79600   11.19400  26.45900 1.000 21.19000 ? 129 LEU A CD1 1 
ATOM   342  C  CD2 . LEU A 1 129 ? 1.12700   11.35400  28.90700 1.000 24.73000 ? 129 LEU A CD2 1 
ATOM   343  N  N   . GLU A 1 130 ? 4.84600   14.93300  27.35000 1.000 23.68000 ? 130 GLU A N   1 
ATOM   344  C  CA  . GLU A 1 130 ? 6.25200   15.28200  27.05500 1.000 26.96000 ? 130 GLU A CA  1 
ATOM   345  C  C   . GLU A 1 130 ? 6.87400   15.97900  28.26400 1.000 26.47000 ? 130 GLU A C   1 
ATOM   346  O  O   . GLU A 1 130 ? 7.96700   15.61900  28.62200 1.000 26.95000 ? 130 GLU A O   1 
ATOM   347  C  CB  . GLU A 1 130 ? 6.35400   16.13800  25.79500 1.000 27.88000 ? 130 GLU A CB  1 
ATOM   348  C  CG  . GLU A 1 130 ? 7.72900   16.10900  25.15200 1.000 29.60000 ? 130 GLU A CG  1 
ATOM   349  C  CD  . GLU A 1 130 ? 7.75800   16.12100  23.64000 1.000 32.41000 ? 130 GLU A CD  1 
ATOM   350  O  OE1 . GLU A 1 130 ? 8.27200   17.04500  23.11400 1.000 28.36000 ? 130 GLU A OE1 1 
ATOM   351  O  OE2 . GLU A 1 130 ? 7.21700   15.19900  23.02200 1.000 26.77000 ? 130 GLU A OE2 1 
ATOM   352  N  N   . ALA A 1 131 ? 6.12000   16.87500  28.86400 1.000 24.83000 ? 131 ALA A N   1 
ATOM   353  C  CA  . ALA A 1 131 ? 6.53100   17.67700  30.02600 1.000 29.07000 ? 131 ALA A CA  1 
ATOM   354  C  C   . ALA A 1 131 ? 6.60000   16.86200  31.32100 1.000 31.91000 ? 131 ALA A C   1 
ATOM   355  O  O   . ALA A 1 131 ? 7.17300   17.33700  32.24800 1.000 31.40000 ? 131 ALA A O   1 
ATOM   356  C  CB  . ALA A 1 131 ? 5.57700   18.82200  30.16700 1.000 23.76000 ? 131 ALA A CB  1 
ATOM   357  N  N   . ASN A 1 132 ? 5.98100   15.69700  31.37100 1.000 30.07000 ? 132 ASN A N   1 
ATOM   358  C  CA  . ASN A 1 132 ? 5.89900   14.92200  32.63000 1.000 31.45000 ? 132 ASN A CA  1 
ATOM   359  C  C   . ASN A 1 132 ? 6.64000   13.60100  32.55000 1.000 27.74000 ? 132 ASN A C   1 
ATOM   360  O  O   . ASN A 1 132 ? 6.17900   12.69900  33.12400 1.000 26.39000 ? 132 ASN A O   1 
ATOM   361  C  CB  . ASN A 1 132 ? 4.45200   14.71300  33.06100 1.000 33.08000 ? 132 ASN A CB  1 
ATOM   362  C  CG  . ASN A 1 132 ? 3.92100   15.91400  33.80100 1.000 38.36000 ? 132 ASN A CG  1 
ATOM   363  O  OD1 . ASN A 1 132 ? 3.03300   16.59200  33.34700 1.000 35.67000 ? 132 ASN A OD1 1 
ATOM   364  N  ND2 . ASN A 1 132 ? 4.49200   16.20600  34.94200 1.000 40.84000 ? 132 ASN A ND2 1 
ATOM   365  N  N   . LEU A 1 133 ? 7.71400   13.53600  31.79600 1.000 25.05000 ? 133 LEU A N   1 
ATOM   366  C  CA  . LEU A 1 133 ? 8.51500   12.30900  31.63300 1.000 27.40000 ? 133 LEU A CA  1 
ATOM   367  C  C   . LEU A 1 133 ? 9.14900   11.87700  32.94800 1.000 32.66000 ? 133 LEU A C   1 
ATOM   368  O  O   . LEU A 1 133 ? 9.32900   10.70600  33.09300 1.000 31.93000 ? 133 LEU A O   1 
ATOM   369  C  CB  . LEU A 1 133 ? 9.56000   12.52700  30.55100 1.000 31.72000 ? 133 LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 133 ? 9.04200   12.49800  29.12800 1.000 27.90000 ? 133 LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 133 ? 10.10600  12.96300  28.17800 1.000 30.73000 ? 133 LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 133 ? 8.59600   11.12200  28.76400 1.000 30.25000 ? 133 LEU A CD2 1 
ATOM   373  N  N   . ASP A 1 134 ? 9.49800   12.81700  33.82900 1.000 31.13000 ? 134 ASP A N   1 
ATOM   374  C  CA  . ASP A 1 134 ? 10.07700  12.52700  35.15400 1.000 29.59000 ? 134 ASP A CA  1 
ATOM   375  C  C   . ASP A 1 134 ? 8.96800   12.31800  36.17600 1.000 36.30000 ? 134 ASP A C   1 
ATOM   376  O  O   . ASP A 1 134 ? 9.29500   12.03500  37.26900 1.000 39.33000 ? 134 ASP A O   1 
ATOM   377  C  CB  . ASP A 1 134 ? 10.90900  13.68900  35.68000 1.000 38.31000 ? 134 ASP A CB  1 
ATOM   378  C  CG  . ASP A 1 134 ? 11.93500  14.24100  34.73000 1.000 36.20000 ? 134 ASP A CG  1 
ATOM   379  O  OD1 . ASP A 1 134 ? 12.53600  13.47700  34.01800 1.000 36.36000 ? 134 ASP A OD1 1 
ATOM   380  O  OD2 . ASP A 1 134 ? 12.06100  15.41700  34.69700 1.000 34.86000 ? 134 ASP A OD2 1 
ATOM   381  N  N   . HIS A 1 135 ? 7.70400   12.48600  35.82600 1.000 34.25000 ? 135 HIS A N   1 
ATOM   382  C  CA  . HIS A 1 135 ? 6.62400   12.27400  36.81200 1.000 38.90000 ? 135 HIS A CA  1 
ATOM   383  C  C   . HIS A 1 135 ? 5.65200   11.23900  36.25700 1.000 41.95000 ? 135 HIS A C   1 
ATOM   384  O  O   . HIS A 1 135 ? 4.64200   11.64600  35.73300 1.000 44.72000 ? 135 HIS A O   1 
ATOM   385  C  CB  . HIS A 1 135 ? 5.86000   13.57300  37.04100 1.000 41.69000 ? 135 HIS A CB  1 
ATOM   386  C  CG  . HIS A 1 135 ? 6.62100   14.69300  37.66000 1.000 45.05000 ? 135 HIS A CG  1 
ATOM   387  N  ND1 . HIS A 1 135 ? 7.21800   15.67700  36.92100 1.000 47.53000 ? 135 HIS A ND1 1 
ATOM   388  C  CD2 . HIS A 1 135 ? 6.83000   15.02500  38.94400 1.000 46.82000 ? 135 HIS A CD2 1 
ATOM   389  C  CE1 . HIS A 1 135 ? 7.78400   16.53900  37.71200 1.000 43.76000 ? 135 HIS A CE1 1 
ATOM   390  N  NE2 . HIS A 1 135 ? 7.55700   16.16300  38.95100 1.000 45.56000 ? 135 HIS A NE2 1 
ATOM   391  N  N   . PRO A 1 136 ? 5.87400   9.91700   36.39700 1.000 42.92000 ? 136 PRO A N   1 
ATOM   392  C  CA  . PRO A 1 136 ? 4.99500   8.89700   35.81100 1.000 40.76000 ? 136 PRO A CA  1 
ATOM   393  C  C   . PRO A 1 136 ? 3.54600   8.91900   36.30900 1.000 42.45000 ? 136 PRO A C   1 
ATOM   394  O  O   . PRO A 1 136 ? 2.68900   8.60100   35.57000 1.000 37.34000 ? 136 PRO A O   1 
ATOM   395  C  CB  . PRO A 1 136 ? 5.69400   7.57800   36.10200 1.000 37.90000 ? 136 PRO A CB  1 
ATOM   396  C  CG  . PRO A 1 136 ? 6.58500   7.87400   37.25300 1.000 43.82000 ? 136 PRO A CG  1 
ATOM   397  C  CD  . PRO A 1 136 ? 7.02000   9.30000   37.05700 1.000 42.05000 ? 136 PRO A CD  1 
ATOM   398  N  N   . GLU A 1 137 ? 3.37100   9.36000   37.54500 1.000 43.01000 ? 137 GLU A N   1 
ATOM   399  C  CA  . GLU A 1 137 ? 2.09900   9.53500   38.24900 1.000 40.71000 ? 137 GLU A CA  1 
ATOM   400  C  C   . GLU A 1 137 ? 1.18700   10.51700  37.51400 1.000 45.84000 ? 137 GLU A C   1 
ATOM   401  O  O   . GLU A 1 137 ? 0.03400   10.17200  37.31100 1.000 47.33000 ? 137 GLU A O   1 
ATOM   402  C  CB  . GLU A 1 137 ? 2.43600   10.17400  39.60100 1.000 49.10000 ? 137 GLU A CB  1 
ATOM   403  C  CG  . GLU A 1 137 ? 3.58700   11.21000  39.61500 1.000 48.40000 ? 137 GLU A CG  1 
ATOM   404  C  CD  . GLU A 1 137 ? 4.91600   10.79200  40.19700 1.000 48.99000 ? 137 GLU A CD  1 
ATOM   405  O  OE1 . GLU A 1 137 ? 5.54600   11.61000  40.82000 1.000 48.49000 ? 137 GLU A OE1 1 
ATOM   406  O  OE2 . GLU A 1 137 ? 5.28300   9.64400   40.04900 1.000 50.65000 ? 137 GLU A OE2 1 
ATOM   407  N  N   . GLN A 1 138 ? 1.71300   11.65100  37.06500 1.000 40.15000 ? 138 GLN A N   1 
ATOM   408  C  CA  . GLN A 1 138 ? 0.91400   12.73500  36.45400 1.000 44.07000 ? 138 GLN A CA  1 
ATOM   409  C  C   . GLN A 1 138 ? 0.55700   12.38200  35.02400 1.000 43.10000 ? 138 GLN A C   1 
ATOM   410  O  O   . GLN A 1 138 ? -0.41100  12.89200  34.52000 1.000 40.16000 ? 138 GLN A O   1 
ATOM   411  C  CB  . GLN A 1 138 ? 1.68400   14.04300  36.52400 1.000 43.44000 ? 138 GLN A CB  1 
ATOM   412  C  CG  . GLN A 1 138 ? 0.83400   15.28500  36.64700 1.000 44.36000 ? 138 GLN A CG  1 
ATOM   413  C  CD  . GLN A 1 138 ? 1.64500   16.40700  36.06100 1.000 48.46000 ? 138 GLN A CD  1 
ATOM   414  O  OE1 . GLN A 1 138 ? 2.75400   16.69000  36.49800 1.000 44.64000 ? 138 GLN A OE1 1 
ATOM   415  N  NE2 . GLN A 1 138 ? 1.10700   17.02800  35.03400 1.000 49.48000 ? 138 GLN A NE2 1 
ATOM   416  N  N   . GLY A 1 139 ? 1.34700   11.49000  34.47000 1.000 40.91000 ? 139 GLY A N   1 
ATOM   417  C  CA  . GLY A 1 139 ? 1.24200   11.07500  33.07800 1.000 40.92000 ? 139 GLY A CA  1 
ATOM   418  C  C   . GLY A 1 139 ? -0.05700  10.38800  32.75000 1.000 36.54000 ? 139 GLY A C   1 
ATOM   419  O  O   . GLY A 1 139 ? -0.59300  10.71900  31.73400 1.000 34.90000 ? 139 GLY A O   1 
ATOM   420  N  N   . VAL A 1 140 ? -0.59500  9.58900   33.65300 1.000 33.78000 ? 140 VAL A N   1 
ATOM   421  C  CA  . VAL A 1 140 ? -1.79700  8.75400   33.38000 1.000 34.87000 ? 140 VAL A CA  1 
ATOM   422  C  C   . VAL A 1 140 ? -2.95000  9.58300   32.82800 1.000 29.90000 ? 140 VAL A C   1 
ATOM   423  O  O   . VAL A 1 140 ? -3.51900  9.16300   31.86800 1.000 27.95000 ? 140 VAL A O   1 
ATOM   424  C  CB  . VAL A 1 140 ? -2.25600  8.00500   34.63500 1.000 32.75000 ? 140 VAL A CB  1 
ATOM   425  C  CG1 . VAL A 1 140 ? -3.29000  6.98100   34.27600 1.000 31.13000 ? 140 VAL A CG1 1 
ATOM   426  C  CG2 . VAL A 1 140 ? -1.11000  7.35400   35.34300 1.000 29.12000 ? 140 VAL A CG2 1 
ATOM   427  N  N   . GLU A 1 141 ? -3.20500  10.73200  33.43200 1.000 35.39000 ? 141 GLU A N   1 
ATOM   428  C  CA  . GLU A 1 141 ? -4.31700  11.61900  33.02300 1.000 33.16000 ? 141 GLU A CA  1 
ATOM   429  C  C   . GLU A 1 141 ? -4.08400  12.06500  31.59300 1.000 28.35000 ? 141 GLU A C   1 
ATOM   430  O  O   . GLU A 1 141 ? -5.00200  12.03300  30.85400 1.000 24.49000 ? 141 GLU A O   1 
ATOM   431  C  CB  . GLU A 1 141 ? -4.40900  12.74900  34.04300 1.000 36.69000 ? 141 GLU A CB  1 
ATOM   432  C  CG  . GLU A 1 141 ? -4.91700  14.07800  33.54100 1.000 41.77000 ? 141 GLU A CG  1 
ATOM   433  C  CD  . GLU A 1 141 ? -4.51200  15.25700  34.42400 1.000 44.72000 ? 141 GLU A CD  1 
ATOM   434  O  OE1 . GLU A 1 141 ? -4.05600  15.01500  35.53500 1.000 43.57000 ? 141 GLU A OE1 1 
ATOM   435  O  OE2 . GLU A 1 141 ? -4.63000  16.38500  33.98300 1.000 41.36000 ? 141 GLU A OE2 1 
ATOM   436  N  N   . HIS A 1 142 ? -2.84700  12.41800  31.27200 1.000 26.64000 ? 142 HIS A N   1 
ATOM   437  C  CA  . HIS A 1 142 ? -2.47800  12.86200  29.91300 1.000 26.55000 ? 142 HIS A CA  1 
ATOM   438  C  C   . HIS A 1 142 ? -2.57000  11.74500  28.88600 1.000 24.49000 ? 142 HIS A C   1 
ATOM   439  O  O   . HIS A 1 142 ? -2.87100  12.04300  27.81400 1.000 21.56000 ? 142 HIS A O   1 
ATOM   440  C  CB  . HIS A 1 142 ? -1.20400  13.69700  29.95500 1.000 29.69000 ? 142 HIS A CB  1 
ATOM   441  C  CG  . HIS A 1 142 ? -1.27900  14.75900  30.99700 1.000 30.59000 ? 142 HIS A CG  1 
ATOM   442  N  ND1 . HIS A 1 142 ? -2.27100  15.66900  31.04600 1.000 32.22000 ? 142 HIS A ND1 1 
ATOM   443  C  CD2 . HIS A 1 142 ? -0.49000  15.02700  32.03900 1.000 31.88000 ? 142 HIS A CD2 1 
ATOM   444  C  CE1 . HIS A 1 142 ? -2.06100  16.46700  32.04700 1.000 38.13000 ? 142 HIS A CE1 1 
ATOM   445  N  NE2 . HIS A 1 142 ? -1.00700  16.09300  32.66200 1.000 35.33000 ? 142 HIS A NE2 1 
ATOM   446  N  N   . ASP A 1 143 ? -2.20900  10.53000  29.26300 1.000 22.82000 ? 143 ASP A N   1 
ATOM   447  C  CA  . ASP A 1 143 ? -2.26800  9.34700   28.37800 1.000 24.97000 ? 143 ASP A CA  1 
ATOM   448  C  C   . ASP A 1 143 ? -3.71400  9.05600   27.97400 1.000 18.07000 ? 143 ASP A C   1 
ATOM   449  O  O   . ASP A 1 143 ? -3.95200  8.92100   26.86100 1.000 16.13000 ? 143 ASP A O   1 
ATOM   450  C  CB  . ASP A 1 143 ? -1.55700  8.14800   28.97400 1.000 17.32000 ? 143 ASP A CB  1 
ATOM   451  C  CG  . ASP A 1 143 ? -1.75000  6.95200   28.08700 1.000 22.48000 ? 143 ASP A CG  1 
ATOM   452  O  OD1 . ASP A 1 143 ? -1.19200  6.91400   27.04700 1.000 24.20000 ? 143 ASP A OD1 1 
ATOM   453  O  OD2 . ASP A 1 143 ? -2.47900  6.11200   28.45300 1.000 27.45000 ? 143 ASP A OD2 1 
ATOM   454  N  N   . ILE A 1 144 ? -4.61400  9.12300   28.91800 1.000 18.82000 ? 144 ILE A N   1 
ATOM   455  C  CA  . ILE A 1 144 ? -6.06800  8.97200   28.67700 1.000 21.87000 ? 144 ILE A CA  1 
ATOM   456  C  C   . ILE A 1 144 ? -6.53000  10.09000  27.73500 1.000 21.49000 ? 144 ILE A C   1 
ATOM   457  O  O   . ILE A 1 144 ? -7.07800  9.79000   26.74200 1.000 25.33000 ? 144 ILE A O   1 
ATOM   458  C  CB  . ILE A 1 144 ? -6.76600  9.02200   30.05100 1.000 26.17000 ? 144 ILE A CB  1 
ATOM   459  C  CG1 . ILE A 1 144 ? -6.38500  7.82600   30.91900 1.000 26.88000 ? 144 ILE A CG1 1 
ATOM   460  C  CG2 . ILE A 1 144 ? -8.25800  9.21600   29.93800 1.000 23.68000 ? 144 ILE A CG2 1 
ATOM   461  C  CD1 . ILE A 1 144 ? -6.80800  7.89700   32.33400 1.000 27.86000 ? 144 ILE A CD1 1 
ATOM   462  N  N   . ALA A 1 145 ? -6.12700  11.31600  27.98200 1.000 20.33000 ? 145 ALA A N   1 
ATOM   463  C  CA  . ALA A 1 145 ? -6.52800  12.44200  27.13000 1.000 16.71000 ? 145 ALA A CA  1 
ATOM   464  C  C   . ALA A 1 145 ? -6.00500  12.25000  25.72700 1.000 19.72000 ? 145 ALA A C   1 
ATOM   465  O  O   . ALA A 1 145 ? -6.70900  12.52000  24.83400 1.000 23.73000 ? 145 ALA A O   1 
ATOM   466  C  CB  . ALA A 1 145 ? -6.00000  13.70100  27.70000 1.000 18.56000 ? 145 ALA A CB  1 
ATOM   467  N  N   . PHE A 1 146 ? -4.78700  11.79800  25.56600 1.000 18.48000 ? 146 PHE A N   1 
ATOM   468  C  CA  . PHE A 1 146 ? -4.29100  11.59600  24.19100 1.000 18.37000 ? 146 PHE A CA  1 
ATOM   469  C  C   . PHE A 1 146 ? -5.09600  10.52400  23.44500 1.000 21.62000 ? 146 PHE A C   1 
ATOM   470  O  O   . PHE A 1 146 ? -5.41500  10.77300  22.32800 1.000 18.49000 ? 146 PHE A O   1 
ATOM   471  C  CB  . PHE A 1 146 ? -2.81600  11.21700  24.24000 1.000 17.52000 ? 146 PHE A CB  1 
ATOM   472  C  CG  . PHE A 1 146 ? -2.14000  10.96200  22.93200 1.000 17.49000 ? 146 PHE A CG  1 
ATOM   473  C  CD1 . PHE A 1 146 ? -1.80400  11.99400  22.10200 1.000 18.10000 ? 146 PHE A CD1 1 
ATOM   474  C  CD2 . PHE A 1 146 ? -1.76400  9.69500   22.56200 1.000 19.54000 ? 146 PHE A CD2 1 
ATOM   475  C  CE1 . PHE A 1 146 ? -1.19000  11.74900  20.89900 1.000 20.53000 ? 146 PHE A CE1 1 
ATOM   476  C  CE2 . PHE A 1 146 ? -1.09300  9.45900   21.38500 1.000 17.78000 ? 146 PHE A CE2 1 
ATOM   477  C  CZ  . PHE A 1 146 ? -0.82500  10.48500  20.54100 1.000 19.54000 ? 146 PHE A CZ  1 
ATOM   478  N  N   . HIS A 1 147 ? -5.35000  9.38000   24.07700 1.000 16.84000 ? 147 HIS A N   1 
ATOM   479  C  CA  . HIS A 1 147 ? -6.08500  8.27500   23.41000 1.000 24.33000 ? 147 HIS A CA  1 
ATOM   480  C  C   . HIS A 1 147 ? -7.52900  8.70500   23.11500 1.000 20.73000 ? 147 HIS A C   1 
ATOM   481  O  O   . HIS A 1 147 ? -8.02100  8.37200   22.13200 1.000 21.98000 ? 147 HIS A O   1 
ATOM   482  C  CB  . HIS A 1 147 ? -5.89900  6.93300   24.11700 1.000 18.83000 ? 147 HIS A CB  1 
ATOM   483  C  CG  . HIS A 1 147 ? -4.51400  6.37100   24.09000 1.000 24.18000 ? 147 HIS A CG  1 
ATOM   484  N  ND1 . HIS A 1 147 ? -3.97400  5.77000   23.01300 1.000 22.01000 ? 147 HIS A ND1 1 
ATOM   485  C  CD2 . HIS A 1 147 ? -3.58200  6.30900   25.03200 1.000 17.55000 ? 147 HIS A CD2 1 
ATOM   486  C  CE1 . HIS A 1 147 ? -2.77600  5.39300   23.27400 1.000 19.14000 ? 147 HIS A CE1 1 
ATOM   487  N  NE2 . HIS A 1 147 ? -2.49200  5.71300   24.51200 1.000 21.74000 ? 147 HIS A NE2 1 
ATOM   488  N  N   . VAL A 1 148 ? -8.14300  9.42600   24.03300 1.000 25.15000 ? 148 VAL A N   1 
ATOM   489  C  CA  . VAL A 1 148 ? -9.51900  9.98400   23.91300 1.000 25.17000 ? 148 VAL A CA  1 
ATOM   490  C  C   . VAL A 1 148 ? -9.59600  11.00100  22.78900 1.000 23.45000 ? 148 VAL A C   1 
ATOM   491  O  O   . VAL A 1 148 ? -10.49900 10.90900  22.05500 1.000 26.68000 ? 148 VAL A O   1 
ATOM   492  C  CB  . VAL A 1 148 ? -9.98300  10.56700  25.24400 1.000 27.36000 ? 148 VAL A CB  1 
ATOM   493  C  CG1 . VAL A 1 148 ? -11.00200 11.67400  25.08300 1.000 27.82000 ? 148 VAL A CG1 1 
ATOM   494  C  CG2 . VAL A 1 148 ? -10.42800 9.48200   26.18300 1.000 25.63000 ? 148 VAL A CG2 1 
ATOM   495  N  N   . ALA A 1 149 ? -8.60900  11.86100  22.62400 1.000 24.86000 ? 149 ALA A N   1 
ATOM   496  C  CA  . ALA A 1 149 ? -8.64800  12.82000  21.50700 1.000 23.32000 ? 149 ALA A CA  1 
ATOM   497  C  C   . ALA A 1 149 ? -8.60900  12.06500  20.19400 1.000 22.99000 ? 149 ALA A C   1 
ATOM   498  O  O   . ALA A 1 149 ? -9.24600  12.50000  19.32000 1.000 24.90000 ? 149 ALA A O   1 
ATOM   499  C  CB  . ALA A 1 149 ? -7.51900  13.79700  21.57900 1.000 29.30000 ? 149 ALA A CB  1 
ATOM   500  N  N   . ILE A 1 150 ? -7.82400  11.00900  20.10100 1.000 23.35000 ? 150 ILE A N   1 
ATOM   501  C  CA  . ILE A 1 150 ? -7.80500  10.19800  18.86300 1.000 22.39000 ? 150 ILE A CA  1 
ATOM   502  C  C   . ILE A 1 150 ? -9.17600  9.56800   18.62000 1.000 22.74000 ? 150 ILE A C   1 
ATOM   503  O  O   . ILE A 1 150 ? -9.60900  9.60100   17.53000 1.000 23.56000 ? 150 ILE A O   1 
ATOM   504  C  CB  . ILE A 1 150 ? -6.71900  9.12700   18.89100 1.000 24.39000 ? 150 ILE A CB  1 
ATOM   505  C  CG1 . ILE A 1 150 ? -5.34800  9.74600   19.13500 1.000 32.34000 ? 150 ILE A CG1 1 
ATOM   506  C  CG2 . ILE A 1 150 ? -6.77800  8.31100   17.62000 1.000 28.89000 ? 150 ILE A CG2 1 
ATOM   507  C  CD1 . ILE A 1 150 ? -4.27500  8.78300   19.53600 1.000 28.33000 ? 150 ILE A CD1 1 
ATOM   508  N  N   . ALA A 1 151 ? -9.82400  9.04500   19.63900 1.000 21.97000 ? 151 ALA A N   1 
ATOM   509  C  CA  . ALA A 1 151 ? -11.16100 8.45300   19.48500 1.000 23.62000 ? 151 ALA A CA  1 
ATOM   510  C  C   . ALA A 1 151 ? -12.15600 9.51700   19.00700 1.000 26.66000 ? 151 ALA A C   1 
ATOM   511  O  O   . ALA A 1 151 ? -12.94300 9.20700   18.16400 1.000 30.30000 ? 151 ALA A O   1 
ATOM   512  C  CB  . ALA A 1 151 ? -11.58600 7.80900   20.75900 1.000 25.86000 ? 151 ALA A CB  1 
ATOM   513  N  N   . ALA A 1 152 ? -12.06400 10.74500  19.50700 1.000 29.44000 ? 152 ALA A N   1 
ATOM   514  C  CA  . ALA A 1 152 ? -12.93400 11.84400  19.04600 1.000 26.58000 ? 152 ALA A CA  1 
ATOM   515  C  C   . ALA A 1 152 ? -12.68900 12.11800  17.58100 1.000 23.72000 ? 152 ALA A C   1 
ATOM   516  O  O   . ALA A 1 152 ? -13.65100 12.24300  16.90700 1.000 22.89000 ? 152 ALA A O   1 
ATOM   517  C  CB  . ALA A 1 152 ? -12.75700 13.07900  19.86100 1.000 25.24000 ? 152 ALA A CB  1 
ATOM   518  N  N   . ALA A 1 153 ? -11.44400 12.04600  17.12100 1.000 22.68000 ? 153 ALA A N   1 
ATOM   519  C  CA  . ALA A 1 153 ? -11.01700 12.32800  15.72800 1.000 23.39000 ? 153 ALA A CA  1 
ATOM   520  C  C   . ALA A 1 153 ? -11.51000 11.30400  14.70400 1.000 24.33000 ? 153 ALA A C   1 
ATOM   521  O  O   . ALA A 1 153 ? -11.31200 11.52700  13.55600 1.000 25.45000 ? 153 ALA A O   1 
ATOM   522  C  CB  . ALA A 1 153 ? -9.55200  12.56400  15.61300 1.000 20.66000 ? 153 ALA A CB  1 
ATOM   523  N  N   . THR A 1 154 ? -12.01000 10.16500  15.14300 1.000 23.93000 ? 154 THR A N   1 
ATOM   524  C  CA  . THR A 1 154 ? -12.68300 9.19100   14.26600 1.000 28.66000 ? 154 THR A CA  1 
ATOM   525  C  C   . THR A 1 154 ? -13.95400 9.82800   13.72900 1.000 24.23000 ? 154 THR A C   1 
ATOM   526  O  O   . THR A 1 154 ? -14.29800 9.47600   12.67800 1.000 30.41000 ? 154 THR A O   1 
ATOM   527  C  CB  . THR A 1 154 ? -13.03400 7.85600   14.95300 1.000 27.97000 ? 154 THR A CB  1 
ATOM   528  O  OG1 . THR A 1 154 ? -14.22200 7.94800   15.71500 1.000 22.45000 ? 154 THR A OG1 1 
ATOM   529  C  CG2 . THR A 1 154 ? -11.91700 7.26800   15.78700 1.000 24.76000 ? 154 THR A CG2 1 
ATOM   530  N  N   . HIS A 1 155 ? -14.64200 10.62200  14.55500 1.000 26.98000 ? 155 HIS A N   1 
ATOM   531  C  CA  . HIS A 1 155 ? -15.92900 11.33500  14.34100 1.000 30.57000 ? 155 HIS A CA  1 
ATOM   532  C  C   . HIS A 1 155 ? -17.05300 10.30500  14.25600 1.000 36.84000 ? 155 HIS A C   1 
ATOM   533  O  O   . HIS A 1 155 ? -17.99300 10.53500  13.52400 1.000 34.05000 ? 155 HIS A O   1 
ATOM   534  C  CB  . HIS A 1 155 ? -15.90800 12.21800  13.09400 1.000 28.61000 ? 155 HIS A CB  1 
ATOM   535  C  CG  . HIS A 1 155 ? -15.11100 13.45900  13.25500 1.000 32.22000 ? 155 HIS A CG  1 
ATOM   536  N  ND1 . HIS A 1 155 ? -13.98700 13.69900  12.54100 1.000 29.66000 ? 155 HIS A ND1 1 
ATOM   537  C  CD2 . HIS A 1 155 ? -15.26100 14.49800  14.08200 1.000 29.74000 ? 155 HIS A CD2 1 
ATOM   538  C  CE1 . HIS A 1 155 ? -13.52000 14.85400  12.89800 1.000 35.03000 ? 155 HIS A CE1 1 
ATOM   539  N  NE2 . HIS A 1 155 ? -14.26500 15.34800  13.83300 1.000 32.54000 ? 155 HIS A NE2 1 
ATOM   540  N  N   . ASN A 1 156 ? -16.85700 9.16600   14.90800 1.000 29.55000 ? 156 ASN A N   1 
ATOM   541  C  CA  . ASN A 1 156 ? -17.81600 8.05800   14.95000 1.000 32.25000 ? 156 ASN A CA  1 
ATOM   542  C  C   . ASN A 1 156 ? -18.16400 8.05900   16.39900 1.000 34.30000 ? 156 ASN A C   1 
ATOM   543  O  O   . ASN A 1 156 ? -17.31000 7.71900   17.16300 1.000 34.73000 ? 156 ASN A O   1 
ATOM   544  C  CB  . ASN A 1 156 ? -17.13900 6.72800   14.63200 1.000 31.17000 ? 156 ASN A CB  1 
ATOM   545  C  CG  . ASN A 1 156 ? -18.08000 5.54800   14.65400 1.000 28.42000 ? 156 ASN A CG  1 
ATOM   546  O  OD1 . ASN A 1 156 ? -18.86200 5.40600   15.55000 1.000 28.25000 ? 156 ASN A OD1 1 
ATOM   547  N  ND2 . ASN A 1 156 ? -17.99900 4.71800   13.65500 1.000 27.17000 ? 156 ASN A ND2 1 
ATOM   548  N  N   . ARG A 1 157 ? -19.39500 8.40700   16.71500 1.000 31.66000 ? 157 ARG A N   1 
ATOM   549  C  CA  . ARG A 1 157 ? -19.83700 8.52200   18.11200 1.000 32.15000 ? 157 ARG A CA  1 
ATOM   550  C  C   . ARG A 1 157 ? -19.74500 7.16100   18.78300 1.000 31.61000 ? 157 ARG A C   1 
ATOM   551  O  O   . ARG A 1 157 ? -19.37200 7.13700   19.90900 1.000 31.71000 ? 157 ARG A O   1 
ATOM   552  C  CB  . ARG A 1 157 ? -21.24400 9.10900   18.14200 1.000 35.08000 ? 157 ARG A CB  1 
ATOM   553  C  CG  . ARG A 1 157 ? -21.83700 9.31000   19.52000 1.000 41.55000 ? 157 ARG A CG  1 
ATOM   554  C  CD  . ARG A 1 157 ? -21.44600 10.59300  20.21500 1.000 50.60000 ? 157 ARG A CD  1 
ATOM   555  N  NE  . ARG A 1 157 ? -22.14300 10.71000  21.48100 1.000 54.95000 ? 157 ARG A NE  1 
ATOM   556  C  CZ  . ARG A 1 157 ? -21.67200 11.32000  22.54800 1.000 51.82000 ? 157 ARG A CZ  1 
ATOM   557  N  NH1 . ARG A 1 157 ? -20.45500 11.82100  22.53900 1.000 56.91000 ? 157 ARG A NH1 1 
ATOM   558  N  NH2 . ARG A 1 157 ? -22.37800 11.34400  23.65500 1.000 46.92000 ? 157 ARG A NH2 1 
ATOM   559  N  N   . TYR A 1 158 ? -20.08100 6.09200   18.07700 1.000 31.20000 ? 158 TYR A N   1 
ATOM   560  C  CA  . TYR A 1 158 ? -20.07700 4.75400   18.69800 1.000 34.17000 ? 158 TYR A CA  1 
ATOM   561  C  C   . TYR A 1 158 ? -18.67600 4.33000   19.12800 1.000 32.26000 ? 158 TYR A C   1 
ATOM   562  O  O   . TYR A 1 158 ? -18.47400 4.04800   20.27200 1.000 28.88000 ? 158 TYR A O   1 
ATOM   563  C  CB  . TYR A 1 158 ? -20.80100 3.76800   17.78600 1.000 33.82000 ? 158 TYR A CB  1 
ATOM   564  C  CG  . TYR A 1 158 ? -21.48200 2.71600   18.58700 1.000 34.34000 ? 158 TYR A CG  1 
ATOM   565  C  CD1 . TYR A 1 158 ? -22.72900 2.89600   19.13100 1.000 33.65000 ? 158 TYR A CD1 1 
ATOM   566  C  CD2 . TYR A 1 158 ? -20.81400 1.55500   18.87000 1.000 40.34000 ? 158 TYR A CD2 1 
ATOM   567  C  CE1 . TYR A 1 158 ? -23.30200 1.90800   19.91500 1.000 40.76000 ? 158 TYR A CE1 1 
ATOM   568  C  CE2 . TYR A 1 158 ? -21.37300 0.54900   19.62400 1.000 37.49000 ? 158 TYR A CE2 1 
ATOM   569  C  CZ  . TYR A 1 158 ? -22.62200 0.72300   20.15200 1.000 38.19000 ? 158 TYR A CZ  1 
ATOM   570  O  OH  . TYR A 1 158 ? -23.08400 -0.27700  20.94200 1.000 39.37000 ? 158 TYR A OH  1 
ATOM   571  N  N   . TYR A 1 159 ? -17.72900 4.48900   18.22900 1.000 31.32000 ? 159 TYR A N   1 
ATOM   572  C  CA  . TYR A 1 159 ? -16.31000 4.15300   18.44800 1.000 30.40000 ? 159 TYR A CA  1 
ATOM   573  C  C   . TYR A 1 159 ? -15.74500 5.02700   19.57200 1.000 30.45000 ? 159 TYR A C   1 
ATOM   574  O  O   . TYR A 1 159 ? -15.04800 4.58000   20.41600 1.000 25.71000 ? 159 TYR A O   1 
ATOM   575  C  CB  . TYR A 1 159 ? -15.63300 4.41900   17.11200 1.000 28.09000 ? 159 TYR A CB  1 
ATOM   576  C  CG  . TYR A 1 159 ? -14.59800 3.45000   16.64800 1.000 22.17000 ? 159 TYR A CG  1 
ATOM   577  C  CD1 . TYR A 1 159 ? -13.63000 3.01900   17.50600 1.000 21.12000 ? 159 TYR A CD1 1 
ATOM   578  C  CD2 . TYR A 1 159 ? -14.55200 3.03200   15.34600 1.000 20.28000 ? 159 TYR A CD2 1 
ATOM   579  C  CE1 . TYR A 1 159 ? -12.64600 2.16600   17.08900 1.000 20.37000 ? 159 TYR A CE1 1 
