data_8S7N
# 
_entry.id   8S7N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8S7N         pdb_00008s7n 10.2210/pdb8s7n/pdb 
WWPDB D_1292137007 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-01-22 
3 'Structure model' 1 2 2025-02-05 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 3 'Structure model' citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S7N 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-04 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Mattevi 
_pdbx_contact_author.name_last          Andrea 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guerriere, T.B.' 1 0009-0003-3232-6822 
'Mattevi, A.'     2 0000-0002-9523-7128 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1046 
_citation.page_last                 1060 
_citation.title                     
'Dehydrogenase versus oxidase function: the interplay between substrate binding and flavin microenvironment.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c05944 
_citation.pdbx_database_id_PubMed   39781101 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guerriere, T.B.' 1  ? 
primary 'Vancheri, A.'    2  ? 
primary 'Ricotti, I.'     3  ? 
primary 'Serapian, S.A.'  4  ? 
primary 'Eggerichs, D.'   5  ? 
primary 'Tischler, D.'    6  ? 
primary 'Colombo, G.'     7  ? 
primary 'Mascotti, M.L.'  8  ? 
primary 'Fraaije, M.W.'   9  ? 
primary 'Mattevi, A.'     10 ? 
# 
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 Oxidoreductase                                                                       58261.840 2   ? ? ? ? 
2 non-polymer nat 'FLAVIN-ADENINE DINUCLEOTIDE'                                                        785.550   2   ? ? ? ? 
3 non-polymer syn 'NITRATE ION'                                                                        62.005    8   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                              106.120   3   ? ? ? ? 
5 non-polymer syn 'PENTAETHYLENE GLYCOL'                                                               238.278   2   ? ? ? ? 
6 non-polymer syn '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' 354.436   1   ? ? ? ? 
7 non-polymer syn '2-methoxy-4-(prop-2-en-1-yl)phenol'                                                 164.201   2   ? ? ? ? 
8 water       nat water                                                                                18.015    917 ? ? ? ? 
# 
_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       
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDLGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDLGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE'                                                        FAD 
3 'NITRATE ION'                                                                        NO3 
4 'DI(HYDROXYETHYL)ETHER'                                                              PEG 
5 'PENTAETHYLENE GLYCOL'                                                               1PE 
6 '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' PE4 
7 '2-methoxy-4-(prop-2-en-1-yl)phenol'                                                 EOL 
8 water                                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ALA n 
1 4   PRO n 
1 5   LEU n 
1 6   PRO n 
1 7   GLU n 
1 8   GLY n 
1 9   VAL n 
1 10  SER n 
1 11  ALA n 
1 12  GLU n 
1 13  ALA n 
1 14  MET n 
1 15  SER n 
1 16  SER n 
1 17  ALA n 
1 18  LEU n 
1 19  ASP n 
1 20  ARG n 
1 21  PHE n 
1 22  ALA n 
1 23  ARG n 
1 24  ILE n 
1 25  VAL n 
1 26  GLY n 
1 27  ALA n 
1 28  ASP n 
1 29  TRP n 
1 30  VAL n 
1 31  PHE n 
1 32  THR n 
1 33  GLU n 
1 34  ASP n 
1 35  LYS n 
1 36  ILE n 
1 37  THR n 
1 38  PRO n 
1 39  TYR n 
1 40  GLU n 
1 41  ASP n 
1 42  PRO n 
1 43  TYR n 
1 44  THR n 
1 45  ILE n 
1 46  SER n 
1 47  ASN n 
1 48  ASP n 
1 49  GLU n 
1 50  THR n 
1 51  GLU n 
1 52  HIS n 
1 53  ARG n 
1 54  PRO n 
1 55  TYR n 
1 56  ALA n 
1 57  ALA n 
1 58  VAL n 
1 59  ALA n 
1 60  PRO n 
1 61  ALA n 
1 62  SER n 
1 63  THR n 
1 64  GLU n 
1 65  GLU n 
1 66  VAL n 
1 67  GLN n 
1 68  GLU n 
1 69  ILE n 
1 70  VAL n 
1 71  ARG n 
1 72  VAL n 
1 73  ALA n 
1 74  ASN n 
1 75  GLU n 
1 76  PHE n 
1 77  GLY n 
1 78  VAL n 
1 79  PRO n 
1 80  LEU n 
1 81  TRP n 
1 82  PRO n 
1 83  VAL n 
1 84  SER n 
1 85  ARG n 
1 86  GLY n 
1 87  LYS n 
1 88  ASN n 
1 89  PHE n 
1 90  ALA n 
1 91  TYR n 
1 92  GLY n 
1 93  GLY n 
1 94  ALA n 
1 95  ALA n 
1 96  PRO n 
1 97  VAL n 
1 98  MET n 
1 99  SER n 
1 100 GLY n 
1 101 THR n 
1 102 VAL n 
1 103 VAL n 
1 104 LEU n 
1 105 ASP n 
1 106 MET n 
1 107 ASN n 
1 108 ARG n 
1 109 MET n 
1 110 ASN n 
1 111 ARG n 
1 112 ILE n 
1 113 LEU n 
1 114 GLU n 
1 115 VAL n 
1 116 ASN n 
1 117 GLU n 
1 118 GLU n 
1 119 PHE n 
1 120 GLY n 
1 121 TYR n 
1 122 ALA n 
1 123 LEU n 
1 124 VAL n 
1 125 GLU n 
1 126 PRO n 
1 127 GLY n 
1 128 VAL n 
1 129 SER n 
1 130 TYR n 
1 131 PHE n 
1 132 GLU n 
1 133 LEU n 
1 134 TYR n 
1 135 ASP n 
1 136 TYR n 
1 137 ILE n 
1 138 GLN n 
1 139 GLU n 
1 140 LYS n 
1 141 GLY n 
1 142 LEU n 
1 143 LYS n 
1 144 LEU n 
1 145 TRP n 
1 146 ILE n 
1 147 ASP n 
1 148 VAL n 
1 149 PRO n 
1 150 ASP n 
1 151 LEU n 
1 152 GLY n 
1 153 TRP n 
1 154 GLY n 
1 155 SER n 
1 156 VAL n 
1 157 VAL n 
1 158 GLY n 
1 159 ASN n 
1 160 ALA n 
1 161 LEU n 
1 162 ASP n 
1 163 HIS n 
1 164 GLY n 
1 165 ILE n 
1 166 GLY n 
1 167 TYR n 
1 168 THR n 
1 169 PRO n 
1 170 TYR n 
1 171 GLY n 
1 172 ASP n 
1 173 HIS n 
1 174 PHE n 
1 175 ALA n 
1 176 MET n 
1 177 GLN n 
1 178 CYS n 
1 179 GLY n 
1 180 MET n 
1 181 GLU n 
1 182 VAL n 
1 183 VAL n 
1 184 LEU n 
1 185 PRO n 
1 186 ASN n 
1 187 GLY n 
1 188 GLU n 
1 189 VAL n 
1 190 VAL n 
1 191 ARG n 
1 192 THR n 
1 193 GLY n 
1 194 MET n 
1 195 GLY n 
1 196 ALA n 
1 197 MET n 
1 198 PRO n 
1 199 GLY n 
1 200 ASN n 
1 201 ASN n 
1 202 THR n 
1 203 TRP n 
1 204 GLN n 
1 205 LEU n 
1 206 PHE n 
1 207 LYS n 
1 208 TYR n 
1 209 GLY n 
1 210 TYR n 
1 211 GLY n 
1 212 PRO n 
1 213 TYR n 
1 214 VAL n 
1 215 ASP n 
1 216 GLY n 
1 217 ILE n 
1 218 PHE n 
1 219 SER n 
1 220 GLN n 
1 221 SER n 
1 222 ASN n 
1 223 PHE n 
1 224 GLY n 
1 225 VAL n 
1 226 VAL n 
1 227 THR n 
1 228 LYS n 
1 229 MET n 
1 230 GLY n 
1 231 ILE n 
1 232 TRP n 
1 233 LEU n 
1 234 MET n 
1 235 PRO n 
1 236 GLU n 
1 237 PRO n 
1 238 ALA n 
1 239 GLY n 
1 240 TYR n 
1 241 ARG n 
1 242 PRO n 
1 243 TYR n 
1 244 LEU n 
1 245 ILE n 
1 246 THR n 
1 247 PHE n 
1 248 GLU n 
1 249 ASN n 
1 250 GLU n 
1 251 ASP n 
1 252 ASP n 
1 253 ILE n 
1 254 GLU n 
1 255 THR n 
1 256 VAL n 
1 257 THR n 
1 258 GLU n 
1 259 ARG n 
1 260 LEU n 
1 261 ARG n 
1 262 PRO n 
1 263 LEU n 
1 264 LYS n 
1 265 VAL n 
1 266 ALA n 
1 267 GLY n 
1 268 VAL n 
1 269 ILE n 
1 270 GLN n 
1 271 ASN n 
1 272 GLY n 
1 273 ALA n 
1 274 THR n 
1 275 VAL n 
1 276 ARG n 
1 277 SER n 
1 278 LEU n 
1 279 VAL n 
1 280 LEU n 
1 281 ASP n 
1 282 ALA n 
1 283 ALA n 
1 284 ILE n 
1 285 THR n 
1 286 ARG n 
1 287 THR n 
1 288 LYS n 
1 289 SER n 
1 290 GLN n 
1 291 TYR n 
1 292 TYR n 
1 293 ASP n 
1 294 GLY n 
1 295 ASP n 
1 296 GLY n 
1 297 PRO n 
1 298 ILE n 
1 299 PRO n 
1 300 PRO n 
1 301 SER n 
1 302 VAL n 
1 303 ALA n 
1 304 LYS n 
1 305 THR n 
1 306 MET n 
1 307 MET n 
1 308 ALA n 
1 309 ASP n 
1 310 LEU n 
1 311 ASP n 
1 312 LEU n 
1 313 GLY n 
1 314 MET n 
1 315 TRP n 
1 316 ASN n 
1 317 PHE n 
1 318 CYS n 
1 319 GLY n 
1 320 ALA n 
1 321 LEU n 
1 322 TYR n 
1 323 GLY n 
1 324 PRO n 
1 325 PRO n 
1 326 PRO n 
1 327 VAL n 
1 328 MET n 
1 329 ASP n 
1 330 THR n 
1 331 LEU n 
1 332 TRP n 
1 333 THR n 
1 334 ALA n 
1 335 ILE n 
1 336 ARG n 
1 337 ASP n 
1 338 SER n 
1 339 PHE n 
1 340 ALA n 
1 341 ASP n 
1 342 ILE n 
1 343 PRO n 
1 344 GLY n 
1 345 VAL n 
1 346 LYS n 
1 347 PHE n 
1 348 TYR n 
1 349 PHE n 
1 350 PRO n 
1 351 GLU n 
1 352 ASP n 
1 353 ARG n 
1 354 ARG n 
1 355 HIS n 
1 356 LYS n 
1 357 VAL n 
1 358 ASP n 
1 359 LEU n 
1 360 LEU n 
1 361 LEU n 
1 362 HIS n 
1 363 ARG n 
1 364 ALA n 
1 365 GLU n 
1 366 THR n 
1 367 MET n 
1 368 LYS n 
1 369 GLY n 
1 370 VAL n 
1 371 PRO n 
1 372 LYS n 
1 373 LEU n 
1 374 THR n 
1 375 GLU n 
1 376 PHE n 
1 377 ASN n 
1 378 PHE n 
1 379 LEU n 
1 380 ASN n 
1 381 TRP n 
1 382 ASP n 
1 383 GLY n 
1 384 GLY n 
1 385 GLY n 
1 386 GLY n 
1 387 HIS n 
1 388 VAL n 
1 389 GLY n 
1 390 PHE n 
1 391 SER n 
1 392 PRO n 
1 393 VAL n 
1 394 SER n 
1 395 PRO n 
1 396 ILE n 
1 397 THR n 
1 398 GLY n 
1 399 LYS n 
1 400 ASP n 
1 401 ALA n 
1 402 ILE n 
1 403 LYS n 
1 404 GLN n 
1 405 TYR n 
1 406 ASN n 
1 407 MET n 
1 408 VAL n 
1 409 SER n 
1 410 SER n 
1 411 ARG n 
1 412 VAL n 
1 413 ARG n 
1 414 GLU n 
1 415 TYR n 
1 416 GLY n 
1 417 PHE n 
1 418 ASP n 
1 419 TYR n 
1 420 MET n 
1 421 GLY n 
1 422 LEU n 
1 423 LEU n 
1 424 ALA n 
1 425 ILE n 
1 426 GLY n 
1 427 TRP n 
1 428 ARG n 
1 429 ASP n 
1 430 LEU n 
1 431 HIS n 
1 432 HIS n 
1 433 VAL n 
1 434 THR n 
1 435 VAL n 
1 436 ILE n 
1 437 VAL n 
1 438 TYR n 
1 439 ASP n 
1 440 LYS n 
1 441 THR n 
1 442 ASP n 
1 443 PRO n 
1 444 ASP n 
1 445 GLU n 
1 446 ARG n 
1 447 LYS n 
1 448 LYS n 
1 449 LEU n 
1 450 ASP n 
1 451 GLU n 
1 452 LEU n 
1 453 PHE n 
1 454 ASN n 
1 455 ILE n 
1 456 LEU n 
1 457 VAL n 
1 458 ASP n 
1 459 GLU n 
1 460 ALA n 
1 461 ALA n 
1 462 ALA n 
1 463 GLU n 
1 464 GLY n 
1 465 TYR n 
1 466 GLY n 
1 467 GLU n 
1 468 TYR n 
1 469 ARG n 
1 470 THR n 
1 471 HIS n 
1 472 ILE n 
1 473 ARG n 
1 474 TYR n 
1 475 MET n 
1 476 ASP n 
1 477 ARG n 
1 478 ILE n 
1 479 ALA n 
1 480 LYS n 
1 481 THR n 
1 482 TYR n 
1 483 SER n 
1 484 TRP n 
1 485 ASN n 
1 486 ASP n 
1 487 ASN n 
1 488 ALA n 
1 489 LEU n 
1 490 TRP n 
1 491 LYS n 
1 492 MET n 
1 493 HIS n 
1 494 GLU n 
1 495 THR n 
1 496 ILE n 
1 497 LYS n 
1 498 ASP n 
1 499 ALA n 
1 500 LEU n 
1 501 ASP n 
1 502 PRO n 
1 503 ASN n 
1 504 GLY n 
1 505 ILE n 
1 506 LEU n 
1 507 ALA n 
1 508 PRO n 
1 509 GLY n 
1 510 LYS n 
1 511 SER n 
1 512 GLY n 
1 513 ILE n 
1 514 TRP n 
1 515 GLY n 
1 516 LYS n 
1 517 ASN n 
1 518 ARG n 
1 519 ARG n 
1 520 LYS n 
1 521 ALA 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                   521 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CW354_13745 
_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      'Marinicaulis flavus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2058213 
_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               NEB10beta 
_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 
1PE non-polymer         . 'PENTAETHYLENE GLYCOL'                                                               PEG400 'C10 H22 O6' 
238.278 
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 
EOL non-polymer         . '2-methoxy-4-(prop-2-en-1-yl)phenol'                                                 eugenol 
'C10 H12 O2'        164.201 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                                                        ? 
'C27 H33 N9 O15 P2' 785.550 
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 
NO3 non-polymer         . 'NITRATE ION'                                                                        ? 'N O3 -1' 62.005  
PE4 non-polymer         . '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' 
'POLYETHYLENE GLYCOL PEG4000' 'C16 H34 O8'        354.436 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                              ? 'C4 H10 O3' 
106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ASN 47  47  47  ASN ASN A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  TRP 81  81  81  TRP TRP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 TRP 145 145 145 TRP TRP A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 MET 180 180 180 MET MET A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 MET 197 197 197 MET MET A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ASN 222 222 222 ASN ASN A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 TRP 232 232 232 TRP TRP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ARG 261 261 261 ARG ARG A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 GLN 290 290 290 GLN GLN A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 MET 307 307 307 MET MET A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 THR 333 333 333 THR THR A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 PRO 343 343 343 PRO PRO A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 HIS 362 362 362 HIS HIS A . n 
A 1 363 ARG 363 363 363 ARG ARG A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 MET 367 367 367 MET MET A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 TRP 381 381 381 TRP TRP A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 HIS 387 387 387 HIS HIS A . n 
A 1 388 VAL 388 388 388 VAL VAL A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 PRO 395 395 395 PRO PRO A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 LYS 399 399 399 LYS LYS A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 ALA 401 401 401 ALA ALA A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 TYR 405 405 405 TYR TYR A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 MET 407 407 407 MET MET A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLY 426 426 426 GLY GLY A . n 
A 1 427 TRP 427 427 427 TRP TRP A . n 
A 1 428 ARG 428 428 428 ARG ARG A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 HIS 431 431 431 HIS HIS A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 THR 434 434 434 THR THR A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 ILE 436 436 436 ILE ILE A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 TYR 438 438 438 TYR TYR A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 THR 441 441 441 THR THR A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 PRO 443 443 443 PRO PRO A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 LYS 448 448 448 LYS LYS A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 ASP 450 450 450 ASP ASP A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 ASN 454 454 454 ASN ASN A . n 
A 1 455 ILE 455 455 455 ILE ILE A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ALA 462 462 462 ALA ALA A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 GLU 467 467 467 GLU GLU A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 THR 470 470 470 THR THR A . n 
A 1 471 HIS 471 471 471 HIS HIS A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 TYR 474 474 474 TYR TYR A . n 
A 1 475 MET 475 475 475 MET MET A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ALA 479 479 479 ALA ALA A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 TYR 482 482 482 TYR TYR A . n 
A 1 483 SER 483 483 483 SER SER A . n 
A 1 484 TRP 484 484 484 TRP TRP A . n 
A 1 485 ASN 485 485 485 ASN ASN A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 MET 492 492 492 MET MET A . n 
A 1 493 HIS 493 493 493 HIS HIS A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 THR 495 495 495 THR THR A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 LYS 497 497 497 LYS LYS A . n 
A 1 498 ASP 498 498 498 ASP ASP A . n 
A 1 499 ALA 499 499 499 ALA ALA A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 PRO 502 502 502 PRO PRO A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 GLY 504 504 504 GLY GLY A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 LEU 506 506 506 LEU LEU A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 PRO 508 508 508 PRO PRO A . n 
A 1 509 GLY 509 509 509 GLY GLY A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 ILE 513 513 513 ILE ILE A . n 
A 1 514 TRP 514 514 514 TRP TRP A . n 
A 1 515 GLY 515 515 515 GLY GLY A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 ASN 517 517 517 ASN ASN A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 LYS 520 520 ?   ?   ?   A . n 
A 1 521 ALA 521 521 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   ALA 3   3   3   ALA ALA B . n 
B 1 4   PRO 4   4   4   PRO PRO B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  MET 14  14  14  MET MET B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  GLU 33  33  33  GLU GLU B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ASN 47  47  47  ASN ASN B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  TYR 55  55  55  TYR TYR B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  TRP 81  81  81  TRP TRP B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  MET 98  98  98  MET MET B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 THR 101 101 101 THR THR B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 MET 109 109 109 MET MET B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 TYR 136 136 136 TYR TYR B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 TRP 145 145 145 TRP TRP B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 TRP 153 153 153 TRP TRP B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 VAL 156 156 156 VAL VAL B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 GLN 177 177 177 GLN GLN B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 MET 180 180 180 MET MET B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 GLU 188 188 188 GLU GLU B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 MET 194 194 194 MET MET B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 MET 197 197 197 MET MET B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 TRP 203 203 203 TRP TRP B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 TYR 210 210 210 TYR TYR B . n 
B 1 211 GLY 211 211 211 GLY GLY B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 PHE 218 218 218 PHE PHE B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 ASN 222 222 222 ASN ASN B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 TRP 232 232 232 TRP TRP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 TYR 243 243 243 TYR TYR B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 GLU 250 250 250 GLU GLU B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 ARG 261 261 261 ARG ARG B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 ILE 269 269 269 ILE ILE B . n 
B 1 270 GLN 270 270 270 GLN GLN B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 ASP 281 281 281 ASP ASP B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 GLN 290 290 290 GLN GLN B . n 
B 1 291 TYR 291 291 291 TYR TYR B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 GLY 294 294 294 GLY GLY B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 PRO 297 297 297 PRO PRO B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 LYS 304 304 304 LYS LYS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 MET 306 306 306 MET MET B . n 
B 1 307 MET 307 307 307 MET MET B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 ASP 309 309 309 ASP ASP B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 GLY 313 313 313 GLY GLY B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 TRP 315 315 315 TRP TRP B . n 
B 1 316 ASN 316 316 316 ASN ASN B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 CYS 318 318 318 CYS CYS B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 TYR 322 322 322 TYR TYR B . n 
B 1 323 GLY 323 323 323 GLY GLY B . n 
B 1 324 PRO 324 324 324 PRO PRO B . n 
B 1 325 PRO 325 325 325 PRO PRO B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 MET 328 328 328 MET MET B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 THR 330 330 330 THR THR B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 TRP 332 332 332 TRP TRP B . n 
B 1 333 THR 333 333 333 THR THR B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 ARG 336 336 336 ARG ARG B . n 
B 1 337 ASP 337 337 337 ASP ASP B . n 
B 1 338 SER 338 338 338 SER SER B . n 
B 1 339 PHE 339 339 339 PHE PHE B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 ASP 341 341 341 ASP ASP B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 PRO 343 343 343 PRO PRO B . n 
B 1 344 GLY 344 344 344 GLY GLY B . n 
B 1 345 VAL 345 345 345 VAL VAL B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 ARG 353 353 353 ARG ARG B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 HIS 355 355 355 HIS HIS B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 HIS 362 362 362 HIS HIS B . n 
B 1 363 ARG 363 363 363 ARG ARG B . n 
B 1 364 ALA 364 364 364 ALA ALA B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 MET 367 367 367 MET MET B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 PRO 371 371 371 PRO PRO B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 GLU 375 375 375 GLU GLU B . n 
B 1 376 PHE 376 376 376 PHE PHE B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 TRP 381 381 381 TRP TRP B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 GLY 383 383 383 GLY GLY B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 HIS 387 387 387 HIS HIS B . n 
B 1 388 VAL 388 388 388 VAL VAL B . n 
B 1 389 GLY 389 389 389 GLY GLY B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 SER 391 391 391 SER SER B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 VAL 393 393 393 VAL VAL B . n 
B 1 394 SER 394 394 394 SER SER B . n 
B 1 395 PRO 395 395 395 PRO PRO B . n 
B 1 396 ILE 396 396 396 ILE ILE B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLY 398 398 398 GLY GLY B . n 
B 1 399 LYS 399 399 399 LYS LYS B . n 
B 1 400 ASP 400 400 400 ASP ASP B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 ILE 402 402 402 ILE ILE B . n 
B 1 403 LYS 403 403 403 LYS LYS B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 TYR 405 405 405 TYR TYR B . n 
B 1 406 ASN 406 406 406 ASN ASN B . n 
B 1 407 MET 407 407 407 MET MET B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 SER 409 409 409 SER SER B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 VAL 412 412 412 VAL VAL B . n 
B 1 413 ARG 413 413 413 ARG ARG B . n 
B 1 414 GLU 414 414 414 GLU GLU B . n 
B 1 415 TYR 415 415 415 TYR TYR B . n 
B 1 416 GLY 416 416 416 GLY GLY B . n 
B 1 417 PHE 417 417 417 PHE PHE B . n 
B 1 418 ASP 418 418 418 ASP ASP B . n 
B 1 419 TYR 419 419 419 TYR TYR B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLY 421 421 421 GLY GLY B . n 
B 1 422 LEU 422 422 422 LEU LEU B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 ALA 424 424 424 ALA ALA B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLY 426 426 426 GLY GLY B . n 
B 1 427 TRP 427 427 427 TRP TRP B . n 
B 1 428 ARG 428 428 428 ARG ARG B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 HIS 431 431 431 HIS HIS B . n 
B 1 432 HIS 432 432 432 HIS HIS B . n 
B 1 433 VAL 433 433 433 VAL VAL B . n 
B 1 434 THR 434 434 434 THR THR B . n 
B 1 435 VAL 435 435 435 VAL VAL B . n 
B 1 436 ILE 436 436 436 ILE ILE B . n 
B 1 437 VAL 437 437 437 VAL VAL B . n 
B 1 438 TYR 438 438 438 TYR TYR B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 THR 441 441 441 THR THR B . n 
B 1 442 ASP 442 442 442 ASP ASP B . n 
B 1 443 PRO 443 443 443 PRO PRO B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 LYS 448 448 448 LYS LYS B . n 
B 1 449 LEU 449 449 449 LEU LEU B . n 
B 1 450 ASP 450 450 450 ASP ASP B . n 
B 1 451 GLU 451 451 451 GLU GLU B . n 
B 1 452 LEU 452 452 452 LEU LEU B . n 
B 1 453 PHE 453 453 453 PHE PHE B . n 
B 1 454 ASN 454 454 454 ASN ASN B . n 
B 1 455 ILE 455 455 455 ILE ILE B . n 
B 1 456 LEU 456 456 456 LEU LEU B . n 
B 1 457 VAL 457 457 457 VAL VAL B . n 
B 1 458 ASP 458 458 458 ASP ASP B . n 
B 1 459 GLU 459 459 459 GLU GLU B . n 
B 1 460 ALA 460 460 460 ALA ALA B . n 
B 1 461 ALA 461 461 461 ALA ALA B . n 
B 1 462 ALA 462 462 462 ALA ALA B . n 
B 1 463 GLU 463 463 463 GLU GLU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 TYR 465 465 465 TYR TYR B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 GLU 467 467 467 GLU GLU B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 THR 470 470 470 THR THR B . n 
B 1 471 HIS 471 471 471 HIS HIS B . n 
B 1 472 ILE 472 472 472 ILE ILE B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 TYR 474 474 474 TYR TYR B . n 
B 1 475 MET 475 475 475 MET MET B . n 
B 1 476 ASP 476 476 476 ASP ASP B . n 
B 1 477 ARG 477 477 477 ARG ARG B . n 
B 1 478 ILE 478 478 478 ILE ILE B . n 
B 1 479 ALA 479 479 479 ALA ALA B . n 
B 1 480 LYS 480 480 480 LYS LYS B . n 
B 1 481 THR 481 481 481 THR THR B . n 
B 1 482 TYR 482 482 482 TYR TYR B . n 
B 1 483 SER 483 483 483 SER SER B . n 
B 1 484 TRP 484 484 484 TRP TRP B . n 
B 1 485 ASN 485 485 485 ASN ASN B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 ASN 487 487 487 ASN ASN B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 LEU 489 489 489 LEU LEU B . n 
B 1 490 TRP 490 490 490 TRP TRP B . n 
B 1 491 LYS 491 491 491 LYS LYS B . n 
B 1 492 MET 492 492 492 MET MET B . n 
B 1 493 HIS 493 493 493 HIS HIS B . n 
B 1 494 GLU 494 494 494 GLU GLU B . n 
B 1 495 THR 495 495 495 THR THR B . n 
B 1 496 ILE 496 496 496 ILE ILE B . n 
B 1 497 LYS 497 497 497 LYS LYS B . n 
B 1 498 ASP 498 498 498 ASP ASP B . n 
B 1 499 ALA 499 499 499 ALA ALA B . n 
B 1 500 LEU 500 500 500 LEU LEU B . n 
B 1 501 ASP 501 501 501 ASP ASP B . n 
B 1 502 PRO 502 502 502 PRO PRO B . n 
B 1 503 ASN 503 503 503 ASN ASN B . n 
B 1 504 GLY 504 504 504 GLY GLY B . n 
B 1 505 ILE 505 505 505 ILE ILE B . n 
B 1 506 LEU 506 506 506 LEU LEU B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 PRO 508 508 508 PRO PRO B . n 
B 1 509 GLY 509 509 509 GLY GLY B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 SER 511 511 511 SER SER B . n 
B 1 512 GLY 512 512 512 GLY GLY B . n 
B 1 513 ILE 513 513 513 ILE ILE B . n 
B 1 514 TRP 514 514 514 TRP TRP B . n 
B 1 515 GLY 515 515 515 GLY GLY B . n 
B 1 516 LYS 516 516 516 LYS LYS B . n 
B 1 517 ASN 517 517 517 ASN ASN B . n 
B 1 518 ARG 518 518 518 ARG ARG B . n 
B 1 519 ARG 519 519 519 ARG ARG B . n 
B 1 520 LYS 520 520 ?   ?   ?   B . n 
B 1 521 ALA 521 521 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        EOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   EOL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FAD 1   601  601 FAD FAD A . 
D 3 NO3 1   602  603 NO3 NO3 A . 
E 3 NO3 1   603  606 NO3 NO3 A . 
F 4 PEG 1   604  609 PEG PEG A . 
G 5 1PE 1   605  613 1PE 1PE A . 
H 6 PE4 1   606  614 PE4 PE4 A . 
I 3 NO3 1   607  616 NO3 NO3 A . 
J 4 PEG 1   608  617 PEG PEG A . 
K 7 EOL 1   609  618 EOL EOL A . 
L 3 NO3 1   610  614 NO3 NO3 A . 
M 3 NO3 1   601  604 NO3 NO3 B . 
N 2 FAD 1   602  601 FAD FAD B . 
O 3 NO3 1   603  603 NO3 NO3 B . 
P 3 NO3 1   604  604 NO3 NO3 B . 
Q 3 NO3 1   605  605 NO3 NO3 B . 
R 4 PEG 1   606  610 PEG PEG B . 
S 5 1PE 1   607  612 1PE 1PE B . 
T 7 EOL 1   608  615 EOL EOL B . 
U 8 HOH 1   701  652 HOH HOH A . 
U 8 HOH 2   702  689 HOH HOH A . 
U 8 HOH 3   703  153 HOH HOH A . 
U 8 HOH 4   704  673 HOH HOH A . 
U 8 HOH 5   705  767 HOH HOH A . 
U 8 HOH 6   706  779 HOH HOH A . 
U 8 HOH 7   707  284 HOH HOH A . 
U 8 HOH 8   708  703 HOH HOH A . 
U 8 HOH 9   709  510 HOH HOH A . 
U 8 HOH 10  710  892 HOH HOH A . 
U 8 HOH 11  711  204 HOH HOH A . 
U 8 HOH 12  712  121 HOH HOH A . 
U 8 HOH 13  713  801 HOH HOH A . 
U 8 HOH 14  714  850 HOH HOH A . 
U 8 HOH 15  715  654 HOH HOH A . 
U 8 HOH 16  716  710 HOH HOH A . 
U 8 HOH 17  717  746 HOH HOH A . 
U 8 HOH 18  718  250 HOH HOH A . 
U 8 HOH 19  719  254 HOH HOH A . 
U 8 HOH 20  720  647 HOH HOH A . 
U 8 HOH 21  721  81  HOH HOH A . 
U 8 HOH 22  722  118 HOH HOH A . 
U 8 HOH 23  723  473 HOH HOH A . 
U 8 HOH 24  724  409 HOH HOH A . 
U 8 HOH 25  725  449 HOH HOH A . 
U 8 HOH 26  726  784 HOH HOH A . 
U 8 HOH 27  727  509 HOH HOH A . 
U 8 HOH 28  728  587 HOH HOH A . 
U 8 HOH 29  729  181 HOH HOH A . 
U 8 HOH 30  730  797 HOH HOH A . 
U 8 HOH 31  731  324 HOH HOH A . 
U 8 HOH 32  732  199 HOH HOH A . 
U 8 HOH 33  733  354 HOH HOH A . 
U 8 HOH 34  734  111 HOH HOH A . 
U 8 HOH 35  735  428 HOH HOH A . 
U 8 HOH 36  736  460 HOH HOH A . 
U 8 HOH 37  737  321 HOH HOH A . 
U 8 HOH 38  738  726 HOH HOH A . 
U 8 HOH 39  739  127 HOH HOH A . 
U 8 HOH 40  740  10  HOH HOH A . 
U 8 HOH 41  741  751 HOH HOH A . 
U 8 HOH 42  742  182 HOH HOH A . 
U 8 HOH 43  743  378 HOH HOH A . 
U 8 HOH 44  744  266 HOH HOH A . 
U 8 HOH 45  745  488 HOH HOH A . 
U 8 HOH 46  746  142 HOH HOH A . 
U 8 HOH 47  747  821 HOH HOH A . 
U 8 HOH 48  748  192 HOH HOH A . 
U 8 HOH 49  749  552 HOH HOH A . 
U 8 HOH 50  750  11  HOH HOH A . 
U 8 HOH 51  751  536 HOH HOH A . 
U 8 HOH 52  752  54  HOH HOH A . 
U 8 HOH 53  753  453 HOH HOH A . 
U 8 HOH 54  754  141 HOH HOH A . 
U 8 HOH 55  755  755 HOH HOH A . 
U 8 HOH 56  756  639 HOH HOH A . 
U 8 HOH 57  757  545 HOH HOH A . 
U 8 HOH 58  758  549 HOH HOH A . 
U 8 HOH 59  759  213 HOH HOH A . 
U 8 HOH 60  760  290 HOH HOH A . 
U 8 HOH 61  761  52  HOH HOH A . 
U 8 HOH 62  762  76  HOH HOH A . 
U 8 HOH 63  763  734 HOH HOH A . 
U 8 HOH 64  764  146 HOH HOH A . 
U 8 HOH 65  765  86  HOH HOH A . 
U 8 HOH 66  766  571 HOH HOH A . 
U 8 HOH 67  767  690 HOH HOH A . 
U 8 HOH 68  768  47  HOH HOH A . 
U 8 HOH 69  769  5   HOH HOH A . 
U 8 HOH 70  770  36  HOH HOH A . 
U 8 HOH 71  771  6   HOH HOH A . 
U 8 HOH 72  772  613 HOH HOH A . 
U 8 HOH 73  773  844 HOH HOH A . 
U 8 HOH 74  774  209 HOH HOH A . 
U 8 HOH 75  775  387 HOH HOH A . 
U 8 HOH 76  776  277 HOH HOH A . 
U 8 HOH 77  777  697 HOH HOH A . 
U 8 HOH 78  778  159 HOH HOH A . 
U 8 HOH 79  779  598 HOH HOH A . 
U 8 HOH 80  780  375 HOH HOH A . 
U 8 HOH 81  781  480 HOH HOH A . 
U 8 HOH 82  782  236 HOH HOH A . 
U 8 HOH 83  783  151 HOH HOH A . 
U 8 HOH 84  784  660 HOH HOH A . 
U 8 HOH 85  785  517 HOH HOH A . 
U 8 HOH 86  786  46  HOH HOH A . 
U 8 HOH 87  787  147 HOH HOH A . 
U 8 HOH 88  788  747 HOH HOH A . 
U 8 HOH 89  789  168 HOH HOH A . 
U 8 HOH 90  790  398 HOH HOH A . 
U 8 HOH 91  791  436 HOH HOH A . 
U 8 HOH 92  792  100 HOH HOH A . 
U 8 HOH 93  793  92  HOH HOH A . 
U 8 HOH 94  794  648 HOH HOH A . 
U 8 HOH 95  795  173 HOH HOH A . 
U 8 HOH 96  796  753 HOH HOH A . 
U 8 HOH 97  797  59  HOH HOH A . 
U 8 HOH 98  798  655 HOH HOH A . 
U 8 HOH 99  799  1   HOH HOH A . 
U 8 HOH 100 800  327 HOH HOH A . 
U 8 HOH 101 801  786 HOH HOH A . 
U 8 HOH 102 802  368 HOH HOH A . 
U 8 HOH 103 803  438 HOH HOH A . 
U 8 HOH 104 804  528 HOH HOH A . 
U 8 HOH 105 805  394 HOH HOH A . 
U 8 HOH 106 806  632 HOH HOH A . 
U 8 HOH 107 807  310 HOH HOH A . 
U 8 HOH 108 808  160 HOH HOH A . 
U 8 HOH 109 809  731 HOH HOH A . 
U 8 HOH 110 810  482 HOH HOH A . 
U 8 HOH 111 811  883 HOH HOH A . 
U 8 HOH 112 812  177 HOH HOH A . 
U 8 HOH 113 813  524 HOH HOH A . 
U 8 HOH 114 814  772 HOH HOH A . 
U 8 HOH 115 815  395 HOH HOH A . 
U 8 HOH 116 816  629 HOH HOH A . 
U 8 HOH 117 817  448 HOH HOH A . 
U 8 HOH 118 818  513 HOH HOH A . 
U 8 HOH 119 819  815 HOH HOH A . 
U 8 HOH 120 820  419 HOH HOH A . 
U 8 HOH 121 821  778 HOH HOH A . 
U 8 HOH 122 822  791 HOH HOH A . 
U 8 HOH 123 823  322 HOH HOH A . 
U 8 HOH 124 824  586 HOH HOH A . 
U 8 HOH 125 825  97  HOH HOH A . 
U 8 HOH 126 826  880 HOH HOH A . 
U 8 HOH 127 827  21  HOH HOH A . 
U 8 HOH 128 828  420 HOH HOH A . 
U 8 HOH 129 829  295 HOH HOH A . 
U 8 HOH 130 830  538 HOH HOH A . 
U 8 HOH 131 831  299 HOH HOH A . 
U 8 HOH 132 832  280 HOH HOH A . 
U 8 HOH 133 833  575 HOH HOH A . 
U 8 HOH 134 834  402 HOH HOH A . 
U 8 HOH 135 835  309 HOH HOH A . 
U 8 HOH 136 836  443 HOH HOH A . 
U 8 HOH 137 837  687 HOH HOH A . 
U 8 HOH 138 838  24  HOH HOH A . 
U 8 HOH 139 839  372 HOH HOH A . 
U 8 HOH 140 840  595 HOH HOH A . 
U 8 HOH 141 841  365 HOH HOH A . 
U 8 HOH 142 842  644 HOH HOH A . 
U 8 HOH 143 843  477 HOH HOH A . 
U 8 HOH 144 844  318 HOH HOH A . 
U 8 HOH 145 845  884 HOH HOH A . 
U 8 HOH 146 846  599 HOH HOH A . 
U 8 HOH 147 847  469 HOH HOH A . 
U 8 HOH 148 848  553 HOH HOH A . 
U 8 HOH 149 849  340 HOH HOH A . 
U 8 HOH 150 850  276 HOH HOH A . 
U 8 HOH 151 851  333 HOH HOH A . 
U 8 HOH 152 852  656 HOH HOH A . 
U 8 HOH 153 853  49  HOH HOH A . 
U 8 HOH 154 854  95  HOH HOH A . 
U 8 HOH 155 855  720 HOH HOH A . 
U 8 HOH 156 856  367 HOH HOH A . 
U 8 HOH 157 857  561 HOH HOH A . 
U 8 HOH 158 858  614 HOH HOH A . 
U 8 HOH 159 859  447 HOH HOH A . 
U 8 HOH 160 860  516 HOH HOH A . 
U 8 HOH 161 861  684 HOH HOH A . 
U 8 HOH 162 862  415 HOH HOH A . 
U 8 HOH 163 863  27  HOH HOH A . 
U 8 HOH 164 864  799 HOH HOH A . 
U 8 HOH 165 865  219 HOH HOH A . 
U 8 HOH 166 866  533 HOH HOH A . 
U 8 HOH 167 867  623 HOH HOH A . 
U 8 HOH 168 868  345 HOH HOH A . 
U 8 HOH 169 869  301 HOH HOH A . 
U 8 HOH 170 870  78  HOH HOH A . 
U 8 HOH 171 871  532 HOH HOH A . 
U 8 HOH 172 872  555 HOH HOH A . 
U 8 HOH 173 873  429 HOH HOH A . 
U 8 HOH 174 874  400 HOH HOH A . 
U 8 HOH 175 875  362 HOH HOH A . 
U 8 HOH 176 876  478 HOH HOH A . 
U 8 HOH 177 877  304 HOH HOH A . 
U 8 HOH 178 878  29  HOH HOH A . 
U 8 HOH 179 879  40  HOH HOH A . 
U 8 HOH 180 880  913 HOH HOH A . 
U 8 HOH 181 881  316 HOH HOH A . 
U 8 HOH 182 882  363 HOH HOH A . 
U 8 HOH 183 883  620 HOH HOH A . 
U 8 HOH 184 884  31  HOH HOH A . 
U 8 HOH 185 885  22  HOH HOH A . 
U 8 HOH 186 886  259 HOH HOH A . 
U 8 HOH 187 887  467 HOH HOH A . 
U 8 HOH 188 888  256 HOH HOH A . 
U 8 HOH 189 889  187 HOH HOH A . 
U 8 HOH 190 890  385 HOH HOH A . 
U 8 HOH 191 891  451 HOH HOH A . 
U 8 HOH 192 892  355 HOH HOH A . 
U 8 HOH 193 893  403 HOH HOH A . 
U 8 HOH 194 894  713 HOH HOH A . 
U 8 HOH 195 895  542 HOH HOH A . 
U 8 HOH 196 896  526 HOH HOH A . 
U 8 HOH 197 897  862 HOH HOH A . 
U 8 HOH 198 898  152 HOH HOH A . 
U 8 HOH 199 899  611 HOH HOH A . 
U 8 HOH 200 900  715 HOH HOH A . 
U 8 HOH 201 901  481 HOH HOH A . 
U 8 HOH 202 902  123 HOH HOH A . 
U 8 HOH 203 903  289 HOH HOH A . 
U 8 HOH 204 904  53  HOH HOH A . 
U 8 HOH 205 905  559 HOH HOH A . 
U 8 HOH 206 906  191 HOH HOH A . 
U 8 HOH 207 907  525 HOH HOH A . 
U 8 HOH 208 908  291 HOH HOH A . 
U 8 HOH 209 909  207 HOH HOH A . 
U 8 HOH 210 910  806 HOH HOH A . 
U 8 HOH 211 911  278 HOH HOH A . 
U 8 HOH 212 912  466 HOH HOH A . 
U 8 HOH 213 913  344 HOH HOH A . 
U 8 HOH 214 914  200 HOH HOH A . 
U 8 HOH 215 915  583 HOH HOH A . 
U 8 HOH 216 916  319 HOH HOH A . 
U 8 HOH 217 917  44  HOH HOH A . 
U 8 HOH 218 918  642 HOH HOH A . 
U 8 HOH 219 919  108 HOH HOH A . 
U 8 HOH 220 920  686 HOH HOH A . 
U 8 HOH 221 921  512 HOH HOH A . 
U 8 HOH 222 922  386 HOH HOH A . 
U 8 HOH 223 923  615 HOH HOH A . 
U 8 HOH 224 924  312 HOH HOH A . 
U 8 HOH 225 925  265 HOH HOH A . 
U 8 HOH 226 926  748 HOH HOH A . 
U 8 HOH 227 927  28  HOH HOH A . 
U 8 HOH 228 928  325 HOH HOH A . 
U 8 HOH 229 929  297 HOH HOH A . 
U 8 HOH 230 930  343 HOH HOH A . 
U 8 HOH 231 931  737 HOH HOH A . 
U 8 HOH 232 932  126 HOH HOH A . 
U 8 HOH 233 933  837 HOH HOH A . 
U 8 HOH 234 934  137 HOH HOH A . 
U 8 HOH 235 935  548 HOH HOH A . 
U 8 HOH 236 936  445 HOH HOH A . 
U 8 HOH 237 937  384 HOH HOH A . 
U 8 HOH 238 938  114 HOH HOH A . 
U 8 HOH 239 939  366 HOH HOH A . 
U 8 HOH 240 940  296 HOH HOH A . 
U 8 HOH 241 941  546 HOH HOH A . 
U 8 HOH 242 942  476 HOH HOH A . 
U 8 HOH 243 943  463 HOH HOH A . 
U 8 HOH 244 944  229 HOH HOH A . 
U 8 HOH 245 945  88  HOH HOH A . 
U 8 HOH 246 946  154 HOH HOH A . 
U 8 HOH 247 947  893 HOH HOH A . 
U 8 HOH 248 948  472 HOH HOH A . 
U 8 HOH 249 949  433 HOH HOH A . 
U 8 HOH 250 950  356 HOH HOH A . 
U 8 HOH 251 951  882 HOH HOH A . 
U 8 HOH 252 952  742 HOH HOH A . 
U 8 HOH 253 953  812 HOH HOH A . 
U 8 HOH 254 954  346 HOH HOH A . 
U 8 HOH 255 955  816 HOH HOH A . 
U 8 HOH 256 956  441 HOH HOH A . 
U 8 HOH 257 957  805 HOH HOH A . 
U 8 HOH 258 958  26  HOH HOH A . 
U 8 HOH 259 959  741 HOH HOH A . 
U 8 HOH 260 960  486 HOH HOH A . 
U 8 HOH 261 961  239 HOH HOH A . 
U 8 HOH 262 962  452 HOH HOH A . 
U 8 HOH 263 963  505 HOH HOH A . 
U 8 HOH 264 964  342 HOH HOH A . 
U 8 HOH 265 965  601 HOH HOH A . 
U 8 HOH 266 966  339 HOH HOH A . 
U 8 HOH 267 967  672 HOH HOH A . 
U 8 HOH 268 968  584 HOH HOH A . 
U 8 HOH 269 969  364 HOH HOH A . 
U 8 HOH 270 970  563 HOH HOH A . 
U 8 HOH 271 971  163 HOH HOH A . 
U 8 HOH 272 972  484 HOH HOH A . 
U 8 HOH 273 973  60  HOH HOH A . 
U 8 HOH 274 974  72  HOH HOH A . 
U 8 HOH 275 975  351 HOH HOH A . 
U 8 HOH 276 976  875 HOH HOH A . 
U 8 HOH 277 977  66  HOH HOH A . 
U 8 HOH 278 978  67  HOH HOH A . 
U 8 HOH 279 979  58  HOH HOH A . 
U 8 HOH 280 980  501 HOH HOH A . 
U 8 HOH 281 981  128 HOH HOH A . 
U 8 HOH 282 982  574 HOH HOH A . 
U 8 HOH 283 983  64  HOH HOH A . 
U 8 HOH 284 984  826 HOH HOH A . 
U 8 HOH 285 985  643 HOH HOH A . 
U 8 HOH 286 986  667 HOH HOH A . 
U 8 HOH 287 987  158 HOH HOH A . 
U 8 HOH 288 988  761 HOH HOH A . 
U 8 HOH 289 989  442 HOH HOH A . 
U 8 HOH 290 990  245 HOH HOH A . 
U 8 HOH 291 991  716 HOH HOH A . 
U 8 HOH 292 992  425 HOH HOH A . 
U 8 HOH 293 993  603 HOH HOH A . 
U 8 HOH 294 994  405 HOH HOH A . 
U 8 HOH 295 995  700 HOH HOH A . 
U 8 HOH 296 996  63  HOH HOH A . 
U 8 HOH 297 997  281 HOH HOH A . 
U 8 HOH 298 998  376 HOH HOH A . 
U 8 HOH 299 999  145 HOH HOH A . 
U 8 HOH 300 1000 523 HOH HOH A . 
U 8 HOH 301 1001 232 HOH HOH A . 
U 8 HOH 302 1002 558 HOH HOH A . 
U 8 HOH 303 1003 396 HOH HOH A . 
U 8 HOH 304 1004 55  HOH HOH A . 
U 8 HOH 305 1005 374 HOH HOH A . 
U 8 HOH 306 1006 439 HOH HOH A . 
U 8 HOH 307 1007 750 HOH HOH A . 
U 8 HOH 308 1008 612 HOH HOH A . 
U 8 HOH 309 1009 143 HOH HOH A . 
U 8 HOH 310 1010 668 HOH HOH A . 
U 8 HOH 311 1011 678 HOH HOH A . 
U 8 HOH 312 1012 887 HOH HOH A . 
U 8 HOH 313 1013 71  HOH HOH A . 
U 8 HOH 314 1014 421 HOH HOH A . 
U 8 HOH 315 1015 205 HOH HOH A . 
U 8 HOH 316 1016 165 HOH HOH A . 
U 8 HOH 317 1017 413 HOH HOH A . 
U 8 HOH 318 1018 607 HOH HOH A . 
U 8 HOH 319 1019 423 HOH HOH A . 
U 8 HOH 320 1020 873 HOH HOH A . 
U 8 HOH 321 1021 271 HOH HOH A . 
U 8 HOH 322 1022 82  HOH HOH A . 
U 8 HOH 323 1023 519 HOH HOH A . 
U 8 HOH 324 1024 831 HOH HOH A . 
U 8 HOH 325 1025 540 HOH HOH A . 
U 8 HOH 326 1026 238 HOH HOH A . 
U 8 HOH 327 1027 534 HOH HOH A . 
U 8 HOH 328 1028 817 HOH HOH A . 
U 8 HOH 329 1029 745 HOH HOH A . 
U 8 HOH 330 1030 184 HOH HOH A . 
U 8 HOH 331 1031 808 HOH HOH A . 
U 8 HOH 332 1032 676 HOH HOH A . 
U 8 HOH 333 1033 45  HOH HOH A . 
U 8 HOH 334 1034 727 HOH HOH A . 
U 8 HOH 335 1035 662 HOH HOH A . 
U 8 HOH 336 1036 260 HOH HOH A . 
U 8 HOH 337 1037 714 HOH HOH A . 
U 8 HOH 338 1038 230 HOH HOH A . 
U 8 HOH 339 1039 665 HOH HOH A . 
U 8 HOH 340 1040 397 HOH HOH A . 
U 8 HOH 341 1041 437 HOH HOH A . 
U 8 HOH 342 1042 89  HOH HOH A . 
U 8 HOH 343 1043 3   HOH HOH A . 
U 8 HOH 344 1044 56  HOH HOH A . 
U 8 HOH 345 1045 424 HOH HOH A . 
U 8 HOH 346 1046 514 HOH HOH A . 
U 8 HOH 347 1047 83  HOH HOH A . 
U 8 HOH 348 1048 861 HOH HOH A . 
U 8 HOH 349 1049 241 HOH HOH A . 
U 8 HOH 350 1050 105 HOH HOH A . 
U 8 HOH 351 1051 776 HOH HOH A . 
U 8 HOH 352 1052 798 HOH HOH A . 
U 8 HOH 353 1053 221 HOH HOH A . 
U 8 HOH 354 1054 638 HOH HOH A . 
U 8 HOH 355 1055 440 HOH HOH A . 
U 8 HOH 356 1056 171 HOH HOH A . 
U 8 HOH 357 1057 272 HOH HOH A . 
U 8 HOH 358 1058 743 HOH HOH A . 
U 8 HOH 359 1059 102 HOH HOH A . 
U 8 HOH 360 1060 214 HOH HOH A . 
U 8 HOH 361 1061 800 HOH HOH A . 
U 8 HOH 362 1062 75  HOH HOH A . 
U 8 HOH 363 1063 564 HOH HOH A . 
U 8 HOH 364 1064 828 HOH HOH A . 
U 8 HOH 365 1065 223 HOH HOH A . 
U 8 HOH 366 1066 894 HOH HOH A . 
U 8 HOH 367 1067 852 HOH HOH A . 
U 8 HOH 368 1068 789 HOH HOH A . 
U 8 HOH 369 1069 110 HOH HOH A . 
U 8 HOH 370 1070 220 HOH HOH A . 
U 8 HOH 371 1071 866 HOH HOH A . 
U 8 HOH 372 1072 886 HOH HOH A . 
U 8 HOH 373 1073 90  HOH HOH A . 
U 8 HOH 374 1074 890 HOH HOH A . 
U 8 HOH 375 1075 770 HOH HOH A . 
U 8 HOH 376 1076 669 HOH HOH A . 
U 8 HOH 377 1077 578 HOH HOH A . 
U 8 HOH 378 1078 827 HOH HOH A . 
U 8 HOH 379 1079 795 HOH HOH A . 
U 8 HOH 380 1080 203 HOH HOH A . 
U 8 HOH 381 1081 903 HOH HOH A . 
U 8 HOH 382 1082 37  HOH HOH A . 
U 8 HOH 383 1083 77  HOH HOH A . 
U 8 HOH 384 1084 744 HOH HOH A . 
U 8 HOH 385 1085 51  HOH HOH A . 
U 8 HOH 386 1086 508 HOH HOH A . 
U 8 HOH 387 1087 879 HOH HOH A . 
U 8 HOH 388 1088 172 HOH HOH A . 
U 8 HOH 389 1089 116 HOH HOH A . 
U 8 HOH 390 1090 919 HOH HOH A . 
U 8 HOH 391 1091 633 HOH HOH A . 
U 8 HOH 392 1092 910 HOH HOH A . 
U 8 HOH 393 1093 902 HOH HOH A . 
U 8 HOH 394 1094 810 HOH HOH A . 
U 8 HOH 395 1095 765 HOH HOH A . 
U 8 HOH 396 1096 838 HOH HOH A . 
U 8 HOH 397 1097 897 HOH HOH A . 
U 8 HOH 398 1098 911 HOH HOH A . 
U 8 HOH 399 1099 91  HOH HOH A . 
U 8 HOH 400 1100 694 HOH HOH A . 
U 8 HOH 401 1101 233 HOH HOH A . 
U 8 HOH 402 1102 679 HOH HOH A . 
U 8 HOH 403 1103 500 HOH HOH A . 
U 8 HOH 404 1104 249 HOH HOH A . 
U 8 HOH 405 1105 62  HOH HOH A . 
U 8 HOH 406 1106 849 HOH HOH A . 
U 8 HOH 407 1107 869 HOH HOH A . 
U 8 HOH 408 1108 134 HOH HOH A . 
U 8 HOH 409 1109 898 HOH HOH A . 
U 8 HOH 410 1110 829 HOH HOH A . 
U 8 HOH 411 1111 860 HOH HOH A . 
U 8 HOH 412 1112 244 HOH HOH A . 
U 8 HOH 413 1113 804 HOH HOH A . 
U 8 HOH 414 1114 832 HOH HOH A . 
U 8 HOH 415 1115 109 HOH HOH A . 
U 8 HOH 416 1116 754 HOH HOH A . 
U 8 HOH 417 1117 857 HOH HOH A . 
U 8 HOH 418 1118 252 HOH HOH A . 
U 8 HOH 419 1119 417 HOH HOH A . 
U 8 HOH 420 1120 712 HOH HOH A . 
U 8 HOH 421 1121 851 HOH HOH A . 
U 8 HOH 422 1122 651 HOH HOH A . 
U 8 HOH 423 1123 896 HOH HOH A . 
U 8 HOH 424 1124 775 HOH HOH A . 
U 8 HOH 425 1125 833 HOH HOH A . 
U 8 HOH 426 1126 771 HOH HOH A . 
U 8 HOH 427 1127 724 HOH HOH A . 
U 8 HOH 428 1128 600 HOH HOH A . 
U 8 HOH 429 1129 853 HOH HOH A . 
U 8 HOH 430 1130 706 HOH HOH A . 
U 8 HOH 431 1131 773 HOH HOH A . 
U 8 HOH 432 1132 781 HOH HOH A . 
U 8 HOH 433 1133 769 HOH HOH A . 
U 8 HOH 434 1134 149 HOH HOH A . 
U 8 HOH 435 1135 895 HOH HOH A . 
U 8 HOH 436 1136 863 HOH HOH A . 
U 8 HOH 437 1137 735 HOH HOH A . 
U 8 HOH 438 1138 2   HOH HOH A . 
U 8 HOH 439 1139 490 HOH HOH A . 
U 8 HOH 440 1140 201 HOH HOH A . 
U 8 HOH 441 1141 878 HOH HOH A . 
U 8 HOH 442 1142 793 HOH HOH A . 
U 8 HOH 443 1143 234 HOH HOH A . 
U 8 HOH 444 1144 876 HOH HOH A . 
U 8 HOH 445 1145 148 HOH HOH A . 
U 8 HOH 446 1146 70  HOH HOH A . 
U 8 HOH 447 1147 537 HOH HOH A . 
U 8 HOH 448 1148 188 HOH HOH A . 
U 8 HOH 449 1149 908 HOH HOH A . 
U 8 HOH 450 1150 855 HOH HOH A . 
U 8 HOH 451 1151 904 HOH HOH A . 
V 8 HOH 1   701  680 HOH HOH B . 
V 8 HOH 2   702  877 HOH HOH B . 
V 8 HOH 3   703  43  HOH HOH B . 
V 8 HOH 4   704  774 HOH HOH B . 
V 8 HOH 5   705  18  HOH HOH B . 
V 8 HOH 6   706  161 HOH HOH B . 
V 8 HOH 7   707  268 HOH HOH B . 
V 8 HOH 8   708  253 HOH HOH B . 
V 8 HOH 9   709  9   HOH HOH B . 
V 8 HOH 10  710  834 HOH HOH B . 
V 8 HOH 11  711  617 HOH HOH B . 
V 8 HOH 12  712  768 HOH HOH B . 
V 8 HOH 13  713  782 HOH HOH B . 
V 8 HOH 14  714  670 HOH HOH B . 
V 8 HOH 15  715  626 HOH HOH B . 
V 8 HOH 16  716  570 HOH HOH B . 
V 8 HOH 17  717  68  HOH HOH B . 
V 8 HOH 18  718  178 HOH HOH B . 
V 8 HOH 19  719  406 HOH HOH B . 
V 8 HOH 20  720  822 HOH HOH B . 
V 8 HOH 21  721  785 HOH HOH B . 
V 8 HOH 22  722  624 HOH HOH B . 
V 8 HOH 23  723  889 HOH HOH B . 
V 8 HOH 24  724  32  HOH HOH B . 
V 8 HOH 25  725  692 HOH HOH B . 
V 8 HOH 26  726  12  HOH HOH B . 
V 8 HOH 27  727  604 HOH HOH B . 
V 8 HOH 28  728  17  HOH HOH B . 
V 8 HOH 29  729  464 HOH HOH B . 
V 8 HOH 30  730  242 HOH HOH B . 
V 8 HOH 31  731  730 HOH HOH B . 
V 8 HOH 32  732  222 HOH HOH B . 
V 8 HOH 33  733  20  HOH HOH B . 
V 8 HOH 34  734  125 HOH HOH B . 
V 8 HOH 35  735  273 HOH HOH B . 
V 8 HOH 36  736  762 HOH HOH B . 
V 8 HOH 37  737  93  HOH HOH B . 
V 8 HOH 38  738  640 HOH HOH B . 
V 8 HOH 39  739  103 HOH HOH B . 
V 8 HOH 40  740  858 HOH HOH B . 
V 8 HOH 41  741  888 HOH HOH B . 
V 8 HOH 42  742  198 HOH HOH B . 
V 8 HOH 43  743  622 HOH HOH B . 
V 8 HOH 44  744  286 HOH HOH B . 
V 8 HOH 45  745  569 HOH HOH B . 
V 8 HOH 46  746  636 HOH HOH B . 
V 8 HOH 47  747  288 HOH HOH B . 
V 8 HOH 48  748  377 HOH HOH B . 
V 8 HOH 49  749  370 HOH HOH B . 
V 8 HOH 50  750  8   HOH HOH B . 
V 8 HOH 51  751  122 HOH HOH B . 
V 8 HOH 52  752  228 HOH HOH B . 
V 8 HOH 53  753  411 HOH HOH B . 
V 8 HOH 54  754  543 HOH HOH B . 
V 8 HOH 55  755  274 HOH HOH B . 
V 8 HOH 56  756  426 HOH HOH B . 
V 8 HOH 57  757  783 HOH HOH B . 
V 8 HOH 58  758  497 HOH HOH B . 
V 8 HOH 59  759  196 HOH HOH B . 
V 8 HOH 60  760  739 HOH HOH B . 
V 8 HOH 61  761  468 HOH HOH B . 
V 8 HOH 62  762  380 HOH HOH B . 
V 8 HOH 63  763  618 HOH HOH B . 
V 8 HOH 64  764  605 HOH HOH B . 
V 8 HOH 65  765  871 HOH HOH B . 
V 8 HOH 66  766  427 HOH HOH B . 
V 8 HOH 67  767  224 HOH HOH B . 
V 8 HOH 68  768  412 HOH HOH B . 
V 8 HOH 69  769  302 HOH HOH B . 
V 8 HOH 70  770  717 HOH HOH B . 
V 8 HOH 71  771  565 HOH HOH B . 
V 8 HOH 72  772  79  HOH HOH B . 
V 8 HOH 73  773  308 HOH HOH B . 
V 8 HOH 74  774  457 HOH HOH B . 
V 8 HOH 75  775  129 HOH HOH B . 
V 8 HOH 76  776  900 HOH HOH B . 
V 8 HOH 77  777  915 HOH HOH B . 
V 8 HOH 78  778  606 HOH HOH B . 
V 8 HOH 79  779  133 HOH HOH B . 
V 8 HOH 80  780  96  HOH HOH B . 
V 8 HOH 81  781  7   HOH HOH B . 
V 8 HOH 82  782  306 HOH HOH B . 
V 8 HOH 83  783  74  HOH HOH B . 
V 8 HOH 84  784  721 HOH HOH B . 
V 8 HOH 85  785  740 HOH HOH B . 
V 8 HOH 86  786  422 HOH HOH B . 
V 8 HOH 87  787  393 HOH HOH B . 
V 8 HOH 88  788  823 HOH HOH B . 
V 8 HOH 89  789  369 HOH HOH B . 
V 8 HOH 90  790  140 HOH HOH B . 
V 8 HOH 91  791  707 HOH HOH B . 
V 8 HOH 92  792  435 HOH HOH B . 
V 8 HOH 93  793  458 HOH HOH B . 
V 8 HOH 94  794  554 HOH HOH B . 
V 8 HOH 95  795  567 HOH HOH B . 
V 8 HOH 96  796  580 HOH HOH B . 
V 8 HOH 97  797  503 HOH HOH B . 
V 8 HOH 98  798  315 HOH HOH B . 
V 8 HOH 99  799  330 HOH HOH B . 
V 8 HOH 100 800  432 HOH HOH B . 
V 8 HOH 101 801  637 HOH HOH B . 
V 8 HOH 102 802  674 HOH HOH B . 
V 8 HOH 103 803  335 HOH HOH B . 
V 8 HOH 104 804  474 HOH HOH B . 
V 8 HOH 105 805  361 HOH HOH B . 
V 8 HOH 106 806  471 HOH HOH B . 
V 8 HOH 107 807  16  HOH HOH B . 
V 8 HOH 108 808  589 HOH HOH B . 
V 8 HOH 109 809  212 HOH HOH B . 
V 8 HOH 110 810  50  HOH HOH B . 
V 8 HOH 111 811  811 HOH HOH B . 
V 8 HOH 112 812  294 HOH HOH B . 
V 8 HOH 113 813  664 HOH HOH B . 
V 8 HOH 114 814  162 HOH HOH B . 
V 8 HOH 115 815  736 HOH HOH B . 
V 8 HOH 116 816  431 HOH HOH B . 
V 8 HOH 117 817  382 HOH HOH B . 
V 8 HOH 118 818  841 HOH HOH B . 
V 8 HOH 119 819  459 HOH HOH B . 
V 8 HOH 120 820  136 HOH HOH B . 
V 8 HOH 121 821  663 HOH HOH B . 
V 8 HOH 122 822  511 HOH HOH B . 
V 8 HOH 123 823  263 HOH HOH B . 
V 8 HOH 124 824  489 HOH HOH B . 
V 8 HOH 125 825  210 HOH HOH B . 
V 8 HOH 126 826  341 HOH HOH B . 
V 8 HOH 127 827  275 HOH HOH B . 
V 8 HOH 128 828  155 HOH HOH B . 
V 8 HOH 129 829  305 HOH HOH B . 
V 8 HOH 130 830  311 HOH HOH B . 
V 8 HOH 131 831  298 HOH HOH B . 
V 8 HOH 132 832  359 HOH HOH B . 
V 8 HOH 133 833  357 HOH HOH B . 
V 8 HOH 134 834  30  HOH HOH B . 
V 8 HOH 135 835  139 HOH HOH B . 
V 8 HOH 136 836  556 HOH HOH B . 
V 8 HOH 137 837  216 HOH HOH B . 
V 8 HOH 138 838  572 HOH HOH B . 
V 8 HOH 139 839  645 HOH HOH B . 
V 8 HOH 140 840  190 HOH HOH B . 
V 8 HOH 141 841  675 HOH HOH B . 
V 8 HOH 142 842  408 HOH HOH B . 
V 8 HOH 143 843  591 HOH HOH B . 
V 8 HOH 144 844  646 HOH HOH B . 
V 8 HOH 145 845  416 HOH HOH B . 
V 8 HOH 146 846  450 HOH HOH B . 
V 8 HOH 147 847  407 HOH HOH B . 
V 8 HOH 148 848  763 HOH HOH B . 
V 8 HOH 149 849  487 HOH HOH B . 
V 8 HOH 150 850  283 HOH HOH B . 
V 8 HOH 151 851  792 HOH HOH B . 
V 8 HOH 152 852  568 HOH HOH B . 
V 8 HOH 153 853  332 HOH HOH B . 
V 8 HOH 154 854  358 HOH HOH B . 
V 8 HOH 155 855  360 HOH HOH B . 
V 8 HOH 156 856  581 HOH HOH B . 
V 8 HOH 157 857  150 HOH HOH B . 
V 8 HOH 158 858  243 HOH HOH B . 
V 8 HOH 159 859  594 HOH HOH B . 
V 8 HOH 160 860  61  HOH HOH B . 
V 8 HOH 161 861  661 HOH HOH B . 
V 8 HOH 162 862  293 HOH HOH B . 
V 8 HOH 163 863  170 HOH HOH B . 
V 8 HOH 164 864  693 HOH HOH B . 
V 8 HOH 165 865  573 HOH HOH B . 
V 8 HOH 166 866  350 HOH HOH B . 
V 8 HOH 167 867  300 HOH HOH B . 
V 8 HOH 168 868  323 HOH HOH B . 
V 8 HOH 169 869  729 HOH HOH B . 
V 8 HOH 170 870  336 HOH HOH B . 
V 8 HOH 171 871  326 HOH HOH B . 
V 8 HOH 172 872  85  HOH HOH B . 
V 8 HOH 173 873  641 HOH HOH B . 
V 8 HOH 174 874  764 HOH HOH B . 
V 8 HOH 175 875  495 HOH HOH B . 
V 8 HOH 176 876  446 HOH HOH B . 
V 8 HOH 177 877  94  HOH HOH B . 
V 8 HOH 178 878  608 HOH HOH B . 
V 8 HOH 179 879  479 HOH HOH B . 
V 8 HOH 180 880  596 HOH HOH B . 
V 8 HOH 181 881  498 HOH HOH B . 
V 8 HOH 182 882  135 HOH HOH B . 
V 8 HOH 183 883  334 HOH HOH B . 
V 8 HOH 184 884  544 HOH HOH B . 
V 8 HOH 185 885  379 HOH HOH B . 
V 8 HOH 186 886  348 HOH HOH B . 
V 8 HOH 187 887  84  HOH HOH B . 
V 8 HOH 188 888  33  HOH HOH B . 
V 8 HOH 189 889  39  HOH HOH B . 
V 8 HOH 190 890  404 HOH HOH B . 
V 8 HOH 191 891  388 HOH HOH B . 
V 8 HOH 192 892  485 HOH HOH B . 
V 8 HOH 193 893  918 HOH HOH B . 
V 8 HOH 194 894  529 HOH HOH B . 
V 8 HOH 195 895  550 HOH HOH B . 
V 8 HOH 196 896  48  HOH HOH B . 
V 8 HOH 197 897  235 HOH HOH B . 
V 8 HOH 198 898  515 HOH HOH B . 
V 8 HOH 199 899  120 HOH HOH B . 
V 8 HOH 200 900  279 HOH HOH B . 
V 8 HOH 201 901  35  HOH HOH B . 
V 8 HOH 202 902  144 HOH HOH B . 
V 8 HOH 203 903  541 HOH HOH B . 
V 8 HOH 204 904  282 HOH HOH B . 
V 8 HOH 205 905  99  HOH HOH B . 
V 8 HOH 206 906  13  HOH HOH B . 
V 8 HOH 207 907  269 HOH HOH B . 
V 8 HOH 208 908  371 HOH HOH B . 
V 8 HOH 209 909  226 HOH HOH B . 
V 8 HOH 210 910  231 HOH HOH B . 
V 8 HOH 211 911  349 HOH HOH B . 
V 8 HOH 212 912  338 HOH HOH B . 
V 8 HOH 213 913  699 HOH HOH B . 
V 8 HOH 214 914  590 HOH HOH B . 
V 8 HOH 215 915  389 HOH HOH B . 
V 8 HOH 216 916  292 HOH HOH B . 
V 8 HOH 217 917  483 HOH HOH B . 
V 8 HOH 218 918  518 HOH HOH B . 
V 8 HOH 219 919  839 HOH HOH B . 
V 8 HOH 220 920  905 HOH HOH B . 
V 8 HOH 221 921  41  HOH HOH B . 
V 8 HOH 222 922  353 HOH HOH B . 
V 8 HOH 223 923  658 HOH HOH B . 
V 8 HOH 224 924  790 HOH HOH B . 
V 8 HOH 225 925  331 HOH HOH B . 
V 8 HOH 226 926  352 HOH HOH B . 
V 8 HOH 227 927  698 HOH HOH B . 
V 8 HOH 228 928  106 HOH HOH B . 
V 8 HOH 229 929  777 HOH HOH B . 
V 8 HOH 230 930  87  HOH HOH B . 
V 8 HOH 231 931  65  HOH HOH B . 
V 8 HOH 232 932  499 HOH HOH B . 
V 8 HOH 233 933  240 HOH HOH B . 
V 8 HOH 234 934  719 HOH HOH B . 
V 8 HOH 235 935  491 HOH HOH B . 
V 8 HOH 236 936  285 HOH HOH B . 
V 8 HOH 237 937  434 HOH HOH B . 
V 8 HOH 238 938  539 HOH HOH B . 
V 8 HOH 239 939  248 HOH HOH B . 
V 8 HOH 240 940  373 HOH HOH B . 
V 8 HOH 241 941  303 HOH HOH B . 
V 8 HOH 242 942  702 HOH HOH B . 
V 8 HOH 243 943  202 HOH HOH B . 
V 8 HOH 244 944  320 HOH HOH B . 
V 8 HOH 245 945  399 HOH HOH B . 
V 8 HOH 246 946  454 HOH HOH B . 
V 8 HOH 247 947  846 HOH HOH B . 
V 8 HOH 248 948  616 HOH HOH B . 
V 8 HOH 249 949  307 HOH HOH B . 
V 8 HOH 250 950  390 HOH HOH B . 
V 8 HOH 251 951  597 HOH HOH B . 
V 8 HOH 252 952  705 HOH HOH B . 
V 8 HOH 253 953  131 HOH HOH B . 
V 8 HOH 254 954  462 HOH HOH B . 
V 8 HOH 255 955  708 HOH HOH B . 
V 8 HOH 256 956  381 HOH HOH B . 
V 8 HOH 257 957  843 HOH HOH B . 
V 8 HOH 258 958  631 HOH HOH B . 
V 8 HOH 259 959  683 HOH HOH B . 
V 8 HOH 260 960  794 HOH HOH B . 
V 8 HOH 261 961  677 HOH HOH B . 
V 8 HOH 262 962  157 HOH HOH B . 
V 8 HOH 263 963  649 HOH HOH B . 
V 8 HOH 264 964  659 HOH HOH B . 
V 8 HOH 265 965  547 HOH HOH B . 
V 8 HOH 266 966  383 HOH HOH B . 
V 8 HOH 267 967  25  HOH HOH B . 
V 8 HOH 268 968  80  HOH HOH B . 
V 8 HOH 269 969  329 HOH HOH B . 
V 8 HOH 270 970  506 HOH HOH B . 
V 8 HOH 271 971  759 HOH HOH B . 
V 8 HOH 272 972  287 HOH HOH B . 
V 8 HOH 273 973  328 HOH HOH B . 
V 8 HOH 274 974  577 HOH HOH B . 
V 8 HOH 275 975  347 HOH HOH B . 
V 8 HOH 276 976  787 HOH HOH B . 
V 8 HOH 277 977  695 HOH HOH B . 
V 8 HOH 278 978  494 HOH HOH B . 
V 8 HOH 279 979  621 HOH HOH B . 
V 8 HOH 280 980  461 HOH HOH B . 
V 8 HOH 281 981  733 HOH HOH B . 
V 8 HOH 282 982  138 HOH HOH B . 
V 8 HOH 283 983  475 HOH HOH B . 
V 8 HOH 284 984  112 HOH HOH B . 
V 8 HOH 285 985  625 HOH HOH B . 
V 8 HOH 286 986  527 HOH HOH B . 
V 8 HOH 287 987  392 HOH HOH B . 
V 8 HOH 288 988  551 HOH HOH B . 
V 8 HOH 289 989  444 HOH HOH B . 
V 8 HOH 290 990  258 HOH HOH B . 
V 8 HOH 291 991  237 HOH HOH B . 
V 8 HOH 292 992  270 HOH HOH B . 
V 8 HOH 293 993  456 HOH HOH B . 
V 8 HOH 294 994  455 HOH HOH B . 
V 8 HOH 295 995  507 HOH HOH B . 
V 8 HOH 296 996  749 HOH HOH B . 
V 8 HOH 297 997  14  HOH HOH B . 
V 8 HOH 298 998  738 HOH HOH B . 
V 8 HOH 299 999  73  HOH HOH B . 
V 8 HOH 300 1000 391 HOH HOH B . 
V 8 HOH 301 1001 197 HOH HOH B . 
V 8 HOH 302 1002 19  HOH HOH B . 
V 8 HOH 303 1003 728 HOH HOH B . 
V 8 HOH 304 1004 313 HOH HOH B . 
V 8 HOH 305 1005 593 HOH HOH B . 
V 8 HOH 306 1006 560 HOH HOH B . 
V 8 HOH 307 1007 317 HOH HOH B . 
V 8 HOH 308 1008 246 HOH HOH B . 
V 8 HOH 309 1009 164 HOH HOH B . 
V 8 HOH 310 1010 496 HOH HOH B . 
V 8 HOH 311 1011 156 HOH HOH B . 
V 8 HOH 312 1012 531 HOH HOH B . 
V 8 HOH 313 1013 314 HOH HOH B . 
V 8 HOH 314 1014 521 HOH HOH B . 
V 8 HOH 315 1015 69  HOH HOH B . 
V 8 HOH 316 1016 813 HOH HOH B . 
V 8 HOH 317 1017 856 HOH HOH B . 
V 8 HOH 318 1018 410 HOH HOH B . 
V 8 HOH 319 1019 401 HOH HOH B . 
V 8 HOH 320 1020 180 HOH HOH B . 
V 8 HOH 321 1021 34  HOH HOH B . 
V 8 HOH 322 1022 520 HOH HOH B . 
V 8 HOH 323 1023 635 HOH HOH B . 
V 8 HOH 324 1024 174 HOH HOH B . 
V 8 HOH 325 1025 585 HOH HOH B . 
V 8 HOH 326 1026 881 HOH HOH B . 
V 8 HOH 327 1027 119 HOH HOH B . 
V 8 HOH 328 1028 104 HOH HOH B . 
V 8 HOH 329 1029 107 HOH HOH B . 
V 8 HOH 330 1030 430 HOH HOH B . 
V 8 HOH 331 1031 602 HOH HOH B . 
V 8 HOH 332 1032 609 HOH HOH B . 
V 8 HOH 333 1033 23  HOH HOH B . 
V 8 HOH 334 1034 4   HOH HOH B . 
V 8 HOH 335 1035 130 HOH HOH B . 
V 8 HOH 336 1036 215 HOH HOH B . 
V 8 HOH 337 1037 57  HOH HOH B . 
V 8 HOH 338 1038 825 HOH HOH B . 
V 8 HOH 339 1039 176 HOH HOH B . 
V 8 HOH 340 1040 15  HOH HOH B . 
V 8 HOH 341 1041 194 HOH HOH B . 
V 8 HOH 342 1042 193 HOH HOH B . 
V 8 HOH 343 1043 824 HOH HOH B . 
V 8 HOH 344 1044 711 HOH HOH B . 
V 8 HOH 345 1045 522 HOH HOH B . 
V 8 HOH 346 1046 337 HOH HOH B . 
V 8 HOH 347 1047 247 HOH HOH B . 
V 8 HOH 348 1048 701 HOH HOH B . 
V 8 HOH 349 1049 504 HOH HOH B . 
V 8 HOH 350 1050 211 HOH HOH B . 
V 8 HOH 351 1051 788 HOH HOH B . 
V 8 HOH 352 1052 132 HOH HOH B . 
V 8 HOH 353 1053 757 HOH HOH B . 
V 8 HOH 354 1054 166 HOH HOH B . 
V 8 HOH 355 1055 124 HOH HOH B . 
V 8 HOH 356 1056 760 HOH HOH B . 
V 8 HOH 357 1057 619 HOH HOH B . 
V 8 HOH 358 1058 696 HOH HOH B . 
V 8 HOH 359 1059 909 HOH HOH B . 
V 8 HOH 360 1060 530 HOH HOH B . 
V 8 HOH 361 1061 650 HOH HOH B . 
V 8 HOH 362 1062 840 HOH HOH B . 
V 8 HOH 363 1063 732 HOH HOH B . 
V 8 HOH 364 1064 38  HOH HOH B . 
V 8 HOH 365 1065 681 HOH HOH B . 
V 8 HOH 366 1066 818 HOH HOH B . 
V 8 HOH 367 1067 227 HOH HOH B . 
V 8 HOH 368 1068 493 HOH HOH B . 
V 8 HOH 369 1069 206 HOH HOH B . 
V 8 HOH 370 1070 535 HOH HOH B . 
V 8 HOH 371 1071 704 HOH HOH B . 
V 8 HOH 372 1072 195 HOH HOH B . 
V 8 HOH 373 1073 628 HOH HOH B . 
V 8 HOH 374 1074 251 HOH HOH B . 
V 8 HOH 375 1075 814 HOH HOH B . 
V 8 HOH 376 1076 257 HOH HOH B . 
V 8 HOH 377 1077 723 HOH HOH B . 
V 8 HOH 378 1078 101 HOH HOH B . 
V 8 HOH 379 1079 208 HOH HOH B . 
V 8 HOH 380 1080 872 HOH HOH B . 
V 8 HOH 381 1081 592 HOH HOH B . 
V 8 HOH 382 1082 688 HOH HOH B . 
V 8 HOH 383 1083 264 HOH HOH B . 
V 8 HOH 384 1084 169 HOH HOH B . 
V 8 HOH 385 1085 914 HOH HOH B . 
V 8 HOH 386 1086 117 HOH HOH B . 
V 8 HOH 387 1087 186 HOH HOH B . 
V 8 HOH 388 1088 414 HOH HOH B . 
V 8 HOH 389 1089 465 HOH HOH B . 
V 8 HOH 390 1090 847 HOH HOH B . 
V 8 HOH 391 1091 189 HOH HOH B . 
V 8 HOH 392 1092 470 HOH HOH B . 
V 8 HOH 393 1093 807 HOH HOH B . 
V 8 HOH 394 1094 183 HOH HOH B . 
V 8 HOH 395 1095 685 HOH HOH B . 
V 8 HOH 396 1096 630 HOH HOH B . 
V 8 HOH 397 1097 418 HOH HOH B . 
V 8 HOH 398 1098 217 HOH HOH B . 
V 8 HOH 399 1099 562 HOH HOH B . 
V 8 HOH 400 1100 267 HOH HOH B . 
V 8 HOH 401 1101 912 HOH HOH B . 
V 8 HOH 402 1102 666 HOH HOH B . 
V 8 HOH 403 1103 916 HOH HOH B . 
V 8 HOH 404 1104 709 HOH HOH B . 
V 8 HOH 405 1105 657 HOH HOH B . 
V 8 HOH 406 1106 627 HOH HOH B . 
V 8 HOH 407 1107 167 HOH HOH B . 
V 8 HOH 408 1108 780 HOH HOH B . 
V 8 HOH 409 1109 722 HOH HOH B . 
V 8 HOH 410 1110 848 HOH HOH B . 
V 8 HOH 411 1111 261 HOH HOH B . 
V 8 HOH 412 1112 907 HOH HOH B . 
V 8 HOH 413 1113 854 HOH HOH B . 
V 8 HOH 414 1114 179 HOH HOH B . 
V 8 HOH 415 1115 218 HOH HOH B . 
V 8 HOH 416 1116 634 HOH HOH B . 
V 8 HOH 417 1117 859 HOH HOH B . 
V 8 HOH 418 1118 255 HOH HOH B . 
V 8 HOH 419 1119 802 HOH HOH B . 
V 8 HOH 420 1120 830 HOH HOH B . 
V 8 HOH 421 1121 566 HOH HOH B . 
V 8 HOH 422 1122 766 HOH HOH B . 
V 8 HOH 423 1123 758 HOH HOH B . 
V 8 HOH 424 1124 718 HOH HOH B . 
V 8 HOH 425 1125 870 HOH HOH B . 
V 8 HOH 426 1126 185 HOH HOH B . 
V 8 HOH 427 1127 756 HOH HOH B . 
V 8 HOH 428 1128 796 HOH HOH B . 
V 8 HOH 429 1129 891 HOH HOH B . 
V 8 HOH 430 1130 225 HOH HOH B . 
V 8 HOH 431 1131 819 HOH HOH B . 
V 8 HOH 432 1132 917 HOH HOH B . 
V 8 HOH 433 1133 115 HOH HOH B . 
V 8 HOH 434 1134 868 HOH HOH B . 
V 8 HOH 435 1135 262 HOH HOH B . 
V 8 HOH 436 1136 502 HOH HOH B . 
V 8 HOH 437 1137 874 HOH HOH B . 
V 8 HOH 438 1138 901 HOH HOH B . 
V 8 HOH 439 1139 752 HOH HOH B . 
V 8 HOH 440 1140 582 HOH HOH B . 
V 8 HOH 441 1141 803 HOH HOH B . 
V 8 HOH 442 1142 682 HOH HOH B . 
V 8 HOH 443 1143 899 HOH HOH B . 
V 8 HOH 444 1144 725 HOH HOH B . 
V 8 HOH 445 1145 820 HOH HOH B . 
V 8 HOH 446 1146 610 HOH HOH B . 
V 8 HOH 447 1147 867 HOH HOH B . 
V 8 HOH 448 1148 113 HOH HOH B . 
V 8 HOH 449 1149 836 HOH HOH B . 
V 8 HOH 450 1150 557 HOH HOH B . 
V 8 HOH 451 1151 653 HOH HOH B . 
V 8 HOH 452 1152 576 HOH HOH B . 
V 8 HOH 453 1153 579 HOH HOH B . 
V 8 HOH 454 1154 492 HOH HOH B . 
V 8 HOH 455 1155 864 HOH HOH B . 
V 8 HOH 456 1156 906 HOH HOH B . 
V 8 HOH 457 1157 588 HOH HOH B . 
V 8 HOH 458 1158 98  HOH HOH B . 
V 8 HOH 459 1159 175 HOH HOH B . 
V 8 HOH 460 1160 671 HOH HOH B . 
V 8 HOH 461 1161 42  HOH HOH B . 
V 8 HOH 462 1162 809 HOH HOH B . 
V 8 HOH 463 1163 885 HOH HOH B . 
V 8 HOH 464 1164 835 HOH HOH B . 
V 8 HOH 465 1165 865 HOH HOH B . 
V 8 HOH 466 1166 845 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A MET 1 ? CG ? A MET 1 CG 
2 1 Y 1 A MET 1 ? SD ? A MET 1 SD 
3 1 Y 1 A MET 1 ? CE ? A MET 1 CE 
4 1 Y 1 B MET 1 ? CG ? B MET 1 CG 
5 1 Y 1 B MET 1 ? SD ? B MET 1 SD 
6 1 Y 1 B MET 1 ? CE ? B MET 1 CE 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.9    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S7N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     139.019 
_cell.length_a_esd                 ? 
_cell.length_b                     139.019 
_cell.length_b_esd                 ? 
_cell.length_c                     181.059 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8S7N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 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                   8S7N 
_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             3.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.23 
_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' 
_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    'Condition C4 of the Morpheus screen (Hampton research)' 
_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         2023-01-31 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.999990 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999990 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S7N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               49.20 
_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                                     163464 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.201 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.194 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           107003 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8025 
_reflns_shell.percent_possible_obs                          100.0 
_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                               13.3 
_reflns_shell.pdbx_chi_squared                              0.97 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.9 
_reflns_shell.pdbx_Rrim_I_all                               3.882 
_reflns_shell.pdbx_Rpim_I_all                               1.051 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.388 
_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                                  3.735 
_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]                            0.56 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.56 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.553 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8S7N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             49.20 
_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                     155094 
_refine.ls_number_reflns_R_free                  8262 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15887 
_refine.ls_R_factor_R_free                       0.18397 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15754 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.081 
_refine.pdbx_overall_ESU_R_Free                  0.083 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             2.382 
_refine.overall_SU_ML                            0.067 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        49.20 
_refine_hist.number_atoms_solvent             917 
_refine_hist.number_atoms_total               9330 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8174 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         239 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.013  8641  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  7910  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.705  1.646  11735 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.485  1.577  18228 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.111  5.000  1036  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.607 22.162 444   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.075 15.000 1318  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.499 15.000 52    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  1062  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  9750  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1990  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.047  2.420  4150  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.047  2.419  4149  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.657  3.618  5184  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.656  3.619  5185  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.480  2.805  4491  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.479  2.805  4492  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.981  4.050  6552  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.061  29.819 10256 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.966  29.246 10018 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             599 
_refine_ls_shell.number_reflns_R_work             11336 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.327 
_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   20 
_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                  0.335 
# 
_struct.entry_id                     8S7N 
_struct.title                        'Vanillyl-alcohol dehydrogenase from Marinicaulis flavus: P151L mutant bound to eugenol' 
_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        8S7N 
_struct_keywords.text            'FAD, flavim oxidase, alcohol, enzyme mechanism, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 7 ? 
L N N 3 ? 
M N N 3 ? 
N N N 2 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 5 ? 
T N N 7 ? 
U N N 8 ? 
V N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2S7K3M2_9PROT 
_struct_ref.pdbx_db_accession          A0A2S7K3M2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDPGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8S7N A 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
2 1 8S7N B 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
# 
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 8S7N LEU A 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 1 
2 8S7N LEU B 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13610 ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  33030 ? 
# 
_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,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
_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 SER A 10  ? GLY A 26  ? SER A 10  GLY A 26  1 ? 17 
HELX_P HELX_P2  AA2 THR A 32  ? GLU A 40  ? THR A 32  GLU A 40  5 ? 9  
HELX_P HELX_P3  AA3 SER A 62  ? GLY A 77  ? SER A 62  GLY A 77  1 ? 16 
HELX_P HELX_P4  AA4 SER A 129 ? GLY A 141 ? SER A 129 GLY A 141 1 ? 13 
HELX_P HELX_P5  AA5 SER A 155 ? ASP A 162 ? SER A 155 ASP A 162 1 ? 8  
HELX_P HELX_P6  AA6 HIS A 173 ? ALA A 175 ? HIS A 173 ALA A 175 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 193 ? MET A 197 ? GLY A 193 MET A 197 5 ? 5  
HELX_P HELX_P8  AA8 VAL A 214 ? SER A 219 ? VAL A 214 SER A 219 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 249 ? ASP A 251 ? ASN A 249 ASP A 251 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 252 ? ALA A 266 ? ASP A 252 ALA A 266 1 ? 15 
HELX_P HELX_P11 AB2 LEU A 278 ? ALA A 283 ? LEU A 278 ALA A 283 1 ? 6  
HELX_P HELX_P12 AB3 THR A 287 ? TYR A 291 ? THR A 287 TYR A 291 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 299 ? ASP A 311 ? PRO A 299 ASP A 311 1 ? 13 
HELX_P HELX_P14 AB5 PRO A 324 ? ALA A 340 ? PRO A 324 ALA A 340 1 ? 17 
HELX_P HELX_P15 AB6 PHE A 349 ? ARG A 353 ? PHE A 349 ARG A 353 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 358 ? MET A 367 ? ASP A 358 MET A 367 1 ? 10 
HELX_P HELX_P17 AB8 LEU A 373 ? TRP A 381 ? LEU A 373 TRP A 381 5 ? 9  
HELX_P HELX_P18 AB9 THR A 397 ? TYR A 415 ? THR A 397 TYR A 415 1 ? 19 
HELX_P HELX_P19 AC1 ASP A 442 ? GLU A 463 ? ASP A 442 GLU A 463 1 ? 22 
HELX_P HELX_P20 AC2 HIS A 471 ? ARG A 473 ? HIS A 471 ARG A 473 5 ? 3  
HELX_P HELX_P21 AC3 TYR A 474 ? TYR A 482 ? TYR A 474 TYR A 482 1 ? 9  
HELX_P HELX_P22 AC4 SER A 483 ? ASP A 501 ? SER A 483 ASP A 501 1 ? 19 
HELX_P HELX_P23 AC5 GLY A 509 ? ILE A 513 ? GLY A 509 ILE A 513 5 ? 5  
HELX_P HELX_P24 AC6 SER B 10  ? GLY B 26  ? SER B 10  GLY B 26  1 ? 17 
HELX_P HELX_P25 AC7 GLU B 33  ? GLU B 40  ? GLU B 33  GLU B 40  5 ? 8  
HELX_P HELX_P26 AC8 SER B 62  ? GLY B 77  ? SER B 62  GLY B 77  1 ? 16 
HELX_P HELX_P27 AC9 SER B 129 ? LYS B 140 ? SER B 129 LYS B 140 1 ? 12 
HELX_P HELX_P28 AD1 SER B 155 ? ASP B 162 ? SER B 155 ASP B 162 1 ? 8  
HELX_P HELX_P29 AD2 HIS B 173 ? ALA B 175 ? HIS B 173 ALA B 175 5 ? 3  
HELX_P HELX_P30 AD3 GLY B 193 ? MET B 197 ? GLY B 193 MET B 197 5 ? 5  
HELX_P HELX_P31 AD4 VAL B 214 ? SER B 219 ? VAL B 214 SER B 219 5 ? 6  
HELX_P HELX_P32 AD5 ASN B 249 ? ASP B 251 ? ASN B 249 ASP B 251 5 ? 3  
HELX_P HELX_P33 AD6 ASP B 252 ? ALA B 266 ? ASP B 252 ALA B 266 1 ? 15 
HELX_P HELX_P34 AD7 LEU B 278 ? ALA B 283 ? LEU B 278 ALA B 283 1 ? 6  
HELX_P HELX_P35 AD8 THR B 287 ? TYR B 291 ? THR B 287 TYR B 291 5 ? 5  
HELX_P HELX_P36 AD9 PRO B 299 ? ASP B 311 ? PRO B 299 ASP B 311 1 ? 13 
HELX_P HELX_P37 AE1 PRO B 324 ? ALA B 340 ? PRO B 324 ALA B 340 1 ? 17 
HELX_P HELX_P38 AE2 PHE B 349 ? ARG B 353 ? PHE B 349 ARG B 353 5 ? 5  
HELX_P HELX_P39 AE3 ASP B 358 ? MET B 367 ? ASP B 358 MET B 367 1 ? 10 
HELX_P HELX_P40 AE4 LEU B 373 ? TRP B 381 ? LEU B 373 TRP B 381 5 ? 9  
HELX_P HELX_P41 AE5 THR B 397 ? TYR B 415 ? THR B 397 TYR B 415 1 ? 19 
HELX_P HELX_P42 AE6 ASP B 442 ? GLU B 463 ? ASP B 442 GLU B 463 1 ? 22 
HELX_P HELX_P43 AE7 HIS B 471 ? ARG B 473 ? HIS B 471 ARG B 473 5 ? 3  
HELX_P HELX_P44 AE8 TYR B 474 ? LYS B 480 ? TYR B 474 LYS B 480 1 ? 7  
HELX_P HELX_P45 AE9 SER B 483 ? ASP B 501 ? SER B 483 ASP B 501 1 ? 19 
HELX_P HELX_P46 AF1 GLY B 509 ? ILE B 513 ? GLY B 509 ILE B 513 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A HIS 387 NE2 ? ? ? 1_555 C FAD . C8M ? ? A HIS 387 A FAD 601 1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale2 covale none ? B HIS 387 NE2 ? ? ? 1_555 N FAD . C8M ? ? B HIS 387 B FAD 602 1_555 ? ? ? ? ? ? ? 1.419 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 FAD C . ? HIS A 387 ? FAD A 601 ? 1_555 HIS A 387 ? 1_555 C8M NE2 HIS 4 FAD None Flavin 
2 FAD N . ? HIS B 387 ? FAD B 602 ? 1_555 HIS B 387 ? 1_555 C8M NE2 HIS 4 FAD None Flavin 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? 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 VAL A 30  ? PHE A 31  ? VAL A 30  PHE A 31  
AA1 2 ALA A 56  ? VAL A 58  ? ALA A 56  VAL A 58  
AA1 3 VAL A 102 ? ASP A 105 ? VAL A 102 ASP A 105 
AA1 4 LEU A 80  ? VAL A 83  ? LEU A 80  VAL A 83  
AA2 1 ILE A 112 ? ASN A 116 ? ILE A 112 ASN A 116 
AA2 2 TYR A 121 ? VAL A 124 ? TYR A 121 VAL A 124 
AA2 3 VAL A 225 ? TRP A 232 ? VAL A 225 TRP A 232 
AA2 4 GLN A 177 ? VAL A 183 ? GLN A 177 VAL A 183 
AA2 5 VAL A 189 ? ARG A 191 ? VAL A 189 ARG A 191 
AA3 1 LEU A 144 ? TRP A 145 ? LEU A 144 TRP A 145 
AA3 2 MET A 234 ? PRO A 235 ? MET A 234 PRO A 235 
AA4 1 LYS A 346 ? TYR A 348 ? LYS A 346 TYR A 348 
AA4 2 TYR A 240 ? PHE A 247 ? TYR A 240 PHE A 247 
AA4 3 TRP A 315 ? TYR A 322 ? TRP A 315 TYR A 322 
AA4 4 THR A 274 ? SER A 277 ? THR A 274 SER A 277 
AA4 5 GLY A 421 ? ILE A 425 ? GLY A 421 ILE A 425 
AA4 6 ASP A 429 ? TYR A 438 ? ASP A 429 TYR A 438 
AA4 7 GLY A 386 ? PHE A 390 ? GLY A 386 PHE A 390 
AA5 1 LYS A 346 ? TYR A 348 ? LYS A 346 TYR A 348 
AA5 2 TYR A 240 ? PHE A 247 ? TYR A 240 PHE A 247 
AA5 3 TRP A 315 ? TYR A 322 ? TRP A 315 TYR A 322 
AA5 4 THR A 274 ? SER A 277 ? THR A 274 SER A 277 
AA5 5 GLY A 421 ? ILE A 425 ? GLY A 421 ILE A 425 
AA5 6 ASP A 429 ? TYR A 438 ? ASP A 429 TYR A 438 
AA5 7 VAL A 393 ? PRO A 395 ? VAL A 393 PRO A 395 
AA6 1 VAL B 30  ? PHE B 31  ? VAL B 30  PHE B 31  
AA6 2 ALA B 56  ? VAL B 58  ? ALA B 56  VAL B 58  
AA6 3 VAL B 102 ? ASP B 105 ? VAL B 102 ASP B 105 
AA6 4 LEU B 80  ? VAL B 83  ? LEU B 80  VAL B 83  
AA7 1 ILE B 112 ? ASN B 116 ? ILE B 112 ASN B 116 
AA7 2 TYR B 121 ? VAL B 124 ? TYR B 121 VAL B 124 
AA7 3 VAL B 225 ? TRP B 232 ? VAL B 225 TRP B 232 
AA7 4 GLN B 177 ? VAL B 183 ? GLN B 177 VAL B 183 
AA7 5 VAL B 189 ? ARG B 191 ? VAL B 189 ARG B 191 
AA8 1 LEU B 144 ? TRP B 145 ? LEU B 144 TRP B 145 
AA8 2 MET B 234 ? PRO B 235 ? MET B 234 PRO B 235 
AA9 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AA9 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AA9 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AA9 4 THR B 274 ? SER B 277 ? THR B 274 SER B 277 
AA9 5 GLY B 421 ? ILE B 425 ? GLY B 421 ILE B 425 
AA9 6 ASP B 429 ? TYR B 438 ? ASP B 429 TYR B 438 
AA9 7 GLY B 386 ? PHE B 390 ? GLY B 386 PHE B 390 
AB1 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AB1 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AB1 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AB1 4 THR B 274 ? SER B 277 ? THR B 274 SER B 277 
AB1 5 GLY B 421 ? ILE B 425 ? GLY B 421 ILE B 425 
AB1 6 ASP B 429 ? TYR B 438 ? ASP B 429 TYR B 438 
AB1 7 VAL B 393 ? PRO B 395 ? VAL B 393 PRO B 395 
# 
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 PHE A 31  ? N PHE A 31  O ALA A 57  ? O ALA A 57  
AA1 2 3 N VAL A 58  ? N VAL A 58  O ASP A 105 ? O ASP A 105 
AA1 3 4 O LEU A 104 ? O LEU A 104 N VAL A 83  ? N VAL A 83  
AA2 1 2 N ASN A 116 ? N ASN A 116 O TYR A 121 ? O TYR A 121 
AA2 2 3 N ALA A 122 ? N ALA A 122 O ILE A 231 ? O ILE A 231 
AA2 3 4 O VAL A 225 ? O VAL A 225 N VAL A 183 ? N VAL A 183 
AA2 4 5 N VAL A 182 ? N VAL A 182 O VAL A 190 ? O VAL A 190 
AA3 1 2 N TRP A 145 ? N TRP A 145 O MET A 234 ? O MET A 234 
AA4 1 2 O LYS A 346 ? O LYS A 346 N THR A 246 ? N THR A 246 
AA4 2 3 N ILE A 245 ? N ILE A 245 O PHE A 317 ? O PHE A 317 
AA4 3 4 O ASN A 316 ? O ASN A 316 N ARG A 276 ? N ARG A 276 
AA4 4 5 N VAL A 275 ? N VAL A 275 O LEU A 423 ? O LEU A 423 
AA4 5 6 N ALA A 424 ? N ALA A 424 O HIS A 431 ? O HIS A 431 
AA4 6 7 O THR A 434 ? O THR A 434 N PHE A 390 ? N PHE A 390 
AA5 1 2 O LYS A 346 ? O LYS A 346 N THR A 246 ? N THR A 246 
AA5 2 3 N ILE A 245 ? N ILE A 245 O PHE A 317 ? O PHE A 317 
AA5 3 4 O ASN A 316 ? O ASN A 316 N ARG A 276 ? N ARG A 276 
AA5 4 5 N VAL A 275 ? N VAL A 275 O LEU A 423 ? O LEU A 423 
AA5 5 6 N ALA A 424 ? N ALA A 424 O HIS A 431 ? O HIS A 431 
AA5 6 7 O LEU A 430 ? O LEU A 430 N SER A 394 ? N SER A 394 
AA6 1 2 N PHE B 31  ? N PHE B 31  O ALA B 57  ? O ALA B 57  
AA6 2 3 N VAL B 58  ? N VAL B 58  O ASP B 105 ? O ASP B 105 
AA6 3 4 O LEU B 104 ? O LEU B 104 N VAL B 83  ? N VAL B 83  
AA7 1 2 N ASN B 116 ? N ASN B 116 O TYR B 121 ? O TYR B 121 
AA7 2 3 N VAL B 124 ? N VAL B 124 O MET B 229 ? O MET B 229 
AA7 3 4 O VAL B 225 ? O VAL B 225 N VAL B 183 ? N VAL B 183 
AA7 4 5 N VAL B 182 ? N VAL B 182 O VAL B 190 ? O VAL B 190 
AA8 1 2 N TRP B 145 ? N TRP B 145 O MET B 234 ? O MET B 234 
AA9 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AA9 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AA9 3 4 O CYS B 318 ? O CYS B 318 N THR B 274 ? N THR B 274 
AA9 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AA9 5 6 N ALA B 424 ? N ALA B 424 O HIS B 431 ? O HIS B 431 
AA9 6 7 O THR B 434 ? O THR B 434 N PHE B 390 ? N PHE B 390 
AB1 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AB1 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AB1 3 4 O CYS B 318 ? O CYS B 318 N THR B 274 ? N THR B 274 
AB1 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AB1 5 6 N ALA B 424 ? N ALA B 424 O HIS B 431 ? O HIS B 431 
AB1 6 7 O LEU B 430 ? O LEU B 430 N SER B 394 ? N SER B 394 
# 
_pdbx_entry_details.entry_id                   8S7N 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             463 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             463 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.171 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.081 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 111 ? ? CZ B ARG 111 ? ? NH1 B ARG 111 ? ? 123.33 120.30 3.03 0.50 N 
2 1 NE B ARG 363 ? ? CZ B ARG 363 ? ? NH1 B ARG 363 ? ? 123.58 120.30 3.28 0.50 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 33  ? ? 48.87   -119.95 
2  1 TYR A 43  ? ? -114.78 70.69   
3  1 LYS A 87  ? ? -99.50  36.02   
4  1 ASN A 88  ? ? -81.30  46.99   
5  1 ALA A 90  ? ? 86.02   -5.99   
6  1 ALA A 273 ? ? -59.97  172.73  
7  1 TYR A 482 ? ? -92.09  54.10   
8  1 ALA A 507 ? ? 39.69   61.60   
9  1 GLU B 33  ? ? -132.71 -87.33  
10 1 TYR B 43  ? ? -112.35 73.11   
11 1 ILE B 45  ? ? -121.10 -52.63  
12 1 LYS B 87  ? ? -96.92  30.32   
13 1 ALA B 90  ? ? 84.02   -7.63   
14 1 GLN B 220 ? ? 38.25   51.90   
15 1 TYR B 482 ? ? -93.87  57.60   
16 1 ALA B 507 ? ? 39.31   59.09   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLY A 166 ? ? TYR A 167 ? ? -145.66 
2 1 GLY B 166 ? ? TYR B 167 ? ? -149.49 
# 
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 ? B HOH 1165 ? 5.82 . 
2 1 O ? B HOH 1166 ? 6.01 . 
# 
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 LYS 520 ? A LYS 520 
2 1 Y 1 A ALA 521 ? A ALA 521 
3 1 Y 1 B LYS 520 ? B LYS 520 
4 1 Y 1 B ALA 521 ? B ALA 521 
# 
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 
1PE OH2    O N N 1   
1PE C12    C N N 2   
1PE C22    C N N 3   
1PE OH3    O N N 4   
1PE C13    C N N 5   
1PE C23    C N N 6   
1PE OH4    O N N 7   
1PE C14    C N N 8   
1PE C24    C N N 9   
1PE OH5    O N N 10  
1PE C15    C N N 11  
1PE C25    C N N 12  
1PE OH6    O N N 13  
1PE C16    C N N 14  
1PE C26    C N N 15  
1PE OH7    O N N 16  
1PE HO2    H N N 17  
1PE H121   H N N 18  
1PE H122   H N N 19  
1PE H221   H N N 20  
1PE H222   H N N 21  
1PE H131   H N N 22  
1PE H132   H N N 23  
1PE H231   H N N 24  
1PE H232   H N N 25  
1PE H141   H N N 26  
1PE H142   H N N 27  
1PE H241   H N N 28  
1PE H242   H N N 29  
1PE H151   H N N 30  
1PE H152   H N N 31  
1PE H251   H N N 32  
1PE H252   H N N 33  
1PE H161   H N N 34  
1PE H162   H N N 35  
1PE H261   H N N 36  
1PE H262   H N N 37  
1PE HO7    H N N 38  
ALA N      N N N 39  
ALA CA     C N S 40  
ALA C      C N N 41  
ALA O      O N N 42  
ALA CB     C N N 43  
ALA OXT    O N N 44  
ALA H      H N N 45  
ALA H2     H N N 46  
ALA HA     H N N 47  
ALA HB1    H N N 48  
ALA HB2    H N N 49  
ALA HB3    H N N 50  
ALA HXT    H N N 51  
ARG N      N N N 52  
ARG CA     C N S 53  
ARG C      C N N 54  
ARG O      O N N 55  
ARG CB     C N N 56  
ARG CG     C N N 57  
ARG CD     C N N 58  
ARG NE     N N N 59  
ARG CZ     C N N 60  
ARG NH1    N N N 61  
ARG NH2    N N N 62  
ARG OXT    O N N 63  
ARG H      H N N 64  
ARG H2     H N N 65  
ARG HA     H N N 66  
ARG HB2    H N N 67  
ARG HB3    H N N 68  
ARG HG2    H N N 69  
ARG HG3    H N N 70  
ARG HD2    H N N 71  
ARG HD3    H N N 72  
ARG HE     H N N 73  
ARG HH11   H N N 74  
ARG HH12   H N N 75  
ARG HH21   H N N 76  
ARG HH22   H N N 77  
ARG HXT    H N N 78  
ASN N      N N N 79  
ASN CA     C N S 80  
ASN C      C N N 81  
ASN O      O N N 82  
ASN CB     C N N 83  
ASN CG     C N N 84  
ASN OD1    O N N 85  
ASN ND2    N N N 86  
ASN OXT    O N N 87  
ASN H      H N N 88  
ASN H2     H N N 89  
ASN HA     H N N 90  
ASN HB2    H N N 91  
ASN HB3    H N N 92  
ASN HD21   H N N 93  
ASN HD22   H N N 94  
ASN HXT    H N N 95  
ASP N      N N N 96  
ASP CA     C N S 97  
ASP C      C N N 98  
ASP O      O N N 99  
ASP CB     C N N 100 
ASP CG     C N N 101 
ASP OD1    O N N 102 
ASP OD2    O N N 103 
ASP OXT    O N N 104 
ASP H      H N N 105 
ASP H2     H N N 106 
ASP HA     H N N 107 
ASP HB2    H N N 108 
ASP HB3    H N N 109 
ASP HD2    H N N 110 
ASP HXT    H N N 111 
CYS N      N N N 112 
CYS CA     C N R 113 
CYS C      C N N 114 
CYS O      O N N 115 
CYS CB     C N N 116 
CYS SG     S N N 117 
CYS OXT    O N N 118 
CYS H      H N N 119 
CYS H2     H N N 120 
CYS HA     H N N 121 
CYS HB2    H N N 122 
CYS HB3    H N N 123 
CYS HG     H N N 124 
CYS HXT    H N N 125 
EOL C1     C Y N 126 
EOL O1     O N N 127 
EOL C2     C Y N 128 
EOL O2     O N N 129 
EOL C3     C Y N 130 
EOL C4     C Y N 131 
EOL C5     C Y N 132 
EOL C6     C Y N 133 
EOL C7     C N N 134 
EOL C8     C N N 135 
EOL C9     C N N 136 
EOL C10    C N N 137 
EOL H1     H N N 138 
EOL HO1    H N N 139 
EOL H4     H N N 140 
EOL H6     H N N 141 
EOL H7     H N N 142 
EOL H7A    H N N 143 
EOL H8     H N N 144 
EOL H9     H N N 145 
EOL H9A    H N N 146 
EOL H10    H N N 147 
EOL H10A   H N N 148 
EOL H10B   H N N 149 
FAD PA     P N R 150 
FAD O1A    O N N 151 
FAD O2A    O N N 152 
FAD O5B    O N N 153 
FAD C5B    C N N 154 
FAD C4B    C N R 155 
FAD O4B    O N N 156 
FAD C3B    C N S 157 
FAD O3B    O N N 158 
FAD C2B    C N R 159 
FAD O2B    O N N 160 
FAD C1B    C N R 161 
FAD N9A    N Y N 162 
FAD C8A    C Y N 163 
FAD N7A    N Y N 164 
FAD C5A    C Y N 165 
FAD C6A    C Y N 166 
FAD N6A    N N N 167 
FAD N1A    N Y N 168 
FAD C2A    C Y N 169 
FAD N3A    N Y N 170 
FAD C4A    C Y N 171 
FAD N1     N N N 172 
FAD C2     C N N 173 
FAD O2     O N N 174 
FAD N3     N N N 175 
FAD C4     C N N 176 
FAD O4     O N N 177 
FAD C4X    C N N 178 
FAD N5     N N N 179 
FAD C5X    C Y N 180 
FAD C6     C Y N 181 
FAD C7     C Y N 182 
FAD C7M    C N N 183 
FAD C8     C Y N 184 
FAD C8M    C N N 185 
FAD C9     C Y N 186 
FAD C9A    C Y N 187 
FAD N10    N N N 188 
FAD C10    C N N 189 
FAD "C1'"  C N N 190 
FAD "C2'"  C N S 191 
FAD "O2'"  O N N 192 
FAD "C3'"  C N S 193 
FAD "O3'"  O N N 194 
FAD "C4'"  C N R 195 
FAD "O4'"  O N N 196 
FAD "C5'"  C N N 197 
FAD "O5'"  O N N 198 
FAD P      P N R 199 
FAD O1P    O N N 200 
FAD O2P    O N N 201 
FAD O3P    O N N 202 
FAD HOA2   H N N 203 
FAD H51A   H N N 204 
FAD H52A   H N N 205 
FAD H4B    H N N 206 
FAD H3B    H N N 207 
FAD HO3A   H N N 208 
FAD H2B    H N N 209 
FAD HO2A   H N N 210 
FAD H1B    H N N 211 
FAD H8A    H N N 212 
FAD H61A   H N N 213 
FAD H62A   H N N 214 
FAD H2A    H N N 215 
FAD HN3    H N N 216 
FAD H6     H N N 217 
FAD HM71   H N N 218 
FAD HM72   H N N 219 
FAD HM73   H N N 220 
FAD HM81   H N N 221 
FAD HM82   H N N 222 
FAD HM83   H N N 223 
FAD H9     H N N 224 
FAD "H1'1" H N N 225 
FAD "H1'2" H N N 226 
FAD "H2'"  H N N 227 
FAD "HO2'" H N N 228 
FAD "H3'"  H N N 229 
FAD "HO3'" H N N 230 
FAD "H4'"  H N N 231 
FAD "HO4'" H N N 232 
FAD "H5'1" H N N 233 
FAD "H5'2" H N N 234 
FAD HOP2   H N N 235 
GLN N      N N N 236 
GLN CA     C N S 237 
GLN C      C N N 238 
GLN O      O N N 239 
GLN CB     C N N 240 
GLN CG     C N N 241 
GLN CD     C N N 242 
GLN OE1    O N N 243 
GLN NE2    N N N 244 
GLN OXT    O N N 245 
GLN H      H N N 246 
GLN H2     H N N 247 
GLN HA     H N N 248 
GLN HB2    H N N 249 
GLN HB3    H N N 250 
GLN HG2    H N N 251 
GLN HG3    H N N 252 
GLN HE21   H N N 253 
GLN HE22   H N N 254 
GLN HXT    H N N 255 
GLU N      N N N 256 
GLU CA     C N S 257 
GLU C      C N N 258 
GLU O      O N N 259 
GLU CB     C N N 260 
GLU CG     C N N 261 
GLU CD     C N N 262 
GLU OE1    O N N 263 
GLU OE2    O N N 264 
GLU OXT    O N N 265 
GLU H      H N N 266 
GLU H2     H N N 267 
GLU HA     H N N 268 
GLU HB2    H N N 269 
GLU HB3    H N N 270 
GLU HG2    H N N 271 
GLU HG3    H N N 272 
GLU HE2    H N N 273 
GLU HXT    H N N 274 
GLY N      N N N 275 
GLY CA     C N N 276 
GLY C      C N N 277 
GLY O      O N N 278 
GLY OXT    O N N 279 
GLY H      H N N 280 
GLY H2     H N N 281 
GLY HA2    H N N 282 
GLY HA3    H N N 283 
GLY HXT    H N N 284 
HIS N      N N N 285 
HIS CA     C N S 286 
HIS C      C N N 287 
HIS O      O N N 288 
HIS CB     C N N 289 
HIS CG     C Y N 290 
HIS ND1    N Y N 291 
HIS CD2    C Y N 292 
HIS CE1    C Y N 293 
HIS NE2    N Y N 294 
HIS OXT    O N N 295 
HIS H      H N N 296 
HIS H2     H N N 297 
HIS HA     H N N 298 
HIS HB2    H N N 299 
HIS HB3    H N N 300 
HIS HD1    H N N 301 
HIS HD2    H N N 302 
HIS HE1    H N N 303 
HIS HE2    H N N 304 
HIS HXT    H N N 305 
HOH O      O N N 306 
HOH H1     H N N 307 
HOH H2     H N N 308 
ILE N      N N N 309 
ILE CA     C N S 310 
ILE C      C N N 311 
ILE O      O N N 312 
ILE CB     C N S 313 
ILE CG1    C N N 314 
ILE CG2    C N N 315 
ILE CD1    C N N 316 
ILE OXT    O N N 317 
ILE H      H N N 318 
ILE H2     H N N 319 
ILE HA     H N N 320 
ILE HB     H N N 321 
ILE HG12   H N N 322 
ILE HG13   H N N 323 
ILE HG21   H N N 324 
ILE HG22   H N N 325 
ILE HG23   H N N 326 
ILE HD11   H N N 327 
ILE HD12   H N N 328 
ILE HD13   H N N 329 
ILE HXT    H N N 330 
LEU N      N N N 331 
LEU CA     C N S 332 
LEU C      C N N 333 
LEU O      O N N 334 
LEU CB     C N N 335 
LEU CG     C N N 336 
LEU CD1    C N N 337 
LEU CD2    C N N 338 
LEU OXT    O N N 339 
LEU H      H N N 340 
LEU H2     H N N 341 
LEU HA     H N N 342 
LEU HB2    H N N 343 
LEU HB3    H N N 344 
LEU HG     H N N 345 
LEU HD11   H N N 346 
LEU HD12   H N N 347 
LEU HD13   H N N 348 
LEU HD21   H N N 349 
LEU HD22   H N N 350 
LEU HD23   H N N 351 
LEU HXT    H N N 352 
LYS N      N N N 353 
LYS CA     C N S 354 
LYS C      C N N 355 
LYS O      O N N 356 
LYS CB     C N N 357 
LYS CG     C N N 358 
LYS CD     C N N 359 
LYS CE     C N N 360 
LYS NZ     N N N 361 
LYS OXT    O N N 362 
LYS H      H N N 363 
LYS H2     H N N 364 
LYS HA     H N N 365 
LYS HB2    H N N 366 
LYS HB3    H N N 367 
LYS HG2    H N N 368 
LYS HG3    H N N 369 
LYS HD2    H N N 370 
LYS HD3    H N N 371 
LYS HE2    H N N 372 
LYS HE3    H N N 373 
LYS HZ1    H N N 374 
LYS HZ2    H N N 375 
LYS HZ3    H N N 376 
LYS HXT    H N N 377 
MET N      N N N 378 
MET CA     C N S 379 
MET C      C N N 380 
MET O      O N N 381 
MET CB     C N N 382 
MET CG     C N N 383 
MET SD     S N N 384 
MET CE     C N N 385 
MET OXT    O N N 386 
MET H      H N N 387 
MET H2     H N N 388 
MET HA     H N N 389 
MET HB2    H N N 390 
MET HB3    H N N 391 
MET HG2    H N N 392 
MET HG3    H N N 393 
MET HE1    H N N 394 
MET HE2    H N N 395 
MET HE3    H N N 396 
MET HXT    H N N 397 
NO3 N      N N N 398 
NO3 O1     O N N 399 
NO3 O2     O N N 400 
NO3 O3     O N N 401 
PE4 O1     O N N 402 
PE4 C1     C N N 403 
PE4 C2     C N N 404 
PE4 O2     O N N 405 
PE4 C3     C N N 406 
PE4 C4     C N N 407 
PE4 O3     O N N 408 
PE4 C5     C N N 409 
PE4 C6     C N N 410 
PE4 O4     O N N 411 
PE4 C7     C N N 412 
PE4 C8     C N N 413 
PE4 O5     O N N 414 
PE4 C9     C N N 415 
PE4 C10    C N N 416 
PE4 O6     O N N 417 
PE4 C11    C N N 418 
PE4 C12    C N N 419 
PE4 O7     O N N 420 
PE4 C13    C N N 421 
PE4 C14    C N N 422 
PE4 O8     O N N 423 
PE4 C15    C N N 424 
PE4 C16    C N N 425 
PE4 HO1    H N N 426 
PE4 H11    H N N 427 
PE4 H12    H N N 428 
PE4 H21    H N N 429 
PE4 H22    H N N 430 
PE4 H31    H N N 431 
PE4 H32    H N N 432 
PE4 H41    H N N 433 
PE4 H42    H N N 434 
PE4 H51    H N N 435 
PE4 H52    H N N 436 
PE4 H61    H N N 437 
PE4 H62    H N N 438 
PE4 H71    H N N 439 
PE4 H72    H N N 440 
PE4 H81    H N N 441 
PE4 H82    H N N 442 
PE4 H91    H N N 443 
PE4 H92    H N N 444 
PE4 H101   H N N 445 
PE4 H102   H N N 446 
PE4 H111   H N N 447 
PE4 H112   H N N 448 
PE4 H121   H N N 449 
PE4 H122   H N N 450 
PE4 H131   H N N 451 
PE4 H132   H N N 452 
PE4 H141   H N N 453 
PE4 H142   H N N 454 
PE4 H151   H N N 455 
PE4 H152   H N N 456 
PE4 H161   H N N 457 
PE4 H162   H N N 458 
PE4 H163   H N N 459 
PEG C1     C N N 460 
PEG O1     O N N 461 
PEG C2     C N N 462 
PEG O2     O N N 463 
PEG C3     C N N 464 
PEG C4     C N N 465 
PEG O4     O N N 466 
PEG H11    H N N 467 
PEG H12    H N N 468 
PEG HO1    H N N 469 
PEG H21    H N N 470 
PEG H22    H N N 471 
PEG H31    H N N 472 
PEG H32    H N N 473 
PEG H41    H N N 474 
PEG H42    H N N 475 
PEG HO4    H N N 476 
PHE N      N N N 477 
PHE CA     C N S 478 
PHE C      C N N 479 
PHE O      O N N 480 
PHE CB     C N N 481 
PHE CG     C Y N 482 
PHE CD1    C Y N 483 
PHE CD2    C Y N 484 
PHE CE1    C Y N 485 
PHE CE2    C Y N 486 
PHE CZ     C Y N 487 
PHE OXT    O N N 488 
PHE H      H N N 489 
PHE H2     H N N 490 
PHE HA     H N N 491 
PHE HB2    H N N 492 
PHE HB3    H N N 493 
PHE HD1    H N N 494 
PHE HD2    H N N 495 
PHE HE1    H N N 496 
PHE HE2    H N N 497 
PHE HZ     H N N 498 
PHE HXT    H N N 499 
PRO N      N N N 500 
PRO CA     C N S 501 
PRO C      C N N 502 
PRO O      O N N 503 
PRO CB     C N N 504 
PRO CG     C N N 505 
PRO CD     C N N 506 
PRO OXT    O N N 507 
PRO H      H N N 508 
PRO HA     H N N 509 
PRO HB2    H N N 510 
PRO HB3    H N N 511 
PRO HG2    H N N 512 
PRO HG3    H N N 513 
PRO HD2    H N N 514 
PRO HD3    H N N 515 
PRO HXT    H N N 516 
SER N      N N N 517 
SER CA     C N S 518 
SER C      C N N 519 
SER O      O N N 520 
SER CB     C N N 521 
SER OG     O N N 522 
SER OXT    O N N 523 
SER H      H N N 524 
SER H2     H N N 525 
SER HA     H N N 526 
SER HB2    H N N 527 
SER HB3    H N N 528 
SER HG     H N N 529 
SER HXT    H N N 530 
THR N      N N N 531 
THR CA     C N S 532 
THR C      C N N 533 
THR O      O N N 534 
THR CB     C N R 535 
THR OG1    O N N 536 
THR CG2    C N N 537 
THR OXT    O N N 538 
THR H      H N N 539 
THR H2     H N N 540 
THR HA     H N N 541 
THR HB     H N N 542 
THR HG1    H N N 543 
THR HG21   H N N 544 
THR HG22   H N N 545 
THR HG23   H N N 546 
THR HXT    H N N 547 
TRP N      N N N 548 
TRP CA     C N S 549 
TRP C      C N N 550 
TRP O      O N N 551 
TRP CB     C N N 552 
TRP CG     C Y N 553 
TRP CD1    C Y N 554 
TRP CD2    C Y N 555 
TRP NE1    N Y N 556 
TRP CE2    C Y N 557 
TRP CE3    C Y N 558 
TRP CZ2    C Y N 559 
TRP CZ3    C Y N 560 
TRP CH2    C Y N 561 
TRP OXT    O N N 562 
TRP H      H N N 563 
TRP H2     H N N 564 
TRP HA     H N N 565 
TRP HB2    H N N 566 
TRP HB3    H N N 567 
TRP HD1    H N N 568 
TRP HE1    H N N 569 
TRP HE3    H N N 570 
TRP HZ2    H N N 571 
TRP HZ3    H N N 572 
TRP HH2    H N N 573 
TRP HXT    H N N 574 
TYR N      N N N 575 
TYR CA     C N S 576 
TYR C      C N N 577 
TYR O      O N N 578 
TYR CB     C N N 579 
TYR CG     C Y N 580 
TYR CD1    C Y N 581 
TYR CD2    C Y N 582 
TYR CE1    C Y N 583 
TYR CE2    C Y N 584 
TYR CZ     C Y N 585 
TYR OH     O N N 586 
TYR OXT    O N N 587 
TYR H      H N N 588 
TYR H2     H N N 589 
TYR HA     H N N 590 
TYR HB2    H N N 591 
TYR HB3    H N N 592 
TYR HD1    H N N 593 
TYR HD2    H N N 594 
TYR HE1    H N N 595 
TYR HE2    H N N 596 
TYR HH     H N N 597 
TYR HXT    H N N 598 
VAL N      N N N 599 
VAL CA     C N S 600 
VAL C      C N N 601 
VAL O      O N N 602 
VAL CB     C N N 603 
VAL CG1    C N N 604 
VAL CG2    C N N 605 
VAL OXT    O N N 606 
VAL H      H N N 607 
VAL H2     H N N 608 
VAL HA     H N N 609 
VAL HB     H N N 610 
VAL HG11   H N N 611 
VAL HG12   H N N 612 
VAL HG13   H N N 613 
VAL HG21   H N N 614 
VAL HG22   H N N 615 
VAL HG23   H N N 616 
VAL HXT    H N N 617 
# 
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 
1PE OH2   C12    sing N N 1   
1PE OH2   HO2    sing N N 2   
1PE C12   C22    sing N N 3   
1PE C12   H121   sing N N 4   
1PE C12   H122   sing N N 5   
1PE C22   OH3    sing N N 6   
1PE C22   H221   sing N N 7   
1PE C22   H222   sing N N 8   
1PE OH3   C23    sing N N 9   
1PE C13   C23    sing N N 10  
1PE C13   OH4    sing N N 11  
1PE C13   H131   sing N N 12  
1PE C13   H132   sing N N 13  
1PE C23   H231   sing N N 14  
1PE C23   H232   sing N N 15  
1PE OH4   C24    sing N N 16  
1PE C14   C24    sing N N 17  
1PE C14   OH5    sing N N 18  
1PE C14   H141   sing N N 19  
1PE C14   H142   sing N N 20  
1PE C24   H241   sing N N 21  
1PE C24   H242   sing N N 22  
1PE OH5   C25    sing N N 23  
1PE C15   C25    sing N N 24  
1PE C15   OH6    sing N N 25  
1PE C15   H151   sing N N 26  
1PE C15   H152   sing N N 27  
1PE C25   H251   sing N N 28  
1PE C25   H252   sing N N 29  
1PE OH6   C26    sing N N 30  
1PE C16   C26    sing N N 31  
1PE C16   OH7    sing N N 32  
1PE C16   H161   sing N N 33  
1PE C16   H162   sing N N 34  
1PE C26   H261   sing N N 35  
1PE C26   H262   sing N N 36  
1PE OH7   HO7    sing N N 37  
ALA N     CA     sing N N 38  
ALA N     H      sing N N 39  
ALA N     H2     sing N N 40  
ALA CA    C      sing N N 41  
ALA CA    CB     sing N N 42  
ALA CA    HA     sing N N 43  
ALA C     O      doub N N 44  
ALA C     OXT    sing N N 45  
ALA CB    HB1    sing N N 46  
ALA CB    HB2    sing N N 47  
ALA CB    HB3    sing N N 48  
ALA OXT   HXT    sing N N 49  
ARG N     CA     sing N N 50  
ARG N     H      sing N N 51  
ARG N     H2     sing N N 52  
ARG CA    C      sing N N 53  
ARG CA    CB     sing N N 54  
ARG CA    HA     sing N N 55  
ARG C     O      doub N N 56  
ARG C     OXT    sing N N 57  
ARG CB    CG     sing N N 58  
ARG CB    HB2    sing N N 59  
ARG CB    HB3    sing N N 60  
ARG CG    CD     sing N N 61  
ARG CG    HG2    sing N N 62  
ARG CG    HG3    sing N N 63  
ARG CD    NE     sing N N 64  
ARG CD    HD2    sing N N 65  
ARG CD    HD3    sing N N 66  
ARG NE    CZ     sing N N 67  
ARG NE    HE     sing N N 68  
ARG CZ    NH1    sing N N 69  
ARG CZ    NH2    doub N N 70  
ARG NH1   HH11   sing N N 71  
ARG NH1   HH12   sing N N 72  
ARG NH2   HH21   sing N N 73  
ARG NH2   HH22   sing N N 74  
ARG OXT   HXT    sing N N 75  
ASN N     CA     sing N N 76  
ASN N     H      sing N N 77  
ASN N     H2     sing N N 78  
ASN CA    C      sing N N 79  
ASN CA    CB     sing N N 80  
ASN CA    HA     sing N N 81  
ASN C     O      doub N N 82  
ASN C     OXT    sing N N 83  
ASN CB    CG     sing N N 84  
ASN CB    HB2    sing N N 85  
ASN CB    HB3    sing N N 86  
ASN CG    OD1    doub N N 87  
ASN CG    ND2    sing N N 88  
ASN ND2   HD21   sing N N 89  
ASN ND2   HD22   sing N N 90  
ASN OXT   HXT    sing N N 91  
ASP N     CA     sing N N 92  
ASP N     H      sing N N 93  
ASP N     H2     sing N N 94  
ASP CA    C      sing N N 95  
ASP CA    CB     sing N N 96  
ASP CA    HA     sing N N 97  
ASP C     O      doub N N 98  
ASP C     OXT    sing N N 99  
ASP CB    CG     sing N N 100 
ASP CB    HB2    sing N N 101 
ASP CB    HB3    sing N N 102 
ASP CG    OD1    doub N N 103 
ASP CG    OD2    sing N N 104 
ASP OD2   HD2    sing N N 105 
ASP OXT   HXT    sing N N 106 
CYS N     CA     sing N N 107 
CYS N     H      sing N N 108 
CYS N     H2     sing N N 109 
CYS CA    C      sing N N 110 
CYS CA    CB     sing N N 111 
CYS CA    HA     sing N N 112 
CYS C     O      doub N N 113 
CYS C     OXT    sing N N 114 
CYS CB    SG     sing N N 115 
CYS CB    HB2    sing N N 116 
CYS CB    HB3    sing N N 117 
CYS SG    HG     sing N N 118 
CYS OXT   HXT    sing N N 119 
EOL C1    C2     doub Y N 120 
EOL C1    C3     sing Y N 121 
EOL O1    C5     sing N N 122 
EOL C2    C4     sing Y N 123 
EOL C2    C7     sing N N 124 
EOL O2    C3     sing N N 125 
EOL O2    C10    sing N N 126 
EOL C3    C5     doub Y N 127 
EOL C4    C6     doub Y N 128 
EOL C5    C6     sing Y N 129 
EOL C7    C8     sing N N 130 
EOL C8    C9     doub N N 131 
EOL C1    H1     sing N N 132 
EOL O1    HO1    sing N N 133 
EOL C4    H4     sing N N 134 
EOL C6    H6     sing N N 135 
EOL C7    H7     sing N N 136 
EOL C7    H7A    sing N N 137 
EOL C8    H8     sing N N 138 
EOL C9    H9     sing N N 139 
EOL C9    H9A    sing N N 140 
EOL C10   H10    sing N N 141 
EOL C10   H10A   sing N N 142 
EOL C10   H10B   sing N N 143 
FAD PA    O1A    doub N N 144 
FAD PA    O2A    sing N N 145 
FAD PA    O5B    sing N N 146 
FAD PA    O3P    sing N N 147 
FAD O2A   HOA2   sing N N 148 
FAD O5B   C5B    sing N N 149 
FAD C5B   C4B    sing N N 150 
FAD C5B   H51A   sing N N 151 
FAD C5B   H52A   sing N N 152 
FAD C4B   O4B    sing N N 153 
FAD C4B   C3B    sing N N 154 
FAD C4B   H4B    sing N N 155 
FAD O4B   C1B    sing N N 156 
FAD C3B   O3B    sing N N 157 
FAD C3B   C2B    sing N N 158 
FAD C3B   H3B    sing N N 159 
FAD O3B   HO3A   sing N N 160 
FAD C2B   O2B    sing N N 161 
FAD C2B   C1B    sing N N 162 
FAD C2B   H2B    sing N N 163 
FAD O2B   HO2A   sing N N 164 
FAD C1B   N9A    sing N N 165 
FAD C1B   H1B    sing N N 166 
FAD N9A   C8A    sing Y N 167 
FAD N9A   C4A    sing Y N 168 
FAD C8A   N7A    doub Y N 169 
FAD C8A   H8A    sing N N 170 
FAD N7A   C5A    sing Y N 171 
FAD C5A   C6A    sing Y N 172 
FAD C5A   C4A    doub Y N 173 
FAD C6A   N6A    sing N N 174 
FAD C6A   N1A    doub Y N 175 
FAD N6A   H61A   sing N N 176 
FAD N6A   H62A   sing N N 177 
FAD N1A   C2A    sing Y N 178 
FAD C2A   N3A    doub Y N 179 
FAD C2A   H2A    sing N N 180 
FAD N3A   C4A    sing Y N 181 
FAD N1    C2     sing N N 182 
FAD N1    C10    doub N N 183 
FAD C2    O2     doub N N 184 
FAD C2    N3     sing N N 185 
FAD N3    C4     sing N N 186 
FAD N3    HN3    sing N N 187 
FAD C4    O4     doub N N 188 
FAD C4    C4X    sing N N 189 
FAD C4X   N5     doub N N 190 
FAD C4X   C10    sing N N 191 
FAD N5    C5X    sing N N 192 
FAD C5X   C6     doub Y N 193 
FAD C5X   C9A    sing Y N 194 
FAD C6    C7     sing Y N 195 
FAD C6    H6     sing N N 196 
FAD C7    C7M    sing N N 197 
FAD C7    C8     doub Y N 198 
FAD C7M   HM71   sing N N 199 
FAD C7M   HM72   sing N N 200 
FAD C7M   HM73   sing N N 201 
FAD C8    C8M    sing N N 202 
FAD C8    C9     sing Y N 203 
FAD C8M   HM81   sing N N 204 
FAD C8M   HM82   sing N N 205 
FAD C8M   HM83   sing N N 206 
FAD C9    C9A    doub Y N 207 
FAD C9    H9     sing N N 208 
FAD C9A   N10    sing N N 209 
FAD N10   C10    sing N N 210 
FAD N10   "C1'"  sing N N 211 
FAD "C1'" "C2'"  sing N N 212 
FAD "C1'" "H1'1" sing N N 213 
FAD "C1'" "H1'2" sing N N 214 
FAD "C2'" "O2'"  sing N N 215 
FAD "C2'" "C3'"  sing N N 216 
FAD "C2'" "H2'"  sing N N 217 
FAD "O2'" "HO2'" sing N N 218 
FAD "C3'" "O3'"  sing N N 219 
FAD "C3'" "C4'"  sing N N 220 
FAD "C3'" "H3'"  sing N N 221 
FAD "O3'" "HO3'" sing N N 222 
FAD "C4'" "O4'"  sing N N 223 
FAD "C4'" "C5'"  sing N N 224 
FAD "C4'" "H4'"  sing N N 225 
FAD "O4'" "HO4'" sing N N 226 
FAD "C5'" "O5'"  sing N N 227 
FAD "C5'" "H5'1" sing N N 228 
FAD "C5'" "H5'2" sing N N 229 
FAD "O5'" P      sing N N 230 
FAD P     O1P    doub N N 231 
FAD P     O2P    sing N N 232 
FAD P     O3P    sing N N 233 
FAD O2P   HOP2   sing N N 234 
GLN N     CA     sing N N 235 
GLN N     H      sing N N 236 
GLN N     H2     sing N N 237 
GLN CA    C      sing N N 238 
GLN CA    CB     sing N N 239 
GLN CA    HA     sing N N 240 
GLN C     O      doub N N 241 
GLN C     OXT    sing N N 242 
GLN CB    CG     sing N N 243 
GLN CB    HB2    sing N N 244 
GLN CB    HB3    sing N N 245 
GLN CG    CD     sing N N 246 
GLN CG    HG2    sing N N 247 
GLN CG    HG3    sing N N 248 
GLN CD    OE1    doub N N 249 
GLN CD    NE2    sing N N 250 
GLN NE2   HE21   sing N N 251 
GLN NE2   HE22   sing N N 252 
GLN OXT   HXT    sing N N 253 
GLU N     CA     sing N N 254 
GLU N     H      sing N N 255 
GLU N     H2     sing N N 256 
GLU CA    C      sing N N 257 
GLU CA    CB     sing N N 258 
GLU CA    HA     sing N N 259 
GLU C     O      doub N N 260 
GLU C     OXT    sing N N 261 
GLU CB    CG     sing N N 262 
GLU CB    HB2    sing N N 263 
GLU CB    HB3    sing N N 264 
GLU CG    CD     sing N N 265 
GLU CG    HG2    sing N N 266 
GLU CG    HG3    sing N N 267 
GLU CD    OE1    doub N N 268 
GLU CD    OE2    sing N N 269 
GLU OE2   HE2    sing N N 270 
GLU OXT   HXT    sing N N 271 
GLY N     CA     sing N N 272 
GLY N     H      sing N N 273 
GLY N     H2     sing N N 274 
GLY CA    C      sing N N 275 
GLY CA    HA2    sing N N 276 
GLY CA    HA3    sing N N 277 
GLY C     O      doub N N 278 
GLY C     OXT    sing N N 279 
GLY OXT   HXT    sing N N 280 
HIS N     CA     sing N N 281 
HIS N     H      sing N N 282 
HIS N     H2     sing N N 283 
HIS CA    C      sing N N 284 
HIS CA    CB     sing N N 285 
HIS CA    HA     sing N N 286 
HIS C     O      doub N N 287 
HIS C     OXT    sing N N 288 
HIS CB    CG     sing N N 289 
HIS CB    HB2    sing N N 290 
HIS CB    HB3    sing N N 291 
HIS CG    ND1    sing Y N 292 
HIS CG    CD2    doub Y N 293 
HIS ND1   CE1    doub Y N 294 
HIS ND1   HD1    sing N N 295 
HIS CD2   NE2    sing Y N 296 
HIS CD2   HD2    sing N N 297 
HIS CE1   NE2    sing Y N 298 
HIS CE1   HE1    sing N N 299 
HIS NE2   HE2    sing N N 300 
HIS OXT   HXT    sing N N 301 
HOH O     H1     sing N N 302 
HOH O     H2     sing N N 303 
ILE N     CA     sing N N 304 
ILE N     H      sing N N 305 
ILE N     H2     sing N N 306 
ILE CA    C      sing N N 307 
ILE CA    CB     sing N N 308 
ILE CA    HA     sing N N 309 
ILE C     O      doub N N 310 
ILE C     OXT    sing N N 311 
ILE CB    CG1    sing N N 312 
ILE CB    CG2    sing N N 313 
ILE CB    HB     sing N N 314 
ILE CG1   CD1    sing N N 315 
ILE CG1   HG12   sing N N 316 
ILE CG1   HG13   sing N N 317 
ILE CG2   HG21   sing N N 318 
ILE CG2   HG22   sing N N 319 
ILE CG2   HG23   sing N N 320 
ILE CD1   HD11   sing N N 321 
ILE CD1   HD12   sing N N 322 
ILE CD1   HD13   sing N N 323 
ILE OXT   HXT    sing N N 324 
LEU N     CA     sing N N 325 
LEU N     H      sing N N 326 
LEU N     H2     sing N N 327 
LEU CA    C      sing N N 328 
LEU CA    CB     sing N N 329 
LEU CA    HA     sing N N 330 
LEU C     O      doub N N 331 
LEU C     OXT    sing N N 332 
LEU CB    CG     sing N N 333 
LEU CB    HB2    sing N N 334 
LEU CB    HB3    sing N N 335 
LEU CG    CD1    sing N N 336 
LEU CG    CD2    sing N N 337 
LEU CG    HG     sing N N 338 
LEU CD1   HD11   sing N N 339 
LEU CD1   HD12   sing N N 340 
LEU CD1   HD13   sing N N 341 
LEU CD2   HD21   sing N N 342 
LEU CD2   HD22   sing N N 343 
LEU CD2   HD23   sing N N 344 
LEU OXT   HXT    sing N N 345 
LYS N     CA     sing N N 346 
LYS N     H      sing N N 347 
LYS N     H2     sing N N 348 
LYS CA    C      sing N N 349 
LYS CA    CB     sing N N 350 
LYS CA    HA     sing N N 351 
LYS C     O      doub N N 352 
LYS C     OXT    sing N N 353 
LYS CB    CG     sing N N 354 
LYS CB    HB2    sing N N 355 
LYS CB    HB3    sing N N 356 
LYS CG    CD     sing N N 357 
LYS CG    HG2    sing N N 358 
LYS CG    HG3    sing N N 359 
LYS CD    CE     sing N N 360 
LYS CD    HD2    sing N N 361 
LYS CD    HD3    sing N N 362 
LYS CE    NZ     sing N N 363 
LYS CE    HE2    sing N N 364 
LYS CE    HE3    sing N N 365 
LYS NZ    HZ1    sing N N 366 
LYS NZ    HZ2    sing N N 367 
LYS NZ    HZ3    sing N N 368 
LYS OXT   HXT    sing N N 369 
MET N     CA     sing N N 370 
MET N     H      sing N N 371 
MET N     H2     sing N N 372 
MET CA    C      sing N N 373 
MET CA    CB     sing N N 374 
MET CA    HA     sing N N 375 
MET C     O      doub N N 376 
MET C     OXT    sing N N 377 
MET CB    CG     sing N N 378 
MET CB    HB2    sing N N 379 
MET CB    HB3    sing N N 380 
MET CG    SD     sing N N 381 
MET CG    HG2    sing N N 382 
MET CG    HG3    sing N N 383 
MET SD    CE     sing N N 384 
MET CE    HE1    sing N N 385 
MET CE    HE2    sing N N 386 
MET CE    HE3    sing N N 387 
MET OXT   HXT    sing N N 388 
NO3 N     O1     doub N N 389 
NO3 N     O2     sing N N 390 
NO3 N     O3     sing N N 391 
PE4 O1    C1     sing N N 392 
PE4 O1    HO1    sing N N 393 
PE4 C1    C2     sing N N 394 
PE4 C1    H11    sing N N 395 
PE4 C1    H12    sing N N 396 
PE4 C2    O2     sing N N 397 
PE4 C2    H21    sing N N 398 
PE4 C2    H22    sing N N 399 
PE4 O2    C3     sing N N 400 
PE4 C3    C4     sing N N 401 
PE4 C3    H31    sing N N 402 
PE4 C3    H32    sing N N 403 
PE4 C4    O3     sing N N 404 
PE4 C4    H41    sing N N 405 
PE4 C4    H42    sing N N 406 
PE4 O3    C5     sing N N 407 
PE4 C5    C6     sing N N 408 
PE4 C5    H51    sing N N 409 
PE4 C5    H52    sing N N 410 
PE4 C6    O4     sing N N 411 
PE4 C6    H61    sing N N 412 
PE4 C6    H62    sing N N 413 
PE4 O4    C7     sing N N 414 
PE4 C7    C8     sing N N 415 
PE4 C7    H71    sing N N 416 
PE4 C7    H72    sing N N 417 
PE4 C8    O5     sing N N 418 
PE4 C8    H81    sing N N 419 
PE4 C8    H82    sing N N 420 
PE4 O5    C9     sing N N 421 
PE4 C9    C10    sing N N 422 
PE4 C9    H91    sing N N 423 
PE4 C9    H92    sing N N 424 
PE4 C10   O6     sing N N 425 
PE4 C10   H101   sing N N 426 
PE4 C10   H102   sing N N 427 
PE4 O6    C11    sing N N 428 
PE4 C11   C12    sing N N 429 
PE4 C11   H111   sing N N 430 
PE4 C11   H112   sing N N 431 
PE4 C12   O7     sing N N 432 
PE4 C12   H121   sing N N 433 
PE4 C12   H122   sing N N 434 
PE4 O7    C13    sing N N 435 
PE4 C13   C14    sing N N 436 
PE4 C13   H131   sing N N 437 
PE4 C13   H132   sing N N 438 
PE4 C14   O8     sing N N 439 
PE4 C14   H141   sing N N 440 
PE4 C14   H142   sing N N 441 
PE4 O8    C15    sing N N 442 
PE4 C15   C16    sing N N 443 
PE4 C15   H151   sing N N 444 
PE4 C15   H152   sing N N 445 
PE4 C16   H161   sing N N 446 
PE4 C16   H162   sing N N 447 
PE4 C16   H163   sing N N 448 
PEG C1    O1     sing N N 449 
PEG C1    C2     sing N N 450 
PEG C1    H11    sing N N 451 
PEG C1    H12    sing N N 452 
PEG O1    HO1    sing N N 453 
PEG C2    O2     sing N N 454 
PEG C2    H21    sing N N 455 
PEG C2    H22    sing N N 456 
PEG O2    C3     sing N N 457 
PEG C3    C4     sing N N 458 
PEG C3    H31    sing N N 459 
PEG C3    H32    sing N N 460 
PEG C4    O4     sing N N 461 
PEG C4    H41    sing N N 462 
PEG C4    H42    sing N N 463 
PEG O4    HO4    sing N N 464 
PHE N     CA     sing N N 465 
PHE N     H      sing N N 466 
PHE N     H2     sing N N 467 
PHE CA    C      sing N N 468 
PHE CA    CB     sing N N 469 
PHE CA    HA     sing N N 470 
PHE C     O      doub N N 471 
PHE C     OXT    sing N N 472 
PHE CB    CG     sing N N 473 
PHE CB    HB2    sing N N 474 
PHE CB    HB3    sing N N 475 
PHE CG    CD1    doub Y N 476 
PHE CG    CD2    sing Y N 477 
PHE CD1   CE1    sing Y N 478 
PHE CD1   HD1    sing N N 479 
PHE CD2   CE2    doub Y N 480 
PHE CD2   HD2    sing N N 481 
PHE CE1   CZ     doub Y N 482 
PHE CE1   HE1    sing N N 483 
PHE CE2   CZ     sing Y N 484 
PHE CE2   HE2    sing N N 485 
PHE CZ    HZ     sing N N 486 
PHE OXT   HXT    sing N N 487 
PRO N     CA     sing N N 488 
PRO N     CD     sing N N 489 
PRO N     H      sing N N 490 
PRO CA    C      sing N N 491 
PRO CA    CB     sing N N 492 
PRO CA    HA     sing N N 493 
PRO C     O      doub N N 494 
PRO C     OXT    sing N N 495 
PRO CB    CG     sing N N 496 
PRO CB    HB2    sing N N 497 
PRO CB    HB3    sing N N 498 
PRO CG    CD     sing N N 499 
PRO CG    HG2    sing N N 500 
PRO CG    HG3    sing N N 501 
PRO CD    HD2    sing N N 502 
PRO CD    HD3    sing N N 503 
PRO OXT   HXT    sing N N 504 
SER N     CA     sing N N 505 
SER N     H      sing N N 506 
SER N     H2     sing N N 507 
SER CA    C      sing N N 508 
SER CA    CB     sing N N 509 
SER CA    HA     sing N N 510 
SER C     O      doub N N 511 
SER C     OXT    sing N N 512 
SER CB    OG     sing N N 513 
SER CB    HB2    sing N N 514 
SER CB    HB3    sing N N 515 
SER OG    HG     sing N N 516 
SER OXT   HXT    sing N N 517 
THR N     CA     sing N N 518 
THR N     H      sing N N 519 
THR N     H2     sing N N 520 
THR CA    C      sing N N 521 
THR CA    CB     sing N N 522 
THR CA    HA     sing N N 523 
THR C     O      doub N N 524 
THR C     OXT    sing N N 525 
THR CB    OG1    sing N N 526 
THR CB    CG2    sing N N 527 
THR CB    HB     sing N N 528 
THR OG1   HG1    sing N N 529 
THR CG2   HG21   sing N N 530 
THR CG2   HG22   sing N N 531 
THR CG2   HG23   sing N N 532 
THR OXT   HXT    sing N N 533 
TRP N     CA     sing N N 534 
TRP N     H      sing N N 535 
TRP N     H2     sing N N 536 
TRP CA    C      sing N N 537 
TRP CA    CB     sing N N 538 
TRP CA    HA     sing N N 539 
TRP C     O      doub N N 540 
TRP C     OXT    sing N N 541 
TRP CB    CG     sing N N 542 
TRP CB    HB2    sing N N 543 
TRP CB    HB3    sing N N 544 
TRP CG    CD1    doub Y N 545 
TRP CG    CD2    sing Y N 546 
TRP CD1   NE1    sing Y N 547 
TRP CD1   HD1    sing N N 548 
TRP CD2   CE2    doub Y N 549 
TRP CD2   CE3    sing Y N 550 
TRP NE1   CE2    sing Y N 551 
TRP NE1   HE1    sing N N 552 
TRP CE2   CZ2    sing Y N 553 
TRP CE3   CZ3    doub Y N 554 
TRP CE3   HE3    sing N N 555 
TRP CZ2   CH2    doub Y N 556 
TRP CZ2   HZ2    sing N N 557 
TRP CZ3   CH2    sing Y N 558 
TRP CZ3   HZ3    sing N N 559 
TRP CH2   HH2    sing N N 560 
TRP OXT   HXT    sing N N 561 
TYR N     CA     sing N N 562 
TYR N     H      sing N N 563 
TYR N     H2     sing N N 564 
TYR CA    C      sing N N 565 
TYR CA    CB     sing N N 566 
TYR CA    HA     sing N N 567 
TYR C     O      doub N N 568 
TYR C     OXT    sing N N 569 
TYR CB    CG     sing N N 570 
TYR CB    HB2    sing N N 571 
TYR CB    HB3    sing N N 572 
TYR CG    CD1    doub Y N 573 
TYR CG    CD2    sing Y N 574 
TYR CD1   CE1    sing Y N 575 
TYR CD1   HD1    sing N N 576 
TYR CD2   CE2    doub Y N 577 
TYR CD2   HD2    sing N N 578 
TYR CE1   CZ     doub Y N 579 
TYR CE1   HE1    sing N N 580 
TYR CE2   CZ     sing Y N 581 
TYR CE2   HE2    sing N N 582 
TYR CZ    OH     sing N N 583 
TYR OH    HH     sing N N 584 
TYR OXT   HXT    sing N N 585 
VAL N     CA     sing N N 586 
VAL N     H      sing N N 587 
VAL N     H2     sing N N 588 
VAL CA    C      sing N N 589 
VAL CA    CB     sing N N 590 
VAL CA    HA     sing N N 591 
VAL C     O      doub N N 592 
VAL C     OXT    sing N N 593 
VAL CB    CG1    sing N N 594 
VAL CB    CG2    sing N N 595 
VAL CB    HB     sing N N 596 
VAL CG1   HG11   sing N N 597 
VAL CG1   HG12   sing N N 598 
VAL CG1   HG13   sing N N 599 
VAL CG2   HG21   sing N N 600 
VAL CG2   HG22   sing N N 601 
VAL CG2   HG23   sing N N 602 
VAL OXT   HXT    sing N N 603 
# 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'B-Ligzymes (GA 824017)' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S7N 
_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]   0.007193 
_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]   0.007193 
_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]   0.005523 
_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     . MET A 1 1   ? -35.512 83.474  51.163 1.00 59.69 ? 1    MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? -35.480 84.424  52.318 1.00 62.79 ? 1    MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? -34.288 84.021  53.195 1.00 58.18 ? 1    MET A C     1 
ATOM   4    O O     . MET A 1 1   ? -33.247 84.647  53.058 1.00 54.83 ? 1    MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? -36.781 84.417  53.144 1.00 65.25 ? 1    MET A CB    1 
ATOM   6    N N     . ALA A 1 2   ? -34.422 82.991  54.034 1.00 52.02 ? 2    ALA A N     1 
ATOM   7    C CA    . ALA A 1 2   ? -33.402 82.610  55.046 1.00 48.77 ? 2    ALA A CA    1 
ATOM   8    C C     . ALA A 1 2   ? -32.183 81.945  54.369 1.00 47.51 ? 2    ALA A C     1 
ATOM   9    O O     . ALA A 1 2   ? -32.314 81.279  53.320 1.00 40.75 ? 2    ALA A O     1 
ATOM   10   C CB    . ALA A 1 2   ? -34.025 81.727  56.099 1.00 43.94 ? 2    ALA A CB    1 
ATOM   11   N N     . ALA A 1 3   ? -30.994 82.117  54.936 1.00 41.24 ? 3    ALA A N     1 
ATOM   12   C CA    . ALA A 1 3   ? -29.767 81.447  54.444 1.00 36.45 ? 3    ALA A CA    1 
ATOM   13   C C     . ALA A 1 3   ? -29.979 79.930  54.418 1.00 33.67 ? 3    ALA A C     1 
ATOM   14   O O     . ALA A 1 3   ? -30.554 79.365  55.333 1.00 31.76 ? 3    ALA A O     1 
ATOM   15   C CB    . ALA A 1 3   ? -28.617 81.799  55.344 1.00 36.76 ? 3    ALA A CB    1 
ATOM   16   N N     . PRO A 1 4   ? -29.420 79.215  53.427 1.00 31.03 ? 4    PRO A N     1 
ATOM   17   C CA    . PRO A 1 4   ? -29.391 77.764  53.449 1.00 33.17 ? 4    PRO A CA    1 
ATOM   18   C C     . PRO A 1 4   ? -28.315 77.272  54.428 1.00 37.08 ? 4    PRO A C     1 
ATOM   19   O O     . PRO A 1 4   ? -27.333 77.984  54.732 1.00 33.20 ? 4    PRO A O     1 
ATOM   20   C CB    . PRO A 1 4   ? -29.029 77.391  52.005 1.00 32.97 ? 4    PRO A CB    1 
ATOM   21   C CG    . PRO A 1 4   ? -28.191 78.548  51.529 1.00 36.91 ? 4    PRO A CG    1 
ATOM   22   C CD    . PRO A 1 4   ? -28.705 79.769  52.275 1.00 36.75 ? 4    PRO A CD    1 
ATOM   23   N N     . LEU A 1 5   ? -28.467 76.033  54.853 1.00 32.95 ? 5    LEU A N     1 
ATOM   24   C CA    . LEU A 1 5   ? -27.381 75.342  55.563 1.00 32.95 ? 5    LEU A CA    1 
ATOM   25   C C     . LEU A 1 5   ? -26.179 75.276  54.619 1.00 35.96 ? 5    LEU A C     1 
ATOM   26   O O     . LEU A 1 5   ? -26.321 75.238  53.396 1.00 33.99 ? 5    LEU A O     1 
ATOM   27   C CB    . LEU A 1 5   ? -27.836 73.955  55.998 1.00 30.74 ? 5    LEU A CB    1 
ATOM   28   C CG    . LEU A 1 5   ? -28.840 73.908  57.148 1.00 32.60 ? 5    LEU A CG    1 
ATOM   29   C CD1   . LEU A 1 5   ? -29.594 72.563  57.156 1.00 32.33 ? 5    LEU A CD1   1 
ATOM   30   C CD2   . LEU A 1 5   ? -28.123 74.134  58.461 1.00 35.68 ? 5    LEU A CD2   1 
ATOM   31   N N     . PRO A 1 6   ? -24.940 75.237  55.163 1.00 32.18 ? 6    PRO A N     1 
ATOM   32   C CA    . PRO A 1 6   ? -23.784 74.965  54.330 1.00 34.21 ? 6    PRO A CA    1 
ATOM   33   C C     . PRO A 1 6   ? -23.893 73.523  53.822 1.00 35.13 ? 6    PRO A C     1 
ATOM   34   O O     . PRO A 1 6   ? -24.370 72.650  54.540 1.00 36.09 ? 6    PRO A O     1 
ATOM   35   C CB    . PRO A 1 6   ? -22.584 75.224  55.256 1.00 37.21 ? 6    PRO A CB    1 
ATOM   36   C CG    . PRO A 1 6   ? -23.114 75.095  56.654 1.00 35.19 ? 6    PRO A CG    1 
ATOM   37   C CD    . PRO A 1 6   ? -24.615 75.338  56.592 1.00 31.45 ? 6    PRO A CD    1 
ATOM   38   N N     . GLU A 1 7   ? -23.443 73.294  52.596 1.00 37.64 ? 7    GLU A N     1 
ATOM   39   C CA    . GLU A 1 7   ? -23.436 71.935  52.012 1.00 40.84 ? 7    GLU A CA    1 
ATOM   40   C C     . GLU A 1 7   ? -22.653 70.992  52.929 1.00 39.29 ? 7    GLU A C     1 
ATOM   41   O O     . GLU A 1 7   ? -21.613 71.370  53.429 1.00 37.73 ? 7    GLU A O     1 
ATOM   42   C CB    . GLU A 1 7   ? -22.897 71.974  50.593 1.00 48.14 ? 7    GLU A CB    1 
ATOM   43   C CG    . GLU A 1 7   ? -22.739 70.595  50.008 1.00 60.01 ? 7    GLU A CG    1 
ATOM   44   C CD    . GLU A 1 7   ? -22.643 70.613  48.502 1.00 66.45 ? 7    GLU A CD    1 
ATOM   45   O OE1   . GLU A 1 7   ? -22.601 69.526  47.912 1.00 78.53 ? 7    GLU A OE1   1 
ATOM   46   O OE2   . GLU A 1 7   ? -22.614 71.716  47.935 1.00 77.26 ? 7    GLU A OE2   1 
ATOM   47   N N     . GLY A 1 8   ? -23.203 69.811  53.189 1.00 39.91 ? 8    GLY A N     1 
ATOM   48   C CA    . GLY A 1 8   ? -22.572 68.736  53.965 1.00 36.83 ? 8    GLY A CA    1 
ATOM   49   C C     . GLY A 1 8   ? -22.866 68.876  55.430 1.00 35.04 ? 8    GLY A C     1 
ATOM   50   O O     . GLY A 1 8   ? -22.418 68.031  56.194 1.00 39.19 ? 8    GLY A O     1 
ATOM   51   N N     . VAL A 1 9   ? -23.594 69.918  55.835 1.00 34.94 ? 9    VAL A N     1 
ATOM   52   C CA    . VAL A 1 9   ? -23.937 70.146  57.263 1.00 33.71 ? 9    VAL A CA    1 
ATOM   53   C C     . VAL A 1 9   ? -25.459 69.963  57.456 1.00 33.35 ? 9    VAL A C     1 
ATOM   54   O O     . VAL A 1 9   ? -26.267 70.742  56.903 1.00 32.15 ? 9    VAL A O     1 
ATOM   55   C CB    . VAL A 1 9   ? -23.484 71.549  57.738 1.00 35.65 ? 9    VAL A CB    1 
ATOM   56   C CG1   . VAL A 1 9   ? -23.864 71.781  59.176 1.00 35.32 ? 9    VAL A CG1   1 
ATOM   57   C CG2   . VAL A 1 9   ? -21.986 71.803  57.521 1.00 38.54 ? 9    VAL A CG2   1 
ATOM   58   N N     . SER A 1 10  ? -25.837 69.033  58.313 1.00 34.83 ? 10   SER A N     1 
ATOM   59   C CA    . SER A 1 10  ? -27.251 68.693  58.604 1.00 34.33 ? 10   SER A CA    1 
ATOM   60   C C     . SER A 1 10  ? -27.834 69.743  59.540 1.00 36.84 ? 10   SER A C     1 
ATOM   61   O O     . SER A 1 10  ? -27.059 70.422  60.232 1.00 33.77 ? 10   SER A O     1 
ATOM   62   C CB    . SER A 1 10  ? -27.339 67.322  59.186 1.00 32.58 ? 10   SER A CB    1 
ATOM   63   O OG    . SER A 1 10  ? -26.907 67.317  60.538 1.00 35.69 ? 10   SER A OG    1 
ATOM   64   N N     . ALA A 1 11  ? -29.162 69.870  59.569 1.00 37.49 ? 11   ALA A N     1 
ATOM   65   C CA    . ALA A 1 11  ? -29.907 70.732  60.511 1.00 35.75 ? 11   ALA A CA    1 
ATOM   66   C C     . ALA A 1 11  ? -29.512 70.407  61.954 1.00 33.06 ? 11   ALA A C     1 
ATOM   67   O O     . ALA A 1 11  ? -29.452 71.340  62.778 1.00 35.23 ? 11   ALA A O     1 
ATOM   68   C CB    . ALA A 1 11  ? -31.392 70.536  60.332 1.00 38.49 ? 11   ALA A CB    1 
ATOM   69   N N     . GLU A 1 12  ? -29.313 69.130  62.261 1.00 35.71 ? 12   GLU A N     1 
ATOM   70   C CA    . GLU A 1 12  ? -28.997 68.629  63.629 1.00 42.41 ? 12   GLU A CA    1 
ATOM   71   C C     . GLU A 1 12  ? -27.580 69.108  64.004 1.00 34.07 ? 12   GLU A C     1 
ATOM   72   O O     . GLU A 1 12  ? -27.396 69.585  65.129 1.00 38.04 ? 12   GLU A O     1 
ATOM   73   C CB    . GLU A 1 12  ? -29.100 67.095  63.681 1.00 44.94 ? 12   GLU A CB    1 
ATOM   74   C CG    . GLU A 1 12  ? -30.514 66.537  63.455 1.00 54.90 ? 12   GLU A CG    1 
ATOM   75   C CD    . GLU A 1 12  ? -31.141 66.673  62.056 1.00 63.16 ? 12   GLU A CD    1 
ATOM   76   O OE1   . GLU A 1 12  ? -32.354 66.981  61.975 1.00 64.76 ? 12   GLU A OE1   1 
ATOM   77   O OE2   . GLU A 1 12  ? -30.427 66.500  61.033 1.00 55.19 ? 12   GLU A OE2   1 
ATOM   78   N N     . ALA A 1 13  ? -26.622 68.941  63.094 1.00 36.14 ? 13   ALA A N     1 
ATOM   79   C CA    . ALA A 1 13  ? -25.218 69.349  63.313 1.00 36.40 ? 13   ALA A CA    1 
ATOM   80   C C     . ALA A 1 13  ? -25.209 70.862  63.567 1.00 33.29 ? 13   ALA A C     1 
ATOM   81   O O     . ALA A 1 13  ? -24.587 71.256  64.568 1.00 31.48 ? 13   ALA A O     1 
ATOM   82   C CB    . ALA A 1 13  ? -24.334 68.930  62.169 1.00 36.36 ? 13   ALA A CB    1 
ATOM   83   N N     . MET A 1 14  ? -25.922 71.658  62.752 1.00 30.12 ? 14   MET A N     1 
ATOM   84   C CA    . MET A 1 14  ? -25.942 73.139  62.894 1.00 29.50 ? 14   MET A CA    1 
ATOM   85   C C     . MET A 1 14  ? -26.569 73.489  64.228 1.00 30.05 ? 14   MET A C     1 
ATOM   86   O O     . MET A 1 14  ? -26.026 74.347  64.966 1.00 28.24 ? 14   MET A O     1 
ATOM   87   C CB    . MET A 1 14  ? -26.695 73.868  61.773 1.00 28.76 ? 14   MET A CB    1 
ATOM   88   C CG    . MET A 1 14  ? -26.765 75.363  61.984 1.00 32.05 ? 14   MET A CG    1 
ATOM   89   S SD    . MET A 1 14  ? -25.118 76.198  61.914 1.00 30.43 ? 14   MET A SD    1 
ATOM   90   C CE    . MET A 1 14  ? -24.835 76.193  60.142 1.00 30.27 ? 14   MET A CE    1 
ATOM   91   N N     . SER A 1 15  ? -27.680 72.846  64.555 1.00 30.89 ? 15   SER A N     1 
ATOM   92   C CA    . SER A 1 15  ? -28.433 73.146  65.794 1.00 31.78 ? 15   SER A CA    1 
ATOM   93   C C     . SER A 1 15  ? -27.569 72.808  67.024 1.00 29.33 ? 15   SER A C     1 
ATOM   94   O O     . SER A 1 15  ? -27.532 73.618  67.966 1.00 29.23 ? 15   SER A O     1 
ATOM   95   C CB    . SER A 1 15  ? -29.777 72.395  65.793 1.00 35.69 ? 15   SER A CB    1 
ATOM   96   O OG    . SER A 1 15  ? -30.417 72.569  67.048 1.00 46.91 ? 15   SER A OG    1 
ATOM   97   N N     . SER A 1 16  ? -26.891 71.670  67.016 1.00 29.77 ? 16   SER A N     1 
ATOM   98   C CA    . SER A 1 16  ? -25.965 71.250  68.103 1.00 34.18 ? 16   SER A CA    1 
ATOM   99   C C     . SER A 1 16  ? -24.800 72.251  68.231 1.00 31.03 ? 16   SER A C     1 
ATOM   100  O O     . SER A 1 16  ? -24.425 72.641  69.356 1.00 30.49 ? 16   SER A O     1 
ATOM   101  C CB    . SER A 1 16  ? -25.448 69.865  67.858 1.00 35.74 ? 16   SER A CB    1 
ATOM   102  O OG    . SER A 1 16  ? -26.498 68.929  67.940 1.00 37.92 ? 16   SER A OG    1 
ATOM   103  N N     . ALA A 1 17  ? -24.217 72.679  67.124 1.00 28.56 ? 17   ALA A N     1 
ATOM   104  C CA    . ALA A 1 17  ? -23.130 73.678  67.187 1.00 26.22 ? 17   ALA A CA    1 
ATOM   105  C C     . ALA A 1 17  ? -23.670 74.960  67.796 1.00 24.05 ? 17   ALA A C     1 
ATOM   106  O O     . ALA A 1 17  ? -23.016 75.565  68.712 1.00 24.27 ? 17   ALA A O     1 
ATOM   107  C CB    . ALA A 1 17  ? -22.542 73.910  65.810 1.00 27.11 ? 17   ALA A CB    1 
ATOM   108  N N     . LEU A 1 18  ? -24.797 75.456  67.306 1.00 25.00 ? 18   LEU A N     1 
ATOM   109  C CA    . LEU A 1 18  ? -25.295 76.762  67.804 1.00 24.86 ? 18   LEU A CA    1 
ATOM   110  C C     . LEU A 1 18  ? -25.632 76.671  69.298 1.00 27.68 ? 18   LEU A C     1 
ATOM   111  O O     . LEU A 1 18  ? -25.417 77.704  69.981 1.00 23.11 ? 18   LEU A O     1 
ATOM   112  C CB    . LEU A 1 18  ? -26.500 77.268  67.007 1.00 27.42 ? 18   LEU A CB    1 
ATOM   113  C CG    . LEU A 1 18  ? -26.240 77.607  65.545 1.00 28.96 ? 18   LEU A CG    1 
ATOM   114  C CD1   . LEU A 1 18  ? -27.487 78.169  64.899 1.00 31.41 ? 18   LEU A CD1   1 
ATOM   115  C CD2   . LEU A 1 18  ? -25.086 78.577  65.362 1.00 31.19 ? 18   LEU A CD2   1 
ATOM   116  N N     . ASP A 1 19  ? -26.163 75.544  69.797 1.00 28.71 ? 19   ASP A N     1 
ATOM   117  C CA    . ASP A 1 19  ? -26.423 75.422  71.268 1.00 30.57 ? 19   ASP A CA    1 
ATOM   118  C C     . ASP A 1 19  ? -25.076 75.489  71.988 1.00 25.96 ? 19   ASP A C     1 
ATOM   119  O O     . ASP A 1 19  ? -24.994 76.155  73.005 1.00 24.82 ? 19   ASP A O     1 
ATOM   120  C CB    . ASP A 1 19  ? -27.084 74.122  71.776 1.00 34.85 ? 19   ASP A CB    1 
ATOM   121  C CG    . ASP A 1 19  ? -27.014 73.895  73.327 1.00 45.16 ? 19   ASP A CG    1 
ATOM   122  O OD1   . ASP A 1 19  ? -27.619 74.725  74.130 1.00 48.46 ? 19   ASP A OD1   1 
ATOM   123  O OD2   . ASP A 1 19  ? -26.341 72.887  73.758 1.00 45.20 ? 19   ASP A OD2   1 
ATOM   124  N N     . ARG A 1 20  ? -24.049 74.824  71.469 1.00 25.40 ? 20   ARG A N     1 
ATOM   125  C CA    . ARG A 1 20  ? -22.720 74.798  72.157 1.00 27.06 ? 20   ARG A CA    1 
ATOM   126  C C     . ARG A 1 20  ? -22.090 76.184  72.117 1.00 26.08 ? 20   ARG A C     1 
ATOM   127  O O     . ARG A 1 20  ? -21.453 76.584  73.135 1.00 26.79 ? 20   ARG A O     1 
ATOM   128  C CB    . ARG A 1 20  ? -21.873 73.661  71.602 1.00 27.47 ? 20   ARG A CB    1 
ATOM   129  C CG    . ARG A 1 20  ? -22.401 72.313  72.076 1.00 30.60 ? 20   ARG A CG    1 
ATOM   130  C CD    . ARG A 1 20  ? -21.627 71.230  71.381 1.00 32.72 ? 20   ARG A CD    1 
ATOM   131  N NE    . ARG A 1 20  ? -21.824 69.865  71.857 1.00 42.19 ? 20   ARG A NE    1 
ATOM   132  C CZ    . ARG A 1 20  ? -22.936 69.155  71.725 1.00 44.83 ? 20   ARG A CZ    1 
ATOM   133  N NH1   . ARG A 1 20  ? -24.018 69.682  71.182 1.00 53.17 ? 20   ARG A NH1   1 
ATOM   134  N NH2   . ARG A 1 20  ? -22.964 67.905  72.133 1.00 44.57 ? 20   ARG A NH2   1 
ATOM   135  N N     . PHE A 1 21  ? -22.245 76.898  71.004 1.00 24.72 ? 21   PHE A N     1 
ATOM   136  C CA    . PHE A 1 21  ? -21.785 78.302  70.924 1.00 24.30 ? 21   PHE A CA    1 
ATOM   137  C C     . PHE A 1 21  ? -22.441 79.112  72.033 1.00 26.61 ? 21   PHE A C     1 
ATOM   138  O O     . PHE A 1 21  ? -21.743 79.938  72.708 1.00 24.67 ? 21   PHE A O     1 
ATOM   139  C CB    . PHE A 1 21  ? -22.067 78.956  69.573 1.00 23.75 ? 21   PHE A CB    1 
ATOM   140  C CG    . PHE A 1 21  ? -21.306 78.378  68.409 1.00 23.73 ? 21   PHE A CG    1 
ATOM   141  C CD1   . PHE A 1 21  ? -20.196 77.570  68.563 1.00 24.07 ? 21   PHE A CD1   1 
ATOM   142  C CD2   . PHE A 1 21  ? -21.749 78.639  67.115 1.00 27.15 ? 21   PHE A CD2   1 
ATOM   143  C CE1   . PHE A 1 21  ? -19.523 77.057  67.456 1.00 26.35 ? 21   PHE A CE1   1 
ATOM   144  C CE2   . PHE A 1 21  ? -21.064 78.145  66.014 1.00 24.43 ? 21   PHE A CE2   1 
ATOM   145  C CZ    . PHE A 1 21  ? -19.966 77.345  66.189 1.00 26.31 ? 21   PHE A CZ    1 
ATOM   146  N N     . ALA A 1 22  ? -23.731 78.890  72.285 1.00 26.73 ? 22   ALA A N     1 
