data_8ZHS
# 
_entry.id   8ZHS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8ZHS         pdb_00008zhs 10.2210/pdb8zhs/pdb 
WWPDB D_1300047685 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            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.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZHS 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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                 4 
_pdbx_contact_author.email              xgao@email.sdu.edu.cn 
_pdbx_contact_author.name_first         Xiang 
_pdbx_contact_author.name_last          Gao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6397-5639 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, J.H.' 1 0000-0003-4788-6796 
'Chen, Z.' 2 0000-0002-3761-5653 
'Gao, X.'  3 0000-0001-6397-5639 
# 
_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            'Cell Host Microbe' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1934-6069 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                200 
_citation.page_last                 ? 
_citation.title                     
'A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.chom.2025.01.008 
_citation.pdbx_database_id_PubMed   39909037 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lim, B.'          1 ? 
primary 'Xu, J.'           2 ? 
primary 'Wierzbicki, I.H.' 3 ? 
primary 'Gonzalez, C.G.'   4 ? 
primary 'Chen, Z.'         5 ? 
primary 'Gonzalez, D.J.'   6 ? 
primary 'Gao, X.'          7 ? 
primary 'Goodman, A.L.'    8 ? 
# 
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 'Maltose/maltodextrin-binding periplasmic protein,N-terminal Bte1' 55985.680 2   ? D108A/K109A/E198A/N199A/K265A 
? 
;Sequence reference of MBP for strain 'Acinetobacter baumannii' is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt id P0AEX9.
;
2 polymer     man 'C-terminal Bte1'                                                  12963.899 2   ? ?                             
? ? 
3 non-polymer syn GLYCEROL                                                           92.094    10  ? ?                             
? ? 
4 water       nat water                                                              18.015    418 ? ?                             
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTAARAFAAAGKEIEIKKLPEFEAMVNAGNTTYTG
LVEGIGYVYWTTETLYFIRTNPEQLWAIPKYQQIPFPYFQRKDAIIETKTLHTLHVLSKDELLKLDYDAYYAFYGIVEEM
LKFIHRADAIKSYCEIPLPIIKSK
;
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTAARAFAAAGKEIEIKKLPEFEAMVNAGNTTYTG
LVEGIGYVYWTTETLYFIRTNPEQLWAIPKYQQIPFPYFQRKDAIIETKTLHTLHVLSKDELLKLDYDAYYAFYGIVEEM
LKFIHRADAIKSYCEIPLPIIKSK
;
A,B ? 
2 'polypeptide(L)' no no 
;IGDGLSLISIIDEVGNGEYWSAAGDILLFAAGKTKLSPYMTVISLGTWMYETDLMQWRLACINYSDYKKTLIKYRELQKK
FESGDKSVEEKMNECHKILNSHYIEMQKNLGNL
;
;IGDGLSLISIIDEVGNGEYWSAAGDILLFAAGKTKLSPYMTVISLGTWMYETDLMQWRLACINYSDYKKTLIKYRELQKK
FESGDKSVEEKMNECHKILNSHYIEMQKNLGNL
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL GOL 
4 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   ILE n 
1 4   GLU n 
1 5   GLU n 
1 6   GLY n 
1 7   LYS n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  TRP n 
1 12  ILE n 
1 13  ASN n 
1 14  GLY n 
1 15  ASP n 
1 16  LYS n 
1 17  GLY n 
1 18  TYR n 
1 19  ASN n 
1 20  GLY n 
1 21  LEU n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  GLY n 
1 26  LYS n 
1 27  LYS n 
1 28  PHE n 
1 29  GLU n 
1 30  LYS n 
1 31  ASP n 
1 32  THR n 
1 33  GLY n 
1 34  ILE n 
1 35  LYS n 
1 36  VAL n 
1 37  THR n 
1 38  VAL n 
1 39  GLU n 
1 40  HIS n 
1 41  PRO n 
1 42  ASP n 
1 43  LYS n 
1 44  LEU n 
1 45  GLU n 
1 46  GLU n 
1 47  LYS n 
1 48  PHE n 
1 49  PRO n 
1 50  GLN n 
1 51  VAL n 
1 52  ALA n 
1 53  ALA n 
1 54  THR n 
1 55  GLY n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  ASP n 
1 60  ILE n 
1 61  ILE n 
1 62  PHE n 
1 63  TRP n 
1 64  ALA n 
1 65  HIS n 
1 66  ASP n 
1 67  ARG n 
1 68  PHE n 
1 69  GLY n 
1 70  GLY n 
1 71  TYR n 
1 72  ALA n 
1 73  GLN n 
1 74  SER n 
1 75  GLY n 
1 76  LEU n 
1 77  LEU n 
1 78  ALA n 
1 79  GLU n 
1 80  ILE n 
1 81  THR n 
1 82  PRO n 
1 83  ALA n 
1 84  ALA n 
1 85  ALA n 
1 86  PHE n 
1 87  GLN n 
1 88  ASP n 
1 89  LYS n 
1 90  LEU n 
1 91  TYR n 
1 92  PRO n 
1 93  PHE n 
1 94  THR n 
1 95  TRP n 
1 96  ASP n 
1 97  ALA n 
1 98  VAL n 
1 99  ARG n 
1 100 TYR n 
1 101 ASN n 
1 102 GLY n 
1 103 LYS n 
1 104 LEU n 
1 105 ILE n 
1 106 ALA n 
1 107 TYR n 
1 108 PRO n 
1 109 ILE n 
1 110 ALA n 
1 111 VAL n 
1 112 GLU n 
1 113 ALA n 
1 114 LEU n 
1 115 SER n 
1 116 LEU n 
1 117 ILE n 
1 118 TYR n 
1 119 ASN n 
1 120 LYS n 
1 121 ASP n 
1 122 LEU n 
1 123 LEU n 
1 124 PRO n 
1 125 ASN n 
1 126 PRO n 
1 127 PRO n 
1 128 LYS n 
1 129 THR n 
1 130 TRP n 
1 131 GLU n 
1 132 GLU n 
1 133 ILE n 
1 134 PRO n 
1 135 ALA n 
1 136 LEU n 
1 137 ASP n 
1 138 LYS n 
1 139 GLU n 
1 140 LEU n 
1 141 LYS n 
1 142 ALA n 
1 143 LYS n 
1 144 GLY n 
1 145 LYS n 
1 146 SER n 
1 147 ALA n 
1 148 LEU n 
1 149 MET n 
1 150 PHE n 
1 151 ASN n 
1 152 LEU n 
1 153 GLN n 
1 154 GLU n 
1 155 PRO n 
1 156 TYR n 
1 157 PHE n 
1 158 THR n 
1 159 TRP n 
1 160 PRO n 
1 161 LEU n 
1 162 ILE n 
1 163 ALA n 
1 164 ALA n 
1 165 ASP n 
1 166 GLY n 
1 167 GLY n 
1 168 TYR n 
1 169 ALA n 
1 170 PHE n 
1 171 LYS n 
1 172 TYR n 
1 173 ALA n 
1 174 ALA n 
1 175 GLY n 
1 176 LYS n 
1 177 TYR n 
1 178 ASP n 
1 179 ILE n 
1 180 LYS n 
1 181 ASP n 
1 182 VAL n 
1 183 GLY n 
1 184 VAL n 
1 185 ASP n 
1 186 ASN n 
1 187 ALA n 
1 188 GLY n 
1 189 ALA n 
1 190 LYS n 
1 191 ALA n 
1 192 GLY n 
1 193 LEU n 
1 194 THR n 
1 195 PHE n 
1 196 LEU n 
1 197 VAL n 
1 198 ASP n 
1 199 LEU n 
1 200 ILE n 
1 201 LYS n 
1 202 ASN n 
1 203 LYS n 
1 204 HIS n 
1 205 MET n 
1 206 ASN n 
1 207 ALA n 
1 208 ASP n 
1 209 THR n 
1 210 ASP n 
1 211 TYR n 
1 212 SER n 
1 213 ILE n 
1 214 ALA n 
1 215 GLU n 
1 216 ALA n 
1 217 ALA n 
1 218 PHE n 
1 219 ASN n 
1 220 LYS n 
1 221 GLY n 
1 222 GLU n 
1 223 THR n 
1 224 ALA n 
1 225 MET n 
1 226 THR n 
1 227 ILE n 
1 228 ASN n 
1 229 GLY n 
1 230 PRO n 
1 231 TRP n 
1 232 ALA n 
1 233 TRP n 
1 234 SER n 
1 235 ASN n 
1 236 ILE n 
1 237 ASP n 
1 238 THR n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 ASN n 
1 243 TYR n 
1 244 GLY n 
1 245 VAL n 
1 246 THR n 
1 247 VAL n 
1 248 LEU n 
1 249 PRO n 
1 250 THR n 
1 251 PHE n 
1 252 LYS n 
1 253 GLY n 
1 254 GLN n 
1 255 PRO n 
1 256 SER n 
1 257 LYS n 
1 258 PRO n 
1 259 PHE n 
1 260 VAL n 
1 261 GLY n 
1 262 VAL n 
1 263 LEU n 
1 264 SER n 
1 265 ALA n 
1 266 GLY n 
1 267 ILE n 
1 268 ASN n 
1 269 ALA n 
1 270 ALA n 
1 271 SER n 
1 272 PRO n 
1 273 ASN n 
1 274 LYS n 
1 275 GLU n 
1 276 LEU n 
1 277 ALA n 
1 278 LYS n 
1 279 GLU n 
1 280 PHE n 
1 281 LEU n 
1 282 GLU n 
1 283 ASN n 
1 284 TYR n 
1 285 LEU n 
1 286 LEU n 
1 287 THR n 
1 288 ASP n 
1 289 GLU n 
1 290 GLY n 
1 291 LEU n 
1 292 GLU n 
1 293 ALA n 
1 294 VAL n 
1 295 ASN n 
1 296 LYS n 
1 297 ASP n 
1 298 LYS n 
1 299 PRO n 
1 300 LEU n 
1 301 GLY n 
1 302 ALA n 
1 303 VAL n 
1 304 ALA n 
1 305 LEU n 
1 306 LYS n 
1 307 SER n 
1 308 TYR n 
1 309 GLU n 
1 310 GLU n 
1 311 GLU n 
1 312 LEU n 
1 313 ALA n 
1 314 LYS n 
1 315 ASP n 
1 316 PRO n 
1 317 ARG n 
1 318 ILE n 
1 319 ALA n 
1 320 ALA n 
1 321 THR n 
1 322 MET n 
1 323 GLU n 
1 324 ASN n 
1 325 ALA n 
1 326 GLN n 
1 327 LYS n 
1 328 GLY n 
1 329 GLU n 
1 330 ILE n 
1 331 MET n 
1 332 PRO n 
1 333 ASN n 
1 334 ILE n 
1 335 PRO n 
1 336 GLN n 
1 337 MET n 
1 338 SER n 
1 339 ALA n 
1 340 PHE n 
1 341 TRP n 
1 342 TYR n 
1 343 ALA n 
1 344 VAL n 
1 345 ARG n 
1 346 THR n 
1 347 ALA n 
1 348 VAL n 
1 349 ILE n 
1 350 ASN n 
1 351 ALA n 
1 352 ALA n 
1 353 SER n 
1 354 GLY n 
1 355 ARG n 
1 356 GLN n 
1 357 THR n 
1 358 VAL n 
1 359 ASP n 
1 360 GLU n 
1 361 ALA n 
1 362 LEU n 
1 363 LYS n 
1 364 ASP n 
1 365 ALA n 
1 366 GLN n 
1 367 THR n 
1 368 ALA n 
1 369 ALA n 
1 370 ARG n 
1 371 ALA n 
1 372 PHE n 
1 373 ALA n 
1 374 ALA n 
1 375 ALA n 
1 376 GLY n 
1 377 LYS n 
1 378 GLU n 
1 379 ILE n 
1 380 GLU n 
1 381 ILE n 
1 382 LYS n 
1 383 LYS n 
1 384 LEU n 
1 385 PRO n 
1 386 GLU n 
1 387 PHE n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 VAL n 
1 392 ASN n 
1 393 ALA n 
1 394 GLY n 
1 395 ASN n 
1 396 THR n 
1 397 THR n 
1 398 TYR n 
1 399 THR n 
1 400 GLY n 
1 401 LEU n 
1 402 VAL n 
1 403 GLU n 
1 404 GLY n 
1 405 ILE n 
1 406 GLY n 
1 407 TYR n 
1 408 VAL n 
1 409 TYR n 
1 410 TRP n 
1 411 THR n 
1 412 THR n 
1 413 GLU n 
1 414 THR n 
1 415 LEU n 
1 416 TYR n 
1 417 PHE n 
1 418 ILE n 
1 419 ARG n 
1 420 THR n 
1 421 ASN n 
1 422 PRO n 
1 423 GLU n 
1 424 GLN n 
1 425 LEU n 
1 426 TRP n 
1 427 ALA n 
1 428 ILE n 
1 429 PRO n 
1 430 LYS n 
1 431 TYR n 
1 432 GLN n 
1 433 GLN n 
1 434 ILE n 
1 435 PRO n 
1 436 PHE n 
1 437 PRO n 
1 438 TYR n 
1 439 PHE n 
1 440 GLN n 
1 441 ARG n 
1 442 LYS n 
1 443 ASP n 
1 444 ALA n 
1 445 ILE n 
1 446 ILE n 
1 447 GLU n 
1 448 THR n 
1 449 LYS n 
1 450 THR n 
1 451 LEU n 
1 452 HIS n 
1 453 THR n 
1 454 LEU n 
1 455 HIS n 
1 456 VAL n 
1 457 LEU n 
1 458 SER n 
1 459 LYS n 
1 460 ASP n 
1 461 GLU n 
1 462 LEU n 
1 463 LEU n 
1 464 LYS n 
1 465 LEU n 
1 466 ASP n 
1 467 TYR n 
1 468 ASP n 
1 469 ALA n 
1 470 TYR n 
1 471 TYR n 
1 472 ALA n 
1 473 PHE n 
1 474 TYR n 
1 475 GLY n 
1 476 ILE n 
1 477 VAL n 
1 478 GLU n 
1 479 GLU n 
1 480 MET n 
1 481 LEU n 
1 482 LYS n 
1 483 PHE n 
1 484 ILE n 
1 485 HIS n 
1 486 ARG n 
1 487 ALA n 
1 488 ASP n 
1 489 ALA n 
1 490 ILE n 
1 491 LYS n 
1 492 SER n 
1 493 TYR n 
1 494 CYS n 
1 495 GLU n 
1 496 ILE n 
1 497 PRO n 
1 498 LEU n 
1 499 PRO n 
1 500 ILE n 
1 501 ILE n 
1 502 LYS n 
1 503 SER n 
1 504 LYS n 
2 1   ILE n 
2 2   GLY n 
2 3   ASP n 
2 4   GLY n 
2 5   LEU n 
2 6   SER n 
2 7   LEU n 
2 8   ILE n 
2 9   SER n 
2 10  ILE n 
2 11  ILE n 
2 12  ASP n 
2 13  GLU n 
2 14  VAL n 
2 15  GLY n 
2 16  ASN n 
2 17  GLY n 
2 18  GLU n 
2 19  TYR n 
2 20  TRP n 
2 21  SER n 
2 22  ALA n 
2 23  ALA n 
2 24  GLY n 
2 25  ASP n 
2 26  ILE n 
2 27  LEU n 
2 28  LEU n 
2 29  PHE n 
2 30  ALA n 
2 31  ALA n 
2 32  GLY n 
2 33  LYS n 
2 34  THR n 
2 35  LYS n 
2 36  LEU n 
2 37  SER n 
2 38  PRO n 
2 39  TYR n 
2 40  MET n 
2 41  THR n 
2 42  VAL n 
2 43  ILE n 
2 44  SER n 
2 45  LEU n 
2 46  GLY n 
2 47  THR n 
2 48  TRP n 
2 49  MET n 
2 50  TYR n 
2 51  GLU n 
2 52  THR n 
2 53  ASP n 
2 54  LEU n 
2 55  MET n 
2 56  GLN n 
2 57  TRP n 
2 58  ARG n 
2 59  LEU n 
2 60  ALA n 
2 61  CYS n 
2 62  ILE n 
2 63  ASN n 
2 64  TYR n 
2 65  SER n 
2 66  ASP n 
2 67  TYR n 
2 68  LYS n 
2 69  LYS n 
2 70  THR n 
2 71  LEU n 
2 72  ILE n 
2 73  LYS n 
2 74  TYR n 
2 75  ARG n 
2 76  GLU n 
2 77  LEU n 
2 78  GLN n 
2 79  LYS n 
2 80  LYS n 
2 81  PHE n 
2 82  GLU n 
2 83  SER n 
2 84  GLY n 
2 85  ASP n 
2 86  LYS n 
2 87  SER n 
2 88  VAL n 
2 89  GLU n 
2 90  GLU n 
2 91  LYS n 
2 92  MET n 
2 93  ASN n 
2 94  GLU n 
2 95  CYS n 
2 96  HIS n 
2 97  LYS n 
2 98  ILE n 
2 99  LEU n 
2 100 ASN n 
2 101 SER n 
2 102 HIS n 
2 103 TYR n 
2 104 ILE n 
2 105 GLU n 
2 106 MET n 
2 107 GLN n 
2 108 LYS n 
2 109 ASN n 
2 110 LEU n 
2 111 GLY n 
2 112 ASN n 
2 113 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   375 ? ? 'malE, b4034, JW3994' ? ? ? ? ? ? 'Escherichia coli K-12'          83333  ? ? ? ? ? ? 
? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 376 504 ? ? BF9343_1937           ? ? ? ? ? ? 'Bacteroides fragilis NCTC 9343' 272559 ? ? ? ? ? ? 
? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   113 ? ? BF9343_1937           ? ? ? ? ? ? 'Bacteroides fragilis NCTC 9343' 272559 ? ? ? ? ? ? 
? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
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   20  20  MET MET A . n 
A 1 2   LYS 2   21  21  LYS LYS A . n 
A 1 3   ILE 3   22  22  ILE ILE A . n 
A 1 4   GLU 4   23  23  GLU GLU A . n 
A 1 5   GLU 5   24  24  GLU GLU A . n 
A 1 6   GLY 6   25  25  GLY GLY A . n 
A 1 7   LYS 7   26  26  LYS LYS A . n 
A 1 8   LEU 8   27  27  LEU LEU A . n 
A 1 9   VAL 9   28  28  VAL VAL A . n 
A 1 10  ILE 10  29  29  ILE ILE A . n 
A 1 11  TRP 11  30  30  TRP TRP A . n 
A 1 12  ILE 12  31  31  ILE ILE A . n 
A 1 13  ASN 13  32  32  ASN ASN A . n 
A 1 14  GLY 14  33  33  GLY GLY A . n 
A 1 15  ASP 15  34  34  ASP ASP A . n 
A 1 16  LYS 16  35  35  LYS LYS A . n 
A 1 17  GLY 17  36  36  GLY GLY A . n 
A 1 18  TYR 18  37  37  TYR TYR A . n 
A 1 19  ASN 19  38  38  ASN ASN A . n 
A 1 20  GLY 20  39  39  GLY GLY A . n 
A 1 21  LEU 21  40  40  LEU LEU A . n 
A 1 22  ALA 22  41  41  ALA ALA A . n 
A 1 23  GLU 23  42  42  GLU GLU A . n 
A 1 24  VAL 24  43  43  VAL VAL A . n 
A 1 25  GLY 25  44  44  GLY GLY A . n 
A 1 26  LYS 26  45  45  LYS LYS A . n 
A 1 27  LYS 27  46  46  LYS LYS A . n 
A 1 28  PHE 28  47  47  PHE PHE A . n 
A 1 29  GLU 29  48  48  GLU GLU A . n 
A 1 30  LYS 30  49  49  LYS LYS A . n 
A 1 31  ASP 31  50  50  ASP ASP A . n 
A 1 32  THR 32  51  51  THR THR A . n 
A 1 33  GLY 33  52  52  GLY GLY A . n 
A 1 34  ILE 34  53  53  ILE ILE A . n 
A 1 35  LYS 35  54  54  LYS LYS A . n 
A 1 36  VAL 36  55  55  VAL VAL A . n 
A 1 37  THR 37  56  56  THR THR A . n 
A 1 38  VAL 38  57  57  VAL VAL A . n 
A 1 39  GLU 39  58  58  GLU GLU A . n 
A 1 40  HIS 40  59  59  HIS HIS A . n 
A 1 41  PRO 41  60  60  PRO PRO A . n 
A 1 42  ASP 42  61  61  ASP ASP A . n 
A 1 43  LYS 43  62  62  LYS LYS A . n 
A 1 44  LEU 44  63  63  LEU LEU A . n 
A 1 45  GLU 45  64  64  GLU GLU A . n 
A 1 46  GLU 46  65  65  GLU GLU A . n 
A 1 47  LYS 47  66  66  LYS LYS A . n 
A 1 48  PHE 48  67  67  PHE PHE A . n 
A 1 49  PRO 49  68  68  PRO PRO A . n 
A 1 50  GLN 50  69  69  GLN GLN A . n 
A 1 51  VAL 51  70  70  VAL VAL A . n 
A 1 52  ALA 52  71  71  ALA ALA A . n 
A 1 53  ALA 53  72  72  ALA ALA A . n 
A 1 54  THR 54  73  73  THR THR A . n 
A 1 55  GLY 55  74  74  GLY GLY A . n 
A 1 56  ASP 56  75  75  ASP ASP A . n 
A 1 57  GLY 57  76  76  GLY GLY A . n 
A 1 58  PRO 58  77  77  PRO PRO A . n 
A 1 59  ASP 59  78  78  ASP ASP A . n 
A 1 60  ILE 60  79  79  ILE ILE A . n 
A 1 61  ILE 61  80  80  ILE ILE A . n 
A 1 62  PHE 62  81  81  PHE PHE A . n 
A 1 63  TRP 63  82  82  TRP TRP A . n 
A 1 64  ALA 64  83  83  ALA ALA A . n 
A 1 65  HIS 65  84  84  HIS HIS A . n 
A 1 66  ASP 66  85  85  ASP ASP A . n 
A 1 67  ARG 67  86  86  ARG ARG A . n 
A 1 68  PHE 68  87  87  PHE PHE A . n 
A 1 69  GLY 69  88  88  GLY GLY A . n 
A 1 70  GLY 70  89  89  GLY GLY A . n 
A 1 71  TYR 71  90  90  TYR TYR A . n 
A 1 72  ALA 72  91  91  ALA ALA A . n 
A 1 73  GLN 73  92  92  GLN GLN A . n 
A 1 74  SER 74  93  93  SER SER A . n 
A 1 75  GLY 75  94  94  GLY GLY A . n 
A 1 76  LEU 76  95  95  LEU LEU A . n 
A 1 77  LEU 77  96  96  LEU LEU A . n 
A 1 78  ALA 78  97  97  ALA ALA A . n 
A 1 79  GLU 79  98  98  GLU GLU A . n 
A 1 80  ILE 80  99  99  ILE ILE A . n 
A 1 81  THR 81  100 100 THR THR A . n 
A 1 82  PRO 82  101 101 PRO PRO A . n 
A 1 83  ALA 83  102 102 ALA ALA A . n 
A 1 84  ALA 84  103 103 ALA ALA A . n 
A 1 85  ALA 85  104 104 ALA ALA A . n 
A 1 86  PHE 86  105 105 PHE PHE A . n 
A 1 87  GLN 87  106 106 GLN GLN A . n 
A 1 88  ASP 88  107 107 ASP ASP A . n 
A 1 89  LYS 89  108 108 LYS LYS A . n 
A 1 90  LEU 90  109 109 LEU LEU A . n 
A 1 91  TYR 91  110 110 TYR TYR A . n 
A 1 92  PRO 92  111 111 PRO PRO A . n 
A 1 93  PHE 93  112 112 PHE PHE A . n 
A 1 94  THR 94  113 113 THR THR A . n 
A 1 95  TRP 95  114 114 TRP TRP A . n 
A 1 96  ASP 96  115 115 ASP ASP A . n 
A 1 97  ALA 97  116 116 ALA ALA A . n 
A 1 98  VAL 98  117 117 VAL VAL A . n 
A 1 99  ARG 99  118 118 ARG ARG A . n 
A 1 100 TYR 100 119 119 TYR TYR A . n 
A 1 101 ASN 101 120 120 ASN ASN A . n 
A 1 102 GLY 102 121 121 GLY GLY A . n 
A 1 103 LYS 103 122 122 LYS LYS A . n 
A 1 104 LEU 104 123 123 LEU LEU A . n 
A 1 105 ILE 105 124 124 ILE ILE A . n 
A 1 106 ALA 106 125 125 ALA ALA A . n 
A 1 107 TYR 107 126 126 TYR TYR A . n 
A 1 108 PRO 108 127 127 PRO PRO A . n 
A 1 109 ILE 109 128 128 ILE ILE A . n 
A 1 110 ALA 110 129 129 ALA ALA A . n 
A 1 111 VAL 111 130 130 VAL VAL A . n 
A 1 112 GLU 112 131 131 GLU GLU A . n 
A 1 113 ALA 113 132 132 ALA ALA A . n 
A 1 114 LEU 114 133 133 LEU LEU A . n 
A 1 115 SER 115 134 134 SER SER A . n 
A 1 116 LEU 116 135 135 LEU LEU A . n 
A 1 117 ILE 117 136 136 ILE ILE A . n 
A 1 118 TYR 118 137 137 TYR TYR A . n 
A 1 119 ASN 119 138 138 ASN ASN A . n 
A 1 120 LYS 120 139 139 LYS LYS A . n 
A 1 121 ASP 121 140 140 ASP ASP A . n 
A 1 122 LEU 122 141 141 LEU LEU A . n 
A 1 123 LEU 123 142 142 LEU LEU A . n 
A 1 124 PRO 124 143 143 PRO PRO A . n 
A 1 125 ASN 125 144 144 ASN ASN A . n 
A 1 126 PRO 126 145 145 PRO PRO A . n 
A 1 127 PRO 127 146 146 PRO PRO A . n 
A 1 128 LYS 128 147 147 LYS LYS A . n 
A 1 129 THR 129 148 148 THR THR A . n 
A 1 130 TRP 130 149 149 TRP TRP A . n 
A 1 131 GLU 131 150 150 GLU GLU A . n 
A 1 132 GLU 132 151 151 GLU GLU A . n 
A 1 133 ILE 133 152 152 ILE ILE A . n 
A 1 134 PRO 134 153 153 PRO PRO A . n 
A 1 135 ALA 135 154 154 ALA ALA A . n 
A 1 136 LEU 136 155 155 LEU LEU A . n 
A 1 137 ASP 137 156 156 ASP ASP A . n 
A 1 138 LYS 138 157 157 LYS LYS A . n 
A 1 139 GLU 139 158 158 GLU GLU A . n 
A 1 140 LEU 140 159 159 LEU LEU A . n 
A 1 141 LYS 141 160 160 LYS LYS A . n 
A 1 142 ALA 142 161 161 ALA ALA A . n 
A 1 143 LYS 143 162 162 LYS LYS A . n 
A 1 144 GLY 144 163 163 GLY GLY A . n 
A 1 145 LYS 145 164 164 LYS LYS A . n 
A 1 146 SER 146 165 165 SER SER A . n 
A 1 147 ALA 147 166 166 ALA ALA A . n 
A 1 148 LEU 148 167 167 LEU LEU A . n 
A 1 149 MET 149 168 168 MET MET A . n 
A 1 150 PHE 150 169 169 PHE PHE A . n 
A 1 151 ASN 151 170 170 ASN ASN A . n 
A 1 152 LEU 152 171 171 LEU LEU A . n 
A 1 153 GLN 153 172 172 GLN GLN A . n 
A 1 154 GLU 154 173 173 GLU GLU A . n 
A 1 155 PRO 155 174 174 PRO PRO A . n 
A 1 156 TYR 156 175 175 TYR TYR A . n 
A 1 157 PHE 157 176 176 PHE PHE A . n 
A 1 158 THR 158 177 177 THR THR A . n 
A 1 159 TRP 159 178 178 TRP TRP A . n 
A 1 160 PRO 160 179 179 PRO PRO A . n 
A 1 161 LEU 161 180 180 LEU LEU A . n 
A 1 162 ILE 162 181 181 ILE ILE A . n 
A 1 163 ALA 163 182 182 ALA ALA A . n 
A 1 164 ALA 164 183 183 ALA ALA A . n 
A 1 165 ASP 165 184 184 ASP ASP A . n 
A 1 166 GLY 166 185 185 GLY GLY A . n 
A 1 167 GLY 167 186 186 GLY GLY A . n 
A 1 168 TYR 168 187 187 TYR TYR A . n 
A 1 169 ALA 169 188 188 ALA ALA A . n 
A 1 170 PHE 170 189 189 PHE PHE A . n 
A 1 171 LYS 171 190 190 LYS LYS A . n 
A 1 172 TYR 172 191 191 TYR TYR A . n 
A 1 173 ALA 173 192 192 ALA ALA A . n 
A 1 174 ALA 174 193 193 ALA ALA A . n 
A 1 175 GLY 175 194 194 GLY GLY A . n 
A 1 176 LYS 176 195 195 LYS LYS A . n 
A 1 177 TYR 177 196 196 TYR TYR A . n 
A 1 178 ASP 178 197 197 ASP ASP A . n 
A 1 179 ILE 179 198 198 ILE ILE A . n 
A 1 180 LYS 180 199 199 LYS LYS A . n 
A 1 181 ASP 181 200 200 ASP ASP A . n 
A 1 182 VAL 182 201 201 VAL VAL A . n 
A 1 183 GLY 183 202 202 GLY GLY A . n 
A 1 184 VAL 184 203 203 VAL VAL A . n 
A 1 185 ASP 185 204 204 ASP ASP A . n 
A 1 186 ASN 186 205 205 ASN ASN A . n 
A 1 187 ALA 187 206 206 ALA ALA A . n 
A 1 188 GLY 188 207 207 GLY GLY A . n 
A 1 189 ALA 189 208 208 ALA ALA A . n 
A 1 190 LYS 190 209 209 LYS LYS A . n 
A 1 191 ALA 191 210 210 ALA ALA A . n 
A 1 192 GLY 192 211 211 GLY GLY A . n 
A 1 193 LEU 193 212 212 LEU LEU A . n 
A 1 194 THR 194 213 213 THR THR A . n 
A 1 195 PHE 195 214 214 PHE PHE A . n 
A 1 196 LEU 196 215 215 LEU LEU A . n 
A 1 197 VAL 197 216 216 VAL VAL A . n 
A 1 198 ASP 198 217 217 ASP ASP A . n 
A 1 199 LEU 199 218 218 LEU LEU A . n 
A 1 200 ILE 200 219 219 ILE ILE A . n 
A 1 201 LYS 201 220 220 LYS LYS A . n 
A 1 202 ASN 202 221 221 ASN ASN A . n 
A 1 203 LYS 203 222 222 LYS LYS A . n 
A 1 204 HIS 204 223 223 HIS HIS A . n 
A 1 205 MET 205 224 224 MET MET A . n 
A 1 206 ASN 206 225 225 ASN ASN A . n 
A 1 207 ALA 207 226 226 ALA ALA A . n 
A 1 208 ASP 208 227 227 ASP ASP A . n 
A 1 209 THR 209 228 228 THR THR A . n 
A 1 210 ASP 210 229 229 ASP ASP A . n 
A 1 211 TYR 211 230 230 TYR TYR A . n 
A 1 212 SER 212 231 231 SER SER A . n 
A 1 213 ILE 213 232 232 ILE ILE A . n 
A 1 214 ALA 214 233 233 ALA ALA A . n 
A 1 215 GLU 215 234 234 GLU GLU A . n 
A 1 216 ALA 216 235 235 ALA ALA A . n 
A 1 217 ALA 217 236 236 ALA ALA A . n 
A 1 218 PHE 218 237 237 PHE PHE A . n 
A 1 219 ASN 219 238 238 ASN ASN A . n 
A 1 220 LYS 220 239 239 LYS LYS A . n 
A 1 221 GLY 221 240 240 GLY GLY A . n 
A 1 222 GLU 222 241 241 GLU GLU A . n 
A 1 223 THR 223 242 242 THR THR A . n 
A 1 224 ALA 224 243 243 ALA ALA A . n 
A 1 225 MET 225 244 244 MET MET A . n 
A 1 226 THR 226 245 245 THR THR A . n 
A 1 227 ILE 227 246 246 ILE ILE A . n 
A 1 228 ASN 228 247 247 ASN ASN A . n 
A 1 229 GLY 229 248 248 GLY GLY A . n 
A 1 230 PRO 230 249 249 PRO PRO A . n 
A 1 231 TRP 231 250 250 TRP TRP A . n 
A 1 232 ALA 232 251 251 ALA ALA A . n 
A 1 233 TRP 233 252 252 TRP TRP A . n 
A 1 234 SER 234 253 253 SER SER A . n 
A 1 235 ASN 235 254 254 ASN ASN A . n 
A 1 236 ILE 236 255 255 ILE ILE A . n 
A 1 237 ASP 237 256 256 ASP ASP A . n 
A 1 238 THR 238 257 257 THR THR A . n 
A 1 239 SER 239 258 258 SER SER A . n 
A 1 240 ALA 240 259 259 ALA ALA A . n 
A 1 241 VAL 241 260 260 VAL VAL A . n 
A 1 242 ASN 242 261 261 ASN ASN A . n 
A 1 243 TYR 243 262 262 TYR TYR A . n 
A 1 244 GLY 244 263 263 GLY GLY A . n 
A 1 245 VAL 245 264 264 VAL VAL A . n 
A 1 246 THR 246 265 265 THR THR A . n 
A 1 247 VAL 247 266 266 VAL VAL A . n 
A 1 248 LEU 248 267 267 LEU LEU A . n 
A 1 249 PRO 249 268 268 PRO PRO A . n 
A 1 250 THR 250 269 269 THR THR A . n 
A 1 251 PHE 251 270 270 PHE PHE A . n 
A 1 252 LYS 252 271 271 LYS LYS A . n 
A 1 253 GLY 253 272 272 GLY GLY A . n 
A 1 254 GLN 254 273 273 GLN GLN A . n 
A 1 255 PRO 255 274 274 PRO PRO A . n 
A 1 256 SER 256 275 275 SER SER A . n 
A 1 257 LYS 257 276 276 LYS LYS A . n 
A 1 258 PRO 258 277 277 PRO PRO A . n 
A 1 259 PHE 259 278 278 PHE PHE A . n 
A 1 260 VAL 260 279 279 VAL VAL A . n 
A 1 261 GLY 261 280 280 GLY GLY A . n 
A 1 262 VAL 262 281 281 VAL VAL A . n 
A 1 263 LEU 263 282 282 LEU LEU A . n 
A 1 264 SER 264 283 283 SER SER A . n 
A 1 265 ALA 265 284 284 ALA ALA A . n 
A 1 266 GLY 266 285 285 GLY GLY A . n 
A 1 267 ILE 267 286 286 ILE ILE A . n 
A 1 268 ASN 268 287 287 ASN ASN A . n 
A 1 269 ALA 269 288 288 ALA ALA A . n 
A 1 270 ALA 270 289 289 ALA ALA A . n 
A 1 271 SER 271 290 290 SER SER A . n 
A 1 272 PRO 272 291 291 PRO PRO A . n 
A 1 273 ASN 273 292 292 ASN ASN A . n 
A 1 274 LYS 274 293 293 LYS LYS A . n 
A 1 275 GLU 275 294 294 GLU GLU A . n 
A 1 276 LEU 276 295 295 LEU LEU A . n 
A 1 277 ALA 277 296 296 ALA ALA A . n 
A 1 278 LYS 278 297 297 LYS LYS A . n 
A 1 279 GLU 279 298 298 GLU GLU A . n 
A 1 280 PHE 280 299 299 PHE PHE A . n 
A 1 281 LEU 281 300 300 LEU LEU A . n 
A 1 282 GLU 282 301 301 GLU GLU A . n 
A 1 283 ASN 283 302 302 ASN ASN A . n 
A 1 284 TYR 284 303 303 TYR TYR A . n 
A 1 285 LEU 285 304 304 LEU LEU A . n 
A 1 286 LEU 286 305 305 LEU LEU A . n 
A 1 287 THR 287 306 306 THR THR A . n 
A 1 288 ASP 288 307 307 ASP ASP A . n 
A 1 289 GLU 289 308 308 GLU GLU A . n 
A 1 290 GLY 290 309 309 GLY GLY A . n 
A 1 291 LEU 291 310 310 LEU LEU A . n 
A 1 292 GLU 292 311 311 GLU GLU A . n 
A 1 293 ALA 293 312 312 ALA ALA A . n 
A 1 294 VAL 294 313 313 VAL VAL A . n 
A 1 295 ASN 295 314 314 ASN ASN A . n 
A 1 296 LYS 296 315 315 LYS LYS A . n 
A 1 297 ASP 297 316 316 ASP ASP A . n 
A 1 298 LYS 298 317 317 LYS LYS A . n 
A 1 299 PRO 299 318 318 PRO PRO A . n 
A 1 300 LEU 300 319 319 LEU LEU A . n 
A 1 301 GLY 301 320 320 GLY GLY A . n 
A 1 302 ALA 302 321 321 ALA ALA A . n 
A 1 303 VAL 303 322 322 VAL VAL A . n 
A 1 304 ALA 304 323 323 ALA ALA A . n 
A 1 305 LEU 305 324 324 LEU LEU A . n 
A 1 306 LYS 306 325 325 LYS LYS A . n 
A 1 307 SER 307 326 326 SER SER A . n 
A 1 308 TYR 308 327 327 TYR TYR A . n 
A 1 309 GLU 309 328 328 GLU GLU A . n 
A 1 310 GLU 310 329 329 GLU GLU A . n 
A 1 311 GLU 311 330 330 GLU GLU A . n 
A 1 312 LEU 312 331 331 LEU LEU A . n 
A 1 313 ALA 313 332 332 ALA ALA A . n 
A 1 314 LYS 314 333 333 LYS LYS A . n 
A 1 315 ASP 315 334 334 ASP ASP A . n 
A 1 316 PRO 316 335 335 PRO PRO A . n 
A 1 317 ARG 317 336 336 ARG ARG A . n 
A 1 318 ILE 318 337 337 ILE ILE A . n 
A 1 319 ALA 319 338 338 ALA ALA A . n 
A 1 320 ALA 320 339 339 ALA ALA A . n 
A 1 321 THR 321 340 340 THR THR A . n 
A 1 322 MET 322 341 341 MET MET A . n 
A 1 323 GLU 323 342 342 GLU GLU A . n 
A 1 324 ASN 324 343 343 ASN ASN A . n 
A 1 325 ALA 325 344 344 ALA ALA A . n 
A 1 326 GLN 326 345 345 GLN GLN A . n 
A 1 327 LYS 327 346 346 LYS LYS A . n 
A 1 328 GLY 328 347 347 GLY GLY A . n 
A 1 329 GLU 329 348 348 GLU GLU A . n 
A 1 330 ILE 330 349 349 ILE ILE A . n 
A 1 331 MET 331 350 350 MET MET A . n 
A 1 332 PRO 332 351 351 PRO PRO A . n 
A 1 333 ASN 333 352 352 ASN ASN A . n 
A 1 334 ILE 334 353 353 ILE ILE A . n 
A 1 335 PRO 335 354 354 PRO PRO A . n 
A 1 336 GLN 336 355 355 GLN GLN A . n 
A 1 337 MET 337 356 356 MET MET A . n 
A 1 338 SER 338 357 357 SER SER A . n 
A 1 339 ALA 339 358 358 ALA ALA A . n 
A 1 340 PHE 340 359 359 PHE PHE A . n 
A 1 341 TRP 341 360 360 TRP TRP A . n 
A 1 342 TYR 342 361 361 TYR TYR A . n 
A 1 343 ALA 343 362 362 ALA ALA A . n 
A 1 344 VAL 344 363 363 VAL VAL A . n 
A 1 345 ARG 345 364 364 ARG ARG A . n 
A 1 346 THR 346 365 365 THR THR A . n 
A 1 347 ALA 347 366 366 ALA ALA A . n 
A 1 348 VAL 348 367 367 VAL VAL A . n 
A 1 349 ILE 349 368 368 ILE ILE A . n 
A 1 350 ASN 350 369 369 ASN ASN A . n 
A 1 351 ALA 351 370 370 ALA ALA A . n 
A 1 352 ALA 352 371 371 ALA ALA A . n 
A 1 353 SER 353 372 372 SER SER A . n 
A 1 354 GLY 354 373 373 GLY GLY A . n 
A 1 355 ARG 355 374 374 ARG ARG A . n 
A 1 356 GLN 356 375 375 GLN GLN A . n 
A 1 357 THR 357 376 376 THR THR A . n 
A 1 358 VAL 358 377 377 VAL VAL A . n 
A 1 359 ASP 359 378 378 ASP ASP A . n 
A 1 360 GLU 360 379 379 GLU GLU A . n 
A 1 361 ALA 361 380 380 ALA ALA A . n 
A 1 362 LEU 362 381 381 LEU LEU A . n 
A 1 363 LYS 363 382 382 LYS LYS A . n 
A 1 364 ASP 364 383 383 ASP ASP A . n 
A 1 365 ALA 365 384 384 ALA ALA A . n 
A 1 366 GLN 366 385 385 GLN GLN A . n 
A 1 367 THR 367 386 386 THR THR A . n 
A 1 368 ALA 368 387 387 ALA ALA A . n 
A 1 369 ALA 369 388 388 ALA ALA A . n 
A 1 370 ARG 370 389 389 ARG ARG A . n 
A 1 371 ALA 371 390 390 ALA ALA A . n 
A 1 372 PHE 372 391 391 PHE PHE A . n 
A 1 373 ALA 373 392 392 ALA ALA A . n 
A 1 374 ALA 374 393 393 ALA ALA A . n 
A 1 375 ALA 375 394 394 ALA ALA A . n 
A 1 376 GLY 376 395 395 GLY GLY A . n 
A 1 377 LYS 377 396 396 LYS LYS A . n 
A 1 378 GLU 378 397 397 GLU GLU A . n 
A 1 379 ILE 379 398 398 ILE ILE A . n 
A 1 380 GLU 380 399 399 GLU GLU A . n 
A 1 381 ILE 381 400 400 ILE ILE A . n 
A 1 382 LYS 382 401 401 LYS LYS A . n 
A 1 383 LYS 383 402 402 LYS LYS A . n 
A 1 384 LEU 384 403 403 LEU LEU A . n 
A 1 385 PRO 385 404 404 PRO PRO A . n 
A 1 386 GLU 386 405 405 GLU GLU A . n 
A 1 387 PHE 387 406 406 PHE PHE A . n 
A 1 388 GLU 388 407 407 GLU GLU A . n 
A 1 389 ALA 389 408 408 ALA ALA A . n 
A 1 390 MET 390 409 409 MET MET A . n 
A 1 391 VAL 391 410 410 VAL VAL A . n 
A 1 392 ASN 392 411 411 ASN ASN A . n 
A 1 393 ALA 393 412 412 ALA ALA A . n 
A 1 394 GLY 394 413 413 GLY GLY A . n 
A 1 395 ASN 395 414 414 ASN ASN A . n 
A 1 396 THR 396 415 415 THR THR A . n 
A 1 397 THR 397 416 416 THR THR A . n 
A 1 398 TYR 398 417 417 TYR TYR A . n 
A 1 399 THR 399 418 418 THR THR A . n 
A 1 400 GLY 400 419 419 GLY GLY A . n 
A 1 401 LEU 401 420 420 LEU LEU A . n 
A 1 402 VAL 402 421 421 VAL VAL A . n 
A 1 403 GLU 403 422 422 GLU GLU A . n 
A 1 404 GLY 404 423 423 GLY GLY A . n 
A 1 405 ILE 405 424 424 ILE ILE A . n 
A 1 406 GLY 406 425 425 GLY GLY A . n 
A 1 407 TYR 407 426 426 TYR TYR A . n 
A 1 408 VAL 408 427 427 VAL VAL A . n 
A 1 409 TYR 409 428 428 TYR TYR A . n 
A 1 410 TRP 410 429 429 TRP TRP A . n 
A 1 411 THR 411 430 430 THR THR A . n 
A 1 412 THR 412 431 431 THR THR A . n 
A 1 413 GLU 413 432 432 GLU GLU A . n 
A 1 414 THR 414 433 433 THR THR A . n 
A 1 415 LEU 415 434 434 LEU LEU A . n 
A 1 416 TYR 416 435 435 TYR TYR A . n 
A 1 417 PHE 417 436 436 PHE PHE A . n 
A 1 418 ILE 418 437 437 ILE ILE A . n 
A 1 419 ARG 419 438 438 ARG ARG A . n 
A 1 420 THR 420 439 439 THR THR A . n 
A 1 421 ASN 421 440 440 ASN ASN A . n 
A 1 422 PRO 422 441 441 PRO PRO A . n 
A 1 423 GLU 423 442 442 GLU GLU A . n 
A 1 424 GLN 424 443 443 GLN GLN A . n 
A 1 425 LEU 425 444 444 LEU LEU A . n 
A 1 426 TRP 426 445 445 TRP TRP A . n 
A 1 427 ALA 427 446 446 ALA ALA A . n 
A 1 428 ILE 428 447 447 ILE ILE A . n 
A 1 429 PRO 429 448 448 PRO PRO A . n 
A 1 430 LYS 430 449 449 LYS LYS A . n 
A 1 431 TYR 431 450 450 TYR TYR A . n 
A 1 432 GLN 432 451 451 GLN GLN A . n 
A 1 433 GLN 433 452 452 GLN GLN A . n 
A 1 434 ILE 434 453 453 ILE ILE A . n 
A 1 435 PRO 435 454 454 PRO PRO A . n 
A 1 436 PHE 436 455 455 PHE PHE A . n 
A 1 437 PRO 437 456 456 PRO PRO A . n 
A 1 438 TYR 438 457 457 TYR TYR A . n 
A 1 439 PHE 439 458 458 PHE PHE A . n 
A 1 440 GLN 440 459 459 GLN GLN A . n 
A 1 441 ARG 441 460 460 ARG ARG A . n 
A 1 442 LYS 442 461 461 LYS LYS A . n 
A 1 443 ASP 443 462 462 ASP ASP A . n 
A 1 444 ALA 444 463 463 ALA ALA A . n 
A 1 445 ILE 445 464 464 ILE ILE A . n 
A 1 446 ILE 446 465 465 ILE ILE A . n 
A 1 447 GLU 447 466 466 GLU GLU A . n 
A 1 448 THR 448 467 467 THR THR A . n 
A 1 449 LYS 449 468 468 LYS LYS A . n 
A 1 450 THR 450 469 469 THR THR A . n 
A 1 451 LEU 451 470 470 LEU LEU A . n 
A 1 452 HIS 452 471 471 HIS HIS A . n 
A 1 453 THR 453 472 472 THR THR A . n 
A 1 454 LEU 454 473 473 LEU LEU A . n 
A 1 455 HIS 455 474 474 HIS HIS A . n 
A 1 456 VAL 456 475 475 VAL VAL A . n 
A 1 457 LEU 457 476 476 LEU LEU A . n 
A 1 458 SER 458 477 477 SER SER A . n 
A 1 459 LYS 459 478 478 LYS LYS A . n 
A 1 460 ASP 460 479 479 ASP ASP A . n 
A 1 461 GLU 461 480 480 GLU GLU A . n 
A 1 462 LEU 462 481 481 LEU LEU A . n 
A 1 463 LEU 463 482 482 LEU LEU A . n 
A 1 464 LYS 464 483 483 LYS LYS A . n 
A 1 465 LEU 465 484 484 LEU LEU A . n 
A 1 466 ASP 466 485 485 ASP ASP A . n 
A 1 467 TYR 467 486 486 TYR TYR A . n 
A 1 468 ASP 468 487 487 ASP ASP A . n 
A 1 469 ALA 469 488 488 ALA ALA A . n 
A 1 470 TYR 470 489 489 TYR TYR A . n 
A 1 471 TYR 471 490 490 TYR TYR A . n 
A 1 472 ALA 472 491 491 ALA ALA A . n 
A 1 473 PHE 473 492 492 PHE PHE A . n 
A 1 474 TYR 474 493 493 TYR TYR A . n 
A 1 475 GLY 475 494 494 GLY GLY A . n 
A 1 476 ILE 476 495 495 ILE ILE A . n 
A 1 477 VAL 477 496 496 VAL VAL A . n 
A 1 478 GLU 478 497 497 GLU GLU A . n 
A 1 479 GLU 479 498 498 GLU GLU A . n 
A 1 480 MET 480 499 499 MET MET A . n 
A 1 481 LEU 481 500 500 LEU LEU A . n 
A 1 482 LYS 482 501 501 LYS LYS A . n 
A 1 483 PHE 483 502 502 PHE PHE A . n 
A 1 484 ILE 484 503 503 ILE ILE A . n 
A 1 485 HIS 485 504 504 HIS HIS A . n 
A 1 486 ARG 486 505 505 ARG ARG A . n 
A 1 487 ALA 487 506 506 ALA ALA A . n 
A 1 488 ASP 488 507 507 ASP ASP A . n 
A 1 489 ALA 489 508 508 ALA ALA A . n 
A 1 490 ILE 490 509 509 ILE ILE A . n 
A 1 491 LYS 491 510 510 LYS LYS A . n 
A 1 492 SER 492 511 511 SER SER A . n 
A 1 493 TYR 493 512 512 TYR TYR A . n 
A 1 494 CYS 494 513 513 CYS CYS A . n 
A 1 495 GLU 495 514 514 GLU GLU A . n 
A 1 496 ILE 496 515 515 ILE ILE A . n 
A 1 497 PRO 497 516 516 PRO PRO A . n 
A 1 498 LEU 498 517 517 LEU LEU A . n 
A 1 499 PRO 499 518 518 PRO PRO A . n 
A 1 500 ILE 500 519 519 ILE ILE A . n 
A 1 501 ILE 501 520 520 ILE ILE A . n 
A 1 502 LYS 502 521 521 LYS LYS A . n 
A 1 503 SER 503 522 522 SER SER A . n 
A 1 504 LYS 504 523 523 LYS LYS A . n 
B 1 1   MET 1   20  ?   ?   ?   B . n 
B 1 2   LYS 2   21  21  LYS LYS B . n 
B 1 3   ILE 3   22  22  ILE ILE B . n 
B 1 4   GLU 4   23  23  GLU GLU B . n 
B 1 5   GLU 5   24  24  GLU GLU B . n 
B 1 6   GLY 6   25  25  GLY GLY B . n 
B 1 7   LYS 7   26  26  LYS LYS B . n 
B 1 8   LEU 8   27  27  LEU LEU B . n 
B 1 9   VAL 9   28  28  VAL VAL B . n 
B 1 10  ILE 10  29  29  ILE ILE B . n 
B 1 11  TRP 11  30  30  TRP TRP B . n 
B 1 12  ILE 12  31  31  ILE ILE B . n 
B 1 13  ASN 13  32  32  ASN ASN B . n 
B 1 14  GLY 14  33  33  GLY GLY B . n 
B 1 15  ASP 15  34  34  ASP ASP B . n 
B 1 16  LYS 16  35  35  LYS LYS B . n 
B 1 17  GLY 17  36  36  GLY GLY B . n 
B 1 18  TYR 18  37  37  TYR TYR B . n 
B 1 19  ASN 19  38  38  ASN ASN B . n 
B 1 20  GLY 20  39  39  GLY GLY B . n 
B 1 21  LEU 21  40  40  LEU LEU B . n 
B 1 22  ALA 22  41  41  ALA ALA B . n 
B 1 23  GLU 23  42  42  GLU GLU B . n 
B 1 24  VAL 24  43  43  VAL VAL B . n 
B 1 25  GLY 25  44  44  GLY GLY B . n 
B 1 26  LYS 26  45  45  LYS LYS B . n 
B 1 27  LYS 27  46  46  LYS LYS B . n 
B 1 28  PHE 28  47  47  PHE PHE B . n 
B 1 29  GLU 29  48  48  GLU GLU B . n 
B 1 30  LYS 30  49  49  LYS LYS B . n 
B 1 31  ASP 31  50  50  ASP ASP B . n 
B 1 32  THR 32  51  51  THR THR B . n 
B 1 33  GLY 33  52  52  GLY GLY B . n 
B 1 34  ILE 34  53  53  ILE ILE B . n 
B 1 35  LYS 35  54  54  LYS LYS B . n 
B 1 36  VAL 36  55  55  VAL VAL B . n 
B 1 37  THR 37  56  56  THR THR B . n 
B 1 38  VAL 38  57  57  VAL VAL B . n 
B 1 39  GLU 39  58  58  GLU GLU B . n 
B 1 40  HIS 40  59  59  HIS HIS B . n 
B 1 41  PRO 41  60  60  PRO PRO B . n 
B 1 42  ASP 42  61  61  ASP ASP B . n 
B 1 43  LYS 43  62  62  LYS LYS B . n 
B 1 44  LEU 44  63  63  LEU LEU B . n 
B 1 45  GLU 45  64  64  GLU GLU B . n 
B 1 46  GLU 46  65  65  GLU GLU B . n 
B 1 47  LYS 47  66  66  LYS LYS B . n 
B 1 48  PHE 48  67  67  PHE PHE B . n 
B 1 49  PRO 49  68  68  PRO PRO B . n 
B 1 50  GLN 50  69  69  GLN GLN B . n 
B 1 51  VAL 51  70  70  VAL VAL B . n 
B 1 52  ALA 52  71  71  ALA ALA B . n 
B 1 53  ALA 53  72  72  ALA ALA B . n 
B 1 54  THR 54  73  73  THR THR B . n 
B 1 55  GLY 55  74  74  GLY GLY B . n 
B 1 56  ASP 56  75  75  ASP ASP B . n 
B 1 57  GLY 57  76  76  GLY GLY B . n 
B 1 58  PRO 58  77  77  PRO PRO B . n 
B 1 59  ASP 59  78  78  ASP ASP B . n 
B 1 60  ILE 60  79  79  ILE ILE B . n 
B 1 61  ILE 61  80  80  ILE ILE B . n 
B 1 62  PHE 62  81  81  PHE PHE B . n 
B 1 63  TRP 63  82  82  TRP TRP B . n 
B 1 64  ALA 64  83  83  ALA ALA B . n 
B 1 65  HIS 65  84  84  HIS HIS B . n 
B 1 66  ASP 66  85  85  ASP ASP B . n 
B 1 67  ARG 67  86  86  ARG ARG B . n 
B 1 68  PHE 68  87  87  PHE PHE B . n 
B 1 69  GLY 69  88  88  GLY GLY B . n 
B 1 70  GLY 70  89  89  GLY GLY B . n 
B 1 71  TYR 71  90  90  TYR TYR B . n 
B 1 72  ALA 72  91  91  ALA ALA B . n 
B 1 73  GLN 73  92  92  GLN GLN B . n 
B 1 74  SER 74  93  93  SER SER B . n 
B 1 75  GLY 75  94  94  GLY GLY B . n 
B 1 76  LEU 76  95  95  LEU LEU B . n 
B 1 77  LEU 77  96  96  LEU LEU B . n 
B 1 78  ALA 78  97  97  ALA ALA B . n 
B 1 79  GLU 79  98  98  GLU GLU B . n 
B 1 80  ILE 80  99  99  ILE ILE B . n 
B 1 81  THR 81  100 100 THR THR B . n 
B 1 82  PRO 82  101 101 PRO PRO B . n 
B 1 83  ALA 83  102 102 ALA ALA B . n 
B 1 84  ALA 84  103 103 ALA ALA B . n 
B 1 85  ALA 85  104 104 ALA ALA B . n 
B 1 86  PHE 86  105 105 PHE PHE B . n 
B 1 87  GLN 87  106 106 GLN GLN B . n 
B 1 88  ASP 88  107 107 ASP ASP B . n 
B 1 89  LYS 89  108 108 LYS LYS B . n 
B 1 90  LEU 90  109 109 LEU LEU B . n 
B 1 91  TYR 91  110 110 TYR TYR B . n 
B 1 92  PRO 92  111 111 PRO PRO B . n 
B 1 93  PHE 93  112 112 PHE PHE B . n 
B 1 94  THR 94  113 113 THR THR B . n 
B 1 95  TRP 95  114 114 TRP TRP B . n 
B 1 96  ASP 96  115 115 ASP ASP B . n 
B 1 97  ALA 97  116 116 ALA ALA B . n 
B 1 98  VAL 98  117 117 VAL VAL B . n 
B 1 99  ARG 99  118 118 ARG ARG B . n 
B 1 100 TYR 100 119 119 TYR TYR B . n 
B 1 101 ASN 101 120 120 ASN ASN B . n 
B 1 102 GLY 102 121 121 GLY GLY B . n 
B 1 103 LYS 103 122 122 LYS LYS B . n 
B 1 104 LEU 104 123 123 LEU LEU B . n 
B 1 105 ILE 105 124 124 ILE ILE B . n 
B 1 106 ALA 106 125 125 ALA ALA B . n 
B 1 107 TYR 107 126 126 TYR TYR B . n 
B 1 108 PRO 108 127 127 PRO PRO B . n 
B 1 109 ILE 109 128 128 ILE ILE B . n 
B 1 110 ALA 110 129 129 ALA ALA B . n 
B 1 111 VAL 111 130 130 VAL VAL B . n 
B 1 112 GLU 112 131 131 GLU GLU B . n 
B 1 113 ALA 113 132 132 ALA ALA B . n 
B 1 114 LEU 114 133 133 LEU LEU B . n 
B 1 115 SER 115 134 134 SER SER B . n 
B 1 116 LEU 116 135 135 LEU LEU B . n 
B 1 117 ILE 117 136 136 ILE ILE B . n 
B 1 118 TYR 118 137 137 TYR TYR B . n 
B 1 119 ASN 119 138 138 ASN ASN B . n 
B 1 120 LYS 120 139 139 LYS LYS B . n 
B 1 121 ASP 121 140 140 ASP ASP B . n 
B 1 122 LEU 122 141 141 LEU LEU B . n 
B 1 123 LEU 123 142 142 LEU LEU B . n 
B 1 124 PRO 124 143 143 PRO PRO B . n 
B 1 125 ASN 125 144 144 ASN ASN B . n 
B 1 126 PRO 126 145 145 PRO PRO B . n 
B 1 127 PRO 127 146 146 PRO PRO B . n 
B 1 128 LYS 128 147 147 LYS LYS B . n 
B 1 129 THR 129 148 148 THR THR B . n 
B 1 130 TRP 130 149 149 TRP TRP B . n 
B 1 131 GLU 131 150 150 GLU GLU B . n 
B 1 132 GLU 132 151 151 GLU GLU B . n 
B 1 133 ILE 133 152 152 ILE ILE B . n 
B 1 134 PRO 134 153 153 PRO PRO B . n 
B 1 135 ALA 135 154 154 ALA ALA B . n 
B 1 136 LEU 136 155 155 LEU LEU B . n 
B 1 137 ASP 137 156 156 ASP ASP B . n 
B 1 138 LYS 138 157 157 LYS LYS B . n 
B 1 139 GLU 139 158 158 GLU GLU B . n 
B 1 140 LEU 140 159 159 LEU LEU B . n 
B 1 141 LYS 141 160 160 LYS LYS B . n 
B 1 142 ALA 142 161 161 ALA ALA B . n 
B 1 143 LYS 143 162 162 LYS LYS B . n 
B 1 144 GLY 144 163 163 GLY GLY B . n 
B 1 145 LYS 145 164 164 LYS LYS B . n 
B 1 146 SER 146 165 165 SER SER B . n 
B 1 147 ALA 147 166 166 ALA ALA B . n 
B 1 148 LEU 148 167 167 LEU LEU B . n 
B 1 149 MET 149 168 168 MET MET B . n 
B 1 150 PHE 150 169 169 PHE PHE B . n 
B 1 151 ASN 151 170 170 ASN ASN B . n 
B 1 152 LEU 152 171 171 LEU LEU B . n 
B 1 153 GLN 153 172 172 GLN GLN B . n 
B 1 154 GLU 154 173 173 GLU GLU B . n 
B 1 155 PRO 155 174 174 PRO PRO B . n 
B 1 156 TYR 156 175 175 TYR TYR B . n 
B 1 157 PHE 157 176 176 PHE PHE B . n 
B 1 158 THR 158 177 177 THR THR B . n 
B 1 159 TRP 159 178 178 TRP TRP B . n 
B 1 160 PRO 160 179 179 PRO PRO B . n 
B 1 161 LEU 161 180 180 LEU LEU B . n 
B 1 162 ILE 162 181 181 ILE ILE B . n 
B 1 163 ALA 163 182 182 ALA ALA B . n 
B 1 164 ALA 164 183 183 ALA ALA B . n 
B 1 165 ASP 165 184 184 ASP ASP B . n 
B 1 166 GLY 166 185 185 GLY GLY B . n 
B 1 167 GLY 167 186 186 GLY GLY B . n 
B 1 168 TYR 168 187 187 TYR TYR B . n 
B 1 169 ALA 169 188 188 ALA ALA B . n 
B 1 170 PHE 170 189 189 PHE PHE B . n 
B 1 171 LYS 171 190 190 LYS LYS B . n 
B 1 172 TYR 172 191 191 TYR TYR B . n 
B 1 173 ALA 173 192 192 ALA ALA B . n 
B 1 174 ALA 174 193 193 ALA ALA B . n 
B 1 175 GLY 175 194 194 GLY GLY B . n 
B 1 176 LYS 176 195 195 LYS LYS B . n 
B 1 177 TYR 177 196 196 TYR TYR B . n 
B 1 178 ASP 178 197 197 ASP ASP B . n 
B 1 179 ILE 179 198 198 ILE ILE B . n 
B 1 180 LYS 180 199 199 LYS LYS B . n 
B 1 181 ASP 181 200 200 ASP ASP B . n 
B 1 182 VAL 182 201 201 VAL VAL B . n 
B 1 183 GLY 183 202 202 GLY GLY B . n 
B 1 184 VAL 184 203 203 VAL VAL B . n 
B 1 185 ASP 185 204 204 ASP ASP B . n 
B 1 186 ASN 186 205 205 ASN ASN B . n 
B 1 187 ALA 187 206 206 ALA ALA B . n 
B 1 188 GLY 188 207 207 GLY GLY B . n 
B 1 189 ALA 189 208 208 ALA ALA B . n 
B 1 190 LYS 190 209 209 LYS LYS B . n 
B 1 191 ALA 191 210 210 ALA ALA B . n 
B 1 192 GLY 192 211 211 GLY GLY B . n 
B 1 193 LEU 193 212 212 LEU LEU B . n 
B 1 194 THR 194 213 213 THR THR B . n 
B 1 195 PHE 195 214 214 PHE PHE B . n 
B 1 196 LEU 196 215 215 LEU LEU B . n 
B 1 197 VAL 197 216 216 VAL VAL B . n 
B 1 198 ASP 198 217 217 ASP ASP B . n 
B 1 199 LEU 199 218 218 LEU LEU B . n 
B 1 200 ILE 200 219 219 ILE ILE B . n 
B 1 201 LYS 201 220 220 LYS LYS B . n 
B 1 202 ASN 202 221 221 ASN ASN B . n 
B 1 203 LYS 203 222 222 LYS LYS B . n 
B 1 204 HIS 204 223 223 HIS HIS B . n 
B 1 205 MET 205 224 224 MET MET B . n 
B 1 206 ASN 206 225 225 ASN ASN B . n 
B 1 207 ALA 207 226 226 ALA ALA B . n 
B 1 208 ASP 208 227 227 ASP ASP B . n 
B 1 209 THR 209 228 228 THR THR B . n 
B 1 210 ASP 210 229 229 ASP ASP B . n 
B 1 211 TYR 211 230 230 TYR TYR B . n 
B 1 212 SER 212 231 231 SER SER B . n 
B 1 213 ILE 213 232 232 ILE ILE B . n 
B 1 214 ALA 214 233 233 ALA ALA B . n 
B 1 215 GLU 215 234 234 GLU GLU B . n 
B 1 216 ALA 216 235 235 ALA ALA B . n 
B 1 217 ALA 217 236 236 ALA ALA B . n 
B 1 218 PHE 218 237 237 PHE PHE B . n 
B 1 219 ASN 219 238 238 ASN ASN B . n 
B 1 220 LYS 220 239 239 LYS LYS B . n 
B 1 221 GLY 221 240 240 GLY GLY B . n 
B 1 222 GLU 222 241 241 GLU GLU B . n 
B 1 223 THR 223 242 242 THR THR B . n 
B 1 224 ALA 224 243 243 ALA ALA B . n 
B 1 225 MET 225 244 244 MET MET B . n 
B 1 226 THR 226 245 245 THR THR B . n 
B 1 227 ILE 227 246 246 ILE ILE B . n 
B 1 228 ASN 228 247 247 ASN ASN B . n 
B 1 229 GLY 229 248 248 GLY GLY B . n 
B 1 230 PRO 230 249 249 PRO PRO B . n 
B 1 231 TRP 231 250 250 TRP TRP B . n 
B 1 232 ALA 232 251 251 ALA ALA B . n 
B 1 233 TRP 233 252 252 TRP TRP B . n 
B 1 234 SER 234 253 253 SER SER B . n 
B 1 235 ASN 235 254 254 ASN ASN B . n 
B 1 236 ILE 236 255 255 ILE ILE B . n 
B 1 237 ASP 237 256 256 ASP ASP B . n 
B 1 238 THR 238 257 257 THR THR B . n 
B 1 239 SER 239 258 258 SER SER B . n 
B 1 240 ALA 240 259 259 ALA ALA B . n 
B 1 241 VAL 241 260 260 VAL VAL B . n 
B 1 242 ASN 242 261 261 ASN ASN B . n 
B 1 243 TYR 243 262 262 TYR TYR B . n 
B 1 244 GLY 244 263 263 GLY GLY B . n 
B 1 245 VAL 245 264 264 VAL VAL B . n 
B 1 246 THR 246 265 265 THR THR B . n 
B 1 247 VAL 247 266 266 VAL VAL B . n 
B 1 248 LEU 248 267 267 LEU LEU B . n 
B 1 249 PRO 249 268 268 PRO PRO B . n 
B 1 250 THR 250 269 269 THR THR B . n 
B 1 251 PHE 251 270 270 PHE PHE B . n 
B 1 252 LYS 252 271 271 LYS LYS B . n 
B 1 253 GLY 253 272 272 GLY GLY B . n 
B 1 254 GLN 254 273 273 GLN GLN B . n 
B 1 255 PRO 255 274 274 PRO PRO B . n 
B 1 256 SER 256 275 275 SER SER B . n 
B 1 257 LYS 257 276 276 LYS LYS B . n 
B 1 258 PRO 258 277 277 PRO PRO B . n 
B 1 259 PHE 259 278 278 PHE PHE B . n 
B 1 260 VAL 260 279 279 VAL VAL B . n 
B 1 261 GLY 261 280 280 GLY GLY B . n 
B 1 262 VAL 262 281 281 VAL VAL B . n 
B 1 263 LEU 263 282 282 LEU LEU B . n 
B 1 264 SER 264 283 283 SER SER B . n 
B 1 265 ALA 265 284 284 ALA ALA B . n 
B 1 266 GLY 266 285 285 GLY GLY B . n 
B 1 267 ILE 267 286 286 ILE ILE B . n 
B 1 268 ASN 268 287 287 ASN ASN B . n 
B 1 269 ALA 269 288 288 ALA ALA B . n 
B 1 270 ALA 270 289 289 ALA ALA B . n 
B 1 271 SER 271 290 290 SER SER B . n 
B 1 272 PRO 272 291 291 PRO PRO B . n 
B 1 273 ASN 273 292 292 ASN ASN B . n 
B 1 274 LYS 274 293 293 LYS LYS B . n 
B 1 275 GLU 275 294 294 GLU GLU B . n 
B 1 276 LEU 276 295 295 LEU LEU B . n 
B 1 277 ALA 277 296 296 ALA ALA B . n 
B 1 278 LYS 278 297 297 LYS LYS B . n 
B 1 279 GLU 279 298 298 GLU GLU B . n 
B 1 280 PHE 280 299 299 PHE PHE B . n 
B 1 281 LEU 281 300 300 LEU LEU B . n 
B 1 282 GLU 282 301 301 GLU GLU B . n 
B 1 283 ASN 283 302 302 ASN ASN B . n 
B 1 284 TYR 284 303 303 TYR TYR B . n 
B 1 285 LEU 285 304 304 LEU LEU B . n 
B 1 286 LEU 286 305 305 LEU LEU B . n 
B 1 287 THR 287 306 306 THR THR B . n 
B 1 288 ASP 288 307 307 ASP ASP B . n 
B 1 289 GLU 289 308 308 GLU GLU B . n 
B 1 290 GLY 290 309 309 GLY GLY B . n 
B 1 291 LEU 291 310 310 LEU LEU B . n 
B 1 292 GLU 292 311 311 GLU GLU B . n 
B 1 293 ALA 293 312 312 ALA ALA B . n 
B 1 294 VAL 294 313 313 VAL VAL B . n 
B 1 295 ASN 295 314 314 ASN ASN B . n 
B 1 296 LYS 296 315 315 LYS LYS B . n 
B 1 297 ASP 297 316 316 ASP ASP B . n 
B 1 298 LYS 298 317 317 LYS LYS B . n 
B 1 299 PRO 299 318 318 PRO PRO B . n 
B 1 300 LEU 300 319 319 LEU LEU B . n 
B 1 301 GLY 301 320 320 GLY GLY B . n 
B 1 302 ALA 302 321 321 ALA ALA B . n 
B 1 303 VAL 303 322 322 VAL VAL B . n 
B 1 304 ALA 304 323 323 ALA ALA B . n 
B 1 305 LEU 305 324 324 LEU LEU B . n 
B 1 306 LYS 306 325 325 LYS LYS B . n 
B 1 307 SER 307 326 326 SER SER B . n 
B 1 308 TYR 308 327 327 TYR TYR B . n 
B 1 309 GLU 309 328 328 GLU GLU B . n 
B 1 310 GLU 310 329 329 GLU GLU B . n 
B 1 311 GLU 311 330 330 GLU GLU B . n 
B 1 312 LEU 312 331 331 LEU LEU B . n 
B 1 313 ALA 313 332 332 ALA ALA B . n 
B 1 314 LYS 314 333 333 LYS LYS B . n 
B 1 315 ASP 315 334 334 ASP ASP B . n 
B 1 316 PRO 316 335 335 PRO PRO B . n 
B 1 317 ARG 317 336 336 ARG ARG B . n 
B 1 318 ILE 318 337 337 ILE ILE B . n 
B 1 319 ALA 319 338 338 ALA ALA B . n 
B 1 320 ALA 320 339 339 ALA ALA B . n 
B 1 321 THR 321 340 340 THR THR B . n 
B 1 322 MET 322 341 341 MET MET B . n 
B 1 323 GLU 323 342 342 GLU GLU B . n 
B 1 324 ASN 324 343 343 ASN ASN B . n 
B 1 325 ALA 325 344 344 ALA ALA B . n 
B 1 326 GLN 326 345 345 GLN GLN B . n 
B 1 327 LYS 327 346 346 LYS LYS B . n 
B 1 328 GLY 328 347 347 GLY GLY B . n 
B 1 329 GLU 329 348 348 GLU GLU B . n 
B 1 330 ILE 330 349 349 ILE ILE B . n 
B 1 331 MET 331 350 350 MET MET B . n 
B 1 332 PRO 332 351 351 PRO PRO B . n 
B 1 333 ASN 333 352 352 ASN ASN B . n 
B 1 334 ILE 334 353 353 ILE ILE B . n 
B 1 335 PRO 335 354 354 PRO PRO B . n 
B 1 336 GLN 336 355 355 GLN GLN B . n 
B 1 337 MET 337 356 356 MET MET B . n 
B 1 338 SER 338 357 357 SER SER B . n 
B 1 339 ALA 339 358 358 ALA ALA B . n 
B 1 340 PHE 340 359 359 PHE PHE B . n 
B 1 341 TRP 341 360 360 TRP TRP B . n 
B 1 342 TYR 342 361 361 TYR TYR B . n 
B 1 343 ALA 343 362 362 ALA ALA B . n 
B 1 344 VAL 344 363 363 VAL VAL B . n 
B 1 345 ARG 345 364 364 ARG ARG B . n 
B 1 346 THR 346 365 365 THR THR B . n 
B 1 347 ALA 347 366 366 ALA ALA B . n 
B 1 348 VAL 348 367 367 VAL VAL B . n 
B 1 349 ILE 349 368 368 ILE ILE B . n 
B 1 350 ASN 350 369 369 ASN ASN B . n 
B 1 351 ALA 351 370 370 ALA ALA B . n 
B 1 352 ALA 352 371 371 ALA ALA B . n 
B 1 353 SER 353 372 372 SER SER B . n 
B 1 354 GLY 354 373 373 GLY GLY B . n 
B 1 355 ARG 355 374 374 ARG ARG B . n 
B 1 356 GLN 356 375 375 GLN GLN B . n 
B 1 357 THR 357 376 376 THR THR B . n 
B 1 358 VAL 358 377 377 VAL VAL B . n 
B 1 359 ASP 359 378 378 ASP ASP B . n 
B 1 360 GLU 360 379 379 GLU GLU B . n 
B 1 361 ALA 361 380 380 ALA ALA B . n 
B 1 362 LEU 362 381 381 LEU LEU B . n 
B 1 363 LYS 363 382 382 LYS LYS B . n 
B 1 364 ASP 364 383 383 ASP ASP B . n 
B 1 365 ALA 365 384 384 ALA ALA B . n 
B 1 366 GLN 366 385 385 GLN GLN B . n 
B 1 367 THR 367 386 386 THR THR B . n 
B 1 368 ALA 368 387 387 ALA ALA B . n 
B 1 369 ALA 369 388 388 ALA ALA B . n 
B 1 370 ARG 370 389 389 ARG ARG B . n 
B 1 371 ALA 371 390 390 ALA ALA B . n 
B 1 372 PHE 372 391 391 PHE PHE B . n 
B 1 373 ALA 373 392 392 ALA ALA B . n 
B 1 374 ALA 374 393 393 ALA ALA B . n 
B 1 375 ALA 375 394 394 ALA ALA B . n 
B 1 376 GLY 376 395 395 GLY GLY B . n 
B 1 377 LYS 377 396 396 LYS LYS B . n 
B 1 378 GLU 378 397 397 GLU GLU B . n 
B 1 379 ILE 379 398 398 ILE ILE B . n 
B 1 380 GLU 380 399 399 GLU GLU B . n 
B 1 381 ILE 381 400 400 ILE ILE B . n 
B 1 382 LYS 382 401 401 LYS LYS B . n 
B 1 383 LYS 383 402 402 LYS LYS B . n 
B 1 384 LEU 384 403 403 LEU LEU B . n 
B 1 385 PRO 385 404 404 PRO PRO B . n 
B 1 386 GLU 386 405 405 GLU GLU B . n 
B 1 387 PHE 387 406 406 PHE PHE B . n 
B 1 388 GLU 388 407 407 GLU GLU B . n 
B 1 389 ALA 389 408 408 ALA ALA B . n 
B 1 390 MET 390 409 409 MET MET B . n 
B 1 391 VAL 391 410 410 VAL VAL B . n 
B 1 392 ASN 392 411 411 ASN ASN B . n 
B 1 393 ALA 393 412 412 ALA ALA B . n 
B 1 394 GLY 394 413 413 GLY GLY B . n 
B 1 395 ASN 395 414 414 ASN ASN B . n 
B 1 396 THR 396 415 415 THR THR B . n 
B 1 397 THR 397 416 416 THR THR B . n 
B 1 398 TYR 398 417 417 TYR TYR B . n 
B 1 399 THR 399 418 418 THR THR B . n 
B 1 400 GLY 400 419 419 GLY GLY B . n 
B 1 401 LEU 401 420 420 LEU LEU B . n 
B 1 402 VAL 402 421 421 VAL VAL B . n 
B 1 403 GLU 403 422 422 GLU GLU B . n 
B 1 404 GLY 404 423 423 GLY GLY B . n 
B 1 405 ILE 405 424 424 ILE ILE B . n 
B 1 406 GLY 406 425 425 GLY GLY B . n 
B 1 407 TYR 407 426 426 TYR TYR B . n 
B 1 408 VAL 408 427 427 VAL VAL B . n 
B 1 409 TYR 409 428 428 TYR TYR B . n 
B 1 410 TRP 410 429 429 TRP TRP B . n 
B 1 411 THR 411 430 430 THR THR B . n 
B 1 412 THR 412 431 431 THR THR B . n 
B 1 413 GLU 413 432 432 GLU GLU B . n 
B 1 414 THR 414 433 433 THR THR B . n 
B 1 415 LEU 415 434 434 LEU LEU B . n 
B 1 416 TYR 416 435 435 TYR TYR B . n 
B 1 417 PHE 417 436 436 PHE PHE B . n 
B 1 418 ILE 418 437 437 ILE ILE B . n 
B 1 419 ARG 419 438 438 ARG ARG B . n 
B 1 420 THR 420 439 439 THR THR B . n 
B 1 421 ASN 421 440 440 ASN ASN B . n 
B 1 422 PRO 422 441 441 PRO PRO B . n 
B 1 423 GLU 423 442 442 GLU GLU B . n 
B 1 424 GLN 424 443 443 GLN GLN B . n 
B 1 425 LEU 425 444 444 LEU LEU B . n 
B 1 426 TRP 426 445 445 TRP TRP B . n 
B 1 427 ALA 427 446 446 ALA ALA B . n 
B 1 428 ILE 428 447 447 ILE ILE B . n 
B 1 429 PRO 429 448 448 PRO PRO B . n 
B 1 430 LYS 430 449 449 LYS LYS B . n 
B 1 431 TYR 431 450 450 TYR TYR B . n 
B 1 432 GLN 432 451 451 GLN GLN B . n 
B 1 433 GLN 433 452 452 GLN GLN B . n 
B 1 434 ILE 434 453 453 ILE ILE B . n 
B 1 435 PRO 435 454 454 PRO PRO B . n 
B 1 436 PHE 436 455 455 PHE PHE B . n 
B 1 437 PRO 437 456 456 PRO PRO B . n 
B 1 438 TYR 438 457 457 TYR TYR B . n 
B 1 439 PHE 439 458 458 PHE PHE B . n 
B 1 440 GLN 440 459 459 GLN GLN B . n 
B 1 441 ARG 441 460 460 ARG ARG B . n 
B 1 442 LYS 442 461 461 LYS LYS B . n 
B 1 443 ASP 443 462 462 ASP ASP B . n 
B 1 444 ALA 444 463 463 ALA ALA B . n 
B 1 445 ILE 445 464 464 ILE ILE B . n 
B 1 446 ILE 446 465 465 ILE ILE B . n 
B 1 447 GLU 447 466 466 GLU GLU B . n 
B 1 448 THR 448 467 467 THR THR B . n 
B 1 449 LYS 449 468 468 LYS LYS B . n 
B 1 450 THR 450 469 469 THR THR B . n 
B 1 451 LEU 451 470 470 LEU LEU B . n 
B 1 452 HIS 452 471 471 HIS HIS B . n 
B 1 453 THR 453 472 472 THR THR B . n 
B 1 454 LEU 454 473 473 LEU LEU B . n 
B 1 455 HIS 455 474 474 HIS HIS B . n 
B 1 456 VAL 456 475 475 VAL VAL B . n 
B 1 457 LEU 457 476 476 LEU LEU B . n 
B 1 458 SER 458 477 477 SER SER B . n 
B 1 459 LYS 459 478 478 LYS LYS B . n 
B 1 460 ASP 460 479 479 ASP ASP B . n 
B 1 461 GLU 461 480 480 GLU GLU B . n 
B 1 462 LEU 462 481 481 LEU LEU B . n 
B 1 463 LEU 463 482 482 LEU LEU B . n 
B 1 464 LYS 464 483 483 LYS LYS B . n 
B 1 465 LEU 465 484 484 LEU LEU B . n 
B 1 466 ASP 466 485 485 ASP ASP B . n 
B 1 467 TYR 467 486 486 TYR TYR B . n 
B 1 468 ASP 468 487 487 ASP ASP B . n 
B 1 469 ALA 469 488 488 ALA ALA B . n 
B 1 470 TYR 470 489 489 TYR TYR B . n 
B 1 471 TYR 471 490 490 TYR TYR B . n 
B 1 472 ALA 472 491 491 ALA ALA B . n 
B 1 473 PHE 473 492 492 PHE PHE B . n 
B 1 474 TYR 474 493 493 TYR TYR B . n 
B 1 475 GLY 475 494 494 GLY GLY B . n 
B 1 476 ILE 476 495 495 ILE ILE B . n 
B 1 477 VAL 477 496 496 VAL VAL B . n 
B 1 478 GLU 478 497 497 GLU GLU B . n 
B 1 479 GLU 479 498 498 GLU GLU B . n 
B 1 480 MET 480 499 499 MET MET B . n 
B 1 481 LEU 481 500 500 LEU LEU B . n 
B 1 482 LYS 482 501 501 LYS LYS B . n 
B 1 483 PHE 483 502 502 PHE PHE B . n 
B 1 484 ILE 484 503 503 ILE ILE B . n 
B 1 485 HIS 485 504 504 HIS HIS B . n 
B 1 486 ARG 486 505 505 ARG ARG B . n 
B 1 487 ALA 487 506 506 ALA ALA B . n 
B 1 488 ASP 488 507 507 ASP ASP B . n 
B 1 489 ALA 489 508 508 ALA ALA B . n 
B 1 490 ILE 490 509 509 ILE ILE B . n 
B 1 491 LYS 491 510 510 LYS LYS B . n 
B 1 492 SER 492 511 511 SER SER B . n 
B 1 493 TYR 493 512 512 TYR TYR B . n 
B 1 494 CYS 494 513 513 CYS CYS B . n 
B 1 495 GLU 495 514 514 GLU GLU B . n 
B 1 496 ILE 496 515 515 ILE ILE B . n 
B 1 497 PRO 497 516 516 PRO PRO B . n 
B 1 498 LEU 498 517 517 LEU LEU B . n 
B 1 499 PRO 499 518 518 PRO PRO B . n 
B 1 500 ILE 500 519 519 ILE ILE B . n 
B 1 501 ILE 501 520 520 ILE ILE B . n 
B 1 502 LYS 502 521 521 LYS LYS B . n 
B 1 503 SER 503 522 522 SER SER B . n 
B 1 504 LYS 504 523 523 LYS LYS B . n 
C 2 1   ILE 1   565 ?   ?   ?   C . n 
C 2 2   GLY 2   566 566 GLY GLY C . n 
C 2 3   ASP 3   567 567 ASP ASP C . n 
C 2 4   GLY 4   568 568 GLY GLY C . n 
C 2 5   LEU 5   569 569 LEU LEU C . n 
C 2 6   SER 6   570 570 SER SER C . n 
C 2 7   LEU 7   571 571 LEU LEU C . n 
C 2 8   ILE 8   572 572 ILE ILE C . n 
C 2 9   SER 9   573 573 SER SER C . n 
C 2 10  ILE 10  574 574 ILE ILE C . n 
C 2 11  ILE 11  575 575 ILE ILE C . n 
C 2 12  ASP 12  576 576 ASP ASP C . n 
C 2 13  GLU 13  577 577 GLU GLU C . n 
C 2 14  VAL 14  578 578 VAL VAL C . n 
C 2 15  GLY 15  579 579 GLY GLY C . n 
C 2 16  ASN 16  580 580 ASN ASN C . n 
C 2 17  GLY 17  581 581 GLY GLY C . n 
C 2 18  GLU 18  582 582 GLU GLU C . n 
C 2 19  TYR 19  583 583 TYR TYR C . n 
C 2 20  TRP 20  584 584 TRP TRP C . n 
C 2 21  SER 21  585 585 SER SER C . n 
C 2 22  ALA 22  586 586 ALA ALA C . n 
C 2 23  ALA 23  587 587 ALA ALA C . n 
C 2 24  GLY 24  588 588 GLY GLY C . n 
C 2 25  ASP 25  589 589 ASP ASP C . n 
C 2 26  ILE 26  590 590 ILE ILE C . n 
C 2 27  LEU 27  591 591 LEU LEU C . n 
C 2 28  LEU 28  592 592 LEU LEU C . n 
C 2 29  PHE 29  593 593 PHE PHE C . n 
C 2 30  ALA 30  594 594 ALA ALA C . n 
C 2 31  ALA 31  595 595 ALA ALA C . n 
C 2 32  GLY 32  596 596 GLY GLY C . n 
C 2 33  LYS 33  597 597 LYS LYS C . n 
C 2 34  THR 34  598 598 THR THR C . n 
C 2 35  LYS 35  599 599 LYS LYS C . n 
C 2 36  LEU 36  600 600 LEU LEU C . n 
C 2 37  SER 37  601 601 SER SER C . n 
C 2 38  PRO 38  602 602 PRO PRO C . n 
C 2 39  TYR 39  603 603 TYR TYR C . n 
C 2 40  MET 40  604 604 MET MET C . n 
C 2 41  THR 41  605 605 THR THR C . n 
C 2 42  VAL 42  606 606 VAL VAL C . n 
C 2 43  ILE 43  607 607 ILE ILE C . n 
C 2 44  SER 44  608 608 SER SER C . n 
C 2 45  LEU 45  609 609 LEU LEU C . n 
C 2 46  GLY 46  610 610 GLY GLY C . n 
C 2 47  THR 47  611 611 THR THR C . n 
C 2 48  TRP 48  612 612 TRP TRP C . n 
C 2 49  MET 49  613 613 MET MET C . n 
C 2 50  TYR 50  614 614 TYR TYR C . n 
C 2 51  GLU 51  615 615 GLU GLU C . n 
C 2 52  THR 52  616 616 THR THR C . n 
C 2 53  ASP 53  617 617 ASP ASP C . n 
C 2 54  LEU 54  618 618 LEU LEU C . n 
C 2 55  MET 55  619 619 MET MET C . n 
C 2 56  GLN 56  620 620 GLN GLN C . n 
C 2 57  TRP 57  621 621 TRP TRP C . n 
C 2 58  ARG 58  622 622 ARG ARG C . n 
C 2 59  LEU 59  623 623 LEU LEU C . n 
C 2 60  ALA 60  624 624 ALA ALA C . n 
C 2 61  CYS 61  625 625 CYS CYS C . n 
C 2 62  ILE 62  626 626 ILE ILE C . n 
C 2 63  ASN 63  627 627 ASN ASN C . n 
C 2 64  TYR 64  628 628 TYR TYR C . n 
C 2 65  SER 65  629 629 SER SER C . n 
C 2 66  ASP 66  630 630 ASP ASP C . n 
C 2 67  TYR 67  631 631 TYR TYR C . n 
C 2 68  LYS 68  632 632 LYS LYS C . n 
C 2 69  LYS 69  633 633 LYS LYS C . n 
C 2 70  THR 70  634 634 THR THR C . n 
C 2 71  LEU 71  635 635 LEU LEU C . n 
C 2 72  ILE 72  636 636 ILE ILE C . n 
C 2 73  LYS 73  637 637 LYS LYS C . n 
C 2 74  TYR 74  638 638 TYR TYR C . n 
C 2 75  ARG 75  639 639 ARG ARG C . n 
C 2 76  GLU 76  640 640 GLU GLU C . n 
C 2 77  LEU 77  641 641 LEU LEU C . n 
C 2 78  GLN 78  642 642 GLN GLN C . n 
C 2 79  LYS 79  643 643 LYS LYS C . n 
C 2 80  LYS 80  644 644 LYS LYS C . n 
C 2 81  PHE 81  645 645 PHE PHE C . n 
C 2 82  GLU 82  646 646 GLU GLU C . n 
C 2 83  SER 83  647 647 SER SER C . n 
C 2 84  GLY 84  648 648 GLY GLY C . n 
C 2 85  ASP 85  649 649 ASP ASP C . n 
C 2 86  LYS 86  650 650 LYS LYS C . n 
C 2 87  SER 87  651 651 SER SER C . n 
C 2 88  VAL 88  652 652 VAL VAL C . n 
C 2 89  GLU 89  653 653 GLU GLU C . n 
C 2 90  GLU 90  654 654 GLU GLU C . n 
C 2 91  LYS 91  655 655 LYS LYS C . n 
C 2 92  MET 92  656 656 MET MET C . n 
C 2 93  ASN 93  657 657 ASN ASN C . n 
C 2 94  GLU 94  658 658 GLU GLU C . n 
C 2 95  CYS 95  659 659 CYS CYS C . n 
C 2 96  HIS 96  660 660 HIS HIS C . n 
C 2 97  LYS 97  661 661 LYS LYS C . n 
C 2 98  ILE 98  662 662 ILE ILE C . n 
C 2 99  LEU 99  663 663 LEU LEU C . n 
C 2 100 ASN 100 664 664 ASN ASN C . n 
C 2 101 SER 101 665 665 SER SER C . n 
C 2 102 HIS 102 666 666 HIS HIS C . n 
C 2 103 TYR 103 667 667 TYR TYR C . n 
C 2 104 ILE 104 668 668 ILE ILE C . n 
C 2 105 GLU 105 669 669 GLU GLU C . n 
C 2 106 MET 106 670 670 MET MET C . n 
C 2 107 GLN 107 671 671 GLN GLN C . n 
C 2 108 LYS 108 672 672 LYS LYS C . n 
C 2 109 ASN 109 673 673 ASN ASN C . n 
C 2 110 LEU 110 674 674 LEU LEU C . n 
C 2 111 GLY 111 675 675 GLY GLY C . n 
C 2 112 ASN 112 676 676 ASN ASN C . n 
C 2 113 LEU 113 677 677 LEU LEU C . n 
D 2 1   ILE 1   565 565 ILE ILE D . n 
D 2 2   GLY 2   566 566 GLY GLY D . n 
D 2 3   ASP 3   567 567 ASP ASP D . n 
D 2 4   GLY 4   568 568 GLY GLY D . n 
D 2 5   LEU 5   569 569 LEU LEU D . n 
D 2 6   SER 6   570 570 SER SER D . n 
D 2 7   LEU 7   571 571 LEU LEU D . n 
D 2 8   ILE 8   572 572 ILE ILE D . n 
D 2 9   SER 9   573 573 SER SER D . n 
D 2 10  ILE 10  574 574 ILE ILE D . n 
D 2 11  ILE 11  575 575 ILE ILE D . n 
D 2 12  ASP 12  576 576 ASP ASP D . n 
D 2 13  GLU 13  577 577 GLU GLU D . n 
D 2 14  VAL 14  578 578 VAL VAL D . n 
D 2 15  GLY 15  579 579 GLY GLY D . n 
D 2 16  ASN 16  580 580 ASN ASN D . n 
D 2 17  GLY 17  581 581 GLY GLY D . n 
D 2 18  GLU 18  582 582 GLU GLU D . n 
D 2 19  TYR 19  583 583 TYR TYR D . n 
D 2 20  TRP 20  584 584 TRP TRP D . n 
D 2 21  SER 21  585 585 SER SER D . n 
D 2 22  ALA 22  586 586 ALA ALA D . n 
D 2 23  ALA 23  587 587 ALA ALA D . n 
D 2 24  GLY 24  588 588 GLY GLY D . n 
D 2 25  ASP 25  589 589 ASP ASP D . n 
D 2 26  ILE 26  590 590 ILE ILE D . n 
D 2 27  LEU 27  591 591 LEU LEU D . n 
D 2 28  LEU 28  592 592 LEU LEU D . n 
D 2 29  PHE 29  593 593 PHE PHE D . n 
D 2 30  ALA 30  594 594 ALA ALA D . n 
D 2 31  ALA 31  595 595 ALA ALA D . n 
D 2 32  GLY 32  596 596 GLY GLY D . n 
D 2 33  LYS 33  597 597 LYS LYS D . n 
D 2 34  THR 34  598 598 THR THR D . n 
D 2 35  LYS 35  599 599 LYS LYS D . n 
D 2 36  LEU 36  600 600 LEU LEU D . n 
D 2 37  SER 37  601 601 SER SER D . n 
D 2 38  PRO 38  602 602 PRO PRO D . n 
D 2 39  TYR 39  603 603 TYR TYR D . n 
D 2 40  MET 40  604 604 MET MET D . n 
D 2 41  THR 41  605 605 THR THR D . n 
D 2 42  VAL 42  606 606 VAL VAL D . n 
D 2 43  ILE 43  607 607 ILE ILE D . n 
D 2 44  SER 44  608 608 SER SER D . n 
D 2 45  LEU 45  609 609 LEU LEU D . n 
D 2 46  GLY 46  610 610 GLY GLY D . n 
D 2 47  THR 47  611 611 THR THR D . n 
D 2 48  TRP 48  612 612 TRP TRP D . n 
D 2 49  MET 49  613 613 MET MET D . n 
D 2 50  TYR 50  614 614 TYR TYR D . n 
D 2 51  GLU 51  615 615 GLU GLU D . n 
D 2 52  THR 52  616 616 THR THR D . n 
D 2 53  ASP 53  617 617 ASP ASP D . n 
D 2 54  LEU 54  618 618 LEU LEU D . n 
D 2 55  MET 55  619 619 MET MET D . n 
D 2 56  GLN 56  620 620 GLN GLN D . n 
D 2 57  TRP 57  621 621 TRP TRP D . n 
D 2 58  ARG 58  622 622 ARG ARG D . n 
D 2 59  LEU 59  623 623 LEU LEU D . n 
D 2 60  ALA 60  624 624 ALA ALA D . n 
D 2 61  CYS 61  625 625 CYS CYS D . n 
D 2 62  ILE 62  626 626 ILE ILE D . n 
D 2 63  ASN 63  627 627 ASN ASN D . n 
D 2 64  TYR 64  628 628 TYR TYR D . n 
D 2 65  SER 65  629 629 SER SER D . n 
D 2 66  ASP 66  630 630 ASP ASP D . n 
D 2 67  TYR 67  631 631 TYR TYR D . n 
D 2 68  LYS 68  632 632 LYS LYS D . n 
D 2 69  LYS 69  633 633 LYS LYS D . n 
D 2 70  THR 70  634 634 THR THR D . n 
D 2 71  LEU 71  635 635 LEU LEU D . n 
D 2 72  ILE 72  636 636 ILE ILE D . n 
D 2 73  LYS 73  637 637 LYS LYS D . n 
D 2 74  TYR 74  638 638 TYR TYR D . n 
D 2 75  ARG 75  639 639 ARG ARG D . n 
D 2 76  GLU 76  640 640 GLU GLU D . n 
D 2 77  LEU 77  641 ?   ?   ?   D . n 
D 2 78  GLN 78  642 ?   ?   ?   D . n 
D 2 79  LYS 79  643 ?   ?   ?   D . n 
D 2 80  LYS 80  644 ?   ?   ?   D . n 
D 2 81  PHE 81  645 ?   ?   ?   D . n 
D 2 82  GLU 82  646 ?   ?   ?   D . n 
D 2 83  SER 83  647 ?   ?   ?   D . n 
D 2 84  GLY 84  648 ?   ?   ?   D . n 
D 2 85  ASP 85  649 ?   ?   ?   D . n 
D 2 86  LYS 86  650 ?   ?   ?   D . n 
D 2 87  SER 87  651 ?   ?   ?   D . n 
D 2 88  VAL 88  652 ?   ?   ?   D . n 
D 2 89  GLU 89  653 ?   ?   ?   D . n 
D 2 90  GLU 90  654 ?   ?   ?   D . n 
D 2 91  LYS 91  655 ?   ?   ?   D . n 
D 2 92  MET 92  656 ?   ?   ?   D . n 
D 2 93  ASN 93  657 ?   ?   ?   D . n 
D 2 94  GLU 94  658 ?   ?   ?   D . n 
D 2 95  CYS 95  659 659 CYS CYS D . n 
D 2 96  HIS 96  660 660 HIS HIS D . n 
D 2 97  LYS 97  661 661 LYS LYS D . n 
D 2 98  ILE 98  662 662 ILE ILE D . n 
D 2 99  LEU 99  663 663 LEU LEU D . n 
D 2 100 ASN 100 664 664 ASN ASN D . n 
D 2 101 SER 101 665 665 SER SER D . n 
D 2 102 HIS 102 666 666 HIS HIS D . n 
D 2 103 TYR 103 667 667 TYR TYR D . n 
D 2 104 ILE 104 668 668 ILE ILE D . n 
D 2 105 GLU 105 669 669 GLU GLU D . n 
D 2 106 MET 106 670 670 MET MET D . n 
D 2 107 GLN 107 671 671 GLN GLN D . n 
D 2 108 LYS 108 672 672 LYS LYS D . n 
D 2 109 ASN 109 673 673 ASN ASN D . n 
D 2 110 LEU 110 674 674 LEU LEU D . n 
D 2 111 GLY 111 675 675 GLY GLY D . n 
D 2 112 ASN 112 676 676 ASN ASN D . n 
D 2 113 LEU 113 677 677 LEU LEU D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GOL 1   701  701  GOL GOL A . 
F 3 GOL 1   702  801  GOL GOL A . 
G 3 GOL 1   703  901  GOL GOL A . 
H 3 GOL 1   704  1001 GOL GOL A . 
I 3 GOL 1   701  701  GOL GOL B . 
J 3 GOL 1   702  801  GOL GOL B . 
K 3 GOL 1   703  901  GOL GOL B . 
L 3 GOL 1   704  1001 GOL GOL B . 
M 3 GOL 1   1101 1101 GOL GOL C . 
N 3 GOL 1   1102 1    GOL GOL C . 
O 4 HOH 1   801  282  HOH HOH A . 
O 4 HOH 2   802  36   HOH HOH A . 
O 4 HOH 3   803  403  HOH HOH A . 
O 4 HOH 4   804  179  HOH HOH A . 
O 4 HOH 5   805  436  HOH HOH A . 
O 4 HOH 6   806  429  HOH HOH A . 
O 4 HOH 7   807  97   HOH HOH A . 
O 4 HOH 8   808  167  HOH HOH A . 
O 4 HOH 9   809  71   HOH HOH A . 
O 4 HOH 10  810  553  HOH HOH A . 
O 4 HOH 11  811  298  HOH HOH A . 
O 4 HOH 12  812  342  HOH HOH A . 
O 4 HOH 13  813  169  HOH HOH A . 
O 4 HOH 14  814  126  HOH HOH A . 
O 4 HOH 15  815  74   HOH HOH A . 
O 4 HOH 16  816  203  HOH HOH A . 
O 4 HOH 17  817  131  HOH HOH A . 
O 4 HOH 18  818  122  HOH HOH A . 
O 4 HOH 19  819  336  HOH HOH A . 
O 4 HOH 20  820  350  HOH HOH A . 
O 4 HOH 21  821  38   HOH HOH A . 
O 4 HOH 22  822  14   HOH HOH A . 
O 4 HOH 23  823  368  HOH HOH A . 
O 4 HOH 24  824  132  HOH HOH A . 
O 4 HOH 25  825  136  HOH HOH A . 
O 4 HOH 26  826  11   HOH HOH A . 
O 4 HOH 27  827  269  HOH HOH A . 
O 4 HOH 28  828  383  HOH HOH A . 
O 4 HOH 29  829  77   HOH HOH A . 
O 4 HOH 30  830  301  HOH HOH A . 
O 4 HOH 31  831  251  HOH HOH A . 
O 4 HOH 32  832  285  HOH HOH A . 
O 4 HOH 33  833  191  HOH HOH A . 
O 4 HOH 34  834  160  HOH HOH A . 
O 4 HOH 35  835  273  HOH HOH A . 
O 4 HOH 36  836  228  HOH HOH A . 
O 4 HOH 37  837  433  HOH HOH A . 
O 4 HOH 38  838  221  HOH HOH A . 
O 4 HOH 39  839  373  HOH HOH A . 
O 4 HOH 40  840  61   HOH HOH A . 
O 4 HOH 41  841  119  HOH HOH A . 
O 4 HOH 42  842  460  HOH HOH A . 
O 4 HOH 43  843  116  HOH HOH A . 
O 4 HOH 44  844  154  HOH HOH A . 
O 4 HOH 45  845  155  HOH HOH A . 
O 4 HOH 46  846  290  HOH HOH A . 
O 4 HOH 47  847  244  HOH HOH A . 
O 4 HOH 48  848  37   HOH HOH A . 
O 4 HOH 49  849  556  HOH HOH A . 
O 4 HOH 50  850  109  HOH HOH A . 
O 4 HOH 51  851  360  HOH HOH A . 
O 4 HOH 52  852  442  HOH HOH A . 
O 4 HOH 53  853  15   HOH HOH A . 
O 4 HOH 54  854  27   HOH HOH A . 
O 4 HOH 55  855  41   HOH HOH A . 
O 4 HOH 56  856  4    HOH HOH A . 
O 4 HOH 57  857  324  HOH HOH A . 
O 4 HOH 58  858  142  HOH HOH A . 
O 4 HOH 59  859  348  HOH HOH A . 
O 4 HOH 60  860  110  HOH HOH A . 
O 4 HOH 61  861  162  HOH HOH A . 
O 4 HOH 62  862  502  HOH HOH A . 
O 4 HOH 63  863  539  HOH HOH A . 
O 4 HOH 64  864  125  HOH HOH A . 
O 4 HOH 65  865  195  HOH HOH A . 
O 4 HOH 66  866  279  HOH HOH A . 
O 4 HOH 67  867  84   HOH HOH A . 
O 4 HOH 68  868  3    HOH HOH A . 
O 4 HOH 69  869  55   HOH HOH A . 
O 4 HOH 70  870  135  HOH HOH A . 
O 4 HOH 71  871  177  HOH HOH A . 
O 4 HOH 72  872  89   HOH HOH A . 
O 4 HOH 73  873  245  HOH HOH A . 
O 4 HOH 74  874  254  HOH HOH A . 
O 4 HOH 75  875  33   HOH HOH A . 
O 4 HOH 76  876  491  HOH HOH A . 
O 4 HOH 77  877  452  HOH HOH A . 
O 4 HOH 78  878  274  HOH HOH A . 
O 4 HOH 79  879  117  HOH HOH A . 
O 4 HOH 80  880  335  HOH HOH A . 
O 4 HOH 81  881  174  HOH HOH A . 
O 4 HOH 82  882  357  HOH HOH A . 
O 4 HOH 83  883  10   HOH HOH A . 
O 4 HOH 84  884  317  HOH HOH A . 
O 4 HOH 85  885  85   HOH HOH A . 
O 4 HOH 86  886  139  HOH HOH A . 
O 4 HOH 87  887  50   HOH HOH A . 
O 4 HOH 88  888  353  HOH HOH A . 
O 4 HOH 89  889  123  HOH HOH A . 
O 4 HOH 90  890  92   HOH HOH A . 
O 4 HOH 91  891  214  HOH HOH A . 
O 4 HOH 92  892  428  HOH HOH A . 
O 4 HOH 93  893  209  HOH HOH A . 
O 4 HOH 94  894  83   HOH HOH A . 
O 4 HOH 95  895  537  HOH HOH A . 
O 4 HOH 96  896  293  HOH HOH A . 
O 4 HOH 97  897  19   HOH HOH A . 
O 4 HOH 98  898  114  HOH HOH A . 
O 4 HOH 99  899  376  HOH HOH A . 
O 4 HOH 100 900  557  HOH HOH A . 
O 4 HOH 101 901  208  HOH HOH A . 
O 4 HOH 102 902  319  HOH HOH A . 
O 4 HOH 103 903  219  HOH HOH A . 
O 4 HOH 104 904  158  HOH HOH A . 
O 4 HOH 105 905  129  HOH HOH A . 
O 4 HOH 106 906  63   HOH HOH A . 
O 4 HOH 107 907  535  HOH HOH A . 
O 4 HOH 108 908  28   HOH HOH A . 
O 4 HOH 109 909  265  HOH HOH A . 
O 4 HOH 110 910  395  HOH HOH A . 
O 4 HOH 111 911  172  HOH HOH A . 
O 4 HOH 112 912  188  HOH HOH A . 