ATOM   580  C  CE2 . TYR A 1 159 ? -13.58000 2.16600   14.90800 1.000 20.03000 ? 159 TYR A CE2 1 
ATOM   581  C  CZ  . TYR A 1 159 ? -12.62200 1.74500   15.79500 1.000 21.25000 ? 159 TYR A CZ  1 
ATOM   582  O  OH  . TYR A 1 159 ? -11.64200 0.90600   15.44100 1.000 28.06000 ? 159 TYR A OH  1 
ATOM   583  N  N   . GLN A 1 160 ? -16.12400 6.29200   19.56200 1.000 30.56000 ? 160 GLN A N   1 
ATOM   584  C  CA  . GLN A 1 160 ? -15.60800 7.28000   20.53000 1.000 34.78000 ? 160 GLN A CA  1 
ATOM   585  C  C   . GLN A 1 160 ? -16.03700 6.91000   21.93700 1.000 38.41000 ? 160 GLN A C   1 
ATOM   586  O  O   . GLN A 1 160 ? -15.20500 6.94900   22.83100 1.000 37.95000 ? 160 GLN A O   1 
ATOM   587  C  CB  . GLN A 1 160 ? -16.09600 8.66500   20.13800 1.000 31.80000 ? 160 GLN A CB  1 
ATOM   588  C  CG  . GLN A 1 160 ? -15.88600 9.73200   21.17300 1.000 30.71000 ? 160 GLN A CG  1 
ATOM   589  C  CD  . GLN A 1 160 ? -16.29800 11.09000  20.64700 1.000 38.68000 ? 160 GLN A CD  1 
ATOM   590  O  OE1 . GLN A 1 160 ? -17.22300 11.24200  19.86900 1.000 40.09000 ? 160 GLN A OE1 1 
ATOM   591  N  NE2 . GLN A 1 160 ? -15.60400 12.10800  21.08400 1.000 33.77000 ? 160 GLN A NE2 1 
ATOM   592  N  N   . ASP A 1 161 ? -17.30700 6.57200   22.08400 1.000 33.33000 ? 161 ASP A N   1 
ATOM   593  C  CA  . ASP A 1 161 ? -17.90600 6.22400   23.39600 1.000 36.40000 ? 161 ASP A CA  1 
ATOM   594  C  C   . ASP A 1 161 ? -17.40600 4.87500   23.94000 1.000 28.65000 ? 161 ASP A C   1 
ATOM   595  O  O   . ASP A 1 161 ? -17.23500 4.76100   25.11500 1.000 22.78000 ? 161 ASP A O   1 
ATOM   596  C  CB  . ASP A 1 161 ? -19.37900 6.60700   23.43400 1.000 35.14000 ? 161 ASP A CB  1 
ATOM   597  C  CG  . ASP A 1 161 ? -19.64400 8.09800   23.33500 1.000 44.02000 ? 161 ASP A CG  1 
ATOM   598  O  OD1 . ASP A 1 161 ? -18.74300 8.86900   23.01400 1.000 42.09000 ? 161 ASP A OD1 1 
ATOM   599  O  OD2 . ASP A 1 161 ? -20.74700 8.45000   23.58900 1.000 42.86000 ? 161 ASP A OD2 1 
ATOM   600  N  N   . LEU A 1 162 ? -17.23600 3.89700   23.07200 1.000 28.88000 ? 162 LEU A N   1 
ATOM   601  C  CA  . LEU A 1 162 ? -16.67000 2.61300   23.52100 1.000 30.89000 ? 162 LEU A CA  1 
ATOM   602  C  C   . LEU A 1 162 ? -15.23800 2.84900   24.04200 1.000 30.31000 ? 162 LEU A C   1 
ATOM   603  O  O   . LEU A 1 162 ? -14.92100 2.31300   25.06700 1.000 25.82000 ? 162 LEU A O   1 
ATOM   604  C  CB  . LEU A 1 162 ? -16.70700 1.66100   22.32300 1.000 25.81000 ? 162 LEU A CB  1 
ATOM   605  C  CG  . LEU A 1 162 ? -15.93500 0.36300   22.47900 1.000 31.12000 ? 162 LEU A CG  1 
ATOM   606  C  CD1 . LEU A 1 162 ? -16.36400 -0.37000  23.72100 1.000 29.32000 ? 162 LEU A CD1 1 
ATOM   607  C  CD2 . LEU A 1 162 ? -16.04700 -0.52000  21.25500 1.000 20.99000 ? 162 LEU A CD2 1 
ATOM   608  N  N   . LEU A 1 163 ? -14.43600 3.65200   23.33200 1.000 30.46000 ? 163 LEU A N   1 
ATOM   609  C  CA  . LEU A 1 163 ? -13.00600 3.94500   23.67200 1.000 36.58000 ? 163 LEU A CA  1 
ATOM   610  C  C   . LEU A 1 163 ? -12.86000 4.77600   24.94100 1.000 32.18000 ? 163 LEU A C   1 
ATOM   611  O  O   . LEU A 1 163 ? -12.06000 4.41900   25.73600 1.000 28.98000 ? 163 LEU A O   1 
ATOM   612  C  CB  . LEU A 1 163 ? -12.18700 4.44300   22.48000 1.000 30.50000 ? 163 LEU A CB  1 
ATOM   613  C  CG  . LEU A 1 163 ? -11.83700 3.32400   21.50300 1.000 28.17000 ? 163 LEU A CG  1 
ATOM   614  C  CD1 . LEU A 1 163 ? -11.37000 3.82300   20.17300 1.000 21.23000 ? 163 LEU A CD1 1 
ATOM   615  C  CD2 . LEU A 1 163 ? -10.83900 2.36700   22.08800 1.000 25.65000 ? 163 LEU A CD2 1 
ATOM   616  N  N   . GLN A 1 164 ? -13.75800 5.72900   25.14800 1.000 31.19000 ? 164 GLN A N   1 
ATOM   617  C  CA  . GLN A 1 164 ? -13.77700 6.59500   26.34500 1.000 32.59000 ? 164 GLN A CA  1 
ATOM   618  C  C   . GLN A 1 164 ? -13.96500 5.70400   27.56100 1.000 31.41000 ? 164 GLN A C   1 
ATOM   619  O  O   . GLN A 1 164 ? -13.31900 5.94300   28.55800 1.000 28.40000 ? 164 GLN A O   1 
ATOM   620  C  CB  . GLN A 1 164 ? -15.00100 7.48800   26.24300 1.000 36.81000 ? 164 GLN A CB  1 
ATOM   621  C  CG  . GLN A 1 164 ? -14.94000 8.75600   27.04500 1.000 39.01000 ? 164 GLN A CG  1 
ATOM   622  C  CD  . GLN A 1 164 ? -15.57600 9.88000   26.26600 1.000 46.08000 ? 164 GLN A CD  1 
ATOM   623  O  OE1 . GLN A 1 164 ? -16.65800 10.32900  26.57900 1.000 51.86000 ? 164 GLN A OE1 1 
ATOM   624  N  NE2 . GLN A 1 164 ? -14.93900 10.28500  25.19300 1.000 39.58000 ? 164 GLN A NE2 1 
ATOM   625  N  N   . TYR A 1 165 ? -14.87900 4.74700   27.44600 1.000 29.58000 ? 165 TYR A N   1 
ATOM   626  C  CA  . TYR A 1 165 ? -15.13800 3.74500   28.48200 1.000 25.05000 ? 165 TYR A CA  1 
ATOM   627  C  C   . TYR A 1 165 ? -13.94700 2.81100   28.67400 1.000 26.44000 ? 165 TYR A C   1 
ATOM   628  O  O   . TYR A 1 165 ? -13.61700 2.64900   29.75200 1.000 28.20000 ? 165 TYR A O   1 
ATOM   629  C  CB  . TYR A 1 165 ? -16.34000 2.89000   28.11300 1.000 26.84000 ? 165 TYR A CB  1 
ATOM   630  C  CG  . TYR A 1 165 ? -16.41600 1.73700   29.06200 1.000 28.84000 ? 165 TYR A CG  1 
ATOM   631  C  CD1 . TYR A 1 165 ? -16.50700 2.00300   30.39500 1.000 30.63000 ? 165 TYR A CD1 1 
ATOM   632  C  CD2 . TYR A 1 165 ? -16.34600 0.42500   28.65900 1.000 24.94000 ? 165 TYR A CD2 1 
ATOM   633  C  CE1 . TYR A 1 165 ? -16.54300 1.00300   31.31800 1.000 32.02000 ? 165 TYR A CE1 1 
ATOM   634  C  CE2 . TYR A 1 165 ? -16.43200 -0.60000  29.57700 1.000 26.81000 ? 165 TYR A CE2 1 
ATOM   635  C  CZ  . TYR A 1 165 ? -16.51900 -0.30200  30.91500 1.000 30.92000 ? 165 TYR A CZ  1 
ATOM   636  O  OH  . TYR A 1 165 ? -16.52600 -1.20000  31.91300 1.000 29.13000 ? 165 TYR A OH  1 
ATOM   637  N  N   . LEU A 1 166 ? -13.34500 2.27100   27.62300 1.000 27.37000 ? 166 LEU A N   1 
ATOM   638  C  CA  . LEU A 1 166 ? -12.19700 1.33000   27.71600 1.000 29.68000 ? 166 LEU A CA  1 
ATOM   639  C  C   . LEU A 1 166 ? -10.90300 2.01200   28.18000 1.000 32.43000 ? 166 LEU A C   1 
ATOM   640  O  O   . LEU A 1 166 ? -10.11800 1.34300   28.78600 1.000 26.63000 ? 166 LEU A O   1 
ATOM   641  C  CB  . LEU A 1 166 ? -11.98000 0.55500   26.42300 1.000 29.94000 ? 166 LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 166 ? -13.04400 -0.47000  26.10900 1.000 30.57000 ? 166 LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 166 ? -12.63200 -1.33100  24.94400 1.000 35.28000 ? 166 LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 166 ? -13.31000 -1.29700  27.32700 1.000 26.89000 ? 166 LEU A CD2 1 
ATOM   645  N  N   . ASN A 1 167 ? -10.73300 3.31100   27.94900 1.000 27.89000 ? 167 ASN A N   1 
ATOM   646  C  CA  . ASN A 1 167 ? -9.49300  3.96400   28.42800 1.000 31.92000 ? 167 ASN A CA  1 
ATOM   647  C  C   . ASN A 1 167 ? -9.58800  4.47900   29.86300 1.000 28.12000 ? 167 ASN A C   1 
ATOM   648  O  O   . ASN A 1 167 ? -8.73100  5.12900   30.28200 1.000 32.14000 ? 167 ASN A O   1 
ATOM   649  C  CB  . ASN A 1 167 ? -8.60100  4.60300   27.36100 1.000 35.85000 ? 167 ASN A CB  1 
ATOM   650  C  CG  . ASN A 1 167 ? -9.23200  5.73200   26.59400 1.000 38.14000 ? 167 ASN A CG  1 
ATOM   651  O  OD1 . ASN A 1 167 ? -9.44700  6.79400   27.14700 1.000 40.69000 ? 167 ASN A OD1 1 
ATOM   652  N  ND2 . ASN A 1 167 ? -9.47200  5.51100   25.32100 1.000 33.31000 ? 167 ASN A ND2 1 
ATOM   653  N  N   . LEU A 1 168 ? -10.63500 4.14800   30.58200 1.000 28.34000 ? 168 LEU A N   1 
ATOM   654  C  CA  . LEU A 1 168 ? -10.68400 4.43600   32.02700 1.000 31.54000 ? 168 LEU A CA  1 
ATOM   655  C  C   . LEU A 1 168 ? -10.17500 3.20800   32.79800 1.000 32.70000 ? 168 LEU A C   1 
ATOM   656  O  O   . LEU A 1 168 ? -10.09100 3.26700   33.98300 1.000 32.46000 ? 168 LEU A O   1 
ATOM   657  C  CB  . LEU A 1 168 ? -12.10400 4.80600   32.43200 1.000 27.61000 ? 168 LEU A CB  1 
ATOM   658  C  CG  . LEU A 1 168 ? -12.67900 6.00800   31.71100 1.000 32.12000 ? 168 LEU A CG  1 
ATOM   659  C  CD1 . LEU A 1 168 ? -14.11500 6.21700   32.11600 1.000 31.54000 ? 168 LEU A CD1 1 
ATOM   660  C  CD2 . LEU A 1 168 ? -11.85700 7.24500   31.97800 1.000 34.04000 ? 168 LEU A CD2 1 
ATOM   661  N  N   . GLN A 1 169 ? -9.77600  2.17100   32.09000 1.000 27.53000 ? 169 GLN A N   1 
ATOM   662  C  CA  . GLN A 1 169 ? -9.31100  0.90800   32.67000 1.000 33.66000 ? 169 GLN A CA  1 
ATOM   663  C  C   . GLN A 1 169 ? -8.19000  1.18200   33.66000 1.000 31.55000 ? 169 GLN A C   1 
ATOM   664  O  O   . GLN A 1 169 ? -7.28900  1.92600   33.37700 1.000 33.77000 ? 169 GLN A O   1 
ATOM   665  C  CB  . GLN A 1 169 ? -8.76400  0.05500   31.53000 1.000 29.84000 ? 169 GLN A CB  1 
ATOM   666  C  CG  . GLN A 1 169 ? -8.61100  -1.40800  31.84100 1.000 27.61000 ? 169 GLN A CG  1 
ATOM   667  C  CD  . GLN A 1 169 ? -8.30400  -2.15100  30.56900 1.000 36.66000 ? 169 GLN A CD  1 
ATOM   668  O  OE1 . GLN A 1 169 ? -8.99000  -2.02400  29.56700 1.000 35.36000 ? 169 GLN A OE1 1 
ATOM   669  N  NE2 . GLN A 1 169 ? -7.21100  -2.88500  30.57800 1.000 34.28000 ? 169 GLN A NE2 1 
ATOM   670  N  N   . LEU A 1 170 ? -8.26300  0.52000   34.78700 1.000 32.37000 ? 170 LEU A N   1 
ATOM   671  C  CA  . LEU A 1 170 ? -7.23600  0.64600   35.83000 1.000 34.37000 ? 170 LEU A CA  1 
ATOM   672  C  C   . LEU A 1 170 ? -5.90800  0.03200   35.38600 1.000 33.52000 ? 170 LEU A C   1 
ATOM   673  O  O   . LEU A 1 170 ? -5.86200  -0.82900  34.59000 1.000 25.99000 ? 170 LEU A O   1 
ATOM   674  C  CB  . LEU A 1 170 ? -7.76100  0.01000   37.10300 1.000 32.11000 ? 170 LEU A CB  1 
ATOM   675  C  CG  . LEU A 1 170 ? -9.11800  0.51300   37.55700 1.000 29.67000 ? 170 LEU A CG  1 
ATOM   676  C  CD1 . LEU A 1 170 ? -9.42000  -0.02500  38.92100 1.000 27.11000 ? 170 LEU A CD1 1 
ATOM   677  C  CD2 . LEU A 1 170 ? -9.15800  2.02000   37.55100 1.000 35.29000 ? 170 LEU A CD2 1 
ATOM   678  N  N   . ARG A 1 171 ? -4.84900  0.59400   35.90800 1.000 42.24000 ? 171 ARG A N   1 
ATOM   679  C  CA  . ARG A 1 171 ? -3.47400  0.18000   35.57200 1.000 39.80000 ? 171 ARG A CA  1 
ATOM   680  C  C   . ARG A 1 171 ? -2.85900  -0.54900  36.76200 1.000 39.50000 ? 171 ARG A C   1 
ATOM   681  O  O   . ARG A 1 171 ? -3.45900  -0.57200  37.80300 1.000 39.56000 ? 171 ARG A O   1 
ATOM   682  C  CB  . ARG A 1 171 ? -2.70200  1.37700   35.03200 1.000 37.56000 ? 171 ARG A CB  1 
ATOM   683  N  N   . LEU A 1 172 ? -1.71000  -1.16800  36.53500 1.000 40.68000 ? 172 LEU A N   1 
ATOM   684  C  CA  . LEU A 1 172 ? -0.98400  -1.96400  37.54800 1.000 37.66000 ? 172 LEU A CA  1 
ATOM   685  C  C   . LEU A 1 172 ? -0.56600  -1.08100  38.72600 1.000 37.82000 ? 172 LEU A C   1 
ATOM   686  O  O   . LEU A 1 172 ? -0.06700  -0.00200  38.51600 1.000 39.53000 ? 172 LEU A O   1 
ATOM   687  C  CB  . LEU A 1 172 ? 0.20100   -2.62100  36.83700 1.000 39.74000 ? 172 LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 172 ? 1.18200   -3.39000  37.72400 1.000 45.62000 ? 172 LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 172 ? 0.58800   -4.64900  38.31000 1.000 39.66000 ? 172 LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 172 ? 2.48800   -3.67000  37.02100 1.000 40.00000 ? 172 LEU A CD2 1 
ATOM   691  N  N   . ALA A 1 173 ? -0.70200  -1.60200  39.92700 1.000 37.86000 ? 173 ALA A N   1 
ATOM   692  C  CA  . ALA A 1 173 ? -0.37200  -0.86700  41.16300 1.000 40.27000 ? 173 ALA A CA  1 
ATOM   693  C  C   . ALA A 1 173 ? 1.09000   -0.40400  41.20100 1.000 46.29000 ? 173 ALA A C   1 
ATOM   694  O  O   . ALA A 1 173 ? 1.96800   -1.15200  40.86700 1.000 45.55000 ? 173 ALA A O   1 
ATOM   695  C  CB  . ALA A 1 173 ? -0.64500  -1.75600  42.33100 1.000 36.72000 ? 173 ALA A CB  1 
ATOM   696  N  N   . VAL A 1 174 ? 1.28700   0.80600   41.70200 1.000 50.79000 ? 174 VAL A N   1 
ATOM   697  C  CA  . VAL A 1 174 ? 2.60300   1.46200   41.89800 1.000 52.35000 ? 174 VAL A CA  1 
ATOM   698  C  C   . VAL A 1 174 ? 3.38200   0.73100   42.99400 1.000 56.28000 ? 174 VAL A C   1 
ATOM   699  O  O   . VAL A 1 174 ? 2.84000   0.51900   44.05700 1.000 61.17000 ? 174 VAL A O   1 
ATOM   700  C  CB  . VAL A 1 174 ? 2.34400   2.91700   42.32100 1.000 57.12000 ? 174 VAL A CB  1 
ATOM   701  N  N   . SER A 1 175 ? 4.64100   0.42700   42.74400 1.000 55.68000 ? 175 SER A N   1 
ATOM   702  C  CA  . SER A 1 175 ? 5.51800   -0.24800  43.73400 1.000 59.39000 ? 175 SER A CA  1 
ATOM   703  C  C   . SER A 1 175 ? 6.79300   0.56900   43.84100 1.000 60.70000 ? 175 SER A C   1 
ATOM   704  O  O   . SER A 1 175 ? 7.22600   1.04500   42.79100 1.000 60.00000 ? 175 SER A O   1 
ATOM   705  C  CB  . SER A 1 175 ? 5.88400   -1.62800  43.28000 1.000 52.24000 ? 175 SER A CB  1 
ATOM   706  N  N   . THR A 1 176 ? 7.42400   0.62200   45.02400 1.000 62.10000 ? 176 THR A N   1 
ATOM   707  C  CA  . THR A 1 176 ? 8.71100   1.35700   45.14800 1.000 57.63000 ? 176 THR A CA  1 
ATOM   708  C  C   . THR A 1 176 ? 9.74300   0.71900   44.20600 1.000 57.98000 ? 176 THR A C   1 
ATOM   709  O  O   . THR A 1 176 ? 10.42400  1.44500   43.49600 1.000 55.07000 ? 176 THR A O   1 
ATOM   710  C  CB  . THR A 1 176 ? 9.22700   1.32800   46.58400 1.000 48.66000 ? 176 THR A CB  1 
ATOM   711  N  N   . ALA A 1 177 ? 9.79100   -0.60600  44.17100 1.000 59.95000 ? 177 ALA A N   1 
ATOM   712  C  CA  . ALA A 1 177 ? 10.72300  -1.36600  43.31700 1.000 57.06000 ? 177 ALA A CA  1 
ATOM   713  C  C   . ALA A 1 177 ? 10.42200  -1.12200  41.84900 1.000 52.91000 ? 177 ALA A C   1 
ATOM   714  O  O   . ALA A 1 177 ? 11.33700  -0.92600  41.08800 1.000 53.51000 ? 177 ALA A O   1 
ATOM   715  C  CB  . ALA A 1 177 ? 10.61400  -2.83100  43.65300 1.000 52.19000 ? 177 ALA A CB  1 
ATOM   716  N  N   . ARG A 1 178 ? 9.16000   -1.15700  41.47800 1.000 60.25000 ? 178 ARG A N   1 
ATOM   717  C  CA  . ARG A 1 178 ? 8.80400   -0.99300  40.04800 1.000 59.17000 ? 178 ARG A CA  1 
ATOM   718  C  C   . ARG A 1 178 ? 9.12000   0.42200   39.57900 1.000 54.67000 ? 178 ARG A C   1 
ATOM   719  O  O   . ARG A 1 178 ? 9.66800   0.53900   38.50600 1.000 53.22000 ? 178 ARG A O   1 
ATOM   720  C  CB  . ARG A 1 178 ? 7.33300   -1.32200  39.81300 1.000 53.97000 ? 178 ARG A CB  1 
ATOM   721  C  CG  . ARG A 1 178 ? 7.09600   -1.97500  38.46800 1.000 54.20000 ? 178 ARG A CG  1 
ATOM   722  C  CD  . ARG A 1 178 ? 7.19100   -3.47900  38.56300 1.000 52.71000 ? 178 ARG A CD  1 
ATOM   723  N  NE  . ARG A 1 178 ? 6.01700   -4.00400  39.20900 1.000 56.10000 ? 178 ARG A NE  1 
ATOM   724  C  CZ  . ARG A 1 178 ? 5.79300   -5.29100  39.36800 1.000 56.01000 ? 178 ARG A CZ  1 
ATOM   725  N  NH1 . ARG A 1 178 ? 6.68400   -6.15200  38.95200 1.000 48.64000 ? 178 ARG A NH1 1 
ATOM   726  N  NH2 . ARG A 1 178 ? 4.69100   -5.71900  39.94000 1.000 57.60000 ? 178 ARG A NH2 1 
ATOM   727  N  N   . THR A 1 179 ? 8.77600   1.41600   40.38700 1.000 49.31000 ? 179 THR A N   1 
ATOM   728  C  CA  . THR A 1 179 ? 9.02500   2.85000   40.11300 1.000 57.58000 ? 179 THR A CA  1 
ATOM   729  C  C   . THR A 1 179 ? 10.52100  3.14200   39.99700 1.000 57.66000 ? 179 THR A C   1 
ATOM   730  O  O   . THR A 1 179 ? 10.79700  4.15900   39.43200 1.000 55.44000 ? 179 THR A O   1 
ATOM   731  C  CB  . THR A 1 179 ? 8.13000   3.83400   40.88300 1.000 62.46000 ? 179 THR A CB  1 
ATOM   732  O  OG1 . THR A 1 179 ? 8.16400   5.02300   40.10500 1.000 59.93000 ? 179 THR A OG1 1 
ATOM   733  C  CG2 . THR A 1 179 ? 8.56900   4.11800   42.30000 1.000 58.17000 ? 179 THR A CG2 1 
ATOM   734  N  N   . ASN A 1 180 ? 11.33700  2.48900   40.83500 1.000 57.36000 ? 180 ASN A N   1 
ATOM   735  C  CA  . ASN A 1 180 ? 12.81400  2.64000   40.74700 1.000 52.68000 ? 180 ASN A CA  1 
ATOM   736  C  C   . ASN A 1 180 ? 13.33400  1.94600   39.49100 1.000 50.27000 ? 180 ASN A C   1 
ATOM   737  O  O   . ASN A 1 180 ? 14.15700  2.51500   38.82600 1.000 51.09000 ? 180 ASN A O   1 
ATOM   738  C  CB  . ASN A 1 180 ? 13.55400  2.21700   42.02100 1.000 52.91000 ? 180 ASN A CB  1 
ATOM   739  N  N   . SER A 1 181 ? 12.89100  0.72700   39.21700 1.000 52.42000 ? 181 SER A N   1 
ATOM   740  C  CA  . SER A 1 181 ? 13.36100  0.03200   37.99200 1.000 53.68000 ? 181 SER A CA  1 
ATOM   741  C  C   . SER A 1 181 ? 12.87900  0.71000   36.70600 1.000 53.98000 ? 181 SER A C   1 
ATOM   742  O  O   . SER A 1 181 ? 13.61400  0.62300   35.73700 1.000 53.46000 ? 181 SER A O   1 
ATOM   743  C  CB  . SER A 1 181 ? 13.12500  -1.44400  38.00100 1.000 53.90000 ? 181 SER A CB  1 
ATOM   744  O  OG  . SER A 1 181 ? 11.88800  -1.76700  37.41500 1.000 48.99000 ? 181 SER A OG  1 
ATOM   745  N  N   . ARG A 1 182 ? 11.64600  1.22600   36.66700 1.000 49.40000 ? 182 ARG A N   1 
ATOM   746  C  CA  . ARG A 1 182 ? 11.12900  1.95500   35.47400 1.000 52.48000 ? 182 ARG A CA  1 
ATOM   747  C  C   . ARG A 1 182 ? 11.92000  3.25600   35.20500 1.000 46.92000 ? 182 ARG A C   1 
ATOM   748  O  O   . ARG A 1 182 ? 12.06700  3.61000   34.07200 1.000 40.48000 ? 182 ARG A O   1 
ATOM   749  C  CB  . ARG A 1 182 ? 9.60600   2.08000   35.51200 1.000 49.46000 ? 182 ARG A CB  1 
ATOM   750  C  CG  . ARG A 1 182 ? 8.88800   0.74500   35.38300 1.000 48.98000 ? 182 ARG A CG  1 
ATOM   751  C  CD  . ARG A 1 182 ? 7.40200   0.82100   35.60500 1.000 54.15000 ? 182 ARG A CD  1 
ATOM   752  N  NE  . ARG A 1 182 ? 6.57000   -0.31400  35.24300 1.000 53.71000 ? 182 ARG A NE  1 
ATOM   753  C  CZ  . ARG A 1 182 ? 5.25100   -0.30000  35.35800 1.000 54.06000 ? 182 ARG A CZ  1 
ATOM   754  N  NH1 . ARG A 1 182 ? 4.63600   0.77600   35.79200 1.000 47.25000 ? 182 ARG A NH1 1 
ATOM   755  N  NH2 . ARG A 1 182 ? 4.54300   -1.36400  35.05100 1.000 54.94000 ? 182 ARG A NH2 1 
ATOM   756  N  N   . ARG A 1 183 ? 12.32600  3.98400   36.23500 1.000 46.20000 ? 183 ARG A N   1 
ATOM   757  C  CA  . ARG A 1 183 ? 13.15400  5.20000   36.02000 1.000 50.58000 ? 183 ARG A CA  1 
ATOM   758  C  C   . ARG A 1 183 ? 14.50700  4.80700   35.41200 1.000 51.24000 ? 183 ARG A C   1 
ATOM   759  O  O   . ARG A 1 183 ? 14.83400  5.34200   34.38200 1.000 46.02000 ? 183 ARG A O   1 
ATOM   760  C  CB  . ARG A 1 183 ? 13.34900  5.94400   37.33800 1.000 51.34000 ? 183 ARG A CB  1 
ATOM   761  N  N   . GLN A 1 184 ? 15.15600  3.76700   35.94600 1.000 52.62000 ? 184 GLN A N   1 
ATOM   762  C  CA  . GLN A 1 184 ? 16.45200  3.24800   35.43600 1.000 47.19000 ? 184 GLN A CA  1 
ATOM   763  C  C   . GLN A 1 184 ? 16.25100  2.74700   34.01200 1.000 49.74000 ? 184 GLN A C   1 
ATOM   764  O  O   . GLN A 1 184 ? 17.10600  2.99000   33.19500 1.000 47.32000 ? 184 GLN A O   1 
ATOM   765  C  CB  . GLN A 1 184 ? 17.03100  2.16600   36.34700 1.000 49.33000 ? 184 GLN A CB  1 
ATOM   766  C  CG  . GLN A 1 184 ? 18.29100  1.52300   35.77800 1.000 48.65000 ? 184 GLN A CG  1 
ATOM   767  C  CD  . GLN A 1 184 ? 19.43800  2.49600   35.70800 1.000 48.41000 ? 184 GLN A CD  1 
ATOM   768  O  OE1 . GLN A 1 184 ? 19.60400  3.32800   36.58000 1.000 46.86000 ? 184 GLN A OE1 1 
ATOM   769  N  NE2 . GLN A 1 184 ? 20.23100  2.40900   34.65700 1.000 45.33000 ? 184 GLN A NE2 1 
ATOM   770  N  N   . GLU A 1 185 ? 15.10600  2.10900   33.75800 1.000 51.42000 ? 185 GLU A N   1 
ATOM   771  C  CA  . GLU A 1 185 ? 14.50600  1.65500   32.48600 1.000 49.67000 ? 185 GLU A CA  1 
ATOM   772  C  C   . GLU A 1 185 ? 14.48800  2.79400   31.46000 1.000 44.05000 ? 185 GLU A C   1 
ATOM   773  O  O   . GLU A 1 185 ? 14.62100  2.51500   30.29500 1.000 46.12000 ? 185 GLU A O   1 
ATOM   774  C  CB  . GLU A 1 185 ? 13.02700  1.35600   32.72500 1.000 53.34000 ? 185 GLU A CB  1 
ATOM   775  C  CG  . GLU A 1 185 ? 12.64400  -0.03800  33.17200 1.000 53.84000 ? 185 GLU A CG  1 
ATOM   776  C  CD  . GLU A 1 185 ? 11.61400  -0.66400  32.23100 1.000 60.08000 ? 185 GLU A CD  1 
ATOM   777  O  OE1 . GLU A 1 185 ? 10.67600  -1.34900  32.71700 1.000 54.78000 ? 185 GLU A OE1 1 
ATOM   778  O  OE2 . GLU A 1 185 ? 11.76000  -0.46000  31.01100 1.000 56.65000 ? 185 GLU A OE2 1 
ATOM   779  N  N   . GLY A 1 186 ? 14.10000  3.96800   31.93100 1.000 41.85000 ? 186 GLY A N   1 
ATOM   780  C  CA  . GLY A 1 186 ? 13.72800  5.06100   31.01900 1.000 47.68000 ? 186 GLY A CA  1 
ATOM   781  C  C   . GLY A 1 186 ? 12.49700  4.64900   30.22200 1.000 42.77000 ? 186 GLY A C   1 
ATOM   782  O  O   . GLY A 1 186 ? 12.47400  4.83100   29.04600 1.000 41.53000 ? 186 GLY A O   1 
ATOM   783  N  N   . LEU A 1 187 ? 11.54100  4.03400   30.90700 1.000 38.50000 ? 187 LEU A N   1 
ATOM   784  C  CA  . LEU A 1 187 ? 10.31200  3.49300   30.29500 1.000 32.87000 ? 187 LEU A CA  1 
ATOM   785  C  C   . LEU A 1 187 ? 9.52300   4.61300   29.62600 1.000 33.23000 ? 187 LEU A C   1 
ATOM   786  O  O   . LEU A 1 187 ? 9.17300   4.42700   28.51700 1.000 31.17000 ? 187 LEU A O   1 
ATOM   787  C  CB  . LEU A 1 187 ? 9.47400   2.84700   31.40300 1.000 34.35000 ? 187 LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 187 ? 8.01200   2.58100   31.04600 1.000 33.77000 ? 187 LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 187 ? 7.89800   1.81200   29.76700 1.000 31.20000 ? 187 LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 187 ? 7.24600   1.89000   32.14200 1.000 31.87000 ? 187 LEU A CD2 1 
ATOM   791  N  N   . THR A 1 188 ? 9.38700   5.75300   30.28500 1.000 30.40000 ? 188 THR A N   1 
ATOM   792  C  CA  . THR A 1 188 ? 8.59000   6.89900   29.81100 1.000 30.51000 ? 188 THR A CA  1 
ATOM   793  C  C   . THR A 1 188 ? 9.16000   7.36600   28.48000 1.000 27.68000 ? 188 THR A C   1 
ATOM   794  O  O   . THR A 1 188 ? 8.39400   7.63600   27.62600 1.000 30.48000 ? 188 THR A O   1 
ATOM   795  C  CB  . THR A 1 188 ? 8.45600   8.00100   30.87700 1.000 29.54000 ? 188 THR A CB  1 
ATOM   796  O  OG1 . THR A 1 188 ? 9.71300   8.61700   31.09800 1.000 33.32000 ? 188 THR A OG1 1 
ATOM   797  C  CG2 . THR A 1 188 ? 7.92300   7.54700   32.21100 1.000 22.81000 ? 188 THR A CG2 1 
ATOM   798  N  N   . ALA A 1 189 ? 10.46800  7.40500   28.30500 1.000 30.35000 ? 189 ALA A N   1 
ATOM   799  C  CA  . ALA A 1 189 ? 10.93300  7.87000   26.97900 1.000 31.49000 ? 189 ALA A CA  1 
ATOM   800  C  C   . ALA A 1 189 ? 10.55700  6.88600   25.86000 1.000 25.41000 ? 189 ALA A C   1 
ATOM   801  O  O   . ALA A 1 189 ? 10.29300  7.30600   24.76000 1.000 22.30000 ? 189 ALA A O   1 
ATOM   802  C  CB  . ALA A 1 189 ? 12.38400  8.24000   27.00200 1.000 22.55000 ? 189 ALA A CB  1 
ATOM   803  N  N   . VAL A 1 190 ? 10.63900  5.59900   26.14800 1.000 25.60000 ? 190 VAL A N   1 
ATOM   804  C  CA  . VAL A 1 190 ? 10.27000  4.55700   25.13900 1.000 30.04000 ? 190 VAL A CA  1 
ATOM   805  C  C   . VAL A 1 190 ? 8.79600   4.69900   24.78300 1.000 20.73000 ? 190 VAL A C   1 
ATOM   806  O  O   . VAL A 1 190 ? 8.50000   4.65500   23.63900 1.000 21.21000 ? 190 VAL A O   1 
ATOM   807  C  CB  . VAL A 1 190 ? 10.54700  3.15000   25.67600 1.000 26.73000 ? 190 VAL A CB  1 
ATOM   808  C  CG1 . VAL A 1 190 ? 10.04000  2.08500   24.74900 1.000 21.65000 ? 190 VAL A CG1 1 
ATOM   809  C  CG2 . VAL A 1 190 ? 12.00600  2.95400   26.04900 1.000 23.25000 ? 190 VAL A CG2 1 
ATOM   810  N  N   . VAL A 1 191 ? 7.96600   4.88100   25.79400 1.000 19.78000 ? 191 VAL A N   1 
ATOM   811  C  CA  . VAL A 1 191 ? 6.50200   5.04500   25.63300 1.000 22.06000 ? 191 VAL A CA  1 
ATOM   812  C  C   . VAL A 1 191 ? 6.18800   6.33900   24.89700 1.000 23.44000 ? 191 VAL A C   1 
ATOM   813  O  O   . VAL A 1 191 ? 5.35200   6.27400   24.03400 1.000 20.72000 ? 191 VAL A O   1 
ATOM   814  C  CB  . VAL A 1 191 ? 5.72700   4.91500   26.95000 1.000 23.17000 ? 191 VAL A CB  1 
ATOM   815  C  CG1 . VAL A 1 191 ? 4.27600   5.29700   26.77400 1.000 17.72000 ? 191 VAL A CG1 1 
ATOM   816  C  CG2 . VAL A 1 191 ? 5.84000   3.52600   27.51800 1.000 20.05000 ? 191 VAL A CG2 1 