ATOM   147  C CA    . ALA A 1 22  ? -24.471 79.684  73.299 1.00 27.36 ? 22   ALA A CA    1 
ATOM   148  C C     . ALA A 1 22  ? -23.963 79.374  74.712 1.00 25.41 ? 22   ALA A C     1 
ATOM   149  O O     . ALA A 1 22  ? -23.836 80.304  75.532 1.00 28.41 ? 22   ALA A O     1 
ATOM   150  C CB    . ALA A 1 22  ? -25.955 79.418  73.173 1.00 29.33 ? 22   ALA A CB    1 
ATOM   151  N N     . ARG A 1 23  ? -23.643 78.124  75.003 1.00 24.56 ? 23   ARG A N     1 
ATOM   152  C CA    . ARG A 1 23  ? -23.006 77.765  76.302 1.00 25.86 ? 23   ARG A CA    1 
ATOM   153  C C     . ARG A 1 23  ? -21.672 78.496  76.464 1.00 30.64 ? 23   ARG A C     1 
ATOM   154  O O     . ARG A 1 23  ? -21.335 78.931  77.574 1.00 27.78 ? 23   ARG A O     1 
ATOM   155  C CB    . ARG A 1 23  ? -22.766 76.269  76.337 1.00 27.15 ? 23   ARG A CB    1 
ATOM   156  C CG    . ARG A 1 23  ? -24.074 75.503  76.249 1.00 27.56 ? 23   ARG A CG    1 
ATOM   157  C CD    . ARG A 1 23  ? -23.773 74.120  76.627 1.00 28.31 ? 23   ARG A CD    1 
ATOM   158  N NE    . ARG A 1 23  ? -24.865 73.243  76.375 1.00 27.72 ? 23   ARG A NE    1 
ATOM   159  C CZ    . ARG A 1 23  ? -25.033 72.079  76.966 1.00 34.39 ? 23   ARG A CZ    1 
ATOM   160  N NH1   . ARG A 1 23  ? -24.164 71.650  77.883 1.00 30.38 ? 23   ARG A NH1   1 
ATOM   161  N NH2   . ARG A 1 23  ? -26.092 71.354  76.633 1.00 34.25 ? 23   ARG A NH2   1 
ATOM   162  N N     . ILE A 1 24  ? -20.906 78.633  75.380 1.00 26.97 ? 24   ILE A N     1 
ATOM   163  C CA    . ILE A 1 24  ? -19.571 79.271  75.463 1.00 24.56 ? 24   ILE A CA    1 
ATOM   164  C C     . ILE A 1 24  ? -19.709 80.770  75.673 1.00 24.76 ? 24   ILE A C     1 
ATOM   165  O O     . ILE A 1 24  ? -19.036 81.251  76.529 1.00 24.47 ? 24   ILE A O     1 
ATOM   166  C CB    . ILE A 1 24  ? -18.746 78.960  74.201 1.00 24.46 ? 24   ILE A CB    1 
ATOM   167  C CG1   . ILE A 1 24  ? -18.395 77.478  74.125 1.00 23.86 ? 24   ILE A CG1   1 
ATOM   168  C CG2   . ILE A 1 24  ? -17.531 79.873  74.178 1.00 24.77 ? 24   ILE A CG2   1 
ATOM   169  C CD1   . ILE A 1 24  ? -18.139 76.985  72.714 1.00 25.97 ? 24   ILE A CD1   1 
ATOM   170  N N     . VAL A 1 25  ? -20.489 81.479  74.850 1.00 21.59 ? 25   VAL A N     1 
ATOM   171  C CA    . VAL A 1 25  ? -20.487 82.962  74.841 1.00 23.83 ? 25   VAL A CA    1 
ATOM   172  C C     . VAL A 1 25  ? -21.655 83.500  75.679 1.00 25.07 ? 25   VAL A C     1 
ATOM   173  O O     . VAL A 1 25  ? -21.659 84.685  75.993 1.00 25.34 ? 25   VAL A O     1 
ATOM   174  C CB    . VAL A 1 25  ? -20.500 83.551  73.416 1.00 22.40 ? 25   VAL A CB    1 
ATOM   175  C CG1   . VAL A 1 25  ? -19.246 83.118  72.658 1.00 22.78 ? 25   VAL A CG1   1 
ATOM   176  C CG2   . VAL A 1 25  ? -21.757 83.181  72.631 1.00 23.68 ? 25   VAL A CG2   1 
ATOM   177  N N     . GLY A 1 26  ? -22.633 82.664  76.003 1.00 29.97 ? 26   GLY A N     1 
ATOM   178  C CA    . GLY A 1 26  ? -23.901 83.201  76.526 1.00 33.38 ? 26   GLY A CA    1 
ATOM   179  C C     . GLY A 1 26  ? -24.960 83.301  75.440 1.00 38.96 ? 26   GLY A C     1 
ATOM   180  O O     . GLY A 1 26  ? -24.633 83.650  74.260 1.00 30.52 ? 26   GLY A O     1 
ATOM   181  N N     . ALA A 1 27  ? -26.207 82.991  75.807 1.00 34.06 ? 27   ALA A N     1 
ATOM   182  C CA    . ALA A 1 27  ? -27.297 82.808  74.828 1.00 34.75 ? 27   ALA A CA    1 
ATOM   183  C C     . ALA A 1 27  ? -27.552 84.150  74.156 1.00 27.82 ? 27   ALA A C     1 
ATOM   184  O O     . ALA A 1 27  ? -28.003 84.152  73.035 1.00 34.89 ? 27   ALA A O     1 
ATOM   185  C CB    . ALA A 1 27  ? -28.536 82.256  75.513 1.00 39.42 ? 27   ALA A CB    1 
ATOM   186  N N     . ASP A 1 28  ? -27.225 85.267  74.786 1.00 28.90 ? 28   ASP A N     1 
ATOM   187  C CA    . ASP A 1 28  ? -27.491 86.607  74.177 1.00 31.03 ? 28   ASP A CA    1 
ATOM   188  C C     . ASP A 1 28  ? -26.555 86.887  72.976 1.00 30.39 ? 28   ASP A C     1 
ATOM   189  O O     . ASP A 1 28  ? -26.836 87.858  72.241 1.00 30.92 ? 28   ASP A O     1 
ATOM   190  C CB    . ASP A 1 28  ? -27.273 87.756  75.161 1.00 34.50 ? 28   ASP A CB    1 
ATOM   191  C CG    . ASP A 1 28  ? -28.238 87.800  76.342 1.00 40.94 ? 28   ASP A CG    1 
ATOM   192  O OD1   . ASP A 1 28  ? -29.319 87.228  76.235 1.00 37.60 ? 28   ASP A OD1   1 
ATOM   193  O OD2   . ASP A 1 28  ? -27.875 88.393  77.349 1.00 46.99 ? 28   ASP A OD2   1 
ATOM   194  N N     . TRP A 1 29  ? -25.476 86.102  72.793 1.00 30.29 ? 29   TRP A N     1 
ATOM   195  C CA    . TRP A 1 29  ? -24.366 86.485  71.875 1.00 26.96 ? 29   TRP A CA    1 
ATOM   196  C C     . TRP A 1 29  ? -24.262 85.491  70.727 1.00 26.60 ? 29   TRP A C     1 
ATOM   197  O O     . TRP A 1 29  ? -23.211 85.463  70.030 1.00 25.06 ? 29   TRP A O     1 
ATOM   198  C CB    . TRP A 1 29  ? -23.063 86.603  72.663 1.00 26.42 ? 29   TRP A CB    1 
ATOM   199  C CG    . TRP A 1 29  ? -23.145 87.683  73.682 1.00 25.65 ? 29   TRP A CG    1 
ATOM   200  C CD1   . TRP A 1 29  ? -23.082 87.508  75.031 1.00 27.69 ? 29   TRP A CD1   1 
ATOM   201  C CD2   . TRP A 1 29  ? -23.318 89.088  73.457 1.00 25.17 ? 29   TRP A CD2   1 
ATOM   202  N NE1   . TRP A 1 29  ? -23.197 88.713  75.654 1.00 30.36 ? 29   TRP A NE1   1 
ATOM   203  C CE2   . TRP A 1 29  ? -23.360 89.699  74.725 1.00 26.36 ? 29   TRP A CE2   1 
ATOM   204  C CE3   . TRP A 1 29  ? -23.443 89.896  72.331 1.00 27.03 ? 29   TRP A CE3   1 
ATOM   205  C CZ2   . TRP A 1 29  ? -23.509 91.068  74.896 1.00 29.17 ? 29   TRP A CZ2   1 
ATOM   206  C CZ3   . TRP A 1 29  ? -23.586 91.253  72.492 1.00 29.20 ? 29   TRP A CZ3   1 
ATOM   207  C CH2   . TRP A 1 29  ? -23.623 91.831  73.758 1.00 28.82 ? 29   TRP A CH2   1 
ATOM   208  N N     . VAL A 1 30  ? -25.323 84.731  70.509 1.00 24.94 ? 30   VAL A N     1 
ATOM   209  C CA    . VAL A 1 30  ? -25.515 83.951  69.258 1.00 26.97 ? 30   VAL A CA    1 
ATOM   210  C C     . VAL A 1 30  ? -26.697 84.550  68.526 1.00 26.80 ? 30   VAL A C     1 
ATOM   211  O O     . VAL A 1 30  ? -27.797 84.549  69.056 1.00 27.62 ? 30   VAL A O     1 
ATOM   212  C CB    . VAL A 1 30  ? -25.734 82.467  69.531 1.00 26.55 ? 30   VAL A CB    1 
ATOM   213  C CG1   . VAL A 1 30  ? -26.003 81.707  68.243 1.00 27.94 ? 30   VAL A CG1   1 
ATOM   214  C CG2   . VAL A 1 30  ? -24.568 81.869  70.294 1.00 27.49 ? 30   VAL A CG2   1 
ATOM   215  N N     . PHE A 1 31  ? -26.483 85.012  67.325 1.00 23.05 ? 31   PHE A N     1 
ATOM   216  C CA    . PHE A 1 31  ? -27.465 85.795  66.559 1.00 25.33 ? 31   PHE A CA    1 
ATOM   217  C C     . PHE A 1 31  ? -27.986 84.931  65.432 1.00 28.67 ? 31   PHE A C     1 
ATOM   218  O O     . PHE A 1 31  ? -27.171 84.428  64.633 1.00 26.75 ? 31   PHE A O     1 
ATOM   219  C CB    . PHE A 1 31  ? -26.801 87.071  66.057 1.00 26.01 ? 31   PHE A CB    1 
ATOM   220  C CG    . PHE A 1 31  ? -26.250 87.949  67.158 1.00 28.71 ? 31   PHE A CG    1 
ATOM   221  C CD1   . PHE A 1 31  ? -27.009 88.256  68.269 1.00 31.48 ? 31   PHE A CD1   1 
ATOM   222  C CD2   . PHE A 1 31  ? -24.988 88.527  67.055 1.00 30.28 ? 31   PHE A CD2   1 
ATOM   223  C CE1   . PHE A 1 31  ? -26.519 89.120  69.244 1.00 35.57 ? 31   PHE A CE1   1 
ATOM   224  C CE2   . PHE A 1 31  ? -24.496 89.382  68.033 1.00 31.59 ? 31   PHE A CE2   1 
ATOM   225  C CZ    . PHE A 1 31  ? -25.259 89.668  69.133 1.00 32.03 ? 31   PHE A CZ    1 
ATOM   226  N N     . THR A 1 32  ? -29.305 84.720  65.404 1.00 27.48 ? 32   THR A N     1 
ATOM   227  C CA    . THR A 1 32  ? -29.990 83.960  64.336 1.00 28.66 ? 32   THR A CA    1 
ATOM   228  C C     . THR A 1 32  ? -31.177 84.788  63.846 1.00 33.15 ? 32   THR A C     1 
ATOM   229  O O     . THR A 1 32  ? -31.414 85.867  64.438 1.00 35.41 ? 32   THR A O     1 
ATOM   230  C CB    . THR A 1 32  ? -30.502 82.610  64.841 1.00 30.50 ? 32   THR A CB    1 
ATOM   231  O OG1   . THR A 1 32  ? -31.360 82.926  65.941 1.00 30.91 ? 32   THR A OG1   1 
ATOM   232  C CG2   . THR A 1 32  ? -29.387 81.696  65.268 1.00 32.84 ? 32   THR A CG2   1 
ATOM   233  N N     . GLU A 1 33  ? -31.902 84.300  62.843 1.00 34.91 ? 33   GLU A N     1 
ATOM   234  C CA    . GLU A 1 33  ? -33.174 84.926  62.380 1.00 42.12 ? 33   GLU A CA    1 
ATOM   235  C C     . GLU A 1 33  ? -32.974 86.433  62.177 1.00 38.76 ? 33   GLU A C     1 
ATOM   236  O O     . GLU A 1 33  ? -32.099 86.783  61.391 1.00 35.99 ? 33   GLU A O     1 
ATOM   237  C CB    . GLU A 1 33  ? -34.276 84.634  63.396 1.00 48.72 ? 33   GLU A CB    1 
ATOM   238  C CG    . GLU A 1 33  ? -34.535 83.156  63.574 1.00 57.75 ? 33   GLU A CG    1 
ATOM   239  C CD    . GLU A 1 33  ? -35.663 82.912  64.557 1.00 71.02 ? 33   GLU A CD    1 
ATOM   240  O OE1   . GLU A 1 33  ? -35.443 82.172  65.530 1.00 83.91 ? 33   GLU A OE1   1 
ATOM   241  O OE2   . GLU A 1 33  ? -36.749 83.494  64.360 1.00 85.25 ? 33   GLU A OE2   1 
ATOM   242  N N     . ASP A 1 34  ? -33.716 87.288  62.889 1.00 35.44 ? 34   ASP A N     1 
ATOM   243  C CA    . ASP A 1 34  ? -33.785 88.753  62.623 1.00 41.99 ? 34   ASP A CA    1 
ATOM   244  C C     . ASP A 1 34  ? -32.482 89.427  63.062 1.00 38.05 ? 34   ASP A C     1 
ATOM   245  O O     . ASP A 1 34  ? -32.162 90.502  62.523 1.00 40.83 ? 34   ASP A O     1 
ATOM   246  C CB    . ASP A 1 34  ? -35.025 89.411  63.258 1.00 53.69 ? 34   ASP A CB    1 
ATOM   247  C CG    . ASP A 1 34  ? -35.287 89.056  64.724 1.00 65.50 ? 34   ASP A CG    1 
ATOM   248  O OD1   . ASP A 1 34  ? -35.601 87.865  65.024 1.00 58.55 ? 34   ASP A OD1   1 
ATOM   249  O OD2   . ASP A 1 34  ? -35.212 89.986  65.560 1.00 78.32 ? 34   ASP A OD2   1 
ATOM   250  N N     . LYS A 1 35  ? -31.705 88.825  63.960 1.00 30.18 ? 35   LYS A N     1 
ATOM   251  C CA    . LYS A 1 35  ? -30.474 89.497  64.435 1.00 33.05 ? 35   LYS A CA    1 
ATOM   252  C C     . LYS A 1 35  ? -29.301 89.288  63.443 1.00 33.18 ? 35   LYS A C     1 
ATOM   253  O O     . LYS A 1 35  ? -28.196 89.772  63.731 1.00 31.95 ? 35   LYS A O     1 
ATOM   254  C CB    . LYS A 1 35  ? -30.192 89.041  65.870 1.00 39.05 ? 35   LYS A CB    1 
ATOM   255  C CG    . LYS A 1 35  ? -31.104 89.656  66.931 1.00 42.35 ? 35   LYS A CG    1 
ATOM   256  C CD    . LYS A 1 35  ? -30.499 89.505  68.343 1.00 48.86 ? 35   LYS A CD    1 
ATOM   257  C CE    . LYS A 1 35  ? -31.198 90.290  69.444 1.00 52.62 ? 35   LYS A CE    1 
ATOM   258  N NZ    . LYS A 1 35  ? -30.383 90.375  70.695 1.00 44.82 ? 35   LYS A NZ    1 
ATOM   259  N N     . ILE A 1 36  ? -29.508 88.597  62.317 1.00 31.16 ? 36   ILE A N     1 
ATOM   260  C CA    . ILE A 1 36  ? -28.436 88.319  61.306 1.00 32.19 ? 36   ILE A CA    1 
ATOM   261  C C     . ILE A 1 36  ? -28.261 89.524  60.377 1.00 31.83 ? 36   ILE A C     1 
ATOM   262  O O     . ILE A 1 36  ? -27.206 89.576  59.688 1.00 28.07 ? 36   ILE A O     1 
ATOM   263  C CB    . ILE A 1 36  ? -28.744 87.026  60.519 1.00 37.14 ? 36   ILE A CB    1 
ATOM   264  C CG1   . ILE A 1 36  ? -28.897 85.838  61.469 1.00 51.11 ? 36   ILE A CG1   1 
ATOM   265  C CG2   . ILE A 1 36  ? -27.658 86.722  59.507 1.00 45.09 ? 36   ILE A CG2   1 
ATOM   266  C CD1   . ILE A 1 36  ? -29.522 84.575  60.834 1.00 54.45 ? 36   ILE A CD1   1 
ATOM   267  N N     . THR A 1 37  ? -29.221 90.463  60.294 1.00 30.55 ? 37   THR A N     1 
ATOM   268  C CA    . THR A 1 37  ? -29.246 91.471  59.189 1.00 30.22 ? 37   THR A CA    1 
ATOM   269  C C     . THR A 1 37  ? -27.978 92.320  59.148 1.00 27.63 ? 37   THR A C     1 
ATOM   270  O O     . THR A 1 37  ? -27.482 92.635  58.062 1.00 26.21 ? 37   THR A O     1 
ATOM   271  C CB    . THR A 1 37  ? -30.515 92.346  59.190 1.00 32.52 ? 37   THR A CB    1 
ATOM   272  O OG1   . THR A 1 37  ? -30.582 92.998  60.454 1.00 39.55 ? 37   THR A OG1   1 
ATOM   273  C CG2   . THR A 1 37  ? -31.757 91.508  58.993 1.00 32.66 ? 37   THR A CG2   1 
ATOM   274  N N     . PRO A 1 38  ? -27.351 92.710  60.270 1.00 24.46 ? 38   PRO A N     1 
ATOM   275  C CA    . PRO A 1 38  ? -26.127 93.514  60.171 1.00 27.90 ? 38   PRO A CA    1 
ATOM   276  C C     . PRO A 1 38  ? -24.921 92.801  59.515 1.00 28.38 ? 38   PRO A C     1 
ATOM   277  O O     . PRO A 1 38  ? -23.959 93.459  59.118 1.00 30.91 ? 38   PRO A O     1 
ATOM   278  C CB    . PRO A 1 38  ? -25.779 93.844  61.632 1.00 28.05 ? 38   PRO A CB    1 
ATOM   279  C CG    . PRO A 1 38  ? -27.032 93.515  62.420 1.00 29.96 ? 38   PRO A CG    1 
ATOM   280  C CD    . PRO A 1 38  ? -27.744 92.424  61.648 1.00 27.11 ? 38   PRO A CD    1 
ATOM   281  N N     . TYR A 1 39  ? -24.990 91.474  59.419 1.00 24.99 ? 39   TYR A N     1 
ATOM   282  C CA    . TYR A 1 39  ? -23.923 90.597  58.877 1.00 24.14 ? 39   TYR A CA    1 
ATOM   283  C C     . TYR A 1 39  ? -24.099 90.398  57.382 1.00 24.58 ? 39   TYR A C     1 
ATOM   284  O O     . TYR A 1 39  ? -23.215 89.775  56.775 1.00 24.00 ? 39   TYR A O     1 
ATOM   285  C CB    . TYR A 1 39  ? -23.885 89.262  59.621 1.00 25.07 ? 39   TYR A CB    1 
ATOM   286  C CG    . TYR A 1 39  ? -23.572 89.482  61.074 1.00 25.63 ? 39   TYR A CG    1 
ATOM   287  C CD1   . TYR A 1 39  ? -22.269 89.729  61.487 1.00 27.26 ? 39   TYR A CD1   1 
ATOM   288  C CD2   . TYR A 1 39  ? -24.595 89.599  62.006 1.00 23.60 ? 39   TYR A CD2   1 
ATOM   289  C CE1   . TYR A 1 39  ? -21.958 90.027  62.807 1.00 24.17 ? 39   TYR A CE1   1 
ATOM   290  C CE2   . TYR A 1 39  ? -24.302 89.900  63.320 1.00 25.73 ? 39   TYR A CE2   1 
ATOM   291  C CZ    . TYR A 1 39  ? -22.992 90.094  63.723 1.00 27.31 ? 39   TYR A CZ    1 
ATOM   292  O OH    . TYR A 1 39  ? -22.733 90.347  65.030 1.00 25.07 ? 39   TYR A OH    1 
ATOM   293  N N     . GLU A 1 40  ? -25.197 90.883  56.800 1.00 24.42 ? 40   GLU A N     1 
ATOM   294  C CA    . GLU A 1 40  ? -25.396 90.778  55.333 1.00 25.27 ? 40   GLU A CA    1 
ATOM   295  C C     . GLU A 1 40  ? -24.513 91.844  54.682 1.00 22.02 ? 40   GLU A C     1 
ATOM   296  O O     . GLU A 1 40  ? -24.231 92.861  55.295 1.00 20.76 ? 40   GLU A O     1 
ATOM   297  C CB    . GLU A 1 40  ? -26.867 90.968  54.930 1.00 27.17 ? 40   GLU A CB    1 
ATOM   298  C CG    . GLU A 1 40  ? -27.818 90.015  55.648 1.00 26.34 ? 40   GLU A CG    1 
ATOM   299  C CD    . GLU A 1 40  ? -27.951 88.630  55.054 1.00 28.43 ? 40   GLU A CD    1 
ATOM   300  O OE1   . GLU A 1 40  ? -27.328 88.365  53.993 1.00 26.83 ? 40   GLU A OE1   1 
ATOM   301  O OE2   . GLU A 1 40  ? -28.667 87.798  55.655 1.00 31.37 ? 40   GLU A OE2   1 
ATOM   302  N N     . ASP A 1 41  ? -24.045 91.591  53.470 1.00 22.26 ? 41   ASP A N     1 
ATOM   303  C CA    . ASP A 1 41  ? -23.312 92.614  52.713 1.00 21.50 ? 41   ASP A CA    1 
ATOM   304  C C     . ASP A 1 41  ? -24.257 93.786  52.563 1.00 23.83 ? 41   ASP A C     1 
ATOM   305  O O     . ASP A 1 41  ? -25.321 93.583  52.000 1.00 23.95 ? 41   ASP A O     1 
ATOM   306  C CB    . ASP A 1 41  ? -22.908 92.076  51.351 1.00 21.87 ? 41   ASP A CB    1 
ATOM   307  C CG    . ASP A 1 41  ? -22.056 93.022  50.538 1.00 21.33 ? 41   ASP A CG    1 
ATOM   308  O OD1   . ASP A 1 41  ? -21.863 94.171  50.996 1.00 21.95 ? 41   ASP A OD1   1 
ATOM   309  O OD2   . ASP A 1 41  ? -21.612 92.585  49.427 1.00 21.35 ? 41   ASP A OD2   1 
ATOM   310  N N     . PRO A 1 42  ? -23.924 95.006  53.031 1.00 23.88 ? 42   PRO A N     1 
ATOM   311  C CA    . PRO A 1 42  ? -24.830 96.129  52.805 1.00 26.86 ? 42   PRO A CA    1 
ATOM   312  C C     . PRO A 1 42  ? -24.883 96.525  51.318 1.00 30.26 ? 42   PRO A C     1 
ATOM   313  O O     . PRO A 1 42  ? -25.847 97.153  50.908 1.00 28.66 ? 42   PRO A O     1 
ATOM   314  C CB    . PRO A 1 42  ? -24.195 97.253  53.606 1.00 27.07 ? 42   PRO A CB    1 
ATOM   315  C CG    . PRO A 1 42  ? -22.703 96.914  53.608 1.00 25.65 ? 42   PRO A CG    1 
ATOM   316  C CD    . PRO A 1 42  ? -22.680 95.396  53.719 1.00 24.18 ? 42   PRO A CD    1 
ATOM   317  N N     . TYR A 1 43  ? -23.856 96.169  50.535 1.00 26.75 ? 43   TYR A N     1 
ATOM   318  C CA    . TYR A 1 43  ? -23.727 96.629  49.127 1.00 25.57 ? 43   TYR A CA    1 
ATOM   319  C C     . TYR A 1 43  ? -23.842 95.409  48.211 1.00 27.32 ? 43   TYR A C     1 
ATOM   320  O O     . TYR A 1 43  ? -22.882 95.004  47.549 1.00 27.00 ? 43   TYR A O     1 
ATOM   321  C CB    . TYR A 1 43  ? -22.455 97.437  48.940 1.00 26.00 ? 43   TYR A CB    1 
ATOM   322  C CG    . TYR A 1 43  ? -22.240 98.642  49.831 1.00 25.12 ? 43   TYR A CG    1 
ATOM   323  C CD1   . TYR A 1 43  ? -23.264 99.406  50.361 1.00 26.81 ? 43   TYR A CD1   1 
ATOM   324  C CD2   . TYR A 1 43  ? -20.956 99.081  50.074 1.00 24.31 ? 43   TYR A CD2   1 
ATOM   325  C CE1   . TYR A 1 43  ? -23.015 100.500 51.177 1.00 26.75 ? 43   TYR A CE1   1 
ATOM   326  C CE2   . TYR A 1 43  ? -20.688 100.173 50.878 1.00 25.42 ? 43   TYR A CE2   1 
ATOM   327  C CZ    . TYR A 1 43  ? -21.718 100.896 51.435 1.00 26.92 ? 43   TYR A CZ    1 
ATOM   328  O OH    . TYR A 1 43  ? -21.442 101.969 52.250 1.00 29.65 ? 43   TYR A OH    1 
ATOM   329  N N     . THR A 1 44  ? -25.067 94.885  48.150 1.00 27.27 ? 44   THR A N     1 
ATOM   330  C CA    . THR A 1 44  ? -25.440 93.676  47.393 1.00 27.38 ? 44   THR A CA    1 
ATOM   331  C C     . THR A 1 44  ? -24.955 93.790  45.945 1.00 26.75 ? 44   THR A C     1 
ATOM   332  O O     . THR A 1 44  ? -25.071 94.888  45.346 1.00 25.64 ? 44   THR A O     1 
ATOM   333  C CB    . THR A 1 44  ? -26.958 93.475  47.409 1.00 30.45 ? 44   THR A CB    1 
ATOM   334  O OG1   . THR A 1 44  ? -27.449 93.737  48.726 1.00 27.74 ? 44   THR A OG1   1 
ATOM   335  C CG2   . THR A 1 44  ? -27.323 92.066  47.002 1.00 31.24 ? 44   THR A CG2   1 
ATOM   336  N N     . ILE A 1 45  ? -24.446 92.690  45.415 1.00 25.10 ? 45   ILE A N     1 
ATOM   337  C CA    . ILE A 1 45  ? -24.040 92.579  43.983 1.00 25.66 ? 45   ILE A CA    1 
ATOM   338  C C     . ILE A 1 45  ? -24.871 91.480  43.328 1.00 30.05 ? 45   ILE A C     1 
ATOM   339  O O     . ILE A 1 45  ? -25.442 91.749  42.256 1.00 29.14 ? 45   ILE A O     1 
ATOM   340  C CB    . ILE A 1 45  ? -22.531 92.346  43.842 1.00 26.39 ? 45   ILE A CB    1 
ATOM   341  C CG1   . ILE A 1 45  ? -21.736 93.493  44.468 1.00 25.75 ? 45   ILE A CG1   1 
ATOM   342  C CG2   . ILE A 1 45  ? -22.170 92.112  42.375 1.00 24.82 ? 45   ILE A CG2   1 
ATOM   343  C CD1   . ILE A 1 45  ? -20.226 93.364  44.322 1.00 27.58 ? 45   ILE A CD1   1 
ATOM   344  N N     . SER A 1 46  ? -24.913 90.289  43.911 1.00 29.60 ? 46   SER A N     1 
ATOM   345  C CA    . SER A 1 46  ? -25.651 89.132  43.341 1.00 32.18 ? 46   SER A CA    1 
ATOM   346  C C     . SER A 1 46  ? -27.146 89.462  43.252 1.00 33.09 ? 46   SER A C     1 
ATOM   347  O O     . SER A 1 46  ? -27.687 90.138  44.156 1.00 30.25 ? 46   SER A O     1 
ATOM   348  C CB    . SER A 1 46  ? -25.431 87.886  44.141 1.00 33.31 ? 46   SER A CB    1 
ATOM   349  O OG    . SER A 1 46  ? -26.004 86.762  43.495 1.00 32.23 ? 46   SER A OG    1 
ATOM   350  N N     . ASN A 1 47  ? -27.785 88.939  42.217 1.00 33.20 ? 47   ASN A N     1 
ATOM   351  C CA    . ASN A 1 47  ? -29.255 88.861  42.070 1.00 35.23 ? 47   ASN A CA    1 
ATOM   352  C C     . ASN A 1 47  ? -29.743 87.495  42.532 1.00 35.94 ? 47   ASN A C     1 
ATOM   353  O O     . ASN A 1 47  ? -30.929 87.285  42.517 1.00 32.65 ? 47   ASN A O     1 
ATOM   354  C CB    . ASN A 1 47  ? -29.657 89.167  40.623 1.00 35.60 ? 47   ASN A CB    1 
ATOM   355  C CG    . ASN A 1 47  ? -29.627 90.657  40.383 1.00 36.83 ? 47   ASN A CG    1 
ATOM   356  O OD1   . ASN A 1 47  ? -29.844 91.439  41.314 1.00 31.26 ? 47   ASN A OD1   1 
ATOM   357  N ND2   . ASN A 1 47  ? -29.367 91.061  39.148 1.00 36.41 ? 47   ASN A ND2   1 
ATOM   358  N N     . ASP A 1 48  ? -28.859 86.646  43.046 1.00 34.95 ? 48   ASP A N     1 
ATOM   359  C CA    . ASP A 1 48  ? -29.247 85.352  43.640 1.00 33.69 ? 48   ASP A CA    1 
ATOM   360  C C     . ASP A 1 48  ? -29.261 85.504  45.161 1.00 36.23 ? 48   ASP A C     1 
ATOM   361  O O     . ASP A 1 48  ? -28.193 85.538  45.785 1.00 35.56 ? 48   ASP A O     1 
ATOM   362  C CB    . ASP A 1 48  ? -28.317 84.247  43.144 1.00 34.43 ? 48   ASP A CB    1 
ATOM   363  C CG    . ASP A 1 48  ? -28.710 82.858  43.606 1.00 35.46 ? 48   ASP A CG    1 
ATOM   364  O OD1   . ASP A 1 48  ? -29.440 82.747  44.619 1.00 33.33 ? 48   ASP A OD1   1 
ATOM   365  O OD2   . ASP A 1 48  ? -28.249 81.899  42.971 1.00 36.65 ? 48   ASP A OD2   1 
ATOM   366  N N     . GLU A 1 49  ? -30.449 85.483  45.741 1.00 36.22 ? 49   GLU A N     1 
ATOM   367  C CA    . GLU A 1 49  ? -30.676 85.644  47.193 1.00 38.22 ? 49   GLU A CA    1 
ATOM   368  C C     . GLU A 1 49  ? -30.071 84.491  47.984 1.00 31.76 ? 49   GLU A C     1 
ATOM   369  O O     . GLU A 1 49  ? -30.065 84.618  49.209 1.00 34.54 ? 49   GLU A O     1 
ATOM   370  C CB    . GLU A 1 49  ? -32.168 85.700  47.499 1.00 46.18 ? 49   GLU A CB    1 
ATOM   371  C CG    . GLU A 1 49  ? -32.741 87.062  47.210 1.00 58.82 ? 49   GLU A CG    1 
ATOM   372  C CD    . GLU A 1 49  ? -34.028 87.308  47.959 1.00 70.69 ? 49   GLU A CD    1 
ATOM   373  O OE1   . GLU A 1 49  ? -34.163 86.773  49.095 1.00 79.27 ? 49   GLU A OE1   1 
ATOM   374  O OE2   . GLU A 1 49  ? -34.873 88.030  47.407 1.00 80.71 ? 49   GLU A OE2   1 
ATOM   375  N N     . THR A 1 50  ? -29.625 83.408  47.353 1.00 28.48 ? 50   THR A N     1 
ATOM   376  C CA    . THR A 1 50  ? -29.012 82.279  48.105 1.00 33.01 ? 50   THR A CA    1 
ATOM   377  C C     . THR A 1 50  ? -27.496 82.508  48.272 1.00 30.52 ? 50   THR A C     1 
ATOM   378  O O     . THR A 1 50  ? -26.872 81.657  48.891 1.00 30.59 ? 50   THR A O     1 
ATOM   379  C CB    . THR A 1 50  ? -29.254 80.899  47.479 1.00 31.69 ? 50   THR A CB    1 
ATOM   380  O OG1   . THR A 1 50  ? -28.587 80.819  46.225 1.00 31.70 ? 50   THR A OG1   1 
ATOM   381  C CG2   . THR A 1 50  ? -30.719 80.563  47.318 1.00 35.93 ? 50   THR A CG2   1 
ATOM   382  N N     . GLU A 1 51  ? -26.923 83.596  47.752 1.00 27.65 ? 51   GLU A N     1 
ATOM   383  C CA    . GLU A 1 51  ? -25.432 83.745  47.742 1.00 29.83 ? 51   GLU A CA    1 
ATOM   384  C C     . GLU A 1 51  ? -24.964 84.676  48.864 1.00 26.24 ? 51   GLU A C     1 
ATOM   385  O O     . GLU A 1 51  ? -25.635 85.685  49.117 1.00 25.62 ? 51   GLU A O     1 
ATOM   386  C CB    . GLU A 1 51  ? -24.944 84.173  46.357 1.00 32.72 ? 51   GLU A CB    1 
ATOM   387  C CG    . GLU A 1 51  ? -25.112 83.067  45.298 1.00 32.99 ? 51   GLU A CG    1 
ATOM   388  C CD    . GLU A 1 51  ? -24.483 83.366  43.947 1.00 37.06 ? 51   GLU A CD    1 
ATOM   389  O OE1   . GLU A 1 51  ? -24.627 84.493  43.444 1.00 36.98 ? 51   GLU A OE1   1 
ATOM   390  O OE2   . GLU A 1 51  ? -23.895 82.458  43.377 1.00 40.80 ? 51   GLU A OE2   1 
ATOM   391  N N     . HIS A 1 52  ? -23.827 84.327  49.492 1.00 25.46 ? 52   HIS A N     1 
ATOM   392  C CA    . HIS A 1 52  ? -23.107 85.157  50.492 1.00 24.32 ? 52   HIS A CA    1 
ATOM   393  C C     . HIS A 1 52  ? -24.000 85.420  51.713 1.00 23.43 ? 52   HIS A C     1 
ATOM   394  O O     . HIS A 1 52  ? -23.859 86.477  52.345 1.00 27.59 ? 52   HIS A O     1 
ATOM   395  C CB    . HIS A 1 52  ? -22.540 86.431  49.847 1.00 26.79 ? 52   HIS A CB    1 
ATOM   396  C CG    . HIS A 1 52  ? -21.900 86.220  48.502 1.00 28.58 ? 52   HIS A CG    1 
ATOM   397  N ND1   . HIS A 1 52  ? -20.827 85.393  48.320 1.00 33.28 ? 52   HIS A ND1   1 
ATOM   398  C CD2   . HIS A 1 52  ? -22.209 86.714  47.271 1.00 32.64 ? 52   HIS A CD2   1 
ATOM   399  C CE1   . HIS A 1 52  ? -20.512 85.375  47.032 1.00 36.02 ? 52   HIS A CE1   1 
ATOM   400  N NE2   . HIS A 1 52  ? -21.362 86.162  46.356 1.00 34.07 ? 52   HIS A NE2   1 
ATOM   401  N N     . ARG A 1 53  ? -24.831 84.440  52.090 1.00 25.14 ? 53   ARG A N     1 
ATOM   402  C CA    . ARG A 1 53  ? -25.751 84.551  53.245 1.00 23.76 ? 53   ARG A CA    1 
ATOM   403  C C     . ARG A 1 53  ? -25.157 83.864  54.481 1.00 22.66 ? 53   ARG A C     1 
ATOM   404  O O     . ARG A 1 53  ? -25.019 82.644  54.527 1.00 23.52 ? 53   ARG A O     1 
ATOM   405  C CB    . ARG A 1 53  ? -27.092 83.883  52.913 1.00 26.90 ? 53   ARG A CB    1 
ATOM   406  C CG    . ARG A 1 53  ? -27.693 84.302  51.578 1.00 27.99 ? 53   ARG A CG    1 
ATOM   407  C CD    . ARG A 1 53  ? -27.908 85.805  51.416 1.00 28.90 ? 53   ARG A CD    1 
ATOM   408  N NE    . ARG A 1 53  ? -28.687 86.363  52.495 1.00 29.82 ? 53   ARG A NE    1 
ATOM   409  C CZ    . ARG A 1 53  ? -29.991 86.119  52.707 1.00 35.45 ? 53   ARG A CZ    1 
ATOM   410  N NH1   . ARG A 1 53  ? -30.687 85.344  51.887 1.00 31.56 ? 53   ARG A NH1   1 
ATOM   411  N NH2   . ARG A 1 53  ? -30.594 86.642  53.755 1.00 33.48 ? 53   ARG A NH2   1 
ATOM   412  N N     . PRO A 1 54  ? -24.897 84.627  55.554 1.00 21.70 ? 54   PRO A N     1 
ATOM   413  C CA    . PRO A 1 54  ? -24.430 84.053  56.801 1.00 23.94 ? 54   PRO A CA    1 
ATOM   414  C C     . PRO A 1 54  ? -25.636 83.329  57.432 1.00 26.19 ? 54   PRO A C     1 
ATOM   415  O O     . PRO A 1 54  ? -26.743 83.870  57.416 1.00 29.28 ? 54   PRO A O     1 
ATOM   416  C CB    . PRO A 1 54  ? -23.960 85.276  57.602 1.00 21.56 ? 54   PRO A CB    1 
ATOM   417  C CG    . PRO A 1 54  ? -24.758 86.417  57.078 1.00 22.66 ? 54   PRO A CG    1 
ATOM   418  C CD    . PRO A 1 54  ? -25.076 86.085  55.637 1.00 22.64 ? 54   PRO A CD    1 
ATOM   419  N N     . TYR A 1 55  ? -25.411 82.155  57.998 1.00 25.19 ? 55   TYR A N     1 
ATOM   420  C CA    . TYR A 1 55  ? -26.453 81.379  58.703 1.00 27.24 ? 55   TYR A CA    1 
ATOM   421  C C     . TYR A 1 55  ? -26.798 81.987  60.065 1.00 30.00 ? 55   TYR A C     1 
ATOM   422  O O     . TYR A 1 55  ? -27.937 81.860  60.530 1.00 28.96 ? 55   TYR A O     1 
ATOM   423  C CB    . TYR A 1 55  ? -26.020 79.942  58.931 1.00 28.52 ? 55   TYR A CB    1 
ATOM   424  C CG    . TYR A 1 55  ? -27.200 79.058  59.200 1.00 30.09 ? 55   TYR A CG    1 
ATOM   425  C CD1   . TYR A 1 55  ? -27.941 78.540  58.147 1.00 34.30 ? 55   TYR A CD1   1 
ATOM   426  C CD2   . TYR A 1 55  ? -27.596 78.770  60.496 1.00 35.22 ? 55   TYR A CD2   1 
ATOM   427  C CE1   . TYR A 1 55  ? -29.048 77.746  58.366 1.00 34.68 ? 55   TYR A CE1   1 
ATOM   428  C CE2   . TYR A 1 55  ? -28.713 77.986  60.739 1.00 37.58 ? 55   TYR A CE2   1 
ATOM   429  C CZ    . TYR A 1 55  ? -29.443 77.495  59.668 1.00 39.33 ? 55   TYR A CZ    1 
ATOM   430  O OH    . TYR A 1 55  ? -30.523 76.702  59.845 1.00 48.85 ? 55   TYR A OH    1 
ATOM   431  N N     . ALA A 1 56  ? -25.802 82.570  60.714 1.00 23.94 ? 56   ALA A N     1 
ATOM   432  C CA    . ALA A 1 56  ? -25.832 82.987  62.125 1.00 24.93 ? 56   ALA A CA    1 
ATOM   433  C C     . ALA A 1 56  ? -24.559 83.773  62.391 1.00 23.79 ? 56   ALA A C     1 
ATOM   434  O O     . ALA A 1 56  ? -23.631 83.772  61.544 1.00 22.53 ? 56   ALA A O     1 
ATOM   435  C CB    . ALA A 1 56  ? -25.944 81.790  63.042 1.00 25.63 ? 56   ALA A CB    1 
ATOM   436  N N     . ALA A 1 57  ? -24.472 84.362  63.563 1.00 24.71 ? 57   ALA A N     1 
ATOM   437  C CA    . ALA A 1 57  ? -23.220 84.945  64.045 1.00 20.79 ? 57   ALA A CA    1 
ATOM   438  C C     . ALA A 1 57  ? -23.062 84.600  65.521 1.00 25.80 ? 57   ALA A C     1 
ATOM   439  O O     . ALA A 1 57  ? -24.079 84.438  66.231 1.00 26.06 ? 57   ALA A O     1 
ATOM   440  C CB    . ALA A 1 57  ? -23.230 86.419  63.818 1.00 21.66 ? 57   ALA A CB    1 
ATOM   441  N N     . VAL A 1 58  ? -21.819 84.587  65.969 1.00 22.74 ? 58   VAL A N     1 
ATOM   442  C CA    . VAL A 1 58  ? -21.458 84.365  67.387 1.00 21.08 ? 58   VAL A CA    1 
ATOM   443  C C     . VAL A 1 58  ? -20.420 85.424  67.768 1.00 25.00 ? 58   VAL A C     1 
ATOM   444  O O     . VAL A 1 58  ? -19.473 85.691  66.990 1.00 23.42 ? 58   VAL A O     1 
ATOM   445  C CB    . VAL A 1 58  ? -20.984 82.924  67.610 1.00 22.07 ? 58   VAL A CB    1 
ATOM   446  C CG1   . VAL A 1 58  ? -19.800 82.523  66.740 1.00 25.85 ? 58   VAL A CG1   1 
ATOM   447  C CG2   . VAL A 1 58  ? -20.657 82.673  69.073 1.00 24.06 ? 58   VAL A CG2   1 
ATOM   448  N N     . ALA A 1 59  ? -20.645 86.077  68.900 1.00 21.00 ? 59   ALA A N     1 
ATOM   449  C CA    . ALA A 1 59  ? -19.880 87.262  69.336 1.00 22.50 ? 59   ALA A CA    1 
ATOM   450  C C     . ALA A 1 59  ? -19.144 86.972  70.638 1.00 21.59 ? 59   ALA A C     1 
ATOM   451  O O     . ALA A 1 59  ? -19.623 87.275  71.717 1.00 21.34 ? 59   ALA A O     1 
ATOM   452  C CB    . ALA A 1 59  ? -20.810 88.439  69.394 1.00 23.36 ? 59   ALA A CB    1 
ATOM   453  N N     . PRO A 1 60  ? -17.955 86.339  70.579 1.00 20.79 ? 60   PRO A N     1 
ATOM   454  C CA    . PRO A 1 60  ? -17.191 86.025  71.790 1.00 21.49 ? 60   PRO A CA    1 
ATOM   455  C C     . PRO A 1 60  ? -16.560 87.255  72.446 1.00 20.78 ? 60   PRO A C     1 
ATOM   456  O O     . PRO A 1 60  ? -16.330 88.240  71.762 1.00 25.82 ? 60   PRO A O     1 
ATOM   457  C CB    . PRO A 1 60  ? -16.108 85.059  71.299 1.00 22.00 ? 60   PRO A CB    1 
ATOM   458  C CG    . PRO A 1 60  ? -15.899 85.518  69.860 1.00 21.32 ? 60   PRO A CG    1 
ATOM   459  C CD    . PRO A 1 60  ? -17.302 85.806  69.368 1.00 23.15 ? 60   PRO A CD    1 
ATOM   460  N N     . ALA A 1 61  ? -16.193 87.134  73.716 1.00 22.84 ? 61   ALA A N     1 
ATOM   461  C CA    . ALA A 1 61  ? -15.552 88.226  74.484 1.00 24.47 ? 61   ALA A CA    1 
ATOM   462  C C     . ALA A 1 61  ? -14.141 87.857  74.961 1.00 21.91 ? 61   ALA A C     1 
ATOM   463  O O     . ALA A 1 61  ? -13.560 88.663  75.665 1.00 23.89 ? 61   ALA A O     1 
ATOM   464  C CB    . ALA A 1 61  ? -16.424 88.633  75.671 1.00 29.55 ? 61   ALA A CB    1 
ATOM   465  N N     . SER A 1 62  ? -13.569 86.714  74.606 1.00 21.96 ? 62   SER A N     1 
ATOM   466  C CA    . SER A 1 62  ? -12.207 86.320  75.036 1.00 19.56 ? 62   SER A CA    1 
ATOM   467  C C     . SER A 1 62  ? -11.587 85.347  74.043 1.00 20.02 ? 62   SER A C     1 
ATOM   468  O O     . SER A 1 62  ? -12.330 84.612  73.318 1.00 22.68 ? 62   SER A O     1 
ATOM   469  C CB    . SER A 1 62  ? -12.254 85.702  76.431 1.00 21.39 ? 62   SER A CB    1 
ATOM   470  O OG    . SER A 1 62  ? -12.781 84.384  76.347 1.00 21.10 ? 62   SER A OG    1 
ATOM   471  N N     . THR A 1 63  ? -10.269 85.270  74.023 1.00 20.92 ? 63   THR A N     1 
ATOM   472  C CA    . THR A 1 63  ? -9.533  84.250  73.240 1.00 21.70 ? 63   THR A CA    1 
ATOM   473  C C     . THR A 1 63  ? -10.036 82.856  73.626 1.00 22.05 ? 63   THR A C     1 
ATOM   474  O O     . THR A 1 63  ? -10.228 82.028  72.779 1.00 19.88 ? 63   THR A O     1 
ATOM   475  C CB    . THR A 1 63  ? -8.024  84.407  73.459 1.00 21.36 ? 63   THR A CB    1 
ATOM   476  O OG1   . THR A 1 63  ? -7.731  85.685  72.905 1.00 23.38 ? 63   THR A OG1   1 
ATOM   477  C CG2   . THR A 1 63  ? -7.212  83.339  72.774 1.00 23.26 ? 63   THR A CG2   1 
ATOM   478  N N     . GLU A 1 64  ? -10.247 82.596  74.912 1.00 22.32 ? 64   GLU A N     1 
ATOM   479  C CA    . GLU A 1 64  ? -10.727 81.263  75.344 1.00 21.90 ? 64   GLU A CA    1 
ATOM   480  C C     . GLU A 1 64  ? -12.041 80.932  74.645 1.00 17.92 ? 64   GLU A C     1 
ATOM   481  O O     . GLU A 1 64  ? -12.205 79.779  74.170 1.00 20.88 ? 64   GLU A O     1 
ATOM   482  C CB    . GLU A 1 64  ? -10.888 81.234  76.871 1.00 23.46 ? 64   GLU A CB    1 
ATOM   483  C CG    . GLU A 1 64  ? -11.433 79.874  77.274 1.00 28.15 ? 64   GLU A CG    1 
ATOM   484  C CD    . GLU A 1 64  ? -11.829 79.733  78.735 1.00 30.58 ? 64   GLU A CD    1 
ATOM   485  O OE1   . GLU A 1 64  ? -11.636 80.698  79.461 1.00 25.56 ? 64   GLU A OE1   1 
ATOM   486  O OE2   . GLU A 1 64  ? -12.364 78.660  79.086 1.00 34.97 ? 64   GLU A OE2   1 
ATOM   487  N N     . GLU A 1 65  ? -12.951 81.892  74.556 1.00 18.74 ? 65   GLU A N     1 
ATOM   488  C CA    . GLU A 1 65  ? -14.271 81.664  73.870 1.00 20.55 ? 65   GLU A CA    1 
ATOM   489  C C     . GLU A 1 65  ? -14.043 81.369  72.369 1.00 22.09 ? 65   GLU A C     1 
ATOM   490  O O     . GLU A 1 65  ? -14.690 80.469  71.803 1.00 19.80 ? 65   GLU A O     1 
ATOM   491  C CB    . GLU A 1 65  ? -15.161 82.882  74.054 1.00 20.93 ? 65   GLU A CB    1 
ATOM   492  C CG    . GLU A 1 65  ? -15.757 82.925  75.459 1.00 23.36 ? 65   GLU A CG    1 
ATOM   493  C CD    . GLU A 1 65  ? -16.581 84.129  75.876 1.00 24.76 ? 65   GLU A CD    1 
ATOM   494  O OE1   . GLU A 1 65  ? -17.209 84.824  75.060 1.00 24.46 ? 65   GLU A OE1   1 
ATOM   495  O OE2   . GLU A 1 65  ? -16.686 84.291  77.093 1.00 34.70 ? 65   GLU A OE2   1 
ATOM   496  N N     . VAL A 1 66  ? -13.129 82.117  71.748 1.00 22.02 ? 66   VAL A N     1 
ATOM   497  C CA    . VAL A 1 66  ? -12.746 81.888  70.324 1.00 19.98 ? 66   VAL A CA    1 
ATOM   498  C C     . VAL A 1 66  ? -12.259 80.447  70.205 1.00 18.54 ? 66   VAL A C     1 
ATOM   499  O O     . VAL A 1 66  ? -12.706 79.775  69.285 1.00 19.50 ? 66   VAL A O     1 
ATOM   500  C CB    . VAL A 1 66  ? -11.683 82.891  69.834 1.00 19.06 ? 66   VAL A CB    1 
ATOM   501  C CG1   . VAL A 1 66  ? -11.176 82.472  68.461 1.00 20.47 ? 66   VAL A CG1   1 
ATOM   502  C CG2   . VAL A 1 66  ? -12.219 84.294  69.831 1.00 18.20 ? 66   VAL A CG2   1 
ATOM   503  N N     . GLN A 1 67  ? -11.367 79.981  71.091 1.00 17.93 ? 67   GLN A N     1 
ATOM   504  C CA    . GLN A 1 67  ? -10.825 78.606  71.031 1.00 18.68 ? 67   GLN A CA    1 
ATOM   505  C C     . GLN A 1 67  ? -11.958 77.554  71.147 1.00 20.88 ? 67   GLN A C     1 
ATOM   506  O O     . GLN A 1 67  ? -11.973 76.575  70.364 1.00 18.69 ? 67   GLN A O     1 
ATOM   507  C CB    . GLN A 1 67  ? -9.813  78.372  72.146 1.00 19.70 ? 67   GLN A CB    1 
ATOM   508  C CG    . GLN A 1 67  ? -8.537  79.186  72.015 1.00 20.70 ? 67   GLN A CG    1 
ATOM   509  C CD    . GLN A 1 67  ? -7.664  78.849  73.190 1.00 21.72 ? 67   GLN A CD    1 
ATOM   510  O OE1   . GLN A 1 67  ? -7.687  79.527  74.192 1.00 21.77 ? 67   GLN A OE1   1 
ATOM   511  N NE2   . GLN A 1 67  ? -6.913  77.783  73.069 1.00 20.69 ? 67   GLN A NE2   1 
ATOM   512  N N     . GLU A 1 68  ? -12.902 77.747  72.051 1.00 20.71 ? 68   GLU A N     1 
ATOM   513  C CA    . GLU A 1 68  ? -13.997 76.768  72.259 1.00 23.37 ? 68   GLU A CA    1 
ATOM   514  C C     . GLU A 1 68  ? -14.962 76.794  71.061 1.00 22.01 ? 68   GLU A C     1 
ATOM   515  O O     . GLU A 1 68  ? -15.446 75.709  70.689 1.00 21.42 ? 68   GLU A O     1 
ATOM   516  C CB    . GLU A 1 68  ? -14.720 77.081  73.572 1.00 25.35 ? 68   GLU A CB    1 
ATOM   517  C CG    . GLU A 1 68  ? -13.803 76.994  74.770 1.00 29.02 ? 68   GLU A CG    1 
ATOM   518  C CD    . GLU A 1 68  ? -13.451 75.603  75.250 1.00 36.19 ? 68   GLU A CD    1 
ATOM   519  O OE1   . GLU A 1 68  ? -13.048 74.728  74.462 1.00 37.75 ? 68   GLU A OE1   1 
ATOM   520  O OE2   . GLU A 1 68  ? -13.590 75.397  76.450 1.00 48.85 ? 68   GLU A OE2   1 
ATOM   521  N N     . ILE A 1 69  ? -15.241 77.967  70.491 1.00 21.39 ? 69   ILE A N     1 
ATOM   522  C CA    . ILE A 1 69  ? -16.057 78.066  69.236 1.00 21.32 ? 69   ILE A CA    1 
ATOM   523  C C     . ILE A 1 69  ? -15.343 77.244  68.155 1.00 20.56 ? 69   ILE A C     1 
ATOM   524  O O     . ILE A 1 69  ? -16.006 76.459  67.436 1.00 22.32 ? 69   ILE A O     1 
ATOM   525  C CB    . ILE A 1 69  ? -16.301 79.516  68.836 1.00 21.71 ? 69   ILE A CB    1 
ATOM   526  C CG1   . ILE A 1 69  ? -17.217 80.205  69.847 1.00 21.72 ? 69   ILE A CG1   1 
ATOM   527  C CG2   . ILE A 1 69  ? -16.883 79.678  67.425 1.00 22.94 ? 69   ILE A CG2   1 
ATOM   528  C CD1   . ILE A 1 69  ? -17.112 81.694  69.841 1.00 21.47 ? 69   ILE A CD1   1 
ATOM   529  N N     . VAL A 1 70  ? -14.049 77.452  67.979 1.00 19.56 ? 70   VAL A N     1 
ATOM   530  C CA    . VAL A 1 70  ? -13.310 76.733  66.895 1.00 20.28 ? 70   VAL A CA    1 
ATOM   531  C C     . VAL A 1 70  ? -13.356 75.223  67.166 1.00 21.01 ? 70   VAL A C     1 
ATOM   532  O O     . VAL A 1 70  ? -13.537 74.410  66.234 1.00 20.06 ? 70   VAL A O     1 
ATOM   533  C CB    . VAL A 1 70  ? -11.877 77.270  66.767 1.00 19.52 ? 70   VAL A CB    1 
ATOM   534  C CG1   . VAL A 1 70  ? -11.024 76.355  65.918 1.00 21.17 ? 70   VAL A CG1   1 
ATOM   535  C CG2   . VAL A 1 70  ? -11.875 78.683  66.218 1.00 19.87 ? 70   VAL A CG2   1 
ATOM   536  N N     . ARG A 1 71  ? -13.168 74.798  68.411 1.00 21.40 ? 71   ARG A N     1 
ATOM   537  C CA    . ARG A 1 71  ? -13.244 73.337  68.729 1.00 22.39 ? 71   ARG A CA    1 
ATOM   538  C C     . ARG A 1 71  ? -14.637 72.795  68.376 1.00 20.57 ? 71   ARG A C     1 
ATOM   539  O O     . ARG A 1 71  ? -14.717 71.691  67.809 1.00 21.93 ? 71   ARG A O     1 
ATOM   540  C CB    . ARG A 1 71  ? -12.901 73.121  70.209 1.00 21.72 ? 71   ARG A CB    1 
ATOM   541  C CG    . ARG A 1 71  ? -11.420 73.281  70.502 1.00 23.51 ? 71   ARG A CG    1 
ATOM   542  C CD    . ARG A 1 71  ? -11.175 73.631  71.950 1.00 24.76 ? 71   ARG A CD    1 
ATOM   543  N NE    . ARG A 1 71  ? -9.755  73.798  72.169 1.00 26.34 ? 71   ARG A NE    1 
ATOM   544  C CZ    . ARG A 1 71  ? -9.218  74.434  73.214 1.00 27.57 ? 71   ARG A CZ    1 
ATOM   545  N NH1   . ARG A 1 71  ? -9.967  74.943  74.167 1.00 28.37 ? 71   ARG A NH1   1 
ATOM   546  N NH2   . ARG A 1 71  ? -7.907  74.522  73.326 1.00 29.38 ? 71   ARG A NH2   1 
ATOM   547  N N     . VAL A 1 72  ? -15.692 73.524  68.716 1.00 21.05 ? 72   VAL A N     1 
ATOM   548  C CA    . VAL A 1 72  ? -17.078 73.047  68.432 1.00 24.29 ? 72   VAL A CA    1 
ATOM   549  C C     . VAL A 1 72  ? -17.270 73.023  66.916 1.00 22.75 ? 72   VAL A C     1 
ATOM   550  O O     . VAL A 1 72  ? -17.840 72.066  66.385 1.00 25.87 ? 72   VAL A O     1 
ATOM   551  C CB    . VAL A 1 72  ? -18.117 73.939  69.144 1.00 23.93 ? 72   VAL A CB    1 
ATOM   552  C CG1   . VAL A 1 72  ? -19.512 73.742  68.597 1.00 25.24 ? 72   VAL A CG1   1 
ATOM   553  C CG2   . VAL A 1 72  ? -18.085 73.706  70.643 1.00 24.13 ? 72   VAL A CG2   1 
ATOM   554  N N     . ALA A 1 73  ? -16.752 74.015  66.202 1.00 22.42 ? 73   ALA A N     1 
ATOM   555  C CA    . ALA A 1 73  ? -16.891 74.051  64.730 1.00 20.91 ? 73   ALA A CA    1 
ATOM   556  C C     . ALA A 1 73  ? -16.306 72.779  64.139 1.00 20.90 ? 73   ALA A C     1 
ATOM   557  O O     . ALA A 1 73  ? -16.921 72.191  63.216 1.00 23.77 ? 73   ALA A O     1 
ATOM   558  C CB    . ALA A 1 73  ? -16.252 75.313  64.173 1.00 22.32 ? 73   ALA A CB    1 
ATOM   559  N N     . ASN A 1 74  ? -15.149 72.340  64.628 1.00 21.25 ? 74   ASN A N     1 
ATOM   560  C CA    . ASN A 1 74  ? -14.484 71.111  64.123 1.00 23.01 ? 74   ASN A CA    1 
ATOM   561  C C     . ASN A 1 74  ? -15.365 69.886  64.420 1.00 25.52 ? 74   ASN A C     1 
ATOM   562  O O     . ASN A 1 74  ? -15.521 69.001  63.544 1.00 23.64 ? 74   ASN A O     1 
ATOM   563  C CB    . ASN A 1 74  ? -13.114 70.869  64.758 1.00 20.94 ? 74   ASN A CB    1 
ATOM   564  C CG    . ASN A 1 74  ? -12.028 71.648  64.043 1.00 23.63 ? 74   ASN A CG    1 
ATOM   565  O OD1   . ASN A 1 74  ? -11.617 71.272  62.961 1.00 21.02 ? 74   ASN A OD1   1 
ATOM   566  N ND2   . ASN A 1 74  ? -11.611 72.769  64.610 1.00 22.18 ? 74   ASN A ND2   1 
ATOM   567  N N     . GLU A 1 75  ? -15.952 69.859  65.601 1.00 25.66 ? 75   GLU A N     1 
ATOM   568  C CA    . GLU A 1 75  ? -16.733 68.685  66.051 1.00 30.02 ? 75   GLU A CA    1 
ATOM   569  C C     . GLU A 1 75  ? -17.934 68.493  65.120 1.00 28.77 ? 75   GLU A C     1 
ATOM   570  O O     . GLU A 1 75  ? -18.213 67.358  64.743 1.00 28.98 ? 75   GLU A O     1 
ATOM   571  C CB    . GLU A 1 75  ? -17.114 68.890  67.513 1.00 33.22 ? 75   GLU A CB    1 
ATOM   572  C CG    . GLU A 1 75  ? -17.511 67.581  68.161 1.00 44.60 ? 75   GLU A CG    1 
ATOM   573  C CD    . GLU A 1 75  ? -18.062 67.762  69.561 1.00 44.85 ? 75   GLU A CD    1 
ATOM   574  O OE1   . GLU A 1 75  ? -18.920 66.931  69.928 1.00 54.70 ? 75   GLU A OE1   1 
ATOM   575  O OE2   . GLU A 1 75  ? -17.673 68.768  70.233 1.00 46.29 ? 75   GLU A OE2   1 
ATOM   576  N N     . PHE A 1 76  ? -18.570 69.572  64.689 1.00 27.25 ? 76   PHE A N     1 
ATOM   577  C CA    . PHE A 1 76  ? -19.828 69.510  63.905 1.00 27.13 ? 76   PHE A CA    1 
ATOM   578  C C     . PHE A 1 76  ? -19.626 69.900  62.447 1.00 29.72 ? 76   PHE A C     1 
ATOM   579  O O     . PHE A 1 76  ? -20.626 69.875  61.730 1.00 26.93 ? 76   PHE A O     1 
ATOM   580  C CB    . PHE A 1 76  ? -20.876 70.374  64.603 1.00 26.24 ? 76   PHE A CB    1 
ATOM   581  C CG    . PHE A 1 76  ? -21.271 69.763  65.927 1.00 29.36 ? 76   PHE A CG    1 
ATOM   582  C CD1   . PHE A 1 76  ? -22.049 68.605  65.962 1.00 33.36 ? 76   PHE A CD1   1 
ATOM   583  C CD2   . PHE A 1 76  ? -20.782 70.271  67.117 1.00 29.58 ? 76   PHE A CD2   1 
ATOM   584  C CE1   . PHE A 1 76  ? -22.402 68.018  67.172 1.00 36.02 ? 76   PHE A CE1   1 
ATOM   585  C CE2   . PHE A 1 76  ? -21.112 69.666  68.328 1.00 34.59 ? 76   PHE A CE2   1 
ATOM   586  C CZ    . PHE A 1 76  ? -21.925 68.547  68.352 1.00 35.21 ? 76   PHE A CZ    1 
ATOM   587  N N     . GLY A 1 77  ? -18.411 70.251  62.017 1.00 28.37 ? 77   GLY A N     1 
ATOM   588  C CA    . GLY A 1 77  ? -18.148 70.598  60.604 1.00 23.80 ? 77   GLY A CA    1 
ATOM   589  C C     . GLY A 1 77  ? -18.844 71.879  60.203 1.00 24.54 ? 77   GLY A C     1 
ATOM   590  O O     . GLY A 1 77  ? -19.196 72.037  59.010 1.00 25.15 ? 77   GLY A O     1 
ATOM   591  N N     . VAL A 1 78  ? -19.072 72.782  61.150 1.00 22.81 ? 78   VAL A N     1 
ATOM   592  C CA    . VAL A 1 78  ? -19.759 74.071  60.893 1.00 23.01 ? 78   VAL A CA    1 
ATOM   593  C C     . VAL A 1 78  ? -18.703 75.133  60.596 1.00 24.18 ? 78   VAL A C     1 
ATOM   594  O O     . VAL A 1 78  ? -17.878 75.428  61.462 1.00 22.76 ? 78   VAL A O     1 
ATOM   595  C CB    . VAL A 1 78  ? -20.649 74.462  62.083 1.00 24.52 ? 78   VAL A CB    1 
ATOM   596  C CG1   . VAL A 1 78  ? -21.168 75.890  61.977 1.00 26.15 ? 78   VAL A CG1   1 
ATOM   597  C CG2   . VAL A 1 78  ? -21.801 73.478  62.253 1.00 26.74 ? 78   VAL A CG2   1 
ATOM   598  N N     . PRO A 1 79  ? -18.702 75.720  59.382 1.00 22.05 ? 79   PRO A N     1 
ATOM   599  C CA    . PRO A 1 79  ? -17.693 76.711  59.021 1.00 23.06 ? 79   PRO A CA    1 
ATOM   600  C C     . PRO A 1 79  ? -17.987 78.088  59.635 1.00 22.78 ? 79   PRO A C     1 
ATOM   601  O O     . PRO A 1 79  ? -19.170 78.505  59.829 1.00 21.63 ? 79   PRO A O     1 
ATOM   602  C CB    . PRO A 1 79  ? -17.728 76.708  57.483 1.00 26.36 ? 79   PRO A CB    1 
ATOM   603  C CG    . PRO A 1 79  ? -19.184 76.340  57.129 1.00 26.92 ? 79   PRO A CG    1 
ATOM   604  C CD    . PRO A 1 79  ? -19.654 75.475  58.282 1.00 25.38 ? 79   PRO A CD    1 
ATOM   605  N N     . LEU A 1 80  ? -16.889 78.788  59.948 1.00 21.98 ? 80   LEU A N     1 
ATOM   606  C CA    . LEU A 1 80  ? -16.863 80.137  60.562 1.00 20.51 ? 80   LEU A CA    1 
ATOM   607  C C     . LEU A 1 80  ? -16.292 81.154  59.584 1.00 20.09 ? 80   LEU A C     1 
ATOM   608  O O     . LEU A 1 80  ? -15.421 80.792  58.808 1.00 20.03 ? 80   LEU A O     1 
ATOM   609  C CB    . LEU A 1 80  ? -15.956 80.085  61.776 1.00 21.67 ? 80   LEU A CB    1 
ATOM   610  C CG    . LEU A 1 80  ? -16.361 79.041  62.816 1.00 23.84 ? 80   LEU A CG    1 
ATOM   611  C CD1   . LEU A 1 80  ? -15.258 78.828  63.846 1.00 22.43 ? 80   LEU A CD1   1 
ATOM   612  C CD2   . LEU A 1 80  ? -17.662 79.481  63.480 1.00 23.30 ? 80   LEU A CD2   1 
ATOM   613  N N     . TRP A 1 81  ? -16.746 82.396  59.699 1.00 19.47 ? 81   TRP A N     1 
ATOM   614  C CA    . TRP A 1 81  ? -16.193 83.556  58.956 1.00 19.12 ? 81   TRP A CA    1 
ATOM   615  C C     . TRP A 1 81  ? -15.691 84.567  59.983 1.00 19.76 ? 81   TRP A C     1 
ATOM   616  O O     . TRP A 1 81  ? -16.452 85.408  60.453 1.00 19.28 ? 81   TRP A O     1 
ATOM   617  C CB    . TRP A 1 81  ? -17.267 84.160  58.031 1.00 19.24 ? 81   TRP A CB    1 
ATOM   618  C CG    . TRP A 1 81  ? -16.687 85.170  57.092 1.00 20.01 ? 81   TRP A CG    1 
ATOM   619  C CD1   . TRP A 1 81  ? -16.664 86.518  57.268 1.00 22.05 ? 81   TRP A CD1   1 
ATOM   620  C CD2   . TRP A 1 81  ? -16.025 84.920  55.845 1.00 20.59 ? 81   TRP A CD2   1 
ATOM   621  N NE1   . TRP A 1 81  ? -15.993 87.126  56.242 1.00 22.12 ? 81   TRP A NE1   1 
ATOM   622  C CE2   . TRP A 1 81  ? -15.569 86.178  55.365 1.00 22.11 ? 81   TRP A CE2   1 
ATOM   623  C CE3   . TRP A 1 81  ? -15.703 83.777  55.123 1.00 20.11 ? 81   TRP A CE3   1 
ATOM   624  C CZ2   . TRP A 1 81  ? -14.884 86.326  54.155 1.00 21.36 ? 81   TRP A CZ2   1 
ATOM   625  C CZ3   . TRP A 1 81  ? -15.053 83.923  53.914 1.00 22.48 ? 81   TRP A CZ3   1 
ATOM   626  C CH2   . TRP A 1 81  ? -14.626 85.171  53.453 1.00 21.26 ? 81   TRP A CH2   1 
ATOM   627  N N     . PRO A 1 82  ? -14.412 84.541  60.376 1.00 19.31 ? 82   PRO A N     1 
ATOM   628  C CA    . PRO A 1 82  ? -13.907 85.486  61.387 1.00 20.98 ? 82   PRO A CA    1 
ATOM   629  C C     . PRO A 1 82  ? -13.798 86.908  60.863 1.00 21.21 ? 82   PRO A C     1 
ATOM   630  O O     . PRO A 1 82  ? -13.321 87.132  59.758 1.00 20.99 ? 82   PRO A O     1 
ATOM   631  C CB    . PRO A 1 82  ? -12.501 84.960  61.704 1.00 22.04 ? 82   PRO A CB    1 
ATOM   632  C CG    . PRO A 1 82  ? -12.560 83.550  61.231 1.00 21.27 ? 82   PRO A CG    1 
ATOM   633  C CD    . PRO A 1 82  ? -13.370 83.602  59.965 1.00 20.31 ? 82   PRO A CD    1 
ATOM   634  N N     . VAL A 1 83  ? -14.327 87.839  61.627 1.00 18.50 ? 83   VAL A N     1 
ATOM   635  C CA    . VAL A 1 83  ? -14.159 89.280  61.356 1.00 20.85 ? 83   VAL A CA    1 
ATOM   636  C C     . VAL A 1 83  ? -13.712 89.969  62.648 1.00 22.09 ? 83   VAL A C     1 
ATOM   637  O O     . VAL A 1 83  ? -14.113 89.514  63.727 1.00 22.96 ? 83   VAL A O     1 
ATOM   638  C CB    . VAL A 1 83  ? -15.453 89.877  60.776 1.00 22.78 ? 83   VAL A CB    1 
ATOM   639  C CG1   . VAL A 1 83  ? -15.995 89.056  59.608 1.00 23.16 ? 83   VAL A CG1   1 
ATOM   640  C CG2   . VAL A 1 83  ? -16.543 90.055  61.822 1.00 22.78 ? 83   VAL A CG2   1 
ATOM   641  N N     . SER A 1 84  ? -12.958 91.065  62.553 1.00 19.74 ? 84   SER A N     1 
ATOM   642  C CA    . SER A 1 84  ? -12.491 91.825  63.741 1.00 20.28 ? 84   SER A CA    1 
ATOM   643  C C     . SER A 1 84  ? -13.610 92.793  64.132 1.00 20.13 ? 84   SER A C     1 
ATOM   644  O O     . SER A 1 84  ? -14.114 92.730  65.273 1.00 22.02 ? 84   SER A O     1 
ATOM   645  C CB    . SER A 1 84  ? -11.186 92.515  63.450 1.00 18.88 ? 84   SER A CB    1 
ATOM   646  O OG    . SER A 1 84  ? -10.161 91.567  63.236 1.00 17.56 ? 84   SER A OG    1 
ATOM   647  N N     . ARG A 1 85  ? -14.035 93.633  63.196 1.00 22.65 ? 85   ARG A N     1 
ATOM   648  C CA    . ARG A 1 85  ? -15.247 94.475  63.353 1.00 24.21 ? 85   ARG A CA    1 
ATOM   649  C C     . ARG A 1 85  ? -16.262 94.229  62.232 1.00 23.21 ? 85   ARG A C     1 
ATOM   650  O O     . ARG A 1 85  ? -17.423 94.626  62.427 1.00 24.94 ? 85   ARG A O     1 
ATOM   651  C CB    . ARG A 1 85  ? -14.866 95.948  63.450 1.00 24.52 ? 85   ARG A CB    1 
ATOM   652  C CG    . ARG A 1 85  ? -14.170 96.227  64.767 1.00 25.35 ? 85   ARG A CG    1 
ATOM   653  C CD    . ARG A 1 85  ? -13.729 97.655  64.932 1.00 26.69 ? 85   ARG A CD    1 
ATOM   654  N NE    . ARG A 1 85  ? -14.761 98.648  64.768 1.00 25.41 ? 85   ARG A NE    1 
ATOM   655  C CZ    . ARG A 1 85  ? -15.633 99.017  65.701 1.00 29.35 ? 85   ARG A CZ    1 
ATOM   656  N NH1   . ARG A 1 85  ? -15.616 98.454  66.898 1.00 27.19 ? 85   ARG A NH1   1 
ATOM   657  N NH2   . ARG A 1 85  ? -16.519 99.960  65.418 1.00 26.64 ? 85   ARG A NH2   1 
ATOM   658  N N     . GLY A 1 86  ? -15.858 93.634  61.103 1.00 21.48 ? 86   GLY A N     1 
ATOM   659  C CA    . GLY A 1 86  ? -16.756 93.311  59.984 1.00 23.40 ? 86   GLY A CA    1 
ATOM   660  C C     . GLY A 1 86  ? -17.237 94.538  59.227 1.00 24.71 ? 86   GLY A C     1 
ATOM   661  O O     . GLY A 1 86  ? -18.401 94.487  58.670 1.00 26.04 ? 86   GLY A O     1 
ATOM   662  N N     . LYS A 1 87  ? -16.426 95.594  59.173 1.00 22.86 ? 87   LYS A N     1 
ATOM   663  C CA    . LYS A 1 87  ? -16.806 96.825  58.436 1.00 24.10 ? 87   LYS A CA    1 
ATOM   664  C C     . LYS A 1 87  ? -16.126 96.837  57.045 1.00 22.44 ? 87   LYS A C     1 
ATOM   665  O O     . LYS A 1 87  ? -15.893 97.928  56.523 1.00 21.64 ? 87   LYS A O     1 
ATOM   666  C CB    . LYS A 1 87  ? -16.486 98.079  59.243 1.00 25.42 ? 87   LYS A CB    1 
ATOM   667  C CG    . LYS A 1 87  ? -16.917 98.053  60.699 1.00 30.46 ? 87   LYS A CG    1 
ATOM   668  C CD    . LYS A 1 87  ? -18.346 97.613  60.913 1.00 32.48 ? 87   LYS A CD    1 
ATOM   669  C CE    . LYS A 1 87  ? -18.751 97.607  62.381 1.00 36.84 ? 87   LYS A CE    1 
ATOM   670  N NZ    . LYS A 1 87  ? -20.005 96.843  62.616 1.00 39.80 ? 87   LYS A NZ    1 
ATOM   671  N N     . ASN A 1 88  ? -15.988 95.678  56.411 1.00 21.12 ? 88   ASN A N     1 
ATOM   672  C CA    . ASN A 1 88  ? -15.263 95.535  55.122 1.00 19.91 ? 88   ASN A CA    1 
ATOM   673  C C     . ASN A 1 88  ? -16.158 95.936  53.953 1.00 20.26 ? 88   ASN A C     1 
ATOM   674  O O     . ASN A 1 88  ? -16.199 95.212  52.916 1.00 22.15 ? 88   ASN A O     1 
ATOM   675  C CB    . ASN A 1 88  ? -14.621 94.147  54.966 1.00 19.48 ? 88   ASN A CB    1 
ATOM   676  C CG    . ASN A 1 88  ? -13.355 94.167  54.134 1.00 20.07 ? 88   ASN A CG    1 
ATOM   677  O OD1   . ASN A 1 88  ? -12.714 95.222  53.953 1.00 19.99 ? 88   ASN A OD1   1 
ATOM   678  N ND2   . ASN A 1 88  ? -12.943 92.980  53.712 1.00 21.21 ? 88   ASN A ND2   1 
ATOM   679  N N     . PHE A 1 89  ? -16.823 97.074  54.090 1.00 21.93 ? 89   PHE A N     1 
ATOM   680  C CA    . PHE A 1 89  ? -17.786 97.601  53.092 1.00 20.88 ? 89   PHE A CA    1 
ATOM   681  C C     . PHE A 1 89  ? -17.033 97.910  51.790 1.00 21.35 ? 89   PHE A C     1 
ATOM   682  O O     . PHE A 1 89  ? -15.902 98.426  51.887 1.00 21.05 ? 89   PHE A O     1 
ATOM   683  C CB    . PHE A 1 89  ? -18.501 98.813  53.675 1.00 24.80 ? 89   PHE A CB    1 
ATOM   684  C CG    . PHE A 1 89  ? -19.207 98.504  54.972 1.00 26.76 ? 89   PHE A CG    1 
ATOM   685  C CD1   . PHE A 1 89  ? -19.850 97.292  55.154 1.00 32.30 ? 89   PHE A CD1   1 
ATOM   686  C CD2   . PHE A 1 89  ? -19.099 99.352  56.043 1.00 34.52 ? 89   PHE A CD2   1 
ATOM   687  C CE1   . PHE A 1 89  ? -20.447 96.964  56.359 1.00 33.21 ? 89   PHE A CE1   1 
ATOM   688  C CE2   . PHE A 1 89  ? -19.681 99.022  57.254 1.00 36.42 ? 89   PHE A CE2   1 
ATOM   689  C CZ    . PHE A 1 89  ? -20.375 97.851  57.394 1.00 34.76 ? 89   PHE A CZ    1 
ATOM   690  N N     . ALA A 1 90  ? -17.653 97.544  50.666 1.00 22.29 ? 90   ALA A N     1 
ATOM   691  C CA    . ALA A 1 90  ? -17.115 97.569  49.274 1.00 22.66 ? 90   ALA A CA    1 
ATOM   692  C C     . ALA A 1 90  ? -16.346 96.264  48.991 1.00 22.26 ? 90   ALA A C     1 
ATOM   693  O O     . ALA A 1 90  ? -16.102 95.987  47.773 1.00 21.06 ? 90   ALA A O     1 
ATOM   694  C CB    . ALA A 1 90  ? -16.268 98.788  49.022 1.00 24.27 ? 90   ALA A CB    1 
ATOM   695  N N     . TYR A 1 91  ? -16.165 95.398  50.008 1.00 20.29 ? 91   TYR A N     1 
ATOM   696  C CA    . TYR A 1 91  ? -15.580 94.053  49.810 1.00 21.67 ? 91   TYR A CA    1 
ATOM   697  C C     . TYR A 1 91  ? -16.461 92.946  50.412 1.00 22.49 ? 91   TYR A C     1 
ATOM   698  O O     . TYR A 1 91  ? -15.966 91.803  50.501 1.00 20.99 ? 91   TYR A O     1 
ATOM   699  C CB    . TYR A 1 91  ? -14.167 94.041  50.375 1.00 21.49 ? 91   TYR A CB    1 
ATOM   700  C CG    . TYR A 1 91  ? -13.172 94.935  49.659 1.00 19.67 ? 91   TYR A CG    1 
ATOM   701  C CD1   . TYR A 1 91  ? -13.014 94.889  48.274 1.00 22.47 ? 91   TYR A CD1   1 
ATOM   702  C CD2   . TYR A 1 91  ? -12.333 95.784  50.375 1.00 21.45 ? 91   TYR A CD2   1 
ATOM   703  C CE1   . TYR A 1 91  ? -12.057 95.668  47.637 1.00 21.36 ? 91   TYR A CE1   1 
ATOM   704  C CE2   . TYR A 1 91  ? -11.414 96.609  49.744 1.00 22.56 ? 91   TYR A CE2   1 
ATOM   705  C CZ    . TYR A 1 91  ? -11.233 96.500  48.375 1.00 22.11 ? 91   TYR A CZ    1 
ATOM   706  O OH    . TYR A 1 91  ? -10.294 97.303  47.790 1.00 24.75 ? 91   TYR A OH    1 
ATOM   707  N N     . GLY A 1 92  ? -17.683 93.254  50.826 1.00 21.91 ? 92   GLY A N     1 
ATOM   708  C CA    . GLY A 1 92  ? -18.626 92.229  51.348 1.00 21.63 ? 92   GLY A CA    1 
ATOM   709  C C     . GLY A 1 92  ? -19.169 92.524  52.747 1.00 21.85 ? 92   GLY A C     1 
ATOM   710  O O     . GLY A 1 92  ? -20.053 91.781  53.190 1.00 21.07 ? 92   GLY A O     1 
ATOM   711  N N     . GLY A 1 93  ? -18.681 93.569  53.413 1.00 19.99 ? 93   GLY A N     1 
ATOM   712  C CA    . GLY A 1 93  ? -19.019 93.795  54.824 1.00 21.89 ? 93   GLY A CA    1 
ATOM   713  C C     . GLY A 1 93  ? -18.542 92.598  55.645 1.00 20.72 ? 93   GLY A C     1 
ATOM   714  O O     . GLY A 1 93  ? -17.441 92.151  55.422 1.00 20.99 ? 93   GLY A O     1 
ATOM   715  N N     . ALA A 1 94  ? -19.396 92.050  56.509 1.00 20.85 ? 94   ALA A N     1 
ATOM   716  C CA    . ALA A 1 94  ? -19.114 90.896  57.376 1.00 21.08 ? 94   ALA A CA    1 
ATOM   717  C C     . ALA A 1 94  ? -19.564 89.608  56.693 1.00 22.39 ? 94   ALA A C     1 
ATOM   718  O O     . ALA A 1 94  ? -19.482 88.516  57.293 1.00 21.54 ? 94   ALA A O     1 
ATOM   719  C CB    . ALA A 1 94  ? -19.810 91.109  58.700 1.00 23.73 ? 94   ALA A CB    1 
ATOM   720  N N     . ALA A 1 95  ? -20.058 89.684  55.464 1.00 21.21 ? 95   ALA A N     1 
ATOM   721  C CA    . ALA A 1 95  ? -20.680 88.487  54.879 1.00 19.98 ? 95   ALA A CA    1 
ATOM   722  C C     . ALA A 1 95  ? -19.627 87.487  54.410 1.00 20.77 ? 95   ALA A C     1 
ATOM   723  O O     . ALA A 1 95  ? -18.534 87.863  53.959 1.00 21.61 ? 95   ALA A O     1 
ATOM   724  C CB    . ALA A 1 95  ? -21.586 88.870  53.734 1.00 21.62 ? 95   ALA A CB    1 
ATOM   725  N N     . PRO A 1 96  ? -19.961 86.182  54.430 1.00 21.75 ? 96   PRO A N     1 
ATOM   726  C CA    . PRO A 1 96  ? -19.036 85.130  54.006 1.00 20.24 ? 96   PRO A CA    1 
ATOM   727  C C     . PRO A 1 96  ? -19.127 84.861  52.504 1.00 22.69 ? 96   PRO A C     1 
ATOM   728  O O     . PRO A 1 96  ? -20.156 85.184  51.879 1.00 23.85 ? 96   PRO A O     1 
ATOM   729  C CB    . PRO A 1 96  ? -19.561 83.905  54.783 1.00 20.62 ? 96   PRO A CB    1 
ATOM   730  C CG    . PRO A 1 96  ? -21.061 84.120  54.808 1.00 21.37 ? 96   PRO A CG    1 
ATOM   731  C CD    . PRO A 1 96  ? -21.221 85.615  54.990 1.00 20.83 ? 96   PRO A CD    1 
ATOM   732  N N     . VAL A 1 97  ? -18.081 84.240  51.954 1.00 22.40 ? 97   VAL A N     1 
ATOM   733  C CA    . VAL A 1 97  ? -18.098 83.768  50.547 1.00 21.97 ? 97   VAL A CA    1 
ATOM   734  C C     . VAL A 1 97  ? -19.193 82.702  50.395 1.00 24.17 ? 97   VAL A C     1 
ATOM   735  O O     . VAL A 1 97  ? -19.986 82.780  49.436 1.00 24.18 ? 97   VAL A O     1 
ATOM   736  C CB    . VAL A 1 97  ? -16.736 83.211  50.120 1.00 21.51 ? 97   VAL A CB    1 
ATOM   737  C CG1   . VAL A 1 97  ? -16.857 82.478  48.782 1.00 23.01 ? 97   VAL A CG1   1 
ATOM   738  C CG2   . VAL A 1 97  ? -15.680 84.321  50.056 1.00 20.79 ? 97   VAL A CG2   1 
ATOM   739  N N     . MET A 1 98  ? -19.229 81.732  51.312 1.00 23.03 ? 98   MET A N     1 
ATOM   740  C CA    . MET A 1 98  ? -20.069 80.522  51.188 1.00 22.51 ? 98   MET A CA    1 
ATOM   741  C C     . MET A 1 98  ? -21.283 80.652  52.106 1.00 23.99 ? 98   MET A C     1 
ATOM   742  O O     . MET A 1 98  ? -21.116 80.720  53.331 1.00 24.25 ? 98   MET A O     1 
ATOM   743  C CB    . MET A 1 98  ? -19.294 79.263  51.552 1.00 24.89 ? 98   MET A CB    1 
ATOM   744  C CG    . MET A 1 98  ? -20.061 77.996  51.177 1.00 26.37 ? 98   MET A CG    1 
ATOM   745  S SD    . MET A 1 98  ? -19.292 76.563  51.858 1.00 27.32 ? 98   MET A SD    1 
ATOM   746  C CE    . MET A 1 98  ? -19.752 76.740  53.579 1.00 26.97 ? 98   MET A CE    1 
ATOM   747  N N     . SER A 1 99  ? -22.470 80.665  51.513 1.00 23.25 ? 99   SER A N     1 
ATOM   748  C CA    . SER A 1 99  ? -23.759 80.720  52.244 1.00 26.21 ? 99   SER A CA    1 
ATOM   749  C C     . SER A 1 99  ? -23.794 79.604  53.277 1.00 23.21 ? 99   SER A C     1 
ATOM   750  O O     . SER A 1 99  ? -23.364 78.528  52.966 1.00 24.14 ? 99   SER A O     1 
ATOM   751  C CB    . SER A 1 99  ? -24.887 80.622  51.292 1.00 26.69 ? 99   SER A CB    1 
ATOM   752  O OG    . SER A 1 99  ? -25.050 81.861  50.680 1.00 27.61 ? 99   SER A OG    1 
ATOM   753  N N     . GLY A 1 100 ? -24.267 79.905  54.479 1.00 24.14 ? 100  GLY A N     1 
ATOM   754  C CA    . GLY A 1 100 ? -24.401 78.923  55.560 1.00 24.75 ? 100  GLY A CA    1 
ATOM   755  C C     . GLY A 1 100 ? -23.242 79.007  56.535 1.00 25.53 ? 100  GLY A C     1 
ATOM   756  O O     . GLY A 1 100 ? -23.352 78.427  57.598 1.00 26.86 ? 100  GLY A O     1 
ATOM   757  N N     . THR A 1 101 ? -22.170 79.712  56.193 1.00 21.90 ? 101  THR A N     1 
ATOM   758  C CA    . THR A 1 101 ? -21.057 79.992  57.126 1.00 21.06 ? 101  THR A CA    1 
ATOM   759  C C     . THR A 1 101 ? -21.626 80.826  58.287 1.00 21.49 ? 101  THR A C     1 
ATOM   760  O O     . THR A 1 101 ? -22.438 81.743  58.056 1.00 22.35 ? 101  THR A O     1 
ATOM   761  C CB    . THR A 1 101 ? -19.921 80.711  56.386 1.00 20.26 ? 101  THR A CB    1 
ATOM   762  O OG1   . THR A 1 101 ? -19.494 79.983  55.226 1.00 20.61 ? 101  THR A OG1   1 
ATOM   763  C CG2   . THR A 1 101 ? -18.717 80.869  57.277 1.00 21.14 ? 101  THR A CG2   1 
ATOM   764  N N     . VAL A 1 102 ? -21.179 80.558  59.493 1.00 20.57 ? 102  VAL A N     1 
ATOM   765  C CA    . VAL A 1 102 ? -21.476 81.367  60.696 1.00 21.75 ? 102  VAL A CA    1 
ATOM   766  C C     . VAL A 1 102 ? -20.394 82.431  60.890 1.00 22.35 ? 102  VAL A C     1 
ATOM   767  O O     . VAL A 1 102 ? -19.236 82.075  60.991 1.00 21.99 ? 102  VAL A O     1 
ATOM   768  C CB    . VAL A 1 102 ? -21.544 80.449  61.906 1.00 22.62 ? 102  VAL A CB    1 
ATOM   769  C CG1   . VAL A 1 102 ? -21.736 81.235  63.176 1.00 23.93 ? 102  VAL A CG1   1 
ATOM   770  C CG2   . VAL A 1 102 ? -22.621 79.394  61.710 1.00 23.45 ? 102  VAL A CG2   1 
ATOM   771  N N     . VAL A 1 103 ? -20.769 83.683  60.993 1.00 19.96 ? 103  VAL A N     1 
ATOM   772  C CA    . VAL A 1 103 ? -19.803 84.780  61.246 1.00 21.16 ? 103  VAL A CA    1 
ATOM   773  C C     . VAL A 1 103 ? -19.305 84.697  62.690 1.00 22.16 ? 103  VAL A C     1 
ATOM   774  O O     . VAL A 1 103 ? -20.113 84.535  63.629 1.00 22.22 ? 103  VAL A O     1 
ATOM   775  C CB    . VAL A 1 103 ? -20.423 86.149  60.966 1.00 20.24 ? 103  VAL A CB    1 
ATOM   776  C CG1   . VAL A 1 103 ? -19.480 87.282  61.338 1.00 21.93 ? 103  VAL A CG1   1 
ATOM   777  C CG2   . VAL A 1 103 ? -20.854 86.256  59.535 1.00 21.19 ? 103  VAL A CG2   1 
ATOM   778  N N     . LEU A 1 104 ? -17.993 84.744  62.849 1.00 20.90 ? 104  LEU A N     1 
ATOM   779  C CA    . LEU A 1 104 ? -17.317 84.810  64.158 1.00 19.40 ? 104  LEU A CA    1 
ATOM   780  C C     . LEU A 1 104 ? -16.880 86.251  64.355 1.00 20.20 ? 104  LEU A C     1 
ATOM   781  O O     . LEU A 1 104 ? -15.850 86.703  63.764 1.00 18.84 ? 104  LEU A O     1 
ATOM   782  C CB    . LEU A 1 104 ? -16.182 83.785  64.191 1.00 22.37 ? 104  LEU A CB    1 
ATOM   783  C CG    . LEU A 1 104 ? -15.247 83.904  65.392 1.00 27.20 ? 104  LEU A CG    1 
ATOM   784  C CD1   . LEU A 1 104 ? -15.961 83.609  66.657 1.00 31.80 ? 104  LEU A CD1   1 
ATOM   785  C CD2   . LEU A 1 104 ? -14.061 82.974  65.230 1.00 29.71 ? 104  LEU A CD2   1 
ATOM   786  N N     . ASP A 1 105 ? -17.698 86.977  65.100 1.00 19.10 ? 105  ASP A N     1 
ATOM   787  C CA    . ASP A 1 105 ? -17.654 88.437  65.200 1.00 20.87 ? 105  ASP A CA    1 
ATOM   788  C C     . ASP A 1 105 ? -16.898 88.782  66.476 1.00 22.41 ? 105  ASP A C     1 
ATOM   789  O O     . ASP A 1 105 ? -17.384 88.416  67.569 1.00 21.50 ? 105  ASP A O     1 
ATOM   790  C CB    . ASP A 1 105 ? -19.070 89.013  65.233 1.00 22.83 ? 105  ASP A CB    1 
ATOM   791  C CG    . ASP A 1 105 ? -19.133 90.503  65.508 1.00 24.69 ? 105  ASP A CG    1 
ATOM   792  O OD1   . ASP A 1 105 ? -18.057 91.138  65.658 1.00 26.17 ? 105  ASP A OD1   1 
ATOM   793  O OD2   . ASP A 1 105 ? -20.248 91.027  65.530 1.00 26.85 ? 105  ASP A OD2   1 
ATOM   794  N N     . MET A 1 106 ? -15.760 89.461  66.361 1.00 19.57 ? 106  MET A N     1 
ATOM   795  C CA    . MET A 1 106 ? -14.871 89.691  67.532 1.00 19.91 ? 106  MET A CA    1 
ATOM   796  C C     . MET A 1 106 ? -14.974 91.128  68.028 1.00 19.12 ? 106  MET A C     1 
ATOM   797  O O     . MET A 1 106 ? -14.108 91.576  68.784 1.00 21.02 ? 106  MET A O     1 
ATOM   798  C CB    . MET A 1 106 ? -13.438 89.274  67.185 1.00 22.11 ? 106  MET A CB    1 
ATOM   799  C CG    . MET A 1 106 ? -13.311 87.773  67.266 1.00 24.46 ? 106  MET A CG    1 
ATOM   800  S SD    . MET A 1 106 ? -11.697 87.113  66.919 1.00 25.82 ? 106  MET A SD    1 
ATOM   801  C CE    . MET A 1 106 ? -11.687 87.516  65.175 1.00 26.91 ? 106  MET A CE    1 
ATOM   802  N N     . ASN A 1 107 ? -16.048 91.819  67.676 1.00 19.97 ? 107  ASN A N     1 
ATOM   803  C CA    . ASN A 1 107 ? -16.308 93.214  68.075 1.00 21.96 ? 107  ASN A CA    1 
ATOM   804  C C     . ASN A 1 107 ? -16.167 93.387  69.591 1.00 20.56 ? 107  ASN A C     1 
ATOM   805  O O     . ASN A 1 107 ? -15.629 94.427  70.023 1.00 22.00 ? 107  ASN A O     1 
ATOM   806  C CB    . ASN A 1 107 ? -17.700 93.636  67.600 1.00 25.04 ? 107  ASN A CB    1 
ATOM   807  C CG    . ASN A 1 107 ? -17.638 94.384  66.294 1.00 29.09 ? 107  ASN A CG    1 
ATOM   808  O OD1   . ASN A 1 107 ? -17.904 93.839  65.183 1.00 32.20 ? 107  ASN A OD1   1 
ATOM   809  N ND2   . ASN A 1 107 ? -17.228 95.631  66.413 1.00 25.65 ? 107  ASN A ND2   1 
ATOM   810  N N     . ARG A 1 108 ? -16.662 92.440  70.372 1.00 19.82 ? 108  ARG A N     1 
ATOM   811  C CA    . ARG A 1 108 ? -16.701 92.597  71.842 1.00 22.38 ? 108  ARG A CA    1 
ATOM   812  C C     . ARG A 1 108 ? -15.292 92.410  72.409 1.00 24.70 ? 108  ARG A C     1 
ATOM   813  O O     . ARG A 1 108 ? -15.089 92.751  73.562 1.00 21.68 ? 108  ARG A O     1 
ATOM   814  C CB    . ARG A 1 108 ? -17.699 91.629  72.483 1.00 21.84 ? 108  ARG A CB    1 
ATOM   815  C CG    . ARG A 1 108 ? -19.122 91.784  71.968 1.00 26.04 ? 108  ARG A CG    1 
ATOM   816  C CD    . ARG A 1 108 ? -20.054 90.672  72.397 1.00 25.53 ? 108  ARG A CD    1 
ATOM   817  N NE    . ARG A 1 108 ? -20.173 90.747  73.847 1.00 24.62 ? 108  ARG A NE    1 
ATOM   818  C CZ    . ARG A 1 108 ? -19.973 89.734  74.703 1.00 25.83 ? 108  ARG A CZ    1 
ATOM   819  N NH1   . ARG A 1 108 ? -19.764 88.487  74.306 1.00 27.83 ? 108  ARG A NH1   1 
ATOM   820  N NH2   . ARG A 1 108 ? -20.022 89.982  76.001 1.00 25.84 ? 108  ARG A NH2   1 
ATOM   821  N N     . MET A 1 109 ? -14.330 91.860  71.663 1.00 21.19 ? 109  MET A N     1 
ATOM   822  C CA    . MET A 1 109 ? -12.940 91.757  72.145 1.00 20.87 ? 109  MET A CA    1 
ATOM   823  C C     . MET A 1 109 ? -12.234 93.063  71.794 1.00 23.20 ? 109  MET A C     1 
ATOM   824  O O     . MET A 1 109 ? -11.583 93.135  70.739 1.00 20.13 ? 109  MET A O     1 
ATOM   825  C CB    . MET A 1 109 ? -12.240 90.545  71.567 1.00 22.27 ? 109  MET A CB    1 
ATOM   826  C CG    . MET A 1 109 ? -12.868 89.250  72.014 1.00 23.06 ? 109  MET A CG    1 
ATOM   827  S SD    . MET A 1 109 ? -12.341 87.797  71.092 1.00 23.77 ? 109  MET A SD    1 
ATOM   828  C CE    . MET A 1 109 ? -10.605 87.738  71.491 1.00 26.03 ? 109  MET A CE    1 
ATOM   829  N N     . ASN A 1 110 ? -12.501 94.111  72.575 1.00 20.40 ? 110  ASN A N     1 
ATOM   830  C CA    . ASN A 1 110 ? -12.078 95.478  72.226 1.00 21.21 ? 110  ASN A CA    1 
ATOM   831  C C     . ASN A 1 110 ? -11.152 96.069  73.292 1.00 20.69 ? 110  ASN A C     1 
ATOM   832  O O     . ASN A 1 110 ? -11.149 97.256  73.439 1.00 22.34 ? 110  ASN A O     1 
ATOM   833  C CB    . ASN A 1 110 ? -13.320 96.311  71.983 1.00 25.21 ? 110  ASN A CB    1 
ATOM   834  C CG    . ASN A 1 110 ? -14.125 96.468  73.257 1.00 28.36 ? 110  ASN A CG    1 
ATOM   835  O OD1   . ASN A 1 110 ? -13.847 95.892  74.278 1.00 22.68 ? 110  ASN A OD1   1 
ATOM   836  N ND2   . ASN A 1 110 ? -15.102 97.310  73.196 1.00 33.36 ? 110  ASN A ND2   1 
ATOM   837  N N     . ARG A 1 111 ? -10.354 95.271  73.969 1.00 19.94 ? 111  ARG A N     1 
ATOM   838  C CA    . ARG A 1 111 ? -9.324  95.767  74.898 1.00 21.47 ? 111  ARG A CA    1 
ATOM   839  C C     . ARG A 1 111 ? -8.143  96.398  74.123 1.00 20.71 ? 111  ARG A C     1 
ATOM   840  O O     . ARG A 1 111 ? -7.593  95.752  73.184 1.00 19.32 ? 111  ARG A O     1 
ATOM   841  C CB    . ARG A 1 111 ? -8.883  94.577  75.752 1.00 25.59 ? 111  ARG A CB    1 
ATOM   842  C CG    . ARG A 1 111 ? -7.854  94.868  76.835 1.00 36.24 ? 111  ARG A CG    1 
ATOM   843  C CD    . ARG A 1 111 ? -7.378  93.637  77.644 1.00 39.83 ? 111  ARG A CD    1 
ATOM   844  N NE    . ARG A 1 111 ? -6.164  93.908  78.450 1.00 39.61 ? 111  ARG A NE    1 
ATOM   845  C CZ    . ARG A 1 111 ? -5.242  93.012  78.876 1.00 39.76 ? 111  ARG A CZ    1 
ATOM   846  N NH1   . ARG A 1 111 ? -5.363  91.712  78.662 1.00 39.03 ? 111  ARG A NH1   1 
ATOM   847  N NH2   . ARG A 1 111 ? -4.169  93.445  79.523 1.00 38.72 ? 111  ARG A NH2   1 
ATOM   848  N N     . ILE A 1 112 ? -7.755  97.590  74.536 1.00 20.52 ? 112  ILE A N     1 
ATOM   849  C CA    . ILE A 1 112 ? -6.430  98.175  74.218 1.00 20.41 ? 112  ILE A CA    1 
ATOM   850  C C     . ILE A 1 112 ? -5.511  97.662  75.308 1.00 21.96 ? 112  ILE A C     1 
ATOM   851  O O     . ILE A 1 112 ? -5.681  98.130  76.472 1.00 20.54 ? 112  ILE A O     1 
ATOM   852  C CB    . ILE A 1 112 ? -6.553  99.694  74.124 1.00 21.00 ? 112  ILE A CB    1 
ATOM   853  C CG1   . ILE A 1 112 ? -7.510  100.050 72.986 1.00 20.16 ? 112  ILE A CG1   1 
ATOM   854  C CG2   . ILE A 1 112 ? -5.186  100.361 73.984 1.00 22.46 ? 112  ILE A CG2   1 
ATOM   855  C CD1   . ILE A 1 112 ? -7.882  101.517 72.937 1.00 20.27 ? 112  ILE A CD1   1 
ATOM   856  N N     . LEU A 1 113 ? -4.698  96.642  75.021 1.00 18.69 ? 113  LEU A N     1 
ATOM   857  C CA    . LEU A 1 113 ? -3.817  96.030  76.056 1.00 20.97 ? 113  LEU A CA    1 
ATOM   858  C C     . LEU A 1 113 ? -2.747  97.019  76.518 1.00 20.81 ? 113  LEU A C     1 
ATOM   859  O O     . LEU A 1 113 ? -2.411  97.052  77.746 1.00 18.37 ? 113  LEU A O     1 
ATOM   860  C CB    . LEU A 1 113 ? -3.186  94.731  75.539 1.00 24.23 ? 113  LEU A CB    1 
ATOM   861  C CG    . LEU A 1 113 ? -4.094  93.507  75.552 1.00 28.65 ? 113  LEU A CG    1 
ATOM   862  C CD1   . LEU A 1 113 ? -4.860  93.384  74.269 1.00 26.20 ? 113  LEU A CD1   1 
ATOM   863  C CD2   . LEU A 1 113 ? -3.287  92.226  75.795 1.00 31.78 ? 113  LEU A CD2   1 
ATOM   864  N N     . GLU A 1 114 ? -2.174  97.777  75.577 1.00 17.72 ? 114  GLU A N     1 
ATOM   865  C CA    . GLU A 1 114 ? -1.099  98.724  75.875 1.00 19.66 ? 114  GLU A CA    1 
ATOM   866  C C     . GLU A 1 114 ? -0.967  99.688  74.726 1.00 19.18 ? 114  GLU A C     1 
ATOM   867  O O     . GLU A 1 114 ? -1.127  99.282  73.557 1.00 18.62 ? 114  GLU A O     1 
ATOM   868  C CB    . GLU A 1 114 ? 0.236   98.007  76.093 1.00 24.16 ? 114  GLU A CB    1 
ATOM   869  C CG    . GLU A 1 114 ? 1.339   98.966  76.493 1.00 27.59 ? 114  GLU A CG    1 
ATOM   870  C CD    . GLU A 1 114 ? 2.717   98.340  76.672 1.00 28.98 ? 114  GLU A CD    1 
ATOM   871  O OE1   . GLU A 1 114 ? 2.937   97.182  76.203 1.00 25.87 ? 114  GLU A OE1   1 
ATOM   872  O OE2   . GLU A 1 114 ? 3.582   99.050  77.259 1.00 29.87 ? 114  GLU A OE2   1 
ATOM   873  N N     . VAL A 1 115 ? -0.686  100.936 75.062 1.00 19.75 ? 115  VAL A N     1 
ATOM   874  C CA    . VAL A 1 115 ? -0.164  101.927 74.095 1.00 19.45 ? 115  VAL A CA    1 
ATOM   875  C C     . VAL A 1 115 ? 1.097   102.493 74.681 1.00 22.07 ? 115  VAL A C     1 
ATOM   876  O O     . VAL A 1 115 ? 1.026   102.985 75.822 1.00 22.33 ? 115  VAL A O     1 
ATOM   877  C CB    . VAL A 1 115 ? -1.142  103.056 73.789 1.00 20.33 ? 115  VAL A CB    1 
ATOM   878  C CG1   . VAL A 1 115 ? -0.526  104.028 72.783 1.00 20.49 ? 115  VAL A CG1   1 
ATOM   879  C CG2   . VAL A 1 115 ? -2.452  102.539 73.265 1.00 19.52 ? 115  VAL A CG2   1 
ATOM   880  N N     . ASN A 1 116 ? 2.211   102.308 73.980 1.00 18.82 ? 116  ASN A N     1 
ATOM   881  C CA    . ASN A 1 116 ? 3.550   102.603 74.528 1.00 19.90 ? 116  ASN A CA    1 
ATOM   882  C C     . ASN A 1 116 ? 4.090   103.841 73.794 1.00 20.58 ? 116  ASN A C     1 
ATOM   883  O O     . ASN A 1 116 ? 4.418   103.742 72.613 1.00 19.65 ? 116  ASN A O     1 
ATOM   884  C CB    . ASN A 1 116 ? 4.442   101.369 74.446 1.00 19.82 ? 116  ASN A CB    1 
ATOM   885  C CG    . ASN A 1 116 ? 5.751   101.563 75.162 1.00 19.77 ? 116  ASN A CG    1 
ATOM   886  O OD1   . ASN A 1 116 ? 6.469   102.543 74.927 1.00 23.27 ? 116  ASN A OD1   1 
ATOM   887  N ND2   . ASN A 1 116 ? 6.059   100.666 76.063 1.00 20.49 ? 116  ASN A ND2   1 
ATOM   888  N N     . GLU A 1 117 ? 4.134   104.976 74.476 1.00 18.72 ? 117  GLU A N     1 
ATOM   889  C CA    . GLU A 1 117 ? 4.594   106.250 73.870 1.00 22.63 ? 117  GLU A CA    1 
ATOM   890  C C     . GLU A 1 117 ? 6.091   106.156 73.530 1.00 21.16 ? 117  GLU A C     1 
ATOM   891  O O     . GLU A 1 117 ? 6.476   106.535 72.397 1.00 22.94 ? 117  GLU A O     1 
ATOM   892  C CB    . GLU A 1 117 ? 4.274   107.417 74.802 1.00 25.15 ? 117  GLU A CB    1 
ATOM   893  C CG    . GLU A 1 117 ? 4.662   108.744 74.200 1.00 25.64 ? 117  GLU A CG    1 
ATOM   894  C CD    . GLU A 1 117 ? 4.492   109.902 75.174 1.00 28.26 ? 117  GLU A CD    1 
ATOM   895  O OE1   . GLU A 1 117 ? 5.220   109.942 76.119 1.00 35.49 ? 117  GLU A OE1   1 
ATOM   896  O OE2   . GLU A 1 117 ? 3.603   110.675 75.011 1.00 24.57 ? 117  GLU A OE2   1 
ATOM   897  N N     . GLU A 1 118 ? 6.925   105.661 74.427 1.00 20.16 ? 118  GLU A N     1 
ATOM   898  C CA    . GLU A 1 118 ? 8.376   105.816 74.214 1.00 26.17 ? 118  GLU A CA    1 
ATOM   899  C C     . GLU A 1 118 ? 8.827   104.825 73.132 1.00 22.35 ? 118  GLU A C     1 
ATOM   900  O O     . GLU A 1 118 ? 9.771   105.177 72.412 1.00 20.54 ? 118  GLU A O     1 
ATOM   901  C CB    . GLU A 1 118 ? 9.148   105.734 75.514 1.00 31.08 ? 118  GLU A CB    1 
ATOM   902  C CG    . GLU A 1 118 ? 9.144   104.376 76.097 1.00 36.69 ? 118  GLU A CG    1 
ATOM   903  C CD    . GLU A 1 118 ? 9.812   104.384 77.461 1.00 45.42 ? 118  GLU A CD    1 
ATOM   904  O OE1   . GLU A 1 118 ? 10.044  105.511 77.970 1.00 52.69 ? 118  GLU A OE1   1 
ATOM   905  O OE2   . GLU A 1 118 ? 10.113  103.274 77.988 1.00 47.91 ? 118  GLU A OE2   1 
ATOM   906  N N     . PHE A 1 119 ? 8.163   103.682 72.958 1.00 20.12 ? 119  PHE A N     1 
ATOM   907  C CA    . PHE A 1 119 ? 8.495   102.775 71.826 1.00 20.15 ? 119  PHE A CA    1 
ATOM   908  C C     . PHE A 1 119 ? 7.567   102.923 70.625 1.00 21.35 ? 119  PHE A C     1 
ATOM   909  O O     . PHE A 1 119 ? 7.861   102.288 69.593 1.00 23.52 ? 119  PHE A O     1 
ATOM   910  C CB    . PHE A 1 119 ? 8.544   101.331 72.281 1.00 21.64 ? 119  PHE A CB    1 
ATOM   911  C CG    . PHE A 1 119 ? 9.814   101.009 72.992 1.00 24.60 ? 119  PHE A CG    1 
ATOM   912  C CD1   . PHE A 1 119 ? 10.989  100.830 72.254 1.00 27.20 ? 119  PHE A CD1   1 
ATOM   913  C CD2   . PHE A 1 119 ? 9.825   100.806 74.355 1.00 24.76 ? 119  PHE A CD2   1 
ATOM   914  C CE1   . PHE A 1 119 ? 12.170  100.464 72.884 1.00 25.77 ? 119  PHE A CE1   1 
ATOM   915  C CE2   . PHE A 1 119 ? 11.013  100.474 74.991 1.00 24.96 ? 119  PHE A CE2   1 
ATOM   916  C CZ    . PHE A 1 119 ? 12.171  100.335 74.262 1.00 26.54 ? 119  PHE A CZ    1 
ATOM   917  N N     . GLY A 1 120 ? 6.528   103.741 70.704 1.00 19.32 ? 120  GLY A N     1 
ATOM   918  C CA    . GLY A 1 120 ? 5.601   103.966 69.595 1.00 16.94 ? 120  GLY A CA    1 
ATOM   919  C C     . GLY A 1 120 ? 4.957   102.690 69.131 1.00 19.25 ? 120  GLY A C     1 
ATOM   920  O O     . GLY A 1 120 ? 5.231   102.219 68.007 1.00 18.29 ? 120  GLY A O     1 
ATOM   921  N N     . TYR A 1 121 ? 4.101   102.104 69.951 1.00 16.76 ? 121  TYR A N     1 
ATOM   922  C CA    . TYR A 1 121 ? 3.328   100.923 69.520 1.00 16.77 ? 121  TYR A CA    1 
ATOM   923  C C     . TYR A 1 121 ? 2.023   100.832 70.299 1.00 17.10 ? 121  TYR A C     1 
ATOM   924  O O     . TYR A 1 121 ? 1.876   101.414 71.406 1.00 18.24 ? 121  TYR A O     1 
ATOM   925  C CB    . TYR A 1 121 ? 4.155   99.638  69.635 1.00 18.37 ? 121  TYR A CB    1 
ATOM   926  C CG    . TYR A 1 121 ? 4.370   99.073  71.013 1.00 17.86 ? 121  TYR A CG    1 
ATOM   927  C CD1   . TYR A 1 121 ? 3.353   98.487  71.760 1.00 18.16 ? 121  TYR A CD1   1 
ATOM   928  C CD2   . TYR A 1 121 ? 5.622   99.178  71.584 1.00 18.52 ? 121  TYR A CD2   1 
ATOM   929  C CE1   . TYR A 1 121 ? 3.628   97.931  72.999 1.00 19.17 ? 121  TYR A CE1   1 
ATOM   930  C CE2   . TYR A 1 121 ? 5.901   98.646  72.827 1.00 18.10 ? 121  TYR A CE2   1 
ATOM   931  C CZ    . TYR A 1 121 ? 4.901   98.010  73.525 1.00 18.91 ? 121  TYR A CZ    1 
ATOM   932  O OH    . TYR A 1 121 ? 5.231   97.559  74.767 1.00 20.47 ? 121  TYR A OH    1 
ATOM   933  N N     . ALA A 1 122 ? 1.113   100.032 69.769 1.00 18.57 ? 122  ALA A N     1 
ATOM   934  C CA    . ALA A 1 122 ? -0.085  99.597  70.517 1.00 18.32 ? 122  ALA A CA    1 
ATOM   935  C C     . ALA A 1 122 ? -0.206  98.093  70.388 1.00 20.40 ? 122  ALA A C     1 
ATOM   936  O O     . ALA A 1 122 ? 0.195   97.549  69.374 1.00 19.84 ? 122  ALA A O     1 
ATOM   937  C CB    . ALA A 1 122 ? -1.311  100.301 69.997 1.00 17.88 ? 122  ALA A CB    1 
ATOM   938  N N     . LEU A 1 123 ? -0.784  97.464  71.408 1.00 18.26 ? 123  LEU A N     1 
ATOM   939  C CA    . LEU A 1 123 ? -1.198  96.053  71.377 1.00 16.79 ? 123  LEU A CA    1 
ATOM   940  C C     . LEU A 1 123 ? -2.697  96.033  71.595 1.00 18.33 ? 123  LEU A C     1 
ATOM   941  O O     . LEU A 1 123 ? -3.155  96.518  72.648 1.00 17.24 ? 123  LEU A O     1 
ATOM   942  C CB    . LEU A 1 123 ? -0.419  95.258  72.430 1.00 17.02 ? 123  LEU A CB    1 
ATOM   943  C CG    . LEU A 1 123 ? -0.811  93.786  72.607 1.00 17.34 ? 123  LEU A CG    1 
ATOM   944  C CD1   . LEU A 1 123 ? -0.540  92.989  71.319 1.00 17.54 ? 123  LEU A CD1   1 
ATOM   945  C CD2   . LEU A 1 123 ? -0.059  93.168  73.777 1.00 19.00 ? 123  LEU A CD2   1 
ATOM   946  N N     . VAL A 1 124 ? -3.433  95.499  70.634 1.00 17.70 ? 124  VAL A N     1 
ATOM   947  C CA    . VAL A 1 124 ? -4.900  95.656  70.596 1.00 18.14 ? 124  VAL A CA    1 
ATOM   948  C C     . VAL A 1 124 ? -5.564  94.312  70.304 1.00 18.65 ? 124  VAL A C     1 
ATOM   949  O O     . VAL A 1 124 ? -4.982  93.463  69.597 1.00 16.85 ? 124  VAL A O     1 
ATOM   950  C CB    . VAL A 1 124 ? -5.292  96.741  69.586 1.00 19.28 ? 124  VAL A CB    1 
ATOM   951  C CG1   . VAL A 1 124 ? -4.838  98.120  70.068 1.00 18.48 ? 124  VAL A CG1   1 
ATOM   952  C CG2   . VAL A 1 124 ? -4.776  96.451  68.170 1.00 18.75 ? 124  VAL A CG2   1 
ATOM   953  N N     . GLU A 1 125 ? -6.825  94.204  70.689 1.00 17.66 ? 125  GLU A N     1 
ATOM   954  C CA    . GLU A 1 125 ? -7.722  93.120  70.281 1.00 16.35 ? 125  GLU A CA    1 
ATOM   955  C C     . GLU A 1 125 ? -8.462  93.558  69.028 1.00 17.80 ? 125  GLU A C     1 
ATOM   956  O O     . GLU A 1 125 ? -8.478  94.724  68.641 1.00 18.02 ? 125  GLU A O     1 
ATOM   957  C CB    . GLU A 1 125 ? -8.703  92.765  71.391 1.00 18.91 ? 125  GLU A CB    1 
ATOM   958  C CG    . GLU A 1 125 ? -8.040  92.089  72.586 1.00 19.72 ? 125  GLU A CG    1 
ATOM   959  C CD    . GLU A 1 125 ? -9.030  91.639  73.670 1.00 25.03 ? 125  GLU A CD    1 
ATOM   960  O OE1   . GLU A 1 125 ? -10.096 92.295  73.833 1.00 21.42 ? 125  GLU A OE1   1 
ATOM   961  O OE2   . GLU A 1 125 ? -8.726  90.614  74.322 1.00 25.73 ? 125  GLU A OE2   1 
ATOM   962  N N     . PRO A 1 126 ? -9.106  92.603  68.341 1.00 19.22 ? 126  PRO A N     1 
ATOM   963  C CA    . PRO A 1 126 ? -9.673  92.879  67.011 1.00 17.81 ? 126  PRO A CA    1 
ATOM   964  C C     . PRO A 1 126 ? -10.818 93.896  66.993 1.00 20.69 ? 126  PRO A C     1 
ATOM   965  O O     . PRO A 1 126 ? -11.012 94.611  65.991 1.00 19.29 ? 126  PRO A O     1 
ATOM   966  C CB    . PRO A 1 126 ? -10.144 91.487  66.552 1.00 17.30 ? 126  PRO A CB    1 
ATOM   967  C CG    . PRO A 1 126 ? -9.316  90.547  67.354 1.00 17.71 ? 126  PRO A CG    1 
ATOM   968  C CD    . PRO A 1 126 ? -9.115  91.179  68.702 1.00 17.13 ? 126  PRO A CD    1 
ATOM   969  N N     . GLY A 1 127 ? -11.560 93.991  68.109 1.00 20.20 ? 127  GLY A N     1 
ATOM   970  C CA    . GLY A 1 127 ? -12.696 94.911  68.201 1.00 19.37 ? 127  GLY A CA    1 
ATOM   971  C C     . GLY A 1 127 ? -12.331 96.370  68.370 1.00 20.22 ? 127  GLY A C     1 
ATOM   972  O O     . GLY A 1 127 ? -13.241 97.221  68.219 1.00 19.42 ? 127  GLY A O     1 
ATOM   973  N N     . VAL A 1 128 ? -11.063 96.693  68.596 1.00 20.24 ? 128  VAL A N     1 
ATOM   974  C CA    . VAL A 1 128 ? -10.627 98.094  68.735 1.00 19.28 ? 128  VAL A CA    1 
ATOM   975  C C     . VAL A 1 128 ? -10.757 98.800  67.392 1.00 19.88 ? 128  VAL A C     1 
ATOM   976  O O     . VAL A 1 128 ? -10.138 98.395  66.392 1.00 18.54 ? 128  VAL A O     1 
ATOM   977  C CB    . VAL A 1 128 ? -9.214  98.177  69.294 1.00 19.93 ? 128  VAL A CB    1 
ATOM   978  C CG1   . VAL A 1 128 ? -8.781  99.628  69.402 1.00 21.39 ? 128  VAL A CG1   1 
ATOM   979  C CG2   . VAL A 1 128 ? -9.130  97.480  70.635 1.00 22.41 ? 128  VAL A CG2   1 
ATOM   980  N N     . SER A 1 129 ? -11.551 99.850  67.369 1.00 19.46 ? 129  SER A N     1 
ATOM   981  C CA    . SER A 1 129 ? -11.695 100.727 66.193 1.00 18.44 ? 129  SER A CA    1 
ATOM   982  C C     . SER A 1 129 ? -10.577 101.762 66.147 1.00 17.60 ? 129  SER A C     1 
ATOM   983  O O     . SER A 1 129 ? -9.944  102.060 67.169 1.00 17.80 ? 129  SER A O     1 
ATOM   984  C CB    . SER A 1 129 ? -13.044 101.406 66.196 1.00 21.29 ? 129  SER A CB    1 
ATOM   985  O OG    . SER A 1 129 ? -13.105 102.385 67.206 1.00 19.22 ? 129  SER A OG    1 
ATOM   986  N N     . TYR A 1 130 ? -10.412 102.388 65.005 1.00 16.96 ? 130  TYR A N     1 
ATOM   987  C CA    . TYR A 1 130 ? -9.485  103.534 64.912 1.00 18.52 ? 130  TYR A CA    1 
ATOM   988  C C     . TYR A 1 130 ? -9.983  104.685 65.804 1.00 18.30 ? 130  TYR A C     1 
ATOM   989  O O     . TYR A 1 130 ? -9.142  105.325 66.456 1.00 17.39 ? 130  TYR A O     1 
ATOM   990  C CB    . TYR A 1 130 ? -9.317  103.983 63.470 1.00 18.45 ? 130  TYR A CB    1 
ATOM   991  C CG    . TYR A 1 130 ? -8.687  102.962 62.564 1.00 19.15 ? 130  TYR A CG    1 
ATOM   992  C CD1   . TYR A 1 130 ? -7.318  102.793 62.531 1.00 20.18 ? 130  TYR A CD1   1 
ATOM   993  C CD2   . TYR A 1 130 ? -9.464  102.130 61.760 1.00 20.23 ? 130  TYR A CD2   1 
ATOM   994  C CE1   . TYR A 1 130 ? -6.716  101.871 61.670 1.00 18.81 ? 130  TYR A CE1   1 
ATOM   995  C CE2   . TYR A 1 130 ? -8.885  101.186 60.917 1.00 18.68 ? 130  TYR A CE2   1 
ATOM   996  C CZ    . TYR A 1 130 ? -7.503  101.043 60.884 1.00 20.41 ? 130  TYR A CZ    1 
ATOM   997  O OH    . TYR A 1 130 ? -6.934  100.177 59.993 1.00 20.00 ? 130  TYR A OH    1 
ATOM   998  N N     . PHE A 1 131 ? -11.282 104.965 65.852 1.00 18.09 ? 131  PHE A N     1 
ATOM   999  C CA    . PHE A 1 131 ? -11.823 105.952 66.830 1.00 20.44 ? 131  PHE A CA    1 
ATOM   1000 C C     . PHE A 1 131 ? -11.372 105.651 68.256 1.00 18.25 ? 131  PHE A C     1 
ATOM   1001 O O     . PHE A 1 131 ? -10.937 106.579 68.986 1.00 20.54 ? 131  PHE A O     1 
ATOM   1002 C CB    . PHE A 1 131 ? -13.346 106.037 66.755 1.00 21.88 ? 131  PHE A CB    1 
ATOM   1003 C CG    . PHE A 1 131 ? -13.850 106.806 65.573 1.00 20.42 ? 131  PHE A CG    1 
ATOM   1004 C CD1   . PHE A 1 131 ? -13.636 108.161 65.497 1.00 22.26 ? 131  PHE A CD1   1 
ATOM   1005 C CD2   . PHE A 1 131 ? -14.546 106.170 64.565 1.00 22.16 ? 131  PHE A CD2   1 
ATOM   1006 C CE1   . PHE A 1 131 ? -14.100 108.887 64.409 1.00 24.26 ? 131  PHE A CE1   1 
ATOM   1007 C CE2   . PHE A 1 131 ? -15.012 106.895 63.473 1.00 25.46 ? 131  PHE A CE2   1 
ATOM   1008 C CZ    . PHE A 1 131 ? -14.774 108.251 63.392 1.00 22.98 ? 131  PHE A CZ    1 
ATOM   1009 N N     . GLU A 1 132 ? -11.533 104.411 68.704 1.00 22.00 ? 132  GLU A N     1 
ATOM   1010 C CA    . GLU A 1 132 ? -11.227 104.067 70.114 1.00 20.17 ? 132  GLU A CA    1 
ATOM   1011 C C     . GLU A 1 132 ? -9.733  104.266 70.363 1.00 21.75 ? 132  GLU A C     1 
ATOM   1012 O O     . GLU A 1 132 ? -9.358  104.836 71.414 1.00 18.79 ? 132  GLU A O     1 
ATOM   1013 C CB    . GLU A 1 132 ? -11.692 102.653 70.430 1.00 23.50 ? 132  GLU A CB    1 
ATOM   1014 C CG    . GLU A 1 132 ? -13.192 102.506 70.529 1.00 25.64 ? 132  GLU A CG    1 
ATOM   1015 C CD    . GLU A 1 132 ? -13.749 101.078 70.432 1.00 28.11 ? 132  GLU A CD    1 
ATOM   1016 O OE1   . GLU A 1 132 ? -13.025 100.090 70.110 1.00 24.91 ? 132  GLU A OE1   1 
ATOM   1017 O OE2   . GLU A 1 132 ? -14.959 100.973 70.508 1.00 35.14 ? 132  GLU A OE2   1 
ATOM   1018 N N     . LEU A 1 133 ? -8.853  103.816 69.448 1.00 19.00 ? 133  LEU A N     1 
ATOM   1019 C CA    . LEU A 1 133 ? -7.401  103.924 69.711 1.00 19.93 ? 133  LEU A CA    1 
ATOM   1020 C C     . LEU A 1 133 ? -7.020  105.401 69.711 1.00 17.71 ? 133  LEU A C     1 
ATOM   1021 O O     . LEU A 1 133 ? -6.222  105.801 70.577 1.00 18.78 ? 133  LEU A O     1 
ATOM   1022 C CB    . LEU A 1 133 ? -6.599  103.105 68.684 1.00 19.09 ? 133  LEU A CB    1 
ATOM   1023 C CG    . LEU A 1 133 ? -5.083  103.205 68.812 1.00 18.33 ? 133  LEU A CG    1 
ATOM   1024 C CD1   . LEU A 1 133 ? -4.637  102.676 70.166 1.00 19.95 ? 133  LEU A CD1   1 
ATOM   1025 C CD2   . LEU A 1 133 ? -4.407  102.435 67.675 1.00 19.34 ? 133  LEU A CD2   1 
ATOM   1026 N N     . TYR A 1 134 ? -7.532  106.173 68.750 1.00 19.57 ? 134  TYR A N     1 
ATOM   1027 C CA    . TYR A 1 134 ? -7.301  107.643 68.650 1.00 19.96 ? 134  TYR A CA    1 
ATOM   1028 C C     . TYR A 1 134 ? -7.773  108.342 69.948 1.00 22.44 ? 134  TYR A C     1 
ATOM   1029 O O     . TYR A 1 134 ? -6.989  109.099 70.578 1.00 19.30 ? 134  TYR A O     1 
ATOM   1030 C CB    . TYR A 1 134 ? -8.044  108.220 67.452 1.00 21.13 ? 134  TYR A CB    1 
ATOM   1031 C CG    . TYR A 1 134 ? -7.826  109.701 67.278 1.00 22.19 ? 134  TYR A CG    1 
ATOM   1032 C CD1   . TYR A 1 134 ? -6.693  110.195 66.686 1.00 22.19 ? 134  TYR A CD1   1 
ATOM   1033 C CD2   . TYR A 1 134 ? -8.774  110.616 67.716 1.00 23.95 ? 134  TYR A CD2   1 
ATOM   1034 C CE1   . TYR A 1 134 ? -6.503  111.555 66.507 1.00 24.71 ? 134  TYR A CE1   1 
ATOM   1035 C CE2   . TYR A 1 134 ? -8.613  111.983 67.546 1.00 23.99 ? 134  TYR A CE2   1 
ATOM   1036 C CZ    . TYR A 1 134 ? -7.473  112.450 66.934 1.00 24.40 ? 134  TYR A CZ    1 
ATOM   1037 O OH    . TYR A 1 134 ? -7.311  113.772 66.756 1.00 26.59 ? 134  TYR A OH    1 
ATOM   1038 N N     . ASP A 1 135 ? -8.986  108.035 70.384 1.00 22.72 ? 135  ASP A N     1 
ATOM   1039 C CA    . ASP A 1 135 ? -9.546  108.676 71.605 1.00 22.09 ? 135  ASP A CA    1 
ATOM   1040 C C     . ASP A 1 135 ? -8.744  108.275 72.838 1.00 23.12 ? 135  ASP A C     1 
ATOM   1041 O O     . ASP A 1 135 ? -8.536  109.128 73.701 1.00 24.34 ? 135  ASP A O     1 
ATOM   1042 C CB    . ASP A 1 135 ? -11.028 108.372 71.751 1.00 23.09 ? 135  ASP A CB    1 
ATOM   1043 C CG    . ASP A 1 135 ? -11.901 109.046 70.702 1.00 24.27 ? 135  ASP A CG    1 
ATOM   1044 O OD1   . ASP A 1 135 ? -11.426 109.930 69.966 1.00 27.23 ? 135  ASP A OD1   1 
ATOM   1045 O OD2   . ASP A 1 135 ? -13.057 108.627 70.597 1.00 29.91 ? 135  ASP A OD2   1 
ATOM   1046 N N     . TYR A 1 136 ? -8.284  107.033 72.956 1.00 22.23 ? 136  TYR A N     1 
ATOM   1047 C CA    . TYR A 1 136 ? -7.448  106.612 74.095 1.00 22.88 ? 136  TYR A CA    1 
ATOM   1048 C C     . TYR A 1 136 ? -6.191  107.483 74.117 1.00 23.39 ? 136  TYR A C     1 
ATOM   1049 O O     . TYR A 1 136 ? -5.816  108.062 75.154 1.00 23.54 ? 136  TYR A O     1 
ATOM   1050 C CB    . TYR A 1 136 ? -7.180  105.126 73.959 1.00 23.61 ? 136  TYR A CB    1 
ATOM   1051 C CG    . TYR A 1 136 ? -6.309  104.550 75.028 1.00 28.08 ? 136  TYR A CG    1 
ATOM   1052 C CD1   . TYR A 1 136 ? -4.943  104.720 74.992 1.00 25.71 ? 136  TYR A CD1   1 
ATOM   1053 C CD2   . TYR A 1 136 ? -6.865  103.864 76.093 1.00 32.49 ? 136  TYR A CD2   1 
ATOM   1054 C CE1   . TYR A 1 136 ? -4.135  104.190 75.980 1.00 29.95 ? 136  TYR A CE1   1 
ATOM   1055 C CE2   . TYR A 1 136 ? -6.068  103.320 77.087 1.00 35.77 ? 136  TYR A CE2   1 
ATOM   1056 C CZ    . TYR A 1 136 ? -4.698  103.474 77.026 1.00 34.37 ? 136  TYR A CZ    1 
ATOM   1057 O OH    . TYR A 1 136 ? -3.908  102.943 78.002 1.00 40.32 ? 136  TYR A OH    1 
ATOM   1058 N N     . ILE A 1 137 ? -5.527  107.608 72.970 1.00 22.18 ? 137  ILE A N     1 
ATOM   1059 C CA    . ILE A 1 137 ? -4.266  108.385 72.854 1.00 22.82 ? 137  ILE A CA    1 
ATOM   1060 C C     . ILE A 1 137 ? -4.516  109.852 73.263 1.00 23.14 ? 137  ILE A C     1 
ATOM   1061 O O     . ILE A 1 137 ? -3.732  110.397 74.061 1.00 22.44 ? 137  ILE A O     1 
ATOM   1062 C CB    . ILE A 1 137 ? -3.676  108.235 71.441 1.00 21.40 ? 137  ILE A CB    1 
ATOM   1063 C CG1   . ILE A 1 137 ? -3.033  106.854 71.302 1.00 24.82 ? 137  ILE A CG1   1 
ATOM   1064 C CG2   . ILE A 1 137 ? -2.668  109.341 71.172 1.00 21.50 ? 137  ILE A CG2   1 
ATOM   1065 C CD1   . ILE A 1 137 ? -2.729  106.445 69.898 1.00 23.83 ? 137  ILE A CD1   1 
ATOM   1066 N N     . GLN A 1 138 ? -5.565  110.474 72.747 1.00 25.58 ? 138  GLN A N     1 
ATOM   1067 C CA    . GLN A 1 138 ? -5.857  111.900 73.059 1.00 28.85 ? 138  GLN A CA    1 
ATOM   1068 C C     . GLN A 1 138 ? -6.170  112.054 74.543 1.00 29.00 ? 138  GLN A C     1 
ATOM   1069 O O     . GLN A 1 138 ? -5.624  113.017 75.177 1.00 29.85 ? 138  GLN A O     1 
ATOM   1070 C CB    . GLN A 1 138 ? -7.075  112.433 72.322 1.00 30.46 ? 138  GLN A CB    1 
ATOM   1071 C CG    . GLN A 1 138 ? -6.976  112.343 70.815 1.00 34.29 ? 138  GLN A CG    1 
ATOM   1072 C CD    . GLN A 1 138 ? -5.628  112.688 70.234 1.00 36.63 ? 138  GLN A CD    1 
ATOM   1073 O OE1   . GLN A 1 138 ? -5.082  113.767 70.430 1.00 33.87 ? 138  GLN A OE1   1 
ATOM   1074 N NE2   . GLN A 1 138 ? -5.096  111.751 69.467 1.00 39.70 ? 138  GLN A NE2   1 
ATOM   1075 N N     . GLU A 1 139 ? -6.921  111.115 75.113 1.00 27.31 ? 139  GLU A N     1 
ATOM   1076 C CA    . GLU A 1 139 ? -7.335  111.213 76.547 1.00 35.20 ? 139  GLU A CA    1 
ATOM   1077 C C     . GLU A 1 139 ? -6.093  111.098 77.424 1.00 37.45 ? 139  GLU A C     1 
ATOM   1078 O O     . GLU A 1 139 ? -6.031  111.827 78.404 1.00 32.68 ? 139  GLU A O     1 
ATOM   1079 C CB    . GLU A 1 139 ? -8.328  110.139 76.982 1.00 38.02 ? 139  GLU A CB    1 
ATOM   1080 C CG    . GLU A 1 139 ? -9.704  110.278 76.351 1.00 47.92 ? 139  GLU A CG    1 
ATOM   1081 C CD    . GLU A 1 139 ? -10.547 108.999 76.382 1.00 59.90 ? 139  GLU A CD    1 
ATOM   1082 O OE1   . GLU A 1 139 ? -11.610 108.945 75.693 1.00 58.72 ? 139  GLU A OE1   1 
ATOM   1083 O OE2   . GLU A 1 139 ? -10.129 108.036 77.075 1.00 65.56 ? 139  GLU A OE2   1 
ATOM   1084 N N     . LYS A 1 140 ? -5.133  110.226 77.083 1.00 31.60 ? 140  LYS A N     1 
ATOM   1085 C CA    . LYS A 1 140 ? -3.924  110.020 77.905 1.00 28.21 ? 140  LYS A CA    1 
ATOM   1086 C C     . LYS A 1 140 ? -2.866  111.075 77.576 1.00 26.04 ? 140  LYS A C     1 
ATOM   1087 O O     . LYS A 1 140 ? -1.838  111.048 78.228 1.00 31.77 ? 140  LYS A O     1 
ATOM   1088 C CB    . LYS A 1 140 ? -3.387  108.586 77.809 1.00 30.96 ? 140  LYS A CB    1 
ATOM   1089 C CG    . LYS A 1 140 ? -4.272  107.484 78.373 1.00 36.58 ? 140  LYS A CG    1 
ATOM   1090 C CD    . LYS A 1 140 ? -4.946  107.853 79.673 1.00 48.24 ? 140  LYS A CD    1 
ATOM   1091 C CE    . LYS A 1 140 ? -6.004  106.875 80.156 1.00 57.68 ? 140  LYS A CE    1 
ATOM   1092 N NZ    . LYS A 1 140 ? -5.510  105.476 80.112 1.00 69.43 ? 140  LYS A NZ    1 
ATOM   1093 N N     . GLY A 1 141 ? -3.050  111.898 76.557 1.00 24.10 ? 141  GLY A N     1 
ATOM   1094 C CA    . GLY A 1 141 ? -2.064  112.901 76.123 1.00 27.40 ? 141  GLY A CA    1 
ATOM   1095 C C     . GLY A 1 141 ? -0.775  112.258 75.605 1.00 29.18 ? 141  GLY A C     1 
ATOM   1096 O O     . GLY A 1 141 ? 0.285   112.891 75.705 1.00 26.02 ? 141  GLY A O     1 
ATOM   1097 N N     . LEU A 1 142 ? -0.868  111.070 75.008 1.00 24.93 ? 142  LEU A N     1 
ATOM   1098 C CA    . LEU A 1 142 ? 0.298   110.366 74.407 1.00 24.48 ? 142  LEU A CA    1 
ATOM   1099 C C     . LEU A 1 142 ? 0.671   111.068 73.096 1.00 23.26 ? 142  LEU A C     1 
ATOM   1100 O O     . LEU A 1 142 ? -0.226  111.426 72.284 1.00 21.60 ? 142  LEU A O     1 
ATOM   1101 C CB    . LEU A 1 142 ? -0.017  108.867 74.234 1.00 22.80 ? 142  LEU A CB    1 
ATOM   1102 C CG    . LEU A 1 142 ? -0.363  108.117 75.510 1.00 25.57 ? 142  LEU A CG    1 
ATOM   1103 C CD1   . LEU A 1 142 ? -0.391  106.644 75.274 1.00 26.29 ? 142  LEU A CD1   1 
ATOM   1104 C CD2   . LEU A 1 142 ? 0.620   108.414 76.637 1.00 26.26 ? 142  LEU A CD2   1 
ATOM   1105 N N     . LYS A 1 143 ? 1.952   111.298 72.895 1.00 21.45 ? 143  LYS A N     1 
ATOM   1106 C CA    . LYS A 1 143 ? 2.481   112.003 71.694 1.00 23.24 ? 143  LYS A CA    1 
ATOM   1107 C C     . LYS A 1 143 ? 2.715   111.013 70.536 1.00 21.86 ? 143  LYS A C     1 
ATOM   1108 O O     . LYS A 1 143 ? 3.859   110.860 70.068 1.00 21.72 ? 143  LYS A O     1 
ATOM   1109 C CB    . LYS A 1 143 ? 3.754   112.743 72.070 1.00 27.52 ? 143  LYS A CB    1 
ATOM   1110 C CG    . LYS A 1 143 ? 3.522   113.871 73.071 1.00 36.86 ? 143  LYS A CG    1 
ATOM   1111 C CD    . LYS A 1 143 ? 4.819   114.180 73.830 1.00 49.57 ? 143  LYS A CD    1 
ATOM   1112 C CE    . LYS A 1 143 ? 5.202   115.643 73.800 1.00 65.29 ? 143  LYS A CE    1 
ATOM   1113 N NZ    . LYS A 1 143 ? 4.048   116.509 74.151 1.00 75.95 ? 143  LYS A NZ    1 
ATOM   1114 N N     . LEU A 1 144 ? 1.618   110.477 70.026 1.00 21.44 ? 144  LEU A N     1 
ATOM   1115 C CA    . LEU A 1 144 ? 1.599   109.444 68.981 1.00 22.34 ? 144  LEU A CA    1 
ATOM   1116 C C     . LEU A 1 144 ? 0.500   109.801 68.020 1.00 20.50 ? 144  LEU A C     1 
ATOM   1117 O O     . LEU A 1 144 ? -0.558  110.210 68.462 1.00 20.41 ? 144  LEU A O     1 
ATOM   1118 C CB    . LEU A 1 144 ? 1.286   108.072 69.567 1.00 20.44 ? 144  LEU A CB    1 
ATOM   1119 C CG    . LEU A 1 144 ? 2.292   107.548 70.570 1.00 23.72 ? 144  LEU A CG    1 
ATOM   1120 C CD1   . LEU A 1 144 ? 1.725   106.306 71.254 1.00 25.95 ? 144  LEU A CD1   1 
ATOM   1121 C CD2   . LEU A 1 144 ? 3.625   107.281 69.910 1.00 22.07 ? 144  LEU A CD2   1 
ATOM   1122 N N     . TRP A 1 145 ? 0.731   109.487 66.761 1.00 18.45 ? 145  TRP A N     1 
ATOM   1123 C CA    . TRP A 1 145 ? -0.295  109.507 65.712 1.00 20.92 ? 145  TRP A CA    1 
ATOM   1124 C C     . TRP A 1 145 ? -0.573  108.071 65.295 1.00 22.08 ? 145  TRP A C     1 
ATOM   1125 O O     . TRP A 1 145 ? 0.330   107.222 65.392 1.00 21.56 ? 145  TRP A O     1 
ATOM   1126 C CB    . TRP A 1 145 ? 0.175   110.345 64.519 1.00 21.40 ? 145  TRP A CB    1 
ATOM   1127 C CG    . TRP A 1 145 ? 0.203   111.812 64.779 1.00 22.95 ? 145  TRP A CG    1 
ATOM   1128 C CD1   . TRP A 1 145 ? -0.079  112.439 65.964 1.00 23.64 ? 145  TRP A CD1   1 
ATOM   1129 C CD2   . TRP A 1 145 ? 0.516   112.847 63.834 1.00 21.21 ? 145  TRP A CD2   1 
ATOM   1130 N NE1   . TRP A 1 145 ? 0.040   113.793 65.800 1.00 25.40 ? 145  TRP A NE1   1 
ATOM   1131 C CE2   . TRP A 1 145 ? 0.401   114.076 64.519 1.00 24.54 ? 145  TRP A CE2   1 
ATOM   1132 C CE3   . TRP A 1 145 ? 0.895   112.856 62.495 1.00 23.81 ? 145  TRP A CE3   1 
ATOM   1133 C CZ2   . TRP A 1 145 ? 0.608   115.304 63.900 1.00 26.03 ? 145  TRP A CZ2   1 
ATOM   1134 C CZ3   . TRP A 1 145 ? 1.072   114.061 61.869 1.00 23.34 ? 145  TRP A CZ3   1 
ATOM   1135 C CH2   . TRP A 1 145 ? 0.918   115.267 62.567 1.00 25.38 ? 145  TRP A CH2   1 
ATOM   1136 N N     . ILE A 1 146 ? -1.804  107.827 64.896 1.00 20.11 ? 146  ILE A N     1 
ATOM   1137 C CA    . ILE A 1 146 ? -2.240  106.546 64.305 1.00 18.83 ? 146  ILE A CA    1 
ATOM   1138 C C     . ILE A 1 146 ? -2.299  106.750 62.807 1.00 18.62 ? 146  ILE A C     1 
ATOM   1139 O O     . ILE A 1 146 ? -2.003  107.859 62.325 1.00 18.85 ? 146  ILE A O     1 
ATOM   1140 C CB    . ILE A 1 146 ? -3.549  106.049 64.933 1.00 18.19 ? 146  ILE A CB    1 
ATOM   1141 C CG1   . ILE A 1 146 ? -4.752  106.951 64.639 1.00 19.28 ? 146  ILE A CG1   1 
ATOM   1142 C CG2   . ILE A 1 146 ? -3.360  105.860 66.418 1.00 19.29 ? 146  ILE A CG2   1 
ATOM   1143 C CD1   . ILE A 1 146 ? -6.071  106.230 64.873 1.00 19.65 ? 146  ILE A CD1   1 
ATOM   1144 N N     . ASP A 1 147 ? -2.542  105.668 62.093 1.00 19.16 ? 147  ASP A N     1 
ATOM   1145 C CA    . ASP A 1 147 ? -2.679  105.731 60.624 1.00 20.08 ? 147  ASP A CA    1 
ATOM   1146 C C     . ASP A 1 147 ? -4.042  105.152 60.291 1.00 19.82 ? 147  ASP A C     1 
ATOM   1147 O O     . ASP A 1 147 ? -4.263  103.976 60.579 1.00 18.97 ? 147  ASP A O     1 
ATOM   1148 C CB    . ASP A 1 147 ? -1.524  105.032 59.911 1.00 20.44 ? 147  ASP A CB    1 
ATOM   1149 C CG    . ASP A 1 147 ? -1.594  105.307 58.425 1.00 19.03 ? 147  ASP A CG    1 
ATOM   1150 O OD1   . ASP A 1 147 ? -2.599  104.852 57.811 1.00 18.66 ? 147  ASP A OD1   1 
ATOM   1151 O OD2   . ASP A 1 147 ? -0.688  106.022 57.935 1.00 17.81 ? 147  ASP A OD2   1 
ATOM   1152 N N     . VAL A 1 148 ? -4.915  105.972 59.707 1.00 19.56 ? 148  VAL A N     1 
ATOM   1153 C CA    . VAL A 1 148 ? -6.331  105.599 59.485 1.00 18.40 ? 148  VAL A CA    1 
ATOM   1154 C C     . VAL A 1 148 ? -6.567  105.412 58.003 1.00 18.20 ? 148  VAL A C     1 
ATOM   1155 O O     . VAL A 1 148 ? -6.067  106.172 57.171 1.00 20.12 ? 148  VAL A O     1 
ATOM   1156 C CB    . VAL A 1 148 ? -7.326  106.632 60.065 1.00 20.23 ? 148  VAL A CB    1 
ATOM   1157 C CG1   . VAL A 1 148 ? -7.209  106.751 61.569 1.00 19.99 ? 148  VAL A CG1   1 
ATOM   1158 C CG2   . VAL A 1 148 ? -7.214  107.989 59.392 1.00 18.72 ? 148  VAL A CG2   1 
ATOM   1159 N N     . PRO A 1 149 ? -7.432  104.453 57.664 1.00 18.74 ? 149  PRO A N     1 
ATOM   1160 C CA    . PRO A 1 149 ? -8.036  104.417 56.347 1.00 20.68 ? 149  PRO A CA    1 
ATOM   1161 C C     . PRO A 1 149 ? -9.087  105.553 56.350 1.00 22.53 ? 149  PRO A C     1 
ATOM   1162 O O     . PRO A 1 149 ? -9.227  106.317 57.368 1.00 19.20 ? 149  PRO A O     1 
ATOM   1163 C CB    . PRO A 1 149 ? -8.632  103.026 56.287 1.00 20.29 ? 149  PRO A CB    1 
ATOM   1164 C CG    . PRO A 1 149 ? -9.066  102.772 57.720 1.00 21.55 ? 149  PRO A CG    1 
ATOM   1165 C CD    . PRO A 1 149 ? -8.072  103.503 58.598 1.00 18.76 ? 149  PRO A CD    1 
ATOM   1166 N N     . ASP A 1 150 ? -9.771  105.741 55.231 1.00 23.75 ? 150  ASP A N     1 
ATOM   1167 C CA    . ASP A 1 150 ? -10.773 106.833 55.124 1.00 26.85 ? 150  ASP A CA    1 
ATOM   1168 C C     . ASP A 1 150 ? -11.848 106.638 56.211 1.00 26.77 ? 150  ASP A C     1 
ATOM   1169 O O     . ASP A 1 150 ? -12.430 107.644 56.612 1.00 30.18 ? 150  ASP A O     1 
ATOM   1170 C CB    . ASP A 1 150 ? -11.410 106.883 53.744 1.00 27.71 ? 150  ASP A CB    1 
ATOM   1171 C CG    . ASP A 1 150 ? -10.483 107.403 52.674 1.00 30.01 ? 150  ASP A CG    1 
ATOM   1172 O OD1   . ASP A 1 150 ? -9.695  108.363 52.952 1.00 32.10 ? 150  ASP A OD1   1 
ATOM   1173 O OD2   . ASP A 1 150 ? -10.582 106.864 51.573 1.00 34.62 ? 150  ASP A OD2   1 
ATOM   1174 N N     . LEU A 1 151 ? -12.212 105.402 56.579 1.00 24.36 ? 151  LEU A N     1 
ATOM   1175 C CA    . LEU A 1 151 ? -13.346 105.219 57.523 1.00 25.28 ? 151  LEU A CA    1 
ATOM   1176 C C     . LEU A 1 151 ? -12.822 104.803 58.904 1.00 27.12 ? 151  LEU A C     1 
ATOM   1177 O O     . LEU A 1 151 ? -12.307 103.675 59.054 1.00 30.66 ? 151  LEU A O     1 
ATOM   1178 C CB    . LEU A 1 151 ? -14.350 104.245 56.913 1.00 26.28 ? 151  LEU A CB    1 
ATOM   1179 C CG    . LEU A 1 151 ? -14.840 104.686 55.525 1.00 26.14 ? 151  LEU A CG    1 
ATOM   1180 C CD1   . LEU A 1 151 ? -15.629 103.592 54.908 1.00 30.83 ? 151  LEU A CD1   1 
ATOM   1181 C CD2   . LEU A 1 151 ? -15.663 105.949 55.646 1.00 28.52 ? 151  LEU A CD2   1 
ATOM   1182 N N     . GLY A 1 152 ? -13.030 105.647 59.907 1.00 22.21 ? 152  GLY A N     1 
ATOM   1183 C CA    . GLY A 1 152 ? -12.457 105.417 61.250 1.00 21.80 ? 152  GLY A CA    1 
ATOM   1184 C C     . GLY A 1 152 ? -13.137 104.343 62.072 1.00 20.84 ? 152  GLY A C     1 
ATOM   1185 O O     . GLY A 1 152 ? -12.601 103.962 63.119 1.00 21.77 ? 152  GLY A O     1 
ATOM   1186 N N     . TRP A 1 153 ? -14.286 103.833 61.651 1.00 21.38 ? 153  TRP A N     1 
ATOM   1187 C CA    . TRP A 1 153 ? -15.043 102.845 62.452 1.00 21.03 ? 153  TRP A CA    1 
ATOM   1188 C C     . TRP A 1 153 ? -14.558 101.406 62.208 1.00 23.79 ? 153  TRP A C     1 
ATOM   1189 O O     . TRP A 1 153 ? -15.108 100.499 62.835 1.00 22.50 ? 153  TRP A O     1 
ATOM   1190 C CB    . TRP A 1 153 ? -16.542 102.996 62.240 1.00 20.85 ? 153  TRP A CB    1 
ATOM   1191 C CG    . TRP A 1 153 ? -17.079 102.658 60.888 1.00 22.91 ? 153  TRP A CG    1 
ATOM   1192 C CD1   . TRP A 1 153 ? -16.444 102.132 59.803 1.00 24.27 ? 153  TRP A CD1   1 
ATOM   1193 C CD2   . TRP A 1 153 ? -18.440 102.843 60.497 1.00 24.62 ? 153  TRP A CD2   1 
ATOM   1194 N NE1   . TRP A 1 153 ? -17.331 101.960 58.773 1.00 26.34 ? 153  TRP A NE1   1 
ATOM   1195 C CE2   . TRP A 1 153 ? -18.570 102.375 59.181 1.00 25.95 ? 153  TRP A CE2   1 
ATOM   1196 C CE3   . TRP A 1 153 ? -19.556 103.353 61.160 1.00 24.50 ? 153  TRP A CE3   1 
ATOM   1197 C CZ2   . TRP A 1 153 ? -19.782 102.390 58.501 1.00 27.75 ? 153  TRP A CZ2   1 
ATOM   1198 C CZ3   . TRP A 1 153 ? -20.749 103.392 60.477 1.00 26.97 ? 153  TRP A CZ3   1 
ATOM   1199 C CH2   . TRP A 1 153 ? -20.866 102.891 59.186 1.00 24.83 ? 153  TRP A CH2   1 
ATOM   1200 N N     . GLY A 1 154 ? -13.559 101.219 61.347 1.00 22.00 ? 154  GLY A N     1 
ATOM   1201 C CA    . GLY A 1 154 ? -12.989 99.891  61.053 1.00 21.74 ? 154  GLY A CA    1 
ATOM   1202 C C     . GLY A 1 154 ? -12.070 99.447  62.173 1.00 19.36 ? 154  GLY A C     1 
ATOM   1203 O O     . GLY A 1 154 ? -11.919 100.173 63.161 1.00 21.57 ? 154  GLY A O     1 
ATOM   1204 N N     . SER A 1 155 ? -11.462 98.289  62.012 1.00 18.74 ? 155  SER A N     1 
ATOM   1205 C CA    . SER A 1 155 ? -10.575 97.625  62.990 1.00 18.53 ? 155  SER A CA    1 
ATOM   1206 C C     . SER A 1 155 ? -9.104  97.898  62.632 1.00 18.48 ? 155  SER A C     1 
ATOM   1207 O O     . SER A 1 155 ? -8.687  97.547  61.501 1.00 19.73 ? 155  SER A O     1 
ATOM   1208 C CB    . SER A 1 155 ? -10.871 96.158  62.999 1.00 16.73 ? 155  SER A CB    1 
ATOM   1209 O OG    . SER A 1 155 ? -9.910  95.460  63.757 1.00 17.57 ? 155  SER A OG    1 
ATOM   1210 N N     . VAL A 1 156 ? -8.321  98.343  63.613 1.00 17.70 ? 156  VAL A N     1 
ATOM   1211 C CA    . VAL A 1 156 ? -6.857  98.410  63.525 1.00 18.23 ? 156  VAL A CA    1 
ATOM   1212 C C     . VAL A 1 156 ? -6.320  97.045  63.061 1.00 19.74 ? 156  VAL A C     1 
ATOM   1213 O O     . VAL A 1 156 ? -5.519  97.030  62.131 1.00 17.09 ? 156  VAL A O     1 
ATOM   1214 C CB    . VAL A 1 156 ? -6.249  98.826  64.869 1.00 19.26 ? 156  VAL A CB    1 
ATOM   1215 C CG1   . VAL A 1 156 ? -4.731  98.976  64.758 1.00 20.83 ? 156  VAL A CG1   1 
ATOM   1216 C CG2   . VAL A 1 156 ? -6.865  100.121 65.331 1.00 20.67 ? 156  VAL A CG2   1 
ATOM   1217 N N     . VAL A 1 157 ? -6.819  95.954  63.627 1.00 17.95 ? 157  VAL A N     1 
ATOM   1218 C CA    . VAL A 1 157 ? -6.430  94.563  63.283 1.00 17.74 ? 157  VAL A CA    1 
ATOM   1219 C C     . VAL A 1 157 ? -7.031  94.162  61.939 1.00 18.35 ? 157  VAL A C     1 
ATOM   1220 O O     . VAL A 1 157 ? -6.246  93.750  61.032 1.00 20.44 ? 157  VAL A O     1 
ATOM   1221 C CB    . VAL A 1 157 ? -6.853  93.592  64.391 1.00 17.84 ? 157  VAL A CB    1 
ATOM   1222 C CG1   . VAL A 1 157 ? -6.648  92.160  64.002 1.00 18.43 ? 157  VAL A CG1   1 
ATOM   1223 C CG2   . VAL A 1 157 ? -6.134  93.903  65.687 1.00 18.85 ? 157  VAL A CG2   1 
ATOM   1224 N N     . GLY A 1 158 ? -8.335  94.195  61.805 1.00 16.45 ? 158  GLY A N     1 
ATOM   1225 C CA    . GLY A 1 158 ? -8.985  93.598  60.613 1.00 18.27 ? 158  GLY A CA    1 
ATOM   1226 C C     . GLY A 1 158 ? -8.503  94.277  59.331 1.00 18.64 ? 158  GLY A C     1 
ATOM   1227 O O     . GLY A 1 158 ? -8.296  93.586  58.276 1.00 17.82 ? 158  GLY A O     1 
ATOM   1228 N N     . ASN A 1 159 ? -8.422  95.596  59.349 1.00 18.65 ? 159  ASN A N     1 
ATOM   1229 C CA    . ASN A 1 159 ? -7.992  96.355  58.155 1.00 18.69 ? 159  ASN A CA    1 
ATOM   1230 C C     . ASN A 1 159 ? -6.560  95.925  57.798 1.00 19.42 ? 159  ASN A C     1 
ATOM   1231 O O     . ASN A 1 159 ? -6.304  95.592  56.621 1.00 17.68 ? 159  ASN A O     1 
ATOM   1232 C CB    . ASN A 1 159 ? -8.121  97.845  58.404 1.00 20.15 ? 159  ASN A CB    1 
ATOM   1233 C CG    . ASN A 1 159 ? -7.516  98.644  57.275 1.00 21.14 ? 159  ASN A CG    1 
ATOM   1234 O OD1   . ASN A 1 159 ? -6.292  98.768  57.206 1.00 22.24 ? 159  ASN A OD1   1 
ATOM   1235 N ND2   . ASN A 1 159 ? -8.349  99.119  56.373 1.00 21.02 ? 159  ASN A ND2   1 
ATOM   1236 N N     . ALA A 1 160 ? -5.650  95.921  58.766 1.00 17.85 ? 160  ALA A N     1 
ATOM   1237 C CA    . ALA A 1 160 ? -4.252  95.494  58.534 1.00 19.27 ? 160  ALA A CA    1 
ATOM   1238 C C     . ALA A 1 160 ? -4.233  94.090  57.933 1.00 20.12 ? 160  ALA A C     1 
ATOM   1239 O O     . ALA A 1 160 ? -3.485  93.830  56.979 1.00 16.81 ? 160  ALA A O     1 
ATOM   1240 C CB    . ALA A 1 160 ? -3.471  95.560  59.818 1.00 19.78 ? 160  ALA A CB    1 
ATOM   1241 N N     . LEU A 1 161 ? -5.018  93.163  58.485 1.00 18.01 ? 161  LEU A N     1 
ATOM   1242 C CA    . LEU A 1 161 ? -4.992  91.771  58.047 1.00 16.00 ? 161  LEU A CA    1 
ATOM   1243 C C     . LEU A 1 161 ? -5.458  91.671  56.602 1.00 19.26 ? 161  LEU A C     1 
ATOM   1244 O O     . LEU A 1 161 ? -4.944  90.770  55.887 1.00 19.06 ? 161  LEU A O     1 
ATOM   1245 C CB    . LEU A 1 161 ? -5.850  90.906  58.969 1.00 18.82 ? 161  LEU A CB    1 
ATOM   1246 C CG    . LEU A 1 161 ? -5.237  90.620  60.342 1.00 18.21 ? 161  LEU A CG    1 
ATOM   1247 C CD1   . LEU A 1 161 ? -6.211  89.785  61.150 1.00 20.07 ? 161  LEU A CD1   1 
ATOM   1248 C CD2   . LEU A 1 161 ? -3.913  89.887  60.258 1.00 19.05 ? 161  LEU A CD2   1 
ATOM   1249 N N     . ASP A 1 162 ? -6.346  92.553  56.147 1.00 17.69 ? 162  ASP A N     1 
ATOM   1250 C CA    . ASP A 1 162 ? -6.785  92.535  54.745 1.00 17.60 ? 162  ASP A CA    1 
ATOM   1251 C C     . ASP A 1 162 ? -5.822  93.367  53.886 1.00 17.43 ? 162  ASP A C     1 
ATOM   1252 O O     . ASP A 1 162 ? -6.173  93.581  52.721 1.00 18.35 ? 162  ASP A O     1 
ATOM   1253 C CB    . ASP A 1 162 ? -8.233  92.970  54.586 1.00 19.73 ? 162  ASP A CB    1 
ATOM   1254 C CG    . ASP A 1 162 ? -8.989  92.180  53.529 1.00 21.00 ? 162  ASP A CG    1 
ATOM   1255 O OD1   . ASP A 1 162 ? -8.651  90.981  53.339 1.00 23.25 ? 162  ASP A OD1   1 
ATOM   1256 O OD2   . ASP A 1 162 ? -9.944  92.741  52.929 1.00 20.98 ? 162  ASP A OD2   1 
ATOM   1257 N N     . HIS A 1 163 ? -4.648  93.748  54.383 1.00 16.25 ? 163  HIS A N     1 
ATOM   1258 C CA    . HIS A 1 163 ? -3.606  94.528  53.645 1.00 18.56 ? 163  HIS A CA    1 
ATOM   1259 C C     . HIS A 1 163 ? -4.120  95.945  53.347 1.00 17.34 ? 163  HIS A C     1 
ATOM   1260 O O     . HIS A 1 163 ? -3.694  96.565  52.339 1.00 17.23 ? 163  HIS A O     1 
ATOM   1261 C CB    . HIS A 1 163 ? -3.121  93.787  52.372 1.00 17.81 ? 163  HIS A CB    1 
ATOM   1262 C CG    . HIS A 1 163 ? -2.573  92.419  52.624 1.00 18.05 ? 163  HIS A CG    1 
ATOM   1263 N ND1   . HIS A 1 163 ? -2.336  91.536  51.567 1.00 17.62 ? 163  HIS A ND1   1 
ATOM   1264 C CD2   . HIS A 1 163 ? -2.201  91.780  53.766 1.00 18.36 ? 163  HIS A CD2   1 
ATOM   1265 C CE1   . HIS A 1 163 ? -1.788  90.437  52.063 1.00 19.23 ? 163  HIS A CE1   1 
ATOM   1266 N NE2   . HIS A 1 163 ? -1.666  90.553  53.408 1.00 18.10 ? 163  HIS A NE2   1 
ATOM   1267 N N     . GLY A 1 164 ? -4.872  96.522  54.293 1.00 17.85 ? 164  GLY A N     1 
ATOM   1268 C CA    . GLY A 1 164 ? -5.461  97.854  54.134 1.00 18.23 ? 164  GLY A CA    1 
ATOM   1269 C C     . GLY A 1 164 ? -4.402  98.941  54.195 1.00 19.90 ? 164  GLY A C     1 
ATOM   1270 O O     . GLY A 1 164 ? -3.223  98.709  54.624 1.00 16.93 ? 164  GLY A O     1 
ATOM   1271 N N     . ILE A 1 165 ? -4.796  100.131 53.747 1.00 19.69 ? 165  ILE A N     1 
ATOM   1272 C CA    . ILE A 1 165 ? -3.893  101.277 53.577 1.00 20.11 ? 165  ILE A CA    1 
ATOM   1273 C C     . ILE A 1 165 ? -4.481  102.531 54.196 1.00 19.93 ? 165  ILE A C     1 
ATOM   1274 O O     . ILE A 1 165 ? -5.694  102.730 54.210 1.00 19.78 ? 165  ILE A O     1 
ATOM   1275 C CB    . ILE A 1 165 ? -3.554  101.476 52.087 1.00 22.44 ? 165  ILE A CB    1 
ATOM   1276 C CG1   . ILE A 1 165 ? -4.785  101.790 51.237 1.00 26.07 ? 165  ILE A CG1   1 
ATOM   1277 C CG2   . ILE A 1 165 ? -2.833  100.241 51.579 1.00 22.63 ? 165  ILE A CG2   1 
ATOM   1278 C CD1   . ILE A 1 165 ? -4.434  102.127 49.790 1.00 28.54 ? 165  ILE A CD1   1 
ATOM   1279 N N     . GLY A 1 166 ? -3.573  103.410 54.571 1.00 18.86 ? 166  GLY A N     1 
ATOM   1280 C CA    . GLY A 1 166 ? -3.883  104.793 54.973 1.00 20.41 ? 166  GLY A CA    1 
ATOM   1281 C C     . GLY A 1 166 ? -2.816  105.735 54.472 1.00 18.66 ? 166  GLY A C     1 
ATOM   1282 O O     . GLY A 1 166 ? -2.163  105.386 53.439 1.00 19.48 ? 166  GLY A O     1 
ATOM   1283 N N     . TYR A 1 167 ? -2.714  106.912 55.097 1.00 18.44 ? 167  TYR A N     1 
ATOM   1284 C CA    . TYR A 1 167 ? -2.337  108.157 54.387 1.00 18.24 ? 167  TYR A CA    1 
ATOM   1285 C C     . TYR A 1 167 ? -1.274  108.932 55.122 1.00 18.05 ? 167  TYR A C     1 
ATOM   1286 O O     . TYR A 1 167 ? -1.066  110.100 54.735 1.00 19.57 ? 167  TYR A O     1 
ATOM   1287 C CB    . TYR A 1 167 ? -3.605  108.938 54.026 1.00 19.49 ? 167  TYR A CB    1 
ATOM   1288 C CG    . TYR A 1 167 ? -4.580  108.072 53.271 1.00 19.00 ? 167  TYR A CG    1 
ATOM   1289 C CD1   . TYR A 1 167 ? -4.299  107.693 51.967 1.00 21.74 ? 167  TYR A CD1   1 
ATOM   1290 C CD2   . TYR A 1 167 ? -5.737  107.574 53.872 1.00 18.28 ? 167  TYR A CD2   1 
ATOM   1291 C CE1   . TYR A 1 167 ? -5.145  106.830 51.277 1.00 21.72 ? 167  TYR A CE1   1 
ATOM   1292 C CE2   . TYR A 1 167 ? -6.611  106.727 53.192 1.00 20.42 ? 167  TYR A CE2   1 
ATOM   1293 C CZ    . TYR A 1 167 ? -6.298  106.343 51.895 1.00 21.87 ? 167  TYR A CZ    1 
ATOM   1294 O OH    . TYR A 1 167 ? -7.113  105.488 51.234 1.00 21.65 ? 167  TYR A OH    1 
ATOM   1295 N N     . THR A 1 168 ? -0.590  108.303 56.100 1.00 18.66 ? 168  THR A N     1 
ATOM   1296 C CA    . THR A 1 168 ? 0.593   108.870 56.794 1.00 19.32 ? 168  THR A CA    1 
ATOM   1297 C C     . THR A 1 168 ? 1.819   108.058 56.364 1.00 19.37 ? 168  THR A C     1 
ATOM   1298 O O     . THR A 1 168 ? 1.715   107.129 55.554 1.00 18.41 ? 168  THR A O     1 
ATOM   1299 C CB    . THR A 1 168 ? 0.411   108.901 58.333 1.00 20.27 ? 168  THR A CB    1 
ATOM   1300 O OG1   . THR A 1 168 ? 0.839   107.671 58.953 1.00 19.36 ? 168  THR A OG1   1 
ATOM   1301 C CG2   . THR A 1 168 ? -1.000  109.266 58.710 1.00 19.43 ? 168  THR A CG2   1 
ATOM   1302 N N     . PRO A 1 169 ? 3.015   108.331 56.917 1.00 18.70 ? 169  PRO A N     1 
ATOM   1303 C CA    . PRO A 1 169 ? 4.173   107.496 56.628 1.00 20.85 ? 169  PRO A CA    1 
ATOM   1304 C C     . PRO A 1 169 ? 3.973   106.058 57.105 1.00 21.62 ? 169  PRO A C     1 
ATOM   1305 O O     . PRO A 1 169 ? 4.678   105.221 56.618 1.00 19.50 ? 169  PRO A O     1 
ATOM   1306 C CB    . PRO A 1 169 ? 5.322   108.201 57.368 1.00 21.28 ? 169  PRO A CB    1 
ATOM   1307 C CG    . PRO A 1 169 ? 4.837   109.650 57.426 1.00 21.00 ? 169  PRO A CG    1 
ATOM   1308 C CD    . PRO A 1 169 ? 3.369   109.512 57.700 1.00 19.54 ? 169  PRO A CD    1 
ATOM   1309 N N     . TYR A 1 170 ? 3.005   105.799 57.998 1.00 18.92 ? 170  TYR A N     1 
ATOM   1310 C CA    . TYR A 1 170 ? 2.666   104.449 58.506 1.00 18.72 ? 170  TYR A CA    1 
ATOM   1311 C C     . TYR A 1 170 ? 1.470   103.870 57.734 1.00 18.48 ? 170  TYR A C     1 
ATOM   1312 O O     . TYR A 1 170 ? 0.736   103.028 58.251 1.00 19.14 ? 170  TYR A O     1 
ATOM   1313 C CB    . TYR A 1 170 ? 2.448   104.538 60.017 1.00 18.39 ? 170  TYR A CB    1 
ATOM   1314 C CG    . TYR A 1 170 ? 3.711   104.583 60.863 1.00 17.75 ? 170  TYR A CG    1 
ATOM   1315 C CD1   . TYR A 1 170 ? 4.701   105.534 60.673 1.00 18.03 ? 170  TYR A CD1   1 
ATOM   1316 C CD2   . TYR A 1 170 ? 3.907   103.702 61.905 1.00 16.03 ? 170  TYR A CD2   1 
ATOM   1317 C CE1   . TYR A 1 170 ? 5.868   105.563 61.443 1.00 17.89 ? 170  TYR A CE1   1 
ATOM   1318 C CE2   . TYR A 1 170 ? 5.048   103.719 62.692 1.00 16.43 ? 170  TYR A CE2   1 
ATOM   1319 C CZ    . TYR A 1 170 ? 6.032   104.669 62.491 1.00 16.49 ? 170  TYR A CZ    1 
ATOM   1320 O OH    . TYR A 1 170 ? 7.159   104.702 63.263 1.00 19.32 ? 170  TYR A OH    1 
ATOM   1321 N N     . GLY A 1 171 ? 1.308   104.258 56.454 1.00 17.82 ? 171  GLY A N     1 
ATOM   1322 C CA    . GLY A 1 171 ? 0.153   103.913 55.617 1.00 18.65 ? 171  GLY A CA    1 
ATOM   1323 C C     . GLY A 1 171 ? 0.063   102.450 55.204 1.00 18.45 ? 171  GLY A C     1 
ATOM   1324 O O     . GLY A 1 171 ? -1.041  102.026 54.776 1.00 18.81 ? 171  GLY A O     1 
ATOM   1325 N N     . ASP A 1 172 ? 1.157   101.681 55.221 1.00 18.28 ? 172  ASP A N     1 
ATOM   1326 C CA    . ASP A 1 172 ? 1.060   100.240 54.896 1.00 19.03 ? 172  ASP A CA    1 
ATOM   1327 C C     . ASP A 1 172 ? 0.742   99.512  56.212 1.00 17.32 ? 172  ASP A C     1 
ATOM   1328 O O     . ASP A 1 172 ? 1.692   99.219  56.974 1.00 17.61 ? 172  ASP A O     1 
ATOM   1329 C CB    . ASP A 1 172 ? 2.343   99.738  54.240 1.00 20.99 ? 172  ASP A CB    1 
ATOM   1330 C CG    . ASP A 1 172 ? 2.278   98.293  53.778 1.00 22.41 ? 172  ASP A CG    1 
ATOM   1331 O OD1   . ASP A 1 172 ? 1.448   97.493  54.288 1.00 21.67 ? 172  ASP A OD1   1 
ATOM   1332 O OD2   . ASP A 1 172 ? 3.069   97.986  52.894 1.00 22.14 ? 172  ASP A OD2   1 
ATOM   1333 N N     . HIS A 1 173 ? -0.532  99.284  56.509 1.00 17.03 ? 173  HIS A N     1 
ATOM   1334 C CA    . HIS A 1 173 ? -0.974  98.854  57.872 1.00 17.45 ? 173  HIS A CA    1 
ATOM   1335 C C     . HIS A 1 173 ? -0.322  97.518  58.234 1.00 16.99 ? 173  HIS A C     1 
ATOM   1336 O O     . HIS A 1 173 ? 0.248   97.393  59.339 1.00 17.88 ? 173  HIS A O     1 
ATOM   1337 C CB    . HIS A 1 173 ? -2.490  98.858  57.954 1.00 18.85 ? 173  HIS A CB    1 
ATOM   1338 C CG    . HIS A 1 173 ? -3.080  100.231 57.835 1.00 18.65 ? 173  HIS A CG    1 
ATOM   1339 N ND1   . HIS A 1 173 ? -4.432  100.442 57.633 1.00 19.29 ? 173  HIS A ND1   1 
ATOM   1340 C CD2   . HIS A 1 173 ? -2.506  101.447 57.891 1.00 19.57 ? 173  HIS A CD2   1 
ATOM   1341 C CE1   . HIS A 1 173 ? -4.672  101.727 57.591 1.00 19.76 ? 173  HIS A CE1   1 
ATOM   1342 N NE2   . HIS A 1 173 ? -3.498  102.383 57.740 1.00 19.96 ? 173  HIS A NE2   1 
ATOM   1343 N N     . PHE A 1 174 ? -0.379  96.529  57.349 1.00 16.96 ? 174  PHE A N     1 
ATOM   1344 C CA    . PHE A 1 174 ? 0.228   95.228  57.675 1.00 17.32 ? 174  PHE A CA    1 
ATOM   1345 C C     . PHE A 1 174 ? 1.739   95.381  57.872 1.00 18.56 ? 174  PHE A C     1 
ATOM   1346 O O     . PHE A 1 174 ? 2.275   94.637  58.735 1.00 17.29 ? 174  PHE A O     1 
ATOM   1347 C CB    . PHE A 1 174 ? -0.154  94.111  56.724 1.00 18.71 ? 174  PHE A CB    1 
ATOM   1348 C CG    . PHE A 1 174 ? 0.181   92.770  57.343 1.00 18.05 ? 174  PHE A CG    1 
ATOM   1349 C CD1   . PHE A 1 174 ? -0.508  92.298  58.437 1.00 18.62 ? 174  PHE A CD1   1 
ATOM   1350 C CD2   . PHE A 1 174 ? 1.265   92.044  56.910 1.00 17.40 ? 174  PHE A CD2   1 
ATOM   1351 C CE1   . PHE A 1 174 ? -0.132  91.133  59.077 1.00 18.29 ? 174  PHE A CE1   1 
ATOM   1352 C CE2   . PHE A 1 174 ? 1.626   90.860  57.525 1.00 18.22 ? 174  PHE A CE2   1 
ATOM   1353 C CZ    . PHE A 1 174 ? 0.907   90.376  58.580 1.00 18.40 ? 174  PHE A CZ    1 
ATOM   1354 N N     . ALA A 1 175 ? 2.418   96.259  57.134 1.00 16.99 ? 175  ALA A N     1 
ATOM   1355 C CA    . ALA A 1 175 ? 3.875   96.376  57.295 1.00 18.29 ? 175  ALA A CA    1 
ATOM   1356 C C     . ALA A 1 175 ? 4.200   96.850  58.728 1.00 17.26 ? 175  ALA A C     1 
ATOM   1357 O O     . ALA A 1 175 ? 5.283   96.527  59.238 1.00 18.93 ? 175  ALA A O     1 
ATOM   1358 C CB    . ALA A 1 175 ? 4.489   97.292  56.254 1.00 18.01 ? 175  ALA A CB    1 
ATOM   1359 N N     . MET A 1 176 ? 3.339   97.630  59.352 1.00 16.13 ? 176  MET A N     1 
ATOM   1360 C CA    . MET A 1 176 ? 3.597   98.162  60.712 1.00 17.31 ? 176  MET A CA    1 
ATOM   1361 C C     . MET A 1 176 ? 3.182   97.165  61.816 1.00 18.00 ? 176  MET A C     1 
ATOM   1362 O O     . MET A 1 176 ? 3.473   97.468  62.999 1.00 17.52 ? 176  MET A O     1 
ATOM   1363 C CB    . MET A 1 176 ? 2.843   99.477  60.879 1.00 17.38 ? 176  MET A CB    1 
ATOM   1364 C CG    . MET A 1 176 ? 3.165   100.481 59.792 1.00 20.45 ? 176  MET A CG    1 
ATOM   1365 S SD    . MET A 1 176 ? 4.923   100.958 59.843 1.00 25.21 ? 176  MET A SD    1 
ATOM   1366 C CE    . MET A 1 176 ? 5.440   100.138 58.363 1.00 28.23 ? 176  MET A CE    1 
ATOM   1367 N N     . GLN A 1 177 ? 2.654   95.985  61.463 1.00 18.82 ? 177  GLN A N     1 
ATOM   1368 C CA    . GLN A 1 177 ? 2.289   94.910  62.421 1.00 17.79 ? 177  GLN A CA    1 
ATOM   1369 C C     . GLN A 1 177 ? 3.534   94.319  63.081 1.00 17.13 ? 177  GLN A C     1 
ATOM   1370 O O     . GLN A 1 177 ? 4.609   94.159  62.450 1.00 17.30 ? 177  GLN A O     1 
ATOM   1371 C CB    . GLN A 1 177 ? 1.425   93.851  61.738 1.00 17.65 ? 177  GLN A CB    1 
ATOM   1372 C CG    . GLN A 1 177 ? 1.039   92.697  62.665 1.00 17.74 ? 177  GLN A CG    1 
ATOM   1373 C CD    . GLN A 1 177 ? 2.029   91.550  62.595 1.00 20.11 ? 177  GLN A CD    1 
ATOM   1374 O OE1   . GLN A 1 177 ? 2.708   91.339  61.588 1.00 19.22 ? 177  GLN A OE1   1 
ATOM   1375 N NE2   . GLN A 1 177 ? 2.074   90.752  63.642 1.00 18.79 ? 177  GLN A NE2   1 
ATOM   1376 N N     . CYS A 1 178 ? 3.480   94.084  64.386 1.00 15.89 ? 178  CYS A N     1 
ATOM   1377 C CA    . CYS A 1 178 ? 4.596   93.443  65.078 1.00 15.12 ? 178  CYS A CA    1 
ATOM   1378 C C     . CYS A 1 178 ? 4.044   92.578  66.213 1.00 16.88 ? 178  CYS A C     1 
ATOM   1379 O O     . CYS A 1 178 ? 3.586   93.163  67.231 1.00 17.54 ? 178  CYS A O     1 
ATOM   1380 C CB    . CYS A 1 178 ? 5.550   94.508  65.620 1.00 15.83 ? 178  CYS A CB    1 
ATOM   1381 S SG    . CYS A 1 178 ? 7.070   93.826  66.322 1.00 18.52 ? 178  CYS A SG    1 
ATOM   1382 N N     . GLY A 1 179 ? 4.134   91.261  66.078 1.00 17.61 ? 179  GLY A N     1 
ATOM   1383 C CA    . GLY A 1 179 ? 3.607   90.307  67.083 1.00 16.80 ? 179  GLY A CA    1 
ATOM   1384 C C     . GLY A 1 179 ? 2.103   90.070  66.892 1.00 16.24 ? 179  GLY A C     1 
ATOM   1385 O O     . GLY A 1 179 ? 1.312   91.043  66.679 1.00 16.93 ? 179  GLY A O     1 
ATOM   1386 N N     . MET A 1 180 ? 1.663   88.815  66.934 1.00 18.09 ? 180  MET A N     1 
ATOM   1387 C CA    . MET A 1 180 ? 0.211   88.536  66.953 1.00 16.43 ? 180  MET A CA    1 
ATOM   1388 C C     . MET A 1 180 ? -0.041  87.279  67.775 1.00 16.19 ? 180  MET A C     1 
ATOM   1389 O O     . MET A 1 180 ? 0.871   86.431  67.945 1.00 17.74 ? 180  MET A O     1 
ATOM   1390 C CB    . MET A 1 180 ? -0.389  88.407  65.555 1.00 18.22 ? 180  MET A CB    1 
ATOM   1391 C CG    . MET A 1 180 ? 0.269   87.390  64.695 1.00 19.34 ? 180  MET A CG    1 
ATOM   1392 S SD    . MET A 1 180 ? -0.644  87.066  63.161 1.00 18.73 ? 180  MET A SD    1 
ATOM   1393 C CE    . MET A 1 180 ? -0.499  88.641  62.318 1.00 20.46 ? 180  MET A CE    1 
ATOM   1394 N N     . GLU A 1 181 ? -1.249  87.168  68.297 1.00 16.75 ? 181  GLU A N     1 
ATOM   1395 C CA    . GLU A 1 181 ? -1.765  85.923  68.916 1.00 17.40 ? 181  GLU A CA    1 
ATOM   1396 C C     . GLU A 1 181 ? -2.797  85.360  67.956 1.00 16.11 ? 181  GLU A C     1 
ATOM   1397 O O     . GLU A 1 181 ? -3.633  86.138  67.428 1.00 17.95 ? 181  GLU A O     1 
ATOM   1398 C CB    . GLU A 1 181 ? -2.359  86.201  70.292 1.00 18.61 ? 181  GLU A CB    1 
ATOM   1399 C CG    . GLU A 1 181 ? -2.935  84.939  70.939 1.00 18.48 ? 181  GLU A CG    1 
ATOM   1400 C CD    . GLU A 1 181 ? -3.596  85.317  72.264 1.00 19.85 ? 181  GLU A CD    1 
ATOM   1401 O OE1   . GLU A 1 181 ? -2.876  85.404  73.254 1.00 20.92 ? 181  GLU A OE1   1 
ATOM   1402 O OE2   . GLU A 1 181 ? -4.776  85.708  72.239 1.00 21.77 ? 181  GLU A OE2   1 
ATOM   1403 N N     . VAL A 1 182 ? -2.694  84.074  67.679 1.00 16.96 ? 182  VAL A N     1 
ATOM   1404 C CA    . VAL A 1 182 ? -3.553  83.374  66.697 1.00 16.53 ? 182  VAL A CA    1 
ATOM   1405 C C     . VAL A 1 182 ? -4.143  82.133  67.346 1.00 16.17 ? 182  VAL A C     1 
ATOM   1406 O O     . VAL A 1 182 ? -3.410  81.291  67.918 1.00 17.54 ? 182  VAL A O     1 
ATOM   1407 C CB    . VAL A 1 182 ? -2.757  83.005  65.433 1.00 17.83 ? 182  VAL A CB    1 
ATOM   1408 C CG1   . VAL A 1 182 ? -3.698  82.483  64.379 1.00 18.58 ? 182  VAL A CG1   1 
ATOM   1409 C CG2   . VAL A 1 182 ? -1.929  84.202  64.926 1.00 18.47 ? 182  VAL A CG2   1 
ATOM   1410 N N     . VAL A 1 183 ? -5.433  81.984  67.166 1.00 18.50 ? 183  VAL A N     1 
ATOM   1411 C CA    . VAL A 1 183 ? -6.128  80.702  67.387 1.00 18.10 ? 183  VAL A CA    1 
ATOM   1412 C C     . VAL A 1 183 ? -6.093  79.947  66.070 1.00 17.88 ? 183  VAL A C     1 
ATOM   1413 O O     . VAL A 1 183 ? -6.718  80.381  65.112 1.00 19.12 ? 183  VAL A O     1 
ATOM   1414 C CB    . VAL A 1 183 ? -7.533  80.913  67.952 1.00 17.71 ? 183  VAL A CB    1 
ATOM   1415 C CG1   . VAL A 1 183 ? -8.210  79.558  68.073 1.00 20.14 ? 183  VAL A CG1   1 
ATOM   1416 C CG2   . VAL A 1 183 ? -7.492  81.647  69.314 1.00 20.14 ? 183  VAL A CG2   1 
ATOM   1417 N N     . LEU A 1 184 ? -5.345  78.848  66.033 1.00 18.10 ? 184  LEU A N     1 
ATOM   1418 C CA    . LEU A 1 184 ? -5.221  77.989  64.855 1.00 17.89 ? 184  LEU A CA    1 
ATOM   1419 C C     . LEU A 1 184 ? -6.533  77.247  64.658 1.00 19.69 ? 184  LEU A C     1 
ATOM   1420 O O     . LEU A 1 184 ? -7.387  77.176  65.542 1.00 17.59 ? 184  LEU A O     1 
ATOM   1421 C CB    . LEU A 1 184 ? -4.052  77.024  65.042 1.00 20.01 ? 184  LEU A CB    1 
ATOM   1422 C CG    . LEU A 1 184 ? -2.695  77.687  65.239 1.00 21.24 ? 184  LEU A CG    1 
ATOM   1423 C CD1   . LEU A 1 184 ? -1.642  76.630  65.542 1.00 20.59 ? 184  LEU A CD1   1 
ATOM   1424 C CD2   . LEU A 1 184 ? -2.321  78.511  64.005 1.00 21.65 ? 184  LEU A CD2   1 
ATOM   1425 N N     . PRO A 1 185 ? -6.723  76.654  63.471 1.00 19.10 ? 185  PRO A N     1 
ATOM   1426 C CA    . PRO A 1 185 ? -7.993  76.032  63.135 1.00 21.04 ? 185  PRO A CA    1 
ATOM   1427 C C     . PRO A 1 185 ? -8.300  74.793  63.990 1.00 21.44 ? 185  PRO A C     1 
ATOM   1428 O O     . PRO A 1 185 ? -9.443  74.361  63.953 1.00 22.41 ? 185  PRO A O     1 
ATOM   1429 C CB    . PRO A 1 185 ? -7.835  75.699  61.637 1.00 20.67 ? 185  PRO A CB    1 
ATOM   1430 C CG    . PRO A 1 185 ? -6.735  76.614  61.162 1.00 19.34 ? 185  PRO A CG    1 
ATOM   1431 C CD    . PRO A 1 185 ? -5.780  76.692  62.339 1.00 22.15 ? 185  PRO A CD    1 
ATOM   1432 N N     . ASN A 1 186 ? -7.328  74.270  64.737 1.00 20.54 ? 186  ASN A N     1 
ATOM   1433 C CA    . ASN A 1 186 ? -7.555  73.138  65.667 1.00 21.51 ? 186  ASN A CA    1 
ATOM   1434 C C     . ASN A 1 186 ? -7.965  73.693  67.043 1.00 22.02 ? 186  ASN A C     1 
ATOM   1435 O O     . ASN A 1 186 ? -8.208  72.887  67.949 1.00 22.07 ? 186  ASN A O     1 
ATOM   1436 C CB    . ASN A 1 186 ? -6.331  72.209  65.702 1.00 22.41 ? 186  ASN A CB    1 
ATOM   1437 C CG    . ASN A 1 186 ? -5.109  72.901  66.290 1.00 21.37 ? 186  ASN A CG    1 
ATOM   1438 O OD1   . ASN A 1 186 ? -5.151  74.092  66.580 1.00 20.52 ? 186  ASN A OD1   1 
ATOM   1439 N ND2   . ASN A 1 186 ? -4.008  72.190  66.443 1.00 23.37 ? 186  ASN A ND2   1 
ATOM   1440 N N     . GLY A 1 187 ? -7.999  75.021  67.235 1.00 19.14 ? 187  GLY A N     1 
ATOM   1441 C CA    . GLY A 1 187 ? -8.399  75.658  68.495 1.00 20.27 ? 187  GLY A CA    1 
ATOM   1442 C C     . GLY A 1 187 ? -7.211  75.918  69.440 1.00 20.25 ? 187  GLY A C     1 
ATOM   1443 O O     . GLY A 1 187 ? -7.433  76.420  70.545 1.00 20.46 ? 187  GLY A O     1 
ATOM   1444 N N     . GLU A 1 188 ? -5.989  75.533  69.081 1.00 19.53 ? 188  GLU A N     1 
ATOM   1445 C CA    . GLU A 1 188 ? -4.772  75.784  69.895 1.00 19.51 ? 188  GLU A CA    1 
ATOM   1446 C C     . GLU A 1 188 ? -4.362  77.236  69.655 1.00 20.96 ? 188  GLU A C     1 
ATOM   1447 O O     . GLU A 1 188 ? -4.574  77.741  68.526 1.00 20.27 ? 188  GLU A O     1 
ATOM   1448 C CB    . GLU A 1 188 ? -3.658  74.792  69.524 1.00 20.67 ? 188  GLU A CB    1 
ATOM   1449 C CG    . GLU A 1 188 ? -4.014  73.344  69.807 1.00 23.00 ? 188  GLU A CG    1 
ATOM   1450 C CD    . GLU A 1 188 ? -4.249  73.203  71.292 1.00 25.13 ? 188  GLU A CD    1 
ATOM   1451 O OE1   . GLU A 1 188 ? -3.323  73.557  72.004 1.00 28.21 ? 188  GLU A OE1   1 
ATOM   1452 O OE2   . GLU A 1 188 ? -5.386  72.935  71.707 1.00 29.12 ? 188  GLU A OE2   1 
ATOM   1453 N N     . VAL A 1 189 ? -3.756  77.871  70.648 1.00 19.58 ? 189  VAL A N     1 
ATOM   1454 C CA    . VAL A 1 189 ? -3.337  79.291  70.564 1.00 20.03 ? 189  VAL A CA    1 
ATOM   1455 C C     . VAL A 1 189 ? -1.807  79.375  70.493 1.00 18.25 ? 189  VAL A C     1 
ATOM   1456 O O     . VAL A 1 189 ? -1.085  78.681  71.232 1.00 17.16 ? 189  VAL A O     1 
ATOM   1457 C CB    . VAL A 1 189 ? -3.975  80.146  71.688 1.00 20.01 ? 189  VAL A CB    1 
ATOM   1458 C CG1   . VAL A 1 189 ? -3.610  79.691  73.064 1.00 22.77 ? 189  VAL A CG1   1 