O 4 HOH 113 913  256  HOH HOH A . 
O 4 HOH 114 914  182  HOH HOH A . 
O 4 HOH 115 915  483  HOH HOH A . 
O 4 HOH 116 916  138  HOH HOH A . 
O 4 HOH 117 917  205  HOH HOH A . 
O 4 HOH 118 918  379  HOH HOH A . 
O 4 HOH 119 919  464  HOH HOH A . 
O 4 HOH 120 920  68   HOH HOH A . 
O 4 HOH 121 921  286  HOH HOH A . 
O 4 HOH 122 922  349  HOH HOH A . 
O 4 HOH 123 923  193  HOH HOH A . 
O 4 HOH 124 924  283  HOH HOH A . 
O 4 HOH 125 925  517  HOH HOH A . 
O 4 HOH 126 926  151  HOH HOH A . 
O 4 HOH 127 927  288  HOH HOH A . 
O 4 HOH 128 928  18   HOH HOH A . 
O 4 HOH 129 929  545  HOH HOH A . 
O 4 HOH 130 930  565  HOH HOH A . 
O 4 HOH 131 931  398  HOH HOH A . 
O 4 HOH 132 932  217  HOH HOH A . 
O 4 HOH 133 933  47   HOH HOH A . 
O 4 HOH 134 934  258  HOH HOH A . 
O 4 HOH 135 935  492  HOH HOH A . 
O 4 HOH 136 936  78   HOH HOH A . 
O 4 HOH 137 937  192  HOH HOH A . 
O 4 HOH 138 938  240  HOH HOH A . 
O 4 HOH 139 939  81   HOH HOH A . 
O 4 HOH 140 940  540  HOH HOH A . 
O 4 HOH 141 941  555  HOH HOH A . 
O 4 HOH 142 942  218  HOH HOH A . 
O 4 HOH 143 943  133  HOH HOH A . 
O 4 HOH 144 944  338  HOH HOH A . 
O 4 HOH 145 945  359  HOH HOH A . 
O 4 HOH 146 946  17   HOH HOH A . 
O 4 HOH 147 947  518  HOH HOH A . 
O 4 HOH 148 948  272  HOH HOH A . 
O 4 HOH 149 949  225  HOH HOH A . 
O 4 HOH 150 950  330  HOH HOH A . 
O 4 HOH 151 951  175  HOH HOH A . 
O 4 HOH 152 952  247  HOH HOH A . 
O 4 HOH 153 953  62   HOH HOH A . 
O 4 HOH 154 954  233  HOH HOH A . 
O 4 HOH 155 955  339  HOH HOH A . 
O 4 HOH 156 956  358  HOH HOH A . 
O 4 HOH 157 957  564  HOH HOH A . 
O 4 HOH 158 958  198  HOH HOH A . 
O 4 HOH 159 959  127  HOH HOH A . 
O 4 HOH 160 960  385  HOH HOH A . 
O 4 HOH 161 961  281  HOH HOH A . 
O 4 HOH 162 962  235  HOH HOH A . 
O 4 HOH 163 963  532  HOH HOH A . 
O 4 HOH 164 964  554  HOH HOH A . 
O 4 HOH 165 965  337  HOH HOH A . 
O 4 HOH 166 966  451  HOH HOH A . 
O 4 HOH 167 967  484  HOH HOH A . 
O 4 HOH 168 968  44   HOH HOH A . 
O 4 HOH 169 969  186  HOH HOH A . 
O 4 HOH 170 970  267  HOH HOH A . 
O 4 HOH 171 971  189  HOH HOH A . 
O 4 HOH 172 972  255  HOH HOH A . 
O 4 HOH 173 973  73   HOH HOH A . 
O 4 HOH 174 974  29   HOH HOH A . 
O 4 HOH 175 975  563  HOH HOH A . 
O 4 HOH 176 976  512  HOH HOH A . 
O 4 HOH 177 977  414  HOH HOH A . 
O 4 HOH 178 978  481  HOH HOH A . 
O 4 HOH 179 979  259  HOH HOH A . 
O 4 HOH 180 980  538  HOH HOH A . 
O 4 HOH 181 981  522  HOH HOH A . 
O 4 HOH 182 982  480  HOH HOH A . 
O 4 HOH 183 983  120  HOH HOH A . 
O 4 HOH 184 984  500  HOH HOH A . 
O 4 HOH 185 985  533  HOH HOH A . 
O 4 HOH 186 986  266  HOH HOH A . 
O 4 HOH 187 987  536  HOH HOH A . 
O 4 HOH 188 988  372  HOH HOH A . 
O 4 HOH 189 989  525  HOH HOH A . 
O 4 HOH 190 990  463  HOH HOH A . 
O 4 HOH 191 991  408  HOH HOH A . 
O 4 HOH 192 992  411  HOH HOH A . 
O 4 HOH 193 993  510  HOH HOH A . 
P 4 HOH 1   801  277  HOH HOH B . 
P 4 HOH 2   802  498  HOH HOH B . 
P 4 HOH 3   803  213  HOH HOH B . 
P 4 HOH 4   804  529  HOH HOH B . 
P 4 HOH 5   805  137  HOH HOH B . 
P 4 HOH 6   806  246  HOH HOH B . 
P 4 HOH 7   807  351  HOH HOH B . 
P 4 HOH 8   808  49   HOH HOH B . 
P 4 HOH 9   809  13   HOH HOH B . 
P 4 HOH 10  810  216  HOH HOH B . 
P 4 HOH 11  811  393  HOH HOH B . 
P 4 HOH 12  812  544  HOH HOH B . 
P 4 HOH 13  813  332  HOH HOH B . 
P 4 HOH 14  814  130  HOH HOH B . 
P 4 HOH 15  815  26   HOH HOH B . 
P 4 HOH 16  816  241  HOH HOH B . 
P 4 HOH 17  817  501  HOH HOH B . 
P 4 HOH 18  818  144  HOH HOH B . 
P 4 HOH 19  819  243  HOH HOH B . 
P 4 HOH 20  820  86   HOH HOH B . 
P 4 HOH 21  821  46   HOH HOH B . 
P 4 HOH 22  822  30   HOH HOH B . 
P 4 HOH 23  823  547  HOH HOH B . 
P 4 HOH 24  824  220  HOH HOH B . 
P 4 HOH 25  825  106  HOH HOH B . 
P 4 HOH 26  826  223  HOH HOH B . 
P 4 HOH 27  827  54   HOH HOH B . 
P 4 HOH 28  828  94   HOH HOH B . 
P 4 HOH 29  829  157  HOH HOH B . 
P 4 HOH 30  830  365  HOH HOH B . 
P 4 HOH 31  831  43   HOH HOH B . 
P 4 HOH 32  832  57   HOH HOH B . 
P 4 HOH 33  833  278  HOH HOH B . 
P 4 HOH 34  834  163  HOH HOH B . 
P 4 HOH 35  835  364  HOH HOH B . 
P 4 HOH 36  836  23   HOH HOH B . 
P 4 HOH 37  837  343  HOH HOH B . 
P 4 HOH 38  838  93   HOH HOH B . 
P 4 HOH 39  839  2    HOH HOH B . 
P 4 HOH 40  840  8    HOH HOH B . 
P 4 HOH 41  841  173  HOH HOH B . 
P 4 HOH 42  842  543  HOH HOH B . 
P 4 HOH 43  843  21   HOH HOH B . 
P 4 HOH 44  844  519  HOH HOH B . 
P 4 HOH 45  845  249  HOH HOH B . 
P 4 HOH 46  846  24   HOH HOH B . 
P 4 HOH 47  847  224  HOH HOH B . 
P 4 HOH 48  848  420  HOH HOH B . 
P 4 HOH 49  849  284  HOH HOH B . 
P 4 HOH 50  850  102  HOH HOH B . 
P 4 HOH 51  851  541  HOH HOH B . 
P 4 HOH 52  852  6    HOH HOH B . 
P 4 HOH 53  853  520  HOH HOH B . 
P 4 HOH 54  854  226  HOH HOH B . 
P 4 HOH 55  855  159  HOH HOH B . 
P 4 HOH 56  856  82   HOH HOH B . 
P 4 HOH 57  857  180  HOH HOH B . 
P 4 HOH 58  858  280  HOH HOH B . 
P 4 HOH 59  859  550  HOH HOH B . 
P 4 HOH 60  860  5    HOH HOH B . 
P 4 HOH 61  861  318  HOH HOH B . 
P 4 HOH 62  862  64   HOH HOH B . 
P 4 HOH 63  863  118  HOH HOH B . 
P 4 HOH 64  864  166  HOH HOH B . 
P 4 HOH 65  865  264  HOH HOH B . 
P 4 HOH 66  866  434  HOH HOH B . 
P 4 HOH 67  867  531  HOH HOH B . 
P 4 HOH 68  868  72   HOH HOH B . 
P 4 HOH 69  869  521  HOH HOH B . 
P 4 HOH 70  870  153  HOH HOH B . 
P 4 HOH 71  871  149  HOH HOH B . 
P 4 HOH 72  872  310  HOH HOH B . 
P 4 HOH 73  873  150  HOH HOH B . 
P 4 HOH 74  874  309  HOH HOH B . 
P 4 HOH 75  875  69   HOH HOH B . 
P 4 HOH 76  876  253  HOH HOH B . 
P 4 HOH 77  877  66   HOH HOH B . 
P 4 HOH 78  878  386  HOH HOH B . 
P 4 HOH 79  879  299  HOH HOH B . 
P 4 HOH 80  880  1    HOH HOH B . 
P 4 HOH 81  881  22   HOH HOH B . 
P 4 HOH 82  882  331  HOH HOH B . 
P 4 HOH 83  883  20   HOH HOH B . 
P 4 HOH 84  884  99   HOH HOH B . 
P 4 HOH 85  885  227  HOH HOH B . 
P 4 HOH 86  886  551  HOH HOH B . 
P 4 HOH 87  887  65   HOH HOH B . 
P 4 HOH 88  888  320  HOH HOH B . 
P 4 HOH 89  889  270  HOH HOH B . 
P 4 HOH 90  890  134  HOH HOH B . 
P 4 HOH 91  891  445  HOH HOH B . 
P 4 HOH 92  892  108  HOH HOH B . 
P 4 HOH 93  893  112  HOH HOH B . 
P 4 HOH 94  894  79   HOH HOH B . 
P 4 HOH 95  895  333  HOH HOH B . 
P 4 HOH 96  896  147  HOH HOH B . 
P 4 HOH 97  897  390  HOH HOH B . 
P 4 HOH 98  898  271  HOH HOH B . 
P 4 HOH 99  899  100  HOH HOH B . 
P 4 HOH 100 900  12   HOH HOH B . 
P 4 HOH 101 901  165  HOH HOH B . 
P 4 HOH 102 902  552  HOH HOH B . 
P 4 HOH 103 903  145  HOH HOH B . 
P 4 HOH 104 904  16   HOH HOH B . 
P 4 HOH 105 905  430  HOH HOH B . 
P 4 HOH 106 906  34   HOH HOH B . 
P 4 HOH 107 907  45   HOH HOH B . 
P 4 HOH 108 908  234  HOH HOH B . 
P 4 HOH 109 909  53   HOH HOH B . 
P 4 HOH 110 910  315  HOH HOH B . 
P 4 HOH 111 911  42   HOH HOH B . 
P 4 HOH 112 912  80   HOH HOH B . 
P 4 HOH 113 913  215  HOH HOH B . 
P 4 HOH 114 914  107  HOH HOH B . 
P 4 HOH 115 915  495  HOH HOH B . 
P 4 HOH 116 916  146  HOH HOH B . 
P 4 HOH 117 917  148  HOH HOH B . 
P 4 HOH 118 918  105  HOH HOH B . 
P 4 HOH 119 919  128  HOH HOH B . 
P 4 HOH 120 920  211  HOH HOH B . 
P 4 HOH 121 921  40   HOH HOH B . 
P 4 HOH 122 922  96   HOH HOH B . 
P 4 HOH 123 923  140  HOH HOH B . 
P 4 HOH 124 924  314  HOH HOH B . 
P 4 HOH 125 925  199  HOH HOH B . 
P 4 HOH 126 926  559  HOH HOH B . 
P 4 HOH 127 927  200  HOH HOH B . 
P 4 HOH 128 928  229  HOH HOH B . 
P 4 HOH 129 929  523  HOH HOH B . 
P 4 HOH 130 930  546  HOH HOH B . 
P 4 HOH 131 931  32   HOH HOH B . 
P 4 HOH 132 932  321  HOH HOH B . 
P 4 HOH 133 933  399  HOH HOH B . 
P 4 HOH 134 934  548  HOH HOH B . 
P 4 HOH 135 935  31   HOH HOH B . 
P 4 HOH 136 936  378  HOH HOH B . 
P 4 HOH 137 937  340  HOH HOH B . 
P 4 HOH 138 938  275  HOH HOH B . 
P 4 HOH 139 939  103  HOH HOH B . 
P 4 HOH 140 940  25   HOH HOH B . 
P 4 HOH 141 941  402  HOH HOH B . 
P 4 HOH 142 942  87   HOH HOH B . 
P 4 HOH 143 943  239  HOH HOH B . 
P 4 HOH 144 944  98   HOH HOH B . 
P 4 HOH 145 945  311  HOH HOH B . 
P 4 HOH 146 946  313  HOH HOH B . 
P 4 HOH 147 947  252  HOH HOH B . 
P 4 HOH 148 948  232  HOH HOH B . 
P 4 HOH 149 949  230  HOH HOH B . 
P 4 HOH 150 950  88   HOH HOH B . 
P 4 HOH 151 951  296  HOH HOH B . 
P 4 HOH 152 952  262  HOH HOH B . 
P 4 HOH 153 953  237  HOH HOH B . 
P 4 HOH 154 954  51   HOH HOH B . 
P 4 HOH 155 955  115  HOH HOH B . 
P 4 HOH 156 956  504  HOH HOH B . 
P 4 HOH 157 957  113  HOH HOH B . 
P 4 HOH 158 958  397  HOH HOH B . 
P 4 HOH 159 959  152  HOH HOH B . 
P 4 HOH 160 960  161  HOH HOH B . 
P 4 HOH 161 961  326  HOH HOH B . 
P 4 HOH 162 962  104  HOH HOH B . 
P 4 HOH 163 963  303  HOH HOH B . 
P 4 HOH 164 964  394  HOH HOH B . 
P 4 HOH 165 965  52   HOH HOH B . 
P 4 HOH 166 966  141  HOH HOH B . 
P 4 HOH 167 967  499  HOH HOH B . 
P 4 HOH 168 968  222  HOH HOH B . 
P 4 HOH 169 969  530  HOH HOH B . 
P 4 HOH 170 970  190  HOH HOH B . 
P 4 HOH 171 971  561  HOH HOH B . 
P 4 HOH 172 972  489  HOH HOH B . 
P 4 HOH 173 973  212  HOH HOH B . 
P 4 HOH 174 974  526  HOH HOH B . 
P 4 HOH 175 975  352  HOH HOH B . 
P 4 HOH 176 976  231  HOH HOH B . 
P 4 HOH 177 977  527  HOH HOH B . 
P 4 HOH 178 978  356  HOH HOH B . 
P 4 HOH 179 979  242  HOH HOH B . 
P 4 HOH 180 980  558  HOH HOH B . 
P 4 HOH 181 981  560  HOH HOH B . 
P 4 HOH 182 982  67   HOH HOH B . 
P 4 HOH 183 983  59   HOH HOH B . 
P 4 HOH 184 984  257  HOH HOH B . 
P 4 HOH 185 985  508  HOH HOH B . 
P 4 HOH 186 986  507  HOH HOH B . 
P 4 HOH 187 987  511  HOH HOH B . 
P 4 HOH 188 988  419  HOH HOH B . 
P 4 HOH 189 989  427  HOH HOH B . 
P 4 HOH 190 990  524  HOH HOH B . 
P 4 HOH 191 991  494  HOH HOH B . 
P 4 HOH 192 992  401  HOH HOH B . 
P 4 HOH 193 993  528  HOH HOH B . 
P 4 HOH 194 994  534  HOH HOH B . 
P 4 HOH 195 995  441  HOH HOH B . 
P 4 HOH 196 996  514  HOH HOH B . 
P 4 HOH 197 997  268  HOH HOH B . 
P 4 HOH 198 998  505  HOH HOH B . 
P 4 HOH 199 999  513  HOH HOH B . 
Q 4 HOH 1   1201 90   HOH HOH C . 
Q 4 HOH 2   1202 39   HOH HOH C . 
Q 4 HOH 3   1203 178  HOH HOH C . 
Q 4 HOH 4   1204 111  HOH HOH C . 
Q 4 HOH 5   1205 58   HOH HOH C . 
Q 4 HOH 6   1206 101  HOH HOH C . 
Q 4 HOH 7   1207 9    HOH HOH C . 
Q 4 HOH 8   1208 183  HOH HOH C . 
Q 4 HOH 9   1209 423  HOH HOH C . 
Q 4 HOH 10  1210 204  HOH HOH C . 
Q 4 HOH 11  1211 305  HOH HOH C . 
Q 4 HOH 12  1212 56   HOH HOH C . 
Q 4 HOH 13  1213 48   HOH HOH C . 
Q 4 HOH 14  1214 562  HOH HOH C . 
R 4 HOH 1   701  70   HOH HOH D . 
R 4 HOH 2   702  389  HOH HOH D . 
R 4 HOH 3   703  7    HOH HOH D . 
R 4 HOH 4   704  367  HOH HOH D . 
R 4 HOH 5   705  196  HOH HOH D . 
R 4 HOH 6   706  542  HOH HOH D . 
R 4 HOH 7   707  238  HOH HOH D . 
R 4 HOH 8   708  143  HOH HOH D . 
R 4 HOH 9   709  91   HOH HOH D . 
R 4 HOH 10  710  76   HOH HOH D . 
R 4 HOH 11  711  549  HOH HOH D . 
R 4 HOH 12  712  207  HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? Blu-Ice  ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZHS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.175 
_cell.length_a_esd                 ? 
_cell.length_b                     253.874 
_cell.length_b_esd                 ? 
_cell.length_c                     56.320 
_cell.length_c_esd                 ? 
_cell.volume                       1489513.285 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZHS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZHS 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.19 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% v/v 2-Propanol, 0.1 M BICINE pH 8.5 and 30% w/v PEG1500' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-08-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_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                        'NFPSS BEAMLINE BL18U' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U 
_diffrn_source.pdbx_synchrotron_site       NFPSS 
# 
_reflns.B_iso_Wilson_estimate                          40.30 
_reflns.entry_id                                       8ZHS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               42.13 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     55319 
_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                           93.21 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.56 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4 
_reflns_shell.d_res_low                                     2.5 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4190 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.53 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.72 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZHS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             42.13 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     55314 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  53314 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.24 
_refine.ls_percent_reflns_R_free                 3.62 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1895 
_refine.ls_R_factor_R_free                       0.2378 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1876 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.5905 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2881 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        42.13 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               10039 
_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        9561 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_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' ? 0.0079  ? 9845  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1735  ? 13336 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0636  ? 1450  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0084  ? 1689  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.3147 ? 3593  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.46  . . 105 2795 69.18 . . . . 0.2725 . . . . . . . . . . . 0.3753 
'X-RAY DIFFRACTION' 2.46 2.53  . . 120 3222 80.51 . . . . 0.2673 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 2.53 2.60  . . 129 3411 84.51 . . . . 0.2511 . . . . . . . . . . . 0.3411 
'X-RAY DIFFRACTION' 2.60 2.69  . . 137 3661 90.43 . . . . 0.2479 . . . . . . . . . . . 0.2778 
'X-RAY DIFFRACTION' 2.69 2.78  . . 141 3759 94.20 . . . . 0.2372 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 2.78 2.90  . . 147 3912 96.41 . . . . 0.2188 . . . . . . . . . . . 0.2741 
'X-RAY DIFFRACTION' 2.90 3.03  . . 147 3925 97.35 . . . . 0.2145 . . . . . . . . . . . 0.2927 
'X-RAY DIFFRACTION' 3.03 3.19  . . 150 4011 98.37 . . . . 0.2133 . . . . . . . . . . . 0.2946 
'X-RAY DIFFRACTION' 3.19 3.39  . . 150 3998 98.60 . . . . 0.2023 . . . . . . . . . . . 0.2551 
'X-RAY DIFFRACTION' 3.39 3.65  . . 151 4031 99.36 . . . . 0.1792 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 3.65 4.01  . . 154 4099 99.32 . . . . 0.1598 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 4.02 4.60  . . 154 4083 99.60 . . . . 0.1493 . . . . . . . . . . . 0.1934 
'X-RAY DIFFRACTION' 4.60 5.79  . . 156 4167 99.54 . . . . 0.1587 . . . . . . . . . . . 0.2030 
'X-RAY DIFFRACTION' 5.79 42.13 . . 159 4240 97.04 . . . . 0.1749 . . . . . . . . . . . 0.1899 
# 
_struct.entry_id                     8ZHS 
_struct.title                        'Structure of Mbp-Bte1 fusion protein' 
_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        8ZHS 
_struct_keywords.text            'antibacterial toxin, ANTITOXIN' 
_struct_keywords.pdbx_keywords   ANTITOXIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP MALE_ECOLI   P0AEX9 ? 1 
;KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT
PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL
IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT
MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
27  
2 UNP Q5LDT7_BACFN Q5LDT7 ? 1 
;GKEIEIKKLPEFEAMVNAGNTTYTGLVEGIGYVYWTTETLYFIRTNPEQLWAIPKYQQIPFPYFQRKDAIIETKTLHTLH
VLSKDELLKLDYDAYYAFYGIVEEMLKFIHRADAIKSYCEIPLPIIKSK
;
2   
3 UNP Q5LDT7_BACFN Q5LDT7 ? 2 
;IGDGLSLISIIDEVGNGEYWSAAGDILLFAAGKTKLSPYMTVISLGTWMYETDLMQWRLACINYSDYKKTLIKYRELQKK
FESGDKSVEEKMNECHKILNSHYIEMQKNLGNL
;
172 
# 
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 8ZHS A 2   ? 367 ? P0AEX9 27  ? 392 ? 21  386 
2 2 8ZHS A 376 ? 504 ? Q5LDT7 2   ? 130 ? 395 523 
3 1 8ZHS B 2   ? 367 ? P0AEX9 27  ? 392 ? 21  386 
4 2 8ZHS B 376 ? 504 ? Q5LDT7 2   ? 130 ? 395 523 
5 3 8ZHS C 1   ? 113 ? Q5LDT7 172 ? 284 ? 565 677 
6 3 8ZHS D 1   ? 113 ? Q5LDT7 172 ? 284 ? 565 677 
# 
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 8ZHS MET A 1   ? UNP P0AEX9 ?   ?   'initiating methionine' 20  1  
1 8ZHS ALA A 83  ? UNP P0AEX9 ASP 108 'engineered mutation'   102 2  
1 8ZHS ALA A 84  ? UNP P0AEX9 LYS 109 'engineered mutation'   103 3  
1 8ZHS ALA A 173 ? UNP P0AEX9 GLU 198 'engineered mutation'   192 4  
1 8ZHS ALA A 174 ? UNP P0AEX9 ASN 199 'engineered mutation'   193 5  
1 8ZHS ALA A 240 ? UNP P0AEX9 LYS 265 'engineered mutation'   259 6  
1 8ZHS ALA A 368 ? UNP P0AEX9 ?   ?   linker                  387 7  
1 8ZHS ALA A 369 ? UNP P0AEX9 ?   ?   linker                  388 8  
1 8ZHS ARG A 370 ? UNP P0AEX9 ?   ?   linker                  389 9  
1 8ZHS ALA A 371 ? UNP P0AEX9 ?   ?   linker                  390 10 
1 8ZHS PHE A 372 ? UNP P0AEX9 ?   ?   linker                  391 11 
1 8ZHS ALA A 373 ? UNP P0AEX9 ?   ?   linker                  392 12 
1 8ZHS ALA A 374 ? UNP P0AEX9 ?   ?   linker                  393 13 
1 8ZHS ALA A 375 ? UNP P0AEX9 ?   ?   linker                  394 14 
3 8ZHS MET B 1   ? UNP P0AEX9 ?   ?   'initiating methionine' 20  15 
3 8ZHS ALA B 83  ? UNP P0AEX9 ASP 108 'engineered mutation'   102 16 
3 8ZHS ALA B 84  ? UNP P0AEX9 LYS 109 'engineered mutation'   103 17 
3 8ZHS ALA B 173 ? UNP P0AEX9 GLU 198 'engineered mutation'   192 18 
3 8ZHS ALA B 174 ? UNP P0AEX9 ASN 199 'engineered mutation'   193 19 
3 8ZHS ALA B 240 ? UNP P0AEX9 LYS 265 'engineered mutation'   259 20 
3 8ZHS ALA B 368 ? UNP P0AEX9 ?   ?   linker                  387 21 
3 8ZHS ALA B 369 ? UNP P0AEX9 ?   ?   linker                  388 22 
3 8ZHS ARG B 370 ? UNP P0AEX9 ?   ?   linker                  389 23 
3 8ZHS ALA B 371 ? UNP P0AEX9 ?   ?   linker                  390 24 
3 8ZHS PHE B 372 ? UNP P0AEX9 ?   ?   linker                  391 25 
3 8ZHS ALA B 373 ? UNP P0AEX9 ?   ?   linker                  392 26 
3 8ZHS ALA B 374 ? UNP P0AEX9 ?   ?   linker                  393 27 
3 8ZHS ALA B 375 ? UNP P0AEX9 ?   ?   linker                  394 28 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 16360 ? 
1 MORE         -97   ? 
1 'SSA (A^2)'  50580 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 17  ? GLY A 33  ? GLY A 36  GLY A 52  1 ? 17 
HELX_P HELX_P2  AA2 LYS A 43  ? ALA A 53  ? LYS A 62  ALA A 72  1 ? 11 
HELX_P HELX_P3  AA3 ARG A 67  ? SER A 74  ? ARG A 86  SER A 93  1 ? 8  
HELX_P HELX_P4  AA4 ALA A 83  ? ASP A 88  ? ALA A 102 ASP A 107 1 ? 6  
HELX_P HELX_P5  AA5 TYR A 91  ? VAL A 98  ? TYR A 110 VAL A 117 1 ? 8  
HELX_P HELX_P6  AA6 THR A 129 ? GLU A 131 ? THR A 148 GLU A 150 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 132 ? ALA A 142 ? GLU A 151 ALA A 161 1 ? 11 
HELX_P HELX_P8  AA8 GLU A 154 ? ALA A 164 ? GLU A 173 ALA A 183 1 ? 11 
HELX_P HELX_P9  AA9 ASN A 186 ? ASN A 202 ? ASN A 205 ASN A 221 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 210 ? LYS A 220 ? ASP A 229 LYS A 239 1 ? 11 
HELX_P HELX_P11 AB2 GLY A 229 ? TRP A 231 ? GLY A 248 TRP A 250 5 ? 3  
HELX_P HELX_P12 AB3 ALA A 232 ? SER A 239 ? ALA A 251 SER A 258 1 ? 8  
HELX_P HELX_P13 AB4 ASN A 273 ? TYR A 284 ? ASN A 292 TYR A 303 1 ? 12 
HELX_P HELX_P14 AB5 THR A 287 ? LYS A 298 ? THR A 306 LYS A 317 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 305 ? ALA A 313 ? LEU A 324 ALA A 332 1 ? 9  
HELX_P HELX_P16 AB7 ASP A 315 ? GLY A 328 ? ASP A 334 GLY A 347 1 ? 14 
HELX_P HELX_P17 AB8 GLN A 336 ? SER A 353 ? GLN A 355 SER A 372 1 ? 18 
HELX_P HELX_P18 AB9 THR A 357 ? GLY A 376 ? THR A 376 GLY A 395 1 ? 20 
HELX_P HELX_P19 AC1 LYS A 383 ? ALA A 393 ? LYS A 402 ALA A 412 1 ? 11 
HELX_P HELX_P20 AC2 SER A 458 ? LEU A 465 ? SER A 477 LEU A 484 1 ? 8  
HELX_P HELX_P21 AC3 ALA A 472 ? CYS A 494 ? ALA A 491 CYS A 513 1 ? 23 
HELX_P HELX_P22 AC4 GLY B 17  ? GLY B 33  ? GLY B 36  GLY B 52  1 ? 17 
HELX_P HELX_P23 AC5 LYS B 43  ? ALA B 53  ? LYS B 62  ALA B 72  1 ? 11 
HELX_P HELX_P24 AC6 ARG B 67  ? SER B 74  ? ARG B 86  SER B 93  1 ? 8  
HELX_P HELX_P25 AC7 ALA B 83  ? LYS B 89  ? ALA B 102 LYS B 108 1 ? 7  
HELX_P HELX_P26 AC8 TYR B 91  ? ALA B 97  ? TYR B 110 ALA B 116 1 ? 7  
HELX_P HELX_P27 AC9 GLU B 132 ? LYS B 143 ? GLU B 151 LYS B 162 1 ? 12 
HELX_P HELX_P28 AD1 GLU B 154 ? ALA B 164 ? GLU B 173 ALA B 183 1 ? 11 
HELX_P HELX_P29 AD2 ASN B 186 ? ASN B 202 ? ASN B 205 ASN B 221 1 ? 17 
HELX_P HELX_P30 AD3 ASP B 210 ? LYS B 220 ? ASP B 229 LYS B 239 1 ? 11 
HELX_P HELX_P31 AD4 GLY B 229 ? TRP B 231 ? GLY B 248 TRP B 250 5 ? 3  
HELX_P HELX_P32 AD5 ALA B 232 ? ALA B 240 ? ALA B 251 ALA B 259 1 ? 9  
HELX_P HELX_P33 AD6 ASN B 273 ? TYR B 284 ? ASN B 292 TYR B 303 1 ? 12 
HELX_P HELX_P34 AD7 THR B 287 ? LYS B 298 ? THR B 306 LYS B 317 1 ? 12 
HELX_P HELX_P35 AD8 LEU B 305 ? ALA B 313 ? LEU B 324 ALA B 332 1 ? 9  
HELX_P HELX_P36 AD9 ASP B 315 ? GLY B 328 ? ASP B 334 GLY B 347 1 ? 14 
HELX_P HELX_P37 AE1 GLN B 336 ? SER B 353 ? GLN B 355 SER B 372 1 ? 18 
HELX_P HELX_P38 AE2 THR B 357 ? GLY B 376 ? THR B 376 GLY B 395 1 ? 20 
HELX_P HELX_P39 AE3 LYS B 383 ? ALA B 393 ? LYS B 402 ALA B 412 1 ? 11 
HELX_P HELX_P40 AE4 SER B 458 ? LEU B 465 ? SER B 477 LEU B 484 1 ? 8  
HELX_P HELX_P41 AE5 ALA B 472 ? CYS B 494 ? ALA B 491 CYS B 513 1 ? 23 
HELX_P HELX_P42 AE6 SER C 37  ? GLY C 46  ? SER C 601 GLY C 610 1 ? 10 
HELX_P HELX_P43 AE7 TYR C 50  ? SER C 83  ? TYR C 614 SER C 647 1 ? 34 
HELX_P HELX_P44 AE8 VAL C 88  ? ASN C 112 ? VAL C 652 ASN C 676 1 ? 25 
HELX_P HELX_P45 AE9 SER D 37  ? GLY D 46  ? SER D 601 GLY D 610 1 ? 10 
HELX_P HELX_P46 AF1 TYR D 50  ? ARG D 75  ? TYR D 614 ARG D 639 1 ? 26 
HELX_P HELX_P47 AF2 HIS D 96  ? GLY D 111 ? HIS D 660 GLY D 675 1 ? 16 
# 
_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 
disulf1 disulf ? ? A CYS 494 SG ? ? ? 1_555 D CYS 61 SG ? ? A CYS 513 D CYS 625 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf2 disulf ? ? B CYS 494 SG ? ? ? 1_555 C CYS 61 SG ? ? B CYS 513 C CYS 625 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
# 
_struct_conn_type.id          disulf 
_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 CYS A 494 ? CYS D 61 ? CYS A 513 ? 1_555 CYS D 625 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 494 ? CYS C 61 ? CYS B 513 ? 1_555 CYS C 625 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
AB1 ? 6 ? 
AB2 ? 5 ? 
AB3 ? 2 ? 
AB4 ? 4 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
AB7 ? 6 ? 
AB8 ? 6 ? 
AB9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? parallel      
AB7 5 6 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB8 5 6 ? anti-parallel 
AB9 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 36  ? GLU A 39  ? VAL A 55  GLU A 58  
AA1 2 LEU A 8   ? TRP A 11  ? LEU A 27  TRP A 30  
AA1 3 ILE A 60  ? ALA A 64  ? ILE A 79  ALA A 83  
AA1 4 PHE A 259 ? ILE A 267 ? PHE A 278 ILE A 286 
AA1 5 TYR A 107 ? GLU A 112 ? TYR A 126 GLU A 131 
AA1 6 ALA A 302 ? VAL A 303 ? ALA A 321 VAL A 322 
AA2 1 VAL A 36  ? GLU A 39  ? VAL A 55  GLU A 58  
AA2 2 LEU A 8   ? TRP A 11  ? LEU A 27  TRP A 30  
AA2 3 ILE A 60  ? ALA A 64  ? ILE A 79  ALA A 83  
AA2 4 PHE A 259 ? ILE A 267 ? PHE A 278 ILE A 286 
AA2 5 GLU A 329 ? ILE A 330 ? GLU A 348 ILE A 349 
AA3 1 ARG A 99  ? TYR A 100 ? ARG A 118 TYR A 119 
AA3 2 LYS A 103 ? LEU A 104 ? LYS A 122 LEU A 123 
AA4 1 SER A 146 ? LEU A 148 ? SER A 165 LEU A 167 
AA4 2 THR A 223 ? ASN A 228 ? THR A 242 ASN A 247 
AA4 3 SER A 115 ? ASN A 119 ? SER A 134 ASN A 138 
AA4 4 TYR A 243 ? THR A 246 ? TYR A 262 THR A 265 
AA5 1 TYR A 168 ? ALA A 173 ? TYR A 187 ALA A 192 
AA5 2 LYS A 176 ? GLY A 183 ? LYS A 195 GLY A 202 
AA6 1 THR A 250 ? PHE A 251 ? THR A 269 PHE A 270 
AA6 2 GLN A 254 ? PRO A 255 ? GLN A 273 PRO A 274 
AA7 1 ILE A 381 ? LYS A 382 ? ILE A 400 LYS A 401 
AA7 2 GLY A 400 ? VAL A 402 ? GLY A 419 VAL A 421 
AA7 3 GLY A 406 ? ARG A 419 ? GLY A 425 ARG A 438 
AA7 4 LYS A 430 ? ILE A 434 ? LYS A 449 ILE A 453 
AA7 5 GLU C 18  ? TRP C 20  ? GLU C 582 TRP C 584 
AA7 6 LEU C 27  ? PHE C 29  ? LEU C 591 PHE C 593 
AA8 1 ILE A 381 ? LYS A 382 ? ILE A 400 LYS A 401 
AA8 2 GLY A 400 ? VAL A 402 ? GLY A 419 VAL A 421 
AA8 3 GLY A 406 ? ARG A 419 ? GLY A 425 ARG A 438 
AA8 4 ILE A 446 ? LEU A 457 ? ILE A 465 LEU A 476 
AA8 5 SER C 9   ? ILE C 11  ? SER C 573 ILE C 575 
AA8 6 LYS C 35  ? LEU C 36  ? LYS C 599 LEU C 600 
AA9 1 ILE A 501 ? LYS A 502 ? ILE A 520 LYS A 521 
AA9 2 THR D 47  ? TRP D 48  ? THR D 611 TRP D 612 
AB1 1 VAL B 36  ? GLU B 39  ? VAL B 55  GLU B 58  
AB1 2 LEU B 8   ? TRP B 11  ? LEU B 27  TRP B 30  
AB1 3 ILE B 60  ? ALA B 64  ? ILE B 79  ALA B 83  
AB1 4 PHE B 259 ? ILE B 267 ? PHE B 278 ILE B 286 
AB1 5 TYR B 107 ? GLU B 112 ? TYR B 126 GLU B 131 
AB1 6 ALA B 302 ? VAL B 303 ? ALA B 321 VAL B 322 
AB2 1 VAL B 36  ? GLU B 39  ? VAL B 55  GLU B 58  
AB2 2 LEU B 8   ? TRP B 11  ? LEU B 27  TRP B 30  
AB2 3 ILE B 60  ? ALA B 64  ? ILE B 79  ALA B 83  
AB2 4 PHE B 259 ? ILE B 267 ? PHE B 278 ILE B 286 
AB2 5 GLU B 329 ? ILE B 330 ? GLU B 348 ILE B 349 
AB3 1 ARG B 99  ? TYR B 100 ? ARG B 118 TYR B 119 
AB3 2 LYS B 103 ? LEU B 104 ? LYS B 122 LEU B 123 
AB4 1 SER B 146 ? LEU B 148 ? SER B 165 LEU B 167 
AB4 2 THR B 223 ? ASN B 228 ? THR B 242 ASN B 247 
AB4 3 SER B 115 ? ASN B 119 ? SER B 134 ASN B 138 
AB4 4 TYR B 243 ? THR B 246 ? TYR B 262 THR B 265 
AB5 1 TYR B 168 ? ALA B 173 ? TYR B 187 ALA B 192 
AB5 2 LYS B 176 ? GLY B 183 ? LYS B 195 GLY B 202 
AB6 1 THR B 250 ? PHE B 251 ? THR B 269 PHE B 270 
AB6 2 GLN B 254 ? PRO B 255 ? GLN B 273 PRO B 274 
AB7 1 ILE B 381 ? LYS B 382 ? ILE B 400 LYS B 401 
AB7 2 GLY B 400 ? VAL B 402 ? GLY B 419 VAL B 421 
AB7 3 GLY B 406 ? ARG B 419 ? GLY B 425 ARG B 438 
AB7 4 LYS B 430 ? GLN B 433 ? LYS B 449 GLN B 452 
AB7 5 GLU D 18  ? TRP D 20  ? GLU D 582 TRP D 584 
AB7 6 LEU D 27  ? PHE D 29  ? LEU D 591 PHE D 593 
AB8 1 ILE B 381 ? LYS B 382 ? ILE B 400 LYS B 401 
AB8 2 GLY B 400 ? VAL B 402 ? GLY B 419 VAL B 421 
AB8 3 GLY B 406 ? ARG B 419 ? GLY B 425 ARG B 438 
AB8 4 ILE B 446 ? LEU B 457 ? ILE B 465 LEU B 476 
AB8 5 SER D 9   ? ILE D 11  ? SER D 573 ILE D 575 
AB8 6 LYS D 35  ? LEU D 36  ? LYS D 599 LEU D 600 
AB9 1 ILE B 501 ? LYS B 502 ? ILE B 520 LYS B 521 
AB9 2 THR C 47  ? TRP C 48  ? THR C 611 TRP C 612 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 39  ? O GLU A 58  N ILE A 10  ? N ILE A 29  
AA1 2 3 N TRP A 11  ? N TRP A 30  O PHE A 62  ? O PHE A 81  
AA1 3 4 N ILE A 61  ? N ILE A 80  O GLY A 266 ? O GLY A 285 
AA1 4 5 O LEU A 263 ? O LEU A 282 N ILE A 109 ? N ILE A 128 
AA1 5 6 N VAL A 111 ? N VAL A 130 O ALA A 302 ? O ALA A 321 
AA2 1 2 O GLU A 39  ? O GLU A 58  N ILE A 10  ? N ILE A 29  
AA2 2 3 N TRP A 11  ? N TRP A 30  O PHE A 62  ? O PHE A 81  
AA2 3 4 N ILE A 61  ? N ILE A 80  O GLY A 266 ? O GLY A 285 
AA2 4 5 N VAL A 260 ? N VAL A 279 O GLU A 329 ? O GLU A 348 
AA3 1 2 N TYR A 100 ? N TYR A 119 O LYS A 103 ? O LYS A 122 
AA4 1 2 N SER A 146 ? N SER A 165 O ALA A 224 ? O ALA A 243 
AA4 2 3 O ALA A 224 ? O ALA A 243 N ASN A 119 ? N ASN A 138 
AA4 3 4 N LEU A 116 ? N LEU A 135 O THR A 246 ? O THR A 265 
AA5 1 2 N LYS A 171 ? N LYS A 190 O ASP A 178 ? O ASP A 197 
AA6 1 2 N PHE A 251 ? N PHE A 270 O GLN A 254 ? O GLN A 273 
AA7 1 2 N LYS A 382 ? N LYS A 401 O LEU A 401 ? O LEU A 420 
AA7 2 3 N VAL A 402 ? N VAL A 421 O GLY A 406 ? O GLY A 425 
AA7 3 4 N ILE A 418 ? N ILE A 437 O GLN A 432 ? O GLN A 451 
AA7 4 5 N TYR A 431 ? N TYR A 450 O GLU C 18  ? O GLU C 582 
AA7 5 6 N TYR C 19  ? N TYR C 583 O PHE C 29  ? O PHE C 593 
AA8 1 2 N LYS A 382 ? N LYS A 401 O LEU A 401 ? O LEU A 420 
AA8 2 3 N VAL A 402 ? N VAL A 421 O GLY A 406 ? O GLY A 425 
AA8 3 4 N GLU A 413 ? N GLU A 432 O LEU A 451 ? O LEU A 470 
AA8 4 5 N HIS A 452 ? N HIS A 471 O ILE C 10  ? O ILE C 574 
AA8 5 6 N SER C 9   ? N SER C 573 O LEU C 36  ? O LEU C 600 
AA9 1 2 N ILE A 501 ? N ILE A 520 O TRP D 48  ? O TRP D 612 
AB1 1 2 O GLU B 39  ? O GLU B 58  N ILE B 10  ? N ILE B 29  
AB1 2 3 N TRP B 11  ? N TRP B 30  O PHE B 62  ? O PHE B 81  
AB1 3 4 N ILE B 61  ? N ILE B 80  O GLY B 266 ? O GLY B 285 
AB1 4 5 O ALA B 265 ? O ALA B 284 N TYR B 107 ? N TYR B 126 
AB1 5 6 N VAL B 111 ? N VAL B 130 O ALA B 302 ? O ALA B 321 
AB2 1 2 O GLU B 39  ? O GLU B 58  N ILE B 10  ? N ILE B 29  
AB2 2 3 N TRP B 11  ? N TRP B 30  O PHE B 62  ? O PHE B 81  
AB2 3 4 N ILE B 61  ? N ILE B 80  O GLY B 266 ? O GLY B 285 
AB2 4 5 N VAL B 260 ? N VAL B 279 O GLU B 329 ? O GLU B 348 
AB3 1 2 N TYR B 100 ? N TYR B 119 O LYS B 103 ? O LYS B 122 
AB4 1 2 N SER B 146 ? N SER B 165 O ALA B 224 ? O ALA B 243 
AB4 2 3 O THR B 226 ? O THR B 245 N ILE B 117 ? N ILE B 136 
AB4 3 4 N TYR B 118 ? N TYR B 137 O GLY B 244 ? O GLY B 263 
AB5 1 2 N LYS B 171 ? N LYS B 190 O ASP B 181 ? O ASP B 200 
AB6 1 2 N PHE B 251 ? N PHE B 270 O GLN B 254 ? O GLN B 273 
AB7 1 2 N LYS B 382 ? N LYS B 401 O LEU B 401 ? O LEU B 420 
AB7 2 3 N VAL B 402 ? N VAL B 421 O GLY B 406 ? O GLY B 425 
AB7 3 4 N ILE B 418 ? N ILE B 437 O GLN B 432 ? O GLN B 451 
AB7 4 5 N TYR B 431 ? N TYR B 450 O GLU D 18  ? O GLU D 582 
AB7 5 6 N TYR D 19  ? N TYR D 583 O PHE D 29  ? O PHE D 593 
AB8 1 2 N LYS B 382 ? N LYS B 401 O LEU B 401 ? O LEU B 420 
AB8 2 3 N VAL B 402 ? N VAL B 421 O GLY B 406 ? O GLY B 425 
AB8 3 4 N TYR B 407 ? N TYR B 426 O LEU B 457 ? O LEU B 476 
AB8 4 5 N HIS B 452 ? N HIS B 471 O ILE D 10  ? O ILE D 574 
AB8 5 6 N SER D 9   ? N SER D 573 O LEU D 36  ? O LEU D 600 
AB9 1 2 N ILE B 501 ? N ILE B 520 O TRP C 48  ? O TRP C 612 
# 
_pdbx_entry_details.entry_id                   8ZHS 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 TRP A 445 ? ? -99.03  53.26  
2 1 TYR A 457 ? ? 74.16   -6.87  
3 1 ALA B 192 ? ? -161.53 113.06 
4 1 TYR B 457 ? ? 65.55   -3.16  
5 1 CYS B 513 ? ? -172.84 132.43 
6 1 ARG D 639 ? ? -80.41  35.34  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B MET 20  ? B MET 1  
2  1 Y 1 C ILE 565 ? C ILE 1  
3  1 Y 1 D LEU 641 ? D LEU 77 
4  1 Y 1 D GLN 642 ? D GLN 78 
5  1 Y 1 D LYS 643 ? D LYS 79 
6  1 Y 1 D LYS 644 ? D LYS 80 
7  1 Y 1 D PHE 645 ? D PHE 81 
8  1 Y 1 D GLU 646 ? D GLU 82 
9  1 Y 1 D SER 647 ? D SER 83 
10 1 Y 1 D GLY 648 ? D GLY 84 
11 1 Y 1 D ASP 649 ? D ASP 85 
12 1 Y 1 D LYS 650 ? D LYS 86 
13 1 Y 1 D SER 651 ? D SER 87 
14 1 Y 1 D VAL 652 ? D VAL 88 
15 1 Y 1 D GLU 653 ? D GLU 89 
16 1 Y 1 D GLU 654 ? D GLU 90 
17 1 Y 1 D LYS 655 ? D LYS 91 
18 1 Y 1 D MET 656 ? D MET 92 
19 1 Y 1 D ASN 657 ? D ASN 93 
20 1 Y 1 D GLU 658 ? D GLU 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1N3W 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZHS 
_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]   0.009599 
_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]   0.003939 
_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]   0.017756 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . MET A 1 1   ? 6.76400   -63.68800 -37.69400 1.000 30.00000  ? 20   MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? 6.80300   -62.75600 -38.84100 1.000 30.00000  ? 20   MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? 6.95200   -61.34200 -38.31200 1.000 30.00000  ? 20   MET A C   1 
ATOM   4     O O   . MET A 1 1   ? 6.28500   -60.99200 -37.36800 1.000 30.00000  ? 20   MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? 5.50500   -62.80200 -39.64100 1.000 30.00000  ? 20   MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? 5.54700   -63.71100 -40.83000 1.000 30.00000  ? 20   MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? 7.00900   -63.43800 -41.80500 1.000 30.00000  ? 20   MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? 8.12300   -64.60800 -41.03400 1.000 30.00000  ? 20   MET A CE  1 
ATOM   9     N N   . LYS A 1 2   ? 7.84700   -60.59100 -38.92600 1.000 60.09000  ? 21   LYS A N   1 
ATOM   10    C CA  . LYS A 1 2   ? 8.04200   -59.16800 -38.60900 1.000 45.51000  ? 21   LYS A CA  1 
ATOM   11    C C   . LYS A 1 2   ? 7.26400   -58.36800 -39.65800 1.000 50.72000  ? 21   LYS A C   1 
ATOM   12    O O   . LYS A 1 2   ? 6.85700   -58.92000 -40.68300 1.000 44.86000  ? 21   LYS A O   1 
ATOM   13    C CB  . LYS A 1 2   ? 9.53800   -58.86000 -38.67500 1.000 43.32000  ? 21   LYS A CB  1 
ATOM   14    C CG  . LYS A 1 2   ? 10.05700  -57.77600 -37.74500 1.000 39.79000  ? 21   LYS A CG  1 
ATOM   15    C CD  . LYS A 1 2   ? 10.25800  -58.22800 -36.32300 1.000 51.74000  ? 21   LYS A CD  1 
ATOM   16    C CE  . LYS A 1 2   ? 11.43000  -59.16200 -36.15200 1.000 61.59000  ? 21   LYS A CE  1 
ATOM   17    N NZ  . LYS A 1 2   ? 11.52700  -60.10500 -37.28600 1.000 50.09000  ? 21   LYS A NZ  1 
ATOM   18    N N   . ILE A 1 3   ? 7.06100   -57.09100 -39.39500 1.000 45.02000  ? 22   ILE A N   1 
ATOM   19    C CA  . ILE A 1 3   ? 6.34000   -56.25700 -40.38400 1.000 43.92000  ? 22   ILE A CA  1 
ATOM   20    C C   . ILE A 1 3   ? 7.17000   -56.22200 -41.66800 1.000 45.32000  ? 22   ILE A C   1 
ATOM   21    O O   . ILE A 1 3   ? 8.36500   -56.04100 -41.58500 1.000 49.36000  ? 22   ILE A O   1 
ATOM   22    C CB  . ILE A 1 3   ? 6.12800   -54.85900 -39.79900 1.000 44.16000  ? 22   ILE A CB  1 
ATOM   23    C CG1 . ILE A 1 3   ? 4.80600   -54.76200 -39.04400 1.000 43.51000  ? 22   ILE A CG1 1 
ATOM   24    C CG2 . ILE A 1 3   ? 6.24400   -53.81300 -40.88000 1.000 45.61000  ? 22   ILE A CG2 1 
ATOM   25    C CD1 . ILE A 1 3   ? 4.68200   -53.52300 -38.21300 1.000 44.63000  ? 22   ILE A CD1 1 
ATOM   26    N N   . GLU A 1 4   ? 6.53000   -56.40700 -42.81300 1.000 48.61000  ? 23   GLU A N   1 
ATOM   27    C CA  . GLU A 1 4   ? 7.21200   -56.37200 -44.09800 1.000 47.54000  ? 23   GLU A CA  1 
ATOM   28    C C   . GLU A 1 4   ? 6.23500   -55.75100 -45.08000 1.000 42.30000  ? 23   GLU A C   1 
ATOM   29    O O   . GLU A 1 4   ? 5.04800   -56.10200 -45.05500 1.000 42.00000  ? 23   GLU A O   1 
ATOM   30    C CB  . GLU A 1 4   ? 7.62800   -57.78600 -44.50900 1.000 51.70000  ? 23   GLU A CB  1 
ATOM   31    C CG  . GLU A 1 4   ? 8.21300   -57.90200 -45.88700 1.000 54.40000  ? 23   GLU A CG  1 
ATOM   32    C CD  . GLU A 1 4   ? 8.54600   -59.35900 -46.27500 1.000 63.09000  ? 23   GLU A CD  1 
ATOM   33    O OE1 . GLU A 1 4   ? 8.50300   -60.25400 -45.39800 1.000 56.06000  ? 23   GLU A OE1 1 
ATOM   34    O OE2 . GLU A 1 4   ? 8.73900   -59.60200 -47.48500 1.000 68.74000  ? 23   GLU A OE2 1 
ATOM   35    N N   . GLU A 1 5   ? 6.70400   -54.82000 -45.90800 1.000 47.94000  ? 24   GLU A N   1 
ATOM   36    C CA  . GLU A 1 5   ? 5.81000   -54.07500 -46.78900 1.000 44.17000  ? 24   GLU A CA  1 
ATOM   37    C C   . GLU A 1 5   ? 5.16400   -55.03400 -47.77800 1.000 51.26000  ? 24   GLU A C   1 
ATOM   38    O O   . GLU A 1 5   ? 5.84700   -55.87900 -48.36500 1.000 62.98000  ? 24   GLU A O   1 
ATOM   39    C CB  . GLU A 1 5   ? 6.60000   -52.98900 -47.53200 1.000 51.03000  ? 24   GLU A CB  1 
ATOM   40    C CG  . GLU A 1 5   ? 5.73800   -51.81300 -47.94700 1.000 63.62000  ? 24   GLU A CG  1 
ATOM   41    C CD  . GLU A 1 5   ? 6.52100   -50.71800 -48.68700 1.000 76.34000  ? 24   GLU A CD  1 
ATOM   42    O OE1 . GLU A 1 5   ? 7.55500   -51.04800 -49.30800 1.000 77.70000  ? 24   GLU A OE1 1 
ATOM   43    O OE2 . GLU A 1 5   ? 6.16200   -49.52400 -48.52300 1.000 79.12000  ? 24   GLU A OE2 1 
ATOM   44    N N   . GLY A 1 6   ? 3.84900   -54.91600 -47.95600 1.000 42.44000  ? 25   GLY A N   1 
ATOM   45    C CA  . GLY A 1 6   ? 3.12600   -55.72100 -48.92900 1.000 42.71000  ? 25   GLY A CA  1 
ATOM   46    C C   . GLY A 1 6   ? 2.44200   -56.94500 -48.35800 1.000 46.07000  ? 25   GLY A C   1 
ATOM   47    O O   . GLY A 1 6   ? 1.81400   -57.69800 -49.11600 1.000 46.96000  ? 25   GLY A O   1 
ATOM   48    N N   . LYS A 1 7   ? 2.53000   -57.15300 -47.04500 1.000 43.47000  ? 26   LYS A N   1 
ATOM   49    C CA  . LYS A 1 7   ? 1.94200   -58.28600 -46.36300 1.000 42.13000  ? 26   LYS A CA  1 
ATOM   50    C C   . LYS A 1 7   ? 1.43400   -57.83300 -45.00400 1.000 42.89000  ? 26   LYS A C   1 
ATOM   51    O O   . LYS A 1 7   ? 1.73900   -56.72900 -44.53300 1.000 40.29000  ? 26   LYS A O   1 
ATOM   52    C CB  . LYS A 1 7   ? 2.95100   -59.44100 -46.26900 1.000 52.17000  ? 26   LYS A CB  1 
ATOM   53    C CG  . LYS A 1 7   ? 4.36500   -58.99400 -45.97900 1.000 52.90000  ? 26   LYS A CG  1 
ATOM   54    C CD  . LYS A 1 7   ? 5.20000   -60.21700 -45.89000 1.000 56.41000  ? 26   LYS A CD  1 
ATOM   55    C CE  . LYS A 1 7   ? 5.13300   -60.85700 -47.24400 1.000 70.68000  ? 26   LYS A CE  1 
ATOM   56    N NZ  . LYS A 1 7   ? 6.24600   -61.77900 -47.60500 1.000 68.96000  ? 26   LYS A NZ  1 
ATOM   57    N N   . LEU A 1 8   ? 0.63300   -58.68400 -44.35700 1.000 41.16000  ? 27   LEU A N   1 
ATOM   58    C CA  . LEU A 1 8   ? 0.03400   -58.34600 -43.07300 1.000 39.40000  ? 27   LEU A CA  1 
ATOM   59    C C   . LEU A 1 8   ? 0.37200   -59.40100 -42.02600 1.000 34.94000  ? 27   LEU A C   1 
ATOM   60    O O   . LEU A 1 8   ? 0.25300   -60.60300 -42.28300 1.000 38.38000  ? 27   LEU A O   1 
ATOM   61    C CB  . LEU A 1 8   ? -1.48300  -58.18000 -43.20100 1.000 38.20000  ? 27   LEU A CB  1 
ATOM   62    C CG  . LEU A 1 8   ? -1.97000  -56.96300 -43.99900 1.000 35.28000  ? 27   LEU A CG  1 
ATOM   63    C CD1 . LEU A 1 8   ? -3.50400  -56.98500 -44.15300 1.000 39.81000  ? 27   LEU A CD1 1 
ATOM   64    C CD2 . LEU A 1 8   ? -1.50900  -55.67800 -43.33000 1.000 28.00000  ? 27   LEU A CD2 1 
ATOM   65    N N   . VAL A 1 9   ? 0.78700   -58.94500 -40.84700 1.000 29.22000  ? 28   VAL A N   1 
ATOM   66    C CA  . VAL A 1 9   ? 0.94800   -59.79700 -39.67700 1.000 35.43000  ? 28   VAL A CA  1 
ATOM   67    C C   . VAL A 1 9   ? -0.06200  -59.33500 -38.64000 1.000 37.85000  ? 28   VAL A C   1 
ATOM   68    O O   . VAL A 1 9   ? -0.14200  -58.13600 -38.33700 1.000 34.93000  ? 28   VAL A O   1 
ATOM   69    C CB  . VAL A 1 9   ? 2.37100   -59.72600 -39.09200 1.000 38.70000  ? 28   VAL A CB  1 
ATOM   70    C CG1 . VAL A 1 9   ? 2.52200   -60.72100 -37.94400 1.000 40.03000  ? 28   VAL A CG1 1 
ATOM   71    C CG2 . VAL A 1 9   ? 3.38700   -59.97100 -40.14800 1.000 36.17000  ? 28   VAL A CG2 1 
ATOM   72    N N   . ILE A 1 10  ? -0.81600  -60.27900 -38.08000 1.000 39.30000  ? 29   ILE A N   1 
ATOM   73    C CA  . ILE A 1 10  ? -1.85400  -59.98200 -37.10200 1.000 34.50000  ? 29   ILE A CA  1 
ATOM   74    C C   . ILE A 1 10  ? -1.54100  -60.71200 -35.80400 1.000 37.67000  ? 29   ILE A C   1 
ATOM   75    O O   . ILE A 1 10  ? -1.26000  -61.91700 -35.81900 1.000 36.42000  ? 29   ILE A O   1 
ATOM   76    C CB  . ILE A 1 10  ? -3.24300  -60.38500 -37.62300 1.000 37.91000  ? 29   ILE A CB  1 
ATOM   77    C CG1 . ILE A 1 10  ? -3.61500  -59.55800 -38.85400 1.000 37.65000  ? 29   ILE A CG1 1 
ATOM   78    C CG2 . ILE A 1 10  ? -4.29100  -60.23800 -36.52900 1.000 32.05000  ? 29   ILE A CG2 1 
ATOM   79    C CD1 . ILE A 1 10  ? -4.89700  -60.03700 -39.52700 1.000 36.32000  ? 29   ILE A CD1 1 
ATOM   80    N N   . TRP A 1 11  ? -1.60800  -59.98500 -34.68400 1.000 35.78000  ? 30   TRP A N   1 
ATOM   81    C CA  . TRP A 1 11  ? -1.56900  -60.57600 -33.35000 1.000 36.83000  ? 30   TRP A CA  1 
ATOM   82    C C   . TRP A 1 11  ? -2.97000  -60.59900 -32.74500 1.000 37.41000  ? 30   TRP A C   1 
ATOM   83    O O   . TRP A 1 11  ? -3.64300  -59.56400 -32.68600 1.000 31.57000  ? 30   TRP A O   1 
ATOM   84    C CB  . TRP A 1 11  ? -0.63700  -59.80900 -32.40800 1.000 36.49000  ? 30   TRP A CB  1 
ATOM   85    C CG  . TRP A 1 11  ? 0.83300   -59.89400 -32.72100 1.000 40.26000  ? 30   TRP A CG  1 
ATOM   86    C CD1 . TRP A 1 11  ? 1.42000   -60.52800 -33.78000 1.000 42.37000  ? 30   TRP A CD1 1 
ATOM   87    C CD2 . TRP A 1 11  ? 1.89900   -59.38000 -31.91900 1.000 33.27000  ? 30   TRP A CD2 1 
ATOM   88    N NE1 . TRP A 1 11  ? 2.78400   -60.40300 -33.70800 1.000 33.20000  ? 30   TRP A NE1 1 
ATOM   89    C CE2 . TRP A 1 11  ? 3.10500   -59.70400 -32.57100 1.000 37.05000  ? 30   TRP A CE2 1 
ATOM   90    C CE3 . TRP A 1 11  ? 1.95000   -58.65500 -30.72300 1.000 35.79000  ? 30   TRP A CE3 1 
ATOM   91    C CZ2 . TRP A 1 11  ? 4.35800   -59.33300 -32.06300 1.000 34.38000  ? 30   TRP A CZ2 1 
ATOM   92    C CZ3 . TRP A 1 11  ? 3.19300   -58.28500 -30.21600 1.000 41.15000  ? 30   TRP A CZ3 1 
ATOM   93    C CH2 . TRP A 1 11  ? 4.37900   -58.62500 -30.88700 1.000 40.50000  ? 30   TRP A CH2 1 
ATOM   94    N N   . ILE A 1 12  ? -3.38700  -61.77400 -32.27000 1.000 37.79000  ? 31   ILE A N   1 
ATOM   95    C CA  . ILE A 1 12  ? -4.66200  -61.96200 -31.58600 1.000 36.21000  ? 31   ILE A CA  1 
ATOM   96    C C   . ILE A 1 12  ? -4.44200  -62.99700 -30.48700 1.000 37.95000  ? 31   ILE A C   1 
ATOM   97    O O   . ILE A 1 12  ? -3.56300  -63.85500 -30.59800 1.000 39.97000  ? 31   ILE A O   1 
ATOM   98    C CB  . ILE A 1 12  ? -5.77100  -62.40500 -32.57700 1.000 35.60000  ? 31   ILE A CB  1 
ATOM   99    C CG1 . ILE A 1 12  ? -7.16300  -62.39700 -31.92800 1.000 35.68000  ? 31   ILE A CG1 1 
ATOM   100   C CG2 . ILE A 1 12  ? -5.45900  -63.76900 -33.15100 1.000 38.45000  ? 31   ILE A CG2 1 
ATOM   101   C CD1 . ILE A 1 12  ? -8.32900  -62.55900 -32.92500 1.000 25.11000  ? 31   ILE A CD1 1 
ATOM   102   N N   . ASN A 1 13  ? -5.23300  -62.91600 -29.41400 1.000 37.14000  ? 32   ASN A N   1 
ATOM   103   C CA  . ASN A 1 13  ? -4.98700  -63.78900 -28.27300 1.000 41.15000  ? 32   ASN A CA  1 
ATOM   104   C C   . ASN A 1 13  ? -5.27800  -65.24100 -28.63700 1.000 41.60000  ? 32   ASN A C   1 
ATOM   105   O O   . ASN A 1 13  ? -6.12500  -65.53900 -29.48100 1.000 37.13000  ? 32   ASN A O   1 
ATOM   106   C CB  . ASN A 1 13  ? -5.84700  -63.41400 -27.06600 1.000 41.03000  ? 32   ASN A CB  1 
ATOM   107   C CG  . ASN A 1 13  ? -5.23400  -63.89100 -25.75500 1.000 46.99000  ? 32   ASN A CG  1 
ATOM   108   O OD1 . ASN A 1 13  ? -4.02700  -64.14100 -25.68200 1.000 52.97000  ? 32   ASN A OD1 1 
ATOM   109   N ND2 . ASN A 1 13  ? -6.06900  -64.11500 -24.75200 1.000 47.62000  ? 32   ASN A ND2 1 
ATOM   110   N N   . GLY A 1 14  ? -4.57800  -66.15300 -27.96200 1.000 47.24000  ? 33   GLY A N   1 
ATOM   111   C CA  . GLY A 1 14  ? -4.72200  -67.56600 -28.25800 1.000 41.23000  ? 33   GLY A CA  1 
ATOM   112   C C   . GLY A 1 14  ? -6.10200  -68.12300 -27.98900 1.000 39.45000  ? 33   GLY A C   1 
ATOM   113   O O   . GLY A 1 14  ? -6.45500  -69.16300 -28.55100 1.000 43.49000  ? 33   GLY A O   1 
ATOM   114   N N   . ASP A 1 15  ? -6.89200  -67.46800 -27.14100 1.000 38.89000  ? 34   ASP A N   1 
ATOM   115   C CA  . ASP A 1 15  ? -8.21600  -67.97700 -26.81600 1.000 42.17000  ? 34   ASP A CA  1 
ATOM   116   C C   . ASP A 1 15  ? -9.29000  -67.49600 -27.79100 1.000 41.64000  ? 34   ASP A C   1 
ATOM   117   O O   . ASP A 1 15  ? -10.47500 -67.75300 -27.56100 1.000 41.73000  ? 34   ASP A O   1 
ATOM   118   C CB  . ASP A 1 15  ? -8.60000  -67.60000 -25.37400 1.000 45.72000  ? 34   ASP A CB  1 
ATOM   119   C CG  . ASP A 1 15  ? -8.80900  -66.10000 -25.17600 1.000 51.86000  ? 34   ASP A CG  1 
ATOM   120   O OD1 . ASP A 1 15  ? -8.57900  -65.30000 -26.11300 1.000 54.40000  ? 34   ASP A OD1 1 
ATOM   121   O OD2 . ASP A 1 15  ? -9.23700  -65.71600 -24.06900 1.000 52.11000  ? 34   ASP A OD2 1 
ATOM   122   N N   . LYS A 1 16  ? -8.90500  -66.79400 -28.85400 1.000 42.50000  ? 35   LYS A N   1 
ATOM   123   C CA  . LYS A 1 16  ? -9.82300  -66.29600 -29.86900 1.000 44.58000  ? 35   LYS A CA  1 
ATOM   124   C C   . LYS A 1 16  ? -9.77900  -67.18600 -31.11200 1.000 43.60000  ? 35   LYS A C   1 
ATOM   125   O O   . LYS A 1 16  ? -8.92400  -68.06100 -31.25400 1.000 43.30000  ? 35   LYS A O   1 
ATOM   126   C CB  . LYS A 1 16  ? -9.47700  -64.84500 -30.22800 1.000 38.56000  ? 35   LYS A CB  1 
ATOM   127   C CG  . LYS A 1 16  ? -9.54300  -63.86300 -29.05000 1.000 45.12000  ? 35   LYS A CG  1 
ATOM   128   C CD  . LYS A 1 16  ? -10.98400 -63.58300 -28.61500 1.000 39.39000  ? 35   LYS A CD  1 
ATOM   129   C CE  . LYS A 1 16  ? -11.08400 -62.46000 -27.56000 1.000 42.44000  ? 35   LYS A CE  1 
ATOM   130   N NZ  . LYS A 1 16  ? -10.69500 -62.85500 -26.17800 1.000 53.95000  ? 35   LYS A NZ  1 
ATOM   131   N N   . GLY A 1 17  ? -10.72400 -66.95100 -32.02100 1.000 41.97000  ? 36   GLY A N   1 
ATOM   132   C CA  . GLY A 1 17  ? -10.86600 -67.76600 -33.22000 1.000 46.09000  ? 36   GLY A CA  1 
ATOM   133   C C   . GLY A 1 17  ? -9.87500  -67.43500 -34.31700 1.000 43.21000  ? 36   GLY A C   1 
ATOM   134   O O   . GLY A 1 17  ? -10.24100 -66.94300 -35.39200 1.000 46.17000  ? 36   GLY A O   1 
ATOM   135   N N   . TYR A 1 18  ? -8.59200  -67.61900 -33.98900 1.000 40.14000  ? 37   TYR A N   1 
ATOM   136   C CA  . TYR A 1 18  ? -7.43300  -67.30300 -34.86600 1.000 36.43000  ? 37   TYR A CA  1 
ATOM   137   C C   . TYR A 1 18  ? -7.45100  -68.12700 -36.15200 1.000 37.52000  ? 37   TYR A C   1 
ATOM   138   O O   . TYR A 1 18  ? -7.10500  -67.60200 -37.17900 1.000 38.64000  ? 37   TYR A O   1 
ATOM   139   C CB  . TYR A 1 18  ? -6.10700  -67.30300 -34.10300 1.000 39.19000  ? 37   TYR A CB  1 
ATOM   140   C CG  . TYR A 1 18  ? -5.69100  -68.56800 -33.40500 1.000 42.14000  ? 37   TYR A CG  1 
ATOM   141   C CD1 . TYR A 1 18  ? -5.23700  -69.66500 -34.10500 1.000 47.81000  ? 37   TYR A CD1 1 
ATOM   142   C CD2 . TYR A 1 18  ? -5.67800  -68.64300 -32.03100 1.000 41.92000  ? 37   TYR A CD2 1 
ATOM   143   C CE1 . TYR A 1 18  ? -4.84500  -70.82400 -33.46700 1.000 42.43000  ? 37   TYR A CE1 1 
ATOM   144   C CE2 . TYR A 1 18  ? -5.28500  -69.78900 -31.37200 1.000 49.78000  ? 37   TYR A CE2 1 
ATOM   145   C CZ  . TYR A 1 18  ? -4.86200  -70.88400 -32.09200 1.000 52.19000  ? 37   TYR A CZ  1 
ATOM   146   O OH  . TYR A 1 18  ? -4.46800  -72.01200 -31.44500 1.000 52.94000  ? 37   TYR A OH  1 
ATOM   147   N N   . ASN A 1 19  ? -7.80200  -69.39900 -36.06000 1.000 39.21000  ? 38   ASN A N   1 
ATOM   148   C CA  . ASN A 1 19  ? -7.94300  -70.22800 -37.25000 1.000 40.39000  ? 38   ASN A CA  1 
ATOM   149   C C   . ASN A 1 19  ? -8.97800  -69.63300 -38.19500 1.000 45.94000  ? 38   ASN A C   1 
ATOM   150   O O   . ASN A 1 19  ? -8.75100  -69.53300 -39.40700 1.000 40.92000  ? 38   ASN A O   1 
ATOM   151   C CB  . ASN A 1 19  ? -8.36500  -71.63500 -36.83300 1.000 43.08000  ? 38   ASN A CB  1 
ATOM   152   C CG  . ASN A 1 19  ? -7.36800  -72.30300 -35.89700 1.000 46.51000  ? 38   ASN A CG  1 
ATOM   153   O OD1 . ASN A 1 19  ? -6.17400  -72.37300 -36.18300 1.000 41.09000  ? 38   ASN A OD1 1 
ATOM   154   N ND2 . ASN A 1 19  ? -7.85600  -72.74900 -34.74000 1.000 45.80000  ? 38   ASN A ND2 1 
ATOM   155   N N   . GLY A 1 20  ? -10.13400 -69.23300 -37.64600 1.000 44.27000  ? 39   GLY A N   1 
ATOM   156   C CA  . GLY A 1 20  ? -11.14800 -68.57200 -38.45300 1.000 35.21000  ? 39   GLY A CA  1 
ATOM   157   C C   . GLY A 1 20  ? -10.65000 -67.26800 -39.04300 1.000 38.00000  ? 39   GLY A C   1 
ATOM   158   O O   . GLY A 1 20  ? -10.93600 -66.94600 -40.20000 1.000 42.34000  ? 39   GLY A O   1 
ATOM   159   N N   . LEU A 1 21  ? -9.89500  -66.49900 -38.25800 1.000 38.21000  ? 40   LEU A N   1 
ATOM   160   C CA  . LEU A 1 21  ? -9.27900  -65.29200 -38.79400 1.000 36.60000  ? 40   LEU A CA  1 
ATOM   161   C C   . LEU A 1 21  ? -8.25300  -65.62600 -39.87200 1.000 43.31000  ? 40   LEU A C   1 
ATOM   162   O O   . LEU A 1 21  ? -8.03700  -64.83200 -40.79700 1.000 39.48000  ? 40   LEU A O   1 
ATOM   163   C CB  . LEU A 1 21  ? -8.62800  -64.49600 -37.66300 1.000 35.13000  ? 40   LEU A CB  1 
ATOM   164   C CG  . LEU A 1 21  ? -8.13100  -63.10400 -38.04700 1.000 40.89000  ? 40   LEU A CG  1 
ATOM   165   C CD1 . LEU A 1 21  ? -9.32200  -62.25200 -38.48300 1.000 36.14000  ? 40   LEU A CD1 1 
ATOM   166   C CD2 . LEU A 1 21  ? -7.36200  -62.41400 -36.91700 1.000 28.38000  ? 40   LEU A CD2 1 
ATOM   167   N N   . ALA A 1 22  ? -7.59900  -66.78500 -39.76600 1.000 38.59000  ? 41   ALA A N   1 
ATOM   168   C CA  . ALA A 1 22  ? -6.64900  -67.17900 -40.79900 1.000 40.05000  ? 41   ALA A CA  1 
ATOM   169   C C   . ALA A 1 22  ? -7.35800  -67.42300 -42.12500 1.000 43.42000  ? 41   ALA A C   1 
ATOM   170   O O   . ALA A 1 22  ? -6.84500  -67.05000 -43.18500 1.000 45.31000  ? 41   ALA A O   1 
ATOM   171   C CB  . ALA A 1 22  ? -5.87100  -68.42000 -40.36100 1.000 39.70000  ? 41   ALA A CB  1 
ATOM   172   N N   . GLU A 1 23  ? -8.54800  -68.03700 -42.08100 1.000 41.38000  ? 42   GLU A N   1 
ATOM   173   C CA  . GLU A 1 23  ? -9.33400  -68.24300 -43.29500 1.000 38.69000  ? 42   GLU A CA  1 
ATOM   174   C C   . GLU A 1 23  ? -9.67600  -66.91500 -43.94300 1.000 41.08000  ? 42   GLU A C   1 
ATOM   175   O O   . GLU A 1 23  ? -9.59700  -66.77900 -45.16800 1.000 41.82000  ? 42   GLU A O   1 
ATOM   176   C CB  . GLU A 1 23  ? -10.63000 -68.98400 -42.98800 1.000 46.56000  ? 42   GLU A CB  1 
ATOM   177   C CG  . GLU A 1 23  ? -10.44300 -70.30400 -42.29500 1.000 50.98000  ? 42   GLU A CG  1 
ATOM   178   C CD  . GLU A 1 23  ? -11.72800 -71.06900 -42.09800 1.000 63.81000  ? 42   GLU A CD  1 
ATOM   179   O OE1 . GLU A 1 23  ? -12.81000 -70.52400 -42.44000 1.000 58.74000  ? 42   GLU A OE1 1 
ATOM   180   O OE2 . GLU A 1 23  ? -11.65000 -72.22300 -41.60400 1.000 65.60000  ? 42   GLU A OE2 1 
ATOM   181   N N   . VAL A 1 24  ? -10.05200 -65.92600 -43.13300 1.000 39.70000  ? 43   VAL A N   1 
ATOM   182   C CA  . VAL A 1 24  ? -10.34500 -64.60300 -43.66200 1.000 40.32000  ? 43   VAL A CA  1 
ATOM   183   C C   . VAL A 1 24  ? -9.10600  -64.00600 -44.31800 1.000 41.26000  ? 43   VAL A C   1 
ATOM   184   O O   . VAL A 1 24  ? -9.20500  -63.30200 -45.32900 1.000 41.70000  ? 43   VAL A O   1 
ATOM   185   C CB  . VAL A 1 24  ? -10.89100 -63.70600 -42.53300 1.000 36.01000  ? 43   VAL A CB  1 
ATOM   186   C CG1 . VAL A 1 24  ? -11.21100 -62.31500 -43.04900 1.000 33.83000  ? 43   VAL A CG1 1 
ATOM   187   C CG2 . VAL A 1 24  ? -12.12200 -64.34500 -41.89600 1.000 37.05000  ? 43   VAL A CG2 1 
ATOM   188   N N   . GLY A 1 25  ? -7.92500  -64.26600 -43.75700 1.000 39.95000  ? 44   GLY A N   1 
ATOM   189   C CA  . GLY A 1 25  ? -6.70300  -63.78100 -44.37900 1.000 43.26000  ? 44   GLY A CA  1 
ATOM   190   C C   . GLY A 1 25  ? -6.40900  -64.48300 -45.69100 1.000 47.20000  ? 44   GLY A C   1 
ATOM   191   O O   . GLY A 1 25  ? -5.83900  -63.88900 -46.61400 1.000 41.84000  ? 44   GLY A O   1 
ATOM   192   N N   . LYS A 1 26  ? -6.78800  -65.76100 -45.78900 1.000 45.11000  ? 45   LYS A N   1 
ATOM   193   C CA  . LYS A 1 26  ? -6.57900  -66.51000 -47.02500 1.000 43.83000  ? 45   LYS A CA  1 
ATOM   194   C C   . LYS A 1 26  ? -7.49400  -66.02700 -48.15300 1.000 41.07000  ? 45   LYS A C   1 
ATOM   195   O O   . LYS A 1 26  ? -7.04200  -65.88600 -49.29100 1.000 45.10000  ? 45   LYS A O   1 
ATOM   196   C CB  . LYS A 1 26  ? -6.71000  -68.01600 -46.74100 1.000 42.38000  ? 45   LYS A CB  1 
ATOM   197   C CG  . LYS A 1 26  ? -5.33900  -68.67200 -46.43800 1.000 48.45000  ? 45   LYS A CG  1 
ATOM   198   C CD  . LYS A 1 26  ? -5.42600  -70.02400 -45.71600 1.000 57.53000  ? 45   LYS A CD  1 
ATOM   199   C CE  . LYS A 1 26  ? -5.46800  -69.90300 -44.13500 1.000 69.29000  ? 45   LYS A CE  1 
ATOM   200   N NZ  . LYS A 1 26  ? -5.58400  -71.29500 -43.51200 1.000 62.40000  ? 45   LYS A NZ  1 
ATOM   201   N N   . LYS A 1 27  ? -8.75500  -65.70600 -47.85300 1.000 43.10000  ? 46   LYS A N   1 
ATOM   202   C CA  . LYS A 1 27  ? -9.63500  -65.05400 -48.82300 1.000 37.83000  ? 46   LYS A CA  1 
ATOM   203   C C   . LYS A 1 27  ? -9.08000  -63.68600 -49.25200 1.000 44.53000  ? 46   LYS A C   1 
ATOM   204   O O   . LYS A 1 27  ? -9.20800  -63.26900 -50.41600 1.000 48.31000  ? 46   LYS A O   1 
ATOM   205   C CB  . LYS A 1 27  ? -11.03000 -64.95600 -48.17800 1.000 41.61000  ? 46   LYS A CB  1 
ATOM   206   C CG  . LYS A 1 27  ? -12.16700 -64.34000 -49.02100 1.000 47.93000  ? 46   LYS A CG  1 
ATOM   207   C CD  . LYS A 1 27  ? -13.55300 -64.54700 -48.41900 1.000 61.39000  ? 46   LYS A CD  1 
ATOM   208   C CE  . LYS A 1 27  ? -14.54200 -63.90200 -49.27200 1.000 68.74000  ? 46   LYS A CE  1 
ATOM   209   N NZ  . LYS A 1 27  ? -14.84900 -64.89300 -50.23800 1.000 66.00000  ? 46   LYS A NZ  1 
ATOM   210   N N   . PHE A 1 28  ? -8.45100  -62.97800 -48.31900 1.000 42.71000  ? 47   PHE A N   1 
ATOM   211   C CA  . PHE A 1 28  ? -7.84400  -61.69800 -48.65200 1.000 39.35000  ? 47   PHE A CA  1 
ATOM   212   C C   . PHE A 1 28  ? -6.65700  -61.89700 -49.57900 1.000 44.27000  ? 47   PHE A C   1 
ATOM   213   O O   . PHE A 1 28  ? -6.41900  -61.08700 -50.48100 1.000 46.52000  ? 47   PHE A O   1 
ATOM   214   C CB  . PHE A 1 28  ? -7.44000  -60.97700 -47.37100 1.000 35.29000  ? 47   PHE A CB  1 
ATOM   215   C CG  . PHE A 1 28  ? -6.96700  -59.57200 -47.59300 1.000 36.59000  ? 47   PHE A CG  1 
ATOM   216   C CD1 . PHE A 1 28  ? -7.86300  -58.57900 -47.96100 1.000 38.02000  ? 47   PHE A CD1 1 
ATOM   217   C CD2 . PHE A 1 28  ? -5.64300  -59.23100 -47.39800 1.000 38.73000  ? 47   PHE A CD2 1 
ATOM   218   C CE1 . PHE A 1 28  ? -7.44000  -57.27200 -48.15500 1.000 39.35000  ? 47   PHE A CE1 1 
ATOM   219   C CE2 . PHE A 1 28  ? -5.21100  -57.91800 -47.59000 1.000 40.58000  ? 47   PHE A CE2 1 
ATOM   220   C CZ  . PHE A 1 28  ? -6.11200  -56.94100 -47.97200 1.000 36.64000  ? 47   PHE A CZ  1 
ATOM   221   N N   . GLU A 1 29  ? -5.90700  -62.97500 -49.37700 1.000 43.60000  ? 48   GLU A N   1 
ATOM   222   C CA  . GLU A 1 29  ? -4.80400  -63.27700 -50.27500 1.000 50.92000  ? 48   GLU A CA  1 
ATOM   223   C C   . GLU A 1 29  ? -5.32100  -63.64800 -51.65400 1.000 48.09000  ? 48   GLU A C   1 
ATOM   224   O O   . GLU A 1 29  ? -4.85500  -63.12900 -52.67300 1.000 48.51000  ? 48   GLU A O   1 
ATOM   225   C CB  . GLU A 1 29  ? -4.00100  -64.43500 -49.71900 1.000 55.41000  ? 48   GLU A CB  1 
ATOM   226   C CG  . GLU A 1 29  ? -2.60700  -64.50300 -50.26500 1.000 54.94000  ? 48   GLU A CG  1 
ATOM   227   C CD  . GLU A 1 29  ? -1.90100  -65.76600 -49.84100 1.000 67.30000  ? 48   GLU A CD  1 
ATOM   228   O OE1 . GLU A 1 29  ? -2.60500  -66.79400 -49.69800 1.000 62.93000  ? 48   GLU A OE1 1 
ATOM   229   O OE2 . GLU A 1 29  ? -0.68300  -65.68600 -49.51400 1.000 77.19000  ? 48   GLU A OE2 1 
ATOM   230   N N   . LYS A 1 30  ? -6.27500  -64.57400 -51.69400 1.000 45.68000  ? 49   LYS A N   1 
ATOM   231   C CA  . LYS A 1 30  ? -6.77800  -65.06800 -52.96400 1.000 47.09000  ? 49   LYS A CA  1 
ATOM   232   C C   . LYS A 1 30  ? -7.38000  -63.93700 -53.78100 1.000 53.52000  ? 49   LYS A C   1 
ATOM   233   O O   . LYS A 1 30  ? -7.27600  -63.93000 -55.01100 1.000 62.22000  ? 49   LYS A O   1 
ATOM   234   C CB  . LYS A 1 30  ? -7.81300  -66.16900 -52.72600 1.000 49.51000  ? 49   LYS A CB  1 
ATOM   235   C CG  . LYS A 1 30  ? -8.21300  -66.91500 -53.98800 1.000 61.24000  ? 49   LYS A CG  1 
ATOM   236   C CD  . LYS A 1 30  ? -9.26900  -67.98500 -53.71500 1.000 68.73000  ? 49   LYS A CD  1 
ATOM   237   C CE  . LYS A 1 30  ? -10.68500 -67.39700 -53.67100 1.000 67.44000  ? 49   LYS A CE  1 
ATOM   238   N NZ  . LYS A 1 30  ? -11.16500 -67.00100 -55.03900 1.000 65.60000  ? 49   LYS A NZ  1 
ATOM   239   N N   . ASP A 1 31  ? -8.00700  -62.96200 -53.12100 1.000 50.96000  ? 50   ASP A N   1 
ATOM   240   C CA  . ASP A 1 31  ? -8.59500  -61.86200 -53.87400 1.000 48.76000  ? 50   ASP A CA  1 
ATOM   241   C C   . ASP A 1 31  ? -7.58700  -60.76700 -54.21300 1.000 45.48000  ? 50   ASP A C   1 
ATOM   242   O O   . ASP A 1 31  ? -7.74000  -60.09700 -55.23600 1.000 41.61000  ? 50   ASP A O   1 
ATOM   243   C CB  . ASP A 1 31  ? -9.76800  -61.23500 -53.11200 1.000 46.55000  ? 50   ASP A CB  1 
ATOM   244   C CG  . ASP A 1 31  ? -10.96000 -62.17500 -52.97200 1.000 59.42000  ? 50   ASP A CG  1 
ATOM   245   O OD1 . ASP A 1 31  ? -11.03500 -63.17400 -53.72700 1.000 57.11000  ? 50   ASP A OD1 1 
ATOM   246   O OD2 . ASP A 1 31  ? -11.85600 -61.87700 -52.14600 1.000 52.46000  ? 50   ASP A OD2 1 
ATOM   247   N N   . THR A 1 32  ? -6.57300  -60.54400 -53.37700 1.000 41.36000  ? 51   THR A N   1 
ATOM   248   C CA  . THR A 1 32  ? -5.71000  -59.38100 -53.54600 1.000 43.61000  ? 51   THR A CA  1 
ATOM   249   C C   . THR A 1 32  ? -4.22600  -59.69800 -53.64900 1.000 44.17000  ? 51   THR A C   1 
ATOM   250   O O   . THR A 1 32  ? -3.44800  -58.79800 -53.97800 1.000 49.34000  ? 51   THR A O   1 
ATOM   251   C CB  . THR A 1 32  ? -5.90100  -58.38600 -52.38700 1.000 44.25000  ? 51   THR A CB  1 
ATOM   252   O OG1 . THR A 1 32  ? -5.49700  -58.99700 -51.15200 1.000 41.05000  ? 51   THR A OG1 1 
ATOM   253   C CG2 . THR A 1 32  ? -7.35700  -57.93300 -52.29100 1.000 42.07000  ? 51   THR A CG2 1 
ATOM   254   N N   . GLY A 1 33  ? -3.80600  -60.92400 -53.35300 1.000 47.28000  ? 52   GLY A N   1 
ATOM   255   C CA  . GLY A 1 33  ? -2.40500  -61.27300 -53.38400 1.000 41.73000  ? 52   GLY A CA  1 
ATOM   256   C C   . GLY A 1 33  ? -1.62600  -60.96200 -52.12400 1.000 48.77000  ? 52   GLY A C   1 
ATOM   257   O O   . GLY A 1 33  ? -0.45200  -61.35300 -52.03100 1.000 54.05000  ? 52   GLY A O   1 
ATOM   258   N N   . ILE A 1 34  ? -2.23100  -60.29600 -51.14400 1.000 46.48000  ? 53   ILE A N   1 
ATOM   259   C CA  . ILE A 1 34  ? -1.52500  -59.91100 -49.92400 1.000 51.36000  ? 53   ILE A CA  1 
ATOM   260   C C   . ILE A 1 34  ? -1.57200  -61.06600 -48.93000 1.000 53.33000  ? 53   ILE A C   1 
ATOM   261   O O   . ILE A 1 34  ? -2.64900  -61.48000 -48.48400 1.000 49.59000  ? 53   ILE A O   1 
ATOM   262   C CB  . ILE A 1 34  ? -2.11800  -58.63300 -49.31100 1.000 48.56000  ? 53   ILE A CB  1 
ATOM   263   C CG1 . ILE A 1 34  ? -1.77300  -57.41600 -50.17500 1.000 47.55000  ? 53   ILE A CG1 1 
ATOM   264   C CG2 . ILE A 1 34  ? -1.62800  -58.43800 -47.87600 1.000 43.73000  ? 53   ILE A CG2 1 
ATOM   265   C CD1 . ILE A 1 34  ? -2.79300  -57.09400 -51.22300 1.000 50.04000  ? 53   ILE A CD1 1 
ATOM   266   N N   . LYS A 1 35  ? -0.39800  -61.57500 -48.57400 1.000 53.49000  ? 54   LYS A N   1 
ATOM   267   C CA  . LYS A 1 35  ? -0.30700  -62.63200 -47.58600 1.000 53.58000  ? 54   LYS A CA  1 
ATOM   268   C C   . LYS A 1 35  ? -0.69100  -62.08500 -46.22100 1.000 46.62000  ? 54   LYS A C   1 
ATOM   269   O O   . LYS A 1 35  ? -0.32000  -60.96700 -45.84700 1.000 50.91000  ? 54   LYS A O   1 
ATOM   270   C CB  . LYS A 1 35  ? 1.10500   -63.20300 -47.57300 1.000 52.32000  ? 54   LYS A CB  1 
ATOM   271   C CG  . LYS A 1 35  ? 1.55100   -63.66100 -48.97100 1.000 77.34000  ? 54   LYS A CG  1 
ATOM   272   C CD  . LYS A 1 35  ? 2.94800   -64.28800 -49.03700 1.000 93.13000  ? 54   LYS A CD  1 
ATOM   273   C CE  . LYS A 1 35  ? 3.26000   -64.76300 -50.47100 1.000 100.60000 ? 54   LYS A CE  1 
ATOM   274   N NZ  . LYS A 1 35  ? 3.11800   -63.68500 -51.50500 1.000 103.68000 ? 54   LYS A NZ  1 
ATOM   275   N N   . VAL A 1 36  ? -1.45600  -62.87400 -45.48000 1.000 40.98000  ? 55   VAL A N   1 
ATOM   276   C CA  . VAL A 1 36  ? -1.87500  -62.50500 -44.13600 1.000 45.83000  ? 55   VAL A CA  1 
ATOM   277   C C   . VAL A 1 36  ? -1.40900  -63.61600 -43.21000 1.000 42.50000  ? 55   VAL A C   1 
ATOM   278   O O   . VAL A 1 36  ? -1.71300  -64.79200 -43.43800 1.000 45.10000  ? 55   VAL A O   1 
ATOM   279   C CB  . VAL A 1 36  ? -3.39400  -62.29400 -44.04100 1.000 43.67000  ? 55   VAL A CB  1 
ATOM   280   C CG1 . VAL A 1 36  ? -3.75500  -61.78600 -42.66100 1.000 50.02000  ? 55   VAL A CG1 1 
ATOM   281   C CG2 . VAL A 1 36  ? -3.86100  -61.34000 -45.13200 1.000 41.49000  ? 55   VAL A CG2 1 
ATOM   282   N N   . THR A 1 37  ? -0.64600  -63.24500 -42.19000 1.000 40.48000  ? 56   THR A N   1 
ATOM   283   C CA  . THR A 1 37  ? -0.08700  -64.17100 -41.21900 1.000 42.05000  ? 56   THR A CA  1 
ATOM   284   C C   . THR A 1 37  ? -0.70600  -63.88200 -39.85900 1.000 38.24000  ? 56   THR A C   1 
ATOM   285   O O   . THR A 1 37  ? -0.53600  -62.78300 -39.32100 1.000 40.93000  ? 56   THR A O   1 
ATOM   286   C CB  . THR A 1 37  ? 1.43500   -64.01500 -41.15900 1.000 42.99000  ? 56   THR A CB  1 
ATOM   287   O OG1 . THR A 1 37  ? 1.99100   -64.27900 -42.45200 1.000 47.21000  ? 56   THR A OG1 1 
ATOM   288   C CG2 . THR A 1 37  ? 2.04800   -64.95900 -40.12200 1.000 41.97000  ? 56   THR A CG2 1 
ATOM   289   N N   . VAL A 1 38  ? -1.38700  -64.86600 -39.28700 1.000 39.36000  ? 57   VAL A N   1 
ATOM   290   C CA  . VAL A 1 38  ? -2.08000  -64.68500 -38.01600 1.000 38.83000  ? 57   VAL A CA  1 
ATOM   291   C C   . VAL A 1 38  ? -1.27000  -65.36800 -36.92400 1.000 42.40000  ? 57   VAL A C   1 
ATOM   292   O O   . VAL A 1 38  ? -1.06800  -66.58800 -36.95700 1.000 39.83000  ? 57   VAL A O   1 
ATOM   293   C CB  . VAL A 1 38  ? -3.51100  -65.24000 -38.07500 1.000 40.51000  ? 57   VAL A CB  1 
ATOM   294   C CG1 . VAL A 1 38  ? -4.19900  -65.06300 -36.72600 1.000 37.72000  ? 57   VAL A CG1 1 
ATOM   295   C CG2 . VAL A 1 38  ? -4.29700  -64.56400 -39.17300 1.000 36.59000  ? 57   VAL A CG2 1 
ATOM   296   N N   . GLU A 1 39  ? -0.81300  -64.58700 -35.95000 1.000 39.08000  ? 58   GLU A N   1 
ATOM   297   C CA  . GLU A 1 39  ? -0.01400  -65.10200 -34.84900 1.000 44.05000  ? 58   GLU A CA  1 
ATOM   298   C C   . GLU A 1 39  ? -0.73800  -64.85300 -33.53600 1.000 45.05000  ? 58   GLU A C   1 
ATOM   299   O O   . GLU A 1 39  ? -1.46400  -63.86400 -33.38700 1.000 44.21000  ? 58   GLU A O   1 
ATOM   300   C CB  . GLU A 1 39  ? 1.37400   -64.44900 -34.79200 1.000 38.81000  ? 58   GLU A CB  1 
ATOM   301   C CG  . GLU A 1 39  ? 2.21800   -64.66800 -36.03500 1.000 47.86000  ? 58   GLU A CG  1 
ATOM   302   C CD  . GLU A 1 39  ? 3.61700   -64.08900 -35.90500 1.000 52.98000  ? 58   GLU A CD  1 
ATOM   303   O OE1 . GLU A 1 39  ? 3.91500   -63.45900 -34.86100 1.000 49.96000  ? 58   GLU A OE1 1 
ATOM   304   O OE2 . GLU A 1 39  ? 4.41100   -64.25700 -36.85600 1.000 48.54000  ? 58   GLU A OE2 1 
ATOM   305   N N   . HIS A 1 40  ? -0.52200  -65.74600 -32.57300 1.000 42.49000  ? 59   HIS A N   1 
ATOM   306   C CA  . HIS A 1 40  ? -1.06400  -65.58600 -31.22700 1.000 39.92000  ? 59   HIS A CA  1 
ATOM   307   C C   . HIS A 1 40  ? 0.06000   -65.72500 -30.21000 1.000 42.93000  ? 59   HIS A C   1 
ATOM   308   O O   . HIS A 1 40  ? 0.13100   -66.70200 -29.45900 1.000 42.22000  ? 59   HIS A O   1 
ATOM   309   C CB  . HIS A 1 40  ? -2.22100  -66.55800 -30.98200 1.000 37.37000  ? 59   HIS A CB  1 
ATOM   310   C CG  . HIS A 1 40  ? -1.92600  -67.98300 -31.33000 1.000 39.85000  ? 59   HIS A CG  1 
ATOM   311   N ND1 . HIS A 1 40  ? -1.49900  -68.90700 -30.40100 1.000 47.67000  ? 59   HIS A ND1 1 
ATOM   312   C CD2 . HIS A 1 40  ? -2.01300  -68.64500 -32.50700 1.000 41.10000  ? 59   HIS A CD2 1 
ATOM   313   C CE1 . HIS A 1 40  ? -1.33600  -70.07800 -30.99200 1.000 46.50000  ? 59   HIS A CE1 1 
ATOM   314   N NE2 . HIS A 1 40  ? -1.63800  -69.94500 -32.27000 1.000 45.35000  ? 59   HIS A NE2 1 
ATOM   315   N N   . PRO A 1 41  ? 0.94200   -64.72700 -30.14300 1.000 40.24000  ? 60   PRO A N   1 
ATOM   316   C CA  . PRO A 1 41  ? 2.06900   -64.79000 -29.21200 1.000 41.53000  ? 60   PRO A CA  1 
ATOM   317   C C   . PRO A 1 41  ? 1.62200   -64.80200 -27.75800 1.000 45.64000  ? 60   PRO A C   1 
ATOM   318   O O   . PRO A 1 41  ? 0.57700   -64.25800 -27.39400 1.000 43.98000  ? 60   PRO A O   1 
ATOM   319   C CB  . PRO A 1 41  ? 2.85300   -63.51000 -29.52200 1.000 36.40000  ? 60   PRO A CB  1 
ATOM   320   C CG  . PRO A 1 41  ? 2.39300   -63.09100 -30.87300 1.000 41.60000  ? 60   PRO A CG  1 
ATOM   321   C CD  . PRO A 1 41  ? 0.97400   -63.50600 -30.96200 1.000 36.40000  ? 60   PRO A CD  1 
ATOM   322   N N   . ASP A 1 42  ? 2.44700   -65.42500 -26.92000 1.000 50.05000  ? 61   ASP A N   1 
ATOM   323   C CA  . ASP A 1 42  ? 2.29700   -65.29200 -25.47900 1.000 51.04000  ? 61   ASP A CA  1 
ATOM   324   C C   . ASP A 1 42  ? 2.53700   -63.84500 -25.06800 1.000 46.15000  ? 61   ASP A C   1 
ATOM   325   O O   . ASP A 1 42  ? 3.40500   -63.17300 -25.62100 1.000 45.73000  ? 61   ASP A O   1 
ATOM   326   C CB  . ASP A 1 42  ? 3.29500   -66.20500 -24.76300 1.000 50.29000  ? 61   ASP A CB  1 
ATOM   327   C CG  . ASP A 1 42  ? 2.92800   -67.66600 -24.85800 1.000 60.92000  ? 61   ASP A CG  1 
ATOM   328   O OD1 . ASP A 1 42  ? 1.72800   -67.97900 -24.69300 1.000 61.28000  ? 61   ASP A OD1 1 
ATOM   329   O OD2 . ASP A 1 42  ? 3.82200   -68.49400 -25.14900 1.000 62.81000  ? 61   ASP A OD2 1 
ATOM   330   N N   . LYS A 1 43  ? 1.75400   -63.36600 -24.09400 1.000 41.73000  ? 62   LYS A N   1 
ATOM   331   C CA  . LYS A 1 43  ? 1.95900   -62.04900 -23.47900 1.000 51.86000  ? 62   LYS A CA  1 
ATOM   332   C C   . LYS A 1 43  ? 2.04100   -60.96100 -24.54300 1.000 51.32000  ? 62   LYS A C   1 
ATOM   333   O O   . LYS A 1 43  ? 2.91800   -60.08900 -24.51100 1.000 51.89000  ? 62   LYS A O   1 
ATOM   334   C CB  . LYS A 1 43  ? 3.22300   -62.03300 -22.59400 1.000 52.78000  ? 62   LYS A CB  1 
ATOM   335   C CG  . LYS A 1 43  ? 3.05400   -62.34700 -21.11900 1.000 62.99000  ? 62   LYS A CG  1 
ATOM   336   C CD  . LYS A 1 43  ? 4.30100   -62.95300 -20.58100 1.000 87.35000  ? 62   LYS A CD  1 
ATOM   337   C CE  . LYS A 1 43  ? 5.36300   -61.95000 -20.52000 1.000 92.93000  ? 62   LYS A CE  1 
ATOM   338   N NZ  . LYS A 1 43  ? 6.56800   -62.24300 -19.68200 1.000 100.43000 ? 62   LYS A NZ  1 
ATOM   339   N N   . LEU A 1 44  ? 1.11200   -61.02700 -25.50900 1.000 44.05000  ? 63   LEU A N   1 
ATOM   340   C CA  . LEU A 1 44  ? 1.19400   -60.13200 -26.66100 1.000 42.64000  ? 63   LEU A CA  1 
ATOM   341   C C   . LEU A 1 44  ? 0.79300   -58.71100 -26.29900 1.000 40.43000  ? 63   LEU A C   1 
ATOM   342   O O   . LEU A 1 44  ? 1.26100   -57.76400 -26.93700 1.000 40.12000  ? 63   LEU A O   1 
ATOM   343   C CB  . LEU A 1 44  ? 0.31500   -60.64300 -27.82000 1.000 39.06000  ? 63   LEU A CB  1 
ATOM   344   C CG  . LEU A 1 44  ? -1.20900  -60.60400 -27.81800 1.000 39.68000  ? 63   LEU A CG  1 
ATOM   345   C CD1 . LEU A 1 44  ? -1.71300  -59.26100 -28.33700 1.000 30.11000  ? 63   LEU A CD1 1 
ATOM   346   C CD2 . LEU A 1 44  ? -1.75000  -61.74000 -28.66700 1.000 35.64000  ? 63   LEU A CD2 1 
ATOM   347   N N   . GLU A 1 45  ? -0.05100  -58.53400 -25.28100 1.000 42.45000  ? 64   GLU A N   1 
ATOM   348   C CA  . GLU A 1 45  ? -0.44300  -57.18000 -24.91400 1.000 41.41000  ? 64   GLU A CA  1 
ATOM   349   C C   . GLU A 1 45  ? 0.67200   -56.43700 -24.18900 1.000 41.99000  ? 64   GLU A C   1 
ATOM   350   O O   . GLU A 1 45  ? 0.66700   -55.20300 -24.16500 1.000 38.69000  ? 64   GLU A O   1 
ATOM   351   C CB  . GLU A 1 45  ? -1.71300  -57.17600 -24.05000 1.000 47.34000  ? 64   GLU A CB  1 
ATOM   352   C CG  . GLU A 1 45  ? -1.53100  -57.51200 -22.56300 1.000 44.24000  ? 64   GLU A CG  1 
ATOM   353   C CD  . GLU A 1 45  ? -1.54600  -59.00000 -22.27300 1.000 47.77000  ? 64   GLU A CD  1 
ATOM   354   O OE1 . GLU A 1 45  ? -1.32000  -59.79100 -23.21100 1.000 46.98000  ? 64   GLU A OE1 1 
ATOM   355   O OE2 . GLU A 1 45  ? -1.80300  -59.38000 -21.10700 1.000 48.28000  ? 64   GLU A OE2 1 
ATOM   356   N N   . GLU A 1 46  ? 1.62200   -57.14600 -23.58900 1.000 46.56000  ? 65   GLU A N   1 
ATOM   357   C CA  . GLU A 1 46  ? 2.76400   -56.45300 -23.00100 1.000 55.70000  ? 65   GLU A CA  1 