ATOM   817  N  N   . HIS A 1 192 ? 6.90300   7.42000   25.18900 1.000 19.08000 ? 192 HIS A N   1 
ATOM   818  C  CA  . HIS A 1 192 ? 6.66500   8.72500   24.53400 1.000 20.89000 ? 192 HIS A CA  1 
ATOM   819  C  C   . HIS A 1 192 ? 6.88900   8.61900   23.04100 1.000 21.72000 ? 192 HIS A C   1 
ATOM   820  O  O   . HIS A 1 192 ? 6.10000   9.14800   22.34400 1.000 18.30000 ? 192 HIS A O   1 
ATOM   821  C  CB  . HIS A 1 192 ? 7.50100   9.85100   25.11900 1.000 22.54000 ? 192 HIS A CB  1 
ATOM   822  C  CG  . HIS A 1 192 ? 6.98900   11.18400  24.71800 1.000 25.75000 ? 192 HIS A CG  1 
ATOM   823  N  ND1 . HIS A 1 192 ? 5.75500   11.61700  25.06800 1.000 22.17000 ? 192 HIS A ND1 1 
ATOM   824  C  CD2 . HIS A 1 192 ? 7.53100   12.16700  23.99700 1.000 21.70000 ? 192 HIS A CD2 1 
ATOM   825  C  CE1 . HIS A 1 192 ? 5.56600   12.80100  24.60600 1.000 21.22000 ? 192 HIS A CE1 1 
ATOM   826  N  NE2 . HIS A 1 192 ? 6.62500   13.15800  23.96200 1.000 24.01000 ? 192 HIS A NE2 1 
ATOM   827  N  N   . GLN A 1 193 ? 7.92200   7.88700   22.63400 1.000 20.90000 ? 193 GLN A N   1 
ATOM   828  C  CA  . GLN A 1 193 ? 8.25500   7.65400   21.20900 1.000 20.25000 ? 193 GLN A CA  1 
ATOM   829  C  C   . GLN A 1 193 ? 7.09400   6.90600   20.55600 1.000 18.86000 ? 193 GLN A C   1 
ATOM   830  O  O   . GLN A 1 193 ? 6.85200   7.14900   19.43400 1.000 19.43000 ? 193 GLN A O   1 
ATOM   831  C  CB  . GLN A 1 193 ? 9.59800   6.95900   21.00600 1.000 20.00000 ? 193 GLN A CB  1 
ATOM   832  C  CG  . GLN A 1 193 ? 10.78800  7.88600   20.99200 1.000 28.53000 ? 193 GLN A CG  1 
ATOM   833  C  CD  . GLN A 1 193 ? 12.10600  7.26600   21.37200 1.000 39.67000 ? 193 GLN A CD  1 
ATOM   834  O  OE1 . GLN A 1 193 ? 12.87700  6.86900   20.53200 1.000 48.90000 ? 193 GLN A OE1 1 
ATOM   835  N  NE2 . GLN A 1 193 ? 12.40500  7.20600   22.64700 1.000 40.20000 ? 193 GLN A NE2 1 
ATOM   836  N  N   . GLU A 1 194 ? 6.50400   5.94700   21.24500 1.000 17.65000 ? 194 GLU A N   1 
ATOM   837  C  CA  . GLU A 1 194 ? 5.32600   5.23100   20.71100 1.000 19.31000 ? 194 GLU A CA  1 
ATOM   838  C  C   . GLU A 1 194 ? 4.11100   6.15700   20.62600 1.000 16.12000 ? 194 GLU A C   1 
ATOM   839  O  O   . GLU A 1 194 ? 3.57700   6.19000   19.60100 1.000 18.32000 ? 194 GLU A O   1 
ATOM   840  C  CB  . GLU A 1 194 ? 4.94100   4.07000   21.61900 1.000 19.62000 ? 194 GLU A CB  1 
ATOM   841  C  CG  . GLU A 1 194 ? 5.89800   2.92000   21.64900 1.000 19.07000 ? 194 GLU A CG  1 
ATOM   842  C  CD  . GLU A 1 194 ? 5.58500   1.96200   22.77900 1.000 24.01000 ? 194 GLU A CD  1 
ATOM   843  O  OE1 . GLU A 1 194 ? 6.37600   1.11900   23.02400 1.000 29.26000 ? 194 GLU A OE1 1 
ATOM   844  O  OE2 . GLU A 1 194 ? 4.57500   2.09800   23.41900 1.000 22.36000 ? 194 GLU A OE2 1 
ATOM   845  N  N   . HIS A 1 195 ? 3.79900   6.91600   21.68100 1.000 16.10000 ? 195 HIS A N   1 
ATOM   846  C  CA  . HIS A 1 195 ? 2.66100   7.87400   21.62000 1.000 18.24000 ? 195 HIS A CA  1 
ATOM   847  C  C   . HIS A 1 195 ? 2.91900   8.86800   20.47900 1.000 20.54000 ? 195 HIS A C   1 
ATOM   848  O  O   . HIS A 1 195 ? 1.98100   9.14300   19.70500 1.000 21.61000 ? 195 HIS A O   1 
ATOM   849  C  CB  . HIS A 1 195 ? 2.47500   8.57500   22.97200 1.000 14.23000 ? 195 HIS A CB  1 
ATOM   850  C  CG  . HIS A 1 195 ? 1.54700   7.86100   23.89600 1.000 17.04000 ? 195 HIS A CG  1 
ATOM   851  N  ND1 . HIS A 1 195 ? 1.44900   8.18000   25.23700 1.000 19.73000 ? 195 HIS A ND1 1 
ATOM   852  C  CD2 . HIS A 1 195 ? 0.67700   6.85000   23.68300 1.000 16.26000 ? 195 HIS A CD2 1 
ATOM   853  C  CE1 . HIS A 1 195 ? 0.55900   7.39600   25.81000 1.000 15.55000 ? 195 HIS A CE1 1 
ATOM   854  N  NE2 . HIS A 1 195 ? 0.07100   6.57000   24.87700 1.000 15.82000 ? 195 HIS A NE2 1 
ATOM   855  N  N   . VAL A 1 196 ? 4.15400   9.37600   20.39600 1.000 20.79000 ? 196 VAL A N   1 
ATOM   856  C  CA  . VAL A 1 196 ? 4.60400   10.33800  19.33200 1.000 19.82000 ? 196 VAL A CA  1 
ATOM   857  C  C   . VAL A 1 196 ? 4.49200   9.81300   17.88500 1.000 20.45000 ? 196 VAL A C   1 
ATOM   858  O  O   . VAL A 1 196 ? 4.19900   10.59300  17.03500 1.000 21.20000 ? 196 VAL A O   1 
ATOM   859  C  CB  . VAL A 1 196 ? 6.02300   10.86100  19.62400 1.000 19.97000 ? 196 VAL A CB  1 
ATOM   860  C  CG1 . VAL A 1 196 ? 6.73700   11.37400  18.41200 1.000 20.12000 ? 196 VAL A CG1 1 
ATOM   861  C  CG2 . VAL A 1 196 ? 6.03900   11.90700  20.70300 1.000 19.89000 ? 196 VAL A CG2 1 
ATOM   862  N  N   . ALA A 1 197 ? 4.80800   8.55000   17.63000 1.000 16.27000 ? 197 ALA A N   1 
ATOM   863  C  CA  . ALA A 1 197 ? 4.72300   7.91900   16.30400 1.000 18.36000 ? 197 ALA A CA  1 
ATOM   864  C  C   . ALA A 1 197 ? 3.28500   7.89000   15.75700 1.000 25.85000 ? 197 ALA A C   1 
ATOM   865  O  O   . ALA A 1 197 ? 3.13500   7.86400   14.57800 1.000 26.93000 ? 197 ALA A O   1 
ATOM   866  C  CB  . ALA A 1 197 ? 5.40800   6.59600   16.29700 1.000 17.05000 ? 197 ALA A CB  1 
ATOM   867  N  N   . VAL A 1 198 ? 2.29700   7.72900   16.61500 1.000 24.29000 ? 198 VAL A N   1 
ATOM   868  C  CA  . VAL A 1 198 ? 0.85500   7.78500   16.27200 1.000 20.94000 ? 198 VAL A CA  1 
ATOM   869  C  C   . VAL A 1 198 ? 0.44400   9.21500   15.90200 1.000 25.30000 ? 198 VAL A C   1 
ATOM   870  O  O   . VAL A 1 198 ? -0.21000  9.36500   14.92200 1.000 25.10000 ? 198 VAL A O   1 
ATOM   871  C  CB  . VAL A 1 198 ? 0.02400   7.24400   17.44900 1.000 18.99000 ? 198 VAL A CB  1 
ATOM   872  C  CG1 . VAL A 1 198 ? -1.44600  7.30100   17.16700 1.000 24.36000 ? 198 VAL A CG1 1 
ATOM   873  C  CG2 . VAL A 1 198 ? 0.42600   5.83800   17.84500 1.000 21.41000 ? 198 VAL A CG2 1 
ATOM   874  N  N   . TYR A 1 199 ? 0.85700   10.21000  16.68500 1.000 23.49000 ? 199 TYR A N   1 
ATOM   875  C  CA  . TYR A 1 199 ? 0.53600   11.63300  16.41200 1.000 25.09000 ? 199 TYR A CA  1 
ATOM   876  C  C   . TYR A 1 199 ? 1.16100   12.07300  15.09200 1.000 27.66000 ? 199 TYR A C   1 
ATOM   877  O  O   . TYR A 1 199 ? 0.45700   12.63500  14.30200 1.000 29.00000 ? 199 TYR A O   1 
ATOM   878  C  CB  . TYR A 1 199 ? 0.95300   12.55000  17.55300 1.000 25.47000 ? 199 TYR A CB  1 
ATOM   879  C  CG  . TYR A 1 199 ? 0.78300   14.01600  17.26100 1.000 29.89000 ? 199 TYR A CG  1 
ATOM   880  C  CD1 . TYR A 1 199 ? -0.39600  14.66500  17.52800 1.000 26.78000 ? 199 TYR A CD1 1 
ATOM   881  C  CD2 . TYR A 1 199 ? 1.79700   14.74400  16.68000 1.000 31.17000 ? 199 TYR A CD2 1 
ATOM   882  C  CE1 . TYR A 1 199 ? -0.55200  16.00100  17.26200 1.000 29.60000 ? 199 TYR A CE1 1 
ATOM   883  C  CE2 . TYR A 1 199 ? 1.67000   16.08700  16.41500 1.000 30.39000 ? 199 TYR A CE2 1 
ATOM   884  C  CZ  . TYR A 1 199 ? 0.48200   16.70900  16.70100 1.000 33.31000 ? 199 TYR A CZ  1 
ATOM   885  O  OH  . TYR A 1 199 ? 0.34000   18.01800  16.45400 1.000 32.05000 ? 199 TYR A OH  1 
ATOM   886  N  N   . ASP A 1 200 ? 2.40400   11.70600  14.84200 1.000 22.22000 ? 200 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 200 ? 3.05400   12.07300  13.57100 1.000 25.99000 ? 200 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 200 ? 2.29500   11.44500  12.39800 1.000 31.71000 ? 200 ASP A C   1 
ATOM   889  O  O   . ASP A 1 200 ? 2.09700   12.12600  11.42800 1.000 32.91000 ? 200 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 200 ? 4.51300   11.62300  13.53400 1.000 25.73000 ? 200 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 200 ? 5.50300   12.59500  14.14600 1.000 34.22000 ? 200 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 200 ? 5.10700   13.48900  14.88000 1.000 35.61000 ? 200 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 200 ? 6.65700   12.45500  13.86400 1.000 46.04000 ? 200 ASP A OD2 1 
ATOM   894  N  N   . ALA A 1 201 ? 1.90700   10.17800  12.49900 1.000 28.82000 ? 201 ALA A N   1 
ATOM   895  C  CA  . ALA A 1 201 ? 1.19600   9.52100   11.38800 1.000 29.89000 ? 201 ALA A CA  1 
ATOM   896  C  C   . ALA A 1 201 ? -0.18800  10.14600  11.15400 1.000 27.11000 ? 201 ALA A C   1 
ATOM   897  O  O   . ALA A 1 201 ? -0.51900  10.37900  10.06200 1.000 30.64000 ? 201 ALA A O   1 
ATOM   898  C  CB  . ALA A 1 201 ? 1.15700   8.03800   11.61200 1.000 28.66000 ? 201 ALA A CB  1 
ATOM   899  N  N   . ILE A 1 202 ? -0.92200  10.43100  12.20800 1.000 26.39000 ? 202 ILE A N   1 
ATOM   900  C  CA  . ILE A 1 202 ? -2.24900  11.08200  12.15800 1.000 24.25000 ? 202 ILE A CA  1 
ATOM   901  C  C   . ILE A 1 202 ? -2.13000  12.50000  11.59500 1.000 29.13000 ? 202 ILE A C   1 
ATOM   902  O  O   . ILE A 1 202 ? -2.90100  12.86600  10.75800 1.000 33.72000 ? 202 ILE A O   1 
ATOM   903  C  CB  . ILE A 1 202 ? -2.86400  11.06600  13.55000 1.000 23.82000 ? 202 ILE A CB  1 
ATOM   904  C  CG1 . ILE A 1 202 ? -3.26100  9.64300   13.93700 1.000 27.43000 ? 202 ILE A CG1 1 
ATOM   905  C  CG2 . ILE A 1 202 ? -4.03800  11.99200  13.57500 1.000 27.10000 ? 202 ILE A CG2 1 
ATOM   906  C  CD1 . ILE A 1 202 ? -3.88000  9.49900   15.27400 1.000 23.36000 ? 202 ILE A CD1 1 
ATOM   907  N  N   . LEU A 1 203 ? -1.11500  13.23600  11.99100 1.000 27.83000 ? 203 LEU A N   1 
ATOM   908  C  CA  . LEU A 1 203 ? -0.87400  14.61600  11.50300 1.000 35.75000 ? 203 LEU A CA  1 
ATOM   909  C  C   . LEU A 1 203 ? -0.61700  14.59800  9.99600  1.000 32.71000 ? 203 LEU A C   1 
ATOM   910  O  O   . LEU A 1 203 ? -1.16700  15.42300  9.33500  1.000 27.43000 ? 203 LEU A O   1 
ATOM   911  C  CB  . LEU A 1 203 ? 0.28200   15.19800  12.32000 1.000 32.50000 ? 203 LEU A CB  1 
ATOM   912  C  CG  . LEU A 1 203 ? 0.97300   16.44500  11.82500 1.000 31.60000 ? 203 LEU A CG  1 
ATOM   913  C  CD1 . LEU A 1 203 ? -0.02300  17.53000  11.54400 1.000 34.72000 ? 203 LEU A CD1 1 
ATOM   914  C  CD2 . LEU A 1 203 ? 1.97400   16.88800  12.85500 1.000 31.42000 ? 203 LEU A CD2 1 
ATOM   915  N  N   . ALA A 1 204 ? 0.07500   13.57300  9.51000  1.000 29.45000 ? 204 ALA A N   1 
ATOM   916  C  CA  . ALA A 1 204 ? 0.45700   13.36300  8.10600  1.000 30.21000 ? 204 ALA A CA  1 
ATOM   917  C  C   . ALA A 1 204 ? -0.69100  12.84800  7.23300  1.000 33.88000 ? 204 ALA A C   1 
ATOM   918  O  O   . ALA A 1 204 ? -0.44800  12.57100  6.10000  1.000 32.99000 ? 204 ALA A O   1 
ATOM   919  C  CB  . ALA A 1 204 ? 1.60600   12.40900  8.07200  1.000 31.48000 ? 204 ALA A CB  1 
ATOM   920  N  N   . GLY A 1 205 ? -1.86700  12.65400  7.79300  1.000 33.52000 ? 205 GLY A N   1 
ATOM   921  C  CA  . GLY A 1 205 ? -3.01100  12.13000  7.04200  1.000 33.05000 ? 205 GLY A CA  1 
ATOM   922  C  C   . GLY A 1 205 ? -2.67000  10.80800  6.42300  1.000 31.90000 ? 205 GLY A C   1 
ATOM   923  O  O   . GLY A 1 205 ? -3.00800  10.61800  5.32500  1.000 39.10000 ? 205 GLY A O   1 
ATOM   924  N  N   . ASP A 1 206 ? -1.98500  9.94500   7.14400  1.000 36.21000 ? 206 ASP A N   1 
ATOM   925  C  CA  . ASP A 1 206 ? -1.53900  8.63600   6.62900  1.000 34.68000 ? 206 ASP A CA  1 
ATOM   926  C  C   . ASP A 1 206 ? -2.14600  7.47400   7.42900  1.000 37.56000 ? 206 ASP A C   1 
ATOM   927  O  O   . ASP A 1 206 ? -1.61200  7.14200   8.45000  1.000 34.89000 ? 206 ASP A O   1 
ATOM   928  C  CB  . ASP A 1 206 ? -0.03500  8.66700   6.71500  1.000 35.15000 ? 206 ASP A CB  1 
ATOM   929  C  CG  . ASP A 1 206 ? 0.63500   7.53400   6.01600  1.000 45.53000 ? 206 ASP A CG  1 
ATOM   930  O  OD1 . ASP A 1 206 ? -0.07500  6.65500   5.56500  1.000 45.63000 ? 206 ASP A OD1 1 
ATOM   931  O  OD2 . ASP A 1 206 ? 1.85000   7.57000   5.95600  1.000 48.06000 ? 206 ASP A OD2 1 
ATOM   932  N  N   . PRO A 1 207 ? -3.22400  6.82700   6.94600  1.000 38.21000 ? 207 PRO A N   1 
ATOM   933  C  CA  . PRO A 1 207 ? -3.93000  5.75400   7.65500  1.000 35.76000 ? 207 PRO A CA  1 
ATOM   934  C  C   . PRO A 1 207 ? -3.22600  4.43100   7.92400  1.000 31.80000 ? 207 PRO A C   1 
ATOM   935  O  O   . PRO A 1 207 ? -3.39000  3.94000   8.91500  1.000 33.96000 ? 207 PRO A O   1 
ATOM   936  C  CB  . PRO A 1 207 ? -5.19000  5.50500   6.84800  1.000 35.78000 ? 207 PRO A CB  1 
ATOM   937  C  CG  . PRO A 1 207 ? -5.27700  6.69700   5.96300  1.000 38.24000 ? 207 PRO A CG  1 
ATOM   938  C  CD  . PRO A 1 207 ? -3.84800  7.08500   5.67900  1.000 38.81000 ? 207 PRO A CD  1 
ATOM   939  N  N   . ASP A 1 208 ? -2.50100  3.90700   6.96800  1.000 36.66000 ? 208 ASP A N   1 
ATOM   940  C  CA  . ASP A 1 208 ? -1.75100  2.65900   7.22000  1.000 35.87000 ? 208 ASP A CA  1 
ATOM   941  C  C   . ASP A 1 208 ? -0.64500  2.92400   8.23700  1.000 33.34000 ? 208 ASP A C   1 
ATOM   942  O  O   . ASP A 1 208 ? -0.35400  2.08300   9.00700  1.000 31.69000 ? 208 ASP A O   1 
ATOM   943  C  CB  . ASP A 1 208 ? -1.31500  1.99800   5.91400  1.000 42.34000 ? 208 ASP A CB  1 
ATOM   944  C  CG  . ASP A 1 208 ? -2.44800  1.80600   4.92700  1.000 49.57000 ? 208 ASP A CG  1 
ATOM   945  O  OD1 . ASP A 1 208 ? -3.54400  1.44400   5.37100  1.000 44.82000 ? 208 ASP A OD1 1 
ATOM   946  O  OD2 . ASP A 1 208 ? -2.20700  2.02100   3.73700  1.000 48.24000 ? 208 ASP A OD2 1 
ATOM   947  N  N   . ARG A 1 209 ? 0.00400   4.06300   8.14100  1.000 34.94000 ? 209 ARG A N   1 
ATOM   948  C  CA  . ARG A 1 209 ? 1.07500   4.40300   9.09400  1.000 32.03000 ? 209 ARG A CA  1 
ATOM   949  C  C   . ARG A 1 209 ? 0.50500   4.58700   10.49900 1.000 27.37000 ? 209 ARG A C   1 
ATOM   950  O  O   . ARG A 1 209 ? 1.10400   4.12700   11.41800 1.000 26.49000 ? 209 ARG A O   1 
ATOM   951  C  CB  . ARG A 1 209 ? 1.86800   5.57300   8.53900  1.000 31.43000 ? 209 ARG A CB  1 
ATOM   952  C  CG  . ARG A 1 209 ? 2.98200   6.03200   9.44300  1.000 31.52000 ? 209 ARG A CG  1 
ATOM   953  C  CD  . ARG A 1 209 ? 3.81400   6.85700   8.51400  1.000 38.87000 ? 209 ARG A CD  1 
ATOM   954  N  NE  . ARG A 1 209 ? 4.53400   7.86000   9.23600  1.000 36.76000 ? 209 ARG A NE  1 
ATOM   955  C  CZ  . ARG A 1 209 ? 4.36200   9.13900   9.04600  1.000 41.90000 ? 209 ARG A CZ  1 
ATOM   956  N  NH1 . ARG A 1 209 ? 3.51100   9.55300   8.13500  1.000 37.16000 ? 209 ARG A NH1 1 
ATOM   957  N  NH2 . ARG A 1 209 ? 5.07400   10.00600  9.72600  1.000 42.48000 ? 209 ARG A NH2 1 
ATOM   958  N  N   . ALA A 1 210 ? -0.63000  5.24100   10.60700 1.000 26.80000 ? 210 ALA A N   1 
ATOM   959  C  CA  . ALA A 1 210 ? -1.28700  5.44800   11.90800 1.000 27.24000 ? 210 ALA A CA  1 
ATOM   960  C  C   . ALA A 1 210 ? -1.73400  4.13100   12.53500 1.000 25.68000 ? 210 ALA A C   1 
ATOM   961  O  O   . ALA A 1 210 ? -1.53900  4.00800   13.65800 1.000 25.68000 ? 210 ALA A O   1 
ATOM   962  C  CB  . ALA A 1 210 ? -2.43700  6.38500   11.73900 1.000 27.29000 ? 210 ALA A CB  1 
ATOM   963  N  N   . ARG A 1 211 ? -2.31400  3.21400   11.77000 1.000 27.03000 ? 211 ARG A N   1 
ATOM   964  C  CA  . ARG A 1 211 ? -2.78800  1.90000   12.24600 1.000 26.84000 ? 211 ARG A CA  1 
ATOM   965  C  C   . ARG A 1 211 ? -1.59400  1.09700   12.73400 1.000 22.25000 ? 211 ARG A C   1 
ATOM   966  O  O   . ARG A 1 211 ? -1.68500  0.56300   13.76800 1.000 21.64000 ? 211 ARG A O   1 
ATOM   967  C  CB  . ARG A 1 211 ? -3.49500  1.12000   11.13500 1.000 28.53000 ? 211 ARG A CB  1 
ATOM   968  C  CG  . ARG A 1 211 ? -3.91800  -0.29400  11.51400 1.000 25.75000 ? 211 ARG A CG  1 
ATOM   969  C  CD  . ARG A 1 211 ? -4.49900  -1.09700  10.38100 1.000 22.67000 ? 211 ARG A CD  1 
ATOM   970  N  NE  . ARG A 1 211 ? -5.64100  -0.46000  9.78800  1.000 27.74000 ? 211 ARG A NE  1 
ATOM   971  C  CZ  . ARG A 1 211 ? -6.90400  -0.67900  10.11700 1.000 31.39000 ? 211 ARG A CZ  1 
ATOM   972  N  NH1 . ARG A 1 211 ? -7.21300  -1.55700  11.04600 1.000 28.25000 ? 211 ARG A NH1 1 
ATOM   973  N  NH2 . ARG A 1 211 ? -7.86200  -0.03600  9.49300  1.000 25.11000 ? 211 ARG A NH2 1 
ATOM   974  N  N   . LEU A 1 212 ? -0.51000  1.11200   11.98100 1.000 24.07000 ? 212 LEU A N   1 
ATOM   975  C  CA  . LEU A 1 212 ? 0.71300   0.38400   12.35200 1.000 23.51000 ? 212 LEU A CA  1 
ATOM   976  C  C   . LEU A 1 212 ? 1.28000   0.94900   13.65100 1.000 24.89000 ? 212 LEU A C   1 
ATOM   977  O  O   . LEU A 1 212 ? 1.49500   0.17000   14.53200 1.000 25.18000 ? 212 LEU A O   1 
ATOM   978  C  CB  . LEU A 1 212 ? 1.69200   0.53400   11.19800 1.000 24.76000 ? 212 LEU A CB  1 
ATOM   979  C  CG  . LEU A 1 212 ? 2.80700   -0.49900  11.08900 1.000 37.55000 ? 212 LEU A CG  1 
ATOM   980  C  CD1 . LEU A 1 212 ? 2.37800   -1.87600  11.56900 1.000 27.41000 ? 212 LEU A CD1 1 
ATOM   981  C  CD2 . LEU A 1 212 ? 3.28700   -0.59000  9.65800  1.000 41.39000 ? 212 LEU A CD2 1 
ATOM   982  N  N   . ALA A 1 213 ? 1.37500   2.26800   13.80700 1.000 21.98000 ? 213 ALA A N   1 
ATOM   983  C  CA  . ALA A 1 213 ? 1.86100   2.86300   15.07300 1.000 22.14000 ? 213 ALA A CA  1 
ATOM   984  C  C   . ALA A 1 213 ? 0.91600   2.59700   16.25400 1.000 22.58000 ? 213 ALA A C   1 
ATOM   985  O  O   . ALA A 1 213 ? 1.39700   2.31500   17.27800 1.000 20.35000 ? 213 ALA A O   1 
ATOM   986  C  CB  . ALA A 1 213 ? 2.17300   4.31600   14.92600 1.000 19.76000 ? 213 ALA A CB  1 
ATOM   987  N  N   . ALA A 1 214 ? -0.38600  2.70500   16.08200 1.000 19.03000 ? 214 ALA A N   1 
ATOM   988  C  CA  . ALA A 1 214 ? -1.29400  2.45100   17.21700 1.000 19.40000 ? 214 ALA A CA  1 
ATOM   989  C  C   . ALA A 1 214 ? -1.25600  0.99300   17.70100 1.000 20.63000 ? 214 ALA A C   1 
ATOM   990  O  O   . ALA A 1 214 ? -1.29900  0.80000   18.85800 1.000 17.06000 ? 214 ALA A O   1 
ATOM   991  C  CB  . ALA A 1 214 ? -2.67700  2.92800   16.92100 1.000 19.31000 ? 214 ALA A CB  1 
ATOM   992  N  N   . THR A 1 215 ? -1.18700  0.04800   16.77800 1.000 22.27000 ? 215 THR A N   1 
ATOM   993  C  CA  . THR A 1 215 ? -1.14600  -1.39600  17.08000 1.000 22.59000 ? 215 THR A CA  1 
ATOM   994  C  C   . THR A 1 215 ? 0.15600   -1.74400  17.78000 1.000 23.76000 ? 215 THR A C   1 
ATOM   995  O  O   . THR A 1 215 ? 0.11800   -2.53400  18.65900 1.000 24.01000 ? 215 THR A O   1 
ATOM   996  C  CB  . THR A 1 215 ? -1.61000  -2.28600  15.92400 1.000 23.81000 ? 215 THR A CB  1 
ATOM   997  O  OG1 . THR A 1 215 ? -0.72400  -2.29400  14.83000 1.000 26.77000 ? 215 THR A OG1 1 
ATOM   998  C  CG2 . THR A 1 215 ? -2.96400  -1.89700  15.41000 1.000 24.75000 ? 215 THR A CG2 1 
ATOM   999  N  N   . ARG A 1 216 ? 1.23600   -1.13800  17.33900 1.000 24.15000 ? 216 ARG A N   1 
ATOM   1000 C  CA  . ARG A 1 216 ? 2.55700   -1.33200  17.94200 1.000 20.97000 ? 216 ARG A CA  1 
ATOM   1001 C  C   . ARG A 1 216 ? 2.52000   -0.82200  19.37400 1.000 20.27000 ? 216 ARG A C   1 
ATOM   1002 O  O   . ARG A 1 216 ? 2.96300   -1.56200  20.19300 1.000 18.74000 ? 216 ARG A O   1 
ATOM   1003 C  CB  . ARG A 1 216 ? 3.64200   -0.68800  17.09100 1.000 25.27000 ? 216 ARG A CB  1 
ATOM   1004 C  CG  . ARG A 1 216 ? 4.97900   -1.37200  17.26700 1.000 31.78000 ? 216 ARG A CG  1 
ATOM   1005 C  CD  . ARG A 1 216 ? 6.20900   -0.55100  17.04900 1.000 29.64000 ? 216 ARG A CD  1 
ATOM   1006 N  NE  . ARG A 1 216 ? 7.28500   -1.24700  17.68700 1.000 37.00000 ? 216 ARG A NE  1 
ATOM   1007 C  CZ  . ARG A 1 216 ? 8.05900   -0.81200  18.66800 1.000 40.35000 ? 216 ARG A CZ  1 
ATOM   1008 N  NH1 . ARG A 1 216 ? 7.90500   0.38300   19.21200 1.000 30.32000 ? 216 ARG A NH1 1 
ATOM   1009 N  NH2 . ARG A 1 216 ? 8.99500   -1.62300  19.11600 1.000 40.50000 ? 216 ARG A NH2 1 
ATOM   1010 N  N   . HIS A 1 217 ? 1.87000   0.31700   19.61500 1.000 17.77000 ? 217 HIS A N   1 
ATOM   1011 C  CA  . HIS A 1 217 ? 1.76900   0.90200   20.98000 1.000 19.92000 ? 217 HIS A CA  1 
ATOM   1012 C  C   . HIS A 1 217 ? 1.04900   -0.07900  21.90200 1.000 18.75000 ? 217 HIS A C   1 
ATOM   1013 O  O   . HIS A 1 217 ? 1.46300   -0.23900  23.00900 1.000 17.77000 ? 217 HIS A O   1 
ATOM   1014 C  CB  . HIS A 1 217 ? 1.12100   2.29200   21.02500 1.000 13.22000 ? 217 HIS A CB  1 
ATOM   1015 C  CG  . HIS A 1 217 ? 0.86100   2.85800   22.37900 1.000 14.27000 ? 217 HIS A CG  1 
ATOM   1016 N  ND1 . HIS A 1 217 ? 1.76000   2.83600   23.36800 1.000 16.15000 ? 217 HIS A ND1 1 
ATOM   1017 C  CD2 . HIS A 1 217 ? -0.19100  3.50500   22.88200 1.000 16.55000 ? 217 HIS A CD2 1 
ATOM   1018 C  CE1 . HIS A 1 217 ? 1.27400   3.39500   24.41400 1.000 14.92000 ? 217 HIS A CE1 1 
ATOM   1019 N  NE2 . HIS A 1 217 ? 0.08900   3.83300   24.15300 1.000 16.72000 ? 217 HIS A NE2 1 
ATOM   1020 N  N   . LEU A 1 218 ? -0.02300  -0.66100  21.41800 1.000 16.99000 ? 218 LEU A N   1 
ATOM   1021 C  CA  . LEU A 1 218 ? -0.74900  -1.62800  22.25400 1.000 18.45000 ? 218 LEU A CA  1 
ATOM   1022 C  C   . LEU A 1 218 ? 0.04400   -2.93800  22.44200 1.000 17.63000 ? 218 LEU A C   1 
ATOM   1023 O  O   . LEU A 1 218 ? 0.09200   -3.37100  23.52600 1.000 16.44000 ? 218 LEU A O   1 
ATOM   1024 C  CB  . LEU A 1 218 ? -2.19700  -1.72000  21.78400 1.000 18.33000 ? 218 LEU A CB  1 
ATOM   1025 C  CG  . LEU A 1 218 ? -3.16400  -0.70200  22.41000 1.000 24.74000 ? 218 LEU A CG  1 
ATOM   1026 C  CD1 . LEU A 1 218 ? -3.19500  -0.78700  23.89900 1.000 25.30000 ? 218 LEU A CD1 1 
ATOM   1027 C  CD2 . LEU A 1 218 ? -2.91600  0.72900   22.02400 1.000 12.89000 ? 218 LEU A CD2 1 
ATOM   1028 N  N   . GLN A 1 219 ? 0.71400   -3.44800  21.41400 1.000 17.53000 ? 219 GLN A N   1 
ATOM   1029 C  CA  . GLN A 1 219 ? 1.50400   -4.70600  21.47400 1.000 20.94000 ? 219 GLN A CA  1 
ATOM   1030 C  C   . GLN A 1 219 ? 2.64100   -4.55900  22.50900 1.000 25.43000 ? 219 GLN A C   1 
ATOM   1031 O  O   . GLN A 1 219 ? 2.73600   -5.39800  23.36400 1.000 23.44000 ? 219 GLN A O   1 
ATOM   1032 C  CB  . GLN A 1 219 ? 2.08700   -5.02600  20.09500 1.000 21.83000 ? 219 GLN A CB  1 
ATOM   1033 C  CG  . GLN A 1 219 ? 1.41300   -6.14400  19.32300 1.000 32.82000 ? 219 GLN A CG  1 
ATOM   1034 C  CD  . GLN A 1 219 ? 1.47800   -6.00500  17.81800 1.000 41.16000 ? 219 GLN A CD  1 
ATOM   1035 O  OE1 . GLN A 1 219 ? 1.79100   -4.95300  17.28600 1.000 42.31000 ? 219 GLN A OE1 1 
ATOM   1036 N  NE2 . GLN A 1 219 ? 1.17800   -7.06100  17.09500 1.000 33.67000 ? 219 GLN A NE2 1 
ATOM   1037 N  N   . GLN A 1 220 ? 3.37100   -3.45000  22.47800 1.000 18.60000 ? 220 GLN A N   1 
ATOM   1038 C  CA  . GLN A 1 220 ? 4.46200   -3.15400  23.42700 1.000 19.08000 ? 220 GLN A CA  1 
ATOM   1039 C  C   . GLN A 1 220 ? 3.92200   -3.01500  24.84500 1.000 20.14000 ? 220 GLN A C   1 
ATOM   1040 O  O   . GLN A 1 220 ? 4.53700   -3.51900  25.73700 1.000 17.77000 ? 220 GLN A O   1 
ATOM   1041 C  CB  . GLN A 1 220 ? 5.22800   -1.92300  22.97900 1.000 19.20000 ? 220 GLN A CB  1 
ATOM   1042 C  CG  . GLN A 1 220 ? 5.87400   -2.09500  21.63500 1.000 21.80000 ? 220 GLN A CG  1 
ATOM   1043 C  CD  . GLN A 1 220 ? 6.76400   -3.30500  21.61300 1.000 32.47000 ? 220 GLN A CD  1 
ATOM   1044 O  OE1 . GLN A 1 220 ? 7.89000   -3.25500  22.05800 1.000 32.22000 ? 220 GLN A OE1 1 
ATOM   1045 N  NE2 . GLN A 1 220 ? 6.24700   -4.41600  21.12600 1.000 28.70000 ? 220 GLN A NE2 1 
ATOM   1046 N  N   . ALA A 1 221 ? 2.79600   -2.34600  25.00000 1.000 15.66000 ? 221 ALA A N   1 
ATOM   1047 C  CA  . ALA A 1 221 ? 2.23300   -2.20900  26.33800 1.000 16.22000 ? 221 ALA A CA  1 
ATOM   1048 C  C   . ALA A 1 221 ? 1.81500   -3.58000  26.91400 1.000 16.71000 ? 221 ALA A C   1 
ATOM   1049 O  O   . ALA A 1 221 ? 2.15900   -3.84400  28.02200 1.000 15.16000 ? 221 ALA A O   1 
ATOM   1050 C  CB  . ALA A 1 221 ? 1.13600   -1.18900  26.33600 1.000 17.14000 ? 221 ALA A CB  1 
ATOM   1051 N  N   . ALA A 1 222 ? 1.17100   -4.43400  26.12800 1.000 15.25000 ? 222 ALA A N   1 
ATOM   1052 C  CA  . ALA A 1 222 ? 0.76900   -5.78800  26.61400 1.000 20.69000 ? 222 ALA A CA  1 
ATOM   1053 C  C   . ALA A 1 222 ? 2.01400   -6.61700  27.00900 1.000 16.92000 ? 222 ALA A C   1 
ATOM   1054 O  O   . ALA A 1 222 ? 2.01500   -7.18000  28.01500 1.000 13.72000 ? 222 ALA A O   1 
