data_8QO7
# 
_entry.id   8QO7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QO7         pdb_00008qo7 10.2210/pdb8qo7/pdb 
WWPDB D_1292133640 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QO7 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QNA unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN9 unspecified 
PDB . 8QMX unspecified 
PDB . 8QN3 unspecified 
PDB . 8QNE unspecified 
PDB . 8QNK unspecified 
PDB . 8QNP unspecified 
PDB . 8QNM unspecified 
PDB . 8QNW unspecified 
PDB . 8QNX unspecified 
PDB . 8QNY unspecified 
PDB . 8QO6 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              peter.macheroux@tugraz.at 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Macheroux 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0242-454X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bijelic, A.'      1 ? 
'Macheroux, P.'    2 ? 
'Kerschbaumer, B.' 3 ? 
# 
_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 structures of OPR3 wildtype and variants in complex with NAD(P)H' 
_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 'Kerschbaumer, B.' 1 ? 
primary 'Bijelic, A.'      2 ? 
primary 'Macheroux, P.'    3 ? 
# 
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 '12-oxophytodienoate reductase 3' 44373.121 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE' 456.344   1   ? ? ? ? 
3 non-polymer syn 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
747.437   2   ? ? ? ? 
4 non-polymer syn 'SULFATE ION' 96.063    1   ? ? ? ? 
5 water       nat water 18.015    531 ? ? ? ? 
# 
_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       
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPEYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPEYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE' FMN 
3 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
5J8 
4 'SULFATE ION' SO4 
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   MET n 
1 8   ALA n 
1 9   SER n 
1 10  SER n 
1 11  ALA n 
1 12  GLN n 
1 13  ASP n 
1 14  GLY n 
1 15  ASN n 
1 16  ASN n 
1 17  PRO n 
1 18  LEU n 
1 19  PHE n 
1 20  SER n 
1 21  PRO n 
1 22  TYR n 
1 23  LYS n 
1 24  MET n 
1 25  GLY n 
1 26  LYS n 
1 27  PHE n 
1 28  ASN n 
1 29  LEU n 
1 30  SER n 
1 31  HIS n 
1 32  ARG n 
1 33  VAL n 
1 34  VAL n 
1 35  LEU n 
1 36  ALA n 
1 37  PRO n 
1 38  MET n 
1 39  THR n 
1 40  ARG n 
1 41  CYS n 
1 42  ARG n 
1 43  ALA n 
1 44  LEU n 
1 45  ASN n 
1 46  ASN n 
1 47  ILE n 
1 48  PRO n 
1 49  GLN n 
1 50  ALA n 
1 51  ALA n 
1 52  LEU n 
1 53  GLY n 
1 54  GLU n 
1 55  TYR n 
1 56  TYR n 
1 57  GLU n 
1 58  GLN n 
1 59  ARG n 
1 60  ALA n 
1 61  THR n 
1 62  ALA n 
1 63  GLY n 
1 64  GLY n 
1 65  PHE n 
1 66  LEU n 
1 67  ILE n 
1 68  THR n 
1 69  GLU n 
1 70  GLY n 
1 71  THR n 
1 72  MET n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  THR n 
1 77  SER n 
1 78  ALA n 
1 79  GLY n 
1 80  PHE n 
1 81  PRO n 
1 82  HIS n 
1 83  VAL n 
1 84  PRO n 
1 85  GLY n 
1 86  ILE n 
1 87  PHE n 
1 88  THR n 
1 89  LYS n 
1 90  GLU n 
1 91  GLN n 
1 92  VAL n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  LYS n 
1 97  LYS n 
1 98  ILE n 
1 99  VAL n 
1 100 ASP n 
1 101 VAL n 
1 102 VAL n 
1 103 HIS n 
1 104 ALA n 
1 105 LYS n 
1 106 GLY n 
1 107 ALA n 
1 108 VAL n 
1 109 ILE n 
1 110 PHE n 
1 111 CYS n 
1 112 GLN n 
1 113 LEU n 
1 114 TRP n 
1 115 HIS n 
1 116 VAL n 
1 117 GLY n 
1 118 ARG n 
1 119 ALA n 
1 120 SER n 
1 121 HIS n 
1 122 GLU n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 PRO n 
1 127 ALA n 
1 128 GLY n 
1 129 ALA n 
1 130 ALA n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 SER n 
1 135 THR n 
1 136 GLU n 
1 137 LYS n 
1 138 PRO n 
1 139 ILE n 
1 140 SER n 
1 141 ASN n 
1 142 ARG n 
1 143 TRP n 
1 144 ARG n 
1 145 ILE n 
1 146 LEU n 
1 147 MET n 
1 148 PRO n 
1 149 ASP n 
1 150 GLY n 
1 151 THR n 
1 152 HIS n 
1 153 GLY n 
1 154 ILE n 
1 155 TYR n 
1 156 PRO n 
1 157 LYS n 
1 158 PRO n 
1 159 ARG n 
1 160 ALA n 
1 161 ILE n 
1 162 GLY n 
1 163 THR n 
1 164 TYR n 
1 165 GLU n 
1 166 ILE n 
1 167 SER n 
1 168 GLN n 
1 169 VAL n 
1 170 VAL n 
1 171 GLU n 
1 172 ASP n 
1 173 TYR n 
1 174 ARG n 
1 175 ARG n 
1 176 SER n 
1 177 ALA n 
1 178 LEU n 
1 179 ASN n 
1 180 ALA n 
1 181 ILE n 
1 182 GLU n 
1 183 ALA n 
1 184 GLY n 
1 185 PHE n 
1 186 ASP n 
1 187 GLY n 
1 188 ILE n 
1 189 GLU n 
1 190 ILE n 
1 191 HIS n 
1 192 GLY n 
1 193 ALA n 
1 194 HIS n 
1 195 GLY n 
1 196 TYR n 
1 197 LEU n 
1 198 ILE n 
1 199 ASP n 
1 200 GLN n 
1 201 PHE n 
1 202 LEU n 
1 203 LYS n 
1 204 ASP n 
1 205 GLY n 
1 206 ILE n 
1 207 ASN n 
1 208 ASP n 
1 209 ARG n 
1 210 THR n 
1 211 ASP n 
1 212 GLU n 
1 213 TYR n 
1 214 GLY n 
1 215 GLY n 
1 216 SER n 
1 217 LEU n 
1 218 ALA n 
1 219 ASN n 
1 220 ARG n 
1 221 CYS n 
1 222 LYS n 
1 223 PHE n 
1 224 ILE n 
1 225 THR n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 GLN n 
1 230 ALA n 
1 231 VAL n 
1 232 VAL n 
1 233 SER n 
1 234 ALA n 
1 235 ILE n 
1 236 GLY n 
1 237 ALA n 
1 238 ASP n 
1 239 ARG n 
1 240 VAL n 
1 241 GLY n 
1 242 VAL n 
1 243 ARG n 
1 244 VAL n 
1 245 SER n 
1 246 PRO n 
1 247 ALA n 
1 248 ILE n 
1 249 ASP n 
1 250 HIS n 
1 251 LEU n 
1 252 ASP n 
1 253 ALA n 
1 254 MET n 
1 255 ASP n 
1 256 SER n 
1 257 ASN n 
1 258 PRO n 
1 259 LEU n 
1 260 SER n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 ALA n 
1 265 VAL n 
1 266 VAL n 
1 267 GLU n 
1 268 ARG n 
1 269 LEU n 
1 270 ASN n 
1 271 LYS n 
1 272 ILE n 
1 273 GLN n 
1 274 LEU n 
1 275 HIS n 
1 276 SER n 
1 277 GLY n 
1 278 SER n 
1 279 LYS n 
1 280 LEU n 
1 281 ALA n 
1 282 TYR n 
1 283 LEU n 
1 284 HIS n 
1 285 VAL n 
1 286 THR n 
1 287 GLN n 
1 288 PRO n 
1 289 GLU n 
1 290 TYR n 
1 291 VAL n 
1 292 ALA n 
1 293 TYR n 
1 294 GLY n 
1 295 GLN n 
1 296 THR n 
1 297 GLU n 
1 298 ALA n 
1 299 GLY n 
1 300 ARG n 
1 301 LEU n 
1 302 GLY n 
1 303 SER n 
1 304 GLU n 
1 305 GLU n 
1 306 GLU n 
1 307 GLU n 
1 308 ALA n 
1 309 ARG n 
1 310 LEU n 
1 311 MET n 
1 312 ARG n 
1 313 THR n 
1 314 LEU n 
1 315 ARG n 
1 316 ASN n 
1 317 ALA n 
1 318 TYR n 
1 319 GLN n 
1 320 GLY n 
1 321 THR n 
1 322 PHE n 
1 323 ILE n 
1 324 CYS n 
1 325 SER n 
1 326 GLY n 
1 327 GLY n 
1 328 TYR n 
1 329 THR n 
1 330 ARG n 
1 331 GLU n 
1 332 LEU n 
1 333 GLY n 
1 334 ILE n 
1 335 GLU n 
1 336 ALA n 
1 337 VAL n 
1 338 ALA n 
1 339 GLN n 
1 340 GLY n 
1 341 ASP n 
1 342 ALA n 
1 343 ASP n 
1 344 LEU n 
1 345 VAL n 
1 346 SER n 
1 347 TYR n 
1 348 GLY n 
1 349 ARG n 
1 350 LEU n 
1 351 PHE n 
1 352 ILE n 
1 353 SER n 
1 354 ASN n 
1 355 PRO n 
1 356 ASP n 
1 357 LEU n 
1 358 VAL n 
1 359 MET n 
1 360 ARG n 
1 361 ILE n 
1 362 LYS n 
1 363 LEU n 
1 364 ASN n 
1 365 ALA n 
1 366 PRO n 
1 367 LEU n 
1 368 ASN n 
1 369 LYS n 
1 370 TYR n 
1 371 ASN n 
1 372 ARG n 
1 373 LYS n 
1 374 THR n 
1 375 PHE n 
1 376 TYR n 
1 377 THR n 
1 378 GLN n 
1 379 ASP n 
1 380 PRO n 
1 381 VAL n 
1 382 VAL n 
1 383 GLY n 
1 384 TYR n 
1 385 THR n 
1 386 ASP n 
1 387 TYR n 
1 388 PRO n 
1 389 PHE n 
1 390 LEU n 
1 391 GLN n 
1 392 GLY n 
1 393 ASN n 
1 394 GLY n 
1 395 SER n 
1 396 ASN n 
1 397 GLY n 
1 398 PRO n 
1 399 LEU n 
1 400 SER n 
1 401 ARG n 
1 402 LEU 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                   402 
_entity_src_gen.gene_src_common_name               tomato 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 OPR3 
_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      'Solanum lycopersicum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4081 
_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 
5J8 non-polymer         . 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
?                          'C21 H32 N7 O17 P3' 747.437 
ALA 'L-peptide linking' y ALANINE ?                          'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?                          'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                          'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                          'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                          'C3 H7 N O2 S'      121.158 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE' 'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P'   456.344 
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 
SO4 non-polymer         . 'SULFATE ION' ?                          'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE ?                          'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                          'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                          'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                          'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   MET 7   1   ?   ?   ?   A . n 
A 1 8   ALA 8   2   ?   ?   ?   A . n 
A 1 9   SER 9   3   ?   ?   ?   A . n 
A 1 10  SER 10  4   ?   ?   ?   A . n 
A 1 11  ALA 11  5   ?   ?   ?   A . n 
A 1 12  GLN 12  6   ?   ?   ?   A . n 
A 1 13  ASP 13  7   ?   ?   ?   A . n 
A 1 14  GLY 14  8   ?   ?   ?   A . n 
A 1 15  ASN 15  9   ?   ?   ?   A . n 
A 1 16  ASN 16  10  10  ASN ASN A . n 
A 1 17  PRO 17  11  11  PRO PRO A . n 
A 1 18  LEU 18  12  12  LEU LEU A . n 
A 1 19  PHE 19  13  13  PHE PHE A . n 
A 1 20  SER 20  14  14  SER SER A . n 
A 1 21  PRO 21  15  15  PRO PRO A . n 
A 1 22  TYR 22  16  16  TYR TYR A . n 
A 1 23  LYS 23  17  17  LYS LYS A . n 
A 1 24  MET 24  18  18  MET MET A . n 
A 1 25  GLY 25  19  19  GLY GLY A . n 
A 1 26  LYS 26  20  20  LYS LYS A . n 
A 1 27  PHE 27  21  21  PHE PHE A . n 
A 1 28  ASN 28  22  22  ASN ASN A . n 
A 1 29  LEU 29  23  23  LEU LEU A . n 
A 1 30  SER 30  24  24  SER SER A . n 
A 1 31  HIS 31  25  25  HIS HIS A . n 
A 1 32  ARG 32  26  26  ARG ARG A . n 
A 1 33  VAL 33  27  27  VAL VAL A . n 
A 1 34  VAL 34  28  28  VAL VAL A . n 
A 1 35  LEU 35  29  29  LEU LEU A . n 
A 1 36  ALA 36  30  30  ALA ALA A . n 
A 1 37  PRO 37  31  31  PRO PRO A . n 
A 1 38  MET 38  32  32  MET MET A . n 
A 1 39  THR 39  33  33  THR THR A . n 
A 1 40  ARG 40  34  34  ARG ARG A . n 
A 1 41  CYS 41  35  35  CYS CYS A . n 
A 1 42  ARG 42  36  36  ARG ARG A . n 
A 1 43  ALA 43  37  37  ALA ALA A . n 
A 1 44  LEU 44  38  38  LEU LEU A . n 
A 1 45  ASN 45  39  39  ASN ASN A . n 
A 1 46  ASN 46  40  40  ASN ASN A . n 
A 1 47  ILE 47  41  41  ILE ILE A . n 
A 1 48  PRO 48  42  42  PRO PRO A . n 
A 1 49  GLN 49  43  43  GLN GLN A . n 
A 1 50  ALA 50  44  44  ALA ALA A . n 
A 1 51  ALA 51  45  45  ALA ALA A . n 
A 1 52  LEU 52  46  46  LEU LEU A . n 
A 1 53  GLY 53  47  47  GLY GLY A . n 
A 1 54  GLU 54  48  48  GLU GLU A . n 
A 1 55  TYR 55  49  49  TYR TYR A . n 
A 1 56  TYR 56  50  50  TYR TYR A . n 
A 1 57  GLU 57  51  51  GLU GLU A . n 
A 1 58  GLN 58  52  52  GLN GLN A . n 
A 1 59  ARG 59  53  53  ARG ARG A . n 
A 1 60  ALA 60  54  54  ALA ALA A . n 
A 1 61  THR 61  55  55  THR THR A . n 
A 1 62  ALA 62  56  56  ALA ALA A . n 
A 1 63  GLY 63  57  57  GLY GLY A . n 
A 1 64  GLY 64  58  58  GLY GLY A . n 
A 1 65  PHE 65  59  59  PHE PHE A . n 
A 1 66  LEU 66  60  60  LEU LEU A . n 
A 1 67  ILE 67  61  61  ILE ILE A . n 
A 1 68  THR 68  62  62  THR THR A . n 
A 1 69  GLU 69  63  63  GLU GLU A . n 
A 1 70  GLY 70  64  64  GLY GLY A . n 
A 1 71  THR 71  65  65  THR THR A . n 
A 1 72  MET 72  66  66  MET MET A . n 
A 1 73  ILE 73  67  67  ILE ILE A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  PRO 75  69  69  PRO PRO A . n 
A 1 76  THR 76  70  70  THR THR A . n 
A 1 77  SER 77  71  71  SER SER A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  PHE 80  74  74  PHE PHE A . n 
A 1 81  PRO 81  75  75  PRO PRO A . n 
A 1 82  HIS 82  76  76  HIS HIS A . n 
A 1 83  VAL 83  77  77  VAL VAL A . n 
A 1 84  PRO 84  78  78  PRO PRO A . n 
A 1 85  GLY 85  79  79  GLY GLY A . n 
A 1 86  ILE 86  80  80  ILE ILE A . n 
A 1 87  PHE 87  81  81  PHE PHE A . n 
A 1 88  THR 88  82  82  THR THR A . n 
A 1 89  LYS 89  83  83  LYS LYS A . n 
A 1 90  GLU 90  84  84  GLU GLU A . n 
A 1 91  GLN 91  85  85  GLN GLN A . n 
A 1 92  VAL 92  86  86  VAL VAL A . n 
A 1 93  ARG 93  87  87  ARG ARG A . n 
A 1 94  GLU 94  88  88  GLU GLU A . n 
A 1 95  TRP 95  89  89  TRP TRP A . n 
A 1 96  LYS 96  90  90  LYS LYS A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  ILE 98  92  92  ILE ILE A . n 
A 1 99  VAL 99  93  93  VAL VAL A . n 
A 1 100 ASP 100 94  94  ASP ASP A . n 
A 1 101 VAL 101 95  95  VAL VAL A . n 
A 1 102 VAL 102 96  96  VAL VAL A . n 
A 1 103 HIS 103 97  97  HIS HIS A . n 
A 1 104 ALA 104 98  98  ALA ALA A . n 
A 1 105 LYS 105 99  99  LYS LYS A . n 
A 1 106 GLY 106 100 100 GLY GLY A . n 
A 1 107 ALA 107 101 101 ALA ALA A . n 
A 1 108 VAL 108 102 102 VAL VAL A . n 
A 1 109 ILE 109 103 103 ILE ILE A . n 
A 1 110 PHE 110 104 104 PHE PHE A . n 
A 1 111 CYS 111 105 105 CYS CYS A . n 
A 1 112 GLN 112 106 106 GLN GLN A . n 
A 1 113 LEU 113 107 107 LEU LEU A . n 
A 1 114 TRP 114 108 108 TRP TRP A . n 
A 1 115 HIS 115 109 109 HIS HIS A . n 
A 1 116 VAL 116 110 110 VAL VAL A . n 
A 1 117 GLY 117 111 111 GLY GLY A . n 
A 1 118 ARG 118 112 112 ARG ARG A . n 
A 1 119 ALA 119 113 113 ALA ALA A . n 
A 1 120 SER 120 114 114 SER SER A . n 
A 1 121 HIS 121 115 115 HIS HIS A . n 
A 1 122 GLU 122 116 116 GLU GLU A . n 
A 1 123 VAL 123 117 117 VAL VAL A . n 
A 1 124 TYR 124 118 118 TYR TYR A . n 
A 1 125 GLN 125 119 119 GLN GLN A . n 
A 1 126 PRO 126 120 120 PRO PRO A . n 
A 1 127 ALA 127 121 121 ALA ALA A . n 
A 1 128 GLY 128 122 122 GLY GLY A . n 
A 1 129 ALA 129 123 123 ALA ALA A . n 
A 1 130 ALA 130 124 124 ALA ALA A . n 
A 1 131 PRO 131 125 125 PRO PRO A . n 
A 1 132 ILE 132 126 126 ILE ILE A . n 
A 1 133 SER 133 127 127 SER SER A . n 
A 1 134 SER 134 128 128 SER SER A . n 
A 1 135 THR 135 129 129 THR THR A . n 
A 1 136 GLU 136 130 130 GLU GLU A . n 
A 1 137 LYS 137 131 131 LYS LYS A . n 
A 1 138 PRO 138 132 132 PRO PRO A . n 
A 1 139 ILE 139 133 133 ILE ILE A . n 
A 1 140 SER 140 134 134 SER SER A . n 
A 1 141 ASN 141 135 135 ASN ASN A . n 
A 1 142 ARG 142 136 136 ARG ARG A . n 
A 1 143 TRP 143 137 137 TRP TRP A . n 
A 1 144 ARG 144 138 138 ARG ARG A . n 
A 1 145 ILE 145 139 139 ILE ILE A . n 
A 1 146 LEU 146 140 140 LEU LEU A . n 
A 1 147 MET 147 141 141 MET MET A . n 
A 1 148 PRO 148 142 142 PRO PRO A . n 
A 1 149 ASP 149 143 143 ASP ASP A . n 
A 1 150 GLY 150 144 144 GLY GLY A . n 
A 1 151 THR 151 145 145 THR THR A . n 
A 1 152 HIS 152 146 146 HIS HIS A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 ILE 154 148 148 ILE ILE A . n 
A 1 155 TYR 155 149 149 TYR TYR A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 LYS 157 151 151 LYS LYS A . n 
A 1 158 PRO 158 152 152 PRO PRO A . n 
A 1 159 ARG 159 153 153 ARG ARG A . n 
A 1 160 ALA 160 154 154 ALA ALA A . n 
A 1 161 ILE 161 155 155 ILE ILE A . n 
A 1 162 GLY 162 156 156 GLY GLY A . n 
A 1 163 THR 163 157 157 THR THR A . n 
A 1 164 TYR 164 158 158 TYR TYR A . n 
A 1 165 GLU 165 159 159 GLU GLU A . n 
A 1 166 ILE 166 160 160 ILE ILE A . n 
A 1 167 SER 167 161 161 SER SER A . n 
A 1 168 GLN 168 162 162 GLN GLN A . n 
A 1 169 VAL 169 163 163 VAL VAL A . n 
A 1 170 VAL 170 164 164 VAL VAL A . n 
A 1 171 GLU 171 165 165 GLU GLU A . n 
A 1 172 ASP 172 166 166 ASP ASP A . n 
A 1 173 TYR 173 167 167 TYR TYR A . n 
A 1 174 ARG 174 168 168 ARG ARG A . n 
A 1 175 ARG 175 169 169 ARG ARG A . n 
A 1 176 SER 176 170 170 SER SER A . n 
A 1 177 ALA 177 171 171 ALA ALA A . n 
A 1 178 LEU 178 172 172 LEU LEU A . n 
A 1 179 ASN 179 173 173 ASN ASN A . n 
A 1 180 ALA 180 174 174 ALA ALA A . n 
A 1 181 ILE 181 175 175 ILE ILE A . n 
A 1 182 GLU 182 176 176 GLU GLU A . n 
A 1 183 ALA 183 177 177 ALA ALA A . n 
A 1 184 GLY 184 178 178 GLY GLY A . n 
A 1 185 PHE 185 179 179 PHE PHE A . n 
A 1 186 ASP 186 180 180 ASP ASP A . n 
A 1 187 GLY 187 181 181 GLY GLY A . n 
A 1 188 ILE 188 182 182 ILE ILE A . n 
A 1 189 GLU 189 183 183 GLU GLU A . n 
A 1 190 ILE 190 184 184 ILE ILE A . n 
A 1 191 HIS 191 185 185 HIS HIS A . n 
A 1 192 GLY 192 186 186 GLY GLY A . n 
A 1 193 ALA 193 187 187 ALA ALA A . n 
A 1 194 HIS 194 188 188 HIS HIS A . n 
A 1 195 GLY 195 189 189 GLY GLY A . n 
A 1 196 TYR 196 190 190 TYR TYR A . n 
A 1 197 LEU 197 191 191 LEU LEU A . n 
A 1 198 ILE 198 192 192 ILE ILE A . n 
A 1 199 ASP 199 193 193 ASP ASP A . n 
A 1 200 GLN 200 194 194 GLN GLN A . n 
A 1 201 PHE 201 195 195 PHE PHE A . n 
A 1 202 LEU 202 196 196 LEU LEU A . n 
A 1 203 LYS 203 197 197 LYS LYS A . n 
A 1 204 ASP 204 198 198 ASP ASP A . n 
A 1 205 GLY 205 199 199 GLY GLY A . n 
A 1 206 ILE 206 200 200 ILE ILE A . n 
A 1 207 ASN 207 201 201 ASN ASN A . n 
A 1 208 ASP 208 202 202 ASP ASP A . n 
A 1 209 ARG 209 203 203 ARG ARG A . n 
A 1 210 THR 210 204 204 THR THR A . n 
A 1 211 ASP 211 205 205 ASP ASP A . n 
A 1 212 GLU 212 206 206 GLU GLU A . n 
A 1 213 TYR 213 207 207 TYR TYR A . n 
A 1 214 GLY 214 208 208 GLY GLY A . n 
A 1 215 GLY 215 209 209 GLY GLY A . n 
A 1 216 SER 216 210 210 SER SER A . n 
A 1 217 LEU 217 211 211 LEU LEU A . n 
A 1 218 ALA 218 212 212 ALA ALA A . n 
A 1 219 ASN 219 213 213 ASN ASN A . n 
A 1 220 ARG 220 214 214 ARG ARG A . n 
A 1 221 CYS 221 215 215 CYS CYS A . n 
A 1 222 LYS 222 216 216 LYS LYS A . n 
A 1 223 PHE 223 217 217 PHE PHE A . n 
A 1 224 ILE 224 218 218 ILE ILE A . n 
A 1 225 THR 225 219 219 THR THR A . n 
A 1 226 GLN 226 220 220 GLN GLN A . n 
A 1 227 VAL 227 221 221 VAL VAL A . n 
A 1 228 VAL 228 222 222 VAL VAL A . n 
A 1 229 GLN 229 223 223 GLN GLN A . n 
A 1 230 ALA 230 224 224 ALA ALA A . n 
A 1 231 VAL 231 225 225 VAL VAL A . n 
A 1 232 VAL 232 226 226 VAL VAL A . n 
A 1 233 SER 233 227 227 SER SER A . n 
A 1 234 ALA 234 228 228 ALA ALA A . n 
A 1 235 ILE 235 229 229 ILE ILE A . n 
A 1 236 GLY 236 230 230 GLY GLY A . n 
A 1 237 ALA 237 231 231 ALA ALA A . n 
A 1 238 ASP 238 232 232 ASP ASP A . n 
A 1 239 ARG 239 233 233 ARG ARG A . n 
A 1 240 VAL 240 234 234 VAL VAL A . n 
A 1 241 GLY 241 235 235 GLY GLY A . n 
A 1 242 VAL 242 236 236 VAL VAL A . n 
A 1 243 ARG 243 237 237 ARG ARG A . n 
A 1 244 VAL 244 238 238 VAL VAL A . n 
A 1 245 SER 245 239 239 SER SER A . n 
A 1 246 PRO 246 240 240 PRO PRO A . n 
A 1 247 ALA 247 241 241 ALA ALA A . n 
A 1 248 ILE 248 242 242 ILE ILE A . n 
A 1 249 ASP 249 243 243 ASP ASP A . n 
A 1 250 HIS 250 244 244 HIS HIS A . n 
A 1 251 LEU 251 245 245 LEU LEU A . n 
A 1 252 ASP 252 246 246 ASP ASP A . n 
A 1 253 ALA 253 247 247 ALA ALA A . n 
A 1 254 MET 254 248 248 MET MET A . n 
A 1 255 ASP 255 249 249 ASP ASP A . n 
A 1 256 SER 256 250 250 SER SER A . n 
A 1 257 ASN 257 251 251 ASN ASN A . n 
A 1 258 PRO 258 252 252 PRO PRO A . n 
A 1 259 LEU 259 253 253 LEU LEU A . n 
A 1 260 SER 260 254 254 SER SER A . n 
A 1 261 LEU 261 255 255 LEU LEU A . n 
A 1 262 GLY 262 256 256 GLY GLY A . n 
A 1 263 LEU 263 257 257 LEU LEU A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 VAL 265 259 259 VAL VAL A . n 
A 1 266 VAL 266 260 260 VAL VAL A . n 
A 1 267 GLU 267 261 261 GLU GLU A . n 
A 1 268 ARG 268 262 262 ARG ARG A . n 
A 1 269 LEU 269 263 263 LEU LEU A . n 
A 1 270 ASN 270 264 264 ASN ASN A . n 
A 1 271 LYS 271 265 265 LYS LYS A . n 
A 1 272 ILE 272 266 266 ILE ILE A . n 
A 1 273 GLN 273 267 267 GLN GLN A . n 
A 1 274 LEU 274 268 268 LEU LEU A . n 
A 1 275 HIS 275 269 269 HIS HIS A . n 
A 1 276 SER 276 270 270 SER SER A . n 
A 1 277 GLY 277 271 271 GLY GLY A . n 
A 1 278 SER 278 272 272 SER SER A . n 
A 1 279 LYS 279 273 273 LYS LYS A . n 
A 1 280 LEU 280 274 274 LEU LEU A . n 
A 1 281 ALA 281 275 275 ALA ALA A . n 
A 1 282 TYR 282 276 276 TYR TYR A . n 
A 1 283 LEU 283 277 277 LEU LEU A . n 
A 1 284 HIS 284 278 278 HIS HIS A . n 
A 1 285 VAL 285 279 279 VAL VAL A . n 
A 1 286 THR 286 280 280 THR THR A . n 
A 1 287 GLN 287 281 281 GLN GLN A . n 
A 1 288 PRO 288 282 282 PRO PRO A . n 
A 1 289 GLU 289 283 ?   ?   ?   A . n 
A 1 290 TYR 290 284 ?   ?   ?   A . n 
A 1 291 VAL 291 285 ?   ?   ?   A . n 
A 1 292 ALA 292 286 ?   ?   ?   A . n 
A 1 293 TYR 293 287 ?   ?   ?   A . n 
A 1 294 GLY 294 288 ?   ?   ?   A . n 
A 1 295 GLN 295 289 ?   ?   ?   A . n 
A 1 296 THR 296 290 ?   ?   ?   A . n 
A 1 297 GLU 297 291 ?   ?   ?   A . n 
A 1 298 ALA 298 292 ?   ?   ?   A . n 
A 1 299 GLY 299 293 ?   ?   ?   A . n 
A 1 300 ARG 300 294 ?   ?   ?   A . n 
A 1 301 LEU 301 295 ?   ?   ?   A . n 
A 1 302 GLY 302 296 ?   ?   ?   A . n 
A 1 303 SER 303 297 ?   ?   ?   A . n 
A 1 304 GLU 304 298 ?   ?   ?   A . n 
A 1 305 GLU 305 299 ?   ?   ?   A . n 
A 1 306 GLU 306 300 ?   ?   ?   A . n 
A 1 307 GLU 307 301 ?   ?   ?   A . n 
A 1 308 ALA 308 302 ?   ?   ?   A . n 
A 1 309 ARG 309 303 303 ARG ARG A . n 
A 1 310 LEU 310 304 304 LEU LEU A . n 
A 1 311 MET 311 305 305 MET MET A . n 
A 1 312 ARG 312 306 306 ARG ARG A . n 
A 1 313 THR 313 307 307 THR THR A . n 
A 1 314 LEU 314 308 308 LEU LEU A . n 
A 1 315 ARG 315 309 309 ARG ARG A . n 
A 1 316 ASN 316 310 310 ASN ASN A . n 
A 1 317 ALA 317 311 311 ALA ALA A . n 
A 1 318 TYR 318 312 312 TYR TYR A . n 
A 1 319 GLN 319 313 313 GLN GLN A . n 
A 1 320 GLY 320 314 314 GLY GLY A . n 
A 1 321 THR 321 315 315 THR THR A . n 
A 1 322 PHE 322 316 316 PHE PHE A . n 
A 1 323 ILE 323 317 317 ILE ILE A . n 
A 1 324 CYS 324 318 318 CYS CYS A . n 
A 1 325 SER 325 319 319 SER SER A . n 
A 1 326 GLY 326 320 320 GLY GLY A . n 
A 1 327 GLY 327 321 321 GLY GLY A . n 
A 1 328 TYR 328 322 322 TYR TYR A . n 
A 1 329 THR 329 323 323 THR THR A . n 
A 1 330 ARG 330 324 324 ARG ARG A . n 
A 1 331 GLU 331 325 325 GLU GLU A . n 
A 1 332 LEU 332 326 326 LEU LEU A . n 
A 1 333 GLY 333 327 327 GLY GLY A . n 
A 1 334 ILE 334 328 328 ILE ILE A . n 
A 1 335 GLU 335 329 329 GLU GLU A . n 
A 1 336 ALA 336 330 330 ALA ALA A . n 
A 1 337 VAL 337 331 331 VAL VAL A . n 
A 1 338 ALA 338 332 332 ALA ALA A . n 
A 1 339 GLN 339 333 333 GLN GLN A . n 
A 1 340 GLY 340 334 334 GLY GLY A . n 
A 1 341 ASP 341 335 335 ASP ASP A . n 
A 1 342 ALA 342 336 336 ALA ALA A . n 
A 1 343 ASP 343 337 337 ASP ASP A . n 
A 1 344 LEU 344 338 338 LEU LEU A . n 
A 1 345 VAL 345 339 339 VAL VAL A . n 
A 1 346 SER 346 340 340 SER SER A . n 
A 1 347 TYR 347 341 341 TYR TYR A . n 
A 1 348 GLY 348 342 342 GLY GLY A . n 
A 1 349 ARG 349 343 343 ARG ARG A . n 
A 1 350 LEU 350 344 344 LEU LEU A . n 
A 1 351 PHE 351 345 345 PHE PHE A . n 
A 1 352 ILE 352 346 346 ILE ILE A . n 
A 1 353 SER 353 347 347 SER SER A . n 
A 1 354 ASN 354 348 348 ASN ASN A . n 
A 1 355 PRO 355 349 349 PRO PRO A . n 
A 1 356 ASP 356 350 350 ASP ASP A . n 
A 1 357 LEU 357 351 351 LEU LEU A . n 
A 1 358 VAL 358 352 352 VAL VAL A . n 
A 1 359 MET 359 353 353 MET MET A . n 
A 1 360 ARG 360 354 354 ARG ARG A . n 
A 1 361 ILE 361 355 355 ILE ILE A . n 
A 1 362 LYS 362 356 356 LYS LYS A . n 
A 1 363 LEU 363 357 357 LEU LEU A . n 
A 1 364 ASN 364 358 358 ASN ASN A . n 
A 1 365 ALA 365 359 359 ALA ALA A . n 
A 1 366 PRO 366 360 360 PRO PRO A . n 
A 1 367 LEU 367 361 361 LEU LEU A . n 
A 1 368 ASN 368 362 362 ASN ASN A . n 
A 1 369 LYS 369 363 363 LYS LYS A . n 
A 1 370 TYR 370 364 364 TYR TYR A . n 
A 1 371 ASN 371 365 365 ASN ASN A . n 
A 1 372 ARG 372 366 366 ARG ARG A . n 
A 1 373 LYS 373 367 367 LYS LYS A . n 
A 1 374 THR 374 368 368 THR THR A . n 
A 1 375 PHE 375 369 369 PHE PHE A . n 
A 1 376 TYR 376 370 370 TYR TYR A . n 
A 1 377 THR 377 371 371 THR THR A . n 
A 1 378 GLN 378 372 372 GLN GLN A . n 
A 1 379 ASP 379 373 373 ASP ASP A . n 
A 1 380 PRO 380 374 374 PRO PRO A . n 
A 1 381 VAL 381 375 375 VAL VAL A . n 
A 1 382 VAL 382 376 376 VAL VAL A . n 
A 1 383 GLY 383 377 377 GLY GLY A . n 
A 1 384 TYR 384 378 378 TYR TYR A . n 
A 1 385 THR 385 379 379 THR THR A . n 
A 1 386 ASP 386 380 380 ASP ASP A . n 
A 1 387 TYR 387 381 381 TYR TYR A . n 
A 1 388 PRO 388 382 382 PRO PRO A . n 
A 1 389 PHE 389 383 383 PHE PHE A . n 
A 1 390 LEU 390 384 384 LEU LEU A . n 
A 1 391 GLN 391 385 ?   ?   ?   A . n 
A 1 392 GLY 392 386 ?   ?   ?   A . n 
A 1 393 ASN 393 387 ?   ?   ?   A . n 
A 1 394 GLY 394 388 ?   ?   ?   A . n 
A 1 395 SER 395 389 ?   ?   ?   A . n 
A 1 396 ASN 396 390 ?   ?   ?   A . n 
A 1 397 GLY 397 391 ?   ?   ?   A . n 
A 1 398 PRO 398 392 ?   ?   ?   A . n 
A 1 399 LEU 399 393 ?   ?   ?   A . n 
A 1 400 SER 400 394 ?   ?   ?   A . n 
A 1 401 ARG 401 395 ?   ?   ?   A . n 
A 1 402 LEU 402 396 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5J8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5J8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1   401  395 FMN FMN A . 
C 3 5J8 1   402  396 5J8 5J8 A . 
D 3 5J8 1   403  397 5J8 5J8 A . 
E 4 SO4 1   404  398 SO4 SO4 A . 
F 5 HOH 1   501  368 HOH HOH A . 
F 5 HOH 2   502  394 HOH HOH A . 
F 5 HOH 3   503  264 HOH HOH A . 
F 5 HOH 4   504  231 HOH HOH A . 
F 5 HOH 5   505  451 HOH HOH A . 
F 5 HOH 6   506  315 HOH HOH A . 
F 5 HOH 7   507  442 HOH HOH A . 
F 5 HOH 8   508  183 HOH HOH A . 
F 5 HOH 9   509  454 HOH HOH A . 
F 5 HOH 10  510  106 HOH HOH A . 
F 5 HOH 11  511  395 HOH HOH A . 
F 5 HOH 12  512  281 HOH HOH A . 
F 5 HOH 13  513  206 HOH HOH A . 
F 5 HOH 14  514  429 HOH HOH A . 
F 5 HOH 15  515  333 HOH HOH A . 
F 5 HOH 16  516  261 HOH HOH A . 
F 5 HOH 17  517  401 HOH HOH A . 
F 5 HOH 18  518  254 HOH HOH A . 
F 5 HOH 19  519  330 HOH HOH A . 
F 5 HOH 20  520  373 HOH HOH A . 
F 5 HOH 21  521  299 HOH HOH A . 
F 5 HOH 22  522  111 HOH HOH A . 
F 5 HOH 23  523  266 HOH HOH A . 
F 5 HOH 24  524  349 HOH HOH A . 
F 5 HOH 25  525  142 HOH HOH A . 
F 5 HOH 26  526  270 HOH HOH A . 
F 5 HOH 27  527  59  HOH HOH A . 
F 5 HOH 28  528  487 HOH HOH A . 
F 5 HOH 29  529  525 HOH HOH A . 
F 5 HOH 30  530  196 HOH HOH A . 
F 5 HOH 31  531  265 HOH HOH A . 
F 5 HOH 32  532  82  HOH HOH A . 
F 5 HOH 33  533  73  HOH HOH A . 
F 5 HOH 34  534  198 HOH HOH A . 
F 5 HOH 35  535  494 HOH HOH A . 
F 5 HOH 36  536  269 HOH HOH A . 
F 5 HOH 37  537  147 HOH HOH A . 
F 5 HOH 38  538  323 HOH HOH A . 
F 5 HOH 39  539  235 HOH HOH A . 
F 5 HOH 40  540  302 HOH HOH A . 
F 5 HOH 41  541  448 HOH HOH A . 
F 5 HOH 42  542  243 HOH HOH A . 
F 5 HOH 43  543  69  HOH HOH A . 
F 5 HOH 44  544  58  HOH HOH A . 
F 5 HOH 45  545  223 HOH HOH A . 
F 5 HOH 46  546  156 HOH HOH A . 
F 5 HOH 47  547  31  HOH HOH A . 
F 5 HOH 48  548  64  HOH HOH A . 
F 5 HOH 49  549  340 HOH HOH A . 
F 5 HOH 50  550  141 HOH HOH A . 
F 5 HOH 51  551  163 HOH HOH A . 
F 5 HOH 52  552  185 HOH HOH A . 
F 5 HOH 53  553  20  HOH HOH A . 
F 5 HOH 54  554  202 HOH HOH A . 
F 5 HOH 55  555  178 HOH HOH A . 
F 5 HOH 56  556  280 HOH HOH A . 
F 5 HOH 57  557  201 HOH HOH A . 
F 5 HOH 58  558  157 HOH HOH A . 
F 5 HOH 59  559  118 HOH HOH A . 
F 5 HOH 60  560  189 HOH HOH A . 
F 5 HOH 61  561  336 HOH HOH A . 
F 5 HOH 62  562  62  HOH HOH A . 
F 5 HOH 63  563  123 HOH HOH A . 
F 5 HOH 64  564  470 HOH HOH A . 
F 5 HOH 65  565  170 HOH HOH A . 
F 5 HOH 66  566  40  HOH HOH A . 
F 5 HOH 67  567  376 HOH HOH A . 
F 5 HOH 68  568  109 HOH HOH A . 
F 5 HOH 69  569  80  HOH HOH A . 
F 5 HOH 70  570  47  HOH HOH A . 
F 5 HOH 71  571  121 HOH HOH A . 
F 5 HOH 72  572  390 HOH HOH A . 
F 5 HOH 73  573  26  HOH HOH A . 
F 5 HOH 74  574  30  HOH HOH A . 
F 5 HOH 75  575  277 HOH HOH A . 
F 5 HOH 76  576  51  HOH HOH A . 
F 5 HOH 77  577  63  HOH HOH A . 
F 5 HOH 78  578  112 HOH HOH A . 
F 5 HOH 79  579  84  HOH HOH A . 
F 5 HOH 80  580  41  HOH HOH A . 
F 5 HOH 81  581  197 HOH HOH A . 
F 5 HOH 82  582  24  HOH HOH A . 
F 5 HOH 83  583  2   HOH HOH A . 
F 5 HOH 84  584  86  HOH HOH A . 
F 5 HOH 85  585  68  HOH HOH A . 
F 5 HOH 86  586  77  HOH HOH A . 
F 5 HOH 87  587  290 HOH HOH A . 
F 5 HOH 88  588  87  HOH HOH A . 
F 5 HOH 89  589  53  HOH HOH A . 
F 5 HOH 90  590  126 HOH HOH A . 
F 5 HOH 91  591  27  HOH HOH A . 
F 5 HOH 92  592  39  HOH HOH A . 
F 5 HOH 93  593  374 HOH HOH A . 
F 5 HOH 94  594  355 HOH HOH A . 
F 5 HOH 95  595  160 HOH HOH A . 
F 5 HOH 96  596  207 HOH HOH A . 
F 5 HOH 97  597  335 HOH HOH A . 
F 5 HOH 98  598  303 HOH HOH A . 
F 5 HOH 99  599  337 HOH HOH A . 
F 5 HOH 100 600  237 HOH HOH A . 
F 5 HOH 101 601  89  HOH HOH A . 
F 5 HOH 102 602  28  HOH HOH A . 
F 5 HOH 103 603  98  HOH HOH A . 
F 5 HOH 104 604  289 HOH HOH A . 
F 5 HOH 105 605  1   HOH HOH A . 
F 5 HOH 106 606  5   HOH HOH A . 
F 5 HOH 107 607  101 HOH HOH A . 
F 5 HOH 108 608  57  HOH HOH A . 
F 5 HOH 109 609  144 HOH HOH A . 
F 5 HOH 110 610  205 HOH HOH A . 
F 5 HOH 111 611  21  HOH HOH A . 
F 5 HOH 112 612  48  HOH HOH A . 
F 5 HOH 113 613  94  HOH HOH A . 
F 5 HOH 114 614  15  HOH HOH A . 
F 5 HOH 115 615  34  HOH HOH A . 
F 5 HOH 116 616  17  HOH HOH A . 
F 5 HOH 117 617  233 HOH HOH A . 
F 5 HOH 118 618  90  HOH HOH A . 
F 5 HOH 119 619  175 HOH HOH A . 
F 5 HOH 120 620  61  HOH HOH A . 
F 5 HOH 121 621  476 HOH HOH A . 
F 5 HOH 122 622  257 HOH HOH A . 
F 5 HOH 123 623  298 HOH HOH A . 
F 5 HOH 124 624  66  HOH HOH A . 
F 5 HOH 125 625  164 HOH HOH A . 
F 5 HOH 126 626  83  HOH HOH A . 
F 5 HOH 127 627  391 HOH HOH A . 
F 5 HOH 128 628  523 HOH HOH A . 
F 5 HOH 129 629  113 HOH HOH A . 
F 5 HOH 130 630  245 HOH HOH A . 
F 5 HOH 131 631  475 HOH HOH A . 
F 5 HOH 132 632  88  HOH HOH A . 
F 5 HOH 133 633  224 HOH HOH A . 
F 5 HOH 134 634  173 HOH HOH A . 
F 5 HOH 135 635  318 HOH HOH A . 
F 5 HOH 136 636  6   HOH HOH A . 
F 5 HOH 137 637  345 HOH HOH A . 
F 5 HOH 138 638  380 HOH HOH A . 
F 5 HOH 139 639  149 HOH HOH A . 
F 5 HOH 140 640  411 HOH HOH A . 
F 5 HOH 141 641  50  HOH HOH A . 
F 5 HOH 142 642  65  HOH HOH A . 
F 5 HOH 143 643  23  HOH HOH A . 
F 5 HOH 144 644  191 HOH HOH A . 
F 5 HOH 145 645  493 HOH HOH A . 
F 5 HOH 146 646  8   HOH HOH A . 
F 5 HOH 147 647  213 HOH HOH A . 
F 5 HOH 148 648  361 HOH HOH A . 
F 5 HOH 149 649  114 HOH HOH A . 
F 5 HOH 150 650  537 HOH HOH A . 
F 5 HOH 151 651  396 HOH HOH A . 
F 5 HOH 152 652  35  HOH HOH A . 
F 5 HOH 153 653  533 HOH HOH A . 
F 5 HOH 154 654  325 HOH HOH A . 
F 5 HOH 155 655  33  HOH HOH A . 
F 5 HOH 156 656  71  HOH HOH A . 
F 5 HOH 157 657  22  HOH HOH A . 
F 5 HOH 158 658  332 HOH HOH A . 
F 5 HOH 159 659  313 HOH HOH A . 
F 5 HOH 160 660  432 HOH HOH A . 
F 5 HOH 161 661  287 HOH HOH A . 
F 5 HOH 162 662  13  HOH HOH A . 
F 5 HOH 163 663  137 HOH HOH A . 
F 5 HOH 164 664  19  HOH HOH A . 
F 5 HOH 165 665  535 HOH HOH A . 
F 5 HOH 166 666  55  HOH HOH A . 
F 5 HOH 167 667  219 HOH HOH A . 
F 5 HOH 168 668  291 HOH HOH A . 
F 5 HOH 169 669  49  HOH HOH A . 
F 5 HOH 170 670  12  HOH HOH A . 
F 5 HOH 171 671  271 HOH HOH A . 
F 5 HOH 172 672  457 HOH HOH A . 
F 5 HOH 173 673  294 HOH HOH A . 
F 5 HOH 174 674  119 HOH HOH A . 
F 5 HOH 175 675  42  HOH HOH A . 
F 5 HOH 176 676  212 HOH HOH A . 
F 5 HOH 177 677  67  HOH HOH A . 
F 5 HOH 178 678  346 HOH HOH A . 
F 5 HOH 179 679  54  HOH HOH A . 
F 5 HOH 180 680  75  HOH HOH A . 
F 5 HOH 181 681  85  HOH HOH A . 
F 5 HOH 182 682  412 HOH HOH A . 
F 5 HOH 183 683  174 HOH HOH A . 
F 5 HOH 184 684  259 HOH HOH A . 
F 5 HOH 185 685  96  HOH HOH A . 
F 5 HOH 186 686  122 HOH HOH A . 
F 5 HOH 187 687  134 HOH HOH A . 
F 5 HOH 188 688  214 HOH HOH A . 
F 5 HOH 189 689  116 HOH HOH A . 
F 5 HOH 190 690  276 HOH HOH A . 
F 5 HOH 191 691  492 HOH HOH A . 
F 5 HOH 192 692  192 HOH HOH A . 
F 5 HOH 193 693  3   HOH HOH A . 
F 5 HOH 194 694  138 HOH HOH A . 
F 5 HOH 195 695  329 HOH HOH A . 
F 5 HOH 196 696  70  HOH HOH A . 
F 5 HOH 197 697  44  HOH HOH A . 
F 5 HOH 198 698  440 HOH HOH A . 
F 5 HOH 199 699  450 HOH HOH A . 
F 5 HOH 200 700  320 HOH HOH A . 
F 5 HOH 201 701  167 HOH HOH A . 
F 5 HOH 202 702  288 HOH HOH A . 
F 5 HOH 203 703  151 HOH HOH A . 
F 5 HOH 204 704  46  HOH HOH A . 
F 5 HOH 205 705  152 HOH HOH A . 
F 5 HOH 206 706  426 HOH HOH A . 
F 5 HOH 207 707  60  HOH HOH A . 
F 5 HOH 208 708  497 HOH HOH A . 
F 5 HOH 209 709  222 HOH HOH A . 
F 5 HOH 210 710  389 HOH HOH A . 
F 5 HOH 211 711  247 HOH HOH A . 
F 5 HOH 212 712  199 HOH HOH A . 
F 5 HOH 213 713  443 HOH HOH A . 
F 5 HOH 214 714  143 HOH HOH A . 
F 5 HOH 215 715  232 HOH HOH A . 
F 5 HOH 216 716  125 HOH HOH A . 
F 5 HOH 217 717  18  HOH HOH A . 
F 5 HOH 218 718  91  HOH HOH A . 
F 5 HOH 219 719  162 HOH HOH A . 
F 5 HOH 220 720  103 HOH HOH A . 
F 5 HOH 221 721  14  HOH HOH A . 
F 5 HOH 222 722  255 HOH HOH A . 
F 5 HOH 223 723  530 HOH HOH A . 
F 5 HOH 224 724  518 HOH HOH A . 
F 5 HOH 225 725  32  HOH HOH A . 
F 5 HOH 226 726  407 HOH HOH A . 
F 5 HOH 227 727  9   HOH HOH A . 
F 5 HOH 228 728  204 HOH HOH A . 
F 5 HOH 229 729  74  HOH HOH A . 
F 5 HOH 230 730  25  HOH HOH A . 
F 5 HOH 231 731  234 HOH HOH A . 
F 5 HOH 232 732  301 HOH HOH A . 
F 5 HOH 233 733  150 HOH HOH A . 
F 5 HOH 234 734  108 HOH HOH A . 
F 5 HOH 235 735  38  HOH HOH A . 
F 5 HOH 236 736  248 HOH HOH A . 
F 5 HOH 237 737  358 HOH HOH A . 
F 5 HOH 238 738  16  HOH HOH A . 
F 5 HOH 239 739  455 HOH HOH A . 
F 5 HOH 240 740  4   HOH HOH A . 
F 5 HOH 241 741  458 HOH HOH A . 
F 5 HOH 242 742  418 HOH HOH A . 
F 5 HOH 243 743  176 HOH HOH A . 
F 5 HOH 244 744  159 HOH HOH A . 
F 5 HOH 245 745  504 HOH HOH A . 
F 5 HOH 246 746  273 HOH HOH A . 
F 5 HOH 247 747  321 HOH HOH A . 
F 5 HOH 248 748  11  HOH HOH A . 
F 5 HOH 249 749  7   HOH HOH A . 
F 5 HOH 250 750  260 HOH HOH A . 
F 5 HOH 251 751  424 HOH HOH A . 
F 5 HOH 252 752  139 HOH HOH A . 
F 5 HOH 253 753  79  HOH HOH A . 
F 5 HOH 254 754  148 HOH HOH A . 
F 5 HOH 255 755  227 HOH HOH A . 
F 5 HOH 256 756  381 HOH HOH A . 
F 5 HOH 257 757  221 HOH HOH A . 
F 5 HOH 258 758  484 HOH HOH A . 
F 5 HOH 259 759  120 HOH HOH A . 
F 5 HOH 260 760  10  HOH HOH A . 
F 5 HOH 261 761  510 HOH HOH A . 
F 5 HOH 262 762  256 HOH HOH A . 
F 5 HOH 263 763  184 HOH HOH A . 
F 5 HOH 264 764  344 HOH HOH A . 
F 5 HOH 265 765  56  HOH HOH A . 
F 5 HOH 266 766  166 HOH HOH A . 
F 5 HOH 267 767  43  HOH HOH A . 
F 5 HOH 268 768  350 HOH HOH A . 
F 5 HOH 269 769  342 HOH HOH A . 
F 5 HOH 270 770  107 HOH HOH A . 
F 5 HOH 271 771  509 HOH HOH A . 
F 5 HOH 272 772  145 HOH HOH A . 
F 5 HOH 273 773  217 HOH HOH A . 
F 5 HOH 274 774  129 HOH HOH A . 
F 5 HOH 275 775  421 HOH HOH A . 
F 5 HOH 276 776  37  HOH HOH A . 
F 5 HOH 277 777  117 HOH HOH A . 
F 5 HOH 278 778  128 HOH HOH A . 
F 5 HOH 279 779  72  HOH HOH A . 
F 5 HOH 280 780  97  HOH HOH A . 
F 5 HOH 281 781  155 HOH HOH A . 
F 5 HOH 282 782  534 HOH HOH A . 
F 5 HOH 283 783  105 HOH HOH A . 
F 5 HOH 284 784  78  HOH HOH A . 
F 5 HOH 285 785  352 HOH HOH A . 
F 5 HOH 286 786  305 HOH HOH A . 
F 5 HOH 287 787  226 HOH HOH A . 
F 5 HOH 288 788  309 HOH HOH A . 
F 5 HOH 289 789  135 HOH HOH A . 
F 5 HOH 290 790  215 HOH HOH A . 
F 5 HOH 291 791  29  HOH HOH A . 
F 5 HOH 292 792  100 HOH HOH A . 
F 5 HOH 293 793  172 HOH HOH A . 
F 5 HOH 294 794  310 HOH HOH A . 
F 5 HOH 295 795  36  HOH HOH A . 
F 5 HOH 296 796  52  HOH HOH A . 
F 5 HOH 297 797  403 HOH HOH A . 
F 5 HOH 298 798  536 HOH HOH A . 
F 5 HOH 299 799  386 HOH HOH A . 
F 5 HOH 300 800  370 HOH HOH A . 
F 5 HOH 301 801  102 HOH HOH A . 
F 5 HOH 302 802  251 HOH HOH A . 
F 5 HOH 303 803  193 HOH HOH A . 
F 5 HOH 304 804  104 HOH HOH A . 
F 5 HOH 305 805  133 HOH HOH A . 
F 5 HOH 306 806  124 HOH HOH A . 
F 5 HOH 307 807  327 HOH HOH A . 
F 5 HOH 308 808  186 HOH HOH A . 
F 5 HOH 309 809  195 HOH HOH A . 
F 5 HOH 310 810  486 HOH HOH A . 
F 5 HOH 311 811  93  HOH HOH A . 
F 5 HOH 312 812  304 HOH HOH A . 
F 5 HOH 313 813  154 HOH HOH A . 
F 5 HOH 314 814  218 HOH HOH A . 
F 5 HOH 315 815  158 HOH HOH A . 
F 5 HOH 316 816  200 HOH HOH A . 
F 5 HOH 317 817  99  HOH HOH A . 
F 5 HOH 318 818  279 HOH HOH A . 
F 5 HOH 319 819  495 HOH HOH A . 
F 5 HOH 320 820  307 HOH HOH A . 
F 5 HOH 321 821  131 HOH HOH A . 
F 5 HOH 322 822  507 HOH HOH A . 
F 5 HOH 323 823  308 HOH HOH A . 
F 5 HOH 324 824  398 HOH HOH A . 
F 5 HOH 325 825  187 HOH HOH A . 
F 5 HOH 326 826  244 HOH HOH A . 
F 5 HOH 327 827  110 HOH HOH A . 
F 5 HOH 328 828  363 HOH HOH A . 
F 5 HOH 329 829  249 HOH HOH A . 
F 5 HOH 330 830  95  HOH HOH A . 
F 5 HOH 331 831  441 HOH HOH A . 
F 5 HOH 332 832  339 HOH HOH A . 
F 5 HOH 333 833  274 HOH HOH A . 
F 5 HOH 334 834  462 HOH HOH A . 
F 5 HOH 335 835  366 HOH HOH A . 
F 5 HOH 336 836  246 HOH HOH A . 
F 5 HOH 337 837  278 HOH HOH A . 
F 5 HOH 338 838  331 HOH HOH A . 
F 5 HOH 339 839  228 HOH HOH A . 
F 5 HOH 340 840  427 HOH HOH A . 
F 5 HOH 341 841  296 HOH HOH A . 
F 5 HOH 342 842  161 HOH HOH A . 
F 5 HOH 343 843  519 HOH HOH A . 
F 5 HOH 344 844  503 HOH HOH A . 
F 5 HOH 345 845  416 HOH HOH A . 
F 5 HOH 346 846  268 HOH HOH A . 
F 5 HOH 347 847  356 HOH HOH A . 
F 5 HOH 348 848  182 HOH HOH A . 
F 5 HOH 349 849  324 HOH HOH A . 
F 5 HOH 350 850  168 HOH HOH A . 
F 5 HOH 351 851  477 HOH HOH A . 
F 5 HOH 352 852  446 HOH HOH A . 
F 5 HOH 353 853  469 HOH HOH A . 
F 5 HOH 354 854  357 HOH HOH A . 
F 5 HOH 355 855  419 HOH HOH A . 
F 5 HOH 356 856  353 HOH HOH A . 
F 5 HOH 357 857  258 HOH HOH A . 
F 5 HOH 358 858  351 HOH HOH A . 
F 5 HOH 359 859  522 HOH HOH A . 
F 5 HOH 360 860  409 HOH HOH A . 
F 5 HOH 361 861  92  HOH HOH A . 
F 5 HOH 362 862  362 HOH HOH A . 
F 5 HOH 363 863  181 HOH HOH A . 
F 5 HOH 364 864  483 HOH HOH A . 
F 5 HOH 365 865  521 HOH HOH A . 
F 5 HOH 366 866  341 HOH HOH A . 
F 5 HOH 367 867  511 HOH HOH A . 
F 5 HOH 368 868  415 HOH HOH A . 
F 5 HOH 369 869  180 HOH HOH A . 
F 5 HOH 370 870  463 HOH HOH A . 
F 5 HOH 371 871  365 HOH HOH A . 
F 5 HOH 372 872  387 HOH HOH A . 
F 5 HOH 373 873  460 HOH HOH A . 
F 5 HOH 374 874  410 HOH HOH A . 
F 5 HOH 375 875  292 HOH HOH A . 
F 5 HOH 376 876  506 HOH HOH A . 
F 5 HOH 377 877  367 HOH HOH A . 
F 5 HOH 378 878  225 HOH HOH A . 
F 5 HOH 379 879  153 HOH HOH A . 
F 5 HOH 380 880  239 HOH HOH A . 
F 5 HOH 381 881  529 HOH HOH A . 
F 5 HOH 382 882  242 HOH HOH A . 
F 5 HOH 383 883  190 HOH HOH A . 
F 5 HOH 384 884  375 HOH HOH A . 
F 5 HOH 385 885  238 HOH HOH A . 
F 5 HOH 386 886  169 HOH HOH A . 
F 5 HOH 387 887  420 HOH HOH A . 
F 5 HOH 388 888  422 HOH HOH A . 
F 5 HOH 389 889  471 HOH HOH A . 
F 5 HOH 390 890  388 HOH HOH A . 
F 5 HOH 391 891  516 HOH HOH A . 
F 5 HOH 392 892  297 HOH HOH A . 
F 5 HOH 393 893  436 HOH HOH A . 
F 5 HOH 394 894  515 HOH HOH A . 
F 5 HOH 395 895  284 HOH HOH A . 
F 5 HOH 396 896  402 HOH HOH A . 
F 5 HOH 397 897  514 HOH HOH A . 
F 5 HOH 398 898  343 HOH HOH A . 
F 5 HOH 399 899  479 HOH HOH A . 
F 5 HOH 400 900  531 HOH HOH A . 
F 5 HOH 401 901  283 HOH HOH A . 
F 5 HOH 402 902  385 HOH HOH A . 
F 5 HOH 403 903  383 HOH HOH A . 
F 5 HOH 404 904  452 HOH HOH A . 
F 5 HOH 405 905  295 HOH HOH A . 
F 5 HOH 406 906  311 HOH HOH A . 
F 5 HOH 407 907  326 HOH HOH A . 
F 5 HOH 408 908  317 HOH HOH A . 
F 5 HOH 409 909  382 HOH HOH A . 
F 5 HOH 410 910  314 HOH HOH A . 
F 5 HOH 411 911  177 HOH HOH A . 
F 5 HOH 412 912  435 HOH HOH A . 
F 5 HOH 413 913  319 HOH HOH A . 
F 5 HOH 414 914  140 HOH HOH A . 
F 5 HOH 415 915  262 HOH HOH A . 
F 5 HOH 416 916  208 HOH HOH A . 
F 5 HOH 417 917  81  HOH HOH A . 
F 5 HOH 418 918  528 HOH HOH A . 
F 5 HOH 419 919  347 HOH HOH A . 
F 5 HOH 420 920  210 HOH HOH A . 
F 5 HOH 421 921  439 HOH HOH A . 
F 5 HOH 422 922  502 HOH HOH A . 
F 5 HOH 423 923  115 HOH HOH A . 
F 5 HOH 424 924  252 HOH HOH A . 
F 5 HOH 425 925  428 HOH HOH A . 
F 5 HOH 426 926  230 HOH HOH A . 
F 5 HOH 427 927  517 HOH HOH A . 
F 5 HOH 428 928  406 HOH HOH A . 
F 5 HOH 429 929  312 HOH HOH A . 
F 5 HOH 430 930  501 HOH HOH A . 
F 5 HOH 431 931  526 HOH HOH A . 
F 5 HOH 432 932  500 HOH HOH A . 
F 5 HOH 433 933  513 HOH HOH A . 
F 5 HOH 434 934  496 HOH HOH A . 
F 5 HOH 435 935  399 HOH HOH A . 
F 5 HOH 436 936  127 HOH HOH A . 
F 5 HOH 437 937  377 HOH HOH A . 
F 5 HOH 438 938  437 HOH HOH A . 
F 5 HOH 439 939  211 HOH HOH A . 
F 5 HOH 440 940  216 HOH HOH A . 
F 5 HOH 441 941  433 HOH HOH A . 
F 5 HOH 442 942  267 HOH HOH A . 
F 5 HOH 443 943  253 HOH HOH A . 
F 5 HOH 444 944  397 HOH HOH A . 
F 5 HOH 445 945  453 HOH HOH A . 
F 5 HOH 446 946  449 HOH HOH A . 
F 5 HOH 447 947  194 HOH HOH A . 
F 5 HOH 448 948  229 HOH HOH A . 
F 5 HOH 449 949  404 HOH HOH A . 
F 5 HOH 450 950  498 HOH HOH A . 
F 5 HOH 451 951  384 HOH HOH A . 
F 5 HOH 452 952  136 HOH HOH A . 
F 5 HOH 453 953  413 HOH HOH A . 
F 5 HOH 454 954  425 HOH HOH A . 
F 5 HOH 455 955  360 HOH HOH A . 
F 5 HOH 456 956  130 HOH HOH A . 
F 5 HOH 457 957  485 HOH HOH A . 
F 5 HOH 458 958  76  HOH HOH A . 
F 5 HOH 459 959  272 HOH HOH A . 
F 5 HOH 460 960  316 HOH HOH A . 
F 5 HOH 461 961  146 HOH HOH A . 
F 5 HOH 462 962  306 HOH HOH A . 
F 5 HOH 463 963  338 HOH HOH A . 
F 5 HOH 464 964  379 HOH HOH A . 
F 5 HOH 465 965  322 HOH HOH A . 
F 5 HOH 466 966  508 HOH HOH A . 
F 5 HOH 467 967  478 HOH HOH A . 
F 5 HOH 468 968  414 HOH HOH A . 
F 5 HOH 469 969  209 HOH HOH A . 
F 5 HOH 470 970  359 HOH HOH A . 
F 5 HOH 471 971  348 HOH HOH A . 
F 5 HOH 472 972  250 HOH HOH A . 
F 5 HOH 473 973  282 HOH HOH A . 
F 5 HOH 474 974  480 HOH HOH A . 
F 5 HOH 475 975  45  HOH HOH A . 
F 5 HOH 476 976  263 HOH HOH A . 
F 5 HOH 477 977  466 HOH HOH A . 
F 5 HOH 478 978  491 HOH HOH A . 
F 5 HOH 479 979  456 HOH HOH A . 
F 5 HOH 480 980  371 HOH HOH A . 
F 5 HOH 481 981  438 HOH HOH A . 
F 5 HOH 482 982  392 HOH HOH A . 
F 5 HOH 483 983  400 HOH HOH A . 
F 5 HOH 484 984  431 HOH HOH A . 
F 5 HOH 485 985  240 HOH HOH A . 
F 5 HOH 486 986  434 HOH HOH A . 
F 5 HOH 487 987  241 HOH HOH A . 
F 5 HOH 488 988  372 HOH HOH A . 
F 5 HOH 489 989  364 HOH HOH A . 
F 5 HOH 490 990  467 HOH HOH A . 
F 5 HOH 491 991  459 HOH HOH A . 
F 5 HOH 492 992  505 HOH HOH A . 
F 5 HOH 493 993  171 HOH HOH A . 
F 5 HOH 494 994  461 HOH HOH A . 
F 5 HOH 495 995  474 HOH HOH A . 
F 5 HOH 496 996  532 HOH HOH A . 
F 5 HOH 497 997  468 HOH HOH A . 
F 5 HOH 498 998  369 HOH HOH A . 
F 5 HOH 499 999  527 HOH HOH A . 
F 5 HOH 500 1000 405 HOH HOH A . 
F 5 HOH 501 1001 220 HOH HOH A . 
F 5 HOH 502 1002 488 HOH HOH A . 
F 5 HOH 503 1003 481 HOH HOH A . 
F 5 HOH 504 1004 354 HOH HOH A . 
F 5 HOH 505 1005 285 HOH HOH A . 
F 5 HOH 506 1006 524 HOH HOH A . 
F 5 HOH 507 1007 445 HOH HOH A . 
F 5 HOH 508 1008 132 HOH HOH A . 
F 5 HOH 509 1009 482 HOH HOH A . 
F 5 HOH 510 1010 286 HOH HOH A . 
F 5 HOH 511 1011 179 HOH HOH A . 
F 5 HOH 512 1012 499 HOH HOH A . 
F 5 HOH 513 1013 165 HOH HOH A . 
F 5 HOH 514 1014 203 HOH HOH A . 
F 5 HOH 515 1015 328 HOH HOH A . 
F 5 HOH 516 1016 417 HOH HOH A . 
F 5 HOH 517 1017 490 HOH HOH A . 
F 5 HOH 518 1018 520 HOH HOH A . 
F 5 HOH 519 1019 188 HOH HOH A . 
F 5 HOH 520 1020 447 HOH HOH A . 
F 5 HOH 521 1021 275 HOH HOH A . 
F 5 HOH 522 1022 393 HOH HOH A . 
F 5 HOH 523 1023 236 HOH HOH A . 
F 5 HOH 524 1024 300 HOH HOH A . 
F 5 HOH 525 1025 464 HOH HOH A . 
F 5 HOH 526 1026 293 HOH HOH A . 
F 5 HOH 527 1027 334 HOH HOH A . 
F 5 HOH 528 1028 430 HOH HOH A . 
F 5 HOH 529 1029 489 HOH HOH A . 
F 5 HOH 530 1030 423 HOH HOH A . 
F 5 HOH 531 1031 472 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 20  ? CG    ? A LYS 26  CG    
2  1 Y 1 A LYS 20  ? CD    ? A LYS 26  CD    
3  1 Y 1 A LYS 20  ? CE    ? A LYS 26  CE    
4  1 Y 1 A LYS 20  ? NZ    ? A LYS 26  NZ    
5  1 Y 1 A GLU 116 ? CG    ? A GLU 122 CG    
6  1 Y 1 A GLU 116 ? CD    ? A GLU 122 CD    
7  1 Y 1 A GLU 116 ? OE1   ? A GLU 122 OE1   
8  1 Y 1 A GLU 116 ? OE2   ? A GLU 122 OE2   
9  1 Y 1 A ARG 136 ? CG    ? A ARG 142 CG    
10 1 Y 1 A ARG 136 ? CD    ? A ARG 142 CD    
11 1 Y 1 A ARG 136 ? NE    ? A ARG 142 NE    
12 1 Y 1 A ARG 136 ? CZ    ? A ARG 142 CZ    
13 1 Y 1 A ARG 136 ? NH1   ? A ARG 142 NH1   
14 1 Y 1 A ARG 136 ? NH2   ? A ARG 142 NH2   
15 1 Y 1 A ASP 243 ? CG    ? A ASP 249 CG    
16 1 Y 1 A ASP 243 ? OD1   ? A ASP 249 OD1   
17 1 Y 1 A ASP 243 ? OD2   ? A ASP 249 OD2   
18 1 Y 1 A GLU 329 ? CG    ? A GLU 335 CG    
19 1 Y 1 A GLU 329 ? CD    ? A GLU 335 CD    
20 1 Y 1 A GLU 329 ? OE1   ? A GLU 335 OE1   
21 1 Y 1 A GLU 329 ? OE2   ? A GLU 335 OE2   
22 1 N 1 A 5J8 402 ? C4    ? C 5J8 1   C4    
23 1 N 1 A 5J8 402 ? C5    ? C 5J8 1   C5    
24 1 N 1 A 5J8 402 ? C6    ? C 5J8 1   C6    
25 1 N 1 A 5J8 402 ? C8    ? C 5J8 1   C8    
26 1 N 1 A 5J8 402 ? N1    ? C 5J8 1   N1    
27 1 N 1 A 5J8 402 ? N3    ? C 5J8 1   N3    
28 1 N 1 A 5J8 402 ? "C5'" ? C 5J8 1   "C5'" 
29 1 N 1 A 5J8 402 ? "C4'" ? C 5J8 1   "C4'" 
30 1 N 1 A 5J8 402 ? "O4'" ? C 5J8 1   "O4'" 
31 1 N 1 A 5J8 402 ? "C3'" ? C 5J8 1   "C3'" 
32 1 N 1 A 5J8 402 ? "O3'" ? C 5J8 1   "O3'" 
33 1 N 1 A 5J8 402 ? "C2'" ? C 5J8 1   "C2'" 
34 1 N 1 A 5J8 402 ? "O2'" ? C 5J8 1   "O2'" 
35 1 N 1 A 5J8 402 ? "P2'" ? C 5J8 1   "P2'" 
36 1 N 1 A 5J8 402 ? OP1   ? C 5J8 1   OP1   
37 1 N 1 A 5J8 402 ? OP3   ? C 5J8 1   OP3   
38 1 N 1 A 5J8 402 ? OP2   ? C 5J8 1   OP2   
39 1 N 1 A 5J8 402 ? "C1'" ? C 5J8 1   "C1'" 
40 1 N 1 A 5J8 402 ? N9    ? C 5J8 1   N9    
41 1 N 1 A 5J8 402 ? N7    ? C 5J8 1   N7    
42 1 N 1 A 5J8 402 ? C2    ? C 5J8 1   C2    
43 1 N 1 A 5J8 402 ? N6    ? C 5J8 1   N6    
44 1 N 1 A 5J8 403 ? NBU   ? D 5J8 1   NBU   
45 1 N 1 A 5J8 403 ? CBT   ? D 5J8 1   CBT   
46 1 N 1 A 5J8 403 ? OBV   ? D 5J8 1   OBV   
47 1 N 1 A 5J8 403 ? CBR   ? D 5J8 1   CBR   
48 1 N 1 A 5J8 403 ? CBQ   ? D 5J8 1   CBQ   
49 1 N 1 A 5J8 403 ? CBS   ? D 5J8 1   CBS   
50 1 N 1 A 5J8 403 ? CBN   ? D 5J8 1   CBN   
51 1 N 1 A 5J8 403 ? CBO   ? D 5J8 1   CBO   
52 1 N 1 A 5J8 403 ? NBP   ? D 5J8 1   NBP   
53 1 N 1 A 5J8 403 ? CBM   ? D 5J8 1   CBM   
54 1 N 1 A 5J8 403 ? OBG   ? D 5J8 1   OBG   
55 1 N 1 A 5J8 403 ? CBF   ? D 5J8 1   CBF   
56 1 N 1 A 5J8 403 ? OBI   ? D 5J8 1   OBI   
57 1 N 1 A 5J8 403 ? CBE   ? D 5J8 1   CBE   
58 1 N 1 A 5J8 403 ? OBJ   ? D 5J8 1   OBJ   
59 1 N 1 A 5J8 403 ? CBH   ? D 5J8 1   CBH   
60 1 N 1 A 5J8 403 ? CBK   ? D 5J8 1   CBK   
61 1 N 1 A 5J8 403 ? OBL   ? D 5J8 1   OBL   
62 1 N 1 A 5J8 403 ? PAA   ? D 5J8 1   PAA   
63 1 N 1 A 5J8 403 ? OAC   ? D 5J8 1   OAC   
64 1 N 1 A 5J8 403 ? OAB   ? D 5J8 1   OAB   
# 
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 ? ? ? '(dev_4761)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? '(dev_4761)' 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QO7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     88.400 
_cell.length_a_esd                 ? 
_cell.length_b                     90.270 
_cell.length_b_esd                 ? 