ATOM   1459 C CG2   . VAL A 1 189 ? -3.633  81.624  71.520 1.00 21.30 ? 189  VAL A CG2   1 
ATOM   1460 N N     . VAL A 1 190 ? -1.313  80.253  69.618 1.00 17.67 ? 190  VAL A N     1 
ATOM   1461 C CA    . VAL A 1 190 ? 0.132   80.536  69.463 1.00 17.80 ? 190  VAL A CA    1 
ATOM   1462 C C     . VAL A 1 190 ? 0.353   82.049  69.476 1.00 17.75 ? 190  VAL A C     1 
ATOM   1463 O O     . VAL A 1 190 ? -0.575  82.842  69.148 1.00 19.18 ? 190  VAL A O     1 
ATOM   1464 C CB    . VAL A 1 190 ? 0.688   79.978  68.135 1.00 20.63 ? 190  VAL A CB    1 
ATOM   1465 C CG1   . VAL A 1 190 ? 0.560   78.479  68.061 1.00 22.68 ? 190  VAL A CG1   1 
ATOM   1466 C CG2   . VAL A 1 190 ? 0.044   80.647  66.934 1.00 22.13 ? 190  VAL A CG2   1 
ATOM   1467 N N     . ARG A 1 191 ? 1.538   82.446  69.900 1.00 17.24 ? 191  ARG A N     1 
ATOM   1468 C CA    . ARG A 1 191 ? 2.003   83.842  69.773 1.00 17.17 ? 191  ARG A CA    1 
ATOM   1469 C C     . ARG A 1 191 ? 3.250   83.835  68.873 1.00 17.16 ? 191  ARG A C     1 
ATOM   1470 O O     . ARG A 1 191 ? 4.142   82.997  69.077 1.00 16.53 ? 191  ARG A O     1 
ATOM   1471 C CB    . ARG A 1 191 ? 2.251   84.372  71.173 1.00 17.48 ? 191  ARG A CB    1 
ATOM   1472 C CG    . ARG A 1 191 ? 0.955   84.703  71.907 1.00 17.14 ? 191  ARG A CG    1 
ATOM   1473 C CD    . ARG A 1 191 ? 1.231   85.127  73.333 1.00 18.70 ? 191  ARG A CD    1 
ATOM   1474 N NE    . ARG A 1 191 ? -0.040  85.410  73.950 1.00 18.77 ? 191  ARG A NE    1 
ATOM   1475 C CZ    . ARG A 1 191 ? -0.251  85.631  75.240 1.00 21.45 ? 191  ARG A CZ    1 
ATOM   1476 N NH1   . ARG A 1 191 ? 0.732   85.735  76.096 1.00 22.08 ? 191  ARG A NH1   1 
ATOM   1477 N NH2   . ARG A 1 191 ? -1.482  85.744  75.685 1.00 22.80 ? 191  ARG A NH2   1 
ATOM   1478 N N     . THR A 1 192 ? 3.304   84.763  67.922 1.00 16.04 ? 192  THR A N     1 
ATOM   1479 C CA    . THR A 1 192 ? 4.409   84.844  66.950 1.00 16.22 ? 192  THR A CA    1 
ATOM   1480 C C     . THR A 1 192 ? 5.524   85.706  67.540 1.00 17.30 ? 192  THR A C     1 
ATOM   1481 O O     . THR A 1 192 ? 5.297   86.474  68.502 1.00 16.69 ? 192  THR A O     1 
ATOM   1482 C CB    . THR A 1 192 ? 3.927   85.460  65.632 1.00 15.51 ? 192  THR A CB    1 
ATOM   1483 O OG1   . THR A 1 192 ? 3.487   86.789  65.905 1.00 16.18 ? 192  THR A OG1   1 
ATOM   1484 C CG2   . THR A 1 192 ? 2.801   84.671  65.003 1.00 16.71 ? 192  THR A CG2   1 
ATOM   1485 N N     . GLY A 1 193 ? 6.694   85.618  66.937 1.00 19.44 ? 193  GLY A N     1 
ATOM   1486 C CA    . GLY A 1 193 ? 7.799   86.556  67.196 1.00 19.10 ? 193  GLY A CA    1 
ATOM   1487 C C     . GLY A 1 193 ? 8.297   86.339  68.604 1.00 17.76 ? 193  GLY A C     1 
ATOM   1488 O O     . GLY A 1 193 ? 8.342   85.177  69.060 1.00 17.16 ? 193  GLY A O     1 
ATOM   1489 N N     . MET A 1 194 ? 8.583   87.432  69.302 1.00 18.18 ? 194  MET A N     1 
ATOM   1490 C CA    . MET A 1 194 ? 9.134   87.340  70.654 1.00 17.70 ? 194  MET A CA    1 
ATOM   1491 C C     . MET A 1 194 ? 8.024   86.947  71.655 1.00 18.25 ? 194  MET A C     1 
ATOM   1492 O O     . MET A 1 194 ? 8.380   86.601  72.799 1.00 17.91 ? 194  MET A O     1 
ATOM   1493 C CB    . MET A 1 194 ? 9.789   88.664  71.021 1.00 17.80 ? 194  MET A CB    1 
ATOM   1494 C CG    . MET A 1 194 ? 10.988  89.004  70.110 1.00 17.93 ? 194  MET A CG    1 
ATOM   1495 S SD    . MET A 1 194 ? 12.214  87.753  70.015 1.00 20.10 ? 194  MET A SD    1 
ATOM   1496 C CE    . MET A 1 194 ? 12.783  87.640  71.715 1.00 19.30 ? 194  MET A CE    1 
ATOM   1497 N N     . GLY A 1 195 ? 6.759   86.938  71.223 1.00 19.41 ? 195  GLY A N     1 
ATOM   1498 C CA    . GLY A 1 195 ? 5.618   86.485  72.030 1.00 18.89 ? 195  GLY A CA    1 
ATOM   1499 C C     . GLY A 1 195 ? 5.754   85.028  72.431 1.00 18.47 ? 195  GLY A C     1 
ATOM   1500 O O     . GLY A 1 195 ? 5.142   84.646  73.449 1.00 18.79 ? 195  GLY A O     1 
ATOM   1501 N N     . ALA A 1 196 ? 6.507   84.227  71.663 1.00 16.67 ? 196  ALA A N     1 
ATOM   1502 C CA    . ALA A 1 196 ? 6.740   82.795  71.938 1.00 16.48 ? 196  ALA A CA    1 
ATOM   1503 C C     . ALA A 1 196 ? 7.712   82.624  73.103 1.00 17.04 ? 196  ALA A C     1 
ATOM   1504 O O     . ALA A 1 196 ? 7.823   81.526  73.610 1.00 19.10 ? 196  ALA A O     1 
ATOM   1505 C CB    . ALA A 1 196 ? 7.169   82.118  70.683 1.00 16.66 ? 196  ALA A CB    1 
ATOM   1506 N N     . MET A 1 197 ? 8.437   83.676  73.503 1.00 19.11 ? 197  MET A N     1 
ATOM   1507 C CA    . MET A 1 197 ? 9.416   83.679  74.623 1.00 18.48 ? 197  MET A CA    1 
ATOM   1508 C C     . MET A 1 197 ? 8.656   84.023  75.906 1.00 18.22 ? 197  MET A C     1 
ATOM   1509 O O     . MET A 1 197 ? 8.205   85.131  76.085 1.00 18.67 ? 197  MET A O     1 
ATOM   1510 C CB    . MET A 1 197 ? 10.547  84.681  74.357 1.00 19.09 ? 197  MET A CB    1 
ATOM   1511 C CG    . MET A 1 197 ? 11.461  85.062  75.537 1.00 22.12 ? 197  MET A CG    1 
ATOM   1512 S SD    . MET A 1 197 ? 12.355  83.721  76.252 1.00 26.18 ? 197  MET A SD    1 
ATOM   1513 C CE    . MET A 1 197 ? 13.328  83.139  74.857 1.00 23.67 ? 197  MET A CE    1 
ATOM   1514 N N     . PRO A 1 198 ? 8.503   83.070  76.850 1.00 18.88 ? 198  PRO A N     1 
ATOM   1515 C CA    . PRO A 1 198 ? 7.872   83.381  78.141 1.00 20.77 ? 198  PRO A CA    1 
ATOM   1516 C C     . PRO A 1 198 ? 8.628   84.487  78.869 1.00 19.78 ? 198  PRO A C     1 
ATOM   1517 O O     . PRO A 1 198 ? 9.847   84.463  78.859 1.00 20.96 ? 198  PRO A O     1 
ATOM   1518 C CB    . PRO A 1 198 ? 7.956   82.090  78.960 1.00 24.04 ? 198  PRO A CB    1 
ATOM   1519 C CG    . PRO A 1 198 ? 8.315   81.019  77.935 1.00 25.75 ? 198  PRO A CG    1 
ATOM   1520 C CD    . PRO A 1 198 ? 9.022   81.705  76.761 1.00 20.61 ? 198  PRO A CD    1 
ATOM   1521 N N     . GLY A 1 199 ? 7.906   85.490  79.336 1.00 21.17 ? 199  GLY A N     1 
ATOM   1522 C CA    . GLY A 1 199 ? 8.510   86.579  80.116 1.00 24.28 ? 199  GLY A CA    1 
ATOM   1523 C C     . GLY A 1 199 ? 9.243   87.588  79.229 1.00 23.67 ? 199  GLY A C     1 
ATOM   1524 O O     . GLY A 1 199 ? 10.006  88.357  79.763 1.00 21.74 ? 199  GLY A O     1 
ATOM   1525 N N     . ASN A 1 200 ? 9.014   87.586  77.912 1.00 20.81 ? 200  ASN A N     1 
ATOM   1526 C CA    . ASN A 1 200 ? 9.628   88.565  76.982 1.00 21.05 ? 200  ASN A CA    1 
ATOM   1527 C C     . ASN A 1 200 ? 9.147   89.971  77.306 1.00 22.02 ? 200  ASN A C     1 
ATOM   1528 O O     . ASN A 1 200 ? 7.997   90.179  77.868 1.00 19.59 ? 200  ASN A O     1 
ATOM   1529 C CB    . ASN A 1 200 ? 9.304   88.262  75.517 1.00 20.63 ? 200  ASN A CB    1 
ATOM   1530 C CG    . ASN A 1 200 ? 7.898   88.652  75.173 1.00 19.51 ? 200  ASN A CG    1 
ATOM   1531 O OD1   . ASN A 1 200 ? 7.649   89.778  74.786 1.00 20.51 ? 200  ASN A OD1   1 
ATOM   1532 N ND2   . ASN A 1 200 ? 6.960   87.727  75.325 1.00 20.40 ? 200  ASN A ND2   1 
ATOM   1533 N N     . ASN A 1 201 ? 9.953   90.947  76.864 1.00 21.96 ? 201  ASN A N     1 
ATOM   1534 C CA    . ASN A 1 201 ? 9.542   92.365  76.848 1.00 22.47 ? 201  ASN A CA    1 
ATOM   1535 C C     . ASN A 1 201 ? 9.763   92.920  75.445 1.00 22.27 ? 201  ASN A C     1 
ATOM   1536 O O     . ASN A 1 201 ? 10.080  94.117  75.357 1.00 23.93 ? 201  ASN A O     1 
ATOM   1537 C CB    . ASN A 1 201 ? 10.307  93.206  77.894 1.00 21.56 ? 201  ASN A CB    1 
ATOM   1538 C CG    . ASN A 1 201 ? 11.834  93.052  77.877 1.00 25.76 ? 201  ASN A CG    1 
ATOM   1539 O OD1   . ASN A 1 201 ? 12.449  92.368  77.027 1.00 22.48 ? 201  ASN A OD1   1 
ATOM   1540 N ND2   . ASN A 1 201 ? 12.488  93.701  78.845 1.00 26.18 ? 201  ASN A ND2   1 
ATOM   1541 N N     . THR A 1 202 ? 9.607   92.095  74.402 1.00 20.26 ? 202  THR A N     1 
ATOM   1542 C CA    . THR A 1 202 ? 9.991   92.483  73.020 1.00 19.53 ? 202  THR A CA    1 
ATOM   1543 C C     . THR A 1 202 ? 8.928   92.098  71.983 1.00 18.96 ? 202  THR A C     1 
ATOM   1544 O O     . THR A 1 202 ? 9.171   92.354  70.803 1.00 17.17 ? 202  THR A O     1 
ATOM   1545 C CB    . THR A 1 202 ? 11.356  91.858  72.693 1.00 21.94 ? 202  THR A CB    1 
ATOM   1546 O OG1   . THR A 1 202 ? 11.350  90.506  73.132 1.00 21.15 ? 202  THR A OG1   1 
ATOM   1547 C CG2   . THR A 1 202 ? 12.509  92.605  73.338 1.00 22.95 ? 202  THR A CG2   1 
ATOM   1548 N N     . TRP A 1 203 ? 7.763   91.583  72.382 1.00 18.13 ? 203  TRP A N     1 
ATOM   1549 C CA    . TRP A 1 203 ? 6.716   91.170  71.413 1.00 18.57 ? 203  TRP A CA    1 
ATOM   1550 C C     . TRP A 1 203 ? 6.450   92.263  70.392 1.00 18.88 ? 203  TRP A C     1 
ATOM   1551 O O     . TRP A 1 203 ? 6.295   91.925  69.225 1.00 19.05 ? 203  TRP A O     1 
ATOM   1552 C CB    . TRP A 1 203 ? 5.432   90.765  72.141 1.00 18.80 ? 203  TRP A CB    1 
ATOM   1553 C CG    . TRP A 1 203 ? 4.511   89.887  71.366 1.00 17.82 ? 203  TRP A CG    1 
ATOM   1554 C CD1   . TRP A 1 203 ? 4.765   89.175  70.215 1.00 17.14 ? 203  TRP A CD1   1 
ATOM   1555 C CD2   . TRP A 1 203 ? 3.160   89.596  71.754 1.00 16.75 ? 203  TRP A CD2   1 
ATOM   1556 N NE1   . TRP A 1 203 ? 3.669   88.424  69.882 1.00 17.03 ? 203  TRP A NE1   1 
ATOM   1557 C CE2   . TRP A 1 203 ? 2.665   88.665  70.814 1.00 17.56 ? 203  TRP A CE2   1 
ATOM   1558 C CE3   . TRP A 1 203 ? 2.343   90.010  72.832 1.00 19.20 ? 203  TRP A CE3   1 
ATOM   1559 C CZ2   . TRP A 1 203 ? 1.370   88.151  70.911 1.00 17.12 ? 203  TRP A CZ2   1 
ATOM   1560 C CZ3   . TRP A 1 203 ? 1.079   89.462  72.945 1.00 18.90 ? 203  TRP A CZ3   1 
ATOM   1561 C CH2   . TRP A 1 203 ? 0.586   88.589  71.963 1.00 17.54 ? 203  TRP A CH2   1 
ATOM   1562 N N     . GLN A 1 204 ? 6.259   93.515  70.831 1.00 16.13 ? 204  GLN A N     1 
ATOM   1563 C CA    . GLN A 1 204 ? 5.926   94.625  69.925 1.00 17.29 ? 204  GLN A CA    1 
ATOM   1564 C C     . GLN A 1 204 ? 7.213   95.385  69.487 1.00 16.12 ? 204  GLN A C     1 
ATOM   1565 O O     . GLN A 1 204 ? 7.084   96.458  68.919 1.00 16.76 ? 204  GLN A O     1 
ATOM   1566 C CB    . GLN A 1 204 ? 4.905   95.547  70.624 1.00 16.70 ? 204  GLN A CB    1 
ATOM   1567 C CG    . GLN A 1 204 ? 3.482   95.124  70.366 1.00 17.84 ? 204  GLN A CG    1 
ATOM   1568 C CD    . GLN A 1 204 ? 3.155   93.780  70.965 1.00 20.57 ? 204  GLN A CD    1 
ATOM   1569 O OE1   . GLN A 1 204 ? 3.096   93.635  72.182 1.00 20.97 ? 204  GLN A OE1   1 
ATOM   1570 N NE2   . GLN A 1 204 ? 3.038   92.756  70.118 1.00 17.77 ? 204  GLN A NE2   1 
ATOM   1571 N N     . LEU A 1 205 ? 8.414   94.870  69.744 1.00 17.77 ? 205  LEU A N     1 
ATOM   1572 C CA    . LEU A 1 205 ? 9.666   95.607  69.415 1.00 17.54 ? 205  LEU A CA    1 
ATOM   1573 C C     . LEU A 1 205 ? 10.442  94.928  68.261 1.00 19.20 ? 205  LEU A C     1 
ATOM   1574 O O     . LEU A 1 205 ? 11.161  95.622  67.552 1.00 18.65 ? 205  LEU A O     1 
ATOM   1575 C CB    . LEU A 1 205 ? 10.509  95.674  70.684 1.00 19.18 ? 205  LEU A CB    1 
ATOM   1576 C CG    . LEU A 1 205 ? 9.866   96.397  71.878 1.00 19.04 ? 205  LEU A CG    1 
ATOM   1577 C CD1   . LEU A 1 205 ? 10.889  96.599  72.973 1.00 20.18 ? 205  LEU A CD1   1 
ATOM   1578 C CD2   . LEU A 1 205 ? 9.286   97.741  71.440 1.00 19.08 ? 205  LEU A CD2   1 
ATOM   1579 N N     . PHE A 1 206 ? 10.389  93.610  68.136 1.00 18.94 ? 206  PHE A N     1 
ATOM   1580 C CA    . PHE A 1 206 ? 11.135  92.851  67.098 1.00 17.02 ? 206  PHE A CA    1 
ATOM   1581 C C     . PHE A 1 206 ? 10.179  91.912  66.400 1.00 16.13 ? 206  PHE A C     1 
ATOM   1582 O O     . PHE A 1 206 ? 9.668   90.985  67.055 1.00 16.52 ? 206  PHE A O     1 
ATOM   1583 C CB    . PHE A 1 206 ? 12.299  92.115  67.737 1.00 17.95 ? 206  PHE A CB    1 
ATOM   1584 C CG    . PHE A 1 206 ? 13.112  91.310  66.753 1.00 19.02 ? 206  PHE A CG    1 
ATOM   1585 C CD1   . PHE A 1 206 ? 13.548  91.872  65.568 1.00 19.42 ? 206  PHE A CD1   1 
ATOM   1586 C CD2   . PHE A 1 206 ? 13.382  89.984  67.000 1.00 19.21 ? 206  PHE A CD2   1 
ATOM   1587 C CE1   . PHE A 1 206 ? 14.278  91.098  64.669 1.00 20.77 ? 206  PHE A CE1   1 
ATOM   1588 C CE2   . PHE A 1 206 ? 14.171  89.227  66.135 1.00 18.46 ? 206  PHE A CE2   1 
ATOM   1589 C CZ    . PHE A 1 206 ? 14.594  89.782  64.959 1.00 17.81 ? 206  PHE A CZ    1 
ATOM   1590 N N     . LYS A 1 207 ? 10.003  92.099  65.098 1.00 16.17 ? 207  LYS A N     1 
ATOM   1591 C CA    . LYS A 1 207 ? 9.016   91.309  64.316 1.00 17.47 ? 207  LYS A CA    1 
ATOM   1592 C C     . LYS A 1 207 ? 9.320   89.801  64.345 1.00 17.53 ? 207  LYS A C     1 
ATOM   1593 O O     . LYS A 1 207 ? 8.364   88.990  64.512 1.00 16.70 ? 207  LYS A O     1 
ATOM   1594 C CB    . LYS A 1 207 ? 8.965   91.809  62.883 1.00 18.70 ? 207  LYS A CB    1 
ATOM   1595 C CG    . LYS A 1 207 ? 8.250   93.134  62.708 1.00 19.62 ? 207  LYS A CG    1 
ATOM   1596 C CD    . LYS A 1 207 ? 8.554   93.730  61.333 1.00 20.20 ? 207  LYS A CD    1 
ATOM   1597 C CE    . LYS A 1 207 ? 7.569   94.750  60.814 1.00 21.99 ? 207  LYS A CE    1 
ATOM   1598 N NZ    . LYS A 1 207 ? 6.277   94.142  60.410 1.00 22.78 ? 207  LYS A NZ    1 
ATOM   1599 N N     . TYR A 1 208 ? 10.562  89.397  64.071 1.00 17.79 ? 208  TYR A N     1 
ATOM   1600 C CA    . TYR A 1 208 ? 10.779  88.019  63.578 1.00 16.85 ? 208  TYR A CA    1 
ATOM   1601 C C     . TYR A 1 208 ? 10.651  86.986  64.708 1.00 17.09 ? 208  TYR A C     1 
ATOM   1602 O O     . TYR A 1 208 ? 10.147  85.898  64.509 1.00 16.22 ? 208  TYR A O     1 
ATOM   1603 C CB    . TYR A 1 208 ? 12.131  87.865  62.869 1.00 17.16 ? 208  TYR A CB    1 
ATOM   1604 C CG    . TYR A 1 208 ? 12.330  88.777  61.679 1.00 17.24 ? 208  TYR A CG    1 
ATOM   1605 C CD1   . TYR A 1 208 ? 11.305  89.079  60.811 1.00 19.44 ? 208  TYR A CD1   1 
ATOM   1606 C CD2   . TYR A 1 208 ? 13.539  89.400  61.469 1.00 19.15 ? 208  TYR A CD2   1 
ATOM   1607 C CE1   . TYR A 1 208 ? 11.491  89.918  59.729 1.00 18.88 ? 208  TYR A CE1   1 
ATOM   1608 C CE2   . TYR A 1 208 ? 13.741  90.258  60.406 1.00 18.05 ? 208  TYR A CE2   1 
ATOM   1609 C CZ    . TYR A 1 208 ? 12.702  90.549  59.553 1.00 18.58 ? 208  TYR A CZ    1 
ATOM   1610 O OH    . TYR A 1 208 ? 12.899  91.394  58.498 1.00 16.39 ? 208  TYR A OH    1 
ATOM   1611 N N     . GLY A 1 209 ? 11.192  87.280  65.873 1.00 16.84 ? 209  GLY A N     1 
ATOM   1612 C CA    . GLY A 1 209 ? 11.538  86.217  66.815 1.00 17.97 ? 209  GLY A CA    1 
ATOM   1613 C C     . GLY A 1 209 ? 12.615  85.350  66.209 1.00 18.52 ? 209  GLY A C     1 
ATOM   1614 O O     . GLY A 1 209 ? 13.650  85.872  65.689 1.00 17.91 ? 209  GLY A O     1 
ATOM   1615 N N     . TYR A 1 210 ? 12.404  84.050  66.266 1.00 16.78 ? 210  TYR A N     1 
ATOM   1616 C CA    . TYR A 1 210 ? 13.373  83.061  65.755 1.00 16.50 ? 210  TYR A CA    1 
ATOM   1617 C C     . TYR A 1 210 ? 12.606  82.066  64.911 1.00 16.29 ? 210  TYR A C     1 
ATOM   1618 O O     . TYR A 1 210 ? 11.496  81.672  65.275 1.00 16.92 ? 210  TYR A O     1 
ATOM   1619 C CB    . TYR A 1 210 ? 14.059  82.381  66.934 1.00 16.99 ? 210  TYR A CB    1 
ATOM   1620 C CG    . TYR A 1 210 ? 14.897  81.161  66.613 1.00 16.87 ? 210  TYR A CG    1 
ATOM   1621 C CD1   . TYR A 1 210 ? 16.116  81.230  65.965 1.00 19.03 ? 210  TYR A CD1   1 
ATOM   1622 C CD2   . TYR A 1 210 ? 14.469  79.915  67.014 1.00 17.96 ? 210  TYR A CD2   1 
ATOM   1623 C CE1   . TYR A 1 210 ? 16.881  80.078  65.720 1.00 21.05 ? 210  TYR A CE1   1 
ATOM   1624 C CE2   . TYR A 1 210 ? 15.246  78.782  66.848 1.00 20.27 ? 210  TYR A CE2   1 
ATOM   1625 C CZ    . TYR A 1 210 ? 16.473  78.859  66.205 1.00 19.82 ? 210  TYR A CZ    1 
ATOM   1626 O OH    . TYR A 1 210 ? 17.219  77.701  66.066 1.00 23.85 ? 210  TYR A OH    1 
ATOM   1627 N N     . GLY A 1 211 ? 13.239  81.597  63.856 1.00 15.73 ? 211  GLY A N     1 
ATOM   1628 C CA    . GLY A 1 211 ? 12.585  80.592  63.009 1.00 18.42 ? 211  GLY A CA    1 
ATOM   1629 C C     . GLY A 1 211 ? 11.726  81.192  61.926 1.00 17.24 ? 211  GLY A C     1 
ATOM   1630 O O     . GLY A 1 211 ? 11.853  82.375  61.610 1.00 19.27 ? 211  GLY A O     1 
ATOM   1631 N N     . PRO A 1 212 ? 10.886  80.352  61.259 1.00 17.41 ? 212  PRO A N     1 
ATOM   1632 C CA    . PRO A 1 212 ? 10.084  80.826  60.142 1.00 16.41 ? 212  PRO A CA    1 
ATOM   1633 C C     . PRO A 1 212 ? 9.228   82.033  60.555 1.00 17.39 ? 212  PRO A C     1 
ATOM   1634 O O     . PRO A 1 212 ? 8.643   82.027  61.642 1.00 17.75 ? 212  PRO A O     1 
ATOM   1635 C CB    . PRO A 1 212 ? 9.250   79.598  59.754 1.00 18.13 ? 212  PRO A CB    1 
ATOM   1636 C CG    . PRO A 1 212 ? 10.081  78.423  60.202 1.00 17.75 ? 212  PRO A CG    1 
ATOM   1637 C CD    . PRO A 1 212 ? 10.759  78.900  61.474 1.00 17.46 ? 212  PRO A CD    1 
ATOM   1638 N N     . TYR A 1 213 ? 9.142   83.026  59.668 1.00 16.81 ? 213  TYR A N     1 
ATOM   1639 C CA    . TYR A 1 213 ? 8.398   84.283  59.919 1.00 16.84 ? 213  TYR A CA    1 
ATOM   1640 C C     . TYR A 1 213 ? 6.987   84.121  59.355 1.00 18.29 ? 213  TYR A C     1 
ATOM   1641 O O     . TYR A 1 213 ? 6.781   84.261  58.154 1.00 17.03 ? 213  TYR A O     1 
ATOM   1642 C CB    . TYR A 1 213 ? 9.183   85.496  59.401 1.00 18.02 ? 213  TYR A CB    1 
ATOM   1643 C CG    . TYR A 1 213 ? 8.512   86.837  59.552 1.00 17.70 ? 213  TYR A CG    1 
ATOM   1644 C CD1   . TYR A 1 213 ? 7.848   87.199  60.728 1.00 17.35 ? 213  TYR A CD1   1 
ATOM   1645 C CD2   . TYR A 1 213 ? 8.665   87.806  58.584 1.00 19.39 ? 213  TYR A CD2   1 
ATOM   1646 C CE1   . TYR A 1 213 ? 7.271   88.452  60.869 1.00 17.73 ? 213  TYR A CE1   1 
ATOM   1647 C CE2   . TYR A 1 213 ? 8.115   89.067  58.708 1.00 19.35 ? 213  TYR A CE2   1 
ATOM   1648 C CZ    . TYR A 1 213 ? 7.396   89.382  59.849 1.00 20.54 ? 213  TYR A CZ    1 
ATOM   1649 O OH    . TYR A 1 213 ? 6.879   90.633  59.947 1.00 23.34 ? 213  TYR A OH    1 
ATOM   1650 N N     . VAL A 1 214 ? 6.017   83.853  60.233 1.00 18.41 ? 214  VAL A N     1 
ATOM   1651 C CA    . VAL A 1 214 ? 4.692   83.338  59.788 1.00 18.44 ? 214  VAL A CA    1 
ATOM   1652 C C     . VAL A 1 214 ? 3.604   84.404  59.869 1.00 17.34 ? 214  VAL A C     1 
ATOM   1653 O O     . VAL A 1 214 ? 2.499   84.043  59.500 1.00 18.40 ? 214  VAL A O     1 
ATOM   1654 C CB    . VAL A 1 214 ? 4.300   82.090  60.599 1.00 19.98 ? 214  VAL A CB    1 
ATOM   1655 C CG1   . VAL A 1 214 ? 5.303   80.973  60.360 1.00 21.07 ? 214  VAL A CG1   1 
ATOM   1656 C CG2   . VAL A 1 214 ? 4.144   82.387  62.091 1.00 22.51 ? 214  VAL A CG2   1 
ATOM   1657 N N     . ASP A 1 215 ? 3.837   85.572  60.483 1.00 16.42 ? 215  ASP A N     1 
ATOM   1658 C CA    . ASP A 1 215 ? 2.722   86.498  60.777 1.00 17.08 ? 215  ASP A CA    1 
ATOM   1659 C C     . ASP A 1 215 ? 1.922   86.731  59.485 1.00 17.47 ? 215  ASP A C     1 
ATOM   1660 O O     . ASP A 1 215 ? 0.707   86.771  59.518 1.00 16.78 ? 215  ASP A O     1 
ATOM   1661 C CB    . ASP A 1 215 ? 3.217   87.829  61.346 1.00 17.37 ? 215  ASP A CB    1 
ATOM   1662 C CG    . ASP A 1 215 ? 3.942   87.669  62.672 1.00 18.26 ? 215  ASP A CG    1 
ATOM   1663 O OD1   . ASP A 1 215 ? 4.902   86.884  62.707 1.00 17.06 ? 215  ASP A OD1   1 
ATOM   1664 O OD2   . ASP A 1 215 ? 3.468   88.269  63.653 1.00 17.78 ? 215  ASP A OD2   1 
ATOM   1665 N N     . GLY A 1 216 ? 2.615   86.903  58.364 1.00 16.95 ? 216  GLY A N     1 
ATOM   1666 C CA    . GLY A 1 216 ? 2.014   87.158  57.051 1.00 16.78 ? 216  GLY A CA    1 
ATOM   1667 C C     . GLY A 1 216 ? 0.995   86.113  56.601 1.00 17.00 ? 216  GLY A C     1 
ATOM   1668 O O     . GLY A 1 216 ? 0.045   86.504  55.848 1.00 16.30 ? 216  GLY A O     1 
ATOM   1669 N N     . ILE A 1 217 ? 1.143   84.860  57.005 1.00 16.33 ? 217  ILE A N     1 
ATOM   1670 C CA    . ILE A 1 217 ? 0.245   83.778  56.505 1.00 18.00 ? 217  ILE A CA    1 
ATOM   1671 C C     . ILE A 1 217 ? -1.127  83.939  57.131 1.00 18.30 ? 217  ILE A C     1 
ATOM   1672 O O     . ILE A 1 217 ? -2.056  83.292  56.627 1.00 17.15 ? 217  ILE A O     1 
ATOM   1673 C CB    . ILE A 1 217 ? 0.782   82.349  56.688 1.00 18.55 ? 217  ILE A CB    1 
ATOM   1674 C CG1   . ILE A 1 217 ? 0.611   81.804  58.101 1.00 17.03 ? 217  ILE A CG1   1 
ATOM   1675 C CG2   . ILE A 1 217 ? 2.211   82.277  56.234 1.00 17.94 ? 217  ILE A CG2   1 
ATOM   1676 C CD1   . ILE A 1 217 ? 1.047   80.368  58.266 1.00 18.43 ? 217  ILE A CD1   1 
ATOM   1677 N N     . PHE A 1 218 ? -1.287  84.815  58.128 1.00 17.19 ? 218  PHE A N     1 
ATOM   1678 C CA    . PHE A 1 218 ? -2.615  85.005  58.744 1.00 17.27 ? 218  PHE A CA    1 
ATOM   1679 C C     . PHE A 1 218 ? -3.267  86.269  58.190 1.00 19.75 ? 218  PHE A C     1 
ATOM   1680 O O     . PHE A 1 218 ? -4.335  86.583  58.680 1.00 20.41 ? 218  PHE A O     1 
ATOM   1681 C CB    . PHE A 1 218 ? -2.511  84.995  60.263 1.00 16.81 ? 218  PHE A CB    1 
ATOM   1682 C CG    . PHE A 1 218 ? -1.920  83.713  60.764 1.00 17.09 ? 218  PHE A CG    1 
ATOM   1683 C CD1   . PHE A 1 218 ? -2.637  82.520  60.698 1.00 19.01 ? 218  PHE A CD1   1 
ATOM   1684 C CD2   . PHE A 1 218 ? -0.641  83.671  61.294 1.00 17.26 ? 218  PHE A CD2   1 
ATOM   1685 C CE1   . PHE A 1 218 ? -2.071  81.336  61.136 1.00 16.87 ? 218  PHE A CE1   1 
ATOM   1686 C CE2   . PHE A 1 218 ? -0.095  82.484  61.754 1.00 18.30 ? 218  PHE A CE2   1 
ATOM   1687 C CZ    . PHE A 1 218 ? -0.799  81.310  61.660 1.00 18.02 ? 218  PHE A CZ    1 
ATOM   1688 N N     . SER A 1 219 ? -2.644  86.950  57.219 1.00 16.25 ? 219  SER A N     1 
ATOM   1689 C CA    . SER A 1 219 ? -3.242  88.113  56.532 1.00 15.99 ? 219  SER A CA    1 
ATOM   1690 C C     . SER A 1 219 ? -3.849  87.617  55.207 1.00 17.11 ? 219  SER A C     1 
ATOM   1691 O O     . SER A 1 219 ? -3.317  86.637  54.642 1.00 18.17 ? 219  SER A O     1 
ATOM   1692 C CB    . SER A 1 219 ? -2.169  89.188  56.337 1.00 18.31 ? 219  SER A CB    1 
ATOM   1693 O OG    . SER A 1 219 ? -1.177  88.807  55.377 1.00 16.77 ? 219  SER A OG    1 
ATOM   1694 N N     . GLN A 1 220 ? -4.975  88.197  54.806 1.00 17.58 ? 220  GLN A N     1 
ATOM   1695 C CA    . GLN A 1 220 ? -5.830  87.772  53.649 1.00 18.88 ? 220  GLN A CA    1 
ATOM   1696 C C     . GLN A 1 220 ? -5.948  86.251  53.634 1.00 19.47 ? 220  GLN A C     1 
ATOM   1697 O O     . GLN A 1 220 ? -5.713  85.610  52.594 1.00 18.80 ? 220  GLN A O     1 
ATOM   1698 C CB    . GLN A 1 220 ? -5.283  88.358  52.338 1.00 18.46 ? 220  GLN A CB    1 
ATOM   1699 C CG    . GLN A 1 220 ? -5.512  89.855  52.210 1.00 18.02 ? 220  GLN A CG    1 
ATOM   1700 C CD    . GLN A 1 220 ? -5.429  90.331  50.781 1.00 18.66 ? 220  GLN A CD    1 
ATOM   1701 O OE1   . GLN A 1 220 ? -4.998  89.618  49.901 1.00 18.74 ? 220  GLN A OE1   1 
ATOM   1702 N NE2   . GLN A 1 220 ? -5.877  91.552  50.544 1.00 17.68 ? 220  GLN A NE2   1 
ATOM   1703 N N     . SER A 1 221 ? -6.289  85.671  54.782 1.00 19.19 ? 221  SER A N     1 
ATOM   1704 C CA    . SER A 1 221 ? -6.083  84.229  55.015 1.00 20.00 ? 221  SER A CA    1 
ATOM   1705 C C     . SER A 1 221 ? -7.256  83.604  55.786 1.00 19.70 ? 221  SER A C     1 
ATOM   1706 O O     . SER A 1 221 ? -7.999  84.339  56.456 1.00 17.93 ? 221  SER A O     1 
ATOM   1707 C CB    . SER A 1 221 ? -4.843  84.058  55.808 1.00 23.00 ? 221  SER A CB    1 
ATOM   1708 O OG    . SER A 1 221 ? -4.573  82.707  55.966 1.00 22.95 ? 221  SER A OG    1 
ATOM   1709 N N     . ASN A 1 222 ? -7.322  82.281  55.735 1.00 18.66 ? 222  ASN A N     1 
ATOM   1710 C CA    . ASN A 1 222 ? -8.247  81.458  56.543 1.00 19.14 ? 222  ASN A CA    1 
ATOM   1711 C C     . ASN A 1 222 ? -7.418  80.389  57.233 1.00 19.07 ? 222  ASN A C     1 
ATOM   1712 O O     . ASN A 1 222 ? -7.918  79.228  57.385 1.00 20.15 ? 222  ASN A O     1 
ATOM   1713 C CB    . ASN A 1 222 ? -9.392  80.955  55.674 1.00 19.09 ? 222  ASN A CB    1 
ATOM   1714 C CG    . ASN A 1 222 ? -8.967  80.118  54.502 1.00 19.37 ? 222  ASN A CG    1 
ATOM   1715 O OD1   . ASN A 1 222 ? -7.791  79.778  54.370 1.00 20.45 ? 222  ASN A OD1   1 
ATOM   1716 N ND2   . ASN A 1 222 ? -9.933  79.796  53.649 1.00 20.61 ? 222  ASN A ND2   1 
ATOM   1717 N N     . PHE A 1 223 ? -6.175  80.737  57.601 1.00 17.26 ? 223  PHE A N     1 
ATOM   1718 C CA    . PHE A 1 223 ? -5.241  79.810  58.287 1.00 16.27 ? 223  PHE A CA    1 
ATOM   1719 C C     . PHE A 1 223 ? -5.354  79.923  59.816 1.00 17.04 ? 223  PHE A C     1 
ATOM   1720 O O     . PHE A 1 223 ? -4.754  79.120  60.482 1.00 18.90 ? 223  PHE A O     1 
ATOM   1721 C CB    . PHE A 1 223 ? -3.786  79.995  57.868 1.00 16.88 ? 223  PHE A CB    1 
ATOM   1722 C CG    . PHE A 1 223 ? -3.468  79.713  56.421 1.00 17.50 ? 223  PHE A CG    1 
ATOM   1723 C CD1   . PHE A 1 223 ? -4.335  79.004  55.600 1.00 18.83 ? 223  PHE A CD1   1 
ATOM   1724 C CD2   . PHE A 1 223 ? -2.283  80.175  55.880 1.00 17.82 ? 223  PHE A CD2   1 
ATOM   1725 C CE1   . PHE A 1 223 ? -4.015  78.755  54.276 1.00 19.03 ? 223  PHE A CE1   1 
ATOM   1726 C CE2   . PHE A 1 223 ? -1.938  79.872  54.574 1.00 17.91 ? 223  PHE A CE2   1 
ATOM   1727 C CZ    . PHE A 1 223 ? -2.815  79.175  53.769 1.00 19.34 ? 223  PHE A CZ    1 
ATOM   1728 N N     . GLY A 1 224 ? -6.056  80.927  60.332 1.00 17.31 ? 224  GLY A N     1 
ATOM   1729 C CA    . GLY A 1 224 ? -6.234  81.105  61.771 1.00 17.87 ? 224  GLY A CA    1 
ATOM   1730 C C     . GLY A 1 224 ? -7.109  82.297  62.081 1.00 19.21 ? 224  GLY A C     1 
ATOM   1731 O O     . GLY A 1 224 ? -7.433  83.069  61.176 1.00 19.39 ? 224  GLY A O     1 
ATOM   1732 N N     . VAL A 1 225 ? -7.386  82.478  63.371 1.00 17.63 ? 225  VAL A N     1 
ATOM   1733 C CA    . VAL A 1 225 ? -8.174  83.591  63.926 1.00 17.53 ? 225  VAL A CA    1 
ATOM   1734 C C     . VAL A 1 225 ? -7.243  84.455  64.771 1.00 17.48 ? 225  VAL A C     1 
ATOM   1735 O O     . VAL A 1 225 ? -6.797  84.012  65.837 1.00 17.75 ? 225  VAL A O     1 
ATOM   1736 C CB    . VAL A 1 225 ? -9.375  83.095  64.756 1.00 18.58 ? 225  VAL A CB    1 
ATOM   1737 C CG1   . VAL A 1 225 ? -10.201 84.285  65.234 1.00 17.69 ? 225  VAL A CG1   1 
ATOM   1738 C CG2   . VAL A 1 225 ? -10.234 82.115  63.966 1.00 19.40 ? 225  VAL A CG2   1 
ATOM   1739 N N     . VAL A 1 226 ? -6.935  85.666  64.290 1.00 18.16 ? 226  VAL A N     1 
ATOM   1740 C CA    . VAL A 1 226 ? -6.047  86.575  65.052 1.00 16.32 ? 226  VAL A CA    1 
ATOM   1741 C C     . VAL A 1 226 ? -6.852  87.167  66.216 1.00 16.88 ? 226  VAL A C     1 
ATOM   1742 O O     . VAL A 1 226 ? -7.928  87.751  65.949 1.00 17.46 ? 226  VAL A O     1 
ATOM   1743 C CB    . VAL A 1 226 ? -5.506  87.662  64.117 1.00 16.44 ? 226  VAL A CB    1 
ATOM   1744 C CG1   . VAL A 1 226 ? -4.677  88.623  64.906 1.00 16.74 ? 226  VAL A CG1   1 
ATOM   1745 C CG2   . VAL A 1 226 ? -4.694  87.034  62.984 1.00 18.36 ? 226  VAL A CG2   1 
ATOM   1746 N N     . THR A 1 227 ? -6.316  87.079  67.421 1.00 16.07 ? 227  THR A N     1 
ATOM   1747 C CA    . THR A 1 227 ? -7.011  87.518  68.648 1.00 16.59 ? 227  THR A CA    1 
ATOM   1748 C C     . THR A 1 227 ? -6.304  88.673  69.341 1.00 18.04 ? 227  THR A C     1 
ATOM   1749 O O     . THR A 1 227 ? -6.950  89.261  70.255 1.00 17.48 ? 227  THR A O     1 
ATOM   1750 C CB    . THR A 1 227 ? -7.234  86.339  69.586 1.00 16.43 ? 227  THR A CB    1 
ATOM   1751 O OG1   . THR A 1 227 ? -6.012  85.657  69.846 1.00 17.13 ? 227  THR A OG1   1 
ATOM   1752 C CG2   . THR A 1 227 ? -8.257  85.375  69.029 1.00 17.98 ? 227  THR A CG2   1 
ATOM   1753 N N     . LYS A 1 228 ? -5.024  88.905  69.059 1.00 17.57 ? 228  LYS A N     1 
ATOM   1754 C CA    . LYS A 1 228 ? -4.290  90.106  69.532 1.00 16.17 ? 228  LYS A CA    1 
ATOM   1755 C C     . LYS A 1 228 ? -3.309  90.465  68.443 1.00 17.12 ? 228  LYS A C     1 
ATOM   1756 O O     . LYS A 1 228 ? -2.784  89.542  67.785 1.00 17.50 ? 228  LYS A O     1 
ATOM   1757 C CB    . LYS A 1 228 ? -3.510  89.899  70.828 1.00 17.25 ? 228  LYS A CB    1 
ATOM   1758 C CG    . LYS A 1 228 ? -4.288  89.360  72.031 1.00 18.70 ? 228  LYS A CG    1 
ATOM   1759 C CD    . LYS A 1 228 ? -3.409  89.084  73.208 1.00 17.96 ? 228  LYS A CD    1 
ATOM   1760 C CE    . LYS A 1 228 ? -4.115  88.760  74.519 1.00 21.21 ? 228  LYS A CE    1 
ATOM   1761 N NZ    . LYS A 1 228 ? -5.129  87.713  74.328 1.00 21.50 ? 228  LYS A NZ    1 
ATOM   1762 N N     . MET A 1 229 ? -2.983  91.743  68.327 1.00 18.01 ? 229  MET A N     1 
ATOM   1763 C CA    . MET A 1 229 ? -1.987  92.149  67.300 1.00 18.17 ? 229  MET A CA    1 
ATOM   1764 C C     . MET A 1 229 ? -1.283  93.414  67.787 1.00 16.87 ? 229  MET A C     1 
ATOM   1765 O O     . MET A 1 229 ? -1.959  94.374  68.303 1.00 16.81 ? 229  MET A O     1 
ATOM   1766 C CB    . MET A 1 229 ? -2.691  92.436  65.970 1.00 17.89 ? 229  MET A CB    1 
ATOM   1767 C CG    . MET A 1 229 ? -1.738  92.564  64.808 1.00 17.70 ? 229  MET A CG    1 
ATOM   1768 S SD    . MET A 1 229 ? -2.524  93.201  63.300 1.00 19.72 ? 229  MET A SD    1 
ATOM   1769 C CE    . MET A 1 229 ? -2.412  94.959  63.633 1.00 22.60 ? 229  MET A CE    1 
ATOM   1770 N N     . GLY A 1 230 ? 0.019   93.437  67.616 1.00 16.47 ? 230  GLY A N     1 
ATOM   1771 C CA    . GLY A 1 230 ? 0.800   94.653  67.845 1.00 17.13 ? 230  GLY A CA    1 
ATOM   1772 C C     . GLY A 1 230 ? 0.858   95.495  66.587 1.00 16.59 ? 230  GLY A C     1 
ATOM   1773 O O     . GLY A 1 230 ? 0.845   94.919  65.510 1.00 16.92 ? 230  GLY A O     1 
ATOM   1774 N N     . ILE A 1 231 ? 1.002   96.797  66.724 1.00 17.41 ? 231  ILE A N     1 
ATOM   1775 C CA    . ILE A 1 231 ? 1.200   97.716  65.559 1.00 17.70 ? 231  ILE A CA    1 
ATOM   1776 C C     . ILE A 1 231 ? 2.104   98.856  65.999 1.00 16.95 ? 231  ILE A C     1 
ATOM   1777 O O     . ILE A 1 231 ? 1.933   99.387  67.107 1.00 17.15 ? 231  ILE A O     1 
ATOM   1778 C CB    . ILE A 1 231 ? -0.134  98.183  64.947 1.00 17.41 ? 231  ILE A CB    1 
ATOM   1779 C CG1   . ILE A 1 231 ? 0.060   98.777  63.559 1.00 19.32 ? 231  ILE A CG1   1 
ATOM   1780 C CG2   . ILE A 1 231 ? -0.843  99.149  65.862 1.00 19.57 ? 231  ILE A CG2   1 
ATOM   1781 C CD1   . ILE A 1 231 ? -1.216  98.961  62.726 1.00 20.90 ? 231  ILE A CD1   1 
ATOM   1782 N N     . TRP A 1 232 ? 3.074   99.192  65.154 1.00 15.87 ? 232  TRP A N     1 
ATOM   1783 C CA    . TRP A 1 232 ? 3.943   100.348 65.362 1.00 16.83 ? 232  TRP A CA    1 
ATOM   1784 C C     . TRP A 1 232 ? 3.144   101.618 65.073 1.00 16.99 ? 232  TRP A C     1 
ATOM   1785 O O     . TRP A 1 232 ? 2.357   101.640 64.128 1.00 18.66 ? 232  TRP A O     1 
ATOM   1786 C CB    . TRP A 1 232 ? 5.214   100.221 64.512 1.00 17.50 ? 232  TRP A CB    1 
ATOM   1787 C CG    . TRP A 1 232 ? 6.102   99.118  64.996 1.00 17.71 ? 232  TRP A CG    1 
ATOM   1788 C CD1   . TRP A 1 232 ? 6.105   98.514  66.211 1.00 17.98 ? 232  TRP A CD1   1 
ATOM   1789 C CD2   . TRP A 1 232 ? 7.157   98.502  64.246 1.00 18.26 ? 232  TRP A CD2   1 
ATOM   1790 N NE1   . TRP A 1 232 ? 7.073   97.545  66.266 1.00 20.16 ? 232  TRP A NE1   1 
ATOM   1791 C CE2   . TRP A 1 232 ? 7.738   97.521  65.074 1.00 20.14 ? 232  TRP A CE2   1 
ATOM   1792 C CE3   . TRP A 1 232 ? 7.632   98.656  62.941 1.00 22.62 ? 232  TRP A CE3   1 
ATOM   1793 C CZ2   . TRP A 1 232 ? 8.785   96.704  64.653 1.00 21.10 ? 232  TRP A CZ2   1 
ATOM   1794 C CZ3   . TRP A 1 232 ? 8.687   97.855  62.528 1.00 23.30 ? 232  TRP A CZ3   1 
ATOM   1795 C CH2   . TRP A 1 232 ? 9.263   96.915  63.382 1.00 21.99 ? 232  TRP A CH2   1 
ATOM   1796 N N     . LEU A 1 233 ? 3.395   102.645 65.891 1.00 16.86 ? 233  LEU A N     1 
ATOM   1797 C CA    . LEU A 1 233 ? 2.759   103.966 65.813 1.00 16.29 ? 233  LEU A CA    1 
ATOM   1798 C C     . LEU A 1 233 ? 3.844   105.046 65.656 1.00 17.98 ? 233  LEU A C     1 
ATOM   1799 O O     . LEU A 1 233 ? 4.904   104.996 66.276 1.00 18.52 ? 233  LEU A O     1 
ATOM   1800 C CB    . LEU A 1 233 ? 1.939   104.238 67.073 1.00 17.61 ? 233  LEU A CB    1 
ATOM   1801 C CG    . LEU A 1 233 ? 0.799   103.283 67.368 1.00 18.48 ? 233  LEU A CG    1 
ATOM   1802 C CD1   . LEU A 1 233 ? 0.176   103.658 68.715 1.00 19.07 ? 233  LEU A CD1   1 
ATOM   1803 C CD2   . LEU A 1 233 ? -0.244  103.284 66.251 1.00 17.13 ? 233  LEU A CD2   1 
ATOM   1804 N N     . MET A 1 234 ? 3.527   106.038 64.855 1.00 18.63 ? 234  MET A N     1 
ATOM   1805 C CA    . MET A 1 234 ? 4.422   107.174 64.584 1.00 18.55 ? 234  MET A CA    1 
ATOM   1806 C C     . MET A 1 234 ? 4.447   108.156 65.750 1.00 18.59 ? 234  MET A C     1 
ATOM   1807 O O     . MET A 1 234 ? 3.405   108.661 66.170 1.00 18.98 ? 234  MET A O     1 
ATOM   1808 C CB    . MET A 1 234 ? 3.979   107.923 63.341 1.00 20.58 ? 234  MET A CB    1 
ATOM   1809 C CG    . MET A 1 234 ? 5.050   108.945 62.902 1.00 22.20 ? 234  MET A CG    1 
ATOM   1810 S SD    . MET A 1 234 ? 4.669   109.595 61.252 1.00 26.66 ? 234  MET A SD    1 
ATOM   1811 C CE    . MET A 1 234 ? 3.192   110.484 61.637 1.00 24.67 ? 234  MET A CE    1 
ATOM   1812 N N     . PRO A 1 235 ? 5.647   108.476 66.256 1.00 19.11 ? 235  PRO A N     1 
ATOM   1813 C CA    . PRO A 1 235 ? 5.826   109.603 67.179 1.00 20.75 ? 235  PRO A CA    1 
ATOM   1814 C C     . PRO A 1 235 ? 5.256   110.880 66.526 1.00 22.30 ? 235  PRO A C     1 
ATOM   1815 O O     . PRO A 1 235 ? 5.439   111.103 65.351 1.00 20.51 ? 235  PRO A O     1 
ATOM   1816 C CB    . PRO A 1 235 ? 7.333   109.694 67.447 1.00 21.27 ? 235  PRO A CB    1 
ATOM   1817 C CG    . PRO A 1 235 ? 7.820   108.326 67.080 1.00 22.13 ? 235  PRO A CG    1 
ATOM   1818 C CD    . PRO A 1 235 ? 6.920   107.816 65.963 1.00 19.12 ? 235  PRO A CD    1 
ATOM   1819 N N     . GLU A 1 236 ? 4.553   111.701 67.312 1.00 19.96 ? 236  GLU A N     1 
ATOM   1820 C CA    . GLU A 1 236 ? 4.059   112.991 66.799 1.00 22.46 ? 236  GLU A CA    1 
ATOM   1821 C C     . GLU A 1 236 ? 5.248   113.758 66.232 1.00 20.33 ? 236  GLU A C     1 
ATOM   1822 O O     . GLU A 1 236 ? 6.239   113.910 66.928 1.00 20.00 ? 236  GLU A O     1 
ATOM   1823 C CB    . GLU A 1 236 ? 3.430   113.799 67.944 1.00 26.19 ? 236  GLU A CB    1 
ATOM   1824 C CG    . GLU A 1 236 ? 2.829   115.123 67.466 1.00 31.10 ? 236  GLU A CG    1 
ATOM   1825 C CD    . GLU A 1 236 ? 1.920   115.731 68.521 1.00 37.88 ? 236  GLU A CD    1 
ATOM   1826 O OE1   . GLU A 1 236 ? 2.396   115.878 69.640 1.00 35.86 ? 236  GLU A OE1   1 
ATOM   1827 O OE2   . GLU A 1 236 ? 0.702   115.872 68.238 1.00 46.53 ? 236  GLU A OE2   1 
ATOM   1828 N N     . PRO A 1 237 ? 5.206   114.243 64.981 1.00 20.10 ? 237  PRO A N     1 
ATOM   1829 C CA    . PRO A 1 237 ? 6.347   114.974 64.419 1.00 25.40 ? 237  PRO A CA    1 
ATOM   1830 C C     . PRO A 1 237 ? 6.410   116.440 64.906 1.00 26.76 ? 237  PRO A C     1 
ATOM   1831 O O     . PRO A 1 237 ? 5.457   116.936 65.520 1.00 26.28 ? 237  PRO A O     1 
ATOM   1832 C CB    . PRO A 1 237 ? 6.094   114.848 62.902 1.00 24.93 ? 237  PRO A CB    1 
ATOM   1833 C CG    . PRO A 1 237 ? 4.595   114.890 62.818 1.00 25.42 ? 237  PRO A CG    1 
ATOM   1834 C CD    . PRO A 1 237 ? 4.094   114.101 64.032 1.00 22.36 ? 237  PRO A CD    1 
ATOM   1835 N N     . ALA A 1 238 ? 7.549   117.061 64.644 1.00 26.17 ? 238  ALA A N     1 
ATOM   1836 C CA    . ALA A 1 238 ? 7.897   118.436 65.022 1.00 29.66 ? 238  ALA A CA    1 
ATOM   1837 C C     . ALA A 1 238 ? 7.133   119.394 64.109 1.00 28.24 ? 238  ALA A C     1 
ATOM   1838 O O     . ALA A 1 238 ? 7.070   120.566 64.440 1.00 33.00 ? 238  ALA A O     1 
ATOM   1839 C CB    . ALA A 1 238 ? 9.408   118.615 64.916 1.00 32.29 ? 238  ALA A CB    1 
ATOM   1840 N N     . GLY A 1 239 ? 6.538   118.907 63.024 1.00 24.29 ? 239  GLY A N     1 
ATOM   1841 C CA    . GLY A 1 239 ? 5.759   119.759 62.111 1.00 24.46 ? 239  GLY A CA    1 
ATOM   1842 C C     . GLY A 1 239 ? 5.010   118.942 61.105 1.00 24.68 ? 239  GLY A C     1 
ATOM   1843 O O     . GLY A 1 239 ? 5.294   117.765 60.996 1.00 24.45 ? 239  GLY A O     1 
ATOM   1844 N N     . TYR A 1 240 ? 4.088   119.575 60.391 1.00 22.93 ? 240  TYR A N     1 
ATOM   1845 C CA    . TYR A 1 240 ? 3.123   118.897 59.514 1.00 23.93 ? 240  TYR A CA    1 
ATOM   1846 C C     . TYR A 1 240 ? 2.540   119.901 58.551 1.00 24.38 ? 240  TYR A C     1 
ATOM   1847 O O     . TYR A 1 240 ? 2.017   120.896 59.014 1.00 25.66 ? 240  TYR A O     1 
ATOM   1848 C CB    . TYR A 1 240 ? 2.029   118.246 60.356 1.00 24.96 ? 240  TYR A CB    1 
ATOM   1849 C CG    . TYR A 1 240 ? 0.920   117.654 59.524 1.00 24.24 ? 240  TYR A CG    1 
ATOM   1850 C CD1   . TYR A 1 240 ? 1.149   116.533 58.741 1.00 22.62 ? 240  TYR A CD1   1 
ATOM   1851 C CD2   . TYR A 1 240 ? -0.355  118.194 59.530 1.00 23.81 ? 240  TYR A CD2   1 
ATOM   1852 C CE1   . TYR A 1 240 ? 0.153   115.998 57.948 1.00 23.45 ? 240  TYR A CE1   1 
ATOM   1853 C CE2   . TYR A 1 240 ? -1.370  117.644 58.776 1.00 25.86 ? 240  TYR A CE2   1 
ATOM   1854 C CZ    . TYR A 1 240 ? -1.118  116.528 57.990 1.00 23.74 ? 240  TYR A CZ    1 
ATOM   1855 O OH    . TYR A 1 240 ? -2.100  115.966 57.239 1.00 22.77 ? 240  TYR A OH    1 
ATOM   1856 N N     . ARG A 1 241 ? 2.652   119.666 57.261 1.00 25.63 ? 241  ARG A N     1 
ATOM   1857 C CA    . ARG A 1 241 ? 2.112   120.600 56.252 1.00 24.45 ? 241  ARG A CA    1 
ATOM   1858 C C     . ARG A 1 241 ? 1.497   119.809 55.116 1.00 23.76 ? 241  ARG A C     1 
ATOM   1859 O O     . ARG A 1 241 ? 2.211   119.299 54.248 1.00 25.26 ? 241  ARG A O     1 
ATOM   1860 C CB    . ARG A 1 241 ? 3.207   121.514 55.697 1.00 28.53 ? 241  ARG A CB    1 
ATOM   1861 C CG    . ARG A 1 241 ? 3.675   122.588 56.670 1.00 39.68 ? 241  ARG A CG    1 
ATOM   1862 C CD    . ARG A 1 241 ? 4.474   123.715 56.003 1.00 55.47 ? 241  ARG A CD    1 
ATOM   1863 N NE    . ARG A 1 241 ? 5.484   124.302 56.902 1.00 53.56 ? 241  ARG A NE    1 
ATOM   1864 C CZ    . ARG A 1 241 ? 6.766   124.520 56.617 1.00 51.20 ? 241  ARG A CZ    1 
ATOM   1865 N NH1   . ARG A 1 241 ? 7.286   124.250 55.420 1.00 52.84 ? 241  ARG A NH1   1 
ATOM   1866 N NH2   . ARG A 1 241 ? 7.524   125.018 57.569 1.00 56.34 ? 241  ARG A NH2   1 
ATOM   1867 N N     . PRO A 1 242 ? 0.160   119.721 55.066 1.00 23.74 ? 242  PRO A N     1 
ATOM   1868 C CA    . PRO A 1 242 ? -0.508  119.027 53.978 1.00 22.95 ? 242  PRO A CA    1 
ATOM   1869 C C     . PRO A 1 242 ? -0.609  119.915 52.747 1.00 22.78 ? 242  PRO A C     1 
ATOM   1870 O O     . PRO A 1 242 ? -0.720  121.125 52.880 1.00 23.07 ? 242  PRO A O     1 
ATOM   1871 C CB    . PRO A 1 242 ? -1.912  118.727 54.532 1.00 25.08 ? 242  PRO A CB    1 
ATOM   1872 C CG    . PRO A 1 242 ? -2.136  119.781 55.620 1.00 28.35 ? 242  PRO A CG    1 
ATOM   1873 C CD    . PRO A 1 242 ? -0.771  120.208 56.123 1.00 26.86 ? 242  PRO A CD    1 
ATOM   1874 N N     . TYR A 1 243 ? -0.673  119.307 51.578 1.00 21.72 ? 243  TYR A N     1 
ATOM   1875 C CA    . TYR A 1 243 ? -0.660  120.052 50.284 1.00 24.32 ? 243  TYR A CA    1 
ATOM   1876 C C     . TYR A 1 243 ? -1.550  119.363 49.266 1.00 25.18 ? 243  TYR A C     1 
ATOM   1877 O O     . TYR A 1 243 ? -1.873  118.165 49.420 1.00 23.05 ? 243  TYR A O     1 
ATOM   1878 C CB    . TYR A 1 243 ? 0.778   120.245 49.778 1.00 23.88 ? 243  TYR A CB    1 
ATOM   1879 C CG    . TYR A 1 243 ? 1.521   118.965 49.508 1.00 23.19 ? 243  TYR A CG    1 
ATOM   1880 C CD1   . TYR A 1 243 ? 1.290   118.241 48.355 1.00 23.45 ? 243  TYR A CD1   1 
ATOM   1881 C CD2   . TYR A 1 243 ? 2.406   118.432 50.422 1.00 23.70 ? 243  TYR A CD2   1 
ATOM   1882 C CE1   . TYR A 1 243 ? 1.923   117.036 48.105 1.00 19.92 ? 243  TYR A CE1   1 
ATOM   1883 C CE2   . TYR A 1 243 ? 3.065   117.232 50.182 1.00 22.78 ? 243  TYR A CE2   1 
ATOM   1884 C CZ    . TYR A 1 243 ? 2.832   116.535 49.017 1.00 22.84 ? 243  TYR A CZ    1 
ATOM   1885 O OH    . TYR A 1 243 ? 3.456   115.327 48.784 1.00 23.90 ? 243  TYR A OH    1 
ATOM   1886 N N     . LEU A 1 244 ? -2.000  120.136 48.263 1.00 23.67 ? 244  LEU A N     1 
ATOM   1887 C CA    . LEU A 1 244 ? -2.781  119.639 47.120 1.00 24.35 ? 244  LEU A CA    1 
ATOM   1888 C C     . LEU A 1 244 ? -2.177  120.273 45.865 1.00 26.87 ? 244  LEU A C     1 
ATOM   1889 O O     . LEU A 1 244 ? -1.971  121.478 45.880 1.00 26.92 ? 244  LEU A O     1 
ATOM   1890 C CB    . LEU A 1 244 ? -4.252  120.016 47.265 1.00 25.82 ? 244  LEU A CB    1 
ATOM   1891 C CG    . LEU A 1 244 ? -5.136  119.619 46.081 1.00 27.15 ? 244  LEU A CG    1 
ATOM   1892 C CD1   . LEU A 1 244 ? -5.359  118.118 46.026 1.00 29.77 ? 244  LEU A CD1   1 
ATOM   1893 C CD2   . LEU A 1 244 ? -6.482  120.332 46.147 1.00 27.97 ? 244  LEU A CD2   1 
ATOM   1894 N N     . ILE A 1 245 ? -1.802  119.444 44.904 1.00 27.10 ? 245  ILE A N     1 
ATOM   1895 C CA    . ILE A 1 245 ? -1.330  119.857 43.559 1.00 25.05 ? 245  ILE A CA    1 
ATOM   1896 C C     . ILE A 1 245 ? -2.362  119.354 42.577 1.00 24.85 ? 245  ILE A C     1 
ATOM   1897 O O     . ILE A 1 245 ? -2.616  118.154 42.548 1.00 24.23 ? 245  ILE A O     1 
ATOM   1898 C CB    . ILE A 1 245 ? 0.074   119.301 43.298 1.00 26.65 ? 245  ILE A CB    1 
ATOM   1899 C CG1   . ILE A 1 245 ? 1.007   119.669 44.453 1.00 28.57 ? 245  ILE A CG1   1 
ATOM   1900 C CG2   . ILE A 1 245 ? 0.591   119.764 41.923 1.00 26.68 ? 245  ILE A CG2   1 
ATOM   1901 C CD1   . ILE A 1 245 ? 2.418   119.190 44.322 1.00 28.89 ? 245  ILE A CD1   1 
ATOM   1902 N N     . THR A 1 246 ? -2.982  120.249 41.790 1.00 25.68 ? 246  THR A N     1 
ATOM   1903 C CA    . THR A 1 246 ? -4.036  119.855 40.829 1.00 25.47 ? 246  THR A CA    1 
ATOM   1904 C C     . THR A 1 246 ? -3.492  119.940 39.400 1.00 25.38 ? 246  THR A C     1 
ATOM   1905 O O     . THR A 1 246 ? -2.647  120.765 39.145 1.00 24.30 ? 246  THR A O     1 
ATOM   1906 C CB    . THR A 1 246 ? -5.271  120.748 40.988 1.00 28.74 ? 246  THR A CB    1 
ATOM   1907 O OG1   . THR A 1 246 ? -4.934  122.084 40.597 1.00 28.37 ? 246  THR A OG1   1 
ATOM   1908 C CG2   . THR A 1 246 ? -5.768  120.773 42.420 1.00 29.83 ? 246  THR A CG2   1 
ATOM   1909 N N     . PHE A 1 247 ? -4.006  119.086 38.533 1.00 28.19 ? 247  PHE A N     1 
ATOM   1910 C CA    . PHE A 1 247 ? -3.621  118.979 37.113 1.00 28.89 ? 247  PHE A CA    1 
ATOM   1911 C C     . PHE A 1 247 ? -4.883  119.079 36.278 1.00 28.14 ? 247  PHE A C     1 
ATOM   1912 O O     . PHE A 1 247 ? -5.875  118.386 36.588 1.00 29.94 ? 247  PHE A O     1 
ATOM   1913 C CB    . PHE A 1 247 ? -2.881  117.663 36.852 1.00 27.89 ? 247  PHE A CB    1 
ATOM   1914 C CG    . PHE A 1 247 ? -1.708  117.476 37.771 1.00 28.41 ? 247  PHE A CG    1 
ATOM   1915 C CD1   . PHE A 1 247 ? -0.526  118.143 37.543 1.00 26.96 ? 247  PHE A CD1   1 
ATOM   1916 C CD2   . PHE A 1 247 ? -1.824  116.735 38.932 1.00 26.36 ? 247  PHE A CD2   1 
ATOM   1917 C CE1   . PHE A 1 247 ? 0.523   118.068 38.442 1.00 26.45 ? 247  PHE A CE1   1 
ATOM   1918 C CE2   . PHE A 1 247 ? -0.749  116.621 39.799 1.00 26.32 ? 247  PHE A CE2   1 
ATOM   1919 C CZ    . PHE A 1 247 ? 0.411   117.293 39.563 1.00 26.07 ? 247  PHE A CZ    1 
ATOM   1920 N N     . GLU A 1 248 ? -4.805  119.864 35.202 1.00 33.07 ? 248  GLU A N     1 
ATOM   1921 C CA    . GLU A 1 248 ? -5.969  120.217 34.342 1.00 35.12 ? 248  GLU A CA    1 
ATOM   1922 C C     . GLU A 1 248 ? -6.398  119.072 33.438 1.00 30.64 ? 248  GLU A C     1 
ATOM   1923 O O     . GLU A 1 248 ? -7.591  119.035 33.103 1.00 31.51 ? 248  GLU A O     1 
ATOM   1924 C CB    . GLU A 1 248 ? -5.609  121.365 33.416 1.00 44.30 ? 248  GLU A CB    1 
ATOM   1925 C CG    . GLU A 1 248 ? -5.410  122.659 34.152 1.00 58.52 ? 248  GLU A CG    1 
ATOM   1926 C CD    . GLU A 1 248 ? -6.617  123.589 34.155 1.00 68.61 ? 248  GLU A CD    1 
ATOM   1927 O OE1   . GLU A 1 248 ? -7.594  123.318 33.405 1.00 65.26 ? 248  GLU A OE1   1 
ATOM   1928 O OE2   . GLU A 1 248 ? -6.552  124.602 34.899 1.00 74.30 ? 248  GLU A OE2   1 
ATOM   1929 N N     . ASN A 1 249 ? -5.479  118.217 32.964 1.00 30.47 ? 249  ASN A N     1 
ATOM   1930 C CA    . ASN A 1 249 ? -5.818  117.293 31.848 1.00 31.01 ? 249  ASN A CA    1 
ATOM   1931 C C     . ASN A 1 249 ? -5.823  115.841 32.294 1.00 31.04 ? 249  ASN A C     1 
ATOM   1932 O O     . ASN A 1 249 ? -4.839  115.402 32.963 1.00 29.74 ? 249  ASN A O     1 
ATOM   1933 C CB    . ASN A 1 249 ? -4.838  117.485 30.699 1.00 36.23 ? 249  ASN A CB    1 
ATOM   1934 C CG    . ASN A 1 249 ? -4.828  118.925 30.249 1.00 36.04 ? 249  ASN A CG    1 
ATOM   1935 O OD1   . ASN A 1 249 ? -5.773  119.380 29.633 1.00 36.92 ? 249  ASN A OD1   1 
ATOM   1936 N ND2   . ASN A 1 249 ? -3.793  119.655 30.582 1.00 36.63 ? 249  ASN A ND2   1 
ATOM   1937 N N     . GLU A 1 250 ? -6.783  115.064 31.807 1.00 28.12 ? 250  GLU A N     1 
ATOM   1938 C CA    . GLU A 1 250 ? -6.804  113.636 32.177 1.00 34.75 ? 250  GLU A CA    1 
ATOM   1939 C C     . GLU A 1 250 ? -5.457  112.999 31.775 1.00 36.12 ? 250  GLU A C     1 
ATOM   1940 O O     . GLU A 1 250 ? -5.034  112.076 32.476 1.00 30.83 ? 250  GLU A O     1 
ATOM   1941 C CB    . GLU A 1 250 ? -8.042  112.937 31.621 1.00 35.36 ? 250  GLU A CB    1 
ATOM   1942 C CG    . GLU A 1 250 ? -8.066  112.804 30.114 1.00 36.45 ? 250  GLU A CG    1 
ATOM   1943 C CD    . GLU A 1 250 ? -9.296  112.068 29.593 1.00 40.24 ? 250  GLU A CD    1 
ATOM   1944 O OE1   . GLU A 1 250 ? -10.053 111.448 30.400 1.00 39.22 ? 250  GLU A OE1   1 
ATOM   1945 O OE2   . GLU A 1 250 ? -9.476  112.067 28.384 1.00 41.17 ? 250  GLU A OE2   1 
ATOM   1946 N N     . ASP A 1 251 ? -4.811  113.427 30.677 1.00 33.43 ? 251  ASP A N     1 
ATOM   1947 C CA    . ASP A 1 251 ? -3.555  112.794 30.180 1.00 34.36 ? 251  ASP A CA    1 
ATOM   1948 C C     . ASP A 1 251 ? -2.341  113.229 31.020 1.00 29.52 ? 251  ASP A C     1 
ATOM   1949 O O     . ASP A 1 251 ? -1.298  112.588 30.898 1.00 30.93 ? 251  ASP A O     1 
ATOM   1950 C CB    . ASP A 1 251 ? -3.352  113.050 28.680 1.00 34.52 ? 251  ASP A CB    1 
ATOM   1951 C CG    . ASP A 1 251 ? -4.301  112.276 27.767 1.00 39.76 ? 251  ASP A CG    1 
ATOM   1952 O OD1   . ASP A 1 251 ? -5.015  111.379 28.224 1.00 40.23 ? 251  ASP A OD1   1 
ATOM   1953 O OD2   . ASP A 1 251 ? -4.293  112.567 26.567 1.00 53.43 ? 251  ASP A OD2   1 
ATOM   1954 N N     . ASP A 1 252 ? -2.464  114.226 31.899 1.00 30.22 ? 252  ASP A N     1 
ATOM   1955 C CA    . ASP A 1 252 ? -1.351  114.648 32.780 1.00 30.82 ? 252  ASP A CA    1 
ATOM   1956 C C     . ASP A 1 252 ? -0.894  113.476 33.681 1.00 27.05 ? 252  ASP A C     1 
ATOM   1957 O O     . ASP A 1 252 ? 0.229   113.562 34.156 1.00 26.60 ? 252  ASP A O     1 
ATOM   1958 C CB    . ASP A 1 252 ? -1.724  115.857 33.636 1.00 33.32 ? 252  ASP A CB    1 
ATOM   1959 C CG    . ASP A 1 252 ? -1.780  117.149 32.846 1.00 37.77 ? 252  ASP A CG    1 
ATOM   1960 O OD1   . ASP A 1 252 ? -1.135  117.187 31.776 1.00 33.02 ? 252  ASP A OD1   1 
ATOM   1961 O OD2   . ASP A 1 252 ? -2.430  118.114 33.317 1.00 38.11 ? 252  ASP A OD2   1 
ATOM   1962 N N     . ILE A 1 253 ? -1.712  112.441 33.889 1.00 26.21 ? 253  ILE A N     1 
ATOM   1963 C CA    . ILE A 1 253 ? -1.419  111.407 34.919 1.00 27.83 ? 253  ILE A CA    1 
ATOM   1964 C C     . ILE A 1 253 ? -0.164  110.658 34.467 1.00 28.04 ? 253  ILE A C     1 
ATOM   1965 O O     . ILE A 1 253 ? 0.585   110.170 35.339 1.00 26.46 ? 253  ILE A O     1 
ATOM   1966 C CB    . ILE A 1 253 ? -2.616  110.482 35.208 1.00 28.33 ? 253  ILE A CB    1 
ATOM   1967 C CG1   . ILE A 1 253 ? -2.373  109.623 36.454 1.00 29.51 ? 253  ILE A CG1   1 
ATOM   1968 C CG2   . ILE A 1 253 ? -3.010  109.624 34.001 1.00 31.35 ? 253  ILE A CG2   1 
ATOM   1969 C CD1   . ILE A 1 253 ? -1.953  110.428 37.692 1.00 31.46 ? 253  ILE A CD1   1 
ATOM   1970 N N     . GLU A 1 254 ? 0.066   110.592 33.147 1.00 30.10 ? 254  GLU A N     1 
ATOM   1971 C CA    . GLU A 1 254 ? 1.265   109.920 32.596 1.00 28.89 ? 254  GLU A CA    1 
ATOM   1972 C C     . GLU A 1 254 ? 2.509   110.630 33.112 1.00 25.06 ? 254  GLU A C     1 
ATOM   1973 O O     . GLU A 1 254 ? 3.343   109.965 33.766 1.00 23.95 ? 254  GLU A O     1 
ATOM   1974 C CB    . GLU A 1 254 ? 1.248   109.873 31.067 1.00 30.80 ? 254  GLU A CB    1 
ATOM   1975 C CG    . GLU A 1 254 ? 2.442   109.101 30.509 1.00 33.46 ? 254  GLU A CG    1 
ATOM   1976 C CD    . GLU A 1 254 ? 2.407   108.810 29.010 1.00 36.51 ? 254  GLU A CD    1 
ATOM   1977 O OE1   . GLU A 1 254 ? 1.415   109.149 28.349 1.00 35.25 ? 254  GLU A OE1   1 
ATOM   1978 O OE2   . GLU A 1 254 ? 3.378   108.224 28.528 1.00 38.22 ? 254  GLU A OE2   1 
ATOM   1979 N N     . THR A 1 255 ? 2.673   111.919 32.841 1.00 27.17 ? 255  THR A N     1 
ATOM   1980 C CA    . THR A 1 255 ? 3.905   112.636 33.261 1.00 27.00 ? 255  THR A CA    1 
ATOM   1981 C C     . THR A 1 255 ? 3.939   112.750 34.795 1.00 27.15 ? 255  THR A C     1 
ATOM   1982 O O     . THR A 1 255 ? 5.040   112.698 35.395 1.00 25.84 ? 255  THR A O     1 
ATOM   1983 C CB    . THR A 1 255 ? 4.084   114.002 32.576 1.00 28.52 ? 255  THR A CB    1 
ATOM   1984 O OG1   . THR A 1 255 ? 5.430   114.417 32.817 1.00 28.98 ? 255  THR A OG1   1 
ATOM   1985 C CG2   . THR A 1 255 ? 3.197   115.117 33.085 1.00 27.93 ? 255  THR A CG2   1 
ATOM   1986 N N     . VAL A 1 256 ? 2.781   112.951 35.419 1.00 24.41 ? 256  VAL A N     1 
ATOM   1987 C CA    . VAL A 1 256 ? 2.727   113.119 36.906 1.00 25.56 ? 256  VAL A CA    1 
ATOM   1988 C C     . VAL A 1 256 ? 3.294   111.852 37.540 1.00 22.08 ? 256  VAL A C     1 
ATOM   1989 O O     . VAL A 1 256 ? 4.077   111.981 38.461 1.00 22.07 ? 256  VAL A O     1 
ATOM   1990 C CB    . VAL A 1 256 ? 1.296   113.425 37.391 1.00 26.17 ? 256  VAL A CB    1 
ATOM   1991 C CG1   . VAL A 1 256 ? 1.132   113.225 38.897 1.00 24.26 ? 256  VAL A CG1   1 
ATOM   1992 C CG2   . VAL A 1 256 ? 0.889   114.851 36.978 1.00 26.69 ? 256  VAL A CG2   1 
ATOM   1993 N N     . THR A 1 257 ? 2.888   110.679 37.059 1.00 23.46 ? 257  THR A N     1 
ATOM   1994 C CA    . THR A 1 257 ? 3.368   109.410 37.633 1.00 24.40 ? 257  THR A CA    1 
ATOM   1995 C C     . THR A 1 257 ? 4.885   109.285 37.439 1.00 26.46 ? 257  THR A C     1 
ATOM   1996 O O     . THR A 1 257 ? 5.582   108.848 38.378 1.00 23.13 ? 257  THR A O     1 
ATOM   1997 C CB    . THR A 1 257 ? 2.564   108.245 37.091 1.00 24.78 ? 257  THR A CB    1 
ATOM   1998 O OG1   . THR A 1 257 ? 1.195   108.516 37.406 1.00 26.70 ? 257  THR A OG1   1 
ATOM   1999 C CG2   . THR A 1 257 ? 3.029   106.936 37.694 1.00 25.81 ? 257  THR A CG2   1 
ATOM   2000 N N     . GLU A 1 258 ? 5.409   109.648 36.261 1.00 26.26 ? 258  GLU A N     1 
ATOM   2001 C CA    . GLU A 1 258 ? 6.862   109.609 36.007 1.00 26.24 ? 258  GLU A CA    1 
ATOM   2002 C C     . GLU A 1 258 ? 7.577   110.450 37.062 1.00 23.11 ? 258  GLU A C     1 
ATOM   2003 O O     . GLU A 1 258 ? 8.627   109.988 37.551 1.00 23.62 ? 258  GLU A O     1 
ATOM   2004 C CB    . GLU A 1 258 ? 7.186   110.116 34.593 1.00 26.48 ? 258  GLU A CB    1 
ATOM   2005 C CG    . GLU A 1 258 ? 6.834   109.107 33.521 1.00 26.76 ? 258  GLU A CG    1 
ATOM   2006 C CD    . GLU A 1 258 ? 7.603   107.797 33.621 1.00 27.92 ? 258  GLU A CD    1 
ATOM   2007 O OE1   . GLU A 1 258 ? 8.812   107.858 33.405 1.00 28.69 ? 258  GLU A OE1   1 
ATOM   2008 O OE2   . GLU A 1 258 ? 6.999   106.741 33.941 1.00 25.72 ? 258  GLU A OE2   1 
ATOM   2009 N N     . ARG A 1 259 ? 7.033   111.616 37.426 1.00 20.72 ? 259  ARG A N     1 
ATOM   2010 C CA    . ARG A 1 259 ? 7.705   112.530 38.390 1.00 22.41 ? 259  ARG A CA    1 
ATOM   2011 C C     . ARG A 1 259 ? 7.536   112.005 39.817 1.00 22.14 ? 259  ARG A C     1 
ATOM   2012 O O     . ARG A 1 259 ? 8.424   112.246 40.620 1.00 21.29 ? 259  ARG A O     1 
ATOM   2013 C CB    . ARG A 1 259 ? 7.167   113.960 38.269 1.00 25.02 ? 259  ARG A CB    1 
ATOM   2014 C CG    . ARG A 1 259 ? 7.451   114.540 36.876 1.00 28.40 ? 259  ARG A CG    1 
ATOM   2015 C CD    . ARG A 1 259 ? 6.339   115.439 36.442 1.00 30.37 ? 259  ARG A CD    1 
ATOM   2016 N NE    . ARG A 1 259 ? 6.396   115.834 35.029 1.00 35.52 ? 259  ARG A NE    1 
ATOM   2017 C CZ    . ARG A 1 259 ? 6.891   116.983 34.582 1.00 34.15 ? 259  ARG A CZ    1 
ATOM   2018 N NH1   . ARG A 1 259 ? 7.397   117.883 35.398 1.00 30.79 ? 259  ARG A NH1   1 
ATOM   2019 N NH2   . ARG A 1 259 ? 6.865   117.237 33.288 1.00 37.44 ? 259  ARG A NH2   1 
ATOM   2020 N N     . LEU A 1 260 ? 6.430   111.316 40.111 1.00 22.60 ? 260  LEU A N     1 
ATOM   2021 C CA    . LEU A 1 260 ? 6.195   110.812 41.501 1.00 22.03 ? 260  LEU A CA    1 
ATOM   2022 C C     . LEU A 1 260 ? 7.210   109.700 41.804 1.00 23.32 ? 260  LEU A C     1 
ATOM   2023 O O     . LEU A 1 260 ? 7.665   109.603 42.955 1.00 20.81 ? 260  LEU A O     1 
ATOM   2024 C CB    . LEU A 1 260 ? 4.780   110.237 41.611 1.00 23.58 ? 260  LEU A CB    1 
ATOM   2025 C CG    . LEU A 1 260 ? 3.641   111.254 41.694 1.00 24.78 ? 260  LEU A CG    1 
ATOM   2026 C CD1   . LEU A 1 260 ? 2.308   110.546 41.541 1.00 25.88 ? 260  LEU A CD1   1 
ATOM   2027 C CD2   . LEU A 1 260 ? 3.737   112.054 42.958 1.00 25.67 ? 260  LEU A CD2   1 
ATOM   2028 N N     . ARG A 1 261 ? 7.543   108.876 40.799 1.00 21.49 ? 261  ARG A N     1 
ATOM   2029 C CA    . ARG A 1 261 ? 8.404   107.683 41.008 1.00 20.22 ? 261  ARG A CA    1 
ATOM   2030 C C     . ARG A 1 261 ? 9.673   108.025 41.794 1.00 20.97 ? 261  ARG A C     1 
ATOM   2031 O O     . ARG A 1 261 ? 9.867   107.460 42.876 1.00 22.26 ? 261  ARG A O     1 
ATOM   2032 C CB    . ARG A 1 261 ? 8.750   106.977 39.715 1.00 19.53 ? 261  ARG A CB    1 
ATOM   2033 C CG    . ARG A 1 261 ? 9.617   105.749 39.973 1.00 22.11 ? 261  ARG A CG    1 
ATOM   2034 C CD    . ARG A 1 261 ? 9.791   104.926 38.728 1.00 22.70 ? 261  ARG A CD    1 
ATOM   2035 N NE    . ARG A 1 261 ? 10.378  105.773 37.706 1.00 24.12 ? 261  ARG A NE    1 
ATOM   2036 C CZ    . ARG A 1 261 ? 9.761   106.204 36.617 1.00 25.42 ? 261  ARG A CZ    1 
ATOM   2037 N NH1   . ARG A 1 261 ? 8.508   105.872 36.384 1.00 25.26 ? 261  ARG A NH1   1 
ATOM   2038 N NH2   . ARG A 1 261 ? 10.421  106.954 35.745 1.00 25.39 ? 261  ARG A NH2   1 
ATOM   2039 N N     . PRO A 1 262 ? 10.641  108.842 41.308 1.00 20.44 ? 262  PRO A N     1 
ATOM   2040 C CA    . PRO A 1 262 ? 11.879  109.036 42.054 1.00 19.76 ? 262  PRO A CA    1 
ATOM   2041 C C     . PRO A 1 262 ? 11.632  109.670 43.443 1.00 21.70 ? 262  PRO A C     1 
ATOM   2042 O O     . PRO A 1 262 ? 12.343  109.357 44.377 1.00 22.87 ? 262  PRO A O     1 
ATOM   2043 C CB    . PRO A 1 262 ? 12.743  109.961 41.165 1.00 20.97 ? 262  PRO A CB    1 
ATOM   2044 C CG    . PRO A 1 262 ? 11.733  110.635 40.277 1.00 20.37 ? 262  PRO A CG    1 
ATOM   2045 C CD    . PRO A 1 262 ? 10.640  109.589 40.035 1.00 23.02 ? 262  PRO A CD    1 
ATOM   2046 N N     . LEU A 1 263 ? 10.619  110.551 43.561 1.00 23.07 ? 263  LEU A N     1 
ATOM   2047 C CA    . LEU A 1 263 ? 10.272  111.206 44.859 1.00 22.93 ? 263  LEU A CA    1 
ATOM   2048 C C     . LEU A 1 263 ? 9.849   110.128 45.893 1.00 20.79 ? 263  LEU A C     1 
ATOM   2049 O O     . LEU A 1 263 ? 10.248  110.200 47.053 1.00 20.83 ? 263  LEU A O     1 
ATOM   2050 C CB    . LEU A 1 263 ? 9.153   112.231 44.611 1.00 21.28 ? 263  LEU A CB    1 
ATOM   2051 C CG    . LEU A 1 263 ? 9.526   113.459 43.777 1.00 23.80 ? 263  LEU A CG    1 
ATOM   2052 C CD1   . LEU A 1 263 ? 8.290   114.303 43.498 1.00 24.16 ? 263  LEU A CD1   1 
ATOM   2053 C CD2   . LEU A 1 263 ? 10.590  114.310 44.458 1.00 24.24 ? 263  LEU A CD2   1 
ATOM   2054 N N     . LYS A 1 264 ? 9.032   109.175 45.471 1.00 20.26 ? 264  LYS A N     1 
ATOM   2055 C CA    . LYS A 1 264 ? 8.554   108.125 46.373 1.00 20.68 ? 264  LYS A CA    1 
ATOM   2056 C C     . LYS A 1 264 ? 9.683   107.135 46.665 1.00 22.23 ? 264  LYS A C     1 
ATOM   2057 O O     . LYS A 1 264 ? 9.964   106.876 47.842 1.00 20.77 ? 264  LYS A O     1 
ATOM   2058 C CB    . LYS A 1 264 ? 7.323   107.415 45.825 1.00 20.78 ? 264  LYS A CB    1 
ATOM   2059 C CG    . LYS A 1 264 ? 6.767   106.440 46.862 1.00 25.68 ? 264  LYS A CG    1 
ATOM   2060 C CD    . LYS A 1 264 ? 6.293   107.219 48.121 1.00 27.19 ? 264  LYS A CD    1 
ATOM   2061 C CE    . LYS A 1 264 ? 5.835   106.318 49.227 1.00 32.88 ? 264  LYS A CE    1 
ATOM   2062 N NZ    . LYS A 1 264 ? 5.704   107.022 50.529 1.00 34.38 ? 264  LYS A NZ    1 
ATOM   2063 N N     . VAL A 1 265 ? 10.344  106.603 45.650 1.00 22.04 ? 265  VAL A N     1 
ATOM   2064 C CA    . VAL A 1 265 ? 11.375  105.552 45.889 1.00 23.54 ? 265  VAL A CA    1 
ATOM   2065 C C     . VAL A 1 265 ? 12.450  106.084 46.869 1.00 23.89 ? 265  VAL A C     1 
ATOM   2066 O O     . VAL A 1 265 ? 13.005  105.286 47.663 1.00 25.08 ? 265  VAL A O     1 
ATOM   2067 C CB    . VAL A 1 265 ? 11.933  105.069 44.540 1.00 25.69 ? 265  VAL A CB    1 
ATOM   2068 C CG1   . VAL A 1 265 ? 13.107  104.135 44.731 1.00 29.19 ? 265  VAL A CG1   1 
ATOM   2069 C CG2   . VAL A 1 265 ? 10.862  104.426 43.684 1.00 25.26 ? 265  VAL A CG2   1 
ATOM   2070 N N     . ALA A 1 266 ? 12.764  107.385 46.840 1.00 22.88 ? 266  ALA A N     1 
ATOM   2071 C CA    . ALA A 1 266 ? 13.796  107.994 47.695 1.00 24.45 ? 266  ALA A CA    1 
ATOM   2072 C C     . ALA A 1 266 ? 13.187  108.461 49.017 1.00 26.43 ? 266  ALA A C     1 
ATOM   2073 O O     . ALA A 1 266 ? 13.955  108.807 49.849 1.00 27.67 ? 266  ALA A O     1 
ATOM   2074 C CB    . ALA A 1 266 ? 14.536  109.109 47.019 1.00 25.90 ? 266  ALA A CB    1 
ATOM   2075 N N     . GLY A 1 267 ? 11.877  108.350 49.214 1.00 25.76 ? 267  GLY A N     1 
ATOM   2076 C CA    . GLY A 1 267 ? 11.231  108.719 50.485 1.00 25.31 ? 267  GLY A CA    1 
ATOM   2077 C C     . GLY A 1 267 ? 11.033  110.233 50.617 1.00 26.32 ? 267  GLY A C     1 
ATOM   2078 O O     . GLY A 1 267 ? 10.701  110.685 51.727 1.00 21.83 ? 267  GLY A O     1 
ATOM   2079 N N     . VAL A 1 268 ? 11.208  111.030 49.547 1.00 24.67 ? 268  VAL A N     1 
ATOM   2080 C CA    . VAL A 1 268 ? 10.991  112.507 49.605 1.00 24.81 ? 268  VAL A CA    1 
ATOM   2081 C C     . VAL A 1 268 ? 9.492   112.769 49.858 1.00 23.95 ? 268  VAL A C     1 
ATOM   2082 O O     . VAL A 1 268 ? 9.136   113.708 50.616 1.00 22.43 ? 268  VAL A O     1 
ATOM   2083 C CB    . VAL A 1 268 ? 11.454  113.166 48.290 1.00 26.64 ? 268  VAL A CB    1 
ATOM   2084 C CG1   . VAL A 1 268 ? 11.003  114.606 48.222 1.00 26.86 ? 268  VAL A CG1   1 
ATOM   2085 C CG2   . VAL A 1 268 ? 12.965  113.041 48.085 1.00 26.60 ? 268  VAL A CG2   1 
ATOM   2086 N N     . ILE A 1 269 ? 8.629   112.020 49.184 1.00 22.29 ? 269  ILE A N     1 
ATOM   2087 C CA    . ILE A 1 269 ? 7.188   111.899 49.525 1.00 21.68 ? 269  ILE A CA    1 
ATOM   2088 C C     . ILE A 1 269 ? 7.100   110.925 50.705 1.00 22.82 ? 269  ILE A C     1 
ATOM   2089 O O     . ILE A 1 269 ? 7.290   109.689 50.511 1.00 23.76 ? 269  ILE A O     1 
ATOM   2090 C CB    . ILE A 1 269 ? 6.337   111.465 48.326 1.00 22.41 ? 269  ILE A CB    1 
ATOM   2091 C CG1   . ILE A 1 269 ? 6.346   112.560 47.259 1.00 23.51 ? 269  ILE A CG1   1 
ATOM   2092 C CG2   . ILE A 1 269 ? 4.917   111.122 48.753 1.00 23.61 ? 269  ILE A CG2   1 
ATOM   2093 C CD1   . ILE A 1 269 ? 5.764   112.084 45.950 1.00 26.45 ? 269  ILE A CD1   1 
ATOM   2094 N N     . GLN A 1 270 ? 6.868   111.464 51.893 1.00 21.87 ? 270  GLN A N     1 
ATOM   2095 C CA    . GLN A 1 270 ? 7.035   110.689 53.146 1.00 21.27 ? 270  GLN A CA    1 
ATOM   2096 C C     . GLN A 1 270 ? 5.832   109.770 53.403 1.00 22.83 ? 270  GLN A C     1 
ATOM   2097 O O     . GLN A 1 270 ? 6.006   108.805 54.113 1.00 21.11 ? 270  GLN A O     1 
ATOM   2098 C CB    . GLN A 1 270 ? 7.210   111.648 54.298 1.00 21.08 ? 270  GLN A CB    1 
ATOM   2099 C CG    . GLN A 1 270 ? 8.547   112.399 54.284 1.00 20.27 ? 270  GLN A CG    1 
ATOM   2100 C CD    . GLN A 1 270 ? 8.431   113.666 55.096 1.00 21.56 ? 270  GLN A CD    1 
ATOM   2101 O OE1   . GLN A 1 270 ? 7.617   114.524 54.795 1.00 21.47 ? 270  GLN A OE1   1 
ATOM   2102 N NE2   . GLN A 1 270 ? 9.193   113.758 56.172 1.00 22.70 ? 270  GLN A NE2   1 
ATOM   2103 N N     . ASN A 1 271 ? 4.632   110.106 52.922 1.00 22.47 ? 271  ASN A N     1 
ATOM   2104 C CA    . ASN A 1 271 ? 3.412   109.363 53.286 1.00 21.39 ? 271  ASN A CA    1 
ATOM   2105 C C     . ASN A 1 271 ? 2.905   108.589 52.066 1.00 22.30 ? 271  ASN A C     1 
ATOM   2106 O O     . ASN A 1 271 ? 3.450   108.739 50.947 1.00 23.49 ? 271  ASN A O     1 
ATOM   2107 C CB    . ASN A 1 271 ? 2.337   110.283 53.887 1.00 21.89 ? 271  ASN A CB    1 
ATOM   2108 C CG    . ASN A 1 271 ? 1.853   111.380 52.950 1.00 24.11 ? 271  ASN A CG    1 
ATOM   2109 O OD1   . ASN A 1 271 ? 2.623   111.944 52.154 1.00 23.46 ? 271  ASN A OD1   1 
ATOM   2110 N ND2   . ASN A 1 271 ? 0.595   111.756 53.109 1.00 22.75 ? 271  ASN A ND2   1 
ATOM   2111 N N     . GLY A 1 272 ? 1.896   107.768 52.324 1.00 26.64 ? 272  GLY A N     1 
ATOM   2112 C CA    . GLY A 1 272 ? 1.055   107.101 51.314 1.00 26.96 ? 272  GLY A CA    1 
ATOM   2113 C C     . GLY A 1 272 ? 0.126   108.135 50.716 1.00 26.82 ? 272  GLY A C     1 
ATOM   2114 O O     . GLY A 1 272 ? -1.101  108.022 50.871 1.00 27.35 ? 272  GLY A O     1 
ATOM   2115 N N     . ALA A 1 273 ? 0.715   109.148 50.096 1.00 23.32 ? 273  ALA A N     1 
ATOM   2116 C CA    . ALA A 1 273 ? -0.011  110.192 49.370 1.00 24.67 ? 273  ALA A CA    1 
ATOM   2117 C C     . ALA A 1 273 ? -0.811  109.533 48.247 1.00 27.07 ? 273  ALA A C     1 
ATOM   2118 O O     . ALA A 1 273 ? -0.576  108.316 47.939 1.00 30.77 ? 273  ALA A O     1 
ATOM   2119 C CB    . ALA A 1 273 ? 0.978   111.216 48.871 1.00 25.90 ? 273  ALA A CB    1 
ATOM   2120 N N     . THR A 1 274 ? -1.650  110.332 47.581 1.00 24.95 ? 274  THR A N     1 
ATOM   2121 C CA    . THR A 1 274 ? -2.748  109.862 46.724 1.00 25.28 ? 274  THR A CA    1 
ATOM   2122 C C     . THR A 1 274 ? -2.890  110.800 45.535 1.00 23.79 ? 274  THR A C     1 
ATOM   2123 O O     . THR A 1 274 ? -2.695  112.034 45.651 1.00 22.58 ? 274  THR A O     1 
ATOM   2124 C CB    . THR A 1 274 ? -4.051  109.746 47.517 1.00 25.53 ? 274  THR A CB    1 
ATOM   2125 O OG1   . THR A 1 274 ? -4.381  111.029 48.045 1.00 25.43 ? 274  THR A OG1   1 
ATOM   2126 C CG2   . THR A 1 274 ? -3.977  108.787 48.681 1.00 26.02 ? 274  THR A CG2   1 
ATOM   2127 N N     . VAL A 1 275 ? -3.267  110.240 44.413 1.00 24.15 ? 275  VAL A N     1 
ATOM   2128 C CA    . VAL A 1 275 ? -3.701  111.039 43.248 1.00 25.86 ? 275  VAL A CA    1 
ATOM   2129 C C     . VAL A 1 275 ? -5.121  110.591 42.943 1.00 29.10 ? 275  VAL A C     1 
ATOM   2130 O O     . VAL A 1 275 ? -5.311  109.389 42.705 1.00 29.45 ? 275  VAL A O     1 
ATOM   2131 C CB    . VAL A 1 275 ? -2.781  110.873 42.032 1.00 26.55 ? 275  VAL A CB    1 
ATOM   2132 C CG1   . VAL A 1 275 ? -3.088  111.925 40.989 1.00 27.97 ? 275  VAL A CG1   1 
ATOM   2133 C CG2   . VAL A 1 275 ? -1.321  110.965 42.392 1.00 26.32 ? 275  VAL A CG2   1 
ATOM   2134 N N     . ARG A 1 276 ? -6.076  111.512 43.038 1.00 28.54 ? 276  ARG A N     1 
ATOM   2135 C CA    . ARG A 1 276 ? -7.526  111.165 43.031 1.00 26.95 ? 276  ARG A CA    1 
ATOM   2136 C C     . ARG A 1 276 ? -8.160  111.886 41.837 1.00 24.24 ? 276  ARG A C     1 
ATOM   2137 O O     . ARG A 1 276 ? -7.748  113.005 41.528 1.00 23.86 ? 276  ARG A O     1 
ATOM   2138 C CB    . ARG A 1 276 ? -8.143  111.499 44.407 1.00 29.18 ? 276  ARG A CB    1 
ATOM   2139 C CG    . ARG A 1 276 ? -7.812  110.464 45.484 1.00 29.67 ? 276  ARG A CG    1 
ATOM   2140 C CD    . ARG A 1 276 ? -8.063  110.839 46.957 1.00 29.75 ? 276  ARG A CD    1 
ATOM   2141 N NE    . ARG A 1 276 ? -9.393  111.378 47.131 1.00 28.82 ? 276  ARG A NE    1 
ATOM   2142 C CZ    . ARG A 1 276 ? -10.413 110.822 47.829 1.00 30.50 ? 276  ARG A CZ    1 
ATOM   2143 N NH1   . ARG A 1 276 ? -10.289 109.646 48.422 1.00 27.43 ? 276  ARG A NH1   1 
ATOM   2144 N NH2   . ARG A 1 276 ? -11.579 111.471 47.911 1.00 29.57 ? 276  ARG A NH2   1 
ATOM   2145 N N     . SER A 1 277 ? -9.053  111.207 41.117 1.00 25.94 ? 277  SER A N     1 
ATOM   2146 C CA    . SER A 1 277 ? -9.710  111.774 39.925 1.00 28.98 ? 277  SER A CA    1 
ATOM   2147 C C     . SER A 1 277 ? -10.692 112.878 40.369 1.00 28.09 ? 277  SER A C     1 
ATOM   2148 O O     . SER A 1 277 ? -11.179 112.871 41.516 1.00 24.08 ? 277  SER A O     1 
ATOM   2149 C CB    . SER A 1 277 ? -10.381 110.718 39.065 1.00 31.05 ? 277  SER A CB    1 
ATOM   2150 O OG    . SER A 1 277 ? -11.479 110.069 39.721 1.00 29.11 ? 277  SER A OG    1 
ATOM   2151 N N     . LEU A 1 278 ? -11.050 113.740 39.439 1.00 26.42 ? 278  LEU A N     1 
ATOM   2152 C CA    . LEU A 1 278 ? -11.994 114.857 39.682 1.00 26.51 ? 278  LEU A CA    1 
ATOM   2153 C C     . LEU A 1 278 ? -13.253 114.370 40.407 1.00 24.97 ? 278  LEU A C     1 
ATOM   2154 O O     . LEU A 1 278 ? -13.649 115.015 41.367 1.00 27.14 ? 278  LEU A O     1 
ATOM   2155 C CB    . LEU A 1 278 ? -12.370 115.461 38.335 1.00 28.15 ? 278  LEU A CB    1 
ATOM   2156 C CG    . LEU A 1 278 ? -13.510 116.479 38.379 1.00 28.26 ? 278  LEU A CG    1 
ATOM   2157 C CD1   . LEU A 1 278 ? -13.108 117.699 39.174 1.00 25.85 ? 278  LEU A CD1   1 
ATOM   2158 C CD2   . LEU A 1 278 ? -13.908 116.830 36.960 1.00 32.86 ? 278  LEU A CD2   1 
ATOM   2159 N N     . VAL A 1 279 ? -13.941 113.358 39.905 1.00 27.72 ? 279  VAL A N     1 
ATOM   2160 C CA    . VAL A 1 279 ? -15.292 113.060 40.442 1.00 30.54 ? 279  VAL A CA    1 
ATOM   2161 C C     . VAL A 1 279 ? -15.153 112.506 41.858 1.00 31.94 ? 279  VAL A C     1 
ATOM   2162 O O     . VAL A 1 279 ? -16.007 112.797 42.701 1.00 31.55 ? 279  VAL A O     1 
ATOM   2163 C CB    . VAL A 1 279 ? -16.082 112.093 39.547 1.00 30.83 ? 279  VAL A CB    1 
ATOM   2164 C CG1   . VAL A 1 279 ? -17.442 111.784 40.155 1.00 31.13 ? 279  VAL A CG1   1 
ATOM   2165 C CG2   . VAL A 1 279 ? -16.268 112.662 38.146 1.00 31.05 ? 279  VAL A CG2   1 
ATOM   2166 N N     . LEU A 1 280 ? -14.158 111.659 42.109 1.00 28.08 ? 280  LEU A N     1 
ATOM   2167 C CA    . LEU A 1 280 ? -13.980 111.121 43.482 1.00 27.58 ? 280  LEU A CA    1 
ATOM   2168 C C     . LEU A 1 280 ? -13.842 112.314 44.432 1.00 27.52 ? 280  LEU A C     1 
ATOM   2169 O O     . LEU A 1 280 ? -14.432 112.307 45.527 1.00 27.66 ? 280  LEU A O     1 
ATOM   2170 C CB    . LEU A 1 280 ? -12.754 110.211 43.502 1.00 27.57 ? 280  LEU A CB    1 
ATOM   2171 C CG    . LEU A 1 280 ? -12.406 109.653 44.875 1.00 28.55 ? 280  LEU A CG    1 
ATOM   2172 C CD1   . LEU A 1 280 ? -13.609 108.988 45.541 1.00 28.26 ? 280  LEU A CD1   1 
ATOM   2173 C CD2   . LEU A 1 280 ? -11.254 108.673 44.726 1.00 29.12 ? 280  LEU A CD2   1 
ATOM   2174 N N     . ASP A 1 281 ? -13.077 113.321 44.054 1.00 26.24 ? 281  ASP A N     1 
ATOM   2175 C CA    . ASP A 1 281 ? -12.833 114.464 44.961 1.00 27.24 ? 281  ASP A CA    1 
ATOM   2176 C C     . ASP A 1 281 ? -14.049 115.401 45.008 1.00 30.48 ? 281  ASP A C     1 
ATOM   2177 O O     . ASP A 1 281 ? -14.414 115.829 46.095 1.00 27.38 ? 281  ASP A O     1 
ATOM   2178 C CB    . ASP A 1 281 ? -11.550 115.172 44.548 1.00 28.15 ? 281  ASP A CB    1 
ATOM   2179 C CG    . ASP A 1 281 ? -10.321 114.520 45.164 1.00 31.60 ? 281  ASP A CG    1 
ATOM   2180 O OD1   . ASP A 1 281 ? -10.495 113.604 46.025 1.00 29.15 ? 281  ASP A OD1   1 
ATOM   2181 O OD2   . ASP A 1 281 ? -9.201  114.966 44.820 1.00 33.75 ? 281  ASP A OD2   1 
ATOM   2182 N N     . ALA A 1 282 ? -14.663 115.716 43.870 1.00 26.93 ? 282  ALA A N     1 
ATOM   2183 C CA    . ALA A 1 282 ? -15.849 116.604 43.832 1.00 27.02 ? 282  ALA A CA    1 
ATOM   2184 C C     . ALA A 1 282 ? -16.958 116.011 44.719 1.00 27.16 ? 282  ALA A C     1 
ATOM   2185 O O     . ALA A 1 282 ? -17.667 116.788 45.403 1.00 29.11 ? 282  ALA A O     1 
ATOM   2186 C CB    . ALA A 1 282 ? -16.320 116.788 42.408 1.00 25.73 ? 282  ALA A CB    1 
ATOM   2187 N N     . ALA A 1 283 ? -17.118 114.693 44.701 1.00 25.85 ? 283  ALA A N     1 
ATOM   2188 C CA    . ALA A 1 283 ? -18.227 113.990 45.352 1.00 24.96 ? 283  ALA A CA    1 
ATOM   2189 C C     . ALA A 1 283 ? -18.119 114.085 46.876 1.00 26.57 ? 283  ALA A C     1 
ATOM   2190 O O     . ALA A 1 283 ? -19.087 113.707 47.526 1.00 26.63 ? 283  ALA A O     1 
ATOM   2191 C CB    . ALA A 1 283 ? -18.318 112.581 44.865 1.00 25.32 ? 283  ALA A CB    1 
ATOM   2192 N N     . ILE A 1 284 ? -16.989 114.499 47.422 1.00 26.15 ? 284  ILE A N     1 
ATOM   2193 C CA    . ILE A 1 284 ? -16.877 114.703 48.897 1.00 28.55 ? 284  ILE A CA    1 
ATOM   2194 C C     . ILE A 1 284 ? -17.702 115.944 49.270 1.00 31.71 ? 284  ILE A C     1 
ATOM   2195 O O     . ILE A 1 284 ? -18.142 116.025 50.443 1.00 26.63 ? 284  ILE A O     1 
ATOM   2196 C CB    . ILE A 1 284 ? -15.407 114.817 49.342 1.00 28.51 ? 284  ILE A CB    1 
ATOM   2197 C CG1   . ILE A 1 284 ? -14.614 113.555 48.971 1.00 31.84 ? 284  ILE A CG1   1 
ATOM   2198 C CG2   . ILE A 1 284 ? -15.303 115.114 50.836 1.00 29.91 ? 284  ILE A CG2   1 
ATOM   2199 C CD1   . ILE A 1 284 ? -15.211 112.251 49.502 1.00 32.39 ? 284  ILE A CD1   1 
ATOM   2200 N N     . THR A 1 285 ? -17.916 116.904 48.346 1.00 33.23 ? 285  THR A N     1 
ATOM   2201 C CA    . THR A 1 285 ? -18.681 118.133 48.708 1.00 29.45 ? 285  THR A CA    1 
ATOM   2202 C C     . THR A 1 285 ? -19.861 118.464 47.770 1.00 34.46 ? 285  THR A C     1 
ATOM   2203 O O     . THR A 1 285 ? -20.549 119.449 48.111 1.00 33.01 ? 285  THR A O     1 
ATOM   2204 C CB    . THR A 1 285 ? -17.754 119.338 48.902 1.00 28.83 ? 285  THR A CB    1 
ATOM   2205 O OG1   . THR A 1 285 ? -17.193 119.698 47.646 1.00 28.25 ? 285  THR A OG1   1 
ATOM   2206 C CG2   . THR A 1 285 ? -16.626 119.070 49.874 1.00 32.62 ? 285  THR A CG2   1 
ATOM   2207 N N     . ARG A 1 286 ? -20.121 117.719 46.685 1.00 30.66 ? 286  ARG A N     1 
ATOM   2208 C CA    . ARG A 1 286 ? -21.178 118.047 45.684 1.00 27.68 ? 286  ARG A CA    1 
ATOM   2209 C C     . ARG A 1 286 ? -21.772 116.762 45.163 1.00 27.69 ? 286  ARG A C     1 
ATOM   2210 O O     . ARG A 1 286 ? -21.176 115.671 45.384 1.00 30.81 ? 286  ARG A O     1 
ATOM   2211 C CB    . ARG A 1 286 ? -20.668 118.844 44.488 1.00 27.86 ? 286  ARG A CB    1 
ATOM   2212 C CG    . ARG A 1 286 ? -19.908 120.113 44.836 1.00 28.61 ? 286  ARG A CG    1 
ATOM   2213 C CD    . ARG A 1 286 ? -20.868 121.232 45.236 1.00 32.51 ? 286  ARG A CD    1 
ATOM   2214 N NE    . ARG A 1 286 ? -20.263 122.529 45.473 1.00 30.24 ? 286  ARG A NE    1 
ATOM   2215 C CZ    . ARG A 1 286 ? -19.764 122.954 46.617 1.00 34.80 ? 286  ARG A CZ    1 
ATOM   2216 N NH1   . ARG A 1 286 ? -19.761 122.174 47.689 1.00 35.94 ? 286  ARG A NH1   1 
ATOM   2217 N NH2   . ARG A 1 286 ? -19.209 124.148 46.684 1.00 34.63 ? 286  ARG A NH2   1 
ATOM   2218 N N     . THR A 1 287 ? -22.954 116.864 44.563 1.00 31.07 ? 287  THR A N     1 
ATOM   2219 C CA    . THR A 1 287 ? -23.623 115.760 43.849 1.00 30.83 ? 287  THR A CA    1 
ATOM   2220 C C     . THR A 1 287 ? -23.648 116.095 42.347 1.00 31.20 ? 287  THR A C     1 
ATOM   2221 O O     . THR A 1 287 ? -23.505 117.292 41.983 1.00 30.32 ? 287  THR A O     1 
ATOM   2222 C CB    . THR A 1 287 ? -25.034 115.519 44.398 1.00 36.16 ? 287  THR A CB    1 
ATOM   2223 O OG1   . THR A 1 287 ? -25.748 116.719 44.087 1.00 34.75 ? 287  THR A OG1   1 
ATOM   2224 C CG2   . THR A 1 287 ? -25.033 115.171 45.878 1.00 36.78 ? 287  THR A CG2   1 
ATOM   2225 N N     . LYS A 1 288 ? -23.825 115.073 41.514 1.00 32.16 ? 288  LYS A N     1 
ATOM   2226 C CA    . LYS A 1 288 ? -23.839 115.251 40.044 1.00 33.36 ? 288  LYS A CA    1 
ATOM   2227 C C     . LYS A 1 288 ? -24.978 116.227 39.673 1.00 38.76 ? 288  LYS A C     1 
ATOM   2228 O O     . LYS A 1 288 ? -24.736 117.167 38.865 1.00 36.03 ? 288  LYS A O     1 
ATOM   2229 C CB    . LYS A 1 288 ? -24.014 113.909 39.363 1.00 33.89 ? 288  LYS A CB    1 
ATOM   2230 C CG    . LYS A 1 288 ? -23.894 113.971 37.846 1.00 38.84 ? 288  LYS A CG    1 
ATOM   2231 C CD    . LYS A 1 288 ? -23.963 112.606 37.234 1.00 37.37 ? 288  LYS A CD    1 
ATOM   2232 C CE    . LYS A 1 288 ? -25.385 112.101 37.166 1.00 42.50 ? 288  LYS A CE    1 
ATOM   2233 N NZ    . LYS A 1 288 ? -25.435 110.713 36.648 1.00 45.09 ? 288  LYS A NZ    1 
ATOM   2234 N N     . SER A 1 289 ? -26.151 116.046 40.296 1.00 38.63 ? 289  SER A N     1 
ATOM   2235 C CA    . SER A 1 289 ? -27.358 116.910 40.123 1.00 38.28 ? 289  SER A CA    1 
ATOM   2236 C C     . SER A 1 289 ? -27.012 118.393 40.291 1.00 35.77 ? 289  SER A C     1 
ATOM   2237 O O     . SER A 1 289 ? -27.691 119.204 39.714 1.00 38.88 ? 289  SER A O     1 
ATOM   2238 C CB    . SER A 1 289 ? -28.445 116.507 41.085 1.00 38.19 ? 289  SER A CB    1 
ATOM   2239 O OG    . SER A 1 289 ? -28.014 116.802 42.405 1.00 39.82 ? 289  SER A OG    1 
ATOM   2240 N N     . GLN A 1 290 ? -25.981 118.784 41.028 1.00 35.92 ? 290  GLN A N     1 
ATOM   2241 C CA    . GLN A 1 290 ? -25.663 120.230 41.130 1.00 34.66 ? 290  GLN A CA    1 
ATOM   2242 C C     . GLN A 1 290 ? -24.965 120.745 39.859 1.00 36.37 ? 290  GLN A C     1 
ATOM   2243 O O     . GLN A 1 290 ? -24.710 121.935 39.809 1.00 35.99 ? 290  GLN A O     1 
ATOM   2244 C CB    . GLN A 1 290 ? -24.810 120.546 42.353 1.00 34.29 ? 290  GLN A CB    1 
ATOM   2245 C CG    . GLN A 1 290 ? -25.506 120.193 43.664 1.00 39.30 ? 290  GLN A CG    1 
ATOM   2246 C CD    . GLN A 1 290 ? -24.592 120.374 44.847 1.00 41.52 ? 290  GLN A CD    1 
ATOM   2247 O OE1   . GLN A 1 290 ? -23.834 119.483 45.205 1.00 38.32 ? 290  GLN A OE1   1 
ATOM   2248 N NE2   . GLN A 1 290 ? -24.639 121.543 45.458 1.00 38.58 ? 290  GLN A NE2   1 
ATOM   2249 N N     . TYR A 1 291 ? -24.590 119.886 38.915 1.00 37.15 ? 291  TYR A N     1 
ATOM   2250 C CA    . TYR A 1 291 ? -23.868 120.302 37.685 1.00 37.99 ? 291  TYR A CA    1 
ATOM   2251 C C     . TYR A 1 291 ? -24.546 119.748 36.431 1.00 35.67 ? 291  TYR A C     1 
ATOM   2252 O O     . TYR A 1 291 ? -24.232 120.240 35.352 1.00 38.72 ? 291  TYR A O     1 
ATOM   2253 C CB    . TYR A 1 291 ? -22.406 119.836 37.756 1.00 35.52 ? 291  TYR A CB    1 
ATOM   2254 C CG    . TYR A 1 291 ? -21.618 120.462 38.879 1.00 35.24 ? 291  TYR A CG    1 
ATOM   2255 C CD1   . TYR A 1 291 ? -21.080 121.733 38.760 1.00 32.91 ? 291  TYR A CD1   1 
ATOM   2256 C CD2   . TYR A 1 291 ? -21.439 119.797 40.088 1.00 36.08 ? 291  TYR A CD2   1 
ATOM   2257 C CE1   . TYR A 1 291 ? -20.374 122.320 39.796 1.00 33.99 ? 291  TYR A CE1   1 
ATOM   2258 C CE2   . TYR A 1 291 ? -20.727 120.375 41.124 1.00 34.15 ? 291  TYR A CE2   1 
ATOM   2259 C CZ    . TYR A 1 291 ? -20.186 121.630 40.981 1.00 33.32 ? 291  TYR A CZ    1 
ATOM   2260 O OH    . TYR A 1 291 ? -19.492 122.212 41.998 1.00 32.09 ? 291  TYR A OH    1 
ATOM   2261 N N     . TYR A 1 292 ? -25.357 118.698 36.537 1.00 33.39 ? 292  TYR A N     1 
ATOM   2262 C CA    . TYR A 1 292 ? -25.771 117.921 35.359 1.00 38.00 ? 292  TYR A CA    1 
ATOM   2263 C C     . TYR A 1 292 ? -27.046 117.140 35.665 1.00 42.23 ? 292  TYR A C     1 
ATOM   2264 O O     . TYR A 1 292 ? -27.067 116.369 36.662 1.00 40.44 ? 292  TYR A O     1 
ATOM   2265 C CB    . TYR A 1 292 ? -24.612 117.013 34.948 1.00 36.13 ? 292  TYR A CB    1 
ATOM   2266 C CG    . TYR A 1 292 ? -24.854 116.159 33.726 1.00 38.74 ? 292  TYR A CG    1 
ATOM   2267 C CD1   . TYR A 1 292 ? -25.030 116.713 32.457 1.00 37.13 ? 292  TYR A CD1   1 
ATOM   2268 C CD2   . TYR A 1 292 ? -24.858 114.779 33.837 1.00 40.80 ? 292  TYR A CD2   1 
ATOM   2269 C CE1   . TYR A 1 292 ? -25.241 115.903 31.344 1.00 39.63 ? 292  TYR A CE1   1 
ATOM   2270 C CE2   . TYR A 1 292 ? -25.022 113.957 32.730 1.00 45.79 ? 292  TYR A CE2   1 
ATOM   2271 C CZ    . TYR A 1 292 ? -25.229 114.523 31.481 1.00 41.66 ? 292  TYR A CZ    1 
ATOM   2272 O OH    . TYR A 1 292 ? -25.396 113.659 30.438 1.00 42.09 ? 292  TYR A OH    1 
ATOM   2273 N N     . ASP A 1 293 ? -28.038 117.242 34.766 1.00 43.81 ? 293  ASP A N     1 
ATOM   2274 C CA    . ASP A 1 293 ? -29.357 116.573 34.952 1.00 51.10 ? 293  ASP A CA    1 
ATOM   2275 C C     . ASP A 1 293 ? -29.416 115.274 34.140 1.00 45.72 ? 293  ASP A C     1 
ATOM   2276 O O     . ASP A 1 293 ? -30.368 114.520 34.350 1.00 50.57 ? 293  ASP A O     1 
ATOM   2277 C CB    . ASP A 1 293 ? -30.546 117.521 34.731 1.00 60.07 ? 293  ASP A CB    1 
ATOM   2278 C CG    . ASP A 1 293 ? -30.390 118.514 33.598 1.00 70.77 ? 293  ASP A CG    1 
ATOM   2279 O OD1   . ASP A 1 293 ? -29.235 118.882 33.268 1.00 87.18 ? 293  ASP A OD1   1 
ATOM   2280 O OD2   . ASP A 1 293 ? -31.426 118.924 33.067 1.00 81.42 ? 293  ASP A OD2   1 
ATOM   2281 N N     . GLY A 1 294 ? -28.387 114.950 33.352 1.00 48.01 ? 294  GLY A N     1 
ATOM   2282 C CA    . GLY A 1 294 ? -28.334 113.723 32.534 1.00 48.49 ? 294  GLY A CA    1 
ATOM   2283 C C     . GLY A 1 294 ? -28.301 112.454 33.363 1.00 49.90 ? 294  GLY A C     1 
ATOM   2284 O O     . GLY A 1 294 ? -27.913 112.505 34.538 1.00 50.87 ? 294  GLY A O     1 
ATOM   2285 N N     . ASP A 1 295 ? -28.650 111.341 32.730 1.00 54.37 ? 295  ASP A N     1 
ATOM   2286 C CA    . ASP A 1 295 ? -28.880 110.021 33.368 1.00 65.49 ? 295  ASP A CA    1 
ATOM   2287 C C     . ASP A 1 295 ? -27.571 109.385 33.878 1.00 66.51 ? 295  ASP A C     1 
ATOM   2288 O O     . ASP A 1 295 ? -27.559 108.847 35.019 1.00 85.59 ? 295  ASP A O     1 
ATOM   2289 C CB    . ASP A 1 295 ? -29.551 109.086 32.363 1.00 69.87 ? 295  ASP A CB    1 
ATOM   2290 C CG    . ASP A 1 295 ? -30.596 108.220 33.024 1.00 84.19 ? 295  ASP A CG    1 
ATOM   2291 O OD1   . ASP A 1 295 ? -31.137 108.670 34.059 1.00 91.09 ? 295  ASP A OD1   1 
ATOM   2292 O OD2   . ASP A 1 295 ? -30.851 107.112 32.510 1.00 95.44 ? 295  ASP A OD2   1 
ATOM   2293 N N     . GLY A 1 296 ? -26.519 109.394 33.062 1.00 54.72 ? 296  GLY A N     1 
ATOM   2294 C CA    . GLY A 1 296 ? -25.309 108.585 33.298 1.00 46.25 ? 296  GLY A CA    1 
ATOM   2295 C C     . GLY A 1 296 ? -24.098 109.477 33.532 1.00 39.24 ? 296  GLY A C     1 
ATOM   2296 O O     . GLY A 1 296 ? -24.199 110.534 34.168 1.00 36.50 ? 296  GLY A O     1 
ATOM   2297 N N     . PRO A 1 297 ? -22.901 109.081 33.059 1.00 36.77 ? 297  PRO A N     1 
ATOM   2298 C CA    . PRO A 1 297 ? -21.679 109.751 33.491 1.00 35.41 ? 297  PRO A CA    1 
ATOM   2299 C C     . PRO A 1 297 ? -21.523 111.162 32.923 1.00 37.36 ? 297  PRO A C     1 
ATOM   2300 O O     . PRO A 1 297 ? -22.144 111.473 31.886 1.00 33.54 ? 297  PRO A O     1 
ATOM   2301 C CB    . PRO A 1 297 ? -20.547 108.810 33.014 1.00 36.54 ? 297  PRO A CB    1 
ATOM   2302 C CG    . PRO A 1 297 ? -21.164 107.976 31.903 1.00 37.65 ? 297  PRO A CG    1 
ATOM   2303 C CD    . PRO A 1 297 ? -22.650 107.924 32.182 1.00 39.98 ? 297  PRO A CD    1 
ATOM   2304 N N     . ILE A 1 298 ? -20.648 111.957 33.552 1.00 34.72 ? 298  ILE A N     1 
ATOM   2305 C CA    . ILE A 1 298 ? -20.528 113.411 33.227 1.00 35.51 ? 298  ILE A CA    1 
ATOM   2306 C C     . ILE A 1 298 ? -19.845 113.561 31.878 1.00 38.34 ? 298  ILE A C     1 
ATOM   2307 O O     . ILE A 1 298 ? -18.879 112.848 31.582 1.00 32.74 ? 298  ILE A O     1 
ATOM   2308 C CB    . ILE A 1 298 ? -19.841 114.222 34.341 1.00 35.46 ? 298  ILE A CB    1 
ATOM   2309 C CG1   . ILE A 1 298 ? -18.407 113.765 34.630 1.00 37.81 ? 298  ILE A CG1   1 
ATOM   2310 C CG2   . ILE A 1 298 ? -20.717 114.161 35.600 1.00 35.51 ? 298  ILE A CG2   1 
ATOM   2311 C CD1   . ILE A 1 298 ? -17.575 114.808 35.377 1.00 38.49 ? 298  ILE A CD1   1 
ATOM   2312 N N     . PRO A 1 299 ? -20.352 114.480 31.023 1.00 35.09 ? 299  PRO A N     1 
ATOM   2313 C CA    . PRO A 1 299 ? -19.637 114.881 29.802 1.00 34.15 ? 299  PRO A CA    1 
ATOM   2314 C C     . PRO A 1 299 ? -18.481 115.820 30.136 1.00 32.85 ? 299  PRO A C     1 
ATOM   2315 O O     . PRO A 1 299 ? -18.464 116.436 31.213 1.00 29.56 ? 299  PRO A O     1 
ATOM   2316 C CB    . PRO A 1 299 ? -20.720 115.631 28.968 1.00 33.39 ? 299  PRO A CB    1 
ATOM   2317 C CG    . PRO A 1 299 ? -21.644 116.216 30.047 1.00 35.49 ? 299  PRO A CG    1 
ATOM   2318 C CD    . PRO A 1 299 ? -21.624 115.213 31.201 1.00 35.13 ? 299  PRO A CD    1 
ATOM   2319 N N     . PRO A 1 300 ? -17.477 115.965 29.224 1.00 36.58 ? 300  PRO A N     1 
ATOM   2320 C CA    . PRO A 1 300 ? -16.375 116.921 29.401 1.00 37.69 ? 300  PRO A CA    1 
ATOM   2321 C C     . PRO A 1 300 ? -16.691 118.361 29.847 1.00 39.49 ? 300  PRO A C     1 
ATOM   2322 O O     . PRO A 1 300 ? -15.928 118.916 30.625 1.00 40.79 ? 300  PRO A O     1 
ATOM   2323 C CB    . PRO A 1 300 ? -15.760 116.943 27.992 1.00 42.04 ? 300  PRO A CB    1 
ATOM   2324 C CG    . PRO A 1 300 ? -15.886 115.507 27.537 1.00 39.51 ? 300  PRO A CG    1 
ATOM   2325 C CD    . PRO A 1 300 ? -17.257 115.097 28.046 1.00 38.90 ? 300  PRO A CD    1 
ATOM   2326 N N     . SER A 1 301 ? -17.769 118.970 29.384 1.00 33.49 ? 301  SER A N     1 
ATOM   2327 C CA    . SER A 1 301 ? -18.037 120.409 29.708 1.00 39.73 ? 301  SER A CA    1 
ATOM   2328 C C     . SER A 1 301 ? -18.405 120.558 31.191 1.00 36.04 ? 301  SER A C     1 
ATOM   2329 O O     . SER A 1 301 ? -18.149 121.625 31.817 1.00 38.34 ? 301  SER A O     1 
ATOM   2330 C CB    . SER A 1 301 ? -19.160 120.937 28.839 1.00 40.29 ? 301  SER A CB    1 
ATOM   2331 O OG    . SER A 1 301 ? -20.304 120.076 28.932 1.00 37.91 ? 301  SER A OG    1 
ATOM   2332 N N     . VAL A 1 302 ? -19.113 119.556 31.696 1.00 37.02 ? 302  VAL A N     1 
ATOM   2333 C CA    . VAL A 1 302 ? -19.524 119.467 33.126 1.00 36.92 ? 302  VAL A CA    1 
ATOM   2334 C C     . VAL A 1 302 ? -18.258 119.279 33.981 1.00 34.95 ? 302  VAL A C     1 
ATOM   2335 O O     . VAL A 1 302 ? -18.139 119.931 35.039 1.00 37.58 ? 302  VAL A O     1 
ATOM   2336 C CB    . VAL A 1 302 ? -20.549 118.328 33.310 1.00 40.69 ? 302  VAL A CB    1 
ATOM   2337 C CG1   . VAL A 1 302 ? -20.723 117.910 34.785 1.00 39.18 ? 302  VAL A CG1   1 
ATOM   2338 C CG2   . VAL A 1 302 ? -21.874 118.712 32.655 1.00 40.44 ? 302  VAL A CG2   1 
ATOM   2339 N N     . ALA A 1 303 ? -17.327 118.427 33.553 1.00 35.06 ? 303  ALA A N     1 
ATOM   2340 C CA    . ALA A 1 303 ? -16.029 118.271 34.250 1.00 34.99 ? 303  ALA A CA    1 
ATOM   2341 C C     . ALA A 1 303 ? -15.365 119.647 34.338 1.00 32.40 ? 303  ALA A C     1 
ATOM   2342 O O     . ALA A 1 303 ? -14.969 120.042 35.426 1.00 30.02 ? 303  ALA A O     1 
ATOM   2343 C CB    . ALA A 1 303 ? -15.173 117.249 33.555 1.00 36.23 ? 303  ALA A CB    1 
ATOM   2344 N N     . LYS A 1 304 ? -15.320 120.418 33.254 1.00 31.01 ? 304  LYS A N     1 
ATOM   2345 C CA    . LYS A 1 304 ? -14.578 121.711 33.267 1.00 31.85 ? 304  LYS A CA    1 
ATOM   2346 C C     . LYS A 1 304 ? -15.253 122.690 34.215 1.00 32.02 ? 304  LYS A C     1 
ATOM   2347 O O     . LYS A 1 304 ? -14.528 123.453 34.943 1.00 33.52 ? 304  LYS A O     1 
ATOM   2348 C CB    . LYS A 1 304 ? -14.454 122.270 31.844 1.00 38.66 ? 304  LYS A CB    1 
ATOM   2349 C CG    . LYS A 1 304 ? -13.621 121.381 30.921 1.00 43.72 ? 304  LYS A CG    1 
ATOM   2350 C CD    . LYS A 1 304 ? -13.714 121.741 29.449 1.00 51.87 ? 304  LYS A CD    1 
ATOM   2351 C CE    . LYS A 1 304 ? -13.203 123.142 29.162 1.00 53.80 ? 304  LYS A CE    1 
ATOM   2352 N NZ    . LYS A 1 304 ? -11.725 123.225 29.265 1.00 56.81 ? 304  LYS A NZ    1 
ATOM   2353 N N     . THR A 1 305 ? -16.586 122.671 34.267 1.00 32.32 ? 305  THR A N     1 
ATOM   2354 C CA    . THR A 1 305 ? -17.343 123.572 35.179 1.00 33.98 ? 305  THR A CA    1 
ATOM   2355 C C     . THR A 1 305 ? -16.975 123.216 36.632 1.00 32.93 ? 305  THR A C     1 
ATOM   2356 O O     . THR A 1 305 ? -16.633 124.125 37.472 1.00 30.23 ? 305  THR A O     1 
ATOM   2357 C CB    . THR A 1 305 ? -18.858 123.445 34.953 1.00 39.16 ? 305  THR A CB    1 
ATOM   2358 O OG1   . THR A 1 305 ? -19.129 123.721 33.581 1.00 37.20 ? 305  THR A OG1   1 
ATOM   2359 C CG2   . THR A 1 305 ? -19.659 124.382 35.831 1.00 40.15 ? 305  THR A CG2   1 
ATOM   2360 N N     . MET A 1 306 ? -17.032 121.922 36.942 1.00 34.55 ? 306  MET A N     1 
ATOM   2361 C CA    . MET A 1 306 ? -16.722 121.396 38.307 1.00 32.03 ? 306  MET A CA    1 
ATOM   2362 C C     . MET A 1 306 ? -15.316 121.830 38.724 1.00 30.27 ? 306  MET A C     1 
ATOM   2363 O O     . MET A 1 306 ? -15.136 122.329 39.863 1.00 30.30 ? 306  MET A O     1 
ATOM   2364 C CB    . MET A 1 306 ? -16.838 119.873 38.317 1.00 31.90 ? 306  MET A CB    1 
ATOM   2365 C CG    . MET A 1 306 ? -18.220 119.366 38.235 1.00 29.93 ? 306  MET A CG    1 
ATOM   2366 S SD    . MET A 1 306 ? -18.284 117.624 37.753 1.00 40.25 ? 306  MET A SD    1 
ATOM   2367 C CE    . MET A 1 306 ? -17.467 116.930 39.195 1.00 41.45 ? 306  MET A CE    1 
ATOM   2368 N N     . MET A 1 307 ? -14.330 121.694 37.825 1.00 32.01 ? 307  MET A N     1 
ATOM   2369 C CA    . MET A 1 307 ? -12.905 121.991 38.135 1.00 31.19 ? 307  MET A CA    1 
ATOM   2370 C C     . MET A 1 307 ? -12.777 123.454 38.556 1.00 29.84 ? 307  MET A C     1 
ATOM   2371 O O     . MET A 1 307 ? -12.107 123.741 39.575 1.00 29.86 ? 307  MET A O     1 
ATOM   2372 C CB    . MET A 1 307 ? -11.985 121.667 36.944 1.00 33.20 ? 307  MET A CB    1 
ATOM   2373 C CG    . MET A 1 307 ? -11.875 120.172 36.712 1.00 34.11 ? 307  MET A CG    1 
ATOM   2374 S SD    . MET A 1 307 ? -11.309 119.809 35.014 1.00 37.87 ? 307  MET A SD    1 
ATOM   2375 C CE    . MET A 1 307 ? -9.862  120.854 34.976 1.00 35.06 ? 307  MET A CE    1 
ATOM   2376 N N     . ALA A 1 308 ? -13.359 124.378 37.792 1.00 33.10 ? 308  ALA A N     1 
ATOM   2377 C CA    . ALA A 1 308 ? -13.225 125.836 38.068 1.00 32.23 ? 308  ALA A CA    1 
ATOM   2378 C C     . ALA A 1 308 ? -14.037 126.205 39.311 1.00 29.30 ? 308  ALA A C     1 
ATOM   2379 O O     . ALA A 1 308 ? -13.612 127.069 40.022 1.00 30.16 ? 308  ALA A O     1 
ATOM   2380 C CB    . ALA A 1 308 ? -13.731 126.627 36.882 1.00 39.61 ? 308  ALA A CB    1 
ATOM   2381 N N     . ASP A 1 309 ? -15.199 125.580 39.511 1.00 30.05 ? 309  ASP A N     1 
ATOM   2382 C CA    . ASP A 1 309 ? -16.076 125.851 40.683 1.00 33.32 ? 309  ASP A CA    1 
ATOM   2383 C C     . ASP A 1 309 ? -15.352 125.431 41.986 1.00 35.88 ? 309  ASP A C     1 
ATOM   2384 O O     . ASP A 1 309 ? -15.359 126.225 42.953 1.00 33.14 ? 309  ASP A O     1 
ATOM   2385 C CB    . ASP A 1 309 ? -17.420 125.140 40.498 1.00 33.43 ? 309  ASP A CB    1 
ATOM   2386 C CG    . ASP A 1 309 ? -18.430 125.515 41.580 1.00 37.70 ? 309  ASP A CG    1 
ATOM   2387 O OD1   . ASP A 1 309 ? -18.377 126.659 41.997 1.00 40.94 ? 309  ASP A OD1   1 
ATOM   2388 O OD2   . ASP A 1 309 ? -19.202 124.627 42.034 1.00 41.77 ? 309  ASP A OD2   1 
ATOM   2389 N N     . LEU A 1 310 ? -14.663 124.275 41.993 1.00 33.27 ? 310  LEU A N     1 
ATOM   2390 C CA    . LEU A 1 310 ? -14.144 123.646 43.259 1.00 31.12 ? 310  LEU A CA    1 
ATOM   2391 C C     . LEU A 1 310 ? -12.642 123.822 43.453 1.00 30.55 ? 310  LEU A C     1 
ATOM   2392 O O     . LEU A 1 310 ? -12.146 123.483 44.550 1.00 30.47 ? 310  LEU A O     1 
ATOM   2393 C CB    . LEU A 1 310 ? -14.531 122.178 43.243 1.00 30.72 ? 310  LEU A CB    1 
ATOM   2394 C CG    . LEU A 1 310 ? -16.031 121.961 43.164 1.00 30.90 ? 310  LEU A CG    1 
ATOM   2395 C CD1   . LEU A 1 310 ? -16.372 120.516 42.944 1.00 32.28 ? 310  LEU A CD1   1 
ATOM   2396 C CD2   . LEU A 1 310 ? -16.718 122.526 44.406 1.00 34.91 ? 310  LEU A CD2   1 
ATOM   2397 N N     . ASP A 1 311 ? -11.924 124.413 42.496 1.00 31.81 ? 311  ASP A N     1 
ATOM   2398 C CA    . ASP A 1 311 ? -10.434 124.457 42.517 1.00 32.00 ? 311  ASP A CA    1 
ATOM   2399 C C     . ASP A 1 311 ? -9.909  123.012 42.612 1.00 26.35 ? 311  ASP A C     1 
ATOM   2400 O O     . ASP A 1 311 ? -9.039  122.722 43.431 1.00 29.42 ? 311  ASP A O     1 
ATOM   2401 C CB    . ASP A 1 311 ? -9.937  125.389 43.617 1.00 31.77 ? 311  ASP A CB    1 
ATOM   2402 C CG    . ASP A 1 311 ? -10.160 126.857 43.281 1.00 38.45 ? 311  ASP A CG    1 
ATOM   2403 O OD1   . ASP A 1 311 ? -10.715 127.113 42.196 1.00 36.05 ? 311  ASP A OD1   1 
ATOM   2404 O OD2   . ASP A 1 311 ? -9.741  127.723 44.081 1.00 35.11 ? 311  ASP A OD2   1 
ATOM   2405 N N     . LEU A 1 312 ? -10.460 122.123 41.792 1.00 32.15 ? 312  LEU A N     1 
ATOM   2406 C CA    . LEU A 1 312 ? -9.938  120.746 41.588 1.00 31.06 ? 312  LEU A CA    1 
ATOM   2407 C C     . LEU A 1 312 ? -9.469  120.589 40.139 1.00 34.57 ? 312  LEU A C     1 
ATOM   2408 O O     . LEU A 1 312 ? -9.981  121.312 39.247 1.00 32.32 ? 312  LEU A O     1 
ATOM   2409 C CB    . LEU A 1 312 ? -11.035 119.729 41.897 1.00 30.97 ? 312  LEU A CB    1 
ATOM   2410 C CG    . LEU A 1 312 ? -11.556 119.766 43.343 1.00 30.67 ? 312  LEU A CG    1 
ATOM   2411 C CD1   . LEU A 1 312 ? -12.724 118.791 43.519 1.00 29.00 ? 312  LEU A CD1   1 
ATOM   2412 C CD2   . LEU A 1 312 ? -10.434 119.449 44.324 1.00 27.63 ? 312  LEU A CD2   1 
ATOM   2413 N N     . GLY A 1 313 ? -8.608  119.595 39.919 1.00 32.05 ? 313  GLY A N     1 
ATOM   2414 C CA    . GLY A 1 313 ? -8.141  119.160 38.596 1.00 27.95 ? 313  GLY A CA    1 
ATOM   2415 C C     . GLY A 1 313 ? -8.812  117.905 38.156 1.00 28.72 ? 313  GLY A C     1 
ATOM   2416 O O     . GLY A 1 313 ? -9.611  117.319 38.908 1.00 28.60 ? 313  GLY A O     1 
ATOM   2417 N N     . MET A 1 314 ? -8.464  117.449 36.958 1.00 25.74 ? 314  MET A N     1 
ATOM   2418 C CA    . MET A 1 314 ? -8.851  116.104 36.533 1.00 27.11 ? 314  MET A CA    1 
ATOM   2419 C C     . MET A 1 314 ? -8.096  115.102 37.422 1.00 24.11 ? 314  MET A C     1 
ATOM   2420 O O     . MET A 1 314 ? -8.630  113.980 37.676 1.00 24.42 ? 314  MET A O     1 
ATOM   2421 C CB    . MET A 1 314 ? -8.531  115.917 35.041 1.00 33.05 ? 314  MET A CB    1 
ATOM   2422 C CG    . MET A 1 314 ? -9.536  116.609 34.120 1.00 35.35 ? 314  MET A CG    1 
ATOM   2423 S SD    . MET A 1 314 ? -11.191 115.962 34.319 1.00 34.38 ? 314  MET A SD    1 
ATOM   2424 C CE    . MET A 1 314 ? -11.103 114.305 33.638 1.00 38.63 ? 314  MET A CE    1 
ATOM   2425 N N     . TRP A 1 315 ? -6.925  115.502 37.894 1.00 24.92 ? 315  TRP A N     1 
ATOM   2426 C CA    . TRP A 1 315 ? -6.132  114.718 38.869 1.00 26.76 ? 315  TRP A CA    1 
ATOM   2427 C C     . TRP A 1 315 ? -5.713  115.639 39.996 1.00 26.34 ? 315  TRP A C     1 
ATOM   2428 O O     . TRP A 1 315 ? -5.309  116.796 39.750 1.00 26.95 ? 315  TRP A O     1 
ATOM   2429 C CB    . TRP A 1 315 ? -4.923  114.033 38.214 1.00 26.96 ? 315  TRP A CB    1 
ATOM   2430 C CG    . TRP A 1 315 ? -5.302  112.996 37.223 1.00 24.78 ? 315  TRP A CG    1 
ATOM   2431 C CD1   . TRP A 1 315 ? -5.272  113.145 35.862 1.00 27.28 ? 315  TRP A CD1   1 
ATOM   2432 C CD2   . TRP A 1 315 ? -5.829  111.689 37.476 1.00 26.72 ? 315  TRP A CD2   1 
ATOM   2433 N NE1   . TRP A 1 315 ? -5.707  112.001 35.263 1.00 26.21 ? 315  TRP A NE1   1 
ATOM   2434 C CE2   . TRP A 1 315 ? -6.046  111.086 36.222 1.00 28.67 ? 315  TRP A CE2   1 
ATOM   2435 C CE3   . TRP A 1 315 ? -6.135  110.950 38.613 1.00 28.09 ? 315  TRP A CE3   1 
ATOM   2436 C CZ2   . TRP A 1 315 ? -6.547  109.789 36.094 1.00 30.64 ? 315  TRP A CZ2   1 
ATOM   2437 C CZ3   . TRP A 1 315 ? -6.568  109.653 38.491 1.00 28.22 ? 315  TRP A CZ3   1 
ATOM   2438 C CH2   . TRP A 1 315 ? -6.784  109.076 37.243 1.00 29.10 ? 315  TRP A CH2   1 
ATOM   2439 N N     . ASN A 1 316 ? -5.841  115.136 41.217 1.00 24.01 ? 316  ASN A N     1 
ATOM   2440 C CA    . ASN A 1 316 ? -5.530  115.911 42.437 1.00 24.45 ? 316  ASN A CA    1 
ATOM   2441 C C     . ASN A 1 316 ? -4.555  115.104 43.297 1.00 24.74 ? 316  ASN A C     1 
ATOM   2442 O O     . ASN A 1 316 ? -4.979  114.036 43.797 1.00 23.61 ? 316  ASN A O     1 
ATOM   2443 C CB    . ASN A 1 316 ? -6.840  116.180 43.172 1.00 26.10 ? 316  ASN A CB    1 
ATOM   2444 C CG    . ASN A 1 316 ? -7.798  116.924 42.260 1.00 25.27 ? 316  ASN A CG    1 
ATOM   2445 O OD1   . ASN A 1 316 ? -7.649  118.116 42.077 1.00 28.95 ? 316  ASN A OD1   1 
ATOM   2446 N ND2   . ASN A 1 316 ? -8.740  116.215 41.671 1.00 28.41 ? 316  ASN A ND2   1 
ATOM   2447 N N     . PHE A 1 317 ? -3.355  115.628 43.477 1.00 23.57 ? 317  PHE A N     1 
ATOM   2448 C CA    . PHE A 1 317 ? -2.254  114.962 44.200 1.00 23.40 ? 317  PHE A CA    1 
ATOM   2449 C C     . PHE A 1 317 ? -2.232  115.568 45.603 1.00 25.22 ? 317  PHE A C     1 
ATOM   2450 O O     . PHE A 1 317 ? -1.874  116.734 45.797 1.00 24.20 ? 317  PHE A O     1 
ATOM   2451 C CB    . PHE A 1 317 ? -0.941  115.076 43.435 1.00 26.20 ? 317  PHE A CB    1 
ATOM   2452 C CG    . PHE A 1 317 ? 0.294   114.778 44.242 1.00 23.80 ? 317  PHE A CG    1 
ATOM   2453 C CD1   . PHE A 1 317 ? 0.325   113.730 45.146 1.00 25.01 ? 317  PHE A CD1   1 
ATOM   2454 C CD2   . PHE A 1 317 ? 1.462   115.475 44.035 1.00 25.80 ? 317  PHE A CD2   1 
ATOM   2455 C CE1   . PHE A 1 317 ? 1.463   113.452 45.891 1.00 25.32 ? 317  PHE A CE1   1 
ATOM   2456 C CE2   . PHE A 1 317 ? 2.599   115.209 44.794 1.00 28.73 ? 317  PHE A CE2   1 
ATOM   2457 C CZ    . PHE A 1 317 ? 2.609   114.188 45.703 1.00 24.92 ? 317  PHE A CZ    1 
ATOM   2458 N N     . CYS A 1 318 ? -2.640  114.757 46.572 1.00 24.52 ? 318  CYS A N     1 
ATOM   2459 C CA    . CYS A 1 318 ? -2.751  115.169 47.978 1.00 24.73 ? 318  CYS A CA    1 
ATOM   2460 C C     . CYS A 1 318 ? -1.696  114.433 48.808 1.00 23.57 ? 318  CYS A C     1 
ATOM   2461 O O     . CYS A 1 318 ? -1.676  113.183 48.799 1.00 24.37 ? 318  CYS A O     1 
ATOM   2462 C CB    . CYS A 1 318 ? -4.182  114.899 48.410 1.00 30.03 ? 318  CYS A CB    1 
ATOM   2463 S SG    . CYS A 1 318 ? -4.497  115.708 49.973 1.00 38.94 ? 318  CYS A SG    1 
ATOM   2464 N N     . GLY A 1 319 ? -0.767  115.170 49.395 1.00 22.58 ? 319  GLY A N     1 
ATOM   2465 C CA    . GLY A 1 319 ? 0.295   114.606 50.242 1.00 22.24 ? 319  GLY A CA    1 
ATOM   2466 C C     . GLY A 1 319 ? 0.533   115.455 51.468 1.00 21.13 ? 319  GLY A C     1 
ATOM   2467 O O     . GLY A 1 319 ? -0.178  116.452 51.680 1.00 23.25 ? 319  GLY A O     1 
ATOM   2468 N N     . ALA A 1 320 ? 1.504   115.099 52.279 1.00 20.31 ? 320  ALA A N     1 
ATOM   2469 C CA    . ALA A 1 320 ? 1.889   115.963 53.407 1.00 20.59 ? 320  ALA A CA    1 
ATOM   2470 C C     . ALA A 1 320 ? 3.367   115.835 53.693 1.00 21.60 ? 320  ALA A C     1 
ATOM   2471 O O     . ALA A 1 320 ? 3.943   114.790 53.423 1.00 21.25 ? 320  ALA A O     1 
ATOM   2472 C CB    . ALA A 1 320 ? 1.052   115.627 54.619 1.00 21.83 ? 320  ALA A CB    1 
ATOM   2473 N N     . LEU A 1 321 ? 3.915   116.917 54.238 1.00 22.35 ? 321  LEU A N     1 
ATOM   2474 C CA    . LEU A 1 321 ? 5.274   117.049 54.751 1.00 24.08 ? 321  LEU A CA    1 
ATOM   2475 C C     . LEU A 1 321 ? 5.203   116.841 56.266 1.00 24.51 ? 321  LEU A C     1 
ATOM   2476 O O     . LEU A 1 321 ? 4.258   117.379 56.925 1.00 23.49 ? 321  LEU A O     1 
ATOM   2477 C CB    . LEU A 1 321 ? 5.782   118.457 54.425 1.00 23.31 ? 321  LEU A CB    1 
ATOM   2478 C CG    . LEU A 1 321 ? 5.566   118.922 52.990 1.00 25.44 ? 321  LEU A CG    1 
ATOM   2479 C CD1   . LEU A 1 321 ? 5.857   120.409 52.854 1.00 26.50 ? 321  LEU A CD1   1 
ATOM   2480 C CD2   . LEU A 1 321 ? 6.489   118.136 52.079 1.00 26.64 ? 321  LEU A CD2   1 
ATOM   2481 N N     . TYR A 1 322 ? 6.218   116.187 56.794 1.00 22.33 ? 322  TYR A N     1 
ATOM   2482 C CA    . TYR A 1 322 ? 6.343   115.859 58.219 1.00 21.84 ? 322  TYR A CA    1 
ATOM   2483 C C     . TYR A 1 322 ? 7.748   116.171 58.669 1.00 21.74 ? 322  TYR A C     1 
ATOM   2484 O O     . TYR A 1 322 ? 8.710   115.776 57.998 1.00 24.26 ? 322  TYR A O     1 
ATOM   2485 C CB    . TYR A 1 322 ? 6.030   114.375 58.452 1.00 20.28 ? 322  TYR A CB    1 
ATOM   2486 C CG    . TYR A 1 322 ? 4.713   113.873 57.911 1.00 20.70 ? 322  TYR A CG    1 
ATOM   2487 C CD1   . TYR A 1 322 ? 4.548   113.576 56.576 1.00 21.00 ? 322  TYR A CD1   1 
ATOM   2488 C CD2   . TYR A 1 322 ? 3.630   113.623 58.746 1.00 20.68 ? 322  TYR A CD2   1 
ATOM   2489 C CE1   . TYR A 1 322 ? 3.363   113.061 56.074 1.00 21.73 ? 322  TYR A CE1   1 
ATOM   2490 C CE2   . TYR A 1 322 ? 2.426   113.159 58.250 1.00 20.46 ? 322  TYR A CE2   1 
ATOM   2491 C CZ    . TYR A 1 322 ? 2.293   112.849 56.911 1.00 19.64 ? 322  TYR A CZ    1 
ATOM   2492 O OH    . TYR A 1 322 ? 1.131   112.355 56.416 1.00 18.83 ? 322  TYR A OH    1 
ATOM   2493 N N     . GLY A 1 323 ? 7.861   116.751 59.854 1.00 22.90 ? 323  GLY A N     1 
ATOM   2494 C CA    . GLY A 1 323 ? 9.123   116.942 60.564 1.00 25.08 ? 323  GLY A CA    1 
ATOM   2495 C C     . GLY A 1 323 ? 9.419   118.423 60.808 1.00 25.59 ? 323  GLY A C     1 
ATOM   2496 O O     . GLY A 1 323 ? 8.553   119.301 60.655 1.00 21.88 ? 323  GLY A O     1 
ATOM   2497 N N     . PRO A 1 324 ? 10.644  118.731 61.261 1.00 25.77 ? 324  PRO A N     1 
ATOM   2498 C CA    . PRO A 1 324 ? 11.036  120.111 61.501 1.00 31.08 ? 324  PRO A CA    1 
ATOM   2499 C C     . PRO A 1 324 ? 10.862  120.939 60.232 1.00 28.52 ? 324  PRO A C     1 
ATOM   2500 O O     . PRO A 1 324 ? 11.060  120.441 59.113 1.00 27.29 ? 324  PRO A O     1 
ATOM   2501 C CB    . PRO A 1 324 ? 12.526  120.055 61.907 1.00 31.12 ? 324  PRO A CB    1 
ATOM   2502 C CG    . PRO A 1 324 ? 12.830  118.594 62.159 1.00 30.78 ? 324  PRO A CG    1 
ATOM   2503 C CD    . PRO A 1 324 ? 11.715  117.778 61.537 1.00 28.97 ? 324  PRO A CD    1 
ATOM   2504 N N     . PRO A 1 325 ? 10.537  122.241 60.379 1.00 33.35 ? 325  PRO A N     1 
ATOM   2505 C CA    . PRO A 1 325 ? 10.428  123.144 59.230 1.00 34.25 ? 325  PRO A CA    1 
ATOM   2506 C C     . PRO A 1 325 ? 11.595  123.103 58.235 1.00 31.67 ? 325  PRO A C     1 
ATOM   2507 O O     . PRO A 1 325 ? 11.361  123.081 57.032 1.00 31.48 ? 325  PRO A O     1 
ATOM   2508 C CB    . PRO A 1 325 ? 10.253  124.509 59.915 1.00 37.46 ? 325  PRO A CB    1 
ATOM   2509 C CG    . PRO A 1 325 ? 9.507   124.158 61.196 1.00 35.74 ? 325  PRO A CG    1 
ATOM   2510 C CD    . PRO A 1 325 ? 10.221  122.909 61.664 1.00 34.99 ? 325  PRO A CD    1 
ATOM   2511 N N     . PRO A 1 326 ? 12.886  123.067 58.622 1.00 31.47 ? 326  PRO A N     1 
ATOM   2512 C CA    . PRO A 1 326 ? 13.942  122.980 57.609 1.00 32.89 ? 326  PRO A CA    1 
ATOM   2513 C C     . PRO A 1 326 ? 13.840  121.703 56.769 1.00 31.82 ? 326  PRO A C     1 
ATOM   2514 O O     . PRO A 1 326 ? 14.161  121.715 55.584 1.00 31.24 ? 326  PRO A O     1 
ATOM   2515 C CB    . PRO A 1 326 ? 15.254  123.008 58.387 1.00 32.64 ? 326  PRO A CB    1 
ATOM   2516 C CG    . PRO A 1 326 ? 14.878  123.551 59.742 1.00 36.64 ? 326  PRO A CG    1 
ATOM   2517 C CD    . PRO A 1 326 ? 13.422  123.184 59.983 1.00 33.88 ? 326  PRO A CD    1 
ATOM   2518 N N     . VAL A 1 327 ? 13.388  120.604 57.374 1.00 29.02 ? 327  VAL A N     1 
ATOM   2519 C CA    . VAL A 1 327 ? 13.199  119.333 56.623 1.00 26.72 ? 327  VAL A CA    1 
ATOM   2520 C C     . VAL A 1 327 ? 12.022  119.514 55.658 1.00 26.27 ? 327  VAL A C     1 
ATOM   2521 O O     . VAL A 1 327 ? 12.155  119.217 54.436 1.00 23.96 ? 327  VAL A O     1 
ATOM   2522 C CB    . VAL A 1 327 ? 13.010  118.140 57.572 1.00 27.21 ? 327  VAL A CB    1 
ATOM   2523 C CG1   . VAL A 1 327 ? 12.577  116.914 56.796 1.00 26.79 ? 327  VAL A CG1   1 
ATOM   2524 C CG2   . VAL A 1 327 ? 14.258  117.855 58.377 1.00 27.78 ? 327  VAL A CG2   1 
ATOM   2525 N N     . MET A 1 328 ? 10.892  120.020 56.157 1.00 27.15 ? 328  MET A N     1 
ATOM   2526 C CA    . MET A 1 328 ? 9.680   120.194 55.318 1.00 27.97 ? 328  MET A CA    1 
ATOM   2527 C C     . MET A 1 328 ? 10.013  121.129 54.151 1.00 27.67 ? 328  MET A C     1 
ATOM   2528 O O     . MET A 1 328 ? 9.590   120.820 53.016 1.00 28.05 ? 328  MET A O     1 
ATOM   2529 C CB    . MET A 1 328 ? 8.480   120.689 56.136 1.00 27.12 ? 328  MET A CB    1 
ATOM   2530 C CG    . MET A 1 328 ? 8.024   119.609 57.170 1.00 27.74 ? 328  MET A CG    1 
ATOM   2531 S SD    . MET A 1 328 ? 6.393   120.012 57.866 1.00 27.07 ? 328  MET A SD    1 
ATOM   2532 C CE    . MET A 1 328 ? 6.829   121.454 58.839 1.00 29.90 ? 328  MET A CE    1 
ATOM   2533 N N     . ASP A 1 329 ? 10.786  122.190 54.388 1.00 26.89 ? 329  ASP A N     1 
ATOM   2534 C CA    . ASP A 1 329 ? 11.137  123.173 53.318 1.00 28.27 ? 329  ASP A CA    1 
ATOM   2535 C C     . ASP A 1 329 ? 11.966  122.456 52.244 1.00 26.84 ? 329  ASP A C     1 
ATOM   2536 O O     . ASP A 1 329 ? 11.690  122.666 51.068 1.00 26.47 ? 329  ASP A O     1 
ATOM   2537 C CB    . ASP A 1 329 ? 11.932  124.385 53.842 1.00 30.24 ? 329  ASP A CB    1 
ATOM   2538 C CG    . ASP A 1 329 ? 11.160  125.374 54.707 1.00 33.34 ? 329  ASP A CG    1 
ATOM   2539 O OD1   . ASP A 1 329 ? 9.969   125.531 54.488 1.00 34.97 ? 329  ASP A OD1   1 
ATOM   2540 O OD2   . ASP A 1 329 ? 11.766  125.969 55.621 1.00 40.54 ? 329  ASP A OD2   1 
ATOM   2541 N N     . THR A 1 330 ? 12.968  121.674 52.639 1.00 26.05 ? 330  THR A N     1 
ATOM   2542 C CA    . THR A 1 330 ? 13.831  120.954 51.673 1.00 26.23 ? 330  THR A CA    1 
ATOM   2543 C C     . THR A 1 330 ? 12.999  119.982 50.843 1.00 29.04 ? 330  THR A C     1 
ATOM   2544 O O     . THR A 1 330 ? 13.186  119.949 49.610 1.00 26.35 ? 330  THR A O     1 
ATOM   2545 C CB    . THR A 1 330 ? 14.941  120.178 52.368 1.00 26.63 ? 330  THR A CB    1 
ATOM   2546 O OG1   . THR A 1 330 ? 15.690  121.126 53.099 1.00 29.63 ? 330  THR A OG1   1 
ATOM   2547 C CG2   . THR A 1 330 ? 15.839  119.439 51.405 1.00 30.25 ? 330  THR A CG2   1 
ATOM   2548 N N     . LEU A 1 331 ? 12.119  119.186 51.471 1.00 26.65 ? 331  LEU A N     1 
ATOM   2549 C CA    . LEU A 1 331 ? 11.342  118.190 50.707 1.00 25.46 ? 331  LEU A CA    1 
ATOM   2550 C C     . LEU A 1 331 ? 10.339  118.930 49.824 1.00 24.69 ? 331  LEU A C     1 
ATOM   2551 O O     . LEU A 1 331 ? 10.130  118.511 48.702 1.00 24.86 ? 331  LEU A O     1 
ATOM   2552 C CB    . LEU A 1 331 ? 10.648  117.211 51.661 1.00 26.95 ? 331  LEU A CB    1 
ATOM   2553 C CG    . LEU A 1 331 ? 11.572  116.478 52.627 1.00 26.81 ? 331  LEU A CG    1 
ATOM   2554 C CD1   . LEU A 1 331 ? 10.763  115.561 53.536 1.00 28.98 ? 331  LEU A CD1   1 
ATOM   2555 C CD2   . LEU A 1 331 ? 12.625  115.680 51.902 1.00 28.28 ? 331  LEU A CD2   1 
ATOM   2556 N N     . TRP A 1 332 ? 9.748   120.024 50.286 1.00 21.95 ? 332  TRP A N     1 
ATOM   2557 C CA    . TRP A 1 332 ? 8.782   120.756 49.444 1.00 21.53 ? 332  TRP A CA    1 
ATOM   2558 C C     . TRP A 1 332 ? 9.476   121.279 48.171 1.00 24.03 ? 332  TRP A C     1 
ATOM   2559 O O     . TRP A 1 332 ? 8.893   121.176 47.062 1.00 26.12 ? 332  TRP A O     1 
ATOM   2560 C CB    . TRP A 1 332 ? 8.090   121.871 50.234 1.00 23.72 ? 332  TRP A CB    1 
ATOM   2561 C CG    . TRP A 1 332 ? 7.091   122.586 49.390 1.00 24.65 ? 332  TRP A CG    1 
ATOM   2562 C CD1   . TRP A 1 332 ? 7.139   123.915 49.041 1.00 28.18 ? 332  TRP A CD1   1 
ATOM   2563 C CD2   . TRP A 1 332 ? 5.910   122.044 48.764 1.00 24.38 ? 332  TRP A CD2   1 
ATOM   2564 N NE1   . TRP A 1 332 ? 6.106   124.216 48.210 1.00 26.85 ? 332  TRP A NE1   1 
ATOM   2565 C CE2   . TRP A 1 332 ? 5.341   123.101 48.005 1.00 27.21 ? 332  TRP A CE2   1 
ATOM   2566 C CE3   . TRP A 1 332 ? 5.336   120.778 48.670 1.00 25.20 ? 332  TRP A CE3   1 
ATOM   2567 C CZ2   . TRP A 1 332 ? 4.181   122.940 47.259 1.00 30.18 ? 332  TRP A CZ2   1 
ATOM   2568 C CZ3   . TRP A 1 332 ? 4.194   120.611 47.926 1.00 27.50 ? 332  TRP A CZ3   1 
ATOM   2569 C CH2   . TRP A 1 332 ? 3.609   121.683 47.246 1.00 29.25 ? 332  TRP A CH2   1 
ATOM   2570 N N     . THR A 1 333 ? 10.665  121.856 48.295 1.00 25.77 ? 333  THR A N     1 
ATOM   2571 C CA    . THR A 1 333 ? 11.372  122.378 47.096 1.00 27.51 ? 333  THR A CA    1 
ATOM   2572 C C     . THR A 1 333 ? 11.452  121.256 46.072 1.00 26.33 ? 333  THR A C     1 
ATOM   2573 O O     . THR A 1 333 ? 11.144  121.519 44.900 1.00 26.51 ? 333  THR A O     1 
ATOM   2574 C CB    . THR A 1 333 ? 12.751  122.956 47.424 1.00 30.93 ? 333  THR A CB    1 
ATOM   2575 O OG1   . THR A 1 333 ? 12.534  124.021 48.339 1.00 31.37 ? 333  THR A OG1   1 
ATOM   2576 C CG2   . THR A 1 333 ? 13.483  123.429 46.186 1.00 34.55 ? 333  THR A CG2   1 
ATOM   2577 N N     . ALA A 1 334 ? 11.823  120.040 46.478 1.00 25.51 ? 334  ALA A N     1 
ATOM   2578 C CA    . ALA A 1 334 ? 12.011  118.923 45.524 1.00 23.26 ? 334  ALA A CA    1 
ATOM   2579 C C     . ALA A 1 334 ? 10.675  118.535 44.918 1.00 25.66 ? 334  ALA A C     1 
ATOM   2580 O O     . ALA A 1 334 ? 10.596  118.228 43.726 1.00 27.03 ? 334  ALA A O     1 
ATOM   2581 C CB    . ALA A 1 334 ? 12.675  117.776 46.206 1.00 25.47 ? 334  ALA A CB    1 
ATOM   2582 N N     . ILE A 1 335 ? 9.635   118.491 45.734 1.00 24.47 ? 335  ILE A N     1 
ATOM   2583 C CA    . ILE A 1 335 ? 8.296   118.078 45.258 1.00 25.79 ? 335  ILE A CA    1 
ATOM   2584 C C     . ILE A 1 335 ? 7.769   119.186 44.324 1.00 26.06 ? 335  ILE A C     1 
ATOM   2585 O O     . ILE A 1 335 ? 7.334   118.855 43.186 1.00 25.98 ? 335  ILE A O     1 
ATOM   2586 C CB    . ILE A 1 335 ? 7.343   117.759 46.441 1.00 26.47 ? 335  ILE A CB    1 
ATOM   2587 C CG1   . ILE A 1 335 ? 7.820   116.539 47.247 1.00 27.38 ? 335  ILE A CG1   1 
ATOM   2588 C CG2   . ILE A 1 335 ? 5.927   117.601 45.941 1.00 26.44 ? 335  ILE A CG2   1 
ATOM   2589 C CD1   . ILE A 1 335 ? 7.148   116.353 48.596 1.00 27.39 ? 335  ILE A CD1   1 
ATOM   2590 N N     . ARG A 1 336 ? 7.747   120.438 44.772 1.00 27.80 ? 336  ARG A N     1 
ATOM   2591 C CA    . ARG A 1 336 ? 7.162   121.546 43.960 1.00 29.78 ? 336  ARG A CA    1 
ATOM   2592 C C     . ARG A 1 336 ? 7.918   121.607 42.621 1.00 26.08 ? 336  ARG A C     1 
ATOM   2593 O O     . ARG A 1 336 ? 7.267   121.606 41.576 1.00 27.56 ? 336  ARG A O     1 
ATOM   2594 C CB    . ARG A 1 336 ? 7.225   122.890 44.704 1.00 31.77 ? 336  ARG A CB    1 
ATOM   2595 C CG    . ARG A 1 336 ? 6.579   124.091 43.995 1.00 35.37 ? 336  ARG A CG    1 
ATOM   2596 C CD    . ARG A 1 336 ? 7.075   125.384 44.657 1.00 40.24 ? 336  ARG A CD    1 
ATOM   2597 N NE    . ARG A 1 336 ? 8.553   125.395 44.550 1.00 51.21 ? 336  ARG A NE    1 
ATOM   2598 C CZ    . ARG A 1 336 ? 9.453   125.922 45.401 1.00 53.83 ? 336  ARG A CZ    1 
ATOM   2599 N NH1   . ARG A 1 336 ? 9.099   126.561 46.509 1.00 59.60 ? 336  ARG A NH1   1 
ATOM   2600 N NH2   . ARG A 1 336 ? 10.734  125.756 45.147 1.00 45.70 ? 336  ARG A NH2   1 
ATOM   2601 N N     . ASP A 1 337 ? 9.247   121.606 42.642 1.00 29.26 ? 337  ASP A N     1 
ATOM   2602 C CA    . ASP A 1 337 ? 10.023  121.751 41.375 1.00 30.71 ? 337  ASP A CA    1 
ATOM   2603 C C     . ASP A 1 337 ? 9.756   120.575 40.424 1.00 34.03 ? 337  ASP A C     1 
ATOM   2604 O O     . ASP A 1 337 ? 9.905   120.770 39.213 1.00 31.64 ? 337  ASP A O     1 
ATOM   2605 C CB    . ASP A 1 337 ? 11.518  121.934 41.619 1.00 32.38 ? 337  ASP A CB    1 
ATOM   2606 C CG    . ASP A 1 337 ? 11.886  123.224 42.308 1.00 34.84 ? 337  ASP A CG    1 
ATOM   2607 O OD1   . ASP A 1 337 ? 10.977  124.025 42.558 1.00 35.34 ? 337  ASP A OD1   1 
ATOM   2608 O OD2   . ASP A 1 337 ? 13.075  123.366 42.675 1.00 39.58 ? 337  ASP A OD2   1 
ATOM   2609 N N     . SER A 1 338 ? 9.335   119.403 40.895 1.00 27.54 ? 338  SER A N     1 
ATOM   2610 C CA    . SER A 1 338 ? 9.096   118.231 40.025 1.00 28.11 ? 338  SER A CA    1 
ATOM   2611 C C     . SER A 1 338 ? 7.891   118.478 39.134 1.00 30.33 ? 338  SER A C     1 
ATOM   2612 O O     . SER A 1 338 ? 7.808   117.756 38.147 1.00 30.60 ? 338  SER A O     1 
ATOM   2613 C CB    . SER A 1 338 ? 8.844   116.950 40.786 1.00 29.54 ? 338  SER A CB    1 
ATOM   2614 O OG    . SER A 1 338 ? 9.998   116.528 41.459 1.00 29.90 ? 338  SER A OG    1 
ATOM   2615 N N     . PHE A 1 339 ? 6.937   119.332 39.532 1.00 27.66 ? 339  PHE A N     1 
ATOM   2616 C CA    . PHE A 1 339 ? 5.626   119.467 38.829 1.00 28.69 ? 339  PHE A CA    1 
ATOM   2617 C C     . PHE A 1 339 ? 5.452   120.863 38.190 1.00 27.70 ? 339  PHE A C     1 
ATOM   2618 O O     . PHE A 1 339 ? 4.450   121.045 37.453 1.00 29.84 ? 339  PHE A O     1 
ATOM   2619 C CB    . PHE A 1 339 ? 4.470   119.168 39.772 1.00 27.63 ? 339  PHE A CB    1 
ATOM   2620 C CG    . PHE A 1 339 ? 4.553   117.771 40.323 1.00 25.88 ? 339  PHE A CG    1 
ATOM   2621 C CD1   . PHE A 1 339 ? 4.127   116.703 39.563 1.00 27.99 ? 339  PHE A CD1   1 
ATOM   2622 C CD2   . PHE A 1 339 ? 5.069   117.534 41.580 1.00 27.20 ? 339  PHE A CD2   1 
ATOM   2623 C CE1   . PHE A 1 339 ? 4.275   115.397 40.023 1.00 27.97 ? 339  PHE A CE1   1 
ATOM   2624 C CE2   . PHE A 1 339 ? 5.168   116.230 42.073 1.00 26.94 ? 339  PHE A CE2   1 
ATOM   2625 C CZ    . PHE A 1 339 ? 4.799   115.168 41.277 1.00 28.17 ? 339  PHE A CZ    1 
ATOM   2626 N N     . ALA A 1 340 ? 6.346   121.796 38.480 1.00 28.69 ? 340  ALA A N     1 
ATOM   2627 C CA    . ALA A 1 340 ? 6.131   123.254 38.268 1.00 32.94 ? 340  ALA A CA    1 
ATOM   2628 C C     . ALA A 1 340 ? 5.956   123.550 36.771 1.00 36.41 ? 340  ALA A C     1 
ATOM   2629 O O     . ALA A 1 340 ? 5.217   124.478 36.397 1.00 37.85 ? 340  ALA A O     1 
ATOM   2630 C CB    . ALA A 1 340 ? 7.305   123.994 38.833 1.00 34.73 ? 340  ALA A CB    1 
ATOM   2631 N N     . ASP A 1 341 ? 6.558   122.733 35.915 1.00 34.11 ? 341  ASP A N     1 
ATOM   2632 C CA    . ASP A 1 341 ? 6.637   123.053 34.478 1.00 34.45 ? 341  ASP A CA    1 
ATOM   2633 C C     . ASP A 1 341 ? 5.474   122.417 33.741 1.00 36.75 ? 341  ASP A C     1 
ATOM   2634 O O     . ASP A 1 341 ? 5.437   122.547 32.507 1.00 37.89 ? 341  ASP A O     1 
ATOM   2635 C CB    . ASP A 1 341 ? 8.020   122.682 33.935 1.00 36.90 ? 341  ASP A CB    1 
ATOM   2636 C CG    . ASP A 1 341 ? 8.284   121.221 33.687 1.00 37.88 ? 341  ASP A CG    1 
ATOM   2637 O OD1   . ASP A 1 341 ? 7.381   120.388 33.848 1.00 40.61 ? 341  ASP A OD1   1 
ATOM   2638 O OD2   . ASP A 1 341 ? 9.408   120.935 33.298 1.00 50.95 ? 341  ASP A OD2   1 
ATOM   2639 N N     . ILE A 1 342 ? 4.559   121.725 34.426 1.00 32.45 ? 342  ILE A N     1 
ATOM   2640 C CA    . ILE A 1 342 ? 3.414   121.067 33.739 1.00 31.49 ? 342  ILE A CA    1 
ATOM   2641 C C     . ILE A 1 342 ? 2.380   122.151 33.429 1.00 34.43 ? 342  ILE A C     1 
ATOM   2642 O O     . ILE A 1 342 ? 1.904   122.821 34.340 1.00 33.64 ? 342  ILE A O     1 
ATOM   2643 C CB    . ILE A 1 342 ? 2.810   119.910 34.573 1.00 31.19 ? 342  ILE A CB    1 
ATOM   2644 C CG1   . ILE A 1 342 ? 3.803   118.745 34.720 1.00 32.05 ? 342  ILE A CG1   1 
ATOM   2645 C CG2   . ILE A 1 342 ? 1.498   119.442 33.963 1.00 29.51 ? 342  ILE A CG2   1 
ATOM   2646 C CD1   . ILE A 1 342 ? 3.541   117.863 35.948 1.00 29.85 ? 342  ILE A CD1   1 
ATOM   2647 N N     . PRO A 1 343 ? 1.959   122.360 32.158 1.00 33.88 ? 343  PRO A N     1 
ATOM   2648 C CA    . PRO A 1 343 ? 0.940   123.390 31.885 1.00 33.35 ? 343  PRO A CA    1 
ATOM   2649 C C     . PRO A 1 343 ? -0.344  123.138 32.706 1.00 33.00 ? 343  PRO A C     1 
ATOM   2650 O O     . PRO A 1 343 ? -0.900  122.005 32.646 1.00 32.78 ? 343  PRO A O     1 
ATOM   2651 C CB    . PRO A 1 343 ? 0.644   123.208 30.380 1.00 35.98 ? 343  PRO A CB    1 
ATOM   2652 C CG    . PRO A 1 343 ? 1.964   122.591 29.821 1.00 36.50 ? 343  PRO A CG    1 
ATOM   2653 C CD    . PRO A 1 343 ? 2.420   121.658 30.942 1.00 34.63 ? 343  PRO A CD    1 
ATOM   2654 N N     . GLY A 1 344 ? -0.828  124.169 33.392 1.00 30.71 ? 344  GLY A N     1 
ATOM   2655 C CA    . GLY A 1 344 ? -2.131  124.146 34.092 1.00 32.83 ? 344  GLY A CA    1 
ATOM   2656 C C     . GLY A 1 344 ? -2.012  123.617 35.537 1.00 33.01 ? 344  GLY A C     1 
ATOM   2657 O O     . GLY A 1 344 ? -3.045  123.579 36.233 1.00 35.49 ? 344  GLY A O     1 
ATOM   2658 N N     . VAL A 1 345 ? -0.803  123.297 36.009 1.00 35.78 ? 345  VAL A N     1 
ATOM   2659 C CA    . VAL A 1 345 ? -0.564  122.831 37.409 1.00 34.52 ? 345  VAL A CA    1 
ATOM   2660 C C     . VAL A 1 345 ? -0.944  123.965 38.369 1.00 35.90 ? 345  VAL A C     1 
ATOM   2661 O O     . VAL A 1 345 ? -0.574  125.106 38.110 1.00 35.05 ? 345  VAL A O     1 
ATOM   2662 C CB    . VAL A 1 345 ? 0.893   122.384 37.640 1.00 31.69 ? 345  VAL A CB    1 
ATOM   2663 C CG1   . VAL A 1 345 ? 1.892   123.520 37.597 1.00 28.96 ? 345  VAL A CG1   1 
ATOM   2664 C CG2   . VAL A 1 345 ? 1.052   121.652 38.966 1.00 29.79 ? 345  VAL A CG2   1 
ATOM   2665 N N     . LYS A 1 346 ? -1.535  123.639 39.516 1.00 29.85 ? 346  LYS A N     1 
ATOM   2666 C CA    . LYS A 1 346 ? -1.749  124.600 40.634 1.00 30.18 ? 346  LYS A CA    1 
ATOM   2667 C C     . LYS A 1 346 ? -1.382  123.947 41.967 1.00 29.58 ? 346  LYS A C     1 
ATOM   2668 O O     . LYS A 1 346 ? -1.587  122.736 42.070 1.00 27.32 ? 346  LYS A O     1 
ATOM   2669 C CB    . LYS A 1 346 ? -3.201  125.084 40.674 1.00 34.31 ? 346  LYS A CB    1 
ATOM   2670 C CG    . LYS A 1 346 ? -3.632  125.885 39.453 1.00 40.71 ? 346  LYS A CG    1 
ATOM   2671 C CD    . LYS A 1 346 ? -5.125  125.977 39.277 1.00 49.36 ? 346  LYS A CD    1 
ATOM   2672 C CE    . LYS A 1 346 ? -5.509  126.825 38.078 1.00 57.07 ? 346  LYS A CE    1 
ATOM   2673 N NZ    . LYS A 1 346 ? -5.414  126.042 36.817 1.00 65.13 ? 346  LYS A NZ    1 
ATOM   2674 N N     . PHE A 1 347 ? -0.762  124.719 42.856 1.00 27.75 ? 347  PHE A N     1 
ATOM   2675 C CA    . PHE A 1 347 ? -0.231  124.308 44.173 1.00 28.84 ? 347  PHE A CA    1 
ATOM   2676 C C     . PHE A 1 347 ? -1.063  125.010 45.242 1.00 32.10 ? 347  PHE A C     1 
ATOM   2677 O O     . PHE A 1 347 ? -1.376  126.197 45.089 1.00 32.80 ? 347  PHE A O     1 
ATOM   2678 C CB    . PHE A 1 347 ? 1.233   124.686 44.312 1.00 28.29 ? 347  PHE A CB    1 
ATOM   2679 C CG    . PHE A 1 347 ? 2.141   124.055 43.285 1.00 32.31 ? 347  PHE A CG    1 
ATOM   2680 C CD1   . PHE A 1 347 ? 2.740   122.815 43.523 1.00 30.60 ? 347  PHE A CD1   1 
ATOM   2681 C CD2   . PHE A 1 347 ? 2.417   124.693 42.079 1.00 32.50 ? 347  PHE A CD2   1 
ATOM   2682 C CE1   . PHE A 1 347 ? 3.558   122.223 42.569 1.00 30.53 ? 347  PHE A CE1   1 
ATOM   2683 C CE2   . PHE A 1 347 ? 3.243   124.100 41.131 1.00 34.08 ? 347  PHE A CE2   1 
ATOM   2684 C CZ    . PHE A 1 347 ? 3.821   122.869 41.376 1.00 30.28 ? 347  PHE A CZ    1 
ATOM   2685 N N     . TYR A 1 348 ? -1.438  124.288 46.284 1.00 27.48 ? 348  TYR A N     1 
ATOM   2686 C CA    . TYR A 1 348 ? -2.301  124.795 47.375 1.00 27.05 ? 348  TYR A CA    1 
ATOM   2687 C C     . TYR A 1 348 ? -1.826  124.218 48.705 1.00 30.21 ? 348  TYR A C     1 
ATOM   2688 O O     . TYR A 1 348 ? -1.567  122.992 48.828 1.00 27.70 ? 348  TYR A O     1 
ATOM   2689 C CB    . TYR A 1 348 ? -3.757  124.374 47.194 1.00 26.54 ? 348  TYR A CB    1 
ATOM   2690 C CG    . TYR A 1 348 ? -4.464  124.800 45.930 1.00 27.26 ? 348  TYR A CG    1 
ATOM   2691 C CD1   . TYR A 1 348 ? -4.494  123.962 44.836 1.00 26.03 ? 348  TYR A CD1   1 
ATOM   2692 C CD2   . TYR A 1 348 ? -5.180  125.995 45.849 1.00 30.91 ? 348  TYR A CD2   1 
ATOM   2693 C CE1   . TYR A 1 348 ? -5.173  124.301 43.680 1.00 25.65 ? 348  TYR A CE1   1 
ATOM   2694 C CE2   . TYR A 1 348 ? -5.870  126.355 44.695 1.00 30.85 ? 348  TYR A CE2   1 
ATOM   2695 C CZ    . TYR A 1 348 ? -5.861  125.506 43.608 1.00 28.97 ? 348  TYR A CZ    1 
ATOM   2696 O OH    . TYR A 1 348 ? -6.549  125.772 42.464 1.00 28.49 ? 348  TYR A OH    1 
ATOM   2697 N N     . PHE A 1 349 ? -1.671  125.100 49.679 1.00 28.53 ? 349  PHE A N     1 
ATOM   2698 C CA    . PHE A 1 349 ? -1.717  124.737 51.115 1.00 29.84 ? 349  PHE A CA    1 
ATOM   2699 C C     . PHE A 1 349 ? -3.110  125.087 51.626 1.00 30.55 ? 349  PHE A C     1 
ATOM   2700 O O     . PHE A 1 349 ? -3.867  125.745 50.923 1.00 30.25 ? 349  PHE A O     1 
ATOM   2701 C CB    . PHE A 1 349 ? -0.552  125.387 51.846 1.00 30.83 ? 349  PHE A CB    1 
ATOM   2702 C CG    . PHE A 1 349 ? 0.771   124.826 51.394 1.00 36.13 ? 349  PHE A CG    1 
ATOM   2703 C CD1   . PHE A 1 349 ? 1.290   123.683 51.974 1.00 40.29 ? 349  PHE A CD1   1 
ATOM   2704 C CD2   . PHE A 1 349 ? 1.469   125.400 50.339 1.00 43.54 ? 349  PHE A CD2   1 
ATOM   2705 C CE1   . PHE A 1 349 ? 2.491   123.148 51.534 1.00 39.78 ? 349  PHE A CE1   1 
ATOM   2706 C CE2   . PHE A 1 349 ? 2.665   124.849 49.894 1.00 42.89 ? 349  PHE A CE2   1 
ATOM   2707 C CZ    . PHE A 1 349 ? 3.159   123.723 50.487 1.00 37.17 ? 349  PHE A CZ    1 
ATOM   2708 N N     . PRO A 1 350 ? -3.489  124.641 52.840 1.00 30.82 ? 350  PRO A N     1 
ATOM   2709 C CA    . PRO A 1 350 ? -4.840  124.861 53.360 1.00 34.61 ? 350  PRO A CA    1 
ATOM   2710 C C     . PRO A 1 350 ? -5.301  126.337 53.328 1.00 33.18 ? 350  PRO A C     1 
ATOM   2711 O O     . PRO A 1 350 ? -6.417  126.537 52.920 1.00 31.02 ? 350  PRO A O     1 
ATOM   2712 C CB    . PRO A 1 350 ? -4.686  124.363 54.805 1.00 31.91 ? 350  PRO A CB    1 
ATOM   2713 C CG    . PRO A 1 350 ? -3.707  123.221 54.645 1.00 36.11 ? 350  PRO A CG    1 
ATOM   2714 C CD    . PRO A 1 350 ? -2.652  123.870 53.771 1.00 34.07 ? 350  PRO A CD    1 
ATOM   2715 N N     . GLU A 1 351 ? -4.403  127.279 53.670 1.00 29.89 ? 351  GLU A N     1 
ATOM   2716 C CA    . GLU A 1 351 ? -4.651  128.738 53.693 1.00 37.31 ? 351  GLU A CA    1 
ATOM   2717 C C     . GLU A 1 351 ? -4.988  129.227 52.287 1.00 41.16 ? 351  GLU A C     1 
ATOM   2718 O O     . GLU A 1 351 ? -5.499  130.319 52.199 1.00 40.24 ? 351  GLU A O     1 
ATOM   2719 C CB    . GLU A 1 351 ? -3.473  129.529 54.279 1.00 37.42 ? 351  GLU A CB    1 
ATOM   2720 C CG    . GLU A 1 351 ? -2.143  129.347 53.550 1.00 43.12 ? 351  GLU A CG    1 
ATOM   2721 C CD    . GLU A 1 351 ? -1.249  128.222 54.066 1.00 41.78 ? 351  GLU A CD    1 
ATOM   2722 O OE1   . GLU A 1 351 ? -1.794  127.222 54.660 1.00 39.43 ? 351  GLU A OE1   1 
ATOM   2723 O OE2   . GLU A 1 351 ? 0.001   128.348 53.905 1.00 43.51 ? 351  GLU A OE2   1 
ATOM   2724 N N     . ASP A 1 352 ? -4.717  128.459 51.229 1.00 34.96 ? 352  ASP A N     1 
ATOM   2725 C CA    . ASP A 1 352 ? -4.948  128.916 49.842 1.00 35.16 ? 352  ASP A CA    1 
ATOM   2726 C C     . ASP A 1 352 ? -6.285  128.408 49.336 1.00 34.37 ? 352  ASP A C     1 
ATOM   2727 O O     . ASP A 1 352 ? -6.588  128.679 48.182 1.00 35.36 ? 352  ASP A O     1 
ATOM   2728 C CB    . ASP A 1 352 ? -3.881  128.418 48.868 1.00 37.61 ? 352  ASP A CB    1 
ATOM   2729 C CG    . ASP A 1 352 ? -2.486  128.825 49.270 1.00 34.33 ? 352  ASP A CG    1 
ATOM   2730 O OD1   . ASP A 1 352 ? -2.289  130.017 49.522 1.00 40.07 ? 352  ASP A OD1   1 
ATOM   2731 O OD2   . ASP A 1 352 ? -1.624  127.934 49.396 1.00 36.04 ? 352  ASP A OD2   1 
ATOM   2732 N N     . ARG A 1 353 ? -7.031  127.642 50.124 1.00 28.60 ? 353  ARG A N     1 
ATOM   2733 C CA    . ARG A 1 353 ? -8.292  127.048 49.631 1.00 31.11 ? 353  ARG A CA    1 
ATOM   2734 C C     . ARG A 1 353 ? -9.408  128.054 49.895 1.00 33.92 ? 353  ARG A C     1 
ATOM   2735 O O     . ARG A 1 353 ? -9.456  128.589 51.018 1.00 34.01 ? 353  ARG A O     1 
ATOM   2736 C CB    . ARG A 1 353 ? -8.567  125.687 50.284 1.00 30.89 ? 353  ARG A CB    1 
ATOM   2737 C CG    . ARG A 1 353 ? -7.455  124.664 50.015 1.00 29.56 ? 353  ARG A CG    1 
ATOM   2738 C CD    . ARG A 1 353 ? -7.327  124.260 48.571 1.00 26.53 ? 353  ARG A CD    1 
ATOM   2739 N NE    . ARG A 1 353 ? -8.484  123.536 48.090 1.00 26.66 ? 353  ARG A NE    1 
ATOM   2740 C CZ    . ARG A 1 353 ? -8.745  123.260 46.832 1.00 28.04 ? 353  ARG A CZ    1 
ATOM   2741 N NH1   . ARG A 1 353 ? -7.932  123.660 45.863 1.00 30.94 ? 353  ARG A NH1   1 
ATOM   2742 N NH2   . ARG A 1 353 ? -9.846  122.595 46.531 1.00 28.84 ? 353  ARG A NH2   1 
ATOM   2743 N N     . ARG A 1 354 ? -10.261 128.315 48.917 1.00 34.33 ? 354  ARG A N     1 
ATOM   2744 C CA    . ARG A 1 354 ? -11.266 129.390 49.120 1.00 40.73 ? 354  ARG A CA    1 
ATOM   2745 C C     . ARG A 1 354 ? -12.554 128.789 49.697 1.00 39.69 ? 354  ARG A C     1 
ATOM   2746 O O     . ARG A 1 354 ? -13.283 129.534 50.287 1.00 36.35 ? 354  ARG A O     1 
ATOM   2747 C CB    . ARG A 1 354 ? -11.406 130.276 47.885 1.00 39.06 ? 354  ARG A CB    1 
ATOM   2748 C CG    . ARG A 1 354 ? -11.835 129.592 46.609 1.00 44.58 ? 354  ARG A CG    1 
ATOM   2749 C CD    . ARG A 1 354 ? -11.615 130.481 45.370 1.00 41.38 ? 354  ARG A CD    1 
ATOM   2750 N NE    . ARG A 1 354 ? -11.885 129.594 44.252 1.00 41.08 ? 354  ARG A NE    1 
ATOM   2751 C CZ    . ARG A 1 354 ? -13.091 129.225 43.840 1.00 46.89 ? 354  ARG A CZ    1 
ATOM   2752 N NH1   . ARG A 1 354 ? -14.188 129.746 44.383 1.00 48.53 ? 354  ARG A NH1   1 
ATOM   2753 N NH2   . ARG A 1 354 ? -13.203 128.354 42.848 1.00 46.69 ? 354  ARG A NH2   1 
ATOM   2754 N N     . HIS A 1 355 ? -12.789 127.483 49.632 1.00 33.03 ? 355  HIS A N     1 
ATOM   2755 C CA    . HIS A 1 355 ? -14.029 126.893 50.183 1.00 31.94 ? 355  HIS A CA    1 
ATOM   2756 C C     . HIS A 1 355 ? -13.802 126.504 51.649 1.00 34.83 ? 355  HIS A C     1 
ATOM   2757 O O     . HIS A 1 355 ? -12.703 126.018 52.008 1.00 34.43 ? 355  HIS A O     1 
ATOM   2758 C CB    . HIS A 1 355 ? -14.487 125.728 49.320 1.00 36.71 ? 355  HIS A CB    1 
ATOM   2759 C CG    . HIS A 1 355 ? -14.879 126.055 47.922 1.00 41.11 ? 355  HIS A CG    1 
ATOM   2760 N ND1   . HIS A 1 355 ? -16.186 126.278 47.561 1.00 47.51 ? 355  HIS A ND1   1 
ATOM   2761 C CD2   . HIS A 1 355 ? -14.171 126.074 46.771 1.00 41.96 ? 355  HIS A CD2   1 
ATOM   2762 C CE1   . HIS A 1 355 ? -16.263 126.455 46.259 1.00 44.05 ? 355  HIS A CE1   1 
ATOM   2763 N NE2   . HIS A 1 355 ? -15.044 126.353 45.762 1.00 42.27 ? 355  HIS A NE2   1 
ATOM   2764 N N     . LYS A 1 356 ? -14.793 126.717 52.500 1.00 38.28 ? 356  LYS A N     1 
ATOM   2765 C CA    . LYS A 1 356 ? -14.674 126.408 53.947 1.00 39.76 ? 356  LYS A CA    1 
ATOM   2766 C C     . LYS A 1 356 ? -14.805 124.888 54.106 1.00 36.70 ? 356  LYS A C     1 
ATOM   2767 O O     . LYS A 1 356 ? -14.139 124.316 54.960 1.00 36.27 ? 356  LYS A O     1 
ATOM   2768 C CB    . LYS A 1 356 ? -15.736 127.205 54.700 1.00 47.37 ? 356  LYS A CB    1 
ATOM   2769 C CG    . LYS A 1 356 ? -15.830 126.902 56.180 1.00 57.48 ? 356  LYS A CG    1 
ATOM   2770 C CD    . LYS A 1 356 ? -17.253 127.010 56.678 1.00 65.98 ? 356  LYS A CD    1 