ATOM   1055 C  CB  . ALA A 1 222 ? -0.08400  -6.49300  25.59100 1.000 11.68000 ? 222 ALA A CB  1 
ATOM   1056 N  N   . SER A 1 223 ? 3.04200   -6.56200  26.18900 1.000 17.66000 ? 223 SER A N   1 
ATOM   1057 C  CA  . SER A 1 223 ? 4.34900   -7.22300  26.37900 1.000 20.56000 ? 223 SER A CA  1 
ATOM   1058 C  C   . SER A 1 223 ? 5.04300   -6.71400  27.64800 1.000 22.68000 ? 223 SER A C   1 
ATOM   1059 O  O   . SER A 1 223 ? 5.44800   -7.54000  28.41100 1.000 19.48000 ? 223 SER A O   1 
ATOM   1060 C  CB  . SER A 1 223 ? 5.19500   -7.02700  25.19100 1.000 21.75000 ? 223 SER A CB  1 
ATOM   1061 O  OG  . SER A 1 223 ? 4.89500   -7.98500  24.22800 1.000 25.43000 ? 223 SER A OG  1 
ATOM   1062 N  N   . ARG A 1 224 ? 5.06100   -5.40300  27.88400 1.000 20.61000 ? 224 ARG A N   1 
ATOM   1063 C  CA  . ARG A 1 224 ? 5.63500   -4.83900  29.13400 1.000 18.97000 ? 224 ARG A CA  1 
ATOM   1064 C  C   . ARG A 1 224 ? 4.80900   -5.29900  30.33300 1.000 19.17000 ? 224 ARG A C   1 
ATOM   1065 O  O   . ARG A 1 224 ? 5.37500   -5.59300  31.32600 1.000 21.39000 ? 224 ARG A O   1 
ATOM   1066 C  CB  . ARG A 1 224 ? 5.75200   -3.30600  29.14600 1.000 19.09000 ? 224 ARG A CB  1 
ATOM   1067 C  CG  . ARG A 1 224 ? 6.73600   -2.70500  28.15500 1.000 18.92000 ? 224 ARG A CG  1 
ATOM   1068 C  CD  . ARG A 1 224 ? 6.89200   -1.19700  28.23000 1.000 19.44000 ? 224 ARG A CD  1 
ATOM   1069 N  NE  . ARG A 1 224 ? 5.81500   -0.40900  27.66000 1.000 19.44000 ? 224 ARG A NE  1 
ATOM   1070 C  CZ  . ARG A 1 224 ? 5.69200   -0.05900  26.41400 1.000 18.08000 ? 224 ARG A CZ  1 
ATOM   1071 N  NH1 . ARG A 1 224 ? 4.65600   0.63600   26.05200 1.000 17.41000 ? 224 ARG A NH1 1 
ATOM   1072 N  NH2 . ARG A 1 224 ? 6.57000   -0.42800  25.52400 1.000 19.94000 ? 224 ARG A NH2 1 
ATOM   1073 N  N   . LEU A 1 225 ? 3.49600   -5.30200  30.20100 1.000 17.16000 ? 225 LEU A N   1 
ATOM   1074 C  CA  . LEU A 1 225 ? 2.58800   -5.65600  31.30600 1.000 18.16000 ? 225 LEU A CA  1 
ATOM   1075 C  C   . LEU A 1 225 ? 2.76600   -7.11700  31.72400 1.000 21.79000 ? 225 LEU A C   1 
ATOM   1076 O  O   . LEU A 1 225 ? 2.76500   -7.36500  32.86000 1.000 24.36000 ? 225 LEU A O   1 
ATOM   1077 C  CB  . LEU A 1 225 ? 1.16300   -5.31300  30.89500 1.000 18.65000 ? 225 LEU A CB  1 
ATOM   1078 C  CG  . LEU A 1 225 ? 0.07200   -5.77100  31.84000 1.000 20.83000 ? 225 LEU A CG  1 
ATOM   1079 C  CD1 . LEU A 1 225 ? 0.36600   -5.35100  33.23600 1.000 20.74000 ? 225 LEU A CD1 1 
ATOM   1080 C  CD2 . LEU A 1 225 ? -1.29900  -5.28100  31.41600 1.000 29.53000 ? 225 LEU A CD2 1 
ATOM   1081 N  N   . ARG A 1 226 ? 2.93000   -8.01800  30.77900 1.000 20.34000 ? 226 ARG A N   1 
ATOM   1082 C  CA  . ARG A 1 226 ? 3.17700   -9.46200  31.02600 1.000 26.61000 ? 226 ARG A CA  1 
ATOM   1083 C  C   . ARG A 1 226 ? 4.45700   -9.63200  31.84800 1.000 20.49000 ? 226 ARG A C   1 
ATOM   1084 O  O   . ARG A 1 226 ? 4.41300   -10.29000 32.79000 1.000 21.17000 ? 226 ARG A O   1 
ATOM   1085 C  CB  . ARG A 1 226 ? 3.23600   -10.20600 29.68900 1.000 19.07000 ? 226 ARG A CB  1 
ATOM   1086 C  CG  . ARG A 1 226 ? 3.72200   -11.63800 29.77700 1.000 28.38000 ? 226 ARG A CG  1 
ATOM   1087 C  CD  . ARG A 1 226 ? 3.77800   -12.37900 28.47700 1.000 24.77000 ? 226 ARG A CD  1 
ATOM   1088 N  NE  . ARG A 1 226 ? 2.50900   -12.43800 27.82000 1.000 26.18000 ? 226 ARG A NE  1 
ATOM   1089 C  CZ  . ARG A 1 226 ? 2.28100   -11.97000 26.62700 1.000 28.45000 ? 226 ARG A CZ  1 
ATOM   1090 N  NH1 . ARG A 1 226 ? 1.08200   -12.09100 26.10000 1.000 25.04000 ? 226 ARG A NH1 1 
ATOM   1091 N  NH2 . ARG A 1 226 ? 3.25500   -11.40200 25.95300 1.000 24.67000 ? 226 ARG A NH2 1 
ATOM   1092 N  N   . LEU A 1 227 ? 5.52900   -8.97900  31.45500 1.000 21.93000 ? 227 LEU A N   1 
ATOM   1093 C  CA  . LEU A 1 227 ? 6.82100   -9.06500  32.17100 1.000 23.56000 ? 227 LEU A CA  1 
ATOM   1094 C  C   . LEU A 1 227 ? 6.65100   -8.54600  33.60500 1.000 25.08000 ? 227 LEU A C   1 
ATOM   1095 O  O   . LEU A 1 227 ? 7.15300   -9.17200  34.47100 1.000 25.49000 ? 227 LEU A O   1 
ATOM   1096 C  CB  . LEU A 1 227 ? 7.87800   -8.32300  31.35300 1.000 22.22000 ? 227 LEU A CB  1 
ATOM   1097 C  CG  . LEU A 1 227 ? 9.34300   -8.63600  31.62000 1.000 24.66000 ? 227 LEU A CG  1 
ATOM   1098 C  CD1 . LEU A 1 227 ? 9.62200   -10.11700 31.55500 1.000 26.08000 ? 227 LEU A CD1 1 
ATOM   1099 C  CD2 . LEU A 1 227 ? 10.22400  -7.91800  30.64300 1.000 18.73000 ? 227 LEU A CD2 1 
ATOM   1100 N  N   . ASP A 1 228 ? 5.90800   -7.46600  33.83500 1.000 27.38000 ? 228 ASP A N   1 
ATOM   1101 C  CA  . ASP A 1 228 ? 5.67200   -6.98100  35.22200 1.000 27.17000 ? 228 ASP A CA  1 
ATOM   1102 C  C   . ASP A 1 228 ? 4.87000   -7.98700  36.03200 1.000 30.32000 ? 228 ASP A C   1 
ATOM   1103 O  O   . ASP A 1 228 ? 5.20000   -8.18300  37.15100 1.000 34.49000 ? 228 ASP A O   1 
ATOM   1104 C  CB  . ASP A 1 228 ? 4.99000   -5.63000  35.30000 1.000 30.96000 ? 228 ASP A CB  1 
ATOM   1105 C  CG  . ASP A 1 228 ? 5.82600   -4.49100  34.77600 1.000 42.90000 ? 228 ASP A CG  1 
ATOM   1106 O  OD1 . ASP A 1 228 ? 7.05200   -4.62400  34.73500 1.000 48.18000 ? 228 ASP A OD1 1 
ATOM   1107 O  OD2 . ASP A 1 228 ? 5.24300   -3.50400  34.39700 1.000 43.97000 ? 228 ASP A OD2 1 
ATOM   1108 N  N   . LEU A 1 229 ? 3.85300   -8.59700  35.46000 1.000 26.45000 ? 229 LEU A N   1 
ATOM   1109 C  CA  . LEU A 1 229 ? 3.04900   -9.58100  36.21000 1.000 26.74000 ? 229 LEU A CA  1 
ATOM   1110 C  C   . LEU A 1 229 ? 3.88600   -10.82100 36.55900 1.000 28.52000 ? 229 LEU A C   1 
ATOM   1111 O  O   . LEU A 1 229 ? 3.69500   -11.35100 37.58400 1.000 29.66000 ? 229 LEU A O   1 
ATOM   1112 C  CB  . LEU A 1 229 ? 1.70200   -9.81100  35.54100 1.000 25.08000 ? 229 LEU A CB  1 
ATOM   1113 C  CG  . LEU A 1 229 ? 0.82700   -8.56400  35.47800 1.000 27.63000 ? 229 LEU A CG  1 
ATOM   1114 C  CD1 . LEU A 1 229 ? -0.33400  -8.72300  34.54900 1.000 21.65000 ? 229 LEU A CD1 1 
ATOM   1115 C  CD2 . LEU A 1 229 ? 0.33900   -8.14000  36.83800 1.000 29.66000 ? 229 LEU A CD2 1 
ATOM   1116 N  N   . LEU A 1 230 ? 4.79500   -11.24300 35.70200 1.000 24.68000 ? 230 LEU A N   1 
ATOM   1117 C  CA  . LEU A 1 230 ? 5.69000   -12.38400 36.00100 1.000 32.04000 ? 230 LEU A CA  1 
ATOM   1118 C  C   . LEU A 1 230 ? 6.82800   -12.01500 36.95800 1.000 34.07000 ? 230 LEU A C   1 
ATOM   1119 O  O   . LEU A 1 230 ? 7.47300   -12.89800 37.36800 1.000 31.89000 ? 230 LEU A O   1 
ATOM   1120 C  CB  . LEU A 1 230 ? 6.33500   -12.87700 34.70800 1.000 26.31000 ? 230 LEU A CB  1 
ATOM   1121 C  CG  . LEU A 1 230 ? 5.53800   -13.81500 33.83700 1.000 24.86000 ? 230 LEU A CG  1 
ATOM   1122 C  CD1 . LEU A 1 230 ? 6.34400   -14.11900 32.61700 1.000 27.93000 ? 230 LEU A CD1 1 
ATOM   1123 C  CD2 . LEU A 1 230 ? 5.22100   -15.08900 34.55800 1.000 28.60000 ? 230 LEU A CD2 1 
ATOM   1124 N  N   . SER A 1 231 ? 7.07900   -10.75400 37.25300 1.000 33.19000 ? 231 SER A N   1 
ATOM   1125 C  CA  . SER A 1 231 ? 8.30900   -10.49000 38.03200 1.000 38.49000 ? 231 SER A CA  1 
ATOM   1126 C  C   . SER A 1 231 ? 8.20800   -10.15100 39.52000 1.000 45.38000 ? 231 SER A C   1 
ATOM   1127 O  O   . SER A 1 231 ? 9.21900   -10.22000 40.12700 1.000 59.23000 ? 231 SER A O   1 
ATOM   1128 C  CB  . SER A 1 231 ? 9.21900   -9.59500  37.28800 1.000 40.46000 ? 231 SER A CB  1 
ATOM   1129 O  OG  . SER A 1 231 ? 9.57700   -10.21200 36.07500 1.000 38.53000 ? 231 SER A OG  1 
ATOM   1130 N  N   . PRO A 1 232 ? 7.07800   -9.95500  40.20200 1.000 46.84000 ? 232 PRO A N   1 
ATOM   1131 C  CA  . PRO A 1 232 ? 7.12100   -9.56500  41.60300 1.000 53.16000 ? 232 PRO A CA  1 
ATOM   1132 C  C   . PRO A 1 232 ? 7.24400   -10.74300 42.56900 1.000 52.85000 ? 232 PRO A C   1 
ATOM   1133 O  O   . PRO A 1 232 ? 8.21400   -10.74000 43.25800 1.000 59.06000 ? 232 PRO A O   1 
ATOM   1134 C  CB  . PRO A 1 232 ? 5.76100   -8.95500  41.87600 1.000 51.01000 ? 232 PRO A CB  1 
ATOM   1135 C  CG  . PRO A 1 232 ? 5.01000   -9.09300  40.57400 1.000 54.51000 ? 232 PRO A CG  1 
ATOM   1136 C  CD  . PRO A 1 232 ? 5.73700   -10.12500 39.74300 1.000 48.66000 ? 232 PRO A CD  1 
ATOM   1137 N  N   . ASP B 1 88  ? -29.72400 8.66900   11.16800 1.000 59.56000 ? 88  ASP B N   1 
ATOM   1138 C  CA  . ASP B 1 88  ? -30.39400 7.35600   11.26700 1.000 60.11000 ? 88  ASP B CA  1 
ATOM   1139 C  C   . ASP B 1 88  ? -29.69600 6.37700   10.35200 1.000 56.45000 ? 88  ASP B C   1 
ATOM   1140 O  O   . ASP B 1 88  ? -29.42600 5.29800   10.79100 1.000 55.93000 ? 88  ASP B O   1 
ATOM   1141 C  CB  . ASP B 1 88  ? -31.86900 7.38800   10.89800 1.000 64.67000 ? 88  ASP B CB  1 
ATOM   1142 C  CG  . ASP B 1 88  ? -32.53000 6.04300   11.15800 1.000 69.26000 ? 88  ASP B CG  1 
ATOM   1143 O  OD1 . ASP B 1 88  ? -32.18900 5.07400   10.46600 1.000 66.89000 ? 88  ASP B OD1 1 
ATOM   1144 O  OD2 . ASP B 1 88  ? -33.36200 5.98000   12.05000 1.000 71.50000 ? 88  ASP B OD2 1 
ATOM   1145 N  N   . ARG B 1 89  ? -29.51200 6.72600   9.09000  1.000 53.45000 ? 89  ARG B N   1 
ATOM   1146 C  CA  . ARG B 1 89  ? -28.70100 5.84300   8.21200  1.000 52.52000 ? 89  ARG B CA  1 
ATOM   1147 C  C   . ARG B 1 89  ? -27.22800 5.93800   8.64400  1.000 52.06000 ? 89  ARG B C   1 
ATOM   1148 O  O   . ARG B 1 89  ? -26.52700 5.02700   8.32800  1.000 48.66000 ? 89  ARG B O   1 
ATOM   1149 C  CB  . ARG B 1 89  ? -28.96900 6.01100   6.71500  1.000 42.25000 ? 89  ARG B CB  1 
ATOM   1150 N  N   . GLU B 1 90  ? -26.80500 7.10300   9.15300  1.000 51.67000 ? 90  GLU B N   1 
ATOM   1151 C  CA  . GLU B 1 90  ? -25.46900 7.40500   9.72900  1.000 52.36000 ? 90  GLU B CA  1 
ATOM   1152 C  C   . GLU B 1 90  ? -25.35300 6.93200   11.18800 1.000 52.50000 ? 90  GLU B C   1 
ATOM   1153 O  O   . GLU B 1 90  ? -24.25600 6.94300   11.71600 1.000 47.54000 ? 90  GLU B O   1 
ATOM   1154 C  CB  . GLU B 1 90  ? -25.15300 8.88700   9.61800  1.000 53.87000 ? 90  GLU B CB  1 
ATOM   1155 C  CG  . GLU B 1 90  ? -24.79000 9.36500   8.22700  1.000 56.08000 ? 90  GLU B CG  1 
ATOM   1156 C  CD  . GLU B 1 90  ? -24.55600 10.86000  8.25500  1.000 54.50000 ? 90  GLU B CD  1 
ATOM   1157 O  OE1 . GLU B 1 90  ? -25.02200 11.47300  9.21500  1.000 54.31000 ? 90  GLU B OE1 1 
ATOM   1158 O  OE2 . GLU B 1 90  ? -23.90500 11.38200  7.37000  1.000 46.90000 ? 90  GLU B OE2 1 
ATOM   1159 N  N   . GLN B 1 91  ? -26.45300 6.77600   11.90100 1.000 51.60000 ? 91  GLN B N   1 
ATOM   1160 C  CA  . GLN B 1 91  ? -26.32600 6.14300   13.23400 1.000 48.39000 ? 91  GLN B CA  1 
ATOM   1161 C  C   . GLN B 1 91  ? -26.00900 4.66500   12.97900 1.000 45.51000 ? 91  GLN B C   1 
ATOM   1162 O  O   . GLN B 1 91  ? -25.16100 4.09100   13.63900 1.000 43.21000 ? 91  GLN B O   1 
ATOM   1163 C  CB  . GLN B 1 91  ? -27.59800 6.35200   14.04400 1.000 50.40000 ? 91  GLN B CB  1 
ATOM   1164 N  N   . LEU B 1 92  ? -26.68600 4.09400   12.00500 1.000 40.41000 ? 92  LEU B N   1 
ATOM   1165 C  CA  . LEU B 1 92  ? -26.49300 2.69600   11.59600 1.000 40.53000 ? 92  LEU B CA  1 
ATOM   1166 C  C   . LEU B 1 92  ? -25.10900 2.57000   11.00000 1.000 40.43000 ? 92  LEU B C   1 
ATOM   1167 O  O   . LEU B 1 92  ? -24.40200 1.65700   11.33600 1.000 39.87000 ? 92  LEU B O   1 
ATOM   1168 C  CB  . LEU B 1 92  ? -27.52400 2.40200   10.51300 1.000 44.37000 ? 92  LEU B CB  1 
ATOM   1169 C  CG  . LEU B 1 92  ? -27.88000 0.95500   10.21600 1.000 39.48000 ? 92  LEU B CG  1 
ATOM   1170 C  CD1 . LEU B 1 92  ? -27.95800 0.15500   11.47600 1.000 35.03000 ? 92  LEU B CD1 1 
ATOM   1171 C  CD2 . LEU B 1 92  ? -29.20700 0.92400   9.51200  1.000 35.24000 ? 92  LEU B CD2 1 
ATOM   1172 N  N   . ALA B 1 93  ? -24.73800 3.53700   10.18900 1.000 37.40000 ? 93  ALA B N   1 
ATOM   1173 C  CA  . ALA B 1 93  ? -23.45700 3.45700   9.46700  1.000 42.44000 ? 93  ALA B CA  1 
ATOM   1174 C  C   . ALA B 1 93  ? -22.25600 3.42600   10.42000 1.000 33.74000 ? 93  ALA B C   1 
ATOM   1175 O  O   . ALA B 1 93  ? -21.29600 2.88700   10.02600 1.000 28.48000 ? 93  ALA B O   1 
ATOM   1176 C  CB  . ALA B 1 93  ? -23.34900 4.52200   8.41000  1.000 39.55000 ? 93  ALA B CB  1 
ATOM   1177 N  N   . SER B 1 94  ? -22.36200 4.10400   11.54500 1.000 31.93000 ? 94  SER B N   1 
ATOM   1178 C  CA  . SER B 1 94  ? -21.34100 4.18800   12.60400 1.000 32.36000 ? 94  SER B CA  1 
ATOM   1179 C  C   . SER B 1 94  ? -21.07600 2.81600   13.23000 1.000 31.58000 ? 94  SER B C   1 
ATOM   1180 O  O   . SER B 1 94  ? -19.95500 2.55200   13.56300 1.000 28.57000 ? 94  SER B O   1 
ATOM   1181 C  CB  . SER B 1 94  ? -21.74700 5.19700   13.61000 1.000 35.78000 ? 94  SER B CB  1 
ATOM   1182 O  OG  . SER B 1 94  ? -21.42800 6.48600   13.16100 1.000 37.73000 ? 94  SER B OG  1 
ATOM   1183 N  N   . VAL B 1 95  ? -22.13000 2.04500   13.48300 1.000 32.32000 ? 95  VAL B N   1 
ATOM   1184 C  CA  . VAL B 1 95  ? -22.02800 0.64900   13.97800 1.000 30.62000 ? 95  VAL B CA  1 
ATOM   1185 C  C   . VAL B 1 95  ? -21.42400 -0.20100  12.86300 1.000 30.31000 ? 95  VAL B C   1 
ATOM   1186 O  O   . VAL B 1 95  ? -20.60200 -1.00400  13.12000 1.000 28.52000 ? 95  VAL B O   1 
ATOM   1187 C  CB  . VAL B 1 95  ? -23.36800 0.09600   14.49200 1.000 29.88000 ? 95  VAL B CB  1 
ATOM   1188 C  CG1 . VAL B 1 95  ? -23.21600 -1.34600  14.88300 1.000 28.30000 ? 95  VAL B CG1 1 
ATOM   1189 C  CG2 . VAL B 1 95  ? -23.85700 0.89500   15.67900 1.000 32.78000 ? 95  VAL B CG2 1 
ATOM   1190 N  N   . TYR B 1 96  ? -21.85100 0.03900   11.63900 1.000 32.63000 ? 96  TYR B N   1 
ATOM   1191 C  CA  . TYR B 1 96  ? -21.33800 -0.79600  10.53800 1.000 32.74000 ? 96  TYR B CA  1 
ATOM   1192 C  C   . TYR B 1 96  ? -19.83300 -0.61500  10.38400 1.000 29.80000 ? 96  TYR B C   1 
ATOM   1193 O  O   . TYR B 1 96  ? -19.18900 -1.56900  10.09600 1.000 28.71000 ? 96  TYR B O   1 
ATOM   1194 C  CB  . TYR B 1 96  ? -22.08600 -0.52500  9.24000  1.000 37.33000 ? 96  TYR B CB  1 
ATOM   1195 C  CG  . TYR B 1 96  ? -23.08200 -1.58200  8.84600  1.000 44.12000 ? 96  TYR B CG  1 
ATOM   1196 C  CD1 . TYR B 1 96  ? -22.67500 -2.77000  8.28500  1.000 47.19000 ? 96  TYR B CD1 1 
ATOM   1197 C  CD2 . TYR B 1 96  ? -24.43100 -1.37700  9.00200  1.000 43.81000 ? 96  TYR B CD2 1 
ATOM   1198 C  CE1 . TYR B 1 96  ? -23.58800 -3.73100  7.88800  1.000 51.67000 ? 96  TYR B CE1 1 
ATOM   1199 C  CE2 . TYR B 1 96  ? -25.35500 -2.32900  8.63500  1.000 46.48000 ? 96  TYR B CE2 1 
ATOM   1200 C  CZ  . TYR B 1 96  ? -24.93700 -3.51300  8.07800  1.000 54.34000 ? 96  TYR B CZ  1 
ATOM   1201 O  OH  . TYR B 1 96  ? -25.86300 -4.44900  7.71400  1.000 64.80000 ? 96  TYR B OH  1 
ATOM   1202 N  N   . GLU B 1 97  ? -19.34800 0.60700   10.52400 1.000 25.40000 ? 97  GLU B N   1 
ATOM   1203 C  CA  . GLU B 1 97  ? -17.91500 0.94400   10.42800 1.000 30.18000 ? 97  GLU B CA  1 
ATOM   1204 C  C   . GLU B 1 97  ? -17.13000 0.20400   11.52100 1.000 22.97000 ? 97  GLU B C   1 
ATOM   1205 O  O   . GLU B 1 97  ? -16.19500 -0.43800  11.15300 1.000 24.25000 ? 97  GLU B O   1 
ATOM   1206 C  CB  . GLU B 1 97  ? -17.83400 2.46600   10.53700 1.000 33.51000 ? 97  GLU B CB  1 
ATOM   1207 C  CG  . GLU B 1 97  ? -16.48400 3.11800   10.59400 1.000 34.86000 ? 97  GLU B CG  1 
ATOM   1208 C  CD  . GLU B 1 97  ? -16.55700 4.62400   10.33300 1.000 35.72000 ? 97  GLU B CD  1 
ATOM   1209 O  OE1 . GLU B 1 97  ? -16.34500 5.00700   9.22500  1.000 36.65000 ? 97  GLU B OE1 1 
ATOM   1210 O  OE2 . GLU B 1 97  ? -16.88300 5.36100   11.19700 1.000 30.24000 ? 97  GLU B OE2 1 
ATOM   1211 N  N   . LEU B 1 98  ? -17.58400 0.25700   12.77200 1.000 20.62000 ? 98  LEU B N   1 
ATOM   1212 C  CA  . LEU B 1 98  ? -16.92400 -0.41400  13.91700 1.000 21.73000 ? 98  LEU B CA  1 
ATOM   1213 C  C   . LEU B 1 98  ? -16.91800 -1.93600  13.71700 1.000 24.15000 ? 98  LEU B C   1 
ATOM   1214 O  O   . LEU B 1 98  ? -15.91700 -2.53700  13.97400 1.000 19.21000 ? 98  LEU B O   1 
ATOM   1215 C  CB  . LEU B 1 98  ? -17.62800 -0.03400  15.21500 1.000 17.33000 ? 98  LEU B CB  1 
ATOM   1216 C  CG  . LEU B 1 98  ? -17.03300 -0.62100  16.48800 1.000 19.30000 ? 98  LEU B CG  1 
ATOM   1217 C  CD1 . LEU B 1 98  ? -15.64100 -0.08200  16.71500 1.000 21.24000 ? 98  LEU B CD1 1 
ATOM   1218 C  CD2 . LEU B 1 98  ? -17.90100 -0.32500  17.67900 1.000 17.78000 ? 98  LEU B CD2 1 
ATOM   1219 N  N   . ARG B 1 99  ? -18.01100 -2.50200  13.22300 1.000 25.25000 ? 99  ARG B N   1 
ATOM   1220 C  CA  . ARG B 1 99  ? -18.09500 -3.95700  12.98700 1.000 24.84000 ? 99  ARG B CA  1 
ATOM   1221 C  C   . ARG B 1 99  ? -17.09400 -4.34800  11.91400 1.000 23.56000 ? 99  ARG B C   1 
ATOM   1222 O  O   . ARG B 1 99  ? -16.45900 -5.34900  12.05700 1.000 24.95000 ? 99  ARG B O   1 
ATOM   1223 C  CB  . ARG B 1 99  ? -19.50300 -4.39000  12.58900 1.000 30.26000 ? 99  ARG B CB  1 
ATOM   1224 C  CG  . ARG B 1 99  ? -19.69800 -5.89200  12.65300 1.000 31.99000 ? 99  ARG B CG  1 
ATOM   1225 C  CD  . ARG B 1 99  ? -19.86400 -6.61900  11.34500 1.000 36.53000 ? 99  ARG B CD  1 
ATOM   1226 N  NE  . ARG B 1 99  ? -21.26300 -6.56600  11.01300 1.000 38.48000 ? 99  ARG B NE  1 
ATOM   1227 C  CZ  . ARG B 1 99  ? -21.76700 -6.09900  9.89500  1.000 44.99000 ? 99  ARG B CZ  1 
ATOM   1228 N  NH1 . ARG B 1 99  ? -20.98700 -5.67700  8.92100  1.000 45.78000 ? 99  ARG B NH1 1 
ATOM   1229 N  NH2 . ARG B 1 99  ? -23.06300 -6.07100  9.73500  1.000 42.67000 ? 99  ARG B NH2 1 
ATOM   1230 N  N   . MET B 1 100 ? -16.96900 -3.51200  10.90000 1.000 26.06000 ? 100 MET B N   1 
ATOM   1231 C  CA  . MET B 1 100 ? -16.04600 -3.77100  9.77900  1.000 27.97000 ? 100 MET B CA  1 
ATOM   1232 C  C   . MET B 1 100 ? -14.62500 -3.88700  10.31500 1.000 24.68000 ? 100 MET B C   1 
ATOM   1233 O  O   . MET B 1 100 ? -13.96900 -4.80500  9.91800  1.000 27.97000 ? 100 MET B O   1 
ATOM   1234 C  CB  . MET B 1 100 ? -16.09700 -2.62800  8.76700  1.000 25.22000 ? 100 MET B CB  1 
ATOM   1235 C  CG  . MET B 1 100 ? -15.09500 -2.78400  7.66600  1.000 26.66000 ? 100 MET B CG  1 
ATOM   1236 S  SD  . MET B 1 100 ? -15.43500 -1.77500  6.25300  1.000 46.94000 ? 100 MET B SD  1 
ATOM   1237 C  CE  . MET B 1 100 ? -17.22000 -1.79800  6.22100  1.000 32.12000 ? 100 MET B CE  1 
ATOM   1238 N  N   . GLU B 1 101 ? -14.21200 -2.99700  11.20400 1.000 23.04000 ? 101 GLU B N   1 
ATOM   1239 C  CA  . GLU B 1 101 ? -12.84200 -3.01700  11.76700 1.000 25.37000 ? 101 GLU B CA  1 
ATOM   1240 C  C   . GLU B 1 101 ? -12.60300 -4.28200  12.58400 1.000 25.33000 ? 101 GLU B C   1 
ATOM   1241 O  O   . GLU B 1 101 ? -11.59600 -4.90300  12.36900 1.000 27.50000 ? 101 GLU B O   1 
ATOM   1242 C  CB  . GLU B 1 101 ? -12.63600 -1.80800  12.66900 1.000 24.35000 ? 101 GLU B CB  1 
ATOM   1243 C  CG  . GLU B 1 101 ? -12.29600 -0.56400  11.90100 1.000 29.63000 ? 101 GLU B CG  1 
ATOM   1244 C  CD  . GLU B 1 101 ? -11.08600 -0.79600  11.02900 1.000 33.97000 ? 101 GLU B CD  1 
ATOM   1245 O  OE1 . GLU B 1 101 ? -10.15200 -1.42200  11.49700 1.000 34.13000 ? 101 GLU B OE1 1 
ATOM   1246 O  OE2 . GLU B 1 101 ? -11.12300 -0.42500  9.89000  1.000 34.59000 ? 101 GLU B OE2 1 
ATOM   1247 N  N   . LEU B 1 102 ? -13.54400 -4.62600  13.45300 1.000 21.86000 ? 102 LEU B N   1 
ATOM   1248 C  CA  . LEU B 1 102 ? -13.48200 -5.81300  14.33600 1.000 24.20000 ? 102 LEU B CA  1 
ATOM   1249 C  C   . LEU B 1 102 ? -13.54800 -7.11300  13.54300 1.000 24.33000 ? 102 LEU B C   1 
ATOM   1250 O  O   . LEU B 1 102 ? -12.76600 -7.96000  13.83900 1.000 27.32000 ? 102 LEU B O   1 
ATOM   1251 C  CB  . LEU B 1 102 ? -14.67800 -5.76300  15.27300 1.000 30.00000 ? 102 LEU B CB  1 
ATOM   1252 C  CG  . LEU B 1 102 ? -14.48100 -4.91800  16.50300 1.000 30.00000 ? 102 LEU B CG  1 
ATOM   1253 C  CD1 . LEU B 1 102 ? -15.70000 -5.00900  17.38600 1.000 30.00000 ? 102 LEU B CD1 1 
ATOM   1254 C  CD2 . LEU B 1 102 ? -13.20200 -5.36200  17.18200 1.000 30.00000 ? 102 LEU B CD2 1 
ATOM   1255 N  N   . GLU B 1 103 ? -14.42500 -7.21300  12.54600 1.000 21.28000 ? 103 GLU B N   1 
ATOM   1256 C  CA  . GLU B 1 103 ? -14.53100 -8.45300  11.73300 1.000 27.37000 ? 103 GLU B CA  1 
ATOM   1257 C  C   . GLU B 1 103 ? -13.21700 -8.70700  11.00000 1.000 25.06000 ? 103 GLU B C   1 
ATOM   1258 O  O   . GLU B 1 103 ? -12.80800 -9.83800  10.94400 1.000 24.70000 ? 103 GLU B O   1 
ATOM   1259 C  CB  . GLU B 1 103 ? -15.70200 -8.42400  10.75400 1.000 29.69000 ? 103 GLU B CB  1 
ATOM   1260 C  CG  . GLU B 1 103 ? -17.03600 -8.70700  11.40600 1.000 35.63000 ? 103 GLU B CG  1 
ATOM   1261 C  CD  . GLU B 1 103 ? -17.77500 -9.99900  11.11300 1.000 35.33000 ? 103 GLU B CD  1 
ATOM   1262 O  OE1 . GLU B 1 103 ? -17.17300 -10.93200 10.57400 1.000 40.88000 ? 103 GLU B OE1 1 
ATOM   1263 O  OE2 . GLU B 1 103 ? -18.95800 -10.04500 11.42300 1.000 38.74000 ? 103 GLU B OE2 1 
ATOM   1264 N  N   . GLY B 1 104 ? -12.57700 -7.65500  10.50600 1.000 24.59000 ? 104 GLY B N   1 
ATOM   1265 C  CA  . GLY B 1 104 ? -11.28400 -7.78400  9.82200  1.000 22.25000 ? 104 GLY B CA  1 
ATOM   1266 C  C   . GLY B 1 104 ? -10.26400 -8.36900  10.76500 1.000 24.81000 ? 104 GLY B C   1 
ATOM   1267 O  O   . GLY B 1 104 ? -9.58000  -9.26700  10.36200 1.000 25.10000 ? 104 GLY B O   1 
ATOM   1268 N  N   . GLY B 1 105 ? -10.24500 -7.88900  12.00100 1.000 24.79000 ? 105 GLY B N   1 
ATOM   1269 C  CA  . GLY B 1 105 ? -9.37700  -8.38900  13.07800 1.000 30.91000 ? 105 GLY B CA  1 
ATOM   1270 C  C   . GLY B 1 105 ? -9.69300  -9.80800  13.51000 1.000 27.28000 ? 105 GLY B C   1 
ATOM   1271 O  O   . GLY B 1 105 ? -8.78100  -10.50200 13.86700 1.000 27.72000 ? 105 GLY B O   1 
ATOM   1272 N  N   . ALA B 1 106 ? -10.96600 -10.17100 13.55800 1.000 22.88000 ? 106 ALA B N   1 
ATOM   1273 C  CA  . ALA B 1 106 ? -11.38000 -11.52600 13.97100 1.000 21.10000 ? 106 ALA B CA  1 
ATOM   1274 C  C   . ALA B 1 106 ? -10.86400 -12.56200 12.98400 1.000 20.63000 ? 106 ALA B C   1 
ATOM   1275 O  O   . ALA B 1 106 ? -10.37400 -13.54100 13.41900 1.000 20.02000 ? 106 ALA B O   1 
ATOM   1276 C  CB  . ALA B 1 106 ? -12.87100 -11.61400 14.10600 1.000 23.97000 ? 106 ALA B CB  1 
ATOM   1277 N  N   . ALA B 1 107 ? -10.96100 -12.28300 11.69600 1.000 26.19000 ? 107 ALA B N   1 
ATOM   1278 C  CA  . ALA B 1 107 ? -10.46800 -13.18700 10.64300 1.000 22.47000 ? 107 ALA B CA  1 
ATOM   1279 C  C   . ALA B 1 107 ? -8.94600  -13.37000 10.75400 1.000 24.49000 ? 107 ALA B C   1 
ATOM   1280 O  O   . ALA B 1 107 ? -8.48900  -14.39700 10.39800 1.000 23.49000 ? 107 ALA B O   1 
ATOM   1281 C  CB  . ALA B 1 107 ? -10.91200 -12.71200 9.30400  1.000 17.39000 ? 107 ALA B CB  1 
ATOM   1282 N  N   . ALA B 1 108 ? -8.20700  -12.31900 11.10600 1.000 27.66000 ? 108 ALA B N   1 
ATOM   1283 C  CA  . ALA B 1 108 ? -6.74500  -12.36500 11.30100 1.000 23.97000 ? 108 ALA B CA  1 
ATOM   1284 C  C   . ALA B 1 108 ? -6.35700  -13.27000 12.46900 1.000 25.56000 ? 108 ALA B C   1 
ATOM   1285 O  O   . ALA B 1 108 ? -5.44800  -13.99700 12.31300 1.000 25.69000 ? 108 ALA B O   1 
ATOM   1286 C  CB  . ALA B 1 108 ? -6.22900  -10.97800 11.51600 1.000 27.10000 ? 108 ALA B CB  1 
ATOM   1287 N  N   . LEU B 1 109 ? -7.03500  -13.15800 13.59900 1.000 25.10000 ? 109 LEU B N   1 
ATOM   1288 C  CA  . LEU B 1 109 ? -6.78700  -13.98800 14.78800 1.000 24.26000 ? 109 LEU B CA  1 
ATOM   1289 C  C   . LEU B 1 109 ? -7.14400  -15.43100 14.46200 1.000 27.56000 ? 109 LEU B C   1 
ATOM   1290 O  O   . LEU B 1 109 ? -6.37100  -16.25800 14.78500 1.000 31.90000 ? 109 LEU B O   1 
ATOM   1291 C  CB  . LEU B 1 109 ? -7.59200  -13.46900 15.97400 1.000 22.04000 ? 109 LEU B CB  1 
ATOM   1292 C  CG  . LEU B 1 109 ? -7.19000  -12.10600 16.51800 1.000 26.03000 ? 109 LEU B CG  1 
ATOM   1293 C  CD1 . LEU B 1 109 ? -8.05800  -11.69900 17.66900 1.000 20.88000 ? 109 LEU B CD1 1 