_cell.length_c                     49.480 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8QO7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8QO7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.71 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM MES/Tris, 10 mM ammonium sulfate, 14% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033 
_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                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QO7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               45.13 
_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                                     78424 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.66 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          31.68 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.4 
_reflns_shell.d_res_low                                     1.42 
_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                             37199 
_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                                  0.812 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8QO7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.40 
_refine.ls_d_res_low                             45.13 
_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                     78424 
_refine.ls_number_reflns_R_free                  3922 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1523 
_refine.ls_R_factor_R_free                       0.1708 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1514 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.02 
_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                            0.11 
_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.pdbx_number_atoms_protein        2749 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         89 
_refine_hist.number_atoms_solvent             531 
_refine_hist.number_atoms_total               3369 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        45.13 
# 
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' ? 0.017  ? 2920 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.611  ? 3985 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.736 ? 414  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.110  ? 436  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.021  ? 505  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.40 1.42  . . 132 2496 95.00  . . . . 0.2044 . . . . . . . . . . . 0.2349 
'X-RAY DIFFRACTION' 1.42 1.44  . . 136 2592 99.00  . . . . 0.1938 . . . . . . . . . . . 0.2427 
'X-RAY DIFFRACTION' 1.44 1.45  . . 138 2618 99.00  . . . . 0.1799 . . . . . . . . . . . 0.2008 
'X-RAY DIFFRACTION' 1.45 1.47  . . 137 2615 99.00  . . . . 0.1711 . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 1.47 1.49  . . 139 2634 100.00 . . . . 0.1663 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 1.49 1.52  . . 138 2611 100.00 . . . . 0.1589 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.52 1.54  . . 139 2654 100.00 . . . . 0.1537 . . . . . . . . . . . 0.1859 
'X-RAY DIFFRACTION' 1.54 1.57  . . 137 2604 100.00 . . . . 0.1456 . . . . . . . . . . . 0.2101 
'X-RAY DIFFRACTION' 1.57 1.59  . . 141 2669 100.00 . . . . 0.1442 . . . . . . . . . . . 0.1649 
'X-RAY DIFFRACTION' 1.59 1.62  . . 138 2635 100.00 . . . . 0.1413 . . . . . . . . . . . 0.1698 
'X-RAY DIFFRACTION' 1.62 1.65  . . 142 2681 100.00 . . . . 0.1424 . . . . . . . . . . . 0.1737 
'X-RAY DIFFRACTION' 1.65 1.69  . . 137 2619 100.00 . . . . 0.1377 . . . . . . . . . . . 0.1748 
'X-RAY DIFFRACTION' 1.69 1.72  . . 140 2650 100.00 . . . . 0.1493 . . . . . . . . . . . 0.1606 
'X-RAY DIFFRACTION' 1.72 1.76  . . 140 2672 100.00 . . . . 0.1434 . . . . . . . . . . . 0.1612 
'X-RAY DIFFRACTION' 1.76 1.81  . . 140 2642 100.00 . . . . 0.1465 . . . . . . . . . . . 0.1690 
'X-RAY DIFFRACTION' 1.81 1.86  . . 138 2639 100.00 . . . . 0.1524 . . . . . . . . . . . 0.1550 
'X-RAY DIFFRACTION' 1.86 1.91  . . 142 2695 100.00 . . . . 0.1608 . . . . . . . . . . . 0.2054 
'X-RAY DIFFRACTION' 1.91 1.97  . . 139 2645 100.00 . . . . 0.1545 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 1.97 2.04  . . 140 2642 100.00 . . . . 0.1523 . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 2.04 2.13  . . 140 2660 100.00 . . . . 0.1462 . . . . . . . . . . . 0.1506 
'X-RAY DIFFRACTION' 2.13 2.22  . . 141 2687 100.00 . . . . 0.1449 . . . . . . . . . . . 0.1532 
'X-RAY DIFFRACTION' 2.22 2.34  . . 142 2690 100.00 . . . . 0.1483 . . . . . . . . . . . 0.1609 
'X-RAY DIFFRACTION' 2.34 2.49  . . 140 2671 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1860 
'X-RAY DIFFRACTION' 2.49 2.68  . . 142 2694 100.00 . . . . 0.1616 . . . . . . . . . . . 0.1742 
'X-RAY DIFFRACTION' 2.68 2.95  . . 143 2715 100.00 . . . . 0.1547 . . . . . . . . . . . 0.1452 
'X-RAY DIFFRACTION' 2.95 3.37  . . 142 2707 100.00 . . . . 0.1471 . . . . . . . . . . . 0.1693 
'X-RAY DIFFRACTION' 3.37 4.25  . . 146 2776 100.00 . . . . 0.1379 . . . . . . . . . . . 0.1368 
'X-RAY DIFFRACTION' 4.25 45.13 . . 153 2889 100.00 . . . . 0.1567 . . . . . . . . . . . 0.1761 
# 
_struct.entry_id                     8QO7 
_struct.title                        'OPR3 variant R283E in complex with NADPH4' 
_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        8QO7 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, NADPH, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    OPR3_SOLLC 
_struct_ref.pdbx_db_accession          Q9FEW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QO7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 7 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 402 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9FEW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  396 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       396 
# 
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 8QO7 HIS A 1   ? UNP Q9FEW9 ?   ?   'expression tag'      -5  1 
1 8QO7 HIS A 2   ? UNP Q9FEW9 ?   ?   'expression tag'      -4  2 
1 8QO7 HIS A 3   ? UNP Q9FEW9 ?   ?   'expression tag'      -3  3 
1 8QO7 HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'      -2  4 
1 8QO7 HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'      -1  5 
1 8QO7 HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'      0   6 
1 8QO7 GLU A 289 ? UNP Q9FEW9 ARG 283 'engineered mutation' 283 7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,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 ASN A 16  ? SER A 20  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 43  ? ILE A 47  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 49  ? ALA A 60  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 88  ? LYS A 105 ? THR A 82  LYS A 99  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 121 ? ALA A 129 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 162 ? ALA A 183 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 196 ? LYS A 203 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 216 ? CYS A 221 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 221 ? GLY A 236 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 257 ? GLY A 277 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 LEU A 310 ? TYR A 318 ? LEU A 304 TYR A 312 1 ? 9  
HELX_P HELX_P12 AB3 THR A 329 ? GLN A 339 ? THR A 323 GLN A 333 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 348 ? ASN A 354 ? GLY A 342 ASN A 348 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 356 ? ASN A 364 ? ASP A 350 ASN A 358 1 ? 9  
HELX_P HELX_P15 AB6 ASN A 371 ? PHE A 375 ? ASN A 365 PHE A 369 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA2 1 2  ? parallel      
AA2 2 3  ? parallel      
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? parallel      
AA2 6 7  ? parallel      
AA2 7 8  ? parallel      
AA2 8 9  ? parallel      
AA2 9 10 ? parallel      
AA3 1 2  ? parallel      
AA4 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  TYR A 22  ? MET A 24  ? TYR A 16  MET A 18  
AA1 2  PHE A 27  ? LEU A 29  ? PHE A 21  LEU A 23  
AA2 1  THR A 71  ? MET A 72  ? THR A 65  MET A 66  
AA2 2  VAL A 108 ? TRP A 114 ? VAL A 102 TRP A 108 
AA2 3  GLY A 187 ? GLY A 192 ? GLY A 181 GLY A 186 
AA2 4  VAL A 240 ? VAL A 244 ? VAL A 234 VAL A 238 
AA2 5  TYR A 282 ? THR A 286 ? TYR A 276 THR A 280 
AA2 6  PHE A 322 ? SER A 325 ? PHE A 316 SER A 319 
AA2 7  LEU A 344 ? TYR A 347 ? LEU A 338 TYR A 341 
AA2 8  VAL A 33  ? LEU A 35  ? VAL A 27  LEU A 29  
AA2 9  PHE A 65  ? ILE A 67  ? PHE A 59  ILE A 61  
AA2 10 VAL A 108 ? TRP A 114 ? VAL A 102 TRP A 108 
AA3 1  ILE A 132 ? SER A 133 ? ILE A 126 SER A 127 
AA3 2  ARG A 159 ? ALA A 160 ? ARG A 153 ALA A 154 
AA4 1  ILE A 145 ? LEU A 146 ? ILE A 139 LEU A 140 
AA4 2  HIS A 152 ? GLY A 153 ? HIS A 146 GLY A 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N MET A 24  ? N MET A 18  O PHE A 27  ? O PHE A 21  
AA2 1 2  N THR A 71  ? N THR A 65  O TRP A 114 ? O TRP A 108 
AA2 2 3  N LEU A 113 ? N LEU A 107 O GLU A 189 ? O GLU A 183 
AA2 3 4  N ILE A 190 ? N ILE A 184 O GLY A 241 ? O GLY A 235 
AA2 4 5  N VAL A 242 ? N VAL A 236 O HIS A 284 ? O HIS A 278 
AA2 5 6  N LEU A 283 ? N LEU A 277 O ILE A 323 ? O ILE A 317 
AA2 6 7  N CYS A 324 ? N CYS A 318 O SER A 346 ? O SER A 340 
AA2 7 8  O VAL A 345 ? O VAL A 339 N VAL A 34  ? N VAL A 28  
AA2 8 9  N LEU A 35  ? N LEU A 29  O PHE A 65  ? O PHE A 59  
AA2 9 10 N LEU A 66  ? N LEU A 60  O VAL A 108 ? O VAL A 102 
AA3 1 2  N SER A 133 ? N SER A 127 O ARG A 159 ? O ARG A 153 
AA4 1 2  N ILE A 145 ? N ILE A 139 O GLY A 153 ? O GLY A 147 
# 
_pdbx_entry_details.entry_id                   8QO7 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 O  A HOH 617 ? ? O A HOH 639 ? ? 2.01 
2  1 O  A HOH 508 ? ? O A HOH 653 ? ? 2.01 
3  1 O  A HOH 534 ? ? O A HOH 794 ? ? 2.05 
4  1 O  A HOH 860 ? ? O A HOH 964 ? ? 2.09 
5  1 O1 A SO4 404 ? ? O A HOH 501 ? ? 2.10 
6  1 O  A HOH 724 ? ? O A HOH 983 ? ? 2.12 
7  1 O  A HOH 723 ? ? O A HOH 881 ? ? 2.12 
8  1 O  A HOH 702 ? ? O A HOH 715 ? ? 2.16 
9  1 O  A HOH 787 ? ? O A HOH 874 ? ? 2.17 
10 1 O  A HOH 881 ? ? O A HOH 900 ? ? 2.18 
11 1 O  A HOH 509 ? ? O A HOH 698 ? ? 2.18 
12 1 O  A HOH 621 ? ? O A HOH 899 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              232 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              232 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              232 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                125.98 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            7.68 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 63  ? ? -42.46  150.67 
2 1 ALA A 121 ? ? 58.72   17.11  
3 1 ASN A 135 ? ? -69.93  4.58   
4 1 HIS A 244 ? ? -36.82  134.98 
5 1 ALA A 247 ? ? -118.87 68.74  
6 1 ASP A 350 ? ? -90.62  40.30  
7 1 TYR A 378 ? ? -126.36 -62.78 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 26  ? ? 0.081 'SIDE CHAIN' 
2 1 ARG A 262 ? ? 0.131 'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1026 ? 5.81 . 
2 1 O ? A HOH 1027 ? 6.13 . 
3 1 O ? A HOH 1028 ? 6.23 . 
4 1 O ? A HOH 1029 ? 6.40 . 
5 1 O ? A HOH 1030 ? 7.27 . 
6 1 O ? A HOH 1031 ? 7.74 . 
# 
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 HIS -5  ? A HIS 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A MET 1   ? A MET 7   
8  1 Y 1 A ALA 2   ? A ALA 8   
9  1 Y 1 A SER 3   ? A SER 9   
10 1 Y 1 A SER 4   ? A SER 10  
11 1 Y 1 A ALA 5   ? A ALA 11  
12 1 Y 1 A GLN 6   ? A GLN 12  
13 1 Y 1 A ASP 7   ? A ASP 13  
14 1 Y 1 A GLY 8   ? A GLY 14  
15 1 Y 1 A ASN 9   ? A ASN 15  
16 1 Y 1 A GLU 283 ? A GLU 289 
17 1 Y 1 A TYR 284 ? A TYR 290 
18 1 Y 1 A VAL 285 ? A VAL 291 
19 1 Y 1 A ALA 286 ? A ALA 292 
20 1 Y 1 A TYR 287 ? A TYR 293 
21 1 Y 1 A GLY 288 ? A GLY 294 
22 1 Y 1 A GLN 289 ? A GLN 295 
23 1 Y 1 A THR 290 ? A THR 296 
24 1 Y 1 A GLU 291 ? A GLU 297 
25 1 Y 1 A ALA 292 ? A ALA 298 
26 1 Y 1 A GLY 293 ? A GLY 299 
27 1 Y 1 A ARG 294 ? A ARG 300 
28 1 Y 1 A LEU 295 ? A LEU 301 
29 1 Y 1 A GLY 296 ? A GLY 302 
30 1 Y 1 A SER 297 ? A SER 303 
31 1 Y 1 A GLU 298 ? A GLU 304 
32 1 Y 1 A GLU 299 ? A GLU 305 
33 1 Y 1 A GLU 300 ? A GLU 306 
34 1 Y 1 A GLU 301 ? A GLU 307 
35 1 Y 1 A ALA 302 ? A ALA 308 
36 1 Y 1 A GLN 385 ? A GLN 391 
37 1 Y 1 A GLY 386 ? A GLY 392 
38 1 Y 1 A ASN 387 ? A ASN 393 
39 1 Y 1 A GLY 388 ? A GLY 394 
40 1 Y 1 A SER 389 ? A SER 395 
41 1 Y 1 A ASN 390 ? A ASN 396 
42 1 Y 1 A GLY 391 ? A GLY 397 
43 1 Y 1 A PRO 392 ? A PRO 398 
44 1 Y 1 A LEU 393 ? A LEU 399 
45 1 Y 1 A SER 394 ? A SER 400 
46 1 Y 1 A ARG 395 ? A ARG 401 
47 1 Y 1 A LEU 396 ? A LEU 402 
# 
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 
5J8 C4     C Y N 1   
5J8 C5     C Y N 2   
5J8 C6     C Y N 3   
5J8 C8     C Y N 4   
5J8 N1     N Y N 5   
5J8 N3     N Y N 6   
5J8 NBU    N N N 7   
5J8 CBT    C N N 8   
5J8 OBV    O N N 9   
5J8 CBR    C N N 10  
5J8 CBQ    C N N 11  
5J8 CBS    C N N 12  
5J8 CBN    C N N 13  
5J8 CBO    C N N 14  
5J8 NBP    N N N 15  
5J8 CBM    C N R 16  
5J8 OBG    O N N 17  
5J8 CBF    C N R 18  
5J8 OBI    O N N 19  
5J8 CBE    C N S 20  
5J8 OBJ    O N N 21  
5J8 CBH    C N R 22  
5J8 CBK    C N N 23  
5J8 OBL    O N N 24  
5J8 PAA    P N N 25  
5J8 OAC    O N N 26  
5J8 OAB    O N N 27  
5J8 OAD    O N N 28  
5J8 PAE    P N N 29  
5J8 OAG    O N N 30  
5J8 OAF    O N N 31  
5J8 "O5'"  O N N 32  
5J8 "C5'"  C N N 33  
5J8 "C4'"  C N R 34  
5J8 "O4'"  O N N 35  
5J8 "C3'"  C N R 36  
5J8 "O3'"  O N N 37  
5J8 "C2'"  C N R 38  
5J8 "O2'"  O N N 39  
5J8 "P2'"  P N N 40  
5J8 OP1    O N N 41  
5J8 OP3    O N N 42  
5J8 OP2    O N N 43  
5J8 "C1'"  C N R 44  
5J8 N9     N Y N 45  
5J8 N7     N Y N 46  
5J8 C2     C Y N 47  
5J8 N6     N N N 48  
5J8 H1     H N N 49  
5J8 H2     H N N 50  
5J8 H3     H N N 51  
5J8 H5     H N N 52  
5J8 H7     H N N 53  
5J8 H8     H N N 54  
5J8 H9     H N N 55  
5J8 H10    H N N 56  
5J8 H11    H N N 57  
5J8 H12    H N N 58  
5J8 H13    H N N 59  
5J8 H14    H N N 60  
5J8 H15    H N N 61  
5J8 H16    H N N 62  
5J8 H17    H N N 63  
5J8 H18    H N N 64  
5J8 H19    H N N 65  
5J8 H20    H N N 66  
5J8 H21    H N N 67  
5J8 H22    H N N 68  
5J8 H23    H N N 69  
5J8 H24    H N N 70  
5J8 H25    H N N 71  
5J8 H26    H N N 72  
5J8 H27    H N N 73  
5J8 H28    H N N 74  
5J8 H29    H N N 75  
5J8 H30    H N N 76  
5J8 H31    H N N 77  
5J8 H32    H N N 78  
5J8 H4     H N N 79  
5J8 H6     H N N 80  
ALA N      N N N 81  
ALA CA     C N S 82  
ALA C      C N N 83  
ALA O      O N N 84  
ALA CB     C N N 85  
ALA OXT    O N N 86  
ALA H      H N N 87  
ALA H2     H N N 88  
ALA HA     H N N 89  
ALA HB1    H N N 90  
ALA HB2    H N N 91  
ALA HB3    H N N 92  
ALA HXT    H N N 93  
ARG N      N N N 94  
ARG CA     C N S 95  
ARG C      C N N 96  
ARG O      O N N 97  
ARG CB     C N N 98  
ARG CG     C N N 99  
ARG CD     C N N 100 
ARG NE     N N N 101 
ARG CZ     C N N 102 
ARG NH1    N N N 103 
ARG NH2    N N N 104 
ARG OXT    O N N 105 
ARG H      H N N 106 
ARG H2     H N N 107 
ARG HA     H N N 108 
ARG HB2    H N N 109 
ARG HB3    H N N 110 
ARG HG2    H N N 111 
ARG HG3    H N N 112 
ARG HD2    H N N 113 
ARG HD3    H N N 114 
ARG HE     H N N 115 
ARG HH11   H N N 116 
ARG HH12   H N N 117 
ARG HH21   H N N 118 
ARG HH22   H N N 119 
ARG HXT    H N N 120 
ASN N      N N N 121 
ASN CA     C N S 122 
ASN C      C N N 123 
ASN O      O N N 124 
ASN CB     C N N 125 
ASN CG     C N N 126 
ASN OD1    O N N 127 
ASN ND2    N N N 128 
ASN OXT    O N N 129 
ASN H      H N N 130 
ASN H2     H N N 131 
ASN HA     H N N 132 
ASN HB2    H N N 133 
ASN HB3    H N N 134 
ASN HD21   H N N 135 
ASN HD22   H N N 136 
ASN HXT    H N N 137 
ASP N      N N N 138 
ASP CA     C N S 139 
ASP C      C N N 140 
ASP O      O N N 141 
ASP CB     C N N 142 
ASP CG     C N N 143 
ASP OD1    O N N 144 
ASP OD2    O N N 145 
ASP OXT    O N N 146 
ASP H      H N N 147 
ASP H2     H N N 148 
ASP HA     H N N 149 
ASP HB2    H N N 150 
ASP HB3    H N N 151 
ASP HD2    H N N 152 
ASP HXT    H N N 153 
CYS N      N N N 154 
CYS CA     C N R 155 
CYS C      C N N 156 
CYS O      O N N 157 
CYS CB     C N N 158 
CYS SG     S N N 159 
CYS OXT    O N N 160 
CYS H      H N N 161 
CYS H2     H N N 162 
CYS HA     H N N 163 
CYS HB2    H N N 164 
CYS HB3    H N N 165 
CYS HG     H N N 166 
CYS HXT    H N N 167 
FMN N1     N N N 168 
FMN C2     C N N 169 
FMN O2     O N N 170 
FMN N3     N N N 171 
FMN C4     C N N 172 
FMN O4     O N N 173 
FMN C4A    C N N 174 
FMN N5     N N N 175 
FMN C5A    C Y N 176 
FMN C6     C Y N 177 
FMN C7     C Y N 178 
FMN C7M    C N N 179 
FMN C8     C Y N 180 
FMN C8M    C N N 181 
FMN C9     C Y N 182 
FMN C9A    C Y N 183 
FMN N10    N N N 184 
FMN C10    C N N 185 
FMN "C1'"  C N N 186 
FMN "C2'"  C N S 187 
FMN "O2'"  O N N 188 
FMN "C3'"  C N S 189 
FMN "O3'"  O N N 190 
FMN "C4'"  C N R 191 
FMN "O4'"  O N N 192 
FMN "C5'"  C N N 193 
FMN "O5'"  O N N 194 
FMN P      P N N 195 
FMN O1P    O N N 196 
FMN O2P    O N N 197 
FMN O3P    O N N 198 
FMN HN3    H N N 199 
FMN H6     H N N 200 
FMN HM71   H N N 201 
FMN HM72   H N N 202 
FMN HM73   H N N 203 
FMN HM81   H N N 204 
FMN HM82   H N N 205 
FMN HM83   H N N 206 
FMN H9     H N N 207 
FMN "H1'1" H N N 208 
FMN "H1'2" H N N 209 
FMN "H2'"  H N N 210 
FMN "HO2'" H N N 211 
FMN "H3'"  H N N 212 
FMN "HO3'" H N N 213 
FMN "H4'"  H N N 214 
FMN "HO4'" H N N 215 
FMN "H5'1" H N N 216 
FMN "H5'2" H N N 217 
FMN HOP2   H N N 218 
FMN HOP3   H N N 219 
GLN N      N N N 220 
GLN CA     C N S 221 
GLN C      C N N 222 
GLN O      O N N 223 
GLN CB     C N N 224 
GLN CG     C N N 225 
GLN CD     C N N 226 
GLN OE1    O N N 227 
GLN NE2    N N N 228 
GLN OXT    O N N 229 
GLN H      H N N 230 
GLN H2     H N N 231 
GLN HA     H N N 232 
GLN HB2    H N N 233 
GLN HB3    H N N 234 
GLN HG2    H N N 235 
GLN HG3    H N N 236 
GLN HE21   H N N 237 
GLN HE22   H N N 238 
GLN HXT    H N N 239 
GLU N      N N N 240 
GLU CA     C N S 241 
GLU C      C N N 242 
GLU O      O N N 243 
GLU CB     C N N 244 
GLU CG     C N N 245 
GLU CD     C N N 246 
GLU OE1    O N N 247 
GLU OE2    O N N 248 
GLU OXT    O N N 249 
GLU H      H N N 250 
GLU H2     H N N 251 
GLU HA     H N N 252 
GLU HB2    H N N 253 
GLU HB3    H N N 254 
GLU HG2    H N N 255 
GLU HG3    H N N 256 
GLU HE2    H N N 257 
GLU HXT    H N N 258 
GLY N      N N N 259 
GLY CA     C N N 260 
GLY C      C N N 261 
GLY O      O N N 262 
GLY OXT    O N N 263 
GLY H      H N N 264 
GLY H2     H N N 265 
GLY HA2    H N N 266 
GLY HA3    H N N 267 
GLY HXT    H N N 268 
HIS N      N N N 269 
HIS CA     C N S 270 
HIS C      C N N 271 
HIS O      O N N 272 
HIS CB     C N N 273 
HIS CG     C Y N 274 
HIS ND1    N Y N 275 
HIS CD2    C Y N 276 
HIS CE1    C Y N 277 
HIS NE2    N Y N 278 
HIS OXT    O N N 279 
HIS H      H N N 280 
HIS H2     H N N 281 
HIS HA     H N N 282 
HIS HB2    H N N 283 
HIS HB3    H N N 284 
HIS HD1    H N N 285 
HIS HD2    H N N 286 
HIS HE1    H N N 287 
HIS HE2    H N N 288 
HIS HXT    H N N 289 
HOH O      O N N 290 
HOH H1     H N N 291 
HOH H2     H N N 292 
ILE N      N N N 293 
ILE CA     C N S 294 
ILE C      C N N 295 
ILE O      O N N 296 
ILE CB     C N S 297 
ILE CG1    C N N 298 
ILE CG2    C N N 299 
ILE CD1    C N N 300 
ILE OXT    O N N 301 
ILE H      H N N 302 
ILE H2     H N N 303 
ILE HA     H N N 304 
ILE HB     H N N 305 
ILE HG12   H N N 306 
ILE HG13   H N N 307 
ILE HG21   H N N 308 
ILE HG22   H N N 309 
ILE HG23   H N N 310 
ILE HD11   H N N 311 
ILE HD12   H N N 312 
ILE HD13   H N N 313 
ILE HXT    H N N 314 
LEU N      N N N 315 
LEU CA     C N S 316 
LEU C      C N N 317 
LEU O      O N N 318 
LEU CB     C N N 319 
LEU CG     C N N 320 
LEU CD1    C N N 321 
LEU CD2    C N N 322 
LEU OXT    O N N 323 
LEU H      H N N 324 
LEU H2     H N N 325 
LEU HA     H N N 326 
LEU HB2    H N N 327 
LEU HB3    H N N 328 
LEU HG     H N N 329 
LEU HD11   H N N 330 
LEU HD12   H N N 331 
LEU HD13   H N N 332 
LEU HD21   H N N 333 
LEU HD22   H N N 334 
LEU HD23   H N N 335 
LEU HXT    H N N 336 
LYS N      N N N 337 
LYS CA     C N S 338 
LYS C      C N N 339 
LYS O      O N N 340 
LYS CB     C N N 341 
LYS CG     C N N 342 
LYS CD     C N N 343 
LYS CE     C N N 344 
LYS NZ     N N N 345 
LYS OXT    O N N 346 
LYS H      H N N 347 
LYS H2     H N N 348 
LYS HA     H N N 349 
LYS HB2    H N N 350 
LYS HB3    H N N 351 
LYS HG2    H N N 352 
LYS HG3    H N N 353 
LYS HD2    H N N 354 
LYS HD3    H N N 355 
LYS HE2    H N N 356 
LYS HE3    H N N 357 
LYS HZ1    H N N 358 
LYS HZ2    H N N 359 
LYS HZ3    H N N 360 
LYS HXT    H N N 361 
MET N      N N N 362 
MET CA     C N S 363 
MET C      C N N 364 
MET O      O N N 365 
MET CB     C N N 366 
MET CG     C N N 367 
MET SD     S N N 368 
MET CE     C N N 369 
MET OXT    O N N 370 
MET H      H N N 371 
MET H2     H N N 372 
MET HA     H N N 373 
MET HB2    H N N 374 
MET HB3    H N N 375 
MET HG2    H N N 376 
MET HG3    H N N 377 
MET HE1    H N N 378 
MET HE2    H N N 379 
MET HE3    H N N 380 
MET HXT    H N N 381 
PHE N      N N N 382 
PHE CA     C N S 383 
PHE C      C N N 384 
PHE O      O N N 385 
PHE CB     C N N 386 
PHE CG     C Y N 387 
PHE CD1    C Y N 388 
PHE CD2    C Y N 389 
PHE CE1    C Y N 390 
PHE CE2    C Y N 391 
PHE CZ     C Y N 392 
PHE OXT    O N N 393 
PHE H      H N N 394 
PHE H2     H N N 395 
PHE HA     H N N 396 
PHE HB2    H N N 397 
PHE HB3    H N N 398 
PHE HD1    H N N 399 
PHE HD2    H N N 400 
PHE HE1    H N N 401 
PHE HE2    H N N 402 
PHE HZ     H N N 403 
PHE HXT    H N N 404 
PRO N      N N N 405 
PRO CA     C N S 406 
PRO C      C N N 407 
PRO O      O N N 408 
PRO CB     C N N 409 
PRO CG     C N N 410 
PRO CD     C N N 411 
PRO OXT    O N N 412 
PRO H      H N N 413 
PRO HA     H N N 414 
PRO HB2    H N N 415 
PRO HB3    H N N 416 
PRO HG2    H N N 417 
PRO HG3    H N N 418 
PRO HD2    H N N 419 
PRO HD3    H N N 420 
PRO HXT    H N N 421 
SER N      N N N 422 
SER CA     C N S 423 
SER C      C N N 424 
SER O      O N N 425 
SER CB     C N N 426 
SER OG     O N N 427 
SER OXT    O N N 428 
SER H      H N N 429 
SER H2     H N N 430 
SER HA     H N N 431 
SER HB2    H N N 432 
SER HB3    H N N 433 
SER HG     H N N 434 
SER HXT    H N N 435 
SO4 S      S N N 436 
SO4 O1     O N N 437 
SO4 O2     O N N 438 
SO4 O3     O N N 439 
SO4 O4     O N N 440 
THR N      N N N 441 
THR CA     C N S 442 
THR C      C N N 443 
THR O      O N N 444 
THR CB     C N R 445 
THR OG1    O N N 446 
THR CG2    C N N 447 
THR OXT    O N N 448 
THR H      H N N 449 
THR H2     H N N 450 
THR HA     H N N 451 
THR HB     H N N 452 
THR HG1    H N N 453 
THR HG21   H N N 454 
THR HG22   H N N 455 
THR HG23   H N N 456 
THR HXT    H N N 457 
TRP N      N N N 458 
TRP CA     C N S 459 
TRP C      C N N 460 
TRP O      O N N 461 
TRP CB     C N N 462 
TRP CG     C Y N 463 
TRP CD1    C Y N 464 
TRP CD2    C Y N 465 
TRP NE1    N Y N 466 
TRP CE2    C Y N 467 
TRP CE3    C Y N 468 
TRP CZ2    C Y N 469 
TRP CZ3    C Y N 470 
TRP CH2    C Y N 471 
TRP OXT    O N N 472 
TRP H      H N N 473 
TRP H2     H N N 474 
TRP HA     H N N 475 
TRP HB2    H N N 476 
TRP HB3    H N N 477 
TRP HD1    H N N 478 
TRP HE1    H N N 479 
TRP HE3    H N N 480 
TRP HZ2    H N N 481 
TRP HZ3    H N N 482 
TRP HH2    H N N 483 
TRP HXT    H N N 484 
TYR N      N N N 485 
TYR CA     C N S 486 
TYR C      C N N 487 
TYR O      O N N 488 
TYR CB     C N N 489 
TYR CG     C Y N 490 
TYR CD1    C Y N 491 
TYR CD2    C Y N 492 
TYR CE1    C Y N 493 
TYR CE2    C Y N 494 
TYR CZ     C Y N 495 
TYR OH     O N N 496 
TYR OXT    O N N 497 
TYR H      H N N 498 
TYR H2     H N N 499 
TYR HA     H N N 500 
TYR HB2    H N N 501 
TYR HB3    H N N 502 
TYR HD1    H N N 503 
TYR HD2    H N N 504 
TYR HE1    H N N 505 
TYR HE2    H N N 506 
TYR HH     H N N 507 
TYR HXT    H N N 508 
VAL N      N N N 509 
VAL CA     C N S 510 
VAL C      C N N 511 
VAL O      O N N 512 
VAL CB     C N N 513 
VAL CG1    C N N 514 
VAL CG2    C N N 515 
VAL OXT    O N N 516 
VAL H      H N N 517 
VAL H2     H N N 518 
VAL HA     H N N 519 
VAL HB     H N N 520 
VAL HG11   H N N 521 
VAL HG12   H N N 522 
VAL HG13   H N N 523 
VAL HG21   H N N 524 
VAL HG22   H N N 525 
VAL HG23   H N N 526 
VAL HXT    H N N 527 
# 
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 
5J8 OP3   "P2'"  doub N N 1   
5J8 OP2   "P2'"  sing N N 2   
5J8 OP1   "P2'"  sing N N 3   
5J8 "P2'" "O2'"  sing N N 4   
5J8 "O2'" "C2'"  sing N N 5   
5J8 "C2'" "C3'"  sing N N 6   
5J8 "C2'" "C1'"  sing N N 7   
5J8 OAC   PAA    doub N N 8   
5J8 C2    N1     sing Y N 9   
5J8 C2    N3     doub Y N 10  
5J8 N1    C6     doub Y N 11  
5J8 OAG   PAE    doub N N 12  
5J8 "C3'" "O3'"  sing N N 13  
5J8 "C3'" "C4'"  sing N N 14  
5J8 N3    C4     sing Y N 15  
5J8 C6    N6     sing N N 16  
5J8 C6    C5     sing Y N 17  
5J8 OBV   CBT    doub N N 18  
5J8 CBS   CBR    sing N N 19  
5J8 CBS   CBN    sing N N 20  
5J8 CBR   CBT    sing N N 21  
5J8 CBR   CBQ    doub N N 22  
5J8 C4    C5     doub Y N 23  
5J8 C4    N9     sing Y N 24  
5J8 CBN   CBO    sing N N 25  
5J8 C5    N7     sing Y N 26  
5J8 CBT   NBU    sing N N 27  
5J8 CBO   NBP    sing N N 28  
5J8 OBI   CBF    sing N N 29  
5J8 "O5'" PAE    sing N N 30  
5J8 "O5'" "C5'"  sing N N 31  
5J8 N9    "C1'"  sing N N 32  
5J8 N9    C8     sing Y N 33  
5J8 "C1'" "O4'"  sing N N 34  
5J8 N7    C8     doub Y N 35  
5J8 NBP   CBQ    sing N N 36  
5J8 NBP   CBM    sing N N 37  
5J8 PAE   OAD    sing N N 38  
5J8 PAE   OAF    sing N N 39  
5J8 PAA   OAD    sing N N 40  
5J8 PAA   OBL    sing N N 41  
5J8 PAA   OAB    sing N N 42  
5J8 CBF   CBM    sing N N 43  
5J8 CBF   CBE    sing N N 44  
5J8 "C4'" "C5'"  sing N N 45  
5J8 "C4'" "O4'"  sing N N 46  
5J8 OBL   CBK    sing N N 47  
5J8 CBM   OBG    sing N N 48  
5J8 CBE   OBJ    sing N N 49  
5J8 CBE   CBH    sing N N 50  
5J8 OBG   CBH    sing N N 51  
5J8 CBK   CBH    sing N N 52  
5J8 C8    H1     sing N N 53  
5J8 NBU   H2     sing N N 54  
5J8 NBU   H3     sing N N 55  
5J8 CBQ   H5     sing N N 56  
5J8 CBS   H7     sing N N 57  
5J8 CBS   H8     sing N N 58  
5J8 CBN   H9     sing N N 59  
5J8 CBO   H10    sing N N 60  
5J8 CBM   H11    sing N N 61  
5J8 CBF   H12    sing N N 62  
5J8 OBI   H13    sing N N 63  
5J8 CBE   H14    sing N N 64  
5J8 OBJ   H15    sing N N 65  
5J8 CBH   H16    sing N N 66  
5J8 CBK   H17    sing N N 67  
5J8 CBK   H18    sing N N 68  
5J8 OAB   H19    sing N N 69  
5J8 OAF   H20    sing N N 70  
5J8 "C5'" H21    sing N N 71  
5J8 "C5'" H22    sing N N 72  
5J8 "C4'" H23    sing N N 73  
5J8 "C3'" H24    sing N N 74  
5J8 "O3'" H25    sing N N 75  
5J8 "C2'" H26    sing N N 76  
5J8 OP1   H27    sing N N 77  
5J8 OP2   H28    sing N N 78  
5J8 "C1'" H29    sing N N 79  
5J8 C2    H30    sing N N 80  
5J8 N6    H31    sing N N 81  
5J8 N6    H32    sing N N 82  
5J8 CBN   H4     sing N N 83  
5J8 CBO   H6     sing N N 84  
ALA N     CA     sing N N 85  
ALA N     H      sing N N 86  
ALA N     H2     sing N N 87  
ALA CA    C      sing N N 88  
ALA CA    CB     sing N N 89  
ALA CA    HA     sing N N 90  
ALA C     O      doub N N 91  
ALA C     OXT    sing N N 92  
ALA CB    HB1    sing N N 93  
ALA CB    HB2    sing N N 94  
ALA CB    HB3    sing N N 95  
ALA OXT   HXT    sing N N 96  
ARG N     CA     sing N N 97  
ARG N     H      sing N N 98  
ARG N     H2     sing N N 99  
ARG CA    C      sing N N 100 
ARG CA    CB     sing N N 101 
ARG CA    HA     sing N N 102 
ARG C     O      doub N N 103 
ARG C     OXT    sing N N 104 
ARG CB    CG     sing N N 105 
ARG CB    HB2    sing N N 106 
ARG CB    HB3    sing N N 107 
ARG CG    CD     sing N N 108 
ARG CG    HG2    sing N N 109 
ARG CG    HG3    sing N N 110 
ARG CD    NE     sing N N 111 
ARG CD    HD2    sing N N 112 
ARG CD    HD3    sing N N 113 
ARG NE    CZ     sing N N 114 
ARG NE    HE     sing N N 115 
ARG CZ    NH1    sing N N 116 
ARG CZ    NH2    doub N N 117 
ARG NH1   HH11   sing N N 118 
ARG NH1   HH12   sing N N 119 
ARG NH2   HH21   sing N N 120 
ARG NH2   HH22   sing N N 121 
ARG OXT   HXT    sing N N 122 
ASN N     CA     sing N N 123 
ASN N     H      sing N N 124 
ASN N     H2     sing N N 125 
ASN CA    C      sing N N 126 
ASN CA    CB     sing N N 127 
ASN CA    HA     sing N N 128 
ASN C     O      doub N N 129 
ASN C     OXT    sing N N 130 
ASN CB    CG     sing N N 131 
ASN CB    HB2    sing N N 132 
ASN CB    HB3    sing N N 133 
ASN CG    OD1    doub N N 134 
ASN CG    ND2    sing N N 135 
ASN ND2   HD21   sing N N 136 
ASN ND2   HD22   sing N N 137 
ASN OXT   HXT    sing N N 138 
ASP N     CA     sing N N 139 
ASP N     H      sing N N 140 
ASP N     H2     sing N N 141 
ASP CA    C      sing N N 142 
ASP CA    CB     sing N N 143 
ASP CA    HA     sing N N 144 
ASP C     O      doub N N 145 
ASP C     OXT    sing N N 146 
ASP CB    CG     sing N N 147 
ASP CB    HB2    sing N N 148 
ASP CB    HB3    sing N N 149 
ASP CG    OD1    doub N N 150 
ASP CG    OD2    sing N N 151 
ASP OD2   HD2    sing N N 152 
ASP OXT   HXT    sing N N 153 
CYS N     CA     sing N N 154 
CYS N     H      sing N N 155 
CYS N     H2     sing N N 156 
CYS CA    C      sing N N 157 
CYS CA    CB     sing N N 158 
CYS CA    HA     sing N N 159 
CYS C     O      doub N N 160 
CYS C     OXT    sing N N 161 
CYS CB    SG     sing N N 162 
CYS CB    HB2    sing N N 163 
CYS CB    HB3    sing N N 164 
CYS SG    HG     sing N N 165 
CYS OXT   HXT    sing N N 166 
FMN N1    C2     sing N N 167 
FMN N1    C10    doub N N 168 
FMN C2    O2     doub N N 169 
FMN C2    N3     sing N N 170 
FMN N3    C4     sing N N 171 
FMN N3    HN3    sing N N 172 
FMN C4    O4     doub N N 173 
FMN C4    C4A    sing N N 174 
FMN C4A   N5     doub N N 175 
FMN C4A   C10    sing N N 176 
FMN N5    C5A    sing N N 177 
FMN C5A   C6     doub Y N 178 
FMN C5A   C9A    sing Y N 179 
FMN C6    C7     sing Y N 180 
FMN C6    H6     sing N N 181 
FMN C7    C7M    sing N N 182 
FMN C7    C8     doub Y N 183 
FMN C7M   HM71   sing N N 184 
FMN C7M   HM72   sing N N 185 
FMN C7M   HM73   sing N N 186 
FMN C8    C8M    sing N N 187 
FMN C8    C9     sing Y N 188 
FMN C8M   HM81   sing N N 189 
FMN C8M   HM82   sing N N 190 
FMN C8M   HM83   sing N N 191 
FMN C9    C9A    doub Y N 192 
FMN C9    H9     sing N N 193 
FMN C9A   N10    sing N N 194 
FMN N10   C10    sing N N 195 
FMN N10   "C1'"  sing N N 196 
FMN "C1'" "C2'"  sing N N 197 
FMN "C1'" "H1'1" sing N N 198 
FMN "C1'" "H1'2" sing N N 199 
FMN "C2'" "O2'"  sing N N 200 
FMN "C2'" "C3'"  sing N N 201 
FMN "C2'" "H2'"  sing N N 202 
FMN "O2'" "HO2'" sing N N 203 
FMN "C3'" "O3'"  sing N N 204 
FMN "C3'" "C4'"  sing N N 205 
FMN "C3'" "H3'"  sing N N 206 
FMN "O3'" "HO3'" sing N N 207 
FMN "C4'" "O4'"  sing N N 208 
FMN "C4'" "C5'"  sing N N 209 
FMN "C4'" "H4'"  sing N N 210 
FMN "O4'" "HO4'" sing N N 211 
FMN "C5'" "O5'"  sing N N 212 
FMN "C5'" "H5'1" sing N N 213 
FMN "C5'" "H5'2" sing N N 214 
FMN "O5'" P      sing N N 215 
FMN P     O1P    doub N N 216 
FMN P     O2P    sing N N 217 
FMN P     O3P    sing N N 218 
FMN O2P   HOP2   sing N N 219 
FMN O3P   HOP3   sing N N 220 
GLN N     CA     sing N N 221 
GLN N     H      sing N N 222 
GLN N     H2     sing N N 223 
GLN CA    C      sing N N 224 
GLN CA    CB     sing N N 225 
GLN CA    HA     sing N N 226 
GLN C     O      doub N N 227 
GLN C     OXT    sing N N 228 
GLN CB    CG     sing N N 229 
GLN CB    HB2    sing N N 230 
GLN CB    HB3    sing N N 231 
GLN CG    CD     sing N N 232 
GLN CG    HG2    sing N N 233 
GLN CG    HG3    sing N N 234 
GLN CD    OE1    doub N N 235 
GLN CD    NE2    sing N N 236 
GLN NE2   HE21   sing N N 237 
GLN NE2   HE22   sing N N 238 
GLN OXT   HXT    sing N N 239 
GLU N     CA     sing N N 240 
GLU N     H      sing N N 241 
GLU N     H2     sing N N 242 
GLU CA    C      sing N N 243 
GLU CA    CB     sing N N 244 
GLU CA    HA     sing N N 245 
GLU C     O      doub N N 246 
GLU C     OXT    sing N N 247 
GLU CB    CG     sing N N 248 
GLU CB    HB2    sing N N 249 
GLU CB    HB3    sing N N 250 
GLU CG    CD     sing N N 251 
GLU CG    HG2    sing N N 252 
GLU CG    HG3    sing N N 253 
GLU CD    OE1    doub N N 254 
GLU CD    OE2    sing N N 255 
GLU OE2   HE2    sing N N 256 
GLU OXT   HXT    sing N N 257 
GLY N     CA     sing N N 258 
GLY N     H      sing N N 259 
GLY N     H2     sing N N 260 
GLY CA    C      sing N N 261 
GLY CA    HA2    sing N N 262 
GLY CA    HA3    sing N N 263 
GLY C     O      doub N N 264 
GLY C     OXT    sing N N 265 
GLY OXT   HXT    sing N N 266 
HIS N     CA     sing N N 267 
HIS N     H      sing N N 268 
HIS N     H2     sing N N 269 
HIS CA    C      sing N N 270 
HIS CA    CB     sing N N 271 
HIS CA    HA     sing N N 272 
HIS C     O      doub N N 273 
HIS C     OXT    sing N N 274 
HIS CB    CG     sing N N 275 
HIS CB    HB2    sing N N 276 
HIS CB    HB3    sing N N 277 
HIS CG    ND1    sing Y N 278 
HIS CG    CD2    doub Y N 279 
HIS ND1   CE1    doub Y N 280 
HIS ND1   HD1    sing N N 281 
HIS CD2   NE2    sing Y N 282 
HIS CD2   HD2    sing N N 283 
HIS CE1   NE2    sing Y N 284 
HIS CE1   HE1    sing N N 285 
HIS NE2   HE2    sing N N 286 
HIS OXT   HXT    sing N N 287 
HOH O     H1     sing N N 288 
HOH O     H2     sing N N 289 
ILE N     CA     sing N N 290 
ILE N     H      sing N N 291 
ILE N     H2     sing N N 292 
ILE CA    C      sing N N 293 
ILE CA    CB     sing N N 294 
ILE CA    HA     sing N N 295 
ILE C     O      doub N N 296 
ILE C     OXT    sing N N 297 
ILE CB    CG1    sing N N 298 
ILE CB    CG2    sing N N 299 
ILE CB    HB     sing N N 300 
ILE CG1   CD1    sing N N 301 
ILE CG1   HG12   sing N N 302 
ILE CG1   HG13   sing N N 303 
ILE CG2   HG21   sing N N 304 
ILE CG2   HG22   sing N N 305 
ILE CG2   HG23   sing N N 306 
ILE CD1   HD11   sing N N 307 
ILE CD1   HD12   sing N N 308 
ILE CD1   HD13   sing N N 309 
ILE OXT   HXT    sing N N 310 
LEU N     CA     sing N N 311 
LEU N     H      sing N N 312 
LEU N     H2     sing N N 313 
LEU CA    C      sing N N 314 
LEU CA    CB     sing N N 315 
LEU CA    HA     sing N N 316 
LEU C     O      doub N N 317 
LEU C     OXT    sing N N 318 
LEU CB    CG     sing N N 319 
LEU CB    HB2    sing N N 320 
LEU CB    HB3    sing N N 321 
LEU CG    CD1    sing N N 322 
LEU CG    CD2    sing N N 323 
LEU CG    HG     sing N N 324 
LEU CD1   HD11   sing N N 325 
LEU CD1   HD12   sing N N 326 
LEU CD1   HD13   sing N N 327 
LEU CD2   HD21   sing N N 328 
LEU CD2   HD22   sing N N 329 
LEU CD2   HD23   sing N N 330 
LEU OXT   HXT    sing N N 331 
LYS N     CA     sing N N 332 
LYS N     H      sing N N 333 
LYS N     H2     sing N N 334 
LYS CA    C      sing N N 335 
LYS CA    CB     sing N N 336 
LYS CA    HA     sing N N 337 
LYS C     O      doub N N 338 
LYS C     OXT    sing N N 339 
LYS CB    CG     sing N N 340 
LYS CB    HB2    sing N N 341 
LYS CB    HB3    sing N N 342 
LYS CG    CD     sing N N 343 
LYS CG    HG2    sing N N 344 
LYS CG    HG3    sing N N 345 
LYS CD    CE     sing N N 346 
LYS CD    HD2    sing N N 347 
LYS CD    HD3    sing N N 348 
LYS CE    NZ     sing N N 349 
LYS CE    HE2    sing N N 350 
LYS CE    HE3    sing N N 351 
LYS NZ    HZ1    sing N N 352 
LYS NZ    HZ2    sing N N 353 
LYS NZ    HZ3    sing N N 354 
LYS OXT   HXT    sing N N 355 
MET N     CA     sing N N 356 
MET N     H      sing N N 357 
MET N     H2     sing N N 358 
MET CA    C      sing N N 359 
MET CA    CB     sing N N 360 
MET CA    HA     sing N N 361 
MET C     O      doub N N 362 
MET C     OXT    sing N N 363 
MET CB    CG     sing N N 364 
MET CB    HB2    sing N N 365 
MET CB    HB3    sing N N 366 
MET CG    SD     sing N N 367 
MET CG    HG2    sing N N 368 
MET CG    HG3    sing N N 369 
MET SD    CE     sing N N 370 
MET CE    HE1    sing N N 371 
MET CE    HE2    sing N N 372 
MET CE    HE3    sing N N 373 
MET OXT   HXT    sing N N 374 
PHE N     CA     sing N N 375 
PHE N     H      sing N N 376 
PHE N     H2     sing N N 377 
PHE CA    C      sing N N 378 
PHE CA    CB     sing N N 379 
PHE CA    HA     sing N N 380 
PHE C     O      doub N N 381 
PHE C     OXT    sing N N 382 
PHE CB    CG     sing N N 383 
PHE CB    HB2    sing N N 384 
PHE CB    HB3    sing N N 385 
PHE CG    CD1    doub Y N 386 
PHE CG    CD2    sing Y N 387 
PHE CD1   CE1    sing Y N 388 
PHE CD1   HD1    sing N N 389 
PHE CD2   CE2    doub Y N 390 
PHE CD2   HD2    sing N N 391 
PHE CE1   CZ     doub Y N 392 
PHE CE1   HE1    sing N N 393 
PHE CE2   CZ     sing Y N 394 
PHE CE2   HE2    sing N N 395 
PHE CZ    HZ     sing N N 396 
PHE OXT   HXT    sing N N 397 
PRO N     CA     sing N N 398 
PRO N     CD     sing N N 399 
PRO N     H      sing N N 400 
PRO CA    C      sing N N 401 
PRO CA    CB     sing N N 402 
PRO CA    HA     sing N N 403 
PRO C     O      doub N N 404 
PRO C     OXT    sing N N 405 
PRO CB    CG     sing N N 406 
PRO CB    HB2    sing N N 407 
PRO CB    HB3    sing N N 408 
PRO CG    CD     sing N N 409 
PRO CG    HG2    sing N N 410 
PRO CG    HG3    sing N N 411 
PRO CD    HD2    sing N N 412 
PRO CD    HD3    sing N N 413 
PRO OXT   HXT    sing N N 414 
SER N     CA     sing N N 415 
SER N     H      sing N N 416 
SER N     H2     sing N N 417 
SER CA    C      sing N N 418 
SER CA    CB     sing N N 419 
SER CA    HA     sing N N 420 
SER C     O      doub N N 421 
SER C     OXT    sing N N 422 
SER CB    OG     sing N N 423 
SER CB    HB2    sing N N 424 
SER CB    HB3    sing N N 425 
SER OG    HG     sing N N 426 
SER OXT   HXT    sing N N 427 
SO4 S     O1     doub N N 428 
SO4 S     O2     doub N N 429 
SO4 S     O3     sing N N 430 
SO4 S     O4     sing N N 431 
THR N     CA     sing N N 432 
THR N     H      sing N N 433 
THR N     H2     sing N N 434 
THR CA    C      sing N N 435 
THR CA    CB     sing N N 436 
THR CA    HA     sing N N 437 
THR C     O      doub N N 438 
THR C     OXT    sing N N 439 
THR CB    OG1    sing N N 440 
THR CB    CG2    sing N N 441 
THR CB    HB     sing N N 442 
THR OG1   HG1    sing N N 443 
THR CG2   HG21   sing N N 444 
THR CG2   HG22   sing N N 445 
THR CG2   HG23   sing N N 446 
THR OXT   HXT    sing N N 447 
TRP N     CA     sing N N 448 
TRP N     H      sing N N 449 
TRP N     H2     sing N N 450 
TRP CA    C      sing N N 451 
TRP CA    CB     sing N N 452 
TRP CA    HA     sing N N 453 
TRP C     O      doub N N 454 
TRP C     OXT    sing N N 455 
TRP CB    CG     sing N N 456 
TRP CB    HB2    sing N N 457 
TRP CB    HB3    sing N N 458 
TRP CG    CD1    doub Y N 459 
TRP CG    CD2    sing Y N 460 
TRP CD1   NE1    sing Y N 461 
TRP CD1   HD1    sing N N 462 
TRP CD2   CE2    doub Y N 463 
TRP CD2   CE3    sing Y N 464 
TRP NE1   CE2    sing Y N 465 
TRP NE1   HE1    sing N N 466 
TRP CE2   CZ2    sing Y N 467 
TRP CE3   CZ3    doub Y N 468 
TRP CE3   HE3    sing N N 469 
TRP CZ2   CH2    doub Y N 470 
TRP CZ2   HZ2    sing N N 471 
TRP CZ3   CH2    sing Y N 472 
TRP CZ3   HZ3    sing N N 473 
TRP CH2   HH2    sing N N 474 
TRP OXT   HXT    sing N N 475 
TYR N     CA     sing N N 476 
TYR N     H      sing N N 477 
TYR N     H2     sing N N 478 
TYR CA    C      sing N N 479 
TYR CA    CB     sing N N 480 
TYR CA    HA     sing N N 481 
TYR C     O      doub N N 482 
TYR C     OXT    sing N N 483 
TYR CB    CG     sing N N 484 
TYR CB    HB2    sing N N 485 
TYR CB    HB3    sing N N 486 
TYR CG    CD1    doub Y N 487 
TYR CG    CD2    sing Y N 488 
TYR CD1   CE1    sing Y N 489 
TYR CD1   HD1    sing N N 490 
TYR CD2   CE2    doub Y N 491 
TYR CD2   HD2    sing N N 492 
TYR CE1   CZ     doub Y N 493 
TYR CE1   HE1    sing N N 494 
TYR CE2   CZ     sing Y N 495 
TYR CE2   HE2    sing N N 496 
TYR CZ    OH     sing N N 497 
TYR OH    HH     sing N N 498 
TYR OXT   HXT    sing N N 499 
VAL N     CA     sing N N 500 
VAL N     H      sing N N 501 
VAL N     H2     sing N N 502 
VAL CA    C      sing N N 503 
VAL CA    CB     sing N N 504 
VAL CA    HA     sing N N 505 
VAL C     O      doub N N 506 
VAL C     OXT    sing N N 507 
VAL CB    CG1    sing N N 508 
VAL CB    CG2    sing N N 509 
VAL CB    HB     sing N N 510 
VAL CG1   HG11   sing N N 511 
VAL CG1   HG12   sing N N 512 
VAL CG1   HG13   sing N N 513 
VAL CG2   HG21   sing N N 514 
VAL CG2   HG22   sing N N 515 
VAL CG2   HG23   sing N N 516 
VAL OXT   HXT    sing N N 517 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2hs6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QO7 
_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]   0.011312 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011078 
_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]   0.020210 
_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 
C 
N 
O 
P 
S 
# 
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     . ASN A 1 16  ? 36.985 9.961  0.847  1.00 28.70  ? 10   ASN A N     1 
ATOM   2    C CA    . ASN A 1 16  ? 36.662 10.469 2.196  1.00 24.09  ? 10   ASN A CA    1 
ATOM   3    C C     . ASN A 1 16  ? 35.216 10.103 2.540  1.00 19.73  ? 10   ASN A C     1 
ATOM   4    O O     . ASN A 1 16  ? 34.269 10.530 1.875  1.00 19.65  ? 10   ASN A O     1 
ATOM   5    C CB    . ASN A 1 16  ? 36.871 11.982 2.216  1.00 26.79  ? 10   ASN A CB    1 
ATOM   6    C CG    . ASN A 1 16  ? 36.640 12.605 3.566  1.00 22.12  ? 10   ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 16  ? 35.932 12.067 4.408  1.00 21.05  ? 10   ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 16  ? 37.164 13.822 3.749  1.00 24.30  ? 10   ASN A ND2   1 
ATOM   9    N N     . PRO A 1 17  ? 35.024 9.263  3.558  1.00 19.81  ? 11   PRO A N     1 
ATOM   10   C CA    . PRO A 1 17  ? 33.666 8.770  3.821  1.00 20.94  ? 11   PRO A CA    1 
ATOM   11   C C     . PRO A 1 17  ? 32.717 9.851  4.351  1.00 15.82  ? 11   PRO A C     1 
ATOM   12   O O     . PRO A 1 17  ? 31.475 9.646  4.259  1.00 16.08  ? 11   PRO A O     1 
ATOM   13   C CB    . PRO A 1 17  ? 33.872 7.675  4.866  1.00 22.72  ? 11   PRO A CB    1 
ATOM   14   C CG    . PRO A 1 17  ? 35.112 8.100  5.557  1.00 22.94  ? 11   PRO A CG    1 
ATOM   15   C CD    . PRO A 1 17  ? 36.020 8.691  4.486  1.00 22.97  ? 11   PRO A CD    1 
ATOM   16   N N     . LEU A 1 18  ? 33.259 10.973 4.847  1.00 16.29  ? 12   LEU A N     1 
ATOM   17   C CA    . LEU A 1 18  ? 32.382 12.084 5.192  1.00 15.89  ? 12   LEU A CA    1 
ATOM   18   C C     . LEU A 1 18  ? 31.674 12.653 3.983  1.00 15.87  ? 12   LEU A C     1 
ATOM   19   O O     . LEU A 1 18  ? 30.699 13.399 4.134  1.00 14.99  ? 12   LEU A O     1 
ATOM   20   C CB    . LEU A 1 18  ? 33.136 13.233 5.852  1.00 16.30  ? 12   LEU A CB    1 
ATOM   21   C CG    . LEU A 1 18  ? 33.628 12.907 7.239  1.00 15.90  ? 12   LEU A CG    1 
ATOM   22   C CD1   . LEU A 1 18  ? 34.530 14.035 7.756  1.00 17.50  ? 12   LEU A CD1   1 
ATOM   23   C CD2   . LEU A 1 18  ? 32.416 12.690 8.204  1.00 17.36  ? 12   LEU A CD2   1 
ATOM   24   N N     . PHE A 1 19  ? 32.138 12.350 2.770  1.00 14.48  ? 13   PHE A N     1 
ATOM   25   C CA    . PHE A 1 19  ? 31.551 12.857 1.544  1.00 14.83  ? 13   PHE A CA    1 
ATOM   26   C C     . PHE A 1 19  ? 30.811 11.777 0.790  1.00 16.30  ? 13   PHE A C     1 
ATOM   27   O O     . PHE A 1 19  ? 30.510 11.934 -0.392 1.00 19.70  ? 13   PHE A O     1 
ATOM   28   C CB    . PHE A 1 19  ? 32.585 13.638 0.705  1.00 15.15  ? 13   PHE A CB    1 
ATOM   29   C CG    . PHE A 1 19  ? 32.928 14.923 1.392  1.00 16.58  ? 13   PHE A CG    1 
ATOM   30   C CD1   . PHE A 1 19  ? 33.899 14.943 2.366  1.00 17.85  ? 13   PHE A CD1   1 
ATOM   31   C CD2   . PHE A 1 19  ? 32.115 16.057 1.222  1.00 16.36  ? 13   PHE A CD2   1 
ATOM   32   C CE1   . PHE A 1 19  ? 34.138 16.092 3.135  1.00 23.62  ? 13   PHE A CE1   1 
ATOM   33   C CE2   . PHE A 1 19  ? 32.353 17.208 1.974  1.00 17.43  ? 13   PHE A CE2   1 
ATOM   34   C CZ    . PHE A 1 19  ? 33.369 17.219 2.931  1.00 17.12  ? 13   PHE A CZ    1 
ATOM   35   N N     . SER A 1 20  ? 30.450 10.722 1.463  1.00 17.30  ? 14   SER A N     1 
ATOM   36   C CA    . SER A 1 20  ? 29.501 9.856  0.791  1.00 16.82  ? 14   SER A CA    1 
ATOM   37   C C     . SER A 1 20  ? 28.075 10.269 1.127  1.00 18.79  ? 14   SER A C     1 
ATOM   38   O O     . SER A 1 20  ? 27.790 10.680 2.276  1.00 16.85  ? 14   SER A O     1 
ATOM   39   C CB    . SER A 1 20  ? 29.722 8.404  1.142  1.00 25.89  ? 14   SER A CB    1 
ATOM   40   O OG    . SER A 1 20  ? 29.572 8.220  2.482  1.00 26.99  ? 14   SER A OG    1 
ATOM   41   N N     . PRO A 1 21  ? 27.158 10.194 0.190  1.00 14.06  ? 15   PRO A N     1 
ATOM   42   C CA    . PRO A 1 21  ? 25.792 10.654 0.424  1.00 15.26  ? 15   PRO A CA    1 
ATOM   43   C C     . PRO A 1 21  ? 25.128 9.748  1.450  1.00 15.61  ? 15   PRO A C     1 
ATOM   44   O O     . PRO A 1 21  ? 25.518 8.596  1.700  1.00 17.69  ? 15   PRO A O     1 
ATOM   45   C CB    . PRO A 1 21  ? 25.115 10.495 -0.944 1.00 18.24  ? 15   PRO A CB    1 
ATOM   46   C CG    . PRO A 1 21  ? 25.997 9.451  -1.677 1.00 26.06  ? 15   PRO A CG    1 
ATOM   47   C CD    . PRO A 1 21  ? 27.387 9.744  -1.204 1.00 18.60  ? 15   PRO A CD    1 
ATOM   48   N N     . TYR A 1 22  ? 24.123 10.321 2.102  1.00 16.09  ? 16   TYR A N     1 
ATOM   49   C CA    . TYR A 1 22  ? 23.400 9.583  3.123  1.00 13.56  ? 16   TYR A CA    1 
ATOM   50   C C     . TYR A 1 22  ? 21.948 10.027 3.085  1.00 14.15  ? 16   TYR A C     1 
ATOM   51   O O     . TYR A 1 22  ? 21.666 11.230 3.002  1.00 15.99  ? 16   TYR A O     1 
ATOM   52   C CB    . TYR A 1 22  ? 23.964 9.936  4.518  1.00 14.40  ? 16   TYR A CB    1 
ATOM   53   C CG    . TYR A 1 22  ? 23.273 9.098  5.577  1.00 14.56  ? 16   TYR A CG    1 
ATOM   54   C CD1   . TYR A 1 22  ? 23.586 7.765  5.762  1.00 15.36  ? 16   TYR A CD1   1 
ATOM   55   C CD2   . TYR A 1 22  ? 22.274 9.661  6.415  1.00 14.51  ? 16   TYR A CD2   1 
ATOM   56   C CE1   . TYR A 1 22  ? 22.923 7.001  6.674  1.00 14.64  ? 16   TYR A CE1   1 
ATOM   57   C CE2   . TYR A 1 22  ? 21.615 8.890  7.339  1.00 15.44  ? 16   TYR A CE2   1 
ATOM   58   C CZ    . TYR A 1 22  ? 21.943 7.546  7.459  1.00 14.71  ? 16   TYR A CZ    1 
ATOM   59   O OH    . TYR A 1 22  ? 21.332 6.759  8.411  1.00 15.74  ? 16   TYR A OH    1 
ATOM   60   N N     . LYS A 1 23  ? 21.020 9.099  3.197  1.00 15.16  ? 17   LYS A N     1 
ATOM   61   C CA    . LYS A 1 23  ? 19.594 9.375  3.146  1.00 15.97  ? 17   LYS A CA    1 
ATOM   62   C C     . LYS A 1 23  ? 19.049 9.437  4.591  1.00 16.79  ? 17   LYS A C     1 
ATOM   63   O O     . LYS A 1 23  ? 18.961 8.414  5.294  1.00 20.68  ? 17   LYS A O     1 
ATOM   64   C CB    . LYS A 1 23  ? 18.976 8.243  2.332  1.00 22.94  ? 17   LYS A CB    1 
ATOM   65   C CG    . LYS A 1 23  ? 17.567 7.974  2.607  1.00 38.35  ? 17   LYS A CG    1 
ATOM   66   C CD    . LYS A 1 23  ? 16.762 9.036  2.038  1.00 31.53  ? 17   LYS A CD    1 
ATOM   67   C CE    . LYS A 1 23  ? 16.049 8.654  0.742  1.00 44.03  ? 17   LYS A CE    1 
ATOM   68   N NZ    . LYS A 1 23  ? 15.108 9.800  0.441  1.00 37.20  ? 17   LYS A NZ    1 
ATOM   69   N N     . MET A 1 24  ? 18.778 10.651 5.070  1.00 15.36  ? 18   MET A N     1 
ATOM   70   C CA    . MET A 1 24  ? 18.261 10.861 6.421  1.00 15.71  ? 18   MET A CA    1 
ATOM   71   C C     . MET A 1 24  ? 16.764 10.937 6.249  1.00 18.51  ? 18   MET A C     1 
ATOM   72   O O     . MET A 1 24  ? 16.199 12.009 6.074  1.00 19.32  ? 18   MET A O     1 
ATOM   73   C CB    . MET A 1 24  ? 18.836 12.141 7.003  1.00 17.20  ? 18   MET A CB    1 
ATOM   74   C CG    . MET A 1 24  ? 18.442 12.390 8.476  1.00 17.43  ? 18   MET A CG    1 
ATOM   75   S SD    . MET A 1 24  ? 19.218 13.863 9.153  1.00 18.73  ? 18   MET A SD    1 
ATOM   76   C CE    . MET A 1 24  ? 18.354 15.213 8.291  1.00 17.56  ? 18   MET A CE    1 
ATOM   77   N N     . GLY A 1 25  ? 16.175 9.720  6.081  1.00 23.38  ? 19   GLY A N     1 
ATOM   78   C CA    . GLY A 1 25  ? 14.758 9.548  5.817  1.00 25.94  ? 19   GLY A CA    1 
ATOM   79   C C     . GLY A 1 25  ? 14.323 10.267 4.585  1.00 22.81  ? 19   GLY A C     1 
ATOM   80   O O     . GLY A 1 25  ? 14.766 9.882  3.526  1.00 29.56  ? 19   GLY A O     1 
ATOM   81   N N     . LYS A 1 26  ? 13.530 11.356 4.649  1.00 25.58  ? 20   LYS A N     1 
ATOM   82   C CA    . LYS A 1 26  ? 13.160 11.929 3.353  1.00 22.65  ? 20   LYS A CA    1 
ATOM   83   C C     . LYS A 1 26  ? 14.240 12.827 2.757  1.00 18.07  ? 20   LYS A C     1 
ATOM   84   O O     . LYS A 1 26  ? 14.138 13.168 1.576  1.00 22.67  ? 20   LYS A O     1 
ATOM   85   C CB    . LYS A 1 26  ? 11.835 12.715 3.398  1.00 30.06  ? 20   LYS A CB    1 
ATOM   86   N N     . PHE A 1 27  ? 15.318 13.117 3.477  1.00 15.46  ? 21   PHE A N     1 
ATOM   87   C CA    . PHE A 1 27  ? 16.302 14.098 3.049  1.00 16.63  ? 21   PHE A CA    1 
ATOM   88   C C     . PHE A 1 27  ? 17.532 13.408 2.464  1.00 14.80  ? 21   PHE A C     1 
ATOM   89   O O     . PHE A 1 27  ? 18.219 12.635 3.128  1.00 17.54  ? 21   PHE A O     1 
ATOM   90   C CB    . PHE A 1 27  ? 16.700 14.933 4.280  1.00 17.38  ? 21   PHE A CB    1 
ATOM   91   C CG    . PHE A 1 27  ? 15.489 15.588 4.955  1.00 20.14  ? 21   PHE A CG    1 
ATOM   92   C CD1   . PHE A 1 27  ? 14.779 16.546 4.277  1.00 18.91  ? 21   PHE A CD1   1 
ATOM   93   C CD2   . PHE A 1 27  ? 15.044 15.165 6.210  1.00 20.84  ? 21   PHE A CD2   1 
ATOM   94   C CE1   . PHE A 1 27  ? 13.609 17.117 4.847  1.00 20.91  ? 21   PHE A CE1   1 
ATOM   95   C CE2   . PHE A 1 27  ? 13.915 15.723 6.786  1.00 22.02  ? 21   PHE A CE2   1 
ATOM   96   C CZ    . PHE A 1 27  ? 13.184 16.697 6.089  1.00 23.64  ? 21   PHE A CZ    1 
ATOM   97   N N     . ASN A 1 28  ? 17.871 13.746 1.249  1.00 16.00  ? 22   ASN A N     1 
ATOM   98   C CA    . ASN A 1 28  ? 19.071 13.200 0.597  1.00 16.11  ? 22   ASN A CA    1 
ATOM   99   C C     . ASN A 1 28  ? 20.235 14.138 0.896  1.00 14.74  ? 22   ASN A C     1 