ATOM   2771 C CE    . LYS A 1 356 ? -17.480 126.298 57.994 1.00 68.59 ? 356  LYS A CE    1 
ATOM   2772 N NZ    . LYS A 1 356 ? -18.531 127.002 58.763 1.00 70.59 ? 356  LYS A NZ    1 
ATOM   2773 N N     . VAL A 1 357 ? -15.631 124.265 53.271 1.00 31.18 ? 357  VAL A N     1 
ATOM   2774 C CA    . VAL A 1 357 ? -15.823 122.799 53.215 1.00 32.93 ? 357  VAL A CA    1 
ATOM   2775 C C     . VAL A 1 357 ? -15.164 122.319 51.916 1.00 34.50 ? 357  VAL A C     1 
ATOM   2776 O O     . VAL A 1 357 ? -15.651 122.635 50.824 1.00 31.81 ? 357  VAL A O     1 
ATOM   2777 C CB    . VAL A 1 357 ? -17.309 122.425 53.308 1.00 36.35 ? 357  VAL A CB    1 
ATOM   2778 C CG1   . VAL A 1 357 ? -17.483 120.910 53.290 1.00 36.95 ? 357  VAL A CG1   1 
ATOM   2779 C CG2   . VAL A 1 357 ? -17.950 123.066 54.554 1.00 33.96 ? 357  VAL A CG2   1 
ATOM   2780 N N     . ASP A 1 358 ? -14.063 121.594 52.050 1.00 31.19 ? 358  ASP A N     1 
ATOM   2781 C CA    . ASP A 1 358 ? -13.057 121.470 50.962 1.00 29.70 ? 358  ASP A CA    1 
ATOM   2782 C C     . ASP A 1 358 ? -12.270 120.164 51.095 1.00 29.31 ? 358  ASP A C     1 
ATOM   2783 O O     . ASP A 1 358 ? -11.935 119.755 52.245 1.00 25.41 ? 358  ASP A O     1 
ATOM   2784 C CB    . ASP A 1 358 ? -12.107 122.653 51.011 1.00 29.98 ? 358  ASP A CB    1 
ATOM   2785 C CG    . ASP A 1 358 ? -11.103 122.630 49.876 1.00 30.58 ? 358  ASP A CG    1 
ATOM   2786 O OD1   . ASP A 1 358 ? -11.524 122.864 48.729 1.00 30.40 ? 358  ASP A OD1   1 
ATOM   2787 O OD2   . ASP A 1 358 ? -9.908  122.366 50.176 1.00 29.94 ? 358  ASP A OD2   1 
ATOM   2788 N N     . LEU A 1 359 ? -11.907 119.608 49.952 1.00 29.22 ? 359  LEU A N     1 
ATOM   2789 C CA    . LEU A 1 359 ? -11.162 118.344 49.888 1.00 28.97 ? 359  LEU A CA    1 
ATOM   2790 C C     . LEU A 1 359 ? -9.869  118.413 50.694 1.00 24.80 ? 359  LEU A C     1 
ATOM   2791 O O     . LEU A 1 359 ? -9.629  117.506 51.494 1.00 28.60 ? 359  LEU A O     1 
ATOM   2792 C CB    . LEU A 1 359 ? -10.833 117.976 48.448 1.00 32.71 ? 359  LEU A CB    1 
ATOM   2793 C CG    . LEU A 1 359 ? -10.014 116.703 48.436 1.00 37.69 ? 359  LEU A CG    1 
ATOM   2794 C CD1   . LEU A 1 359 ? -10.963 115.533 48.558 1.00 37.06 ? 359  LEU A CD1   1 
ATOM   2795 C CD2   . LEU A 1 359 ? -9.084  116.641 47.264 1.00 52.47 ? 359  LEU A CD2   1 
ATOM   2796 N N     . LEU A 1 360 ? -9.018  119.402 50.463 1.00 24.34 ? 360  LEU A N     1 
ATOM   2797 C CA    . LEU A 1 360 ? -7.733  119.505 51.181 1.00 24.58 ? 360  LEU A CA    1 
ATOM   2798 C C     . LEU A 1 360 ? -7.960  119.662 52.678 1.00 24.54 ? 360  LEU A C     1 
ATOM   2799 O O     . LEU A 1 360 ? -7.219  119.010 53.452 1.00 23.67 ? 360  LEU A O     1 
ATOM   2800 C CB    . LEU A 1 360 ? -6.884  120.649 50.626 1.00 26.35 ? 360  LEU A CB    1 
ATOM   2801 C CG    . LEU A 1 360 ? -5.538  120.863 51.328 1.00 27.17 ? 360  LEU A CG    1 
ATOM   2802 C CD1   . LEU A 1 360 ? -4.716  119.570 51.380 1.00 27.61 ? 360  LEU A CD1   1 
ATOM   2803 C CD2   . LEU A 1 360 ? -4.729  121.962 50.641 1.00 28.84 ? 360  LEU A CD2   1 
ATOM   2804 N N     . LEU A 1 361 ? -8.915  120.496 53.105 1.00 23.21 ? 361  LEU A N     1 
ATOM   2805 C CA    . LEU A 1 361 ? -9.101  120.725 54.558 1.00 25.89 ? 361  LEU A CA    1 
ATOM   2806 C C     . LEU A 1 361 ? -9.558  119.390 55.178 1.00 24.21 ? 361  LEU A C     1 
ATOM   2807 O O     . LEU A 1 361 ? -9.190  119.108 56.298 1.00 24.83 ? 361  LEU A O     1 
ATOM   2808 C CB    . LEU A 1 361 ? -10.097 121.865 54.798 1.00 28.87 ? 361  LEU A CB    1 
ATOM   2809 C CG    . LEU A 1 361 ? -9.670  123.212 54.232 1.00 34.23 ? 361  LEU A CG    1 
ATOM   2810 C CD1   . LEU A 1 361 ? -10.606 124.319 54.689 1.00 39.75 ? 361  LEU A CD1   1 
ATOM   2811 C CD2   . LEU A 1 361 ? -8.235  123.542 54.605 1.00 36.48 ? 361  LEU A CD2   1 
ATOM   2812 N N     . HIS A 1 362 ? -10.289 118.572 54.432 1.00 26.08 ? 362  HIS A N     1 
ATOM   2813 C CA    . HIS A 1 362 ? -10.706 117.234 54.912 1.00 27.89 ? 362  HIS A CA    1 
ATOM   2814 C C     . HIS A 1 362 ? -9.477  116.295 54.980 1.00 26.64 ? 362  HIS A C     1 
ATOM   2815 O O     . HIS A 1 362 ? -9.156  115.798 56.054 1.00 23.46 ? 362  HIS A O     1 
ATOM   2816 C CB    . HIS A 1 362 ? -11.828 116.655 54.054 1.00 29.69 ? 362  HIS A CB    1 
ATOM   2817 C CG    . HIS A 1 362 ? -11.922 115.224 54.384 1.00 35.88 ? 362  HIS A CG    1 
ATOM   2818 N ND1   . HIS A 1 362 ? -11.740 114.226 53.433 1.00 41.73 ? 362  HIS A ND1   1 
ATOM   2819 C CD2   . HIS A 1 362 ? -12.004 114.624 55.602 1.00 37.00 ? 362  HIS A CD2   1 
ATOM   2820 C CE1   . HIS A 1 362 ? -11.772 113.055 54.068 1.00 37.34 ? 362  HIS A CE1   1 
ATOM   2821 N NE2   . HIS A 1 362 ? -11.923 113.273 55.400 1.00 40.66 ? 362  HIS A NE2   1 
ATOM   2822 N N     . ARG A 1 363 ? -8.714  116.155 53.898 1.00 23.41 ? 363  ARG A N     1 
ATOM   2823 C CA    . ARG A 1 363 ? -7.608  115.152 53.857 1.00 24.31 ? 363  ARG A CA    1 
ATOM   2824 C C     . ARG A 1 363 ? -6.429  115.583 54.728 1.00 23.82 ? 363  ARG A C     1 
ATOM   2825 O O     . ARG A 1 363 ? -5.646  114.674 55.174 1.00 22.32 ? 363  ARG A O     1 
ATOM   2826 C CB    . ARG A 1 363 ? -7.218  114.863 52.405 1.00 26.83 ? 363  ARG A CB    1 
ATOM   2827 C CG    . ARG A 1 363 ? -8.360  114.222 51.627 1.00 26.21 ? 363  ARG A CG    1 
ATOM   2828 C CD    . ARG A 1 363 ? -7.921  113.360 50.463 1.00 29.13 ? 363  ARG A CD    1 
ATOM   2829 N NE    . ARG A 1 363 ? -7.114  112.214 50.886 1.00 28.98 ? 363  ARG A NE    1 
ATOM   2830 C CZ    . ARG A 1 363 ? -7.577  111.058 51.343 1.00 29.73 ? 363  ARG A CZ    1 
ATOM   2831 N NH1   . ARG A 1 363 ? -8.875  110.814 51.401 1.00 31.35 ? 363  ARG A NH1   1 
ATOM   2832 N NH2   . ARG A 1 363 ? -6.728  110.113 51.707 1.00 35.79 ? 363  ARG A NH2   1 
ATOM   2833 N N     . ALA A 1 364 ? -6.303  116.872 55.045 1.00 21.70 ? 364  ALA A N     1 
ATOM   2834 C CA    . ALA A 1 364 ? -5.323  117.349 56.038 1.00 24.39 ? 364  ALA A CA    1 
ATOM   2835 C C     . ALA A 1 364 ? -5.515  116.612 57.375 1.00 24.04 ? 364  ALA A C     1 
ATOM   2836 O O     . ALA A 1 364 ? -4.532  116.475 58.129 1.00 23.87 ? 364  ALA A O     1 
ATOM   2837 C CB    . ALA A 1 364 ? -5.472  118.825 56.269 1.00 27.89 ? 364  ALA A CB    1 
ATOM   2838 N N     . GLU A 1 365 ? -6.746  116.243 57.704 1.00 23.67 ? 365  GLU A N     1 
ATOM   2839 C CA    . GLU A 1 365 ? -7.026  115.480 58.954 1.00 25.22 ? 365  GLU A CA    1 
ATOM   2840 C C     . GLU A 1 365 ? -6.596  114.010 58.763 1.00 23.21 ? 365  GLU A C     1 
ATOM   2841 O O     . GLU A 1 365 ? -5.895  113.486 59.607 1.00 20.52 ? 365  GLU A O     1 
ATOM   2842 C CB    . GLU A 1 365 ? -8.478  115.693 59.347 1.00 28.08 ? 365  GLU A CB    1 
ATOM   2843 C CG    . GLU A 1 365 ? -8.731  117.143 59.780 1.00 34.24 ? 365  GLU A CG    1 
ATOM   2844 C CD    . GLU A 1 365 ? -9.881  117.164 60.747 1.00 45.15 ? 365  GLU A CD    1 
ATOM   2845 O OE1   . GLU A 1 365 ? -9.613  117.037 61.941 1.00 54.74 ? 365  GLU A OE1   1 
ATOM   2846 O OE2   . GLU A 1 365 ? -11.031 117.174 60.282 1.00 50.86 ? 365  GLU A OE2   1 
ATOM   2847 N N     . THR A 1 366 ? -6.997  113.398 57.665 1.00 21.05 ? 366  THR A N     1 
ATOM   2848 C CA    . THR A 1 366 ? -6.694  111.993 57.325 1.00 22.08 ? 366  THR A CA    1 
ATOM   2849 C C     . THR A 1 366 ? -5.173  111.775 57.350 1.00 23.20 ? 366  THR A C     1 
ATOM   2850 O O     . THR A 1 366 ? -4.706  110.790 57.926 1.00 22.13 ? 366  THR A O     1 
ATOM   2851 C CB    . THR A 1 366 ? -7.316  111.679 55.966 1.00 25.30 ? 366  THR A CB    1 
ATOM   2852 O OG1   . THR A 1 366 ? -8.669  112.175 55.968 1.00 27.08 ? 366  THR A OG1   1 
ATOM   2853 C CG2   . THR A 1 366 ? -7.240  110.208 55.654 1.00 24.77 ? 366  THR A CG2   1 
ATOM   2854 N N     . MET A 1 367 ? -4.415  112.706 56.771 1.00 21.57 ? 367  MET A N     1 
ATOM   2855 C CA    . MET A 1 367 ? -2.953  112.529 56.636 1.00 22.53 ? 367  MET A CA    1 
ATOM   2856 C C     . MET A 1 367 ? -2.250  112.822 57.956 1.00 19.82 ? 367  MET A C     1 
ATOM   2857 O O     . MET A 1 367 ? -1.009  112.638 58.018 1.00 20.64 ? 367  MET A O     1 
ATOM   2858 C CB    . MET A 1 367 ? -2.417  113.352 55.460 1.00 19.47 ? 367  MET A CB    1 
ATOM   2859 C CG    . MET A 1 367 ? -2.976  112.862 54.163 1.00 19.96 ? 367  MET A CG    1 
ATOM   2860 S SD    . MET A 1 367 ? -2.288  113.775 52.729 1.00 22.97 ? 367  MET A SD    1 
ATOM   2861 C CE    . MET A 1 367 ? -2.916  115.434 53.022 1.00 26.41 ? 367  MET A CE    1 
ATOM   2862 N N     . LYS A 1 368 ? -2.957  113.239 59.018 1.00 21.99 ? 368  LYS A N     1 
ATOM   2863 C CA    . LYS A 1 368 ? -2.315  113.158 60.350 1.00 20.66 ? 368  LYS A CA    1 
ATOM   2864 C C     . LYS A 1 368 ? -3.048  112.156 61.244 1.00 20.52 ? 368  LYS A C     1 
ATOM   2865 O O     . LYS A 1 368 ? -2.848  112.201 62.460 1.00 20.42 ? 368  LYS A O     1 
ATOM   2866 C CB    . LYS A 1 368 ? -2.149  114.517 61.017 1.00 24.60 ? 368  LYS A CB    1 
ATOM   2867 C CG    . LYS A 1 368 ? -3.447  115.224 61.251 1.00 27.34 ? 368  LYS A CG    1 
ATOM   2868 C CD    . LYS A 1 368 ? -3.237  116.603 61.876 1.00 34.16 ? 368  LYS A CD    1 
ATOM   2869 C CE    . LYS A 1 368 ? -4.508  117.427 61.775 1.00 42.70 ? 368  LYS A CE    1 
ATOM   2870 N NZ    . LYS A 1 368 ? -4.525  118.552 62.742 1.00 52.03 ? 368  LYS A NZ    1 
ATOM   2871 N N     . GLY A 1 369 ? -3.750  111.205 60.654 1.00 21.42 ? 369  GLY A N     1 
ATOM   2872 C CA    . GLY A 1 369 ? -4.320  110.065 61.389 1.00 18.77 ? 369  GLY A CA    1 
ATOM   2873 C C     . GLY A 1 369 ? -5.536  110.426 62.233 1.00 19.12 ? 369  GLY A C     1 
ATOM   2874 O O     . GLY A 1 369 ? -5.720  109.795 63.316 1.00 20.11 ? 369  GLY A O     1 
ATOM   2875 N N     . VAL A 1 370 ? -6.341  111.399 61.805 1.00 20.49 ? 370  VAL A N     1 
ATOM   2876 C CA    . VAL A 1 370 ? -7.609  111.745 62.517 1.00 20.45 ? 370  VAL A CA    1 
ATOM   2877 C C     . VAL A 1 370 ? -8.724  110.901 61.934 1.00 20.99 ? 370  VAL A C     1 
ATOM   2878 O O     . VAL A 1 370 ? -9.017  110.996 60.755 1.00 21.76 ? 370  VAL A O     1 
ATOM   2879 C CB    . VAL A 1 370 ? -7.901  113.250 62.485 1.00 20.91 ? 370  VAL A CB    1 
ATOM   2880 C CG1   . VAL A 1 370 ? -9.218  113.565 63.224 1.00 23.22 ? 370  VAL A CG1   1 
ATOM   2881 C CG2   . VAL A 1 370 ? -6.730  114.021 63.075 1.00 22.40 ? 370  VAL A CG2   1 
ATOM   2882 N N     . PRO A 1 371 ? -9.334  109.970 62.697 1.00 19.03 ? 371  PRO A N     1 
ATOM   2883 C CA    . PRO A 1 371 ? -10.371 109.122 62.143 1.00 21.07 ? 371  PRO A CA    1 
ATOM   2884 C C     . PRO A 1 371 ? -11.660 109.930 61.883 1.00 22.27 ? 371  PRO A C     1 
ATOM   2885 O O     . PRO A 1 371 ? -12.017 110.737 62.730 1.00 20.35 ? 371  PRO A O     1 
ATOM   2886 C CB    . PRO A 1 371 ? -10.613 108.053 63.222 1.00 21.02 ? 371  PRO A CB    1 
ATOM   2887 C CG    . PRO A 1 371 ? -10.159 108.709 64.492 1.00 21.37 ? 371  PRO A CG    1 
ATOM   2888 C CD    . PRO A 1 371 ? -9.066  109.678 64.099 1.00 20.62 ? 371  PRO A CD    1 
ATOM   2889 N N     . LYS A 1 372 ? -12.329 109.645 60.768 1.00 21.44 ? 372  LYS A N     1 
ATOM   2890 C CA    . LYS A 1 372 ? -13.549 110.357 60.329 1.00 24.83 ? 372  LYS A CA    1 
ATOM   2891 C C     . LYS A 1 372 ? -14.472 109.379 59.597 1.00 24.82 ? 372  LYS A C     1 
ATOM   2892 O O     . LYS A 1 372 ? -14.035 108.270 59.277 1.00 23.37 ? 372  LYS A O     1 
ATOM   2893 C CB    . LYS A 1 372 ? -13.158 111.535 59.421 1.00 25.98 ? 372  LYS A CB    1 
ATOM   2894 C CG    . LYS A 1 372 ? -12.326 112.601 60.113 1.00 28.07 ? 372  LYS A CG    1 
ATOM   2895 C CD    . LYS A 1 372 ? -12.097 113.806 59.279 1.00 33.11 ? 372  LYS A CD    1 
ATOM   2896 C CE    . LYS A 1 372 ? -13.284 114.745 59.218 1.00 38.26 ? 372  LYS A CE    1 
ATOM   2897 N NZ    . LYS A 1 372 ? -13.080 115.806 58.195 1.00 36.19 ? 372  LYS A NZ    1 
ATOM   2898 N N     . LEU A 1 373 ? -15.674 109.827 59.238 1.00 21.21 ? 373  LEU A N     1 
ATOM   2899 C CA    . LEU A 1 373 ? -16.638 109.044 58.437 1.00 22.91 ? 373  LEU A CA    1 
ATOM   2900 C C     . LEU A 1 373 ? -17.119 109.857 57.220 1.00 25.57 ? 373  LEU A C     1 
ATOM   2901 O O     . LEU A 1 373 ? -18.112 109.463 56.573 1.00 26.85 ? 373  LEU A O     1 
ATOM   2902 C CB    . LEU A 1 373 ? -17.782 108.613 59.353 1.00 25.52 ? 373  LEU A CB    1 
ATOM   2903 C CG    . LEU A 1 373 ? -17.434 107.646 60.477 1.00 23.87 ? 373  LEU A CG    1 
ATOM   2904 C CD1   . LEU A 1 373 ? -18.631 107.461 61.387 1.00 25.74 ? 373  LEU A CD1   1 
ATOM   2905 C CD2   . LEU A 1 373 ? -17.004 106.315 59.924 1.00 23.67 ? 373  LEU A CD2   1 
ATOM   2906 N N     . THR A 1 374 ? -16.358 110.857 56.802 1.00 24.66 ? 374  THR A N     1 
ATOM   2907 C CA    . THR A 1 374 ? -16.802 111.759 55.720 1.00 27.57 ? 374  THR A CA    1 
ATOM   2908 C C     . THR A 1 374 ? -16.635 111.131 54.341 1.00 28.75 ? 374  THR A C     1 
ATOM   2909 O O     . THR A 1 374 ? -17.318 111.591 53.404 1.00 24.84 ? 374  THR A O     1 
ATOM   2910 C CB    . THR A 1 374 ? -16.139 113.117 55.906 1.00 31.33 ? 374  THR A CB    1 
ATOM   2911 O OG1   . THR A 1 374 ? -14.767 112.906 56.005 1.00 37.89 ? 374  THR A OG1   1 
ATOM   2912 C CG2   . THR A 1 374 ? -16.570 113.823 57.167 1.00 36.22 ? 374  THR A CG2   1 
ATOM   2913 N N     . GLU A 1 375 ? -15.829 110.075 54.189 1.00 24.86 ? 375  GLU A N     1 
ATOM   2914 C CA    . GLU A 1 375 ? -15.567 109.527 52.846 1.00 24.12 ? 375  GLU A CA    1 
ATOM   2915 C C     . GLU A 1 375 ? -16.826 108.920 52.226 1.00 22.58 ? 375  GLU A C     1 
ATOM   2916 O O     . GLU A 1 375 ? -16.897 108.884 51.004 1.00 23.26 ? 375  GLU A O     1 
ATOM   2917 C CB    . GLU A 1 375 ? -14.398 108.541 52.897 1.00 26.68 ? 375  GLU A CB    1 
ATOM   2918 C CG    . GLU A 1 375 ? -13.774 108.370 51.548 1.00 27.86 ? 375  GLU A CG    1 
ATOM   2919 C CD    . GLU A 1 375 ? -13.082 109.567 50.913 1.00 29.91 ? 375  GLU A CD    1 
ATOM   2920 O OE1   . GLU A 1 375 ? -12.631 110.455 51.648 1.00 29.79 ? 375  GLU A OE1   1 
ATOM   2921 O OE2   . GLU A 1 375 ? -12.930 109.539 49.642 1.00 30.76 ? 375  GLU A OE2   1 
ATOM   2922 N N     . PHE A 1 376 ? -17.821 108.509 53.009 1.00 21.57 ? 376  PHE A N     1 
ATOM   2923 C CA    . PHE A 1 376 ? -19.113 107.986 52.529 1.00 22.13 ? 376  PHE A CA    1 
ATOM   2924 C C     . PHE A 1 376 ? -19.845 109.053 51.714 1.00 22.29 ? 376  PHE A C     1 
ATOM   2925 O O     . PHE A 1 376 ? -20.725 108.676 50.953 1.00 23.43 ? 376  PHE A O     1 
ATOM   2926 C CB    . PHE A 1 376 ? -19.984 107.492 53.676 1.00 25.49 ? 376  PHE A CB    1 
ATOM   2927 C CG    . PHE A 1 376 ? -19.587 106.173 54.268 1.00 25.25 ? 376  PHE A CG    1 
ATOM   2928 C CD1   . PHE A 1 376 ? -19.458 105.043 53.470 1.00 23.39 ? 376  PHE A CD1   1 
ATOM   2929 C CD2   . PHE A 1 376 ? -19.404 106.047 55.641 1.00 24.53 ? 376  PHE A CD2   1 
ATOM   2930 C CE1   . PHE A 1 376 ? -19.112 103.825 54.026 1.00 24.58 ? 376  PHE A CE1   1 
ATOM   2931 C CE2   . PHE A 1 376 ? -19.061 104.820 56.196 1.00 27.11 ? 376  PHE A CE2   1 
ATOM   2932 C CZ    . PHE A 1 376 ? -18.921 103.710 55.385 1.00 27.74 ? 376  PHE A CZ    1 
ATOM   2933 N N     . ASN A 1 377 ? -19.425 110.307 51.814 1.00 21.24 ? 377  ASN A N     1 
ATOM   2934 C CA    . ASN A 1 377 ? -20.057 111.403 51.066 1.00 23.70 ? 377  ASN A CA    1 
ATOM   2935 C C     . ASN A 1 377 ? -20.073 111.058 49.572 1.00 28.59 ? 377  ASN A C     1 
ATOM   2936 O O     . ASN A 1 377 ? -21.013 111.496 48.888 1.00 23.55 ? 377  ASN A O     1 
ATOM   2937 C CB    . ASN A 1 377 ? -19.349 112.728 51.304 1.00 23.66 ? 377  ASN A CB    1 
ATOM   2938 C CG    . ASN A 1 377 ? -19.663 113.329 52.657 1.00 25.24 ? 377  ASN A CG    1 
ATOM   2939 O OD1   . ASN A 1 377 ? -20.339 112.720 53.501 1.00 25.27 ? 377  ASN A OD1   1 
ATOM   2940 N ND2   . ASN A 1 377 ? -19.026 114.447 52.900 1.00 24.69 ? 377  ASN A ND2   1 
ATOM   2941 N N     . PHE A 1 378 ? -19.066 110.342 49.040 1.00 26.94 ? 378  PHE A N     1 
ATOM   2942 C CA    . PHE A 1 378 ? -19.064 110.140 47.567 1.00 25.29 ? 378  PHE A CA    1 
ATOM   2943 C C     . PHE A 1 378 ? -20.225 109.247 47.138 1.00 22.83 ? 378  PHE A C     1 
ATOM   2944 O O     . PHE A 1 378 ? -20.576 109.258 45.937 1.00 27.10 ? 378  PHE A O     1 
ATOM   2945 C CB    . PHE A 1 378 ? -17.677 109.741 47.050 1.00 25.93 ? 378  PHE A CB    1 
ATOM   2946 C CG    . PHE A 1 378 ? -17.191 108.359 47.360 1.00 24.75 ? 378  PHE A CG    1 
ATOM   2947 C CD1   . PHE A 1 378 ? -17.864 107.238 46.895 1.00 25.58 ? 378  PHE A CD1   1 
ATOM   2948 C CD2   . PHE A 1 378 ? -15.994 108.194 48.039 1.00 24.43 ? 378  PHE A CD2   1 
ATOM   2949 C CE1   . PHE A 1 378 ? -17.388 105.955 47.138 1.00 27.61 ? 378  PHE A CE1   1 
ATOM   2950 C CE2   . PHE A 1 378 ? -15.512 106.913 48.284 1.00 26.04 ? 378  PHE A CE2   1 
ATOM   2951 C CZ    . PHE A 1 378 ? -16.211 105.796 47.841 1.00 26.92 ? 378  PHE A CZ    1 
ATOM   2952 N N     . LEU A 1 379 ? -20.814 108.461 48.034 1.00 24.49 ? 379  LEU A N     1 
ATOM   2953 C CA    . LEU A 1 379 ? -21.955 107.594 47.699 1.00 25.56 ? 379  LEU A CA    1 
ATOM   2954 C C     . LEU A 1 379 ? -23.192 108.425 47.321 1.00 26.34 ? 379  LEU A C     1 
ATOM   2955 O O     . LEU A 1 379 ? -24.150 107.791 46.806 1.00 27.72 ? 379  LEU A O     1 
ATOM   2956 C CB    . LEU A 1 379 ? -22.277 106.654 48.861 1.00 26.54 ? 379  LEU A CB    1 
ATOM   2957 C CG    . LEU A 1 379 ? -21.187 105.655 49.255 1.00 24.65 ? 379  LEU A CG    1 
ATOM   2958 C CD1   . LEU A 1 379 ? -21.608 104.783 50.436 1.00 26.39 ? 379  LEU A CD1   1 
ATOM   2959 C CD2   . LEU A 1 379 ? -20.797 104.795 48.073 1.00 24.99 ? 379  LEU A CD2   1 
ATOM   2960 N N     . ASN A 1 380 ? -23.218 109.732 47.609 1.00 29.22 ? 380  ASN A N     1 
ATOM   2961 C CA    . ASN A 1 380 ? -24.395 110.576 47.245 1.00 29.42 ? 380  ASN A CA    1 
ATOM   2962 C C     . ASN A 1 380 ? -24.334 110.989 45.767 1.00 32.78 ? 380  ASN A C     1 
ATOM   2963 O O     . ASN A 1 380 ? -25.268 111.683 45.336 1.00 31.54 ? 380  ASN A O     1 
ATOM   2964 C CB    . ASN A 1 380 ? -24.488 111.852 48.068 1.00 28.36 ? 380  ASN A CB    1 
ATOM   2965 C CG    . ASN A 1 380 ? -24.558 111.567 49.557 1.00 28.56 ? 380  ASN A CG    1 
ATOM   2966 O OD1   . ASN A 1 380 ? -25.491 110.916 50.039 1.00 28.23 ? 380  ASN A OD1   1 
ATOM   2967 N ND2   . ASN A 1 380 ? -23.546 112.031 50.276 1.00 30.02 ? 380  ASN A ND2   1 
ATOM   2968 N N     . TRP A 1 381 ? -23.251 110.658 45.049 1.00 30.08 ? 381  TRP A N     1 
ATOM   2969 C CA    . TRP A 1 381 ? -22.887 111.357 43.792 1.00 28.91 ? 381  TRP A CA    1 
ATOM   2970 C C     . TRP A 1 381 ? -24.076 111.286 42.828 1.00 28.15 ? 381  TRP A C     1 
ATOM   2971 O O     . TRP A 1 381 ? -24.410 112.304 42.224 1.00 27.20 ? 381  TRP A O     1 
ATOM   2972 C CB    . TRP A 1 381 ? -21.621 110.769 43.143 1.00 28.53 ? 381  TRP A CB    1 
ATOM   2973 C CG    . TRP A 1 381 ? -21.301 111.433 41.831 1.00 27.50 ? 381  TRP A CG    1 
ATOM   2974 C CD1   . TRP A 1 381 ? -21.408 110.878 40.591 1.00 30.13 ? 381  TRP A CD1   1 
ATOM   2975 C CD2   . TRP A 1 381 ? -20.910 112.792 41.610 1.00 28.58 ? 381  TRP A CD2   1 
ATOM   2976 N NE1   . TRP A 1 381 ? -21.061 111.787 39.630 1.00 29.10 ? 381  TRP A NE1   1 
ATOM   2977 C CE2   . TRP A 1 381 ? -20.772 112.974 40.221 1.00 27.73 ? 381  TRP A CE2   1 
ATOM   2978 C CE3   . TRP A 1 381 ? -20.650 113.881 42.438 1.00 32.34 ? 381  TRP A CE3   1 
ATOM   2979 C CZ2   . TRP A 1 381 ? -20.381 114.179 39.660 1.00 27.24 ? 381  TRP A CZ2   1 
ATOM   2980 C CZ3   . TRP A 1 381 ? -20.278 115.080 41.877 1.00 31.15 ? 381  TRP A CZ3   1 
ATOM   2981 C CH2   . TRP A 1 381 ? -20.176 115.235 40.496 1.00 28.62 ? 381  TRP A CH2   1 
ATOM   2982 N N     . ASP A 1 382 ? -24.709 110.130 42.724 1.00 31.68 ? 382  ASP A N     1 
ATOM   2983 C CA    . ASP A 1 382 ? -25.741 109.846 41.687 1.00 36.83 ? 382  ASP A CA    1 
ATOM   2984 C C     . ASP A 1 382 ? -27.070 109.518 42.356 1.00 37.85 ? 382  ASP A C     1 
ATOM   2985 O O     . ASP A 1 382 ? -27.803 108.691 41.810 1.00 35.82 ? 382  ASP A O     1 
ATOM   2986 C CB    . ASP A 1 382 ? -25.276 108.681 40.805 1.00 43.61 ? 382  ASP A CB    1 
ATOM   2987 C CG    . ASP A 1 382 ? -25.995 108.593 39.467 1.00 54.80 ? 382  ASP A CG    1 
ATOM   2988 O OD1   . ASP A 1 382 ? -26.465 109.664 38.973 1.00 54.44 ? 382  ASP A OD1   1 
ATOM   2989 O OD2   . ASP A 1 382 ? -26.080 107.459 38.933 1.00 60.13 ? 382  ASP A OD2   1 
ATOM   2990 N N     . GLY A 1 383 ? -27.307 110.029 43.563 1.00 35.27 ? 383  GLY A N     1 
ATOM   2991 C CA    . GLY A 1 383 ? -28.596 109.891 44.247 1.00 36.37 ? 383  GLY A CA    1 
ATOM   2992 C C     . GLY A 1 383 ? -28.602 108.787 45.287 1.00 41.58 ? 383  GLY A C     1 
ATOM   2993 O O     . GLY A 1 383 ? -29.673 108.535 45.826 1.00 42.07 ? 383  GLY A O     1 
ATOM   2994 N N     . GLY A 1 384 ? -27.459 108.195 45.643 1.00 37.39 ? 384  GLY A N     1 
ATOM   2995 C CA    . GLY A 1 384 ? -27.414 107.262 46.786 1.00 36.17 ? 384  GLY A CA    1 
ATOM   2996 C C     . GLY A 1 384 ? -27.144 105.850 46.299 1.00 41.34 ? 384  GLY A C     1 
ATOM   2997 O O     . GLY A 1 384 ? -27.980 105.296 45.580 1.00 45.88 ? 384  GLY A O     1 
ATOM   2998 N N     . GLY A 1 385 ? -25.971 105.311 46.608 1.00 33.79 ? 385  GLY A N     1 
ATOM   2999 C CA    . GLY A 1 385 ? -25.627 103.946 46.213 1.00 31.03 ? 385  GLY A CA    1 
ATOM   3000 C C     . GLY A 1 385 ? -24.699 103.248 47.188 1.00 26.89 ? 385  GLY A C     1 
ATOM   3001 O O     . GLY A 1 385 ? -24.287 103.836 48.197 1.00 27.64 ? 385  GLY A O     1 
ATOM   3002 N N     . GLY A 1 386 ? -24.399 102.002 46.868 1.00 26.17 ? 386  GLY A N     1 
ATOM   3003 C CA    . GLY A 1 386 ? -23.253 101.312 47.482 1.00 26.90 ? 386  GLY A CA    1 
ATOM   3004 C C     . GLY A 1 386 ? -22.046 101.482 46.588 1.00 27.31 ? 386  GLY A C     1 
ATOM   3005 O O     . GLY A 1 386 ? -22.128 102.217 45.535 1.00 23.54 ? 386  GLY A O     1 
ATOM   3006 N N     . HIS A 1 387 ? -20.961 100.803 46.919 1.00 22.63 ? 387  HIS A N     1 
ATOM   3007 C CA    . HIS A 1 387 ? -19.758 100.839 46.057 1.00 24.42 ? 387  HIS A CA    1 
ATOM   3008 C C     . HIS A 1 387 ? -19.048 99.504  46.172 1.00 25.88 ? 387  HIS A C     1 
ATOM   3009 O O     . HIS A 1 387 ? -19.354 98.719  47.094 1.00 25.07 ? 387  HIS A O     1 
ATOM   3010 C CB    . HIS A 1 387 ? -18.903 102.074 46.366 1.00 22.31 ? 387  HIS A CB    1 
ATOM   3011 C CG    . HIS A 1 387 ? -18.008 102.002 47.554 1.00 23.52 ? 387  HIS A CG    1 
ATOM   3012 N ND1   . HIS A 1 387 ? -16.632 101.980 47.411 1.00 22.99 ? 387  HIS A ND1   1 
ATOM   3013 C CD2   . HIS A 1 387 ? -18.255 102.049 48.879 1.00 22.58 ? 387  HIS A CD2   1 
ATOM   3014 C CE1   . HIS A 1 387 ? -16.070 102.037 48.604 1.00 25.00 ? 387  HIS A CE1   1 
ATOM   3015 N NE2   . HIS A 1 387 ? -17.052 102.056 49.552 1.00 24.95 ? 387  HIS A NE2   1 
ATOM   3016 N N     . VAL A 1 388 ? -18.235 99.237  45.180 1.00 23.92 ? 388  VAL A N     1 
ATOM   3017 C CA    . VAL A 1 388 ? -17.312 98.084  45.186 1.00 24.34 ? 388  VAL A CA    1 
ATOM   3018 C C     . VAL A 1 388 ? -15.952 98.608  44.721 1.00 25.66 ? 388  VAL A C     1 
ATOM   3019 O O     . VAL A 1 388 ? -15.909 99.544  43.900 1.00 23.57 ? 388  VAL A O     1 
ATOM   3020 C CB    . VAL A 1 388 ? -17.848 96.928  44.328 1.00 24.30 ? 388  VAL A CB    1 
ATOM   3021 C CG1   . VAL A 1 388 ? -17.885 97.325  42.859 1.00 23.31 ? 388  VAL A CG1   1 
ATOM   3022 C CG2   . VAL A 1 388 ? -17.026 95.662  44.535 1.00 25.20 ? 388  VAL A CG2   1 
ATOM   3023 N N     . GLY A 1 389 ? -14.878 98.036  45.274 1.00 24.29 ? 389  GLY A N     1 
ATOM   3024 C CA    . GLY A 1 389 ? -13.526 98.459  44.920 1.00 26.72 ? 389  GLY A CA    1 
ATOM   3025 C C     . GLY A 1 389 ? -12.936 97.517  43.881 1.00 25.97 ? 389  GLY A C     1 
ATOM   3026 O O     . GLY A 1 389 ? -12.809 96.345  44.154 1.00 26.14 ? 389  GLY A O     1 
ATOM   3027 N N     . PHE A 1 390 ? -12.550 98.055  42.754 1.00 24.25 ? 390  PHE A N     1 
ATOM   3028 C CA    . PHE A 1 390 ? -11.752 97.320  41.753 1.00 25.75 ? 390  PHE A CA    1 
ATOM   3029 C C     . PHE A 1 390 ? -10.349 97.828  41.956 1.00 22.36 ? 390  PHE A C     1 
ATOM   3030 O O     . PHE A 1 390 ? -10.119 99.027  41.710 1.00 25.63 ? 390  PHE A O     1 
ATOM   3031 C CB    . PHE A 1 390 ? -12.247 97.529  40.326 1.00 25.83 ? 390  PHE A CB    1 
ATOM   3032 C CG    . PHE A 1 390 ? -11.343 96.822  39.350 1.00 25.71 ? 390  PHE A CG    1 
ATOM   3033 C CD1   . PHE A 1 390 ? -11.249 95.431  39.367 1.00 27.20 ? 390  PHE A CD1   1 
ATOM   3034 C CD2   . PHE A 1 390 ? -10.522 97.537  38.497 1.00 25.13 ? 390  PHE A CD2   1 
ATOM   3035 C CE1   . PHE A 1 390 ? -10.377 94.764  38.513 1.00 26.55 ? 390  PHE A CE1   1 
ATOM   3036 C CE2   . PHE A 1 390 ? -9.660  96.871  37.636 1.00 23.68 ? 390  PHE A CE2   1 
ATOM   3037 C CZ    . PHE A 1 390 ? -9.590  95.492  37.630 1.00 26.60 ? 390  PHE A CZ    1 
ATOM   3038 N N     . SER A 1 391 ? -9.441  96.968  42.446 1.00 22.94 ? 391  SER A N     1 
ATOM   3039 C CA    . SER A 1 391 ? -8.187  97.439  43.064 1.00 22.36 ? 391  SER A CA    1 
ATOM   3040 C C     . SER A 1 391 ? -6.926  96.799  42.473 1.00 26.09 ? 391  SER A C     1 
ATOM   3041 O O     . SER A 1 391 ? -6.177  96.131  43.207 1.00 25.00 ? 391  SER A O     1 
ATOM   3042 C CB    . SER A 1 391 ? -8.274  97.133  44.565 1.00 22.69 ? 391  SER A CB    1 
ATOM   3043 O OG    . SER A 1 391 ? -9.559  97.460  45.113 1.00 25.49 ? 391  SER A OG    1 
ATOM   3044 N N     . PRO A 1 392 ? -6.626  96.996  41.169 1.00 24.25 ? 392  PRO A N     1 
ATOM   3045 C CA    . PRO A 1 392 ? -5.374  96.532  40.592 1.00 21.67 ? 392  PRO A CA    1 
ATOM   3046 C C     . PRO A 1 392 ? -4.158  97.277  41.121 1.00 22.84 ? 392  PRO A C     1 
ATOM   3047 O O     . PRO A 1 392 ? -4.220  98.465  41.465 1.00 23.76 ? 392  PRO A O     1 
ATOM   3048 C CB    . PRO A 1 392 ? -5.565  96.792  39.065 1.00 20.87 ? 392  PRO A CB    1 
ATOM   3049 C CG    . PRO A 1 392 ? -6.560  97.958  39.045 1.00 23.48 ? 392  PRO A CG    1 
ATOM   3050 C CD    . PRO A 1 392 ? -7.505  97.630  40.167 1.00 21.93 ? 392  PRO A CD    1 
ATOM   3051 N N     . VAL A 1 393 ? -3.036  96.562  41.071 1.00 21.43 ? 393  VAL A N     1 
ATOM   3052 C CA    . VAL A 1 393 ? -1.692  97.082  41.351 1.00 22.67 ? 393  VAL A CA    1 
ATOM   3053 C C     . VAL A 1 393 ? -1.074  97.576  40.046 1.00 24.49 ? 393  VAL A C     1 
ATOM   3054 O O     . VAL A 1 393 ? -1.184  96.866  39.056 1.00 25.73 ? 393  VAL A O     1 
ATOM   3055 C CB    . VAL A 1 393 ? -0.816  95.997  42.006 1.00 24.81 ? 393  VAL A CB    1 
ATOM   3056 C CG1   . VAL A 1 393 ? 0.586   96.523  42.274 1.00 28.70 ? 393  VAL A CG1   1 
ATOM   3057 C CG2   . VAL A 1 393 ? -1.444  95.525  43.305 1.00 28.46 ? 393  VAL A CG2   1 
ATOM   3058 N N     . SER A 1 394 ? -0.254  98.628  40.125 1.00 23.88 ? 394  SER A N     1 
ATOM   3059 C CA    . SER A 1 394 ? 0.496   99.196  38.976 1.00 24.12 ? 394  SER A CA    1 
ATOM   3060 C C     . SER A 1 394 ? 1.913   99.518  39.421 1.00 25.34 ? 394  SER A C     1 
ATOM   3061 O O     . SER A 1 394 ? 2.123   99.958  40.559 1.00 25.24 ? 394  SER A O     1 
ATOM   3062 C CB    . SER A 1 394 ? -0.249  100.448 38.461 1.00 22.81 ? 394  SER A CB    1 
ATOM   3063 O OG    . SER A 1 394 ? 0.520   101.148 37.510 1.00 23.99 ? 394  SER A OG    1 
ATOM   3064 N N     . PRO A 1 395 ? 2.917   99.398  38.536 1.00 22.98 ? 395  PRO A N     1 
ATOM   3065 C CA    . PRO A 1 395 ? 4.172   100.116 38.731 1.00 24.56 ? 395  PRO A CA    1 
ATOM   3066 C C     . PRO A 1 395 ? 3.904   101.627 38.859 1.00 27.85 ? 395  PRO A C     1 
ATOM   3067 O O     . PRO A 1 395 ? 2.914   102.129 38.274 1.00 27.32 ? 395  PRO A O     1 
ATOM   3068 C CB    . PRO A 1 395 ? 4.981   99.885  37.451 1.00 21.73 ? 395  PRO A CB    1 
ATOM   3069 C CG    . PRO A 1 395 ? 4.299   98.678  36.826 1.00 21.44 ? 395  PRO A CG    1 
ATOM   3070 C CD    . PRO A 1 395 ? 2.850   98.783  37.215 1.00 23.75 ? 395  PRO A CD    1 
ATOM   3071 N N     . ILE A 1 396 ? 4.791   102.336 39.553 1.00 26.02 ? 396  ILE A N     1 
ATOM   3072 C CA    . ILE A 1 396 ? 4.827   103.820 39.480 1.00 24.97 ? 396  ILE A CA    1 
ATOM   3073 C C     . ILE A 1 396 ? 5.469   104.230 38.148 1.00 24.34 ? 396  ILE A C     1 
ATOM   3074 O O     . ILE A 1 396 ? 6.532   104.827 38.128 1.00 21.91 ? 396  ILE A O     1 
ATOM   3075 C CB    . ILE A 1 396 ? 5.511   104.449 40.699 1.00 24.77 ? 396  ILE A CB    1 
ATOM   3076 C CG1   . ILE A 1 396 ? 5.127   103.733 41.998 1.00 24.57 ? 396  ILE A CG1   1 
ATOM   3077 C CG2   . ILE A 1 396 ? 5.120   105.927 40.711 1.00 24.58 ? 396  ILE A CG2   1 
ATOM   3078 C CD1   . ILE A 1 396 ? 5.875   104.224 43.212 1.00 24.97 ? 396  ILE A CD1   1 
ATOM   3079 N N     . THR A 1 397 ? 4.733   104.022 37.067 1.00 25.09 ? 397  THR A N     1 
ATOM   3080 C CA    . THR A 1 397 ? 5.123   104.359 35.689 1.00 27.04 ? 397  THR A CA    1 
ATOM   3081 C C     . THR A 1 397 ? 3.954   105.063 35.008 1.00 28.22 ? 397  THR A C     1 
ATOM   3082 O O     . THR A 1 397 ? 2.868   104.512 35.069 1.00 28.52 ? 397  THR A O     1 
ATOM   3083 C CB    . THR A 1 397 ? 5.478   103.052 34.962 1.00 34.28 ? 397  THR A CB    1 
ATOM   3084 O OG1   . THR A 1 397 ? 6.643   102.461 35.546 1.00 30.50 ? 397  THR A OG1   1 
ATOM   3085 C CG2   . THR A 1 397 ? 5.718   103.278 33.497 1.00 37.86 ? 397  THR A CG2   1 
ATOM   3086 N N     . GLY A 1 398 ? 4.208   106.168 34.326 1.00 26.54 ? 398  GLY A N     1 
ATOM   3087 C CA    . GLY A 1 398 ? 3.183   106.892 33.565 1.00 29.70 ? 398  GLY A CA    1 
ATOM   3088 C C     . GLY A 1 398 ? 2.441   105.979 32.616 1.00 30.36 ? 398  GLY A C     1 
ATOM   3089 O O     . GLY A 1 398 ? 1.238   106.068 32.534 1.00 28.14 ? 398  GLY A O     1 
ATOM   3090 N N     . LYS A 1 399 ? 3.158   105.112 31.905 1.00 27.94 ? 399  LYS A N     1 
ATOM   3091 C CA    . LYS A 1 399 ? 2.559   104.288 30.843 1.00 27.10 ? 399  LYS A CA    1 
ATOM   3092 C C     . LYS A 1 399 ? 1.512   103.380 31.464 1.00 24.53 ? 399  LYS A C     1 
ATOM   3093 O O     . LYS A 1 399 ? 0.430   103.214 30.840 1.00 25.67 ? 399  LYS A O     1 
ATOM   3094 C CB    . LYS A 1 399 ? 3.652   103.504 30.107 1.00 30.49 ? 399  LYS A CB    1 
ATOM   3095 C CG    . LYS A 1 399 ? 3.159   102.457 29.120 1.00 33.25 ? 399  LYS A CG    1 
ATOM   3096 C CD    . LYS A 1 399 ? 4.360   101.650 28.621 1.00 39.36 ? 399  LYS A CD    1 
ATOM   3097 C CE    . LYS A 1 399 ? 3.952   100.461 27.805 1.00 44.42 ? 399  LYS A CE    1 
ATOM   3098 N NZ    . LYS A 1 399 ? 3.622   100.897 26.430 1.00 47.08 ? 399  LYS A NZ    1 
ATOM   3099 N N     . ASP A 1 400 ? 1.838   102.754 32.600 1.00 23.10 ? 400  ASP A N     1 
ATOM   3100 C CA    . ASP A 1 400 ? 0.909   101.828 33.284 1.00 24.15 ? 400  ASP A CA    1 
ATOM   3101 C C     . ASP A 1 400 ? -0.296  102.603 33.855 1.00 22.76 ? 400  ASP A C     1 
ATOM   3102 O O     . ASP A 1 400 ? -1.413  102.082 33.810 1.00 23.44 ? 400  ASP A O     1 
ATOM   3103 C CB    . ASP A 1 400 ? 1.623   100.977 34.338 1.00 24.44 ? 400  ASP A CB    1 
ATOM   3104 C CG    . ASP A 1 400 ? 2.658   100.076 33.696 1.00 23.22 ? 400  ASP A CG    1 
ATOM   3105 O OD1   . ASP A 1 400 ? 2.256   99.036  33.141 1.00 24.65 ? 400  ASP A OD1   1 
ATOM   3106 O OD2   . ASP A 1 400 ? 3.820   100.456 33.724 1.00 24.41 ? 400  ASP A OD2   1 
ATOM   3107 N N     . ALA A 1 401 ? -0.051  103.723 34.487 1.00 25.83 ? 401  ALA A N     1 
ATOM   3108 C CA    . ALA A 1 401 ? -1.107  104.484 35.192 1.00 27.97 ? 401  ALA A CA    1 
ATOM   3109 C C     . ALA A 1 401 ? -2.101  104.970 34.140 1.00 26.02 ? 401  ALA A C     1 
ATOM   3110 O O     . ALA A 1 401 ? -3.288  104.767 34.318 1.00 25.31 ? 401  ALA A O     1 
ATOM   3111 C CB    . ALA A 1 401 ? -0.507  105.639 35.949 1.00 26.20 ? 401  ALA A CB    1 
ATOM   3112 N N     . ILE A 1 402 ? -1.624  105.514 33.030 1.00 26.79 ? 402  ILE A N     1 
ATOM   3113 C CA    . ILE A 1 402 ? -2.584  106.007 32.005 1.00 26.49 ? 402  ILE A CA    1 
ATOM   3114 C C     . ILE A 1 402 ? -3.249  104.822 31.278 1.00 29.11 ? 402  ILE A C     1 
ATOM   3115 O O     . ILE A 1 402 ? -4.444  104.950 30.939 1.00 29.74 ? 402  ILE A O     1 
ATOM   3116 C CB    . ILE A 1 402 ? -1.972  107.063 31.083 1.00 27.26 ? 402  ILE A CB    1 
ATOM   3117 C CG1   . ILE A 1 402 ? -3.078  107.873 30.405 1.00 28.67 ? 402  ILE A CG1   1 
ATOM   3118 C CG2   . ILE A 1 402 ? -1.029  106.418 30.074 1.00 32.05 ? 402  ILE A CG2   1 
ATOM   3119 C CD1   . ILE A 1 402 ? -2.576  109.127 29.686 1.00 28.80 ? 402  ILE A CD1   1 
ATOM   3120 N N     . LYS A 1 403 ? -2.561  103.695 31.076 1.00 28.03 ? 403  LYS A N     1 
ATOM   3121 C CA    . LYS A 1 403 ? -3.184  102.485 30.489 1.00 27.83 ? 403  LYS A CA    1 
ATOM   3122 C C     . LYS A 1 403 ? -4.342  102.050 31.399 1.00 28.77 ? 403  LYS A C     1 
ATOM   3123 O O     . LYS A 1 403 ? -5.433  101.778 30.878 1.00 26.25 ? 403  LYS A O     1 
ATOM   3124 C CB    . LYS A 1 403 ? -2.132  101.387 30.320 1.00 28.81 ? 403  LYS A CB    1 
ATOM   3125 C CG    . LYS A 1 403 ? -2.606  100.025 29.826 1.00 30.27 ? 403  LYS A CG    1 
ATOM   3126 C CD    . LYS A 1 403 ? -3.439  100.093 28.571 1.00 41.21 ? 403  LYS A CD    1 
ATOM   3127 C CE    . LYS A 1 403 ? -3.628  98.761  27.860 1.00 49.21 ? 403  LYS A CE    1 
ATOM   3128 N NZ    . LYS A 1 403 ? -4.187  98.911  26.492 1.00 47.56 ? 403  LYS A NZ    1 
ATOM   3129 N N     . GLN A 1 404 ? -4.104  101.957 32.717 1.00 27.68 ? 404  GLN A N     1 
ATOM   3130 C CA    . GLN A 1 404 ? -5.145  101.461 33.659 1.00 27.77 ? 404  GLN A CA    1 
ATOM   3131 C C     . GLN A 1 404 ? -6.318  102.467 33.674 1.00 26.97 ? 404  GLN A C     1 
ATOM   3132 O O     . GLN A 1 404 ? -7.472  102.033 33.713 1.00 27.36 ? 404  GLN A O     1 
ATOM   3133 C CB    . GLN A 1 404 ? -4.587  101.224 35.061 1.00 27.33 ? 404  GLN A CB    1 
ATOM   3134 C CG    . GLN A 1 404 ? -3.692  99.995  35.138 1.00 28.87 ? 404  GLN A CG    1 
ATOM   3135 C CD    . GLN A 1 404 ? -3.412  99.514  36.539 1.00 25.85 ? 404  GLN A CD    1 
ATOM   3136 O OE1   . GLN A 1 404 ? -4.006  99.982  37.497 1.00 27.09 ? 404  GLN A OE1   1 
ATOM   3137 N NE2   . GLN A 1 404 ? -2.558  98.491  36.644 1.00 31.81 ? 404  GLN A NE2   1 
ATOM   3138 N N     . TYR A 1 405 ? -6.005  103.750 33.707 1.00 26.81 ? 405  TYR A N     1 
ATOM   3139 C CA    . TYR A 1 405 ? -7.006  104.830 33.708 1.00 27.56 ? 405  TYR A CA    1 
ATOM   3140 C C     . TYR A 1 405 ? -7.903  104.633 32.490 1.00 30.31 ? 405  TYR A C     1 
ATOM   3141 O O     . TYR A 1 405 ? -9.139  104.570 32.651 1.00 27.43 ? 405  TYR A O     1 
ATOM   3142 C CB    . TYR A 1 405 ? -6.341  106.202 33.751 1.00 27.70 ? 405  TYR A CB    1 
ATOM   3143 C CG    . TYR A 1 405 ? -7.302  107.316 33.443 1.00 31.41 ? 405  TYR A CG    1 
ATOM   3144 C CD1   . TYR A 1 405 ? -8.395  107.548 34.273 1.00 33.60 ? 405  TYR A CD1   1 
ATOM   3145 C CD2   . TYR A 1 405 ? -7.159  108.098 32.310 1.00 30.27 ? 405  TYR A CD2   1 
ATOM   3146 C CE1   . TYR A 1 405 ? -9.323  108.542 33.984 1.00 31.51 ? 405  TYR A CE1   1 
ATOM   3147 C CE2   . TYR A 1 405 ? -8.087  109.077 31.996 1.00 34.18 ? 405  TYR A CE2   1 
ATOM   3148 C CZ    . TYR A 1 405 ? -9.173  109.293 32.838 1.00 32.83 ? 405  TYR A CZ    1 
ATOM   3149 O OH    . TYR A 1 405 ? -10.085 110.265 32.584 1.00 32.48 ? 405  TYR A OH    1 
ATOM   3150 N N     . ASN A 1 406 ? -7.304  104.552 31.300 1.00 28.81 ? 406  ASN A N     1 
ATOM   3151 C CA    . ASN A 1 406 ? -8.062  104.414 30.018 1.00 30.33 ? 406  ASN A CA    1 
ATOM   3152 C C     . ASN A 1 406 ? -8.921  103.144 30.045 1.00 28.57 ? 406  ASN A C     1 
ATOM   3153 O O     . ASN A 1 406 ? -10.140 103.216 29.706 1.00 29.76 ? 406  ASN A O     1 
ATOM   3154 C CB    . ASN A 1 406 ? -7.108  104.483 28.811 1.00 32.02 ? 406  ASN A CB    1 
ATOM   3155 C CG    . ASN A 1 406 ? -6.674  105.914 28.571 1.00 35.14 ? 406  ASN A CG    1 
ATOM   3156 O OD1   . ASN A 1 406 ? -7.453  106.818 28.783 1.00 38.28 ? 406  ASN A OD1   1 
ATOM   3157 N ND2   . ASN A 1 406 ? -5.446  106.150 28.160 1.00 35.80 ? 406  ASN A ND2   1 
ATOM   3158 N N     . MET A 1 407 ? -8.350  102.022 30.459 1.00 29.23 ? 407  MET A N     1 
ATOM   3159 C CA    . MET A 1 407 ? -9.059  100.716 30.451 1.00 30.26 ? 407  MET A CA    1 
ATOM   3160 C C     . MET A 1 407 ? -10.264 100.792 31.396 1.00 31.04 ? 407  MET A C     1 
ATOM   3161 O O     . MET A 1 407 ? -11.344 100.273 31.064 1.00 27.54 ? 407  MET A O     1 
ATOM   3162 C CB    . MET A 1 407 ? -8.140  99.605  30.968 1.00 33.66 ? 407  MET A CB    1 
ATOM   3163 C CG    . MET A 1 407 ? -7.019  99.264  30.023 1.00 39.00 ? 407  MET A CG    1 
ATOM   3164 S SD    . MET A 1 407 ? -5.915  98.032  30.785 1.00 36.38 ? 407  MET A SD    1 
ATOM   3165 C CE    . MET A 1 407 ? -6.953  96.580  30.656 1.00 34.61 ? 407  MET A CE    1 
ATOM   3166 N N     . VAL A 1 408 ? -10.031 101.302 32.602 1.00 26.93 ? 408  VAL A N     1 
ATOM   3167 C CA    . VAL A 1 408 ? -11.031 101.255 33.688 1.00 27.84 ? 408  VAL A CA    1 
ATOM   3168 C C     . VAL A 1 408 ? -12.064 102.361 33.452 1.00 28.10 ? 408  VAL A C     1 
ATOM   3169 O O     . VAL A 1 408 ? -13.250 102.052 33.476 1.00 25.19 ? 408  VAL A O     1 
ATOM   3170 C CB    . VAL A 1 408 ? -10.387 101.369 35.071 1.00 26.13 ? 408  VAL A CB    1 
ATOM   3171 C CG1   . VAL A 1 408 ? -11.463 101.476 36.131 1.00 29.04 ? 408  VAL A CG1   1 
ATOM   3172 C CG2   . VAL A 1 408 ? -9.509  100.148 35.342 1.00 29.41 ? 408  VAL A CG2   1 
ATOM   3173 N N     . SER A 1 409 ? -11.647 103.598 33.260 1.00 28.78 ? 409  SER A N     1 
ATOM   3174 C CA    . SER A 1 409 ? -12.646 104.697 33.097 1.00 30.44 ? 409  SER A CA    1 
ATOM   3175 C C     . SER A 1 409 ? -13.530 104.432 31.878 1.00 30.01 ? 409  SER A C     1 
ATOM   3176 O O     . SER A 1 409 ? -14.751 104.651 32.002 1.00 30.60 ? 409  SER A O     1 
ATOM   3177 C CB    . SER A 1 409 ? -12.071 106.053 33.025 1.00 29.66 ? 409  SER A CB    1 
ATOM   3178 O OG    . SER A 1 409 ? -11.358 106.171 31.849 1.00 36.53 ? 409  SER A OG    1 
ATOM   3179 N N     . SER A 1 410 ? -12.993 103.955 30.748 1.00 29.14 ? 410  SER A N     1 
ATOM   3180 C CA    . SER A 1 410 ? -13.810 103.620 29.536 1.00 29.80 ? 410  SER A CA    1 
ATOM   3181 C C     . SER A 1 410 ? -14.937 102.672 29.875 1.00 30.33 ? 410  SER A C     1 
ATOM   3182 O O     . SER A 1 410 ? -16.063 102.876 29.437 1.00 29.91 ? 410  SER A O     1 
ATOM   3183 C CB    . SER A 1 410 ? -12.987 102.933 28.484 1.00 34.59 ? 410  SER A CB    1 
ATOM   3184 O OG    . SER A 1 410 ? -12.044 103.856 28.056 1.00 41.74 ? 410  SER A OG    1 
ATOM   3185 N N     . ARG A 1 411 ? -14.593 101.570 30.520 1.00 28.84 ? 411  ARG A N     1 
ATOM   3186 C CA    . ARG A 1 411 ? -15.576 100.496 30.761 1.00 27.29 ? 411  ARG A CA    1 
ATOM   3187 C C     . ARG A 1 411 ? -16.604 100.963 31.796 1.00 28.96 ? 411  ARG A C     1 
ATOM   3188 O O     . ARG A 1 411 ? -17.781 100.677 31.634 1.00 28.90 ? 411  ARG A O     1 
ATOM   3189 C CB    . ARG A 1 411 ? -14.830 99.254  31.232 1.00 30.34 ? 411  ARG A CB    1 
ATOM   3190 C CG    . ARG A 1 411 ? -14.002 98.631  30.123 1.00 32.96 ? 411  ARG A CG    1 
ATOM   3191 C CD    . ARG A 1 411 ? -14.968 98.051  29.105 1.00 32.76 ? 411  ARG A CD    1 
ATOM   3192 N NE    . ARG A 1 411 ? -14.262 97.167  28.204 1.00 34.87 ? 411  ARG A NE    1 
ATOM   3193 C CZ    . ARG A 1 411 ? -14.755 96.736  27.051 1.00 43.37 ? 411  ARG A CZ    1 
ATOM   3194 N NH1   . ARG A 1 411 ? -15.944 97.138  26.637 1.00 40.97 ? 411  ARG A NH1   1 
ATOM   3195 N NH2   . ARG A 1 411 ? -14.043 95.918  26.304 1.00 41.39 ? 411  ARG A NH2   1 
ATOM   3196 N N     . VAL A 1 412 ? -16.137 101.584 32.876 1.00 28.56 ? 412  VAL A N     1 
ATOM   3197 C CA    . VAL A 1 412 ? -17.021 102.084 33.953 1.00 28.76 ? 412  VAL A CA    1 
ATOM   3198 C C     . VAL A 1 412 ? -18.058 103.044 33.337 1.00 29.86 ? 412  VAL A C     1 
ATOM   3199 O O     . VAL A 1 412 ? -19.231 102.826 33.551 1.00 25.41 ? 412  VAL A O     1 
ATOM   3200 C CB    . VAL A 1 412 ? -16.154 102.700 35.063 1.00 30.14 ? 412  VAL A CB    1 
ATOM   3201 C CG1   . VAL A 1 412 ? -16.993 103.466 36.030 1.00 33.70 ? 412  VAL A CG1   1 
ATOM   3202 C CG2   . VAL A 1 412 ? -15.406 101.591 35.799 1.00 28.56 ? 412  VAL A CG2   1 
ATOM   3203 N N     . ARG A 1 413 ? -17.626 104.029 32.555 1.00 29.64 ? 413  ARG A N     1 
ATOM   3204 C CA    . ARG A 1 413 ? -18.519 105.028 31.895 1.00 31.84 ? 413  ARG A CA    1 
ATOM   3205 C C     . ARG A 1 413 ? -19.447 104.334 30.896 1.00 32.12 ? 413  ARG A C     1 
ATOM   3206 O O     . ARG A 1 413 ? -20.661 104.634 30.886 1.00 30.95 ? 413  ARG A O     1 
ATOM   3207 C CB    . ARG A 1 413 ? -17.662 106.132 31.285 1.00 30.53 ? 413  ARG A CB    1 
ATOM   3208 C CG    . ARG A 1 413 ? -17.002 106.998 32.348 1.00 30.75 ? 413  ARG A CG    1 
ATOM   3209 C CD    . ARG A 1 413 ? -15.997 108.010 31.791 1.00 33.76 ? 413  ARG A CD    1 
ATOM   3210 N NE    . ARG A 1 413 ? -16.653 108.808 30.777 1.00 35.06 ? 413  ARG A NE    1 
ATOM   3211 C CZ    . ARG A 1 413 ? -17.347 109.916 31.006 1.00 37.82 ? 413  ARG A CZ    1 
ATOM   3212 N NH1   . ARG A 1 413 ? -17.426 110.448 32.222 1.00 38.55 ? 413  ARG A NH1   1 
ATOM   3213 N NH2   . ARG A 1 413 ? -17.932 110.525 29.990 1.00 36.48 ? 413  ARG A NH2   1 
ATOM   3214 N N     . GLU A 1 414 ? -18.934 103.361 30.154 1.00 34.18 ? 414  GLU A N     1 
ATOM   3215 C CA    . GLU A 1 414 ? -19.739 102.586 29.176 1.00 32.28 ? 414  GLU A CA    1 
ATOM   3216 C C     . GLU A 1 414 ? -20.894 101.887 29.908 1.00 35.59 ? 414  GLU A C     1 
ATOM   3217 O O     . GLU A 1 414 ? -21.985 101.769 29.299 1.00 32.36 ? 414  GLU A O     1 
ATOM   3218 C CB    . GLU A 1 414 ? -18.829 101.642 28.381 1.00 33.31 ? 414  GLU A CB    1 
ATOM   3219 C CG    . GLU A 1 414 ? -19.577 100.596 27.574 1.00 35.94 ? 414  GLU A CG    1 
ATOM   3220 C CD    . GLU A 1 414 ? -18.725 99.444  27.037 1.00 42.22 ? 414  GLU A CD    1 
ATOM   3221 O OE1   . GLU A 1 414 ? -17.509 99.383  27.347 1.00 38.55 ? 414  GLU A OE1   1 
ATOM   3222 O OE2   . GLU A 1 414 ? -19.279 98.601  26.326 1.00 42.45 ? 414  GLU A OE2   1 
ATOM   3223 N N     . TYR A 1 415 ? -20.706 101.431 31.152 1.00 29.91 ? 415  TYR A N     1 
ATOM   3224 C CA    . TYR A 1 415 ? -21.745 100.714 31.931 1.00 29.82 ? 415  TYR A CA    1 
ATOM   3225 C C     . TYR A 1 415 ? -22.600 101.705 32.738 1.00 29.14 ? 415  TYR A C     1 
ATOM   3226 O O     . TYR A 1 415 ? -23.456 101.246 33.493 1.00 32.44 ? 415  TYR A O     1 
ATOM   3227 C CB    . TYR A 1 415 ? -21.088 99.601  32.760 1.00 30.31 ? 415  TYR A CB    1 
ATOM   3228 C CG    . TYR A 1 415 ? -20.881 98.353  31.935 1.00 29.90 ? 415  TYR A CG    1 
ATOM   3229 C CD1   . TYR A 1 415 ? -19.869 98.245  30.986 1.00 30.68 ? 415  TYR A CD1   1 
ATOM   3230 C CD2   . TYR A 1 415 ? -21.760 97.298  32.064 1.00 31.92 ? 415  TYR A CD2   1 
ATOM   3231 C CE1   . TYR A 1 415 ? -19.732 97.114  30.196 1.00 30.57 ? 415  TYR A CE1   1 
ATOM   3232 C CE2   . TYR A 1 415 ? -21.642 96.160  31.275 1.00 33.75 ? 415  TYR A CE2   1 
ATOM   3233 C CZ    . TYR A 1 415 ? -20.634 96.075  30.338 1.00 32.98 ? 415  TYR A CZ    1 
ATOM   3234 O OH    . TYR A 1 415 ? -20.580 94.945  29.586 1.00 35.27 ? 415  TYR A OH    1 
ATOM   3235 N N     . GLY A 1 416 ? -22.407 103.016 32.556 1.00 30.32 ? 416  GLY A N     1 
ATOM   3236 C CA    . GLY A 1 416 ? -23.330 104.050 33.066 1.00 35.46 ? 416  GLY A CA    1 
ATOM   3237 C C     . GLY A 1 416 ? -22.920 104.629 34.410 1.00 34.99 ? 416  GLY A C     1 
ATOM   3238 O O     . GLY A 1 416 ? -23.708 105.415 34.957 1.00 33.43 ? 416  GLY A O     1 
ATOM   3239 N N     . PHE A 1 417 ? -21.693 104.360 34.877 1.00 30.72 ? 417  PHE A N     1 
ATOM   3240 C CA    . PHE A 1 417 ? -21.166 104.908 36.154 1.00 28.91 ? 417  PHE A CA    1 
ATOM   3241 C C     . PHE A 1 417 ? -20.115 105.959 35.870 1.00 26.77 ? 417  PHE A C     1 
ATOM   3242 O O     . PHE A 1 417 ? -19.415 105.853 34.881 1.00 30.05 ? 417  PHE A O     1 
ATOM   3243 C CB    . PHE A 1 417 ? -20.619 103.775 37.029 1.00 28.54 ? 417  PHE A CB    1 
ATOM   3244 C CG    . PHE A 1 417 ? -21.536 102.592 37.131 1.00 27.77 ? 417  PHE A CG    1 
ATOM   3245 C CD1   . PHE A 1 417 ? -22.737 102.693 37.819 1.00 29.77 ? 417  PHE A CD1   1 
ATOM   3246 C CD2   . PHE A 1 417 ? -21.232 101.395 36.510 1.00 28.29 ? 417  PHE A CD2   1 
ATOM   3247 C CE1   . PHE A 1 417 ? -23.603 101.613 37.887 1.00 27.83 ? 417  PHE A CE1   1 
ATOM   3248 C CE2   . PHE A 1 417 ? -22.077 100.302 36.624 1.00 29.01 ? 417  PHE A CE2   1 
ATOM   3249 C CZ    . PHE A 1 417 ? -23.261 100.415 37.313 1.00 26.17 ? 417  PHE A CZ    1 
ATOM   3250 N N     . ASP A 1 418 ? -19.986 106.955 36.730 1.00 25.77 ? 418  ASP A N     1 
ATOM   3251 C CA    . ASP A 1 418 ? -18.809 107.846 36.711 1.00 27.50 ? 418  ASP A CA    1 
ATOM   3252 C C     . ASP A 1 418 ? -17.565 107.080 37.178 1.00 27.89 ? 418  ASP A C     1 
ATOM   3253 O O     . ASP A 1 418 ? -17.677 106.291 38.143 1.00 25.69 ? 418  ASP A O     1 
ATOM   3254 C CB    . ASP A 1 418 ? -19.035 109.129 37.499 1.00 31.71 ? 418  ASP A CB    1 
ATOM   3255 C CG    . ASP A 1 418 ? -19.764 110.185 36.675 1.00 37.81 ? 418  ASP A CG    1 
ATOM   3256 O OD1   . ASP A 1 418 ? -19.210 110.610 35.619 1.00 31.30 ? 418  ASP A OD1   1 
ATOM   3257 O OD2   . ASP A 1 418 ? -20.921 110.468 37.032 1.00 35.33 ? 418  ASP A OD2   1 
ATOM   3258 N N     . TYR A 1 419 ? -16.421 107.414 36.581 1.00 26.96 ? 419  TYR A N     1 
ATOM   3259 C CA    . TYR A 1 419 ? -15.076 106.974 37.026 1.00 28.98 ? 419  TYR A CA    1 
ATOM   3260 C C     . TYR A 1 419 ? -14.730 107.761 38.286 1.00 25.71 ? 419  TYR A C     1 
ATOM   3261 O O     . TYR A 1 419 ? -14.700 108.982 38.260 1.00 28.72 ? 419  TYR A O     1 
ATOM   3262 C CB    . TYR A 1 419 ? -13.974 107.134 35.958 1.00 30.00 ? 419  TYR A CB    1 
ATOM   3263 C CG    . TYR A 1 419 ? -12.588 106.750 36.450 1.00 28.42 ? 419  TYR A CG    1 
ATOM   3264 C CD1   . TYR A 1 419 ? -12.238 105.424 36.681 1.00 29.16 ? 419  TYR A CD1   1 
ATOM   3265 C CD2   . TYR A 1 419 ? -11.623 107.713 36.704 1.00 28.79 ? 419  TYR A CD2   1 
ATOM   3266 C CE1   . TYR A 1 419 ? -10.972 105.072 37.156 1.00 27.21 ? 419  TYR A CE1   1 
ATOM   3267 C CE2   . TYR A 1 419 ? -10.342 107.381 37.123 1.00 26.14 ? 419  TYR A CE2   1 
ATOM   3268 C CZ    . TYR A 1 419 ? -10.018 106.057 37.376 1.00 30.51 ? 419  TYR A CZ    1 
ATOM   3269 O OH    . TYR A 1 419 ? -8.743  105.747 37.783 1.00 26.98 ? 419  TYR A OH    1 
ATOM   3270 N N     . MET A 1 420 ? -14.419 107.041 39.356 1.00 26.54 ? 420  MET A N     1 
ATOM   3271 C CA    . MET A 1 420 ? -13.884 107.615 40.603 1.00 27.04 ? 420  MET A CA    1 
ATOM   3272 C C     . MET A 1 420 ? -12.650 106.791 40.986 1.00 26.45 ? 420  MET A C     1 
ATOM   3273 O O     . MET A 1 420 ? -12.817 105.651 41.514 1.00 26.79 ? 420  MET A O     1 
ATOM   3274 C CB    . MET A 1 420 ? -14.954 107.525 41.697 1.00 24.11 ? 420  MET A CB    1 
ATOM   3275 C CG    . MET A 1 420 ? -16.189 108.410 41.462 1.00 28.23 ? 420  MET A CG    1 
ATOM   3276 S SD    . MET A 1 420 ? -17.369 108.015 42.805 1.00 32.75 ? 420  MET A SD    1 
ATOM   3277 C CE    . MET A 1 420 ? -18.508 109.387 42.627 1.00 34.34 ? 420  MET A CE    1 
ATOM   3278 N N     . GLY A 1 421 ? -11.470 107.342 40.729 1.00 27.42 ? 421  GLY A N     1 
ATOM   3279 C CA    . GLY A 1 421 ? -10.204 106.607 40.761 1.00 29.10 ? 421  GLY A CA    1 
ATOM   3280 C C     . GLY A 1 421 ? -9.244  107.173 41.779 1.00 27.49 ? 421  GLY A C     1 
ATOM   3281 O O     . GLY A 1 421 ? -9.026  108.391 41.782 1.00 28.37 ? 421  GLY A O     1 
ATOM   3282 N N     . LEU A 1 422 ? -8.638  106.287 42.572 1.00 27.49 ? 422  LEU A N     1 
ATOM   3283 C CA    . LEU A 1 422 ? -7.583  106.615 43.558 1.00 27.88 ? 422  LEU A CA    1 
ATOM   3284 C C     . LEU A 1 422 ? -6.320  105.862 43.113 1.00 28.48 ? 422  LEU A C     1 
ATOM   3285 O O     . LEU A 1 422 ? -6.404  104.640 42.899 1.00 26.09 ? 422  LEU A O     1 
ATOM   3286 C CB    . LEU A 1 422 ? -8.065  106.138 44.943 1.00 29.13 ? 422  LEU A CB    1 
ATOM   3287 C CG    . LEU A 1 422 ? -6.956  105.913 45.982 1.00 31.15 ? 422  LEU A CG    1 
ATOM   3288 C CD1   . LEU A 1 422 ? -6.254  107.206 46.285 1.00 32.58 ? 422  LEU A CD1   1 
ATOM   3289 C CD2   . LEU A 1 422 ? -7.473  105.301 47.282 1.00 34.84 ? 422  LEU A CD2   1 
ATOM   3290 N N     . LEU A 1 423 ? -5.187  106.549 43.037 1.00 29.89 ? 423  LEU A N     1 
ATOM   3291 C CA    . LEU A 1 423 ? -3.824  105.950 42.908 1.00 27.76 ? 423  LEU A CA    1 
ATOM   3292 C C     . LEU A 1 423 ? -3.112  106.199 44.242 1.00 27.25 ? 423  LEU A C     1 
ATOM   3293 O O     . LEU A 1 423 ? -2.688  107.344 44.476 1.00 25.66 ? 423  LEU A O     1 
ATOM   3294 C CB    . LEU A 1 423 ? -3.110  106.616 41.736 1.00 28.94 ? 423  LEU A CB    1 
ATOM   3295 C CG    . LEU A 1 423 ? -3.801  106.421 40.395 1.00 33.49 ? 423  LEU A CG    1 
ATOM   3296 C CD1   . LEU A 1 423 ? -3.168  107.294 39.328 1.00 34.23 ? 423  LEU A CD1   1 
ATOM   3297 C CD2   . LEU A 1 423 ? -3.729  104.970 39.963 1.00 36.02 ? 423  LEU A CD2   1 
ATOM   3298 N N     . ALA A 1 424 ? -3.133  105.210 45.133 1.00 23.27 ? 424  ALA A N     1 
ATOM   3299 C CA    . ALA A 1 424 ? -2.529  105.314 46.477 1.00 25.22 ? 424  ALA A CA    1 
ATOM   3300 C C     . ALA A 1 424 ? -1.045  104.942 46.325 1.00 27.74 ? 424  ALA A C     1 
ATOM   3301 O O     . ALA A 1 424 ? -0.760  103.846 45.817 1.00 27.19 ? 424  ALA A O     1 
ATOM   3302 C CB    . ALA A 1 424 ? -3.259  104.447 47.500 1.00 26.68 ? 424  ALA A CB    1 
ATOM   3303 N N     . ILE A 1 425 ? -0.131  105.831 46.688 1.00 26.75 ? 425  ILE A N     1 
ATOM   3304 C CA    . ILE A 1 425 ? 1.306   105.654 46.345 1.00 29.04 ? 425  ILE A CA    1 
ATOM   3305 C C     . ILE A 1 425 ? 1.902   104.820 47.450 1.00 26.65 ? 425  ILE A C     1 
ATOM   3306 O O     . ILE A 1 425 ? 1.973   105.336 48.546 1.00 26.48 ? 425  ILE A O     1 
ATOM   3307 C CB    . ILE A 1 425 ? 2.030   107.010 46.235 1.00 30.80 ? 425  ILE A CB    1 
ATOM   3308 C CG1   . ILE A 1 425 ? 1.379   107.931 45.192 1.00 28.34 ? 425  ILE A CG1   1 
ATOM   3309 C CG2   . ILE A 1 425 ? 3.519   106.800 45.971 1.00 33.71 ? 425  ILE A CG2   1 
ATOM   3310 C CD1   . ILE A 1 425 ? 1.774   109.398 45.410 1.00 27.03 ? 425  ILE A CD1   1 
ATOM   3311 N N     . GLY A 1 426 ? 2.299   103.574 47.191 1.00 23.59 ? 426  GLY A N     1 
ATOM   3312 C CA    . GLY A 1 426 ? 3.064   102.788 48.167 1.00 24.30 ? 426  GLY A CA    1 
ATOM   3313 C C     . GLY A 1 426 ? 4.548   102.938 47.912 1.00 25.24 ? 426  GLY A C     1 
ATOM   3314 O O     . GLY A 1 426 ? 4.978   103.845 47.203 1.00 28.00 ? 426  GLY A O     1 
ATOM   3315 N N     . TRP A 1 427 ? 5.341   102.058 48.478 1.00 26.46 ? 427  TRP A N     1 
ATOM   3316 C CA    . TRP A 1 427 ? 6.813   102.254 48.473 1.00 30.15 ? 427  TRP A CA    1 
ATOM   3317 C C     . TRP A 1 427 ? 7.340   102.218 47.026 1.00 25.01 ? 427  TRP A C     1 
ATOM   3318 O O     . TRP A 1 427 ? 8.127   103.070 46.685 1.00 27.32 ? 427  TRP A O     1 
ATOM   3319 C CB    . TRP A 1 427 ? 7.448   101.197 49.358 1.00 36.97 ? 427  TRP A CB    1 
ATOM   3320 C CG    . TRP A 1 427 ? 7.301   101.569 50.804 1.00 54.62 ? 427  TRP A CG    1 
ATOM   3321 C CD1   . TRP A 1 427 ? 7.694   102.741 51.398 1.00 56.03 ? 427  TRP A CD1   1 
ATOM   3322 C CD2   . TRP A 1 427 ? 6.689   100.778 51.839 1.00 55.34 ? 427  TRP A CD2   1 
ATOM   3323 N NE1   . TRP A 1 427 ? 7.386   102.730 52.732 1.00 60.21 ? 427  TRP A NE1   1 
ATOM   3324 C CE2   . TRP A 1 427 ? 6.781   101.534 53.035 1.00 60.94 ? 427  TRP A CE2   1 
ATOM   3325 C CE3   . TRP A 1 427 ? 6.078   99.520  51.856 1.00 46.10 ? 427  TRP A CE3   1 
ATOM   3326 C CZ2   . TRP A 1 427 ? 6.320   101.048 54.255 1.00 51.89 ? 427  TRP A CZ2   1 
ATOM   3327 C CZ3   . TRP A 1 427 ? 5.646   99.036  53.058 1.00 53.67 ? 427  TRP A CZ3   1 
ATOM   3328 C CH2   . TRP A 1 427 ? 5.760   99.792  54.238 1.00 62.41 ? 427  TRP A CH2   1 
ATOM   3329 N N     . ARG A 1 428 ? 6.872   101.268 46.226 1.00 21.60 ? 428  ARG A N     1 
ATOM   3330 C CA    . ARG A 1 428 ? 7.380   101.067 44.838 1.00 22.33 ? 428  ARG A CA    1 
ATOM   3331 C C     . ARG A 1 428 ? 6.222   100.787 43.887 1.00 19.05 ? 428  ARG A C     1 
ATOM   3332 O O     . ARG A 1 428 ? 6.492   100.415 42.750 1.00 19.54 ? 428  ARG A O     1 
ATOM   3333 C CB    . ARG A 1 428 ? 8.388   99.920  44.871 1.00 22.41 ? 428  ARG A CB    1 
ATOM   3334 C CG    . ARG A 1 428 ? 9.832   100.361 44.719 1.00 25.99 ? 428  ARG A CG    1 
ATOM   3335 C CD    . ARG A 1 428 ? 10.596  100.204 45.936 1.00 27.84 ? 428  ARG A CD    1 
ATOM   3336 N NE    . ARG A 1 428 ? 12.044  100.422 45.884 1.00 25.90 ? 428  ARG A NE    1 
ATOM   3337 C CZ    . ARG A 1 428 ? 12.730  100.887 46.919 1.00 25.41 ? 428  ARG A CZ    1 
ATOM   3338 N NH1   . ARG A 1 428 ? 12.083  101.206 48.033 1.00 28.26 ? 428  ARG A NH1   1 
ATOM   3339 N NH2   . ARG A 1 428 ? 14.053  100.983 46.880 1.00 24.05 ? 428  ARG A NH2   1 
ATOM   3340 N N     . ASP A 1 429 ? 4.986   100.900 44.366 1.00 20.19 ? 429  ASP A N     1 
ATOM   3341 C CA    . ASP A 1 429 ? 3.768   100.516 43.624 1.00 21.87 ? 429  ASP A CA    1 
ATOM   3342 C C     . ASP A 1 429 ? 2.720   101.632 43.710 1.00 20.80 ? 429  ASP A C     1 
ATOM   3343 O O     . ASP A 1 429 ? 2.713   102.411 44.674 1.00 20.15 ? 429  ASP A O     1 
ATOM   3344 C CB    . ASP A 1 429 ? 3.229   99.191  44.141 1.00 22.49 ? 429  ASP A CB    1 
ATOM   3345 C CG    . ASP A 1 429 ? 2.364   99.336  45.381 1.00 25.62 ? 429  ASP A CG    1 
ATOM   3346 O OD1   . ASP A 1 429 ? 2.922   99.407  46.489 1.00 28.61 ? 429  ASP A OD1   1 
ATOM   3347 O OD2   . ASP A 1 429 ? 1.143   99.462  45.203 1.00 36.16 ? 429  ASP A OD2   1 
ATOM   3348 N N     . LEU A 1 430 ? 1.789   101.633 42.789 1.00 23.55 ? 430  LEU A N     1 
ATOM   3349 C CA    . LEU A 1 430 ? 0.448   102.284 42.990 1.00 25.89 ? 430  LEU A CA    1 
ATOM   3350 C C     . LEU A 1 430 ? -0.633  101.230 43.244 1.00 26.55 ? 430  LEU A C     1 
ATOM   3351 O O     . LEU A 1 430 ? -0.726  100.254 42.465 1.00 28.14 ? 430  LEU A O     1 
ATOM   3352 C CB    . LEU A 1 430 ? 0.053   103.073 41.750 1.00 25.83 ? 430  LEU A CB    1 
ATOM   3353 C CG    . LEU A 1 430 ? 1.070   104.129 41.311 1.00 28.27 ? 430  LEU A CG    1 
ATOM   3354 C CD1   . LEU A 1 430 ? 0.645   104.747 39.982 1.00 28.33 ? 430  LEU A CD1   1 
ATOM   3355 C CD2   . LEU A 1 430 ? 1.280   105.225 42.383 1.00 26.63 ? 430  LEU A CD2   1 
ATOM   3356 N N     . HIS A 1 431 ? -1.405  101.400 44.321 1.00 23.06 ? 431  HIS A N     1 
ATOM   3357 C CA    . HIS A 1 431 ? -2.712  100.725 44.455 1.00 22.95 ? 431  HIS A CA    1 
ATOM   3358 C C     . HIS A 1 431 ? -3.709  101.586 43.682 1.00 23.88 ? 431  HIS A C     1 
ATOM   3359 O O     . HIS A 1 431 ? -4.018  102.713 44.151 1.00 25.13 ? 431  HIS A O     1 
ATOM   3360 C CB    . HIS A 1 431 ? -3.170  100.587 45.910 1.00 24.72 ? 431  HIS A CB    1 
ATOM   3361 C CG    . HIS A 1 431 ? -2.404  99.563  46.646 1.00 28.90 ? 431  HIS A CG    1 
ATOM   3362 N ND1   . HIS A 1 431 ? -2.950  98.822  47.676 1.00 34.59 ? 431  HIS A ND1   1 
ATOM   3363 C CD2   . HIS A 1 431 ? -1.140  99.125  46.463 1.00 31.73 ? 431  HIS A CD2   1 
ATOM   3364 C CE1   . HIS A 1 431 ? -2.008  98.036  48.171 1.00 27.39 ? 431  HIS A CE1   1 
ATOM   3365 N NE2   . HIS A 1 431 ? -0.898  98.185  47.432 1.00 37.83 ? 431  HIS A NE2   1 
ATOM   3366 N N     . HIS A 1 432 ? -4.257  101.062 42.604 1.00 24.96 ? 432  HIS A N     1 
ATOM   3367 C CA    . HIS A 1 432 ? -5.246  101.815 41.781 1.00 25.61 ? 432  HIS A CA    1 
ATOM   3368 C C     . HIS A 1 432 ? -6.636  101.346 42.202 1.00 25.01 ? 432  HIS A C     1 
ATOM   3369 O O     . HIS A 1 432 ? -7.077  100.290 41.763 1.00 26.02 ? 432  HIS A O     1 
ATOM   3370 C CB    . HIS A 1 432 ? -4.938  101.669 40.284 1.00 24.86 ? 432  HIS A CB    1 
ATOM   3371 C CG    . HIS A 1 432 ? -5.963  102.288 39.391 1.00 27.41 ? 432  HIS A CG    1 
ATOM   3372 N ND1   . HIS A 1 432 ? -6.038  101.999 38.010 1.00 26.18 ? 432  HIS A ND1   1 
ATOM   3373 C CD2   . HIS A 1 432 ? -6.963  103.175 39.625 1.00 28.71 ? 432  HIS A CD2   1 
ATOM   3374 C CE1   . HIS A 1 432 ? -7.051  102.706 37.464 1.00 27.09 ? 432  HIS A CE1   1 
ATOM   3375 N NE2   . HIS A 1 432 ? -7.654  103.399 38.412 1.00 26.87 ? 432  HIS A NE2   1 
ATOM   3376 N N     . VAL A 1 433 ? -7.267  102.059 43.122 1.00 25.99 ? 433  VAL A N     1 
ATOM   3377 C CA    . VAL A 1 433 ? -8.607  101.654 43.613 1.00 28.08 ? 433  VAL A CA    1 
ATOM   3378 C C     . VAL A 1 433 ? -9.661  102.486 42.863 1.00 28.08 ? 433  VAL A C     1 
ATOM   3379 O O     . VAL A 1 433 ? -9.661  103.671 43.033 1.00 27.31 ? 433  VAL A O     1 
ATOM   3380 C CB    . VAL A 1 433 ? -8.710  101.815 45.142 1.00 27.09 ? 433  VAL A CB    1 
ATOM   3381 C CG1   . VAL A 1 433 ? -10.071 101.349 45.658 1.00 29.86 ? 433  VAL A CG1   1 
ATOM   3382 C CG2   . VAL A 1 433 ? -7.613  101.023 45.856 1.00 29.74 ? 433  VAL A CG2   1 
ATOM   3383 N N     . THR A 1 434 ? -10.492 101.857 42.032 1.00 27.58 ? 434  THR A N     1 
ATOM   3384 C CA    . THR A 1 434 ? -11.662 102.506 41.398 1.00 26.40 ? 434  THR A CA    1 
ATOM   3385 C C     . THR A 1 434 ? -12.836 102.143 42.273 1.00 24.46 ? 434  THR A C     1 
ATOM   3386 O O     . THR A 1 434 ? -13.092 100.948 42.428 1.00 24.85 ? 434  THR A O     1 
ATOM   3387 C CB    . THR A 1 434 ? -11.837 102.054 39.944 1.00 26.89 ? 434  THR A CB    1 
ATOM   3388 O OG1   . THR A 1 434 ? -10.658 102.520 39.317 1.00 29.14 ? 434  THR A OG1   1 
ATOM   3389 C CG2   . THR A 1 434 ? -13.077 102.606 39.281 1.00 29.32 ? 434  THR A CG2   1 
ATOM   3390 N N     . VAL A 1 435 ? -13.511 103.145 42.828 1.00 26.49 ? 435  VAL A N     1 
ATOM   3391 C CA    . VAL A 1 435 ? -14.759 102.892 43.596 1.00 25.73 ? 435  VAL A CA    1 
ATOM   3392 C C     . VAL A 1 435 ? -15.925 103.120 42.644 1.00 25.36 ? 435  VAL A C     1 
ATOM   3393 O O     . VAL A 1 435 ? -16.020 104.214 42.052 1.00 23.53 ? 435  VAL A O     1 
ATOM   3394 C CB    . VAL A 1 435 ? -14.805 103.726 44.883 1.00 27.11 ? 435  VAL A CB    1 
ATOM   3395 C CG1   . VAL A 1 435 ? -13.768 103.171 45.860 1.00 26.27 ? 435  VAL A CG1   1 
ATOM   3396 C CG2   . VAL A 1 435 ? -14.570 105.201 44.626 1.00 26.36 ? 435  VAL A CG2   1 
ATOM   3397 N N     . ILE A 1 436 ? -16.682 102.049 42.402 1.00 24.14 ? 436  ILE A N     1 
ATOM   3398 C CA    . ILE A 1 436 ? -17.811 102.096 41.454 1.00 22.85 ? 436  ILE A CA    1 
ATOM   3399 C C     . ILE A 1 436 ? -19.074 102.231 42.296 1.00 23.04 ? 436  ILE A C     1 
ATOM   3400 O O     . ILE A 1 436 ? -19.402 101.286 43.012 1.00 22.20 ? 436  ILE A O     1 
ATOM   3401 C CB    . ILE A 1 436 ? -17.835 100.878 40.548 1.00 24.34 ? 436  ILE A CB    1 
ATOM   3402 C CG1   . ILE A 1 436 ? -16.478 100.633 39.879 1.00 26.01 ? 436  ILE A CG1   1 
ATOM   3403 C CG2   . ILE A 1 436 ? -18.937 101.050 39.537 1.00 24.62 ? 436  ILE A CG2   1 
ATOM   3404 C CD1   . ILE A 1 436 ? -16.382 99.270  39.239 1.00 23.90 ? 436  ILE A CD1   1 
ATOM   3405 N N     . VAL A 1 437 ? -19.708 103.387 42.207 1.00 22.65 ? 437  VAL A N     1 
ATOM   3406 C CA    . VAL A 1 437 ? -20.946 103.735 42.961 1.00 24.12 ? 437  VAL A CA    1 
ATOM   3407 C C     . VAL A 1 437 ? -22.144 103.294 42.127 1.00 23.76 ? 437  VAL A C     1 
ATOM   3408 O O     . VAL A 1 437 ? -22.239 103.638 40.923 1.00 24.72 ? 437  VAL A O     1 
ATOM   3409 C CB    . VAL A 1 437 ? -20.968 105.226 43.311 1.00 27.33 ? 437  VAL A CB    1 
ATOM   3410 C CG1   . VAL A 1 437 ? -22.261 105.604 44.048 1.00 29.88 ? 437  VAL A CG1   1 
ATOM   3411 C CG2   . VAL A 1 437 ? -19.746 105.605 44.134 1.00 27.25 ? 437  VAL A CG2   1 
ATOM   3412 N N     . TYR A 1 438 ? -23.040 102.535 42.720 1.00 21.50 ? 438  TYR A N     1 
ATOM   3413 C CA    . TYR A 1 438 ? -24.156 101.913 41.969 1.00 24.10 ? 438  TYR A CA    1 
ATOM   3414 C C     . TYR A 1 438 ? -25.369 101.777 42.884 1.00 25.89 ? 438  TYR A C     1 
ATOM   3415 O O     . TYR A 1 438 ? -25.253 101.665 44.122 1.00 26.91 ? 438  TYR A O     1 
ATOM   3416 C CB    . TYR A 1 438 ? -23.723 100.572 41.373 1.00 25.70 ? 438  TYR A CB    1 
ATOM   3417 C CG    . TYR A 1 438 ? -23.420 99.516  42.395 1.00 24.66 ? 438  TYR A CG    1 
ATOM   3418 C CD1   . TYR A 1 438 ? -22.227 99.517  43.102 1.00 26.45 ? 438  TYR A CD1   1 
ATOM   3419 C CD2   . TYR A 1 438 ? -24.348 98.527  42.682 1.00 26.87 ? 438  TYR A CD2   1 
ATOM   3420 C CE1   . TYR A 1 438 ? -21.970 98.556  44.079 1.00 26.19 ? 438  TYR A CE1   1 
ATOM   3421 C CE2   . TYR A 1 438 ? -24.119 97.589  43.672 1.00 28.35 ? 438  TYR A CE2   1 
ATOM   3422 C CZ    . TYR A 1 438 ? -22.925 97.592  44.378 1.00 27.68 ? 438  TYR A CZ    1 
ATOM   3423 O OH    . TYR A 1 438 ? -22.711 96.654  45.365 1.00 27.89 ? 438  TYR A OH    1 
ATOM   3424 N N     . ASP A 1 439 ? -26.537 101.722 42.271 1.00 29.24 ? 439  ASP A N     1 
ATOM   3425 C CA    . ASP A 1 439 ? -27.799 101.535 43.029 1.00 31.28 ? 439  ASP A CA    1 
ATOM   3426 C C     . ASP A 1 439 ? -27.900 100.064 43.429 1.00 28.25 ? 439  ASP A C     1 
ATOM   3427 O O     . ASP A 1 439 ? -28.373 99.259  42.640 1.00 29.12 ? 439  ASP A O     1 
ATOM   3428 C CB    . ASP A 1 439 ? -29.000 102.045 42.242 1.00 34.21 ? 439  ASP A CB    1 
ATOM   3429 C CG    . ASP A 1 439 ? -30.275 101.959 43.057 1.00 35.90 ? 439  ASP A CG    1 
ATOM   3430 O OD1   . ASP A 1 439 ? -30.215 101.535 44.260 1.00 31.39 ? 439  ASP A OD1   1 
ATOM   3431 O OD2   . ASP A 1 439 ? -31.317 102.275 42.473 1.00 36.39 ? 439  ASP A OD2   1 
ATOM   3432 N N     . LYS A 1 440 ? -27.466 99.742  44.647 1.00 29.31 ? 440  LYS A N     1 
ATOM   3433 C CA    . LYS A 1 440 ? -27.387 98.350  45.161 1.00 31.40 ? 440  LYS A CA    1 
ATOM   3434 C C     . LYS A 1 440 ? -28.797 97.769  45.351 1.00 28.78 ? 440  LYS A C     1 
ATOM   3435 O O     . LYS A 1 440 ? -28.873 96.570  45.582 1.00 28.72 ? 440  LYS A O     1 
ATOM   3436 C CB    . LYS A 1 440 ? -26.594 98.320  46.477 1.00 33.45 ? 440  LYS A CB    1 
ATOM   3437 C CG    . LYS A 1 440 ? -27.425 98.162  47.748 1.00 39.30 ? 440  LYS A CG    1 
ATOM   3438 C CD    . LYS A 1 440 ? -27.341 99.282  48.678 1.00 47.38 ? 440  LYS A CD    1 
ATOM   3439 C CE    . LYS A 1 440 ? -28.510 99.289  49.644 1.00 48.54 ? 440  LYS A CE    1 
ATOM   3440 N NZ    . LYS A 1 440 ? -28.843 97.949  50.165 1.00 45.31 ? 440  LYS A NZ    1 
ATOM   3441 N N     . THR A 1 441 ? -29.860 98.592  45.360 1.00 30.56 ? 441  THR A N     1 
ATOM   3442 C CA    . THR A 1 441 ? -31.281 98.143  45.568 1.00 31.51 ? 441  THR A CA    1 
ATOM   3443 C C     . THR A 1 441 ? -31.932 97.776  44.234 1.00 32.30 ? 441  THR A C     1 
ATOM   3444 O O     . THR A 1 441 ? -33.006 97.190  44.276 1.00 33.98 ? 441  THR A O     1 
ATOM   3445 C CB    . THR A 1 441 ? -32.166 99.215  46.228 1.00 30.02 ? 441  THR A CB    1 
ATOM   3446 O OG1   . THR A 1 441 ? -32.431 100.159 45.195 1.00 30.64 ? 441  THR A OG1   1 
ATOM   3447 C CG2   . THR A 1 441 ? -31.515 99.931  47.393 1.00 30.38 ? 441  THR A CG2   1 
ATOM   3448 N N     . ASP A 1 442 ? -31.255 97.995  43.107 1.00 31.48 ? 442  ASP A N     1 
ATOM   3449 C CA    . ASP A 1 442 ? -31.841 97.812  41.754 1.00 32.90 ? 442  ASP A CA    1 
ATOM   3450 C C     . ASP A 1 442 ? -31.217 96.607  41.060 1.00 29.84 ? 442  ASP A C     1 
ATOM   3451 O O     . ASP A 1 442 ? -30.082 96.673  40.618 1.00 31.45 ? 442  ASP A O     1 
ATOM   3452 C CB    . ASP A 1 442 ? -31.617 99.097  40.957 1.00 33.43 ? 442  ASP A CB    1 
ATOM   3453 C CG    . ASP A 1 442 ? -32.200 99.062  39.566 1.00 37.42 ? 442  ASP A CG    1 
ATOM   3454 O OD1   . ASP A 1 442 ? -32.543 97.956  39.093 1.00 42.60 ? 442  ASP A OD1   1 
ATOM   3455 O OD2   . ASP A 1 442 ? -32.280 100.142 38.969 1.00 43.31 ? 442  ASP A OD2   1 
ATOM   3456 N N     . PRO A 1 443 ? -31.954 95.510  40.812 1.00 32.09 ? 443  PRO A N     1 
ATOM   3457 C CA    . PRO A 1 443 ? -31.372 94.333  40.176 1.00 34.52 ? 443  PRO A CA    1 
ATOM   3458 C C     . PRO A 1 443 ? -30.753 94.608  38.808 1.00 35.36 ? 443  PRO A C     1 
ATOM   3459 O O     . PRO A 1 443 ? -29.829 93.904  38.463 1.00 34.93 ? 443  PRO A O     1 
ATOM   3460 C CB    . PRO A 1 443 ? -32.545 93.349  39.985 1.00 36.02 ? 443  PRO A CB    1 
ATOM   3461 C CG    . PRO A 1 443 ? -33.572 93.809  40.969 1.00 36.98 ? 443  PRO A CG    1 
ATOM   3462 C CD    . PRO A 1 443 ? -33.366 95.302  41.151 1.00 34.27 ? 443  PRO A CD    1 
ATOM   3463 N N     . ASP A 1 444 ? -31.266 95.577  38.046 1.00 35.73 ? 444  ASP A N     1 
ATOM   3464 C CA    . ASP A 1 444 ? -30.699 95.849  36.697 1.00 37.45 ? 444  ASP A CA    1 
ATOM   3465 C C     . ASP A 1 444 ? -29.319 96.506  36.848 1.00 31.16 ? 444  ASP A C     1 
ATOM   3466 O O     . ASP A 1 444 ? -28.434 96.152  36.066 1.00 32.93 ? 444  ASP A O     1 
ATOM   3467 C CB    . ASP A 1 444 ? -31.626 96.695  35.822 1.00 39.36 ? 444  ASP A CB    1 
ATOM   3468 C CG    . ASP A 1 444 ? -32.868 95.925  35.407 1.00 49.23 ? 444  ASP A CG    1 
ATOM   3469 O OD1   . ASP A 1 444 ? -32.764 94.710  35.144 1.00 50.98 ? 444  ASP A OD1   1 
ATOM   3470 O OD2   . ASP A 1 444 ? -33.929 96.538  35.383 1.00 54.70 ? 444  ASP A OD2   1 
ATOM   3471 N N     . GLU A 1 445 ? -29.145 97.404  37.812 1.00 30.03 ? 445  GLU A N     1 
ATOM   3472 C CA    . GLU A 1 445 ? -27.850 98.058  38.104 1.00 32.03 ? 445  GLU A CA    1 
ATOM   3473 C C     . GLU A 1 445 ? -26.851 97.039  38.683 1.00 30.33 ? 445  GLU A C     1 
ATOM   3474 O O     . GLU A 1 445 ? -25.674 97.092  38.264 1.00 31.16 ? 445  GLU A O     1 
ATOM   3475 C CB    . GLU A 1 445 ? -28.008 99.242  39.045 1.00 34.14 ? 445  GLU A CB    1 
ATOM   3476 C CG    . GLU A 1 445 ? -28.813 100.369 38.436 1.00 44.72 ? 445  GLU A CG    1 
ATOM   3477 C CD    . GLU A 1 445 ? -28.154 100.969 37.207 1.00 46.95 ? 445  GLU A CD    1 
ATOM   3478 O OE1   . GLU A 1 445 ? -27.079 101.538 37.392 1.00 43.60 ? 445  GLU A OE1   1 
ATOM   3479 O OE2   . GLU A 1 445 ? -28.722 100.836 36.079 1.00 50.61 ? 445  GLU A OE2   1 
ATOM   3480 N N     . ARG A 1 446 ? -27.289 96.150  39.577 1.00 28.16 ? 446  ARG A N     1 
ATOM   3481 C CA    . ARG A 1 446 ? -26.416 95.074  40.127 1.00 28.06 ? 446  ARG A CA    1 
ATOM   3482 C C     . ARG A 1 446 ? -25.967 94.141  39.009 1.00 31.31 ? 446  ARG A C     1 
ATOM   3483 O O     . ARG A 1 446 ? -24.815 93.717  39.051 1.00 29.44 ? 446  ARG A O     1 
ATOM   3484 C CB    . ARG A 1 446 ? -27.118 94.277  41.223 1.00 31.63 ? 446  ARG A CB    1 
ATOM   3485 C CG    . ARG A 1 446 ? -27.463 95.111  42.444 1.00 30.53 ? 446  ARG A CG    1 
ATOM   3486 C CD    . ARG A 1 446 ? -27.886 94.232  43.602 1.00 33.10 ? 446  ARG A CD    1 
ATOM   3487 N NE    . ARG A 1 446 ? -29.019 93.341  43.345 1.00 33.50 ? 446  ARG A NE    1 
ATOM   3488 C CZ    . ARG A 1 446 ? -30.195 93.362  43.994 1.00 30.88 ? 446  ARG A CZ    1 
ATOM   3489 N NH1   . ARG A 1 446 ? -30.455 94.250  44.936 1.00 32.38 ? 446  ARG A NH1   1 
ATOM   3490 N NH2   . ARG A 1 446 ? -31.106 92.457  43.709 1.00 31.00 ? 446  ARG A NH2   1 
ATOM   3491 N N     . LYS A 1 447 ? -26.827 93.828  38.037 1.00 31.28 ? 447  LYS A N     1 
ATOM   3492 C CA    . LYS A 1 447 ? -26.437 92.973  36.886 1.00 29.18 ? 447  LYS A CA    1 
ATOM   3493 C C     . LYS A 1 447 ? -25.363 93.679  36.056 1.00 30.52 ? 447  LYS A C     1 
ATOM   3494 O O     . LYS A 1 447 ? -24.344 93.065  35.735 1.00 32.60 ? 447  LYS A O     1 
ATOM   3495 C CB    . LYS A 1 447 ? -27.662 92.648  36.036 1.00 34.06 ? 447  LYS A CB    1 
ATOM   3496 C CG    . LYS A 1 447 ? -27.404 91.653  34.923 1.00 36.65 ? 447  LYS A CG    1 
ATOM   3497 C CD    . LYS A 1 447 ? -28.685 91.253  34.223 1.00 43.79 ? 447  LYS A CD    1 
ATOM   3498 C CE    . LYS A 1 447 ? -28.405 90.372  33.023 1.00 48.33 ? 447  LYS A CE    1 
ATOM   3499 N NZ    . LYS A 1 447 ? -27.682 91.144  31.988 1.00 51.41 ? 447  LYS A NZ    1 
ATOM   3500 N N     . LYS A 1 448 ? -25.530 94.951  35.752 1.00 31.46 ? 448  LYS A N     1 
ATOM   3501 C CA    . LYS A 1 448 ? -24.521 95.727  34.976 1.00 33.09 ? 448  LYS A CA    1 
ATOM   3502 C C     . LYS A 1 448 ? -23.194 95.781  35.765 1.00 30.77 ? 448  LYS A C     1 
ATOM   3503 O O     . LYS A 1 448 ? -22.124 95.668  35.158 1.00 28.27 ? 448  LYS A O     1 
ATOM   3504 C CB    . LYS A 1 448 ? -24.985 97.173  34.740 1.00 37.04 ? 448  LYS A CB    1 
ATOM   3505 C CG    . LYS A 1 448 ? -26.013 97.335  33.632 1.00 44.35 ? 448  LYS A CG    1 
ATOM   3506 C CD    . LYS A 1 448 ? -26.699 98.704  33.609 1.00 53.75 ? 448  LYS A CD    1 
ATOM   3507 C CE    . LYS A 1 448 ? -26.018 99.699  32.692 1.00 59.08 ? 448  LYS A CE    1 
ATOM   3508 N NZ    . LYS A 1 448 ? -26.654 101.038 32.750 1.00 66.50 ? 448  LYS A NZ    1 
ATOM   3509 N N     . LEU A 1 449 ? -23.275 96.066  37.056 1.00 26.38 ? 449  LEU A N     1 
ATOM   3510 C CA    . LEU A 1 449 ? -22.078 96.204  37.917 1.00 26.87 ? 449  LEU A CA    1 
ATOM   3511 C C     . LEU A 1 449 ? -21.311 94.892  37.909 1.00 24.68 ? 449  LEU A C     1 
ATOM   3512 O O     . LEU A 1 449 ? -20.090 94.922  37.681 1.00 26.09 ? 449  LEU A O     1 
ATOM   3513 C CB    . LEU A 1 449 ? -22.457 96.557  39.344 1.00 30.68 ? 449  LEU A CB    1 
ATOM   3514 C CG    . LEU A 1 449 ? -21.201 96.606  40.192 1.00 33.11 ? 449  LEU A CG    1 
ATOM   3515 C CD1   . LEU A 1 449 ? -20.488 97.920  39.993 1.00 30.67 ? 449  LEU A CD1   1 
ATOM   3516 C CD2   . LEU A 1 449 ? -21.471 96.262  41.602 1.00 36.07 ? 449  LEU A CD2   1 
ATOM   3517 N N     . ASP A 1 450 ? -22.013 93.781  38.072 1.00 29.59 ? 450  ASP A N     1 
ATOM   3518 C CA    . ASP A 1 450 ? -21.398 92.424  38.097 1.00 29.87 ? 450  ASP A CA    1 
ATOM   3519 C C     . ASP A 1 450 ? -20.706 92.143  36.766 1.00 32.44 ? 450  ASP A C     1 
ATOM   3520 O O     . ASP A 1 450 ? -19.570 91.631  36.766 1.00 29.56 ? 450  ASP A O     1 
ATOM   3521 C CB    . ASP A 1 450 ? -22.436 91.342  38.367 1.00 30.95 ? 450  ASP A CB    1 
ATOM   3522 C CG    . ASP A 1 450 ? -21.821 90.022  38.822 1.00 39.14 ? 450  ASP A CG    1 
ATOM   3523 O OD1   . ASP A 1 450 ? -20.677 90.020  39.358 1.00 32.25 ? 450  ASP A OD1   1 
ATOM   3524 O OD2   . ASP A 1 450 ? -22.524 89.012  38.720 1.00 40.86 ? 450  ASP A OD2   1 
ATOM   3525 N N     . GLU A 1 451 ? -21.373 92.423  35.639 1.00 30.77 ? 451  GLU A N     1 
ATOM   3526 C CA    . GLU A 1 451 ? -20.774 92.168  34.307 1.00 31.91 ? 451  GLU A CA    1 
ATOM   3527 C C     . GLU A 1 451 ? -19.563 93.064  34.115 1.00 28.88 ? 451  GLU A C     1 
ATOM   3528 O O     . GLU A 1 451 ? -18.540 92.596  33.606 1.00 28.55 ? 451  GLU A O     1 
ATOM   3529 C CB    . GLU A 1 451 ? -21.788 92.432  33.191 1.00 38.26 ? 451  GLU A CB    1 
ATOM   3530 C CG    . GLU A 1 451 ? -22.812 91.329  33.174 1.00 47.99 ? 451  GLU A CG    1 
ATOM   3531 C CD    . GLU A 1 451 ? -24.011 91.556  32.275 1.00 57.05 ? 451  GLU A CD    1 
ATOM   3532 O OE1   . GLU A 1 451 ? -25.043 90.831  32.500 1.00 48.29 ? 451  GLU A OE1   1 
ATOM   3533 O OE2   . GLU A 1 451 ? -23.898 92.436  31.361 1.00 46.70 ? 451  GLU A OE2   1 
ATOM   3534 N N     . LEU A 1 452 ? -19.670 94.324  34.504 1.00 26.47 ? 452  LEU A N     1 
ATOM   3535 C CA    . LEU A 1 452 ? -18.544 95.287  34.393 1.00 24.63 ? 452  LEU A CA    1 
ATOM   3536 C C     . LEU A 1 452 ? -17.349 94.789  35.215 1.00 25.53 ? 452  LEU A C     1 
ATOM   3537 O O     . LEU A 1 452 ? -16.170 94.864  34.736 1.00 23.82 ? 452  LEU A O     1 
ATOM   3538 C CB    . LEU A 1 452 ? -19.033 96.637  34.908 1.00 27.06 ? 452  LEU A CB    1 
ATOM   3539 C CG    . LEU A 1 452 ? -17.957 97.660  35.215 1.00 25.81 ? 452  LEU A CG    1 
ATOM   3540 C CD1   . LEU A 1 452 ? -17.221 98.061  33.954 1.00 25.90 ? 452  LEU A CD1   1 
ATOM   3541 C CD2   . LEU A 1 452 ? -18.579 98.863  35.937 1.00 29.94 ? 452  LEU A CD2   1 
ATOM   3542 N N     . PHE A 1 453 ? -17.602 94.363  36.439 1.00 25.04 ? 453  PHE A N     1 
ATOM   3543 C CA    . PHE A 1 453 ? -16.508 93.929  37.342 1.00 25.89 ? 453  PHE A CA    1 
ATOM   3544 C C     . PHE A 1 453 ? -15.744 92.762  36.702 1.00 26.89 ? 453  PHE A C     1 
ATOM   3545 O O     . PHE A 1 453 ? -14.521 92.794  36.694 1.00 25.85 ? 453  PHE A O     1 
ATOM   3546 C CB    . PHE A 1 453 ? -17.013 93.490  38.702 1.00 24.27 ? 453  PHE A CB    1 
ATOM   3547 C CG    . PHE A 1 453 ? -15.951 93.611  39.764 1.00 22.47 ? 453  PHE A CG    1 
ATOM   3548 C CD1   . PHE A 1 453 ? -15.086 92.563  40.027 1.00 23.75 ? 453  PHE A CD1   1 
ATOM   3549 C CD2   . PHE A 1 453 ? -15.806 94.795  40.475 1.00 23.01 ? 453  PHE A CD2   1 
ATOM   3550 C CE1   . PHE A 1 453 ? -14.115 92.674  41.017 1.00 24.40 ? 453  PHE A CE1   1 
ATOM   3551 C CE2   . PHE A 1 453 ? -14.832 94.905  41.458 1.00 22.87 ? 453  PHE A CE2   1 
ATOM   3552 C CZ    . PHE A 1 453 ? -13.976 93.853  41.713 1.00 23.15 ? 453  PHE A CZ    1 
ATOM   3553 N N     . ASN A 1 454 ? -16.467 91.765  36.196 1.00 27.70 ? 454  ASN A N     1 
ATOM   3554 C CA    . ASN A 1 454 ? -15.869 90.572  35.539 1.00 26.24 ? 454  ASN A CA    1 
ATOM   3555 C C     . ASN A 1 454 ? -14.978 91.011  34.392 1.00 26.19 ? 454  ASN A C     1 
ATOM   3556 O O     . ASN A 1 454 ? -13.908 90.443  34.199 1.00 30.03 ? 454  ASN A O     1 
ATOM   3557 C CB    . ASN A 1 454 ? -16.952 89.587  35.140 1.00 29.17 ? 454  ASN A CB    1 
ATOM   3558 C CG    . ASN A 1 454 ? -17.401 88.792  36.343 1.00 32.10 ? 454  ASN A CG    1 
ATOM   3559 O OD1   . ASN A 1 454 ? -16.571 88.314  37.099 1.00 39.58 ? 454  ASN A OD1   1 
ATOM   3560 N ND2   . ASN A 1 454 ? -18.688 88.690  36.569 1.00 35.66 ? 454  ASN A ND2   1 
ATOM   3561 N N     . ILE A 1 455 ? -15.411 91.995  33.622 1.00 27.88 ? 455  ILE A N     1 
ATOM   3562 C CA    . ILE A 1 455 ? -14.653 92.517  32.472 1.00 26.69 ? 455  ILE A CA    1 
ATOM   3563 C C     . ILE A 1 455 ? -13.404 93.227  32.978 1.00 29.22 ? 455  ILE A C     1 
ATOM   3564 O O     . ILE A 1 455 ? -12.355 93.100  32.360 1.00 27.52 ? 455  ILE A O     1 
ATOM   3565 C CB    . ILE A 1 455 ? -15.563 93.453  31.635 1.00 29.48 ? 455  ILE A CB    1 
ATOM   3566 C CG1   . ILE A 1 455 ? -16.667 92.672  30.927 1.00 32.87 ? 455  ILE A CG1   1 
ATOM   3567 C CG2   . ILE A 1 455 ? -14.759 94.317  30.683 1.00 27.70 ? 455  ILE A CG2   1 
ATOM   3568 C CD1   . ILE A 1 455 ? -17.660 93.580  30.212 1.00 36.21 ? 455  ILE A CD1   1 
ATOM   3569 N N     . LEU A 1 456 ? -13.509 94.061  34.008 1.00 25.34 ? 456  LEU A N     1 
ATOM   3570 C CA    . LEU A 1 456 ? -12.325 94.809  34.511 1.00 23.71 ? 456  LEU A CA    1 
ATOM   3571 C C     . LEU A 1 456 ? -11.258 93.802  34.960 1.00 21.44 ? 456  LEU A C     1 
ATOM   3572 O O     . LEU A 1 456 ? -10.093 94.044  34.704 1.00 23.92 ? 456  LEU A O     1 
ATOM   3573 C CB    . LEU A 1 456 ? -12.766 95.695  35.678 1.00 24.40 ? 456  LEU A CB    1 
ATOM   3574 C CG    . LEU A 1 456 ? -13.679 96.865  35.292 1.00 23.64 ? 456  LEU A CG    1 
ATOM   3575 C CD1   . LEU A 1 456 ? -14.197 97.539  36.551 1.00 25.86 ? 456  LEU A CD1   1 
ATOM   3576 C CD2   . LEU A 1 456 ? -12.973 97.876  34.400 1.00 21.90 ? 456  LEU A CD2   1 
ATOM   3577 N N     . VAL A 1 457 ? -11.673 92.757  35.662 1.00 22.92 ? 457  VAL A N     1 
ATOM   3578 C CA    . VAL A 1 457 ? -10.736 91.717  36.185 1.00 23.61 ? 457  VAL A CA    1 
ATOM   3579 C C     . VAL A 1 457 ? -10.018 91.083  34.995 1.00 26.35 ? 457  VAL A C     1 
ATOM   3580 O O     . VAL A 1 457 ? -8.769  91.122  34.972 1.00 23.92 ? 457  VAL A O     1 
ATOM   3581 C CB    . VAL A 1 457 ? -11.478 90.677  37.007 1.00 24.22 ? 457  VAL A CB    1 
ATOM   3582 C CG1   . VAL A 1 457 ? -10.620 89.446  37.289 1.00 24.50 ? 457  VAL A CG1   1 
ATOM   3583 C CG2   . VAL A 1 457 ? -11.979 91.318  38.285 1.00 25.67 ? 457  VAL A CG2   1 
ATOM   3584 N N     . ASP A 1 458 ? -10.794 90.594  34.020 1.00 29.45 ? 458  ASP A N     1 
ATOM   3585 C CA    . ASP A 1 458 ? -10.269 89.824  32.849 1.00 28.81 ? 458  ASP A CA    1 
ATOM   3586 C C     . ASP A 1 458 ? -9.397  90.744  32.012 1.00 26.11 ? 458  ASP A C     1 
ATOM   3587 O O     . ASP A 1 458 ? -8.291  90.334  31.625 1.00 28.75 ? 458  ASP A O     1 
ATOM   3588 C CB    . ASP A 1 458 ? -11.396 89.208  32.021 1.00 28.12 ? 458  ASP A CB    1 
ATOM   3589 C CG    . ASP A 1 458 ? -12.181 88.135  32.758 1.00 31.83 ? 458  ASP A CG    1 
ATOM   3590 O OD1   . ASP A 1 458 ? -11.777 87.724  33.856 1.00 36.01 ? 458  ASP A OD1   1 
ATOM   3591 O OD2   . ASP A 1 458 ? -13.255 87.800  32.285 1.00 37.27 ? 458  ASP A OD2   1 
ATOM   3592 N N     . GLU A 1 459 ? -9.798  91.990  31.781 1.00 27.55 ? 459  GLU A N     1 
ATOM   3593 C CA    . GLU A 1 459 ? -8.950  92.904  30.958 1.00 27.05 ? 459  GLU A CA    1 
ATOM   3594 C C     . GLU A 1 459 ? -7.666  93.277  31.682 1.00 28.39 ? 459  GLU A C     1 
ATOM   3595 O O     . GLU A 1 459 ? -6.610  93.428  31.009 1.00 26.12 ? 459  GLU A O     1 
ATOM   3596 C CB    . GLU A 1 459 ? -9.713  94.154  30.521 1.00 29.33 ? 459  GLU A CB    1 
ATOM   3597 C CG    . GLU A 1 459 ? -10.837 93.794  29.579 1.00 30.58 ? 459  GLU A CG    1 
ATOM   3598 C CD    . GLU A 1 459 ? -11.489 94.987  28.878 1.00 34.95 ? 459  GLU A CD    1 
ATOM   3599 O OE1   . GLU A 1 459 ? -11.399 96.131  29.361 1.00 35.18 ? 459  GLU A OE1   1 
ATOM   3600 O OE2   . GLU A 1 459 ? -12.024 94.758  27.816 1.00 38.92 ? 459  GLU A OE2   1 
ATOM   3601 N N     . ALA A 1 460 ? -7.724  93.540  32.999 1.00 24.97 ? 460  ALA A N     1 
ATOM   3602 C CA    . ALA A 1 460 ? -6.500  93.848  33.782 1.00 23.81 ? 460  ALA A CA    1 
ATOM   3603 C C     . ALA A 1 460 ? -5.545  92.642  33.718 1.00 20.05 ? 460  ALA A C     1 
ATOM   3604 O O     . ALA A 1 460 ? -4.358  92.834  33.472 1.00 21.78 ? 460  ALA A O     1 
ATOM   3605 C CB    . ALA A 1 460 ? -6.868  94.188  35.220 1.00 25.54 ? 460  ALA A CB    1 
ATOM   3606 N N     . ALA A 1 461 ? -6.063  91.442  33.944 1.00 21.77 ? 461  ALA A N     1 
ATOM   3607 C CA    . ALA A 1 461 ? -5.252  90.200  33.957 1.00 23.99 ? 461  ALA A CA    1 
ATOM   3608 C C     . ALA A 1 461 ? -4.665  89.951  32.558 1.00 26.98 ? 461  ALA A C     1 
ATOM   3609 O O     . ALA A 1 461 ? -3.488  89.557  32.483 1.00 25.82 ? 461  ALA A O     1 
ATOM   3610 C CB    . ALA A 1 461 ? -6.085  89.038  34.383 1.00 24.89 ? 461  ALA A CB    1 
ATOM   3611 N N     . ALA A 1 462 ? -5.410  90.258  31.487 1.00 26.17 ? 462  ALA A N     1 
ATOM   3612 C CA    . ALA A 1 462 ? -4.860  90.156  30.117 1.00 28.35 ? 462  ALA A CA    1 
ATOM   3613 C C     . ALA A 1 462 ? -3.698  91.129  29.944 1.00 27.48 ? 462  ALA A C     1 
ATOM   3614 O O     . ALA A 1 462 ? -2.885  90.905  29.048 1.00 30.37 ? 462  ALA A O     1 
ATOM   3615 C CB    . ALA A 1 462 ? -5.939  90.367  29.060 1.00 28.87 ? 462  ALA A CB    1 
ATOM   3616 N N     . GLU A 1 463 ? -3.584  92.181  30.744 1.00 27.46 ? 463  GLU A N     1 
ATOM   3617 C CA    . GLU A 1 463 ? -2.453  93.139  30.663 1.00 24.71 ? 463  GLU A CA    1 
ATOM   3618 C C     . GLU A 1 463 ? -1.421  92.858  31.777 1.00 25.13 ? 463  GLU A C     1 
ATOM   3619 O O     . GLU A 1 463 ? -0.526  93.714  32.002 1.00 23.89 ? 463  GLU A O     1 
ATOM   3620 C CB    . GLU A 1 463 ? -2.953  94.577  30.775 1.00 28.62 ? 463  GLU A CB    1 
ATOM   3621 C CG    . GLU A 1 463 ? -3.636  95.122  29.521 1.00 33.72 ? 463  GLU A CG    1 
ATOM   3622 C CD    . GLU A 1 463 ? -2.706  95.353  28.325 1.00 28.48 ? 463  GLU A CD    1 
ATOM   3623 O OE1   . GLU A 1 463 ? -1.603  95.878  28.474 1.00 32.77 ? 463  GLU A OE1   1 
ATOM   3624 O OE2   . GLU A 1 463 ? -3.089  94.952  27.276 1.00 38.64 ? 463  GLU A OE2   1 
ATOM   3625 N N     . GLY A 1 464 ? -1.523  91.714  32.471 1.00 25.16 ? 464  GLY A N     1 
ATOM   3626 C CA    . GLY A 1 464 ? -0.506  91.411  33.500 1.00 25.27 ? 464  GLY A CA    1 
ATOM   3627 C C     . GLY A 1 464 ? -0.715  92.209  34.777 1.00 24.96 ? 464  GLY A C     1 
ATOM   3628 O O     . GLY A 1 464 ? 0.283   92.422  35.546 1.00 23.16 ? 464  GLY A O     1 
ATOM   3629 N N     . TYR A 1 465 ? -1.960  92.638  35.035 1.00 22.63 ? 465  TYR A N     1 
ATOM   3630 C CA    . TYR A 1 465 ? -2.277  93.433  36.260 1.00 23.12 ? 465  TYR A CA    1 
ATOM   3631 C C     . TYR A 1 465 ? -3.196  92.602  37.170 1.00 21.57 ? 465  TYR A C     1 
ATOM   3632 O O     . TYR A 1 465 ? -4.210  92.050  36.722 1.00 23.33 ? 465  TYR A O     1 
ATOM   3633 C CB    . TYR A 1 465 ? -2.883  94.809  35.945 1.00 24.32 ? 465  TYR A CB    1 
ATOM   3634 C CG    . TYR A 1 465 ? -2.105  95.750  35.049 1.00 24.01 ? 465  TYR A CG    1 
ATOM   3635 C CD1   . TYR A 1 465 ? -0.785  96.083  35.293 1.00 21.75 ? 465  TYR A CD1   1 
ATOM   3636 C CD2   . TYR A 1 465 ? -2.734  96.337  33.946 1.00 26.06 ? 465  TYR A CD2   1 
ATOM   3637 C CE1   . TYR A 1 465 ? -0.113  96.997  34.507 1.00 24.16 ? 465  TYR A CE1   1 
ATOM   3638 C CE2   . TYR A 1 465 ? -2.058  97.215  33.118 1.00 28.25 ? 465  TYR A CE2   1 
ATOM   3639 C CZ    . TYR A 1 465 ? -0.754  97.549  33.402 1.00 26.97 ? 465  TYR A CZ    1 
ATOM   3640 O OH    . TYR A 1 465 ? -0.124  98.443  32.617 1.00 24.92 ? 465  TYR A OH    1 
ATOM   3641 N N     . GLY A 1 466 ? -2.819  92.480  38.456 1.00 22.95 ? 466  GLY A N     1 
ATOM   3642 C CA    . GLY A 1 466 ? -3.657  91.728  39.405 1.00 20.33 ? 466  GLY A CA    1 
ATOM   3643 C C     . GLY A 1 466 ? -4.151  92.644  40.524 1.00 19.52 ? 466  GLY A C     1 
ATOM   3644 O O     . GLY A 1 466 ? -3.456  93.616  40.845 1.00 21.43 ? 466  GLY A O     1 
ATOM   3645 N N     . GLU A 1 467 ? -5.245  92.258  41.181 1.00 21.48 ? 467  GLU A N     1 
ATOM   3646 C CA    . GLU A 1 467 ? -5.851  93.046  42.277 1.00 20.93 ? 467  GLU A CA    1 
ATOM   3647 C C     . GLU A 1 467 ? -5.140  92.681  43.583 1.00 20.94 ? 467  GLU A C     1 
ATOM   3648 O O     . GLU A 1 467 ? -4.785  91.496  43.730 1.00 20.16 ? 467  GLU A O     1 
ATOM   3649 C CB    . GLU A 1 467 ? -7.350  92.775  42.348 1.00 22.43 ? 467  GLU A CB    1 
ATOM   3650 C CG    . GLU A 1 467 ? -8.142  93.525  41.280 1.00 27.08 ? 467  GLU A CG    1 
ATOM   3651 C CD    . GLU A 1 467 ? -7.982  92.931  39.883 1.00 33.59 ? 467  GLU A CD    1 
ATOM   3652 O OE1   . GLU A 1 467 ? -7.143  93.479  39.097 1.00 30.88 ? 467  GLU A OE1   1 
ATOM   3653 O OE2   . GLU A 1 467 ? -8.677  91.915  39.593 1.00 33.55 ? 467  GLU A OE2   1 
ATOM   3654 N N     . TYR A 1 468 ? -4.976  93.647  44.497 1.00 17.93 ? 468  TYR A N     1 
ATOM   3655 C CA    . TYR A 1 468 ? -4.356  93.431  45.836 1.00 19.21 ? 468  TYR A CA    1 
ATOM   3656 C C     . TYR A 1 468 ? -5.427  92.938  46.829 1.00 19.15 ? 468  TYR A C     1 
ATOM   3657 O O     . TYR A 1 468 ? -5.068  92.385  47.922 1.00 17.97 ? 468  TYR A O     1 
ATOM   3658 C CB    . TYR A 1 468 ? -3.620  94.700  46.330 1.00 18.62 ? 468  TYR A CB    1 
ATOM   3659 C CG    . TYR A 1 468 ? -4.429  95.638  47.191 1.00 21.16 ? 468  TYR A CG    1 
ATOM   3660 C CD1   . TYR A 1 468 ? -5.423  96.495  46.687 1.00 23.98 ? 468  TYR A CD1   1 
ATOM   3661 C CD2   . TYR A 1 468 ? -4.238  95.638  48.562 1.00 19.35 ? 468  TYR A CD2   1 
ATOM   3662 C CE1   . TYR A 1 468 ? -6.208  97.298  47.518 1.00 24.47 ? 468  TYR A CE1   1 
ATOM   3663 C CE2   . TYR A 1 468 ? -5.018  96.418  49.395 1.00 22.68 ? 468  TYR A CE2   1 
ATOM   3664 C CZ    . TYR A 1 468 ? -5.979  97.298  48.894 1.00 26.52 ? 468  TYR A CZ    1 
ATOM   3665 O OH    . TYR A 1 468 ? -6.718  98.040  49.821 1.00 24.65 ? 468  TYR A OH    1 
ATOM   3666 N N     . ARG A 1 469 ? -6.700  93.194  46.527 1.00 18.82 ? 469  ARG A N     1 
ATOM   3667 C CA    . ARG A 1 469 ? -7.824  93.000  47.482 1.00 18.38 ? 469  ARG A CA    1 
ATOM   3668 C C     . ARG A 1 469 ? -9.117  92.955  46.698 1.00 21.27 ? 469  ARG A C     1 
ATOM   3669 O O     . ARG A 1 469 ? -9.235  93.676  45.640 1.00 22.31 ? 469  ARG A O     1 
ATOM   3670 C CB    . ARG A 1 469 ? -7.771  94.143  48.477 1.00 17.85 ? 469  ARG A CB    1 
ATOM   3671 C CG    . ARG A 1 469 ? -8.627  93.991  49.719 1.00 21.16 ? 469  ARG A CG    1 
ATOM   3672 C CD    . ARG A 1 469 ? -8.360  95.195  50.580 1.00 20.97 ? 469  ARG A CD    1 
ATOM   3673 N NE    . ARG A 1 469 ? -9.184  95.229  51.798 1.00 20.68 ? 469  ARG A NE    1 
ATOM   3674 C CZ    . ARG A 1 469 ? -9.208  96.254  52.626 1.00 22.47 ? 469  ARG A CZ    1 
ATOM   3675 N NH1   . ARG A 1 469 ? -8.463  97.306  52.363 1.00 22.64 ? 469  ARG A NH1   1 
ATOM   3676 N NH2   . ARG A 1 469 ? -9.975  96.238  53.698 1.00 21.67 ? 469  ARG A NH2   1 
ATOM   3677 N N     . THR A 1 470 ? -10.074 92.160  47.153 1.00 20.06 ? 470  THR A N     1 
ATOM   3678 C CA    . THR A 1 470 ? -11.327 92.079  46.395 1.00 22.56 ? 470  THR A CA    1 
ATOM   3679 C C     . THR A 1 470 ? -12.483 91.708  47.309 1.00 24.73 ? 470  THR A C     1 
ATOM   3680 O O     . THR A 1 470 ? -12.306 91.353  48.491 1.00 21.45 ? 470  THR A O     1 
ATOM   3681 C CB    . THR A 1 470 ? -11.175 91.120  45.214 1.00 21.46 ? 470  THR A CB    1 
ATOM   3682 O OG1   . THR A 1 470 ? -12.194 91.468  44.272 1.00 21.29 ? 470  THR A OG1   1 
ATOM   3683 C CG2   . THR A 1 470 ? -11.260 89.675  45.660 1.00 22.66 ? 470  THR A CG2   1 
ATOM   3684 N N     . HIS A 1 471 ? -13.652 91.836  46.717 1.00 21.53 ? 471  HIS A N     1 
ATOM   3685 C CA    . HIS A 1 471 ? -14.959 91.497  47.313 1.00 22.12 ? 471  HIS A CA    1 
ATOM   3686 C C     . HIS A 1 471 ? -15.103 89.978  47.394 1.00 19.62 ? 471  HIS A C     1 
ATOM   3687 O O     . HIS A 1 471 ? -14.648 89.270  46.502 1.00 20.51 ? 471  HIS A O     1 
ATOM   3688 C CB    . HIS A 1 471 ? -16.044 92.124  46.443 1.00 22.06 ? 471  HIS A CB    1 
ATOM   3689 C CG    . HIS A 1 471 ? -17.437 92.048  46.974 1.00 22.43 ? 471  HIS A CG    1 
ATOM   3690 N ND1   . HIS A 1 471 ? -18.200 90.913  46.877 1.00 23.10 ? 471  HIS A ND1   1 
ATOM   3691 C CD2   . HIS A 1 471 ? -18.224 93.005  47.527 1.00 21.80 ? 471  HIS A CD2   1 
ATOM   3692 C CE1   . HIS A 1 471 ? -19.406 91.166  47.370 1.00 25.43 ? 471  HIS A CE1   1 
ATOM   3693 N NE2   . HIS A 1 471 ? -19.424 92.444  47.795 1.00 20.29 ? 471  HIS A NE2   1 
ATOM   3694 N N     . ILE A 1 472 ? -15.815 89.500  48.396 1.00 20.76 ? 472  ILE A N     1 
ATOM   3695 C CA    . ILE A 1 472 ? -16.129 88.060  48.587 1.00 19.78 ? 472  ILE A CA    1 
ATOM   3696 C C     . ILE A 1 472 ? -16.624 87.400  47.292 1.00 22.14 ? 472  ILE A C     1 
ATOM   3697 O O     . ILE A 1 472 ? -16.335 86.187  47.069 1.00 21.99 ? 472  ILE A O     1 
ATOM   3698 C CB    . ILE A 1 472 ? -17.139 87.868  49.745 1.00 20.22 ? 472  ILE A CB    1 
ATOM   3699 C CG1   . ILE A 1 472 ? -18.409 88.703  49.558 1.00 21.83 ? 472  ILE A CG1   1 
ATOM   3700 C CG2   . ILE A 1 472 ? -16.451 88.134  51.084 1.00 18.10 ? 472  ILE A CG2   1 
ATOM   3701 C CD1   . ILE A 1 472 ? -19.439 88.578  50.676 1.00 23.81 ? 472  ILE A CD1   1 
ATOM   3702 N N     . ARG A 1 473 ? -17.409 88.105  46.495 1.00 22.08 ? 473  ARG A N     1 
ATOM   3703 C CA    . ARG A 1 473 ? -18.000 87.528  45.279 1.00 21.25 ? 473  ARG A CA    1 
ATOM   3704 C C     . ARG A 1 473 ? -16.905 87.139  44.285 1.00 20.63 ? 473  ARG A C     1 
ATOM   3705 O O     . ARG A 1 473 ? -17.129 86.228  43.476 1.00 22.62 ? 473  ARG A O     1 
ATOM   3706 C CB    . ARG A 1 473 ? -18.972 88.544  44.669 1.00 24.03 ? 473  ARG A CB    1 
ATOM   3707 C CG    . ARG A 1 473 ? -19.686 88.009  43.430 1.00 25.81 ? 473  ARG A CG    1 
ATOM   3708 C CD    . ARG A 1 473 ? -20.952 88.818  43.150 1.00 28.57 ? 473  ARG A CD    1 
ATOM   3709 N NE    . ARG A 1 473 ? -21.563 88.365  41.905 1.00 32.99 ? 473  ARG A NE    1 
ATOM   3710 C CZ    . ARG A 1 473 ? -22.351 87.286  41.747 1.00 32.46 ? 473  ARG A CZ    1 
ATOM   3711 N NH1   . ARG A 1 473 ? -22.649 86.484  42.755 1.00 33.67 ? 473  ARG A NH1   1 
ATOM   3712 N NH2   . ARG A 1 473 ? -22.876 87.037  40.557 1.00 37.23 ? 473  ARG A NH2   1 
ATOM   3713 N N     . TYR A 1 474 ? -15.797 87.876  44.263 1.00 20.29 ? 474  TYR A N     1 
ATOM   3714 C CA    . TYR A 1 474 ? -14.724 87.713  43.254 1.00 23.20 ? 474  TYR A CA    1 
ATOM   3715 C C     . TYR A 1 474 ? -13.478 87.031  43.827 1.00 23.70 ? 474  TYR A C     1 
ATOM   3716 O O     . TYR A 1 474 ? -12.477 86.954  43.074 1.00 23.06 ? 474  TYR A O     1 
ATOM   3717 C CB    . TYR A 1 474 ? -14.398 89.050  42.592 1.00 22.94 ? 474  TYR A CB    1 
ATOM   3718 C CG    . TYR A 1 474 ? -15.655 89.691  42.056 1.00 22.24 ? 474  TYR A CG    1 
ATOM   3719 C CD1   . TYR A 1 474 ? -16.330 89.169  40.970 1.00 25.01 ? 474  TYR A CD1   1 
ATOM   3720 C CD2   . TYR A 1 474 ? -16.218 90.752  42.718 1.00 24.11 ? 474  TYR A CD2   1 
ATOM   3721 C CE1   . TYR A 1 474 ? -17.520 89.740  40.529 1.00 26.03 ? 474  TYR A CE1   1 
ATOM   3722 C CE2   . TYR A 1 474 ? -17.363 91.369  42.267 1.00 24.32 ? 474  TYR A CE2   1 
ATOM   3723 C CZ    . TYR A 1 474 ? -18.042 90.833  41.192 1.00 28.36 ? 474  TYR A CZ    1 
ATOM   3724 O OH    . TYR A 1 474 ? -19.206 91.436  40.813 1.00 29.13 ? 474  TYR A OH    1 
ATOM   3725 N N     . MET A 1 475 ? -13.520 86.481  45.030 1.00 22.25 ? 475  MET A N     1 
ATOM   3726 C CA    . MET A 1 475 ? -12.250 85.956  45.591 1.00 19.58 ? 475  MET A CA    1 
ATOM   3727 C C     . MET A 1 475 ? -11.731 84.770  44.776 1.00 20.88 ? 475  MET A C     1 
ATOM   3728 O O     . MET A 1 475 ? -10.487 84.680  44.655 1.00 20.35 ? 475  MET A O     1 
ATOM   3729 C CB    . MET A 1 475 ? -12.342 85.649  47.079 1.00 19.23 ? 475  MET A CB    1 
ATOM   3730 C CG    . MET A 1 475 ? -12.423 86.910  47.895 1.00 20.02 ? 475  MET A CG    1 
ATOM   3731 S SD    . MET A 1 475 ? -12.749 86.566  49.637 1.00 19.65 ? 475  MET A SD    1 
ATOM   3732 C CE    . MET A 1 475 ? -12.630 88.223  50.289 1.00 22.47 ? 475  MET A CE    1 
ATOM   3733 N N     . ASP A 1 476 ? -12.588 83.859  44.305 1.00 20.36 ? 476  ASP A N     1 
ATOM   3734 C CA    . ASP A 1 476 ? -12.142 82.743  43.449 1.00 23.04 ? 476  ASP A CA    1 
ATOM   3735 C C     . ASP A 1 476 ? -11.581 83.308  42.150 1.00 22.19 ? 476  ASP A C     1 
ATOM   3736 O O     . ASP A 1 476 ? -10.559 82.828  41.691 1.00 21.65 ? 476  ASP A O     1 
ATOM   3737 C CB    . ASP A 1 476 ? -13.256 81.764  43.098 1.00 26.65 ? 476  ASP A CB    1 
ATOM   3738 C CG    . ASP A 1 476 ? -13.502 80.727  44.158 1.00 30.71 ? 476  ASP A CG    1 
ATOM   3739 O OD1   . ASP A 1 476 ? -12.766 80.706  45.175 1.00 25.94 ? 476  ASP A OD1   1 
ATOM   3740 O OD2   . ASP A 1 476 ? -14.446 79.953  43.969 1.00 38.32 ? 476  ASP A OD2   1 
ATOM   3741 N N     . ARG A 1 477 ? -12.271 84.263  41.556 1.00 22.91 ? 477  ARG A N     1 
ATOM   3742 C CA    . ARG A 1 477 ? -11.889 84.768  40.216 1.00 27.48 ? 477  ARG A CA    1 
ATOM   3743 C C     . ARG A 1 477 ? -10.496 85.409  40.323 1.00 24.84 ? 477  ARG A C     1 
ATOM   3744 O O     . ARG A 1 477 ? -9.624  85.175  39.441 1.00 22.81 ? 477  ARG A O     1 
ATOM   3745 C CB    . ARG A 1 477 ? -12.941 85.735  39.657 1.00 30.35 ? 477  ARG A CB    1 
ATOM   3746 C CG    . ARG A 1 477 ? -12.849 85.860  38.140 1.00 44.59 ? 477  ARG A CG    1 
ATOM   3747 C CD    . ARG A 1 477 ? -13.484 87.124  37.598 1.00 59.31 ? 477  ARG A CD    1 
ATOM   3748 N NE    . ARG A 1 477 ? -13.710 87.106  36.151 1.00 59.29 ? 477  ARG A NE    1 
ATOM   3749 C CZ    . ARG A 1 477 ? -14.664 86.408  35.560 1.00 69.05 ? 477  ARG A CZ    1 
ATOM   3750 N NH1   . ARG A 1 477 ? -15.473 85.648  36.279 1.00 78.52 ? 477  ARG A NH1   1 
ATOM   3751 N NH2   . ARG A 1 477 ? -14.811 86.454  34.249 1.00 76.90 ? 477  ARG A NH2   1 
ATOM   3752 N N     . ILE A 1 478 ? -10.260 86.193  41.366 1.00 22.28 ? 478  ILE A N     1 
ATOM   3753 C CA    . ILE A 1 478 ? -8.928  86.849  41.541 1.00 22.66 ? 478  ILE A CA    1 
ATOM   3754 C C     . ILE A 1 478 ? -7.829  85.804  41.820 1.00 19.98 ? 478  ILE A C     1 
ATOM   3755 O O     . ILE A 1 478 ? -6.764  85.901  41.195 1.00 20.28 ? 478  ILE A O     1 
ATOM   3756 C CB    . ILE A 1 478 ? -9.011  87.946  42.610 1.00 21.77 ? 478  ILE A CB    1 
ATOM   3757 C CG1   . ILE A 1 478 ? -10.047 89.017  42.230 1.00 26.41 ? 478  ILE A CG1   1 
ATOM   3758 C CG2   . ILE A 1 478 ? -7.633  88.519  42.868 1.00 21.76 ? 478  ILE A CG2   1 
ATOM   3759 C CD1   . ILE A 1 478 ? -9.895  89.596  40.886 1.00 29.17 ? 478  ILE A CD1   1 
ATOM   3760 N N     . ALA A 1 479 ? -8.076  84.797  42.672 1.00 19.46 ? 479  ALA A N     1 
ATOM   3761 C CA    . ALA A 1 479 ? -7.120  83.693  42.918 1.00 18.76 ? 479  ALA A CA    1 
ATOM   3762 C C     . ALA A 1 479 ? -6.718  83.063  41.577 1.00 23.58 ? 479  ALA A C     1 
ATOM   3763 O O     . ALA A 1 479 ? -5.501  82.773  41.385 1.00 20.49 ? 479  ALA A O     1 
ATOM   3764 C CB    . ALA A 1 479 ? -7.684  82.657  43.873 1.00 20.17 ? 479  ALA A CB    1 
ATOM   3765 N N     . LYS A 1 480 ? -7.691  82.851  40.677 1.00 23.20 ? 480  LYS A N     1 
ATOM   3766 C CA    . LYS A 1 480 ? -7.459  82.174  39.372 1.00 22.13 ? 480  LYS A CA    1 
ATOM   3767 C C     . LYS A 1 480 ? -6.645  83.035  38.409 1.00 21.64 ? 480  LYS A C     1 
ATOM   3768 O O     . LYS A 1 480 ? -6.035  82.436  37.485 1.00 23.17 ? 480  LYS A O     1 
ATOM   3769 C CB    . LYS A 1 480 ? -8.788  81.733  38.744 1.00 24.75 ? 480  LYS A CB    1 
ATOM   3770 C CG    . LYS A 1 480 ? -9.452  80.570  39.470 1.00 28.10 ? 480  LYS A CG    1 
ATOM   3771 C CD    . LYS A 1 480 ? -10.821 80.207  38.872 1.00 33.74 ? 480  LYS A CD    1 
ATOM   3772 C CE    . LYS A 1 480 ? -11.625 79.257  39.749 1.00 44.10 ? 480  LYS A CE    1 
ATOM   3773 N NZ    . LYS A 1 480 ? -10.916 77.974  40.014 1.00 41.61 ? 480  LYS A NZ    1 
ATOM   3774 N N     . THR A 1 481 ? -6.487  84.320  38.663 1.00 21.13 ? 481  THR A N     1 
ATOM   3775 C CA    . THR A 1 481 ? -5.592  85.206  37.873 1.00 19.96 ? 481  THR A CA    1 
ATOM   3776 C C     . THR A 1 481 ? -4.125  85.019  38.273 1.00 20.77 ? 481  THR A C     1 
ATOM   3777 O O     . THR A 1 481 ? -3.253  85.295  37.426 1.00 20.05 ? 481  THR A O     1 
ATOM   3778 C CB    . THR A 1 481 ? -5.959  86.686  37.951 1.00 22.67 ? 481  THR A CB    1 
ATOM   3779 O OG1   . THR A 1 481 ? -5.690  87.269  39.237 1.00 20.66 ? 481  THR A OG1   1 
ATOM   3780 C CG2   . THR A 1 481 ? -7.382  86.946  37.514 1.00 21.66 ? 481  THR A CG2   1 
ATOM   3781 N N     . TYR A 1 482 ? -3.840  84.534  39.489 1.00 20.13 ? 482  TYR A N     1 
ATOM   3782 C CA    . TYR A 1 482 ? -2.462  84.333  40.013 1.00 19.23 ? 482  TYR A CA    1 
ATOM   3783 C C     . TYR A 1 482 ? -2.002  82.906  39.701 1.00 19.05 ? 482  TYR A C     1 
ATOM   3784 O O     . TYR A 1 482 ? -1.528  82.181  40.564 1.00 20.67 ? 482  TYR A O     1 
ATOM   3785 C CB    . TYR A 1 482 ? -2.417  84.761  41.481 1.00 18.91 ? 482  TYR A CB    1 
ATOM   3786 C CG    . TYR A 1 482 ? -2.485  86.252  41.717 1.00 18.74 ? 482  TYR A CG    1 
ATOM   3787 C CD1   . TYR A 1 482 ? -1.344  87.048  41.642 1.00 20.37 ? 482  TYR A CD1   1 
ATOM   3788 C CD2   . TYR A 1 482 ? -3.671  86.883  42.041 1.00 19.78 ? 482  TYR A CD2   1 
ATOM   3789 C CE1   . TYR A 1 482 ? -1.379  88.415  41.886 1.00 19.94 ? 482  TYR A CE1   1 
ATOM   3790 C CE2   . TYR A 1 482 ? -3.735  88.265  42.226 1.00 19.18 ? 482  TYR A CE2   1 
ATOM   3791 C CZ    . TYR A 1 482 ? -2.595  89.034  42.149 1.00 19.26 ? 482  TYR A CZ    1 
ATOM   3792 O OH    . TYR A 1 482 ? -2.666  90.385  42.397 1.00 18.89 ? 482  TYR A OH    1 
ATOM   3793 N N     . SER A 1 483 ? -2.086  82.557  38.411 1.00 19.82 ? 483  SER A N     1 
ATOM   3794 C CA    . SER A 1 483 ? -2.084  81.173  37.865 1.00 22.14 ? 483  SER A CA    1 
ATOM   3795 C C     . SER A 1 483 ? -0.695  80.735  37.385 1.00 20.69 ? 483  SER A C     1 
ATOM   3796 O O     . SER A 1 483 ? -0.607  79.670  36.768 1.00 20.97 ? 483  SER A O     1 
ATOM   3797 C CB    . SER A 1 483 ? -3.039  81.072  36.721 1.00 22.29 ? 483  SER A CB    1 
ATOM   3798 O OG    . SER A 1 483 ? -2.546  81.935  35.700 1.00 22.57 ? 483  SER A OG    1 
ATOM   3799 N N     . TRP A 1 484 ? 0.367   81.476  37.660 1.00 20.14 ? 484  TRP A N     1 
ATOM   3800 C CA    . TRP A 1 484 ? 1.698   81.085  37.158 1.00 19.93 ? 484  TRP A CA    1 
ATOM   3801 C C     . TRP A 1 484 ? 1.978   79.606  37.475 1.00 20.61 ? 484  TRP A C     1 
ATOM   3802 O O     . TRP A 1 484 ? 1.738   79.134  38.629 1.00 16.88 ? 484  TRP A O     1 
ATOM   3803 C CB    . TRP A 1 484 ? 2.806   82.000  37.686 1.00 20.26 ? 484  TRP A CB    1 
ATOM   3804 C CG    . TRP A 1 484 ? 4.127   81.653  37.069 1.00 19.23 ? 484  TRP A CG    1 
ATOM   3805 C CD1   . TRP A 1 484 ? 4.530   81.947  35.792 1.00 20.47 ? 484  TRP A CD1   1 
ATOM   3806 C CD2   . TRP A 1 484 ? 5.175   80.863  37.650 1.00 19.05 ? 484  TRP A CD2   1 
ATOM   3807 N NE1   . TRP A 1 484 ? 5.782   81.434  35.564 1.00 21.50 ? 484  TRP A NE1   1 
ATOM   3808 C CE2   . TRP A 1 484 ? 6.182   80.715  36.667 1.00 21.16 ? 484  TRP A CE2   1 
ATOM   3809 C CE3   . TRP A 1 484 ? 5.358   80.246  38.894 1.00 19.38 ? 484  TRP A CE3   1 
ATOM   3810 C CZ2   . TRP A 1 484 ? 7.370   80.016  36.898 1.00 19.56 ? 484  TRP A CZ2   1 
ATOM   3811 C CZ3   . TRP A 1 484 ? 6.516   79.534  39.120 1.00 19.80 ? 484  TRP A CZ3   1 
ATOM   3812 C CH2   . TRP A 1 484 ? 7.513   79.422  38.129 1.00 20.97 ? 484  TRP A CH2   1 
ATOM   3813 N N     . ASN A 1 485 ? 2.581   78.892  36.520 1.00 19.53 ? 485  ASN A N     1 
ATOM   3814 C CA    . ASN A 1 485 ? 2.975   77.467  36.693 1.00 20.07 ? 485  ASN A CA    1 
ATOM   3815 C C     . ASN A 1 485 ? 1.757   76.605  37.066 1.00 19.45 ? 485  ASN A C     1 
ATOM   3816 O O     . ASN A 1 485 ? 1.811   75.849  38.065 1.00 18.34 ? 485  ASN A O     1 
ATOM   3817 C CB    . ASN A 1 485 ? 4.147   77.305  37.660 1.00 20.73 ? 485  ASN A CB    1 
ATOM   3818 C CG    . ASN A 1 485 ? 4.690   75.891  37.634 1.00 23.52 ? 485  ASN A CG    1 
ATOM   3819 O OD1   . ASN A 1 485 ? 4.549   75.209  36.626 1.00 20.17 ? 485  ASN A OD1   1 
ATOM   3820 N ND2   . ASN A 1 485 ? 5.267   75.436  38.732 1.00 20.61 ? 485  ASN A ND2   1 
ATOM   3821 N N     . ASP A 1 486 ? 0.681   76.697  36.285 1.00 20.20 ? 486  ASP A N     1 
ATOM   3822 C CA    . ASP A 1 486 ? -0.568  75.905  36.519 1.00 22.53 ? 486  ASP A CA    1 
ATOM   3823 C C     . ASP A 1 486 ? -1.071  76.082  37.969 1.00 21.71 ? 486  ASP A C     1 
ATOM   3824 O O     . ASP A 1 486 ? -1.321  75.036  38.647 1.00 20.54 ? 486  ASP A O     1 
ATOM   3825 C CB    . ASP A 1 486 ? -0.351  74.411  36.246 1.00 27.03 ? 486  ASP A CB    1 
ATOM   3826 C CG    . ASP A 1 486 ? -1.659  73.613  36.180 1.00 35.90 ? 486  ASP A CG    1 
ATOM   3827 O OD1   . ASP A 1 486 ? -2.725  74.220  35.856 1.00 44.91 ? 486  ASP A OD1   1 
ATOM   3828 O OD2   . ASP A 1 486 ? -1.662  72.439  36.582 1.00 43.86 ? 486  ASP A OD2   1 
ATOM   3829 N N     . ASN A 1 487 ? -1.184  77.329  38.457 1.00 20.89 ? 487  ASN A N     1 
ATOM   3830 C CA    . ASN A 1 487 ? -1.773  77.610  39.791 1.00 20.95 ? 487  ASN A CA    1 
ATOM   3831 C C     . ASN A 1 487 ? -0.901  76.993  40.892 1.00 19.58 ? 487  ASN A C     1 
ATOM   3832 O O     . ASN A 1 487 ? -1.452  76.538  41.930 1.00 20.66 ? 487  ASN A O     1 
ATOM   3833 C CB    . ASN A 1 487 ? -3.204  77.080  39.874 1.00 22.27 ? 487  ASN A CB    1 
ATOM   3834 C CG    . ASN A 1 487 ? -4.036  77.614  38.737 1.00 24.53 ? 487  ASN A CG    1 
ATOM   3835 O OD1   . ASN A 1 487 ? -4.271  76.899  37.764 1.00 29.09 ? 487  ASN A OD1   1 
ATOM   3836 N ND2   . ASN A 1 487 ? -4.367  78.883  38.799 1.00 22.44 ? 487  ASN A ND2   1 
ATOM   3837 N N     . ALA A 1 488 ? 0.420   77.077  40.742 1.00 19.05 ? 488  ALA A N     1 
ATOM   3838 C CA    . ALA A 1 488 ? 1.389   76.552  41.737 1.00 19.92 ? 488  ALA A CA    1 
ATOM   3839 C C     . ALA A 1 488 ? 1.190   77.190  43.122 1.00 18.11 ? 488  ALA A C     1 
ATOM   3840 O O     . ALA A 1 488 ? 1.224   76.429  44.130 1.00 18.31 ? 488  ALA A O     1 
ATOM   3841 C CB    . ALA A 1 488 ? 2.791   76.730  41.209 1.00 20.04 ? 488  ALA A CB    1 
ATOM   3842 N N     . LEU A 1 489 ? 1.000   78.498  43.190 1.00 17.85 ? 489  LEU A N     1 
ATOM   3843 C CA    . LEU A 1 489 ? 0.919   79.170  44.515 1.00 18.80 ? 489  LEU A CA    1 
ATOM   3844 C C     . LEU A 1 489 ? -0.341  78.699  45.250 1.00 18.43 ? 489  LEU A C     1 
ATOM   3845 O O     . LEU A 1 489 ? -0.225  78.361  46.440 1.00 18.38 ? 489  LEU A O     1 
ATOM   3846 C CB    . LEU A 1 489 ? 1.002   80.687  44.362 1.00 19.03 ? 489  LEU A CB    1 
ATOM   3847 C CG    . LEU A 1 489 ? 1.114   81.443  45.695 1.00 20.52 ? 489  LEU A CG    1 
ATOM   3848 C CD1   . LEU A 1 489 ? 2.349   80.977  46.454 1.00 23.14 ? 489  LEU A CD1   1 
ATOM   3849 C CD2   . LEU A 1 489 ? 1.169   82.919  45.471 1.00 21.07 ? 489  LEU A CD2   1 
ATOM   3850 N N     . TRP A 1 490 ? -1.487  78.588  44.583 1.00 17.94 ? 490  TRP A N     1 
ATOM   3851 C CA    . TRP A 1 490 ? -2.721  78.130  45.270 1.00 19.51 ? 490  TRP A CA    1 
ATOM   3852 C C     . TRP A 1 490 ? -2.637  76.655  45.647 1.00 20.46 ? 490  TRP A C     1 
ATOM   3853 O O     . TRP A 1 490 ? -3.227  76.286  46.668 1.00 19.61 ? 490  TRP A O     1 
ATOM   3854 C CB    . TRP A 1 490 ? -4.014  78.531  44.522 1.00 19.79 ? 490  TRP A CB    1 
ATOM   3855 C CG    . TRP A 1 490 ? -4.581  79.754  45.171 1.00 19.64 ? 490  TRP A CG    1 
ATOM   3856 C CD1   . TRP A 1 490 ? -5.721  79.818  45.919 1.00 19.69 ? 490  TRP A CD1   1 
ATOM   3857 C CD2   . TRP A 1 490 ? -4.027  81.087  45.183 1.00 19.98 ? 490  TRP A CD2   1 
ATOM   3858 N NE1   . TRP A 1 490 ? -5.909  81.089  46.381 1.00 19.41 ? 490  TRP A NE1   1 
ATOM   3859 C CE2   . TRP A 1 490 ? -4.878  81.882  45.975 1.00 18.81 ? 490  TRP A CE2   1 
ATOM   3860 C CE3   . TRP A 1 490 ? -2.896  81.691  44.622 1.00 19.73 ? 490  TRP A CE3   1 
ATOM   3861 C CZ2   . TRP A 1 490 ? -4.637  83.224  46.211 1.00 20.95 ? 490  TRP A CZ2   1 
ATOM   3862 C CZ3   . TRP A 1 490 ? -2.648  83.003  44.899 1.00 22.38 ? 490  TRP A CZ3   1 
ATOM   3863 C CH2   . TRP A 1 490 ? -3.505  83.772  45.666 1.00 19.77 ? 490  TRP A CH2   1 
ATOM   3864 N N     . LYS A 1 491 ? -1.900  75.837  44.906 1.00 20.36 ? 491  LYS A N     1 
ATOM   3865 C CA    . LYS A 1 491 ? -1.689  74.450  45.318 1.00 20.85 ? 491  LYS A CA    1 
ATOM   3866 C C     . LYS A 1 491 ? -0.919  74.435  46.635 1.00 20.58 ? 491  LYS A C     1 
ATOM   3867 O O     . LYS A 1 491 ? -1.282  73.662  47.522 1.00 18.62 ? 491  LYS A O     1 
ATOM   3868 C CB    . LYS A 1 491 ? -0.995  73.673  44.211 1.00 21.96 ? 491  LYS A CB    1 
ATOM   3869 C CG    . LYS A 1 491 ? -1.890  73.406  43.007 1.00 24.25 ? 491  LYS A CG    1 
ATOM   3870 C CD    . LYS A 1 491 ? -1.112  72.708  41.889 1.00 25.64 ? 491  LYS A CD    1 
ATOM   3871 C CE    . LYS A 1 491 ? -1.954  72.644  40.618 1.00 28.59 ? 491  LYS A CE    1 
ATOM   3872 N NZ    . LYS A 1 491 ? -1.122  72.183  39.484 1.00 29.45 ? 491  LYS A NZ    1 
ATOM   3873 N N     . MET A 1 492 ? 0.064   75.300  46.784 1.00 18.74 ? 492  MET A N     1 
ATOM   3874 C CA    . MET A 1 492 ? 0.779   75.418  48.073 1.00 18.50 ? 492  MET A CA    1 
ATOM   3875 C C     . MET A 1 492 ? -0.188  75.940  49.162 1.00 18.45 ? 492  MET A C     1 
ATOM   3876 O O     . MET A 1 492 ? -0.222  75.344  50.260 1.00 17.26 ? 492  MET A O     1 
ATOM   3877 C CB    . MET A 1 492 ? 1.977   76.357  47.942 1.00 19.04 ? 492  MET A CB    1 
ATOM   3878 C CG    . MET A 1 492 ? 2.857   76.372  49.169 1.00 20.97 ? 492  MET A CG    1 
ATOM   3879 S SD    . MET A 1 492 ? 3.894   77.835  49.224 1.00 26.36 ? 492  MET A SD    1 
ATOM   3880 C CE    . MET A 1 492 ? 2.692   79.076  49.619 1.00 26.51 ? 492  MET A CE    1 
ATOM   3881 N N     . HIS A 1 493 ? -0.956  76.993  48.907 1.00 16.45 ? 493  HIS A N     1 
ATOM   3882 C CA    . HIS A 1 493 ? -1.926  77.477  49.928 1.00 18.75 ? 493  HIS A CA    1 
ATOM   3883 C C     . HIS A 1 493 ? -2.863  76.340  50.361 1.00 18.38 ? 493  HIS A C     1 
ATOM   3884 O O     . HIS A 1 493 ? -3.117  76.191  51.574 1.00 19.70 ? 493  HIS A O     1 
ATOM   3885 C CB    . HIS A 1 493 ? -2.735  78.679  49.439 1.00 18.09 ? 493  HIS A CB    1 
ATOM   3886 C CG    . HIS A 1 493 ? -1.942  79.914  49.212 1.00 16.96 ? 493  HIS A CG    1 
ATOM   3887 N ND1   . HIS A 1 493 ? -0.955  80.306  50.074 1.00 17.34 ? 493  HIS A ND1   1 
ATOM   3888 C CD2   . HIS A 1 493 ? -2.119  80.935  48.346 1.00 19.09 ? 493  HIS A CD2   1 
ATOM   3889 C CE1   . HIS A 1 493 ? -0.452  81.446  49.650 1.00 19.61 ? 493  HIS A CE1   1 
ATOM   3890 N NE2   . HIS A 1 493 ? -1.151  81.879  48.591 1.00 17.32 ? 493  HIS A NE2   1 
ATOM   3891 N N     . GLU A 1 494 ? -3.357  75.541  49.416 1.00 18.63 ? 494  GLU A N     1 
ATOM   3892 C CA    . GLU A 1 494 ? -4.274  74.426  49.738 1.00 19.90 ? 494  GLU A CA    1 
ATOM   3893 C C     . GLU A 1 494 ? -3.539  73.370  50.575 1.00 18.08 ? 494  GLU A C     1 
ATOM   3894 O O     . GLU A 1 494 ? -4.203  72.732  51.430 1.00 20.27 ? 494  GLU A O     1 
ATOM   3895 C CB    . GLU A 1 494 ? -4.897  73.861  48.448 1.00 19.43 ? 494  GLU A CB    1 
ATOM   3896 C CG    . GLU A 1 494 ? -5.923  74.809  47.843 1.00 22.69 ? 494  GLU A CG    1 
ATOM   3897 C CD    . GLU A 1 494 ? -7.292  74.892  48.547 1.00 26.68 ? 494  GLU A CD    1 
ATOM   3898 O OE1   . GLU A 1 494 ? -7.595  74.068  49.504 1.00 31.06 ? 494  GLU A OE1   1 
ATOM   3899 O OE2   . GLU A 1 494 ? -8.105  75.785  48.129 1.00 26.64 ? 494  GLU A OE2   1 
ATOM   3900 N N     . THR A 1 495 ? -2.253  73.128  50.334 1.00 19.97 ? 495  THR A N     1 
ATOM   3901 C CA    . THR A 1 495 ? -1.440  72.193  51.157 1.00 20.23 ? 495  THR A CA    1 
ATOM   3902 C C     . THR A 1 495 ? -1.393  72.671  52.611 1.00 19.47 ? 495  THR A C     1 
ATOM   3903 O O     . THR A 1 495 ? -1.614  71.863  53.538 1.00 20.89 ? 495  THR A O     1 
ATOM   3904 C CB    . THR A 1 495 ? -0.033  72.030  50.591 1.00 23.36 ? 495  THR A CB    1 
ATOM   3905 O OG1   . THR A 1 495 ? -0.244  71.513  49.295 1.00 23.92 ? 495  THR A OG1   1 
ATOM   3906 C CG2   . THR A 1 495 ? 0.842   71.091  51.375 1.00 25.64 ? 495  THR A CG2   1 
ATOM   3907 N N     . ILE A 1 496 ? -1.102  73.945  52.818 1.00 20.66 ? 496  ILE A N     1 
ATOM   3908 C CA    . ILE A 1 496 ? -1.006  74.543  54.189 1.00 19.93 ? 496  ILE A CA    1 
ATOM   3909 C C     . ILE A 1 496 ? -2.409  74.568  54.791 1.00 18.68 ? 496  ILE A C     1 
ATOM   3910 O O     . ILE A 1 496 ? -2.564  74.201  55.973 1.00 19.98 ? 496  ILE A O     1 
ATOM   3911 C CB    . ILE A 1 496 ? -0.366  75.940  54.114 1.00 20.59 ? 496  ILE A CB    1 
ATOM   3912 C CG1   . ILE A 1 496 ? 1.057   75.863  53.551 1.00 21.27 ? 496  ILE A CG1   1 
ATOM   3913 C CG2   . ILE A 1 496 ? -0.433  76.627  55.479 1.00 21.75 ? 496  ILE A CG2   1 
ATOM   3914 C CD1   . ILE A 1 496 ? 1.626   77.211  53.162 1.00 22.53 ? 496  ILE A CD1   1 
ATOM   3915 N N     . LYS A 1 497 ? -3.403  74.934  53.999 1.00 18.28 ? 497  LYS A N     1 
ATOM   3916 C CA    . LYS A 1 497 ? -4.801  74.939  54.493 1.00 19.24 ? 497  LYS A CA    1 
ATOM   3917 C C     . LYS A 1 497 ? -5.199  73.543  55.024 1.00 21.90 ? 497  LYS A C     1 
ATOM   3918 O O     . LYS A 1 497 ? -5.775  73.436  56.141 1.00 21.63 ? 497  LYS A O     1 
ATOM   3919 C CB    . LYS A 1 497 ? -5.765  75.323  53.370 1.00 19.38 ? 497  LYS A CB    1 
ATOM   3920 C CG    . LYS A 1 497 ? -7.236  75.281  53.752 1.00 20.43 ? 497  LYS A CG    1 
ATOM   3921 C CD    . LYS A 1 497 ? -7.583  76.292  54.772 1.00 19.82 ? 497  LYS A CD    1 
ATOM   3922 C CE    . LYS A 1 497 ? -9.081  76.539  54.829 1.00 21.78 ? 497  LYS A CE    1 
ATOM   3923 N NZ    . LYS A 1 497 ? -9.434  77.276  56.063 1.00 20.30 ? 497  LYS A NZ    1 
ATOM   3924 N N     . ASP A 1 498 ? -4.919  72.491  54.280 1.00 20.41 ? 498  ASP A N     1 
ATOM   3925 C CA    . ASP A 1 498 ? -5.302  71.122  54.701 1.00 21.95 ? 498  ASP A CA    1 
ATOM   3926 C C     . ASP A 1 498 ? -4.513  70.666  55.928 1.00 22.52 ? 498  ASP A C     1 
ATOM   3927 O O     . ASP A 1 498 ? -5.086  69.853  56.699 1.00 24.11 ? 498  ASP A O     1 
ATOM   3928 C CB    . ASP A 1 498 ? -5.142  70.111  53.581 1.00 22.52 ? 498  ASP A CB    1 
ATOM   3929 C CG    . ASP A 1 498 ? -6.132  70.317  52.469 1.00 24.29 ? 498  ASP A CG    1 
ATOM   3930 O OD1   . ASP A 1 498 ? -7.214  70.956  52.689 1.00 23.81 ? 498  ASP A OD1   1 
ATOM   3931 O OD2   . ASP A 1 498 ? -5.818  69.825  51.394 1.00 24.71 ? 498  ASP A OD2   1 
ATOM   3932 N N     . ALA A 1 499 ? -3.314  71.186  56.143 1.00 20.26 ? 499  ALA A N     1 
ATOM   3933 C CA    . ALA A 1 499 ? -2.458  70.802  57.289 1.00 22.90 ? 499  ALA A CA    1 
ATOM   3934 C C     . ALA A 1 499 ? -2.967  71.511  58.552 1.00 23.29 ? 499  ALA A C     1 
ATOM   3935 O O     . ALA A 1 499 ? -3.118  70.854  59.596 1.00 21.38 ? 499  ALA A O     1 
ATOM   3936 C CB    . ALA A 1 499 ? -1.038  71.204  57.002 1.00 25.29 ? 499  ALA A CB    1 
ATOM   3937 N N     . LEU A 1 500 ? -3.258  72.810  58.451 1.00 19.86 ? 500  LEU A N     1 
ATOM   3938 C CA    . LEU A 1 500 ? -3.698  73.624  59.608 1.00 20.99 ? 500  LEU A CA    1 
ATOM   3939 C C     . LEU A 1 500 ? -5.177  73.394  59.912 1.00 22.08 ? 500  LEU A C     1 
ATOM   3940 O O     . LEU A 1 500 ? -5.547  73.480  61.113 1.00 20.80 ? 500  LEU A O     1 
ATOM   3941 C CB    . LEU A 1 500 ? -3.404  75.098  59.350 1.00 20.82 ? 500  LEU A CB    1 
ATOM   3942 C CG    . LEU A 1 500 ? -1.931  75.517  59.367 1.00 20.60 ? 500  LEU A CG    1 
ATOM   3943 C CD1   . LEU A 1 500 ? -1.786  76.975  59.029 1.00 20.46 ? 500  LEU A CD1   1 
ATOM   3944 C CD2   . LEU A 1 500 ? -1.272  75.234  60.688 1.00 23.61 ? 500  LEU A CD2   1 
ATOM   3945 N N     . ASP A 1 501 ? -5.996  73.155  58.874 1.00 21.15 ? 501  ASP A N     1 
ATOM   3946 C CA    . ASP A 1 501 ? -7.473  73.147  58.984 1.00 23.06 ? 501  ASP A CA    1 
ATOM   3947 C C     . ASP A 1 501 ? -8.028  71.947  58.213 1.00 21.19 ? 501  ASP A C     1 
ATOM   3948 O O     . ASP A 1 501 ? -8.703  72.123  57.192 1.00 20.85 ? 501  ASP A O     1 
ATOM   3949 C CB    . ASP A 1 501 ? -8.052  74.452  58.428 1.00 23.05 ? 501  ASP A CB    1 
ATOM   3950 C CG    . ASP A 1 501 ? -9.535  74.680  58.708 1.00 21.19 ? 501  ASP A CG    1 
ATOM   3951 O OD1   . ASP A 1 501 ? -10.155 73.875  59.503 1.00 22.04 ? 501  ASP A OD1   1 
ATOM   3952 O OD2   . ASP A 1 501 ? -10.111 75.623  58.120 1.00 21.70 ? 501  ASP A OD2   1 
ATOM   3953 N N     . PRO A 1 502 ? -7.693  70.710  58.623 1.00 22.81 ? 502  PRO A N     1 
ATOM   3954 C CA    . PRO A 1 502 ? -8.149  69.515  57.904 1.00 22.75 ? 502  PRO A CA    1 
ATOM   3955 C C     . PRO A 1 502 ? -9.666  69.481  57.754 1.00 23.05 ? 502  PRO A C     1 
ATOM   3956 O O     . PRO A 1 502 ? -10.090 69.032  56.732 1.00 23.53 ? 502  PRO A O     1 
ATOM   3957 C CB    . PRO A 1 502 ? -7.602  68.328  58.715 1.00 25.27 ? 502  PRO A CB    1 
ATOM   3958 C CG    . PRO A 1 502 ? -7.236  68.909  60.060 1.00 25.20 ? 502  PRO A CG    1 
ATOM   3959 C CD    . PRO A 1 502 ? -6.881  70.363  59.812 1.00 22.89 ? 502  PRO A CD    1 
ATOM   3960 N N     . ASN A 1 503 ? -10.437 70.032  58.704 1.00 21.55 ? 503  ASN A N     1 
ATOM   3961 C CA    . ASN A 1 503 ? -11.914 69.993  58.607 1.00 23.92 ? 503  ASN A CA    1 
ATOM   3962 C C     . ASN A 1 503 ? -12.416 71.164  57.764 1.00 24.83 ? 503  ASN A C     1 
ATOM   3963 O O     . ASN A 1 503 ? -13.624 71.212  57.563 1.00 24.44 ? 503  ASN A O     1 
ATOM   3964 C CB    . ASN A 1 503 ? -12.546 69.902  59.999 1.00 24.53 ? 503  ASN A CB    1 
ATOM   3965 C CG    . ASN A 1 503 ? -12.149 68.602  60.664 1.00 25.42 ? 503  ASN A CG    1 
ATOM   3966 O OD1   . ASN A 1 503 ? -12.118 67.560  60.025 1.00 26.97 ? 503  ASN A OD1   1 
ATOM   3967 N ND2   . ASN A 1 503 ? -11.685 68.666  61.880 1.00 24.32 ? 503  ASN A ND2   1 
ATOM   3968 N N     . GLY A 1 504 ? -11.559 72.106  57.333 1.00 21.45 ? 504  GLY A N     1 
ATOM   3969 C CA    . GLY A 1 504 ? -12.017 73.217  56.474 1.00 21.91 ? 504  GLY A CA    1 
ATOM   3970 C C     . GLY A 1 504 ? -13.030 74.090  57.182 1.00 22.25 ? 504  GLY A C     1 
ATOM   3971 O O     . GLY A 1 504 ? -13.904 74.663  56.499 1.00 21.66 ? 504  GLY A O     1 
ATOM   3972 N N     . ILE A 1 505 ? -12.902 74.297  58.500 1.00 19.41 ? 505  ILE A N     1 
ATOM   3973 C CA    . ILE A 1 505 ? -13.934 75.099  59.212 1.00 21.14 ? 505  ILE A CA    1 
ATOM   3974 C C     . ILE A 1 505 ? -13.579 76.583  59.315 1.00 22.86 ? 505  ILE A C     1 
ATOM   3975 O O     . ILE A 1 505 ? -14.476 77.332  59.777 1.00 24.56 ? 505  ILE A O     1 
ATOM   3976 C CB    . ILE A 1 505 ? -14.333 74.466  60.561 1.00 24.78 ? 505  ILE A CB    1 
ATOM   3977 C CG1   . ILE A 1 505 ? -13.137 74.065  61.406 1.00 25.67 ? 505  ILE A CG1   1 
ATOM   3978 C CG2   . ILE A 1 505 ? -15.253 73.267  60.332 1.00 25.95 ? 505  ILE A CG2   1 
ATOM   3979 C CD1   . ILE A 1 505 ? -12.447 75.242  62.038 1.00 24.74 ? 505  ILE A CD1   1 
ATOM   3980 N N     . LEU A 1 506 ? -12.394 77.064  58.893 1.00 20.52 ? 506  LEU A N     1 
ATOM   3981 C CA    . LEU A 1 506 ? -12.200 78.541  58.845 1.00 20.41 ? 506  LEU A CA    1 
ATOM   3982 C C     . LEU A 1 506 ? -12.433 79.098  57.436 1.00 19.21 ? 506  LEU A C     1 
ATOM   3983 O O     . LEU A 1 506 ? -11.708 78.771  56.521 1.00 20.03 ? 506  LEU A O     1 
ATOM   3984 C CB    . LEU A 1 506 ? -10.828 78.977  59.364 1.00 21.25 ? 506  LEU A CB    1 
ATOM   3985 C CG    . LEU A 1 506 ? -10.518 78.648  60.808 1.00 21.37 ? 506  LEU A CG    1 
ATOM   3986 C CD1   . LEU A 1 506 ? -9.205  79.371  61.168 1.00 22.48 ? 506  LEU A CD1   1 
ATOM   3987 C CD2   . LEU A 1 506 ? -11.631 79.038  61.782 1.00 23.20 ? 506  LEU A CD2   1 
ATOM   3988 N N     . ALA A 1 507 ? -13.410 79.987  57.335 1.00 19.82 ? 507  ALA A N     1 
ATOM   3989 C CA    . ALA A 1 507 ? -13.668 80.925  56.223 1.00 20.50 ? 507  ALA A CA    1 
ATOM   3990 C C     . ALA A 1 507 ? -13.415 80.259  54.867 1.00 20.81 ? 507  ALA A C     1 
ATOM   3991 O O     . ALA A 1 507 ? -12.618 80.714  54.051 1.00 19.94 ? 507  ALA A O     1 
ATOM   3992 C CB    . ALA A 1 507 ? -12.868 82.171  56.412 1.00 19.89 ? 507  ALA A CB    1 
ATOM   3993 N N     . PRO A 1 508 ? -14.150 79.196  54.519 1.00 21.73 ? 508  PRO A N     1 
ATOM   3994 C CA    . PRO A 1 508 ? -13.983 78.573  53.198 1.00 22.05 ? 508  PRO A CA    1 
ATOM   3995 C C     . PRO A 1 508 ? -14.258 79.594  52.091 1.00 22.85 ? 508  PRO A C     1 
ATOM   3996 O O     . PRO A 1 508 ? -15.269 80.336  52.179 1.00 20.92 ? 508  PRO A O     1 
ATOM   3997 C CB    . PRO A 1 508 ? -14.997 77.418  53.168 1.00 24.25 ? 508  PRO A CB    1 
ATOM   3998 C CG    . PRO A 1 508 ? -15.870 77.608  54.382 1.00 25.99 ? 508  PRO A CG    1 
ATOM   3999 C CD    . PRO A 1 508 ? -15.137 78.498  55.359 1.00 24.73 ? 508  PRO A CD    1 
ATOM   4000 N N     . GLY A 1 509 ? -13.328 79.715  51.129 1.00 20.43 ? 509  GLY A N     1 
ATOM   4001 C CA    . GLY A 1 509 ? -13.461 80.684  50.027 1.00 20.76 ? 509  GLY A CA    1 
ATOM   4002 C C     . GLY A 1 509 ? -12.659 81.969  50.260 1.00 18.32 ? 509  GLY A C     1 
ATOM   4003 O O     . GLY A 1 509 ? -12.449 82.740  49.310 1.00 17.50 ? 509  GLY A O     1 
ATOM   4004 N N     . LYS A 1 510 ? -12.230 82.248  51.494 1.00 17.96 ? 510  LYS A N     1 
ATOM   4005 C CA    . LYS A 1 510 ? -11.406 83.454  51.701 1.00 18.43 ? 510  LYS A CA    1 
ATOM   4006 C C     . LYS A 1 510 ? -10.161 83.353  50.786 1.00 16.93 ? 510  LYS A C     1 
ATOM   4007 O O     . LYS A 1 510 ? -9.427  82.320  50.791 1.00 16.40 ? 510  LYS A O     1 
ATOM   4008 C CB    . LYS A 1 510 ? -11.024 83.643  53.172 1.00 19.54 ? 510  LYS A CB    1 
ATOM   4009 C CG    . LYS A 1 510 ? -10.080 84.823  53.399 1.00 19.45 ? 510  LYS A CG    1 
ATOM   4010 C CD    . LYS A 1 510 ? -10.655 86.205  53.102 1.00 19.46 ? 510  LYS A CD    1 
ATOM   4011 C CE    . LYS A 1 510 ? -9.646  87.312  53.341 1.00 19.03 ? 510  LYS A CE    1 
ATOM   4012 N NZ    . LYS A 1 510 ? -10.098 88.612  52.766 1.00 21.41 ? 510  LYS A NZ    1 
ATOM   4013 N N     . SER A 1 511 ? -9.934  84.383  49.982 1.00 17.74 ? 511  SER A N     1 
ATOM   4014 C CA    . SER A 1 511 ? -8.787  84.478  49.039 1.00 17.56 ? 511  SER A CA    1 
ATOM   4015 C C     . SER A 1 511 ? -8.789  83.297  48.072 1.00 19.33 ? 511  SER A C     1 
ATOM   4016 O O     . SER A 1 511 ? -7.707  82.937  47.532 1.00 18.05 ? 511  SER A O     1 
ATOM   4017 C CB    . SER A 1 511 ? -7.479  84.585  49.800 1.00 19.40 ? 511  SER A CB    1 
ATOM   4018 O OG    . SER A 1 511 ? -7.445  85.759  50.616 1.00 18.82 ? 511  SER A OG    1 
ATOM   4019 N N     . GLY A 1 512 ? -9.958  82.685  47.833 1.00 18.53 ? 512  GLY A N     1 
ATOM   4020 C CA    . GLY A 1 512 ? -10.038 81.551  46.895 1.00 18.75 ? 512  GLY A CA    1 
ATOM   4021 C C     . GLY A 1 512 ? -9.454  80.280  47.477 1.00 20.85 ? 512  GLY A C     1 
ATOM   4022 O O     . GLY A 1 512 ? -9.223  79.375  46.717 1.00 18.53 ? 512  GLY A O     1 
ATOM   4023 N N     . ILE A 1 513 ? -9.314  80.179  48.800 1.00 19.14 ? 513  ILE A N     1 
ATOM   4024 C CA    . ILE A 1 513 ? -8.743  78.994  49.492 1.00 19.35 ? 513  ILE A CA    1 
ATOM   4025 C C     . ILE A 1 513 ? -9.902  78.219  50.129 1.00 20.83 ? 513  ILE A C     1 
ATOM   4026 O O     . ILE A 1 513 ? -10.650 78.818  50.967 1.00 18.68 ? 513  ILE A O     1 
ATOM   4027 C CB    . ILE A 1 513 ? -7.672  79.399  50.520 1.00 17.77 ? 513  ILE A CB    1 
ATOM   4028 C CG1   . ILE A 1 513 ? -6.524  80.175  49.862 1.00 19.27 ? 513  ILE A CG1   1 
ATOM   4029 C CG2   . ILE A 1 513 ? -7.181  78.166  51.282 1.00 18.39 ? 513  ILE A CG2   1 
ATOM   4030 C CD1   . ILE A 1 513 ? -5.604  80.859  50.859 1.00 19.37 ? 513  ILE A CD1   1 
ATOM   4031 N N     . TRP A 1 514 ? -10.094 76.962  49.715 1.00 20.81 ? 514  TRP A N     1 
ATOM   4032 C CA    . TRP A 1 514 ? -11.273 76.149  50.137 1.00 22.02 ? 514  TRP A CA    1 
ATOM   4033 C C     . TRP A 1 514 ? -10.966 75.007  51.101 1.00 23.97 ? 514  TRP A C     1 
ATOM   4034 O O     . TRP A 1 514 ? -11.844 74.704  51.979 1.00 26.34 ? 514  TRP A O     1 
ATOM   4035 C CB    . TRP A 1 514 ? -11.969 75.640  48.871 1.00 22.60 ? 514  TRP A CB    1 
ATOM   4036 C CG    . TRP A 1 514 ? -12.695 76.775  48.224 1.00 22.69 ? 514  TRP A CG    1 
ATOM   4037 C CD1   . TRP A 1 514 ? -12.228 77.586  47.243 1.00 21.96 ? 514  TRP A CD1   1 
ATOM   4038 C CD2   . TRP A 1 514 ? -14.037 77.222  48.507 1.00 23.56 ? 514  TRP A CD2   1 
ATOM   4039 N NE1   . TRP A 1 514 ? -13.164 78.534  46.930 1.00 23.39 ? 514  TRP A NE1   1 
ATOM   4040 C CE2   . TRP A 1 514 ? -14.295 78.325  47.672 1.00 23.62 ? 514  TRP A CE2   1 
ATOM   4041 C CE3   . TRP A 1 514 ? -15.033 76.806  49.392 1.00 24.51 ? 514  TRP A CE3   1 
ATOM   4042 C CZ2   . TRP A 1 514 ? -15.512 79.003  47.666 1.00 23.32 ? 514  TRP A CZ2   1 
ATOM   4043 C CZ3   . TRP A 1 514 ? -16.231 77.485  49.405 1.00 24.50 ? 514  TRP A CZ3   1 
ATOM   4044 C CH2   . TRP A 1 514 ? -16.470 78.549  48.539 1.00 24.30 ? 514  TRP A CH2   1 
ATOM   4045 N N     . GLY A 1 515 ? -9.856  74.306  50.936 1.00 24.13 ? 515  GLY A N     1 
ATOM   4046 C CA    . GLY A 1 515 ? -9.671  73.105  51.793 1.00 24.16 ? 515  GLY A CA    1 
ATOM   4047 C C     . GLY A 1 515 ? -10.259 71.865  51.118 1.00 24.37 ? 515  GLY A C     1 
ATOM   4048 O O     . GLY A 1 515 ? -11.244 72.005  50.292 1.00 25.16 ? 515  GLY A O     1 
ATOM   4049 N N     . LYS A 1 516 ? -9.697  70.703  51.386 1.00 25.05 ? 516  LYS A N     1 
ATOM   4050 C CA    . LYS A 1 516 ? -9.950  69.471  50.577 1.00 28.34 ? 516  LYS A CA    1 
ATOM   4051 C C     . LYS A 1 516 ? -11.415 69.051  50.632 1.00 28.07 ? 516  LYS A C     1 
ATOM   4052 O O     . LYS A 1 516 ? -11.891 68.594  49.614 1.00 29.26 ? 516  LYS A O     1 
ATOM   4053 C CB    . LYS A 1 516 ? -9.048  68.312  50.997 1.00 31.94 ? 516  LYS A CB    1 
ATOM   4054 C CG    . LYS A 1 516 ? -9.286  67.783  52.394 1.00 41.47 ? 516  LYS A CG    1 
ATOM   4055 C CD    . LYS A 1 516 ? -8.267  66.709  52.774 1.00 49.98 ? 516  LYS A CD    1 
ATOM   4056 C CE    . LYS A 1 516 ? -7.838  66.801  54.230 1.00 55.89 ? 516  LYS A CE    1 
ATOM   4057 N NZ    . LYS A 1 516 ? -9.007  66.627  55.128 1.00 52.86 ? 516  LYS A NZ    1 
ATOM   4058 N N     . ASN A 1 517 ? -12.157 69.329  51.688 1.00 25.94 ? 517  ASN A N     1 
ATOM   4059 C CA    . ASN A 1 517 ? -13.570 68.891  51.787 1.00 30.23 ? 517  ASN A CA    1 
ATOM   4060 C C     . ASN A 1 517 ? -14.420 69.671  50.767 1.00 34.92 ? 517  ASN A C     1 
ATOM   4061 O O     . ASN A 1 517 ? -15.467 69.152  50.417 1.00 33.59 ? 517  ASN A O     1 
ATOM   4062 C CB    . ASN A 1 517 ? -14.148 69.069  53.201 1.00 30.35 ? 517  ASN A CB    1 
ATOM   4063 C CG    . ASN A 1 517 ? -13.542 68.106  54.197 1.00 35.99 ? 517  ASN A CG    1 
ATOM   4064 O OD1   . ASN A 1 517 ? -12.859 67.145  53.837 1.00 35.39 ? 517  ASN A OD1   1 
ATOM   4065 N ND2   . ASN A 1 517 ? -13.762 68.358  55.468 1.00 39.56 ? 517  ASN A ND2   1 
ATOM   4066 N N     . ARG A 1 518 ? -14.021 70.874  50.341 1.00 30.19 ? 518  ARG A N     1 
ATOM   4067 C CA    . ARG A 1 518 ? -14.859 71.730  49.454 1.00 34.57 ? 518  ARG A CA    1 
ATOM   4068 C C     . ARG A 1 518 ? -14.225 72.075  48.093 1.00 39.23 ? 518  ARG A C     1 
ATOM   4069 O O     . ARG A 1 518 ? -14.952 72.645  47.317 1.00 47.38 ? 518  ARG A O     1 
ATOM   4070 C CB    . ARG A 1 518 ? -15.303 72.997  50.182 1.00 33.07 ? 518  ARG A CB    1 
ATOM   4071 C CG    . ARG A 1 518 ? -16.075 72.694  51.454 1.00 32.17 ? 518  ARG A CG    1 
ATOM   4072 C CD    . ARG A 1 518 ? -16.686 73.923  52.085 1.00 35.14 ? 518  ARG A CD    1 
ATOM   4073 N NE    . ARG A 1 518 ? -17.345 73.589  53.331 1.00 32.83 ? 518  ARG A NE    1 
ATOM   4074 C CZ    . ARG A 1 518 ? -18.616 73.145  53.457 1.00 38.55 ? 518  ARG A CZ    1 
ATOM   4075 N NH1   . ARG A 1 518 ? -19.442 73.024  52.419 1.00 38.04 ? 518  ARG A NH1   1 
ATOM   4076 N NH2   . ARG A 1 518 ? -19.076 72.876  54.659 1.00 41.60 ? 518  ARG A NH2   1 
ATOM   4077 N N     . ARG A 1 519 ? -12.987 71.748  47.718 1.00 42.86 ? 519  ARG A N     1 
ATOM   4078 C CA    . ARG A 1 519 ? -12.551 72.190  46.352 1.00 47.63 ? 519  ARG A CA    1 
ATOM   4079 C C     . ARG A 1 519 ? -12.936 71.154  45.283 1.00 46.97 ? 519  ARG A C     1 
ATOM   4080 O O     . ARG A 1 519 ? -12.933 69.970  45.631 1.00 43.29 ? 519  ARG A O     1 
ATOM   4081 C CB    . ARG A 1 519 ? -11.073 72.593  46.270 1.00 51.97 ? 519  ARG A CB    1 
ATOM   4082 C CG    . ARG A 1 519 ? -10.124 71.894  47.211 1.00 49.44 ? 519  ARG A CG    1 