ATOM   358   C C   . GLU A 1 46  ? 3.95900   -56.40000 -23.94100 1.000 50.03000  ? 65   GLU A C   1 
ATOM   359   O O   . GLU A 1 46  ? 4.72100   -55.42500 -23.90100 1.000 44.35000  ? 65   GLU A O   1 
ATOM   360   C CB  . GLU A 1 46  ? 3.16300   -57.09000 -21.66200 1.000 44.97000  ? 65   GLU A CB  1 
ATOM   361   C CG  . GLU A 1 46  ? 2.10200   -56.86900 -20.57100 1.000 59.94000  ? 65   GLU A CG  1 
ATOM   362   C CD  . GLU A 1 46  ? 1.76400   -55.38300 -20.33100 1.000 64.98000  ? 65   GLU A CD  1 
ATOM   363   O OE1 . GLU A 1 46  ? 2.66900   -54.51600 -20.44900 1.000 63.64000  ? 65   GLU A OE1 1 
ATOM   364   O OE2 . GLU A 1 46  ? 0.58300   -55.08200 -20.03600 1.000 65.13000  ? 65   GLU A OE2 1 
ATOM   365   N N   . LYS A 1 47  ? 4.11200   -57.40200 -24.81300 1.000 42.08000  ? 66   LYS A N   1 
ATOM   366   C CA  . LYS A 1 47  ? 5.13200   -57.32700 -25.85000 1.000 44.40000  ? 66   LYS A CA  1 
ATOM   367   C C   . LYS A 1 47  ? 4.90700   -56.12900 -26.75400 1.000 46.23000  ? 66   LYS A C   1 
ATOM   368   O O   . LYS A 1 47  ? 5.86200   -55.43500 -27.12100 1.000 48.69000  ? 66   LYS A O   1 
ATOM   369   C CB  . LYS A 1 47  ? 5.14700   -58.60900 -26.67900 1.000 43.84000  ? 66   LYS A CB  1 
ATOM   370   C CG  . LYS A 1 47  ? 5.81200   -59.77600 -25.98200 1.000 52.59000  ? 66   LYS A CG  1 
ATOM   371   C CD  . LYS A 1 47  ? 5.65500   -61.07500 -26.75200 1.000 53.08000  ? 66   LYS A CD  1 
ATOM   372   C CE  . LYS A 1 47  ? 6.25400   -62.23500 -25.96500 1.000 48.77000  ? 66   LYS A CE  1 
ATOM   373   N NZ  . LYS A 1 47  ? 6.00200   -63.53400 -26.64800 1.000 52.04000  ? 66   LYS A NZ  1 
ATOM   374   N N   . PHE A 1 48  ? 3.65100   -55.86600 -27.12000 1.000 43.73000  ? 67   PHE A N   1 
ATOM   375   C CA  . PHE A 1 48  ? 3.35500   -54.85500 -28.12500 1.000 41.87000  ? 67   PHE A CA  1 
ATOM   376   C C   . PHE A 1 48  ? 3.93300   -53.48300 -27.76900 1.000 41.80000  ? 67   PHE A C   1 
ATOM   377   O O   . PHE A 1 48  ? 4.69200   -52.93400 -28.57500 1.000 43.36000  ? 67   PHE A O   1 
ATOM   378   C CB  . PHE A 1 48  ? 1.84600   -54.74900 -28.36500 1.000 38.04000  ? 67   PHE A CB  1 
ATOM   379   C CG  . PHE A 1 48  ? 1.48700   -53.72700 -29.39800 1.000 39.13000  ? 67   PHE A CG  1 
ATOM   380   C CD1 . PHE A 1 48  ? 1.65800   -54.00100 -30.74900 1.000 33.97000  ? 67   PHE A CD1 1 
ATOM   381   C CD2 . PHE A 1 48  ? 1.01000   -52.48300 -29.01400 1.000 32.71000  ? 67   PHE A CD2 1 
ATOM   382   C CE1 . PHE A 1 48  ? 1.34400   -53.06300 -31.70100 1.000 33.29000  ? 67   PHE A CE1 1 
ATOM   383   C CE2 . PHE A 1 48  ? 0.70100   -51.53400 -29.95600 1.000 33.07000  ? 67   PHE A CE2 1 
ATOM   384   C CZ  . PHE A 1 48  ? 0.86100   -51.82100 -31.30800 1.000 35.79000  ? 67   PHE A CZ  1 
ATOM   385   N N   . PRO A 1 49  ? 3.65400   -52.90300 -26.59400 1.000 44.15000  ? 68   PRO A N   1 
ATOM   386   C CA  . PRO A 1 49  ? 4.25800   -51.59300 -26.29700 1.000 43.38000  ? 68   PRO A CA  1 
ATOM   387   C C   . PRO A 1 49  ? 5.77000   -51.62700 -26.21400 1.000 48.09000  ? 68   PRO A C   1 
ATOM   388   O O   . PRO A 1 49  ? 6.41400   -50.60300 -26.47100 1.000 53.58000  ? 68   PRO A O   1 
ATOM   389   C CB  . PRO A 1 49  ? 3.62400   -51.20200 -24.95700 1.000 38.87000  ? 68   PRO A CB  1 
ATOM   390   C CG  . PRO A 1 49  ? 3.23900   -52.48000 -24.33700 1.000 43.28000  ? 68   PRO A CG  1 
ATOM   391   C CD  . PRO A 1 49  ? 2.83400   -53.38200 -25.46700 1.000 41.34000  ? 68   PRO A CD  1 
ATOM   392   N N   . GLN A 1 50  ? 6.36000   -52.77300 -25.86600 1.000 51.68000  ? 69   GLN A N   1 
ATOM   393   C CA  . GLN A 1 50  ? 7.81600   -52.85900 -25.77700 1.000 48.54000  ? 69   GLN A CA  1 
ATOM   394   C C   . GLN A 1 50  ? 8.45900   -52.83800 -27.15900 1.000 51.80000  ? 69   GLN A C   1 
ATOM   395   O O   . GLN A 1 50  ? 9.48200   -52.17500 -27.35800 1.000 66.79000  ? 69   GLN A O   1 
ATOM   396   C CB  . GLN A 1 50  ? 8.21900   -54.11500 -25.00000 1.000 45.82000  ? 69   GLN A CB  1 
ATOM   397   C CG  . GLN A 1 50  ? 7.98700   -53.99500 -23.49400 1.000 60.42000  ? 69   GLN A CG  1 
ATOM   398   C CD  . GLN A 1 50  ? 8.11000   -55.32500 -22.75000 1.000 75.08000  ? 69   GLN A CD  1 
ATOM   399   O OE1 . GLN A 1 50  ? 8.18200   -56.39600 -23.36000 1.000 72.30000  ? 69   GLN A OE1 1 
ATOM   400   N NE2 . GLN A 1 50  ? 8.14000   -55.25600 -21.42000 1.000 79.23000  ? 69   GLN A NE2 1 
ATOM   401   N N   . VAL A 1 51  ? 7.86900   -53.54100 -28.13100 1.000 47.60000  ? 70   VAL A N   1 
ATOM   402   C CA  . VAL A 1 51  ? 8.47600   -53.68900 -29.45000 1.000 44.47000  ? 70   VAL A CA  1 
ATOM   403   C C   . VAL A 1 51  ? 7.87700   -52.76300 -30.50500 1.000 57.38000  ? 70   VAL A C   1 
ATOM   404   O O   . VAL A 1 51  ? 8.51900   -52.54100 -31.54300 1.000 60.36000  ? 70   VAL A O   1 
ATOM   405   C CB  . VAL A 1 51  ? 8.37200   -55.14300 -29.95600 1.000 46.99000  ? 70   VAL A CB  1 
ATOM   406   C CG1 . VAL A 1 51  ? 8.94900   -56.11800 -28.94700 1.000 39.02000  ? 70   VAL A CG1 1 
ATOM   407   C CG2 . VAL A 1 51  ? 6.92500   -55.49100 -30.33100 1.000 48.18000  ? 70   VAL A CG2 1 
ATOM   408   N N   . ALA A 1 52  ? 6.65600   -52.25600 -30.30400 1.000 56.90000  ? 71   ALA A N   1 
ATOM   409   C CA  . ALA A 1 52  ? 6.07000   -51.38100 -31.31500 1.000 58.98000  ? 71   ALA A CA  1 
ATOM   410   C C   . ALA A 1 52  ? 6.91600   -50.13200 -31.49800 1.000 66.40000  ? 71   ALA A C   1 
ATOM   411   O O   . ALA A 1 52  ? 7.06000   -49.62600 -32.61900 1.000 67.78000  ? 71   ALA A O   1 
ATOM   412   C CB  . ALA A 1 52  ? 4.63000   -51.01800 -30.95100 1.000 51.21000  ? 71   ALA A CB  1 
ATOM   413   N N   . ALA A 1 53  ? 7.50300   -49.63700 -30.40300 1.000 68.53000  ? 72   ALA A N   1 
ATOM   414   C CA  . ALA A 1 53  ? 8.41400   -48.50300 -30.49500 1.000 76.47000  ? 72   ALA A CA  1 
ATOM   415   C C   . ALA A 1 53  ? 9.59700   -48.81500 -31.40400 1.000 78.59000  ? 72   ALA A C   1 
ATOM   416   O O   . ALA A 1 53  ? 10.04100  -47.95200 -32.17000 1.000 88.86000  ? 72   ALA A O   1 
ATOM   417   C CB  . ALA A 1 53  ? 8.89200   -48.10400 -29.10000 1.000 74.46000  ? 72   ALA A CB  1 
ATOM   418   N N   . THR A 1 54  ? 10.12300  -50.04200 -31.34200 1.000 77.45000  ? 73   THR A N   1 
ATOM   419   C CA  . THR A 1 54  ? 11.27000  -50.42600 -32.15600 1.000 71.84000  ? 73   THR A CA  1 
ATOM   420   C C   . THR A 1 54  ? 10.85100  -50.99200 -33.50700 1.000 73.46000  ? 73   THR A C   1 
ATOM   421   O O   . THR A 1 54  ? 11.67700  -51.59400 -34.20500 1.000 72.20000  ? 73   THR A O   1 
ATOM   422   C CB  . THR A 1 54  ? 12.13700  -51.45200 -31.42800 1.000 68.32000  ? 73   THR A CB  1 
ATOM   423   O OG1 . THR A 1 54  ? 11.54700  -52.74800 -31.54200 1.000 71.92000  ? 73   THR A OG1 1 
ATOM   424   C CG2 . THR A 1 54  ? 12.21100  -51.09000 -29.95600 1.000 75.39000  ? 73   THR A CG2 1 
ATOM   425   N N   . GLY A 1 55  ? 9.58400   -50.83100 -33.87700 1.000 70.70000  ? 74   GLY A N   1 
ATOM   426   C CA  . GLY A 1 55  ? 9.12600   -51.27100 -35.18000 1.000 67.56000  ? 74   GLY A CA  1 
ATOM   427   C C   . GLY A 1 55  ? 9.12200   -52.77000 -35.39700 1.000 64.32000  ? 74   GLY A C   1 
ATOM   428   O O   . GLY A 1 55  ? 9.11100   -53.21000 -36.55100 1.000 64.79000  ? 74   GLY A O   1 
ATOM   429   N N   . ASP A 1 56  ? 9.10200   -53.58300 -34.33500 1.000 57.78000  ? 75   ASP A N   1 
ATOM   430   C CA  . ASP A 1 56  ? 8.98400   -55.02600 -34.54800 1.000 60.48000  ? 75   ASP A CA  1 
ATOM   431   C C   . ASP A 1 56  ? 7.64800   -55.60000 -34.09400 1.000 60.00000  ? 75   ASP A C   1 
ATOM   432   O O   . ASP A 1 56  ? 7.57700   -56.79900 -33.80100 1.000 55.24000  ? 75   ASP A O   1 
ATOM   433   C CB  . ASP A 1 56  ? 10.09500  -55.83900 -33.87800 1.000 65.95000  ? 75   ASP A CB  1 
ATOM   434   C CG  . ASP A 1 56  ? 11.47400  -55.46400 -34.36300 1.000 77.75000  ? 75   ASP A CG  1 
ATOM   435   O OD1 . ASP A 1 56  ? 11.62900  -54.37500 -34.96200 1.000 80.26000  ? 75   ASP A OD1 1 
ATOM   436   O OD2 . ASP A 1 56  ? 12.33400  -56.38300 -34.34600 1.000 80.00000  ? 75   ASP A OD2 1 
ATOM   437   N N   . GLY A 1 57  ? 6.59300   -54.78600 -34.02800 1.000 54.78000  ? 76   GLY A N   1 
ATOM   438   C CA  . GLY A 1 57  ? 5.28500   -55.29400 -33.67500 1.000 48.76000  ? 76   GLY A CA  1 
ATOM   439   C C   . GLY A 1 57  ? 4.51600   -55.79500 -34.88300 1.000 45.92000  ? 76   GLY A C   1 
ATOM   440   O O   . GLY A 1 57  ? 5.06300   -55.91700 -35.98300 1.000 35.70000  ? 76   GLY A O   1 
ATOM   441   N N   . PRO A 1 58  ? 3.23300   -56.10300 -34.70200 1.000 45.07000  ? 77   PRO A N   1 
ATOM   442   C CA  . PRO A 1 58  ? 2.39900   -56.53800 -35.82900 1.000 35.65000  ? 77   PRO A CA  1 
ATOM   443   C C   . PRO A 1 58  ? 1.84800   -55.34600 -36.59700 1.000 34.27000  ? 77   PRO A C   1 
ATOM   444   O O   . PRO A 1 58  ? 1.96900   -54.19700 -36.18800 1.000 40.08000  ? 77   PRO A O   1 
ATOM   445   C CB  . PRO A 1 58  ? 1.26800   -57.30900 -35.15400 1.000 38.66000  ? 77   PRO A CB  1 
ATOM   446   C CG  . PRO A 1 58  ? 1.15100   -56.66500 -33.80500 1.000 36.57000  ? 77   PRO A CG  1 
ATOM   447   C CD  . PRO A 1 58  ? 2.54500   -56.26100 -33.40900 1.000 37.57000  ? 77   PRO A CD  1 
ATOM   448   N N   . ASP A 1 59  ? 1.24900   -55.64300 -37.74800 1.000 34.94000  ? 78   ASP A N   1 
ATOM   449   C CA  . ASP A 1 59  ? 0.45300   -54.64100 -38.45000 1.000 37.72000  ? 78   ASP A CA  1 
ATOM   450   C C   . ASP A 1 59  ? -0.82300  -54.33800 -37.67700 1.000 36.29000  ? 78   ASP A C   1 
ATOM   451   O O   . ASP A 1 59  ? -1.19000  -53.16800 -37.49000 1.000 37.05000  ? 78   ASP A O   1 
ATOM   452   C CB  . ASP A 1 59  ? 0.10400   -55.16100 -39.84600 1.000 43.82000  ? 78   ASP A CB  1 
ATOM   453   C CG  . ASP A 1 59  ? 1.30200   -55.22700 -40.76300 1.000 44.41000  ? 78   ASP A CG  1 
ATOM   454   O OD1 . ASP A 1 59  ? 1.94300   -54.17200 -40.98400 1.000 39.48000  ? 78   ASP A OD1 1 
ATOM   455   O OD2 . ASP A 1 59  ? 1.64500   -56.36300 -41.17500 1.000 45.16000  ? 78   ASP A OD2 1 
ATOM   456   N N   . ILE A 1 60  ? -1.49600  -55.39200 -37.20500 1.000 31.33000  ? 79   ILE A N   1 
ATOM   457   C CA  . ILE A 1 60  ? -2.78300  -55.31000 -36.52500 1.000 32.10000  ? 79   ILE A CA  1 
ATOM   458   C C   . ILE A 1 60  ? -2.69500  -56.06500 -35.20400 1.000 36.33000  ? 79   ILE A C   1 
ATOM   459   O O   . ILE A 1 60  ? -2.09400  -57.14400 -35.13600 1.000 34.08000  ? 79   ILE A O   1 
ATOM   460   C CB  . ILE A 1 60  ? -3.91700  -55.89900 -37.38900 1.000 33.51000  ? 79   ILE A CB  1 
ATOM   461   C CG1 . ILE A 1 60  ? -4.04000  -55.15900 -38.71900 1.000 33.79000  ? 79   ILE A CG1 1 
ATOM   462   C CG2 . ILE A 1 60  ? -5.22900  -55.85200 -36.64500 1.000 33.06000  ? 79   ILE A CG2 1 
ATOM   463   C CD1 . ILE A 1 60  ? -4.92800  -55.86700 -39.69100 1.000 28.16000  ? 79   ILE A CD1 1 
ATOM   464   N N   . ILE A 1 61  ? -3.30700  -55.51300 -34.15700 1.000 31.82000  ? 80   ILE A N   1 
ATOM   465   C CA  . ILE A 1 61  ? -3.34300  -56.14600 -32.84600 1.000 30.23000  ? 80   ILE A CA  1 
ATOM   466   C C   . ILE A 1 61  ? -4.78600  -56.20900 -32.36300 1.000 30.21000  ? 80   ILE A C   1 
ATOM   467   O O   . ILE A 1 61  ? -5.50300  -55.20100 -32.40500 1.000 29.73000  ? 80   ILE A O   1 
ATOM   468   C CB  . ILE A 1 61  ? -2.45100  -55.39500 -31.83700 1.000 31.83000  ? 80   ILE A CB  1 
ATOM   469   C CG1 . ILE A 1 61  ? -2.51500  -56.07000 -30.47100 1.000 29.44000  ? 80   ILE A CG1 1 
ATOM   470   C CG2 . ILE A 1 61  ? -2.77300  -53.89600 -31.80900 1.000 27.84000  ? 80   ILE A CG2 1 
ATOM   471   C CD1 . ILE A 1 61  ? -1.45800  -55.60600 -29.53600 1.000 34.19000  ? 80   ILE A CD1 1 
ATOM   472   N N   . PHE A 1 62  ? -5.22600  -57.38800 -31.92300 1.000 29.49000  ? 81   PHE A N   1 
ATOM   473   C CA  . PHE A 1 62  ? -6.54100  -57.50900 -31.30900 1.000 30.02000  ? 81   PHE A CA  1 
ATOM   474   C C   . PHE A 1 62  ? -6.37600  -57.54000 -29.80000 1.000 31.64000  ? 81   PHE A C   1 
ATOM   475   O O   . PHE A 1 62  ? -5.54600  -58.29800 -29.28900 1.000 35.07000  ? 81   PHE A O   1 
ATOM   476   C CB  . PHE A 1 62  ? -7.31400  -58.76200 -31.72200 1.000 29.73000  ? 81   PHE A CB  1 
ATOM   477   C CG  . PHE A 1 62  ? -7.67000  -58.83900 -33.17800 1.000 35.31000  ? 81   PHE A CG  1 
ATOM   478   C CD1 . PHE A 1 62  ? -6.83500  -58.35000 -34.17500 1.000 31.50000  ? 81   PHE A CD1 1 
ATOM   479   C CD2 . PHE A 1 62  ? -8.95300  -59.23200 -33.52700 1.000 30.16000  ? 81   PHE A CD2 1 
ATOM   480   C CE1 . PHE A 1 62  ? -7.21400  -58.41300 -35.50700 1.000 31.39000  ? 81   PHE A CE1 1 
ATOM   481   C CE2 . PHE A 1 62  ? -9.35400  -59.26700 -34.85600 1.000 31.97000  ? 81   PHE A CE2 1 
ATOM   482   C CZ  . PHE A 1 62  ? -8.48600  -58.85400 -35.85100 1.000 26.14000  ? 81   PHE A CZ  1 
ATOM   483   N N   . TRP A 1 63  ? -7.16900  -56.73500 -29.08900 1.000 33.66000  ? 82   TRP A N   1 
ATOM   484   C CA  . TRP A 1 63  ? -7.19000  -56.80600 -27.62700 1.000 34.45000  ? 82   TRP A CA  1 
ATOM   485   C C   . TRP A 1 63  ? -8.39300  -56.02400 -27.10300 1.000 34.41000  ? 82   TRP A C   1 
ATOM   486   O O   . TRP A 1 63  ? -9.06900  -55.30300 -27.84400 1.000 27.33000  ? 82   TRP A O   1 
ATOM   487   C CB  . TRP A 1 63  ? -5.89700  -56.26400 -27.00200 1.000 33.06000  ? 82   TRP A CB  1 
ATOM   488   C CG  . TRP A 1 63  ? -5.68200  -56.79200 -25.62500 1.000 33.89000  ? 82   TRP A CG  1 
ATOM   489   C CD1 . TRP A 1 63  ? -5.93700  -56.16200 -24.44100 1.000 34.48000  ? 82   TRP A CD1 1 
ATOM   490   C CD2 . TRP A 1 63  ? -5.17500  -58.08700 -25.29200 1.000 34.69000  ? 82   TRP A CD2 1 
ATOM   491   N NE1 . TRP A 1 63  ? -5.63000  -56.99600 -23.39000 1.000 32.06000  ? 82   TRP A NE1 1 
ATOM   492   C CE2 . TRP A 1 63  ? -5.16300  -58.18400 -23.89000 1.000 32.57000  ? 82   TRP A CE2 1 
ATOM   493   C CE3 . TRP A 1 63  ? -4.73400  -59.17800 -26.05100 1.000 36.60000  ? 82   TRP A CE3 1 
ATOM   494   C CZ2 . TRP A 1 63  ? -4.72200  -59.32700 -23.22900 1.000 40.63000  ? 82   TRP A CZ2 1 
ATOM   495   C CZ3 . TRP A 1 63  ? -4.30300  -60.31200 -25.39600 1.000 39.87000  ? 82   TRP A CZ3 1 
ATOM   496   C CH2 . TRP A 1 63  ? -4.29500  -60.37800 -23.99800 1.000 41.63000  ? 82   TRP A CH2 1 
ATOM   497   N N   . ALA A 1 64  ? -8.64400  -56.18400 -25.80100 1.000 31.94000  ? 83   ALA A N   1 
ATOM   498   C CA  . ALA A 1 64  ? -9.63100  -55.37500 -25.10200 1.000 35.66000  ? 83   ALA A CA  1 
ATOM   499   C C   . ALA A 1 64  ? -9.36900  -53.89000 -25.31700 1.000 32.63000  ? 83   ALA A C   1 
ATOM   500   O O   . ALA A 1 64  ? -8.23200  -53.42700 -25.20700 1.000 27.57000  ? 83   ALA A O   1 
ATOM   501   C CB  . ALA A 1 64  ? -9.59400  -55.70300 -23.61300 1.000 34.84000  ? 83   ALA A CB  1 
ATOM   502   N N   . HIS A 1 65  ? -10.43300 -53.13900 -25.61200 1.000 29.41000  ? 84   HIS A N   1 
ATOM   503   C CA  . HIS A 1 65  ? -10.25200 -51.74400 -25.99800 1.000 30.00000  ? 84   HIS A CA  1 
ATOM   504   C C   . HIS A 1 65  ? -9.55400  -50.93400 -24.91100 1.000 36.15000  ? 84   HIS A C   1 
ATOM   505   O O   . HIS A 1 65  ? -8.79400  -50.01200 -25.23200 1.000 29.90000  ? 84   HIS A O   1 
ATOM   506   C CB  . HIS A 1 65  ? -11.58800 -51.07900 -26.31900 1.000 26.82000  ? 84   HIS A CB  1 
ATOM   507   C CG  . HIS A 1 65  ? -12.38300 -50.72000 -25.10300 1.000 31.29000  ? 84   HIS A CG  1 
ATOM   508   N ND1 . HIS A 1 65  ? -13.17600 -51.62700 -24.43600 1.000 27.37000  ? 84   HIS A ND1 1 
ATOM   509   C CD2 . HIS A 1 65  ? -12.48600 -49.55400 -24.42000 1.000 27.44000  ? 84   HIS A CD2 1 
ATOM   510   C CE1 . HIS A 1 65  ? -13.74700 -51.03200 -23.40200 1.000 29.97000  ? 84   HIS A CE1 1 
ATOM   511   N NE2 . HIS A 1 65  ? -13.35400 -49.77200 -23.37700 1.000 27.92000  ? 84   HIS A NE2 1 
ATOM   512   N N   . ASP A 1 66  ? -9.80900  -51.22500 -23.62600 1.000 32.94000  ? 85   ASP A N   1 
ATOM   513   C CA  . ASP A 1 66  ? -9.24800  -50.34200 -22.60600 1.000 34.03000  ? 85   ASP A CA  1 
ATOM   514   C C   . ASP A 1 66  ? -7.72900  -50.43000 -22.52900 1.000 37.63000  ? 85   ASP A C   1 
ATOM   515   O O   . ASP A 1 66  ? -7.09000  -49.48600 -22.04800 1.000 42.16000  ? 85   ASP A O   1 
ATOM   516   C CB  . ASP A 1 66  ? -9.84800  -50.60100 -21.21000 1.000 30.59000  ? 85   ASP A CB  1 
ATOM   517   C CG  . ASP A 1 66  ? -9.65700  -52.02100 -20.72600 1.000 34.57000  ? 85   ASP A CG  1 
ATOM   518   O OD1 . ASP A 1 66  ? -9.53900  -52.93900 -21.56700 1.000 43.08000  ? 85   ASP A OD1 1 
ATOM   519   O OD2 . ASP A 1 66  ? -9.50900  -52.20500 -19.49500 1.000 49.34000  ? 85   ASP A OD2 1 
ATOM   520   N N   . ARG A 1 67  ? -7.12900  -51.52000 -23.00700 1.000 34.60000  ? 86   ARG A N   1 
ATOM   521   C CA  . ARG A 1 67  ? -5.67400  -51.55200 -23.07900 1.000 31.72000  ? 86   ARG A CA  1 
ATOM   522   C C   . ARG A 1 67  ? -5.14700  -50.59700 -24.15000 1.000 37.59000  ? 86   ARG A C   1 
ATOM   523   O O   . ARG A 1 67  ? -4.02800  -50.08800 -24.02100 1.000 36.61000  ? 86   ARG A O   1 
ATOM   524   C CB  . ARG A 1 67  ? -5.19200  -52.97700 -23.34300 1.000 34.07000  ? 86   ARG A CB  1 
ATOM   525   C CG  . ARG A 1 67  ? -3.68100  -53.14100 -23.23800 1.000 44.03000  ? 86   ARG A CG  1 
ATOM   526   C CD  . ARG A 1 67  ? -3.22000  -52.93400 -21.79200 1.000 47.63000  ? 86   ARG A CD  1 
ATOM   527   N NE  . ARG A 1 67  ? -1.76900  -53.01700 -21.65000 1.000 54.58000  ? 86   ARG A NE  1 
ATOM   528   C CZ  . ARG A 1 67  ? -0.94500  -52.00300 -21.88800 1.000 57.13000  ? 86   ARG A CZ  1 
ATOM   529   N NH1 . ARG A 1 67  ? -1.39900  -50.82900 -22.31100 1.000 49.32000  ? 86   ARG A NH1 1 
ATOM   530   N NH2 . ARG A 1 67  ? 0.36300   -52.16900 -21.70300 1.000 50.03000  ? 86   ARG A NH2 1 
ATOM   531   N N   . PHE A 1 68  ? -5.93700  -50.33200 -25.20500 1.000 34.31000  ? 87   PHE A N   1 
ATOM   532   C CA  . PHE A 1 68  ? -5.46800  -49.48600 -26.30600 1.000 32.27000  ? 87   PHE A CA  1 
ATOM   533   C C   . PHE A 1 68  ? -5.27500  -48.03600 -25.89400 1.000 34.12000  ? 87   PHE A C   1 
ATOM   534   O O   . PHE A 1 68  ? -4.61600  -47.28300 -26.62500 1.000 32.96000  ? 87   PHE A O   1 
ATOM   535   C CB  . PHE A 1 68  ? -6.43100  -49.51100 -27.50400 1.000 31.81000  ? 87   PHE A CB  1 
ATOM   536   C CG  . PHE A 1 68  ? -6.37800  -50.77500 -28.32300 1.000 27.54000  ? 87   PHE A CG  1 
ATOM   537   C CD1 . PHE A 1 68  ? -5.44500  -51.75900 -28.05800 1.000 28.06000  ? 87   PHE A CD1 1 
ATOM   538   C CD2 . PHE A 1 68  ? -7.22600  -50.94200 -29.40200 1.000 24.76000  ? 87   PHE A CD2 1 
ATOM   539   C CE1 . PHE A 1 68  ? -5.39100  -52.91200 -28.81900 1.000 27.35000  ? 87   PHE A CE1 1 
ATOM   540   C CE2 . PHE A 1 68  ? -7.17700  -52.08800 -30.17300 1.000 29.04000  ? 87   PHE A CE2 1 
ATOM   541   C CZ  . PHE A 1 68  ? -6.24900  -53.07500 -29.88000 1.000 32.39000  ? 87   PHE A CZ  1 
ATOM   542   N N   . GLY A 1 69  ? -5.84300  -47.62100 -24.75900 1.000 28.03000  ? 88   GLY A N   1 
ATOM   543   C CA  . GLY A 1 69  ? -5.61800  -46.26100 -24.29200 1.000 33.76000  ? 88   GLY A CA  1 
ATOM   544   C C   . GLY A 1 69  ? -4.15000  -45.97600 -24.02300 1.000 37.42000  ? 88   GLY A C   1 
ATOM   545   O O   . GLY A 1 69  ? -3.61600  -44.93900 -24.43200 1.000 37.43000  ? 88   GLY A O   1 
ATOM   546   N N   . GLY A 1 70  ? -3.47400  -46.89900 -23.33000 1.000 37.55000  ? 89   GLY A N   1 
ATOM   547   C CA  . GLY A 1 70  ? -2.04600  -46.74300 -23.10500 1.000 36.27000  ? 89   GLY A CA  1 
ATOM   548   C C   . GLY A 1 70  ? -1.25200  -46.77200 -24.39600 1.000 37.52000  ? 89   GLY A C   1 
ATOM   549   O O   . GLY A 1 70  ? -0.31400  -45.99300 -24.57700 1.000 42.32000  ? 89   GLY A O   1 
ATOM   550   N N   . TYR A 1 71  ? -1.62200  -47.66500 -25.31700 1.000 32.23000  ? 90   TYR A N   1 
ATOM   551   C CA  . TYR A 1 71  ? -0.95600  -47.69600 -26.61300 1.000 36.74000  ? 90   TYR A CA  1 
ATOM   552   C C   . TYR A 1 71  ? -1.09500  -46.35500 -27.32000 1.000 38.49000  ? 90   TYR A C   1 
ATOM   553   O O   . TYR A 1 71  ? -0.11600  -45.80400 -27.84100 1.000 38.18000  ? 90   TYR A O   1 
ATOM   554   C CB  . TYR A 1 71  ? -1.54800  -48.79700 -27.48800 1.000 34.59000  ? 90   TYR A CB  1 
ATOM   555   C CG  . TYR A 1 71  ? -1.40100  -50.19600 -26.95100 1.000 35.41000  ? 90   TYR A CG  1 
ATOM   556   C CD1 . TYR A 1 71  ? -0.61400  -50.46700 -25.84100 1.000 31.43000  ? 90   TYR A CD1 1 
ATOM   557   C CD2 . TYR A 1 71  ? -2.03500  -51.25500 -27.58300 1.000 33.68000  ? 90   TYR A CD2 1 
ATOM   558   C CE1 . TYR A 1 71  ? -0.48200  -51.75500 -25.36700 1.000 37.65000  ? 90   TYR A CE1 1 
ATOM   559   C CE2 . TYR A 1 71  ? -1.91400  -52.53700 -27.11800 1.000 38.69000  ? 90   TYR A CE2 1 
ATOM   560   C CZ  . TYR A 1 71  ? -1.13400  -52.78800 -26.01500 1.000 43.51000  ? 90   TYR A CZ  1 
ATOM   561   O OH  . TYR A 1 71  ? -1.02400  -54.08900 -25.57700 1.000 45.56000  ? 90   TYR A OH  1 
ATOM   562   N N   . ALA A 1 72  ? -2.31700  -45.81800 -27.34100 1.000 32.98000  ? 91   ALA A N   1 
ATOM   563   C CA  . ALA A 1 72  ? -2.56400  -44.54700 -28.00800 1.000 34.22000  ? 91   ALA A CA  1 
ATOM   564   C C   . ALA A 1 72  ? -1.86800  -43.40800 -27.28900 1.000 35.25000  ? 91   ALA A C   1 
ATOM   565   O O   . ALA A 1 72  ? -1.37400  -42.47600 -27.93400 1.000 39.92000  ? 91   ALA A O   1 
ATOM   566   C CB  . ALA A 1 72  ? -4.06200  -44.27000 -28.10600 1.000 31.17000  ? 91   ALA A CB  1 
ATOM   567   N N   . GLN A 1 73  ? -1.82200  -43.46000 -25.95500 1.000 30.05000  ? 92   GLN A N   1 
ATOM   568   C CA  . GLN A 1 73  ? -1.10800  -42.42500 -25.21700 1.000 35.35000  ? 92   GLN A CA  1 
ATOM   569   C C   . GLN A 1 73  ? 0.35300   -42.35700 -25.63200 1.000 34.94000  ? 92   GLN A C   1 
ATOM   570   O O   . GLN A 1 73  ? 0.94800   -41.27500 -25.61500 1.000 34.53000  ? 92   GLN A O   1 
ATOM   571   C CB  . GLN A 1 73  ? -1.22200  -42.66700 -23.71300 1.000 41.90000  ? 92   GLN A CB  1 
ATOM   572   C CG  . GLN A 1 73  ? -0.55700  -41.59400 -22.85900 1.000 35.38000  ? 92   GLN A CG  1 
ATOM   573   C CD  . GLN A 1 73  ? -1.18200  -40.23100 -23.07600 1.000 45.37000  ? 92   GLN A CD  1 
ATOM   574   O OE1 . GLN A 1 73  ? -2.38000  -40.11700 -23.35400 1.000 46.17000  ? 92   GLN A OE1 1 
ATOM   575   N NE2 . GLN A 1 73  ? -0.38100  -39.18400 -22.91500 1.000 44.78000  ? 92   GLN A NE2 1 
ATOM   576   N N   . SER A 1 74  ? 0.93800   -43.49000 -26.02000 1.000 29.65000  ? 93   SER A N   1 
ATOM   577   C CA  . SER A 1 74  ? 2.31400   -43.54800 -26.49000 1.000 35.48000  ? 93   SER A CA  1 
ATOM   578   C C   . SER A 1 74  ? 2.43300   -43.34500 -27.99900 1.000 39.40000  ? 93   SER A C   1 
ATOM   579   O O   . SER A 1 74  ? 3.53600   -43.46300 -28.54000 1.000 47.68000  ? 93   SER A O   1 
ATOM   580   C CB  . SER A 1 74  ? 2.95000   -44.88600 -26.10300 1.000 31.29000  ? 93   SER A CB  1 
ATOM   581   O OG  . SER A 1 74  ? 2.97800   -45.05800 -24.69400 1.000 41.20000  ? 93   SER A OG  1 
ATOM   582   N N   . GLY A 1 75  ? 1.33400   -43.06600 -28.69400 1.000 41.23000  ? 94   GLY A N   1 
ATOM   583   C CA  . GLY A 1 75  ? 1.40700   -42.89400 -30.13400 1.000 31.26000  ? 94   GLY A CA  1 
ATOM   584   C C   . GLY A 1 75  ? 1.66700   -44.17300 -30.89800 1.000 35.23000  ? 94   GLY A C   1 
ATOM   585   O O   . GLY A 1 75  ? 2.19100   -44.12500 -32.01200 1.000 36.16000  ? 94   GLY A O   1 
ATOM   586   N N   . LEU A 1 76  ? 1.30900   -45.32600 -30.33500 1.000 38.78000  ? 95   LEU A N   1 
ATOM   587   C CA  . LEU A 1 76  ? 1.63900   -46.59200 -30.97200 1.000 37.06000  ? 95   LEU A CA  1 
ATOM   588   C C   . LEU A 1 76  ? 0.58600   -47.07300 -31.96300 1.000 34.88000  ? 95   LEU A C   1 
ATOM   589   O O   . LEU A 1 76  ? 0.85900   -48.01400 -32.71500 1.000 33.86000  ? 95   LEU A O   1 
ATOM   590   C CB  . LEU A 1 76  ? 1.84500   -47.66300 -29.91200 1.000 32.05000  ? 95   LEU A CB  1 
ATOM   591   C CG  . LEU A 1 76  ? 2.92900   -47.28600 -28.91000 1.000 41.19000  ? 95   LEU A CG  1 
ATOM   592   C CD1 . LEU A 1 76  ? 3.01600   -48.35800 -27.82800 1.000 36.99000  ? 95   LEU A CD1 1 
ATOM   593   C CD2 . LEU A 1 76  ? 4.26900   -47.04900 -29.61300 1.000 36.81000  ? 95   LEU A CD2 1 
ATOM   594   N N   . LEU A 1 77  ? -0.59700  -46.45900 -31.99300 1.000 33.70000  ? 96   LEU A N   1 
ATOM   595   C CA  . LEU A 1 77  ? -1.69700  -46.92200 -32.82500 1.000 29.49000  ? 96   LEU A CA  1 
ATOM   596   C C   . LEU A 1 77  ? -2.02800  -45.89000 -33.89500 1.000 30.85000  ? 96   LEU A C   1 
ATOM   597   O O   . LEU A 1 77  ? -2.11500  -44.68700 -33.61900 1.000 30.51000  ? 96   LEU A O   1 
ATOM   598   C CB  . LEU A 1 77  ? -2.94400  -47.21600 -31.98400 1.000 30.83000  ? 96   LEU A CB  1 
ATOM   599   C CG  . LEU A 1 77  ? -2.92600  -48.43800 -31.06500 1.000 29.68000  ? 96   LEU A CG  1 
ATOM   600   C CD1 . LEU A 1 77  ? -4.20300  -48.50300 -30.24100 1.000 30.26000  ? 96   LEU A CD1 1 
ATOM   601   C CD2 . LEU A 1 77  ? -2.74500  -49.72800 -31.85000 1.000 26.30000  ? 96   LEU A CD2 1 
ATOM   602   N N   . ALA A 1 78  ? -2.21300  -46.37300 -35.11900 1.000 29.44000  ? 97   ALA A N   1 
ATOM   603   C CA  . ALA A 1 78  ? -2.61900  -45.51000 -36.21700 1.000 33.64000  ? 97   ALA A CA  1 
ATOM   604   C C   . ALA A 1 78  ? -4.02500  -44.96400 -35.98000 1.000 37.11000  ? 97   ALA A C   1 
ATOM   605   O O   . ALA A 1 78  ? -4.92500  -45.68600 -35.53800 1.000 33.04000  ? 97   ALA A O   1 
ATOM   606   C CB  . ALA A 1 78  ? -2.55800  -46.27800 -37.53100 1.000 28.99000  ? 97   ALA A CB  1 
ATOM   607   N N   . GLU A 1 79  ? -4.20800  -43.67300 -36.26300 1.000 31.52000  ? 98   GLU A N   1 
ATOM   608   C CA  . GLU A 1 79  ? -5.52900  -43.06100 -36.19200 1.000 33.30000  ? 98   GLU A CA  1 
ATOM   609   C C   . GLU A 1 79  ? -6.30200  -43.34400 -37.47900 1.000 39.98000  ? 98   GLU A C   1 
ATOM   610   O O   . GLU A 1 79  ? -5.78400  -43.13200 -38.58000 1.000 42.06000  ? 98   GLU A O   1 
ATOM   611   C CB  . GLU A 1 79  ? -5.41100  -41.55400 -35.97000 1.000 36.16000  ? 98   GLU A CB  1 
ATOM   612   C CG  . GLU A 1 79  ? -6.77600  -40.85000 -35.93200 1.000 53.95000  ? 98   GLU A CG  1 
ATOM   613   C CD  . GLU A 1 79  ? -6.66000  -39.33800 -35.81200 1.000 61.49000  ? 98   GLU A CD  1 
ATOM   614   O OE1 . GLU A 1 79  ? -5.51000  -38.83300 -35.82600 1.000 63.68000  ? 98   GLU A OE1 1 
ATOM   615   O OE2 . GLU A 1 79  ? -7.71200  -38.66100 -35.71800 1.000 54.09000  ? 98   GLU A OE2 1 
ATOM   616   N N   . ILE A 1 80  ? -7.53800  -43.81500 -37.34300 1.000 38.03000  ? 99   ILE A N   1 
ATOM   617   C CA  . ILE A 1 80  ? -8.36500  -44.18900 -38.48400 1.000 38.34000  ? 99   ILE A CA  1 
ATOM   618   C C   . ILE A 1 80  ? -9.54500  -43.23600 -38.59700 1.000 41.15000  ? 99   ILE A C   1 
ATOM   619   O O   . ILE A 1 80  ? -10.03700 -42.68700 -37.60300 1.000 44.08000  ? 99   ILE A O   1 
ATOM   620   C CB  . ILE A 1 80  ? -8.87300  -45.64000 -38.37000 1.000 36.54000  ? 99   ILE A CB  1 
ATOM   621   C CG1 . ILE A 1 80  ? -9.83800  -45.75300 -37.19100 1.000 33.42000  ? 99   ILE A CG1 1 
ATOM   622   C CG2 . ILE A 1 80  ? -7.70500  -46.59800 -38.18700 1.000 38.12000  ? 99   ILE A CG2 1 
ATOM   623   C CD1 . ILE A 1 80  ? -10.61900 -47.03300 -37.13500 1.000 30.43000  ? 99   ILE A CD1 1 
ATOM   624   N N   . THR A 1 81  ? -10.00500 -43.04700 -39.83000 1.000 35.53000  ? 100  THR A N   1 
ATOM   625   C CA  . THR A 1 81  ? -11.24800 -42.32800 -40.12000 1.000 43.44000  ? 100  THR A CA  1 
ATOM   626   C C   . THR A 1 81  ? -12.00600 -43.06400 -41.22000 1.000 35.90000  ? 100  THR A C   1 
ATOM   627   O O   . THR A 1 81  ? -12.00200 -42.65700 -42.38300 1.000 36.81000  ? 100  THR A O   1 
ATOM   628   C CB  . THR A 1 81  ? -10.96800 -40.86600 -40.49100 1.000 45.57000  ? 100  THR A CB  1 
ATOM   629   O OG1 . THR A 1 81  ? -9.85000  -40.79700 -41.38200 1.000 53.75000  ? 100  THR A OG1 1 
ATOM   630   C CG2 . THR A 1 81  ? -10.70900 -40.01600 -39.24900 1.000 46.65000  ? 100  THR A CG2 1 
ATOM   631   N N   . PRO A 1 82  ? -12.65700 -44.17500 -40.88000 1.000 37.70000  ? 101  PRO A N   1 
ATOM   632   C CA  . PRO A 1 82  ? -13.42800 -44.92000 -41.88100 1.000 31.08000  ? 101  PRO A CA  1 
ATOM   633   C C   . PRO A 1 82  ? -14.64200 -44.13500 -42.35700 1.000 34.66000  ? 101  PRO A C   1 
ATOM   634   O O   . PRO A 1 82  ? -15.14100 -43.22800 -41.68600 1.000 35.23000  ? 101  PRO A O   1 
ATOM   635   C CB  . PRO A 1 82  ? -13.84700 -46.19200 -41.13700 1.000 32.42000  ? 101  PRO A CB  1 
ATOM   636   C CG  . PRO A 1 82  ? -13.83000 -45.80500 -39.69100 1.000 33.68000  ? 101  PRO A CG  1 
ATOM   637   C CD  . PRO A 1 82  ? -12.74000 -44.78900 -39.54100 1.000 34.44000  ? 101  PRO A CD  1 
ATOM   638   N N   . ALA A 1 83  ? -15.11500 -44.50700 -43.54700 1.000 32.83000  ? 102  ALA A N   1 
ATOM   639   C CA  . ALA A 1 83  ? -16.19800 -43.79100 -44.20300 1.000 37.12000  ? 102  ALA A CA  1 
ATOM   640   C C   . ALA A 1 83  ? -17.47400 -43.83700 -43.36700 1.000 35.23000  ? 102  ALA A C   1 
ATOM   641   O O   . ALA A 1 83  ? -17.68200 -44.73200 -42.53800 1.000 30.81000  ? 102  ALA A O   1 
ATOM   642   C CB  . ALA A 1 83  ? -16.46400 -44.37400 -45.58500 1.000 33.60000  ? 102  ALA A CB  1 
ATOM   643   N N   . ALA A 1 84  ? -18.33800 -42.84600 -43.60500 1.000 36.19000  ? 103  ALA A N   1 
ATOM   644   C CA  . ALA A 1 84  ? -19.59400 -42.74300 -42.87000 1.000 34.05000  ? 103  ALA A CA  1 
ATOM   645   C C   . ALA A 1 84  ? -20.37600 -44.04400 -42.93100 1.000 30.11000  ? 103  ALA A C   1 
ATOM   646   O O   . ALA A 1 84  ? -20.82000 -44.56700 -41.90300 1.000 36.24000  ? 103  ALA A O   1 
ATOM   647   C CB  . ALA A 1 84  ? -20.43300 -41.59500 -43.42800 1.000 31.33000  ? 103  ALA A CB  1 
ATOM   648   N N   . ALA A 1 85  ? -20.54100 -44.59000 -44.13400 1.000 27.87000  ? 104  ALA A N   1 
ATOM   649   C CA  . ALA A 1 85  ? -21.35200 -45.79400 -44.28100 1.000 32.01000  ? 104  ALA A CA  1 
ATOM   650   C C   . ALA A 1 85  ? -20.72700 -46.95900 -43.53800 1.000 31.01000  ? 104  ALA A C   1 
ATOM   651   O O   . ALA A 1 85  ? -21.43700 -47.79700 -42.97100 1.000 32.86000  ? 104  ALA A O   1 
ATOM   652   C CB  . ALA A 1 85  ? -21.54100 -46.14100 -45.75800 1.000 28.20000  ? 104  ALA A CB  1 
ATOM   653   N N   . PHE A 1 86  ? -19.39800 -47.04100 -43.53700 1.000 30.87000  ? 105  PHE A N   1 
ATOM   654   C CA  . PHE A 1 86  ? -18.77200 -48.12900 -42.80700 1.000 26.95000  ? 105  PHE A CA  1 
ATOM   655   C C   . PHE A 1 86  ? -19.01100 -48.00300 -41.31200 1.000 32.35000  ? 105  PHE A C   1 
ATOM   656   O O   . PHE A 1 86  ? -19.27800 -49.00500 -40.63900 1.000 32.42000  ? 105  PHE A O   1 
ATOM   657   C CB  . PHE A 1 86  ? -17.28200 -48.21200 -43.06600 1.000 24.90000  ? 105  PHE A CB  1 
ATOM   658   C CG  . PHE A 1 86  ? -16.65900 -49.33300 -42.32100 1.000 29.37000  ? 105  PHE A CG  1 
ATOM   659   C CD1 . PHE A 1 86  ? -16.82000 -50.63100 -42.76300 1.000 29.66000  ? 105  PHE A CD1 1 
ATOM   660   C CD2 . PHE A 1 86  ? -16.00400 -49.11100 -41.12400 1.000 29.87000  ? 105  PHE A CD2 1 
ATOM   661   C CE1 . PHE A 1 86  ? -16.28700 -51.68800 -42.06000 1.000 30.12000  ? 105  PHE A CE1 1 
ATOM   662   C CE2 . PHE A 1 86  ? -15.48900 -50.16300 -40.41000 1.000 33.48000  ? 105  PHE A CE2 1 
ATOM   663   C CZ  . PHE A 1 86  ? -15.62400 -51.45600 -40.88400 1.000 34.26000  ? 105  PHE A CZ  1 
ATOM   664   N N   . GLN A 1 87  ? -18.89100 -46.79000 -40.76200 1.000 32.62000  ? 106  GLN A N   1 
ATOM   665   C CA  . GLN A 1 87  ? -19.13900 -46.63800 -39.33100 1.000 32.97000  ? 106  GLN A CA  1 
ATOM   666   C C   . GLN A 1 87  ? -20.57800 -47.00900 -39.00700 1.000 31.54000  ? 106  GLN A C   1 
ATOM   667   O O   . GLN A 1 87  ? -20.84700 -47.66100 -37.99600 1.000 35.97000  ? 106  GLN A O   1 
ATOM   668   C CB  . GLN A 1 87  ? -18.84000 -45.21200 -38.86100 1.000 32.78000  ? 106  GLN A CB  1 
ATOM   669   C CG  . GLN A 1 87  ? -17.47700 -44.66900 -39.27800 1.000 32.98000  ? 106  GLN A CG  1 
ATOM   670   C CD  . GLN A 1 87  ? -17.03900 -43.45300 -38.46700 1.000 37.04000  ? 106  GLN A CD  1 
ATOM   671   O OE1 . GLN A 1 87  ? -17.56200 -43.18600 -37.38600 1.000 35.21000  ? 106  GLN A OE1 1 
ATOM   672   N NE2 . GLN A 1 87  ? -16.12500 -42.66400 -39.03400 1.000 31.70000  ? 106  GLN A NE2 1 
ATOM   673   N N   . ASP A 1 88  ? -21.51200 -46.65300 -39.88600 1.000 31.07000  ? 107  ASP A N   1 
ATOM   674   C CA  . ASP A 1 88  ? -22.92200 -46.92400 -39.62800 1.000 36.93000  ? 107  ASP A CA  1 
ATOM   675   C C   . ASP A 1 88  ? -23.25300 -48.41700 -39.63300 1.000 31.27000  ? 107  ASP A C   1 
ATOM   676   O O   . ASP A 1 88  ? -24.35900 -48.78300 -39.23500 1.000 24.96000  ? 107  ASP A O   1 
ATOM   677   C CB  . ASP A 1 88  ? -23.76800 -46.14500 -40.64600 1.000 35.54000  ? 107  ASP A CB  1 
ATOM   678   C CG  . ASP A 1 88  ? -25.23200 -46.10300 -40.28000 1.000 41.06000  ? 107  ASP A CG  1 
ATOM   679   O OD1 . ASP A 1 88  ? -25.55000 -45.56600 -39.19900 1.000 40.14000  ? 107  ASP A OD1 1 
ATOM   680   O OD2 . ASP A 1 88  ? -26.07600 -46.52800 -41.10300 1.000 48.55000  ? 107  ASP A OD2 1 
ATOM   681   N N   . LYS A 1 89  ? -22.32700 -49.28200 -40.06100 1.000 33.77000  ? 108  LYS A N   1 
ATOM   682   C CA  . LYS A 1 89  ? -22.53200 -50.72800 -39.97800 1.000 35.68000  ? 108  LYS A CA  1 
ATOM   683   C C   . LYS A 1 89  ? -22.40600 -51.25300 -38.55400 1.000 35.14000  ? 108  LYS A C   1 
ATOM   684   O O   . LYS A 1 89  ? -22.90700 -52.34600 -38.25400 1.000 31.67000  ? 108  LYS A O   1 
ATOM   685   C CB  . LYS A 1 89  ? -21.52900 -51.45700 -40.87200 1.000 37.76000  ? 108  LYS A CB  1 
ATOM   686   C CG  . LYS A 1 89  ? -21.77000 -51.27600 -42.36000 1.000 34.72000  ? 108  LYS A CG  1 
ATOM   687   C CD  . LYS A 1 89  ? -20.62500 -51.85100 -43.18800 1.000 36.51000  ? 108  LYS A CD  1 
ATOM   688   C CE  . LYS A 1 89  ? -20.59000 -53.37400 -43.12900 1.000 40.49000  ? 108  LYS A CE  1 
ATOM   689   N NZ  . LYS A 1 89  ? -19.59200 -53.95100 -44.08000 1.000 38.47000  ? 108  LYS A NZ  1 
ATOM   690   N N   . LEU A 1 90  ? -21.74300 -50.49900 -37.68300 1.000 31.79000  ? 109  LEU A N   1 
ATOM   691   C CA  . LEU A 1 90  ? -21.38900 -50.89800 -36.32700 1.000 36.92000  ? 109  LEU A CA  1 
ATOM   692   C C   . LEU A 1 90  ? -22.23000 -50.10400 -35.33300 1.000 33.96000  ? 109  LEU A C   1 
ATOM   693   O O   . LEU A 1 90  ? -22.69300 -49.00100 -35.64300 1.000 30.08000  ? 109  LEU A O   1 
ATOM   694   C CB  . LEU A 1 90  ? -19.89000 -50.66400 -36.08400 1.000 31.98000  ? 109  LEU A CB  1 
ATOM   695   C CG  . LEU A 1 90  ? -18.90900 -51.77300 -36.48900 1.000 32.86000  ? 109  LEU A CG  1 
ATOM   696   C CD1 . LEU A 1 90  ? -19.10500 -52.20700 -37.90600 1.000 30.39000  ? 109  LEU A CD1 1 
ATOM   697   C CD2 . LEU A 1 90  ? -17.49500 -51.25500 -36.36300 1.000 32.01000  ? 109  LEU A CD2 1 
ATOM   698   N N   . TYR A 1 91  ? -22.45200 -50.67200 -34.14600 1.000 31.43000  ? 110  TYR A N   1 
ATOM   699   C CA  . TYR A 1 91  ? -23.26000 -49.96500 -33.15100 1.000 31.31000  ? 110  TYR A CA  1 
ATOM   700   C C   . TYR A 1 91  ? -22.49900 -48.73600 -32.68000 1.000 37.17000  ? 110  TYR A C   1 
ATOM   701   O O   . TYR A 1 91  ? -21.29800 -48.83200 -32.38700 1.000 30.83000  ? 110  TYR A O   1 
ATOM   702   C CB  . TYR A 1 91  ? -23.59900 -50.83600 -31.94800 1.000 26.74000  ? 110  TYR A CB  1 
ATOM   703   C CG  . TYR A 1 91  ? -24.56800 -51.95800 -32.21300 1.000 31.61000  ? 110  TYR A CG  1 
ATOM   704   C CD1 . TYR A 1 91  ? -25.93800 -51.72600 -32.26500 1.000 31.89000  ? 110  TYR A CD1 1 
ATOM   705   C CD2 . TYR A 1 91  ? -24.11200 -53.26100 -32.37200 1.000 32.16000  ? 110  TYR A CD2 1 
ATOM   706   C CE1 . TYR A 1 91  ? -26.82500 -52.76600 -32.49400 1.000 31.68000  ? 110  TYR A CE1 1 
ATOM   707   C CE2 . TYR A 1 91  ? -24.98700 -54.30100 -32.59500 1.000 34.43000  ? 110  TYR A CE2 1 
ATOM   708   C CZ  . TYR A 1 91  ? -26.33900 -54.05500 -32.66100 1.000 37.03000  ? 110  TYR A CZ  1 
ATOM   709   O OH  . TYR A 1 91  ? -27.19800 -55.10700 -32.89200 1.000 40.27000  ? 110  TYR A OH  1 
ATOM   710   N N   . PRO A 1 92  ? -23.15100 -47.57600 -32.58500 1.000 34.91000  ? 111  PRO A N   1 
ATOM   711   C CA  . PRO A 1 92  ? -22.42100 -46.35800 -32.19000 1.000 29.61000  ? 111  PRO A CA  1 
ATOM   712   C C   . PRO A 1 92  ? -21.65600 -46.48200 -30.88200 1.000 36.10000  ? 111  PRO A C   1 
ATOM   713   O O   . PRO A 1 92  ? -20.52400 -45.98400 -30.80400 1.000 43.14000  ? 111  PRO A O   1 
ATOM   714   C CB  . PRO A 1 92  ? -23.53100 -45.30500 -32.10600 1.000 31.54000  ? 111  PRO A CB  1 
ATOM   715   C CG  . PRO A 1 92  ? -24.58000 -45.78900 -33.08700 1.000 27.37000  ? 111  PRO A CG  1 
ATOM   716   C CD  . PRO A 1 92  ? -24.54200 -47.29600 -32.99300 1.000 25.76000  ? 111  PRO A CD  1 
ATOM   717   N N   . PHE A 1 93  ? -22.20500 -47.14700 -29.85700 1.000 34.42000  ? 112  PHE A N   1 
ATOM   718   C CA  . PHE A 1 93  ? -21.49600 -47.14900 -28.57800 1.000 38.25000  ? 112  PHE A CA  1 
ATOM   719   C C   . PHE A 1 93  ? -20.16700 -47.88400 -28.68200 1.000 37.65000  ? 112  PHE A C   1 
ATOM   720   O O   . PHE A 1 93  ? -19.23200 -47.57200 -27.93900 1.000 30.15000  ? 112  PHE A O   1 
ATOM   721   C CB  . PHE A 1 93  ? -22.34500 -47.76100 -27.46400 1.000 28.66000  ? 112  PHE A CB  1 
ATOM   722   C CG  . PHE A 1 93  ? -22.43900 -49.26600 -27.50000 1.000 32.05000  ? 112  PHE A CG  1 
ATOM   723   C CD1 . PHE A 1 93  ? -23.37600 -49.90600 -28.30500 1.000 31.36000  ? 112  PHE A CD1 1 
ATOM   724   C CD2 . PHE A 1 93  ? -21.63000 -50.03900 -26.68300 1.000 33.28000  ? 112  PHE A CD2 1 
ATOM   725   C CE1 . PHE A 1 93  ? -23.48000 -51.29200 -28.32200 1.000 29.29000  ? 112  PHE A CE1 1 
ATOM   726   C CE2 . PHE A 1 93  ? -21.72600 -51.42400 -26.69700 1.000 36.07000  ? 112  PHE A CE2 1 
ATOM   727   C CZ  . PHE A 1 93  ? -22.65900 -52.05200 -27.51400 1.000 31.22000  ? 112  PHE A CZ  1 
ATOM   728   N N   . THR A 1 94  ? -20.06100 -48.86500 -29.58800 1.000 33.74000  ? 113  THR A N   1 
ATOM   729   C CA  . THR A 1 94  ? -18.78800 -49.56100 -29.73700 1.000 36.24000  ? 113  THR A CA  1 
ATOM   730   C C   . THR A 1 94  ? -17.73100 -48.64600 -30.33300 1.000 28.21000  ? 113  THR A C   1 
ATOM   731   O O   . THR A 1 94  ? -16.55400 -48.77000 -29.99000 1.000 30.54000  ? 113  THR A O   1 
ATOM   732   C CB  . THR A 1 94  ? -18.95100 -50.83000 -30.58200 1.000 35.96000  ? 113  THR A CB  1 
ATOM   733   O OG1 . THR A 1 94  ? -19.40700 -50.49400 -31.89600 1.000 37.11000  ? 113  THR A OG1 1 
ATOM   734   C CG2 . THR A 1 94  ? -19.94800 -51.77600 -29.92000 1.000 32.78000  ? 113  THR A CG2 1 
ATOM   735   N N   . TRP A 1 95  ? -18.12400 -47.70100 -31.19300 1.000 27.23000  ? 114  TRP A N   1 
ATOM   736   C CA  . TRP A 1 95  ? -17.14400 -46.73100 -31.66200 1.000 27.31000  ? 114  TRP A CA  1 
ATOM   737   C C   . TRP A 1 95  ? -16.63300 -45.85800 -30.53200 1.000 32.16000  ? 114  TRP A C   1 
ATOM   738   O O   . TRP A 1 95  ? -15.47200 -45.43900 -30.55300 1.000 33.32000  ? 114  TRP A O   1 
ATOM   739   C CB  . TRP A 1 95  ? -17.70900 -45.86000 -32.78000 1.000 31.46000  ? 114  TRP A CB  1 
ATOM   740   C CG  . TRP A 1 95  ? -17.75600 -46.54900 -34.11700 1.000 32.19000  ? 114  TRP A CG  1 
ATOM   741   C CD1 . TRP A 1 95  ? -18.86800 -46.92000 -34.82600 1.000 35.23000  ? 114  TRP A CD1 1 
ATOM   742   C CD2 . TRP A 1 95  ? -16.63100 -47.00400 -34.87600 1.000 32.51000  ? 114  TRP A CD2 1 
ATOM   743   N NE1 . TRP A 1 95  ? -18.49900 -47.54000 -35.99400 1.000 32.94000  ? 114  TRP A NE1 1 
ATOM   744   C CE2 . TRP A 1 95  ? -17.13100 -47.61300 -36.04400 1.000 31.38000  ? 114  TRP A CE2 1 
ATOM   745   C CE3 . TRP A 1 95  ? -15.24400 -46.94300 -34.68400 1.000 31.33000  ? 114  TRP A CE3 1 
ATOM   746   C CZ2 . TRP A 1 95  ? -16.29100 -48.14900 -37.02300 1.000 36.65000  ? 114  TRP A CZ2 1 
ATOM   747   C CZ3 . TRP A 1 95  ? -14.41800 -47.47900 -35.65100 1.000 33.45000  ? 114  TRP A CZ3 1 
ATOM   748   C CH2 . TRP A 1 95  ? -14.94100 -48.07000 -36.80900 1.000 32.77000  ? 114  TRP A CH2 1 
ATOM   749   N N   . ASP A 1 96  ? -17.46400 -45.57600 -29.53200 1.000 36.18000  ? 115  ASP A N   1 
ATOM   750   C CA  . ASP A 1 96  ? -16.98000 -44.79200 -28.40100 1.000 31.38000  ? 115  ASP A CA  1 
ATOM   751   C C   . ASP A 1 96  ? -15.84300 -45.49700 -27.68100 1.000 31.00000  ? 115  ASP A C   1 
ATOM   752   O O   . ASP A 1 96  ? -14.95000 -44.83500 -27.13900 1.000 29.66000  ? 115  ASP A O   1 
ATOM   753   C CB  . ASP A 1 96  ? -18.12300 -44.49800 -27.43300 1.000 33.12000  ? 115  ASP A CB  1 
ATOM   754   C CG  . ASP A 1 96  ? -19.16200 -43.56300 -28.03100 1.000 37.29000  ? 115  ASP A CG  1 
ATOM   755   O OD1 . ASP A 1 96  ? -18.81600 -42.77500 -28.93200 1.000 37.25000  ? 115  ASP A OD1 1 
ATOM   756   O OD2 . ASP A 1 96  ? -20.32200 -43.60900 -27.59200 1.000 34.46000  ? 115  ASP A OD2 1 
ATOM   757   N N   . ALA A 1 97  ? -15.85200 -46.83400 -27.66200 1.000 29.18000  ? 116  ALA A N   1 
ATOM   758   C CA  . ALA A 1 97  ? -14.81700 -47.56500 -26.93800 1.000 24.37000  ? 116  ALA A CA  1 
ATOM   759   C C   . ALA A 1 97  ? -13.44800 -47.45000 -27.58900 1.000 32.65000  ? 116  ALA A C   1 
ATOM   760   O O   . ALA A 1 97  ? -12.44100 -47.68200 -26.91000 1.000 33.49000  ? 116  ALA A O   1 
ATOM   761   C CB  . ALA A 1 97  ? -15.19800 -49.04200 -26.81600 1.000 27.12000  ? 116  ALA A CB  1 
ATOM   762   N N   . VAL A 1 98  ? -13.38100 -47.12000 -28.87900 1.000 25.77000  ? 117  VAL A N   1 
ATOM   763   C CA  . VAL A 1 98  ? -12.10300 -46.99600 -29.56700 1.000 27.00000  ? 117  VAL A CA  1 
ATOM   764   C C   . VAL A 1 98  ? -11.77800 -45.53900 -29.88300 1.000 29.11000  ? 117  VAL A C   1 
ATOM   765   O O   . VAL A 1 98  ? -10.97500 -45.26300 -30.77300 1.000 32.38000  ? 117  VAL A O   1 
ATOM   766   C CB  . VAL A 1 98  ? -12.04500 -47.87000 -30.83400 1.000 26.59000  ? 117  VAL A CB  1 
ATOM   767   C CG1 . VAL A 1 98  ? -12.11700 -49.34000 -30.45700 1.000 28.96000  ? 117  VAL A CG1 1 
ATOM   768   C CG2 . VAL A 1 98  ? -13.16800 -47.51000 -31.77400 1.000 24.23000  ? 117  VAL A CG2 1 
ATOM   769   N N   . ARG A 1 99  ? -12.39300 -44.60000 -29.17400 1.000 25.67000  ? 118  ARG A N   1 
ATOM   770   C CA  . ARG A 1 99  ? -11.94500 -43.21700 -29.21500 1.000 30.78000  ? 118  ARG A CA  1 
ATOM   771   C C   . ARG A 1 99  ? -10.94700 -42.99600 -28.09100 1.000 37.18000  ? 118  ARG A C   1 
ATOM   772   O O   . ARG A 1 99  ? -11.14700 -43.46500 -26.96800 1.000 36.04000  ? 118  ARG A O   1 
ATOM   773   C CB  . ARG A 1 99  ? -13.11800 -42.24300 -29.06800 1.000 31.29000  ? 118  ARG A CB  1 
ATOM   774   C CG  . ARG A 1 99  ? -14.14700 -42.35000 -30.17600 1.000 36.67000  ? 118  ARG A CG  1 
ATOM   775   C CD  . ARG A 1 99  ? -15.25400 -41.30500 -30.09600 1.000 37.02000  ? 118  ARG A CD  1 
ATOM   776   N NE  . ARG A 1 99  ? -16.32400 -41.64800 -31.03000 1.000 50.45000  ? 118  ARG A NE  1 
ATOM   777   C CZ  . ARG A 1 99  ? -16.33500 -41.32500 -32.32000 1.000 57.40000  ? 118  ARG A CZ  1 
ATOM   778   N NH1 . ARG A 1 99  ? -15.35300 -40.61800 -32.86700 1.000 52.75000  ? 118  ARG A NH1 1 
ATOM   779   N NH2 . ARG A 1 99  ? -17.34800 -41.73400 -33.08400 1.000 45.34000  ? 118  ARG A NH2 1 
ATOM   780   N N   . TYR A 1 100 ? -9.86000  -42.29700 -28.39800 1.000 36.68000  ? 119  TYR A N   1 
ATOM   781   C CA  . TYR A 1 100 ? -8.91000  -41.87800 -27.37700 1.000 33.80000  ? 119  TYR A CA  1 
ATOM   782   C C   . TYR A 1 100 ? -8.63900  -40.39400 -27.55400 1.000 35.40000  ? 119  TYR A C   1 
ATOM   783   O O   . TYR A 1 100 ? -8.07400  -39.98200 -28.57300 1.000 39.15000  ? 119  TYR A O   1 
ATOM   784   C CB  . TYR A 1 100 ? -7.60400  -42.66400 -27.45500 1.000 26.91000  ? 119  TYR A CB  1 
ATOM   785   C CG  . TYR A 1 100 ? -6.70700  -42.39100 -26.26900 1.000 34.23000  ? 119  TYR A CG  1 
ATOM   786   C CD1 . TYR A 1 100 ? -6.90400  -43.04300 -25.05300 1.000 34.60000  ? 119  TYR A CD1 1 
ATOM   787   C CD2 . TYR A 1 100 ? -5.69100  -41.45500 -26.35500 1.000 33.62000  ? 119  TYR A CD2 1 
ATOM   788   C CE1 . TYR A 1 100 ? -6.08200  -42.78300 -23.96100 1.000 35.45000  ? 119  TYR A CE1 1 
ATOM   789   C CE2 . TYR A 1 100 ? -4.87600  -41.19100 -25.29000 1.000 37.69000  ? 119  TYR A CE2 1 
ATOM   790   C CZ  . TYR A 1 100 ? -5.07000  -41.85200 -24.09200 1.000 41.09000  ? 119  TYR A CZ  1 
ATOM   791   O OH  . TYR A 1 100 ? -4.23000  -41.56300 -23.04200 1.000 40.52000  ? 119  TYR A OH  1 
ATOM   792   N N   . ASN A 1 101 ? -9.03400  -39.59900 -26.56600 1.000 35.24000  ? 120  ASN A N   1 
ATOM   793   C CA  . ASN A 1 101 ? -8.90500  -38.15100 -26.64500 1.000 37.23000  ? 120  ASN A CA  1 
ATOM   794   C C   . ASN A 1 101 ? -9.46300  -37.62300 -27.96300 1.000 42.02000  ? 120  ASN A C   1 
ATOM   795   O O   . ASN A 1 101 ? -8.84700  -36.79200 -28.63100 1.000 41.88000  ? 120  ASN A O   1 
ATOM   796   C CB  . ASN A 1 101 ? -7.45600  -37.70400 -26.48000 1.000 39.20000  ? 120  ASN A CB  1 
ATOM   797   C CG  . ASN A 1 101 ? -7.35400  -36.23300 -26.17400 1.000 41.99000  ? 120  ASN A CG  1 
ATOM   798   O OD1 . ASN A 1 101 ? -8.35700  -35.58800 -25.85400 1.000 43.44000  ? 120  ASN A OD1 1 
ATOM   799   N ND2 . ASN A 1 101 ? -6.17100  -35.67100 -26.34900 1.000 35.73000  ? 120  ASN A ND2 1 
ATOM   800   N N   . GLY A 1 102 ? -10.62100 -38.14200 -28.36400 1.000 38.93000  ? 121  GLY A N   1 
ATOM   801   C CA  . GLY A 1 102 ? -11.30300 -37.67800 -29.54700 1.000 37.84000  ? 121  GLY A CA  1 
ATOM   802   C C   . GLY A 1 102 ? -10.93900 -38.38800 -30.83400 1.000 41.87000  ? 121  GLY A C   1 
ATOM   803   O O   . GLY A 1 102 ? -11.64300 -38.21000 -31.83800 1.000 46.84000  ? 121  GLY A O   1 
ATOM   804   N N   . LYS A 1 103 ? -9.88100  -39.19700 -30.83700 1.000 38.81000  ? 122  LYS A N   1 
ATOM   805   C CA  . LYS A 1 103 ? -9.36300  -39.82300 -32.04700 1.000 31.73000  ? 122  LYS A CA  1 
ATOM   806   C C   . LYS A 1 103 ? -9.79400  -41.27600 -32.10500 1.000 33.25000  ? 122  LYS A C   1 
ATOM   807   O O   . LYS A 1 103 ? -9.67300  -41.99700 -31.11100 1.000 35.73000  ? 122  LYS A O   1 
ATOM   808   C CB  . LYS A 1 103 ? -7.84300  -39.80100 -32.07200 1.000 40.61000  ? 122  LYS A CB  1 
ATOM   809   C CG  . LYS A 1 103 ? -7.16500  -38.47900 -32.08800 1.000 45.99000  ? 122  LYS A CG  1 
ATOM   810   C CD  . LYS A 1 103 ? -5.70000  -38.80000 -32.24000 1.000 51.83000  ? 122  LYS A CD  1 
ATOM   811   C CE  . LYS A 1 103 ? -4.85100  -37.58000 -32.38200 1.000 62.16000  ? 122  LYS A CE  1 
ATOM   812   N NZ  . LYS A 1 103 ? -3.46000  -37.97300 -32.74700 1.000 66.25000  ? 122  LYS A NZ  1 
ATOM   813   N N   . LEU A 1 104 ? -10.25400 -41.71700 -33.27100 1.000 32.67000  ? 123  LEU A N   1 
ATOM   814   C CA  . LEU A 1 104 ? -10.49200 -43.14000 -33.46300 1.000 32.24000  ? 123  LEU A CA  1 
ATOM   815   C C   . LEU A 1 104 ? -9.15900  -43.84800 -33.63800 1.000 31.13000  ? 123  LEU A C   1 
ATOM   816   O O   . LEU A 1 104 ? -8.34700  -43.46000 -34.48100 1.000 31.01000  ? 123  LEU A O   1 
ATOM   817   C CB  . LEU A 1 104 ? -11.40000 -43.38800 -34.67100 1.000 27.29000  ? 123  LEU A CB  1 
ATOM   818   C CG  . LEU A 1 104 ? -12.85300 -42.96300 -34.47100 1.000 37.19000  ? 123  LEU A CG  1 
ATOM   819   C CD1 . LEU A 1 104 ? -13.66100 -43.12800 -35.75400 1.000 30.00000  ? 123  LEU A CD1 1 
ATOM   820   C CD2 . LEU A 1 104 ? -13.46100 -43.78100 -33.35600 1.000 31.11000  ? 123  LEU A CD2 1 
ATOM   821   N N   . ILE A 1 105 ? -8.93000  -44.88800 -32.84300 1.000 27.19000  ? 124  ILE A N   1 
ATOM   822   C CA  . ILE A 1 105 ? -7.63400  -45.54900 -32.89000 1.000 27.09000  ? 124  ILE A CA  1 
ATOM   823   C C   . ILE A 1 105 ? -7.75800  -47.05700 -33.09300 1.000 26.90000  ? 124  ILE A C   1 
ATOM   824   O O   . ILE A 1 105 ? -6.75700  -47.77300 -33.01500 1.000 29.22000  ? 124  ILE A O   1 
ATOM   825   C CB  . ILE A 1 105 ? -6.80900  -45.22200 -31.62700 1.000 28.85000  ? 124  ILE A CB  1 
ATOM   826   C CG1 . ILE A 1 105 ? -7.65100  -45.36700 -30.34800 1.000 26.05000  ? 124  ILE A CG1 1 
ATOM   827   C CG2 . ILE A 1 105 ? -6.22400  -43.81300 -31.72000 1.000 25.28000  ? 124  ILE A CG2 1 
ATOM   828   C CD1 . ILE A 1 105 ? -7.74900  -46.77100 -29.81000 1.000 20.98000  ? 124  ILE A CD1 1 
ATOM   829   N N   . ALA A 1 106 ? -8.95700  -47.56400 -33.37700 1.000 28.99000  ? 125  ALA A N   1 
ATOM   830   C CA  . ALA A 1 106 ? -9.08600  -49.00900 -33.56800 1.000 26.80000  ? 125  ALA A CA  1 
ATOM   831   C C   . ALA A 1 106 ? -10.45200 -49.33100 -34.15700 1.000 28.51000  ? 125  ALA A C   1 
ATOM   832   O O   . ALA A 1 106 ? -11.29500 -48.44600 -34.33800 1.000 24.69000  ? 125  ALA A O   1 
ATOM   833   C CB  . ALA A 1 106 ? -8.88100  -49.77200 -32.25400 1.000 28.13000  ? 125  ALA A CB  1 
ATOM   834   N N   . TYR A 1 107 ? -10.66500 -50.62700 -34.46200 1.000 29.35000  ? 126  TYR A N   1 
ATOM   835   C CA  . TYR A 1 107 ? -11.99400 -50.99100 -34.91800 1.000 27.27000  ? 126  TYR A CA  1 
ATOM   836   C C   . TYR A 1 107 ? -12.66900 -51.91300 -33.92700 1.000 27.48000  ? 126  TYR A C   1 
ATOM   837   O O   . TYR A 1 107 ? -12.08200 -52.93500 -33.55000 1.000 34.39000  ? 126  TYR A O   1 
ATOM   838   C CB  . TYR A 1 107 ? -12.03600 -51.68900 -36.28400 1.000 28.55000  ? 126  TYR A CB  1 
ATOM   839   C CG  . TYR A 1 107 ? -11.49900 -50.98200 -37.49000 1.000 32.16000  ? 126  TYR A CG  1 
ATOM   840   C CD1 . TYR A 1 107 ? -10.21600 -50.45400 -37.52800 1.000 32.39000  ? 126  TYR A CD1 1 
ATOM   841   C CD2 . TYR A 1 107 ? -12.38300 -50.62600 -38.50300 1.000 27.28000  ? 126  TYR A CD2 1 
ATOM   842   C CE1 . TYR A 1 107 ? -9.76400  -49.78400 -38.65500 1.000 33.41000  ? 126  TYR A CE1 1 
ATOM   843   C CE2 . TYR A 1 107 ? -11.97300 -49.92200 -39.59000 1.000 27.49000  ? 126  TYR A CE2 1 
ATOM   844   C CZ  . TYR A 1 107 ? -10.66700 -49.49600 -39.67200 1.000 32.98000  ? 126  TYR A CZ  1 
ATOM   845   O OH  . TYR A 1 107 ? -10.26900 -48.79500 -40.78500 1.000 33.08000  ? 126  TYR A OH  1 
ATOM   846   N N   . PRO A 1 108 ? -13.92800 -51.65300 -33.58200 1.000 26.69000  ? 127  PRO A N   1 
ATOM   847   C CA  . PRO A 1 108 ? -14.62800 -52.51200 -32.62100 1.000 29.90000  ? 127  PRO A CA  1 
ATOM   848   C C   . PRO A 1 108 ? -14.93300 -53.86100 -33.24400 1.000 30.22000  ? 127  PRO A C   1 
ATOM   849   O O   . PRO A 1 108 ? -15.37700 -53.94000 -34.39100 1.000 30.00000  ? 127  PRO A O   1 
ATOM   850   C CB  . PRO A 1 108 ? -15.92800 -51.74700 -32.34500 1.000 28.86000  ? 127  PRO A CB  1 
ATOM   851   C CG  . PRO A 1 108 ? -15.72800 -50.37500 -32.94700 1.000 33.45000  ? 127  PRO A CG  1 
ATOM   852   C CD  . PRO A 1 108 ? -14.80400 -50.59300 -34.10100 1.000 28.87000  ? 127  PRO A CD  1 
ATOM   853   N N   . ILE A 1 109 ? -14.73600 -54.92800 -32.47500 1.000 25.52000  ? 128  ILE A N   1 
ATOM   854   C CA  . ILE A 1 109 ? -15.05000 -56.25200 -33.00700 1.000 32.11000  ? 128  ILE A CA  1 
ATOM   855   C C   . ILE A 1 109 ? -16.18400 -56.93100 -32.24600 1.000 34.79000  ? 128  ILE A C   1 
ATOM   856   O O   . ILE A 1 109 ? -17.19800 -57.30100 -32.84200 1.000 30.63000  ? 128  ILE A O   1 
ATOM   857   C CB  . ILE A 1 109 ? -13.81200 -57.15800 -33.01200 1.000 28.54000  ? 128  ILE A CB  1 
ATOM   858   C CG1 . ILE A 1 109 ? -12.68800 -56.47500 -33.77500 1.000 33.52000  ? 128  ILE A CG1 1 
ATOM   859   C CG2 . ILE A 1 109 ? -14.16400 -58.48400 -33.68000 1.000 26.32000  ? 128  ILE A CG2 1 
ATOM   860   C CD1 . ILE A 1 109 ? -13.07300 -56.16500 -35.19500 1.000 28.61000  ? 128  ILE A CD1 1 
ATOM   861   N N   . ALA A 1 110 ? -16.00800 -57.13400 -30.93900 1.000 34.20000  ? 129  ALA A N   1 
ATOM   862   C CA  . ALA A 1 110 ? -16.95800 -57.86700 -30.11000 1.000 30.00000  ? 129  ALA A CA  1 
ATOM   863   C C   . ALA A 1 110 ? -17.23100 -57.07700 -28.84100 1.000 30.89000  ? 129  ALA A C   1 
ATOM   864   O O   . ALA A 1 110 ? -16.54600 -56.10000 -28.53000 1.000 35.32000  ? 129  ALA A O   1 
ATOM   865   C CB  . ALA A 1 110 ? -16.45500 -59.27700 -29.77100 1.000 28.40000  ? 129  ALA A CB  1 
ATOM   866   N N   . VAL A 1 111 ? -18.25400 -57.51500 -28.11100 1.000 34.70000  ? 130  VAL A N   1 
ATOM   867   C CA  . VAL A 1 111 ? -18.78700 -56.80500 -26.95000 1.000 34.21000  ? 130  VAL A CA  1 
ATOM   868   C C   . VAL A 1 111 ? -19.04100 -57.81000 -25.83100 1.000 30.33000  ? 130  VAL A C   1 
ATOM   869   O O   . VAL A 1 111 ? -19.67700 -58.84500 -26.05900 1.000 34.11000  ? 130  VAL A O   1 
ATOM   870   C CB  . VAL A 1 111 ? -20.10100 -56.08400 -27.31100 1.000 31.95000  ? 130  VAL A CB  1 
ATOM   871   C CG1 . VAL A 1 111 ? -20.69700 -55.45200 -26.10300 1.000 34.78000  ? 130  VAL A CG1 1 
ATOM   872   C CG2 . VAL A 1 111 ? -19.87600 -55.05000 -28.40500 1.000 31.63000  ? 130  VAL A CG2 1 
ATOM   873   N N   . GLU A 1 112 ? -18.58200 -57.51000 -24.61800 1.000 29.40000  ? 131  GLU A N   1 
ATOM   874   C CA  . GLU A 1 112 ? -19.00800 -58.31400 -23.47800 1.000 33.38000  ? 131  GLU A CA  1 
ATOM   875   C C   . GLU A 1 112 ? -19.40600 -57.42700 -22.30600 1.000 33.35000  ? 131  GLU A C   1 
ATOM   876   O O   . GLU A 1 112 ? -18.92800 -56.29700 -22.16100 1.000 30.41000  ? 131  GLU A O   1 
ATOM   877   C CB  . GLU A 1 112 ? -17.95200 -59.32400 -23.01500 1.000 32.36000  ? 131  GLU A CB  1 
ATOM   878   C CG  . GLU A 1 112 ? -16.76200 -58.77400 -22.27600 1.000 39.67000  ? 131  GLU A CG  1 
ATOM   879   C CD  . GLU A 1 112 ? -15.79800 -59.88800 -21.85700 1.000 52.11000  ? 131  GLU A CD  1 
ATOM   880   O OE1 . GLU A 1 112 ? -16.09000 -61.07600 -22.15300 1.000 45.32000  ? 131  GLU A OE1 1 
ATOM   881   O OE2 . GLU A 1 112 ? -14.75400 -59.57500 -21.23200 1.000 50.46000  ? 131  GLU A OE2 1 
ATOM   882   N N   . ALA A 1 113 ? -20.32800 -57.95400 -21.49800 1.000 34.49000  ? 132  ALA A N   1 
ATOM   883   C CA  . ALA A 1 113 ? -20.82500 -57.30300 -20.29200 1.000 35.17000  ? 132  ALA A CA  1 
ATOM   884   C C   . ALA A 1 113 ? -21.49400 -58.35600 -19.41900 1.000 28.72000  ? 132  ALA A C   1 
ATOM   885   O O   . ALA A 1 113 ? -21.83800 -59.44600 -19.88400 1.000 33.10000  ? 132  ALA A O   1 
ATOM   886   C CB  . ALA A 1 113 ? -21.79400 -56.16300 -20.61900 1.000 26.75000  ? 132  ALA A CB  1 
ATOM   887   N N   . LEU A 1 114 ? -21.65100 -58.01900 -18.14000 1.000 30.39000  ? 133  LEU A N   1 
ATOM   888   C CA  . LEU A 1 114 ? -22.37600 -58.85500 -17.18800 1.000 33.15000  ? 133  LEU A CA  1 
ATOM   889   C C   . LEU A 1 114 ? -23.85700 -58.93900 -17.53700 1.000 31.22000  ? 133  LEU A C   1 
ATOM   890   O O   . LEU A 1 114 ? -24.44600 -57.99900 -18.07600 1.000 28.38000  ? 133  LEU A O   1 
ATOM   891   C CB  . LEU A 1 114 ? -22.24200 -58.27000 -15.78400 1.000 30.42000  ? 133  LEU A CB  1 
ATOM   892   C CG  . LEU A 1 114 ? -20.87600 -58.27200 -15.11500 1.000 28.22000  ? 133  LEU A CG  1 
ATOM   893   C CD1 . LEU A 1 114 ? -20.90600 -57.35000 -13.90900 1.000 21.27000  ? 133  LEU A CD1 1 
ATOM   894   C CD2 . LEU A 1 114 ? -20.58900 -59.68600 -14.69400 1.000 28.99000  ? 133  LEU A CD2 1 
ATOM   895   N N   . SER A 1 115 ? -24.47600 -60.06400 -17.18600 1.000 32.59000  ? 134  SER A N   1 
ATOM   896   C CA  . SER A 1 115 ? -25.92700 -60.19200 -17.28400 1.000 31.80000  ? 134  SER A CA  1 
ATOM   897   C C   . SER A 1 115 ? -26.48400 -60.83900 -16.02400 1.000 36.74000  ? 134  SER A C   1 
ATOM   898   O O   . SER A 1 115 ? -25.74200 -61.29200 -15.14400 1.000 29.44000  ? 134  SER A O   1 
ATOM   899   C CB  . SER A 1 115 ? -26.35100 -61.01100 -18.50800 1.000 26.04000  ? 134  SER A CB  1 
ATOM   900   O OG  . SER A 1 115 ? -26.04300 -60.33600 -19.70600 1.000 29.17000  ? 134  SER A OG  1 
ATOM   901   N N   . LEU A 1 116 ? -27.81800 -60.87000 -15.94800 1.000 33.34000  ? 135  LEU A N   1 
ATOM   902   C CA  . LEU A 1 116 ? -28.50100 -61.62700 -14.90800 1.000 30.80000  ? 135  LEU A CA  1 
ATOM   903   C C   . LEU A 1 116 ? -28.63700 -63.06100 -15.39800 1.000 32.55000  ? 135  LEU A C   1 
ATOM   904   O O   . LEU A 1 116 ? -29.17500 -63.30400 -16.48200 1.000 38.04000  ? 135  LEU A O   1 
ATOM   905   C CB  . LEU A 1 116 ? -29.86600 -61.01600 -14.59000 1.000 30.80000  ? 135  LEU A CB  1 
ATOM   906   C CG  . LEU A 1 116 ? -30.67900 -61.56200 -13.41100 1.000 34.58000  ? 135  LEU A CG  1 
ATOM   907   C CD1 . LEU A 1 116 ? -29.95200 -61.33000 -12.09500 1.000 35.46000  ? 135  LEU A CD1 1 
ATOM   908   C CD2 . LEU A 1 116 ? -32.07200 -60.93600 -13.34200 1.000 31.76000  ? 135  LEU A CD2 1 
ATOM   909   N N   . ILE A 1 117 ? -28.10300 -64.00000 -14.62700 1.000 33.95000  ? 136  ILE A N   1 
ATOM   910   C CA  . ILE A 1 117 ? -28.19700 -65.42600 -14.90900 1.000 36.95000  ? 136  ILE A CA  1 
ATOM   911   C C   . ILE A 1 117 ? -29.13500 -66.00900 -13.86200 1.000 36.79000  ? 136  ILE A C   1 
ATOM   912   O O   . ILE A 1 117 ? -29.02800 -65.66500 -12.67800 1.000 35.75000  ? 136  ILE A O   1 
ATOM   913   C CB  . ILE A 1 117 ? -26.81100 -66.09600 -14.86500 1.000 32.89000  ? 136  ILE A CB  1 
ATOM   914   C CG1 . ILE A 1 117 ? -25.86000 -65.40700 -15.84300 1.000 41.88000  ? 136  ILE A CG1 1 
ATOM   915   C CG2 . ILE A 1 117 ? -26.90600 -67.57700 -15.20900 1.000 30.57000  ? 136  ILE A CG2 1 
ATOM   916   C CD1 . ILE A 1 117 ? -24.39100 -65.79100 -15.65400 1.000 28.76000  ? 136  ILE A CD1 1 
ATOM   917   N N   . TYR A 1 118 ? -30.08100 -66.84600 -14.29200 1.000 35.77000  ? 137  TYR A N   1 
ATOM   918   C CA  . TYR A 1 118 ? -31.14400 -67.29600 -13.39900 1.000 36.57000  ? 137  TYR A CA  1 
ATOM   919   C C   . TYR A 1 118 ? -31.44100 -68.77300 -13.61000 1.000 39.39000  ? 137  TYR A C   1 
ATOM   920   O O   . TYR A 1 118 ? -31.19500 -69.32700 -14.68400 1.000 39.81000  ? 137  TYR A O   1 
ATOM   921   C CB  . TYR A 1 118 ? -32.40400 -66.43200 -13.57900 1.000 42.21000  ? 137  TYR A CB  1 
ATOM   922   C CG  . TYR A 1 118 ? -33.04600 -66.46300 -14.96400 1.000 46.98000  ? 137  TYR A CG  1 
ATOM   923   C CD1 . TYR A 1 118 ? -32.49500 -65.74200 -16.02700 1.000 44.42000  ? 137  TYR A CD1 1 
ATOM   924   C CD2 . TYR A 1 118 ? -34.25100 -67.13100 -15.18700 1.000 44.75000  ? 137  TYR A CD2 1 
ATOM   925   C CE1 . TYR A 1 118 ? -33.09100 -65.74700 -17.28700 1.000 40.34000  ? 137  TYR A CE1 1 
ATOM   926   C CE2 . TYR A 1 118 ? -34.85300 -67.13500 -16.44200 1.000 39.10000  ? 137  TYR A CE2 1 
ATOM   927   C CZ  . TYR A 1 118 ? -34.26900 -66.44300 -17.48300 1.000 41.51000  ? 137  TYR A CZ  1 
ATOM   928   O OH  . TYR A 1 118 ? -34.88700 -66.45800 -18.71600 1.000 47.25000  ? 137  TYR A OH  1 
ATOM   929   N N   . ASN A 1 119 ? -31.95100 -69.40700 -12.55300 1.000 35.07000  ? 138  ASN A N   1 
ATOM   930   C CA  . ASN A 1 119 ? -32.34300 -70.81400 -12.58900 1.000 36.37000  ? 138  ASN A CA  1 
ATOM   931   C C   . ASN A 1 119 ? -33.82300 -70.91000 -12.96000 1.000 47.55000  ? 138  ASN A C   1 
ATOM   932   O O   . ASN A 1 119 ? -34.70300 -70.51200 -12.18100 1.000 41.45000  ? 138  ASN A O   1 
ATOM   933   C CB  . ASN A 1 119 ? -32.04400 -71.48900 -11.25100 1.000 40.66000  ? 138  ASN A CB  1 
ATOM   934   C CG  . ASN A 1 119 ? -32.23500 -73.00000 -11.29500 1.000 44.79000  ? 138  ASN A CG  1 
ATOM   935   O OD1 . ASN A 1 119 ? -32.89000 -73.53700 -12.19700 1.000 41.95000  ? 138  ASN A OD1 1 
ATOM   936   N ND2 . ASN A 1 119 ? -31.57900 -73.70100 -10.37000 1.000 35.47000  ? 138  ASN A ND2 1 
ATOM   937   N N   . LYS A 1 120 ? -34.09000 -71.44900 -14.15700 1.000 45.42000  ? 139  LYS A N   1 
ATOM   938   C CA  . LYS A 1 120 ? -35.45200 -71.47300 -14.68300 1.000 45.06000  ? 139  LYS A CA  1 
ATOM   939   C C   . LYS A 1 120 ? -36.36500 -72.32400 -13.81700 1.000 48.54000  ? 139  LYS A C   1 
ATOM   940   O O   . LYS A 1 120 ? -37.52500 -71.96000 -13.58600 1.000 50.39000  ? 139  LYS A O   1 
ATOM   941   C CB  . LYS A 1 120 ? -35.45200 -71.98600 -16.11900 1.000 43.23000  ? 139  LYS A CB  1 
ATOM   942   C CG  . LYS A 1 120 ? -34.86600 -71.01200 -17.12600 1.000 51.07000  ? 139  LYS A CG  1 
ATOM   943   C CD  . LYS A 1 120 ? -34.83800 -71.61800 -18.51900 1.000 44.97000  ? 139  LYS A CD  1 
ATOM   944   C CE  . LYS A 1 120 ? -34.31200 -70.62300 -19.52600 1.000 50.33000  ? 139  LYS A CE  1 
ATOM   945   N NZ  . LYS A 1 120 ? -34.18900 -71.21900 -20.88100 1.000 55.79000  ? 139  LYS A NZ  1 
ATOM   946   N N   . ASP A 1 121 ? -35.86500 -73.46700 -13.34200 1.000 47.16000  ? 140  ASP A N   1 
ATOM   947   C CA  . ASP A 1 121 ? -36.67300 -74.32500 -12.48400 1.000 48.42000  ? 140  ASP A CA  1 
ATOM   948   C C   . ASP A 1 121 ? -37.02300 -73.62900 -11.17800 1.000 44.65000  ? 140  ASP A C   1 
ATOM   949   O O   . ASP A 1 121 ? -38.17700 -73.67000 -10.74000 1.000 53.06000  ? 140  ASP A O   1 
ATOM   950   C CB  . ASP A 1 121 ? -35.94300 -75.64300 -12.23000 1.000 46.77000  ? 140  ASP A CB  1 
ATOM   951   C CG  . ASP A 1 121 ? -35.87800 -76.51300 -13.47200 1.000 61.67000  ? 140  ASP A CG  1 
ATOM   952   O OD1 . ASP A 1 121 ? -36.80900 -76.42100 -14.30800 1.000 57.74000  ? 140  ASP A OD1 1 
ATOM   953   O OD2 . ASP A 1 121 ? -34.90200 -77.28100 -13.62100 1.000 69.35000  ? 140  ASP A OD2 1 
ATOM   954   N N   . LEU A 1 122 ? -36.05600 -72.96100 -10.55700 1.000 44.08000  ? 141  LEU A N   1 
ATOM   955   C CA  . LEU A 1 122 ? -36.33900 -72.24900 -9.31900  1.000 41.09000  ? 141  LEU A CA  1 
ATOM   956   C C   . LEU A 1 122 ? -37.07000 -70.93600 -9.56400  1.000 40.70000  ? 141  LEU A C   1 
ATOM   957   O O   . LEU A 1 122 ? -37.83900 -70.49000 -8.70900  1.000 41.75000  ? 141  LEU A O   1 
ATOM   958   C CB  . LEU A 1 122 ? -35.04100 -71.96700 -8.56600  1.000 37.75000  ? 141  LEU A CB  1 
ATOM   959   C CG  . LEU A 1 122 ? -34.16900 -73.16100 -8.17800  1.000 44.10000  ? 141  LEU A CG  1 
ATOM   960   C CD1 . LEU A 1 122 ? -32.85900 -72.66900 -7.54600  1.000 43.50000  ? 141  LEU A CD1 1 
ATOM   961   C CD2 . LEU A 1 122 ? -34.89900 -74.11100 -7.25100  1.000 40.50000  ? 141  LEU A CD2 1 
ATOM   962   N N   . LEU A 1 123 ? -36.84000 -70.29000 -10.70300 1.000 42.81000  ? 142  LEU A N   1 
ATOM   963   C CA  . LEU A 1 123 ? -37.29500 -68.91600 -10.91600 1.000 45.41000  ? 142  LEU A CA  1 
ATOM   964   C C   . LEU A 1 123 ? -37.64400 -68.71900 -12.38300 1.000 47.75000  ? 142  LEU A C   1 
ATOM   965   O O   . LEU A 1 123 ? -36.88200 -68.11900 -13.15000 1.000 49.31000  ? 142  LEU A O   1 
ATOM   966   C CB  . LEU A 1 123 ? -36.22500 -67.92000 -10.46700 1.000 47.77000  ? 142  LEU A CB  1 
ATOM   967   C CG  . LEU A 1 123 ? -36.57200 -66.43300 -10.44800 1.000 46.57000  ? 142  LEU A CG  1 
ATOM   968   C CD1 . LEU A 1 123 ? -37.73400 -66.17800 -9.50400  1.000 51.04000  ? 142  LEU A CD1 1 
ATOM   969   C CD2 . LEU A 1 123 ? -35.35100 -65.63500 -10.01600 1.000 42.20000  ? 142  LEU A CD2 1 
ATOM   970   N N   . PRO A 1 124 ? -38.80400 -69.21900 -12.81400 1.000 49.70000  ? 143  PRO A N   1 
ATOM   971   C CA  . PRO A 1 124 ? -39.17600 -69.07400 -14.23400 1.000 48.37000  ? 143  PRO A CA  1 
ATOM   972   C C   . PRO A 1 124 ? -39.28200 -67.62700 -14.67000 1.000 46.69000  ? 143  PRO A C   1 
ATOM   973   O O   . PRO A 1 124 ? -39.05500 -67.31500 -15.84700 1.000 46.39000  ? 143  PRO A O   1 
ATOM   974   C CB  . PRO A 1 124 ? -40.54000 -69.77700 -14.31500 1.000 48.57000  ? 143  PRO A CB  1 
ATOM   975   C CG  . PRO A 1 124 ? -40.61100 -70.65800 -13.08600 1.000 51.38000  ? 143  PRO A CG  1 
ATOM   976   C CD  . PRO A 1 124 ? -39.84700 -69.90600 -12.03100 1.000 47.16000  ? 143  PRO A CD  1 
ATOM   977   N N   . ASN A 1 125 ? -39.66900 -66.76900 -13.73300 1.000 41.26000  ? 144  ASN A N   1 
ATOM   978   C CA  . ASN A 1 125 ? -39.87200 -65.33100 -14.02000 1.000 45.53000  ? 144  ASN A CA  1 
ATOM   979   C C   . ASN A 1 125 ? -38.86600 -64.48100 -13.24900 1.000 43.65000  ? 144  ASN A C   1 
ATOM   980   O O   . ASN A 1 125 ? -39.18200 -64.03600 -12.16400 1.000 38.09000  ? 144  ASN A O   1 
ATOM   981   C CB  . ASN A 1 125 ? -41.32200 -64.91400 -13.79600 1.000 46.52000  ? 144  ASN A CB  1 
ATOM   982   C CG  . ASN A 1 125 ? -42.24500 -65.61300 -14.76000 1.000 51.52000  ? 144  ASN A CG  1 
ATOM   983   O OD1 . ASN A 1 125 ? -42.23100 -65.33600 -15.94600 1.000 43.60000  ? 144  ASN A OD1 1 
ATOM   984   N ND2 . ASN A 1 125 ? -43.01400 -66.55700 -14.26100 1.000 57.80000  ? 144  ASN A ND2 1 
ATOM   985   N N   . PRO A 1 126 ? -37.67400 -64.22000 -13.81200 1.000 48.28000  ? 145  PRO A N   1 
ATOM   986   C CA  . PRO A 1 126 ? -36.67300 -63.42300 -13.14400 1.000 44.61000  ? 145  PRO A CA  1 
ATOM   987   C C   . PRO A 1 126 ? -37.18900 -61.99900 -12.94000 1.000 41.72000  ? 145  PRO A C   1 
ATOM   988   O O   . PRO A 1 126 ? -37.83500 -61.48700 -13.78700 1.000 41.87000  ? 145  PRO A O   1 
ATOM   989   C CB  . PRO A 1 126 ? -35.49000 -63.45500 -14.11000 1.000 44.12000  ? 145  PRO A CB  1 
ATOM   990   C CG  . PRO A 1 126 ? -36.11500 -63.74000 -15.43700 1.000 46.09000  ? 145  PRO A CG  1 
ATOM   991   C CD  . PRO A 1 126 ? -37.23800 -64.68900 -15.11300 1.000 42.87000  ? 145  PRO A CD  1 
ATOM   992   N N   . PRO A 1 127 ? -36.88000 -61.36300 -11.80300 1.000 38.92000  ? 146  PRO A N   1 
ATOM   993   C CA  . PRO A 1 127 ? -37.34300 -60.01700 -11.52300 1.000 37.41000  ? 146  PRO A CA  1 
ATOM   994   C C   . PRO A 1 127 ? -36.81200 -58.94200 -12.47500 1.000 36.06000  ? 146  PRO A C   1 
ATOM   995   O O   . PRO A 1 127 ? -35.71000 -58.99300 -12.87100 1.000 40.59000  ? 146  PRO A O   1 
ATOM   996   C CB  . PRO A 1 127 ? -36.76300 -59.74600 -10.13800 1.000 41.04000  ? 146  PRO A CB  1 
ATOM   997   C CG  . PRO A 1 127 ? -35.57700 -60.64600 -10.07600 1.000 43.23000  ? 146  PRO A CG  1 
ATOM   998   C CD  . PRO A 1 127 ? -36.05600 -61.90400 -10.75000 1.000 40.59000  ? 146  PRO A CD  1 
ATOM   999   N N   . LYS A 1 128 ? -37.67000 -58.00800 -12.82900 1.000 36.02000  ? 147  LYS A N   1 
ATOM   1000  C CA  . LYS A 1 128 ? -37.26000 -56.87900 -13.65000 1.000 34.14000  ? 147  LYS A CA  1 
ATOM   1001  C C   . LYS A 1 128 ? -36.64000 -55.75600 -12.83400 1.000 39.92000  ? 147  LYS A C   1 
ATOM   1002  O O   . LYS A 1 128 ? -35.93300 -54.91300 -13.40400 1.000 37.59000  ? 147  LYS A O   1 
ATOM   1003  C CB  . LYS A 1 128 ? -38.45700 -56.32000 -14.42900 1.000 33.03000  ? 147  LYS A CB  1 
ATOM   1004  C CG  . LYS A 1 128 ? -39.10000 -57.30300 -15.40800 1.000 37.88000  ? 147  LYS A CG  1 
ATOM   1005  C CD  . LYS A 1 128 ? -38.14300 -57.65400 -16.55500 1.000 49.92000  ? 147  LYS A CD  1 
ATOM   1006  C CE  . LYS A 1 128 ? -38.78200 -58.58800 -17.58600 1.000 46.55000  ? 147  LYS A CE  1 
ATOM   1007  N NZ  . LYS A 1 128 ? -39.82700 -57.90600 -18.41100 1.000 43.54000  ? 147  LYS A NZ  1 
ATOM   1008  N N   . THR A 1 129 ? -36.88100 -55.72800 -11.52200 1.000 34.33000  ? 148  THR A N   1 
ATOM   1009  C CA  . THR A 1 129 ? -36.32600 -54.70500 -10.64900 1.000 36.29000  ? 148  THR A CA  1 
ATOM   1010  C C   . THR A 1 129 ? -35.54400 -55.33600 -9.50500  1.000 35.28000  ? 148  THR A C   1 
ATOM   1011  O O   . THR A 1 129 ? -35.82700 -56.45900 -9.07100  1.000 35.94000  ? 148  THR A O   1 
ATOM   1012  C CB  . THR A 1 129 ? -37.42200 -53.81300 -10.04700 1.000 37.79000  ? 148  THR A CB  1 
ATOM   1013  O OG1 . THR A 1 129 ? -38.24000 -54.60100 -9.17600  1.000 36.00000  ? 148  THR A OG1 1 
ATOM   1014  C CG2 . THR A 1 129 ? -38.29300 -53.21400 -11.13700 1.000 24.75000  ? 148  THR A CG2 1 
ATOM   1015  N N   . TRP A 1 130 ? -34.55100 -54.58700 -9.02100  1.000 37.91000  ? 149  TRP A N   1 
ATOM   1016  C CA  . TRP A 1 130 ? -33.88900 -54.94700 -7.77200  1.000 37.96000  ? 149  TRP A CA  1 
ATOM   1017  C C   . TRP A 1 130 ? -34.85200 -54.88000 -6.59100  1.000 37.90000  ? 149  TRP A C   1 
ATOM   1018  O O   . TRP A 1 130 ? -34.74100 -55.66800 -5.64500  1.000 34.23000  ? 149  TRP A O   1 
ATOM   1019  C CB  . TRP A 1 130 ? -32.69700 -54.02500 -7.52600  1.000 41.27000  ? 149  TRP A CB  1 
ATOM   1020  C CG  . TRP A 1 130 ? -31.46800 -54.33800 -8.33600  1.000 40.41000  ? 149  TRP A CG  1 
ATOM   1021  C CD1 . TRP A 1 130 ? -31.12700 -53.82000 -9.55100  1.000 34.39000  ? 149  TRP A CD1 1 
ATOM   1022  C CD2 . TRP A 1 130 ? -30.38900 -55.20000 -7.95100  1.000 38.27000  ? 149  TRP A CD2 1 