ATOM   100  O O     . ASN A 1 28  ? 20.383 15.195 0.262  1.00 18.23  ? 22   ASN A O     1 
ATOM   101  C CB    . ASN A 1 28  ? 18.841 13.170 -0.911 1.00 16.62  ? 22   ASN A CB    1 
ATOM   102  C CG    . ASN A 1 28  ? 17.729 12.218 -1.300 1.00 20.05  ? 22   ASN A CG    1 
ATOM   103  O OD1   . ASN A 1 28  ? 17.691 11.075 -0.820 1.00 21.50  ? 22   ASN A OD1   1 
ATOM   104  N ND2   . ASN A 1 28  ? 16.741 12.733 -2.049 1.00 24.88  ? 22   ASN A ND2   1 
ATOM   105  N N     . LEU A 1 29  ? 21.119 13.734 1.809  1.00 12.98  ? 23   LEU A N     1 
ATOM   106  C CA    . LEU A 1 29  ? 22.271 14.559 2.163  1.00 12.43  ? 23   LEU A CA    1 
ATOM   107  C C     . LEU A 1 29  ? 23.462 14.218 1.286  1.00 12.62  ? 23   LEU A C     1 
ATOM   108  O O     . LEU A 1 29  ? 23.659 13.054 0.894  1.00 13.78  ? 23   LEU A O     1 
ATOM   109  C CB    . LEU A 1 29  ? 22.653 14.334 3.617  1.00 12.54  ? 23   LEU A CB    1 
ATOM   110  C CG    . LEU A 1 29  ? 21.546 14.627 4.615  1.00 10.30  ? 23   LEU A CG    1 
ATOM   111  C CD1   . LEU A 1 29  ? 22.080 14.393 6.030  1.00 13.19  ? 23   LEU A CD1   1 
ATOM   112  C CD2   . LEU A 1 29  ? 21.002 16.050 4.473  1.00 12.81  ? 23   LEU A CD2   1 
ATOM   113  N N     . SER A 1 30  ? 24.214 15.215 0.900  1.00 12.13  ? 24   SER A N     1 
ATOM   114  C CA    A SER A 1 30  ? 25.366 14.973 0.035  0.54 12.82  ? 24   SER A CA    1 
ATOM   115  C CA    B SER A 1 30  ? 25.376 15.016 0.034  0.46 12.83  ? 24   SER A CA    1 
ATOM   116  C C     . SER A 1 30  ? 26.645 14.692 0.804  1.00 13.55  ? 24   SER A C     1 
ATOM   117  O O     . SER A 1 30  ? 27.620 14.192 0.210  1.00 14.48  ? 24   SER A O     1 
ATOM   118  C CB    A SER A 1 30  ? 25.631 16.177 -0.868 0.54 12.65  ? 24   SER A CB    1 
ATOM   119  C CB    B SER A 1 30  ? 25.640 16.263 -0.833 0.46 12.65  ? 24   SER A CB    1 
ATOM   120  O OG    A SER A 1 30  ? 25.941 17.288 -0.069 0.54 15.12  ? 24   SER A OG    1 
ATOM   121  O OG    B SER A 1 30  ? 24.516 16.574 -1.647 0.46 15.44  ? 24   SER A OG    1 
ATOM   122  N N     . HIS A 1 31  ? 26.665 14.978 2.098  1.00 12.06  ? 25   HIS A N     1 
ATOM   123  C CA    . HIS A 1 31  ? 27.831 14.733 2.914  1.00 12.74  ? 25   HIS A CA    1 
ATOM   124  C C     . HIS A 1 31  ? 27.353 14.670 4.361  1.00 12.12  ? 25   HIS A C     1 
ATOM   125  O O     . HIS A 1 31  ? 26.181 14.939 4.647  1.00 11.78  ? 25   HIS A O     1 
ATOM   126  C CB    . HIS A 1 31  ? 28.920 15.799 2.748  1.00 12.01  ? 25   HIS A CB    1 
ATOM   127  C CG    . HIS A 1 31  ? 28.473 17.148 3.187  1.00 10.68  ? 25   HIS A CG    1 
ATOM   128  N ND1   . HIS A 1 31  ? 28.356 17.511 4.533  1.00 10.41  ? 25   HIS A ND1   1 
ATOM   129  C CD2   . HIS A 1 31  ? 28.029 18.183 2.443  1.00 10.74  ? 25   HIS A CD2   1 
ATOM   130  C CE1   . HIS A 1 31  ? 27.898 18.756 4.561  1.00 10.20  ? 25   HIS A CE1   1 
ATOM   131  N NE2   . HIS A 1 31  ? 27.680 19.181 3.313  1.00 10.29  ? 25   HIS A NE2   1 
ATOM   132  N N     . ARG A 1 32  ? 28.258 14.247 5.232  1.00 11.59  ? 26   ARG A N     1 
ATOM   133  C CA    . ARG A 1 32  ? 27.900 13.850 6.607  1.00 11.14  ? 26   ARG A CA    1 
ATOM   134  C C     . ARG A 1 32  ? 28.376 14.821 7.654  1.00 11.15  ? 26   ARG A C     1 
ATOM   135  O O     . ARG A 1 32  ? 28.306 14.489 8.839  1.00 11.51  ? 26   ARG A O     1 
ATOM   136  C CB    . ARG A 1 32  ? 28.450 12.437 6.873  1.00 12.09  ? 26   ARG A CB    1 
ATOM   137  C CG    . ARG A 1 32  ? 27.851 11.431 5.850  1.00 16.57  ? 26   ARG A CG    1 
ATOM   138  C CD    . ARG A 1 32  ? 28.594 10.218 5.853  1.00 18.76  ? 26   ARG A CD    1 
ATOM   139  N NE    . ARG A 1 32  ? 27.950 9.317  4.887  1.00 16.70  ? 26   ARG A NE    1 
ATOM   140  C CZ    . ARG A 1 32  ? 27.382 8.169  5.195  1.00 14.58  ? 26   ARG A CZ    1 
ATOM   141  N NH1   . ARG A 1 32  ? 27.104 7.841  6.440  1.00 15.60  ? 26   ARG A NH1   1 
ATOM   142  N NH2   . ARG A 1 32  ? 27.140 7.287  4.217  1.00 15.37  ? 26   ARG A NH2   1 
ATOM   143  N N     . VAL A 1 33  ? 28.826 15.986 7.258  1.00 10.50  ? 27   VAL A N     1 
ATOM   144  C CA    . VAL A 1 33  ? 29.290 17.014 8.179  1.00 10.54  ? 27   VAL A CA    1 
ATOM   145  C C     . VAL A 1 33  ? 28.108 17.880 8.565  1.00 9.83   ? 27   VAL A C     1 
ATOM   146  O O     . VAL A 1 33  ? 27.502 18.530 7.708  1.00 11.69  ? 27   VAL A O     1 
ATOM   147  C CB    . VAL A 1 33  ? 30.398 17.870 7.531  1.00 10.86  ? 27   VAL A CB    1 
ATOM   148  C CG1   . VAL A 1 33  ? 30.888 19.014 8.458  1.00 13.90  ? 27   VAL A CG1   1 
ATOM   149  C CG2   . VAL A 1 33  ? 31.576 16.972 7.141  1.00 15.97  ? 27   VAL A CG2   1 
ATOM   150  N N     . VAL A 1 34  ? 27.736 17.874 9.845  1.00 9.37   ? 28   VAL A N     1 
ATOM   151  C CA    . VAL A 1 34  ? 26.537 18.552 10.333 1.00 9.64   ? 28   VAL A CA    1 
ATOM   152  C C     . VAL A 1 34  ? 26.951 19.740 11.190 1.00 9.33   ? 28   VAL A C     1 
ATOM   153  O O     . VAL A 1 34  ? 27.890 19.642 12.004 1.00 10.19  ? 28   VAL A O     1 
ATOM   154  C CB    . VAL A 1 34  ? 25.719 17.536 11.163 1.00 8.77   ? 28   VAL A CB    1 
ATOM   155  C CG1   . VAL A 1 34  ? 24.472 18.177 11.809 1.00 9.93   ? 28   VAL A CG1   1 
ATOM   156  C CG2   . VAL A 1 34  ? 25.277 16.337 10.276 1.00 10.08  ? 28   VAL A CG2   1 
ATOM   157  N N     . LEU A 1 35  ? 26.206 20.848 11.072 1.00 9.48   ? 29   LEU A N     1 
ATOM   158  C CA    . LEU A 1 35  ? 26.349 21.964 12.021 1.00 7.95   ? 29   LEU A CA    1 
ATOM   159  C C     . LEU A 1 35  ? 25.606 21.598 13.296 1.00 9.14   ? 29   LEU A C     1 
ATOM   160  O O     . LEU A 1 35  ? 24.379 21.475 13.326 1.00 9.84   ? 29   LEU A O     1 
ATOM   161  C CB    . LEU A 1 35  ? 25.783 23.267 11.411 1.00 8.96   ? 29   LEU A CB    1 
ATOM   162  C CG    . LEU A 1 35  ? 25.693 24.447 12.396 1.00 9.11   ? 29   LEU A CG    1 
ATOM   163  C CD1   . LEU A 1 35  ? 27.048 24.958 12.858 1.00 11.48  ? 29   LEU A CD1   1 
ATOM   164  C CD2   . LEU A 1 35  ? 24.916 25.609 11.777 1.00 11.31  ? 29   LEU A CD2   1 
ATOM   165  N N     . ALA A 1 36  ? 26.359 21.442 14.388 1.00 9.11   ? 30   ALA A N     1 
ATOM   166  C CA    . ALA A 1 36  ? 25.749 21.195 15.696 1.00 7.99   ? 30   ALA A CA    1 
ATOM   167  C C     . ALA A 1 36  ? 24.984 22.435 16.158 1.00 8.88   ? 30   ALA A C     1 
ATOM   168  O O     . ALA A 1 36  ? 25.370 23.558 15.852 1.00 9.55   ? 30   ALA A O     1 
ATOM   169  C CB    . ALA A 1 36  ? 26.858 20.866 16.701 1.00 10.35  ? 30   ALA A CB    1 
ATOM   170  N N     . PRO A 1 37  ? 23.962 22.244 16.975 1.00 8.51   ? 31   PRO A N     1 
ATOM   171  C CA    . PRO A 1 37  ? 23.200 23.397 17.526 1.00 7.93   ? 31   PRO A CA    1 
ATOM   172  C C     . PRO A 1 37  ? 24.086 24.196 18.453 1.00 8.71   ? 31   PRO A C     1 
ATOM   173  O O     . PRO A 1 37  ? 24.684 23.635 19.386 1.00 9.27   ? 31   PRO A O     1 
ATOM   174  C CB    . PRO A 1 37  ? 22.061 22.718 18.298 1.00 8.87   ? 31   PRO A CB    1 
ATOM   175  C CG    . PRO A 1 37  ? 22.632 21.309 18.671 1.00 8.60   ? 31   PRO A CG    1 
ATOM   176  C CD    . PRO A 1 37  ? 23.471 20.936 17.468 1.00 8.34   ? 31   PRO A CD    1 
ATOM   177  N N     . MET A 1 38  ? 24.135 25.502 18.251 1.00 8.63   ? 32   MET A N     1 
ATOM   178  C CA    . MET A 1 38  ? 24.943 26.375 19.131 1.00 8.99   ? 32   MET A CA    1 
ATOM   179  C C     . MET A 1 38  ? 24.255 27.686 19.422 1.00 9.59   ? 32   MET A C     1 
ATOM   180  O O     . MET A 1 38  ? 24.066 28.527 18.532 1.00 9.45   ? 32   MET A O     1 
ATOM   181  C CB    . MET A 1 38  ? 26.284 26.691 18.493 1.00 10.93  ? 32   MET A CB    1 
ATOM   182  C CG    . MET A 1 38  ? 27.188 25.437 18.589 1.00 12.59  ? 32   MET A CG    1 
ATOM   183  S SD    . MET A 1 38  ? 28.816 25.827 17.875 1.00 13.28  ? 32   MET A SD    1 
ATOM   184  C CE    . MET A 1 38  ? 28.360 25.996 16.127 1.00 13.89  ? 32   MET A CE    1 
ATOM   185  N N     . THR A 1 39  ? 23.969 27.874 20.690 1.00 9.02   ? 33   THR A N     1 
ATOM   186  C CA    . THR A 1 39  ? 23.514 29.150 21.259 1.00 8.88   ? 33   THR A CA    1 
ATOM   187  C C     . THR A 1 39  ? 24.573 30.235 21.083 1.00 10.34  ? 33   THR A C     1 
ATOM   188  O O     . THR A 1 39  ? 25.709 30.036 21.493 1.00 9.87   ? 33   THR A O     1 
ATOM   189  C CB    . THR A 1 39  ? 23.266 28.914 22.744 1.00 8.76   ? 33   THR A CB    1 
ATOM   190  O OG1   . THR A 1 39  ? 22.145 28.011 22.897 1.00 10.24  ? 33   THR A OG1   1 
ATOM   191  C CG2   . THR A 1 39  ? 22.939 30.191 23.506 1.00 9.77   ? 33   THR A CG2   1 
ATOM   192  N N     . ARG A 1 40  ? 24.193 31.332 20.413 1.00 9.14   ? 34   ARG A N     1 
ATOM   193  C CA    . ARG A 1 40  ? 25.106 32.432 20.152 1.00 8.56   ? 34   ARG A CA    1 
ATOM   194  C C     . ARG A 1 40  ? 24.594 33.764 20.664 1.00 9.71   ? 34   ARG A C     1 
ATOM   195  O O     . ARG A 1 40  ? 25.366 34.731 20.718 1.00 9.65   ? 34   ARG A O     1 
ATOM   196  C CB    . ARG A 1 40  ? 25.448 32.512 18.652 1.00 8.68   ? 34   ARG A CB    1 
ATOM   197  C CG    . ARG A 1 40  ? 25.989 31.188 18.067 1.00 9.79   ? 34   ARG A CG    1 
ATOM   198  C CD    . ARG A 1 40  ? 27.278 30.701 18.695 1.00 10.04  ? 34   ARG A CD    1 
ATOM   199  N NE    . ARG A 1 40  ? 28.326 31.741 18.729 1.00 9.67   ? 34   ARG A NE    1 
ATOM   200  C CZ    . ARG A 1 40  ? 29.039 32.150 17.690 1.00 9.23   ? 34   ARG A CZ    1 
ATOM   201  N NH1   . ARG A 1 40  ? 28.880 31.616 16.485 1.00 9.98   ? 34   ARG A NH1   1 
ATOM   202  N NH2   . ARG A 1 40  ? 29.904 33.166 17.861 1.00 10.72  ? 34   ARG A NH2   1 
ATOM   203  N N     . CYS A 1 41  ? 23.315 33.867 21.036 1.00 8.60   ? 35   CYS A N     1 
ATOM   204  C CA    . CYS A 1 41  ? 22.816 35.058 21.740 1.00 8.21   ? 35   CYS A CA    1 
ATOM   205  C C     . CYS A 1 41  ? 22.793 36.311 20.844 1.00 10.23  ? 35   CYS A C     1 
ATOM   206  O O     . CYS A 1 41  ? 22.915 37.419 21.373 1.00 10.56  ? 35   CYS A O     1 
ATOM   207  C CB    . CYS A 1 41  ? 23.562 35.329 23.072 1.00 9.17   ? 35   CYS A CB    1 
ATOM   208  S SG    . CYS A 1 41  ? 23.662 33.868 24.106 1.00 10.38  ? 35   CYS A SG    1 
ATOM   209  N N     . ARG A 1 42  ? 22.560 36.169 19.528 1.00 8.81   ? 36   ARG A N     1 
ATOM   210  C CA    . ARG A 1 42  ? 22.408 37.345 18.666 1.00 8.39   ? 36   ARG A CA    1 
ATOM   211  C C     . ARG A 1 42  ? 20.964 37.587 18.306 1.00 10.20  ? 36   ARG A C     1 
ATOM   212  O O     . ARG A 1 42  ? 20.689 38.579 17.608 1.00 10.54  ? 36   ARG A O     1 
ATOM   213  C CB    . ARG A 1 42  ? 23.219 37.158 17.382 1.00 9.44   ? 36   ARG A CB    1 
ATOM   214  C CG    . ARG A 1 42  ? 24.672 37.692 17.423 1.00 9.39   ? 36   ARG A CG    1 
ATOM   215  C CD    . ARG A 1 42  ? 25.570 36.820 18.315 1.00 10.57  ? 36   ARG A CD    1 
ATOM   216  N NE    . ARG A 1 42  ? 26.952 37.310 18.208 1.00 9.24   ? 36   ARG A NE    1 
ATOM   217  C CZ    . ARG A 1 42  ? 27.975 36.714 18.791 1.00 9.23   ? 36   ARG A CZ    1 
ATOM   218  N NH1   . ARG A 1 42  ? 27.818 35.585 19.479 1.00 9.52   ? 36   ARG A NH1   1 
ATOM   219  N NH2   . ARG A 1 42  ? 29.195 37.179 18.589 1.00 10.07  ? 36   ARG A NH2   1 
ATOM   220  N N     . ALA A 1 43  ? 20.030 36.767 18.805 1.00 9.34   ? 37   ALA A N     1 
ATOM   221  C CA    . ALA A 1 43  ? 18.595 36.934 18.475 1.00 9.94   ? 37   ALA A CA    1 
ATOM   222  C C     . ALA A 1 43  ? 17.992 37.899 19.482 1.00 10.13  ? 37   ALA A C     1 
ATOM   223  O O     . ALA A 1 43  ? 17.287 37.536 20.409 1.00 10.34  ? 37   ALA A O     1 
ATOM   224  C CB    . ALA A 1 43  ? 17.900 35.575 18.479 1.00 9.32   ? 37   ALA A CB    1 
ATOM   225  N N     . LEU A 1 44  ? 18.285 39.180 19.256 1.00 10.13  ? 38   LEU A N     1 
ATOM   226  C CA    . LEU A 1 44  ? 17.944 40.215 20.255 1.00 10.92  ? 38   LEU A CA    1 
ATOM   227  C C     . LEU A 1 44  ? 16.449 40.210 20.574 1.00 11.48  ? 38   LEU A C     1 
ATOM   228  O O     . LEU A 1 44  ? 15.613 40.117 19.653 1.00 11.44  ? 38   LEU A O     1 
ATOM   229  C CB    . LEU A 1 44  ? 18.371 41.613 19.741 1.00 12.15  ? 38   LEU A CB    1 
ATOM   230  C CG    . LEU A 1 44  ? 19.837 41.737 19.332 1.00 12.11  ? 38   LEU A CG    1 
ATOM   231  C CD1   . LEU A 1 44  ? 20.152 43.197 18.988 1.00 14.63  ? 38   LEU A CD1   1 
ATOM   232  C CD2   . LEU A 1 44  ? 20.779 41.288 20.436 1.00 13.75  ? 38   LEU A CD2   1 
ATOM   233  N N     . ASN A 1 45  ? 16.135 40.244 21.886 1.00 10.92  ? 39   ASN A N     1 
ATOM   234  C CA    . ASN A 1 45  ? 14.756 40.251 22.371 1.00 12.58  ? 39   ASN A CA    1 
ATOM   235  C C     . ASN A 1 45  ? 13.992 39.006 21.962 1.00 13.02  ? 39   ASN A C     1 
ATOM   236  O O     . ASN A 1 45  ? 12.766 39.006 21.891 1.00 13.39  ? 39   ASN A O     1 
ATOM   237  C CB    . ASN A 1 45  ? 13.984 41.511 21.906 1.00 15.43  ? 39   ASN A CB    1 
ATOM   238  C CG    . ASN A 1 45  ? 14.663 42.807 22.335 1.00 16.77  ? 39   ASN A CG    1 
ATOM   239  O OD1   . ASN A 1 45  ? 15.030 43.601 21.506 1.00 20.99  ? 39   ASN A OD1   1 
ATOM   240  N ND2   . ASN A 1 45  ? 14.850 42.980 23.606 1.00 17.34  ? 39   ASN A ND2   1 
ATOM   241  N N     . ASN A 1 46  ? 14.745 37.922 21.713 1.00 9.98   ? 40   ASN A N     1 
ATOM   242  C CA    . ASN A 1 46  ? 14.224 36.579 21.369 1.00 10.20  ? 40   ASN A CA    1 
ATOM   243  C C     . ASN A 1 46  ? 13.627 36.538 19.956 1.00 9.76   ? 40   ASN A C     1 
ATOM   244  O O     . ASN A 1 46  ? 12.925 35.572 19.591 1.00 10.93  ? 40   ASN A O     1 
ATOM   245  C CB    . ASN A 1 46  ? 13.215 35.996 22.375 1.00 11.27  ? 40   ASN A CB    1 
ATOM   246  C CG    . ASN A 1 46  ? 13.660 36.138 23.825 1.00 9.86   ? 40   ASN A CG    1 
ATOM   247  O OD1   . ASN A 1 46  ? 12.922 36.699 24.631 1.00 15.92  ? 40   ASN A OD1   1 
ATOM   248  N ND2   . ASN A 1 46  ? 14.822 35.643 24.182 1.00 10.58  ? 40   ASN A ND2   1 
ATOM   249  N N     . ILE A 1 47  ? 13.934 37.532 19.143 1.00 11.16  ? 41   ILE A N     1 
ATOM   250  C CA    . ILE A 1 47  ? 13.461 37.605 17.764 1.00 11.43  ? 41   ILE A CA    1 
ATOM   251  C C     . ILE A 1 47  ? 14.642 37.241 16.870 1.00 11.69  ? 41   ILE A C     1 
ATOM   252  O O     . ILE A 1 47  ? 15.711 37.863 16.986 1.00 12.47  ? 41   ILE A O     1 
ATOM   253  C CB    . ILE A 1 47  ? 12.935 39.009 17.405 1.00 12.67  ? 41   ILE A CB    1 
ATOM   254  C CG1   . ILE A 1 47  ? 11.857 39.466 18.381 1.00 15.76  ? 41   ILE A CG1   1 
ATOM   255  C CG2   . ILE A 1 47  ? 12.339 38.976 15.937 1.00 15.91  ? 41   ILE A CG2   1 
ATOM   256  C CD1   . ILE A 1 47  ? 10.721 38.557 18.524 1.00 24.30  ? 41   ILE A CD1   1 
ATOM   257  N N     . PRO A 1 48  ? 14.518 36.259 15.980 1.00 9.64   ? 42   PRO A N     1 
ATOM   258  C CA    . PRO A 1 48  ? 15.591 36.033 15.006 1.00 9.95   ? 42   PRO A CA    1 
ATOM   259  C C     . PRO A 1 48  ? 15.879 37.333 14.265 1.00 15.29  ? 42   PRO A C     1 
ATOM   260  O O     . PRO A 1 48  ? 14.960 38.118 13.931 1.00 14.80  ? 42   PRO A O     1 
ATOM   261  C CB    . PRO A 1 48  ? 15.009 34.934 14.093 1.00 13.27  ? 42   PRO A CB    1 
ATOM   262  C CG    . PRO A 1 48  ? 13.955 34.254 14.909 1.00 12.93  ? 42   PRO A CG    1 
ATOM   263  C CD    . PRO A 1 48  ? 13.360 35.352 15.786 1.00 12.21  ? 42   PRO A CD    1 
ATOM   264  N N     . GLN A 1 49  ? 17.149 37.597 14.067 1.00 12.79  ? 43   GLN A N     1 
ATOM   265  C CA    . GLN A 1 49  ? 17.609 38.825 13.406 1.00 11.60  ? 43   GLN A CA    1 
ATOM   266  C C     . GLN A 1 49  ? 18.259 38.484 12.081 1.00 13.07  ? 43   GLN A C     1 
ATOM   267  O O     . GLN A 1 49  ? 18.723 37.369 11.837 1.00 12.86  ? 43   GLN A O     1 
ATOM   268  C CB    . GLN A 1 49  ? 18.616 39.532 14.336 1.00 12.97  ? 43   GLN A CB    1 
ATOM   269  C CG    . GLN A 1 49  ? 18.046 39.895 15.678 1.00 14.31  ? 43   GLN A CG    1 
ATOM   270  C CD    . GLN A 1 49  ? 16.950 40.940 15.633 1.00 17.87  ? 43   GLN A CD    1 
ATOM   271  O OE1   . GLN A 1 49  ? 16.921 41.827 14.728 1.00 21.28  ? 43   GLN A OE1   1 
ATOM   272  N NE2   . GLN A 1 49  ? 16.060 40.901 16.586 1.00 16.34  ? 43   GLN A NE2   1 
ATOM   273  N N     . ALA A 1 50  ? 18.431 39.523 11.247 1.00 14.24  ? 44   ALA A N     1 
ATOM   274  C CA    . ALA A 1 50  ? 19.149 39.406 9.981  1.00 12.84  ? 44   ALA A CA    1 
ATOM   275  C C     . ALA A 1 50  ? 20.531 38.787 10.170 1.00 13.76  ? 44   ALA A C     1 
ATOM   276  O O     . ALA A 1 50  ? 20.992 38.037 9.309  1.00 14.58  ? 44   ALA A O     1 
ATOM   277  C CB    . ALA A 1 50  ? 19.295 40.806 9.354  1.00 15.18  ? 44   ALA A CB    1 
ATOM   278  N N     . ALA A 1 51  ? 21.226 39.106 11.263 1.00 13.11  ? 45   ALA A N     1 
ATOM   279  C CA    . ALA A 1 51  ? 22.551 38.517 11.478 1.00 12.85  ? 45   ALA A CA    1 
ATOM   280  C C     . ALA A 1 51  ? 22.497 36.981 11.472 1.00 12.59  ? 45   ALA A C     1 
ATOM   281  O O     . ALA A 1 51  ? 23.411 36.335 10.951 1.00 12.50  ? 45   ALA A O     1 
ATOM   282  C CB    . ALA A 1 51  ? 23.153 39.024 12.793 1.00 15.96  ? 45   ALA A CB    1 
ATOM   283  N N     . LEU A 1 52  ? 21.441 36.376 12.061 1.00 11.47  ? 46   LEU A N     1 
ATOM   284  C CA    . LEU A 1 52  ? 21.303 34.905 12.027 1.00 10.95  ? 46   LEU A CA    1 
ATOM   285  C C     . LEU A 1 52  ? 21.206 34.408 10.605 1.00 11.49  ? 46   LEU A C     1 
ATOM   286  O O     . LEU A 1 52  ? 21.781 33.370 10.267 1.00 10.90  ? 46   LEU A O     1 
ATOM   287  C CB    . LEU A 1 52  ? 20.069 34.438 12.767 1.00 10.83  ? 46   LEU A CB    1 
ATOM   288  C CG    . LEU A 1 52  ? 20.261 34.289 14.276 1.00 9.99   ? 46   LEU A CG    1 
ATOM   289  C CD1   . LEU A 1 52  ? 20.544 35.626 14.997 1.00 11.95  ? 46   LEU A CD1   1 
ATOM   290  C CD2   . LEU A 1 52  ? 19.007 33.623 14.901 1.00 12.28  ? 46   LEU A CD2   1 
ATOM   291  N N     . GLY A 1 53  ? 20.486 35.144 9.737  1.00 11.69  ? 47   GLY A N     1 
ATOM   292  C CA    . GLY A 1 53  ? 20.447 34.749 8.331  1.00 12.93  ? 47   GLY A CA    1 
ATOM   293  C C     . GLY A 1 53  ? 21.824 34.722 7.702  1.00 11.26  ? 47   GLY A C     1 
ATOM   294  O O     . GLY A 1 53  ? 22.164 33.772 6.979  1.00 12.34  ? 47   GLY A O     1 
ATOM   295  N N     . GLU A 1 54  ? 22.615 35.767 7.943  1.00 12.62  ? 48   GLU A N     1 
ATOM   296  C CA    . GLU A 1 54  ? 23.963 35.788 7.378  1.00 13.25  ? 48   GLU A CA    1 
ATOM   297  C C     . GLU A 1 54  ? 24.804 34.622 7.917  1.00 10.85  ? 48   GLU A C     1 
ATOM   298  O O     . GLU A 1 54  ? 25.480 33.909 7.162  1.00 11.70  ? 48   GLU A O     1 
ATOM   299  C CB    . GLU A 1 54  ? 24.628 37.127 7.648  1.00 14.49  ? 48   GLU A CB    1 
ATOM   300  C CG    . GLU A 1 54  ? 26.067 37.184 7.173  1.00 21.39  ? 48   GLU A CG    1 
ATOM   301  C CD    . GLU A 1 54  ? 26.537 38.592 6.879  1.00 45.70  ? 48   GLU A CD    1 
ATOM   302  O OE1   . GLU A 1 54  ? 25.712 39.531 6.970  1.00 55.60  ? 48   GLU A OE1   1 
ATOM   303  O OE2   . GLU A 1 54  ? 27.733 38.750 6.535  1.00 54.83  ? 48   GLU A OE2   1 
ATOM   304  N N     . TYR A 1 55  ? 24.712 34.357 9.236  1.00 10.82  ? 49   TYR A N     1 
ATOM   305  C CA    . TYR A 1 55  ? 25.510 33.303 9.858  1.00 9.62   ? 49   TYR A CA    1 
ATOM   306  C C     . TYR A 1 55  ? 25.156 31.921 9.308  1.00 8.93   ? 49   TYR A C     1 
ATOM   307  O O     . TYR A 1 55  ? 26.042 31.125 8.981  1.00 9.72   ? 49   TYR A O     1 
ATOM   308  C CB    . TYR A 1 55  ? 25.156 33.343 11.325 1.00 10.94  ? 49   TYR A CB    1 
ATOM   309  C CG    . TYR A 1 55  ? 25.715 32.240 12.196 1.00 10.32  ? 49   TYR A CG    1 
ATOM   310  C CD1   . TYR A 1 55  ? 27.076 32.218 12.622 1.00 9.57   ? 49   TYR A CD1   1 
ATOM   311  C CD2   . TYR A 1 55  ? 24.877 31.242 12.631 1.00 10.31  ? 49   TYR A CD2   1 
ATOM   312  C CE1   . TYR A 1 55  ? 27.517 31.271 13.496 1.00 9.60   ? 49   TYR A CE1   1 
ATOM   313  C CE2   . TYR A 1 55  ? 25.350 30.260 13.510 1.00 11.63  ? 49   TYR A CE2   1 
ATOM   314  C CZ    . TYR A 1 55  ? 26.651 30.317 13.965 1.00 11.61  ? 49   TYR A CZ    1 
ATOM   315  O OH    . TYR A 1 55  ? 27.069 29.410 14.891 1.00 13.15  ? 49   TYR A OH    1 
ATOM   316  N N     . TYR A 1 56  ? 23.843 31.581 9.261  1.00 9.40   ? 50   TYR A N     1 
ATOM   317  C CA    . TYR A 1 56  ? 23.483 30.254 8.740  1.00 9.39   ? 50   TYR A CA    1 
ATOM   318  C C     . TYR A 1 56  ? 23.735 30.144 7.249  1.00 10.03  ? 50   TYR A C     1 
ATOM   319  O O     . TYR A 1 56  ? 24.178 29.073 6.796  1.00 10.66  ? 50   TYR A O     1 
ATOM   320  C CB    . TYR A 1 56  ? 22.042 29.912 9.106  1.00 10.79  ? 50   TYR A CB    1 
ATOM   321  C CG    . TYR A 1 56  ? 21.824 29.630 10.589 1.00 9.07   ? 50   TYR A CG    1 
ATOM   322  C CD1   . TYR A 1 56  ? 22.335 28.467 11.178 1.00 10.96  ? 50   TYR A CD1   1 
ATOM   323  C CD2   . TYR A 1 56  ? 21.105 30.511 11.360 1.00 10.14  ? 50   TYR A CD2   1 
ATOM   324  C CE1   . TYR A 1 56  ? 22.168 28.229 12.574 1.00 10.06  ? 50   TYR A CE1   1 
ATOM   325  C CE2   . TYR A 1 56  ? 20.926 30.284 12.716 1.00 10.09  ? 50   TYR A CE2   1 
ATOM   326  C CZ    . TYR A 1 56  ? 21.465 29.168 13.276 1.00 9.21   ? 50   TYR A CZ    1 
ATOM   327  O OH    . TYR A 1 56  ? 21.261 28.878 14.603 1.00 10.68  ? 50   TYR A OH    1 
ATOM   328  N N     . GLU A 1 57  ? 23.516 31.243 6.493  1.00 10.58  ? 51   GLU A N     1 
ATOM   329  C CA    . GLU A 1 57  ? 23.798 31.183 5.054  1.00 10.91  ? 51   GLU A CA    1 
ATOM   330  C C     . GLU A 1 57  ? 25.264 30.880 4.809  1.00 10.89  ? 51   GLU A C     1 
ATOM   331  O O     . GLU A 1 57  ? 25.611 30.100 3.904  1.00 12.68  ? 51   GLU A O     1 
ATOM   332  C CB    . GLU A 1 57  ? 23.406 32.508 4.417  1.00 12.72  ? 51   GLU A CB    1 
ATOM   333  C CG    . GLU A 1 57  ? 23.521 32.490 2.854  1.00 15.17  ? 51   GLU A CG    1 
ATOM   334  C CD    . GLU A 1 57  ? 23.212 33.858 2.297  1.00 27.57  ? 51   GLU A CD    1 
ATOM   335  O OE1   . GLU A 1 57  ? 23.753 34.857 2.835  1.00 36.90  ? 51   GLU A OE1   1 
ATOM   336  O OE2   . GLU A 1 57  ? 22.409 33.950 1.330  1.00 33.18  ? 51   GLU A OE2   1 
ATOM   337  N N     . GLN A 1 58  ? 26.149 31.479 5.631  1.00 11.02  ? 52   GLN A N     1 
ATOM   338  C CA    . GLN A 1 58  ? 27.580 31.272 5.413  1.00 9.64   ? 52   GLN A CA    1 
ATOM   339  C C     . GLN A 1 58  ? 27.973 29.820 5.567  1.00 11.34  ? 52   GLN A C     1 
ATOM   340  O O     . GLN A 1 58  ? 28.914 29.363 4.897  1.00 12.49  ? 52   GLN A O     1 
ATOM   341  C CB    . GLN A 1 58  ? 28.418 32.046 6.445  1.00 11.49  ? 52   GLN A CB    1 
ATOM   342  C CG    . GLN A 1 58  ? 28.527 33.569 6.193  1.00 11.77  ? 52   GLN A CG    1 
ATOM   343  C CD    . GLN A 1 58  ? 29.374 34.292 7.248  1.00 12.02  ? 52   GLN A CD    1 
ATOM   344  O OE1   . GLN A 1 58  ? 29.615 33.803 8.331  1.00 13.45  ? 52   GLN A OE1   1 
ATOM   345  N NE2   . GLN A 1 58  ? 29.777 35.509 6.949  1.00 15.01  ? 52   GLN A NE2   1 
ATOM   346  N N     . ARG A 1 59  ? 27.296 29.071 6.460  1.00 10.73  ? 53   ARG A N     1 
ATOM   347  C CA    . ARG A 1 59  ? 27.675 27.720 6.795  1.00 10.87  ? 53   ARG A CA    1 
ATOM   348  C C     . ARG A 1 59  ? 26.901 26.669 6.013  1.00 11.56  ? 53   ARG A C     1 
ATOM   349  O O     . ARG A 1 59  ? 27.333 25.514 5.926  1.00 12.44  ? 53   ARG A O     1 
ATOM   350  C CB    . ARG A 1 59  ? 27.410 27.546 8.293  1.00 10.80  ? 53   ARG A CB    1 
ATOM   351  C CG    . ARG A 1 59  ? 28.516 28.336 9.063  1.00 11.70  ? 53   ARG A CG    1 
ATOM   352  C CD    . ARG A 1 59  ? 28.200 28.735 10.519 1.00 10.90  ? 53   ARG A CD    1 
ATOM   353  N NE    . ARG A 1 59  ? 29.307 29.478 11.096 1.00 10.45  ? 53   ARG A NE    1 
ATOM   354  C CZ    . ARG A 1 59  ? 29.680 30.691 10.689 1.00 11.75  ? 53   ARG A CZ    1 
ATOM   355  N NH1   . ARG A 1 59  ? 28.922 31.438 9.882  1.00 11.26  ? 53   ARG A NH1   1 
ATOM   356  N NH2   . ARG A 1 59  ? 30.867 31.183 11.072 1.00 11.85  ? 53   ARG A NH2   1 
ATOM   357  N N     . ALA A 1 60  ? 25.825 27.074 5.352  1.00 10.48  ? 54   ALA A N     1 
ATOM   358  C CA    . ALA A 1 60  ? 24.999 26.173 4.566  1.00 11.63  ? 54   ALA A CA    1 
ATOM   359  C C     . ALA A 1 60  ? 25.730 25.726 3.315  1.00 11.86  ? 54   ALA A C     1 
ATOM   360  O O     . ALA A 1 60  ? 26.430 26.509 2.671  1.00 13.25  ? 54   ALA A O     1 
ATOM   361  C CB    . ALA A 1 60  ? 23.720 26.919 4.142  1.00 12.01  ? 54   ALA A CB    1 
ATOM   362  N N     . THR A 1 61  ? 25.541 24.477 2.961  1.00 10.21  ? 55   THR A N     1 
ATOM   363  C CA    . THR A 1 61  ? 26.082 23.850 1.746  1.00 10.98  ? 55   THR A CA    1 
ATOM   364  C C     . THR A 1 61  ? 25.007 23.005 1.093  1.00 10.51  ? 55   THR A C     1 
ATOM   365  O O     . THR A 1 61  ? 24.050 22.550 1.731  1.00 10.06  ? 55   THR A O     1 
ATOM   366  C CB    . THR A 1 61  ? 27.303 22.955 2.028  1.00 10.42  ? 55   THR A CB    1 
ATOM   367  O OG1   . THR A 1 61  ? 26.954 21.931 2.987  1.00 11.76  ? 55   THR A OG1   1 
ATOM   368  C CG2   . THR A 1 61  ? 28.466 23.780 2.560  1.00 12.78  ? 55   THR A CG2   1 
ATOM   369  N N     . ALA A 1 62  ? 25.173 22.784 -0.216 1.00 12.15  ? 56   ALA A N     1 
ATOM   370  C CA    . ALA A 1 62  ? 24.200 21.996 -0.967 1.00 12.49  ? 56   ALA A CA    1 
ATOM   371  C C     . ALA A 1 62  ? 24.183 20.577 -0.443 1.00 12.12  ? 56   ALA A C     1 
ATOM   372  O O     . ALA A 1 62  ? 25.231 19.922 -0.391 1.00 14.31  ? 56   ALA A O     1 
ATOM   373  C CB    . ALA A 1 62  ? 24.606 21.995 -2.455 1.00 12.28  ? 56   ALA A CB    1 
ATOM   374  N N     . GLY A 1 63  ? 23.020 20.126 0.014  1.00 10.43  ? 57   GLY A N     1 
ATOM   375  C CA    . GLY A 1 63  ? 22.938 18.792 0.566  1.00 12.52  ? 57   GLY A CA    1 
ATOM   376  C C     . GLY A 1 63  ? 23.525 18.632 1.955  1.00 11.20  ? 57   GLY A C     1 
ATOM   377  O O     . GLY A 1 63  ? 23.658 17.502 2.425  1.00 12.82  ? 57   GLY A O     1 
ATOM   378  N N     . GLY A 1 64  ? 23.832 19.724 2.626  1.00 11.18  ? 58   GLY A N     1 
ATOM   379  C CA    . GLY A 1 64  ? 24.341 19.693 3.994  1.00 11.36  ? 58   GLY A CA    1 
ATOM   380  C C     . GLY A 1 64  ? 23.237 19.908 5.011  1.00 10.02  ? 58   GLY A C     1 
ATOM   381  O O     . GLY A 1 64  ? 22.295 20.637 4.752  1.00 12.18  ? 58   GLY A O     1 
ATOM   382  N N     . PHE A 1 65  ? 23.405 19.319 6.196  1.00 9.38   ? 59   PHE A N     1 
ATOM   383  C CA    . PHE A 1 65  ? 22.416 19.405 7.259  1.00 8.83   ? 59   PHE A CA    1 
ATOM   384  C C     . PHE A 1 65  ? 22.885 20.366 8.346  1.00 10.08  ? 59   PHE A C     1 
ATOM   385  O O     . PHE A 1 65  ? 24.037 20.282 8.811  1.00 9.76   ? 59   PHE A O     1 
ATOM   386  C CB    . PHE A 1 65  ? 22.163 18.017 7.834  1.00 9.09   ? 59   PHE A CB    1 
ATOM   387  C CG    . PHE A 1 65  ? 21.190 17.978 8.964  1.00 8.45   ? 59   PHE A CG    1 
ATOM   388  C CD1   . PHE A 1 65  ? 20.037 18.751 8.934  1.00 10.59  ? 59   PHE A CD1   1 
ATOM   389  C CD2   . PHE A 1 65  ? 21.403 17.108 10.047 1.00 9.76   ? 59   PHE A CD2   1 
ATOM   390  C CE1   . PHE A 1 65  ? 19.106 18.713 9.990  1.00 11.34  ? 59   PHE A CE1   1 
ATOM   391  C CE2   . PHE A 1 65  ? 20.482 17.061 11.100 1.00 11.04  ? 59   PHE A CE2   1 
ATOM   392  C CZ    . PHE A 1 65  ? 19.337 17.851 11.082 1.00 10.95  ? 59   PHE A CZ    1 
ATOM   393  N N     . LEU A 1 66  ? 22.001 21.273 8.742  1.00 8.80   ? 60   LEU A N     1 
ATOM   394  C CA    . LEU A 1 66  ? 22.256 22.289 9.764  1.00 9.02   ? 60   LEU A CA    1 
ATOM   395  C C     . LEU A 1 66  ? 21.217 22.148 10.852 1.00 8.53   ? 60   LEU A C     1 
ATOM   396  O O     . LEU A 1 66  ? 20.026 21.959 10.566 1.00 9.14   ? 60   LEU A O     1 
ATOM   397  C CB    . LEU A 1 66  ? 22.065 23.713 9.197  1.00 9.35   ? 60   LEU A CB    1 
ATOM   398  C CG    . LEU A 1 66  ? 22.955 24.162 8.026  1.00 12.69  ? 60   LEU A CG    1 
ATOM   399  C CD1   . LEU A 1 66  ? 22.630 25.649 7.673  1.00 16.42  ? 60   LEU A CD1   1 
ATOM   400  C CD2   . LEU A 1 66  ? 24.411 24.021 8.248  1.00 14.64  ? 60   LEU A CD2   1 
ATOM   401  N N     . ILE A 1 67  ? 21.647 22.306 12.108 1.00 7.86   ? 61   ILE A N     1 
ATOM   402  C CA    . ILE A 1 67  ? 20.737 22.340 13.255 1.00 8.01   ? 61   ILE A CA    1 
ATOM   403  C C     . ILE A 1 67  ? 20.907 23.715 13.877 1.00 8.73   ? 61   ILE A C     1 
ATOM   404  O O     . ILE A 1 67  ? 22.035 24.140 14.110 1.00 9.54   ? 61   ILE A O     1 
ATOM   405  C CB    . ILE A 1 67  ? 21.055 21.224 14.270 1.00 7.99   ? 61   ILE A CB    1 
ATOM   406  C CG1   . ILE A 1 67  ? 21.027 19.826 13.599 1.00 9.31   ? 61   ILE A CG1   1 
ATOM   407  C CG2   . ILE A 1 67  ? 20.002 21.259 15.394 1.00 9.92   ? 61   ILE A CG2   1 
ATOM   408  C CD1   . ILE A 1 67  ? 21.747 18.772 14.432 1.00 10.53  ? 61   ILE A CD1   1 
ATOM   409  N N     . THR A 1 68  ? 19.797 24.407 14.134 1.00 9.29   ? 62   THR A N     1 
ATOM   410  C CA    . THR A 1 68  ? 19.899 25.734 14.743 1.00 8.50   ? 62   THR A CA    1 
ATOM   411  C C     . THR A 1 68  ? 20.320 25.672 16.218 1.00 8.71   ? 62   THR A C     1 
ATOM   412  O O     . THR A 1 68  ? 20.131 24.669 16.922 1.00 9.37   ? 62   THR A O     1 
ATOM   413  C CB    . THR A 1 68  ? 18.569 26.505 14.709 1.00 8.76   ? 62   THR A CB    1 
ATOM   414  O OG1   . THR A 1 68  ? 17.613 25.953 15.635 1.00 8.70   ? 62   THR A OG1   1 
ATOM   415  C CG2   . THR A 1 68  ? 17.977 26.619 13.322 1.00 10.21  ? 62   THR A CG2   1 
ATOM   416  N N     . GLU A 1 69  ? 20.787 26.828 16.691 1.00 8.18   ? 63   GLU A N     1 
ATOM   417  C CA    . GLU A 1 69  ? 20.818 27.141 18.103 1.00 8.78   ? 63   GLU A CA    1 
ATOM   418  C C     . GLU A 1 69  ? 19.527 26.704 18.785 1.00 8.52   ? 63   GLU A C     1 
ATOM   419  O O     . GLU A 1 69  ? 18.414 26.769 18.212 1.00 8.05   ? 63   GLU A O     1 
ATOM   420  C CB    . GLU A 1 69  ? 21.013 28.659 18.280 1.00 10.16  ? 63   GLU A CB    1 
ATOM   421  C CG    . GLU A 1 69  ? 19.802 29.512 17.704 1.00 10.23  ? 63   GLU A CG    1 
ATOM   422  C CD    . GLU A 1 69  ? 20.264 30.879 17.193 1.00 11.88  ? 63   GLU A CD    1 
ATOM   423  O OE1   . GLU A 1 69  ? 20.348 31.852 17.985 1.00 12.37  ? 63   GLU A OE1   1 
ATOM   424  O OE2   . GLU A 1 69  ? 20.772 30.939 16.037 1.00 13.13  ? 63   GLU A OE2   1 
ATOM   425  N N     . GLY A 1 70  ? 19.630 26.368 20.068 1.00 7.60   ? 64   GLY A N     1 
ATOM   426  C CA    . GLY A 1 70  ? 18.429 26.099 20.853 1.00 7.99   ? 64   GLY A CA    1 
ATOM   427  C C     . GLY A 1 70  ? 17.437 27.255 20.790 1.00 7.93   ? 64   GLY A C     1 
ATOM   428  O O     . GLY A 1 70  ? 17.816 28.423 20.896 1.00 9.15   ? 64   GLY A O     1 
ATOM   429  N N     . THR A 1 71  ? 16.161 26.916 20.636 1.00 8.12   ? 65   THR A N     1 
ATOM   430  C CA    . THR A 1 71  ? 15.113 27.910 20.365 1.00 9.08   ? 65   THR A CA    1 
ATOM   431  C C     . THR A 1 71  ? 13.993 27.727 21.364 1.00 8.08   ? 65   THR A C     1 
ATOM   432  O O     . THR A 1 71  ? 13.539 26.600 21.603 1.00 9.18   ? 65   THR A O     1 
ATOM   433  C CB    . THR A 1 71  ? 14.632 27.723 18.927 1.00 8.51   ? 65   THR A CB    1 
ATOM   434  O OG1   . THR A 1 71  ? 15.732 28.009 18.051 1.00 9.87   ? 65   THR A OG1   1 
ATOM   435  C CG2   . THR A 1 71  ? 13.536 28.686 18.545 1.00 10.82  ? 65   THR A CG2   1 
ATOM   436  N N     . MET A 1 72  ? 13.600 28.824 22.022 1.00 9.16   ? 66   MET A N     1 
ATOM   437  C CA    . MET A 1 72  ? 12.525 28.772 23.026 1.00 8.18   ? 66   MET A CA    1 
ATOM   438  C C     . MET A 1 72  ? 11.203 28.238 22.520 1.00 9.25   ? 66   MET A C     1 
ATOM   439  O O     . MET A 1 72  ? 10.745 28.586 21.432 1.00 9.59   ? 66   MET A O     1 
ATOM   440  C CB    . MET A 1 72  ? 12.249 30.132 23.656 1.00 9.56   ? 66   MET A CB    1 
ATOM   441  C CG    . MET A 1 72  ? 13.475 30.922 24.144 1.00 10.01  ? 66   MET A CG    1 
ATOM   442  S SD    . MET A 1 72  ? 13.138 32.639 24.507 1.00 10.86  ? 66   MET A SD    1 
ATOM   443  C CE    . MET A 1 72  ? 11.820 32.575 25.791 1.00 12.63  ? 66   MET A CE    1 
ATOM   444  N N     . ILE A 1 73  ? 10.552 27.464 23.385 1.00 8.96   ? 67   ILE A N     1 
ATOM   445  C CA    . ILE A 1 73  ? 9.220  26.915 23.107 1.00 9.36   ? 67   ILE A CA    1 
ATOM   446  C C     . ILE A 1 73  ? 8.119  27.671 23.815 1.00 10.64  ? 67   ILE A C     1 
ATOM   447  O O     . ILE A 1 73  ? 6.935  27.342 23.598 1.00 11.80  ? 67   ILE A O     1 
ATOM   448  C CB    . ILE A 1 73  ? 9.134  25.408 23.437 1.00 9.08   ? 67   ILE A CB    1 
ATOM   449  C CG1   . ILE A 1 73  ? 9.312  25.162 24.951 1.00 8.72   ? 67   ILE A CG1   1 
ATOM   450  C CG2   . ILE A 1 73  ? 10.166 24.651 22.615 1.00 10.48  ? 67   ILE A CG2   1 
ATOM   451  C CD1   . ILE A 1 73  ? 9.015  23.699 25.348 1.00 10.59  ? 67   ILE A CD1   1 
ATOM   452  N N     . SER A 1 74  ? 8.463  28.603 24.715 1.00 10.64  ? 68   SER A N     1 
ATOM   453  C CA    . SER A 1 74  ? 7.490  29.307 25.519 1.00 11.23  ? 68   SER A CA    1 
ATOM   454  C C     . SER A 1 74  ? 8.186  30.441 26.228 1.00 12.83  ? 68   SER A C     1 
ATOM   455  O O     . SER A 1 74  ? 9.413  30.484 26.284 1.00 12.00  ? 68   SER A O     1 
ATOM   456  C CB    . SER A 1 74  ? 6.894  28.383 26.549 1.00 13.62  ? 68   SER A CB    1 
ATOM   457  O OG    . SER A 1 74  ? 7.864  28.185 27.602 1.00 13.84  ? 68   SER A OG    1 
ATOM   458  N N     . PRO A 1 75  ? 7.438  31.370 26.829 1.00 13.00  ? 69   PRO A N     1 
ATOM   459  C CA    . PRO A 1 75  ? 8.081  32.495 27.513 1.00 14.17  ? 69   PRO A CA    1 
ATOM   460  C C     . PRO A 1 75  ? 8.912  32.100 28.720 1.00 13.16  ? 69   PRO A C     1 
ATOM   461  O O     . PRO A 1 75  ? 9.709  32.931 29.172 1.00 15.13  ? 69   PRO A O     1 
ATOM   462  C CB    . PRO A 1 75  ? 6.883  33.369 27.953 1.00 16.96  ? 69   PRO A CB    1 
ATOM   463  C CG    . PRO A 1 75  ? 5.820  33.068 26.963 1.00 17.97  ? 69   PRO A CG    1 
ATOM   464  C CD    . PRO A 1 75  ? 5.968  31.571 26.663 1.00 13.79  ? 69   PRO A CD    1 
ATOM   465  N N     . THR A 1 76  ? 8.737  30.914 29.281 1.00 11.94  ? 70   THR A N     1 
ATOM   466  C CA    . THR A 1 76  ? 9.410  30.460 30.494 1.00 13.69  ? 70   THR A CA    1 
ATOM   467  C C     . THR A 1 76  ? 10.572 29.514 30.201 1.00 12.48  ? 70   THR A C     1 
ATOM   468  O O     . THR A 1 76  ? 11.250 29.011 31.115 1.00 13.47  ? 70   THR A O     1 
ATOM   469  C CB    . THR A 1 76  ? 8.356  29.868 31.465 1.00 16.84  ? 70   THR A CB    1 
ATOM   470  O OG1   . THR A 1 76  ? 7.633  28.879 30.715 1.00 19.80  ? 70   THR A OG1   1 
ATOM   471  C CG2   . THR A 1 76  ? 7.376  30.913 31.981 1.00 19.37  ? 70   THR A CG2   1 
ATOM   472  N N     . SER A 1 77  ? 10.904 29.340 28.922 1.00 10.88  ? 71   SER A N     1 
ATOM   473  C CA    . SER A 1 77  ? 11.831 28.294 28.531 1.00 12.48  ? 71   SER A CA    1 
ATOM   474  C C     . SER A 1 77  ? 13.289 28.740 28.451 1.00 10.95  ? 71   SER A C     1 
ATOM   475  O O     . SER A 1 77  ? 14.156 27.881 28.139 1.00 10.68  ? 71   SER A O     1 
ATOM   476  C CB    . SER A 1 77  ? 11.345 27.671 27.186 1.00 13.27  ? 71   SER A CB    1 
ATOM   477  O OG    . SER A 1 77  ? 11.442 28.662 26.231 1.00 14.14  ? 71   SER A OG    1 
ATOM   478  N N     . ALA A 1 78  ? 13.609 30.032 28.643 1.00 10.81  ? 72   ALA A N     1 
ATOM   479  C CA    . ALA A 1 78  ? 14.957 30.566 28.380 1.00 11.52  ? 72   ALA A CA    1 
ATOM   480  C C     . ALA A 1 78  ? 15.784 30.719 29.639 1.00 10.37  ? 72   ALA A C     1 
ATOM   481  O O     . ALA A 1 78  ? 15.279 31.023 30.752 1.00 10.59  ? 72   ALA A O     1 
ATOM   482  C CB    . ALA A 1 78  ? 14.948 31.969 27.723 1.00 12.45  ? 72   ALA A CB    1 
ATOM   483  N N     . GLY A 1 79  ? 17.088 30.537 29.426 1.00 9.07   ? 73   GLY A N     1 
ATOM   484  C CA    . GLY A 1 79  ? 18.079 30.743 30.482 1.00 9.22   ? 73   GLY A CA    1 
ATOM   485  C C     . GLY A 1 79  ? 19.364 31.380 29.988 1.00 10.03  ? 73   GLY A C     1 
ATOM   486  O O     . GLY A 1 79  ? 20.409 31.245 30.638 1.00 10.11  ? 73   GLY A O     1 
ATOM   487  N N     . PHE A 1 80  ? 19.333 32.001 28.810 1.00 11.26  ? 74   PHE A N     1 
ATOM   488  C CA    . PHE A 1 80  ? 20.442 32.712 28.178 1.00 9.92   ? 74   PHE A CA    1 
ATOM   489  C C     . PHE A 1 80  ? 19.839 33.979 27.569 1.00 10.47  ? 74   PHE A C     1 
ATOM   490  O O     . PHE A 1 80  ? 18.631 34.028 27.265 1.00 10.22  ? 74   PHE A O     1 
ATOM   491  C CB    . PHE A 1 80  ? 21.100 31.891 27.040 1.00 10.35  ? 74   PHE A CB    1 
ATOM   492  C CG    . PHE A 1 80  ? 22.209 30.965 27.456 1.00 9.94   ? 74   PHE A CG    1 
ATOM   493  C CD1   . PHE A 1 80  ? 21.912 29.738 28.077 1.00 11.92  ? 74   PHE A CD1   1 
ATOM   494  C CD2   . PHE A 1 80  ? 23.530 31.272 27.183 1.00 11.23  ? 74   PHE A CD2   1 
ATOM   495  C CE1   . PHE A 1 80  ? 22.964 28.860 28.424 1.00 11.36  ? 74   PHE A CE1   1 
ATOM   496  C CE2   . PHE A 1 80  ? 24.603 30.412 27.545 1.00 11.67  ? 74   PHE A CE2   1 
ATOM   497  C CZ    . PHE A 1 80  ? 24.251 29.178 28.193 1.00 10.78  ? 74   PHE A CZ    1 
ATOM   498  N N     . PRO A 1 81  ? 20.630 35.014 27.408 1.00 9.39   ? 75   PRO A N     1 
ATOM   499  C CA    . PRO A 1 81  ? 20.105 36.252 26.831 1.00 9.68   ? 75   PRO A CA    1 
ATOM   500  C C     . PRO A 1 81  ? 20.012 36.164 25.321 1.00 9.18   ? 75   PRO A C     1 
ATOM   501  O O     . PRO A 1 81  ? 20.869 35.590 24.647 1.00 10.35  ? 75   PRO A O     1 
ATOM   502  C CB    . PRO A 1 81  ? 21.181 37.289 27.228 1.00 11.20  ? 75   PRO A CB    1 
ATOM   503  C CG    . PRO A 1 81  ? 22.457 36.513 27.281 1.00 12.81  ? 75   PRO A CG    1 
ATOM   504  C CD    . PRO A 1 81  ? 22.073 35.086 27.746 1.00 10.48  ? 75   PRO A CD    1 
ATOM   505  N N     . HIS A 1 82  ? 18.944 36.761 24.763 1.00 9.87   ? 76   HIS A N     1 
ATOM   506  C CA    . HIS A 1 82  ? 18.871 37.009 23.329 1.00 9.65   ? 76   HIS A CA    1 
ATOM   507  C C     . HIS A 1 82  ? 18.970 35.723 22.517 1.00 8.66   ? 76   HIS A C     1 
ATOM   508  O O     . HIS A 1 82  ? 19.651 35.668 21.463 1.00 9.21   ? 76   HIS A O     1 
ATOM   509  C CB    . HIS A 1 82  ? 19.865 38.104 22.898 1.00 10.62  ? 76   HIS A CB    1 
ATOM   510  C CG    . HIS A 1 82  ? 19.656 39.379 23.678 1.00 10.41  ? 76   HIS A CG    1 
ATOM   511  N ND1   . HIS A 1 82  ? 18.456 40.036 23.661 1.00 11.03  ? 76   HIS A ND1   1 
ATOM   512  C CD2   . HIS A 1 82  ? 20.449 40.018 24.578 1.00 12.74  ? 76   HIS A CD2   1 
ATOM   513  C CE1   . HIS A 1 82  ? 18.521 41.066 24.513 1.00 12.94  ? 76   HIS A CE1   1 
ATOM   514  N NE2   . HIS A 1 82  ? 19.714 41.072 25.070 1.00 13.77  ? 76   HIS A NE2   1 
ATOM   515  N N     . VAL A 1 83  ? 18.290 34.697 23.032 1.00 9.07   ? 77   VAL A N     1 
ATOM   516  C CA    . VAL A 1 83  ? 18.111 33.455 22.269 1.00 9.39   ? 77   VAL A CA    1 
ATOM   517  C C     . VAL A 1 83  ? 16.793 33.506 21.535 1.00 9.97   ? 77   VAL A C     1 
ATOM   518  O O     . VAL A 1 83  ? 15.822 34.081 22.029 1.00 10.01  ? 77   VAL A O     1 
ATOM   519  C CB    . VAL A 1 83  ? 18.237 32.253 23.182 1.00 10.58  ? 77   VAL A CB    1 
ATOM   520  C CG1   . VAL A 1 83  ? 19.677 32.246 23.785 1.00 11.47  ? 77   VAL A CG1   1 
ATOM   521  C CG2   . VAL A 1 83  ? 17.192 32.253 24.280 1.00 12.00  ? 77   VAL A CG2   1 
ATOM   522  N N     . PRO A 1 84  ? 16.700 32.932 20.357 1.00 8.14   ? 78   PRO A N     1 
ATOM   523  C CA    . PRO A 1 84  ? 15.447 33.047 19.604 1.00 9.17   ? 78   PRO A CA    1 
ATOM   524  C C     . PRO A 1 84  ? 14.357 32.200 20.208 1.00 9.25   ? 78   PRO A C     1 
ATOM   525  O O     . PRO A 1 84  ? 14.622 31.144 20.801 1.00 9.16   ? 78   PRO A O     1 
ATOM   526  C CB    . PRO A 1 84  ? 15.833 32.545 18.209 1.00 9.37   ? 78   PRO A CB    1 
ATOM   527  C CG    . PRO A 1 84  ? 16.965 31.539 18.462 1.00 9.73   ? 78   PRO A CG    1 
ATOM   528  C CD    . PRO A 1 84  ? 17.719 32.103 19.666 1.00 9.52   ? 78   PRO A CD    1 
ATOM   529  N N     . GLY A 1 85  ? 13.107 32.584 19.941 1.00 10.17  ? 79   GLY A N     1 
ATOM   530  C CA    . GLY A 1 85  ? 11.966 31.718 20.162 1.00 9.16   ? 79   GLY A CA    1 
ATOM   531  C C     . GLY A 1 85  ? 11.325 31.307 18.854 1.00 9.47   ? 79   GLY A C     1 
ATOM   532  O O     . GLY A 1 85  ? 11.620 31.807 17.773 1.00 10.22  ? 79   GLY A O     1 
ATOM   533  N N     . ILE A 1 86  ? 10.400 30.341 18.994 1.00 10.28  ? 80   ILE A N     1 
ATOM   534  C CA    . ILE A 1 86  ? 9.540  29.987 17.865 1.00 11.24  ? 80   ILE A CA    1 
ATOM   535  C C     . ILE A 1 86  ? 8.131  29.754 18.398 1.00 13.06  ? 80   ILE A C     1 
ATOM   536  O O     . ILE A 1 86  ? 7.358  29.000 17.805 1.00 13.43  ? 80   ILE A O     1 
ATOM   537  C CB    . ILE A 1 86  ? 10.169 28.840 17.039 1.00 10.01  ? 80   ILE A CB    1 
ATOM   538  C CG1   . ILE A 1 86  ? 9.490  28.796 15.631 1.00 13.64  ? 80   ILE A CG1   1 
ATOM   539  C CG2   . ILE A 1 86  ? 10.169 27.467 17.761 1.00 12.02  ? 80   ILE A CG2   1 
ATOM   540  C CD1   . ILE A 1 86  ? 10.377 28.145 14.596 1.00 15.13  ? 80   ILE A CD1   1 
ATOM   541  N N     . PHE A 1 87  ? 7.768  30.466 19.431 1.00 11.98  ? 81   PHE A N     1 
ATOM   542  C CA    . PHE A 1 87  ? 6.437  30.324 20.013 1.00 11.13  ? 81   PHE A CA    1 
ATOM   543  C C     . PHE A 1 87  ? 5.478  31.434 19.631 1.00 15.80  ? 81   PHE A C     1 
ATOM   544  O O     . PHE A 1 87  ? 4.290  31.324 19.980 1.00 18.39  ? 81   PHE A O     1 
ATOM   545  C CB    . PHE A 1 87  ? 6.517  30.128 21.572 1.00 13.18  ? 81   PHE A CB    1 
ATOM   546  C CG    . PHE A 1 87  ? 7.216  31.251 22.294 1.00 12.26  ? 81   PHE A CG    1 
ATOM   547  C CD1   . PHE A 1 87  ? 8.611  31.256 22.436 1.00 11.29  ? 81   PHE A CD1   1 
ATOM   548  C CD2   . PHE A 1 87  ? 6.502  32.350 22.780 1.00 14.79  ? 81   PHE A CD2   1 
ATOM   549  C CE1   . PHE A 1 87  ? 9.240  32.300 23.100 1.00 12.78  ? 81   PHE A CE1   1 
ATOM   550  C CE2   . PHE A 1 87  ? 7.128  33.393 23.392 1.00 14.70  ? 81   PHE A CE2   1 
ATOM   551  C CZ    . PHE A 1 87  ? 8.503  33.410 23.573 1.00 14.55  ? 81   PHE A CZ    1 
ATOM   552  N N     . THR A 1 88  ? 5.947  32.479 18.961 1.00 12.86  ? 82   THR A N     1 
ATOM   553  C CA    . THR A 1 88  ? 5.066  33.546 18.477 1.00 15.04  ? 82   THR A CA    1 
ATOM   554  C C     . THR A 1 88  ? 5.086  33.611 16.958 1.00 16.69  ? 82   THR A C     1 
ATOM   555  O O     . THR A 1 88  ? 6.042  33.201 16.300 1.00 14.52  ? 82   THR A O     1 
ATOM   556  C CB    . THR A 1 88  ? 5.420  34.933 18.977 1.00 16.95  ? 82   THR A CB    1 
ATOM   557  O OG1   . THR A 1 88  ? 6.595  35.411 18.337 1.00 15.98  ? 82   THR A OG1   1 
ATOM   558  C CG2   . THR A 1 88  ? 5.650  35.004 20.514 1.00 18.48  ? 82   THR A CG2   1 
ATOM   559  N N     . LYS A 1 89  ? 4.020  34.201 16.395 1.00 17.78  ? 83   LYS A N     1 
ATOM   560  C CA    . LYS A 1 89  ? 3.971  34.309 14.937 1.00 15.96  ? 83   LYS A CA    1 
ATOM   561  C C     . LYS A 1 89  ? 4.984  35.323 14.417 1.00 14.09  ? 83   LYS A C     1 
ATOM   562  O O     . LYS A 1 89  ? 5.480  35.147 13.297 1.00 15.74  ? 83   LYS A O     1 
ATOM   563  C CB    . LYS A 1 89  ? 2.540  34.653 14.469 1.00 20.70  ? 83   LYS A CB    1 
ATOM   564  C CG    . LYS A 1 89  ? 1.486  33.560 14.623 1.00 20.89  ? 83   LYS A CG    1 
ATOM   565  C CD    . LYS A 1 89  ? 1.967  32.120 14.326 1.00 26.97  ? 83   LYS A CD    1 
ATOM   566  C CE    . LYS A 1 89  ? 0.861  31.071 14.558 1.00 25.40  ? 83   LYS A CE    1 
ATOM   567  N NZ    . LYS A 1 89  ? 1.215  29.684 14.025 1.00 31.51  ? 83   LYS A NZ    1 
ATOM   568  N N     . GLU A 1 90  ? 5.325  36.353 15.174 1.00 15.52  ? 84   GLU A N     1 
ATOM   569  C CA    . GLU A 1 90  ? 6.410  37.246 14.785 1.00 14.75  ? 84   GLU A CA    1 
ATOM   570  C C     . GLU A 1 90  ? 7.738  36.489 14.655 1.00 14.83  ? 84   GLU A C     1 
ATOM   571  O O     . GLU A 1 90  ? 8.496  36.683 13.688 1.00 15.35  ? 84   GLU A O     1 
ATOM   572  C CB    . GLU A 1 90  ? 6.571  38.352 15.835 1.00 18.23  ? 84   GLU A CB    1 
ATOM   573  C CG    . GLU A 1 90  ? 7.850  39.154 15.639 1.00 23.35  ? 84   GLU A CG    1 
ATOM   574  C CD    . GLU A 1 90  ? 8.027  40.278 16.672 1.00 35.24  ? 84   GLU A CD    1 
ATOM   575  O OE1   . GLU A 1 90  ? 8.515  41.367 16.295 1.00 37.50  ? 84   GLU A OE1   1 
ATOM   576  O OE2   . GLU A 1 90  ? 7.677  40.057 17.864 1.00 27.20  ? 84   GLU A OE2   1 
ATOM   577  N N     . GLN A 1 91  ? 8.016  35.581 15.622 1.00 13.08  ? 85   GLN A N     1 
ATOM   578  C CA    . GLN A 1 91  ? 9.230  34.770 15.501 1.00 12.81  ? 85   GLN A CA    1 
ATOM   579  C C     . GLN A 1 91  ? 9.183  33.846 14.296 1.00 13.02  ? 85   GLN A C     1 
ATOM   580  O O     . GLN A 1 91  ? 10.193 33.713 13.592 1.00 12.54  ? 85   GLN A O     1 
ATOM   581  C CB    . GLN A 1 91  ? 9.435  33.956 16.773 1.00 12.46  ? 85   GLN A CB    1 
ATOM   582  C CG    . GLN A 1 91  ? 9.796  34.812 17.963 1.00 12.59  ? 85   GLN A CG    1 
ATOM   583  C CD    . GLN A 1 91  ? 9.430  34.131 19.289 1.00 12.15  ? 85   GLN A CD    1 
ATOM   584  O OE1   . GLN A 1 91  ? 8.829  33.076 19.330 1.00 11.71  ? 85   GLN A OE1   1 
ATOM   585  N NE2   . GLN A 1 91  ? 9.813  34.748 20.393 1.00 14.98  ? 85   GLN A NE2   1 
ATOM   586  N N     . VAL A 1 92  ? 8.029  33.243 13.990 1.00 11.50  ? 86   VAL A N     1 
ATOM   587  C CA    . VAL A 1 92  ? 7.885  32.436 12.777 1.00 11.56  ? 86   VAL A CA    1 
ATOM   588  C C     . VAL A 1 92  ? 8.214  33.252 11.524 1.00 12.52  ? 86   VAL A C     1 
ATOM   589  O O     . VAL A 1 92  ? 8.943  32.785 10.636 1.00 12.51  ? 86   VAL A O     1 
ATOM   590  C CB    . VAL A 1 92  ? 6.472  31.836 12.694 1.00 12.97  ? 86   VAL A CB    1 
ATOM   591  C CG1   . VAL A 1 92  ? 6.191  31.190 11.291 1.00 15.24  ? 86   VAL A CG1   1 
ATOM   592  C CG2   . VAL A 1 92  ? 6.209  30.852 13.795 1.00 14.75  ? 86   VAL A CG2   1 
ATOM   593  N N     . ARG A 1 93  ? 7.659  34.469 11.415 1.00 13.03  ? 87   ARG A N     1 
ATOM   594  C CA    . ARG A 1 93  ? 7.895  35.281 10.225 1.00 14.44  ? 87   ARG A CA    1 
ATOM   595  C C     . ARG A 1 93  ? 9.374  35.585 10.052 1.00 12.28  ? 87   ARG A C     1 
ATOM   596  O O     . ARG A 1 93  ? 9.888  35.583 8.932  1.00 13.73  ? 87   ARG A O     1 
ATOM   597  C CB    . ARG A 1 93  ? 7.100  36.584 10.349 1.00 15.85  ? 87   ARG A CB    1 
ATOM   598  C CG    . ARG A 1 93  ? 5.622  36.369 10.170 1.00 21.36  ? 87   ARG A CG    1 
ATOM   599  C CD    . ARG A 1 93  ? 4.874  37.715 10.025 1.00 28.93  ? 87   ARG A CD    1 
ATOM   600  N NE    . ARG A 1 93  ? 5.023  38.569 11.203 1.00 26.63  ? 87   ARG A NE    1 
ATOM   601  C CZ    . ARG A 1 93  ? 4.189  38.590 12.229 1.00 25.65  ? 87   ARG A CZ    1 
ATOM   602  N NH1   . ARG A 1 93  ? 3.178  37.738 12.317 1.00 31.60  ? 87   ARG A NH1   1 
ATOM   603  N NH2   . ARG A 1 93  ? 4.366  39.499 13.177 1.00 32.27  ? 87   ARG A NH2   1 
ATOM   604  N N     . GLU A 1 94  ? 10.090 35.849 11.156 1.00 12.49  ? 88   GLU A N     1 
ATOM   605  C CA    . GLU A 1 94  ? 11.503 36.176 11.046 1.00 11.89  ? 88   GLU A CA    1 
ATOM   606  C C     . GLU A 1 94  ? 12.344 34.926 10.765 1.00 12.64  ? 88   GLU A C     1 
ATOM   607  O O     . GLU A 1 94  ? 13.321 34.980 10.009 1.00 12.76  ? 88   GLU A O     1 
ATOM   608  C CB    . GLU A 1 94  ? 11.963 36.938 12.285 1.00 14.10  ? 88   GLU A CB    1 
ATOM   609  C CG    . GLU A 1 94  ? 11.319 38.328 12.520 1.00 14.50  ? 88   GLU A CG    1 
ATOM   610  C CD    . GLU A 1 94  ? 11.248 39.114 11.226 1.00 22.22  ? 88   GLU A CD    1 
ATOM   611  O OE1   . GLU A 1 94  ? 12.318 39.405 10.670 1.00 20.74  ? 88   GLU A OE1   1 
ATOM   612  O OE2   . GLU A 1 94  ? 10.111 39.465 10.833 1.00 27.08  ? 88   GLU A OE2   1 
ATOM   613  N N     . TRP A 1 95  ? 11.973 33.794 11.362 1.00 11.46  ? 89   TRP A N     1 
ATOM   614  C CA    . TRP A 1 95  ? 12.685 32.576 11.023 1.00 9.82   ? 89   TRP A CA    1 
ATOM   615  C C     . TRP A 1 95  ? 12.498 32.192 9.565  1.00 10.50  ? 89   TRP A C     1 
ATOM   616  O O     . TRP A 1 95  ? 13.434 31.636 8.969  1.00 11.29  ? 89   TRP A O     1 
ATOM   617  C CB    . TRP A 1 95  ? 12.161 31.419 11.848 1.00 10.90  ? 89   TRP A CB    1 
ATOM   618  C CG    . TRP A 1 95  ? 12.840 31.226 13.187 1.00 9.18   ? 89   TRP A CG    1 
ATOM   619  C CD1   . TRP A 1 95  ? 12.213 31.269 14.395 1.00 10.40  ? 89   TRP A CD1   1 
ATOM   620  C CD2   . TRP A 1 95  ? 14.216 30.899 13.434 1.00 9.66   ? 89   TRP A CD2   1 
ATOM   621  N NE1   . TRP A 1 95  ? 13.120 30.945 15.404 1.00 10.36  ? 89   TRP A NE1   1 
ATOM   622  C CE2   . TRP A 1 95  ? 14.350 30.728 14.831 1.00 9.92   ? 89   TRP A CE2   1 
ATOM   623  C CE3   . TRP A 1 95  ? 15.352 30.717 12.599 1.00 10.60  ? 89   TRP A CE3   1 
ATOM   624  C CZ2   . TRP A 1 95  ? 15.572 30.339 15.409 1.00 10.08  ? 89   TRP A CZ2   1 
ATOM   625  C CZ3   . TRP A 1 95  ? 16.573 30.390 13.203 1.00 11.14  ? 89   TRP A CZ3   1 
ATOM   626  C CH2   . TRP A 1 95  ? 16.664 30.183 14.592 1.00 10.16  ? 89   TRP A CH2   1 
ATOM   627  N N     . LYS A 1 96  ? 11.316 32.448 8.964  1.00 10.70  ? 90   LYS A N     1 
ATOM   628  C CA    . LYS A 1 96  ? 11.106 32.122 7.555  1.00 11.82  ? 90   LYS A CA    1 
ATOM   629  C C     . LYS A 1 96  ? 12.159 32.755 6.686  1.00 10.67  ? 90   LYS A C     1 
ATOM   630  O O     . LYS A 1 96  ? 12.627 32.129 5.725  1.00 11.99  ? 90   LYS A O     1 
ATOM   631  C CB    . LYS A 1 96  ? 9.715  32.603 7.127  1.00 13.08  ? 90   LYS A CB    1 
ATOM   632  C CG    . LYS A 1 96  ? 9.384  32.096 5.703  1.00 20.42  ? 90   LYS A CG    1 
ATOM   633  C CD    . LYS A 1 96  ? 8.026  32.555 5.194  1.00 32.93  ? 90   LYS A CD    1 
ATOM   634  C CE    . LYS A 1 96  ? 7.037  32.607 6.341  1.00 46.08  ? 90   LYS A CE    1 
ATOM   635  N NZ    . LYS A 1 96  ? 6.258  31.353 6.735  1.00 43.85  ? 90   LYS A NZ    1 
ATOM   636  N N     . LYS A 1 97  ? 12.573 33.979 6.995  1.00 11.32  ? 91   LYS A N     1 
ATOM   637  C CA    . LYS A 1 97  ? 13.569 34.643 6.167  1.00 11.94  ? 91   LYS A CA    1 
ATOM   638  C C     . LYS A 1 97  ? 14.916 33.939 6.239  1.00 12.51  ? 91   LYS A C     1 
ATOM   639  O O     . LYS A 1 97  ? 15.652 33.875 5.240  1.00 15.06  ? 91   LYS A O     1 
ATOM   640  C CB    . LYS A 1 97  ? 13.737 36.102 6.610  1.00 15.17  ? 91   LYS A CB    1 
ATOM   641  C CG    . LYS A 1 97  ? 12.465 36.955 6.397  1.00 17.61  ? 91   LYS A CG    1 
ATOM   642  C CD    . LYS A 1 97  ? 12.320 38.069 7.433  1.00 26.56  ? 91   LYS A CD    1 
ATOM   643  C CE    . LYS A 1 97  ? 12.841 39.368 7.093  1.00 41.26  ? 91   LYS A CE    1 
ATOM   644  N NZ    . LYS A 1 97  ? 12.058 40.302 7.983  1.00 32.06  ? 91   LYS A NZ    1 
ATOM   645  N N     . ILE A 1 98  ? 15.264 33.392 7.386  1.00 12.28  ? 92   ILE A N     1 
ATOM   646  C CA    . ILE A 1 98  ? 16.517 32.651 7.565  1.00 12.03  ? 92   ILE A CA    1 