ATOM   4083 C CD    . ARG A 1 519 ? -8.668  72.178  46.848 1.00 48.67 ? 519  ARG A CD    1 
ATOM   4084 N NE    . ARG A 1 519 ? -7.876  71.001  47.221 1.00 43.07 ? 519  ARG A NE    1 
ATOM   4085 C CZ    . ARG A 1 519 ? -7.351  70.756  48.440 1.00 40.74 ? 519  ARG A CZ    1 
ATOM   4086 N NH1   . ARG A 1 519 ? -7.464  71.615  49.438 1.00 35.82 ? 519  ARG A NH1   1 
ATOM   4087 N NH2   . ARG A 1 519 ? -6.723  69.621  48.653 1.00 42.18 ? 519  ARG A NH2   1 
ATOM   4088 N N     . MET B 1 1   ? 36.534  59.611  61.479 1.00 58.51 ? 1    MET B N     1 
ATOM   4089 C CA    . MET B 1 1   ? 36.926  60.819  60.711 1.00 54.65 ? 1    MET B CA    1 
ATOM   4090 C C     . MET B 1 1   ? 35.815  61.081  59.672 1.00 53.74 ? 1    MET B C     1 
ATOM   4091 O O     . MET B 1 1   ? 35.233  62.140  59.776 1.00 48.94 ? 1    MET B O     1 
ATOM   4092 C CB    . MET B 1 1   ? 38.299  60.671  60.036 1.00 57.05 ? 1    MET B CB    1 
ATOM   4093 N N     . ALA B 1 2   ? 35.474  60.137  58.771 1.00 43.89 ? 2    ALA B N     1 
ATOM   4094 C CA    . ALA B 1 2   ? 34.482  60.358  57.686 1.00 39.72 ? 2    ALA B CA    1 
ATOM   4095 C C     . ALA B 1 2   ? 33.081  60.490  58.289 1.00 40.32 ? 2    ALA B C     1 
ATOM   4096 O O     . ALA B 1 2   ? 32.826  59.918  59.366 1.00 39.10 ? 2    ALA B O     1 
ATOM   4097 C CB    . ALA B 1 2   ? 34.494  59.268  56.653 1.00 38.75 ? 2    ALA B CB    1 
ATOM   4098 N N     . ALA B 1 3   ? 32.186  61.192  57.583 1.00 37.11 ? 3    ALA B N     1 
ATOM   4099 C CA    . ALA B 1 3   ? 30.807  61.468  58.018 1.00 33.61 ? 3    ALA B CA    1 
ATOM   4100 C C     . ALA B 1 3   ? 30.080  60.141  58.074 1.00 30.80 ? 3    ALA B C     1 
ATOM   4101 O O     . ALA B 1 3   ? 30.242  59.320  57.187 1.00 29.33 ? 3    ALA B O     1 
ATOM   4102 C CB    . ALA B 1 3   ? 30.122  62.403  57.046 1.00 36.13 ? 3    ALA B CB    1 
ATOM   4103 N N     . PRO B 1 4   ? 29.203  59.929  59.060 1.00 29.27 ? 4    PRO B N     1 
ATOM   4104 C CA    . PRO B 1 4   ? 28.300  58.788  59.026 1.00 31.94 ? 4    PRO B CA    1 
ATOM   4105 C C     . PRO B 1 4   ? 27.131  59.027  58.069 1.00 32.84 ? 4    PRO B C     1 
ATOM   4106 O O     . PRO B 1 4   ? 26.786  60.190  57.811 1.00 32.20 ? 4    PRO B O     1 
ATOM   4107 C CB    . PRO B 1 4   ? 27.754  58.729  60.449 1.00 30.66 ? 4    PRO B CB    1 
ATOM   4108 C CG    . PRO B 1 4   ? 27.766  60.183  60.890 1.00 31.81 ? 4    PRO B CG    1 
ATOM   4109 C CD    . PRO B 1 4   ? 28.952  60.829  60.194 1.00 30.73 ? 4    PRO B CD    1 
ATOM   4110 N N     . LEU B 1 5   ? 26.532  57.946  57.590 1.00 27.72 ? 5    LEU B N     1 
ATOM   4111 C CA    . LEU B 1 5   ? 25.193  57.997  56.961 1.00 28.88 ? 5    LEU B CA    1 
ATOM   4112 C C     . LEU B 1 5   ? 24.179  58.594  57.933 1.00 31.28 ? 5    LEU B C     1 
ATOM   4113 O O     . LEU B 1 5   ? 24.211  58.360  59.133 1.00 29.53 ? 5    LEU B O     1 
ATOM   4114 C CB    . LEU B 1 5   ? 24.741  56.598  56.525 1.00 29.86 ? 5    LEU B CB    1 
ATOM   4115 C CG    . LEU B 1 5   ? 25.533  55.976  55.380 1.00 27.44 ? 5    LEU B CG    1 
ATOM   4116 C CD1   . LEU B 1 5   ? 25.317  54.467  55.318 1.00 31.15 ? 5    LEU B CD1   1 
ATOM   4117 C CD2   . LEU B 1 5   ? 25.160  56.612  54.064 1.00 27.55 ? 5    LEU B CD2   1 
ATOM   4118 N N     . PRO B 1 6   ? 23.185  59.366  57.430 1.00 29.25 ? 6    PRO B N     1 
ATOM   4119 C CA    . PRO B 1 6   ? 22.098  59.818  58.270 1.00 33.01 ? 6    PRO B CA    1 
ATOM   4120 C C     . PRO B 1 6   ? 21.261  58.611  58.706 1.00 36.60 ? 6    PRO B C     1 
ATOM   4121 O O     . PRO B 1 6   ? 21.148  57.673  57.960 1.00 32.21 ? 6    PRO B O     1 
ATOM   4122 C CB    . PRO B 1 6   ? 21.336  60.777  57.348 1.00 33.07 ? 6    PRO B CB    1 
ATOM   4123 C CG    . PRO B 1 6   ? 21.631  60.338  55.982 1.00 31.69 ? 6    PRO B CG    1 
ATOM   4124 C CD    . PRO B 1 6   ? 22.991  59.686  56.015 1.00 30.36 ? 6    PRO B CD    1 
ATOM   4125 N N     . GLU B 1 7   ? 20.734  58.656  59.921 1.00 36.89 ? 7    GLU B N     1 
ATOM   4126 C CA    . GLU B 1 7   ? 19.929  57.555  60.489 1.00 39.46 ? 7    GLU B CA    1 
ATOM   4127 C C     . GLU B 1 7   ? 18.754  57.253  59.559 1.00 39.26 ? 7    GLU B C     1 
ATOM   4128 O O     . GLU B 1 7   ? 18.064  58.185  59.115 1.00 37.57 ? 7    GLU B O     1 
ATOM   4129 C CB    . GLU B 1 7   ? 19.475  57.874  61.911 1.00 43.98 ? 7    GLU B CB    1 
ATOM   4130 C CG    . GLU B 1 7   ? 18.976  56.644  62.649 1.00 57.31 ? 7    GLU B CG    1 
ATOM   4131 C CD    . GLU B 1 7   ? 17.711  56.847  63.470 1.00 69.78 ? 7    GLU B CD    1 
ATOM   4132 O OE1   . GLU B 1 7   ? 17.754  57.658  64.426 1.00 66.94 ? 7    GLU B OE1   1 
ATOM   4133 O OE2   . GLU B 1 7   ? 16.677  56.201  63.135 1.00 78.05 ? 7    GLU B OE2   1 
ATOM   4134 N N     . GLY B 1 8   ? 18.560  55.974  59.229 1.00 38.98 ? 8    GLY B N     1 
ATOM   4135 C CA    . GLY B 1 8   ? 17.428  55.519  58.414 1.00 35.69 ? 8    GLY B CA    1 
ATOM   4136 C C     . GLY B 1 8   ? 17.768  55.523  56.952 1.00 32.50 ? 8    GLY B C     1 
ATOM   4137 O O     . GLY B 1 8   ? 16.917  55.188  56.174 1.00 39.21 ? 8    GLY B O     1 
ATOM   4138 N N     . VAL B 1 9   ? 18.986  55.866  56.577 1.00 30.83 ? 9    VAL B N     1 
ATOM   4139 C CA    . VAL B 1 9   ? 19.398  55.863  55.158 1.00 29.68 ? 9    VAL B CA    1 
ATOM   4140 C C     . VAL B 1 9   ? 20.506  54.817  54.960 1.00 32.78 ? 9    VAL B C     1 
ATOM   4141 O O     . VAL B 1 9   ? 21.577  54.947  55.566 1.00 32.29 ? 9    VAL B O     1 
ATOM   4142 C CB    . VAL B 1 9   ? 19.855  57.258  54.694 1.00 33.90 ? 9    VAL B CB    1 
ATOM   4143 C CG1   . VAL B 1 9   ? 20.238  57.234  53.228 1.00 33.19 ? 9    VAL B CG1   1 
ATOM   4144 C CG2   . VAL B 1 9   ? 18.789  58.328  54.967 1.00 37.25 ? 9    VAL B CG2   1 
ATOM   4145 N N     . SER B 1 10  ? 20.292  53.881  54.044 1.00 32.68 ? 10   SER B N     1 
ATOM   4146 C CA    . SER B 1 10  ? 21.237  52.769  53.770 1.00 34.91 ? 10   SER B CA    1 
ATOM   4147 C C     . SER B 1 10  ? 22.343  53.288  52.852 1.00 35.59 ? 10   SER B C     1 
ATOM   4148 O O     . SER B 1 10  ? 22.096  54.305  52.119 1.00 29.43 ? 10   SER B O     1 
ATOM   4149 C CB    . SER B 1 10  ? 20.516  51.605  53.147 1.00 34.11 ? 10   SER B CB    1 
ATOM   4150 O OG    . SER B 1 10  ? 20.204  51.925  51.790 1.00 35.28 ? 10   SER B OG    1 
ATOM   4151 N N     . ALA B 1 11  ? 23.482  52.580  52.814 1.00 32.99 ? 11   ALA B N     1 
ATOM   4152 C CA    . ALA B 1 11  ? 24.615  52.872  51.911 1.00 31.43 ? 11   ALA B CA    1 
ATOM   4153 C C     . ALA B 1 11  ? 24.085  52.866  50.488 1.00 34.69 ? 11   ALA B C     1 
ATOM   4154 O O     . ALA B 1 11  ? 24.559  53.689  49.669 1.00 34.26 ? 11   ALA B O     1 
ATOM   4155 C CB    . ALA B 1 11  ? 25.752  51.888  52.087 1.00 32.01 ? 11   ALA B CB    1 
ATOM   4156 N N     . GLU B 1 12  ? 23.130  51.980  50.206 1.00 35.42 ? 12   GLU B N     1 
ATOM   4157 C CA    . GLU B 1 12  ? 22.607  51.765  48.826 1.00 38.11 ? 12   GLU B CA    1 
ATOM   4158 C C     . GLU B 1 12  ? 21.740  52.976  48.424 1.00 31.49 ? 12   GLU B C     1 
ATOM   4159 O O     . GLU B 1 12  ? 21.892  53.454  47.319 1.00 34.54 ? 12   GLU B O     1 
ATOM   4160 C CB    . GLU B 1 12  ? 21.828  50.443  48.740 1.00 45.92 ? 12   GLU B CB    1 
ATOM   4161 C CG    . GLU B 1 12  ? 22.673  49.191  49.048 1.00 57.15 ? 12   GLU B CG    1 
ATOM   4162 C CD    . GLU B 1 12  ? 23.107  48.925  50.504 1.00 58.92 ? 12   GLU B CD    1 
ATOM   4163 O OE1   . GLU B 1 12  ? 22.280  49.086  51.462 1.00 55.67 ? 12   GLU B OE1   1 
ATOM   4164 O OE2   . GLU B 1 12  ? 24.293  48.559  50.689 1.00 70.51 ? 12   GLU B OE2   1 
ATOM   4165 N N     . ALA B 1 13  ? 20.831  53.406  49.290 1.00 31.84 ? 13   ALA B N     1 
ATOM   4166 C CA    . ALA B 1 13  ? 19.986  54.594  49.073 1.00 32.96 ? 13   ALA B CA    1 
ATOM   4167 C C     . ALA B 1 13  ? 20.884  55.834  48.895 1.00 30.90 ? 13   ALA B C     1 
ATOM   4168 O O     . ALA B 1 13  ? 20.660  56.566  47.911 1.00 29.04 ? 13   ALA B O     1 
ATOM   4169 C CB    . ALA B 1 13  ? 18.999  54.742  50.199 1.00 31.08 ? 13   ALA B CB    1 
ATOM   4170 N N     . MET B 1 14  ? 21.901  56.033  49.747 1.00 28.62 ? 14   MET B N     1 
ATOM   4171 C CA    . MET B 1 14  ? 22.843  57.179  49.614 1.00 30.83 ? 14   MET B CA    1 
ATOM   4172 C C     . MET B 1 14  ? 23.555  57.106  48.267 1.00 32.98 ? 14   MET B C     1 
ATOM   4173 O O     . MET B 1 14  ? 23.613  58.121  47.532 1.00 30.33 ? 14   MET B O     1 
ATOM   4174 C CB    . MET B 1 14  ? 23.889  57.231  50.734 1.00 29.85 ? 14   MET B CB    1 
ATOM   4175 C CG    . MET B 1 14  ? 24.851  58.404  50.614 1.00 31.55 ? 14   MET B CG    1 
ATOM   4176 S SD    . MET B 1 14  ? 24.005  60.053  50.670 1.00 30.75 ? 14   MET B SD    1 
ATOM   4177 C CE    . MET B 1 14  ? 23.685  60.248  52.414 1.00 29.51 ? 14   MET B CE    1 
ATOM   4178 N N     . SER B 1 15  ? 24.045  55.921  47.921 1.00 35.85 ? 15   SER B N     1 
ATOM   4179 C CA    . SER B 1 15  ? 24.882  55.748  46.719 1.00 33.61 ? 15   SER B CA    1 
ATOM   4180 C C     . SER B 1 15  ? 24.024  55.997  45.459 1.00 29.39 ? 15   SER B C     1 
ATOM   4181 O O     . SER B 1 15  ? 24.533  56.600  44.476 1.00 26.77 ? 15   SER B O     1 
ATOM   4182 C CB    . SER B 1 15  ? 25.514  54.384  46.746 1.00 39.84 ? 15   SER B CB    1 
ATOM   4183 O OG    . SER B 1 15  ? 26.117  54.125  45.500 1.00 45.16 ? 15   SER B OG    1 
ATOM   4184 N N     . SER B 1 16  ? 22.785  55.528  45.453 1.00 29.73 ? 16   SER B N     1 
ATOM   4185 C CA    . SER B 1 16  ? 21.839  55.754  44.332 1.00 35.29 ? 16   SER B CA    1 
ATOM   4186 C C     . SER B 1 16  ? 21.508  57.250  44.243 1.00 31.87 ? 16   SER B C     1 
ATOM   4187 O O     . SER B 1 16  ? 21.376  57.764  43.125 1.00 29.66 ? 16   SER B O     1 
ATOM   4188 C CB    . SER B 1 16  ? 20.572  54.963  44.492 1.00 36.71 ? 16   SER B CB    1 
ATOM   4189 O OG    . SER B 1 16  ? 20.850  53.590  44.456 1.00 39.59 ? 16   SER B OG    1 
ATOM   4190 N N     . ALA B 1 17  ? 21.373  57.932  45.380 1.00 29.02 ? 17   ALA B N     1 
ATOM   4191 C CA    . ALA B 1 17  ? 21.072  59.375  45.390 1.00 27.71 ? 17   ALA B CA    1 
ATOM   4192 C C     . ALA B 1 17  ? 22.252  60.122  44.798 1.00 23.46 ? 17   ALA B C     1 
ATOM   4193 O O     . ALA B 1 17  ? 22.036  60.967  43.897 1.00 22.42 ? 17   ALA B O     1 
ATOM   4194 C CB    . ALA B 1 17  ? 20.733  59.868  46.782 1.00 26.60 ? 17   ALA B CB    1 
ATOM   4195 N N     . LEU B 1 18  ? 23.468  59.813  45.219 1.00 25.47 ? 18   LEU B N     1 
ATOM   4196 C CA    . LEU B 1 18  ? 24.641  60.570  44.729 1.00 25.96 ? 18   LEU B CA    1 
ATOM   4197 C C     . LEU B 1 18  ? 24.884  60.321  43.215 1.00 27.74 ? 18   LEU B C     1 
ATOM   4198 O O     . LEU B 1 18  ? 25.262  61.321  42.528 1.00 25.59 ? 18   LEU B O     1 
ATOM   4199 C CB    . LEU B 1 18  ? 25.859  60.230  45.576 1.00 28.66 ? 18   LEU B CB    1 
ATOM   4200 C CG    . LEU B 1 18  ? 25.808  60.619  47.055 1.00 30.98 ? 18   LEU B CG    1 
ATOM   4201 C CD1   . LEU B 1 18  ? 27.105  60.224  47.714 1.00 32.42 ? 18   LEU B CD1   1 
ATOM   4202 C CD2   . LEU B 1 18  ? 25.581  62.098  47.247 1.00 30.90 ? 18   LEU B CD2   1 
ATOM   4203 N N     . ASP B 1 19  ? 24.679  59.100  42.681 1.00 29.02 ? 19   ASP B N     1 
ATOM   4204 C CA    . ASP B 1 19  ? 24.721  58.856  41.204 1.00 28.77 ? 19   ASP B CA    1 
ATOM   4205 C C     . ASP B 1 19  ? 23.679  59.769  40.512 1.00 24.96 ? 19   ASP B C     1 
ATOM   4206 O O     . ASP B 1 19  ? 24.047  60.456  39.545 1.00 25.25 ? 19   ASP B O     1 
ATOM   4207 C CB    . ASP B 1 19  ? 24.468  57.406  40.757 1.00 36.64 ? 19   ASP B CB    1 
ATOM   4208 C CG    . ASP B 1 19  ? 24.236  57.228  39.232 1.00 38.24 ? 19   ASP B CG    1 
ATOM   4209 O OD1   . ASP B 1 19  ? 25.228  57.391  38.438 1.00 41.28 ? 19   ASP B OD1   1 
ATOM   4210 O OD2   . ASP B 1 19  ? 23.041  56.964  38.822 1.00 43.93 ? 19   ASP B OD2   1 
ATOM   4211 N N     . ARG B 1 20  ? 22.453  59.829  41.024 1.00 24.15 ? 20   ARG B N     1 
ATOM   4212 C CA    . ARG B 1 20  ? 21.379  60.625  40.372 1.00 26.60 ? 20   ARG B CA    1 
ATOM   4213 C C     . ARG B 1 20  ? 21.766  62.098  40.418 1.00 24.10 ? 20   ARG B C     1 
ATOM   4214 O O     . ARG B 1 20  ? 21.551  62.783  39.425 1.00 24.24 ? 20   ARG B O     1 
ATOM   4215 C CB    . ARG B 1 20  ? 20.022  60.229  40.933 1.00 26.88 ? 20   ARG B CB    1 
ATOM   4216 C CG    . ARG B 1 20  ? 19.524  58.933  40.306 1.00 32.76 ? 20   ARG B CG    1 
ATOM   4217 C CD    . ARG B 1 20  ? 18.568  58.324  41.291 1.00 41.90 ? 20   ARG B CD    1 
ATOM   4218 N NE    . ARG B 1 20  ? 17.837  57.118  40.899 1.00 48.92 ? 20   ARG B NE    1 
ATOM   4219 C CZ    . ARG B 1 20  ? 18.367  55.919  40.714 1.00 51.23 ? 20   ARG B CZ    1 
ATOM   4220 N NH1   . ARG B 1 20  ? 19.679  55.714  40.739 1.00 60.10 ? 20   ARG B NH1   1 
ATOM   4221 N NH2   . ARG B 1 20  ? 17.548  54.928  40.442 1.00 49.47 ? 20   ARG B NH2   1 
ATOM   4222 N N     . PHE B 1 21  ? 22.304  62.573  41.542 1.00 24.34 ? 21   PHE B N     1 
ATOM   4223 C CA    . PHE B 1 21  ? 22.768  63.977  41.661 1.00 22.97 ? 21   PHE B CA    1 
ATOM   4224 C C     . PHE B 1 21  ? 23.793  64.252  40.566 1.00 22.10 ? 21   PHE B C     1 
ATOM   4225 O O     . PHE B 1 21  ? 23.721  65.307  39.883 1.00 22.47 ? 21   PHE B O     1 
ATOM   4226 C CB    . PHE B 1 21  ? 23.311  64.299  43.062 1.00 21.91 ? 21   PHE B CB    1 
ATOM   4227 C CG    . PHE B 1 21  ? 22.352  64.223  44.223 1.00 22.26 ? 21   PHE B CG    1 
ATOM   4228 C CD1   . PHE B 1 21  ? 20.984  64.282  44.071 1.00 20.65 ? 21   PHE B CD1   1 
ATOM   4229 C CD2   . PHE B 1 21  ? 22.857  64.033  45.497 1.00 24.31 ? 21   PHE B CD2   1 
ATOM   4230 C CE1   . PHE B 1 21  ? 20.131  64.201  45.159 1.00 23.71 ? 21   PHE B CE1   1 
ATOM   4231 C CE2   . PHE B 1 21  ? 22.018  63.982  46.590 1.00 25.35 ? 21   PHE B CE2   1 
ATOM   4232 C CZ    . PHE B 1 21  ? 20.653  64.045  46.415 1.00 26.80 ? 21   PHE B CZ    1 
ATOM   4233 N N     . ALA B 1 22  ? 24.751  63.345  40.372 1.00 25.38 ? 22   ALA B N     1 
ATOM   4234 C CA    . ALA B 1 22  ? 25.832  63.510  39.361 1.00 26.48 ? 22   ALA B CA    1 
ATOM   4235 C C     . ALA B 1 22  ? 25.237  63.561  37.945 1.00 23.26 ? 22   ALA B C     1 
ATOM   4236 O O     . ALA B 1 22  ? 25.723  64.325  37.128 1.00 22.53 ? 22   ALA B O     1 
ATOM   4237 C CB    . ALA B 1 22  ? 26.901  62.428  39.525 1.00 26.08 ? 22   ALA B CB    1 
ATOM   4238 N N     . ARG B 1 23  ? 24.186  62.817  37.661 1.00 23.38 ? 23   ARG B N     1 
ATOM   4239 C CA    . ARG B 1 23  ? 23.499  62.885  36.338 1.00 24.49 ? 23   ARG B CA    1 
ATOM   4240 C C     . ARG B 1 23  ? 22.834  64.239  36.150 1.00 29.37 ? 23   ARG B C     1 
ATOM   4241 O O     . ARG B 1 23  ? 22.844  64.766  35.044 1.00 26.09 ? 23   ARG B O     1 
ATOM   4242 C CB    . ARG B 1 23  ? 22.404  61.825  36.273 1.00 25.00 ? 23   ARG B CB    1 
ATOM   4243 C CG    . ARG B 1 23  ? 22.936  60.398  36.289 1.00 25.25 ? 23   ARG B CG    1 
ATOM   4244 C CD    . ARG B 1 23  ? 21.799  59.479  35.975 1.00 25.53 ? 23   ARG B CD    1 
ATOM   4245 N NE    . ARG B 1 23  ? 22.130  58.108  36.266 1.00 26.69 ? 23   ARG B NE    1 
ATOM   4246 C CZ    . ARG B 1 23  ? 21.543  57.040  35.734 1.00 33.88 ? 23   ARG B CZ    1 
ATOM   4247 N NH1   . ARG B 1 23  ? 20.551  57.203  34.870 1.00 32.77 ? 23   ARG B NH1   1 
ATOM   4248 N NH2   . ARG B 1 23  ? 21.958  55.811  36.075 1.00 33.28 ? 23   ARG B NH2   1 
ATOM   4249 N N     . ILE B 1 24  ? 22.289  64.812  37.226 1.00 27.05 ? 24   ILE B N     1 
ATOM   4250 C CA    . ILE B 1 24  ? 21.589  66.113  37.155 1.00 24.33 ? 24   ILE B CA    1 
ATOM   4251 C C     . ILE B 1 24  ? 22.583  67.249  36.956 1.00 22.92 ? 24   ILE B C     1 
ATOM   4252 O O     . ILE B 1 24  ? 22.331  68.071  36.106 1.00 23.69 ? 24   ILE B O     1 
ATOM   4253 C CB    . ILE B 1 24  ? 20.734  66.328  38.418 1.00 24.40 ? 24   ILE B CB    1 
ATOM   4254 C CG1   . ILE B 1 24  ? 19.577  65.335  38.424 1.00 24.74 ? 24   ILE B CG1   1 
ATOM   4255 C CG2   . ILE B 1 24  ? 20.283  67.782  38.485 1.00 24.27 ? 24   ILE B CG2   1 
ATOM   4256 C CD1   . ILE B 1 24  ? 18.989  65.096  39.776 1.00 27.22 ? 24   ILE B CD1   1 
ATOM   4257 N N     . VAL B 1 25  ? 23.645  67.327  37.737 1.00 22.49 ? 25   VAL B N     1 
ATOM   4258 C CA    . VAL B 1 25  ? 24.553  68.499  37.766 1.00 23.27 ? 25   VAL B CA    1 
ATOM   4259 C C     . VAL B 1 25  ? 25.842  68.252  36.991 1.00 24.61 ? 25   VAL B C     1 
ATOM   4260 O O     . VAL B 1 25  ? 26.560  69.263  36.682 1.00 25.91 ? 25   VAL B O     1 
ATOM   4261 C CB    . VAL B 1 25  ? 24.849  68.927  39.206 1.00 23.65 ? 25   VAL B CB    1 
ATOM   4262 C CG1   . VAL B 1 25  ? 23.560  69.294  39.934 1.00 23.49 ? 25   VAL B CG1   1 
ATOM   4263 C CG2   . VAL B 1 25  ? 25.651  67.900  40.008 1.00 22.20 ? 25   VAL B CG2   1 
ATOM   4264 N N     . GLY B 1 26  ? 26.157  66.993  36.718 1.00 28.81 ? 26   GLY B N     1 
ATOM   4265 C CA    . GLY B 1 26  ? 27.485  66.617  36.206 1.00 28.21 ? 26   GLY B CA    1 
ATOM   4266 C C     . GLY B 1 26  ? 28.371  66.081  37.316 1.00 32.84 ? 26   GLY B C     1 
ATOM   4267 O O     . GLY B 1 26  ? 28.380  66.645  38.472 1.00 29.32 ? 26   GLY B O     1 
ATOM   4268 N N     . ALA B 1 27  ? 29.198  65.082  36.995 1.00 30.60 ? 27   ALA B N     1 
ATOM   4269 C CA    . ALA B 1 27  ? 30.057  64.415  37.992 1.00 27.59 ? 27   ALA B CA    1 
ATOM   4270 C C     . ALA B 1 27  ? 31.009  65.433  38.619 1.00 26.26 ? 27   ALA B C     1 
ATOM   4271 O O     . ALA B 1 27  ? 31.322  65.272  39.782 1.00 28.12 ? 27   ALA B O     1 
ATOM   4272 C CB    . ALA B 1 27  ? 30.825  63.282  37.341 1.00 33.44 ? 27   ALA B CB    1 
ATOM   4273 N N     . ASP B 1 28  ? 31.414  66.502  37.934 1.00 26.20 ? 28   ASP B N     1 
ATOM   4274 C CA    . ASP B 1 28  ? 32.369  67.479  38.548 1.00 26.27 ? 28   ASP B CA    1 
ATOM   4275 C C     . ASP B 1 28  ? 31.753  68.244  39.761 1.00 23.20 ? 28   ASP B C     1 
ATOM   4276 O O     . ASP B 1 28  ? 32.516  68.842  40.512 1.00 23.90 ? 28   ASP B O     1 
ATOM   4277 C CB    . ASP B 1 28  ? 32.823  68.543  37.533 1.00 31.61 ? 28   ASP B CB    1 
ATOM   4278 C CG    . ASP B 1 28  ? 33.651  67.983  36.366 1.00 33.76 ? 28   ASP B CG    1 
ATOM   4279 O OD1   . ASP B 1 28  ? 34.243  66.914  36.543 1.00 31.36 ? 28   ASP B OD1   1 
ATOM   4280 O OD2   . ASP B 1 28  ? 33.588  68.557  35.292 1.00 41.67 ? 28   ASP B OD2   1 
ATOM   4281 N N     . TRP B 1 29  ? 30.446  68.210  39.964 1.00 25.50 ? 29   TRP B N     1 
ATOM   4282 C CA    . TRP B 1 29  ? 29.752  69.111  40.951 1.00 23.70 ? 29   TRP B CA    1 
ATOM   4283 C C     . TRP B 1 29  ? 29.048  68.295  42.034 1.00 24.19 ? 29   TRP B C     1 
ATOM   4284 O O     . TRP B 1 29  ? 28.135  68.834  42.683 1.00 24.25 ? 29   TRP B O     1 
ATOM   4285 C CB    . TRP B 1 29  ? 28.790  70.008  40.178 1.00 23.61 ? 29   TRP B CB    1 
ATOM   4286 C CG    . TRP B 1 29  ? 29.507  70.841  39.176 1.00 23.70 ? 29   TRP B CG    1 
ATOM   4287 C CD1   . TRP B 1 29  ? 29.408  70.729  37.824 1.00 25.32 ? 29   TRP B CD1   1 
ATOM   4288 C CD2   . TRP B 1 29  ? 30.488  71.858  39.430 1.00 24.06 ? 29   TRP B CD2   1 
ATOM   4289 N NE1   . TRP B 1 29  ? 30.214  71.651  37.234 1.00 27.49 ? 29   TRP B NE1   1 
ATOM   4290 C CE2   . TRP B 1 29  ? 30.897  72.349  38.175 1.00 24.79 ? 29   TRP B CE2   1 
ATOM   4291 C CE3   . TRP B 1 29  ? 31.059  72.407  40.569 1.00 24.45 ? 29   TRP B CE3   1 
ATOM   4292 C CZ2   . TRP B 1 29  ? 31.839  73.361  38.032 1.00 29.85 ? 29   TRP B CZ2   1 
ATOM   4293 C CZ3   . TRP B 1 29  ? 31.962  73.442  40.445 1.00 29.83 ? 29   TRP B CZ3   1 
ATOM   4294 C CH2   . TRP B 1 29  ? 32.352  73.904  39.185 1.00 28.27 ? 29   TRP B CH2   1 
ATOM   4295 N N     . VAL B 1 30  ? 29.490  67.054  42.249 1.00 25.59 ? 30   VAL B N     1 
ATOM   4296 C CA    . VAL B 1 30  ? 29.137  66.237  43.433 1.00 23.91 ? 30   VAL B CA    1 
ATOM   4297 C C     . VAL B 1 30  ? 30.439  65.997  44.182 1.00 28.10 ? 30   VAL B C     1 
ATOM   4298 O O     . VAL B 1 30  ? 31.348  65.411  43.611 1.00 26.24 ? 30   VAL B O     1 
ATOM   4299 C CB    . VAL B 1 30  ? 28.435  64.922  43.081 1.00 25.22 ? 30   VAL B CB    1 
ATOM   4300 C CG1   . VAL B 1 30  ? 28.141  64.103  44.324 1.00 26.94 ? 30   VAL B CG1   1 
ATOM   4301 C CG2   . VAL B 1 30  ? 27.170  65.118  42.293 1.00 27.17 ? 30   VAL B CG2   1 
ATOM   4302 N N     . PHE B 1 31  ? 30.535  66.458  45.419 1.00 25.62 ? 31   PHE B N     1 
ATOM   4303 C CA    . PHE B 1 31  ? 31.771  66.473  46.229 1.00 27.06 ? 31   PHE B CA    1 
ATOM   4304 C C     . PHE B 1 31  ? 31.601  65.449  47.351 1.00 31.55 ? 31   PHE B C     1 
ATOM   4305 O O     . PHE B 1 31  ? 30.623  65.551  48.098 1.00 28.39 ? 31   PHE B O     1 
ATOM   4306 C CB    . PHE B 1 31  ? 32.000  67.885  46.769 1.00 30.21 ? 31   PHE B CB    1 
ATOM   4307 C CG    . PHE B 1 31  ? 32.153  68.921  45.685 1.00 29.43 ? 31   PHE B CG    1 
ATOM   4308 C CD1   . PHE B 1 31  ? 33.275  68.932  44.856 1.00 34.42 ? 31   PHE B CD1   1 
ATOM   4309 C CD2   . PHE B 1 31  ? 31.163  69.858  45.442 1.00 30.09 ? 31   PHE B CD2   1 
ATOM   4310 C CE1   . PHE B 1 31  ? 33.423  69.883  43.850 1.00 36.04 ? 31   PHE B CE1   1 
ATOM   4311 C CE2   . PHE B 1 31  ? 31.303  70.804  44.424 1.00 33.91 ? 31   PHE B CE2   1 
ATOM   4312 C CZ    . PHE B 1 31  ? 32.416  70.804  43.613 1.00 33.33 ? 31   PHE B CZ    1 
ATOM   4313 N N     . THR B 1 32  ? 32.469  64.441  47.457 1.00 31.92 ? 32   THR B N     1 
ATOM   4314 C CA    . THR B 1 32  ? 32.225  63.345  48.433 1.00 37.92 ? 32   THR B CA    1 
ATOM   4315 C C     . THR B 1 32  ? 33.348  63.079  49.428 1.00 45.71 ? 32   THR B C     1 
ATOM   4316 O O     . THR B 1 32  ? 33.045  62.410  50.463 1.00 62.43 ? 32   THR B O     1 
ATOM   4317 C CB    . THR B 1 32  ? 31.933  62.019  47.748 1.00 38.34 ? 32   THR B CB    1 
ATOM   4318 O OG1   . THR B 1 32  ? 33.043  61.771  46.876 1.00 38.77 ? 32   THR B OG1   1 
ATOM   4319 C CG2   . THR B 1 32  ? 30.625  62.071  46.996 1.00 42.89 ? 32   THR B CG2   1 
ATOM   4320 N N     . GLU B 1 33  ? 34.609  63.376  49.200 1.00 47.50 ? 33   GLU B N     1 
ATOM   4321 C CA    . GLU B 1 33  ? 35.491  62.722  50.230 1.00 54.59 ? 33   GLU B CA    1 
ATOM   4322 C C     . GLU B 1 33  ? 36.482  63.706  50.780 1.00 55.56 ? 33   GLU B C     1 
ATOM   4323 O O     . GLU B 1 33  ? 36.128  64.314  51.798 1.00 45.39 ? 33   GLU B O     1 
ATOM   4324 C CB    . GLU B 1 33  ? 36.158  61.453  49.712 1.00 64.50 ? 33   GLU B CB    1 
ATOM   4325 C CG    . GLU B 1 33  ? 35.290  60.230  49.954 1.00 70.15 ? 33   GLU B CG    1 
ATOM   4326 C CD    . GLU B 1 33  ? 35.324  59.194  48.850 1.00 80.53 ? 33   GLU B CD    1 
ATOM   4327 O OE1   . GLU B 1 33  ? 36.358  59.103  48.149 1.00 84.06 ? 33   GLU B OE1   1 
ATOM   4328 O OE2   . GLU B 1 33  ? 34.317  58.472  48.701 1.00 88.79 ? 33   GLU B OE2   1 
ATOM   4329 N N     . ASP B 1 34  ? 37.630  63.836  50.112 1.00 57.58 ? 34   ASP B N     1 
ATOM   4330 C CA    . ASP B 1 34  ? 38.659  64.869  50.403 1.00 61.89 ? 34   ASP B CA    1 
ATOM   4331 C C     . ASP B 1 34  ? 38.040  66.205  50.026 1.00 57.93 ? 34   ASP B C     1 
ATOM   4332 O O     . ASP B 1 34  ? 38.403  67.268  50.620 1.00 63.71 ? 34   ASP B O     1 
ATOM   4333 C CB    . ASP B 1 34  ? 39.950  64.608  49.621 1.00 79.59 ? 34   ASP B CB    1 
ATOM   4334 C CG    . ASP B 1 34  ? 39.673  64.107  48.209 1.00 86.41 ? 34   ASP B CG    1 
ATOM   4335 O OD1   . ASP B 1 34  ? 39.011  63.039  48.083 1.00 75.54 ? 34   ASP B OD1   1 
ATOM   4336 O OD2   . ASP B 1 34  ? 40.060  64.812  47.250 1.00 90.82 ? 34   ASP B OD2   1 
ATOM   4337 N N     . LYS B 1 35  ? 37.063  66.159  49.122 1.00 43.13 ? 35   LYS B N     1 
ATOM   4338 C CA    . LYS B 1 35  ? 36.508  67.406  48.582 1.00 41.22 ? 35   LYS B CA    1 
ATOM   4339 C C     . LYS B 1 35  ? 35.377  67.916  49.489 1.00 34.12 ? 35   LYS B C     1 
ATOM   4340 O O     . LYS B 1 35  ? 34.824  68.927  49.131 1.00 32.35 ? 35   LYS B O     1 
ATOM   4341 C CB    . LYS B 1 35  ? 36.107  67.177  47.121 1.00 49.68 ? 35   LYS B CB    1 
ATOM   4342 C CG    . LYS B 1 35  ? 37.247  66.731  46.199 1.00 55.39 ? 35   LYS B CG    1 
ATOM   4343 C CD    . LYS B 1 35  ? 37.040  67.174  44.746 1.00 71.03 ? 35   LYS B CD    1 
ATOM   4344 C CE    . LYS B 1 35  ? 37.427  66.135  43.705 1.00 82.43 ? 35   LYS B CE    1 
ATOM   4345 N NZ    . LYS B 1 35  ? 38.554  66.600  42.863 1.00 92.11 ? 35   LYS B NZ    1 
ATOM   4346 N N     . ILE B 1 36  ? 35.070  67.288  50.632 1.00 32.95 ? 36   ILE B N     1 
ATOM   4347 C CA    . ILE B 1 36  ? 33.968  67.741  51.539 1.00 31.84 ? 36   ILE B CA    1 
ATOM   4348 C C     . ILE B 1 36  ? 34.477  68.855  52.471 1.00 33.16 ? 36   ILE B C     1 
ATOM   4349 O O     . ILE B 1 36  ? 33.658  69.572  53.059 1.00 26.60 ? 36   ILE B O     1 
ATOM   4350 C CB    . ILE B 1 36  ? 33.342  66.552  52.306 1.00 36.64 ? 36   ILE B CB    1 
ATOM   4351 C CG1   . ILE B 1 36  ? 31.949  66.887  52.836 1.00 42.13 ? 36   ILE B CG1   1 
ATOM   4352 C CG2   . ILE B 1 36  ? 34.220  66.039  53.440 1.00 39.04 ? 36   ILE B CG2   1 
ATOM   4353 C CD1   . ILE B 1 36  ? 30.973  67.290  51.761 1.00 44.12 ? 36   ILE B CD1   1 
ATOM   4354 N N     . THR B 1 37  ? 35.794  69.023  52.594 1.00 31.99 ? 37   THR B N     1 
ATOM   4355 C CA    . THR B 1 37  ? 36.475  69.944  53.548 1.00 34.60 ? 37   THR B CA    1 
ATOM   4356 C C     . THR B 1 37  ? 35.818  71.326  53.587 1.00 31.44 ? 37   THR B C     1 
ATOM   4357 O O     . THR B 1 37  ? 35.528  71.844  54.659 1.00 29.78 ? 37   THR B O     1 
ATOM   4358 C CB    . THR B 1 37  ? 37.981  69.949  53.224 1.00 41.09 ? 37   THR B CB    1 
ATOM   4359 O OG1   . THR B 1 37  ? 38.535  68.905  54.033 1.00 43.50 ? 37   THR B OG1   1 
ATOM   4360 C CG2   . THR B 1 37  ? 38.677  71.265  53.475 1.00 48.00 ? 37   THR B CG2   1 
ATOM   4361 N N     . PRO B 1 38  ? 35.552  72.001  52.450 1.00 32.29 ? 38   PRO B N     1 
ATOM   4362 C CA    . PRO B 1 38  ? 34.972  73.351  52.504 1.00 32.41 ? 38   PRO B CA    1 
ATOM   4363 C C     . PRO B 1 38  ? 33.572  73.404  53.144 1.00 29.94 ? 38   PRO B C     1 
ATOM   4364 O O     . PRO B 1 38  ? 33.089  74.481  53.470 1.00 30.90 ? 38   PRO B O     1 
ATOM   4365 C CB    . PRO B 1 38  ? 34.933  73.776  51.020 1.00 36.29 ? 38   PRO B CB    1 
ATOM   4366 C CG    . PRO B 1 38  ? 35.946  72.857  50.317 1.00 36.57 ? 38   PRO B CG    1 
ATOM   4367 C CD    . PRO B 1 38  ? 35.849  71.548  51.075 1.00 37.20 ? 38   PRO B CD    1 
ATOM   4368 N N     . TYR B 1 39  ? 32.898  72.252  53.291 1.00 25.75 ? 39   TYR B N     1 
ATOM   4369 C CA    . TYR B 1 39  ? 31.497  72.206  53.776 1.00 24.58 ? 39   TYR B CA    1 
ATOM   4370 C C     . TYR B 1 39  ? 31.483  71.926  55.273 1.00 26.86 ? 39   TYR B C     1 
ATOM   4371 O O     . TYR B 1 39  ? 30.401  72.018  55.909 1.00 25.55 ? 39   TYR B O     1 
ATOM   4372 C CB    . TYR B 1 39  ? 30.688  71.207  52.954 1.00 24.72 ? 39   TYR B CB    1 
ATOM   4373 C CG    . TYR B 1 39  ? 30.593  71.671  51.529 1.00 24.07 ? 39   TYR B CG    1 
ATOM   4374 C CD1   . TYR B 1 39  ? 29.678  72.632  51.148 1.00 26.90 ? 39   TYR B CD1   1 
ATOM   4375 C CD2   . TYR B 1 39  ? 31.492  71.223  50.576 1.00 26.38 ? 39   TYR B CD2   1 
ATOM   4376 C CE1   . TYR B 1 39  ? 29.628  73.120  49.849 1.00 24.73 ? 39   TYR B CE1   1 
ATOM   4377 C CE2   . TYR B 1 39  ? 31.423  71.655  49.263 1.00 28.65 ? 39   TYR B CE2   1 
ATOM   4378 C CZ    . TYR B 1 39  ? 30.477  72.598  48.895 1.00 26.77 ? 39   TYR B CZ    1 
ATOM   4379 O OH    . TYR B 1 39  ? 30.404  73.045  47.617 1.00 28.75 ? 39   TYR B OH    1 
ATOM   4380 N N     . GLU B 1 40  ? 32.648  71.620  55.842 1.00 25.60 ? 40   GLU B N     1 
ATOM   4381 C CA    . GLU B 1 40  ? 32.757  71.428  57.307 1.00 23.72 ? 40   GLU B CA    1 
ATOM   4382 C C     . GLU B 1 40  ? 32.636  72.830  57.922 1.00 23.58 ? 40   GLU B C     1 
ATOM   4383 O O     . GLU B 1 40  ? 33.042  73.828  57.279 1.00 23.90 ? 40   GLU B O     1 
ATOM   4384 C CB    . GLU B 1 40  ? 34.094  70.810  57.732 1.00 24.35 ? 40   GLU B CB    1 
ATOM   4385 C CG    . GLU B 1 40  ? 34.399  69.459  57.097 1.00 26.32 ? 40   GLU B CG    1 
ATOM   4386 C CD    . GLU B 1 40  ? 33.656  68.257  57.656 1.00 29.99 ? 40   GLU B CD    1 
ATOM   4387 O OE1   . GLU B 1 40  ? 32.920  68.415  58.671 1.00 27.89 ? 40   GLU B OE1   1 
ATOM   4388 O OE2   . GLU B 1 40  ? 33.808  67.143  57.074 1.00 31.94 ? 40   GLU B OE2   1 
ATOM   4389 N N     . ASP B 1 41  ? 32.091  72.923  59.122 1.00 24.28 ? 41   ASP B N     1 
ATOM   4390 C CA    . ASP B 1 41  ? 32.092  74.188  59.882 1.00 22.43 ? 41   ASP B CA    1 
ATOM   4391 C C     . ASP B 1 41  ? 33.544  74.606  60.066 1.00 24.98 ? 41   ASP B C     1 
ATOM   4392 O O     . ASP B 1 41  ? 34.308  73.861  60.668 1.00 24.40 ? 41   ASP B O     1 
ATOM   4393 C CB    . ASP B 1 41  ? 31.414  73.983  61.240 1.00 25.43 ? 41   ASP B CB    1 
ATOM   4394 C CG    . ASP B 1 41  ? 31.266  75.245  62.082 1.00 24.81 ? 41   ASP B CG    1 
ATOM   4395 O OD1   . ASP B 1 41  ? 31.783  76.316  61.653 1.00 24.16 ? 41   ASP B OD1   1 
ATOM   4396 O OD2   . ASP B 1 41  ? 30.689  75.132  63.195 1.00 25.53 ? 41   ASP B OD2   1 
ATOM   4397 N N     . PRO B 1 42  ? 33.981  75.801  59.610 1.00 25.89 ? 42   PRO B N     1 
ATOM   4398 C CA    . PRO B 1 42  ? 35.370  76.211  59.835 1.00 29.01 ? 42   PRO B CA    1 
ATOM   4399 C C     . PRO B 1 42  ? 35.693  76.465  61.309 1.00 28.31 ? 42   PRO B C     1 
ATOM   4400 O O     . PRO B 1 42  ? 36.839  76.356  61.670 1.00 25.91 ? 42   PRO B O     1 
ATOM   4401 C CB    . PRO B 1 42  ? 35.526  77.520  59.056 1.00 27.73 ? 42   PRO B CB    1 
ATOM   4402 C CG    . PRO B 1 42  ? 34.094  78.024  58.879 1.00 28.36 ? 42   PRO B CG    1 
ATOM   4403 C CD    . PRO B 1 42  ? 33.190  76.803  58.871 1.00 27.21 ? 42   PRO B CD    1 
ATOM   4404 N N     . TYR B 1 43  ? 34.681  76.836  62.114 1.00 25.12 ? 43   TYR B N     1 
ATOM   4405 C CA    . TYR B 1 43  ? 34.863  77.219  63.533 1.00 25.67 ? 43   TYR B CA    1 
ATOM   4406 C C     . TYR B 1 43  ? 34.200  76.147  64.400 1.00 26.29 ? 43   TYR B C     1 
ATOM   4407 O O     . TYR B 1 43  ? 33.149  76.378  65.045 1.00 27.38 ? 43   TYR B O     1 
ATOM   4408 C CB    . TYR B 1 43  ? 34.371  78.645  63.754 1.00 24.41 ? 43   TYR B CB    1 
ATOM   4409 C CG    . TYR B 1 43  ? 34.984  79.672  62.820 1.00 23.67 ? 43   TYR B CG    1 
ATOM   4410 C CD1   . TYR B 1 43  ? 36.269  79.553  62.289 1.00 26.05 ? 43   TYR B CD1   1 
ATOM   4411 C CD2   . TYR B 1 43  ? 34.248  80.792  62.456 1.00 26.57 ? 43   TYR B CD2   1 
ATOM   4412 C CE1   . TYR B 1 43  ? 36.794  80.518  61.423 1.00 26.87 ? 43   TYR B CE1   1 
ATOM   4413 C CE2   . TYR B 1 43  ? 34.756  81.765  61.601 1.00 25.41 ? 43   TYR B CE2   1 
ATOM   4414 C CZ    . TYR B 1 43  ? 36.025  81.624  61.078 1.00 27.11 ? 43   TYR B CZ    1 
ATOM   4415 O OH    . TYR B 1 43  ? 36.458  82.623  60.259 1.00 31.59 ? 43   TYR B OH    1 
ATOM   4416 N N     . THR B 1 44  ? 34.862  74.996  64.454 1.00 25.05 ? 44   THR B N     1 
ATOM   4417 C CA    . THR B 1 44  ? 34.459  73.815  65.242 1.00 24.43 ? 44   THR B CA    1 
ATOM   4418 C C     . THR B 1 44  ? 34.101  74.215  66.677 1.00 26.80 ? 44   THR B C     1 
ATOM   4419 O O     . THR B 1 44  ? 34.815  75.066  67.275 1.00 27.13 ? 44   THR B O     1 
ATOM   4420 C CB    . THR B 1 44  ? 35.601  72.790  65.248 1.00 26.76 ? 44   THR B CB    1 
ATOM   4421 O OG1   . THR B 1 44  ? 36.098  72.674  63.905 1.00 26.12 ? 44   THR B OG1   1 
ATOM   4422 C CG2   . THR B 1 44  ? 35.116  71.452  65.753 1.00 27.66 ? 44   THR B CG2   1 
ATOM   4423 N N     . ILE B 1 45  ? 33.056  73.595  67.213 1.00 27.10 ? 45   ILE B N     1 
ATOM   4424 C CA    . ILE B 1 45  ? 32.701  73.699  68.655 1.00 27.30 ? 45   ILE B CA    1 
ATOM   4425 C C     . ILE B 1 45  ? 32.698  72.310  69.304 1.00 29.55 ? 45   ILE B C     1 
ATOM   4426 O O     . ILE B 1 45  ? 33.284  72.146  70.380 1.00 27.49 ? 45   ILE B O     1 
ATOM   4427 C CB    . ILE B 1 45  ? 31.356  74.432  68.818 1.00 25.24 ? 45   ILE B CB    1 
ATOM   4428 C CG1   . ILE B 1 45  ? 31.393  75.824  68.163 1.00 26.33 ? 45   ILE B CG1   1 
ATOM   4429 C CG2   . ILE B 1 45  ? 31.010  74.511  70.292 1.00 25.86 ? 45   ILE B CG2   1 
ATOM   4430 C CD1   . ILE B 1 45  ? 30.075  76.639  68.289 1.00 26.45 ? 45   ILE B CD1   1 
ATOM   4431 N N     . SER B 1 46  ? 31.978  71.352  68.734 1.00 27.22 ? 46   SER B N     1 
ATOM   4432 C CA    . SER B 1 46  ? 31.880  69.986  69.290 1.00 32.87 ? 46   SER B CA    1 
ATOM   4433 C C     . SER B 1 46  ? 33.282  69.357  69.379 1.00 32.35 ? 46   SER B C     1 
ATOM   4434 O O     . SER B 1 46  ? 34.068  69.537  68.411 1.00 30.73 ? 46   SER B O     1 
ATOM   4435 C CB    . SER B 1 46  ? 30.975  69.150  68.430 1.00 34.97 ? 46   SER B CB    1 
ATOM   4436 O OG    . SER B 1 46  ? 30.761  67.892  69.040 1.00 33.93 ? 46   SER B OG    1 
ATOM   4437 N N     . ASN B 1 47  ? 33.535  68.545  70.411 1.00 31.03 ? 47   ASN B N     1 
ATOM   4438 C CA    . ASN B 1 47  ? 34.717  67.635  70.469 1.00 33.42 ? 47   ASN B CA    1 
ATOM   4439 C C     . ASN B 1 47  ? 34.331  66.234  69.991 1.00 36.66 ? 47   ASN B C     1 
ATOM   4440 O O     . ASN B 1 47  ? 35.190  65.342  70.032 1.00 36.62 ? 47   ASN B O     1 
ATOM   4441 C CB    . ASN B 1 47  ? 35.337  67.593  71.881 1.00 33.68 ? 47   ASN B CB    1 
ATOM   4442 C CG    . ASN B 1 47  ? 36.083  68.874  72.151 1.00 35.31 ? 47   ASN B CG    1 
ATOM   4443 O OD1   . ASN B 1 47  ? 36.629  69.492  71.211 1.00 33.57 ? 47   ASN B OD1   1 
ATOM   4444 N ND2   . ASN B 1 47  ? 36.092  69.297  73.401 1.00 33.54 ? 47   ASN B ND2   1 
ATOM   4445 N N     . ASP B 1 48  ? 33.082  66.059  69.566 1.00 35.68 ? 48   ASP B N     1 
ATOM   4446 C CA    . ASP B 1 48  ? 32.552  64.810  68.998 1.00 33.97 ? 48   ASP B CA    1 
ATOM   4447 C C     . ASP B 1 48  ? 32.588  64.935  67.473 1.00 37.72 ? 48   ASP B C     1 
ATOM   4448 O O     . ASP B 1 48  ? 31.660  65.568  66.876 1.00 31.14 ? 48   ASP B O     1 
ATOM   4449 C CB    . ASP B 1 48  ? 31.168  64.535  69.565 1.00 37.27 ? 48   ASP B CB    1 
ATOM   4450 C CG    . ASP B 1 48  ? 30.571  63.218  69.121 1.00 33.17 ? 48   ASP B CG    1 
ATOM   4451 O OD1   . ASP B 1 48  ? 31.038  62.670  68.126 1.00 35.16 ? 48   ASP B OD1   1 
ATOM   4452 O OD2   . ASP B 1 48  ? 29.598  62.795  69.748 1.00 38.54 ? 48   ASP B OD2   1 
ATOM   4453 N N     . GLU B 1 49  ? 33.548  64.245  66.875 1.00 34.19 ? 49   GLU B N     1 
ATOM   4454 C CA    . GLU B 1 49  ? 33.797  64.227  65.411 1.00 39.35 ? 49   GLU B CA    1 
ATOM   4455 C C     . GLU B 1 49  ? 32.649  63.580  64.620 1.00 31.68 ? 49   GLU B C     1 
ATOM   4456 O O     . GLU B 1 49  ? 32.695  63.675  63.395 1.00 35.59 ? 49   GLU B O     1 
ATOM   4457 C CB    . GLU B 1 49  ? 35.131  63.524  65.165 1.00 44.92 ? 49   GLU B CB    1 
ATOM   4458 C CG    . GLU B 1 49  ? 36.288  64.390  65.601 1.00 58.21 ? 49   GLU B CG    1 
ATOM   4459 C CD    . GLU B 1 49  ? 37.638  63.969  65.038 1.00 74.62 ? 49   GLU B CD    1 
ATOM   4460 O OE1   . GLU B 1 49  ? 37.695  62.895  64.372 1.00 72.54 ? 49   GLU B OE1   1 
ATOM   4461 O OE2   . GLU B 1 49  ? 38.632  64.722  65.266 1.00 85.12 ? 49   GLU B OE2   1 
ATOM   4462 N N     . THR B 1 50  ? 31.641  62.973  65.249 1.00 30.44 ? 50   THR B N     1 
ATOM   4463 C CA    . THR B 1 50  ? 30.471  62.443  64.515 1.00 31.37 ? 50   THR B CA    1 
ATOM   4464 C C     . THR B 1 50  ? 29.395  63.542  64.302 1.00 31.28 ? 50   THR B C     1 
ATOM   4465 O O     . THR B 1 50  ? 28.391  63.214  63.671 1.00 30.53 ? 50   THR B O     1 
ATOM   4466 C CB    . THR B 1 50  ? 29.850  61.218  65.209 1.00 33.47 ? 50   THR B CB    1 
ATOM   4467 O OG1   . THR B 1 50  ? 29.302  61.622  66.463 1.00 31.75 ? 50   THR B OG1   1 
ATOM   4468 C CG2   . THR B 1 50  ? 30.828  60.064  65.398 1.00 35.61 ? 50   THR B CG2   1 
ATOM   4469 N N     . GLU B 1 51  ? 29.540  64.749  64.855 1.00 28.95 ? 51   GLU B N     1 
ATOM   4470 C CA    . GLU B 1 51  ? 28.469  65.780  64.859 1.00 28.61 ? 51   GLU B CA    1 
ATOM   4471 C C     . GLU B 1 51  ? 28.675  66.834  63.762 1.00 25.47 ? 51   GLU B C     1 
ATOM   4472 O O     . GLU B 1 51  ? 29.825  67.306  63.568 1.00 25.13 ? 51   GLU B O     1 
ATOM   4473 C CB    . GLU B 1 51  ? 28.403  66.450  66.221 1.00 32.09 ? 51   GLU B CB    1 
ATOM   4474 C CG    . GLU B 1 51  ? 27.872  65.500  67.266 1.00 34.06 ? 51   GLU B CG    1 
ATOM   4475 C CD    . GLU B 1 51  ? 27.647  66.132  68.626 1.00 38.96 ? 51   GLU B CD    1 
ATOM   4476 O OE1   . GLU B 1 51  ? 28.468  66.982  69.060 1.00 35.09 ? 51   GLU B OE1   1 
ATOM   4477 O OE2   . GLU B 1 51  ? 26.676  65.733  69.265 1.00 39.03 ? 51   GLU B OE2   1 
ATOM   4478 N N     . HIS B 1 52  ? 27.570  67.250  63.115 1.00 23.98 ? 52   HIS B N     1 
ATOM   4479 C CA    . HIS B 1 52  ? 27.519  68.368  62.134 1.00 23.97 ? 52   HIS B CA    1 
ATOM   4480 C C     . HIS B 1 52  ? 28.379  68.038  60.920 1.00 24.15 ? 52   HIS B C     1 
ATOM   4481 O O     . HIS B 1 52  ? 28.985  68.971  60.312 1.00 24.70 ? 52   HIS B O     1 
ATOM   4482 C CB    . HIS B 1 52  ? 27.928  69.695  62.798 1.00 25.79 ? 52   HIS B CB    1 
ATOM   4483 C CG    . HIS B 1 52  ? 27.278  69.906  64.130 1.00 28.58 ? 52   HIS B CG    1 
ATOM   4484 N ND1   . HIS B 1 52  ? 25.922  69.842  64.289 1.00 34.49 ? 52   HIS B ND1   1 
ATOM   4485 C CD2   . HIS B 1 52  ? 27.797  70.178  65.352 1.00 31.72 ? 52   HIS B CD2   1 
ATOM   4486 C CE1   . HIS B 1 52  ? 25.635  70.032  65.569 1.00 34.30 ? 52   HIS B CE1   1 
ATOM   4487 N NE2   . HIS B 1 52  ? 26.770  70.236  66.251 1.00 32.46 ? 52   HIS B NE2   1 
ATOM   4488 N N     . ARG B 1 53  ? 28.444  66.756  60.551 1.00 22.95 ? 53   ARG B N     1 
ATOM   4489 C CA    . ARG B 1 53  ? 29.305  66.289  59.446 1.00 23.52 ? 53   ARG B CA    1 
ATOM   4490 C C     . ARG B 1 53  ? 28.470  66.105  58.178 1.00 24.55 ? 53   ARG B C     1 
ATOM   4491 O O     . ARG B 1 53  ? 27.694  65.165  58.081 1.00 25.31 ? 53   ARG B O     1 
ATOM   4492 C CB    . ARG B 1 53  ? 30.002  64.982  59.843 1.00 24.17 ? 53   ARG B CB    1 
ATOM   4493 C CG    . ARG B 1 53  ? 30.758  65.050  61.159 1.00 22.79 ? 53   ARG B CG    1 
ATOM   4494 C CD    . ARG B 1 53  ? 31.874  66.072  61.209 1.00 25.22 ? 53   ARG B CD    1 
ATOM   4495 N NE    . ARG B 1 53  ? 32.767  65.936  60.079 1.00 26.63 ? 53   ARG B NE    1 
ATOM   4496 C CZ    . ARG B 1 53  ? 33.700  64.979  59.964 1.00 32.34 ? 53   ARG B CZ    1 
ATOM   4497 N NH1   . ARG B 1 53  ? 33.858  64.053  60.902 1.00 32.56 ? 53   ARG B NH1   1 
ATOM   4498 N NH2   . ARG B 1 53  ? 34.439  64.920  58.885 1.00 31.48 ? 53   ARG B NH2   1 
ATOM   4499 N N     . PRO B 1 54  ? 28.704  66.907  57.120 1.00 21.45 ? 54   PRO B N     1 
ATOM   4500 C CA    . PRO B 1 54  ? 28.019  66.697  55.847 1.00 23.14 ? 54   PRO B CA    1 
ATOM   4501 C C     . PRO B 1 54  ? 28.554  65.425  55.178 1.00 27.01 ? 54   PRO B C     1 
ATOM   4502 O O     . PRO B 1 54  ? 29.768  65.205  55.206 1.00 28.47 ? 54   PRO B O     1 
ATOM   4503 C CB    . PRO B 1 54  ? 28.423  67.861  54.967 1.00 20.77 ? 54   PRO B CB    1 
ATOM   4504 C CG    . PRO B 1 54  ? 29.650  68.425  55.607 1.00 22.53 ? 54   PRO B CG    1 
ATOM   4505 C CD    . PRO B 1 54  ? 29.694  67.971  57.055 1.00 22.77 ? 54   PRO B CD    1 
ATOM   4506 N N     . TYR B 1 55  ? 27.671  64.654  54.569 1.00 23.61 ? 55   TYR B N     1 
ATOM   4507 C CA    . TYR B 1 55  ? 28.068  63.403  53.883 1.00 24.29 ? 55   TYR B CA    1 
ATOM   4508 C C     . TYR B 1 55  ? 28.699  63.718  52.540 1.00 27.68 ? 55   TYR B C     1 
ATOM   4509 O O     . TYR B 1 55  ? 29.617  63.024  52.090 1.00 24.03 ? 55   TYR B O     1 
ATOM   4510 C CB    . TYR B 1 55  ? 26.876  62.493  53.643 1.00 27.48 ? 55   TYR B CB    1 
ATOM   4511 C CG    . TYR B 1 55  ? 27.325  61.097  53.351 1.00 28.07 ? 55   TYR B CG    1 
ATOM   4512 C CD1   . TYR B 1 55  ? 27.659  60.241  54.385 1.00 29.97 ? 55   TYR B CD1   1 
ATOM   4513 C CD2   . TYR B 1 55  ? 27.482  60.670  52.056 1.00 31.50 ? 55   TYR B CD2   1 
ATOM   4514 C CE1   . TYR B 1 55  ? 28.117  58.962  54.127 1.00 32.23 ? 55   TYR B CE1   1 
ATOM   4515 C CE2   . TYR B 1 55  ? 27.941  59.395  51.781 1.00 31.62 ? 55   TYR B CE2   1 
ATOM   4516 C CZ    . TYR B 1 55  ? 28.268  58.550  52.821 1.00 34.14 ? 55   TYR B CZ    1 
ATOM   4517 O OH    . TYR B 1 55  ? 28.699  57.288  52.556 1.00 39.42 ? 55   TYR B OH    1 
ATOM   4518 N N     . ALA B 1 56  ? 28.204  64.773  51.904 1.00 25.19 ? 56   ALA B N     1 
ATOM   4519 C CA    . ALA B 1 56  ? 28.600  65.149  50.541 1.00 23.29 ? 56   ALA B CA    1 
ATOM   4520 C C     . ALA B 1 56  ? 27.994  66.518  50.270 1.00 23.58 ? 56   ALA B C     1 
ATOM   4521 O O     . ALA B 1 56  ? 27.192  66.996  51.100 1.00 20.91 ? 56   ALA B O     1 
ATOM   4522 C CB    . ALA B 1 56  ? 28.058  64.104  49.580 1.00 25.09 ? 56   ALA B CB    1 
ATOM   4523 N N     . ALA B 1 57  ? 28.293  67.073  49.104 1.00 22.01 ? 57   ALA B N     1 
ATOM   4524 C CA    . ALA B 1 57  ? 27.693  68.320  48.629 1.00 20.94 ? 57   ALA B CA    1 
ATOM   4525 C C     . ALA B 1 57  ? 27.403  68.181  47.147 1.00 24.92 ? 57   ALA B C     1 
ATOM   4526 O O     . ALA B 1 57  ? 28.163  67.475  46.427 1.00 24.83 ? 57   ALA B O     1 
ATOM   4527 C CB    . ALA B 1 57  ? 28.602  69.502  48.892 1.00 22.05 ? 57   ALA B CB    1 
ATOM   4528 N N     . VAL B 1 58  ? 26.385  68.901  46.702 1.00 20.81 ? 58   VAL B N     1 
ATOM   4529 C CA    . VAL B 1 58  ? 25.968  68.921  45.280 1.00 21.26 ? 58   VAL B CA    1 
ATOM   4530 C C     . VAL B 1 58  ? 25.774  70.397  44.929 1.00 24.43 ? 58   VAL B C     1 
ATOM   4531 O O     . VAL B 1 58  ? 25.172  71.138  45.750 1.00 21.31 ? 58   VAL B O     1 
ATOM   4532 C CB    . VAL B 1 58  ? 24.758  68.030  44.993 1.00 23.29 ? 58   VAL B CB    1 
ATOM   4533 C CG1   . VAL B 1 58  ? 23.505  68.347  45.777 1.00 26.94 ? 58   VAL B CG1   1 
ATOM   4534 C CG2   . VAL B 1 58  ? 24.385  68.076  43.521 1.00 24.79 ? 58   VAL B CG2   1 
ATOM   4535 N N     . ALA B 1 59  ? 26.307  70.814  43.785 1.00 22.45 ? 59   ALA B N     1 
ATOM   4536 C CA    . ALA B 1 59  ? 26.365  72.228  43.358 1.00 22.59 ? 59   ALA B CA    1 
ATOM   4537 C C     . ALA B 1 59  ? 25.625  72.439  42.044 1.00 23.85 ? 59   ALA B C     1 
ATOM   4538 O O     . ALA B 1 59  ? 26.261  72.479  40.976 1.00 24.52 ? 59   ALA B O     1 
ATOM   4539 C CB    . ALA B 1 59  ? 27.803  72.680  43.325 1.00 22.46 ? 59   ALA B CB    1 
ATOM   4540 N N     . PRO B 1 60  ? 24.274  72.619  42.098 1.00 21.89 ? 60   PRO B N     1 
ATOM   4541 C CA    . PRO B 1 60  ? 23.478  72.850  40.897 1.00 22.57 ? 60   PRO B CA    1 
ATOM   4542 C C     . PRO B 1 60  ? 23.721  74.222  40.260 1.00 22.26 ? 60   PRO B C     1 
ATOM   4543 O O     . PRO B 1 60  ? 24.205  75.181  40.951 1.00 24.64 ? 60   PRO B O     1 
ATOM   4544 C CB    . PRO B 1 60  ? 22.015  72.710  41.372 1.00 22.12 ? 60   PRO B CB    1 
ATOM   4545 C CG    . PRO B 1 60  ? 22.098  73.132  42.841 1.00 22.65 ? 60   PRO B CG    1 
ATOM   4546 C CD    . PRO B 1 60  ? 23.429  72.587  43.308 1.00 21.47 ? 60   PRO B CD    1 
ATOM   4547 N N     . ALA B 1 61  ? 23.330  74.354  38.974 1.00 24.81 ? 61   ALA B N     1 
ATOM   4548 C CA    . ALA B 1 61  ? 23.506  75.628  38.241 1.00 25.50 ? 61   ALA B CA    1 
ATOM   4549 C C     . ALA B 1 61  ? 22.165  76.144  37.727 1.00 26.43 ? 61   ALA B C     1 
ATOM   4550 O O     . ALA B 1 61  ? 22.182  77.121  37.037 1.00 23.92 ? 61   ALA B O     1 
ATOM   4551 C CB    . ALA B 1 61  ? 24.538  75.459  37.137 1.00 30.94 ? 61   ALA B CB    1 
ATOM   4552 N N     . SER B 1 62  ? 21.037  75.529  38.040 1.00 20.44 ? 62   SER B N     1 
ATOM   4553 C CA    . SER B 1 62  ? 19.722  76.065  37.632 1.00 21.56 ? 62   SER B CA    1 
ATOM   4554 C C     . SER B 1 62  ? 18.647  75.636  38.610 1.00 19.89 ? 62   SER B C     1 
ATOM   4555 O O     . SER B 1 62  ? 18.833  74.623  39.299 1.00 19.79 ? 62   SER B O     1 
ATOM   4556 C CB    . SER B 1 62  ? 19.338  75.582  36.246 1.00 22.32 ? 62   SER B CB    1 
ATOM   4557 O OG    . SER B 1 62  ? 19.160  74.179  36.288 1.00 20.30 ? 62   SER B OG    1 
ATOM   4558 N N     . THR B 1 63  ? 17.508  76.322  38.566 1.00 22.95 ? 63   THR B N     1 
ATOM   4559 C CA    . THR B 1 63  ? 16.309  75.959  39.349 1.00 21.30 ? 63   THR B CA    1 
ATOM   4560 C C     . THR B 1 63  ? 15.900  74.552  38.960 1.00 22.48 ? 63   THR B C     1 
ATOM   4561 O O     . THR B 1 63  ? 15.590  73.765  39.826 1.00 19.84 ? 63   THR B O     1 
ATOM   4562 C CB    . THR B 1 63  ? 15.180  76.985  39.129 1.00 21.45 ? 63   THR B CB    1 
ATOM   4563 O OG1   . THR B 1 63  ? 15.627  78.212  39.699 1.00 23.16 ? 63   THR B OG1   1 
ATOM   4564 C CG2   . THR B 1 63  ? 13.899  76.564  39.781 1.00 21.83 ? 63   THR B CG2   1 
ATOM   4565 N N     . GLU B 1 64  ? 15.851  74.241  37.657 1.00 22.47 ? 64   GLU B N     1 
ATOM   4566 C CA    . GLU B 1 64  ? 15.501  72.873  37.225 1.00 21.01 ? 64   GLU B CA    1 
ATOM   4567 C C     . GLU B 1 64  ? 16.415  71.863  37.954 1.00 19.43 ? 64   GLU B C     1 
ATOM   4568 O O     . GLU B 1 64  ? 15.921  70.815  38.406 1.00 21.47 ? 64   GLU B O     1 
ATOM   4569 C CB    . GLU B 1 64  ? 15.717  72.695  35.699 1.00 23.85 ? 64   GLU B CB    1 
ATOM   4570 C CG    . GLU B 1 64  ? 15.395  71.260  35.299 1.00 26.96 ? 64   GLU B CG    1 
ATOM   4571 C CD    . GLU B 1 64  ? 15.603  70.910  33.839 1.00 33.21 ? 64   GLU B CD    1 
ATOM   4572 O OE1   . GLU B 1 64  ? 16.107  71.758  33.136 1.00 25.07 ? 64   GLU B OE1   1 
ATOM   4573 O OE2   . GLU B 1 64  ? 15.238  69.769  33.452 1.00 33.05 ? 64   GLU B OE2   1 
ATOM   4574 N N     . GLU B 1 65  ? 17.715  72.117  38.038 1.00 18.13 ? 65   GLU B N     1 
ATOM   4575 C CA    . GLU B 1 65  ? 18.639  71.141  38.700 1.00 19.65 ? 65   GLU B CA    1 
ATOM   4576 C C     . GLU B 1 65  ? 18.266  71.030  40.189 1.00 20.97 ? 65   GLU B C     1 
ATOM   4577 O O     . GLU B 1 65  ? 18.294  69.918  40.759 1.00 19.67 ? 65   GLU B O     1 
ATOM   4578 C CB    . GLU B 1 65  ? 20.093  71.521  38.502 1.00 21.26 ? 65   GLU B CB    1 
ATOM   4579 C CG    . GLU B 1 65  ? 20.590  71.225  37.078 1.00 23.88 ? 65   GLU B CG    1 
ATOM   4580 C CD    . GLU B 1 65  ? 21.995  71.708  36.739 1.00 27.82 ? 65   GLU B CD    1 
ATOM   4581 O OE1   . GLU B 1 65  ? 22.836  71.886  37.639 1.00 26.31 ? 65   GLU B OE1   1 
ATOM   4582 O OE2   . GLU B 1 65  ? 22.270  71.834  35.524 1.00 34.75 ? 65   GLU B OE2   1 
ATOM   4583 N N     . VAL B 1 66  ? 17.904  72.147  40.826 1.00 20.09 ? 66   VAL B N     1 
ATOM   4584 C CA    . VAL B 1 66  ? 17.479  72.092  42.261 1.00 17.83 ? 66   VAL B CA    1 
ATOM   4585 C C     . VAL B 1 66  ? 16.223  71.204  42.354 1.00 19.00 ? 66   VAL B C     1 
ATOM   4586 O O     . VAL B 1 66  ? 16.129  70.350  43.259 1.00 17.86 ? 66   VAL B O     1 
ATOM   4587 C CB    . VAL B 1 66  ? 17.236  73.516  42.791 1.00 18.20 ? 66   VAL B CB    1 
ATOM   4588 C CG1   . VAL B 1 66  ? 16.589  73.482  44.163 1.00 18.33 ? 66   VAL B CG1   1 
ATOM   4589 C CG2   . VAL B 1 66  ? 18.510  74.339  42.770 1.00 19.59 ? 66   VAL B CG2   1 
ATOM   4590 N N     . GLN B 1 67  ? 15.240  71.400  41.484 1.00 17.75 ? 67   GLN B N     1 
ATOM   4591 C CA    . GLN B 1 67  ? 13.985  70.613  41.510 1.00 19.98 ? 67   GLN B CA    1 
ATOM   4592 C C     . GLN B 1 67  ? 14.329  69.120  41.435 1.00 22.34 ? 67   GLN B C     1 
ATOM   4593 O O     . GLN B 1 67  ? 13.752  68.323  42.199 1.00 20.63 ? 67   GLN B O     1 
ATOM   4594 C CB    . GLN B 1 67  ? 13.043  70.995  40.369 1.00 21.58 ? 67   GLN B CB    1 
ATOM   4595 C CG    . GLN B 1 67  ? 12.437  72.376  40.504 1.00 21.04 ? 67   GLN B CG    1 
ATOM   4596 C CD    . GLN B 1 67  ? 11.501  72.679  39.373 1.00 23.26 ? 67   GLN B CD    1 
ATOM   4597 O OE1   . GLN B 1 67  ? 10.297  72.331  39.386 1.00 24.24 ? 67   GLN B OE1   1 
ATOM   4598 N NE2   . GLN B 1 67  ? 12.069  73.321  38.378 1.00 18.76 ? 67   GLN B NE2   1 
ATOM   4599 N N     . GLU B 1 68  ? 15.203  68.762  40.495 1.00 23.77 ? 68   GLU B N     1 
ATOM   4600 C CA    . GLU B 1 68  ? 15.540  67.339  40.229 1.00 22.56 ? 68   GLU B CA    1 
ATOM   4601 C C     . GLU B 1 68  ? 16.259  66.762  41.455 1.00 21.70 ? 68   GLU B C     1 
ATOM   4602 O O     . GLU B 1 68  ? 15.975  65.602  41.850 1.00 21.82 ? 68   GLU B O     1 
ATOM   4603 C CB    . GLU B 1 68  ? 16.350  67.240  38.925 1.00 25.11 ? 68   GLU B CB    1 
ATOM   4604 C CG    . GLU B 1 68  ? 15.496  67.624  37.734 1.00 26.57 ? 68   GLU B CG    1 
ATOM   4605 C CD    . GLU B 1 68  ? 14.506  66.571  37.254 1.00 36.89 ? 68   GLU B CD    1 
ATOM   4606 O OE1   . GLU B 1 68  ? 13.614  66.122  37.993 1.00 35.66 ? 68   GLU B OE1   1 
ATOM   4607 O OE2   . GLU B 1 68  ? 14.592  66.246  36.084 1.00 55.76 ? 68   GLU B OE2   1 
ATOM   4608 N N     . ILE B 1 69  ? 17.164  67.529  42.051 1.00 20.02 ? 69   ILE B N     1 
ATOM   4609 C CA    . ILE B 1 69  ? 17.847  67.111  43.298 1.00 20.58 ? 69   ILE B CA    1 
ATOM   4610 C C     . ILE B 1 69  ? 16.818  66.868  44.391 1.00 20.05 ? 69   ILE B C     1 
ATOM   4611 O O     . ILE B 1 69  ? 16.932  65.829  45.094 1.00 21.74 ? 69   ILE B O     1 
ATOM   4612 C CB    . ILE B 1 69  ? 18.916  68.137  43.689 1.00 21.23 ? 69   ILE B CB    1 
ATOM   4613 C CG1   . ILE B 1 69  ? 20.073  68.084  42.689 1.00 20.53 ? 69   ILE B CG1   1 
ATOM   4614 C CG2   . ILE B 1 69  ? 19.349  67.889  45.113 1.00 21.46 ? 69   ILE B CG2   1 
ATOM   4615 C CD1   . ILE B 1 69  ? 20.985  69.251  42.730 1.00 20.83 ? 69   ILE B CD1   1 
ATOM   4616 N N     . VAL B 1 70  ? 15.844  67.771  44.546 1.00 17.68 ? 70   VAL B N     1 
ATOM   4617 C CA    . VAL B 1 70  ? 14.835  67.621  45.612 1.00 18.82 ? 70   VAL B CA    1 
ATOM   4618 C C     . VAL B 1 70  ? 13.980  66.372  45.332 1.00 20.36 ? 70   VAL B C     1 
ATOM   4619 O O     . VAL B 1 70  ? 13.659  65.583  46.268 1.00 18.76 ? 70   VAL B O     1 
ATOM   4620 C CB    . VAL B 1 70  ? 14.016  68.921  45.720 1.00 21.06 ? 70   VAL B CB    1 
ATOM   4621 C CG1   . VAL B 1 70  ? 12.773  68.721  46.563 1.00 21.30 ? 70   VAL B CG1   1 
ATOM   4622 C CG2   . VAL B 1 70  ? 14.883  70.055  46.283 1.00 20.79 ? 70   VAL B CG2   1 
ATOM   4623 N N     . ARG B 1 71  ? 13.604  66.143  44.078 1.00 22.30 ? 71   ARG B N     1 
ATOM   4624 C CA    . ARG B 1 71  ? 12.803  64.931  43.723 1.00 21.93 ? 71   ARG B CA    1 
ATOM   4625 C C     . ARG B 1 71  ? 13.584  63.650  44.074 1.00 21.53 ? 71   ARG B C     1 
ATOM   4626 O O     . ARG B 1 71  ? 12.973  62.718  44.646 1.00 23.53 ? 71   ARG B O     1 
ATOM   4627 C CB    . ARG B 1 71  ? 12.424  64.997  42.248 1.00 24.48 ? 71   ARG B CB    1 
ATOM   4628 C CG    . ARG B 1 71  ? 11.317  66.004  41.972 1.00 25.23 ? 71   ARG B CG    1 
ATOM   4629 C CD    . ARG B 1 71  ? 11.271  66.333  40.476 1.00 26.51 ? 71   ARG B CD    1 
ATOM   4630 N NE    . ARG B 1 71  ? 10.327  67.400  40.220 1.00 25.63 ? 71   ARG B NE    1 
ATOM   4631 C CZ    . ARG B 1 71  ? 10.321  68.183  39.140 1.00 28.07 ? 71   ARG B CZ    1 
ATOM   4632 N NH1   . ARG B 1 71  ? 11.224  68.069  38.192 1.00 27.98 ? 71   ARG B NH1   1 
ATOM   4633 N NH2   . ARG B 1 71  ? 9.376   69.081  39.003 1.00 29.17 ? 71   ARG B NH2   1 
ATOM   4634 N N     . VAL B 1 72  ? 14.868  63.608  43.763 1.00 21.99 ? 72   VAL B N     1 
ATOM   4635 C CA    . VAL B 1 72  ? 15.754  62.438  44.043 1.00 23.47 ? 72   VAL B CA    1 
ATOM   4636 C C     . VAL B 1 72  ? 15.856  62.251  45.557 1.00 24.33 ? 72   VAL B C     1 
ATOM   4637 O O     . VAL B 1 72  ? 15.693  61.100  46.053 1.00 25.80 ? 72   VAL B O     1 
ATOM   4638 C CB    . VAL B 1 72  ? 17.124  62.594  43.377 1.00 24.27 ? 72   VAL B CB    1 
ATOM   4639 C CG1   . VAL B 1 72  ? 18.127  61.609  43.971 1.00 26.14 ? 72   VAL B CG1   1 
ATOM   4640 C CG2   . VAL B 1 72  ? 17.007  62.414  41.854 1.00 25.88 ? 72   VAL B CG2   1 
ATOM   4641 N N     . ALA B 1 73  ? 16.095  63.328  46.296 1.00 25.03 ? 73   ALA B N     1 
ATOM   4642 C CA    . ALA B 1 73  ? 16.124  63.304  47.780 1.00 22.86 ? 73   ALA B CA    1 
ATOM   4643 C C     . ALA B 1 73  ? 14.858  62.629  48.312 1.00 23.42 ? 73   ALA B C     1 
ATOM   4644 O O     . ALA B 1 73  ? 14.975  61.779  49.207 1.00 22.84 ? 73   ALA B O     1 
ATOM   4645 C CB    . ALA B 1 73  ? 16.263  64.691  48.367 1.00 23.24 ? 73   ALA B CB    1 
ATOM   4646 N N     . ASN B 1 74  ? 13.686  63.023  47.842 1.00 21.34 ? 74   ASN B N     1 
ATOM   4647 C CA    . ASN B 1 74  ? 12.417  62.404  48.283 1.00 22.83 ? 74   ASN B CA    1 
ATOM   4648 C C     . ASN B 1 74  ? 12.407  60.896  47.956 1.00 26.46 ? 74   ASN B C     1 
ATOM   4649 O O     . ASN B 1 74  ? 12.022  60.105  48.795 1.00 24.79 ? 74   ASN B O     1 
ATOM   4650 C CB    . ASN B 1 74  ? 11.215  63.043  47.615 1.00 22.83 ? 74   ASN B CB    1 
ATOM   4651 C CG    . ASN B 1 74  ? 10.807  64.303  48.353 1.00 22.48 ? 74   ASN B CG    1 
ATOM   4652 O OD1   . ASN B 1 74  ? 10.230  64.234  49.440 1.00 22.16 ? 74   ASN B OD1   1 
ATOM   4653 N ND2   . ASN B 1 74  ? 11.181  65.422  47.789 1.00 22.71 ? 74   ASN B ND2   1 
ATOM   4654 N N     . GLU B 1 75  ? 12.856  60.533  46.774 1.00 27.71 ? 75   GLU B N     1 
ATOM   4655 C CA    . GLU B 1 75  ? 12.822  59.129  46.303 1.00 31.21 ? 75   GLU B CA    1 
ATOM   4656 C C     . GLU B 1 75  ? 13.692  58.254  47.218 1.00 30.06 ? 75   GLU B C     1 
ATOM   4657 O O     . GLU B 1 75  ? 13.253  57.176  47.541 1.00 27.95 ? 75   GLU B O     1 
ATOM   4658 C CB    . GLU B 1 75  ? 13.267  59.104  44.845 1.00 34.67 ? 75   GLU B CB    1 
ATOM   4659 C CG    . GLU B 1 75  ? 13.086  57.766  44.184 1.00 45.87 ? 75   GLU B CG    1 
ATOM   4660 C CD    . GLU B 1 75  ? 13.620  57.679  42.765 1.00 52.57 ? 75   GLU B CD    1 
ATOM   4661 O OE1   . GLU B 1 75  ? 13.782  56.530  42.319 1.00 72.06 ? 75   GLU B OE1   1 
ATOM   4662 O OE2   . GLU B 1 75  ? 13.939  58.749  42.134 1.00 53.20 ? 75   GLU B OE2   1 
ATOM   4663 N N     . PHE B 1 76  ? 14.858  58.703  47.657 1.00 25.16 ? 76   PHE B N     1 
ATOM   4664 C CA    . PHE B 1 76  ? 15.794  57.876  48.448 1.00 25.87 ? 76   PHE B CA    1 
ATOM   4665 C C     . PHE B 1 76  ? 15.842  58.243  49.927 1.00 29.46 ? 76   PHE B C     1 
ATOM   4666 O O     . PHE B 1 76  ? 16.637  57.624  50.653 1.00 28.70 ? 76   PHE B O     1 
ATOM   4667 C CB    . PHE B 1 76  ? 17.160  57.966  47.803 1.00 27.98 ? 76   PHE B CB    1 
ATOM   4668 C CG    . PHE B 1 76  ? 17.111  57.293  46.469 1.00 32.50 ? 76   PHE B CG    1 
ATOM   4669 C CD1   . PHE B 1 76  ? 17.033  55.902  46.392 1.00 40.89 ? 76   PHE B CD1   1 
ATOM   4670 C CD2   . PHE B 1 76  ? 17.005  58.028  45.315 1.00 30.95 ? 76   PHE B CD2   1 
ATOM   4671 C CE1   . PHE B 1 76  ? 16.936  55.258  45.162 1.00 39.81 ? 76   PHE B CE1   1 
ATOM   4672 C CE2   . PHE B 1 76  ? 16.900  57.382  44.085 1.00 38.29 ? 76   PHE B CE2   1 
ATOM   4673 C CZ    . PHE B 1 76  ? 16.867  56.004  44.012 1.00 37.78 ? 76   PHE B CZ    1 
ATOM   4674 N N     . GLY B 1 77  ? 15.049  59.218  50.377 1.00 25.55 ? 77   GLY B N     1 
ATOM   4675 C CA    . GLY B 1 77  ? 15.031  59.587  51.806 1.00 23.44 ? 77   GLY B CA    1 
ATOM   4676 C C     . GLY B 1 77  ? 16.327  60.261  52.228 1.00 24.31 ? 77   GLY B C     1 
ATOM   4677 O O     . GLY B 1 77  ? 16.673  60.163  53.397 1.00 24.12 ? 77   GLY B O     1 
ATOM   4678 N N     . VAL B 1 78  ? 17.038  60.916  51.311 1.00 23.61 ? 78   VAL B N     1 
ATOM   4679 C CA    . VAL B 1 78  ? 18.358  61.533  51.572 1.00 23.29 ? 78   VAL B CA    1 
ATOM   4680 C C     . VAL B 1 78  ? 18.154  63.020  51.883 1.00 22.23 ? 78   VAL B C     1 
ATOM   4681 O O     . VAL B 1 78  ? 17.752  63.794  51.021 1.00 21.58 ? 78   VAL B O     1 
ATOM   4682 C CB    . VAL B 1 78  ? 19.292  61.305  50.384 1.00 26.35 ? 78   VAL B CB    1 
ATOM   4683 C CG1   . VAL B 1 78  ? 20.543  62.157  50.515 1.00 25.12 ? 78   VAL B CG1   1 
ATOM   4684 C CG2   . VAL B 1 78  ? 19.646  59.827  50.246 1.00 28.37 ? 78   VAL B CG2   1 
ATOM   4685 N N     . PRO B 1 79  ? 18.423  63.473  53.118 1.00 22.00 ? 79   PRO B N     1 
ATOM   4686 C CA    . PRO B 1 79  ? 18.186  64.866  53.497 1.00 21.13 ? 79   PRO B CA    1 
ATOM   4687 C C     . PRO B 1 79  ? 19.253  65.812  52.924 1.00 21.06 ? 79   PRO B C     1 
ATOM   4688 O O     . PRO B 1 79  ? 20.444  65.441  52.741 1.00 21.36 ? 79   PRO B O     1 
ATOM   4689 C CB    . PRO B 1 79  ? 18.234  64.867  55.028 1.00 23.99 ? 79   PRO B CB    1 
ATOM   4690 C CG    . PRO B 1 79  ? 19.133  63.670  55.358 1.00 25.33 ? 79   PRO B CG    1 
ATOM   4691 C CD    . PRO B 1 79  ? 19.014  62.697  54.214 1.00 24.45 ? 79   PRO B CD    1 
ATOM   4692 N N     . LEU B 1 80  ? 18.799  67.014  52.598 1.00 18.43 ? 80   LEU B N     1 
ATOM   4693 C CA    . LEU B 1 80  ? 19.624  68.083  51.997 1.00 18.53 ? 80   LEU B CA    1 
ATOM   4694 C C     . LEU B 1 80  ? 19.806  69.254  52.962 1.00 17.83 ? 80   LEU B C     1 
ATOM   4695 O O     . LEU B 1 80  ? 18.925  69.505  53.767 1.00 20.43 ? 80   LEU B O     1 
ATOM   4696 C CB    . LEU B 1 80  ? 18.894  68.594  50.771 1.00 18.07 ? 80   LEU B CB    1 
ATOM   4697 C CG    . LEU B 1 80  ? 18.617  67.564  49.692 1.00 19.61 ? 80   LEU B CG    1 
ATOM   4698 C CD1   . LEU B 1 80  ? 17.653  68.133  48.684 1.00 20.55 ? 80   LEU B CD1   1 
ATOM   4699 C CD2   . LEU B 1 80  ? 19.922  67.131  49.049 1.00 22.78 ? 80   LEU B CD2   1 
ATOM   4700 N N     . TRP B 1 81  ? 20.891  69.995  52.830 1.00 19.05 ? 81   TRP B N     1 
ATOM   4701 C CA    . TRP B 1 81  ? 21.086  71.240  53.615 1.00 18.57 ? 81   TRP B CA    1 
ATOM   4702 C C     . TRP B 1 81  ? 21.301  72.375  52.627 1.00 20.40 ? 81   TRP B C     1 
ATOM   4703 O O     . TRP B 1 81  ? 22.416  72.539  52.163 1.00 18.36 ? 81   TRP B O     1 
ATOM   4704 C CB    . TRP B 1 81  ? 22.242  71.085  54.594 1.00 19.68 ? 81   TRP B CB    1 
ATOM   4705 C CG    . TRP B 1 81  ? 22.378  72.252  55.518 1.00 20.13 ? 81   TRP B CG    1 
ATOM   4706 C CD1   . TRP B 1 81  ? 23.206  73.322  55.366 1.00 19.40 ? 81   TRP B CD1   1 
ATOM   4707 C CD2   . TRP B 1 81  ? 21.659  72.463  56.741 1.00 20.69 ? 81   TRP B CD2   1 
ATOM   4708 N NE1   . TRP B 1 81  ? 23.009  74.213  56.382 1.00 21.48 ? 81   TRP B NE1   1 
ATOM   4709 C CE2   . TRP B 1 81  ? 22.086  73.713  57.248 1.00 20.92 ? 81   TRP B CE2   1 
ATOM   4710 C CE3   . TRP B 1 81  ? 20.753  71.696  57.486 1.00 20.68 ? 81   TRP B CE3   1 
ATOM   4711 C CZ2   . TRP B 1 81  ? 21.640  74.207  58.471 1.00 21.55 ? 81   TRP B CZ2   1 
ATOM   4712 C CZ3   . TRP B 1 81  ? 20.291  72.200  58.682 1.00 22.21 ? 81   TRP B CZ3   1 
ATOM   4713 C CH2   . TRP B 1 81  ? 20.706  73.452  59.142 1.00 19.98 ? 81   TRP B CH2   1 
ATOM   4714 N N     . PRO B 1 82  ? 20.238  73.108  52.221 1.00 19.90 ? 82   PRO B N     1 
ATOM   4715 C CA    . PRO B 1 82  ? 20.389  74.144  51.206 1.00 19.83 ? 82   PRO B CA    1 
ATOM   4716 C C     . PRO B 1 82  ? 21.136  75.358  51.738 1.00 20.07 ? 82   PRO B C     1 
ATOM   4717 O O     . PRO B 1 82  ? 20.827  75.865  52.825 1.00 18.45 ? 82   PRO B O     1 
ATOM   4718 C CB    . PRO B 1 82  ? 18.953  74.545  50.807 1.00 21.02 ? 82   PRO B CB    1 
ATOM   4719 C CG    . PRO B 1 82  ? 18.082  73.390  51.298 1.00 21.39 ? 82   PRO B CG    1 
ATOM   4720 C CD    . PRO B 1 82  ? 18.813  72.875  52.546 1.00 21.24 ? 82   PRO B CD    1 
ATOM   4721 N N     . VAL B 1 83  ? 22.101  75.814  50.960 1.00 17.74 ? 83   VAL B N     1 
ATOM   4722 C CA    . VAL B 1 83  ? 22.854  77.063  51.272 1.00 19.01 ? 83   VAL B CA    1 
ATOM   4723 C C     . VAL B 1 83  ? 22.943  77.886  49.985 1.00 20.16 ? 83   VAL B C     1 
ATOM   4724 O O     . VAL B 1 83  ? 23.022  77.286  48.902 1.00 19.40 ? 83   VAL B O     1 
ATOM   4725 C CB    . VAL B 1 83  ? 24.235  76.823  51.861 1.00 20.34 ? 83   VAL B CB    1 
ATOM   4726 C CG1   . VAL B 1 83  ? 24.189  75.914  53.076 1.00 23.52 ? 83   VAL B CG1   1 
ATOM   4727 C CG2   . VAL B 1 83  ? 25.228  76.300  50.830 1.00 22.40 ? 83   VAL B CG2   1 
ATOM   4728 N N     . SER B 1 84  ? 22.990  79.200  50.098 1.00 17.72 ? 84   SER B N     1 
ATOM   4729 C CA    . SER B 1 84  ? 23.059  80.118  48.930 1.00 19.44 ? 84   SER B CA    1 
ATOM   4730 C C     . SER B 1 84  ? 24.532  80.249  48.552 1.00 19.80 ? 84   SER B C     1 
ATOM   4731 O O     . SER B 1 84  ? 24.903  79.943  47.420 1.00 21.32 ? 84   SER B O     1 
ATOM   4732 C CB    . SER B 1 84  ? 22.455  81.452  49.271 1.00 17.94 ? 84   SER B CB    1 
ATOM   4733 O OG    . SER B 1 84  ? 21.077  81.381  49.389 1.00 19.38 ? 84   SER B OG    1 
ATOM   4734 N N     . ARG B 1 85  ? 25.351  80.679  49.517 1.00 18.72 ? 85   ARG B N     1 
ATOM   4735 C CA    . ARG B 1 85  ? 26.814  80.668  49.347 1.00 19.99 ? 85   ARG B CA    1 
ATOM   4736 C C     . ARG B 1 85  ? 27.495  79.915  50.486 1.00 19.77 ? 85   ARG B C     1 
ATOM   4737 O O     . ARG B 1 85  ? 28.665  79.487  50.285 1.00 20.83 ? 85   ARG B O     1 
ATOM   4738 C CB    . ARG B 1 85  ? 27.384  82.076  49.221 1.00 20.19 ? 85   ARG B CB    1 
ATOM   4739 C CG    . ARG B 1 85  ? 27.126  82.704  47.869 1.00 20.97 ? 85   ARG B CG    1 
ATOM   4740 C CD    . ARG B 1 85  ? 27.540  84.144  47.818 1.00 21.48 ? 85   ARG B CD    1 
ATOM   4741 N NE    . ARG B 1 85  ? 28.941  84.312  47.989 1.00 23.83 ? 85   ARG B NE    1 
ATOM   4742 C CZ    . ARG B 1 85  ? 29.874  84.114  47.067 1.00 25.16 ? 85   ARG B CZ    1 
ATOM   4743 N NH1   . ARG B 1 85  ? 29.547  83.777  45.839 1.00 26.19 ? 85   ARG B NH1   1 
ATOM   4744 N NH2   . ARG B 1 85  ? 31.131  84.332  47.381 1.00 27.24 ? 85   ARG B NH2   1 
ATOM   4745 N N     . GLY B 1 86  ? 26.824  79.699  51.617 1.00 20.05 ? 86   GLY B N     1 
ATOM   4746 C CA    . GLY B 1 86  ? 27.367  78.819  52.682 1.00 20.51 ? 86   GLY B CA    1 
ATOM   4747 C C     . GLY B 1 86  ? 28.441  79.503  53.515 1.00 22.80 ? 86   GLY B C     1 
ATOM   4748 O O     . GLY B 1 86  ? 29.236  78.790  54.180 1.00 24.71 ? 86   GLY B O     1 
ATOM   4749 N N     . LYS B 1 87  ? 28.436  80.829  53.564 1.00 21.17 ? 87   LYS B N     1 
ATOM   4750 C CA    . LYS B 1 87  ? 29.454  81.611  54.325 1.00 21.64 ? 87   LYS B CA    1 
ATOM   4751 C C     . LYS B 1 87  ? 28.906  81.987  55.700 1.00 19.84 ? 87   LYS B C     1 
ATOM   4752 O O     . LYS B 1 87  ? 29.314  82.999  56.263 1.00 19.58 ? 87   LYS B O     1 
ATOM   4753 C CB    . LYS B 1 87  ? 29.878  82.848  53.541 1.00 24.70 ? 87   LYS B CB    1 
ATOM   4754 C CG    . LYS B 1 87  ? 30.161  82.526  52.090 1.00 25.04 ? 87   LYS B CG    1 
ATOM   4755 C CD    . LYS B 1 87  ? 31.260  81.517  51.952 1.00 26.79 ? 87   LYS B CD    1 
ATOM   4756 C CE    . LYS B 1 87  ? 31.696  81.378  50.498 1.00 28.33 ? 87   LYS B CE    1 
ATOM   4757 N NZ    . LYS B 1 87  ? 32.775  80.370  50.387 1.00 31.82 ? 87   LYS B NZ    1 
ATOM   4758 N N     . ASN B 1 88  ? 28.035  81.159  56.259 1.00 22.09 ? 88   ASN B N     1 
ATOM   4759 C CA    . ASN B 1 88  ? 27.407  81.486  57.549 1.00 20.39 ? 88   ASN B CA    1 
ATOM   4760 C C     . ASN B 1 88  ? 28.411  81.214  58.686 1.00 22.67 ? 88   ASN B C     1 
ATOM   4761 O O     . ASN B 1 88  ? 28.042  80.554  59.708 1.00 20.78 ? 88   ASN B O     1 
ATOM   4762 C CB    . ASN B 1 88  ? 26.111  80.715  57.704 1.00 22.14 ? 88   ASN B CB    1 
ATOM   4763 C CG    . ASN B 1 88  ? 25.075  81.475  58.506 1.00 23.05 ? 88   ASN B CG    1 
ATOM   4764 O OD1   . ASN B 1 88  ? 25.176  82.690  58.674 1.00 20.74 ? 88   ASN B OD1   1 
ATOM   4765 N ND2   . ASN B 1 88  ? 24.058  80.758  58.952 1.00 21.28 ? 88   ASN B ND2   1 
ATOM   4766 N N     . PHE B 1 89  ? 29.617  81.777  58.572 1.00 20.99 ? 89   PHE B N     1 
ATOM   4767 C CA    . PHE B 1 89  ? 30.668  81.685  59.613 1.00 21.02 ? 89   PHE B CA    1 
ATOM   4768 C C     . PHE B 1 89  ? 30.202  82.280  60.931 1.00 21.51 ? 89   PHE B C     1 
ATOM   4769 O O     . PHE B 1 89  ? 29.525  83.326  60.926 1.00 22.22 ? 89   PHE B O     1 
ATOM   4770 C CB    . PHE B 1 89  ? 31.954  82.366  59.145 1.00 25.88 ? 89   PHE B CB    1 
ATOM   4771 C CG    . PHE B 1 89  ? 32.433  81.831  57.813 1.00 31.00 ? 89   PHE B CG    1 
ATOM   4772 C CD1   . PHE B 1 89  ? 32.245  80.495  57.480 1.00 34.57 ? 89   PHE B CD1   1 
ATOM   4773 C CD2   . PHE B 1 89  ? 32.913  82.685  56.828 1.00 39.73 ? 89   PHE B CD2   1 
ATOM   4774 C CE1   . PHE B 1 89  ? 32.664  79.990  56.254 1.00 39.96 ? 89   PHE B CE1   1 
ATOM   4775 C CE2   . PHE B 1 89  ? 33.328  82.185  55.598 1.00 39.58 ? 89   PHE B CE2   1 
ATOM   4776 C CZ    . PHE B 1 89  ? 33.216  80.831  55.321 1.00 39.14 ? 89   PHE B CZ    1 
ATOM   4777 N N     . ALA B 1 90  ? 30.519  81.558  62.006 1.00 19.88 ? 90   ALA B N     1 
ATOM   4778 C CA    . ALA B 1 90  ? 30.099  81.772  63.411 1.00 22.32 ? 90   ALA B CA    1 
ATOM   4779 C C     . ALA B 1 90  ? 28.725  81.157  63.700 1.00 22.96 ? 90   ALA B C     1 
ATOM   4780 O O     . ALA B 1 90  ? 28.311  81.196  64.881 1.00 22.36 ? 90   ALA B O     1 
ATOM   4781 C CB    . ALA B 1 90  ? 30.102  83.244  63.757 1.00 23.99 ? 90   ALA B CB    1 
ATOM   4782 N N     . TYR B 1 91  ? 28.009  80.661  62.683 1.00 21.78 ? 91   TYR B N     1 
ATOM   4783 C CA    . TYR B 1 91  ? 26.712  79.953  62.859 1.00 19.66 ? 91   TYR B CA    1 
ATOM   4784 C C     . TYR B 1 91  ? 26.757  78.568  62.196 1.00 20.34 ? 91   TYR B C     1 
ATOM   4785 O O     . TYR B 1 91  ? 25.703  77.944  62.079 1.00 19.58 ? 91   TYR B O     1 
ATOM   4786 C CB    . TYR B 1 91  ? 25.598  80.807  62.255 1.00 19.75 ? 91   TYR B CB    1 
ATOM   4787 C CG    . TYR B 1 91  ? 25.282  82.109  62.961 1.00 20.59 ? 91   TYR B CG    1 
ATOM   4788 C CD1   . TYR B 1 91  ? 25.139  82.189  64.339 1.00 21.70 ? 91   TYR B CD1   1 
ATOM   4789 C CD2   . TYR B 1 91  ? 25.220  83.294  62.248 1.00 20.16 ? 91   TYR B CD2   1 
ATOM   4790 C CE1   . TYR B 1 91  ? 24.821  83.385  64.970 1.00 21.88 ? 91   TYR B CE1   1 
ATOM   4791 C CE2   . TYR B 1 91  ? 24.920  84.493  62.873 1.00 21.58 ? 91   TYR B CE2   1 
ATOM   4792 C CZ    . TYR B 1 91  ? 24.679  84.543  64.237 1.00 22.70 ? 91   TYR B CZ    1 
ATOM   4793 O OH    . TYR B 1 91  ? 24.376  85.750  64.837 1.00 22.61 ? 91   TYR B OH    1 
ATOM   4794 N N     . GLY B 1 92  ? 27.946  78.110  61.783 1.00 21.38 ? 92   GLY B N     1 
ATOM   4795 C CA    . GLY B 1 92  ? 28.186  76.735  61.329 1.00 20.55 ? 92   GLY B CA    1 
ATOM   4796 C C     . GLY B 1 92  ? 28.796  76.656  59.942 1.00 21.23 ? 92   GLY B C     1 
ATOM   4797 O O     . GLY B 1 92  ? 29.019  75.522  59.467 1.00 21.42 ? 92   GLY B O     1 
ATOM   4798 N N     . GLY B 1 93  ? 28.983  77.795  59.270 1.00 20.11 ? 93   GLY B N     1 
ATOM   4799 C CA    . GLY B 1 93  ? 29.372  77.821  57.858 1.00 20.78 ? 93   GLY B CA    1 
ATOM   4800 C C     . GLY B 1 93  ? 28.313  77.142  56.994 1.00 22.38 ? 93   GLY B C     1 
ATOM   4801 O O     . GLY B 1 93  ? 27.098  77.436  57.174 1.00 21.80 ? 93   GLY B O     1 
ATOM   4802 N N     . ALA B 1 94  ? 28.737  76.178  56.166 1.00 20.92 ? 94   ALA B N     1 
ATOM   4803 C CA    . ALA B 1 94  ? 27.842  75.381  55.284 1.00 21.11 ? 94   ALA B CA    1 
ATOM   4804 C C     . ALA B 1 94  ? 27.447  74.042  55.913 1.00 21.14 ? 94   ALA B C     1 
ATOM   4805 O O     . ALA B 1 94  ? 26.725  73.255  55.261 1.00 20.62 ? 94   ALA B O     1 
ATOM   4806 C CB    . ALA B 1 94  ? 28.483  75.213  53.920 1.00 21.88 ? 94   ALA B CB    1 
ATOM   4807 N N     . ALA B 1 95  ? 27.858  73.769  57.159 1.00 20.67 ? 95   ALA B N     1 
ATOM   4808 C CA    . ALA B 1 95  ? 27.650  72.453  57.793 1.00 21.21 ? 95   ALA B CA    1 
ATOM   4809 C C     . ALA B 1 95  ? 26.191  72.286  58.226 1.00 21.76 ? 95   ALA B C     1 
ATOM   4810 O O     . ALA B 1 95  ? 25.527  73.221  58.651 1.00 20.07 ? 95   ALA B O     1 
ATOM   4811 C CB    . ALA B 1 95  ? 28.577  72.269  58.978 1.00 22.29 ? 95   ALA B CB    1 
ATOM   4812 N N     . PRO B 1 96  ? 25.647  71.055  58.137 1.00 21.82 ? 96   PRO B N     1 
ATOM   4813 C CA    . PRO B 1 96  ? 24.305  70.785  58.613 1.00 19.70 ? 96   PRO B CA    1 
ATOM   4814 C C     . PRO B 1 96  ? 24.195  70.441  60.095 1.00 20.48 ? 96   PRO B C     1 
ATOM   4815 O O     . PRO B 1 96  ? 25.169  70.037  60.769 1.00 19.01 ? 96   PRO B O     1 
ATOM   4816 C CB    . PRO B 1 96  ? 23.935  69.589  57.760 1.00 21.41 ? 96   PRO B CB    1 
ATOM   4817 C CG    . PRO B 1 96  ? 25.216  68.817  57.741 1.00 23.62 ? 96   PRO B CG    1 
ATOM   4818 C CD    . PRO B 1 96  ? 26.292  69.876  57.540 1.00 22.98 ? 96   PRO B CD    1 
ATOM   4819 N N     . VAL B 1 97  ? 22.994  70.652  60.618 1.00 21.76 ? 97   VAL B N     1 
ATOM   4820 C CA    . VAL B 1 97  ? 22.679  70.232  62.002 1.00 21.34 ? 97   VAL B CA    1 
ATOM   4821 C C     . VAL B 1 97  ? 22.934  68.745  62.151 1.00 23.14 ? 97   VAL B C     1 
ATOM   4822 O O     . VAL B 1 97  ? 23.570  68.367  63.147 1.00 24.78 ? 97   VAL B O     1 
ATOM   4823 C CB    . VAL B 1 97  ? 21.253  70.576  62.425 1.00 21.65 ? 97   VAL B CB    1 
ATOM   4824 C CG1   . VAL B 1 97  ? 20.969  69.893  63.763 1.00 24.49 ? 97   VAL B CG1   1 
ATOM   4825 C CG2   . VAL B 1 97  ? 21.083  72.073  62.500 1.00 19.71 ? 97   VAL B CG2   1 
ATOM   4826 N N     . MET B 1 98  ? 22.376  67.956  61.234 1.00 22.74 ? 98   MET B N     1 
ATOM   4827 C CA    . MET B 1 98  ? 22.349  66.486  61.361 1.00 23.32 ? 98   MET B CA    1 
ATOM   4828 C C     . MET B 1 98  ? 23.448  65.888  60.465 1.00 21.76 ? 98   MET B C     1 
ATOM   4829 O O     . MET B 1 98  ? 23.395  66.071  59.234 1.00 23.58 ? 98   MET B O     1 
ATOM   4830 C CB    . MET B 1 98  ? 20.959  65.944  60.993 1.00 22.56 ? 98   MET B CB    1 
ATOM   4831 C CG    . MET B 1 98  ? 20.844  64.448  61.333 1.00 23.22 ? 98   MET B CG    1 
ATOM   4832 S SD    . MET B 1 98  ? 19.364  63.701  60.678 1.00 25.98 ? 98   MET B SD    1 
ATOM   4833 C CE    . MET B 1 98  ? 19.676  63.696  58.922 1.00 25.64 ? 98   MET B CE    1 
ATOM   4834 N N     . SER B 1 99  ? 24.429  65.189  61.045 1.00 21.53 ? 99   SER B N     1 
ATOM   4835 C CA    . SER B 1 99  ? 25.462  64.455  60.257 1.00 21.42 ? 99   SER B CA    1 
ATOM   4836 C C     . SER B 1 99  ? 24.776  63.539  59.247 1.00 20.84 ? 99   SER B C     1 
ATOM   4837 O O     . SER B 1 99  ? 23.721  62.899  59.567 1.00 23.26 ? 99   SER B O     1 
ATOM   4838 C CB    . SER B 1 99  ? 26.379  63.653  61.157 1.00 23.32 ? 99   SER B CB    1 
ATOM   4839 O OG    . SER B 1 99  ? 27.135  64.518  62.001 1.00 22.49 ? 99   SER B OG    1 
ATOM   4840 N N     . GLY B 1 100 ? 25.385  63.411  58.093 1.00 21.79 ? 100  GLY B N     1 
ATOM   4841 C CA    . GLY B 1 100 ? 24.878  62.550  57.015 1.00 22.56 ? 100  GLY B CA    1 
ATOM   4842 C C     . GLY B 1 100 ? 24.087  63.355  56.012 1.00 23.62 ? 100  GLY B C     1 
ATOM   4843 O O     . GLY B 1 100 ? 23.802  62.821  54.955 1.00 21.94 ? 100  GLY B O     1 
ATOM   4844 N N     . THR B 1 101 ? 23.627  64.555  56.384 1.00 22.79 ? 101  THR B N     1 
ATOM   4845 C CA    . THR B 1 101 ? 22.924  65.460  55.432 1.00 22.28 ? 101  THR B CA    1 
ATOM   4846 C C     . THR B 1 101 ? 23.886  65.813  54.281 1.00 21.03 ? 101  THR B C     1 
ATOM   4847 O O     . THR B 1 101 ? 25.078  66.079  54.538 1.00 22.33 ? 101  THR B O     1 
ATOM   4848 C CB    . THR B 1 101 ? 22.399  66.710  56.146 1.00 20.90 ? 101  THR B CB    1 
ATOM   4849 O OG1   . THR B 1 101 ? 21.652  66.321  57.300 1.00 20.51 ? 101  THR B OG1   1 
ATOM   4850 C CG2   . THR B 1 101 ? 21.507  67.530  55.246 1.00 20.12 ? 101  THR B CG2   1 
ATOM   4851 N N     . VAL B 1 102 ? 23.327  65.953  53.073 1.00 21.45 ? 102  VAL B N     1 
ATOM   4852 C CA    . VAL B 1 102 ? 24.048  66.383  51.853 1.00 20.48 ? 102  VAL B CA    1 
ATOM   4853 C C     . VAL B 1 102 ? 23.847  67.883  51.666 1.00 19.62 ? 102  VAL B C     1 
ATOM   4854 O O     . VAL B 1 102 ? 22.720  68.299  51.547 1.00 19.63 ? 102  VAL B O     1 
ATOM   4855 C CB    . VAL B 1 102 ? 23.574  65.586  50.628 1.00 20.87 ? 102  VAL B CB    1 
ATOM   4856 C CG1   . VAL B 1 102 ? 24.183  66.080  49.329 1.00 21.12 ? 102  VAL B CG1   1 
ATOM   4857 C CG2   . VAL B 1 102 ? 23.851  64.112  50.804 1.00 21.93 ? 102  VAL B CG2   1 
ATOM   4858 N N     . VAL B 1 103 ? 24.914  68.662  51.570 1.00 20.69 ? 103  VAL B N     1 
ATOM   4859 C CA    . VAL B 1 103 ? 24.780  70.121  51.325 1.00 20.28 ? 103  VAL B CA    1 
ATOM   4860 C C     . VAL B 1 103 ? 24.308  70.357  49.887 1.00 21.18 ? 103  VAL B C     1 
ATOM   4861 O O     . VAL B 1 103 ? 24.810  69.726  48.943 1.00 21.66 ? 103  VAL B O     1 
ATOM   4862 C CB    . VAL B 1 103 ? 26.072  70.877  51.645 1.00 20.82 ? 103  VAL B CB    1 
ATOM   4863 C CG1   . VAL B 1 103 ? 25.955  72.347  51.324 1.00 21.24 ? 103  VAL B CG1   1 
ATOM   4864 C CG2   . VAL B 1 103 ? 26.466  70.664  53.075 1.00 23.11 ? 103  VAL B CG2   1 
ATOM   4865 N N     . LEU B 1 104 ? 23.347  71.233  49.734 1.00 18.92 ? 104  LEU B N     1 
ATOM   4866 C CA    . LEU B 1 104 ? 22.844  71.693  48.405 1.00 20.00 ? 104  LEU B CA    1 
ATOM   4867 C C     . LEU B 1 104 ? 23.392  73.103  48.255 1.00 18.85 ? 104  LEU B C     1 
ATOM   4868 O O     . LEU B 1 104 ? 22.865  74.047  48.907 1.00 19.11 ? 104  LEU B O     1 
ATOM   4869 C CB    . LEU B 1 104 ? 21.321  71.625  48.393 1.00 22.12 ? 104  LEU B CB    1 
ATOM   4870 C CG    . LEU B 1 104 ? 20.598  72.239  47.183 1.00 26.70 ? 104  LEU B CG    1 
ATOM   4871 C CD1   . LEU B 1 104 ? 21.065  71.601  45.961 1.00 29.88 ? 104  LEU B CD1   1 
ATOM   4872 C CD2   . LEU B 1 104 ? 19.109  72.015  47.299 1.00 28.27 ? 104  LEU B CD2   1 
ATOM   4873 N N     . ASP B 1 105 ? 24.508  73.218  47.553 1.00 19.27 ? 105  ASP B N     1 
ATOM   4874 C CA    . ASP B 1 105 ? 25.313  74.452  47.461 1.00 20.76 ? 105  ASP B CA    1 
ATOM   4875 C C     . ASP B 1 105 ? 24.897  75.200  46.196 1.00 19.93 ? 105  ASP B C     1 
ATOM   4876 O O     . ASP B 1 105 ? 25.173  74.691  45.111 1.00 21.42 ? 105  ASP B O     1 
ATOM   4877 C CB    . ASP B 1 105 ? 26.787  74.102  47.496 1.00 24.07 ? 105  ASP B CB    1 
ATOM   4878 C CG    . ASP B 1 105 ? 27.687  75.323  47.353 1.00 26.50 ? 105  ASP B CG    1 
ATOM   4879 O OD1   . ASP B 1 105 ? 27.138  76.461  47.226 1.00 23.60 ? 105  ASP B OD1   1 
ATOM   4880 O OD2   . ASP B 1 105 ? 28.931  75.119  47.391 1.00 29.88 ? 105  ASP B OD2   1 
ATOM   4881 N N     . MET B 1 106 ? 24.253  76.356  46.318 1.00 19.11 ? 106  MET B N     1 
ATOM   4882 C CA    . MET B 1 106 ? 23.763  77.131  45.143 1.00 19.24 ? 106  MET B CA    1 
ATOM   4883 C C     . MET B 1 106 ? 24.736  78.230  44.696 1.00 17.66 ? 106  MET B C     1 
ATOM   4884 O O     . MET B 1 106 ? 24.315  79.109  43.933 1.00 18.26 ? 106  MET B O     1 
ATOM   4885 C CB    . MET B 1 106 ? 22.343  77.623  45.425 1.00 20.98 ? 106  MET B CB    1 
ATOM   4886 C CG    . MET B 1 106 ? 21.345  76.432  45.348 1.00 22.33 ? 106  MET B CG    1 
ATOM   4887 S SD    . MET B 1 106 ? 19.653  76.930  45.675 1.00 24.51 ? 106  MET B SD    1 
ATOM   4888 C CE    . MET B 1 106 ? 19.854  77.315  47.410 1.00 24.60 ? 106  MET B CE    1 
ATOM   4889 N N     . ASN B 1 107 ? 26.003  78.150  45.080 1.00 19.23 ? 107  ASN B N     1 
ATOM   4890 C CA    . ASN B 1 107 ? 27.058  79.105  44.675 1.00 22.31 ? 107  ASN B CA    1 
ATOM   4891 C C     . ASN B 1 107 ? 27.023  79.362  43.168 1.00 21.77 ? 107  ASN B C     1 
ATOM   4892 O O     . ASN B 1 107 ? 27.269  80.509  42.808 1.00 21.62 ? 107  ASN B O     1 
ATOM   4893 C CB    . ASN B 1 107 ? 28.476  78.654  45.023 1.00 27.91 ? 107  ASN B CB    1 
ATOM   4894 C CG    . ASN B 1 107 ? 28.895  79.344  46.289 1.00 32.74 ? 107  ASN B CG    1 
ATOM   4895 O OD1   . ASN B 1 107 ? 29.237  80.523  46.237 1.00 32.92 ? 107  ASN B OD1   1 
ATOM   4896 N ND2   . ASN B 1 107 ? 28.847  78.650  47.430 1.00 34.88 ? 107  ASN B ND2   1 
ATOM   4897 N N     . ARG B 1 108 ? 26.829  78.336  42.343 1.00 21.86 ? 108  ARG B N     1 
ATOM   4898 C CA    . ARG B 1 108 ? 26.992  78.454  40.871 1.00 20.31 ? 108  ARG B CA    1 
ATOM   4899 C C     . ARG B 1 108 ? 25.760  79.080  40.266 1.00 22.31 ? 108  ARG B C     1 
ATOM   4900 O O     . ARG B 1 108 ? 25.842  79.537  39.127 1.00 21.04 ? 108  ARG B O     1 
ATOM   4901 C CB    . ARG B 1 108 ? 27.260  77.093  40.253 1.00 21.48 ? 108  ARG B CB    1 
ATOM   4902 C CG    . ARG B 1 108 ? 28.572  76.518  40.771 1.00 24.13 ? 108  ARG B CG    1 
ATOM   4903 C CD    . ARG B 1 108 ? 28.703  75.085  40.336 1.00 26.41 ? 108  ARG B CD    1 
ATOM   4904 N NE    . ARG B 1 108 ? 28.789  75.054  38.886 1.00 24.55 ? 108  ARG B NE    1 
ATOM   4905 C CZ    . ARG B 1 108 ? 28.104  74.284  38.067 1.00 25.29 ? 108  ARG B CZ    1 
ATOM   4906 N NH1   . ARG B 1 108 ? 27.235  73.404  38.508 1.00 26.14 ? 108  ARG B NH1   1 
ATOM   4907 N NH2   . ARG B 1 108 ? 28.297  74.402  36.758 1.00 27.37 ? 108  ARG B NH2   1 
ATOM   4908 N N     . MET B 1 109 ? 24.680  79.187  41.030 1.00 20.89 ? 109  MET B N     1 
ATOM   4909 C CA    . MET B 1 109 ? 23.479  79.947  40.607 1.00 21.66 ? 109  MET B CA    1 
ATOM   4910 C C     . MET B 1 109 ? 23.710  81.421  40.964 1.00 20.05 ? 109  MET B C     1 
ATOM   4911 O O     . MET B 1 109 ? 23.200  81.899  41.997 1.00 19.11 ? 109  MET B O     1 
ATOM   4912 C CB    . MET B 1 109 ? 22.238  79.332  41.260 1.00 20.09 ? 109  MET B CB    1 
ATOM   4913 C CG    . MET B 1 109 ? 21.974  77.968  40.719 1.00 21.56 ? 109  MET B CG    1 
ATOM   4914 S SD    . MET B 1 109 ? 20.657  77.054  41.565 1.00 23.25 ? 109  MET B SD    1 
ATOM   4915 C CE    . MET B 1 109 ? 19.229  78.103  41.307 1.00 22.53 ? 109  MET B CE    1 
ATOM   4916 N N     . ASN B 1 110 ? 24.532  82.116  40.160 1.00 19.39 ? 110  ASN B N     1 
ATOM   4917 C CA    . ASN B 1 110 ? 25.034  83.461  40.500 1.00 19.78 ? 110  ASN B CA    1 
ATOM   4918 C C     . ASN B 1 110 ? 24.621  84.498  39.450 1.00 20.38 ? 110  ASN B C     1 
ATOM   4919 O O     . ASN B 1 110 ? 25.320  85.495  39.333 1.00 19.62 ? 110  ASN B O     1 
ATOM   4920 C CB    . ASN B 1 110 ? 26.527  83.383  40.796 1.00 23.63 ? 110  ASN B CB    1 
ATOM   4921 C CG    . ASN B 1 110 ? 27.316  83.092  39.538 1.00 26.68 ? 110  ASN B CG    1 
ATOM   4922 O OD1   . ASN B 1 110 ? 26.771  82.852  38.465 1.00 22.40 ? 110  ASN B OD1   1 
ATOM   4923 N ND2   . ASN B 1 110 ? 28.598  83.180  39.674 1.00 32.54 ? 110  ASN B ND2   1 
ATOM   4924 N N     . ARG B 1 111 ? 23.479  84.317  38.800 1.00 18.55 ? 111  ARG B N     1 
ATOM   4925 C CA    . ARG B 1 111 ? 22.939  85.287  37.830 1.00 21.37 ? 111  ARG B CA    1 
ATOM   4926 C C     . ARG B 1 111 ? 22.307  86.475  38.581 1.00 22.15 ? 111  ARG B C     1 
ATOM   4927 O O     . ARG B 1 111 ? 21.515  86.287  39.528 1.00 18.20 ? 111  ARG B O     1 
ATOM   4928 C CB    . ARG B 1 111 ? 21.954  84.585  36.906 1.00 27.47 ? 111  ARG B CB    1 
ATOM   4929 C CG    . ARG B 1 111 ? 21.179  85.476  35.944 1.00 36.85 ? 111  ARG B CG    1 
ATOM   4930 C CD    . ARG B 1 111 ? 20.254  84.680  34.984 1.00 44.12 ? 111  ARG B CD    1 
ATOM   4931 N NE    . ARG B 1 111 ? 19.310  85.568  34.281 1.00 43.13 ? 111  ARG B NE    1 
ATOM   4932 C CZ    . ARG B 1 111 ? 18.031  85.300  33.896 1.00 42.87 ? 111  ARG B CZ    1 
ATOM   4933 N NH1   . ARG B 1 111 ? 17.430  84.136  34.119 1.00 43.33 ? 111  ARG B NH1   1 
ATOM   4934 N NH2   . ARG B 1 111 ? 17.332  86.265  33.310 1.00 39.06 ? 111  ARG B NH2   1 
ATOM   4935 N N     . ILE B 1 112 ? 22.722  87.669  38.189 1.00 20.33 ? 112  ILE B N     1 
ATOM   4936 C CA    . ILE B 1 112 ? 22.002  88.915  38.517 1.00 20.81 ? 112  ILE B CA    1 
ATOM   4937 C C     . ILE B 1 112 ? 20.948  89.124  37.433 1.00 23.02 ? 112  ILE B C     1 
ATOM   4938 O O     . ILE B 1 112 ? 21.320  89.465  36.306 1.00 19.63 ? 112  ILE B O     1 
ATOM   4939 C CB    . ILE B 1 112 ? 22.995  90.063  38.653 1.00 21.75 ? 112  ILE B CB    1 
ATOM   4940 C CG1   . ILE B 1 112 ? 24.005  89.787  39.764 1.00 20.34 ? 112  ILE B CG1   1 
ATOM   4941 C CG2   . ILE B 1 112 ? 22.236  91.387  38.851 1.00 24.16 ? 112  ILE B CG2   1 
ATOM   4942 C CD1   . ILE B 1 112 ? 25.123  90.817  39.801 1.00 21.42 ? 112  ILE B CD1   1 
ATOM   4943 N N     . LEU B 1 113 ? 19.685  88.813  37.696 1.00 20.86 ? 113  LEU B N     1 
ATOM   4944 C CA    . LEU B 1 113 ? 18.655  88.799  36.631 1.00 20.44 ? 113  LEU B CA    1 
ATOM   4945 C C     . LEU B 1 113 ? 18.359  90.234  36.199 1.00 19.76 ? 113  LEU B C     1 
ATOM   4946 O O     . LEU B 1 113 ? 18.064  90.504  35.010 1.00 19.36 ? 113  LEU B O     1 
ATOM   4947 C CB    . LEU B 1 113 ? 17.371  88.150  37.147 1.00 23.46 ? 113  LEU B CB    1 
ATOM   4948 C CG    . LEU B 1 113 ? 17.323  86.618  37.230 1.00 29.08 ? 113  LEU B CG    1 
ATOM   4949 C CD1   . LEU B 1 113 ? 17.720  86.088  38.560 1.00 25.42 ? 113  LEU B CD1   1 
ATOM   4950 C CD2   . LEU B 1 113 ? 15.891  86.144  36.929 1.00 33.25 ? 113  LEU B CD2   1 
ATOM   4951 N N     . GLU B 1 114 ? 18.282  91.131  37.175 1.00 19.21 ? 114  GLU B N     1 
ATOM   4952 C CA    . GLU B 1 114 ? 17.969  92.543  36.887 1.00 21.20 ? 114  GLU B CA    1 
ATOM   4953 C C     . GLU B 1 114 ? 18.487  93.411  38.020 1.00 18.83 ? 114  GLU B C     1 
ATOM   4954 O O     . GLU B 1 114 ? 18.291  93.035  39.182 1.00 18.41 ? 114  GLU B O     1 
ATOM   4955 C CB    . GLU B 1 114 ? 16.461  92.725  36.707 1.00 23.89 ? 114  GLU B CB    1 
ATOM   4956 C CG    . GLU B 1 114 ? 16.145  94.043  36.061 1.00 28.16 ? 114  GLU B CG    1 
ATOM   4957 C CD    . GLU B 1 114 ? 14.672  94.408  36.019 1.00 32.24 ? 114  GLU B CD    1 
ATOM   4958 O OE1   . GLU B 1 114 ? 13.800  93.599  36.501 1.00 30.88 ? 114  GLU B OE1   1 
ATOM   4959 O OE2   . GLU B 1 114 ? 14.417  95.526  35.529 1.00 33.80 ? 114  GLU B OE2   1 
ATOM   4960 N N     . VAL B 1 115 ? 19.036  94.561  37.697 1.00 16.84 ? 115  VAL B N     1 
ATOM   4961 C CA    . VAL B 1 115 ? 19.116  95.690  38.667 1.00 17.30 ? 115  VAL B CA    1 
ATOM   4962 C C     . VAL B 1 115 ? 18.390  96.858  38.042 1.00 19.38 ? 115  VAL B C     1 
ATOM   4963 O O     . VAL B 1 115 ? 18.737  97.250  36.895 1.00 20.52 ? 115  VAL B O     1 
ATOM   4964 C CB    . VAL B 1 115 ? 20.546  96.042  39.053 1.00 18.99 ? 115  VAL B CB    1 
ATOM   4965 C CG1   . VAL B 1 115 ? 20.507  97.145  40.105 1.00 20.28 ? 115  VAL B CG1   1 
ATOM   4966 C CG2   . VAL B 1 115 ? 21.305  94.819  39.525 1.00 20.76 ? 115  VAL B CG2   1 
ATOM   4967 N N     . ASN B 1 116 ? 17.399  97.393  38.732 1.00 18.50 ? 116  ASN B N     1 
ATOM   4968 C CA    . ASN B 1 116 ? 16.508  98.440  38.183 1.00 20.10 ? 116  ASN B CA    1 
ATOM   4969 C C     . ASN B 1 116 ? 16.779  99.744  38.923 1.00 20.54 ? 116  ASN B C     1 
ATOM   4970 O O     . ASN B 1 116 ? 16.521  99.847  40.132 1.00 19.15 ? 116  ASN B O     1 
ATOM   4971 C CB    . ASN B 1 116 ? 15.052  97.995  38.258 1.00 21.37 ? 116  ASN B CB    1 
ATOM   4972 C CG    . ASN B 1 116 ? 14.096  98.960  37.585 1.00 21.39 ? 116  ASN B CG    1 
ATOM   4973 O OD1   . ASN B 1 116 ? 14.039  100.135 37.890 1.00 24.95 ? 116  ASN B OD1   1 
ATOM   4974 N ND2   . ASN B 1 116 ? 13.246  98.440  36.733 1.00 23.79 ? 116  ASN B ND2   1 
ATOM   4975 N N     . GLU B 1 117 ? 17.329  100.715 38.227 1.00 19.58 ? 117  GLU B N     1 
ATOM   4976 C CA    . GLU B 1 117 ? 17.713  101.991 38.850 1.00 21.01 ? 117  GLU B CA    1 
ATOM   4977 C C     . GLU B 1 117 ? 16.443  102.776 39.190 1.00 21.35 ? 117  GLU B C     1 
ATOM   4978 O O     . GLU B 1 117 ? 16.397  103.304 40.284 1.00 24.18 ? 117  GLU B O     1 
ATOM   4979 C CB    . GLU B 1 117 ? 18.616  102.837 37.934 1.00 20.82 ? 117  GLU B CB    1 
ATOM   4980 C CG    . GLU B 1 117 ? 19.191  104.038 38.624 1.00 21.92 ? 117  GLU B CG    1 
ATOM   4981 C CD    . GLU B 1 117 ? 20.013  104.835 37.614 1.00 29.06 ? 117  GLU B CD    1 
ATOM   4982 O OE1   . GLU B 1 117 ? 19.470  105.134 36.556 1.00 33.89 ? 117  GLU B OE1   1 
ATOM   4983 O OE2   . GLU B 1 117 ? 21.201  104.949 37.787 1.00 25.39 ? 117  GLU B OE2   1 
ATOM   4984 N N     . GLU B 1 118 ? 15.490  102.864 38.267 1.00 20.94 ? 118  GLU B N     1 
ATOM   4985 C CA    . GLU B 1 118 ? 14.290  103.724 38.368 1.00 22.70 ? 118  GLU B CA    1 
ATOM   4986 C C     . GLU B 1 118 ? 13.443  103.293 39.562 1.00 22.67 ? 118  GLU B C     1 
ATOM   4987 O O     . GLU B 1 118 ? 12.885  104.169 40.240 1.00 22.49 ? 118  GLU B O     1 
ATOM   4988 C CB    . GLU B 1 118 ? 13.433  103.569 37.116 1.00 27.23 ? 118  GLU B CB    1 
ATOM   4989 C CG    . GLU B 1 118 ? 13.787  104.511 35.994 1.00 40.73 ? 118  GLU B CG    1 
ATOM   4990 C CD    . GLU B 1 118 ? 12.839  104.325 34.809 1.00 52.62 ? 118  GLU B CD    1 
ATOM   4991 O OE1   . GLU B 1 118 ? 11.965  103.400 34.863 1.00 59.16 ? 118  GLU B OE1   1 
ATOM   4992 O OE2   . GLU B 1 118 ? 12.976  105.077 33.812 1.00 82.41 ? 118  GLU B OE2   1 
ATOM   4993 N N     . PHE B 1 119 ? 13.344  101.989 39.810 1.00 19.83 ? 119  PHE B N     1 
ATOM   4994 C CA    . PHE B 1 119 ? 12.569  101.499 40.972 1.00 21.06 ? 119  PHE B CA    1 
ATOM   4995 C C     . PHE B 1 119 ? 13.442  101.079 42.145 1.00 25.85 ? 119  PHE B C     1 
ATOM   4996 O O     . PHE B 1 119 ? 12.827  100.685 43.179 1.00 26.07 ? 119  PHE B O     1 
ATOM   4997 C CB    . PHE B 1 119 ? 11.683  100.355 40.522 1.00 22.18 ? 119  PHE B CB    1 
ATOM   4998 C CG    . PHE B 1 119 ? 10.463  100.845 39.812 1.00 23.01 ? 119  PHE B CG    1 
ATOM   4999 C CD1   . PHE B 1 119 ? 9.433   101.437 40.544 1.00 30.87 ? 119  PHE B CD1   1 
ATOM   5000 C CD2   . PHE B 1 119 ? 10.337  100.689 38.456 1.00 27.05 ? 119  PHE B CD2   1 
ATOM   5001 C CE1   . PHE B 1 119 ? 8.278   101.872 39.911 1.00 29.52 ? 119  PHE B CE1   1 
ATOM   5002 C CE2   . PHE B 1 119 ? 9.207   101.166 37.810 1.00 29.61 ? 119  PHE B CE2   1 
ATOM   5003 C CZ    . PHE B 1 119 ? 8.197   101.760 38.539 1.00 30.62 ? 119  PHE B CZ    1 
ATOM   5004 N N     . GLY B 1 120 ? 14.762  101.109 42.004 1.00 19.20 ? 120  GLY B N     1 
ATOM   5005 C CA    . GLY B 1 120 ? 15.662  100.727 43.102 1.00 18.42 ? 120  GLY B CA    1 
ATOM   5006 C C     . GLY B 1 120 ? 15.396  99.314  43.602 1.00 18.15 ? 120  GLY B C     1 
ATOM   5007 O O     . GLY B 1 120 ? 14.892  99.127  44.722 1.00 17.34 ? 120  GLY B O     1 
ATOM   5008 N N     . TYR B 1 121 ? 15.705  98.320  42.792 1.00 18.15 ? 121  TYR B N     1 
ATOM   5009 C CA    . TYR B 1 121 ? 15.659  96.895  43.217 1.00 18.27 ? 121  TYR B CA    1 
ATOM   5010 C C     . TYR B 1 121 ? 16.652  96.073  42.415 1.00 19.17 ? 121  TYR B C     1 
ATOM   5011 O O     . TYR B 1 121 ? 17.145  96.516  41.347 1.00 17.03 ? 121  TYR B O     1 
ATOM   5012 C CB    . TYR B 1 121 ? 14.267  96.300  43.085 1.00 15.77 ? 121  TYR B CB    1 
ATOM   5013 C CG    . TYR B 1 121 ? 13.756  96.045  41.696 1.00 16.81 ? 121  TYR B CG    1 
ATOM   5014 C CD1   . TYR B 1 121 ? 14.175  94.971  40.943 1.00 17.26 ? 121  TYR B CD1   1 
ATOM   5015 C CD2   . TYR B 1 121 ? 12.762  96.845  41.166 1.00 17.31 ? 121  TYR B CD2   1 
ATOM   5016 C CE1   . TYR B 1 121 ? 13.655  94.720  39.675 1.00 17.83 ? 121  TYR B CE1   1 
ATOM   5017 C CE2   . TYR B 1 121 ? 12.227  96.605  39.903 1.00 17.73 ? 121  TYR B CE2   1 
ATOM   5018 C CZ    . TYR B 1 121 ? 12.670  95.532  39.159 1.00 18.05 ? 121  TYR B CZ    1 
ATOM   5019 O OH    . TYR B 1 121 ? 12.158  95.344  37.900 1.00 21.90 ? 121  TYR B OH    1 
ATOM   5020 N N     . ALA B 1 122 ? 16.955  94.905  42.960 1.00 17.76 ? 122  ALA B N     1 
ATOM   5021 C CA    . ALA B 1 122 ? 17.683  93.815  42.271 1.00 17.08 ? 122  ALA B CA    1 
ATOM   5022 C C     . ALA B 1 122 ? 16.866  92.518  42.351 1.00 19.94 ? 122  ALA B C     1 
ATOM   5023 O O     . ALA B 1 122 ? 16.089  92.312  43.333 1.00 17.74 ? 122  ALA B O     1 
ATOM   5024 C CB    . ALA B 1 122 ? 19.054  93.649  42.866 1.00 17.48 ? 122  ALA B CB    1 
ATOM   5025 N N     . LEU B 1 123 ? 16.973  91.701  41.309 1.00 17.04 ? 123  LEU B N     1 
ATOM   5026 C CA    . LEU B 1 123 ? 16.440  90.318  41.322 1.00 16.29 ? 123  LEU B CA    1 
ATOM   5027 C C     . LEU B 1 123 ? 17.657  89.424  41.111 1.00 17.10 ? 123  LEU B C     1 
ATOM   5028 O O     . LEU B 1 123 ? 18.339  89.584  40.077 1.00 17.89 ? 123  LEU B O     1 
ATOM   5029 C CB    . LEU B 1 123 ? 15.408  90.193  40.216 1.00 16.43 ? 123  LEU B CB    1 
ATOM   5030 C CG    . LEU B 1 123 ? 14.837  88.787  40.021 1.00 17.64 ? 123  LEU B CG    1 
ATOM   5031 C CD1   . LEU B 1 123 ? 14.133  88.309  41.277 1.00 18.18 ? 123  LEU B CD1   1 
ATOM   5032 C CD2   . LEU B 1 123 ? 13.921  88.771  38.808 1.00 19.48 ? 123  LEU B CD2   1 
ATOM   5033 N N     . VAL B 1 124 ? 17.964  88.584  42.089 1.00 16.34 ? 124  VAL B N     1 
ATOM   5034 C CA    . VAL B 1 124 ? 19.217  87.793  42.116 1.00 17.31 ? 124  VAL B CA    1 
ATOM   5035 C C     . VAL B 1 124 ? 18.959  86.327  42.444 1.00 18.11 ? 124  VAL B C     1 
ATOM   5036 O O     . VAL B 1 124 ? 17.989  85.972  43.170 1.00 18.08 ? 124  VAL B O     1 
ATOM   5037 C CB    . VAL B 1 124 ? 20.192  88.424  43.126 1.00 17.88 ? 124  VAL B CB    1 
ATOM   5038 C CG1   . VAL B 1 124 ? 20.684  89.769  42.664 1.00 18.36 ? 124  VAL B CG1   1 
ATOM   5039 C CG2   . VAL B 1 124 ? 19.592  88.546  44.518 1.00 18.43 ? 124  VAL B CG2   1 
ATOM   5040 N N     . GLU B 1 125 ? 19.878  85.516  41.971 1.00 18.22 ? 125  GLU B N     1 
ATOM   5041 C CA    . GLU B 1 125 ? 20.000  84.113  42.362 1.00 18.38 ? 125  GLU B CA    1 
ATOM   5042 C C     . GLU B 1 125 ? 20.866  84.025  43.611 1.00 17.51 ? 125  GLU B C     1 
ATOM   5043 O O     . GLU B 1 125 ? 21.540  84.970  44.015 1.00 18.09 ? 125  GLU B O     1 
ATOM   5044 C CB    . GLU B 1 125 ? 20.590  83.317  41.211 1.00 18.96 ? 125  GLU B CB    1 
ATOM   5045 C CG    . GLU B 1 125 ? 19.692  83.184  40.033 1.00 18.19 ? 125  GLU B CG    1 
ATOM   5046 C CD    . GLU B 1 125 ? 20.245  82.179  39.020 1.00 21.88 ? 125  GLU B CD    1 
ATOM   5047 O OE1   . GLU B 1 125 ? 21.473  82.088  38.911 1.00 21.39 ? 125  GLU B OE1   1 
ATOM   5048 O OE2   . GLU B 1 125 ? 19.430  81.544  38.332 1.00 22.45 ? 125  GLU B OE2   1 
ATOM   5049 N N     . PRO B 1 126 ? 20.812  82.876  44.310 1.00 17.31 ? 126  PRO B N     1 
ATOM   5050 C CA    . PRO B 1 126 ? 21.414  82.757  45.642 1.00 16.86 ? 126  PRO B CA    1 
ATOM   5051 C C     . PRO B 1 126 ? 22.940  82.849  45.700 1.00 17.49 ? 126  PRO B C     1 
ATOM   5052 O O     . PRO B 1 126 ? 23.503  83.242  46.710 1.00 17.61 ? 126  PRO B O     1 
ATOM   5053 C CB    . PRO B 1 126 ? 20.992  81.352  46.052 1.00 17.41 ? 126  PRO B CB    1 
ATOM   5054 C CG    . PRO B 1 126 ? 19.736  81.062  45.279 1.00 17.09 ? 126  PRO B CG    1 
ATOM   5055 C CD    . PRO B 1 126 ? 20.019  81.701  43.948 1.00 15.61 ? 126  PRO B CD    1 
ATOM   5056 N N     . GLY B 1 127 ? 23.615  82.485  44.605 1.00 16.34 ? 127  GLY B N     1 
ATOM   5057 C CA    . GLY B 1 127 ? 25.084  82.501  44.578 1.00 17.79 ? 127  GLY B CA    1 
ATOM   5058 C C     . GLY B 1 127 ? 25.645  83.890  44.393 1.00 18.77 ? 127  GLY B C     1 
ATOM   5059 O O     . GLY B 1 127 ? 26.862  84.031  44.455 1.00 19.15 ? 127  GLY B O     1 
ATOM   5060 N N     . VAL B 1 128 ? 24.805  84.908  44.140 1.00 20.56 ? 128  VAL B N     1 
ATOM   5061 C CA    . VAL B 1 128 ? 25.272  86.311  43.993 1.00 18.45 ? 128  VAL B CA    1 
ATOM   5062 C C     . VAL B 1 128 ? 25.816  86.840  45.337 1.00 19.88 ? 128  VAL B C     1 
ATOM   5063 O O     . VAL B 1 128 ? 25.093  86.874  46.334 1.00 19.25 ? 128  VAL B O     1 
ATOM   5064 C CB    . VAL B 1 128 ? 24.160  87.206  43.415 1.00 19.25 ? 128  VAL B CB    1 
ATOM   5065 C CG1   . VAL B 1 128 ? 24.625  88.644  43.305 1.00 18.66 ? 128  VAL B CG1   1 
ATOM   5066 C CG2   . VAL B 1 128 ? 23.676  86.716  42.060 1.00 19.62 ? 128  VAL B CG2   1 
ATOM   5067 N N     . SER B 1 129 ? 27.078  87.238  45.367 1.00 18.15 ? 129  SER B N     1 
ATOM   5068 C CA    . SER B 1 129 ? 27.748  87.814  46.564 1.00 18.34 ? 129  SER B CA    1 
ATOM   5069 C C     . SER B 1 129 ? 27.477  89.309  46.653 1.00 16.34 ? 129  SER B C     1 
ATOM   5070 O O     . SER B 1 129 ? 27.075  89.943  45.637 1.00 17.62 ? 129  SER B O     1 
ATOM   5071 C CB    . SER B 1 129 ? 29.234  87.545  46.570 1.00 19.92 ? 129  SER B CB    1 
ATOM   5072 O OG    . SER B 1 129 ? 29.912  88.351  45.607 1.00 17.66 ? 129  SER B OG    1 
ATOM   5073 N N     . TYR B 1 130 ? 27.677  89.885  47.830 1.00 16.28 ? 130  TYR B N     1 
ATOM   5074 C CA    . TYR B 1 130 ? 27.642  91.362  47.944 1.00 17.15 ? 130  TYR B CA    1 
ATOM   5075 C C     . TYR B 1 130 ? 28.718  91.966  47.003 1.00 17.72 ? 130  TYR B C     1 
ATOM   5076 O O     . TYR B 1 130 ? 28.390  92.979  46.354 1.00 19.15 ? 130  TYR B O     1 
ATOM   5077 C CB    . TYR B 1 130 ? 27.775  91.822  49.385 1.00 18.14 ? 130  TYR B CB    1 
ATOM   5078 C CG    . TYR B 1 130 ? 26.620  91.356  50.253 1.00 17.78 ? 130  TYR B CG    1 
ATOM   5079 C CD1   . TYR B 1 130 ? 25.430  92.044  50.295 1.00 18.45 ? 130  TYR B CD1   1 
ATOM   5080 C CD2   . TYR B 1 130 ? 26.724  90.229  51.042 1.00 19.86 ? 130  TYR B CD2   1 
ATOM   5081 C CE1   . TYR B 1 130 ? 24.372  91.634  51.109 1.00 18.40 ? 130  TYR B CE1   1 
ATOM   5082 C CE2   . TYR B 1 130 ? 25.690  89.806  51.866 1.00 19.65 ? 130  TYR B CE2   1 
ATOM   5083 C CZ    . TYR B 1 130 ? 24.520  90.535  51.935 1.00 18.37 ? 130  TYR B CZ    1 
ATOM   5084 O OH    . TYR B 1 130 ? 23.521  90.139  52.786 1.00 20.19 ? 130  TYR B OH    1 
ATOM   5085 N N     . PHE B 1 131 ? 29.924  91.414  46.948 1.00 19.23 ? 131  PHE B N     1 
ATOM   5086 C CA    . PHE B 1 131 ? 30.985  91.916  46.027 1.00 19.68 ? 131  PHE B CA    1 
ATOM   5087 C C     . PHE B 1 131 ? 30.441  91.949  44.595 1.00 21.03 ? 131  PHE B C     1 
ATOM   5088 O O     . PHE B 1 131 ? 30.589  92.976  43.901 1.00 20.43 ? 131  PHE B O     1 
ATOM   5089 C CB    . PHE B 1 131 ? 32.255  91.081  46.127 1.00 20.16 ? 131  PHE B CB    1 
ATOM   5090 C CG    . PHE B 1 131 ? 33.081  91.355  47.341 1.00 20.13 ? 131  PHE B CG    1 
ATOM   5091 C CD1   . PHE B 1 131 ? 33.668  92.590  47.529 1.00 24.47 ? 131  PHE B CD1   1 
ATOM   5092 C CD2   . PHE B 1 131 ? 33.312  90.369  48.265 1.00 24.11 ? 131  PHE B CD2   1 
ATOM   5093 C CE1   . PHE B 1 131 ? 34.438  92.845  48.652 1.00 24.30 ? 131  PHE B CE1   1 
ATOM   5094 C CE2   . PHE B 1 131 ? 34.059  90.630  49.398 1.00 23.56 ? 131  PHE B CE2   1 
ATOM   5095 C CZ    . PHE B 1 131 ? 34.618  91.868  49.592 1.00 24.04 ? 131  PHE B CZ    1 
ATOM   5096 N N     . GLU B 1 132 ? 29.765  90.871  44.165 1.00 19.78 ? 132  GLU B N     1 
ATOM   5097 C CA    . GLU B 1 132 ? 29.320  90.747  42.766 1.00 19.13 ? 132  GLU B CA    1 
ATOM   5098 C C     . GLU B 1 132 ? 28.231  91.765  42.457 1.00 19.70 ? 132  GLU B C     1 
ATOM   5099 O O     . GLU B 1 132 ? 28.263  92.389  41.368 1.00 19.74 ? 132  GLU B O     1 
ATOM   5100 C CB    . GLU B 1 132 ? 28.869  89.332  42.449 1.00 20.77 ? 132  GLU B CB    1 
ATOM   5101 C CG    . GLU B 1 132 ? 30.031  88.380  42.435 1.00 22.43 ? 132  GLU B CG    1 
ATOM   5102 C CD    . GLU B 1 132 ? 29.652  86.910  42.475 1.00 27.28 ? 132  GLU B CD    1 
ATOM   5103 O OE1   . GLU B 1 132 ? 28.456  86.567  42.709 1.00 24.58 ? 132  GLU B OE1   1 
ATOM   5104 O OE2   . GLU B 1 132 ? 30.580  86.115  42.291 1.00 29.55 ? 132  GLU B OE2   1 
ATOM   5105 N N     . LEU B 1 133 ? 27.287  91.944  43.360 1.00 16.50 ? 133  LEU B N     1 
ATOM   5106 C CA    . LEU B 1 133 ? 26.192  92.890  43.113 1.00 17.95 ? 133  LEU B CA    1 
ATOM   5107 C C     . LEU B 1 133 ? 26.774  94.311  43.100 1.00 17.62 ? 133  LEU B C     1 
ATOM   5108 O O     . LEU B 1 133 ? 26.366  95.134  42.244 1.00 19.45 ? 133  LEU B O     1 
ATOM   5109 C CB    . LEU B 1 133 ? 25.093  92.700  44.168 1.00 17.77 ? 133  LEU B CB    1 
ATOM   5110 C CG    . LEU B 1 133 ? 23.899  93.621  43.994 1.00 18.51 ? 133  LEU B CG    1 
ATOM   5111 C CD1   . LEU B 1 133 ? 23.281  93.515  42.611 1.00 21.88 ? 133  LEU B CD1   1 
ATOM   5112 C CD2   . LEU B 1 133 ? 22.850  93.368  45.040 1.00 21.95 ? 133  LEU B CD2   1 
ATOM   5113 N N     . TYR B 1 134 ? 27.617  94.632  44.063 1.00 18.14 ? 134  TYR B N     1 
ATOM   5114 C CA    . TYR B 1 134 ? 28.267  95.958  44.134 1.00 18.05 ? 134  TYR B CA    1 
ATOM   5115 C C     . TYR B 1 134 ? 29.030  96.240  42.829 1.00 18.96 ? 134  TYR B C     1 
ATOM   5116 O O     . TYR B 1 134 ? 28.818  97.289  42.182 1.00 17.95 ? 134  TYR B O     1 
ATOM   5117 C CB    . TYR B 1 134 ? 29.254  95.969  45.280 1.00 18.62 ? 134  TYR B CB    1 
ATOM   5118 C CG    . TYR B 1 134 ? 29.940  97.306  45.444 1.00 19.38 ? 134  TYR B CG    1 
ATOM   5119 C CD1   . TYR B 1 134 ? 29.262  98.392  45.994 1.00 19.21 ? 134  TYR B CD1   1 
ATOM   5120 C CD2   . TYR B 1 134 ? 31.214  97.518  44.943 1.00 21.46 ? 134  TYR B CD2   1 
ATOM   5121 C CE1   . TYR B 1 134 ? 29.899  99.606  46.198 1.00 20.84 ? 134  TYR B CE1   1 
ATOM   5122 C CE2   . TYR B 1 134 ? 31.872  98.732  45.139 1.00 23.57 ? 134  TYR B CE2   1 
ATOM   5123 C CZ    . TYR B 1 134 ? 31.206  99.776  45.760 1.00 23.43 ? 134  TYR B CZ    1 
ATOM   5124 O OH    . TYR B 1 134 ? 31.827  100.967 45.941 1.00 26.00 ? 134  TYR B OH    1 
ATOM   5125 N N     . ASP B 1 135 ? 29.827  95.279  42.394 1.00 21.00 ? 135  ASP B N     1 
ATOM   5126 C CA    . ASP B 1 135 ? 30.644  95.498  41.168 1.00 22.73 ? 135  ASP B CA    1 
ATOM   5127 C C     . ASP B 1 135 ? 29.749  95.693  39.946 1.00 23.20 ? 135  ASP B C     1 
ATOM   5128 O O     . ASP B 1 135 ? 30.085  96.522  39.088 1.00 22.84 ? 135  ASP B O     1 
ATOM   5129 C CB    . ASP B 1 135 ? 31.617  94.359  40.934 1.00 22.39 ? 135  ASP B CB    1 
ATOM   5130 C CG    . ASP B 1 135 ? 32.758  94.324  41.912 1.00 24.50 ? 135  ASP B CG    1 
ATOM   5131 O OD1   . ASP B 1 135 ? 32.914  95.257  42.747 1.00 25.31 ? 135  ASP B OD1   1 
ATOM   5132 O OD2   . ASP B 1 135 ? 33.399  93.298  41.900 1.00 26.93 ? 135  ASP B OD2   1 
ATOM   5133 N N     . TYR B 1 136 ? 28.669  94.933  39.811 1.00 21.92 ? 136  TYR B N     1 
ATOM   5134 C CA    . TYR B 1 136 ? 27.707  95.063  38.697 1.00 21.19 ? 136  TYR B CA    1 
ATOM   5135 C C     . TYR B 1 136 ? 27.180  96.508  38.650 1.00 22.71 ? 136  TYR B C     1 
ATOM   5136 O O     . TYR B 1 136 ? 27.123  97.170  37.589 1.00 19.05 ? 136  TYR B O     1 
ATOM   5137 C CB    . TYR B 1 136 ? 26.604  94.020  38.901 1.00 21.15 ? 136  TYR B CB    1 
ATOM   5138 C CG    . TYR B 1 136 ? 25.576  93.994  37.840 1.00 21.02 ? 136  TYR B CG    1 
ATOM   5139 C CD1   . TYR B 1 136 ? 24.510  94.858  37.858 1.00 24.35 ? 136  TYR B CD1   1 
ATOM   5140 C CD2   . TYR B 1 136 ? 25.772  93.187  36.732 1.00 25.52 ? 136  TYR B CD2   1 
ATOM   5141 C CE1   . TYR B 1 136 ? 23.564  94.832  36.852 1.00 25.01 ? 136  TYR B CE1   1 
ATOM   5142 C CE2   . TYR B 1 136 ? 24.827  93.128  35.733 1.00 27.57 ? 136  TYR B CE2   1 
ATOM   5143 C CZ    . TYR B 1 136 ? 23.721  93.947  35.804 1.00 27.62 ? 136  TYR B CZ    1 
ATOM   5144 O OH    . TYR B 1 136 ? 22.818  93.900  34.804 1.00 28.83 ? 136  TYR B OH    1 
ATOM   5145 N N     . ILE B 1 137 ? 26.750  97.002  39.808 1.00 20.44 ? 137  ILE B N     1 
ATOM   5146 C CA    . ILE B 1 137 ? 26.162  98.359  39.926 1.00 20.16 ? 137  ILE B CA    1 
ATOM   5147 C C     . ILE B 1 137 ? 27.192  99.429  39.526 1.00 21.50 ? 137  ILE B C     1 
ATOM   5148 O O     . ILE B 1 137 ? 26.801  100.345 38.764 1.00 22.32 ? 137  ILE B O     1 
ATOM   5149 C CB    . ILE B 1 137 ? 25.596  98.552  41.336 1.00 19.90 ? 137  ILE B CB    1 
ATOM   5150 C CG1   . ILE B 1 137 ? 24.316  97.700  41.455 1.00 20.77 ? 137  ILE B CG1   1 
ATOM   5151 C CG2   . ILE B 1 137 ? 25.378  100.043 41.662 1.00 21.39 ? 137  ILE B CG2   1 
ATOM   5152 C CD1   . ILE B 1 137 ? 23.866  97.534  42.884 1.00 21.69 ? 137  ILE B CD1   1 
ATOM   5153 N N     . GLN B 1 138 ? 28.417  99.325  40.015 1.00 21.64 ? 138  GLN B N     1 
ATOM   5154 C CA    . GLN B 1 138 ? 29.518  100.284 39.674 1.00 26.80 ? 138  GLN B CA    1 
ATOM   5155 C C     . GLN B 1 138 ? 29.810  100.215 38.161 1.00 27.21 ? 138  GLN B C     1 
ATOM   5156 O O     . GLN B 1 138 ? 29.744  101.255 37.485 1.00 28.67 ? 138  GLN B O     1 
ATOM   5157 C CB    . GLN B 1 138 ? 30.788  99.988  40.461 1.00 28.59 ? 138  GLN B CB    1 
ATOM   5158 C CG    . GLN B 1 138 ? 30.642  99.994  41.958 1.00 32.45 ? 138  GLN B CG    1 
ATOM   5159 C CD    . GLN B 1 138 ? 29.749  101.076 42.530 1.00 41.38 ? 138  GLN B CD    1 
ATOM   5160 O OE1   . GLN B 1 138 ? 30.060  102.262 42.459 1.00 39.26 ? 138  GLN B OE1   1 
ATOM   5161 N NE2   . GLN B 1 138 ? 28.638  100.656 43.139 1.00 39.01 ? 138  GLN B NE2   1 
ATOM   5162 N N     . GLU B 1 139 ? 29.940  99.014  37.603 1.00 27.20 ? 139  GLU B N     1 
ATOM   5163 C CA    . GLU B 1 139 ? 30.206  98.792  36.161 1.00 29.45 ? 139  GLU B CA    1 
ATOM   5164 C C     . GLU B 1 139 ? 29.093  99.403  35.305 1.00 34.25 ? 139  GLU B C     1 
ATOM   5165 O O     . GLU B 1 139 ? 29.416  100.013 34.285 1.00 30.98 ? 139  GLU B O     1 
ATOM   5166 C CB    . GLU B 1 139 ? 30.333  97.312  35.797 1.00 28.97 ? 139  GLU B CB    1 
ATOM   5167 C CG    . GLU B 1 139 ? 31.580  96.665  36.342 1.00 29.99 ? 139  GLU B CG    1 
ATOM   5168 C CD    . GLU B 1 139 ? 31.493  95.144  36.507 1.00 28.83 ? 139  GLU B CD    1 
ATOM   5169 O OE1   . GLU B 1 139 ? 30.501  94.497  36.078 1.00 29.30 ? 139  GLU B OE1   1 
ATOM   5170 O OE2   . GLU B 1 139 ? 32.435  94.610  37.069 1.00 37.09 ? 139  GLU B OE2   1 
ATOM   5171 N N     . LYS B 1 140 ? 27.831  99.255  35.703 1.00 25.84 ? 140  LYS B N     1 
ATOM   5172 C CA    . LYS B 1 140 ? 26.695  99.735  34.909 1.00 25.61 ? 140  LYS B CA    1 
ATOM   5173 C C     . LYS B 1 140 ? 26.473  101.227 35.186 1.00 23.66 ? 140  LYS B C     1 
ATOM   5174 O O     . LYS B 1 140 ? 25.584  101.786 34.527 1.00 24.38 ? 140  LYS B O     1 
ATOM   5175 C CB    . LYS B 1 140 ? 25.491  98.806  35.110 1.00 29.22 ? 140  LYS B CB    1 
ATOM   5176 C CG    . LYS B 1 140 ? 25.663  97.395  34.567 1.00 36.29 ? 140  LYS B CG    1 
ATOM   5177 C CD    . LYS B 1 140 ? 24.876  97.143  33.322 1.00 50.42 ? 140  LYS B CD    1 
ATOM   5178 C CE    . LYS B 1 140 ? 25.070  95.760  32.726 1.00 56.27 ? 140  LYS B CE    1 
ATOM   5179 N NZ    . LYS B 1 140 ? 26.393  95.642  32.072 1.00 54.66 ? 140  LYS B NZ    1 
ATOM   5180 N N     . GLY B 1 141 ? 27.151  101.825 36.168 1.00 23.22 ? 141  GLY B N     1 
ATOM   5181 C CA    . GLY B 1 141 ? 27.018  103.254 36.521 1.00 25.62 ? 141  GLY B CA    1 
ATOM   5182 C C     . GLY B 1 141 ? 25.677  103.570 37.172 1.00 24.78 ? 141  GLY B C     1 
ATOM   5183 O O     . GLY B 1 141 ? 25.156  104.647 36.914 1.00 26.05 ? 141  GLY B O     1 
ATOM   5184 N N     . LEU B 1 142 ? 25.055  102.597 37.861 1.00 22.69 ? 142  LEU B N     1 
ATOM   5185 C CA    . LEU B 1 142 ? 23.673  102.770 38.387 1.00 22.47 ? 142  LEU B CA    1 
ATOM   5186 C C     . LEU B 1 142 ? 23.769  103.518 39.732 1.00 20.85 ? 142  LEU B C     1 
ATOM   5187 O O     . LEU B 1 142 ? 24.664  103.221 40.523 1.00 21.12 ? 142  LEU B O     1 
ATOM   5188 C CB    . LEU B 1 142 ? 22.964  101.418 38.525 1.00 22.33 ? 142  LEU B CB    1 
ATOM   5189 C CG    . LEU B 1 142 ? 22.790  100.593 37.245 1.00 22.99 ? 142  LEU B CG    1 
ATOM   5190 C CD1   . LEU B 1 142 ? 22.024  99.324  37.528 1.00 23.79 ? 142  LEU B CD1   1 
ATOM   5191 C CD2   . LEU B 1 142 ? 22.115  101.367 36.143 1.00 24.39 ? 142  LEU B CD2   1 
ATOM   5192 N N     . LYS B 1 143 ? 22.861  104.441 39.989 1.00 18.90 ? 143  LYS B N     1 
ATOM   5193 C CA    . LYS B 1 143 ? 22.929  105.315 41.184 1.00 20.72 ? 143  LYS B CA    1 
ATOM   5194 C C     . LYS B 1 143 ? 22.155  104.656 42.330 1.00 19.14 ? 143  LYS B C     1 
ATOM   5195 O O     . LYS B 1 143 ? 21.113  105.202 42.758 1.00 19.83 ? 143  LYS B O     1 
ATOM   5196 C CB    . LYS B 1 143 ? 22.337  106.661 40.793 1.00 24.35 ? 143  LYS B CB    1 
ATOM   5197 C CG    . LYS B 1 143 ? 23.044  107.342 39.617 1.00 29.24 ? 143  LYS B CG    1 
ATOM   5198 C CD    . LYS B 1 143 ? 24.539  107.338 39.641 1.00 30.97 ? 143  LYS B CD    1 
ATOM   5199 C CE    . LYS B 1 143 ? 25.040  108.054 38.390 1.00 40.37 ? 143  LYS B CE    1 
ATOM   5200 N NZ    . LYS B 1 143 ? 26.501  108.016 38.270 1.00 45.67 ? 143  LYS B NZ    1 
ATOM   5201 N N     . LEU B 1 144 ? 22.641  103.491 42.715 1.00 18.52 ? 144  LEU B N     1 
ATOM   5202 C CA    . LEU B 1 144 ? 22.069  102.682 43.793 1.00 17.98 ? 144  LEU B CA    1 
ATOM   5203 C C     . LEU B 1 144 ? 23.158  102.282 44.743 1.00 19.72 ? 144  LEU B C     1 
ATOM   5204 O O     . LEU B 1 144 ? 24.327  102.034 44.325 1.00 20.14 ? 144  LEU B O     1 
ATOM   5205 C CB    . LEU B 1 144 ? 21.412  101.435 43.212 1.00 18.87 ? 144  LEU B CB    1 
ATOM   5206 C CG    . LEU B 1 144 ? 20.304  101.676 42.227 1.00 20.33 ? 144  LEU B CG    1 
ATOM   5207 C CD1   . LEU B 1 144 ? 19.950  100.350 41.546 1.00 22.80 ? 144  LEU B CD1   1 
ATOM   5208 C CD2   . LEU B 1 144 ? 19.090  102.307 42.873 1.00 20.14 ? 144  LEU B CD2   1 
ATOM   5209 N N     . TRP B 1 145 ? 22.771  102.204 46.013 1.00 18.27 ? 145  TRP B N     1 
ATOM   5210 C CA    . TRP B 1 145 ? 23.615  101.596 47.054 1.00 18.25 ? 145  TRP B CA    1 
ATOM   5211 C C     . TRP B 1 145 ? 23.015  100.247 47.443 1.00 20.55 ? 145  TRP B C     1 
ATOM   5212 O O     . TRP B 1 145 ? 21.779  100.107 47.351 1.00 18.58 ? 145  TRP B O     1 
ATOM   5213 C CB    . TRP B 1 145 ? 23.701  102.515 48.279 1.00 18.91 ? 145  TRP B CB    1 
ATOM   5214 C CG    . TRP B 1 145 ? 24.503  103.753 48.060 1.00 20.46 ? 145  TRP B CG    1 
ATOM   5215 C CD1   . TRP B 1 145 ? 25.151  104.076 46.902 1.00 23.01 ? 145  TRP B CD1   1 
ATOM   5216 C CD2   . TRP B 1 145 ? 24.894  104.747 49.030 1.00 21.37 ? 145  TRP B CD2   1 
ATOM   5217 N NE1   . TRP B 1 145 ? 25.870  105.216 47.078 1.00 22.58 ? 145  TRP B NE1   1 
ATOM   5218 C CE2   . TRP B 1 145 ? 25.710  105.675 48.354 1.00 22.18 ? 145  TRP B CE2   1 
ATOM   5219 C CE3   . TRP B 1 145 ? 24.594  104.984 50.365 1.00 23.52 ? 145  TRP B CE3   1 
ATOM   5220 C CZ2   . TRP B 1 145 ? 26.250  106.808 48.976 1.00 24.91 ? 145  TRP B CZ2   1 
ATOM   5221 C CZ3   . TRP B 1 145 ? 25.116  106.103 50.981 1.00 21.94 ? 145  TRP B CZ3   1 
ATOM   5222 C CH2   . TRP B 1 145 ? 25.927  106.995 50.295 1.00 22.03 ? 145  TRP B CH2   1 
ATOM   5223 N N     . ILE B 1 146 ? 23.880  99.304  47.850 1.00 19.14 ? 146  ILE B N     1 
ATOM   5224 C CA    . ILE B 1 146 ? 23.440  98.036  48.464 1.00 18.06 ? 146  ILE B CA    1 
ATOM   5225 C C     . ILE B 1 146 ? 23.605  98.196  49.958 1.00 19.26 ? 146  ILE B C     1 
ATOM   5226 O O     . ILE B 1 146 ? 24.111  99.270  50.423 1.00 18.99 ? 146  ILE B O     1 
ATOM   5227 C CB    . ILE B 1 146 ? 24.212  96.829  47.871 1.00 19.24 ? 146  ILE B CB    1 
ATOM   5228 C CG1   . ILE B 1 146 ? 25.706  96.844  48.170 1.00 18.58 ? 146  ILE B CG1   1 
ATOM   5229 C CG2   . ILE B 1 146 ? 23.998  96.776  46.378 1.00 20.03 ? 146  ILE B CG2   1 
ATOM   5230 C CD1   . ILE B 1 146 ? 26.387  95.530  47.834 1.00 20.43 ? 146  ILE B CD1   1 
ATOM   5231 N N     . ASP B 1 147 ? 23.221  97.165  50.694 1.00 16.89 ? 147  ASP B N     1 
ATOM   5232 C CA    . ASP B 1 147 ? 23.360  97.155  52.152 1.00 18.55 ? 147  ASP B CA    1 
ATOM   5233 C C     . ASP B 1 147 ? 24.115  95.882  52.463 1.00 19.14 ? 147  ASP B C     1 
ATOM   5234 O O     . ASP B 1 147 ? 23.576  94.788  52.170 1.00 19.64 ? 147  ASP B O     1 
ATOM   5235 C CB    . ASP B 1 147 ? 22.001  97.286  52.830 1.00 18.33 ? 147  ASP B CB    1 
ATOM   5236 C CG    . ASP B 1 147 ? 22.185  97.441  54.334 1.00 17.66 ? 147  ASP B CG    1 
ATOM   5237 O OD1   . ASP B 1 147 ? 22.717  96.498  54.932 1.00 18.74 ? 147  ASP B OD1   1 
ATOM   5238 O OD2   . ASP B 1 147 ? 21.903  98.549  54.856 1.00 17.42 ? 147  ASP B OD2   1 
ATOM   5239 N N     . VAL B 1 148 ? 25.267  96.020  53.108 1.00 17.63 ? 148  VAL B N     1 
ATOM   5240 C CA    . VAL B 1 148 ? 26.200  94.891  53.306 1.00 17.87 ? 148  VAL B CA    1 
ATOM   5241 C C     . VAL B 1 148 ? 26.292  94.545  54.773 1.00 16.66 ? 148  VAL B C     1 
ATOM   5242 O O     . VAL B 1 148 ? 26.373  95.426  55.626 1.00 17.92 ? 148  VAL B O     1 
ATOM   5243 C CB    . VAL B 1 148 ? 27.593  95.150  52.708 1.00 17.87 ? 148  VAL B CB    1 
ATOM   5244 C CG1   . VAL B 1 148 ? 27.442  95.439  51.229 1.00 19.25 ? 148  VAL B CG1   1 
ATOM   5245 C CG2   . VAL B 1 148 ? 28.358  96.228  53.434 1.00 17.64 ? 148  VAL B CG2   1 
ATOM   5246 N N     . PRO B 1 149 ? 26.389  93.243  55.085 1.00 17.94 ? 149  PRO B N     1 
ATOM   5247 C CA    . PRO B 1 149 ? 26.864  92.834  56.405 1.00 19.19 ? 149  PRO B CA    1 
ATOM   5248 C C     . PRO B 1 149 ? 28.381  93.135  56.424 1.00 21.36 ? 149  PRO B C     1 
ATOM   5249 O O     . PRO B 1 149 ? 28.915  93.568  55.392 1.00 21.78 ? 149  PRO B O     1 
ATOM   5250 C CB    . PRO B 1 149 ? 26.453  91.358  56.435 1.00 21.37 ? 149  PRO B CB    1 
ATOM   5251 C CG    . PRO B 1 149 ? 26.747  90.916  55.015 1.00 21.24 ? 149  PRO B CG    1 
ATOM   5252 C CD    . PRO B 1 149 ? 26.341  92.108  54.157 1.00 17.50 ? 149  PRO B CD    1 
ATOM   5253 N N     . ASP B 1 150 ? 29.078  92.828  57.525 1.00 22.08 ? 150  ASP B N     1 
ATOM   5254 C CA    . ASP B 1 150 ? 30.531  93.121  57.667 1.00 24.37 ? 150  ASP B CA    1 
ATOM   5255 C C     . ASP B 1 150 ? 31.378  92.363  56.636 1.00 25.18 ? 150  ASP B C     1 
ATOM   5256 O O     . ASP B 1 150 ? 32.363  92.949  56.201 1.00 29.56 ? 150  ASP B O     1 
ATOM   5257 C CB    . ASP B 1 150 ? 31.087  92.815  59.049 1.00 24.22 ? 150  ASP B CB    1 
ATOM   5258 C CG    . ASP B 1 150 ? 30.629  93.808  60.097 1.00 26.55 ? 150  ASP B CG    1 
ATOM   5259 O OD1   . ASP B 1 150 ? 30.478  94.984  59.759 1.00 28.27 ? 150  ASP B OD1   1 
ATOM   5260 O OD2   . ASP B 1 150 ? 30.313  93.357  61.200 1.00 37.65 ? 150  ASP B OD2   1 
ATOM   5261 N N     . LEU B 1 151 ? 31.005  91.152  56.239 1.00 27.45 ? 151  LEU B N     1 
ATOM   5262 C CA    . LEU B 1 151 ? 31.778  90.360  55.248 1.00 28.22 ? 151  LEU B CA    1 
ATOM   5263 C C     . LEU B 1 151 ? 31.051  90.354  53.903 1.00 27.19 ? 151  LEU B C     1 
ATOM   5264 O O     . LEU B 1 151 ? 29.977  89.764  53.784 1.00 29.04 ? 151  LEU B O     1 
ATOM   5265 C CB    . LEU B 1 151 ? 32.018  88.949  55.792 1.00 33.17 ? 151  LEU B CB    1 
ATOM   5266 C CG    . LEU B 1 151 ? 32.673  88.926  57.181 1.00 36.63 ? 151  LEU B CG    1 
ATOM   5267 C CD1   . LEU B 1 151 ? 32.884  87.499  57.695 1.00 37.82 ? 151  LEU B CD1   1 
ATOM   5268 C CD2   . LEU B 1 151 ? 33.995  89.706  57.176 1.00 38.50 ? 151  LEU B CD2   1 
ATOM   5269 N N     . GLY B 1 152 ? 31.701  90.909  52.883 1.00 24.35 ? 152  GLY B N     1 
ATOM   5270 C CA    . GLY B 1 152 ? 31.095  91.048  51.555 1.00 24.47 ? 152  GLY B CA    1 
ATOM   5271 C C     . GLY B 1 152 ? 31.064  89.757  50.768 1.00 22.20 ? 152  GLY B C     1 
ATOM   5272 O O     . GLY B 1 152 ? 30.447  89.789  49.701 1.00 22.72 ? 152  GLY B O     1 
ATOM   5273 N N     . TRP B 1 153 ? 31.670  88.655  51.251 1.00 21.46 ? 153  TRP B N     1 
ATOM   5274 C CA    . TRP B 1 153 ? 31.693  87.395  50.480 1.00 21.74 ? 153  TRP B CA    1 
ATOM   5275 C C     . TRP B 1 153 ? 30.389  86.621  50.670 1.00 19.68 ? 153  TRP B C     1 
ATOM   5276 O O     . TRP B 1 153 ? 30.262  85.598  50.047 1.00 22.03 ? 153  TRP B O     1 
ATOM   5277 C CB    . TRP B 1 153 ? 32.921  86.530  50.782 1.00 26.39 ? 153  TRP B CB    1 
ATOM   5278 C CG    . TRP B 1 153 ? 33.139  86.143  52.194 1.00 33.81 ? 153  TRP B CG    1 
ATOM   5279 C CD1   . TRP B 1 153 ? 32.221  85.998  53.198 1.00 42.51 ? 153  TRP B CD1   1 
ATOM   5280 C CD2   . TRP B 1 153 ? 34.425  85.839  52.764 1.00 52.72 ? 153  TRP B CD2   1 
ATOM   5281 N NE1   . TRP B 1 153 ? 32.845  85.614  54.353 1.00 49.13 ? 153  TRP B NE1   1 
ATOM   5282 C CE2   . TRP B 1 153 ? 34.202  85.525  54.127 1.00 56.97 ? 153  TRP B CE2   1 
ATOM   5283 C CE3   . TRP B 1 153 ? 35.740  85.837  52.266 1.00 58.45 ? 153  TRP B CE3   1 
ATOM   5284 C CZ2   . TRP B 1 153 ? 35.258  85.219  54.997 1.00 65.28 ? 153  TRP B CZ2   1 
ATOM   5285 C CZ3   . TRP B 1 153 ? 36.776  85.504  53.121 1.00 64.65 ? 153  TRP B CZ3   1 
ATOM   5286 C CH2   . TRP B 1 153 ? 36.536  85.194  54.465 1.00 67.15 ? 153  TRP B CH2   1 
ATOM   5287 N N     . GLY B 1 154 ? 29.465  87.107  51.498 1.00 20.40 ? 154  GLY B N     1 
ATOM   5288 C CA    . GLY B 1 154 ? 28.185  86.426  51.755 1.00 21.20 ? 154  GLY B CA    1 
ATOM   5289 C C     . GLY B 1 154 ? 27.212  86.595  50.615 1.00 18.95 ? 154  GLY B C     1 
ATOM   5290 O O     . GLY B 1 154 ? 27.501  87.324  49.616 1.00 19.13 ? 154  GLY B O     1 
ATOM   5291 N N     . SER B 1 155 ? 26.066  85.955  50.748 1.00 19.14 ? 155  SER B N     1 
ATOM   5292 C CA    . SER B 1 155 ? 24.974  85.931  49.756 1.00 17.26 ? 155  SER B CA    1 
ATOM   5293 C C     . SER B 1 155 ? 23.926  87.006  50.064 1.00 19.69 ? 155  SER B C     1 
ATOM   5294 O O     . SER B 1 155 ? 23.382  87.032  51.201 1.00 18.29 ? 155  SER B O     1 
ATOM   5295 C CB    . SER B 1 155 ? 24.322  84.593  49.730 1.00 17.07 ? 155  SER B CB    1 
ATOM   5296 O OG    . SER B 1 155 ? 23.097  84.686  48.985 1.00 16.07 ? 155  SER B OG    1 
ATOM   5297 N N     . VAL B 1 156 ? 23.590  87.822  49.080 1.00 19.00 ? 156  VAL B N     1 
ATOM   5298 C CA    . VAL B 1 156 ? 22.434  88.751  49.183 1.00 17.72 ? 156  VAL B CA    1 
ATOM   5299 C C     . VAL B 1 156 ? 21.177  87.983  49.618 1.00 18.73 ? 156  VAL B C     1 
ATOM   5300 O O     . VAL B 1 156 ? 20.463  88.451  50.541 1.00 17.93 ? 156  VAL B O     1 
ATOM   5301 C CB    . VAL B 1 156 ? 22.180  89.488  47.885 1.00 16.86 ? 156  VAL B CB    1 
ATOM   5302 C CG1   . VAL B 1 156 ? 21.005  90.455  48.050 1.00 18.52 ? 156  VAL B CG1   1 
ATOM   5303 C CG2   . VAL B 1 156 ? 23.453  90.174  47.406 1.00 18.61 ? 156  VAL B CG2   1 
ATOM   5304 N N     . VAL B 1 157 ? 20.942  86.825  49.035 1.00 17.13 ? 157  VAL B N     1 
ATOM   5305 C CA    . VAL B 1 157 ? 19.789  85.951  49.367 1.00 17.91 ? 157  VAL B CA    1 
ATOM   5306 C C     . VAL B 1 157 ? 19.973  85.278  50.733 1.00 17.17 ? 157  VAL B C     1 
ATOM   5307 O O     . VAL B 1 157 ? 19.068  85.417  51.605 1.00 18.01 ? 157  VAL B O     1 
ATOM   5308 C CB    . VAL B 1 157 ? 19.566  84.907  48.258 1.00 17.33 ? 157  VAL B CB    1 
ATOM   5309 C CG1   . VAL B 1 157 ? 18.490  83.926  48.693 1.00 18.86 ? 157  VAL B CG1   1 
ATOM   5310 C CG2   . VAL B 1 157 ? 19.186  85.574  46.964 1.00 18.61 ? 157  VAL B CG2   1 
ATOM   5311 N N     . GLY B 1 158 ? 21.054  84.525  50.924 1.00 16.48 ? 158  GLY B N     1 
ATOM   5312 C CA    . GLY B 1 158 ? 21.235  83.661  52.096 1.00 15.20 ? 158  GLY B CA    1 
ATOM   5313 C C     . GLY B 1 158 ? 21.254  84.457  53.368 1.00 16.59 ? 158  GLY B C     1 
ATOM   5314 O O     . GLY B 1 158 ? 20.602  84.069  54.371 1.00 17.01 ? 158  GLY B O     1 
ATOM   5315 N N     . ASN B 1 159 ? 21.958  85.591  53.358 1.00 17.04 ? 159  ASN B N     1 
ATOM   5316 C CA    . ASN B 1 159 ? 22.011  86.453  54.548 1.00 16.22 ? 159  ASN B CA    1 
ATOM   5317 C C     . ASN B 1 159 ? 20.599  86.963  54.875 1.00 16.98 ? 159  ASN B C     1 
ATOM   5318 O O     . ASN B 1 159 ? 20.221  86.896  56.061 1.00 17.56 ? 159  ASN B O     1 
ATOM   5319 C CB    . ASN B 1 159 ? 22.998  87.580  54.309 1.00 17.26 ? 159  ASN B CB    1 
ATOM   5320 C CG    . ASN B 1 159 ? 23.000  88.558  55.451 1.00 17.88 ? 159  ASN B CG    1 
ATOM   5321 O OD1   . ASN B 1 159 ? 22.094  89.380  55.585 1.00 20.09 ? 159  ASN B OD1   1 
ATOM   5322 N ND2   . ASN B 1 159 ? 23.997  88.436  56.283 1.00 19.70 ? 159  ASN B ND2   1 
ATOM   5323 N N     . ALA B 1 160 ? 19.822  87.441  53.893 1.00 16.19 ? 160  ALA B N     1 
ATOM   5324 C CA    . ALA B 1 160 ? 18.491  87.992  54.158 1.00 18.34 ? 160  ALA B CA    1 
ATOM   5325 C C     . ALA B 1 160 ? 17.634  86.861  54.762 1.00 19.21 ? 160  ALA B C     1 
ATOM   5326 O O     . ALA B 1 160 ? 16.818  87.117  55.669 1.00 16.64 ? 160  ALA B O     1 
ATOM   5327 C CB    . ALA B 1 160 ? 17.917  88.539  52.860 1.00 18.43 ? 160  ALA B CB    1 
ATOM   5328 N N     . LEU B 1 161 ? 17.723  85.663  54.165 1.00 18.05 ? 161  LEU B N     1 
ATOM   5329 C CA    . LEU B 1 161 ? 16.882  84.535  54.605 1.00 17.66 ? 161  LEU B CA    1 
ATOM   5330 C C     . LEU B 1 161 ? 17.216  84.168  56.044 1.00 17.60 ? 161  LEU B C     1 
ATOM   5331 O O     . LEU B 1 161 ? 16.263  83.711  56.721 1.00 19.16 ? 161  LEU B O     1 
ATOM   5332 C CB    . LEU B 1 161 ? 17.047  83.318  53.686 1.00 17.25 ? 161  LEU B CB    1 
ATOM   5333 C CG    . LEU B 1 161 ? 16.508  83.474  52.277 1.00 16.99 ? 161  LEU B CG    1 
ATOM   5334 C CD1   . LEU B 1 161 ? 16.765  82.199  51.457 1.00 18.70 ? 161  LEU B CD1   1 
ATOM   5335 C CD2   . LEU B 1 161 ? 15.055  83.790  52.321 1.00 20.14 ? 161  LEU B CD2   1 
ATOM   5336 N N     . ASP B 1 162 ? 18.451  84.379  56.508 1.00 17.14 ? 162  ASP B N     1 
ATOM   5337 C CA    . ASP B 1 162 ? 18.799  84.083  57.916 1.00 16.75 ? 162  ASP B CA    1 
ATOM   5338 C C     . ASP B 1 162 ? 18.512  85.305  58.797 1.00 15.67 ? 162  ASP B C     1 
ATOM   5339 O O     . ASP B 1 162 ? 18.987  85.302  59.933 1.00 16.65 ? 162  ASP B O     1 
ATOM   5340 C CB    . ASP B 1 162 ? 20.208  83.539  58.055 1.00 16.98 ? 162  ASP B CB    1 
ATOM   5341 C CG    . ASP B 1 162 ? 20.358  82.425  59.091 1.00 19.81 ? 162  ASP B CG    1 
ATOM   5342 O OD1   . ASP B 1 162 ? 19.367  81.688  59.339 1.00 22.86 ? 162  ASP B OD1   1 
ATOM   5343 O OD2   . ASP B 1 162 ? 21.456  82.315  59.666 1.00 20.66 ? 162  ASP B OD2   1 
ATOM   5344 N N     . HIS B 1 163 ? 17.772  86.281  58.306 1.00 16.15 ? 163  HIS B N     1 
ATOM   5345 C CA    . HIS B 1 163 ? 17.396  87.534  59.042 1.00 16.40 ? 163  HIS B CA    1 
ATOM   5346 C C     . HIS B 1 163 ? 18.636  88.393  59.347 1.00 16.91 ? 163  HIS B C     1 
ATOM   5347 O O     . HIS B 1 163 ? 18.692  89.084  60.364 1.00 15.97 ? 163  HIS B O     1 
ATOM   5348 C CB    . HIS B 1 163 ? 16.578  87.213  60.287 1.00 18.66 ? 163  HIS B CB    1 
ATOM   5349 C CG    . HIS B 1 163 ? 15.314  86.462  60.028 1.00 16.79 ? 163  HIS B CG    1 
ATOM   5350 N ND1   . HIS B 1 163 ? 14.619  85.899  61.067 1.00 16.57 ? 163  HIS B ND1   1 
ATOM   5351 C CD2   . HIS B 1 163 ? 14.608  86.223  58.894 1.00 19.03 ? 163  HIS B CD2   1 
ATOM   5352 C CE1   . HIS B 1 163 ? 13.553  85.272  60.569 1.00 17.65 ? 163  HIS B CE1   1 
ATOM   5353 N NE2   . HIS B 1 163 ? 13.530  85.426  59.211 1.00 18.81 ? 163  HIS B NE2   1 
ATOM   5354 N N     . GLY B 1 164 ? 19.596  88.388  58.418 1.00 17.57 ? 164  GLY B N     1 
ATOM   5355 C CA    . GLY B 1 164 ? 20.832  89.153  58.521 1.00 17.39 ? 164  GLY B CA    1 
ATOM   5356 C C     . GLY B 1 164 ? 20.630  90.663  58.544 1.00 18.14 ? 164  GLY B C     1 
ATOM   5357 O O     . GLY B 1 164 ? 19.584  91.209  58.079 1.00 19.14 ? 164  GLY B O     1 
ATOM   5358 N N     . ILE B 1 165 ? 21.681  91.332  59.007 1.00 19.83 ? 165  ILE B N     1 
ATOM   5359 C CA    . ILE B 1 165 ? 21.643  92.802  59.156 1.00 21.20 ? 165  ILE B CA    1 
ATOM   5360 C C     . ILE B 1 165 ? 22.895  93.453  58.561 1.00 19.09 ? 165  ILE B C     1 
ATOM   5361 O O     . ILE B 1 165 ? 24.026  92.853  58.541 1.00 18.38 ? 165  ILE B O     1 
ATOM   5362 C CB    . ILE B 1 165 ? 21.467  93.143  60.629 1.00 24.28 ? 165  ILE B CB    1 
ATOM   5363 C CG1   . ILE B 1 165 ? 22.655  92.640  61.430 1.00 25.38 ? 165  ILE B CG1   1 
ATOM   5364 C CG2   . ILE B 1 165 ? 20.153  92.584  61.134 1.00 27.27 ? 165  ILE B CG2   1 
ATOM   5365 C CD1   . ILE B 1 165 ? 22.685  93.164  62.848 1.00 28.50 ? 165  ILE B CD1   1 
ATOM   5366 N N     . GLY B 1 166 ? 22.672  94.658  58.087 1.00 18.03 ? 166  GLY B N     1 
ATOM   5367 C CA    . GLY B 1 166 ? 23.736  95.621  57.726 1.00 18.28 ? 166  GLY B CA    1 
ATOM   5368 C C     . GLY B 1 166 ? 23.451  97.003  58.298 1.00 18.21 ? 166  GLY B C     1 
ATOM   5369 O O     . GLY B 1 166 ? 22.630  97.139  59.234 1.00 17.34 ? 166  GLY B O     1 
ATOM   5370 N N     . TYR B 1 167 ? 24.049  98.042  57.695 1.00 18.78 ? 167  TYR B N     1 
ATOM   5371 C CA    . TYR B 1 167 ? 24.423  99.258  58.437 1.00 19.14 ? 167  TYR B CA    1 
ATOM   5372 C C     . TYR B 1 167 ? 24.024  100.523 57.677 1.00 19.56 ? 167  TYR B C     1 
ATOM   5373 O O     . TYR B 1 167 ? 24.505  101.627 58.063 1.00 18.66 ? 167  TYR B O     1 
ATOM   5374 C CB    . TYR B 1 167 ? 25.910  99.111  58.776 1.00 17.87 ? 167  TYR B CB    1 
ATOM   5375 C CG    . TYR B 1 167 ? 26.186  97.824  59.487 1.00 17.13 ? 167  TYR B CG    1 
ATOM   5376 C CD1   . TYR B 1 167 ? 25.780  97.642  60.799 1.00 19.91 ? 167  TYR B CD1   1 
ATOM   5377 C CD2   . TYR B 1 167 ? 26.768  96.749  58.860 1.00 17.32 ? 167  TYR B CD2   1 
ATOM   5378 C CE1   . TYR B 1 167 ? 25.914  96.426  61.446 1.00 19.00 ? 167  TYR B CE1   1 
ATOM   5379 C CE2   . TYR B 1 167 ? 27.047  95.579  59.540 1.00 17.58 ? 167  TYR B CE2   1 
ATOM   5380 C CZ    . TYR B 1 167 ? 26.578  95.385  60.820 1.00 19.35 ? 167  TYR B CZ    1 
ATOM   5381 O OH    . TYR B 1 167 ? 26.794  94.188  61.456 1.00 20.94 ? 167  TYR B OH    1 
ATOM   5382 N N     . THR B 1 168 ? 23.139  100.427 56.682 1.00 17.85 ? 168  THR B N     1 
ATOM   5383 C CA    . THR B 1 168 ? 22.531  101.615 56.027 1.00 17.05 ? 168  THR B CA    1 
ATOM   5384 C C     . THR B 1 168 ? 21.077  101.719 56.461 1.00 17.26 ? 168  THR B C     1 
ATOM   5385 O O     . THR B 1 168 ? 20.607  100.872 57.214 1.00 16.89 ? 168  THR B O     1 
ATOM   5386 C CB    . THR B 1 168 ? 22.666  101.561 54.495 1.00 17.70 ? 168  THR B CB    1 
ATOM   5387 O OG1   . THR B 1 168 ? 21.645  100.776 53.840 1.00 17.77 ? 168  THR B OG1   1 
ATOM   5388 C CG2   . THR B 1 168 ? 24.032  101.050 54.085 1.00 19.05 ? 168  THR B CG2   1 
ATOM   5389 N N     . PRO B 1 169 ? 20.260  102.661 55.923 1.00 17.76 ? 169  PRO B N     1 
ATOM   5390 C CA    . PRO B 1 169 ? 18.826  102.616 56.181 1.00 18.58 ? 169  PRO B CA    1 
ATOM   5391 C C     . PRO B 1 169 ? 18.142  101.317 55.706 1.00 20.55 ? 169  PRO B C     1 
ATOM   5392 O O     . PRO B 1 169 ? 17.047  100.987 56.146 1.00 17.48 ? 169  PRO B O     1 
ATOM   5393 C CB    . PRO B 1 169 ? 18.265  103.872 55.477 1.00 17.61 ? 169  PRO B CB    1 
ATOM   5394 C CG    . PRO B 1 169 ? 19.516  104.792 55.387 1.00 18.81 ? 169  PRO B CG    1 