ATOM   1023  N NE1 . TRP A 1 130 ? -29.92200 -54.33100 -9.96500  1.000 32.35000  ? 149  TRP A NE1 1 
ATOM   1024  C CE2 . TRP A 1 130 ? -29.44400 -55.18000 -9.00100  1.000 37.64000  ? 149  TRP A CE2 1 
ATOM   1025  C CE3 . TRP A 1 130 ? -30.13800 -55.99900 -6.82600  1.000 30.34000  ? 149  TRP A CE3 1 
ATOM   1026  C CZ2 . TRP A 1 130 ? -28.25700 -55.92100 -8.95700  1.000 34.62000  ? 149  TRP A CZ2 1 
ATOM   1027  C CZ3 . TRP A 1 130 ? -28.96400 -56.73900 -6.78500  1.000 40.09000  ? 149  TRP A CZ3 1 
ATOM   1028  C CH2 . TRP A 1 130 ? -28.03300 -56.69100 -7.84600  1.000 40.98000  ? 149  TRP A CH2 1 
ATOM   1029  N N   . GLU A 1 131 ? -35.80100 -53.94000 -6.62400  1.000 37.12000  ? 150  GLU A N   1 
ATOM   1030  C CA  . GLU A 1 131 ? -36.63700 -53.68900 -5.45400  1.000 34.72000  ? 150  GLU A CA  1 
ATOM   1031  C C   . GLU A 1 131 ? -37.48200 -54.89100 -5.03900  1.000 34.62000  ? 150  GLU A C   1 
ATOM   1032  O O   . GLU A 1 131 ? -37.87600 -54.97100 -3.87100  1.000 37.86000  ? 150  GLU A O   1 
ATOM   1033  C CB  . GLU A 1 131 ? -37.53700 -52.48500 -5.70500  1.000 34.72000  ? 150  GLU A CB  1 
ATOM   1034  C CG  . GLU A 1 131 ? -36.82400 -51.13400 -5.70200  1.000 32.37000  ? 150  GLU A CG  1 
ATOM   1035  C CD  . GLU A 1 131 ? -36.20700 -50.78100 -7.03900  1.000 37.15000  ? 150  GLU A CD  1 
ATOM   1036  O OE1 . GLU A 1 131 ? -36.20500 -51.64300 -7.94900  1.000 36.42000  ? 150  GLU A OE1 1 
ATOM   1037  O OE2 . GLU A 1 131 ? -35.77900 -49.61300 -7.20100  1.000 33.00000  ? 150  GLU A OE2 1 
ATOM   1038  N N   . GLU A 1 132 ? -37.77200 -55.81900 -5.94800  1.000 36.73000  ? 151  GLU A N   1 
ATOM   1039  C CA  . GLU A 1 132 ? -38.54300 -57.02000 -5.62400  1.000 41.55000  ? 151  GLU A CA  1 
ATOM   1040  C C   . GLU A 1 132 ? -37.69200 -58.20600 -5.18600  1.000 44.89000  ? 151  GLU A C   1 
ATOM   1041  O O   . GLU A 1 132 ? -38.25800 -59.25500 -4.84800  1.000 42.88000  ? 151  GLU A O   1 
ATOM   1042  C CB  . GLU A 1 132 ? -39.42300 -57.42300 -6.81800  1.000 38.05000  ? 151  GLU A CB  1 
ATOM   1043  C CG  . GLU A 1 132 ? -38.71700 -57.34100 -8.14500  1.000 36.94000  ? 151  GLU A CG  1 
ATOM   1044  C CD  . GLU A 1 132 ? -39.61000 -57.68500 -9.33000  1.000 41.36000  ? 151  GLU A CD  1 
ATOM   1045  O OE1 . GLU A 1 132 ? -40.57600 -58.45900 -9.18300  1.000 47.23000  ? 151  GLU A OE1 1 
ATOM   1046  O OE2 . GLU A 1 132 ? -39.42200 -57.06600 -10.39200 1.000 50.65000  ? 151  GLU A OE2 1 
ATOM   1047  N N   . ILE A 1 133 ? -36.36800 -58.06500 -5.17700  1.000 39.00000  ? 152  ILE A N   1 
ATOM   1048  C CA  . ILE A 1 133 ? -35.44300 -59.11100 -4.73700  1.000 41.83000  ? 152  ILE A CA  1 
ATOM   1049  C C   . ILE A 1 133 ? -35.61900 -59.49000 -3.26700  1.000 42.59000  ? 152  ILE A C   1 
ATOM   1050  O O   . ILE A 1 133 ? -35.56700 -60.68800 -2.95100  1.000 48.16000  ? 152  ILE A O   1 
ATOM   1051  C CB  . ILE A 1 133 ? -33.98300 -58.69600 -4.98100  1.000 40.53000  ? 152  ILE A CB  1 
ATOM   1052  C CG1 . ILE A 1 133 ? -33.71300 -58.52900 -6.47000  1.000 42.49000  ? 152  ILE A CG1 1 
ATOM   1053  C CG2 . ILE A 1 133 ? -33.04900 -59.73700 -4.40600  1.000 30.99000  ? 152  ILE A CG2 1 
ATOM   1054  C CD1 . ILE A 1 133 ? -33.79200 -59.81300 -7.20700  1.000 41.52000  ? 152  ILE A CD1 1 
ATOM   1055  N N   . PRO A 1 134 ? -35.77300 -58.52900 -2.31300  1.000 35.99000  ? 153  PRO A N   1 
ATOM   1056  C CA  . PRO A 1 134 ? -35.97500 -58.93200 -0.91100  1.000 39.94000  ? 153  PRO A CA  1 
ATOM   1057  C C   . PRO A 1 134 ? -37.11200 -59.92800 -0.75700  1.000 46.03000  ? 153  PRO A C   1 
ATOM   1058  O O   . PRO A 1 134 ? -36.91100 -61.04500 -0.26500  1.000 46.97000  ? 153  PRO A O   1 
ATOM   1059  C CB  . PRO A 1 134 ? -36.30000 -57.60800 -0.20700  1.000 35.19000  ? 153  PRO A CB  1 
ATOM   1060  C CG  . PRO A 1 134 ? -35.64500 -56.56900 -1.04900  1.000 32.88000  ? 153  PRO A CG  1 
ATOM   1061  C CD  . PRO A 1 134 ? -35.77500 -57.05700 -2.45100  1.000 34.10000  ? 153  PRO A CD  1 
ATOM   1062  N N   . ALA A 1 135 ? -38.30600 -59.52600 -1.21600  1.000 47.07000  ? 154  ALA A N   1 
ATOM   1063  C CA  . ALA A 1 135 ? -39.48900 -60.37700 -1.12300  1.000 41.95000  ? 154  ALA A CA  1 
ATOM   1064  C C   . ALA A 1 135 ? -39.26500 -61.72200 -1.79700  1.000 44.90000  ? 154  ALA A C   1 
ATOM   1065  O O   . ALA A 1 135 ? -39.70500 -62.76400 -1.29800  1.000 46.77000  ? 154  ALA A O   1 
ATOM   1066  C CB  . ALA A 1 135 ? -40.68400 -59.66400 -1.75300  1.000 32.68000  ? 154  ALA A CB  1 
ATOM   1067  N N   . LEU A 1 136 ? -38.58300 -61.72000 -2.93900  1.000 47.70000  ? 155  LEU A N   1 
ATOM   1068  C CA  . LEU A 1 136 ? -38.30600 -62.97300 -3.62600  1.000 46.73000  ? 155  LEU A CA  1 
ATOM   1069  C C   . LEU A 1 136 ? -37.44500 -63.88300 -2.75900  1.000 47.79000  ? 155  LEU A C   1 
ATOM   1070  O O   . LEU A 1 136 ? -37.61300 -65.10900 -2.77500  1.000 47.12000  ? 155  LEU A O   1 
ATOM   1071  C CB  . LEU A 1 136 ? -37.63500 -62.66300 -4.96300  1.000 42.50000  ? 155  LEU A CB  1 
ATOM   1072  C CG  . LEU A 1 136 ? -37.49600 -63.73900 -6.02900  1.000 42.75000  ? 155  LEU A CG  1 
ATOM   1073  C CD1 . LEU A 1 136 ? -38.87700 -64.22300 -6.40700  1.000 45.38000  ? 155  LEU A CD1 1 
ATOM   1074  C CD2 . LEU A 1 136 ? -36.82200 -63.13400 -7.23800  1.000 41.41000  ? 155  LEU A CD2 1 
ATOM   1075  N N   . ASP A 1 137 ? -36.55300 -63.28700 -1.96200  1.000 46.58000  ? 156  ASP A N   1 
ATOM   1076  C CA  . ASP A 1 137 ? -35.63600 -64.05000 -1.12200  1.000 49.69000  ? 156  ASP A CA  1 
ATOM   1077  C C   . ASP A 1 137 ? -36.36900 -64.68700 0.05300   1.000 47.72000  ? 156  ASP A C   1 
ATOM   1078  O O   . ASP A 1 137 ? -36.07800 -65.83000 0.42600   1.000 44.92000  ? 156  ASP A O   1 
ATOM   1079  C CB  . ASP A 1 137 ? -34.49800 -63.12800 -0.66200  1.000 47.22000  ? 156  ASP A CB  1 
ATOM   1080  C CG  . ASP A 1 137 ? -33.43600 -63.83900 0.16500   1.000 49.77000  ? 156  ASP A CG  1 
ATOM   1081  O OD1 . ASP A 1 137 ? -32.67700 -64.67500 -0.39500  1.000 46.20000  ? 156  ASP A OD1 1 
ATOM   1082  O OD2 . ASP A 1 137 ? -33.32900 -63.50600 1.37200   1.000 45.89000  ? 156  ASP A OD2 1 
ATOM   1083  N N   . LYS A 1 138 ? -37.34500 -63.98100 0.62900   1.000 52.63000  ? 157  LYS A N   1 
ATOM   1084  C CA  . LYS A 1 138 ? -38.17100 -64.58700 1.67000   1.000 49.45000  ? 157  LYS A CA  1 
ATOM   1085  C C   . LYS A 1 138 ? -38.82700 -65.86700 1.17000   1.000 47.31000  ? 157  LYS A C   1 
ATOM   1086  O O   . LYS A 1 138 ? -38.74200 -66.91800 1.81900   1.000 49.13000  ? 157  LYS A O   1 
ATOM   1087  C CB  . LYS A 1 138 ? -39.22000 -63.58900 2.15000   1.000 42.37000  ? 157  LYS A CB  1 
ATOM   1088  C CG  . LYS A 1 138 ? -38.61500 -62.34000 2.79100   1.000 58.14000  ? 157  LYS A CG  1 
ATOM   1089  C CD  . LYS A 1 138 ? -39.69200 -61.36100 3.22900   1.000 59.75000  ? 157  LYS A CD  1 
ATOM   1090  C CE  . LYS A 1 138 ? -39.07400 -60.10200 3.84300   1.000 58.28000  ? 157  LYS A CE  1 
ATOM   1091  N NZ  . LYS A 1 138 ? -38.10600 -59.41400 2.92200   1.000 54.75000  ? 157  LYS A NZ  1 
ATOM   1092  N N   . GLU A 1 139 ? -39.44700 -65.81200 -0.01000  1.000 40.87000  ? 158  GLU A N   1 
ATOM   1093  C CA  . GLU A 1 139 ? -40.06300 -67.01200 -0.56500  1.000 51.40000  ? 158  GLU A CA  1 
ATOM   1094  C C   . GLU A 1 139 ? -39.03900 -68.12000 -0.75500  1.000 53.16000  ? 158  GLU A C   1 
ATOM   1095  O O   . GLU A 1 139 ? -39.25300 -69.25900 -0.32600  1.000 52.89000  ? 158  GLU A O   1 
ATOM   1096  C CB  . GLU A 1 139 ? -40.77100 -66.69500 -1.88200  1.000 62.58000  ? 158  GLU A CB  1 
ATOM   1097  C CG  . GLU A 1 139 ? -42.10700 -66.01600 -1.66600  1.000 63.66000  ? 158  GLU A CG  1 
ATOM   1098  C CD  . GLU A 1 139 ? -42.88100 -65.81300 -2.94800  1.000 80.84000  ? 158  GLU A CD  1 
ATOM   1099  O OE1 . GLU A 1 139 ? -42.26600 -65.90200 -4.03500  1.000 84.28000  ? 158  GLU A OE1 1 
ATOM   1100  O OE2 . GLU A 1 139 ? -44.12300 -65.65300 -2.86200  1.000 93.26000  ? 158  GLU A OE2 1 
ATOM   1101  N N   . LEU A 1 140 ? -37.90100 -67.79600 -1.36500  1.000 54.57000  ? 159  LEU A N   1 
ATOM   1102  C CA  . LEU A 1 140 ? -36.89300 -68.81700 -1.62200  1.000 49.90000  ? 159  LEU A CA  1 
ATOM   1103  C C   . LEU A 1 140 ? -36.21700 -69.29100 -0.33700  1.000 50.44000  ? 159  LEU A C   1 
ATOM   1104  O O   . LEU A 1 140 ? -35.85800 -70.47200 -0.23100  1.000 49.13000  ? 159  LEU A O   1 
ATOM   1105  C CB  . LEU A 1 140 ? -35.88500 -68.27900 -2.63700  1.000 47.08000  ? 159  LEU A CB  1 
ATOM   1106  C CG  . LEU A 1 140 ? -36.53100 -68.19500 -4.02500  1.000 47.71000  ? 159  LEU A CG  1 
ATOM   1107  C CD1 . LEU A 1 140 ? -35.73400 -67.34200 -4.97700  1.000 35.49000  ? 159  LEU A CD1 1 
ATOM   1108  C CD2 . LEU A 1 140 ? -36.66200 -69.59800 -4.59100  1.000 44.98000  ? 159  LEU A CD2 1 
ATOM   1109  N N   . LYS A 1 141 ? -36.04700 -68.40700 0.65500   1.000 47.61000  ? 160  LYS A N   1 
ATOM   1110  C CA  . LYS A 1 141 ? -35.45500 -68.84400 1.91800   1.000 49.56000  ? 160  LYS A CA  1 
ATOM   1111  C C   . LYS A 1 141 ? -36.34200 -69.85400 2.63100   1.000 57.96000  ? 160  LYS A C   1 
ATOM   1112  O O   . LYS A 1 141 ? -35.83100 -70.74300 3.32100   1.000 60.52000  ? 160  LYS A O   1 
ATOM   1113  C CB  . LYS A 1 141 ? -35.15500 -67.64700 2.83200   1.000 49.23000  ? 160  LYS A CB  1 
ATOM   1114  C CG  . LYS A 1 141 ? -33.97200 -66.79400 2.37700   1.000 44.07000  ? 160  LYS A CG  1 
ATOM   1115  C CD  . LYS A 1 141 ? -32.63700 -67.49000 2.63700   1.000 44.24000  ? 160  LYS A CD  1 
ATOM   1116  C CE  . LYS A 1 141 ? -31.47100 -66.73100 2.00500   1.000 40.25000  ? 160  LYS A CE  1 
ATOM   1117  N NZ  . LYS A 1 141 ? -31.30100 -65.35800 2.55100   1.000 41.35000  ? 160  LYS A NZ  1 
ATOM   1118  N N   . ALA A 1 142 ? -37.66500 -69.75200 2.46700   1.000 52.65000  ? 161  ALA A N   1 
ATOM   1119  C CA  . ALA A 1 142 ? -38.54000 -70.75400 3.06700   1.000 58.10000  ? 161  ALA A CA  1 
ATOM   1120  C C   . ALA A 1 142 ? -38.44200 -72.10600 2.36800   1.000 62.49000  ? 161  ALA A C   1 
ATOM   1121  O O   . ALA A 1 142 ? -38.90500 -73.10600 2.92400   1.000 58.20000  ? 161  ALA A O   1 
ATOM   1122  C CB  . ALA A 1 142 ? -39.99700 -70.26800 3.07100   1.000 41.11000  ? 161  ALA A CB  1 
ATOM   1123  N N   . LYS A 1 143 ? -37.83600 -72.16600 1.18200   1.000 63.16000  ? 162  LYS A N   1 
ATOM   1124  C CA  . LYS A 1 143 ? -37.58600 -73.42300 0.48700   1.000 62.82000  ? 162  LYS A CA  1 
ATOM   1125  C C   . LYS A 1 143 ? -36.18600 -73.96600 0.74500   1.000 56.28000  ? 162  LYS A C   1 
ATOM   1126  O O   . LYS A 1 143 ? -35.82000 -75.00000 0.18600   1.000 57.42000  ? 162  LYS A O   1 
ATOM   1127  C CB  . LYS A 1 143 ? -37.80600 -73.25700 -1.02100  1.000 60.39000  ? 162  LYS A CB  1 
ATOM   1128  C CG  . LYS A 1 143 ? -39.23400 -72.89700 -1.44000  1.000 63.35000  ? 162  LYS A CG  1 
ATOM   1129  C CD  . LYS A 1 143 ? -39.36300 -72.88700 -2.96100  1.000 70.45000  ? 162  LYS A CD  1 
ATOM   1130  C CE  . LYS A 1 143 ? -40.79100 -72.63800 -3.42300  1.000 82.61000  ? 162  LYS A CE  1 
ATOM   1131  N NZ  . LYS A 1 143 ? -41.23400 -71.23300 -3.17800  1.000 92.87000  ? 162  LYS A NZ  1 
ATOM   1132  N N   . GLY A 1 144 ? -35.39600 -73.30200 1.58100   1.000 49.79000  ? 163  GLY A N   1 
ATOM   1133  C CA  . GLY A 1 144 ? -34.02300 -73.72000 1.76900   1.000 55.50000  ? 163  GLY A CA  1 
ATOM   1134  C C   . GLY A 1 144 ? -33.07500 -73.24600 0.69600   1.000 53.96000  ? 163  GLY A C   1 
ATOM   1135  O O   . GLY A 1 144 ? -31.98700 -73.81400 0.54700   1.000 53.71000  ? 163  GLY A O   1 
ATOM   1136  N N   . LYS A 1 145 ? -33.45700 -72.22600 -0.07000  1.000 47.23000  ? 164  LYS A N   1 
ATOM   1137  C CA  . LYS A 1 145 ? -32.63000 -71.68500 -1.14200  1.000 48.44000  ? 164  LYS A CA  1 
ATOM   1138  C C   . LYS A 1 145 ? -32.63900 -70.16200 -1.03300  1.000 43.82000  ? 164  LYS A C   1 
ATOM   1139  O O   . LYS A 1 145 ? -33.24100 -69.60200 -0.11400  1.000 48.76000  ? 164  LYS A O   1 
ATOM   1140  C CB  . LYS A 1 145 ? -33.13000 -72.21300 -2.49400  1.000 46.42000  ? 164  LYS A CB  1 
ATOM   1141  C CG  . LYS A 1 145 ? -32.97100 -73.72900 -2.56500  1.000 46.69000  ? 164  LYS A CG  1 
ATOM   1142  C CD  . LYS A 1 145 ? -33.34500 -74.33700 -3.88500  1.000 49.12000  ? 164  LYS A CD  1 
ATOM   1143  C CE  . LYS A 1 145 ? -33.21500 -75.86000 -3.82000  1.000 54.40000  ? 164  LYS A CE  1 
ATOM   1144  N NZ  . LYS A 1 145 ? -31.80300 -76.32100 -3.61800  1.000 50.02000  ? 164  LYS A NZ  1 
ATOM   1145  N N   . SER A 1 146 ? -31.93200 -69.47800 -1.93000  1.000 41.94000  ? 165  SER A N   1 
ATOM   1146  C CA  . SER A 1 146 ? -31.86700 -68.02300 -1.87500  1.000 40.83000  ? 165  SER A CA  1 
ATOM   1147  C C   . SER A 1 146 ? -32.08600 -67.41800 -3.25600  1.000 32.56000  ? 165  SER A C   1 
ATOM   1148  O O   . SER A 1 146 ? -31.93500 -68.08000 -4.28700  1.000 37.65000  ? 165  SER A O   1 
ATOM   1149  C CB  . SER A 1 146 ? -30.52800 -67.54200 -1.31500  1.000 37.06000  ? 165  SER A CB  1 
ATOM   1150  O OG  . SER A 1 146 ? -29.49000 -67.87400 -2.21000  1.000 42.06000  ? 165  SER A OG  1 
ATOM   1151  N N   . ALA A 1 147 ? -32.43900 -66.13100 -3.26000  1.000 35.85000  ? 166  ALA A N   1 
ATOM   1152  C CA  . ALA A 1 147 ? -32.68000 -65.42200 -4.51500  1.000 42.35000  ? 166  ALA A CA  1 
ATOM   1153  C C   . ALA A 1 147 ? -31.39100 -65.21600 -5.30300  1.000 42.57000  ? 166  ALA A C   1 
ATOM   1154  O O   . ALA A 1 147 ? -31.27900 -65.63900 -6.46000  1.000 38.78000  ? 166  ALA A O   1 
ATOM   1155  C CB  . ALA A 1 147 ? -33.35000 -64.07400 -4.23500  1.000 38.78000  ? 166  ALA A CB  1 
ATOM   1156  N N   . LEU A 1 148 ? -30.40400 -64.56300 -4.69400  1.000 36.72000  ? 167  LEU A N   1 
ATOM   1157  C CA  . LEU A 1 148 ? -29.31500 -63.96700 -5.45800  1.000 40.59000  ? 167  LEU A CA  1 
ATOM   1158  C C   . LEU A 1 148 ? -27.99900 -64.10300 -4.72500  1.000 37.77000  ? 167  LEU A C   1 
ATOM   1159  O O   . LEU A 1 148 ? -27.90400 -63.73300 -3.55400  1.000 38.17000  ? 167  LEU A O   1 
ATOM   1160  C CB  . LEU A 1 148 ? -29.58500 -62.48400 -5.72100  1.000 39.80000  ? 167  LEU A CB  1 
ATOM   1161  C CG  . LEU A 1 148 ? -28.49400 -61.74100 -6.48500  1.000 38.67000  ? 167  LEU A CG  1 
ATOM   1162  C CD1 . LEU A 1 148 ? -28.30800 -62.35100 -7.87400  1.000 34.10000  ? 167  LEU A CD1 1 
ATOM   1163  C CD2 . LEU A 1 148 ? -28.84000 -60.25800 -6.56700  1.000 31.78000  ? 167  LEU A CD2 1 
ATOM   1164  N N   . MET A 1 149 ? -26.98800 -64.61500 -5.42400  1.000 43.88000  ? 168  MET A N   1 
ATOM   1165  C CA  . MET A 1 149 ? -25.61600 -64.59800 -4.93100  1.000 39.70000  ? 168  MET A CA  1 
ATOM   1166  C C   . MET A 1 149 ? -24.68400 -64.22500 -6.06900  1.000 34.92000  ? 168  MET A C   1 
ATOM   1167  O O   . MET A 1 149 ? -24.67900 -64.88800 -7.11200  1.000 39.17000  ? 168  MET A O   1 
ATOM   1168  C CB  . MET A 1 149 ? -25.21500 -65.95000 -4.35000  1.000 42.16000  ? 168  MET A CB  1 
ATOM   1169  C CG  . MET A 1 149 ? -25.97700 -66.29700 -3.09500  1.000 48.07000  ? 168  MET A CG  1 
ATOM   1170  S SD  . MET A 1 149 ? -25.28700 -67.78300 -2.38800  1.000 64.12000  ? 168  MET A SD  1 
ATOM   1171  C CE  . MET A 1 149 ? -23.69400 -67.10900 -1.89900  1.000 47.69000  ? 168  MET A CE  1 
ATOM   1172  N N   . PHE A 1 150 ? -23.89500 -63.17400 -5.86900  1.000 29.47000  ? 169  PHE A N   1 
ATOM   1173  C CA  . PHE A 1 150 ? -22.84600 -62.81600 -6.80700  1.000 30.91000  ? 169  PHE A CA  1 
ATOM   1174  C C   . PHE A 1 150 ? -21.65000 -62.27100 -6.02900  1.000 37.25000  ? 169  PHE A C   1 
ATOM   1175  O O   . PHE A 1 150 ? -21.71500 -62.03800 -4.81800  1.000 36.78000  ? 169  PHE A O   1 
ATOM   1176  C CB  . PHE A 1 150 ? -23.36100 -61.82900 -7.87200  1.000 27.85000  ? 169  PHE A CB  1 
ATOM   1177  C CG  . PHE A 1 150 ? -23.73900 -60.47700 -7.33300  1.000 28.98000  ? 169  PHE A CG  1 
ATOM   1178  C CD1 . PHE A 1 150 ? -24.94700 -60.28500 -6.68900  1.000 33.54000  ? 169  PHE A CD1 1 
ATOM   1179  C CD2 . PHE A 1 150 ? -22.92100 -59.38300 -7.54100  1.000 26.90000  ? 169  PHE A CD2 1 
ATOM   1180  C CE1 . PHE A 1 150 ? -25.30900 -59.03300 -6.20800  1.000 32.71000  ? 169  PHE A CE1 1 
ATOM   1181  C CE2 . PHE A 1 150 ? -23.28000 -58.12800 -7.06700  1.000 26.85000  ? 169  PHE A CE2 1 
ATOM   1182  C CZ  . PHE A 1 150 ? -24.47600 -57.95600 -6.40200  1.000 30.70000  ? 169  PHE A CZ  1 
ATOM   1183  N N   . ASN A 1 151 ? -20.53500 -62.09800 -6.73600  1.000 29.91000  ? 170  ASN A N   1 
ATOM   1184  C CA  . ASN A 1 151 ? -19.30000 -61.59400 -6.14700  1.000 36.16000  ? 170  ASN A CA  1 
ATOM   1185  C C   . ASN A 1 151 ? -19.46900 -60.18000 -5.60000  1.000 32.52000  ? 170  ASN A C   1 
ATOM   1186  O O   . ASN A 1 151 ? -19.55600 -59.22600 -6.37100  1.000 34.29000  ? 170  ASN A O   1 
ATOM   1187  C CB  . ASN A 1 151 ? -18.18900 -61.62900 -7.20700  1.000 33.65000  ? 170  ASN A CB  1 
ATOM   1188  C CG  . ASN A 1 151 ? -16.82500 -61.23400 -6.65800  1.000 42.25000  ? 170  ASN A CG  1 
ATOM   1189  O OD1 . ASN A 1 151 ? -16.66600 -60.95000 -5.46600  1.000 37.26000  ? 170  ASN A OD1 1 
ATOM   1190  N ND2 . ASN A 1 151 ? -15.83400 -61.19000 -7.54200  1.000 42.16000  ? 170  ASN A ND2 1 
ATOM   1191  N N   . LEU A 1 152 ? -19.48800 -60.01600 -4.28000  1.000 32.68000  ? 171  LEU A N   1 
ATOM   1192  C CA  . LEU A 1 152 ? -19.59500 -58.68700 -3.68900  1.000 32.77000  ? 171  LEU A CA  1 
ATOM   1193  C C   . LEU A 1 152 ? -18.23700 -58.03400 -3.43400  1.000 39.70000  ? 171  LEU A C   1 
ATOM   1194  O O   . LEU A 1 152 ? -18.18800 -56.85400 -3.06800  1.000 40.01000  ? 171  LEU A O   1 
ATOM   1195  C CB  . LEU A 1 152 ? -20.38000 -58.74600 -2.37600  1.000 28.50000  ? 171  LEU A CB  1 
ATOM   1196  C CG  . LEU A 1 152 ? -21.80400 -59.28500 -2.52400  1.000 38.33000  ? 171  LEU A CG  1 
ATOM   1197  C CD1 . LEU A 1 152 ? -22.56100 -59.22600 -1.21000  1.000 29.84000  ? 171  LEU A CD1 1 
ATOM   1198  C CD2 . LEU A 1 152 ? -22.56400 -58.57200 -3.63400  1.000 30.84000  ? 171  LEU A CD2 1 
ATOM   1199  N N   . GLN A 1 153 ? -17.13600 -58.76300 -3.61800  1.000 36.84000  ? 172  GLN A N   1 
ATOM   1200  C CA  . GLN A 1 153 ? -15.83300 -58.25400 -3.21600  1.000 34.69000  ? 172  GLN A CA  1 
ATOM   1201  C C   . GLN A 1 153 ? -15.26500 -57.25300 -4.20800  1.000 40.19000  ? 172  GLN A C   1 
ATOM   1202  O O   . GLN A 1 153 ? -14.52000 -56.35400 -3.80400  1.000 40.61000  ? 172  GLN A O   1 
ATOM   1203  C CB  . GLN A 1 153 ? -14.85600 -59.41300 -3.03900  1.000 32.65000  ? 172  GLN A CB  1 
ATOM   1204  C CG  . GLN A 1 153 ? -15.38000 -60.47900 -2.10100  1.000 35.10000  ? 172  GLN A CG  1 
ATOM   1205  C CD  . GLN A 1 153 ? -15.76800 -59.91000 -0.75200  1.000 39.90000  ? 172  GLN A CD  1 
ATOM   1206  O OE1 . GLN A 1 153 ? -15.06300 -59.07100 -0.19600  1.000 35.80000  ? 172  GLN A OE1 1 
ATOM   1207  N NE2 . GLN A 1 153 ? -16.92300 -60.33200 -0.24000  1.000 40.83000  ? 172  GLN A NE2 1 
ATOM   1208  N N   . GLU A 1 154 ? -15.59800 -57.39100 -5.49700  1.000 37.96000  ? 173  GLU A N   1 
ATOM   1209  C CA  . GLU A 1 154 ? -14.95600 -56.62200 -6.55100  1.000 33.30000  ? 173  GLU A CA  1 
ATOM   1210  C C   . GLU A 1 154 ? -15.94000 -55.63200 -7.16300  1.000 34.30000  ? 173  GLU A C   1 
ATOM   1211  O O   . GLU A 1 154 ? -17.01100 -56.04400 -7.63300  1.000 36.62000  ? 173  GLU A O   1 
ATOM   1212  C CB  . GLU A 1 154 ? -14.39900 -57.56500 -7.61900  1.000 35.33000  ? 173  GLU A CB  1 
ATOM   1213  C CG  . GLU A 1 154 ? -13.46700 -58.64400 -7.03900  1.000 34.99000  ? 173  GLU A CG  1 
ATOM   1214  C CD  . GLU A 1 154 ? -12.27500 -58.07100 -6.25900  1.000 46.36000  ? 173  GLU A CD  1 
ATOM   1215  O OE1 . GLU A 1 154 ? -11.75600 -56.98900 -6.62400  1.000 42.21000  ? 173  GLU A OE1 1 
ATOM   1216  O OE2 . GLU A 1 154 ? -11.87100 -58.70100 -5.25700  1.000 46.72000  ? 173  GLU A OE2 1 
ATOM   1217  N N   . PRO A 1 155 ? -15.62100 -54.33600 -7.20000  1.000 33.98000  ? 174  PRO A N   1 
ATOM   1218  C CA  . PRO A 1 155 ? -16.60600 -53.34500 -7.66900  1.000 30.00000  ? 174  PRO A CA  1 
ATOM   1219  C C   . PRO A 1 155 ? -17.06800 -53.56700 -9.09200  1.000 29.11000  ? 174  PRO A C   1 
ATOM   1220  O O   . PRO A 1 155 ? -18.12100 -53.04900 -9.47300  1.000 36.37000  ? 174  PRO A O   1 
ATOM   1221  C CB  . PRO A 1 155 ? -15.85000 -52.01600 -7.54800  1.000 34.85000  ? 174  PRO A CB  1 
ATOM   1222  C CG  . PRO A 1 155 ? -14.76100 -52.28500 -6.57800  1.000 29.20000  ? 174  PRO A CG  1 
ATOM   1223  C CD  . PRO A 1 155 ? -14.35700 -53.70600 -6.79900  1.000 34.91000  ? 174  PRO A CD  1 
ATOM   1224  N N   . TYR A 1 156 ? -16.30000 -54.29600 -9.89900  1.000 34.07000  ? 175  TYR A N   1 
ATOM   1225  C CA  . TYR A 1 156 ? -16.73600 -54.64900 -11.24500 1.000 30.16000  ? 175  TYR A CA  1 
ATOM   1226  C C   . TYR A 1 156 ? -18.09800 -55.32100 -11.21800 1.000 32.90000  ? 175  TYR A C   1 
ATOM   1227  O O   . TYR A 1 156 ? -18.90200 -55.14500 -12.14100 1.000 28.72000  ? 175  TYR A O   1 
ATOM   1228  C CB  . TYR A 1 156 ? -15.70500 -55.57500 -11.89000 1.000 27.92000  ? 175  TYR A CB  1 
ATOM   1229  C CG  . TYR A 1 156 ? -16.05800 -56.04600 -13.27600 1.000 30.32000  ? 175  TYR A CG  1 
ATOM   1230  C CD1 . TYR A 1 156 ? -15.73400 -55.29400 -14.39900 1.000 32.22000  ? 175  TYR A CD1 1 
ATOM   1231  C CD2 . TYR A 1 156 ? -16.73900 -57.24300 -13.45900 1.000 30.74000  ? 175  TYR A CD2 1 
ATOM   1232  C CE1 . TYR A 1 156 ? -16.06000 -55.74200 -15.67200 1.000 33.18000  ? 175  TYR A CE1 1 
ATOM   1233  C CE2 . TYR A 1 156 ? -17.07800 -57.69000 -14.71800 1.000 32.39000  ? 175  TYR A CE2 1 
ATOM   1234  C CZ  . TYR A 1 156 ? -16.74200 -56.94000 -15.81800 1.000 34.92000  ? 175  TYR A CZ  1 
ATOM   1235  O OH  . TYR A 1 156 ? -17.08800 -57.40500 -17.06300 1.000 35.96000  ? 175  TYR A OH  1 
ATOM   1236  N N   . PHE A 1 157 ? -18.36800 -56.11500 -10.17700 1.000 26.85000  ? 176  PHE A N   1 
ATOM   1237  C CA  . PHE A 1 157 ? -19.63800 -56.81400 -10.05500 1.000 30.54000  ? 176  PHE A CA  1 
ATOM   1238  C C   . PHE A 1 157 ? -20.71000 -55.98800 -9.35900  1.000 31.59000  ? 176  PHE A C   1 
ATOM   1239  O O   . PHE A 1 157 ? -21.89500 -56.13400 -9.68000  1.000 34.04000  ? 176  PHE A O   1 
ATOM   1240  C CB  . PHE A 1 157 ? -19.43800 -58.13800 -9.31600  1.000 29.00000  ? 176  PHE A CB  1 
ATOM   1241  C CG  . PHE A 1 157 ? -18.70800 -59.17100 -10.12800 1.000 31.05000  ? 176  PHE A CG  1 
ATOM   1242  C CD1 . PHE A 1 157 ? -19.40400 -60.01000 -10.98000 1.000 36.08000  ? 176  PHE A CD1 1 
ATOM   1243  C CD2 . PHE A 1 157 ? -17.33300 -59.26100 -10.08800 1.000 33.54000  ? 176  PHE A CD2 1 
ATOM   1244  C CE1 . PHE A 1 157 ? -18.74700 -60.94900 -11.74700 1.000 31.33000  ? 176  PHE A CE1 1 
ATOM   1245  C CE2 . PHE A 1 157 ? -16.67000 -60.19600 -10.85700 1.000 35.26000  ? 176  PHE A CE2 1 
ATOM   1246  C CZ  . PHE A 1 157 ? -17.39000 -61.04200 -11.68600 1.000 34.87000  ? 176  PHE A CZ  1 
ATOM   1247  N N   . THR A 1 158 ? -20.33200 -55.10800 -8.44000  1.000 29.20000  ? 177  THR A N   1 
ATOM   1248  C CA  . THR A 1 158 ? -21.31500 -54.34400 -7.68200  1.000 30.79000  ? 177  THR A CA  1 
ATOM   1249  C C   . THR A 1 158 ? -21.62000 -52.99100 -8.30200  1.000 34.39000  ? 177  THR A C   1 
ATOM   1250  O O   . THR A 1 158 ? -22.66400 -52.40400 -7.98900  1.000 35.11000  ? 177  THR A O   1 
ATOM   1251  C CB  . THR A 1 158 ? -20.84000 -54.13600 -6.23500  1.000 35.31000  ? 177  THR A CB  1 
ATOM   1252  O OG1 . THR A 1 158 ? -19.58400 -53.43500 -6.22500  1.000 27.87000  ? 177  THR A OG1 1 
ATOM   1253  C CG2 . THR A 1 158 ? -20.68600 -55.47700 -5.52200  1.000 30.73000  ? 177  THR A CG2 1 
ATOM   1254  N N   . TRP A 1 159 ? -20.74800 -52.48600 -9.17300  1.000 27.15000  ? 178  TRP A N   1 
ATOM   1255  C CA  . TRP A 1 159 ? -21.00300 -51.17900 -9.76500  1.000 28.15000  ? 178  TRP A CA  1 
ATOM   1256  C C   . TRP A 1 159 ? -22.24800 -51.11100 -10.65800 1.000 33.47000  ? 178  TRP A C   1 
ATOM   1257  O O   . TRP A 1 159 ? -22.81900 -50.01100 -10.75500 1.000 33.77000  ? 178  TRP A O   1 
ATOM   1258  C CB  . TRP A 1 159 ? -19.76700 -50.71800 -10.54700 1.000 33.03000  ? 178  TRP A CB  1 
ATOM   1259  C CG  . TRP A 1 159 ? -19.85100 -49.29200 -10.96700 1.000 32.42000  ? 178  TRP A CG  1 
ATOM   1260  C CD1 . TRP A 1 159 ? -20.07700 -48.81200 -12.22700 1.000 30.07000  ? 178  TRP A CD1 1 
ATOM   1261  C CD2 . TRP A 1 159 ? -19.72800 -48.14700 -10.11500 1.000 32.77000  ? 178  TRP A CD2 1 
ATOM   1262  N NE1 . TRP A 1 159 ? -20.09200 -47.43200 -12.21000 1.000 32.86000  ? 178  TRP A NE1 1 
ATOM   1263  C CE2 . TRP A 1 159 ? -19.88200 -47.00500 -10.92200 1.000 37.52000  ? 178  TRP A CE2 1 
ATOM   1264  C CE3 . TRP A 1 159 ? -19.50200 -47.98000 -8.74500  1.000 34.06000  ? 178  TRP A CE3 1 
ATOM   1265  C CZ2 . TRP A 1 159 ? -19.81300 -45.71400 -10.40300 1.000 35.20000  ? 178  TRP A CZ2 1 
ATOM   1266  C CZ3 . TRP A 1 159 ? -19.43100 -46.69700 -8.23600  1.000 31.95000  ? 178  TRP A CZ3 1 
ATOM   1267  C CH2 . TRP A 1 159 ? -19.59200 -45.58400 -9.06000  1.000 34.12000  ? 178  TRP A CH2 1 
ATOM   1268  N N   . PRO A 1 160 ? -22.70100 -52.17700 -11.34700 1.000 30.92000  ? 179  PRO A N   1 
ATOM   1269  C CA  . PRO A 1 160 ? -23.94500 -52.03200 -12.13900 1.000 33.64000  ? 179  PRO A CA  1 
ATOM   1270  C C   . PRO A 1 160 ? -25.13700 -51.53200 -11.33500 1.000 35.18000  ? 179  PRO A C   1 
ATOM   1271  O O   . PRO A 1 160 ? -25.88600 -50.66400 -11.81100 1.000 30.87000  ? 179  PRO A O   1 
ATOM   1272  C CB  . PRO A 1 160 ? -24.18300 -53.45200 -12.67100 1.000 29.22000  ? 179  PRO A CB  1 
ATOM   1273  C CG  . PRO A 1 160 ? -22.81800 -54.05300 -12.73700 1.000 28.28000  ? 179  PRO A CG  1 
ATOM   1274  C CD  . PRO A 1 160 ? -22.06400 -53.49300 -11.57600 1.000 28.30000  ? 179  PRO A CD  1 
ATOM   1275  N N   . LEU A 1 161 ? -25.32500 -52.04700 -10.11600 1.000 31.73000  ? 180  LEU A N   1 
ATOM   1276  C CA  . LEU A 1 161 ? -26.37400 -51.53500 -9.24000  1.000 26.04000  ? 180  LEU A CA  1 
ATOM   1277  C C   . LEU A 1 161 ? -26.08000 -50.11000 -8.79600  1.000 34.26000  ? 180  LEU A C   1 
ATOM   1278  O O   . LEU A 1 161 ? -26.97700 -49.25900 -8.76200  1.000 38.41000  ? 180  LEU A O   1 
ATOM   1279  C CB  . LEU A 1 161 ? -26.52300 -52.44500 -8.02800  1.000 29.44000  ? 180  LEU A CB  1 
ATOM   1280  C CG  . LEU A 1 161 ? -27.43300 -51.93700 -6.90400  1.000 35.72000  ? 180  LEU A CG  1 
ATOM   1281  C CD1 . LEU A 1 161 ? -28.87200 -51.66300 -7.37500  1.000 36.81000  ? 180  LEU A CD1 1 
ATOM   1282  C CD2 . LEU A 1 161 ? -27.42800 -52.95000 -5.77200  1.000 29.64000  ? 180  LEU A CD2 1 
ATOM   1283  N N   . ILE A 1 162 ? -24.82700 -49.84200 -8.42800  1.000 31.13000  ? 181  ILE A N   1 
ATOM   1284  C CA  . ILE A 1 162 ? -24.46400 -48.54900 -7.86600  1.000 29.77000  ? 181  ILE A CA  1 
ATOM   1285  C C   . ILE A 1 162 ? -24.60800 -47.44200 -8.90100  1.000 31.21000  ? 181  ILE A C   1 
ATOM   1286  O O   . ILE A 1 162 ? -24.98300 -46.31400 -8.56700  1.000 36.96000  ? 181  ILE A O   1 
ATOM   1287  C CB  . ILE A 1 162 ? -23.04000 -48.65000 -7.29100  1.000 31.10000  ? 181  ILE A CB  1 
ATOM   1288  C CG1 . ILE A 1 162 ? -23.03800 -49.68900 -6.17300  1.000 31.27000  ? 181  ILE A CG1 1 
ATOM   1289  C CG2 . ILE A 1 162 ? -22.55700 -47.31200 -6.75800  1.000 33.07000  ? 181  ILE A CG2 1 
ATOM   1290  C CD1 . ILE A 1 162 ? -21.69300 -50.06400 -5.65500  1.000 32.12000  ? 181  ILE A CD1 1 
ATOM   1291  N N   . ALA A 1 163 ? -24.31700 -47.73600 -10.16600 1.000 34.77000  ? 182  ALA A N   1 
ATOM   1292  C CA  . ALA A 1 163 ? -24.38400 -46.73000 -11.21500 1.000 34.28000  ? 182  ALA A CA  1 
ATOM   1293  C C   . ALA A 1 163 ? -25.78900 -46.52900 -11.75300 1.000 37.32000  ? 182  ALA A C   1 
ATOM   1294  O O   . ALA A 1 163 ? -26.02900 -45.51400 -12.41900 1.000 38.16000  ? 182  ALA A O   1 
ATOM   1295  C CB  . ALA A 1 163 ? -23.46700 -47.11000 -12.37900 1.000 31.50000  ? 182  ALA A CB  1 
ATOM   1296  N N   . ALA A 1 164 ? -26.71200 -47.45500 -11.46400 1.000 28.13000  ? 183  ALA A N   1 
ATOM   1297  C CA  . ALA A 1 164 ? -28.02400 -47.42900 -12.10100 1.000 30.95000  ? 183  ALA A CA  1 
ATOM   1298  C C   . ALA A 1 164 ? -28.65900 -46.05200 -12.01400 1.000 33.58000  ? 183  ALA A C   1 
ATOM   1299  O O   . ALA A 1 164 ? -29.15500 -45.52000 -13.01200 1.000 35.26000  ? 183  ALA A O   1 
ATOM   1300  C CB  . ALA A 1 164 ? -28.93800 -48.47500 -11.46700 1.000 33.88000  ? 183  ALA A CB  1 
ATOM   1301  N N   . ASP A 1 165 ? -28.63300 -45.43800 -10.84100 1.000 34.02000  ? 184  ASP A N   1 
ATOM   1302  C CA  . ASP A 1 165 ? -29.32000 -44.16900 -10.69200 1.000 35.71000  ? 184  ASP A CA  1 
ATOM   1303  C C   . ASP A 1 165 ? -28.39000 -42.96900 -10.80600 1.000 37.70000  ? 184  ASP A C   1 
ATOM   1304  O O   . ASP A 1 165 ? -28.80900 -41.85100 -10.48700 1.000 38.43000  ? 184  ASP A O   1 
ATOM   1305  C CB  . ASP A 1 165 ? -30.06800 -44.10900 -9.36600  1.000 40.47000  ? 184  ASP A CB  1 
ATOM   1306  C CG  . ASP A 1 165 ? -31.16800 -43.08100 -9.38900  1.000 48.23000  ? 184  ASP A CG  1 
ATOM   1307  O OD1 . ASP A 1 165 ? -31.49800 -42.59600 -10.49600 1.000 56.87000  ? 184  ASP A OD1 1 
ATOM   1308  O OD2 . ASP A 1 165 ? -31.66200 -42.71600 -8.30600  1.000 59.75000  ? 184  ASP A OD2 1 
ATOM   1309  N N   . GLY A 1 166 ? -27.14600 -43.15900 -11.24300 1.000 35.72000  ? 185  GLY A N   1 
ATOM   1310  C CA  . GLY A 1 166 ? -26.30200 -41.99900 -11.48500 1.000 34.06000  ? 185  GLY A CA  1 
ATOM   1311  C C   . GLY A 1 166 ? -24.81200 -42.08800 -11.18400 1.000 39.09000  ? 185  GLY A C   1 
ATOM   1312  O O   . GLY A 1 166 ? -24.08700 -41.13000 -11.45200 1.000 37.94000  ? 185  GLY A O   1 
ATOM   1313  N N   . GLY A 1 167 ? -24.32600 -43.20100 -10.63400 1.000 37.79000  ? 186  GLY A N   1 
ATOM   1314  C CA  . GLY A 1 167 ? -22.89900 -43.34600 -10.42000 1.000 36.56000  ? 186  GLY A CA  1 
ATOM   1315  C C   . GLY A 1 167 ? -22.13800 -43.42800 -11.73300 1.000 42.40000  ? 186  GLY A C   1 
ATOM   1316  O O   . GLY A 1 167 ? -22.63200 -43.91600 -12.74200 1.000 38.43000  ? 186  GLY A O   1 
ATOM   1317  N N   . TYR A 1 168 ? -20.90700 -42.92300 -11.72700 1.000 39.47000  ? 187  TYR A N   1 
ATOM   1318  C CA  . TYR A 1 168 ? -19.97700 -43.11700 -12.83700 1.000 34.20000  ? 187  TYR A CA  1 
ATOM   1319  C C   . TYR A 1 168 ? -18.54700 -42.99700 -12.34600 1.000 36.64000  ? 187  TYR A C   1 
ATOM   1320  O O   . TYR A 1 168 ? -18.28100 -42.42300 -11.29600 1.000 36.05000  ? 187  TYR A O   1 
ATOM   1321  C CB  . TYR A 1 168 ? -20.27600 -42.15600 -14.01700 1.000 30.33000  ? 187  TYR A CB  1 
ATOM   1322  C CG  . TYR A 1 168 ? -20.31500 -40.67500 -13.67100 1.000 35.48000  ? 187  TYR A CG  1 
ATOM   1323  C CD1 . TYR A 1 168 ? -21.53600 -40.08700 -13.28900 1.000 31.15000  ? 187  TYR A CD1 1 
ATOM   1324  C CD2 . TYR A 1 168 ? -19.20600 -39.87500 -13.74300 1.000 32.92000  ? 187  TYR A CD2 1 
ATOM   1325  C CE1 . TYR A 1 168 ? -21.60000 -38.72900 -12.99000 1.000 28.45000  ? 187  TYR A CE1 1 
ATOM   1326  C CE2 . TYR A 1 168 ? -19.25400 -38.50800 -13.44500 1.000 37.23000  ? 187  TYR A CE2 1 
ATOM   1327  C CZ  . TYR A 1 168 ? -20.48100 -37.94300 -13.06600 1.000 38.49000  ? 187  TYR A CZ  1 
ATOM   1328  O OH  . TYR A 1 168 ? -20.61700 -36.60000 -12.76000 1.000 38.71000  ? 187  TYR A OH  1 
ATOM   1329  N N   . ALA A 1 169 ? -17.62600 -43.55800 -13.13300 1.000 32.92000  ? 188  ALA A N   1 
ATOM   1330  C CA  . ALA A 1 169 ? -16.21100 -43.51300 -12.78200 1.000 29.79000  ? 188  ALA A CA  1 
ATOM   1331  C C   . ALA A 1 169 ? -15.59300 -42.18400 -13.20700 1.000 34.95000  ? 188  ALA A C   1 
ATOM   1332  O O   . ALA A 1 169 ? -15.21900 -41.35900 -12.36600 1.000 36.83000  ? 188  ALA A O   1 
ATOM   1333  C CB  . ALA A 1 169 ? -15.47200 -44.68600 -13.42600 1.000 31.89000  ? 188  ALA A CB  1 
ATOM   1334  N N   . PHE A 1 170 ? -15.53300 -41.93600 -14.50900 1.000 34.04000  ? 189  PHE A N   1 
ATOM   1335  C CA  . PHE A 1 170 ? -15.10800 -40.64400 -15.02800 1.000 38.59000  ? 189  PHE A CA  1 
ATOM   1336  C C   . PHE A 1 170 ? -16.08300 -40.22300 -16.11800 1.000 33.36000  ? 189  PHE A C   1 
ATOM   1337  O O   . PHE A 1 170 ? -16.52500 -41.05000 -16.92500 1.000 32.72000  ? 189  PHE A O   1 
ATOM   1338  C CB  . PHE A 1 170 ? -13.66800 -40.69500 -15.57900 1.000 32.63000  ? 189  PHE A CB  1 
ATOM   1339  C CG  . PHE A 1 170 ? -12.64300 -41.11100 -14.55800 1.000 33.04000  ? 189  PHE A CG  1 
ATOM   1340  C CD1 . PHE A 1 170 ? -12.27100 -40.25100 -13.54000 1.000 35.32000  ? 189  PHE A CD1 1 
ATOM   1341  C CD2 . PHE A 1 170 ? -12.03900 -42.35900 -14.63400 1.000 31.68000  ? 189  PHE A CD2 1 
ATOM   1342  C CE1 . PHE A 1 170 ? -11.34000 -40.64000 -12.59300 1.000 33.34000  ? 189  PHE A CE1 1 
ATOM   1343  C CE2 . PHE A 1 170 ? -11.09600 -42.75100 -13.70300 1.000 37.93000  ? 189  PHE A CE2 1 
ATOM   1344  C CZ  . PHE A 1 170 ? -10.74500 -41.89200 -12.67600 1.000 33.32000  ? 189  PHE A CZ  1 
ATOM   1345  N N   . LYS A 1 171 ? -16.40900 -38.93500 -16.15200 1.000 33.03000  ? 190  LYS A N   1 
ATOM   1346  C CA  . LYS A 1 171 ? -17.38200 -38.47300 -17.13000 1.000 37.41000  ? 190  LYS A CA  1 
ATOM   1347  C C   . LYS A 1 171 ? -16.81900 -38.63100 -18.53500 1.000 32.92000  ? 190  LYS A C   1 
ATOM   1348  O O   . LYS A 1 171 ? -15.68900 -38.24600 -18.80600 1.000 36.10000  ? 190  LYS A O   1 
ATOM   1349  C CB  . LYS A 1 171 ? -17.73700 -37.00600 -16.90100 1.000 39.74000  ? 190  LYS A CB  1 
ATOM   1350  C CG  . LYS A 1 171 ? -18.98800 -36.66800 -17.64700 1.000 36.14000  ? 190  LYS A CG  1 
ATOM   1351  C CD  . LYS A 1 171 ? -20.13500 -37.37900 -16.92800 1.000 46.21000  ? 190  LYS A CD  1 
ATOM   1352  C CE  . LYS A 1 171 ? -21.40500 -37.50400 -17.77100 1.000 46.72000  ? 190  LYS A CE  1 
ATOM   1353  N NZ  . LYS A 1 171 ? -21.99500 -36.22300 -18.26800 1.000 63.70000  ? 190  LYS A NZ  1 
ATOM   1354  N N   . TYR A 1 172 ? -17.63500 -39.14800 -19.44400 1.000 40.52000  ? 191  TYR A N   1 
ATOM   1355  C CA  . TYR A 1 172 ? -17.24500 -39.28500 -20.86400 1.000 33.80000  ? 191  TYR A CA  1 
ATOM   1356  C C   . TYR A 1 172 ? -18.04600 -38.27600 -21.67500 1.000 36.58000  ? 191  TYR A C   1 
ATOM   1357  O O   . TYR A 1 172 ? -19.21000 -38.08700 -21.40900 1.000 39.66000  ? 191  TYR A O   1 
ATOM   1358  C CB  . TYR A 1 172 ? -17.52300 -40.69400 -21.38200 1.000 36.20000  ? 191  TYR A CB  1 
ATOM   1359  C CG  . TYR A 1 172 ? -17.34300 -40.89000 -22.86600 1.000 41.95000  ? 191  TYR A CG  1 
ATOM   1360  C CD1 . TYR A 1 172 ? -18.30600 -40.48900 -23.77400 1.000 48.33000  ? 191  TYR A CD1 1 
ATOM   1361  C CD2 . TYR A 1 172 ? -16.20900 -41.48900 -23.37100 1.000 42.12000  ? 191  TYR A CD2 1 
ATOM   1362  C CE1 . TYR A 1 172 ? -18.14500 -40.66200 -25.13500 1.000 37.25000  ? 191  TYR A CE1 1 
ATOM   1363  C CE2 . TYR A 1 172 ? -16.03800 -41.68800 -24.72700 1.000 45.93000  ? 191  TYR A CE2 1 
ATOM   1364  C CZ  . TYR A 1 172 ? -17.01400 -41.28800 -25.61400 1.000 43.39000  ? 191  TYR A CZ  1 
ATOM   1365  O OH  . TYR A 1 172 ? -16.84200 -41.48200 -26.94400 1.000 40.67000  ? 191  TYR A OH  1 
ATOM   1366  N N   . ALA A 1 173 ? -17.38200 -37.61600 -22.60500 1.000 41.10000  ? 192  ALA A N   1 
ATOM   1367  C CA  . ALA A 1 173 ? -18.00700 -36.65400 -23.50900 1.000 35.81000  ? 192  ALA A CA  1 
ATOM   1368  C C   . ALA A 1 173 ? -17.13200 -36.52700 -24.74600 1.000 35.89000  ? 192  ALA A C   1 
ATOM   1369  O O   . ALA A 1 173 ? -15.98700 -36.07100 -24.64700 1.000 46.75000  ? 192  ALA A O   1 
ATOM   1370  C CB  . ALA A 1 173 ? -18.16700 -35.29600 -22.83200 1.000 25.98000  ? 192  ALA A CB  1 
ATOM   1371  N N   . ALA A 1 174 ? -17.66300 -36.93800 -25.89900 1.000 42.32000  ? 193  ALA A N   1 
ATOM   1372  C CA  . ALA A 1 174 ? -17.04500 -36.67900 -27.19500 1.000 36.18000  ? 193  ALA A CA  1 
ATOM   1373  C C   . ALA A 1 174 ? -15.65500 -37.29000 -27.27200 1.000 38.90000  ? 193  ALA A C   1 
ATOM   1374  O O   . ALA A 1 174 ? -14.67400 -36.61400 -27.58500 1.000 45.24000  ? 193  ALA A O   1 
ATOM   1375  C CB  . ALA A 1 174 ? -17.00100 -35.17800 -27.48900 1.000 37.81000  ? 193  ALA A CB  1 
ATOM   1376  N N   . GLY A 1 175 ? -15.56900 -38.57700 -26.94200 1.000 43.34000  ? 194  GLY A N   1 
ATOM   1377  C CA  . GLY A 1 175 ? -14.31700 -39.29800 -27.06200 1.000 41.25000  ? 194  GLY A CA  1 
ATOM   1378  C C   . GLY A 1 175 ? -13.25000 -38.94100 -26.05100 1.000 38.49000  ? 194  GLY A C   1 
ATOM   1379  O O   . GLY A 1 175 ? -12.07500 -39.24700 -26.28500 1.000 39.06000  ? 194  GLY A O   1 
ATOM   1380  N N   . LYS A 1 176 ? -13.61800 -38.31400 -24.93700 1.000 36.25000  ? 195  LYS A N   1 
ATOM   1381  C CA  . LYS A 1 176 ? -12.66700 -37.80000 -23.96000 1.000 37.43000  ? 195  LYS A CA  1 
ATOM   1382  C C   . LYS A 1 176 ? -13.18700 -38.07500 -22.55500 1.000 42.16000  ? 195  LYS A C   1 
ATOM   1383  O O   . LYS A 1 176 ? -14.39000 -37.94200 -22.29800 1.000 44.19000  ? 195  LYS A O   1 
ATOM   1384  C CB  . LYS A 1 176 ? -12.47600 -36.29200 -24.15000 1.000 35.96000  ? 195  LYS A CB  1 
ATOM   1385  C CG  . LYS A 1 176 ? -11.41000 -35.67200 -23.30900 1.000 35.15000  ? 195  LYS A CG  1 
ATOM   1386  C CD  . LYS A 1 176 ? -11.52500 -34.16400 -23.37900 1.000 34.81000  ? 195  LYS A CD  1 
ATOM   1387  C CE  . LYS A 1 176 ? -10.28200 -33.49900 -22.81600 1.000 43.36000  ? 195  LYS A CE  1 
ATOM   1388  N NZ  . LYS A 1 176 ? -9.99100  -33.81700 -21.41000 1.000 46.91000  ? 195  LYS A NZ  1 
ATOM   1389  N N   . TYR A 1 177 ? -12.29000 -38.45100 -21.64600 1.000 39.48000  ? 196  TYR A N   1 
ATOM   1390  C CA  . TYR A 1 177 ? -12.64500 -38.58500 -20.23800 1.000 33.23000  ? 196  TYR A CA  1 
ATOM   1391  C C   . TYR A 1 177 ? -12.12900 -37.40200 -19.43700 1.000 30.87000  ? 196  TYR A C   1 
ATOM   1392  O O   . TYR A 1 177 ? -11.01000 -36.93200 -19.65100 1.000 39.16000  ? 196  TYR A O   1 
ATOM   1393  C CB  . TYR A 1 177 ? -12.11300 -39.88500 -19.64300 1.000 33.25000  ? 196  TYR A CB  1 
ATOM   1394  C CG  . TYR A 1 177 ? -12.88400 -41.08000 -20.12000 1.000 40.11000  ? 196  TYR A CG  1 
ATOM   1395  C CD1 . TYR A 1 177 ? -14.12600 -41.37900 -19.57800 1.000 36.10000  ? 196  TYR A CD1 1 
ATOM   1396  C CD2 . TYR A 1 177 ? -12.38900 -41.89900 -21.12900 1.000 34.87000  ? 196  TYR A CD2 1 
ATOM   1397  C CE1 . TYR A 1 177 ? -14.84300 -42.46700 -20.01100 1.000 33.88000  ? 196  TYR A CE1 1 
ATOM   1398  C CE2 . TYR A 1 177 ? -13.10800 -42.98900 -21.57200 1.000 35.80000  ? 196  TYR A CE2 1 
ATOM   1399  C CZ  . TYR A 1 177 ? -14.33900 -43.26100 -21.01300 1.000 37.16000  ? 196  TYR A CZ  1 
ATOM   1400  O OH  . TYR A 1 177 ? -15.07000 -44.34200 -21.44100 1.000 34.30000  ? 196  TYR A OH  1 
ATOM   1401  N N   . ASP A 1 178 ? -12.96400 -36.91900 -18.52300 1.000 36.23000  ? 197  ASP A N   1 
ATOM   1402  C CA  . ASP A 1 178 ? -12.60000 -35.86200 -17.58100 1.000 40.08000  ? 197  ASP A CA  1 
ATOM   1403  C C   . ASP A 1 178 ? -12.35100 -36.51800 -16.22800 1.000 37.44000  ? 197  ASP A C   1 
ATOM   1404  O O   . ASP A 1 178 ? -13.29100 -36.92100 -15.53800 1.000 42.82000  ? 197  ASP A O   1 
ATOM   1405  C CB  . ASP A 1 178 ? -13.70000 -34.81100 -17.48900 1.000 45.96000  ? 197  ASP A CB  1 
ATOM   1406  C CG  . ASP A 1 178 ? -13.28000 -33.59600 -16.68900 1.000 44.60000  ? 197  ASP A CG  1 
ATOM   1407  O OD1 . ASP A 1 178 ? -12.12800 -33.55300 -16.22300 1.000 47.57000  ? 197  ASP A OD1 1 
ATOM   1408  O OD2 . ASP A 1 178 ? -14.10700 -32.68100 -16.51700 1.000 52.25000  ? 197  ASP A OD2 1 
ATOM   1409  N N   . ILE A 1 179 ? -11.07700 -36.62200 -15.83600 1.000 40.80000  ? 198  ILE A N   1 
ATOM   1410  C CA  . ILE A 1 179 ? -10.75400 -37.20800 -14.53200 1.000 47.20000  ? 198  ILE A CA  1 
ATOM   1411  C C   . ILE A 1 179 ? -11.00000 -36.25200 -13.37800 1.000 42.44000  ? 198  ILE A C   1 
ATOM   1412  O O   . ILE A 1 179 ? -10.81500 -36.65000 -12.22200 1.000 42.83000  ? 198  ILE A O   1 
ATOM   1413  C CB  . ILE A 1 179 ? -9.29900  -37.72800 -14.46000 1.000 40.05000  ? 198  ILE A CB  1 
ATOM   1414  C CG1 . ILE A 1 179 ? -8.29700  -36.61500 -14.75200 1.000 41.09000  ? 198  ILE A CG1 1 
ATOM   1415  C CG2 . ILE A 1 179 ? -9.07600  -38.86400 -15.42300 1.000 41.40000  ? 198  ILE A CG2 1 
ATOM   1416  C CD1 . ILE A 1 179 ? -6.87300  -37.04600 -14.50400 1.000 46.68000  ? 198  ILE A CD1 1 
ATOM   1417  N N   . LYS A 1 180 ? -11.53100 -35.07200 -13.67100 1.000 39.84000  ? 199  LYS A N   1 
ATOM   1418  C CA  . LYS A 1 180 ? -11.88900 -34.12700 -12.59300 1.000 42.54000  ? 199  LYS A CA  1 
ATOM   1419  C C   . LYS A 1 180 ? -13.38100 -34.27000 -12.30500 1.000 43.85000  ? 199  LYS A C   1 
ATOM   1420  O O   . LYS A 1 180 ? -13.86700 -33.56600 -11.45100 1.000 49.11000  ? 199  LYS A O   1 
ATOM   1421  C CB  . LYS A 1 180 ? -11.56200 -32.69300 -12.99900 1.000 43.26000  ? 199  LYS A CB  1 
ATOM   1422  C CG  . LYS A 1 180 ? -10.09900 -32.31400 -12.91800 1.000 37.74000  ? 199  LYS A CG  1 
ATOM   1423  C CD  . LYS A 1 180 ? -9.86400  -30.86800 -13.20400 1.000 47.70000  ? 199  LYS A CD  1 
ATOM   1424  C CE  . LYS A 1 180 ? -9.40200  -30.08100 -11.99700 1.000 58.57000  ? 199  LYS A CE  1 
ATOM   1425  N NZ  . LYS A 1 180 ? -10.47900 -29.25900 -11.40600 1.000 58.49000  ? 199  LYS A NZ  1 
ATOM   1426  N N   . ASP A 1 181 ? -14.06000 -35.16800 -13.00900 1.000 45.56000  ? 200  ASP A N   1 
ATOM   1427  C CA  . ASP A 1 181 ? -15.49600 -35.37600 -12.84000 1.000 40.27000  ? 200  ASP A CA  1 
ATOM   1428  C C   . ASP A 1 181 ? -15.70300 -36.84600 -12.48900 1.000 40.34000  ? 200  ASP A C   1 
ATOM   1429  O O   . ASP A 1 181 ? -15.94300 -37.68400 -13.36200 1.000 42.35000  ? 200  ASP A O   1 
ATOM   1430  C CB  . ASP A 1 181 ? -16.25300 -34.96400 -14.08800 1.000 42.65000  ? 200  ASP A CB  1 
ATOM   1431  C CG  . ASP A 1 181 ? -17.74900 -35.03900 -13.92100 1.000 44.63000  ? 200  ASP A CG  1 
ATOM   1432  O OD1 . ASP A 1 181 ? -18.23000 -35.53600 -12.87100 1.000 45.47000  ? 200  ASP A OD1 1 
ATOM   1433  O OD2 . ASP A 1 181 ? -18.45900 -34.57900 -14.83800 1.000 56.00000  ? 200  ASP A OD2 1 
ATOM   1434  N N   . VAL A 1 182 ? -15.61200 -37.14400 -11.20500 1.000 36.64000  ? 201  VAL A N   1 
ATOM   1435  C CA  . VAL A 1 182 ? -15.81600 -38.48600 -10.68500 1.000 38.23000  ? 201  VAL A CA  1 
ATOM   1436  C C   . VAL A 1 182 ? -17.24400 -38.58100 -10.17600 1.000 38.73000  ? 201  VAL A C   1 
ATOM   1437  O O   . VAL A 1 182 ? -17.76500 -37.62800 -9.58300  1.000 40.76000  ? 201  VAL A O   1 
ATOM   1438  C CB  . VAL A 1 182 ? -14.79100 -38.79600 -9.58200  1.000 36.07000  ? 201  VAL A CB  1 
ATOM   1439  C CG1 . VAL A 1 182 ? -15.09500 -40.11900 -8.92700  1.000 33.74000  ? 201  VAL A CG1 1 
ATOM   1440  C CG2 . VAL A 1 182 ? -13.39100 -38.79400 -10.16900 1.000 38.19000  ? 201  VAL A CG2 1 
ATOM   1441  N N   . GLY A 1 183 ? -17.89800 -39.70700 -10.44600 1.000 32.86000  ? 202  GLY A N   1 
ATOM   1442  C CA  . GLY A 1 183 ? -19.28500 -39.85600 -10.05300 1.000 35.53000  ? 202  GLY A CA  1 
ATOM   1443  C C   . GLY A 1 183 ? -19.47900 -40.87000 -8.94700  1.000 39.35000  ? 202  GLY A C   1 
ATOM   1444  O O   . GLY A 1 183 ? -20.44300 -41.64500 -8.96500  1.000 38.27000  ? 202  GLY A O   1 
ATOM   1445  N N   . VAL A 1 184 ? -18.57000 -40.86800 -7.97600  1.000 35.58000  ? 203  VAL A N   1 
ATOM   1446  C CA  . VAL A 1 184 ? -18.58000 -41.88600 -6.93000  1.000 36.24000  ? 203  VAL A CA  1 
ATOM   1447  C C   . VAL A 1 184 ? -19.45100 -41.48200 -5.74600  1.000 37.47000  ? 203  VAL A C   1 
ATOM   1448  O O   . VAL A 1 184 ? -20.11800 -42.33500 -5.15400  1.000 42.48000  ? 203  VAL A O   1 
ATOM   1449  C CB  . VAL A 1 184 ? -17.13500 -42.21600 -6.49700  1.000 38.26000  ? 203  VAL A CB  1 
ATOM   1450  C CG1 . VAL A 1 184 ? -17.13200 -43.06000 -5.24900  1.000 29.74000  ? 203  VAL A CG1 1 
ATOM   1451  C CG2 . VAL A 1 184 ? -16.41800 -42.97900 -7.60800  1.000 34.11000  ? 203  VAL A CG2 1 
ATOM   1452  N N   . ASP A 1 185 ? -19.50800 -40.19700 -5.37300  1.000 35.77000  ? 204  ASP A N   1 
ATOM   1453  C CA  . ASP A 1 185 ? -20.31400 -39.79600 -4.22400  1.000 39.73000  ? 204  ASP A CA  1 
ATOM   1454  C C   . ASP A 1 185 ? -21.53100 -38.95300 -4.60300  1.000 39.25000  ? 204  ASP A C   1 
ATOM   1455  O O   . ASP A 1 185 ? -21.93800 -38.07700 -3.83900  1.000 47.60000  ? 204  ASP A O   1 
ATOM   1456  C CB  . ASP A 1 185 ? -19.49000 -39.03700 -3.18200  1.000 41.46000  ? 204  ASP A CB  1 
ATOM   1457  C CG  . ASP A 1 185 ? -19.09300 -37.64200 -3.64000  1.000 46.60000  ? 204  ASP A CG  1 
ATOM   1458  O OD1 . ASP A 1 185 ? -19.27200 -37.30600 -4.83500  1.000 46.75000  ? 204  ASP A OD1 1 
ATOM   1459  O OD2 . ASP A 1 185 ? -18.62400 -36.86200 -2.78100  1.000 51.01000  ? 204  ASP A OD2 1 
ATOM   1460  N N   . ASN A 1 186 ? -22.13500 -39.19100 -5.75400  1.000 37.86000  ? 205  ASN A N   1 
ATOM   1461  C CA  . ASN A 1 186 ? -23.32400 -38.41800 -6.07200  1.000 42.34000  ? 205  ASN A CA  1 
ATOM   1462  C C   . ASN A 1 186 ? -24.56200 -39.16200 -5.57200  1.000 36.45000  ? 205  ASN A C   1 
ATOM   1463  O O   . ASN A 1 186 ? -24.47400 -40.26900 -5.03200  1.000 35.18000  ? 205  ASN A O   1 
ATOM   1464  C CB  . ASN A 1 186 ? -23.36500 -38.10200 -7.56900  1.000 40.47000  ? 205  ASN A CB  1 
ATOM   1465  C CG  . ASN A 1 186 ? -23.51700 -39.33700 -8.44100  1.000 43.13000  ? 205  ASN A CG  1 
ATOM   1466  O OD1 . ASN A 1 186 ? -23.99500 -40.39100 -8.00400  1.000 41.47000  ? 205  ASN A OD1 1 
ATOM   1467  N ND2 . ASN A 1 186 ? -23.03500 -39.23000 -9.67200  1.000 45.51000  ? 205  ASN A ND2 1 
ATOM   1468  N N   . ALA A 1 187 ? -25.73600 -38.55500 -5.75600  1.000 41.33000  ? 206  ALA A N   1 
ATOM   1469  C CA  . ALA A 1 187 ? -26.94400 -39.10900 -5.15300  1.000 37.01000  ? 206  ALA A CA  1 
ATOM   1470  C C   . ALA A 1 187 ? -27.26700 -40.48300 -5.71700  1.000 36.50000  ? 206  ALA A C   1 
ATOM   1471  O O   . ALA A 1 187 ? -27.77100 -41.35500 -4.99900  1.000 38.18000  ? 206  ALA A O   1 
ATOM   1472  C CB  . ALA A 1 187 ? -28.11900 -38.15800 -5.35300  1.000 39.97000  ? 206  ALA A CB  1 
ATOM   1473  N N   . GLY A 1 188 ? -26.99100 -40.69300 -7.00300  1.000 35.25000  ? 207  GLY A N   1 
ATOM   1474  C CA  . GLY A 1 188 ? -27.28600 -41.98100 -7.61000  1.000 39.44000  ? 207  GLY A CA  1 
ATOM   1475  C C   . GLY A 1 188 ? -26.49000 -43.11800 -6.99800  1.000 37.30000  ? 207  GLY A C   1 
ATOM   1476  O O   . GLY A 1 188 ? -27.04400 -44.16700 -6.65900  1.000 35.13000  ? 207  GLY A O   1 
ATOM   1477  N N   . ALA A 1 189 ? -25.17700 -42.92100 -6.83900  1.000 34.64000  ? 208  ALA A N   1 
ATOM   1478  C CA  . ALA A 1 189 ? -24.33900 -43.97600 -6.27400  1.000 33.29000  ? 208  ALA A CA  1 
ATOM   1479  C C   . ALA A 1 189 ? -24.73200 -44.27800 -4.83200  1.000 35.85000  ? 208  ALA A C   1 
ATOM   1480  O O   . ALA A 1 189 ? -24.75500 -45.44300 -4.40600  1.000 34.00000  ? 208  ALA A O   1 
ATOM   1481  C CB  . ALA A 1 189 ? -22.86500 -43.57700 -6.36200  1.000 31.89000  ? 208  ALA A CB  1 
ATOM   1482  N N   . LYS A 1 190 ? -25.05100 -43.24000 -4.06200  1.000 32.22000  ? 209  LYS A N   1 
ATOM   1483  C CA  . LYS A 1 190 ? -25.45100 -43.46600 -2.67900  1.000 37.31000  ? 209  LYS A CA  1 
ATOM   1484  C C   . LYS A 1 190 ? -26.72600 -44.29000 -2.60700  1.000 38.60000  ? 209  LYS A C   1 
ATOM   1485  O O   . LYS A 1 190 ? -26.82600 -45.22300 -1.80000  1.000 41.73000  ? 209  LYS A O   1 
ATOM   1486  C CB  . LYS A 1 190 ? -25.63200 -42.13100 -1.96400  1.000 36.98000  ? 209  LYS A CB  1 
ATOM   1487  C CG  . LYS A 1 190 ? -24.33100 -41.38300 -1.74100  1.000 36.80000  ? 209  LYS A CG  1 
ATOM   1488  C CD  . LYS A 1 190 ? -24.60000 -40.03600 -1.09500  1.000 40.33000  ? 209  LYS A CD  1 
ATOM   1489  C CE  . LYS A 1 190 ? -23.31500 -39.26500 -0.87600  1.000 44.86000  ? 209  LYS A CE  1 
ATOM   1490  N NZ  . LYS A 1 190 ? -23.59200 -37.96400 -0.20600  1.000 51.48000  ? 209  LYS A NZ  1 
ATOM   1491  N N   . ALA A 1 191 ? -27.71200 -43.96900 -3.44700  1.000 33.67000  ? 210  ALA A N   1 
ATOM   1492  C CA  . ALA A 1 191 ? -28.94900 -44.74000 -3.44000  1.000 33.22000  ? 210  ALA A CA  1 
ATOM   1493  C C   . ALA A 1 191 ? -28.67400 -46.19800 -3.78000  1.000 32.51000  ? 210  ALA A C   1 
ATOM   1494  O O   . ALA A 1 191 ? -29.14600 -47.11200 -3.09400  1.000 35.68000  ? 210  ALA A O   1 
ATOM   1495  C CB  . ALA A 1 191 ? -29.94700 -44.13100 -4.42300  1.000 34.62000  ? 210  ALA A CB  1 
ATOM   1496  N N   . GLY A 1 192 ? -27.87100 -46.43200 -4.81800  1.000 30.05000  ? 211  GLY A N   1 
ATOM   1497  C CA  . GLY A 1 192 ? -27.60200 -47.79600 -5.23000  1.000 29.78000  ? 211  GLY A CA  1 
ATOM   1498  C C   . GLY A 1 192 ? -26.83300 -48.58100 -4.19000  1.000 30.91000  ? 211  GLY A C   1 
ATOM   1499  O O   . GLY A 1 192 ? -27.15800 -49.73800 -3.91500  1.000 30.56000  ? 211  GLY A O   1 
ATOM   1500  N N   . LEU A 1 193 ? -25.80000 -47.97100 -3.60300  1.000 35.34000  ? 212  LEU A N   1 
ATOM   1501  C CA  . LEU A 1 193 ? -25.03800 -48.65700 -2.56200  1.000 36.40000  ? 212  LEU A CA  1 
ATOM   1502  C C   . LEU A 1 193 ? -25.86700 -48.85400 -1.29700  1.000 37.34000  ? 212  LEU A C   1 
ATOM   1503  O O   . LEU A 1 193 ? -25.70900 -49.86700 -0.60300  1.000 39.54000  ? 212  LEU A O   1 
ATOM   1504  C CB  . LEU A 1 193 ? -23.75100 -47.89300 -2.25500  1.000 33.40000  ? 212  LEU A CB  1 
ATOM   1505  C CG  . LEU A 1 193 ? -22.80300 -48.47900 -1.20200  1.000 38.14000  ? 212  LEU A CG  1 
ATOM   1506  C CD1 . LEU A 1 193 ? -22.45800 -49.92900 -1.51300  1.000 35.36000  ? 212  LEU A CD1 1 
ATOM   1507  C CD2 . LEU A 1 193 ? -21.52100 -47.64700 -1.16700  1.000 30.13000  ? 212  LEU A CD2 1 
ATOM   1508  N N   . THR A 1 194 ? -26.74700 -47.90000 -0.96900  1.000 37.81000  ? 213  THR A N   1 
ATOM   1509  C CA  . THR A 1 194 ? -27.64400 -48.09900 0.17000   1.000 38.62000  ? 213  THR A CA  1 
ATOM   1510  C C   . THR A 1 194 ? -28.49100 -49.34700 -0.02500  1.000 41.40000  ? 213  THR A C   1 
ATOM   1511  O O   . THR A 1 194 ? -28.66600 -50.15100 0.90000   1.000 34.98000  ? 213  THR A O   1 
ATOM   1512  C CB  . THR A 1 194 ? -28.54900 -46.88300 0.37200   1.000 33.71000  ? 213  THR A CB  1 
ATOM   1513  O OG1 . THR A 1 194 ? -27.76100 -45.74700 0.74200   1.000 36.10000  ? 213  THR A OG1 1 
ATOM   1514  C CG2 . THR A 1 194 ? -29.58900 -47.15900 1.44500   1.000 32.74000  ? 213  THR A CG2 1 
ATOM   1515  N N   . PHE A 1 195 ? -29.00900 -49.52800 -1.23300  1.000 37.21000  ? 214  PHE A N   1 
ATOM   1516  C CA  . PHE A 1 195 ? -29.83300 -50.72000 -1.52900  1.000 34.28000  ? 214  PHE A CA  1 
ATOM   1517  C C   . PHE A 1 195 ? -28.95300 -51.97000 -1.48800  1.000 40.76000  ? 214  PHE A C   1 
ATOM   1518  O O   . PHE A 1 195 ? -29.42400 -53.01300 -1.05900  1.000 36.84000  ? 214  PHE A O   1 
ATOM   1519  C CB  . PHE A 1 195 ? -30.57200 -50.54700 -2.85100  1.000 36.47000  ? 214  PHE A CB  1 
ATOM   1520  C CG  . PHE A 1 195 ? -31.51400 -51.67600 -3.13800  1.000 45.17000  ? 214  PHE A CG  1 
ATOM   1521  C CD1 . PHE A 1 195 ? -31.03700 -52.88500 -3.59200  1.000 40.80000  ? 214  PHE A CD1 1 
ATOM   1522  C CD2 . PHE A 1 195 ? -32.86600 -51.54300 -2.91700  1.000 34.00000  ? 214  PHE A CD2 1 
ATOM   1523  C CE1 . PHE A 1 195 ? -31.89900 -53.93400 -3.83300  1.000 43.23000  ? 214  PHE A CE1 1 
ATOM   1524  C CE2 . PHE A 1 195 ? -33.72400 -52.59400 -3.16100  1.000 32.90000  ? 214  PHE A CE2 1 
ATOM   1525  C CZ  . PHE A 1 195 ? -33.23800 -53.78400 -3.61700  1.000 35.74000  ? 214  PHE A CZ  1 
ATOM   1526  N N   . LEU A 1 196 ? -27.71300 -51.86200 -1.95500  1.000 33.93000  ? 215  LEU A N   1 
ATOM   1527  C CA  . LEU A 1 196 ? -26.81100 -53.00100 -1.85900  1.000 36.59000  ? 215  LEU A CA  1 
ATOM   1528  C C   . LEU A 1 196 ? -26.53700 -53.36600 -0.40400  1.000 37.44000  ? 215  LEU A C   1 
ATOM   1529  O O   . LEU A 1 196 ? -26.52100 -54.55100 -0.04800  1.000 36.22000  ? 215  LEU A O   1 
ATOM   1530  C CB  . LEU A 1 196 ? -25.50900 -52.69900 -2.59800  1.000 32.27000  ? 215  LEU A CB  1 
ATOM   1531  C CG  . LEU A 1 196 ? -24.48700 -53.82500 -2.56500  1.000 34.83000  ? 215  LEU A CG  1 
ATOM   1532  C CD1 . LEU A 1 196 ? -25.09600 -55.07100 -3.12900  1.000 34.41000  ? 215  LEU A CD1 1 
ATOM   1533  C CD2 . LEU A 1 196 ? -23.25200 -53.43600 -3.38100  1.000 43.18000  ? 215  LEU A CD2 1 
ATOM   1534  N N   . VAL A 1 197 ? -26.32600 -52.36300 0.45000   1.000 34.46000  ? 216  VAL A N   1 
ATOM   1535  C CA  . VAL A 1 197 ? -25.99600 -52.63000 1.84700   1.000 44.35000  ? 216  VAL A CA  1 
ATOM   1536  C C   . VAL A 1 197 ? -27.20300 -53.18500 2.59700   1.000 43.76000  ? 216  VAL A C   1 
ATOM   1537  O O   . VAL A 1 197 ? -27.06500 -54.10100 3.41600   1.000 39.82000  ? 216  VAL A O   1 
ATOM   1538  C CB  . VAL A 1 197 ? -25.43400 -51.36200 2.51400   1.000 39.48000  ? 216  VAL A CB  1 
ATOM   1539  C CG1 . VAL A 1 197 ? -25.29300 -51.57200 3.99300   1.000 41.78000  ? 216  VAL A CG1 1 
ATOM   1540  C CG2 . VAL A 1 197 ? -24.07700 -51.01700 1.91500   1.000 40.06000  ? 216  VAL A CG2 1 
ATOM   1541  N N   . ASP A 1 198 ? -28.40600 -52.66000 2.32000   1.000 45.93000  ? 217  ASP A N   1 
ATOM   1542  C CA  . ASP A 1 198 ? -29.59700 -53.14100 3.02500   1.000 45.52000  ? 217  ASP A CA  1 
ATOM   1543  C C   . ASP A 1 198 ? -29.88000 -54.60400 2.70700   1.000 42.66000  ? 217  ASP A C   1 
ATOM   1544  O O   . ASP A 1 198 ? -30.29800 -55.36400 3.58800   1.000 42.18000  ? 217  ASP A O   1 
ATOM   1545  C CB  . ASP A 1 198 ? -30.82800 -52.29000 2.69700   1.000 37.84000  ? 217  ASP A CB  1 
ATOM   1546  C CG  . ASP A 1 198 ? -30.75200 -50.88700 3.28200   1.000 49.53000  ? 217  ASP A CG  1 
ATOM   1547  O OD1 . ASP A 1 198 ? -29.96100 -50.65900 4.22300   1.000 52.77000  ? 217  ASP A OD1 1 
ATOM   1548  O OD2 . ASP A 1 198 ? -31.52800 -50.01800 2.83300   1.000 61.01000  ? 217  ASP A OD2 1 
ATOM   1549  N N   . LEU A 1 199 ? -29.67100 -55.01600 1.45400   1.000 37.18000  ? 218  LEU A N   1 
ATOM   1550  C CA  . LEU A 1 199 ? -29.74800 -56.43800 1.13200   1.000 39.02000  ? 218  LEU A CA  1 
ATOM   1551  C C   . LEU A 1 199 ? -28.85500 -57.26500 2.04900   1.000 43.46000  ? 218  LEU A C   1 
ATOM   1552  O O   . LEU A 1 199 ? -29.18400 -58.40700 2.39000   1.000 43.54000  ? 218  LEU A O   1 
ATOM   1553  C CB  . LEU A 1 199 ? -29.34600 -56.67400 -0.32100  1.000 32.63000  ? 218  LEU A CB  1 
ATOM   1554  C CG  . LEU A 1 199 ? -30.28300 -56.16700 -1.39500  1.000 38.42000  ? 218  LEU A CG  1 
ATOM   1555  C CD1 . LEU A 1 199 ? -29.61500 -56.34600 -2.74500  1.000 33.61000  ? 218  LEU A CD1 1 
ATOM   1556  C CD2 . LEU A 1 199 ? -31.58400 -56.94300 -1.33400  1.000 34.13000  ? 218  LEU A CD2 1 
ATOM   1557  N N   . ILE A 1 200 ? -27.70400 -56.71300 2.43500   1.000 39.58000  ? 219  ILE A N   1 
ATOM   1558  C CA  . ILE A 1 200 ? -26.76900 -57.43000 3.29100   1.000 40.44000  ? 219  ILE A CA  1 
ATOM   1559  C C   . ILE A 1 200 ? -27.21400 -57.37700 4.74900   1.000 46.07000  ? 219  ILE A C   1 
ATOM   1560  O O   . ILE A 1 200 ? -27.16700 -58.38600 5.45900   1.000 47.38000  ? 219  ILE A O   1 
ATOM   1561  C CB  . ILE A 1 200 ? -25.35600 -56.85700 3.09600   1.000 43.05000  ? 219  ILE A CB  1 
ATOM   1562  C CG1 . ILE A 1 200 ? -24.87100 -57.13100 1.66600   1.000 39.55000  ? 219  ILE A CG1 1 
ATOM   1563  C CG2 . ILE A 1 200 ? -24.39500 -57.41100 4.13600   1.000 42.11000  ? 219  ILE A CG2 1 
ATOM   1564  C CD1 . ILE A 1 200 ? -23.54900 -56.46600 1.30500   1.000 28.59000  ? 219  ILE A CD1 1 
ATOM   1565  N N   . LYS A 1 201 ? -27.66300 -56.20500 5.21100   1.000 48.13000  ? 220  LYS A N   1 
ATOM   1566  C CA  . LYS A 1 201 ? -28.13100 -56.06200 6.59000   1.000 40.51000  ? 220  LYS A CA  1 
ATOM   1567  C C   . LYS A 1 201 ? -29.38700 -56.89800 6.85700   1.000 45.95000  ? 220  LYS A C   1 
ATOM   1568  O O   . LYS A 1 201 ? -29.51300 -57.50400 7.92700   1.000 47.25000  ? 220  LYS A O   1 
ATOM   1569  C CB  . LYS A 1 201 ? -28.39100 -54.59000 6.90100   1.000 43.42000  ? 220  LYS A CB  1 
ATOM   1570  C CG  . LYS A 1 201 ? -27.14300 -53.72500 6.96700   1.000 48.87000  ? 220  LYS A CG  1 
ATOM   1571  C CD  . LYS A 1 201 ? -27.53300 -52.30100 7.30800   1.000 56.83000  ? 220  LYS A CD  1 
ATOM   1572  C CE  . LYS A 1 201 ? -26.33300 -51.39800 7.42500   1.000 60.49000  ? 220  LYS A CE  1 
ATOM   1573  N NZ  . LYS A 1 201 ? -26.76000 -50.00600 7.72600   1.000 70.81000  ? 220  LYS A NZ  1 
ATOM   1574  N N   . ASN A 1 202 ? -30.32800 -56.94600 5.90400   1.000 40.52000  ? 221  ASN A N   1 
ATOM   1575  C CA  . ASN A 1 202 ? -31.55200 -57.73000 6.04800   1.000 39.52000  ? 221  ASN A CA  1 
ATOM   1576  C C   . ASN A 1 202 ? -31.34700 -59.22600 5.70800   1.000 42.17000  ? 221  ASN A C   1 
ATOM   1577  O O   . ASN A 1 202 ? -32.34300 -59.94400 5.50300   1.000 42.52000  ? 221  ASN A O   1 
ATOM   1578  C CB  . ASN A 1 202 ? -32.66000 -57.13300 5.17400   1.000 32.47000  ? 221  ASN A CB  1 
ATOM   1579  C CG  . ASN A 1 202 ? -33.09700 -55.72200 5.64400   1.000 37.10000  ? 221  ASN A CG  1 
ATOM   1580  O OD1 . ASN A 1 202 ? -33.19600 -55.45700 6.84300   1.000 44.41000  ? 221  ASN A OD1 1 
ATOM   1581  N ND2 . ASN A 1 202 ? -33.37700 -54.83000 4.69900   1.000 36.75000  ? 221  ASN A ND2 1 
ATOM   1582  N N   . LYS A 1 203 ? -30.08500 -59.67500 5.60400   1.000 38.74000  ? 222  LYS A N   1 
ATOM   1583  C CA  . LYS A 1 203 ? -29.68000 -61.06600 5.37300   1.000 44.47000  ? 222  LYS A CA  1 
ATOM   1584  C C   . LYS A 1 203 ? -30.15800 -61.64900 4.04100   1.000 46.49000  ? 222  LYS A C   1 
ATOM   1585  O O   . LYS A 1 203 ? -30.38400 -62.86500 3.92400   1.000 47.85000  ? 222  LYS A O   1 
ATOM   1586  C CB  . LYS A 1 203 ? -30.16100 -61.94800 6.50800   1.000 49.77000  ? 222  LYS A CB  1 
ATOM   1587  C CG  . LYS A 1 203 ? -29.87100 -61.38300 7.84400   1.000 54.05000  ? 222  LYS A CG  1 
ATOM   1588  C CD  . LYS A 1 203 ? -28.51000 -61.83000 8.17600   1.000 49.56000  ? 222  LYS A CD  1 
ATOM   1589  C CE  . LYS A 1 203 ? -28.28200 -61.72500 9.71200   1.000 62.57000  ? 222  LYS A CE  1 
ATOM   1590  N NZ  . LYS A 1 203 ? -26.87100 -62.04400 10.12500  1.000 70.73000  ? 222  LYS A NZ  1 
ATOM   1591  N N   . HIS A 1 204 ? -30.38400 -60.82100 3.02600   1.000 44.58000  ? 223  HIS A N   1 
ATOM   1592  C CA  . HIS A 1 204 ? -30.66100 -61.43500 1.72800   1.000 42.47000  ? 223  HIS A CA  1 
ATOM   1593  C C   . HIS A 1 204 ? -29.36400 -61.79900 1.01600   1.000 48.17000  ? 223  HIS A C   1 
ATOM   1594  O O   . HIS A 1 204 ? -29.34200 -62.72500 0.19600   1.000 48.71000  ? 223  HIS A O   1 
ATOM   1595  C CB  . HIS A 1 204 ? -31.52900 -60.53200 0.85100   1.000 43.22000  ? 223  HIS A CB  1 
ATOM   1596  C CG  . HIS A 1 204 ? -32.78400 -60.07000 1.52800   1.000 42.25000  ? 223  HIS A CG  1 
ATOM   1597  N ND1 . HIS A 1 204 ? -33.79100 -60.94400 1.91100   1.000 40.15000  ? 223  HIS A ND1 1 
ATOM   1598  C CD2 . HIS A 1 204 ? -33.19400 -58.82400 1.87900   1.000 41.97000  ? 223  HIS A CD2 1 
ATOM   1599  C CE1 . HIS A 1 204 ? -34.75300 -60.25100 2.49100   1.000 43.82000  ? 223  HIS A CE1 1 
ATOM   1600  N NE2 . HIS A 1 204 ? -34.41700 -58.96900 2.48200   1.000 41.16000  ? 223  HIS A NE2 1 
ATOM   1601  N N   . MET A 1 205 ? -28.26700 -61.10000 1.32900   1.000 44.03000  ? 224  MET A N   1 
ATOM   1602  C CA  . MET A 1 205 ? -26.94200 -61.46800 0.85100   1.000 50.65000  ? 224  MET A CA  1 
ATOM   1603  C C   . MET A 1 205 ? -25.94600 -61.37900 1.99800   1.000 46.87000  ? 224  MET A C   1 
ATOM   1604  O O   . MET A 1 205 ? -26.15900 -60.65800 2.98000   1.000 48.68000  ? 224  MET A O   1 
ATOM   1605  C CB  . MET A 1 205 ? -26.46400 -60.57600 -0.30400  1.000 39.19000  ? 224  MET A CB  1 
ATOM   1606  C CG  . MET A 1 205 ? -27.33100 -60.66200 -1.54400  1.000 44.67000  ? 224  MET A CG  1 
ATOM   1607  S SD  . MET A 1 205 ? -26.53300 -59.94200 -2.98700  1.000 39.67000  ? 224  MET A SD  1 
ATOM   1608  C CE  . MET A 1 205 ? -26.52900 -58.20300 -2.57200  1.000 33.30000  ? 224  MET A CE  1 
ATOM   1609  N N   . ASN A 1 206 ? -24.84600 -62.11200 1.85500   1.000 46.84000  ? 225  ASN A N   1 
ATOM   1610  C CA  . ASN A 1 206 ? -23.78200 -62.14900 2.84700   1.000 44.03000  ? 225  ASN A CA  1 
ATOM   1611  C C   . ASN A 1 206 ? -22.61500 -61.30300 2.36100   1.000 42.23000  ? 225  ASN A C   1 
ATOM   1612  O O   . ASN A 1 206 ? -22.18700 -61.43100 1.21100   1.000 42.82000  ? 225  ASN A O   1 
ATOM   1613  C CB  . ASN A 1 206 ? -23.31600 -63.58200 3.10600   1.000 51.48000  ? 225  ASN A CB  1 
ATOM   1614  C CG  . ASN A 1 206 ? -24.43800 -64.48300 3.60600   1.000 69.16000  ? 225  ASN A CG  1 
ATOM   1615  O OD1 . ASN A 1 206 ? -25.31900 -64.06300 4.37200   1.000 60.90000  ? 225  ASN A OD1 1 
ATOM   1616  N ND2 . ASN A 1 206 ? -24.39600 -65.74400 3.19000   1.000 71.60000  ? 225  ASN A ND2 1 
ATOM   1617  N N   . ALA A 1 207 ? -22.08900 -60.45300 3.24400   1.000 48.71000  ? 226  ALA A N   1 
ATOM   1618  C CA  . ALA A 1 207 ? -21.05600 -59.50300 2.84100   1.000 46.36000  ? 226  ALA A CA  1 
ATOM   1619  C C   . ALA A 1 207 ? -19.76000 -60.16600 2.37700   1.000 41.61000  ? 226  ALA A C   1 
ATOM   1620  O O   . ALA A 1 207 ? -18.93400 -59.49600 1.74100   1.000 38.49000  ? 226  ALA A O   1 
ATOM   1621  C CB  . ALA A 1 207 ? -20.74600 -58.54000 3.98400   1.000 38.94000  ? 226  ALA A CB  1 
ATOM   1622  N N   . ASP A 1 208 ? -19.52900 -61.44000 2.69000   1.000 37.44000  ? 227  ASP A N   1 
ATOM   1623  C CA  . ASP A 1 208 ? -18.27000 -62.06300 2.30000   1.000 43.19000  ? 227  ASP A CA  1 
ATOM   1624  C C   . ASP A 1 208 ? -18.36900 -62.91300 1.03700   1.000 41.41000  ? 227  ASP A C   1 
ATOM   1625  O O   . ASP A 1 208 ? -17.38500 -63.56900 0.67300   1.000 36.87000  ? 227  ASP A O   1 
ATOM   1626  C CB  . ASP A 1 208 ? -17.70600 -62.91100 3.45600   1.000 44.82000  ? 227  ASP A CB  1 
ATOM   1627  C CG  . ASP A 1 208 ? -18.55000 -64.13100 3.76800   1.000 56.89000  ? 227  ASP A CG  1 
ATOM   1628  O OD1 . ASP A 1 208 ? -19.60000 -64.34100 3.11000   1.000 58.94000  ? 227  ASP A OD1 1 
ATOM   1629  O OD2 . ASP A 1 208 ? -18.15600 -64.89100 4.69000   1.000 50.17000  ? 227  ASP A OD2 1 
ATOM   1630  N N   . THR A 1 209 ? -19.51700 -62.91900 0.36000   1.000 40.19000  ? 228  THR A N   1 
ATOM   1631  C CA  . THR A 1 209 ? -19.64400 -63.70500 -0.86300  1.000 39.82000  ? 228  THR A CA  1 
ATOM   1632  C C   . THR A 1 209 ? -18.69000 -63.18800 -1.93400  1.000 40.10000  ? 228  THR A C   1 
ATOM   1633  O O   . THR A 1 209 ? -18.61100 -61.98200 -2.19000  1.000 40.38000  ? 228  THR A O   1 
ATOM   1634  C CB  . THR A 1 209 ? -21.08400 -63.67300 -1.36200  1.000 36.28000  ? 228  THR A CB  1 
ATOM   1635  O OG1 . THR A 1 209 ? -21.91900 -64.30200 -0.39000  1.000 41.15000  ? 228  THR A OG1 1 
ATOM   1636  C CG2 . THR A 1 209 ? -21.21200 -64.41800 -2.66500  1.000 35.57000  ? 228  THR A CG2 1 
ATOM   1637  N N   . ASP A 1 210 ? -17.94700 -64.10200 -2.54300  1.000 38.91000  ? 229  ASP A N   1 
ATOM   1638  C CA  . ASP A 1 210 ? -16.98300 -63.74600 -3.57200  1.000 38.80000  ? 229  ASP A CA  1 
ATOM   1639  C C   . ASP A 1 210 ? -17.31000 -64.51900 -4.85300  1.000 43.34000  ? 229  ASP A C   1 
ATOM   1640  O O   . ASP A 1 210 ? -18.36700 -65.15200 -4.97000  1.000 43.83000  ? 229  ASP A O   1 
ATOM   1641  C CB  . ASP A 1 210 ? -15.55500 -63.98300 -3.05900  1.000 30.59000  ? 229  ASP A CB  1 
ATOM   1642  C CG  . ASP A 1 210 ? -15.23500 -65.45400 -2.81800  1.000 39.06000  ? 229  ASP A CG  1 
ATOM   1643  O OD1 . ASP A 1 210 ? -16.07600 -66.32600 -3.11500  1.000 44.01000  ? 229  ASP A OD1 1 
ATOM   1644  O OD2 . ASP A 1 210 ? -14.13000 -65.74400 -2.30600  1.000 41.49000  ? 229  ASP A OD2 1 
ATOM   1645  N N   . TYR A 1 211 ? -16.40000 -64.45000 -5.82900  1.000 43.45000  ? 230  TYR A N   1 
ATOM   1646  C CA  . TYR A 1 211 ? -16.66400 -65.08200 -7.11900  1.000 40.96000  ? 230  TYR A CA  1 
ATOM   1647  C C   . TYR A 1 211 ? -16.80100 -66.59200 -6.98200  1.000 43.78000  ? 230  TYR A C   1 
ATOM   1648  O O   . TYR A 1 211 ? -17.73000 -67.19300 -7.53500  1.000 40.88000  ? 230  TYR A O   1 
ATOM   1649  C CB  . TYR A 1 211 ? -15.55000 -64.74100 -8.09900  1.000 35.50000  ? 230  TYR A CB  1 
ATOM   1650  C CG  . TYR A 1 211 ? -15.80400 -65.23800 -9.49600  1.000 35.35000  ? 230  TYR A CG  1 
ATOM   1651  C CD1 . TYR A 1 211 ? -16.73100 -64.61600 -10.30700 1.000 39.74000  ? 230  TYR A CD1 1 
ATOM   1652  C CD2 . TYR A 1 211 ? -15.09900 -66.30900 -10.01900 1.000 45.65000  ? 230  TYR A CD2 1 
ATOM   1653  C CE1 . TYR A 1 211 ? -16.96700 -65.05100 -11.59600 1.000 41.67000  ? 230  TYR A CE1 1 
ATOM   1654  C CE2 . TYR A 1 211 ? -15.32900 -66.75100 -11.30800 1.000 41.32000  ? 230  TYR A CE2 1 
ATOM   1655  C CZ  . TYR A 1 211 ? -16.26500 -66.11800 -12.08900 1.000 36.11000  ? 230  TYR A CZ  1 
ATOM   1656  O OH  . TYR A 1 211 ? -16.51500 -66.54600 -13.36900 1.000 40.40000  ? 230  TYR A OH  1 
ATOM   1657  N N   . SER A 1 212 ? -15.88900 -67.21800 -6.23800  1.000 43.16000  ? 231  SER A N   1 
ATOM   1658  C CA  . SER A 1 212 ? -15.93600 -68.66400 -6.06100  1.000 39.81000  ? 231  SER A CA  1 
ATOM   1659  C C   . SER A 1 212 ? -17.19500 -69.09000 -5.31200  1.000 42.36000  ? 231  SER A C   1 
ATOM   1660  O O   . SER A 1 212 ? -17.84400 -70.07800 -5.67900  1.000 42.18000  ? 231  SER A O   1 
ATOM   1661  C CB  . SER A 1 212 ? -14.68400 -69.13200 -5.32300  1.000 43.04000  ? 231  SER A CB  1 
ATOM   1662  O OG  . SER A 1 212 ? -14.75200 -70.51200 -5.03400  1.000 57.00000  ? 231  SER A OG  1 
ATOM   1663  N N   . ILE A 1 213 ? -17.56300 -68.35200 -4.26600  1.000 38.72000  ? 232  ILE A N   1 
ATOM   1664  C CA  . ILE A 1 213 ? -18.73100 -68.72000 -3.47200  1.000 41.84000  ? 232  ILE A CA  1 
ATOM   1665  C C   . ILE A 1 213 ? -20.00200 -68.63400 -4.31200  1.000 43.73000  ? 232  ILE A C   1 
ATOM   1666  O O   . ILE A 1 213 ? -20.79300 -69.58400 -4.36400  1.000 44.90000  ? 232  ILE A O   1 
ATOM   1667  C CB  . ILE A 1 213 ? -18.81700 -67.84800 -2.20400  1.000 39.18000  ? 232  ILE A CB  1 
ATOM   1668  C CG1 . ILE A 1 213 ? -17.66200 -68.18500 -1.24600  1.000 41.39000  ? 232  ILE A CG1 1 
ATOM   1669  C CG2 . ILE A 1 213 ? -20.17000 -68.01900 -1.51600  1.000 37.19000  ? 232  ILE A CG2 1 
ATOM   1670  C CD1 . ILE A 1 213 ? -17.48700 -67.19700 -0.08100  1.000 29.75000  ? 232  ILE A CD1 1 
ATOM   1671  N N   . ALA A 1 214 ? -20.20300 -67.50700 -5.00200  1.000 38.57000  ? 233  ALA A N   1 
ATOM   1672  C CA  . ALA A 1 214 ? -21.38300 -67.35600 -5.84600  1.000 35.67000  ? 233  ALA A CA  1 
ATOM   1673  C C   . ALA A 1 214 ? -21.42000 -68.40400 -6.94900  1.000 40.10000  ? 233  ALA A C   1 
ATOM   1674  O O   . ALA A 1 214 ? -22.48200 -68.96200 -7.24800  1.000 41.54000  ? 233  ALA A O   1 
ATOM   1675  C CB  . ALA A 1 214 ? -21.43000 -65.95500 -6.45000  1.000 33.71000  ? 233  ALA A CB  1 
ATOM   1676  N N   . GLU A 1 215 ? -20.27400 -68.68700 -7.57100  1.000 41.62000  ? 234  GLU A N   1 
ATOM   1677  C CA  . GLU A 1 215 ? -20.27900 -69.62200 -8.69300  1.000 42.41000  ? 234  GLU A CA  1 
ATOM   1678  C C   . GLU A 1 215 ? -20.71100 -71.01000 -8.24400  1.000 45.40000  ? 234  GLU A C   1 
ATOM   1679  O O   . GLU A 1 215 ? -21.53700 -71.65800 -8.89800  1.000 50.40000  ? 234  GLU A O   1 
ATOM   1680  C CB  . GLU A 1 215 ? -18.90500 -69.69500 -9.35300  1.000 39.83000  ? 234  GLU A CB  1 
ATOM   1681  C CG  . GLU A 1 215 ? -19.01300 -70.35500 -10.70600 1.000 47.20000  ? 234  GLU A CG  1 
ATOM   1682  C CD  . GLU A 1 215 ? -17.69200 -70.56000 -11.38600 1.000 46.77000  ? 234  GLU A CD  1 
ATOM   1683  O OE1 . GLU A 1 215 ? -16.65100 -70.49200 -10.70400 1.000 57.29000  ? 234  GLU A OE1 1 
ATOM   1684  O OE2 . GLU A 1 215 ? -17.70000 -70.72100 -12.62500 1.000 43.01000  ? 234  GLU A OE2 1 
ATOM   1685  N N   . ALA A 1 216 ? -20.16500 -71.48100 -7.11900  1.000 40.22000  ? 235  ALA A N   1 
ATOM   1686  C CA  . ALA A 1 216 ? -20.53800 -72.79500 -6.60900  1.000 44.27000  ? 235  ALA A CA  1 