ATOM   1294 C  CD2 . LEU B 1 109 ? -5.74300  -12.08000 16.94200 1.000 31.92000 ? 109 LEU B CD2 1 
ATOM   1295 N  N   . ALA B 1 110 ? -8.25900  -15.65000 13.76600 1.000 26.38000 ? 110 ALA B N   1 
ATOM   1296 C  CA  . ALA B 1 110 ? -8.79100  -16.96900 13.36000 1.000 26.78000 ? 110 ALA B CA  1 
ATOM   1297 C  C   . ALA B 1 110 ? -7.84000  -17.63500 12.38100 1.000 29.38000 ? 110 ALA B C   1 
ATOM   1298 O  O   . ALA B 1 110 ? -7.76800  -18.81000 12.38100 1.000 31.94000 ? 110 ALA B O   1 
ATOM   1299 C  CB  . ALA B 1 110 ? -10.19500 -16.90700 12.83800 1.000 18.65000 ? 110 ALA B CB  1 
ATOM   1300 N  N   . ALA B 1 111 ? -7.18000  -16.85900 11.54700 1.000 26.76000 ? 111 ALA B N   1 
ATOM   1301 C  CA  . ALA B 1 111 ? -6.20100  -17.39800 10.60000 1.000 31.46000 ? 111 ALA B CA  1 
ATOM   1302 C  C   . ALA B 1 111 ? -5.05600  -18.07200 11.37700 1.000 35.13000 ? 111 ALA B C   1 
ATOM   1303 O  O   . ALA B 1 111 ? -4.61500  -19.11100 10.95900 1.000 32.09000 ? 111 ALA B O   1 
ATOM   1304 C  CB  . ALA B 1 111 ? -5.71500  -16.29000 9.72400  1.000 29.22000 ? 111 ALA B CB  1 
ATOM   1305 N  N   . ARG B 1 112 ? -4.61500  -17.48200 12.47700 1.000 33.27000 ? 112 ARG B N   1 
ATOM   1306 C  CA  . ARG B 1 112 ? -3.53300  -18.09200 13.26200 1.000 31.91000 ? 112 ARG B CA  1 
ATOM   1307 C  C   . ARG B 1 112 ? -4.02000  -19.04500 14.34900 1.000 31.07000 ? 112 ARG B C   1 
ATOM   1308 O  O   . ARG B 1 112 ? -3.28000  -19.87800 14.66000 1.000 40.59000 ? 112 ARG B O   1 
ATOM   1309 C  CB  . ARG B 1 112 ? -2.60400  -17.01800 13.82400 1.000 33.16000 ? 112 ARG B CB  1 
ATOM   1310 C  CG  . ARG B 1 112 ? -3.09100  -16.36000 15.09400 1.000 31.23000 ? 112 ARG B CG  1 
ATOM   1311 C  CD  . ARG B 1 112 ? -2.11700  -15.28300 15.51300 1.000 35.64000 ? 112 ARG B CD  1 
ATOM   1312 N  N   . ARG B 1 113 ? -5.21400  -18.92600 14.89300 1.000 30.45000 ? 113 ARG B N   1 
ATOM   1313 C  CA  . ARG B 1 113 ? -5.54200  -19.78800 16.04400 1.000 32.16000 ? 113 ARG B CA  1 
ATOM   1314 C  C   . ARG B 1 113 ? -6.55800  -20.89700 15.75500 1.000 34.17000 ? 113 ARG B C   1 
ATOM   1315 O  O   . ARG B 1 113 ? -6.87400  -21.60800 16.68700 1.000 29.80000 ? 113 ARG B O   1 
ATOM   1316 C  CB  . ARG B 1 113 ? -6.11900  -18.90000 17.14300 1.000 34.85000 ? 113 ARG B CB  1 
ATOM   1317 C  CG  . ARG B 1 113 ? -5.13800  -17.90000 17.71600 1.000 32.60000 ? 113 ARG B CG  1 
ATOM   1318 C  CD  . ARG B 1 113 ? -5.61300  -17.28300 18.98800 1.000 33.32000 ? 113 ARG B CD  1 
ATOM   1319 N  NE  . ARG B 1 113 ? -5.02700  -15.97000 19.04700 1.000 40.77000 ? 113 ARG B NE  1 
ATOM   1320 C  CZ  . ARG B 1 113 ? -4.84900  -15.28400 20.15400 1.000 42.43000 ? 113 ARG B CZ  1 
ATOM   1321 N  NH1 . ARG B 1 113 ? -4.26600  -14.10800 20.11700 1.000 41.49000 ? 113 ARG B NH1 1 
ATOM   1322 N  NH2 . ARG B 1 113 ? -5.20200  -15.78700 21.30800 1.000 43.66000 ? 113 ARG B NH2 1 
ATOM   1323 N  N   . ARG B 1 114 ? -6.98700  -21.06700 14.51700 1.000 32.25000 ? 114 ARG B N   1 
ATOM   1324 C  CA  . ARG B 1 114 ? -8.10000  -22.01000 14.22200 1.000 39.41000 ? 114 ARG B CA  1 
ATOM   1325 C  C   . ARG B 1 114 ? -7.76800  -23.46500 14.52400 1.000 34.13000 ? 114 ARG B C   1 
ATOM   1326 O  O   . ARG B 1 114 ? -6.86600  -24.01600 13.97100 1.000 34.95000 ? 114 ARG B O   1 
ATOM   1327 C  CB  . ARG B 1 114 ? -8.40200  -22.00300 12.72800 1.000 34.55000 ? 114 ARG B CB  1 
ATOM   1328 C  CG  . ARG B 1 114 ? -7.11200  -22.28900 11.99000 1.000 36.94000 ? 114 ARG B CG  1 
ATOM   1329 C  CD  . ARG B 1 114 ? -7.12200  -22.31600 10.51600 1.000 35.84000 ? 114 ARG B CD  1 
ATOM   1330 N  NE  . ARG B 1 114 ? -5.93000  -22.82100 9.92800  1.000 38.85000 ? 114 ARG B NE  1 
ATOM   1331 C  CZ  . ARG B 1 114 ? -5.31200  -23.93900 10.21400 1.000 37.73000 ? 114 ARG B CZ  1 
ATOM   1332 N  NH1 . ARG B 1 114 ? -5.71200  -24.73900 11.17500 1.000 36.56000 ? 114 ARG B NH1 1 
ATOM   1333 N  NH2 . ARG B 1 114 ? -4.27400  -24.26600 9.49800  1.000 45.48000 ? 114 ARG B NH2 1 
ATOM   1334 N  N   . ASN B 1 115 ? -8.67400  -24.06900 15.23700 1.000 37.23000 ? 115 ASN B N   1 
ATOM   1335 C  CA  . ASN B 1 115 ? -8.65900  -25.50800 15.56000 1.000 31.67000 ? 115 ASN B CA  1 
ATOM   1336 C  C   . ASN B 1 115 ? -9.22700  -26.28800 14.39400 1.000 36.05000 ? 115 ASN B C   1 
ATOM   1337 O  O   . ASN B 1 115 ? -9.82500  -25.70700 13.53100 1.000 38.78000 ? 115 ASN B O   1 
ATOM   1338 C  CB  . ASN B 1 115 ? -9.85700  -25.84700 16.43100 1.000 29.61000 ? 115 ASN B CB  1 
ATOM   1339 C  CG  . ASN B 1 115 ? -9.54500  -25.83900 17.88400 1.000 35.69000 ? 115 ASN B CG  1 
ATOM   1340 O  OD1 . ASN B 1 115 ? -8.42200  -26.07700 18.24000 1.000 43.87000 ? 115 ASN B OD1 1 
ATOM   1341 N  ND2 . ASN B 1 115 ? -10.52600 -25.62300 18.72000 1.000 37.22000 ? 115 ASN B ND2 1 
ATOM   1342 N  N   . ALA B 1 116 ? -9.08600  -27.60700 14.45600 1.000 42.17000 ? 116 ALA B N   1 
ATOM   1343 C  CA  . ALA B 1 116 ? -9.81000  -28.53600 13.57200 1.000 37.22000 ? 116 ALA B CA  1 
ATOM   1344 C  C   . ALA B 1 116 ? -11.29300 -28.37900 13.91100 1.000 33.73000 ? 116 ALA B C   1 
ATOM   1345 O  O   . ALA B 1 116 ? -12.05300 -28.42600 13.02100 1.000 38.56000 ? 116 ALA B O   1 
ATOM   1346 C  CB  . ALA B 1 116 ? -9.33400  -29.93900 13.80400 1.000 36.54000 ? 116 ALA B CB  1 
ATOM   1347 N  N   . THR B 1 117 ? -11.66500 -28.21900 15.17100 1.000 32.75000 ? 117 THR B N   1 
ATOM   1348 C  CA  . THR B 1 117 ? -13.06900 -27.95500 15.55900 1.000 32.14000 ? 117 THR B CA  1 
ATOM   1349 C  C   . THR B 1 117 ? -13.54500 -26.64800 14.91800 1.000 34.18000 ? 117 THR B C   1 
ATOM   1350 O  O   . THR B 1 117 ? -14.61000 -26.64200 14.36600 1.000 36.06000 ? 117 THR B O   1 
ATOM   1351 C  CB  . THR B 1 117 ? -13.21300 -27.87700 17.07500 1.000 31.52000 ? 117 THR B CB  1 
ATOM   1352 O  OG1 . THR B 1 117 ? -13.03900 -29.19900 17.54800 1.000 34.12000 ? 117 THR B OG1 1 
ATOM   1353 C  CG2 . THR B 1 117 ? -14.55400 -27.36200 17.52800 1.000 24.05000 ? 117 THR B CG2 1 
ATOM   1354 N  N   . ASP B 1 118 ? -12.71900 -25.61300 14.91100 1.000 32.76000 ? 118 ASP B N   1 
ATOM   1355 C  CA  . ASP B 1 118 ? -13.11200 -24.33100 14.29500 1.000 33.05000 ? 118 ASP B CA  1 
ATOM   1356 C  C   . ASP B 1 118 ? -13.29800 -24.55800 12.80800 1.000 32.47000 ? 118 ASP B C   1 
ATOM   1357 O  O   . ASP B 1 118 ? -14.26200 -24.10600 12.27400 1.000 34.03000 ? 118 ASP B O   1 
ATOM   1358 C  CB  . ASP B 1 118 ? -12.12900 -23.20500 14.60600 1.000 29.86000 ? 118 ASP B CB  1 
ATOM   1359 C  CG  . ASP B 1 118 ? -11.95400 -22.86400 16.07700 1.000 32.32000 ? 118 ASP B CG  1 
ATOM   1360 O  OD1 . ASP B 1 118 ? -12.92000 -22.67200 16.76800 1.000 34.59000 ? 118 ASP B OD1 1 
ATOM   1361 O  OD2 . ASP B 1 118 ? -10.85400 -22.79500 16.50300 1.000 31.87000 ? 118 ASP B OD2 1 
ATOM   1362 N  N   . LEU B 1 119 ? -12.41300 -25.31500 12.19400 1.000 31.45000 ? 119 LEU B N   1 
ATOM   1363 C  CA  . LEU B 1 119 ? -12.56500 -25.56200 10.75000 1.000 31.54000 ? 119 LEU B CA  1 
ATOM   1364 C  C   . LEU B 1 119 ? -13.87400 -26.30000 10.44000 1.000 33.74000 ? 119 LEU B C   1 
ATOM   1365 O  O   . LEU B 1 119 ? -14.35000 -26.14800 9.38900  1.000 35.12000 ? 119 LEU B O   1 
ATOM   1366 C  CB  . LEU B 1 119 ? -11.33400 -26.26700 10.20000 1.000 32.48000 ? 119 LEU B CB  1 
ATOM   1367 C  CG  . LEU B 1 119 ? -10.08900 -25.39800 10.06700 1.000 36.68000 ? 119 LEU B CG  1 
ATOM   1368 C  CD1 . LEU B 1 119 ? -8.93700  -26.21400 9.52400  1.000 34.13000 ? 119 LEU B CD1 1 
ATOM   1369 C  CD2 . LEU B 1 119 ? -10.32900 -24.18700 9.19900  1.000 26.00000 ? 119 LEU B CD2 1 
ATOM   1370 N  N   . ALA B 1 120 ? -14.34000 -27.19400 11.28600 1.000 32.44000 ? 120 ALA B N   1 
ATOM   1371 C  CA  . ALA B 1 120 ? -15.59600 -27.90100 10.98500 1.000 33.85000 ? 120 ALA B CA  1 
ATOM   1372 C  C   . ALA B 1 120 ? -16.78400 -26.94500 11.01900 1.000 37.14000 ? 120 ALA B C   1 
ATOM   1373 O  O   . ALA B 1 120 ? -17.51800 -26.89400 10.08100 1.000 36.86000 ? 120 ALA B O   1 
ATOM   1374 C  CB  . ALA B 1 120 ? -15.77400 -29.01400 11.97400 1.000 35.31000 ? 120 ALA B CB  1 
ATOM   1375 N  N   . ALA B 1 121 ? -16.86600 -26.12800 12.04200 1.000 34.65000 ? 121 ALA B N   1 
ATOM   1376 C  CA  . ALA B 1 121 ? -17.99400 -25.19600 12.13700 1.000 35.13000 ? 121 ALA B CA  1 
ATOM   1377 C  C   . ALA B 1 121 ? -18.00100 -24.24100 10.93600 1.000 34.08000 ? 121 ALA B C   1 
ATOM   1378 O  O   . ALA B 1 121 ? -19.04600 -23.98400 10.43400 1.000 32.83000 ? 121 ALA B O   1 
ATOM   1379 C  CB  . ALA B 1 121 ? -17.91900 -24.47300 13.44900 1.000 34.50000 ? 121 ALA B CB  1 
ATOM   1380 N  N   . MET B 1 122 ? -16.85900 -23.74100 10.49900 1.000 32.88000 ? 122 MET B N   1 
ATOM   1381 C  CA  . MET B 1 122 ? -16.89300 -22.86900 9.31200  1.000 28.10000 ? 122 MET B CA  1 
ATOM   1382 C  C   . MET B 1 122 ? -17.29100 -23.68200 8.08600  1.000 33.85000 ? 122 MET B C   1 
ATOM   1383 O  O   . MET B 1 122 ? -17.88900 -23.10700 7.22100  1.000 31.18000 ? 122 MET B O   1 
ATOM   1384 C  CB  . MET B 1 122 ? -15.56300 -22.18900 9.04000  1.000 29.89000 ? 122 MET B CB  1 
ATOM   1385 C  CG  . MET B 1 122 ? -14.89000 -21.71700 10.26800 1.000 32.32000 ? 122 MET B CG  1 
ATOM   1386 S  SD  . MET B 1 122 ? -13.41000 -20.85100 9.95700  1.000 31.87000 ? 122 MET B SD  1 
ATOM   1387 C  CE  . MET B 1 122 ? -12.74300 -20.90800 11.59600 1.000 30.37000 ? 122 MET B CE  1 
ATOM   1388 N  N   . ALA B 1 123 ? -16.79000 -24.91400 7.96800  1.000 29.58000 ? 123 ALA B N   1 
ATOM   1389 C  CA  . ALA B 1 123 ? -17.12200 -25.78900 6.82900  1.000 29.17000 ? 123 ALA B CA  1 
ATOM   1390 C  C   . ALA B 1 123 ? -18.56600 -26.25500 6.88000  1.000 27.13000 ? 123 ALA B C   1 
ATOM   1391 O  O   . ALA B 1 123 ? -19.17100 -26.21900 5.89500  1.000 33.74000 ? 123 ALA B O   1 
ATOM   1392 C  CB  . ALA B 1 123 ? -16.17700 -26.93900 6.69200  1.000 38.63000 ? 123 ALA B CB  1 
ATOM   1393 N  N   . GLU B 1 124 ? -19.08100 -26.60400 8.02600  1.000 26.53000 ? 124 GLU B N   1 
ATOM   1394 C  CA  . GLU B 1 124 ? -20.47500 -27.06200 7.93000  1.000 31.58000 ? 124 GLU B CA  1 
ATOM   1395 C  C   . GLU B 1 124 ? -21.37600 -25.86800 7.60700  1.000 33.67000 ? 124 GLU B C   1 
ATOM   1396 O  O   . GLU B 1 124 ? -22.15900 -25.97800 6.71300  1.000 31.04000 ? 124 GLU B O   1 
ATOM   1397 C  CB  . GLU B 1 124 ? -20.95200 -27.47700 9.31600  1.000 33.02000 ? 124 GLU B CB  1 
ATOM   1398 C  CG  . GLU B 1 124 ? -20.70000 -28.90300 9.69300  1.000 45.80000 ? 124 GLU B CG  1 
ATOM   1399 C  CD  . GLU B 1 124 ? -19.46400 -29.23800 10.49500 1.000 55.68000 ? 124 GLU B CD  1 
ATOM   1400 O  OE1 . GLU B 1 124 ? -19.22100 -28.58500 11.51200 1.000 62.87000 ? 124 GLU B OE1 1 
ATOM   1401 O  OE2 . GLU B 1 124 ? -18.77400 -30.18900 10.11700 1.000 61.53000 ? 124 GLU B OE2 1 
ATOM   1402 N  N   . ALA B 1 125 ? -21.11200 -24.66100 8.10300  1.000 30.98000 ? 125 ALA B N   1 
ATOM   1403 C  CA  . ALA B 1 125 ? -21.91400 -23.46700 7.80000  1.000 30.65000 ? 125 ALA B CA  1 
ATOM   1404 C  C   . ALA B 1 125 ? -21.79000 -23.14900 6.31800  1.000 31.32000 ? 125 ALA B C   1 
ATOM   1405 O  O   . ALA B 1 125 ? -22.77200 -22.81100 5.72400  1.000 32.59000 ? 125 ALA B O   1 
ATOM   1406 C  CB  . ALA B 1 125 ? -21.51500 -22.32400 8.69100  1.000 25.32000 ? 125 ALA B CB  1 
ATOM   1407 N  N   . LEU B 1 126 ? -20.59800 -23.29300 5.78000  1.000 29.38000 ? 126 LEU B N   1 
ATOM   1408 C  CA  . LEU B 1 126 ? -20.35800 -22.99900 4.36100  1.000 30.51000 ? 126 LEU B CA  1 
ATOM   1409 C  C   . LEU B 1 126 ? -21.11100 -23.97500 3.44600  1.000 33.74000 ? 126 LEU B C   1 
ATOM   1410 O  O   . LEU B 1 126 ? -21.58200 -23.53900 2.43800  1.000 31.94000 ? 126 LEU B O   1 
ATOM   1411 C  CB  . LEU B 1 126 ? -18.85300 -22.97300 4.12200  1.000 28.69000 ? 126 LEU B CB  1 
ATOM   1412 C  CG  . LEU B 1 126 ? -18.43100 -22.27500 2.84700  1.000 31.65000 ? 126 LEU B CG  1 
ATOM   1413 C  CD1 . LEU B 1 126 ? -18.89800 -20.84100 2.80700  1.000 29.35000 ? 126 LEU B CD1 1 
ATOM   1414 C  CD2 . LEU B 1 126 ? -16.94200 -22.36000 2.62300  1.000 37.29000 ? 126 LEU B CD2 1 
ATOM   1415 N  N   . ALA B 1 127 ? -21.14600 -25.25400 3.78800  1.000 34.13000 ? 127 ALA B N   1 
ATOM   1416 C  CA  . ALA B 1 127 ? -21.85500 -26.29000 3.01000  1.000 37.65000 ? 127 ALA B CA  1 
ATOM   1417 C  C   . ALA B 1 127 ? -23.37600 -26.06700 3.07800  1.000 38.22000 ? 127 ALA B C   1 
ATOM   1418 O  O   . ALA B 1 127 ? -24.01900 -26.17500 2.07200  1.000 36.29000 ? 127 ALA B O   1 
ATOM   1419 C  CB  . ALA B 1 127 ? -21.39400 -27.65300 3.43800  1.000 33.14000 ? 127 ALA B CB  1 
ATOM   1420 N  N   . ALA B 1 128 ? -23.89900 -25.71700 4.24200  1.000 35.59000 ? 128 ALA B N   1 
ATOM   1421 C  CA  . ALA B 1 128 ? -25.31600 -25.34700 4.35000  1.000 34.47000 ? 128 ALA B CA  1 
ATOM   1422 C  C   . ALA B 1 128 ? -25.57000 -24.08200 3.51100  1.000 41.47000 ? 128 ALA B C   1 
ATOM   1423 O  O   . ALA B 1 128 ? -26.58600 -23.99000 2.85800  1.000 40.55000 ? 128 ALA B O   1 
ATOM   1424 C  CB  . ALA B 1 128 ? -25.62000 -25.11000 5.78400  1.000 32.85000 ? 128 ALA B CB  1 
ATOM   1425 N  N   . LEU B 1 129 ? -24.65300 -23.12400 3.52600  1.000 37.29000 ? 129 LEU B N   1 
ATOM   1426 C  CA  . LEU B 1 129 ? -24.80700 -21.89900 2.71400  1.000 36.24000 ? 129 LEU B CA  1 
ATOM   1427 C  C   . LEU B 1 129 ? -24.81200 -22.26800 1.23100  1.000 36.30000 ? 129 LEU B C   1 
ATOM   1428 O  O   . LEU B 1 129 ? -25.49000 -21.63200 0.49200  1.000 41.32000 ? 129 LEU B O   1 
ATOM   1429 C  CB  . LEU B 1 129 ? -23.64800 -20.95200 3.03400  1.000 39.23000 ? 129 LEU B CB  1 
ATOM   1430 C  CG  . LEU B 1 129 ? -23.94000 -19.86500 4.06300  1.000 39.07000 ? 129 LEU B CG  1 
ATOM   1431 C  CD1 . LEU B 1 129 ? -22.71200 -19.05500 4.35100  1.000 35.19000 ? 129 LEU B CD1 1 
ATOM   1432 C  CD2 . LEU B 1 129 ? -25.04900 -18.96500 3.58600  1.000 33.09000 ? 129 LEU B CD2 1 
ATOM   1433 N  N   . GLU B 1 130 ? -23.97000 -23.19400 0.82800  1.000 35.45000 ? 130 GLU B N   1 
ATOM   1434 C  CA  . GLU B 1 130 ? -23.91100 -23.65800 -0.57200 1.000 40.34000 ? 130 GLU B CA  1 
ATOM   1435 C  C   . GLU B 1 130 ? -25.17100 -24.44200 -0.95700 1.000 39.27000 ? 130 GLU B C   1 
ATOM   1436 O  O   . GLU B 1 130 ? -25.53300 -24.35500 -2.08400 1.000 40.01000 ? 130 GLU B O   1 
ATOM   1437 C  CB  . GLU B 1 130 ? -22.58300 -24.33600 -0.89900 1.000 40.29000 ? 130 GLU B CB  1 
ATOM   1438 N  N   . ALA B 1 131 ? -25.72500 -25.23200 -0.05300 1.000 35.35000 ? 131 ALA B N   1 
ATOM   1439 C  CA  . ALA B 1 131 ? -26.95000 -26.02500 -0.28700 1.000 40.38000 ? 131 ALA B CA  1 
ATOM   1440 C  C   . ALA B 1 131 ? -28.19600 -25.15500 -0.49400 1.000 45.70000 ? 131 ALA B C   1 
ATOM   1441 O  O   . ALA B 1 131 ? -29.01000 -25.48400 -1.31300 1.000 44.32000 ? 131 ALA B O   1 
ATOM   1442 C  CB  . ALA B 1 131 ? -27.19100 -26.91800 0.89600  1.000 38.88000 ? 131 ALA B CB  1 
ATOM   1443 N  N   . ASN B 1 132 ? -28.28600 -24.07000 0.25700  1.000 45.50000 ? 132 ASN B N   1 
ATOM   1444 C  CA  . ASN B 1 132 ? -29.48100 -23.21500 0.36100  1.000 42.47000 ? 132 ASN B CA  1 
ATOM   1445 C  C   . ASN B 1 132 ? -29.35800 -21.95500 -0.46900 1.000 43.00000 ? 132 ASN B C   1 
ATOM   1446 O  O   . ASN B 1 132 ? -29.90300 -20.97900 -0.06900 1.000 42.68000 ? 132 ASN B O   1 
ATOM   1447 C  CB  . ASN B 1 132 ? -29.73700 -22.91200 1.82300  1.000 41.56000 ? 132 ASN B CB  1 
ATOM   1448 C  CG  . ASN B 1 132 ? -30.10000 -24.17600 2.55900  1.000 46.12000 ? 132 ASN B CG  1 
ATOM   1449 O  OD1 . ASN B 1 132 ? -29.47800 -24.53900 3.53000  1.000 44.63000 ? 132 ASN B OD1 1 
ATOM   1450 N  ND2 . ASN B 1 132 ? -31.10300 -24.87700 2.07300  1.000 49.79000 ? 132 ASN B ND2 1 
ATOM   1451 N  N   . LEU B 1 133 ? -28.61900 -22.00400 -1.55700 1.000 43.33000 ? 133 LEU B N   1 
ATOM   1452 C  CA  . LEU B 1 133 ? -28.40800 -20.83200 -2.43800 1.000 46.20000 ? 133 LEU B CA  1 
ATOM   1453 C  C   . LEU B 1 133 ? -29.73400 -20.31600 -3.03600 1.000 59.77000 ? 133 LEU B C   1 
ATOM   1454 O  O   . LEU B 1 133 ? -29.82500 -19.09500 -3.26300 1.000 59.20000 ? 133 LEU B O   1 
ATOM   1455 C  CB  . LEU B 1 133 ? -27.38900 -21.21800 -3.51000 1.000 43.92000 ? 133 LEU B CB  1 
ATOM   1456 N  N   . ASP B 1 134 ? -30.68800 -21.21800 -3.32300 1.000 59.43000 ? 134 ASP B N   1 
ATOM   1457 C  CA  . ASP B 1 134 ? -32.02100 -20.96200 -3.91400 1.000 53.42000 ? 134 ASP B CA  1 
ATOM   1458 C  C   . ASP B 1 134 ? -33.08300 -20.74000 -2.83300 1.000 59.01000 ? 134 ASP B C   1 
ATOM   1459 O  O   . ASP B 1 134 ? -34.26100 -20.80500 -3.18200 1.000 66.19000 ? 134 ASP B O   1 
ATOM   1460 C  CB  . ASP B 1 134 ? -32.41200 -22.09800 -4.86100 1.000 53.45000 ? 134 ASP B CB  1 
ATOM   1461 C  CG  . ASP B 1 134 ? -31.35000 -22.34400 -5.91200 1.000 56.58000 ? 134 ASP B CG  1 
ATOM   1462 O  OD1 . ASP B 1 134 ? -31.20800 -21.53700 -6.81100 1.000 55.76000 ? 134 ASP B OD1 1 
ATOM   1463 O  OD2 . ASP B 1 134 ? -30.60700 -23.28700 -5.74800 1.000 59.45000 ? 134 ASP B OD2 1 
ATOM   1464 N  N   . HIS B 1 135 ? -32.72000 -20.63800 -1.55400 1.000 53.91000 ? 135 HIS B N   1 
ATOM   1465 C  CA  . HIS B 1 135 ? -33.69300 -20.34400 -0.46800 1.000 54.34000 ? 135 HIS B CA  1 
ATOM   1466 C  C   . HIS B 1 135 ? -33.12900 -19.25500 0.44200  1.000 54.30000 ? 135 HIS B C   1 
ATOM   1467 O  O   . HIS B 1 135 ? -32.83700 -19.58600 1.57000  1.000 53.33000 ? 135 HIS B O   1 
ATOM   1468 C  CB  . HIS B 1 135 ? -34.06600 -21.59200 0.34400  1.000 50.46000 ? 135 HIS B CB  1 
ATOM   1469 C  CG  . HIS B 1 135 ? -34.24900 -22.82800 -0.46300 1.000 60.00000 ? 135 HIS B CG  1 
ATOM   1470 N  ND1 . HIS B 1 135 ? -35.47100 -23.25200 -0.90500 1.000 60.43000 ? 135 HIS B ND1 1 
ATOM   1471 C  CD2 . HIS B 1 135 ? -33.35800 -23.68500 -0.98300 1.000 57.76000 ? 135 HIS B CD2 1 
ATOM   1472 C  CE1 . HIS B 1 135 ? -35.32300 -24.32400 -1.63300 1.000 58.88000 ? 135 HIS B CE1 1 
ATOM   1473 N  NE2 . HIS B 1 135 ? -34.05300 -24.61000 -1.68100 1.000 62.21000 ? 135 HIS B NE2 1 
ATOM   1474 N  N   . PRO B 1 136 ? -33.13900 -17.95800 0.07200  1.000 59.82000 ? 136 PRO B N   1 
ATOM   1475 C  CA  . PRO B 1 136 ? -32.49700 -16.90700 0.87400  1.000 54.82000 ? 136 PRO B CA  1 
ATOM   1476 C  C   . PRO B 1 136 ? -32.87900 -16.86700 2.36300  1.000 54.49000 ? 136 PRO B C   1 
ATOM   1477 O  O   . PRO B 1 136 ? -32.03900 -16.69400 3.18000  1.000 48.04000 ? 136 PRO B O   1 
ATOM   1478 C  CB  . PRO B 1 136 ? -33.08700 -15.66000 0.21400  1.000 47.35000 ? 136 PRO B CB  1 
ATOM   1479 C  CG  . PRO B 1 136 ? -33.13900 -16.01500 -1.23500 1.000 49.06000 ? 136 PRO B CG  1 
ATOM   1480 C  CD  . PRO B 1 136 ? -33.64300 -17.43900 -1.20800 1.000 58.75000 ? 136 PRO B CD  1 
ATOM   1481 N  N   . GLU B 1 137 ? -34.14000 -17.10200 2.66300  1.000 55.96000 ? 137 GLU B N   1 
ATOM   1482 C  CA  . GLU B 1 137 ? -34.60600 -17.08800 4.06200  1.000 54.27000 ? 137 GLU B CA  1 
ATOM   1483 C  C   . GLU B 1 137 ? -33.92700 -18.18700 4.89700  1.000 51.70000 ? 137 GLU B C   1 
ATOM   1484 O  O   . GLU B 1 137 ? -33.73400 -17.95100 6.05500  1.000 51.86000 ? 137 GLU B O   1 
ATOM   1485 C  CB  . GLU B 1 137 ? -36.13200 -17.06700 4.08300  1.000 53.02000 ? 137 GLU B CB  1 
ATOM   1486 N  N   . GLN B 1 138 ? -33.71600 -19.39100 4.37500  1.000 52.74000 ? 138 GLN B N   1 
ATOM   1487 C  CA  . GLN B 1 138 ? -33.01600 -20.45600 5.16800  1.000 54.04000 ? 138 GLN B CA  1 
ATOM   1488 C  C   . GLN B 1 138 ? -31.52900 -20.14200 5.31000  1.000 49.52000 ? 138 GLN B C   1 
ATOM   1489 O  O   . GLN B 1 138 ? -30.95000 -20.62400 6.23700  1.000 47.72000 ? 138 GLN B O   1 
ATOM   1490 C  CB  . GLN B 1 138 ? -33.13300 -21.88100 4.62300  1.000 49.04000 ? 138 GLN B CB  1 
ATOM   1491 C  CG  . GLN B 1 138 ? -34.22300 -22.72200 5.26400  1.000 54.30000 ? 138 GLN B CG  1 
ATOM   1492 C  CD  . GLN B 1 138 ? -34.24600 -22.75900 6.77600  1.000 59.00000 ? 138 GLN B CD  1 
ATOM   1493 O  OE1 . GLN B 1 138 ? -33.24500 -22.55100 7.44600  1.000 61.77000 ? 138 GLN B OE1 1 
ATOM   1494 N  NE2 . GLN B 1 138 ? -35.41100 -23.03500 7.33700  1.000 57.35000 ? 138 GLN B NE2 1 
ATOM   1495 N  N   . GLY B 1 139 ? -30.94400 -19.48300 4.31800  1.000 43.90000 ? 139 GLY B N   1 
ATOM   1496 C  CA  . GLY B 1 139 ? -29.50900 -19.16600 4.29200  1.000 38.84000 ? 139 GLY B CA  1 
ATOM   1497 C  C   . GLY B 1 139 ? -29.07200 -18.17200 5.34400  1.000 38.63000 ? 139 GLY B C   1 
ATOM   1498 O  O   . GLY B 1 139 ? -27.90900 -18.12800 5.61400  1.000 42.19000 ? 139 GLY B O   1 
ATOM   1499 N  N   . VAL B 1 140 ? -29.97300 -17.35100 5.84800  1.000 35.54000 ? 140 VAL B N   1 
ATOM   1500 C  CA  . VAL B 1 140 ? -29.59900 -16.29800 6.82000  1.000 36.09000 ? 140 VAL B CA  1 
ATOM   1501 C  C   . VAL B 1 140 ? -29.04300 -16.92800 8.08000  1.000 32.18000 ? 140 VAL B C   1 
ATOM   1502 O  O   . VAL B 1 140 ? -28.05600 -16.46700 8.53000  1.000 28.81000 ? 140 VAL B O   1 
ATOM   1503 C  CB  . VAL B 1 140 ? -30.78300 -15.37300 7.12300  1.000 43.30000 ? 140 VAL B CB  1 
ATOM   1504 C  CG1 . VAL B 1 140 ? -30.56100 -14.60300 8.40800  1.000 38.34000 ? 140 VAL B CG1 1 
ATOM   1505 C  CG2 . VAL B 1 140 ? -31.05200 -14.43800 5.96300  1.000 37.05000 ? 140 VAL B CG2 1 
ATOM   1506 N  N   . GLU B 1 141 ? -29.64700 -18.00900 8.53700  1.000 32.26000 ? 141 GLU B N   1 
ATOM   1507 C  CA  . GLU B 1 141 ? -29.17600 -18.70700 9.74900  1.000 32.79000 ? 141 GLU B CA  1 
ATOM   1508 C  C   . GLU B 1 141 ? -27.73100 -19.19700 9.55800  1.000 32.23000 ? 141 GLU B C   1 
ATOM   1509 O  O   . GLU B 1 141 ? -27.00500 -19.16400 10.50500 1.000 31.59000 ? 141 GLU B O   1 
ATOM   1510 C  CB  . GLU B 1 141 ? -30.10300 -19.87400 10.06600 1.000 31.43000 ? 141 GLU B CB  1 
ATOM   1511 N  N   . HIS B 1 142 ? -27.40300 -19.71500 8.39100  1.000 27.05000 ? 142 HIS B N   1 
ATOM   1512 C  CA  . HIS B 1 142 ? -26.05000 -20.19800 8.05000  1.000 29.49000 ? 142 HIS B CA  1 
ATOM   1513 C  C   . HIS B 1 142 ? -25.02500 -19.06600 7.95300  1.000 32.10000 ? 142 HIS B C   1 
ATOM   1514 O  O   . HIS B 1 142 ? -23.96800 -19.27200 8.40100  1.000 33.37000 ? 142 HIS B O   1 
ATOM   1515 C  CB  . HIS B 1 142 ? -26.11500 -21.15700 6.86300  1.000 30.61000 ? 142 HIS B CB  1 
ATOM   1516 C  CG  . HIS B 1 142 ? -27.19300 -22.15500 7.05400  1.000 33.92000 ? 142 HIS B CG  1 
ATOM   1517 N  ND1 . HIS B 1 142 ? -27.89500 -22.68600 6.02100  1.000 38.13000 ? 142 HIS B ND1 1 
ATOM   1518 C  CD2 . HIS B 1 142 ? -27.72600 -22.66700 8.16700  1.000 33.07000 ? 142 HIS B CD2 1 
ATOM   1519 C  CE1 . HIS B 1 142 ? -28.78900 -23.49300 6.48500  1.000 37.48000 ? 142 HIS B CE1 1 
ATOM   1520 N  NE2 . HIS B 1 142 ? -28.71100 -23.49200 7.78100  1.000 39.96000 ? 142 HIS B NE2 1 
ATOM   1521 N  N   . ASP B 1 143 ? -25.36000 -17.91800 7.37900  1.000 31.65000 ? 143 ASP B N   1 
ATOM   1522 C  CA  . ASP B 1 143 ? -24.42000 -16.77500 7.31300  1.000 29.84000 ? 143 ASP B CA  1 
ATOM   1523 C  C   . ASP B 1 143 ? -24.08400 -16.33100 8.73600  1.000 29.92000 ? 143 ASP B C   1 
ATOM   1524 O  O   . ASP B 1 143 ? -22.95400 -16.16100 9.02900  1.000 26.51000 ? 143 ASP B O   1 
ATOM   1525 C  CB  . ASP B 1 143 ? -24.96500 -15.59900 6.51100  1.000 29.11000 ? 143 ASP B CB  1 
ATOM   1526 C  CG  . ASP B 1 143 ? -24.11100 -14.35200 6.66400  1.000 35.57000 ? 143 ASP B CG  1 
ATOM   1527 O  OD1 . ASP B 1 143 ? -23.08600 -14.23600 5.99300  1.000 33.40000 ? 143 ASP B OD1 1 
ATOM   1528 O  OD2 . ASP B 1 143 ? -24.46200 -13.52700 7.47300  1.000 41.02000 ? 143 ASP B OD2 1 
ATOM   1529 N  N   . ILE B 1 144 ? -25.07800 -16.28900 9.59900  1.000 28.03000 ? 144 ILE B N   1 
ATOM   1530 C  CA  . ILE B 1 144 ? -24.85500 -15.96600 11.01600 1.000 27.10000 ? 144 ILE B CA  1 
ATOM   1531 C  C   . ILE B 1 144 ? -23.91700 -17.02000 11.57600 1.000 27.76000 ? 144 ILE B C   1 
ATOM   1532 O  O   . ILE B 1 144 ? -22.91400 -16.63200 12.07500 1.000 25.49000 ? 144 ILE B O   1 