ATOM   5395 C CD    . PRO B 1 169 ? 20.658  103.819 55.111 1.00 18.61 ? 169  PRO B CD    1 
ATOM   5396 N N     . TYR B 1 170 ? 18.802  100.542 54.840 1.00 18.92 ? 170  TYR B N     1 
ATOM   5397 C CA    . TYR B 1 170 ? 18.238  99.269  54.299 1.00 18.87 ? 170  TYR B CA    1 
ATOM   5398 C C     . TYR B 1 170 ? 18.864  98.075  55.041 1.00 18.93 ? 170  TYR B C     1 
ATOM   5399 O O     . TYR B 1 170 ? 18.975  96.922  54.502 1.00 18.07 ? 170  TYR B O     1 
ATOM   5400 C CB    . TYR B 1 170 ? 18.461  99.250  52.785 1.00 17.97 ? 170  TYR B CB    1 
ATOM   5401 C CG    . TYR B 1 170 ? 17.491  100.039 51.946 1.00 17.15 ? 170  TYR B CG    1 
ATOM   5402 C CD1   . TYR B 1 170 ? 17.211  101.391 52.162 1.00 21.00 ? 170  TYR B CD1   1 
ATOM   5403 C CD2   . TYR B 1 170 ? 16.844  99.435  50.871 1.00 17.32 ? 170  TYR B CD2   1 
ATOM   5404 C CE1   . TYR B 1 170 ? 16.288  102.087 51.374 1.00 20.35 ? 170  TYR B CE1   1 
ATOM   5405 C CE2   . TYR B 1 170 ? 15.969  100.145 50.049 1.00 18.02 ? 170  TYR B CE2   1 
ATOM   5406 C CZ    . TYR B 1 170 ? 15.658  101.455 50.307 1.00 16.78 ? 170  TYR B CZ    1 
ATOM   5407 O OH    . TYR B 1 170 ? 14.767  102.092 49.476 1.00 17.68 ? 170  TYR B OH    1 
ATOM   5408 N N     . GLY B 1 171 ? 19.230  98.311  56.310 1.00 16.26 ? 171  GLY B N     1 
ATOM   5409 C CA    . GLY B 1 171 ? 19.973  97.343  57.126 1.00 18.25 ? 171  GLY B CA    1 
ATOM   5410 C C     . GLY B 1 171 ? 19.159  96.121  57.558 1.00 18.75 ? 171  GLY B C     1 
ATOM   5411 O O     . GLY B 1 171 ? 19.773  95.104  57.990 1.00 21.00 ? 171  GLY B O     1 
ATOM   5412 N N     . ASP B 1 172 ? 17.843  96.159  57.468 1.00 19.08 ? 172  ASP B N     1 
ATOM   5413 C CA    . ASP B 1 172 ? 17.051  94.945  57.789 1.00 20.42 ? 172  ASP B CA    1 
ATOM   5414 C C     . ASP B 1 172 ? 16.827  94.155  56.502 1.00 16.38 ? 172  ASP B C     1 
ATOM   5415 O O     . ASP B 1 172 ? 15.906  94.492  55.710 1.00 16.17 ? 172  ASP B O     1 
ATOM   5416 C CB    . ASP B 1 172 ? 15.723  95.289  58.468 1.00 21.58 ? 172  ASP B CB    1 
ATOM   5417 C CG    . ASP B 1 172 ? 14.941  94.064  58.918 1.00 22.68 ? 172  ASP B CG    1 
ATOM   5418 O OD1   . ASP B 1 172 ? 15.145  92.943  58.350 1.00 19.76 ? 172  ASP B OD1   1 
ATOM   5419 O OD2   . ASP B 1 172 ? 14.099  94.289  59.801 1.00 22.81 ? 172  ASP B OD2   1 
ATOM   5420 N N     . HIS B 1 173 ? 17.703  93.215  56.238 1.00 15.83 ? 173  HIS B N     1 
ATOM   5421 C CA    . HIS B 1 173 ? 17.840  92.673  54.862 1.00 17.15 ? 173  HIS B CA    1 
ATOM   5422 C C     . HIS B 1 173 ? 16.564  91.968  54.451 1.00 18.67 ? 173  HIS B C     1 
ATOM   5423 O O     . HIS B 1 173 ? 16.042  92.211  53.325 1.00 17.77 ? 173  HIS B O     1 
ATOM   5424 C CB    . HIS B 1 173 ? 19.044  91.769  54.761 1.00 18.53 ? 173  HIS B CB    1 
ATOM   5425 C CG    . HIS B 1 173 ? 20.338  92.505  54.870 1.00 19.25 ? 173  HIS B CG    1 
ATOM   5426 N ND1   . HIS B 1 173 ? 21.497  91.837  55.070 1.00 19.37 ? 173  HIS B ND1   1 
ATOM   5427 C CD2   . HIS B 1 173 ? 20.637  93.826  54.834 1.00 20.00 ? 173  HIS B CD2   1 
ATOM   5428 C CE1   . HIS B 1 173 ? 22.495  92.706  55.118 1.00 22.02 ? 173  HIS B CE1   1 
ATOM   5429 N NE2   . HIS B 1 173 ? 22.000  93.931  54.946 1.00 22.01 ? 173  HIS B NE2   1 
ATOM   5430 N N     . PHE B 1 174 ? 16.034  91.117  55.330 1.00 17.83 ? 174  PHE B N     1 
ATOM   5431 C CA    . PHE B 1 174 ? 14.801  90.415  54.965 1.00 16.31 ? 174  PHE B CA    1 
ATOM   5432 C C     . PHE B 1 174 ? 13.633  91.409  54.780 1.00 16.30 ? 174  PHE B C     1 
ATOM   5433 O O     . PHE B 1 174 ? 12.810  91.154  53.916 1.00 16.73 ? 174  PHE B O     1 
ATOM   5434 C CB    . PHE B 1 174 ? 14.448  89.312  55.957 1.00 16.96 ? 174  PHE B CB    1 
ATOM   5435 C CG    . PHE B 1 174 ? 13.374  88.447  55.343 1.00 17.18 ? 174  PHE B CG    1 
ATOM   5436 C CD1   . PHE B 1 174 ? 13.666  87.648  54.232 1.00 17.83 ? 174  PHE B CD1   1 
ATOM   5437 C CD2   . PHE B 1 174 ? 12.071  88.481  55.790 1.00 17.88 ? 174  PHE B CD2   1 
ATOM   5438 C CE1   . PHE B 1 174 ? 12.682  86.912  53.579 1.00 17.76 ? 174  PHE B CE1   1 
ATOM   5439 C CE2   . PHE B 1 174 ? 11.089  87.726  55.143 1.00 18.02 ? 174  PHE B CE2   1 
ATOM   5440 C CZ    . PHE B 1 174 ? 11.385  86.935  54.047 1.00 18.13 ? 174  PHE B CZ    1 
ATOM   5441 N N     . ALA B 1 175 ? 13.537  92.517  55.542 1.00 15.84 ? 175  ALA B N     1 
ATOM   5442 C CA    . ALA B 1 175 ? 12.458  93.503  55.397 1.00 16.22 ? 175  ALA B CA    1 
ATOM   5443 C C     . ALA B 1 175 ? 12.510  94.128  53.994 1.00 17.33 ? 175  ALA B C     1 
ATOM   5444 O O     . ALA B 1 175 ? 11.460  94.540  53.501 1.00 17.49 ? 175  ALA B O     1 
ATOM   5445 C CB    . ALA B 1 175 ? 12.524  94.580  56.476 1.00 18.43 ? 175  ALA B CB    1 
ATOM   5446 N N     . MET B 1 176 ? 13.668  94.155  53.348 1.00 15.75 ? 176  MET B N     1 
ATOM   5447 C CA    . MET B 1 176 ? 13.825  94.787  52.005 1.00 16.34 ? 176  MET B CA    1 
ATOM   5448 C C     . MET B 1 176 ? 13.507  93.774  50.883 1.00 18.90 ? 176  MET B C     1 
ATOM   5449 O O     . MET B 1 176 ? 13.441  94.187  49.684 1.00 16.91 ? 176  MET B O     1 
ATOM   5450 C CB    . MET B 1 176 ? 15.233  95.373  51.870 1.00 17.35 ? 176  MET B CB    1 
ATOM   5451 C CG    . MET B 1 176 ? 15.589  96.453  52.928 1.00 19.72 ? 176  MET B CG    1 
ATOM   5452 S SD    . MET B 1 176 ? 14.422  97.852  52.906 1.00 26.69 ? 176  MET B SD    1 
ATOM   5453 C CE    . MET B 1 176 ? 13.446  97.434  54.331 1.00 28.47 ? 176  MET B CE    1 
ATOM   5454 N N     . GLN B 1 177 ? 13.177  92.523  51.245 1.00 19.86 ? 177  GLN B N     1 
ATOM   5455 C CA    . GLN B 1 177 ? 12.896  91.447  50.254 1.00 19.16 ? 177  GLN B CA    1 
ATOM   5456 C C     . GLN B 1 177 ? 11.565  91.724  49.589 1.00 16.49 ? 177  GLN B C     1 
ATOM   5457 O O     . GLN B 1 177 ? 10.625  92.292  50.207 1.00 18.43 ? 177  GLN B O     1 
ATOM   5458 C CB    . GLN B 1 177 ? 12.988  90.062  50.906 1.00 20.54 ? 177  GLN B CB    1 
ATOM   5459 C CG    . GLN B 1 177 ? 12.601  88.909  50.008 1.00 18.86 ? 177  GLN B CG    1 
ATOM   5460 C CD    . GLN B 1 177 ? 11.134  88.558  50.076 1.00 18.42 ? 177  GLN B CD    1 
ATOM   5461 O OE1   . GLN B 1 177 ? 10.459  88.825  51.059 1.00 18.30 ? 177  GLN B OE1   1 
ATOM   5462 N NE2   . GLN B 1 177 ? 10.596  88.012  48.992 1.00 18.93 ? 177  GLN B NE2   1 
ATOM   5463 N N     . CYS B 1 178 ? 11.474  91.442  48.305 1.00 16.26 ? 178  CYS B N     1 
ATOM   5464 C CA    . CYS B 1 178 ? 10.215  91.606  47.570 1.00 16.21 ? 178  CYS B CA    1 
ATOM   5465 C C     . CYS B 1 178 ? 10.172  90.603  46.416 1.00 17.15 ? 178  CYS B C     1 
ATOM   5466 O O     . CYS B 1 178 ? 10.887  90.820  45.430 1.00 17.70 ? 178  CYS B O     1 
ATOM   5467 C CB    . CYS B 1 178 ? 10.088  93.056  47.104 1.00 17.63 ? 178  CYS B CB    1 
ATOM   5468 S SG    . CYS B 1 178 ? 8.480   93.448  46.390 1.00 18.01 ? 178  CYS B SG    1 
ATOM   5469 N N     . GLY B 1 179 ? 9.299   89.605  46.519 1.00 15.96 ? 179  GLY B N     1 
ATOM   5470 C CA    . GLY B 1 179 ? 9.150   88.522  45.538 1.00 16.49 ? 179  GLY B CA    1 
ATOM   5471 C C     . GLY B 1 179 ? 10.218  87.445  45.729 1.00 16.37 ? 179  GLY B C     1 
ATOM   5472 O O     . GLY B 1 179 ? 11.402  87.751  46.010 1.00 17.13 ? 179  GLY B O     1 
ATOM   5473 N N     . MET B 1 180 ? 9.838   86.185  45.611 1.00 15.48 ? 180  MET B N     1 
ATOM   5474 C CA    . MET B 1 180 ? 10.829  85.094  45.618 1.00 15.80 ? 180  MET B CA    1 
ATOM   5475 C C     . MET B 1 180 ? 10.278  83.929  44.818 1.00 15.67 ? 180  MET B C     1 
ATOM   5476 O O     . MET B 1 180 ? 9.046   83.854  44.628 1.00 19.39 ? 180  MET B O     1 
ATOM   5477 C CB    . MET B 1 180 ? 11.226  84.675  47.053 1.00 17.38 ? 180  MET B CB    1 
ATOM   5478 C CG    . MET B 1 180 ? 10.098  84.181  47.892 1.00 19.01 ? 180  MET B CG    1 
ATOM   5479 S SD    . MET B 1 180 ? 10.691  83.348  49.420 1.00 19.15 ? 180  MET B SD    1 
ATOM   5480 C CE    . MET B 1 180 ? 11.554  84.657  50.283 1.00 18.73 ? 180  MET B CE    1 
ATOM   5481 N N     . GLU B 1 181 ? 11.202  83.138  44.278 1.00 16.49 ? 181  GLU B N     1 
ATOM   5482 C CA    . GLU B 1 181 ? 10.915  81.836  43.661 1.00 16.50 ? 181  GLU B CA    1 
ATOM   5483 C C     . GLU B 1 181 ? 11.418  80.769  44.625 1.00 17.57 ? 181  GLU B C     1 
ATOM   5484 O O     . GLU B 1 181 ? 12.515  80.926  45.181 1.00 16.86 ? 181  GLU B O     1 
ATOM   5485 C CB    . GLU B 1 181 ? 11.592  81.734  42.293 1.00 16.71 ? 181  GLU B CB    1 
ATOM   5486 C CG    . GLU B 1 181 ? 11.294  80.416  41.634 1.00 16.53 ? 181  GLU B CG    1 
ATOM   5487 C CD    . GLU B 1 181 ? 12.017  80.349  40.297 1.00 18.88 ? 181  GLU B CD    1 
ATOM   5488 O OE1   . GLU B 1 181 ? 13.207  79.918  40.319 1.00 20.21 ? 181  GLU B OE1   1 
ATOM   5489 O OE2   . GLU B 1 181 ? 11.411  80.851  39.312 1.00 20.02 ? 181  GLU B OE2   1 
ATOM   5490 N N     . VAL B 1 182 ? 10.576  79.781  44.890 1.00 17.00 ? 182  VAL B N     1 
ATOM   5491 C CA    . VAL B 1 182 ? 10.841  78.720  45.881 1.00 16.70 ? 182  VAL B CA    1 
ATOM   5492 C C     . VAL B 1 182 ? 10.593  77.362  45.219 1.00 16.63 ? 182  VAL B C     1 
ATOM   5493 O O     . VAL B 1 182 ? 9.518   77.138  44.606 1.00 17.38 ? 182  VAL B O     1 
ATOM   5494 C CB    . VAL B 1 182 ? 10.003  78.884  47.156 1.00 18.07 ? 182  VAL B CB    1 
ATOM   5495 C CG1   . VAL B 1 182 ? 10.476  77.904  48.207 1.00 20.08 ? 182  VAL B CG1   1 
ATOM   5496 C CG2   . VAL B 1 182 ? 10.075  80.322  47.667 1.00 21.20 ? 182  VAL B CG2   1 
ATOM   5497 N N     . VAL B 1 183 ? 11.566  76.487  45.395 1.00 17.90 ? 183  VAL B N     1 
ATOM   5498 C CA    . VAL B 1 183 ? 11.386  75.052  45.151 1.00 17.79 ? 183  VAL B CA    1 
ATOM   5499 C C     . VAL B 1 183 ? 10.855  74.441  46.452 1.00 19.09 ? 183  VAL B C     1 
ATOM   5500 O O     . VAL B 1 183 ? 11.586  74.408  47.432 1.00 20.14 ? 183  VAL B O     1 
ATOM   5501 C CB    . VAL B 1 183 ? 12.651  74.384  44.608 1.00 17.12 ? 183  VAL B CB    1 
ATOM   5502 C CG1   . VAL B 1 183 ? 12.390  72.895  44.448 1.00 19.15 ? 183  VAL B CG1   1 
ATOM   5503 C CG2   . VAL B 1 183 ? 13.077  75.015  43.276 1.00 17.17 ? 183  VAL B CG2   1 
ATOM   5504 N N     . LEU B 1 184 ? 9.596   74.013  46.428 1.00 19.06 ? 184  LEU B N     1 
ATOM   5505 C CA    . LEU B 1 184 ? 8.921   73.420  47.606 1.00 18.17 ? 184  LEU B CA    1 
ATOM   5506 C C     . LEU B 1 184 ? 9.557   72.049  47.812 1.00 19.17 ? 184  LEU B C     1 
ATOM   5507 O O     . LEU B 1 184 ? 10.243  71.508  46.940 1.00 17.66 ? 184  LEU B O     1 
ATOM   5508 C CB    . LEU B 1 184 ? 7.412   73.362  47.389 1.00 18.91 ? 184  LEU B CB    1 
ATOM   5509 C CG    . LEU B 1 184 ? 6.714   74.708  47.216 1.00 20.65 ? 184  LEU B CG    1 
ATOM   5510 C CD1   . LEU B 1 184 ? 5.219   74.506  46.983 1.00 24.41 ? 184  LEU B CD1   1 
ATOM   5511 C CD2   . LEU B 1 184 ? 6.945   75.573  48.427 1.00 19.99 ? 184  LEU B CD2   1 
ATOM   5512 N N     . PRO B 1 185 ? 9.383   71.461  48.998 1.00 17.96 ? 185  PRO B N     1 
ATOM   5513 C CA    . PRO B 1 185 ? 10.038  70.200  49.310 1.00 20.12 ? 185  PRO B CA    1 
ATOM   5514 C C     . PRO B 1 185 ? 9.573   69.017  48.431 1.00 21.34 ? 185  PRO B C     1 
ATOM   5515 O O     . PRO B 1 185 ? 10.240  68.000  48.511 1.00 20.12 ? 185  PRO B O     1 
ATOM   5516 C CB    . PRO B 1 185 ? 9.712   69.957  50.797 1.00 20.06 ? 185  PRO B CB    1 
ATOM   5517 C CG    . PRO B 1 185 ? 9.279   71.339  51.287 1.00 18.94 ? 185  PRO B CG    1 
ATOM   5518 C CD    . PRO B 1 185 ? 8.609   72.001  50.110 1.00 18.86 ? 185  PRO B CD    1 
ATOM   5519 N N     . ASN B 1 186 ? 8.490   69.153  47.660 1.00 19.42 ? 186  ASN B N     1 
ATOM   5520 C CA    . ASN B 1 186 ? 8.042   68.113  46.693 1.00 23.34 ? 186  ASN B CA    1 
ATOM   5521 C C     . ASN B 1 186 ? 8.676   68.314  45.321 1.00 23.63 ? 186  ASN B C     1 
ATOM   5522 O O     . ASN B 1 186 ? 8.344   67.545  44.420 1.00 25.09 ? 186  ASN B O     1 
ATOM   5523 C CB    . ASN B 1 186 ? 6.513   68.042  46.597 1.00 24.41 ? 186  ASN B CB    1 
ATOM   5524 C CG    . ASN B 1 186 ? 5.898   69.339  46.103 1.00 26.35 ? 186  ASN B CG    1 
ATOM   5525 O OD1   . ASN B 1 186 ? 6.616   70.317  45.884 1.00 21.76 ? 186  ASN B OD1   1 
ATOM   5526 N ND2   . ASN B 1 186 ? 4.584   69.346  45.928 1.00 26.69 ? 186  ASN B ND2   1 
ATOM   5527 N N     . GLY B 1 187 ? 9.547   69.303  45.163 1.00 20.54 ? 187  GLY B N     1 
ATOM   5528 C CA    . GLY B 1 187 ? 10.203  69.633  43.893 1.00 20.64 ? 187  GLY B CA    1 
ATOM   5529 C C     . GLY B 1 187 ? 9.390   70.549  42.979 1.00 19.83 ? 187  GLY B C     1 
ATOM   5530 O O     . GLY B 1 187 ? 9.901   70.834  41.889 1.00 22.15 ? 187  GLY B O     1 
ATOM   5531 N N     . GLU B 1 188 ? 8.214   71.011  43.381 1.00 20.02 ? 188  GLU B N     1 
ATOM   5532 C CA    . GLU B 1 188 ? 7.421   71.977  42.574 1.00 20.97 ? 188  GLU B CA    1 
ATOM   5533 C C     . GLU B 1 188 ? 7.939   73.396  42.820 1.00 20.98 ? 188  GLU B C     1 
ATOM   5534 O O     . GLU B 1 188 ? 8.436   73.701  43.945 1.00 22.46 ? 188  GLU B O     1 
ATOM   5535 C CB    . GLU B 1 188 ? 5.955   71.858  42.927 1.00 23.71 ? 188  GLU B CB    1 
ATOM   5536 C CG    . GLU B 1 188 ? 5.393   70.478  42.564 1.00 25.47 ? 188  GLU B CG    1 
ATOM   5537 C CD    . GLU B 1 188 ? 5.405   70.222  41.088 1.00 28.53 ? 188  GLU B CD    1 
ATOM   5538 O OE1   . GLU B 1 188 ? 4.719   71.018  40.399 1.00 31.66 ? 188  GLU B OE1   1 
ATOM   5539 O OE2   . GLU B 1 188 ? 6.223   69.384  40.639 1.00 29.98 ? 188  GLU B OE2   1 
ATOM   5540 N N     . VAL B 1 189 ? 7.809   74.256  41.827 1.00 17.96 ? 189  VAL B N     1 
ATOM   5541 C CA    . VAL B 1 189 ? 8.299   75.649  41.902 1.00 18.85 ? 189  VAL B CA    1 
ATOM   5542 C C     . VAL B 1 189 ? 7.096   76.614  42.021 1.00 18.38 ? 189  VAL B C     1 
ATOM   5543 O O     . VAL B 1 189 ? 6.084   76.424  41.325 1.00 18.32 ? 189  VAL B O     1 
ATOM   5544 C CB    . VAL B 1 189 ? 9.303   75.987  40.777 1.00 20.34 ? 189  VAL B CB    1 
ATOM   5545 C CG1   . VAL B 1 189 ? 8.745   75.805  39.401 1.00 24.36 ? 189  VAL B CG1   1 
ATOM   5546 C CG2   . VAL B 1 189 ? 9.822   77.401  40.938 1.00 22.46 ? 189  VAL B CG2   1 
ATOM   5547 N N     . VAL B 1 190 ? 7.177   77.570  42.962 1.00 16.83 ? 190  VAL B N     1 
ATOM   5548 C CA    . VAL B 1 190 ? 6.185   78.669  43.127 1.00 16.82 ? 190  VAL B CA    1 
ATOM   5549 C C     . VAL B 1 190 ? 6.908   80.013  43.067 1.00 17.76 ? 190  VAL B C     1 
ATOM   5550 O O     . VAL B 1 190 ? 8.086   80.062  43.439 1.00 17.85 ? 190  VAL B O     1 
ATOM   5551 C CB    . VAL B 1 190 ? 5.421   78.553  44.459 1.00 20.25 ? 190  VAL B CB    1 
ATOM   5552 C CG1   . VAL B 1 190 ? 4.669   77.248  44.551 1.00 24.28 ? 190  VAL B CG1   1 
ATOM   5553 C CG2   . VAL B 1 190 ? 6.361   78.676  45.637 1.00 22.07 ? 190  VAL B CG2   1 
ATOM   5554 N N     . ARG B 1 191 ? 6.174   81.050  42.676 1.00 17.64 ? 191  ARG B N     1 
ATOM   5555 C CA    . ARG B 1 191 ? 6.617   82.447  42.778 1.00 17.26 ? 191  ARG B CA    1 
ATOM   5556 C C     . ARG B 1 191 ? 5.609   83.189  43.659 1.00 18.05 ? 191  ARG B C     1 
ATOM   5557 O O     . ARG B 1 191 ? 4.392   83.033  43.506 1.00 16.13 ? 191  ARG B O     1 
ATOM   5558 C CB    . ARG B 1 191 ? 6.791   83.055  41.396 1.00 17.92 ? 191  ARG B CB    1 
ATOM   5559 C CG    . ARG B 1 191 ? 7.970   82.463  40.634 1.00 19.70 ? 191  ARG B CG    1 
ATOM   5560 C CD    . ARG B 1 191 ? 8.073   83.092  39.264 1.00 20.59 ? 191  ARG B CD    1 
ATOM   5561 N NE    . ARG B 1 191 ? 9.245   82.517  38.645 1.00 21.82 ? 191  ARG B NE    1 
ATOM   5562 C CZ    . ARG B 1 191 ? 9.522   82.559  37.357 1.00 22.29 ? 191  ARG B CZ    1 
ATOM   5563 N NH1   . ARG B 1 191 ? 8.706   83.157  36.511 1.00 21.62 ? 191  ARG B NH1   1 
ATOM   5564 N NH2   . ARG B 1 191 ? 10.586  81.913  36.914 1.00 23.14 ? 191  ARG B NH2   1 
ATOM   5565 N N     . THR B 1 192 ? 6.129   83.915  44.635 1.00 18.24 ? 192  THR B N     1 
ATOM   5566 C CA    . THR B 1 192 ? 5.290   84.649  45.593 1.00 16.93 ? 192  THR B CA    1 
ATOM   5567 C C     . THR B 1 192 ? 4.873   85.989  45.015 1.00 17.57 ? 192  THR B C     1 
ATOM   5568 O O     . THR B 1 192 ? 5.503   86.508  44.106 1.00 17.43 ? 192  THR B O     1 
ATOM   5569 C CB    . THR B 1 192 ? 6.014   84.834  46.932 1.00 16.82 ? 192  THR B CB    1 
ATOM   5570 O OG1   . THR B 1 192 ? 7.150   85.684  46.736 1.00 15.79 ? 192  THR B OG1   1 
ATOM   5571 C CG2   . THR B 1 192 ? 6.463   83.516  47.533 1.00 17.90 ? 192  THR B CG2   1 
ATOM   5572 N N     . GLY B 1 193 ? 3.882   86.580  45.666 1.00 17.18 ? 193  GLY B N     1 
ATOM   5573 C CA    . GLY B 1 193 ? 3.467   87.954  45.419 1.00 18.59 ? 193  GLY B CA    1 
ATOM   5574 C C     . GLY B 1 193 ? 3.014   88.124  43.996 1.00 16.61 ? 193  GLY B C     1 
ATOM   5575 O O     . GLY B 1 193 ? 2.277   87.249  43.485 1.00 15.68 ? 193  GLY B O     1 
ATOM   5576 N N     . MET B 1 194 ? 3.453   89.201  43.369 1.00 16.85 ? 194  MET B N     1 
ATOM   5577 C CA    . MET B 1 194 ? 2.982   89.503  42.005 1.00 17.53 ? 194  MET B CA    1 
ATOM   5578 C C     . MET B 1 194 ? 3.643   88.543  41.008 1.00 18.66 ? 194  MET B C     1 
ATOM   5579 O O     . MET B 1 194 ? 3.147   88.492  39.850 1.00 19.07 ? 194  MET B O     1 
ATOM   5580 C CB    . MET B 1 194 ? 3.283   90.965  41.677 1.00 18.15 ? 194  MET B CB    1 
ATOM   5581 C CG    . MET B 1 194 ? 2.478   91.952  42.553 1.00 20.27 ? 194  MET B CG    1 
ATOM   5582 S SD    . MET B 1 194 ? 0.716   91.675  42.636 1.00 20.75 ? 194  MET B SD    1 
ATOM   5583 C CE    . MET B 1 194 ? 0.192   91.904  40.947 1.00 21.03 ? 194  MET B CE    1 
ATOM   5584 N N     . GLY B 1 195 ? 4.611   87.726  41.457 1.00 17.41 ? 195  GLY B N     1 
ATOM   5585 C CA    . GLY B 1 195 ? 5.282   86.759  40.572 1.00 16.08 ? 195  GLY B CA    1 
ATOM   5586 C C     . GLY B 1 195 ? 4.324   85.652  40.166 1.00 17.98 ? 195  GLY B C     1 
ATOM   5587 O O     . GLY B 1 195 ? 4.609   84.963  39.174 1.00 18.80 ? 195  GLY B O     1 
ATOM   5588 N N     . ALA B 1 196 ? 3.249   85.454  40.935 1.00 17.85 ? 196  ALA B N     1 
ATOM   5589 C CA    . ALA B 1 196 ? 2.194   84.466  40.630 1.00 17.30 ? 196  ALA B CA    1 
ATOM   5590 C C     . ALA B 1 196 ? 1.276   84.942  39.483 1.00 19.39 ? 196  ALA B C     1 
ATOM   5591 O O     . ALA B 1 196 ? 0.520   84.064  38.978 1.00 18.63 ? 196  ALA B O     1 
ATOM   5592 C CB    . ALA B 1 196 ? 1.423   84.143  41.877 1.00 16.24 ? 196  ALA B CB    1 
ATOM   5593 N N     . MET B 1 197 ? 1.348   86.210  39.071 1.00 19.63 ? 197  MET B N     1 
ATOM   5594 C CA    . MET B 1 197 ? 0.531   86.798  37.954 1.00 19.64 ? 197  MET B CA    1 
ATOM   5595 C C     . MET B 1 197 ? 1.316   86.595  36.662 1.00 21.15 ? 197  MET B C     1 
ATOM   5596 O O     . MET B 1 197 ? 2.354   87.210  36.474 1.00 20.90 ? 197  MET B O     1 
ATOM   5597 C CB    . MET B 1 197 ? 0.278   88.292  38.200 1.00 19.94 ? 197  MET B CB    1 
ATOM   5598 C CG    . MET B 1 197 ? -0.253  89.144  37.060 1.00 22.68 ? 197  MET B CG    1 
ATOM   5599 S SD    . MET B 1 197 ? -1.707  88.527  36.381 1.00 29.68 ? 197  MET B SD    1 
ATOM   5600 C CE    . MET B 1 197 ? -2.835  88.738  37.764 1.00 27.84 ? 197  MET B CE    1 
ATOM   5601 N N     . PRO B 1 198 ? 0.877   85.739  35.709 1.00 21.18 ? 198  PRO B N     1 
ATOM   5602 C CA    . PRO B 1 198 ? 1.603   85.627  34.436 1.00 21.81 ? 198  PRO B CA    1 
ATOM   5603 C C     . PRO B 1 198 ? 1.667   86.983  33.737 1.00 21.31 ? 198  PRO B C     1 
ATOM   5604 O O     . PRO B 1 198 ? 0.662   87.677  33.733 1.00 20.96 ? 198  PRO B O     1 
ATOM   5605 C CB    . PRO B 1 198 ? 0.741   84.676  33.577 1.00 24.32 ? 198  PRO B CB    1 
ATOM   5606 C CG    . PRO B 1 198 ? -0.112  83.953  34.584 1.00 25.60 ? 198  PRO B CG    1 
ATOM   5607 C CD    . PRO B 1 198 ? -0.345  84.924  35.740 1.00 23.32 ? 198  PRO B CD    1 
ATOM   5608 N N     . GLY B 1 199 ? 2.838   87.333  33.216 1.00 22.24 ? 199  GLY B N     1 
ATOM   5609 C CA    . GLY B 1 199 ? 3.080   88.598  32.496 1.00 22.07 ? 199  GLY B CA    1 
ATOM   5610 C C     . GLY B 1 199 ? 3.082   89.821  33.394 1.00 23.97 ? 199  GLY B C     1 
ATOM   5611 O O     . GLY B 1 199 ? 2.925   90.926  32.860 1.00 22.47 ? 199  GLY B O     1 
ATOM   5612 N N     . ASN B 1 200 ? 3.259   89.657  34.714 1.00 20.01 ? 200  ASN B N     1 
ATOM   5613 C CA    . ASN B 1 200 ? 3.308   90.809  35.643 1.00 21.27 ? 200  ASN B CA    1 
ATOM   5614 C C     . ASN B 1 200 ? 4.513   91.693  35.329 1.00 20.68 ? 200  ASN B C     1 
ATOM   5615 O O     . ASN B 1 200 ? 5.547   91.191  34.801 1.00 21.25 ? 200  ASN B O     1 
ATOM   5616 C CB    . ASN B 1 200 ? 3.415   90.356  37.103 1.00 20.73 ? 200  ASN B CB    1 
ATOM   5617 C CG    . ASN B 1 200 ? 4.778   89.835  37.452 1.00 20.55 ? 200  ASN B CG    1 
ATOM   5618 O OD1   . ASN B 1 200 ? 5.654   90.607  37.877 1.00 21.95 ? 200  ASN B OD1   1 
ATOM   5619 N ND2   . ASN B 1 200 ? 4.976   88.528  37.259 1.00 20.33 ? 200  ASN B ND2   1 
ATOM   5620 N N     . ASN B 1 201 ? 4.457   92.928  35.806 1.00 19.71 ? 201  ASN B N     1 
ATOM   5621 C CA    . ASN B 1 201 ? 5.607   93.848  35.809 1.00 22.41 ? 201  ASN B CA    1 
ATOM   5622 C C     . ASN B 1 201 ? 5.755   94.411  37.223 1.00 23.55 ? 201  ASN B C     1 
ATOM   5623 O O     . ASN B 1 201 ? 6.295   95.507  37.346 1.00 23.15 ? 201  ASN B O     1 
ATOM   5624 C CB    . ASN B 1 201 ? 5.473   94.955  34.745 1.00 21.74 ? 201  ASN B CB    1 
ATOM   5625 C CG    . ASN B 1 201 ? 4.200   95.785  34.792 1.00 24.65 ? 201  ASN B CG    1 
ATOM   5626 O OD1   . ASN B 1 201 ? 3.272   95.579  35.605 1.00 24.79 ? 201  ASN B OD1   1 
ATOM   5627 N ND2   . ASN B 1 201 ? 4.071   96.656  33.794 1.00 26.23 ? 201  ASN B ND2   1 
ATOM   5628 N N     . THR B 1 202 ? 5.418   93.634  38.250 1.00 21.81 ? 202  THR B N     1 
ATOM   5629 C CA    . THR B 1 202 ? 5.331   94.164  39.625 1.00 21.40 ? 202  THR B CA    1 
ATOM   5630 C C     . THR B 1 202 ? 5.947   93.216  40.659 1.00 21.23 ? 202  THR B C     1 
ATOM   5631 O O     . THR B 1 202 ? 5.851   93.573  41.853 1.00 19.24 ? 202  THR B O     1 
ATOM   5632 C CB    . THR B 1 202 ? 3.874   94.477  39.960 1.00 21.75 ? 202  THR B CB    1 
ATOM   5633 O OG1   . THR B 1 202 ? 3.067   93.385  39.518 1.00 20.50 ? 202  THR B OG1   1 
ATOM   5634 C CG2   . THR B 1 202 ? 3.377   95.765  39.310 1.00 22.96 ? 202  THR B CG2   1 
ATOM   5635 N N     . TRP B 1 203 ? 6.627   92.139  40.257 1.00 17.81 ? 203  TRP B N     1 
ATOM   5636 C CA    . TRP B 1 203 ? 7.170   91.132  41.229 1.00 18.53 ? 203  TRP B CA    1 
ATOM   5637 C C     . TRP B 1 203 ? 8.067   91.791  42.291 1.00 17.82 ? 203  TRP B C     1 
ATOM   5638 O O     . TRP B 1 203 ? 7.998   91.450  43.486 1.00 18.88 ? 203  TRP B O     1 
ATOM   5639 C CB    . TRP B 1 203 ? 7.976   90.070  40.473 1.00 18.63 ? 203  TRP B CB    1 
ATOM   5640 C CG    . TRP B 1 203 ? 8.232   88.811  41.225 1.00 17.88 ? 203  TRP B CG    1 
ATOM   5641 C CD1   . TRP B 1 203 ? 7.606   88.381  42.365 1.00 18.42 ? 203  TRP B CD1   1 
ATOM   5642 C CD2   . TRP B 1 203 ? 9.147   87.768  40.840 1.00 16.78 ? 203  TRP B CD2   1 
ATOM   5643 N NE1   . TRP B 1 203 ? 8.061   87.136  42.696 1.00 19.51 ? 203  TRP B NE1   1 
ATOM   5644 C CE2   . TRP B 1 203 ? 8.965   86.707  41.753 1.00 18.60 ? 203  TRP B CE2   1 
ATOM   5645 C CE3   . TRP B 1 203 ? 10.039  87.603  39.776 1.00 17.87 ? 203  TRP B CE3   1 
ATOM   5646 C CZ2   . TRP B 1 203 ? 9.724   85.532  41.689 1.00 18.20 ? 203  TRP B CZ2   1 
ATOM   5647 C CZ3   . TRP B 1 203 ? 10.693  86.397  39.646 1.00 19.41 ? 203  TRP B CZ3   1 
ATOM   5648 C CH2   . TRP B 1 203 ? 10.567  85.394  40.605 1.00 20.05 ? 203  TRP B CH2   1 
ATOM   5649 N N     . GLN B 1 204 ? 8.922   92.707  41.858 1.00 16.98 ? 204  GLN B N     1 
ATOM   5650 C CA    . GLN B 1 204 ? 9.865   93.435  42.738 1.00 17.60 ? 204  GLN B CA    1 
ATOM   5651 C C     . GLN B 1 204 ? 9.303   94.798  43.185 1.00 17.20 ? 204  GLN B C     1 
ATOM   5652 O O     . GLN B 1 204 ? 10.061  95.541  43.834 1.00 18.82 ? 204  GLN B O     1 
ATOM   5653 C CB    . GLN B 1 204 ? 11.254  93.531  42.071 1.00 18.64 ? 204  GLN B CB    1 
ATOM   5654 C CG    . GLN B 1 204 ? 12.136  92.327  42.379 1.00 19.01 ? 204  GLN B CG    1 
ATOM   5655 C CD    . GLN B 1 204 ? 11.560  91.088  41.731 1.00 19.37 ? 204  GLN B CD    1 
ATOM   5656 O OE1   . GLN B 1 204 ? 11.493  90.958  40.505 1.00 18.39 ? 204  GLN B OE1   1 
ATOM   5657 N NE2   . GLN B 1 204 ? 11.011  90.205  42.542 1.00 18.37 ? 204  GLN B NE2   1 
ATOM   5658 N N     . LEU B 1 205 ? 8.043   95.110  42.906 1.00 16.56 ? 205  LEU B N     1 
ATOM   5659 C CA    . LEU B 1 205 ? 7.429   96.420  43.237 1.00 16.86 ? 205  LEU B CA    1 
ATOM   5660 C C     . LEU B 1 205 ? 6.417   96.334  44.405 1.00 18.25 ? 205  LEU B C     1 
ATOM   5661 O O     . LEU B 1 205 ? 6.255   97.341  45.127 1.00 20.34 ? 205  LEU B O     1 
ATOM   5662 C CB    . LEU B 1 205 ? 6.746   96.929  41.977 1.00 16.89 ? 205  LEU B CB    1 
ATOM   5663 C CG    . LEU B 1 205 ? 7.680   97.210  40.786 1.00 17.88 ? 205  LEU B CG    1 
ATOM   5664 C CD1   . LEU B 1 205 ? 6.966   98.043  39.740 1.00 20.27 ? 205  LEU B CD1   1 
ATOM   5665 C CD2   . LEU B 1 205 ? 8.921   97.919  41.225 1.00 18.07 ? 205  LEU B CD2   1 
ATOM   5666 N N     . PHE B 1 206 ? 5.687   95.237  44.534 1.00 19.08 ? 206  PHE B N     1 
ATOM   5667 C CA    . PHE B 1 206 ? 4.638   95.108  45.580 1.00 19.46 ? 206  PHE B CA    1 
ATOM   5668 C C     . PHE B 1 206 ? 4.829   93.755  46.268 1.00 18.76 ? 206  PHE B C     1 
ATOM   5669 O O     . PHE B 1 206 ? 4.748   92.718  45.618 1.00 17.17 ? 206  PHE B O     1 
ATOM   5670 C CB    . PHE B 1 206 ? 3.247   95.213  44.966 1.00 19.65 ? 206  PHE B CB    1 
ATOM   5671 C CG    . PHE B 1 206 ? 2.095   95.022  45.925 1.00 20.30 ? 206  PHE B CG    1 
ATOM   5672 C CD1   . PHE B 1 206 ? 2.018   95.736  47.106 1.00 19.81 ? 206  PHE B CD1   1 
ATOM   5673 C CD2   . PHE B 1 206 ? 1.086   94.105  45.645 1.00 17.81 ? 206  PHE B CD2   1 
ATOM   5674 C CE1   . PHE B 1 206 ? 0.971   95.535  47.983 1.00 20.14 ? 206  PHE B CE1   1 
ATOM   5675 C CE2   . PHE B 1 206 ? 0.028   93.925  46.506 1.00 18.22 ? 206  PHE B CE2   1 
ATOM   5676 C CZ    . PHE B 1 206 ? -0.051  94.660  47.660 1.00 19.34 ? 206  PHE B CZ    1 
ATOM   5677 N N     . LYS B 1 207 ? 5.116   93.787  47.564 1.00 17.26 ? 207  LYS B N     1 
ATOM   5678 C CA    . LYS B 1 207 ? 5.430   92.553  48.338 1.00 17.34 ? 207  LYS B CA    1 
ATOM   5679 C C     . LYS B 1 207 ? 4.250   91.562  48.332 1.00 18.14 ? 207  LYS B C     1 
ATOM   5680 O O     . LYS B 1 207 ? 4.493   90.381  48.137 1.00 17.46 ? 207  LYS B O     1 
ATOM   5681 C CB    . LYS B 1 207 ? 5.775   92.895  49.785 1.00 18.40 ? 207  LYS B CB    1 
ATOM   5682 C CG    . LYS B 1 207 ? 7.078   93.607  49.980 1.00 19.14 ? 207  LYS B CG    1 
ATOM   5683 C CD    . LYS B 1 207 ? 7.177   94.178  51.395 1.00 21.27 ? 207  LYS B CD    1 
ATOM   5684 C CE    . LYS B 1 207 ? 8.584   94.446  51.890 1.00 21.34 ? 207  LYS B CE    1 
ATOM   5685 N NZ    . LYS B 1 207 ? 9.249   93.193  52.321 1.00 21.70 ? 207  LYS B NZ    1 
ATOM   5686 N N     . TYR B 1 208 ? 3.011   91.965  48.620 1.00 18.74 ? 208  TYR B N     1 
ATOM   5687 C CA    . TYR B 1 208 ? 1.989   90.985  49.085 1.00 16.99 ? 208  TYR B CA    1 
ATOM   5688 C C     . TYR B 1 208 ? 1.461   90.108  47.946 1.00 17.83 ? 208  TYR B C     1 
ATOM   5689 O O     . TYR B 1 208 ? 1.165   88.930  48.152 1.00 19.85 ? 208  TYR B O     1 
ATOM   5690 C CB    . TYR B 1 208 ? 0.822   91.670  49.791 1.00 16.72 ? 208  TYR B CB    1 
ATOM   5691 C CG    . TYR B 1 208 ? 1.220   92.526  50.968 1.00 15.67 ? 208  TYR B CG    1 
ATOM   5692 C CD1   . TYR B 1 208 ? 2.228   92.144  51.839 1.00 18.04 ? 208  TYR B CD1   1 
ATOM   5693 C CD2   . TYR B 1 208 ? 0.594   93.735  51.198 1.00 16.99 ? 208  TYR B CD2   1 
ATOM   5694 C CE1   . TYR B 1 208 ? 2.615   92.936  52.916 1.00 19.84 ? 208  TYR B CE1   1 
ATOM   5695 C CE2   . TYR B 1 208 ? 0.962   94.551  52.266 1.00 18.29 ? 208  TYR B CE2   1 
ATOM   5696 C CZ    . TYR B 1 208 ? 1.937   94.129  53.157 1.00 18.57 ? 208  TYR B CZ    1 
ATOM   5697 O OH    . TYR B 1 208 ? 2.321   94.943  54.168 1.00 20.23 ? 208  TYR B OH    1 
ATOM   5698 N N     . GLY B 1 209 ? 1.272   90.661  46.760 1.00 16.67 ? 209  GLY B N     1 
ATOM   5699 C CA    . GLY B 1 209 ? 0.323   90.038  45.830 1.00 17.38 ? 209  GLY B CA    1 
ATOM   5700 C C     . GLY B 1 209 ? -1.048  89.964  46.457 1.00 18.58 ? 209  GLY B C     1 
ATOM   5701 O O     . GLY B 1 209 ? -1.559  91.011  46.997 1.00 19.64 ? 209  GLY B O     1 
ATOM   5702 N N     . TYR B 1 210 ? -1.655  88.794  46.369 1.00 18.82 ? 210  TYR B N     1 
ATOM   5703 C CA    . TYR B 1 210 ? -3.026  88.539  46.853 1.00 20.13 ? 210  TYR B CA    1 
ATOM   5704 C C     . TYR B 1 210 ? -3.007  87.278  47.708 1.00 19.01 ? 210  TYR B C     1 
ATOM   5705 O O     . TYR B 1 210 ? -2.306  86.319  47.381 1.00 16.16 ? 210  TYR B O     1 
ATOM   5706 C CB    . TYR B 1 210 ? -3.976  88.408  45.659 1.00 19.06 ? 210  TYR B CB    1 
ATOM   5707 C CG    . TYR B 1 210 ? -5.369  87.916  45.959 1.00 18.98 ? 210  TYR B CG    1 
ATOM   5708 C CD1   . TYR B 1 210 ? -6.316  88.704  46.607 1.00 21.59 ? 210  TYR B CD1   1 
ATOM   5709 C CD2   . TYR B 1 210 ? -5.762  86.661  45.560 1.00 20.08 ? 210  TYR B CD2   1 
ATOM   5710 C CE1   . TYR B 1 210 ? -7.618  88.254  46.807 1.00 21.30 ? 210  TYR B CE1   1 
ATOM   5711 C CE2   . TYR B 1 210 ? -7.046  86.193  45.775 1.00 20.25 ? 210  TYR B CE2   1 
ATOM   5712 C CZ    . TYR B 1 210 ? -7.989  87.002  46.370 1.00 20.32 ? 210  TYR B CZ    1 
ATOM   5713 O OH    . TYR B 1 210 ? -9.261  86.498  46.484 1.00 21.76 ? 210  TYR B OH    1 
ATOM   5714 N N     . GLY B 1 211 ? -3.774  87.301  48.797 1.00 16.77 ? 211  GLY B N     1 
ATOM   5715 C CA    . GLY B 1 211 ? -3.905  86.111  49.638 1.00 17.71 ? 211  GLY B CA    1 
ATOM   5716 C C     . GLY B 1 211 ? -2.817  86.048  50.703 1.00 17.29 ? 211  GLY B C     1 
ATOM   5717 O O     . GLY B 1 211 ? -2.163  87.036  51.030 1.00 18.06 ? 211  GLY B O     1 
ATOM   5718 N N     . PRO B 1 212 ? -2.624  84.873  51.319 1.00 16.50 ? 212  PRO B N     1 
ATOM   5719 C CA    . PRO B 1 212 ? -1.685  84.774  52.416 1.00 17.13 ? 212  PRO B CA    1 
ATOM   5720 C C     . PRO B 1 212 ? -0.291  85.264  51.999 1.00 18.05 ? 212  PRO B C     1 
ATOM   5721 O O     . PRO B 1 212 ? 0.212   84.916  50.899 1.00 17.24 ? 212  PRO B O     1 
ATOM   5722 C CB    . PRO B 1 212 ? -1.730  83.308  52.818 1.00 18.27 ? 212  PRO B CB    1 
ATOM   5723 C CG    . PRO B 1 212 ? -3.053  82.806  52.294 1.00 18.92 ? 212  PRO B CG    1 
ATOM   5724 C CD    . PRO B 1 212 ? -3.364  83.636  51.072 1.00 17.92 ? 212  PRO B CD    1 
ATOM   5725 N N     . TYR B 1 213 ? 0.358   85.997  52.909 1.00 16.67 ? 213  TYR B N     1 
ATOM   5726 C CA    . TYR B 1 213 ? 1.690   86.588  52.651 1.00 16.16 ? 213  TYR B CA    1 
ATOM   5727 C C     . TYR B 1 213 ? 2.714   85.598  53.202 1.00 17.46 ? 213  TYR B C     1 
ATOM   5728 O O     . TYR B 1 213 ? 2.943   85.577  54.409 1.00 16.62 ? 213  TYR B O     1 
ATOM   5729 C CB    . TYR B 1 213 ? 1.794   87.983  53.298 1.00 18.38 ? 213  TYR B CB    1 
ATOM   5730 C CG    . TYR B 1 213 ? 3.109   88.692  53.116 1.00 17.73 ? 213  TYR B CG    1 
ATOM   5731 C CD1   . TYR B 1 213 ? 3.862   88.542  51.941 1.00 17.70 ? 213  TYR B CD1   1 
ATOM   5732 C CD2   . TYR B 1 213 ? 3.596   89.548  54.086 1.00 20.08 ? 213  TYR B CD2   1 
ATOM   5733 C CE1   . TYR B 1 213 ? 5.056   89.237  51.752 1.00 16.94 ? 213  TYR B CE1   1 
ATOM   5734 C CE2   . TYR B 1 213 ? 4.764   90.273  53.906 1.00 19.97 ? 213  TYR B CE2   1 
ATOM   5735 C CZ    . TYR B 1 213 ? 5.519   90.073  52.756 1.00 20.11 ? 213  TYR B CZ    1 
ATOM   5736 O OH    . TYR B 1 213 ? 6.675   90.752  52.611 1.00 22.26 ? 213  TYR B OH    1 
ATOM   5737 N N     . VAL B 1 214 ? 3.303   84.784  52.350 1.00 16.38 ? 214  VAL B N     1 
ATOM   5738 C CA    . VAL B 1 214 ? 4.078   83.573  52.747 1.00 17.40 ? 214  VAL B CA    1 
ATOM   5739 C C     . VAL B 1 214 ? 5.580   83.749  52.624 1.00 15.77 ? 214  VAL B C     1 
ATOM   5740 O O     . VAL B 1 214 ? 6.269   82.811  53.069 1.00 16.79 ? 214  VAL B O     1 
ATOM   5741 C CB    . VAL B 1 214 ? 3.641   82.327  51.961 1.00 20.37 ? 214  VAL B CB    1 
ATOM   5742 C CG1   . VAL B 1 214 ? 2.164   82.028  52.175 1.00 22.71 ? 214  VAL B CG1   1 
ATOM   5743 C CG2   . VAL B 1 214 ? 3.986   82.428  50.480 1.00 19.97 ? 214  VAL B CG2   1 
ATOM   5744 N N     . ASP B 1 215 ? 6.111   84.866  52.104 1.00 16.04 ? 215  ASP B N     1 
ATOM   5745 C CA    . ASP B 1 215 ? 7.567   84.956  51.858 1.00 17.15 ? 215  ASP B CA    1 
ATOM   5746 C C     . ASP B 1 215 ? 8.332   84.601  53.134 1.00 16.21 ? 215  ASP B C     1 
ATOM   5747 O O     . ASP B 1 215 ? 9.347   83.883  53.077 1.00 16.82 ? 215  ASP B O     1 
ATOM   5748 C CB    . ASP B 1 215 ? 7.933   86.331  51.315 1.00 17.08 ? 215  ASP B CB    1 
ATOM   5749 C CG    . ASP B 1 215 ? 7.291   86.592  49.964 1.00 18.88 ? 215  ASP B CG    1 
ATOM   5750 O OD1   . ASP B 1 215 ? 6.079   86.624  49.899 1.00 18.69 ? 215  ASP B OD1   1 
ATOM   5751 O OD2   . ASP B 1 215 ? 8.037   86.762  48.990 1.00 17.98 ? 215  ASP B OD2   1 
ATOM   5752 N N     . GLY B 1 216 ? 7.908   85.152  54.271 1.00 16.04 ? 216  GLY B N     1 
ATOM   5753 C CA    . GLY B 1 216 ? 8.651   84.982  55.515 1.00 16.48 ? 216  GLY B CA    1 
ATOM   5754 C C     . GLY B 1 216 ? 8.745   83.525  55.949 1.00 15.43 ? 216  GLY B C     1 
ATOM   5755 O O     . GLY B 1 216 ? 9.651   83.191  56.734 1.00 14.01 ? 216  GLY B O     1 
ATOM   5756 N N     . ILE B 1 217 ? 7.872   82.624  55.494 1.00 16.52 ? 217  ILE B N     1 
ATOM   5757 C CA    . ILE B 1 217 ? 7.936   81.232  56.016 1.00 16.11 ? 217  ILE B CA    1 
ATOM   5758 C C     . ILE B 1 217 ? 9.150   80.533  55.416 1.00 16.76 ? 217  ILE B C     1 
ATOM   5759 O O     . ILE B 1 217 ? 9.512   79.483  55.954 1.00 16.22 ? 217  ILE B O     1 
ATOM   5760 C CB    . ILE B 1 217 ? 6.628   80.425  55.835 1.00 17.66 ? 217  ILE B CB    1 
ATOM   5761 C CG1   . ILE B 1 217 ? 6.450   79.911  54.416 1.00 16.98 ? 217  ILE B CG1   1 
ATOM   5762 C CG2   . ILE B 1 217 ? 5.407   81.219  56.303 1.00 18.42 ? 217  ILE B CG2   1 
ATOM   5763 C CD1   . ILE B 1 217 ? 5.291   78.939  54.239 1.00 18.04 ? 217  ILE B CD1   1 
ATOM   5764 N N     . PHE B 1 218 ? 9.795   81.097  54.401 1.00 16.20 ? 218  PHE B N     1 
ATOM   5765 C CA    . PHE B 1 218 ? 10.994  80.482  53.775 1.00 16.78 ? 218  PHE B CA    1 
ATOM   5766 C C     . PHE B 1 218 ? 12.259  81.110  54.361 1.00 18.93 ? 218  PHE B C     1 
ATOM   5767 O O     . PHE B 1 218 ? 13.362  80.740  53.929 1.00 22.46 ? 218  PHE B O     1 
ATOM   5768 C CB    . PHE B 1 218 ? 10.892  80.605  52.261 1.00 15.36 ? 218  PHE B CB    1 
ATOM   5769 C CG    . PHE B 1 218 ? 9.657   79.926  51.751 1.00 17.66 ? 218  PHE B CG    1 
ATOM   5770 C CD1   . PHE B 1 218 ? 9.559   78.546  51.831 1.00 17.41 ? 218  PHE B CD1   1 
ATOM   5771 C CD2   . PHE B 1 218 ? 8.598   80.641  51.230 1.00 16.14 ? 218  PHE B CD2   1 
ATOM   5772 C CE1   . PHE B 1 218 ? 8.428   77.886  51.379 1.00 19.03 ? 218  PHE B CE1   1 
ATOM   5773 C CE2   . PHE B 1 218 ? 7.464   79.970  50.801 1.00 18.51 ? 218  PHE B CE2   1 
ATOM   5774 C CZ    . PHE B 1 218 ? 7.375   78.608  50.871 1.00 18.55 ? 218  PHE B CZ    1 
ATOM   5775 N N     . SER B 1 219 ? 12.114  82.015  55.343 1.00 17.41 ? 219  SER B N     1 
ATOM   5776 C CA    . SER B 1 219 ? 13.258  82.597  56.072 1.00 15.85 ? 219  SER B CA    1 
ATOM   5777 C C     . SER B 1 219 ? 13.489  81.829  57.382 1.00 16.95 ? 219  SER B C     1 
ATOM   5778 O O     . SER B 1 219 ? 12.481  81.375  58.016 1.00 16.35 ? 219  SER B O     1 
ATOM   5779 C CB    . SER B 1 219 ? 13.052  84.103  56.302 1.00 16.69 ? 219  SER B CB    1 
ATOM   5780 O OG    . SER B 1 219 ? 12.062  84.431  57.262 1.00 16.47 ? 219  SER B OG    1 
ATOM   5781 N N     . GLN B 1 220 ? 14.749  81.687  57.802 1.00 16.24 ? 220  GLN B N     1 
ATOM   5782 C CA    . GLN B 1 220 ? 15.164  80.834  58.944 1.00 16.54 ? 220  GLN B CA    1 
ATOM   5783 C C     . GLN B 1 220 ? 14.331  79.543  58.948 1.00 18.00 ? 220  GLN B C     1 
ATOM   5784 O O     . GLN B 1 220 ? 13.780  79.141  59.996 1.00 16.80 ? 220  GLN B O     1 
ATOM   5785 C CB    . GLN B 1 220 ? 15.039  81.612  60.262 1.00 17.45 ? 220  GLN B CB    1 
ATOM   5786 C CG    . GLN B 1 220 ? 16.133  82.651  60.449 1.00 16.94 ? 220  GLN B CG    1 
ATOM   5787 C CD    . GLN B 1 220 ? 16.391  83.055  61.878 1.00 19.65 ? 220  GLN B CD    1 
ATOM   5788 O OE1   . GLN B 1 220 ? 15.569  82.785  62.758 1.00 19.32 ? 220  GLN B OE1   1 
ATOM   5789 N NE2   . GLN B 1 220 ? 17.470  83.808  62.094 1.00 18.04 ? 220  GLN B NE2   1 
ATOM   5790 N N     . SER B 1 221 ? 14.301  78.873  57.807 1.00 17.84 ? 221  SER B N     1 
ATOM   5791 C CA    . SER B 1 221 ? 13.297  77.828  57.539 1.00 20.54 ? 221  SER B CA    1 
ATOM   5792 C C     . SER B 1 221 ? 13.877  76.621  56.782 1.00 18.63 ? 221  SER B C     1 
ATOM   5793 O O     . SER B 1 221 ? 14.915  76.759  56.107 1.00 17.24 ? 221  SER B O     1 
ATOM   5794 C CB    . SER B 1 221 ? 12.185  78.454  56.737 1.00 21.03 ? 221  SER B CB    1 
ATOM   5795 O OG    . SER B 1 221 ? 11.192  77.489  56.556 1.00 22.60 ? 221  SER B OG    1 
ATOM   5796 N N     . ASN B 1 222 ? 13.128  75.515  56.804 1.00 17.18 ? 222  ASN B N     1 
ATOM   5797 C CA    . ASN B 1 222 ? 13.409  74.307  55.988 1.00 18.18 ? 222  ASN B CA    1 
ATOM   5798 C C     . ASN B 1 222 ? 12.119  73.948  55.246 1.00 18.26 ? 222  ASN B C     1 
ATOM   5799 O O     . ASN B 1 222 ? 11.873  72.788  55.046 1.00 21.34 ? 222  ASN B O     1 
ATOM   5800 C CB    . ASN B 1 222 ? 14.042  73.209  56.823 1.00 17.71 ? 222  ASN B CB    1 
ATOM   5801 C CG    . ASN B 1 222 ? 13.214  72.750  57.996 1.00 17.42 ? 222  ASN B CG    1 
ATOM   5802 O OD1   . ASN B 1 222 ? 12.108  73.229  58.184 1.00 16.58 ? 222  ASN B OD1   1 
ATOM   5803 N ND2   . ASN B 1 222 ? 13.781  71.855  58.809 1.00 18.12 ? 222  ASN B ND2   1 
ATOM   5804 N N     . PHE B 1 223 ? 11.319  74.944  54.860 1.00 16.48 ? 223  PHE B N     1 
ATOM   5805 C CA    . PHE B 1 223 ? 10.019  74.722  54.184 1.00 17.65 ? 223  PHE B CA    1 
ATOM   5806 C C     . PHE B 1 223 ? 10.201  74.763  52.673 1.00 18.83 ? 223  PHE B C     1 
ATOM   5807 O O     . PHE B 1 223 ? 9.230   74.510  51.955 1.00 20.87 ? 223  PHE B O     1 
ATOM   5808 C CB    . PHE B 1 223 ? 8.975   75.752  54.615 1.00 17.39 ? 223  PHE B CB    1 
ATOM   5809 C CG    . PHE B 1 223 ? 8.539   75.680  56.052 1.00 18.20 ? 223  PHE B CG    1 
ATOM   5810 C CD1   . PHE B 1 223 ? 8.819   74.584  56.862 1.00 18.88 ? 223  PHE B CD1   1 
ATOM   5811 C CD2   . PHE B 1 223 ? 7.865   76.750  56.603 1.00 17.26 ? 223  PHE B CD2   1 
ATOM   5812 C CE1   . PHE B 1 223 ? 8.366   74.567  58.168 1.00 18.12 ? 223  PHE B CE1   1 
ATOM   5813 C CE2   . PHE B 1 223 ? 7.391   76.707  57.897 1.00 18.98 ? 223  PHE B CE2   1 
ATOM   5814 C CZ    . PHE B 1 223 ? 7.659   75.626  58.678 1.00 18.03 ? 223  PHE B CZ    1 
ATOM   5815 N N     . GLY B 1 224 ? 11.383  75.171  52.203 1.00 19.72 ? 224  GLY B N     1 
ATOM   5816 C CA    . GLY B 1 224 ? 11.613  75.292  50.758 1.00 18.92 ? 224  GLY B CA    1 
ATOM   5817 C C     . GLY B 1 224 ? 13.027  75.722  50.448 1.00 18.64 ? 224  GLY B C     1 
ATOM   5818 O O     . GLY B 1 224 ? 13.755  76.129  51.382 1.00 19.20 ? 224  GLY B O     1 
ATOM   5819 N N     . VAL B 1 225 ? 13.371  75.684  49.163 1.00 17.20 ? 225  VAL B N     1 
ATOM   5820 C CA    . VAL B 1 225 ? 14.672  76.163  48.637 1.00 18.42 ? 225  VAL B CA    1 
ATOM   5821 C C     . VAL B 1 225 ? 14.425  77.399  47.801 1.00 17.86 ? 225  VAL B C     1 
ATOM   5822 O O     . VAL B 1 225 ? 13.830  77.284  46.713 1.00 16.87 ? 225  VAL B O     1 
ATOM   5823 C CB    . VAL B 1 225 ? 15.392  75.078  47.816 1.00 20.12 ? 225  VAL B CB    1 
ATOM   5824 C CG1   . VAL B 1 225 ? 16.759  75.578  47.363 1.00 19.88 ? 225  VAL B CG1   1 
ATOM   5825 C CG2   . VAL B 1 225 ? 15.512  73.793  48.628 1.00 19.78 ? 225  VAL B CG2   1 
ATOM   5826 N N     . VAL B 1 226 ? 14.955  78.525  48.251 1.00 16.68 ? 226  VAL B N     1 
ATOM   5827 C CA    . VAL B 1 226 ? 14.747  79.798  47.535 1.00 16.77 ? 226  VAL B CA    1 
ATOM   5828 C C     . VAL B 1 226 ? 15.741  79.844  46.376 1.00 16.85 ? 226  VAL B C     1 
ATOM   5829 O O     . VAL B 1 226 ? 16.933  79.644  46.632 1.00 16.60 ? 226  VAL B O     1 
ATOM   5830 C CB    . VAL B 1 226 ? 14.917  81.001  48.473 1.00 17.76 ? 226  VAL B CB    1 
ATOM   5831 C CG1   . VAL B 1 226 ? 14.830  82.296  47.678 1.00 18.56 ? 226  VAL B CG1   1 
ATOM   5832 C CG2   . VAL B 1 226 ? 13.899  80.937  49.573 1.00 17.36 ? 226  VAL B CG2   1 
ATOM   5833 N N     . THR B 1 227 ? 15.257  80.070  45.151 1.00 16.52 ? 227  THR B N     1 
ATOM   5834 C CA    . THR B 1 227 ? 16.116  80.006  43.937 1.00 17.22 ? 227  THR B CA    1 
ATOM   5835 C C     . THR B 1 227 ? 16.202  81.357  43.248 1.00 16.48 ? 227  THR B C     1 
ATOM   5836 O O     . THR B 1 227 ? 17.099  81.502  42.405 1.00 18.62 ? 227  THR B O     1 
ATOM   5837 C CB    . THR B 1 227 ? 15.598  78.913  42.976 1.00 17.63 ? 227  THR B CB    1 
ATOM   5838 O OG1   . THR B 1 227 ? 14.222  79.137  42.752 1.00 17.82 ? 227  THR B OG1   1 
ATOM   5839 C CG2   . THR B 1 227 ? 15.815  77.531  43.527 1.00 17.77 ? 227  THR B CG2   1 
ATOM   5840 N N     . LYS B 1 228 ? 15.308  82.311  43.565 1.00 15.72 ? 228  LYS B N     1 
ATOM   5841 C CA    . LYS B 1 228 ? 15.393  83.711  43.069 1.00 15.90 ? 228  LYS B CA    1 
ATOM   5842 C C     . LYS B 1 228 ? 14.785  84.602  44.149 1.00 15.18 ? 228  LYS B C     1 
ATOM   5843 O O     . LYS B 1 228 ? 13.840  84.161  44.782 1.00 16.16 ? 228  LYS B O     1 
ATOM   5844 C CB    . LYS B 1 228 ? 14.649  83.988  41.773 1.00 15.93 ? 228  LYS B CB    1 
ATOM   5845 C CG    . LYS B 1 228 ? 15.029  83.138  40.558 1.00 17.34 ? 228  LYS B CG    1 
ATOM   5846 C CD    . LYS B 1 228 ? 14.102  83.399  39.370 1.00 19.40 ? 228  LYS B CD    1 
ATOM   5847 C CE    . LYS B 1 228 ? 14.492  82.656  38.103 1.00 21.24 ? 228  LYS B CE    1 
ATOM   5848 N NZ    . LYS B 1 228 ? 14.716  81.214  38.349 1.00 23.31 ? 228  LYS B NZ    1 
ATOM   5849 N N     . MET B 1 229 ? 15.355  85.765  44.374 1.00 16.23 ? 229  MET B N     1 
ATOM   5850 C CA    . MET B 1 229 ? 14.825  86.701  45.394 1.00 17.03 ? 229  MET B CA    1 
ATOM   5851 C C     . MET B 1 229 ? 14.990  88.121  44.881 1.00 16.76 ? 229  MET B C     1 
ATOM   5852 O O     . MET B 1 229 ? 16.075  88.510  44.345 1.00 17.50 ? 229  MET B O     1 
ATOM   5853 C CB    . MET B 1 229 ? 15.548  86.517  46.719 1.00 17.10 ? 229  MET B CB    1 
ATOM   5854 C CG    . MET B 1 229 ? 14.810  87.142  47.857 1.00 18.57 ? 229  MET B CG    1 
ATOM   5855 S SD    . MET B 1 229 ? 15.811  87.137  49.352 1.00 18.94 ? 229  MET B SD    1 
ATOM   5856 C CE    . MET B 1 229 ? 16.744  88.627  49.040 1.00 19.58 ? 229  MET B CE    1 
ATOM   5857 N N     . GLY B 1 230 ? 13.941  88.907  45.043 1.00 17.83 ? 230  GLY B N     1 
ATOM   5858 C CA    . GLY B 1 230 ? 14.005  90.364  44.834 1.00 16.47 ? 230  GLY B CA    1 
ATOM   5859 C C     . GLY B 1 230 ? 14.401  91.087  46.112 1.00 17.54 ? 230  GLY B C     1 
ATOM   5860 O O     . GLY B 1 230 ? 14.082  90.600  47.208 1.00 17.02 ? 230  GLY B O     1 
ATOM   5861 N N     . ILE B 1 231 ? 15.072  92.221  45.980 1.00 15.60 ? 231  ILE B N     1 
ATOM   5862 C CA    . ILE B 1 231 ? 15.468  93.028  47.169 1.00 16.61 ? 231  ILE B CA    1 
ATOM   5863 C C     . ILE B 1 231 ? 15.425  94.492  46.757 1.00 17.57 ? 231  ILE B C     1 
ATOM   5864 O O     . ILE B 1 231 ? 15.883  94.863  45.660 1.00 17.30 ? 231  ILE B O     1 
ATOM   5865 C CB    . ILE B 1 231 ? 16.802  92.608  47.771 1.00 18.30 ? 231  ILE B CB    1 
ATOM   5866 C CG1   . ILE B 1 231 ? 17.012  93.238  49.142 1.00 18.95 ? 231  ILE B CG1   1 
ATOM   5867 C CG2   . ILE B 1 231 ? 17.988  92.912  46.878 1.00 19.11 ? 231  ILE B CG2   1 
ATOM   5868 C CD1   . ILE B 1 231 ? 18.106  92.547  49.936 1.00 19.99 ? 231  ILE B CD1   1 
ATOM   5869 N N     . TRP B 1 232 ? 14.804  95.313  47.574 1.00 16.83 ? 232  TRP B N     1 
ATOM   5870 C CA    . TRP B 1 232 ? 14.821  96.771  47.314 1.00 17.97 ? 232  TRP B CA    1 
ATOM   5871 C C     . TRP B 1 232 ? 16.213  97.324  47.607 1.00 18.90 ? 232  TRP B C     1 
ATOM   5872 O O     . TRP B 1 232 ? 16.908  96.848  48.544 1.00 17.74 ? 232  TRP B O     1 
ATOM   5873 C CB    . TRP B 1 232 ? 13.716  97.447  48.125 1.00 17.62 ? 232  TRP B CB    1 
ATOM   5874 C CG    . TRP B 1 232 ? 12.351  97.052  47.698 1.00 19.37 ? 232  TRP B CG    1 
ATOM   5875 C CD1   . TRP B 1 232 ? 11.951  96.559  46.490 1.00 19.20 ? 232  TRP B CD1   1 
ATOM   5876 C CD2   . TRP B 1 232 ? 11.163  97.184  48.501 1.00 18.92 ? 232  TRP B CD2   1 
ATOM   5877 N NE1   . TRP B 1 232 ? 10.585  96.388  46.478 1.00 20.80 ? 232  TRP B NE1   1 
ATOM   5878 C CE2   . TRP B 1 232 ? 10.088  96.745  47.710 1.00 20.09 ? 232  TRP B CE2   1 
ATOM   5879 C CE3   . TRP B 1 232 ? 10.917  97.659  49.799 1.00 21.53 ? 232  TRP B CE3   1 
ATOM   5880 C CZ2   . TRP B 1 232 ? 8.769   96.791  48.172 1.00 21.48 ? 232  TRP B CZ2   1 
ATOM   5881 C CZ3   . TRP B 1 232 ? 9.614   97.678  50.262 1.00 21.91 ? 232  TRP B CZ3   1 
ATOM   5882 C CH2   . TRP B 1 232 ? 8.558   97.264  49.448 1.00 20.14 ? 232  TRP B CH2   1 
ATOM   5883 N N     . LEU B 1 233 ? 16.582  98.331  46.835 1.00 18.05 ? 233  LEU B N     1 
ATOM   5884 C CA    . LEU B 1 233 ? 17.892  98.974  46.959 1.00 18.70 ? 233  LEU B CA    1 
ATOM   5885 C C     . LEU B 1 233 ? 17.687  100.480 47.150 1.00 18.96 ? 233  LEU B C     1 
ATOM   5886 O O     . LEU B 1 233 ? 16.804  101.093 46.518 1.00 19.31 ? 233  LEU B O     1 
ATOM   5887 C CB    . LEU B 1 233 ? 18.715  98.715  45.691 1.00 18.71 ? 233  LEU B CB    1 
ATOM   5888 C CG    . LEU B 1 233 ? 19.101  97.288  45.368 1.00 20.28 ? 233  LEU B CG    1 
ATOM   5889 C CD1   . LEU B 1 233 ? 19.906  97.288  44.074 1.00 19.75 ? 233  LEU B CD1   1 
ATOM   5890 C CD2   . LEU B 1 233 ? 19.880  96.620  46.509 1.00 21.54 ? 233  LEU B CD2   1 
ATOM   5891 N N     . MET B 1 234 ? 18.522  101.076 47.982 1.00 18.11 ? 234  MET B N     1 
ATOM   5892 C CA    . MET B 1 234 ? 18.415  102.526 48.260 1.00 20.10 ? 234  MET B CA    1 
ATOM   5893 C C     . MET B 1 234 ? 18.980  103.350 47.092 1.00 18.26 ? 234  MET B C     1 
ATOM   5894 O O     . MET B 1 234 ? 20.114  103.132 46.622 1.00 18.22 ? 234  MET B O     1 
ATOM   5895 C CB    . MET B 1 234 ? 19.218  102.867 49.507 1.00 21.05 ? 234  MET B CB    1 
ATOM   5896 C CG    . MET B 1 234 ? 18.967  104.311 49.979 1.00 23.96 ? 234  MET B CG    1 
ATOM   5897 S SD    . MET B 1 234 ? 19.749  104.571 51.583 1.00 25.88 ? 234  MET B SD    1 
ATOM   5898 C CE    . MET B 1 234 ? 21.459  104.487 51.197 1.00 27.50 ? 234  MET B CE    1 
ATOM   5899 N N     . PRO B 1 235 ? 18.212  104.329 46.585 1.00 18.17 ? 235  PRO B N     1 
ATOM   5900 C CA    . PRO B 1 235 ? 18.760  105.296 45.639 1.00 20.18 ? 235  PRO B CA    1 
ATOM   5901 C C     . PRO B 1 235 ? 19.943  106.035 46.269 1.00 18.78 ? 235  PRO B C     1 
ATOM   5902 O O     . PRO B 1 235 ? 19.951  106.317 47.464 1.00 18.92 ? 235  PRO B O     1 
ATOM   5903 C CB    . PRO B 1 235 ? 17.591  106.253 45.327 1.00 20.15 ? 235  PRO B CB    1 
ATOM   5904 C CG    . PRO B 1 235 ? 16.369  105.471 45.707 1.00 22.27 ? 235  PRO B CG    1 
ATOM   5905 C CD    . PRO B 1 235 ? 16.792  104.573 46.847 1.00 19.17 ? 235  PRO B CD    1 
ATOM   5906 N N     . GLU B 1 236 ? 20.969  106.324 45.473 1.00 20.54 ? 236  GLU B N     1 
ATOM   5907 C CA    . GLU B 1 236 ? 22.130  107.065 46.000 1.00 20.79 ? 236  GLU B CA    1 
ATOM   5908 C C     . GLU B 1 236 ? 21.599  108.377 46.577 1.00 21.00 ? 236  GLU B C     1 
ATOM   5909 O O     . GLU B 1 236 ? 20.856  109.091 45.923 1.00 21.79 ? 236  GLU B O     1 
ATOM   5910 C CB    . GLU B 1 236 ? 23.123  107.301 44.859 1.00 24.86 ? 236  GLU B CB    1 
ATOM   5911 C CG    . GLU B 1 236 ? 24.193  108.308 45.144 1.00 30.09 ? 236  GLU B CG    1 
ATOM   5912 C CD    . GLU B 1 236 ? 25.038  108.474 43.870 1.00 38.04 ? 236  GLU B CD    1 
ATOM   5913 O OE1   . GLU B 1 236 ? 24.547  109.097 42.908 1.00 39.32 ? 236  GLU B OE1   1 
ATOM   5914 O OE2   . GLU B 1 236 ? 26.073  107.841 43.802 1.00 40.41 ? 236  GLU B OE2   1 
ATOM   5915 N N     . PRO B 1 237 ? 21.895  108.711 47.832 1.00 20.74 ? 237  PRO B N     1 
ATOM   5916 C CA    . PRO B 1 237 ? 21.336  109.912 48.439 1.00 24.21 ? 237  PRO B CA    1 
ATOM   5917 C C     . PRO B 1 237 ? 22.131  111.157 47.996 1.00 23.43 ? 237  PRO B C     1 
ATOM   5918 O O     . PRO B 1 237 ? 23.210  111.055 47.423 1.00 21.52 ? 237  PRO B O     1 
ATOM   5919 C CB    . PRO B 1 237 ? 21.471  109.642 49.935 1.00 23.81 ? 237  PRO B CB    1 
ATOM   5920 C CG    . PRO B 1 237 ? 22.687  108.768 50.018 1.00 24.22 ? 237  PRO B CG    1 
ATOM   5921 C CD    . PRO B 1 237 ? 22.728  107.941 48.741 1.00 22.64 ? 237  PRO B CD    1 
ATOM   5922 N N     . ALA B 1 238 ? 21.607  112.319 48.324 1.00 24.12 ? 238  ALA B N     1 
ATOM   5923 C CA    . ALA B 1 238 ? 22.208  113.618 47.934 1.00 26.35 ? 238  ALA B CA    1 
ATOM   5924 C C     . ALA B 1 238 ? 23.353  113.974 48.872 1.00 27.91 ? 238  ALA B C     1 
ATOM   5925 O O     . ALA B 1 238 ? 23.997  114.979 48.606 1.00 27.90 ? 238  ALA B O     1 
ATOM   5926 C CB    . ALA B 1 238 ? 21.148  114.674 47.970 1.00 27.99 ? 238  ALA B CB    1 
ATOM   5927 N N     . GLY B 1 239 ? 23.567  113.228 49.959 1.00 23.33 ? 239  GLY B N     1 
ATOM   5928 C CA    . GLY B 1 239 ? 24.687  113.508 50.863 1.00 22.23 ? 239  GLY B CA    1 
ATOM   5929 C C     . GLY B 1 239 ? 24.821  112.366 51.859 1.00 23.35 ? 239  GLY B C     1 
ATOM   5930 O O     . GLY B 1 239 ? 23.902  111.514 51.948 1.00 21.07 ? 239  GLY B O     1 
ATOM   5931 N N     . TYR B 1 240 ? 25.970  112.292 52.468 1.00 22.10 ? 240  TYR B N     1 
ATOM   5932 C CA    . TYR B 1 240 ? 26.396  111.189 53.340 1.00 20.44 ? 240  TYR B CA    1 
ATOM   5933 C C     . TYR B 1 240 ? 27.458  111.695 54.297 1.00 20.50 ? 240  TYR B C     1 
ATOM   5934 O O     . TYR B 1 240 ? 28.507  112.101 53.812 1.00 19.94 ? 240  TYR B O     1 
ATOM   5935 C CB    . TYR B 1 240 ? 26.947  110.063 52.485 1.00 21.13 ? 240  TYR B CB    1 
ATOM   5936 C CG    . TYR B 1 240 ? 27.459  108.906 53.284 1.00 19.10 ? 240  TYR B CG    1 
ATOM   5937 C CD1   . TYR B 1 240 ? 26.605  108.195 54.129 1.00 20.29 ? 240  TYR B CD1   1 
ATOM   5938 C CD2   . TYR B 1 240 ? 28.781  108.516 53.196 1.00 19.99 ? 240  TYR B CD2   1 
ATOM   5939 C CE1   . TYR B 1 240 ? 27.076  107.110 54.856 1.00 20.35 ? 240  TYR B CE1   1 
ATOM   5940 C CE2   . TYR B 1 240 ? 29.263  107.452 53.941 1.00 20.72 ? 240  TYR B CE2   1 
ATOM   5941 C CZ    . TYR B 1 240 ? 28.408  106.749 54.787 1.00 21.10 ? 240  TYR B CZ    1 
ATOM   5942 O OH    . TYR B 1 240 ? 28.909  105.674 55.481 1.00 17.90 ? 240  TYR B OH    1 
ATOM   5943 N N     . ARG B 1 241 ? 27.224  111.572 55.597 1.00 20.66 ? 241  ARG B N     1 
ATOM   5944 C CA    . ARG B 1 241 ? 28.181  111.992 56.654 1.00 22.69 ? 241  ARG B CA    1 
ATOM   5945 C C     . ARG B 1 241 ? 28.226  110.973 57.771 1.00 20.92 ? 241  ARG B C     1 
ATOM   5946 O O     . ARG B 1 241 ? 27.377  110.976 58.667 1.00 22.66 ? 241  ARG B O     1 
ATOM   5947 C CB    . ARG B 1 241 ? 27.752  113.340 57.229 1.00 23.46 ? 241  ARG B CB    1 
ATOM   5948 C CG    . ARG B 1 241 ? 27.814  114.459 56.208 1.00 26.36 ? 241  ARG B CG    1 
ATOM   5949 C CD    . ARG B 1 241 ? 27.397  115.733 56.931 1.00 31.77 ? 241  ARG B CD    1 
ATOM   5950 N NE    . ARG B 1 241 ? 27.022  116.837 56.061 1.00 39.05 ? 241  ARG B NE    1 
ATOM   5951 C CZ    . ARG B 1 241 ? 26.267  117.888 56.470 1.00 40.27 ? 241  ARG B CZ    1 
ATOM   5952 N NH1   . ARG B 1 241 ? 25.868  117.991 57.737 1.00 37.64 ? 241  ARG B NH1   1 
ATOM   5953 N NH2   . ARG B 1 241 ? 25.946  118.826 55.603 1.00 42.92 ? 241  ARG B NH2   1 
ATOM   5954 N N     . PRO B 1 242 ? 29.222  110.073 57.742 1.00 21.26 ? 242  PRO B N     1 
ATOM   5955 C CA    . PRO B 1 242 ? 29.425  109.138 58.836 1.00 21.04 ? 242  PRO B CA    1 
ATOM   5956 C C     . PRO B 1 242 ? 30.022  109.842 60.057 1.00 23.24 ? 242  PRO B C     1 
ATOM   5957 O O     . PRO B 1 242 ? 30.697  110.867 59.917 1.00 21.00 ? 242  PRO B O     1 
ATOM   5958 C CB    . PRO B 1 242 ? 30.406  108.100 58.266 1.00 22.38 ? 242  PRO B CB    1 
ATOM   5959 C CG    . PRO B 1 242 ? 31.059  108.746 57.097 1.00 23.32 ? 242  PRO B CG    1 
ATOM   5960 C CD    . PRO B 1 242 ? 30.181  109.882 56.634 1.00 21.12 ? 242  PRO B CD    1 
ATOM   5961 N N     . TYR B 1 243 ? 29.734  109.292 61.236 1.00 21.17 ? 243  TYR B N     1 
ATOM   5962 C CA    . TYR B 1 243 ? 30.159  109.856 62.523 1.00 20.22 ? 243  TYR B CA    1 
ATOM   5963 C C     . TYR B 1 243 ? 30.451  108.712 63.483 1.00 20.73 ? 243  TYR B C     1 
ATOM   5964 O O     . TYR B 1 243 ? 29.945  107.556 63.380 1.00 20.43 ? 243  TYR B O     1 
ATOM   5965 C CB    . TYR B 1 243 ? 29.112  110.857 63.011 1.00 20.97 ? 243  TYR B CB    1 
ATOM   5966 C CG    . TYR B 1 243 ? 27.766  110.248 63.324 1.00 20.37 ? 243  TYR B CG    1 
ATOM   5967 C CD1   . TYR B 1 243 ? 27.562  109.521 64.485 1.00 21.04 ? 243  TYR B CD1   1 
ATOM   5968 C CD2   . TYR B 1 243 ? 26.701  110.382 62.441 1.00 19.62 ? 243  TYR B CD2   1 
ATOM   5969 C CE1   . TYR B 1 243 ? 26.333  108.929 64.749 1.00 22.54 ? 243  TYR B CE1   1 
ATOM   5970 C CE2   . TYR B 1 243 ? 25.490  109.754 62.664 1.00 20.29 ? 243  TYR B CE2   1 
ATOM   5971 C CZ    . TYR B 1 243 ? 25.283  109.078 63.849 1.00 23.46 ? 243  TYR B CZ    1 
ATOM   5972 O OH    . TYR B 1 243 ? 24.067  108.480 64.064 1.00 22.75 ? 243  TYR B OH    1 
ATOM   5973 N N     . LEU B 1 244 ? 31.271  109.047 64.468 1.00 22.40 ? 244  LEU B N     1 
ATOM   5974 C CA    . LEU B 1 244 ? 31.569  108.205 65.635 1.00 22.28 ? 244  LEU B CA    1 
ATOM   5975 C C     . LEU B 1 244 ? 31.403  109.032 66.913 1.00 23.97 ? 244  LEU B C     1 
ATOM   5976 O O     . LEU B 1 244 ? 32.017  110.103 67.006 1.00 22.86 ? 244  LEU B O     1 
ATOM   5977 C CB    . LEU B 1 244 ? 32.994  107.690 65.472 1.00 23.33 ? 244  LEU B CB    1 
ATOM   5978 C CG    . LEU B 1 244 ? 33.547  106.950 66.684 1.00 24.09 ? 244  LEU B CG    1 
ATOM   5979 C CD1   . LEU B 1 244 ? 32.818  105.624 66.885 1.00 27.42 ? 244  LEU B CD1   1 
ATOM   5980 C CD2   . LEU B 1 244 ? 35.037  106.695 66.526 1.00 26.93 ? 244  LEU B CD2   1 
ATOM   5981 N N     . ILE B 1 245 ? 30.642  108.524 67.888 1.00 21.83 ? 245  ILE B N     1 
ATOM   5982 C CA    . ILE B 1 245 ? 30.537  109.139 69.241 1.00 21.40 ? 245  ILE B CA    1 
ATOM   5983 C C     . ILE B 1 245 ? 31.092  108.138 70.244 1.00 20.35 ? 245  ILE B C     1 
ATOM   5984 O O     . ILE B 1 245 ? 30.591  107.009 70.279 1.00 20.79 ? 245  ILE B O     1 
ATOM   5985 C CB    . ILE B 1 245 ? 29.091  109.558 69.523 1.00 22.69 ? 245  ILE B CB    1 
ATOM   5986 C CG1   . ILE B 1 245 ? 28.518  110.332 68.339 1.00 22.86 ? 245  ILE B CG1   1 
ATOM   5987 C CG2   . ILE B 1 245 ? 28.992  110.336 70.831 1.00 23.68 ? 245  ILE B CG2   1 
ATOM   5988 C CD1   . ILE B 1 245 ? 27.099  110.815 68.508 1.00 23.35 ? 245  ILE B CD1   1 
ATOM   5989 N N     . THR B 1 246 ? 32.142  108.475 71.009 1.00 22.26 ? 246  THR B N     1 
ATOM   5990 C CA    . THR B 1 246 ? 32.771  107.530 71.957 1.00 21.25 ? 246  THR B CA    1 
ATOM   5991 C C     . THR B 1 246 ? 32.394  107.885 73.402 1.00 23.35 ? 246  THR B C     1 
ATOM   5992 O O     . THR B 1 246 ? 32.120  109.052 73.698 1.00 21.29 ? 246  THR B O     1 
ATOM   5993 C CB    . THR B 1 246 ? 34.284  107.465 71.800 1.00 23.75 ? 246  THR B CB    1 
ATOM   5994 O OG1   . THR B 1 246 ? 34.794  108.712 72.248 1.00 22.01 ? 246  THR B OG1   1 
ATOM   5995 C CG2   . THR B 1 246 ? 34.708  107.212 70.379 1.00 23.02 ? 246  THR B CG2   1 
ATOM   5996 N N     . PHE B 1 247 ? 32.268  106.858 74.228 1.00 23.60 ? 247  PHE B N     1 
ATOM   5997 C CA    . PHE B 1 247 ? 31.890  107.000 75.658 1.00 24.71 ? 247  PHE B CA    1 
ATOM   5998 C C     . PHE B 1 247 ? 33.000  106.341 76.457 1.00 24.13 ? 247  PHE B C     1 
ATOM   5999 O O     . PHE B 1 247 ? 33.401  105.198 76.148 1.00 24.36 ? 247  PHE B O     1 
ATOM   6000 C CB    . PHE B 1 247 ? 30.490  106.408 75.910 1.00 23.42 ? 247  PHE B CB    1 
ATOM   6001 C CG    . PHE B 1 247 ? 29.433  106.974 74.991 1.00 21.35 ? 247  PHE B CG    1 
ATOM   6002 C CD1   . PHE B 1 247 ? 28.899  108.217 75.218 1.00 21.60 ? 247  PHE B CD1   1 
ATOM   6003 C CD2   . PHE B 1 247 ? 29.079  106.319 73.817 1.00 21.44 ? 247  PHE B CD2   1 
ATOM   6004 C CE1   . PHE B 1 247 ? 27.971  108.772 74.349 1.00 21.19 ? 247  PHE B CE1   1 
ATOM   6005 C CE2   . PHE B 1 247 ? 28.169  106.875 72.929 1.00 22.65 ? 247  PHE B CE2   1 
ATOM   6006 C CZ    . PHE B 1 247 ? 27.608  108.101 73.206 1.00 21.40 ? 247  PHE B CZ    1 
ATOM   6007 N N     . GLU B 1 248 ? 33.394  107.039 77.522 1.00 26.63 ? 248  GLU B N     1 
ATOM   6008 C CA    . GLU B 1 248 ? 34.509  106.706 78.449 1.00 28.52 ? 248  GLU B CA    1 
ATOM   6009 C C     . GLU B 1 248 ? 34.197  105.472 79.310 1.00 28.32 ? 248  GLU B C     1 
ATOM   6010 O O     . GLU B 1 248 ? 35.156  104.719 79.612 1.00 30.49 ? 248  GLU B O     1 
ATOM   6011 C CB    . GLU B 1 248 ? 34.752  107.981 79.269 1.00 35.31 ? 248  GLU B CB    1 
ATOM   6012 C CG    . GLU B 1 248 ? 35.839  107.878 80.313 1.00 44.29 ? 248  GLU B CG    1 
ATOM   6013 C CD    . GLU B 1 248 ? 37.257  107.747 79.763 1.00 47.42 ? 248  GLU B CD    1 
ATOM   6014 O OE1   . GLU B 1 248 ? 38.166  107.361 80.561 1.00 37.33 ? 248  GLU B OE1   1 
ATOM   6015 O OE2   . GLU B 1 248 ? 37.447  107.993 78.527 1.00 39.97 ? 248  GLU B OE2   1 
ATOM   6016 N N     . ASN B 1 249 ? 32.954  105.292 79.789 1.00 27.10 ? 249  ASN B N     1 
ATOM   6017 C CA    . ASN B 1 249 ? 32.649  104.369 80.933 1.00 25.05 ? 249  ASN B CA    1 
ATOM   6018 C C     . ASN B 1 249 ? 31.805  103.192 80.463 1.00 25.63 ? 249  ASN B C     1 
ATOM   6019 O O     . ASN B 1 249 ? 30.825  103.462 79.732 1.00 25.09 ? 249  ASN B O     1 
ATOM   6020 C CB    . ASN B 1 249 ? 31.946  105.151 82.039 1.00 31.33 ? 249  ASN B CB    1 
ATOM   6021 C CG    . ASN B 1 249 ? 32.751  106.368 82.449 1.00 31.72 ? 249  ASN B CG    1 
ATOM   6022 O OD1   . ASN B 1 249 ? 32.377  107.524 82.215 1.00 37.79 ? 249  ASN B OD1   1 
ATOM   6023 N ND2   . ASN B 1 249 ? 33.882  106.086 83.067 1.00 30.32 ? 249  ASN B ND2   1 
ATOM   6024 N N     . GLU B 1 250 ? 32.117  101.957 80.871 1.00 24.97 ? 250  GLU B N     1 
ATOM   6025 C CA    . GLU B 1 250 ? 31.263  100.793 80.497 1.00 27.15 ? 250  GLU B CA    1 
ATOM   6026 C C     . GLU B 1 250 ? 29.813  101.087 80.911 1.00 27.16 ? 250  GLU B C     1 
ATOM   6027 O O     . GLU B 1 250 ? 28.890  100.683 80.172 1.00 27.50 ? 250  GLU B O     1 
ATOM   6028 C CB    . GLU B 1 250 ? 31.828  99.478  81.026 1.00 30.69 ? 250  GLU B CB    1 
ATOM   6029 C CG    . GLU B 1 250 ? 31.832  99.338  82.532 1.00 31.26 ? 250  GLU B CG    1 
ATOM   6030 C CD    . GLU B 1 250 ? 32.418  97.997  82.935 1.00 34.09 ? 250  GLU B CD    1 
ATOM   6031 O OE1   . GLU B 1 250 ? 32.574  97.102  82.029 1.00 32.64 ? 250  GLU B OE1   1 
ATOM   6032 O OE2   . GLU B 1 250 ? 32.699  97.841  84.135 1.00 35.42 ? 250  GLU B OE2   1 
ATOM   6033 N N     . ASP B 1 251 ? 29.574  101.786 82.023 1.00 28.48 ? 251  ASP B N     1 
ATOM   6034 C CA    . ASP B 1 251 ? 28.181  101.953 82.543 1.00 27.67 ? 251  ASP B CA    1 
ATOM   6035 C C     . ASP B 1 251 ? 27.455  103.050 81.752 1.00 28.09 ? 251  ASP B C     1 
ATOM   6036 O O     . ASP B 1 251 ? 26.228  103.202 81.927 1.00 25.47 ? 251  ASP B O     1 
ATOM   6037 C CB    . ASP B 1 251 ? 28.158  102.216 84.049 1.00 30.01 ? 251  ASP B CB    1 
ATOM   6038 C CG    . ASP B 1 251 ? 28.504  101.018 84.926 1.00 34.04 ? 251  ASP B CG    1 
ATOM   6039 O OD1   . ASP B 1 251 ? 28.661  99.862  84.423 1.00 34.72 ? 251  ASP B OD1   1 
ATOM   6040 O OD2   . ASP B 1 251 ? 28.616  101.241 86.123 1.00 42.34 ? 251  ASP B OD2   1 
ATOM   6041 N N     . ASP B 1 252 ? 28.141  103.795 80.884 1.00 26.81 ? 252  ASP B N     1 
ATOM   6042 C CA    . ASP B 1 252 ? 27.464  104.821 80.051 1.00 24.83 ? 252  ASP B CA    1 
ATOM   6043 C C     . ASP B 1 252 ? 26.452  104.142 79.120 1.00 19.96 ? 252  ASP B C     1 
ATOM   6044 O O     . ASP B 1 252 ? 25.590  104.821 78.650 1.00 22.46 ? 252  ASP B O     1 
ATOM   6045 C CB    . ASP B 1 252 ? 28.440  105.661 79.220 1.00 27.71 ? 252  ASP B CB    1 
ATOM   6046 C CG    . ASP B 1 252 ? 29.280  106.678 79.987 1.00 29.78 ? 252  ASP B CG    1 
ATOM   6047 O OD1   . ASP B 1 252 ? 28.840  107.099 81.015 1.00 29.55 ? 252  ASP B OD1   1 
ATOM   6048 O OD2   . ASP B 1 252 ? 30.382  107.041 79.517 1.00 29.83 ? 252  ASP B OD2   1 
ATOM   6049 N N     . ILE B 1 253 ? 26.562  102.854 78.829 1.00 23.22 ? 253  ILE B N     1 
ATOM   6050 C CA    . ILE B 1 253 ? 25.631  102.229 77.843 1.00 25.13 ? 253  ILE B CA    1 
ATOM   6051 C C     . ILE B 1 253 ? 24.174  102.379 78.327 1.00 26.10 ? 253  ILE B C     1 
ATOM   6052 O O     . ILE B 1 253 ? 23.242  102.448 77.485 1.00 24.62 ? 253  ILE B O     1 
ATOM   6053 C CB    . ILE B 1 253 ? 26.019  100.780 77.535 1.00 27.49 ? 253  ILE B CB    1 
ATOM   6054 C CG1   . ILE B 1 253 ? 25.294  100.301 76.272 1.00 28.15 ? 253  ILE B CG1   1 
ATOM   6055 C CG2   . ILE B 1 253 ? 25.845  99.842  78.743 1.00 26.81 ? 253  ILE B CG2   1 
ATOM   6056 C CD1   . ILE B 1 253 ? 25.494  101.196 75.062 1.00 27.78 ? 253  ILE B CD1   1 
ATOM   6057 N N     . GLU B 1 254 ? 23.953  102.510 79.628 1.00 26.00 ? 254  GLU B N     1 
ATOM   6058 C CA    . GLU B 1 254 ? 22.571  102.661 80.153 1.00 25.21 ? 254  GLU B CA    1 
ATOM   6059 C C     . GLU B 1 254 ? 21.981  103.983 79.669 1.00 25.22 ? 254  GLU B C     1 
ATOM   6060 O O     . GLU B 1 254 ? 20.980  103.949 78.986 1.00 24.55 ? 254  GLU B O     1 
ATOM   6061 C CB    . GLU B 1 254 ? 22.539  102.608 81.685 1.00 26.53 ? 254  GLU B CB    1 
ATOM   6062 C CG    . GLU B 1 254 ? 21.120  102.653 82.218 1.00 26.93 ? 254  GLU B CG    1 
ATOM   6063 C CD    . GLU B 1 254 ? 20.980  102.332 83.700 1.00 31.50 ? 254  GLU B CD    1 
ATOM   6064 O OE1   . GLU B 1 254 ? 21.947  101.860 84.316 1.00 31.52 ? 254  GLU B OE1   1 
ATOM   6065 O OE2   . GLU B 1 254 ? 19.902  102.580 84.228 1.00 33.08 ? 254  GLU B OE2   1 
ATOM   6066 N N     . THR B 1 255 ? 22.589  105.116 79.974 1.00 21.28 ? 255  THR B N     1 
ATOM   6067 C CA    . THR B 1 255 ? 22.037  106.417 79.544 1.00 24.89 ? 255  THR B CA    1 
ATOM   6068 C C     . THR B 1 255 ? 22.101  106.555 78.012 1.00 22.44 ? 255  THR B C     1 
ATOM   6069 O O     . THR B 1 255 ? 21.186  107.185 77.412 1.00 22.91 ? 255  THR B O     1 
ATOM   6070 C CB    . THR B 1 255 ? 22.690  107.583 80.309 1.00 26.35 ? 255  THR B CB    1 
ATOM   6071 O OG1   . THR B 1 255 ? 21.922  108.753 80.088 1.00 27.31 ? 255  THR B OG1   1 
ATOM   6072 C CG2   . THR B 1 255 ? 24.075  107.924 79.843 1.00 31.94 ? 255  THR B CG2   1 
ATOM   6073 N N     . VAL B 1 256 ? 23.167  106.060 77.385 1.00 23.62 ? 256  VAL B N     1 
ATOM   6074 C CA    . VAL B 1 256 ? 23.328  106.144 75.900 1.00 21.11 ? 256  VAL B CA    1 
ATOM   6075 C C     . VAL B 1 256 ? 22.104  105.468 75.236 1.00 19.92 ? 256  VAL B C     1 
ATOM   6076 O O     . VAL B 1 256 ? 21.515  106.087 74.344 1.00 21.09 ? 256  VAL B O     1 
ATOM   6077 C CB    . VAL B 1 256 ? 24.659  105.491 75.478 1.00 20.22 ? 256  VAL B CB    1 
ATOM   6078 C CG1   . VAL B 1 256 ? 24.654  105.185 73.978 1.00 20.81 ? 256  VAL B CG1   1 
ATOM   6079 C CG2   . VAL B 1 256 ? 25.842  106.370 75.832 1.00 20.78 ? 256  VAL B CG2   1 
ATOM   6080 N N     . THR B 1 257 ? 21.703  104.280 75.708 1.00 22.07 ? 257  THR B N     1 
ATOM   6081 C CA    . THR B 1 257 ? 20.556  103.520 75.140 1.00 24.10 ? 257  THR B CA    1 
ATOM   6082 C C     . THR B 1 257 ? 19.261  104.299 75.363 1.00 23.88 ? 257  THR B C     1 
ATOM   6083 O O     . THR B 1 257 ? 18.435  104.383 74.444 1.00 21.33 ? 257  THR B O     1 
ATOM   6084 C CB    . THR B 1 257 ? 20.480  102.111 75.703 1.00 22.82 ? 257  THR B CB    1 
ATOM   6085 O OG1   . THR B 1 257 ? 21.727  101.505 75.384 1.00 23.86 ? 257  THR B OG1   1 
ATOM   6086 C CG2   . THR B 1 257 ? 19.307  101.346 75.112 1.00 21.75 ? 257  THR B CG2   1 
ATOM   6087 N N     . GLU B 1 258 ? 19.065  104.891 76.544 1.00 23.75 ? 258  GLU B N     1 
ATOM   6088 C CA    . GLU B 1 258 ? 17.885  105.751 76.798 1.00 21.58 ? 258  GLU B CA    1 
ATOM   6089 C C     . GLU B 1 258 ? 17.804  106.870 75.760 1.00 22.60 ? 258  GLU B C     1 
ATOM   6090 O O     . GLU B 1 258 ? 16.673  107.224 75.304 1.00 21.55 ? 258  GLU B O     1 
ATOM   6091 C CB    . GLU B 1 258 ? 17.947  106.336 78.230 1.00 22.70 ? 258  GLU B CB    1 
ATOM   6092 C CG    . GLU B 1 258 ? 17.645  105.274 79.282 1.00 23.93 ? 258  GLU B CG    1 
ATOM   6093 C CD    . GLU B 1 258 ? 16.253  104.660 79.133 1.00 21.82 ? 258  GLU B CD    1 
ATOM   6094 O OE1   . GLU B 1 258 ? 15.321  105.410 79.352 1.00 25.19 ? 258  GLU B OE1   1 
ATOM   6095 O OE2   . GLU B 1 258 ? 16.100  103.466 78.747 1.00 23.95 ? 258  GLU B OE2   1 
ATOM   6096 N N     . ARG B 1 259 ? 18.926  107.501 75.448 1.00 23.18 ? 259  ARG B N     1 
ATOM   6097 C CA    . ARG B 1 259 ? 18.965  108.625 74.484 1.00 22.26 ? 259  ARG B CA    1 
ATOM   6098 C C     . ARG B 1 259 ? 18.787  108.141 73.039 1.00 19.90 ? 259  ARG B C     1 
ATOM   6099 O O     . ARG B 1 259 ? 18.191  108.883 72.238 1.00 21.51 ? 259  ARG B O     1 
ATOM   6100 C CB    . ARG B 1 259 ? 20.279  109.402 74.640 1.00 23.23 ? 259  ARG B CB    1 
ATOM   6101 C CG    . ARG B 1 259 ? 20.413  110.146 75.964 1.00 28.03 ? 259  ARG B CG    1 
ATOM   6102 C CD    . ARG B 1 259 ? 21.860  110.139 76.411 1.00 31.26 ? 259  ARG B CD    1 
ATOM   6103 N NE    . ARG B 1 259 ? 22.043  110.554 77.812 1.00 30.73 ? 259  ARG B NE    1 
ATOM   6104 C CZ    . ARG B 1 259 ? 22.330  111.783 78.222 1.00 34.64 ? 259  ARG B CZ    1 
ATOM   6105 N NH1   . ARG B 1 259 ? 22.509  112.768 77.353 1.00 29.71 ? 259  ARG B NH1   1 
ATOM   6106 N NH2   . ARG B 1 259 ? 22.483  112.000 79.520 1.00 35.26 ? 259  ARG B NH2   1 
ATOM   6107 N N     . LEU B 1 260 ? 19.270  106.940 72.692 1.00 21.44 ? 260  LEU B N     1 
ATOM   6108 C CA    . LEU B 1 260 ? 19.110  106.382 71.314 1.00 21.36 ? 260  LEU B CA    1 
ATOM   6109 C C     . LEU B 1 260 ? 17.634  106.109 71.013 1.00 22.69 ? 260  LEU B C     1 
ATOM   6110 O O     . LEU B 1 260 ? 17.221  106.267 69.874 1.00 20.30 ? 260  LEU B O     1 
ATOM   6111 C CB    . LEU B 1 260 ? 19.877  105.057 71.197 1.00 20.20 ? 260  LEU B CB    1 
ATOM   6112 C CG    . LEU B 1 260 ? 21.388  105.156 71.167 1.00 23.09 ? 260  LEU B CG    1 
ATOM   6113 C CD1   . LEU B 1 260 ? 22.030  103.780 71.234 1.00 22.90 ? 260  LEU B CD1   1 
ATOM   6114 C CD2   . LEU B 1 260 ? 21.825  105.856 69.888 1.00 24.70 ? 260  LEU B CD2   1 
ATOM   6115 N N     . ARG B 1 261 ? 16.867  105.657 72.001 1.00 21.98 ? 261  ARG B N     1 
ATOM   6116 C CA    . ARG B 1 261 ? 15.482  105.190 71.756 1.00 20.87 ? 261  ARG B CA    1 
ATOM   6117 C C     . ARG B 1 261 ? 14.651  106.249 71.023 1.00 20.63 ? 261  ARG B C     1 
ATOM   6118 O O     . ARG B 1 261 ? 14.153  105.942 69.953 1.00 20.67 ? 261  ARG B O     1 
ATOM   6119 C CB    . ARG B 1 261 ? 14.808  104.732 73.054 1.00 20.27 ? 261  ARG B CB    1 
ATOM   6120 C CG    . ARG B 1 261 ? 13.379  104.264 72.810 1.00 22.07 ? 261  ARG B CG    1 
ATOM   6121 C CD    . ARG B 1 261 ? 12.715  103.866 74.122 1.00 23.37 ? 261  ARG B CD    1 
ATOM   6122 N NE    . ARG B 1 261 ? 12.777  104.833 75.205 1.00 21.61 ? 261  ARG B NE    1 
ATOM   6123 C CZ    . ARG B 1 261 ? 13.489  104.728 76.330 1.00 25.82 ? 261  ARG B CZ    1 
ATOM   6124 N NH1   . ARG B 1 261 ? 14.269  103.693 76.587 1.00 27.64 ? 261  ARG B NH1   1 
ATOM   6125 N NH2   . ARG B 1 261 ? 13.457  105.704 77.206 1.00 26.64 ? 261  ARG B NH2   1 
ATOM   6126 N N     . PRO B 1 262 ? 14.402  107.479 71.534 1.00 18.58 ? 262  PRO B N     1 
ATOM   6127 C CA    . PRO B 1 262 ? 13.540  108.423 70.814 1.00 21.60 ? 262  PRO B CA    1 
ATOM   6128 C C     . PRO B 1 262 ? 14.099  108.776 69.414 1.00 21.70 ? 262  PRO B C     1 
ATOM   6129 O O     . PRO B 1 262 ? 13.332  108.971 68.469 1.00 20.18 ? 262  PRO B O     1 
ATOM   6130 C CB    . PRO B 1 262 ? 13.442  109.632 71.781 1.00 21.24 ? 262  PRO B CB    1 
ATOM   6131 C CG    . PRO B 1 262 ? 14.658  109.495 72.694 1.00 21.35 ? 262  PRO B CG    1 
ATOM   6132 C CD    . PRO B 1 262 ? 14.847  108.002 72.822 1.00 21.31 ? 262  PRO B CD    1 
ATOM   6133 N N     . LEU B 1 263 ? 15.420  108.880 69.297 1.00 20.92 ? 263  LEU B N     1 
ATOM   6134 C CA    . LEU B 1 263 ? 16.076  109.203 67.992 1.00 19.84 ? 263  LEU B CA    1 
ATOM   6135 C C     . LEU B 1 263 ? 15.794  108.080 66.990 1.00 20.16 ? 263  LEU B C     1 
ATOM   6136 O O     . LEU B 1 263 ? 15.538  108.397 65.840 1.00 20.97 ? 263  LEU B O     1 
ATOM   6137 C CB    . LEU B 1 263 ? 17.584  109.362 68.180 1.00 20.74 ? 263  LEU B CB    1 
ATOM   6138 C CG    . LEU B 1 263 ? 18.013  110.532 69.062 1.00 22.20 ? 263  LEU B CG    1 
ATOM   6139 C CD1   . LEU B 1 263 ? 19.490  110.408 69.303 1.00 23.25 ? 263  LEU B CD1   1 
ATOM   6140 C CD2   . LEU B 1 263 ? 17.638  111.861 68.399 1.00 22.12 ? 263  LEU B CD2   1 
ATOM   6141 N N     . LYS B 1 264 ? 15.902  106.813 67.393 1.00 19.66 ? 264  LYS B N     1 
ATOM   6142 C CA    . LYS B 1 264 ? 15.639  105.701 66.428 1.00 19.85 ? 264  LYS B CA    1 
ATOM   6143 C C     . LYS B 1 264 ? 14.134  105.569 66.154 1.00 21.02 ? 264  LYS B C     1 
ATOM   6144 O O     . LYS B 1 264 ? 13.736  105.483 64.982 1.00 19.76 ? 264  LYS B O     1 
ATOM   6145 C CB    . LYS B 1 264 ? 16.254  104.401 66.926 1.00 21.79 ? 264  LYS B CB    1 
ATOM   6146 C CG    . LYS B 1 264 ? 16.131  103.265 65.904 1.00 25.62 ? 264  LYS B CG    1 
ATOM   6147 C CD    . LYS B 1 264 ? 17.020  103.540 64.680 1.00 27.44 ? 264  LYS B CD    1 
ATOM   6148 C CE    . LYS B 1 264 ? 16.879  102.512 63.587 1.00 30.01 ? 264  LYS B CE    1 
ATOM   6149 N NZ    . LYS B 1 264 ? 17.256  103.040 62.267 1.00 30.16 ? 264  LYS B NZ    1 
ATOM   6150 N N     . VAL B 1 265 ? 13.287  105.604 67.180 1.00 20.57 ? 265  VAL B N     1 
ATOM   6151 C CA    . VAL B 1 265 ? 11.830  105.383 66.979 1.00 23.80 ? 265  VAL B CA    1 
ATOM   6152 C C     . VAL B 1 265 ? 11.291  106.448 65.999 1.00 22.84 ? 265  VAL B C     1 
ATOM   6153 O O     . VAL B 1 265 ? 10.381  106.112 65.204 1.00 24.11 ? 265  VAL B O     1 
ATOM   6154 C CB    . VAL B 1 265 ? 11.099  105.342 68.346 1.00 25.49 ? 265  VAL B CB    1 
ATOM   6155 C CG1   . VAL B 1 265 ? 9.601   105.281 68.168 1.00 28.17 ? 265  VAL B CG1   1 
ATOM   6156 C CG2   . VAL B 1 265 ? 11.549  104.184 69.228 1.00 25.82 ? 265  VAL B CG2   1 
ATOM   6157 N N     . ALA B 1 266 ? 11.812  107.681 66.033 1.00 21.27 ? 266  ALA B N     1 
ATOM   6158 C CA    . ALA B 1 266 ? 11.369  108.807 65.186 1.00 22.45 ? 266  ALA B CA    1 
ATOM   6159 C C     . ALA B 1 266 ? 12.119  108.788 63.849 1.00 21.30 ? 266  ALA B C     1 
ATOM   6160 O O     . ALA B 1 266 ? 11.732  109.532 62.982 1.00 22.30 ? 266  ALA B O     1 
ATOM   6161 C CB    . ALA B 1 266 ? 11.581  110.146 65.864 1.00 23.43 ? 266  ALA B CB    1 
ATOM   6162 N N     . GLY B 1 267 ? 13.124  107.932 63.691 1.00 20.33 ? 267  GLY B N     1 
ATOM   6163 C CA    . GLY B 1 267 ? 13.898  107.839 62.447 1.00 21.85 ? 267  GLY B CA    1 
ATOM   6164 C C     . GLY B 1 267 ? 14.919  108.957 62.266 1.00 21.54 ? 267  GLY B C     1 
ATOM   6165 O O     . GLY B 1 267 ? 15.477  109.085 61.176 1.00 21.96 ? 267  GLY B O     1 
ATOM   6166 N N     . VAL B 1 268 ? 15.287  109.663 63.333 1.00 21.96 ? 268  VAL B N     1 
ATOM   6167 C CA    . VAL B 1 268 ? 16.371  110.679 63.276 1.00 21.57 ? 268  VAL B CA    1 
ATOM   6168 C C     . VAL B 1 268 ? 17.715  109.955 63.051 1.00 20.66 ? 268  VAL B C     1 
ATOM   6169 O O     . VAL B 1 268 ? 18.588  110.432 62.268 1.00 21.32 ? 268  VAL B O     1 
ATOM   6170 C CB    . VAL B 1 268 ? 16.357  111.508 64.572 1.00 21.16 ? 268  VAL B CB    1 
ATOM   6171 C CG1   . VAL B 1 268 ? 17.565  112.422 64.643 1.00 23.19 ? 268  VAL B CG1   1 
ATOM   6172 C CG2   . VAL B 1 268 ? 15.060  112.293 64.713 1.00 24.12 ? 268  VAL B CG2   1 
ATOM   6173 N N     . ILE B 1 269 ? 17.911  108.815 63.689 1.00 20.01 ? 269  ILE B N     1 
ATOM   6174 C CA    . ILE B 1 269 ? 19.014  107.885 63.317 1.00 21.49 ? 269  ILE B CA    1 
ATOM   6175 C C     . ILE B 1 269 ? 18.479  107.048 62.142 1.00 20.70 ? 269  ILE B C     1 
ATOM   6176 O O     . ILE B 1 269 ? 17.535  106.289 62.320 1.00 21.63 ? 269  ILE B O     1 
ATOM   6177 C CB    . ILE B 1 269 ? 19.407  107.022 64.533 1.00 22.84 ? 269  ILE B CB    1 
ATOM   6178 C CG1   . ILE B 1 269 ? 20.042  107.880 65.637 1.00 22.40 ? 269  ILE B CG1   1 
ATOM   6179 C CG2   . ILE B 1 269 ? 20.318  105.875 64.114 1.00 22.01 ? 269  ILE B CG2   1 
ATOM   6180 C CD1   . ILE B 1 269 ? 20.251  107.084 66.935 1.00 26.14 ? 269  ILE B CD1   1 
ATOM   6181 N N     . GLN B 1 270 ? 18.989  107.283 60.950 1.00 20.14 ? 270  GLN B N     1 
ATOM   6182 C CA    . GLN B 1 270 ? 18.364  106.802 59.694 1.00 20.22 ? 270  GLN B CA    1 
ATOM   6183 C C     . GLN B 1 270 ? 18.772  105.356 59.404 1.00 18.94 ? 270  GLN B C     1 
ATOM   6184 O O     . GLN B 1 270 ? 18.019  104.653 58.694 1.00 22.84 ? 270  GLN B O     1 
ATOM   6185 C CB    . GLN B 1 270 ? 18.812  107.758 58.584 1.00 19.97 ? 270  GLN B CB    1 
ATOM   6186 C CG    . GLN B 1 270 ? 18.133  109.131 58.621 1.00 20.67 ? 270  GLN B CG    1 
ATOM   6187 C CD    . GLN B 1 270 ? 18.940  110.082 57.770 1.00 20.67 ? 270  GLN B CD    1 
ATOM   6188 O OE1   . GLN B 1 270 ? 20.098  110.354 58.048 1.00 20.09 ? 270  GLN B OE1   1 
ATOM   6189 N NE2   . GLN B 1 270 ? 18.343  110.547 56.706 1.00 19.79 ? 270  GLN B NE2   1 
ATOM   6190 N N     . ASN B 1 271 ? 19.942  104.927 59.863 1.00 19.53 ? 271  ASN B N     1 
ATOM   6191 C CA    . ASN B 1 271 ? 20.536  103.601 59.510 1.00 20.34 ? 271  ASN B CA    1 
ATOM   6192 C C     . ASN B 1 271 ? 20.468  102.640 60.707 1.00 21.33 ? 271  ASN B C     1 
ATOM   6193 O O     . ASN B 1 271 ? 20.152  103.080 61.813 1.00 21.54 ? 271  ASN B O     1 
ATOM   6194 C CB    . ASN B 1 271 ? 21.959  103.692 58.952 1.00 21.55 ? 271  ASN B CB    1 
ATOM   6195 C CG    . ASN B 1 271 ? 22.989  104.328 59.885 1.00 19.59 ? 271  ASN B CG    1 
ATOM   6196 O OD1   . ASN B 1 271 ? 22.720  105.213 60.686 1.00 22.74 ? 271  ASN B OD1   1 
ATOM   6197 N ND2   . ASN B 1 271 ? 24.212  103.913 59.733 1.00 20.61 ? 271  ASN B ND2   1 
ATOM   6198 N N     . GLY B 1 272 ? 20.757  101.377 60.422 1.00 24.26 ? 272  GLY B N     1 
ATOM   6199 C CA    . GLY B 1 272 ? 21.128  100.343 61.390 1.00 26.45 ? 272  GLY B CA    1 
ATOM   6200 C C     . GLY B 1 272 ? 22.473  100.670 62.000 1.00 27.79 ? 272  GLY B C     1 
ATOM   6201 O O     . GLY B 1 272 ? 23.426  99.830  61.875 1.00 27.70 ? 272  GLY B O     1 
ATOM   6202 N N     . ALA B 1 273 ? 22.525  101.811 62.690 1.00 24.67 ? 273  ALA B N     1 
ATOM   6203 C CA    . ALA B 1 273 ? 23.718  102.266 63.408 1.00 26.08 ? 273  ALA B CA    1 
ATOM   6204 C C     . ALA B 1 273 ? 24.079  101.225 64.479 1.00 27.40 ? 273  ALA B C     1 
ATOM   6205 O O     . ALA B 1 273 ? 23.187  100.398 64.828 1.00 25.25 ? 273  ALA B O     1 
ATOM   6206 C CB    . ALA B 1 273 ? 23.446  103.641 63.956 1.00 26.51 ? 273  ALA B CB    1 
ATOM   6207 N N     . THR B 1 274 ? 25.304  101.297 65.028 1.00 23.08 ? 274  THR B N     1 
ATOM   6208 C CA    . THR B 1 274 ? 25.842  100.320 65.988 1.00 22.56 ? 274  THR B CA    1 
ATOM   6209 C C     . THR B 1 274 ? 26.463  101.007 67.187 1.00 21.85 ? 274  THR B C     1 
ATOM   6210 O O     . THR B 1 274 ? 27.105  102.072 67.046 1.00 23.18 ? 274  THR B O     1 
ATOM   6211 C CB    . THR B 1 274 ? 26.843  99.418  65.272 1.00 24.79 ? 274  THR B CB    1 
ATOM   6212 O OG1   . THR B 1 274 ? 27.831  100.243 64.663 1.00 23.69 ? 274  THR B OG1   1 
ATOM   6213 C CG2   . THR B 1 274 ? 26.210  98.577  64.176 1.00 25.44 ? 274  THR B CG2   1 
ATOM   6214 N N     . VAL B 1 275 ? 26.408  100.346 68.312 1.00 21.90 ? 275  VAL B N     1 
ATOM   6215 C CA    . VAL B 1 275 ? 27.236  100.713 69.493 1.00 21.79 ? 275  VAL B CA    1 
ATOM   6216 C C     . VAL B 1 275 ? 28.089  99.473  69.806 1.00 26.61 ? 275  VAL B C     1 
ATOM   6217 O O     . VAL B 1 275 ? 27.514  98.354  70.075 1.00 25.79 ? 275  VAL B O     1 
ATOM   6218 C CB    . VAL B 1 275 ? 26.412  101.164 70.712 1.00 24.92 ? 275  VAL B CB    1 
ATOM   6219 C CG1   . VAL B 1 275 ? 27.327  101.798 71.751 1.00 26.70 ? 275  VAL B CG1   1 
ATOM   6220 C CG2   . VAL B 1 275 ? 25.316  102.113 70.327 1.00 25.74 ? 275  VAL B CG2   1 
ATOM   6221 N N     . ARG B 1 276 ? 29.408  99.608  69.654 1.00 24.67 ? 276  ARG B N     1 
ATOM   6222 C CA    . ARG B 1 276 ? 30.365  98.471  69.674 1.00 25.23 ? 276  ARG B CA    1 
ATOM   6223 C C     . ARG B 1 276 ? 31.271  98.668  70.890 1.00 23.83 ? 276  ARG B C     1 
ATOM   6224 O O     . ARG B 1 276 ? 31.647  99.822  71.203 1.00 21.82 ? 276  ARG B O     1 
ATOM   6225 C CB    . ARG B 1 276 ? 31.060  98.379  68.310 1.00 27.64 ? 276  ARG B CB    1 
ATOM   6226 C CG    . ARG B 1 276 ? 30.123  97.863  67.217 1.00 33.69 ? 276  ARG B CG    1 
ATOM   6227 C CD    . ARG B 1 276 ? 30.616  97.980  65.769 1.00 35.35 ? 276  ARG B CD    1 
ATOM   6228 N NE    . ARG B 1 276 ? 31.993  97.608  65.585 1.00 30.61 ? 276  ARG B NE    1 
ATOM   6229 C CZ    . ARG B 1 276 ? 32.484  96.565  64.884 1.00 35.90 ? 276  ARG B CZ    1 
ATOM   6230 N NH1   . ARG B 1 276 ? 31.689  95.657  64.331 1.00 30.86 ? 276  ARG B NH1   1 
ATOM   6231 N NH2   . ARG B 1 276 ? 33.805  96.380  64.828 1.00 34.98 ? 276  ARG B NH2   1 
ATOM   6232 N N     . SER B 1 277 ? 31.579  97.586  71.583 1.00 22.30 ? 277  SER B N     1 
ATOM   6233 C CA    . SER B 1 277 ? 32.434  97.654  72.780 1.00 24.70 ? 277  SER B CA    1 
ATOM   6234 C C     . SER B 1 277 ? 33.902  97.886  72.343 1.00 25.33 ? 277  SER B C     1 
ATOM   6235 O O     . SER B 1 277 ? 34.285  97.542  71.198 1.00 22.05 ? 277  SER B O     1 
ATOM   6236 C CB    . SER B 1 277 ? 32.285  96.427  73.643 1.00 22.40 ? 277  SER B CB    1 
ATOM   6237 O OG    . SER B 1 277 ? 32.894  95.326  73.004 1.00 24.14 ? 277  SER B OG    1 
ATOM   6238 N N     . LEU B 1 278 ? 34.714  98.393  73.253 1.00 22.41 ? 278  LEU B N     1 
ATOM   6239 C CA    . LEU B 1 278 ? 36.154  98.692  72.995 1.00 23.38 ? 278  LEU B CA    1 
ATOM   6240 C C     . LEU B 1 278 ? 36.856  97.534  72.274 1.00 22.87 ? 278  LEU B C     1 
ATOM   6241 O O     . LEU B 1 278 ? 37.513  97.767  71.271 1.00 24.07 ? 278  LEU B O     1 
ATOM   6242 C CB    . LEU B 1 278 ? 36.843  98.896  74.338 1.00 22.63 ? 278  LEU B CB    1 
ATOM   6243 C CG    . LEU B 1 278 ? 38.357  99.029  74.250 1.00 24.75 ? 278  LEU B CG    1 
ATOM   6244 C CD1   . LEU B 1 278 ? 38.724  100.257 73.419 1.00 23.52 ? 278  LEU B CD1   1 
ATOM   6245 C CD2   . LEU B 1 278 ? 38.941  99.147  75.651 1.00 24.78 ? 278  LEU B CD2   1 
ATOM   6246 N N     . VAL B 1 279 ? 36.809  96.327  72.806 1.00 21.89 ? 279  VAL B N     1 
ATOM   6247 C CA    . VAL B 1 279 ? 37.729  95.272  72.301 1.00 22.20 ? 279  VAL B CA    1 
ATOM   6248 C C     . VAL B 1 279 ? 37.286  94.908  70.898 1.00 24.58 ? 279  VAL B C     1 
ATOM   6249 O O     . VAL B 1 279 ? 38.158  94.604  70.063 1.00 24.22 ? 279  VAL B O     1 
ATOM   6250 C CB    . VAL B 1 279 ? 37.813  94.075  73.266 1.00 23.60 ? 279  VAL B CB    1 
ATOM   6251 C CG1   . VAL B 1 279 ? 38.667  92.943  72.757 1.00 24.49 ? 279  VAL B CG1   1 
ATOM   6252 C CG2   . VAL B 1 279 ? 38.314  94.523  74.621 1.00 24.28 ? 279  VAL B CG2   1 
ATOM   6253 N N     . LEU B 1 280 ? 35.974  94.900  70.635 1.00 23.05 ? 280  LEU B N     1 
ATOM   6254 C CA    . LEU B 1 280 ? 35.497  94.537  69.275 1.00 25.58 ? 280  LEU B CA    1 
ATOM   6255 C C     . LEU B 1 280 ? 36.108  95.549  68.298 1.00 23.16 ? 280  LEU B C     1 
ATOM   6256 O O     . LEU B 1 280 ? 36.545  95.155  67.237 1.00 24.77 ? 280  LEU B O     1 
ATOM   6257 C CB    . LEU B 1 280 ? 33.971  94.544  69.236 1.00 24.71 ? 280  LEU B CB    1 
ATOM   6258 C CG    . LEU B 1 280 ? 33.366  94.316  67.856 1.00 23.88 ? 280  LEU B CG    1 
ATOM   6259 C CD1   . LEU B 1 280 ? 33.964  93.083  67.189 1.00 25.03 ? 280  LEU B CD1   1 
ATOM   6260 C CD2   . LEU B 1 280 ? 31.866  94.172  67.981 1.00 27.63 ? 280  LEU B CD2   1 
ATOM   6261 N N     . ASP B 1 281 ? 36.169  96.811  68.668 1.00 23.68 ? 281  ASP B N     1 
ATOM   6262 C CA    . ASP B 1 281 ? 36.628  97.887  67.750 1.00 23.65 ? 281  ASP B CA    1 
ATOM   6263 C C     . ASP B 1 281 ? 38.162  97.931  67.715 1.00 23.55 ? 281  ASP B C     1 
ATOM   6264 O O     . ASP B 1 281 ? 38.703  97.979  66.589 1.00 25.18 ? 281  ASP B O     1 
ATOM   6265 C CB    . ASP B 1 281 ? 36.044  99.228  68.122 1.00 23.76 ? 281  ASP B CB    1 
ATOM   6266 C CG    . ASP B 1 281 ? 34.634  99.435  67.590 1.00 29.08 ? 281  ASP B CG    1 
ATOM   6267 O OD1   . ASP B 1 281 ? 34.208  98.660  66.694 1.00 27.93 ? 281  ASP B OD1   1 
ATOM   6268 O OD2   . ASP B 1 281 ? 33.981  100.360 68.084 1.00 31.66 ? 281  ASP B OD2   1 
ATOM   6269 N N     . ALA B 1 282 ? 38.832  97.715  68.850 1.00 20.06 ? 282  ALA B N     1 
ATOM   6270 C CA    . ALA B 1 282 ? 40.304  97.707  68.889 1.00 21.82 ? 282  ALA B CA    1 
ATOM   6271 C C     . ALA B 1 282 ? 40.842  96.554  68.039 1.00 25.20 ? 282  ALA B C     1 
ATOM   6272 O O     . ALA B 1 282 ? 41.864  96.751  67.378 1.00 23.29 ? 282  ALA B O     1 
ATOM   6273 C CB    . ALA B 1 282 ? 40.785  97.629  70.303 1.00 22.27 ? 282  ALA B CB    1 
ATOM   6274 N N     . ALA B 1 283 ? 40.168  95.399  68.027 1.00 22.90 ? 283  ALA B N     1 
ATOM   6275 C CA    . ALA B 1 283 ? 40.667  94.169  67.371 1.00 23.61 ? 283  ALA B CA    1 
ATOM   6276 C C     . ALA B 1 283 ? 40.611  94.274  65.840 1.00 23.77 ? 283  ALA B C     1 
ATOM   6277 O O     . ALA B 1 283 ? 41.171  93.398  65.157 1.00 21.91 ? 283  ALA B O     1 
ATOM   6278 C CB    . ALA B 1 283 ? 39.911  92.989  67.900 1.00 26.33 ? 283  ALA B CB    1 
ATOM   6279 N N     . ILE B 1 284 ? 39.956  95.306  65.309 1.00 24.08 ? 284  ILE B N     1 
ATOM   6280 C CA    . ILE B 1 284 ? 39.942  95.562  63.843 1.00 23.75 ? 284  ILE B CA    1 
ATOM   6281 C C     . ILE B 1 284 ? 41.336  96.026  63.426 1.00 24.93 ? 284  ILE B C     1 
ATOM   6282 O O     . ILE B 1 284 ? 41.722  95.747  62.308 1.00 24.85 ? 284  ILE B O     1 
ATOM   6283 C CB    . ILE B 1 284 ? 38.861  96.583  63.426 1.00 27.01 ? 284  ILE B CB    1 
ATOM   6284 C CG1   . ILE B 1 284 ? 37.485  96.087  63.850 1.00 28.78 ? 284  ILE B CG1   1 
ATOM   6285 C CG2   . ILE B 1 284 ? 38.928  96.869  61.922 1.00 28.96 ? 284  ILE B CG2   1 
ATOM   6286 C CD1   . ILE B 1 284 ? 37.196  94.645  63.435 1.00 31.03 ? 284  ILE B CD1   1 
ATOM   6287 N N     . THR B 1 285 ? 42.092  96.692  64.290 1.00 25.52 ? 285  THR B N     1 
ATOM   6288 C CA    . THR B 1 285 ? 43.412  97.274  63.894 1.00 26.74 ? 285  THR B CA    1 
ATOM   6289 C C     . THR B 1 285 ? 44.545  96.867  64.828 1.00 29.03 ? 285  THR B C     1 
ATOM   6290 O O     . THR B 1 285 ? 45.705  97.244  64.520 1.00 26.11 ? 285  THR B O     1 
ATOM   6291 C CB    . THR B 1 285 ? 43.363  98.795  63.845 1.00 23.88 ? 285  THR B CB    1 
ATOM   6292 O OG1   . THR B 1 285 ? 43.149  99.415  65.114 1.00 23.31 ? 285  THR B OG1   1 
ATOM   6293 C CG2   . THR B 1 285 ? 42.296  99.271  62.895 1.00 25.03 ? 285  THR B CG2   1 
ATOM   6294 N N     . ARG B 1 286 ? 44.278  96.173  65.932 1.00 24.98 ? 286  ARG B N     1 
ATOM   6295 C CA    . ARG B 1 286 ? 45.364  95.805  66.884 1.00 24.84 ? 286  ARG B CA    1 
ATOM   6296 C C     . ARG B 1 286 ? 45.140  94.388  67.396 1.00 27.27 ? 286  ARG B C     1 
ATOM   6297 O O     . ARG B 1 286 ? 44.015  93.857  67.256 1.00 23.98 ? 286  ARG B O     1 
ATOM   6298 C CB    . ARG B 1 286 ? 45.395  96.758  68.084 1.00 25.53 ? 286  ARG B CB    1 
ATOM   6299 C CG    . ARG B 1 286 ? 45.661  98.209  67.734 1.00 24.56 ? 286  ARG B CG    1 
ATOM   6300 C CD    . ARG B 1 286 ? 47.115  98.395  67.325 1.00 26.84 ? 286  ARG B CD    1 
ATOM   6301 N NE    . ARG B 1 286 ? 47.433  99.807  67.149 1.00 28.44 ? 286  ARG B NE    1 
ATOM   6302 C CZ    . ARG B 1 286 ? 47.209  100.481 66.028 1.00 28.09 ? 286  ARG B CZ    1 
ATOM   6303 N NH1   . ARG B 1 286 ? 46.681  99.886  64.975 1.00 27.56 ? 286  ARG B NH1   1 
ATOM   6304 N NH2   . ARG B 1 286 ? 47.524  101.748 65.951 1.00 28.37 ? 286  ARG B NH2   1 
ATOM   6305 N N     . THR B 1 287 ? 46.159  93.823  68.034 1.00 25.30 ? 287  THR B N     1 
ATOM   6306 C CA    . THR B 1 287 ? 46.064  92.530  68.726 1.00 25.04 ? 287  THR B CA    1 
ATOM   6307 C C     . THR B 1 287 ? 46.336  92.743  70.216 1.00 23.10 ? 287  THR B C     1 
ATOM   6308 O O     . THR B 1 287 ? 46.919  93.751  70.601 1.00 22.89 ? 287  THR B O     1 
ATOM   6309 C CB    . THR B 1 287 ? 46.994  91.471  68.122 1.00 25.36 ? 287  THR B CB    1 
ATOM   6310 O OG1   . THR B 1 287 ? 48.325  91.927  68.354 1.00 27.31 ? 287  THR B OG1   1 
ATOM   6311 C CG2   . THR B 1 287 ? 46.736  91.224  66.661 1.00 27.50 ? 287  THR B CG2   1 
ATOM   6312 N N     . LYS B 1 288 ? 45.832  91.833  71.023 1.00 23.72 ? 288  LYS B N     1 
ATOM   6313 C CA    . LYS B 1 288 ? 45.931  91.925  72.489 1.00 23.47 ? 288  LYS B CA    1 
ATOM   6314 C C     . LYS B 1 288 ? 47.412  92.043  72.905 1.00 22.00 ? 288  LYS B C     1 
ATOM   6315 O O     . LYS B 1 288 ? 47.725  92.860  73.822 1.00 23.48 ? 288  LYS B O     1 
ATOM   6316 C CB    . LYS B 1 288 ? 45.329  90.652  73.079 1.00 25.25 ? 288  LYS B CB    1 
ATOM   6317 C CG    . LYS B 1 288 ? 45.247  90.676  74.592 1.00 29.32 ? 288  LYS B CG    1 
ATOM   6318 C CD    . LYS B 1 288 ? 44.395  89.574  75.217 1.00 32.67 ? 288  LYS B CD    1 
ATOM   6319 C CE    . LYS B 1 288 ? 45.203  88.333  75.453 1.00 39.85 ? 288  LYS B CE    1 
ATOM   6320 N NZ    . LYS B 1 288 ? 44.435  87.308  76.213 1.00 48.06 ? 288  LYS B NZ    1 
ATOM   6321 N N     . SER B 1 289 ? 48.293  91.290  72.244 1.00 20.73 ? 289  SER B N     1 
ATOM   6322 C CA    . SER B 1 289 ? 49.744  91.202  72.574 1.00 25.32 ? 289  SER B CA    1 
ATOM   6323 C C     . SER B 1 289 ? 50.414  92.567  72.387 1.00 25.58 ? 289  SER B C     1 
ATOM   6324 O O     . SER B 1 289 ? 51.464  92.764  72.957 1.00 25.66 ? 289  SER B O     1 
ATOM   6325 C CB    . SER B 1 289 ? 50.426  90.164  71.745 1.00 23.31 ? 289  SER B CB    1 
ATOM   6326 O OG    . SER B 1 289 ? 50.246  90.475  70.368 1.00 26.79 ? 289  SER B OG    1 
ATOM   6327 N N     . GLN B 1 290 ? 49.796  93.513  71.682 1.00 22.43 ? 290  GLN B N     1 
ATOM   6328 C CA    . GLN B 1 290 ? 50.387  94.873  71.526 1.00 25.68 ? 290  GLN B CA    1 
ATOM   6329 C C     . GLN B 1 290 ? 50.172  95.677  72.812 1.00 25.82 ? 290  GLN B C     1 
ATOM   6330 O O     . GLN B 1 290 ? 50.810  96.725  72.959 1.00 23.47 ? 290  GLN B O     1 
ATOM   6331 C CB    . GLN B 1 290 ? 49.839  95.589  70.284 1.00 25.49 ? 290  GLN B CB    1 
ATOM   6332 C CG    . GLN B 1 290 ? 50.223  94.890  68.982 1.00 25.04 ? 290  GLN B CG    1 
ATOM   6333 C CD    . GLN B 1 290 ? 49.577  95.532  67.775 1.00 28.25 ? 290  GLN B CD    1 
ATOM   6334 O OE1   . GLN B 1 290 ? 48.377  95.446  67.546 1.00 25.76 ? 290  GLN B OE1   1 
ATOM   6335 N NE2   . GLN B 1 290 ? 50.365  96.257  67.006 1.00 27.79 ? 290  GLN B NE2   1 
ATOM   6336 N N     . TYR B 1 291 ? 49.303  95.224  73.711 1.00 24.28 ? 291  TYR B N     1 
ATOM   6337 C CA    . TYR B 1 291 ? 49.017  95.990  74.937 1.00 23.14 ? 291  TYR B CA    1 
ATOM   6338 C C     . TYR B 1 291 ? 49.142  95.146  76.207 1.00 23.91 ? 291  TYR B C     1 
ATOM   6339 O O     . TYR B 1 291 ? 49.162  95.758  77.276 1.00 25.77 ? 291  TYR B O     1 
ATOM   6340 C CB    . TYR B 1 291 ? 47.624  96.588  74.868 1.00 21.50 ? 291  TYR B CB    1 
ATOM   6341 C CG    . TYR B 1 291 ? 47.391  97.508  73.705 1.00 22.97 ? 291  TYR B CG    1 
ATOM   6342 C CD1   . TYR B 1 291 ? 47.686  98.858  73.803 1.00 22.22 ? 291  TYR B CD1   1 
ATOM   6343 C CD2   . TYR B 1 291 ? 46.836  97.045  72.525 1.00 22.78 ? 291  TYR B CD2   1 
ATOM   6344 C CE1   . TYR B 1 291 ? 47.467  99.725  72.760 1.00 23.66 ? 291  TYR B CE1   1 
ATOM   6345 C CE2   . TYR B 1 291 ? 46.641  97.904  71.458 1.00 23.13 ? 291  TYR B CE2   1 
ATOM   6346 C CZ    . TYR B 1 291 ? 46.975  99.235  71.559 1.00 26.22 ? 291  TYR B CZ    1 
ATOM   6347 O OH    . TYR B 1 291 ? 46.769  100.091 70.503 1.00 27.30 ? 291  TYR B OH    1 
ATOM   6348 N N     . TYR B 1 292 ? 49.217  93.834  76.115 1.00 25.31 ? 292  TYR B N     1 
ATOM   6349 C CA    . TYR B 1 292 ? 49.083  92.937  77.294 1.00 25.25 ? 292  TYR B CA    1 
ATOM   6350 C C     . TYR B 1 292 ? 49.758  91.601  76.983 1.00 27.16 ? 292  TYR B C     1 
ATOM   6351 O O     . TYR B 1 292 ? 49.460  91.000  75.936 1.00 29.12 ? 292  TYR B O     1 
ATOM   6352 C CB    . TYR B 1 292 ? 47.589  92.781  77.621 1.00 24.76 ? 292  TYR B CB    1 
ATOM   6353 C CG    . TYR B 1 292 ? 47.248  92.002  78.862 1.00 26.02 ? 292  TYR B CG    1 
ATOM   6354 C CD1   . TYR B 1 292 ? 47.728  92.391  80.105 1.00 28.92 ? 292  TYR B CD1   1 
ATOM   6355 C CD2   . TYR B 1 292 ? 46.415  90.892  78.808 1.00 31.14 ? 292  TYR B CD2   1 
ATOM   6356 C CE1   . TYR B 1 292 ? 47.397  91.696  81.256 1.00 29.93 ? 292  TYR B CE1   1 
ATOM   6357 C CE2   . TYR B 1 292 ? 46.078  90.183  79.954 1.00 29.44 ? 292  TYR B CE2   1 
ATOM   6358 C CZ    . TYR B 1 292 ? 46.571  90.592  81.175 1.00 30.19 ? 292  TYR B CZ    1 
ATOM   6359 O OH    . TYR B 1 292 ? 46.228  89.924  82.306 1.00 34.75 ? 292  TYR B OH    1 
ATOM   6360 N N     . ASP B 1 293 ? 50.572  91.105  77.916 1.00 25.72 ? 293  ASP B N     1 
ATOM   6361 C CA    . ASP B 1 293 ? 51.261  89.804  77.804 1.00 28.85 ? 293  ASP B CA    1 
ATOM   6362 C C     . ASP B 1 293 ? 50.430  88.697  78.460 1.00 29.70 ? 293  ASP B C     1 
ATOM   6363 O O     . ASP B 1 293 ? 50.799  87.568  78.264 1.00 31.54 ? 293  ASP B O     1 
ATOM   6364 C CB    . ASP B 1 293 ? 52.636  89.864  78.466 1.00 29.74 ? 293  ASP B CB    1 
ATOM   6365 C CG    . ASP B 1 293 ? 53.556  90.899  77.821 1.00 33.55 ? 293  ASP B CG    1 
ATOM   6366 O OD1   . ASP B 1 293 ? 53.443  91.092  76.598 1.00 34.41 ? 293  ASP B OD1   1 
ATOM   6367 O OD2   . ASP B 1 293 ? 54.371  91.514  78.568 1.00 42.07 ? 293  ASP B OD2   1 
ATOM   6368 N N     . GLY B 1 294 ? 49.394  89.001  79.236 1.00 29.75 ? 294  GLY B N     1 
ATOM   6369 C CA    . GLY B 1 294 ? 48.661  87.964  79.987 1.00 34.21 ? 294  GLY B CA    1 
ATOM   6370 C C     . GLY B 1 294 ? 47.826  87.064  79.080 1.00 33.61 ? 294  GLY B C     1 
ATOM   6371 O O     . GLY B 1 294 ? 47.631  87.418  77.892 1.00 34.15 ? 294  GLY B O     1 
ATOM   6372 N N     . ASP B 1 295 ? 47.369  85.923  79.615 1.00 36.47 ? 295  ASP B N     1 
ATOM   6373 C CA    . ASP B 1 295 ? 46.491  84.956  78.899 1.00 43.93 ? 295  ASP B CA    1 
ATOM   6374 C C     . ASP B 1 295 ? 45.034  85.298  79.201 1.00 36.34 ? 295  ASP B C     1 
ATOM   6375 O O     . ASP B 1 295 ? 44.158  84.950  78.424 1.00 44.72 ? 295  ASP B O     1 
ATOM   6376 C CB    . ASP B 1 295 ? 46.753  83.506  79.301 1.00 52.46 ? 295  ASP B CB    1 
ATOM   6377 C CG    . ASP B 1 295 ? 48.043  82.972  78.727 1.00 62.52 ? 295  ASP B CG    1 
ATOM   6378 O OD1   . ASP B 1 295 ? 48.230  83.134  77.508 1.00 66.76 ? 295  ASP B OD1   1 
ATOM   6379 O OD2   . ASP B 1 295 ? 48.863  82.445  79.515 1.00 77.88 ? 295  ASP B OD2   1 
ATOM   6380 N N     . GLY B 1 296 ? 44.763  85.989  80.286 1.00 40.37 ? 296  GLY B N     1 
ATOM   6381 C CA    . GLY B 1 296 ? 43.344  86.289  80.556 1.00 46.97 ? 296  GLY B CA    1 
ATOM   6382 C C     . GLY B 1 296 ? 42.726  87.283  79.566 1.00 41.12 ? 296  GLY B C     1 
ATOM   6383 O O     . GLY B 1 296 ? 43.345  87.783  78.619 1.00 37.41 ? 296  GLY B O     1 
ATOM   6384 N N     . PRO B 1 297 ? 41.463  87.632  79.826 1.00 34.76 ? 297  PRO B N     1 
ATOM   6385 C CA    . PRO B 1 297 ? 40.888  88.867  79.313 1.00 30.69 ? 297  PRO B CA    1 
ATOM   6386 C C     . PRO B 1 297 ? 41.612  90.083  79.900 1.00 28.27 ? 297  PRO B C     1 
ATOM   6387 O O     . PRO B 1 297 ? 42.233  90.028  80.950 1.00 27.69 ? 297  PRO B O     1 
ATOM   6388 C CB    . PRO B 1 297 ? 39.422  88.861  79.783 1.00 31.40 ? 297  PRO B CB    1 
ATOM   6389 C CG    . PRO B 1 297 ? 39.371  87.838  80.915 1.00 36.09 ? 297  PRO B CG    1 
ATOM   6390 C CD    . PRO B 1 297 ? 40.524  86.871  80.674 1.00 35.79 ? 297  PRO B CD    1 
ATOM   6391 N N     . ILE B 1 298 ? 41.442  91.210  79.244 1.00 27.62 ? 298  ILE B N     1 
ATOM   6392 C CA    . ILE B 1 298 ? 42.274  92.404  79.549 1.00 25.20 ? 298  ILE B CA    1 
ATOM   6393 C C     . ILE B 1 298 ? 41.810  92.993  80.862 1.00 27.67 ? 298  ILE B C     1 
ATOM   6394 O O     . ILE B 1 298 ? 40.618  92.994  81.186 1.00 26.22 ? 298  ILE B O     1 
ATOM   6395 C CB    . ILE B 1 298 ? 42.235  93.455  78.424 1.00 25.77 ? 298  ILE B CB    1 
ATOM   6396 C CG1   . ILE B 1 298 ? 40.822  94.022  78.207 1.00 24.42 ? 298  ILE B CG1   1 
ATOM   6397 C CG2   . ILE B 1 298 ? 42.849  92.863  77.165 1.00 25.76 ? 298  ILE B CG2   1 
ATOM   6398 C CD1   . ILE B 1 298 ? 40.777  95.226  77.297 1.00 25.12 ? 298  ILE B CD1   1 
ATOM   6399 N N     . PRO B 1 299 ? 42.758  93.536  81.648 1.00 25.69 ? 299  PRO B N     1 
ATOM   6400 C CA    . PRO B 1 299 ? 42.398  94.304  82.821 1.00 25.90 ? 299  PRO B CA    1 
ATOM   6401 C C     . PRO B 1 299 ? 42.078  95.742  82.472 1.00 25.40 ? 299  PRO B C     1 
ATOM   6402 O O     . PRO B 1 299 ? 42.351  96.200  81.365 1.00 24.24 ? 299  PRO B O     1 
ATOM   6403 C CB    . PRO B 1 299 ? 43.706  94.195  83.621 1.00 29.00 ? 299  PRO B CB    1 
ATOM   6404 C CG    . PRO B 1 299 ? 44.769  94.284  82.542 1.00 27.00 ? 299  PRO B CG    1 
ATOM   6405 C CD    . PRO B 1 299 ? 44.226  93.347  81.491 1.00 29.47 ? 299  PRO B CD    1 
ATOM   6406 N N     . PRO B 1 300 ? 41.525  96.520  83.419 1.00 23.73 ? 300  PRO B N     1 
ATOM   6407 C CA    . PRO B 1 300 ? 41.136  97.900  83.138 1.00 26.96 ? 300  PRO B CA    1 
ATOM   6408 C C     . PRO B 1 300 ? 42.228  98.846  82.595 1.00 26.77 ? 300  PRO B C     1 
ATOM   6409 O O     . PRO B 1 300 ? 41.911  99.672  81.748 1.00 26.26 ? 300  PRO B O     1 
ATOM   6410 C CB    . PRO B 1 300 ? 40.661  98.382  84.526 1.00 27.77 ? 300  PRO B CB    1 
ATOM   6411 C CG    . PRO B 1 300 ? 40.141  97.112  85.183 1.00 29.88 ? 300  PRO B CG    1 
ATOM   6412 C CD    . PRO B 1 300 ? 41.140  96.067  84.772 1.00 27.23 ? 300  PRO B CD    1 
ATOM   6413 N N     . SER B 1 301 ? 43.454  98.758  83.114 1.00 25.08 ? 301  SER B N     1 
ATOM   6414 C CA    . SER B 1 301 ? 44.596  99.621  82.680 1.00 22.99 ? 301  SER B CA    1 
ATOM   6415 C C     . SER B 1 301 ? 44.825  99.415  81.181 1.00 22.59 ? 301  SER B C     1 
ATOM   6416 O O     . SER B 1 301 ? 45.125  100.411 80.463 1.00 27.15 ? 301  SER B O     1 
ATOM   6417 C CB    . SER B 1 301 ? 45.863  99.302  83.437 1.00 22.18 ? 301  SER B CB    1 
ATOM   6418 O OG    . SER B 1 301 ? 46.317  97.982  83.170 1.00 22.06 ? 301  SER B OG    1 
ATOM   6419 N N     . VAL B 1 302 ? 44.694  98.175  80.729 1.00 23.07 ? 302  VAL B N     1 
ATOM   6420 C CA    . VAL B 1 302 ? 44.863  97.806  79.295 1.00 24.47 ? 302  VAL B CA    1 
ATOM   6421 C C     . VAL B 1 302 ? 43.731  98.436  78.483 1.00 25.32 ? 302  VAL B C     1 
ATOM   6422 O O     . VAL B 1 302 ? 44.015  99.076  77.449 1.00 23.86 ? 302  VAL B O     1 
ATOM   6423 C CB    . VAL B 1 302 ? 44.956  96.299  79.087 1.00 25.01 ? 302  VAL B CB    1 
ATOM   6424 C CG1   . VAL B 1 302 ? 44.779  95.943  77.621 1.00 26.20 ? 302  VAL B CG1   1 
ATOM   6425 C CG2   . VAL B 1 302 ? 46.285  95.758  79.588 1.00 26.17 ? 302  VAL B CG2   1 
ATOM   6426 N N     . ALA B 1 303 ? 42.484  98.303  78.929 1.00 26.19 ? 303  ALA B N     1 
ATOM   6427 C CA    . ALA B 1 303 ? 41.331  98.962  78.271 1.00 24.15 ? 303  ALA B CA    1 
ATOM   6428 C C     . ALA B 1 303 ? 41.601  100.470 78.139 1.00 24.81 ? 303  ALA B C     1 
ATOM   6429 O O     . ALA B 1 303 ? 41.484  101.033 77.054 1.00 23.94 ? 303  ALA B O     1 
ATOM   6430 C CB    . ALA B 1 303 ? 40.076  98.659  79.056 1.00 25.64 ? 303  ALA B CB    1 
ATOM   6431 N N     . LYS B 1 304 ? 42.014  101.134 79.200 1.00 24.83 ? 304  LYS B N     1 
ATOM   6432 C CA    . LYS B 1 304 ? 42.221  102.589 79.169 1.00 26.38 ? 304  LYS B CA    1 
ATOM   6433 C C     . LYS B 1 304 ? 43.387  102.968 78.234 1.00 23.84 ? 304  LYS B C     1 
ATOM   6434 O O     . LYS B 1 304 ? 43.303  103.985 77.532 1.00 23.98 ? 304  LYS B O     1 
ATOM   6435 C CB    . LYS B 1 304 ? 42.482  103.063 80.597 1.00 32.27 ? 304  LYS B CB    1 
ATOM   6436 C CG    . LYS B 1 304 ? 42.486  104.563 80.742 1.00 44.75 ? 304  LYS B CG    1 
ATOM   6437 C CD    . LYS B 1 304 ? 41.104  105.211 80.530 1.00 51.35 ? 304  LYS B CD    1 
ATOM   6438 C CE    . LYS B 1 304 ? 41.055  106.694 80.880 1.00 52.85 ? 304  LYS B CE    1 
ATOM   6439 N NZ    . LYS B 1 304 ? 40.728  107.545 79.710 1.00 53.58 ? 304  LYS B NZ    1 
ATOM   6440 N N     . THR B 1 305 ? 44.459  102.201 78.236 1.00 25.17 ? 305  THR B N     1 
ATOM   6441 C CA    . THR B 1 305 ? 45.621  102.449 77.351 1.00 24.69 ? 305  THR B CA    1 
ATOM   6442 C C     . THR B 1 305 ? 45.143  102.354 75.900 1.00 24.46 ? 305  THR B C     1 
ATOM   6443 O O     . THR B 1 305 ? 45.477  103.257 75.098 1.00 23.80 ? 305  THR B O     1 
ATOM   6444 C CB    . THR B 1 305 ? 46.770  101.480 77.678 1.00 25.13 ? 305  THR B CB    1 
ATOM   6445 O OG1   . THR B 1 305 ? 47.139  101.648 79.052 1.00 23.27 ? 305  THR B OG1   1 
ATOM   6446 C CG2   . THR B 1 305 ? 47.956  101.634 76.750 1.00 24.53 ? 305  THR B CG2   1 
ATOM   6447 N N     . MET B 1 306 ? 44.422  101.277 75.558 1.00 22.44 ? 306  MET B N     1 
ATOM   6448 C CA    . MET B 1 306 ? 43.877  101.093 74.187 1.00 23.96 ? 306  MET B CA    1 
ATOM   6449 C C     . MET B 1 306 ? 42.968  102.281 73.824 1.00 22.75 ? 306  MET B C     1 
ATOM   6450 O O     . MET B 1 306 ? 43.018  102.776 72.684 1.00 22.46 ? 306  MET B O     1 
ATOM   6451 C CB    . MET B 1 306 ? 43.082  99.793  74.112 1.00 25.23 ? 306  MET B CB    1 
ATOM   6452 C CG    . MET B 1 306 ? 43.902  98.528  73.814 1.00 30.30 ? 306  MET B CG    1 
ATOM   6453 S SD    . MET B 1 306 ? 43.008  97.016  74.240 1.00 41.86 ? 306  MET B SD    1 
ATOM   6454 C CE    . MET B 1 306 ? 41.396  97.289  73.530 1.00 44.62 ? 306  MET B CE    1 
ATOM   6455 N N     . MET B 1 307 ? 42.113  102.715 74.741 1.00 22.42 ? 307  MET B N     1 
ATOM   6456 C CA    . MET B 1 307 ? 41.191  103.855 74.483 1.00 23.39 ? 307  MET B CA    1 
ATOM   6457 C C     . MET B 1 307 ? 42.004  105.117 74.111 1.00 24.43 ? 307  MET B C     1 
ATOM   6458 O O     . MET B 1 307 ? 41.685  105.799 73.154 1.00 24.05 ? 307  MET B O     1 
ATOM   6459 C CB    . MET B 1 307 ? 40.324  104.135 75.723 1.00 22.33 ? 307  MET B CB    1 
ATOM   6460 C CG    . MET B 1 307 ? 39.278  103.043 75.978 1.00 24.77 ? 307  MET B CG    1 
ATOM   6461 S SD    . MET B 1 307 ? 38.588  103.123 77.662 1.00 27.28 ? 307  MET B SD    1 
ATOM   6462 C CE    . MET B 1 307 ? 37.941  104.780 77.700 1.00 25.39 ? 307  MET B CE    1 
ATOM   6463 N N     . ALA B 1 308 ? 42.979  105.491 74.927 1.00 24.16 ? 308  ALA B N     1 
ATOM   6464 C CA    . ALA B 1 308 ? 43.843  106.654 74.697 1.00 24.01 ? 308  ALA B CA    1 
ATOM   6465 C C     . ALA B 1 308 ? 44.663  106.454 73.409 1.00 23.92 ? 308  ALA B C     1 
ATOM   6466 O O     . ALA B 1 308 ? 44.849  107.420 72.705 1.00 25.58 ? 308  ALA B O     1 
ATOM   6467 C CB    . ALA B 1 308 ? 44.783  106.821 75.887 1.00 26.44 ? 308  ALA B CB    1 
ATOM   6468 N N     . ASP B 1 309 ? 45.216  105.269 73.166 1.00 23.97 ? 309  ASP B N     1 
ATOM   6469 C CA    . ASP B 1 309 ? 46.050  105.010 71.961 1.00 23.50 ? 309  ASP B CA    1 
ATOM   6470 C C     . ASP B 1 309 ? 45.232  105.136 70.682 1.00 24.19 ? 309  ASP B C     1 
ATOM   6471 O O     . ASP B 1 309 ? 45.797  105.621 69.681 1.00 25.85 ? 309  ASP B O     1 
ATOM   6472 C CB    . ASP B 1 309 ? 46.666  103.616 72.015 1.00 25.16 ? 309  ASP B CB    1 
ATOM   6473 C CG    . ASP B 1 309 ? 47.891  103.420 71.119 1.00 27.91 ? 309  ASP B CG    1 
ATOM   6474 O OD1   . ASP B 1 309 ? 48.642  104.418 70.923 1.00 28.59 ? 309  ASP B OD1   1 
ATOM   6475 O OD2   . ASP B 1 309 ? 48.044  102.304 70.571 1.00 27.31 ? 309  ASP B OD2   1 
ATOM   6476 N N     . LEU B 1 310 ? 43.981  104.653 70.678 1.00 24.51 ? 310  LEU B N     1 
ATOM   6477 C CA    . LEU B 1 310 ? 43.211  104.437 69.428 1.00 24.98 ? 310  LEU B CA    1 
ATOM   6478 C C     . LEU B 1 310 ? 42.105  105.483 69.267 1.00 24.45 ? 310  LEU B C     1 
ATOM   6479 O O     . LEU B 1 310 ? 41.435  105.451 68.214 1.00 25.42 ? 310  LEU B O     1 
ATOM   6480 C CB    . LEU B 1 310 ? 42.667  103.003 69.438 1.00 25.75 ? 310  LEU B CB    1 
ATOM   6481 C CG    . LEU B 1 310 ? 43.717  101.899 69.538 1.00 26.20 ? 310  LEU B CG    1 
ATOM   6482 C CD1   . LEU B 1 310 ? 43.055  100.551 69.687 1.00 27.46 ? 310  LEU B CD1   1 
ATOM   6483 C CD2   . LEU B 1 310 ? 44.608  101.892 68.295 1.00 26.35 ? 310  LEU B CD2   1 
ATOM   6484 N N     . ASP B 1 311 ? 41.905  106.357 70.257 1.00 23.62 ? 311  ASP B N     1 
ATOM   6485 C CA    . ASP B 1 311 ? 40.774  107.318 70.296 1.00 24.15 ? 311  ASP B CA    1 
ATOM   6486 C C     . ASP B 1 311 ? 39.478  106.513 70.167 1.00 25.16 ? 311  ASP B C     1 
ATOM   6487 O O     . ASP B 1 311 ? 38.631  106.773 69.257 1.00 24.34 ? 311  ASP B O     1 
ATOM   6488 C CB    . ASP B 1 311 ? 40.933  108.397 69.214 1.00 28.86 ? 311  ASP B CB    1 
ATOM   6489 C CG    . ASP B 1 311 ? 42.123  109.320 69.477 1.00 30.05 ? 311  ASP B CG    1 
ATOM   6490 O OD1   . ASP B 1 311 ? 42.607  109.343 70.593 1.00 36.08 ? 311  ASP B OD1   1 
ATOM   6491 O OD2   . ASP B 1 311 ? 42.560  109.972 68.563 1.00 33.91 ? 311  ASP B OD2   1 
ATOM   6492 N N     . LEU B 1 312 ? 39.327  105.547 71.062 1.00 25.17 ? 312  LEU B N     1 
ATOM   6493 C CA    . LEU B 1 312 ? 38.096  104.749 71.203 1.00 23.35 ? 312  LEU B CA    1 
ATOM   6494 C C     . LEU B 1 312 ? 37.588  104.920 72.641 1.00 24.50 ? 312  LEU B C     1 
ATOM   6495 O O     . LEU B 1 312 ? 38.407  105.256 73.538 1.00 23.64 ? 312  LEU B O     1 
ATOM   6496 C CB    . LEU B 1 312 ? 38.383  103.275 70.894 1.00 24.03 ? 312  LEU B CB    1 
ATOM   6497 C CG    . LEU B 1 312 ? 38.776  102.962 69.443 1.00 25.23 ? 312  LEU B CG    1 
ATOM   6498 C CD1   . LEU B 1 312 ? 39.091  101.485 69.267 1.00 23.02 ? 312  LEU B CD1   1 
ATOM   6499 C CD2   . LEU B 1 312 ? 37.700  103.398 68.468 1.00 26.85 ? 312  LEU B CD2   1 
ATOM   6500 N N     . GLY B 1 313 ? 36.291  104.687 72.850 1.00 24.69 ? 313  GLY B N     1 
ATOM   6501 C CA    . GLY B 1 313 ? 35.750  104.586 74.222 1.00 25.00 ? 313  GLY B CA    1 
ATOM   6502 C C     . GLY B 1 313 ? 35.485  103.153 74.608 1.00 23.30 ? 313  GLY B C     1 
ATOM   6503 O O     . GLY B 1 313 ? 35.692  102.218 73.800 1.00 25.53 ? 313  GLY B O     1 
ATOM   6504 N N     . MET B 1 314 ? 34.921  102.954 75.806 1.00 22.58 ? 314  MET B N     1 
ATOM   6505 C CA    . MET B 1 314 ? 34.411  101.638 76.193 1.00 21.97 ? 314  MET B CA    1 
ATOM   6506 C C     . MET B 1 314 ? 33.222  101.285 75.310 1.00 21.24 ? 314  MET B C     1 
ATOM   6507 O O     . MET B 1 314 ? 33.044  100.071 74.974 1.00 24.81 ? 314  MET B O     1 
ATOM   6508 C CB    . MET B 1 314 ? 34.035  101.617 77.684 1.00 24.31 ? 314  MET B CB    1 
ATOM   6509 C CG    . MET B 1 314 ? 35.264  101.589 78.600 1.00 25.88 ? 314  MET B CG    1 
ATOM   6510 S SD    . MET B 1 314 ? 36.261  100.126 78.329 1.00 29.72 ? 314  MET B SD    1 
ATOM   6511 C CE    . MET B 1 314 ? 35.238  98.854  79.078 1.00 33.29 ? 314  MET B CE    1 
ATOM   6512 N N     . TRP B 1 315 ? 32.494  102.296 74.860 1.00 24.47 ? 315  TRP B N     1 
ATOM   6513 C CA    . TRP B 1 315 ? 31.401  102.115 73.867 1.00 25.13 ? 315  TRP B CA    1 
ATOM   6514 C C     . TRP B 1 315 ? 31.600  103.116 72.728 1.00 23.96 ? 315  TRP B C     1 
ATOM   6515 O O     . TRP B 1 315 ? 31.908  104.280 72.970 1.00 22.26 ? 315  TRP B O     1 
ATOM   6516 C CB    . TRP B 1 315 ? 30.018  102.266 74.521 1.00 25.96 ? 315  TRP B CB    1 
ATOM   6517 C CG    . TRP B 1 315 ? 29.713  101.205 75.536 1.00 23.19 ? 315  TRP B CG    1 
ATOM   6518 C CD1   . TRP B 1 315 ? 29.794  101.329 76.897 1.00 23.69 ? 315  TRP B CD1   1 
ATOM   6519 C CD2   . TRP B 1 315 ? 29.303  99.854  75.272 1.00 22.41 ? 315  TRP B CD2   1 
ATOM   6520 N NE1   . TRP B 1 315 ? 29.468  100.143 77.491 1.00 24.43 ? 315  TRP B NE1   1 
ATOM   6521 C CE2   . TRP B 1 315 ? 29.169  99.217  76.522 1.00 22.81 ? 315  TRP B CE2   1 
ATOM   6522 C CE3   . TRP B 1 315 ? 29.097  99.097  74.129 1.00 23.43 ? 315  TRP B CE3   1 
ATOM   6523 C CZ2   . TRP B 1 315 ? 28.775  97.893  76.633 1.00 23.99 ? 315  TRP B CZ2   1 
ATOM   6524 C CZ3   . TRP B 1 315 ? 28.746  97.765  74.240 1.00 24.78 ? 315  TRP B CZ3   1 
ATOM   6525 C CH2   . TRP B 1 315 ? 28.561  97.178  75.484 1.00 22.98 ? 315  TRP B CH2   1 
ATOM   6526 N N     . ASN B 1 316 ? 31.360  102.668 71.507 1.00 22.11 ? 316  ASN B N     1 
ATOM   6527 C CA    . ASN B 1 316 ? 31.647  103.448 70.279 1.00 20.94 ? 316  ASN B CA    1 
ATOM   6528 C C     . ASN B 1 316 ? 30.406  103.414 69.390 1.00 22.00 ? 316  ASN B C     1 
ATOM   6529 O O     . ASN B 1 316 ? 30.049  102.301 68.850 1.00 21.59 ? 316  ASN B O     1 
ATOM   6530 C CB    . ASN B 1 316 ? 32.863  102.832 69.592 1.00 23.62 ? 316  ASN B CB    1 
ATOM   6531 C CG    . ASN B 1 316 ? 34.070  102.861 70.502 1.00 27.31 ? 316  ASN B CG    1 
ATOM   6532 O OD1   . ASN B 1 316 ? 34.589  103.926 70.799 1.00 26.04 ? 316  ASN B OD1   1 
ATOM   6533 N ND2   . ASN B 1 316 ? 34.430  101.718 71.073 1.00 28.39 ? 316  ASN B ND2   1 
ATOM   6534 N N     . PHE B 1 317 ? 29.714  104.537 69.319 1.00 20.21 ? 317  PHE B N     1 
ATOM   6535 C CA    . PHE B 1 317 ? 28.475  104.697 68.553 1.00 20.90 ? 317  PHE B CA    1 
ATOM   6536 C C     . PHE B 1 317 ? 28.866  105.191 67.157 1.00 21.62 ? 317  PHE B C     1 
ATOM   6537 O O     . PHE B 1 317 ? 29.261  106.331 66.972 1.00 20.10 ? 317  PHE B O     1 
ATOM   6538 C CB    . PHE B 1 317 ? 27.497  105.597 69.307 1.00 21.87 ? 317  PHE B CB    1 
ATOM   6539 C CG    . PHE B 1 317 ? 26.287  106.048 68.529 1.00 19.08 ? 317  PHE B CG    1 
ATOM   6540 C CD1   . PHE B 1 317 ? 25.660  105.229 67.603 1.00 21.32 ? 317  PHE B CD1   1 
ATOM   6541 C CD2   . PHE B 1 317 ? 25.732  107.286 68.784 1.00 20.64 ? 317  PHE B CD2   1 
ATOM   6542 C CE1   . PHE B 1 317 ? 24.548  105.677 66.911 1.00 20.64 ? 317  PHE B CE1   1 
ATOM   6543 C CE2   . PHE B 1 317 ? 24.629  107.728 68.098 1.00 21.74 ? 317  PHE B CE2   1 
ATOM   6544 C CZ    . PHE B 1 317 ? 24.035  106.922 67.157 1.00 22.60 ? 317  PHE B CZ    1 
ATOM   6545 N N     . CYS B 1 318 ? 28.650  104.335 66.179 1.00 21.23 ? 318  CYS B N     1 
ATOM   6546 C CA    . CYS B 1 318 ? 28.953  104.608 64.771 1.00 22.48 ? 318  CYS B CA    1 
ATOM   6547 C C     . CYS B 1 318 ? 27.658  104.653 63.960 1.00 23.12 ? 318  CYS B C     1 
ATOM   6548 O O     . CYS B 1 318 ? 26.902  103.632 63.917 1.00 21.33 ? 318  CYS B O     1 
ATOM   6549 C CB    . CYS B 1 318 ? 29.888  103.493 64.376 1.00 32.22 ? 318  CYS B CB    1 
ATOM   6550 S SG    . CYS B 1 318 ? 30.902  104.025 63.027 1.00 50.45 ? 318  CYS B SG    1 
ATOM   6551 N N     . GLY B 1 319 ? 27.362  105.806 63.389 1.00 19.95 ? 319  GLY B N     1 
ATOM   6552 C CA    . GLY B 1 319 ? 26.173  105.988 62.551 1.00 19.96 ? 319  GLY B CA    1 
ATOM   6553 C C     . GLY B 1 319 ? 26.483  106.860 61.350 1.00 21.67 ? 319  GLY B C     1 
ATOM   6554 O O     . GLY B 1 319 ? 27.677  107.212 61.128 1.00 19.87 ? 319  GLY B O     1 
ATOM   6555 N N     . ALA B 1 320 ? 25.470  107.197 60.582 1.00 20.34 ? 320  ALA B N     1 
ATOM   6556 C CA    . ALA B 1 320 ? 25.676  108.103 59.444 1.00 22.51 ? 320  ALA B CA    1 
ATOM   6557 C C     . ALA B 1 320 ? 24.399  108.889 59.182 1.00 21.86 ? 320  ALA B C     1 
ATOM   6558 O O     . ALA B 1 320 ? 23.290  108.392 59.440 1.00 19.46 ? 320  ALA B O     1 
ATOM   6559 C CB    . ALA B 1 320 ? 26.131  107.312 58.237 1.00 20.57 ? 320  ALA B CB    1 
ATOM   6560 N N     . LEU B 1 321 ? 24.603  110.075 58.651 1.00 20.52 ? 321  LEU B N     1 
ATOM   6561 C CA    . LEU B 1 321 ? 23.552  110.963 58.131 1.00 21.34 ? 321  LEU B CA    1 
ATOM   6562 C C     . LEU B 1 321 ? 23.464  110.786 56.619 1.00 21.16 ? 321  LEU B C     1 
ATOM   6563 O O     . LEU B 1 321 ? 24.515  110.555 55.961 1.00 21.46 ? 321  LEU B O     1 
ATOM   6564 C CB    . LEU B 1 321 ? 23.910  112.394 58.484 1.00 21.13 ? 321  LEU B CB    1 
ATOM   6565 C CG    . LEU B 1 321 ? 24.338  112.638 59.918 1.00 23.44 ? 321  LEU B CG    1 
ATOM   6566 C CD1   . LEU B 1 321 ? 24.977  114.018 60.018 1.00 26.39 ? 321  LEU B CD1   1 
ATOM   6567 C CD2   . LEU B 1 321 ? 23.140  112.539 60.831 1.00 24.40 ? 321  LEU B CD2   1 
ATOM   6568 N N     . TYR B 1 322 ? 22.261  110.884 56.088 1.00 19.98 ? 322  TYR B N     1 
ATOM   6569 C CA    . TYR B 1 322 ? 22.006  110.645 54.645 1.00 19.41 ? 322  TYR B CA    1 
ATOM   6570 C C     . TYR B 1 322 ? 21.032  111.719 54.204 1.00 21.42 ? 322  TYR B C     1 
ATOM   6571 O O     . TYR B 1 322 ? 20.075  112.017 54.936 1.00 21.41 ? 322  TYR B O     1 
ATOM   6572 C CB    . TYR B 1 322 ? 21.368  109.266 54.396 1.00 19.98 ? 322  TYR B CB    1 
ATOM   6573 C CG    . TYR B 1 322 ? 22.121  108.078 54.944 1.00 19.31 ? 322  TYR B CG    1 
ATOM   6574 C CD1   . TYR B 1 322 ? 22.022  107.723 56.282 1.00 19.04 ? 322  TYR B CD1   1 
ATOM   6575 C CD2   . TYR B 1 322 ? 22.929  107.304 54.127 1.00 19.11 ? 322  TYR B CD2   1 
ATOM   6576 C CE1   . TYR B 1 322 ? 22.701  106.632 56.796 1.00 20.38 ? 322  TYR B CE1   1 
ATOM   6577 C CE2   . TYR B 1 322 ? 23.619  106.215 54.624 1.00 20.03 ? 322  TYR B CE2   1 
ATOM   6578 C CZ    . TYR B 1 322 ? 23.470  105.852 55.954 1.00 19.49 ? 322  TYR B CZ    1 
ATOM   6579 O OH    . TYR B 1 322 ? 24.169  104.801 56.441 1.00 18.57 ? 322  TYR B OH    1 
ATOM   6580 N N     . GLY B 1 323 ? 21.280  112.274 53.038 1.00 22.67 ? 323  GLY B N     1 
ATOM   6581 C CA    . GLY B 1 323 ? 20.336  113.169 52.366 1.00 23.45 ? 323  GLY B CA    1 
ATOM   6582 C C     . GLY B 1 323 ? 20.944  114.543 52.112 1.00 24.21 ? 323  GLY B C     1 
ATOM   6583 O O     . GLY B 1 323 ? 22.145  114.752 52.237 1.00 22.88 ? 323  GLY B O     1 
ATOM   6584 N N     . PRO B 1 324 ? 20.077  115.486 51.705 1.00 25.42 ? 324  PRO B N     1 
ATOM   6585 C CA    . PRO B 1 324 ? 20.464  116.857 51.411 1.00 28.22 ? 324  PRO B CA    1 
ATOM   6586 C C     . PRO B 1 324 ? 21.134  117.447 52.646 1.00 27.67 ? 324  PRO B C     1 
ATOM   6587 O O     . PRO B 1 324 ? 20.709  117.170 53.766 1.00 24.81 ? 324  PRO B O     1 
ATOM   6588 C CB    . PRO B 1 324 ? 19.124  117.557 51.124 1.00 27.59 ? 324  PRO B CB    1 
ATOM   6589 C CG    . PRO B 1 324 ? 18.149  116.469 50.838 1.00 29.61 ? 324  PRO B CG    1 
ATOM   6590 C CD    . PRO B 1 324 ? 18.636  115.243 51.559 1.00 26.82 ? 324  PRO B CD    1 
ATOM   6591 N N     . PRO B 1 325 ? 22.185  118.260 52.489 1.00 27.69 ? 325  PRO B N     1 
ATOM   6592 C CA    . PRO B 1 325 ? 22.829  118.918 53.628 1.00 28.70 ? 325  PRO B CA    1 
ATOM   6593 C C     . PRO B 1 325 ? 21.914  119.555 54.675 1.00 27.28 ? 325  PRO B C     1 
ATOM   6594 O O     . PRO B 1 325 ? 22.175  119.392 55.870 1.00 28.10 ? 325  PRO B O     1 
ATOM   6595 C CB    . PRO B 1 325 ? 23.692  120.005 52.958 1.00 30.34 ? 325  PRO B CB    1 
ATOM   6596 C CG    . PRO B 1 325 ? 24.060  119.376 51.631 1.00 31.88 ? 325  PRO B CG    1 
ATOM   6597 C CD    . PRO B 1 325 ? 22.824  118.596 51.201 1.00 32.89 ? 325  PRO B CD    1 
ATOM   6598 N N     . PRO B 1 326 ? 20.840  120.287 54.309 1.00 26.88 ? 326  PRO B N     1 
ATOM   6599 C CA    . PRO B 1 326 ? 19.958  120.882 55.318 1.00 29.04 ? 326  PRO B CA    1 
ATOM   6600 C C     . PRO B 1 326 ? 19.258  119.806 56.143 1.00 28.71 ? 326  PRO B C     1 
ATOM   6601 O O     . PRO B 1 326 ? 19.082  119.977 57.347 1.00 29.70 ? 326  PRO B O     1 
ATOM   6602 C CB    . PRO B 1 326 ? 18.952  121.779 54.578 1.00 28.53 ? 326  PRO B CB    1 
ATOM   6603 C CG    . PRO B 1 326 ? 19.360  121.752 53.128 1.00 31.18 ? 326  PRO B CG    1 
ATOM   6604 C CD    . PRO B 1 326 ? 20.511  120.769 52.945 1.00 30.21 ? 326  PRO B CD    1 
ATOM   6605 N N     . VAL B 1 327 ? 18.940  118.678 55.534 1.00 26.38 ? 327  VAL B N     1 
ATOM   6606 C CA    . VAL B 1 327 ? 18.343  117.575 56.336 1.00 25.26 ? 327  VAL B CA    1 
ATOM   6607 C C     . VAL B 1 327 ? 19.407  117.023 57.297 1.00 23.60 ? 327  VAL B C     1 
ATOM   6608 O O     . VAL B 1 327 ? 19.109  116.868 58.489 1.00 23.15 ? 327  VAL B O     1 
ATOM   6609 C CB    . VAL B 1 327 ? 17.766  116.486 55.430 1.00 25.40 ? 327  VAL B CB    1 
ATOM   6610 C CG1   . VAL B 1 327 ? 17.398  115.257 56.222 1.00 26.15 ? 327  VAL B CG1   1 
ATOM   6611 C CG2   . VAL B 1 327 ? 16.602  117.033 54.656 1.00 27.63 ? 327  VAL B CG2   1 
ATOM   6612 N N     . MET B 1 328 ? 20.593  116.711 56.798 1.00 23.16 ? 328  MET B N     1 
ATOM   6613 C CA    . MET B 1 328 ? 21.674  116.138 57.627 1.00 23.27 ? 328  MET B CA    1 
ATOM   6614 C C     . MET B 1 328 ? 22.048  117.107 58.770 1.00 26.00 ? 328  MET B C     1 
ATOM   6615 O O     . MET B 1 328 ? 22.279  116.610 59.891 1.00 22.52 ? 328  MET B O     1 
ATOM   6616 C CB    . MET B 1 328 ? 22.908  115.770 56.810 1.00 23.85 ? 328  MET B CB    1 
ATOM   6617 C CG    . MET B 1 328 ? 22.624  114.706 55.713 1.00 21.52 ? 328  MET B CG    1 
ATOM   6618 S SD    . MET B 1 328 ? 24.187  114.062 55.051 1.00 22.97 ? 328  MET B SD    1 
ATOM   6619 C CE    . MET B 1 328 ? 24.759  115.424 54.020 1.00 23.91 ? 328  MET B CE    1 
ATOM   6620 N N     . ASP B 1 329 ? 22.132  118.414 58.523 1.00 25.41 ? 329  ASP B N     1 
ATOM   6621 C CA    . ASP B 1 329 ? 22.416  119.414 59.605 1.00 30.58 ? 329  ASP B CA    1 
ATOM   6622 C C     . ASP B 1 329 ? 21.377  119.329 60.735 1.00 24.26 ? 329  ASP B C     1 
ATOM   6623 O O     . ASP B 1 329 ? 21.767  119.291 61.932 1.00 25.82 ? 329  ASP B O     1 
ATOM   6624 C CB    . ASP B 1 329 ? 22.433  120.837 59.041 1.00 32.51 ? 329  ASP B CB    1 
ATOM   6625 C CG    . ASP B 1 329 ? 23.614  121.057 58.108 1.00 31.97 ? 329  ASP B CG    1 
ATOM   6626 O OD1   . ASP B 1 329 ? 24.648  120.361 58.259 1.00 34.35 ? 329  ASP B OD1   1 
ATOM   6627 O OD2   . ASP B 1 329 ? 23.500  121.929 57.261 1.00 34.67 ? 329  ASP B OD2   1 
ATOM   6628 N N     . THR B 1 330 ? 20.103  119.269 60.382 1.00 24.17 ? 330  THR B N     1 
ATOM   6629 C CA    . THR B 1 330 ? 18.993  119.152 61.364 1.00 26.18 ? 330  THR B CA    1 
ATOM   6630 C C     . THR B 1 330 ? 19.126  117.872 62.185 1.00 27.54 ? 330  THR B C     1 
ATOM   6631 O O     . THR B 1 330 ? 18.934  117.925 63.413 1.00 23.84 ? 330  THR B O     1 
ATOM   6632 C CB    . THR B 1 330 ? 17.635  119.184 60.678 1.00 27.17 ? 330  THR B CB    1 
ATOM   6633 O OG1   . THR B 1 330 ? 17.597  120.401 59.950 1.00 31.59 ? 330  THR B OG1   1 
ATOM   6634 C CG2   . THR B 1 330 ? 16.486  119.057 61.655 1.00 29.08 ? 330  THR B CG2   1 
ATOM   6635 N N     . LEU B 1 331 ? 19.405  116.731 61.548 1.00 25.73 ? 331  LEU B N     1 
ATOM   6636 C CA    . LEU B 1 331 ? 19.475  115.431 62.263 1.00 25.03 ? 331  LEU B CA    1 
ATOM   6637 C C     . LEU B 1 331 ? 20.693  115.447 63.173 1.00 22.57 ? 331  LEU B C     1 
ATOM   6638 O O     . LEU B 1 331 ? 20.569  114.973 64.316 1.00 23.60 ? 331  LEU B O     1 
ATOM   6639 C CB    . LEU B 1 331 ? 19.515  114.263 61.268 1.00 26.28 ? 331  LEU B CB    1 
ATOM   6640 C CG    . LEU B 1 331 ? 18.329  114.222 60.326 1.00 27.42 ? 331  LEU B CG    1 
ATOM   6641 C CD1   . LEU B 1 331 ? 18.401  113.036 59.394 1.00 30.60 ? 331  LEU B CD1   1 
ATOM   6642 C CD2   . LEU B 1 331 ? 17.019  114.211 61.086 1.00 29.23 ? 331  LEU B CD2   1 
ATOM   6643 N N     . TRP B 1 332 ? 21.806  115.991 62.700 1.00 21.82 ? 332  TRP B N     1 
ATOM   6644 C CA    . TRP B 1 332 ? 23.066  116.035 63.484 1.00 24.48 ? 332  TRP B CA    1 
ATOM   6645 C C     . TRP B 1 332 ? 22.870  116.857 64.771 1.00 22.08 ? 332  TRP B C     1 
ATOM   6646 O O     . TRP B 1 332 ? 23.335  116.385 65.828 1.00 23.42 ? 332  TRP B O     1 
ATOM   6647 C CB    . TRP B 1 332 ? 24.273  116.530 62.660 1.00 24.86 ? 332  TRP B CB    1 
ATOM   6648 C CG    . TRP B 1 332 ? 25.508  116.497 63.497 1.00 25.71 ? 332  TRP B CG    1 
ATOM   6649 C CD1   . TRP B 1 332 ? 26.308  117.551 63.855 1.00 25.63 ? 332  TRP B CD1   1 
ATOM   6650 C CD2   . TRP B 1 332 ? 26.062  115.333 64.131 1.00 25.84 ? 332  TRP B CD2   1 
ATOM   6651 N NE1   . TRP B 1 332 ? 27.284  117.116 64.723 1.00 26.39 ? 332  TRP B NE1   1 
ATOM   6652 C CE2   . TRP B 1 332 ? 27.166  115.766 64.895 1.00 26.41 ? 332  TRP B CE2   1 
ATOM   6653 C CE3   . TRP B 1 332 ? 25.713  113.977 64.171 1.00 25.08 ? 332  TRP B CE3   1 
ATOM   6654 C CZ2   . TRP B 1 332 ? 27.943  114.891 65.627 1.00 25.79 ? 332  TRP B CZ2   1 
ATOM   6655 C CZ3   . TRP B 1 332 ? 26.492  113.119 64.898 1.00 26.23 ? 332  TRP B CZ3   1 
ATOM   6656 C CH2   . TRP B 1 332 ? 27.572  113.577 65.649 1.00 27.10 ? 332  TRP B CH2   1 
ATOM   6657 N N     . THR B 1 333 ? 22.170  117.986 64.685 1.00 23.74 ? 333  THR B N     1 
ATOM   6658 C CA    . THR B 1 333 ? 21.874  118.844 65.872 1.00 24.04 ? 333  THR B CA    1 
ATOM   6659 C C     . THR B 1 333 ? 21.126  117.971 66.885 1.00 25.39 ? 333  THR B C     1 
ATOM   6660 O O     . THR B 1 333 ? 21.510  117.977 68.058 1.00 25.90 ? 333  THR B O     1 
ATOM   6661 C CB    . THR B 1 333 ? 21.165  120.135 65.448 1.00 26.83 ? 333  THR B CB    1 
ATOM   6662 O OG1   . THR B 1 333 ? 22.040  120.889 64.607 1.00 27.39 ? 333  THR B OG1   1 
ATOM   6663 C CG2   . THR B 1 333 ? 20.807  121.029 66.615 1.00 29.97 ? 333  THR B CG2   1 
ATOM   6664 N N     . ALA B 1 334 ? 20.135  117.170 66.445 1.00 23.53 ? 334  ALA B N     1 
ATOM   6665 C CA    . ALA B 1 334 ? 19.284  116.391 67.373 1.00 25.43 ? 334  ALA B CA    1 
ATOM   6666 C C     . ALA B 1 334 ? 20.128  115.258 67.957 1.00 25.35 ? 334  ALA B C     1 
ATOM   6667 O O     . ALA B 1 334 ? 20.024  114.998 69.145 1.00 23.68 ? 334  ALA B O     1 
ATOM   6668 C CB    . ALA B 1 334 ? 18.038  115.910 66.689 1.00 26.31 ? 334  ALA B CB    1 
ATOM   6669 N N     . ILE B 1 335 ? 21.016  114.645 67.168 1.00 20.94 ? 335  ILE B N     1 
ATOM   6670 C CA    . ILE B 1 335 ? 21.809  113.495 67.664 1.00 21.74 ? 335  ILE B CA    1 
ATOM   6671 C C     . ILE B 1 335 ? 22.860  114.050 68.618 1.00 22.32 ? 335  ILE B C     1 
ATOM   6672 O O     . ILE B 1 335 ? 22.998  113.528 69.744 1.00 23.34 ? 335  ILE B O     1 
ATOM   6673 C CB    . ILE B 1 335 ? 22.419  112.688 66.492 1.00 21.50 ? 335  ILE B CB    1 
ATOM   6674 C CG1   . ILE B 1 335 ? 21.327  111.987 65.670 1.00 21.87 ? 335  ILE B CG1   1 
ATOM   6675 C CG2   . ILE B 1 335 ? 23.419  111.692 67.002 1.00 23.35 ? 335  ILE B CG2   1 
ATOM   6676 C CD1   . ILE B 1 335 ? 21.750  111.609 64.306 1.00 23.51 ? 335  ILE B CD1   1 
ATOM   6677 N N     . ARG B 1 336 ? 23.606  115.050 68.159 1.00 20.88 ? 336  ARG B N     1 
ATOM   6678 C CA    . ARG B 1 336 ? 24.723  115.590 68.961 1.00 24.28 ? 336  ARG B CA    1 
ATOM   6679 C C     . ARG B 1 336 ? 24.196  116.100 70.305 1.00 24.44 ? 336  ARG B C     1 
ATOM   6680 O O     . ARG B 1 336 ? 24.802  115.767 71.339 1.00 25.24 ? 336  ARG B O     1 
ATOM   6681 C CB    . ARG B 1 336 ? 25.417  116.760 68.267 1.00 24.17 ? 336  ARG B CB    1 
ATOM   6682 C CG    . ARG B 1 336 ? 26.696  117.146 69.003 1.00 32.51 ? 336  ARG B CG    1 
ATOM   6683 C CD    . ARG B 1 336 ? 27.357  118.385 68.455 1.00 37.23 ? 336  ARG B CD    1 
ATOM   6684 N NE    . ARG B 1 336 ? 28.806  118.334 68.718 1.00 44.91 ? 336  ARG B NE    1 
ATOM   6685 C CZ    . ARG B 1 336 ? 29.395  118.746 69.833 1.00 46.77 ? 336  ARG B CZ    1 
ATOM   6686 N NH1   . ARG B 1 336 ? 28.658  119.225 70.823 1.00 52.13 ? 336  ARG B NH1   1 
ATOM   6687 N NH2   . ARG B 1 336 ? 30.708  118.665 69.978 1.00 47.70 ? 336  ARG B NH2   1 
ATOM   6688 N N     . ASP B 1 337 ? 23.158  116.932 70.264 1.00 25.32 ? 337  ASP B N     1 
ATOM   6689 C CA    . ASP B 1 337 ? 22.529  117.471 71.510 1.00 29.25 ? 337  ASP B CA    1 
ATOM   6690 C C     . ASP B 1 337 ? 22.086  116.345 72.446 1.00 30.36 ? 337  ASP B C     1 
ATOM   6691 O O     . ASP B 1 337 ? 22.052  116.617 73.634 1.00 26.36 ? 337  ASP B O     1 
ATOM   6692 C CB    . ASP B 1 337 ? 21.352  118.401 71.229 1.00 30.20 ? 337  ASP B CB    1 
ATOM   6693 C CG    . ASP B 1 337 ? 21.756  119.701 70.570 1.00 33.60 ? 337  ASP B CG    1 
ATOM   6694 O OD1   . ASP B 1 337 ? 22.997  119.895 70.363 1.00 35.55 ? 337  ASP B OD1   1 
ATOM   6695 O OD2   . ASP B 1 337 ? 20.842  120.478 70.220 1.00 38.43 ? 337  ASP B OD2   1 
ATOM   6696 N N     . SER B 1 338 ? 21.747  115.140 71.965 1.00 26.48 ? 338  SER B N     1 
ATOM   6697 C CA    . SER B 1 338 ? 21.239  114.031 72.824 1.00 27.00 ? 338  SER B CA    1 
ATOM   6698 C C     . SER B 1 338 ? 22.365  113.475 73.687 1.00 26.44 ? 338  SER B C     1 
ATOM   6699 O O     . SER B 1 338 ? 22.046  112.820 74.655 1.00 25.89 ? 338  SER B O     1 
ATOM   6700 C CB    . SER B 1 338 ? 20.599  112.891 72.042 1.00 24.28 ? 338  SER B CB    1 
ATOM   6701 O OG    . SER B 1 338 ? 19.480  113.366 71.325 1.00 26.88 ? 338  SER B OG    1 
ATOM   6702 N N     . PHE B 1 339 ? 23.635  113.621 73.279 1.00 23.99 ? 339  PHE B N     1 
ATOM   6703 C CA    . PHE B 1 339 ? 24.757  112.941 73.966 1.00 23.62 ? 339  PHE B CA    1 
ATOM   6704 C C     . PHE B 1 339 ? 25.694  113.952 74.643 1.00 24.15 ? 339  PHE B C     1 
ATOM   6705 O O     . PHE B 1 339 ? 26.566  113.478 75.378 1.00 25.78 ? 339  PHE B O     1 
ATOM   6706 C CB    . PHE B 1 339 ? 25.509  112.023 72.984 1.00 24.11 ? 339  PHE B CB    1 