ATOM   647  C C     . ILE A 1 98  ? 16.443 31.297 6.892  1.00 11.16  ? 92   ILE A C     1 
ATOM   648  O O     . ILE A 1 98  ? 17.369 30.873 6.167  1.00 12.95  ? 92   ILE A O     1 
ATOM   649  C CB    . ILE A 1 98  ? 16.773 32.535 9.082  1.00 11.37  ? 92   ILE A CB    1 
ATOM   650  C CG1   . ILE A 1 98  ? 17.050 33.926 9.637  1.00 12.76  ? 92   ILE A CG1   1 
ATOM   651  C CG2   . ILE A 1 98  ? 17.890 31.529 9.359  1.00 13.99  ? 92   ILE A CG2   1 
ATOM   652  C CD1   . ILE A 1 98  ? 16.778 34.035 11.182 1.00 14.27  ? 92   ILE A CD1   1 
ATOM   653  N N     . VAL A 1 99  ? 15.338 30.588 7.097  1.00 10.94  ? 93   VAL A N     1 
ATOM   654  C CA    . VAL A 1 99  ? 15.174 29.294 6.453  1.00 10.72  ? 93   VAL A CA    1 
ATOM   655  C C     . VAL A 1 99  ? 15.255 29.435 4.938  1.00 11.81  ? 93   VAL A C     1 
ATOM   656  O O     . VAL A 1 99  ? 15.872 28.605 4.257  1.00 11.00  ? 93   VAL A O     1 
ATOM   657  C CB    . VAL A 1 99  ? 13.852 28.672 6.898  1.00 11.50  ? 93   VAL A CB    1 
ATOM   658  C CG1   . VAL A 1 99  ? 13.555 27.409 6.113  1.00 13.55  ? 93   VAL A CG1   1 
ATOM   659  C CG2   . VAL A 1 99  ? 13.922 28.320 8.421  1.00 14.14  ? 93   VAL A CG2   1 
ATOM   660  N N     . ASP A 1 100 ? 14.648 30.496 4.382  1.00 11.71  ? 94   ASP A N     1 
ATOM   661  C CA    . ASP A 1 100 ? 14.676 30.675 2.916  1.00 11.96  ? 94   ASP A CA    1 
ATOM   662  C C     . ASP A 1 100 ? 16.080 30.857 2.390  1.00 11.99  ? 94   ASP A C     1 
ATOM   663  O O     . ASP A 1 100 ? 16.426 30.265 1.357  1.00 12.84  ? 94   ASP A O     1 
ATOM   664  C CB    . ASP A 1 100 ? 13.787 31.856 2.522  1.00 13.35  ? 94   ASP A CB    1 
ATOM   665  C CG    . ASP A 1 100 ? 12.318 31.520 2.613  1.00 16.38  ? 94   ASP A CG    1 
ATOM   666  O OD1   . ASP A 1 100 ? 11.934 30.347 2.821  1.00 19.45  ? 94   ASP A OD1   1 
ATOM   667  O OD2   . ASP A 1 100 ? 11.512 32.500 2.546  1.00 23.72  ? 94   ASP A OD2   1 
ATOM   668  N N     . VAL A 1 101 ? 16.932 31.625 3.068  1.00 10.57  ? 95   VAL A N     1 
ATOM   669  C CA    . VAL A 1 101 ? 18.304 31.790 2.575  1.00 12.01  ? 95   VAL A CA    1 
ATOM   670  C C     . VAL A 1 101 ? 19.103 30.483 2.679  1.00 11.46  ? 95   VAL A C     1 
ATOM   671  O O     . VAL A 1 101 ? 19.973 30.178 1.836  1.00 13.56  ? 95   VAL A O     1 
ATOM   672  C CB    . VAL A 1 101 ? 19.072 33.007 3.137  1.00 14.19  ? 95   VAL A CB    1 
ATOM   673  C CG1   . VAL A 1 101 ? 18.315 34.338 2.782  1.00 16.90  ? 95   VAL A CG1   1 
ATOM   674  C CG2   . VAL A 1 101 ? 19.371 32.886 4.649  1.00 17.66  ? 95   VAL A CG2   1 
ATOM   675  N N     . VAL A 1 102 ? 18.824 29.651 3.675  1.00 12.10  ? 96   VAL A N     1 
ATOM   676  C CA    . VAL A 1 102 ? 19.519 28.355 3.768  1.00 11.61  ? 96   VAL A CA    1 
ATOM   677  C C     . VAL A 1 102 ? 19.041 27.409 2.678  1.00 11.13  ? 96   VAL A C     1 
ATOM   678  O O     . VAL A 1 102 ? 19.837 26.724 2.031  1.00 11.05  ? 96   VAL A O     1 
ATOM   679  C CB    . VAL A 1 102 ? 19.288 27.794 5.203  1.00 12.60  ? 96   VAL A CB    1 
ATOM   680  C CG1   . VAL A 1 102 ? 19.701 26.348 5.296  1.00 15.01  ? 96   VAL A CG1   1 
ATOM   681  C CG2   . VAL A 1 102 ? 20.071 28.705 6.201  1.00 12.90  ? 96   VAL A CG2   1 
ATOM   682  N N     . HIS A 1 103 ? 17.742 27.355 2.464  1.00 11.28  ? 97   HIS A N     1 
ATOM   683  C CA    . HIS A 1 103 ? 17.198 26.514 1.388  1.00 10.63  ? 97   HIS A CA    1 
ATOM   684  C C     . HIS A 1 103 ? 17.669 26.974 0.006  1.00 12.00  ? 97   HIS A C     1 
ATOM   685  O O     . HIS A 1 103 ? 17.814 26.135 -0.891 1.00 12.19  ? 97   HIS A O     1 
ATOM   686  C CB    . HIS A 1 103 ? 15.680 26.489 1.489  1.00 10.75  ? 97   HIS A CB    1 
ATOM   687  C CG    . HIS A 1 103 ? 15.187 25.610 2.565  1.00 10.95  ? 97   HIS A CG    1 
ATOM   688  N ND1   . HIS A 1 103 ? 13.888 25.668 3.019  1.00 14.64  ? 97   HIS A ND1   1 
ATOM   689  C CD2   . HIS A 1 103 ? 15.783 24.606 3.233  1.00 11.53  ? 97   HIS A CD2   1 
ATOM   690  C CE1   . HIS A 1 103 ? 13.730 24.739 3.964  1.00 13.11  ? 97   HIS A CE1   1 
ATOM   691  N NE2   . HIS A 1 103 ? 14.857 24.076 4.090  1.00 13.14  ? 97   HIS A NE2   1 
ATOM   692  N N     . ALA A 1 104 ? 17.926 28.263 -0.167 1.00 11.28  ? 98   ALA A N     1 
ATOM   693  C CA    . ALA A 1 104 ? 18.447 28.728 -1.461 1.00 12.63  ? 98   ALA A CA    1 
ATOM   694  C C     . ALA A 1 104 ? 19.829 28.169 -1.743 1.00 14.87  ? 98   ALA A C     1 
ATOM   695  O O     . ALA A 1 104 ? 20.221 28.110 -2.927 1.00 16.69  ? 98   ALA A O     1 
ATOM   696  C CB    . ALA A 1 104 ? 18.473 30.253 -1.452 1.00 13.64  ? 98   ALA A CB    1 
ATOM   697  N N     . LYS A 1 105 ? 20.582 27.719 -0.738 1.00 12.46  ? 99   LYS A N     1 
ATOM   698  C CA    . LYS A 1 105 ? 21.877 27.063 -0.913 1.00 12.90  ? 99   LYS A CA    1 
ATOM   699  C C     . LYS A 1 105 ? 21.736 25.561 -1.021 1.00 13.85  ? 99   LYS A C     1 
ATOM   700  O O     . LYS A 1 105 ? 22.754 24.886 -1.225 1.00 18.11  ? 99   LYS A O     1 
ATOM   701  C CB    . LYS A 1 105 ? 22.814 27.439 0.202  1.00 19.44  ? 99   LYS A CB    1 
ATOM   702  C CG    . LYS A 1 105 ? 23.120 28.922 0.014  1.00 24.44  ? 99   LYS A CG    1 
ATOM   703  C CD    . LYS A 1 105 ? 24.292 29.380 0.813  1.00 29.59  ? 99   LYS A CD    1 
ATOM   704  C CE    . LYS A 1 105 ? 25.627 28.813 0.287  1.00 27.06  ? 99   LYS A CE    1 
ATOM   705  N NZ    . LYS A 1 105 ? 26.657 29.281 1.283  1.00 22.74  ? 99   LYS A NZ    1 
ATOM   706  N N     . GLY A 1 106 ? 20.520 25.014 -0.968 1.00 11.04  ? 100  GLY A N     1 
ATOM   707  C CA    . GLY A 1 106 ? 20.314 23.582 -1.046 1.00 11.43  ? 100  GLY A CA    1 
ATOM   708  C C     . GLY A 1 106 ? 20.519 22.816 0.254  1.00 11.60  ? 100  GLY A C     1 
ATOM   709  O O     . GLY A 1 106 ? 20.598 21.581 0.195  1.00 12.72  ? 100  GLY A O     1 
ATOM   710  N N     . ALA A 1 107 ? 20.594 23.507 1.384  1.00 10.87  ? 101  ALA A N     1 
ATOM   711  C CA    . ALA A 1 107 ? 20.825 22.826 2.657  1.00 9.93   ? 101  ALA A CA    1 
ATOM   712  C C     . ALA A 1 107 ? 19.495 22.430 3.284  1.00 10.07  ? 101  ALA A C     1 
ATOM   713  O O     . ALA A 1 107 ? 18.418 22.890 2.883  1.00 11.36  ? 101  ALA A O     1 
ATOM   714  C CB    . ALA A 1 107 ? 21.565 23.795 3.574  1.00 13.09  ? 101  ALA A CB    1 
ATOM   715  N N     . VAL A 1 108 ? 19.590 21.495 4.222  1.00 9.77   ? 102  VAL A N     1 
ATOM   716  C CA    . VAL A 1 108 ? 18.471 21.027 5.056  1.00 10.90  ? 102  VAL A CA    1 
ATOM   717  C C     . VAL A 1 108 ? 18.678 21.593 6.467  1.00 10.78  ? 102  VAL A C     1 
ATOM   718  O O     . VAL A 1 108 ? 19.808 21.601 6.953  1.00 10.06  ? 102  VAL A O     1 
ATOM   719  C CB    . VAL A 1 108 ? 18.522 19.478 5.085  1.00 11.56  ? 102  VAL A CB    1 
ATOM   720  C CG1   . VAL A 1 108 ? 17.435 18.918 6.036  1.00 13.40  ? 102  VAL A CG1   1 
ATOM   721  C CG2   . VAL A 1 108 ? 18.276 18.943 3.673  1.00 12.31  ? 102  VAL A CG2   1 
ATOM   722  N N     . ILE A 1 109 ? 17.619 22.117 7.113  1.00 8.73   ? 103  ILE A N     1 
ATOM   723  C CA    . ILE A 1 109 ? 17.799 22.775 8.412  1.00 8.99   ? 103  ILE A CA    1 
ATOM   724  C C     . ILE A 1 109 ? 16.684 22.348 9.360  1.00 8.93   ? 103  ILE A C     1 
ATOM   725  O O     . ILE A 1 109 ? 15.487 22.379 9.013  1.00 9.83   ? 103  ILE A O     1 
ATOM   726  C CB    . ILE A 1 109 ? 17.942 24.309 8.272  1.00 9.30   ? 103  ILE A CB    1 
ATOM   727  C CG1   . ILE A 1 109 ? 18.208 24.956 9.644  1.00 9.65   ? 103  ILE A CG1   1 
ATOM   728  C CG2   . ILE A 1 109 ? 16.723 24.942 7.511  1.00 10.87  ? 103  ILE A CG2   1 
ATOM   729  C CD1   . ILE A 1 109 ? 18.688 26.401 9.485  1.00 13.11  ? 103  ILE A CD1   1 
ATOM   730  N N     . PHE A 1 110 ? 17.085 21.924 10.551 1.00 8.04   ? 104  PHE A N     1 
ATOM   731  C CA    . PHE A 1 110 ? 16.166 21.633 11.654 1.00 7.88   ? 104  PHE A CA    1 
ATOM   732  C C     . PHE A 1 110 ? 16.308 22.693 12.741 1.00 8.40   ? 104  PHE A C     1 
ATOM   733  O O     . PHE A 1 110 ? 17.418 23.163 13.036 1.00 9.82   ? 104  PHE A O     1 
ATOM   734  C CB    . PHE A 1 110 ? 16.491 20.271 12.327 1.00 9.23   ? 104  PHE A CB    1 
ATOM   735  C CG    . PHE A 1 110 ? 15.919 19.051 11.585 1.00 7.72   ? 104  PHE A CG    1 
ATOM   736  C CD1   . PHE A 1 110 ? 15.646 19.081 10.207 1.00 9.90   ? 104  PHE A CD1   1 
ATOM   737  C CD2   . PHE A 1 110 ? 15.658 17.905 12.314 1.00 8.53   ? 104  PHE A CD2   1 
ATOM   738  C CE1   . PHE A 1 110 ? 15.119 17.887 9.586  1.00 11.19  ? 104  PHE A CE1   1 
ATOM   739  C CE2   . PHE A 1 110 ? 15.153 16.765 11.721 1.00 9.34   ? 104  PHE A CE2   1 
ATOM   740  C CZ    . PHE A 1 110 ? 14.885 16.738 10.380 1.00 10.33  ? 104  PHE A CZ    1 
ATOM   741  N N     . CYS A 1 111 ? 15.197 23.033 13.368 1.00 8.13   ? 105  CYS A N     1 
ATOM   742  C CA    . CYS A 1 111 ? 15.165 23.951 14.512 1.00 8.43   ? 105  CYS A CA    1 
ATOM   743  C C     . CYS A 1 111 ? 15.266 23.147 15.811 1.00 8.52   ? 105  CYS A C     1 
ATOM   744  O O     . CYS A 1 111 ? 14.420 22.278 16.060 1.00 9.20   ? 105  CYS A O     1 
ATOM   745  C CB    . CYS A 1 111 ? 13.832 24.724 14.498 1.00 8.39   ? 105  CYS A CB    1 
ATOM   746  S SG    . CYS A 1 111 ? 13.740 25.932 15.849 1.00 10.95  ? 105  CYS A SG    1 
ATOM   747  N N     . GLN A 1 112 ? 16.263 23.446 16.650 1.00 8.02   ? 106  GLN A N     1 
ATOM   748  C CA    . GLN A 1 112 ? 16.337 22.770 17.967 1.00 6.85   ? 106  GLN A CA    1 
ATOM   749  C C     . GLN A 1 112 ? 15.393 23.426 18.975 1.00 7.09   ? 106  GLN A C     1 
ATOM   750  O O     . GLN A 1 112 ? 15.520 24.631 19.226 1.00 9.15   ? 106  GLN A O     1 
ATOM   751  C CB    . GLN A 1 112 ? 17.785 22.787 18.468 1.00 8.46   ? 106  GLN A CB    1 
ATOM   752  C CG    . GLN A 1 112 ? 17.840 21.893 19.735 1.00 9.70   ? 106  GLN A CG    1 
ATOM   753  C CD    . GLN A 1 112 ? 19.135 22.010 20.475 1.00 8.16   ? 106  GLN A CD    1 
ATOM   754  O OE1   . GLN A 1 112 ? 19.490 23.070 20.991 1.00 9.02   ? 106  GLN A OE1   1 
ATOM   755  N NE2   . GLN A 1 112 ? 19.827 20.866 20.573 1.00 8.65   ? 106  GLN A NE2   1 
ATOM   756  N N     . LEU A 1 113 ? 14.489 22.650 19.558 1.00 7.90   ? 107  LEU A N     1 
ATOM   757  C CA    . LEU A 1 113 ? 13.509 23.148 20.538 1.00 9.00   ? 107  LEU A CA    1 
ATOM   758  C C     . LEU A 1 113 ? 14.086 22.954 21.938 1.00 7.64   ? 107  LEU A C     1 
ATOM   759  O O     . LEU A 1 113 ? 14.372 21.813 22.333 1.00 8.90   ? 107  LEU A O     1 
ATOM   760  C CB    . LEU A 1 113 ? 12.187 22.377 20.363 1.00 8.90   ? 107  LEU A CB    1 
ATOM   761  C CG    . LEU A 1 113 ? 11.555 22.485 18.970 1.00 9.13   ? 107  LEU A CG    1 
ATOM   762  C CD1   . LEU A 1 113 ? 10.179 21.773 19.027 1.00 10.89  ? 107  LEU A CD1   1 
ATOM   763  C CD2   . LEU A 1 113 ? 11.435 23.926 18.527 1.00 11.18  ? 107  LEU A CD2   1 
ATOM   764  N N     . TRP A 1 114 ? 14.243 24.055 22.680 1.00 8.66   ? 108  TRP A N     1 
ATOM   765  C CA    . TRP A 1 114 ? 15.044 24.064 23.908 1.00 8.79   ? 108  TRP A CA    1 
ATOM   766  C C     . TRP A 1 114 ? 14.272 24.681 25.069 1.00 10.22  ? 108  TRP A C     1 
ATOM   767  O O     . TRP A 1 114 ? 13.882 25.866 24.983 1.00 11.31  ? 108  TRP A O     1 
ATOM   768  C CB    . TRP A 1 114 ? 16.277 24.930 23.663 1.00 9.51   ? 108  TRP A CB    1 
ATOM   769  C CG    . TRP A 1 114 ? 17.278 25.009 24.777 1.00 8.79   ? 108  TRP A CG    1 
ATOM   770  C CD1   . TRP A 1 114 ? 17.543 24.090 25.771 1.00 9.53   ? 108  TRP A CD1   1 
ATOM   771  C CD2   . TRP A 1 114 ? 18.203 26.101 24.940 1.00 9.26   ? 108  TRP A CD2   1 
ATOM   772  N NE1   . TRP A 1 114 ? 18.604 24.571 26.532 1.00 9.86   ? 108  TRP A NE1   1 
ATOM   773  C CE2   . TRP A 1 114 ? 19.058 25.772 26.005 1.00 8.92   ? 108  TRP A CE2   1 
ATOM   774  C CE3   . TRP A 1 114 ? 18.430 27.300 24.238 1.00 9.72   ? 108  TRP A CE3   1 
ATOM   775  C CZ2   . TRP A 1 114 ? 20.073 26.634 26.430 1.00 10.44  ? 108  TRP A CZ2   1 
ATOM   776  C CZ3   . TRP A 1 114 ? 19.473 28.132 24.652 1.00 10.68  ? 108  TRP A CZ3   1 
ATOM   777  C CH2   . TRP A 1 114 ? 20.259 27.790 25.742 1.00 10.34  ? 108  TRP A CH2   1 
ATOM   778  N N     . HIS A 1 115 ? 14.107 23.929 26.149 1.00 8.83   ? 109  HIS A N     1 
ATOM   779  C CA    . HIS A 1 115 ? 13.616 24.459 27.415 1.00 9.31   ? 109  HIS A CA    1 
ATOM   780  C C     . HIS A 1 115 ? 14.685 24.159 28.467 1.00 8.81   ? 109  HIS A C     1 
ATOM   781  O O     . HIS A 1 115 ? 15.103 23.011 28.647 1.00 9.06   ? 109  HIS A O     1 
ATOM   782  C CB    . HIS A 1 115 ? 12.282 23.772 27.793 1.00 9.08   ? 109  HIS A CB    1 
ATOM   783  C CG    . HIS A 1 115 ? 11.549 24.472 28.892 1.00 8.57   ? 109  HIS A CG    1 
ATOM   784  N ND1   . HIS A 1 115 ? 12.131 24.793 30.110 1.00 9.30   ? 109  HIS A ND1   1 
ATOM   785  C CD2   . HIS A 1 115 ? 10.263 24.913 28.944 1.00 10.18  ? 109  HIS A CD2   1 
ATOM   786  C CE1   . HIS A 1 115 ? 11.239 25.431 30.858 1.00 10.45  ? 109  HIS A CE1   1 
ATOM   787  N NE2   . HIS A 1 115 ? 10.093 25.507 30.186 1.00 12.26  ? 109  HIS A NE2   1 
ATOM   788  N N     . VAL A 1 116 ? 15.137 25.208 29.146 1.00 8.49   ? 110  VAL A N     1 
ATOM   789  C CA    . VAL A 1 116 ? 16.222 25.103 30.125 1.00 8.62   ? 110  VAL A CA    1 
ATOM   790  C C     . VAL A 1 116 ? 15.802 24.572 31.481 1.00 8.55   ? 110  VAL A C     1 
ATOM   791  O O     . VAL A 1 116 ? 16.681 24.227 32.288 1.00 8.11   ? 110  VAL A O     1 
ATOM   792  C CB    . VAL A 1 116 ? 16.898 26.470 30.365 1.00 8.30   ? 110  VAL A CB    1 
ATOM   793  C CG1   . VAL A 1 116 ? 17.516 27.021 29.065 1.00 10.16  ? 110  VAL A CG1   1 
ATOM   794  C CG2   . VAL A 1 116 ? 15.941 27.498 30.986 1.00 9.90   ? 110  VAL A CG2   1 
ATOM   795  N N     . GLY A 1 117 ? 14.493 24.527 31.776 1.00 8.24   ? 111  GLY A N     1 
ATOM   796  C CA    . GLY A 1 117 ? 14.065 24.154 33.129 1.00 9.48   ? 111  GLY A CA    1 
ATOM   797  C C     . GLY A 1 117 ? 14.725 24.990 34.204 1.00 7.77   ? 111  GLY A C     1 
ATOM   798  O O     . GLY A 1 117 ? 14.693 26.223 34.142 1.00 9.81   ? 111  GLY A O     1 
ATOM   799  N N     . ARG A 1 118 ? 15.335 24.328 35.192 1.00 9.11   ? 112  ARG A N     1 
ATOM   800  C CA    . ARG A 1 118 ? 15.859 25.041 36.351 1.00 9.03   ? 112  ARG A CA    1 
ATOM   801  C C     . ARG A 1 118 ? 17.102 25.866 36.028 1.00 9.32   ? 112  ARG A C     1 
ATOM   802  O O     . ARG A 1 118 ? 17.576 26.628 36.887 1.00 10.09  ? 112  ARG A O     1 
ATOM   803  C CB    . ARG A 1 118 ? 16.154 24.088 37.529 1.00 9.93   ? 112  ARG A CB    1 
ATOM   804  C CG    . ARG A 1 118 ? 17.393 23.222 37.303 1.00 8.11   ? 112  ARG A CG    1 
ATOM   805  C CD    . ARG A 1 118 ? 17.519 22.213 38.450 1.00 10.18  ? 112  ARG A CD    1 
ATOM   806  N NE    . ARG A 1 118 ? 18.695 21.388 38.273 1.00 9.29   ? 112  ARG A NE    1 
ATOM   807  C CZ    . ARG A 1 118 ? 19.280 20.719 39.255 1.00 11.29  ? 112  ARG A CZ    1 
ATOM   808  N NH1   . ARG A 1 118 ? 18.792 20.727 40.506 1.00 12.94  ? 112  ARG A NH1   1 
ATOM   809  N NH2   . ARG A 1 118 ? 20.385 20.044 38.985 1.00 12.83  ? 112  ARG A NH2   1 
ATOM   810  N N     . ALA A 1 119 ? 17.681 25.702 34.831 1.00 9.08   ? 113  ALA A N     1 
ATOM   811  C CA    . ALA A 1 119 ? 18.922 26.426 34.473 1.00 8.91   ? 113  ALA A CA    1 
ATOM   812  C C     . ALA A 1 119 ? 18.547 27.808 33.926 1.00 9.65   ? 113  ALA A C     1 
ATOM   813  O O     . ALA A 1 119 ? 18.695 28.124 32.737 1.00 10.41  ? 113  ALA A O     1 
ATOM   814  C CB    . ALA A 1 119 ? 19.735 25.593 33.473 1.00 9.93   ? 113  ALA A CB    1 
ATOM   815  N N     . SER A 1 120 ? 17.992 28.607 34.823 1.00 10.40  ? 114  SER A N     1 
ATOM   816  C CA    . SER A 1 120 ? 17.479 29.932 34.445 1.00 10.00  ? 114  SER A CA    1 
ATOM   817  C C     . SER A 1 120 ? 17.687 30.850 35.633 1.00 10.36  ? 114  SER A C     1 
ATOM   818  O O     . SER A 1 120 ? 18.431 30.517 36.562 1.00 11.32  ? 114  SER A O     1 
ATOM   819  C CB    . SER A 1 120 ? 16.012 29.855 33.990 1.00 10.66  ? 114  SER A CB    1 
ATOM   820  O OG    . SER A 1 120 ? 15.614 31.114 33.388 1.00 11.14  ? 114  SER A OG    1 
ATOM   821  N N     . HIS A 1 121 ? 17.081 32.035 35.564 1.00 11.01  ? 115  HIS A N     1 
ATOM   822  C CA    . HIS A 1 121 ? 17.223 33.071 36.592 1.00 10.67  ? 115  HIS A CA    1 
ATOM   823  C C     . HIS A 1 121 ? 16.019 33.951 36.459 1.00 12.00  ? 115  HIS A C     1 
ATOM   824  O O     . HIS A 1 121 ? 15.406 34.050 35.391 1.00 11.51  ? 115  HIS A O     1 
ATOM   825  C CB    . HIS A 1 121 ? 18.498 33.851 36.308 1.00 11.12  ? 115  HIS A CB    1 
ATOM   826  C CG    . HIS A 1 121 ? 18.923 34.814 37.387 1.00 11.84  ? 115  HIS A CG    1 
ATOM   827  N ND1   . HIS A 1 121 ? 18.348 36.067 37.528 1.00 13.58  ? 115  HIS A ND1   1 
ATOM   828  C CD2   . HIS A 1 121 ? 19.903 34.712 38.313 1.00 13.31  ? 115  HIS A CD2   1 
ATOM   829  C CE1   . HIS A 1 121 ? 18.968 36.686 38.528 1.00 13.64  ? 115  HIS A CE1   1 
ATOM   830  N NE2   . HIS A 1 121 ? 19.900 35.892 39.019 1.00 14.16  ? 115  HIS A NE2   1 
ATOM   831  N N     . GLU A 1 122 ? 15.664 34.617 37.563 1.00 14.67  ? 116  GLU A N     1 
ATOM   832  C CA    . GLU A 1 122 ? 14.542 35.551 37.507 1.00 14.56  ? 116  GLU A CA    1 
ATOM   833  C C     . GLU A 1 122 ? 14.672 36.559 36.378 1.00 14.27  ? 116  GLU A C     1 
ATOM   834  O O     . GLU A 1 122 ? 13.658 36.960 35.818 1.00 13.81  ? 116  GLU A O     1 
ATOM   835  C CB    . GLU A 1 122 ? 14.435 36.286 38.873 1.00 19.12  ? 116  GLU A CB    1 
ATOM   836  N N     . VAL A 1 123 ? 15.894 36.991 36.035 1.00 11.31  ? 117  VAL A N     1 
ATOM   837  C CA    . VAL A 1 123 ? 16.047 37.964 34.963 1.00 13.16  ? 117  VAL A CA    1 
ATOM   838  C C     . VAL A 1 123 ? 15.545 37.412 33.623 1.00 12.81  ? 117  VAL A C     1 
ATOM   839  O O     . VAL A 1 123 ? 15.285 38.198 32.733 1.00 14.72  ? 117  VAL A O     1 
ATOM   840  C CB    . VAL A 1 123 ? 17.492 38.501 34.820 1.00 12.37  ? 117  VAL A CB    1 
ATOM   841  C CG1   . VAL A 1 123 ? 18.464 37.480 34.203 1.00 15.68  ? 117  VAL A CG1   1 
ATOM   842  C CG2   . VAL A 1 123 ? 17.576 39.780 33.995 1.00 22.70  ? 117  VAL A CG2   1 
ATOM   843  N N     . TYR A 1 124 ? 15.474 36.085 33.457 1.00 12.13  ? 118  TYR A N     1 
ATOM   844  C CA    . TYR A 1 124 ? 15.051 35.481 32.204 1.00 11.32  ? 118  TYR A CA    1 
ATOM   845  C C     . TYR A 1 124 ? 13.620 35.030 32.243 1.00 12.66  ? 118  TYR A C     1 
ATOM   846  O O     . TYR A 1 124 ? 13.124 34.528 31.232 1.00 13.78  ? 118  TYR A O     1 
ATOM   847  C CB    . TYR A 1 124 ? 15.958 34.262 31.865 1.00 10.59  ? 118  TYR A CB    1 
ATOM   848  C CG    . TYR A 1 124 ? 17.409 34.674 31.603 1.00 9.58   ? 118  TYR A CG    1 
ATOM   849  C CD1   . TYR A 1 124 ? 17.686 35.636 30.595 1.00 10.88  ? 118  TYR A CD1   1 
ATOM   850  C CD2   . TYR A 1 124 ? 18.458 34.133 32.331 1.00 10.78  ? 118  TYR A CD2   1 
ATOM   851  C CE1   . TYR A 1 124 ? 18.985 36.035 30.345 1.00 9.44   ? 118  TYR A CE1   1 
ATOM   852  C CE2   . TYR A 1 124 ? 19.747 34.496 32.054 1.00 11.00  ? 118  TYR A CE2   1 
ATOM   853  C CZ    . TYR A 1 124 ? 20.012 35.472 31.089 1.00 10.80  ? 118  TYR A CZ    1 
ATOM   854  O OH    . TYR A 1 124 ? 21.296 35.864 30.839 1.00 10.74  ? 118  TYR A OH    1 
ATOM   855  N N     . GLN A 1 125 ? 12.918 35.178 33.393 1.00 12.86  ? 119  GLN A N     1 
ATOM   856  C CA    . GLN A 1 125 ? 11.553 34.655 33.533 1.00 14.31  ? 119  GLN A CA    1 
ATOM   857  C C     . GLN A 1 125 ? 10.531 35.790 33.500 1.00 14.41  ? 119  GLN A C     1 
ATOM   858  O O     . GLN A 1 125 ? 10.761 36.843 34.129 1.00 16.35  ? 119  GLN A O     1 
ATOM   859  C CB    . GLN A 1 125 ? 11.451 33.907 34.865 1.00 13.54  ? 119  GLN A CB    1 
ATOM   860  C CG    . GLN A 1 125 ? 12.238 32.579 34.819 1.00 13.04  ? 119  GLN A CG    1 
ATOM   861  C CD    . GLN A 1 125 ? 11.697 31.614 33.793 1.00 13.20  ? 119  GLN A CD    1 
ATOM   862  O OE1   . GLN A 1 125 ? 10.480 31.564 33.588 1.00 16.03  ? 119  GLN A OE1   1 
ATOM   863  N NE2   . GLN A 1 125 ? 12.559 30.940 33.114 1.00 12.69  ? 119  GLN A NE2   1 
ATOM   864  N N     . PRO A 1 126 ? 9.364  35.567 32.921 1.00 16.30  ? 120  PRO A N     1 
ATOM   865  C CA    . PRO A 1 126 ? 8.283  36.573 33.012 1.00 19.31  ? 120  PRO A CA    1 
ATOM   866  C C     . PRO A 1 126 ? 7.973  36.848 34.465 1.00 19.19  ? 120  PRO A C     1 
ATOM   867  O O     . PRO A 1 126 ? 7.886  35.935 35.290 1.00 20.02  ? 120  PRO A O     1 
ATOM   868  C CB    . PRO A 1 126 ? 7.093  35.886 32.330 1.00 20.82  ? 120  PRO A CB    1 
ATOM   869  C CG    . PRO A 1 126 ? 7.710  34.835 31.466 1.00 27.39  ? 120  PRO A CG    1 
ATOM   870  C CD    . PRO A 1 126 ? 8.991  34.385 32.135 1.00 18.48  ? 120  PRO A CD    1 
ATOM   871  N N     . ALA A 1 127 ? 7.797  38.138 34.769 1.00 18.29  ? 121  ALA A N     1 
ATOM   872  C CA    . ALA A 1 127 ? 7.469  38.621 36.121 1.00 19.40  ? 121  ALA A CA    1 
ATOM   873  C C     . ALA A 1 127 ? 8.500  38.234 37.137 1.00 18.90  ? 121  ALA A C     1 
ATOM   874  O O     . ALA A 1 127 ? 8.213  38.222 38.348 1.00 23.06  ? 121  ALA A O     1 
ATOM   875  C CB    . ALA A 1 127 ? 6.071  38.158 36.575 1.00 23.52  ? 121  ALA A CB    1 
ATOM   876  N N     . GLY A 1 128 ? 9.706  37.842 36.705 1.00 15.72  ? 122  GLY A N     1 
ATOM   877  C CA    . GLY A 1 128 ? 10.720 37.438 37.653 1.00 17.39  ? 122  GLY A CA    1 
ATOM   878  C C     . GLY A 1 128 ? 10.368 36.176 38.437 1.00 16.10  ? 122  GLY A C     1 
ATOM   879  O O     . GLY A 1 128 ? 10.908 35.962 39.521 1.00 19.34  ? 122  GLY A O     1 
ATOM   880  N N     . ALA A 1 129 ? 9.545  35.298 37.871 1.00 15.70  ? 123  ALA A N     1 
ATOM   881  C CA    . ALA A 1 129 ? 9.095  34.116 38.598 1.00 17.26  ? 123  ALA A CA    1 
ATOM   882  C C     . ALA A 1 129 ? 10.185 33.047 38.622 1.00 16.41  ? 123  ALA A C     1 
ATOM   883  O O     . ALA A 1 129 ? 11.162 33.095 37.873 1.00 16.03  ? 123  ALA A O     1 
ATOM   884  C CB    . ALA A 1 129 ? 7.872  33.535 37.901 1.00 20.52  ? 123  ALA A CB    1 
ATOM   885  N N     . ALA A 1 130 ? 10.019 32.091 39.524 1.00 15.66  ? 124  ALA A N     1 
ATOM   886  C CA    . ALA A 1 130 ? 10.932 30.962 39.590 1.00 13.62  ? 124  ALA A CA    1 
ATOM   887  C C     . ALA A 1 130 ? 10.858 30.127 38.301 1.00 13.14  ? 124  ALA A C     1 
ATOM   888  O O     . ALA A 1 130 ? 9.793  29.896 37.741 1.00 14.41  ? 124  ALA A O     1 
ATOM   889  C CB    . ALA A 1 130 ? 10.593 30.080 40.799 1.00 15.47  ? 124  ALA A CB    1 
ATOM   890  N N     . PRO A 1 131 ? 11.988 29.634 37.823 1.00 11.50  ? 125  PRO A N     1 
ATOM   891  C CA    . PRO A 1 131 ? 11.984 28.664 36.717 1.00 10.91  ? 125  PRO A CA    1 
ATOM   892  C C     . PRO A 1 131 ? 11.339 27.348 37.136 1.00 12.01  ? 125  PRO A C     1 
ATOM   893  O O     . PRO A 1 131 ? 11.143 27.074 38.318 1.00 13.10  ? 125  PRO A O     1 
ATOM   894  C CB    . PRO A 1 131 ? 13.462 28.445 36.426 1.00 13.93  ? 125  PRO A CB    1 
ATOM   895  C CG    . PRO A 1 131 ? 14.162 28.766 37.639 1.00 19.22  ? 125  PRO A CG    1 
ATOM   896  C CD    . PRO A 1 131 ? 13.332 29.899 38.335 1.00 13.31  ? 125  PRO A CD    1 
ATOM   897  N N     . ILE A 1 132 ? 11.006 26.521 36.174 1.00 11.21  ? 126  ILE A N     1 
ATOM   898  C CA    . ILE A 1 132 ? 10.318 25.241 36.447 1.00 10.74  ? 126  ILE A CA    1 
ATOM   899  C C     . ILE A 1 132 ? 11.284 24.074 36.322 1.00 10.13  ? 126  ILE A C     1 
ATOM   900  O O     . ILE A 1 132 ? 12.281 24.120 35.581 1.00 11.53  ? 126  ILE A O     1 
ATOM   901  C CB    . ILE A 1 132 ? 9.105  25.026 35.517 1.00 13.73  ? 126  ILE A CB    1 
ATOM   902  C CG1   . ILE A 1 132 ? 9.497  24.982 34.033 1.00 13.06  ? 126  ILE A CG1   1 
ATOM   903  C CG2   . ILE A 1 132 ? 8.014  26.075 35.788 1.00 16.60  ? 126  ILE A CG2   1 
ATOM   904  C CD1   . ILE A 1 132 ? 8.535  24.088 33.233 1.00 16.63  ? 126  ILE A CD1   1 
ATOM   905  N N     . SER A 1 133 ? 10.937 22.953 36.975 1.00 10.09  ? 127  SER A N     1 
ATOM   906  C CA    . SER A 1 133 ? 11.750 21.754 36.852 1.00 10.00  ? 127  SER A CA    1 
ATOM   907  C C     . SER A 1 133 ? 10.986 20.533 37.320 1.00 11.21  ? 127  SER A C     1 
ATOM   908  O O     . SER A 1 133 ? 9.821  20.613 37.733 1.00 11.28  ? 127  SER A O     1 
ATOM   909  C CB    . SER A 1 133 ? 13.035 21.918 37.699 1.00 12.54  ? 127  SER A CB    1 
ATOM   910  O OG    . SER A 1 133 ? 13.985 20.879 37.483 1.00 11.95  ? 127  SER A OG    1 
ATOM   911  N N     . SER A 1 134 ? 11.667 19.395 37.256 1.00 10.90  ? 128  SER A N     1 
ATOM   912  C CA    . SER A 1 134 ? 11.153 18.173 37.896 1.00 11.28  ? 128  SER A CA    1 
ATOM   913  C C     . SER A 1 134 ? 11.189 18.254 39.396 1.00 12.12  ? 128  SER A C     1 
ATOM   914  O O     . SER A 1 134 ? 10.388 17.600 40.035 1.00 12.27  ? 128  SER A O     1 
ATOM   915  C CB    . SER A 1 134 ? 12.015 17.004 37.452 1.00 12.55  ? 128  SER A CB    1 
ATOM   916  O OG    . SER A 1 134 ? 13.383 17.283 37.826 1.00 12.40  ? 128  SER A OG    1 
ATOM   917  N N     . THR A 1 135 ? 12.071 19.099 39.936 1.00 12.78  ? 129  THR A N     1 
ATOM   918  C CA    . THR A 1 135 ? 12.504 19.122 41.324 1.00 12.86  ? 129  THR A CA    1 
ATOM   919  C C     . THR A 1 135 ? 12.399 20.553 41.840 1.00 11.06  ? 129  THR A C     1 
ATOM   920  O O     . THR A 1 135 ? 12.292 21.486 41.053 1.00 11.87  ? 129  THR A O     1 
ATOM   921  C CB    . THR A 1 135 ? 14.040 18.704 41.352 1.00 14.92  ? 129  THR A CB    1 
ATOM   922  O OG1   . THR A 1 135 ? 14.483 18.659 42.671 1.00 16.50  ? 129  THR A OG1   1 
ATOM   923  C CG2   . THR A 1 135 ? 15.050 19.673 40.558 1.00 16.38  ? 129  THR A CG2   1 
ATOM   924  N N     . GLU A 1 136 ? 12.439 20.713 43.186 1.00 12.56  ? 130  GLU A N     1 
ATOM   925  C CA    . GLU A 1 136 ? 12.618 22.022 43.786 1.00 11.59  ? 130  GLU A CA    1 
ATOM   926  C C     . GLU A 1 136 ? 14.055 22.323 44.158 1.00 11.79  ? 130  GLU A C     1 
ATOM   927  O O     . GLU A 1 136 ? 14.299 23.412 44.706 1.00 13.74  ? 130  GLU A O     1 
ATOM   928  C CB    . GLU A 1 136 ? 11.770 22.164 45.074 1.00 17.03  ? 130  GLU A CB    1 
ATOM   929  C CG    . GLU A 1 136 ? 10.336 21.731 44.930 1.00 28.84  ? 130  GLU A CG    1 
ATOM   930  C CD    . GLU A 1 136 ? 9.456  22.187 46.083 1.00 46.89  ? 130  GLU A CD    1 
ATOM   931  O OE1   . GLU A 1 136 ? 8.268  21.799 46.098 1.00 62.45  ? 130  GLU A OE1   1 
ATOM   932  O OE2   . GLU A 1 136 ? 9.947  22.936 46.956 1.00 59.84  ? 130  GLU A OE2   1 
ATOM   933  N N     . LYS A 1 137 ? 14.994 21.466 43.851 1.00 11.41  ? 131  LYS A N     1 
ATOM   934  C CA    . LYS A 1 137 ? 16.380 21.741 44.219 1.00 13.06  ? 131  LYS A CA    1 
ATOM   935  C C     . LYS A 1 137 ? 17.047 22.648 43.189 1.00 11.93  ? 131  LYS A C     1 
ATOM   936  O O     . LYS A 1 137 ? 16.898 22.420 41.956 1.00 11.72  ? 131  LYS A O     1 
ATOM   937  C CB    . LYS A 1 137 ? 17.148 20.432 44.236 1.00 14.95  ? 131  LYS A CB    1 
ATOM   938  C CG    . LYS A 1 137 ? 16.847 19.485 45.434 1.00 16.55  ? 131  LYS A CG    1 
ATOM   939  C CD    . LYS A 1 137 ? 17.070 20.247 46.816 1.00 24.90  ? 131  LYS A CD    1 
ATOM   940  C CE    . LYS A 1 137 ? 17.058 19.335 48.072 1.00 36.51  ? 131  LYS A CE    1 
ATOM   941  N NZ    . LYS A 1 137 ? 18.136 19.745 49.134 1.00 29.51  ? 131  LYS A NZ    1 
ATOM   942  N N     . PRO A 1 138 ? 17.797 23.636 43.620 1.00 10.94  ? 132  PRO A N     1 
ATOM   943  C CA    . PRO A 1 138 ? 18.579 24.465 42.688 1.00 10.67  ? 132  PRO A CA    1 
ATOM   944  C C     . PRO A 1 138 ? 19.823 23.745 42.205 1.00 11.67  ? 132  PRO A C     1 
ATOM   945  O O     . PRO A 1 138 ? 20.364 22.845 42.851 1.00 12.60  ? 132  PRO A O     1 
ATOM   946  C CB    . PRO A 1 138 ? 18.993 25.655 43.570 1.00 12.85  ? 132  PRO A CB    1 
ATOM   947  C CG    . PRO A 1 138 ? 19.134 25.057 45.014 1.00 14.99  ? 132  PRO A CG    1 
ATOM   948  C CD    . PRO A 1 138 ? 18.019 24.005 45.051 1.00 12.87  ? 132  PRO A CD    1 
ATOM   949  N N     . ILE A 1 139 ? 20.282 24.137 40.986 1.00 10.78  ? 133  ILE A N     1 
ATOM   950  C CA    . ILE A 1 139 ? 21.661 23.806 40.627 1.00 10.46  ? 133  ILE A CA    1 
ATOM   951  C C     . ILE A 1 139 ? 22.576 24.341 41.743 1.00 11.98  ? 133  ILE A C     1 
ATOM   952  O O     . ILE A 1 139 ? 22.343 25.433 42.268 1.00 12.59  ? 133  ILE A O     1 
ATOM   953  C CB    . ILE A 1 139 ? 21.952 24.411 39.238 1.00 9.63   ? 133  ILE A CB    1 
ATOM   954  C CG1   . ILE A 1 139 ? 21.064 23.779 38.154 1.00 10.43  ? 133  ILE A CG1   1 
ATOM   955  C CG2   . ILE A 1 139 ? 23.449 24.252 38.901 1.00 12.05  ? 133  ILE A CG2   1 
ATOM   956  C CD1   . ILE A 1 139 ? 21.001 24.619 36.911 1.00 11.40  ? 133  ILE A CD1   1 
ATOM   957  N N     . SER A 1 140 ? 23.626 23.599 42.063 1.00 12.59  ? 134  SER A N     1 
ATOM   958  C CA    . SER A 1 140 ? 24.505 24.074 43.125 1.00 15.45  ? 134  SER A CA    1 
ATOM   959  C C     . SER A 1 140 ? 25.362 25.233 42.670 1.00 17.92  ? 134  SER A C     1 
ATOM   960  O O     . SER A 1 140 ? 25.549 25.498 41.469 1.00 14.66  ? 134  SER A O     1 
ATOM   961  C CB    . SER A 1 140 ? 25.390 22.953 43.643 1.00 17.11  ? 134  SER A CB    1 
ATOM   962  O OG    . SER A 1 140 ? 26.382 22.652 42.717 1.00 18.86  ? 134  SER A OG    1 
ATOM   963  N N     . ASN A 1 141 ? 25.914 25.919 43.651 1.00 16.70  ? 135  ASN A N     1 
ATOM   964  C CA    . ASN A 1 141 ? 26.802 27.035 43.367 1.00 17.60  ? 135  ASN A CA    1 
ATOM   965  C C     . ASN A 1 141 ? 28.155 26.622 42.767 1.00 17.01  ? 135  ASN A C     1 
ATOM   966  O O     . ASN A 1 141 ? 28.941 27.540 42.463 1.00 22.60  ? 135  ASN A O     1 
ATOM   967  C CB    . ASN A 1 141 ? 26.967 27.985 44.564 1.00 26.02  ? 135  ASN A CB    1 
ATOM   968  C CG    . ASN A 1 141 ? 27.681 27.341 45.704 1.00 29.36  ? 135  ASN A CG    1 
ATOM   969  O OD1   . ASN A 1 141 ? 28.188 26.208 45.605 1.00 28.11  ? 135  ASN A OD1   1 
ATOM   970  N ND2   . ASN A 1 141 ? 27.720 28.053 46.832 1.00 32.33  ? 135  ASN A ND2   1 
ATOM   971  N N     . ARG A 1 142 ? 28.382 25.349 42.471 1.00 17.77  ? 136  ARG A N     1 
ATOM   972  C CA    . ARG A 1 142 ? 29.480 24.919 41.613 1.00 16.90  ? 136  ARG A CA    1 
ATOM   973  C C     . ARG A 1 142 ? 29.324 25.524 40.209 1.00 19.67  ? 136  ARG A C     1 
ATOM   974  O O     . ARG A 1 142 ? 30.315 25.690 39.476 1.00 22.29  ? 136  ARG A O     1 
ATOM   975  C CB    . ARG A 1 142 ? 29.480 23.383 41.485 1.00 17.93  ? 136  ARG A CB    1 
ATOM   976  N N     . TRP A 1 143 ? 28.103 25.915 39.835 1.00 14.59  ? 137  TRP A N     1 
ATOM   977  C CA    . TRP A 1 143 ? 27.821 26.412 38.496 1.00 13.31  ? 137  TRP A CA    1 
ATOM   978  C C     . TRP A 1 143 ? 27.187 27.774 38.634 1.00 12.00  ? 137  TRP A C     1 
ATOM   979  O O     . TRP A 1 143 ? 26.424 28.033 39.558 1.00 14.40  ? 137  TRP A O     1 
ATOM   980  C CB    . TRP A 1 143 ? 26.807 25.470 37.813 1.00 13.32  ? 137  TRP A CB    1 
ATOM   981  C CG    . TRP A 1 143 ? 27.255 24.048 37.770 1.00 16.15  ? 137  TRP A CG    1 
ATOM   982  C CD1   . TRP A 1 143 ? 26.971 23.064 38.667 1.00 17.03  ? 137  TRP A CD1   1 
ATOM   983  C CD2   . TRP A 1 143 ? 28.057 23.467 36.756 1.00 21.62  ? 137  TRP A CD2   1 
ATOM   984  N NE1   . TRP A 1 143 ? 27.575 21.913 38.290 1.00 19.21  ? 137  TRP A NE1   1 
ATOM   985  C CE2   . TRP A 1 143 ? 28.241 22.116 37.110 1.00 20.83  ? 137  TRP A CE2   1 
ATOM   986  C CE3   . TRP A 1 143 ? 28.641 23.952 35.570 1.00 21.79  ? 137  TRP A CE3   1 
ATOM   987  C CZ2   . TRP A 1 143 ? 28.995 21.226 36.315 1.00 28.28  ? 137  TRP A CZ2   1 
ATOM   988  C CZ3   . TRP A 1 143 ? 29.396 23.071 34.786 1.00 29.37  ? 137  TRP A CZ3   1 
ATOM   989  C CH2   . TRP A 1 143 ? 29.567 21.716 35.177 1.00 31.59  ? 137  TRP A CH2   1 
ATOM   990  N N     . ARG A 1 144 ? 27.462 28.648 37.645 1.00 12.48  ? 138  ARG A N     1 
ATOM   991  C CA    . ARG A 1 144 ? 26.921 30.010 37.674 1.00 12.64  ? 138  ARG A CA    1 
ATOM   992  C C     . ARG A 1 144 ? 26.368 30.343 36.293 1.00 12.41  ? 138  ARG A C     1 
ATOM   993  O O     . ARG A 1 144 ? 26.848 29.835 35.282 1.00 14.61  ? 138  ARG A O     1 
ATOM   994  C CB    . ARG A 1 144 ? 28.018 31.054 38.000 1.00 15.99  ? 138  ARG A CB    1 
ATOM   995  C CG    . ARG A 1 144 ? 28.703 30.808 39.379 1.00 19.79  ? 138  ARG A CG    1 
ATOM   996  C CD    . ARG A 1 144 ? 27.773 31.226 40.510 1.00 28.83  ? 138  ARG A CD    1 
ATOM   997  N NE    . ARG A 1 144 ? 28.290 30.735 41.784 1.00 33.46  ? 138  ARG A NE    1 
ATOM   998  C CZ    . ARG A 1 144 ? 29.046 31.439 42.613 1.00 59.68  ? 138  ARG A CZ    1 
ATOM   999  N NH1   . ARG A 1 144 ? 29.340 32.712 42.370 1.00 51.12  ? 138  ARG A NH1   1 
ATOM   1000 N NH2   . ARG A 1 144 ? 29.540 30.846 43.703 1.00 49.49  ? 138  ARG A NH2   1 
ATOM   1001 N N     . ILE A 1 145 ? 25.327 31.152 36.254 1.00 10.70  ? 139  ILE A N     1 
ATOM   1002 C CA    . ILE A 1 145 ? 24.598 31.434 35.013 1.00 10.63  ? 139  ILE A CA    1 
ATOM   1003 C C     . ILE A 1 145 ? 25.119 32.738 34.392 1.00 11.10  ? 139  ILE A C     1 
ATOM   1004 O O     . ILE A 1 145 ? 25.326 33.748 35.082 1.00 11.89  ? 139  ILE A O     1 
ATOM   1005 C CB    . ILE A 1 145 ? 23.076 31.467 35.293 1.00 10.24  ? 139  ILE A CB    1 
ATOM   1006 C CG1   . ILE A 1 145 ? 22.312 31.528 33.978 1.00 11.18  ? 139  ILE A CG1   1 
ATOM   1007 C CG2   . ILE A 1 145 ? 22.686 32.660 36.218 1.00 13.45  ? 139  ILE A CG2   1 
ATOM   1008 C CD1   . ILE A 1 145 ? 20.805 31.427 34.076 1.00 11.94  ? 139  ILE A CD1   1 
ATOM   1009 N N     . LEU A 1 146 ? 25.300 32.738 33.100 1.00 10.47  ? 140  LEU A N     1 
ATOM   1010 C CA    . LEU A 1 146 ? 25.630 33.996 32.377 1.00 10.52  ? 140  LEU A CA    1 
ATOM   1011 C C     . LEU A 1 146 ? 24.423 34.938 32.416 1.00 10.42  ? 140  LEU A C     1 
ATOM   1012 O O     . LEU A 1 146 ? 23.308 34.584 32.029 1.00 10.79  ? 140  LEU A O     1 
ATOM   1013 C CB    . LEU A 1 146 ? 25.991 33.637 30.946 1.00 11.75  ? 140  LEU A CB    1 
ATOM   1014 C CG    . LEU A 1 146 ? 26.216 34.851 30.034 1.00 11.94  ? 140  LEU A CG    1 
ATOM   1015 C CD1   . LEU A 1 146 ? 27.495 35.616 30.399 1.00 13.64  ? 140  LEU A CD1   1 
ATOM   1016 C CD2   . LEU A 1 146 ? 26.277 34.306 28.571 1.00 14.41  ? 140  LEU A CD2   1 
ATOM   1017 N N     . MET A 1 147 ? 24.656 36.150 32.893 1.00 10.81  ? 141  MET A N     1 
ATOM   1018 C CA    . MET A 1 147 ? 23.665 37.219 32.951 1.00 11.04  ? 141  MET A CA    1 
ATOM   1019 C C     . MET A 1 147 ? 23.654 38.090 31.736 1.00 11.80  ? 141  MET A C     1 
ATOM   1020 O O     . MET A 1 147 ? 24.615 38.087 30.973 1.00 11.09  ? 141  MET A O     1 
ATOM   1021 C CB    . MET A 1 147 ? 23.770 38.068 34.261 1.00 12.61  ? 141  MET A CB    1 
ATOM   1022 C CG    . MET A 1 147 ? 24.023 37.161 35.464 1.00 12.03  ? 141  MET A CG    1 
ATOM   1023 S SD    . MET A 1 147 ? 22.346 36.582 35.966 1.00 14.69  ? 141  MET A SD    1 
ATOM   1024 C CE    . MET A 1 147 ? 21.474 38.076 36.388 1.00 21.02  ? 141  MET A CE    1 
ATOM   1025 N N     . PRO A 1 148 ? 22.572 38.854 31.519 1.00 11.59  ? 142  PRO A N     1 
ATOM   1026 C CA    . PRO A 1 148 ? 22.531 39.675 30.293 1.00 12.81  ? 142  PRO A CA    1 
ATOM   1027 C C     . PRO A 1 148 ? 23.657 40.704 30.237 1.00 13.73  ? 142  PRO A C     1 
ATOM   1028 O O     . PRO A 1 148 ? 24.014 41.126 29.111 1.00 14.78  ? 142  PRO A O     1 
ATOM   1029 C CB    . PRO A 1 148 ? 21.150 40.341 30.335 1.00 14.17  ? 142  PRO A CB    1 
ATOM   1030 C CG    . PRO A 1 148 ? 20.341 39.479 31.239 1.00 14.97  ? 142  PRO A CG    1 
ATOM   1031 C CD    . PRO A 1 148 ? 21.285 38.820 32.224 1.00 12.90  ? 142  PRO A CD    1 
ATOM   1032 N N     . ASP A 1 149 ? 24.234 41.116 31.376 1.00 12.30  ? 143  ASP A N     1 
ATOM   1033 C CA    . ASP A 1 149 ? 25.275 42.134 31.329 1.00 13.27  ? 143  ASP A CA    1 
ATOM   1034 C C     . ASP A 1 149 ? 26.650 41.503 31.215 1.00 14.84  ? 143  ASP A C     1 
ATOM   1035 O O     . ASP A 1 149 ? 27.655 42.223 31.285 1.00 15.49  ? 143  ASP A O     1 
ATOM   1036 C CB    . ASP A 1 149 ? 25.178 43.056 32.555 1.00 14.08  ? 143  ASP A CB    1 
ATOM   1037 C CG    . ASP A 1 149 ? 25.394 42.368 33.888 1.00 15.48  ? 143  ASP A CG    1 
ATOM   1038 O OD1   . ASP A 1 149 ? 25.687 41.163 33.933 1.00 14.87  ? 143  ASP A OD1   1 
ATOM   1039 O OD2   . ASP A 1 149 ? 25.235 43.029 34.948 1.00 17.88  ? 143  ASP A OD2   1 
ATOM   1040 N N     . GLY A 1 150 ? 26.755 40.174 31.041 1.00 13.66  ? 144  GLY A N     1 
ATOM   1041 C CA    . GLY A 1 150 ? 28.048 39.530 30.930 1.00 16.41  ? 144  GLY A CA    1 
ATOM   1042 C C     . GLY A 1 150 ? 28.669 39.076 32.241 1.00 15.73  ? 144  GLY A C     1 
ATOM   1043 O O     . GLY A 1 150 ? 29.744 38.455 32.212 1.00 18.98  ? 144  GLY A O     1 
ATOM   1044 N N     . THR A 1 151 ? 28.062 39.373 33.386 1.00 13.04  ? 145  THR A N     1 
ATOM   1045 C CA    . THR A 1 151 ? 28.525 38.805 34.643 1.00 13.46  ? 145  THR A CA    1 
ATOM   1046 C C     . THR A 1 151 ? 27.937 37.401 34.794 1.00 14.67  ? 145  THR A C     1 
ATOM   1047 O O     . THR A 1 151 ? 27.149 36.921 33.975 1.00 12.79  ? 145  THR A O     1 
ATOM   1048 C CB    . THR A 1 151 ? 28.074 39.664 35.830 1.00 14.56  ? 145  THR A CB    1 
ATOM   1049 O OG1   . THR A 1 151 ? 26.655 39.708 35.949 1.00 15.18  ? 145  THR A OG1   1 
ATOM   1050 C CG2   . THR A 1 151 ? 28.680 41.121 35.730 1.00 19.14  ? 145  THR A CG2   1 
ATOM   1051 N N     . HIS A 1 152 ? 28.299 36.746 35.890 1.00 13.88  ? 146  HIS A N     1 
ATOM   1052 C CA    . HIS A 1 152 ? 27.751 35.425 36.205 1.00 14.38  ? 146  HIS A CA    1 
ATOM   1053 C C     . HIS A 1 152 ? 26.978 35.517 37.497 1.00 14.65  ? 146  HIS A C     1 
ATOM   1054 O O     . HIS A 1 152 ? 27.413 36.187 38.445 1.00 20.28  ? 146  HIS A O     1 
ATOM   1055 C CB    . HIS A 1 152 ? 28.840 34.350 36.219 1.00 17.06  ? 146  HIS A CB    1 
ATOM   1056 C CG    . HIS A 1 152 ? 29.300 34.016 34.849 1.00 16.97  ? 146  HIS A CG    1 
ATOM   1057 N ND1   . HIS A 1 152 ? 30.184 34.810 34.154 1.00 21.44  ? 146  HIS A ND1   1 
ATOM   1058 C CD2   . HIS A 1 152 ? 28.928 33.026 34.003 1.00 22.92  ? 146  HIS A CD2   1 
ATOM   1059 C CE1   . HIS A 1 152 ? 30.364 34.312 32.945 1.00 22.28  ? 146  HIS A CE1   1 
ATOM   1060 N NE2   . HIS A 1 152 ? 29.603 33.241 32.820 1.00 23.06  ? 146  HIS A NE2   1 
ATOM   1061 N N     . GLY A 1 153 ? 25.787 34.937 37.511 1.00 11.85  ? 147  GLY A N     1 
ATOM   1062 C CA    . GLY A 1 153 ? 24.870 34.967 38.636 1.00 12.51  ? 147  GLY A CA    1 
ATOM   1063 C C     . GLY A 1 153 ? 24.594 33.582 39.225 1.00 11.39  ? 147  GLY A C     1 
ATOM   1064 O O     . GLY A 1 153 ? 25.178 32.576 38.798 1.00 12.75  ? 147  GLY A O     1 
ATOM   1065 N N     . ILE A 1 154 ? 23.655 33.593 40.170 1.00 13.28  ? 148  ILE A N     1 
ATOM   1066 C CA    . ILE A 1 154 ? 23.338 32.402 40.962 1.00 13.11  ? 148  ILE A CA    1 
ATOM   1067 C C     . ILE A 1 154 ? 22.056 31.773 40.442 1.00 10.79  ? 148  ILE A C     1 
ATOM   1068 O O     . ILE A 1 154 ? 21.017 32.427 40.301 1.00 12.48  ? 148  ILE A O     1 
ATOM   1069 C CB    . ILE A 1 154 ? 23.172 32.795 42.434 1.00 14.51  ? 148  ILE A CB    1 
ATOM   1070 C CG1   . ILE A 1 154 ? 24.540 33.254 42.949 1.00 18.91  ? 148  ILE A CG1   1 
ATOM   1071 C CG2   . ILE A 1 154 ? 22.713 31.602 43.269 1.00 15.67  ? 148  ILE A CG2   1 
ATOM   1072 C CD1   . ILE A 1 154 ? 24.380 34.120 44.196 1.00 34.39  ? 148  ILE A CD1   1 
ATOM   1073 N N     . TYR A 1 155 ? 22.125 30.464 40.158 1.00 11.09  ? 149  TYR A N     1 
ATOM   1074 C CA    . TYR A 1 155 ? 20.883 29.749 39.791 1.00 10.76  ? 149  TYR A CA    1 
ATOM   1075 C C     . TYR A 1 155 ? 19.927 29.684 40.987 1.00 10.96  ? 149  TYR A C     1 
ATOM   1076 O O     . TYR A 1 155 ? 20.350 29.284 42.083 1.00 12.93  ? 149  TYR A O     1 
ATOM   1077 C CB    . TYR A 1 155 ? 21.210 28.319 39.356 1.00 12.29  ? 149  TYR A CB    1 
ATOM   1078 C CG    . TYR A 1 155 ? 21.925 28.198 38.024 1.00 10.15  ? 149  TYR A CG    1 
ATOM   1079 C CD1   . TYR A 1 155 ? 21.232 28.374 36.842 1.00 9.76   ? 149  TYR A CD1   1 
ATOM   1080 C CD2   . TYR A 1 155 ? 23.257 27.859 37.997 1.00 10.78  ? 149  TYR A CD2   1 
ATOM   1081 C CE1   . TYR A 1 155 ? 21.906 28.209 35.623 1.00 10.63  ? 149  TYR A CE1   1 
ATOM   1082 C CE2   . TYR A 1 155 ? 23.950 27.711 36.797 1.00 10.35  ? 149  TYR A CE2   1 
ATOM   1083 C CZ    . TYR A 1 155 ? 23.229 27.896 35.635 1.00 11.12  ? 149  TYR A CZ    1 
ATOM   1084 O OH    . TYR A 1 155 ? 23.941 27.747 34.449 1.00 13.85  ? 149  TYR A OH    1 
ATOM   1085 N N     . PRO A 1 156 ? 18.678 30.075 40.820 1.00 12.00  ? 150  PRO A N     1 
ATOM   1086 C CA    . PRO A 1 156 ? 17.687 30.065 41.908 1.00 11.90  ? 150  PRO A CA    1 
ATOM   1087 C C     . PRO A 1 156 ? 17.029 28.714 42.083 1.00 13.65  ? 150  PRO A C     1 
ATOM   1088 O O     . PRO A 1 156 ? 17.194 27.778 41.287 1.00 13.48  ? 150  PRO A O     1 
ATOM   1089 C CB    . PRO A 1 156 ? 16.651 31.076 41.401 1.00 14.18  ? 150  PRO A CB    1 
ATOM   1090 C CG    . PRO A 1 156 ? 16.577 30.778 39.869 1.00 15.15  ? 150  PRO A CG    1 
ATOM   1091 C CD    . PRO A 1 156 ? 18.076 30.614 39.568 1.00 13.86  ? 150  PRO A CD    1 
ATOM   1092 N N     . LYS A 1 157 ? 16.269 28.603 43.170 1.00 12.86  ? 151  LYS A N     1 
ATOM   1093 C CA    . LYS A 1 157 ? 15.476 27.402 43.387 1.00 14.77  ? 151  LYS A CA    1 
ATOM   1094 C C     . LYS A 1 157 ? 14.352 27.359 42.344 1.00 13.38  ? 151  LYS A C     1 
ATOM   1095 O O     . LYS A 1 157 ? 13.634 28.343 42.169 1.00 14.03  ? 151  LYS A O     1 
ATOM   1096 C CB    . LYS A 1 157 ? 14.889 27.565 44.826 1.00 20.67  ? 151  LYS A CB    1 
ATOM   1097 C CG    . LYS A 1 157 ? 14.038 26.492 45.301 1.00 27.00  ? 151  LYS A CG    1 
ATOM   1098 C CD    . LYS A 1 157 ? 13.871 26.707 46.825 1.00 24.05  ? 151  LYS A CD    1 
ATOM   1099 C CE    . LYS A 1 157 ? 12.665 27.619 47.095 1.00 29.96  ? 151  LYS A CE    1 
ATOM   1100 N NZ    . LYS A 1 157 ? 12.491 27.865 48.618 1.00 27.89  ? 151  LYS A NZ    1 
ATOM   1101 N N     . PRO A 1 158 ? 14.128 26.237 41.672 1.00 11.89  ? 152  PRO A N     1 
ATOM   1102 C CA    . PRO A 1 158 ? 12.995 26.137 40.746 1.00 10.74  ? 152  PRO A CA    1 
ATOM   1103 C C     . PRO A 1 158 ? 11.743 25.693 41.494 1.00 11.77  ? 152  PRO A C     1 
ATOM   1104 O O     . PRO A 1 158 ? 11.798 25.278 42.656 1.00 13.78  ? 152  PRO A O     1 
ATOM   1105 C CB    . PRO A 1 158 ? 13.435 25.016 39.765 1.00 12.34  ? 152  PRO A CB    1 
ATOM   1106 C CG    . PRO A 1 158 ? 14.252 24.080 40.669 1.00 11.37  ? 152  PRO A CG    1 
ATOM   1107 C CD    . PRO A 1 158 ? 15.016 25.059 41.571 1.00 14.09  ? 152  PRO A CD    1 
ATOM   1108 N N     . ARG A 1 159 ? 10.637 25.723 40.788 1.00 12.05  ? 153  ARG A N     1 
ATOM   1109 C CA    . ARG A 1 159 ? 9.349  25.180 41.232 1.00 11.82  ? 153  ARG A CA    1 
ATOM   1110 C C     . ARG A 1 159 ? 9.158  23.821 40.545 1.00 12.92  ? 153  ARG A C     1 
ATOM   1111 O O     . ARG A 1 159 ? 9.341  23.716 39.311 1.00 13.13  ? 153  ARG A O     1 
ATOM   1112 C CB    . ARG A 1 159 ? 8.287  26.198 40.816 1.00 17.91  ? 153  ARG A CB    1 
ATOM   1113 C CG    . ARG A 1 159 ? 6.868  25.866 41.053 1.00 22.10  ? 153  ARG A CG    1 
ATOM   1114 C CD    . ARG A 1 159 ? 5.972  27.079 40.631 1.00 19.31  ? 153  ARG A CD    1 
ATOM   1115 N NE    . ARG A 1 159 ? 5.901  27.463 39.213 1.00 18.39  ? 153  ARG A NE    1 
ATOM   1116 C CZ    . ARG A 1 159 ? 5.256  26.782 38.254 1.00 15.05  ? 153  ARG A CZ    1 
ATOM   1117 N NH1   . ARG A 1 159 ? 4.657  25.630 38.539 1.00 19.83  ? 153  ARG A NH1   1 
ATOM   1118 N NH2   . ARG A 1 159 ? 5.143  27.303 37.055 1.00 16.84  ? 153  ARG A NH2   1 
ATOM   1119 N N     . ALA A 1 160 ? 8.797  22.779 41.304 1.00 13.23  ? 154  ALA A N     1 
ATOM   1120 C CA    . ALA A 1 160 ? 8.572  21.453 40.737 1.00 12.61  ? 154  ALA A CA    1 
ATOM   1121 C C     . ALA A 1 160 ? 7.158  21.397 40.177 1.00 15.08  ? 154  ALA A C     1 
ATOM   1122 O O     . ALA A 1 160 ? 6.186  21.693 40.875 1.00 16.61  ? 154  ALA A O     1 
ATOM   1123 C CB    . ALA A 1 160 ? 8.739  20.379 41.824 1.00 14.29  ? 154  ALA A CB    1 
ATOM   1124 N N     . ILE A 1 161 ? 7.033  21.078 38.934 1.00 12.88  ? 155  ILE A N     1 
ATOM   1125 C CA    . ILE A 1 161 ? 5.718  21.126 38.269 1.00 12.55  ? 155  ILE A CA    1 
ATOM   1126 C C     . ILE A 1 161 ? 4.919  19.829 38.475 1.00 12.07  ? 155  ILE A C     1 
ATOM   1127 O O     . ILE A 1 161 ? 5.461  18.738 38.574 1.00 11.94  ? 155  ILE A O     1 
ATOM   1128 C CB    . ILE A 1 161 ? 5.888  21.439 36.775 1.00 12.51  ? 155  ILE A CB    1 
ATOM   1129 C CG1   . ILE A 1 161 ? 6.729  20.390 36.054 1.00 13.22  ? 155  ILE A CG1   1 
ATOM   1130 C CG2   . ILE A 1 161 ? 6.485  22.837 36.624 1.00 14.40  ? 155  ILE A CG2   1 
ATOM   1131 C CD1   . ILE A 1 161 ? 6.798  20.668 34.474 1.00 15.15  ? 155  ILE A CD1   1 
ATOM   1132 N N     . GLY A 1 162 ? 3.598  19.985 38.477 1.00 11.23  ? 156  GLY A N     1 
ATOM   1133 C CA    . GLY A 1 162 ? 2.683  18.838 38.527 1.00 11.39  ? 156  GLY A CA    1 
ATOM   1134 C C     . GLY A 1 162 ? 2.438  18.267 37.140 1.00 11.10  ? 156  GLY A C     1 
ATOM   1135 O O     . GLY A 1 162 ? 2.972  18.729 36.121 1.00 11.21  ? 156  GLY A O     1 
ATOM   1136 N N     . THR A 1 163 ? 1.593  17.216 37.094 1.00 9.80   ? 157  THR A N     1 
ATOM   1137 C CA    . THR A 1 163 ? 1.437  16.518 35.817 1.00 10.73  ? 157  THR A CA    1 
ATOM   1138 C C     . THR A 1 163 ? 0.582  17.283 34.809 1.00 10.54  ? 157  THR A C     1 
ATOM   1139 O O     . THR A 1 163 ? 0.821  17.165 33.603 1.00 10.42  ? 157  THR A O     1 
ATOM   1140 C CB    . THR A 1 163 ? 0.917  15.104 35.980 1.00 10.34  ? 157  THR A CB    1 
ATOM   1141 O OG1   . THR A 1 163 ? -0.447 15.173 36.456 1.00 11.84  ? 157  THR A OG1   1 
ATOM   1142 C CG2   . THR A 1 163 ? 1.721  14.293 36.956 1.00 11.29  ? 157  THR A CG2   1 
ATOM   1143 N N     . TYR A 1 164 ? -0.378 18.112 35.255 1.00 10.61  ? 158  TYR A N     1 
ATOM   1144 C CA    . TYR A 1 164 ? -1.033 18.973 34.281 1.00 10.54  ? 158  TYR A CA    1 
ATOM   1145 C C     . TYR A 1 164 ? -0.023 19.917 33.645 1.00 8.94   ? 158  TYR A C     1 
ATOM   1146 O O     . TYR A 1 164 ? 0.020  20.073 32.406 1.00 10.05  ? 158  TYR A O     1 
ATOM   1147 C CB    . TYR A 1 164 ? -2.138 19.805 34.982 1.00 12.08  ? 158  TYR A CB    1 
ATOM   1148 C CG    . TYR A 1 164 ? -2.691 20.858 34.037 1.00 11.64  ? 158  TYR A CG    1 
ATOM   1149 C CD1   . TYR A 1 164 ? -3.382 20.511 32.871 1.00 13.48  ? 158  TYR A CD1   1 
ATOM   1150 C CD2   . TYR A 1 164 ? -2.477 22.209 34.302 1.00 13.59  ? 158  TYR A CD2   1 
ATOM   1151 C CE1   . TYR A 1 164 ? -3.851 21.500 32.013 1.00 13.47  ? 158  TYR A CE1   1 
ATOM   1152 C CE2   . TYR A 1 164 ? -3.004 23.202 33.379 1.00 13.46  ? 158  TYR A CE2   1 
ATOM   1153 C CZ    . TYR A 1 164 ? -3.651 22.762 32.305 1.00 13.91  ? 158  TYR A CZ    1 
ATOM   1154 O OH    . TYR A 1 164 ? -4.156 23.751 31.433 1.00 24.44  ? 158  TYR A OH    1 
ATOM   1155 N N     . GLU A 1 165 ? 0.818  20.534 34.463 1.00 10.24  ? 159  GLU A N     1 
ATOM   1156 C CA    . GLU A 1 165 ? 1.765  21.468 33.861 1.00 11.01  ? 159  GLU A CA    1 
ATOM   1157 C C     . GLU A 1 165 ? 2.756  20.726 32.956 1.00 10.90  ? 159  GLU A C     1 
ATOM   1158 O O     . GLU A 1 165 ? 3.165  21.246 31.909 1.00 10.53  ? 159  GLU A O     1 
ATOM   1159 C CB    . GLU A 1 165 ? 2.520  22.208 34.959 1.00 11.44  ? 159  GLU A CB    1 
ATOM   1160 C CG    . GLU A 1 165 ? 3.435  23.302 34.399 1.00 14.88  ? 159  GLU A CG    1 
ATOM   1161 C CD    . GLU A 1 165 ? 3.704  24.355 35.411 1.00 19.34  ? 159  GLU A CD    1 
ATOM   1162 O OE1   . GLU A 1 165 ? 3.152  24.300 36.558 1.00 19.58  ? 159  GLU A OE1   1 
ATOM   1163 O OE2   . GLU A 1 165 ? 4.453  25.325 35.039 1.00 21.03  ? 159  GLU A OE2   1 
ATOM   1164 N N     . ILE A 1 166 ? 3.186  19.522 33.342 1.00 10.88  ? 160  ILE A N     1 
ATOM   1165 C CA    . ILE A 1 166 ? 3.992  18.715 32.408 1.00 10.63  ? 160  ILE A CA    1 
ATOM   1166 C C     . ILE A 1 166 ? 3.289  18.598 31.074 1.00 10.85  ? 160  ILE A C     1 
ATOM   1167 O O     . ILE A 1 166 ? 3.909  18.777 30.015 1.00 10.69  ? 160  ILE A O     1 
ATOM   1168 C CB    . ILE A 1 166 ? 4.309  17.340 33.009 1.00 10.93  ? 160  ILE A CB    1 
ATOM   1169 C CG1   . ILE A 1 166 ? 5.326  17.461 34.126 1.00 11.73  ? 160  ILE A CG1   1 
ATOM   1170 C CG2   . ILE A 1 166 ? 4.806  16.340 31.898 1.00 13.51  ? 160  ILE A CG2   1 
ATOM   1171 C CD1   . ILE A 1 166 ? 5.449  16.180 35.040 1.00 12.44  ? 160  ILE A CD1   1 
ATOM   1172 N N     . SER A 1 167 ? 1.990  18.261 31.091 1.00 10.73  ? 161  SER A N     1 
ATOM   1173 C CA    . SER A 1 167 ? 1.284  18.087 29.816 1.00 10.99  ? 161  SER A CA    1 
ATOM   1174 C C     . SER A 1 167 ? 1.218  19.399 29.040 1.00 10.37  ? 161  SER A C     1 
ATOM   1175 O O     . SER A 1 167 ? 1.213  19.381 27.799 1.00 11.06  ? 161  SER A O     1 
ATOM   1176 C CB    . SER A 1 167 ? -0.140 17.475 30.009 1.00 11.04  ? 161  SER A CB    1 
ATOM   1177 O OG    . SER A 1 167 ? -1.038 18.469 30.565 1.00 12.30  ? 161  SER A OG    1 
ATOM   1178 N N     . GLN A 1 168 ? 1.215  20.537 29.726 1.00 10.08  ? 162  GLN A N     1 
ATOM   1179 C CA    . GLN A 1 168 ? 1.209  21.807 28.995 1.00 11.09  ? 162  GLN A CA    1 
ATOM   1180 C C     . GLN A 1 168 ? 2.578  22.148 28.431 1.00 11.11  ? 162  GLN A C     1 
ATOM   1181 O O     . GLN A 1 168 ? 2.635  22.735 27.353 1.00 11.81  ? 162  GLN A O     1 
ATOM   1182 C CB    . GLN A 1 168 ? 0.714  22.922 29.904 1.00 13.35  ? 162  GLN A CB    1 
ATOM   1183 C CG    . GLN A 1 168 ? -0.801 22.675 30.319 1.00 17.96  ? 162  GLN A CG    1 
ATOM   1184 C CD    . GLN A 1 168 ? -1.700 22.225 29.141 1.00 25.47  ? 162  GLN A CD    1 
ATOM   1185 O OE1   . GLN A 1 168 ? -2.064 21.029 28.976 1.00 26.73  ? 162  GLN A OE1   1 
ATOM   1186 N NE2   . GLN A 1 168 ? -2.046 23.186 28.305 1.00 27.08  ? 162  GLN A NE2   1 
ATOM   1187 N N     . VAL A 1 169 ? 3.671  21.732 29.100 1.00 10.71  ? 163  VAL A N     1 
ATOM   1188 C CA    . VAL A 1 169 ? 4.982  21.903 28.485 1.00 10.90  ? 163  VAL A CA    1 
ATOM   1189 C C     . VAL A 1 169 ? 5.088  21.033 27.247 1.00 9.48   ? 163  VAL A C     1 
ATOM   1190 O O     . VAL A 1 169 ? 5.592  21.473 26.202 1.00 9.68   ? 163  VAL A O     1 
ATOM   1191 C CB    . VAL A 1 169 ? 6.077  21.586 29.499 1.00 10.18  ? 163  VAL A CB    1 
ATOM   1192 C CG1   . VAL A 1 169 ? 7.419  21.718 28.804 1.00 10.59  ? 163  VAL A CG1   1 
ATOM   1193 C CG2   . VAL A 1 169 ? 6.058  22.526 30.696 1.00 11.27  ? 163  VAL A CG2   1 