ATOM   1533 C  CB  . ILE B 1 144 ? -26.18800 -16.00200 11.76100 1.000 26.14000 ? 144 ILE B CB  1 
ATOM   1534 C  CG1 . ILE B 1 144 ? -27.07500 -14.82100 11.39300 1.000 24.69000 ? 144 ILE B CG1 1 
ATOM   1535 C  CG2 . ILE B 1 144 ? -25.98700 -16.13500 13.24500 1.000 23.50000 ? 144 ILE B CG2 1 
ATOM   1536 C  CD1 . ILE B 1 144 ? -28.28600 -14.73000 12.22800 1.000 26.51000 ? 144 ILE B CD1 1 
ATOM   1537 N  N   . ALA B 1 145 ? -24.18800 -18.29300 11.31500 1.000 26.31000 ? 145 ALA B N   1 
ATOM   1538 C  CA  . ALA B 1 145 ? -23.39100 -19.40400 11.85700 1.000 20.78000 ? 145 ALA B CA  1 
ATOM   1539 C  C   . ALA B 1 145 ? -21.95900 -19.33000 11.34700 1.000 20.84000 ? 145 ALA B C   1 
ATOM   1540 O  O   . ALA B 1 145 ? -21.11800 -19.59500 12.09800 1.000 23.99000 ? 145 ALA B O   1 
ATOM   1541 C  CB  . ALA B 1 145 ? -24.04200 -20.72800 11.55400 1.000 26.31000 ? 145 ALA B CB  1 
ATOM   1542 N  N   . PHE B 1 146 ? -21.74700 -18.98700 10.10000 1.000 21.85000 ? 146 PHE B N   1 
ATOM   1543 C  CA  . PHE B 1 146 ? -20.38800 -18.86100 9.52500  1.000 21.69000 ? 146 PHE B CA  1 
ATOM   1544 C  C   . PHE B 1 146 ? -19.54200 -17.76600 10.19800 1.000 24.55000 ? 146 PHE B C   1 
ATOM   1545 O  O   . PHE B 1 146 ? -18.44600 -18.07400 10.56300 1.000 19.81000 ? 146 PHE B O   1 
ATOM   1546 C  CB  . PHE B 1 146 ? -20.55000 -18.56500 8.03900  1.000 23.26000 ? 146 PHE B CB  1 
ATOM   1547 C  CG  . PHE B 1 146 ? -19.29900 -18.38400 7.23800  1.000 25.28000 ? 146 PHE B CG  1 
ATOM   1548 C  CD1 . PHE B 1 146 ? -18.38700 -19.39900 7.10300  1.000 23.32000 ? 146 PHE B CD1 1 
ATOM   1549 C  CD2 . PHE B 1 146 ? -19.03900 -17.18800 6.60800  1.000 25.88000 ? 146 PHE B CD2 1 
ATOM   1550 C  CE1 . PHE B 1 146 ? -17.24500 -19.21200 6.35100  1.000 27.38000 ? 146 PHE B CE1 1 
ATOM   1551 C  CE2 . PHE B 1 146 ? -17.89600 -17.00700 5.86100  1.000 27.69000 ? 146 PHE B CE2 1 
ATOM   1552 C  CZ  . PHE B 1 146 ? -16.98700 -18.01400 5.75200  1.000 28.77000 ? 146 PHE B CZ  1 
ATOM   1553 N  N   . HIS B 1 147 ? -20.09100 -16.56000 10.36500 1.000 19.68000 ? 147 HIS B N   1 
ATOM   1554 C  CA  . HIS B 1 147 ? -19.41800 -15.40400 11.01300 1.000 24.37000 ? 147 HIS B CA  1 
ATOM   1555 C  C   . HIS B 1 147 ? -19.21100 -15.72300 12.49200 1.000 23.34000 ? 147 HIS B C   1 
ATOM   1556 O  O   . HIS B 1 147 ? -18.20500 -15.42700 13.00800 1.000 22.90000 ? 147 HIS B O   1 
ATOM   1557 C  CB  . HIS B 1 147 ? -20.07000 -14.07000 10.66100 1.000 21.96000 ? 147 HIS B CB  1 
ATOM   1558 C  CG  . HIS B 1 147 ? -20.03200 -13.70100 9.21600  1.000 26.31000 ? 147 HIS B CG  1 
ATOM   1559 N  ND1 . HIS B 1 147 ? -18.89400 -13.47200 8.54200  1.000 22.58000 ? 147 HIS B ND1 1 
ATOM   1560 C  CD2 . HIS B 1 147 ? -21.01200 -13.49200 8.33200  1.000 26.02000 ? 147 HIS B CD2 1 
ATOM   1561 C  CE1 . HIS B 1 147 ? -19.16500 -13.15700 7.31500  1.000 28.63000 ? 147 HIS B CE1 1 
ATOM   1562 N  NE2 . HIS B 1 147 ? -20.46500 -13.15600 7.14100  1.000 28.50000 ? 147 HIS B NE2 1 
ATOM   1563 N  N   . VAL B 1 148 ? -20.17100 -16.39200 13.09700 1.000 22.13000 ? 148 VAL B N   1 
ATOM   1564 C  CA  . VAL B 1 148 ? -20.05500 -16.83800 14.50100 1.000 22.81000 ? 148 VAL B CA  1 
ATOM   1565 C  C   . VAL B 1 148 ? -18.90500 -17.85000 14.63200 1.000 24.19000 ? 148 VAL B C   1 
ATOM   1566 O  O   . VAL B 1 148 ? -18.23700 -17.84500 15.59300 1.000 26.10000 ? 148 VAL B O   1 
ATOM   1567 C  CB  . VAL B 1 148 ? -21.40000 -17.39100 14.96400 1.000 22.74000 ? 148 VAL B CB  1 
ATOM   1568 C  CG1 . VAL B 1 148 ? -21.25000 -18.31100 16.14100 1.000 18.35000 ? 148 VAL B CG1 1 
ATOM   1569 C  CG2 . VAL B 1 148 ? -22.38700 -16.28100 15.24600 1.000 21.78000 ? 148 VAL B CG2 1 
ATOM   1570 N  N   . ALA B 1 149 ? -18.73000 -18.72100 13.66600 1.000 21.86000 ? 149 ALA B N   1 
ATOM   1571 C  CA  . ALA B 1 149 ? -17.60800 -19.66900 13.70500 1.000 25.78000 ? 149 ALA B CA  1 
ATOM   1572 C  C   . ALA B 1 149 ? -16.28700 -18.89800 13.57900 1.000 23.40000 ? 149 ALA B C   1 
ATOM   1573 O  O   . ALA B 1 149 ? -15.37100 -19.32900 14.15200 1.000 25.86000 ? 149 ALA B O   1 
ATOM   1574 C  CB  . ALA B 1 149 ? -17.77100 -20.77900 12.70100 1.000 21.24000 ? 149 ALA B CB  1 
ATOM   1575 N  N   . ILE B 1 150 ? -16.20300 -17.86100 12.75600 1.000 21.88000 ? 150 ILE B N   1 
ATOM   1576 C  CA  . ILE B 1 150 ? -14.94300 -17.07800 12.68800 1.000 24.40000 ? 150 ILE B CA  1 
ATOM   1577 C  C   . ILE B 1 150 ? -14.66900 -16.39700 14.04300 1.000 24.84000 ? 150 ILE B C   1 
ATOM   1578 O  O   . ILE B 1 150 ? -13.56200 -16.52200 14.54200 1.000 21.14000 ? 150 ILE B O   1 
ATOM   1579 C  CB  . ILE B 1 150 ? -14.93300 -16.12100 11.49600 1.000 21.35000 ? 150 ILE B CB  1 
ATOM   1580 C  CG1 . ILE B 1 150 ? -14.98800 -16.87600 10.17600 1.000 23.90000 ? 150 ILE B CG1 1 
ATOM   1581 C  CG2 . ILE B 1 150 ? -13.73100 -15.21700 11.56200 1.000 23.73000 ? 150 ILE B CG2 1 
ATOM   1582 C  CD1 . ILE B 1 150 ? -15.44100 -16.06400 9.02000  1.000 21.71000 ? 150 ILE B CD1 1 
ATOM   1583 N  N   . ALA B 1 151 ? -15.70800 -15.83000 14.65000 1.000 24.52000 ? 151 ALA B N   1 
ATOM   1584 C  CA  . ALA B 1 151 ? -15.61500 -15.17300 15.96200 1.000 21.22000 ? 151 ALA B CA  1 
ATOM   1585 C  C   . ALA B 1 151 ? -15.15500 -16.16700 17.01400 1.000 25.52000 ? 151 ALA B C   1 
ATOM   1586 O  O   . ALA B 1 151 ? -14.27800 -15.82000 17.70800 1.000 29.01000 ? 151 ALA B O   1 
ATOM   1587 C  CB  . ALA B 1 151 ? -16.94600 -14.63700 16.34200 1.000 22.34000 ? 151 ALA B CB  1 
ATOM   1588 N  N   . ALA B 1 152 ? -15.70900 -17.37600 17.04600 1.000 28.74000 ? 152 ALA B N   1 
ATOM   1589 C  CA  . ALA B 1 152 ? -15.32000 -18.44900 17.99100 1.000 22.45000 ? 152 ALA B CA  1 
ATOM   1590 C  C   . ALA B 1 152 ? -13.88800 -18.89300 17.74200 1.000 24.13000 ? 152 ALA B C   1 
ATOM   1591 O  O   . ALA B 1 152 ? -13.29200 -19.24700 18.66500 1.000 30.71000 ? 152 ALA B O   1 
ATOM   1592 C  CB  . ALA B 1 152 ? -16.27900 -19.59600 18.00500 1.000 20.84000 ? 152 ALA B CB  1 
ATOM   1593 N  N   . ALA B 1 153 ? -13.39300 -18.83700 16.51400 1.000 23.92000 ? 153 ALA B N   1 
ATOM   1594 C  CA  . ALA B 1 153 ? -12.00100 -19.19700 16.16900 1.000 26.60000 ? 153 ALA B CA  1 
ATOM   1595 C  C   . ALA B 1 153 ? -10.94500 -18.21500 16.71400 1.000 29.09000 ? 153 ALA B C   1 
ATOM   1596 O  O   . ALA B 1 153 ? -9.79800  -18.52500 16.60500 1.000 25.78000 ? 153 ALA B O   1 
ATOM   1597 C  CB  . ALA B 1 153 ? -11.84500 -19.44000 14.72000 1.000 22.46000 ? 153 ALA B CB  1 
ATOM   1598 N  N   . THR B 1 154 ? -11.33200 -17.02400 17.14000 1.000 27.86000 ? 154 THR B N   1 
ATOM   1599 C  CA  . THR B 1 154 ? -10.40600 -16.05400 17.77000 1.000 26.28000 ? 154 THR B CA  1 
ATOM   1600 C  C   . THR B 1 154 ? -9.87800  -16.60300 19.09800 1.000 26.33000 ? 154 THR B C   1 
ATOM   1601 O  O   . THR B 1 154 ? -8.82800  -16.22800 19.46400 1.000 25.29000 ? 154 THR B O   1 
ATOM   1602 C  CB  . THR B 1 154 ? -11.04400 -14.67500 17.98500 1.000 24.54000 ? 154 THR B CB  1 
ATOM   1603 O  OG1 . THR B 1 154 ? -11.93200 -14.69900 19.08600 1.000 21.35000 ? 154 THR B OG1 1 
ATOM   1604 C  CG2 . THR B 1 154 ? -11.67500 -14.07700 16.74800 1.000 19.12000 ? 154 THR B CG2 1 
ATOM   1605 N  N   . HIS B 1 155 ? -10.69800 -17.34000 19.84100 1.000 28.72000 ? 155 HIS B N   1 
ATOM   1606 C  CA  . HIS B 1 155 ? -10.37900 -17.85400 21.19600 1.000 31.53000 ? 155 HIS B CA  1 
ATOM   1607 C  C   . HIS B 1 155 ? -10.18700 -16.68600 22.16400 1.000 30.99000 ? 155 HIS B C   1 
ATOM   1608 O  O   . HIS B 1 155 ? -9.39300  -16.80300 23.06700 1.000 34.25000 ? 155 HIS B O   1 
ATOM   1609 C  CB  . HIS B 1 155 ? -9.22000  -18.86400 21.23300 1.000 30.07000 ? 155 HIS B CB  1 
ATOM   1610 C  CG  . HIS B 1 155 ? -9.52800  -20.11500 20.50000 1.000 37.60000 ? 155 HIS B CG  1 
ATOM   1611 N  ND1 . HIS B 1 155 ? -10.42800 -21.01200 20.94400 1.000 36.42000 ? 155 HIS B ND1 1 
ATOM   1612 C  CD2 . HIS B 1 155 ? -9.05700  -20.61300 19.35800 1.000 34.60000 ? 155 HIS B CD2 1 
ATOM   1613 C  CE1 . HIS B 1 155 ? -10.52700 -21.97200 20.09000 1.000 34.86000 ? 155 HIS B CE1 1 
ATOM   1614 N  NE2 . HIS B 1 155 ? -9.70700  -21.75000 19.13400 1.000 32.65000 ? 155 HIS B NE2 1 
ATOM   1615 N  N   . ASN B 1 156 ? -10.92700 -15.60500 21.96000 1.000 30.42000 ? 156 ASN B N   1 
ATOM   1616 C  CA  . ASN B 1 156 ? -10.87500 -14.40400 22.79900 1.000 23.01000 ? 156 ASN B CA  1 
ATOM   1617 C  C   . ASN B 1 156 ? -12.29900 -14.14500 23.23300 1.000 22.63000 ? 156 ASN B C   1 
ATOM   1618 O  O   . ASN B 1 156 ? -13.03900 -13.62700 22.48700 1.000 21.87000 ? 156 ASN B O   1 
ATOM   1619 C  CB  . ASN B 1 156 ? -10.25400 -13.23600 22.04200 1.000 23.07000 ? 156 ASN B CB  1 
ATOM   1620 C  CG  . ASN B 1 156 ? -10.03900 -12.00200 22.88300 1.000 22.83000 ? 156 ASN B CG  1 
ATOM   1621 O  OD1 . ASN B 1 156 ? -10.71800 -11.76600 23.86000 1.000 22.04000 ? 156 ASN B OD1 1 
ATOM   1622 N  ND2 . ASN B 1 156 ? -9.07300  -11.21100 22.50500 1.000 24.18000 ? 156 ASN B ND2 1 
ATOM   1623 N  N   . ARG B 1 157 ? -12.60600 -14.42400 24.46700 1.000 21.45000 ? 157 ARG B N   1 
ATOM   1624 C  CA  . ARG B 1 157 ? -13.98300 -14.22100 24.93400 1.000 26.81000 ? 157 ARG B CA  1 
ATOM   1625 C  C   . ARG B 1 157 ? -14.44000 -12.74100 24.83100 1.000 27.13000 ? 157 ARG B C   1 
ATOM   1626 O  O   . ARG B 1 157 ? -15.52400 -12.53700 24.34000 1.000 25.25000 ? 157 ARG B O   1 
ATOM   1627 C  CB  . ARG B 1 157 ? -14.08000 -14.82800 26.33000 1.000 25.52000 ? 157 ARG B CB  1 
ATOM   1628 C  CG  . ARG B 1 157 ? -15.47200 -15.30200 26.68000 1.000 39.35000 ? 157 ARG B CG  1 
ATOM   1629 C  CD  . ARG B 1 157 ? -15.72300 -15.18800 28.16500 1.000 44.00000 ? 157 ARG B CD  1 
ATOM   1630 N  NE  . ARG B 1 157 ? -16.59300 -16.19700 28.75200 1.000 44.74000 ? 157 ARG B NE  1 
ATOM   1631 C  CZ  . ARG B 1 157 ? -17.87400 -16.06500 29.00600 1.000 42.17000 ? 157 ARG B CZ  1 
ATOM   1632 N  NH1 . ARG B 1 157 ? -18.49400 -17.05900 29.58000 1.000 46.21000 ? 157 ARG B NH1 1 
ATOM   1633 N  NH2 . ARG B 1 157 ? -18.53700 -14.96100 28.71500 1.000 41.02000 ? 157 ARG B NH2 1 
ATOM   1634 N  N   . TYR B 1 158 ? -13.61100 -11.77700 25.22400 1.000 24.44000 ? 158 TYR B N   1 
ATOM   1635 C  CA  . TYR B 1 158 ? -13.95200 -10.33200 25.18700 1.000 23.25000 ? 158 TYR B CA  1 
ATOM   1636 C  C   . TYR B 1 158 ? -14.22700 -9.88100  23.75300 1.000 22.43000 ? 158 TYR B C   1 
ATOM   1637 O  O   . TYR B 1 158 ? -15.17300 -9.21500  23.54500 1.000 23.90000 ? 158 TYR B O   1 
ATOM   1638 C  CB  . TYR B 1 158 ? -12.90000 -9.50300  25.92800 1.000 24.22000 ? 158 TYR B CB  1 
ATOM   1639 C  CG  . TYR B 1 158 ? -12.68600 -9.91000  27.35500 1.000 25.82000 ? 158 TYR B CG  1 
ATOM   1640 C  CD1 . TYR B 1 158 ? -13.55700 -9.52500  28.34000 1.000 30.01000 ? 158 TYR B CD1 1 
ATOM   1641 C  CD2 . TYR B 1 158 ? -11.64200 -10.72400 27.72300 1.000 28.21000 ? 158 TYR B CD2 1 
ATOM   1642 C  CE1 . TYR B 1 158 ? -13.39700 -9.92600  29.65400 1.000 32.17000 ? 158 TYR B CE1 1 
ATOM   1643 C  CE2 . TYR B 1 158 ? -11.46200 -11.14300 29.02400 1.000 26.85000 ? 158 TYR B CE2 1 
ATOM   1644 C  CZ  . TYR B 1 158 ? -12.33800 -10.73700 29.99500 1.000 31.45000 ? 158 TYR B CZ  1 
ATOM   1645 O  OH  . TYR B 1 158 ? -12.19000 -11.14600 31.27200 1.000 35.65000 ? 158 TYR B OH  1 
ATOM   1646 N  N   . TYR B 1 159 ? -13.42100 -10.31400 22.81000 1.000 21.92000 ? 159 TYR B N   1 
ATOM   1647 C  CA  . TYR B 1 159 ? -13.57300 -9.99800  21.37700 1.000 19.95000 ? 159 TYR B CA  1 
ATOM   1648 C  C   . TYR B 1 159 ? -14.87900 -10.57600 20.82900 1.000 21.43000 ? 159 TYR B C   1 
ATOM   1649 O  O   . TYR B 1 159 ? -15.51000 -9.91400  20.09700 1.000 24.40000 ? 159 TYR B O   1 
ATOM   1650 C  CB  . TYR B 1 159 ? -12.39600 -10.60000 20.60900 1.000 23.74000 ? 159 TYR B CB  1 
ATOM   1651 C  CG  . TYR B 1 159 ? -11.95900 -9.89000  19.35500 1.000 22.85000 ? 159 TYR B CG  1 
ATOM   1652 C  CD1 . TYR B 1 159 ? -12.80100 -9.72100  18.28000 1.000 19.41000 ? 159 TYR B CD1 1 
ATOM   1653 C  CD2 . TYR B 1 159 ? -10.67800 -9.40100  19.25000 1.000 22.74000 ? 159 TYR B CD2 1 
ATOM   1654 C  CE1 . TYR B 1 159 ? -12.39400 -9.04400  17.15600 1.000 22.95000 ? 159 TYR B CE1 1 
ATOM   1655 C  CE2 . TYR B 1 159 ? -10.24000 -8.75500  18.12000 1.000 21.59000 ? 159 TYR B CE2 1 
ATOM   1656 C  CZ  . TYR B 1 159 ? -11.10400 -8.57100  17.07100 1.000 24.49000 ? 159 TYR B CZ  1 
ATOM   1657 O  OH  . TYR B 1 159 ? -10.69400 -7.90600  15.99100 1.000 26.15000 ? 159 TYR B OH  1 
ATOM   1658 N  N   . GLN B 1 160 ? -15.20400 -11.81900 21.14900 1.000 25.08000 ? 160 GLN B N   1 
ATOM   1659 C  CA  . GLN B 1 160 ? -16.43400 -12.51900 20.70800 1.000 23.23000 ? 160 GLN B CA  1 
ATOM   1660 C  C   . GLN B 1 160 ? -17.67000 -11.85300 21.29800 1.000 24.01000 ? 160 GLN B C   1 
ATOM   1661 O  O   . GLN B 1 160 ? -18.57900 -11.63700 20.59200 1.000 28.00000 ? 160 GLN B O   1 
ATOM   1662 C  CB  . GLN B 1 160 ? -16.46400 -13.95400 21.20200 1.000 22.94000 ? 160 GLN B CB  1 
ATOM   1663 C  CG  . GLN B 1 160 ? -15.52100 -14.89900 20.51800 1.000 25.94000 ? 160 GLN B CG  1 
ATOM   1664 C  CD  . GLN B 1 160 ? -15.41500 -16.21100 21.25900 1.000 35.12000 ? 160 GLN B CD  1 
ATOM   1665 O  OE1 . GLN B 1 160 ? -16.42400 -16.85500 21.55500 1.000 35.18000 ? 160 GLN B OE1 1 
ATOM   1666 N  NE2 . GLN B 1 160 ? -14.19100 -16.65100 21.51200 1.000 28.65000 ? 160 GLN B NE2 1 
ATOM   1667 N  N   . ASP B 1 161 ? -17.64700 -11.50800 22.55900 1.000 25.13000 ? 161 ASP B N   1 
ATOM   1668 C  CA  . ASP B 1 161 ? -18.83100 -10.86400 23.13700 1.000 26.28000 ? 161 ASP B CA  1 
ATOM   1669 C  C   . ASP B 1 161 ? -19.09800 -9.53100  22.44800 1.000 26.64000 ? 161 ASP B C   1 
ATOM   1670 O  O   . ASP B 1 161 ? -20.21800 -9.31400  22.13600 1.000 25.12000 ? 161 ASP B O   1 
ATOM   1671 C  CB  . ASP B 1 161 ? -18.70900 -10.71600 24.64300 1.000 35.11000 ? 161 ASP B CB  1 
ATOM   1672 C  CG  . ASP B 1 161 ? -19.00600 -11.95900 25.45600 1.000 40.16000 ? 161 ASP B CG  1 
ATOM   1673 O  OD1 . ASP B 1 161 ? -18.95800 -13.05600 24.93100 1.000 35.79000 ? 161 ASP B OD1 1 
ATOM   1674 O  OD2 . ASP B 1 161 ? -19.23900 -11.78700 26.63200 1.000 47.29000 ? 161 ASP B OD2 1 
ATOM   1675 N  N   . LEU B 1 162 ? -18.07700 -8.70800  22.20100 1.000 22.27000 ? 162 LEU B N   1 
ATOM   1676 C  CA  . LEU B 1 162 ? -18.31200 -7.42200  21.51700 1.000 22.97000 ? 162 LEU B CA  1 
ATOM   1677 C  C   . LEU B 1 162 ? -18.82500 -7.59800  20.08500 1.000 24.18000 ? 162 LEU B C   1 
ATOM   1678 O  O   . LEU B 1 162 ? -19.73200 -6.91100  19.71000 1.000 23.53000 ? 162 LEU B O   1 
ATOM   1679 C  CB  . LEU B 1 162 ? -17.08100 -6.54000  21.54100 1.000 21.82000 ? 162 LEU B CB  1 
ATOM   1680 C  CG  . LEU B 1 162 ? -17.37000 -5.15800  20.99500 1.000 15.00000 ? 162 LEU B CG  1 
ATOM   1681 C  CD1 . LEU B 1 162 ? -18.51500 -4.54300  21.75400 1.000 18.81000 ? 162 LEU B CD1 1 
ATOM   1682 C  CD2 . LEU B 1 162 ? -16.15000 -4.29200  21.07900 1.000 22.07000 ? 162 LEU B CD2 1 
ATOM   1683 N  N   . LEU B 1 163 ? -18.25300 -8.52700  19.34200 1.000 24.00000 ? 163 LEU B N   1 
ATOM   1684 C  CA  . LEU B 1 163 ? -18.70100 -8.79900  17.97100 1.000 20.84000 ? 163 LEU B CA  1 
ATOM   1685 C  C   . LEU B 1 163 ? -20.13600 -9.30900  18.00800 1.000 26.56000 ? 163 LEU B C   1 
ATOM   1686 O  O   . LEU B 1 163 ? -20.88100 -8.92600  17.15800 1.000 28.29000 ? 163 LEU B O   1 
ATOM   1687 C  CB  . LEU B 1 163 ? -17.75100 -9.78500  17.31100 1.000 19.66000 ? 163 LEU B CB  1 
ATOM   1688 C  CG  . LEU B 1 163 ? -16.83900 -9.21100  16.24300 1.000 26.09000 ? 163 LEU B CG  1 
ATOM   1689 C  CD1 . LEU B 1 163 ? -15.97800 -10.25700 15.59100 1.000 23.94000 ? 163 LEU B CD1 1 
ATOM   1690 C  CD2 . LEU B 1 163 ? -17.61900 -8.44700  15.19600 1.000 28.47000 ? 163 LEU B CD2 1 
ATOM   1691 N  N   . GLN B 1 164 ? -20.46700 -10.16400 18.95400 1.000 22.30000 ? 164 GLN B N   1 
ATOM   1692 C  CA  . GLN B 1 164 ? -21.84300 -10.67800 19.00700 1.000 26.90000 ? 164 GLN B CA  1 
ATOM   1693 C  C   . GLN B 1 164 ? -22.84600 -9.55900  19.31400 1.000 27.10000 ? 164 GLN B C   1 
ATOM   1694 O  O   . GLN B 1 164 ? -23.80600 -9.47100  18.65500 1.000 25.73000 ? 164 GLN B O   1 
ATOM   1695 C  CB  . GLN B 1 164 ? -21.91500 -11.86600 19.94500 1.000 29.50000 ? 164 GLN B CB  1 
ATOM   1696 C  CG  . GLN B 1 164 ? -23.32600 -12.27300 20.26000 1.000 38.26000 ? 164 GLN B CG  1 
ATOM   1697 C  CD  . GLN B 1 164 ? -24.08400 -12.77200 19.06000 1.000 45.89000 ? 164 GLN B CD  1 
ATOM   1698 O  OE1 . GLN B 1 164 ? -24.64800 -12.00100 18.28400 1.000 41.34000 ? 164 GLN B OE1 1 
ATOM   1699 N  NE2 . GLN B 1 164 ? -24.11700 -14.08400 18.92200 1.000 39.18000 ? 164 GLN B NE2 1 
ATOM   1700 N  N   . TYR B 1 165 ? -22.52200 -8.69000  20.23900 1.000 27.25000 ? 165 TYR B N   1 
ATOM   1701 C  CA  . TYR B 1 165 ? -23.38800 -7.55200  20.60500 1.000 24.30000 ? 165 TYR B CA  1 
ATOM   1702 C  C   . TYR B 1 165 ? -23.57400 -6.59900  19.42300 1.000 27.37000 ? 165 TYR B C   1 
ATOM   1703 O  O   . TYR B 1 165 ? -24.70600 -6.24700  19.20300 1.000 26.22000 ? 165 TYR B O   1 
ATOM   1704 C  CB  . TYR B 1 165 ? -22.81700 -6.91300  21.86300 1.000 21.28000 ? 165 TYR B CB  1 
ATOM   1705 C  CG  . TYR B 1 165 ? -23.40200 -5.61700  22.33800 1.000 29.33000 ? 165 TYR B CG  1 
ATOM   1706 C  CD1 . TYR B 1 165 ? -24.64700 -5.57400  22.91100 1.000 25.29000 ? 165 TYR B CD1 1 
ATOM   1707 C  CD2 . TYR B 1 165 ? -22.66500 -4.44800  22.33200 1.000 29.58000 ? 165 TYR B CD2 1 
ATOM   1708 C  CE1 . TYR B 1 165 ? -25.16400 -4.41600  23.44100 1.000 27.61000 ? 165 TYR B CE1 1 
ATOM   1709 C  CE2 . TYR B 1 165 ? -23.16100 -3.27200  22.86700 1.000 28.74000 ? 165 TYR B CE2 1 
ATOM   1710 C  CZ  . TYR B 1 165 ? -24.42600 -3.25100  23.40800 1.000 34.83000 ? 165 TYR B CZ  1 
ATOM   1711 O  OH  . TYR B 1 165 ? -24.98900 -2.11600  23.87200 1.000 30.91000 ? 165 TYR B OH  1 
ATOM   1712 N  N   . LEU B 1 166 ? -22.51100 -6.25300  18.69200 1.000 25.90000 ? 166 LEU B N   1 
ATOM   1713 C  CA  . LEU B 1 166 ? -22.62400 -5.36700  17.51200 1.000 26.62000 ? 166 LEU B CA  1 
ATOM   1714 C  C   . LEU B 1 166 ? -23.47200 -6.04700  16.42300 1.000 25.39000 ? 166 LEU B C   1 
ATOM   1715 O  O   . LEU B 1 166 ? -24.25900 -5.39800  15.83300 1.000 21.45000 ? 166 LEU B O   1 
ATOM   1716 C  CB  . LEU B 1 166 ? -21.25400 -4.96200  16.97600 1.000 19.82000 ? 166 LEU B CB  1 
ATOM   1717 C  CG  . LEU B 1 166 ? -20.32000 -4.21200  17.91000 1.000 25.43000 ? 166 LEU B CG  1 
ATOM   1718 C  CD1 . LEU B 1 166 ? -19.00300 -3.96800  17.23800 1.000 19.89000 ? 166 LEU B CD1 1 
ATOM   1719 C  CD2 . LEU B 1 166 ? -20.90400 -2.89400  18.35300 1.000 29.75000 ? 166 LEU B CD2 1 
ATOM   1720 N  N   . ASN B 1 167 ? -23.27600 -7.33400  16.20600 1.000 23.77000 ? 167 ASN B N   1 
ATOM   1721 C  CA  . ASN B 1 167 ? -23.99700 -8.13100  15.19000 1.000 26.07000 ? 167 ASN B CA  1 
ATOM   1722 C  C   . ASN B 1 167 ? -25.48800 -8.20800  15.53900 1.000 25.35000 ? 167 ASN B C   1 
ATOM   1723 O  O   . ASN B 1 167 ? -26.28000 -7.97500  14.69600 1.000 25.48000 ? 167 ASN B O   1 
ATOM   1724 C  CB  . ASN B 1 167 ? -23.30900 -9.47000  14.99700 1.000 26.29000 ? 167 ASN B CB  1 
ATOM   1725 C  CG  . ASN B 1 167 ? -22.04000 -9.38300  14.18800 1.000 29.93000 ? 167 ASN B CG  1 
ATOM   1726 O  OD1 . ASN B 1 167 ? -21.93000 -8.62000  13.26500 1.000 29.37000 ? 167 ASN B OD1 1 
ATOM   1727 N  ND2 . ASN B 1 167 ? -21.07800 -10.18600 14.53700 1.000 25.87000 ? 167 ASN B ND2 1 
ATOM   1728 N  N   . LEU B 1 168 ? -25.78500 -8.42000  16.80400 1.000 24.07000 ? 168 LEU B N   1 
ATOM   1729 C  CA  . LEU B 1 168 ? -27.15800 -8.46000  17.33000 1.000 26.85000 ? 168 LEU B CA  1 
ATOM   1730 C  C   . LEU B 1 168 ? -27.80800 -7.08600  17.09800 1.000 26.40000 ? 168 LEU B C   1 
ATOM   1731 O  O   . LEU B 1 168 ? -28.90400 -7.06500  16.61400 1.000 25.82000 ? 168 LEU B O   1 
ATOM   1732 C  CB  . LEU B 1 168 ? -27.08300 -8.87100  18.80500 1.000 25.32000 ? 168 LEU B CB  1 
ATOM   1733 C  CG  . LEU B 1 168 ? -28.37500 -9.27000  19.49100 1.000 29.23000 ? 168 LEU B CG  1 
ATOM   1734 C  CD1 . LEU B 1 168 ? -28.88300 -10.57100 18.93800 1.000 30.87000 ? 168 LEU B CD1 1 
ATOM   1735 C  CD2 . LEU B 1 168 ? -28.21300 -9.38200  20.98100 1.000 25.09000 ? 168 LEU B CD2 1 
ATOM   1736 N  N   . GLN B 1 169 ? -27.08800 -6.00100  17.34400 1.000 22.17000 ? 169 GLN B N   1 
ATOM   1737 C  CA  . GLN B 1 169 ? -27.61800 -4.64000  17.14800 1.000 22.95000 ? 169 GLN B CA  1 
ATOM   1738 C  C   . GLN B 1 169 ? -27.94700 -4.38800  15.69100 1.000 21.56000 ? 169 GLN B C   1 
ATOM   1739 O  O   . GLN B 1 169 ? -28.92000 -3.79300  15.47200 1.000 21.99000 ? 169 GLN B O   1 
ATOM   1740 C  CB  . GLN B 1 169 ? -26.60000 -3.58000  17.52900 1.000 25.34000 ? 169 GLN B CB  1 
ATOM   1741 C  CG  . GLN B 1 169 ? -26.66700 -3.11700  18.96200 1.000 27.82000 ? 169 GLN B CG  1 
ATOM   1742 C  CD  . GLN B 1 169 ? -25.55500 -2.15900  19.29600 1.000 31.10000 ? 169 GLN B CD  1 
ATOM   1743 O  OE1 . GLN B 1 169 ? -25.56300 -1.02100  18.88300 1.000 30.94000 ? 169 GLN B OE1 1 
ATOM   1744 N  NE2 . GLN B 1 169 ? -24.57400 -2.62300  20.02400 1.000 26.19000 ? 169 GLN B NE2 1 
ATOM   1745 N  N   . LEU B 1 170 ? -27.09300 -4.82200  14.77700 1.000 23.67000 ? 170 LEU B N   1 
ATOM   1746 C  CA  . LEU B 1 170 ? -27.29200 -4.61800  13.32900 1.000 26.22000 ? 170 LEU B CA  1 
ATOM   1747 C  C   . LEU B 1 170 ? -28.50600 -5.38300  12.80100 1.000 28.91000 ? 170 LEU B C   1 
ATOM   1748 O  O   . LEU B 1 170 ? -29.16600 -4.82300  11.99300 1.000 27.31000 ? 170 LEU B O   1 
ATOM   1749 C  CB  . LEU B 1 170 ? -26.02400 -4.92700  12.54100 1.000 27.30000 ? 170 LEU B CB  1 
ATOM   1750 C  CG  . LEU B 1 170 ? -24.81700 -4.03800  12.81300 1.000 35.57000 ? 170 LEU B CG  1 
ATOM   1751 C  CD1 . LEU B 1 170 ? -23.61600 -4.50600  12.02200 1.000 30.92000 ? 170 LEU B CD1 1 
ATOM   1752 C  CD2 . LEU B 1 170 ? -25.10900 -2.57400  12.54800 1.000 31.48000 ? 170 LEU B CD2 1 
ATOM   1753 N  N   . ARG B 1 171 ? -28.72500 -6.61300  13.24900 1.000 26.48000 ? 171 ARG B N   1 
ATOM   1754 C  CA  . ARG B 1 171 ? -29.88800 -7.43500  12.84900 1.000 27.74000 ? 171 ARG B CA  1 
ATOM   1755 C  C   . ARG B 1 171 ? -31.17400 -6.75400  13.30600 1.000 25.30000 ? 171 ARG B C   1 
ATOM   1756 O  O   . ARG B 1 171 ? -32.02800 -6.61800  12.52800 1.000 31.07000 ? 171 ARG B O   1 
ATOM   1757 C  CB  . ARG B 1 171 ? -29.75300 -8.86000  13.39400 1.000 22.90000 ? 171 ARG B CB  1 
ATOM   1758 C  CG  . ARG B 1 171 ? -28.71900 -9.69700  12.66300 1.000 27.87000 ? 171 ARG B CG  1 
ATOM   1759 C  CD  . ARG B 1 171 ? -28.66200 -11.20300 12.80200 1.000 28.71000 ? 171 ARG B CD  1 
ATOM   1760 N  NE  . ARG B 1 171 ? -28.46800 -11.74300 14.11600 1.000 28.75000 ? 171 ARG B NE  1 
ATOM   1761 C  CZ  . ARG B 1 171 ? -27.33400 -11.83800 14.77200 1.000 32.94000 ? 171 ARG B CZ  1 
ATOM   1762 N  NH1 . ARG B 1 171 ? -26.21000 -11.44000 14.22000 1.000 30.40000 ? 171 ARG B NH1 1 
ATOM   1763 N  NH2 . ARG B 1 171 ? -27.33100 -12.35100 15.98300 1.000 29.20000 ? 171 ARG B NH2 1 
ATOM   1764 N  N   . LEU B 1 172 ? -31.21300 -6.25700  14.51600 1.000 25.09000 ? 172 LEU B N   1 
ATOM   1765 C  CA  . LEU B 1 172 ? -32.39000 -5.56700  15.06200 1.000 27.32000 ? 172 LEU B CA  1 
ATOM   1766 C  C   . LEU B 1 172 ? -32.68400 -4.27300  14.27600 1.000 35.62000 ? 172 LEU B C   1 
ATOM   1767 O  O   . LEU B 1 172 ? -33.84000 -3.97200  14.06200 1.000 34.81000 ? 172 LEU B O   1 
ATOM   1768 C  CB  . LEU B 1 172 ? -32.10300 -5.34100  16.54800 1.000 27.99000 ? 172 LEU B CB  1 
ATOM   1769 C  CG  . LEU B 1 172 ? -33.15100 -4.63600  17.39800 1.000 34.75000 ? 172 LEU B CG  1 
ATOM   1770 C  CD1 . LEU B 1 172 ? -34.32100 -5.53700  17.70300 1.000 34.01000 ? 172 LEU B CD1 1 
ATOM   1771 C  CD2 . LEU B 1 172 ? -32.54600 -4.13300  18.67500 1.000 29.24000 ? 172 LEU B CD2 1 