ATOM   1687  C C   . ALA A 1 216 ? -22.01700 -72.85200 -6.24300  1.000 44.98000  ? 235  ALA A C   1 
ATOM   1688  O O   . ALA A 1 216 ? -22.70300 -73.83200 -6.55000  1.000 42.38000  ? 235  ALA A O   1 
ATOM   1689  C CB  . ALA A 1 216 ? -19.67700 -73.14500 -5.39800  1.000 41.28000  ? 235  ALA A CB  1 
ATOM   1690  N N   . ALA A 1 217 ? -22.52800 -71.81200 -5.58700  1.000 42.70000  ? 236  ALA A N   1 
ATOM   1691  C CA  . ALA A 1 217 ? -23.91200 -71.84800 -5.12900  1.000 42.68000  ? 236  ALA A CA  1 
ATOM   1692  C C   . ALA A 1 217 ? -24.87900 -71.93500 -6.30400  1.000 47.26000  ? 236  ALA A C   1 
ATOM   1693  O O   . ALA A 1 217 ? -25.83500 -72.72300 -6.27900  1.000 43.77000  ? 236  ALA A O   1 
ATOM   1694  C CB  . ALA A 1 217 ? -24.21000 -70.62400 -4.26300  1.000 39.45000  ? 236  ALA A CB  1 
ATOM   1695  N N   . PHE A 1 218 ? -24.64100 -71.14000 -7.35300  1.000 46.21000  ? 237  PHE A N   1 
ATOM   1696  C CA  . PHE A 1 218 ? -25.54900 -71.16200 -8.49600  1.000 46.01000  ? 237  PHE A CA  1 
ATOM   1697  C C   . PHE A 1 218 ? -25.43200 -72.46200 -9.28500  1.000 47.01000  ? 237  PHE A C   1 
ATOM   1698  O O   . PHE A 1 218 ? -26.44700 -73.01400 -9.72800  1.000 44.30000  ? 237  PHE A O   1 
ATOM   1699  C CB  . PHE A 1 218 ? -25.30400 -69.97500 -9.42700  1.000 41.57000  ? 237  PHE A CB  1 
ATOM   1700  C CG  . PHE A 1 218 ? -26.35100 -69.84500 -10.49700 1.000 42.06000  ? 237  PHE A CG  1 
ATOM   1701  C CD1 . PHE A 1 218 ? -27.56700 -69.21300 -10.22200 1.000 41.03000  ? 237  PHE A CD1 1 
ATOM   1702  C CD2 . PHE A 1 218 ? -26.16100 -70.41200 -11.74700 1.000 36.76000  ? 237  PHE A CD2 1 
ATOM   1703  C CE1 . PHE A 1 218 ? -28.54800 -69.11100 -11.19000 1.000 37.35000  ? 237  PHE A CE1 1 
ATOM   1704  C CE2 . PHE A 1 218 ? -27.14600 -70.32200 -12.71600 1.000 39.88000  ? 237  PHE A CE2 1 
ATOM   1705  C CZ  . PHE A 1 218 ? -28.34300 -69.66800 -12.43700 1.000 36.00000  ? 237  PHE A CZ  1 
ATOM   1706  N N   . ASN A 1 219 ? -24.20600 -72.95200 -9.50400  1.000 45.07000  ? 238  ASN A N   1 
ATOM   1707  C CA  . ASN A 1 219 ? -24.07600 -74.16800 -10.29800 1.000 47.88000  ? 238  ASN A CA  1 
ATOM   1708  C C   . ASN A 1 219 ? -24.54100 -75.40700 -9.54300  1.000 46.52000  ? 238  ASN A C   1 
ATOM   1709  O O   . ASN A 1 219 ? -24.81100 -76.43200 -10.17900 1.000 44.61000  ? 238  ASN A O   1 
ATOM   1710  C CB  . ASN A 1 219 ? -22.63900 -74.36500 -10.78300 1.000 38.60000  ? 238  ASN A CB  1 
ATOM   1711  C CG  . ASN A 1 219 ? -22.19200 -73.26400 -11.72000 1.000 44.72000  ? 238  ASN A CG  1 
ATOM   1712  O OD1 . ASN A 1 219 ? -23.01300 -72.60600 -12.35500 1.000 44.31000  ? 238  ASN A OD1 1 
ATOM   1713  N ND2 . ASN A 1 219 ? -20.88300 -73.11400 -11.87700 1.000 47.00000  ? 238  ASN A ND2 1 
ATOM   1714  N N   . LYS A 1 220 ? -24.66300 -75.32900 -8.21900  1.000 46.95000  ? 239  LYS A N   1 
ATOM   1715  C CA  . LYS A 1 220 ? -25.18700 -76.41100 -7.39500  1.000 49.79000  ? 239  LYS A CA  1 
ATOM   1716  C C   . LYS A 1 220 ? -26.69100 -76.30800 -7.17300  1.000 44.55000  ? 239  LYS A C   1 
ATOM   1717  O O   . LYS A 1 220 ? -27.26300 -77.17300 -6.50700  1.000 46.41000  ? 239  LYS A O   1 
ATOM   1718  C CB  . LYS A 1 220 ? -24.47100 -76.43500 -6.03400  1.000 47.25000  ? 239  LYS A CB  1 
ATOM   1719  C CG  . LYS A 1 220 ? -23.01900 -76.92800 -6.03300  1.000 49.09000  ? 239  LYS A CG  1 
ATOM   1720  C CD  . LYS A 1 220 ? -22.42400 -76.74700 -4.62900  1.000 60.24000  ? 239  LYS A CD  1 
ATOM   1721  C CE  . LYS A 1 220 ? -20.95200 -77.15100 -4.50200  1.000 63.63000  ? 239  LYS A CE  1 
ATOM   1722  N NZ  . LYS A 1 220 ? -20.72000 -78.62400 -4.43200  1.000 72.01000  ? 239  LYS A NZ  1 
ATOM   1723  N N   . GLY A 1 221 ? -27.33900 -75.27600 -7.70800  1.000 45.13000  ? 240  GLY A N   1 
ATOM   1724  C CA  . GLY A 1 221 ? -28.77700 -75.12900 -7.58200  1.000 45.28000  ? 240  GLY A CA  1 
ATOM   1725  C C   . GLY A 1 221 ? -29.25500 -74.50800 -6.29000  1.000 50.59000  ? 240  GLY A C   1 
ATOM   1726  O O   . GLY A 1 221 ? -30.44900 -74.59800 -5.97700  1.000 48.02000  ? 240  GLY A O   1 
ATOM   1727  N N   . GLU A 1 222 ? -28.36200 -73.86700 -5.53200  1.000 46.02000  ? 241  GLU A N   1 
ATOM   1728  C CA  . GLU A 1 222 ? -28.69400 -73.35100 -4.21100  1.000 45.84000  ? 241  GLU A CA  1 
ATOM   1729  C C   . GLU A 1 222 ? -29.21800 -71.92400 -4.23000  1.000 50.53000  ? 241  GLU A C   1 
ATOM   1730  O O   . GLU A 1 222 ? -29.88900 -71.51100 -3.27300  1.000 48.21000  ? 241  GLU A O   1 
ATOM   1731  C CB  . GLU A 1 222 ? -27.46600 -73.40600 -3.31000  1.000 47.60000  ? 241  GLU A CB  1 
ATOM   1732  C CG  . GLU A 1 222 ? -26.98500 -74.80300 -3.02600  1.000 51.92000  ? 241  GLU A CG  1 
ATOM   1733  C CD  . GLU A 1 222 ? -25.75900 -74.81100 -2.14400  1.000 60.42000  ? 241  GLU A CD  1 
ATOM   1734  O OE1 . GLU A 1 222 ? -25.19100 -73.71900 -1.90200  1.000 57.73000  ? 241  GLU A OE1 1 
ATOM   1735  O OE2 . GLU A 1 222 ? -25.37700 -75.90900 -1.67900  1.000 66.24000  ? 241  GLU A OE2 1 
ATOM   1736  N N   . THR A 1 223 ? -28.91300 -71.15500 -5.27300  1.000 43.06000  ? 242  THR A N   1 
ATOM   1737  C CA  . THR A 1 223 ? -29.40900 -69.79500 -5.39100  1.000 40.82000  ? 242  THR A CA  1 
ATOM   1738  C C   . THR A 1 223 ? -30.08800 -69.64000 -6.74500  1.000 43.14000  ? 242  THR A C   1 
ATOM   1739  O O   . THR A 1 223 ? -29.67000 -70.24100 -7.74200  1.000 38.89000  ? 242  THR A O   1 
ATOM   1740  C CB  . THR A 1 223 ? -28.27600 -68.76500 -5.20100  1.000 36.82000  ? 242  THR A CB  1 
ATOM   1741  O OG1 . THR A 1 223 ? -28.82000 -67.44300 -5.10600  1.000 39.46000  ? 242  THR A OG1 1 
ATOM   1742  C CG2 . THR A 1 223 ? -27.29500 -68.81000 -6.35400  1.000 45.74000  ? 242  THR A CG2 1 
ATOM   1743  N N   . ALA A 1 224 ? -31.15800 -68.84000 -6.76700  1.000 34.90000  ? 243  ALA A N   1 
ATOM   1744  C CA  . ALA A 1 224 ? -31.96400 -68.71600 -7.97700  1.000 37.85000  ? 243  ALA A CA  1 
ATOM   1745  C C   . ALA A 1 224 ? -31.28100 -67.88600 -9.05500  1.000 35.88000  ? 243  ALA A C   1 
ATOM   1746  O O   . ALA A 1 224 ? -31.58000 -68.05800 -10.24100 1.000 35.12000  ? 243  ALA A O   1 
ATOM   1747  C CB  . ALA A 1 224 ? -33.32000 -68.09800 -7.64500  1.000 34.28000  ? 243  ALA A CB  1 
ATOM   1748  N N   . MET A 1 225 ? -30.37400 -66.98800 -8.67200  1.000 40.44000  ? 244  MET A N   1 
ATOM   1749  C CA  . MET A 1 225 ? -29.79900 -66.02300 -9.59500  1.000 35.42000  ? 244  MET A CA  1 
ATOM   1750  C C   . MET A 1 225 ? -28.36400 -65.72300 -9.20300  1.000 35.60000  ? 244  MET A C   1 
ATOM   1751  O O   . MET A 1 225 ? -28.03400 -65.66400 -8.01800  1.000 39.46000  ? 244  MET A O   1 
ATOM   1752  C CB  . MET A 1 225 ? -30.57700 -64.70600 -9.58600  1.000 36.81000  ? 244  MET A CB  1 
ATOM   1753  C CG  . MET A 1 225 ? -31.96900 -64.76500 -10.15000 1.000 34.03000  ? 244  MET A CG  1 
ATOM   1754  S SD  . MET A 1 225 ? -32.67800 -63.11900 -10.04300 1.000 40.10000  ? 244  MET A SD  1 
ATOM   1755  C CE  . MET A 1 225 ? -32.99900 -63.01300 -8.28400  1.000 46.06000  ? 244  MET A CE  1 
ATOM   1756  N N   . THR A 1 226 ? -27.52400 -65.50200 -10.21300 1.000 40.30000  ? 245  THR A N   1 
ATOM   1757  C CA  . THR A 1 226 ? -26.19400 -64.93000 -10.04500 1.000 36.70000  ? 245  THR A CA  1 
ATOM   1758  C C   . THR A 1 226 ? -26.00600 -63.84000 -11.09900 1.000 34.78000  ? 245  THR A C   1 
ATOM   1759  O O   . THR A 1 226 ? -26.82500 -63.67400 -12.00000 1.000 32.04000  ? 245  THR A O   1 
ATOM   1760  C CB  . THR A 1 226 ? -25.08900 -65.98700 -10.15400 1.000 36.84000  ? 245  THR A CB  1 
ATOM   1761  O OG1 . THR A 1 226 ? -23.83500 -65.41000 -9.76700  1.000 37.79000  ? 245  THR A OG1 1 
ATOM   1762  C CG2 . THR A 1 226 ? -24.96600 -66.49100 -11.57700 1.000 27.40000  ? 245  THR A CG2 1 
ATOM   1763  N N   . ILE A 1 227 ? -24.93500 -63.06500 -10.96500 1.000 36.93000  ? 246  ILE A N   1 
ATOM   1764  C CA  . ILE A 1 227 ? -24.57900 -62.05000 -11.95100 1.000 36.13000  ? 246  ILE A CA  1 
ATOM   1765  C C   . ILE A 1 227 ? -23.19300 -62.38400 -12.46800 1.000 31.66000  ? 246  ILE A C   1 
ATOM   1766  O O   . ILE A 1 227 ? -22.23200 -62.42600 -11.69100 1.000 31.53000  ? 246  ILE A O   1 
ATOM   1767  C CB  . ILE A 1 227 ? -24.60400 -60.63100 -11.36700 1.000 33.28000  ? 246  ILE A CB  1 
ATOM   1768  C CG1 . ILE A 1 227 ? -26.01900 -60.23000 -10.97200 1.000 27.24000  ? 246  ILE A CG1 1 
ATOM   1769  C CG2 . ILE A 1 227 ? -24.03200 -59.64200 -12.36300 1.000 25.70000  ? 246  ILE A CG2 1 
ATOM   1770  C CD1 . ILE A 1 227 ? -26.06400 -58.88200 -10.31900 1.000 26.88000  ? 246  ILE A CD1 1 
ATOM   1771  N N   . ASN A 1 228 ? -23.07500 -62.60500 -13.77100 1.000 32.20000  ? 247  ASN A N   1 
ATOM   1772  C CA  . ASN A 1 228 ? -21.78100 -63.00900 -14.28800 1.000 28.83000  ? 247  ASN A CA  1 
ATOM   1773  C C   . ASN A 1 228 ? -21.77800 -62.79100 -15.79600 1.000 31.45000  ? 247  ASN A C   1 
ATOM   1774  O O   . ASN A 1 228 ? -22.81000 -62.49500 -16.40200 1.000 38.39000  ? 247  ASN A O   1 
ATOM   1775  C CB  . ASN A 1 228 ? -21.50700 -64.45800 -13.87500 1.000 33.73000  ? 247  ASN A CB  1 
ATOM   1776  C CG  . ASN A 1 228 ? -20.03800 -64.73100 -13.63200 1.000 41.27000  ? 247  ASN A CG  1 
ATOM   1777  O OD1 . ASN A 1 228 ? -19.17300 -63.93200 -13.99400 1.000 37.92000  ? 247  ASN A OD1 1 
ATOM   1778  N ND2 . ASN A 1 228 ? -19.75800 -65.81200 -12.91100 1.000 37.85000  ? 247  ASN A ND2 1 
ATOM   1779  N N   . GLY A 1 229 ? -20.59600 -62.91000 -16.38900 1.000 32.45000  ? 248  GLY A N   1 
ATOM   1780  C CA  . GLY A 1 229 ? -20.41100 -62.68600 -17.80300 1.000 25.78000  ? 248  GLY A CA  1 
ATOM   1781  C C   . GLY A 1 229 ? -20.35100 -63.98300 -18.59000 1.000 32.64000  ? 248  GLY A C   1 
ATOM   1782  O O   . GLY A 1 229 ? -20.50800 -65.08000 -18.03900 1.000 31.75000  ? 248  GLY A O   1 
ATOM   1783  N N   . PRO A 1 230 ? -20.14100 -63.87500 -19.90800 1.000 28.68000  ? 249  PRO A N   1 
ATOM   1784  C CA  . PRO A 1 230 ? -20.19600 -65.07300 -20.76500 1.000 32.42000  ? 249  PRO A CA  1 
ATOM   1785  C C   . PRO A 1 230 ? -19.10200 -66.09000 -20.47900 1.000 38.16000  ? 249  PRO A C   1 
ATOM   1786  O O   . PRO A 1 230 ? -19.26300 -67.26900 -20.82800 1.000 36.92000  ? 249  PRO A O   1 
ATOM   1787  C CB  . PRO A 1 230 ? -20.06900 -64.49400 -22.18200 1.000 29.60000  ? 249  PRO A CB  1 
ATOM   1788  C CG  . PRO A 1 230 ? -20.48000 -63.04700 -22.04800 1.000 28.91000  ? 249  PRO A CG  1 
ATOM   1789  C CD  . PRO A 1 230 ? -19.98200 -62.64100 -20.69400 1.000 29.43000  ? 249  PRO A CD  1 
ATOM   1790  N N   . TRP A 1 231 ? -17.99200 -65.67300 -19.86400 1.000 34.64000  ? 250  TRP A N   1 
ATOM   1791  C CA  . TRP A 1 231 ? -16.92400 -66.60200 -19.51400 1.000 35.65000  ? 250  TRP A CA  1 
ATOM   1792  C C   . TRP A 1 231 ? -17.39100 -67.66000 -18.52100 1.000 42.15000  ? 250  TRP A C   1 
ATOM   1793  O O   . TRP A 1 231 ? -16.73700 -68.70200 -18.39200 1.000 46.63000  ? 250  TRP A O   1 
ATOM   1794  C CB  . TRP A 1 231 ? -15.73000 -65.82600 -18.93900 1.000 30.53000  ? 250  TRP A CB  1 
ATOM   1795  C CG  . TRP A 1 231 ? -16.15200 -64.96200 -17.77300 1.000 37.12000  ? 250  TRP A CG  1 
ATOM   1796  C CD1 . TRP A 1 231 ? -16.27600 -65.35000 -16.47000 1.000 32.81000  ? 250  TRP A CD1 1 
ATOM   1797  C CD2 . TRP A 1 231 ? -16.53700 -63.57900 -17.81800 1.000 32.59000  ? 250  TRP A CD2 1 
ATOM   1798  N NE1 . TRP A 1 231 ? -16.71000 -64.29500 -15.69900 1.000 35.09000  ? 250  TRP A NE1 1 
ATOM   1799  C CE2 . TRP A 1 231 ? -16.87900 -63.19700 -16.50400 1.000 35.39000  ? 250  TRP A CE2 1 
ATOM   1800  C CE3 . TRP A 1 231 ? -16.62500 -62.63200 -18.83800 1.000 31.90000  ? 250  TRP A CE3 1 
ATOM   1801  C CZ2 . TRP A 1 231 ? -17.30200 -61.90500 -16.18500 1.000 35.94000  ? 250  TRP A CZ2 1 
ATOM   1802  C CZ3 . TRP A 1 231 ? -17.04300 -61.34800 -18.51900 1.000 31.66000  ? 250  TRP A CZ3 1 
ATOM   1803  C CH2 . TRP A 1 231 ? -17.37300 -60.99700 -17.20400 1.000 32.53000  ? 250  TRP A CH2 1 
ATOM   1804  N N   . ALA A 1 232 ? -18.50200 -67.41700 -17.81300 1.000 36.83000  ? 251  ALA A N   1 
ATOM   1805  C CA  . ALA A 1 232 ? -19.03300 -68.34900 -16.81900 1.000 38.55000  ? 251  ALA A CA  1 
ATOM   1806  C C   . ALA A 1 232 ? -19.99400 -69.37500 -17.40200 1.000 33.83000  ? 251  ALA A C   1 
ATOM   1807  O O   . ALA A 1 232 ? -20.33300 -70.34100 -16.70900 1.000 33.53000  ? 251  ALA A O   1 
ATOM   1808  C CB  . ALA A 1 232 ? -19.75500 -67.58800 -15.70100 1.000 34.16000  ? 251  ALA A CB  1 
ATOM   1809  N N   . TRP A 1 233 ? -20.41800 -69.19600 -18.65500 1.000 40.03000  ? 252  TRP A N   1 
ATOM   1810  C CA  . TRP A 1 233 ? -21.47900 -70.02400 -19.22100 1.000 39.68000  ? 252  TRP A CA  1 
ATOM   1811  C C   . TRP A 1 233 ? -21.06000 -71.48100 -19.30800 1.000 41.12000  ? 252  TRP A C   1 
ATOM   1812  O O   . TRP A 1 233 ? -21.87000 -72.38400 -19.05800 1.000 43.51000  ? 252  TRP A O   1 
ATOM   1813  C CB  . TRP A 1 233 ? -21.86600 -69.50600 -20.60400 1.000 37.29000  ? 252  TRP A CB  1 
ATOM   1814  C CG  . TRP A 1 233 ? -22.54000 -68.18300 -20.57200 1.000 33.39000  ? 252  TRP A CG  1 
ATOM   1815  C CD1 . TRP A 1 233 ? -22.94200 -67.49200 -19.46900 1.000 34.05000  ? 252  TRP A CD1 1 
ATOM   1816  C CD2 . TRP A 1 233 ? -22.90900 -67.38900 -21.70000 1.000 29.84000  ? 252  TRP A CD2 1 
ATOM   1817  N NE1 . TRP A 1 233 ? -23.53200 -66.30700 -19.84000 1.000 31.34000  ? 252  TRP A NE1 1 
ATOM   1818  C CE2 . TRP A 1 233 ? -23.52000 -66.22000 -21.20600 1.000 33.24000  ? 252  TRP A CE2 1 
ATOM   1819  C CE3 . TRP A 1 233 ? -22.77500 -67.55000 -23.08000 1.000 29.06000  ? 252  TRP A CE3 1 
ATOM   1820  C CZ2 . TRP A 1 233 ? -24.00000 -65.22100 -22.04500 1.000 32.53000  ? 252  TRP A CZ2 1 
ATOM   1821  C CZ3 . TRP A 1 233 ? -23.23700 -66.55900 -23.90600 1.000 33.60000  ? 252  TRP A CZ3 1 
ATOM   1822  C CH2 . TRP A 1 233 ? -23.85000 -65.40800 -23.39000 1.000 33.20000  ? 252  TRP A CH2 1 
ATOM   1823  N N   . SER A 1 234 ? -19.80300 -71.72600 -19.67700 1.000 43.35000  ? 253  SER A N   1 
ATOM   1824  C CA  . SER A 1 234 ? -19.31300 -73.09200 -19.83800 1.000 44.35000  ? 253  SER A CA  1 
ATOM   1825  C C   . SER A 1 234 ? -19.50800 -73.91000 -18.56600 1.000 41.74000  ? 253  SER A C   1 
ATOM   1826  O O   . SER A 1 234 ? -20.02500 -75.03300 -18.61500 1.000 43.04000  ? 253  SER A O   1 
ATOM   1827  C CB  . SER A 1 234 ? -17.84000 -73.06500 -20.23600 1.000 39.97000  ? 253  SER A CB  1 
ATOM   1828  O OG  . SER A 1 234 ? -17.31900 -74.37500 -20.23900 1.000 56.68000  ? 253  SER A OG  1 
ATOM   1829  N N   . ASN A 1 235 ? -19.12300 -73.35100 -17.41100 1.000 40.49000  ? 254  ASN A N   1 
ATOM   1830  C CA  . ASN A 1 235 ? -19.25000 -74.09100 -16.15600 1.000 38.46000  ? 254  ASN A CA  1 
ATOM   1831  C C   . ASN A 1 235 ? -20.70700 -74.39100 -15.83400 1.000 47.51000  ? 254  ASN A C   1 
ATOM   1832  O O   . ASN A 1 235 ? -21.02200 -75.45500 -15.28800 1.000 47.72000  ? 254  ASN A O   1 
ATOM   1833  C CB  . ASN A 1 235 ? -18.60300 -73.32500 -15.00100 1.000 35.59000  ? 254  ASN A CB  1 
ATOM   1834  C CG  . ASN A 1 235 ? -17.08300 -73.31200 -15.08900 1.000 51.83000  ? 254  ASN A CG  1 
ATOM   1835  O OD1 . ASN A 1 235 ? -16.47200 -74.27600 -15.56000 1.000 51.16000  ? 254  ASN A OD1 1 
ATOM   1836  N ND2 . ASN A 1 235 ? -16.46200 -72.24100 -14.59600 1.000 42.34000  ? 254  ASN A ND2 1 
ATOM   1837  N N   . ILE A 1 236 ? -21.61200 -73.46400 -16.15400 1.000 43.34000  ? 255  ILE A N   1 
ATOM   1838  C CA  . ILE A 1 236 ? -23.02100 -73.72700 -15.90700 1.000 45.94000  ? 255  ILE A CA  1 
ATOM   1839  C C   . ILE A 1 236 ? -23.51300 -74.84700 -16.81700 1.000 49.25000  ? 255  ILE A C   1 
ATOM   1840  O O   . ILE A 1 236 ? -24.32900 -75.68500 -16.40900 1.000 48.38000  ? 255  ILE A O   1 
ATOM   1841  C CB  . ILE A 1 236 ? -23.85400 -72.45100 -16.09300 1.000 45.86000  ? 255  ILE A CB  1 
ATOM   1842  C CG1 . ILE A 1 236 ? -23.22200 -71.28600 -15.34200 1.000 39.85000  ? 255  ILE A CG1 1 
ATOM   1843  C CG2 . ILE A 1 236 ? -25.22700 -72.66500 -15.50300 1.000 41.98000  ? 255  ILE A CG2 1 
ATOM   1844  C CD1 . ILE A 1 236 ? -23.82300 -69.94800 -15.69800 1.000 34.64000  ? 255  ILE A CD1 1 
ATOM   1845  N N   . ASP A 1 237 ? -23.02600 -74.87400 -18.06400 1.000 48.24000  ? 256  ASP A N   1 
ATOM   1846  C CA  . ASP A 1 237 ? -23.40100 -75.93400 -18.99600 1.000 47.91000  ? 256  ASP A CA  1 
ATOM   1847  C C   . ASP A 1 237 ? -23.08200 -77.30500 -18.41600 1.000 48.26000  ? 256  ASP A C   1 
ATOM   1848  O O   . ASP A 1 237 ? -23.90400 -78.22600 -18.46800 1.000 47.75000  ? 256  ASP A O   1 
ATOM   1849  C CB  . ASP A 1 237 ? -22.67500 -75.75000 -20.33200 1.000 46.02000  ? 256  ASP A CB  1 
ATOM   1850  C CG  . ASP A 1 237 ? -23.09200 -74.49100 -21.05900 1.000 48.93000  ? 256  ASP A CG  1 
ATOM   1851  O OD1 . ASP A 1 237 ? -24.21200 -74.00000 -20.79000 1.000 44.36000  ? 256  ASP A OD1 1 
ATOM   1852  O OD2 . ASP A 1 237 ? -22.31400 -74.01000 -21.92300 1.000 41.12000  ? 256  ASP A OD2 1 
ATOM   1853  N N   . THR A 1 238 ? -21.87400 -77.45300 -17.86300 1.000 50.35000  ? 257  THR A N   1 
ATOM   1854  C CA  . THR A 1 238 ? -21.48000 -78.70900 -17.23600 1.000 50.17000  ? 257  THR A CA  1 
ATOM   1855  C C   . THR A 1 238 ? -22.37900 -79.05400 -16.05500 1.000 54.51000  ? 257  THR A C   1 
ATOM   1856  O O   . THR A 1 238 ? -22.67500 -80.23300 -15.82200 1.000 61.13000  ? 257  THR A O   1 
ATOM   1857  C CB  . THR A 1 238 ? -20.01400 -78.62400 -16.80100 1.000 52.95000  ? 257  THR A CB  1 
ATOM   1858  O OG1 . THR A 1 238 ? -19.18100 -78.50600 -17.96200 1.000 49.15000  ? 257  THR A OG1 1 
ATOM   1859  C CG2 . THR A 1 238 ? -19.60100 -79.85100 -15.98900 1.000 50.61000  ? 257  THR A CG2 1 
ATOM   1860  N N   . SER A 1 239 ? -22.83900 -78.05100 -15.31300 1.000 49.09000  ? 258  SER A N   1 
ATOM   1861  C CA  . SER A 1 239 ? -23.74300 -78.33000 -14.21600 1.000 51.17000  ? 258  SER A CA  1 
ATOM   1862  C C   . SER A 1 239 ? -25.10500 -78.74300 -14.76400 1.000 55.12000  ? 258  SER A C   1 
ATOM   1863  O O   . SER A 1 239 ? -25.39500 -78.62300 -15.95700 1.000 53.55000  ? 258  SER A O   1 
ATOM   1864  C CB  . SER A 1 239 ? -23.89300 -77.11000 -13.31100 1.000 50.49000  ? 258  SER A CB  1 
ATOM   1865  O OG  . SER A 1 239 ? -24.62400 -76.08900 -13.97100 1.000 54.14000  ? 258  SER A OG  1 
ATOM   1866  N N   . ALA A 1 240 ? -25.95600 -79.22000 -13.87000 1.000 52.93000  ? 259  ALA A N   1 
ATOM   1867  C CA  . ALA A 1 240 ? -27.28500 -79.66700 -14.25100 1.000 61.80000  ? 259  ALA A CA  1 
ATOM   1868  C C   . ALA A 1 240 ? -28.30500 -78.53300 -14.26400 1.000 60.05000  ? 259  ALA A C   1 
ATOM   1869  O O   . ALA A 1 240 ? -29.50000 -78.79100 -14.44600 1.000 67.14000  ? 259  ALA A O   1 
ATOM   1870  C CB  . ALA A 1 240 ? -27.74600 -80.78500 -13.31300 1.000 57.69000  ? 259  ALA A CB  1 
ATOM   1871  N N   . VAL A 1 241 ? -27.87000 -77.29100 -14.06000 1.000 54.39000  ? 260  VAL A N   1 
ATOM   1872  C CA  . VAL A 1 241 ? -28.81800 -76.19300 -13.93400 1.000 49.98000  ? 260  VAL A CA  1 
ATOM   1873  C C   . VAL A 1 241 ? -29.38200 -75.84900 -15.30400 1.000 48.22000  ? 260  VAL A C   1 
ATOM   1874  O O   . VAL A 1 241 ? -28.64100 -75.71900 -16.29000 1.000 54.92000  ? 260  VAL A O   1 
ATOM   1875  C CB  . VAL A 1 241 ? -28.16000 -74.96700 -13.28500 1.000 48.52000  ? 260  VAL A CB  1 
ATOM   1876  C CG1 . VAL A 1 241 ? -29.15500 -73.80100 -13.23100 1.000 44.15000  ? 260  VAL A CG1 1 
ATOM   1877  C CG2 . VAL A 1 241 ? -27.64700 -75.30200 -11.88500 1.000 47.09000  ? 260  VAL A CG2 1 
ATOM   1878  N N   . ASN A 1 242 ? -30.70400 -75.70900 -15.37100 1.000 45.78000  ? 261  ASN A N   1 
ATOM   1879  C CA  . ASN A 1 242 ? -31.39100 -75.14600 -16.53100 1.000 48.64000  ? 261  ASN A CA  1 
ATOM   1880  C C   . ASN A 1 242 ? -31.38000 -73.63400 -16.36100 1.000 45.52000  ? 261  ASN A C   1 
ATOM   1881  O O   . ASN A 1 242 ? -32.14500 -73.08400 -15.56300 1.000 44.88000  ? 261  ASN A O   1 
ATOM   1882  C CB  . ASN A 1 242 ? -32.81800 -75.66800 -16.62100 1.000 46.78000  ? 261  ASN A CB  1 
ATOM   1883  C CG  . ASN A 1 242 ? -33.54700 -75.16600 -17.85800 1.000 61.65000  ? 261  ASN A CG  1 
ATOM   1884  O OD1 . ASN A 1 242 ? -32.94200 -74.57900 -18.76100 1.000 59.60000  ? 261  ASN A OD1 1 
ATOM   1885  N ND2 . ASN A 1 242 ? -34.87400 -75.31600 -17.86200 1.000 63.04000  ? 261  ASN A ND2 1 
ATOM   1886  N N   . TYR A 1 243 ? -30.51900 -72.94700 -17.10300 1.000 43.52000  ? 262  TYR A N   1 
ATOM   1887  C CA  . TYR A 1 243 ? -30.28600 -71.54300 -16.81500 1.000 44.36000  ? 262  TYR A CA  1 
ATOM   1888  C C   . TYR A 1 243 ? -30.69100 -70.66100 -17.98200 1.000 39.43000  ? 262  TYR A C   1 
ATOM   1889  O O   . TYR A 1 243 ? -30.64000 -71.06400 -19.14800 1.000 41.27000  ? 262  TYR A O   1 
ATOM   1890  C CB  . TYR A 1 243 ? -28.81900 -71.27900 -16.46000 1.000 40.28000  ? 262  TYR A CB  1 
ATOM   1891  C CG  . TYR A 1 243 ? -27.84800 -71.33700 -17.61100 1.000 36.43000  ? 262  TYR A CG  1 
ATOM   1892  C CD1 . TYR A 1 243 ? -27.29600 -72.53800 -18.01900 1.000 38.38000  ? 262  TYR A CD1 1 
ATOM   1893  C CD2 . TYR A 1 243 ? -27.43900 -70.17400 -18.25000 1.000 35.87000  ? 262  TYR A CD2 1 
ATOM   1894  C CE1 . TYR A 1 243 ? -26.38300 -72.58200 -19.05200 1.000 39.20000  ? 262  TYR A CE1 1 
ATOM   1895  C CE2 . TYR A 1 243 ? -26.53000 -70.20600 -19.28100 1.000 34.40000  ? 262  TYR A CE2 1 
ATOM   1896  C CZ  . TYR A 1 243 ? -26.00700 -71.41400 -19.68400 1.000 40.03000  ? 262  TYR A CZ  1 
ATOM   1897  O OH  . TYR A 1 243 ? -25.10000 -71.45000 -20.72100 1.000 37.43000  ? 262  TYR A OH  1 
ATOM   1898  N N   . GLY A 1 244 ? -31.09700 -69.44800 -17.64100 1.000 40.73000  ? 263  GLY A N   1 
ATOM   1899  C CA  . GLY A 1 244 ? -31.29100 -68.40800 -18.62600 1.000 36.54000  ? 263  GLY A CA  1 
ATOM   1900  C C   . GLY A 1 244 ? -30.36400 -67.24000 -18.35900 1.000 40.29000  ? 263  GLY A C   1 
ATOM   1901  O O   . GLY A 1 244 ? -29.81200 -67.10300 -17.26100 1.000 40.90000  ? 263  GLY A O   1 
ATOM   1902  N N   . VAL A 1 245 ? -30.17100 -66.40700 -19.37400 1.000 35.71000  ? 264  VAL A N   1 
ATOM   1903  C CA  . VAL A 1 245 ? -29.41900 -65.16800 -19.26800 1.000 32.05000  ? 264  VAL A CA  1 
ATOM   1904  C C   . VAL A 1 245 ? -30.34300 -64.06700 -19.75800 1.000 33.11000  ? 264  VAL A C   1 
ATOM   1905  O O   . VAL A 1 245 ? -30.98800 -64.22600 -20.79900 1.000 35.87000  ? 264  VAL A O   1 
ATOM   1906  C CB  . VAL A 1 245 ? -28.12400 -65.23700 -20.09600 1.000 31.81000  ? 264  VAL A CB  1 
ATOM   1907  C CG1 . VAL A 1 245 ? -27.34000 -63.95100 -19.98000 1.000 31.71000  ? 264  VAL A CG1 1 
ATOM   1908  C CG2 . VAL A 1 245 ? -27.28300 -66.43800 -19.67100 1.000 30.99000  ? 264  VAL A CG2 1 
ATOM   1909  N N   . THR A 1 246 ? -30.44400 -62.97200 -19.00500 1.000 28.90000  ? 265  THR A N   1 
ATOM   1910  C CA  . THR A 1 246 ? -31.43700 -61.95500 -19.33300 1.000 28.43000  ? 265  THR A CA  1 
ATOM   1911  C C   . THR A 1 246 ? -30.93700 -60.57700 -18.92200 1.000 30.48000  ? 265  THR A C   1 
ATOM   1912  O O   . THR A 1 246 ? -29.82700 -60.41600 -18.41400 1.000 27.63000  ? 265  THR A O   1 
ATOM   1913  C CB  . THR A 1 246 ? -32.78800 -62.26400 -18.67300 1.000 31.51000  ? 265  THR A CB  1 
ATOM   1914  O OG1 . THR A 1 246 ? -33.73600 -61.28400 -19.08900 1.000 39.21000  ? 265  THR A OG1 1 
ATOM   1915  C CG2 . THR A 1 246 ? -32.68700 -62.21500 -17.16400 1.000 34.18000  ? 265  THR A CG2 1 
ATOM   1916  N N   . VAL A 1 247 ? -31.78000 -59.57000 -19.15200 1.000 28.46000  ? 266  VAL A N   1 
ATOM   1917  C CA  . VAL A 1 247 ? -31.40900 -58.20000 -18.82700 1.000 27.95000  ? 266  VAL A CA  1 
ATOM   1918  C C   . VAL A 1 247 ? -31.25800 -58.04800 -17.31300 1.000 29.83000  ? 266  VAL A C   1 
ATOM   1919  O O   . VAL A 1 247 ? -31.97900 -58.67600 -16.52500 1.000 29.34000  ? 266  VAL A O   1 
ATOM   1920  C CB  . VAL A 1 247 ? -32.46400 -57.24500 -19.41600 1.000 34.35000  ? 266  VAL A CB  1 
ATOM   1921  C CG1 . VAL A 1 247 ? -33.83100 -57.49300 -18.77900 1.000 33.70000  ? 266  VAL A CG1 1 
ATOM   1922  C CG2 . VAL A 1 247 ? -32.05200 -55.79100 -19.27200 1.000 32.88000  ? 266  VAL A CG2 1 
ATOM   1923  N N   . LEU A 1 248 ? -30.27900 -57.25600 -16.89100 1.000 36.33000  ? 267  LEU A N   1 
ATOM   1924  C CA  . LEU A 1 248 ? -30.11200 -57.03500 -15.46400 1.000 33.07000  ? 267  LEU A CA  1 
ATOM   1925  C C   . LEU A 1 248 ? -31.31300 -56.25900 -14.93200 1.000 34.72000  ? 267  LEU A C   1 
ATOM   1926  O O   . LEU A 1 248 ? -31.97300 -55.53000 -15.68200 1.000 33.68000  ? 267  LEU A O   1 
ATOM   1927  C CB  . LEU A 1 248 ? -28.81700 -56.27600 -15.16900 1.000 28.44000  ? 267  LEU A CB  1 
ATOM   1928  C CG  . LEU A 1 248 ? -27.50000 -57.04000 -15.33600 1.000 29.88000  ? 267  LEU A CG  1 
ATOM   1929  C CD1 . LEU A 1 248 ? -26.35600 -56.06800 -15.34200 1.000 30.99000  ? 267  LEU A CD1 1 
ATOM   1930  C CD2 . LEU A 1 248 ? -27.29100 -58.02800 -14.22100 1.000 26.27000  ? 267  LEU A CD2 1 
ATOM   1931  N N   . PRO A 1 249 ? -31.63500 -56.42100 -13.65100 1.000 30.81000  ? 268  PRO A N   1 
ATOM   1932  C CA  . PRO A 1 249 ? -32.80600 -55.73900 -13.10100 1.000 31.32000  ? 268  PRO A CA  1 
ATOM   1933  C C   . PRO A 1 249 ? -32.59300 -54.23700 -13.11700 1.000 34.19000  ? 268  PRO A C   1 
ATOM   1934  O O   . PRO A 1 249 ? -31.46200 -53.74800 -13.12900 1.000 37.14000  ? 268  PRO A O   1 
ATOM   1935  C CB  . PRO A 1 249 ? -32.89200 -56.26900 -11.66400 1.000 37.94000  ? 268  PRO A CB  1 
ATOM   1936  C CG  . PRO A 1 249 ? -32.06400 -57.52000 -11.65200 1.000 35.29000  ? 268  PRO A CG  1 
ATOM   1937  C CD  . PRO A 1 249 ? -30.96100 -57.25100 -12.63400 1.000 35.87000  ? 268  PRO A CD  1 
ATOM   1938  N N   . THR A 1 250 ? -33.69800 -53.50700 -13.15100 1.000 35.23000  ? 269  THR A N   1 
ATOM   1939  C CA  . THR A 1 250 ? -33.64000 -52.06900 -12.98900 1.000 30.08000  ? 269  THR A CA  1 
ATOM   1940  C C   . THR A 1 250 ? -33.56400 -51.71900 -11.50500 1.000 35.08000  ? 269  THR A C   1 
ATOM   1941  O O   . THR A 1 250 ? -33.85400 -52.53900 -10.62900 1.000 29.87000  ? 269  THR A O   1 
ATOM   1942  C CB  . THR A 1 250 ? -34.86600 -51.40600 -13.61200 1.000 35.69000  ? 269  THR A CB  1 
ATOM   1943  O OG1 . THR A 1 250 ? -36.02600 -51.87200 -12.92400 1.000 33.61000  ? 269  THR A OG1 1 
ATOM   1944  C CG2 . THR A 1 250 ? -34.99500 -51.77000 -15.09600 1.000 27.14000  ? 269  THR A CG2 1 
ATOM   1945  N N   . PHE A 1 251 ? -33.15700 -50.48400 -11.23300 1.000 27.68000  ? 270  PHE A N   1 
ATOM   1946  C CA  . PHE A 1 251 ? -33.19700 -49.92400 -9.89200  1.000 32.73000  ? 270  PHE A CA  1 
ATOM   1947  C C   . PHE A 1 251 ? -33.70800 -48.49800 -9.98400  1.000 34.85000  ? 270  PHE A C   1 
ATOM   1948  O O   . PHE A 1 251 ? -33.14300 -47.68000 -10.71600 1.000 30.99000  ? 270  PHE A O   1 
ATOM   1949  C CB  . PHE A 1 251 ? -31.81900 -49.96400 -9.21800  1.000 31.84000  ? 270  PHE A CB  1 
ATOM   1950  C CG  . PHE A 1 251 ? -31.76400 -49.22400 -7.90600  1.000 37.24000  ? 270  PHE A CG  1 
ATOM   1951  C CD1 . PHE A 1 251 ? -32.50700 -49.65700 -6.81200  1.000 33.64000  ? 270  PHE A CD1 1 
ATOM   1952  C CD2 . PHE A 1 251 ? -30.92900 -48.11900 -7.75100  1.000 34.24000  ? 270  PHE A CD2 1 
ATOM   1953  C CE1 . PHE A 1 251 ? -32.44600 -48.98000 -5.60500  1.000 30.92000  ? 270  PHE A CE1 1 
ATOM   1954  C CE2 . PHE A 1 251 ? -30.85800 -47.44400 -6.54500  1.000 33.17000  ? 270  PHE A CE2 1 
ATOM   1955  C CZ  . PHE A 1 251 ? -31.62100 -47.87200 -5.47300  1.000 30.73000  ? 270  PHE A CZ  1 
ATOM   1956  N N   . LYS A 1 252 ? -34.76900 -48.20500 -9.23100  1.000 36.02000  ? 271  LYS A N   1 
ATOM   1957  C CA  . LYS A 1 252 ? -35.46500 -46.92800 -9.34300  1.000 35.29000  ? 271  LYS A CA  1 
ATOM   1958  C C   . LYS A 1 252 ? -35.88000 -46.68400 -10.79300 1.000 36.86000  ? 271  LYS A C   1 
ATOM   1959  O O   . LYS A 1 252 ? -35.85100 -45.55800 -11.30100 1.000 37.99000  ? 271  LYS A O   1 
ATOM   1960  C CB  . LYS A 1 252 ? -34.61100 -45.78200 -8.79500  1.000 36.33000  ? 271  LYS A CB  1 
ATOM   1961  C CG  . LYS A 1 252 ? -34.37800 -45.85700 -7.28100  1.000 41.90000  ? 271  LYS A CG  1 
ATOM   1962  C CD  . LYS A 1 252 ? -33.45400 -44.73500 -6.77900  1.000 37.18000  ? 271  LYS A CD  1 
ATOM   1963  C CE  . LYS A 1 252 ? -34.18700 -43.39300 -6.72500  1.000 47.48000  ? 271  LYS A CE  1 
ATOM   1964  N NZ  . LYS A 1 252 ? -33.33800 -42.25800 -6.24500  1.000 44.15000  ? 271  LYS A NZ  1 
ATOM   1965  N N   . GLY A 1 253 ? -36.25100 -47.76900 -11.47200 1.000 31.49000  ? 272  GLY A N   1 
ATOM   1966  C CA  . GLY A 1 253 ? -36.66500 -47.72400 -12.85700 1.000 34.98000  ? 272  GLY A CA  1 
ATOM   1967  C C   . GLY A 1 253 ? -35.55400 -47.53700 -13.86900 1.000 34.94000  ? 272  GLY A C   1 
ATOM   1968  O O   . GLY A 1 253 ? -35.83800 -47.50300 -15.06900 1.000 36.10000  ? 272  GLY A O   1 
ATOM   1969  N N   . GLN A 1 254 ? -34.30800 -47.42000 -13.43900 1.000 36.62000  ? 273  GLN A N   1 
ATOM   1970  C CA  . GLN A 1 254 ? -33.12600 -47.16600 -14.25600 1.000 39.14000  ? 273  GLN A CA  1 
ATOM   1971  C C   . GLN A 1 254 ? -32.39800 -48.47400 -14.52000 1.000 35.05000  ? 273  GLN A C   1 
ATOM   1972  O O   . GLN A 1 254 ? -32.30600 -49.31900 -13.62000 1.000 37.10000  ? 273  GLN A O   1 
ATOM   1973  C CB  . GLN A 1 254 ? -32.20200 -46.20200 -13.51400 1.000 39.34000  ? 273  GLN A CB  1 
ATOM   1974  C CG  . GLN A 1 254 ? -32.91700 -44.90800 -13.16800 1.000 43.43000  ? 273  GLN A CG  1 
ATOM   1975  C CD  . GLN A 1 254 ? -32.90800 -43.89600 -14.28800 1.000 57.19000  ? 273  GLN A CD  1 
ATOM   1976  O OE1 . GLN A 1 254 ? -33.71500 -43.96100 -15.21600 1.000 56.84000  ? 273  GLN A OE1 1 
ATOM   1977  N NE2 . GLN A 1 254 ? -32.08200 -42.86500 -14.12800 1.000 71.20000  ? 273  GLN A NE2 1 
ATOM   1978  N N   . PRO A 1 255 ? -31.88300 -48.70700 -15.72900 1.000 40.35000  ? 274  PRO A N   1 
ATOM   1979  C CA  . PRO A 1 255 ? -31.16200 -49.96000 -15.98200 1.000 34.48000  ? 274  PRO A CA  1 
ATOM   1980  C C   . PRO A 1 255 ? -29.93600 -50.07000 -15.09800 1.000 29.08000  ? 274  PRO A C   1 
ATOM   1981  O O   . PRO A 1 255 ? -29.26700 -49.07100 -14.81700 1.000 30.55000  ? 274  PRO A O   1 
ATOM   1982  C CB  . PRO A 1 255 ? -30.76600 -49.85300 -17.45700 1.000 35.22000  ? 274  PRO A CB  1 
ATOM   1983  C CG  . PRO A 1 255 ? -31.71900 -48.89300 -18.04100 1.000 37.16000  ? 274  PRO A CG  1 
ATOM   1984  C CD  . PRO A 1 255 ? -32.01500 -47.89700 -16.95000 1.000 35.50000  ? 274  PRO A CD  1 
ATOM   1985  N N   . SER A 1 256 ? -29.63900 -51.29700 -14.66600 1.000 28.05000  ? 275  SER A N   1 
ATOM   1986  C CA  . SER A 1 256 ? -28.28800 -51.59300 -14.19000 1.000 30.62000  ? 275  SER A CA  1 
ATOM   1987  C C   . SER A 1 256 ? -27.28100 -51.34300 -15.30800 1.000 27.16000  ? 275  SER A C   1 
ATOM   1988  O O   . SER A 1 256 ? -27.55700 -51.60300 -16.48200 1.000 26.91000  ? 275  SER A O   1 
ATOM   1989  C CB  . SER A 1 256 ? -28.20000 -53.03800 -13.69700 1.000 28.45000  ? 275  SER A CB  1 
ATOM   1990  O OG  . SER A 1 256 ? -28.98400 -53.20300 -12.50600 1.000 32.43000  ? 275  SER A OG  1 
ATOM   1991  N N   . LYS A 1 257 ? -26.10700 -50.81900 -14.94800 1.000 32.80000  ? 276  LYS A N   1 
ATOM   1992  C CA  . LYS A 1 257 ? -25.12800 -50.32900 -15.91700 1.000 29.48000  ? 276  LYS A CA  1 
ATOM   1993  C C   . LYS A 1 257 ? -23.79300 -51.04300 -15.71900 1.000 30.36000  ? 276  LYS A C   1 
ATOM   1994  O O   . LYS A 1 257 ? -22.87900 -50.51300 -15.07100 1.000 29.54000  ? 276  LYS A O   1 
ATOM   1995  C CB  . LYS A 1 257 ? -24.96500 -48.81700 -15.78800 1.000 26.60000  ? 276  LYS A CB  1 
ATOM   1996  C CG  . LYS A 1 257 ? -26.24300 -48.08000 -16.09100 1.000 31.08000  ? 276  LYS A CG  1 
ATOM   1997  C CD  . LYS A 1 257 ? -26.06600 -46.59700 -15.93900 1.000 32.08000  ? 276  LYS A CD  1 
ATOM   1998  C CE  . LYS A 1 257 ? -25.18100 -46.07300 -17.05300 1.000 35.80000  ? 276  LYS A CE  1 
ATOM   1999  N NZ  . LYS A 1 257 ? -25.16200 -44.58800 -17.09800 1.000 42.21000  ? 276  LYS A NZ  1 
ATOM   2000  N N   . PRO A 1 258 ? -23.63500 -52.23700 -16.28200 1.000 30.73000  ? 277  PRO A N   1 
ATOM   2001  C CA  . PRO A 1 258 ? -22.35300 -52.94400 -16.18300 1.000 29.48000  ? 277  PRO A CA  1 
ATOM   2002  C C   . PRO A 1 258 ? -21.30700 -52.30300 -17.08400 1.000 29.59000  ? 277  PRO A C   1 
ATOM   2003  O O   . PRO A 1 258 ? -21.63000 -51.59600 -18.04200 1.000 27.51000  ? 277  PRO A O   1 
ATOM   2004  C CB  . PRO A 1 258 ? -22.69800 -54.35600 -16.65900 1.000 27.86000  ? 277  PRO A CB  1 
ATOM   2005  C CG  . PRO A 1 258 ? -23.82000 -54.11500 -17.65600 1.000 26.92000  ? 277  PRO A CG  1 
ATOM   2006  C CD  . PRO A 1 258 ? -24.60400 -52.94700 -17.13600 1.000 26.63000  ? 277  PRO A CD  1 
ATOM   2007  N N   . PHE A 1 259 ? -20.03500 -52.54000 -16.75900 1.000 29.51000  ? 278  PHE A N   1 
ATOM   2008  C CA  . PHE A 1 259 ? -18.96400 -52.07300 -17.63400 1.000 31.24000  ? 278  PHE A CA  1 
ATOM   2009  C C   . PHE A 1 259 ? -18.87100 -52.95600 -18.86500 1.000 31.62000  ? 278  PHE A C   1 
ATOM   2010  O O   . PHE A 1 259 ? -19.08400 -54.17100 -18.79300 1.000 33.40000  ? 278  PHE A O   1 
ATOM   2011  C CB  . PHE A 1 259 ? -17.60700 -52.04700 -16.92100 1.000 29.18000  ? 278  PHE A CB  1 
ATOM   2012  C CG  . PHE A 1 259 ? -17.44600 -50.91400 -15.95500 1.000 26.75000  ? 278  PHE A CG  1 
ATOM   2013  C CD1 . PHE A 1 259 ? -17.23700 -49.62500 -16.42100 1.000 24.18000  ? 278  PHE A CD1 1 
ATOM   2014  C CD2 . PHE A 1 259 ? -17.47000 -51.13800 -14.58900 1.000 28.10000  ? 278  PHE A CD2 1 
ATOM   2015  C CE1 . PHE A 1 259 ? -17.07900 -48.56600 -15.54400 1.000 23.77000  ? 278  PHE A CE1 1 
ATOM   2016  C CE2 . PHE A 1 259 ? -17.31300 -50.08400 -13.69700 1.000 30.40000  ? 278  PHE A CE2 1 
ATOM   2017  C CZ  . PHE A 1 259 ? -17.11700 -48.79100 -14.17800 1.000 26.47000  ? 278  PHE A CZ  1 
ATOM   2018  N N   . VAL A 1 260 ? -18.53900 -52.33300 -19.99500 1.000 29.16000  ? 279  VAL A N   1 
ATOM   2019  C CA  . VAL A 1 260 ? -18.56100 -52.97900 -21.30000 1.000 30.62000  ? 279  VAL A CA  1 
ATOM   2020  C C   . VAL A 1 260 ? -17.13400 -53.04300 -21.83600 1.000 32.30000  ? 279  VAL A C   1 
ATOM   2021  O O   . VAL A 1 260 ? -16.44600 -52.01800 -21.93700 1.000 28.60000  ? 279  VAL A O   1 
ATOM   2022  C CB  . VAL A 1 260 ? -19.48900 -52.22900 -22.26600 1.000 29.81000  ? 279  VAL A CB  1 
ATOM   2023  C CG1 . VAL A 1 260 ? -19.51700 -52.91700 -23.62200 1.000 29.64000  ? 279  VAL A CG1 1 
ATOM   2024  C CG2 . VAL A 1 260 ? -20.90100 -52.11000 -21.65900 1.000 25.92000  ? 279  VAL A CG2 1 
ATOM   2025  N N   . GLY A 1 261 ? -16.68200 -54.25600 -22.16400 1.000 29.87000  ? 280  GLY A N   1 
ATOM   2026  C CA  . GLY A 1 261 ? -15.39100 -54.45900 -22.79400 1.000 24.49000  ? 280  GLY A CA  1 
ATOM   2027  C C   . GLY A 1 261 ? -15.56600 -54.80300 -24.26900 1.000 31.58000  ? 280  GLY A C   1 
ATOM   2028  O O   . GLY A 1 261 ? -16.35900 -55.67800 -24.62600 1.000 31.47000  ? 280  GLY A O   1 
ATOM   2029  N N   . VAL A 1 262 ? -14.81200 -54.10800 -25.10600 1.000 27.51000  ? 281  VAL A N   1 
ATOM   2030  C CA  . VAL A 1 262 ? -14.95600 -54.20700 -26.55200 1.000 27.92000  ? 281  VAL A CA  1 
ATOM   2031  C C   . VAL A 1 262 ? -13.65400 -54.74100 -27.13000 1.000 28.56000  ? 281  VAL A C   1 
ATOM   2032  O O   . VAL A 1 262 ? -12.63700 -54.03500 -27.13300 1.000 26.85000  ? 281  VAL A O   1 
ATOM   2033  C CB  . VAL A 1 262 ? -15.31600 -52.85200 -27.17100 1.000 29.30000  ? 281  VAL A CB  1 
ATOM   2034  C CG1 . VAL A 1 262 ? -15.28500 -52.93800 -28.68700 1.000 27.87000  ? 281  VAL A CG1 1 
ATOM   2035  C CG2 . VAL A 1 262 ? -16.67600 -52.39100 -26.66400 1.000 26.70000  ? 281  VAL A CG2 1 
ATOM   2036  N N   . LEU A 1 263 ? -13.67200 -55.98800 -27.59900 1.000 28.46000  ? 282  LEU A N   1 
ATOM   2037  C CA  . LEU A 1 263 ? -12.55000 -56.49500 -28.37900 1.000 26.29000  ? 282  LEU A CA  1 
ATOM   2038  C C   . LEU A 1 263 ? -12.38900 -55.63500 -29.62400 1.000 29.58000  ? 282  LEU A C   1 
ATOM   2039  O O   . LEU A 1 263 ? -13.36500 -55.37300 -30.33300 1.000 30.82000  ? 282  LEU A O   1 
ATOM   2040  C CB  . LEU A 1 263 ? -12.78200 -57.95700 -28.75700 1.000 23.54000  ? 282  LEU A CB  1 
ATOM   2041  C CG  . LEU A 1 263 ? -11.73300 -58.61000 -29.66200 1.000 32.56000  ? 282  LEU A CG  1 
ATOM   2042  C CD1 . LEU A 1 263 ? -10.35900 -58.64700 -28.99500 1.000 33.15000  ? 282  LEU A CD1 1 
ATOM   2043  C CD2 . LEU A 1 263 ? -12.17700 -60.00700 -30.06600 1.000 27.59000  ? 282  LEU A CD2 1 
ATOM   2044  N N   . SER A 1 264 ? -11.15800 -55.18700 -29.88900 1.000 25.43000  ? 283  SER A N   1 
ATOM   2045  C CA  . SER A 1 264 ? -10.93700 -54.15000 -30.88800 1.000 28.24000  ? 283  SER A CA  1 
ATOM   2046  C C   . SER A 1 264 ? -9.67800  -54.43600 -31.69800 1.000 33.11000  ? 283  SER A C   1 
ATOM   2047  O O   . SER A 1 264 ? -8.75300  -55.11000 -31.23500 1.000 32.30000  ? 283  SER A O   1 
ATOM   2048  C CB  . SER A 1 264 ? -10.83200 -52.76700 -30.23700 1.000 29.23000  ? 283  SER A CB  1 
ATOM   2049  O OG  . SER A 1 264 ? -12.04500 -52.43200 -29.59500 1.000 36.59000  ? 283  SER A OG  1 
ATOM   2050  N N   . ALA A 1 265 ? -9.64700  -53.87600 -32.91600 1.000 29.36000  ? 284  ALA A N   1 
ATOM   2051  C CA  . ALA A 1 265 ? -8.56000  -54.07400 -33.87000 1.000 34.20000  ? 284  ALA A CA  1 
ATOM   2052  C C   . ALA A 1 265 ? -7.81400  -52.75800 -34.06500 1.000 33.12000  ? 284  ALA A C   1 
ATOM   2053  O O   . ALA A 1 265 ? -8.35800  -51.80500 -34.63400 1.000 35.17000  ? 284  ALA A O   1 
ATOM   2054  C CB  . ALA A 1 265 ? -9.09900  -54.58900 -35.20200 1.000 32.99000  ? 284  ALA A CB  1 
ATOM   2055  N N   . GLY A 1 266 ? -6.56200  -52.71500 -33.62800 1.000 25.79000  ? 285  GLY A N   1 
ATOM   2056  C CA  . GLY A 1 266 ? -5.72800  -51.53000 -33.75300 1.000 29.85000  ? 285  GLY A CA  1 
ATOM   2057  C C   . GLY A 1 266 ? -4.66500  -51.73500 -34.81200 1.000 27.51000  ? 285  GLY A C   1 
ATOM   2058  O O   . GLY A 1 266 ? -4.18000  -52.85100 -35.01800 1.000 30.40000  ? 285  GLY A O   1 
ATOM   2059  N N   . ILE A 1 267 ? -4.30600  -50.65800 -35.49700 1.000 25.66000  ? 286  ILE A N   1 
ATOM   2060  C CA  . ILE A 1 267 ? -3.29100  -50.71000 -36.54000 1.000 33.18000  ? 286  ILE A CA  1 
ATOM   2061  C C   . ILE A 1 267 ? -2.02700  -50.05700 -36.01300 1.000 31.88000  ? 286  ILE A C   1 
ATOM   2062  O O   . ILE A 1 267 ? -2.06100  -48.92500 -35.51400 1.000 30.00000  ? 286  ILE A O   1 
ATOM   2063  C CB  . ILE A 1 267 ? -3.76100  -50.04400 -37.84400 1.000 28.71000  ? 286  ILE A CB  1 
ATOM   2064  C CG1 . ILE A 1 267 ? -4.91700  -50.83200 -38.44400 1.000 28.29000  ? 286  ILE A CG1 1 
ATOM   2065  C CG2 . ILE A 1 267 ? -2.63600  -49.96600 -38.84900 1.000 26.50000  ? 286  ILE A CG2 1 
ATOM   2066  C CD1 . ILE A 1 267 ? -5.55200  -50.12500 -39.61500 1.000 36.41000  ? 286  ILE A CD1 1 
ATOM   2067  N N   . ASN A 1 268 ? -0.91800  -50.77700 -36.13000 1.000 37.65000  ? 287  ASN A N   1 
ATOM   2068  C CA  . ASN A 1 268 ? 0.36700   -50.29300 -35.65400 1.000 32.52000  ? 287  ASN A CA  1 
ATOM   2069  C C   . ASN A 1 268 ? 0.73100   -48.99800 -36.36000 1.000 35.43000  ? 287  ASN A C   1 
ATOM   2070  O O   . ASN A 1 268 ? 0.68500   -48.91500 -37.59000 1.000 39.36000  ? 287  ASN A O   1 
ATOM   2071  C CB  . ASN A 1 268 ? 1.39600   -51.38800 -35.90400 1.000 31.25000  ? 287  ASN A CB  1 
ATOM   2072  C CG  . ASN A 1 268 ? 2.75900   -51.10600 -35.29100 1.000 42.38000  ? 287  ASN A CG  1 
ATOM   2073  O OD1 . ASN A 1 268 ? 3.11700   -49.96800 -34.97000 1.000 41.03000  ? 287  ASN A OD1 1 
ATOM   2074  N ND2 . ASN A 1 268 ? 3.50500   -52.18200 -35.05800 1.000 38.00000  ? 287  ASN A ND2 1 
ATOM   2075  N N   . ALA A 1 269 ? 1.08900   -47.98200 -35.57100 1.000 37.47000  ? 288  ALA A N   1 
ATOM   2076  C CA  . ALA A 1 269 ? 1.48700   -46.69700 -36.14200 1.000 40.57000  ? 288  ALA A CA  1 
ATOM   2077  C C   . ALA A 1 269 ? 2.67700   -46.83900 -37.08000 1.000 40.71000  ? 288  ALA A C   1 
ATOM   2078  O O   . ALA A 1 269 ? 2.83400   -46.04100 -38.01400 1.000 36.97000  ? 288  ALA A O   1 
ATOM   2079  C CB  . ALA A 1 269 ? 1.82300   -45.70100 -35.02900 1.000 35.78000  ? 288  ALA A CB  1 
ATOM   2080  N N   . ALA A 1 270 ? 3.53000   -47.83100 -36.84200 1.000 41.04000  ? 289  ALA A N   1 
ATOM   2081  C CA  . ALA A 1 270 ? 4.73700   -48.01200 -37.63600 1.000 43.37000  ? 289  ALA A CA  1 
ATOM   2082  C C   . ALA A 1 270 ? 4.52100   -48.90200 -38.84600 1.000 43.43000  ? 289  ALA A C   1 
ATOM   2083  O O   . ALA A 1 270 ? 5.48600   -49.18900 -39.55900 1.000 45.14000  ? 289  ALA A O   1 
ATOM   2084  C CB  . ALA A 1 270 ? 5.86000   -48.59600 -36.77500 1.000 32.33000  ? 289  ALA A CB  1 
ATOM   2085  N N   . SER A 1 271 ? 3.30300   -49.35700 -39.09200 1.000 38.62000  ? 290  SER A N   1 
ATOM   2086  C CA  . SER A 1 271 ? 3.07900   -50.23900 -40.22600 1.000 36.17000  ? 290  SER A CA  1 
ATOM   2087  C C   . SER A 1 271 ? 3.16400   -49.45000 -41.52800 1.000 39.75000  ? 290  SER A C   1 
ATOM   2088  O O   . SER A 1 271 ? 2.57900   -48.36600 -41.63100 1.000 41.46000  ? 290  SER A O   1 
ATOM   2089  C CB  . SER A 1 271 ? 1.72700   -50.92800 -40.12400 1.000 32.40000  ? 290  SER A CB  1 
ATOM   2090  O OG  . SER A 1 271 ? 1.49100   -51.72600 -41.27600 1.000 36.33000  ? 290  SER A OG  1 
ATOM   2091  N N   . PRO A 1 272 ? 3.88300   -49.94700 -42.53500 1.000 42.05000  ? 291  PRO A N   1 
ATOM   2092  C CA  . PRO A 1 272 ? 3.81900   -49.33400 -43.86500 1.000 41.67000  ? 291  PRO A CA  1 
ATOM   2093  C C   . PRO A 1 272 ? 2.61500   -49.78700 -44.66800 1.000 37.59000  ? 291  PRO A C   1 
ATOM   2094  O O   . PRO A 1 272 ? 2.44400   -49.34100 -45.80400 1.000 42.37000  ? 291  PRO A O   1 
ATOM   2095  C CB  . PRO A 1 272 ? 5.12700   -49.80200 -44.51700 1.000 39.95000  ? 291  PRO A CB  1 
ATOM   2096  C CG  . PRO A 1 272 ? 5.38400   -51.12800 -43.87800 1.000 40.75000  ? 291  PRO A CG  1 
ATOM   2097  C CD  . PRO A 1 272 ? 4.88000   -51.02900 -42.46500 1.000 39.89000  ? 291  PRO A CD  1 
ATOM   2098  N N   . ASN A 1 273 ? 1.77100   -50.63700 -44.08600 1.000 41.64000  ? 292  ASN A N   1 
ATOM   2099  C CA  . ASN A 1 273 ? 0.67600   -51.29700 -44.78000 1.000 33.51000  ? 292  ASN A CA  1 
ATOM   2100  C C   . ASN A 1 273 ? -0.68400  -50.82000 -44.28300 1.000 40.24000  ? 292  ASN A C   1 
ATOM   2101  O O   . ASN A 1 273 ? -1.64500  -51.59700 -44.24500 1.000 38.54000  ? 292  ASN A O   1 
ATOM   2102  C CB  . ASN A 1 273 ? 0.79500   -52.80700 -44.60400 1.000 35.57000  ? 292  ASN A CB  1 
ATOM   2103  C CG  . ASN A 1 273 ? 2.09100   -53.34900 -45.15400 1.000 38.93000  ? 292  ASN A CG  1 
ATOM   2104  O OD1 . ASN A 1 273 ? 2.56500   -52.90400 -46.19600 1.000 42.37000  ? 292  ASN A OD1 1 
ATOM   2105  N ND2 . ASN A 1 273 ? 2.67300   -54.31500 -44.45600 1.000 39.75000  ? 292  ASN A ND2 1 
ATOM   2106  N N   . LYS A 1 274 ? -0.77500  -49.54900 -43.88900 1.000 37.34000  ? 293  LYS A N   1 
ATOM   2107  C CA  . LYS A 1 274 ? -1.99200  -49.06900 -43.25000 1.000 38.21000  ? 293  LYS A CA  1 
ATOM   2108  C C   . LYS A 1 274 ? -3.21300  -49.25900 -44.14000 1.000 39.94000  ? 293  LYS A C   1 
ATOM   2109  O O   . LYS A 1 274 ? -4.26700  -49.70600 -43.66900 1.000 37.99000  ? 293  LYS A O   1 
ATOM   2110  C CB  . LYS A 1 274 ? -1.83400  -47.60300 -42.85800 1.000 37.36000  ? 293  LYS A CB  1 
ATOM   2111  C CG  . LYS A 1 274 ? -0.87000  -47.38700 -41.72100 1.000 41.53000  ? 293  LYS A CG  1 
ATOM   2112  C CD  . LYS A 1 274 ? -0.87800  -45.94400 -41.27600 1.000 45.38000  ? 293  LYS A CD  1 
ATOM   2113  C CE  . LYS A 1 274 ? -0.03800  -45.76800 -40.03700 1.000 38.95000  ? 293  LYS A CE  1 
ATOM   2114  N NZ  . LYS A 1 274 ? 1.37900   -46.01800 -40.34600 1.000 44.60000  ? 293  LYS A NZ  1 
ATOM   2115  N N   . GLU A 1 275 ? -3.08800  -48.94000 -45.43000 1.000 44.27000  ? 294  GLU A N   1 
ATOM   2116  C CA  . GLU A 1 275 ? -4.22900  -49.05100 -46.33500 1.000 44.27000  ? 294  GLU A CA  1 
ATOM   2117  C C   . GLU A 1 275 ? -4.64000  -50.49900 -46.55200 1.000 41.78000  ? 294  GLU A C   1 
ATOM   2118  O O   . GLU A 1 275 ? -5.84000  -50.80200 -46.62800 1.000 38.13000  ? 294  GLU A O   1 
ATOM   2119  C CB  . GLU A 1 275 ? -3.91100  -48.35600 -47.65200 1.000 42.71000  ? 294  GLU A CB  1 
ATOM   2120  C CG  . GLU A 1 275 ? -3.78900  -46.87700 -47.41100 1.000 53.36000  ? 294  GLU A CG  1 
ATOM   2121  C CD  . GLU A 1 275 ? -5.10300  -46.28700 -46.92700 1.000 66.20000  ? 294  GLU A CD  1 
ATOM   2122  O OE1 . GLU A 1 275 ? -6.14500  -46.57000 -47.56100 1.000 65.39000  ? 294  GLU A OE1 1 
ATOM   2123  O OE2 . GLU A 1 275 ? -5.09900  -45.65200 -45.84300 1.000 67.66000  ? 294  GLU A OE2 1 
ATOM   2124  N N   . LEU A 1 276 ? -3.66600  -51.41000 -46.63700 1.000 37.19000  ? 295  LEU A N   1 
ATOM   2125  C CA  . LEU A 1 276 ? -4.00100  -52.82800 -46.71400 1.000 38.85000  ? 295  LEU A CA  1 
ATOM   2126  C C   . LEU A 1 276 ? -4.68700  -53.30400 -45.43800 1.000 34.13000  ? 295  LEU A C   1 
ATOM   2127  O O   . LEU A 1 276 ? -5.60500  -54.13100 -45.49000 1.000 36.06000  ? 295  LEU A O   1 
ATOM   2128  C CB  . LEU A 1 276 ? -2.74600  -53.64900 -46.98900 1.000 38.55000  ? 295  LEU A CB  1 
ATOM   2129  C CG  . LEU A 1 276 ? -2.08800  -53.41600 -48.35200 1.000 43.40000  ? 295  LEU A CG  1 
ATOM   2130  C CD1 . LEU A 1 276 ? -0.76500  -54.18000 -48.45400 1.000 32.82000  ? 295  LEU A CD1 1 
ATOM   2131  C CD2 . LEU A 1 276 ? -3.03000  -53.81200 -49.46600 1.000 35.09000  ? 295  LEU A CD2 1 
ATOM   2132  N N   . ALA A 1 277 ? -4.25300  -52.79800 -44.28100 1.000 32.85000  ? 296  ALA A N   1 
ATOM   2133  C CA  . ALA A 1 277 ? -4.89100  -53.17800 -43.02300 1.000 34.22000  ? 296  ALA A CA  1 
ATOM   2134  C C   . ALA A 1 277 ? -6.33100  -52.68200 -42.95500 1.000 32.07000  ? 296  ALA A C   1 
ATOM   2135  O O   . ALA A 1 277 ? -7.22700  -53.43400 -42.55600 1.000 30.20000  ? 296  ALA A O   1 
ATOM   2136  C CB  . ALA A 1 277 ? -4.08200  -52.65100 -41.83700 1.000 27.40000  ? 296  ALA A CB  1 
ATOM   2137  N N   . LYS A 1 278 ? -6.57400  -51.42100 -43.34200 1.000 33.31000  ? 297  LYS A N   1 
ATOM   2138  C CA  . LYS A 1 278 ? -7.93800  -50.89300 -43.35000 1.000 33.55000  ? 297  LYS A CA  1 
ATOM   2139  C C   . LYS A 1 278 ? -8.80500  -51.66200 -44.32800 1.000 35.90000  ? 297  LYS A C   1 
ATOM   2140  O O   . LYS A 1 278 ? -9.97600  -51.95100 -44.04600 1.000 34.59000  ? 297  LYS A O   1 
ATOM   2141  C CB  . LYS A 1 278 ? -7.94000  -49.41500 -43.73400 1.000 33.46000  ? 297  LYS A CB  1 
ATOM   2142  C CG  . LYS A 1 278 ? -6.98400  -48.62500 -42.91600 1.000 35.96000  ? 297  LYS A CG  1 
ATOM   2143  C CD  . LYS A 1 278 ? -7.02700  -47.14600 -43.16600 1.000 41.06000  ? 297  LYS A CD  1 
ATOM   2144  C CE  . LYS A 1 278 ? -5.82800  -46.52800 -42.45200 1.000 55.20000  ? 297  LYS A CE  1 
ATOM   2145  N NZ  . LYS A 1 278 ? -5.80900  -45.03900 -42.49400 1.000 64.21000  ? 297  LYS A NZ  1 
ATOM   2146  N N   . GLU A 1 279 ? -8.25300  -51.97800 -45.50000 1.000 37.70000  ? 298  GLU A N   1 
ATOM   2147  C CA  . GLU A 1 279 ? -9.00900  -52.73400 -46.49100 1.000 37.94000  ? 298  GLU A CA  1 
ATOM   2148  C C   . GLU A 1 279 ? -9.38000  -54.11000 -45.96100 1.000 33.48000  ? 298  GLU A C   1 
ATOM   2149  O O   . GLU A 1 279 ? -10.52900 -54.54700 -46.08900 1.000 34.78000  ? 298  GLU A O   1 
ATOM   2150  C CB  . GLU A 1 279 ? -8.20700  -52.85800 -47.78400 1.000 34.53000  ? 298  GLU A CB  1 
ATOM   2151  C CG  . GLU A 1 279 ? -8.93000  -53.69700 -48.81600 1.000 42.44000  ? 298  GLU A CG  1 
ATOM   2152  C CD  . GLU A 1 279 ? -8.20600  -53.77300 -50.13700 1.000 50.15000  ? 298  GLU A CD  1 
ATOM   2153  O OE1 . GLU A 1 279 ? -7.13100  -53.13800 -50.26900 1.000 56.83000  ? 298  GLU A OE1 1 
ATOM   2154  O OE2 . GLU A 1 279 ? -8.71600  -54.48000 -51.04200 1.000 47.45000  ? 298  GLU A OE2 1 
ATOM   2155  N N   . PHE A 1 280 ? -8.41700  -54.80200 -45.35200 1.000 32.98000  ? 299  PHE A N   1 
ATOM   2156  C CA  . PHE A 1 280 ? -8.68100  -56.12100 -44.78500 1.000 30.79000  ? 299  PHE A CA  1 
ATOM   2157  C C   . PHE A 1 280 ? -9.77000  -56.05900 -43.72300 1.000 32.11000  ? 299  PHE A C   1 
ATOM   2158  O O   . PHE A 1 280 ? -10.70800 -56.86600 -43.72500 1.000 32.20000  ? 299  PHE A O   1 
ATOM   2159  C CB  . PHE A 1 280 ? -7.39000  -56.69500 -44.19300 1.000 37.99000  ? 299  PHE A CB  1 
ATOM   2160  C CG  . PHE A 1 280 ? -7.60200  -57.94700 -43.39800 1.000 31.58000  ? 299  PHE A CG  1 
ATOM   2161  C CD1 . PHE A 1 280 ? -7.79300  -59.16200 -44.03000 1.000 30.82000  ? 299  PHE A CD1 1 
ATOM   2162  C CD2 . PHE A 1 280 ? -7.64400  -57.89800 -42.01400 1.000 27.41000  ? 299  PHE A CD2 1 
ATOM   2163  C CE1 . PHE A 1 280 ? -8.02300  -60.31400 -43.30000 1.000 35.40000  ? 299  PHE A CE1 1 
ATOM   2164  C CE2 . PHE A 1 280 ? -7.85900  -59.05100 -41.26500 1.000 30.30000  ? 299  PHE A CE2 1 
ATOM   2165  C CZ  . PHE A 1 280 ? -8.05100  -60.26000 -41.91100 1.000 35.91000  ? 299  PHE A CZ  1 
ATOM   2166  N N   . LEU A 1 281 ? -9.66200  -55.10000 -42.80300 1.000 31.40000  ? 300  LEU A N   1 
ATOM   2167  C CA  . LEU A 1 281 ? -10.60500 -55.03800 -41.69300 1.000 36.10000  ? 300  LEU A CA  1 
ATOM   2168  C C   . LEU A 1 281 ? -11.98000 -54.56500 -42.16000 1.000 35.22000  ? 300  LEU A C   1 
ATOM   2169  O O   . LEU A 1 281 ? -13.00300 -55.12100 -41.74600 1.000 37.00000  ? 300  LEU A O   1 
ATOM   2170  C CB  . LEU A 1 281 ? -10.04700 -54.13500 -40.58500 1.000 25.67000  ? 300  LEU A CB  1 
ATOM   2171  C CG  . LEU A 1 281 ? -8.80700  -54.64100 -39.82400 1.000 28.76000  ? 300  LEU A CG  1 
ATOM   2172  C CD1 . LEU A 1 281 ? -8.19800  -53.56000 -38.94300 1.000 24.70000  ? 300  LEU A CD1 1 
ATOM   2173  C CD2 . LEU A 1 281 ? -9.10700  -55.89100 -38.98400 1.000 23.21000  ? 300  LEU A CD2 1 
ATOM   2174  N N   . GLU A 1 282 ? -12.02800 -53.54800 -43.02400 1.000 32.74000  ? 301  GLU A N   1 
ATOM   2175  C CA  . GLU A 1 282 ? -13.32100 -52.99600 -43.42100 1.000 33.50000  ? 301  GLU A CA  1 
ATOM   2176  C C   . GLU A 1 282 ? -14.01300 -53.85600 -44.47500 1.000 34.85000  ? 301  GLU A C   1 
ATOM   2177  O O   . GLU A 1 282 ? -15.22400 -54.08600 -44.38400 1.000 31.16000  ? 301  GLU A O   1 
ATOM   2178  C CB  . GLU A 1 282 ? -13.16100 -51.55800 -43.91400 1.000 30.92000  ? 301  GLU A CB  1 
ATOM   2179  C CG  . GLU A 1 282 ? -12.66700 -50.63300 -42.82500 1.000 31.01000  ? 301  GLU A CG  1 
ATOM   2180  C CD  . GLU A 1 282 ? -12.49700 -49.20800 -43.28700 1.000 36.14000  ? 301  GLU A CD  1 
ATOM   2181  O OE1 . GLU A 1 282 ? -12.75300 -48.92200 -44.47800 1.000 34.47000  ? 301  GLU A OE1 1 
ATOM   2182  O OE2 . GLU A 1 282 ? -12.07000 -48.37600 -42.46100 1.000 32.67000  ? 301  GLU A OE2 1 
ATOM   2183  N N   . ASN A 1 283 ? -13.28200 -54.35800 -45.47300 1.000 32.55000  ? 302  ASN A N   1 
ATOM   2184  C CA  . ASN A 1 283 ? -13.93800 -55.17400 -46.48100 1.000 33.25000  ? 302  ASN A CA  1 
ATOM   2185  C C   . ASN A 1 283 ? -13.82900 -56.67500 -46.25500 1.000 31.28000  ? 302  ASN A C   1 
ATOM   2186  O O   . ASN A 1 283 ? -14.44700 -57.42800 -47.01300 1.000 33.51000  ? 302  ASN A O   1 
ATOM   2187  C CB  . ASN A 1 283 ? -13.42200 -54.85700 -47.88800 1.000 35.88000  ? 302  ASN A CB  1 
ATOM   2188  C CG  . ASN A 1 283 ? -14.02400 -53.58800 -48.44800 1.000 41.27000  ? 302  ASN A CG  1 
ATOM   2189  O OD1 . ASN A 1 283 ? -15.16700 -53.24300 -48.12700 1.000 38.50000  ? 302  ASN A OD1 1 
ATOM   2190  N ND2 . ASN A 1 283 ? -13.29300 -52.92000 -49.34200 1.000 36.23000  ? 302  ASN A ND2 1 
ATOM   2191  N N   . TYR A 1 284 ? -13.04300 -57.16000 -45.29500 1.000 29.30000  ? 303  TYR A N   1 
ATOM   2192  C CA  . TYR A 1 284 ? -13.06300 -58.61000 -45.14900 1.000 31.20000  ? 303  TYR A CA  1 
ATOM   2193  C C   . TYR A 1 284 ? -13.44600 -59.08300 -43.75800 1.000 33.75000  ? 303  TYR A C   1 
ATOM   2194  O O   . TYR A 1 284 ? -14.26600 -60.00000 -43.63900 1.000 34.48000  ? 303  TYR A O   1 
ATOM   2195  C CB  . TYR A 1 284 ? -11.74600 -59.30200 -45.58700 1.000 34.47000  ? 303  TYR A CB  1 
ATOM   2196  C CG  . TYR A 1 284 ? -11.45200 -59.21100 -47.08500 1.000 39.44000  ? 303  TYR A CG  1 
ATOM   2197  C CD1 . TYR A 1 284 ? -11.52400 -58.00600 -47.77500 1.000 37.57000  ? 303  TYR A CD1 1 
ATOM   2198  C CD2 . TYR A 1 284 ? -11.39300 -60.37300 -47.84700 1.000 41.13000  ? 303  TYR A CD2 1 
ATOM   2199  C CE1 . TYR A 1 284 ? -11.32100 -57.94100 -49.14100 1.000 37.74000  ? 303  TYR A CE1 1 
ATOM   2200  C CE2 . TYR A 1 284 ? -11.22700 -60.32600 -49.22200 1.000 42.05000  ? 303  TYR A CE2 1 
ATOM   2201  C CZ  . TYR A 1 284 ? -11.19300 -59.10700 -49.86300 1.000 42.55000  ? 303  TYR A CZ  1 
ATOM   2202  O OH  . TYR A 1 284 ? -11.02900 -59.05900 -51.23200 1.000 47.42000  ? 303  TYR A OH  1 
ATOM   2203  N N   . LEU A 1 285 ? -12.88200 -58.51200 -42.69500 1.000 33.01000  ? 304  LEU A N   1 
ATOM   2204  C CA  . LEU A 1 285 ? -13.20600 -59.02500 -41.36800 1.000 28.71000  ? 304  LEU A CA  1 
ATOM   2205  C C   . LEU A 1 285 ? -14.58100 -58.55600 -40.89900 1.000 36.80000  ? 304  LEU A C   1 
ATOM   2206  O O   . LEU A 1 285 ? -15.44600 -59.37700 -40.55200 1.000 33.72000  ? 304  LEU A O   1 
ATOM   2207  C CB  . LEU A 1 285 ? -12.12900 -58.62600 -40.37200 1.000 30.98000  ? 304  LEU A CB  1 
ATOM   2208  C CG  . LEU A 1 285 ? -12.43300 -59.17000 -38.98100 1.000 33.03000  ? 304  LEU A CG  1 
ATOM   2209  C CD1 . LEU A 1 285 ? -12.59200 -60.68500 -39.02200 1.000 29.26000  ? 304  LEU A CD1 1 
ATOM   2210  C CD2 . LEU A 1 285 ? -11.32500 -58.75400 -38.01500 1.000 26.39000  ? 304  LEU A CD2 1 
ATOM   2211  N N   . LEU A 1 286 ? -14.81100 -57.24000 -40.89000 1.000 32.98000  ? 305  LEU A N   1 
ATOM   2212  C CA  . LEU A 1 286 ? -16.06300 -56.68000 -40.36600 1.000 35.18000  ? 305  LEU A CA  1 
ATOM   2213  C C   . LEU A 1 286 ? -17.16200 -56.76400 -41.43200 1.000 37.93000  ? 305  LEU A C   1 
ATOM   2214  O O   . LEU A 1 286 ? -17.65000 -55.77000 -41.97700 1.000 32.51000  ? 305  LEU A O   1 
ATOM   2215  C CB  . LEU A 1 286 ? -15.82200 -55.26300 -39.86900 1.000 38.22000  ? 305  LEU A CB  1 
ATOM   2216  C CG  . LEU A 1 286 ? -15.03100 -55.24500 -38.55200 1.000 29.43000  ? 305  LEU A CG  1 
ATOM   2217  C CD1 . LEU A 1 286 ? -14.43200 -53.88800 -38.27100 1.000 22.24000  ? 305  LEU A CD1 1 
ATOM   2218  C CD2 . LEU A 1 286 ? -15.98700 -55.63800 -37.43300 1.000 22.44000  ? 305  LEU A CD2 1 
ATOM   2219  N N   . THR A 1 287 ? -17.53500 -58.00800 -41.73000 1.000 32.20000  ? 306  THR A N   1 
ATOM   2220  C CA  . THR A 1 287 ? -18.60600 -58.35300 -42.65000 1.000 32.25000  ? 306  THR A CA  1 
ATOM   2221  C C   . THR A 1 287 ? -19.25900 -59.61400 -42.10100 1.000 31.79000  ? 306  THR A C   1 
ATOM   2222  O O   . THR A 1 287 ? -18.65600 -60.32700 -41.29900 1.000 31.31000  ? 306  THR A O   1 
ATOM   2223  C CB  . THR A 1 287 ? -18.08200 -58.60000 -44.07800 1.000 34.30000  ? 306  THR A CB  1 
ATOM   2224  O OG1 . THR A 1 287 ? -17.23300 -59.75800 -44.08100 1.000 34.74000  ? 306  THR A OG1 1 
ATOM   2225  C CG2 . THR A 1 287 ? -17.32100 -57.39000 -44.63600 1.000 33.64000  ? 306  THR A CG2 1 
ATOM   2226  N N   . ASP A 1 288 ? -20.50100 -59.89000 -42.52800 1.000 34.10000  ? 307  ASP A N   1 
ATOM   2227  C CA  . ASP A 1 288 ? -21.15700 -61.11800 -42.07800 1.000 35.70000  ? 307  ASP A CA  1 
ATOM   2228  C C   . ASP A 1 288 ? -20.24500 -62.32100 -42.28900 1.000 36.55000  ? 307  ASP A C   1 
ATOM   2229  O O   . ASP A 1 288 ? -20.04700 -63.12400 -41.37500 1.000 38.17000  ? 307  ASP A O   1 
ATOM   2230  C CB  . ASP A 1 288 ? -22.49000 -61.35500 -42.80300 1.000 37.74000  ? 307  ASP A CB  1 
ATOM   2231  C CG  . ASP A 1 288 ? -23.57000 -60.35400 -42.42200 1.000 40.10000  ? 307  ASP A CG  1 
ATOM   2232  O OD1 . ASP A 1 288 ? -23.48900 -59.78000 -41.32800 1.000 42.01000  ? 307  ASP A OD1 1 
ATOM   2233  O OD2 . ASP A 1 288 ? -24.52100 -60.16900 -43.21600 1.000 47.64000  ? 307  ASP A OD2 1 
ATOM   2234  N N   . GLU A 1 289 ? -19.65300 -62.45200 -43.48400 1.000 41.43000  ? 308  GLU A N   1 
ATOM   2235  C CA  . GLU A 1 289 ? -18.85900 -63.65300 -43.74200 1.000 44.03000  ? 308  GLU A CA  1 
ATOM   2236  C C   . GLU A 1 289 ? -17.53500 -63.62600 -42.99500 1.000 34.36000  ? 308  GLU A C   1 
ATOM   2237  O O   . GLU A 1 289 ? -17.03800 -64.68400 -42.59700 1.000 34.80000  ? 308  GLU A O   1 
ATOM   2238  C CB  . GLU A 1 289 ? -18.64300 -63.87800 -45.24500 1.000 39.02000  ? 308  GLU A CB  1 
ATOM   2239  C CG  . GLU A 1 289 ? -19.92100 -64.25800 -45.92000 1.000 64.77000  ? 308  GLU A CG  1 
ATOM   2240  C CD  . GLU A 1 289 ? -20.69000 -63.12000 -46.59400 1.000 78.49000  ? 308  GLU A CD  1 
ATOM   2241  O OE1 . GLU A 1 289 ? -20.03100 -62.16200 -47.11200 1.000 84.57000  ? 308  GLU A OE1 1 
ATOM   2242  O OE2 . GLU A 1 289 ? -21.88600 -63.12700 -46.51000 1.000 71.29000  ? 308  GLU A OE2 1 
ATOM   2243  N N   . GLY A 1 290 ? -16.96200 -62.44300 -42.75800 1.000 30.20000  ? 309  GLY A N   1 
ATOM   2244  C CA  . GLY A 1 290 ? -15.73700 -62.38500 -41.96700 1.000 34.19000  ? 309  GLY A CA  1 
ATOM   2245  C C   . GLY A 1 290 ? -15.92400 -62.80600 -40.51400 1.000 40.41000  ? 309  GLY A C   1 
ATOM   2246  O O   . GLY A 1 290 ? -15.19900 -63.66900 -40.00000 1.000 40.10000  ? 309  GLY A O   1 
ATOM   2247  N N   . LEU A 1 291 ? -16.88300 -62.18500 -39.82100 1.000 36.49000  ? 310  LEU A N   1 
ATOM   2248  C CA  . LEU A 1 291 ? -17.10600 -62.51400 -38.41400 1.000 35.87000  ? 310  LEU A CA  1 
ATOM   2249  C C   . LEU A 1 291 ? -17.60400 -63.94800 -38.24700 1.000 34.91000  ? 310  LEU A C   1 
ATOM   2250  O O   . LEU A 1 291 ? -17.22500 -64.63600 -37.29500 1.000 43.70000  ? 310  LEU A O   1 
ATOM   2251  C CB  . LEU A 1 291 ? -18.07700 -61.51100 -37.79000 1.000 37.92000  ? 310  LEU A CB  1 
ATOM   2252  C CG  . LEU A 1 291 ? -17.46100 -60.11100 -37.66000 1.000 36.11000  ? 310  LEU A CG  1 
ATOM   2253  C CD1 . LEU A 1 291 ? -18.43900 -59.12800 -37.01600 1.000 34.99000  ? 310  LEU A CD1 1 
ATOM   2254  C CD2 . LEU A 1 291 ? -16.15700 -60.19200 -36.87400 1.000 30.24000  ? 310  LEU A CD2 1 
ATOM   2255  N N   . GLU A 1 292 ? -18.34900 -64.42300 -39.22700 1.000 39.77000  ? 311  GLU A N   1 
ATOM   2256  C CA  . GLU A 1 292 ? -18.85300 -65.80600 -39.16000 1.000 40.43000  ? 311  GLU A CA  1 
ATOM   2257  C C   . GLU A 1 292 ? -17.66300 -66.76400 -39.16500 1.000 43.41000  ? 311  GLU A C   1 
ATOM   2258  O O   . GLU A 1 292 ? -17.67700 -67.69700 -38.38800 1.000 45.51000  ? 311  GLU A O   1 
ATOM   2259  C CB  . GLU A 1 292 ? -19.86500 -66.03000 -40.27600 1.000 41.02000  ? 311  GLU A CB  1 
ATOM   2260  C CG  . GLU A 1 292 ? -19.72400 -67.36000 -40.95400 1.000 54.01000  ? 311  GLU A CG  1 
ATOM   2261  C CD  . GLU A 1 292 ? -20.72700 -68.38500 -40.48200 1.000 63.01000  ? 311  GLU A CD  1 
ATOM   2262  O OE1 . GLU A 1 292 ? -21.02100 -68.41100 -39.28800 1.000 64.19000  ? 311  GLU A OE1 1 
ATOM   2263  O OE2 . GLU A 1 292 ? -21.20500 -69.14600 -41.31900 1.000 72.74000  ? 311  GLU A OE2 1 
ATOM   2264  N N   . ALA A 1 293 ? -16.65800 -66.52100 -39.99400 1.000 35.23000  ? 312  ALA A N   1 
ATOM   2265  C CA  . ALA A 1 293 ? -15.50700 -67.41900 -40.00800 1.000 40.58000  ? 312  ALA A CA  1 
ATOM   2266  C C   . ALA A 1 293 ? -14.83100 -67.46600 -38.64600 1.000 40.03000  ? 312  ALA A C   1 
ATOM   2267  O O   . ALA A 1 293 ? -14.44200 -68.54100 -38.17200 1.000 39.94000  ? 312  ALA A O   1 
ATOM   2268  C CB  . ALA A 1 293 ? -14.51200 -66.98600 -41.08500 1.000 38.44000  ? 312  ALA A CB  1 
ATOM   2269  N N   . VAL A 1 294 ? -14.68200 -66.30800 -38.00200 1.000 38.41000  ? 313  VAL A N   1 
ATOM   2270  C CA  . VAL A 1 294 ? -14.05800 -66.26900 -36.68500 1.000 41.87000  ? 313  VAL A CA  1 
ATOM   2271  C C   . VAL A 1 294 ? -14.96900 -66.91100 -35.64800 1.000 44.21000  ? 313  VAL A C   1 
ATOM   2272  O O   . VAL A 1 294 ? -14.54300 -67.78400 -34.88000 1.000 47.38000  ? 313  VAL A O   1 
ATOM   2273  C CB  . VAL A 1 294 ? -13.69900 -64.82300 -36.30900 1.000 37.93000  ? 313  VAL A CB  1 
ATOM   2274  C CG1 . VAL A 1 294 ? -13.09300 -64.77600 -34.91200 1.000 36.69000  ? 313  VAL A CG1 1 
ATOM   2275  C CG2 . VAL A 1 294 ? -12.74400 -64.23100 -37.34400 1.000 38.53000  ? 313  VAL A CG2 1 
ATOM   2276  N N   . ASN A 1 295 ? -16.24400 -66.50700 -35.63100 1.000 44.17000  ? 314  ASN A N   1 
ATOM   2277  C CA  . ASN A 1 295 ? -17.20100 -67.04300 -34.66300 1.000 38.22000  ? 314  ASN A CA  1 
ATOM   2278  C C   . ASN A 1 295 ? -17.30800 -68.55700 -34.77700 1.000 41.47000  ? 314  ASN A C   1 
ATOM   2279  O O   . ASN A 1 295 ? -17.46100 -69.25900 -33.77200 1.000 41.93000  ? 314  ASN A O   1 
ATOM   2280  C CB  . ASN A 1 295 ? -18.58200 -66.44500 -34.90400 1.000 39.23000  ? 314  ASN A CB  1 
ATOM   2281  C CG  . ASN A 1 295 ? -19.50700 -66.62200 -33.72300 1.000 42.30000  ? 314  ASN A CG  1 
ATOM   2282  O OD1 . ASN A 1 295 ? -19.07000 -66.63900 -32.57400 1.000 44.11000  ? 314  ASN A OD1 1 
ATOM   2283  N ND2 . ASN A 1 295 ? -20.76600 -66.92000 -34.00900 1.000 48.47000  ? 314  ASN A ND2 1 
ATOM   2284  N N   . LYS A 1 296 ? -17.30300 -69.06300 -36.00700 1.000 39.78000  ? 315  LYS A N   1 
ATOM   2285  C CA  . LYS A 1 296 ? -17.35200 -70.49800 -36.25200 1.000 42.77000  ? 315  LYS A CA  1 
ATOM   2286  C C   . LYS A 1 296 ? -16.16200 -71.21200 -35.59000 1.000 51.44000  ? 315  LYS A C   1 
ATOM   2287  O O   . LYS A 1 296 ? -16.30400 -72.32100 -35.05500 1.000 52.64000  ? 315  LYS A O   1 
ATOM   2288  C CB  . LYS A 1 296 ? -17.47600 -70.66600 -37.78200 1.000 49.93000  ? 315  LYS A CB  1 
ATOM   2289  C CG  . LYS A 1 296 ? -17.40300 -72.03900 -38.45600 1.000 62.47000  ? 315  LYS A CG  1 
ATOM   2290  C CD  . LYS A 1 296 ? -18.15800 -72.09100 -39.78800 1.000 57.55000  ? 315  LYS A CD  1 
ATOM   2291  C CE  . LYS A 1 296 ? -17.53700 -73.10100 -40.61600 1.000 66.36000  ? 315  LYS A CE  1 
ATOM   2292  N NZ  . LYS A 1 296 ? -17.93700 -74.36100 -40.05300 1.000 63.28000  ? 315  LYS A NZ  1 
ATOM   2293  N N   . ASP A 1 297 ? -15.00500 -70.54700 -35.52900 1.000 48.56000  ? 316  ASP A N   1 
ATOM   2294  C CA  . ASP A 1 297 ? -13.83300 -71.15100 -34.90100 1.000 47.93000  ? 316  ASP A CA  1 
ATOM   2295  C C   . ASP A 1 297 ? -13.97500 -71.14700 -33.37900 1.000 52.23000  ? 316  ASP A C   1 
ATOM   2296  O O   . ASP A 1 297 ? -13.98700 -72.20700 -32.73800 1.000 51.40000  ? 316  ASP A O   1 
ATOM   2297  C CB  . ASP A 1 297 ? -12.57000 -70.41100 -35.36800 1.000 45.71000  ? 316  ASP A CB  1 
ATOM   2298  C CG  . ASP A 1 297 ? -11.28500 -71.19300 -35.09600 1.000 52.17000  ? 316  ASP A CG  1 
ATOM   2299  O OD1 . ASP A 1 297 ? -11.16300 -72.32300 -35.62000 1.000 50.66000  ? 316  ASP A OD1 1 
ATOM   2300  O OD2 . ASP A 1 297 ? -10.35800 -70.65300 -34.45000 1.000 46.91000  ? 316  ASP A OD2 1 
ATOM   2301  N N   . LYS A 1 298 ? -14.11500 -69.95900 -32.78100 1.000 45.13000  ? 317  LYS A N   1 
ATOM   2302  C CA  . LYS A 1 298 ? -14.33600 -69.82800 -31.35600 1.000 41.50000  ? 317  LYS A CA  1 
ATOM   2303  C C   . LYS A 1 298 ? -15.32100 -68.67700 -31.19500 1.000 49.46000  ? 317  LYS A C   1 
ATOM   2304  O O   . LYS A 1 298 ? -15.14500 -67.62700 -31.84000 1.000 48.66000  ? 317  LYS A O   1 
ATOM   2305  C CB  . LYS A 1 298 ? -13.04500 -69.54400 -30.59300 1.000 48.94000  ? 317  LYS A CB  1 
ATOM   2306  C CG  . LYS A 1 298 ? -12.01900 -70.63500 -30.74600 1.000 49.65000  ? 317  LYS A CG  1 
ATOM   2307  C CD  . LYS A 1 298 ? -10.75000 -70.26400 -30.04500 1.000 52.43000  ? 317  LYS A CD  1 
ATOM   2308  C CE  . LYS A 1 298 ? -9.63900  -71.23000 -30.41100 1.000 57.35000  ? 317  LYS A CE  1 
ATOM   2309  N NZ  . LYS A 1 298 ? -8.33800  -70.80600 -29.81700 1.000 51.33000  ? 317  LYS A NZ  1 
ATOM   2310  N N   . PRO A 1 299 ? -16.34800 -68.82700 -30.36000 1.000 42.85000  ? 318  PRO A N   1 
ATOM   2311  C CA  . PRO A 1 299 ? -17.43100 -67.83800 -30.34200 1.000 47.53000  ? 318  PRO A CA  1 
ATOM   2312  C C   . PRO A 1 299 ? -16.93800 -66.46700 -29.89900 1.000 42.36000  ? 318  PRO A C   1 
ATOM   2313  O O   . PRO A 1 299 ? -16.19200 -66.33800 -28.92700 1.000 39.70000  ? 318  PRO A O   1 
ATOM   2314  C CB  . PRO A 1 299 ? -18.43400 -68.42600 -29.34000 1.000 51.85000  ? 318  PRO A CB  1 
ATOM   2315  C CG  . PRO A 1 299 ? -18.08400 -69.88700 -29.25200 1.000 53.36000  ? 318  PRO A CG  1 
ATOM   2316  C CD  . PRO A 1 299 ? -16.59400 -69.92500 -29.41400 1.000 42.76000  ? 318  PRO A CD  1 
ATOM   2317  N N   . LEU A 1 300 ? -17.37700 -65.43700 -30.62000 1.000 37.81000  ? 319  LEU A N   1 
ATOM   2318  C CA  . LEU A 1 300 ? -17.05600 -64.06300 -30.26100 1.000 32.31000  ? 319  LEU A CA  1 
ATOM   2319  C C   . LEU A 1 300 ? -17.97200 -63.50200 -29.17900 1.000 43.25000  ? 319  LEU A C   1 
ATOM   2320  O O   . LEU A 1 300 ? -17.63200 -62.48300 -28.56100 1.000 37.75000  ? 319  LEU A O   1 
ATOM   2321  C CB  . LEU A 1 300 ? -17.12600 -63.18600 -31.51100 1.000 35.02000  ? 319  LEU A CB  1 
ATOM   2322  C CG  . LEU A 1 300 ? -16.04000 -63.43700 -32.57100 1.000 41.38000  ? 319  LEU A CG  1 
ATOM   2323  C CD1 . LEU A 1 300 ? -16.42700 -62.82500 -33.90300 1.000 36.39000  ? 319  LEU A CD1 1 
ATOM   2324  C CD2 . LEU A 1 300 ? -14.71000 -62.86000 -32.10900 1.000 29.93000  ? 319  LEU A CD2 1 
ATOM   2325  N N   . GLY A 1 301 ? -19.11300 -64.14200 -28.92000 1.000 31.93000  ? 320  GLY A N   1 
ATOM   2326  C CA  . GLY A 1 301 ? -20.11900 -63.50100 -28.09400 1.000 31.96000  ? 320  GLY A CA  1 
ATOM   2327  C C   . GLY A 1 301 ? -20.95300 -62.52500 -28.90900 1.000 37.11000  ? 320  GLY A C   1 
ATOM   2328  O O   . GLY A 1 301 ? -21.25500 -62.76000 -30.08100 1.000 36.55000  ? 320  GLY A O   1 
ATOM   2329  N N   . ALA A 1 302 ? -21.34600 -61.42200 -28.27100 1.000 32.34000  ? 321  ALA A N   1 
ATOM   2330  C CA  . ALA A 1 302 ? -22.01400 -60.35000 -28.99800 1.000 33.08000  ? 321  ALA A CA  1 
ATOM   2331  C C   . ALA A 1 302 ? -20.99300 -59.57800 -29.82200 1.000 35.40000  ? 321  ALA A C   1 
ATOM   2332  O O   . ALA A 1 302 ? -19.85700 -59.37000 -29.38000 1.000 33.14000  ? 321  ALA A O   1 
ATOM   2333  C CB  . ALA A 1 302 ? -22.73400 -59.41400 -28.03100 1.000 30.92000  ? 321  ALA A CB  1 
ATOM   2334  N N   . VAL A 1 303 ? -21.38700 -59.14900 -31.02700 1.000 29.98000  ? 322  VAL A N   1 
ATOM   2335  C CA  . VAL A 1 303 ? -20.43600 -58.50500 -31.92600 1.000 31.75000  ? 322  VAL A CA  1 
ATOM   2336  C C   . VAL A 1 303 ? -20.90900 -57.09800 -32.24700 1.000 32.17000  ? 322  VAL A C   1 
ATOM   2337  O O   . VAL A 1 303 ? -22.08700 -56.76700 -32.10100 1.000 27.14000  ? 322  VAL A O   1 
ATOM   2338  C CB  . VAL A 1 303 ? -20.21700 -59.30500 -33.21900 1.000 35.28000  ? 322  VAL A CB  1 
ATOM   2339  C CG1 . VAL A 1 303 ? -19.55500 -60.64000 -32.91000 1.000 29.95000  ? 322  VAL A CG1 1 
ATOM   2340  C CG2 . VAL A 1 303 ? -21.53900 -59.49800 -33.93200 1.000 34.10000  ? 322  VAL A CG2 1 
ATOM   2341  N N   . ALA A 1 304 ? -19.96100 -56.26400 -32.70000 1.000 25.84000  ? 323  ALA A N   1 
ATOM   2342  C CA  . ALA A 1 304 ? -20.24100 -54.85900 -32.96900 1.000 28.36000  ? 323  ALA A CA  1 
ATOM   2343  C C   . ALA A 1 304 ? -20.94300 -54.62100 -34.30700 1.000 31.37000  ? 323  ALA A C   1 
ATOM   2344  O O   . ALA A 1 304 ? -21.46400 -53.51400 -34.53200 1.000 24.59000  ? 323  ALA A O   1 
ATOM   2345  C CB  . ALA A 1 304 ? -18.93800 -54.05600 -32.91000 1.000 23.83000  ? 323  ALA A CB  1 
ATOM   2346  N N   . LEU A 1 305 ? -20.99600 -55.62700 -35.18100 1.000 29.22000  ? 324  LEU A N   1 
ATOM   2347  C CA  . LEU A 1 305 ? -21.58100 -55.49300 -36.51400 1.000 32.66000  ? 324  LEU A CA  1 
ATOM   2348  C C   . LEU A 1 305 ? -23.07200 -55.81200 -36.44100 1.000 31.95000  ? 324  LEU A C   1 
ATOM   2349  O O   . LEU A 1 305 ? -23.45300 -56.95900 -36.18400 1.000 33.38000  ? 324  LEU A O   1 
ATOM   2350  C CB  . LEU A 1 305 ? -20.88600 -56.43100 -37.49600 1.000 28.13000  ? 324  LEU A CB  1 