ATOM   1194 N N     . VAL A 1 170 ? 4.585  19.785 27.319 1.00 9.32   ? 164  VAL A N     1 
ATOM   1195 C CA    . VAL A 1 170 ? 4.534  18.947 26.119 1.00 9.25   ? 164  VAL A CA    1 
ATOM   1196 C C     . VAL A 1 170 ? 3.791  19.666 24.998 1.00 9.70   ? 164  VAL A C     1 
ATOM   1197 O O     . VAL A 1 170 ? 4.238  19.651 23.829 1.00 10.55  ? 164  VAL A O     1 
ATOM   1198 C CB    . VAL A 1 170 ? 3.930  17.566 26.417 1.00 10.19  ? 164  VAL A CB    1 
ATOM   1199 C CG1   . VAL A 1 170 ? 3.681  16.739 25.128 1.00 11.46  ? 164  VAL A CG1   1 
ATOM   1200 C CG2   . VAL A 1 170 ? 4.812  16.822 27.392 1.00 12.22  ? 164  VAL A CG2   1 
ATOM   1201 N N     . GLU A 1 171 ? 2.654  20.296 25.312 1.00 10.60  ? 165  GLU A N     1 
ATOM   1202 C CA    . GLU A 1 171 ? 1.947  21.057 24.294 1.00 11.68  ? 165  GLU A CA    1 
ATOM   1203 C C     . GLU A 1 171 ? 2.756  22.215 23.729 1.00 10.74  ? 165  GLU A C     1 
ATOM   1204 O O     . GLU A 1 171 ? 2.628  22.522 22.526 1.00 11.31  ? 165  GLU A O     1 
ATOM   1205 C CB    . GLU A 1 171 ? 0.578  21.463 24.852 1.00 13.84  ? 165  GLU A CB    1 
ATOM   1206 C CG    . GLU A 1 171 ? -0.346 22.199 23.893 1.00 18.00  ? 165  GLU A CG    1 
ATOM   1207 C CD    . GLU A 1 171 ? -0.646 21.429 22.633 1.00 24.73  ? 165  GLU A CD    1 
ATOM   1208 O OE1   . GLU A 1 171 ? -0.625 20.189 22.602 1.00 22.60  ? 165  GLU A OE1   1 
ATOM   1209 O OE2   . GLU A 1 171 ? -1.081 22.104 21.664 1.00 28.93  ? 165  GLU A OE2   1 
ATOM   1210 N N     . ASP A 1 172 ? 3.577  22.859 24.555 1.00 10.41  ? 166  ASP A N     1 
ATOM   1211 C CA    . ASP A 1 172 ? 4.454  23.925 24.050 1.00 10.39  ? 166  ASP A CA    1 
ATOM   1212 C C     . ASP A 1 172 ? 5.461  23.365 23.040 1.00 9.62   ? 166  ASP A C     1 
ATOM   1213 O O     . ASP A 1 172 ? 5.711  23.985 22.013 1.00 10.00  ? 166  ASP A O     1 
ATOM   1214 C CB    . ASP A 1 172 ? 5.195  24.588 25.202 1.00 10.30  ? 166  ASP A CB    1 
ATOM   1215 C CG    . ASP A 1 172 ? 4.296  25.429 26.092 1.00 15.20  ? 166  ASP A CG    1 
ATOM   1216 O OD1   . ASP A 1 172 ? 4.666  25.607 27.279 1.00 17.01  ? 166  ASP A OD1   1 
ATOM   1217 O OD2   . ASP A 1 172 ? 3.279  25.954 25.599 1.00 18.41  ? 166  ASP A OD2   1 
ATOM   1218 N N     . TYR A 1 173 ? 6.027  22.178 23.297 1.00 9.57   ? 167  TYR A N     1 
ATOM   1219 C CA    . TYR A 1 173 ? 6.845  21.552 22.272 1.00 8.56   ? 167  TYR A CA    1 
ATOM   1220 C C     . TYR A 1 173 ? 6.031  21.245 21.017 1.00 9.66   ? 167  TYR A C     1 
ATOM   1221 O O     . TYR A 1 173 ? 6.529  21.482 19.910 1.00 10.54  ? 167  TYR A O     1 
ATOM   1222 C CB    . TYR A 1 173 ? 7.462  20.242 22.789 1.00 10.47  ? 167  TYR A CB    1 
ATOM   1223 C CG    . TYR A 1 173 ? 8.639  20.365 23.716 1.00 8.74   ? 167  TYR A CG    1 
ATOM   1224 C CD1   . TYR A 1 173 ? 9.905  20.562 23.186 1.00 9.34   ? 167  TYR A CD1   1 
ATOM   1225 C CD2   . TYR A 1 173 ? 8.494  20.212 25.079 1.00 9.00   ? 167  TYR A CD2   1 
ATOM   1226 C CE1   . TYR A 1 173 ? 11.013 20.662 24.027 1.00 9.11   ? 167  TYR A CE1   1 
ATOM   1227 C CE2   . TYR A 1 173 ? 9.580  20.249 25.915 1.00 9.52   ? 167  TYR A CE2   1 
ATOM   1228 C CZ    . TYR A 1 173 ? 10.835 20.518 25.388 1.00 9.85   ? 167  TYR A CZ    1 
ATOM   1229 O OH    . TYR A 1 173 ? 11.915 20.542 26.277 1.00 10.78  ? 167  TYR A OH    1 
ATOM   1230 N N     . ARG A 1 174 ? 4.798  20.751 21.159 1.00 10.79  ? 168  ARG A N     1 
ATOM   1231 C CA    . ARG A 1 174 ? 3.984  20.407 19.994 1.00 11.63  ? 168  ARG A CA    1 
ATOM   1232 C C     . ARG A 1 174 ? 3.697  21.655 19.157 1.00 10.24  ? 168  ARG A C     1 
ATOM   1233 O O     . ARG A 1 174 ? 3.847  21.642 17.924 1.00 11.86  ? 168  ARG A O     1 
ATOM   1234 C CB    . ARG A 1 174 ? 2.707  19.739 20.497 1.00 11.86  ? 168  ARG A CB    1 
ATOM   1235 C CG    . ARG A 1 174 ? 2.053  19.069 19.289 1.00 15.57  ? 168  ARG A CG    1 
ATOM   1236 C CD    . ARG A 1 174 ? 0.794  18.351 19.714 1.00 18.47  ? 168  ARG A CD    1 
ATOM   1237 N NE    . ARG A 1 174 ? -0.211 19.360 19.857 1.00 20.23  ? 168  ARG A NE    1 
ATOM   1238 C CZ    . ARG A 1 174 ? -0.937 19.810 18.849 1.00 26.23  ? 168  ARG A CZ    1 
ATOM   1239 N NH1   . ARG A 1 174 ? -0.917 19.205 17.655 1.00 26.17  ? 168  ARG A NH1   1 
ATOM   1240 N NH2   . ARG A 1 174 ? -1.646 20.917 19.024 1.00 33.74  ? 168  ARG A NH2   1 
ATOM   1241 N N     . ARG A 1 175 ? 3.317  22.757 19.818 1.00 9.99   ? 169  ARG A N     1 
ATOM   1242 C CA    . ARG A 1 175 ? 2.974  23.978 19.085 1.00 10.27  ? 169  ARG A CA    1 
ATOM   1243 C C     . ARG A 1 175 ? 4.206  24.590 18.453 1.00 11.39  ? 169  ARG A C     1 
ATOM   1244 O O     . ARG A 1 175 ? 4.125  25.119 17.335 1.00 11.93  ? 169  ARG A O     1 
ATOM   1245 C CB    . ARG A 1 175 ? 2.332  25.000 20.003 1.00 12.99  ? 169  ARG A CB    1 
ATOM   1246 C CG    . ARG A 1 175 ? 1.010  24.480 20.577 1.00 21.36  ? 169  ARG A CG    1 
ATOM   1247 C CD    . ARG A 1 175 ? 0.297  25.531 21.407 1.00 33.33  ? 169  ARG A CD    1 
ATOM   1248 N NE    . ARG A 1 175 ? -0.929 24.968 21.969 1.00 44.22  ? 169  ARG A NE    1 
ATOM   1249 C CZ    . ARG A 1 175 ? -2.090 25.598 22.060 1.00 61.84  ? 169  ARG A CZ    1 
ATOM   1250 N NH1   . ARG A 1 175 ? -2.252 26.818 21.570 1.00 67.18  ? 169  ARG A NH1   1 
ATOM   1251 N NH2   . ARG A 1 175 ? -3.110 24.994 22.671 1.00 50.46  ? 169  ARG A NH2   1 
ATOM   1252 N N     . SER A 1 176 ? 5.366  24.507 19.127 1.00 10.34  ? 170  SER A N     1 
ATOM   1253 C CA    . SER A 1 176 ? 6.588  25.034 18.577 1.00 9.75   ? 170  SER A CA    1 
ATOM   1254 C C     . SER A 1 176 ? 7.014  24.221 17.361 1.00 10.22  ? 170  SER A C     1 
ATOM   1255 O O     . SER A 1 176 ? 7.540  24.797 16.405 1.00 10.20  ? 170  SER A O     1 
ATOM   1256 C CB    . SER A 1 176 ? 7.680  25.065 19.653 1.00 11.24  ? 170  SER A CB    1 
ATOM   1257 O OG    . SER A 1 176 ? 7.390  26.051 20.629 1.00 13.21  ? 170  SER A OG    1 
ATOM   1258 N N     . ALA A 1 177 ? 6.806  22.886 17.370 1.00 9.78   ? 171  ALA A N     1 
ATOM   1259 C CA    . ALA A 1 177 ? 7.148  22.078 16.203 1.00 9.14   ? 171  ALA A CA    1 
ATOM   1260 C C     . ALA A 1 177 ? 6.277  22.469 15.019 1.00 10.66  ? 171  ALA A C     1 
ATOM   1261 O O     . ALA A 1 177 ? 6.786  22.579 13.895 1.00 10.95  ? 171  ALA A O     1 
ATOM   1262 C CB    . ALA A 1 177 ? 6.984  20.581 16.529 1.00 11.49  ? 171  ALA A CB    1 
ATOM   1263 N N     . LEU A 1 178 ? 4.985  22.713 15.271 1.00 11.06  ? 172  LEU A N     1 
ATOM   1264 C CA    . LEU A 1 178 ? 4.113  23.154 14.182 1.00 10.55  ? 172  LEU A CA    1 
ATOM   1265 C C     . LEU A 1 178 ? 4.547  24.514 13.661 1.00 10.90  ? 172  LEU A C     1 
ATOM   1266 O O     . LEU A 1 178 ? 4.547  24.737 12.443 1.00 11.36  ? 172  LEU A O     1 
ATOM   1267 C CB    . LEU A 1 178 ? 2.645  23.187 14.646 1.00 11.98  ? 172  LEU A CB    1 
ATOM   1268 C CG    . LEU A 1 178 ? 2.070  21.813 14.876 1.00 12.23  ? 172  LEU A CG    1 
ATOM   1269 C CD1   . LEU A 1 178 ? 0.788  21.942 15.660 1.00 17.36  ? 172  LEU A CD1   1 
ATOM   1270 C CD2   . LEU A 1 178 ? 1.794  21.088 13.541 1.00 14.33  ? 172  LEU A CD2   1 
ATOM   1271 N N     . ASN A 1 179 ? 4.928  25.429 14.564 1.00 9.77   ? 173  ASN A N     1 
ATOM   1272 C CA    . ASN A 1 179 ? 5.428  26.733 14.135 1.00 9.58   ? 173  ASN A CA    1 
ATOM   1273 C C     . ASN A 1 179 ? 6.713  26.599 13.322 1.00 11.31  ? 173  ASN A C     1 
ATOM   1274 O O     . ASN A 1 179 ? 6.925  27.330 12.346 1.00 10.91  ? 173  ASN A O     1 
ATOM   1275 C CB    . ASN A 1 179 ? 5.672  27.623 15.349 1.00 10.73  ? 173  ASN A CB    1 
ATOM   1276 C CG    . ASN A 1 179 ? 4.419  28.261 15.878 1.00 16.17  ? 173  ASN A CG    1 
ATOM   1277 O OD1   . ASN A 1 179 ? 3.323  28.128 15.312 1.00 16.44  ? 173  ASN A OD1   1 
ATOM   1278 N ND2   . ASN A 1 179 ? 4.564  28.948 17.008 1.00 16.97  ? 173  ASN A ND2   1 
ATOM   1279 N N     . ALA A 1 180 ? 7.590  25.667 13.676 1.00 9.61   ? 174  ALA A N     1 
ATOM   1280 C CA    . ALA A 1 180 ? 8.795  25.473 12.896 1.00 9.04   ? 174  ALA A CA    1 
ATOM   1281 C C     . ALA A 1 180 ? 8.455  25.042 11.479 1.00 9.51   ? 174  ALA A C     1 
ATOM   1282 O O     . ALA A 1 180 ? 9.069  25.526 10.522 1.00 10.30  ? 174  ALA A O     1 
ATOM   1283 C CB    . ALA A 1 180 ? 9.699  24.457 13.595 1.00 10.91  ? 174  ALA A CB    1 
ATOM   1284 N N     . ILE A 1 181 ? 7.507  24.100 11.325 1.00 10.37  ? 175  ILE A N     1 
ATOM   1285 C CA    . ILE A 1 181 ? 7.102  23.701 9.978  1.00 10.99  ? 175  ILE A CA    1 
ATOM   1286 C C     . ILE A 1 181 ? 6.495  24.884 9.245  1.00 12.04  ? 175  ILE A C     1 
ATOM   1287 O O     . ILE A 1 181 ? 6.791  25.100 8.038  1.00 11.92  ? 175  ILE A O     1 
ATOM   1288 C CB    . ILE A 1 181 ? 6.146  22.502 10.093 1.00 12.94  ? 175  ILE A CB    1 
ATOM   1289 C CG1   . ILE A 1 181 ? 6.852  21.260 10.608 1.00 14.40  ? 175  ILE A CG1   1 
ATOM   1290 C CG2   . ILE A 1 181 ? 5.446  22.268 8.711  1.00 15.32  ? 175  ILE A CG2   1 
ATOM   1291 C CD1   . ILE A 1 181 ? 8.059  20.907 9.904  1.00 15.34  ? 175  ILE A CD1   1 
ATOM   1292 N N     . GLU A 1 182 ? 5.725  25.730 9.953  1.00 10.34  ? 176  GLU A N     1 
ATOM   1293 C CA    . GLU A 1 182 ? 5.164  26.915 9.299  1.00 11.94  ? 176  GLU A CA    1 
ATOM   1294 C C     . GLU A 1 182 ? 6.248  27.859 8.794  1.00 13.83  ? 176  GLU A C     1 
ATOM   1295 O O     . GLU A 1 182 ? 6.087  28.498 7.735  1.00 14.87  ? 176  GLU A O     1 
ATOM   1296 C CB    . GLU A 1 182 ? 4.258  27.637 10.308 1.00 13.34  ? 176  GLU A CB    1 
ATOM   1297 C CG    . GLU A 1 182 ? 3.436  28.797 9.689  1.00 17.65  ? 176  GLU A CG    1 
ATOM   1298 C CD    . GLU A 1 182 ? 2.586  29.552 10.687 1.00 30.83  ? 176  GLU A CD    1 
ATOM   1299 O OE1   . GLU A 1 182 ? 2.392  30.775 10.524 1.00 34.10  ? 176  GLU A OE1   1 
ATOM   1300 O OE2   . GLU A 1 182 ? 2.094  28.918 11.635 1.00 30.18  ? 176  GLU A OE2   1 
ATOM   1301 N N     . ALA A 1 183 ? 7.371  27.998 9.504  1.00 11.80  ? 177  ALA A N     1 
ATOM   1302 C CA    . ALA A 1 183 ? 8.480  28.834 9.064  1.00 11.23  ? 177  ALA A CA    1 
ATOM   1303 C C     . ALA A 1 183 ? 9.244  28.195 7.931  1.00 12.67  ? 177  ALA A C     1 
ATOM   1304 O O     . ALA A 1 183 ? 10.104 28.872 7.370  1.00 14.48  ? 177  ALA A O     1 
ATOM   1305 C CB    . ALA A 1 183 ? 9.427  29.069 10.235 1.00 12.04  ? 177  ALA A CB    1 
ATOM   1306 N N     . GLY A 1 184 ? 8.964  26.961 7.608  1.00 10.44  ? 178  GLY A N     1 
ATOM   1307 C CA    . GLY A 1 184 ? 9.622  26.257 6.535  1.00 11.70  ? 178  GLY A CA    1 
ATOM   1308 C C     . GLY A 1 184 ? 10.745 25.324 6.948  1.00 10.41  ? 178  GLY A C     1 
ATOM   1309 O O     . GLY A 1 184 ? 11.391 24.727 6.072  1.00 11.16  ? 178  GLY A O     1 
ATOM   1310 N N     . PHE A 1 185 ? 11.057 25.233 8.254  1.00 9.63   ? 179  PHE A N     1 
ATOM   1311 C CA    . PHE A 1 185 ? 12.061 24.238 8.645  1.00 9.24   ? 179  PHE A CA    1 
ATOM   1312 C C     . PHE A 1 185 ? 11.734 22.852 8.123  1.00 10.03  ? 179  PHE A C     1 
ATOM   1313 O O     . PHE A 1 185 ? 10.584 22.450 8.025  1.00 11.48  ? 179  PHE A O     1 
ATOM   1314 C CB    . PHE A 1 185 ? 12.150 24.182 10.180 1.00 10.20  ? 179  PHE A CB    1 
ATOM   1315 C CG    . PHE A 1 185 ? 12.925 25.337 10.792 1.00 9.06   ? 179  PHE A CG    1 
ATOM   1316 C CD1   . PHE A 1 185 ? 14.330 25.342 10.750 1.00 9.56   ? 179  PHE A CD1   1 
ATOM   1317 C CD2   . PHE A 1 185 ? 12.257 26.384 11.376 1.00 8.85   ? 179  PHE A CD2   1 
ATOM   1318 C CE1   . PHE A 1 185 ? 15.049 26.399 11.304 1.00 9.78   ? 179  PHE A CE1   1 
ATOM   1319 C CE2   . PHE A 1 185 ? 12.983 27.454 11.954 1.00 9.83   ? 179  PHE A CE2   1 
ATOM   1320 C CZ    . PHE A 1 185 ? 14.374 27.455 11.900 1.00 10.51  ? 179  PHE A CZ    1 
ATOM   1321 N N     . ASP A 1 186 ? 12.792 22.111 7.829  1.00 9.56   ? 180  ASP A N     1 
ATOM   1322 C CA    . ASP A 1 186 ? 12.610 20.718 7.396  1.00 9.61   ? 180  ASP A CA    1 
ATOM   1323 C C     . ASP A 1 186 ? 12.221 19.808 8.562  1.00 9.50   ? 180  ASP A C     1 
ATOM   1324 O O     . ASP A 1 186 ? 11.628 18.742 8.328  1.00 11.11  ? 180  ASP A O     1 
ATOM   1325 C CB    . ASP A 1 186 ? 13.959 20.268 6.816  1.00 10.20  ? 180  ASP A CB    1 
ATOM   1326 C CG    . ASP A 1 186 ? 14.282 21.066 5.569  1.00 11.25  ? 180  ASP A CG    1 
ATOM   1327 O OD1   . ASP A 1 186 ? 13.507 20.967 4.571  1.00 14.28  ? 180  ASP A OD1   1 
ATOM   1328 O OD2   . ASP A 1 186 ? 15.216 21.861 5.582  1.00 12.07  ? 180  ASP A OD2   1 
ATOM   1329 N N     . GLY A 1 187 ? 12.518 20.207 9.809  1.00 9.24   ? 181  GLY A N     1 
ATOM   1330 C CA    . GLY A 1 187 ? 12.159 19.415 10.968 1.00 9.89   ? 181  GLY A CA    1 
ATOM   1331 C C     . GLY A 1 187 ? 12.660 20.122 12.194 1.00 8.33   ? 181  GLY A C     1 
ATOM   1332 O O     . GLY A 1 187 ? 13.065 21.302 12.147 1.00 8.62   ? 181  GLY A O     1 
ATOM   1333 N N     . ILE A 1 188 ? 12.544 19.399 13.299 1.00 8.49   ? 182  ILE A N     1 
ATOM   1334 C CA    . ILE A 1 188 ? 12.958 19.936 14.592 1.00 7.92   ? 182  ILE A CA    1 
ATOM   1335 C C     . ILE A 1 188 ? 13.828 18.902 15.301 1.00 9.22   ? 182  ILE A C     1 
ATOM   1336 O O     . ILE A 1 188 ? 13.722 17.693 15.073 1.00 9.46   ? 182  ILE A O     1 
ATOM   1337 C CB    . ILE A 1 188 ? 11.770 20.365 15.520 1.00 8.95   ? 182  ILE A CB    1 
ATOM   1338 C CG1   . ILE A 1 188 ? 10.871 19.184 15.906 1.00 9.41   ? 182  ILE A CG1   1 
ATOM   1339 C CG2   . ILE A 1 188 ? 10.954 21.425 14.787 1.00 10.34  ? 182  ILE A CG2   1 
ATOM   1340 C CD1   . ILE A 1 188 ? 11.319 18.439 17.196 1.00 12.25  ? 182  ILE A CD1   1 
ATOM   1341 N N     . GLU A 1 189 ? 14.675 19.394 16.206 1.00 7.96   ? 183  GLU A N     1 
ATOM   1342 C CA    . GLU A 1 189 ? 15.415 18.523 17.140 1.00 7.99   ? 183  GLU A CA    1 
ATOM   1343 C C     . GLU A 1 189 ? 14.942 18.769 18.562 1.00 7.07   ? 183  GLU A C     1 
ATOM   1344 O O     . GLU A 1 189 ? 14.898 19.937 18.994 1.00 9.16   ? 183  GLU A O     1 
ATOM   1345 C CB    . GLU A 1 189 ? 16.908 18.804 17.041 1.00 8.66   ? 183  GLU A CB    1 
ATOM   1346 C CG    . GLU A 1 189 ? 17.733 17.870 17.971 1.00 10.56  ? 183  GLU A CG    1 
ATOM   1347 C CD    . GLU A 1 189 ? 19.206 18.051 17.820 1.00 10.25  ? 183  GLU A CD    1 
ATOM   1348 O OE1   . GLU A 1 189 ? 19.821 17.394 16.962 1.00 10.82  ? 183  GLU A OE1   1 
ATOM   1349 O OE2   . GLU A 1 189 ? 19.812 18.859 18.556 1.00 10.29  ? 183  GLU A OE2   1 
ATOM   1350 N N     . ILE A 1 190 ? 14.640 17.736 19.318 1.00 8.26   ? 184  ILE A N     1 
ATOM   1351 C CA    . ILE A 1 190 ? 14.305 17.881 20.734 1.00 8.57   ? 184  ILE A CA    1 
ATOM   1352 C C     . ILE A 1 190 ? 15.623 17.969 21.512 1.00 8.67   ? 184  ILE A C     1 
ATOM   1353 O O     . ILE A 1 190 ? 16.432 17.014 21.501 1.00 9.87   ? 184  ILE A O     1 
ATOM   1354 C CB    . ILE A 1 190 ? 13.466 16.707 21.212 1.00 9.16   ? 184  ILE A CB    1 
ATOM   1355 C CG1   . ILE A 1 190 ? 12.083 16.688 20.539 1.00 9.80   ? 184  ILE A CG1   1 
ATOM   1356 C CG2   . ILE A 1 190 ? 13.321 16.722 22.745 1.00 11.41  ? 184  ILE A CG2   1 
ATOM   1357 C CD1   . ILE A 1 190 ? 11.278 17.954 20.796 1.00 10.58  ? 184  ILE A CD1   1 
ATOM   1358 N N     . HIS A 1 191 ? 15.862 19.101 22.195 1.00 8.15   ? 185  HIS A N     1 
ATOM   1359 C CA    . HIS A 1 191 ? 17.037 19.236 23.087 1.00 8.74   ? 185  HIS A CA    1 
ATOM   1360 C C     . HIS A 1 191 ? 16.760 18.501 24.392 1.00 10.23  ? 185  HIS A C     1 
ATOM   1361 O O     . HIS A 1 191 ? 16.109 19.048 25.280 1.00 10.02  ? 185  HIS A O     1 
ATOM   1362 C CB    . HIS A 1 191 ? 17.349 20.695 23.336 1.00 8.13   ? 185  HIS A CB    1 
ATOM   1363 C CG    . HIS A 1 191 ? 18.668 20.926 24.010 1.00 7.42   ? 185  HIS A CG    1 
ATOM   1364 N ND1   . HIS A 1 191 ? 19.344 19.941 24.718 1.00 10.68  ? 185  HIS A ND1   1 
ATOM   1365 C CD2   . HIS A 1 191 ? 19.441 22.030 24.006 1.00 10.83  ? 185  HIS A CD2   1 
ATOM   1366 C CE1   . HIS A 1 191 ? 20.461 20.492 25.191 1.00 11.68  ? 185  HIS A CE1   1 
ATOM   1367 N NE2   . HIS A 1 191 ? 20.556 21.747 24.743 1.00 9.97   ? 185  HIS A NE2   1 
ATOM   1368 N N     . GLY A 1 192 ? 17.243 17.260 24.490 1.00 8.23   ? 186  GLY A N     1 
ATOM   1369 C CA    . GLY A 1 192 ? 17.126 16.472 25.717 1.00 8.79   ? 186  GLY A CA    1 
ATOM   1370 C C     . GLY A 1 192 ? 18.430 16.300 26.447 1.00 8.98   ? 186  GLY A C     1 
ATOM   1371 O O     . GLY A 1 192 ? 18.588 15.264 27.145 1.00 10.60  ? 186  GLY A O     1 
ATOM   1372 N N     . ALA A 1 193 ? 19.368 17.186 26.250 1.00 8.78   ? 187  ALA A N     1 
ATOM   1373 C CA    . ALA A 1 193 ? 20.737 17.027 26.715 1.00 9.80   ? 187  ALA A CA    1 
ATOM   1374 C C     . ALA A 1 193 ? 21.100 18.103 27.769 1.00 9.03   ? 187  ALA A C     1 
ATOM   1375 O O     . ALA A 1 193 ? 20.330 19.027 28.106 1.00 9.76   ? 187  ALA A O     1 
ATOM   1376 C CB    . ALA A 1 193 ? 21.685 17.076 25.498 1.00 11.43  ? 187  ALA A CB    1 
ATOM   1377 N N     . HIS A 1 194 ? 22.319 17.960 28.301 1.00 10.41  ? 188  HIS A N     1 
ATOM   1378 C CA    . HIS A 1 194 ? 23.086 19.030 28.972 1.00 9.97   ? 188  HIS A CA    1 
ATOM   1379 C C     . HIS A 1 194 ? 22.460 19.574 30.248 1.00 11.45  ? 188  HIS A C     1 
ATOM   1380 O O     . HIS A 1 194 ? 22.717 20.736 30.638 1.00 11.73  ? 188  HIS A O     1 
ATOM   1381 C CB    . HIS A 1 194 ? 23.433 20.193 28.021 1.00 11.58  ? 188  HIS A CB    1 
ATOM   1382 C CG    . HIS A 1 194 ? 24.266 19.827 26.845 1.00 13.01  ? 188  HIS A CG    1 
ATOM   1383 N ND1   . HIS A 1 194 ? 23.878 20.174 25.569 1.00 16.48  ? 188  HIS A ND1   1 
ATOM   1384 C CD2   . HIS A 1 194 ? 25.468 19.219 26.720 1.00 30.94  ? 188  HIS A CD2   1 
ATOM   1385 C CE1   . HIS A 1 194 ? 24.768 19.731 24.701 1.00 17.92  ? 188  HIS A CE1   1 
ATOM   1386 N NE2   . HIS A 1 194 ? 25.772 19.199 25.373 1.00 23.17  ? 188  HIS A NE2   1 
ATOM   1387 N N     . GLY A 1 195 ? 21.661 18.778 30.942 1.00 10.19  ? 189  GLY A N     1 
ATOM   1388 C CA    . GLY A 1 195 ? 21.145 19.233 32.212 1.00 9.31   ? 189  GLY A CA    1 
ATOM   1389 C C     . GLY A 1 195 ? 20.008 20.216 32.151 1.00 9.73   ? 189  GLY A C     1 
ATOM   1390 O O     . GLY A 1 195 ? 19.638 20.786 33.178 1.00 9.85   ? 189  GLY A O     1 
ATOM   1391 N N     . TYR A 1 196 ? 19.364 20.340 30.976 1.00 8.56   ? 190  TYR A N     1 
ATOM   1392 C CA    . TYR A 1 196 ? 18.207 21.223 30.776 1.00 8.16   ? 190  TYR A CA    1 
ATOM   1393 C C     . TYR A 1 196 ? 16.936 20.453 31.143 1.00 8.67   ? 190  TYR A C     1 
ATOM   1394 O O     . TYR A 1 196 ? 16.997 19.437 31.825 1.00 8.89   ? 190  TYR A O     1 
ATOM   1395 C CB    . TYR A 1 196 ? 18.299 21.859 29.387 1.00 8.98   ? 190  TYR A CB    1 
ATOM   1396 C CG    . TYR A 1 196 ? 19.484 22.776 29.294 1.00 8.73   ? 190  TYR A CG    1 
ATOM   1397 C CD1   . TYR A 1 196 ? 19.621 23.885 30.104 1.00 9.20   ? 190  TYR A CD1   1 
ATOM   1398 C CD2   . TYR A 1 196 ? 20.489 22.518 28.361 1.00 10.59  ? 190  TYR A CD2   1 
ATOM   1399 C CE1   . TYR A 1 196 ? 20.737 24.720 30.006 1.00 10.47  ? 190  TYR A CE1   1 
ATOM   1400 C CE2   . TYR A 1 196 ? 21.594 23.312 28.280 1.00 10.87  ? 190  TYR A CE2   1 
ATOM   1401 C CZ    . TYR A 1 196 ? 21.691 24.385 29.065 1.00 10.02  ? 190  TYR A CZ    1 
ATOM   1402 O OH    . TYR A 1 196 ? 22.832 25.260 28.950 1.00 15.02  ? 190  TYR A OH    1 
ATOM   1403 N N     . LEU A 1 197 ? 15.749 20.983 30.819 1.00 8.88   ? 191  LEU A N     1 
ATOM   1404 C CA    . LEU A 1 197 ? 14.505 20.461 31.424 1.00 9.15   ? 191  LEU A CA    1 
ATOM   1405 C C     . LEU A 1 197 ? 14.348 18.949 31.254 1.00 9.71   ? 191  LEU A C     1 
ATOM   1406 O O     . LEU A 1 197 ? 14.006 18.235 32.197 1.00 8.88   ? 191  LEU A O     1 
ATOM   1407 C CB    . LEU A 1 197 ? 13.285 21.203 30.846 1.00 8.95   ? 191  LEU A CB    1 
ATOM   1408 C CG    . LEU A 1 197 ? 11.952 20.737 31.436 1.00 9.59   ? 191  LEU A CG    1 
ATOM   1409 C CD1   . LEU A 1 197 ? 11.831 21.109 32.918 1.00 10.44  ? 191  LEU A CD1   1 
ATOM   1410 C CD2   . LEU A 1 197 ? 10.761 21.350 30.724 1.00 11.19  ? 191  LEU A CD2   1 
ATOM   1411 N N     . ILE A 1 198 ? 14.479 18.469 30.032 1.00 9.66   ? 192  ILE A N     1 
ATOM   1412 C CA    . ILE A 1 198 ? 14.280 17.034 29.800 1.00 9.35   ? 192  ILE A CA    1 
ATOM   1413 C C     . ILE A 1 198 ? 15.268 16.208 30.606 1.00 10.05  ? 192  ILE A C     1 
ATOM   1414 O O     . ILE A 1 198 ? 14.891 15.210 31.249 1.00 9.19   ? 192  ILE A O     1 
ATOM   1415 C CB    . ILE A 1 198 ? 14.306 16.730 28.301 1.00 8.19   ? 192  ILE A CB    1 
ATOM   1416 C CG1   . ILE A 1 198 ? 13.040 17.286 27.655 1.00 10.26  ? 192  ILE A CG1   1 
ATOM   1417 C CG2   . ILE A 1 198 ? 14.401 15.207 28.041 1.00 11.62  ? 192  ILE A CG2   1 
ATOM   1418 C CD1   . ILE A 1 198 ? 13.079 17.276 26.127 1.00 10.54  ? 192  ILE A CD1   1 
ATOM   1419 N N     . ASP A 1 199 ? 16.555 16.599 30.592 1.00 9.91   ? 193  ASP A N     1 
ATOM   1420 C CA    . ASP A 1 199 ? 17.555 15.923 31.409 1.00 10.51  ? 193  ASP A CA    1 
ATOM   1421 C C     . ASP A 1 199 ? 17.271 16.009 32.896 1.00 9.69   ? 193  ASP A C     1 
ATOM   1422 O O     . ASP A 1 199 ? 17.670 15.102 33.629 1.00 11.90  ? 193  ASP A O     1 
ATOM   1423 C CB    . ASP A 1 199 ? 18.916 16.512 31.060 1.00 13.37  ? 193  ASP A CB    1 
ATOM   1424 C CG    . ASP A 1 199 ? 20.017 15.529 31.030 1.00 13.93  ? 193  ASP A CG    1 
ATOM   1425 O OD1   . ASP A 1 199 ? 19.827 14.337 30.737 1.00 14.70  ? 193  ASP A OD1   1 
ATOM   1426 O OD2   . ASP A 1 199 ? 21.170 16.002 31.307 1.00 16.54  ? 193  ASP A OD2   1 
ATOM   1427 N N     . GLN A 1 200 ? 16.596 17.068 33.365 1.00 9.13   ? 194  GLN A N     1 
ATOM   1428 C CA    . GLN A 1 200 ? 16.209 17.159 34.771 1.00 10.40  ? 194  GLN A CA    1 
ATOM   1429 C C     . GLN A 1 200 ? 15.190 16.100 35.155 1.00 9.41   ? 194  GLN A C     1 
ATOM   1430 O O     . GLN A 1 200 ? 15.088 15.737 36.334 1.00 10.81  ? 194  GLN A O     1 
ATOM   1431 C CB    . GLN A 1 200 ? 15.674 18.586 35.079 1.00 8.96   ? 194  GLN A CB    1 
ATOM   1432 C CG    . GLN A 1 200 ? 16.801 19.629 35.047 1.00 8.98   ? 194  GLN A CG    1 
ATOM   1433 C CD    . GLN A 1 200 ? 16.286 21.008 34.666 1.00 8.99   ? 194  GLN A CD    1 
ATOM   1434 O OE1   . GLN A 1 200 ? 15.194 21.411 35.063 1.00 10.03  ? 194  GLN A OE1   1 
ATOM   1435 N NE2   . GLN A 1 200 ? 17.105 21.764 33.950 1.00 8.94   ? 194  GLN A NE2   1 
ATOM   1436 N N     . PHE A 1 201 ? 14.407 15.600 34.175 1.00 9.13   ? 195  PHE A N     1 
ATOM   1437 C CA    . PHE A 1 201 ? 13.561 14.417 34.408 1.00 9.57   ? 195  PHE A CA    1 
ATOM   1438 C C     . PHE A 1 201 ? 14.317 13.098 34.237 1.00 9.70   ? 195  PHE A C     1 
ATOM   1439 O O     . PHE A 1 201 ? 14.092 12.158 35.014 1.00 10.86  ? 195  PHE A O     1 
ATOM   1440 C CB    . PHE A 1 201 ? 12.319 14.464 33.486 1.00 10.88  ? 195  PHE A CB    1 
ATOM   1441 C CG    . PHE A 1 201 ? 11.233 15.406 33.958 1.00 9.66   ? 195  PHE A CG    1 
ATOM   1442 C CD1   . PHE A 1 201 ? 11.239 16.753 33.643 1.00 11.03  ? 195  PHE A CD1   1 
ATOM   1443 C CD2   . PHE A 1 201 ? 10.235 14.929 34.794 1.00 9.62   ? 195  PHE A CD2   1 
ATOM   1444 C CE1   . PHE A 1 201 ? 10.251 17.630 34.107 1.00 10.74  ? 195  PHE A CE1   1 
ATOM   1445 C CE2   . PHE A 1 201 ? 9.236  15.747 35.257 1.00 10.21  ? 195  PHE A CE2   1 
ATOM   1446 C CZ    . PHE A 1 201 ? 9.238  17.140 34.924 1.00 11.21  ? 195  PHE A CZ    1 
ATOM   1447 N N     . LEU A 1 202 ? 15.221 13.021 33.260 1.00 9.31   ? 196  LEU A N     1 
ATOM   1448 C CA    . LEU A 1 202 ? 15.931 11.778 32.959 1.00 9.56   ? 196  LEU A CA    1 
ATOM   1449 C C     . LEU A 1 202 ? 16.887 11.363 34.042 1.00 10.29  ? 196  LEU A C     1 
ATOM   1450 O O     . LEU A 1 202 ? 16.971 10.163 34.356 1.00 11.81  ? 196  LEU A O     1 
ATOM   1451 C CB    . LEU A 1 202 ? 16.750 11.920 31.668 1.00 11.05  ? 196  LEU A CB    1 
ATOM   1452 C CG    . LEU A 1 202 ? 15.960 11.956 30.394 1.00 9.67   ? 196  LEU A CG    1 
ATOM   1453 C CD1   . LEU A 1 202 ? 16.985 12.253 29.240 1.00 12.49  ? 196  LEU A CD1   1 
ATOM   1454 C CD2   . LEU A 1 202 ? 15.255 10.618 30.119 1.00 10.39  ? 196  LEU A CD2   1 
ATOM   1455 N N     . LYS A 1 203 ? 17.647 12.303 34.606 1.00 10.06  ? 197  LYS A N     1 
ATOM   1456 C CA    . LYS A 1 203 ? 18.844 11.976 35.417 1.00 11.52  ? 197  LYS A CA    1 
ATOM   1457 C C     . LYS A 1 203 ? 18.416 11.709 36.865 1.00 11.45  ? 197  LYS A C     1 
ATOM   1458 O O     . LYS A 1 203 ? 17.774 12.548 37.500 1.00 12.40  ? 197  LYS A O     1 
ATOM   1459 C CB    . LYS A 1 203 ? 19.863 13.118 35.353 1.00 10.58  ? 197  LYS A CB    1 
ATOM   1460 C CG    . LYS A 1 203 ? 20.445 13.416 33.948 1.00 15.81  ? 197  LYS A CG    1 
ATOM   1461 C CD    . LYS A 1 203 ? 21.430 12.374 33.643 1.00 16.28  ? 197  LYS A CD    1 
ATOM   1462 C CE    . LYS A 1 203 ? 21.996 12.509 32.215 1.00 13.35  ? 197  LYS A CE    1 
ATOM   1463 N NZ    . LYS A 1 203 ? 22.887 13.652 31.992 1.00 16.56  ? 197  LYS A NZ    1 
ATOM   1464 N N     . ASP A 1 204 ? 18.856 10.567 37.434 1.00 11.91  ? 198  ASP A N     1 
ATOM   1465 C CA    . ASP A 1 204 ? 18.497 10.266 38.818 1.00 13.63  ? 198  ASP A CA    1 
ATOM   1466 C C     . ASP A 1 204 ? 19.240 11.127 39.812 1.00 15.52  ? 198  ASP A C     1 
ATOM   1467 O O     . ASP A 1 204 ? 18.811 11.165 40.974 1.00 17.46  ? 198  ASP A O     1 
ATOM   1468 C CB    . ASP A 1 204 ? 18.553 8.766  39.142 1.00 14.86  ? 198  ASP A CB    1 
ATOM   1469 C CG    . ASP A 1 204 ? 19.949 8.192  39.114 1.00 18.78  ? 198  ASP A CG    1 
ATOM   1470 O OD1   . ASP A 1 204 ? 20.954 8.887  38.992 1.00 17.92  ? 198  ASP A OD1   1 
ATOM   1471 O OD2   . ASP A 1 204 ? 20.055 6.937  39.217 1.00 24.11  ? 198  ASP A OD2   1 
ATOM   1472 N N     . GLY A 1 205 ? 20.248 11.873 39.390 1.00 12.72  ? 199  GLY A N     1 
ATOM   1473 C CA    . GLY A 1 205 ? 20.867 12.862 40.257 1.00 14.31  ? 199  GLY A CA    1 
ATOM   1474 C C     . GLY A 1 205 ? 20.025 14.086 40.461 1.00 18.78  ? 199  GLY A C     1 
ATOM   1475 O O     . GLY A 1 205 ? 20.271 14.835 41.428 1.00 20.96  ? 199  GLY A O     1 
ATOM   1476 N N     . ILE A 1 206 ? 18.990 14.282 39.642 1.00 13.18  ? 200  ILE A N     1 
ATOM   1477 C CA    . ILE A 1 206 ? 18.146 15.467 39.712 1.00 15.24  ? 200  ILE A CA    1 
ATOM   1478 C C     . ILE A 1 206 ? 16.742 15.083 40.079 1.00 14.26  ? 200  ILE A C     1 
ATOM   1479 O O     . ILE A 1 206 ? 16.113 15.715 40.942 1.00 19.09  ? 200  ILE A O     1 
ATOM   1480 C CB    . ILE A 1 206 ? 18.172 16.250 38.396 1.00 15.00  ? 200  ILE A CB    1 
ATOM   1481 C CG1   . ILE A 1 206 ? 19.559 16.744 38.081 1.00 15.54  ? 200  ILE A CG1   1 
ATOM   1482 C CG2   . ILE A 1 206 ? 17.232 17.495 38.399 1.00 14.65  ? 200  ILE A CG2   1 
ATOM   1483 C CD1   . ILE A 1 206 ? 19.671 17.422 36.658 1.00 15.20  ? 200  ILE A CD1   1 
ATOM   1484 N N     . ASN A 1 207 ? 16.177 14.095 39.375 1.00 12.65  ? 201  ASN A N     1 
ATOM   1485 C CA    . ASN A 1 207 ? 14.772 13.774 39.529 1.00 13.57  ? 201  ASN A CA    1 
ATOM   1486 C C     . ASN A 1 207 ? 14.597 13.057 40.841 1.00 19.28  ? 201  ASN A C     1 
ATOM   1487 O O     . ASN A 1 207 ? 14.881 11.874 40.948 1.00 21.82  ? 201  ASN A O     1 
ATOM   1488 C CB    . ASN A 1 207 ? 14.308 12.969 38.326 1.00 12.52  ? 201  ASN A CB    1 
ATOM   1489 C CG    . ASN A 1 207 ? 12.848 12.677 38.322 1.00 13.07  ? 201  ASN A CG    1 
ATOM   1490 O OD1   . ASN A 1 207 ? 12.215 12.690 39.396 1.00 14.83  ? 201  ASN A OD1   1 
ATOM   1491 N ND2   . ASN A 1 207 ? 12.279 12.343 37.161 1.00 11.72  ? 201  ASN A ND2   1 
ATOM   1492 N N     . ASP A 1 208 ? 14.046 13.808 41.830 1.00 18.98  ? 202  ASP A N     1 
ATOM   1493 C CA    . ASP A 1 208 ? 13.721 13.279 43.146 1.00 21.11  ? 202  ASP A CA    1 
ATOM   1494 C C     . ASP A 1 208 ? 12.208 13.156 43.331 1.00 22.44  ? 202  ASP A C     1 
ATOM   1495 O O     . ASP A 1 208 ? 11.727 13.278 44.461 1.00 23.17  ? 202  ASP A O     1 
ATOM   1496 C CB    . ASP A 1 208 ? 14.334 14.116 44.292 1.00 17.67  ? 202  ASP A CB    1 
ATOM   1497 C CG    . ASP A 1 208 ? 13.982 15.609 44.277 1.00 24.71  ? 202  ASP A CG    1 
ATOM   1498 O OD1   . ASP A 1 208 ? 13.371 16.141 43.323 1.00 19.19  ? 202  ASP A OD1   1 
ATOM   1499 O OD2   . ASP A 1 208 ? 14.505 16.353 45.186 1.00 20.85  ? 202  ASP A OD2   1 
ATOM   1500 N N     . ARG A 1 209 ? 11.429 12.966 42.242 1.00 17.52  ? 203  ARG A N     1 
ATOM   1501 C CA    . ARG A 1 209 ? 9.968  12.893 42.326 1.00 16.44  ? 203  ARG A CA    1 
ATOM   1502 C C     . ARG A 1 209 ? 9.504  11.555 42.875 1.00 20.48  ? 203  ARG A C     1 
ATOM   1503 O O     . ARG A 1 209 ? 10.157 10.529 42.682 1.00 22.87  ? 203  ARG A O     1 
ATOM   1504 C CB    . ARG A 1 209 ? 9.359  13.102 40.929 1.00 13.67  ? 203  ARG A CB    1 
ATOM   1505 C CG    . ARG A 1 209 ? 9.713  14.448 40.282 1.00 14.15  ? 203  ARG A CG    1 
ATOM   1506 C CD    . ARG A 1 209 ? 9.102  14.507 38.933 1.00 12.48  ? 203  ARG A CD    1 
ATOM   1507 N NE    . ARG A 1 209 ? 7.646  14.683 38.973 1.00 11.54  ? 203  ARG A NE    1 
ATOM   1508 C CZ    . ARG A 1 209 ? 7.042  15.856 38.868 1.00 11.15  ? 203  ARG A CZ    1 
ATOM   1509 N NH1   . ARG A 1 209 ? 7.738  17.007 38.825 1.00 11.01  ? 203  ARG A NH1   1 
ATOM   1510 N NH2   . ARG A 1 209 ? 5.713  15.902 38.783 1.00 13.11  ? 203  ARG A NH2   1 
ATOM   1511 N N     . THR A 1 210 ? 8.324  11.576 43.517 1.00 21.25  ? 204  THR A N     1 
ATOM   1512 C CA    . THR A 1 210 ? 7.653  10.361 43.986 1.00 22.06  ? 204  THR A CA    1 
ATOM   1513 C C     . THR A 1 210 ? 6.339  10.094 43.274 1.00 26.14  ? 204  THR A C     1 
ATOM   1514 O O     . THR A 1 210 ? 5.585  9.203  43.672 1.00 26.10  ? 204  THR A O     1 
ATOM   1515 C CB    . THR A 1 210 ? 7.424  10.411 45.501 1.00 30.96  ? 204  THR A CB    1 
ATOM   1516 O OG1   . THR A 1 210 ? 6.474  11.444 45.782 1.00 30.34  ? 204  THR A OG1   1 
ATOM   1517 C CG2   . THR A 1 210 ? 8.719  10.686 46.214 1.00 30.76  ? 204  THR A CG2   1 
ATOM   1518 N N     . ASP A 1 211 ? 6.041  10.816 42.219 1.00 16.44  ? 205  ASP A N     1 
ATOM   1519 C CA    . ASP A 1 211 ? 4.852  10.550 41.447 1.00 16.25  ? 205  ASP A CA    1 
ATOM   1520 C C     . ASP A 1 211 ? 5.226  9.674  40.230 1.00 15.69  ? 205  ASP A C     1 
ATOM   1521 O O     . ASP A 1 211 ? 6.317  9.088  40.190 1.00 16.24  ? 205  ASP A O     1 
ATOM   1522 C CB    . ASP A 1 211 ? 4.126  11.869 41.083 1.00 18.71  ? 205  ASP A CB    1 
ATOM   1523 C CG    . ASP A 1 211 ? 4.867  12.711 40.007 1.00 14.46  ? 205  ASP A CG    1 
ATOM   1524 O OD1   . ASP A 1 211 ? 6.014  12.366 39.669 1.00 15.36  ? 205  ASP A OD1   1 
ATOM   1525 O OD2   . ASP A 1 211 ? 4.229  13.668 39.570 1.00 17.20  ? 205  ASP A OD2   1 
ATOM   1526 N N     . GLU A 1 212 ? 4.357  9.634  39.238 1.00 16.56  ? 206  GLU A N     1 
ATOM   1527 C CA    . GLU A 1 212 ? 4.602  8.698  38.136 1.00 16.29  ? 206  GLU A CA    1 
ATOM   1528 C C     . GLU A 1 212 ? 5.722  9.144  37.191 1.00 16.09  ? 206  GLU A C     1 
ATOM   1529 O O     . GLU A 1 212 ? 6.043  8.413  36.260 1.00 16.69  ? 206  GLU A O     1 
ATOM   1530 C CB    . GLU A 1 212 ? 3.347  8.458  37.304 1.00 21.75  ? 206  GLU A CB    1 
ATOM   1531 C CG    . GLU A 1 212 ? 2.792  9.672  36.633 1.00 22.95  ? 206  GLU A CG    1 
ATOM   1532 C CD    . GLU A 1 212 ? 1.626  10.322 37.412 1.00 49.43  ? 206  GLU A CD    1 
ATOM   1533 O OE1   . GLU A 1 212 ? 0.711  10.773 36.681 1.00 39.64  ? 206  GLU A OE1   1 
ATOM   1534 O OE2   . GLU A 1 212 ? 1.601  10.384 38.696 1.00 42.04  ? 206  GLU A OE2   1 
ATOM   1535 N N     . TYR A 1 213 ? 6.274  10.353 37.360 1.00 14.56  ? 207  TYR A N     1 
ATOM   1536 C CA    . TYR A 1 213 ? 7.436  10.783 36.574 1.00 11.69  ? 207  TYR A CA    1 
ATOM   1537 C C     . TYR A 1 213 ? 8.752  10.616 37.296 1.00 14.27  ? 207  TYR A C     1 
ATOM   1538 O O     . TYR A 1 213 ? 9.775  11.099 36.800 1.00 14.27  ? 207  TYR A O     1 
ATOM   1539 C CB    . TYR A 1 213 ? 7.245  12.240 36.187 1.00 12.05  ? 207  TYR A CB    1 
ATOM   1540 C CG    . TYR A 1 213 ? 6.187  12.430 35.173 1.00 12.46  ? 207  TYR A CG    1 
ATOM   1541 C CD1   . TYR A 1 213 ? 4.833  12.529 35.512 1.00 13.49  ? 207  TYR A CD1   1 
ATOM   1542 C CD2   . TYR A 1 213 ? 6.515  12.511 33.808 1.00 12.11  ? 207  TYR A CD2   1 
ATOM   1543 C CE1   . TYR A 1 213 ? 3.855  12.671 34.548 1.00 14.22  ? 207  TYR A CE1   1 
ATOM   1544 C CE2   . TYR A 1 213 ? 5.558  12.659 32.846 1.00 13.28  ? 207  TYR A CE2   1 
ATOM   1545 C CZ    . TYR A 1 213 ? 4.220  12.756 33.198 1.00 13.86  ? 207  TYR A CZ    1 
ATOM   1546 O OH    . TYR A 1 213 ? 3.236  12.903 32.230 1.00 15.52  ? 207  TYR A OH    1 
ATOM   1547 N N     . GLY A 1 214 ? 8.768  9.925  38.454 1.00 15.16  ? 208  GLY A N     1 
ATOM   1548 C CA    . GLY A 1 214 ? 9.994  9.747  39.195 1.00 15.34  ? 208  GLY A CA    1 
ATOM   1549 C C     . GLY A 1 214 ? 10.148 8.332  39.704 1.00 15.79  ? 208  GLY A C     1 
ATOM   1550 O O     . GLY A 1 214 ? 9.209  7.567  39.737 1.00 18.21  ? 208  GLY A O     1 
ATOM   1551 N N     . GLY A 1 215 ? 11.372 8.093  40.131 1.00 20.13  ? 209  GLY A N     1 
ATOM   1552 C CA    . GLY A 1 215 ? 11.895 6.888  40.730 1.00 26.45  ? 209  GLY A CA    1 
ATOM   1553 C C     . GLY A 1 215 ? 12.544 6.015  39.679 1.00 22.16  ? 209  GLY A C     1 
ATOM   1554 O O     . GLY A 1 215 ? 13.742 6.121  39.285 1.00 23.24  ? 209  GLY A O     1 
ATOM   1555 N N     . SER A 1 216 ? 11.694 5.133  39.189 1.00 17.38  ? 210  SER A N     1 
ATOM   1556 C CA    . SER A 1 216 ? 12.216 4.105  38.343 1.00 16.84  ? 210  SER A CA    1 
ATOM   1557 C C     . SER A 1 216 ? 12.739 4.724  37.067 1.00 16.58  ? 210  SER A C     1 
ATOM   1558 O O     . SER A 1 216 ? 12.342 5.842  36.659 1.00 15.41  ? 210  SER A O     1 
ATOM   1559 C CB    . SER A 1 216 ? 11.140 3.100  37.958 1.00 16.79  ? 210  SER A CB    1 
ATOM   1560 O OG    . SER A 1 216 ? 10.136 3.678  37.142 1.00 14.88  ? 210  SER A OG    1 
ATOM   1561 N N     . LEU A 1 217 ? 13.621 4.004  36.412 1.00 15.37  ? 211  LEU A N     1 
ATOM   1562 C CA    . LEU A 1 217 ? 14.092 4.379  35.098 1.00 18.21  ? 211  LEU A CA    1 
ATOM   1563 C C     . LEU A 1 217 ? 12.931 4.595  34.117 1.00 16.19  ? 211  LEU A C     1 
ATOM   1564 O O     . LEU A 1 217 ? 12.885 5.588  33.349 1.00 14.69  ? 211  LEU A O     1 
ATOM   1565 C CB    . LEU A 1 217 ? 15.018 3.250  34.668 1.00 23.23  ? 211  LEU A CB    1 
ATOM   1566 C CG    . LEU A 1 217 ? 15.807 3.537  33.444 1.00 18.62  ? 211  LEU A CG    1 
ATOM   1567 C CD1   . LEU A 1 217 ? 16.430 4.943  33.445 1.00 20.32  ? 211  LEU A CD1   1 
ATOM   1568 C CD2   . LEU A 1 217 ? 16.873 2.437  33.323 1.00 20.90  ? 211  LEU A CD2   1 
ATOM   1569 N N     . ALA A 1 218 ? 11.911 3.742  34.159 1.00 14.01  ? 212  ALA A N     1 
ATOM   1570 C CA    . ALA A 1 218 ? 10.795 3.902  33.252 1.00 13.52  ? 212  ALA A CA    1 
ATOM   1571 C C     . ALA A 1 218 ? 10.062 5.214  33.520 1.00 12.62  ? 212  ALA A C     1 
ATOM   1572 O O     . ALA A 1 218 ? 9.650  5.927  32.579 1.00 14.03  ? 212  ALA A O     1 
ATOM   1573 C CB    . ALA A 1 218 ? 9.816  2.719  33.428 1.00 16.41  ? 212  ALA A CB    1 
ATOM   1574 N N     . ASN A 1 219 ? 9.874  5.532  34.796 1.00 12.98  ? 213  ASN A N     1 
ATOM   1575 C CA    . ASN A 1 219 ? 9.144  6.763  35.130 1.00 12.59  ? 213  ASN A CA    1 
ATOM   1576 C C     . ASN A 1 219 ? 9.968  7.972  34.736 1.00 11.57  ? 213  ASN A C     1 
ATOM   1577 O O     . ASN A 1 219 ? 9.417  8.962  34.234 1.00 12.02  ? 213  ASN A O     1 
ATOM   1578 C CB    . ASN A 1 219 ? 8.861  6.783  36.620 1.00 13.57  ? 213  ASN A CB    1 
ATOM   1579 C CG    . ASN A 1 219 ? 7.698  5.885  37.004 1.00 16.12  ? 213  ASN A CG    1 
ATOM   1580 O OD1   . ASN A 1 219 ? 7.062  5.273  36.134 1.00 18.28  ? 213  ASN A OD1   1 
ATOM   1581 N ND2   . ASN A 1 219 ? 7.386  5.869  38.320 1.00 19.18  ? 213  ASN A ND2   1 
ATOM   1582 N N     . ARG A 1 220 ? 11.289 7.902  34.904 1.00 11.86  ? 214  ARG A N     1 
ATOM   1583 C CA    . ARG A 1 220 ? 12.155 9.022  34.523 1.00 11.47  ? 214  ARG A CA    1 
ATOM   1584 C C     . ARG A 1 220 ? 12.201 9.252  33.023 1.00 11.54  ? 214  ARG A C     1 
ATOM   1585 O O     . ARG A 1 220 ? 12.398 10.397 32.599 1.00 11.41  ? 214  ARG A O     1 
ATOM   1586 C CB    . ARG A 1 220 ? 13.574 8.819  35.072 1.00 11.32  ? 214  ARG A CB    1 
ATOM   1587 C CG    . ARG A 1 220 ? 13.606 8.960  36.583 1.00 12.47  ? 214  ARG A CG    1 
ATOM   1588 C CD    . ARG A 1 220 ? 15.083 8.886  37.104 1.00 16.36  ? 214  ARG A CD    1 
ATOM   1589 N NE    . ARG A 1 220 ? 15.592 7.491  37.098 1.00 20.74  ? 214  ARG A NE    1 
ATOM   1590 C CZ    . ARG A 1 220 ? 16.717 7.010  36.569 1.00 22.03  ? 214  ARG A CZ    1 
ATOM   1591 N NH1   . ARG A 1 220 ? 17.458 7.691  35.676 1.00 24.37  ? 214  ARG A NH1   1 
ATOM   1592 N NH2   . ARG A 1 220 ? 17.107 5.788  36.934 1.00 24.75  ? 214  ARG A NH2   1 
ATOM   1593 N N     . CYS A 1 221 ? 11.925 8.228  32.220 1.00 10.58  ? 215  CYS A N     1 
ATOM   1594 C CA    . CYS A 1 221 ? 11.862 8.369  30.790 1.00 11.05  ? 215  CYS A CA    1 
ATOM   1595 C C     . CYS A 1 221 ? 10.509 8.803  30.273 1.00 10.21  ? 215  CYS A C     1 
ATOM   1596 O O     . CYS A 1 221 ? 10.399 9.054  29.078 1.00 10.72  ? 215  CYS A O     1 
ATOM   1597 C CB    . CYS A 1 221 ? 12.216 7.002  30.113 1.00 12.08  ? 215  CYS A CB    1 
ATOM   1598 S SG    . CYS A 1 221 ? 13.992 6.581  30.272 1.00 14.64  ? 215  CYS A SG    1 
ATOM   1599 N N     . LYS A 1 222 ? 9.503  8.936  31.119 1.00 10.10  ? 216  LYS A N     1 
ATOM   1600 C CA    . LYS A 1 222 ? 8.165  9.291  30.639 1.00 10.64  ? 216  LYS A CA    1 
ATOM   1601 C C     . LYS A 1 222 ? 8.146  10.662 29.973 1.00 10.39  ? 216  LYS A C     1 
ATOM   1602 O O     . LYS A 1 222 ? 7.518  10.813 28.924 1.00 11.37  ? 216  LYS A O     1 
ATOM   1603 C CB    . LYS A 1 222 ? 7.154  9.241  31.791 1.00 11.94  ? 216  LYS A CB    1 
ATOM   1604 C CG    . LYS A 1 222 ? 6.745  7.833  32.107 1.00 18.82  ? 216  LYS A CG    1 
ATOM   1605 C CD    . LYS A 1 222 ? 5.682  7.936  33.192 1.00 24.66  ? 216  LYS A CD    1 
ATOM   1606 C CE    . LYS A 1 222 ? 5.149  6.563  33.494 1.00 28.14  ? 216  LYS A CE    1 
ATOM   1607 N NZ    . LYS A 1 222 ? 4.738  6.412  34.852 1.00 23.62  ? 216  LYS A NZ    1 
ATOM   1608 N N     . PHE A 1 223 ? 8.809  11.657 30.563 1.00 10.36  ? 217  PHE A N     1 
ATOM   1609 C CA    . PHE A 1 223 ? 8.709  13.003 29.990 1.00 9.44   ? 217  PHE A CA    1 
ATOM   1610 C C     . PHE A 1 223 ? 9.291  13.063 28.591 1.00 9.51   ? 217  PHE A C     1 
ATOM   1611 O O     . PHE A 1 223 ? 8.616  13.564 27.674 1.00 10.35  ? 217  PHE A O     1 
ATOM   1612 C CB    . PHE A 1 223 ? 9.370  14.002 30.943 1.00 10.56  ? 217  PHE A CB    1 
ATOM   1613 C CG    . PHE A 1 223 ? 9.195  15.431 30.492 1.00 11.67  ? 217  PHE A CG    1 
ATOM   1614 C CD1   . PHE A 1 223 ? 7.917  15.973 30.208 1.00 16.23  ? 217  PHE A CD1   1 
ATOM   1615 C CD2   . PHE A 1 223 ? 10.290 16.223 30.195 1.00 13.07  ? 217  PHE A CD2   1 
ATOM   1616 C CE1   . PHE A 1 223 ? 7.793  17.328 29.763 1.00 15.52  ? 217  PHE A CE1   1 
ATOM   1617 C CE2   . PHE A 1 223 ? 10.154 17.546 29.788 1.00 12.17  ? 217  PHE A CE2   1 
ATOM   1618 C CZ    . PHE A 1 223 ? 8.946  18.105 29.596 1.00 13.37  ? 217  PHE A CZ    1 
ATOM   1619 N N     . ILE A 1 224 ? 10.514 12.556 28.364 1.00 9.85   ? 218  ILE A N     1 
ATOM   1620 C CA    . ILE A 1 224 ? 11.044 12.610 26.999 1.00 9.57   ? 218  ILE A CA    1 
ATOM   1621 C C     . ILE A 1 224 ? 10.172 11.800 26.049 1.00 10.34  ? 218  ILE A C     1 
ATOM   1622 O O     . ILE A 1 224 ? 9.967  12.186 24.888 1.00 10.09  ? 218  ILE A O     1 
ATOM   1623 C CB    . ILE A 1 224 ? 12.525 12.196 26.925 1.00 9.64   ? 218  ILE A CB    1 
ATOM   1624 C CG1   . ILE A 1 224 ? 13.073 12.664 25.568 1.00 10.87  ? 218  ILE A CG1   1 
ATOM   1625 C CG2   . ILE A 1 224 ? 12.760 10.664 27.154 1.00 12.03  ? 218  ILE A CG2   1 
ATOM   1626 C CD1   . ILE A 1 224 ? 14.621 12.432 25.446 1.00 11.20  ? 218  ILE A CD1   1 
ATOM   1627 N N     . THR A 1 225 ? 9.646  10.665 26.523 1.00 9.90   ? 219  THR A N     1 
ATOM   1628 C CA    . THR A 1 225 ? 8.796  9.871  25.641 1.00 10.45  ? 219  THR A CA    1 
ATOM   1629 C C     . THR A 1 225 ? 7.563  10.665 25.216 1.00 10.23  ? 219  THR A C     1 
ATOM   1630 O O     . THR A 1 225 ? 7.206  10.682 24.031 1.00 10.49  ? 219  THR A O     1 
ATOM   1631 C CB    . THR A 1 225 ? 8.347  8.610  26.374 1.00 13.35  ? 219  THR A CB    1 
ATOM   1632 O OG1   . THR A 1 225 ? 9.494  7.809  26.746 1.00 13.84  ? 219  THR A OG1   1 
ATOM   1633 C CG2   . THR A 1 225 ? 7.458  7.764  25.471 1.00 13.69  ? 219  THR A CG2   1 
ATOM   1634 N N     . GLN A 1 226 ? 6.921  11.350 26.182 1.00 9.79   ? 220  GLN A N     1 
ATOM   1635 C CA    . GLN A 1 226 ? 5.722  12.136 25.844 1.00 11.31  ? 220  GLN A CA    1 
ATOM   1636 C C     . GLN A 1 226 ? 6.031  13.335 24.955 1.00 10.86  ? 220  GLN A C     1 
ATOM   1637 O O     . GLN A 1 226 ? 5.258  13.661 24.039 1.00 10.73  ? 220  GLN A O     1 
ATOM   1638 C CB    . GLN A 1 226 ? 5.000  12.557 27.132 1.00 11.64  ? 220  GLN A CB    1 
ATOM   1639 C CG    . GLN A 1 226 ? 4.373  11.366 27.832 1.00 11.95  ? 220  GLN A CG    1 
ATOM   1640 C CD    . GLN A 1 226 ? 3.981  11.651 29.269 1.00 15.09  ? 220  GLN A CD    1 
ATOM   1641 O OE1   . GLN A 1 226 ? 4.024  12.778 29.719 1.00 16.38  ? 220  GLN A OE1   1 
ATOM   1642 N NE2   . GLN A 1 226 ? 3.721  10.577 30.016 1.00 25.38  ? 220  GLN A NE2   1 
ATOM   1643 N N     . VAL A 1 227 ? 7.177  13.986 25.155 1.00 9.63   ? 221  VAL A N     1 
ATOM   1644 C CA    . VAL A 1 227 ? 7.571  15.084 24.257 1.00 9.98   ? 221  VAL A CA    1 
ATOM   1645 C C     . VAL A 1 227 ? 7.754  14.575 22.830 1.00 9.50   ? 221  VAL A C     1 
ATOM   1646 O O     . VAL A 1 227 ? 7.216  15.149 21.860 1.00 10.99  ? 221  VAL A O     1 
ATOM   1647 C CB    . VAL A 1 227 ? 8.871  15.732 24.781 1.00 9.00   ? 221  VAL A CB    1 
ATOM   1648 C CG1   . VAL A 1 227 ? 9.393  16.740 23.728 1.00 10.41  ? 221  VAL A CG1   1 
ATOM   1649 C CG2   . VAL A 1 227 ? 8.635  16.475 26.106 1.00 9.58   ? 221  VAL A CG2   1 
ATOM   1650 N N     . VAL A 1 228 ? 8.494  13.478 22.680 1.00 8.86   ? 222  VAL A N     1 
ATOM   1651 C CA    . VAL A 1 228 ? 8.746  12.940 21.368 1.00 9.22   ? 222  VAL A CA    1 
ATOM   1652 C C     . VAL A 1 228 ? 7.459  12.464 20.712 1.00 10.14  ? 222  VAL A C     1 
ATOM   1653 O O     . VAL A 1 228 ? 7.212  12.775 19.531 1.00 10.87  ? 222  VAL A O     1 
ATOM   1654 C CB    . VAL A 1 228 ? 9.836  11.847 21.401 1.00 10.96  ? 222  VAL A CB    1 
ATOM   1655 C CG1   . VAL A 1 228 ? 10.001 11.188 19.989 1.00 12.12  ? 222  VAL A CG1   1 
ATOM   1656 C CG2   . VAL A 1 228 ? 11.141 12.428 21.853 1.00 12.38  ? 222  VAL A CG2   1 
ATOM   1657 N N     . GLN A 1 229 ? 6.597  11.782 21.464 1.00 10.50  ? 223  GLN A N     1 
ATOM   1658 C CA    . GLN A 1 229 ? 5.343  11.315 20.889 1.00 11.45  ? 223  GLN A CA    1 
ATOM   1659 C C     . GLN A 1 229 ? 4.514  12.494 20.408 1.00 10.24  ? 223  GLN A C     1 
ATOM   1660 O O     . GLN A 1 229 ? 3.889  12.440 19.325 1.00 11.44  ? 223  GLN A O     1 
ATOM   1661 C CB    . GLN A 1 229 ? 4.523  10.593 21.938 1.00 11.28  ? 223  GLN A CB    1 
ATOM   1662 C CG    . GLN A 1 229 ? 4.871  9.118  22.056 1.00 15.93  ? 223  GLN A CG    1 
ATOM   1663 C CD    . GLN A 1 229 ? 4.496  8.424  23.373 1.00 18.48  ? 223  GLN A CD    1 
ATOM   1664 O OE1   . GLN A 1 229 ? 4.108  9.040  24.419 1.00 17.15  ? 223  GLN A OE1   1 
ATOM   1665 N NE2   . GLN A 1 229 ? 4.434  7.081  23.252 1.00 18.85  ? 223  GLN A NE2   1 
ATOM   1666 N N     . ALA A 1 230 ? 4.468  13.602 21.175 1.00 10.43  ? 224  ALA A N     1 
ATOM   1667 C CA    . ALA A 1 230 ? 3.652  14.747 20.730 1.00 10.37  ? 224  ALA A CA    1 
ATOM   1668 C C     . ALA A 1 230 ? 4.173  15.379 19.463 1.00 11.79  ? 224  ALA A C     1 
ATOM   1669 O O     . ALA A 1 230 ? 3.391  15.674 18.538 1.00 12.66  ? 224  ALA A O     1 
ATOM   1670 C CB    . ALA A 1 230 ? 3.639  15.793 21.833 1.00 12.05  ? 224  ALA A CB    1 
ATOM   1671 N N     . VAL A 1 231 ? 5.486  15.572 19.349 1.00 10.09  ? 225  VAL A N     1 
ATOM   1672 C CA    . VAL A 1 231 ? 6.001  16.201 18.134 1.00 11.21  ? 225  VAL A CA    1 
ATOM   1673 C C     . VAL A 1 231 ? 5.899  15.249 16.952 1.00 10.44  ? 225  VAL A C     1 
ATOM   1674 O O     . VAL A 1 231 ? 5.613  15.704 15.830 1.00 12.04  ? 225  VAL A O     1 
ATOM   1675 C CB    . VAL A 1 231 ? 7.414  16.813 18.300 1.00 10.50  ? 225  VAL A CB    1 
ATOM   1676 C CG1   . VAL A 1 231 ? 7.405  17.937 19.324 1.00 12.45  ? 225  VAL A CG1   1 
ATOM   1677 C CG2   . VAL A 1 231 ? 8.458  15.784 18.660 1.00 13.76  ? 225  VAL A CG2   1 
ATOM   1678 N N     . VAL A 1 232 ? 6.118  13.946 17.160 1.00 10.70  ? 226  VAL A N     1 
ATOM   1679 C CA    . VAL A 1 232 ? 5.922  12.954 16.090 1.00 10.09  ? 226  VAL A CA    1 
ATOM   1680 C C     . VAL A 1 232 ? 4.485  13.002 15.580 1.00 12.21  ? 226  VAL A C     1 
ATOM   1681 O O     . VAL A 1 232 ? 4.244  13.008 14.361 1.00 14.26  ? 226  VAL A O     1 
ATOM   1682 C CB    . VAL A 1 232 ? 6.287  11.554 16.591 1.00 13.69  ? 226  VAL A CB    1 
ATOM   1683 C CG1   . VAL A 1 232 ? 5.650  10.469 15.630 1.00 14.12  ? 226  VAL A CG1   1 
ATOM   1684 C CG2   . VAL A 1 232 ? 7.819  11.402 16.750 1.00 14.36  ? 226  VAL A CG2   1 
ATOM   1685 N N     . SER A 1 233 ? 3.519  13.024 16.482 1.00 13.00  ? 227  SER A N     1 
ATOM   1686 C CA    . SER A 1 233 ? 2.115  13.103 16.047 1.00 14.11  ? 227  SER A CA    1 
ATOM   1687 C C     . SER A 1 233 ? 1.835  14.368 15.261 1.00 15.59  ? 227  SER A C     1 
ATOM   1688 O O     . SER A 1 233 ? 1.035  14.352 14.307 1.00 17.99  ? 227  SER A O     1 
ATOM   1689 C CB    . SER A 1 233 ? 1.182  13.057 17.248 1.00 17.46  ? 227  SER A CB    1 
ATOM   1690 O OG    . SER A 1 233 ? 1.321  11.789 17.851 1.00 33.18  ? 227  SER A OG    1 
ATOM   1691 N N     . ALA A 1 234 ? 2.464  15.479 15.615 1.00 12.56  ? 228  ALA A N     1 
ATOM   1692 C CA    . ALA A 1 234 ? 2.146  16.739 14.969 1.00 13.33  ? 228  ALA A CA    1 
ATOM   1693 C C     . ALA A 1 234 ? 2.808  16.918 13.623 1.00 12.39  ? 228  ALA A C     1 
ATOM   1694 O O     . ALA A 1 234 ? 2.176  17.514 12.726 1.00 14.63  ? 228  ALA A O     1 
ATOM   1695 C CB    . ALA A 1 234 ? 2.576  17.888 15.882 1.00 14.31  ? 228  ALA A CB    1 
ATOM   1696 N N     . ILE A 1 235 ? 4.056  16.464 13.459 1.00 12.33  ? 229  ILE A N     1 
ATOM   1697 C CA    . ILE A 1 235 ? 4.797  16.793 12.235 1.00 11.28  ? 229  ILE A CA    1 
ATOM   1698 C C     . ILE A 1 235 ? 5.349  15.585 11.499 1.00 12.41  ? 229  ILE A C     1 
ATOM   1699 O O     . ILE A 1 235 ? 5.877  15.746 10.391 1.00 13.03  ? 229  ILE A O     1 
ATOM   1700 C CB    . ILE A 1 235 ? 5.896  17.857 12.442 1.00 11.46  ? 229  ILE A CB    1 
ATOM   1701 C CG1   . ILE A 1 235 ? 7.079  17.322 13.259 1.00 13.67  ? 229  ILE A CG1   1 
ATOM   1702 C CG2   . ILE A 1 235 ? 5.291  19.137 13.085 1.00 13.08  ? 229  ILE A CG2   1 
ATOM   1703 C CD1   . ILE A 1 235 ? 8.230  18.298 13.212 1.00 13.98  ? 229  ILE A CD1   1 
ATOM   1704 N N     . GLY A 1 236 ? 5.221  14.391 12.089 1.00 11.45  ? 230  GLY A N     1 
ATOM   1705 C CA    . GLY A 1 236 ? 5.726  13.151 11.494 1.00 11.95  ? 230  GLY A CA    1 
ATOM   1706 C C     . GLY A 1 236 ? 7.111  12.816 12.007 1.00 11.09  ? 230  GLY A C     1 
ATOM   1707 O O     . GLY A 1 236 ? 7.982  13.686 12.165 1.00 12.15  ? 230  GLY A O     1 
ATOM   1708 N N     . ALA A 1 237 ? 7.336  11.546 12.271 1.00 10.97  ? 231  ALA A N     1 
ATOM   1709 C CA    . ALA A 1 237 ? 8.599  11.142 12.894 1.00 12.86  ? 231  ALA A CA    1 
ATOM   1710 C C     . ALA A 1 237 ? 9.800  11.504 12.023 1.00 12.47  ? 231  ALA A C     1 
ATOM   1711 O O     . ALA A 1 237 ? 10.871 11.812 12.558 1.00 11.41  ? 231  ALA A O     1 
ATOM   1712 C CB    . ALA A 1 237 ? 8.611  9.630  13.168 1.00 14.74  ? 231  ALA A CB    1 
ATOM   1713 N N     . ASP A 1 238 ? 9.650  11.470 10.674 1.00 12.12  ? 232  ASP A N     1 
ATOM   1714 C CA    . ASP A 1 238 ? 10.799 11.725 9.829  1.00 11.50  ? 232  ASP A CA    1 
ATOM   1715 C C     . ASP A 1 238 ? 11.289 13.162 9.891  1.00 11.63  ? 232  ASP A C     1 
ATOM   1716 O O     . ASP A 1 238 ? 12.345 13.456 9.316  1.00 12.80  ? 232  ASP A O     1 
ATOM   1717 C CB    . ASP A 1 238 ? 10.480 11.278 8.393  1.00 15.49  ? 232  ASP A CB    1 
ATOM   1718 C CG    . ASP A 1 238 ? 9.332  12.009 7.767  1.00 20.64  ? 232  ASP A CG    1 
ATOM   1719 O OD1   . ASP A 1 238 ? 8.525  12.733 8.357  1.00 25.15  ? 232  ASP A OD1   1 
ATOM   1720 O OD2   . ASP A 1 238 ? 9.135  11.752 6.540  1.00 35.85  ? 232  ASP A OD2   1 
ATOM   1721 N N     . ARG A 1 239 ? 10.557 14.026 10.578 1.00 10.81  ? 233  ARG A N     1 
ATOM   1722 C CA    . ARG A 1 239 ? 10.943 15.425 10.756 1.00 10.67  ? 233  ARG A CA    1 
ATOM   1723 C C     . ARG A 1 239 ? 11.387 15.705 12.173 1.00 9.79   ? 233  ARG A C     1 
ATOM   1724 O O     . ARG A 1 239 ? 11.447 16.881 12.555 1.00 10.67  ? 233  ARG A O     1 
ATOM   1725 C CB    . ARG A 1 239 ? 9.806  16.349 10.339 1.00 10.03  ? 233  ARG A CB    1 
ATOM   1726 C CG    . ARG A 1 239 ? 9.426  16.165 8.821  1.00 12.34  ? 233  ARG A CG    1 
ATOM   1727 C CD    . ARG A 1 239 ? 8.576  17.355 8.325  1.00 14.41  ? 233  ARG A CD    1 
ATOM   1728 N NE    . ARG A 1 239 ? 8.235  17.134 6.915  1.00 20.85  ? 233  ARG A NE    1 
ATOM   1729 C CZ    . ARG A 1 239 ? 8.800  17.764 5.890  1.00 34.60  ? 233  ARG A CZ    1 
ATOM   1730 N NH1   . ARG A 1 239 ? 9.903  18.515 6.034  1.00 19.34  ? 233  ARG A NH1   1 
ATOM   1731 N NH2   . ARG A 1 239 ? 8.300  17.574 4.676  1.00 27.82  ? 233  ARG A NH2   1 
ATOM   1732 N N     . VAL A 1 240 ? 11.661 14.664 12.952 1.00 10.29  ? 234  VAL A N     1 
ATOM   1733 C CA    . VAL A 1 240 ? 11.992 14.793 14.385 1.00 9.80   ? 234  VAL A CA    1 
ATOM   1734 C C     . VAL A 1 240 ? 13.308 14.113 14.665 1.00 10.45  ? 234  VAL A C     1 
ATOM   1735 O O     . VAL A 1 240 ? 13.447 12.891 14.451 1.00 11.38  ? 234  VAL A O     1 
ATOM   1736 C CB    . VAL A 1 240 ? 10.904 14.200 15.262 1.00 9.53   ? 234  VAL A CB    1 
ATOM   1737 C CG1   . VAL A 1 240 ? 11.372 14.288 16.771 1.00 10.74  ? 234  VAL A CG1   1 
ATOM   1738 C CG2   . VAL A 1 240 ? 9.561  14.936 15.075 1.00 10.02  ? 234  VAL A CG2   1 
ATOM   1739 N N     . GLY A 1 241 ? 14.271 14.886 15.181 1.00 8.56   ? 235  GLY A N     1 