ATOM   6707 C CG    . PHE B 1 339 ? 24.620  110.925 72.464 1.00 21.24 ? 339  PHE B CG    1 
ATOM   6708 C CD1   . PHE B 1 339 ? 24.283  109.868 73.272 1.00 24.13 ? 339  PHE B CD1   1 
ATOM   6709 C CD2   . PHE B 1 339 ? 24.001  111.034 71.235 1.00 26.02 ? 339  PHE B CD2   1 
ATOM   6710 C CE1   . PHE B 1 339 ? 23.403  108.889 72.832 1.00 24.40 ? 339  PHE B CE1   1 
ATOM   6711 C CE2   . PHE B 1 339 ? 23.094  110.070 70.813 1.00 23.89 ? 339  PHE B CE2   1 
ATOM   6712 C CZ    . PHE B 1 339 ? 22.809  108.999 71.607 1.00 23.95 ? 339  PHE B CZ    1 
ATOM   6713 N N     . ALA B 1 340 ? 25.568  115.243 74.336 1.00 25.38 ? 340  ALA B N     1 
ATOM   6714 C CA    . ALA B 1 340 ? 26.641  116.247 74.540 1.00 27.67 ? 340  ALA B CA    1 
ATOM   6715 C C     . ALA B 1 340 ? 26.888  116.444 76.030 1.00 29.33 ? 340  ALA B C     1 
ATOM   6716 O O     . ALA B 1 340 ? 27.988  116.857 76.316 1.00 28.84 ? 340  ALA B O     1 
ATOM   6717 C CB    . ALA B 1 340 ? 26.330  117.574 73.908 1.00 26.13 ? 340  ALA B CB    1 
ATOM   6718 N N     . ASP B 1 341 ? 25.961  116.073 76.923 1.00 29.21 ? 341  ASP B N     1 
ATOM   6719 C CA    . ASP B 1 341 ? 26.133  116.334 78.377 1.00 31.31 ? 341  ASP B CA    1 
ATOM   6720 C C     . ASP B 1 341 ? 26.644  115.088 79.112 1.00 33.60 ? 341  ASP B C     1 
ATOM   6721 O O     . ASP B 1 341 ? 26.822  115.143 80.326 1.00 31.63 ? 341  ASP B O     1 
ATOM   6722 C CB    . ASP B 1 341 ? 24.841  116.931 78.933 1.00 35.87 ? 341  ASP B CB    1 
ATOM   6723 C CG    . ASP B 1 341 ? 23.735  115.918 79.146 1.00 39.05 ? 341  ASP B CG    1 
ATOM   6724 O OD1   . ASP B 1 341 ? 23.879  114.785 78.717 1.00 42.99 ? 341  ASP B OD1   1 
ATOM   6725 O OD2   . ASP B 1 341 ? 22.767  116.275 79.777 1.00 46.57 ? 341  ASP B OD2   1 
ATOM   6726 N N     . ILE B 1 342 ? 26.920  113.980 78.443 1.00 29.00 ? 342  ILE B N     1 
ATOM   6727 C CA    . ILE B 1 342 ? 27.472  112.799 79.151 1.00 27.19 ? 342  ILE B CA    1 
ATOM   6728 C C     . ILE B 1 342 ? 28.947  113.058 79.405 1.00 31.45 ? 342  ILE B C     1 
ATOM   6729 O O     . ILE B 1 342 ? 29.685  113.354 78.453 1.00 29.78 ? 342  ILE B O     1 
ATOM   6730 C CB    . ILE B 1 342 ? 27.259  111.530 78.330 1.00 27.12 ? 342  ILE B CB    1 
ATOM   6731 C CG1   . ILE B 1 342 ? 25.762  111.294 78.102 1.00 28.75 ? 342  ILE B CG1   1 
ATOM   6732 C CG2   . ILE B 1 342 ? 27.991  110.353 78.959 1.00 25.71 ? 342  ILE B CG2   1 
ATOM   6733 C CD1   . ILE B 1 342 ? 25.484  110.343 76.953 1.00 29.19 ? 342  ILE B CD1   1 
ATOM   6734 N N     . PRO B 1 343 ? 29.422  112.998 80.674 1.00 28.51 ? 343  PRO B N     1 
ATOM   6735 C CA    . PRO B 1 343 ? 30.845  113.202 80.945 1.00 29.27 ? 343  PRO B CA    1 
ATOM   6736 C C     . PRO B 1 343 ? 31.704  112.216 80.147 1.00 27.88 ? 343  PRO B C     1 
ATOM   6737 O O     . PRO B 1 343 ? 31.450  110.992 80.162 1.00 28.52 ? 343  PRO B O     1 
ATOM   6738 C CB    . PRO B 1 343 ? 31.020  112.946 82.456 1.00 29.23 ? 343  PRO B CB    1 
ATOM   6739 C CG    . PRO B 1 343 ? 29.608  113.222 83.013 1.00 33.24 ? 343  PRO B CG    1 
ATOM   6740 C CD    . PRO B 1 343 ? 28.646  112.770 81.915 1.00 32.15 ? 343  PRO B CD    1 
ATOM   6741 N N     . GLY B 1 344 ? 32.727  112.743 79.490 1.00 24.95 ? 344  GLY B N     1 
ATOM   6742 C CA    . GLY B 1 344 ? 33.734  111.915 78.785 1.00 27.27 ? 344  GLY B CA    1 
ATOM   6743 C C     . GLY B 1 344 ? 33.365  111.678 77.316 1.00 28.08 ? 344  GLY B C     1 
ATOM   6744 O O     . GLY B 1 344 ? 34.126  110.977 76.625 1.00 25.91 ? 344  GLY B O     1 
ATOM   6745 N N     . VAL B 1 345 ? 32.212  112.155 76.864 1.00 26.44 ? 345  VAL B N     1 
ATOM   6746 C CA    . VAL B 1 345 ? 31.752  111.901 75.452 1.00 27.31 ? 345  VAL B CA    1 
ATOM   6747 C C     . VAL B 1 345 ? 32.697  112.622 74.489 1.00 27.89 ? 345  VAL B C     1 
ATOM   6748 O O     . VAL B 1 345 ? 33.118  113.740 74.793 1.00 25.45 ? 345  VAL B O     1 
ATOM   6749 C CB    . VAL B 1 345 ? 30.301  112.360 75.230 1.00 24.22 ? 345  VAL B CB    1 
ATOM   6750 C CG1   . VAL B 1 345 ? 30.124  113.871 75.369 1.00 26.58 ? 345  VAL B CG1   1 
ATOM   6751 C CG2   . VAL B 1 345 ? 29.766  111.887 73.898 1.00 25.52 ? 345  VAL B CG2   1 
ATOM   6752 N N     . LYS B 1 346 ? 32.964  112.019 73.332 1.00 27.05 ? 346  LYS B N     1 
ATOM   6753 C CA    . LYS B 1 346 ? 33.732  112.655 72.231 1.00 26.84 ? 346  LYS B CA    1 
ATOM   6754 C C     . LYS B 1 346 ? 32.996  112.380 70.928 1.00 26.66 ? 346  LYS B C     1 
ATOM   6755 O O     . LYS B 1 346 ? 32.473  111.254 70.781 1.00 24.05 ? 346  LYS B O     1 
ATOM   6756 C CB    . LYS B 1 346 ? 35.123  112.017 72.169 1.00 29.64 ? 346  LYS B CB    1 
ATOM   6757 C CG    . LYS B 1 346 ? 35.956  112.147 73.427 1.00 30.59 ? 346  LYS B CG    1 
ATOM   6758 C CD    . LYS B 1 346 ? 36.474  113.530 73.552 1.00 35.98 ? 346  LYS B CD    1 
ATOM   6759 C CE    . LYS B 1 346 ? 37.705  113.753 72.690 1.00 45.45 ? 346  LYS B CE    1 
ATOM   6760 N NZ    . LYS B 1 346 ? 38.007  115.195 72.530 1.00 46.43 ? 346  LYS B NZ    1 
ATOM   6761 N N     . PHE B 1 347 ? 32.967  113.376 70.053 1.00 26.89 ? 347  PHE B N     1 
ATOM   6762 C CA    . PHE B 1 347 ? 32.343  113.376 68.710 1.00 26.17 ? 347  PHE B CA    1 
ATOM   6763 C C     . PHE B 1 347 ? 33.421  113.425 67.622 1.00 27.88 ? 347  PHE B C     1 
ATOM   6764 O O     . PHE B 1 347 ? 34.318  114.316 67.682 1.00 26.67 ? 347  PHE B O     1 
ATOM   6765 C CB    . PHE B 1 347 ? 31.441  114.589 68.545 1.00 27.09 ? 347  PHE B CB    1 
ATOM   6766 C CG    . PHE B 1 347 ? 30.328  114.662 69.553 1.00 28.12 ? 347  PHE B CG    1 
ATOM   6767 C CD1   . PHE B 1 347 ? 29.141  113.993 69.336 1.00 24.80 ? 347  PHE B CD1   1 
ATOM   6768 C CD2   . PHE B 1 347 ? 30.508  115.337 70.759 1.00 31.20 ? 347  PHE B CD2   1 
ATOM   6769 C CE1   . PHE B 1 347 ? 28.111  114.067 70.257 1.00 28.75 ? 347  PHE B CE1   1 
ATOM   6770 C CE2   . PHE B 1 347 ? 29.483  115.381 71.696 1.00 31.18 ? 347  PHE B CE2   1 
ATOM   6771 C CZ    . PHE B 1 347 ? 28.287  114.747 71.448 1.00 29.95 ? 347  PHE B CZ    1 
ATOM   6772 N N     . TYR B 1 348 ? 33.324  112.535 66.615 1.00 24.33 ? 348  TYR B N     1 
ATOM   6773 C CA    . TYR B 1 348 ? 34.271  112.554 65.480 1.00 23.40 ? 348  TYR B CA    1 
ATOM   6774 C C     . TYR B 1 348 ? 33.536  112.452 64.158 1.00 23.21 ? 348  TYR B C     1 
ATOM   6775 O O     . TYR B 1 348 ? 32.615  111.666 64.046 1.00 21.70 ? 348  TYR B O     1 
ATOM   6776 C CB    . TYR B 1 348 ? 35.263  111.406 65.586 1.00 23.17 ? 348  TYR B CB    1 
ATOM   6777 C CG    . TYR B 1 348 ? 36.045  111.312 66.864 1.00 24.06 ? 348  TYR B CG    1 
ATOM   6778 C CD1   . TYR B 1 348 ? 35.585  110.555 67.931 1.00 25.73 ? 348  TYR B CD1   1 
ATOM   6779 C CD2   . TYR B 1 348 ? 37.302  111.892 66.985 1.00 25.21 ? 348  TYR B CD2   1 
ATOM   6780 C CE1   . TYR B 1 348 ? 36.325  110.410 69.093 1.00 26.31 ? 348  TYR B CE1   1 
ATOM   6781 C CE2   . TYR B 1 348 ? 38.053  111.764 68.152 1.00 27.90 ? 348  TYR B CE2   1 
ATOM   6782 C CZ    . TYR B 1 348 ? 37.564  111.031 69.222 1.00 28.31 ? 348  TYR B CZ    1 
ATOM   6783 O OH    . TYR B 1 348 ? 38.313  110.854 70.366 1.00 28.47 ? 348  TYR B OH    1 
ATOM   6784 N N     . PHE B 1 349 ? 33.956  113.257 63.182 1.00 24.75 ? 349  PHE B N     1 
ATOM   6785 C CA    . PHE B 1 349 ? 33.807  112.956 61.736 1.00 25.40 ? 349  PHE B CA    1 
ATOM   6786 C C     . PHE B 1 349 ? 35.138  112.389 61.255 1.00 24.35 ? 349  PHE B C     1 
ATOM   6787 O O     . PHE B 1 349 ? 36.134  112.371 61.996 1.00 23.88 ? 349  PHE B O     1 
ATOM   6788 C CB    . PHE B 1 349 ? 33.328  114.196 60.970 1.00 26.62 ? 349  PHE B CB    1 
ATOM   6789 C CG    . PHE B 1 349 ? 32.038  114.761 61.490 1.00 29.80 ? 349  PHE B CG    1 
ATOM   6790 C CD1   . PHE B 1 349 ? 30.883  113.994 61.492 1.00 30.36 ? 349  PHE B CD1   1 
ATOM   6791 C CD2   . PHE B 1 349 ? 31.957  116.066 61.954 1.00 33.47 ? 349  PHE B CD2   1 
ATOM   6792 C CE1   . PHE B 1 349 ? 29.678  114.512 61.938 1.00 33.40 ? 349  PHE B CE1   1 
ATOM   6793 C CE2   . PHE B 1 349 ? 30.748  116.592 62.393 1.00 34.78 ? 349  PHE B CE2   1 
ATOM   6794 C CZ    . PHE B 1 349 ? 29.615  115.806 62.404 1.00 35.39 ? 349  PHE B CZ    1 
ATOM   6795 N N     . PRO B 1 350 ? 35.176  111.780 60.054 1.00 22.23 ? 350  PRO B N     1 
ATOM   6796 C CA    . PRO B 1 350 ? 36.409  111.120 59.609 1.00 23.80 ? 350  PRO B CA    1 
ATOM   6797 C C     . PRO B 1 350 ? 37.611  112.085 59.643 1.00 22.09 ? 350  PRO B C     1 
ATOM   6798 O O     . PRO B 1 350 ? 38.674  111.645 59.978 1.00 24.28 ? 350  PRO B O     1 
ATOM   6799 C CB    . PRO B 1 350 ? 36.028  110.647 58.191 1.00 24.94 ? 350  PRO B CB    1 
ATOM   6800 C CG    . PRO B 1 350 ? 34.523  110.345 58.328 1.00 23.10 ? 350  PRO B CG    1 
ATOM   6801 C CD    . PRO B 1 350 ? 34.015  111.493 59.172 1.00 23.22 ? 350  PRO B CD    1 
ATOM   6802 N N     . GLU B 1 351 ? 37.397  113.353 59.311 1.00 24.65 ? 351  GLU B N     1 
ATOM   6803 C CA    . GLU B 1 351 ? 38.497  114.357 59.175 1.00 28.19 ? 351  GLU B CA    1 
ATOM   6804 C C     . GLU B 1 351 ? 39.109  114.574 60.557 1.00 30.87 ? 351  GLU B C     1 
ATOM   6805 O O     . GLU B 1 351 ? 40.224  114.983 60.617 1.00 30.94 ? 351  GLU B O     1 
ATOM   6806 C CB    . GLU B 1 351 ? 38.001  115.670 58.577 1.00 30.62 ? 351  GLU B CB    1 
ATOM   6807 C CG    . GLU B 1 351 ? 37.351  116.557 59.572 1.00 38.24 ? 351  GLU B CG    1 
ATOM   6808 C CD    . GLU B 1 351 ? 35.953  116.961 59.196 1.00 48.32 ? 351  GLU B CD    1 
ATOM   6809 O OE1   . GLU B 1 351 ? 35.153  116.049 58.849 1.00 63.92 ? 351  GLU B OE1   1 
ATOM   6810 O OE2   . GLU B 1 351 ? 35.672  118.163 59.272 1.00 54.14 ? 351  GLU B OE2   1 
ATOM   6811 N N     . ASP B 1 352 ? 38.415  114.192 61.622 1.00 29.43 ? 352  ASP B N     1 
ATOM   6812 C CA    . ASP B 1 352 ? 38.866  114.380 63.021 1.00 29.17 ? 352  ASP B CA    1 
ATOM   6813 C C     . ASP B 1 352 ? 39.701  113.179 63.450 1.00 29.82 ? 352  ASP B C     1 
ATOM   6814 O O     . ASP B 1 352 ? 40.167  113.201 64.572 1.00 33.63 ? 352  ASP B O     1 
ATOM   6815 C CB    . ASP B 1 352 ? 37.700  114.551 63.990 1.00 30.25 ? 352  ASP B CB    1 
ATOM   6816 C CG    . ASP B 1 352 ? 36.805  115.731 63.711 1.00 34.32 ? 352  ASP B CG    1 
ATOM   6817 O OD1   . ASP B 1 352 ? 37.368  116.814 63.525 1.00 31.76 ? 352  ASP B OD1   1 
ATOM   6818 O OD2   . ASP B 1 352 ? 35.531  115.572 63.665 1.00 28.66 ? 352  ASP B OD2   1 
ATOM   6819 N N     . ARG B 1 353 ? 39.843  112.123 62.656 1.00 26.02 ? 353  ARG B N     1 
ATOM   6820 C CA    . ARG B 1 353 ? 40.500  110.899 63.166 1.00 25.63 ? 353  ARG B CA    1 
ATOM   6821 C C     . ARG B 1 353 ? 41.989  111.009 62.872 1.00 28.04 ? 353  ARG B C     1 
ATOM   6822 O O     . ARG B 1 353 ? 42.324  111.366 61.743 1.00 30.95 ? 353  ARG B O     1 
ATOM   6823 C CB    . ARG B 1 353 ? 39.892  109.613 62.601 1.00 25.44 ? 353  ARG B CB    1 
ATOM   6824 C CG    . ARG B 1 353 ? 38.395  109.497 62.834 1.00 25.12 ? 353  ARG B CG    1 
ATOM   6825 C CD    . ARG B 1 353 ? 38.076  109.315 64.312 1.00 23.38 ? 353  ARG B CD    1 
ATOM   6826 N NE    . ARG B 1 353 ? 38.546  108.028 64.737 1.00 23.81 ? 353  ARG B NE    1 
ATOM   6827 C CZ    . ARG B 1 353 ? 38.626  107.626 66.003 1.00 23.43 ? 353  ARG B CZ    1 
ATOM   6828 N NH1   . ARG B 1 353 ? 38.244  108.434 66.969 1.00 22.01 ? 353  ARG B NH1   1 
ATOM   6829 N NH2   . ARG B 1 353 ? 39.061  106.412 66.277 1.00 23.60 ? 353  ARG B NH2   1 
ATOM   6830 N N     . ARG B 1 354 ? 42.812  110.525 63.790 1.00 28.41 ? 354  ARG B N     1 
ATOM   6831 C CA    . ARG B 1 354 ? 44.292  110.642 63.740 1.00 32.89 ? 354  ARG B CA    1 
ATOM   6832 C C     . ARG B 1 354 ? 44.884  109.523 62.894 1.00 28.67 ? 354  ARG B C     1 
ATOM   6833 O O     . ARG B 1 354 ? 45.833  109.784 62.235 1.00 35.34 ? 354  ARG B O     1 
ATOM   6834 C CB    . ARG B 1 354 ? 44.959  110.439 65.112 1.00 35.21 ? 354  ARG B CB    1 
ATOM   6835 C CG    . ARG B 1 354 ? 44.973  111.626 66.047 1.00 46.21 ? 354  ARG B CG    1 
ATOM   6836 C CD    . ARG B 1 354 ? 46.041  111.339 67.115 1.00 52.70 ? 354  ARG B CD    1 
ATOM   6837 N NE    . ARG B 1 354 ? 45.584  110.449 68.187 1.00 46.08 ? 354  ARG B NE    1 
ATOM   6838 C CZ    . ARG B 1 354 ? 46.135  109.275 68.545 1.00 48.05 ? 354  ARG B CZ    1 
ATOM   6839 N NH1   . ARG B 1 354 ? 47.213  108.798 67.934 1.00 42.14 ? 354  ARG B NH1   1 
ATOM   6840 N NH2   . ARG B 1 354 ? 45.589  108.579 69.550 1.00 46.40 ? 354  ARG B NH2   1 
ATOM   6841 N N     . HIS B 1 355 ? 44.425  108.290 63.025 1.00 26.40 ? 355  HIS B N     1 
ATOM   6842 C CA    . HIS B 1 355 ? 45.038  107.095 62.400 1.00 26.47 ? 355  HIS B CA    1 
ATOM   6843 C C     . HIS B 1 355 ? 44.528  106.928 60.966 1.00 25.83 ? 355  HIS B C     1 
ATOM   6844 O O     . HIS B 1 355 ? 43.363  107.188 60.724 1.00 28.28 ? 355  HIS B O     1 
ATOM   6845 C CB    . HIS B 1 355 ? 44.780  105.828 63.218 1.00 29.46 ? 355  HIS B CB    1 
ATOM   6846 C CG    . HIS B 1 355 ? 45.360  105.825 64.598 1.00 31.36 ? 355  HIS B CG    1 
ATOM   6847 N ND1   . HIS B 1 355 ? 44.701  106.377 65.663 1.00 35.30 ? 355  HIS B ND1   1 
ATOM   6848 C CD2   . HIS B 1 355 ? 46.487  105.285 65.098 1.00 32.30 ? 355  HIS B CD2   1 
ATOM   6849 C CE1   . HIS B 1 355 ? 45.419  106.203 66.765 1.00 36.20 ? 355  HIS B CE1   1 
ATOM   6850 N NE2   . HIS B 1 355 ? 46.502  105.539 66.458 1.00 33.30 ? 355  HIS B NE2   1 
ATOM   6851 N N     . LYS B 1 356 ? 45.415  106.536 60.066 1.00 27.97 ? 356  LYS B N     1 
ATOM   6852 C CA    . LYS B 1 356 ? 45.133  106.234 58.638 1.00 31.88 ? 356  LYS B CA    1 
ATOM   6853 C C     . LYS B 1 356 ? 44.304  104.949 58.569 1.00 31.30 ? 356  LYS B C     1 
ATOM   6854 O O     . LYS B 1 356 ? 43.427  104.859 57.700 1.00 32.49 ? 356  LYS B O     1 
ATOM   6855 C CB    . LYS B 1 356 ? 46.477  106.104 57.908 1.00 39.15 ? 356  LYS B CB    1 
ATOM   6856 C CG    . LYS B 1 356 ? 46.385  105.671 56.442 1.00 47.85 ? 356  LYS B CG    1 
ATOM   6857 C CD    . LYS B 1 356 ? 47.734  105.634 55.711 1.00 46.20 ? 356  LYS B CD    1 
ATOM   6858 C CE    . LYS B 1 356 ? 47.639  105.033 54.320 1.00 47.59 ? 356  LYS B CE    1 
ATOM   6859 N NZ    . LYS B 1 356 ? 47.098  105.998 53.331 1.00 45.80 ? 356  LYS B NZ    1 
ATOM   6860 N N     . VAL B 1 357 ? 44.654  103.954 59.393 1.00 28.81 ? 357  VAL B N     1 
ATOM   6861 C CA    . VAL B 1 357 ? 43.909  102.676 59.553 1.00 29.95 ? 357  VAL B CA    1 
ATOM   6862 C C     . VAL B 1 357 ? 43.105  102.791 60.857 1.00 29.33 ? 357  VAL B C     1 
ATOM   6863 O O     . VAL B 1 357 ? 43.720  102.831 61.947 1.00 27.44 ? 357  VAL B O     1 
ATOM   6864 C CB    . VAL B 1 357 ? 44.880  101.492 59.548 1.00 32.53 ? 357  VAL B CB    1 
ATOM   6865 C CG1   . VAL B 1 357 ? 44.156  100.161 59.737 1.00 36.29 ? 357  VAL B CG1   1 
ATOM   6866 C CG2   . VAL B 1 357 ? 45.692  101.501 58.238 1.00 36.15 ? 357  VAL B CG2   1 
ATOM   6867 N N     . ASP B 1 358 ? 41.796  102.950 60.731 1.00 26.58 ? 358  ASP B N     1 
ATOM   6868 C CA    . ASP B 1 358 ? 40.922  103.463 61.819 1.00 28.03 ? 358  ASP B CA    1 
ATOM   6869 C C     . ASP B 1 358 ? 39.509  102.878 61.714 1.00 28.66 ? 358  ASP B C     1 
ATOM   6870 O O     . ASP B 1 358 ? 38.993  102.758 60.571 1.00 24.50 ? 358  ASP B O     1 
ATOM   6871 C CB    . ASP B 1 358 ? 40.851  104.977 61.735 1.00 25.12 ? 358  ASP B CB    1 
ATOM   6872 C CG    . ASP B 1 358 ? 40.132  105.612 62.893 1.00 26.04 ? 358  ASP B CG    1 
ATOM   6873 O OD1   . ASP B 1 358 ? 40.733  105.697 64.033 1.00 24.69 ? 358  ASP B OD1   1 
ATOM   6874 O OD2   . ASP B 1 358 ? 38.973  106.057 62.659 1.00 25.50 ? 358  ASP B OD2   1 
ATOM   6875 N N     . LEU B 1 359 ? 38.880  102.614 62.868 1.00 27.76 ? 359  LEU B N     1 
ATOM   6876 C CA    . LEU B 1 359 ? 37.462  102.166 62.936 1.00 27.32 ? 359  LEU B CA    1 
ATOM   6877 C C     . LEU B 1 359 ? 36.514  103.029 62.093 1.00 23.93 ? 359  LEU B C     1 
ATOM   6878 O O     . LEU B 1 359 ? 35.693  102.468 61.313 1.00 26.45 ? 359  LEU B O     1 
ATOM   6879 C CB    . LEU B 1 359 ? 36.979  102.197 64.384 1.00 30.82 ? 359  LEU B CB    1 
ATOM   6880 C CG    . LEU B 1 359 ? 35.472  101.950 64.482 1.00 35.21 ? 359  LEU B CG    1 
ATOM   6881 C CD1   . LEU B 1 359 ? 35.239  100.463 64.262 1.00 35.44 ? 359  LEU B CD1   1 
ATOM   6882 C CD2   . LEU B 1 359 ? 34.921  102.501 65.777 1.00 39.37 ? 359  LEU B CD2   1 
ATOM   6883 N N     . LEU B 1 360 ? 36.480  104.333 62.299 1.00 21.34 ? 360  LEU B N     1 
ATOM   6884 C CA    . LEU B 1 360 ? 35.478  105.174 61.627 1.00 23.69 ? 360  LEU B CA    1 
ATOM   6885 C C     . LEU B 1 360 ? 35.698  105.183 60.108 1.00 26.71 ? 360  LEU B C     1 
ATOM   6886 O O     . LEU B 1 360 ? 34.711  105.130 59.357 1.00 23.85 ? 360  LEU B O     1 
ATOM   6887 C CB    . LEU B 1 360 ? 35.482  106.571 62.199 1.00 23.06 ? 360  LEU B CB    1 
ATOM   6888 C CG    . LEU B 1 360 ? 34.578  107.551 61.467 1.00 24.51 ? 360  LEU B CG    1 
ATOM   6889 C CD1   . LEU B 1 360 ? 33.143  107.036 61.421 1.00 26.64 ? 360  LEU B CD1   1 
ATOM   6890 C CD2   . LEU B 1 360 ? 34.630  108.925 62.122 1.00 26.22 ? 360  LEU B CD2   1 
ATOM   6891 N N     . LEU B 1 361 ? 36.938  105.244 59.663 1.00 27.74 ? 361  LEU B N     1 
ATOM   6892 C CA    . LEU B 1 361 ? 37.227  105.273 58.200 1.00 28.64 ? 361  LEU B CA    1 
ATOM   6893 C C     . LEU B 1 361 ? 36.751  103.945 57.599 1.00 25.21 ? 361  LEU B C     1 
ATOM   6894 O O     . LEU B 1 361 ? 36.193  103.947 56.491 1.00 25.07 ? 361  LEU B O     1 
ATOM   6895 C CB    . LEU B 1 361 ? 38.727  105.473 58.008 1.00 28.57 ? 361  LEU B CB    1 
ATOM   6896 C CG    . LEU B 1 361 ? 39.204  106.923 58.087 1.00 34.74 ? 361  LEU B CG    1 
ATOM   6897 C CD1   . LEU B 1 361 ? 38.674  107.670 59.327 1.00 29.59 ? 361  LEU B CD1   1 
ATOM   6898 C CD2   . LEU B 1 361 ? 40.729  106.943 58.033 1.00 32.64 ? 361  LEU B CD2   1 
ATOM   6899 N N     . HIS B 1 362 ? 36.945  102.842 58.320 1.00 25.38 ? 362  HIS B N     1 
ATOM   6900 C CA    . HIS B 1 362 ? 36.442  101.512 57.864 1.00 29.10 ? 362  HIS B CA    1 
ATOM   6901 C C     . HIS B 1 362 ? 34.899  101.502 57.816 1.00 24.69 ? 362  HIS B C     1 
ATOM   6902 O O     . HIS B 1 362 ? 34.327  101.180 56.747 1.00 23.03 ? 362  HIS B O     1 
ATOM   6903 C CB    . HIS B 1 362 ? 37.036  100.384 58.722 1.00 31.06 ? 362  HIS B CB    1 
ATOM   6904 C CG    . HIS B 1 362 ? 36.320  99.122  58.444 1.00 42.78 ? 362  HIS B CG    1 
ATOM   6905 N ND1   . HIS B 1 362 ? 35.605  98.415  59.426 1.00 51.59 ? 362  HIS B ND1   1 
ATOM   6906 C CD2   . HIS B 1 362 ? 36.104  98.492  57.266 1.00 48.35 ? 362  HIS B CD2   1 
ATOM   6907 C CE1   . HIS B 1 362 ? 35.011  97.383  58.846 1.00 54.00 ? 362  HIS B CE1   1 
ATOM   6908 N NE2   . HIS B 1 362 ? 35.306  97.403  57.518 1.00 58.64 ? 362  HIS B NE2   1 
ATOM   6909 N N     . ARG B 1 363 ? 34.224  101.866 58.919 1.00 21.93 ? 363  ARG B N     1 
ATOM   6910 C CA    . ARG B 1 363 ? 32.753  101.764 58.996 1.00 21.69 ? 363  ARG B CA    1 
ATOM   6911 C C     . ARG B 1 363 ? 32.093  102.811 58.098 1.00 22.51 ? 363  ARG B C     1 
ATOM   6912 O O     . ARG B 1 363 ? 30.968  102.548 57.641 1.00 20.72 ? 363  ARG B O     1 
ATOM   6913 C CB    . ARG B 1 363 ? 32.317  101.763 60.451 1.00 26.24 ? 363  ARG B CB    1 
ATOM   6914 C CG    . ARG B 1 363 ? 32.883  100.504 61.110 1.00 28.06 ? 363  ARG B CG    1 
ATOM   6915 C CD    . ARG B 1 363 ? 32.032  99.998  62.220 1.00 31.32 ? 363  ARG B CD    1 
ATOM   6916 N NE    . ARG B 1 363 ? 30.714  99.571  61.764 1.00 27.31 ? 363  ARG B NE    1 
ATOM   6917 C CZ    . ARG B 1 363 ? 30.382  98.358  61.304 1.00 27.18 ? 363  ARG B CZ    1 
ATOM   6918 N NH1   . ARG B 1 363 ? 31.253  97.387  61.113 1.00 25.91 ? 363  ARG B NH1   1 
ATOM   6919 N NH2   . ARG B 1 363 ? 29.121  98.140  61.005 1.00 26.22 ? 363  ARG B NH2   1 
ATOM   6920 N N     . ALA B 1 364 ? 32.784  103.906 57.765 1.00 22.16 ? 364  ALA B N     1 
ATOM   6921 C CA    . ALA B 1 364 ? 32.270  104.875 56.785 1.00 20.72 ? 364  ALA B CA    1 
ATOM   6922 C C     . ALA B 1 364 ? 31.991  104.159 55.445 1.00 20.44 ? 364  ALA B C     1 
ATOM   6923 O O     . ALA B 1 364 ? 31.021  104.541 54.759 1.00 23.15 ? 364  ALA B O     1 
ATOM   6924 C CB    . ALA B 1 364 ? 33.258  105.987 56.603 1.00 24.71 ? 364  ALA B CB    1 
ATOM   6925 N N     . GLU B 1 365 ? 32.820  103.201 55.050 1.00 19.36 ? 365  GLU B N     1 
ATOM   6926 C CA    . GLU B 1 365 ? 32.560  102.415 53.802 1.00 21.99 ? 365  GLU B CA    1 
ATOM   6927 C C     . GLU B 1 365 ? 31.365  101.461 54.020 1.00 20.14 ? 365  GLU B C     1 
ATOM   6928 O O     . GLU B 1 365 ? 30.475  101.416 53.184 1.00 19.10 ? 365  GLU B O     1 
ATOM   6929 C CB    . GLU B 1 365 ? 33.848  101.717 53.407 1.00 24.52 ? 365  GLU B CB    1 
ATOM   6930 C CG    . GLU B 1 365 ? 34.905  102.732 52.921 1.00 28.96 ? 365  GLU B CG    1 
ATOM   6931 C CD    . GLU B 1 365 ? 35.835  102.104 51.898 1.00 40.26 ? 365  GLU B CD    1 
ATOM   6932 O OE1   . GLU B 1 365 ? 35.581  102.269 50.675 1.00 51.49 ? 365  GLU B OE1   1 
ATOM   6933 O OE2   . GLU B 1 365 ? 36.743  101.341 52.332 1.00 50.72 ? 365  GLU B OE2   1 
ATOM   6934 N N     . THR B 1 366 ? 31.349  100.753 55.133 1.00 19.84 ? 366  THR B N     1 
ATOM   6935 C CA    . THR B 1 366 ? 30.246  99.816  55.471 1.00 21.54 ? 366  THR B CA    1 
ATOM   6936 C C     . THR B 1 366 ? 28.889  100.531 55.448 1.00 20.57 ? 366  THR B C     1 
ATOM   6937 O O     . THR B 1 366 ? 27.968  99.969  54.881 1.00 18.00 ? 366  THR B O     1 
ATOM   6938 C CB    . THR B 1 366 ? 30.545  99.127  56.789 1.00 21.73 ? 366  THR B CB    1 
ATOM   6939 O OG1   . THR B 1 366 ? 31.891  98.655  56.695 1.00 22.95 ? 366  THR B OG1   1 
ATOM   6940 C CG2   . THR B 1 366 ? 29.602  97.976  57.030 1.00 22.77 ? 366  THR B CG2   1 
ATOM   6941 N N     . MET B 1 367 ? 28.785  101.743 55.997 1.00 19.64 ? 367  MET B N     1 
ATOM   6942 C CA    . MET B 1 367 ? 27.494  102.439 56.158 1.00 19.72 ? 367  MET B CA    1 
ATOM   6943 C C     . MET B 1 367 ? 27.105  103.151 54.852 1.00 20.13 ? 367  MET B C     1 
ATOM   6944 O O     . MET B 1 367 ? 25.983  103.728 54.795 1.00 20.61 ? 367  MET B O     1 
ATOM   6945 C CB    . MET B 1 367 ? 27.600  103.406 57.341 1.00 22.00 ? 367  MET B CB    1 
ATOM   6946 C CG    . MET B 1 367 ? 27.662  102.691 58.662 1.00 20.77 ? 367  MET B CG    1 
ATOM   6947 S SD    . MET B 1 367 ? 27.767  103.780 60.093 1.00 21.94 ? 367  MET B SD    1 
ATOM   6948 C CE    . MET B 1 367 ? 29.226  104.778 59.826 1.00 23.16 ? 367  MET B CE    1 
ATOM   6949 N N     . LYS B 1 368 ? 27.919  103.017 53.793 1.00 19.31 ? 368  LYS B N     1 
ATOM   6950 C CA    . LYS B 1 368 ? 27.440  103.377 52.441 1.00 21.41 ? 368  LYS B CA    1 
ATOM   6951 C C     . LYS B 1 368 ? 27.386  102.136 51.549 1.00 20.36 ? 368  LYS B C     1 
ATOM   6952 O O     . LYS B 1 368 ? 27.247  102.284 50.317 1.00 20.06 ? 368  LYS B O     1 
ATOM   6953 C CB    . LYS B 1 368 ? 28.254  104.512 51.799 1.00 24.86 ? 368  LYS B CB    1 
ATOM   6954 C CG    . LYS B 1 368 ? 29.725  104.268 51.561 1.00 30.22 ? 368  LYS B CG    1 
ATOM   6955 C CD    . LYS B 1 368 ? 30.456  105.502 51.005 1.00 34.62 ? 368  LYS B CD    1 
ATOM   6956 C CE    . LYS B 1 368 ? 29.923  105.931 49.673 1.00 49.46 ? 368  LYS B CE    1 
ATOM   6957 N NZ    . LYS B 1 368 ? 30.980  106.591 48.873 1.00 60.34 ? 368  LYS B NZ    1 
ATOM   6958 N N     . GLY B 1 369 ? 27.378  100.948 52.136 1.00 20.83 ? 369  GLY B N     1 
ATOM   6959 C CA    . GLY B 1 369 ? 27.108  99.723  51.377 1.00 22.41 ? 369  GLY B CA    1 
ATOM   6960 C C     . GLY B 1 369 ? 28.315  99.251  50.554 1.00 22.62 ? 369  GLY B C     1 
ATOM   6961 O O     . GLY B 1 369 ? 28.073  98.599  49.498 1.00 20.40 ? 369  GLY B O     1 
ATOM   6962 N N     . VAL B 1 370 ? 29.541  99.534  50.992 1.00 20.72 ? 370  VAL B N     1 
ATOM   6963 C CA    . VAL B 1 370 ? 30.768  99.058  50.281 1.00 22.52 ? 370  VAL B CA    1 
ATOM   6964 C C     . VAL B 1 370 ? 31.210  97.740  50.899 1.00 21.85 ? 370  VAL B C     1 
ATOM   6965 O O     . VAL B 1 370 ? 31.624  97.700  52.064 1.00 24.36 ? 370  VAL B O     1 
ATOM   6966 C CB    . VAL B 1 370 ? 31.955  100.041 50.285 1.00 24.38 ? 370  VAL B CB    1 
ATOM   6967 C CG1   . VAL B 1 370 ? 33.142  99.438  49.504 1.00 25.83 ? 370  VAL B CG1   1 
ATOM   6968 C CG2   . VAL B 1 370 ? 31.587  101.417 49.732 1.00 24.42 ? 370  VAL B CG2   1 
ATOM   6969 N N     . PRO B 1 371 ? 31.154  96.622  50.151 1.00 20.55 ? 371  PRO B N     1 
ATOM   6970 C CA    . PRO B 1 371 ? 31.545  95.336  50.712 1.00 19.47 ? 371  PRO B CA    1 
ATOM   6971 C C     . PRO B 1 371 ? 33.040  95.285  50.962 1.00 22.01 ? 371  PRO B C     1 
ATOM   6972 O O     . PRO B 1 371 ? 33.788  95.681  50.063 1.00 21.98 ? 371  PRO B O     1 
ATOM   6973 C CB    . PRO B 1 371 ? 31.170  94.308  49.627 1.00 20.52 ? 371  PRO B CB    1 
ATOM   6974 C CG    . PRO B 1 371 ? 31.227  95.099  48.325 1.00 19.75 ? 371  PRO B CG    1 
ATOM   6975 C CD    . PRO B 1 371 ? 30.794  96.509  48.727 1.00 20.88 ? 371  PRO B CD    1 
ATOM   6976 N N     . LYS B 1 372 ? 33.434  94.640  52.047 1.00 24.27 ? 372  LYS B N     1 
ATOM   6977 C CA    . LYS B 1 372 ? 34.853  94.522  52.493 1.00 27.31 ? 372  LYS B CA    1 
ATOM   6978 C C     . LYS B 1 372 ? 34.988  93.239  53.294 1.00 26.05 ? 372  LYS B C     1 
ATOM   6979 O O     . LYS B 1 372 ? 33.946  92.601  53.592 1.00 23.16 ? 372  LYS B O     1 
ATOM   6980 C CB    . LYS B 1 372 ? 35.225  95.760  53.329 1.00 30.48 ? 372  LYS B CB    1 
ATOM   6981 C CG    . LYS B 1 372 ? 35.557  96.972  52.478 1.00 39.57 ? 372  LYS B CG    1 
ATOM   6982 C CD    . LYS B 1 372 ? 35.235  98.288  53.077 1.00 48.13 ? 372  LYS B CD    1 
ATOM   6983 C CE    . LYS B 1 372 ? 35.828  98.497  54.457 1.00 58.64 ? 372  LYS B CE    1 
ATOM   6984 N NZ    . LYS B 1 372 ? 37.178  99.122  54.422 1.00 54.26 ? 372  LYS B NZ    1 
ATOM   6985 N N     . LEU B 1 373 ? 36.215  92.919  53.708 1.00 25.55 ? 373  LEU B N     1 
ATOM   6986 C CA    . LEU B 1 373 ? 36.475  91.758  54.582 1.00 26.64 ? 373  LEU B CA    1 
ATOM   6987 C C     . LEU B 1 373 ? 37.245  92.200  55.836 1.00 27.72 ? 373  LEU B C     1 
ATOM   6988 O O     . LEU B 1 373 ? 37.767  91.309  56.563 1.00 28.68 ? 373  LEU B O     1 
ATOM   6989 C CB    . LEU B 1 373 ? 37.270  90.723  53.782 1.00 28.48 ? 373  LEU B CB    1 
ATOM   6990 C CG    . LEU B 1 373 ? 36.535  90.099  52.597 1.00 30.03 ? 373  LEU B CG    1 
ATOM   6991 C CD1   . LEU B 1 373 ? 37.480  89.232  51.770 1.00 32.13 ? 373  LEU B CD1   1 
ATOM   6992 C CD2   . LEU B 1 373 ? 35.360  89.278  53.091 1.00 30.09 ? 373  LEU B CD2   1 
ATOM   6993 N N     . THR B 1 374 ? 37.346  93.499  56.079 1.00 25.18 ? 374  THR B N     1 
ATOM   6994 C CA    . THR B 1 374 ? 38.166  94.062  57.191 1.00 28.55 ? 374  THR B CA    1 
ATOM   6995 C C     . THR B 1 374 ? 37.758  93.474  58.548 1.00 29.64 ? 374  THR B C     1 
ATOM   6996 O O     . THR B 1 374 ? 38.641  93.182  59.385 1.00 28.95 ? 374  THR B O     1 
ATOM   6997 C CB    . THR B 1 374 ? 37.982  95.574  57.288 1.00 30.69 ? 374  THR B CB    1 
ATOM   6998 O OG1   . THR B 1 374 ? 38.122  96.075  55.962 1.00 33.90 ? 374  THR B OG1   1 
ATOM   6999 C CG2   . THR B 1 374 ? 39.004  96.241  58.189 1.00 33.01 ? 374  THR B CG2   1 
ATOM   7000 N N     . GLU B 1 375 ? 36.467  93.270  58.777 1.00 29.52 ? 375  GLU B N     1 
ATOM   7001 C CA    . GLU B 1 375 ? 35.965  92.721  60.081 1.00 30.89 ? 375  GLU B CA    1 
ATOM   7002 C C     . GLU B 1 375 ? 36.634  91.391  60.469 1.00 28.20 ? 375  GLU B C     1 
ATOM   7003 O O     . GLU B 1 375 ? 36.746  91.063  61.683 1.00 25.62 ? 375  GLU B O     1 
ATOM   7004 C CB    . GLU B 1 375 ? 34.447  92.572  59.954 1.00 34.29 ? 375  GLU B CB    1 
ATOM   7005 C CG    . GLU B 1 375 ? 33.735  92.637  61.274 1.00 35.24 ? 375  GLU B CG    1 
ATOM   7006 C CD    . GLU B 1 375 ? 33.762  93.995  61.956 1.00 36.09 ? 375  GLU B CD    1 
ATOM   7007 O OE1   . GLU B 1 375 ? 34.054  95.017  61.281 1.00 37.79 ? 375  GLU B OE1   1 
ATOM   7008 O OE2   . GLU B 1 375 ? 33.540  93.997  63.191 1.00 32.88 ? 375  GLU B OE2   1 
ATOM   7009 N N     . PHE B 1 376 ? 37.050  90.570  59.506 1.00 26.50 ? 376  PHE B N     1 
ATOM   7010 C CA    . PHE B 1 376 ? 37.744  89.292  59.794 1.00 29.72 ? 376  PHE B CA    1 
ATOM   7011 C C     . PHE B 1 376 ? 38.941  89.501  60.738 1.00 28.78 ? 376  PHE B C     1 
ATOM   7012 O O     . PHE B 1 376 ? 39.318  88.553  61.431 1.00 27.83 ? 376  PHE B O     1 
ATOM   7013 C CB    . PHE B 1 376 ? 38.257  88.682  58.492 1.00 36.73 ? 376  PHE B CB    1 
ATOM   7014 C CG    . PHE B 1 376 ? 38.104  87.195  58.399 1.00 44.51 ? 376  PHE B CG    1 
ATOM   7015 C CD1   . PHE B 1 376 ? 36.834  86.625  58.399 1.00 47.28 ? 376  PHE B CD1   1 
ATOM   7016 C CD2   . PHE B 1 376 ? 39.235  86.376  58.313 1.00 59.89 ? 376  PHE B CD2   1 
ATOM   7017 C CE1   . PHE B 1 376 ? 36.701  85.248  58.326 1.00 58.64 ? 376  PHE B CE1   1 
ATOM   7018 C CE2   . PHE B 1 376 ? 39.103  84.996  58.234 1.00 58.18 ? 376  PHE B CE2   1 
ATOM   7019 C CZ    . PHE B 1 376 ? 37.834  84.439  58.228 1.00 63.67 ? 376  PHE B CZ    1 
ATOM   7020 N N     . ASN B 1 377 ? 39.500  90.710  60.782 1.00 26.80 ? 377  ASN B N     1 
ATOM   7021 C CA    . ASN B 1 377 ? 40.690  91.054  61.592 1.00 27.17 ? 377  ASN B CA    1 
ATOM   7022 C C     . ASN B 1 377 ? 40.472  90.786  63.081 1.00 27.36 ? 377  ASN B C     1 
ATOM   7023 O O     . ASN B 1 377 ? 41.495  90.475  63.746 1.00 27.22 ? 377  ASN B O     1 
ATOM   7024 C CB    . ASN B 1 377 ? 41.071  92.523  61.470 1.00 29.01 ? 377  ASN B CB    1 
ATOM   7025 C CG    . ASN B 1 377 ? 41.606  92.872  60.096 1.00 32.72 ? 377  ASN B CG    1 
ATOM   7026 O OD1   . ASN B 1 377 ? 41.849  92.012  59.267 1.00 35.43 ? 377  ASN B OD1   1 
ATOM   7027 N ND2   . ASN B 1 377 ? 41.679  94.157  59.816 1.00 37.55 ? 377  ASN B ND2   1 
ATOM   7028 N N     . PHE B 1 378 ? 39.247  90.937  63.601 1.00 25.25 ? 378  PHE B N     1 
ATOM   7029 C CA    . PHE B 1 378 ? 39.016  90.713  65.060 1.00 25.07 ? 378  PHE B CA    1 
ATOM   7030 C C     . PHE B 1 378 ? 39.303  89.256  65.431 1.00 24.60 ? 378  PHE B C     1 
ATOM   7031 O O     . PHE B 1 378 ? 39.576  88.968  66.609 1.00 24.81 ? 378  PHE B O     1 
ATOM   7032 C CB    . PHE B 1 378 ? 37.664  91.228  65.552 1.00 23.56 ? 378  PHE B CB    1 
ATOM   7033 C CG    . PHE B 1 378 ? 36.433  90.406  65.243 1.00 25.39 ? 378  PHE B CG    1 
ATOM   7034 C CD1   . PHE B 1 378 ? 36.269  89.120  65.725 1.00 27.71 ? 378  PHE B CD1   1 
ATOM   7035 C CD2   . PHE B 1 378 ? 35.382  90.977  64.530 1.00 27.12 ? 378  PHE B CD2   1 
ATOM   7036 C CE1   . PHE B 1 378 ? 35.114  88.404  65.467 1.00 29.48 ? 378  PHE B CE1   1 
ATOM   7037 C CE2   . PHE B 1 378 ? 34.211  90.271  64.295 1.00 27.66 ? 378  PHE B CE2   1 
ATOM   7038 C CZ    . PHE B 1 378 ? 34.091  88.976  64.753 1.00 30.52 ? 378  PHE B CZ    1 
ATOM   7039 N N     . LEU B 1 379 ? 39.375  88.360  64.463 1.00 25.03 ? 379  LEU B N     1 
ATOM   7040 C CA    . LEU B 1 379 ? 39.694  86.943  64.752 1.00 24.54 ? 379  LEU B CA    1 
ATOM   7041 C C     . LEU B 1 379 ? 41.174  86.760  65.145 1.00 25.75 ? 379  LEU B C     1 
ATOM   7042 O O     . LEU B 1 379 ? 41.520  85.715  65.750 1.00 25.17 ? 379  LEU B O     1 
ATOM   7043 C CB    . LEU B 1 379 ? 39.321  86.123  63.532 1.00 25.61 ? 379  LEU B CB    1 
ATOM   7044 C CG    . LEU B 1 379 ? 37.826  85.988  63.266 1.00 26.19 ? 379  LEU B CG    1 
ATOM   7045 C CD1   . LEU B 1 379 ? 37.615  85.117  62.041 1.00 27.17 ? 379  LEU B CD1   1 
ATOM   7046 C CD2   . LEU B 1 379 ? 37.121  85.384  64.485 1.00 24.49 ? 379  LEU B CD2   1 
ATOM   7047 N N     . ASN B 1 380 ? 42.011  87.748  64.876 1.00 24.31 ? 380  ASN B N     1 
ATOM   7048 C CA    . ASN B 1 380 ? 43.440  87.726  65.254 1.00 25.73 ? 380  ASN B CA    1 
ATOM   7049 C C     . ASN B 1 380 ? 43.688  88.300  66.644 1.00 25.98 ? 380  ASN B C     1 
ATOM   7050 O O     . ASN B 1 380 ? 44.840  88.353  67.039 1.00 27.24 ? 380  ASN B O     1 
ATOM   7051 C CB    . ASN B 1 380 ? 44.255  88.524  64.239 1.00 30.36 ? 380  ASN B CB    1 
ATOM   7052 C CG    . ASN B 1 380 ? 44.366  87.757  62.940 1.00 35.91 ? 380  ASN B CG    1 
ATOM   7053 O OD1   . ASN B 1 380 ? 44.334  86.527  62.921 1.00 45.97 ? 380  ASN B OD1   1 
ATOM   7054 N ND2   . ASN B 1 380 ? 44.456  88.477  61.846 1.00 42.00 ? 380  ASN B ND2   1 
ATOM   7055 N N     . TRP B 1 381 ? 42.655  88.677  67.385 1.00 25.00 ? 381  TRP B N     1 
ATOM   7056 C CA    . TRP B 1 381 ? 42.820  89.404  68.663 1.00 24.54 ? 381  TRP B CA    1 
ATOM   7057 C C     . TRP B 1 381 ? 43.791  88.642  69.568 1.00 23.38 ? 381  TRP B C     1 
ATOM   7058 O O     . TRP B 1 381 ? 44.602  89.307  70.197 1.00 28.80 ? 381  TRP B O     1 
ATOM   7059 C CB    . TRP B 1 381 ? 41.470  89.603  69.353 1.00 22.30 ? 381  TRP B CB    1 
ATOM   7060 C CG    . TRP B 1 381 ? 41.579  90.209  70.708 1.00 22.68 ? 381  TRP B CG    1 
ATOM   7061 C CD1   . TRP B 1 381 ? 41.282  89.620  71.898 1.00 24.17 ? 381  TRP B CD1   1 
ATOM   7062 C CD2   . TRP B 1 381 ? 42.048  91.520  71.015 1.00 23.09 ? 381  TRP B CD2   1 
ATOM   7063 N NE1   . TRP B 1 381 ? 41.479  90.503  72.926 1.00 24.65 ? 381  TRP B NE1   1 
ATOM   7064 C CE2   . TRP B 1 381 ? 41.987  91.659  72.420 1.00 22.14 ? 381  TRP B CE2   1 
ATOM   7065 C CE3   . TRP B 1 381 ? 42.514  92.592  70.248 1.00 26.40 ? 381  TRP B CE3   1 
ATOM   7066 C CZ2   . TRP B 1 381 ? 42.370  92.831  73.071 1.00 25.92 ? 381  TRP B CZ2   1 
ATOM   7067 C CZ3   . TRP B 1 381 ? 42.889  93.753  70.900 1.00 26.03 ? 381  TRP B CZ3   1 
ATOM   7068 C CH2   . TRP B 1 381 ? 42.819  93.867  72.285 1.00 25.21 ? 381  TRP B CH2   1 
ATOM   7069 N N     . ASP B 1 382 ? 43.615  87.334  69.706 1.00 23.92 ? 382  ASP B N     1 
ATOM   7070 C CA    . ASP B 1 382 ? 44.359  86.461  70.645 1.00 28.90 ? 382  ASP B CA    1 
ATOM   7071 C C     . ASP B 1 382 ? 45.272  85.502  69.857 1.00 27.38 ? 382  ASP B C     1 
ATOM   7072 O O     . ASP B 1 382 ? 45.532  84.424  70.351 1.00 30.30 ? 382  ASP B O     1 
ATOM   7073 C CB    . ASP B 1 382 ? 43.396  85.700  71.560 1.00 36.96 ? 382  ASP B CB    1 
ATOM   7074 C CG    . ASP B 1 382 ? 44.055  85.161  72.817 1.00 47.25 ? 382  ASP B CG    1 
ATOM   7075 O OD1   . ASP B 1 382 ? 45.127  85.689  73.195 1.00 53.34 ? 382  ASP B OD1   1 
ATOM   7076 O OD2   . ASP B 1 382 ? 43.517  84.199  73.380 1.00 49.03 ? 382  ASP B OD2   1 
ATOM   7077 N N     . GLY B 1 383 ? 45.717  85.869  68.665 1.00 28.43 ? 383  GLY B N     1 
ATOM   7078 C CA    . GLY B 1 383 ? 46.675  85.049  67.906 1.00 33.25 ? 383  GLY B CA    1 
ATOM   7079 C C     . GLY B 1 383 ? 46.050  84.312  66.724 1.00 33.66 ? 383  GLY B C     1 
ATOM   7080 O O     . GLY B 1 383 ? 46.799  83.736  65.942 1.00 32.78 ? 383  GLY B O     1 
ATOM   7081 N N     . GLY B 1 384 ? 44.730  84.305  66.563 1.00 29.17 ? 384  GLY B N     1 
ATOM   7082 C CA    . GLY B 1 384 ? 44.101  83.590  65.437 1.00 29.07 ? 384  GLY B CA    1 
ATOM   7083 C C     . GLY B 1 384 ? 43.149  82.530  65.924 1.00 29.26 ? 384  GLY B C     1 
ATOM   7084 O O     . GLY B 1 384 ? 43.572  81.552  66.572 1.00 32.61 ? 384  GLY B O     1 
ATOM   7085 N N     . GLY B 1 385 ? 41.862  82.766  65.710 1.00 27.57 ? 385  GLY B N     1 
ATOM   7086 C CA    . GLY B 1 385 ? 40.827  81.840  66.179 1.00 27.90 ? 385  GLY B CA    1 
ATOM   7087 C C     . GLY B 1 385 ? 39.606  81.842  65.292 1.00 27.37 ? 385  GLY B C     1 
ATOM   7088 O O     . GLY B 1 385 ? 39.558  82.572  64.266 1.00 25.48 ? 385  GLY B O     1 
ATOM   7089 N N     . GLY B 1 386 ? 38.629  81.096  65.757 1.00 24.24 ? 386  GLY B N     1 
ATOM   7090 C CA    . GLY B 1 386 ? 37.265  81.164  65.223 1.00 25.25 ? 386  GLY B CA    1 
ATOM   7091 C C     . GLY B 1 386 ? 36.406  82.064  66.075 1.00 24.91 ? 386  GLY B C     1 
ATOM   7092 O O     . GLY B 1 386 ? 36.878  82.626  67.071 1.00 22.77 ? 386  GLY B O     1 
ATOM   7093 N N     . HIS B 1 387 ? 35.141  82.198  65.689 1.00 24.08 ? 387  HIS B N     1 
ATOM   7094 C CA    . HIS B 1 387 ? 34.151  82.839  66.568 1.00 24.62 ? 387  HIS B CA    1 
ATOM   7095 C C     . HIS B 1 387 ? 32.788  82.155  66.448 1.00 23.42 ? 387  HIS B C     1 
ATOM   7096 O O     . HIS B 1 387 ? 32.552  81.348  65.548 1.00 23.47 ? 387  HIS B O     1 
ATOM   7097 C CB    . HIS B 1 387 ? 34.066  84.345  66.336 1.00 20.88 ? 387  HIS B CB    1 
ATOM   7098 C CG    . HIS B 1 387 ? 33.334  84.803  65.124 1.00 21.29 ? 387  HIS B CG    1 
ATOM   7099 N ND1   . HIS B 1 387 ? 32.310  85.720  65.231 1.00 19.47 ? 387  HIS B ND1   1 
ATOM   7100 C CD2   . HIS B 1 387 ? 33.555  84.652  63.795 1.00 21.02 ? 387  HIS B CD2   1 
ATOM   7101 C CE1   . HIS B 1 387 ? 31.898  86.068  64.032 1.00 20.07 ? 387  HIS B CE1   1 
ATOM   7102 N NE2   . HIS B 1 387 ? 32.636  85.450  63.116 1.00 21.45 ? 387  HIS B NE2   1 
ATOM   7103 N N     . VAL B 1 388 ? 31.976  82.419  67.445 1.00 22.96 ? 388  VAL B N     1 
ATOM   7104 C CA    . VAL B 1 388 ? 30.545  82.033  67.433 1.00 22.64 ? 388  VAL B CA    1 
ATOM   7105 C C     . VAL B 1 388 ? 29.781  83.276  67.887 1.00 22.05 ? 388  VAL B C     1 
ATOM   7106 O O     . VAL B 1 388 ? 30.334  84.070  68.714 1.00 23.17 ? 388  VAL B O     1 
ATOM   7107 C CB    . VAL B 1 388 ? 30.284  80.809  68.326 1.00 21.90 ? 388  VAL B CB    1 
ATOM   7108 C CG1   . VAL B 1 388 ? 30.591  81.155  69.766 1.00 22.71 ? 388  VAL B CG1   1 
ATOM   7109 C CG2   . VAL B 1 388 ? 28.861  80.276  68.155 1.00 24.07 ? 388  VAL B CG2   1 
ATOM   7110 N N     . GLY B 1 389 ? 28.574  83.452  67.346 1.00 22.52 ? 389  GLY B N     1 
ATOM   7111 C CA    . GLY B 1 389 ? 27.722  84.589  67.726 1.00 23.28 ? 389  GLY B CA    1 
ATOM   7112 C C     . GLY B 1 389 ? 26.639  84.190  68.720 1.00 23.92 ? 389  GLY B C     1 
ATOM   7113 O O     . GLY B 1 389 ? 25.816  83.339  68.421 1.00 26.00 ? 389  GLY B O     1 
ATOM   7114 N N     . PHE B 1 390 ? 26.643  84.820  69.866 1.00 23.91 ? 390  PHE B N     1 
ATOM   7115 C CA    . PHE B 1 390 ? 25.545  84.757  70.847 1.00 25.59 ? 390  PHE B CA    1 
ATOM   7116 C C     . PHE B 1 390 ? 24.752  86.032  70.656 1.00 21.30 ? 390  PHE B C     1 
ATOM   7117 O O     . PHE B 1 390 ? 25.288  87.107  70.950 1.00 22.93 ? 390  PHE B O     1 
ATOM   7118 C CB    . PHE B 1 390 ? 26.076  84.639  72.276 1.00 25.10 ? 390  PHE B CB    1 
ATOM   7119 C CG    . PHE B 1 390 ? 24.969  84.642  73.285 1.00 24.41 ? 390  PHE B CG    1 
ATOM   7120 C CD1   . PHE B 1 390 ? 24.020  83.626  73.258 1.00 26.36 ? 390  PHE B CD1   1 
ATOM   7121 C CD2   . PHE B 1 390 ? 24.821  85.679  74.186 1.00 21.02 ? 390  PHE B CD2   1 
ATOM   7122 C CE1   . PHE B 1 390 ? 22.933  83.660  74.120 1.00 25.75 ? 390  PHE B CE1   1 
ATOM   7123 C CE2   . PHE B 1 390 ? 23.740  85.704  75.052 1.00 22.01 ? 390  PHE B CE2   1 
ATOM   7124 C CZ    . PHE B 1 390 ? 22.811  84.684  75.038 1.00 24.70 ? 390  PHE B CZ    1 
ATOM   7125 N N     . SER B 1 391 ? 23.505  85.933  70.161 1.00 22.59 ? 391  SER B N     1 
ATOM   7126 C CA    . SER B 1 391 ? 22.793  87.083  69.555 1.00 21.69 ? 391  SER B CA    1 
ATOM   7127 C C     . SER B 1 391 ? 21.382  87.281  70.117 1.00 23.85 ? 391  SER B C     1 
ATOM   7128 O O     . SER B 1 391 ? 20.380  87.098  69.380 1.00 23.96 ? 391  SER B O     1 
ATOM   7129 C CB    . SER B 1 391 ? 22.758  86.899  68.027 1.00 26.06 ? 391  SER B CB    1 
ATOM   7130 O OG    . SER B 1 391 ? 23.939  86.249  67.503 1.00 24.77 ? 391  SER B OG    1 
ATOM   7131 N N     . PRO B 1 392 ? 21.245  87.577  71.432 1.00 24.28 ? 392  PRO B N     1 
ATOM   7132 C CA    . PRO B 1 392 ? 19.968  87.937  72.023 1.00 21.60 ? 392  PRO B CA    1 
ATOM   7133 C C     . PRO B 1 392 ? 19.460  89.266  71.512 1.00 24.68 ? 392  PRO B C     1 
ATOM   7134 O O     . PRO B 1 392 ? 20.260  90.065  71.021 1.00 27.29 ? 392  PRO B O     1 
ATOM   7135 C CB    . PRO B 1 392 ? 20.264  88.066  73.527 1.00 21.59 ? 392  PRO B CB    1 
ATOM   7136 C CG    . PRO B 1 392 ? 21.716  88.443  73.531 1.00 23.70 ? 392  PRO B CG    1 
ATOM   7137 C CD    . PRO B 1 392 ? 22.315  87.558  72.463 1.00 24.91 ? 392  PRO B CD    1 
ATOM   7138 N N     . VAL B 1 393 ? 18.155  89.420  71.616 1.00 20.45 ? 393  VAL B N     1 
ATOM   7139 C CA    . VAL B 1 393 ? 17.400  90.653  71.311 1.00 23.42 ? 393  VAL B CA    1 
ATOM   7140 C C     . VAL B 1 393 ? 17.116  91.400  72.605 1.00 25.88 ? 393  VAL B C     1 
ATOM   7141 O O     . VAL B 1 393 ? 16.748  90.739  73.631 1.00 24.09 ? 393  VAL B O     1 
ATOM   7142 C CB    . VAL B 1 393 ? 16.085  90.304  70.601 1.00 25.94 ? 393  VAL B CB    1 
ATOM   7143 C CG1   . VAL B 1 393 ? 15.234  91.537  70.358 1.00 25.68 ? 393  VAL B CG1   1 
ATOM   7144 C CG2   . VAL B 1 393 ? 16.359  89.524  69.311 1.00 26.64 ? 393  VAL B CG2   1 
ATOM   7145 N N     . SER B 1 394 ? 17.257  92.721  72.556 1.00 25.24 ? 394  SER B N     1 
ATOM   7146 C CA    . SER B 1 394 ? 16.940  93.621  73.691 1.00 28.07 ? 394  SER B CA    1 
ATOM   7147 C C     . SER B 1 394 ? 15.963  94.701  73.234 1.00 26.39 ? 394  SER B C     1 
ATOM   7148 O O     . SER B 1 394 ? 16.051  95.195  72.104 1.00 28.54 ? 394  SER B O     1 
ATOM   7149 C CB    . SER B 1 394 ? 18.249  94.202  74.210 1.00 25.56 ? 394  SER B CB    1 
ATOM   7150 O OG    . SER B 1 394 ? 18.040  95.142  75.248 1.00 22.92 ? 394  SER B OG    1 
ATOM   7151 N N     . PRO B 1 395 ? 15.084  95.197  74.113 1.00 19.96 ? 395  PRO B N     1 
ATOM   7152 C CA    . PRO B 1 395 ? 14.465  96.474  73.865 1.00 21.72 ? 395  PRO B CA    1 
ATOM   7153 C C     . PRO B 1 395 ? 15.575  97.563  73.789 1.00 25.05 ? 395  PRO B C     1 
ATOM   7154 O O     . PRO B 1 395 ? 16.726  97.324  74.309 1.00 22.74 ? 395  PRO B O     1 
ATOM   7155 C CB    . PRO B 1 395 ? 13.638  96.736  75.119 1.00 20.40 ? 395  PRO B CB    1 
ATOM   7156 C CG    . PRO B 1 395 ? 13.570  95.441  75.846 1.00 20.42 ? 395  PRO B CG    1 
ATOM   7157 C CD    . PRO B 1 395 ? 14.779  94.635  75.430 1.00 23.46 ? 395  PRO B CD    1 
ATOM   7158 N N     . ILE B 1 396 ? 15.243  98.722  73.215 1.00 24.57 ? 396  ILE B N     1 
ATOM   7159 C CA    . ILE B 1 396 ? 16.115  99.941  73.255 1.00 22.86 ? 396  ILE B CA    1 
ATOM   7160 C C     . ILE B 1 396 ? 15.871  100.646 74.585 1.00 23.14 ? 396  ILE B C     1 
ATOM   7161 O O     . ILE B 1 396 ? 15.265  101.738 74.634 1.00 21.82 ? 396  ILE B O     1 
ATOM   7162 C CB    . ILE B 1 396 ? 15.940  100.865 72.051 1.00 22.01 ? 396  ILE B CB    1 
ATOM   7163 C CG1   . ILE B 1 396 ? 15.928  100.099 70.738 1.00 22.39 ? 396  ILE B CG1   1 
ATOM   7164 C CG2   . ILE B 1 396 ? 17.092  101.880 72.087 1.00 23.22 ? 396  ILE B CG2   1 
ATOM   7165 C CD1   . ILE B 1 396 ? 15.579  100.970 69.533 1.00 24.84 ? 396  ILE B CD1   1 
ATOM   7166 N N     . THR B 1 397 ? 16.322  100.005 75.654 1.00 22.09 ? 397  THR B N     1 
ATOM   7167 C CA    . THR B 1 397 ? 16.167  100.511 77.023 1.00 23.10 ? 397  THR B CA    1 
ATOM   7168 C C     . THR B 1 397 ? 17.517  100.340 77.728 1.00 24.56 ? 397  THR B C     1 
ATOM   7169 O O     . THR B 1 397 ? 18.095  99.220  77.633 1.00 25.34 ? 397  THR B O     1 
ATOM   7170 C CB    . THR B 1 397 ? 15.066  99.698  77.735 1.00 30.66 ? 397  THR B CB    1 
ATOM   7171 O OG1   . THR B 1 397 ? 13.806  99.820  77.039 1.00 27.92 ? 397  THR B OG1   1 
ATOM   7172 C CG2   . THR B 1 397 ? 14.916  100.134 79.164 1.00 27.99 ? 397  THR B CG2   1 
ATOM   7173 N N     . GLY B 1 398 ? 17.959  101.346 78.473 1.00 22.52 ? 398  GLY B N     1 
ATOM   7174 C CA    . GLY B 1 398 ? 19.249  101.302 79.176 1.00 25.89 ? 398  GLY B CA    1 
ATOM   7175 C C     . GLY B 1 398 ? 19.283  100.149 80.170 1.00 27.08 ? 398  GLY B C     1 
ATOM   7176 O O     . GLY B 1 398 ? 20.262  99.431  80.224 1.00 23.75 ? 398  GLY B O     1 
ATOM   7177 N N     . LYS B 1 399 ? 18.216  99.966  80.942 1.00 28.30 ? 399  LYS B N     1 
ATOM   7178 C CA    . LYS B 1 399 ? 18.153  98.874  81.937 1.00 26.05 ? 399  LYS B CA    1 
ATOM   7179 C C     . LYS B 1 399 ? 18.476  97.527  81.301 1.00 23.61 ? 399  LYS B C     1 
ATOM   7180 O O     . LYS B 1 399 ? 19.288  96.770  81.880 1.00 23.65 ? 399  LYS B O     1 
ATOM   7181 C CB    . LYS B 1 399 ? 16.756  98.809  82.548 1.00 31.87 ? 399  LYS B CB    1 
ATOM   7182 C CG    . LYS B 1 399 ? 16.608  97.748  83.612 1.00 34.62 ? 399  LYS B CG    1 
ATOM   7183 C CD    . LYS B 1 399 ? 15.283  97.891  84.324 1.00 41.82 ? 399  LYS B CD    1 
ATOM   7184 C CE    . LYS B 1 399 ? 15.020  96.748  85.269 1.00 43.19 ? 399  LYS B CE    1 
ATOM   7185 N NZ    . LYS B 1 399 ? 15.545  97.084  86.606 1.00 46.68 ? 399  LYS B NZ    1 
ATOM   7186 N N     . ASP B 1 400 ? 17.873  97.217  80.159 1.00 21.38 ? 400  ASP B N     1 
ATOM   7187 C CA    . ASP B 1 400 ? 18.089  95.922  79.476 1.00 25.31 ? 400  ASP B CA    1 
ATOM   7188 C C     . ASP B 1 400 ? 19.502  95.854  78.871 1.00 24.60 ? 400  ASP B C     1 
ATOM   7189 O O     . ASP B 1 400 ? 20.127  94.785  78.978 1.00 23.71 ? 400  ASP B O     1 
ATOM   7190 C CB    . ASP B 1 400 ? 16.988  95.705  78.424 1.00 24.47 ? 400  ASP B CB    1 
ATOM   7191 C CG    . ASP B 1 400 ? 15.608  95.654  79.063 1.00 22.35 ? 400  ASP B CG    1 
ATOM   7192 O OD1   . ASP B 1 400 ? 15.293  94.599  79.622 1.00 22.88 ? 400  ASP B OD1   1 
ATOM   7193 O OD2   . ASP B 1 400 ? 14.901  96.662  79.005 1.00 23.10 ? 400  ASP B OD2   1 
ATOM   7194 N N     . ALA B 1 401 ? 19.966  96.913  78.185 1.00 27.16 ? 401  ALA B N     1 
ATOM   7195 C CA    . ALA B 1 401 ? 21.296  96.899  77.513 1.00 28.71 ? 401  ALA B CA    1 
ATOM   7196 C C     . ALA B 1 401 ? 22.403  96.665  78.562 1.00 24.95 ? 401  ALA B C     1 
ATOM   7197 O O     . ALA B 1 401 ? 23.236  95.758  78.402 1.00 27.72 ? 401  ALA B O     1 
ATOM   7198 C CB    . ALA B 1 401 ? 21.511  98.173  76.747 1.00 27.72 ? 401  ALA B CB    1 
ATOM   7199 N N     . ILE B 1 402 ? 22.379  97.398  79.649 1.00 26.50 ? 402  ILE B N     1 
ATOM   7200 C CA    . ILE B 1 402 ? 23.433  97.218  80.690 1.00 28.12 ? 402  ILE B CA    1 
ATOM   7201 C C     . ILE B 1 402 ? 23.245  95.872  81.425 1.00 30.10 ? 402  ILE B C     1 
ATOM   7202 O O     . ILE B 1 402 ? 24.259  95.247  81.779 1.00 27.42 ? 402  ILE B O     1 
ATOM   7203 C CB    . ILE B 1 402 ? 23.513  98.402  81.647 1.00 26.52 ? 402  ILE B CB    1 
ATOM   7204 C CG1   . ILE B 1 402 ? 24.904  98.403  82.280 1.00 31.28 ? 402  ILE B CG1   1 
ATOM   7205 C CG2   . ILE B 1 402 ? 22.382  98.357  82.680 1.00 27.81 ? 402  ILE B CG2   1 
ATOM   7206 C CD1   . ILE B 1 402 ? 25.219  99.648  83.049 1.00 29.59 ? 402  ILE B CD1   1 
ATOM   7207 N N     . LYS B 1 403 ? 22.019  95.389  81.627 1.00 27.53 ? 403  LYS B N     1 
ATOM   7208 C CA    . LYS B 1 403 ? 21.808  94.022  82.173 1.00 28.43 ? 403  LYS B CA    1 
ATOM   7209 C C     . LYS B 1 403 ? 22.465  92.979  81.256 1.00 25.84 ? 403  LYS B C     1 
ATOM   7210 O O     . LYS B 1 403 ? 23.221  92.116  81.755 1.00 25.05 ? 403  LYS B O     1 
ATOM   7211 C CB    . LYS B 1 403 ? 20.314  93.733  82.342 1.00 30.83 ? 403  LYS B CB    1 
ATOM   7212 C CG    . LYS B 1 403 ? 19.955  92.351  82.877 1.00 33.47 ? 403  LYS B CG    1 
ATOM   7213 C CD    . LYS B 1 403 ? 20.626  91.990  84.170 1.00 42.49 ? 403  LYS B CD    1 
ATOM   7214 C CE    . LYS B 1 403 ? 19.951  90.833  84.896 1.00 49.04 ? 403  LYS B CE    1 
ATOM   7215 N NZ    . LYS B 1 403 ? 20.687  90.420  86.109 1.00 50.41 ? 403  LYS B NZ    1 
ATOM   7216 N N     . GLN B 1 404 ? 22.178  93.002  79.963 1.00 23.87 ? 404  GLN B N     1 
ATOM   7217 C CA    . GLN B 1 404 ? 22.740  91.999  79.017 1.00 25.09 ? 404  GLN B CA    1 
ATOM   7218 C C     . GLN B 1 404 ? 24.271  92.137  78.960 1.00 26.77 ? 404  GLN B C     1 
ATOM   7219 O O     . GLN B 1 404 ? 24.959  91.088  78.981 1.00 26.40 ? 404  GLN B O     1 
ATOM   7220 C CB    . GLN B 1 404 ? 22.109  92.093  77.630 1.00 25.51 ? 404  GLN B CB    1 
ATOM   7221 C CG    . GLN B 1 404 ? 20.645  91.691  77.592 1.00 25.03 ? 404  GLN B CG    1 
ATOM   7222 C CD    . GLN B 1 404 ? 20.145  91.453  76.188 1.00 24.02 ? 404  GLN B CD    1 
ATOM   7223 O OE1   . GLN B 1 404 ? 20.896  91.421  75.220 1.00 29.24 ? 404  GLN B OE1   1 
ATOM   7224 N NE2   . GLN B 1 404 ? 18.859  91.193  76.076 1.00 24.61 ? 404  GLN B NE2   1 
ATOM   7225 N N     . TYR B 1 405 ? 24.769  93.369  78.932 1.00 26.44 ? 405  TYR B N     1 
ATOM   7226 C CA    . TYR B 1 405 ? 26.217  93.666  78.937 1.00 26.72 ? 405  TYR B CA    1 
ATOM   7227 C C     . TYR B 1 405 ? 26.848  92.951  80.136 1.00 26.63 ? 405  TYR B C     1 
ATOM   7228 O O     . TYR B 1 405 ? 27.761  92.167  79.945 1.00 23.98 ? 405  TYR B O     1 
ATOM   7229 C CB    . TYR B 1 405 ? 26.495  95.172  78.985 1.00 25.81 ? 405  TYR B CB    1 
ATOM   7230 C CG    . TYR B 1 405 ? 27.943  95.463  79.273 1.00 26.48 ? 405  TYR B CG    1 
ATOM   7231 C CD1   . TYR B 1 405 ? 28.917  94.975  78.416 1.00 26.84 ? 405  TYR B CD1   1 
ATOM   7232 C CD2   . TYR B 1 405 ? 28.351  96.172  80.402 1.00 28.65 ? 405  TYR B CD2   1 
ATOM   7233 C CE1   . TYR B 1 405 ? 30.255  95.189  78.660 1.00 25.64 ? 405  TYR B CE1   1 
ATOM   7234 C CE2   . TYR B 1 405 ? 29.693  96.396  80.656 1.00 29.51 ? 405  TYR B CE2   1 
ATOM   7235 C CZ    . TYR B 1 405 ? 30.642  95.924  79.759 1.00 29.54 ? 405  TYR B CZ    1 
ATOM   7236 O OH    . TYR B 1 405 ? 31.982  96.097  79.913 1.00 29.83 ? 405  TYR B OH    1 
ATOM   7237 N N     . ASN B 1 406 ? 26.339  93.222  81.338 1.00 28.12 ? 406  ASN B N     1 
ATOM   7238 C CA    . ASN B 1 406 ? 26.866  92.642  82.604 1.00 28.00 ? 406  ASN B CA    1 
ATOM   7239 C C     . ASN B 1 406 ? 26.814  91.123  82.558 1.00 30.56 ? 406  ASN B C     1 
ATOM   7240 O O     . ASN B 1 406 ? 27.814  90.506  82.951 1.00 29.23 ? 406  ASN B O     1 
ATOM   7241 C CB    . ASN B 1 406 ? 26.122  93.197  83.814 1.00 29.87 ? 406  ASN B CB    1 
ATOM   7242 C CG    . ASN B 1 406 ? 26.551  94.618  84.092 1.00 30.12 ? 406  ASN B CG    1 
ATOM   7243 O OD1   . ASN B 1 406 ? 27.678  94.986  83.840 1.00 37.73 ? 406  ASN B OD1   1 
ATOM   7244 N ND2   . ASN B 1 406 ? 25.677  95.442  84.617 1.00 34.84 ? 406  ASN B ND2   1 
ATOM   7245 N N     . MET B 1 407 ? 25.679  90.554  82.176 1.00 25.92 ? 407  MET B N     1 
ATOM   7246 C CA    . MET B 1 407 ? 25.446  89.086  82.198 1.00 30.10 ? 407  MET B CA    1 
ATOM   7247 C C     . MET B 1 407 ? 26.394  88.388  81.226 1.00 28.32 ? 407  MET B C     1 
ATOM   7248 O O     . MET B 1 407 ? 26.918  87.319  81.530 1.00 25.32 ? 407  MET B O     1 
ATOM   7249 C CB    . MET B 1 407 ? 24.032  88.752  81.714 1.00 29.55 ? 407  MET B CB    1 
ATOM   7250 C CG    . MET B 1 407 ? 22.940  89.218  82.665 1.00 35.92 ? 407  MET B CG    1 
ATOM   7251 S SD    . MET B 1 407 ? 21.330  88.808  81.929 1.00 35.12 ? 407  MET B SD    1 
ATOM   7252 C CE    . MET B 1 407 ? 21.362  87.024  82.071 1.00 34.51 ? 407  MET B CE    1 
ATOM   7253 N N     . VAL B 1 408 ? 26.486  88.920  80.012 1.00 24.68 ? 408  VAL B N     1 
ATOM   7254 C CA    . VAL B 1 408 ? 27.300  88.311  78.928 1.00 27.26 ? 408  VAL B CA    1 
ATOM   7255 C C     . VAL B 1 408 ? 28.796  88.545  79.201 1.00 25.44 ? 408  VAL B C     1 
ATOM   7256 O O     . VAL B 1 408 ? 29.550  87.529  79.190 1.00 25.73 ? 408  VAL B O     1 
ATOM   7257 C CB    . VAL B 1 408 ? 26.861  88.818  77.547 1.00 26.07 ? 408  VAL B CB    1 
ATOM   7258 C CG1   . VAL B 1 408 ? 27.756  88.234  76.469 1.00 26.49 ? 408  VAL B CG1   1 
ATOM   7259 C CG2   . VAL B 1 408 ? 25.384  88.442  77.270 1.00 25.03 ? 408  VAL B CG2   1 
ATOM   7260 N N     . SER B 1 409 ? 29.227  89.777  79.459 1.00 28.13 ? 409  SER B N     1 
ATOM   7261 C CA    . SER B 1 409 ? 30.685  90.055  79.563 1.00 28.48 ? 409  SER B CA    1 
ATOM   7262 C C     . SER B 1 409 ? 31.222  89.330  80.796 1.00 28.11 ? 409  SER B C     1 
ATOM   7263 O O     . SER B 1 409 ? 32.315  88.800  80.690 1.00 27.75 ? 409  SER B O     1 
ATOM   7264 C CB    . SER B 1 409 ? 31.095  91.512  79.597 1.00 31.03 ? 409  SER B CB    1 
ATOM   7265 O OG    . SER B 1 409 ? 30.577  92.147  80.726 1.00 39.74 ? 409  SER B OG    1 
ATOM   7266 N N     . SER B 1 410 ? 30.512  89.329  81.927 1.00 29.30 ? 410  SER B N     1 
ATOM   7267 C CA    . SER B 1 410 ? 31.009  88.677  83.164 1.00 29.52 ? 410  SER B CA    1 
ATOM   7268 C C     . SER B 1 410 ? 31.248  87.196  82.875 1.00 28.03 ? 410  SER B C     1 
ATOM   7269 O O     . SER B 1 410 ? 32.362  86.700  83.160 1.00 29.70 ? 410  SER B O     1 
ATOM   7270 C CB    . SER B 1 410 ? 30.112  88.944  84.331 1.00 32.62 ? 410  SER B CB    1 
ATOM   7271 O OG    . SER B 1 410 ? 28.902  88.274  84.099 1.00 37.19 ? 410  SER B OG    1 
ATOM   7272 N N     . ARG B 1 411 ? 30.330  86.526  82.178 1.00 26.87 ? 411  ARG B N     1 
ATOM   7273 C CA    . ARG B 1 411 ? 30.485  85.091  81.858 1.00 26.57 ? 411  ARG B CA    1 
ATOM   7274 C C     . ARG B 1 411 ? 31.586  84.849  80.826 1.00 25.57 ? 411  ARG B C     1 
ATOM   7275 O O     . ARG B 1 411 ? 32.322  83.857  80.961 1.00 23.98 ? 411  ARG B O     1 
ATOM   7276 C CB    . ARG B 1 411 ? 29.175  84.478  81.349 1.00 29.09 ? 411  ARG B CB    1 
ATOM   7277 C CG    . ARG B 1 411 ? 28.130  84.313  82.436 1.00 31.78 ? 411  ARG B CG    1 
ATOM   7278 C CD    . ARG B 1 411 ? 28.591  83.278  83.451 1.00 33.87 ? 411  ARG B CD    1 
ATOM   7279 N NE    . ARG B 1 411 ? 27.509  83.057  84.392 1.00 37.46 ? 411  ARG B NE    1 
ATOM   7280 C CZ    . ARG B 1 411 ? 27.634  82.562  85.621 1.00 47.32 ? 411  ARG B CZ    1 
ATOM   7281 N NH1   . ARG B 1 411 ? 28.819  82.274  86.130 1.00 47.41 ? 411  ARG B NH1   1 
ATOM   7282 N NH2   . ARG B 1 411 ? 26.555  82.387  86.357 1.00 44.96 ? 411  ARG B NH2   1 
ATOM   7283 N N     . VAL B 1 412 ? 31.619  85.626  79.753 1.00 24.30 ? 412  VAL B N     1 
ATOM   7284 C CA    . VAL B 1 412 ? 32.626  85.420  78.679 1.00 23.77 ? 412  VAL B CA    1 
ATOM   7285 C C     . VAL B 1 412 ? 34.020  85.553  79.318 1.00 25.05 ? 412  VAL B C     1 
ATOM   7286 O O     . VAL B 1 412 ? 34.879  84.680  79.053 1.00 24.80 ? 412  VAL B O     1 
ATOM   7287 C CB    . VAL B 1 412 ? 32.352  86.383  77.519 1.00 29.30 ? 412  VAL B CB    1 
ATOM   7288 C CG1   . VAL B 1 412 ? 33.494  86.462  76.533 1.00 30.85 ? 412  VAL B CG1   1 
ATOM   7289 C CG2   . VAL B 1 412 ? 31.071  86.004  76.782 1.00 29.87 ? 412  VAL B CG2   1 
ATOM   7290 N N     . ARG B 1 413 ? 34.218  86.571  80.146 1.00 24.37 ? 413  ARG B N     1 
ATOM   7291 C CA    . ARG B 1 413 ? 35.506  86.880  80.810 1.00 28.86 ? 413  ARG B CA    1 
ATOM   7292 C C     . ARG B 1 413 ? 35.828  85.800  81.842 1.00 29.62 ? 413  ARG B C     1 
ATOM   7293 O O     . ARG B 1 413 ? 36.985  85.354  81.895 1.00 31.19 ? 413  ARG B O     1 
ATOM   7294 C CB    . ARG B 1 413 ? 35.440  88.286  81.412 1.00 27.17 ? 413  ARG B CB    1 
ATOM   7295 C CG    . ARG B 1 413 ? 35.542  89.364  80.342 1.00 25.44 ? 413  ARG B CG    1 
ATOM   7296 C CD    . ARG B 1 413 ? 35.302  90.741  80.907 1.00 27.17 ? 413  ARG B CD    1 
ATOM   7297 N NE    . ARG B 1 413 ? 36.245  91.041  81.990 1.00 25.57 ? 413  ARG B NE    1 
ATOM   7298 C CZ    . ARG B 1 413 ? 37.486  91.540  81.815 1.00 31.13 ? 413  ARG B CZ    1 
ATOM   7299 N NH1   . ARG B 1 413 ? 37.944  91.830  80.601 1.00 27.84 ? 413  ARG B NH1   1 
ATOM   7300 N NH2   . ARG B 1 413 ? 38.274  91.743  82.854 1.00 28.66 ? 413  ARG B NH2   1 
ATOM   7301 N N     . GLU B 1 414 ? 34.826  85.327  82.585 1.00 30.63 ? 414  GLU B N     1 
ATOM   7302 C CA    . GLU B 1 414 ? 35.017  84.200  83.540 1.00 28.77 ? 414  GLU B CA    1 
ATOM   7303 C C     . GLU B 1 414 ? 35.569  82.986  82.793 1.00 28.60 ? 414  GLU B C     1 
ATOM   7304 O O     . GLU B 1 414 ? 36.441  82.311  83.351 1.00 27.15 ? 414  GLU B O     1 
ATOM   7305 C CB    . GLU B 1 414 ? 33.724  83.911  84.298 1.00 35.82 ? 414  GLU B CB    1 
ATOM   7306 C CG    . GLU B 1 414 ? 33.760  82.603  85.079 1.00 41.99 ? 414  GLU B CG    1 
ATOM   7307 C CD    . GLU B 1 414 ? 32.417  82.167  85.665 1.00 46.37 ? 414  GLU B CD    1 
ATOM   7308 O OE1   . GLU B 1 414 ? 31.372  82.751  85.276 1.00 36.49 ? 414  GLU B OE1   1 
ATOM   7309 O OE2   . GLU B 1 414 ? 32.425  81.263  86.523 1.00 45.11 ? 414  GLU B OE2   1 
ATOM   7310 N N     . TYR B 1 415 ? 35.132  82.703  81.570 1.00 26.11 ? 415  TYR B N     1 
ATOM   7311 C CA    . TYR B 1 415 ? 35.586  81.522  80.804 1.00 25.90 ? 415  TYR B CA    1 
ATOM   7312 C C     . TYR B 1 415 ? 36.855  81.826  80.008 1.00 25.46 ? 415  TYR B C     1 
ATOM   7313 O O     . TYR B 1 415 ? 37.257  80.981  79.183 1.00 27.65 ? 415  TYR B O     1 
ATOM   7314 C CB    . TYR B 1 415 ? 34.418  80.975  79.961 1.00 28.55 ? 415  TYR B CB    1 
ATOM   7315 C CG    . TYR B 1 415 ? 33.485  80.112  80.778 1.00 26.60 ? 415  TYR B CG    1 
ATOM   7316 C CD1   . TYR B 1 415 ? 32.646  80.654  81.738 1.00 25.32 ? 415  TYR B CD1   1 
ATOM   7317 C CD2   . TYR B 1 415 ? 33.529  78.740  80.634 1.00 31.53 ? 415  TYR B CD2   1 
ATOM   7318 C CE1   . TYR B 1 415 ? 31.858  79.850  82.538 1.00 29.30 ? 415  TYR B CE1   1 
ATOM   7319 C CE2   . TYR B 1 415 ? 32.742  77.916  81.412 1.00 33.20 ? 415  TYR B CE2   1 
ATOM   7320 C CZ    . TYR B 1 415 ? 31.906  78.475  82.359 1.00 31.28 ? 415  TYR B CZ    1 
ATOM   7321 O OH    . TYR B 1 415 ? 31.131  77.642  83.093 1.00 35.17 ? 415  TYR B OH    1 
ATOM   7322 N N     . GLY B 1 416 ? 37.445  83.004  80.196 1.00 31.18 ? 416  GLY B N     1 
ATOM   7323 C CA    . GLY B 1 416 ? 38.793  83.316  79.696 1.00 32.05 ? 416  GLY B CA    1 
ATOM   7324 C C     . GLY B 1 416 ? 38.827  84.085  78.394 1.00 33.85 ? 416  GLY B C     1 
ATOM   7325 O O     . GLY B 1 416 ? 39.953  84.315  77.878 1.00 31.69 ? 416  GLY B O     1 
ATOM   7326 N N     . PHE B 1 417 ? 37.680  84.548  77.901 1.00 27.45 ? 417  PHE B N     1 
ATOM   7327 C CA    . PHE B 1 417 ? 37.592  85.253  76.612 1.00 27.46 ? 417  PHE B CA    1 
ATOM   7328 C C     . PHE B 1 417 ? 37.384  86.740  76.878 1.00 25.91 ? 417  PHE B C     1 
ATOM   7329 O O     . PHE B 1 417 ? 36.816  87.108  77.906 1.00 31.46 ? 417  PHE B O     1 
ATOM   7330 C CB    . PHE B 1 417 ? 36.510  84.664  75.695 1.00 26.97 ? 417  PHE B CB    1 
ATOM   7331 C CG    . PHE B 1 417 ? 36.570  83.170  75.528 1.00 24.78 ? 417  PHE B CG    1 
ATOM   7332 C CD1   . PHE B 1 417 ? 37.577  82.557  74.808 1.00 25.03 ? 417  PHE B CD1   1 
ATOM   7333 C CD2   . PHE B 1 417 ? 35.627  82.365  76.143 1.00 26.64 ? 417  PHE B CD2   1 
ATOM   7334 C CE1   . PHE B 1 417 ? 37.602  81.176  74.645 1.00 27.25 ? 417  PHE B CE1   1 
ATOM   7335 C CE2   . PHE B 1 417 ? 35.660  80.986  75.985 1.00 25.57 ? 417  PHE B CE2   1 
ATOM   7336 C CZ    . PHE B 1 417 ? 36.644  80.391  75.248 1.00 25.29 ? 417  PHE B CZ    1 
ATOM   7337 N N     . ASP B 1 418 ? 37.867  87.576  75.962 1.00 24.09 ? 418  ASP B N     1 
ATOM   7338 C CA    . ASP B 1 418 ? 37.499  89.003  76.020 1.00 23.16 ? 418  ASP B CA    1 
ATOM   7339 C C     . ASP B 1 418 ? 36.043  89.141  75.551 1.00 20.46 ? 418  ASP B C     1 
ATOM   7340 O O     . ASP B 1 418 ? 35.630  88.483  74.525 1.00 23.47 ? 418  ASP B O     1 
ATOM   7341 C CB    . ASP B 1 418 ? 38.475  89.866  75.215 1.00 22.79 ? 418  ASP B CB    1 
ATOM   7342 C CG    . ASP B 1 418 ? 39.702  90.270  76.021 1.00 24.71 ? 418  ASP B CG    1 
ATOM   7343 O OD1   . ASP B 1 418 ? 39.530  90.870  77.070 1.00 24.86 ? 418  ASP B OD1   1 
ATOM   7344 O OD2   . ASP B 1 418 ? 40.810  89.868  75.635 1.00 25.99 ? 418  ASP B OD2   1 
ATOM   7345 N N     . TYR B 1 419 ? 35.362  90.102  76.136 1.00 22.71 ? 419  TYR B N     1 
ATOM   7346 C CA    . TYR B 1 419 ? 34.025  90.531  75.664 1.00 24.46 ? 419  TYR B CA    1 
ATOM   7347 C C     . TYR B 1 419 ? 34.124  91.425  74.412 1.00 24.16 ? 419  TYR B C     1 
ATOM   7348 O O     . TYR B 1 419 ? 34.776  92.484  74.473 1.00 27.31 ? 419  TYR B O     1 
ATOM   7349 C CB    . TYR B 1 419 ? 33.273  91.267  76.770 1.00 25.24 ? 419  TYR B CB    1 
ATOM   7350 C CG    . TYR B 1 419 ? 31.932  91.785  76.290 1.00 25.48 ? 419  TYR B CG    1 
ATOM   7351 C CD1   . TYR B 1 419 ? 30.884  90.921  76.033 1.00 27.31 ? 419  TYR B CD1   1 
ATOM   7352 C CD2   . TYR B 1 419 ? 31.739  93.125  75.987 1.00 29.03 ? 419  TYR B CD2   1 
ATOM   7353 C CE1   . TYR B 1 419 ? 29.657  91.389  75.575 1.00 27.17 ? 419  TYR B CE1   1 
ATOM   7354 C CE2   . TYR B 1 419 ? 30.516  93.624  75.572 1.00 27.31 ? 419  TYR B CE2   1 
ATOM   7355 C CZ    . TYR B 1 419 ? 29.472  92.743  75.336 1.00 30.42 ? 419  TYR B CZ    1 
ATOM   7356 O OH    . TYR B 1 419 ? 28.261  93.195  74.902 1.00 28.48 ? 419  TYR B OH    1 
ATOM   7357 N N     . MET B 1 420 ? 33.445  91.022  73.330 1.00 23.98 ? 420  MET B N     1 
ATOM   7358 C CA    . MET B 1 420 ? 33.375  91.754  72.052 1.00 24.72 ? 420  MET B CA    1 
ATOM   7359 C C     . MET B 1 420 ? 31.892  91.843  71.647 1.00 26.61 ? 420  MET B C     1 
ATOM   7360 O O     . MET B 1 420 ? 31.354  90.848  71.104 1.00 25.89 ? 420  MET B O     1 
ATOM   7361 C CB    . MET B 1 420 ? 34.194  91.055  70.970 1.00 24.79 ? 420  MET B CB    1 
ATOM   7362 C CG    . MET B 1 420 ? 35.687  91.035  71.221 1.00 24.47 ? 420  MET B CG    1 
ATOM   7363 S SD    . MET B 1 420 ? 36.376  90.005  69.922 1.00 31.33 ? 420  MET B SD    1 
ATOM   7364 C CE    . MET B 1 420 ? 38.136  90.147  70.250 1.00 33.19 ? 420  MET B CE    1 
ATOM   7365 N N     . GLY B 1 421 ? 31.244  92.958  71.987 1.00 29.67 ? 421  GLY B N     1 
ATOM   7366 C CA    . GLY B 1 421 ? 29.784  93.141  71.859 1.00 28.74 ? 421  GLY B CA    1 
ATOM   7367 C C     . GLY B 1 421 ? 29.402  94.230  70.872 1.00 29.51 ? 421  GLY B C     1 
ATOM   7368 O O     . GLY B 1 421 ? 30.025  95.292  70.902 1.00 26.53 ? 421  GLY B O     1 
ATOM   7369 N N     . LEU B 1 422 ? 28.440  93.921  69.996 1.00 26.42 ? 422  LEU B N     1 
ATOM   7370 C CA    . LEU B 1 422 ? 27.753  94.854  69.044 1.00 25.19 ? 422  LEU B CA    1 
ATOM   7371 C C     . LEU B 1 422 ? 26.309  95.019  69.540 1.00 25.12 ? 422  LEU B C     1 
ATOM   7372 O O     . LEU B 1 422 ? 25.639  93.970  69.832 1.00 26.46 ? 422  LEU B O     1 
ATOM   7373 C CB    . LEU B 1 422 ? 27.785  94.193  67.653 1.00 26.56 ? 422  LEU B CB    1 
ATOM   7374 C CG    . LEU B 1 422 ? 26.731  94.679  66.657 1.00 27.48 ? 422  LEU B CG    1 
ATOM   7375 C CD1   . LEU B 1 422 ? 27.003  96.117  66.312 1.00 31.31 ? 422  LEU B CD1   1 
ATOM   7376 C CD2   . LEU B 1 422 ? 26.680  93.838  65.381 1.00 29.74 ? 422  LEU B CD2   1 
ATOM   7377 N N     . LEU B 1 423 ? 25.831  96.243  69.690 1.00 25.41 ? 423  LEU B N     1 
ATOM   7378 C CA    . LEU B 1 423 ? 24.378  96.554  69.796 1.00 24.71 ? 423  LEU B CA    1 
ATOM   7379 C C     . LEU B 1 423 ? 23.924  97.145  68.476 1.00 24.40 ? 423  LEU B C     1 
ATOM   7380 O O     . LEU B 1 423 ? 24.319  98.331  68.219 1.00 25.49 ? 423  LEU B O     1 
ATOM   7381 C CB    . LEU B 1 423 ? 24.174  97.553  70.924 1.00 25.76 ? 423  LEU B CB    1 
ATOM   7382 C CG    . LEU B 1 423 ? 24.571  97.003  72.275 1.00 29.05 ? 423  LEU B CG    1 
ATOM   7383 C CD1   . LEU B 1 423 ? 24.525  98.107  73.327 1.00 30.70 ? 423  LEU B CD1   1 
ATOM   7384 C CD2   . LEU B 1 423 ? 23.667  95.835  72.693 1.00 30.64 ? 423  LEU B CD2   1 
ATOM   7385 N N     . ALA B 1 424 ? 23.288  96.331  67.610 1.00 22.10 ? 424  ALA B N     1 
ATOM   7386 C CA    . ALA B 1 424 ? 22.876  96.802  66.264 1.00 26.45 ? 424  ALA B CA    1 
ATOM   7387 C C     . ALA B 1 424 ? 21.479  97.392  66.449 1.00 28.08 ? 424  ALA B C     1 
ATOM   7388 O O     . ALA B 1 424 ? 20.576  96.621  66.913 1.00 26.59 ? 424  ALA B O     1 
ATOM   7389 C CB    . ALA B 1 424 ? 22.890  95.699  65.208 1.00 24.31 ? 424  ALA B CB    1 
ATOM   7390 N N     . ILE B 1 425 ? 21.277  98.652  66.059 1.00 25.33 ? 425  ILE B N     1 
ATOM   7391 C CA    . ILE B 1 425 ? 20.024  99.401  66.368 1.00 24.18 ? 425  ILE B CA    1 
ATOM   7392 C C     . ILE B 1 425 ? 19.026  99.114  65.274 1.00 23.06 ? 425  ILE B C     1 
ATOM   7393 O O     . ILE B 1 425 ? 19.254  99.607  64.121 1.00 23.35 ? 425  ILE B O     1 
ATOM   7394 C CB    . ILE B 1 425 ? 20.266  100.909 66.514 1.00 27.20 ? 425  ILE B CB    1 
ATOM   7395 C CG1   . ILE B 1 425 ? 21.403  101.209 67.516 1.00 26.96 ? 425  ILE B CG1   1 
ATOM   7396 C CG2   . ILE B 1 425 ? 18.974  101.592 66.907 1.00 30.15 ? 425  ILE B CG2   1 
ATOM   7397 C CD1   . ILE B 1 425 ? 21.924  102.663 67.398 1.00 26.67 ? 425  ILE B CD1   1 
ATOM   7398 N N     . GLY B 1 426 ? 17.976  98.335  65.589 1.00 19.99 ? 426  GLY B N     1 
ATOM   7399 C CA    . GLY B 1 426 ? 16.910  98.064  64.608 1.00 22.40 ? 426  GLY B CA    1 
ATOM   7400 C C     . GLY B 1 426 ? 15.801  99.096  64.784 1.00 23.60 ? 426  GLY B C     1 
ATOM   7401 O O     . GLY B 1 426 ? 15.982  100.075 65.504 1.00 27.94 ? 426  GLY B O     1 
ATOM   7402 N N     . TRP B 1 427 ? 14.652  98.854  64.218 1.00 25.97 ? 427  TRP B N     1 
ATOM   7403 C CA    . TRP B 1 427 ? 13.560  99.847  64.199 1.00 25.52 ? 427  TRP B CA    1 
ATOM   7404 C C     . TRP B 1 427 ? 13.149  100.137 65.667 1.00 24.63 ? 427  TRP B C     1 
ATOM   7405 O O     . TRP B 1 427 ? 13.104  101.271 66.087 1.00 30.93 ? 427  TRP B O     1 
ATOM   7406 C CB    . TRP B 1 427 ? 12.418  99.301  63.340 1.00 31.96 ? 427  TRP B CB    1 
ATOM   7407 C CG    . TRP B 1 427 ? 12.668  98.667  61.986 1.00 44.55 ? 427  TRP B CG    1 
ATOM   7408 C CD1   . TRP B 1 427 ? 12.532  97.327  61.678 1.00 52.69 ? 427  TRP B CD1   1 
ATOM   7409 C CD2   . TRP B 1 427 ? 12.913  99.318  60.719 1.00 48.33 ? 427  TRP B CD2   1 
ATOM   7410 N NE1   . TRP B 1 427 ? 12.742  97.091  60.342 1.00 42.63 ? 427  TRP B NE1   1 
ATOM   7411 C CE2   . TRP B 1 427 ? 12.974  98.295  59.725 1.00 52.24 ? 427  TRP B CE2   1 
ATOM   7412 C CE3   . TRP B 1 427 ? 13.152  100.646 60.341 1.00 51.46 ? 427  TRP B CE3   1 
ATOM   7413 C CZ2   . TRP B 1 427 ? 13.221  98.570  58.377 1.00 47.69 ? 427  TRP B CZ2   1 
ATOM   7414 C CZ3   . TRP B 1 427 ? 13.385  100.918 59.012 1.00 59.96 ? 427  TRP B CZ3   1 
ATOM   7415 C CH2   . TRP B 1 427 ? 13.440  99.893  58.054 1.00 64.88 ? 427  TRP B CH2   1 
ATOM   7416 N N     . ARG B 1 428 ? 12.931  99.110  66.468 1.00 20.29 ? 428  ARG B N     1 
ATOM   7417 C CA    . ARG B 1 428 ? 12.427  99.298  67.857 1.00 19.68 ? 428  ARG B CA    1 
ATOM   7418 C C     . ARG B 1 428 ? 13.207  98.408  68.815 1.00 19.33 ? 428  ARG B C     1 
ATOM   7419 O O     . ARG B 1 428 ? 12.814  98.322  70.004 1.00 20.55 ? 428  ARG B O     1 
ATOM   7420 C CB    . ARG B 1 428 ? 10.941  98.963  67.897 1.00 22.18 ? 428  ARG B CB    1 
ATOM   7421 C CG    . ARG B 1 428 ? 10.027  100.170 68.073 1.00 26.25 ? 428  ARG B CG    1 
ATOM   7422 C CD    . ARG B 1 428 ? 9.502   100.708 66.845 1.00 26.65 ? 428  ARG B CD    1 
ATOM   7423 N NE    . ARG B 1 428 ? 8.375   101.638 66.935 1.00 26.26 ? 428  ARG B NE    1 
ATOM   7424 C CZ    . ARG B 1 428 ? 8.032   102.403 65.908 1.00 26.30 ? 428  ARG B CZ    1 
ATOM   7425 N NH1   . ARG B 1 428 ? 8.717   102.283 64.781 1.00 26.37 ? 428  ARG B NH1   1 
ATOM   7426 N NH2   . ARG B 1 428 ? 7.033   103.261 65.965 1.00 20.95 ? 428  ARG B NH2   1 
ATOM   7427 N N     . ASP B 1 429 ? 14.246  97.749  68.335 1.00 19.42 ? 429  ASP B N     1 
ATOM   7428 C CA    . ASP B 1 429 ? 15.025  96.745  69.105 1.00 20.59 ? 429  ASP B CA    1 
ATOM   7429 C C     . ASP B 1 429 ? 16.540  96.962  68.983 1.00 21.01 ? 429  ASP B C     1 
ATOM   7430 O O     . ASP B 1 429 ? 17.033  97.660  68.050 1.00 20.68 ? 429  ASP B O     1 
ATOM   7431 C CB    . ASP B 1 429 ? 14.656  95.347  68.613 1.00 22.40 ? 429  ASP B CB    1 
ATOM   7432 C CG    . ASP B 1 429 ? 15.457  94.911  67.364 1.00 27.73 ? 429  ASP B CG    1 
ATOM   7433 O OD1   . ASP B 1 429 ? 15.099  95.317  66.267 1.00 29.01 ? 429  ASP B OD1   1 
ATOM   7434 O OD2   . ASP B 1 429 ? 16.498  94.236  67.534 1.00 29.37 ? 429  ASP B OD2   1 
ATOM   7435 N N     . LEU B 1 430 ? 17.287  96.353  69.889 1.00 24.11 ? 430  LEU B N     1 
ATOM   7436 C CA    . LEU B 1 430 ? 18.729  96.066  69.685 1.00 26.44 ? 430  LEU B CA    1 
ATOM   7437 C C     . LEU B 1 430 ? 18.940  94.568  69.421 1.00 29.30 ? 430  LEU B C     1 
ATOM   7438 O O     . LEU B 1 430 ? 18.501  93.754  70.243 1.00 26.98 ? 430  LEU B O     1 
ATOM   7439 C CB    . LEU B 1 430 ? 19.518  96.473  70.920 1.00 25.13 ? 430  LEU B CB    1 
ATOM   7440 C CG    . LEU B 1 430 ? 19.324  97.935  71.354 1.00 29.72 ? 430  LEU B CG    1 
ATOM   7441 C CD1   . LEU B 1 430 ? 20.073  98.207  72.640 1.00 25.27 ? 430  LEU B CD1   1 
ATOM   7442 C CD2   . LEU B 1 430 ? 19.768  98.926  70.276 1.00 29.18 ? 430  LEU B CD2   1 
ATOM   7443 N N     . HIS B 1 431 ? 19.640  94.216  68.339 1.00 24.09 ? 431  HIS B N     1 
ATOM   7444 C CA    . HIS B 1 431 ? 20.361  92.915  68.260 1.00 23.32 ? 431  HIS B CA    1 
ATOM   7445 C C     . HIS B 1 431 ? 21.673  93.048  69.034 1.00 24.79 ? 431  HIS B C     1 
ATOM   7446 O O     . HIS B 1 431 ? 22.585  93.833  68.592 1.00 24.92 ? 431  HIS B O     1 
ATOM   7447 C CB    . HIS B 1 431 ? 20.640  92.517  66.793 1.00 26.28 ? 431  HIS B CB    1 
ATOM   7448 C CG    . HIS B 1 431 ? 19.396  92.195  66.049 1.00 27.36 ? 431  HIS B CG    1 
ATOM   7449 N ND1   . HIS B 1 431 ? 19.350  91.288  65.004 1.00 31.64 ? 431  HIS B ND1   1 
ATOM   7450 C CD2   . HIS B 1 431 ? 18.143  92.676  66.206 1.00 27.94 ? 431  HIS B CD2   1 
ATOM   7451 C CE1   . HIS B 1 431 ? 18.122  91.263  64.510 1.00 27.32 ? 431  HIS B CE1   1 
ATOM   7452 N NE2   . HIS B 1 431 ? 17.366  92.101  65.227 1.00 35.78 ? 431  HIS B NE2   1 
ATOM   7453 N N     . HIS B 1 432 ? 21.799  92.319  70.132 1.00 21.70 ? 432  HIS B N     1 
ATOM   7454 C CA    . HIS B 1 432 ? 23.030  92.257  70.951 1.00 25.11 ? 432  HIS B CA    1 
ATOM   7455 C C     . HIS B 1 432 ? 23.847  91.044  70.513 1.00 25.46 ? 432  HIS B C     1 
ATOM   7456 O O     . HIS B 1 432 ? 23.551  89.899  70.930 1.00 25.49 ? 432  HIS B O     1 
ATOM   7457 C CB    . HIS B 1 432 ? 22.676  92.286  72.433 1.00 23.83 ? 432  HIS B CB    1 
ATOM   7458 C CG    . HIS B 1 432 ? 23.851  92.171  73.313 1.00 25.17 ? 432  HIS B CG    1 
ATOM   7459 N ND1   . HIS B 1 432 ? 23.727  91.865  74.674 1.00 25.48 ? 432  HIS B ND1   1 
ATOM   7460 C CD2   . HIS B 1 432 ? 25.165  92.433  73.106 1.00 27.08 ? 432  HIS B CD2   1 
ATOM   7461 C CE1   . HIS B 1 432 ? 24.938  91.851  75.233 1.00 23.44 ? 432  HIS B CE1   1 
ATOM   7462 N NE2   . HIS B 1 432 ? 25.835  92.178  74.304 1.00 23.01 ? 432  HIS B NE2   1 
ATOM   7463 N N     . VAL B 1 433 ? 24.811  91.277  69.641 1.00 24.91 ? 433  VAL B N     1 
ATOM   7464 C CA    . VAL B 1 433 ? 25.600  90.154  69.080 1.00 23.37 ? 433  VAL B CA    1 
ATOM   7465 C C     . VAL B 1 433 ? 26.941  90.164  69.787 1.00 23.74 ? 433  VAL B C     1 
ATOM   7466 O O     . VAL B 1 433 ? 27.687  91.160  69.602 1.00 24.54 ? 433  VAL B O     1 
ATOM   7467 C CB    . VAL B 1 433 ? 25.772  90.227  67.561 1.00 24.80 ? 433  VAL B CB    1 
ATOM   7468 C CG1   . VAL B 1 433 ? 26.598  89.037  67.077 1.00 26.10 ? 433  VAL B CG1   1 
ATOM   7469 C CG2   . VAL B 1 433 ? 24.435  90.328  66.840 1.00 24.82 ? 433  VAL B CG2   1 
ATOM   7470 N N     . THR B 1 434 ? 27.220  89.110  70.567 1.00 23.66 ? 434  THR B N     1 
ATOM   7471 C CA    . THR B 1 434 ? 28.529  88.914  71.227 1.00 25.03 ? 434  THR B CA    1 
ATOM   7472 C C     . THR B 1 434 ? 29.287  87.908  70.382 1.00 25.35 ? 434  THR B C     1 
ATOM   7473 O O     . THR B 1 434 ? 28.749  86.834  70.176 1.00 24.36 ? 434  THR B O     1 
ATOM   7474 C CB    . THR B 1 434 ? 28.376  88.489  72.693 1.00 28.11 ? 434  THR B CB    1 
ATOM   7475 O OG1   . THR B 1 434 ? 27.615  89.518  73.328 1.00 26.79 ? 434  THR B OG1   1 
ATOM   7476 C CG2   . THR B 1 434 ? 29.718  88.295  73.363 1.00 28.56 ? 434  THR B CG2   1 
ATOM   7477 N N     . VAL B 1 435 ? 30.445  88.311  69.842 1.00 23.42 ? 435  VAL B N     1 
ATOM   7478 C CA    . VAL B 1 435 ? 31.289  87.407  69.023 1.00 23.35 ? 435  VAL B CA    1 
ATOM   7479 C C     . VAL B 1 435 ? 32.385  86.922  69.979 1.00 26.66 ? 435  VAL B C     1 
ATOM   7480 O O     . VAL B 1 435 ? 33.060  87.751  70.638 1.00 28.03 ? 435  VAL B O     1 
ATOM   7481 C CB    . VAL B 1 435 ? 31.784  88.095  67.738 1.00 23.35 ? 435  VAL B CB    1 
ATOM   7482 C CG1   . VAL B 1 435 ? 30.607  88.311  66.772 1.00 23.61 ? 435  VAL B CG1   1 
ATOM   7483 C CG2   . VAL B 1 435 ? 32.468  89.413  68.018 1.00 22.56 ? 435  VAL B CG2   1 
ATOM   7484 N N     . ILE B 1 436 ? 32.413  85.612  70.183 1.00 25.37 ? 436  ILE B N     1 
ATOM   7485 C CA    . ILE B 1 436 ? 33.354  85.022  71.157 1.00 24.20 ? 436  ILE B CA    1 
ATOM   7486 C C     . ILE B 1 436 ? 34.453  84.379  70.328 1.00 23.88 ? 436  ILE B C     1 
ATOM   7487 O O     . ILE B 1 436 ? 34.150  83.447  69.555 1.00 21.70 ? 436  ILE B O     1 
ATOM   7488 C CB    . ILE B 1 436 ? 32.640  84.032  72.089 1.00 24.58 ? 436  ILE B CB    1 
ATOM   7489 C CG1   . ILE B 1 436 ? 31.357  84.617  72.681 1.00 25.10 ? 436  ILE B CG1   1 
ATOM   7490 C CG2   . ILE B 1 436 ? 33.638  83.628  73.157 1.00 26.02 ? 436  ILE B CG2   1 
ATOM   7491 C CD1   . ILE B 1 436 ? 30.513  83.614  73.414 1.00 27.36 ? 436  ILE B CD1   1 
ATOM   7492 N N     . VAL B 1 437 ? 35.659  84.949  70.435 1.00 23.35 ? 437  VAL B N     1 
ATOM   7493 C CA    . VAL B 1 437 ? 36.844  84.499  69.682 1.00 21.95 ? 437  VAL B CA    1 
ATOM   7494 C C     . VAL B 1 437 ? 37.568  83.471  70.538 1.00 20.70 ? 437  VAL B C     1 
ATOM   7495 O O     . VAL B 1 437 ? 37.838  83.722  71.732 1.00 22.56 ? 437  VAL B O     1 
ATOM   7496 C CB    . VAL B 1 437 ? 37.736  85.693  69.288 1.00 24.42 ? 437  VAL B CB    1 
ATOM   7497 C CG1   . VAL B 1 437 ? 38.985  85.202  68.587 1.00 25.74 ? 437  VAL B CG1   1 
ATOM   7498 C CG2   . VAL B 1 437 ? 36.971  86.677  68.434 1.00 24.61 ? 437  VAL B CG2   1 
ATOM   7499 N N     . TYR B 1 438 ? 37.890  82.360  69.922 1.00 23.22 ? 438  TYR B N     1 
ATOM   7500 C CA    . TYR B 1 438 ? 38.453  81.195  70.637 1.00 23.30 ? 438  TYR B CA    1 
ATOM   7501 C C     . TYR B 1 438 ? 39.312  80.407  69.659 1.00 24.98 ? 438  TYR B C     1 
ATOM   7502 O O     . TYR B 1 438 ? 39.111  80.408  68.424 1.00 26.16 ? 438  TYR B O     1 
ATOM   7503 C CB    . TYR B 1 438 ? 37.315  80.358  71.249 1.00 24.47 ? 438  TYR B CB    1 
ATOM   7504 C CG    . TYR B 1 438 ? 36.467  79.627  70.235 1.00 24.96 ? 438  TYR B CG    1 
ATOM   7505 C CD1   . TYR B 1 438 ? 35.511  80.307  69.502 1.00 27.21 ? 438  TYR B CD1   1 
ATOM   7506 C CD2   . TYR B 1 438 ? 36.702  78.292  69.919 1.00 25.66 ? 438  TYR B CD2   1 
ATOM   7507 C CE1   . TYR B 1 438 ? 34.769  79.669  68.515 1.00 26.27 ? 438  TYR B CE1   1 
ATOM   7508 C CE2   . TYR B 1 438 ? 35.971  77.640  68.929 1.00 25.65 ? 438  TYR B CE2   1 
ATOM   7509 C CZ    . TYR B 1 438 ? 34.999  78.334  68.231 1.00 27.19 ? 438  TYR B CZ    1 
ATOM   7510 O OH    . TYR B 1 438 ? 34.267  77.752  67.239 1.00 29.41 ? 438  TYR B OH    1 
ATOM   7511 N N     . ASP B 1 439 ? 40.228  79.657  70.232 1.00 26.94 ? 439  ASP B N     1 
ATOM   7512 C CA    . ASP B 1 439 ? 41.092  78.729  69.467 1.00 28.03 ? 439  ASP B CA    1 
ATOM   7513 C C     . ASP B 1 439 ? 40.294  77.473  69.141 1.00 26.41 ? 439  ASP B C     1 
ATOM   7514 O O     . ASP B 1 439 ? 40.313  76.528  69.936 1.00 24.93 ? 439  ASP B O     1 
ATOM   7515 C CB    . ASP B 1 439 ? 42.367  78.397  70.258 1.00 29.61 ? 439  ASP B CB    1 
ATOM   7516 C CG    . ASP B 1 439 ? 43.340  77.521  69.495 1.00 32.27 ? 439  ASP B CG    1 
ATOM   7517 O OD1   . ASP B 1 439 ? 43.055  77.145  68.323 1.00 31.96 ? 439  ASP B OD1   1 
ATOM   7518 O OD2   . ASP B 1 439 ? 44.375  77.233  70.089 1.00 34.92 ? 439  ASP B OD2   1 
ATOM   7519 N N     . LYS B 1 440 ? 39.773  77.420  67.922 1.00 27.44 ? 440  LYS B N     1 
ATOM   7520 C CA    . LYS B 1 440 ? 38.878  76.334  67.434 1.00 27.79 ? 440  LYS B CA    1 
ATOM   7521 C C     . LYS B 1 440 ? 39.663  75.028  67.199 1.00 27.78 ? 440  LYS B C     1 
ATOM   7522 O O     . LYS B 1 440 ? 38.999  73.979  67.007 1.00 32.65 ? 440  LYS B O     1 
ATOM   7523 C CB    . LYS B 1 440 ? 38.220  76.808  66.138 1.00 36.18 ? 440  LYS B CB    1 
ATOM   7524 C CG    . LYS B 1 440 ? 39.157  76.714  64.937 1.00 43.52 ? 440  LYS B CG    1 
ATOM   7525 C CD    . LYS B 1 440 ? 39.198  77.901  64.022 1.00 54.36 ? 440  LYS B CD    1 
ATOM   7526 C CE    . LYS B 1 440 ? 40.471  77.960  63.186 1.00 62.72 ? 440  LYS B CE    1 
ATOM   7527 N NZ    . LYS B 1 440 ? 40.369  78.992  62.124 1.00 62.86 ? 440  LYS B NZ    1 
ATOM   7528 N N     . THR B 1 441 ? 40.998  75.041  67.259 1.00 29.44 ? 441  THR B N     1 
ATOM   7529 C CA    . THR B 1 441 ? 41.856  73.823  67.053 1.00 29.49 ? 441  THR B CA    1 
ATOM   7530 C C     . THR B 1 441 ? 42.092  73.140  68.393 1.00 31.79 ? 441  THR B C     1 
ATOM   7531 O O     . THR B 1 441 ? 42.601  72.035  68.374 1.00 33.47 ? 441  THR B O     1 
ATOM   7532 C CB    . THR B 1 441 ? 43.235  74.122  66.436 1.00 30.58 ? 441  THR B CB    1 
ATOM   7533 O OG1   . THR B 1 441 ? 43.942  74.959  67.350 1.00 29.98 ? 441  THR B OG1   1 
ATOM   7534 C CG2   . THR B 1 441 ? 43.184  74.840  65.102 1.00 32.66 ? 441  THR B CG2   1 
ATOM   7535 N N     . ASP B 1 442 ? 41.748  73.803  69.499 1.00 31.77 ? 442  ASP B N     1 
ATOM   7536 C CA    . ASP B 1 442 ? 42.077  73.359  70.878 1.00 31.44 ? 442  ASP B CA    1 
ATOM   7537 C C     . ASP B 1 442 ? 40.831  72.763  71.516 1.00 30.97 ? 442  ASP B C     1 
ATOM   7538 O O     . ASP B 1 442 ? 39.909  73.489  71.868 1.00 30.56 ? 442  ASP B O     1 
ATOM   7539 C CB    . ASP B 1 442 ? 42.647  74.518  71.702 1.00 31.82 ? 442  ASP B CB    1 
ATOM   7540 C CG    . ASP B 1 442 ? 43.144  74.144  73.092 1.00 35.55 ? 442  ASP B CG    1 
ATOM   7541 O OD1   . ASP B 1 442 ? 42.774  73.084  73.604 1.00 33.80 ? 442  ASP B OD1   1 
ATOM   7542 O OD2   . ASP B 1 442 ? 43.860  74.959  73.661 1.00 40.70 ? 442  ASP B OD2   1 
ATOM   7543 N N     . PRO B 1 443 ? 40.799  71.433  71.734 1.00 34.88 ? 443  PRO B N     1 
ATOM   7544 C CA    . PRO B 1 443 ? 39.656  70.773  72.348 1.00 34.06 ? 443  PRO B CA    1 
ATOM   7545 C C     . PRO B 1 443 ? 39.285  71.357  73.713 1.00 32.71 ? 443  PRO B C     1 
ATOM   7546 O O     . PRO B 1 443 ? 38.114  71.355  74.017 1.00 29.13 ? 443  PRO B O     1 
ATOM   7547 C CB    . PRO B 1 443 ? 40.047  69.291  72.475 1.00 33.34 ? 443  PRO B CB    1 
ATOM   7548 C CG    . PRO B 1 443 ? 41.223  69.107  71.559 1.00 34.95 ? 443  PRO B CG    1 
ATOM   7549 C CD    . PRO B 1 443 ? 41.834  70.469  71.304 1.00 36.88 ? 443  PRO B CD    1 
ATOM   7550 N N     . ASP B 1 444 ? 40.249  71.845  74.497 1.00 31.70 ? 444  ASP B N     1 
ATOM   7551 C CA    . ASP B 1 444 ? 39.919  72.362  75.854 1.00 32.10 ? 444  ASP B CA    1 
ATOM   7552 C C     . ASP B 1 444 ? 39.197  73.706  75.699 1.00 29.50 ? 444  ASP B C     1 
ATOM   7553 O O     . ASP B 1 444 ? 38.313  74.039  76.530 1.00 28.23 ? 444  ASP B O     1 
ATOM   7554 C CB    . ASP B 1 444 ? 41.142  72.570  76.754 1.00 38.86 ? 444  ASP B CB    1 
ATOM   7555 C CG    . ASP B 1 444 ? 41.947  71.310  77.007 1.00 44.81 ? 444  ASP B CG    1 
ATOM   7556 O OD1   . ASP B 1 444 ? 41.346  70.239  77.204 1.00 47.65 ? 444  ASP B OD1   1 
ATOM   7557 O OD2   . ASP B 1 444 ? 43.171  71.424  77.012 1.00 55.70 ? 444  ASP B OD2   1 
ATOM   7558 N N     . GLU B 1 445 ? 39.630  74.524  74.749 1.00 29.21 ? 445  GLU B N     1 
ATOM   7559 C CA    . GLU B 1 445 ? 38.983  75.832  74.495 1.00 31.28 ? 445  GLU B CA    1 
ATOM   7560 C C     . GLU B 1 445 ? 37.572  75.571  73.951 1.00 28.24 ? 445  GLU B C     1 
ATOM   7561 O O     . GLU B 1 445 ? 36.655  76.289  74.369 1.00 28.09 ? 445  GLU B O     1 
ATOM   7562 C CB    . GLU B 1 445 ? 39.770  76.711  73.532 1.00 31.18 ? 445  GLU B CB    1 
ATOM   7563 C CG    . GLU B 1 445 ? 41.132  77.134  74.054 1.00 38.90 ? 445  GLU B CG    1 
ATOM   7564 C CD    . GLU B 1 445 ? 41.011  77.940  75.325 1.00 41.28 ? 445  GLU B CD    1 
ATOM   7565 O OE1   . GLU B 1 445 ? 40.438  79.010  75.236 1.00 41.28 ? 445  GLU B OE1   1 
ATOM   7566 O OE2   . GLU B 1 445 ? 41.412  77.424  76.413 1.00 45.58 ? 445  GLU B OE2   1 
ATOM   7567 N N     . ARG B 1 446 ? 37.420  74.623  73.032 1.00 28.05 ? 446  ARG B N     1 
ATOM   7568 C CA    . ARG B 1 446 ? 36.087  74.272  72.461 1.00 28.68 ? 446  ARG B CA    1 
ATOM   7569 C C     . ARG B 1 446 ? 35.162  73.839  73.595 1.00 27.65 ? 446  ARG B C     1 
ATOM   7570 O O     . ARG B 1 446 ? 34.010  74.265  73.644 1.00 25.65 ? 446  ARG B O     1 
ATOM   7571 C CB    . ARG B 1 446 ? 36.257  73.194  71.391 1.00 27.47 ? 446  ARG B CB    1 
ATOM   7572 C CG    . ARG B 1 446 ? 36.961  73.686  70.143 1.00 27.86 ? 446  ARG B CG    1 
ATOM   7573 C CD    . ARG B 1 446 ? 36.723  72.761  68.989 1.00 29.68 ? 446  ARG B CD    1 
ATOM   7574 N NE    . ARG B 1 446 ? 37.151  71.397  69.232 1.00 28.33 ? 446  ARG B NE    1 
ATOM   7575 C CZ    . ARG B 1 446 ? 38.104  70.726  68.592 1.00 34.40 ? 446  ARG B CZ    1 
ATOM   7576 N NH1   . ARG B 1 446 ? 38.832  71.273  67.628 1.00 35.67 ? 446  ARG B NH1   1 
ATOM   7577 N NH2   . ARG B 1 446 ? 38.310  69.467  68.928 1.00 33.09 ? 446  ARG B NH2   1 
ATOM   7578 N N     . LYS B 1 447 ? 35.673  73.054  74.530 1.00 27.45 ? 447  LYS B N     1 
ATOM   7579 C CA    . LYS B 1 447 ? 34.858  72.580  75.676 1.00 27.36 ? 447  LYS B CA    1 
ATOM   7580 C C     . LYS B 1 447 ? 34.379  73.761  76.498 1.00 27.10 ? 447  LYS B C     1 
ATOM   7581 O O     . LYS B 1 447 ? 33.192  73.806  76.827 1.00 26.99 ? 447  LYS B O     1 
ATOM   7582 C CB    . LYS B 1 447 ? 35.638  71.628  76.568 1.00 34.31 ? 447  LYS B CB    1 
ATOM   7583 C CG    . LYS B 1 447 ? 34.843  71.029  77.716 1.00 38.57 ? 447  LYS B CG    1 
ATOM   7584 C CD    . LYS B 1 447 ? 35.638  69.883  78.329 1.00 48.85 ? 447  LYS B CD    1 
ATOM   7585 C CE    . LYS B 1 447 ? 35.010  69.275  79.568 1.00 51.76 ? 447  LYS B CE    1 
ATOM   7586 N NZ    . LYS B 1 447 ? 34.984  70.255  80.672 1.00 57.13 ? 447  LYS B NZ    1 
ATOM   7587 N N     . LYS B 1 448 ? 35.268  74.686  76.843 1.00 27.96 ? 448  LYS B N     1 
ATOM   7588 C CA    . LYS B 1 448 ? 34.908  75.879  77.622 1.00 26.38 ? 448  LYS B CA    1 
ATOM   7589 C C     . LYS B 1 448 ? 33.880  76.709  76.842 1.00 25.45 ? 448  LYS B C     1 
ATOM   7590 O O     . LYS B 1 448 ? 32.963  77.238  77.468 1.00 24.32 ? 448  LYS B O     1 
ATOM   7591 C CB    . LYS B 1 448 ? 36.171  76.697  77.919 1.00 33.34 ? 448  LYS B CB    1 
ATOM   7592 C CG    . LYS B 1 448 ? 37.099  76.059  78.959 1.00 44.64 ? 448  LYS B CG    1 
ATOM   7593 C CD    . LYS B 1 448 ? 38.609  76.289  78.799 1.00 49.40 ? 448  LYS B CD    1 
ATOM   7594 C CE    . LYS B 1 448 ? 38.996  77.736  78.647 1.00 59.01 ? 448  LYS B CE    1 
ATOM   7595 N NZ    . LYS B 1 448 ? 38.381  78.542  79.719 1.00 66.72 ? 448  LYS B NZ    1 
ATOM   7596 N N     . LEU B 1 449 ? 34.127  76.921  75.556 1.00 24.21 ? 449  LEU B N     1 
ATOM   7597 C CA    . LEU B 1 449 ? 33.230  77.743  74.691 1.00 25.55 ? 449  LEU B CA    1 
ATOM   7598 C C     . LEU B 1 449 ? 31.807  77.141  74.717 1.00 24.22 ? 449  LEU B C     1 
ATOM   7599 O O     . LEU B 1 449 ? 30.877  77.879  74.959 1.00 24.73 ? 449  LEU B O     1 
ATOM   7600 C CB    . LEU B 1 449 ? 33.751  77.808  73.261 1.00 26.26 ? 449  LEU B CB    1 
ATOM   7601 C CG    . LEU B 1 449 ? 32.799  78.584  72.342 1.00 27.32 ? 449  LEU B CG    1 
ATOM   7602 C CD1   . LEU B 1 449 ? 32.935  80.071  72.592 1.00 26.29 ? 449  LEU B CD1   1 
ATOM   7603 C CD2   . LEU B 1 449 ? 33.013  78.256  70.923 1.00 35.25 ? 449  LEU B CD2   1 
ATOM   7604 N N     . ASP B 1 450 ? 31.676  75.833  74.516 1.00 26.44 ? 450  ASP B N     1 
ATOM   7605 C CA    . ASP B 1 450 ? 30.377  75.105  74.507 1.00 27.68 ? 450  ASP B CA    1 
ATOM   7606 C C     . ASP B 1 450 ? 29.673  75.270  75.846 1.00 28.31 ? 450  ASP B C     1 
ATOM   7607 O O     . ASP B 1 450 ? 28.452  75.562  75.890 1.00 26.91 ? 450  ASP B O     1 
ATOM   7608 C CB    . ASP B 1 450 ? 30.591  73.637  74.172 1.00 29.94 ? 450  ASP B CB    1 
ATOM   7609 C CG    . ASP B 1 450 ? 29.345  72.898  73.708 1.00 38.14 ? 450  ASP B CG    1 
ATOM   7610 O OD1   . ASP B 1 450 ? 28.355  73.549  73.239 1.00 31.96 ? 450  ASP B OD1   1 
ATOM   7611 O OD2   . ASP B 1 450 ? 29.390  71.663  73.782 1.00 40.14 ? 450  ASP B OD2   1 
ATOM   7612 N N     . GLU B 1 451 ? 30.415  75.106  76.933 1.00 25.05 ? 451  GLU B N     1 
ATOM   7613 C CA    . GLU B 1 451 ? 29.825  75.254  78.273 1.00 27.62 ? 451  GLU B CA    1 
ATOM   7614 C C     . GLU B 1 451 ? 29.353  76.676  78.467 1.00 24.29 ? 451  GLU B C     1 
ATOM   7615 O O     . GLU B 1 451 ? 28.269  76.879  79.037 1.00 25.20 ? 451  GLU B O     1 
ATOM   7616 C CB    . GLU B 1 451 ? 30.810  74.918  79.388 1.00 32.37 ? 451  GLU B CB    1 
ATOM   7617 C CG    . GLU B 1 451 ? 31.105  73.456  79.439 1.00 41.42 ? 451  GLU B CG    1 
ATOM   7618 C CD    . GLU B 1 451 ? 32.079  73.113  80.560 1.00 45.91 ? 451  GLU B CD    1 
ATOM   7619 O OE1   . GLU B 1 451 ? 32.634  72.000  80.447 1.00 46.79 ? 451  GLU B OE1   1 
ATOM   7620 O OE2   . GLU B 1 451 ? 32.240  73.952  81.531 1.00 46.64 ? 451  GLU B OE2   1 
ATOM   7621 N N     . LEU B 1 452 ? 30.178  77.644  78.082 1.00 26.66 ? 452  LEU B N     1 
ATOM   7622 C CA    . LEU B 1 452 ? 29.849  79.074  78.241 1.00 23.09 ? 452  LEU B CA    1 
ATOM   7623 C C     . LEU B 1 452 ? 28.576  79.403  77.424 1.00 21.87 ? 452  LEU B C     1 
ATOM   7624 O O     . LEU B 1 452 ? 27.709  80.157  77.902 1.00 22.44 ? 452  LEU B O     1 
ATOM   7625 C CB    . LEU B 1 452 ? 31.049  79.863  77.720 1.00 26.04 ? 452  LEU B CB    1 
ATOM   7626 C CG    . LEU B 1 452 ? 30.798  81.331  77.416 1.00 25.54 ? 452  LEU B CG    1 
ATOM   7627 C CD1   . LEU B 1 452 ? 30.399  82.086  78.655 1.00 23.97 ? 452  LEU B CD1   1 
ATOM   7628 C CD2   . LEU B 1 452 ? 32.010  81.979  76.760 1.00 25.78 ? 452  LEU B CD2   1 
ATOM   7629 N N     . PHE B 1 453 ? 28.498  78.885  76.214 1.00 24.51 ? 453  PHE B N     1 
ATOM   7630 C CA    . PHE B 1 453 ? 27.403  79.241  75.266 1.00 24.22 ? 453  PHE B CA    1 
ATOM   7631 C C     . PHE B 1 453 ? 26.065  78.759  75.856 1.00 24.20 ? 453  PHE B C     1 
ATOM   7632 O O     . PHE B 1 453 ? 25.121  79.547  75.866 1.00 23.92 ? 453  PHE B O     1 
ATOM   7633 C CB    . PHE B 1 453 ? 27.651  78.716  73.855 1.00 24.54 ? 453  PHE B CB    1 
ATOM   7634 C CG    . PHE B 1 453 ? 26.842  79.448  72.815 1.00 27.35 ? 453  PHE B CG    1 
ATOM   7635 C CD1   . PHE B 1 453 ? 25.517  79.109  72.573 1.00 26.53 ? 453  PHE B CD1   1 
ATOM   7636 C CD2   . PHE B 1 453 ? 27.404  80.478  72.078 1.00 26.46 ? 453  PHE B CD2   1 
ATOM   7637 C CE1   . PHE B 1 453 ? 24.768  79.782  71.618 1.00 25.67 ? 453  PHE B CE1   1 
ATOM   7638 C CE2   . PHE B 1 453 ? 26.661  81.136  71.111 1.00 25.08 ? 453  PHE B CE2   1 
ATOM   7639 C CZ    . PHE B 1 453 ? 25.342  80.799  70.897 1.00 26.02 ? 453  PHE B CZ    1 
ATOM   7640 N N     . ASN B 1 454 ? 26.034  77.536  76.391 1.00 26.22 ? 454  ASN B N     1 
ATOM   7641 C CA    . ASN B 1 454 ? 24.851  76.950  77.067 1.00 23.78 ? 454  ASN B CA    1 
ATOM   7642 C C     . ASN B 1 454 ? 24.466  77.822  78.242 1.00 24.18 ? 454  ASN B C     1 
ATOM   7643 O O     . ASN B 1 454 ? 23.254  78.089  78.396 1.00 27.95 ? 454  ASN B O     1 
ATOM   7644 C CB    . ASN B 1 454 ? 25.057  75.487  77.418 1.00 24.95 ? 454  ASN B CB    1 
ATOM   7645 C CG    . ASN B 1 454 ? 24.970  74.606  76.197 1.00 28.67 ? 454  ASN B CG    1 
ATOM   7646 O OD1   . ASN B 1 454 ? 23.988  74.633  75.475 1.00 40.79 ? 454  ASN B OD1   1 
ATOM   7647 N ND2   . ASN B 1 454 ? 26.004  73.851  75.920 1.00 34.07 ? 454  ASN B ND2   1 
ATOM   7648 N N     . ILE B 1 455 ? 25.438  78.325  79.018 1.00 23.07 ? 455  ILE B N     1 
ATOM   7649 C CA    . ILE B 1 455 ? 25.136  79.214  80.160 1.00 23.16 ? 455  ILE B CA    1 
ATOM   7650 C C     . ILE B 1 455 ? 24.512  80.507  79.634 1.00 23.64 ? 455  ILE B C     1 
ATOM   7651 O O     . ILE B 1 455 ? 23.512  80.970  80.243 1.00 23.12 ? 455  ILE B O     1 
ATOM   7652 C CB    . ILE B 1 455 ? 26.358  79.455  81.079 1.00 25.72 ? 455  ILE B CB    1 
ATOM   7653 C CG1   . ILE B 1 455 ? 26.749  78.200  81.866 1.00 32.33 ? 455  ILE B CG1   1 
ATOM   7654 C CG2   . ILE B 1 455 ? 26.127  80.625  82.014 1.00 25.89 ? 455  ILE B CG2   1 
ATOM   7655 C CD1   . ILE B 1 455 ? 28.197  78.183  82.344 1.00 29.77 ? 455  ILE B CD1   1 
ATOM   7656 N N     . LEU B 1 456 ? 25.102  81.141  78.607 1.00 22.45 ? 456  LEU B N     1 
ATOM   7657 C CA    . LEU B 1 456 ? 24.577  82.446  78.098 1.00 22.33 ? 456  LEU B CA    1 
ATOM   7658 C C     . LEU B 1 456 ? 23.111  82.261  77.632 1.00 20.02 ? 456  LEU B C     1 
ATOM   7659 O O     . LEU B 1 456 ? 22.305  83.108  77.908 1.00 21.06 ? 456  LEU B O     1 
ATOM   7660 C CB    . LEU B 1 456 ? 25.457  82.903  76.932 1.00 22.43 ? 456  LEU B CB    1 
ATOM   7661 C CG    . LEU B 1 456 ? 26.886  83.341  77.296 1.00 23.48 ? 456  LEU B CG    1 
ATOM   7662 C CD1   . LEU B 1 456 ? 27.710  83.647  76.044 1.00 26.39 ? 456  LEU B CD1   1 
ATOM   7663 C CD2   . LEU B 1 456 ? 26.859  84.555  78.191 1.00 22.49 ? 456  LEU B CD2   1 
ATOM   7664 N N     . VAL B 1 457 ? 22.812  81.173  76.943 1.00 21.18 ? 457  VAL B N     1 
ATOM   7665 C CA    . VAL B 1 457 ? 21.428  80.948  76.418 1.00 22.42 ? 457  VAL B CA    1 
ATOM   7666 C C     . VAL B 1 457 ? 20.465  80.826  77.618 1.00 23.30 ? 457  VAL B C     1 
ATOM   7667 O O     . VAL B 1 457 ? 19.433  81.528  77.649 1.00 24.57 ? 457  VAL B O     1 
ATOM   7668 C CB    . VAL B 1 457 ? 21.393  79.696  75.551 1.00 24.69 ? 457  VAL B CB    1 
ATOM   7669 C CG1   . VAL B 1 457 ? 19.952  79.250  75.295 1.00 25.17 ? 457  VAL B CG1   1 
ATOM   7670 C CG2   . VAL B 1 457 ? 22.189  79.885  74.246 1.00 24.45 ? 457  VAL B CG2   1 
ATOM   7671 N N     . ASP B 1 458 ? 20.845  80.025  78.607 1.00 25.00 ? 458  ASP B N     1 
ATOM   7672 C CA    . ASP B 1 458 ? 19.975  79.673  79.772 1.00 26.67 ? 458  ASP B CA    1 
ATOM   7673 C C     . ASP B 1 458 ? 19.768  80.927  80.610 1.00 25.97 ? 458  ASP B C     1 
ATOM   7674 O O     . ASP B 1 458 ? 18.624  81.233  80.929 1.00 26.97 ? 458  ASP B O     1 
ATOM   7675 C CB    . ASP B 1 458 ? 20.501  78.484  80.590 1.00 26.76 ? 458  ASP B CB    1 
ATOM   7676 C CG    . ASP B 1 458 ? 20.543  77.155  79.864 1.00 34.27 ? 458  ASP B CG    1 
ATOM   7677 O OD1   . ASP B 1 458 ? 19.987  77.023  78.730 1.00 35.69 ? 458  ASP B OD1   1 
ATOM   7678 O OD2   . ASP B 1 458 ? 21.214  76.254  80.397 1.00 35.67 ? 458  ASP B OD2   1 
ATOM   7679 N N     . GLU B 1 459 ? 20.825  81.700  80.883 1.00 26.60 ? 459  GLU B N     1 
ATOM   7680 C CA    . GLU B 1 459 ? 20.701  82.921  81.704 1.00 24.78 ? 459  GLU B CA    1 
ATOM   7681 C C     . GLU B 1 459 ? 19.884  83.958  80.966 1.00 23.36 ? 459  GLU B C     1 
ATOM   7682 O O     . GLU B 1 459 ? 19.070  84.643  81.611 1.00 24.47 ? 459  GLU B O     1 
ATOM   7683 C CB    . GLU B 1 459 ? 22.077  83.443  82.135 1.00 27.74 ? 459  GLU B CB    1 
ATOM   7684 C CG    . GLU B 1 459 ? 22.760  82.466  83.073 1.00 29.05 ? 459  GLU B CG    1 
ATOM   7685 C CD    . GLU B 1 459 ? 23.987  82.985  83.805 1.00 33.89 ? 459  GLU B CD    1 
ATOM   7686 O OE1   . GLU B 1 459 ? 24.697  83.822  83.247 1.00 31.32 ? 459  GLU B OE1   1 
ATOM   7687 O OE2   . GLU B 1 459 ? 24.226  82.508  84.928 1.00 29.28 ? 459  GLU B OE2   1 
ATOM   7688 N N     . ALA B 1 460 ? 20.063  84.089  79.647 1.00 21.95 ? 460  ALA B N     1 
ATOM   7689 C CA    . ALA B 1 460 ? 19.279  85.063  78.850 1.00 24.70 ? 460  ALA B CA    1 
ATOM   7690 C C     . ALA B 1 460 ? 17.780  84.670  78.885 1.00 20.01 ? 460  ALA B C     1 
ATOM   7691 O O     . ALA B 1 460 ? 16.958  85.543  79.139 1.00 23.09 ? 460  ALA B O     1 
ATOM   7692 C CB    . ALA B 1 460 ? 19.837  85.151  77.418 1.00 21.97 ? 460  ALA B CB    1 
ATOM   7693 N N     . ALA B 1 461 ? 17.469  83.406  78.619 1.00 22.76 ? 461  ALA B N     1 
ATOM   7694 C CA    . ALA B 1 461 ? 16.083  82.857  78.630 1.00 23.81 ? 461  ALA B CA    1 
ATOM   7695 C C     . ALA B 1 461 ? 15.440  83.086  80.017 1.00 25.18 ? 461  ALA B C     1 
ATOM   7696 O O     . ALA B 1 461 ? 14.286  83.569  80.077 1.00 24.76 ? 461  ALA B O     1 
ATOM   7697 C CB    . ALA B 1 461 ? 16.119  81.395  78.268 1.00 24.25 ? 461  ALA B CB    1 
ATOM   7698 N N     . ALA B 1 462 ? 16.201  82.901  81.108 1.00 25.58 ? 462  ALA B N     1 
ATOM   7699 C CA    . ALA B 1 462 ? 15.666  83.088  82.490 1.00 27.57 ? 462  ALA B CA    1 
ATOM   7700 C C     . ALA B 1 462 ? 15.373  84.571  82.678 1.00 26.26 ? 462  ALA B C     1 
ATOM   7701 O O     . ALA B 1 462 ? 14.565  84.890  83.510 1.00 31.03 ? 462  ALA B O     1 
ATOM   7702 C CB    . ALA B 1 462 ? 16.610  82.542  83.554 1.00 27.68 ? 462  ALA B CB    1 
ATOM   7703 N N     . GLU B 1 463 ? 15.944  85.469  81.878 1.00 25.44 ? 463  GLU B N     1 
ATOM   7704 C CA    . GLU B 1 463 ? 15.643  86.923  81.970 1.00 23.82 ? 463  GLU B CA    1 
ATOM   7705 C C     . GLU B 1 463 ? 14.646  87.322  80.884 1.00 24.44 ? 463  GLU B C     1 
ATOM   7706 O O     . GLU B 1 463 ? 14.404  88.544  80.702 1.00 24.55 ? 463  GLU B O     1 
ATOM   7707 C CB    . GLU B 1 463 ? 16.905  87.790  81.883 1.00 26.95 ? 463  GLU B CB    1 
ATOM   7708 C CG    . GLU B 1 463 ? 17.735  87.781  83.139 1.00 31.99 ? 463  GLU B CG    1 
ATOM   7709 C CD    . GLU B 1 463 ? 17.195  88.639  84.275 1.00 29.07 ? 463  GLU B CD    1 
ATOM   7710 O OE1   . GLU B 1 463 ? 16.507  89.668  84.063 1.00 35.57 ? 463  GLU B OE1   1 
ATOM   7711 O OE2   . GLU B 1 463 ? 17.438  88.234  85.347 1.00 38.38 ? 463  GLU B OE2   1 
ATOM   7712 N N     . GLY B 1 464 ? 14.042  86.341  80.188 1.00 22.98 ? 464  GLY B N     1 
ATOM   7713 C CA    . GLY B 1 464 ? 13.041  86.678  79.166 1.00 22.85 ? 464  GLY B CA    1 
ATOM   7714 C C     . GLY B 1 464 ? 13.686  87.186  77.874 1.00 23.78 ? 464  GLY B C     1 
ATOM   7715 O O     . GLY B 1 464 ? 13.008  87.910  77.107 1.00 23.93 ? 464  GLY B O     1 
ATOM   7716 N N     . TYR B 1 465 ? 14.941  86.821  77.612 1.00 24.53 ? 465  TYR B N     1 
ATOM   7717 C CA    . TYR B 1 465 ? 15.664  87.278  76.375 1.00 24.28 ? 465  TYR B CA    1 
ATOM   7718 C C     . TYR B 1 465 ? 15.907  86.088  75.444 1.00 21.21 ? 465  TYR B C     1 
ATOM   7719 O O     . TYR B 1 465 ? 16.449  85.012  75.861 1.00 22.26 ? 465  TYR B O     1 
ATOM   7720 C CB    . TYR B 1 465 ? 16.988  87.985  76.676 1.00 24.09 ? 465  TYR B CB    1 
ATOM   7721 C CG    . TYR B 1 465 ? 16.914  89.180  77.580 1.00 24.24 ? 465  TYR B CG    1 
ATOM   7722 C CD1   . TYR B 1 465 ? 16.016  90.207  77.374 1.00 21.69 ? 465  TYR B CD1   1 
ATOM   7723 C CD2   . TYR B 1 465 ? 17.805  89.308  78.657 1.00 23.38 ? 465  TYR B CD2   1 
ATOM   7724 C CE1   . TYR B 1 465 ? 16.001  91.327  78.198 1.00 22.13 ? 465  TYR B CE1   1 
ATOM   7725 C CE2   . TYR B 1 465 ? 17.801  90.424  79.471 1.00 24.00 ? 465  TYR B CE2   1 
ATOM   7726 C CZ    . TYR B 1 465 ? 16.864  91.426  79.284 1.00 23.68 ? 465  TYR B CZ    1 
ATOM   7727 O OH    . TYR B 1 465 ? 16.882  92.553  80.080 1.00 24.10 ? 465  TYR B OH    1 
ATOM   7728 N N     . GLY B 1 466 ? 15.493  86.264  74.186 1.00 19.85 ? 466  GLY B N     1 
ATOM   7729 C CA    . GLY B 1 466 ? 15.670  85.220  73.172 1.00 19.39 ? 466  GLY B CA    1 
ATOM   7730 C C     . GLY B 1 466 ? 16.669  85.646  72.104 1.00 19.83 ? 466  GLY B C     1 
ATOM   7731 O O     . GLY B 1 466 ? 16.792  86.852  71.864 1.00 20.56 ? 466  GLY B O     1 
ATOM   7732 N N     . GLU B 1 467 ? 17.304  84.674  71.466 1.00 19.97 ? 467  GLU B N     1 
ATOM   7733 C CA    . GLU B 1 467 ? 18.262  84.908  70.362 1.00 19.75 ? 467  GLU B CA    1 
ATOM   7734 C C     . GLU B 1 467 ? 17.477  85.039  69.054 1.00 19.29 ? 467  GLU B C     1 
ATOM   7735 O O     . GLU B 1 467 ? 16.453  84.291  68.884 1.00 19.80 ? 467  GLU B O     1 
ATOM   7736 C CB    . GLU B 1 467 ? 19.283  83.773  70.288 1.00 21.07 ? 467  GLU B CB    1 
ATOM   7737 C CG    . GLU B 1 467 ? 20.376  83.876  71.345 1.00 25.89 ? 467  GLU B CG    1 
ATOM   7738 C CD    . GLU B 1 467 ? 19.902  83.521  72.749 1.00 29.92 ? 467  GLU B CD    1 
ATOM   7739 O OE1   . GLU B 1 467 ? 19.868  82.317  73.051 1.00 29.33 ? 467  GLU B OE1   1 
ATOM   7740 O OE2   . GLU B 1 467 ? 19.573  84.437  73.515 1.00 31.86 ? 467  GLU B OE2   1 
ATOM   7741 N N     . TYR B 1 468 ? 17.942  85.889  68.138 1.00 18.16 ? 468  TYR B N     1 
ATOM   7742 C CA    . TYR B 1 468 ? 17.304  86.108  66.806 1.00 18.28 ? 468  TYR B CA    1 
ATOM   7743 C C     . TYR B 1 468 ? 17.862  85.118  65.782 1.00 17.06 ? 468  TYR B C     1 
ATOM   7744 O O     . TYR B 1 468 ? 17.229  84.947  64.692 1.00 17.46 ? 468  TYR B O     1 
ATOM   7745 C CB    . TYR B 1 468 ? 17.519  87.546  66.297 1.00 20.70 ? 468  TYR B CB    1 
ATOM   7746 C CG    . TYR B 1 468 ? 18.738  87.787  65.440 1.00 23.13 ? 468  TYR B CG    1 
ATOM   7747 C CD1   . TYR B 1 468 ? 20.040  87.864  65.946 1.00 23.97 ? 468  TYR B CD1   1 
ATOM   7748 C CD2   . TYR B 1 468 ? 18.583  87.969  64.069 1.00 21.17 ? 468  TYR B CD2   1 
ATOM   7749 C CE1   . TYR B 1 468 ? 21.148  88.097  65.110 1.00 25.92 ? 468  TYR B CE1   1 
ATOM   7750 C CE2   . TYR B 1 468 ? 19.667  88.229  63.235 1.00 24.32 ? 468  TYR B CE2   1 
ATOM   7751 C CZ    . TYR B 1 468 ? 20.968  88.269  63.739 1.00 27.33 ? 468  TYR B CZ    1 
ATOM   7752 O OH    . TYR B 1 468 ? 22.009  88.464  62.836 1.00 24.98 ? 468  TYR B OH    1 
ATOM   7753 N N     . ARG B 1 469 ? 19.001  84.520  66.083 1.00 17.22 ? 469  ARG B N     1 
ATOM   7754 C CA    . ARG B 1 469 ? 19.801  83.737  65.117 1.00 17.73 ? 469  ARG B CA    1 
ATOM   7755 C C     . ARG B 1 469 ? 20.833  82.913  65.888 1.00 19.56 ? 469  ARG B C     1 
ATOM   7756 O O     . ARG B 1 469 ? 21.365  83.397  66.906 1.00 19.29 ? 469  ARG B O     1 
ATOM   7757 C CB    . ARG B 1 469 ? 20.491  84.719  64.159 1.00 17.10 ? 469  ARG B CB    1 
ATOM   7758 C CG    . ARG B 1 469 ? 21.054  84.077  62.912 1.00 18.92 ? 469  ARG B CG    1 
ATOM   7759 C CD    . ARG B 1 469 ? 21.605  85.170  62.065 1.00 19.26 ? 469  ARG B CD    1 
ATOM   7760 N NE    . ARG B 1 469 ? 22.286  84.713  60.882 1.00 19.39 ? 469  ARG B NE    1 
ATOM   7761 C CZ    . ARG B 1 469 ? 22.891  85.550  60.032 1.00 20.75 ? 469  ARG B CZ    1 
ATOM   7762 N NH1   . ARG B 1 469 ? 22.958  86.843  60.297 1.00 20.00 ? 469  ARG B NH1   1 
ATOM   7763 N NH2   . ARG B 1 469 ? 23.529  85.057  58.985 1.00 19.32 ? 469  ARG B NH2   1 
ATOM   7764 N N     . THR B 1 470 ? 21.169  81.718  65.427 1.00 17.99 ? 470  THR B N     1 
ATOM   7765 C CA    . THR B 1 470 ? 22.124  80.900  66.195 1.00 19.30 ? 470  THR B CA    1 
ATOM   7766 C C     . THR B 1 470 ? 22.881  79.926  65.304 1.00 20.14 ? 470  THR B C     1 
ATOM   7767 O O     . THR B 1 470 ? 22.570  79.815  64.113 1.00 19.32 ? 470  THR B O     1 
ATOM   7768 C CB    . THR B 1 470 ? 21.471  80.201  67.375 1.00 19.15 ? 470  THR B CB    1 
ATOM   7769 O OG1   . THR B 1 470 ? 22.508  79.872  68.298 1.00 20.15 ? 470  THR B OG1   1 
ATOM   7770 C CG2   . THR B 1 470 ? 20.674  78.984  66.991 1.00 19.85 ? 470  THR B CG2   1 
ATOM   7771 N N     . HIS B 1 471 ? 23.876  79.296  65.920 1.00 20.32 ? 471  HIS B N     1 
ATOM   7772 C CA    . HIS B 1 471 ? 24.762  78.276  65.321 1.00 19.76 ? 471  HIS B CA    1 
ATOM   7773 C C     . HIS B 1 471 ? 23.981  76.963  65.251 1.00 20.75 ? 471  HIS B C     1 
ATOM   7774 O O     . HIS B 1 471 ? 23.163  76.682  66.178 1.00 21.44 ? 471  HIS B O     1 
ATOM   7775 C CB    . HIS B 1 471 ? 26.036  78.153  66.170 1.00 19.03 ? 471  HIS B CB    1 
ATOM   7776 C CG    . HIS B 1 471 ? 27.095  77.249  65.629 1.00 20.58 ? 471  HIS B CG    1 
ATOM   7777 N ND1   . HIS B 1 471 ? 27.006  75.871  65.680 1.00 21.15 ? 471  HIS B ND1   1 
ATOM   7778 C CD2   . HIS B 1 471 ? 28.320  77.531  65.115 1.00 20.40 ? 471  HIS B CD2   1 
ATOM   7779 C CE1   . HIS B 1 471 ? 28.097  75.337  65.130 1.00 21.84 ? 471  HIS B CE1   1 
ATOM   7780 N NE2   . HIS B 1 471 ? 28.948  76.348  64.814 1.00 21.92 ? 471  HIS B NE2   1 
ATOM   7781 N N     . ILE B 1 472 ? 24.264  76.170  64.218 1.00 19.25 ? 472  ILE B N     1 
ATOM   7782 C CA    . ILE B 1 472 ? 23.629  74.843  63.984 1.00 19.52 ? 472  ILE B CA    1 
ATOM   7783 C C     . ILE B 1 472 ? 23.663  74.003  65.263 1.00 20.01 ? 472  ILE B C     1 
ATOM   7784 O O     . ILE B 1 472 ? 22.708  73.221  65.501 1.00 20.79 ? 472  ILE B O     1 
ATOM   7785 C CB    . ILE B 1 472 ? 24.303  74.098  62.809 1.00 19.94 ? 472  ILE B CB    1 
ATOM   7786 C CG1   . ILE B 1 472 ? 25.793  73.846  63.054 1.00 21.33 ? 472  ILE B CG1   1 
ATOM   7787 C CG2   . ILE B 1 472 ? 24.025  74.801  61.491 1.00 20.38 ? 472  ILE B CG2   1 
ATOM   7788 C CD1   . ILE B 1 472 ? 26.560  73.293  61.871 1.00 21.33 ? 472  ILE B CD1   1 
ATOM   7789 N N     . ARG B 1 473 ? 24.698  74.151  66.091 1.00 22.36 ? 473  ARG B N     1 
ATOM   7790 C CA    . ARG B 1 473 ? 24.857  73.305  67.313 1.00 22.31 ? 473  ARG B CA    1 
ATOM   7791 C C     . ARG B 1 473 ? 23.727  73.575  68.312 1.00 19.31 ? 473  ARG B C     1 
ATOM   7792 O O     . ARG B 1 473 ? 23.357  72.655  69.072 1.00 20.67 ? 473  ARG B O     1 
ATOM   7793 C CB    . ARG B 1 473 ? 26.222  73.529  67.957 1.00 25.99 ? 473  ARG B CB    1 
ATOM   7794 C CG    . ARG B 1 473 ? 26.492  72.620  69.154 1.00 26.49 ? 473  ARG B CG    1 
ATOM   7795 C CD    . ARG B 1 473 ? 28.000  72.479  69.440 1.00 30.67 ? 473  ARG B CD    1 
ATOM   7796 N NE    . ARG B 1 473 ? 28.215  71.703  70.665 1.00 32.20 ? 473  ARG B NE    1 
ATOM   7797 C CZ    . ARG B 1 473 ? 28.133  70.373  70.740 1.00 35.04 ? 473  ARG B CZ    1 
ATOM   7798 N NH1   . ARG B 1 473 ? 27.860  69.651  69.660 1.00 33.45 ? 473  ARG B NH1   1 
ATOM   7799 N NH2   . ARG B 1 473 ? 28.327  69.776  71.902 1.00 35.14 ? 473  ARG B NH2   1 
ATOM   7800 N N     . TYR B 1 474 ? 23.206  74.780  68.333 1.00 19.13 ? 474  TYR B N     1 
ATOM   7801 C CA    . TYR B 1 474 ? 22.261  75.283  69.377 1.00 22.64 ? 474  TYR B CA    1 
ATOM   7802 C C     . TYR B 1 474 ? 20.860  75.536  68.806 1.00 22.69 ? 474  TYR B C     1 
ATOM   7803 O O     . TYR B 1 474 ? 20.039  76.135  69.504 1.00 21.71 ? 474  TYR B O     1 
ATOM   7804 C CB    . TYR B 1 474 ? 22.810  76.562  70.023 1.00 22.73 ? 474  TYR B CB    1 
ATOM   7805 C CG    . TYR B 1 474 ? 24.198  76.370  70.570 1.00 22.80 ? 474  TYR B CG    1 
ATOM   7806 C CD1   . TYR B 1 474 ? 24.429  75.578  71.686 1.00 24.43 ? 474  TYR B CD1   1 
ATOM   7807 C CD2   . TYR B 1 474 ? 25.277  76.940  69.924 1.00 24.41 ? 474  TYR B CD2   1 
ATOM   7808 C CE1   . TYR B 1 474 ? 25.717  75.350  72.131 1.00 26.00 ? 474  TYR B CE1   1 
ATOM   7809 C CE2   . TYR B 1 474 ? 26.571  76.708  70.341 1.00 26.15 ? 474  TYR B CE2   1 
ATOM   7810 C CZ    . TYR B 1 474 ? 26.790  75.928  71.462 1.00 27.93 ? 474  TYR B CZ    1 
ATOM   7811 O OH    . TYR B 1 474 ? 28.076  75.725  71.855 1.00 29.21 ? 474  TYR B OH    1 
ATOM   7812 N N     . MET B 1 475 ? 20.574  75.146  67.563 1.00 21.10 ? 475  MET B N     1 
ATOM   7813 C CA    . MET B 1 475 ? 19.237  75.481  66.985 1.00 20.22 ? 475  MET B CA    1 
ATOM   7814 C C     . MET B 1 475 ? 18.088  74.812  67.771 1.00 21.08 ? 475  MET B C     1 
ATOM   7815 O O     . MET B 1 475 ? 17.034  75.453  67.927 1.00 19.86 ? 475  MET B O     1 
ATOM   7816 C CB    . MET B 1 475 ? 19.177  75.135  65.502 1.00 18.35 ? 475  MET B CB    1 
ATOM   7817 C CG    . MET B 1 475 ? 19.941  76.134  64.682 1.00 18.00 ? 475  MET B CG    1 
ATOM   7818 S SD    . MET B 1 475 ? 20.031  75.644  62.947 1.00 18.99 ? 475  MET B SD    1 
ATOM   7819 C CE    . MET B 1 475 ? 20.974  77.023  62.319 1.00 20.17 ? 475  MET B CE    1 
ATOM   7820 N N     . ASP B 1 476 ? 18.258  73.594  68.265 1.00 20.91 ? 476  ASP B N     1 
ATOM   7821 C CA    . ASP B 1 476 ? 17.227  72.922  69.086 1.00 23.78 ? 476  ASP B CA    1 
ATOM   7822 C C     . ASP B 1 476 ? 17.090  73.648  70.417 1.00 23.74 ? 476  ASP B C     1 
ATOM   7823 O O     . ASP B 1 476 ? 15.952  73.901  70.864 1.00 20.95 ? 476  ASP B O     1 
ATOM   7824 C CB    . ASP B 1 476 ? 17.606  71.485  69.412 1.00 27.72 ? 476  ASP B CB    1 
ATOM   7825 C CG    . ASP B 1 476 ? 17.171  70.500  68.388 1.00 30.78 ? 476  ASP B CG    1 
ATOM   7826 O OD1   . ASP B 1 476 ? 16.516  70.921  67.418 1.00 31.57 ? 476  ASP B OD1   1 
ATOM   7827 O OD2   . ASP B 1 476 ? 17.547  69.343  68.536 1.00 36.46 ? 476  ASP B OD2   1 
ATOM   7828 N N     . ARG B 1 477 ? 18.225  73.964  71.031 1.00 21.39 ? 477  ARG B N     1 
ATOM   7829 C CA    . ARG B 1 477 ? 18.245  74.628  72.348 1.00 22.68 ? 477  ARG B CA    1 
ATOM   7830 C C     . ARG B 1 477 ? 17.489  75.968  72.247 1.00 22.22 ? 477  ARG B C     1 
ATOM   7831 O O     . ARG B 1 477 ? 16.699  76.279  73.139 1.00 20.23 ? 477  ARG B O     1 
ATOM   7832 C CB    . ARG B 1 477 ? 19.676  74.770  72.884 1.00 27.24 ? 477  ARG B CB    1 
ATOM   7833 C CG    . ARG B 1 477 ? 19.676  74.941  74.407 1.00 39.56 ? 477  ARG B CG    1 
ATOM   7834 C CD    . ARG B 1 477 ? 20.929  75.550  75.013 1.00 54.68 ? 477  ARG B CD    1 
ATOM   7835 N NE    . ARG B 1 477 ? 21.006  75.405  76.472 1.00 52.67 ? 477  ARG B NE    1 
ATOM   7836 C CZ    . ARG B 1 477 ? 21.320  74.270  77.074 1.00 65.70 ? 477  ARG B CZ    1 
ATOM   7837 N NH1   . ARG B 1 477 ? 21.562  73.191  76.345 1.00 69.43 ? 477  ARG B NH1   1 
ATOM   7838 N NH2   . ARG B 1 477 ? 21.365  74.194  78.394 1.00 67.79 ? 477  ARG B NH2   1 
ATOM   7839 N N     . ILE B 1 478 ? 17.739  76.777  71.211 1.00 21.40 ? 478  ILE B N     1 
ATOM   7840 C CA    . ILE B 1 478 ? 17.063  78.090  71.040 1.00 21.29 ? 478  ILE B CA    1 
ATOM   7841 C C     . ILE B 1 478 ? 15.560  77.883  70.753 1.00 21.28 ? 478  ILE B C     1 
ATOM   7842 O O     . ILE B 1 478 ? 14.742  78.601  71.362 1.00 20.37 ? 478  ILE B O     1 
ATOM   7843 C CB    . ILE B 1 478 ? 17.777  78.958  69.986 1.00 19.65 ? 478  ILE B CB    1 
ATOM   7844 C CG1   . ILE B 1 478 ? 19.214  79.317  70.363 1.00 25.02 ? 478  ILE B CG1   1 
ATOM   7845 C CG2   . ILE B 1 478 ? 16.961  80.201  69.675 1.00 20.64 ? 478  ILE B CG2   1 
ATOM   7846 C CD1   . ILE B 1 478 ? 19.466  79.522  71.787 1.00 27.31 ? 478  ILE B CD1   1 
ATOM   7847 N N     . ALA B 1 479 ? 15.168  76.940  69.889 1.00 20.34 ? 479  ALA B N     1 
ATOM   7848 C CA    . ALA B 1 479 ? 13.735  76.636  69.652 1.00 19.78 ? 479  ALA B CA    1 
ATOM   7849 C C     . ALA B 1 479 ? 13.035  76.379  70.996 1.00 20.01 ? 479  ALA B C     1 
ATOM   7850 O O     . ALA B 1 479 ? 11.934  76.876  71.203 1.00 19.75 ? 479  ALA B O     1 
ATOM   7851 C CB    . ALA B 1 479 ? 13.595  75.458  68.727 1.00 20.20 ? 479  ALA B CB    1 
ATOM   7852 N N     . LYS B 1 480 ? 13.704  75.660  71.900 1.00 19.90 ? 480  LYS B N     1 
ATOM   7853 C CA    . LYS B 1 480 ? 13.080  75.211  73.167 1.00 22.32 ? 480  LYS B CA    1 
ATOM   7854 C C     . LYS B 1 480 ? 12.942  76.397  74.111 1.00 22.03 ? 480  LYS B C     1 
ATOM   7855 O O     . LYS B 1 480 ? 12.218  76.262  75.094 1.00 20.45 ? 480  LYS B O     1 
ATOM   7856 C CB    . LYS B 1 480 ? 13.897  74.061  73.769 1.00 24.26 ? 480  LYS B CB    1 
ATOM   7857 C CG    . LYS B 1 480 ? 13.729  72.736  73.041 1.00 27.74 ? 480  LYS B CG    1 
ATOM   7858 C CD    . LYS B 1 480 ? 14.706  71.649  73.547 1.00 35.33 ? 480  LYS B CD    1 
ATOM   7859 C CE    . LYS B 1 480 ? 14.685  70.380  72.712 1.00 41.50 ? 480  LYS B CE    1 
ATOM   7860 N NZ    . LYS B 1 480 ? 13.295  69.956  72.374 1.00 43.46 ? 480  LYS B NZ    1 
ATOM   7861 N N     . THR B 1 481 ? 13.591  77.541  73.848 1.00 20.04 ? 481  THR B N     1 
ATOM   7862 C CA    . THR B 1 481 ? 13.423  78.739  74.693 1.00 19.47 ? 481  THR B CA    1 
ATOM   7863 C C     . THR B 1 481 ? 12.139  79.479  74.288 1.00 19.19 ? 481  THR B C     1 
ATOM   7864 O O     . THR B 1 481 ? 11.636  80.264  75.102 1.00 17.13 ? 481  THR B O     1 
ATOM   7865 C CB    . THR B 1 481 ? 14.625  79.699  74.645 1.00 20.79 ? 481  THR B CB    1 
ATOM   7866 O OG1   . THR B 1 481 ? 14.676  80.325  73.355 1.00 18.55 ? 481  THR B OG1   1 
ATOM   7867 C CG2   . THR B 1 481 ? 15.925  79.011  75.012 1.00 22.67 ? 481  THR B CG2   1 
ATOM   7868 N N     . TYR B 1 482 ? 11.631  79.264  73.079 1.00 18.50 ? 482  TYR B N     1 
ATOM   7869 C CA    . TYR B 1 482 ? 10.421  79.954  72.568 1.00 19.44 ? 482  TYR B CA    1 
ATOM   7870 C C     . TYR B 1 482 ? 9.209   79.063  72.859 1.00 19.53 ? 482  TYR B C     1 
ATOM   7871 O O     . TYR B 1 482 ? 8.420   78.723  71.981 1.00 17.71 ? 482  TYR B O     1 
ATOM   7872 C CB    . TYR B 1 482 ? 10.626  80.292  71.095 1.00 22.22 ? 482  TYR B CB    1 
ATOM   7873 C CG    . TYR B 1 482 ? 11.571  81.450  70.876 1.00 20.15 ? 482  TYR B CG    1 
ATOM   7874 C CD1   . TYR B 1 482 ? 11.129  82.746  70.977 1.00 19.36 ? 482  TYR B CD1   1 
ATOM   7875 C CD2   . TYR B 1 482 ? 12.883  81.236  70.515 1.00 20.01 ? 482  TYR B CD2   1 
ATOM   7876 C CE1   . TYR B 1 482 ? 11.972  83.819  70.748 1.00 19.98 ? 482  TYR B CE1   1 
ATOM   7877 C CE2   . TYR B 1 482 ? 13.744  82.298  70.320 1.00 20.30 ? 482  TYR B CE2   1 
ATOM   7878 C CZ    . TYR B 1 482 ? 13.293  83.600  70.435 1.00 18.87 ? 482  TYR B CZ    1 
ATOM   7879 O OH    . TYR B 1 482 ? 14.144  84.644  70.192 1.00 19.24 ? 482  TYR B OH    1 
ATOM   7880 N N     . SER B 1 483 ? 9.048   78.766  74.144 1.00 19.72 ? 483  SER B N     1 
ATOM   7881 C CA    . SER B 1 483 ? 8.238   77.633  74.657 1.00 19.35 ? 483  SER B CA    1 
ATOM   7882 C C     . SER B 1 483 ? 6.855   78.081  75.123 1.00 18.65 ? 483  SER B C     1 
ATOM   7883 O O     . SER B 1 483 ? 6.176   77.234  75.709 1.00 19.29 ? 483  SER B O     1 
ATOM   7884 C CB    . SER B 1 483 ? 8.990   76.951  75.803 1.00 21.61 ? 483  SER B CB    1 
ATOM   7885 O OG    . SER B 1 483 ? 9.051   77.865  76.870 1.00 20.48 ? 483  SER B OG    1 
ATOM   7886 N N     . TRP B 1 484 ? 6.424   79.310  74.841 1.00 17.95 ? 484  TRP B N     1 
ATOM   7887 C CA    . TRP B 1 484 ? 5.103   79.796  75.318 1.00 20.83 ? 484  TRP B CA    1 
ATOM   7888 C C     . TRP B 1 484 ? 4.005   78.748  75.013 1.00 19.65 ? 484  TRP B C     1 
ATOM   7889 O O     . TRP B 1 484 ? 3.930   78.201  73.881 1.00 18.25 ? 484  TRP B O     1 
ATOM   7890 C CB    . TRP B 1 484 ? 4.775   81.197  74.805 1.00 19.22 ? 484  TRP B CB    1 
ATOM   7891 C CG    . TRP B 1 484 ? 3.517   81.712  75.423 1.00 19.35 ? 484  TRP B CG    1 
ATOM   7892 C CD1   . TRP B 1 484 ? 3.386   82.165  76.719 1.00 21.71 ? 484  TRP B CD1   1 
ATOM   7893 C CD2   . TRP B 1 484 ? 2.189   81.668  74.869 1.00 18.99 ? 484  TRP B CD2   1 
ATOM   7894 N NE1   . TRP B 1 484 ? 2.078   82.474  76.975 1.00 19.87 ? 484  TRP B NE1   1 
ATOM   7895 C CE2   . TRP B 1 484 ? 1.324   82.188  75.855 1.00 19.92 ? 484  TRP B CE2   1 
ATOM   7896 C CE3   . TRP B 1 484 ? 1.640   81.291  73.630 1.00 19.44 ? 484  TRP B CE3   1 
ATOM   7897 C CZ2   . TRP B 1 484 ? -0.042  82.285  75.656 1.00 21.11 ? 484  TRP B CZ2   1 
ATOM   7898 C CZ3   . TRP B 1 484 ? 0.279   81.399  73.432 1.00 19.75 ? 484  TRP B CZ3   1 
ATOM   7899 C CH2   . TRP B 1 484 ? -0.552  81.914  74.430 1.00 20.27 ? 484  TRP B CH2   1 
ATOM   7900 N N     . ASN B 1 485 ? 3.153   78.495  75.997 1.00 19.42 ? 485  ASN B N     1 
ATOM   7901 C CA    . ASN B 1 485 ? 1.968   77.599  75.848 1.00 18.98 ? 485  ASN B CA    1 
ATOM   7902 C C     . ASN B 1 485 ? 2.468   76.223  75.432 1.00 18.64 ? 485  ASN B C     1 
ATOM   7903 O O     . ASN B 1 485 ? 1.991   75.710  74.420 1.00 17.97 ? 485  ASN B O     1 
ATOM   7904 C CB    . ASN B 1 485 ? 0.910   78.163  74.874 1.00 20.61 ? 485  ASN B CB    1 
ATOM   7905 C CG    . ASN B 1 485 ? -0.343  77.313  74.856 1.00 20.97 ? 485  ASN B CG    1 
ATOM   7906 O OD1   . ASN B 1 485 ? -0.641  76.710  75.893 1.00 22.27 ? 485  ASN B OD1   1 
ATOM   7907 N ND2   . ASN B 1 485 ? -1.058  77.266  73.741 1.00 17.70 ? 485  ASN B ND2   1 
ATOM   7908 N N     . ASP B 1 486 ? 3.394   75.631  76.205 1.00 18.10 ? 486  ASP B N     1 
ATOM   7909 C CA    . ASP B 1 486 ? 3.920   74.268  75.974 1.00 21.41 ? 486  ASP B CA    1 
ATOM   7910 C C     . ASP B 1 486 ? 4.410   74.084  74.526 1.00 20.25 ? 486  ASP B C     1 
ATOM   7911 O O     . ASP B 1 486 ? 3.992   73.104  73.842 1.00 19.43 ? 486  ASP B O     1 
ATOM   7912 C CB    . ASP B 1 486 ? 2.888   73.194  76.343 1.00 27.39 ? 486  ASP B CB    1 
ATOM   7913 C CG    . ASP B 1 486 ? 3.562   71.816  76.397 1.00 36.19 ? 486  ASP B CG    1 
ATOM   7914 O OD1   . ASP B 1 486 ? 4.729   71.753  76.853 1.00 46.15 ? 486  ASP B OD1   1 
ATOM   7915 O OD2   . ASP B 1 486 ? 2.966   70.807  75.903 1.00 47.26 ? 486  ASP B OD2   1 
ATOM   7916 N N     . ASN B 1 487 ? 5.287   74.991  74.060 1.00 20.81 ? 487  ASN B N     1 
ATOM   7917 C CA    . ASN B 1 487 ? 5.940   74.888  72.732 1.00 19.59 ? 487  ASN B CA    1 
ATOM   7918 C C     . ASN B 1 487 ? 4.881   74.951  71.626 1.00 19.21 ? 487  ASN B C     1 
ATOM   7919 O O     . ASN B 1 487 ? 5.011   74.277  70.599 1.00 18.02 ? 487  ASN B O     1 
ATOM   7920 C CB    . ASN B 1 487 ? 6.805   73.644  72.639 1.00 19.77 ? 487  ASN B CB    1 
ATOM   7921 C CG    . ASN B 1 487 ? 7.828   73.603  73.751 1.00 23.85 ? 487  ASN B CG    1 
ATOM   7922 O OD1   . ASN B 1 487 ? 8.770   74.382  73.810 1.00 22.19 ? 487  ASN B OD1   1 
ATOM   7923 N ND2   . ASN B 1 487 ? 7.588   72.743  74.713 1.00 24.87 ? 487  ASN B ND2   1 
ATOM   7924 N N     . ALA B 1 488 ? 3.863   75.764  71.789 1.00 17.81 ? 488  ALA B N     1 
ATOM   7925 C CA    . ALA B 1 488 ? 2.762   75.853  70.818 1.00 18.48 ? 488  ALA B CA    1 
ATOM   7926 C C     . ALA B 1 488 ? 3.281   76.295  69.448 1.00 19.67 ? 488  ALA B C     1 
ATOM   7927 O O     . ALA B 1 488 ? 2.787   75.752  68.431 1.00 19.04 ? 488  ALA B O     1 
ATOM   7928 C CB    . ALA B 1 488 ? 1.712   76.799  71.317 1.00 19.00 ? 488  ALA B CB    1 
ATOM   7929 N N     . LEU B 1 489 ? 4.156   77.299  69.383 1.00 18.13 ? 489  LEU B N     1 
ATOM   7930 C CA    . LEU B 1 489 ? 4.571   77.777  68.036 1.00 16.86 ? 489  LEU B CA    1 
ATOM   7931 C C     . LEU B 1 489 ? 5.330   76.675  67.289 1.00 18.09 ? 489  LEU B C     1 
ATOM   7932 O O     . LEU B 1 489 ? 5.079   76.504  66.069 1.00 17.89 ? 489  LEU B O     1 
ATOM   7933 C CB    . LEU B 1 489 ? 5.432   79.034  68.181 1.00 17.81 ? 489  LEU B CB    1 
ATOM   7934 C CG    . LEU B 1 489 ? 5.761   79.768  66.881 1.00 19.06 ? 489  LEU B CG    1 
ATOM   7935 C CD1   . LEU B 1 489 ? 4.502   80.135  66.131 1.00 21.00 ? 489  LEU B CD1   1 
ATOM   7936 C CD2   . LEU B 1 489 ? 6.596   80.985  67.177 1.00 19.13 ? 489  LEU B CD2   1 
ATOM   7937 N N     . TRP B 1 490 ? 6.227   75.935  67.946 1.00 16.87 ? 490  TRP B N     1 
ATOM   7938 C CA    . TRP B 1 490 ? 6.960   74.857  67.249 1.00 18.78 ? 490  TRP B CA    1 
ATOM   7939 C C     . TRP B 1 490 ? 6.029   73.710  66.856 1.00 18.73 ? 490  TRP B C     1 
ATOM   7940 O O     . TRP B 1 490 ? 6.301   73.081  65.851 1.00 17.32 ? 490  TRP B O     1 
ATOM   7941 C CB    . TRP B 1 490 ? 8.219   74.394  68.014 1.00 18.78 ? 490  TRP B CB    1 
ATOM   7942 C CG    . TRP B 1 490 ? 9.442   75.025  67.395 1.00 20.89 ? 490  TRP B CG    1 
ATOM   7943 C CD1   . TRP B 1 490 ? 10.374  74.417  66.587 1.00 22.23 ? 490  TRP B CD1   1 
ATOM   7944 C CD2   . TRP B 1 490 ? 9.773   76.430  67.370 1.00 20.44 ? 490  TRP B CD2   1 
ATOM   7945 N NE1   . TRP B 1 490 ? 11.308  75.331  66.157 1.00 20.86 ? 490  TRP B NE1   1 
ATOM   7946 C CE2   . TRP B 1 490 ? 10.930  76.578  66.563 1.00 20.28 ? 490  TRP B CE2   1 
ATOM   7947 C CE3   . TRP B 1 490 ? 9.218   77.578  67.944 1.00 19.51 ? 490  TRP B CE3   1 
ATOM   7948 C CZ2   . TRP B 1 490 ? 11.551  77.811  66.385 1.00 22.98 ? 490  TRP B CZ2   1 
ATOM   7949 C CZ3   . TRP B 1 490 ? 9.830   78.797  67.742 1.00 21.18 ? 490  TRP B CZ3   1 
ATOM   7950 C CH2   . TRP B 1 490 ? 10.971  78.910  66.961 1.00 20.60 ? 490  TRP B CH2   1 
ATOM   7951 N N     . LYS B 1 491 ? 4.961   73.438  67.601 1.00 18.51 ? 491  LYS B N     1 
ATOM   7952 C CA    . LYS B 1 491 ? 3.955   72.451  67.144 1.00 19.18 ? 491  LYS B CA    1 
ATOM   7953 C C     . LYS B 1 491 ? 3.346   72.943  65.838 1.00 20.88 ? 491  LYS B C     1 
ATOM   7954 O O     . LYS B 1 491 ? 3.094   72.125  64.891 1.00 19.38 ? 491  LYS B O     1 
ATOM   7955 C CB    . LYS B 1 491 ? 2.899   72.222  68.230 1.00 21.70 ? 491  LYS B CB    1 
ATOM   7956 C CG    . LYS B 1 491 ? 3.509   71.518  69.452 1.00 22.74 ? 491  LYS B CG    1 
ATOM   7957 C CD    . LYS B 1 491 ? 2.623   71.541  70.652 1.00 24.82 ? 491  LYS B CD    1 
ATOM   7958 C CE    . LYS B 1 491 ? 3.154   70.733  71.824 1.00 23.93 ? 491  LYS B CE    1 
ATOM   7959 N NZ    . LYS B 1 491 ? 2.284   70.956  73.001 1.00 25.23 ? 491  LYS B NZ    1 
ATOM   7960 N N     . MET B 1 492 ? 3.060   74.224  65.748 1.00 19.96 ? 492  MET B N     1 
ATOM   7961 C CA    . MET B 1 492 ? 2.525   74.713  64.455 1.00 20.65 ? 492  MET B CA    1 
ATOM   7962 C C     . MET B 1 492 ? 3.614   74.580  63.352 1.00 19.71 ? 492  MET B C     1 
ATOM   7963 O O     . MET B 1 492 ? 3.309   74.141  62.206 1.00 18.41 ? 492  MET B O     1 
ATOM   7964 C CB    . MET B 1 492 ? 2.062   76.165  64.603 1.00 20.64 ? 492  MET B CB    1 
ATOM   7965 C CG    . MET B 1 492 ? 1.453   76.758  63.326 1.00 23.33 ? 492  MET B CG    1 
ATOM   7966 S SD    . MET B 1 492 ? 1.586   78.567  63.292 1.00 25.62 ? 492  MET B SD    1 
ATOM   7967 C CE    . MET B 1 492 ? 3.330   78.688  62.960 1.00 28.86 ? 492  MET B CE    1 
ATOM   7968 N N     . HIS B 1 493 ? 4.857   74.964  63.600 1.00 18.93 ? 493  HIS B N     1 
ATOM   7969 C CA    . HIS B 1 493 ? 5.896   74.841  62.546 1.00 18.20 ? 493  HIS B CA    1 
ATOM   7970 C C     . HIS B 1 493 ? 6.018   73.382  62.070 1.00 19.81 ? 493  HIS B C     1 
ATOM   7971 O O     . HIS B 1 493 ? 6.159   73.165  60.868 1.00 17.10 ? 493  HIS B O     1 
ATOM   7972 C CB    . HIS B 1 493 ? 7.259   75.275  63.104 1.00 19.20 ? 493  HIS B CB    1 
ATOM   7973 C CG    . HIS B 1 493 ? 7.382   76.729  63.329 1.00 19.82 ? 493  HIS B CG    1 
ATOM   7974 N ND1   . HIS B 1 493 ? 6.828   77.631  62.468 1.00 18.81 ? 493  HIS B ND1   1 
ATOM   7975 C CD2   . HIS B 1 493 ? 8.077   77.433  64.257 1.00 18.98 ? 493  HIS B CD2   1 
ATOM   7976 C CE1   . HIS B 1 493 ? 7.162   78.846  62.880 1.00 20.40 ? 493  HIS B CE1   1 
ATOM   7977 N NE2   . HIS B 1 493 ? 7.927   78.741  63.986 1.00 17.38 ? 493  HIS B NE2   1 
ATOM   7978 N N     . GLU B 1 494 ? 5.967   72.415  62.990 1.00 18.09 ? 494  GLU B N     1 
ATOM   7979 C CA    . GLU B 1 494 ? 6.047   70.972  62.693 1.00 20.50 ? 494  GLU B CA    1 
ATOM   7980 C C     . GLU B 1 494 ? 4.813   70.535  61.887 1.00 21.25 ? 494  GLU B C     1 
ATOM   7981 O O     . GLU B 1 494 ? 4.966   69.702  60.975 1.00 19.86 ? 494  GLU B O     1 
ATOM   7982 C CB    . GLU B 1 494 ? 6.206   70.177  63.986 1.00 23.12 ? 494  GLU B CB    1 
ATOM   7983 C CG    . GLU B 1 494 ? 7.587   70.323  64.598 1.00 23.63 ? 494  GLU B CG    1 
ATOM   7984 C CD    . GLU B 1 494 ? 8.752   69.570  63.939 1.00 28.87 ? 494  GLU B CD    1 
ATOM   7985 O OE1   . GLU B 1 494 ? 8.547   68.781  62.962 1.00 32.76 ? 494  GLU B OE1   1 
ATOM   7986 O OE2   . GLU B 1 494 ? 9.908   69.758  64.409 1.00 29.70 ? 494  GLU B OE2   1 
ATOM   7987 N N     . THR B 1 495 ? 3.654   71.139  62.105 1.00 20.07 ? 495  THR B N     1 
ATOM   7988 C CA    . THR B 1 495 ? 2.446   70.859  61.285 1.00 20.44 ? 495  THR B CA    1 
ATOM   7989 C C     . THR B 1 495 ? 2.711   71.286  59.851 1.00 18.65 ? 495  THR B C     1 
ATOM   7990 O O     . THR B 1 495 ? 2.347   70.530  58.873 1.00 18.79 ? 495  THR B O     1 
ATOM   7991 C CB    . THR B 1 495 ? 1.186   71.552  61.843 1.00 21.03 ? 495  THR B CB    1 
ATOM   7992 O OG1   . THR B 1 495 ? 1.005   71.101  63.198 1.00 21.61 ? 495  THR B OG1   1 
ATOM   7993 C CG2   . THR B 1 495 ? -0.039  71.272  61.011 1.00 20.90 ? 495  THR B CG2   1 
ATOM   7994 N N     . ILE B 1 496 ? 3.249   72.485  59.685 1.00 19.08 ? 496  ILE B N     1 
ATOM   7995 C CA    . ILE B 1 496 ? 3.533   73.038  58.324 1.00 18.91 ? 496  ILE B CA    1 
ATOM   7996 C C     . ILE B 1 496 ? 4.659   72.230  57.682 1.00 19.44 ? 496  ILE B C     1 
ATOM   7997 O O     . ILE B 1 496 ? 4.536   71.865  56.481 1.00 18.14 ? 496  ILE B O     1 
ATOM   7998 C CB    . ILE B 1 496 ? 3.819   74.534  58.408 1.00 18.61 ? 496  ILE B CB    1 
ATOM   7999 C CG1   . ILE B 1 496 ? 2.596   75.319  58.898 1.00 19.90 ? 496  ILE B CG1   1 
ATOM   8000 C CG2   . ILE B 1 496 ? 4.274   75.060  57.060 1.00 20.30 ? 496  ILE B CG2   1 
ATOM   8001 C CD1   . ILE B 1 496 ? 2.972   76.726  59.312 1.00 23.60 ? 496  ILE B CD1   1 
ATOM   8002 N N     . LYS B 1 497 ? 5.677   71.880  58.473 1.00 18.03 ? 497  LYS B N     1 
ATOM   8003 C CA    . LYS B 1 497 ? 6.806   71.037  58.002 1.00 19.74 ? 497  LYS B CA    1 
ATOM   8004 C C     . LYS B 1 497 ? 6.308   69.703  57.403 1.00 21.04 ? 497  LYS B C     1 
ATOM   8005 O O     . LYS B 1 497 ? 6.755   69.332  56.289 1.00 20.52 ? 497  LYS B O     1 
ATOM   8006 C CB    . LYS B 1 497 ? 7.764   70.743  59.153 1.00 18.32 ? 497  LYS B CB    1 
ATOM   8007 C CG    . LYS B 1 497 ? 8.954   69.898  58.773 1.00 19.13 ? 497  LYS B CG    1 
ATOM   8008 C CD    . LYS B 1 497 ? 9.775   70.551  57.669 1.00 18.94 ? 497  LYS B CD    1 
ATOM   8009 C CE    . LYS B 1 497 ? 11.134  69.861  57.592 1.00 21.83 ? 497  LYS B CE    1 
ATOM   8010 N NZ    . LYS B 1 497 ? 11.926  70.253  56.405 1.00 21.34 ? 497  LYS B NZ    1 
ATOM   8011 N N     . ASP B 1 498 ? 5.432   69.000  58.120 1.00 19.04 ? 498  ASP B N     1 
ATOM   8012 C CA    . ASP B 1 498 ? 4.917   67.678  57.710 1.00 19.61 ? 498  ASP B CA    1 
ATOM   8013 C C     . ASP B 1 498 ? 4.040   67.825  56.479 1.00 22.83 ? 498  ASP B C     1 
ATOM   8014 O O     . ASP B 1 498 ? 4.040   66.913  55.649 1.00 23.66 ? 498  ASP B O     1 
ATOM   8015 C CB    . ASP B 1 498 ? 4.195   67.011  58.868 1.00 20.15 ? 498  ASP B CB    1 
ATOM   8016 C CG    . ASP B 1 498 ? 5.140   66.528  59.950 1.00 23.26 ? 498  ASP B CG    1 
ATOM   8017 O OD1   . ASP B 1 498 ? 6.361   66.385  59.699 1.00 25.59 ? 498  ASP B OD1   1 
ATOM   8018 O OD2   . ASP B 1 498 ? 4.663   66.349  61.054 1.00 25.17 ? 498  ASP B OD2   1 