ATOM   2351  C CG  . LEU A 1 305 ? -21.32100 -56.31800 -38.95800 1.000 34.84000  ? 324  LEU A CG  1 
ATOM   2352  C CD1 . LEU A 1 305 ? -20.76500 -55.04500 -39.60000 1.000 31.42000  ? 324  LEU A CD1 1 
ATOM   2353  C CD2 . LEU A 1 305 ? -20.91300 -57.56000 -39.72600 1.000 35.65000  ? 324  LEU A CD2 1 
ATOM   2354  N N   . LYS A 1 306 ? -23.91500 -54.81100 -36.70800 1.000 31.07000  ? 325  LYS A N   1 
ATOM   2355  C CA  . LYS A 1 306 ? -25.35100 -54.95200 -36.46200 1.000 36.50000  ? 325  LYS A CA  1 
ATOM   2356  C C   . LYS A 1 306 ? -25.95100 -56.13000 -37.21700 1.000 34.03000  ? 325  LYS A C   1 
ATOM   2357  O O   . LYS A 1 306 ? -26.69900 -56.92900 -36.64500 1.000 36.20000  ? 325  LYS A O   1 
ATOM   2358  C CB  . LYS A 1 306 ? -26.07300 -53.65200 -36.82200 1.000 28.82000  ? 325  LYS A CB  1 
ATOM   2359  C CG  . LYS A 1 306 ? -25.59400 -52.52700 -35.93900 1.000 34.49000  ? 325  LYS A CG  1 
ATOM   2360  C CD  . LYS A 1 306 ? -26.40500 -51.26100 -36.01900 1.000 32.74000  ? 325  LYS A CD  1 
ATOM   2361  C CE  . LYS A 1 306 ? -26.07000 -50.44600 -37.22900 1.000 36.11000  ? 325  LYS A CE  1 
ATOM   2362  N NZ  . LYS A 1 306 ? -26.61000 -49.07000 -37.04600 1.000 46.61000  ? 325  LYS A NZ  1 
ATOM   2363  N N   . SER A 1 307 ? -25.63700 -56.26100 -38.50400 1.000 34.37000  ? 326  SER A N   1 
ATOM   2364  C CA  . SER A 1 307 ? -26.25800 -57.32100 -39.29200 1.000 35.73000  ? 326  SER A CA  1 
ATOM   2365  C C   . SER A 1 307 ? -25.92100 -58.70200 -38.72900 1.000 37.23000  ? 326  SER A C   1 
ATOM   2366  O O   . SER A 1 307 ? -26.81000 -59.53900 -38.54500 1.000 40.00000  ? 326  SER A O   1 
ATOM   2367  C CB  . SER A 1 307 ? -25.85400 -57.18900 -40.76200 1.000 30.22000  ? 326  SER A CB  1 
ATOM   2368  O OG  . SER A 1 307 ? -24.45400 -57.30500 -40.96400 1.000 29.83000  ? 326  SER A OG  1 
ATOM   2369  N N   . TYR A 1 308 ? -24.65100 -58.94900 -38.40300 1.000 33.48000  ? 327  TYR A N   1 
ATOM   2370  C CA  . TYR A 1 308 ? -24.30600 -60.27000 -37.88200 1.000 37.21000  ? 327  TYR A CA  1 
ATOM   2371  C C   . TYR A 1 308 ? -24.73600 -60.43400 -36.42200 1.000 33.98000  ? 327  TYR A C   1 
ATOM   2372  O O   . TYR A 1 308 ? -25.01200 -61.55500 -35.98600 1.000 34.75000  ? 327  TYR A O   1 
ATOM   2373  C CB  . TYR A 1 308 ? -22.80300 -60.55300 -38.06600 1.000 35.47000  ? 327  TYR A CB  1 
ATOM   2374  C CG  . TYR A 1 308 ? -22.43900 -61.99900 -37.75400 1.000 38.68000  ? 327  TYR A CG  1 
ATOM   2375  C CD1 . TYR A 1 308 ? -23.01200 -63.05100 -38.47700 1.000 38.92000  ? 327  TYR A CD1 1 
ATOM   2376  C CD2 . TYR A 1 308 ? -21.50000 -62.31400 -36.78200 1.000 34.76000  ? 327  TYR A CD2 1 
ATOM   2377  C CE1 . TYR A 1 308 ? -22.69400 -64.37700 -38.20500 1.000 35.68000  ? 327  TYR A CE1 1 
ATOM   2378  C CE2 . TYR A 1 308 ? -21.17100 -63.64100 -36.50600 1.000 36.16000  ? 327  TYR A CE2 1 
ATOM   2379  C CZ  . TYR A 1 308 ? -21.77500 -64.66500 -37.21600 1.000 39.19000  ? 327  TYR A CZ  1 
ATOM   2380  O OH  . TYR A 1 308 ? -21.44800 -65.97600 -36.93700 1.000 40.45000  ? 327  TYR A OH  1 
ATOM   2381  N N   . GLU A 1 309 ? -24.81900 -59.34300 -35.65600 1.000 34.93000  ? 328  GLU A N   1 
ATOM   2382  C CA  . GLU A 1 309 ? -25.31300 -59.45400 -34.28400 1.000 42.03000  ? 328  GLU A CA  1 
ATOM   2383  C C   . GLU A 1 309 ? -26.76700 -59.91700 -34.25200 1.000 39.22000  ? 328  GLU A C   1 
ATOM   2384  O O   . GLU A 1 309 ? -27.14900 -60.72500 -33.39500 1.000 33.19000  ? 328  GLU A O   1 
ATOM   2385  C CB  . GLU A 1 309 ? -25.14300 -58.12400 -33.54000 1.000 32.94000  ? 328  GLU A CB  1 
ATOM   2386  C CG  . GLU A 1 309 ? -25.87900 -58.05600 -32.18800 1.000 39.37000  ? 328  GLU A CG  1 
ATOM   2387  C CD  . GLU A 1 309 ? -25.43700 -59.11600 -31.17900 1.000 40.06000  ? 328  GLU A CD  1 
ATOM   2388  O OE1 . GLU A 1 309 ? -24.27600 -59.57900 -31.26200 1.000 36.16000  ? 328  GLU A OE1 1 
ATOM   2389  O OE2 . GLU A 1 309 ? -26.26200 -59.49100 -30.30400 1.000 38.88000  ? 328  GLU A OE2 1 
ATOM   2390  N N   . GLU A 1 310 ? -27.58800 -59.42700 -35.18400 1.000 36.77000  ? 329  GLU A N   1 
ATOM   2391  C CA  . GLU A 1 310 ? -28.96900 -59.89300 -35.25500 1.000 40.43000  ? 329  GLU A CA  1 
ATOM   2392  C C   . GLU A 1 310 ? -29.03800 -61.38100 -35.55800 1.000 41.48000  ? 329  GLU A C   1 
ATOM   2393  O O   . GLU A 1 310 ? -30.01000 -62.04100 -35.17800 1.000 39.85000  ? 329  GLU A O   1 
ATOM   2394  C CB  . GLU A 1 310 ? -29.73800 -59.10100 -36.31400 1.000 38.43000  ? 329  GLU A CB  1 
ATOM   2395  C CG  . GLU A 1 310 ? -29.76400 -57.60600 -36.00700 1.000 48.51000  ? 329  GLU A CG  1 
ATOM   2396  C CD  . GLU A 1 310 ? -30.35900 -56.76200 -37.13700 1.000 64.03000  ? 329  GLU A CD  1 
ATOM   2397  O OE1 . GLU A 1 310 ? -30.80900 -57.34400 -38.15500 1.000 65.19000  ? 329  GLU A OE1 1 
ATOM   2398  O OE2 . GLU A 1 310 ? -30.26600 -55.50700 -37.04500 1.000 60.49000  ? 329  GLU A OE2 1 
ATOM   2399  N N   . GLU A 1 311 ? -28.03100 -61.93100 -36.24600 1.000 39.65000  ? 330  GLU A N   1 
ATOM   2400  C CA  . GLU A 1 311 ? -28.02300 -63.37400 -36.44700 1.000 39.96000  ? 330  GLU A CA  1 
ATOM   2401  C C   . GLU A 1 311 ? -27.67400 -64.09700 -35.15600 1.000 42.69000  ? 330  GLU A C   1 
ATOM   2402  O O   . GLU A 1 311 ? -28.34300 -65.06500 -34.76900 1.000 39.46000  ? 330  GLU A O   1 
ATOM   2403  C CB  . GLU A 1 311 ? -27.04600 -63.76800 -37.55200 1.000 39.88000  ? 330  GLU A CB  1 
ATOM   2404  C CG  . GLU A 1 311 ? -27.19900 -65.23100 -37.94100 1.000 50.74000  ? 330  GLU A CG  1 
ATOM   2405  C CD  . GLU A 1 311 ? -28.58400 -65.51900 -38.53700 1.000 65.97000  ? 330  GLU A CD  1 
ATOM   2406  O OE1 . GLU A 1 311 ? -29.18000 -64.59800 -39.14600 1.000 61.99000  ? 330  GLU A OE1 1 
ATOM   2407  O OE2 . GLU A 1 311 ? -29.09200 -66.65400 -38.37500 1.000 65.52000  ? 330  GLU A OE2 1 
ATOM   2408  N N   . LEU A 1 312 ? -26.62700 -63.62600 -34.46900 1.000 37.39000  ? 331  LEU A N   1 
ATOM   2409  C CA  . LEU A 1 312 ? -26.17600 -64.28000 -33.24600 1.000 32.69000  ? 331  LEU A CA  1 
ATOM   2410  C C   . LEU A 1 312 ? -27.20400 -64.13700 -32.13900 1.000 38.40000  ? 331  LEU A C   1 
ATOM   2411  O O   . LEU A 1 312 ? -27.34500 -65.03700 -31.30700 1.000 32.82000  ? 331  LEU A O   1 
ATOM   2412  C CB  . LEU A 1 312 ? -24.84400 -63.68400 -32.79800 1.000 35.53000  ? 331  LEU A CB  1 
ATOM   2413  C CG  . LEU A 1 312 ? -23.69200 -63.78500 -33.79200 1.000 36.53000  ? 331  LEU A CG  1 
ATOM   2414  C CD1 . LEU A 1 312 ? -22.49400 -63.01700 -33.27000 1.000 33.76000  ? 331  LEU A CD1 1 
ATOM   2415  C CD2 . LEU A 1 312 ? -23.35800 -65.23300 -34.02700 1.000 34.44000  ? 331  LEU A CD2 1 
ATOM   2416  N N   . ALA A 1 313 ? -27.94600 -63.02500 -32.13900 1.000 38.26000  ? 332  ALA A N   1 
ATOM   2417  C CA  . ALA A 1 313 ? -28.89400 -62.70200 -31.08300 1.000 38.11000  ? 332  ALA A CA  1 
ATOM   2418  C C   . ALA A 1 313 ? -30.09100 -63.64000 -31.03800 1.000 39.65000  ? 332  ALA A C   1 
ATOM   2419  O O   . ALA A 1 313 ? -30.84000 -63.59400 -30.05900 1.000 43.66000  ? 332  ALA A O   1 
ATOM   2420  C CB  . ALA A 1 313 ? -29.38400 -61.25900 -31.22200 1.000 34.44000  ? 332  ALA A CB  1 
ATOM   2421  N N   . LYS A 1 314 ? -30.30700 -64.47700 -32.05600 1.000 39.18000  ? 333  LYS A N   1 
ATOM   2422  C CA  . LYS A 1 314 ? -31.35000 -65.49200 -31.92500 1.000 40.98000  ? 333  LYS A CA  1 
ATOM   2423  C C   . LYS A 1 314 ? -31.06900 -66.40200 -30.73300 1.000 39.89000  ? 333  LYS A C   1 
ATOM   2424  O O   . LYS A 1 314 ? -31.99200 -66.97900 -30.15700 1.000 44.98000  ? 333  LYS A O   1 
ATOM   2425  C CB  . LYS A 1 314 ? -31.47400 -66.29000 -33.22200 1.000 45.44000  ? 333  LYS A CB  1 
ATOM   2426  C CG  . LYS A 1 314 ? -32.05600 -65.46600 -34.37700 1.000 46.92000  ? 333  LYS A CG  1 
ATOM   2427  C CD  . LYS A 1 314 ? -32.07400 -66.24300 -35.68000 1.000 53.71000  ? 333  LYS A CD  1 
ATOM   2428  C CE  . LYS A 1 314 ? -32.59000 -65.38500 -36.83200 1.000 58.44000  ? 333  LYS A CE  1 
ATOM   2429  N NZ  . LYS A 1 314 ? -32.58900 -66.12500 -38.13300 1.000 56.81000  ? 333  LYS A NZ  1 
ATOM   2430  N N   . ASP A 1 315 ? -29.81200 -66.52700 -30.34500 1.000 42.44000  ? 334  ASP A N   1 
ATOM   2431  C CA  . ASP A 1 315 ? -29.44600 -67.02000 -29.02500 1.000 39.82000  ? 334  ASP A CA  1 
ATOM   2432  C C   . ASP A 1 315 ? -29.78900 -65.94900 -27.99400 1.000 37.59000  ? 334  ASP A C   1 
ATOM   2433  O O   . ASP A 1 315 ? -29.17900 -64.87200 -28.01400 1.000 36.23000  ? 334  ASP A O   1 
ATOM   2434  C CB  . ASP A 1 315 ? -27.94700 -67.35600 -29.01500 1.000 32.43000  ? 334  ASP A CB  1 
ATOM   2435  C CG  . ASP A 1 315 ? -27.46700 -67.92400 -27.69200 1.000 42.35000  ? 334  ASP A CG  1 
ATOM   2436  O OD1 . ASP A 1 315 ? -28.21900 -67.90300 -26.68900 1.000 41.48000  ? 334  ASP A OD1 1 
ATOM   2437  O OD2 . ASP A 1 315 ? -26.31500 -68.41600 -27.66600 1.000 48.89000  ? 334  ASP A OD2 1 
ATOM   2438  N N   . PRO A 1 316 ? -30.75000 -66.18400 -27.09600 1.000 36.17000  ? 335  PRO A N   1 
ATOM   2439  C CA  . PRO A 1 316 ? -31.12400 -65.13500 -26.12400 1.000 35.87000  ? 335  PRO A CA  1 
ATOM   2440  C C   . PRO A 1 316 ? -30.03100 -64.79100 -25.11300 1.000 37.02000  ? 335  PRO A C   1 
ATOM   2441  O O   . PRO A 1 316 ? -30.06700 -63.68800 -24.54400 1.000 30.62000  ? 335  PRO A O   1 
ATOM   2442  C CB  . PRO A 1 316 ? -32.36000 -65.72300 -25.43400 1.000 30.46000  ? 335  PRO A CB  1 
ATOM   2443  C CG  . PRO A 1 316 ? -32.22200 -67.19700 -25.61900 1.000 34.14000  ? 335  PRO A CG  1 
ATOM   2444  C CD  . PRO A 1 316 ? -31.55800 -67.40400 -26.94400 1.000 34.27000  ? 335  PRO A CD  1 
ATOM   2445  N N   . ARG A 1 317 ? -29.07400 -65.69000 -24.86400 1.000 33.01000  ? 336  ARG A N   1 
ATOM   2446  C CA  . ARG A 1 317 ? -27.94900 -65.34400 -24.00100 1.000 36.80000  ? 336  ARG A CA  1 
ATOM   2447  C C   . ARG A 1 317 ? -27.11300 -64.23000 -24.61800 1.000 34.40000  ? 336  ARG A C   1 
ATOM   2448  O O   . ARG A 1 317 ? -26.65100 -63.32000 -23.91500 1.000 30.93000  ? 336  ARG A O   1 
ATOM   2449  C CB  . ARG A 1 317 ? -27.08200 -66.57000 -23.76300 1.000 34.91000  ? 336  ARG A CB  1 
ATOM   2450  C CG  . ARG A 1 317 ? -27.81400 -67.73500 -23.16200 1.000 31.79000  ? 336  ARG A CG  1 
ATOM   2451  C CD  . ARG A 1 317 ? -26.83600 -68.87600 -22.99000 1.000 34.89000  ? 336  ARG A CD  1 
ATOM   2452  N NE  . ARG A 1 317 ? -26.28700 -69.29300 -24.27300 1.000 36.18000  ? 336  ARG A NE  1 
ATOM   2453  C CZ  . ARG A 1 317 ? -25.28400 -70.14800 -24.40400 1.000 38.25000  ? 336  ARG A CZ  1 
ATOM   2454  N NH1 . ARG A 1 317 ? -24.71600 -70.70800 -23.34900 1.000 40.63000  ? 336  ARG A NH1 1 
ATOM   2455  N NH2 . ARG A 1 317 ? -24.83600 -70.44400 -25.62100 1.000 32.36000  ? 336  ARG A NH2 1 
ATOM   2456  N N   . ILE A 1 318 ? -26.89700 -64.30000 -25.93300 1.000 35.27000  ? 337  ILE A N   1 
ATOM   2457  C CA  . ILE A 1 318 ? -26.14300 -63.26700 -26.63000 1.000 33.75000  ? 337  ILE A CA  1 
ATOM   2458  C C   . ILE A 1 318 ? -26.95000 -61.98100 -26.69900 1.000 32.01000  ? 337  ILE A C   1 
ATOM   2459  O O   . ILE A 1 318 ? -26.41100 -60.88000 -26.52800 1.000 39.69000  ? 337  ILE A O   1 
ATOM   2460  C CB  . ILE A 1 318 ? -25.72600 -63.76900 -28.02400 1.000 31.75000  ? 337  ILE A CB  1 
ATOM   2461  C CG1 . ILE A 1 318 ? -24.78800 -64.97000 -27.87800 1.000 34.18000  ? 337  ILE A CG1 1 
ATOM   2462  C CG2 . ILE A 1 318 ? -25.04700 -62.66300 -28.81500 1.000 31.56000  ? 337  ILE A CG2 1 
ATOM   2463  C CD1 . ILE A 1 318 ? -24.54200 -65.71900 -29.16500 1.000 44.33000  ? 337  ILE A CD1 1 
ATOM   2464  N N   . ALA A 1 319 ? -28.25700 -62.09500 -26.92500 1.000 31.85000  ? 338  ALA A N   1 
ATOM   2465  C CA  . ALA A 1 319 ? -29.10900 -60.91300 -26.94600 1.000 30.45000  ? 338  ALA A CA  1 
ATOM   2466  C C   . ALA A 1 319 ? -29.04300 -60.17000 -25.62400 1.000 30.61000  ? 338  ALA A C   1 
ATOM   2467  O O   . ALA A 1 319 ? -29.05400 -58.93400 -25.59900 1.000 32.86000  ? 338  ALA A O   1 
ATOM   2468  C CB  . ALA A 1 319 ? -30.55100 -61.31000 -27.25700 1.000 31.85000  ? 338  ALA A CB  1 
ATOM   2469  N N   . ALA A 1 320 ? -28.98200 -60.91000 -24.51100 1.000 28.01000  ? 339  ALA A N   1 
ATOM   2470  C CA  . ALA A 1 320 ? -28.89900 -60.27700 -23.19500 1.000 29.32000  ? 339  ALA A CA  1 
ATOM   2471  C C   . ALA A 1 320 ? -27.55800 -59.57900 -22.99300 1.000 33.59000  ? 339  ALA A C   1 
ATOM   2472  O O   . ALA A 1 320 ? -27.50800 -58.46700 -22.45100 1.000 33.33000  ? 339  ALA A O   1 
ATOM   2473  C CB  . ALA A 1 320 ? -29.13400 -61.32000 -22.10300 1.000 28.28000  ? 339  ALA A CB  1 
ATOM   2474  N N   . THR A 1 321 ? -26.45900 -60.21200 -23.41700 1.000 31.11000  ? 340  THR A N   1 
ATOM   2475  C CA  . THR A 1 321 ? -25.15700 -59.55100 -23.36800 1.000 28.68000  ? 340  THR A CA  1 
ATOM   2476  C C   . THR A 1 321 ? -25.20100 -58.20700 -24.08400 1.000 29.58000  ? 340  THR A C   1 
ATOM   2477  O O   . THR A 1 321 ? -24.79900 -57.17900 -23.52700 1.000 26.12000  ? 340  THR A O   1 
ATOM   2478  C CB  . THR A 1 321 ? -24.09100 -60.44300 -23.99900 1.000 27.01000  ? 340  THR A CB  1 
ATOM   2479  O OG1 . THR A 1 321 ? -24.07400 -61.70800 -23.33200 1.000 31.45000  ? 340  THR A OG1 1 
ATOM   2480  C CG2 . THR A 1 321 ? -22.73300 -59.79300 -23.89400 1.000 27.11000  ? 340  THR A CG2 1 
ATOM   2481  N N   . MET A 1 322 ? -25.72100 -58.19000 -25.31700 1.000 28.47000  ? 341  MET A N   1 
ATOM   2482  C CA  . MET A 1 322 ? -25.75800 -56.94300 -26.07500 1.000 29.08000  ? 341  MET A CA  1 
ATOM   2483  C C   . MET A 1 322 ? -26.66500 -55.91400 -25.41100 1.000 31.20000  ? 341  MET A C   1 
ATOM   2484  O O   . MET A 1 322 ? -26.32200 -54.72500 -25.35000 1.000 27.23000  ? 341  MET A O   1 
ATOM   2485  C CB  . MET A 1 322 ? -26.19500 -57.20700 -27.52300 1.000 33.09000  ? 341  MET A CB  1 
ATOM   2486  C CG  . MET A 1 322 ? -26.24200 -55.94800 -28.39600 1.000 31.54000  ? 341  MET A CG  1 
ATOM   2487  S SD  . MET A 1 322 ? -24.66500 -55.05300 -28.49700 1.000 35.72000  ? 341  MET A SD  1 
ATOM   2488  C CE  . MET A 1 322 ? -23.71900 -56.19100 -29.48300 1.000 35.40000  ? 341  MET A CE  1 
ATOM   2489  N N   . GLU A 1 323 ? -27.81900 -56.35100 -24.89200 1.000 26.97000  ? 342  GLU A N   1 
ATOM   2490  C CA  . GLU A 1 323 ? -28.75100 -55.41800 -24.25400 1.000 33.59000  ? 342  GLU A CA  1 
ATOM   2491  C C   . GLU A 1 323 ? -28.13700 -54.77200 -23.01300 1.000 35.56000  ? 342  GLU A C   1 
ATOM   2492  O O   . GLU A 1 323 ? -28.15800 -53.54300 -22.86100 1.000 36.80000  ? 342  GLU A O   1 
ATOM   2493  C CB  . GLU A 1 323 ? -30.05800 -56.13700 -23.90000 1.000 35.82000  ? 342  GLU A CB  1 
ATOM   2494  C CG  . GLU A 1 323 ? -31.11300 -55.23300 -23.27100 1.000 38.67000  ? 342  GLU A CG  1 
ATOM   2495  C CD  . GLU A 1 323 ? -32.43900 -55.93600 -23.07400 1.000 45.80000  ? 342  GLU A CD  1 
ATOM   2496  O OE1 . GLU A 1 323 ? -32.54500 -57.11400 -23.47700 1.000 51.85000  ? 342  GLU A OE1 1 
ATOM   2497  O OE2 . GLU A 1 323 ? -33.37000 -55.32400 -22.50000 1.000 46.45000  ? 342  GLU A OE2 1 
ATOM   2498  N N   . ASN A 1 324 ? -27.56700 -55.58100 -22.11700 1.000 31.09000  ? 343  ASN A N   1 
ATOM   2499  C CA  . ASN A 1 324 ? -26.89800 -55.01100 -20.95100 1.000 30.56000  ? 343  ASN A CA  1 
ATOM   2500  C C   . ASN A 1 324 ? -25.72100 -54.13800 -21.37000 1.000 32.00000  ? 343  ASN A C   1 
ATOM   2501  O O   . ASN A 1 324 ? -25.43100 -53.12100 -20.72700 1.000 29.34000  ? 343  ASN A O   1 
ATOM   2502  C CB  . ASN A 1 324 ? -26.43200 -56.12400 -20.01600 1.000 28.36000  ? 343  ASN A CB  1 
ATOM   2503  C CG  . ASN A 1 324 ? -27.58000 -56.84000 -19.34300 1.000 29.20000  ? 343  ASN A CG  1 
ATOM   2504  O OD1 . ASN A 1 324 ? -28.51400 -56.21600 -18.82300 1.000 32.87000  ? 343  ASN A OD1 1 
ATOM   2505  N ND2 . ASN A 1 324 ? -27.52900 -58.16500 -19.36700 1.000 26.73000  ? 343  ASN A ND2 1 
ATOM   2506  N N   . ALA A 1 325 ? -25.01900 -54.52900 -22.43700 1.000 29.90000  ? 344  ALA A N   1 
ATOM   2507  C CA  . ALA A 1 325 ? -23.91700 -53.71400 -22.93600 1.000 26.42000  ? 344  ALA A CA  1 
ATOM   2508  C C   . ALA A 1 325 ? -24.41000 -52.36100 -23.43400 1.000 28.64000  ? 344  ALA A C   1 
ATOM   2509  O O   . ALA A 1 325 ? -23.80700 -51.32300 -23.16400 1.000 30.50000  ? 344  ALA A O   1 
ATOM   2510  C CB  . ALA A 1 325 ? -23.19300 -54.46400 -24.04300 1.000 23.90000  ? 344  ALA A CB  1 
ATOM   2511  N N   . GLN A 1 326 ? -25.51600 -52.35200 -24.16800 1.000 30.67000  ? 345  GLN A N   1 
ATOM   2512  C CA  . GLN A 1 326 ? -26.04900 -51.09100 -24.67700 1.000 32.82000  ? 345  GLN A CA  1 
ATOM   2513  C C   . GLN A 1 326 ? -26.54100 -50.21100 -23.54700 1.000 32.27000  ? 345  GLN A C   1 
ATOM   2514  O O   . GLN A 1 326 ? -26.47400 -48.97800 -23.63200 1.000 33.16000  ? 345  GLN A O   1 
ATOM   2515  C CB  . GLN A 1 326 ? -27.17400 -51.39300 -25.66900 1.000 31.47000  ? 345  GLN A CB  1 
ATOM   2516  C CG  . GLN A 1 326 ? -26.70200 -52.00400 -26.97200 1.000 29.34000  ? 345  GLN A CG  1 
ATOM   2517  C CD  . GLN A 1 326 ? -27.84200 -52.62900 -27.75500 1.000 39.87000  ? 345  GLN A CD  1 
ATOM   2518  O OE1 . GLN A 1 326 ? -28.93800 -52.82600 -27.21500 1.000 41.07000  ? 345  GLN A OE1 1 
ATOM   2519  N NE2 . GLN A 1 326 ? -27.61300 -52.91000 -29.03000 1.000 37.06000  ? 345  GLN A NE2 1 
ATOM   2520  N N   . LYS A 1 327 ? -27.02200 -50.82400 -22.46400 1.000 29.30000  ? 346  LYS A N   1 
ATOM   2521  C CA  . LYS A 1 327 ? -27.48400 -50.10700 -21.28900 1.000 33.45000  ? 346  LYS A CA  1 
ATOM   2522  C C   . LYS A 1 327 ? -26.37600 -49.78400 -20.29900 1.000 32.54000  ? 346  LYS A C   1 
ATOM   2523  O O   . LYS A 1 327 ? -26.58800 -48.94100 -19.42300 1.000 30.92000  ? 346  LYS A O   1 
ATOM   2524  C CB  . LYS A 1 327 ? -28.57000 -50.93700 -20.59600 1.000 36.09000  ? 346  LYS A CB  1 
ATOM   2525  C CG  . LYS A 1 327 ? -29.88400 -50.87500 -21.36900 1.000 35.69000  ? 346  LYS A CG  1 
ATOM   2526  C CD  . LYS A 1 327 ? -30.87300 -51.92400 -20.90300 1.000 41.58000  ? 346  LYS A CD  1 
ATOM   2527  C CE  . LYS A 1 327 ? -32.19500 -51.74500 -21.62500 1.000 40.94000  ? 346  LYS A CE  1 
ATOM   2528  N NZ  . LYS A 1 327 ? -33.10100 -52.88700 -21.30100 1.000 49.56000  ? 346  LYS A NZ  1 
ATOM   2529  N N   . GLY A 1 328 ? -25.18500 -50.39400 -20.44600 1.000 31.61000  ? 347  GLY A N   1 
ATOM   2530  C CA  . GLY A 1 328 ? -24.07500 -50.18900 -19.54600 1.000 29.45000  ? 347  GLY A CA  1 
ATOM   2531  C C   . GLY A 1 328 ? -23.19400 -49.04500 -19.98300 1.000 34.51000  ? 347  GLY A C   1 
ATOM   2532  O O   . GLY A 1 328 ? -23.54900 -48.22200 -20.82800 1.000 42.05000  ? 347  GLY A O   1 
ATOM   2533  N N   . GLU A 1 329 ? -22.00400 -48.98400 -19.38200 1.000 37.54000  ? 348  GLU A N   1 
ATOM   2534  C CA  . GLU A 1 329 ? -21.03000 -47.97800 -19.77600 1.000 37.40000  ? 348  GLU A CA  1 
ATOM   2535  C C   . GLU A 1 329 ? -19.72500 -48.58300 -20.25500 1.000 35.89000  ? 348  GLU A C   1 
ATOM   2536  O O   . GLU A 1 329 ? -19.20200 -49.54800 -19.67000 1.000 31.63000  ? 348  GLU A O   1 
ATOM   2537  C CB  . GLU A 1 329 ? -20.69100 -46.99200 -18.65500 1.000 41.68000  ? 348  GLU A CB  1 
ATOM   2538  C CG  . GLU A 1 329 ? -21.72700 -45.89900 -18.31000 1.000 49.94000  ? 348  GLU A CG  1 
ATOM   2539  C CD  . GLU A 1 329 ? -22.28500 -45.11900 -19.53800 1.000 51.52000  ? 348  GLU A CD  1 
ATOM   2540  O OE1 . GLU A 1 329 ? -21.88300 -45.37500 -20.69500 1.000 57.37000  ? 348  GLU A OE1 1 
ATOM   2541  O OE2 . GLU A 1 329 ? -23.01100 -44.12800 -19.29300 1.000 55.51000  ? 348  GLU A OE2 1 
ATOM   2542  N N   . ILE A 1 330 ? -19.20100 -47.98100 -21.33000 1.000 30.08000  ? 349  ILE A N   1 
ATOM   2543  C CA  . ILE A 1 330 ? -17.89700 -48.33800 -21.86200 1.000 37.31000  ? 349  ILE A CA  1 
ATOM   2544  C C   . ILE A 1 330 ? -16.84800 -48.20200 -20.77200 1.000 34.13000  ? 349  ILE A C   1 
ATOM   2545  O O   . ILE A 1 330 ? -16.71400 -47.14700 -20.13100 1.000 30.33000  ? 349  ILE A O   1 
ATOM   2546  C CB  . ILE A 1 330 ? -17.57600 -47.43900 -23.06900 1.000 33.25000  ? 349  ILE A CB  1 
ATOM   2547  C CG1 . ILE A 1 330 ? -18.44200 -47.84800 -24.26700 1.000 39.22000  ? 349  ILE A CG1 1 
ATOM   2548  C CG2 . ILE A 1 330 ? -16.12300 -47.48100 -23.41500 1.000 33.84000  ? 349  ILE A CG2 1 
ATOM   2549  C CD1 . ILE A 1 330 ? -18.13800 -49.26400 -24.76900 1.000 37.28000  ? 349  ILE A CD1 1 
ATOM   2550  N N   . MET A 1 331 ? -16.09800 -49.28100 -20.54900 1.000 28.26000  ? 350  MET A N   1 
ATOM   2551  C CA  . MET A 1 331 ? -14.94100 -49.23700 -19.66500 1.000 33.01000  ? 350  MET A CA  1 
ATOM   2552  C C   . MET A 1 331 ? -14.00500 -48.12200 -20.11200 1.000 30.58000  ? 350  MET A C   1 
ATOM   2553  O O   . MET A 1 331 ? -13.55900 -48.13400 -21.26500 1.000 28.60000  ? 350  MET A O   1 
ATOM   2554  C CB  . MET A 1 331 ? -14.19700 -50.56600 -19.69800 1.000 33.75000  ? 350  MET A CB  1 
ATOM   2555  C CG  . MET A 1 331 ? -12.98400 -50.58400 -18.80900 1.000 25.20000  ? 350  MET A CG  1 
ATOM   2556  S SD  . MET A 1 331 ? -13.42400 -50.51900 -17.07300 1.000 42.06000  ? 350  MET A SD  1 
ATOM   2557  C CE  . MET A 1 331 ? -13.90500 -52.22800 -16.81100 1.000 27.98000  ? 350  MET A CE  1 
ATOM   2558  N N   . PRO A 1 332 ? -13.70800 -47.14300 -19.26000 1.000 29.12000  ? 351  PRO A N   1 
ATOM   2559  C CA  . PRO A 1 332 ? -12.77600 -46.08600 -19.65900 1.000 32.88000  ? 351  PRO A CA  1 
ATOM   2560  C C   . PRO A 1 332 ? -11.40600 -46.66900 -19.97500 1.000 36.09000  ? 351  PRO A C   1 
ATOM   2561  O O   . PRO A 1 332 ? -10.91900 -47.56500 -19.28500 1.000 30.35000  ? 351  PRO A O   1 
ATOM   2562  C CB  . PRO A 1 332 ? -12.72800 -45.16700 -18.43300 1.000 34.01000  ? 351  PRO A CB  1 
ATOM   2563  C CG  . PRO A 1 332 ? -14.00800 -45.45700 -17.70000 1.000 31.18000  ? 351  PRO A CG  1 
ATOM   2564  C CD  . PRO A 1 332 ? -14.25300 -46.92200 -17.91300 1.000 28.46000  ? 351  PRO A CD  1 
ATOM   2565  N N   . ASN A 1 333 ? -10.79200 -46.15800 -21.04300 1.000 37.80000  ? 352  ASN A N   1 
ATOM   2566  C CA  . ASN A 1 333 ? -9.49900  -46.63200 -21.51100 1.000 36.53000  ? 352  ASN A CA  1 
ATOM   2567  C C   . ASN A 1 333 ? -8.34500  -45.82500 -20.95400 1.000 38.09000  ? 352  ASN A C   1 
ATOM   2568  O O   . ASN A 1 333 ? -7.25000  -45.85200 -21.52500 1.000 42.77000  ? 352  ASN A O   1 
ATOM   2569  C CB  . ASN A 1 333 ? -9.44800  -46.61900 -23.04100 1.000 30.38000  ? 352  ASN A CB  1 
ATOM   2570  C CG  . ASN A 1 333 ? -9.74600  -45.24900 -23.62600 1.000 27.50000  ? 352  ASN A CG  1 
ATOM   2571  O OD1 . ASN A 1 333 ? -9.89900  -44.26700 -22.90500 1.000 32.39000  ? 352  ASN A OD1 1 
ATOM   2572  N ND2 . ASN A 1 333 ? -9.84000  -45.18300 -24.94400 1.000 30.22000  ? 352  ASN A ND2 1 
ATOM   2573  N N   . ILE A 1 334 ? -8.56200  -45.08500 -19.87500 1.000 34.59000  ? 353  ILE A N   1 
ATOM   2574  C CA  . ILE A 1 334 ? -7.46400  -44.34500 -19.26600 1.000 37.05000  ? 353  ILE A CA  1 
ATOM   2575  C C   . ILE A 1 334 ? -6.96000  -45.12200 -18.05700 1.000 38.27000  ? 353  ILE A C   1 
ATOM   2576  O O   . ILE A 1 334 ? -7.73700  -45.81900 -17.38300 1.000 36.24000  ? 353  ILE A O   1 
ATOM   2577  C CB  . ILE A 1 334 ? -7.88100  -42.91800 -18.88900 1.000 37.36000  ? 353  ILE A CB  1 
ATOM   2578  C CG1 . ILE A 1 334 ? -9.06400  -42.95600 -17.93100 1.000 32.70000  ? 353  ILE A CG1 1 
ATOM   2579  C CG2 . ILE A 1 334 ? -8.13800  -42.09500 -20.14800 1.000 35.94000  ? 353  ILE A CG2 1 
ATOM   2580  C CD1 . ILE A 1 334 ? -9.44300  -41.62700 -17.39000 1.000 41.04000  ? 353  ILE A CD1 1 
ATOM   2581  N N   . PRO A 1 335 ? -5.66300  -45.05400 -17.76600 1.000 37.60000  ? 354  PRO A N   1 
ATOM   2582  C CA  . PRO A 1 335 ? -5.11300  -45.86000 -16.67200 1.000 37.71000  ? 354  PRO A CA  1 
ATOM   2583  C C   . PRO A 1 335 ? -5.52100  -45.36800 -15.30100 1.000 38.06000  ? 354  PRO A C   1 
ATOM   2584  O O   . PRO A 1 335 ? -5.42100  -46.13300 -14.33400 1.000 38.68000  ? 354  PRO A O   1 
ATOM   2585  C CB  . PRO A 1 335 ? -3.60000  -45.74900 -16.89000 1.000 43.48000  ? 354  PRO A CB  1 
ATOM   2586  C CG  . PRO A 1 335 ? -3.44000  -44.45200 -17.59400 1.000 41.50000  ? 354  PRO A CG  1 
ATOM   2587  C CD  . PRO A 1 335 ? -4.63600  -44.25100 -18.44800 1.000 40.47000  ? 354  PRO A CD  1 
ATOM   2588  N N   . GLN A 1 336 ? -6.00500  -44.13100 -15.18800 1.000 38.51000  ? 355  GLN A N   1 
ATOM   2589  C CA  . GLN A 1 336 ? -6.50000  -43.63300 -13.91300 1.000 33.60000  ? 355  GLN A CA  1 
ATOM   2590  C C   . GLN A 1 336 ? -7.68500  -44.42900 -13.39400 1.000 33.91000  ? 355  GLN A C   1 
ATOM   2591  O O   . GLN A 1 336 ? -8.08200  -44.21500 -12.24600 1.000 33.54000  ? 355  GLN A O   1 
ATOM   2592  C CB  . GLN A 1 336 ? -6.88600  -42.16200 -14.02700 1.000 36.06000  ? 355  GLN A CB  1 
ATOM   2593  C CG  . GLN A 1 336 ? -5.70800  -41.21600 -14.23200 1.000 40.65000  ? 355  GLN A CG  1 
ATOM   2594  C CD  . GLN A 1 336 ? -5.20900  -41.22200 -15.66400 1.000 42.09000  ? 355  GLN A CD  1 
ATOM   2595  O OE1 . GLN A 1 336 ? -5.83000  -41.82000 -16.54300 1.000 48.90000  ? 355  GLN A OE1 1 
ATOM   2596  N NE2 . GLN A 1 336 ? -4.11400  -40.51800 -15.91700 1.000 44.63000  ? 355  GLN A NE2 1 
ATOM   2597  N N   . MET A 1 337 ? -8.24100  -45.35500 -14.18000 1.000 33.41000  ? 356  MET A N   1 
ATOM   2598  C CA  . MET A 1 337 ? -9.22300  -46.27800 -13.62000 1.000 35.07000  ? 356  MET A CA  1 
ATOM   2599  C C   . MET A 1 337 ? -8.66600  -47.03600 -12.42500 1.000 35.41000  ? 356  MET A C   1 
ATOM   2600  O O   . MET A 1 337 ? -9.43500  -47.49000 -11.56900 1.000 37.93000  ? 356  MET A O   1 
ATOM   2601  C CB  . MET A 1 337 ? -9.71300  -47.26200 -14.68200 1.000 35.14000  ? 356  MET A CB  1 
ATOM   2602  C CG  . MET A 1 337 ? -10.80600 -46.71300 -15.57400 1.000 36.26000  ? 356  MET A CG  1 
ATOM   2603  S SD  . MET A 1 337 ? -12.29300 -46.36100 -14.61400 1.000 40.17000  ? 356  MET A SD  1 
ATOM   2604  C CE  . MET A 1 337 ? -12.81100 -48.01700 -14.16200 1.000 28.11000  ? 356  MET A CE  1 
ATOM   2605  N N   . SER A 1 338 ? -7.34200  -47.17900 -12.34400 1.000 32.46000  ? 357  SER A N   1 
ATOM   2606  C CA  . SER A 1 338 ? -6.73400  -47.78900 -11.16900 1.000 34.22000  ? 357  SER A CA  1 
ATOM   2607  C C   . SER A 1 338 ? -7.17500  -47.07300 -9.89900  1.000 35.05000  ? 357  SER A C   1 
ATOM   2608  O O   . SER A 1 338 ? -7.55800  -47.71600 -8.91300  1.000 33.87000  ? 357  SER A O   1 
ATOM   2609  C CB  . SER A 1 338 ? -5.21000  -47.76100 -11.29500 1.000 36.94000  ? 357  SER A CB  1 
ATOM   2610  O OG  . SER A 1 338 ? -4.73100  -46.42900 -11.25100 1.000 36.54000  ? 357  SER A OG  1 
ATOM   2611  N N   . ALA A 1 339 ? -7.18100  -45.73800 -9.92700  1.000 31.17000  ? 358  ALA A N   1 
ATOM   2612  C CA  . ALA A 1 339 ? -7.69000  -44.98000 -8.79000  1.000 33.20000  ? 358  ALA A CA  1 
ATOM   2613  C C   . ALA A 1 339 ? -9.13500  -45.34600 -8.49000  1.000 31.46000  ? 358  ALA A C   1 
ATOM   2614  O O   . ALA A 1 339 ? -9.50600  -45.52500 -7.32500  1.000 38.56000  ? 358  ALA A O   1 
ATOM   2615  C CB  . ALA A 1 339 ? -7.57100  -43.48000 -9.05500  1.000 33.26000  ? 358  ALA A CB  1 
ATOM   2616  N N   . PHE A 1 340 ? -9.96500  -45.47000 -9.52600  1.000 30.88000  ? 359  PHE A N   1 
ATOM   2617  C CA  . PHE A 1 340 ? -11.37100 -45.80700 -9.31700  1.000 32.51000  ? 359  PHE A CA  1 
ATOM   2618  C C   . PHE A 1 340 ? -11.51900 -47.14100 -8.60400  1.000 30.74000  ? 359  PHE A C   1 
ATOM   2619  O O   . PHE A 1 340 ? -12.24000 -47.24500 -7.60800  1.000 35.60000  ? 359  PHE A O   1 
ATOM   2620  C CB  . PHE A 1 340 ? -12.11400 -45.84300 -10.65500 1.000 28.87000  ? 359  PHE A CB  1 
ATOM   2621  C CG  . PHE A 1 340 ? -13.53600 -46.32100 -10.54700 1.000 29.85000  ? 359  PHE A CG  1 
ATOM   2622  C CD1 . PHE A 1 340 ? -14.54200 -45.47200 -10.10600 1.000 28.71000  ? 359  PHE A CD1 1 
ATOM   2623  C CD2 . PHE A 1 340 ? -13.85700 -47.63700 -10.85500 1.000 32.14000  ? 359  PHE A CD2 1 
ATOM   2624  C CE1 . PHE A 1 340 ? -15.85600 -45.92400 -10.01000 1.000 28.93000  ? 359  PHE A CE1 1 
ATOM   2625  C CE2 . PHE A 1 340 ? -15.16600 -48.09800 -10.75100 1.000 29.21000  ? 359  PHE A CE2 1 
ATOM   2626  C CZ  . PHE A 1 340 ? -16.16500 -47.24200 -10.33100 1.000 28.82000  ? 359  PHE A CZ  1 
ATOM   2627  N N   . TRP A 1 341 ? -10.84400 -48.18000 -9.09800  1.000 34.71000  ? 360  TRP A N   1 
ATOM   2628  C CA  . TRP A 1 341 ? -11.04100 -49.50300 -8.51600  1.000 33.18000  ? 360  TRP A CA  1 
ATOM   2629  C C   . TRP A 1 341 ? -10.60100 -49.51800 -7.06000  1.000 36.56000  ? 360  TRP A C   1 
ATOM   2630  O O   . TRP A 1 341 ? -11.28300 -50.08700 -6.20200  1.000 36.58000  ? 360  TRP A O   1 
ATOM   2631  C CB  . TRP A 1 341 ? -10.27800 -50.56900 -9.30200  1.000 34.71000  ? 360  TRP A CB  1 
ATOM   2632  C CG  . TRP A 1 341 ? -10.69000 -50.71600 -10.73000 1.000 40.03000  ? 360  TRP A CG  1 
ATOM   2633  C CD1 . TRP A 1 341 ? -9.92900  -50.46500 -11.82500 1.000 38.59000  ? 360  TRP A CD1 1 
ATOM   2634  C CD2 . TRP A 1 341 ? -11.99000 -51.07500 -11.22000 1.000 39.30000  ? 360  TRP A CD2 1 
ATOM   2635  N NE1 . TRP A 1 341 ? -10.65000 -50.69700 -12.96800 1.000 43.11000  ? 360  TRP A NE1 1 
ATOM   2636  C CE2 . TRP A 1 341 ? -11.92300 -51.06300 -12.62400 1.000 43.52000  ? 360  TRP A CE2 1 
ATOM   2637  C CE3 . TRP A 1 341 ? -13.19700 -51.42700 -10.60600 1.000 35.64000  ? 360  TRP A CE3 1 
ATOM   2638  C CZ2 . TRP A 1 341 ? -13.01800 -51.38400 -13.42800 1.000 38.66000  ? 360  TRP A CZ2 1 
ATOM   2639  C CZ3 . TRP A 1 341 ? -14.27400 -51.74300 -11.40000 1.000 36.01000  ? 360  TRP A CZ3 1 
ATOM   2640  C CH2 . TRP A 1 341 ? -14.18000 -51.72000 -12.79800 1.000 30.00000  ? 360  TRP A CH2 1 
ATOM   2641  N N   . TYR A 1 342 ? -9.45100  -48.89500 -6.77300  1.000 34.20000  ? 361  TYR A N   1 
ATOM   2642  C CA  . TYR A 1 342 ? -8.87400  -48.90000 -5.42800  1.000 31.89000  ? 361  TYR A CA  1 
ATOM   2643  C C   . TYR A 1 342 ? -9.80000  -48.22800 -4.41600  1.000 35.49000  ? 361  TYR A C   1 
ATOM   2644  O O   . TYR A 1 342 ? -10.11300 -48.79800 -3.36200  1.000 30.54000  ? 361  TYR A O   1 
ATOM   2645  C CB  . TYR A 1 342 ? -7.51100  -48.20300 -5.47800  1.000 35.88000  ? 361  TYR A CB  1 
ATOM   2646  C CG  . TYR A 1 342 ? -6.73500  -48.18400 -4.18100  1.000 46.13000  ? 361  TYR A CG  1 
ATOM   2647  C CD1 . TYR A 1 342 ? -6.16000  -49.34900 -3.67700  1.000 44.63000  ? 361  TYR A CD1 1 
ATOM   2648  C CD2 . TYR A 1 342 ? -6.53700  -46.99400 -3.48200  1.000 40.89000  ? 361  TYR A CD2 1 
ATOM   2649  C CE1 . TYR A 1 342 ? -5.44200  -49.33600 -2.49800  1.000 40.80000  ? 361  TYR A CE1 1 
ATOM   2650  C CE2 . TYR A 1 342 ? -5.81200  -46.97200 -2.30700  1.000 38.41000  ? 361  TYR A CE2 1 
ATOM   2651  C CZ  . TYR A 1 342 ? -5.27200  -48.14800 -1.82000  1.000 45.37000  ? 361  TYR A CZ  1 
ATOM   2652  O OH  . TYR A 1 342 ? -4.55900  -48.14000 -0.64300  1.000 54.63000  ? 361  TYR A OH  1 
ATOM   2653  N N   . ALA A 1 343 ? -10.25500 -47.01500 -4.72500  1.000 33.04000  ? 362  ALA A N   1 
ATOM   2654  C CA  . ALA A 1 343 ? -11.11400 -46.28500 -3.80100  1.000 36.20000  ? 362  ALA A CA  1 
ATOM   2655  C C   . ALA A 1 343 ? -12.45800 -46.98700 -3.61800  1.000 41.14000  ? 362  ALA A C   1 
ATOM   2656  O O   . ALA A 1 343 ? -12.89800 -47.22800 -2.48600  1.000 42.54000  ? 362  ALA A O   1 
ATOM   2657  C CB  . ALA A 1 343 ? -11.31000 -44.85500 -4.31200  1.000 38.63000  ? 362  ALA A CB  1 
ATOM   2658  N N   . VAL A 1 344 ? -13.11900 -47.33800 -4.72400  1.000 34.70000  ? 363  VAL A N   1 
ATOM   2659  C CA  . VAL A 1 344 ? -14.46800 -47.89200 -4.63700  1.000 34.41000  ? 363  VAL A CA  1 
ATOM   2660  C C   . VAL A 1 344 ? -14.46300 -49.25500 -3.95700  1.000 35.55000  ? 363  VAL A C   1 
ATOM   2661  O O   . VAL A 1 344 ? -15.39600 -49.58800 -3.21000  1.000 31.31000  ? 363  VAL A O   1 
ATOM   2662  C CB  . VAL A 1 344 ? -15.10700 -47.95700 -6.04100  1.000 35.80000  ? 363  VAL A CB  1 
ATOM   2663  C CG1 . VAL A 1 344 ? -16.44200 -48.68200 -6.00100  1.000 27.18000  ? 363  VAL A CG1 1 
ATOM   2664  C CG2 . VAL A 1 344 ? -15.30000 -46.55900 -6.58900  1.000 31.14000  ? 363  VAL A CG2 1 
ATOM   2665  N N   . ARG A 1 345 ? -13.42900 -50.06400 -4.18700  1.000 32.73000  ? 364  ARG A N   1 
ATOM   2666  C CA  . ARG A 1 345 ? -13.39300 -51.37300 -3.54800  1.000 38.16000  ? 364  ARG A CA  1 
ATOM   2667  C C   . ARG A 1 345 ? -13.49200 -51.23000 -2.03400  1.000 37.85000  ? 364  ARG A C   1 
ATOM   2668  O O   . ARG A 1 345 ? -14.28300 -51.92400 -1.37900  1.000 32.94000  ? 364  ARG A O   1 
ATOM   2669  C CB  . ARG A 1 345 ? -12.12000 -52.11700 -3.94400  1.000 34.64000  ? 364  ARG A CB  1 
ATOM   2670  C CG  . ARG A 1 345 ? -12.14000 -53.58100 -3.57600  1.000 38.90000  ? 364  ARG A CG  1 
ATOM   2671  C CD  . ARG A 1 345 ? -10.83800 -54.29600 -3.93600  1.000 44.05000  ? 364  ARG A CD  1 
ATOM   2672  N NE  . ARG A 1 345 ? -10.97500 -55.73000 -3.70400  1.000 50.70000  ? 364  ARG A NE  1 
ATOM   2673  C CZ  . ARG A 1 345 ? -10.84100 -56.31700 -2.51900  1.000 50.49000  ? 364  ARG A CZ  1 
ATOM   2674  N NH1 . ARG A 1 345 ? -10.57100 -55.62000 -1.42300  1.000 39.83000  ? 364  ARG A NH1 1 
ATOM   2675  N NH2 . ARG A 1 345 ? -11.00600 -57.63500 -2.42600  1.000 48.65000  ? 364  ARG A NH2 1 
ATOM   2676  N N   . THR A 1 346 ? -12.72200 -50.29000 -1.47400  1.000 34.49000  ? 365  THR A N   1 
ATOM   2677  C CA  . THR A 1 346 ? -12.73200 -50.03500 -0.03600  1.000 32.56000  ? 365  THR A CA  1 
ATOM   2678  C C   . THR A 1 346 ? -14.09300 -49.54300 0.44000   1.000 33.09000  ? 365  THR A C   1 
ATOM   2679  O O   . THR A 1 346 ? -14.58300 -49.97500 1.48900   1.000 31.09000  ? 365  THR A O   1 
ATOM   2680  C CB  . THR A 1 346 ? -11.63600 -49.02300 0.31000   1.000 32.37000  ? 365  THR A CB  1 
ATOM   2681  O OG1 . THR A 1 346 ? -10.35900 -49.59300 0.00300   1.000 39.60000  ? 365  THR A OG1 1 
ATOM   2682  C CG2 . THR A 1 346 ? -11.67100 -48.66100 1.76800   1.000 25.77000  ? 365  THR A CG2 1 
ATOM   2683  N N   . ALA A 1 347 ? -14.72400 -48.64500 -0.32200  1.000 42.62000  ? 366  ALA A N   1 
ATOM   2684  C CA  . ALA A 1 347 ? -16.00900 -48.08400 0.09500   1.000 31.79000  ? 366  ALA A CA  1 
ATOM   2685  C C   . ALA A 1 347 ? -17.07300 -49.16500 0.23500   1.000 28.33000  ? 366  ALA A C   1 
ATOM   2686  O O   . ALA A 1 347 ? -17.82200 -49.18300 1.21600   1.000 34.28000  ? 366  ALA A O   1 
ATOM   2687  C CB  . ALA A 1 347 ? -16.46300 -47.01000 -0.89400  1.000 31.68000  ? 366  ALA A CB  1 
ATOM   2688  N N   . VAL A 1 348 ? -17.15700 -50.08000 -0.72800  1.000 29.14000  ? 367  VAL A N   1 
ATOM   2689  C CA  . VAL A 1 348 ? -18.16300 -51.13200 -0.63900  1.000 30.61000  ? 367  VAL A CA  1 
ATOM   2690  C C   . VAL A 1 348 ? -17.91000 -52.00500 0.58200   1.000 30.78000  ? 367  VAL A C   1 
ATOM   2691  O O   . VAL A 1 348 ? -18.83900 -52.34600 1.32300   1.000 34.70000  ? 367  VAL A O   1 
ATOM   2692  C CB  . VAL A 1 348 ? -18.20100 -51.95900 -1.93700  1.000 33.01000  ? 367  VAL A CB  1 
ATOM   2693  C CG1 . VAL A 1 348 ? -19.11800 -53.16200 -1.77000  1.000 37.46000  ? 367  VAL A CG1 1 
ATOM   2694  C CG2 . VAL A 1 348 ? -18.69900 -51.10100 -3.09000  1.000 30.15000  ? 367  VAL A CG2 1 
ATOM   2695  N N   . ILE A 1 349 ? -16.65000 -52.35100 0.83100   1.000 33.59000  ? 368  ILE A N   1 
ATOM   2696  C CA  . ILE A 1 349 ? -16.32300 -53.21700 1.96300   1.000 34.22000  ? 368  ILE A CA  1 
ATOM   2697  C C   . ILE A 1 349 ? -16.70500 -52.55500 3.28000   1.000 33.73000  ? 368  ILE A C   1 
ATOM   2698  O O   . ILE A 1 349 ? -17.30700 -53.18800 4.15800   1.000 31.12000  ? 368  ILE A O   1 
ATOM   2699  C CB  . ILE A 1 349 ? -14.83100 -53.59100 1.93800   1.000 37.12000  ? 368  ILE A CB  1 
ATOM   2700  C CG1 . ILE A 1 349 ? -14.55800 -54.60500 0.81600   1.000 34.08000  ? 368  ILE A CG1 1 
ATOM   2701  C CG2 . ILE A 1 349 ? -14.36800 -54.07100 3.31100   1.000 29.27000  ? 368  ILE A CG2 1 
ATOM   2702  C CD1 . ILE A 1 349 ? -13.10900 -54.81900 0.56100   1.000 39.06000  ? 368  ILE A CD1 1 
ATOM   2703  N N   . ASN A 1 350 ? -16.35700 -51.27100 3.43800   1.000 28.89000  ? 369  ASN A N   1 
ATOM   2704  C CA  . ASN A 1 350 ? -16.61200 -50.59900 4.70900   1.000 32.69000  ? 369  ASN A CA  1 
ATOM   2705  C C   . ASN A 1 350 ? -18.09500 -50.33500 4.92300   1.000 32.57000  ? 369  ASN A C   1 
ATOM   2706  O O   . ASN A 1 350 ? -18.57900 -50.39500 6.06000   1.000 32.50000  ? 369  ASN A O   1 
ATOM   2707  C CB  . ASN A 1 350 ? -15.84600 -49.28700 4.80800   1.000 29.78000  ? 369  ASN A CB  1 
ATOM   2708  C CG  . ASN A 1 350 ? -14.36500 -49.49200 4.89000   1.000 30.61000  ? 369  ASN A CG  1 
ATOM   2709  O OD1 . ASN A 1 350 ? -13.89500 -50.57900 5.22900   1.000 33.11000  ? 369  ASN A OD1 1 
ATOM   2710  N ND2 . ASN A 1 350 ? -13.61700 -48.41200 4.70400   1.000 30.20000  ? 369  ASN A ND2 1 
ATOM   2711  N N   . ALA A 1 351 ? -18.82000 -49.99300 3.85800   1.000 33.23000  ? 370  ALA A N   1 
ATOM   2712  C CA  . ALA A 1 351 ? -20.26300 -49.80000 3.97600   1.000 34.14000  ? 370  ALA A CA  1 
ATOM   2713  C C   . ALA A 1 351 ? -20.97100 -51.12200 4.22900   1.000 37.97000  ? 370  ALA A C   1 
ATOM   2714  O O   . ALA A 1 351 ? -21.87900 -51.19600 5.06900   1.000 35.66000  ? 370  ALA A O   1 
ATOM   2715  C CB  . ALA A 1 351 ? -20.81200 -49.13100 2.71400   1.000 32.00000  ? 370  ALA A CB  1 
ATOM   2716  N N   . ALA A 1 352 ? -20.55000 -52.18200 3.53000   1.000 37.99000  ? 371  ALA A N   1 
ATOM   2717  C CA  . ALA A 1 352 ? -21.20200 -53.47800 3.68400   1.000 36.23000  ? 371  ALA A CA  1 
ATOM   2718  C C   . ALA A 1 352 ? -21.11800 -53.97400 5.12100   1.000 41.39000  ? 371  ALA A C   1 
ATOM   2719  O O   . ALA A 1 352 ? -22.07900 -54.55900 5.63300   1.000 39.48000  ? 371  ALA A O   1 
ATOM   2720  C CB  . ALA A 1 352 ? -20.58400 -54.50100 2.73800   1.000 32.65000  ? 371  ALA A CB  1 
ATOM   2721  N N   . SER A 1 353 ? -19.98300 -53.74300 5.79200   1.000 31.89000  ? 372  SER A N   1 
ATOM   2722  C CA  . SER A 1 353 ? -19.78200 -54.22800 7.15200   1.000 35.67000  ? 372  SER A CA  1 
ATOM   2723  C C   . SER A 1 353 ? -20.35400 -53.28800 8.20200   1.000 38.68000  ? 372  SER A C   1 
ATOM   2724  O O   . SER A 1 353 ? -20.36800 -53.63800 9.38500   1.000 41.06000  ? 372  SER A O   1 
ATOM   2725  C CB  . SER A 1 353 ? -18.30100 -54.44700 7.44400   1.000 30.71000  ? 372  SER A CB  1 
ATOM   2726  O OG  . SER A 1 353 ? -17.65400 -53.20400 7.65400   1.000 36.07000  ? 372  SER A OG  1 
ATOM   2727  N N   . GLY A 1 354 ? -20.83100 -52.11400 7.80700   1.000 35.64000  ? 373  GLY A N   1 
ATOM   2728  C CA  . GLY A 1 354 ? -21.31600 -51.16500 8.78200   1.000 36.93000  ? 373  GLY A CA  1 
ATOM   2729  C C   . GLY A 1 354 ? -20.23200 -50.36300 9.44600   1.000 36.38000  ? 373  GLY A C   1 
ATOM   2730  O O   . GLY A 1 354 ? -20.52500 -49.60600 10.38300  1.000 36.30000  ? 373  GLY A O   1 
ATOM   2731  N N   . ARG A 1 355 ? -18.98500 -50.51300 8.99100   1.000 31.88000  ? 374  ARG A N   1 
ATOM   2732  C CA  . ARG A 1 355 ? -17.89100 -49.70900 9.52600   1.000 34.27000  ? 374  ARG A CA  1 
ATOM   2733  C C   . ARG A 1 355 ? -18.12900 -48.22700 9.26800   1.000 35.47000  ? 374  ARG A C   1 
ATOM   2734  O O   . ARG A 1 355 ? -17.75700 -47.37400 10.08500  1.000 32.50000  ? 374  ARG A O   1 
ATOM   2735  C CB  . ARG A 1 355 ? -16.57800 -50.16100 8.89300   1.000 33.66000  ? 374  ARG A CB  1 
ATOM   2736  C CG  . ARG A 1 355 ? -15.36500 -49.48600 9.42400   1.000 30.72000  ? 374  ARG A CG  1 
ATOM   2737  C CD  . ARG A 1 355 ? -14.13300 -50.01600 8.72200   1.000 33.37000  ? 374  ARG A CD  1 
ATOM   2738  N NE  . ARG A 1 355 ? -12.92400 -49.46100 9.31200   1.000 35.09000  ? 374  ARG A NE  1 
ATOM   2739  C CZ  . ARG A 1 355 ? -11.69900 -49.66500 8.85300   1.000 38.08000  ? 374  ARG A CZ  1 
ATOM   2740  N NH1 . ARG A 1 355 ? -11.48500 -50.30900 7.71600   1.000 44.92000  ? 374  ARG A NH1 1 
ATOM   2741  N NH2 . ARG A 1 355 ? -10.66600 -49.19300 9.54100   1.000 33.74000  ? 374  ARG A NH2 1 
ATOM   2742  N N   . GLN A 1 356 ? -18.74800 -47.91500 8.13300   1.000 34.16000  ? 375  GLN A N   1 
ATOM   2743  C CA  . GLN A 1 356 ? -19.05700 -46.56500 7.70100   1.000 35.15000  ? 375  GLN A CA  1 
ATOM   2744  C C   . GLN A 1 356 ? -20.48000 -46.53700 7.17300   1.000 32.62000  ? 375  GLN A C   1 
ATOM   2745  O O   . GLN A 1 356 ? -21.02200 -47.56200 6.75600   1.000 34.96000  ? 375  GLN A O   1 
ATOM   2746  C CB  . GLN A 1 356 ? -18.08300 -46.08400 6.61300   1.000 37.28000  ? 375  GLN A CB  1 
ATOM   2747  C CG  . GLN A 1 356 ? -16.84300 -45.39000 7.10900   1.000 34.54000  ? 375  GLN A CG  1 
ATOM   2748  C CD  . GLN A 1 356 ? -15.86900 -45.06900 5.98500   1.000 35.77000  ? 375  GLN A CD  1 
ATOM   2749  O OE1 . GLN A 1 356 ? -15.77900 -45.79100 4.98600   1.000 36.68000  ? 375  GLN A OE1 1 
ATOM   2750  N NE2 . GLN A 1 356 ? -15.23300 -43.90500 6.08300   1.000 41.34000  ? 375  GLN A NE2 1 
ATOM   2751  N N   . THR A 1 357 ? -21.08700 -45.35500 7.20200   1.000 31.28000  ? 376  THR A N   1 
ATOM   2752  C CA  . THR A 1 357 ? -22.32400 -45.17400 6.46600   1.000 35.70000  ? 376  THR A CA  1 
ATOM   2753  C C   . THR A 1 357 ? -22.02700 -45.16500 4.96800   1.000 35.72000  ? 376  THR A C   1 
ATOM   2754  O O   . THR A 1 357 ? -20.91000 -44.86800 4.53500   1.000 35.48000  ? 376  THR A O   1 
ATOM   2755  C CB  . THR A 1 357 ? -23.01700 -43.86300 6.85400   1.000 34.87000  ? 376  THR A CB  1 
ATOM   2756  O OG1 . THR A 1 357 ? -22.22100 -42.74700 6.43400   1.000 41.51000  ? 376  THR A OG1 1 
ATOM   2757  C CG2 . THR A 1 357 ? -23.24300 -43.77800 8.35800   1.000 34.17000  ? 376  THR A CG2 1 
ATOM   2758  N N   . VAL A 1 358 ? -23.05000 -45.48000 4.16900   1.000 36.56000  ? 377  VAL A N   1 
ATOM   2759  C CA  . VAL A 1 358 ? -22.90500 -45.37300 2.72000   1.000 35.33000  ? 377  VAL A CA  1 
ATOM   2760  C C   . VAL A 1 358 ? -22.44100 -43.97300 2.35200   1.000 40.53000  ? 377  VAL A C   1 
ATOM   2761  O O   . VAL A 1 358 ? -21.52300 -43.78700 1.53900   1.000 37.05000  ? 377  VAL A O   1 
ATOM   2762  C CB  . VAL A 1 358 ? -24.23300 -45.72600 2.02800   1.000 34.05000  ? 377  VAL A CB  1 
ATOM   2763  C CG1 . VAL A 1 358 ? -24.11800 -45.50000 0.52600   1.000 36.20000  ? 377  VAL A CG1 1 
ATOM   2764  C CG2 . VAL A 1 358 ? -24.63000 -47.16000 2.35100   1.000 27.33000  ? 377  VAL A CG2 1 
ATOM   2765  N N   . ASP A 1 359 ? -23.02900 -42.97400 3.00200   1.000 36.84000  ? 378  ASP A N   1 
ATOM   2766  C CA  . ASP A 1 359 ? -22.72500 -41.58500 2.70100   1.000 37.65000  ? 378  ASP A CA  1 
ATOM   2767  C C   . ASP A 1 359 ? -21.24700 -41.26700 2.93700   1.000 39.71000  ? 378  ASP A C   1 
ATOM   2768  O O   . ASP A 1 359 ? -20.57400 -40.73400 2.04400   1.000 40.58000  ? 378  ASP A O   1 
ATOM   2769  C CB  . ASP A 1 359 ? -23.67300 -40.70800 3.52600   1.000 48.26000  ? 378  ASP A CB  1 
ATOM   2770  C CG  . ASP A 1 359 ? -23.66300 -39.25100 3.11400   1.000 62.34000  ? 378  ASP A CG  1 
ATOM   2771  O OD1 . ASP A 1 359 ? -22.64400 -38.77800 2.56500   1.000 64.87000  ? 378  ASP A OD1 1 
ATOM   2772  O OD2 . ASP A 1 359 ? -24.73000 -38.60300 3.24600   1.000 69.37000  ? 378  ASP A OD2 1 
ATOM   2773  N N   . GLU A 1 360 ? -20.70500 -41.61600 4.11300   1.000 36.79000  ? 379  GLU A N   1 
ATOM   2774  C CA  . GLU A 1 360 ? -19.30500 -41.27200 4.37300   1.000 37.82000  ? 379  GLU A CA  1 
ATOM   2775  C C   . GLU A 1 360 ? -18.34900 -42.14200 3.55700   1.000 36.48000  ? 379  GLU A C   1 
ATOM   2776  O O   . GLU A 1 360 ? -17.27800 -41.67200 3.15400   1.000 37.54000  ? 379  GLU A O   1 
ATOM   2777  C CB  . GLU A 1 360 ? -18.98300 -41.33300 5.88200   1.000 44.14000  ? 379  GLU A CB  1 
ATOM   2778  C CG  . GLU A 1 360 ? -19.30200 -42.65800 6.60200   1.000 51.89000  ? 379  GLU A CG  1 
ATOM   2779  C CD  . GLU A 1 360 ? -19.03800 -42.62900 8.13800   1.000 64.79000  ? 379  GLU A CD  1 
ATOM   2780  O OE1 . GLU A 1 360 ? -18.37200 -41.67000 8.62500   1.000 64.56000  ? 379  GLU A OE1 1 
ATOM   2781  O OE2 . GLU A 1 360 ? -19.59300 -43.51100 8.86600   1.000 46.80000  ? 379  GLU A OE2 1 
ATOM   2782  N N   . ALA A 1 361 ? -18.71200 -43.40200 3.28900   1.000 36.27000  ? 380  ALA A N   1 
ATOM   2783  C CA  . ALA A 1 361 ? -17.82800 -44.26900 2.50900   1.000 34.02000  ? 380  ALA A CA  1 
ATOM   2784  C C   . ALA A 1 361 ? -17.60800 -43.72100 1.09700   1.000 35.59000  ? 380  ALA A C   1 
ATOM   2785  O O   . ALA A 1 361 ? -16.47300 -43.67500 0.60700   1.000 37.59000  ? 380  ALA A O   1 
ATOM   2786  C CB  . ALA A 1 361 ? -18.39500 -45.69000 2.46400   1.000 28.58000  ? 380  ALA A CB  1 
ATOM   2787  N N   . LEU A 1 362 ? -18.68000 -43.28600 0.43300   1.000 36.72000  ? 381  LEU A N   1 
ATOM   2788  C CA  . LEU A 1 362 ? -18.55700 -42.75700 -0.91900  1.000 30.92000  ? 381  LEU A CA  1 
ATOM   2789  C C   . LEU A 1 362 ? -17.94800 -41.36700 -0.92000  1.000 31.76000  ? 381  LEU A C   1 
ATOM   2790  O O   . LEU A 1 362 ? -17.24100 -41.00900 -1.87100  1.000 36.36000  ? 381  LEU A O   1 
ATOM   2791  C CB  . LEU A 1 362 ? -19.92000 -42.74800 -1.60100  1.000 32.40000  ? 381  LEU A CB  1 
ATOM   2792  C CG  . LEU A 1 362 ? -20.42600 -44.17200 -1.81000  1.000 29.36000  ? 381  LEU A CG  1 
ATOM   2793  C CD1 . LEU A 1 362 ? -21.82100 -44.16500 -2.38100  1.000 35.28000  ? 381  LEU A CD1 1 
ATOM   2794  C CD2 . LEU A 1 362 ? -19.48100 -44.90800 -2.72500  1.000 28.60000  ? 381  LEU A CD2 1 
ATOM   2795  N N   . LYS A 1 363 ? -18.19100 -40.59200 0.14200   1.000 28.60000  ? 382  LYS A N   1 
ATOM   2796  C CA  . LYS A 1 363 ? -17.45900 -39.34600 0.34400   1.000 34.47000  ? 382  LYS A CA  1 
ATOM   2797  C C   . LYS A 1 363 ? -15.95500 -39.58500 0.36400   1.000 44.08000  ? 382  LYS A C   1 
ATOM   2798  O O   . LYS A 1 363 ? -15.19600 -38.92300 -0.36000  1.000 40.29000  ? 382  LYS A O   1 
ATOM   2799  C CB  . LYS A 1 363 ? -17.88400 -38.66800 1.64800   1.000 41.84000  ? 382  LYS A CB  1 
ATOM   2800  C CG  . LYS A 1 363 ? -16.90900 -37.55300 2.04000   1.000 46.74000  ? 382  LYS A CG  1 
ATOM   2801  C CD  . LYS A 1 363 ? -17.22600 -36.72100 3.32000   1.000 57.70000  ? 382  LYS A CD  1 
ATOM   2802  C CE  . LYS A 1 363 ? -16.73300 -37.31600 4.68400   1.000 61.93000  ? 382  LYS A CE  1 
ATOM   2803  N NZ  . LYS A 1 363 ? -17.82000 -37.95900 5.53700   1.000 76.08000  ? 382  LYS A NZ  1 
ATOM   2804  N N   . ASP A 1 364 ? -15.50300 -40.53400 1.18600   1.000 35.23000  ? 383  ASP A N   1 
ATOM   2805  C CA  . ASP A 1 364 ? -14.07700 -40.81500 1.24300   1.000 36.51000  ? 383  ASP A CA  1 
ATOM   2806  C C   . ASP A 1 364 ? -13.56900 -41.33200 -0.10000  1.000 38.67000  ? 383  ASP A C   1 
ATOM   2807  O O   . ASP A 1 364 ? -12.51100 -40.90200 -0.57900  1.000 38.28000  ? 383  ASP A O   1 
ATOM   2808  C CB  . ASP A 1 364 ? -13.77000 -41.81600 2.36700   1.000 40.07000  ? 383  ASP A CB  1 
ATOM   2809  C CG  . ASP A 1 364 ? -13.96900 -41.22400 3.77300   1.000 48.44000  ? 383  ASP A CG  1 
ATOM   2810  O OD1 . ASP A 1 364 ? -14.00600 -39.97700 3.91100   1.000 46.59000  ? 383  ASP A OD1 1 
ATOM   2811  O OD2 . ASP A 1 364 ? -14.01800 -42.01100 4.75500   1.000 44.25000  ? 383  ASP A OD2 1 
ATOM   2812  N N   . ALA A 1 365 ? -14.32300 -42.23200 -0.73600  1.000 36.95000  ? 384  ALA A N   1 
ATOM   2813  C CA  . ALA A 1 365 ? -13.86600 -42.82700 -1.98900  1.000 32.53000  ? 384  ALA A CA  1 
ATOM   2814  C C   . ALA A 1 365 ? -13.83800 -41.80400 -3.12400  1.000 33.53000  ? 384  ALA A C   1 
ATOM   2815  O O   . ALA A 1 365 ? -12.94000 -41.84400 -3.97200  1.000 34.90000  ? 384  ALA A O   1 
ATOM   2816  C CB  . ALA A 1 365 ? -14.74400 -44.02000 -2.35800  1.000 29.86000  ? 384  ALA A CB  1 
ATOM   2817  N N   . GLN A 1 366 ? -14.81900 -40.89700 -3.17300  1.000 36.92000  ? 385  GLN A N   1 
ATOM   2818  C CA  . GLN A 1 366 ? -14.78300 -39.81000 -4.15200  1.000 32.83000  ? 385  GLN A CA  1 
ATOM   2819  C C   . GLN A 1 366 ? -13.49000 -39.02000 -4.02300  1.000 41.05000  ? 385  GLN A C   1 
ATOM   2820  O O   . GLN A 1 366 ? -12.79700 -38.76600 -5.01500  1.000 38.47000  ? 385  GLN A O   1 
ATOM   2821  C CB  . GLN A 1 366 ? -15.98600 -38.89100 -3.94800  1.000 33.60000  ? 385  GLN A CB  1 
ATOM   2822  C CG  . GLN A 1 366 ? -16.09300 -37.66200 -4.85900  1.000 34.25000  ? 385  GLN A CG  1 
ATOM   2823  C CD  . GLN A 1 366 ? -16.52700 -37.97900 -6.28000  1.000 33.66000  ? 385  GLN A CD  1 
ATOM   2824  O OE1 . GLN A 1 366 ? -17.23400 -38.95300 -6.52200  1.000 42.09000  ? 385  GLN A OE1 1 
ATOM   2825  N NE2 . GLN A 1 366 ? -16.17700 -37.10300 -7.21400  1.000 36.76000  ? 385  GLN A NE2 1 
ATOM   2826  N N   . THR A 1 367 ? -13.13800 -38.65100 -2.78900  1.000 43.47000  ? 386  THR A N   1 
ATOM   2827  C CA  . THR A 1 367 ? -11.93200 -37.87000 -2.54600  1.000 36.68000  ? 386  THR A CA  1 
ATOM   2828  C C   . THR A 1 367 ? -10.68200 -38.66300 -2.88500  1.000 40.97000  ? 386  THR A C   1 
ATOM   2829  O O   . THR A 1 367 ? -9.74700  -38.13100 -3.49500  1.000 43.36000  ? 386  THR A O   1 
ATOM   2830  C CB  . THR A 1 367 ? -11.90000 -37.41800 -1.08700  1.000 37.89000  ? 386  THR A CB  1 
ATOM   2831  O OG1 . THR A 1 367 ? -13.01600 -36.55800 -0.83900  1.000 51.96000  ? 386  THR A OG1 1 
ATOM   2832  C CG2 . THR A 1 367 ? -10.61700 -36.67000 -0.77500  1.000 50.44000  ? 386  THR A CG2 1 
ATOM   2833  N N   . ALA A 1 368 ? -10.64400 -39.93500 -2.48400  1.000 40.44000  ? 387  ALA A N   1 
ATOM   2834  C CA  . ALA A 1 368 ? -9.48100  -40.76900 -2.75700  1.000 33.87000  ? 387  ALA A CA  1 
ATOM   2835  C C   . ALA A 1 368 ? -9.28200  -40.97600 -4.25500  1.000 38.86000  ? 387  ALA A C   1 
ATOM   2836  O O   . ALA A 1 368 ? -8.15000  -40.92000 -4.75000  1.000 40.05000  ? 387  ALA A O   1 
ATOM   2837  C CB  . ALA A 1 368 ? -9.62900  -42.10700 -2.04200  1.000 34.50000  ? 387  ALA A CB  1 
ATOM   2838  N N   . ALA A 1 369 ? -10.36900 -41.21800 -4.99400  1.000 35.74000  ? 388  ALA A N   1 
ATOM   2839  C CA  . ALA A 1 369 ? -10.25900 -41.41100 -6.44000  1.000 35.31000  ? 388  ALA A CA  1 
ATOM   2840  C C   . ALA A 1 369 ? -9.73100  -40.15500 -7.11800  1.000 35.00000  ? 388  ALA A C   1 
ATOM   2841  O O   . ALA A 1 369 ? -8.80000  -40.21800 -7.93000  1.000 37.79000  ? 388  ALA A O   1 
ATOM   2842  C CB  . ALA A 1 369 ? -11.61900 -41.81000 -7.02400  1.000 30.08000  ? 388  ALA A CB  1 
ATOM   2843  N N   . ARG A 1 370 ? -10.30200 -38.99700 -6.77400  1.000 33.72000  ? 389  ARG A N   1 
ATOM   2844  C CA  . ARG A 1 370 ? -9.81600  -37.72300 -7.29500  1.000 35.31000  ? 389  ARG A CA  1 
ATOM   2845  C C   . ARG A 1 370 ? -8.31600  -37.57700 -7.08300  1.000 40.21000  ? 389  ARG A C   1 
ATOM   2846  O O   . ARG A 1 370 ? -7.57400  -37.24500 -8.01400  1.000 39.72000  ? 389  ARG A O   1 
ATOM   2847  C CB  . ARG A 1 370 ? -10.54900 -36.56800 -6.61100  1.000 43.69000  ? 389  ARG A CB  1 
ATOM   2848  C CG  . ARG A 1 370 ? -12.04200 -36.46900 -6.88100  1.000 43.34000  ? 389  ARG A CG  1 
ATOM   2849  C CD  . ARG A 1 370 ? -12.29200 -35.94100 -8.25400  1.000 46.83000  ? 389  ARG A CD  1 
ATOM   2850  N NE  . ARG A 1 370 ? -11.64600 -34.64800 -8.43600  1.000 53.14000  ? 389  ARG A NE  1 
ATOM   2851  C CZ  . ARG A 1 370 ? -12.16000 -33.49300 -8.03600  1.000 56.80000  ? 389  ARG A CZ  1 
ATOM   2852  N NH1 . ARG A 1 370 ? -13.31200 -33.44000 -7.38200  1.000 53.42000  ? 389  ARG A NH1 1 
ATOM   2853  N NH2 . ARG A 1 370 ? -11.50000 -32.36400 -8.29500  1.000 51.58000  ? 389  ARG A NH2 1 
ATOM   2854  N N   . ALA A 1 371 ? -7.85100  -37.83000 -5.85500  1.000 40.98000  ? 390  ALA A N   1 
ATOM   2855  C CA  . ALA A 1 371 ? -6.46000  -37.55600 -5.51700  1.000 34.06000  ? 390  ALA A CA  1 
ATOM   2856  C C   . ALA A 1 371 ? -5.51300  -38.50600 -6.23500  1.000 37.93000  ? 390  ALA A C   1 
ATOM   2857  O O   . ALA A 1 371 ? -4.53400  -38.06700 -6.85100  1.000 40.69000  ? 390  ALA A O   1 
ATOM   2858  C CB  . ALA A 1 371 ? -6.26600  -37.63400 -4.00400  1.000 42.12000  ? 390  ALA A CB  1 
ATOM   2859  N N   . PHE A 1 372 ? -5.77900  -39.81400 -6.17000  1.000 34.12000  ? 391  PHE A N   1 
ATOM   2860  C CA  . PHE A 1 372 ? -4.91500  -40.75900 -6.87800  1.000 43.27000  ? 391  PHE A CA  1 
ATOM   2861  C C   . PHE A 1 372 ? -4.95900  -40.52700 -8.38700  1.000 41.92000  ? 391  PHE A C   1 
ATOM   2862  O O   . PHE A 1 372 ? -3.94000  -40.66600 -9.07500  1.000 42.06000  ? 391  PHE A O   1 
ATOM   2863  C CB  . PHE A 1 372 ? -5.31100  -42.20400 -6.56200  1.000 43.09000  ? 391  PHE A CB  1 
ATOM   2864  C CG  . PHE A 1 372 ? -4.92000  -42.67600 -5.18600  1.000 46.92000  ? 391  PHE A CG  1 
ATOM   2865  C CD1 . PHE A 1 372 ? -3.62600  -43.09000 -4.92600  1.000 43.50000  ? 391  PHE A CD1 1 
ATOM   2866  C CD2 . PHE A 1 372 ? -5.86000  -42.76000 -4.17000  1.000 45.47000  ? 391  PHE A CD2 1 
ATOM   2867  C CE1 . PHE A 1 372 ? -3.27100  -43.54700 -3.67900  1.000 48.48000  ? 391  PHE A CE1 1 
ATOM   2868  C CE2 . PHE A 1 372 ? -5.51100  -43.21300 -2.92100  1.000 46.40000  ? 391  PHE A CE2 1 
ATOM   2869  C CZ  . PHE A 1 372 ? -4.21400  -43.60700 -2.67200  1.000 47.42000  ? 391  PHE A CZ  1 
ATOM   2870  N N   . ALA A 1 373 ? -6.13300  -40.18100 -8.92300  1.000 36.67000  ? 392  ALA A N   1 
ATOM   2871  C CA  . ALA A 1 373 ? -6.22700  -39.89200 -10.35100 1.000 39.95000  ? 392  ALA A CA  1 
ATOM   2872  C C   . ALA A 1 373 ? -5.37600  -38.68300 -10.72100 1.000 44.09000  ? 392  ALA A C   1 
ATOM   2873  O O   . ALA A 1 373 ? -4.66500  -38.69500 -11.73200 1.000 43.04000  ? 392  ALA A O   1 
ATOM   2874  C CB  . ALA A 1 373 ? -7.68100  -39.66200 -10.74600 1.000 34.99000  ? 392  ALA A CB  1 
ATOM   2875  N N   . ALA A 1 374 ? -5.44300  -37.62100 -9.91600  1.000 43.26000  ? 393  ALA A N   1 
ATOM   2876  C CA  . ALA A 1 374 ? -4.58300  -36.47000 -10.15700 1.000 46.91000  ? 393  ALA A CA  1 
ATOM   2877  C C   . ALA A 1 374 ? -3.11800  -36.81600 -9.96400  1.000 44.11000  ? 393  ALA A C   1 
ATOM   2878  O O   . ALA A 1 374 ? -2.25500  -36.28100 -10.66700 1.000 50.48000  ? 393  ALA A O   1 
ATOM   2879  C CB  . ALA A 1 374 ? -4.97400  -35.31300 -9.23500  1.000 48.01000  ? 393  ALA A CB  1 
ATOM   2880  N N   . ALA A 1 375 ? -2.81600  -37.70300 -9.02500  1.000 46.83000  ? 394  ALA A N   1 
ATOM   2881  C CA  . ALA A 1 375 ? -1.42700  -37.95900 -8.67500  1.000 50.42000  ? 394  ALA A CA  1 
ATOM   2882  C C   . ALA A 1 375 ? -0.68300  -38.77400 -9.71900  1.000 50.14000  ? 394  ALA A C   1 
ATOM   2883  O O   . ALA A 1 375 ? 0.55000   -38.72900 -9.75100  1.000 52.99000  ? 394  ALA A O   1 
ATOM   2884  C CB  . ALA A 1 375 ? -1.34800  -38.68100 -7.32400  1.000 47.40000  ? 394  ALA A CB  1 
ATOM   2885  N N   . GLY A 1 376 ? -1.37900  -39.51600 -10.55600 1.000 47.97000  ? 395  GLY A N   1 
ATOM   2886  C CA  . GLY A 1 376 ? -0.69500  -40.34800 -11.52500 1.000 48.31000  ? 395  GLY A CA  1 
ATOM   2887  C C   . GLY A 1 376 ? -1.51100  -41.57000 -11.88000 1.000 53.02000  ? 395  GLY A C   1 
ATOM   2888  O O   . GLY A 1 376 ? -2.56300  -41.84300 -11.30700 1.000 54.21000  ? 395  GLY A O   1 
ATOM   2889  N N   . LYS A 1 377 ? -0.98400  -42.32100 -12.84300 1.000 57.03000  ? 396  LYS A N   1 
ATOM   2890  C CA  . LYS A 1 377 ? -1.75500  -43.37700 -13.48200 1.000 55.67000  ? 396  LYS A CA  1 
ATOM   2891  C C   . LYS A 1 377 ? -1.88500  -44.62400 -12.61000 1.000 53.16000  ? 396  LYS A C   1 
ATOM   2892  O O   . LYS A 1 377 ? -2.76700  -45.45600 -12.87300 1.000 54.80000  ? 396  LYS A O   1 
ATOM   2893  C CB  . LYS A 1 377 ? -1.11100  -43.72500 -14.83100 1.000 62.46000  ? 396  LYS A CB  1 
ATOM   2894  C CG  . LYS A 1 377 ? -1.11800  -42.57400 -15.83800 1.000 63.31000  ? 396  LYS A CG  1 
ATOM   2895  C CD  . LYS A 1 377 ? -0.36300  -42.97700 -17.10300 1.000 73.64000  ? 396  LYS A CD  1 
ATOM   2896  C CE  . LYS A 1 377 ? -0.48100  -41.91200 -18.18500 1.000 75.94000  ? 396  LYS A CE  1 
ATOM   2897  N NZ  . LYS A 1 377 ? 0.22500   -42.28000 -19.45500 1.000 76.44000  ? 396  LYS A NZ  1 
ATOM   2898  N N   . GLU A 1 378 ? -1.03300  -44.79800 -11.59000 1.000 52.49000  ? 397  GLU A N   1 
ATOM   2899  C CA  . GLU A 1 378 ? -1.20500  -45.93900 -10.70300 1.000 53.30000  ? 397  GLU A CA  1 
ATOM   2900  C C   . GLU A 1 378 ? -1.08800  -45.51600 -9.24500  1.000 59.32000  ? 397  GLU A C   1 
ATOM   2901  O O   . GLU A 1 378 ? -0.56700  -44.45000 -8.90800  1.000 59.54000  ? 397  GLU A O   1 
ATOM   2902  C CB  . GLU A 1 378 ? -0.20100  -47.07100 -10.97500 1.000 60.76000  ? 397  GLU A CB  1 
ATOM   2903  C CG  . GLU A 1 378 ? -0.30700  -47.60800 -12.39800 1.000 76.73000  ? 397  GLU A CG  1 
ATOM   2904  C CD  . GLU A 1 378 ? 0.61200   -48.80100 -12.69000 1.000 91.20000  ? 397  GLU A CD  1 
ATOM   2905  O OE1 . GLU A 1 378 ? 1.18900   -49.37500 -11.73800 1.000 83.85000  ? 397  GLU A OE1 1 
ATOM   2906  O OE2 . GLU A 1 378 ? 0.83300   -49.08300 -13.90100 1.000 96.61000  ? 397  GLU A OE2 1 
ATOM   2907  N N   . ILE A 1 379 ? -1.60000  -46.39800 -8.38800  1.000 51.69000  ? 398  ILE A N   1 
ATOM   2908  C CA  . ILE A 1 379 ? -1.70500  -46.21000 -6.94300  1.000 49.69000  ? 398  ILE A CA  1 
ATOM   2909  C C   . ILE A 1 379 ? -0.30700  -46.29200 -6.34600  1.000 58.14000  ? 398  ILE A C   1 
ATOM   2910  O O   . ILE A 1 379 ? 0.30800   -47.36200 -6.33400  1.000 56.08000  ? 398  ILE A O   1 
ATOM   2911  C CB  . ILE A 1 379 ? -2.63200  -47.25900 -6.31600  1.000 42.40000  ? 398  ILE A CB  1 
ATOM   2912  C CG1 . ILE A 1 379 ? -3.96000  -47.30100 -7.07600  1.000 46.44000  ? 398  ILE A CG1 1 
ATOM   2913  C CG2 . ILE A 1 379 ? -2.86200  -46.95300 -4.85600  1.000 50.51000  ? 398  ILE A CG2 1 
ATOM   2914  C CD1 . ILE A 1 379 ? -4.70100  -45.98700 -7.08000  1.000 45.63000  ? 398  ILE A CD1 1 
ATOM   2915  N N   . GLU A 1 380 ? 0.20000   -45.16800 -5.85700  1.000 58.37000  ? 399  GLU A N   1 
ATOM   2916  C CA  . GLU A 1 380 ? 1.46400   -45.17900 -5.14300  1.000 61.38000  ? 399  GLU A CA  1 
ATOM   2917  C C   . GLU A 1 380 ? 1.39500   -44.08100 -4.09900  1.000 61.27000  ? 399  GLU A C   1 
ATOM   2918  O O   . GLU A 1 380 ? 1.01400   -42.94900 -4.41000  1.000 64.47000  ? 399  GLU A O   1 
ATOM   2919  C CB  . GLU A 1 380 ? 2.64800   -44.96800 -6.09500  1.000 72.23000  ? 399  GLU A CB  1 
ATOM   2920  C CG  . GLU A 1 380 ? 4.00600   -45.34800 -5.50000  1.000 64.31000  ? 399  GLU A CG  1 
ATOM   2921  C CD  . GLU A 1 380 ? 5.13400   -45.27900 -6.52000  1.000 84.11000  ? 399  GLU A CD  1 
ATOM   2922  O OE1 . GLU A 1 380 ? 4.89100   -44.78500 -7.64500  1.000 79.03000  ? 399  GLU A OE1 1 
ATOM   2923  O OE2 . GLU A 1 380 ? 6.24900   -45.76400 -6.21500  1.000 96.31000  ? 399  GLU A OE2 1 
ATOM   2924  N N   . ILE A 1 381 ? 1.71200   -44.42500 -2.85900  1.000 54.32000  ? 400  ILE A N   1 
ATOM   2925  C CA  . ILE A 1 381 ? 1.80600   -43.44700 -1.78600  1.000 63.27000  ? 400  ILE A CA  1 
ATOM   2926  C C   . ILE A 1 381 ? 3.09600   -43.71800 -1.02400  1.000 65.30000  ? 400  ILE A C   1 
ATOM   2927  O O   . ILE A 1 381 ? 3.46000   -44.88000 -0.79500  1.000 67.65000  ? 400  ILE A O   1 
ATOM   2928  C CB  . ILE A 1 381 ? 0.56900   -43.47700 -0.86600  1.000 58.81000  ? 400  ILE A CB  1 
ATOM   2929  C CG1 . ILE A 1 381 ? 0.58700   -42.27800 0.09000   1.000 54.06000  ? 400  ILE A CG1 1 
ATOM   2930  C CG2 . ILE A 1 381 ? 0.44300   -44.81400 -0.14300  1.000 62.55000  ? 400  ILE A CG2 1 
ATOM   2931  C CD1 . ILE A 1 381 ? -0.78000  -41.94200 0.67000   1.000 61.75000  ? 400  ILE A CD1 1 
ATOM   2932  N N   . LYS A 1 382 ? 3.82400   -42.65600 -0.69700  1.000 54.87000  ? 401  LYS A N   1 
ATOM   2933  C CA  . LYS A 1 382 ? 5.14000   -42.79700 -0.09700  1.000 57.14000  ? 401  LYS A CA  1 
ATOM   2934  C C   . LYS A 1 382 ? 5.11000   -42.24800 1.32400   1.000 55.94000  ? 401  LYS A C   1 
ATOM   2935  O O   . LYS A 1 382 ? 4.45100   -41.23200 1.59300   1.000 51.66000  ? 401  LYS A O   1 
ATOM   2936  C CB  . LYS A 1 382 ? 6.20500   -42.09500 -0.95800  1.000 57.93000  ? 401  LYS A CB  1 
ATOM   2937  C CG  . LYS A 1 382 ? 7.65300   -42.44800 -0.61600  1.000 61.36000  ? 401  LYS A CG  1 
ATOM   2938  C CD  . LYS A 1 382 ? 8.64000   -41.86700 -1.64500  1.000 55.68000  ? 401  LYS A CD  1 
ATOM   2939  C CE  . LYS A 1 382 ? 8.71700   -42.67300 -2.94600  1.000 52.55000  ? 401  LYS A CE  1 
ATOM   2940  N NZ  . LYS A 1 382 ? 9.43800   -43.97100 -2.80300  1.000 60.97000  ? 401  LYS A NZ  1 
ATOM   2941  N N   . LYS A 1 383 ? 5.76700   -42.97100 2.24600   1.000 66.50000  ? 402  LYS A N   1 
ATOM   2942  C CA  . LYS A 1 383 ? 5.80200   -42.54500 3.64300   1.000 60.33000  ? 402  LYS A CA  1 
ATOM   2943  C C   . LYS A 1 383 ? 6.67200   -41.31000 3.74200   1.000 61.17000  ? 402  LYS A C   1 
ATOM   2944  O O   . LYS A 1 383 ? 7.68900   -41.21000 3.05200   1.000 57.47000  ? 402  LYS A O   1 
ATOM   2945  C CB  . LYS A 1 383 ? 6.38400   -43.60300 4.59400   1.000 63.46000  ? 402  LYS A CB  1 
ATOM   2946  C CG  . LYS A 1 383 ? 5.79500   -45.02000 4.55000   1.000 75.54000  ? 402  LYS A CG  1 
ATOM   2947  C CD  . LYS A 1 383 ? 6.02800   -45.83800 5.81100   1.000 90.59000  ? 402  LYS A CD  1 
ATOM   2948  C CE  . LYS A 1 383 ? 5.66800   -47.18300 5.45300   1.000 85.49000  ? 402  LYS A CE  1 
ATOM   2949  N NZ  . LYS A 1 383 ? 4.23300   -47.11400 5.47900   1.000 88.09000  ? 402  LYS A NZ  1 
ATOM   2950  N N   . LEU A 1 384 ? 6.30700   -40.38600 4.63800   1.000 60.37000  ? 403  LEU A N   1 
ATOM   2951  C CA  . LEU A 1 384 ? 6.99700   -39.09500 4.65400   1.000 58.11000  ? 403  LEU A CA  1 
ATOM   2952  C C   . LEU A 1 384 ? 8.47800   -39.20200 4.99500   1.000 58.95000  ? 403  LEU A C   1 
ATOM   2953  O O   . LEU A 1 384 ? 9.29600   -38.64200 4.24300   1.000 58.21000  ? 403  LEU A O   1 
ATOM   2954  C CB  . LEU A 1 384 ? 6.25900   -38.10500 5.56200   1.000 55.35000  ? 403  LEU A CB  1 
ATOM   2955  C CG  . LEU A 1 384 ? 6.88100   -36.70800 5.65100   1.000 55.27000  ? 403  LEU A CG  1 
ATOM   2956  C CD1 . LEU A 1 384 ? 7.28600   -36.18000 4.29000   1.000 51.58000  ? 403  LEU A CD1 1 
ATOM   2957  C CD2 . LEU A 1 384 ? 5.84200   -35.75800 6.22000   1.000 56.38000  ? 403  LEU A CD2 1 
ATOM   2958  N N   . PRO A 1 385 ? 8.90500   -39.88800 6.06000   1.000 61.14000  ? 404  PRO A N   1 
ATOM   2959  C CA  . PRO A 1 385 ? 10.35900  -40.02700 6.26200   1.000 56.98000  ? 404  PRO A CA  1 
ATOM   2960  C C   . PRO A 1 385 ? 11.05200  -40.61800 5.04700   1.000 54.49000  ? 404  PRO A C   1 
ATOM   2961  O O   . PRO A 1 385 ? 12.12500  -40.15900 4.64100   1.000 54.92000  ? 404  PRO A O   1 
ATOM   2962  C CB  . PRO A 1 385 ? 10.45600  -40.95100 7.48700   1.000 56.24000  ? 404  PRO A CB  1 
ATOM   2963  C CG  . PRO A 1 385 ? 9.16700   -40.75100 8.21600   1.000 61.51000  ? 404  PRO A CG  1 
ATOM   2964  C CD  . PRO A 1 385 ? 8.13800   -40.54200 7.13700   1.000 59.16000  ? 404  PRO A CD  1 
ATOM   2965  N N   . GLU A 1 386 ? 10.41900  -41.60500 4.42800   1.000 54.18000  ? 405  GLU A N   1 
ATOM   2966  C CA  . GLU A 1 386 ? 10.99600  -42.25900 3.26300   1.000 57.13000  ? 405  GLU A CA  1 
ATOM   2967  C C   . GLU A 1 386 ? 11.15700  -41.28200 2.09600   1.000 55.30000  ? 405  GLU A C   1 
ATOM   2968  O O   . GLU A 1 386 ? 12.15900  -41.33000 1.36900   1.000 46.21000  ? 405  GLU A O   1 
ATOM   2969  C CB  . GLU A 1 386 ? 10.11600  -43.46900 2.95800   1.000 69.25000  ? 405  GLU A CB  1 
ATOM   2970  C CG  . GLU A 1 386 ? 10.24400  -44.20800 1.66300   1.000 73.50000  ? 405  GLU A CG  1 
ATOM   2971  C CD  . GLU A 1 386 ? 9.41300   -45.49700 1.72600   1.000 93.09000  ? 405  GLU A CD  1 
ATOM   2972  O OE1 . GLU A 1 386 ? 9.15800   -45.96000 2.87200   1.000 90.10000  ? 405  GLU A OE1 1 
ATOM   2973  O OE2 . GLU A 1 386 ? 8.88300   -45.93900 0.67200   1.000 89.31000  ? 405  GLU A OE2 1 
ATOM   2974  N N   . PHE A 1 387 ? 10.21100  -40.34800 1.94100   1.000 52.66000  ? 406  PHE A N   1 
ATOM   2975  C CA  . PHE A 1 387 ? 10.36800  -39.28600 0.94600   1.000 49.23000  ? 406  PHE A CA  1 
ATOM   2976  C C   . PHE A 1 387 ? 11.43400  -38.27300 1.36300   1.000 50.82000  ? 406  PHE A C   1 
ATOM   2977  O O   . PHE A 1 387 ? 12.27700  -37.87800 0.54800   1.000 51.00000  ? 406  PHE A O   1 
ATOM   2978  C CB  . PHE A 1 387 ? 9.02900   -38.58500 0.70000   1.000 47.03000  ? 406  PHE A CB  1 
ATOM   2979  C CG  . PHE A 1 387 ? 9.12300   -37.40100 -0.22600  1.000 45.44000  ? 406  PHE A CG  1 
ATOM   2980  C CD1 . PHE A 1 387 ? 9.34600   -37.57300 -1.58700  1.000 44.01000  ? 406  PHE A CD1 1 
ATOM   2981  C CD2 . PHE A 1 387 ? 8.97000   -36.11300 0.26800   1.000 44.36000  ? 406  PHE A CD2 1 
ATOM   2982  C CE1 . PHE A 1 387 ? 9.43000   -36.47700 -2.43800  1.000 36.92000  ? 406  PHE A CE1 1 
ATOM   2983  C CE2 . PHE A 1 387 ? 9.05500   -35.01200 -0.57200  1.000 36.79000  ? 406  PHE A CE2 1 
ATOM   2984  C CZ  . PHE A 1 387 ? 9.28200   -35.19200 -1.92900  1.000 34.93000  ? 406  PHE A CZ  1 
ATOM   2985  N N   . GLU A 1 388 ? 11.40300  -37.82500 2.62200   1.000 52.29000  ? 407  GLU A N   1 
ATOM   2986  C CA  . GLU A 1 388 ? 12.41300  -36.87700 3.09100   1.000 49.35000  ? 407  GLU A CA  1 
ATOM   2987  C C   . GLU A 1 388 ? 13.82000  -37.45500 3.00000   1.000 47.75000  ? 407  GLU A C   1 
ATOM   2988  O O   . GLU A 1 388 ? 14.78200  -36.71400 2.76600   1.000 45.73000  ? 407  GLU A O   1 
ATOM   2989  C CB  . GLU A 1 388 ? 12.06900  -36.41900 4.51100   1.000 55.38000  ? 407  GLU A CB  1 
ATOM   2990  C CG  . GLU A 1 388 ? 11.05700  -35.27000 4.52400   1.000 53.30000  ? 407  GLU A CG  1 
ATOM   2991  C CD  . GLU A 1 388 ? 10.39600  -35.04800 5.87200   1.000 62.81000  ? 407  GLU A CD  1 
ATOM   2992  O OE1 . GLU A 1 388 ? 10.40500  -35.98100 6.71100   1.000 61.16000  ? 407  GLU A OE1 1 
ATOM   2993  O OE2 . GLU A 1 388 ? 9.88100   -33.92700 6.09400   1.000 61.15000  ? 407  GLU A OE2 1 
ATOM   2994  N N   . ALA A 1 389 ? 13.95700  -38.77500 3.12900   1.000 49.41000  ? 408  ALA A N   1 
ATOM   2995  C CA  . ALA A 1 389 ? 15.24000  -39.40800 2.84800   1.000 45.18000  ? 408  ALA A CA  1 
ATOM   2996  C C   . ALA A 1 389 ? 15.63300  -39.25800 1.37800   1.000 50.01000  ? 408  ALA A C   1 
ATOM   2997  O O   . ALA A 1 389 ? 16.82000  -39.12100 1.06600   1.000 51.37000  ? 408  ALA A O   1 
ATOM   2998  C CB  . ALA A 1 389 ? 15.19100  -40.88000 3.25700   1.000 42.06000  ? 408  ALA A CB  1 
ATOM   2999  N N   . MET A 1 390 ? 14.66500  -39.28300 0.45600   1.000 52.05000  ? 409  MET A N   1 
ATOM   3000  C CA  . MET A 1 390 ? 14.98900  -38.99600 -0.94100  1.000 48.24000  ? 409  MET A CA  1 
ATOM   3001  C C   . MET A 1 390 ? 15.48800  -37.57000 -1.11300  1.000 44.40000  ? 409  MET A C   1 
ATOM   3002  O O   . MET A 1 390 ? 16.49900  -37.33000 -1.78100  1.000 42.82000  ? 409  MET A O   1 
ATOM   3003  C CB  . MET A 1 390 ? 13.77800  -39.22100 -1.84300  1.000 50.57000  ? 409  MET A CB  1 
ATOM   3004  C CG  . MET A 1 390 ? 13.51900  -40.64100 -2.25200  1.000 56.99000  ? 409  MET A CG  1 
ATOM   3005  S SD  . MET A 1 390 ? 12.08400  -40.70100 -3.34400  1.000 60.94000  ? 409  MET A SD  1 
ATOM   3006  C CE  . MET A 1 390 ? 12.15700  -42.41600 -3.86200  1.000 58.24000  ? 409  MET A CE  1 
ATOM   3007  N N   . VAL A 1 391 ? 14.77500  -36.60600 -0.53400  1.000 42.42000  ? 410  VAL A N   1 
ATOM   3008  C CA  . VAL A 1 391 ? 15.11100  -35.20700 -0.76900  1.000 41.33000  ? 410  VAL A CA  1 
ATOM   3009  C C   . VAL A 1 391 ? 16.49300  -34.89800 -0.21000  1.000 48.71000  ? 410  VAL A C   1 
ATOM   3010  O O   . VAL A 1 391 ? 17.30100  -34.21100 -0.84900  1.000 49.81000  ? 410  VAL A O   1 
ATOM   3011  C CB  . VAL A 1 391 ? 14.03800  -34.29200 -0.15700  1.000 45.03000  ? 410  VAL A CB  1 
ATOM   3012  C CG1 . VAL A 1 391 ? 14.34800  -32.83500 -0.45800  1.000 46.20000  ? 410  VAL A CG1 1 
ATOM   3013  C CG2 . VAL A 1 391 ? 12.65100  -34.69000 -0.64800  1.000 43.07000  ? 410  VAL A CG2 1 
ATOM   3014  N N   . ASN A 1 392 ? 16.79300  -35.41800 0.98300   1.000 49.83000  ? 411  ASN A N   1 
ATOM   3015  C CA  . ASN A 1 392 ? 18.07300  -35.16900 1.63000   1.000 48.68000  ? 411  ASN A CA  1 