ATOM   1740 C CA    . GLY A 1 241 ? 15.496 14.364 15.762 1.00 9.40   ? 235  GLY A CA    1 
ATOM   1741 C C     . GLY A 1 241 ? 15.464 14.514 17.269 1.00 9.48   ? 235  GLY A C     1 
ATOM   1742 O O     . GLY A 1 241 ? 14.729 15.370 17.793 1.00 9.86   ? 235  GLY A O     1 
ATOM   1743 N N     . VAL A 1 242 ? 16.236 13.693 17.959 1.00 8.70   ? 236  VAL A N     1 
ATOM   1744 C CA    . VAL A 1 242 ? 16.276 13.749 19.410 1.00 9.15   ? 236  VAL A CA    1 
ATOM   1745 C C     . VAL A 1 242 ? 17.720 13.778 19.861 1.00 8.51   ? 236  VAL A C     1 
ATOM   1746 O O     . VAL A 1 242 ? 18.515 12.933 19.419 1.00 9.29   ? 236  VAL A O     1 
ATOM   1747 C CB    . VAL A 1 242 ? 15.592 12.491 19.982 1.00 9.52   ? 236  VAL A CB    1 
ATOM   1748 C CG1   . VAL A 1 242 ? 15.614 12.539 21.562 1.00 11.95  ? 236  VAL A CG1   1 
ATOM   1749 C CG2   . VAL A 1 242 ? 14.137 12.401 19.477 1.00 10.93  ? 236  VAL A CG2   1 
ATOM   1750 N N     . ARG A 1 243 ? 18.074 14.713 20.740 1.00 8.40   ? 237  ARG A N     1 
ATOM   1751 C CA    . ARG A 1 243 ? 19.439 14.860 21.251 1.00 9.31   ? 237  ARG A CA    1 
ATOM   1752 C C     . ARG A 1 243 ? 19.499 14.579 22.737 1.00 9.74   ? 237  ARG A C     1 
ATOM   1753 O O     . ARG A 1 243 ? 18.725 15.154 23.519 1.00 9.89   ? 237  ARG A O     1 
ATOM   1754 C CB    . ARG A 1 243 ? 20.004 16.274 20.935 1.00 9.68   ? 237  ARG A CB    1 
ATOM   1755 C CG    . ARG A 1 243 ? 21.529 16.326 21.150 1.00 9.17   ? 237  ARG A CG    1 
ATOM   1756 C CD    . ARG A 1 243 ? 22.066 17.706 20.737 1.00 10.56  ? 237  ARG A CD    1 
ATOM   1757 N NE    . ARG A 1 243 ? 23.459 17.522 20.267 1.00 11.63  ? 237  ARG A NE    1 
ATOM   1758 C CZ    . ARG A 1 243 ? 24.435 18.409 20.352 1.00 11.37  ? 237  ARG A CZ    1 
ATOM   1759 N NH1   . ARG A 1 243 ? 24.346 19.496 21.094 1.00 10.03  ? 237  ARG A NH1   1 
ATOM   1760 N NH2   . ARG A 1 243 ? 25.560 18.211 19.670 1.00 12.31  ? 237  ARG A NH2   1 
ATOM   1761 N N     . VAL A 1 244 ? 20.437 13.705 23.144 1.00 8.03   ? 238  VAL A N     1 
ATOM   1762 C CA    . VAL A 1 244 ? 20.617 13.379 24.568 1.00 9.95   ? 238  VAL A CA    1 
ATOM   1763 C C     . VAL A 1 244 ? 22.093 13.295 24.891 1.00 8.31   ? 238  VAL A C     1 
ATOM   1764 O O     . VAL A 1 244 ? 22.950 13.272 23.998 1.00 10.48  ? 238  VAL A O     1 
ATOM   1765 C CB    . VAL A 1 244 ? 19.913 12.066 24.982 1.00 9.98   ? 238  VAL A CB    1 
ATOM   1766 C CG1   . VAL A 1 244 ? 18.401 12.224 24.892 1.00 10.79  ? 238  VAL A CG1   1 
ATOM   1767 C CG2   . VAL A 1 244 ? 20.465 10.876 24.141 1.00 11.30  ? 238  VAL A CG2   1 
ATOM   1768 N N     . SER A 1 245 ? 22.383 13.312 26.197 1.00 10.00  ? 239  SER A N     1 
ATOM   1769 C CA    . SER A 1 245 ? 23.772 13.296 26.666 1.00 10.39  ? 239  SER A CA    1 
ATOM   1770 C C     . SER A 1 245 ? 23.841 12.552 27.984 1.00 11.29  ? 239  SER A C     1 
ATOM   1771 O O     . SER A 1 245 ? 24.039 13.168 29.037 1.00 12.35  ? 239  SER A O     1 
ATOM   1772 C CB    . SER A 1 245 ? 24.367 14.694 26.779 1.00 10.89  ? 239  SER A CB    1 
ATOM   1773 O OG    . SER A 1 245 ? 23.628 15.517 27.685 1.00 11.57  ? 239  SER A OG    1 
ATOM   1774 N N     . PRO A 1 246 ? 23.623 11.242 27.972 1.00 11.45  ? 240  PRO A N     1 
ATOM   1775 C CA    . PRO A 1 246 ? 23.606 10.493 29.249 1.00 12.85  ? 240  PRO A CA    1 
ATOM   1776 C C     . PRO A 1 246 ? 24.863 10.572 30.045 1.00 13.30  ? 240  PRO A C     1 
ATOM   1777 O O     . PRO A 1 246 ? 24.739 10.448 31.271 1.00 13.85  ? 240  PRO A O     1 
ATOM   1778 C CB    . PRO A 1 246 ? 23.262 9.054  28.842 1.00 14.44  ? 240  PRO A CB    1 
ATOM   1779 C CG    . PRO A 1 246 ? 23.491 8.997  27.368 1.00 15.93  ? 240  PRO A CG    1 
ATOM   1780 C CD    . PRO A 1 246 ? 23.427 10.385 26.785 1.00 11.70  ? 240  PRO A CD    1 
ATOM   1781 N N     . ALA A 1 247 ? 26.030 10.784 29.415 1.00 13.96  ? 241  ALA A N     1 
ATOM   1782 C CA    . ALA A 1 247 ? 27.295 10.825 30.148 1.00 16.67  ? 241  ALA A CA    1 
ATOM   1783 C C     . ALA A 1 247 ? 27.819 12.232 30.406 1.00 18.23  ? 241  ALA A C     1 
ATOM   1784 O O     . ALA A 1 247 ? 28.919 12.388 30.953 1.00 21.21  ? 241  ALA A O     1 
ATOM   1785 C CB    . ALA A 1 247 ? 28.353 10.021 29.357 1.00 19.98  ? 241  ALA A CB    1 
ATOM   1786 N N     . ILE A 1 248 ? 27.097 13.276 30.029 1.00 15.65  ? 242  ILE A N     1 
ATOM   1787 C CA    . ILE A 1 248 ? 27.530 14.644 30.361 1.00 14.54  ? 242  ILE A CA    1 
ATOM   1788 C C     . ILE A 1 248 ? 26.861 15.029 31.667 1.00 16.40  ? 242  ILE A C     1 
ATOM   1789 O O     . ILE A 1 248 ? 25.624 14.906 31.790 1.00 18.45  ? 242  ILE A O     1 
ATOM   1790 C CB    . ILE A 1 248 ? 27.176 15.635 29.245 1.00 13.34  ? 242  ILE A CB    1 
ATOM   1791 C CG1   . ILE A 1 248 ? 27.980 15.311 28.002 1.00 15.95  ? 242  ILE A CG1   1 
ATOM   1792 C CG2   . ILE A 1 248 ? 27.476 17.084 29.709 1.00 18.06  ? 242  ILE A CG2   1 
ATOM   1793 C CD1   . ILE A 1 248 ? 27.820 16.324 26.814 1.00 17.71  ? 242  ILE A CD1   1 
ATOM   1794 N N     . ASP A 1 249 ? 27.657 15.466 32.665 1.00 17.83  ? 243  ASP A N     1 
ATOM   1795 C CA    . ASP A 1 249 ? 27.108 15.771 33.995 1.00 18.98  ? 243  ASP A CA    1 
ATOM   1796 C C     . ASP A 1 249 ? 26.970 17.267 34.339 1.00 24.01  ? 243  ASP A C     1 
ATOM   1797 O O     . ASP A 1 249 ? 26.731 17.599 35.533 1.00 26.10  ? 243  ASP A O     1 
ATOM   1798 C CB    . ASP A 1 249 ? 27.961 15.062 35.066 1.00 26.07  ? 243  ASP A CB    1 
ATOM   1799 N N     . HIS A 1 250 ? 27.099 18.152 33.358 1.00 22.58  ? 244  HIS A N     1 
ATOM   1800 C CA    . HIS A 1 250 ? 26.828 19.622 33.385 1.00 21.68  ? 244  HIS A CA    1 
ATOM   1801 C C     . HIS A 1 250 ? 25.628 20.001 34.236 1.00 18.56  ? 244  HIS A C     1 
ATOM   1802 O O     . HIS A 1 250 ? 24.583 19.369 34.140 1.00 17.03  ? 244  HIS A O     1 
ATOM   1803 C CB    . HIS A 1 250 ? 26.468 19.995 31.913 1.00 22.25  ? 244  HIS A CB    1 
ATOM   1804 C CG    . HIS A 1 250 ? 26.380 21.475 31.608 1.00 22.88  ? 244  HIS A CG    1 
ATOM   1805 N ND1   . HIS A 1 250 ? 25.310 22.046 30.916 1.00 17.87  ? 244  HIS A ND1   1 
ATOM   1806 C CD2   . HIS A 1 250 ? 27.231 22.489 31.918 1.00 21.10  ? 244  HIS A CD2   1 
ATOM   1807 C CE1   . HIS A 1 250 ? 25.523 23.355 30.838 1.00 28.95  ? 244  HIS A CE1   1 
ATOM   1808 N NE2   . HIS A 1 250 ? 26.680 23.638 31.414 1.00 22.66  ? 244  HIS A NE2   1 
ATOM   1809 N N     . LEU A 1 251 ? 25.780 21.061 35.071 1.00 13.77  ? 245  LEU A N     1 
ATOM   1810 C CA    . LEU A 1 251 ? 24.636 21.619 35.818 1.00 13.83  ? 245  LEU A CA    1 
ATOM   1811 C C     . LEU A 1 251 ? 24.060 20.586 36.754 1.00 14.68  ? 245  LEU A C     1 
ATOM   1812 O O     . LEU A 1 251 ? 22.853 20.510 36.972 1.00 13.45  ? 245  LEU A O     1 
ATOM   1813 C CB    . LEU A 1 251 ? 23.534 22.166 34.899 1.00 12.65  ? 245  LEU A CB    1 
ATOM   1814 C CG    . LEU A 1 251 ? 24.056 23.146 33.878 1.00 13.56  ? 245  LEU A CG    1 
ATOM   1815 C CD1   . LEU A 1 251 ? 22.912 23.643 32.996 1.00 13.93  ? 245  LEU A CD1   1 
ATOM   1816 C CD2   . LEU A 1 251 ? 24.795 24.346 34.568 1.00 15.79  ? 245  LEU A CD2   1 
ATOM   1817 N N     . ASP A 1 252 ? 24.942 19.796 37.353 1.00 14.07  ? 246  ASP A N     1 
ATOM   1818 C CA    . ASP A 1 252 ? 24.577 18.835 38.403 1.00 13.54  ? 246  ASP A CA    1 
ATOM   1819 C C     . ASP A 1 252 ? 23.586 17.816 37.877 1.00 15.98  ? 246  ASP A C     1 
ATOM   1820 O O     . ASP A 1 252 ? 22.542 17.597 38.536 1.00 20.98  ? 246  ASP A O     1 
ATOM   1821 C CB    . ASP A 1 252 ? 24.003 19.536 39.664 1.00 16.64  ? 246  ASP A CB    1 
ATOM   1822 C CG    . ASP A 1 252 ? 25.034 20.370 40.402 1.00 15.79  ? 246  ASP A CG    1 
ATOM   1823 O OD1   . ASP A 1 252 ? 26.251 20.142 40.201 1.00 20.10  ? 246  ASP A OD1   1 
ATOM   1824 O OD2   . ASP A 1 252 ? 24.606 21.150 41.291 1.00 20.30  ? 246  ASP A OD2   1 
ATOM   1825 N N     . ALA A 1 253 ? 23.843 17.298 36.675 1.00 14.19  ? 247  ALA A N     1 
ATOM   1826 C CA    . ALA A 1 253 ? 22.973 16.350 35.963 1.00 16.04  ? 247  ALA A CA    1 
ATOM   1827 C C     . ALA A 1 253 ? 23.690 15.038 35.716 1.00 18.45  ? 247  ALA A C     1 
ATOM   1828 O O     . ALA A 1 253 ? 23.924 14.601 34.592 1.00 20.61  ? 247  ALA A O     1 
ATOM   1829 C CB    . ALA A 1 253 ? 22.514 16.989 34.624 1.00 19.76  ? 247  ALA A CB    1 
ATOM   1830 N N     . MET A 1 254 ? 23.927 14.337 36.779 1.00 17.44  ? 248  MET A N     1 
ATOM   1831 C CA    . MET A 1 254 ? 24.556 13.017 36.735 1.00 14.59  ? 248  MET A CA    1 
ATOM   1832 C C     . MET A 1 254 ? 23.493 11.936 36.857 1.00 14.31  ? 248  MET A C     1 
ATOM   1833 O O     . MET A 1 254 ? 22.487 12.077 37.550 1.00 15.00  ? 248  MET A O     1 
ATOM   1834 C CB    . MET A 1 254 ? 25.521 12.889 37.927 1.00 19.89  ? 248  MET A CB    1 
ATOM   1835 C CG    . MET A 1 254 ? 26.252 11.557 38.016 1.00 34.01  ? 248  MET A CG    1 
ATOM   1836 S SD    . MET A 1 254 ? 27.653 11.697 39.167 1.00 63.27  ? 248  MET A SD    1 
ATOM   1837 C CE    . MET A 1 254 ? 28.598 13.038 38.401 1.00 47.81  ? 248  MET A CE    1 
ATOM   1838 N N     . ASP A 1 255 ? 23.753 10.803 36.206 1.00 16.30  ? 249  ASP A N     1 
ATOM   1839 C CA    . ASP A 1 255 ? 23.032 9.573  36.475 1.00 15.66  ? 249  ASP A CA    1 
ATOM   1840 C C     . ASP A 1 255 ? 23.935 8.506  37.056 1.00 13.90  ? 249  ASP A C     1 
ATOM   1841 O O     . ASP A 1 255 ? 25.104 8.404  36.658 1.00 18.67  ? 249  ASP A O     1 
ATOM   1842 C CB    . ASP A 1 255 ? 22.311 9.096  35.216 1.00 17.16  ? 249  ASP A CB    1 
ATOM   1843 C CG    . ASP A 1 255 ? 21.220 8.100  35.555 1.00 16.71  ? 249  ASP A CG    1 
ATOM   1844 O OD1   . ASP A 1 255 ? 20.084 8.494  35.780 1.00 16.16  ? 249  ASP A OD1   1 
ATOM   1845 O OD2   . ASP A 1 255 ? 21.442 6.827  35.508 1.00 18.91  ? 249  ASP A OD2   1 
ATOM   1846 N N     . SER A 1 256 ? 23.361 7.723  37.959 1.00 15.23  ? 250  SER A N     1 
ATOM   1847 C CA    . SER A 1 256 ? 24.091 6.602  38.547 1.00 17.02  ? 250  SER A CA    1 
ATOM   1848 C C     . SER A 1 256 ? 24.478 5.557  37.526 1.00 19.98  ? 250  SER A C     1 
ATOM   1849 O O     . SER A 1 256 ? 25.432 4.813  37.767 1.00 22.02  ? 250  SER A O     1 
ATOM   1850 C CB    . SER A 1 256 ? 23.256 5.956  39.663 1.00 19.09  ? 250  SER A CB    1 
ATOM   1851 O OG    . SER A 1 256 ? 22.041 5.415  39.202 1.00 20.09  ? 250  SER A OG    1 
ATOM   1852 N N     . ASN A 1 257 ? 23.773 5.455  36.393 1.00 18.21  ? 251  ASN A N     1 
ATOM   1853 C CA    . ASN A 1 257 ? 24.088 4.430  35.395 1.00 16.52  ? 251  ASN A CA    1 
ATOM   1854 C C     . ASN A 1 257 ? 23.834 5.045  34.025 1.00 13.75  ? 251  ASN A C     1 
ATOM   1855 O O     . ASN A 1 257 ? 22.801 4.771  33.398 1.00 14.80  ? 251  ASN A O     1 
ATOM   1856 C CB    . ASN A 1 257 ? 23.225 3.189  35.584 1.00 17.25  ? 251  ASN A CB    1 
ATOM   1857 C CG    . ASN A 1 257 ? 23.702 2.005  34.755 1.00 18.64  ? 251  ASN A CG    1 
ATOM   1858 O OD1   . ASN A 1 257 ? 24.431 2.134  33.771 1.00 20.20  ? 251  ASN A OD1   1 
ATOM   1859 N ND2   . ASN A 1 257 ? 23.308 0.800  35.221 1.00 24.38  ? 251  ASN A ND2   1 
ATOM   1860 N N     . PRO A 1 258 ? 24.782 5.810  33.515 1.00 13.65  ? 252  PRO A N     1 
ATOM   1861 C CA    . PRO A 1 258 ? 24.558 6.498  32.238 1.00 13.52  ? 252  PRO A CA    1 
ATOM   1862 C C     . PRO A 1 258 ? 24.247 5.558  31.102 1.00 13.63  ? 252  PRO A C     1 
ATOM   1863 O O     . PRO A 1 258 ? 23.394 5.861  30.254 1.00 12.91  ? 252  PRO A O     1 
ATOM   1864 C CB    . PRO A 1 258 ? 25.867 7.255  31.980 1.00 15.87  ? 252  PRO A CB    1 
ATOM   1865 C CG    . PRO A 1 258 ? 26.412 7.539  33.400 1.00 17.90  ? 252  PRO A CG    1 
ATOM   1866 C CD    . PRO A 1 258 ? 25.988 6.304  34.204 1.00 16.77  ? 252  PRO A CD    1 
ATOM   1867 N N     . LEU A 1 259 ? 24.905 4.391  31.055 1.00 12.64  ? 253  LEU A N     1 
ATOM   1868 C CA    . LEU A 1 259 ? 24.650 3.526  29.925 1.00 12.44  ? 253  LEU A CA    1 
ATOM   1869 C C     . LEU A 1 259 ? 23.232 2.956  29.982 1.00 11.28  ? 253  LEU A C     1 
ATOM   1870 O O     . LEU A 1 259 ? 22.525 2.905  28.957 1.00 11.52  ? 253  LEU A O     1 
ATOM   1871 C CB    . LEU A 1 259 ? 25.670 2.386  29.893 1.00 14.27  ? 253  LEU A CB    1 
ATOM   1872 C CG    . LEU A 1 259 ? 25.449 1.390  28.756 1.00 13.81  ? 253  LEU A CG    1 
ATOM   1873 C CD1   . LEU A 1 259 ? 25.466 1.983  27.369 1.00 17.02  ? 253  LEU A CD1   1 
ATOM   1874 C CD2   . LEU A 1 259 ? 26.523 0.219  28.925 1.00 19.39  ? 253  LEU A CD2   1 
ATOM   1875 N N     . SER A 1 260 ? 22.781 2.505  31.160 1.00 13.31  ? 254  SER A N     1 
ATOM   1876 C CA    . SER A 1 260 ? 21.404 2.013  31.253 1.00 11.20  ? 254  SER A CA    1 
ATOM   1877 C C     . SER A 1 260 ? 20.395 3.116  30.975 1.00 12.82  ? 254  SER A C     1 
ATOM   1878 O O     . SER A 1 260 ? 19.357 2.856  30.384 1.00 12.58  ? 254  SER A O     1 
ATOM   1879 C CB    . SER A 1 260 ? 21.042 1.266  32.561 1.00 13.56  ? 254  SER A CB    1 
ATOM   1880 O OG    . SER A 1 260 ? 21.747 -0.012 32.618 1.00 19.08  ? 254  SER A OG    1 
ATOM   1881 N N     . LEU A 1 261 ? 20.682 4.346  31.399 1.00 11.99  ? 255  LEU A N     1 
ATOM   1882 C CA    . LEU A 1 261 ? 19.766 5.437  31.058 1.00 11.31  ? 255  LEU A CA    1 
ATOM   1883 C C     . LEU A 1 261 ? 19.703 5.647  29.547 1.00 9.14   ? 255  LEU A C     1 
ATOM   1884 O O     . LEU A 1 261 ? 18.611 5.732  28.976 1.00 10.53  ? 255  LEU A O     1 
ATOM   1885 C CB    . LEU A 1 261 ? 20.250 6.707  31.718 1.00 11.64  ? 255  LEU A CB    1 
ATOM   1886 C CG    . LEU A 1 261 ? 19.464 7.970  31.297 1.00 11.05  ? 255  LEU A CG    1 
ATOM   1887 C CD1   . LEU A 1 261 ? 17.981 7.872  31.640 1.00 14.86  ? 255  LEU A CD1   1 
ATOM   1888 C CD2   . LEU A 1 261 ? 20.109 9.182  32.029 1.00 14.67  ? 255  LEU A CD2   1 
ATOM   1889 N N     . GLY A 1 262 ? 20.875 5.705  28.883 1.00 10.37  ? 256  GLY A N     1 
ATOM   1890 C CA    . GLY A 1 262 ? 20.878 5.825  27.432 1.00 10.30  ? 256  GLY A CA    1 
ATOM   1891 C C     . GLY A 1 262 ? 20.135 4.701  26.745 1.00 10.77  ? 256  GLY A C     1 
ATOM   1892 O O     . GLY A 1 262 ? 19.360 4.940  25.804 1.00 11.34  ? 256  GLY A O     1 
ATOM   1893 N N     . LEU A 1 263 ? 20.357 3.448  27.198 1.00 10.23  ? 257  LEU A N     1 
ATOM   1894 C CA    . LEU A 1 263 ? 19.668 2.325  26.526 1.00 9.64   ? 257  LEU A CA    1 
ATOM   1895 C C     . LEU A 1 263 ? 18.178 2.373  26.785 1.00 9.88   ? 257  LEU A C     1 
ATOM   1896 O O     . LEU A 1 263 ? 17.390 1.939  25.924 1.00 11.52  ? 257  LEU A O     1 
ATOM   1897 C CB    . LEU A 1 263 ? 20.261 0.977  27.025 1.00 10.07  ? 257  LEU A CB    1 
ATOM   1898 C CG    . LEU A 1 263 ? 21.682 0.724  26.517 1.00 11.13  ? 257  LEU A CG    1 
ATOM   1899 C CD1   . LEU A 1 263 ? 22.265 -0.555 27.202 1.00 12.53  ? 257  LEU A CD1   1 
ATOM   1900 C CD2   . LEU A 1 263 ? 21.710 0.585  24.986 1.00 12.35  ? 257  LEU A CD2   1 
ATOM   1901 N N     . ALA A 1 264 ? 17.754 2.886  27.950 1.00 10.36  ? 258  ALA A N     1 
ATOM   1902 C CA    . ALA A 1 264 ? 16.322 2.995  28.208 1.00 10.02  ? 258  ALA A CA    1 
ATOM   1903 C C     . ALA A 1 264 ? 15.690 4.041  27.286 1.00 10.74  ? 258  ALA A C     1 
ATOM   1904 O O     . ALA A 1 264 ? 14.582 3.838  26.790 1.00 11.69  ? 258  ALA A O     1 
ATOM   1905 C CB    . ALA A 1 264 ? 16.015 3.313  29.691 1.00 12.30  ? 258  ALA A CB    1 
ATOM   1906 N N     . VAL A 1 265 ? 16.378 5.174  27.079 1.00 10.31  ? 259  VAL A N     1 
ATOM   1907 C CA    . VAL A 1 265 ? 15.859 6.167  26.129 1.00 11.23  ? 259  VAL A CA    1 
ATOM   1908 C C     . VAL A 1 265 ? 15.762 5.564  24.733 1.00 10.53  ? 259  VAL A C     1 
ATOM   1909 O O     . VAL A 1 265 ? 14.753 5.731  24.025 1.00 10.97  ? 259  VAL A O     1 
ATOM   1910 C CB    . VAL A 1 265 ? 16.731 7.425  26.163 1.00 11.01  ? 259  VAL A CB    1 
ATOM   1911 C CG1   . VAL A 1 265 ? 16.294 8.383  25.003 1.00 11.77  ? 259  VAL A CG1   1 
ATOM   1912 C CG2   . VAL A 1 265 ? 16.526 8.147  27.518 1.00 12.89  ? 259  VAL A CG2   1 
ATOM   1913 N N     . VAL A 1 266 ? 16.839 4.877  24.315 1.00 10.42  ? 260  VAL A N     1 
ATOM   1914 C CA    . VAL A 1 266 ? 16.867 4.281  22.973 1.00 10.71  ? 260  VAL A CA    1 
ATOM   1915 C C     . VAL A 1 266 ? 15.712 3.308  22.812 1.00 11.85  ? 260  VAL A C     1 
ATOM   1916 O O     . VAL A 1 266 ? 15.048 3.288  21.779 1.00 11.32  ? 260  VAL A O     1 
ATOM   1917 C CB    . VAL A 1 266 ? 18.238 3.617  22.728 1.00 10.49  ? 260  VAL A CB    1 
ATOM   1918 C CG1   . VAL A 1 266 ? 18.183 2.730  21.453 1.00 12.60  ? 260  VAL A CG1   1 
ATOM   1919 C CG2   . VAL A 1 266 ? 19.307 4.663  22.543 1.00 12.16  ? 260  VAL A CG2   1 
ATOM   1920 N N     . GLU A 1 267 ? 15.467 2.463  23.830 1.00 12.12  ? 261  GLU A N     1 
ATOM   1921 C CA    . GLU A 1 267 ? 14.350 1.532  23.741 1.00 13.07  ? 261  GLU A CA    1 
ATOM   1922 C C     . GLU A 1 267 ? 13.034 2.252  23.510 1.00 12.66  ? 261  GLU A C     1 
ATOM   1923 O O     . GLU A 1 267 ? 12.236 1.792  22.690 1.00 13.88  ? 261  GLU A O     1 
ATOM   1924 C CB    . GLU A 1 267 ? 14.278 0.691  25.023 1.00 17.38  ? 261  GLU A CB    1 
ATOM   1925 C CG    . GLU A 1 267 ? 13.101 -0.325 24.921 1.00 20.39  ? 261  GLU A CG    1 
ATOM   1926 C CD    . GLU A 1 267 ? 12.933 -1.181 26.161 1.00 50.14  ? 261  GLU A CD    1 
ATOM   1927 O OE1   . GLU A 1 267 ? 13.286 -2.389 26.107 1.00 50.61  ? 261  GLU A OE1   1 
ATOM   1928 O OE2   . GLU A 1 267 ? 12.465 -0.644 27.184 1.00 48.97  ? 261  GLU A OE2   1 
ATOM   1929 N N     . ARG A 1 268 ? 12.811 3.380  24.184 1.00 12.35  ? 262  ARG A N     1 
ATOM   1930 C CA    . ARG A 1 268 ? 11.555 4.136  24.043 1.00 12.85  ? 262  ARG A CA    1 
ATOM   1931 C C     . ARG A 1 268 ? 11.465 4.735  22.646 1.00 11.33  ? 262  ARG A C     1 
ATOM   1932 O O     . ARG A 1 268 ? 10.396 4.722  22.022 1.00 13.14  ? 262  ARG A O     1 
ATOM   1933 C CB    . ARG A 1 268 ? 11.500 5.327  25.056 1.00 15.49  ? 262  ARG A CB    1 
ATOM   1934 C CG    . ARG A 1 268 ? 11.666 5.102  26.585 1.00 25.78  ? 262  ARG A CG    1 
ATOM   1935 C CD    . ARG A 1 268 ? 10.690 4.118  27.098 1.00 25.85  ? 262  ARG A CD    1 
ATOM   1936 N NE    . ARG A 1 268 ? 10.754 3.832  28.555 1.00 20.13  ? 262  ARG A NE    1 
ATOM   1937 C CZ    . ARG A 1 268 ? 11.540 2.888  29.125 1.00 23.45  ? 262  ARG A CZ    1 
ATOM   1938 N NH1   . ARG A 1 268 ? 12.634 2.401  28.513 1.00 23.78  ? 262  ARG A NH1   1 
ATOM   1939 N NH2   . ARG A 1 268 ? 11.159 2.319  30.287 1.00 24.94  ? 262  ARG A NH2   1 
ATOM   1940 N N     . LEU A 1 269 ? 12.588 5.210  22.108 1.00 10.17  ? 263  LEU A N     1 
ATOM   1941 C CA    . LEU A 1 269 ? 12.586 5.713  20.726 1.00 10.45  ? 263  LEU A CA    1 
ATOM   1942 C C     . LEU A 1 269 ? 12.256 4.616  19.735 1.00 11.52  ? 263  LEU A C     1 
ATOM   1943 O O     . LEU A 1 269 ? 11.465 4.820  18.794 1.00 10.98  ? 263  LEU A O     1 
ATOM   1944 C CB    . LEU A 1 269 ? 13.915 6.396  20.375 1.00 11.52  ? 263  LEU A CB    1 
ATOM   1945 C CG    . LEU A 1 269 ? 14.277 7.587  21.269 1.00 10.61  ? 263  LEU A CG    1 
ATOM   1946 C CD1   . LEU A 1 269 ? 15.595 8.144  20.749 1.00 13.46  ? 263  LEU A CD1   1 
ATOM   1947 C CD2   . LEU A 1 269 ? 13.183 8.666  21.274 1.00 13.70  ? 263  LEU A CD2   1 
ATOM   1948 N N     . ASN A 1 270 ? 12.871 3.432  19.929 1.00 10.52  ? 264  ASN A N     1 
ATOM   1949 C CA    . ASN A 1 270 ? 12.569 2.314  19.033 1.00 10.72  ? 264  ASN A CA    1 
ATOM   1950 C C     . ASN A 1 270 ? 11.096 1.943  19.110 1.00 11.27  ? 264  ASN A C     1 
ATOM   1951 O O     . ASN A 1 270 ? 10.485 1.662  18.082 1.00 12.58  ? 264  ASN A O     1 
ATOM   1952 C CB    . ASN A 1 270 ? 13.408 1.077  19.382 1.00 10.86  ? 264  ASN A CB    1 
ATOM   1953 C CG    . ASN A 1 270 ? 14.836 1.203  19.004 1.00 11.43  ? 264  ASN A CG    1 
ATOM   1954 O OD1   . ASN A 1 270 ? 15.248 2.073  18.208 1.00 11.67  ? 264  ASN A OD1   1 
ATOM   1955 N ND2   . ASN A 1 270 ? 15.684 0.318  19.574 1.00 13.26  ? 264  ASN A ND2   1 
ATOM   1956 N N     . LYS A 1 271 ? 10.503 1.998  20.310 1.00 11.91  ? 265  LYS A N     1 
ATOM   1957 C CA    . LYS A 1 271 ? 9.085  1.636  20.438 1.00 13.43  ? 265  LYS A CA    1 
ATOM   1958 C C     . LYS A 1 271 ? 8.187  2.697  19.802 1.00 13.96  ? 265  LYS A C     1 
ATOM   1959 O O     . LYS A 1 271 ? 7.154  2.364  19.206 1.00 13.75  ? 265  LYS A O     1 
ATOM   1960 C CB    . LYS A 1 271 ? 8.728  1.450  21.914 1.00 14.80  ? 265  LYS A CB    1 
ATOM   1961 C CG    . LYS A 1 271 ? 9.303  0.161  22.479 1.00 20.23  ? 265  LYS A CG    1 
ATOM   1962 C CD    . LYS A 1 271 ? 8.909  -0.036 23.946 1.00 23.57  ? 265  LYS A CD    1 
ATOM   1963 C CE    . LYS A 1 271 ? 9.355  -1.442 24.424 1.00 33.13  ? 265  LYS A CE    1 
ATOM   1964 N NZ    . LYS A 1 271 ? 9.122  -1.626 25.908 1.00 28.63  ? 265  LYS A NZ    1 
ATOM   1965 N N     . ILE A 1 272 ? 8.532  3.992  19.931 1.00 12.14  ? 266  ILE A N     1 
ATOM   1966 C CA    . ILE A 1 272 ? 7.752  5.037  19.277 1.00 12.12  ? 266  ILE A CA    1 
ATOM   1967 C C     . ILE A 1 272 ? 7.750  4.820  17.775 1.00 12.35  ? 266  ILE A C     1 
ATOM   1968 O O     . ILE A 1 272 ? 6.714  4.929  17.124 1.00 14.14  ? 266  ILE A O     1 
ATOM   1969 C CB    . ILE A 1 272 ? 8.338  6.409  19.622 1.00 13.25  ? 266  ILE A CB    1 
ATOM   1970 C CG1   . ILE A 1 272 ? 8.041  6.731  21.089 1.00 12.01  ? 266  ILE A CG1   1 
ATOM   1971 C CG2   . ILE A 1 272 ? 7.743  7.523  18.716 1.00 15.53  ? 266  ILE A CG2   1 
ATOM   1972 C CD1   . ILE A 1 272 ? 8.791  8.006  21.596 1.00 15.62  ? 266  ILE A CD1   1 
ATOM   1973 N N     . GLN A 1 273 ? 8.910  4.495  17.215 1.00 12.47  ? 267  GLN A N     1 
ATOM   1974 C CA    . GLN A 1 273 ? 8.995  4.248  15.783 1.00 13.08  ? 267  GLN A CA    1 
ATOM   1975 C C     . GLN A 1 273 ? 8.153  3.046  15.365 1.00 14.55  ? 267  GLN A C     1 
ATOM   1976 O O     . GLN A 1 273 ? 7.446  3.100  14.351 1.00 15.59  ? 267  GLN A O     1 
ATOM   1977 C CB    . GLN A 1 273 ? 10.446 3.965  15.366 1.00 12.33  ? 267  GLN A CB    1 
ATOM   1978 C CG    . GLN A 1 273 ? 11.352 5.174  15.577 1.00 11.70  ? 267  GLN A CG    1 
ATOM   1979 C CD    . GLN A 1 273 ? 12.752 5.038  15.179 1.00 13.67  ? 267  GLN A CD    1 
ATOM   1980 O OE1   . GLN A 1 273 ? 13.409 6.071  14.962 1.00 14.08  ? 267  GLN A OE1   1 
ATOM   1981 N NE2   . GLN A 1 273 ? 13.313 3.823  15.145 1.00 12.50  ? 267  GLN A NE2   1 
ATOM   1982 N N     . LEU A 1 274 ? 8.213  1.961  16.140 1.00 14.59  ? 268  LEU A N     1 
ATOM   1983 C CA    . LEU A 1 274 ? 7.445  0.770  15.750 1.00 16.04  ? 268  LEU A CA    1 
ATOM   1984 C C     . LEU A 1 274 ? 5.952  1.061  15.821 1.00 18.01  ? 268  LEU A C     1 
ATOM   1985 O O     . LEU A 1 274 ? 5.186  0.656  14.931 1.00 21.69  ? 268  LEU A O     1 
ATOM   1986 C CB    . LEU A 1 274 ? 7.832  -0.403 16.647 1.00 17.36  ? 268  LEU A CB    1 
ATOM   1987 C CG    . LEU A 1 274 ? 9.161  -0.988 16.194 1.00 25.85  ? 268  LEU A CG    1 
ATOM   1988 C CD1   . LEU A 1 274 ? 9.714  -1.957 17.234 1.00 35.46  ? 268  LEU A CD1   1 
ATOM   1989 C CD2   . LEU A 1 274 ? 9.067  -1.652 14.767 1.00 30.98  ? 268  LEU A CD2   1 
ATOM   1990 N N     . HIS A 1 275 ? 5.521  1.813  16.840 1.00 16.67  ? 269  HIS A N     1 
ATOM   1991 C CA    . HIS A 1 275 ? 4.107  2.132  16.977 1.00 18.57  ? 269  HIS A CA    1 
ATOM   1992 C C     . HIS A 1 275 ? 3.618  3.113  15.905 1.00 22.98  ? 269  HIS A C     1 
ATOM   1993 O O     . HIS A 1 275 ? 2.498  2.960  15.382 1.00 25.58  ? 269  HIS A O     1 
ATOM   1994 C CB    . HIS A 1 275 ? 3.870  2.662  18.369 1.00 19.44  ? 269  HIS A CB    1 
ATOM   1995 C CG    . HIS A 1 275 ? 2.431  2.901  18.655 1.00 22.73  ? 269  HIS A CG    1 
ATOM   1996 N ND1   . HIS A 1 275 ? 1.517  1.863  18.686 1.00 26.60  ? 269  HIS A ND1   1 
ATOM   1997 C CD2   . HIS A 1 275 ? 1.730  4.043  18.854 1.00 26.20  ? 269  HIS A CD2   1 
ATOM   1998 C CE1   . HIS A 1 275 ? 0.317  2.361  18.949 1.00 24.85  ? 269  HIS A CE1   1 
ATOM   1999 N NE2   . HIS A 1 275 ? 0.419  3.677  19.054 1.00 26.90  ? 269  HIS A NE2   1 
ATOM   2000 N N     . SER A 1 276 ? 4.404  4.125  15.567 1.00 19.47  ? 270  SER A N     1 
ATOM   2001 C CA    . SER A 1 276 ? 3.973  5.077  14.549 1.00 19.50  ? 270  SER A CA    1 
ATOM   2002 C C     . SER A 1 276 ? 4.164  4.550  13.132 1.00 21.93  ? 270  SER A C     1 
ATOM   2003 O O     . SER A 1 276 ? 3.648  5.156  12.192 1.00 24.29  ? 270  SER A O     1 
ATOM   2004 C CB    . SER A 1 276 ? 4.721  6.386  14.684 1.00 26.42  ? 270  SER A CB    1 
ATOM   2005 O OG    . SER A 1 276 ? 6.087  6.112  14.544 1.00 25.97  ? 270  SER A OG    1 
ATOM   2006 N N     . GLY A 1 277 ? 4.934  3.492  12.971 1.00 22.11  ? 271  GLY A N     1 
ATOM   2007 C CA    . GLY A 1 277 ? 5.211  2.926  11.660 1.00 24.42  ? 271  GLY A CA    1 
ATOM   2008 C C     . GLY A 1 277 ? 6.184  3.747  10.844 1.00 22.32  ? 271  GLY A C     1 
ATOM   2009 O O     . GLY A 1 277 ? 6.150  3.694  9.614  1.00 24.11  ? 271  GLY A O     1 
ATOM   2010 N N     . SER A 1 278 ? 7.099  4.468  11.499 1.00 19.91  ? 272  SER A N     1 
ATOM   2011 C CA    . SER A 1 278 ? 7.967  5.411  10.813 1.00 19.60  ? 272  SER A CA    1 
ATOM   2012 C C     . SER A 1 278 ? 9.195  5.661  11.665 1.00 19.32  ? 272  SER A C     1 
ATOM   2013 O O     . SER A 1 278 ? 9.122  5.572  12.880 1.00 27.16  ? 272  SER A O     1 
ATOM   2014 C CB    . SER A 1 278 ? 7.238  6.763  10.668 1.00 25.04  ? 272  SER A CB    1 
ATOM   2015 O OG    . SER A 1 278 ? 6.814  7.156  11.976 1.00 32.41  ? 272  SER A OG    1 
ATOM   2016 N N     . LYS A 1 279 ? 10.301 6.024  11.053 1.00 16.96  ? 273  LYS A N     1 
ATOM   2017 C CA    . LYS A 1 279 ? 11.553 6.257  11.761 1.00 16.90  ? 273  LYS A CA    1 
ATOM   2018 C C     . LYS A 1 279 ? 11.739 7.736  12.026 1.00 11.73  ? 273  LYS A C     1 
ATOM   2019 O O     . LYS A 1 279 ? 11.371 8.582  11.207 1.00 14.21  ? 273  LYS A O     1 
ATOM   2020 C CB    . LYS A 1 279 ? 12.780 5.776  10.976 1.00 18.62  ? 273  LYS A CB    1 
ATOM   2021 C CG    . LYS A 1 279 ? 12.676 4.249  10.686 1.00 29.52  ? 273  LYS A CG    1 
ATOM   2022 C CD    . LYS A 1 279 ? 13.139 3.465  11.887 1.00 33.42  ? 273  LYS A CD    1 
ATOM   2023 C CE    . LYS A 1 279 ? 13.916 2.104  11.543 1.00 29.38  ? 273  LYS A CE    1 
ATOM   2024 N NZ    . LYS A 1 279 ? 14.878 2.332  10.409 1.00 43.97  ? 273  LYS A NZ    1 
ATOM   2025 N N     . LEU A 1 280 ? 12.270 8.036  13.216 1.00 11.16  ? 274  LEU A N     1 
ATOM   2026 C CA    . LEU A 1 280 ? 12.722 9.405  13.486 1.00 10.34  ? 274  LEU A CA    1 
ATOM   2027 C C     . LEU A 1 280 ? 13.780 9.802  12.468 1.00 10.61  ? 274  LEU A C     1 
ATOM   2028 O O     . LEU A 1 280 ? 14.416 8.972  11.787 1.00 11.36  ? 274  LEU A O     1 
ATOM   2029 C CB    . LEU A 1 280 ? 13.335 9.462  14.868 1.00 11.86  ? 274  LEU A CB    1 
ATOM   2030 C CG    . LEU A 1 280 ? 12.329 9.188  15.992 1.00 11.54  ? 274  LEU A CG    1 
ATOM   2031 C CD1   . LEU A 1 280 ? 13.037 8.860  17.309 1.00 14.82  ? 274  LEU A CD1   1 
ATOM   2032 C CD2   . LEU A 1 280 ? 11.363 10.350 16.223 1.00 14.52  ? 274  LEU A CD2   1 
ATOM   2033 N N     . ALA A 1 281 ? 13.965 11.131 12.336 1.00 11.23  ? 275  ALA A N     1 
ATOM   2034 C CA    . ALA A 1 281 ? 15.090 11.599 11.523 1.00 10.47  ? 275  ALA A CA    1 
ATOM   2035 C C     . ALA A 1 281 ? 16.401 11.022 12.033 1.00 10.66  ? 275  ALA A C     1 
ATOM   2036 O O     . ALA A 1 281 ? 17.262 10.605 11.240 1.00 11.93  ? 275  ALA A O     1 
ATOM   2037 C CB    . ALA A 1 281 ? 15.134 13.147 11.523 1.00 12.14  ? 275  ALA A CB    1 
ATOM   2038 N N     . TYR A 1 282 ? 16.617 11.082 13.351 1.00 9.73   ? 276  TYR A N     1 
ATOM   2039 C CA    . TYR A 1 282 ? 17.879 10.615 13.924 1.00 9.91   ? 276  TYR A CA    1 
ATOM   2040 C C     . TYR A 1 282 ? 17.837 10.656 15.439 1.00 8.39   ? 276  TYR A C     1 
ATOM   2041 O O     . TYR A 1 282 ? 17.000 11.347 16.044 1.00 9.06   ? 276  TYR A O     1 
ATOM   2042 C CB    . TYR A 1 282 ? 19.093 11.416 13.445 1.00 9.98   ? 276  TYR A CB    1 
ATOM   2043 C CG    . TYR A 1 282 ? 18.951 12.895 13.782 1.00 8.76   ? 276  TYR A CG    1 
ATOM   2044 C CD1   . TYR A 1 282 ? 19.258 13.390 15.054 1.00 9.12   ? 276  TYR A CD1   1 
ATOM   2045 C CD2   . TYR A 1 282 ? 18.446 13.795 12.812 1.00 9.52   ? 276  TYR A CD2   1 
ATOM   2046 C CE1   . TYR A 1 282 ? 19.105 14.758 15.347 1.00 9.72   ? 276  TYR A CE1   1 
ATOM   2047 C CE2   . TYR A 1 282 ? 18.252 15.152 13.114 1.00 9.92   ? 276  TYR A CE2   1 
ATOM   2048 C CZ    . TYR A 1 282 ? 18.615 15.610 14.357 1.00 8.72   ? 276  TYR A CZ    1 
ATOM   2049 O OH    . TYR A 1 282 ? 18.480 16.953 14.667 1.00 10.04  ? 276  TYR A OH    1 
ATOM   2050 N N     . LEU A 1 283 ? 18.813 9.969  16.022 1.00 9.41   ? 277  LEU A N     1 
ATOM   2051 C CA    . LEU A 1 283 ? 19.240 10.115 17.414 1.00 8.98   ? 277  LEU A CA    1 
ATOM   2052 C C     . LEU A 1 283 ? 20.616 10.781 17.378 1.00 8.61   ? 277  LEU A C     1 
ATOM   2053 O O     . LEU A 1 283 ? 21.494 10.394 16.592 1.00 10.67  ? 277  LEU A O     1 
ATOM   2054 C CB    . LEU A 1 283 ? 19.338 8.716  18.096 1.00 8.89   ? 277  LEU A CB    1 
ATOM   2055 C CG    . LEU A 1 283 ? 19.984 8.712  19.483 1.00 9.99   ? 277  LEU A CG    1 
ATOM   2056 C CD1   . LEU A 1 283 ? 19.175 9.538  20.503 1.00 11.81  ? 277  LEU A CD1   1 
ATOM   2057 C CD2   . LEU A 1 283 ? 20.150 7.235  19.939 1.00 12.01  ? 277  LEU A CD2   1 
ATOM   2058 N N     . HIS A 1 284 ? 20.786 11.826 18.188 1.00 9.24   ? 278  HIS A N     1 
ATOM   2059 C CA    . HIS A 1 284 ? 21.997 12.637 18.246 1.00 9.23   ? 278  HIS A CA    1 
ATOM   2060 C C     . HIS A 1 284 ? 22.503 12.541 19.673 1.00 9.93   ? 278  HIS A C     1 
ATOM   2061 O O     . HIS A 1 284 ? 21.799 12.923 20.616 1.00 9.97   ? 278  HIS A O     1 
ATOM   2062 C CB    . HIS A 1 284 ? 21.583 14.080 17.866 1.00 8.81   ? 278  HIS A CB    1 
ATOM   2063 C CG    . HIS A 1 284 ? 22.690 15.070 17.683 1.00 8.64   ? 278  HIS A CG    1 
ATOM   2064 N ND1   . HIS A 1 284 ? 22.422 16.379 17.284 1.00 9.21   ? 278  HIS A ND1   1 
ATOM   2065 C CD2   . HIS A 1 284 ? 24.046 15.007 17.776 1.00 9.74   ? 278  HIS A CD2   1 
ATOM   2066 C CE1   . HIS A 1 284 ? 23.557 17.035 17.097 1.00 9.69   ? 278  HIS A CE1   1 
ATOM   2067 N NE2   . HIS A 1 284 ? 24.569 16.245 17.418 1.00 10.39  ? 278  HIS A NE2   1 
ATOM   2068 N N     . VAL A 1 285 ? 23.721 12.013 19.861 1.00 11.04  ? 279  VAL A N     1 
ATOM   2069 C CA    . VAL A 1 285 ? 24.268 11.849 21.217 1.00 10.90  ? 279  VAL A CA    1 
ATOM   2070 C C     . VAL A 1 285 ? 25.555 12.630 21.315 1.00 10.42  ? 279  VAL A C     1 
ATOM   2071 O O     . VAL A 1 285 ? 26.414 12.537 20.418 1.00 11.64  ? 279  VAL A O     1 
ATOM   2072 C CB    . VAL A 1 285 ? 24.524 10.371 21.597 1.00 10.16  ? 279  VAL A CB    1 
ATOM   2073 C CG1   . VAL A 1 285 ? 25.070 10.279 23.013 1.00 12.67  ? 279  VAL A CG1   1 
ATOM   2074 C CG2   . VAL A 1 285 ? 23.252 9.586  21.461 1.00 10.99  ? 279  VAL A CG2   1 
ATOM   2075 N N     . THR A 1 286 ? 25.681 13.432 22.341 1.00 10.49  ? 280  THR A N     1 
ATOM   2076 C CA    . THR A 1 286 ? 26.882 14.204 22.528 1.00 12.41  ? 280  THR A CA    1 
ATOM   2077 C C     . THR A 1 286 ? 27.563 13.730 23.791 1.00 14.81  ? 280  THR A C     1 
ATOM   2078 O O     . THR A 1 286 ? 26.885 13.360 24.785 1.00 16.39  ? 280  THR A O     1 
ATOM   2079 C CB    . THR A 1 286 ? 26.495 15.724 22.457 1.00 15.40  ? 280  THR A CB    1 
ATOM   2080 O OG1   . THR A 1 286 ? 27.705 16.456 22.392 1.00 19.63  ? 280  THR A OG1   1 
ATOM   2081 C CG2   . THR A 1 286 ? 25.651 16.140 23.621 1.00 17.76  ? 280  THR A CG2   1 
ATOM   2082 N N     . GLN A 1 287 ? 28.866 13.578 23.687 1.00 16.55  ? 281  GLN A N     1 
ATOM   2083 C CA    . GLN A 1 287 ? 29.656 12.997 24.761 1.00 18.25  ? 281  GLN A CA    1 
ATOM   2084 C C     . GLN A 1 287 ? 30.531 14.046 25.427 1.00 20.03  ? 281  GLN A C     1 
ATOM   2085 O O     . GLN A 1 287 ? 30.814 15.105 24.844 1.00 21.88  ? 281  GLN A O     1 
ATOM   2086 C CB    . GLN A 1 287 ? 30.532 11.941 24.110 1.00 16.27  ? 281  GLN A CB    1 
ATOM   2087 C CG    . GLN A 1 287 ? 31.608 12.487 23.215 1.00 16.13  ? 281  GLN A CG    1 
ATOM   2088 C CD    . GLN A 1 287 ? 32.294 11.410 22.457 1.00 26.86  ? 281  GLN A CD    1 
ATOM   2089 O OE1   . GLN A 1 287 ? 32.214 10.228 22.826 1.00 24.30  ? 281  GLN A OE1   1 
ATOM   2090 N NE2   . GLN A 1 287 ? 33.008 11.788 21.424 1.00 24.76  ? 281  GLN A NE2   1 
ATOM   2091 N N     . PRO A 1 288 ? 30.995 13.784 26.660 1.00 22.14  ? 282  PRO A N     1 
ATOM   2092 C CA    . PRO A 1 288 ? 31.893 14.766 27.294 1.00 31.00  ? 282  PRO A CA    1 
ATOM   2093 C C     . PRO A 1 288 ? 33.334 14.613 26.797 1.00 35.31  ? 282  PRO A C     1 
ATOM   2094 O O     . PRO A 1 288 ? 33.613 13.539 26.251 1.00 29.84  ? 282  PRO A O     1 
ATOM   2095 C CB    . PRO A 1 288 ? 31.786 14.418 28.788 1.00 28.04  ? 282  PRO A CB    1 
ATOM   2096 C CG    . PRO A 1 288 ? 31.537 13.015 28.805 1.00 21.05  ? 282  PRO A CG    1 
ATOM   2097 C CD    . PRO A 1 288 ? 30.746 12.614 27.519 1.00 24.29  ? 282  PRO A CD    1 
ATOM   2098 N N     . ARG A 1 309 ? 33.240 3.474  23.849 1.00 35.98  ? 303  ARG A N     1 
ATOM   2099 C CA    . ARG A 1 309 ? 32.365 2.298  23.972 1.00 31.55  ? 303  ARG A CA    1 
ATOM   2100 C C     . ARG A 1 309 ? 30.881 2.605  24.304 1.00 18.36  ? 303  ARG A C     1 
ATOM   2101 O O     . ARG A 1 309 ? 30.007 1.954  23.695 1.00 17.57  ? 303  ARG A O     1 
ATOM   2102 C CB    . ARG A 1 309 ? 32.956 1.245  24.908 1.00 29.92  ? 303  ARG A CB    1 
ATOM   2103 C CG    . ARG A 1 309 ? 32.208 -0.063 24.929 1.00 30.44  ? 303  ARG A CG    1 
ATOM   2104 C CD    . ARG A 1 309 ? 32.975 -1.205 25.623 1.00 25.41  ? 303  ARG A CD    1 
ATOM   2105 N NE    . ARG A 1 309 ? 32.756 -1.181 27.060 1.00 47.08  ? 303  ARG A NE    1 
ATOM   2106 C CZ    . ARG A 1 309 ? 33.629 -1.618 27.960 1.00 53.91  ? 303  ARG A CZ    1 
ATOM   2107 N NH1   . ARG A 1 309 ? 34.785 -2.154 27.598 1.00 61.04  ? 303  ARG A NH1   1 
ATOM   2108 N NH2   . ARG A 1 309 ? 33.329 -1.524 29.253 1.00 51.50  ? 303  ARG A NH2   1 
ATOM   2109 N N     . LEU A 1 310 ? 30.607 3.537  25.216 1.00 17.39  ? 304  LEU A N     1 
ATOM   2110 C CA    . LEU A 1 310 ? 29.229 3.971  25.468 1.00 17.79  ? 304  LEU A CA    1 
ATOM   2111 C C     . LEU A 1 310 ? 28.541 4.472  24.186 1.00 17.25  ? 304  LEU A C     1 
ATOM   2112 O O     . LEU A 1 310 ? 27.415 4.062  23.859 1.00 14.41  ? 304  LEU A O     1 
ATOM   2113 C CB    . LEU A 1 310 ? 29.212 5.012  26.604 1.00 21.46  ? 304  LEU A CB    1 
ATOM   2114 C CG    . LEU A 1 310 ? 28.040 5.066  27.574 1.00 36.80  ? 304  LEU A CG    1 
ATOM   2115 C CD1   . LEU A 1 310 ? 28.223 6.143  28.640 1.00 39.95  ? 304  LEU A CD1   1 
ATOM   2116 C CD2   . LEU A 1 310 ? 26.845 5.409  26.785 1.00 26.45  ? 304  LEU A CD2   1 
ATOM   2117 N N     . MET A 1 311 ? 29.217 5.309  23.414 1.00 15.66  ? 305  MET A N     1 
ATOM   2118 C CA    . MET A 1 311 ? 28.630 5.843  22.193 1.00 15.12  ? 305  MET A CA    1 
ATOM   2119 C C     . MET A 1 311 ? 28.253 4.764  21.205 1.00 15.33  ? 305  MET A C     1 
ATOM   2120 O O     . MET A 1 311 ? 27.128 4.765  20.656 1.00 14.92  ? 305  MET A O     1 
ATOM   2121 C CB    . MET A 1 311 ? 29.570 6.873  21.579 1.00 16.59  ? 305  MET A CB    1 
ATOM   2122 C CG    . MET A 1 311 ? 29.658 8.091  22.457 1.00 26.82  ? 305  MET A CG    1 
ATOM   2123 S SD    . MET A 1 311 ? 28.190 9.162  22.241 1.00 23.71  ? 305  MET A SD    1 
ATOM   2124 C CE    . MET A 1 311 ? 27.953 9.058  20.527 1.00 13.58  ? 305  MET A CE    1 
ATOM   2125 N N     . ARG A 1 312 ? 29.167 3.816  20.964 1.00 14.61  ? 306  ARG A N     1 
ATOM   2126 C CA    . ARG A 1 312 ? 28.889 2.748  20.031 1.00 14.05  ? 306  ARG A CA    1 
ATOM   2127 C C     . ARG A 1 312 ? 27.790 1.819  20.559 1.00 11.26  ? 306  ARG A C     1 
ATOM   2128 O O     . ARG A 1 312 ? 26.970 1.337  19.773 1.00 13.15  ? 306  ARG A O     1 
ATOM   2129 C CB    . ARG A 1 312 ? 30.187 1.987  19.744 1.00 17.38  ? 306  ARG A CB    1 
ATOM   2130 C CG    . ARG A 1 312 ? 30.040 0.967  18.688 1.00 17.31  ? 306  ARG A CG    1 
ATOM   2131 C CD    . ARG A 1 312 ? 29.543 1.559  17.394 1.00 20.17  ? 306  ARG A CD    1 
ATOM   2132 N NE    . ARG A 1 312 ? 29.267 0.530  16.404 1.00 20.64  ? 306  ARG A NE    1 
ATOM   2133 C CZ    . ARG A 1 312 ? 30.101 0.195  15.424 1.00 21.27  ? 306  ARG A CZ    1 
ATOM   2134 N NH1   . ARG A 1 312 ? 31.231 0.843  15.232 1.00 24.57  ? 306  ARG A NH1   1 
ATOM   2135 N NH2   . ARG A 1 312 ? 29.747 -0.762 14.585 1.00 25.66  ? 306  ARG A NH2   1 
ATOM   2136 N N     . THR A 1 313 ? 27.716 1.650  21.876 1.00 12.65  ? 307  THR A N     1 
ATOM   2137 C CA    . THR A 1 313 ? 26.682 0.788  22.420 1.00 13.19  ? 307  THR A CA    1 
ATOM   2138 C C     . THR A 1 313 ? 25.300 1.387  22.191 1.00 12.21  ? 307  THR A C     1 
ATOM   2139 O O     . THR A 1 313 ? 24.355 0.679  21.841 1.00 11.41  ? 307  THR A O     1 
ATOM   2140 C CB    . THR A 1 313 ? 26.936 0.559  23.900 1.00 13.93  ? 307  THR A CB    1 
ATOM   2141 O OG1   . THR A 1 313 ? 28.229 -0.036 24.045 1.00 16.78  ? 307  THR A OG1   1 
ATOM   2142 C CG2   . THR A 1 313 ? 25.910 -0.410 24.473 1.00 14.04  ? 307  THR A CG2   1 
ATOM   2143 N N     . LEU A 1 314 ? 25.160 2.703  22.388 1.00 10.99  ? 308  LEU A N     1 
ATOM   2144 C CA    . LEU A 1 314 ? 23.881 3.355  22.121 1.00 11.18  ? 308  LEU A CA    1 
ATOM   2145 C C     . LEU A 1 314 ? 23.551 3.321  20.635 1.00 9.14   ? 308  LEU A C     1 
ATOM   2146 O O     . LEU A 1 314 ? 22.417 3.047  20.257 1.00 11.64  ? 308  LEU A O     1 
ATOM   2147 C CB    . LEU A 1 314 ? 23.918 4.815  22.624 1.00 11.96  ? 308  LEU A CB    1 
ATOM   2148 C CG    . LEU A 1 314 ? 24.149 4.977  24.154 1.00 12.74  ? 308  LEU A CG    1 
ATOM   2149 C CD1   . LEU A 1 314 ? 24.188 6.503  24.453 1.00 19.33  ? 308  LEU A CD1   1 
ATOM   2150 C CD2   . LEU A 1 314 ? 23.085 4.237  24.872 1.00 15.88  ? 308  LEU A CD2   1 
ATOM   2151 N N     . ARG A 1 315 ? 24.550 3.569  19.764 1.00 10.42  ? 309  ARG A N     1 
ATOM   2152 C CA    . ARG A 1 315 ? 24.310 3.512  18.334 1.00 11.30  ? 309  ARG A CA    1 
ATOM   2153 C C     . ARG A 1 315 ? 23.816 2.131  17.928 1.00 12.49  ? 309  ARG A C     1 
ATOM   2154 O O     . ARG A 1 315 ? 22.835 1.996  17.196 1.00 12.23  ? 309  ARG A O     1 
ATOM   2155 C CB    . ARG A 1 315 ? 25.633 3.848  17.622 1.00 11.86  ? 309  ARG A CB    1 
ATOM   2156 C CG    . ARG A 1 315 ? 25.519 4.013  16.098 1.00 13.48  ? 309  ARG A CG    1 
ATOM   2157 C CD    . ARG A 1 315 ? 25.552 2.658  15.317 1.00 12.47  ? 309  ARG A CD    1 
ATOM   2158 N NE    . ARG A 1 315 ? 26.085 2.914  13.961 1.00 14.62  ? 309  ARG A NE    1 
ATOM   2159 C CZ    . ARG A 1 315 ? 25.469 3.590  13.005 1.00 15.37  ? 309  ARG A CZ    1 
ATOM   2160 N NH1   . ARG A 1 315 ? 24.196 3.968  13.110 1.00 13.22  ? 309  ARG A NH1   1 
ATOM   2161 N NH2   . ARG A 1 315 ? 26.153 3.888  11.887 1.00 16.22  ? 309  ARG A NH2   1 
ATOM   2162 N N     . ASN A 1 316 ? 24.483 1.076  18.447 1.00 11.21  ? 310  ASN A N     1 
ATOM   2163 C CA    . ASN A 1 316 ? 24.102 -0.275 18.038 1.00 11.96  ? 310  ASN A CA    1 
ATOM   2164 C C     . ASN A 1 316 ? 22.712 -0.653 18.553 1.00 10.73  ? 310  ASN A C     1 
ATOM   2165 O O     . ASN A 1 316 ? 22.034 -1.500 17.942 1.00 12.77  ? 310  ASN A O     1 
ATOM   2166 C CB    . ASN A 1 316 ? 25.104 -1.295 18.619 1.00 12.73  ? 310  ASN A CB    1 
ATOM   2167 C CG    . ASN A 1 316 ? 26.442 -1.301 17.936 1.00 14.79  ? 310  ASN A CG    1 
ATOM   2168 O OD1   . ASN A 1 316 ? 26.654 -0.675 16.892 1.00 15.95  ? 310  ASN A OD1   1 
ATOM   2169 N ND2   . ASN A 1 316 ? 27.407 -1.972 18.584 1.00 17.17  ? 310  ASN A ND2   1 
ATOM   2170 N N     . ALA A 1 317 ? 22.257 -0.016 19.637 1.00 10.43  ? 311  ALA A N     1 
ATOM   2171 C CA    . ALA A 1 317 ? 20.936 -0.310 20.158 1.00 10.73  ? 311  ALA A CA    1 
ATOM   2172 C C     . ALA A 1 317 ? 19.806 0.411  19.442 1.00 10.20  ? 311  ALA A C     1 
ATOM   2173 O O     . ALA A 1 317 ? 18.648 0.007  19.560 1.00 11.02  ? 311  ALA A O     1 
ATOM   2174 C CB    . ALA A 1 317 ? 20.900 0.134  21.637 1.00 10.49  ? 311  ALA A CB    1 
ATOM   2175 N N     . TYR A 1 318 ? 20.109 1.474  18.674 1.00 9.66   ? 312  TYR A N     1 
ATOM   2176 C CA    . TYR A 1 318 ? 19.090 2.341  18.108 1.00 11.27  ? 312  TYR A CA    1 
ATOM   2177 C C     . TYR A 1 318 ? 18.784 1.962  16.658 1.00 10.22  ? 312  TYR A C     1 
ATOM   2178 O O     . TYR A 1 318 ? 19.704 1.855  15.832 1.00 10.98  ? 312  TYR A O     1 
ATOM   2179 C CB    . TYR A 1 318 ? 19.569 3.810  18.175 1.00 11.72  ? 312  TYR A CB    1 
ATOM   2180 C CG    . TYR A 1 318 ? 18.579 4.704  17.446 1.00 10.70  ? 312  TYR A CG    1 
ATOM   2181 C CD1   . TYR A 1 318 ? 17.225 4.713  17.801 1.00 10.85  ? 312  TYR A CD1   1 
ATOM   2182 C CD2   . TYR A 1 318 ? 18.987 5.505  16.404 1.00 8.71   ? 312  TYR A CD2   1 
ATOM   2183 C CE1   . TYR A 1 318 ? 16.310 5.486  17.050 1.00 12.23  ? 312  TYR A CE1   1 
ATOM   2184 C CE2   . TYR A 1 318 ? 18.082 6.286  15.650 1.00 10.20  ? 312  TYR A CE2   1 
ATOM   2185 C CZ    . TYR A 1 318 ? 16.797 6.259  15.960 1.00 10.12  ? 312  TYR A CZ    1 
ATOM   2186 O OH    . TYR A 1 318 ? 15.883 6.979  15.204 1.00 11.96  ? 312  TYR A OH    1 
ATOM   2187 N N     . GLN A 1 319 ? 17.484 1.751  16.377 1.00 10.31  ? 313  GLN A N     1 
ATOM   2188 C CA    . GLN A 1 319 ? 17.057 1.419  15.001 1.00 11.74  ? 313  GLN A CA    1 
ATOM   2189 C C     . GLN A 1 319 ? 16.928 2.699  14.176 1.00 12.37  ? 313  GLN A C     1 
ATOM   2190 O O     . GLN A 1 319 ? 15.833 3.212  13.951 1.00 15.22  ? 313  GLN A O     1 
ATOM   2191 C CB    . GLN A 1 319 ? 15.717 0.714  15.050 1.00 12.93  ? 313  GLN A CB    1 
ATOM   2192 C CG    . GLN A 1 319 ? 15.747 -0.657 15.699 1.00 13.82  ? 313  GLN A CG    1 
ATOM   2193 C CD    . GLN A 1 319 ? 14.415 -1.307 15.798 1.00 15.34  ? 313  GLN A CD    1 
ATOM   2194 O OE1   . GLN A 1 319 ? 13.525 -1.053 14.972 1.00 17.76  ? 313  GLN A OE1   1 
ATOM   2195 N NE2   . GLN A 1 319 ? 14.242 -2.198 16.788 1.00 17.39  ? 313  GLN A NE2   1 
ATOM   2196 N N     . GLY A 1 320 ? 18.050 3.217  13.718 1.00 10.53  ? 314  GLY A N     1 
ATOM   2197 C CA    . GLY A 1 320 ? 17.975 4.360  12.826 1.00 11.26  ? 314  GLY A CA    1 
ATOM   2198 C C     . GLY A 1 320 ? 19.294 5.112  12.729 1.00 10.45  ? 314  GLY A C     1 
ATOM   2199 O O     . GLY A 1 320 ? 20.358 4.608  13.056 1.00 11.82  ? 314  GLY A O     1 
ATOM   2200 N N     . THR A 1 321 ? 19.167 6.351  12.241 1.00 11.02  ? 315  THR A N     1 
ATOM   2201 C CA    . THR A 1 321 ? 20.328 7.208  11.956 1.00 12.02  ? 315  THR A CA    1 
ATOM   2202 C C     . THR A 1 321 ? 20.938 7.782  13.230 1.00 10.20  ? 315  THR A C     1 
ATOM   2203 O O     . THR A 1 321 ? 20.200 8.239  14.122 1.00 10.85  ? 315  THR A O     1 
ATOM   2204 C CB    . THR A 1 321 ? 19.840 8.377  11.086 1.00 11.18  ? 315  THR A CB    1 
ATOM   2205 O OG1   . THR A 1 321 ? 19.418 7.845  9.833  1.00 13.75  ? 315  THR A OG1   1 
ATOM   2206 C CG2   . THR A 1 321 ? 20.942 9.401  10.862 1.00 12.23  ? 315  THR A CG2   1 
ATOM   2207 N N     . PHE A 1 322 ? 22.259 7.730  13.338 1.00 10.73  ? 316  PHE A N     1 
ATOM   2208 C CA    . PHE A 1 322 ? 22.956 8.194  14.528 1.00 9.39   ? 316  PHE A CA    1 
ATOM   2209 C C     . PHE A 1 322 ? 23.922 9.319  14.195 1.00 10.61  ? 316  PHE A C     1 
ATOM   2210 O O     . PHE A 1 322 ? 24.788 9.184  13.304 1.00 11.62  ? 316  PHE A O     1 
ATOM   2211 C CB    . PHE A 1 322 ? 23.706 6.992  15.154 1.00 10.89  ? 316  PHE A CB    1 
ATOM   2212 C CG    . PHE A 1 322 ? 24.248 7.245  16.523 1.00 11.03  ? 316  PHE A CG    1 
ATOM   2213 C CD1   . PHE A 1 322 ? 23.426 6.988  17.645 1.00 11.01  ? 316  PHE A CD1   1 
ATOM   2214 C CD2   . PHE A 1 322 ? 25.541 7.676  16.726 1.00 12.14  ? 316  PHE A CD2   1 
ATOM   2215 C CE1   . PHE A 1 322 ? 23.955 7.160  18.959 1.00 11.97  ? 316  PHE A CE1   1 
ATOM   2216 C CE2   . PHE A 1 322 ? 26.077 7.840  17.993 1.00 11.81  ? 316  PHE A CE2   1 
ATOM   2217 C CZ    . PHE A 1 322 ? 25.248 7.578  19.134 1.00 11.36  ? 316  PHE A CZ    1 
ATOM   2218 N N     . ILE A 1 323 ? 23.801 10.419 14.935 1.00 9.61   ? 317  ILE A N     1 
ATOM   2219 C CA    . ILE A 1 323 ? 24.702 11.557 14.820 1.00 10.21  ? 317  ILE A CA    1 
ATOM   2220 C C     . ILE A 1 323 ? 25.546 11.596 16.076 1.00 9.67   ? 317  ILE A C     1 
ATOM   2221 O O     . ILE A 1 323 ? 25.021 11.667 17.183 1.00 10.37  ? 317  ILE A O     1 
ATOM   2222 C CB    . ILE A 1 323 ? 23.942 12.895 14.684 1.00 9.63   ? 317  ILE A CB    1 
ATOM   2223 C CG1   . ILE A 1 323 ? 22.829 12.808 13.647 1.00 9.91   ? 317  ILE A CG1   1 
ATOM   2224 C CG2   . ILE A 1 323 ? 24.988 13.979 14.382 1.00 10.19  ? 317  ILE A CG2   1 
ATOM   2225 C CD1   . ILE A 1 323 ? 22.205 14.171 13.280 1.00 11.48  ? 317  ILE A CD1   1 
ATOM   2226 N N     . CYS A 1 324 ? 26.864 11.519 15.927 1.00 11.21  ? 318  CYS A N     1 
ATOM   2227 C CA    . CYS A 1 324 ? 27.767 11.666 17.068 1.00 11.51  ? 318  CYS A CA    1 
ATOM   2228 C C     . CYS A 1 324 ? 28.302 13.068 17.158 1.00 11.44  ? 318  CYS A C     1 
ATOM   2229 O O     . CYS A 1 324 ? 28.433 13.775 16.151 1.00 12.51  ? 318  CYS A O     1 
ATOM   2230 C CB    . CYS A 1 324 ? 28.914 10.661 16.976 1.00 12.80  ? 318  CYS A CB    1 
ATOM   2231 S SG    . CYS A 1 324 ? 29.986 10.863 15.497 1.00 16.73  ? 318  CYS A SG    1 
ATOM   2232 N N     . SER A 1 325 ? 28.646 13.483 18.368 1.00 12.04  ? 319  SER A N     1 
ATOM   2233 C CA    . SER A 1 325 ? 29.045 14.840 18.622 1.00 12.11  ? 319  SER A CA    1 
ATOM   2234 C C     . SER A 1 325 ? 29.936 14.911 19.870 1.00 11.27  ? 319  SER A C     1 
ATOM   2235 O O     . SER A 1 325 ? 29.743 14.112 20.817 1.00 12.42  ? 319  SER A O     1 
ATOM   2236 C CB    . SER A 1 325 ? 27.732 15.582 18.872 1.00 15.15  ? 319  SER A CB    1 
ATOM   2237 O OG    . SER A 1 325 ? 27.949 16.687 19.649 1.00 21.05  ? 319  SER A OG    1 
ATOM   2238 N N     . GLY A 1 326 ? 30.906 15.852 19.841 1.00 12.97  ? 320  GLY A N     1 
ATOM   2239 C CA    . GLY A 1 326 ? 31.726 16.236 20.997 1.00 13.37  ? 320  GLY A CA    1 
ATOM   2240 C C     . GLY A 1 326 ? 33.189 15.911 20.706 1.00 14.08  ? 320  GLY A C     1 
ATOM   2241 O O     . GLY A 1 326 ? 33.584 14.726 20.741 1.00 17.06  ? 320  GLY A O     1 
ATOM   2242 N N     . GLY A 1 327 ? 33.952 16.937 20.430 1.00 14.82  ? 321  GLY A N     1 
ATOM   2243 C CA    . GLY A 1 327 ? 35.402 16.812 20.260 1.00 15.55  ? 321  GLY A CA    1 
ATOM   2244 C C     . GLY A 1 327 ? 35.821 16.278 18.916 1.00 22.98  ? 321  GLY A C     1 
ATOM   2245 O O     . GLY A 1 327 ? 37.004 15.954 18.754 1.00 23.55  ? 321  GLY A O     1 
ATOM   2246 N N     . TYR A 1 328 ? 34.905 16.113 17.946 1.00 19.42  ? 322  TYR A N     1 
ATOM   2247 C CA    . TYR A 1 328 ? 35.331 15.600 16.647 1.00 18.88  ? 322  TYR A CA    1 
ATOM   2248 C C     . TYR A 1 328 ? 36.185 16.623 15.899 1.00 17.67  ? 322  TYR A C     1 
ATOM   2249 O O     . TYR A 1 328 ? 36.127 17.841 16.093 1.00 19.52  ? 322  TYR A O     1 
ATOM   2250 C CB    . TYR A 1 328 ? 34.121 15.108 15.825 1.00 18.93  ? 322  TYR A CB    1 
ATOM   2251 C CG    . TYR A 1 328 ? 33.587 13.841 16.410 1.00 17.63  ? 322  TYR A CG    1 
ATOM   2252 C CD1   . TYR A 1 328 ? 32.600 13.887 17.427 1.00 16.96  ? 322  TYR A CD1   1 
ATOM   2253 C CD2   . TYR A 1 328 ? 34.091 12.571 16.059 1.00 19.11  ? 322  TYR A CD2   1 
ATOM   2254 C CE1   . TYR A 1 328 ? 32.168 12.761 18.015 1.00 16.57  ? 322  TYR A CE1   1 
ATOM   2255 C CE2   . TYR A 1 328 ? 33.620 11.426 16.639 1.00 21.42  ? 322  TYR A CE2   1 
ATOM   2256 C CZ    . TYR A 1 328 ? 32.666 11.516 17.665 1.00 21.25  ? 322  TYR A CZ    1 
ATOM   2257 O OH    . TYR A 1 328 ? 32.184 10.389 18.297 1.00 21.59  ? 322  TYR A OH    1 
ATOM   2258 N N     . THR A 1 329 ? 37.103 16.060 15.128 1.00 23.08  ? 323  THR A N     1 
ATOM   2259 C CA    . THR A 1 329 ? 37.971 16.778 14.224 1.00 21.74  ? 323  THR A CA    1 
ATOM   2260 C C     . THR A 1 329 ? 37.795 16.076 12.889 1.00 17.17  ? 323  THR A C     1 
ATOM   2261 O O     . THR A 1 329 ? 37.014 15.125 12.737 1.00 19.11  ? 323  THR A O     1 
ATOM   2262 C CB    . THR A 1 329 ? 39.423 16.632 14.693 1.00 25.04  ? 323  THR A CB    1 
ATOM   2263 O OG1   . THR A 1 329 ? 39.694 15.244 14.701 1.00 22.59  ? 323  THR A OG1   1 
ATOM   2264 C CG2   . THR A 1 329 ? 39.623 17.172 16.117 1.00 25.17  ? 323  THR A CG2   1 
ATOM   2265 N N     . ARG A 1 330 ? 38.521 16.562 11.860 1.00 18.92  ? 324  ARG A N     1 
ATOM   2266 C CA    . ARG A 1 330 ? 38.416 15.924 10.556 1.00 18.56  ? 324  ARG A CA    1 
ATOM   2267 C C     . ARG A 1 330 ? 38.723 14.439 10.648 1.00 17.33  ? 324  ARG A C     1 
ATOM   2268 O O     . ARG A 1 330 ? 37.952 13.593 10.214 1.00 18.55  ? 324  ARG A O     1 
ATOM   2269 C CB    . ARG A 1 330 ? 39.379 16.603 9.570  1.00 18.67  ? 324  ARG A CB    1 
ATOM   2270 C CG    . ARG A 1 330 ? 39.339 15.934 8.198  1.00 18.66  ? 324  ARG A CG    1 
ATOM   2271 C CD    . ARG A 1 330 ? 40.252 16.685 7.232  1.00 19.99  ? 324  ARG A CD    1 
ATOM   2272 N NE    . ARG A 1 330 ? 40.111 16.167 5.882  1.00 20.33  ? 324  ARG A NE    1 
ATOM   2273 C CZ    . ARG A 1 330 ? 40.771 15.118 5.426  1.00 19.79  ? 324  ARG A CZ    1 
ATOM   2274 N NH1   . ARG A 1 330 ? 41.609 14.454 6.205  1.00 23.68  ? 324  ARG A NH1   1 
ATOM   2275 N NH2   . ARG A 1 330 ? 40.540 14.702 4.173  1.00 28.73  ? 324  ARG A NH2   1 
ATOM   2276 N N     . GLU A 1 331 ? 39.865 14.110 11.261 1.00 19.26  ? 325  GLU A N     1 
ATOM   2277 C CA    . GLU A 1 331 ? 40.281 12.722 11.286 1.00 20.22  ? 325  GLU A CA    1 
ATOM   2278 C C     . GLU A 1 331 ? 39.380 11.874 12.163 1.00 19.49  ? 325  GLU A C     1 
ATOM   2279 O O     . GLU A 1 331 ? 39.049 10.755 11.791 1.00 19.10  ? 325  GLU A O     1 
ATOM   2280 C CB    . GLU A 1 331 ? 41.730 12.619 11.771 1.00 28.72  ? 325  GLU A CB    1 
ATOM   2281 C CG    . GLU A 1 331 ? 42.770 13.219 10.776 1.00 33.24  ? 325  GLU A CG    1 
ATOM   2282 C CD    . GLU A 1 331 ? 42.563 14.726 10.511 1.00 45.51  ? 325  GLU A CD    1 
ATOM   2283 O OE1   . GLU A 1 331 ? 42.810 15.139 9.326  1.00 35.07  ? 325  GLU A OE1   1 
ATOM   2284 O OE2   . GLU A 1 331 ? 42.158 15.471 11.487 1.00 31.73  ? 325  GLU A OE2   1 
ATOM   2285 N N     . LEU A 1 332 ? 38.917 12.440 13.298 1.00 18.84  ? 326  LEU A N     1 
ATOM   2286 C CA    . LEU A 1 332 ? 38.046 11.639 14.152 1.00 21.22  ? 326  LEU A CA    1 