ATOM   1772 N  N   . ALA B 1 173 ? -31.65300 -3.53700  13.87900 1.000 32.85000 ? 173 ALA B N   1 
ATOM   1773 C  CA  . ALA B 1 173 ? -31.77000 -2.24300  13.17100 1.000 35.94000 ? 173 ALA B CA  1 
ATOM   1774 C  C   . ALA B 1 173 ? -32.19700 -2.32700  11.70300 1.000 34.16000 ? 173 ALA B C   1 
ATOM   1775 O  O   . ALA B 1 173 ? -32.75000 -1.39700  11.22300 1.000 27.33000 ? 173 ALA B O   1 
ATOM   1776 C  CB  . ALA B 1 173 ? -30.51800 -1.43700  13.36900 1.000 32.44000 ? 173 ALA B CB  1 
ATOM   1777 N  N   . VAL B 1 174 ? -31.89100 -3.41400  11.02100 1.000 36.88000 ? 174 VAL B N   1 
ATOM   1778 C  CA  . VAL B 1 174 ? -32.17800 -3.53800  9.57000  1.000 43.84000 ? 174 VAL B CA  1 
ATOM   1779 C  C   . VAL B 1 174 ? -33.19600 -4.65600  9.41500  1.000 48.30000 ? 174 VAL B C   1 
ATOM   1780 O  O   . VAL B 1 174 ? -32.86200 -5.68400  8.86200  1.000 55.79000 ? 174 VAL B O   1 
ATOM   1781 C  CB  . VAL B 1 174 ? -30.91600 -3.80600  8.71900  1.000 41.85000 ? 174 VAL B CB  1 
ATOM   1782 C  CG1 . VAL B 1 174 ? -29.87600 -2.73500  8.87700  1.000 41.04000 ? 174 VAL B CG1 1 
ATOM   1783 C  CG2 . VAL B 1 174 ? -30.26400 -5.12400  9.02600  1.000 40.83000 ? 174 VAL B CG2 1 
ATOM   1784 N  N   . SER B 1 175 ? -34.40300 -4.48300  9.92100  1.000 45.05000 ? 175 SER B N   1 
ATOM   1785 C  CA  . SER B 1 175 ? -35.39300 -5.55400  9.70500  1.000 56.49000 ? 175 SER B CA  1 
ATOM   1786 C  C   . SER B 1 175 ? -36.08600 -5.25700  8.36700  1.000 58.98000 ? 175 SER B C   1 
ATOM   1787 O  O   . SER B 1 175 ? -36.74900 -4.21700  8.27700  1.000 57.22000 ? 175 SER B O   1 
ATOM   1788 C  CB  . SER B 1 175 ? -36.35200 -5.64700  10.84700 1.000 56.30000 ? 175 SER B CB  1 
ATOM   1789 O  OG  . SER B 1 175 ? -35.75100 -6.23400  11.99000 1.000 51.68000 ? 175 SER B OG  1 
ATOM   1790 N  N   . THR B 1 176 ? -35.85700 -6.11500  7.37200  1.000 54.82000 ? 176 THR B N   1 
ATOM   1791 C  CA  . THR B 1 176 ? -36.40500 -5.96500  6.00500  1.000 61.70000 ? 176 THR B CA  1 
ATOM   1792 C  C   . THR B 1 176 ? -37.87600 -5.54900  6.04300  1.000 68.50000 ? 176 THR B C   1 
ATOM   1793 O  O   . THR B 1 176 ? -38.41700 -5.33100  4.94400  1.000 73.24000 ? 176 THR B O   1 
ATOM   1794 C  CB  . THR B 1 176 ? -36.26900 -7.26000  5.20100  1.000 63.77000 ? 176 THR B CB  1 
ATOM   1795 N  N   . GLY B 1 186 ? -26.03900 -10.99800 -8.29500 1.000 58.67000 ? 186 GLY B N   1 
ATOM   1796 C  CA  . GLY B 1 186 ? -26.20000 -12.44100 -8.02900 1.000 60.68000 ? 186 GLY B CA  1 
ATOM   1797 C  C   . GLY B 1 186 ? -26.08200 -12.66800 -6.54400 1.000 60.39000 ? 186 GLY B C   1 
ATOM   1798 O  O   . GLY B 1 186 ? -25.07900 -13.26300 -6.11700 1.000 58.71000 ? 186 GLY B O   1 
ATOM   1799 N  N   . LEU B 1 187 ? -27.13100 -12.31100 -5.81400 1.000 57.22000 ? 187 LEU B N   1 
ATOM   1800 C  CA  . LEU B 1 187 ? -26.99600 -12.25500 -4.35100 1.000 58.73000 ? 187 LEU B CA  1 
ATOM   1801 C  C   . LEU B 1 187 ? -26.60700 -13.60400 -3.76700 1.000 55.24000 ? 187 LEU B C   1 
ATOM   1802 O  O   . LEU B 1 187 ? -25.67200 -13.59300 -3.01000 1.000 53.81000 ? 187 LEU B O   1 
ATOM   1803 C  CB  . LEU B 1 187 ? -28.25500 -11.66300 -3.71000 1.000 65.52000 ? 187 LEU B CB  1 
ATOM   1804 N  N   . THR B 1 188 ? -27.21500 -14.70600 -4.17900 1.000 54.25000 ? 188 THR B N   1 
ATOM   1805 C  CA  . THR B 1 188 ? -26.78000 -15.97000 -3.54100 1.000 55.09000 ? 188 THR B CA  1 
ATOM   1806 C  C   . THR B 1 188 ? -25.31800 -16.25000 -3.88200 1.000 49.29000 ? 188 THR B C   1 
ATOM   1807 O  O   . THR B 1 188 ? -24.56000 -16.42100 -2.96800 1.000 46.35000 ? 188 THR B O   1 
ATOM   1808 C  CB  . THR B 1 188 ? -27.69000 -17.13200 -3.96200 1.000 53.71000 ? 188 THR B CB  1 
ATOM   1809 N  N   . ALA B 1 189 ? -24.97600 -16.14500 -5.15600 1.000 52.50000 ? 189 ALA B N   1 
ATOM   1810 C  CA  . ALA B 1 189 ? -23.64400 -16.45200 -5.71800 1.000 51.52000 ? 189 ALA B CA  1 
ATOM   1811 C  C   . ALA B 1 189 ? -22.52300 -15.45300 -5.41100 1.000 53.04000 ? 189 ALA B C   1 
ATOM   1812 O  O   . ALA B 1 189 ? -21.46400 -15.89900 -5.04600 1.000 51.41000 ? 189 ALA B O   1 
ATOM   1813 C  CB  . ALA B 1 189 ? -23.78400 -16.63600 -7.19300 1.000 52.46000 ? 189 ALA B CB  1 
ATOM   1814 N  N   . VAL B 1 190 ? -22.73500 -14.15900 -5.58400 1.000 50.02000 ? 190 VAL B N   1 
ATOM   1815 C  CA  . VAL B 1 190 ? -21.60400 -13.23800 -5.30100 1.000 51.10000 ? 190 VAL B CA  1 
ATOM   1816 C  C   . VAL B 1 190 ? -21.23800 -13.29200 -3.80700 1.000 49.02000 ? 190 VAL B C   1 
ATOM   1817 O  O   . VAL B 1 190 ? -20.08400 -13.43900 -3.51400 1.000 47.53000 ? 190 VAL B O   1 
ATOM   1818 C  CB  . VAL B 1 190 ? -21.80600 -11.82800 -5.86200 1.000 46.46000 ? 190 VAL B CB  1 
ATOM   1819 C  CG1 . VAL B 1 190 ? -22.76000 -11.01600 -5.02300 1.000 51.17000 ? 190 VAL B CG1 1 
ATOM   1820 C  CG2 . VAL B 1 190 ? -20.47100 -11.12300 -5.99700 1.000 48.19000 ? 190 VAL B CG2 1 
ATOM   1821 N  N   . VAL B 1 191 ? -22.22000 -13.32400 -2.91900 1.000 43.92000 ? 191 VAL B N   1 
ATOM   1822 C  CA  . VAL B 1 191 ? -21.93200 -13.43200 -1.46900 1.000 38.74000 ? 191 VAL B CA  1 
ATOM   1823 C  C   . VAL B 1 191 ? -21.23000 -14.74900 -1.17800 1.000 40.85000 ? 191 VAL B C   1 
ATOM   1824 O  O   . VAL B 1 191 ? -20.47300 -14.78500 -0.27300 1.000 43.88000 ? 191 VAL B O   1 
ATOM   1825 C  CB  . VAL B 1 191 ? -23.16600 -13.25500 -0.58600 1.000 39.05000 ? 191 VAL B CB  1 
ATOM   1826 C  CG1 . VAL B 1 191 ? -22.81000 -13.49800 0.85900  1.000 36.21000 ? 191 VAL B CG1 1 
ATOM   1827 C  CG2 . VAL B 1 191 ? -23.74700 -11.88000 -0.75700 1.000 35.62000 ? 191 VAL B CG2 1 
ATOM   1828 N  N   . HIS B 1 192 ? -21.57300 -15.83300 -1.85600 1.000 44.24000 ? 192 HIS B N   1 
ATOM   1829 C  CA  . HIS B 1 192 ? -20.82900 -17.08000 -1.62500 1.000 38.21000 ? 192 HIS B CA  1 
ATOM   1830 C  C   . HIS B 1 192 ? -19.36500 -16.91200 -2.03100 1.000 38.64000 ? 192 HIS B C   1 
ATOM   1831 O  O   . HIS B 1 192 ? -18.55600 -17.48500 -1.36700 1.000 40.83000 ? 192 HIS B O   1 
ATOM   1832 C  CB  . HIS B 1 192 ? -21.52100 -18.24600 -2.28800 1.000 42.59000 ? 192 HIS B CB  1 
ATOM   1833 C  CG  . HIS B 1 192 ? -21.06200 -19.52700 -1.72700 1.000 30.90000 ? 192 HIS B CG  1 
ATOM   1834 N  ND1 . HIS B 1 192 ? -21.39200 -19.90000 -0.49300 1.000 30.10000 ? 192 HIS B ND1 1 
ATOM   1835 C  CD2 . HIS B 1 192 ? -20.27400 -20.47400 -2.22300 1.000 27.61000 ? 192 HIS B CD2 1 
ATOM   1836 C  CE1 . HIS B 1 192 ? -20.85700 -21.04800 -0.24000 1.000 32.75000 ? 192 HIS B CE1 1 
ATOM   1837 N  NE2 . HIS B 1 192 ? -20.18200 -21.41300 -1.27200 1.000 31.09000 ? 192 HIS B NE2 1 
ATOM   1838 N  N   . GLN B 1 193 ? -19.07300 -16.18700 -3.10500 1.000 41.75000 ? 193 GLN B N   1 
ATOM   1839 C  CA  . GLN B 1 193 ? -17.67100 -15.93400 -3.51900 1.000 46.34000 ? 193 GLN B CA  1 
ATOM   1840 C  C   . GLN B 1 193 ? -16.93900 -15.17600 -2.41500 1.000 41.36000 ? 193 GLN B C   1 
ATOM   1841 O  O   . GLN B 1 193 ? -15.84200 -15.55700 -2.11200 1.000 41.81000 ? 193 GLN B O   1 
ATOM   1842 C  CB  . GLN B 1 193 ? -17.60900 -15.06000 -4.76600 1.000 51.58000 ? 193 GLN B CB  1 
ATOM   1843 C  CG  . GLN B 1 193 ? -16.25800 -14.39900 -5.02200 1.000 54.83000 ? 193 GLN B CG  1 
ATOM   1844 C  CD  . GLN B 1 193 ? -16.01100 -12.97100 -4.57800 1.000 53.34000 ? 193 GLN B CD  1 
ATOM   1845 O  OE1 . GLN B 1 193 ? -16.89900 -12.13600 -4.55700 1.000 52.79000 ? 193 GLN B OE1 1 
ATOM   1846 N  NE2 . GLN B 1 193 ? -14.77200 -12.67100 -4.25400 1.000 41.09000 ? 193 GLN B NE2 1 
ATOM   1847 N  N   . GLU B 1 194 ? -17.55200 -14.15800 -1.83800 1.000 36.75000 ? 194 GLU B N   1 
ATOM   1848 C  CA  . GLU B 1 194 ? -16.90100 -13.40900 -0.73900 1.000 36.30000 ? 194 GLU B CA  1 
ATOM   1849 C  C   . GLU B 1 194 ? -16.75900 -14.28600 0.49900  1.000 34.36000 ? 194 GLU B C   1 
ATOM   1850 O  O   . GLU B 1 194 ? -15.69800 -14.33600 1.03600  1.000 34.63000 ? 194 GLU B O   1 
ATOM   1851 C  CB  . GLU B 1 194 ? -17.72800 -12.19200 -0.35300 1.000 36.32000 ? 194 GLU B CB  1 
ATOM   1852 C  CG  . GLU B 1 194 ? -17.88300 -11.17600 -1.45300 1.000 37.36000 ? 194 GLU B CG  1 
ATOM   1853 C  CD  . GLU B 1 194 ? -19.00100 -10.17600 -1.22500 1.000 39.11000 ? 194 GLU B CD  1 
ATOM   1854 O  OE1 . GLU B 1 194 ? -19.28200 -9.42200  -2.11100 1.000 39.79000 ? 194 GLU B OE1 1 
ATOM   1855 O  OE2 . GLU B 1 194 ? -19.56200 -10.17100 -0.18200 1.000 34.17000 ? 194 GLU B OE2 1 
ATOM   1856 N  N   . HIS B 1 195 ? -17.82000 -15.02400 0.84000  1.000 34.43000 ? 195 HIS B N   1 
ATOM   1857 C  CA  . HIS B 1 195 ? -17.80500 -15.94200 2.01000  1.000 32.09000 ? 195 HIS B CA  1 
ATOM   1858 C  C   . HIS B 1 195 ? -16.69400 -16.98700 1.84200  1.000 34.82000 ? 195 HIS B C   1 
ATOM   1859 O  O   . HIS B 1 195 ? -16.03900 -17.31000 2.85300  1.000 31.03000 ? 195 HIS B O   1 
ATOM   1860 C  CB  . HIS B 1 195 ? -19.18500 -16.58900 2.20100  1.000 36.42000 ? 195 HIS B CB  1 
ATOM   1861 C  CG  . HIS B 1 195 ? -20.08100 -15.82900 3.12000  1.000 33.02000 ? 195 HIS B CG  1 
ATOM   1862 N  ND1 . HIS B 1 195 ? -21.44200 -16.05600 3.17900  1.000 28.63000 ? 195 HIS B ND1 1 
ATOM   1863 C  CD2 . HIS B 1 195 ? -19.82000 -14.85100 4.01400  1.000 30.02000 ? 195 HIS B CD2 1 
ATOM   1864 C  CE1 . HIS B 1 195 ? -21.98200 -15.25000 4.07100  1.000 29.52000 ? 195 HIS B CE1 1 
ATOM   1865 N  NE2 . HIS B 1 195 ? -21.00700 -14.50000 4.59800  1.000 31.93000 ? 195 HIS B NE2 1 
ATOM   1866 N  N   . VAL B 1 196 ? -16.49000 -17.49400 0.61900  1.000 34.99000 ? 196 VAL B N   1 
ATOM   1867 C  CA  . VAL B 1 196 ? -15.42600 -18.52200 0.38100  1.000 39.15000 ? 196 VAL B CA  1 
ATOM   1868 C  C   . VAL B 1 196 ? -13.98100 -17.96800 0.45200  1.000 33.91000 ? 196 VAL B C   1 
ATOM   1869 O  O   . VAL B 1 196 ? -13.11700 -18.67700 0.83000  1.000 35.50000 ? 196 VAL B O   1 
ATOM   1870 C  CB  . VAL B 1 196 ? -15.71200 -19.43200 -0.82900 1.000 33.56000 ? 196 VAL B CB  1 
ATOM   1871 C  CG1 . VAL B 1 196 ? -15.42000 -18.74400 -2.13200 1.000 40.18000 ? 196 VAL B CG1 1 
ATOM   1872 C  CG2 . VAL B 1 196 ? -14.95300 -20.73800 -0.77700 1.000 35.17000 ? 196 VAL B CG2 1 
ATOM   1873 N  N   . ALA B 1 197 ? -13.73400 -16.75600 0.00500  1.000 31.66000 ? 197 ALA B N   1 
ATOM   1874 C  CA  . ALA B 1 197 ? -12.38700 -16.17900 0.05700  1.000 30.08000 ? 197 ALA B CA  1 
ATOM   1875 C  C   . ALA B 1 197 ? -11.93000 -16.02000 1.50900  1.000 30.23000 ? 197 ALA B C   1 
ATOM   1876 O  O   . ALA B 1 197 ? -10.78400 -16.06500 1.73500  1.000 32.60000 ? 197 ALA B O   1 
ATOM   1877 C  CB  . ALA B 1 197 ? -12.34300 -14.91900 -0.72600 1.000 28.49000 ? 197 ALA B CB  1 
ATOM   1878 N  N   . VAL B 1 198 ? -12.82000 -15.70100 2.42600  1.000 32.79000 ? 198 VAL B N   1 
ATOM   1879 C  CA  . VAL B 1 198 ? -12.43500 -15.59900 3.85300  1.000 31.31000 ? 198 VAL B CA  1 
ATOM   1880 C  C   . VAL B 1 198 ? -12.04900 -16.97600 4.37600  1.000 34.71000 ? 198 VAL B C   1 
ATOM   1881 O  O   . VAL B 1 198 ? -11.09300 -17.07000 5.10200  1.000 31.15000 ? 198 VAL B O   1 
ATOM   1882 C  CB  . VAL B 1 198 ? -13.59400 -15.02800 4.67400  1.000 31.53000 ? 198 VAL B CB  1 
ATOM   1883 C  CG1 . VAL B 1 198 ? -13.36700 -15.20100 6.14600  1.000 28.56000 ? 198 VAL B CG1 1 
ATOM   1884 C  CG2 . VAL B 1 198 ? -13.86700 -13.59000 4.34300  1.000 31.90000 ? 198 VAL B CG2 1 
ATOM   1885 N  N   . TYR B 1 199 ? -12.83600 -17.98800 4.01400  1.000 36.35000 ? 199 TYR B N   1 
ATOM   1886 C  CA  . TYR B 1 199 ? -12.60400 -19.37600 4.47000  1.000 32.62000 ? 199 TYR B CA  1 
ATOM   1887 C  C   . TYR B 1 199 ? -11.28900 -19.92100 3.92400  1.000 33.33000 ? 199 TYR B C   1 
ATOM   1888 O  O   . TYR B 1 199 ? -10.65800 -20.54200 4.69600  1.000 38.00000 ? 199 TYR B O   1 
ATOM   1889 C  CB  . TYR B 1 199 ? -13.74600 -20.29300 4.07000  1.000 36.25000 ? 199 TYR B CB  1 
ATOM   1890 C  CG  . TYR B 1 199 ? -13.52400 -21.72700 4.43600  1.000 32.36000 ? 199 TYR B CG  1 
ATOM   1891 C  CD1 . TYR B 1 199 ? -13.48200 -22.11300 5.74900  1.000 32.06000 ? 199 TYR B CD1 1 
ATOM   1892 C  CD2 . TYR B 1 199 ? -13.38200 -22.69800 3.47500  1.000 36.48000 ? 199 TYR B CD2 1 
ATOM   1893 C  CE1 . TYR B 1 199 ? -13.34200 -23.43300 6.10900  1.000 34.96000 ? 199 TYR B CE1 1 
ATOM   1894 C  CE2 . TYR B 1 199 ? -13.18800 -24.02400 3.81300  1.000 37.29000 ? 199 TYR B CE2 1 
ATOM   1895 C  CZ  . TYR B 1 199 ? -13.17400 -24.39200 5.13600  1.000 36.18000 ? 199 TYR B CZ  1 
ATOM   1896 O  OH  . TYR B 1 199 ? -12.98400 -25.67300 5.50300  1.000 42.97000 ? 199 TYR B OH  1 
ATOM   1897 N  N   . ASP B 1 200 ? -10.93500 -19.67300 2.66700  1.000 29.64000 ? 200 ASP B N   1 
ATOM   1898 C  CA  . ASP B 1 200 ? -9.65000  -20.15800 2.10500  1.000 35.34000 ? 200 ASP B CA  1 
ATOM   1899 C  C   . ASP B 1 200 ? -8.46700  -19.47600 2.83100  1.000 42.20000 ? 200 ASP B C   1 
ATOM   1900 O  O   . ASP B 1 200 ? -7.57800  -20.18800 3.31400  1.000 37.73000 ? 200 ASP B O   1 
ATOM   1901 C  CB  . ASP B 1 200 ? -9.61600  -20.04600 0.57500  1.000 31.97000 ? 200 ASP B CB  1 
ATOM   1902 C  CG  . ASP B 1 200 ? -10.64300 -20.87100 -0.18900 1.000 38.73000 ? 200 ASP B CG  1 
ATOM   1903 O  OD1 . ASP B 1 200 ? -11.36400 -21.57600 0.42200  1.000 37.60000 ? 200 ASP B OD1 1 
ATOM   1904 O  OD2 . ASP B 1 200 ? -10.72000 -20.75000 -1.38900 1.000 37.16000 ? 200 ASP B OD2 1 
ATOM   1905 N  N   . ALA B 1 201 ? -8.53200  -18.14800 3.02200  1.000 36.97000 ? 201 ALA B N   1 
ATOM   1906 C  CA  . ALA B 1 201 ? -7.45800  -17.40600 3.70900  1.000 34.97000 ? 201 ALA B CA  1 
ATOM   1907 C  C   . ALA B 1 201 ? -7.34700  -17.93200 5.12400  1.000 33.83000 ? 201 ALA B C   1 
ATOM   1908 O  O   . ALA B 1 201 ? -6.28200  -18.13700 5.55500  1.000 37.11000 ? 201 ALA B O   1 
ATOM   1909 C  CB  . ALA B 1 201 ? -7.76000  -15.93900 3.72400  1.000 35.08000 ? 201 ALA B CB  1 
ATOM   1910 N  N   . ILE B 1 202 ? -8.46200  -18.15200 5.79200  1.000 34.22000 ? 202 ILE B N   1 
ATOM   1911 C  CA  . ILE B 1 202 ? -8.38100  -18.70700 7.15700  1.000 31.98000 ? 202 ILE B CA  1 
ATOM   1912 C  C   . ILE B 1 202 ? -7.81500  -20.12000 7.07000  1.000 34.58000 ? 202 ILE B C   1 
ATOM   1913 O  O   . ILE B 1 202 ? -6.98900  -20.44600 7.85900  1.000 35.42000 ? 202 ILE B O   1 
ATOM   1914 C  CB  . ILE B 1 202 ? -9.72300  -18.60600 7.88300  1.000 31.06000 ? 202 ILE B CB  1 
ATOM   1915 C  CG1 . ILE B 1 202 ? -10.08900 -17.14700 8.16000  1.000 29.53000 ? 202 ILE B CG1 1 
ATOM   1916 C  CG2 . ILE B 1 202 ? -9.73100  -19.46900 9.12300  1.000 28.26000 ? 202 ILE B CG2 1 
ATOM   1917 C  CD1 . ILE B 1 202 ? -11.40300 -16.94000 8.82600  1.000 25.37000 ? 202 ILE B CD1 1 
ATOM   1918 N  N   . LEU B 1 203 ? -8.22100  -20.90400 6.08600  1.000 38.26000 ? 203 LEU B N   1 
ATOM   1919 C  CA  . LEU B 1 203 ? -7.69200  -22.28100 6.00500  1.000 40.40000 ? 203 LEU B CA  1 
ATOM   1920 C  C   . LEU B 1 203 ? -6.18600  -22.25500 5.77800  1.000 36.88000 ? 203 LEU B C   1 
ATOM   1921 O  O   . LEU B 1 203 ? -5.49000  -22.95900 6.47300  1.000 35.11000 ? 203 LEU B O   1 
ATOM   1922 C  CB  . LEU B 1 203 ? -8.42000  -23.10700 4.94800  1.000 37.46000 ? 203 LEU B CB  1 
ATOM   1923 C  CG  . LEU B 1 203 ? -8.08000  -24.58600 5.04700  1.000 38.25000 ? 203 LEU B CG  1 
ATOM   1924 C  CD1 . LEU B 1 203 ? -9.29900  -25.44200 5.23200  1.000 36.09000 ? 203 LEU B CD1 1 
ATOM   1925 C  CD2 . LEU B 1 203 ? -7.27900  -25.02900 3.85800  1.000 45.75000 ? 203 LEU B CD2 1 
ATOM   1926 N  N   . ALA B 1 204 ? -5.71400  -21.35500 4.93800  1.000 33.42000 ? 204 ALA B N   1 
ATOM   1927 C  CA  . ALA B 1 204 ? -4.26700  -21.26100 4.65400  1.000 40.16000 ? 204 ALA B CA  1 
ATOM   1928 C  C   . ALA B 1 204 ? -3.41400  -20.83400 5.85900  1.000 34.49000 ? 204 ALA B C   1 
ATOM   1929 O  O   . ALA B 1 204 ? -2.25500  -21.00000 5.79300  1.000 38.39000 ? 204 ALA B O   1 
ATOM   1930 C  CB  . ALA B 1 204 ? -4.01300  -20.41600 3.44200  1.000 39.25000 ? 204 ALA B CB  1 
ATOM   1931 N  N   . GLY B 1 205 ? -3.97300  -20.23000 6.88800  1.000 33.92000 ? 205 GLY B N   1 
ATOM   1932 C  CA  . GLY B 1 205 ? -3.19700  -19.72700 8.02100  1.000 33.12000 ? 205 GLY B CA  1 
ATOM   1933 C  C   . GLY B 1 205 ? -2.66500  -18.36000 7.69100  1.000 35.14000 ? 205 GLY B C   1 
ATOM   1934 O  O   . GLY B 1 205 ? -1.78800  -17.93700 8.35200  1.000 42.57000 ? 205 GLY B O   1 
ATOM   1935 N  N   . ASP B 1 206 ? -3.20400  -17.71600 6.68000  1.000 33.06000 ? 206 ASP B N   1 
ATOM   1936 C  CA  . ASP B 1 206 ? -2.70700  -16.39700 6.24900  1.000 37.19000 ? 206 ASP B CA  1 
ATOM   1937 C  C   . ASP B 1 206 ? -3.52800  -15.30200 6.91900  1.000 36.38000 ? 206 ASP B C   1 
ATOM   1938 O  O   . ASP B 1 206 ? -4.62100  -15.13300 6.51900  1.000 35.09000 ? 206 ASP B O   1 
ATOM   1939 C  CB  . ASP B 1 206 ? -2.83100  -16.32300 4.73300  1.000 34.34000 ? 206 ASP B CB  1 
ATOM   1940 C  CG  . ASP B 1 206 ? -2.04300  -15.19700 4.11400  1.000 40.70000 ? 206 ASP B CG  1 
ATOM   1941 O  OD1 . ASP B 1 206 ? -1.33000  -14.56300 4.82600  1.000 47.08000 ? 206 ASP B OD1 1 
ATOM   1942 O  OD2 . ASP B 1 206 ? -2.15100  -14.98900 2.94400  1.000 40.72000 ? 206 ASP B OD2 1 
ATOM   1943 N  N   . PRO B 1 207 ? -3.03200  -14.57100 7.93100  1.000 39.73000 ? 207 PRO B N   1 
ATOM   1944 C  CA  . PRO B 1 207 ? -3.78400  -13.51300 8.56800  1.000 32.42000 ? 207 PRO B CA  1 
ATOM   1945 C  C   . PRO B 1 207 ? -4.05500  -12.28400 7.71600  1.000 35.28000 ? 207 PRO B C   1 
ATOM   1946 O  O   . PRO B 1 207 ? -5.08800  -11.79600 7.85000  1.000 33.37000 ? 207 PRO B O   1 
ATOM   1947 C  CB  . PRO B 1 207 ? -3.02800  -13.17100 9.82700  1.000 27.29000 ? 207 PRO B CB  1 
ATOM   1948 C  CG  . PRO B 1 207 ? -2.14300  -14.35600 9.97300  1.000 39.95000 ? 207 PRO B CG  1 
ATOM   1949 C  CD  . PRO B 1 207 ? -1.75600  -14.72400 8.56100  1.000 40.89000 ? 207 PRO B CD  1 
ATOM   1950 N  N   . ASP B 1 208 ? -3.08300  -11.83600 6.92700  1.000 38.31000 ? 208 ASP B N   1 
ATOM   1951 C  CA  . ASP B 1 208 ? -3.27300  -10.62400 6.09200  1.000 37.70000 ? 208 ASP B CA  1 
ATOM   1952 C  C   . ASP B 1 208 ? -4.32800  -10.85900 5.00900  1.000 34.89000 ? 208 ASP B C   1 
ATOM   1953 O  O   . ASP B 1 208 ? -5.16300  -10.03000 4.85900  1.000 35.12000 ? 208 ASP B O   1 
ATOM   1954 C  CB  . ASP B 1 208 ? -1.95400  -10.10400 5.52300  1.000 37.99000 ? 208 ASP B CB  1 
ATOM   1955 C  CG  . ASP B 1 208 ? -0.89500  -9.77500  6.55400  1.000 50.46000 ? 208 ASP B CG  1 
ATOM   1956 O  OD1 . ASP B 1 208 ? -1.17800  -9.02500  7.51500  1.000 48.88000 ? 208 ASP B OD1 1 
ATOM   1957 O  OD2 . ASP B 1 208 ? 0.21300   -10.26500 6.37900  1.000 55.65000 ? 208 ASP B OD2 1 
ATOM   1958 N  N   . ARG B 1 209 ? -4.27700  -11.98000 4.31000  1.000 33.67000 ? 209 ARG B N   1 
ATOM   1959 C  CA  . ARG B 1 209 ? -5.29800  -12.25500 3.27200  1.000 34.64000 ? 209 ARG B CA  1 
ATOM   1960 C  C   . ARG B 1 209 ? -6.67400  -12.42000 3.91400  1.000 30.75000 ? 209 ARG B C   1 
ATOM   1961 O  O   . ARG B 1 209 ? -7.60400  -11.98700 3.32300  1.000 34.72000 ? 209 ARG B O   1 
ATOM   1962 C  CB  . ARG B 1 209 ? -4.94500  -13.48000 2.44000  1.000 40.34000 ? 209 ARG B CB  1 
ATOM   1963 C  CG  . ARG B 1 209 ? -5.41300  -13.39900 0.99800  1.000 38.75000 ? 209 ARG B CG  1 
ATOM   1964 C  CD  . ARG B 1 209 ? -4.76800  -14.47500 0.15800  1.000 43.07000 ? 209 ARG B CD  1 
ATOM   1965 N  NE  . ARG B 1 209 ? -5.63200  -15.59700 -0.14000 1.000 46.80000 ? 209 ARG B NE  1 
ATOM   1966 C  CZ  . ARG B 1 209 ? -5.62600  -16.76700 0.45500  1.000 43.17000 ? 209 ARG B CZ  1 
ATOM   1967 N  NH1 . ARG B 1 209 ? -4.79800  -17.01100 1.43600  1.000 40.54000 ? 209 ARG B NH1 1 
ATOM   1968 N  NH2 . ARG B 1 209 ? -6.45400  -17.69600 0.04800  1.000 41.56000 ? 209 ARG B NH2 1 
ATOM   1969 N  N   . ALA B 1 210 ? -6.75700  -13.04200 5.07500  1.000 30.56000 ? 210 ALA B N   1 
ATOM   1970 C  CA  . ALA B 1 210 ? -8.03300  -13.21300 5.78100  1.000 31.21000 ? 210 ALA B CA  1 
ATOM   1971 C  C   . ALA B 1 210 ? -8.64100  -11.85800 6.14800  1.000 30.56000 ? 210 ALA B C   1 
ATOM   1972 O  O   . ALA B 1 210 ? -9.80800  -11.68200 5.96100  1.000 30.18000 ? 210 ALA B O   1 
ATOM   1973 C  CB  . ALA B 1 210 ? -7.79600  -14.03600 7.00600  1.000 27.25000 ? 210 ALA B CB  1 
ATOM   1974 N  N   . ARG B 1 211 ? -7.83800  -10.94200 6.65800  1.000 27.62000 ? 211 ARG B N   1 
ATOM   1975 C  CA  . ARG B 1 211 ? -8.34000  -9.61300  7.04700  1.000 27.09000 ? 211 ARG B CA  1 
ATOM   1976 C  C   . ARG B 1 211 ? -8.87000  -8.91500  5.80700  1.000 27.02000 ? 211 ARG B C   1 
ATOM   1977 O  O   . ARG B 1 211 ? -9.89000  -8.34800  5.89100  1.000 27.40000 ? 211 ARG B O   1 
ATOM   1978 C  CB  . ARG B 1 211 ? -7.21700  -8.78600  7.66500  1.000 26.66000 ? 211 ARG B CB  1 
ATOM   1979 C  CG  . ARG B 1 211 ? -7.60000  -7.37100  8.05500  1.000 26.05000 ? 211 ARG B CG  1 
ATOM   1980 C  CD  . ARG B 1 211 ? -6.44700  -6.51200  8.51800  1.000 23.62000 ? 211 ARG B CD  1 
ATOM   1981 N  NE  . ARG B 1 211 ? -5.89300  -6.95500  9.75900  1.000 25.63000 ? 211 ARG B NE  1 
ATOM   1982 C  CZ  . ARG B 1 211 ? -6.27400  -6.61100  10.96200 1.000 29.57000 ? 211 ARG B CZ  1 
ATOM   1983 N  NH1 . ARG B 1 211 ? -5.67700  -7.13900  11.99900 1.000 36.73000 ? 211 ARG B NH1 1 
ATOM   1984 N  NH2 . ARG B 1 211 ? -7.25300  -5.77900  11.16900 1.000 29.31000 ? 211 ARG B NH2 1 
ATOM   1985 N  N   . LEU B 1 212 ? -8.14100  -8.97400  4.70800  1.000 29.91000 ? 212 LEU B N   1 
ATOM   1986 C  CA  . LEU B 1 212 ? -8.62600  -8.30400  3.48700  1.000 30.13000 ? 212 LEU B CA  1 
ATOM   1987 C  C   . LEU B 1 212 ? -9.84100  -9.01700  2.91400  1.000 26.52000 ? 212 LEU B C   1 
ATOM   1988 O  O   . LEU B 1 212 ? -10.68000 -8.35200  2.51500  1.000 31.70000 ? 212 LEU B O   1 
ATOM   1989 C  CB  . LEU B 1 212 ? -7.52500  -8.07300  2.45900  1.000 35.39000 ? 212 LEU B CB  1 
ATOM   1990 C  CG  . LEU B 1 212 ? -7.27300  -6.60200  2.12900  1.000 48.02000 ? 212 LEU B CG  1 
ATOM   1991 C  CD1 . LEU B 1 212 ? -6.22100  -6.45500  1.04900  1.000 48.36000 ? 212 LEU B CD1 1 
ATOM   1992 C  CD2 . LEU B 1 212 ? -8.54000  -5.87300  1.72700  1.000 51.93000 ? 212 LEU B CD2 1 
ATOM   1993 N  N   . ALA B 1 213 ? -9.92700  -10.32900 2.95200  1.000 27.09000 ? 213 ALA B N   1 
ATOM   1994 C  CA  . ALA B 1 213 ? -11.15300 -11.00500 2.47800  1.000 28.97000 ? 213 ALA B CA  1 
ATOM   1995 C  C   . ALA B 1 213 ? -12.33800 -10.60300 3.35000  1.000 28.70000 ? 213 ALA B C   1 
ATOM   1996 O  O   . ALA B 1 213 ? -13.31600 -10.16200 2.81200  1.000 30.05000 ? 213 ALA B O   1 
ATOM   1997 C  CB  . ALA B 1 213 ? -10.98600 -12.50000 2.47600  1.000 25.53000 ? 213 ALA B CB  1 
ATOM   1998 N  N   . ALA B 1 214 ? -12.17800 -10.63500 4.65800  1.000 26.50000 ? 214 ALA B N   1 
ATOM   1999 C  CA  . ALA B 1 214 ? -13.28900 -10.27000 5.54300  1.000 22.93000 ? 214 ALA B CA  1 
ATOM   2000 C  C   . ALA B 1 214 ? -13.66800 -8.80000  5.36400  1.000 27.50000 ? 214 ALA B C   1 
ATOM   2001 O  O   . ALA B 1 214 ? -14.81300 -8.50000  5.51400  1.000 27.33000 ? 214 ALA B O   1 
ATOM   2002 C  CB  . ALA B 1 214 ? -13.00300 -10.65600 6.95100  1.000 21.23000 ? 214 ALA B CB  1 
ATOM   2003 N  N   . THR B 1 215 ? -12.69200 -7.93500  5.16200  1.000 25.52000 ? 215 THR B N   1 
ATOM   2004 C  CA  . THR B 1 215 ? -12.94900 -6.50100  4.98200  1.000 27.80000 ? 215 THR B CA  1 
ATOM   2005 C  C   . THR B 1 215 ? -13.67700 -6.26100  3.67000  1.000 30.16000 ? 215 THR B C   1 
ATOM   2006 O  O   . THR B 1 215 ? -14.62700 -5.55700  3.68300  1.000 31.44000 ? 215 THR B O   1 
ATOM   2007 C  CB  . THR B 1 215 ? -11.67100 -5.66600  4.99000  1.000 32.22000 ? 215 THR B CB  1 
ATOM   2008 O  OG1 . THR B 1 215 ? -11.03600 -5.81500  6.25100  1.000 28.36000 ? 215 THR B OG1 1 
ATOM   2009 C  CG2 . THR B 1 215 ? -11.98600 -4.21000  4.76700  1.000 31.18000 ? 215 THR B CG2 1 