ATOM   3016  C C   . ASN A 1 392 ? 19.20900  -35.96400 1.01100   1.000 50.84000  ? 411  ASN A C   1 
ATOM   3017  O O   . ASN A 1 392 ? 20.36700  -35.73600 1.37300   1.000 50.37000  ? 411  ASN A O   1 
ATOM   3018  C CB  . ASN A 1 392 ? 17.96100  -35.48400 3.11700   1.000 45.22000  ? 411  ASN A CB  1 
ATOM   3019  C CG  . ASN A 1 392 ? 16.99400  -34.56400 3.81900   1.000 52.61000  ? 411  ASN A CG  1 
ATOM   3020  O OD1 . ASN A 1 392 ? 16.90900  -33.37400 3.50500   1.000 58.15000  ? 411  ASN A OD1 1 
ATOM   3021  N ND2 . ASN A 1 392 ? 16.25800  -35.10300 4.77700   1.000 55.76000  ? 411  ASN A ND2 1 
ATOM   3022  N N   . ALA A 1 393 ? 18.90900  -36.89600 0.10900   1.000 50.45000  ? 412  ALA A N   1 
ATOM   3023  C CA  . ALA A 1 393 ? 19.92300  -37.55200 -0.70100  1.000 45.03000  ? 412  ALA A CA  1 
ATOM   3024  C C   . ALA A 1 393 ? 20.09100  -36.88700 -2.05700  1.000 50.10000  ? 412  ALA A C   1 
ATOM   3025  O O   . ALA A 1 393 ? 20.87100  -37.37200 -2.87900  1.000 48.17000  ? 412  ALA A O   1 
ATOM   3026  C CB  . ALA A 1 393 ? 19.57700  -39.03200 -0.89200  1.000 41.97000  ? 412  ALA A CB  1 
ATOM   3027  N N   . GLY A 1 394 ? 19.37700  -35.79200 -2.30800  1.000 47.32000  ? 413  GLY A N   1 
ATOM   3028  C CA  . GLY A 1 394 ? 19.42400  -35.15100 -3.60600  1.000 48.26000  ? 413  GLY A CA  1 
ATOM   3029  C C   . GLY A 1 394 ? 18.65000  -35.86800 -4.68700  1.000 50.41000  ? 413  GLY A C   1 
ATOM   3030  O O   . GLY A 1 394 ? 18.83900  -35.57100 -5.87100  1.000 49.57000  ? 413  GLY A O   1 
ATOM   3031  N N   . ASN A 1 395 ? 17.77600  -36.80100 -4.31100  1.000 45.32000  ? 414  ASN A N   1 
ATOM   3032  C CA  . ASN A 1 395 ? 17.02200  -37.60800 -5.26300  1.000 44.59000  ? 414  ASN A CA  1 
ATOM   3033  C C   . ASN A 1 395 ? 15.68600  -36.92800 -5.54700  1.000 47.99000  ? 414  ASN A C   1 
ATOM   3034  O O   . ASN A 1 395 ? 14.81700  -36.84500 -4.67300  1.000 47.63000  ? 414  ASN A O   1 
ATOM   3035  C CB  . ASN A 1 395 ? 16.85700  -39.02700 -4.72100  1.000 46.07000  ? 414  ASN A CB  1 
ATOM   3036  C CG  . ASN A 1 395 ? 16.11900  -39.95100 -5.67600  1.000 53.66000  ? 414  ASN A CG  1 
ATOM   3037  O OD1 . ASN A 1 395 ? 15.47300  -39.51100 -6.62800  1.000 56.28000  ? 414  ASN A OD1 1 
ATOM   3038  N ND2 . ASN A 1 395 ? 16.26200  -41.25000 -5.45500  1.000 58.93000  ? 414  ASN A ND2 1 
ATOM   3039  N N   . THR A 1 396 ? 15.52100  -36.45700 -6.78200  1.000 44.32000  ? 415  THR A N   1 
ATOM   3040  C CA  . THR A 1 396 ? 14.36000  -35.67700 -7.18900  1.000 51.62000  ? 415  THR A CA  1 
ATOM   3041  C C   . THR A 1 396 ? 13.47400  -36.42700 -8.18000  1.000 47.67000  ? 415  THR A C   1 
ATOM   3042  O O   . THR A 1 396 ? 12.77000  -35.80000 -8.97700  1.000 41.75000  ? 415  THR A O   1 
ATOM   3043  C CB  . THR A 1 396 ? 14.82300  -34.34800 -7.78400  1.000 50.61000  ? 415  THR A CB  1 
ATOM   3044  O OG1 . THR A 1 396 ? 15.65200  -34.59800 -8.93400  1.000 45.07000  ? 415  THR A OG1 1 
ATOM   3045  C CG2 . THR A 1 396 ? 15.61800  -33.56800 -6.74100  1.000 42.33000  ? 415  THR A CG2 1 
ATOM   3046  N N   . THR A 1 397 ? 13.50800  -37.76000 -8.15300  1.000 49.43000  ? 416  THR A N   1 
ATOM   3047  C CA  . THR A 1 397 ? 12.81300  -38.55900 -9.15300  1.000 46.88000  ? 416  THR A CA  1 
ATOM   3048  C C   . THR A 1 397 ? 11.34300  -38.79800 -8.82500  1.000 55.00000  ? 416  THR A C   1 
ATOM   3049  O O   . THR A 1 397 ? 10.56200  -39.08800 -9.74100  1.000 57.25000  ? 416  THR A O   1 
ATOM   3050  C CB  . THR A 1 397 ? 13.51300  -39.91000 -9.32200  1.000 46.23000  ? 416  THR A CB  1 
ATOM   3051  O OG1 . THR A 1 397 ? 13.47800  -40.62300 -8.08100  1.000 51.09000  ? 416  THR A OG1 1 
ATOM   3052  C CG2 . THR A 1 397 ? 14.95900  -39.71200 -9.76100  1.000 40.95000  ? 416  THR A CG2 1 
ATOM   3053  N N   . TYR A 1 398 ? 10.94300  -38.69700 -7.55800  1.000 50.63000  ? 417  TYR A N   1 
ATOM   3054  C CA  . TYR A 1 398 ? 9.58700   -39.05800 -7.16900  1.000 48.85000  ? 417  TYR A CA  1 
ATOM   3055  C C   . TYR A 1 398 ? 8.61800   -37.89800 -7.35400  1.000 50.21000  ? 417  TYR A C   1 
ATOM   3056  O O   . TYR A 1 398 ? 8.86800   -36.78300 -6.88200  1.000 45.77000  ? 417  TYR A O   1 
ATOM   3057  C CB  . TYR A 1 398 ? 9.51800   -39.53600 -5.72200  1.000 46.24000  ? 417  TYR A CB  1 
ATOM   3058  C CG  . TYR A 1 398 ? 8.10700   -39.93000 -5.33200  1.000 43.07000  ? 417  TYR A CG  1 
ATOM   3059  C CD1 . TYR A 1 398 ? 7.55300   -41.12100 -5.78000  1.000 42.73000  ? 417  TYR A CD1 1 
ATOM   3060  C CD2 . TYR A 1 398 ? 7.32200   -39.09700 -4.54800  1.000 46.23000  ? 417  TYR A CD2 1 
ATOM   3061  C CE1 . TYR A 1 398 ? 6.27200   -41.48800 -5.43400  1.000 47.31000  ? 417  TYR A CE1 1 
ATOM   3062  C CE2 . TYR A 1 398 ? 6.02400   -39.45400 -4.19400  1.000 46.96000  ? 417  TYR A CE2 1 
ATOM   3063  C CZ  . TYR A 1 398 ? 5.50500   -40.65000 -4.64100  1.000 48.71000  ? 417  TYR A CZ  1 
ATOM   3064  O OH  . TYR A 1 398 ? 4.21900   -41.01400 -4.30200  1.000 48.91000  ? 417  TYR A OH  1 
ATOM   3065  N N   . THR A 1 399 ? 7.50700   -38.18800 -8.02900  1.000 44.61000  ? 418  THR A N   1 
ATOM   3066  C CA  . THR A 1 399 ? 6.35300   -37.31100 -8.17100  1.000 43.88000  ? 418  THR A CA  1 
ATOM   3067  C C   . THR A 1 399 ? 5.14000   -38.12400 -7.74700  1.000 41.11000  ? 418  THR A C   1 
ATOM   3068  O O   . THR A 1 399 ? 4.97000   -39.25700 -8.20600  1.000 40.38000  ? 418  THR A O   1 
ATOM   3069  C CB  . THR A 1 399 ? 6.18200   -36.83900 -9.63000  1.000 42.04000  ? 418  THR A CB  1 
ATOM   3070  O OG1 . THR A 1 399 ? 7.39100   -36.21800 -10.09100 1.000 54.66000  ? 418  THR A OG1 1 
ATOM   3071  C CG2 . THR A 1 399 ? 5.06100   -35.84500 -9.75000  1.000 41.65000  ? 418  THR A CG2 1 
ATOM   3072  N N   . GLY A 1 400 ? 4.31200   -37.58200 -6.87600  1.000 42.80000  ? 419  GLY A N   1 
ATOM   3073  C CA  . GLY A 1 400 ? 3.12000   -38.29400 -6.46900  1.000 43.85000  ? 419  GLY A CA  1 
ATOM   3074  C C   . GLY A 1 400 ? 2.71800   -37.94500 -5.05100  1.000 47.13000  ? 419  GLY A C   1 
ATOM   3075  O O   . GLY A 1 400 ? 3.20400   -36.98200 -4.46300  1.000 41.65000  ? 419  GLY A O   1 
ATOM   3076  N N   . LEU A 1 401 ? 1.79500   -38.75000 -4.52400  1.000 50.76000  ? 420  LEU A N   1 
ATOM   3077  C CA  . LEU A 1 401 ? 1.31200   -38.54600 -3.16600  1.000 49.05000  ? 420  LEU A CA  1 
ATOM   3078  C C   . LEU A 1 401 ? 2.35100   -39.00600 -2.15600  1.000 52.40000  ? 420  LEU A C   1 
ATOM   3079  O O   . LEU A 1 401 ? 3.07800   -39.98200 -2.37700  1.000 47.03000  ? 420  LEU A O   1 
ATOM   3080  C CB  . LEU A 1 401 ? -0.00400  -39.29200 -2.92600  1.000 45.50000  ? 420  LEU A CB  1 
ATOM   3081  C CG  . LEU A 1 401 ? -1.23500  -38.85400 -3.71500  1.000 47.92000  ? 420  LEU A CG  1 
ATOM   3082  C CD1 . LEU A 1 401 ? -2.44100  -39.68900 -3.30900  1.000 47.85000  ? 420  LEU A CD1 1 
ATOM   3083  C CD2 . LEU A 1 401 ? -1.51000  -37.37300 -3.53600  1.000 45.63000  ? 420  LEU A CD2 1 
ATOM   3084  N N   . VAL A 1 402 ? 2.43200   -38.27500 -1.05000  1.000 48.72000  ? 421  VAL A N   1 
ATOM   3085  C CA  . VAL A 1 402 ? 3.30000   -38.62300 0.06300   1.000 48.53000  ? 421  VAL A CA  1 
ATOM   3086  C C   . VAL A 1 402 ? 2.46200   -38.51300 1.32000   1.000 47.99000  ? 421  VAL A C   1 
ATOM   3087  O O   . VAL A 1 402 ? 1.75100   -37.51900 1.50900   1.000 46.22000  ? 421  VAL A O   1 
ATOM   3088  C CB  . VAL A 1 402 ? 4.53100   -37.70400 0.14700   1.000 40.23000  ? 421  VAL A CB  1 
ATOM   3089  C CG1 . VAL A 1 402 ? 5.39300   -38.09800 1.33500   1.000 49.59000  ? 421  VAL A CG1 1 
ATOM   3090  C CG2 . VAL A 1 402 ? 5.30900   -37.75500 -1.15800  1.000 41.20000  ? 421  VAL A CG2 1 
ATOM   3091  N N   . GLU A 1 403 ? 2.52300   -39.52900 2.16800   1.000 53.90000  ? 422  GLU A N   1 
ATOM   3092  C CA  . GLU A 1 403 ? 1.58200   -39.58000 3.27200   1.000 61.28000  ? 422  GLU A CA  1 
ATOM   3093  C C   . GLU A 1 403 ? 1.82200   -38.42700 4.23200   1.000 50.33000  ? 422  GLU A C   1 
ATOM   3094  O O   . GLU A 1 403 ? 2.94900   -38.18400 4.67000   1.000 53.12000  ? 422  GLU A O   1 
ATOM   3095  C CB  . GLU A 1 403 ? 1.67100   -40.92300 3.98900   1.000 66.61000  ? 422  GLU A CB  1 
ATOM   3096  C CG  . GLU A 1 403 ? 0.53000   -41.11400 4.96000   1.000 74.83000  ? 422  GLU A CG  1 
ATOM   3097  C CD  . GLU A 1 403 ? 0.28900   -42.57200 5.27200   1.000 91.04000  ? 422  GLU A CD  1 
ATOM   3098  O OE1 . GLU A 1 403 ? 1.08700   -43.41900 4.80600   1.000 94.27000  ? 422  GLU A OE1 1 
ATOM   3099  O OE2 . GLU A 1 403 ? -0.73300  -42.87200 5.92800   1.000 86.85000  ? 422  GLU A OE2 1 
ATOM   3100  N N   . GLY A 1 404 ? 0.75100   -37.69100 4.52500   1.000 43.28000  ? 423  GLY A N   1 
ATOM   3101  C CA  . GLY A 1 404 ? 0.76900   -36.61900 5.49100   1.000 50.38000  ? 423  GLY A CA  1 
ATOM   3102  C C   . GLY A 1 404 ? 0.64000   -35.23400 4.89100   1.000 59.06000  ? 423  GLY A C   1 
ATOM   3103  O O   . GLY A 1 404 ? -0.01500  -34.37200 5.49100   1.000 66.07000  ? 423  GLY A O   1 
ATOM   3104  N N   . ILE A 1 405 ? 1.23400   -35.00000 3.72500   1.000 50.65000  ? 424  ILE A N   1 
ATOM   3105  C CA  . ILE A 1 405 ? 1.23700   -33.66500 3.14000   1.000 56.93000  ? 424  ILE A CA  1 
ATOM   3106  C C   . ILE A 1 405 ? 0.49000   -33.57100 1.81600   1.000 55.79000  ? 424  ILE A C   1 
ATOM   3107  O O   . ILE A 1 405 ? 0.11500   -32.45400 1.41700   1.000 55.19000  ? 424  ILE A O   1 
ATOM   3108  C CB  . ILE A 1 405 ? 2.67400   -33.13200 2.97600   1.000 60.96000  ? 424  ILE A CB  1 
ATOM   3109  C CG1 . ILE A 1 405 ? 3.54400   -34.18100 2.26900   1.000 55.42000  ? 424  ILE A CG1 1 
ATOM   3110  C CG2 . ILE A 1 405 ? 3.22800   -32.67000 4.32800   1.000 54.19000  ? 424  ILE A CG2 1 
ATOM   3111  C CD1 . ILE A 1 405 ? 4.90700   -33.67400 1.84300   1.000 58.09000  ? 424  ILE A CD1 1 
ATOM   3112  N N   . GLY A 1 406 ? 0.25100   -34.67600 1.11600   1.000 54.21000  ? 425  GLY A N   1 
ATOM   3113  C CA  . GLY A 1 406 ? -0.47600  -34.60400 -0.13600  1.000 53.16000  ? 425  GLY A CA  1 
ATOM   3114  C C   . GLY A 1 406 ? 0.36600   -34.95900 -1.34400  1.000 44.60000  ? 425  GLY A C   1 
ATOM   3115  O O   . GLY A 1 406 ? 1.00200   -36.01800 -1.37400  1.000 41.07000  ? 425  GLY A O   1 
ATOM   3116  N N   . TYR A 1 407 ? 0.38700   -34.07200 -2.33600  1.000 41.47000  ? 426  TYR A N   1 
ATOM   3117  C CA  . TYR A 1 407 ? 1.06800   -34.30400 -3.60300  1.000 42.90000  ? 426  TYR A CA  1 
ATOM   3118  C C   . TYR A 1 407 ? 2.36000   -33.49200 -3.67700  1.000 46.33000  ? 426  TYR A C   1 
ATOM   3119  O O   . TYR A 1 407 ? 2.40100   -32.32500 -3.27300  1.000 42.97000  ? 426  TYR A O   1 
ATOM   3120  C CB  . TYR A 1 407 ? 0.14200   -33.94000 -4.76800  1.000 43.37000  ? 426  TYR A CB  1 
ATOM   3121  C CG  . TYR A 1 407 ? 0.69200   -34.21500 -6.15400  1.000 40.93000  ? 426  TYR A CG  1 
ATOM   3122  C CD1 . TYR A 1 407 ? 0.80800   -35.51800 -6.63000  1.000 43.99000  ? 426  TYR A CD1 1 
ATOM   3123  C CD2 . TYR A 1 407 ? 1.05000   -33.17300 -7.00400  1.000 43.94000  ? 426  TYR A CD2 1 
ATOM   3124  C CE1 . TYR A 1 407 ? 1.29100   -35.77700 -7.90600  1.000 48.78000  ? 426  TYR A CE1 1 
ATOM   3125  C CE2 . TYR A 1 407 ? 1.53200   -33.42000 -8.29100  1.000 46.57000  ? 426  TYR A CE2 1 
ATOM   3126  C CZ  . TYR A 1 407 ? 1.65300   -34.72400 -8.73300  1.000 50.47000  ? 426  TYR A CZ  1 
ATOM   3127  O OH  . TYR A 1 407 ? 2.12700   -34.98300 -10.00100 1.000 51.12000  ? 426  TYR A OH  1 
ATOM   3128  N N   . VAL A 1 408 ? 3.41500   -34.11700 -4.19200  1.000 36.13000  ? 427  VAL A N   1 
ATOM   3129  C CA  . VAL A 1 408 ? 4.69500   -33.45500 -4.39700  1.000 45.22000  ? 427  VAL A CA  1 
ATOM   3130  C C   . VAL A 1 408 ? 5.06400   -33.56500 -5.87000  1.000 48.59000  ? 427  VAL A C   1 
ATOM   3131  O O   . VAL A 1 408 ? 4.74400   -34.56200 -6.53000  1.000 45.47000  ? 427  VAL A O   1 
ATOM   3132  C CB  . VAL A 1 408 ? 5.81500   -34.04100 -3.50200  1.000 35.65000  ? 427  VAL A CB  1 
ATOM   3133  C CG1 . VAL A 1 408 ? 5.46000   -33.90100 -2.03900  1.000 40.76000  ? 427  VAL A CG1 1 
ATOM   3134  C CG2 . VAL A 1 408 ? 6.08500   -35.49300 -3.84600  1.000 35.31000  ? 427  VAL A CG2 1 
ATOM   3135  N N   . TYR A 1 409 ? 5.70800   -32.52000 -6.39100  1.000 45.85000  ? 428  TYR A N   1 
ATOM   3136  C CA  . TYR A 1 409 ? 6.26200   -32.55800 -7.73500  1.000 44.93000  ? 428  TYR A CA  1 
ATOM   3137  C C   . TYR A 1 409 ? 7.36500   -31.51100 -7.83400  1.000 44.74000  ? 428  TYR A C   1 
ATOM   3138  O O   . TYR A 1 409 ? 7.51100   -30.64400 -6.97000  1.000 44.21000  ? 428  TYR A O   1 
ATOM   3139  C CB  . TYR A 1 409 ? 5.17300   -32.34500 -8.80100  1.000 41.82000  ? 428  TYR A CB  1 
ATOM   3140  C CG  . TYR A 1 409 ? 4.63800   -30.93700 -8.93100  1.000 39.62000  ? 428  TYR A CG  1 
ATOM   3141  C CD1 . TYR A 1 409 ? 3.64900   -30.46100 -8.09200  1.000 43.20000  ? 428  TYR A CD1 1 
ATOM   3142  C CD2 . TYR A 1 409 ? 5.08300   -30.10600 -9.94700  1.000 46.76000  ? 428  TYR A CD2 1 
ATOM   3143  C CE1 . TYR A 1 409 ? 3.14500   -29.17500 -8.23700  1.000 42.91000  ? 428  TYR A CE1 1 
ATOM   3144  C CE2 . TYR A 1 409 ? 4.58700   -28.82800 -10.09700 1.000 40.58000  ? 428  TYR A CE2 1 
ATOM   3145  C CZ  . TYR A 1 409 ? 3.62400   -28.36600 -9.24100  1.000 43.90000  ? 428  TYR A CZ  1 
ATOM   3146  O OH  . TYR A 1 409 ? 3.13900   -27.08900 -9.39800  1.000 46.45000  ? 428  TYR A OH  1 
ATOM   3147  N N   . TRP A 1 410 ? 8.13800   -31.59800 -8.90800  1.000 42.58000  ? 429  TRP A N   1 
ATOM   3148  C CA  . TRP A 1 410 ? 9.34400   -30.80900 -9.08100  1.000 40.22000  ? 429  TRP A CA  1 
ATOM   3149  C C   . TRP A 1 410 ? 9.22800   -29.90700 -10.30300 1.000 42.36000  ? 429  TRP A C   1 
ATOM   3150  O O   . TRP A 1 410 ? 8.71900   -30.32400 -11.34600 1.000 34.41000  ? 429  TRP A O   1 
ATOM   3151  C CB  . TRP A 1 410 ? 10.54000  -31.73000 -9.25500  1.000 43.15000  ? 429  TRP A CB  1 
ATOM   3152  C CG  . TRP A 1 410 ? 10.76600  -32.62500 -8.09500  1.000 50.35000  ? 429  TRP A CG  1 
ATOM   3153  C CD1 . TRP A 1 410 ? 10.24400  -33.87200 -7.91400  1.000 48.12000  ? 429  TRP A CD1 1 
ATOM   3154  C CD2 . TRP A 1 410 ? 11.60300  -32.37000 -6.96100  1.000 47.49000  ? 429  TRP A CD2 1 
ATOM   3155  N NE1 . TRP A 1 410 ? 10.68300  -34.40100 -6.72700  1.000 52.16000  ? 429  TRP A NE1 1 
ATOM   3156  C CE2 . TRP A 1 410 ? 11.52500  -33.50200 -6.12400  1.000 52.25000  ? 429  TRP A CE2 1 
ATOM   3157  C CE3 . TRP A 1 410 ? 12.39400  -31.28800 -6.56200  1.000 44.73000  ? 429  TRP A CE3 1 
ATOM   3158  C CZ2 . TRP A 1 410 ? 12.21300  -33.58900 -4.91500  1.000 47.31000  ? 429  TRP A CZ2 1 
ATOM   3159  C CZ3 . TRP A 1 410 ? 13.07900  -31.37600 -5.36700  1.000 47.23000  ? 429  TRP A CZ3 1 
ATOM   3160  C CH2 . TRP A 1 410 ? 12.98500  -32.51900 -4.55700  1.000 48.88000  ? 429  TRP A CH2 1 
ATOM   3161  N N   . THR A 1 411 ? 9.72900   -28.68200 -10.18300 1.000 41.40000  ? 430  THR A N   1 
ATOM   3162  C CA  . THR A 1 411 ? 10.02000  -27.84800 -11.33800 1.000 38.77000  ? 430  THR A CA  1 
ATOM   3163  C C   . THR A 1 411 ? 11.52200  -27.57900 -11.40100 1.000 45.04000  ? 430  THR A C   1 
ATOM   3164  O O   . THR A 1 411 ? 12.21900  -27.54800 -10.37900 1.000 42.18000  ? 430  THR A O   1 
ATOM   3165  C CB  . THR A 1 411 ? 9.25200   -26.52300 -11.31200 1.000 42.55000  ? 430  THR A CB  1 
ATOM   3166  O OG1 . THR A 1 411 ? 9.65500   -25.75300 -10.17400 1.000 46.78000  ? 430  THR A OG1 1 
ATOM   3167  C CG2 . THR A 1 411 ? 7.75100   -26.77500 -11.25900 1.000 41.41000  ? 430  THR A CG2 1 
ATOM   3168  N N   . THR A 1 412 ? 12.01600  -27.39900 -12.61800 1.000 45.37000  ? 431  THR A N   1 
ATOM   3169  C CA  . THR A 1 412 ? 13.44100  -27.31100 -12.88800 1.000 44.21000  ? 431  THR A CA  1 
ATOM   3170  C C   . THR A 1 412 ? 13.77300  -25.99300 -13.56700 1.000 45.58000  ? 431  THR A C   1 
ATOM   3171  O O   . THR A 1 412 ? 12.98200  -25.46900 -14.35900 1.000 48.72000  ? 431  THR A O   1 
ATOM   3172  C CB  . THR A 1 412 ? 13.89600  -28.49200 -13.74300 1.000 45.57000  ? 431  THR A CB  1 
ATOM   3173  O OG1 . THR A 1 412 ? 13.79900  -29.68700 -12.96500 1.000 48.15000  ? 431  THR A OG1 1 
ATOM   3174  C CG2 . THR A 1 412 ? 15.32100  -28.31300 -14.22700 1.000 48.31000  ? 431  THR A CG2 1 
ATOM   3175  N N   . GLU A 1 413 ? 14.94000  -25.46000 -13.21700 1.000 43.37000  ? 432  GLU A N   1 
ATOM   3176  C CA  . GLU A 1 413 ? 15.43500  -24.20700 -13.75000 1.000 41.73000  ? 432  GLU A CA  1 
ATOM   3177  C C   . GLU A 1 413 ? 16.94600  -24.22000 -13.63200 1.000 46.44000  ? 432  GLU A C   1 
ATOM   3178  O O   . GLU A 1 413 ? 17.50600  -24.79700 -12.68800 1.000 38.36000  ? 432  GLU A O   1 
ATOM   3179  C CB  . GLU A 1 413 ? 14.79300  -23.03800 -12.99900 1.000 41.94000  ? 432  GLU A CB  1 
ATOM   3180  C CG  . GLU A 1 413 ? 15.01600  -21.58600 -13.44600 1.000 45.72000  ? 432  GLU A CG  1 
ATOM   3181  C CD  . GLU A 1 413 ? 14.94900  -21.34800 -14.95100 1.000 53.17000  ? 432  GLU A CD  1 
ATOM   3182  O OE1 . GLU A 1 413 ? 15.36700  -22.20900 -15.76400 1.000 54.05000  ? 432  GLU A OE1 1 
ATOM   3183  O OE2 . GLU A 1 413 ? 14.23500  -20.37800 -15.32200 1.000 53.03000  ? 432  GLU A OE2 1 
ATOM   3184  N N   . THR A 1 414 ? 17.60000  -23.63200 -14.62900 1.000 48.47000  ? 433  THR A N   1 
ATOM   3185  C CA  . THR A 1 414 ? 19.05200  -23.53000 -14.65800 1.000 43.46000  ? 433  THR A CA  1 
ATOM   3186  C C   . THR A 1 414 ? 19.45200  -22.10600 -14.29400 1.000 42.20000  ? 433  THR A C   1 
ATOM   3187  O O   . THR A 1 414 ? 18.89500  -21.14100 -14.82900 1.000 40.62000  ? 433  THR A O   1 
ATOM   3188  C CB  . THR A 1 414 ? 19.59200  -23.91300 -16.03600 1.000 48.69000  ? 433  THR A CB  1 
ATOM   3189  O OG1 . THR A 1 414 ? 19.13900  -25.23500 -16.36300 1.000 57.22000  ? 433  THR A OG1 1 
ATOM   3190  C CG2 . THR A 1 414 ? 21.10700  -23.90600 -16.03900 1.000 45.80000  ? 433  THR A CG2 1 
ATOM   3191  N N   . LEU A 1 415 ? 20.38900  -21.98200 -13.36100 1.000 43.11000  ? 434  LEU A N   1 
ATOM   3192  C CA  . LEU A 1 415 ? 20.92900  -20.69900 -12.94100 1.000 40.24000  ? 434  LEU A CA  1 
ATOM   3193  C C   . LEU A 1 415 ? 22.28800  -20.51500 -13.59400 1.000 40.61000  ? 434  LEU A C   1 
ATOM   3194  O O   . LEU A 1 415 ? 23.08400  -21.45300 -13.63600 1.000 46.51000  ? 434  LEU A O   1 
ATOM   3195  C CB  . LEU A 1 415 ? 21.08500  -20.64900 -11.42000 1.000 42.69000  ? 434  LEU A CB  1 
ATOM   3196  C CG  . LEU A 1 415 ? 19.83900  -20.90000 -10.56000 1.000 46.45000  ? 434  LEU A CG  1 
ATOM   3197  C CD1 . LEU A 1 415 ? 20.18800  -20.90500 -9.08700  1.000 35.26000  ? 434  LEU A CD1 1 
ATOM   3198  C CD2 . LEU A 1 415 ? 18.74400  -19.89100 -10.86100 1.000 43.82000  ? 434  LEU A CD2 1 
ATOM   3199  N N   . TYR A 1 416 ? 22.56400  -19.31900 -14.10300 1.000 37.75000  ? 435  TYR A N   1 
ATOM   3200  C CA  . TYR A 1 416 ? 23.89300  -19.03600 -14.62500 1.000 41.08000  ? 435  TYR A CA  1 
ATOM   3201  C C   . TYR A 1 416 ? 24.64700  -18.11200 -13.67900 1.000 47.64000  ? 435  TYR A C   1 
ATOM   3202  O O   . TYR A 1 416 ? 24.04600  -17.23800 -13.04400 1.000 44.11000  ? 435  TYR A O   1 
ATOM   3203  C CB  . TYR A 1 416 ? 23.89500  -18.39600 -16.02000 1.000 39.46000  ? 435  TYR A CB  1 
ATOM   3204  C CG  . TYR A 1 416 ? 23.45100  -19.27600 -17.16600 1.000 46.06000  ? 435  TYR A CG  1 
ATOM   3205  C CD1 . TYR A 1 416 ? 22.49200  -20.27100 -17.00800 1.000 47.69000  ? 435  TYR A CD1 1 
ATOM   3206  C CD2 . TYR A 1 416 ? 24.16500  -19.25200 -18.35300 1.000 45.97000  ? 435  TYR A CD2 1 
ATOM   3207  C CE1 . TYR A 1 416 ? 22.13600  -21.09000 -18.07100 1.000 47.34000  ? 435  TYR A CE1 1 
ATOM   3208  C CE2 . TYR A 1 416 ? 23.84700  -20.08000 -19.40400 1.000 47.18000  ? 435  TYR A CE2 1 
ATOM   3209  C CZ  . TYR A 1 416 ? 22.84100  -20.99900 -19.26600 1.000 49.65000  ? 435  TYR A CZ  1 
ATOM   3210  O OH  . TYR A 1 416 ? 22.55300  -21.81300 -20.34000 1.000 42.32000  ? 435  TYR A OH  1 
ATOM   3211  N N   . PHE A 1 417 ? 25.97100  -18.31000 -13.57300 1.000 44.67000  ? 436  PHE A N   1 
ATOM   3212  C CA  . PHE A 1 417 ? 26.79600  -17.36600 -12.83300 1.000 44.68000  ? 436  PHE A CA  1 
ATOM   3213  C C   . PHE A 1 417 ? 28.05900  -17.02100 -13.61100 1.000 44.50000  ? 436  PHE A C   1 
ATOM   3214  O O   . PHE A 1 417 ? 28.51600  -17.78100 -14.46800 1.000 46.32000  ? 436  PHE A O   1 
ATOM   3215  C CB  . PHE A 1 417 ? 27.26800  -17.82400 -11.43000 1.000 43.98000  ? 436  PHE A CB  1 
ATOM   3216  C CG  . PHE A 1 417 ? 26.20900  -18.44200 -10.56000 1.000 40.39000  ? 436  PHE A CG  1 
ATOM   3217  C CD1 . PHE A 1 417 ? 25.40200  -19.48000 -10.99900 1.000 46.02000  ? 436  PHE A CD1 1 
ATOM   3218  C CD2 . PHE A 1 417 ? 25.87400  -17.81500 -9.37300  1.000 45.00000  ? 436  PHE A CD2 1 
ATOM   3219  C CE1 . PHE A 1 417 ? 24.40900  -20.00500 -10.18200 1.000 47.45000  ? 436  PHE A CE1 1 
ATOM   3220  C CE2 . PHE A 1 417 ? 24.86100  -18.30200 -8.57000  1.000 46.32000  ? 436  PHE A CE2 1 
ATOM   3221  C CZ  . PHE A 1 417 ? 24.12500  -19.40300 -8.97700  1.000 41.77000  ? 436  PHE A CZ  1 
ATOM   3222  N N   . ILE A 1 418 ? 28.62500  -15.86300 -13.27900 1.000 47.68000  ? 437  ILE A N   1 
ATOM   3223  C CA  . ILE A 1 418 ? 29.93400  -15.43200 -13.76500 1.000 46.09000  ? 437  ILE A CA  1 
ATOM   3224  C C   . ILE A 1 418 ? 30.95900  -15.54700 -12.63800 1.000 48.39000  ? 437  ILE A C   1 
ATOM   3225  O O   . ILE A 1 418 ? 30.66600  -15.23500 -11.47300 1.000 49.50000  ? 437  ILE A O   1 
ATOM   3226  C CB  . ILE A 1 418 ? 29.86800  -13.99500 -14.32700 1.000 44.76000  ? 437  ILE A CB  1 
ATOM   3227  C CG1 . ILE A 1 418 ? 31.17000  -13.63300 -15.03000 1.000 45.57000  ? 437  ILE A CG1 1 
ATOM   3228  C CG2 . ILE A 1 418 ? 29.54500  -12.97300 -13.24000 1.000 46.58000  ? 437  ILE A CG2 1 
ATOM   3229  C CD1 . ILE A 1 418 ? 31.11500  -12.33400 -15.79200 1.000 41.35000  ? 437  ILE A CD1 1 
ATOM   3230  N N   . ARG A 1 419 ? 32.15800  -15.98100 -12.99400 1.000 48.74000  ? 438  ARG A N   1 
ATOM   3231  C CA  . ARG A 1 419 ? 33.24200  -16.04900 -11.99400 1.000 52.15000  ? 438  ARG A CA  1 
ATOM   3232  C C   . ARG A 1 419 ? 33.65900  -14.61100 -11.71800 1.000 50.09000  ? 438  ARG A C   1 
ATOM   3233  O O   . ARG A 1 419 ? 33.88400  -13.88400 -12.66400 1.000 56.98000  ? 438  ARG A O   1 
ATOM   3234  C CB  . ARG A 1 419 ? 34.41300  -16.86000 -12.54500 1.000 50.52000  ? 438  ARG A CB  1 
ATOM   3235  C CG  . ARG A 1 419 ? 35.67000  -16.75900 -11.70400 1.000 57.00000  ? 438  ARG A CG  1 
ATOM   3236  C CD  . ARG A 1 419 ? 36.10100  -18.10100 -11.16200 1.000 65.01000  ? 438  ARG A CD  1 
ATOM   3237  N NE  . ARG A 1 419 ? 37.36200  -17.95900 -10.46400 1.000 66.87000  ? 438  ARG A NE  1 
ATOM   3238  C CZ  . ARG A 1 419 ? 38.28100  -18.89800 -10.38800 1.000 64.83000  ? 438  ARG A CZ  1 
ATOM   3239  N NH1 . ARG A 1 419 ? 38.08100  -20.06800 -10.94600 1.000 58.66000  ? 438  ARG A NH1 1 
ATOM   3240  N NH2 . ARG A 1 419 ? 39.40300  -18.66900 -9.74100  1.000 68.55000  ? 438  ARG A NH2 1 
ATOM   3241  N N   . THR A 1 420 ? 33.67900  -14.20700 -10.46100 1.000 50.12000  ? 439  THR A N   1 
ATOM   3242  C CA  . THR A 1 420 ? 34.06100  -12.83700 -10.13800 1.000 54.85000  ? 439  THR A CA  1 
ATOM   3243  C C   . THR A 1 420 ? 35.55300  -12.66600 -9.88900  1.000 56.51000  ? 439  THR A C   1 
ATOM   3244  O O   . THR A 1 420 ? 36.04200  -11.53300 -9.93600  1.000 61.23000  ? 439  THR A O   1 
ATOM   3245  C CB  . THR A 1 420 ? 33.29900  -12.32500 -8.91900  1.000 54.36000  ? 439  THR A CB  1 
ATOM   3246  O OG1 . THR A 1 420 ? 33.57100  -13.16800 -7.78900  1.000 60.30000  ? 439  THR A OG1 1 
ATOM   3247  C CG2 . THR A 1 420 ? 31.81100  -12.29700 -9.19100  1.000 49.55000  ? 439  THR A CG2 1 
ATOM   3248  N N   . ASN A 1 421 ? 36.29800  -13.75000 -9.65000  1.000 57.52000  ? 440  ASN A N   1 
ATOM   3249  C CA  . ASN A 1 421 ? 37.72000  -13.65200 -9.30300  1.000 53.81000  ? 440  ASN A CA  1 
ATOM   3250  C C   . ASN A 1 421 ? 38.58700  -14.51800 -10.21300 1.000 59.94000  ? 440  ASN A C   1 
ATOM   3251  O O   . ASN A 1 421 ? 39.40700  -15.30500 -9.73700  1.000 62.61000  ? 440  ASN A O   1 
ATOM   3252  C CB  . ASN A 1 421 ? 37.93400  -14.04600 -7.84400  1.000 61.43000  ? 440  ASN A CB  1 
ATOM   3253  C CG  . ASN A 1 421 ? 37.51700  -15.48900 -7.55700  1.000 66.47000  ? 440  ASN A CG  1 
ATOM   3254  O OD1 . ASN A 1 421 ? 37.03300  -16.20600 -8.44100  1.000 60.51000  ? 440  ASN A OD1 1 
ATOM   3255  N ND2 . ASN A 1 421 ? 37.74600  -15.92900 -6.32800  1.000 68.43000  ? 440  ASN A ND2 1 
ATOM   3256  N N   . PRO A 1 422 ? 38.44000  -14.39800 -11.53500 1.000 57.39000  ? 441  PRO A N   1 
ATOM   3257  C CA  . PRO A 1 422 ? 39.15200  -15.33600 -12.42700 1.000 61.31000  ? 441  PRO A CA  1 
ATOM   3258  C C   . PRO A 1 422 ? 40.68100  -15.20300 -12.40300 1.000 68.65000  ? 441  PRO A C   1 
ATOM   3259  O O   . PRO A 1 422 ? 41.35700  -16.14600 -12.83600 1.000 66.73000  ? 441  PRO A O   1 
ATOM   3260  C CB  . PRO A 1 422 ? 38.57700  -15.00300 -13.81300 1.000 53.49000  ? 441  PRO A CB  1 
ATOM   3261  C CG  . PRO A 1 422 ? 38.14900  -13.60200 -13.70600 1.000 52.71000  ? 441  PRO A CG  1 
ATOM   3262  C CD  . PRO A 1 422 ? 37.67900  -13.39500 -12.30200 1.000 51.37000  ? 441  PRO A CD  1 
ATOM   3263  N N   . GLU A 1 423 ? 41.23500  -14.07600 -11.95200 1.000 71.34000  ? 442  GLU A N   1 
ATOM   3264  C CA  . GLU A 1 423 ? 42.68300  -13.94200 -11.96500 1.000 74.39000  ? 442  GLU A CA  1 
ATOM   3265  C C   . GLU A 1 423 ? 43.35300  -14.59600 -10.76500 1.000 73.92000  ? 442  GLU A C   1 
ATOM   3266  O O   . GLU A 1 423 ? 44.56100  -14.86900 -10.80700 1.000 81.00000  ? 442  GLU A O   1 
ATOM   3267  C CB  . GLU A 1 423 ? 43.10400  -12.46700 -12.04000 1.000 75.26000  ? 442  GLU A CB  1 
ATOM   3268  C CG  . GLU A 1 423 ? 42.77300  -11.80000 -13.37700 1.000 89.03000  ? 442  GLU A CG  1 
ATOM   3269  C CD  . GLU A 1 423 ? 43.33500  -10.38400 -13.49100 1.000 99.04000  ? 442  GLU A CD  1 
ATOM   3270  O OE1 . GLU A 1 423 ? 43.93300  -9.89100  -12.51200 1.000 96.96000  ? 442  GLU A OE1 1 
ATOM   3271  O OE2 . GLU A 1 423 ? 43.16400  -9.76600  -14.56300 1.000 103.29000 ? 442  GLU A OE2 1 
ATOM   3272  N N   . GLN A 1 424 ? 42.58800  -14.87100 -9.70300  1.000 68.73000  ? 443  GLN A N   1 
ATOM   3273  C CA  . GLN A 1 424 ? 43.11300  -15.44900 -8.46400  1.000 71.77000  ? 443  GLN A CA  1 
ATOM   3274  C C   . GLN A 1 424 ? 43.02000  -16.96500 -8.55800  1.000 74.71000  ? 443  GLN A C   1 
ATOM   3275  O O   . GLN A 1 424 ? 42.05000  -17.58200 -8.10400  1.000 74.06000  ? 443  GLN A O   1 
ATOM   3276  C CB  . GLN A 1 424 ? 42.32000  -14.91800 -7.26400  1.000 69.00000  ? 443  GLN A CB  1 
ATOM   3277  C CG  . GLN A 1 424 ? 42.41400  -13.41900 -7.07000  1.000 76.57000  ? 443  GLN A CG  1 
ATOM   3278  C CD  . GLN A 1 424 ? 41.54800  -12.97100 -5.92400  1.000 86.54000  ? 443  GLN A CD  1 
ATOM   3279  O OE1 . GLN A 1 424 ? 40.85700  -13.78400 -5.31600  1.000 83.28000  ? 443  GLN A OE1 1 
ATOM   3280  N NE2 . GLN A 1 424 ? 41.58300  -11.67600 -5.61000  1.000 87.07000  ? 443  GLN A NE2 1 
ATOM   3281  N N   . LEU A 1 425 ? 44.05500  -17.58200 -9.13500  1.000 80.66000  ? 444  LEU A N   1 
ATOM   3282  C CA  . LEU A 1 425 ? 44.02800  -19.01200 -9.39700  1.000 78.38000  ? 444  LEU A CA  1 
ATOM   3283  C C   . LEU A 1 425 ? 44.22500  -19.81200 -8.12300  1.000 79.16000  ? 444  LEU A C   1 
ATOM   3284  O O   . LEU A 1 425 ? 43.89200  -21.01100 -8.07700  1.000 75.68000  ? 444  LEU A O   1 
ATOM   3285  C CB  . LEU A 1 425 ? 45.17300  -19.39800 -10.33100 1.000 87.88000  ? 444  LEU A CB  1 
ATOM   3286  C CG  . LEU A 1 425 ? 45.72400  -18.40200 -11.34600 1.000 83.71000  ? 444  LEU A CG  1 
ATOM   3287  C CD1 . LEU A 1 425 ? 46.86000  -19.09300 -12.09500 1.000 66.77000  ? 444  LEU A CD1 1 
ATOM   3288  C CD2 . LEU A 1 425 ? 44.72100  -17.71600 -12.30200 1.000 80.54000  ? 444  LEU A CD2 1 
ATOM   3289  N N   . TRP A 1 426 ? 44.84500  -19.18800 -7.12800  1.000 86.99000  ? 445  TRP A N   1 
ATOM   3290  C CA  . TRP A 1 426 ? 45.19700  -19.82400 -5.86800  1.000 90.86000  ? 445  TRP A CA  1 
ATOM   3291  C C   . TRP A 1 426 ? 44.16100  -19.47400 -4.81600  1.000 91.54000  ? 445  TRP A C   1 
ATOM   3292  O O   . TRP A 1 426 ? 44.48500  -18.95600 -3.74300  1.000 94.74000  ? 445  TRP A O   1 
ATOM   3293  C CB  . TRP A 1 426 ? 46.57600  -19.33900 -5.44900  1.000 91.44000  ? 445  TRP A CB  1 
ATOM   3294  C CG  . TRP A 1 426 ? 47.64800  -19.45700 -6.51500  1.000 99.26000  ? 445  TRP A CG  1 
ATOM   3295  C CD1 . TRP A 1 426 ? 47.60400  -20.20300 -7.66700  1.000 98.88000  ? 445  TRP A CD1 1 
ATOM   3296  C CD2 . TRP A 1 426 ? 48.87200  -18.70900 -6.57700  1.000 120.92000 ? 445  TRP A CD2 1 
ATOM   3297  N NE1 . TRP A 1 426 ? 48.75000  -20.00400 -8.40700  1.000 105.32000 ? 445  TRP A NE1 1 
ATOM   3298  C CE2 . TRP A 1 426 ? 49.54000  -19.08800 -7.76100  1.000 121.96000 ? 445  TRP A CE2 1 
ATOM   3299  C CE3 . TRP A 1 426 ? 49.47800  -17.77600 -5.73000  1.000 121.96000 ? 445  TRP A CE3 1 
ATOM   3300  C CZ2 . TRP A 1 426 ? 50.78600  -18.56300 -8.11700  1.000 129.96000 ? 445  TRP A CZ2 1 
ATOM   3301  C CZ3 . TRP A 1 426 ? 50.71200  -17.25600 -6.08500  1.000 123.41000 ? 445  TRP A CZ3 1 
ATOM   3302  C CH2 . TRP A 1 426 ? 51.35300  -17.65000 -7.26600  1.000 126.10000 ? 445  TRP A CH2 1 
ATOM   3303  N N   . ALA A 1 427 ? 42.88900  -19.71600 -5.12700  1.000 89.43000  ? 446  ALA A N   1 
ATOM   3304  C CA  . ALA A 1 427 ? 41.81000  -19.31900 -4.23500  1.000 84.96000  ? 446  ALA A CA  1 
ATOM   3305  C C   . ALA A 1 427 ? 40.52800  -20.03000 -4.64600  1.000 75.43000  ? 446  ALA A C   1 
ATOM   3306  O O   . ALA A 1 427 ? 40.42200  -20.58900 -5.74200  1.000 69.63000  ? 446  ALA A O   1 
ATOM   3307  C CB  . ALA A 1 427 ? 41.61000  -17.79700 -4.22600  1.000 81.56000  ? 446  ALA A CB  1 
ATOM   3308  N N   . ILE A 1 428 ? 39.54600  -19.97100 -3.75300  1.000 82.11000  ? 447  ILE A N   1 
ATOM   3309  C CA  . ILE A 1 428 ? 38.22300  -20.56100 -3.97200  1.000 81.25000  ? 447  ILE A CA  1 
ATOM   3310  C C   . ILE A 1 428 ? 37.45300  -19.72900 -4.99300  1.000 70.95000  ? 447  ILE A C   1 
ATOM   3311  O O   . ILE A 1 428 ? 37.34900  -18.49600 -4.83400  1.000 73.81000  ? 447  ILE A O   1 
ATOM   3312  C CB  . ILE A 1 428 ? 37.46300  -20.65400 -2.64400  1.000 82.71000  ? 447  ILE A CB  1 
ATOM   3313  C CG1 . ILE A 1 428 ? 37.53300  -19.31500 -1.89800  1.000 80.84000  ? 447  ILE A CG1 1 
ATOM   3314  C CG2 . ILE A 1 428 ? 37.98800  -21.81400 -1.80400  1.000 85.32000  ? 447  ILE A CG2 1 
ATOM   3315  C CD1 . ILE A 1 428 ? 36.72300  -19.25500 -0.62700  1.000 78.33000  ? 447  ILE A CD1 1 
ATOM   3316  N N   . PRO A 1 429 ? 36.91300  -20.33800 -6.05200  1.000 67.77000  ? 448  PRO A N   1 
ATOM   3317  C CA  . PRO A 1 429 ? 36.13000  -19.56900 -7.02800  1.000 69.34000  ? 448  PRO A CA  1 
ATOM   3318  C C   . PRO A 1 429 ? 34.94800  -18.87300 -6.37300  1.000 62.62000  ? 448  PRO A C   1 
ATOM   3319  O O   . PRO A 1 429 ? 34.25600  -19.44400 -5.53200  1.000 62.07000  ? 448  PRO A O   1 
ATOM   3320  C CB  . PRO A 1 429 ? 35.66200  -20.63300 -8.02800  1.000 68.33000  ? 448  PRO A CB  1 
ATOM   3321  C CG  . PRO A 1 429 ? 36.65200  -21.73800 -7.89800  1.000 72.74000  ? 448  PRO A CG  1 
ATOM   3322  C CD  . PRO A 1 429 ? 37.03600  -21.75000 -6.43900  1.000 73.43000  ? 448  PRO A CD  1 
ATOM   3323  N N   . LYS A 1 430 ? 34.71900  -17.62800 -6.77000  1.000 63.10000  ? 449  LYS A N   1 
ATOM   3324  C CA  . LYS A 1 430 ? 33.55500  -16.87500 -6.33500  1.000 57.56000  ? 449  LYS A CA  1 
ATOM   3325  C C   . LYS A 1 430 ? 32.71200  -16.55300 -7.56100  1.000 53.11000  ? 449  LYS A C   1 
ATOM   3326  O O   . LYS A 1 430 ? 33.25100  -16.24000 -8.62700  1.000 52.88000  ? 449  LYS A O   1 
ATOM   3327  C CB  . LYS A 1 430 ? 33.97400  -15.60200 -5.59500  1.000 58.90000  ? 449  LYS A CB  1 
ATOM   3328  C CG  . LYS A 1 430 ? 34.83000  -15.89700 -4.36100  1.000 60.23000  ? 449  LYS A CG  1 
ATOM   3329  C CD  . LYS A 1 430 ? 35.23400  -14.64600 -3.58700  1.000 60.73000  ? 449  LYS A CD  1 
ATOM   3330  C CE  . LYS A 1 430 ? 34.07000  -14.11600 -2.76600  1.000 60.65000  ? 449  LYS A CE  1 
ATOM   3331  N NZ  . LYS A 1 430 ? 34.45500  -13.00800 -1.85000  1.000 64.97000  ? 449  LYS A NZ  1 
ATOM   3332  N N   . TYR A 1 431 ? 31.39100  -16.66100 -7.42400  1.000 56.15000  ? 450  TYR A N   1 
ATOM   3333  C CA  . TYR A 1 431 ? 30.48800  -16.50300 -8.55500  1.000 53.30000  ? 450  TYR A CA  1 
ATOM   3334  C C   . TYR A 1 431 ? 29.35300  -15.55700 -8.18700  1.000 50.62000  ? 450  TYR A C   1 
ATOM   3335  O O   . TYR A 1 431 ? 29.00600  -15.39000 -7.01500  1.000 48.95000  ? 450  TYR A O   1 
ATOM   3336  C CB  . TYR A 1 431 ? 29.90000  -17.84900 -9.00300  1.000 46.39000  ? 450  TYR A CB  1 
ATOM   3337  C CG  . TYR A 1 431 ? 30.88900  -18.86900 -9.54600  1.000 49.06000  ? 450  TYR A CG  1 
ATOM   3338  C CD1 . TYR A 1 431 ? 31.30100  -18.84200 -10.87800 1.000 52.65000  ? 450  TYR A CD1 1 
ATOM   3339  C CD2 . TYR A 1 431 ? 31.38600  -19.88100 -8.72900  1.000 49.05000  ? 450  TYR A CD2 1 
ATOM   3340  C CE1 . TYR A 1 431 ? 32.18900  -19.79300 -11.37700 1.000 48.03000  ? 450  TYR A CE1 1 
ATOM   3341  C CE2 . TYR A 1 431 ? 32.26600  -20.82700 -9.21300  1.000 49.42000  ? 450  TYR A CE2 1 
ATOM   3342  C CZ  . TYR A 1 431 ? 32.66500  -20.78100 -10.53800 1.000 54.15000  ? 450  TYR A CZ  1 
ATOM   3343  O OH  . TYR A 1 431 ? 33.54300  -21.72700 -11.01500 1.000 52.88000  ? 450  TYR A OH  1 
ATOM   3344  N N   . GLN A 1 432 ? 28.77500  -14.93800 -9.21400  1.000 52.41000  ? 451  GLN A N   1 
ATOM   3345  C CA  . GLN A 1 432 ? 27.61900  -14.06500 -9.05100  1.000 51.25000  ? 451  GLN A CA  1 
ATOM   3346  C C   . GLN A 1 432 ? 26.59700  -14.37700 -10.14700 1.000 52.44000  ? 451  GLN A C   1 
ATOM   3347  O O   . GLN A 1 432 ? 26.97300  -14.52900 -11.31300 1.000 47.97000  ? 451  GLN A O   1 
ATOM   3348  C CB  . GLN A 1 432 ? 28.02100  -12.59200 -9.10600  1.000 50.18000  ? 451  GLN A CB  1 
ATOM   3349  C CG  . GLN A 1 432 ? 26.86200  -11.63200 -8.92400  1.000 55.99000  ? 451  GLN A CG  1 
ATOM   3350  C CD  . GLN A 1 432 ? 27.31300  -10.18800 -8.90500  1.000 64.14000  ? 451  GLN A CD  1 
ATOM   3351  O OE1 . GLN A 1 432 ? 28.50400  -9.89600  -9.02900  1.000 65.87000  ? 451  GLN A OE1 1 
ATOM   3352  N NE2 . GLN A 1 432 ? 26.36100  -9.27300  -8.76000  1.000 63.57000  ? 451  GLN A NE2 1 
ATOM   3353  N N   . GLN A 1 433 ? 25.31900  -14.46300 -9.77400  1.000 48.88000  ? 452  GLN A N   1 
ATOM   3354  C CA  . GLN A 1 433 ? 24.27300  -14.86100 -10.68700 1.000 49.12000  ? 452  GLN A CA  1 
ATOM   3355  C C   . GLN A 1 433 ? 24.04200  -13.80400 -11.74400 1.000 50.18000  ? 452  GLN A C   1 
ATOM   3356  O O   . GLN A 1 433 ? 24.19100  -12.60700 -11.51300 1.000 48.33000  ? 452  GLN A O   1 
ATOM   3357  C CB  . GLN A 1 433 ? 22.96900  -15.15300 -9.94200  1.000 46.49000  ? 452  GLN A CB  1 
ATOM   3358  C CG  . GLN A 1 433 ? 21.92000  -15.77100 -10.83800 1.000 45.10000  ? 452  GLN A CG  1 
ATOM   3359  C CD  . GLN A 1 433 ? 20.64100  -16.10400 -10.11400 1.000 49.14000  ? 452  GLN A CD  1 
ATOM   3360  O OE1 . GLN A 1 433 ? 20.48100  -15.79400 -8.92900  1.000 44.48000  ? 452  GLN A OE1 1 
ATOM   3361  N NE2 . GLN A 1 433 ? 19.72600  -16.76100 -10.81200 1.000 49.02000  ? 452  GLN A NE2 1 
ATOM   3362  N N   . ILE A 1 434 ? 23.65700  -14.24400 -12.93900 1.000 46.37000  ? 453  ILE A N   1 
ATOM   3363  C CA  . ILE A 1 434 ? 23.44200  -13.34100 -14.09100 1.000 40.84000  ? 453  ILE A CA  1 
ATOM   3364  C C   . ILE A 1 434 ? 22.08400  -13.58900 -14.73500 1.000 42.32000  ? 453  ILE A C   1 
ATOM   3365  O O   . ILE A 1 434 ? 21.61200  -14.72600 -14.77200 1.000 39.80000  ? 453  ILE A O   1 
ATOM   3366  C CB  . ILE A 1 434 ? 24.58100  -13.49600 -15.13600 1.000 42.93000  ? 453  ILE A CB  1 
ATOM   3367  C CG1 . ILE A 1 434 ? 24.76100  -14.96400 -15.55900 1.000 45.39000  ? 453  ILE A CG1 1 
ATOM   3368  C CG2 . ILE A 1 434 ? 25.83600  -12.92800 -14.59100 1.000 36.11000  ? 453  ILE A CG2 1 
ATOM   3369  C CD1 . ILE A 1 434 ? 25.79000  -15.10200 -16.67800 1.000 42.44000  ? 453  ILE A CD1 1 
ATOM   3370  N N   . PRO A 1 435 ? 21.45000  -12.49200 -15.23000 1.000 49.14000  ? 454  PRO A N   1 
ATOM   3371  C CA  . PRO A 1 435 ? 20.08400  -12.56100 -15.72500 1.000 44.55000  ? 454  PRO A CA  1 
ATOM   3372  C C   . PRO A 1 435 ? 19.97000  -13.21900 -17.10900 1.000 47.80000  ? 454  PRO A C   1 
ATOM   3373  O O   . PRO A 1 435 ? 20.96600  -13.34400 -17.85000 1.000 41.85000  ? 454  PRO A O   1 
ATOM   3374  C CB  . PRO A 1 435 ? 19.62300  -11.11800 -15.77100 1.000 48.20000  ? 454  PRO A CB  1 
ATOM   3375  C CG  . PRO A 1 435 ? 20.89300  -10.31100 -15.76900 1.000 41.47000  ? 454  PRO A CG  1 
ATOM   3376  C CD  . PRO A 1 435 ? 21.86700  -11.13100 -14.99200 1.000 40.69000  ? 454  PRO A CD  1 
ATOM   3377  N N   . PHE A 1 436 ? 18.73000  -13.67200 -17.47600 1.000 50.85000  ? 455  PHE A N   1 
ATOM   3378  C CA  . PHE A 1 436 ? 18.29700  -14.64600 -18.48300 1.000 49.92000  ? 455  PHE A CA  1 
ATOM   3379  C C   . PHE A 1 436 ? 19.07600  -14.66300 -19.77900 1.000 63.13000  ? 455  PHE A C   1 
ATOM   3380  O O   . PHE A 1 436 ? 19.54300  -15.74200 -20.15500 1.000 78.29000  ? 455  PHE A O   1 
ATOM   3381  C CB  . PHE A 1 436 ? 16.80100  -14.49700 -18.84000 1.000 58.12000  ? 455  PHE A CB  1 
ATOM   3382  C CG  . PHE A 1 436 ? 16.44600  -15.08100 -20.23000 1.000 47.27000  ? 455  PHE A CG  1 
ATOM   3383  C CD1 . PHE A 1 436 ? 16.74800  -16.41100 -20.56800 1.000 43.23000  ? 455  PHE A CD1 1 
ATOM   3384  C CD2 . PHE A 1 436 ? 15.70500  -14.33600 -21.14200 1.000 50.55000  ? 455  PHE A CD2 1 
ATOM   3385  C CE1 . PHE A 1 436 ? 16.38900  -16.92400 -21.83200 1.000 52.71000  ? 455  PHE A CE1 1 
ATOM   3386  C CE2 . PHE A 1 436 ? 15.33000  -14.86000 -22.39200 1.000 50.48000  ? 455  PHE A CE2 1 
ATOM   3387  C CZ  . PHE A 1 436 ? 15.67100  -16.15200 -22.72800 1.000 49.49000  ? 455  PHE A CZ  1 
ATOM   3388  N N   . PRO A 1 437 ? 19.18900  -13.58800 -20.55100 1.000 53.92000  ? 456  PRO A N   1 
ATOM   3389  C CA  . PRO A 1 437 ? 19.94700  -13.77900 -21.81600 1.000 51.96000  ? 456  PRO A CA  1 
ATOM   3390  C C   . PRO A 1 437 ? 21.36000  -14.28700 -21.54100 1.000 50.02000  ? 456  PRO A C   1 
ATOM   3391  O O   . PRO A 1 437 ? 21.86100  -15.14900 -22.27500 1.000 52.97000  ? 456  PRO A O   1 
ATOM   3392  C CB  . PRO A 1 437 ? 19.90600  -12.39700 -22.47300 1.000 56.54000  ? 456  PRO A CB  1 
ATOM   3393  C CG  . PRO A 1 437 ? 18.71500  -11.73500 -21.83700 1.000 56.69000  ? 456  PRO A CG  1 
ATOM   3394  C CD  . PRO A 1 437 ? 18.66600  -12.20200 -20.42700 1.000 52.92000  ? 456  PRO A CD  1 
ATOM   3395  N N   . TYR A 1 438 ? 21.97700  -13.83500 -20.45200 1.000 44.15000  ? 457  TYR A N   1 
ATOM   3396  C CA  . TYR A 1 438 ? 23.23200  -14.26600 -19.84600 1.000 46.37000  ? 457  TYR A CA  1 
ATOM   3397  C C   . TYR A 1 438 ? 24.47600  -13.82800 -20.59600 1.000 48.05000  ? 457  TYR A C   1 
ATOM   3398  O O   . TYR A 1 438 ? 25.59700  -14.06200 -20.09700 1.000 52.40000  ? 457  TYR A O   1 
ATOM   3399  C CB  . TYR A 1 438 ? 23.36100  -15.78700 -19.67700 1.000 40.54000  ? 457  TYR A CB  1 
ATOM   3400  C CG  . TYR A 1 438 ? 22.15500  -16.51400 -19.14700 1.000 51.15000  ? 457  TYR A CG  1 
ATOM   3401  C CD1 . TYR A 1 438 ? 21.62300  -16.22500 -17.90100 1.000 50.28000  ? 457  TYR A CD1 1 
ATOM   3402  C CD2 . TYR A 1 438 ? 21.61100  -17.56400 -19.87300 1.000 49.88000  ? 457  TYR A CD2 1 
ATOM   3403  C CE1 . TYR A 1 438 ? 20.51500  -16.91800 -17.42000 1.000 45.13000  ? 457  TYR A CE1 1 
ATOM   3404  C CE2 . TYR A 1 438 ? 20.51800  -18.26800 -19.39500 1.000 46.09000  ? 457  TYR A CE2 1 
ATOM   3405  C CZ  . TYR A 1 438 ? 19.97000  -17.94400 -18.18100 1.000 48.82000  ? 457  TYR A CZ  1 
ATOM   3406  O OH  . TYR A 1 438 ? 18.88200  -18.66500 -17.73800 1.000 46.54000  ? 457  TYR A OH  1 
ATOM   3407  N N   . PHE A 1 439 ? 24.35600  -13.23300 -21.77400 1.000 44.35000  ? 458  PHE A N   1 
ATOM   3408  C CA  . PHE A 1 439 ? 25.51800  -13.04500 -22.64300 1.000 41.72000  ? 458  PHE A CA  1 
ATOM   3409  C C   . PHE A 1 439 ? 26.55200  -12.15900 -21.96600 1.000 46.12000  ? 458  PHE A C   1 
ATOM   3410  O O   . PHE A 1 439 ? 26.24400  -11.03500 -21.53500 1.000 47.30000  ? 458  PHE A O   1 
ATOM   3411  C CB  . PHE A 1 439 ? 25.10900  -12.41500 -23.95900 1.000 49.70000  ? 458  PHE A CB  1 
ATOM   3412  C CG  . PHE A 1 439 ? 24.11500  -13.21100 -24.74800 1.000 46.30000  ? 458  PHE A CG  1 
ATOM   3413  C CD1 . PHE A 1 439 ? 24.43200  -14.46900 -25.21700 1.000 44.63000  ? 458  PHE A CD1 1 
ATOM   3414  C CD2 . PHE A 1 439 ? 22.91900  -12.63300 -25.14200 1.000 46.14000  ? 458  PHE A CD2 1 
ATOM   3415  C CE1 . PHE A 1 439 ? 23.52300  -15.18400 -25.98800 1.000 44.64000  ? 458  PHE A CE1 1 
ATOM   3416  C CE2 . PHE A 1 439 ? 22.02000  -13.33400 -25.92600 1.000 52.30000  ? 458  PHE A CE2 1 
ATOM   3417  C CZ  . PHE A 1 439 ? 22.32300  -14.60900 -26.34600 1.000 47.72000  ? 458  PHE A CZ  1 
ATOM   3418  N N   . GLN A 1 440 ? 27.77400  -12.66200 -21.86400 1.000 44.43000  ? 459  GLN A N   1 
ATOM   3419  C CA  . GLN A 1 440 ? 28.90000  -11.91600 -21.32100 1.000 43.61000  ? 459  GLN A CA  1 
ATOM   3420  C C   . GLN A 1 440 ? 30.01300  -11.87100 -22.36300 1.000 41.28000  ? 459  GLN A C   1 
ATOM   3421  O O   . GLN A 1 440 ? 29.99400  -12.61100 -23.35100 1.000 44.35000  ? 459  GLN A O   1 
ATOM   3422  C CB  . GLN A 1 440 ? 29.40200  -12.56900 -20.03200 1.000 43.51000  ? 459  GLN A CB  1 
ATOM   3423  C CG  . GLN A 1 440 ? 28.32500  -12.80500 -18.99300 1.000 46.71000  ? 459  GLN A CG  1 
ATOM   3424  C CD  . GLN A 1 440 ? 27.74300  -11.52600 -18.43000 1.000 53.37000  ? 459  GLN A CD  1 
ATOM   3425  O OE1 . GLN A 1 440 ? 28.46800  -10.56500 -18.17100 1.000 49.87000  ? 459  GLN A OE1 1 
ATOM   3426  N NE2 . GLN A 1 440 ? 26.42000  -11.50300 -18.24800 1.000 45.97000  ? 459  GLN A NE2 1 
ATOM   3427  N N   . ARG A 1 441 ? 31.00300  -11.01400 -22.13900 1.000 51.40000  ? 460  ARG A N   1 
ATOM   3428  C CA  . ARG A 1 441 ? 32.15600  -11.01700 -23.03000 1.000 54.80000  ? 460  ARG A CA  1 
ATOM   3429  C C   . ARG A 1 441 ? 32.87800  -12.35700 -22.98900 1.000 53.75000  ? 460  ARG A C   1 
ATOM   3430  O O   . ARG A 1 441 ? 32.82100  -13.08400 -21.99700 1.000 52.94000  ? 460  ARG A O   1 
ATOM   3431  C CB  . ARG A 1 441 ? 33.11300  -9.87900  -22.68800 1.000 46.86000  ? 460  ARG A CB  1 
ATOM   3432  C CG  . ARG A 1 441 ? 32.54300  -8.58400  -23.16900 1.000 58.29000  ? 460  ARG A CG  1 
ATOM   3433  C CD  . ARG A 1 441 ? 33.52500  -7.44500  -23.14000 1.000 59.65000  ? 460  ARG A CD  1 
ATOM   3434  N NE  . ARG A 1 441 ? 32.94700  -6.27800  -23.79900 1.000 60.93000  ? 460  ARG A NE  1 
ATOM   3435  C CZ  . ARG A 1 441 ? 32.97600  -6.08100  -25.11100 1.000 63.10000  ? 460  ARG A CZ  1 
ATOM   3436  N NH1 . ARG A 1 441 ? 33.49200  -6.98200  -25.93500 1.000 62.52000  ? 460  ARG A NH1 1 
ATOM   3437  N NH2 . ARG A 1 441 ? 32.44000  -4.97400  -25.61200 1.000 59.01000  ? 460  ARG A NH2 1 
ATOM   3438  N N   . LYS A 1 442 ? 33.53900  -12.68900 -24.10300 1.000 56.46000  ? 461  LYS A N   1 
ATOM   3439  C CA  . LYS A 1 442 ? 34.08700  -14.03000 -24.28600 1.000 56.54000  ? 461  LYS A CA  1 
ATOM   3440  C C   . LYS A 1 442 ? 35.07900  -14.40500 -23.19000 1.000 52.91000  ? 461  LYS A C   1 
ATOM   3441  O O   . LYS A 1 442 ? 35.16200  -15.57800 -22.80800 1.000 55.16000  ? 461  LYS A O   1 
ATOM   3442  C CB  . LYS A 1 442 ? 34.74800  -14.15600 -25.65600 1.000 59.16000  ? 461  LYS A CB  1 
ATOM   3443  C CG  . LYS A 1 442 ? 33.77300  -14.05100 -26.83700 1.000 77.98000  ? 461  LYS A CG  1 
ATOM   3444  C CD  . LYS A 1 442 ? 32.88700  -15.30100 -27.01600 1.000 87.57000  ? 461  LYS A CD  1 
ATOM   3445  C CE  . LYS A 1 442 ? 31.50000  -15.13900 -26.39900 1.000 70.63000  ? 461  LYS A CE  1 
ATOM   3446  N NZ  . LYS A 1 442 ? 30.61000  -16.27500 -26.75900 1.000 81.14000  ? 461  LYS A NZ  1 
ATOM   3447  N N   . ASP A 1 443 ? 35.81900  -13.43600 -22.63700 1.000 52.20000  ? 462  ASP A N   1 
ATOM   3448  C CA  . ASP A 1 443 ? 36.75600  -13.80200 -21.57600 1.000 51.60000  ? 462  ASP A CA  1 
ATOM   3449  C C   . ASP A 1 443 ? 36.06800  -14.23600 -20.27800 1.000 57.40000  ? 462  ASP A C   1 
ATOM   3450  O O   . ASP A 1 443 ? 36.73800  -14.79600 -19.40100 1.000 57.96000  ? 462  ASP A O   1 
ATOM   3451  C CB  . ASP A 1 443 ? 37.72000  -12.66200 -21.18300 1.000 57.91000  ? 462  ASP A CB  1 
ATOM   3452  C CG  . ASP A 1 443 ? 37.00400  -11.39500 -20.74800 1.000 68.94000  ? 462  ASP A CG  1 
ATOM   3453  O OD1 . ASP A 1 443 ? 36.10300  -10.91300 -21.48800 1.000 69.68000  ? 462  ASP A OD1 1 
ATOM   3454  O OD2 . ASP A 1 443 ? 37.21300  -11.00300 -19.57500 1.000 77.64000  ? 462  ASP A OD2 1 
ATOM   3455  N N   . ALA A 1 444 ? 34.76800  -13.97000 -20.11000 1.000 53.51000  ? 463  ALA A N   1 
ATOM   3456  C CA  . ALA A 1 444 ? 34.10100  -14.33500 -18.86700 1.000 51.92000  ? 463  ALA A CA  1 
ATOM   3457  C C   . ALA A 1 444 ? 34.00700  -15.85300 -18.72900 1.000 46.24000  ? 463  ALA A C   1 
ATOM   3458  O O   . ALA A 1 444 ? 33.77200  -16.57900 -19.70300 1.000 47.88000  ? 463  ALA A O   1 
ATOM   3459  C CB  . ALA A 1 444 ? 32.71900  -13.70000 -18.80700 1.000 46.15000  ? 463  ALA A CB  1 
ATOM   3460  N N   . ILE A 1 445 ? 34.17400  -16.33200 -17.50500 1.000 42.08000  ? 464  ILE A N   1 
ATOM   3461  C CA  . ILE A 1 445 ? 33.97600  -17.74400 -17.20200 1.000 47.29000  ? 464  ILE A CA  1 
ATOM   3462  C C   . ILE A 1 445 ? 32.55800  -17.93700 -16.68600 1.000 51.98000  ? 464  ILE A C   1 
ATOM   3463  O O   . ILE A 1 445 ? 32.17800  -17.34800 -15.66700 1.000 51.48000  ? 464  ILE A O   1 
ATOM   3464  C CB  . ILE A 1 445 ? 34.99700  -18.24900 -16.17700 1.000 49.14000  ? 464  ILE A CB  1 
ATOM   3465  C CG1 . ILE A 1 445 ? 36.40800  -18.20700 -16.77100 1.000 48.61000  ? 464  ILE A CG1 1 
ATOM   3466  C CG2 . ILE A 1 445 ? 34.62300  -19.65000 -15.72800 1.000 46.91000  ? 464  ILE A CG2 1 
ATOM   3467  C CD1 . ILE A 1 445 ? 37.48500  -18.44600 -15.76800 1.000 50.17000  ? 464  ILE A CD1 1 
ATOM   3468  N N   . ILE A 1 446 ? 31.78700  -18.78000 -17.37300 1.000 50.86000  ? 465  ILE A N   1 
ATOM   3469  C CA  . ILE A 1 446 ? 30.37500  -18.98800 -17.07700 1.000 42.83000  ? 465  ILE A CA  1 
ATOM   3470  C C   . ILE A 1 446 ? 30.19000  -20.35600 -16.43800 1.000 39.12000  ? 465  ILE A C   1 
ATOM   3471  O O   . ILE A 1 446 ? 30.64600  -21.36900 -16.97400 1.000 40.30000  ? 465  ILE A O   1 
ATOM   3472  C CB  . ILE A 1 446 ? 29.51100  -18.85600 -18.34100 1.000 44.31000  ? 465  ILE A CB  1 
ATOM   3473  C CG1 . ILE A 1 446 ? 29.70100  -17.46800 -18.95800 1.000 42.61000  ? 465  ILE A CG1 1 
ATOM   3474  C CG2 . ILE A 1 446 ? 28.05100  -19.12600 -18.01200 1.000 42.58000  ? 465  ILE A CG2 1 
ATOM   3475  C CD1 . ILE A 1 446 ? 29.33500  -16.33700 -18.01000 1.000 45.56000  ? 465  ILE A CD1 1 
ATOM   3476  N N   . GLU A 1 447 ? 29.48500  -20.37900 -15.31500 1.000 45.84000  ? 466  GLU A N   1 
ATOM   3477  C CA  . GLU A 1 447 ? 29.16300  -21.57400 -14.55300 1.000 44.57000  ? 466  GLU A CA  1 
ATOM   3478  C C   . GLU A 1 447 ? 27.64500  -21.66700 -14.42900 1.000 45.48000  ? 466  GLU A C   1 
ATOM   3479  O O   . GLU A 1 447 ? 26.97200  -20.65000 -14.23400 1.000 43.33000  ? 466  GLU A O   1 
ATOM   3480  C CB  . GLU A 1 447 ? 29.86200  -21.48400 -13.18500 1.000 42.32000  ? 466  GLU A CB  1 
ATOM   3481  C CG  . GLU A 1 447 ? 29.58400  -22.53000 -12.11500 1.000 50.77000  ? 466  GLU A CG  1 
ATOM   3482  C CD  . GLU A 1 447 ? 30.02100  -23.93300 -12.46800 1.000 57.15000  ? 466  GLU A CD  1 
ATOM   3483  O OE1 . GLU A 1 447 ? 30.72000  -24.11700 -13.49000 1.000 59.67000  ? 466  GLU A OE1 1 
ATOM   3484  O OE2 . GLU A 1 447 ? 29.73300  -24.84400 -11.65400 1.000 62.83000  ? 466  GLU A OE2 1 
ATOM   3485  N N   . THR A 1 448 ? 27.09600  -22.87000 -14.59900 1.000 41.28000  ? 467  THR A N   1 
ATOM   3486  C CA  . THR A 1 448 ? 25.66300  -23.09400 -14.46400 1.000 43.48000  ? 467  THR A CA  1 
ATOM   3487  C C   . THR A 1 448 ? 25.39600  -24.14900 -13.40000 1.000 46.72000  ? 467  THR A C   1 
ATOM   3488  O O   . THR A 1 448 ? 26.14300  -25.12500 -13.28000 1.000 48.46000  ? 467  THR A O   1 
ATOM   3489  C CB  . THR A 1 448 ? 25.00700  -23.53500 -15.78200 1.000 40.30000  ? 467  THR A CB  1 
ATOM   3490  O OG1 . THR A 1 448 ? 25.54400  -24.79300 -16.19900 1.000 42.49000  ? 467  THR A OG1 1 
ATOM   3491  C CG2 . THR A 1 448 ? 25.22800  -22.50300 -16.86800 1.000 49.71000  ? 467  THR A CG2 1 
ATOM   3492  N N   . LYS A 1 449 ? 24.32400  -23.94200 -12.63400 1.000 43.43000  ? 468  LYS A N   1 
ATOM   3493  C CA  . LYS A 1 449 ? 23.79900  -24.91700 -11.68500 1.000 43.83000  ? 468  LYS A CA  1 
ATOM   3494  C C   . LYS A 1 449 ? 22.34200  -25.21100 -12.02800 1.000 52.39000  ? 468  LYS A C   1 
ATOM   3495  O O   . LYS A 1 449 ? 21.60700  -24.32100 -12.47400 1.000 51.65000  ? 468  LYS A O   1 
ATOM   3496  C CB  . LYS A 1 449 ? 23.90500  -24.41700 -10.23800 1.000 47.53000  ? 468  LYS A CB  1 
ATOM   3497  C CG  . LYS A 1 449 ? 25.32300  -24.15200 -9.74800  1.000 49.08000  ? 468  LYS A CG  1 
ATOM   3498  C CD  . LYS A 1 449 ? 26.13000  -25.43700 -9.66200  1.000 56.96000  ? 468  LYS A CD  1 
ATOM   3499  C CE  . LYS A 1 449 ? 27.53200  -25.16600 -9.14500  1.000 52.31000  ? 468  LYS A CE  1 
ATOM   3500  N NZ  . LYS A 1 449 ? 28.40700  -26.36800 -9.20100  1.000 59.57000  ? 468  LYS A NZ  1 
ATOM   3501  N N   . THR A 1 450 ? 21.92600  -26.46400 -11.83400 1.000 48.96000  ? 469  THR A N   1 
ATOM   3502  C CA  . THR A 1 450 ? 20.57500  -26.90400 -12.16500 1.000 48.61000  ? 469  THR A CA  1 
ATOM   3503  C C   . THR A 1 450 ? 19.76200  -27.06000 -10.88900 1.000 45.10000  ? 469  THR A C   1 
ATOM   3504  O O   . THR A 1 450 ? 20.15900  -27.79700 -9.97500  1.000 47.19000  ? 469  THR A O   1 
ATOM   3505  C CB  . THR A 1 450 ? 20.60000  -28.20900 -12.96200 1.000 49.40000  ? 469  THR A CB  1 
ATOM   3506  O OG1 . THR A 1 450 ? 21.16300  -27.95800 -14.25800 1.000 54.24000  ? 469  THR A OG1 1 
ATOM   3507  C CG2 . THR A 1 450 ? 19.18900  -28.76800 -13.11300 1.000 43.47000  ? 469  THR A CG2 1 
ATOM   3508  N N   . LEU A 1 451 ? 18.61900  -26.38400 -10.83700 1.000 47.82000  ? 470  LEU A N   1 
ATOM   3509  C CA  . LEU A 1 451 ? 17.87400  -26.21500 -9.60700  1.000 42.28000  ? 470  LEU A CA  1 
ATOM   3510  C C   . LEU A 1 451 ? 16.58500  -27.02100 -9.71000  1.000 41.17000  ? 470  LEU A C   1 
ATOM   3511  O O   . LEU A 1 451 ? 15.73100  -26.72600 -10.56000 1.000 44.21000  ? 470  LEU A O   1 
ATOM   3512  C CB  . LEU A 1 451 ? 17.56300  -24.74500 -9.40300  1.000 41.85000  ? 470  LEU A CB  1 
ATOM   3513  C CG  . LEU A 1 451 ? 17.47200  -24.29100 -7.94900  1.000 50.40000  ? 470  LEU A CG  1 
ATOM   3514  C CD1 . LEU A 1 451 ? 18.92000  -24.15100 -7.48500  1.000 58.83000  ? 470  LEU A CD1 1 
ATOM   3515  C CD2 . LEU A 1 451 ? 16.68400  -23.00600 -7.79000  1.000 48.69000  ? 470  LEU A CD2 1 
ATOM   3516  N N   . HIS A 1 452 ? 16.42600  -28.01600 -8.85500  1.000 40.39000  ? 471  HIS A N   1 
ATOM   3517  C CA  . HIS A 1 452 ? 15.18600  -28.77300 -8.77100  1.000 40.84000  ? 471  HIS A CA  1 
ATOM   3518  C C   . HIS A 1 452 ? 14.43200  -28.24700 -7.55700  1.000 43.99000  ? 471  HIS A C   1 
ATOM   3519  O O   . HIS A 1 452 ? 14.89500  -28.40400 -6.42700  1.000 49.60000  ? 471  HIS A O   1 
ATOM   3520  C CB  . HIS A 1 452 ? 15.47600  -30.26500 -8.64800  1.000 41.95000  ? 471  HIS A CB  1 
ATOM   3521  C CG  . HIS A 1 452 ? 16.25500  -30.82800 -9.79600  1.000 42.80000  ? 471  HIS A CG  1 
ATOM   3522  N ND1 . HIS A 1 452 ? 15.69400  -31.07400 -11.03100 1.000 46.63000  ? 471  HIS A ND1 1 
ATOM   3523  C CD2 . HIS A 1 452 ? 17.55600  -31.18700 -9.89600  1.000 49.74000  ? 471  HIS A CD2 1 
ATOM   3524  C CE1 . HIS A 1 452 ? 16.61500  -31.56400 -11.84000 1.000 47.33000  ? 471  HIS A CE1 1 
ATOM   3525  N NE2 . HIS A 1 452 ? 17.75300  -31.64100 -11.17700 1.000 47.61000  ? 471  HIS A NE2 1 
ATOM   3526  N N   . THR A 1 453 ? 13.29100  -27.60500 -7.78600  1.000 38.60000  ? 472  THR A N   1 
ATOM   3527  C CA  . THR A 1 453 ? 12.51700  -26.99700 -6.71200  1.000 46.34000  ? 472  THR A CA  1 
ATOM   3528  C C   . THR A 1 453 ? 11.29800  -27.85100 -6.37700  1.000 51.77000  ? 472  THR A C   1 
ATOM   3529  O O   . THR A 1 453 ? 10.52900  -28.23100 -7.27000  1.000 42.48000  ? 472  THR A O   1 
ATOM   3530  C CB  . THR A 1 453 ? 12.07500  -25.58100 -7.08500  1.000 44.85000  ? 472  THR A CB  1 
ATOM   3531  O OG1 . THR A 1 453 ? 13.23600  -24.77700 -7.32200  1.000 46.77000  ? 472  THR A OG1 1 
ATOM   3532  C CG2 . THR A 1 453 ? 11.25600  -24.96200 -5.96100  1.000 35.91000  ? 472  THR A CG2 1 
ATOM   3533  N N   . LEU A 1 454 ? 11.11900  -28.12700 -5.08800  1.000 47.42000  ? 473  LEU A N   1 
ATOM   3534  C CA  . LEU A 1 454 ? 10.05100  -28.99500 -4.62300  1.000 42.02000  ? 473  LEU A CA  1 
ATOM   3535  C C   . LEU A 1 454 ? 8.75700   -28.22000 -4.41500  1.000 45.90000  ? 473  LEU A C   1 
ATOM   3536  O O   . LEU A 1 454 ? 8.75700   -27.09600 -3.89800  1.000 48.08000  ? 473  LEU A O   1 
ATOM   3537  C CB  . LEU A 1 454 ? 10.45900  -29.68900 -3.32400  1.000 51.26000  ? 473  LEU A CB  1 
ATOM   3538  C CG  . LEU A 1 454 ? 9.40700   -30.62100 -2.72400  1.000 48.45000  ? 473  LEU A CG  1 
ATOM   3539  C CD1 . LEU A 1 454 ? 9.05400   -31.72300 -3.71100  1.000 44.77000  ? 473  LEU A CD1 1 
ATOM   3540  C CD2 . LEU A 1 454 ? 9.91600   -31.20500 -1.42600  1.000 46.22000  ? 473  LEU A CD2 1 
ATOM   3541  N N   . HIS A 1 455 ? 7.65600   -28.84600 -4.82400  1.000 45.70000  ? 474  HIS A N   1 
ATOM   3542  C CA  . HIS A 1 455 ? 6.29700   -28.33800 -4.69700  1.000 43.19000  ? 474  HIS A CA  1 
ATOM   3543  C C   . HIS A 1 455 ? 5.50300   -29.27800 -3.80600  1.000 44.23000  ? 474  HIS A C   1 
ATOM   3544  O O   . HIS A 1 455 ? 5.62200   -30.50000 -3.92700  1.000 42.64000  ? 474  HIS A O   1 
ATOM   3545  C CB  . HIS A 1 455 ? 5.64400   -28.25900 -6.07000  1.000 45.02000  ? 474  HIS A CB  1 
ATOM   3546  C CG  . HIS A 1 455 ? 6.18600   -27.17100 -6.93100  1.000 50.17000  ? 474  HIS A CG  1 
ATOM   3547  N ND1 . HIS A 1 455 ? 5.55800   -25.95400 -7.06500  1.000 54.29000  ? 474  HIS A ND1 1 
ATOM   3548  C CD2 . HIS A 1 455 ? 7.35100   -27.07200 -7.61400  1.000 45.98000  ? 474  HIS A CD2 1 
ATOM   3549  C CE1 . HIS A 1 455 ? 6.27300   -25.18000 -7.86000  1.000 55.42000  ? 474  HIS A CE1 1 
ATOM   3550  N NE2 . HIS A 1 455 ? 7.37800   -25.82500 -8.18800  1.000 48.53000  ? 474  HIS A NE2 1 
ATOM   3551  N N   . VAL A 1 456 ? 4.69100   -28.71800 -2.91200  1.000 48.74000  ? 475  VAL A N   1 
ATOM   3552  C CA  . VAL A 1 456 ? 3.85100   -29.52200 -2.03200  1.000 49.28000  ? 475  VAL A CA  1 
ATOM   3553  C C   . VAL A 1 456 ? 2.42700   -28.99600 -2.11600  1.000 50.44000  ? 475  VAL A C   1 
ATOM   3554  O O   . VAL A 1 456 ? 2.18500   -27.80900 -1.86300  1.000 53.41000  ? 475  VAL A O   1 
ATOM   3555  C CB  . VAL A 1 456 ? 4.33800   -29.50500 -0.57400  1.000 54.24000  ? 475  VAL A CB  1 
ATOM   3556  C CG1 . VAL A 1 456 ? 3.40700   -30.33500 0.28600   1.000 47.10000  ? 475  VAL A CG1 1 
ATOM   3557  C CG2 . VAL A 1 456 ? 5.78200   -30.01100 -0.47400  1.000 53.05000  ? 475  VAL A CG2 1 
ATOM   3558  N N   . LEU A 1 457 ? 1.49000   -29.87300 -2.46600  1.000 48.15000  ? 476  LEU A N   1 
ATOM   3559  C CA  . LEU A 1 457 ? 0.07400   -29.54100 -2.52500  1.000 46.99000  ? 476  LEU A CA  1 
ATOM   3560  C C   . LEU A 1 457 ? -0.69200  -30.49300 -1.62100  1.000 49.63000  ? 476  LEU A C   1 
ATOM   3561  O O   . LEU A 1 457 ? -0.50000  -31.71100 -1.69500  1.000 53.80000  ? 476  LEU A O   1 
ATOM   3562  C CB  . LEU A 1 457 ? -0.46700  -29.64300 -3.95400  1.000 46.83000  ? 476  LEU A CB  1 
ATOM   3563  C CG  . LEU A 1 457 ? 0.09600   -28.68900 -5.00400  1.000 48.18000  ? 476  LEU A CG  1 
ATOM   3564  C CD1 . LEU A 1 457 ? -0.55100  -28.92900 -6.36400  1.000 49.71000  ? 476  LEU A CD1 1 
ATOM   3565  C CD2 . LEU A 1 457 ? -0.06900  -27.24400 -4.55500  1.000 56.78000  ? 476  LEU A CD2 1 
ATOM   3566  N N   . SER A 1 458 ? -1.55500  -29.94400 -0.77200  1.000 50.57000  ? 477  SER A N   1 
ATOM   3567  C CA  . SER A 1 458 ? -2.51200  -30.78600 -0.06600  1.000 52.63000  ? 477  SER A CA  1 
ATOM   3568  C C   . SER A 1 458 ? -3.50900  -31.36800 -1.06100  1.000 48.17000  ? 477  SER A C   1 
ATOM   3569  O O   . SER A 1 458 ? -3.70800  -30.82700 -2.15100  1.000 53.06000  ? 477  SER A O   1 
ATOM   3570  C CB  . SER A 1 458 ? -3.25600  -29.97900 0.99600   1.000 45.84000  ? 477  SER A CB  1 
ATOM   3571  O OG  . SER A 1 458 ? -4.09000  -29.01800 0.37900   1.000 48.14000  ? 477  SER A OG  1 
ATOM   3572  N N   . LYS A 1 459 ? -4.14100  -32.47900 -0.67700  1.000 49.05000  ? 478  LYS A N   1 
ATOM   3573  C CA  . LYS A 1 459 ? -5.17100  -33.09100 -1.51200  1.000 47.09000  ? 478  LYS A CA  1 
ATOM   3574  C C   . LYS A 1 459 ? -6.21400  -32.06200 -1.95400  1.000 49.65000  ? 478  LYS A C   1 
ATOM   3575  O O   . LYS A 1 459 ? -6.61500  -32.05600 -3.12000  1.000 56.08000  ? 478  LYS A O   1 
ATOM   3576  C CB  . LYS A 1 459 ? -5.87000  -34.24300 -0.77500  1.000 47.33000  ? 478  LYS A CB  1 
ATOM   3577  C CG  . LYS A 1 459 ? -5.01900  -35.47100 -0.45400  1.000 51.70000  ? 478  LYS A CG  1 
ATOM   3578  C CD  . LYS A 1 459 ? -5.88900  -36.52900 0.23800   1.000 45.13000  ? 478  LYS A CD  1 
ATOM   3579  C CE  . LYS A 1 459 ? -5.07700  -37.68700 0.81700   1.000 58.94000  ? 478  LYS A CE  1 
ATOM   3580  N NZ  . LYS A 1 459 ? -4.43600  -38.54800 -0.21000  1.000 50.44000  ? 478  LYS A NZ  1 
ATOM   3581  N N   . ASP A 1 460 ? -6.66300  -31.18800 -1.04500  1.000 51.98000  ? 479  ASP A N   1 
ATOM   3582  C CA  . ASP A 1 460 ? -7.63900  -30.16700 -1.42600  1.000 49.31000  ? 479  ASP A CA  1 
ATOM   3583  C C   . ASP A 1 460 ? -7.07600  -29.20200 -2.46000  1.000 52.32000  ? 479  ASP A C   1 
ATOM   3584  O O   . ASP A 1 460 ? -7.76300  -28.85000 -3.42600  1.000 52.02000  ? 479  ASP A O   1 
ATOM   3585  C CB  . ASP A 1 460 ? -8.12400  -29.39100 -0.19900  1.000 59.30000  ? 479  ASP A CB  1 
ATOM   3586  C CG  . ASP A 1 460 ? -9.24000  -30.10100 0.53700   1.000 74.62000  ? 479  ASP A CG  1 
ATOM   3587  O OD1 . ASP A 1 460 ? -10.00500 -30.84000 -0.12500  1.000 77.42000  ? 479  ASP A OD1 1 
ATOM   3588  O OD2 . ASP A 1 460 ? -9.37400  -29.89800 1.76700   1.000 74.38000  ? 479  ASP A OD2 1 
ATOM   3589  N N   . GLU A 1 461 ? -5.83500  -28.74900 -2.26900  1.000 51.26000  ? 480  GLU A N   1 
ATOM   3590  C CA  . GLU A 1 461 ? -5.21200  -27.88600 -3.26900  1.000 51.45000  ? 480  GLU A CA  1 
ATOM   3591  C C   . GLU A 1 461 ? -5.06000  -28.60900 -4.59500  1.000 53.89000  ? 480  GLU A C   1 
ATOM   3592  O O   . GLU A 1 461 ? -5.33300  -28.03500 -5.65700  1.000 55.43000  ? 480  GLU A O   1 
ATOM   3593  C CB  . GLU A 1 461 ? -3.85200  -27.39400 -2.77600  1.000 52.71000  ? 480  GLU A CB  1 
ATOM   3594  C CG  . GLU A 1 461 ? -3.91600  -26.19900 -1.84500  1.000 59.27000  ? 480  GLU A CG  1 
ATOM   3595  C CD  . GLU A 1 461 ? -2.55500  -25.82600 -1.29300  1.000 63.67000  ? 480  GLU A CD  1 
ATOM   3596  O OE1 . GLU A 1 461 ? -1.64900  -26.69400 -1.27900  1.000 61.86000  ? 480  GLU A OE1 1 
ATOM   3597  O OE2 . GLU A 1 461 ? -2.37200  -24.64100 -0.93800  1.000 69.87000  ? 480  GLU A OE2 1 
ATOM   3598  N N   . LEU A 1 462 ? -4.63800  -29.87400 -4.54600  1.000 47.74000  ? 481  LEU A N   1 
ATOM   3599  C CA  . LEU A 1 462 ? -4.47200  -30.65900 -5.76100  1.000 47.94000  ? 481  LEU A CA  1 
ATOM   3600  C C   . LEU A 1 462 ? -5.74400  -30.67600 -6.60600  1.000 52.75000  ? 481  LEU A C   1 
ATOM   3601  O O   . LEU A 1 462 ? -5.67900  -30.63400 -7.83800  1.000 53.76000  ? 481  LEU A O   1 
ATOM   3602  C CB  . LEU A 1 462 ? -4.04800  -32.07700 -5.39600  1.000 40.61000  ? 481  LEU A CB  1 
ATOM   3603  C CG  . LEU A 1 462 ? -3.88200  -33.05600 -6.55400  1.000 48.07000  ? 481  LEU A CG  1 
ATOM   3604  C CD1 . LEU A 1 462 ? -2.83500  -32.55100 -7.53500  1.000 50.95000  ? 481  LEU A CD1 1 
ATOM   3605  C CD2 . LEU A 1 462 ? -3.50100  -34.42400 -6.00800  1.000 41.10000  ? 481  LEU A CD2 1 
ATOM   3606  N N   . LEU A 1 463 ? -6.91500  -30.72800 -5.96600  1.000 51.52000  ? 482  LEU A N   1 
ATOM   3607  C CA  . LEU A 1 463 ? -8.13500  -30.91600 -6.74500  1.000 57.39000  ? 482  LEU A CA  1 
ATOM   3608  C C   . LEU A 1 463 ? -8.52500  -29.66200 -7.52000  1.000 57.07000  ? 482  LEU A C   1 
ATOM   3609  O O   . LEU A 1 463 ? -9.18100  -29.77200 -8.56200  1.000 67.33000  ? 482  LEU A O   1 
ATOM   3610  C CB  . LEU A 1 463 ? -9.29300  -31.37800 -5.86200  1.000 47.95000  ? 482  LEU A CB  1 
ATOM   3611  C CG  . LEU A 1 463 ? -9.08800  -32.70600 -5.11700  1.000 50.69000  ? 482  LEU A CG  1 
ATOM   3612  C CD1 . LEU A 1 463 ? -10.42600 -33.25000 -4.63600  1.000 53.75000  ? 482  LEU A CD1 1 
ATOM   3613  C CD2 . LEU A 1 463 ? -8.28100  -33.74600 -5.89800  1.000 58.47000  ? 482  LEU A CD2 1 
ATOM   3614  N N   . LYS A 1 464 ? -8.14600  -28.47300 -7.04100  1.000 59.42000  ? 483  LYS A N   1 
ATOM   3615  C CA  . LYS A 1 464 ? -8.41900  -27.24100 -7.78100  1.000 58.26000  ? 483  LYS A CA  1 
ATOM   3616  C C   . LYS A 1 464 ? -7.50800  -27.08100 -8.99300  1.000 60.61000  ? 483  LYS A C   1 
ATOM   3617  O O   . LYS A 1 464 ? -7.77800  -26.24100 -9.86300  1.000 57.23000  ? 483  LYS A O   1 
ATOM   3618  C CB  . LYS A 1 464 ? -8.25200  -26.01300 -6.87100  1.000 65.63000  ? 483  LYS A CB  1 
ATOM   3619  C CG  . LYS A 1 464 ? -9.28100  -25.91200 -5.74200  1.000 76.93000  ? 483  LYS A CG  1 
ATOM   3620  C CD  . LYS A 1 464 ? -9.02100  -24.70700 -4.83100  1.000 89.45000  ? 483  LYS A CD  1 
ATOM   3621  C CE  . LYS A 1 464 ? -9.48200  -23.39100 -5.46800  1.000 94.55000  ? 483  LYS A CE  1 
ATOM   3622  N NZ  . LYS A 1 464 ? -9.29500  -22.21300 -4.56500  1.000 99.12000  ? 483  LYS A NZ  1 
ATOM   3623  N N   . LEU A 1 465 ? -6.44400  -27.87300 -9.06200  1.000 59.65000  ? 484  LEU A N   1 
ATOM   3624  C CA  . LEU A 1 465 ? -5.47000  -27.83300 -10.13600 1.000 58.07000  ? 484  LEU A CA  1 
ATOM   3625  C C   . LEU A 1 465 ? -6.06900  -28.42300 -11.40400 1.000 61.33000  ? 484  LEU A C   1 
ATOM   3626  O O   . LEU A 1 465 ? -6.91500  -29.31600 -11.36000 1.000 57.79000  ? 484  LEU A O   1 
ATOM   3627  C CB  . LEU A 1 465 ? -4.22700  -28.60300 -9.69600  1.000 59.08000  ? 484  LEU A CB  1 
ATOM   3628  C CG  . LEU A 1 465 ? -3.08800  -27.83400 -9.02800  1.000 59.28000  ? 484  LEU A CG  1 
ATOM   3629  C CD1 . LEU A 1 465 ? -2.05800  -27.44600 -10.02900 1.000 52.60000  ? 484  LEU A CD1 1 
ATOM   3630  C CD2 . LEU A 1 465 ? -3.65400  -26.53100 -8.44700  1.000 56.07000  ? 484  LEU A CD2 1 
ATOM   3631  N N   . ASP A 1 466 ? -5.61500  -27.92300 -12.55800 1.000 60.67000  ? 485  ASP A N   1 
ATOM   3632  C CA  . ASP A 1 466 ? -6.10200  -28.39300 -13.85400 1.000 57.11000  ? 485  ASP A CA  1 
ATOM   3633  C C   . ASP A 1 466 ? -5.35700  -29.66800 -14.23100 1.000 59.88000  ? 485  ASP A C   1 
ATOM   3634  O O   . ASP A 1 466 ? -4.58300  -29.70200 -15.18800 1.000 65.78000  ? 485  ASP A O   1 
ATOM   3635  C CB  . ASP A 1 466 ? -5.93900  -27.29100 -14.90000 1.000 51.83000  ? 485  ASP A CB  1 
ATOM   3636  C CG  . ASP A 1 466 ? -6.50500  -27.66600 -16.28400 1.000 72.07000  ? 485  ASP A CG  1 
ATOM   3637  O OD1 . ASP A 1 466 ? -7.08100  -28.77700 -16.44000 1.000 82.41000  ? 485  ASP A OD1 1 
ATOM   3638  O OD2 . ASP A 1 466 ? -6.35900  -26.85500 -17.23100 1.000 68.05000  ? 485  ASP A OD2 1 
ATOM   3639  N N   . TYR A 1 467 ? -5.70900  -30.75100 -13.54800 1.000 55.09000  ? 486  TYR A N   1 
ATOM   3640  C CA  . TYR A 1 467 ? -5.10500  -32.06900 -13.85400 1.000 59.87000  ? 486  TYR A CA  1 
ATOM   3641  C C   . TYR A 1 467 ? -5.88000  -32.70300 -15.00800 1.000 57.32000  ? 486  TYR A C   1 
ATOM   3642  O O   . TYR A 1 467 ? -7.06400  -32.42400 -15.15400 1.000 51.74000  ? 486  TYR A O   1 
ATOM   3643  C CB  . TYR A 1 467 ? -4.97300  -32.93900 -12.60200 1.000 61.39000  ? 486  TYR A CB  1 
ATOM   3644  C CG  . TYR A 1 467 ? -6.23500  -33.39400 -11.91400 1.000 55.85000  ? 486  TYR A CG  1 
ATOM   3645  C CD1 . TYR A 1 467 ? -6.88200  -32.60200 -10.98600 1.000 57.97000  ? 486  TYR A CD1 1 
ATOM   3646  C CD2 . TYR A 1 467 ? -6.73300  -34.66100 -12.12700 1.000 56.21000  ? 486  TYR A CD2 1 
ATOM   3647  C CE1 . TYR A 1 467 ? -8.01500  -33.03900 -10.32600 1.000 52.53000  ? 486  TYR A CE1 1 
ATOM   3648  C CE2 . TYR A 1 467 ? -7.86200  -35.11900 -11.47700 1.000 55.37000  ? 486  TYR A CE2 1 
ATOM   3649  C CZ  . TYR A 1 467 ? -8.50500  -34.30400 -10.57400 1.000 54.90000  ? 486  TYR A CZ  1 
ATOM   3650  O OH  . TYR A 1 467 ? -9.62100  -34.76300 -9.95300  1.000 53.27000  ? 486  TYR A OH  1 
ATOM   3651  N N   . ASP A 1 468 ? -5.19500  -33.51000 -15.81400 1.000 54.86000  ? 487  ASP A N   1 
ATOM   3652  C CA  . ASP A 1 468 ? -5.82700  -34.14500 -16.96000 1.000 50.75000  ? 487  ASP A CA  1 
ATOM   3653  C C   . ASP A 1 468 ? -5.26700  -35.54800 -17.19900 1.000 51.21000  ? 487  ASP A C   1 
ATOM   3654  O O   . ASP A 1 468 ? -4.11100  -35.84600 -16.88000 1.000 46.01000  ? 487  ASP A O   1 
ATOM   3655  C CB  . ASP A 1 468 ? -5.63500  -33.29500 -18.20500 1.000 50.29000  ? 487  ASP A CB  1 
ATOM   3656  C CG  . ASP A 1 468 ? -6.44900  -33.77700 -19.35900 1.000 55.43000  ? 487  ASP A CG  1 
ATOM   3657  O OD1 . ASP A 1 468 ? -7.66200  -33.48800 -19.38400 1.000 62.38000  ? 487  ASP A OD1 1 
ATOM   3658  O OD2 . ASP A 1 468 ? -5.87700  -34.45900 -20.23000 1.000 57.49000  ? 487  ASP A OD2 1 
ATOM   3659  N N   . ALA A 1 469 ? -6.09600  -36.40000 -17.81600 1.000 48.19000  ? 488  ALA A N   1 
ATOM   3660  C CA  . ALA A 1 469 ? -5.70800  -37.77700 -18.11100 1.000 46.91000  ? 488  ALA A CA  1 
ATOM   3661  C C   . ALA A 1 469 ? -4.66100  -37.86800 -19.20300 1.000 44.14000  ? 488  ALA A C   1 
ATOM   3662  O O   . ALA A 1 469 ? -3.89600  -38.83900 -19.24400 1.000 42.03000  ? 488  ALA A O   1 
ATOM   3663  C CB  . ALA A 1 469 ? -6.92600  -38.59900 -18.53400 1.000 39.34000  ? 488  ALA A CB  1 
ATOM   3664  N N   . TYR A 1 470 ? -4.61200  -36.88000 -20.08400 1.000 44.58000  ? 489  TYR A N   1 
ATOM   3665  C CA  . TYR A 1 470 ? -3.85400  -36.98700 -21.31500 1.000 45.96000  ? 489  TYR A CA  1 
ATOM   3666  C C   . TYR A 1 470 ? -2.58400  -36.16200 -21.29200 1.000 48.59000  ? 489  TYR A C   1 
ATOM   3667  O O   . TYR A 1 470 ? -1.64000  -36.47600 -22.01700 1.000 42.24000  ? 489  TYR A O   1 
ATOM   3668  C CB  . TYR A 1 470 ? -4.73800  -36.54800 -22.49000 1.000 42.53000  ? 489  TYR A CB  1 
ATOM   3669  C CG  . TYR A 1 470 ? -6.07100  -37.26900 -22.49200 1.000 38.82000  ? 489  TYR A CG  1 
ATOM   3670  C CD1 . TYR A 1 470 ? -6.16700  -38.58800 -22.90300 1.000 35.35000  ? 489  TYR A CD1 1 
ATOM   3671  C CD2 . TYR A 1 470 ? -7.23300  -36.62900 -22.06200 1.000 43.15000  ? 489  TYR A CD2 1 
ATOM   3672  C CE1 . TYR A 1 470 ? -7.37300  -39.25500 -22.89400 1.000 39.30000  ? 489  TYR A CE1 1 
ATOM   3673  C CE2 . TYR A 1 470 ? -8.46000  -37.28700 -22.05400 1.000 41.24000  ? 489  TYR A CE2 1 
ATOM   3674  C CZ  . TYR A 1 470 ? -8.52000  -38.60100 -22.47100 1.000 40.01000  ? 489  TYR A CZ  1 
ATOM   3675  O OH  . TYR A 1 470 ? -9.71900  -39.27400 -22.47100 1.000 36.34000  ? 489  TYR A OH  1 
ATOM   3676  N N   . TYR A 1 471 ? -2.54500  -35.12400 -20.46300 1.000 58.12000  ? 490  TYR A N   1 
ATOM   3677  C CA  . TYR A 1 471 ? -1.40800  -34.22500 -20.36200 1.000 66.03000  ? 490  TYR A CA  1 
ATOM   3678  C C   . TYR A 1 471 ? -1.15700  -33.91700 -18.89300 1.000 66.27000  ? 490  TYR A C   1 
ATOM   3679  O O   . TYR A 1 471 ? -2.10600  -33.66500 -18.14200 1.000 62.35000  ? 490  TYR A O   1 