ATOM   2287 C C     . LEU A 1 332 ? 36.677 11.437 13.511 1.00 19.76  ? 326  LEU A C     1 
ATOM   2288 O O     . LEU A 1 332 ? 36.076 10.392 13.647 1.00 17.83  ? 326  LEU A O     1 
ATOM   2289 C CB    . LEU A 1 332 ? 37.902 12.285 15.538 1.00 21.57  ? 326  LEU A CB    1 
ATOM   2290 C CG    . LEU A 1 332 ? 39.183 12.289 16.413 1.00 27.22  ? 326  LEU A CG    1 
ATOM   2291 C CD1   . LEU A 1 332 ? 39.019 13.189 17.655 1.00 26.09  ? 326  LEU A CD1   1 
ATOM   2292 C CD2   . LEU A 1 332 ? 39.521 10.852 16.768 1.00 29.04  ? 326  LEU A CD2   1 
ATOM   2293 N N     . GLY A 1 333 ? 36.201 12.413 12.735 1.00 17.83  ? 327  GLY A N     1 
ATOM   2294 C CA    . GLY A 1 333 ? 34.912 12.201 12.080 1.00 19.96  ? 327  GLY A CA    1 
ATOM   2295 C C     . GLY A 1 333 ? 34.995 11.212 10.940 1.00 15.89  ? 327  GLY A C     1 
ATOM   2296 O O     . GLY A 1 333 ? 34.118 10.386 10.718 1.00 17.52  ? 327  GLY A O     1 
ATOM   2297 N N     . ILE A 1 334 ? 36.102 11.286 10.171 1.00 17.76  ? 328  ILE A N     1 
ATOM   2298 C CA    . ILE A 1 334 ? 36.336 10.282 9.154  1.00 20.50  ? 328  ILE A CA    1 
ATOM   2299 C C     . ILE A 1 334 ? 36.338 8.880  9.760  1.00 19.81  ? 328  ILE A C     1 
ATOM   2300 O O     . ILE A 1 334 ? 35.684 7.979  9.242  1.00 17.96  ? 328  ILE A O     1 
ATOM   2301 C CB    . ILE A 1 334 ? 37.656 10.570 8.429  1.00 18.81  ? 328  ILE A CB    1 
ATOM   2302 C CG1   . ILE A 1 334 ? 37.471 11.724 7.449  1.00 17.15  ? 328  ILE A CG1   1 
ATOM   2303 C CG2   . ILE A 1 334 ? 38.148 9.322  7.683  1.00 19.91  ? 328  ILE A CG2   1 
ATOM   2304 C CD1   . ILE A 1 334 ? 38.835 12.202 6.825  1.00 18.66  ? 328  ILE A CD1   1 
ATOM   2305 N N     . GLU A 1 335 ? 37.064 8.710  10.875 1.00 21.01  ? 329  GLU A N     1 
ATOM   2306 C CA    . GLU A 1 335 ? 37.111 7.394  11.540 1.00 24.66  ? 329  GLU A CA    1 
ATOM   2307 C C     . GLU A 1 335 ? 35.725 6.964  12.017 1.00 22.20  ? 329  GLU A C     1 
ATOM   2308 O O     . GLU A 1 335 ? 35.339 5.812  11.846 1.00 23.07  ? 329  GLU A O     1 
ATOM   2309 C CB    . GLU A 1 335 ? 38.096 7.409  12.711 1.00 22.97  ? 329  GLU A CB    1 
ATOM   2310 N N     . ALA A 1 336 ? 34.953 7.900  12.601 1.00 19.29  ? 330  ALA A N     1 
ATOM   2311 C CA    . ALA A 1 336 ? 33.612 7.540  13.084 1.00 21.89  ? 330  ALA A CA    1 
ATOM   2312 C C     . ALA A 1 336 ? 32.753 6.967  11.974 1.00 19.12  ? 330  ALA A C     1 
ATOM   2313 O O     . ALA A 1 336 ? 32.066 5.967  12.155 1.00 20.05  ? 330  ALA A O     1 
ATOM   2314 C CB    . ALA A 1 336 ? 32.925 8.747  13.711 1.00 20.18  ? 330  ALA A CB    1 
ATOM   2315 N N     . VAL A 1 337 ? 32.774 7.578  10.789 1.00 18.16  ? 331  VAL A N     1 
ATOM   2316 C CA    . VAL A 1 337 ? 31.952 7.039  9.755  1.00 16.49  ? 331  VAL A CA    1 
ATOM   2317 C C     . VAL A 1 337 ? 32.566 5.784  9.162  1.00 23.21  ? 331  VAL A C     1 
ATOM   2318 O O     . VAL A 1 337 ? 31.848 4.842  8.876  1.00 20.98  ? 331  VAL A O     1 
ATOM   2319 C CB    . VAL A 1 337 ? 31.696 8.104  8.666  1.00 19.23  ? 331  VAL A CB    1 
ATOM   2320 C CG1   . VAL A 1 337 ? 31.020 7.541  7.476  1.00 17.73  ? 331  VAL A CG1   1 
ATOM   2321 C CG2   . VAL A 1 337 ? 30.926 9.299  9.258  1.00 17.64  ? 331  VAL A CG2   1 
ATOM   2322 N N     . ALA A 1 338 ? 33.900 5.771  8.982  1.00 19.32  ? 332  ALA A N     1 
ATOM   2323 C CA    . ALA A 1 338 ? 34.540 4.603  8.374  1.00 23.78  ? 332  ALA A CA    1 
ATOM   2324 C C     . ALA A 1 338 ? 34.343 3.350  9.227  1.00 25.08  ? 332  ALA A C     1 
ATOM   2325 O O     . ALA A 1 338 ? 34.112 2.269  8.675  1.00 28.17  ? 332  ALA A O     1 
ATOM   2326 C CB    . ALA A 1 338 ? 36.030 4.900  8.153  1.00 22.35  ? 332  ALA A CB    1 
ATOM   2327 N N     . GLN A 1 339 ? 34.403 3.478  10.556 1.00 21.04  ? 333  GLN A N     1 
ATOM   2328 C CA    . GLN A 1 339 ? 34.287 2.317  11.451 1.00 22.19  ? 333  GLN A CA    1 
ATOM   2329 C C     . GLN A 1 339 ? 32.868 1.985  11.862 1.00 28.35  ? 333  GLN A C     1 
ATOM   2330 O O     . GLN A 1 339 ? 32.693 1.090  12.713 1.00 27.62  ? 333  GLN A O     1 
ATOM   2331 C CB    . GLN A 1 339 ? 35.158 2.440  12.683 1.00 28.82  ? 333  GLN A CB    1 
ATOM   2332 C CG    . GLN A 1 339 ? 36.588 2.842  12.421 1.00 29.66  ? 333  GLN A CG    1 
ATOM   2333 C CD    . GLN A 1 339 ? 37.197 3.414  13.659 1.00 45.84  ? 333  GLN A CD    1 
ATOM   2334 O OE1   . GLN A 1 339 ? 36.590 3.352  14.736 1.00 51.54  ? 333  GLN A OE1   1 
ATOM   2335 N NE2   . GLN A 1 339 ? 38.412 3.948  13.544 1.00 59.50  ? 333  GLN A NE2   1 
ATOM   2336 N N     . GLY A 1 340 ? 31.861 2.662  11.283 1.00 24.46  ? 334  GLY A N     1 
ATOM   2337 C CA    . GLY A 1 340 ? 30.464 2.372  11.546 1.00 21.99  ? 334  GLY A CA    1 
ATOM   2338 C C     . GLY A 1 340 ? 29.947 2.942  12.853 1.00 17.81  ? 334  GLY A C     1 
ATOM   2339 O O     . GLY A 1 340 ? 28.846 2.555  13.286 1.00 23.10  ? 334  GLY A O     1 
ATOM   2340 N N     . ASP A 1 341 ? 30.692 3.820  13.499 1.00 18.57  ? 335  ASP A N     1 
ATOM   2341 C CA    . ASP A 1 341 ? 30.317 4.351  14.792 1.00 18.62  ? 335  ASP A CA    1 
ATOM   2342 C C     . ASP A 1 341 ? 29.189 5.381  14.674 1.00 20.89  ? 335  ASP A C     1 
ATOM   2343 O O     . ASP A 1 341 ? 28.515 5.643  15.678 1.00 20.00  ? 335  ASP A O     1 
ATOM   2344 C CB    . ASP A 1 341 ? 31.507 5.000  15.503 1.00 24.01  ? 335  ASP A CB    1 
ATOM   2345 C CG    . ASP A 1 341 ? 32.644 4.005  15.775 1.00 40.43  ? 335  ASP A CG    1 
ATOM   2346 O OD1   . ASP A 1 341 ? 32.377 2.781  15.779 1.00 35.36  ? 335  ASP A OD1   1 
ATOM   2347 O OD2   . ASP A 1 341 ? 33.800 4.456  15.955 1.00 35.54  ? 335  ASP A OD2   1 
ATOM   2348 N N     . ALA A 1 342 ? 28.998 6.002  13.493 1.00 15.70  ? 336  ALA A N     1 
ATOM   2349 C CA    . ALA A 1 342 ? 27.972 7.044  13.345 1.00 14.62  ? 336  ALA A CA    1 
ATOM   2350 C C     . ALA A 1 342 ? 27.651 7.162  11.868 1.00 13.35  ? 336  ALA A C     1 
ATOM   2351 O O     . ALA A 1 342 ? 28.482 6.822  11.005 1.00 15.79  ? 336  ALA A O     1 
ATOM   2352 C CB    . ALA A 1 342 ? 28.452 8.392  13.840 1.00 17.03  ? 336  ALA A CB    1 
ATOM   2353 N N     . ASP A 1 343 ? 26.453 7.667  11.576 1.00 12.38  ? 337  ASP A N     1 
ATOM   2354 C CA    . ASP A 1 343 ? 26.103 7.957  10.189 1.00 11.30  ? 337  ASP A CA    1 
ATOM   2355 C C     . ASP A 1 343 ? 26.422 9.387  9.828  1.00 11.32  ? 337  ASP A C     1 
ATOM   2356 O O     . ASP A 1 343 ? 26.816 9.654  8.681  1.00 11.87  ? 337  ASP A O     1 
ATOM   2357 C CB    . ASP A 1 343 ? 24.625 7.707  9.989  1.00 12.79  ? 337  ASP A CB    1 
ATOM   2358 C CG    . ASP A 1 343 ? 24.282 6.298  10.371 1.00 13.56  ? 337  ASP A CG    1 
ATOM   2359 O OD1   . ASP A 1 343 ? 24.791 5.356  9.714  1.00 14.46  ? 337  ASP A OD1   1 
ATOM   2360 O OD2   . ASP A 1 343 ? 23.461 6.092  11.322 1.00 12.66  ? 337  ASP A OD2   1 
ATOM   2361 N N     . LEU A 1 344 ? 26.338 10.310 10.784 1.00 11.40  ? 338  LEU A N     1 
ATOM   2362 C CA    . LEU A 1 344 ? 26.603 11.734 10.585 1.00 10.34  ? 338  LEU A CA    1 
ATOM   2363 C C     . LEU A 1 344 ? 27.422 12.214 11.764 1.00 10.09  ? 338  LEU A C     1 
ATOM   2364 O O     . LEU A 1 344 ? 27.337 11.637 12.865 1.00 10.51  ? 338  LEU A O     1 
ATOM   2365 C CB    . LEU A 1 344 ? 25.281 12.540 10.516 1.00 11.57  ? 338  LEU A CB    1 
ATOM   2366 C CG    . LEU A 1 344 ? 24.275 12.074 9.461  1.00 11.59  ? 338  LEU A CG    1 
ATOM   2367 C CD1   . LEU A 1 344 ? 22.912 12.778 9.652  1.00 12.82  ? 338  LEU A CD1   1 
ATOM   2368 C CD2   . LEU A 1 344 ? 24.837 12.409 8.058  1.00 12.71  ? 338  LEU A CD2   1 
ATOM   2369 N N     . VAL A 1 345 ? 28.213 13.261 11.556 1.00 10.40  ? 339  VAL A N     1 
ATOM   2370 C CA    . VAL A 1 345 ? 29.103 13.771 12.579 1.00 10.94  ? 339  VAL A CA    1 
ATOM   2371 C C     . VAL A 1 345 ? 28.805 15.257 12.702 1.00 10.96  ? 339  VAL A C     1 
ATOM   2372 O O     . VAL A 1 345 ? 28.935 15.995 11.715 1.00 10.22  ? 339  VAL A O     1 
ATOM   2373 C CB    . VAL A 1 345 ? 30.597 13.559 12.228 1.00 12.29  ? 339  VAL A CB    1 
ATOM   2374 C CG1   . VAL A 1 345 ? 31.453 14.113 13.356 1.00 13.66  ? 339  VAL A CG1   1 
ATOM   2375 C CG2   . VAL A 1 345 ? 30.903 12.073 11.980 1.00 12.97  ? 339  VAL A CG2   1 
ATOM   2376 N N     . SER A 1 346 ? 28.462 15.730 13.894 1.00 9.40   ? 340  SER A N     1 
ATOM   2377 C CA    . SER A 1 346 ? 28.205 17.144 14.081 1.00 9.46   ? 340  SER A CA    1 
ATOM   2378 C C     . SER A 1 346 ? 29.386 17.844 14.714 1.00 10.44  ? 340  SER A C     1 
ATOM   2379 O O     . SER A 1 346 ? 30.038 17.288 15.598 1.00 11.73  ? 340  SER A O     1 
ATOM   2380 C CB    . SER A 1 346 ? 26.900 17.400 14.822 1.00 11.54  ? 340  SER A CB    1 
ATOM   2381 O OG    . SER A 1 346 ? 27.025 17.048 16.213 1.00 12.16  ? 340  SER A OG    1 
ATOM   2382 N N     . TYR A 1 347 ? 29.642 19.054 14.260 1.00 9.42   ? 341  TYR A N     1 
ATOM   2383 C CA    . TYR A 1 347 ? 30.734 19.919 14.692 1.00 8.47   ? 341  TYR A CA    1 
ATOM   2384 C C     . TYR A 1 347 ? 30.149 21.208 15.210 1.00 9.62   ? 341  TYR A C     1 
ATOM   2385 O O     . TYR A 1 347 ? 29.337 21.849 14.535 1.00 10.96  ? 341  TYR A O     1 
ATOM   2386 C CB    . TYR A 1 347 ? 31.688 20.219 13.510 1.00 12.27  ? 341  TYR A CB    1 
ATOM   2387 C CG    . TYR A 1 347 ? 32.405 19.010 13.004 1.00 11.20  ? 341  TYR A CG    1 
ATOM   2388 C CD1   . TYR A 1 347 ? 31.799 18.165 12.074 1.00 11.48  ? 341  TYR A CD1   1 
ATOM   2389 C CD2   . TYR A 1 347 ? 33.712 18.719 13.450 1.00 12.51  ? 341  TYR A CD2   1 
ATOM   2390 C CE1   . TYR A 1 347 ? 32.471 17.044 11.582 1.00 13.65  ? 341  TYR A CE1   1 
ATOM   2391 C CE2   . TYR A 1 347 ? 34.355 17.569 13.003 1.00 14.54  ? 341  TYR A CE2   1 
ATOM   2392 C CZ    . TYR A 1 347 ? 33.772 16.770 12.075 1.00 12.98  ? 341  TYR A CZ    1 
ATOM   2393 O OH    . TYR A 1 347 ? 34.424 15.641 11.589 1.00 15.80  ? 341  TYR A OH    1 
ATOM   2394 N N     . GLY A 1 348 ? 30.604 21.605 16.406 1.00 9.36   ? 342  GLY A N     1 
ATOM   2395 C CA    . GLY A 1 348 ? 30.177 22.840 17.009 1.00 10.04  ? 342  GLY A CA    1 
ATOM   2396 C C     . GLY A 1 348 ? 31.239 23.904 16.885 1.00 10.58  ? 342  GLY A C     1 
ATOM   2397 O O     . GLY A 1 348 ? 31.219 24.750 15.987 1.00 11.58  ? 342  GLY A O     1 
ATOM   2398 N N     . ARG A 1 349 ? 32.193 23.879 17.819 1.00 11.60  ? 343  ARG A N     1 
ATOM   2399 C CA    . ARG A 1 349 ? 33.141 24.989 17.893 1.00 11.12  ? 343  ARG A CA    1 
ATOM   2400 C C     . ARG A 1 349 ? 33.891 25.249 16.595 1.00 11.92  ? 343  ARG A C     1 
ATOM   2401 O O     . ARG A 1 349 ? 34.114 26.404 16.241 1.00 11.34  ? 343  ARG A O     1 
ATOM   2402 C CB    . ARG A 1 349 ? 34.121 24.807 19.055 1.00 12.73  ? 343  ARG A CB    1 
ATOM   2403 C CG    . ARG A 1 349 ? 33.418 24.988 20.446 1.00 12.60  ? 343  ARG A CG    1 
ATOM   2404 C CD    . ARG A 1 349 ? 34.292 24.426 21.566 1.00 15.60  ? 343  ARG A CD    1 
ATOM   2405 N NE    . ARG A 1 349 ? 34.336 22.985 21.494 1.00 14.59  ? 343  ARG A NE    1 
ATOM   2406 C CZ    . ARG A 1 349 ? 35.250 22.248 22.113 1.00 20.00  ? 343  ARG A CZ    1 
ATOM   2407 N NH1   . ARG A 1 349 ? 36.108 22.810 22.956 1.00 25.86  ? 343  ARG A NH1   1 
ATOM   2408 N NH2   . ARG A 1 349 ? 35.351 20.952 21.832 1.00 22.40  ? 343  ARG A NH2   1 
ATOM   2409 N N     . LEU A 1 350 ? 34.324 24.181 15.872 1.00 9.96   ? 344  LEU A N     1 
ATOM   2410 C CA    . LEU A 1 350 ? 35.017 24.434 14.607 1.00 10.61  ? 344  LEU A CA    1 
ATOM   2411 C C     . LEU A 1 350 ? 34.127 25.133 13.599 1.00 10.69  ? 344  LEU A C     1 
ATOM   2412 O O     . LEU A 1 350 ? 34.618 25.853 12.707 1.00 10.07  ? 344  LEU A O     1 
ATOM   2413 C CB    . LEU A 1 350 ? 35.558 23.145 14.009 1.00 9.32   ? 344  LEU A CB    1 
ATOM   2414 C CG    . LEU A 1 350 ? 36.797 22.659 14.764 1.00 10.79  ? 344  LEU A CG    1 
ATOM   2415 C CD1   . LEU A 1 350 ? 37.143 21.249 14.302 1.00 14.47  ? 344  LEU A CD1   1 
ATOM   2416 C CD2   . LEU A 1 350 ? 38.006 23.609 14.564 1.00 13.18  ? 344  LEU A CD2   1 
ATOM   2417 N N     . PHE A 1 351 ? 32.783 24.909 13.667 1.00 10.40  ? 345  PHE A N     1 
ATOM   2418 C CA    . PHE A 1 351 ? 31.930 25.649 12.742 1.00 9.59   ? 345  PHE A CA    1 
ATOM   2419 C C     . PHE A 1 351 ? 31.743 27.112 13.129 1.00 10.40  ? 345  PHE A C     1 
ATOM   2420 O O     . PHE A 1 351 ? 31.365 27.905 12.283 1.00 11.43  ? 345  PHE A O     1 
ATOM   2421 C CB    . PHE A 1 351 ? 30.569 24.919 12.700 1.00 11.02  ? 345  PHE A CB    1 
ATOM   2422 C CG    . PHE A 1 351 ? 30.169 24.356 11.348 1.00 10.35  ? 345  PHE A CG    1 
ATOM   2423 C CD1   . PHE A 1 351 ? 30.245 25.155 10.207 1.00 10.58  ? 345  PHE A CD1   1 
ATOM   2424 C CD2   . PHE A 1 351 ? 29.667 23.040 11.252 1.00 11.77  ? 345  PHE A CD2   1 
ATOM   2425 C CE1   . PHE A 1 351 ? 29.812 24.671 8.966  1.00 12.43  ? 345  PHE A CE1   1 
ATOM   2426 C CE2   . PHE A 1 351 ? 29.239 22.562 9.975  1.00 11.04  ? 345  PHE A CE2   1 
ATOM   2427 C CZ    . PHE A 1 351 ? 29.296 23.386 8.872  1.00 11.71  ? 345  PHE A CZ    1 
ATOM   2428 N N     . ILE A 1 352 ? 31.964 27.478 14.390 1.00 10.49  ? 346  ILE A N     1 
ATOM   2429 C CA    . ILE A 1 352 ? 31.935 28.890 14.762 1.00 10.31  ? 346  ILE A CA    1 
ATOM   2430 C C     . ILE A 1 352 ? 32.962 29.656 13.943 1.00 11.31  ? 346  ILE A C     1 
ATOM   2431 O O     . ILE A 1 352 ? 32.659 30.703 13.349 1.00 10.65  ? 346  ILE A O     1 
ATOM   2432 C CB    . ILE A 1 352 ? 32.185 29.028 16.282 1.00 10.53  ? 346  ILE A CB    1 
ATOM   2433 C CG1   . ILE A 1 352 ? 30.954 28.504 17.011 1.00 11.83  ? 346  ILE A CG1   1 
ATOM   2434 C CG2   . ILE A 1 352 ? 32.531 30.506 16.597 1.00 12.15  ? 346  ILE A CG2   1 
ATOM   2435 C CD1   . ILE A 1 352 ? 31.105 28.616 18.571 1.00 15.39  ? 346  ILE A CD1   1 
ATOM   2436 N N     . SER A 1 353 ? 34.204 29.129 13.866 1.00 10.52  ? 347  SER A N     1 
ATOM   2437 C CA    . SER A 1 353 ? 35.268 29.905 13.265 1.00 10.46  ? 347  SER A CA    1 
ATOM   2438 C C     . SER A 1 353 ? 35.614 29.498 11.850 1.00 11.20  ? 347  SER A C     1 
ATOM   2439 O O     . SER A 1 353 ? 36.483 30.127 11.256 1.00 12.31  ? 347  SER A O     1 
ATOM   2440 C CB    . SER A 1 353 ? 36.531 29.811 14.140 1.00 11.17  ? 347  SER A CB    1 
ATOM   2441 O OG    . SER A 1 353 ? 36.840 28.426 14.401 1.00 11.59  ? 347  SER A OG    1 
ATOM   2442 N N     . ASN A 1 354 ? 34.958 28.481 11.286 1.00 10.56  ? 348  ASN A N     1 
ATOM   2443 C CA    . ASN A 1 354 ? 35.224 28.037 9.914  1.00 9.94   ? 348  ASN A CA    1 
ATOM   2444 C C     . ASN A 1 354 ? 33.877 28.007 9.227  1.00 10.65  ? 348  ASN A C     1 
ATOM   2445 O O     . ASN A 1 354 ? 33.211 26.969 9.243  1.00 10.90  ? 348  ASN A O     1 
ATOM   2446 C CB    . ASN A 1 354 ? 35.917 26.676 9.906  1.00 11.12  ? 348  ASN A CB    1 
ATOM   2447 C CG    . ASN A 1 354 ? 37.262 26.732 10.567 1.00 10.33  ? 348  ASN A CG    1 
ATOM   2448 O OD1   . ASN A 1 354 ? 38.242 27.099 9.875  1.00 11.47  ? 348  ASN A OD1   1 
ATOM   2449 N ND2   . ASN A 1 354 ? 37.336 26.476 11.847 1.00 11.09  ? 348  ASN A ND2   1 
ATOM   2450 N N     . PRO A 1 355 ? 33.436 29.131 8.651  1.00 10.02  ? 349  PRO A N     1 
ATOM   2451 C CA    . PRO A 1 355 ? 32.091 29.096 8.031  1.00 12.18  ? 349  PRO A CA    1 
ATOM   2452 C C     . PRO A 1 355 ? 32.053 28.025 6.948  1.00 12.57  ? 349  PRO A C     1 
ATOM   2453 O O     . PRO A 1 355 ? 31.006 27.379 6.737  1.00 11.87  ? 349  PRO A O     1 
ATOM   2454 C CB    . PRO A 1 355 ? 31.902 30.522 7.455  1.00 11.63  ? 349  PRO A CB    1 
ATOM   2455 C CG    . PRO A 1 355 ? 33.371 31.081 7.330  1.00 13.74  ? 349  PRO A CG    1 
ATOM   2456 C CD    . PRO A 1 355 ? 34.077 30.466 8.567  1.00 10.81  ? 349  PRO A CD    1 
ATOM   2457 N N     . ASP A 1 356 ? 33.151 27.889 6.197  1.00 11.56  ? 350  ASP A N     1 
ATOM   2458 C CA    . ASP A 1 356 ? 33.307 26.879 5.155  1.00 10.74  ? 350  ASP A CA    1 
ATOM   2459 C C     . ASP A 1 356 ? 33.921 25.594 5.699  1.00 10.47  ? 350  ASP A C     1 
ATOM   2460 O O     . ASP A 1 356 ? 34.767 24.944 5.055  1.00 11.82  ? 350  ASP A O     1 
ATOM   2461 C CB    . ASP A 1 356 ? 34.118 27.467 3.984  1.00 12.46  ? 350  ASP A CB    1 
ATOM   2462 C CG    . ASP A 1 356 ? 35.412 28.113 4.394  1.00 14.96  ? 350  ASP A CG    1 
ATOM   2463 O OD1   . ASP A 1 356 ? 35.741 28.274 5.577  1.00 15.03  ? 350  ASP A OD1   1 
ATOM   2464 O OD2   . ASP A 1 356 ? 36.120 28.476 3.423  1.00 17.10  ? 350  ASP A OD2   1 
ATOM   2465 N N     . LEU A 1 357 ? 33.532 25.146 6.897  1.00 9.94   ? 351  LEU A N     1 
ATOM   2466 C CA    . LEU A 1 357 ? 34.142 23.950 7.486  1.00 9.98   ? 351  LEU A CA    1 
ATOM   2467 C C     . LEU A 1 357 ? 33.986 22.746 6.567  1.00 10.09  ? 351  LEU A C     1 
ATOM   2468 O O     . LEU A 1 357 ? 34.881 21.908 6.461  1.00 11.08  ? 351  LEU A O     1 
ATOM   2469 C CB    . LEU A 1 357 ? 33.494 23.645 8.837  1.00 11.01  ? 351  LEU A CB    1 
ATOM   2470 C CG    . LEU A 1 357 ? 34.045 22.407 9.545  1.00 10.32  ? 351  LEU A CG    1 
ATOM   2471 C CD1   . LEU A 1 357 ? 35.528 22.597 9.901  1.00 14.30  ? 351  LEU A CD1   1 
ATOM   2472 C CD2   . LEU A 1 357 ? 33.223 22.128 10.802 1.00 11.18  ? 351  LEU A CD2   1 
ATOM   2473 N N     . VAL A 1 358 ? 32.823 22.612 5.920  1.00 11.02  ? 352  VAL A N     1 
ATOM   2474 C CA    . VAL A 1 358 ? 32.615 21.465 5.027  1.00 11.00  ? 352  VAL A CA    1 
ATOM   2475 C C     . VAL A 1 358 ? 33.697 21.427 3.944  1.00 12.92  ? 352  VAL A C     1 
ATOM   2476 O O     . VAL A 1 358 ? 34.359 20.391 3.733  1.00 12.77  ? 352  VAL A O     1 
ATOM   2477 C CB    . VAL A 1 358 ? 31.204 21.496 4.419  1.00 11.40  ? 352  VAL A CB    1 
ATOM   2478 C CG1   . VAL A 1 358 ? 30.999 20.272 3.496  1.00 14.25  ? 352  VAL A CG1   1 
ATOM   2479 C CG2   . VAL A 1 358 ? 30.115 21.444 5.508  1.00 12.25  ? 352  VAL A CG2   1 
ATOM   2480 N N     . MET A 1 359 ? 33.897 22.552 3.256  1.00 12.25  ? 353  MET A N     1 
ATOM   2481 C CA    . MET A 1 359 ? 34.902 22.594 2.195  1.00 13.22  ? 353  MET A CA    1 
ATOM   2482 C C     . MET A 1 359 ? 36.292 22.414 2.762  1.00 14.50  ? 353  MET A C     1 
ATOM   2483 O O     . MET A 1 359 ? 37.137 21.767 2.148  1.00 14.86  ? 353  MET A O     1 
ATOM   2484 C CB    . MET A 1 359 ? 34.820 23.949 1.486  1.00 16.15  ? 353  MET A CB    1 
ATOM   2485 C CG    . MET A 1 359 ? 35.833 24.136 0.328  1.00 20.95  ? 353  MET A CG    1 
ATOM   2486 S SD    . MET A 1 359 ? 35.517 22.946 -1.061 1.00 34.41  ? 353  MET A SD    1 
ATOM   2487 C CE    . MET A 1 359 ? 33.764 22.422 -0.863 1.00 27.90  ? 353  MET A CE    1 
ATOM   2488 N N     . ARG A 1 360 ? 36.569 22.962 3.950  1.00 13.16  ? 354  ARG A N     1 
ATOM   2489 C CA    . ARG A 1 360 ? 37.905 22.763 4.480  1.00 13.30  ? 354  ARG A CA    1 
ATOM   2490 C C     . ARG A 1 360 ? 38.159 21.314 4.819  1.00 15.83  ? 354  ARG A C     1 
ATOM   2491 O O     . ARG A 1 360 ? 39.266 20.798 4.591  1.00 15.79  ? 354  ARG A O     1 
ATOM   2492 C CB    . ARG A 1 360 ? 38.084 23.629 5.716  1.00 12.78  ? 354  ARG A CB    1 
ATOM   2493 C CG    . ARG A 1 360 ? 38.154 25.109 5.411  1.00 12.56  ? 354  ARG A CG    1 
ATOM   2494 C CD    . ARG A 1 360 ? 38.407 25.906 6.693  1.00 15.35  ? 354  ARG A CD    1 
ATOM   2495 N NE    . ARG A 1 360 ? 38.214 27.331 6.483  1.00 13.61  ? 354  ARG A NE    1 
ATOM   2496 C CZ    . ARG A 1 360 ? 39.078 28.278 6.812  1.00 14.52  ? 354  ARG A CZ    1 
ATOM   2497 N NH1   . ARG A 1 360 ? 40.300 27.993 7.255  1.00 15.44  ? 354  ARG A NH1   1 
ATOM   2498 N NH2   . ARG A 1 360 ? 38.719 29.546 6.665  1.00 18.87  ? 354  ARG A NH2   1 
ATOM   2499 N N     . ILE A 1 361 ? 37.166 20.613 5.350  1.00 13.06  ? 355  ILE A N     1 
ATOM   2500 C CA    . ILE A 1 361 ? 37.292 19.184 5.603  1.00 14.66  ? 355  ILE A CA    1 
ATOM   2501 C C     . ILE A 1 361 ? 37.478 18.426 4.288  1.00 14.85  ? 355  ILE A C     1 
ATOM   2502 O O     . ILE A 1 361 ? 38.338 17.538 4.189  1.00 16.31  ? 355  ILE A O     1 
ATOM   2503 C CB    . ILE A 1 361 ? 36.073 18.685 6.411  1.00 14.38  ? 355  ILE A CB    1 
ATOM   2504 C CG1   . ILE A 1 361 ? 36.186 19.213 7.835  1.00 15.32  ? 355  ILE A CG1   1 
ATOM   2505 C CG2   . ILE A 1 361 ? 35.985 17.143 6.390  1.00 16.23  ? 355  ILE A CG2   1 
ATOM   2506 C CD1   . ILE A 1 361 ? 35.052 18.764 8.728  1.00 14.89  ? 355  ILE A CD1   1 
ATOM   2507 N N     . LYS A 1 362 ? 36.725 18.819 3.249  1.00 13.25  ? 356  LYS A N     1 
ATOM   2508 C CA    . LYS A 1 362 ? 36.856 18.154 1.951  1.00 15.87  ? 356  LYS A CA    1 
ATOM   2509 C C     . LYS A 1 362 ? 38.270 18.297 1.400  1.00 16.00  ? 356  LYS A C     1 
ATOM   2510 O O     . LYS A 1 362 ? 38.854 17.315 0.908  1.00 17.96  ? 356  LYS A O     1 
ATOM   2511 C CB    . LYS A 1 362 ? 35.847 18.734 0.963  1.00 16.40  ? 356  LYS A CB    1 
ATOM   2512 C CG    . LYS A 1 362 ? 35.780 17.876 -0.331 1.00 25.40  ? 356  LYS A CG    1 
ATOM   2513 C CD    . LYS A 1 362 ? 34.479 18.148 -1.038 1.00 34.74  ? 356  LYS A CD    1 
ATOM   2514 C CE    . LYS A 1 362 ? 34.173 17.012 -2.020 1.00 52.42  ? 356  LYS A CE    1 
ATOM   2515 N NZ    . LYS A 1 362 ? 33.239 17.461 -3.101 1.00 50.96  ? 356  LYS A NZ    1 
ATOM   2516 N N     . LEU A 1 363 ? 38.853 19.473 1.503  1.00 15.40  ? 357  LEU A N     1 
ATOM   2517 C CA    . LEU A 1 363 ? 40.159 19.778 0.924  1.00 16.13  ? 357  LEU A CA    1 
ATOM   2518 C C     . LEU A 1 363 ? 41.304 19.433 1.848  1.00 18.93  ? 357  LEU A C     1 
ATOM   2519 O O     . LEU A 1 363 ? 42.467 19.540 1.436  1.00 20.63  ? 357  LEU A O     1 
ATOM   2520 C CB    . LEU A 1 363 ? 40.256 21.278 0.627  1.00 18.33  ? 357  LEU A CB    1 
ATOM   2521 C CG    . LEU A 1 363 ? 39.279 21.785 -0.433 1.00 20.50  ? 357  LEU A CG    1 
ATOM   2522 C CD1   . LEU A 1 363 ? 39.423 23.298 -0.596 1.00 22.60  ? 357  LEU A CD1   1 
ATOM   2523 C CD2   . LEU A 1 363 ? 39.513 21.141 -1.803 1.00 23.19  ? 357  LEU A CD2   1 
ATOM   2524 N N     . ASN A 1 364 ? 41.021 19.044 3.091  1.00 14.63  ? 358  ASN A N     1 
ATOM   2525 C CA    . ASN A 1 364 ? 42.002 18.983 4.146  1.00 14.90  ? 358  ASN A CA    1 
ATOM   2526 C C     . ASN A 1 364 ? 42.797 20.279 4.261  1.00 17.81  ? 358  ASN A C     1 
ATOM   2527 O O     . ASN A 1 364 ? 44.017 20.272 4.420  1.00 19.69  ? 358  ASN A O     1 
ATOM   2528 C CB    . ASN A 1 364 ? 42.902 17.748 4.026  1.00 17.03  ? 358  ASN A CB    1 
ATOM   2529 C CG    . ASN A 1 364 ? 43.605 17.448 5.322  1.00 22.76  ? 358  ASN A CG    1 
ATOM   2530 O OD1   . ASN A 1 364 ? 43.285 18.023 6.372  1.00 20.64  ? 358  ASN A OD1   1 
ATOM   2531 N ND2   . ASN A 1 364 ? 44.582 16.545 5.271  1.00 27.38  ? 358  ASN A ND2   1 
ATOM   2532 N N     . ALA A 1 365 ? 42.098 21.400 4.243  1.00 15.80  ? 359  ALA A N     1 
ATOM   2533 C CA    . ALA A 1 365 ? 42.689 22.710 4.439  1.00 16.97  ? 359  ALA A CA    1 
ATOM   2534 C C     . ALA A 1 365 ? 42.789 23.002 5.941  1.00 15.88  ? 359  ALA A C     1 
ATOM   2535 O O     . ALA A 1 365 ? 41.949 22.570 6.731  1.00 15.88  ? 359  ALA A O     1 
ATOM   2536 C CB    . ALA A 1 365 ? 41.812 23.781 3.833  1.00 16.57  ? 359  ALA A CB    1 
ATOM   2537 N N     . PRO A 1 366 ? 43.784 23.765 6.390  1.00 15.48  ? 360  PRO A N     1 
ATOM   2538 C CA    . PRO A 1 366 ? 43.892 24.025 7.838  1.00 15.65  ? 360  PRO A CA    1 
ATOM   2539 C C     . PRO A 1 366 ? 42.703 24.826 8.328  1.00 14.62  ? 360  PRO A C     1 
ATOM   2540 O O     . PRO A 1 366 ? 42.156 25.683 7.623  1.00 15.23  ? 360  PRO A O     1 
ATOM   2541 C CB    . PRO A 1 366 ? 45.204 24.794 7.969  1.00 18.40  ? 360  PRO A CB    1 
ATOM   2542 C CG    . PRO A 1 366 ? 46.014 24.283 6.759  1.00 21.89  ? 360  PRO A CG    1 
ATOM   2543 C CD    . PRO A 1 366 ? 45.001 24.178 5.654  1.00 18.78  ? 360  PRO A CD    1 
ATOM   2544 N N     . LEU A 1 367 ? 42.318 24.504 9.549  1.00 12.24  ? 361  LEU A N     1 
ATOM   2545 C CA    . LEU A 1 367 ? 41.171 25.168 10.185 1.00 10.97  ? 361  LEU A CA    1 
ATOM   2546 C C     . LEU A 1 367 ? 41.621 26.380 10.991 1.00 10.34  ? 361  LEU A C     1 
ATOM   2547 O O     . LEU A 1 367 ? 42.755 26.429 11.527 1.00 11.15  ? 361  LEU A O     1 
ATOM   2548 C CB    . LEU A 1 367 ? 40.516 24.158 11.095 1.00 11.52  ? 361  LEU A CB    1 
ATOM   2549 C CG    . LEU A 1 367 ? 40.115 22.855 10.374 1.00 11.53  ? 361  LEU A CG    1 
ATOM   2550 C CD1   . LEU A 1 367 ? 39.339 22.033 11.361 1.00 16.19  ? 361  LEU A CD1   1 
ATOM   2551 C CD2   . LEU A 1 367 ? 39.251 23.136 9.144  1.00 14.04  ? 361  LEU A CD2   1 
ATOM   2552 N N     . ASN A 1 368 ? 40.728 27.330 11.142 1.00 10.20  ? 362  ASN A N     1 
ATOM   2553 C CA    . ASN A 1 368 ? 40.999 28.557 11.888 1.00 10.33  ? 362  ASN A CA    1 
ATOM   2554 C C     . ASN A 1 368 ? 40.488 28.463 13.324 1.00 9.97   ? 362  ASN A C     1 
ATOM   2555 O O     . ASN A 1 368 ? 39.447 27.824 13.592 1.00 10.78  ? 362  ASN A O     1 
ATOM   2556 C CB    . ASN A 1 368 ? 40.374 29.758 11.208 1.00 12.98  ? 362  ASN A CB    1 
ATOM   2557 C CG    . ASN A 1 368 ? 41.107 30.133 9.939  1.00 15.03  ? 362  ASN A CG    1 
ATOM   2558 O OD1   . ASN A 1 368 ? 42.197 29.626 9.623  1.00 18.05  ? 362  ASN A OD1   1 
ATOM   2559 N ND2   . ASN A 1 368 ? 40.533 31.036 9.160  1.00 19.24  ? 362  ASN A ND2   1 
ATOM   2560 N N     . LYS A 1 369 ? 41.240 29.062 14.267 1.00 10.36  ? 363  LYS A N     1 
ATOM   2561 C CA    . LYS A 1 369 ? 40.878 29.079 15.677 1.00 11.10  ? 363  LYS A CA    1 
ATOM   2562 C C     . LYS A 1 369 ? 39.605 29.895 15.916 1.00 11.33  ? 363  LYS A C     1 
ATOM   2563 O O     . LYS A 1 369 ? 39.270 30.823 15.161 1.00 12.38  ? 363  LYS A O     1 
ATOM   2564 C CB    . LYS A 1 369 ? 42.060 29.617 16.490 1.00 12.98  ? 363  LYS A CB    1 
ATOM   2565 C CG    . LYS A 1 369 ? 42.442 31.017 16.225 1.00 13.51  ? 363  LYS A CG    1 
ATOM   2566 C CD    . LYS A 1 369 ? 43.556 31.497 17.154 1.00 18.63  ? 363  LYS A CD    1 
ATOM   2567 C CE    . LYS A 1 369 ? 43.857 32.982 16.823 1.00 39.34  ? 363  LYS A CE    1 
ATOM   2568 N NZ    . LYS A 1 369 ? 44.809 33.706 17.748 1.00 39.99  ? 363  LYS A NZ    1 
ATOM   2569 N N     . TYR A 1 370 ? 38.954 29.546 17.016 1.00 11.45  ? 364  TYR A N     1 
ATOM   2570 C CA    . TYR A 1 370 ? 37.770 30.263 17.496 1.00 12.62  ? 364  TYR A CA    1 
ATOM   2571 C C     . TYR A 1 370 ? 38.094 31.067 18.738 1.00 16.97  ? 364  TYR A C     1 
ATOM   2572 O O     . TYR A 1 370 ? 39.054 30.796 19.466 1.00 17.47  ? 364  TYR A O     1 
ATOM   2573 C CB    . TYR A 1 370 ? 36.627 29.289 17.765 1.00 12.56  ? 364  TYR A CB    1 
ATOM   2574 C CG    . TYR A 1 370 ? 37.017 28.044 18.504 1.00 14.62  ? 364  TYR A CG    1 
ATOM   2575 C CD1   . TYR A 1 370 ? 37.211 28.077 19.884 1.00 18.27  ? 364  TYR A CD1   1 
ATOM   2576 C CD2   . TYR A 1 370 ? 37.129 26.819 17.842 1.00 15.88  ? 364  TYR A CD2   1 
ATOM   2577 C CE1   . TYR A 1 370 ? 37.544 26.924 20.564 1.00 18.28  ? 364  TYR A CE1   1 
ATOM   2578 C CE2   . TYR A 1 370 ? 37.486 25.645 18.521 1.00 19.14  ? 364  TYR A CE2   1 
ATOM   2579 C CZ    . TYR A 1 370 ? 37.663 25.731 19.879 1.00 17.54  ? 364  TYR A CZ    1 
ATOM   2580 O OH    . TYR A 1 370 ? 37.984 24.493 20.461 1.00 27.04  ? 364  TYR A OH    1 
ATOM   2581 N N     A ASN A 1 371 ? 37.320 32.120 18.935 0.55 13.58  ? 365  ASN A N     1 
ATOM   2582 N N     B ASN A 1 371 ? 37.259 32.051 18.976 0.45 13.55  ? 365  ASN A N     1 
ATOM   2583 C CA    A ASN A 1 371 ? 37.501 33.000 20.093 0.55 12.45  ? 365  ASN A CA    1 
ATOM   2584 C CA    B ASN A 1 371 ? 37.456 32.985 20.078 0.45 12.50  ? 365  ASN A CA    1 
ATOM   2585 C C     A ASN A 1 371 ? 36.308 32.839 21.038 0.55 12.21  ? 365  ASN A C     1 
ATOM   2586 C C     B ASN A 1 371 ? 36.289 32.848 21.051 0.45 12.25  ? 365  ASN A C     1 
ATOM   2587 O O     A ASN A 1 371 ? 35.236 33.416 20.808 0.55 12.91  ? 365  ASN A O     1 
ATOM   2588 O O     B ASN A 1 371 ? 35.208 33.412 20.830 0.45 12.90  ? 365  ASN A O     1 
ATOM   2589 C CB    A ASN A 1 371 ? 37.664 34.454 19.654 0.55 15.59  ? 365  ASN A CB    1 
ATOM   2590 C CB    B ASN A 1 371 ? 37.616 34.382 19.508 0.45 15.27  ? 365  ASN A CB    1 
ATOM   2591 C CG    A ASN A 1 371 ? 37.715 35.430 20.846 0.55 14.65  ? 365  ASN A CG    1 
ATOM   2592 C CG    B ASN A 1 371 ? 38.705 34.428 18.456 0.45 16.85  ? 365  ASN A CG    1 
ATOM   2593 O OD1   A ASN A 1 371 ? 38.016 35.042 22.003 0.55 14.40  ? 365  ASN A OD1   1 
ATOM   2594 O OD1   B ASN A 1 371 ? 39.854 34.029 18.711 0.45 24.63  ? 365  ASN A OD1   1 
ATOM   2595 N ND2   A ASN A 1 371 ? 37.437 36.705 20.567 0.55 19.84  ? 365  ASN A ND2   1 
ATOM   2596 N ND2   B ASN A 1 371 ? 38.355 34.871 17.259 0.45 23.63  ? 365  ASN A ND2   1 
ATOM   2597 N N     . ARG A 1 372 ? 36.521 32.116 22.142 1.00 12.40  ? 366  ARG A N     1 
ATOM   2598 C CA    . ARG A 1 372 ? 35.484 31.881 23.134 1.00 12.44  ? 366  ARG A CA    1 
ATOM   2599 C C     . ARG A 1 372 ? 34.876 33.176 23.692 1.00 12.33  ? 366  ARG A C     1 
ATOM   2600 O O     . ARG A 1 372 ? 33.692 33.186 24.058 1.00 12.50  ? 366  ARG A O     1 
ATOM   2601 C CB    . ARG A 1 372 ? 36.098 31.027 24.241 1.00 15.67  ? 366  ARG A CB    1 
ATOM   2602 C CG    . ARG A 1 372 ? 35.186 30.810 25.426 1.00 22.14  ? 366  ARG A CG    1 
ATOM   2603 C CD    . ARG A 1 372 ? 35.688 29.685 26.319 1.00 24.07  ? 366  ARG A CD    1 
ATOM   2604 N NE    . ARG A 1 372 ? 35.517 28.379 25.676 1.00 29.60  ? 366  ARG A NE    1 
ATOM   2605 C CZ    . ARG A 1 372 ? 34.360 27.724 25.582 1.00 38.03  ? 366  ARG A CZ    1 
ATOM   2606 N NH1   . ARG A 1 372 ? 33.235 28.231 26.076 1.00 28.13  ? 366  ARG A NH1   1 
ATOM   2607 N NH2   . ARG A 1 372 ? 34.320 26.555 24.933 1.00 27.31  ? 366  ARG A NH2   1 
ATOM   2608 N N     . LYS A 1 373 ? 35.642 34.277 23.760 1.00 11.98  ? 367  LYS A N     1 
ATOM   2609 C CA    . LYS A 1 373 ? 35.091 35.499 24.330 1.00 11.24  ? 367  LYS A CA    1 
ATOM   2610 C C     . LYS A 1 373 ? 33.873 35.994 23.587 1.00 12.07  ? 367  LYS A C     1 
ATOM   2611 O O     . LYS A 1 373 ? 33.060 36.689 24.174 1.00 14.01  ? 367  LYS A O     1 
ATOM   2612 C CB    . LYS A 1 373 ? 36.143 36.617 24.353 1.00 14.81  ? 367  LYS A CB    1 
ATOM   2613 C CG    . LYS A 1 373 ? 37.260 36.368 25.416 1.00 20.55  ? 367  LYS A CG    1 
ATOM   2614 C CD    . LYS A 1 373 ? 38.028 37.676 25.609 1.00 24.32  ? 367  LYS A CD    1 
ATOM   2615 C CE    . LYS A 1 373 ? 38.790 37.657 26.945 1.00 43.42  ? 367  LYS A CE    1 
ATOM   2616 N NZ    . LYS A 1 373 ? 39.857 38.699 27.024 1.00 38.51  ? 367  LYS A NZ    1 
ATOM   2617 N N     . THR A 1 374 ? 33.731 35.676 22.307 1.00 10.80  ? 368  THR A N     1 
ATOM   2618 C CA    . THR A 1 374 ? 32.598 36.155 21.514 1.00 10.49  ? 368  THR A CA    1 
ATOM   2619 C C     . THR A 1 374 ? 31.588 35.046 21.178 1.00 9.89   ? 368  THR A C     1 
ATOM   2620 O O     . THR A 1 374 ? 30.747 35.198 20.274 1.00 10.41  ? 368  THR A O     1 
ATOM   2621 C CB    . THR A 1 374 ? 33.032 36.921 20.280 1.00 11.98  ? 368  THR A CB    1 
ATOM   2622 O OG1   . THR A 1 374 ? 33.979 36.126 19.554 1.00 11.92  ? 368  THR A OG1   1 
ATOM   2623 C CG2   . THR A 1 374 ? 33.719 38.266 20.719 1.00 13.69  ? 368  THR A CG2   1 
ATOM   2624 N N     . PHE A 1 375 ? 31.631 33.950 21.933 1.00 9.37   ? 369  PHE A N     1 
ATOM   2625 C CA    . PHE A 1 375 ? 30.625 32.921 21.719 1.00 9.79   ? 369  PHE A CA    1 
ATOM   2626 C C     . PHE A 1 375 ? 29.216 33.439 22.005 1.00 8.87   ? 369  PHE A C     1 
ATOM   2627 O O     . PHE A 1 375 ? 28.265 33.098 21.279 1.00 9.03   ? 369  PHE A O     1 
ATOM   2628 C CB    . PHE A 1 375 ? 30.902 31.688 22.579 1.00 9.75   ? 369  PHE A CB    1 
ATOM   2629 C CG    . PHE A 1 375 ? 31.982 30.791 22.045 1.00 10.59  ? 369  PHE A CG    1 
ATOM   2630 C CD1   . PHE A 1 375 ? 32.696 31.063 20.915 1.00 11.69  ? 369  PHE A CD1   1 
ATOM   2631 C CD2   . PHE A 1 375 ? 32.268 29.639 22.767 1.00 12.80  ? 369  PHE A CD2   1 
ATOM   2632 C CE1   . PHE A 1 375 ? 33.732 30.183 20.511 1.00 13.47  ? 369  PHE A CE1   1 
ATOM   2633 C CE2   . PHE A 1 375 ? 33.278 28.741 22.342 1.00 13.22  ? 369  PHE A CE2   1 
ATOM   2634 C CZ    . PHE A 1 375 ? 33.952 29.040 21.229 1.00 14.24  ? 369  PHE A CZ    1 
ATOM   2635 N N     . TYR A 1 376 ? 29.022 34.228 23.086 1.00 9.39   ? 370  TYR A N     1 
ATOM   2636 C CA    . TYR A 1 376 ? 27.688 34.569 23.600 1.00 9.28   ? 370  TYR A CA    1 
ATOM   2637 C C     . TYR A 1 376 ? 27.455 36.078 23.680 1.00 10.34  ? 370  TYR A C     1 
ATOM   2638 O O     . TYR A 1 376 ? 26.485 36.475 24.350 1.00 12.34  ? 370  TYR A O     1 
ATOM   2639 C CB    . TYR A 1 376 ? 27.503 33.970 25.002 1.00 11.15  ? 370  TYR A CB    1 
ATOM   2640 C CG    . TYR A 1 376 ? 27.749 32.491 25.109 1.00 11.81  ? 370  TYR A CG    1 
ATOM   2641 C CD1   . TYR A 1 376 ? 26.949 31.565 24.429 1.00 11.37  ? 370  TYR A CD1   1 
ATOM   2642 C CD2   . TYR A 1 376 ? 28.780 31.983 25.901 1.00 12.75  ? 370  TYR A CD2   1 
ATOM   2643 C CE1   . TYR A 1 376 ? 27.152 30.197 24.564 1.00 12.26  ? 370  TYR A CE1   1 
ATOM   2644 C CE2   . TYR A 1 376 ? 28.993 30.604 26.018 1.00 15.30  ? 370  TYR A CE2   1 
ATOM   2645 C CZ    . TYR A 1 376 ? 28.175 29.762 25.342 1.00 14.27  ? 370  TYR A CZ    1 
ATOM   2646 O OH    . TYR A 1 376 ? 28.431 28.391 25.480 1.00 17.32  ? 370  TYR A OH    1 
ATOM   2647 N N     . THR A 1 377 ? 28.254 36.883 23.009 1.00 10.62  ? 371  THR A N     1 
ATOM   2648 C CA    . THR A 1 377 ? 28.034 38.325 22.956 1.00 10.41  ? 371  THR A CA    1 
ATOM   2649 C C     . THR A 1 377 ? 26.965 38.662 21.915 1.00 12.84  ? 371  THR A C     1 
ATOM   2650 O O     . THR A 1 377 ? 26.451 37.814 21.195 1.00 11.45  ? 371  THR A O     1 
ATOM   2651 C CB    . THR A 1 377 ? 29.374 38.988 22.692 1.00 11.25  ? 371  THR A CB    1 
ATOM   2652 O OG1   . THR A 1 377 ? 30.012 38.258 21.617 1.00 14.07  ? 371  THR A OG1   1 
ATOM   2653 C CG2   . THR A 1 377 ? 30.289 38.941 23.912 1.00 15.17  ? 371  THR A CG2   1 
ATOM   2654 N N     . GLN A 1 378 ? 26.551 39.946 21.863 1.00 11.22  ? 372  GLN A N     1 
ATOM   2655 C CA    . GLN A 1 378 ? 25.378 40.341 21.082 1.00 11.21  ? 372  GLN A CA    1 
ATOM   2656 C C     . GLN A 1 378 ? 25.716 40.987 19.741 1.00 12.54  ? 372  GLN A C     1 
ATOM   2657 O O     . GLN A 1 378 ? 24.796 41.255 18.969 1.00 13.21  ? 372  GLN A O     1 
ATOM   2658 C CB    . GLN A 1 378 ? 24.500 41.311 21.894 1.00 10.86  ? 372  GLN A CB    1 
ATOM   2659 C CG    . GLN A 1 378 ? 23.615 40.580 22.876 1.00 11.91  ? 372  GLN A CG    1 
ATOM   2660 C CD    . GLN A 1 378 ? 24.433 39.761 23.853 1.00 12.08  ? 372  GLN A CD    1 
ATOM   2661 O OE1   . GLN A 1 378 ? 25.110 40.281 24.706 1.00 13.31  ? 372  GLN A OE1   1 
ATOM   2662 N NE2   . GLN A 1 378 ? 24.341 38.429 23.749 1.00 11.81  ? 372  GLN A NE2   1 
ATOM   2663 N N     . ASP A 1 379 ? 26.977 41.210 19.454 1.00 11.37  ? 373  ASP A N     1 
ATOM   2664 C CA    . ASP A 1 379 ? 27.313 41.950 18.259 1.00 11.21  ? 373  ASP A CA    1 
ATOM   2665 C C     . ASP A 1 379 ? 26.880 41.139 17.034 1.00 12.42  ? 373  ASP A C     1 
ATOM   2666 O O     . ASP A 1 379 ? 27.185 39.945 16.955 1.00 11.70  ? 373  ASP A O     1 
ATOM   2667 C CB    . ASP A 1 379 ? 28.824 42.175 18.243 1.00 13.47  ? 373  ASP A CB    1 
ATOM   2668 C CG    . ASP A 1 379 ? 29.237 43.252 17.247 1.00 19.16  ? 373  ASP A CG    1 
ATOM   2669 O OD1   . ASP A 1 379 ? 29.163 43.033 16.043 1.00 15.35  ? 373  ASP A OD1   1 
ATOM   2670 O OD2   . ASP A 1 379 ? 29.611 44.394 17.681 1.00 22.27  ? 373  ASP A OD2   1 
ATOM   2671 N N     . PRO A 1 380 ? 26.218 41.742 16.050 1.00 12.24  ? 374  PRO A N     1 
ATOM   2672 C CA    . PRO A 1 380 ? 25.747 40.988 14.889 1.00 12.84  ? 374  PRO A CA    1 
ATOM   2673 C C     . PRO A 1 380 ? 26.865 40.540 13.978 1.00 11.74  ? 374  PRO A C     1 
ATOM   2674 O O     . PRO A 1 380 ? 26.593 39.735 13.080 1.00 13.72  ? 374  PRO A O     1 
ATOM   2675 C CB    . PRO A 1 380 ? 24.800 41.977 14.180 1.00 13.43  ? 374  PRO A CB    1 
ATOM   2676 C CG    . PRO A 1 380 ? 25.368 43.334 14.578 1.00 14.39  ? 374  PRO A CG    1 
ATOM   2677 C CD    . PRO A 1 380 ? 25.825 43.166 16.020 1.00 12.27  ? 374  PRO A CD    1 
ATOM   2678 N N     . VAL A 1 381 ? 28.081 41.094 14.101 1.00 11.54  ? 375  VAL A N     1 
ATOM   2679 C CA    . VAL A 1 381 ? 29.191 40.772 13.219 1.00 12.68  ? 375  VAL A CA    1 
ATOM   2680 C C     . VAL A 1 381 ? 30.369 40.155 13.978 1.00 12.51  ? 375  VAL A C     1 
ATOM   2681 O O     . VAL A 1 381 ? 30.873 39.084 13.603 1.00 11.70  ? 375  VAL A O     1 
ATOM   2682 C CB    . VAL A 1 381 ? 29.670 42.026 12.443 1.00 12.47  ? 375  VAL A CB    1 
ATOM   2683 C CG1   . VAL A 1 381 ? 30.891 41.721 11.606 1.00 16.51  ? 375  VAL A CG1   1 
ATOM   2684 C CG2   . VAL A 1 381 ? 28.558 42.581 11.536 1.00 15.78  ? 375  VAL A CG2   1 
ATOM   2685 N N     . VAL A 1 382 ? 30.847 40.840 15.012 1.00 12.31  ? 376  VAL A N     1 
ATOM   2686 C CA    . VAL A 1 382 ? 32.147 40.516 15.598 1.00 12.75  ? 376  VAL A CA    1 
ATOM   2687 C C     . VAL A 1 382 ? 32.083 39.152 16.289 1.00 11.51  ? 376  VAL A C     1 
ATOM   2688 O O     . VAL A 1 382 ? 31.282 38.929 17.205 1.00 11.95  ? 376  VAL A O     1 
ATOM   2689 C CB    . VAL A 1 382 ? 32.598 41.609 16.572 1.00 13.80  ? 376  VAL A CB    1 
ATOM   2690 C CG1   . VAL A 1 382 ? 33.838 41.194 17.324 1.00 14.26  ? 376  VAL A CG1   1 
ATOM   2691 C CG2   . VAL A 1 382 ? 32.839 42.894 15.766 1.00 13.77  ? 376  VAL A CG2   1 
ATOM   2692 N N     . GLY A 1 383 ? 32.925 38.234 15.841 1.00 11.44  ? 377  GLY A N     1 
ATOM   2693 C CA    . GLY A 1 383 ? 32.947 36.873 16.381 1.00 11.77  ? 377  GLY A CA    1 
ATOM   2694 C C     . GLY A 1 383 ? 31.751 36.070 15.953 1.00 10.23  ? 377  GLY A C     1 
ATOM   2695 O O     . GLY A 1 383 ? 31.519 34.989 16.518 1.00 10.89  ? 377  GLY A O     1 
ATOM   2696 N N     . TYR A 1 384 ? 30.996 36.532 14.963 1.00 11.32  ? 378  TYR A N     1 
ATOM   2697 C CA    . TYR A 1 384 ? 29.772 35.845 14.524 1.00 11.57  ? 378  TYR A CA    1 
ATOM   2698 C C     . TYR A 1 384 ? 29.824 35.584 13.026 1.00 11.04  ? 378  TYR A C     1 
ATOM   2699 O O     . TYR A 1 384 ? 29.825 34.427 12.576 1.00 11.77  ? 378  TYR A O     1 
ATOM   2700 C CB    . TYR A 1 384 ? 28.534 36.661 14.967 1.00 11.19  ? 378  TYR A CB    1 
ATOM   2701 C CG    . TYR A 1 384 ? 27.217 35.929 14.830 1.00 9.33   ? 378  TYR A CG    1 
ATOM   2702 C CD1   . TYR A 1 384 ? 27.012 34.694 15.451 1.00 11.01  ? 378  TYR A CD1   1 
ATOM   2703 C CD2   . TYR A 1 384 ? 26.170 36.499 14.120 1.00 11.04  ? 378  TYR A CD2   1 
ATOM   2704 C CE1   . TYR A 1 384 ? 25.778 34.011 15.367 1.00 11.07  ? 378  TYR A CE1   1 
ATOM   2705 C CE2   . TYR A 1 384 ? 24.937 35.831 14.072 1.00 12.06  ? 378  TYR A CE2   1 
ATOM   2706 C CZ    . TYR A 1 384 ? 24.769 34.633 14.703 1.00 11.50  ? 378  TYR A CZ    1 
ATOM   2707 O OH    . TYR A 1 384 ? 23.609 33.904 14.627 1.00 14.66  ? 378  TYR A OH    1 
ATOM   2708 N N     . THR A 1 385 ? 29.874 36.653 12.210 1.00 11.12  ? 379  THR A N     1 
ATOM   2709 C CA    . THR A 1 385 ? 29.904 36.488 10.754 1.00 11.85  ? 379  THR A CA    1 
ATOM   2710 C C     . THR A 1 385 ? 31.203 36.965 10.143 1.00 10.82  ? 379  THR A C     1 
ATOM   2711 O O     . THR A 1 385 ? 31.339 36.923 8.922  1.00 12.88  ? 379  THR A O     1 
ATOM   2712 C CB    . THR A 1 385 ? 28.748 37.213 10.087 1.00 12.99  ? 379  THR A CB    1 
ATOM   2713 O OG1   . THR A 1 385 ? 28.807 38.598 10.451 1.00 14.31  ? 379  THR A OG1   1 
ATOM   2714 C CG2   . THR A 1 385 ? 27.378 36.650 10.502 1.00 15.37  ? 379  THR A CG2   1 
ATOM   2715 N N     . ASP A 1 386 ? 32.168 37.392 10.948 1.00 11.10  ? 380  ASP A N     1 
ATOM   2716 C CA    . ASP A 1 386 ? 33.410 37.957 10.436 1.00 11.62  ? 380  ASP A CA    1 
ATOM   2717 C C     . ASP A 1 386 ? 34.565 36.992 10.485 1.00 14.01  ? 380  ASP A C     1 
ATOM   2718 O O     . ASP A 1 386 ? 35.707 37.394 10.254 1.00 15.34  ? 380  ASP A O     1 
ATOM   2719 C CB    . ASP A 1 386 ? 33.760 39.305 11.114 1.00 14.31  ? 380  ASP A CB    1 
ATOM   2720 C CG    . ASP A 1 386 ? 34.074 39.186 12.552 1.00 16.75  ? 380  ASP A CG    1 
ATOM   2721 O OD1   . ASP A 1 386 ? 33.924 38.084 13.158 1.00 15.04  ? 380  ASP A OD1   1 
ATOM   2722 O OD2   . ASP A 1 386 ? 34.455 40.241 13.167 1.00 18.13  ? 380  ASP A OD2   1 
ATOM   2723 N N     . TYR A 1 387 ? 34.334 35.697 10.750 1.00 12.12  ? 381  TYR A N     1 
ATOM   2724 C CA    . TYR A 1 387 ? 35.389 34.710 10.537 1.00 12.30  ? 381  TYR A CA    1 
ATOM   2725 C C     . TYR A 1 387 ? 35.500 34.446 9.038  1.00 13.89  ? 381  TYR A C     1 
ATOM   2726 O O     . TYR A 1 387 ? 34.496 34.152 8.392  1.00 13.94  ? 381  TYR A O     1 
ATOM   2727 C CB    . TYR A 1 387 ? 35.056 33.400 11.255 1.00 11.67  ? 381  TYR A CB    1 
ATOM   2728 C CG    . TYR A 1 387 ? 35.168 33.416 12.750 1.00 10.86  ? 381  TYR A CG    1 
ATOM   2729 C CD1   . TYR A 1 387 ? 36.405 33.261 13.378 1.00 11.56  ? 381  TYR A CD1   1 
ATOM   2730 C CD2   . TYR A 1 387 ? 34.021 33.511 13.587 1.00 10.76  ? 381  TYR A CD2   1 
ATOM   2731 C CE1   . TYR A 1 387 ? 36.514 33.185 14.761 1.00 12.43  ? 381  TYR A CE1   1 
ATOM   2732 C CE2   . TYR A 1 387 ? 34.122 33.452 14.962 1.00 10.46  ? 381  TYR A CE2   1 
ATOM   2733 C CZ    . TYR A 1 387 ? 35.358 33.288 15.547 1.00 11.22  ? 381  TYR A CZ    1 
ATOM   2734 O OH    . TYR A 1 387 ? 35.455 33.158 16.899 1.00 13.41  ? 381  TYR A OH    1 
ATOM   2735 N N     . PRO A 1 388 ? 36.684 34.559 8.441  1.00 16.37  ? 382  PRO A N     1 
ATOM   2736 C CA    . PRO A 1 388 ? 36.774 34.492 6.986  1.00 16.39  ? 382  PRO A CA    1 
ATOM   2737 C C     . PRO A 1 388 ? 36.689 33.081 6.432  1.00 13.94  ? 382  PRO A C     1 
ATOM   2738 O O     . PRO A 1 388 ? 36.928 32.079 7.104  1.00 15.09  ? 382  PRO A O     1 
ATOM   2739 C CB    . PRO A 1 388 ? 38.170 35.067 6.697  1.00 20.39  ? 382  PRO A CB    1 
ATOM   2740 C CG    . PRO A 1 388 ? 38.924 34.822 7.968  1.00 22.96  ? 382  PRO A CG    1 
ATOM   2741 C CD    . PRO A 1 388 ? 37.910 35.100 9.065  1.00 17.03  ? 382  PRO A CD    1 
ATOM   2742 N N     . PHE A 1 389 ? 36.345 33.044 5.165  1.00 15.88  ? 383  PHE A N     1 
ATOM   2743 C CA    . PHE A 1 389 ? 36.409 31.873 4.353  1.00 15.08  ? 383  PHE A CA    1 
ATOM   2744 C C     . PHE A 1 389 ? 37.842 31.652 3.917  1.00 20.26  ? 383  PHE A C     1 
ATOM   2745 O O     . PHE A 1 389 ? 38.711 32.531 4.048  1.00 20.87  ? 383  PHE A O     1 
ATOM   2746 C CB    . PHE A 1 389 ? 35.566 32.097 3.106  1.00 16.76  ? 383  PHE A CB    1 
ATOM   2747 C CG    . PHE A 1 389 ? 34.077 32.067 3.393  1.00 16.34  ? 383  PHE A CG    1 
ATOM   2748 C CD1   . PHE A 1 389 ? 33.415 33.168 3.951  1.00 18.81  ? 383  PHE A CD1   1 
ATOM   2749 C CD2   . PHE A 1 389 ? 33.355 30.925 3.150  1.00 18.04  ? 383  PHE A CD2   1 
ATOM   2750 C CE1   . PHE A 1 389 ? 32.028 33.079 4.229  1.00 20.20  ? 383  PHE A CE1   1 
ATOM   2751 C CE2   . PHE A 1 389 ? 31.978 30.860 3.414  1.00 18.66  ? 383  PHE A CE2   1 
ATOM   2752 C CZ    . PHE A 1 389 ? 31.342 31.929 3.981  1.00 15.91  ? 383  PHE A CZ    1 
ATOM   2753 N N     . LEU A 1 390 ? 38.090 30.468 3.386  1.00 18.12  ? 384  LEU A N     1 
ATOM   2754 C CA    . LEU A 1 390 ? 39.370 30.217 2.713  1.00 21.25  ? 384  LEU A CA    1 
ATOM   2755 C C     . LEU A 1 390 ? 39.722 31.261 1.652  1.00 28.69  ? 384  LEU A C     1 
ATOM   2756 O O     . LEU A 1 390 ? 38.817 31.667 0.899  1.00 24.43  ? 384  LEU A O     1 
ATOM   2757 C CB    . LEU A 1 390 ? 39.297 28.873 1.997  1.00 21.77  ? 384  LEU A CB    1 
ATOM   2758 C CG    . LEU A 1 390 ? 39.440 27.682 2.906  1.00 23.85  ? 384  LEU A CG    1 
ATOM   2759 C CD1   . LEU A 1 390 ? 39.144 26.438 2.043  1.00 19.91  ? 384  LEU A CD1   1 
ATOM   2760 C CD2   . LEU A 1 390 ? 40.871 27.644 3.467  1.00 30.74  ? 384  LEU A CD2   1 
HETATM 2761 N N1    . FMN B 2 .   ? 24.201 22.114 22.359 1.00 8.65   ? 401  FMN A N1    1 
HETATM 2762 C C2    . FMN B 2 .   ? 22.847 22.074 22.196 1.00 8.36   ? 401  FMN A C2    1 
HETATM 2763 O O2    . FMN B 2 .   ? 22.232 20.995 22.142 1.00 8.26   ? 401  FMN A O2    1 
HETATM 2764 N N3    . FMN B 2 .   ? 22.138 23.247 22.015 1.00 8.40   ? 401  FMN A N3    1 
HETATM 2765 C C4    . FMN B 2 .   ? 22.734 24.492 22.063 1.00 9.87   ? 401  FMN A C4    1 
HETATM 2766 O O4    . FMN B 2 .   ? 22.018 25.521 21.853 1.00 9.43   ? 401  FMN A O4    1 
HETATM 2767 C C4A   . FMN B 2 .   ? 24.130 24.527 22.288 1.00 7.74   ? 401  FMN A C4A   1 
HETATM 2768 N N5    . FMN B 2 .   ? 24.803 25.744 22.340 1.00 8.73   ? 401  FMN A N5    1 
HETATM 2769 C C5A   . FMN B 2 .   ? 26.174 25.736 22.360 1.00 8.29   ? 401  FMN A C5A   1 
HETATM 2770 C C6    . FMN B 2 .   ? 26.818 26.972 22.302 1.00 8.56   ? 401  FMN A C6    1 
HETATM 2771 C C7    . FMN B 2 .   ? 28.182 27.017 22.244 1.00 8.48   ? 401  FMN A C7    1 
HETATM 2772 C C7M   . FMN B 2 .   ? 28.850 28.381 22.168 1.00 11.36  ? 401  FMN A C7M   1 
HETATM 2773 C C8    . FMN B 2 .   ? 28.932 25.822 22.350 1.00 11.49  ? 401  FMN A C8    1 
HETATM 2774 C C8M   . FMN B 2 .   ? 30.460 25.875 22.386 1.00 16.87  ? 401  FMN A C8M   1 
HETATM 2775 C C9    . FMN B 2 .   ? 28.262 24.594 22.429 1.00 11.66  ? 401  FMN A C9    1 
HETATM 2776 C C9A   . FMN B 2 .   ? 26.860 24.540 22.396 1.00 8.83   ? 401  FMN A C9A   1 
HETATM 2777 N N10   . FMN B 2 .   ? 26.196 23.327 22.444 1.00 8.69   ? 401  FMN A N10   1 
HETATM 2778 C C10   . FMN B 2 .   ? 24.818 23.317 22.354 1.00 7.99   ? 401  FMN A C10   1 
HETATM 2779 C "C1'" . FMN B 2 .   ? 26.920 22.011 22.390 1.00 10.00  ? 401  FMN A "C1'" 1 
HETATM 2780 C "C2'" . FMN B 2 .   ? 27.382 21.824 20.915 1.00 9.83   ? 401  FMN A "C2'" 1 
HETATM 2781 O "O2'" . FMN B 2 .   ? 26.253 21.512 20.105 1.00 9.48   ? 401  FMN A "O2'" 1 
HETATM 2782 C "C3'" . FMN B 2 .   ? 28.386 20.671 20.732 1.00 9.79   ? 401  FMN A "C3'" 1 
HETATM 2783 O "O3'" . FMN B 2 .   ? 27.759 19.458 21.155 1.00 10.93  ? 401  FMN A "O3'" 1 
HETATM 2784 C "C4'" . FMN B 2 .   ? 29.676 20.853 21.551 1.00 11.93  ? 401  FMN A "C4'" 1 
HETATM 2785 O "O4'" . FMN B 2 .   ? 30.256 22.119 21.289 1.00 15.99  ? 401  FMN A "O4'" 1 
HETATM 2786 C "C5'" . FMN B 2 .   ? 30.714 19.690 21.455 1.00 17.38  ? 401  FMN A "C5'" 1 
HETATM 2787 O "O5'" . FMN B 2 .   ? 31.072 19.611 20.067 1.00 13.55  ? 401  FMN A "O5'" 1 
HETATM 2788 P P     . FMN B 2 .   ? 32.436 20.314 19.434 1.00 12.73  ? 401  FMN A P     1 
HETATM 2789 O O1P   . FMN B 2 .   ? 33.664 19.587 20.052 1.00 15.82  ? 401  FMN A O1P   1 
HETATM 2790 O O2P   . FMN B 2 .   ? 32.403 21.730 19.759 1.00 12.42  ? 401  FMN A O2P   1 
HETATM 2791 O O3P   . FMN B 2 .   ? 32.281 19.997 17.971 1.00 12.99  ? 401  FMN A O3P   1 
HETATM 2792 N NBU   . 5J8 C 3 .   ? 22.227 25.246 24.976 0.70 13.75  ? 402  5J8 A NBU   1 
HETATM 2793 C CBT   . 5J8 C 3 .   ? 23.179 24.240 25.258 0.70 12.21  ? 402  5J8 A CBT   1 
HETATM 2794 O OBV   . 5J8 C 3 .   ? 22.953 23.054 25.221 0.70 8.77   ? 402  5J8 A OBV   1 
HETATM 2795 C CBR   . 5J8 C 3 .   ? 24.502 24.802 25.673 0.70 13.51  ? 402  5J8 A CBR   1 
HETATM 2796 C CBQ   . 5J8 C 3 .   ? 25.535 23.690 25.837 0.70 13.36  ? 402  5J8 A CBQ   1 
HETATM 2797 C CBS   . 5J8 C 3 .   ? 24.835 26.167 25.847 0.70 13.70  ? 402  5J8 A CBS   1 
HETATM 2798 C CBN   . 5J8 C 3 .   ? 26.180 26.324 26.648 0.70 20.95  ? 402  5J8 A CBN   1 
HETATM 2799 C CBO   . 5J8 C 3 .   ? 27.188 25.592 26.035 0.70 19.22  ? 402  5J8 A CBO   1 
HETATM 2800 N NBP   . 5J8 C 3 .   ? 26.829 24.033 26.137 0.70 16.00  ? 402  5J8 A NBP   1 
HETATM 2801 C CBM   . 5J8 C 3 .   ? 27.589 22.960 26.595 0.70 17.59  ? 402  5J8 A CBM   1 
HETATM 2802 O OBG   . 5J8 C 3 .   ? 27.726 23.421 28.101 0.70 22.55  ? 402  5J8 A OBG   1 
HETATM 2803 C CBF   . 5J8 C 3 .   ? 28.847 22.954 26.163 0.70 21.17  ? 402  5J8 A CBF   1 
HETATM 2804 O OBI   . 5J8 C 3 .   ? 29.111 22.018 25.042 0.70 20.01  ? 402  5J8 A OBI   1 
HETATM 2805 C CBE   . 5J8 C 3 .   ? 29.647 22.404 27.355 0.70 21.75  ? 402  5J8 A CBE   1 
HETATM 2806 O OBJ   . 5J8 C 3 .   ? 29.591 21.043 27.435 0.70 22.98  ? 402  5J8 A OBJ   1 
HETATM 2807 C CBH   . 5J8 C 3 .   ? 28.919 23.037 28.556 0.70 22.19  ? 402  5J8 A CBH   1 
HETATM 2808 C CBK   . 5J8 C 3 .   ? 29.730 24.290 29.031 0.70 29.69  ? 402  5J8 A CBK   1 
HETATM 2809 O OBL   . 5J8 C 3 .   ? 29.874 25.211 27.952 0.70 31.40  ? 402  5J8 A OBL   1 
HETATM 2810 P PAA   . 5J8 C 3 .   ? 30.719 26.629 28.129 0.70 27.69  ? 402  5J8 A PAA   1 
HETATM 2811 O OAC   . 5J8 C 3 .   ? 30.636 27.335 26.760 0.70 22.39  ? 402  5J8 A OAC   1 
HETATM 2812 O OAB   . 5J8 C 3 .   ? 30.018 27.376 29.252 0.70 33.38  ? 402  5J8 A OAB   1 
HETATM 2813 O OAD   . 5J8 C 3 .   ? 32.283 26.337 28.673 0.70 36.99  ? 402  5J8 A OAD   1 
HETATM 2814 P PAE   . 5J8 C 3 .   ? 33.158 24.926 28.650 0.70 64.72  ? 402  5J8 A PAE   1 
HETATM 2815 O OAG   . 5J8 C 3 .   ? 32.944 24.254 27.323 0.70 47.83  ? 402  5J8 A OAG   1 
HETATM 2816 O OAF   . 5J8 C 3 .   ? 32.720 24.001 29.757 0.70 53.99  ? 402  5J8 A OAF   1 
HETATM 2817 O "O5'" . 5J8 C 3 .   ? 34.769 25.293 28.859 0.70 51.64  ? 402  5J8 A "O5'" 1 
HETATM 2818 C C4    . 5J8 D 3 .   ? 2.159  3.215  22.137 0.76 20.08  ? 403  5J8 A C4    1 
HETATM 2819 C C5    . 5J8 D 3 .   ? 1.663  1.959  22.147 0.76 23.08  ? 403  5J8 A C5    1 
HETATM 2820 C C6    . 5J8 D 3 .   ? 2.496  0.897  21.873 0.76 23.77  ? 403  5J8 A C6    1 
HETATM 2821 C C8    . 5J8 D 3 .   ? 0.034  3.334  22.591 0.76 25.14  ? 403  5J8 A C8    1 
HETATM 2822 N N1    . 5J8 D 3 .   ? 3.788  1.112  21.627 0.76 22.89  ? 403  5J8 A N1    1 
HETATM 2823 N N3    . 5J8 D 3 .   ? 3.465  3.448  21.882 0.76 18.36  ? 403  5J8 A N3    1 
HETATM 2824 O OAD   . 5J8 D 3 .   ? -2.235 4.615  26.919 0.76 49.67  ? 403  5J8 A OAD   1 
HETATM 2825 P PAE   . 5J8 D 3 .   ? -2.536 5.723  25.715 0.76 54.17  ? 403  5J8 A PAE   1 
HETATM 2826 O OAG   . 5J8 D 3 .   ? -3.563 5.193  24.750 0.76 48.01  ? 403  5J8 A OAG   1 
HETATM 2827 O OAF   . 5J8 D 3 .   ? -3.008 7.016  26.332 0.76 43.49  ? 403  5J8 A OAF   1 
HETATM 2828 O "O5'" . 5J8 D 3 .   ? -1.115 6.006  24.908 0.76 41.43  ? 403  5J8 A "O5'" 1 
HETATM 2829 C "C5'" . 5J8 D 3 .   ? -0.043 6.737  25.488 0.76 28.11  ? 403  5J8 A "C5'" 1 
HETATM 2830 C "C4'" . 5J8 D 3 .   ? 1.024  6.933  24.367 0.76 25.36  ? 403  5J8 A "C4'" 1 
HETATM 2831 O "O4'" . 5J8 D 3 .   ? 1.518  5.744  24.044 0.76 22.39  ? 403  5J8 A "O4'" 1 
HETATM 2832 C "C3'" . 5J8 D 3 .   ? 0.371  7.465  23.076 0.76 28.73  ? 403  5J8 A "C3'" 1 
HETATM 2833 O "O3'" . 5J8 D 3 .   ? 1.211  8.373  22.456 0.76 24.43  ? 403  5J8 A "O3'" 1 