ATOM   8019 N N     . ALA B 1 499 ? 3.342   68.934  56.326 1.00 21.74 ? 499  ALA B N     1 
ATOM   8020 C CA    . ALA B 1 499 ? 2.487   69.146  55.139 1.00 23.04 ? 499  ALA B CA    1 
ATOM   8021 C C     . ALA B 1 499 ? 3.352   69.475  53.920 1.00 20.80 ? 499  ALA B C     1 
ATOM   8022 O O     . ALA B 1 499 ? 3.086   68.908  52.861 1.00 20.91 ? 499  ALA B O     1 
ATOM   8023 C CB    . ALA B 1 499 ? 1.518   70.258  55.409 1.00 21.90 ? 499  ALA B CB    1 
ATOM   8024 N N     . LEU B 1 500 ? 4.338   70.363  54.018 1.00 19.86 ? 500  LEU B N     1 
ATOM   8025 C CA    . LEU B 1 500 ? 5.146   70.746  52.824 1.00 20.09 ? 500  LEU B CA    1 
ATOM   8026 C C     . LEU B 1 500 ? 6.209   69.697  52.524 1.00 20.19 ? 500  LEU B C     1 
ATOM   8027 O O     . LEU B 1 500 ? 6.528   69.540  51.367 1.00 20.64 ? 500  LEU B O     1 
ATOM   8028 C CB    . LEU B 1 500 ? 5.792   72.119  53.034 1.00 20.26 ? 500  LEU B CB    1 
ATOM   8029 C CG    . LEU B 1 500 ? 4.805   73.270  53.129 1.00 20.03 ? 500  LEU B CG    1 
ATOM   8030 C CD1   . LEU B 1 500 ? 5.553   74.568  53.448 1.00 20.06 ? 500  LEU B CD1   1 
ATOM   8031 C CD2   . LEU B 1 500 ? 4.053   73.393  51.820 1.00 19.85 ? 500  LEU B CD2   1 
ATOM   8032 N N     . ASP B 1 501 ? 6.759   69.041  53.546 1.00 20.28 ? 501  ASP B N     1 
ATOM   8033 C CA    . ASP B 1 501 ? 7.920   68.123  53.446 1.00 20.68 ? 501  ASP B CA    1 
ATOM   8034 C C     . ASP B 1 501 ? 7.625   66.857  54.246 1.00 22.02 ? 501  ASP B C     1 
ATOM   8035 O O     . ASP B 1 501 ? 8.320   66.535  55.238 1.00 20.81 ? 501  ASP B O     1 
ATOM   8036 C CB    . ASP B 1 501 ? 9.177   68.803  53.966 1.00 21.02 ? 501  ASP B CB    1 
ATOM   8037 C CG    . ASP B 1 501 ? 10.473  68.036  53.760 1.00 21.08 ? 501  ASP B CG    1 
ATOM   8038 O OD1   . ASP B 1 501 ? 10.492  67.035  52.962 1.00 21.53 ? 501  ASP B OD1   1 
ATOM   8039 O OD2   . ASP B 1 501 ? 11.478  68.508  54.310 1.00 20.54 ? 501  ASP B OD2   1 
ATOM   8040 N N     . PRO B 1 502 ? 6.641   66.070  53.791 1.00 23.81 ? 502  PRO B N     1 
ATOM   8041 C CA    . PRO B 1 502 ? 6.276   64.840  54.498 1.00 25.23 ? 502  PRO B CA    1 
ATOM   8042 C C     . PRO B 1 502 ? 7.456   63.859  54.654 1.00 25.56 ? 502  PRO B C     1 
ATOM   8043 O O     . PRO B 1 502 ? 7.525   63.175  55.675 1.00 24.11 ? 502  PRO B O     1 
ATOM   8044 C CB    . PRO B 1 502 ? 5.105   64.256  53.657 1.00 27.82 ? 502  PRO B CB    1 
ATOM   8045 C CG    . PRO B 1 502 ? 5.158   64.957  52.329 1.00 28.03 ? 502  PRO B CG    1 
ATOM   8046 C CD    . PRO B 1 502 ? 5.794   66.316  52.601 1.00 25.41 ? 502  PRO B CD    1 
ATOM   8047 N N     . ASN B 1 503 ? 8.408   63.824  53.718 1.00 21.26 ? 503  ASN B N     1 
ATOM   8048 C CA    . ASN B 1 503 ? 9.566   62.906  53.834 1.00 22.18 ? 503  ASN B CA    1 
ATOM   8049 C C     . ASN B 1 503 ? 10.697  63.526  54.666 1.00 23.18 ? 503  ASN B C     1 
ATOM   8050 O O     . ASN B 1 503 ? 11.708  62.856  54.875 1.00 21.92 ? 503  ASN B O     1 
ATOM   8051 C CB    . ASN B 1 503 ? 10.074  62.467  52.467 1.00 24.22 ? 503  ASN B CB    1 
ATOM   8052 C CG    . ASN B 1 503 ? 9.008   61.689  51.739 1.00 25.66 ? 503  ASN B CG    1 
ATOM   8053 O OD1   . ASN B 1 503 ? 8.366   60.844  52.338 1.00 26.49 ? 503  ASN B OD1   1 
ATOM   8054 N ND2   . ASN B 1 503 ? 8.781   62.003  50.487 1.00 24.00 ? 503  ASN B ND2   1 
ATOM   8055 N N     . GLY B 1 504 ? 10.575  64.779  55.076 1.00 22.51 ? 504  GLY B N     1 
ATOM   8056 C CA    . GLY B 1 504 ? 11.603  65.432  55.901 1.00 23.37 ? 504  GLY B CA    1 
ATOM   8057 C C     . GLY B 1 504 ? 12.949  65.523  55.224 1.00 22.65 ? 504  GLY B C     1 
ATOM   8058 O O     . GLY B 1 504 ? 13.944  65.416  55.916 1.00 24.03 ? 504  GLY B O     1 
ATOM   8059 N N     . ILE B 1 505 ? 13.000  65.803  53.923 1.00 19.82 ? 505  ILE B N     1 
ATOM   8060 C CA    . ILE B 1 505 ? 14.303  65.833  53.228 1.00 22.44 ? 505  ILE B CA    1 
ATOM   8061 C C     . ILE B 1 505 ? 14.907  67.237  53.179 1.00 21.14 ? 505  ILE B C     1 
ATOM   8062 O O     . ILE B 1 505 ? 16.082  67.341  52.726 1.00 23.12 ? 505  ILE B O     1 
ATOM   8063 C CB    . ILE B 1 505 ? 14.238  65.135  51.862 1.00 22.89 ? 505  ILE B CB    1 
ATOM   8064 C CG1   . ILE B 1 505 ? 13.138  65.656  50.958 1.00 25.56 ? 505  ILE B CG1   1 
ATOM   8065 C CG2   . ILE B 1 505 ? 14.103  63.659  52.081 1.00 25.07 ? 505  ILE B CG2   1 
ATOM   8066 C CD1   . ILE B 1 505 ? 13.426  67.000  50.361 1.00 26.92 ? 505  ILE B CD1   1 
ATOM   8067 N N     . LEU B 1 506 ? 14.234  68.290  53.639 1.00 19.66 ? 506  LEU B N     1 
ATOM   8068 C CA    . LEU B 1 506 ? 14.935  69.607  53.676 1.00 19.82 ? 506  LEU B CA    1 
ATOM   8069 C C     . LEU B 1 506 ? 15.450  69.901  55.088 1.00 18.77 ? 506  LEU B C     1 
ATOM   8070 O O     . LEU B 1 506 ? 14.628  70.077  56.004 1.00 19.74 ? 506  LEU B O     1 
ATOM   8071 C CB    . LEU B 1 506 ? 14.026  70.742  53.171 1.00 21.10 ? 506  LEU B CB    1 
ATOM   8072 C CG    . LEU B 1 506 ? 13.694  70.745  51.693 1.00 22.03 ? 506  LEU B CG    1 
ATOM   8073 C CD1   . LEU B 1 506 ? 13.047  72.076  51.317 1.00 23.85 ? 506  LEU B CD1   1 
ATOM   8074 C CD2   . LEU B 1 506 ? 14.903  70.469  50.827 1.00 21.84 ? 506  LEU B CD2   1 
ATOM   8075 N N     . ALA B 1 507 ? 16.762  70.058  55.202 1.00 18.45 ? 507  ALA B N     1 
ATOM   8076 C CA    . ALA B 1 507 ? 17.515  70.641  56.345 1.00 20.60 ? 507  ALA B CA    1 
ATOM   8077 C C     . ALA B 1 507 ? 16.935  70.226  57.697 1.00 18.86 ? 507  ALA B C     1 
ATOM   8078 O O     . ALA B 1 507 ? 16.519  71.076  58.490 1.00 18.12 ? 507  ALA B O     1 
ATOM   8079 C CB    . ALA B 1 507 ? 17.601  72.138  56.182 1.00 21.44 ? 507  ALA B CB    1 
ATOM   8080 N N     . PRO B 1 508 ? 16.872  68.916  57.996 1.00 20.07 ? 508  PRO B N     1 
ATOM   8081 C CA    . PRO B 1 508 ? 16.370  68.472  59.287 1.00 20.87 ? 508  PRO B CA    1 
ATOM   8082 C C     . PRO B 1 508 ? 17.182  69.162  60.394 1.00 19.52 ? 508  PRO B C     1 
ATOM   8083 O O     . PRO B 1 508 ? 18.400  69.158  60.382 1.00 20.25 ? 508  PRO B O     1 
ATOM   8084 C CB    . PRO B 1 508 ? 16.443  66.954  59.264 1.00 22.96 ? 508  PRO B CB    1 
ATOM   8085 C CG    . PRO B 1 508 ? 17.307  66.625  58.073 1.00 24.78 ? 508  PRO B CG    1 
ATOM   8086 C CD    . PRO B 1 508 ? 17.205  67.780  57.104 1.00 21.98 ? 508  PRO B CD    1 
ATOM   8087 N N     . GLY B 1 509 ? 16.454  69.803  61.315 1.00 18.24 ? 509  GLY B N     1 
ATOM   8088 C CA    . GLY B 1 509 ? 17.028  70.493  62.466 1.00 19.07 ? 509  GLY B CA    1 
ATOM   8089 C C     . GLY B 1 509 ? 17.169  71.984  62.258 1.00 18.76 ? 509  GLY B C     1 
ATOM   8090 O O     . GLY B 1 509 ? 17.469  72.641  63.216 1.00 18.08 ? 509  GLY B O     1 
ATOM   8091 N N     . LYS B 1 510 ? 17.015  72.517  61.046 1.00 18.25 ? 510  LYS B N     1 
ATOM   8092 C CA    . LYS B 1 510 ? 17.139  73.985  60.852 1.00 18.65 ? 510  LYS B CA    1 
ATOM   8093 C C     . LYS B 1 510 ? 16.081  74.635  61.760 1.00 16.97 ? 510  LYS B C     1 
ATOM   8094 O O     . LYS B 1 510 ? 14.916  74.187  61.760 1.00 17.70 ? 510  LYS B O     1 
ATOM   8095 C CB    . LYS B 1 510 ? 16.952  74.385  59.378 1.00 18.66 ? 510  LYS B CB    1 
ATOM   8096 C CG    . LYS B 1 510 ? 16.819  75.875  59.162 1.00 20.81 ? 510  LYS B CG    1 
ATOM   8097 C CD    . LYS B 1 510 ? 18.114  76.671  59.487 1.00 20.50 ? 510  LYS B CD    1 
ATOM   8098 C CE    . LYS B 1 510 ? 17.998  78.165  59.192 1.00 23.16 ? 510  LYS B CE    1 
ATOM   8099 N NZ    . LYS B 1 510 ? 19.109  78.943  59.835 1.00 23.21 ? 510  LYS B NZ    1 
ATOM   8100 N N     . SER B 1 511 ? 16.484  75.615  62.545 1.00 16.13 ? 511  SER B N     1 
ATOM   8101 C CA    . SER B 1 511 ? 15.635  76.325  63.527 1.00 15.36 ? 511  SER B CA    1 
ATOM   8102 C C     . SER B 1 511 ? 14.917  75.365  64.481 1.00 16.73 ? 511  SER B C     1 
ATOM   8103 O O     . SER B 1 511 ? 13.856  75.780  65.008 1.00 16.42 ? 511  SER B O     1 
ATOM   8104 C CB    . SER B 1 511 ? 14.634  77.210  62.789 1.00 16.97 ? 511  SER B CB    1 
ATOM   8105 O OG    . SER B 1 511 ? 15.290  78.140  61.943 1.00 18.04 ? 511  SER B OG    1 
ATOM   8106 N N     . GLY B 1 512 ? 15.473  74.172  64.742 1.00 17.06 ? 512  GLY B N     1 
ATOM   8107 C CA    . GLY B 1 512 ? 14.843  73.211  65.660 1.00 18.19 ? 512  GLY B CA    1 
ATOM   8108 C C     . GLY B 1 512 ? 13.610  72.573  65.066 1.00 18.15 ? 512  GLY B C     1 
ATOM   8109 O O     . GLY B 1 512 ? 12.845  71.976  65.824 1.00 16.65 ? 512  GLY B O     1 
ATOM   8110 N N     . ILE B 1 513 ? 13.465  72.604  63.738 1.00 17.98 ? 513  ILE B N     1 
ATOM   8111 C CA    . ILE B 1 513 ? 12.336  71.941  63.038 1.00 18.60 ? 513  ILE B CA    1 
ATOM   8112 C C     . ILE B 1 513 ? 12.826  70.633  62.401 1.00 20.42 ? 513  ILE B C     1 
ATOM   8113 O O     . ILE B 1 513 ? 13.706  70.697  61.534 1.00 20.39 ? 513  ILE B O     1 
ATOM   8114 C CB    . ILE B 1 513 ? 11.710  72.902  62.039 1.00 18.12 ? 513  ILE B CB    1 
ATOM   8115 C CG1   . ILE B 1 513 ? 11.266  74.201  62.700 1.00 20.60 ? 513  ILE B CG1   1 
ATOM   8116 C CG2   . ILE B 1 513 ? 10.572  72.214  61.270 1.00 18.26 ? 513  ILE B CG2   1 
ATOM   8117 C CD1   . ILE B 1 513 ? 10.821  75.251  61.683 1.00 20.47 ? 513  ILE B CD1   1 
ATOM   8118 N N     . TRP B 1 514 ? 12.200  69.502  62.744 1.00 19.94 ? 514  TRP B N     1 
ATOM   8119 C CA    . TRP B 1 514 ? 12.684  68.147  62.356 1.00 22.88 ? 514  TRP B CA    1 
ATOM   8120 C C     . TRP B 1 514 ? 11.784  67.386  61.368 1.00 22.69 ? 514  TRP B C     1 
ATOM   8121 O O     . TRP B 1 514 ? 12.340  66.610  60.497 1.00 28.01 ? 514  TRP B O     1 
ATOM   8122 C CB    . TRP B 1 514 ? 12.926  67.336  63.637 1.00 20.29 ? 514  TRP B CB    1 
ATOM   8123 C CG    . TRP B 1 514 ? 14.197  67.811  64.280 1.00 21.02 ? 514  TRP B CG    1 
ATOM   8124 C CD1   . TRP B 1 514 ? 14.311  68.748  65.269 1.00 20.96 ? 514  TRP B CD1   1 
ATOM   8125 C CD2   . TRP B 1 514 ? 15.542  67.399  63.958 1.00 20.50 ? 514  TRP B CD2   1 
ATOM   8126 N NE1   . TRP B 1 514 ? 15.623  68.951  65.570 1.00 21.64 ? 514  TRP B NE1   1 
ATOM   8127 C CE2   . TRP B 1 514 ? 16.404  68.112  64.818 1.00 22.45 ? 514  TRP B CE2   1 
ATOM   8128 C CE3   . TRP B 1 514 ? 16.102  66.456  63.084 1.00 22.83 ? 514  TRP B CE3   1 
ATOM   8129 C CZ2   . TRP B 1 514 ? 17.779  67.925  64.796 1.00 22.46 ? 514  TRP B CZ2   1 
ATOM   8130 C CZ3   . TRP B 1 514 ? 17.463  66.260  63.076 1.00 23.23 ? 514  TRP B CZ3   1 
ATOM   8131 C CH2   . TRP B 1 514 ? 18.288  67.010  63.897 1.00 23.62 ? 514  TRP B CH2   1 
ATOM   8132 N N     . GLY B 1 515 ? 10.482  67.508  61.515 1.00 22.80 ? 515  GLY B N     1 
ATOM   8133 C CA    . GLY B 1 515 ? 9.586   66.688  60.694 1.00 24.23 ? 515  GLY B CA    1 
ATOM   8134 C C     . GLY B 1 515 ? 9.324   65.329  61.356 1.00 23.54 ? 515  GLY B C     1 
ATOM   8135 O O     . GLY B 1 515 ? 10.160  64.848  62.163 1.00 23.57 ? 515  GLY B O     1 
ATOM   8136 N N     . LYS B 1 516 ? 8.182   64.736  61.056 1.00 24.52 ? 516  LYS B N     1 
ATOM   8137 C CA    . LYS B 1 516 ? 7.631   63.567  61.801 1.00 29.07 ? 516  LYS B CA    1 
ATOM   8138 C C     . LYS B 1 516 ? 8.609   62.393  61.767 1.00 28.68 ? 516  LYS B C     1 
ATOM   8139 O O     . LYS B 1 516 ? 8.702   61.743  62.779 1.00 27.01 ? 516  LYS B O     1 
ATOM   8140 C CB    . LYS B 1 516 ? 6.239   63.129  61.315 1.00 33.65 ? 516  LYS B CB    1 
ATOM   8141 C CG    . LYS B 1 516 ? 6.131   62.714  59.855 1.00 41.76 ? 516  LYS B CG    1 
ATOM   8142 C CD    . LYS B 1 516 ? 4.762   62.102  59.544 1.00 51.13 ? 516  LYS B CD    1 
ATOM   8143 C CE    . LYS B 1 516 ? 4.237   62.472  58.170 1.00 56.36 ? 516  LYS B CE    1 
ATOM   8144 N NZ    . LYS B 1 516 ? 5.102   61.879  57.129 1.00 49.41 ? 516  LYS B NZ    1 
ATOM   8145 N N     . ASN B 1 517 ? 9.362   62.171  60.702 1.00 26.68 ? 517  ASN B N     1 
ATOM   8146 C CA    . ASN B 1 517 ? 10.247  60.977  60.661 1.00 32.28 ? 517  ASN B CA    1 
ATOM   8147 C C     . ASN B 1 517 ? 11.356  61.083  61.716 1.00 34.16 ? 517  ASN B C     1 
ATOM   8148 O O     . ASN B 1 517 ? 11.914  60.032  62.088 1.00 33.86 ? 517  ASN B O     1 
ATOM   8149 C CB    . ASN B 1 517 ? 10.874  60.795  59.279 1.00 32.90 ? 517  ASN B CB    1 
ATOM   8150 C CG    . ASN B 1 517 ? 9.848   60.440  58.238 1.00 35.44 ? 517  ASN B CG    1 
ATOM   8151 O OD1   . ASN B 1 517 ? 8.724   60.056  58.568 1.00 35.73 ? 517  ASN B OD1   1 
ATOM   8152 N ND2   . ASN B 1 517 ? 10.212  60.622  56.984 1.00 35.62 ? 517  ASN B ND2   1 
ATOM   8153 N N     . ARG B 1 518 ? 11.775  62.281  62.120 1.00 35.24 ? 518  ARG B N     1 
ATOM   8154 C CA    . ARG B 1 518 ? 12.962  62.416  63.033 1.00 35.91 ? 518  ARG B CA    1 
ATOM   8155 C C     . ARG B 1 518 ? 12.625  63.087  64.369 1.00 41.28 ? 518  ARG B C     1 
ATOM   8156 O O     . ARG B 1 518 ? 13.559  63.261  65.139 1.00 46.11 ? 518  ARG B O     1 
ATOM   8157 C CB    . ARG B 1 518 ? 14.095  63.190  62.382 1.00 30.82 ? 518  ARG B CB    1 
ATOM   8158 C CG    . ARG B 1 518 ? 14.514  62.538  61.081 1.00 32.19 ? 518  ARG B CG    1 
ATOM   8159 C CD    . ARG B 1 518 ? 15.689  63.218  60.436 1.00 34.65 ? 518  ARG B CD    1 
ATOM   8160 N NE    . ARG B 1 518 ? 16.030  62.553  59.176 1.00 31.47 ? 518  ARG B NE    1 
ATOM   8161 C CZ    . ARG B 1 518 ? 16.815  61.451  59.031 1.00 39.70 ? 518  ARG B CZ    1 
ATOM   8162 N NH1   . ARG B 1 518 ? 17.403  60.841  60.058 1.00 33.51 ? 518  ARG B NH1   1 
ATOM   8163 N NH2   . ARG B 1 518 ? 17.003  60.941  57.821 1.00 40.21 ? 518  ARG B NH2   1 
ATOM   8164 N N     . ARG B 1 519 ? 11.367  63.417  64.658 1.00 38.48 ? 519  ARG B N     1 
ATOM   8165 C CA    . ARG B 1 519 ? 11.000  64.066  65.946 1.00 45.82 ? 519  ARG B CA    1 
ATOM   8166 C C     . ARG B 1 519 ? 11.112  63.051  67.097 1.00 44.50 ? 519  ARG B C     1 
ATOM   8167 O O     . ARG B 1 519 ? 10.358  62.082  66.969 1.00 45.06 ? 519  ARG B O     1 
ATOM   8168 C CB    . ARG B 1 519 ? 9.563   64.593  65.902 1.00 48.15 ? 519  ARG B CB    1 
ATOM   8169 C CG    . ARG B 1 519 ? 9.422   65.992  65.333 1.00 48.80 ? 519  ARG B CG    1 
ATOM   8170 C CD    . ARG B 1 519 ? 8.094   66.653  65.698 1.00 46.76 ? 519  ARG B CD    1 
ATOM   8171 N NE    . ARG B 1 519 ? 6.858   66.038  65.195 1.00 48.52 ? 519  ARG B NE    1 
ATOM   8172 C CZ    . ARG B 1 519 ? 6.306   66.183  63.963 1.00 44.84 ? 519  ARG B CZ    1 
ATOM   8173 N NH1   . ARG B 1 519 ? 6.883   66.879  63.003 1.00 34.53 ? 519  ARG B NH1   1 
ATOM   8174 N NH2   . ARG B 1 519 ? 5.169   65.579  63.679 1.00 46.46 ? 519  ARG B NH2   1 
HETATM 8175 P PA    . FAD C 2 .   ? -12.792 93.403  59.027 1.00 20.97 ? 601  FAD A PA    1 
HETATM 8176 O O1A   . FAD C 2 .   ? -14.072 93.463  58.247 1.00 19.14 ? 601  FAD A O1A   1 
HETATM 8177 O O2A   . FAD C 2 .   ? -12.942 93.036  60.471 1.00 19.14 ? 601  FAD A O2A   1 
HETATM 8178 O O5B   . FAD C 2 .   ? -11.743 92.358  58.369 1.00 20.28 ? 601  FAD A O5B   1 
HETATM 8179 C C5B   . FAD C 2 .   ? -11.571 92.268  56.947 1.00 19.14 ? 601  FAD A C5B   1 
HETATM 8180 C C4B   . FAD C 2 .   ? -11.403 90.814  56.591 1.00 20.62 ? 601  FAD A C4B   1 
HETATM 8181 O O4B   . FAD C 2 .   ? -10.117 90.334  57.078 1.00 20.82 ? 601  FAD A O4B   1 
HETATM 8182 C C3B   . FAD C 2 .   ? -12.428 89.813  57.163 1.00 21.82 ? 601  FAD A C3B   1 
HETATM 8183 O O3B   . FAD C 2 .   ? -13.520 89.694  56.264 1.00 21.38 ? 601  FAD A O3B   1 
HETATM 8184 C C2B   . FAD C 2 .   ? -11.600 88.520  57.208 1.00 22.87 ? 601  FAD A C2B   1 
HETATM 8185 O O2B   . FAD C 2 .   ? -11.511 87.899  55.949 1.00 22.31 ? 601  FAD A O2B   1 
HETATM 8186 C C1B   . FAD C 2 .   ? -10.247 89.039  57.641 1.00 21.75 ? 601  FAD A C1B   1 
HETATM 8187 N N9A   . FAD C 2 .   ? -10.087 89.134  59.108 1.00 22.31 ? 601  FAD A N9A   1 
HETATM 8188 C C8A   . FAD C 2 .   ? -10.314 90.251  59.838 1.00 21.69 ? 601  FAD A C8A   1 
HETATM 8189 N N7A   . FAD C 2 .   ? -10.043 90.088  61.116 1.00 22.24 ? 601  FAD A N7A   1 
HETATM 8190 C C5A   . FAD C 2 .   ? -9.565  88.788  61.211 1.00 20.03 ? 601  FAD A C5A   1 
HETATM 8191 C C6A   . FAD C 2 .   ? -9.049  88.070  62.301 1.00 19.12 ? 601  FAD A C6A   1 
HETATM 8192 N N6A   . FAD C 2 .   ? -8.948  88.599  63.521 1.00 19.52 ? 601  FAD A N6A   1 
HETATM 8193 N N1A   . FAD C 2 .   ? -8.597  86.819  62.067 1.00 21.28 ? 601  FAD A N1A   1 
HETATM 8194 C C2A   . FAD C 2 .   ? -8.708  86.342  60.810 1.00 23.29 ? 601  FAD A C2A   1 
HETATM 8195 N N3A   . FAD C 2 .   ? -9.153  86.940  59.701 1.00 20.32 ? 601  FAD A N3A   1 
HETATM 8196 C C4A   . FAD C 2 .   ? -9.558  88.192  59.969 1.00 21.86 ? 601  FAD A C4A   1 
HETATM 8197 N N1    . FAD C 2 .   ? -9.886  100.368 53.043 1.00 20.35 ? 601  FAD A N1    1 
HETATM 8198 C C2    . FAD C 2 .   ? -8.620  100.776 53.264 1.00 20.68 ? 601  FAD A C2    1 
HETATM 8199 O O2    . FAD C 2 .   ? -7.728  99.941  53.520 1.00 17.78 ? 601  FAD A O2    1 
HETATM 8200 N N3    . FAD C 2 .   ? -8.264  102.132 53.164 1.00 21.18 ? 601  FAD A N3    1 
HETATM 8201 C C4    . FAD C 2 .   ? -9.196  103.129 52.898 1.00 20.40 ? 601  FAD A C4    1 
HETATM 8202 O O4    . FAD C 2 .   ? -8.838  104.312 52.852 1.00 19.77 ? 601  FAD A O4    1 
HETATM 8203 C C4X   . FAD C 2 .   ? -10.532 102.706 52.639 1.00 21.16 ? 601  FAD A C4X   1 
HETATM 8204 N N5    . FAD C 2 .   ? -11.475 103.626 52.404 1.00 23.70 ? 601  FAD A N5    1 
HETATM 8205 C C5X   . FAD C 2 .   ? -12.745 103.188 52.124 1.00 22.50 ? 601  FAD A C5X   1 
HETATM 8206 C C6    . FAD C 2 .   ? -13.725 104.153 51.764 1.00 23.01 ? 601  FAD A C6    1 
HETATM 8207 C C7    . FAD C 2 .   ? -15.015 103.790 51.426 1.00 22.75 ? 601  FAD A C7    1 
HETATM 8208 C C7M   . FAD C 2 .   ? -16.048 104.850 51.111 1.00 23.68 ? 601  FAD A C7M   1 
HETATM 8209 C C8    . FAD C 2 .   ? -15.380 102.431 51.442 1.00 22.66 ? 601  FAD A C8    1 
HETATM 8210 C C8M   . FAD C 2 .   ? -16.759 102.015 50.956 1.00 26.68 ? 601  FAD A C8M   1 
HETATM 8211 C C9    . FAD C 2 .   ? -14.421 101.463 51.817 1.00 22.52 ? 601  FAD A C9    1 
HETATM 8212 C C9A   . FAD C 2 .   ? -13.100 101.822 52.162 1.00 21.67 ? 601  FAD A C9A   1 
HETATM 8213 N N10   . FAD C 2 .   ? -12.118 100.884 52.541 1.00 22.97 ? 601  FAD A N10   1 
HETATM 8214 C C10   . FAD C 2 .   ? -10.796 101.286 52.758 1.00 22.53 ? 601  FAD A C10   1 
HETATM 8215 C "C1'" . FAD C 2 .   ? -12.441 99.443  52.602 1.00 21.54 ? 601  FAD A "C1'" 1 
HETATM 8216 C "C2'" . FAD C 2 .   ? -12.967 98.948  53.945 1.00 22.12 ? 601  FAD A "C2'" 1 
HETATM 8217 O "O2'" . FAD C 2 .   ? -14.236 99.510  54.211 1.00 26.30 ? 601  FAD A "O2'" 1 
HETATM 8218 C "C3'" . FAD C 2 .   ? -12.031 99.236  55.138 1.00 22.13 ? 601  FAD A "C3'" 1 
HETATM 8219 O "O3'" . FAD C 2 .   ? -10.725 98.726  54.815 1.00 20.96 ? 601  FAD A "O3'" 1 
HETATM 8220 C "C4'" . FAD C 2 .   ? -12.470 98.673  56.497 1.00 21.29 ? 601  FAD A "C4'" 1 
HETATM 8221 O "O4'" . FAD C 2 .   ? -11.643 99.214  57.527 1.00 22.70 ? 601  FAD A "O4'" 1 
HETATM 8222 C "C5'" . FAD C 2 .   ? -12.318 97.169  56.606 1.00 20.46 ? 601  FAD A "C5'" 1 
HETATM 8223 O "O5'" . FAD C 2 .   ? -13.204 96.633  57.668 1.00 19.71 ? 601  FAD A "O5'" 1 
HETATM 8224 P P     . FAD C 2 .   ? -12.628 96.331  59.110 1.00 20.22 ? 601  FAD A P     1 
HETATM 8225 O O1P   . FAD C 2 .   ? -11.492 97.219  59.458 1.00 19.17 ? 601  FAD A O1P   1 
HETATM 8226 O O2P   . FAD C 2 .   ? -13.807 96.268  60.063 1.00 19.49 ? 601  FAD A O2P   1 
HETATM 8227 O O3P   . FAD C 2 .   ? -12.043 94.837  58.923 1.00 19.37 ? 601  FAD A O3P   1 
HETATM 8228 N N     . NO3 D 3 .   ? -22.442 115.743 49.610 1.00 62.60 ? 602  NO3 A N     1 
HETATM 8229 O O1    . NO3 D 3 .   ? -23.653 116.034 49.479 1.00 56.61 ? 602  NO3 A O1    1 
HETATM 8230 O O2    . NO3 D 3 .   ? -21.750 116.260 50.485 1.00 56.99 ? 602  NO3 A O2    1 
HETATM 8231 O O3    . NO3 D 3 .   ? -21.914 114.943 48.865 1.00 56.70 ? 602  NO3 A O3    1 
HETATM 8232 N N     . NO3 E 3 .   ? 3.439   104.139 52.280 1.00 75.06 ? 603  NO3 A N     1 
HETATM 8233 O O1    . NO3 E 3 .   ? 3.349   103.022 51.747 1.00 65.28 ? 603  NO3 A O1    1 
HETATM 8234 O O2    . NO3 E 3 .   ? 4.110   105.039 51.762 1.00 59.23 ? 603  NO3 A O2    1 
HETATM 8235 O O3    . NO3 E 3 .   ? 2.851   104.355 53.344 1.00 61.50 ? 603  NO3 A O3    1 
HETATM 8236 C C1    . PEG F 4 .   ? -12.473 114.917 29.794 1.00 45.49 ? 604  PEG A C1    1 
HETATM 8237 O O1    . PEG F 4 .   ? -12.319 115.371 28.433 1.00 42.05 ? 604  PEG A O1    1 
HETATM 8238 C C2    . PEG F 4 .   ? -12.657 116.050 30.783 1.00 43.88 ? 604  PEG A C2    1 
HETATM 8239 O O2    . PEG F 4 .   ? -11.551 116.965 30.765 1.00 42.84 ? 604  PEG A O2    1 
HETATM 8240 C C3    . PEG F 4 .   ? -11.845 118.217 31.385 1.00 39.48 ? 604  PEG A C3    1 
HETATM 8241 C C4    . PEG F 4 .   ? -10.662 119.113 31.425 1.00 40.11 ? 604  PEG A C4    1 
HETATM 8242 O O4    . PEG F 4 .   ? -10.395 119.750 30.177 1.00 39.66 ? 604  PEG A O4    1 
HETATM 8243 O OH2   . 1PE G 5 .   ? -25.178 104.162 51.213 1.00 44.57 ? 605  1PE A OH2   1 
HETATM 8244 C C12   . 1PE G 5 .   ? -26.156 103.094 51.417 1.00 41.02 ? 605  1PE A C12   1 
HETATM 8245 C C22   . 1PE G 5 .   ? -26.679 102.408 50.156 1.00 47.94 ? 605  1PE A C22   1 
HETATM 8246 O OH3   . 1PE G 5 .   ? -27.826 103.089 49.603 1.00 56.61 ? 605  1PE A OH3   1 
HETATM 8247 C C13   . 1PE G 5 .   ? -30.233 103.454 50.033 1.00 63.56 ? 605  1PE A C13   1 
HETATM 8248 C C23   . 1PE G 5 .   ? -29.092 102.451 49.786 1.00 57.36 ? 605  1PE A C23   1 
HETATM 8249 O OH4   . 1PE G 5 .   ? -31.111 102.929 51.041 1.00 58.29 ? 605  1PE A OH4   1 
HETATM 8250 C C14   . 1PE G 5 .   ? -32.109 103.620 53.131 1.00 53.74 ? 605  1PE A C14   1 
HETATM 8251 C C24   . 1PE G 5 .   ? -32.013 103.867 51.633 1.00 59.62 ? 605  1PE A C24   1 
HETATM 8252 O OH5   . 1PE G 5 .   ? -32.385 104.807 53.877 1.00 48.09 ? 605  1PE A OH5   1 
HETATM 8253 C C15   . 1PE G 5 .   ? -31.697 107.008 54.679 1.00 35.44 ? 605  1PE A C15   1 
HETATM 8254 C C25   . 1PE G 5 .   ? -31.356 105.785 53.854 1.00 41.43 ? 605  1PE A C25   1 
HETATM 8255 O OH6   . 1PE G 5 .   ? -32.390 107.974 53.886 1.00 38.18 ? 605  1PE A OH6   1 
HETATM 8256 C C16   . 1PE G 5 .   ? -32.790 110.197 53.071 1.00 41.70 ? 605  1PE A C16   1 
HETATM 8257 C C26   . 1PE G 5 .   ? -31.874 109.298 53.880 1.00 38.66 ? 605  1PE A C26   1 
HETATM 8258 O OH7   . 1PE G 5 .   ? -32.846 109.862 51.652 1.00 42.33 ? 605  1PE A OH7   1 
HETATM 8259 O O1    . PE4 H 6 .   ? -20.713 95.213  60.227 1.00 45.77 ? 606  PE4 A O1    1 
HETATM 8260 C C1    . PE4 H 6 .   ? -20.703 94.032  61.042 1.00 44.84 ? 606  PE4 A C1    1 
HETATM 8261 C C2    . PE4 H 6 .   ? -21.934 93.885  61.901 1.00 43.33 ? 606  PE4 A C2    1 
HETATM 8262 O O2    . PE4 H 6 .   ? -21.709 94.570  63.120 1.00 41.23 ? 606  PE4 A O2    1 
HETATM 8263 C C3    . PE4 H 6 .   ? -21.217 93.744  64.176 1.00 43.89 ? 606  PE4 A C3    1 
HETATM 8264 C C4    . PE4 H 6 .   ? -21.111 94.537  65.466 1.00 48.08 ? 606  PE4 A C4    1 
HETATM 8265 O O3    . PE4 H 6 .   ? -20.637 95.877  65.219 1.00 44.76 ? 606  PE4 A O3    1 
HETATM 8266 C C5    . PE4 H 6 .   ? -20.297 96.602  66.415 1.00 45.81 ? 606  PE4 A C5    1 
HETATM 8267 C C6    . PE4 H 6 .   ? -19.635 97.949  66.109 1.00 41.49 ? 606  PE4 A C6    1 
HETATM 8268 O O4    . PE4 H 6 .   ? -20.356 98.607  65.067 1.00 41.74 ? 606  PE4 A O4    1 
HETATM 8269 C C7    . PE4 H 6 .   ? -20.004 99.972  64.816 1.00 43.77 ? 606  PE4 A C7    1 
HETATM 8270 C C8    . PE4 H 6 .   ? -20.870 100.531 63.665 1.00 45.37 ? 606  PE4 A C8    1 
HETATM 8271 O O5    . PE4 H 6 .   ? -20.685 99.782  62.456 1.00 47.19 ? 606  PE4 A O5    1 
HETATM 8272 C C9    . PE4 H 6 .   ? -21.740 99.870  61.489 1.00 50.22 ? 606  PE4 A C9    1 
HETATM 8273 C C10   . PE4 H 6 .   ? -21.673 98.712  60.457 1.00 42.18 ? 606  PE4 A C10   1 
HETATM 8274 O O6    . PE4 H 6 .   ? -22.704 97.728  60.633 1.00 48.38 ? 606  PE4 A O6    1 
HETATM 8275 C C11   . PE4 H 6 .   ? -23.322 97.230  59.419 1.00 53.08 ? 606  PE4 A C11   1 
HETATM 8276 C C12   . PE4 H 6 .   ? -24.213 98.322  58.774 1.00 49.77 ? 606  PE4 A C12   1 
HETATM 8277 O O7    . PE4 H 6 .   ? -24.520 98.137  57.381 1.00 51.04 ? 606  PE4 A O7    1 
HETATM 8278 C C13   . PE4 H 6 .   ? -24.825 99.376  56.688 1.00 51.92 ? 606  PE4 A C13   1 
HETATM 8279 C C14   . PE4 H 6 .   ? -23.553 100.153 56.204 1.00 53.87 ? 606  PE4 A C14   1 
HETATM 8280 O O8    . PE4 H 6 .   ? -23.843 101.544 55.971 1.00 66.29 ? 606  PE4 A O8    1 
HETATM 8281 C C15   . PE4 H 6 .   ? -22.789 102.368 55.439 1.00 49.45 ? 606  PE4 A C15   1 
HETATM 8282 C C16   . PE4 H 6 .   ? -23.248 103.602 54.696 1.00 43.00 ? 606  PE4 A C16   1 
HETATM 8283 N N     . NO3 I 3 .   ? -24.001 97.662  28.758 1.00 72.87 ? 607  NO3 A N     1 
HETATM 8284 O O1    . NO3 I 3 .   ? -24.477 98.581  29.448 1.00 66.85 ? 607  NO3 A O1    1 
HETATM 8285 O O2    . NO3 I 3 .   ? -24.540 96.543  28.741 1.00 75.75 ? 607  NO3 A O2    1 
HETATM 8286 O O3    . NO3 I 3 .   ? -22.999 97.861  28.071 1.00 57.76 ? 607  NO3 A O3    1 
HETATM 8287 C C1    . PEG J 4 .   ? -6.800  77.297  41.696 1.00 52.98 ? 608  PEG A C1    1 
HETATM 8288 O O1    . PEG J 4 .   ? -7.402  77.008  40.410 1.00 50.93 ? 608  PEG A O1    1 
HETATM 8289 C C2    . PEG J 4 .   ? -7.371  78.539  42.350 1.00 41.61 ? 608  PEG A C2    1 
HETATM 8290 O O2    . PEG J 4 .   ? -8.797  78.397  42.449 1.00 58.33 ? 608  PEG A O2    1 
HETATM 8291 C C3    . PEG J 4 .   ? -9.456  79.122  43.497 1.00 44.45 ? 608  PEG A C3    1 
HETATM 8292 C C4    . PEG J 4 .   ? -10.739 78.395  43.930 1.00 58.41 ? 608  PEG A C4    1 
HETATM 8293 O O4    . PEG J 4 .   ? -11.639 77.951  42.872 1.00 48.94 ? 608  PEG A O4    1 
HETATM 8294 C C1    . EOL K 7 .   ? -11.065 102.109 49.146 1.00 27.70 ? 609  EOL A C1    1 
HETATM 8295 O O1    . EOL K 7 .   ? -9.017  99.063  49.159 1.00 27.18 ? 609  EOL A O1    1 
HETATM 8296 C C2    . EOL K 7 .   ? -10.099 103.092 49.373 1.00 29.69 ? 609  EOL A C2    1 
HETATM 8297 O O2    . EOL K 7 .   ? -11.513 99.697  48.868 1.00 29.03 ? 609  EOL A O2    1 
HETATM 8298 C C3    . EOL K 7 .   ? -10.696 100.761 49.124 1.00 26.67 ? 609  EOL A C3    1 
HETATM 8299 C C4    . EOL K 7 .   ? -8.792  102.693 49.592 1.00 29.37 ? 609  EOL A C4    1 
HETATM 8300 C C5    . EOL K 7 .   ? -9.363  100.380 49.317 1.00 26.78 ? 609  EOL A C5    1 
HETATM 8301 C C6    . EOL K 7 .   ? -8.406  101.355 49.548 1.00 28.51 ? 609  EOL A C6    1 
HETATM 8302 C C7    . EOL K 7 .   ? -10.467 104.565 49.475 1.00 33.81 ? 609  EOL A C7    1 
HETATM 8303 C C8    . EOL K 7 .   ? -11.348 105.078 48.432 1.00 41.07 ? 609  EOL A C8    1 
HETATM 8304 C C9    . EOL K 7 .   ? -11.933 106.236 48.473 1.00 45.33 ? 609  EOL A C9    1 
HETATM 8305 C C10   . EOL K 7 .   ? -12.811 99.924  48.362 1.00 30.40 ? 609  EOL A C10   1 
HETATM 8306 N N     . NO3 L 3 .   ? 11.533  101.364 52.127 1.00 69.84 ? 610  NO3 A N     1 
HETATM 8307 O O1    . NO3 L 3 .   ? 11.460  102.042 51.095 1.00 71.28 ? 610  NO3 A O1    1 
HETATM 8308 O O2    . NO3 L 3 .   ? 10.605  100.595 52.416 1.00 58.40 ? 610  NO3 A O2    1 
HETATM 8309 O O3    . NO3 L 3 .   ? 12.507  101.493 52.892 1.00 65.25 ? 610  NO3 A O3    1 
HETATM 8310 N N     . NO3 M 3 .   ? 13.718  90.007  34.829 1.00 51.99 ? 601  NO3 B N     1 
HETATM 8311 O O1    . NO3 M 3 .   ? 13.143  89.002  35.248 1.00 47.11 ? 601  NO3 B O1    1 
HETATM 8312 O O2    . NO3 M 3 .   ? 14.787  89.886  34.245 1.00 54.18 ? 601  NO3 B O2    1 
HETATM 8313 O O3    . NO3 M 3 .   ? 13.201  91.125  34.946 1.00 59.43 ? 601  NO3 B O3    1 
HETATM 8314 P PA    . FAD N 2 .   ? 24.214  81.187  53.669 1.00 21.01 ? 602  FAD B PA    1 
HETATM 8315 O O1A   . FAD N 2 .   ? 25.230  80.486  54.511 1.00 18.38 ? 602  FAD B O1A   1 
HETATM 8316 O O2A   . FAD N 2 .   ? 24.134  80.797  52.219 1.00 18.67 ? 602  FAD B O2A   1 
HETATM 8317 O O5B   . FAD N 2 .   ? 22.721  81.004  54.249 1.00 21.66 ? 602  FAD B O5B   1 
HETATM 8318 C C5B   . FAD N 2 .   ? 22.489  81.002  55.695 1.00 21.54 ? 602  FAD B C5B   1 
HETATM 8319 C C4B   . FAD N 2 .   ? 21.473  79.931  56.056 1.00 21.26 ? 602  FAD B C4B   1 
HETATM 8320 O O4B   . FAD N 2 .   ? 20.187  80.327  55.529 1.00 20.22 ? 602  FAD B O4B   1 
HETATM 8321 C C3B   . FAD N 2 .   ? 21.734  78.525  55.492 1.00 21.90 ? 602  FAD B C3B   1 
HETATM 8322 O O3B   . FAD N 2 .   ? 22.574  77.763  56.365 1.00 23.22 ? 602  FAD B O3B   1 
HETATM 8323 C C2B   . FAD N 2 .   ? 20.322  77.951  55.371 1.00 23.22 ? 602  FAD B C2B   1 
HETATM 8324 O O2B   . FAD N 2 .   ? 19.851  77.511  56.631 1.00 23.86 ? 602  FAD B O2B   1 
HETATM 8325 C C1B   . FAD N 2 .   ? 19.541  79.190  54.952 1.00 23.34 ? 602  FAD B C1B   1 
HETATM 8326 N N9A   . FAD N 2 .   ? 19.491  79.391  53.502 1.00 22.42 ? 602  FAD B N9A   1 
HETATM 8327 C C8A   . FAD N 2 .   ? 20.370  80.170  52.787 1.00 23.04 ? 602  FAD B C8A   1 
HETATM 8328 N N7A   . FAD N 2 .   ? 20.067  80.215  51.503 1.00 21.21 ? 602  FAD B N7A   1 
HETATM 8329 C C5A   . FAD N 2 .   ? 18.905  79.462  51.393 1.00 20.50 ? 602  FAD B C5A   1 
HETATM 8330 C C6A   . FAD N 2 .   ? 18.094  79.177  50.282 1.00 21.25 ? 602  FAD B C6A   1 
HETATM 8331 N N6A   . FAD N 2 .   ? 18.364  79.675  49.074 1.00 20.18 ? 602  FAD B N6A   1 
HETATM 8332 N N1A   . FAD N 2 .   ? 16.986  78.414  50.478 1.00 18.53 ? 602  FAD B N1A   1 
HETATM 8333 C C2A   . FAD N 2 .   ? 16.777  77.936  51.715 1.00 22.93 ? 602  FAD B C2A   1 
HETATM 8334 N N3A   . FAD N 2 .   ? 17.456  78.176  52.845 1.00 21.24 ? 602  FAD B N3A   1 
HETATM 8335 C C4A   . FAD N 2 .   ? 18.525  78.959  52.614 1.00 21.21 ? 602  FAD B C4A   1 
HETATM 8336 N N1    . FAD N 2 .   ? 26.050  88.469  59.655 1.00 19.30 ? 602  FAD B N1    1 
HETATM 8337 C C2    . FAD N 2 .   ? 25.257  89.567  59.518 1.00 20.66 ? 602  FAD B C2    1 
HETATM 8338 O O2    . FAD N 2 .   ? 24.044  89.485  59.236 1.00 18.15 ? 602  FAD B O2    1 
HETATM 8339 N N3    . FAD N 2 .   ? 25.799  90.825  59.594 1.00 21.49 ? 602  FAD B N3    1 
HETATM 8340 C C4    . FAD N 2 .   ? 27.143  91.032  59.846 1.00 21.84 ? 602  FAD B C4    1 
HETATM 8341 O O4    . FAD N 2 .   ? 27.546  92.170  59.923 1.00 21.03 ? 602  FAD B O4    1 
HETATM 8342 C C4X   . FAD N 2 .   ? 27.980  89.911  60.079 1.00 22.72 ? 602  FAD B C4X   1 
HETATM 8343 N N5    . FAD N 2 .   ? 29.280  90.090  60.320 1.00 22.36 ? 602  FAD B N5    1 
HETATM 8344 C C5X   . FAD N 2 .   ? 30.022  88.956  60.605 1.00 24.37 ? 602  FAD B C5X   1 
HETATM 8345 C C6    . FAD N 2 .   ? 31.386  89.100  60.964 1.00 23.08 ? 602  FAD B C6    1 
HETATM 8346 C C7    . FAD N 2 .   ? 32.193  88.018  61.251 1.00 22.41 ? 602  FAD B C7    1 
HETATM 8347 C C7M   . FAD N 2 .   ? 33.655  88.231  61.543 1.00 21.61 ? 602  FAD B C7M   1 
HETATM 8348 C C8    . FAD N 2 .   ? 31.618  86.727  61.302 1.00 21.74 ? 602  FAD B C8    1 
HETATM 8349 C C8M   . FAD N 2 .   ? 32.435  85.517  61.713 1.00 24.05 ? 602  FAD B C8M   1 
HETATM 8350 C C9    . FAD N 2 .   ? 30.286  86.557  60.899 1.00 23.09 ? 602  FAD B C9    1 
HETATM 8351 C C9A   . FAD N 2 .   ? 29.457  87.648  60.573 1.00 22.88 ? 602  FAD B C9A   1 
HETATM 8352 N N10   . FAD N 2 .   ? 28.111  87.516  60.201 1.00 22.07 ? 602  FAD B N10   1 
HETATM 8353 C C10   . FAD N 2 .   ? 27.325  88.634  59.963 1.00 21.21 ? 602  FAD B C10   1 
HETATM 8354 C "C1'" . FAD N 2 .   ? 27.449  86.202  60.104 1.00 24.51 ? 602  FAD B "C1'" 1 
HETATM 8355 C "C2'" . FAD N 2 .   ? 27.555  85.556  58.699 1.00 24.98 ? 602  FAD B "C2'" 1 
HETATM 8356 O "O2'" . FAD N 2 .   ? 28.912  85.333  58.368 1.00 27.80 ? 602  FAD B "O2'" 1 
HETATM 8357 C "C3'" . FAD N 2 .   ? 26.929  86.363  57.553 1.00 22.71 ? 602  FAD B "C3'" 1 
HETATM 8358 O "O3'" . FAD N 2 .   ? 25.576  86.606  57.862 1.00 22.30 ? 602  FAD B "O3'" 1 
HETATM 8359 C "C4'" . FAD N 2 .   ? 26.981  85.681  56.181 1.00 23.49 ? 602  FAD B "C4'" 1 
HETATM 8360 O "O4'" . FAD N 2 .   ? 26.667  86.626  55.145 1.00 20.83 ? 602  FAD B "O4'" 1 
HETATM 8361 C "C5'" . FAD N 2 .   ? 26.022  84.512  56.076 1.00 21.90 ? 602  FAD B "C5'" 1 
HETATM 8362 O "O5'" . FAD N 2 .   ? 26.439  83.579  55.036 1.00 20.02 ? 602  FAD B "O5'" 1 
HETATM 8363 P P     . FAD N 2 .   ? 25.781  83.659  53.580 1.00 20.35 ? 602  FAD B P     1 
HETATM 8364 O O1P   . FAD N 2 .   ? 25.427  85.078  53.277 1.00 20.04 ? 602  FAD B O1P   1 
HETATM 8365 O O2P   . FAD N 2 .   ? 26.708  82.866  52.671 1.00 19.95 ? 602  FAD B O2P   1 
HETATM 8366 O O3P   . FAD N 2 .   ? 24.436  82.769  53.781 1.00 21.18 ? 602  FAD B O3P   1 
HETATM 8367 N N     . NO3 O 3 .   ? 24.489  68.671  32.379 1.00 45.31 ? 603  NO3 B N     1 
HETATM 8368 O O1    . NO3 O 3 .   ? 24.852  67.543  32.004 1.00 54.25 ? 603  NO3 B O1    1 
HETATM 8369 O O2    . NO3 O 3 .   ? 25.219  69.361  33.103 1.00 53.50 ? 603  NO3 B O2    1 
HETATM 8370 O O3    . NO3 O 3 .   ? 23.390  69.096  32.069 1.00 44.24 ? 603  NO3 B O3    1 
HETATM 8371 N N     . NO3 P 3 .   ? 3.318   66.573  42.609 1.00 64.75 ? 604  NO3 B N     1 
HETATM 8372 O O1    . NO3 P 3 .   ? 4.358   66.117  43.120 1.00 54.90 ? 604  NO3 B O1    1 
HETATM 8373 O O2    . NO3 P 3 .   ? 3.281   66.851  41.415 1.00 67.13 ? 604  NO3 B O2    1 
HETATM 8374 O O3    . NO3 P 3 .   ? 2.303   66.713  43.289 1.00 70.76 ? 604  NO3 B O3    1 
HETATM 8375 N N     . NO3 Q 3 .   ? 51.529  100.414 69.920 1.00 68.86 ? 605  NO3 B N     1 
HETATM 8376 O O1    . NO3 Q 3 .   ? 50.810  100.956 70.725 1.00 62.88 ? 605  NO3 B O1    1 
HETATM 8377 O O2    . NO3 Q 3 .   ? 51.988  101.054 68.970 1.00 55.54 ? 605  NO3 B O2    1 
HETATM 8378 O O3    . NO3 Q 3 .   ? 51.797  99.227  70.075 1.00 67.51 ? 605  NO3 B O3    1 
HETATM 8379 C C1    . PEG R 4 .   ? 9.832   71.828  70.930 1.00 49.29 ? 606  PEG B C1    1 
HETATM 8380 O O1    . PEG R 4 .   ? 10.327  71.021  72.042 1.00 46.38 ? 606  PEG B O1    1 
HETATM 8381 C C2    . PEG R 4 .   ? 10.920  72.451  70.089 1.00 36.81 ? 606  PEG B C2    1 
HETATM 8382 O O2    . PEG R 4 .   ? 12.071  71.605  70.147 1.00 49.05 ? 606  PEG B O2    1 
HETATM 8383 C C3    . PEG R 4 .   ? 12.987  71.640  69.039 1.00 40.71 ? 606  PEG B C3    1 
HETATM 8384 C C4    . PEG R 4 .   ? 13.279  70.213  68.562 1.00 45.66 ? 606  PEG B C4    1 
HETATM 8385 O O4    . PEG R 4 .   ? 13.974  69.344  69.493 1.00 44.48 ? 606  PEG B O4    1 
HETATM 8386 O OH2   . 1PE S 5 .   ? 35.361  79.919  52.073 1.00 56.41 ? 607  1PE B OH2   1 
HETATM 8387 C C12   . 1PE S 5 .   ? 35.018  81.277  52.400 1.00 51.44 ? 607  1PE B C12   1 
HETATM 8388 C C22   . 1PE S 5 .   ? 35.779  82.309  51.613 1.00 53.49 ? 607  1PE B C22   1 
HETATM 8389 O OH3   . 1PE S 5 .   ? 34.944  82.971  50.661 1.00 55.12 ? 607  1PE B OH3   1 
HETATM 8390 C C13   . 1PE S 5 .   ? 34.247  83.218  48.378 1.00 55.94 ? 607  1PE B C13   1 
HETATM 8391 C C23   . 1PE S 5 .   ? 35.292  82.693  49.305 1.00 53.53 ? 607  1PE B C23   1 
HETATM 8392 O OH4   . 1PE S 5 .   ? 34.017  82.328  47.277 1.00 55.33 ? 607  1PE B OH4   1 
HETATM 8393 C C14   . 1PE S 5 .   ? 32.487  80.443  46.976 1.00 50.16 ? 607  1PE B C14   1 
HETATM 8394 C C24   . 1PE S 5 .   ? 33.729  80.982  47.640 1.00 48.81 ? 607  1PE B C24   1 
HETATM 8395 O OH5   . 1PE S 5 .   ? 32.551  79.013  47.023 1.00 54.21 ? 607  1PE B OH5   1 
HETATM 8396 C C15   . 1PE S 5 .   ? 32.035  77.231  48.678 1.00 59.67 ? 607  1PE B C15   1 
HETATM 8397 C C25   . 1PE S 5 .   ? 31.531  78.370  47.794 1.00 61.19 ? 607  1PE B C25   1 
HETATM 8398 O OH6   . 1PE S 5 .   ? 31.122  77.066  49.766 1.00 55.62 ? 607  1PE B OH6   1 
HETATM 8399 C C16   . 1PE S 5 .   ? 31.934  77.824  51.859 1.00 55.34 ? 607  1PE B C16   1 
HETATM 8400 C C26   . 1PE S 5 .   ? 31.725  76.654  50.976 1.00 53.10 ? 607  1PE B C26   1 
HETATM 8401 O OH7   . 1PE S 5 .   ? 31.692  77.533  53.233 1.00 55.48 ? 607  1PE B OH7   1 
HETATM 8402 C C1    . EOL T 7 .   ? 27.942  89.058  63.573 1.00 28.99 ? 608  EOL B C1    1 
HETATM 8403 O O1    . EOL T 7 .   ? 24.469  87.988  63.498 1.00 27.38 ? 608  EOL B O1    1 
HETATM 8404 C C2    . EOL T 7 .   ? 27.794  90.429  63.394 1.00 29.29 ? 608  EOL B C2    1 
HETATM 8405 O O2    . EOL T 7 .   ? 26.821  86.873  63.819 1.00 25.14 ? 608  EOL B O2    1 
HETATM 8406 C C3    . EOL T 7 .   ? 26.829  88.234  63.619 1.00 26.92 ? 608  EOL B C3    1 
HETATM 8407 C C4    . EOL T 7 .   ? 26.531  90.945  63.212 1.00 29.52 ? 608  EOL B C4    1 
HETATM 8408 C C5    . EOL T 7 .   ? 25.557  88.789  63.420 1.00 23.95 ? 608  EOL B C5    1 
HETATM 8409 C C6    . EOL T 7 .   ? 25.402  90.139  63.209 1.00 27.05 ? 608  EOL B C6    1 
HETATM 8410 C C7    . EOL T 7 .   ? 29.002  91.340  63.318 1.00 35.49 ? 608  EOL B C7    1 
HETATM 8411 C C8    . EOL T 7 .   ? 30.029  91.174  64.321 1.00 39.40 ? 608  EOL B C8    1 
HETATM 8412 C C9    . EOL T 7 .   ? 31.084  91.920  64.362 1.00 46.98 ? 608  EOL B C9    1 
HETATM 8413 C C10   . EOL T 7 .   ? 27.992  86.166  64.134 1.00 24.74 ? 608  EOL B C10   1 
HETATM 8414 O O     . HOH U 8 .   ? -22.353 93.103  29.869 1.00 40.00 ? 701  HOH A O     1 
HETATM 8415 O O     . HOH U 8 .   ? 4.526   116.459 70.087 1.00 43.60 ? 702  HOH A O     1 
HETATM 8416 O O     . HOH U 8 .   ? -26.738 102.394 39.487 1.00 28.98 ? 703  HOH A O     1 
HETATM 8417 O O     . HOH U 8 .   ? -4.519  67.588  56.785 1.00 47.24 ? 704  HOH A O     1 
HETATM 8418 O O     . HOH U 8 .   ? -15.391 73.464  54.684 1.00 46.64 ? 705  HOH A O     1 
HETATM 8419 O O     . HOH U 8 .   ? -14.198 73.679  78.004 1.00 40.06 ? 706  HOH A O     1 
HETATM 8420 O O     . HOH U 8 .   ? 1.691   93.834  36.950 1.00 22.35 ? 707  HOH A O     1 
HETATM 8421 O O     . HOH U 8 .   ? -21.206 122.685 32.779 1.00 43.17 ? 708  HOH A O     1 
HETATM 8422 O O     . HOH U 8 .   ? -11.536 92.031  75.822 1.00 34.28 ? 709  HOH A O     1 
HETATM 8423 O O     . HOH U 8 .   ? 14.159  102.366 54.539 1.00 49.41 ? 710  HOH A O     1 
HETATM 8424 O O     . HOH U 8 .   ? -32.796 110.373 49.209 1.00 44.51 ? 711  HOH A O     1 
HETATM 8425 O O     . HOH U 8 .   ? -12.290 124.330 34.238 1.00 36.43 ? 712  HOH A O     1 
HETATM 8426 O O     . HOH U 8 .   ? -28.230 114.355 37.611 1.00 46.78 ? 713  HOH A O     1 
HETATM 8427 O O     . HOH U 8 .   ? -22.652 122.188 35.209 1.00 46.64 ? 714  HOH A O     1 
HETATM 8428 O O     . HOH U 8 .   ? 3.608   96.340  51.073 1.00 44.99 ? 715  HOH A O     1 
HETATM 8429 O O     . HOH U 8 .   ? -21.416 68.568  59.718 1.00 45.96 ? 716  HOH A O     1 
HETATM 8430 O O     . HOH U 8 .   ? -21.858 121.496 30.343 1.00 48.42 ? 717  HOH A O     1 
HETATM 8431 O O     . HOH U 8 .   ? 6.149   124.280 53.155 1.00 41.94 ? 718  HOH A O     1 
HETATM 8432 O O     . HOH U 8 .   ? 14.537  121.336 43.097 1.00 40.76 ? 719  HOH A O     1 
HETATM 8433 O O     . HOH U 8 .   ? -13.097 101.442 58.134 1.00 47.04 ? 720  HOH A O     1 
HETATM 8434 O O     . HOH U 8 .   ? -7.084  90.351  76.244 1.00 37.63 ? 721  HOH A O     1 
HETATM 8435 O O     . HOH U 8 .   ? -24.476 111.110 30.913 1.00 43.85 ? 722  HOH A O     1 
HETATM 8436 O O     . HOH U 8 .   ? 12.563  96.305  65.528 1.00 24.11 ? 723  HOH A O     1 
HETATM 8437 O O     . HOH U 8 .   ? -10.897 97.373  31.539 1.00 29.63 ? 724  HOH A O     1 
HETATM 8438 O O     . HOH U 8 .   ? 5.888   99.584  32.495 1.00 26.19 ? 725  HOH A O     1 
HETATM 8439 O O     . HOH U 8 .   ? -29.190 79.519  43.060 1.00 48.10 ? 726  HOH A O     1 
HETATM 8440 O O     . HOH U 8 .   ? -26.626 91.946  50.520 1.00 27.25 ? 727  HOH A O     1 
HETATM 8441 O O     . HOH U 8 .   ? -11.506 110.282 53.947 1.00 34.34 ? 728  HOH A O     1 
HETATM 8442 O O     . HOH U 8 .   ? -25.565 90.919  39.828 1.00 37.03 ? 729  HOH A O     1 
HETATM 8443 O O     . HOH U 8 .   ? -29.281 88.183  71.520 1.00 44.92 ? 730  HOH A O     1 
HETATM 8444 O O     . HOH U 8 .   ? 5.450   91.041  62.044 1.00 18.82 ? 731  HOH A O     1 
HETATM 8445 O O     . HOH U 8 .   ? 14.427  124.538 49.999 1.00 42.89 ? 732  HOH A O     1 
HETATM 8446 O O     . HOH U 8 .   ? -10.898 108.117 58.623 1.00 24.56 ? 733  HOH A O     1 
HETATM 8447 O O     . HOH U 8 .   ? -31.492 102.440 39.819 1.00 42.82 ? 734  HOH A O     1 
HETATM 8448 O O     . HOH U 8 .   ? -1.411  80.430  33.943 1.00 31.78 ? 735  HOH A O     1 
HETATM 8449 O O     . HOH U 8 .   ? -0.003  103.596 28.327 1.00 27.86 ? 736  HOH A O     1 
HETATM 8450 O O     . HOH U 8 .   ? -4.651  99.192  60.684 1.00 18.13 ? 737  HOH A O     1 
HETATM 8451 O O     . HOH U 8 .   ? -7.081  123.052 36.895 1.00 46.39 ? 738  HOH A O     1 
HETATM 8452 O O     . HOH U 8 .   ? -16.665 104.751 27.765 1.00 36.75 ? 739  HOH A O     1 
HETATM 8453 O O     . HOH U 8 .   ? -7.151  123.794 40.914 1.00 31.25 ? 740  HOH A O     1 
HETATM 8454 O O     . HOH U 8 .   ? -27.168 70.484  54.493 1.00 42.42 ? 741  HOH A O     1 
HETATM 8455 O O     . HOH U 8 .   ? -12.261 72.303  74.910 1.00 38.24 ? 742  HOH A O     1 
HETATM 8456 O O     . HOH U 8 .   ? 8.846   106.654 63.047 1.00 22.44 ? 743  HOH A O     1 
HETATM 8457 O O     . HOH U 8 .   ? -8.865  123.606 38.799 1.00 36.18 ? 744  HOH A O     1 
HETATM 8458 O O     . HOH U 8 .   ? -13.501 109.939 56.068 1.00 26.53 ? 745  HOH A O     1 
HETATM 8459 O O     . HOH U 8 .   ? 3.016   112.387 76.868 1.00 36.99 ? 746  HOH A O     1 
HETATM 8460 O O     . HOH U 8 .   ? 3.702   72.760  36.519 1.00 51.36 ? 747  HOH A O     1 
HETATM 8461 O O     . HOH U 8 .   ? -29.762 89.770  45.669 1.00 42.58 ? 748  HOH A O     1 
HETATM 8462 O O     . HOH U 8 .   ? 10.463  109.196 53.841 1.00 33.31 ? 749  HOH A O     1 
HETATM 8463 O O     . HOH U 8 .   ? -15.322 91.428  57.227 1.00 20.39 ? 750  HOH A O     1 
HETATM 8464 O O     . HOH U 8 .   ? -3.632  95.973  79.788 1.00 28.54 ? 751  HOH A O     1 
HETATM 8465 O O     . HOH U 8 .   ? 5.738   89.023  78.427 1.00 34.84 ? 752  HOH A O     1 
HETATM 8466 O O     . HOH U 8 .   ? -11.185 112.395 50.700 1.00 28.69 ? 753  HOH A O     1 
HETATM 8467 O O     . HOH U 8 .   ? -10.012 121.171 28.034 1.00 41.78 ? 754  HOH A O     1 
HETATM 8468 O O     . HOH U 8 .   ? 0.292   107.880 26.377 1.00 47.87 ? 755  HOH A O     1 
HETATM 8469 O O     . HOH U 8 .   ? -16.747 128.534 42.775 1.00 47.69 ? 756  HOH A O     1 
HETATM 8470 O O     . HOH U 8 .   ? -22.560 90.319  48.558 1.00 33.28 ? 757  HOH A O     1 
HETATM 8471 O O     . HOH U 8 .   ? -28.489 85.216  56.024 1.00 27.71 ? 758  HOH A O     1 
HETATM 8472 O O     . HOH U 8 .   ? -25.290 101.350 53.810 1.00 37.62 ? 759  HOH A O     1 
HETATM 8473 O O     . HOH U 8 .   ? -0.475  94.375  38.749 1.00 25.06 ? 760  HOH A O     1 
HETATM 8474 O O     . HOH U 8 .   ? 15.226  120.341 48.033 1.00 38.78 ? 761  HOH A O     1 
HETATM 8475 O O     . HOH U 8 .   ? -9.378  115.321 67.135 1.00 38.57 ? 762  HOH A O     1 
HETATM 8476 O O     . HOH U 8 .   ? -12.305 107.258 29.672 1.00 49.90 ? 763  HOH A O     1 
HETATM 8477 O O     . HOH U 8 .   ? -25.760 101.965 35.026 1.00 45.50 ? 764  HOH A O     1 
HETATM 8478 O O     . HOH U 8 .   ? -29.375 95.392  33.743 1.00 46.84 ? 765  HOH A O     1 
HETATM 8479 O O     . HOH U 8 .   ? -11.741 76.325  78.075 1.00 30.24 ? 766  HOH A O     1 
HETATM 8480 O O     . HOH U 8 .   ? 8.336   108.363 55.227 1.00 42.88 ? 767  HOH A O     1 
HETATM 8481 O O     . HOH U 8 .   ? 1.570   99.623  48.724 1.00 39.12 ? 768  HOH A O     1 
HETATM 8482 O O     . HOH U 8 .   ? 14.497  104.778 49.759 1.00 23.38 ? 769  HOH A O     1 
HETATM 8483 O O     . HOH U 8 .   ? -8.103  120.643 58.127 1.00 35.29 ? 770  HOH A O     1 
HETATM 8484 O O     . HOH U 8 .   ? -5.419  112.701 46.308 1.00 41.47 ? 771  HOH A O     1 
HETATM 8485 O O     . HOH U 8 .   ? 3.798   94.284  74.631 1.00 36.25 ? 772  HOH A O     1 
HETATM 8486 O O     . HOH U 8 .   ? -10.248 105.648 75.980 1.00 48.16 ? 773  HOH A O     1 
HETATM 8487 O O     . HOH U 8 .   ? -10.317 89.179  75.849 1.00 43.33 ? 774  HOH A O     1 
HETATM 8488 O O     . HOH U 8 .   ? 6.350   110.827 70.915 1.00 23.03 ? 775  HOH A O     1 
HETATM 8489 O O     . HOH U 8 .   ? -2.662  92.248  49.054 1.00 18.16 ? 776  HOH A O     1 
HETATM 8490 O O     . HOH U 8 .   ? -10.540 112.194 70.977 1.00 42.19 ? 777  HOH A O     1 
HETATM 8491 O O     . HOH U 8 .   ? -7.193  114.455 46.447 1.00 33.93 ? 778  HOH A O     1 
HETATM 8492 O O     . HOH U 8 .   ? -6.392  79.883  36.939 1.00 31.60 ? 779  HOH A O     1 
HETATM 8493 O O     . HOH U 8 .   ? -19.428 86.087  76.017 1.00 25.10 ? 780  HOH A O     1 
HETATM 8494 O O     . HOH U 8 .   ? -7.712  72.526  70.538 1.00 22.91 ? 781  HOH A O     1 
HETATM 8495 O O     . HOH U 8 .   ? -30.053 94.127  48.882 1.00 38.69 ? 782  HOH A O     1 
HETATM 8496 O O     . HOH U 8 .   ? -25.486 94.758  56.632 1.00 38.10 ? 783  HOH A O     1 
HETATM 8497 O O     . HOH U 8 .   ? -13.164 66.663  57.774 1.00 40.67 ? 784  HOH A O     1 
HETATM 8498 O O     . HOH U 8 .   ? -4.840  122.281 37.965 1.00 27.93 ? 785  HOH A O     1 
HETATM 8499 O O     . HOH U 8 .   ? -15.729 69.767  58.244 1.00 37.41 ? 786  HOH A O     1 
HETATM 8500 O O     . HOH U 8 .   ? 5.134   98.715  79.377 1.00 37.44 ? 787  HOH A O     1 
HETATM 8501 O O     . HOH U 8 .   ? -5.253  72.256  74.264 1.00 49.75 ? 788  HOH A O     1 
HETATM 8502 O O     . HOH U 8 .   ? 8.344   101.312 77.791 1.00 36.78 ? 789  HOH A O     1 
HETATM 8503 O O     . HOH U 8 .   ? -1.574  69.213  53.423 1.00 25.44 ? 790  HOH A O     1 
HETATM 8504 O O     . HOH U 8 .   ? 7.299   108.357 70.653 1.00 24.63 ? 791  HOH A O     1 
HETATM 8505 O O     . HOH U 8 .   ? -7.942  78.371  76.570 1.00 33.12 ? 792  HOH A O     1 
HETATM 8506 O O     . HOH U 8 .   ? 7.276   92.595  58.197 1.00 37.90 ? 793  HOH A O     1 
HETATM 8507 O O     . HOH U 8 .   ? -30.495 88.915  57.230 1.00 39.07 ? 794  HOH A O     1 
HETATM 8508 O O     . HOH U 8 .   ? -23.502 76.930  50.845 1.00 34.12 ? 795  HOH A O     1 
HETATM 8509 O O     . HOH U 8 .   ? -4.483  115.186 74.145 1.00 46.34 ? 796  HOH A O     1 
HETATM 8510 O O     . HOH U 8 .   ? 3.387   125.022 34.512 1.00 39.35 ? 797  HOH A O     1 
HETATM 8511 O O     . HOH U 8 .   ? -17.690 123.779 30.320 1.00 44.22 ? 798  HOH A O     1 
HETATM 8512 O O     . HOH U 8 .   ? 4.646   114.093 50.822 1.00 26.16 ? 799  HOH A O     1 
HETATM 8513 O O     . HOH U 8 .   ? 0.721   107.938 61.602 1.00 18.88 ? 800  HOH A O     1 
HETATM 8514 O O     . HOH U 8 .   ? -6.609  128.344 41.765 1.00 49.79 ? 801  HOH A O     1 
HETATM 8515 O O     . HOH U 8 .   ? -8.994  71.758  54.567 1.00 23.65 ? 802  HOH A O     1 
HETATM 8516 O O     . HOH U 8 .   ? -13.225 111.181 37.938 1.00 27.73 ? 803  HOH A O     1 
HETATM 8517 O O     . HOH U 8 .   ? 10.432  113.970 40.275 1.00 27.34 ? 804  HOH A O     1 
HETATM 8518 O O     . HOH U 8 .   ? -9.701  71.768  61.079 1.00 20.90 ? 805  HOH A O     1 
HETATM 8519 O O     . HOH U 8 .   ? -31.426 80.083  57.753 1.00 44.18 ? 806  HOH A O     1 
HETATM 8520 O O     . HOH U 8 .   ? 0.918   80.511  40.766 1.00 16.69 ? 807  HOH A O     1 
HETATM 8521 O O     . HOH U 8 .   ? -8.803  100.602 39.167 1.00 37.63 ? 808  HOH A O     1 
HETATM 8522 O O     . HOH U 8 .   ? 11.326  105.006 80.261 1.00 50.64 ? 809  HOH A O     1 
HETATM 8523 O O     . HOH U 8 .   ? -13.505 122.859 46.767 1.00 32.15 ? 810  HOH A O     1 
HETATM 8524 O O     . HOH U 8 .   ? 8.088   106.770 51.716 1.00 41.89 ? 811  HOH A O     1 
HETATM 8525 O O     . HOH U 8 .   ? 6.728   122.868 63.119 1.00 44.77 ? 812  HOH A O     1 
HETATM 8526 O O     . HOH U 8 .   ? -18.880 90.291  32.289 1.00 32.36 ? 813  HOH A O     1 
HETATM 8527 O O     . HOH U 8 .   ? -28.680 102.184 46.355 1.00 46.98 ? 814  HOH A O     1 
HETATM 8528 O O     . HOH U 8 .   ? -3.844  86.109  34.944 1.00 22.55 ? 815  HOH A O     1 
HETATM 8529 O O     . HOH U 8 .   ? -6.300  96.509  79.075 1.00 39.45 ? 816  HOH A O     1 
HETATM 8530 O O     . HOH U 8 .   ? -10.212 84.737  57.914 1.00 26.36 ? 817  HOH A O     1 
HETATM 8531 O O     . HOH U 8 .   ? 6.186   91.910  75.493 1.00 29.22 ? 818  HOH A O     1 
HETATM 8532 O O     . HOH U 8 .   ? -12.920 69.762  68.300 1.00 47.57 ? 819  HOH A O     1 
HETATM 8533 O O     . HOH U 8 .   ? -15.963 122.043 48.072 1.00 26.83 ? 820  HOH A O     1 
HETATM 8534 O O     . HOH U 8 .   ? -16.243 80.299  42.008 1.00 46.37 ? 821  HOH A O     1 
HETATM 8535 O O     . HOH U 8 .   ? -7.715  113.520 26.975 1.00 44.98 ? 822  HOH A O     1 
HETATM 8536 O O     . HOH U 8 .   ? 9.003   81.430  64.233 1.00 18.16 ? 823  HOH A O     1 
HETATM 8537 O O     . HOH U 8 .   ? -10.023 84.520  36.868 1.00 27.80 ? 824  HOH A O     1 
HETATM 8538 O O     . HOH U 8 .   ? -4.591  83.079  34.386 1.00 39.19 ? 825  HOH A O     1 
HETATM 8539 O O     . HOH U 8 .   ? -15.689 103.054 67.533 1.00 32.04 ? 826  HOH A O     1 
HETATM 8540 O O     . HOH U 8 .   ? -7.000  93.656  28.357 1.00 30.86 ? 827  HOH A O     1 
HETATM 8541 O O     . HOH U 8 .   ? -16.639 89.640  54.658 1.00 20.42 ? 828  HOH A O     1 
HETATM 8542 O O     . HOH U 8 .   ? 1.047   105.779 63.236 1.00 16.77 ? 829  HOH A O     1 
HETATM 8543 O O     . HOH U 8 .   ? 4.083   75.318  33.974 1.00 32.04 ? 830  HOH A O     1 
HETATM 8544 O O     . HOH U 8 .   ? 7.466   89.793  68.065 1.00 15.94 ? 831  HOH A O     1 
HETATM 8545 O O     . HOH U 8 .   ? -4.165  108.021 57.651 1.00 18.84 ? 832  HOH A O     1 
HETATM 8546 O O     . HOH U 8 .   ? 4.953   84.643  56.209 1.00 35.18 ? 833  HOH A O     1 
HETATM 8547 O O     . HOH U 8 .   ? -15.631 84.002  45.654 1.00 20.20 ? 834  HOH A O     1 
HETATM 8548 O O     . HOH U 8 .   ? 3.804   80.986  70.843 1.00 17.39 ? 835  HOH A O     1 
HETATM 8549 O O     . HOH U 8 .   ? -10.897 104.525 73.608 1.00 25.74 ? 836  HOH A O     1 
HETATM 8550 O O     . HOH U 8 .   ? -17.429 126.699 37.324 1.00 45.79 ? 837  HOH A O     1 
HETATM 8551 O O     . HOH U 8 .   ? -1.961  120.438 34.607 1.00 31.25 ? 838  HOH A O     1 
HETATM 8552 O O     . HOH U 8 .   ? -10.875 91.054  51.036 1.00 21.41 ? 839  HOH A O     1 
HETATM 8553 O O     . HOH U 8 .   ? 5.654   107.959 29.959 1.00 32.39 ? 840  HOH A O     1 
HETATM 8554 O O     . HOH U 8 .   ? -9.238  87.727  50.153 1.00 22.26 ? 841  HOH A O     1 
HETATM 8555 O O     . HOH U 8 .   ? -19.701 113.575 55.986 1.00 40.93 ? 842  HOH A O     1 
HETATM 8556 O O     . HOH U 8 .   ? -15.827 104.509 39.369 1.00 26.32 ? 843  HOH A O     1 
HETATM 8557 O O     . HOH U 8 .   ? -17.541 89.857  69.856 1.00 22.29 ? 844  HOH A O     1 
HETATM 8558 O O     . HOH U 8 .   ? 0.840   127.079 39.312 1.00 52.30 ? 845  HOH A O     1 
HETATM 8559 O O     . HOH U 8 .   ? -15.329 98.323  70.074 1.00 33.10 ? 846  HOH A O     1 
HETATM 8560 O O     . HOH U 8 .   ? 1.334   73.479  39.293 1.00 24.58 ? 847  HOH A O     1 
HETATM 8561 O O     . HOH U 8 .   ? 7.654   111.384 63.806 1.00 27.67 ? 848  HOH A O     1 
HETATM 8562 O O     . HOH U 8 .   ? 3.747   85.657  75.549 1.00 20.71 ? 849  HOH A O     1 
HETATM 8563 O O     . HOH U 8 .   ? -8.289  96.407  66.280 1.00 16.68 ? 850  HOH A O     1 
HETATM 8564 O O     . HOH U 8 .   ? 10.741  84.845  62.075 1.00 22.85 ? 851  HOH A O     1 
HETATM 8565 O O     . HOH U 8 .   ? -25.832 75.796  50.781 1.00 37.57 ? 852  HOH A O     1 
HETATM 8566 O O     . HOH U 8 .   ? -25.242 85.011  40.847 1.00 33.58 ? 853  HOH A O     1 
HETATM 8567 O O     . HOH U 8 .   ? -0.705  119.781 31.083 1.00 36.29 ? 854  HOH A O     1 
HETATM 8568 O O     . HOH U 8 .   ? -13.736 83.748  78.813 1.00 46.78 ? 855  HOH A O     1 
HETATM 8569 O O     . HOH U 8 .   ? -3.549  110.251 64.892 1.00 19.79 ? 856  HOH A O     1 
HETATM 8570 O O     . HOH U 8 .   ? -13.894 106.051 70.867 1.00 36.77 ? 857  HOH A O     1 
HETATM 8571 O O     . HOH U 8 .   ? 11.078  110.457 36.460 1.00 37.15 ? 858  HOH A O     1 
HETATM 8572 O O     . HOH U 8 .   ? 6.474   84.681  63.023 1.00 25.71 ? 859  HOH A O     1 
HETATM 8573 O O     . HOH U 8 .   ? -1.967  105.442 50.713 1.00 25.29 ? 860  HOH A O     1 
HETATM 8574 O O     . HOH U 8 .   ? -11.610 117.983 28.104 1.00 43.47 ? 861  HOH A O     1 
HETATM 8575 O O     . HOH U 8 .   ? 5.729   89.675  64.335 1.00 18.41 ? 862  HOH A O     1 
HETATM 8576 O O     . HOH U 8 .   ? -9.269  126.817 46.612 1.00 35.09 ? 863  HOH A O     1 
HETATM 8577 O O     . HOH U 8 .   ? -15.480 68.049  60.985 1.00 45.76 ? 864  HOH A O     1 
HETATM 8578 O O     . HOH U 8 .   ? -7.801  87.663  31.336 1.00 40.22 ? 865  HOH A O     1 
HETATM 8579 O O     . HOH U 8 .   ? 7.229   112.906 69.268 1.00 34.35 ? 866  HOH A O     1 
HETATM 8580 O O     . HOH U 8 .   ? -29.201 74.303  70.019 1.00 44.12 ? 867  HOH A O     1 
HETATM 8581 O O     . HOH U 8 .   ? -7.444  88.632  72.942 1.00 22.89 ? 868  HOH A O     1 
HETATM 8582 O O     . HOH U 8 .   ? 6.944   114.382 52.148 1.00 26.51 ? 869  HOH A O     1 
HETATM 8583 O O     . HOH U 8 .   ? 9.803   103.488 48.808 1.00 34.32 ? 870  HOH A O     1 
HETATM 8584 O O     . HOH U 8 .   ? -11.517 99.841  72.387 1.00 29.04 ? 871  HOH A O     1 
HETATM 8585 O O     . HOH U 8 .   ? 10.027  96.516  76.685 1.00 28.17 ? 872  HOH A O     1 
HETATM 8586 O O     . HOH U 8 .   ? -16.110 100.695 56.665 1.00 26.97 ? 873  HOH A O     1 
HETATM 8587 O O     . HOH U 8 .   ? -4.714  80.144  41.296 1.00 25.89 ? 874  HOH A O     1 
HETATM 8588 O O     . HOH U 8 .   ? -25.050 88.949  52.448 1.00 24.70 ? 875  HOH A O     1 
HETATM 8589 O O     . HOH U 8 .   ? -18.924 105.791 40.538 1.00 25.41 ? 876  HOH A O     1 
HETATM 8590 O O     . HOH U 8 .   ? -10.949 94.361  43.605 1.00 19.94 ? 877  HOH A O     1 
HETATM 8591 O O     . HOH U 8 .   ? 7.105   112.653 31.534 1.00 38.26 ? 878  HOH A O     1 
HETATM 8592 O O     . HOH U 8 .   ? -12.618 110.821 67.653 1.00 33.13 ? 879  HOH A O     1 
HETATM 8593 O O     . HOH U 8 .   ? -8.955  87.242  75.421 1.00 26.98 ? 880  HOH A O     1 
HETATM 8594 O O     . HOH U 8 .   ? -2.042  79.871  41.970 1.00 18.23 ? 881  HOH A O     1 
HETATM 8595 O O     . HOH U 8 .   ? -13.958 82.366  47.036 1.00 22.54 ? 882  HOH A O     1 
HETATM 8596 O O     . HOH U 8 .   ? -16.705 109.778 34.828 1.00 30.83 ? 883  HOH A O     1 
HETATM 8597 O O     . HOH U 8 .   ? -30.187 82.085  58.954 1.00 36.13 ? 884  HOH A O     1 
HETATM 8598 O O     . HOH U 8 .   ? -8.900  116.064 30.349 1.00 33.73 ? 885  HOH A O     1 
HETATM 8599 O O     . HOH U 8 .   ? -4.479  73.913  37.966 1.00 42.72 ? 886  HOH A O     1 
HETATM 8600 O O     . HOH U 8 .   ? -21.756 113.196 46.464 1.00 27.58 ? 887  HOH A O     1 
HETATM 8601 O O     . HOH U 8 .   ? -17.045 96.723  68.945 1.00 46.23 ? 888  HOH A O     1 
HETATM 8602 O O     . HOH U 8 .   ? -27.233 91.609  65.558 1.00 33.22 ? 889  HOH A O     1 
HETATM 8603 O O     . HOH U 8 .   ? -1.213  96.795  54.558 1.00 18.91 ? 890  HOH A O     1 
HETATM 8604 O O     . HOH U 8 .   ? -9.881  110.815 58.134 1.00 25.82 ? 891  HOH A O     1 
HETATM 8605 O O     . HOH U 8 .   ? -1.582  96.565  50.549 1.00 18.69 ? 892  HOH A O     1 
HETATM 8606 O O     . HOH U 8 .   ? 3.950   92.507  59.304 1.00 22.29 ? 893  HOH A O     1 
HETATM 8607 O O     . HOH U 8 .   ? 11.082  87.810  82.257 1.00 44.37 ? 894  HOH A O     1 
HETATM 8608 O O     . HOH U 8 .   ? 14.709  108.046 43.773 1.00 30.89 ? 895  HOH A O     1 
HETATM 8609 O O     . HOH U 8 .   ? -2.048  87.320  33.260 1.00 27.63 ? 896  HOH A O     1 
HETATM 8610 O O     . HOH U 8 .   ? -3.055  113.743 64.754 1.00 36.22 ? 897  HOH A O     1 
HETATM 8611 O O     . HOH U 8 .   ? -32.751 85.035  44.261 1.00 40.27 ? 898  HOH A O     1 
HETATM 8612 O O     . HOH U 8 .   ? -14.795 118.490 46.780 1.00 28.37 ? 899  HOH A O     1 
HETATM 8613 O O     . HOH U 8 .   ? -30.161 83.217  68.469 1.00 48.17 ? 900  HOH A O     1 
HETATM 8614 O O     . HOH U 8 .   ? -12.936 120.199 47.442 1.00 28.55 ? 901  HOH A O     1 
HETATM 8615 O O     . HOH U 8 .   ? -13.256 76.578  41.080 1.00 44.51 ? 902  HOH A O     1 
HETATM 8616 O O     . HOH U 8 .   ? -17.468 81.297  53.580 1.00 20.42 ? 903  HOH A O     1 
HETATM 8617 O O     . HOH U 8 .   ? 2.862   101.575 78.175 1.00 32.14 ? 904  HOH A O     1 
HETATM 8618 O O     . HOH U 8 .   ? -9.178  112.030 35.766 1.00 31.32 ? 905  HOH A O     1 
HETATM 8619 O O     . HOH U 8 .   ? -25.887 88.155  47.857 1.00 32.68 ? 906  HOH A O     1 
HETATM 8620 O O     . HOH U 8 .   ? 1.346   113.431 30.654 1.00 31.30 ? 907  HOH A O     1 
HETATM 8621 O O     . HOH U 8 .   ? -6.222  89.951  39.779 1.00 22.59 ? 908  HOH A O     1 
HETATM 8622 O O     . HOH U 8 .   ? -0.582  69.580  40.326 1.00 39.33 ? 909  HOH A O     1 
HETATM 8623 O O     . HOH U 8 .   ? -22.788 97.508  64.258 1.00 42.45 ? 910  HOH A O     1 
HETATM 8624 O O     . HOH U 8 .   ? -19.526 95.352  50.034 1.00 21.83 ? 911  HOH A O     1 
HETATM 8625 O O     . HOH U 8 .   ? -12.749 85.626  56.990 1.00 32.32 ? 912  HOH A O     1 
HETATM 8626 O O     . HOH U 8 .   ? 0.406   103.039 62.704 1.00 17.32 ? 913  HOH A O     1 
HETATM 8627 O O     . HOH U 8 .   ? 12.999  118.379 42.312 1.00 42.25 ? 914  HOH A O     1 
HETATM 8628 O O     . HOH U 8 .   ? -35.457 92.620  64.659 1.00 35.95 ? 915  HOH A O     1 
HETATM 8629 O O     . HOH U 8 .   ? -4.258  111.830 50.721 1.00 29.77 ? 916  HOH A O     1 
HETATM 8630 O O     . HOH U 8 .   ? -12.276 76.162  54.790 1.00 36.21 ? 917  HOH A O     1 
HETATM 8631 O O     . HOH U 8 .   ? 0.759   101.982 51.571 1.00 51.45 ? 918  HOH A O     1 
HETATM 8632 O O     . HOH U 8 .   ? -11.969 112.021 65.215 1.00 35.00 ? 919  HOH A O     1 
HETATM 8633 O O     . HOH U 8 .   ? -2.145  113.451 72.501 1.00 42.17 ? 920  HOH A O     1 
HETATM 8634 O O     . HOH U 8 .   ? -5.811  83.950  59.071 1.00 22.38 ? 921  HOH A O     1 
HETATM 8635 O O     . HOH U 8 .   ? 0.333   78.232  33.968 1.00 26.91 ? 922  HOH A O     1 
HETATM 8636 O O     . HOH U 8 .   ? -22.528 81.972  48.576 1.00 29.54 ? 923  HOH A O     1 
HETATM 8637 O O     . HOH U 8 .   ? -3.111  101.493 61.184 1.00 15.98 ? 924  HOH A O     1 
HETATM 8638 O O     . HOH U 8 .   ? -14.573 89.516  30.501 1.00 46.28 ? 925  HOH A O     1 
HETATM 8639 O O     . HOH U 8 .   ? -24.379 105.346 40.316 1.00 43.67 ? 926  HOH A O     1 
HETATM 8640 O O     . HOH U 8 .   ? -3.260  110.569 67.703 1.00 28.17 ? 927  HOH A O     1 
HETATM 8641 O O     . HOH U 8 .   ? -0.378  101.734 60.485 1.00 18.41 ? 928  HOH A O     1 
HETATM 8642 O O     . HOH U 8 .   ? -2.273  103.202 63.419 1.00 16.93 ? 929  HOH A O     1 
HETATM 8643 O O     . HOH U 8 .   ? -21.955 93.411  56.856 1.00 22.63 ? 930  HOH A O     1 
HETATM 8644 O O     . HOH U 8 .   ? 0.286   68.763  49.017 1.00 42.05 ? 931  HOH A O     1 
HETATM 8645 O O     . HOH U 8 .   ? -12.701 109.760 33.503 1.00 34.49 ? 932  HOH A O     1 
HETATM 8646 O O     . HOH U 8 .   ? -16.578 102.932 71.747 1.00 49.75 ? 933  HOH A O     1 
HETATM 8647 O O     . HOH U 8 .   ? -21.903 74.974  50.922 1.00 37.39 ? 934  HOH A O     1 
HETATM 8648 O O     . HOH U 8 .   ? -7.808  89.362  55.766 1.00 33.22 ? 935  HOH A O     1 
HETATM 8649 O O     . HOH U 8 .   ? -9.224  98.706  76.680 1.00 29.48 ? 936  HOH A O     1 
HETATM 8650 O O     . HOH U 8 .   ? 5.991   105.727 31.500 1.00 27.53 ? 937  HOH A O     1 
HETATM 8651 O O     . HOH U 8 .   ? 2.915   98.410  30.460 1.00 37.34 ? 938  HOH A O     1 
HETATM 8652 O O     . HOH U 8 .   ? -12.818 89.079  53.587 1.00 20.61 ? 939  HOH A O     1 
HETATM 8653 O O     . HOH U 8 .   ? -6.874  91.186  37.164 1.00 24.34 ? 940  HOH A O     1 
HETATM 8654 O O     . HOH U 8 .   ? -5.902  115.009 28.590 1.00 33.06 ? 941  HOH A O     1 
HETATM 8655 O O     . HOH U 8 .   ? -26.900 113.633 41.919 1.00 29.47 ? 942  HOH A O     1 
HETATM 8656 O O     . HOH U 8 .   ? -9.305  76.246  76.601 1.00 34.25 ? 943  HOH A O     1 
HETATM 8657 O O     . HOH U 8 .   ? 0.151   126.818 33.093 1.00 43.99 ? 944  HOH A O     1 
HETATM 8658 O O     . HOH U 8 .   ? -19.760 87.344  39.060 1.00 39.78 ? 945  HOH A O     1 
HETATM 8659 O O     . HOH U 8 .   ? -16.227 113.636 30.914 1.00 43.26 ? 946  HOH A O     1 
HETATM 8660 O O     . HOH U 8 .   ? -8.279  77.351  37.724 1.00 50.52 ? 947  HOH A O     1 
HETATM 8661 O O     . HOH U 8 .   ? -9.693  82.526  59.533 1.00 22.42 ? 948  HOH A O     1 
HETATM 8662 O O     . HOH U 8 .   ? -20.797 110.121 57.257 1.00 24.21 ? 949  HOH A O     1 
HETATM 8663 O O     . HOH U 8 .   ? 9.860   83.261  67.592 1.00 19.70 ? 950  HOH A O     1 
HETATM 8664 O O     . HOH U 8 .   ? -18.134 123.562 49.578 1.00 50.02 ? 951  HOH A O     1 
HETATM 8665 O O     . HOH U 8 .   ? -16.538 85.971  38.914 1.00 42.83 ? 952  HOH A O     1 
HETATM 8666 O O     . HOH U 8 .   ? 0.479   115.883 71.763 1.00 46.01 ? 953  HOH A O     1 
HETATM 8667 O O     . HOH U 8 .   ? -3.646  76.167  73.129 1.00 22.77 ? 954  HOH A O     1 
HETATM 8668 O O     . HOH U 8 .   ? -17.266 72.853  56.874 1.00 46.68 ? 955  HOH A O     1 
HETATM 8669 O O     . HOH U 8 .   ? -25.046 107.513 44.103 1.00 29.87 ? 956  HOH A O     1 
HETATM 8670 O O     . HOH U 8 .   ? -3.602  70.789  62.418 1.00 43.71 ? 957  HOH A O     1 
HETATM 8671 O O     . HOH U 8 .   ? -13.099 72.422  53.172 1.00 35.02 ? 958  HOH A O     1 
HETATM 8672 O O     . HOH U 8 .   ? -27.737 112.608 46.460 1.00 45.04 ? 959  HOH A O     1 
HETATM 8673 O O     . HOH U 8 .   ? -9.288  96.609  33.706 1.00 26.65 ? 960  HOH A O     1 
HETATM 8674 O O     . HOH U 8 .   ? 7.826   96.411  75.192 1.00 40.58 ? 961  HOH A O     1 
HETATM 8675 O O     . HOH U 8 .   ? 2.877   79.460  33.721 1.00 25.43 ? 962  HOH A O     1 
HETATM 8676 O O     . HOH U 8 .   ? -24.514 92.507  65.675 1.00 37.92 ? 963  HOH A O     1 
HETATM 8677 O O     . HOH U 8 .   ? -15.134 84.462  42.401 1.00 20.66 ? 964  HOH A O     1 
HETATM 8678 O O     . HOH U 8 .   ? -16.677 112.188 60.536 1.00 30.77 ? 965  HOH A O     1 
HETATM 8679 O O     . HOH U 8 .   ? 8.106   83.945  65.044 1.00 20.23 ? 966  HOH A O     1 
HETATM 8680 O O     . HOH U 8 .   ? -30.872 74.707  53.994 1.00 44.20 ? 967  HOH A O     1 
HETATM 8681 O O     . HOH U 8 .   ? -23.745 67.220  59.108 1.00 39.77 ? 968  HOH A O     1 
HETATM 8682 O O     . HOH U 8 .   ? -6.807  87.191  57.330 1.00 18.72 ? 969  HOH A O     1 
HETATM 8683 O O     . HOH U 8 .   ? 5.415   87.310  57.804 1.00 25.10 ? 970  HOH A O     1 
HETATM 8684 O O     . HOH U 8 .   ? 3.152   105.029 77.189 1.00 28.41 ? 971  HOH A O     1 
HETATM 8685 O O     . HOH U 8 .   ? 9.698   115.461 63.570 1.00 27.52 ? 972  HOH A O     1 
HETATM 8686 O O     . HOH U 8 .   ? -10.270 71.001  67.225 1.00 30.60 ? 973  HOH A O     1 
HETATM 8687 O O     . HOH U 8 .   ? -17.302 100.296 68.352 1.00 39.81 ? 974  HOH A O     1 
HETATM 8688 O O     . HOH U 8 .   ? -14.785 90.838  52.960 1.00 21.32 ? 975  HOH A O     1 
HETATM 8689 O O     . HOH U 8 .   ? -28.393 88.100  47.118 1.00 51.17 ? 976  HOH A O     1 
HETATM 8690 O O     . HOH U 8 .   ? -2.572  71.220  46.646 1.00 41.57 ? 977  HOH A O     1 
HETATM 8691 O O     . HOH U 8 .   ? 10.363  125.157 50.400 1.00 35.73 ? 978  HOH A O     1 
HETATM 8692 O O     . HOH U 8 .   ? -3.630  73.245  63.282 1.00 35.46 ? 979  HOH A O     1 
HETATM 8693 O O     . HOH U 8 .   ? -11.275 125.622 47.851 1.00 30.31 ? 980  HOH A O     1 
HETATM 8694 O O     . HOH U 8 .   ? 8.878   121.021 36.507 1.00 41.31 ? 981  HOH A O     1 
HETATM 8695 O O     . HOH U 8 .   ? -1.178  101.696 77.828 1.00 29.49 ? 982  HOH A O     1 
HETATM 8696 O O     . HOH U 8 .   ? -16.969 94.427  75.021 1.00 39.07 ? 983  HOH A O     1 
HETATM 8697 O O     . HOH U 8 .   ? 1.309   116.081 30.646 1.00 48.35 ? 984  HOH A O     1 
HETATM 8698 O O     . HOH U 8 .   ? -11.928 102.741 55.432 1.00 35.08 ? 985  HOH A O     1 
HETATM 8699 O O     . HOH U 8 .   ? -18.913 118.139 26.838 1.00 43.06 ? 986  HOH A O     1 
HETATM 8700 O O     . HOH U 8 .   ? -0.207  127.432 41.953 1.00 35.33 ? 987  HOH A O     1 
HETATM 8701 O O     . HOH U 8 .   ? -14.758 109.490 72.805 1.00 47.26 ? 988  HOH A O     1 
HETATM 8702 O O     . HOH U 8 .   ? -9.231  84.128  77.182 1.00 25.07 ? 989  HOH A O     1 
HETATM 8703 O O     . HOH U 8 .   ? -5.379  101.090 79.728 1.00 52.55 ? 990  HOH A O     1 
HETATM 8704 O O     . HOH U 8 .   ? 16.374  123.403 51.384 1.00 41.78 ? 991  HOH A O     1 
HETATM 8705 O O     . HOH U 8 .   ? 3.915   102.426 55.885 1.00 26.93 ? 992  HOH A O     1 
HETATM 8706 O O     . HOH U 8 .   ? -20.128 74.409  74.592 1.00 31.21 ? 993  HOH A O     1 
HETATM 8707 O O     . HOH U 8 .   ? 6.712   72.940  39.275 1.00 20.65 ? 994  HOH A O     1 
HETATM 8708 O O     . HOH U 8 .   ? -18.941 73.500  49.565 1.00 44.49 ? 995  HOH A O     1 
HETATM 8709 O O     . HOH U 8 .   ? -18.313 85.858  40.811 1.00 38.45 ? 996  HOH A O     1 
HETATM 8710 O O     . HOH U 8 .   ? -19.971 95.855  47.363 1.00 21.86 ? 997  HOH A O     1 
HETATM 8711 O O     . HOH U 8 .   ? -0.654  73.523  70.760 1.00 27.64 ? 998  HOH A O     1 
HETATM 8712 O O     . HOH U 8 .   ? -23.993 89.994  46.694 1.00 36.35 ? 999  HOH A O     1 
HETATM 8713 O O     . HOH U 8 .   ? -8.357  107.834 49.903 1.00 30.66 ? 1000 HOH A O     1 
HETATM 8714 O O     . HOH U 8 .   ? -31.817 107.154 51.110 1.00 30.10 ? 1001 HOH A O     1 
HETATM 8715 O O     . HOH U 8 .   ? 10.803  111.334 56.642 1.00 33.06 ? 1002 HOH A O     1 
HETATM 8716 O O     . HOH U 8 .   ? 6.770   94.439  73.589 1.00 22.79 ? 1003 HOH A O     1 
HETATM 8717 O O     . HOH U 8 .   ? -30.716 83.964  57.227 1.00 33.70 ? 1004 HOH A O     1 
HETATM 8718 O O     . HOH U 8 .   ? 11.486  94.298  63.791 1.00 19.30 ? 1005 HOH A O     1 
HETATM 8719 O O     . HOH U 8 .   ? -11.332 70.473  54.288 1.00 28.45 ? 1006 HOH A O     1 
HETATM 8720 O O     . HOH U 8 .   ? -30.750 68.728  57.349 1.00 41.79 ? 1007 HOH A O     1 
HETATM 8721 O O     . HOH U 8 .   ? -0.138  103.768 49.907 1.00 34.06 ? 1008 HOH A O     1 
HETATM 8722 O O     . HOH U 8 .   ? -29.580 89.113  36.928 1.00 42.97 ? 1009 HOH A O     1 
HETATM 8723 O O     . HOH U 8 .   ? -23.052 78.171  79.864 1.00 43.92 ? 1010 HOH A O     1 
HETATM 8724 O O     . HOH U 8 .   ? 7.344   99.670  34.843 1.00 34.04 ? 1011 HOH A O     1 
HETATM 8725 O O     . HOH U 8 .   ? -19.211 84.138  43.780 1.00 48.99 ? 1012 HOH A O     1 
HETATM 8726 O O     . HOH U 8 .   ? -26.760 86.935  40.283 1.00 32.95 ? 1013 HOH A O     1 
HETATM 8727 O O     . HOH U 8 .   ? -4.558  69.344  65.789 1.00 29.74 ? 1014 HOH A O     1 
HETATM 8728 O O     . HOH U 8 .   ? -4.604  108.713 26.906 1.00 45.65 ? 1015 HOH A O     1 
HETATM 8729 O O     . HOH U 8 .   ? 6.084   105.262 77.261 1.00 31.32 ? 1016 HOH A O     1 
HETATM 8730 O O     . HOH U 8 .   ? 4.070   88.335  74.900 1.00 27.73 ? 1017 HOH A O     1 
HETATM 8731 O O     . HOH U 8 .   ? 3.497   100.310 50.496 1.00 42.29 ? 1018 HOH A O     1 
HETATM 8732 O O     . HOH U 8 .   ? -13.644 120.461 54.790 1.00 39.19 ? 1019 HOH A O     1 
HETATM 8733 O O     . HOH U 8 .   ? -19.903 68.490  57.761 1.00 55.52 ? 1020 HOH A O     1 
HETATM 8734 O O     . HOH U 8 .   ? -1.238  114.030 69.611 1.00 49.81 ? 1021 HOH A O     1 
HETATM 8735 O O     . HOH U 8 .   ? -5.961  81.481  75.695 1.00 36.87 ? 1022 HOH A O     1 
HETATM 8736 O O     . HOH U 8 .   ? 10.146  107.961 71.332 1.00 31.83 ? 1023 HOH A O     1 
HETATM 8737 O O     . HOH U 8 .   ? -27.034 90.848  72.538 1.00 41.11 ? 1024 HOH A O     1 
HETATM 8738 O O     . HOH U 8 .   ? -30.855 85.922  67.691 1.00 29.52 ? 1025 HOH A O     1 
HETATM 8739 O O     . HOH U 8 .   ? -20.377 93.471  75.119 1.00 37.93 ? 1026 HOH A O     1 
HETATM 8740 O O     . HOH U 8 .   ? -23.937 70.534  74.676 1.00 37.94 ? 1027 HOH A O     1 
HETATM 8741 O O     . HOH U 8 .   ? -14.099 121.883 56.768 1.00 46.16 ? 1028 HOH A O     1 
HETATM 8742 O O     . HOH U 8 .   ? -14.958 107.466 28.645 1.00 52.31 ? 1029 HOH A O     1 
HETATM 8743 O O     . HOH U 8 .   ? -0.582  101.850 48.102 1.00 34.49 ? 1030 HOH A O     1 
HETATM 8744 O O     . HOH U 8 .   ? -21.353 106.815 39.448 1.00 45.18 ? 1031 HOH A O     1 
HETATM 8745 O O     . HOH U 8 .   ? -15.323 73.247  73.070 1.00 43.97 ? 1032 HOH A O     1 
HETATM 8746 O O     . HOH U 8 .   ? 16.109  106.727 50.436 1.00 27.75 ? 1033 HOH A O     1 
HETATM 8747 O O     . HOH U 8 .   ? -6.608  102.909 81.347 1.00 50.55 ? 1034 HOH A O     1 
HETATM 8748 O O     . HOH U 8 .   ? -2.490  120.453 61.483 1.00 43.03 ? 1035 HOH A O     1 
HETATM 8749 O O     . HOH U 8 .   ? -17.740 125.647 51.514 1.00 40.02 ? 1036 HOH A O     1 
HETATM 8750 O O     . HOH U 8 .   ? -15.701 77.207  44.574 1.00 50.75 ? 1037 HOH A O     1 
HETATM 8751 O O     . HOH U 8 .   ? -2.785  128.952 44.954 1.00 48.64 ? 1038 HOH A O     1 
HETATM 8752 O O     . HOH U 8 .   ? -0.226  74.489  34.029 1.00 46.45 ? 1039 HOH A O     1 
HETATM 8753 O O     . HOH U 8 .   ? -1.028  73.014  66.772 1.00 22.96 ? 1040 HOH A O     1 
HETATM 8754 O O     . HOH U 8 .   ? 3.993   122.513 61.410 1.00 29.68 ? 1041 HOH A O     1 
HETATM 8755 O O     . HOH U 8 .   ? 8.169   109.028 75.683 1.00 44.07 ? 1042 HOH A O     1 
HETATM 8756 O O     . HOH U 8 .   ? 2.864   73.781  43.968 1.00 34.33 ? 1043 HOH A O     1 
HETATM 8757 O O     . HOH U 8 .   ? -4.382  83.564  75.285 1.00 30.75 ? 1044 HOH A O     1 
HETATM 8758 O O     . HOH U 8 .   ? -8.854  90.438  49.482 1.00 25.04 ? 1045 HOH A O     1 
HETATM 8759 O O     . HOH U 8 .   ? -5.634  76.122  75.411 1.00 31.53 ? 1046 HOH A O     1 
HETATM 8760 O O     . HOH U 8 .   ? -27.903 112.326 39.841 1.00 41.74 ? 1047 HOH A O     1 
HETATM 8761 O O     . HOH U 8 .   ? -4.539  115.031 65.941 1.00 43.95 ? 1048 HOH A O     1 
HETATM 8762 O O     . HOH U 8 .   ? 10.043  92.347  57.470 1.00 46.61 ? 1049 HOH A O     1 
HETATM 8763 O O     . HOH U 8 .   ? -10.344 111.742 73.531 1.00 43.05 ? 1050 HOH A O     1 
HETATM 8764 O O     . HOH U 8 .   ? -25.653 85.735  77.522 1.00 40.41 ? 1051 HOH A O     1 
HETATM 8765 O O     . HOH U 8 .   ? -11.320 67.382  64.785 1.00 47.24 ? 1052 HOH A O     1 
HETATM 8766 O O     . HOH U 8 .   ? 13.018  107.608 37.673 1.00 42.07 ? 1053 HOH A O     1 
HETATM 8767 O O     . HOH U 8 .   ? 9.786   104.868 32.587 1.00 43.11 ? 1054 HOH A O     1 
HETATM 8768 O O     . HOH U 8 .   ? 0.607   97.989  50.759 1.00 29.40 ? 1055 HOH A O     1 
HETATM 8769 O O     . HOH U 8 .   ? -26.832 99.567  52.886 1.00 35.02 ? 1056 HOH A O     1 
HETATM 8770 O O     . HOH U 8 .   ? -24.494 95.110  64.772 1.00 45.66 ? 1057 HOH A O     1 
HETATM 8771 O O     . HOH U 8 .   ? -2.927  104.237 27.280 1.00 48.02 ? 1058 HOH A O     1 
HETATM 8772 O O     . HOH U 8 .   ? 4.970   91.142  57.306 1.00 36.16 ? 1059 HOH A O     1 
HETATM 8773 O O     . HOH U 8 .   ? 4.836   85.611  78.085 1.00 32.92 ? 1060 HOH A O     1 
HETATM 8774 O O     . HOH U 8 .   ? -29.867 77.060  73.403 1.00 46.20 ? 1061 HOH A O     1 
HETATM 8775 O O     . HOH U 8 .   ? -26.666 98.432  59.904 1.00 38.36 ? 1062 HOH A O     1 
HETATM 8776 O O     . HOH U 8 .   ? 2.948   71.875  48.316 1.00 31.13 ? 1063 HOH A O     1 
HETATM 8777 O O     . HOH U 8 .   ? -3.936  120.042 59.785 1.00 44.16 ? 1064 HOH A O     1 
HETATM 8778 O O     . HOH U 8 .   ? 0.311   98.607  29.020 1.00 47.93 ? 1065 HOH A O     1 
HETATM 8779 O O     . HOH U 8 .   ? -26.835 115.209 48.694 1.00 50.96 ? 1066 HOH A O     1 
HETATM 8780 O O     . HOH U 8 .   ? -14.324 75.323  45.324 1.00 49.63 ? 1067 HOH A O     1 
HETATM 8781 O O     . HOH U 8 .   ? -20.326 88.551  33.557 1.00 45.97 ? 1068 HOH A O     1 
HETATM 8782 O O     . HOH U 8 .   ? -9.737  71.119  74.325 1.00 40.66 ? 1069 HOH A O     1 
HETATM 8783 O O     . HOH U 8 .   ? -10.128 90.316  28.708 1.00 43.67 ? 1070 HOH A O     1 
HETATM 8784 O O     . HOH U 8 .   ? -26.692 91.623  76.951 1.00 59.49 ? 1071 HOH A O     1 
HETATM 8785 O O     . HOH U 8 .   ? -10.196 75.361  44.661 1.00 47.78 ? 1072 HOH A O     1 
HETATM 8786 O O     . HOH U 8 .   ? -28.629 104.828 52.544 1.00 44.81 ? 1073 HOH A O     1 
HETATM 8787 O O     . HOH U 8 .   ? -25.783 107.414 49.844 1.00 43.94 ? 1074 HOH A O     1 
HETATM 8788 O O     . HOH U 8 .   ? -8.856  70.466  71.805 1.00 37.57 ? 1075 HOH A O     1 
HETATM 8789 O O     . HOH U 8 .   ? -9.163  95.407  79.564 1.00 49.25 ? 1076 HOH A O     1 
HETATM 8790 O O     . HOH U 8 .   ? -9.568  69.640  65.348 1.00 30.78 ? 1077 HOH A O     1 
HETATM 8791 O O     . HOH U 8 .   ? -13.231 67.668  66.390 1.00 42.09 ? 1078 HOH A O     1 
HETATM 8792 O O     . HOH U 8 .   ? -28.069 70.725  71.478 1.00 43.41 ? 1079 HOH A O     1 
HETATM 8793 O O     . HOH U 8 .   ? -15.517 79.471  77.540 1.00 41.83 ? 1080 HOH A O     1 
HETATM 8794 O O     . HOH U 8 .   ? 2.741   119.014 64.368 1.00 45.37 ? 1081 HOH A O     1 
HETATM 8795 O O     . HOH U 8 .   ? -25.643 105.484 42.814 1.00 36.75 ? 1082 HOH A O     1 
HETATM 8796 O O     . HOH U 8 .   ? -28.405 113.652 44.158 1.00 38.80 ? 1083 HOH A O     1 
HETATM 8797 O O     . HOH U 8 .   ? 9.238   112.940 65.096 1.00 47.58 ? 1084 HOH A O     1 
HETATM 8798 O O     . HOH U 8 .   ? -11.915 111.275 35.583 1.00 33.35 ? 1085 HOH A O     1 
HETATM 8799 O O     . HOH U 8 .   ? -7.965  70.864  63.147 1.00 29.87 ? 1086 HOH A O     1 
HETATM 8800 O O     . HOH U 8 .   ? -30.137 75.467  63.718 1.00 47.77 ? 1087 HOH A O     1 
HETATM 8801 O O     . HOH U 8 .   ? 6.384   101.928 79.523 1.00 42.96 ? 1088 HOH A O     1 
HETATM 8802 O O     . HOH U 8 .   ? -2.252  106.964 26.483 1.00 46.62 ? 1089 HOH A O     1 
HETATM 8803 O O     . HOH U 8 .   ? -16.331 81.078  79.052 1.00 53.77 ? 1090 HOH A O     1 
HETATM 8804 O O     . HOH U 8 .   ? -7.696  71.734  75.765 1.00 38.13 ? 1091 HOH A O     1 
HETATM 8805 O O     . HOH U 8 .   ? -29.889 89.274  50.526 1.00 52.06 ? 1092 HOH A O     1 
HETATM 8806 O O     . HOH U 8 .   ? 14.001  112.686 44.130 1.00 41.69 ? 1093 HOH A O     1 
HETATM 8807 O O     . HOH U 8 .   ? 5.577   111.132 30.557 1.00 46.52 ? 1094 HOH A O     1 
HETATM 8808 O O     . HOH U 8 .   ? -14.845 111.791 34.659 1.00 43.58 ? 1095 HOH A O     1 
HETATM 8809 O O     . HOH U 8 .   ? 4.151   126.691 46.080 1.00 52.92 ? 1096 HOH A O     1 
HETATM 8810 O O     . HOH U 8 .   ? -3.799  114.868 78.918 1.00 52.63 ? 1097 HOH A O     1 
HETATM 8811 O O     . HOH U 8 .   ? -8.553  132.135 49.952 1.00 53.82 ? 1098 HOH A O     1 
HETATM 8812 O O     . HOH U 8 .   ? -1.841  67.686  55.651 1.00 37.23 ? 1099 HOH A O     1 
HETATM 8813 O O     . HOH U 8 .   ? -12.288 72.022  77.848 1.00 40.95 ? 1100 HOH A O     1 
HETATM 8814 O O     . HOH U 8 .   ? 2.291   125.361 54.855 1.00 45.77 ? 1101 HOH A O     1 
HETATM 8815 O O     . HOH U 8 .   ? 15.477  119.969 45.162 1.00 39.10 ? 1102 HOH A O     1 
HETATM 8816 O O     . HOH U 8 .   ? -1.035  71.050  70.041 1.00 31.14 ? 1103 HOH A O     1 
HETATM 8817 O O     . HOH U 8 .   ? -19.008 68.758  52.093 1.00 41.15 ? 1104 HOH A O     1 
HETATM 8818 O O     . HOH U 8 .   ? 1.288   105.234 27.029 1.00 41.53 ? 1105 HOH A O     1 
HETATM 8819 O O     . HOH U 8 .   ? -32.908 85.093  57.901 1.00 50.96 ? 1106 HOH A O     1 
HETATM 8820 O O     . HOH U 8 .   ? 1.718   127.222 47.365 1.00 56.00 ? 1107 HOH A O     1 
HETATM 8821 O O     . HOH U 8 .   ? -0.544  70.485  67.435 1.00 35.23 ? 1108 HOH A O     1 
HETATM 8822 O O     . HOH U 8 .   ? -14.568 113.241 32.451 1.00 50.42 ? 1109 HOH A O     1 
HETATM 8823 O O     . HOH U 8 .   ? -28.623 121.512 44.948 1.00 47.19 ? 1110 HOH A O     1 
HETATM 8824 O O     . HOH U 8 .   ? -19.867 79.155  47.709 1.00 41.07 ? 1111 HOH A O     1 
HETATM 8825 O O     . HOH U 8 .   ? -17.745 82.498  44.845 1.00 40.25 ? 1112 HOH A O     1 
HETATM 8826 O O     . HOH U 8 .   ? -8.255  85.976  32.904 1.00 45.01 ? 1113 HOH A O     1 
HETATM 8827 O O     . HOH U 8 .   ? 9.258   113.070 33.205 1.00 48.59 ? 1114 HOH A O     1 
HETATM 8828 O O     . HOH U 8 .   ? -13.437 105.504 73.195 1.00 36.18 ? 1115 HOH A O     1 
HETATM 8829 O O     . HOH U 8 .   ? -9.635  114.786 69.980 1.00 44.67 ? 1116 HOH A O     1 
HETATM 8830 O O     . HOH U 8 .   ? -3.717  78.713  33.431 1.00 50.73 ? 1117 HOH A O     1 
HETATM 8831 O O     . HOH U 8 .   ? 5.117   126.946 42.905 1.00 60.42 ? 1118 HOH A O     1 
HETATM 8832 O O     . HOH U 8 .   ? -25.040 89.697  49.852 1.00 30.24 ? 1119 HOH A O     1 
HETATM 8833 O O     . HOH U 8 .   ? 8.631   109.949 57.702 1.00 46.40 ? 1120 HOH A O     1 
HETATM 8834 O O     . HOH U 8 .   ? -31.049 91.226  47.736 1.00 46.55 ? 1121 HOH A O     1 
HETATM 8835 O O     . HOH U 8 .   ? -1.990  68.588  65.855 1.00 38.78 ? 1122 HOH A O     1 
HETATM 8836 O O     . HOH U 8 .   ? -27.625 122.249 36.720 1.00 53.32 ? 1123 HOH A O     1 
HETATM 8837 O O     . HOH U 8 .   ? -10.394 92.131  78.008 1.00 46.46 ? 1124 HOH A O     1 
HETATM 8838 O O     . HOH U 8 .   ? 2.317   72.245  34.556 1.00 47.21 ? 1125 HOH A O     1 
HETATM 8839 O O     . HOH U 8 .   ? 1.960   127.021 34.982 1.00 44.85 ? 1126 HOH A O     1 
HETATM 8840 O O     . HOH U 8 .   ? -17.092 89.076  30.951 1.00 44.84 ? 1127 HOH A O     1 
HETATM 8841 O O     . HOH U 8 .   ? -8.045  73.615  77.734 1.00 29.63 ? 1128 HOH A O     1 
HETATM 8842 O O     . HOH U 8 .   ? -34.607 89.533  59.137 1.00 52.09 ? 1129 HOH A O     1 
HETATM 8843 O O     . HOH U 8 .   ? -11.414 114.589 65.736 1.00 45.28 ? 1130 HOH A O     1 
HETATM 8844 O O     . HOH U 8 .   ? -17.766 67.938  53.925 1.00 48.46 ? 1131 HOH A O     1 
HETATM 8845 O O     . HOH U 8 .   ? 11.220  114.209 37.989 1.00 45.27 ? 1132 HOH A O     1 
HETATM 8846 O O     . HOH U 8 .   ? -16.180 82.575  40.708 1.00 48.62 ? 1133 HOH A O     1 
HETATM 8847 O O     . HOH U 8 .   ? -5.612  69.661  63.195 1.00 33.74 ? 1134 HOH A O     1 
HETATM 8848 O O     . HOH U 8 .   ? -5.660  69.208  69.436 1.00 42.22 ? 1135 HOH A O     1 
HETATM 8849 O O     . HOH U 8 .   ? -1.267  123.655 57.157 1.00 40.36 ? 1136 HOH A O     1 
HETATM 8850 O O     . HOH U 8 .   ? 10.117  109.336 73.790 1.00 43.45 ? 1137 HOH A O     1 
HETATM 8851 O O     . HOH U 8 .   ? -6.588  97.618  34.192 1.00 32.48 ? 1138 HOH A O     1 
HETATM 8852 O O     . HOH U 8 .   ? -0.591  81.818  31.732 1.00 35.59 ? 1139 HOH A O     1 
HETATM 8853 O O     . HOH U 8 .   ? 8.703   76.205  35.429 1.00 58.52 ? 1140 HOH A O     1 
HETATM 8854 O O     . HOH U 8 .   ? 8.239   103.397 59.151 1.00 49.94 ? 1141 HOH A O     1 
HETATM 8855 O O     . HOH U 8 .   ? 0.012   76.420  31.845 1.00 45.66 ? 1142 HOH A O     1 
HETATM 8856 O O     . HOH U 8 .   ? -8.645  91.511  27.293 1.00 40.05 ? 1143 HOH A O     1 
HETATM 8857 O O     . HOH U 8 .   ? -6.657  68.627  67.298 1.00 53.76 ? 1144 HOH A O     1 
HETATM 8858 O O     . HOH U 8 .   ? 16.834  109.752 43.922 1.00 40.81 ? 1145 HOH A O     1 
HETATM 8859 O O     . HOH U 8 .   ? -11.512 101.726 74.161 1.00 39.83 ? 1146 HOH A O     1 
HETATM 8860 O O     . HOH U 8 .   ? 6.964   101.187 30.498 1.00 38.69 ? 1147 HOH A O     1 
HETATM 8861 O O     . HOH U 8 .   ? 7.450   103.732 30.518 1.00 38.13 ? 1148 HOH A O     1 
HETATM 8862 O O     . HOH U 8 .   ? -22.106 93.901  69.225 1.00 51.84 ? 1149 HOH A O     1 
HETATM 8863 O O     . HOH U 8 .   ? -5.944  122.448 57.164 1.00 46.07 ? 1150 HOH A O     1 
HETATM 8864 O O     . HOH U 8 .   ? 14.350  122.752 63.305 1.00 41.92 ? 1151 HOH A O     1 
HETATM 8865 O O     . HOH V 8 .   ? 42.191  106.376 78.466 1.00 47.43 ? 701  HOH B O     1 
HETATM 8866 O O     . HOH V 8 .   ? 10.652  70.426  66.423 1.00 37.02 ? 702  HOH B O     1 
HETATM 8867 O O     . HOH V 8 .   ? 13.718  64.827  34.484 1.00 39.60 ? 703  HOH B O     1 
HETATM 8868 O O     . HOH V 8 .   ? 33.161  95.833  85.246 1.00 50.00 ? 704  HOH B O     1 
HETATM 8869 O O     . HOH V 8 .   ? 13.586  68.395  34.411 1.00 31.93 ? 705  HOH B O     1 
HETATM 8870 O O     . HOH V 8 .   ? 34.193  97.286  61.984 1.00 32.42 ? 706  HOH B O     1 
HETATM 8871 O O     . HOH V 8 .   ? 52.809  97.302  71.046 1.00 42.66 ? 707  HOH B O     1 
HETATM 8872 O O     . HOH V 8 .   ? 14.318  63.639  57.888 1.00 47.42 ? 708  HOH B O     1 
HETATM 8873 O O     . HOH V 8 .   ? 35.072  114.136 57.373 1.00 31.72 ? 709  HOH B O     1 
HETATM 8874 O O     . HOH V 8 .   ? 34.112  95.855  38.294 1.00 52.43 ? 710  HOH B O     1 
HETATM 8875 O O     . HOH V 8 .   ? 49.097  101.948 68.401 1.00 39.33 ? 711  HOH B O     1 
HETATM 8876 O O     . HOH V 8 .   ? 32.664  90.956  41.986 1.00 41.25 ? 712  HOH B O     1 
HETATM 8877 O O     . HOH V 8 .   ? 34.956  103.362 48.566 1.00 45.94 ? 713  HOH B O     1 
HETATM 8878 O O     . HOH V 8 .   ? 36.025  66.615  56.157 1.00 42.79 ? 714  HOH B O     1 
HETATM 8879 O O     . HOH V 8 .   ? 21.656  123.562 57.074 1.00 47.91 ? 715  HOH B O     1 
HETATM 8880 O O     . HOH V 8 .   ? 39.180  107.514 74.184 1.00 32.37 ? 716  HOH B O     1 
HETATM 8881 O O     . HOH V 8 .   ? 44.701  77.218  72.543 1.00 39.98 ? 717  HOH B O     1 
HETATM 8882 O O     . HOH V 8 .   ? 30.812  85.102  85.825 1.00 43.27 ? 718  HOH B O     1 
HETATM 8883 O O     . HOH V 8 .   ? 8.021   90.179  50.608 1.00 22.19 ? 719  HOH B O     1 
HETATM 8884 O O     . HOH V 8 .   ? 33.988  116.846 65.149 1.00 47.81 ? 720  HOH B O     1 
HETATM 8885 O O     . HOH V 8 .   ? 18.572  119.531 69.811 1.00 46.86 ? 721  HOH B O     1 
HETATM 8886 O O     . HOH V 8 .   ? 29.252  87.605  54.804 1.00 39.82 ? 722  HOH B O     1 
HETATM 8887 O O     . HOH V 8 .   ? 41.616  85.387  76.351 1.00 46.16 ? 723  HOH B O     1 
HETATM 8888 O O     . HOH V 8 .   ? 12.774  97.233  80.193 1.00 29.03 ? 724  HOH B O     1 
HETATM 8889 O O     . HOH V 8 .   ? 23.069  76.635  82.035 1.00 39.48 ? 725  HOH B O     1 
HETATM 8890 O O     . HOH V 8 .   ? 40.888  80.105  73.027 1.00 31.06 ? 726  HOH B O     1 
HETATM 8891 O O     . HOH V 8 .   ? 41.385  110.166 66.357 1.00 32.07 ? 727  HOH B O     1 
HETATM 8892 O O     . HOH V 8 .   ? 29.801  109.326 81.661 1.00 30.27 ? 728  HOH B O     1 
HETATM 8893 O O     . HOH V 8 .   ? 16.161  94.742  64.065 1.00 34.27 ? 729  HOH B O     1 
HETATM 8894 O O     . HOH V 8 .   ? 37.113  107.735 76.051 1.00 39.76 ? 730  HOH B O     1 
HETATM 8895 O O     . HOH V 8 .   ? 26.587  56.551  43.027 1.00 48.84 ? 731  HOH B O     1 
HETATM 8896 O O     . HOH V 8 .   ? 32.973  71.331  72.739 1.00 37.73 ? 732  HOH B O     1 
HETATM 8897 O O     . HOH V 8 .   ? 22.563  105.860 35.878 1.00 29.13 ? 733  HOH B O     1 
HETATM 8898 O O     . HOH V 8 .   ? 22.086  54.231  57.927 1.00 36.70 ? 734  HOH B O     1 
HETATM 8899 O O     . HOH V 8 .   ? 31.483  92.407  83.076 1.00 41.71 ? 735  HOH B O     1 
HETATM 8900 O O     . HOH V 8 .   ? 17.818  82.258  36.509 1.00 43.80 ? 736  HOH B O     1 
HETATM 8901 O O     . HOH V 8 .   ? 26.820  117.189 59.954 1.00 43.26 ? 737  HOH B O     1 
HETATM 8902 O O     . HOH V 8 .   ? 25.130  88.942  73.303 1.00 36.89 ? 738  HOH B O     1 
HETATM 8903 O O     . HOH V 8 .   ? 22.761  80.920  37.043 1.00 39.94 ? 739  HOH B O     1 
HETATM 8904 O O     . HOH V 8 .   ? 37.985  108.423 82.878 1.00 48.10 ? 740  HOH B O     1 
HETATM 8905 O O     . HOH V 8 .   ? 1.981   65.449  55.247 1.00 46.21 ? 741  HOH B O     1 
HETATM 8906 O O     . HOH V 8 .   ? 20.693  122.469 63.106 1.00 45.63 ? 742  HOH B O     1 
HETATM 8907 O O     . HOH V 8 .   ? 51.413  103.431 71.016 1.00 36.17 ? 743  HOH B O     1 
HETATM 8908 O O     . HOH V 8 .   ? 14.800  89.088  73.864 1.00 21.74 ? 744  HOH B O     1 
HETATM 8909 O O     . HOH V 8 .   ? 11.466  91.826  38.084 1.00 36.77 ? 745  HOH B O     1 
HETATM 8910 O O     . HOH V 8 .   ? 16.356  55.963  52.598 1.00 41.21 ? 746  HOH B O     1 
HETATM 8911 O O     . HOH V 8 .   ? 12.689  90.049  75.695 1.00 22.64 ? 747  HOH B O     1 
HETATM 8912 O O     . HOH V 8 .   ? 25.158  75.954  58.021 1.00 20.88 ? 748  HOH B O     1 
HETATM 8913 O O     . HOH V 8 .   ? 24.994  78.068  55.407 1.00 21.66 ? 749  HOH B O     1 
HETATM 8914 O O     . HOH V 8 .   ? 31.373  94.141  54.126 1.00 25.74 ? 750  HOH B O     1 
HETATM 8915 O O     . HOH V 8 .   ? 29.730  92.142  36.849 1.00 34.16 ? 751  HOH B O     1 
HETATM 8916 O O     . HOH V 8 .   ? 24.188  59.305  61.550 1.00 40.78 ? 752  HOH B O     1 
HETATM 8917 O O     . HOH V 8 .   ? 17.959  103.701 82.919 1.00 31.20 ? 753  HOH B O     1 
HETATM 8918 O O     . HOH V 8 .   ? 14.844  108.782 76.294 1.00 34.93 ? 754  HOH B O     1 
HETATM 8919 O O     . HOH V 8 .   ? 15.255  86.280  63.635 1.00 17.25 ? 755  HOH B O     1 
HETATM 8920 O O     . HOH V 8 .   ? 19.054  106.624 42.015 1.00 26.21 ? 756  HOH B O     1 
HETATM 8921 O O     . HOH V 8 .   ? 32.874  116.097 73.697 1.00 41.08 ? 757  HOH B O     1 
HETATM 8922 O O     . HOH V 8 .   ? 42.115  107.723 64.941 1.00 27.49 ? 758  HOH B O     1 
HETATM 8923 O O     . HOH V 8 .   ? 10.451  62.428  44.017 1.00 37.66 ? 759  HOH B O     1 
HETATM 8924 O O     . HOH V 8 .   ? 29.534  94.572  33.649 1.00 48.24 ? 760  HOH B O     1 
HETATM 8925 O O     . HOH V 8 .   ? 19.892  96.746  84.427 1.00 28.49 ? 761  HOH B O     1 
HETATM 8926 O O     . HOH V 8 .   ? 8.985   65.593  51.377 1.00 20.70 ? 762  HOH B O     1 
HETATM 8927 O O     . HOH V 8 .   ? 8.861   59.466  54.512 1.00 38.29 ? 763  HOH B O     1 
HETATM 8928 O O     . HOH V 8 .   ? 34.533  94.289  56.817 1.00 32.20 ? 764  HOH B O     1 
HETATM 8929 O O     . HOH V 8 .   ? 41.525  87.435  74.960 1.00 45.94 ? 765  HOH B O     1 
HETATM 8930 O O     . HOH V 8 .   ? 5.483   98.744  47.209 1.00 22.88 ? 766  HOH B O     1 
HETATM 8931 O O     . HOH V 8 .   ? 43.414  103.904 55.253 1.00 45.12 ? 767  HOH B O     1 
HETATM 8932 O O     . HOH V 8 .   ? 7.925   67.584  41.827 1.00 24.55 ? 768  HOH B O     1 
HETATM 8933 O O     . HOH V 8 .   ? 31.366  109.077 78.174 1.00 26.12 ? 769  HOH B O     1 
HETATM 8934 O O     . HOH V 8 .   ? 36.490  110.635 77.728 1.00 45.14 ? 770  HOH B O     1 
HETATM 8935 O O     . HOH V 8 .   ? 31.349  70.130  60.184 1.00 27.05 ? 771  HOH B O     1 
HETATM 8936 O O     . HOH V 8 .   ? 23.022  61.686  61.801 1.00 32.48 ? 772  HOH B O     1 
HETATM 8937 O O     . HOH V 8 .   ? 22.438  108.018 62.043 1.00 24.19 ? 773  HOH B O     1 
HETATM 8938 O O     . HOH V 8 .   ? 30.031  72.722  64.041 1.00 31.92 ? 774  HOH B O     1 
HETATM 8939 O O     . HOH V 8 .   ? 33.981  87.878  84.877 1.00 37.76 ? 775  HOH B O     1 
HETATM 8940 O O     . HOH V 8 .   ? 13.150  106.774 39.912 1.00 42.30 ? 776  HOH B O     1 
HETATM 8941 O O     . HOH V 8 .   ? 30.916  85.094  56.362 1.00 42.22 ? 777  HOH B O     1 
HETATM 8942 O O     . HOH V 8 .   ? 20.819  87.588  33.500 1.00 38.14 ? 778  HOH B O     1 
HETATM 8943 O O     . HOH V 8 .   ? 11.591  72.215  36.029 1.00 37.10 ? 779  HOH B O     1 
HETATM 8944 O O     . HOH V 8 .   ? 28.214  103.077 47.991 1.00 38.13 ? 780  HOH B O     1 
HETATM 8945 O O     . HOH V 8 .   ? 33.038  88.179  73.244 1.00 22.79 ? 781  HOH B O     1 
HETATM 8946 O O     . HOH V 8 .   ? 26.052  75.661  42.817 1.00 19.53 ? 782  HOH B O     1 
HETATM 8947 O O     . HOH V 8 .   ? 19.601  84.727  84.197 1.00 33.69 ? 783  HOH B O     1 
HETATM 8948 O O     . HOH V 8 .   ? 11.471  64.644  37.540 1.00 48.18 ? 784  HOH B O     1 
HETATM 8949 O O     . HOH V 8 .   ? 22.067  100.165 86.342 1.00 46.42 ? 785  HOH B O     1 
HETATM 8950 O O     . HOH V 8 .   ? 29.394  91.249  39.267 1.00 24.39 ? 786  HOH B O     1 
HETATM 8951 O O     . HOH V 8 .   ? 35.014  95.091  74.853 1.00 23.69 ? 787  HOH B O     1 
HETATM 8952 O O     . HOH V 8 .   ? 34.851  68.808  32.980 1.00 38.35 ? 788  HOH B O     1 
HETATM 8953 O O     . HOH V 8 .   ? 31.937  65.252  56.723 1.00 24.82 ? 789  HOH B O     1 
HETATM 8954 O O     . HOH V 8 .   ? 29.373  89.380  57.342 1.00 38.90 ? 790  HOH B O     1 
HETATM 8955 O O     . HOH V 8 .   ? 27.273  103.679 40.642 1.00 41.69 ? 791  HOH B O     1 
HETATM 8956 O O     . HOH V 8 .   ? 0.815   68.367  58.948 1.00 22.52 ? 792  HOH B O     1 
HETATM 8957 O O     . HOH V 8 .   ? 24.946  85.315  81.065 1.00 24.63 ? 793  HOH B O     1 
HETATM 8958 O O     . HOH V 8 .   ? 30.053  115.986 78.424 1.00 37.43 ? 794  HOH B O     1 
HETATM 8959 O O     . HOH V 8 .   ? 29.140  95.155  62.770 1.00 28.57 ? 795  HOH B O     1 
HETATM 8960 O O     . HOH V 8 .   ? 28.152  79.767  37.827 1.00 33.63 ? 796  HOH B O     1 
HETATM 8961 O O     . HOH V 8 .   ? 16.485  75.490  75.672 1.00 26.42 ? 797  HOH B O     1 
HETATM 8962 O O     . HOH V 8 .   ? 21.033  90.742  52.046 1.00 17.84 ? 798  HOH B O     1 
HETATM 8963 O O     . HOH V 8 .   ? -0.465  84.642  48.332 1.00 20.76 ? 799  HOH B O     1 
HETATM 8964 O O     . HOH V 8 .   ? 12.478  80.426  77.628 1.00 22.34 ? 800  HOH B O     1 
HETATM 8965 O O     . HOH V 8 .   ? 29.118  97.235  84.341 1.00 45.52 ? 801  HOH B O     1 
HETATM 8966 O O     . HOH V 8 .   ? -0.232  76.611  78.528 1.00 38.34 ? 802  HOH B O     1 
HETATM 8967 O O     . HOH V 8 .   ? 0.077   88.427  50.538 1.00 21.44 ? 803  HOH B O     1 
HETATM 8968 O O     . HOH V 8 .   ? 7.174   77.486  78.731 1.00 35.60 ? 804  HOH B O     1 
HETATM 8969 O O     . HOH V 8 .   ? 18.435  71.526  65.442 1.00 22.51 ? 805  HOH B O     1 
HETATM 8970 O O     . HOH V 8 .   ? 27.033  87.250  40.390 1.00 27.63 ? 806  HOH B O     1 
HETATM 8971 O O     . HOH V 8 .   ? 34.351  71.607  62.101 1.00 31.00 ? 807  HOH B O     1 
HETATM 8972 O O     . HOH V 8 .   ? 48.715  88.525  75.252 1.00 42.75 ? 808  HOH B O     1 
HETATM 8973 O O     . HOH V 8 .   ? 29.680  101.115 66.389 1.00 39.18 ? 809  HOH B O     1 
HETATM 8974 O O     . HOH V 8 .   ? 14.683  107.776 58.981 1.00 31.44 ? 810  HOH B O     1 
HETATM 8975 O O     . HOH V 8 .   ? 35.645  68.022  66.868 1.00 43.87 ? 811  HOH B O     1 
HETATM 8976 O O     . HOH V 8 .   ? 8.300   66.065  57.882 1.00 23.29 ? 812  HOH B O     1 
HETATM 8977 O O     . HOH V 8 .   ? 24.125  116.184 46.219 1.00 38.68 ? 813  HOH B O     1 
HETATM 8978 O O     . HOH V 8 .   ? 32.068  101.220 66.420 1.00 41.61 ? 814  HOH B O     1 
HETATM 8979 O O     . HOH V 8 .   ? 15.760  105.688 57.694 1.00 43.57 ? 815  HOH B O     1 
HETATM 8980 O O     . HOH V 8 .   ? 16.897  75.700  54.649 1.00 24.98 ? 816  HOH B O     1 
HETATM 8981 O O     . HOH V 8 .   ? 5.705   90.421  44.625 1.00 16.71 ? 817  HOH B O     1 
HETATM 8982 O O     . HOH V 8 .   ? 34.382  64.658  37.983 1.00 48.60 ? 818  HOH B O     1 
HETATM 8983 O O     . HOH V 8 .   ? 24.608  105.330 82.109 1.00 26.33 ? 819  HOH B O     1 
HETATM 8984 O O     . HOH V 8 .   ? 40.302  112.506 71.078 1.00 36.73 ? 820  HOH B O     1 
HETATM 8985 O O     . HOH V 8 .   ? 16.151  97.351  34.603 1.00 38.67 ? 821  HOH B O     1 
HETATM 8986 O O     . HOH V 8 .   ? 32.415  87.405  45.392 1.00 26.13 ? 822  HOH B O     1 
HETATM 8987 O O     . HOH V 8 .   ? 18.375  116.387 70.745 1.00 49.29 ? 823  HOH B O     1 
HETATM 8988 O O     . HOH V 8 .   ? 42.097  104.238 65.910 1.00 25.59 ? 824  HOH B O     1 
HETATM 8989 O O     . HOH V 8 .   ? 31.075  112.792 58.077 1.00 23.96 ? 825  HOH B O     1 
HETATM 8990 O O     . HOH V 8 .   ? 5.393   78.861  71.722 1.00 18.86 ? 826  HOH B O     1 
HETATM 8991 O O     . HOH V 8 .   ? 25.875  98.028  55.156 1.00 16.21 ? 827  HOH B O     1 
HETATM 8992 O O     . HOH V 8 .   ? 42.955  109.272 59.069 1.00 39.71 ? 828  HOH B O     1 
HETATM 8993 O O     . HOH V 8 .   ? 19.174  96.771  49.996 1.00 16.00 ? 829  HOH B O     1 
HETATM 8994 O O     . HOH V 8 .   ? 20.400  99.404  49.554 1.00 18.11 ? 830  HOH B O     1 
HETATM 8995 O O     . HOH V 8 .   ? 20.661  109.766 60.683 1.00 24.83 ? 831  HOH B O     1 
HETATM 8996 O O     . HOH V 8 .   ? 32.109  96.944  54.605 1.00 23.82 ? 832  HOH B O     1 
HETATM 8997 O O     . HOH V 8 .   ? 48.235  98.142  81.282 1.00 25.45 ? 833  HOH B O     1 
HETATM 8998 O O     . HOH V 8 .   ? 17.599  119.538 65.112 1.00 28.12 ? 834  HOH B O     1 
HETATM 8999 O O     . HOH V 8 .   ? 26.482  107.444 82.279 1.00 42.03 ? 835  HOH B O     1 
HETATM 9000 O O     . HOH V 8 .   ? 24.955  66.243  64.071 1.00 29.40 ? 836  HOH B O     1 
HETATM 9001 O O     . HOH V 8 .   ? 19.680  79.471  36.620 1.00 43.16 ? 837  HOH B O     1 
HETATM 9002 O O     . HOH V 8 .   ? 34.864  108.942 74.938 1.00 29.65 ? 838  HOH B O     1 
HETATM 9003 O O     . HOH V 8 .   ? 44.131  88.254  81.968 1.00 43.62 ? 839  HOH B O     1 
HETATM 9004 O O     . HOH V 8 .   ? 27.179  74.786  80.353 1.00 31.91 ? 840  HOH B O     1 
HETATM 9005 O O     . HOH V 8 .   ? 25.613  116.564 50.084 1.00 46.15 ? 841  HOH B O     1 
HETATM 9006 O O     . HOH V 8 .   ? 18.252  107.758 48.997 1.00 26.97 ? 842  HOH B O     1 
HETATM 9007 O O     . HOH V 8 .   ? 31.612  69.000  64.694 1.00 30.18 ? 843  HOH B O     1 
HETATM 9008 O O     . HOH V 8 .   ? 27.865  97.797  31.348 1.00 45.26 ? 844  HOH B O     1 
HETATM 9009 O O     . HOH V 8 .   ? 21.147  80.419  61.576 1.00 23.63 ? 845  HOH B O     1 
HETATM 9010 O O     . HOH V 8 .   ? 31.493  75.550  55.874 1.00 22.57 ? 846  HOH B O     1 
HETATM 9011 O O     . HOH V 8 .   ? 9.733   75.295  71.197 1.00 22.48 ? 847  HOH B O     1 
HETATM 9012 O O     . HOH V 8 .   ? 24.443  120.699 68.216 1.00 43.69 ? 848  HOH B O     1 
HETATM 9013 O O     . HOH V 8 .   ? 17.648  111.509 72.634 1.00 25.93 ? 849  HOH B O     1 
HETATM 9014 O O     . HOH V 8 .   ? 23.192  82.961  68.993 1.00 19.87 ? 850  HOH B O     1 
HETATM 9015 O O     . HOH V 8 .   ? 15.578  61.936  55.738 1.00 46.06 ? 851  HOH B O     1 
HETATM 9016 O O     . HOH V 8 .   ? 10.757  74.034  75.627 1.00 32.30 ? 852  HOH B O     1 
HETATM 9017 O O     . HOH V 8 .   ? 17.031  90.277  62.153 1.00 20.00 ? 853  HOH B O     1 
HETATM 9018 O O     . HOH V 8 .   ? 3.484   81.225  41.691 1.00 17.34 ? 854  HOH B O     1 
HETATM 9019 O O     . HOH V 8 .   ? 6.345   84.989  37.082 1.00 19.43 ? 855  HOH B O     1 
HETATM 9020 O O     . HOH V 8 .   ? 43.194  91.654  65.886 1.00 32.23 ? 856  HOH B O     1 
HETATM 9021 O O     . HOH V 8 .   ? 11.413  77.585  78.192 1.00 41.25 ? 857  HOH B O     1 
HETATM 9022 O O     . HOH V 8 .   ? 40.001  115.306 70.681 1.00 43.07 ? 858  HOH B O     1 
HETATM 9023 O O     . HOH V 8 .   ? 26.653  100.611 45.001 1.00 30.46 ? 859  HOH B O     1 
HETATM 9024 O O     . HOH V 8 .   ? 35.534  74.389  56.335 1.00 36.98 ? 860  HOH B O     1 
HETATM 9025 O O     . HOH V 8 .   ? 30.018  103.688 38.680 1.00 43.72 ? 861  HOH B O     1 
HETATM 9026 O O     . HOH V 8 .   ? 30.826  78.673  62.634 1.00 22.55 ? 862  HOH B O     1 
HETATM 9027 O O     . HOH V 8 .   ? 42.525  78.861  66.269 1.00 38.83 ? 863  HOH B O     1 
HETATM 9028 O O     . HOH V 8 .   ? 33.985  95.066  45.250 1.00 43.07 ? 864  HOH B O     1 
HETATM 9029 O O     . HOH V 8 .   ? 36.493  105.917 54.626 1.00 27.89 ? 865  HOH B O     1 
HETATM 9030 O O     . HOH V 8 .   ? 21.962  100.803 51.117 1.00 18.59 ? 866  HOH B O     1 
HETATM 9031 O O     . HOH V 8 .   ? 15.569  79.733  55.183 1.00 19.31 ? 867  HOH B O     1 
HETATM 9032 O O     . HOH V 8 .   ? 24.261  77.889  59.760 1.00 20.55 ? 868  HOH B O     1 
HETATM 9033 O O     . HOH V 8 .   ? 33.585  109.835 83.029 1.00 45.38 ? 869  HOH B O     1 
HETATM 9034 O O     . HOH V 8 .   ? 20.758  71.891  66.878 1.00 21.15 ? 870  HOH B O     1 
HETATM 9035 O O     . HOH V 8 .   ? 16.776  90.767  58.063 1.00 18.64 ? 871  HOH B O     1 
HETATM 9036 O O     . HOH V 8 .   ? 9.606   96.167  37.353 1.00 35.95 ? 872  HOH B O     1 
HETATM 9037 O O     . HOH V 8 .   ? 32.892  95.553  58.601 1.00 43.87 ? 873  HOH B O     1 
HETATM 9038 O O     . HOH V 8 .   ? 41.384  82.822  62.242 1.00 48.88 ? 874  HOH B O     1 
HETATM 9039 O O     . HOH V 8 .   ? 11.998  102.843 64.130 1.00 33.08 ? 875  HOH B O     1 
HETATM 9040 O O     . HOH V 8 .   ? 11.834  82.617  79.294 1.00 26.76 ? 876  HOH B O     1 
HETATM 9041 O O     . HOH V 8 .   ? 34.086  103.586 84.184 1.00 38.78 ? 877  HOH B O     1 
HETATM 9042 O O     . HOH V 8 .   ? 29.194  83.764  42.603 1.00 31.11 ? 878  HOH B O     1 
HETATM 9043 O O     . HOH V 8 .   ? 37.553  108.774 71.992 1.00 27.32 ? 879  HOH B O     1 
HETATM 9044 O O     . HOH V 8 .   ? 26.074  72.035  73.515 1.00 33.43 ? 880  HOH B O     1 
HETATM 9045 O O     . HOH V 8 .   ? 36.831  115.424 67.866 1.00 38.71 ? 881  HOH B O     1 
HETATM 9046 O O     . HOH V 8 .   ? 12.335  93.091  61.542 1.00 46.96 ? 882  HOH B O     1 
HETATM 9047 O O     . HOH V 8 .   ? 42.482  85.087  68.253 1.00 22.57 ? 883  HOH B O     1 
HETATM 9048 O O     . HOH V 8 .   ? 12.511  95.918  33.580 1.00 32.38 ? 884  HOH B O     1 
HETATM 9049 O O     . HOH V 8 .   ? 17.208  80.689  39.717 1.00 21.40 ? 885  HOH B O     1 
HETATM 9050 O O     . HOH V 8 .   ? 17.941  78.678  62.468 1.00 19.24 ? 886  HOH B O     1 
HETATM 9051 O O     . HOH V 8 .   ? 6.566   88.714  34.144 1.00 36.61 ? 887  HOH B O     1 
HETATM 9052 O O     . HOH V 8 .   ? 16.793  105.279 42.169 1.00 28.72 ? 888  HOH B O     1 
HETATM 9053 O O     . HOH V 8 .   ? 14.507  94.414  82.260 1.00 34.98 ? 889  HOH B O     1 
HETATM 9054 O O     . HOH V 8 .   ? 3.471   85.790  49.560 1.00 23.69 ? 890  HOH B O     1 
HETATM 9055 O O     . HOH V 8 .   ? 25.446  71.787  36.729 1.00 25.31 ? 891  HOH B O     1 
HETATM 9056 O O     . HOH V 8 .   ? 12.908  77.744  53.453 1.00 24.19 ? 892  HOH B O     1 
HETATM 9057 O O     . HOH V 8 .   ? 15.038  104.120 61.028 1.00 44.58 ? 893  HOH B O     1 
HETATM 9058 O O     . HOH V 8 .   ? 40.631  99.930  66.122 1.00 26.99 ? 894  HOH B O     1 
HETATM 9059 O O     . HOH V 8 .   ? 19.702  108.897 43.422 1.00 28.65 ? 895  HOH B O     1 
HETATM 9060 O O     . HOH V 8 .   ? 20.602  60.879  61.555 1.00 35.55 ? 896  HOH B O     1 
HETATM 9061 O O     . HOH V 8 .   ? 48.545  106.181 68.797 1.00 37.18 ? 897  HOH B O     1 
HETATM 9062 O O     . HOH V 8 .   ? 43.663  102.170 64.630 1.00 24.35 ? 898  HOH B O     1 
HETATM 9063 O O     . HOH V 8 .   ? 52.711  93.628  75.271 1.00 41.87 ? 899  HOH B O     1 
HETATM 9064 O O     . HOH V 8 .   ? 22.385  86.299  46.415 1.00 18.46 ? 900  HOH B O     1 
HETATM 9065 O O     . HOH V 8 .   ? 18.377  88.803  32.846 1.00 31.76 ? 901  HOH B O     1 
HETATM 9066 O O     . HOH V 8 .   ? 12.428  60.286  54.132 1.00 41.97 ? 902  HOH B O     1 
HETATM 9067 O O     . HOH V 8 .   ? 16.752  79.238  81.367 1.00 34.39 ? 903  HOH B O     1 
HETATM 9068 O O     . HOH V 8 .   ? 20.702  68.641  58.929 1.00 20.31 ? 904  HOH B O     1 
HETATM 9069 O O     . HOH V 8 .   ? 34.339  70.887  40.065 1.00 49.93 ? 905  HOH B O     1 
HETATM 9070 O O     . HOH V 8 .   ? 36.312  87.295  72.110 1.00 28.79 ? 906  HOH B O     1 
HETATM 9071 O O     . HOH V 8 .   ? 26.026  110.443 40.981 1.00 40.46 ? 907  HOH B O     1 
HETATM 9072 O O     . HOH V 8 .   ? 10.163  90.430  53.307 1.00 18.30 ? 908  HOH B O     1 
HETATM 9073 O O     . HOH V 8 .   ? 34.717  95.424  81.471 1.00 39.78 ? 909  HOH B O     1 
HETATM 9074 O O     . HOH V 8 .   ? 34.498  101.577 82.255 1.00 30.17 ? 910  HOH B O     1 
HETATM 9075 O O     . HOH V 8 .   ? 7.057   89.267  48.279 1.00 18.24 ? 911  HOH B O     1 
HETATM 9076 O O     . HOH V 8 .   ? -0.007  86.692  44.973 1.00 19.61 ? 912  HOH B O     1 
HETATM 9077 O O     . HOH V 8 .   ? 39.062  85.351  83.747 1.00 46.47 ? 913  HOH B O     1 
HETATM 9078 O O     . HOH V 8 .   ? 38.409  94.059  52.427 1.00 33.37 ? 914  HOH B O     1 
HETATM 9079 O O     . HOH V 8 .   ? 40.190  102.381 65.317 1.00 24.12 ? 915  HOH B O     1 
HETATM 9080 O O     . HOH V 8 .   ? 28.232  100.990 62.006 1.00 22.59 ? 916  HOH B O     1 
HETATM 9081 O O     . HOH V 8 .   ? 22.499  97.095  62.020 1.00 25.30 ? 917  HOH B O     1 
HETATM 9082 O O     . HOH V 8 .   ? 11.836  98.032  77.880 1.00 33.39 ? 918  HOH B O     1 
HETATM 9083 O O     . HOH V 8 .   ? 52.568  91.715  69.435 1.00 44.43 ? 919  HOH B O     1 
HETATM 9084 O O     . HOH V 8 .   ? 39.547  80.199  77.602 1.00 40.24 ? 920  HOH B O     1 
HETATM 9085 O O     . HOH V 8 .   ? 0.119   69.426  72.119 1.00 40.87 ? 921  HOH B O     1 
HETATM 9086 O O     . HOH V 8 .   ? 21.615  77.695  58.990 1.00 19.22 ? 922  HOH B O     1 
HETATM 9087 O O     . HOH V 8 .   ? 31.857  100.017 85.676 1.00 47.69 ? 923  HOH B O     1 
HETATM 9088 O O     . HOH V 8 .   ? 41.519  90.853  83.525 1.00 46.93 ? 924  HOH B O     1 
HETATM 9089 O O     . HOH V 8 .   ? 0.908   73.385  73.170 1.00 23.79 ? 925  HOH B O     1 
HETATM 9090 O O     . HOH V 8 .   ? 26.695  100.352 47.807 1.00 18.87 ? 926  HOH B O     1 
HETATM 9091 O O     . HOH V 8 .   ? 46.193  102.051 63.000 1.00 38.09 ? 927  HOH B O     1 
HETATM 9092 O O     . HOH V 8 .   ? 24.619  102.699 84.318 1.00 45.56 ? 928  HOH B O     1 
HETATM 9093 O O     . HOH V 8 .   ? 1.812   91.098  30.295 1.00 43.24 ? 929  HOH B O     1 
HETATM 9094 O O     . HOH V 8 .   ? 29.176  66.887  71.769 1.00 36.32 ? 930  HOH B O     1 
HETATM 9095 O O     . HOH V 8 .   ? 17.641  53.666  53.155 1.00 37.42 ? 931  HOH B O     1 
HETATM 9096 O O     . HOH V 8 .   ? 33.809  94.078  79.241 1.00 32.37 ? 932  HOH B O     1 
HETATM 9097 O O     . HOH V 8 .   ? 20.438  53.921  59.626 1.00 48.49 ? 933  HOH B O     1 
HETATM 9098 O O     . HOH V 8 .   ? 27.908  57.933  39.090 1.00 44.80 ? 934  HOH B O     1 
HETATM 9099 O O     . HOH V 8 .   ? 36.986  91.777  77.850 1.00 27.39 ? 935  HOH B O     1 
HETATM 9100 O O     . HOH V 8 .   ? 18.108  82.735  75.483 1.00 19.63 ? 936  HOH B O     1 
HETATM 9101 O O     . HOH V 8 .   ? 19.529  74.940  55.533 1.00 27.06 ? 937  HOH B O     1 
HETATM 9102 O O     . HOH V 8 .   ? 10.629  109.395 69.129 1.00 24.79 ? 938  HOH B O     1 
HETATM 9103 O O     . HOH V 8 .   ? 30.255  117.429 74.748 1.00 45.78 ? 939  HOH B O     1 
HETATM 9104 O O     . HOH V 8 .   ? 18.945  112.364 49.241 1.00 26.21 ? 940  HOH B O     1 
HETATM 9105 O O     . HOH V 8 .   ? 16.773  82.150  72.892 1.00 20.75 ? 941  HOH B O     1 
HETATM 9106 O O     . HOH V 8 .   ? 7.154   61.835  65.133 1.00 48.33 ? 942  HOH B O     1 
HETATM 9107 O O     . HOH V 8 .   ? 7.386   92.755  54.465 1.00 41.20 ? 943  HOH B O     1 
HETATM 9108 O O     . HOH V 8 .   ? 21.112  93.576  51.519 1.00 19.21 ? 944  HOH B O     1 
HETATM 9109 O O     . HOH V 8 .   ? 3.252   79.206  78.728 1.00 24.32 ? 945  HOH B O     1 
HETATM 9110 O O     . HOH V 8 .   ? 15.238  74.296  52.936 1.00 24.23 ? 946  HOH B O     1 
HETATM 9111 O O     . HOH V 8 .   ? 40.568  91.034  56.948 1.00 49.71 ? 947  HOH B O     1 
HETATM 9112 O O     . HOH V 8 .   ? 30.422  103.314 46.644 1.00 33.66 ? 948  HOH B O     1 
HETATM 9113 O O     . HOH V 8 .   ? 19.071  95.263  52.217 1.00 17.27 ? 949  HOH B O     1 
HETATM 9114 O O     . HOH V 8 .   ? 1.751   86.064  47.450 1.00 23.22 ? 950  HOH B O     1 
HETATM 9115 O O     . HOH V 8 .   ? 11.253  69.767  35.929 1.00 35.64 ? 951  HOH B O     1 
HETATM 9116 O O     . HOH V 8 .   ? 14.184  67.214  71.346 1.00 49.40 ? 952  HOH B O     1 
HETATM 9117 O O     . HOH V 8 .   ? 7.819   97.490  36.015 1.00 33.21 ? 953  HOH B O     1 
HETATM 9118 O O     . HOH V 8 .   ? 31.810  62.086  53.626 1.00 41.26 ? 954  HOH B O     1 
HETATM 9119 O O     . HOH V 8 .   ? 23.938  63.272  32.891 1.00 45.87 ? 955  HOH B O     1 
HETATM 9120 O O     . HOH V 8 .   ? 4.646   76.657  78.539 1.00 24.40 ? 956  HOH B O     1 
HETATM 9121 O O     . HOH V 8 .   ? 4.310   60.725  54.655 1.00 49.09 ? 957  HOH B O     1 
HETATM 9122 O O     . HOH V 8 .   ? 34.342  96.626  47.439 1.00 40.57 ? 958  HOH B O     1 
HETATM 9123 O O     . HOH V 8 .   ? 23.839  50.733  54.947 1.00 41.10 ? 959  HOH B O     1 
HETATM 9124 O O     . HOH V 8 .   ? 34.333  90.812  84.085 1.00 46.68 ? 960  HOH B O     1 
HETATM 9125 O O     . HOH V 8 .   ? 32.963  104.720 48.057 1.00 43.03 ? 961  HOH B O     1 
HETATM 9126 O O     . HOH V 8 .   ? 20.000  94.896  35.040 1.00 31.17 ? 962  HOH B O     1 
HETATM 9127 O O     . HOH V 8 .   ? 19.599  73.069  33.701 1.00 44.22 ? 963  HOH B O     1 
HETATM 9128 O O     . HOH V 8 .   ? 26.887  98.066  85.759 1.00 44.79 ? 964  HOH B O     1 
HETATM 9129 O O     . HOH V 8 .   ? 8.170   91.668  37.039 1.00 30.83 ? 965  HOH B O     1 
HETATM 9130 O O     . HOH V 8 .   ? 47.413  88.879  70.485 1.00 24.54 ? 966  HOH B O     1 
HETATM 9131 O O     . HOH V 8 .   ? 24.308  120.501 62.441 1.00 32.78 ? 967  HOH B O     1 
HETATM 9132 O O     . HOH V 8 .   ? 19.167  92.483  33.262 1.00 40.05 ? 968  HOH B O     1 
HETATM 9133 O O     . HOH V 8 .   ? 7.321   76.498  70.531 1.00 19.53 ? 969  HOH B O     1 
HETATM 9134 O O     . HOH V 8 .   ? 16.036  98.398  56.837 1.00 28.45 ? 970  HOH B O     1 
HETATM 9135 O O     . HOH V 8 .   ? -1.160  73.903  75.632 1.00 50.07 ? 971  HOH B O     1 
HETATM 9136 O O     . HOH V 8 .   ? 31.417  78.730  65.273 1.00 21.83 ? 972  HOH B O     1 
HETATM 9137 O O     . HOH V 8 .   ? 11.876  64.025  59.336 1.00 27.28 ? 973  HOH B O     1 
HETATM 9138 O O     . HOH V 8 .   ? 51.331  92.388  80.373 1.00 34.23 ? 974  HOH B O     1 
HETATM 9139 O O     . HOH V 8 .   ? 9.372   63.640  58.229 1.00 27.23 ? 975  HOH B O     1 
HETATM 9140 O O     . HOH V 8 .   ? 34.781  67.768  75.455 1.00 45.99 ? 976  HOH B O     1 
HETATM 9141 O O     . HOH V 8 .   ? 16.399  90.631  86.774 1.00 44.70 ? 977  HOH B O     1 
HETATM 9142 O O     . HOH V 8 .   ? 15.924  76.047  35.415 1.00 25.93 ? 978  HOH B O     1 
HETATM 9143 O O     . HOH V 8 .   ? 30.699  67.402  35.293 1.00 33.54 ? 979  HOH B O     1 
HETATM 9144 O O     . HOH V 8 .   ? 24.814  87.766  36.211 1.00 29.39 ? 980  HOH B O     1 
HETATM 9145 O O     . HOH V 8 .   ? 35.088  114.441 76.775 1.00 47.13 ? 981  HOH B O     1 
HETATM 9146 O O     . HOH V 8 .   ? 27.446  55.412  58.614 1.00 40.28 ? 982  HOH B O     1 
HETATM 9147 O O     . HOH V 8 .   ? 2.675   72.624  41.644 1.00 33.37 ? 983  HOH B O     1 
HETATM 9148 O O     . HOH V 8 .   ? 28.274  69.715  34.409 1.00 33.95 ? 984  HOH B O     1 
HETATM 9149 O O     . HOH V 8 .   ? 29.265  119.083 65.446 1.00 41.08 ? 985  HOH B O     1 
HETATM 9150 O O     . HOH V 8 .   ? 16.365  102.176 81.313 1.00 26.49 ? 986  HOH B O     1 
HETATM 9151 O O     . HOH V 8 .   ? 23.123  85.691  78.899 1.00 22.84 ? 987  HOH B O     1 
HETATM 9152 O O     . HOH V 8 .   ? 19.423  108.213 81.428 1.00 36.45 ? 988  HOH B O     1 
HETATM 9153 O O     . HOH V 8 .   ? 5.970   87.218  54.829 1.00 22.05 ? 989  HOH B O     1 
HETATM 9154 O O     . HOH V 8 .   ? 16.677  92.218  33.146 1.00 40.16 ? 990  HOH B O     1 
HETATM 9155 O O     . HOH V 8 .   ? 30.612  76.885  37.596 1.00 44.49 ? 991  HOH B O     1 
HETATM 9156 O O     . HOH V 8 .   ? 40.693  83.556  72.157 1.00 38.48 ? 992  HOH B O     1 
HETATM 9157 O O     . HOH V 8 .   ? 31.380  102.272 84.228 1.00 32.29 ? 993  HOH B O     1 
HETATM 9158 O O     . HOH V 8 .   ? 32.193  98.150  76.961 1.00 27.83 ? 994  HOH B O     1 
HETATM 9159 O O     . HOH V 8 .   ? 17.668  80.837  56.865 1.00 30.90 ? 995  HOH B O     1 
HETATM 9160 O O     . HOH V 8 .   ? 31.510  59.355  54.581 1.00 45.05 ? 996  HOH B O     1 
HETATM 9161 O O     . HOH V 8 .   ? 33.094  63.027  55.527 1.00 30.22 ? 997  HOH B O     1 
HETATM 9162 O O     . HOH V 8 .   ? 17.522  78.827  37.101 1.00 28.10 ? 998  HOH B O     1 
HETATM 9163 O O     . HOH V 8 .   ? 24.094  71.827  71.754 1.00 41.62 ? 999  HOH B O     1 
HETATM 9164 O O     . HOH V 8 .   ? 7.541   87.218  37.629 1.00 26.30 ? 1000 HOH B O     1 
HETATM 9165 O O     . HOH V 8 .   ? 33.631  97.818  41.579 1.00 40.91 ? 1001 HOH B O     1 
HETATM 9166 O O     . HOH V 8 .   ? 3.342   66.767  46.429 1.00 35.26 ? 1002 HOH B O     1 
HETATM 9167 O O     . HOH V 8 .   ? 5.704   70.260  74.557 1.00 44.24 ? 1003 HOH B O     1 
HETATM 9168 O O     . HOH V 8 .   ? 21.527  95.262  49.286 1.00 15.64 ? 1004 HOH B O     1 
HETATM 9169 O O     . HOH V 8 .   ? 40.591  102.237 58.177 1.00 34.01 ? 1005 HOH B O     1 
HETATM 9170 O O     . HOH V 8 .   ? 9.030   64.789  45.077 1.00 33.53 ? 1006 HOH B O     1 
HETATM 9171 O O     . HOH V 8 .   ? 20.611  72.523  70.172 1.00 20.58 ? 1007 HOH B O     1 
HETATM 9172 O O     . HOH V 8 .   ? 15.597  109.696 56.209 1.00 35.33 ? 1008 HOH B O     1 
HETATM 9173 O O     . HOH V 8 .   ? 25.779  58.415  35.758 1.00 28.90 ? 1009 HOH B O     1 
HETATM 9174 O O     . HOH V 8 .   ? 6.120   97.066  31.751 1.00 28.88 ? 1010 HOH B O     1 
HETATM 9175 O O     . HOH V 8 .   ? 31.977  84.673  44.421 1.00 41.50 ? 1011 HOH B O     1 
HETATM 9176 O O     . HOH V 8 .   ? 18.130  100.227 35.451 1.00 29.16 ? 1012 HOH B O     1 
HETATM 9177 O O     . HOH V 8 .   ? 5.096   96.364  48.963 1.00 17.82 ? 1013 HOH B O     1 
HETATM 9178 O O     . HOH V 8 .   ? 31.537  67.669  72.372 1.00 31.83 ? 1014 HOH B O     1 
HETATM 9179 O O     . HOH V 8 .   ? 19.303  95.306  64.606 1.00 30.49 ? 1015 HOH B O     1 
HETATM 9180 O O     . HOH V 8 .   ? 29.958  71.820  34.304 1.00 40.68 ? 1016 HOH B O     1 
HETATM 9181 O O     . HOH V 8 .   ? 23.579  69.722  68.898 1.00 47.28 ? 1017 HOH B O     1 
HETATM 9182 O O     . HOH V 8 .   ? 9.089   93.771  39.108 1.00 26.40 ? 1018 HOH B O     1 
HETATM 9183 O O     . HOH V 8 .   ? 0.029   74.672  68.501 1.00 25.65 ? 1019 HOH B O     1 
HETATM 9184 O O     . HOH V 8 .   ? 47.117  103.886 61.041 1.00 38.30 ? 1020 HOH B O     1 
HETATM 9185 O O     . HOH V 8 .   ? 4.908   70.559  49.102 1.00 36.30 ? 1021 HOH B O     1 
HETATM 9186 O O     . HOH V 8 .   ? 38.906  95.308  81.918 1.00 31.06 ? 1022 HOH B O     1 
HETATM 9187 O O     . HOH V 8 .   ? 49.927  98.183  64.780 1.00 41.04 ? 1023 HOH B O     1 
HETATM 9188 O O     . HOH V 8 .   ? 11.885  75.776  36.698 1.00 36.13 ? 1024 HOH B O     1 
HETATM 9189 O O     . HOH V 8 .   ? 31.152  71.633  65.879 1.00 33.08 ? 1025 HOH B O     1 
HETATM 9190 O O     . HOH V 8 .   ? 41.547  82.008  76.839 1.00 54.74 ? 1026 HOH B O     1 
HETATM 9191 O O     . HOH V 8 .   ? 2.815   69.252  65.675 1.00 39.16 ? 1027 HOH B O     1 
HETATM 9192 O O     . HOH V 8 .   ? 22.797  95.523  85.425 1.00 41.28 ? 1028 HOH B O     1 
HETATM 9193 O O     . HOH V 8 .   ? 38.798  86.661  73.255 1.00 32.12 ? 1029 HOH B O     1 
HETATM 9194 O O     . HOH V 8 .   ? 8.306   71.871  37.180 1.00 32.31 ? 1030 HOH B O     1 
HETATM 9195 O O     . HOH V 8 .   ? 48.501  107.078 50.897 1.00 31.34 ? 1031 HOH B O     1 
HETATM 9196 O O     . HOH V 8 .   ? 8.780   109.234 62.416 1.00 30.21 ? 1032 HOH B O     1 
HETATM 9197 O O     . HOH V 8 .   ? 19.118  61.867  37.883 1.00 28.45 ? 1033 HOH B O     1 
HETATM 9198 O O     . HOH V 8 .   ? 13.404  67.696  57.831 1.00 31.23 ? 1034 HOH B O     1 
HETATM 9199 O O     . HOH V 8 .   ? 48.300  85.757  82.491 1.00 46.13 ? 1035 HOH B O     1 
HETATM 9200 O O     . HOH V 8 .   ? 28.757  116.501 53.582 1.00 32.69 ? 1036 HOH B O     1 
HETATM 9201 O O     . HOH V 8 .   ? 26.607  106.378 34.871 1.00 30.44 ? 1037 HOH B O     1 
HETATM 9202 O O     . HOH V 8 .   ? 28.623  105.658 83.696 1.00 50.17 ? 1038 HOH B O     1 
HETATM 9203 O O     . HOH V 8 .   ? 11.804  107.726 75.220 1.00 40.75 ? 1039 HOH B O     1 
HETATM 9204 O O     . HOH V 8 .   ? 15.876  101.856 35.409 1.00 34.66 ? 1040 HOH B O     1 
HETATM 9205 O O     . HOH V 8 .   ? 41.465  110.197 81.036 1.00 44.20 ? 1041 HOH B O     1 
HETATM 9206 O O     . HOH V 8 .   ? 33.918  65.172  34.054 1.00 41.26 ? 1042 HOH B O     1 
HETATM 9207 O O     . HOH V 8 .   ? 21.029  97.072  34.876 1.00 39.75 ? 1043 HOH B O     1 
HETATM 9208 O O     . HOH V 8 .   ? 14.814  63.709  39.445 1.00 46.12 ? 1044 HOH B O     1 
HETATM 9209 O O     . HOH V 8 .   ? -1.123  73.106  64.131 1.00 28.12 ? 1045 HOH B O     1 
HETATM 9210 O O     . HOH V 8 .   ? 19.150  81.005  63.209 1.00 21.48 ? 1046 HOH B O     1 
HETATM 9211 O O     . HOH V 8 .   ? 31.959  70.011  74.217 1.00 44.68 ? 1047 HOH B O     1 
HETATM 9212 O O     . HOH V 8 .   ? 35.258  62.171  68.403 1.00 44.94 ? 1048 HOH B O     1 
HETATM 9213 O O     . HOH V 8 .   ? 20.016  96.905  62.824 1.00 32.89 ? 1049 HOH B O     1 
HETATM 9214 O O     . HOH V 8 .   ? 27.649  114.785 51.699 1.00 25.86 ? 1050 HOH B O     1 
HETATM 9215 O O     . HOH V 8 .   ? 4.996   93.840  55.288 1.00 50.86 ? 1051 HOH B O     1 
HETATM 9216 O O     . HOH V 8 .   ? 26.099  119.635 60.907 1.00 32.70 ? 1052 HOH B O     1 
HETATM 9217 O O     . HOH V 8 .   ? 22.409  67.356  65.851 1.00 47.28 ? 1053 HOH B O     1 
HETATM 9218 O O     . HOH V 8 .   ? 11.783  78.509  37.296 1.00 31.51 ? 1054 HOH B O     1 
HETATM 9219 O O     . HOH V 8 .   ? 13.014  103.548 80.318 1.00 40.62 ? 1055 HOH B O     1 
HETATM 9220 O O     . HOH V 8 .   ? 33.584  67.510  65.338 1.00 49.00 ? 1056 HOH B O     1 
HETATM 9221 O O     . HOH V 8 .   ? 30.580  102.887 34.939 1.00 29.76 ? 1057 HOH B O     1 
HETATM 9222 O O     . HOH V 8 .   ? 54.322  90.664  81.602 1.00 47.88 ? 1058 HOH B O     1 
HETATM 9223 O O     . HOH V 8 .   ? 34.561  64.623  45.105 1.00 35.95 ? 1059 HOH B O     1 
HETATM 9224 O O     . HOH V 8 .   ? 2.675   71.863  45.680 1.00 27.92 ? 1060 HOH B O     1 
HETATM 9225 O O     . HOH V 8 .   ? 14.769  65.644  66.842 1.00 44.93 ? 1061 HOH B O     1 
HETATM 9226 O O     . HOH V 8 .   ? 26.574  103.951 43.142 1.00 44.11 ? 1062 HOH B O     1 
HETATM 9227 O O     . HOH V 8 .   ? 7.711   61.423  47.539 1.00 49.25 ? 1063 HOH B O     1 
HETATM 9228 O O     . HOH V 8 .   ? 5.256   85.677  34.479 1.00 33.88 ? 1064 HOH B O     1 
HETATM 9229 O O     . HOH V 8 .   ? 15.110  96.145  62.273 1.00 40.89 ? 1065 HOH B O     1 
HETATM 9230 O O     . HOH V 8 .   ? 48.284  106.277 61.466 1.00 49.51 ? 1066 HOH B O     1 
HETATM 9231 O O     . HOH V 8 .   ? 17.172  100.579 60.206 1.00 53.68 ? 1067 HOH B O     1 
HETATM 9232 O O     . HOH V 8 .   ? 15.947  92.731  61.916 1.00 29.98 ? 1068 HOH B O     1 
HETATM 9233 O O     . HOH V 8 .   ? 47.801  87.446  72.817 1.00 43.56 ? 1069 HOH B O     1 
HETATM 9234 O O     . HOH V 8 .   ? 41.030  107.934 76.521 1.00 35.28 ? 1070 HOH B O     1 
HETATM 9235 O O     . HOH V 8 .   ? 35.202  68.945  60.908 1.00 48.15 ? 1071 HOH B O     1 
HETATM 9236 O O     . HOH V 8 .   ? 8.278   89.632  55.240 1.00 37.92 ? 1072 HOH B O     1 
HETATM 9237 O O     . HOH V 8 .   ? 28.454  60.540  42.401 1.00 46.03 ? 1073 HOH B O     1 
HETATM 9238 O O     . HOH V 8 .   ? 39.724  75.066  62.714 1.00 50.01 ? 1074 HOH B O     1 
HETATM 9239 O O     . HOH V 8 .   ? 27.082  85.861  36.521 1.00 44.91 ? 1075 HOH B O     1 
HETATM 9240 O O     . HOH V 8 .   ? 26.428  110.986 48.461 1.00 42.95 ? 1076 HOH B O     1 
HETATM 9241 O O     . HOH V 8 .   ? 56.570  88.915  78.660 1.00 51.39 ? 1077 HOH B O     1 
HETATM 9242 O O     . HOH V 8 .   ? 8.674   65.299  38.107 1.00 44.46 ? 1078 HOH B O     1 
HETATM 9243 O O     . HOH V 8 .   ? 48.825  88.050  68.421 1.00 37.66 ? 1079 HOH B O     1 
HETATM 9244 O O     . HOH V 8 .   ? 17.874  110.021 47.344 1.00 49.42 ? 1080 HOH B O     1 
HETATM 9245 O O     . HOH V 8 .   ? 23.423  54.370  41.082 1.00 43.92 ? 1081 HOH B O     1 
HETATM 9246 O O     . HOH V 8 .   ? 16.523  93.128  83.666 1.00 48.16 ? 1082 HOH B O     1 
HETATM 9247 O O     . HOH V 8 .   ? 7.732   65.102  40.603 1.00 36.44 ? 1083 HOH B O     1 
HETATM 9248 O O     . HOH V 8 .   ? 39.109  115.052 67.346 1.00 43.40 ? 1084 HOH B O     1 
HETATM 9249 O O     . HOH V 8 .   ? 33.824  86.570  47.469 1.00 40.23 ? 1085 HOH B O     1 
HETATM 9250 O O     . HOH V 8 .   ? 18.160  95.047  85.470 1.00 42.28 ? 1086 HOH B O     1 
HETATM 9251 O O     . HOH V 8 .   ? 1.967   85.831  30.150 1.00 45.86 ? 1087 HOH B O     1 
HETATM 9252 O O     . HOH V 8 .   ? 34.159  95.934  77.105 1.00 26.86 ? 1088 HOH B O     1 
HETATM 9253 O O     . HOH V 8 .   ? 7.101   65.919  49.225 1.00 26.15 ? 1089 HOH B O     1 
HETATM 9254 O O     . HOH V 8 .   ? 37.463  94.959  84.153 1.00 56.84 ? 1090 HOH B O     1 
HETATM 9255 O O     . HOH V 8 .   ? 19.995  80.053  84.003 1.00 43.66 ? 1091 HOH B O     1 
HETATM 9256 O O     . HOH V 8 .   ? 7.602   64.105  47.023 1.00 34.09 ? 1092 HOH B O     1 
HETATM 9257 O O     . HOH V 8 .   ? 4.673   68.260  66.964 1.00 50.50 ? 1093 HOH B O     1 
HETATM 9258 O O     . HOH V 8 .   ? 14.291  79.920  81.898 1.00 40.81 ? 1094 HOH B O     1 
HETATM 9259 O O     . HOH V 8 .   ? 9.335   60.383  45.913 1.00 43.73 ? 1095 HOH B O     1 
HETATM 9260 O O     . HOH V 8 .   ? 27.226  72.576  79.092 1.00 41.50 ? 1096 HOH B O     1 
HETATM 9261 O O     . HOH V 8 .   ? 41.530  82.987  69.505 1.00 26.27 ? 1097 HOH B O     1 
HETATM 9262 O O     . HOH V 8 .   ? 53.625  103.255 66.546 1.00 39.51 ? 1098 HOH B O     1 
HETATM 9263 O O     . HOH V 8 .   ? 1.736   70.374  42.434 1.00 34.69 ? 1099 HOH B O     1 
HETATM 9264 O O     . HOH V 8 .   ? 7.378   66.981  36.752 1.00 41.58 ? 1100 HOH B O     1 
HETATM 9265 O O     . HOH V 8 .   ? 19.901  70.019  33.330 1.00 45.94 ? 1101 HOH B O     1 
HETATM 9266 O O     . HOH V 8 .   ? 0.920   67.827  46.543 1.00 43.92 ? 1102 HOH B O     1 
HETATM 9267 O O     . HOH V 8 .   ? 18.856  68.465  34.828 1.00 50.64 ? 1103 HOH B O     1 
HETATM 9268 O O     . HOH V 8 .   ? 0.196   66.975  56.841 1.00 40.71 ? 1104 HOH B O     1 
HETATM 9269 O O     . HOH V 8 .   ? 1.041   70.025  44.922 1.00 44.46 ? 1105 HOH B O     1 
HETATM 9270 O O     . HOH V 8 .   ? 19.736  105.911 82.454 1.00 48.60 ? 1106 HOH B O     1 
HETATM 9271 O O     . HOH V 8 .   ? 36.116  63.964  35.107 1.00 42.40 ? 1107 HOH B O     1 
HETATM 9272 O O     . HOH V 8 .   ? 22.324  105.808 83.689 1.00 43.47 ? 1108 HOH B O     1 
HETATM 9273 O O     . HOH V 8 .   ? 19.083  107.837 39.207 1.00 43.78 ? 1109 HOH B O     1 
HETATM 9274 O O     . HOH V 8 .   ? 33.993  106.081 52.847 1.00 49.49 ? 1110 HOH B O     1 
HETATM 9275 O O     . HOH V 8 .   ? 17.140  119.228 67.606 1.00 40.83 ? 1111 HOH B O     1 
HETATM 9276 O O     . HOH V 8 .   ? 27.677  56.559  48.943 1.00 47.27 ? 1112 HOH B O     1 
HETATM 9277 O O     . HOH V 8 .   ? 14.117  112.728 68.908 1.00 48.36 ? 1113 HOH B O     1 
HETATM 9278 O O     . HOH V 8 .   ? 13.546  75.857  34.984 1.00 39.96 ? 1114 HOH B O     1 
HETATM 9279 O O     . HOH V 8 .   ? 44.813  92.485  63.535 1.00 49.22 ? 1115 HOH B O     1 
HETATM 9280 O O     . HOH V 8 .   ? 19.838  98.853  85.591 1.00 46.60 ? 1116 HOH B O     1 
HETATM 9281 O O     . HOH V 8 .   ? 33.657  100.114 37.233 1.00 52.72 ? 1117 HOH B O     1 
HETATM 9282 O O     . HOH V 8 .   ? 13.327  112.133 60.004 1.00 53.39 ? 1118 HOH B O     1 
HETATM 9283 O O     . HOH V 8 .   ? 10.836  106.136 61.074 1.00 44.28 ? 1119 HOH B O     1 
HETATM 9284 O O     . HOH V 8 .   ? 7.329   70.368  68.480 1.00 59.78 ? 1120 HOH B O     1 
HETATM 9285 O O     . HOH V 8 .   ? 36.689  94.369  77.852 1.00 35.92 ? 1121 HOH B O     1 
HETATM 9286 O O     . HOH V 8 .   ? 29.402  117.342 59.372 1.00 47.49 ? 1122 HOH B O     1 
HETATM 9287 O O     . HOH V 8 .   ? 16.840  107.268 55.102 1.00 47.06 ? 1123 HOH B O     1 
HETATM 9288 O O     . HOH V 8 .   ? 24.745  74.909  81.664 1.00 46.49 ? 1124 HOH B O     1 
HETATM 9289 O O     . HOH V 8 .   ? 35.264  67.660  62.710 1.00 50.68 ? 1125 HOH B O     1 
HETATM 9290 O O     . HOH V 8 .   ? 11.197  64.626  34.633 1.00 41.05 ? 1126 HOH B O     1 
HETATM 9291 O O     . HOH V 8 .   ? 7.133   94.962  55.263 1.00 50.39 ? 1127 HOH B O     1 
HETATM 9292 O O     . HOH V 8 .   ? 16.120  77.742  79.625 1.00 46.10 ? 1128 HOH B O     1 
HETATM 9293 O O     . HOH V 8 .   ? 8.704   57.860  49.292 1.00 50.41 ? 1129 HOH B O     1 
HETATM 9294 O O     . HOH V 8 .   ? 21.700  69.262  67.617 1.00 39.99 ? 1130 HOH B O     1 
HETATM 9295 O O     . HOH V 8 .   ? 21.438  65.316  64.766 1.00 44.08 ? 1131 HOH B O     1 
HETATM 9296 O O     . HOH V 8 .   ? 9.036   102.068 60.734 1.00 44.33 ? 1132 HOH B O     1 
HETATM 9297 O O     . HOH V 8 .   ? 30.924  116.069 55.190 1.00 38.90 ? 1133 HOH B O     1 
HETATM 9298 O O     . HOH V 8 .   ? 4.102   86.593  29.379 1.00 46.21 ? 1134 HOH B O     1 
HETATM 9299 O O     . HOH V 8 .   ? 37.135  95.834  80.173 1.00 41.46 ? 1135 HOH B O     1 
HETATM 9300 O O     . HOH V 8 .   ? 31.875  70.772  62.737 1.00 28.26 ? 1136 HOH B O     1 
HETATM 9301 O O     . HOH V 8 .   ? 25.382  111.006 82.263 1.00 49.15 ? 1137 HOH B O     1 
HETATM 9302 O O     . HOH V 8 .   ? 13.782  58.137  58.931 1.00 42.80 ? 1138 HOH B O     1 
HETATM 9303 O O     . HOH V 8 .   ? 32.463  108.036 53.074 1.00 46.15 ? 1139 HOH B O     1 
HETATM 9304 O O     . HOH V 8 .   ? 8.890   68.471  34.788 1.00 36.03 ? 1140 HOH B O     1 
HETATM 9305 O O     . HOH V 8 .   ? 21.988  86.234  85.316 1.00 50.60 ? 1141 HOH B O     1 
HETATM 9306 O O     . HOH V 8 .   ? 15.280  112.626 71.150 1.00 43.44 ? 1142 HOH B O     1 
HETATM 9307 O O     . HOH V 8 .   ? 35.467  78.331  84.208 1.00 45.34 ? 1143 HOH B O     1 
HETATM 9308 O O     . HOH V 8 .   ? 16.877  111.788 74.993 1.00 46.49 ? 1144 HOH B O     1 
HETATM 9309 O O     . HOH V 8 .   ? 20.416  70.438  71.907 1.00 47.31 ? 1145 HOH B O     1 
HETATM 9310 O O     . HOH V 8 .   ? 29.398  105.400 35.749 1.00 32.12 ? 1146 HOH B O     1 
HETATM 9311 O O     . HOH V 8 .   ? 40.206  99.395  58.184 1.00 58.51 ? 1147 HOH B O     1 
HETATM 9312 O O     . HOH V 8 .   ? 4.355   66.526  49.198 1.00 36.30 ? 1148 HOH B O     1 
HETATM 9313 O O     . HOH V 8 .   ? -0.402  72.681  77.816 1.00 47.14 ? 1149 HOH B O     1 
HETATM 9314 O O     . HOH V 8 .   ? 28.221  88.706  38.631 1.00 31.80 ? 1150 HOH B O     1 
HETATM 9315 O O     . HOH V 8 .   ? 7.336   79.011  80.747 1.00 39.59 ? 1151 HOH B O     1 
HETATM 9316 O O     . HOH V 8 .   ? 21.602  88.245  78.632 1.00 31.90 ? 1152 HOH B O     1 
HETATM 9317 O O     . HOH V 8 .   ? 33.813  88.853  43.590 1.00 38.07 ? 1153 HOH B O     1 
HETATM 9318 O O     . HOH V 8 .   ? 30.812  115.632 58.111 1.00 31.05 ? 1154 HOH B O     1 
HETATM 9319 O O     . HOH V 8 .   ? -3.410  80.002  77.026 1.00 53.46 ? 1155 HOH B O     1 
HETATM 9320 O O     . HOH V 8 .   ? 37.785  81.293  56.121 1.00 61.06 ? 1156 HOH B O     1 
HETATM 9321 O O     . HOH V 8 .   ? 12.678  99.070  82.203 1.00 34.52 ? 1157 HOH B O     1 
HETATM 9322 O O     . HOH V 8 .   ? 9.866   111.941 68.967 1.00 39.50 ? 1158 HOH B O     1 
HETATM 9323 O O     . HOH V 8 .   ? 19.688  81.951  85.366 1.00 33.74 ? 1159 HOH B O     1 
HETATM 9324 O O     . HOH V 8 .   ? 17.590  114.534 47.822 1.00 47.96 ? 1160 HOH B O     1 
HETATM 9325 O O     . HOH V 8 .   ? 14.051  101.478 82.460 1.00 33.26 ? 1161 HOH B O     1 
HETATM 9326 O O     . HOH V 8 .   ? 7.995   108.915 59.760 1.00 43.73 ? 1162 HOH B O     1 
HETATM 9327 O O     . HOH V 8 .   ? 14.045  116.006 65.254 1.00 55.73 ? 1163 HOH B O     1 
HETATM 9328 O O     . HOH V 8 .   ? 18.857  116.819 46.431 1.00 46.21 ? 1164 HOH B O     1 
HETATM 9329 O O     . HOH V 8 .   ? 14.092  114.651 67.453 1.00 52.25 ? 1165 HOH B O     1 
HETATM 9330 O O     . HOH V 8 .   ? 10.738  112.022 72.949 1.00 49.49 ? 1166 HOH B O     1 
# 