ATOM   2010 N  N   . ARG B 1 216 ? -13.25200 -6.91800  2.61100  1.000 28.74000 ? 216 ARG B N   1 
ATOM   2011 C  CA  . ARG B 1 216 ? -13.88500 -6.76100  1.29600  1.000 28.98000 ? 216 ARG B CA  1 
ATOM   2012 C  C   . ARG B 1 216 ? -15.32700 -7.25700  1.37600  1.000 31.31000 ? 216 ARG B C   1 
ATOM   2013 O  O   . ARG B 1 216 ? -16.16700 -6.61800  0.82800  1.000 31.94000 ? 216 ARG B O   1 
ATOM   2014 C  CB  . ARG B 1 216 ? -13.04200 -7.40500  0.19700  1.000 29.23000 ? 216 ARG B CB  1 
ATOM   2015 N  N   . HIS B 1 217 ? -15.59000 -8.33800  2.09400  1.000 30.98000 ? 217 HIS B N   1 
ATOM   2016 C  CA  . HIS B 1 217 ? -16.97000 -8.84400  2.20300  1.000 30.32000 ? 217 HIS B CA  1 
ATOM   2017 C  C   . HIS B 1 217 ? -17.83300 -7.79000  2.87900  1.000 32.82000 ? 217 HIS B C   1 
ATOM   2018 O  O   . HIS B 1 217 ? -18.94600 -7.64200  2.48700  1.000 28.28000 ? 217 HIS B O   1 
ATOM   2019 C  CB  . HIS B 1 217 ? -16.99100 -10.18100 2.94200  1.000 28.84000 ? 217 HIS B CB  1 
ATOM   2020 C  CG  . HIS B 1 217 ? -18.31900 -10.66000 3.39400  1.000 26.87000 ? 217 HIS B CG  1 
ATOM   2021 N  ND1 . HIS B 1 217 ? -19.34900 -10.74600 2.58000  1.000 28.11000 ? 217 HIS B ND1 1 
ATOM   2022 C  CD2 . HIS B 1 217 ? -18.75700 -11.12300 4.56400  1.000 31.08000 ? 217 HIS B CD2 1 
ATOM   2023 C  CE1 . HIS B 1 217 ? -20.38000 -11.19100 3.21200  1.000 30.70000 ? 217 HIS B CE1 1 
ATOM   2024 N  NE2 . HIS B 1 217 ? -20.04900 -11.46300 4.41700  1.000 29.14000 ? 217 HIS B NE2 1 
ATOM   2025 N  N   . LEU B 1 218 ? -17.32500 -7.15600  3.91800  1.000 30.29000 ? 218 LEU B N   1 
ATOM   2026 C  CA  . LEU B 1 218 ? -18.12500 -6.13200  4.61100  1.000 32.06000 ? 218 LEU B CA  1 
ATOM   2027 C  C   . LEU B 1 218 ? -18.29000 -4.88000  3.74000  1.000 33.28000 ? 218 LEU B C   1 
ATOM   2028 O  O   . LEU B 1 218 ? -19.27900 -4.25100  3.85000  1.000 33.12000 ? 218 LEU B O   1 
ATOM   2029 C  CB  . LEU B 1 218 ? -17.62100 -5.90900  6.03800  1.000 29.36000 ? 218 LEU B CB  1 
ATOM   2030 C  CG  . LEU B 1 218 ? -17.60800 -7.12000  6.97100  1.000 30.74000 ? 218 LEU B CG  1 
ATOM   2031 C  CD1 . LEU B 1 218 ? -17.49600 -6.69300  8.40300  1.000 33.40000 ? 218 LEU B CD1 1 
ATOM   2032 C  CD2 . LEU B 1 218 ? -18.81700 -7.98800  6.81900  1.000 30.12000 ? 218 LEU B CD2 1 
ATOM   2033 N  N   . GLN B 1 219 ? -17.30900 -4.54400  2.92600  1.000 31.73000 ? 219 GLN B N   1 
ATOM   2034 C  CA  . GLN B 1 219 ? -17.40500 -3.32500  2.09100  1.000 34.66000 ? 219 GLN B CA  1 
ATOM   2035 C  C   . GLN B 1 219 ? -18.40800 -3.52800  0.94700  1.000 39.38000 ? 219 GLN B C   1 
ATOM   2036 O  O   . GLN B 1 219 ? -19.23700 -2.69300  0.74900  1.000 39.05000 ? 219 GLN B O   1 
ATOM   2037 C  CB  . GLN B 1 219 ? -16.02100 -2.87800  1.62700  1.000 37.37000 ? 219 GLN B CB  1 
ATOM   2038 C  CG  . GLN B 1 219 ? -15.38200 -1.82600  2.52500  1.000 35.52000 ? 219 GLN B CG  1 
ATOM   2039 C  CD  . GLN B 1 219 ? -13.87200 -1.86900  2.51100  1.000 41.88000 ? 219 GLN B CD  1 
ATOM   2040 O  OE1 . GLN B 1 219 ? -13.25700 -2.80400  2.03300  1.000 42.54000 ? 219 GLN B OE1 1 
ATOM   2041 N  NE2 . GLN B 1 219 ? -13.25000 -0.82800  3.01100  1.000 40.60000 ? 219 GLN B NE2 1 
ATOM   2042 N  N   . GLN B 1 220 ? -18.35000 -4.65700  0.26400  1.000 41.57000 ? 220 GLN B N   1 
ATOM   2043 C  CA  . GLN B 1 220 ? -19.28000 -4.96200  -0.84000 1.000 37.15000 ? 220 GLN B CA  1 
ATOM   2044 C  C   . GLN B 1 220 ? -20.68900 -5.08900  -0.28900 1.000 34.49000 ? 220 GLN B C   1 
ATOM   2045 O  O   . GLN B 1 220 ? -21.57000 -4.77200  -0.99200 1.000 38.70000 ? 220 GLN B O   1 
ATOM   2046 C  CB  . GLN B 1 220 ? -18.90600 -6.20700  -1.63100 1.000 36.04000 ? 220 GLN B CB  1 
ATOM   2047 C  CG  . GLN B 1 220 ? -17.60300 -6.18500  -2.40600 1.000 43.88000 ? 220 GLN B CG  1 
ATOM   2048 C  CD  . GLN B 1 220 ? -17.05600 -4.89100  -2.95200 1.000 47.81000 ? 220 GLN B CD  1 
ATOM   2049 O  OE1 . GLN B 1 220 ? -17.38500 -4.46300  -4.04900 1.000 51.12000 ? 220 GLN B OE1 1 
ATOM   2050 N  NE2 . GLN B 1 220 ? -16.14400 -4.29800  -2.21000 1.000 47.81000 ? 220 GLN B NE2 1 
ATOM   2051 N  N   . ALA B 1 221 ? -20.85400 -5.64900  0.89100  1.000 32.94000 ? 221 ALA B N   1 
ATOM   2052 C  CA  . ALA B 1 221 ? -22.18700 -5.77800  1.50200  1.000 35.05000 ? 221 ALA B CA  1 
ATOM   2053 C  C   . ALA B 1 221 ? -22.75300 -4.41400  1.84800  1.000 37.92000 ? 221 ALA B C   1 
ATOM   2054 O  O   . ALA B 1 221 ? -23.90200 -4.19900  1.60100  1.000 37.00000 ? 221 ALA B O   1 
ATOM   2055 C  CB  . ALA B 1 221 ? -22.12200 -6.61600  2.74400  1.000 35.93000 ? 221 ALA B CB  1 
ATOM   2056 N  N   . ALA B 1 222 ? -21.91400 -3.54300  2.39700  1.000 37.68000 ? 222 ALA B N   1 
ATOM   2057 C  CA  . ALA B 1 222 ? -22.32600 -2.19200  2.80400  1.000 36.32000 ? 222 ALA B CA  1 
ATOM   2058 C  C   . ALA B 1 222 ? -22.77700 -1.41200  1.57300  1.000 41.77000 ? 222 ALA B C   1 
ATOM   2059 O  O   . ALA B 1 222 ? -23.63400 -0.62800  1.71700  1.000 42.26000 ? 222 ALA B O   1 
ATOM   2060 C  CB  . ALA B 1 222 ? -21.25800 -1.48300  3.57000  1.000 34.57000 ? 222 ALA B CB  1 
ATOM   2061 N  N   . SER B 1 223 ? -22.10000 -1.58500  0.45400  1.000 41.65000 ? 223 SER B N   1 
ATOM   2062 C  CA  . SER B 1 223 ? -22.45300 -0.94100  -0.82100 1.000 39.97000 ? 223 SER B CA  1 
ATOM   2063 C  C   . SER B 1 223 ? -23.79000 -1.48000  -1.30200 1.000 42.07000 ? 223 SER B C   1 
ATOM   2064 O  O   . SER B 1 223 ? -24.49200 -0.77900  -1.97400 1.000 44.02000 ? 223 SER B O   1 
ATOM   2065 C  CB  . SER B 1 223 ? -21.35600 -1.07400  -1.80700 1.000 42.70000 ? 223 SER B CB  1 
ATOM   2066 O  OG  . SER B 1 223 ? -20.16900 -0.52100  -1.27300 1.000 39.45000 ? 223 SER B OG  1 
ATOM   2067 N  N   . ARG B 1 224 ? -24.03100 -2.76100  -1.09900 1.000 42.58000 ? 224 ARG B N   1 
ATOM   2068 C  CA  . ARG B 1 224 ? -25.34300 -3.31100  -1.50700 1.000 42.28000 ? 224 ARG B CA  1 
ATOM   2069 C  C   . ARG B 1 224 ? -26.42900 -2.72600  -0.59600 1.000 43.89000 ? 224 ARG B C   1 
ATOM   2070 O  O   . ARG B 1 224 ? -27.46300 -2.36800  -1.08300 1.000 49.46000 ? 224 ARG B O   1 
ATOM   2071 C  CB  . ARG B 1 224 ? -25.28200 -4.82700  -1.71000 1.000 35.25000 ? 224 ARG B CB  1 
ATOM   2072 C  CG  . ARG B 1 224 ? -24.28700 -5.27400  -2.76600 1.000 33.85000 ? 224 ARG B CG  1 
ATOM   2073 C  CD  . ARG B 1 224 ? -24.15100 -6.75300  -3.02000 1.000 33.29000 ? 224 ARG B CD  1 
ATOM   2074 N  NE  . ARG B 1 224 ? -23.78200 -7.45000  -1.80100 1.000 39.23000 ? 224 ARG B NE  1 
ATOM   2075 C  CZ  . ARG B 1 224 ? -22.67500 -8.11600  -1.54300 1.000 32.84000 ? 224 ARG B CZ  1 
ATOM   2076 N  NH1 . ARG B 1 224 ? -22.53300 -8.66200  -0.36900 1.000 34.60000 ? 224 ARG B NH1 1 
ATOM   2077 N  NH2 . ARG B 1 224 ? -21.70500 -8.22400  -2.41100 1.000 31.45000 ? 224 ARG B NH2 1 
ATOM   2078 N  N   . LEU B 1 225 ? -26.19300 -2.59000  0.68900  1.000 39.20000 ? 225 LEU B N   1 
ATOM   2079 C  CA  . LEU B 1 225 ? -27.29100 -2.05700  1.52900  1.000 41.57000 ? 225 LEU B CA  1 
ATOM   2080 C  C   . LEU B 1 225 ? -27.62000 -0.59700  1.18500  1.000 47.02000 ? 225 LEU B C   1 
ATOM   2081 O  O   . LEU B 1 225 ? -28.76500 -0.33400  0.96200  1.000 45.78000 ? 225 LEU B O   1 
ATOM   2082 C  CB  . LEU B 1 225 ? -26.90800 -2.17900  2.99500  1.000 42.28000 ? 225 LEU B CB  1 
ATOM   2083 C  CG  . LEU B 1 225 ? -28.00900 -1.86200  3.99300  1.000 46.52000 ? 225 LEU B CG  1 
ATOM   2084 C  CD1 . LEU B 1 225 ? -29.23800 -2.70000  3.72400  1.000 41.94000 ? 225 LEU B CD1 1 
ATOM   2085 C  CD2 . LEU B 1 225 ? -27.51700 -2.11400  5.39700  1.000 43.04000 ? 225 LEU B CD2 1 
ATOM   2086 N  N   . ARG B 1 226 ? -26.62000 0.25400   0.97700  1.000 43.59000 ? 226 ARG B N   1 
ATOM   2087 C  CA  . ARG B 1 226 ? -26.80400 1.71200   0.79500  1.000 41.73000 ? 226 ARG B CA  1 
ATOM   2088 C  C   . ARG B 1 226 ? -27.73800 1.93300   -0.38200 1.000 45.56000 ? 226 ARG B C   1 
ATOM   2089 O  O   . ARG B 1 226 ? -28.75400 2.57700   -0.18600 1.000 48.57000 ? 226 ARG B O   1 
ATOM   2090 C  CB  . ARG B 1 226 ? -25.42300 2.28500   0.47000  1.000 40.07000 ? 226 ARG B CB  1 
ATOM   2091 C  CG  . ARG B 1 226 ? -25.22300 3.78200   0.62900  1.000 49.28000 ? 226 ARG B CG  1 
ATOM   2092 C  CD  . ARG B 1 226 ? -23.79500 4.18200   0.94700  1.000 40.68000 ? 226 ARG B CD  1 
ATOM   2093 N  NE  . ARG B 1 226 ? -22.85900 3.46700   0.11900  1.000 44.46000 ? 226 ARG B NE  1 
ATOM   2094 C  CZ  . ARG B 1 226 ? -21.86700 2.70900   0.57300  1.000 48.91000 ? 226 ARG B CZ  1 
ATOM   2095 N  NH1 . ARG B 1 226 ? -21.65700 2.59700   1.86600  1.000 43.04000 ? 226 ARG B NH1 1 
ATOM   2096 N  NH2 . ARG B 1 226 ? -21.08200 2.07900   -0.27100 1.000 43.51000 ? 226 ARG B NH2 1 
ATOM   2097 N  N   . LEU B 1 227 ? -27.44800 1.24800   -1.47400 1.000 41.03000 ? 227 LEU B N   1 
ATOM   2098 C  CA  . LEU B 1 227 ? -28.16300 1.27700   -2.76100 1.000 43.43000 ? 227 LEU B CA  1 
ATOM   2099 C  C   . LEU B 1 227 ? -29.56900 0.66400   -2.69300 1.000 47.81000 ? 227 LEU B C   1 
ATOM   2100 O  O   . LEU B 1 227 ? -30.38500 1.03600   -3.50500 1.000 50.42000 ? 227 LEU B O   1 
ATOM   2101 C  CB  . LEU B 1 227 ? -27.25000 0.53900   -3.72600 1.000 40.58000 ? 227 LEU B CB  1 
ATOM   2102 C  CG  . LEU B 1 227 ? -27.41800 0.79300   -5.21000 1.000 43.68000 ? 227 LEU B CG  1 
ATOM   2103 C  CD1 . LEU B 1 227 ? -27.84400 2.20600   -5.50900 1.000 40.79000 ? 227 LEU B CD1 1 
ATOM   2104 C  CD2 . LEU B 1 227 ? -26.12600 0.46900   -5.89400 1.000 49.48000 ? 227 LEU B CD2 1 
ATOM   2105 N  N   . ASP B 1 228 ? -29.78100 -0.36500  -1.87800 1.000 51.62000 ? 228 ASP B N   1 
ATOM   2106 C  CA  . ASP B 1 228 ? -31.11000 -1.00500  -1.71500 1.000 48.27000 ? 228 ASP B CA  1 
ATOM   2107 C  C   . ASP B 1 228 ? -32.04900 -0.03700  -1.02900 1.000 46.36000 ? 228 ASP B C   1 
ATOM   2108 O  O   . ASP B 1 228 ? -33.13100 0.11400   -1.48700 1.000 53.16000 ? 228 ASP B O   1 
ATOM   2109 C  CB  . ASP B 1 228 ? -31.04000 -2.30500  -0.90400 1.000 48.66000 ? 228 ASP B CB  1 
ATOM   2110 N  N   . LEU B 1 229 ? -31.57100 0.62200   0.00400  1.000 46.69000 ? 229 LEU B N   1 
ATOM   2111 C  CA  . LEU B 1 229 ? -32.37300 1.57600   0.78400  1.000 48.46000 ? 229 LEU B CA  1 
ATOM   2112 C  C   . LEU B 1 229 ? -32.78800 2.78800   -0.07000 1.000 53.84000 ? 229 LEU B C   1 
ATOM   2113 O  O   . LEU B 1 229 ? -33.76200 3.40600   0.27000  1.000 56.27000 ? 229 LEU B O   1 
ATOM   2114 C  CB  . LEU B 1 229 ? -31.57600 1.95900   2.01900  1.000 43.02000 ? 229 LEU B CB  1 
ATOM   2115 C  CG  . LEU B 1 229 ? -31.10900 0.78600   2.86000  1.000 45.42000 ? 229 LEU B CG  1 
ATOM   2116 C  CD1 . LEU B 1 229 ? -30.19600 1.26000   3.96600  1.000 51.98000 ? 229 LEU B CD1 1 
ATOM   2117 C  CD2 . LEU B 1 229 ? -32.26500 0.03200   3.45200  1.000 39.16000 ? 229 LEU B CD2 1 
ATOM   2118 N  N   . LEU B 1 230 ? -31.97900 3.21100   -1.03400 1.000 53.45000 ? 230 LEU B N   1 
ATOM   2119 C  CA  . LEU B 1 230 ? -32.32100 4.35300   -1.93000 1.000 53.12000 ? 230 LEU B CA  1 
ATOM   2120 C  C   . LEU B 1 230 ? -33.45400 3.99900   -2.88600 1.000 49.36000 ? 230 LEU B C   1 
ATOM   2121 O  O   . LEU B 1 230 ? -34.30100 4.81300   -3.07700 1.000 52.13000 ? 230 LEU B O   1 
ATOM   2122 C  CB  . LEU B 1 230 ? -31.06900 4.73500   -2.70900 1.000 50.28000 ? 230 LEU B CB  1 
ATOM   2123 C  CG  . LEU B 1 230 ? -29.99600 5.31700   -1.82200 1.000 45.27000 ? 230 LEU B CG  1 
ATOM   2124 C  CD1 . LEU B 1 230 ? -29.02300 6.10700   -2.64300 1.000 41.27000 ? 230 LEU B CD1 1 
ATOM   2125 C  CD2 . LEU B 1 230 ? -30.63500 6.15400   -0.74400 1.000 41.43000 ? 230 LEU B CD2 1 
ATOM   2126 N  N   . SER B 1 231 ? -33.42900 2.80200   -3.44900 1.000 50.73000 ? 231 SER B N   1 
ATOM   2127 C  CA  . SER B 1 231 ? -34.52400 2.39500   -4.34600 1.000 59.38000 ? 231 SER B CA  1 
ATOM   2128 C  C   . SER B 1 231 ? -35.66400 1.74300   -3.54200 1.000 61.01000 ? 231 SER B C   1 
ATOM   2129 O  O   . SER B 1 231 ? -36.27100 2.44400   -2.70500 1.000 58.54000 ? 231 SER B O   1 
ATOM   2130 C  CB  . SER B 1 231 ? -33.99300 1.49000   -5.39900 1.000 57.64000 ? 231 SER B CB  1 
ATOM   2131 O  OG  . SER B 1 231 ? -32.87200 2.07500   -6.01100 1.000 50.72000 ? 231 SER B OG  1 
HETATM 2132 ZN ZN  . ZN  C 2 .   ? -0.83200  5.09900   25.52400 1.000 24.68000 ? 301 ZN  A ZN  1 
HETATM 2133 ZN ZN  . ZN  D 2 .   ? -21.45800 -12.75100 5.39900  1.000 38.93000 ? 301 ZN  B ZN  1 
HETATM 2134 O  O   . HOH E 3 .   ? 6.90300   -1.76700  35.56300 1.000 30.00000 ? 401 HOH A O   1 
HETATM 2135 O  O   . HOH E 3 .   ? -2.86600  17.31500  34.51000 1.000 43.16000 ? 402 HOH A O   1 
HETATM 2136 O  O   . HOH E 3 .   ? 3.08000   9.35200   5.90400  1.000 42.94000 ? 403 HOH A O   1 
HETATM 2137 O  O   . HOH E 3 .   ? -9.03700  20.99900  20.28100 1.000 25.19000 ? 404 HOH A O   1 
HETATM 2138 O  O   . HOH E 3 .   ? 6.18000   -0.97100  46.29100 1.000 30.00000 ? 405 HOH A O   1 
HETATM 2139 O  O   . HOH E 3 .   ? -24.53200 0.49200   22.77500 1.000 28.29000 ? 406 HOH A O   1 
HETATM 2140 O  O   . HOH E 3 .   ? 8.99900   0.10700   21.45800 1.000 34.31000 ? 407 HOH A O   1 
HETATM 2141 O  O   . HOH E 3 .   ? -2.44900  -9.03000  24.01000 1.000 20.70000 ? 408 HOH A O   1 
HETATM 2142 O  O   . HOH E 3 .   ? 0.34000   -13.31100 29.04600 1.000 26.40000 ? 409 HOH A O   1 
HETATM 2143 O  O   . HOH E 3 .   ? 3.46200   3.52300   18.44300 1.000 21.12000 ? 410 HOH A O   1 
HETATM 2144 O  O   . HOH E 3 .   ? 6.31000   4.14800   41.81100 1.000 30.00000 ? 411 HOH A O   1 
HETATM 2145 O  O   . HOH E 3 .   ? -8.35400  14.65900  24.72600 1.000 25.74000 ? 412 HOH A O   1 
HETATM 2146 O  O   . HOH E 3 .   ? 3.53700   14.02600  10.13600 1.000 31.28000 ? 413 HOH A O   1 
HETATM 2147 O  O   . HOH E 3 .   ? -1.56500  -0.30300  8.44500  1.000 29.54000 ? 414 HOH A O   1 
HETATM 2148 O  O   . HOH E 3 .   ? -0.00400  -8.98400  27.59200 1.000 19.11000 ? 415 HOH A O   1 
HETATM 2149 O  O   . HOH E 3 .   ? 4.69400   7.03600   12.48000 1.000 26.93000 ? 416 HOH A O   1 
HETATM 2150 O  O   . HOH E 3 .   ? 2.15800   -8.05700  22.94500 1.000 23.04000 ? 417 HOH A O   1 
HETATM 2151 O  O   . HOH E 3 .   ? 9.33900   15.54000  33.45300 1.000 30.00000 ? 418 HOH A O   1 
HETATM 2152 O  O   . HOH E 3 .   ? -24.124   9.591     24.893   1.000 38.71000 ? 419 HOH A O   1 
HETATM 2153 O  O   . HOH E 3 .   ? 7.20200   17.98800  35.38400 1.000 48.67000 ? 420 HOH A O   1 
HETATM 2154 O  O   . HOH E 3 .   ? -5.32900  1.83600   38.35200 1.000 41.80000 ? 421 HOH A O   1 
HETATM 2155 O  O   . HOH E 3 .   ? 9.73900   12.40000  40.08800 1.000 30.00000 ? 422 HOH A O   1 
HETATM 2156 O  O   . HOH E 3 .   ? 16.733    7.468     33.884   1.000 32.55000 ? 423 HOH A O   1 
HETATM 2157 O  O   . HOH E 3 .   ? 14.14300  6.12100   27.06500 1.000 30.00000 ? 424 HOH A O   1 
HETATM 2158 O  O   . HOH E 3 .   ? 6.14600   -10.21200 27.49500 1.000 30.00000 ? 425 HOH A O   1 
HETATM 2159 O  O   . HOH E 3 .   ? 11.63700  6.63900   32.20100 1.000 30.00000 ? 426 HOH A O   1 
HETATM 2160 O  O   . HOH E 3 .   ? 15.68700  -1.41400  36.04700 1.000 49.65000 ? 427 HOH A O   1 
HETATM 2161 O  O   . HOH E 3 .   ? -8.71800  5.51500   22.16700 1.000 24.97000 ? 428 HOH A O   1 
HETATM 2162 O  O   . HOH E 3 .   ? 2.70400   1.33700   28.14700 1.000 30.42000 ? 429 HOH A O   1 
HETATM 2163 O  O   . HOH E 3 .   ? -2.50700  3.36200   26.32900 1.000 23.71000 ? 430 HOH A O   1 
HETATM 2164 O  O   . HOH E 3 .   ? -3.62300  -14.00600 40.20200 1.000 31.17000 ? 431 HOH A O   1 
HETATM 2165 O  O   . HOH E 3 .   ? -0.21500  -10.70100 30.06600 1.000 20.40000 ? 432 HOH A O   1 
HETATM 2166 O  O   . HOH E 3 .   ? -5.35300  -3.56200  13.14200 1.000 35.43000 ? 433 HOH A O   1 
HETATM 2167 O  O   . HOH E 3 .   ? -4.49900  16.71400  29.18900 1.000 34.87000 ? 434 HOH A O   1 
HETATM 2168 O  O   . HOH E 3 .   ? -0.33400  -19.55100 37.56400 1.000 36.56000 ? 435 HOH A O   1 
HETATM 2169 O  O   . HOH E 3 .   ? 3.95300   9.46200   26.52800 1.000 19.89000 ? 436 HOH A O   1 
HETATM 2170 O  O   . HOH E 3 .   ? -4.93400  4.30100   27.92700 1.000 30.30000 ? 437 HOH A O   1 
HETATM 2171 O  O   . HOH E 3 .   ? 6.88700   5.82900   9.05000  1.000 50.25000 ? 438 HOH A O   1 
HETATM 2172 O  O   . HOH E 3 .   ? 5.30900   6.80600   41.51900 1.000 53.37000 ? 439 HOH A O   1 
HETATM 2173 O  O   . HOH E 3 .   ? -0.04700  3.26700   27.30900 1.000 23.66000 ? 440 HOH A O   1 
HETATM 2174 O  O   . HOH E 3 .   ? 1.67100   14.62700  4.77000  1.000 39.81000 ? 441 HOH A O   1 
HETATM 2175 O  O   . HOH E 3 .   ? 6.06600   2.55900   17.61400 1.000 26.07000 ? 442 HOH A O   1 
HETATM 2176 O  O   . HOH E 3 .   ? 5.02500   -4.83100  17.91200 1.000 32.81000 ? 443 HOH A O   1 
HETATM 2177 O  O   . HOH E 3 .   ? 8.62700   9.48200   39.95200 1.000 30.00000 ? 444 HOH A O   1 
HETATM 2178 O  O   . HOH E 3 .   ? -3.50600  -5.56800  14.56800 1.000 30.00000 ? 445 HOH A O   1 
HETATM 2179 O  O   . HOH E 3 .   ? 1.91400   -1.53100  30.45900 1.000 30.00000 ? 446 HOH A O   1 
HETATM 2180 O  O   . HOH E 3 .   ? -5.30200  17.25100  27.02400 1.000 27.59000 ? 447 HOH A O   1 
HETATM 2181 O  O   . HOH E 3 .   ? 8.98100   3.83400   19.43100 1.000 23.96000 ? 448 HOH A O   1 
HETATM 2182 O  O   . HOH E 3 .   ? 5.16800   9.13600   28.59600 1.000 26.59000 ? 449 HOH A O   1 
HETATM 2183 O  O   . HOH E 3 .   ? 8.61200   -5.58700  26.90300 1.000 28.49000 ? 450 HOH A O   1 
HETATM 2184 O  O   . HOH E 3 .   ? -7.78800  21.64300  23.05500 1.000 39.92000 ? 451 HOH A O   1 
HETATM 2185 O  O   . HOH E 3 .   ? 19.25100  -0.00500  38.17800 1.000 48.09000 ? 452 HOH A O   1 
HETATM 2186 O  O   . HOH E 3 .   ? -21.17000 12.00400  12.08900 1.000 30.00000 ? 453 HOH A O   1 
HETATM 2187 O  O   . HOH E 3 .   ? 6.58700   -14.44000 44.94500 1.000 30.00000 ? 454 HOH A O   1 
HETATM 2188 O  O   . HOH E 3 .   ? -10.43100 15.17700  23.51900 1.000 24.56000 ? 455 HOH A O   1 
HETATM 2189 O  O   . HOH E 3 .   ? 4.48700   -9.11700  16.79500 1.000 44.92000 ? 456 HOH A O   1 
HETATM 2190 O  O   . HOH E 3 .   ? -11.04700 14.99400  4.50500  1.000 30.00000 ? 457 HOH A O   1 
HETATM 2191 O  O   . HOH E 3 .   ? -21.87200 11.40700  16.11300 1.000 30.00000 ? 458 HOH A O   1 
HETATM 2192 O  O   . HOH E 3 .   ? -3.95900  19.12700  29.76800 1.000 41.67000 ? 459 HOH A O   1 
HETATM 2193 O  O   . HOH E 3 .   ? -6.89400  10.55500  4.16000  1.000 34.62000 ? 460 HOH A O   1 
HETATM 2194 O  O   . HOH E 3 .   ? -13.21200 16.84300  20.01600 1.000 32.32000 ? 461 HOH A O   1 
HETATM 2195 O  O   . HOH E 3 .   ? 16.82700  -0.57100  38.04400 1.000 44.47000 ? 462 HOH A O   1 
HETATM 2196 O  O   . HOH E 3 .   ? 6.08800   -0.86000  13.68400 1.000 36.77000 ? 463 HOH A O   1 
HETATM 2197 O  O   . HOH E 3 .   ? 0.07500   -8.42400  21.10400 1.000 33.00000 ? 464 HOH A O   1 
HETATM 2198 O  O   . HOH E 3 .   ? -11.46000 16.29800  21.08700 1.000 32.26000 ? 465 HOH A O   1 
HETATM 2199 O  O   . HOH E 3 .   ? -11.64500 6.51600   6.04500  1.000 30.00000 ? 466 HOH A O   1 
HETATM 2200 O  O   . HOH E 3 .   ? 15.53000  8.33900   28.78900 1.000 36.61000 ? 467 HOH A O   1 
HETATM 2201 O  O   . HOH E 3 .   ? 6.55100   3.06100   15.46200 1.000 21.87000 ? 468 HOH A O   1 
HETATM 2202 O  O   . HOH E 3 .   ? 9.83000   -4.53400  28.75600 1.000 30.69000 ? 469 HOH A O   1 
HETATM 2203 O  O   . HOH E 3 .   ? -7.85700  4.62600   4.73100  1.000 33.34000 ? 470 HOH A O   1 
HETATM 2204 O  O   . HOH E 3 .   ? 9.296     20.622    41.292   1.000 40.20000 ? 471 HOH A O   1 
HETATM 2205 O  O   . HOH E 3 .   ? 13.02800  0.06000   22.50300 1.000 54.72000 ? 472 HOH A O   1 
HETATM 2206 O  O   . HOH E 3 .   ? 4.70600   14.78200  6.44500  1.000 35.85000 ? 473 HOH A O   1 
HETATM 2207 O  O   . HOH F 3 .   ? -24.62400 11.07700  10.80900 1.000 30.00000 ? 401 HOH B O   1 
HETATM 2208 O  O   . HOH F 3 .   ? -32.77400 -18.80300 7.92700  1.000 35.07000 ? 402 HOH B O   1 
HETATM 2209 O  O   . HOH F 3 .   ? -18.43400 -11.44400 13.35900 1.000 37.44000 ? 403 HOH B O   1 
HETATM 2210 O  O   . HOH F 3 .   ? -21.58700 -8.89400  10.28300 1.000 36.72000 ? 404 HOH B O   1 
HETATM 2211 O  O   . HOH F 3 .   ? -18.03300 -16.63300 19.64400 1.000 32.58000 ? 405 HOH B O   1 
HETATM 2212 O  O   . HOH F 3 .   ? -17.87700 -9.81900  -4.91500 1.000 47.27000 ? 406 HOH B O   1 
HETATM 2213 O  O   . HOH F 3 .   ? -12.32700 -25.67000 20.52400 1.000 26.97000 ? 407 HOH B O   1 
HETATM 2214 O  O   . HOH F 3 .   ? -27.45500 -19.13300 13.05600 1.000 25.32000 ? 408 HOH B O   1 
HETATM 2215 O  O   . HOH F 3 .   ? -15.18800 3.34800   7.54800  1.000 39.61000 ? 409 HOH B O   1 
HETATM 2216 O  O   . HOH F 3 .   ? -9.14100  -4.52600  9.72000  1.000 25.26000 ? 410 HOH B O   1 
HETATM 2217 O  O   . HOH F 3 .   ? -4.73100  -7.38000  5.02500  1.000 31.54000 ? 411 HOH B O   1 
HETATM 2218 O  O   . HOH F 3 .   ? -24.32000 -13.02500 15.41100 1.000 29.04000 ? 412 HOH B O   1 
HETATM 2219 O  O   . HOH F 3 .   ? -26.32700 -19.05100 -0.04600 1.000 39.80000 ? 413 HOH B O   1 
HETATM 2220 O  O   . HOH F 3 .   ? -31.17800 -24.88100 -3.01500 1.000 61.43000 ? 414 HOH B O   1 
HETATM 2221 O  O   . HOH F 3 .   ? -14.38000 -11.76300 0.70300  1.000 28.49000 ? 415 HOH B O   1 
HETATM 2222 O  O   . HOH F 3 .   ? -6.86500  -16.73100 24.39000 1.000 30.00000 ? 416 HOH B O   1 
HETATM 2223 O  O   . HOH F 3 .   ? -23.57200 -11.75400 4.55300  1.000 31.80000 ? 417 HOH B O   1 
HETATM 2224 O  O   . HOH F 3 .   ? -13.84500 -11.00900 -1.92600 1.000 38.21000 ? 418 HOH B O   1 
HETATM 2225 O  O   . HOH F 3 .   ? -7.03700  -22.42400 1.35100  1.000 38.84000 ? 419 HOH B O   1 
HETATM 2226 O  O   . HOH F 3 .   ? -17.12700 -19.73200 22.53100 1.000 28.60000 ? 420 HOH B O   1 
HETATM 2227 O  O   . HOH F 3 .   ? -23.03600 -13.59800 12.93800 1.000 30.73000 ? 421 HOH B O   1 
HETATM 2228 O  O   . HOH F 3 .   ? -36.85700 -17.87200 1.23400  1.000 30.00000 ? 422 HOH B O   1 
HETATM 2229 O  O   . HOH F 3 .   ? -3.26800  -8.75300  9.99500  1.000 32.23000 ? 423 HOH B O   1 
HETATM 2230 O  O   . HOH F 3 .   ? -23.24500 4.79600   16.11200 1.000 38.83000 ? 424 HOH B O   1 
HETATM 2231 O  O   . HOH F 3 .   ? -8.47900  -4.40700  4.82300  1.000 30.00000 ? 425 HOH B O   1 
HETATM 2232 O  O   . HOH F 3 .   ? -26.74100 -13.24200 0.15300  1.000 30.00000 ? 426 HOH B O   1 
HETATM 2233 O  O   . HOH F 3 .   ? -10.63900 -17.10100 26.26900 1.000 36.31000 ? 427 HOH B O   1 
HETATM 2234 O  O   . HOH F 3 .   ? -30.56600 -4.02300  -1.17700 1.000 30.00000 ? 428 HOH B O   1 
HETATM 2235 O  O   . HOH F 3 .   ? -23.31000 -12.53400 10.70400 1.000 29.35000 ? 429 HOH B O   1 
HETATM 2236 O  O   . HOH F 3 .   ? -14.29300 -6.79500  -4.30100 1.000 30.00000 ? 430 HOH B O   1 
HETATM 2237 O  O   . HOH F 3 .   ? -21.27200 -6.07300  -5.45900 1.000 30.00000 ? 431 HOH B O   1 
HETATM 2238 O  O   . HOH F 3 .   ? -22.86200 -10.15600 7.03800  1.000 31.96000 ? 432 HOH B O   1 
HETATM 2239 O  O   . HOH F 3 .   ? -25.34700 -19.50000 14.68900 1.000 28.95000 ? 433 HOH B O   1 
HETATM 2240 O  O   . HOH F 3 .   ? -31.89700 8.52500   6.53300  1.000 30.00000 ? 434 HOH B O   1 
HETATM 2241 O  O   . HOH F 3 .   ? -4.16200  -10.21300 14.29900 1.000 34.88000 ? 435 HOH B O   1 
HETATM 2242 O  O   . HOH F 3 .   ? -30.96700 -2.24600  -6.08200 1.000 29.78000 ? 436 HOH B O   1 
HETATM 2243 O  O   . HOH F 3 .   ? -6.43300  -19.26900 25.13300 1.000 41.53000 ? 437 HOH B O   1 
HETATM 2244 O  O   . HOH F 3 .   ? -21.70500 7.65800   8.06100  1.000 42.54000 ? 438 HOH B O   1 
HETATM 2245 O  O   . HOH F 3 .   ? -15.42900 -6.12800  26.78200 1.000 30.00000 ? 439 HOH B O   1 
HETATM 2246 O  O   . HOH F 3 .   ? -23.11400 -30.62400 8.81300  1.000 50.91000 ? 440 HOH B O   1 
HETATM 2247 O  O   . HOH F 3 .   ? -15.24400 1.52300   -0.50300 1.000 30.00000 ? 441 HOH B O   1 
HETATM 2248 O  O   . HOH F 3 .   ? -34.48500 -9.25100  3.29100  1.000 30.00000 ? 442 HOH B O   1 
# 