HETATM 2834 C "C2'" . 5J8 D 3 .   ? 0.174  6.185  22.224 0.76 20.69  ? 403  5J8 A "C2'" 1 
HETATM 2835 O "O2'" . 5J8 D 3 .   ? 0.167  6.573  20.822 0.76 19.83  ? 403  5J8 A "O2'" 1 
HETATM 2836 P "P2'" . 5J8 D 3 .   ? -1.228 6.739  19.979 0.76 21.57  ? 403  5J8 A "P2'" 1 
HETATM 2837 O OP1   . 5J8 D 3 .   ? -0.820 7.651  18.848 0.76 22.87  ? 403  5J8 A OP1   1 
HETATM 2838 O OP3   . 5J8 D 3 .   ? -2.308 7.399  20.819 0.76 24.48  ? 403  5J8 A OP3   1 
HETATM 2839 O OP2   . 5J8 D 3 .   ? -1.670 5.374  19.495 0.76 25.05  ? 403  5J8 A OP2   1 
HETATM 2840 C "C1'" . 5J8 D 3 .   ? 1.264  5.493  22.497 0.76 19.60  ? 403  5J8 A "C1'" 1 
HETATM 2841 N N9    . 5J8 D 3 .   ? 1.157  4.049  22.380 0.76 18.54  ? 403  5J8 A N9    1 
HETATM 2842 N N7    . 5J8 D 3 .   ? 0.338  2.041  22.421 0.76 22.97  ? 403  5J8 A N7    1 
HETATM 2843 C C2    . 5J8 D 3 .   ? 4.283  2.390  21.630 0.76 21.44  ? 403  5J8 A C2    1 
HETATM 2844 N N6    . 5J8 D 3 .   ? 2.214  -0.535 21.822 0.76 23.86  ? 403  5J8 A N6    1 
HETATM 2845 S S     . SO4 E 4 .   ? 37.824 25.721 24.445 1.00 101.32 ? 404  SO4 A S     1 
HETATM 2846 O O1    . SO4 E 4 .   ? 38.773 25.166 23.427 1.00 57.99  ? 404  SO4 A O1    1 
HETATM 2847 O O2    . SO4 E 4 .   ? 36.444 25.389 23.971 1.00 37.56  ? 404  SO4 A O2    1 
HETATM 2848 O O3    . SO4 E 4 .   ? 38.020 27.222 24.519 1.00 63.54  ? 404  SO4 A O3    1 
HETATM 2849 O O4    . SO4 E 4 .   ? 38.003 25.037 25.781 1.00 62.12  ? 404  SO4 A O4    1 
HETATM 2850 O O     . HOH F 5 .   ? 39.811 23.945 22.067 1.00 37.50  ? 501  HOH A O     1 
HETATM 2851 O O     . HOH F 5 .   ? 10.275 25.106 47.287 1.00 44.14  ? 502  HOH A O     1 
HETATM 2852 O O     . HOH F 5 .   ? 32.179 24.709 25.219 1.00 35.01  ? 503  HOH A O     1 
HETATM 2853 O O     . HOH F 5 .   ? -6.144 23.578 30.250 1.00 31.78  ? 504  HOH A O     1 
HETATM 2854 O O     . HOH F 5 .   ? 29.948 38.574 5.867  1.00 40.76  ? 505  HOH A O     1 
HETATM 2855 O O     . HOH F 5 .   ? 33.775 5.755  23.537 1.00 41.44  ? 506  HOH A O     1 
HETATM 2856 O O     . HOH F 5 .   ? 11.344 4.152  41.356 1.00 35.15  ? 507  HOH A O     1 
HETATM 2857 O O     . HOH F 5 .   ? 14.661 39.278 11.277 1.00 29.44  ? 508  HOH A O     1 
HETATM 2858 O O     . HOH F 5 .   ? 3.442  32.650 9.294  1.00 49.86  ? 509  HOH A O     1 
HETATM 2859 O O     . HOH F 5 .   ? 31.410 46.006 17.107 1.00 21.24  ? 510  HOH A O     1 
HETATM 2860 O O     . HOH F 5 .   ? 27.597 27.956 29.429 1.00 38.83  ? 511  HOH A O     1 
HETATM 2861 O O     . HOH F 5 .   ? 34.227 6.881  16.378 1.00 36.02  ? 512  HOH A O     1 
HETATM 2862 O O     . HOH F 5 .   ? 11.993 34.933 2.913  1.00 27.40  ? 513  HOH A O     1 
HETATM 2863 O O     . HOH F 5 .   ? 23.338 40.379 6.958  1.00 44.58  ? 514  HOH A O     1 
HETATM 2864 O O     . HOH F 5 .   ? 15.018 -2.827 27.888 1.00 38.44  ? 515  HOH A O     1 
HETATM 2865 O O     . HOH F 5 .   ? 10.170 0.393  27.383 1.00 32.11  ? 516  HOH A O     1 
HETATM 2866 O O     . HOH F 5 .   ? 44.104 32.781 19.992 1.00 44.68  ? 517  HOH A O     1 
HETATM 2867 O O     . HOH F 5 .   ? 43.518 17.569 9.204  1.00 30.64  ? 518  HOH A O     1 
HETATM 2868 O O     . HOH F 5 .   ? 35.647 -3.675 29.445 1.00 40.06  ? 519  HOH A O     1 
HETATM 2869 O O     . HOH F 5 .   ? -2.293 9.786  21.759 1.00 37.76  ? 520  HOH A O     1 
HETATM 2870 O O     . HOH F 5 .   ? 1.607  26.334 36.837 1.00 38.03  ? 521  HOH A O     1 
HETATM 2871 O O     . HOH F 5 .   ? 16.839 17.199 42.911 1.00 22.10  ? 522  HOH A O     1 
HETATM 2872 O O     . HOH F 5 .   ? 29.180 5.764  18.161 1.00 28.63  ? 523  HOH A O     1 
HETATM 2873 O O     . HOH F 5 .   ? 20.704 4.389  7.620  1.00 40.66  ? 524  HOH A O     1 
HETATM 2874 O O     . HOH F 5 .   ? 10.492 29.156 4.593  1.00 26.45  ? 525  HOH A O     1 
HETATM 2875 O O     . HOH F 5 .   ? 19.591 5.185  36.567 1.00 31.35  ? 526  HOH A O     1 
HETATM 2876 O O     . HOH F 5 .   ? 14.622 29.280 49.008 1.00 17.97  ? 527  HOH A O     1 
HETATM 2877 O O     . HOH F 5 .   ? 16.564 7.159  6.108  1.00 40.55  ? 528  HOH A O     1 
HETATM 2878 O O     . HOH F 5 .   ? 11.055 8.455  43.953 1.00 43.29  ? 529  HOH A O     1 
HETATM 2879 O O     . HOH F 5 .   ? 31.480 37.871 30.372 1.00 32.36  ? 530  HOH A O     1 
HETATM 2880 O O     . HOH F 5 .   ? 5.788  -0.852 12.901 1.00 33.57  ? 531  HOH A O     1 
HETATM 2881 O O     . HOH F 5 .   ? 29.113 18.435 18.113 1.00 19.12  ? 532  HOH A O     1 
HETATM 2882 O O     . HOH F 5 .   ? 23.434 28.036 31.913 1.00 16.40  ? 533  HOH A O     1 
HETATM 2883 O O     . HOH F 5 .   ? 23.773 16.130 30.428 1.00 25.10  ? 534  HOH A O     1 
HETATM 2884 O O     . HOH F 5 .   ? 22.878 15.200 39.514 1.00 38.80  ? 535  HOH A O     1 
HETATM 2885 O O     . HOH F 5 .   ? 11.505 34.603 41.674 1.00 30.41  ? 536  HOH A O     1 
HETATM 2886 O O     . HOH F 5 .   ? 33.253 37.917 26.480 1.00 29.41  ? 537  HOH A O     1 
HETATM 2887 O O     . HOH F 5 .   ? 22.552 20.538 42.806 1.00 34.24  ? 538  HOH A O     1 
HETATM 2888 O O     . HOH F 5 .   ? 25.675 39.315 38.352 1.00 36.51  ? 539  HOH A O     1 
HETATM 2889 O O     . HOH F 5 .   ? 33.397 8.102  21.840 1.00 37.04  ? 540  HOH A O     1 
HETATM 2890 O O     . HOH F 5 .   ? 7.647  40.062 11.524 1.00 41.99  ? 541  HOH A O     1 
HETATM 2891 O O     . HOH F 5 .   ? 6.133  2.813  36.009 1.00 28.60  ? 542  HOH A O     1 
HETATM 2892 O O     . HOH F 5 .   ? 7.524  26.270 31.049 1.00 17.27  ? 543  HOH A O     1 
HETATM 2893 O O     . HOH F 5 .   ? 21.090 32.079 0.025  1.00 19.66  ? 544  HOH A O     1 
HETATM 2894 O O     . HOH F 5 .   ? 6.400  14.249 7.996  1.00 27.62  ? 545  HOH A O     1 
HETATM 2895 O O     . HOH F 5 .   ? 23.447 3.092  9.558  1.00 25.44  ? 546  HOH A O     1 
HETATM 2896 O O     . HOH F 5 .   ? 22.713 27.985 42.828 1.00 13.79  ? 547  HOH A O     1 
HETATM 2897 O O     . HOH F 5 .   ? 19.635 29.852 -4.821 1.00 18.38  ? 548  HOH A O     1 
HETATM 2898 O O     . HOH F 5 .   ? 10.522 40.376 22.126 1.00 36.65  ? 549  HOH A O     1 
HETATM 2899 O O     . HOH F 5 .   ? 35.487 28.119 0.884  1.00 24.33  ? 550  HOH A O     1 
HETATM 2900 O O     . HOH F 5 .   ? 2.021  14.505 40.753 1.00 26.46  ? 551  HOH A O     1 
HETATM 2901 O O     . HOH F 5 .   ? 38.963 14.798 2.054  1.00 33.56  ? 552  HOH A O     1 
HETATM 2902 O O     . HOH F 5 .   ? 33.300 33.670 18.345 1.00 13.09  ? 553  HOH A O     1 
HETATM 2903 O O     . HOH F 5 .   ? 36.594 40.344 14.723 1.00 28.51  ? 554  HOH A O     1 
HETATM 2904 O O     . HOH F 5 .   ? 29.120 27.554 2.963  1.00 27.04  ? 555  HOH A O     1 
HETATM 2905 O O     . HOH F 5 .   ? 27.795 18.719 37.694 1.00 30.58  ? 556  HOH A O     1 
HETATM 2906 O O     . HOH F 5 .   ? 8.700  4.974  30.286 1.00 34.98  ? 557  HOH A O     1 
HETATM 2907 O O     . HOH F 5 .   ? 29.902 45.195 20.200 1.00 24.75  ? 558  HOH A O     1 
HETATM 2908 O O     . HOH F 5 .   ? 11.009 20.193 4.073  1.00 21.89  ? 559  HOH A O     1 
HETATM 2909 O O     . HOH F 5 .   ? 5.122  25.922 32.528 1.00 25.32  ? 560  HOH A O     1 
HETATM 2910 O O     . HOH F 5 .   ? 22.190 14.309 43.204 1.00 39.43  ? 561  HOH A O     1 
HETATM 2911 O O     . HOH F 5 .   ? 2.504  22.663 38.564 1.00 18.55  ? 562  HOH A O     1 
HETATM 2912 O O     . HOH F 5 .   ? 31.442 22.632 23.891 1.00 21.72  ? 563  HOH A O     1 
HETATM 2913 O O     . HOH F 5 .   ? -2.307 9.058  17.132 1.00 47.14  ? 564  HOH A O     1 
HETATM 2914 O O     . HOH F 5 .   ? 32.014 4.174  21.580 1.00 29.95  ? 565  HOH A O     1 
HETATM 2915 O O     . HOH F 5 .   ? 23.375 31.497 15.794 1.00 14.46  ? 566  HOH A O     1 
HETATM 2916 O O     . HOH F 5 .   ? 27.781 8.442  36.661 1.00 33.43  ? 567  HOH A O     1 
HETATM 2917 O O     . HOH F 5 .   ? 0.506  17.912 23.448 1.00 20.91  ? 568  HOH A O     1 
HETATM 2918 O O     . HOH F 5 .   ? 8.208  1.817  37.158 1.00 20.12  ? 569  HOH A O     1 
HETATM 2919 O O     . HOH F 5 .   ? 17.123 9.002  9.074  1.00 15.78  ? 570  HOH A O     1 
HETATM 2920 O O     . HOH F 5 .   ? -0.454 18.026 12.656 1.00 27.45  ? 571  HOH A O     1 
HETATM 2921 O O     . HOH F 5 .   ? 22.690 18.204 -2.742 1.00 33.52  ? 572  HOH A O     1 
HETATM 2922 O O     . HOH F 5 .   ? 24.586 29.213 41.116 1.00 14.08  ? 573  HOH A O     1 
HETATM 2923 O O     . HOH F 5 .   ? 32.079 17.345 17.586 1.00 13.45  ? 574  HOH A O     1 
HETATM 2924 O O     . HOH F 5 .   ? 15.542 38.632 30.093 1.00 29.56  ? 575  HOH A O     1 
HETATM 2925 O O     . HOH F 5 .   ? 30.815 40.019 19.752 1.00 17.30  ? 576  HOH A O     1 
HETATM 2926 O O     . HOH F 5 .   ? 37.871 31.844 9.614  1.00 18.74  ? 577  HOH A O     1 
HETATM 2927 O O     . HOH F 5 .   ? -1.297 12.699 37.090 1.00 21.95  ? 578  HOH A O     1 
HETATM 2928 O O     . HOH F 5 .   ? 7.308  29.894 38.777 1.00 24.34  ? 579  HOH A O     1 
HETATM 2929 O O     . HOH F 5 .   ? 7.123  25.751 28.487 1.00 15.35  ? 580  HOH A O     1 
HETATM 2930 O O     . HOH F 5 .   ? 2.142  -0.687 18.081 1.00 28.31  ? 581  HOH A O     1 
HETATM 2931 O O     . HOH F 5 .   ? 24.738 28.448 15.923 1.00 12.18  ? 582  HOH A O     1 
HETATM 2932 O O     . HOH F 5 .   ? 21.253 31.869 20.524 1.00 11.24  ? 583  HOH A O     1 
HETATM 2933 O O     . HOH F 5 .   ? 8.993  29.846 35.044 1.00 24.89  ? 584  HOH A O     1 
HETATM 2934 O O     . HOH F 5 .   ? 16.756 21.868 1.015  1.00 16.77  ? 585  HOH A O     1 
HETATM 2935 O O     . HOH F 5 .   ? 40.414 32.696 13.586 1.00 19.72  ? 586  HOH A O     1 
HETATM 2936 O O     . HOH F 5 .   ? 16.621 9.967  42.017 1.00 37.39  ? 587  HOH A O     1 
HETATM 2937 O O     . HOH F 5 .   ? 13.380 30.814 43.243 1.00 22.18  ? 588  HOH A O     1 
HETATM 2938 O O     . HOH F 5 .   ? 26.382 5.318  7.524  1.00 16.95  ? 589  HOH A O     1 
HETATM 2939 O O     . HOH F 5 .   ? 7.591  37.807 19.367 1.00 26.47  ? 590  HOH A O     1 
HETATM 2940 O O     . HOH F 5 .   ? 22.913 32.264 30.476 1.00 12.44  ? 591  HOH A O     1 
HETATM 2941 O O     . HOH F 5 .   ? 20.901 28.481 31.202 1.00 12.73  ? 592  HOH A O     1 
HETATM 2942 O O     . HOH F 5 .   ? 42.083 14.335 15.606 1.00 38.87  ? 593  HOH A O     1 
HETATM 2943 O O     . HOH F 5 .   ? 13.927 11.730 7.948  1.00 23.74  ? 594  HOH A O     1 
HETATM 2944 O O     . HOH F 5 .   ? 25.836 39.866 10.479 1.00 26.41  ? 595  HOH A O     1 
HETATM 2945 O O     . HOH F 5 .   ? 27.866 20.262 -0.939 1.00 27.16  ? 596  HOH A O     1 
HETATM 2946 O O     . HOH F 5 .   ? 26.565 6.604  0.183  1.00 39.28  ? 597  HOH A O     1 
HETATM 2947 O O     . HOH F 5 .   ? 13.787 9.279  40.489 1.00 31.30  ? 598  HOH A O     1 
HETATM 2948 O O     . HOH F 5 .   ? 25.956 34.984 4.416  1.00 31.57  ? 599  HOH A O     1 
HETATM 2949 O O     . HOH F 5 .   ? 28.139 30.350 32.950 1.00 25.76  ? 600  HOH A O     1 
HETATM 2950 O O     . HOH F 5 .   ? 14.344 23.290 47.418 1.00 18.82  ? 601  HOH A O     1 
HETATM 2951 O O     . HOH F 5 .   ? 26.484 22.890 5.484  1.00 12.63  ? 602  HOH A O     1 
HETATM 2952 O O     . HOH F 5 .   ? 21.072 -0.095 14.525 1.00 24.62  ? 603  HOH A O     1 
HETATM 2953 O O     . HOH F 5 .   ? 12.304 36.523 27.271 1.00 27.21  ? 604  HOH A O     1 
HETATM 2954 O O     . HOH F 5 .   ? 14.258 21.039 24.992 1.00 9.84   ? 605  HOH A O     1 
HETATM 2955 O O     . HOH F 5 .   ? 20.170 29.564 21.636 1.00 10.30  ? 606  HOH A O     1 
HETATM 2956 O O     . HOH F 5 .   ? 35.926 36.518 14.123 1.00 23.70  ? 607  HOH A O     1 
HETATM 2957 O O     . HOH F 5 .   ? 28.002 18.820 23.788 1.00 17.00  ? 608  HOH A O     1 
HETATM 2958 O O     . HOH F 5 .   ? 1.941  10.600 24.938 1.00 22.95  ? 609  HOH A O     1 
HETATM 2959 O O     . HOH F 5 .   ? 18.818 17.382 50.299 1.00 25.57  ? 610  HOH A O     1 
HETATM 2960 O O     . HOH F 5 .   ? 20.407 13.494 28.214 1.00 12.28  ? 611  HOH A O     1 
HETATM 2961 O O     . HOH F 5 .   ? 24.594 42.866 25.388 1.00 16.69  ? 612  HOH A O     1 
HETATM 2962 O O     . HOH F 5 .   ? 14.149 21.500 1.975  1.00 21.86  ? 613  HOH A O     1 
HETATM 2963 O O     . HOH F 5 .   ? 16.557 7.451  12.522 1.00 13.92  ? 614  HOH A O     1 
HETATM 2964 O O     . HOH F 5 .   ? 26.411 21.016 7.441  1.00 12.00  ? 615  HOH A O     1 
HETATM 2965 O O     . HOH F 5 .   ? 12.218 32.162 29.918 1.00 13.89  ? 616  HOH A O     1 
HETATM 2966 O O     . HOH F 5 .   ? 25.587 38.271 28.430 1.00 26.68  ? 617  HOH A O     1 
HETATM 2967 O O     . HOH F 5 .   ? 41.278 20.053 7.546  1.00 22.14  ? 618  HOH A O     1 
HETATM 2968 O O     . HOH F 5 .   ? 10.455 26.329 44.788 1.00 28.10  ? 619  HOH A O     1 
HETATM 2969 O O     . HOH F 5 .   ? 19.179 33.769 41.810 1.00 19.60  ? 620  HOH A O     1 
HETATM 2970 O O     . HOH F 5 .   ? 29.428 15.739 -1.130 1.00 36.54  ? 621  HOH A O     1 
HETATM 2971 O O     . HOH F 5 .   ? 25.401 -0.950 14.480 1.00 33.59  ? 622  HOH A O     1 
HETATM 2972 O O     . HOH F 5 .   ? 0.929  9.477  19.971 1.00 31.59  ? 623  HOH A O     1 
HETATM 2973 O O     . HOH F 5 .   ? 20.519 -1.267 30.522 1.00 16.96  ? 624  HOH A O     1 
HETATM 2974 O O     . HOH F 5 .   ? 29.525 45.011 14.190 1.00 23.57  ? 625  HOH A O     1 
HETATM 2975 O O     . HOH F 5 .   ? 34.667 42.668 11.924 1.00 20.74  ? 626  HOH A O     1 
HETATM 2976 O O     . HOH F 5 .   ? 15.273 43.989 14.419 1.00 39.15  ? 627  HOH A O     1 
HETATM 2977 O O     . HOH F 5 .   ? 30.820 25.703 46.156 1.00 44.72  ? 628  HOH A O     1 
HETATM 2978 O O     . HOH F 5 .   ? 21.918 11.735 -0.757 1.00 23.56  ? 629  HOH A O     1 
HETATM 2979 O O     . HOH F 5 .   ? -0.021 12.295 39.798 1.00 29.67  ? 630  HOH A O     1 
HETATM 2980 O O     . HOH F 5 .   ? 21.425 21.816 45.156 1.00 36.37  ? 631  HOH A O     1 
HETATM 2981 O O     . HOH F 5 .   ? 12.114 1.169  15.730 1.00 19.23  ? 632  HOH A O     1 
HETATM 2982 O O     . HOH F 5 .   ? 3.726  7.630  26.737 1.00 26.44  ? 633  HOH A O     1 
HETATM 2983 O O     . HOH F 5 .   ? 35.907 37.527 18.201 1.00 24.25  ? 634  HOH A O     1 
HETATM 2984 O O     . HOH F 5 .   ? 34.843 1.720  6.088  1.00 40.30  ? 635  HOH A O     1 
HETATM 2985 O O     . HOH F 5 .   ? 22.135 33.915 17.696 1.00 11.41  ? 636  HOH A O     1 
HETATM 2986 O O     . HOH F 5 .   ? 11.677 38.075 41.098 1.00 34.74  ? 637  HOH A O     1 
HETATM 2987 O O     . HOH F 5 .   ? 24.897 18.493 -3.577 1.00 36.08  ? 638  HOH A O     1 
HETATM 2988 O O     . HOH F 5 .   ? 25.943 39.894 27.298 1.00 21.49  ? 639  HOH A O     1 
HETATM 2989 O O     . HOH F 5 .   ? 15.704 7.348  40.775 1.00 34.20  ? 640  HOH A O     1 
HETATM 2990 O O     . HOH F 5 .   ? 31.956 33.806 9.780  1.00 14.40  ? 641  HOH A O     1 
HETATM 2991 O O     . HOH F 5 .   ? 26.623 27.138 34.590 1.00 18.17  ? 642  HOH A O     1 
HETATM 2992 O O     . HOH F 5 .   ? 44.644 24.535 12.182 1.00 12.81  ? 643  HOH A O     1 
HETATM 2993 O O     . HOH F 5 .   ? 0.989  6.769  16.968 1.00 32.18  ? 644  HOH A O     1 
HETATM 2994 O O     . HOH F 5 .   ? 18.195 5.649  40.794 1.00 35.13  ? 645  HOH A O     1 
HETATM 2995 O O     . HOH F 5 .   ? 20.338 21.000 35.947 1.00 11.32  ? 646  HOH A O     1 
HETATM 2996 O O     . HOH F 5 .   ? 3.419  25.268 29.718 1.00 32.29  ? 647  HOH A O     1 
HETATM 2997 O O     . HOH F 5 .   ? 20.180 9.945  -0.427 1.00 32.84  ? 648  HOH A O     1 
HETATM 2998 O O     . HOH F 5 .   ? 12.171 27.694 2.084  1.00 22.42  ? 649  HOH A O     1 
HETATM 2999 O O     . HOH F 5 .   ? 6.771  4.274  33.572 1.00 44.54  ? 650  HOH A O     1 
HETATM 3000 O O     . HOH F 5 .   ? 26.805 43.752 37.107 1.00 37.70  ? 651  HOH A O     1 
HETATM 3001 O O     . HOH F 5 .   ? 30.332 24.964 5.568  1.00 13.09  ? 652  HOH A O     1 
HETATM 3002 O O     . HOH F 5 .   ? 14.296 40.555 12.792 1.00 34.50  ? 653  HOH A O     1 
HETATM 3003 O O     . HOH F 5 .   ? 43.622 27.304 5.918  1.00 31.39  ? 654  HOH A O     1 
HETATM 3004 O O     . HOH F 5 .   ? 12.373 12.287 30.571 1.00 12.76  ? 655  HOH A O     1 
HETATM 3005 O O     . HOH F 5 .   ? 8.498  36.316 6.647  1.00 20.87  ? 656  HOH A O     1 
HETATM 3006 O O     . HOH F 5 .   ? 34.099 21.392 16.409 1.00 11.80  ? 657  HOH A O     1 
HETATM 3007 O O     . HOH F 5 .   ? 5.541  21.989 43.556 1.00 35.94  ? 658  HOH A O     1 
HETATM 3008 O O     . HOH F 5 .   ? 21.916 2.647  39.339 1.00 34.09  ? 659  HOH A O     1 
HETATM 3009 O O     . HOH F 5 .   ? -1.962 19.128 15.085 1.00 41.40  ? 660  HOH A O     1 
HETATM 3010 O O     . HOH F 5 .   ? 12.464 39.384 35.176 1.00 33.17  ? 661  HOH A O     1 
HETATM 3011 O O     . HOH F 5 .   ? 23.913 25.850 15.250 1.00 9.53   ? 662  HOH A O     1 
HETATM 3012 O O     . HOH F 5 .   ? 20.676 38.754 6.638  1.00 24.35  ? 663  HOH A O     1 
HETATM 3013 O O     . HOH F 5 .   ? 18.513 26.025 39.571 1.00 11.46  ? 664  HOH A O     1 
HETATM 3014 O O     . HOH F 5 .   ? 4.215  27.654 23.086 1.00 31.01  ? 665  HOH A O     1 
HETATM 3015 O O     . HOH F 5 .   ? 44.752 28.527 9.778  1.00 15.04  ? 666  HOH A O     1 
HETATM 3016 O O     . HOH F 5 .   ? 27.738 26.018 32.413 1.00 26.76  ? 667  HOH A O     1 
HETATM 3017 O O     . HOH F 5 .   ? 36.526 30.604 -0.289 1.00 32.04  ? 668  HOH A O     1 
HETATM 3018 O O     . HOH F 5 .   ? 22.497 41.897 26.896 1.00 13.87  ? 669  HOH A O     1 
HETATM 3019 O O     . HOH F 5 .   ? 24.044 -2.086 22.090 1.00 13.06  ? 670  HOH A O     1 
HETATM 3020 O O     . HOH F 5 .   ? 14.280 40.684 33.517 1.00 29.82  ? 671  HOH A O     1 
HETATM 3021 O O     . HOH F 5 .   ? 10.268 29.528 48.943 1.00 42.96  ? 672  HOH A O     1 
HETATM 3022 O O     . HOH F 5 .   ? 31.111 29.893 29.785 1.00 31.00  ? 673  HOH A O     1 
HETATM 3023 O O     . HOH F 5 .   ? 14.876 35.534 3.128  1.00 21.76  ? 674  HOH A O     1 
HETATM 3024 O O     . HOH F 5 .   ? 15.432 28.345 25.692 1.00 13.26  ? 675  HOH A O     1 
HETATM 3025 O O     . HOH F 5 .   ? 5.130  29.643 29.721 1.00 25.87  ? 676  HOH A O     1 
HETATM 3026 O O     . HOH F 5 .   ? 27.285 37.380 26.877 1.00 16.93  ? 677  HOH A O     1 
HETATM 3027 O O     . HOH F 5 .   ? 1.778  7.241  12.298 1.00 36.18  ? 678  HOH A O     1 
HETATM 3028 O O     . HOH F 5 .   ? 16.808 23.532 -1.161 1.00 14.38  ? 679  HOH A O     1 
HETATM 3029 O O     . HOH F 5 .   ? 2.497  23.883 10.730 1.00 17.98  ? 680  HOH A O     1 
HETATM 3030 O O     . HOH F 5 .   ? 8.300  23.122 6.539  1.00 20.34  ? 681  HOH A O     1 
HETATM 3031 O O     . HOH F 5 .   ? 12.239 -2.602 13.014 1.00 41.72  ? 682  HOH A O     1 
HETATM 3032 O O     . HOH F 5 .   ? 21.811 15.852 -2.066 1.00 26.09  ? 683  HOH A O     1 
HETATM 3033 O O     . HOH F 5 .   ? 10.210 23.698 3.740  1.00 33.67  ? 684  HOH A O     1 
HETATM 3034 O O     . HOH F 5 .   ? 28.895 4.635  9.289  1.00 24.20  ? 685  HOH A O     1 
HETATM 3035 O O     . HOH F 5 .   ? 25.532 11.253 33.845 1.00 22.08  ? 686  HOH A O     1 
HETATM 3036 O O     . HOH F 5 .   ? 4.635  5.725  20.718 1.00 21.96  ? 687  HOH A O     1 
HETATM 3037 O O     . HOH F 5 .   ? 21.414 2.857  11.124 1.00 28.12  ? 688  HOH A O     1 
HETATM 3038 O O     . HOH F 5 .   ? 33.399 36.313 6.963  1.00 24.19  ? 689  HOH A O     1 
HETATM 3039 O O     . HOH F 5 .   ? 19.630 5.685  5.148  1.00 39.71  ? 690  HOH A O     1 
HETATM 3040 O O     . HOH F 5 .   ? 17.567 -1.435 21.721 1.00 25.89  ? 691  HOH A O     1 
HETATM 3041 O O     . HOH F 5 .   ? 1.646  26.609 13.639 1.00 33.09  ? 692  HOH A O     1 
HETATM 3042 O O     . HOH F 5 .   ? 30.602 32.440 14.412 1.00 10.72  ? 693  HOH A O     1 
HETATM 3043 O O     . HOH F 5 .   ? 10.026 35.547 28.182 1.00 25.18  ? 694  HOH A O     1 
HETATM 3044 O O     . HOH F 5 .   ? 3.107  28.825 20.513 1.00 32.85  ? 695  HOH A O     1 
HETATM 3045 O O     . HOH F 5 .   ? 26.673 11.239 26.634 1.00 19.07  ? 696  HOH A O     1 
HETATM 3046 O O     . HOH F 5 .   ? 2.500  13.222 24.445 1.00 15.52  ? 697  HOH A O     1 
HETATM 3047 O O     . HOH F 5 .   ? 5.356  33.354 8.510  1.00 35.54  ? 698  HOH A O     1 
HETATM 3048 O O     . HOH F 5 .   ? 43.522 15.299 13.956 1.00 43.47  ? 699  HOH A O     1 
HETATM 3049 O O     . HOH F 5 .   ? 29.831 10.263 32.581 1.00 45.14  ? 700  HOH A O     1 
HETATM 3050 O O     . HOH F 5 .   ? 10.245 37.482 24.145 1.00 33.05  ? 701  HOH A O     1 
HETATM 3051 O O     . HOH F 5 .   ? 18.355 42.599 12.412 1.00 34.05  ? 702  HOH A O     1 
HETATM 3052 O O     . HOH F 5 .   ? 30.001 40.017 8.311  1.00 27.11  ? 703  HOH A O     1 
HETATM 3053 O O     . HOH F 5 .   ? 0.215  17.317 26.136 1.00 16.78  ? 704  HOH A O     1 
HETATM 3054 O O     . HOH F 5 .   ? 7.602  23.559 43.981 1.00 23.17  ? 705  HOH A O     1 
HETATM 3055 O O     . HOH F 5 .   ? 6.903  36.667 40.320 1.00 39.12  ? 706  HOH A O     1 
HETATM 3056 O O     . HOH F 5 .   ? 14.194 35.630 28.851 1.00 18.29  ? 707  HOH A O     1 
HETATM 3057 O O     . HOH F 5 .   ? 3.616  -2.943 22.339 1.00 44.73  ? 708  HOH A O     1 
HETATM 3058 O O     . HOH F 5 .   ? 8.104  40.236 32.888 1.00 33.83  ? 709  HOH A O     1 
HETATM 3059 O O     . HOH F 5 .   ? 33.246 9.725  -0.643 1.00 35.78  ? 710  HOH A O     1 
HETATM 3060 O O     . HOH F 5 .   ? 2.312  11.829 12.653 1.00 31.31  ? 711  HOH A O     1 
HETATM 3061 O O     . HOH F 5 .   ? 17.841 -0.500 24.548 1.00 24.42  ? 712  HOH A O     1 
HETATM 3062 O O     . HOH F 5 .   ? 13.156 15.533 47.544 1.00 44.86  ? 713  HOH A O     1 
HETATM 3063 O O     . HOH F 5 .   ? 41.280 29.554 20.714 1.00 25.19  ? 714  HOH A O     1 
HETATM 3064 O O     . HOH F 5 .   ? 16.589 41.655 11.609 1.00 29.58  ? 715  HOH A O     1 
HETATM 3065 O O     . HOH F 5 .   ? 2.590  18.948 10.309 1.00 26.08  ? 716  HOH A O     1 
HETATM 3066 O O     . HOH F 5 .   ? 15.455 20.226 27.781 1.00 10.57  ? 717  HOH A O     1 
HETATM 3067 O O     . HOH F 5 .   ? 3.170  9.739  18.524 1.00 19.54  ? 718  HOH A O     1 
HETATM 3068 O O     . HOH F 5 .   ? 16.798 15.647 46.710 1.00 23.28  ? 719  HOH A O     1 
HETATM 3069 O O     . HOH F 5 .   ? -0.739 16.439 17.017 1.00 24.32  ? 720  HOH A O     1 
HETATM 3070 O O     . HOH F 5 .   ? 22.138 3.839  15.140 1.00 13.68  ? 721  HOH A O     1 
HETATM 3071 O O     . HOH F 5 .   ? 0.798  24.918 26.541 1.00 28.52  ? 722  HOH A O     1 
HETATM 3072 O O     . HOH F 5 .   ? 32.639 4.563  26.931 1.00 42.20  ? 723  HOH A O     1 
HETATM 3073 O O     . HOH F 5 .   ? 2.769  32.403 22.141 1.00 43.41  ? 724  HOH A O     1 
HETATM 3074 O O     . HOH F 5 .   ? -3.751 17.611 30.791 1.00 14.05  ? 725  HOH A O     1 
HETATM 3075 O O     . HOH F 5 .   ? 27.908 34.920 41.261 1.00 42.14  ? 726  HOH A O     1 
HETATM 3076 O O     . HOH F 5 .   ? 17.730 29.569 26.817 1.00 10.62  ? 727  HOH A O     1 
HETATM 3077 O O     . HOH F 5 .   ? 22.152 -3.409 15.816 1.00 27.95  ? 728  HOH A O     1 
HETATM 3078 O O     . HOH F 5 .   ? 15.233 37.105 10.115 1.00 20.98  ? 729  HOH A O     1 
HETATM 3079 O O     . HOH F 5 .   ? 30.925 35.035 25.125 1.00 15.15  ? 730  HOH A O     1 
HETATM 3080 O O     . HOH F 5 .   ? 30.450 15.658 32.062 1.00 30.81  ? 731  HOH A O     1 
HETATM 3081 O O     . HOH F 5 .   ? 5.407  34.514 35.512 1.00 37.15  ? 732  HOH A O     1 
HETATM 3082 O O     . HOH F 5 .   ? 39.067 30.863 22.553 1.00 25.71  ? 733  HOH A O     1 
HETATM 3083 O O     . HOH F 5 .   ? 1.979  14.708 29.158 1.00 21.11  ? 734  HOH A O     1 
HETATM 3084 O O     . HOH F 5 .   ? 22.581 40.665 17.068 1.00 13.26  ? 735  HOH A O     1 
HETATM 3085 O O     . HOH F 5 .   ? 32.609 30.517 27.693 1.00 33.44  ? 736  HOH A O     1 
HETATM 3086 O O     . HOH F 5 .   ? 24.052 23.041 4.950  1.00 27.01  ? 737  HOH A O     1 
HETATM 3087 O O     . HOH F 5 .   ? 16.152 35.437 26.929 1.00 11.35  ? 738  HOH A O     1 
HETATM 3088 O O     . HOH F 5 .   ? 39.519 17.171 -1.882 1.00 38.14  ? 739  HOH A O     1 
HETATM 3089 O O     . HOH F 5 .   ? 17.542 18.585 28.635 1.00 10.71  ? 740  HOH A O     1 
HETATM 3090 O O     . HOH F 5 .   ? 31.928 14.968 -2.531 1.00 51.63  ? 741  HOH A O     1 
HETATM 3091 O O     . HOH F 5 .   ? 14.237 -1.085 12.187 1.00 36.26  ? 742  HOH A O     1 
HETATM 3092 O O     . HOH F 5 .   ? 24.986 -1.012 33.741 1.00 27.71  ? 743  HOH A O     1 
HETATM 3093 O O     . HOH F 5 .   ? 40.435 18.671 12.284 1.00 29.91  ? 744  HOH A O     1 
HETATM 3094 O O     . HOH F 5 .   ? 6.693  22.647 48.355 1.00 47.57  ? 745  HOH A O     1 
HETATM 3095 O O     . HOH F 5 .   ? -1.221 28.221 14.499 1.00 36.83  ? 746  HOH A O     1 
HETATM 3096 O O     . HOH F 5 .   ? 5.974  -0.163 19.930 1.00 27.40  ? 747  HOH A O     1 
HETATM 3097 O O     . HOH F 5 .   ? 25.363 17.119 6.387  1.00 11.09  ? 748  HOH A O     1 
HETATM 3098 O O     . HOH F 5 .   ? 9.897  11.655 33.290 1.00 10.96  ? 749  HOH A O     1 
HETATM 3099 O O     . HOH F 5 .   ? 11.986 13.678 6.463  1.00 34.88  ? 750  HOH A O     1 
HETATM 3100 O O     . HOH F 5 .   ? 33.948 0.200  15.961 1.00 47.25  ? 751  HOH A O     1 
HETATM 3101 O O     . HOH F 5 .   ? 10.542 16.779 42.799 1.00 23.15  ? 752  HOH A O     1 
HETATM 3102 O O     . HOH F 5 .   ? 5.233  9.571  12.065 1.00 18.60  ? 753  HOH A O     1 
HETATM 3103 O O     . HOH F 5 .   ? 36.330 8.664  15.947 1.00 26.67  ? 754  HOH A O     1 
HETATM 3104 O O     . HOH F 5 .   ? 10.963 9.818  5.412  1.00 32.36  ? 755  HOH A O     1 
HETATM 3105 O O     . HOH F 5 .   ? 28.182 26.956 49.469 1.00 38.37  ? 756  HOH A O     1 
HETATM 3106 O O     . HOH F 5 .   ? 14.602 46.415 22.035 1.00 27.41  ? 757  HOH A O     1 
HETATM 3107 O O     . HOH F 5 .   ? -1.327 12.675 14.351 1.00 52.34  ? 758  HOH A O     1 
HETATM 3108 O O     . HOH F 5 .   ? 4.196  23.799 40.841 1.00 27.66  ? 759  HOH A O     1 
HETATM 3109 O O     . HOH F 5 .   ? 12.098 27.332 33.476 1.00 11.56  ? 760  HOH A O     1 
HETATM 3110 O O     . HOH F 5 .   ? 3.574  28.153 28.136 1.00 31.00  ? 761  HOH A O     1 
HETATM 3111 O O     . HOH F 5 .   ? 27.522 0.318  11.997 1.00 36.56  ? 762  HOH A O     1 
HETATM 3112 O O     . HOH F 5 .   ? 25.041 26.342 30.491 1.00 29.63  ? 763  HOH A O     1 
HETATM 3113 O O     . HOH F 5 .   ? 7.283  6.827  41.779 1.00 34.23  ? 764  HOH A O     1 
HETATM 3114 O O     . HOH F 5 .   ? 16.772 34.413 40.242 1.00 20.07  ? 765  HOH A O     1 
HETATM 3115 O O     . HOH F 5 .   ? 1.800  35.009 18.088 1.00 28.21  ? 766  HOH A O     1 
HETATM 3116 O O     . HOH F 5 .   ? 16.990 38.039 26.495 1.00 13.01  ? 767  HOH A O     1 
HETATM 3117 O O     . HOH F 5 .   ? 0.216  4.765  15.441 1.00 32.35  ? 768  HOH A O     1 
HETATM 3118 O O     . HOH F 5 .   ? 10.776 5.246  8.287  1.00 41.66  ? 769  HOH A O     1 
HETATM 3119 O O     . HOH F 5 .   ? 18.216 0.178  30.287 1.00 19.34  ? 770  HOH A O     1 
HETATM 3120 O O     . HOH F 5 .   ? 24.737 25.869 46.319 1.00 21.98  ? 771  HOH A O     1 
HETATM 3121 O O     . HOH F 5 .   ? 20.660 18.832 41.702 1.00 24.19  ? 772  HOH A O     1 
HETATM 3122 O O     . HOH F 5 .   ? 6.835  14.095 43.497 1.00 33.21  ? 773  HOH A O     1 
HETATM 3123 O O     . HOH F 5 .   ? 12.930 18.804 45.495 1.00 23.90  ? 774  HOH A O     1 
HETATM 3124 O O     . HOH F 5 .   ? 39.100 35.156 2.806  1.00 40.85  ? 775  HOH A O     1 
HETATM 3125 O O     . HOH F 5 .   ? 24.774 30.452 31.340 1.00 13.82  ? 776  HOH A O     1 
HETATM 3126 O O     . HOH F 5 .   ? 21.791 6.286  2.850  1.00 24.28  ? 777  HOH A O     1 
HETATM 3127 O O     . HOH F 5 .   ? 40.566 31.796 6.211  1.00 26.40  ? 778  HOH A O     1 
HETATM 3128 O O     . HOH F 5 .   ? 12.135 0.996  35.193 1.00 17.67  ? 779  HOH A O     1 
HETATM 3129 O O     . HOH F 5 .   ? 30.505 37.785 37.538 1.00 24.93  ? 780  HOH A O     1 
HETATM 3130 O O     . HOH F 5 .   ? 16.404 15.987 0.024  1.00 23.71  ? 781  HOH A O     1 
HETATM 3131 O O     . HOH F 5 .   ? 10.189 37.715 21.273 1.00 29.78  ? 782  HOH A O     1 
HETATM 3132 O O     . HOH F 5 .   ? 43.639 22.210 10.852 1.00 20.85  ? 783  HOH A O     1 
HETATM 3133 O O     . HOH F 5 .   ? 22.302 36.189 40.713 1.00 18.71  ? 784  HOH A O     1 
HETATM 3134 O O     . HOH F 5 .   ? 19.294 17.000 43.185 1.00 35.29  ? 785  HOH A O     1 
HETATM 3135 O O     . HOH F 5 .   ? 2.312  35.593 10.476 1.00 35.31  ? 786  HOH A O     1 
HETATM 3136 O O     . HOH F 5 .   ? 41.026 31.793 -1.062 1.00 38.19  ? 787  HOH A O     1 
HETATM 3137 O O     . HOH F 5 .   ? 35.331 13.919 22.987 1.00 40.22  ? 788  HOH A O     1 
HETATM 3138 O O     . HOH F 5 .   ? 29.676 27.923 35.812 1.00 23.44  ? 789  HOH A O     1 
HETATM 3139 O O     . HOH F 5 .   ? 27.747 42.108 23.507 1.00 25.46  ? 790  HOH A O     1 
HETATM 3140 O O     . HOH F 5 .   ? 31.831 24.687 3.258  1.00 15.07  ? 791  HOH A O     1 
HETATM 3141 O O     . HOH F 5 .   ? 5.022  18.123 8.827  1.00 21.83  ? 792  HOH A O     1 
HETATM 3142 O O     . HOH F 5 .   ? 35.923 20.108 18.192 1.00 21.46  ? 793  HOH A O     1 
HETATM 3143 O O     . HOH F 5 .   ? 24.514 17.656 31.581 1.00 34.93  ? 794  HOH A O     1 
HETATM 3144 O O     . HOH F 5 .   ? 20.974 41.719 12.664 1.00 16.89  ? 795  HOH A O     1 
HETATM 3145 O O     . HOH F 5 .   ? 26.306 -3.280 21.023 1.00 14.98  ? 796  HOH A O     1 
HETATM 3146 O O     . HOH F 5 .   ? 40.490 34.920 15.180 1.00 39.61  ? 797  HOH A O     1 
HETATM 3147 O O     . HOH F 5 .   ? 0.448  15.633 19.009 1.00 41.93  ? 798  HOH A O     1 
HETATM 3148 O O     . HOH F 5 .   ? 4.848  4.760  39.423 1.00 35.18  ? 799  HOH A O     1 
HETATM 3149 O O     . HOH F 5 .   ? 14.960 42.972 18.590 1.00 32.61  ? 800  HOH A O     1 
HETATM 3150 O O     . HOH F 5 .   ? 32.433 32.963 26.755 1.00 23.95  ? 801  HOH A O     1 
HETATM 3151 O O     . HOH F 5 .   ? 23.228 10.227 40.390 1.00 30.68  ? 802  HOH A O     1 
HETATM 3152 O O     . HOH F 5 .   ? 21.391 0.773  37.512 1.00 31.69  ? 803  HOH A O     1 
HETATM 3153 O O     . HOH F 5 .   ? 15.668 31.021 44.820 1.00 19.17  ? 804  HOH A O     1 
HETATM 3154 O O     . HOH F 5 .   ? 1.426  26.195 16.635 1.00 24.09  ? 805  HOH A O     1 
HETATM 3155 O O     . HOH F 5 .   ? 30.205 -2.571 17.719 1.00 22.89  ? 806  HOH A O     1 
HETATM 3156 O O     . HOH F 5 .   ? 9.227  4.407  40.737 1.00 32.42  ? 807  HOH A O     1 
HETATM 3157 O O     . HOH F 5 .   ? 14.797 1.630  37.831 1.00 33.93  ? 808  HOH A O     1 
HETATM 3158 O O     . HOH F 5 .   ? 8.062  32.675 41.736 1.00 28.19  ? 809  HOH A O     1 
HETATM 3159 O O     . HOH F 5 .   ? 38.643 21.192 22.764 1.00 48.14  ? 810  HOH A O     1 
HETATM 3160 O O     . HOH F 5 .   ? 27.340 24.474 -1.456 1.00 24.91  ? 811  HOH A O     1 
HETATM 3161 O O     . HOH F 5 .   ? 3.843  34.011 11.030 1.00 37.06  ? 812  HOH A O     1 
HETATM 3162 O O     . HOH F 5 .   ? 29.451 31.980 30.081 1.00 23.72  ? 813  HOH A O     1 
HETATM 3163 O O     . HOH F 5 .   ? 7.434  9.998  9.241  1.00 26.85  ? 814  HOH A O     1 
HETATM 3164 O O     . HOH F 5 .   ? 13.316 8.984  8.925  1.00 24.12  ? 815  HOH A O     1 
HETATM 3165 O O     . HOH F 5 .   ? 9.313  7.243  8.465  1.00 34.65  ? 816  HOH A O     1 
HETATM 3166 O O     . HOH F 5 .   ? 17.833 35.735 6.215  1.00 20.74  ? 817  HOH A O     1 
HETATM 3167 O O     . HOH F 5 .   ? 40.844 9.156  9.949  1.00 40.40  ? 818  HOH A O     1 
HETATM 3168 O O     . HOH F 5 .   ? 20.356 20.141 -2.461 1.00 40.15  ? 819  HOH A O     1 
HETATM 3169 O O     . HOH F 5 .   ? 16.189 3.937  39.153 1.00 36.64  ? 820  HOH A O     1 
HETATM 3170 O O     . HOH F 5 .   ? 3.414  37.400 17.283 1.00 23.73  ? 821  HOH A O     1 
HETATM 3171 O O     . HOH F 5 .   ? 32.984 -0.485 9.259  1.00 44.22  ? 822  HOH A O     1 
HETATM 3172 O O     . HOH F 5 .   ? 30.464 18.119 24.853 1.00 36.64  ? 823  HOH A O     1 
HETATM 3173 O O     . HOH F 5 .   ? 35.529 12.716 19.553 1.00 31.94  ? 824  HOH A O     1 
HETATM 3174 O O     . HOH F 5 .   ? 6.301  29.455 35.243 1.00 29.37  ? 825  HOH A O     1 
HETATM 3175 O O     . HOH F 5 .   ? 29.957 42.645 29.341 1.00 27.74  ? 826  HOH A O     1 
HETATM 3176 O O     . HOH F 5 .   ? 36.129 35.724 3.726  1.00 24.60  ? 827  HOH A O     1 
HETATM 3177 O O     . HOH F 5 .   ? 37.302 39.345 22.093 1.00 36.06  ? 828  HOH A O     1 
HETATM 3178 O O     . HOH F 5 .   ? 12.862 24.880 49.139 1.00 26.39  ? 829  HOH A O     1 
HETATM 3179 O O     . HOH F 5 .   ? 31.865 6.454  24.450 1.00 24.38  ? 830  HOH A O     1 
HETATM 3180 O O     . HOH F 5 .   ? 11.951 -3.217 28.787 1.00 30.70  ? 831  HOH A O     1 
HETATM 3181 O O     . HOH F 5 .   ? 12.249 -4.545 16.733 1.00 34.30  ? 832  HOH A O     1 
HETATM 3182 O O     . HOH F 5 .   ? 30.685 8.644  24.984 1.00 41.17  ? 833  HOH A O     1 
HETATM 3183 O O     . HOH F 5 .   ? 17.366 0.945  11.748 1.00 38.33  ? 834  HOH A O     1 
HETATM 3184 O O     . HOH F 5 .   ? 11.046 -0.771 30.307 1.00 37.37  ? 835  HOH A O     1 
HETATM 3185 O O     . HOH F 5 .   ? 27.745 3.845  32.151 1.00 32.23  ? 836  HOH A O     1 
HETATM 3186 O O     . HOH F 5 .   ? 2.130  30.754 17.642 1.00 29.50  ? 837  HOH A O     1 
HETATM 3187 O O     . HOH F 5 .   ? -0.214 11.689 20.539 1.00 37.59  ? 838  HOH A O     1 
HETATM 3188 O O     . HOH F 5 .   ? 28.216 20.776 44.364 1.00 30.70  ? 839  HOH A O     1 
HETATM 3189 O O     . HOH F 5 .   ? 3.971  4.985  25.797 1.00 43.14  ? 840  HOH A O     1 
HETATM 3190 O O     . HOH F 5 .   ? 25.600 4.659  4.893  1.00 31.65  ? 841  HOH A O     1 
HETATM 3191 O O     . HOH F 5 .   ? 28.468 -2.675 22.359 1.00 22.63  ? 842  HOH A O     1 
HETATM 3192 O O     . HOH F 5 .   ? 13.457 42.640 16.921 1.00 40.07  ? 843  HOH A O     1 
HETATM 3193 O O     . HOH F 5 .   ? 38.001 19.275 21.500 1.00 44.93  ? 844  HOH A O     1 
HETATM 3194 O O     . HOH F 5 .   ? 30.516 -0.777 21.991 1.00 38.75  ? 845  HOH A O     1 
HETATM 3195 O O     . HOH F 5 .   ? 8.026  1.807  30.168 1.00 31.84  ? 846  HOH A O     1 
HETATM 3196 O O     . HOH F 5 .   ? 33.725 15.986 23.670 1.00 34.50  ? 847  HOH A O     1 
HETATM 3197 O O     . HOH F 5 .   ? 1.958  9.294  15.926 1.00 26.86  ? 848  HOH A O     1 
HETATM 3198 O O     . HOH F 5 .   ? 18.115 5.038  8.892  1.00 42.40  ? 849  HOH A O     1 
HETATM 3199 O O     . HOH F 5 .   ? 42.743 29.968 6.448  1.00 31.83  ? 850  HOH A O     1 
HETATM 3200 O O     . HOH F 5 .   ? 28.101 41.805 7.635  1.00 45.75  ? 851  HOH A O     1 
HETATM 3201 O O     . HOH F 5 .   ? -1.538 25.710 31.456 1.00 38.31  ? 852  HOH A O     1 
HETATM 3202 O O     . HOH F 5 .   ? 7.765  4.295  23.963 1.00 35.29  ? 853  HOH A O     1 
HETATM 3203 O O     . HOH F 5 .   ? -0.759 10.381 15.705 1.00 42.19  ? 854  HOH A O     1 
HETATM 3204 O O     . HOH F 5 .   ? 25.278 14.105 -3.729 1.00 42.86  ? 855  HOH A O     1 
HETATM 3205 O O     . HOH F 5 .   ? 23.353 28.276 -4.062 1.00 23.32  ? 856  HOH A O     1 
HETATM 3206 O O     . HOH F 5 .   ? 39.529 33.459 11.260 1.00 26.77  ? 857  HOH A O     1 
HETATM 3207 O O     . HOH F 5 .   ? 42.232 33.518 7.658  1.00 39.38  ? 858  HOH A O     1 
HETATM 3208 O O     . HOH F 5 .   ? 2.847  29.215 26.305 1.00 43.60  ? 859  HOH A O     1 
HETATM 3209 O O     . HOH F 5 .   ? 4.877  18.771 41.922 1.00 36.72  ? 860  HOH A O     1 
HETATM 3210 O O     . HOH F 5 .   ? 23.062 -2.734 34.121 1.00 20.75  ? 861  HOH A O     1 
HETATM 3211 O O     . HOH F 5 .   ? 15.885 5.547  10.141 1.00 32.34  ? 862  HOH A O     1 
HETATM 3212 O O     . HOH F 5 .   ? 7.176  6.202  28.611 1.00 30.69  ? 863  HOH A O     1 
HETATM 3213 O O     . HOH F 5 .   ? 12.045 38.399 31.387 1.00 43.73  ? 864  HOH A O     1 
HETATM 3214 O O     . HOH F 5 .   ? 9.245  2.268  9.391  1.00 45.57  ? 865  HOH A O     1 
HETATM 3215 O O     . HOH F 5 .   ? 4.978  7.651  28.752 1.00 33.99  ? 866  HOH A O     1 
HETATM 3216 O O     . HOH F 5 .   ? 36.726 20.630 25.573 1.00 46.95  ? 867  HOH A O     1 
HETATM 3217 O O     . HOH F 5 .   ? 1.359  26.469 39.228 1.00 46.59  ? 868  HOH A O     1 
HETATM 3218 O O     . HOH F 5 .   ? 16.296 33.115 -0.638 1.00 27.95  ? 869  HOH A O     1 
HETATM 3219 O O     . HOH F 5 .   ? 10.062 1.678  12.520 1.00 33.09  ? 870  HOH A O     1 
HETATM 3220 O O     . HOH F 5 .   ? 16.823 44.631 16.821 1.00 36.99  ? 871  HOH A O     1 
HETATM 3221 O O     . HOH F 5 .   ? 20.212 10.664 28.506 1.00 27.96  ? 872  HOH A O     1 
HETATM 3222 O O     . HOH F 5 .   ? -0.453 26.918 10.258 1.00 51.57  ? 873  HOH A O     1 
HETATM 3223 O O     . HOH F 5 .   ? 39.718 33.080 -2.215 1.00 48.45  ? 874  HOH A O     1 
HETATM 3224 O O     . HOH F 5 .   ? 11.918 23.189 1.442  1.00 32.74  ? 875  HOH A O     1 
HETATM 3225 O O     . HOH F 5 .   ? 10.359 40.863 34.966 1.00 43.36  ? 876  HOH A O     1 
HETATM 3226 O O     . HOH F 5 .   ? 20.310 36.186 42.576 1.00 36.73  ? 877  HOH A O     1 
HETATM 3227 O O     . HOH F 5 .   ? 31.901 5.114  19.019 1.00 29.82  ? 878  HOH A O     1 
HETATM 3228 O O     . HOH F 5 .   ? 15.170 40.020 25.635 1.00 24.91  ? 879  HOH A O     1 
HETATM 3229 O O     . HOH F 5 .   ? 29.839 -4.225 20.035 1.00 34.56  ? 880  HOH A O     1 
HETATM 3230 O O     . HOH F 5 .   ? 34.641 5.222  26.694 1.00 44.30  ? 881  HOH A O     1 
HETATM 3231 O O     . HOH F 5 .   ? 15.167 7.255  8.547  1.00 30.18  ? 882  HOH A O     1 
HETATM 3232 O O     . HOH F 5 .   ? 16.773 -0.712 28.346 1.00 26.96  ? 883  HOH A O     1 
HETATM 3233 O O     . HOH F 5 .   ? 3.967  6.970  18.460 1.00 32.13  ? 884  HOH A O     1 
HETATM 3234 O O     . HOH F 5 .   ? 8.915  -0.474 31.172 1.00 30.90  ? 885  HOH A O     1 
HETATM 3235 O O     . HOH F 5 .   ? 2.575  24.990 8.147  1.00 25.87  ? 886  HOH A O     1 
HETATM 3236 O O     . HOH F 5 .   ? 23.142 0.435  13.521 1.00 40.66  ? 887  HOH A O     1 
HETATM 3237 O O     . HOH F 5 .   ? 41.535 34.539 9.859  1.00 41.26  ? 888  HOH A O     1 
HETATM 3238 O O     . HOH F 5 .   ? 22.927 13.114 -2.748 1.00 44.36  ? 889  HOH A O     1 
HETATM 3239 O O     . HOH F 5 .   ? 38.352 36.493 12.707 1.00 35.36  ? 890  HOH A O     1 
HETATM 3240 O O     . HOH F 5 .   ? 13.425 7.960  43.234 1.00 41.29  ? 891  HOH A O     1 
HETATM 3241 O O     . HOH F 5 .   ? 4.624  28.502 33.097 1.00 32.49  ? 892  HOH A O     1 
HETATM 3242 O O     . HOH F 5 .   ? 4.643  38.615 19.491 1.00 43.24  ? 893  HOH A O     1 
HETATM 3243 O O     . HOH F 5 .   ? 34.657 18.474 24.538 1.00 46.88  ? 894  HOH A O     1 
HETATM 3244 O O     . HOH F 5 .   ? 32.618 -1.675 17.618 1.00 31.07  ? 895  HOH A O     1 
HETATM 3245 O O     . HOH F 5 .   ? 7.977  1.868  26.968 1.00 44.42  ? 896  HOH A O     1 
HETATM 3246 O O     . HOH F 5 .   ? 25.658 9.387  40.423 1.00 43.06  ? 897  HOH A O     1 
HETATM 3247 O O     . HOH F 5 .   ? 6.862  21.002 5.331  1.00 34.85  ? 898  HOH A O     1 
HETATM 3248 O O     . HOH F 5 .   ? 29.589 17.919 -0.953 1.00 40.17  ? 899  HOH A O     1 
HETATM 3249 O O     . HOH F 5 .   ? 35.935 3.477  26.544 1.00 46.11  ? 900  HOH A O     1 
HETATM 3250 O O     . HOH F 5 .   ? 0.824  13.449 22.336 1.00 30.06  ? 901  HOH A O     1 
HETATM 3251 O O     . HOH F 5 .   ? 32.416 36.758 4.442  1.00 36.44  ? 902  HOH A O     1 
HETATM 3252 O O     . HOH F 5 .   ? 30.412 29.561 33.702 1.00 39.10  ? 903  HOH A O     1 
HETATM 3253 O O     . HOH F 5 .   ? 26.898 41.530 39.357 1.00 44.99  ? 904  HOH A O     1 
HETATM 3254 O O     . HOH F 5 .   ? 27.288 19.389 -3.629 1.00 34.22  ? 905  HOH A O     1 
HETATM 3255 O O     . HOH F 5 .   ? 34.985 33.987 27.633 1.00 34.85  ? 906  HOH A O     1 
HETATM 3256 O O     . HOH F 5 .   ? 13.448 32.797 41.244 1.00 28.87  ? 907  HOH A O     1 
HETATM 3257 O O     . HOH F 5 .   ? 0.444  28.348 17.936 1.00 45.08  ? 908  HOH A O     1 
HETATM 3258 O O     . HOH F 5 .   ? 32.685 20.162 24.604 1.00 44.36  ? 909  HOH A O     1 
HETATM 3259 O O     . HOH F 5 .   ? 9.134  4.333  7.117  1.00 45.06  ? 910  HOH A O     1 
HETATM 3260 O O     . HOH F 5 .   ? 2.927  9.401  13.384 1.00 28.77  ? 911  HOH A O     1 
HETATM 3261 O O     . HOH F 5 .   ? 30.293 25.422 48.878 1.00 41.91  ? 912  HOH A O     1 
HETATM 3262 O O     . HOH F 5 .   ? 28.273 9.671  25.315 1.00 36.02  ? 913  HOH A O     1 
HETATM 3263 O O     . HOH F 5 .   ? 19.194 33.701 -0.998 1.00 24.04  ? 914  HOH A O     1 
HETATM 3264 O O     . HOH F 5 .   ? 3.993  29.866 24.503 1.00 30.03  ? 915  HOH A O     1 
HETATM 3265 O O     . HOH F 5 .   ? 0.698  10.146 27.452 1.00 36.99  ? 916  HOH A O     1 
HETATM 3266 O O     . HOH F 5 .   ? 9.600  -0.076 35.858 1.00 19.96  ? 917  HOH A O     1 
HETATM 3267 O O     . HOH F 5 .   ? 37.265 1.342  6.383  1.00 47.50  ? 918  HOH A O     1 
HETATM 3268 O O     . HOH F 5 .   ? 8.010  1.706  39.909 1.00 42.41  ? 919  HOH A O     1 
HETATM 3269 O O     . HOH F 5 .   ? -0.472 15.937 21.928 1.00 25.45  ? 920  HOH A O     1 
HETATM 3270 O O     . HOH F 5 .   ? 5.932  35.375 6.611  1.00 29.24  ? 921  HOH A O     1 
HETATM 3271 O O     . HOH F 5 .   ? 42.546 18.448 14.195 1.00 42.29  ? 922  HOH A O     1 
HETATM 3272 O O     . HOH F 5 .   ? 16.954 37.548 8.043  1.00 23.55  ? 923  HOH A O     1 
HETATM 3273 O O     . HOH F 5 .   ? 14.036 20.399 47.641 1.00 33.39  ? 924  HOH A O     1 
HETATM 3274 O O     . HOH F 5 .   ? 7.102  16.559 42.811 1.00 46.92  ? 925  HOH A O     1 
HETATM 3275 O O     . HOH F 5 .   ? 0.471  25.220 12.087 1.00 34.57  ? 926  HOH A O     1 
HETATM 3276 O O     . HOH F 5 .   ? 26.194 4.610  1.281  1.00 50.40  ? 927  HOH A O     1 
HETATM 3277 O O     . HOH F 5 .   ? 24.505 30.476 46.247 1.00 36.00  ? 928  HOH A O     1 
HETATM 3278 O O     . HOH F 5 .   ? 32.229 35.183 30.385 1.00 37.70  ? 929  HOH A O     1 
HETATM 3279 O O     . HOH F 5 .   ? 37.283 42.508 11.283 1.00 44.27  ? 930  HOH A O     1 
HETATM 3280 O O     . HOH F 5 .   ? 38.504 40.246 12.617 1.00 47.95  ? 931  HOH A O     1 
HETATM 3281 O O     . HOH F 5 .   ? 39.584 13.022 0.039  1.00 40.24  ? 932  HOH A O     1 
HETATM 3282 O O     . HOH F 5 .   ? 4.884  9.627  9.337  1.00 43.55  ? 933  HOH A O     1 
HETATM 3283 O O     . HOH F 5 .   ? 9.818  33.264 43.450 1.00 41.61  ? 934  HOH A O     1 
HETATM 3284 O O     . HOH F 5 .   ? 4.244  -1.890 18.518 1.00 40.51  ? 935  HOH A O     1 
HETATM 3285 O O     . HOH F 5 .   ? 27.307 30.250 30.388 1.00 22.50  ? 936  HOH A O     1 
HETATM 3286 O O     . HOH F 5 .   ? 28.177 10.693 34.626 1.00 39.09  ? 937  HOH A O     1 
HETATM 3287 O O     . HOH F 5 .   ? 8.843  6.735  44.149 1.00 43.55  ? 938  HOH A O     1 
HETATM 3288 O O     . HOH F 5 .   ? 14.717 31.312 -2.249 1.00 24.02  ? 939  HOH A O     1 
HETATM 3289 O O     . HOH F 5 .   ? 20.041 36.855 4.902  1.00 29.70  ? 940  HOH A O     1 
HETATM 3290 O O     . HOH F 5 .   ? 10.916 8.393  3.276  1.00 44.56  ? 941  HOH A O     1 
HETATM 3291 O O     . HOH F 5 .   ? 7.162  4.034  26.506 1.00 31.05  ? 942  HOH A O     1 
HETATM 3292 O O     . HOH F 5 .   ? 11.676 7.900  7.121  1.00 35.82  ? 943  HOH A O     1 
HETATM 3293 O O     . HOH F 5 .   ? 13.580 38.222 28.926 1.00 42.32  ? 944  HOH A O     1 
HETATM 3294 O O     . HOH F 5 .   ? 29.019 5.797  35.877 1.00 40.72  ? 945  HOH A O     1 
HETATM 3295 O O     . HOH F 5 .   ? 19.228 7.247  -1.524 1.00 42.48  ? 946  HOH A O     1 
HETATM 3296 O O     . HOH F 5 .   ? 41.823 27.952 22.697 1.00 30.21  ? 947  HOH A O     1 
HETATM 3297 O O     . HOH F 5 .   ? 22.235 31.821 -2.320 1.00 29.92  ? 948  HOH A O     1 
HETATM 3298 O O     . HOH F 5 .   ? 28.228 16.964 -3.636 1.00 39.66  ? 949  HOH A O     1 
HETATM 3299 O O     . HOH F 5 .   ? 7.470  30.058 42.220 1.00 36.29  ? 950  HOH A O     1 
HETATM 3300 O O     . HOH F 5 .   ? 24.964 42.386 10.190 1.00 40.52  ? 951  HOH A O     1 
HETATM 3301 O O     . HOH F 5 .   ? 18.862 32.527 44.408 1.00 25.81  ? 952  HOH A O     1 
HETATM 3302 O O     . HOH F 5 .   ? 36.219 40.706 19.739 1.00 41.23  ? 953  HOH A O     1 
HETATM 3303 O O     . HOH F 5 .   ? 9.760  26.459 2.252  1.00 41.66  ? 954  HOH A O     1 
HETATM 3304 O O     . HOH F 5 .   ? 42.676 31.053 3.432  1.00 34.39  ? 955  HOH A O     1 
HETATM 3305 O O     . HOH F 5 .   ? 41.885 19.604 10.108 1.00 26.54  ? 956  HOH A O     1 
HETATM 3306 O O     . HOH F 5 .   ? 3.183  6.363  30.658 1.00 53.28  ? 957  HOH A O     1 
HETATM 3307 O O     . HOH F 5 .   ? 29.660 36.243 27.261 1.00 19.38  ? 958  HOH A O     1 
HETATM 3308 O O     . HOH F 5 .   ? 6.416  3.385  31.251 1.00 33.72  ? 959  HOH A O     1 
HETATM 3309 O O     . HOH F 5 .   ? 22.482 43.264 11.062 1.00 33.31  ? 960  HOH A O     1 
HETATM 3310 O O     . HOH F 5 .   ? 30.579 33.984 28.619 1.00 21.83  ? 961  HOH A O     1 
HETATM 3311 O O     . HOH F 5 .   ? 19.588 16.533 -3.841 1.00 36.73  ? 962  HOH A O     1 
HETATM 3312 O O     . HOH F 5 .   ? 7.913  -0.251 11.550 1.00 41.39  ? 963  HOH A O     1 
HETATM 3313 O O     . HOH F 5 .   ? 4.843  16.961 42.966 1.00 44.49  ? 964  HOH A O     1 
HETATM 3314 O O     . HOH F 5 .   ? 15.215 34.518 41.950 1.00 27.71  ? 965  HOH A O     1 
HETATM 3315 O O     . HOH F 5 .   ? 8.125  27.823 3.363  1.00 40.78  ? 966  HOH A O     1 
HETATM 3316 O O     . HOH F 5 .   ? 24.279 12.990 41.732 1.00 40.97  ? 967  HOH A O     1 
HETATM 3317 O O     . HOH F 5 .   ? 6.239  1.767  33.553 1.00 39.61  ? 968  HOH A O     1 
HETATM 3318 O O     . HOH F 5 .   ? 9.599  36.134 4.214  1.00 27.03  ? 969  HOH A O     1 
HETATM 3319 O O     . HOH F 5 .   ? 11.258 31.156 44.653 1.00 28.61  ? 970  HOH A O     1 
HETATM 3320 O O     . HOH F 5 .   ? 1.367  26.972 29.929 1.00 44.48  ? 971  HOH A O     1 
HETATM 3321 O O     . HOH F 5 .   ? 33.048 27.989 0.228  1.00 31.82  ? 972  HOH A O     1 
HETATM 3322 O O     . HOH F 5 .   ? 31.038 38.343 27.922 1.00 34.40  ? 973  HOH A O     1 
HETATM 3323 O O     . HOH F 5 .   ? 42.362 14.414 18.213 1.00 45.03  ? 974  HOH A O     1 
HETATM 3324 O O     . HOH F 5 .   ? 17.989 39.110 28.728 1.00 15.70  ? 975  HOH A O     1 
HETATM 3325 O O     . HOH F 5 .   ? 44.417 26.898 3.204  1.00 35.94  ? 976  HOH A O     1 
HETATM 3326 O O     . HOH F 5 .   ? 31.292 9.299  27.188 1.00 43.99  ? 977  HOH A O     1 
HETATM 3327 O O     . HOH F 5 .   ? 24.031 16.628 43.199 1.00 49.90  ? 978  HOH A O     1 
HETATM 3328 O O     . HOH F 5 .   ? 42.283 29.125 -0.533 1.00 46.03  ? 979  HOH A O     1 
HETATM 3329 O O     . HOH F 5 .   ? 29.710 2.857  29.610 1.00 35.24  ? 980  HOH A O     1 
HETATM 3330 O O     . HOH F 5 .   ? 0.365  24.755 32.851 1.00 30.13  ? 981  HOH A O     1 
HETATM 3331 O O     . HOH F 5 .   ? 15.223 38.218 3.985  1.00 42.07  ? 982  HOH A O     1 
HETATM 3332 O O     . HOH F 5 .   ? 3.006  32.317 24.243 1.00 41.30  ? 983  HOH A O     1 
HETATM 3333 O O     . HOH F 5 .   ? 22.572 2.653  6.780  1.00 40.16  ? 984  HOH A O     1 
HETATM 3334 O O     . HOH F 5 .   ? 23.727 38.421 39.967 1.00 32.43  ? 985  HOH A O     1 
HETATM 3335 O O     . HOH F 5 .   ? 42.920 11.979 15.539 1.00 45.13  ? 986  HOH A O     1 
HETATM 3336 O O     . HOH F 5 .   ? 7.662  38.961 6.710  1.00 37.88  ? 987  HOH A O     1 
HETATM 3337 O O     . HOH F 5 .   ? 8.509  36.115 25.859 1.00 37.34  ? 988  HOH A O     1 
HETATM 3338 O O     . HOH F 5 .   ? 37.369 42.389 16.037 1.00 41.32  ? 989  HOH A O     1 
HETATM 3339 O O     . HOH F 5 .   ? -0.751 20.620 10.890 1.00 43.69  ? 990  HOH A O     1 
HETATM 3340 O O     . HOH F 5 .   ? 4.218  37.458 6.756  1.00 49.02  ? 991  HOH A O     1 
HETATM 3341 O O     . HOH F 5 .   ? 10.335 -1.509 11.582 1.00 48.63  ? 992  HOH A O     1 
HETATM 3342 O O     . HOH F 5 .   ? 16.998 0.800  36.894 1.00 24.48  ? 993  HOH A O     1 
HETATM 3343 O O     . HOH F 5 .   ? 2.804  36.968 20.638 1.00 41.87  ? 994  HOH A O     1 
HETATM 3344 O O     . HOH F 5 .   ? 1.200  14.674 26.458 1.00 19.36  ? 995  HOH A O     1 
HETATM 3345 O O     . HOH F 5 .   ? 4.085  31.973 30.406 1.00 42.48  ? 996  HOH A O     1 
HETATM 3346 O O     . HOH F 5 .   ? -0.335 34.529 11.411 1.00 43.88  ? 997  HOH A O     1 
HETATM 3347 O O     . HOH F 5 .   ? 33.309 43.208 9.665  1.00 36.71  ? 998  HOH A O     1 
HETATM 3348 O O     . HOH F 5 .   ? 2.004  36.425 7.903  1.00 48.43  ? 999  HOH A O     1 
HETATM 3349 O O     . HOH F 5 .   ? 34.733 36.547 28.621 1.00 38.67  ? 1000 HOH A O     1 
HETATM 3350 O O     . HOH F 5 .   ? 15.422 35.424 0.583  1.00 28.79  ? 1001 HOH A O     1 
HETATM 3351 O O     . HOH F 5 .   ? -0.530 35.679 16.734 1.00 42.32  ? 1002 HOH A O     1 
HETATM 3352 O O     . HOH F 5 .   ? 37.839 33.364 -3.479 1.00 52.63  ? 1003 HOH A O     1 
HETATM 3353 O O     . HOH F 5 .   ? 32.838 -0.620 20.762 1.00 38.87  ? 1004 HOH A O     1 
HETATM 3354 O O     . HOH F 5 .   ? 18.944 40.743 5.868  1.00 34.89  ? 1005 HOH A O     1 
HETATM 3355 O O     . HOH F 5 .   ? 12.217 6.173  5.322  1.00 49.11  ? 1006 HOH A O     1 
HETATM 3356 O O     . HOH F 5 .   ? 43.486 33.367 3.480  1.00 45.52  ? 1007 HOH A O     1 
HETATM 3357 O O     . HOH F 5 .   ? 31.142 26.506 1.380  1.00 24.35  ? 1008 HOH A O     1 
HETATM 3358 O O     . HOH F 5 .   ? 21.841 43.117 8.534  1.00 43.49  ? 1009 HOH A O     1 
HETATM 3359 O O     . HOH F 5 .   ? 20.537 33.691 -3.202 1.00 35.03  ? 1010 HOH A O     1 
HETATM 3360 O O     . HOH F 5 .   ? 1.781  21.396 9.741  1.00 27.14  ? 1011 HOH A O     1 
HETATM 3361 O O     . HOH F 5 .   ? 0.537  26.673 7.531  1.00 47.78  ? 1012 HOH A O     1 
HETATM 3362 O O     . HOH F 5 .   ? 13.199 0.261  39.664 1.00 27.87  ? 1013 HOH A O     1 
HETATM 3363 O O     . HOH F 5 .   ? 16.473 33.505 44.249 1.00 31.63  ? 1014 HOH A O     1 
HETATM 3364 O O     . HOH F 5 .   ? 16.920 39.533 6.455  1.00 38.51  ? 1015 HOH A O     1 
HETATM 3365 O O     . HOH F 5 .   ? 34.127 32.962 -0.426 1.00 44.14  ? 1016 HOH A O     1 
HETATM 3366 O O     . HOH F 5 .   ? 31.140 40.188 38.354 1.00 45.00  ? 1017 HOH A O     1 
HETATM 3367 O O     . HOH F 5 .   ? 39.679 37.627 4.405  1.00 46.84  ? 1018 HOH A O     1 
HETATM 3368 O O     . HOH F 5 .   ? 8.095  -0.529 33.632 1.00 29.88  ? 1019 HOH A O     1 
HETATM 3369 O O     . HOH F 5 .   ? 31.254 7.698  28.895 1.00 38.23  ? 1020 HOH A O     1 
HETATM 3370 O O     . HOH F 5 .   ? 4.298  34.387 30.337 1.00 38.13  ? 1021 HOH A O     1 
HETATM 3371 O O     . HOH F 5 .   ? 4.172  35.208 24.024 1.00 44.11  ? 1022 HOH A O     1 
HETATM 3372 O O     . HOH F 5 .   ? 26.002 44.726 10.332 1.00 33.45  ? 1023 HOH A O     1 
HETATM 3373 O O     . HOH F 5 .   ? 5.101  36.210 28.875 1.00 30.86  ? 1024 HOH A O     1 
HETATM 3374 O O     . HOH F 5 .   ? 32.200 30.889 -0.069 1.00 43.29  ? 1025 HOH A O     1 
HETATM 3375 O O     . HOH F 5 .   ? 28.318 44.498 8.499  1.00 36.83  ? 1026 HOH A O     1 
HETATM 3376 O O     . HOH F 5 .   ? 1.805  21.644 7.149  1.00 49.96  ? 1027 HOH A O     1 
HETATM 3377 O O     . HOH F 5 .   ? 20.841 36.199 45.260 1.00 42.57  ? 1028 HOH A O     1 
HETATM 3378 O O     . HOH F 5 .   ? 41.917 12.058 20.017 1.00 44.13  ? 1029 HOH A O     1 
HETATM 3379 O O     . HOH F 5 .   ? 15.911 35.303 45.961 1.00 41.61  ? 1030 HOH A O     1 
HETATM 3380 O O     . HOH F 5 .   ? 1.371  34.789 30.196 1.00 54.44  ? 1031 HOH A O     1 
# 