ATOM   3680  C CB  . TYR A 1 471 ? -1.68200  -32.93400 -21.13400 1.000 74.40000  ? 490  TYR A CB  1 
ATOM   3681  C CG  . TYR A 1 471 ? -0.47800  -32.05100 -21.25700 1.000 85.19000  ? 490  TYR A CG  1 
ATOM   3682  C CD1 . TYR A 1 471 ? 0.50900   -32.33600 -22.18700 1.000 91.50000  ? 490  TYR A CD1 1 
ATOM   3683  C CD2 . TYR A 1 471 ? -0.31400  -30.94100 -20.43900 1.000 97.31000  ? 490  TYR A CD2 1 
ATOM   3684  C CE1 . TYR A 1 471 ? 1.61800   -31.53700 -22.31300 1.000 103.27000 ? 490  TYR A CE1 1 
ATOM   3685  C CE2 . TYR A 1 471 ? 0.79900   -30.13100 -20.55500 1.000 107.00000 ? 490  TYR A CE2 1 
ATOM   3686  C CZ  . TYR A 1 471 ? 1.76400   -30.43900 -21.49000 1.000 113.14000 ? 490  TYR A CZ  1 
ATOM   3687  O OH  . TYR A 1 471 ? 2.87600   -29.63800 -21.62300 1.000 124.52000 ? 490  TYR A OH  1 
ATOM   3688  N N   . ALA A 1 472 ? 0.11000   -33.94600 -18.48200 1.000 70.44000  ? 491  ALA A N   1 
ATOM   3689  C CA  . ALA A 1 472 ? 0.45800   -33.66300 -17.09300 1.000 66.65000  ? 491  ALA A CA  1 
ATOM   3690  C C   . ALA A 1 472 ? 0.34800   -32.16600 -16.80500 1.000 64.12000  ? 491  ALA A C   1 
ATOM   3691  O O   . ALA A 1 472 ? 0.88700   -31.33700 -17.54600 1.000 67.98000  ? 491  ALA A O   1 
ATOM   3692  C CB  . ALA A 1 472 ? 1.86600   -34.16800 -16.78500 1.000 64.55000  ? 491  ALA A CB  1 
ATOM   3693  N N   . PHE A 1 473 ? -0.36700  -31.82200 -15.73000 1.000 62.53000  ? 492  PHE A N   1 
ATOM   3694  C CA  . PHE A 1 473 ? -0.62900  -30.41600 -15.42700 1.000 63.20000  ? 492  PHE A CA  1 
ATOM   3695  C C   . PHE A 1 473 ? 0.65100   -29.67300 -15.09000 1.000 60.91000  ? 492  PHE A C   1 
ATOM   3696  O O   . PHE A 1 473 ? 0.77300   -28.46700 -15.34200 1.000 56.60000  ? 492  PHE A O   1 
ATOM   3697  C CB  . PHE A 1 473 ? -1.60100  -30.30800 -14.25100 1.000 62.55000  ? 492  PHE A CB  1 
ATOM   3698  C CG  . PHE A 1 473 ? -0.98200  -30.63500 -12.91400 1.000 61.67000  ? 492  PHE A CG  1 
ATOM   3699  C CD1 . PHE A 1 473 ? -0.92500  -31.94200 -12.44800 1.000 61.52000  ? 492  PHE A CD1 1 
ATOM   3700  C CD2 . PHE A 1 473 ? -0.46000  -29.62000 -12.12200 1.000 63.10000  ? 492  PHE A CD2 1 
ATOM   3701  C CE1 . PHE A 1 473 ? -0.34900  -32.22200 -11.22000 1.000 70.74000  ? 492  PHE A CE1 1 
ATOM   3702  C CE2 . PHE A 1 473 ? 0.11700   -29.89300 -10.90000 1.000 54.84000  ? 492  PHE A CE2 1 
ATOM   3703  C CZ  . PHE A 1 473 ? 0.17200   -31.19000 -10.44500 1.000 63.37000  ? 492  PHE A CZ  1 
ATOM   3704  N N   . TYR A 1 474 ? 1.66700   -30.41000 -14.59400 1.000 64.56000  ? 493  TYR A N   1 
ATOM   3705  C CA  . TYR A 1 474 ? 2.87300   -29.81500 -13.96600 1.000 58.87000  ? 493  TYR A CA  1 
ATOM   3706  C C   . TYR A 1 474 ? 3.77900   -29.30400 -15.05900 1.000 61.83000  ? 493  TYR A C   1 
ATOM   3707  O O   . TYR A 1 474 ? 4.59800   -28.41200 -14.82300 1.000 51.70000  ? 493  TYR A O   1 
ATOM   3708  C CB  . TYR A 1 474 ? 3.53900   -30.77500 -12.97800 1.000 63.25000  ? 493  TYR A CB  1 
ATOM   3709  C CG  . TYR A 1 474 ? 3.87800   -32.15000 -13.48700 1.000 69.92000  ? 493  TYR A CG  1 
ATOM   3710  C CD1 . TYR A 1 474 ? 4.81200   -32.34800 -14.48500 1.000 71.16000  ? 493  TYR A CD1 1 
ATOM   3711  C CD2 . TYR A 1 474 ? 3.28700   -33.27000 -12.93700 1.000 71.42000  ? 493  TYR A CD2 1 
ATOM   3712  C CE1 . TYR A 1 474 ? 5.12200   -33.61600 -14.94400 1.000 76.33000  ? 493  TYR A CE1 1 
ATOM   3713  C CE2 . TYR A 1 474 ? 3.58700   -34.54300 -13.38200 1.000 65.23000  ? 493  TYR A CE2 1 
ATOM   3714  C CZ  . TYR A 1 474 ? 4.51300   -34.72100 -14.38400 1.000 76.93000  ? 493  TYR A CZ  1 
ATOM   3715  O OH  . TYR A 1 474 ? 4.80200   -35.98100 -14.81000 1.000 78.97000  ? 493  TYR A OH  1 
ATOM   3716  N N   . GLY A 1 475 ? 3.58200   -29.89700 -16.22000 1.000 47.14000  ? 494  GLY A N   1 
ATOM   3717  C CA  . GLY A 1 475 ? 4.30500   -29.45100 -17.38600 1.000 49.71000  ? 494  GLY A CA  1 
ATOM   3718  C C   . GLY A 1 475 ? 4.08900   -27.98900 -17.69500 1.000 45.97000  ? 494  GLY A C   1 
ATOM   3719  O O   . GLY A 1 475 ? 5.05400   -27.24400 -17.87700 1.000 50.02000  ? 494  GLY A O   1 
ATOM   3720  N N   . ILE A 1 476 ? 2.83200   -27.55700 -17.76400 1.000 51.45000  ? 495  ILE A N   1 
ATOM   3721  C CA  . ILE A 1 476 ? 2.57000   -26.15800 -18.08400 1.000 49.21000  ? 495  ILE A CA  1 
ATOM   3722  C C   . ILE A 1 476 ? 3.00800   -25.26100 -16.93000 1.000 44.17000  ? 495  ILE A C   1 
ATOM   3723  O O   . ILE A 1 476 ? 3.48300   -24.13600 -17.14000 1.000 39.17000  ? 495  ILE A O   1 
ATOM   3724  C CB  . ILE A 1 476 ? 1.08600   -25.95600 -18.45200 1.000 46.15000  ? 495  ILE A CB  1 
ATOM   3725  C CG1 . ILE A 1 476 ? 0.91200   -24.65400 -19.22200 1.000 41.30000  ? 495  ILE A CG1 1 
ATOM   3726  C CG2 . ILE A 1 476 ? 0.20800   -25.94600 -17.21800 1.000 51.33000  ? 495  ILE A CG2 1 
ATOM   3727  C CD1 . ILE A 1 476 ? 1.61900   -24.68500 -20.57300 1.000 48.30000  ? 495  ILE A CD1 1 
ATOM   3728  N N   . VAL A 1 477 ? 2.86700   -25.74800 -15.69700 1.000 40.67000  ? 496  VAL A N   1 
ATOM   3729  C CA  . VAL A 1 477 ? 3.32900   -24.98800 -14.54000 1.000 47.02000  ? 496  VAL A CA  1 
ATOM   3730  C C   . VAL A 1 477 ? 4.81700   -24.70700 -14.66000 1.000 45.86000  ? 496  VAL A C   1 
ATOM   3731  O O   . VAL A 1 477 ? 5.27400   -23.57200 -14.47100 1.000 42.91000  ? 496  VAL A O   1 
ATOM   3732  C CB  . VAL A 1 477 ? 3.00500   -25.73900 -13.23800 1.000 47.37000  ? 496  VAL A CB  1 
ATOM   3733  C CG1 . VAL A 1 477 ? 3.69600   -25.07900 -12.05800 1.000 41.67000  ? 496  VAL A CG1 1 
ATOM   3734  C CG2 . VAL A 1 477 ? 1.50300   -25.78200 -13.02200 1.000 37.89000  ? 496  VAL A CG2 1 
ATOM   3735  N N   . GLU A 1 478 ? 5.59600   -25.73200 -15.00000 1.000 43.27000  ? 497  GLU A N   1 
ATOM   3736  C CA  . GLU A 1 478 ? 7.02600   -25.51600 -15.14600 1.000 39.60000  ? 497  GLU A CA  1 
ATOM   3737  C C   . GLU A 1 478 ? 7.30200   -24.49300 -16.24000 1.000 43.57000  ? 497  GLU A C   1 
ATOM   3738  O O   . GLU A 1 478 ? 8.13200   -23.59500 -16.05600 1.000 40.49000  ? 497  GLU A O   1 
ATOM   3739  C CB  . GLU A 1 478 ? 7.73300   -26.83100 -15.45200 1.000 42.36000  ? 497  GLU A CB  1 
ATOM   3740  C CG  . GLU A 1 478 ? 9.18200   -26.84500 -15.02500 1.000 43.27000  ? 497  GLU A CG  1 
ATOM   3741  C CD  . GLU A 1 478 ? 9.89700   -28.10700 -15.44900 1.000 46.39000  ? 497  GLU A CD  1 
ATOM   3742  O OE1 . GLU A 1 478 ? 9.47600   -28.73100 -16.44400 1.000 49.16000  ? 497  GLU A OE1 1 
ATOM   3743  O OE2 . GLU A 1 478 ? 10.80900  -28.54300 -14.71800 1.000 53.07000  ? 497  GLU A OE2 1 
ATOM   3744  N N   . GLU A 1 479 ? 6.60400   -24.59500 -17.38300 1.000 46.56000  ? 498  GLU A N   1 
ATOM   3745  C CA  . GLU A 1 479 ? 6.81800   -23.60800 -18.44200 1.000 43.31000  ? 498  GLU A CA  1 
ATOM   3746  C C   . GLU A 1 479 ? 6.31800   -22.23800 -18.04500 1.000 43.11000  ? 498  GLU A C   1 
ATOM   3747  O O   . GLU A 1 479 ? 6.85400   -21.22400 -18.50000 1.000 45.81000  ? 498  GLU A O   1 
ATOM   3748  C CB  . GLU A 1 479 ? 6.14400   -24.02500 -19.74600 1.000 42.16000  ? 498  GLU A CB  1 
ATOM   3749  C CG  . GLU A 1 479 ? 6.76400   -25.23600 -20.41000 1.000 50.54000  ? 498  GLU A CG  1 
ATOM   3750  C CD  . GLU A 1 479 ? 6.20600   -25.48300 -21.80800 1.000 62.59000  ? 498  GLU A CD  1 
ATOM   3751  O OE1 . GLU A 1 479 ? 5.32200   -24.71700 -22.26300 1.000 54.57000  ? 498  GLU A OE1 1 
ATOM   3752  O OE2 . GLU A 1 479 ? 6.64100   -26.46800 -22.44800 1.000 82.98000  ? 498  GLU A OE2 1 
ATOM   3753  N N   . MET A 1 480 ? 5.28700   -22.17000 -17.21100 1.000 43.36000  ? 499  MET A N   1 
ATOM   3754  C CA  . MET A 1 480 ? 4.86000   -20.86800 -16.72100 1.000 46.00000  ? 499  MET A CA  1 
ATOM   3755  C C   . MET A 1 480 ? 5.93600   -20.25500 -15.83300 1.000 37.86000  ? 499  MET A C   1 
ATOM   3756  O O   . MET A 1 480 ? 6.29400   -19.08300 -15.98100 1.000 40.65000  ? 499  MET A O   1 
ATOM   3757  C CB  . MET A 1 480 ? 3.54500   -20.99900 -15.96200 1.000 49.40000  ? 499  MET A CB  1 
ATOM   3758  C CG  . MET A 1 480 ? 2.87200   -19.67100 -15.81800 1.000 55.22000  ? 499  MET A CG  1 
ATOM   3759  S SD  . MET A 1 480 ? 2.16500   -19.26700 -17.42000 1.000 70.47000  ? 499  MET A SD  1 
ATOM   3760  C CE  . MET A 1 480 ? 2.58300   -17.54500 -17.43900 1.000 45.17000  ? 499  MET A CE  1 
ATOM   3761  N N   . LEU A 1 481 ? 6.48000   -21.03900 -14.90400 1.000 31.34000  ? 500  LEU A N   1 
ATOM   3762  C CA  . LEU A 1 481 ? 7.52500   -20.51900 -14.03600 1.000 43.72000  ? 500  LEU A CA  1 
ATOM   3763  C C   . LEU A 1 481 ? 8.75800   -20.11700 -14.83700 1.000 43.01000  ? 500  LEU A C   1 
ATOM   3764  O O   . LEU A 1 481 ? 9.35400   -19.06500 -14.57300 1.000 41.94000  ? 500  LEU A O   1 
ATOM   3765  C CB  . LEU A 1 481 ? 7.89300   -21.56500 -12.97600 1.000 40.45000  ? 500  LEU A CB  1 
ATOM   3766  C CG  . LEU A 1 481 ? 6.84000   -21.86700 -11.91000 1.000 37.75000  ? 500  LEU A CG  1 
ATOM   3767  C CD1 . LEU A 1 481 ? 7.26100   -23.09300 -11.11900 1.000 37.03000  ? 500  LEU A CD1 1 
ATOM   3768  C CD2 . LEU A 1 481 ? 6.66100   -20.67400 -10.98000 1.000 36.24000  ? 500  LEU A CD2 1 
ATOM   3769  N N   . LYS A 1 482 ? 9.14600   -20.92700 -15.82800 1.000 36.01000  ? 501  LYS A N   1 
ATOM   3770  C CA  . LYS A 1 482 ? 10.31700  -20.59300 -16.62600 1.000 37.38000  ? 501  LYS A CA  1 
ATOM   3771  C C   . LYS A 1 482 ? 10.09000  -19.31900 -17.42900 1.000 40.87000  ? 501  LYS A C   1 
ATOM   3772  O O   . LYS A 1 482 ? 11.00100  -18.49200 -17.55600 1.000 42.18000  ? 501  LYS A O   1 
ATOM   3773  C CB  . LYS A 1 482 ? 10.70500  -21.77400 -17.51700 1.000 43.73000  ? 501  LYS A CB  1 
ATOM   3774  C CG  . LYS A 1 482 ? 11.27700  -22.91200 -16.67700 1.000 41.98000  ? 501  LYS A CG  1 
ATOM   3775  C CD  . LYS A 1 482 ? 11.52000  -24.22900 -17.39200 1.000 45.91000  ? 501  LYS A CD  1 
ATOM   3776  C CE  . LYS A 1 482 ? 12.78100  -24.21900 -18.22400 1.000 59.95000  ? 501  LYS A CE  1 
ATOM   3777  N NZ  . LYS A 1 482 ? 13.17600  -25.61300 -18.58900 1.000 66.31000  ? 501  LYS A NZ  1 
ATOM   3778  N N   . PHE A 1 483 ? 8.87700   -19.12100 -17.94600 1.000 35.81000  ? 502  PHE A N   1 
ATOM   3779  C CA  . PHE A 1 483 ? 8.58800   -17.90500 -18.69900 1.000 33.44000  ? 502  PHE A CA  1 
ATOM   3780  C C   . PHE A 1 483 ? 8.65500   -16.64800 -17.83000 1.000 37.24000  ? 502  PHE A C   1 
ATOM   3781  O O   . PHE A 1 483 ? 9.19300   -15.62600 -18.26200 1.000 44.27000  ? 502  PHE A O   1 
ATOM   3782  C CB  . PHE A 1 483 ? 7.21800   -18.01500 -19.36800 1.000 45.24000  ? 502  PHE A CB  1 
ATOM   3783  C CG  . PHE A 1 483 ? 6.74000   -16.72800 -19.96400 1.000 44.41000  ? 502  PHE A CG  1 
ATOM   3784  C CD1 . PHE A 1 483 ? 7.35400   -16.19800 -21.09100 1.000 38.55000  ? 502  PHE A CD1 1 
ATOM   3785  C CD2 . PHE A 1 483 ? 5.67300   -16.04300 -19.39500 1.000 43.30000  ? 502  PHE A CD2 1 
ATOM   3786  C CE1 . PHE A 1 483 ? 6.92500   -15.00900 -21.63100 1.000 37.22000  ? 502  PHE A CE1 1 
ATOM   3787  C CE2 . PHE A 1 483 ? 5.22900   -14.85100 -19.93800 1.000 45.00000  ? 502  PHE A CE2 1 
ATOM   3788  C CZ  . PHE A 1 483 ? 5.85700   -14.33300 -21.05700 1.000 45.42000  ? 502  PHE A CZ  1 
ATOM   3789  N N   . ILE A 1 484 ? 8.10200   -16.67800 -16.61600 1.000 36.46000  ? 503  ILE A N   1 
ATOM   3790  C CA  . ILE A 1 484 ? 8.06200   -15.44000 -15.84000 1.000 42.48000  ? 503  ILE A CA  1 
ATOM   3791  C C   . ILE A 1 484 ? 9.44500   -15.09900 -15.29900 1.000 40.87000  ? 503  ILE A C   1 
ATOM   3792  O O   . ILE A 1 484 ? 9.79400   -13.92000 -15.15900 1.000 40.73000  ? 503  ILE A O   1 
ATOM   3793  C CB  . ILE A 1 484 ? 7.00500   -15.50700 -14.71800 1.000 41.70000  ? 503  ILE A CB  1 
ATOM   3794  C CG1 . ILE A 1 484 ? 7.29200   -16.62800 -13.72100 1.000 47.67000  ? 503  ILE A CG1 1 
ATOM   3795  C CG2 . ILE A 1 484 ? 5.60300   -15.64300 -15.30800 1.000 45.30000  ? 503  ILE A CG2 1 
ATOM   3796  C CD1 . ILE A 1 484 ? 6.42000   -16.55700 -12.45800 1.000 45.25000  ? 503  ILE A CD1 1 
ATOM   3797  N N   . HIS A 1 485 ? 10.22800  -16.12100 -14.94100 1.000 42.13000  ? 504  HIS A N   1 
ATOM   3798  C CA  . HIS A 1 485 ? 11.63500  -15.93700 -14.59700 1.000 41.89000  ? 504  HIS A CA  1 
ATOM   3799  C C   . HIS A 1 485 ? 12.36600  -15.21100 -15.71700 1.000 43.53000  ? 504  HIS A C   1 
ATOM   3800  O O   . HIS A 1 485 ? 13.04200  -14.20000 -15.48800 1.000 46.35000  ? 504  HIS A O   1 
ATOM   3801  C CB  . HIS A 1 485 ? 12.25600  -17.30700 -14.35800 1.000 41.23000  ? 504  HIS A CB  1 
ATOM   3802  C CG  . HIS A 1 485 ? 13.72800  -17.27600 -14.10900 1.000 45.56000  ? 504  HIS A CG  1 
ATOM   3803  N ND1 . HIS A 1 485 ? 14.26300  -16.88000 -12.90400 1.000 43.07000  ? 504  HIS A ND1 1 
ATOM   3804  C CD2 . HIS A 1 485 ? 14.77700  -17.60100 -14.90100 1.000 46.47000  ? 504  HIS A CD2 1 
ATOM   3805  C CE1 . HIS A 1 485 ? 15.57900  -16.96200 -12.96300 1.000 47.98000  ? 504  HIS A CE1 1 
ATOM   3806  N NE2 . HIS A 1 485 ? 15.91800  -17.40100 -14.16100 1.000 49.31000  ? 504  HIS A NE2 1 
ATOM   3807  N N   . ARG A 1 486 ? 12.18900  -15.72000 -16.95900 1.000 37.81000  ? 505  ARG A N   1 
ATOM   3808  C CA  . ARG A 1 486 ? 12.77900  -15.15100 -18.17600 1.000 42.74000  ? 505  ARG A CA  1 
ATOM   3809  C C   . ARG A 1 486 ? 12.35400  -13.72700 -18.38100 1.000 42.54000  ? 505  ARG A C   1 
ATOM   3810  O O   . ARG A 1 486 ? 13.20700  -12.87000 -18.58500 1.000 44.94000  ? 505  ARG A O   1 
ATOM   3811  C CB  . ARG A 1 486 ? 12.37900  -15.89600 -19.45600 1.000 47.37000  ? 505  ARG A CB  1 
ATOM   3812  C CG  . ARG A 1 486 ? 13.45600  -16.66200 -20.05500 1.000 47.37000  ? 505  ARG A CG  1 
ATOM   3813  C CD  . ARG A 1 486 ? 13.63300  -17.79600 -19.06600 1.000 43.04000  ? 505  ARG A CD  1 
ATOM   3814  N NE  . ARG A 1 486 ? 14.30300  -19.04000 -19.53600 1.000 47.64000  ? 505  ARG A NE  1 
ATOM   3815  C CZ  . ARG A 1 486 ? 14.51800  -20.13000 -18.80700 1.000 59.35000  ? 505  ARG A CZ  1 
ATOM   3816  N NH1 . ARG A 1 486 ? 14.20100  -20.18900 -17.52700 1.000 59.66000  ? 505  ARG A NH1 1 
ATOM   3817  N NH2 . ARG A 1 486 ? 14.88700  -21.23300 -19.42200 1.000 62.62000  ? 505  ARG A NH2 1 
ATOM   3818  N N   . ALA A 1 487 ? 11.04800  -13.44100 -18.31700 1.000 46.06000  ? 506  ALA A N   1 
ATOM   3819  C CA  . ALA A 1 487 ? 10.54400  -12.10800 -18.64400 1.000 40.26000  ? 506  ALA A CA  1 
ATOM   3820  C C   . ALA A 1 487 ? 11.06600  -11.04800 -17.67500 1.000 40.90000  ? 506  ALA A C   1 
ATOM   3821  O O   . ALA A 1 487 ? 11.41100  -9.92300  -18.07200 1.000 47.79000  ? 506  ALA A O   1 
ATOM   3822  C CB  . ALA A 1 487 ? 9.01200   -12.14900 -18.64300 1.000 43.39000  ? 506  ALA A CB  1 
ATOM   3823  N N   . ASP A 1 488 ? 11.09200  -11.38400 -16.39500 1.000 44.59000  ? 507  ASP A N   1 
ATOM   3824  C CA  . ASP A 1 488 ? 11.66100  -10.50300 -15.39400 1.000 46.86000  ? 507  ASP A CA  1 
ATOM   3825  C C   . ASP A 1 488 ? 13.15800  -10.34800 -15.58100 1.000 50.60000  ? 507  ASP A C   1 
ATOM   3826  O O   . ASP A 1 488 ? 13.69400  -9.24500  -15.43300 1.000 52.91000  ? 507  ASP A O   1 
ATOM   3827  C CB  . ASP A 1 488 ? 11.34600  -11.05200 -14.01300 1.000 51.53000  ? 507  ASP A CB  1 
ATOM   3828  C CG  . ASP A 1 488 ? 12.00600  -10.26000 -12.90900 1.000 63.91000  ? 507  ASP A CG  1 
ATOM   3829  O OD1 . ASP A 1 488 ? 11.57500  -9.10900  -12.67200 1.000 73.56000  ? 507  ASP A OD1 1 
ATOM   3830  O OD2 . ASP A 1 488 ? 12.94200  -10.79800 -12.26300 1.000 62.11000  ? 507  ASP A OD2 1 
ATOM   3831  N N   . ALA A 1 489 ? 13.85300  -11.44200 -15.89500 1.000 47.08000  ? 508  ALA A N   1 
ATOM   3832  C CA  . ALA A 1 489 ? 15.30600  -11.38100 -15.99000 1.000 46.78000  ? 508  ALA A CA  1 
ATOM   3833  C C   . ALA A 1 489 ? 15.75500  -10.52900 -17.16900 1.000 49.78000  ? 508  ALA A C   1 
ATOM   3834  O O   . ALA A 1 489 ? 16.68900  -9.73200  -17.04300 1.000 50.14000  ? 508  ALA A O   1 
ATOM   3835  C CB  . ALA A 1 489 ? 15.87800  -12.79000 -16.08400 1.000 44.48000  ? 508  ALA A CB  1 
ATOM   3836  N N   . ILE A 1 490 ? 15.08900  -10.65700 -18.31500 1.000 49.28000  ? 509  ILE A N   1 
ATOM   3837  C CA  . ILE A 1 490 ? 15.56900  -9.95000  -19.49900 1.000 47.33000  ? 509  ILE A CA  1 
ATOM   3838  C C   . ILE A 1 490 ? 15.42500  -8.43900  -19.34000 1.000 53.18000  ? 509  ILE A C   1 
ATOM   3839  O O   . ILE A 1 490 ? 16.30400  -7.68700  -19.77200 1.000 50.21000  ? 509  ILE A O   1 
ATOM   3840  C CB  . ILE A 1 490 ? 14.88100  -10.48500 -20.77500 1.000 49.59000  ? 509  ILE A CB  1 
ATOM   3841  C CG1 . ILE A 1 490 ? 15.62500  -10.03300 -22.02000 1.000 43.81000  ? 509  ILE A CG1 1 
ATOM   3842  C CG2 . ILE A 1 490 ? 13.43400  -10.01800 -20.85200 1.000 44.64000  ? 509  ILE A CG2 1 
ATOM   3843  C CD1 . ILE A 1 490 ? 15.23700  -10.79600 -23.25100 1.000 33.86000  ? 509  ILE A CD1 1 
ATOM   3844  N N   . LYS A 1 491 ? 14.35200  -7.95100  -18.69900 1.000 53.39000  ? 510  LYS A N   1 
ATOM   3845  C CA  . LYS A 1 491 ? 14.31800  -6.51500  -18.41600 1.000 57.12000  ? 510  LYS A CA  1 
ATOM   3846  C C   . LYS A 1 491 ? 15.44700  -6.11600  -17.48400 1.000 54.58000  ? 510  LYS A C   1 
ATOM   3847  O O   . LYS A 1 491 ? 15.93700  -4.98600  -17.55100 1.000 56.38000  ? 510  LYS A O   1 
ATOM   3848  C CB  . LYS A 1 491 ? 12.98200  -6.05400  -17.80500 1.000 59.64000  ? 510  LYS A CB  1 
ATOM   3849  C CG  . LYS A 1 491 ? 11.80400  -5.97400  -18.77200 1.000 73.49000  ? 510  LYS A CG  1 
ATOM   3850  C CD  . LYS A 1 491 ? 10.68600  -5.08000  -18.21800 1.000 81.17000  ? 510  LYS A CD  1 
ATOM   3851  C CE  . LYS A 1 491 ? 11.03500  -3.59500  -18.38600 1.000 91.41000  ? 510  LYS A CE  1 
ATOM   3852  N NZ  . LYS A 1 491 ? 10.99300  -3.13200  -19.80700 1.000 91.90000  ? 510  LYS A NZ  1 
ATOM   3853  N N   . SER A 1 492 ? 15.87000  -7.02900  -16.61800 1.000 53.47000  ? 511  SER A N   1 
ATOM   3854  C CA  . SER A 1 492 ? 16.98100  -6.75200  -15.72100 1.000 52.89000  ? 511  SER A CA  1 
ATOM   3855  C C   . SER A 1 492 ? 18.30500  -6.71900  -16.47600 1.000 54.74000  ? 511  SER A C   1 
ATOM   3856  O O   . SER A 1 492 ? 19.22400  -5.98300  -16.09100 1.000 54.81000  ? 511  SER A O   1 
ATOM   3857  C CB  . SER A 1 492 ? 17.00700  -7.77900  -14.60800 1.000 44.67000  ? 511  SER A CB  1 
ATOM   3858  O OG  . SER A 1 492 ? 18.17000  -7.64800  -13.81600 1.000 62.47000  ? 511  SER A OG  1 
ATOM   3859  N N   . TYR A 1 493 ? 18.41500  -7.50400  -17.54800 1.000 52.58000  ? 512  TYR A N   1 
ATOM   3860  C CA  . TYR A 1 493 ? 19.68600  -7.70700  -18.23800 1.000 47.74000  ? 512  TYR A CA  1 
ATOM   3861  C C   . TYR A 1 493 ? 19.97500  -6.61500  -19.26200 1.000 53.82000  ? 512  TYR A C   1 
ATOM   3862  O O   . TYR A 1 493 ? 21.09400  -6.09800  -19.32700 1.000 56.85000  ? 512  TYR A O   1 
ATOM   3863  C CB  . TYR A 1 493 ? 19.67900  -9.07300  -18.92100 1.000 46.99000  ? 512  TYR A CB  1 
ATOM   3864  C CG  . TYR A 1 493 ? 20.82400  -9.26700  -19.88400 1.000 49.69000  ? 512  TYR A CG  1 
ATOM   3865  C CD1 . TYR A 1 493 ? 22.10700  -9.55700  -19.43300 1.000 49.99000  ? 512  TYR A CD1 1 
ATOM   3866  C CD2 . TYR A 1 493 ? 20.62700  -9.13700  -21.25200 1.000 45.09000  ? 512  TYR A CD2 1 
ATOM   3867  C CE1 . TYR A 1 493 ? 23.16200  -9.72800  -20.32100 1.000 47.18000  ? 512  TYR A CE1 1 
ATOM   3868  C CE2 . TYR A 1 493 ? 21.66300  -9.30500  -22.14600 1.000 52.09000  ? 512  TYR A CE2 1 
ATOM   3869  C CZ  . TYR A 1 493 ? 22.93900  -9.59900  -21.67100 1.000 49.71000  ? 512  TYR A CZ  1 
ATOM   3870  O OH  . TYR A 1 493 ? 23.98400  -9.76500  -22.55100 1.000 48.52000  ? 512  TYR A OH  1 
ATOM   3871  N N   . CYS A 1 494 ? 18.99700  -6.30300  -20.11000 1.000 53.94000  ? 513  CYS A N   1 
ATOM   3872  C CA  . CYS A 1 494 ? 19.16900  -5.35300  -21.20400 1.000 57.10000  ? 513  CYS A CA  1 
ATOM   3873  C C   . CYS A 1 494 ? 17.80600  -4.96700  -21.76300 1.000 54.99000  ? 513  CYS A C   1 
ATOM   3874  O O   . CYS A 1 494 ? 17.02900  -5.84100  -22.16600 1.000 53.18000  ? 513  CYS A O   1 
ATOM   3875  C CB  . CYS A 1 494 ? 20.05300  -5.95200  -22.30100 1.000 46.78000  ? 513  CYS A CB  1 
ATOM   3876  S SG  . CYS A 1 494 ? 20.28400  -4.93100  -23.76400 1.000 57.02000  ? 513  CYS A SG  1 
ATOM   3877  N N   . GLU A 1 495 ? 17.50200  -3.67300  -21.79800 1.000 56.94000  ? 514  GLU A N   1 
ATOM   3878  C CA  . GLU A 1 495 ? 16.19300  -3.21700  -22.24700 1.000 63.32000  ? 514  GLU A CA  1 
ATOM   3879  C C   . GLU A 1 495 ? 16.13700  -2.87900  -23.73300 1.000 54.95000  ? 514  GLU A C   1 
ATOM   3880  O O   . GLU A 1 495 ? 15.08400  -2.44800  -24.21600 1.000 53.95000  ? 514  GLU A O   1 
ATOM   3881  C CB  . GLU A 1 495 ? 15.72400  -2.02100  -21.39300 1.000 66.13000  ? 514  GLU A CB  1 
ATOM   3882  C CG  . GLU A 1 495 ? 16.72700  -0.88700  -21.18300 1.000 71.90000  ? 514  GLU A CG  1 
ATOM   3883  C CD  . GLU A 1 495 ? 17.46700  -1.01800  -19.85100 1.000 84.96000  ? 514  GLU A CD  1 
ATOM   3884  O OE1 . GLU A 1 495 ? 17.39600  -2.10500  -19.23300 1.000 83.20000  ? 514  GLU A OE1 1 
ATOM   3885  O OE2 . GLU A 1 495 ? 18.10800  -0.03400  -19.41500 1.000 86.21000  ? 514  GLU A OE2 1 
ATOM   3886  N N   . ILE A 1 496 ? 17.22100  -3.09100  -24.46900 1.000 51.00000  ? 515  ILE A N   1 
ATOM   3887  C CA  . ILE A 1 496 ? 17.16500  -2.90400  -25.92000 1.000 50.12000  ? 515  ILE A CA  1 
ATOM   3888  C C   . ILE A 1 496 ? 16.16800  -3.89400  -26.50500 1.000 54.96000  ? 515  ILE A C   1 
ATOM   3889  O O   . ILE A 1 496 ? 16.23400  -5.09700  -26.18100 1.000 56.30000  ? 515  ILE A O   1 
ATOM   3890  C CB  . ILE A 1 496 ? 18.55900  -3.08900  -26.54500 1.000 54.67000  ? 515  ILE A CB  1 
ATOM   3891  C CG1 . ILE A 1 496 ? 19.51400  -2.00200  -26.05700 1.000 51.24000  ? 515  ILE A CG1 1 
ATOM   3892  C CG2 . ILE A 1 496 ? 18.48100  -3.08400  -28.06900 1.000 50.08000  ? 515  ILE A CG2 1 
ATOM   3893  C CD1 . ILE A 1 496 ? 20.95100  -2.26300  -26.42700 1.000 54.77000  ? 515  ILE A CD1 1 
ATOM   3894  N N   . PRO A 1 497 ? 15.22300  -3.45100  -27.33800 1.000 56.63000  ? 516  PRO A N   1 
ATOM   3895  C CA  . PRO A 1 497 ? 14.17200  -4.35900  -27.82000 1.000 53.42000  ? 516  PRO A CA  1 
ATOM   3896  C C   . PRO A 1 497 ? 14.75800  -5.50200  -28.63400 1.000 55.67000  ? 516  PRO A C   1 
ATOM   3897  O O   . PRO A 1 497 ? 15.68100  -5.31200  -29.42800 1.000 55.32000  ? 516  PRO A O   1 
ATOM   3898  C CB  . PRO A 1 497 ? 13.29100  -3.45200  -28.68800 1.000 52.36000  ? 516  PRO A CB  1 
ATOM   3899  C CG  . PRO A 1 497 ? 13.61500  -2.04500  -28.24200 1.000 53.38000  ? 516  PRO A CG  1 
ATOM   3900  C CD  . PRO A 1 497 ? 15.06400  -2.08600  -27.86800 1.000 52.34000  ? 516  PRO A CD  1 
ATOM   3901  N N   . LEU A 1 498 ? 14.20200  -6.69300  -28.43600 1.000 52.01000  ? 517  LEU A N   1 
ATOM   3902  C CA  . LEU A 1 498 ? 14.67900  -7.86500  -29.16000 1.000 52.75000  ? 517  LEU A CA  1 
ATOM   3903  C C   . LEU A 1 498 ? 14.33300  -7.75800  -30.64200 1.000 47.42000  ? 517  LEU A C   1 
ATOM   3904  O O   . LEU A 1 498 ? 13.26200  -7.26400  -30.99300 1.000 52.01000  ? 517  LEU A O   1 
ATOM   3905  C CB  . LEU A 1 498 ? 14.08800  -9.14300  -28.57400 1.000 52.69000  ? 517  LEU A CB  1 
ATOM   3906  C CG  . LEU A 1 498 ? 14.73800  -9.60200  -27.27100 1.000 45.79000  ? 517  LEU A CG  1 
ATOM   3907  C CD1 . LEU A 1 498 ? 13.93500  -10.71600 -26.65700 1.000 48.51000  ? 517  LEU A CD1 1 
ATOM   3908  C CD2 . LEU A 1 498 ? 16.13500  -10.09000 -27.57700 1.000 45.19000  ? 517  LEU A CD2 1 
ATOM   3909  N N   . PRO A 1 499 ? 15.22500  -8.20900  -31.53200 1.000 52.15000  ? 518  PRO A N   1 
ATOM   3910  C CA  . PRO A 1 499 ? 15.00700  -8.15200  -32.99900 1.000 46.48000  ? 518  PRO A CA  1 
ATOM   3911  C C   . PRO A 1 499 ? 14.08000  -9.25600  -33.49400 1.000 50.23000  ? 518  PRO A C   1 
ATOM   3912  O O   . PRO A 1 499 ? 14.47900  -10.18800 -34.20000 1.000 47.46000  ? 518  PRO A O   1 
ATOM   3913  C CB  . PRO A 1 499 ? 16.43100  -8.29900  -33.54700 1.000 51.66000  ? 518  PRO A CB  1 
ATOM   3914  C CG  . PRO A 1 499 ? 17.15000  -9.10800  -32.50400 1.000 52.06000  ? 518  PRO A CG  1 
ATOM   3915  C CD  . PRO A 1 499 ? 16.57600  -8.69200  -31.18000 1.000 49.89000  ? 518  PRO A CD  1 
ATOM   3916  N N   . ILE A 1 500 ? 12.80700  -9.14200  -33.14100 1.000 50.26000  ? 519  ILE A N   1 
ATOM   3917  C CA  . ILE A 1 500 ? 11.83400  -10.20600 -33.35900 1.000 46.38000  ? 519  ILE A CA  1 
ATOM   3918  C C   . ILE A 1 500 ? 11.14100  -9.99900  -34.70200 1.000 58.21000  ? 519  ILE A C   1 
ATOM   3919  O O   . ILE A 1 500 ? 10.69400  -8.89000  -35.01600 1.000 57.26000  ? 519  ILE A O   1 
ATOM   3920  C CB  . ILE A 1 500 ? 10.81900  -10.24000 -32.20300 1.000 52.96000  ? 519  ILE A CB  1 
ATOM   3921  C CG1 . ILE A 1 500 ? 11.54300  -10.55500 -30.88400 1.000 49.29000  ? 519  ILE A CG1 1 
ATOM   3922  C CG2 . ILE A 1 500 ? 9.69400   -11.22800 -32.49200 1.000 48.33000  ? 519  ILE A CG2 1 
ATOM   3923  C CD1 . ILE A 1 500 ? 10.72600  -10.27600 -29.63900 1.000 46.35000  ? 519  ILE A CD1 1 
ATOM   3924  N N   . ILE A 1 501 ? 11.06600  -11.06200 -35.50200 1.000 57.80000  ? 520  ILE A N   1 
ATOM   3925  C CA  . ILE A 1 501 ? 10.31700  -11.05800 -36.75600 1.000 55.47000  ? 520  ILE A CA  1 
ATOM   3926  C C   . ILE A 1 501 ? 8.94800   -11.65300 -36.48000 1.000 55.79000  ? 520  ILE A C   1 
ATOM   3927  O O   . ILE A 1 501 ? 8.82200   -12.79800 -36.04000 1.000 57.34000  ? 520  ILE A O   1 
ATOM   3928  C CB  . ILE A 1 501 ? 11.03700  -11.81100 -37.88100 1.000 57.39000  ? 520  ILE A CB  1 
ATOM   3929  C CG1 . ILE A 1 501 ? 12.27800  -11.05200 -38.34000 1.000 54.02000  ? 520  ILE A CG1 1 
ATOM   3930  C CG2 . ILE A 1 501 ? 10.07600  -12.03900 -39.03800 1.000 56.75000  ? 520  ILE A CG2 1 
ATOM   3931  C CD1 . ILE A 1 501 ? 13.13100  -11.85300 -39.29100 1.000 54.00000  ? 520  ILE A CD1 1 
ATOM   3932  N N   . LYS A 1 502 ? 7.92900   -10.85400 -36.74200 1.000 65.05000  ? 521  LYS A N   1 
ATOM   3933  C CA  . LYS A 1 502 ? 6.55300   -11.11900 -36.36000 1.000 62.36000  ? 521  LYS A CA  1 
ATOM   3934  C C   . LYS A 1 502 ? 5.75100   -11.34400 -37.63700 1.000 59.26000  ? 521  LYS A C   1 
ATOM   3935  O O   . LYS A 1 502 ? 5.87200   -10.57000 -38.59100 1.000 56.14000  ? 521  LYS A O   1 
ATOM   3936  C CB  . LYS A 1 502 ? 6.05800   -9.91700  -35.54800 1.000 67.99000  ? 521  LYS A CB  1 
ATOM   3937  C CG  . LYS A 1 502 ? 4.79600   -10.01500 -34.75500 1.000 70.71000  ? 521  LYS A CG  1 
ATOM   3938  C CD  . LYS A 1 502 ? 4.69800   -8.67500  -34.05300 1.000 74.26000  ? 521  LYS A CD  1 
ATOM   3939  C CE  . LYS A 1 502 ? 3.46700   -8.53200  -33.22400 1.000 74.52000  ? 521  LYS A CE  1 
ATOM   3940  N NZ  . LYS A 1 502 ? 3.27400   -7.09200  -32.92000 1.000 79.73000  ? 521  LYS A NZ  1 
ATOM   3941  N N   . SER A 1 503 ? 4.97800   -12.42200 -37.68000 1.000 68.19000  ? 522  SER A N   1 
ATOM   3942  C CA  . SER A 1 503 ? 4.36500   -12.84900 -38.93200 1.000 78.05000  ? 522  SER A CA  1 
ATOM   3943  C C   . SER A 1 503 ? 2.98500   -12.21800 -39.10900 1.000 80.02000  ? 522  SER A C   1 
ATOM   3944  O O   . SER A 1 503 ? 2.21500   -12.10500 -38.14800 1.000 78.85000  ? 522  SER A O   1 
ATOM   3945  C CB  . SER A 1 503 ? 4.24400   -14.37200 -38.99000 1.000 67.94000  ? 522  SER A CB  1 
ATOM   3946  O OG  . SER A 1 503 ? 3.25500   -14.83000 -38.08400 1.000 62.73000  ? 522  SER A OG  1 
ATOM   3947  N N   . LYS A 1 504 ? 2.67800   -11.81300 -40.34600 1.000 83.72000  ? 523  LYS A N   1 
ATOM   3948  C CA  . LYS A 1 504 ? 1.36900   -11.25100 -40.69200 1.000 96.59000  ? 523  LYS A CA  1 
ATOM   3949  C C   . LYS A 1 504 ? 1.10700   -9.99500  -39.85300 1.000 98.86000  ? 523  LYS A C   1 
ATOM   3950  O O   . LYS A 1 504 ? 0.12800   -9.27600  -40.05000 1.000 94.59000  ? 523  LYS A O   1 
ATOM   3951  C CB  . LYS A 1 504 ? 0.26700   -12.31300 -40.48600 1.000 91.71000  ? 523  LYS A CB  1 
ATOM   3952  C CG  . LYS A 1 504 ? -1.19400  -11.89500 -40.70900 1.000 102.37000 ? 523  LYS A CG  1 
ATOM   3953  C CD  . LYS A 1 504 ? -1.57800  -11.66400 -42.16600 1.000 101.89000 ? 523  LYS A CD  1 
ATOM   3954  C CE  . LYS A 1 504 ? -3.09300  -11.49400 -42.29300 1.000 99.88000  ? 523  LYS A CE  1 
ATOM   3955  N NZ  . LYS A 1 504 ? -3.59200  -10.27200 -41.59700 1.000 99.40000  ? 523  LYS A NZ  1 
ATOM   3956  N N   . LYS B 1 2   ? 26.70000  -47.11400 -7.15800  1.000 79.75000  ? 21   LYS B N   1 
ATOM   3957  C CA  . LYS B 1 2   ? 27.36800  -48.29500 -7.70500  1.000 80.47000  ? 21   LYS B CA  1 
ATOM   3958  C C   . LYS B 1 2   ? 28.81500  -48.42800 -7.25500  1.000 72.32000  ? 21   LYS B C   1 
ATOM   3959  O O   . LYS B 1 2   ? 29.29200  -49.53300 -7.01700  1.000 76.43000  ? 21   LYS B O   1 
ATOM   3960  C CB  . LYS B 1 2   ? 27.30500  -48.29100 -9.23200  1.000 78.56000  ? 21   LYS B CB  1 
ATOM   3961  C CG  . LYS B 1 2   ? 25.91500  -48.52200 -9.76800  1.000 85.99000  ? 21   LYS B CG  1 
ATOM   3962  C CD  . LYS B 1 2   ? 25.45300  -49.92100 -9.37500  1.000 100.20000 ? 21   LYS B CD  1 
ATOM   3963  C CE  . LYS B 1 2   ? 24.06700  -50.24700 -9.91700  1.000 96.44000  ? 21   LYS B CE  1 
ATOM   3964  N NZ  . LYS B 1 2   ? 23.59900  -51.58600 -9.45000  1.000 86.76000  ? 21   LYS B NZ  1 
ATOM   3965  N N   . ILE B 1 3   ? 29.52000  -47.30500 -7.14200  1.000 68.24000  ? 22   ILE B N   1 
ATOM   3966  C CA  . ILE B 1 3   ? 30.91200  -47.34600 -6.71000  1.000 73.23000  ? 22   ILE B CA  1 
ATOM   3967  C C   . ILE B 1 3   ? 30.96700  -47.67100 -5.22200  1.000 69.68000  ? 22   ILE B C   1 
ATOM   3968  O O   . ILE B 1 3   ? 30.31000  -47.02000 -4.40100  1.000 71.07000  ? 22   ILE B O   1 
ATOM   3969  C CB  . ILE B 1 3   ? 31.61400  -46.02200 -7.05200  1.000 67.80000  ? 22   ILE B CB  1 
ATOM   3970  C CG1 . ILE B 1 3   ? 31.66700  -45.87300 -8.57600  1.000 66.91000  ? 22   ILE B CG1 1 
ATOM   3971  C CG2 . ILE B 1 3   ? 33.00200  -45.95900 -6.40700  1.000 58.77000  ? 22   ILE B CG2 1 
ATOM   3972  C CD1 . ILE B 1 3   ? 31.91300  -44.46700 -9.06700  1.000 59.26000  ? 22   ILE B CD1 1 
ATOM   3973  N N   . GLU B 1 4   ? 31.74300  -48.69500 -4.87500  1.000 62.06000  ? 23   GLU B N   1 
ATOM   3974  C CA  . GLU B 1 4   ? 31.75800  -49.21900 -3.51900  1.000 58.36000  ? 23   GLU B CA  1 
ATOM   3975  C C   . GLU B 1 4   ? 32.47500  -48.26500 -2.56900  1.000 61.92000  ? 23   GLU B C   1 
ATOM   3976  O O   . GLU B 1 4   ? 33.60300  -47.83600 -2.82600  1.000 66.50000  ? 23   GLU B O   1 
ATOM   3977  C CB  . GLU B 1 4   ? 32.41400  -50.59600 -3.51800  1.000 62.61000  ? 23   GLU B CB  1 
ATOM   3978  C CG  . GLU B 1 4   ? 32.57000  -51.23500 -2.15000  1.000 66.55000  ? 23   GLU B CG  1 
ATOM   3979  C CD  . GLU B 1 4   ? 33.06200  -52.66800 -2.24100  1.000 78.58000  ? 23   GLU B CD  1 
ATOM   3980  O OE1 . GLU B 1 4   ? 33.12900  -53.20200 -3.37400  1.000 75.25000  ? 23   GLU B OE1 1 
ATOM   3981  O OE2 . GLU B 1 4   ? 33.41900  -53.24500 -1.18700  1.000 76.21000  ? 23   GLU B OE2 1 
ATOM   3982  N N   . GLU B 1 5   ? 31.81600  -47.95000 -1.45900  1.000 58.68000  ? 24   GLU B N   1 
ATOM   3983  C CA  . GLU B 1 5   ? 32.33700  -47.01000 -0.48100  1.000 57.25000  ? 24   GLU B CA  1 
ATOM   3984  C C   . GLU B 1 5   ? 33.38000  -47.68000 0.40100   1.000 59.12000  ? 24   GLU B C   1 
ATOM   3985  O O   . GLU B 1 5   ? 33.31700  -48.88700 0.66500   1.000 58.89000  ? 24   GLU B O   1 
ATOM   3986  C CB  . GLU B 1 5   ? 31.22200  -46.51000 0.42800   1.000 62.18000  ? 24   GLU B CB  1 
ATOM   3987  C CG  . GLU B 1 5   ? 31.50900  -45.22500 1.16200   1.000 64.21000  ? 24   GLU B CG  1 
ATOM   3988  C CD  . GLU B 1 5   ? 30.73700  -45.15800 2.45900   1.000 84.67000  ? 24   GLU B CD  1 
ATOM   3989  O OE1 . GLU B 1 5   ? 30.47700  -46.24200 3.03200   1.000 88.51000  ? 24   GLU B OE1 1 
ATOM   3990  O OE2 . GLU B 1 5   ? 30.30200  -44.05400 2.85200   1.000 88.69000  ? 24   GLU B OE2 1 
ATOM   3991  N N   . GLY B 1 6   ? 34.30900  -46.87200 0.90600   1.000 53.32000  ? 25   GLY B N   1 
ATOM   3992  C CA  . GLY B 1 6   ? 35.35400  -47.36700 1.77000   1.000 49.46000  ? 25   GLY B CA  1 
ATOM   3993  C C   . GLY B 1 6   ? 36.50400  -48.03000 1.05600   1.000 51.15000  ? 25   GLY B C   1 
ATOM   3994  O O   . GLY B 1 6   ? 37.34000  -48.66200 1.70500   1.000 51.72000  ? 25   GLY B O   1 
ATOM   3995  N N   . LYS B 1 7   ? 36.55300  -47.94500 -0.25900  1.000 54.37000  ? 26   LYS B N   1 
ATOM   3996  C CA  . LYS B 1 7   ? 37.56800  -48.62600 -1.03600  1.000 52.53000  ? 26   LYS B CA  1 
ATOM   3997  C C   . LYS B 1 7   ? 37.93100  -47.70100 -2.19100  1.000 54.18000  ? 26   LYS B C   1 
ATOM   3998  O O   . LYS B 1 7   ? 37.16800  -46.79300 -2.53300  1.000 52.37000  ? 26   LYS B O   1 
ATOM   3999  C CB  . LYS B 1 7   ? 37.06000  -50.02800 -1.47000  1.000 56.86000  ? 26   LYS B CB  1 
ATOM   4000  C CG  . LYS B 1 7   ? 38.04900  -50.83400 -2.33100  1.000 72.60000  ? 26   LYS B CG  1 
ATOM   4001  C CD  . LYS B 1 7   ? 37.65000  -52.26500 -2.86700  1.000 75.58000  ? 26   LYS B CD  1 
ATOM   4002  C CE  . LYS B 1 7   ? 37.79400  -53.47300 -1.90500  1.000 78.62000  ? 26   LYS B CE  1 
ATOM   4003  N NZ  . LYS B 1 7   ? 37.91000  -54.66100 -2.83300  1.000 72.01000  ? 26   LYS B NZ  1 
ATOM   4004  N N   . LEU B 1 8   ? 39.12600  -47.88000 -2.75400  1.000 48.93000  ? 27   LEU B N   1 
ATOM   4005  C CA  . LEU B 1 8   ? 39.57100  -47.06600 -3.87900  1.000 46.17000  ? 27   LEU B CA  1 
ATOM   4006  C C   . LEU B 1 8   ? 39.91100  -47.94600 -5.06700  1.000 44.46000  ? 27   LEU B C   1 
ATOM   4007  O O   . LEU B 1 8   ? 40.70500  -48.88500 -4.94900  1.000 46.71000  ? 27   LEU B O   1 
ATOM   4008  C CB  . LEU B 1 8   ? 40.78900  -46.19800 -3.54200  1.000 49.22000  ? 27   LEU B CB  1 
ATOM   4009  C CG  . LEU B 1 8   ? 40.65600  -44.92500 -2.71200  1.000 48.71000  ? 27   LEU B CG  1 
ATOM   4010  C CD1 . LEU B 1 8   ? 42.02600  -44.27200 -2.57200  1.000 40.44000  ? 27   LEU B CD1 1 
ATOM   4011  C CD2 . LEU B 1 8   ? 39.67000  -43.94700 -3.32100  1.000 38.10000  ? 27   LEU B CD2 1 
ATOM   4012  N N   . VAL B 1 9   ? 39.31600  -47.61300 -6.20700  1.000 46.29000  ? 28   VAL B N   1 
ATOM   4013  C CA  . VAL B 1 9   ? 39.56600  -48.25400 -7.49100  1.000 42.84000  ? 28   VAL B CA  1 
ATOM   4014  C C   . VAL B 1 9   ? 40.23800  -47.22500 -8.39100  1.000 43.65000  ? 28   VAL B C   1 
ATOM   4015  O O   . VAL B 1 9   ? 39.70700  -46.12400 -8.58400  1.000 40.68000  ? 28   VAL B O   1 
ATOM   4016  C CB  . VAL B 1 9   ? 38.25800  -48.76400 -8.12400  1.000 39.63000  ? 28   VAL B CB  1 
ATOM   4017  C CG1 . VAL B 1 9   ? 38.52900  -49.43400 -9.44500  1.000 44.79000  ? 28   VAL B CG1 1 
ATOM   4018  C CG2 . VAL B 1 9   ? 37.53100  -49.70500 -7.18300  1.000 37.40000  ? 28   VAL B CG2 1 
ATOM   4019  N N   . ILE B 1 10  ? 41.40100  -47.57300 -8.93800  1.000 44.09000  ? 29   ILE B N   1 
ATOM   4020  C CA  . ILE B 1 10  ? 42.18500  -46.65000 -9.74900  1.000 36.93000  ? 29   ILE B CA  1 
ATOM   4021  C C   . ILE B 1 10  ? 42.34100  -47.22200 -11.15000 1.000 41.02000  ? 29   ILE B C   1 
ATOM   4022  O O   . ILE B 1 10  ? 42.72300  -48.38700 -11.31200 1.000 38.28000  ? 29   ILE B O   1 
ATOM   4023  C CB  . ILE B 1 10  ? 43.56200  -46.37700 -9.13000  1.000 40.72000  ? 29   ILE B CB  1 
ATOM   4024  C CG1 . ILE B 1 10  ? 43.41800  -45.78200 -7.73200  1.000 40.95000  ? 29   ILE B CG1 1 
ATOM   4025  C CG2 . ILE B 1 10  ? 44.34400  -45.41500 -10.00000 1.000 36.61000  ? 29   ILE B CG2 1 
ATOM   4026  C CD1 . ILE B 1 10  ? 44.73700  -45.63500 -7.03000  1.000 33.31000  ? 29   ILE B CD1 1 
ATOM   4027  N N   . TRP B 1 11  ? 42.05000  -46.39900 -12.15800 1.000 37.61000  ? 30   TRP B N   1 
ATOM   4028  C CA  . TRP B 1 11  ? 42.32100  -46.73500 -13.55000 1.000 34.99000  ? 30   TRP B CA  1 
ATOM   4029  C C   . TRP B 1 11  ? 43.51900  -45.94700 -14.06400 1.000 37.44000  ? 30   TRP B C   1 
ATOM   4030  O O   . TRP B 1 11  ? 43.58100  -44.72100 -13.92300 1.000 35.09000  ? 30   TRP B O   1 
ATOM   4031  C CB  . TRP B 1 11  ? 41.11500  -46.47100 -14.45100 1.000 33.77000  ? 30   TRP B CB  1 
ATOM   4032  C CG  . TRP B 1 11  ? 40.04800  -47.51200 -14.34700 1.000 45.51000  ? 30   TRP B CG  1 
ATOM   4033  C CD1 . TRP B 1 11  ? 40.03600  -48.59600 -13.51700 1.000 42.96000  ? 30   TRP B CD1 1 
ATOM   4034  C CD2 . TRP B 1 11  ? 38.87000  -47.61000 -15.15500 1.000 36.19000  ? 30   TRP B CD2 1 
ATOM   4035  N NE1 . TRP B 1 11  ? 38.90300  -49.34000 -13.73200 1.000 42.07000  ? 30   TRP B NE1 1 
ATOM   4036  C CE2 . TRP B 1 11  ? 38.17800  -48.76200 -14.74200 1.000 38.70000  ? 30   TRP B CE2 1 
ATOM   4037  C CE3 . TRP B 1 11  ? 38.33300  -46.83300 -16.18500 1.000 36.91000  ? 30   TRP B CE3 1 
ATOM   4038  C CZ2 . TRP B 1 11  ? 36.97500  -49.15500 -15.32200 1.000 35.99000  ? 30   TRP B CZ2 1 
ATOM   4039  C CZ3 . TRP B 1 11  ? 37.14100  -47.22300 -16.75700 1.000 33.41000  ? 30   TRP B CZ3 1 
ATOM   4040  C CH2 . TRP B 1 11  ? 36.47400  -48.37300 -16.32500 1.000 37.54000  ? 30   TRP B CH2 1 
ATOM   4041  N N   . ILE B 1 12  ? 44.45400  -46.66500 -14.67700 1.000 36.86000  ? 31   ILE B N   1 
ATOM   4042  C CA  . ILE B 1 12  ? 45.63800  -46.08800 -15.29400 1.000 37.86000  ? 31   ILE B CA  1 
ATOM   4043  C C   . ILE B 1 12  ? 45.96200  -46.95300 -16.49800 1.000 39.04000  ? 31   ILE B C   1 
ATOM   4044  O O   . ILE B 1 12  ? 45.62300  -48.13800 -16.53100 1.000 41.76000  ? 31   ILE B O   1 
ATOM   4045  C CB  . ILE B 1 12  ? 46.81700  -46.02600 -14.29800 1.000 39.37000  ? 31   ILE B CB  1 
ATOM   4046  C CG1 . ILE B 1 12  ? 48.02000  -45.30400 -14.91300 1.000 38.18000  ? 31   ILE B CG1 1 
ATOM   4047  C CG2 . ILE B 1 12  ? 47.18500  -47.42800 -13.82000 1.000 34.28000  ? 31   ILE B CG2 1 
ATOM   4048  C CD1 . ILE B 1 12  ? 49.10000  -44.94600 -13.89900 1.000 29.41000  ? 31   ILE B CD1 1 
ATOM   4049  N N   . ASN B 1 13  ? 46.61200  -46.35900 -17.49600 1.000 34.78000  ? 32   ASN B N   1 
ATOM   4050  C CA  . ASN B 1 13  ? 46.87900  -47.08100 -18.73100 1.000 37.98000  ? 32   ASN B CA  1 
ATOM   4051  C C   . ASN B 1 13  ? 47.89800  -48.20100 -18.52400 1.000 44.51000  ? 32   ASN B C   1 
ATOM   4052  O O   . ASN B 1 13  ? 48.80700  -48.10800 -17.69000 1.000 37.29000  ? 32   ASN B O   1 
ATOM   4053  C CB  . ASN B 1 13  ? 47.41400  -46.14800 -19.80500 1.000 41.61000  ? 32   ASN B CB  1 
ATOM   4054  C CG  . ASN B 1 13  ? 47.34500  -46.76900 -21.17200 1.000 42.58000  ? 32   ASN B CG  1 
ATOM   4055  O OD1 . ASN B 1 13  ? 46.60000  -47.72300 -21.38300 1.000 42.50000  ? 32   ASN B OD1 1 
ATOM   4056  N ND2 . ASN B 1 13  ? 48.20400  -46.31700 -22.07600 1.000 52.16000  ? 32   ASN B ND2 1 
ATOM   4057  N N   . GLY B 1 14  ? 47.76700  -49.24500 -19.34900 1.000 41.86000  ? 33   GLY B N   1 
ATOM   4058  C CA  . GLY B 1 14  ? 48.61700  -50.42000 -19.25200 1.000 43.31000  ? 33   GLY B CA  1 
ATOM   4059  C C   . GLY B 1 14  ? 50.09700  -50.17800 -19.49700 1.000 44.74000  ? 33   GLY B C   1 
ATOM   4060  O O   . GLY B 1 14  ? 50.92100  -50.99200 -19.06800 1.000 42.25000  ? 33   GLY B O   1 
ATOM   4061  N N   . ASP B 1 15  ? 50.46600  -49.09200 -20.17400 1.000 46.97000  ? 34   ASP B N   1 
ATOM   4062  C CA  . ASP B 1 15  ? 51.88500  -48.83300 -20.41500 1.000 47.45000  ? 34   ASP B CA  1 
ATOM   4063  C C   . ASP B 1 15  ? 52.54200  -48.04000 -19.28800 1.000 48.96000  ? 34   ASP B C   1 
ATOM   4064  O O   . ASP B 1 15  ? 53.72400  -47.69200 -19.40000 1.000 54.35000  ? 34   ASP B O   1 
ATOM   4065  C CB  . ASP B 1 15  ? 52.09500  -48.10600 -21.75500 1.000 43.81000  ? 34   ASP B CB  1 
ATOM   4066  C CG  . ASP B 1 15  ? 51.52600  -46.69200 -21.76400 1.000 54.86000  ? 34   ASP B CG  1 
ATOM   4067  O OD1 . ASP B 1 15  ? 50.90500  -46.26700 -20.76100 1.000 53.44000  ? 34   ASP B OD1 1 
ATOM   4068  O OD2 . ASP B 1 15  ? 51.71700  -45.99600 -22.78500 1.000 55.74000  ? 34   ASP B OD2 1 
ATOM   4069  N N   . LYS B 1 16  ? 51.80600  -47.74700 -18.22000 1.000 41.47000  ? 35   LYS B N   1 
ATOM   4070  C CA  . LYS B 1 16  ? 52.31200  -47.00400 -17.07800 1.000 39.85000  ? 35   LYS B CA  1 
ATOM   4071  C C   . LYS B 1 16  ? 52.69400  -47.96200 -15.94900 1.000 43.95000  ? 35   LYS B C   1 
ATOM   4072  O O   . LYS B 1 16  ? 52.32900  -49.14200 -15.94900 1.000 44.91000  ? 35   LYS B O   1 
ATOM   4073  C CB  . LYS B 1 16  ? 51.26000  -45.99600 -16.60300 1.000 39.38000  ? 35   LYS B CB  1 
ATOM   4074  C CG  . LYS B 1 16  ? 50.78300  -45.00100 -17.67500 1.000 42.59000  ? 35   LYS B CG  1 
ATOM   4075  C CD  . LYS B 1 16  ? 51.85400  -43.99200 -18.04400 1.000 41.79000  ? 35   LYS B CD  1 
ATOM   4076  C CE  . LYS B 1 16  ? 51.32800  -42.91500 -18.98600 1.000 46.84000  ? 35   LYS B CE  1 
ATOM   4077  N NZ  . LYS B 1 16  ? 51.13500  -43.38300 -20.38700 1.000 48.43000  ? 35   LYS B NZ  1 
ATOM   4078  N N   . GLY B 1 17  ? 53.41800  -47.42500 -14.96200 1.000 36.46000  ? 36   GLY B N   1 
ATOM   4079  C CA  . GLY B 1 17  ? 53.88500  -48.19700 -13.81700 1.000 42.52000  ? 36   GLY B CA  1 
ATOM   4080  C C   . GLY B 1 17  ? 52.80800  -48.57000 -12.81200 1.000 45.93000  ? 36   GLY B C   1 
ATOM   4081  O O   . GLY B 1 17  ? 52.76500  -48.06400 -11.68400 1.000 43.65000  ? 36   GLY B O   1 
ATOM   4082  N N   . TYR B 1 18  ? 51.88700  -49.41600 -13.27100 1.000 44.29000  ? 37   TYR B N   1 
ATOM   4083  C CA  . TYR B 1 18  ? 50.68700  -49.82000 -12.49700 1.000 44.74000  ? 37   TYR B CA  1 
ATOM   4084  C C   . TYR B 1 18  ? 51.05000  -50.63300 -11.25600 1.000 46.06000  ? 37   TYR B C   1 
ATOM   4085  O O   . TYR B 1 18  ? 50.38600  -50.45300 -10.26000 1.000 50.50000  ? 37   TYR B O   1 
ATOM   4086  C CB  . TYR B 1 18  ? 49.61500  -50.45200 -13.39000 1.000 44.59000  ? 37   TYR B CB  1 
ATOM   4087  C CG  . TYR B 1 18  ? 50.00300  -51.68900 -14.15400 1.000 48.66000  ? 37   TYR B CG  1 
ATOM   4088  C CD1 . TYR B 1 18  ? 50.09700  -52.91700 -13.53300 1.000 48.29000  ? 37   TYR B CD1 1 
ATOM   4089  C CD2 . TYR B 1 18  ? 50.22800  -51.64300 -15.51400 1.000 48.38000  ? 37   TYR B CD2 1 
ATOM   4090  C CE1 . TYR B 1 18  ? 50.44500  -54.05500 -14.22900 1.000 49.82000  ? 37   TYR B CE1 1 
ATOM   4091  C CE2 . TYR B 1 18  ? 50.57800  -52.77000 -16.22700 1.000 42.80000  ? 37   TYR B CE2 1 
ATOM   4092  C CZ  . TYR B 1 18  ? 50.68200  -53.98000 -15.58200 1.000 44.27000  ? 37   TYR B CZ  1 
ATOM   4093  O OH  . TYR B 1 18  ? 51.02800  -55.09700 -16.27000 1.000 52.18000  ? 37   TYR B OH  1 
ATOM   4094  N N   . ASN B 1 19  ? 52.03000  -51.52300 -11.35000 1.000 42.67000  ? 38   ASN B N   1 
ATOM   4095  C CA  . ASN B 1 19  ? 52.47200  -52.30600 -10.19800 1.000 48.85000  ? 38   ASN B CA  1 
ATOM   4096  C C   . ASN B 1 19  ? 53.06100  -51.40500 -9.12300  1.000 48.48000  ? 38   ASN B C   1 
ATOM   4097  O O   . ASN B 1 19  ? 52.78600  -51.58500 -7.93200  1.000 45.00000  ? 38   ASN B O   1 
ATOM   4098  C CB  . ASN B 1 19  ? 53.50800  -53.35500 -10.62000 1.000 45.23000  ? 38   ASN B CB  1 
ATOM   4099  C CG  . ASN B 1 19  ? 52.90000  -54.51200 -11.38100 1.000 52.61000  ? 38   ASN B CG  1 
ATOM   4100  O OD1 . ASN B 1 19  ? 51.82100  -55.00200 -11.04000 1.000 53.04000  ? 38   ASN B OD1 1 
ATOM   4101  N ND2 . ASN B 1 19  ? 53.59700  -54.96600 -12.41700 1.000 57.23000  ? 38   ASN B ND2 1 
ATOM   4102  N N   . GLY B 1 20  ? 53.89800  -50.44500 -9.52900  1.000 44.95000  ? 39   GLY B N   1 
ATOM   4103  C CA  . GLY B 1 20  ? 54.43200  -49.48800 -8.57700  1.000 38.92000  ? 39   GLY B CA  1 
ATOM   4104  C C   . GLY B 1 20  ? 53.34500  -48.67400 -7.90200  1.000 45.62000  ? 39   GLY B C   1 
ATOM   4105  O O   . GLY B 1 20  ? 53.39100  -48.44500 -6.69300  1.000 52.49000  ? 39   GLY B O   1 
ATOM   4106  N N   . LEU B 1 21  ? 52.34700  -48.23400 -8.67100  1.000 39.53000  ? 40   LEU B N   1 
ATOM   4107  C CA  . LEU B 1 21  ? 51.23200  -47.50600 -8.07800  1.000 39.93000  ? 40   LEU B CA  1 
ATOM   4108  C C   . LEU B 1 21  ? 50.47200  -48.38300 -7.08600  1.000 45.66000  ? 40   LEU B C   1 
ATOM   4109  O O   . LEU B 1 21  ? 50.04200  -47.91200 -6.02100  1.000 37.89000  ? 40   LEU B O   1 
ATOM   4110  C CB  . LEU B 1 21  ? 50.30500  -46.99500 -9.18000  1.000 37.57000  ? 40   LEU B CB  1 
ATOM   4111  C CG  . LEU B 1 21  ? 49.07700  -46.17600 -8.77700  1.000 31.86000  ? 40   LEU B CG  1 
ATOM   4112  C CD1 . LEU B 1 21  ? 49.48800  -44.91800 -8.03600  1.000 27.73000  ? 40   LEU B CD1 1 
ATOM   4113  C CD2 . LEU B 1 21  ? 48.27000  -45.83400 -10.03200 1.000 27.93000  ? 40   LEU B CD2 1 
ATOM   4114  N N   . ALA B 1 22  ? 50.31600  -49.66900 -7.40900  1.000 40.07000  ? 41   ALA B N   1 
ATOM   4115  C CA  . ALA B 1 22  ? 49.63900  -50.57100 -6.48900  1.000 41.56000  ? 41   ALA B CA  1 
ATOM   4116  C C   . ALA B 1 22  ? 50.38700  -50.69500 -5.17100  1.000 45.37000  ? 41   ALA B C   1 
ATOM   4117  O O   . ALA B 1 22  ? 49.75800  -50.86400 -4.11900  1.000 43.80000  ? 41   ALA B O   1 
ATOM   4118  C CB  . ALA B 1 22  ? 49.46600  -51.94700 -7.12400  1.000 39.58000  ? 41   ALA B CB  1 
ATOM   4119  N N   . GLU B 1 23  ? 51.72200  -50.62100 -5.19200  1.000 46.37000  ? 42   GLU B N   1 
ATOM   4120  C CA  . GLU B 1 23  ? 52.42600  -50.75400 -3.92300  1.000 50.42000  ? 42   GLU B CA  1 
ATOM   4121  C C   . GLU B 1 23  ? 52.32900  -49.47100 -3.09800  1.000 44.24000  ? 42   GLU B C   1 
ATOM   4122  O O   . GLU B 1 23  ? 52.36300  -49.53400 -1.86400  1.000 45.95000  ? 42   GLU B O   1 
ATOM   4123  C CB  . GLU B 1 23  ? 53.87800  -51.19200 -4.15100  1.000 45.87000  ? 42   GLU B CB  1 
ATOM   4124  C CG  . GLU B 1 23  ? 54.86800  -50.15800 -4.60200  1.000 54.36000  ? 42   GLU B CG  1 
ATOM   4125  C CD  . GLU B 1 23  ? 56.19700  -50.80200 -4.96900  1.000 70.00000  ? 42   GLU B CD  1 
ATOM   4126  O OE1 . GLU B 1 23  ? 56.25400  -52.05300 -4.99400  1.000 74.10000  ? 42   GLU B OE1 1 
ATOM   4127  O OE2 . GLU B 1 23  ? 57.18300  -50.07400 -5.21600  1.000 72.61000  ? 42   GLU B OE2 1 
ATOM   4128  N N   . VAL B 1 24  ? 52.16000  -48.31200 -3.74300  1.000 43.20000  ? 43   VAL B N   1 
ATOM   4129  C CA  . VAL B 1 24  ? 51.75800  -47.12600 -2.99000  1.000 46.10000  ? 43   VAL B CA  1 
ATOM   4130  C C   . VAL B 1 24  ? 50.38800  -47.35500 -2.35800  1.000 47.39000  ? 43   VAL B C   1 
ATOM   4131  O O   . VAL B 1 24  ? 50.11600  -46.87700 -1.24600  1.000 47.18000  ? 43   VAL B O   1 
ATOM   4132  C CB  . VAL B 1 24  ? 51.76900  -45.87200 -3.88800  1.000 40.76000  ? 43   VAL B CB  1 
ATOM   4133  C CG1 . VAL B 1 24  ? 51.35300  -44.63800 -3.09600  1.000 40.75000  ? 43   VAL B CG1 1 
ATOM   4134  C CG2 . VAL B 1 24  ? 53.13200  -45.66000 -4.48200  1.000 36.65000  ? 43   VAL B CG2 1 
ATOM   4135  N N   . GLY B 1 25  ? 49.51200  -48.10100 -3.04300  1.000 45.55000  ? 44   GLY B N   1 
ATOM   4136  C CA  . GLY B 1 25  ? 48.22900  -48.45400 -2.45200  1.000 44.87000  ? 44   GLY B CA  1 
ATOM   4137  C C   . GLY B 1 25  ? 48.37000  -49.30100 -1.20100  1.000 47.56000  ? 44   GLY B C   1 
ATOM   4138  O O   . GLY B 1 25  ? 47.62800  -49.12300 -0.23000  1.000 46.41000  ? 44   GLY B O   1 
ATOM   4139  N N   . LYS B 1 26  ? 49.32600  -50.23100 -1.20100  1.000 43.69000  ? 45   LYS B N   1 
ATOM   4140  C CA  . LYS B 1 26  ? 49.49800  -51.07900 -0.03500  1.000 48.38000  ? 45   LYS B CA  1 
ATOM   4141  C C   . LYS B 1 26  ? 50.04500  -50.27800 1.13600   1.000 50.94000  ? 45   LYS B C   1 
ATOM   4142  O O   . LYS B 1 26  ? 49.67000  -50.51900 2.28300   1.000 56.64000  ? 45   LYS B O   1 
ATOM   4143  C CB  . LYS B 1 26  ? 50.41000  -52.24400 -0.39700  1.000 44.02000  ? 45   LYS B CB  1 
ATOM   4144  C CG  . LYS B 1 26  ? 50.06800  -52.84300 -1.77700  1.000 64.11000  ? 45   LYS B CG  1 
ATOM   4145  C CD  . LYS B 1 26  ? 50.67300  -54.27100 -1.91400  1.000 68.91000  ? 45   LYS B CD  1 
ATOM   4146  C CE  . LYS B 1 26  ? 50.55500  -54.91100 -3.34400  1.000 64.57000  ? 45   LYS B CE  1 
ATOM   4147  N NZ  . LYS B 1 26  ? 51.34700  -54.10800 -4.37700  1.000 67.60000  ? 45   LYS B NZ  1 
ATOM   4148  N N   . LYS B 1 27  ? 50.90200  -49.29600 0.85600   1.000 49.84000  ? 46   LYS B N   1 
ATOM   4149  C CA  . LYS B 1 27  ? 51.28900  -48.34200 1.88400   1.000 50.88000  ? 46   LYS B CA  1 
ATOM   4150  C C   . LYS B 1 27  ? 50.06800  -47.59500 2.40600   1.000 54.58000  ? 46   LYS B C   1 
ATOM   4151  O O   . LYS B 1 27  ? 49.97600  -47.29200 3.60300   1.000 58.70000  ? 46   LYS B O   1 
ATOM   4152  C CB  . LYS B 1 27  ? 52.31700  -47.36300 1.31700   1.000 52.96000  ? 46   LYS B CB  1 
ATOM   4153  C CG  . LYS B 1 27  ? 52.87100  -46.37500 2.32000   1.000 58.69000  ? 46   LYS B CG  1 
ATOM   4154  C CD  . LYS B 1 27  ? 53.90200  -45.47700 1.65100   1.000 67.55000  ? 46   LYS B CD  1 
ATOM   4155  C CE  . LYS B 1 27  ? 54.53500  -44.53300 2.65700   1.000 74.05000  ? 46   LYS B CE  1 
ATOM   4156  N NZ  . LYS B 1 27  ? 53.55200  -43.53400 3.16500   1.000 81.33000  ? 46   LYS B NZ  1 
ATOM   4157  N N   . PHE B 1 28  ? 49.11400  -47.29300 1.52300   1.000 52.40000  ? 47   PHE B N   1 
ATOM   4158  C CA  . PHE B 1 28  ? 47.90900  -46.57900 1.93700   1.000 48.59000  ? 47   PHE B CA  1 
ATOM   4159  C C   . PHE B 1 28  ? 46.99200  -47.47200 2.77200   1.000 52.66000  ? 47   PHE B C   1 
ATOM   4160  O O   . PHE B 1 28  ? 46.38100  -47.00800 3.74100   1.000 49.79000  ? 47   PHE B O   1 
ATOM   4161  C CB  . PHE B 1 28  ? 47.18600  -46.05200 0.69700   1.000 42.25000  ? 47   PHE B CB  1 
ATOM   4162  C CG  . PHE B 1 28  ? 46.00700  -45.18500 0.99900   1.000 40.06000  ? 47   PHE B CG  1 
ATOM   4163  C CD1 . PHE B 1 28  ? 46.18200  -43.86900 1.38100   1.000 40.12000  ? 47   PHE B CD1 1 
ATOM   4164  C CD2 . PHE B 1 28  ? 44.71600  -45.68500 0.90100   1.000 44.20000  ? 47   PHE B CD2 1 
ATOM   4165  C CE1 . PHE B 1 28  ? 45.09400  -43.05100 1.66700   1.000 44.53000  ? 47   PHE B CE1 1 
ATOM   4166  C CE2 . PHE B 1 28  ? 43.61100  -44.87600 1.18500   1.000 47.26000  ? 47   PHE B CE2 1 
ATOM   4167  C CZ  . PHE B 1 28  ? 43.80600  -43.55600 1.56900   1.000 48.72000  ? 47   PHE B CZ  1 
ATOM   4168  N N   . GLU B 1 29  ? 46.85400  -48.74400 2.38800   1.000 54.42000  ? 48   GLU B N   1 
ATOM   4169  C CA  . GLU B 1 29  ? 46.06800  -49.68800 3.18100   1.000 52.93000  ? 48   GLU B CA  1 
ATOM   4170  C C   . GLU B 1 29  ? 46.71400  -49.92500 4.53600   1.000 58.66000  ? 48   GLU B C   1 
ATOM   4171  O O   . GLU B 1 29  ? 46.04200  -49.93500 5.57700   1.000 51.07000  ? 48   GLU B O   1 
ATOM   4172  C CB  . GLU B 1 29  ? 45.94100  -51.00800 2.43000   1.000 51.34000  ? 48   GLU B CB  1 
ATOM   4173  C CG  . GLU B 1 29  ? 45.16300  -52.06200 3.18100   1.000 59.28000  ? 48   GLU B CG  1 
ATOM   4174  C CD  . GLU B 1 29  ? 45.13400  -53.38900 2.45000   1.000 59.98000  ? 48   GLU B CD  1 
ATOM   4175  O OE1 . GLU B 1 29  ? 45.74500  -53.48300 1.36600   1.000 57.52000  ? 48   GLU B OE1 1 
ATOM   4176  O OE2 . GLU B 1 29  ? 44.51400  -54.34400 2.96300   1.000 68.71000  ? 48   GLU B OE2 1 
ATOM   4177  N N   . LYS B 1 30  ? 48.03400  -50.11600 4.52800   1.000 56.18000  ? 49   LYS B N   1 
ATOM   4178  C CA  . LYS B 1 30  ? 48.76200  -50.36900 5.75800   1.000 55.17000  ? 49   LYS B CA  1 
ATOM   4179  C C   . LYS B 1 30  ? 48.50100  -49.28400 6.79600   1.000 60.79000  ? 49   LYS B C   1 
ATOM   4180  O O   . LYS B 1 30  ? 48.38600  -49.57600 7.99300   1.000 58.57000  ? 49   LYS B O   1 
ATOM   4181  C CB  . LYS B 1 30  ? 50.25600  -50.46900 5.46600   1.000 56.39000  ? 49   LYS B CB  1 
ATOM   4182  C CG  . LYS B 1 30  ? 51.03200  -50.76800 6.71600   1.000 63.95000  ? 49   LYS B CG  1 
ATOM   4183  C CD  . LYS B 1 30  ? 52.55700  -50.77100 6.57400   1.000 72.93000  ? 49   LYS B CD  1 
ATOM   4184  C CE  . LYS B 1 30  ? 53.22800  -49.39100 6.79600   1.000 75.50000  ? 49   LYS B CE  1 
ATOM   4185  N NZ  . LYS B 1 30  ? 53.59000  -48.75300 5.47100   1.000 73.29000  ? 49   LYS B NZ  1 
ATOM   4186  N N   . ASP B 1 31  ? 48.41200  -48.02400 6.36000   1.000 59.32000  ? 50   ASP B N   1 
ATOM   4187  C CA  . ASP B 1 31  ? 48.22500  -46.91600 7.29100   1.000 58.39000  ? 50   ASP B CA  1 
ATOM   4188  C C   . ASP B 1 31  ? 46.77100  -46.66900 7.65300   1.000 53.02000  ? 50   ASP B C   1 
ATOM   4189  O O   . ASP B 1 31  ? 46.48900  -46.23600 8.77600   1.000 57.51000  ? 50   ASP B O   1 
ATOM   4190  C CB  . ASP B 1 31  ? 48.78900  -45.61100 6.72600   1.000 60.52000  ? 50   ASP B CB  1 
ATOM   4191  C CG  . ASP B 1 31  ? 50.29600  -45.62300 6.62200   1.000 59.42000  ? 50   ASP B CG  1 
ATOM   4192  O OD1 . ASP B 1 31  ? 50.93200  -46.47700 7.27500   1.000 61.38000  ? 50   ASP B OD1 1 
ATOM   4193  O OD2 . ASP B 1 31  ? 50.83900  -44.73200 5.93400   1.000 54.51000  ? 50   ASP B OD2 1 
ATOM   4194  N N   . THR B 1 32  ? 45.84400  -46.90600 6.72800   1.000 46.47000  ? 51   THR B N   1 
ATOM   4195  C CA  . THR B 1 32  ? 44.45500  -46.51000 6.92000   1.000 52.82000  ? 51   THR B CA  1 
ATOM   4196  C C   . THR B 1 32  ? 43.47100  -47.66800 6.90600   1.000 51.21000  ? 51   THR B C   1 
ATOM   4197  O O   . THR B 1 32  ? 42.29900  -47.46000 7.23000   1.000 50.29000  ? 51   THR B O   1 
ATOM   4198  C CB  . THR B 1 32  ? 44.01700  -45.51000 5.83300   1.000 55.50000  ? 51   THR B CB  1 
ATOM   4199  O OG1 . THR B 1 32  ? 43.93500  -46.18100 4.56300   1.000 51.60000  ? 51   THR B OG1 1 
ATOM   4200  C CG2 . THR B 1 32  ? 45.00900  -44.35600 5.73100   1.000 53.35000  ? 51   THR B CG2 1 
ATOM   4201  N N   . GLY B 1 33  ? 43.89200  -48.86400 6.51100   1.000 55.05000  ? 52   GLY B N   1 
ATOM   4202  C CA  . GLY B 1 33  ? 42.97900  -49.97700 6.39700   1.000 47.67000  ? 52   GLY B CA  1 
ATOM   4203  C C   . GLY B 1 33  ? 42.17600  -50.02400 5.11800   1.000 48.68000  ? 52   GLY B C   1 
ATOM   4204  O O   . GLY B 1 33  ? 41.43000  -50.99100 4.92500   1.000 50.60000  ? 52   GLY B O   1 
ATOM   4205  N N   . ILE B 1 34  ? 42.32100  -49.03300 4.23400   1.000 47.70000  ? 53   ILE B N   1 
ATOM   4206  C CA  . ILE B 1 34  ? 41.53500  -48.94100 3.00000   1.000 55.13000  ? 53   ILE B CA  1 
ATOM   4207  C C   . ILE B 1 34  ? 42.25500  -49.64700 1.85700   1.000 51.28000  ? 53   ILE B C   1 
ATOM   4208  O O   . ILE B 1 34  ? 43.37200  -49.27000 1.48300   1.000 45.34000  ? 53   ILE B O   1 
ATOM   4209  C CB  . ILE B 1 34  ? 41.24800  -47.47800 2.62900   1.000 55.73000  ? 53   ILE B CB  1 
ATOM   4210  C CG1 . ILE B 1 34  ? 40.16800  -46.88600 3.53700   1.000 58.77000  ? 53   ILE B CG1 1 
ATOM   4211  C CG2 . ILE B 1 34  ? 40.84600  -47.36500 1.17100   1.000 54.60000  ? 53   ILE B CG2 1 
ATOM   4212  C CD1 . ILE B 1 34  ? 40.69400  -46.24500 4.78200   1.000 62.68000  ? 53   ILE B CD1 1 
ATOM   4213  N N   . LYS B 1 35  ? 41.60700  -50.65500 1.28100   1.000 45.54000  ? 54   LYS B N   1 
ATOM   4214  C CA  . LYS B 1 35  ? 42.19600  -51.32500 0.13300   1.000 54.34000  ? 54   LYS B CA  1 
ATOM   4215  C C   . LYS B 1 35  ? 42.14900  -50.42700 -1.09300  1.000 59.89000  ? 54   LYS B C   1 
ATOM   4216  O O   . LYS B 1 35  ? 41.18100  -49.69100 -1.31700  1.000 57.78000  ? 54   LYS B O   1 
ATOM   4217  C CB  . LYS B 1 35  ? 41.49900  -52.64900 -0.17900  1.000 60.16000  ? 54   LYS B CB  1 
ATOM   4218  C CG  . LYS B 1 35  ? 41.74600  -53.80000 0.79200   1.000 72.05000  ? 54   LYS B CG  1 
ATOM   4219  C CD  . LYS B 1 35  ? 41.21100  -55.10400 0.17200   1.000 78.84000  ? 54   LYS B CD  1 
ATOM   4220  C CE  . LYS B 1 35  ? 41.48000  -56.33900 1.04200   1.000 78.28000  ? 54   LYS B CE  1 
ATOM   4221  N NZ  . LYS B 1 35  ? 40.88100  -56.23400 2.41300   1.000 74.50000  ? 54   LYS B NZ  1 
ATOM   4222  N N   . VAL B 1 36  ? 43.21000  -50.51400 -1.89000  1.000 51.78000  ? 55   VAL B N   1 
ATOM   4223  C CA  . VAL B 1 36  ? 43.37500  -49.75500 -3.11800  1.000 52.71000  ? 55   VAL B CA  1 
ATOM   4224  C C   . VAL B 1 36  ? 43.61300  -50.75200 -4.23900  1.000 50.74000  ? 55   VAL B C   1 
ATOM   4225  O O   . VAL B 1 36  ? 44.59800  -51.49900 -4.20000  1.000 54.69000  ? 55   VAL B O   1 
ATOM   4226  C CB  . VAL B 1 36  ? 44.54900  -48.77500 -3.00400  1.000 48.58000  ? 55   VAL B CB  1 
ATOM   4227  C CG1 . VAL B 1 36  ? 44.72000  -48.00300 -4.29200  1.000 39.16000  ? 55   VAL B CG1 1 
ATOM   4228  C CG2 . VAL B 1 36  ? 44.34700  -47.85900 -1.80900  1.000 44.67000  ? 55   VAL B CG2 1 
ATOM   4229  N N   . THR B 1 37  ? 42.72700  -50.75800 -5.23700  1.000 49.02000  ? 56   THR B N   1 
ATOM   4230  C CA  . THR B 1 37  ? 42.81800  -51.66200 -6.38200  1.000 47.39000  ? 56   THR B CA  1 
ATOM   4231  C C   . THR B 1 37  ? 43.17100  -50.87500 -7.64100  1.000 47.85000  ? 56   THR B C   1 
ATOM   4232  O O   . THR B 1 37  ? 42.48700  -49.90300 -7.98300  1.000 47.66000  ? 56   THR B O   1 
ATOM   4233  C CB  . THR B 1 37  ? 41.50900  -52.42600 -6.57200  1.000 47.06000  ? 56   THR B CB  1 
ATOM   4234  O OG1 . THR B 1 37  ? 41.28100  -53.26000 -5.43000  1.000 57.69000  ? 56   THR B OG1 1 
ATOM   4235  C CG2 . THR B 1 37  ? 41.56800  -53.28700 -7.81500  1.000 48.36000  ? 56   THR B CG2 1 
ATOM   4236  N N   . VAL B 1 38  ? 44.23100  -51.30200 -8.33000  1.000 47.71000  ? 57   VAL B N   1 
ATOM   4237  C CA  . VAL B 1 38  ? 44.73100  -50.63600 -9.53000  1.000 44.55000  ? 57   VAL B CA  1 
ATOM   4238  C C   . VAL B 1 38  ? 44.39000  -51.49600 -10.74000 1.000 44.38000  ? 57   VAL B C   1 
ATOM   4239  O O   . VAL B 1 38  ? 44.80000  -52.66000 -10.81300 1.000 50.46000  ? 57   VAL B O   1 
ATOM   4240  C CB  . VAL B 1 38  ? 46.24400  -50.39200 -9.45600  1.000 42.87000  ? 57   VAL B CB  1 
ATOM   4241  C CG1 . VAL B 1 38  ? 46.73100  -49.79100 -10.76500 1.000 45.16000  ? 57   VAL B CG1 1 
ATOM   4242  C CG2 . VAL B 1 38  ? 46.58300  -49.48200 -8.28900  1.000 39.14000  ? 57   VAL B CG2 1 
ATOM   4243  N N   . GLU B 1 39  ? 43.66000  -50.91800 -11.69700 1.000 38.73000  ? 58   GLU B N   1 
ATOM   4244  C CA  . GLU B 1 39  ? 43.26000  -51.59800 -12.92100 1.000 42.12000  ? 58   GLU B CA  1 
ATOM   4245  C C   . GLU B 1 39  ? 43.75600  -50.83600 -14.14600 1.000 43.70000  ? 58   GLU B C   1 
ATOM   4246  O O   . GLU B 1 39  ? 43.90800  -49.61100 -14.12400 1.000 43.44000  ? 58   GLU B O   1 
ATOM   4247  C CB  . GLU B 1 39  ? 41.73400  -51.74600 -12.99600 1.000 44.69000  ? 58   GLU B CB  1 
ATOM   4248  C CG  . GLU B 1 39  ? 41.18500  -52.65000 -11.91900 1.000 52.63000  ? 58   GLU B CG  1 
ATOM   4249  C CD  . GLU B 1 39  ? 39.67200  -52.71800 -11.89800 1.000 51.49000  ? 58   GLU B CD  1 
ATOM   4250  O OE1 . GLU B 1 39  ? 39.00400  -51.97300 -12.65300 1.000 49.69000  ? 58   GLU B OE1 1 
ATOM   4251  O OE2 . GLU B 1 39  ? 39.15500  -53.52000 -11.09600 1.000 56.76000  ? 58   GLU B OE2 1 
ATOM   4252  N N   . HIS B 1 40  ? 44.00300  -51.57200 -15.22600 1.000 45.26000  ? 59   HIS B N   1 
ATOM   4253  C CA  . HIS B 1 40  ? 44.41400  -50.99200 -16.50500 1.000 47.37000  ? 59   HIS B CA  1 
ATOM   4254  C C   . HIS B 1 40  ? 43.59000  -51.58500 -17.64300 1.000 45.91000  ? 59   HIS B C   1 
ATOM   4255  O O   . HIS B 1 40  ? 44.11600  -52.30300 -18.50100 1.000 49.74000  ? 59   HIS B O   1 
ATOM   4256  C CB  . HIS B 1 40  ? 45.91400  -51.19100 -16.73100 1.000 38.80000  ? 59   HIS B CB  1 
ATOM   4257  C CG  . HIS B 1 40  ? 46.38600  -52.59300 -16.49900 1.000 43.21000  ? 59   HIS B CG  1 
ATOM   4258  N ND1 . HIS B 1 40  ? 46.37100  -53.56100 -17.48000 1.000 41.63000  ? 59   HIS B ND1 1 
ATOM   4259  C CD2 . HIS B 1 40  ? 46.90400  -53.18400 -15.39400 1.000 44.37000  ? 59   HIS B CD2 1 
ATOM   4260  C CE1 . HIS B 1 40  ? 46.85300  -54.68900 -16.98700 1.000 39.12000  ? 59   HIS B CE1 1 
ATOM   4261  N NE2 . HIS B 1 40  ? 47.18400  -54.48700 -15.72400 1.000 44.13000  ? 59   HIS B NE2 1 
ATOM   4262  N N   . PRO B 1 41  ? 42.29400  -51.28600 -17.69200 1.000 42.79000  ? 60   PRO B N   1 
ATOM   4263  C CA  . PRO B 1 41  ? 41.46300  -51.83900 -18.76600 1.000 43.09000  ? 60   PRO B CA  1 
ATOM   4264  C C   . PRO B 1 41  ? 41.79600  -51.21200 -20.10900 1.000 45.42000  ? 60   PRO B C   1 
ATOM   4265  O O   . PRO B 1 41  ? 42.21900  -50.05600 -20.19800 1.000 42.08000  ? 60   PRO B O   1 
ATOM   4266  C CB  . PRO B 1 41  ? 40.03500  -51.49300 -18.32700 1.000 37.19000  ? 60   PRO B CB  1 
ATOM   4267  C CG  . PRO B 1 41  ? 40.18700  -50.28400 -17.48900 1.000 37.53000  ? 60   PRO B CG  1 
ATOM   4268  C CD  . PRO B 1 41  ? 41.51900  -50.41300 -16.79000 1.000 45.72000  ? 60   PRO B CD  1 
ATOM   4269  N N   . ASP B 1 42  ? 41.59100  -52.00200 -21.16300 1.000 49.41000  ? 61   ASP B N   1 
ATOM   4270  C CA  . ASP B 1 42  ? 41.80500  -51.52700 -22.52200 1.000 40.66000  ? 61   ASP B CA  1 
ATOM   4271  C C   . ASP B 1 42  ? 40.84200  -50.39100 -22.84300 1.000 41.63000  ? 61   ASP B C   1 
ATOM   4272  O O   . ASP B 1 42  ? 39.68100  -50.40500 -22.43000 1.000 39.65000  ? 61   ASP B O   1 
ATOM   4273  C CB  . ASP B 1 42  ? 41.62900  -52.68200 -23.51300 1.000 44.10000  ? 61   ASP B CB  1 
ATOM   4274  C CG  . ASP B 1 42  ? 42.04400  -52.31100 -24.93100 1.000 50.34000  ? 61   ASP B CG  1 
ATOM   4275  O OD1 . ASP B 1 42  ? 43.25600  -52.09400 -25.16100 1.000 49.61000  ? 61   ASP B OD1 1 
ATOM   4276  O OD2 . ASP B 1 42  ? 41.16900  -52.26800 -25.82100 1.000 49.75000  ? 61   ASP B OD2 1 
ATOM   4277  N N   . LYS B 1 43  ? 41.34500  -49.39300 -23.57000 1.000 45.98000  ? 62   LYS B N   1 
ATOM   4278  C CA  . LYS B 1 43  ? 40.55700  -48.22800 -23.98100 1.000 41.45000  ? 62   LYS B CA  1 
ATOM   4279  C C   . LYS B 1 43  ? 39.80500  -47.62900 -22.79400 1.000 44.56000  ? 62   LYS B C   1 
ATOM   4280  O O   . LYS B 1 43  ? 38.61700  -47.30800 -22.87600 1.000 48.27000  ? 62   LYS B O   1 
ATOM   4281  C CB  . LYS B 1 43  ? 39.61300  -48.58500 -25.13800 1.000 34.58000  ? 62   LYS B CB  1 
ATOM   4282  C CG  . LYS B 1 43  ? 40.38100  -48.87500 -26.43700 1.000 41.26000  ? 62   LYS B CG  1 
ATOM   4283  C CD  . LYS B 1 43  ? 39.51500  -49.01500 -27.69100 1.000 45.27000  ? 62   LYS B CD  1 
ATOM   4284  C CE  . LYS B 1 43  ? 38.87600  -50.39300 -27.82500 1.000 48.67000  ? 62   LYS B CE  1 
ATOM   4285  N NZ  . LYS B 1 43  ? 38.16700  -50.55800 -29.13700 1.000 43.86000  ? 62   LYS B NZ  1 
ATOM   4286  N N   . LEU B 1 44  ? 40.51400  -47.47400 -21.66900 1.000 37.55000  ? 63   LEU B N   1 
ATOM   4287  C CA  . LEU B 1 44  ? 39.86700  -46.96400 -20.46600 1.000 43.61000  ? 63   LEU B CA  1 
ATOM   4288  C C   . LEU B 1 44  ? 39.43400  -45.51300 -20.63600 1.000 41.64000  ? 63   LEU B C   1 
ATOM   4289  O O   . LEU B 1 44  ? 38.49700  -45.06400 -19.96300 1.000 37.61000  ? 63   LEU B O   1 
ATOM   4290  C CB  . LEU B 1 44  ? 40.79700  -47.09900 -19.25400 1.000 38.14000  ? 63   LEU B CB  1 
ATOM   4291  C CG  . LEU B 1 44  ? 42.02700  -46.19900 -19.11600 1.000 39.15000  ? 63   LEU B CG  1 
ATOM   4292  C CD1 . LEU B 1 44  ? 41.69300  -44.87700 -18.42500 1.000 33.74000  ? 63   LEU B CD1 1 
ATOM   4293  C CD2 . LEU B 1 44  ? 43.13600  -46.91300 -18.36100 1.000 38.78000  ? 63   LEU B CD2 1 
ATOM   4294  N N   . GLU B 1 45  ? 40.10500  -44.76300 -21.51500 1.000 39.78000  ? 64   GLU B N   1 
ATOM   4295  C CA  . GLU B 1 45  ? 39.75300  -43.36200 -21.69900 1.000 40.72000  ? 64   GLU B CA  1 
ATOM   4296  C C   . GLU B 1 45  ? 38.44200  -43.20100 -22.44800 1.000 41.90000  ? 64   GLU B C   1 
ATOM   4297  O O   . GLU B 1 45  ? 37.84000  -42.12500 -22.39200 1.000 45.05000  ? 64   GLU B O   1 
ATOM   4298  C CB  . GLU B 1 45  ? 40.87300  -42.61700 -22.43500 1.000 40.24000  ? 64   GLU B CB  1 
ATOM   4299  C CG  . GLU B 1 45  ? 40.94700  -42.86400 -23.94000 1.000 40.65000  ? 64   GLU B CG  1 
ATOM   4300  C CD  . GLU B 1 45  ? 41.66600  -44.14700 -24.31200 1.000 43.49000  ? 64   GLU B CD  1 
ATOM   4301  O OE1 . GLU B 1 45  ? 41.79900  -45.03900 -23.44300 1.000 45.91000  ? 64   GLU B OE1 1 
ATOM   4302  O OE2 . GLU B 1 45  ? 42.11100  -44.26100 -25.47600 1.000 50.55000  ? 64   GLU B OE2 1 
ATOM   4303  N N   . GLU B 1 46  ? 37.99600  -44.24400 -23.14700 1.000 45.29000  ? 65   GLU B N   1 
ATOM   4304  C CA  . GLU B 1 46  ? 36.68400  -44.26100 -23.78100 1.000 46.16000  ? 65   GLU B CA  1 
ATOM   4305  C C   . GLU B 1 46  ? 35.65000  -44.99400 -22.94000 1.000 52.65000  ? 65   GLU B C   1 
ATOM   4306  O O   . GLU B 1 46  ? 34.46000  -44.65100 -22.98400 1.000 53.15000  ? 65   GLU B O   1 
ATOM   4307  C CB  . GLU B 1 46  ? 36.79300  -44.91100 -25.16500 1.000 43.81000  ? 65   GLU B CB  1 
ATOM   4308  C CG  . GLU B 1 46  ? 37.64500  -44.08900 -26.11900 1.000 51.90000  ? 65   GLU B CG  1 
ATOM   4309  C CD  . GLU B 1 46  ? 36.96300  -42.79300 -26.54200 1.000 68.45000  ? 65   GLU B CD  1 
ATOM   4310  O OE1 . GLU B 1 46  ? 35.75900  -42.83400 -26.87200 1.000 80.32000  ? 65   GLU B OE1 1 
ATOM   4311  O OE2 . GLU B 1 46  ? 37.60800  -41.72400 -26.47100 1.000 70.19000  ? 65   GLU B OE2 1 
ATOM   4312  N N   . LYS B 1 47  ? 36.08200  -45.98800 -22.16400 1.000 47.12000  ? 66   LYS B N   1 
ATOM   4313  C CA  . LYS B 1 47  ? 35.17100  -46.63700 -21.23000 1.000 44.80000  ? 66   LYS B CA  1 
ATOM   4314  C C   . LYS B 1 47  ? 34.74100  -45.68000 -20.12400 1.000 48.04000  ? 66   LYS B C   1 
ATOM   4315  O O   . LYS B 1 47  ? 33.57700  -45.69300 -19.70700 1.000 45.68000  ? 66   LYS B O   1 
ATOM   4316  C CB  . LYS B 1 47  ? 35.83000  -47.88900 -20.64600 1.000 45.04000  ? 66   LYS B CB  1 
ATOM   4317  C CG  . LYS B 1 47  ? 36.00700  -49.01300 -21.66400 1.000 44.25000  ? 66   LYS B CG  1 
ATOM   4318  C CD  . LYS B 1 47  ? 36.66100  -50.26300 -21.07400 1.000 36.87000  ? 66   LYS B CD  1 
ATOM   4319  C CE  . LYS B 1 47  ? 36.78400  -51.34200 -22.15300 1.000 42.61000  ? 66   LYS B CE  1 
ATOM   4320  N NZ  . LYS B 1 47  ? 37.45600  -52.58100 -21.67600 1.000 47.68000  ? 66   LYS B NZ  1 
ATOM   4321  N N   . PHE B 1 48  ? 35.66000  -44.83600 -19.64400 1.000 47.55000  ? 67   PHE B N   1 
ATOM   4322  C CA  . PHE B 1 48  ? 35.35700  -43.99200 -18.48700 1.000 46.31000  ? 67   PHE B CA  1 
ATOM   4323  C C   . PHE B 1 48  ? 34.10800  -43.13100 -18.66500 1.000 45.34000  ? 67   PHE B C   1 
ATOM   4324  O O   . PHE B 1 48  ? 33.25600  -43.13900 -17.76200 1.000 44.73000  ? 67   PHE B O   1 
ATOM   4325  C CB  . PHE B 1 48  ? 36.55900  -43.10500 -18.13300 1.000 34.35000  ? 67   PHE B CB  1 
ATOM   4326  C CG  . PHE B 1 48  ? 36.34200  -42.28400 -16.89300 1.000 33.76000  ? 67   PHE B CG  1 
ATOM   4327  C CD1 . PHE B 1 48  ? 36.49100  -42.85600 -15.63500 1.000 35.84000  ? 67   PHE B CD1 1 
ATOM   4328  C CD2 . PHE B 1 48  ? 35.94700  -40.95900 -16.98100 1.000 32.34000  ? 67   PHE B CD2 1 
ATOM   4329  C CE1 . PHE B 1 48  ? 36.27900  -42.11400 -14.48900 1.000 30.52000  ? 67   PHE B CE1 1 
ATOM   4330  C CE2 . PHE B 1 48  ? 35.72500  -40.21500 -15.84300 1.000 31.80000  ? 67   PHE B CE2 1 
ATOM   4331  C CZ  . PHE B 1 48  ? 35.89600  -40.79200 -14.59200 1.000 34.91000  ? 67   PHE B CZ  1 
ATOM   4332  N N   . PRO B 1 49  ? 33.92800  -42.37700 -19.76100 1.000 46.76000  ? 68   PRO B N   1 
ATOM   4333  C CA  . PRO B 1 49  ? 32.70500  -41.56100 -19.88000 1.000 51.21000  ? 68   PRO B CA  1 
ATOM   4334  C C   . PRO B 1 49  ? 31.44300  -42.39800 -19.86600 1.000 49.70000  ? 68   PRO B C   1 
ATOM   4335  O O   . PRO B 1 49  ? 30.41300  -41.96500 -19.33700 1.000 52.21000  ? 68   PRO B O   1 
ATOM   4336  C CB  . PRO B 1 49  ? 32.88200  -40.85500 -21.23100 1.000 49.55000  ? 68   PRO B CB  1 
ATOM   4337  C CG  . PRO B 1 49  ? 34.31800  -40.94700 -21.53400 1.000 51.55000  ? 68   PRO B CG  1 
ATOM   4338  C CD  . PRO B 1 49  ? 34.78600  -42.23600 -20.94900 1.000 44.60000  ? 68   PRO B CD  1 
ATOM   4339  N N   . GLN B 1 50  ? 31.50800  -43.60200 -20.43500 1.000 52.57000  ? 69   GLN B N   1 
ATOM   4340  C CA  . GLN B 1 50  ? 30.33100  -44.45300 -20.55100 1.000 52.94000  ? 69   GLN B CA  1 
ATOM   4341  C C   . GLN B 1 50  ? 29.88100  -44.96500 -19.19000 1.000 50.15000  ? 69   GLN B C   1 
ATOM   4342  O O   . GLN B 1 50  ? 28.67700  -45.07900 -18.93700 1.000 60.75000  ? 69   GLN B O   1 
ATOM   4343  C CB  . GLN B 1 50  ? 30.63600  -45.60900 -21.50600 1.000 52.22000  ? 69   GLN B CB  1 
ATOM   4344  C CG  . GLN B 1 50  ? 30.86900  -45.14700 -22.94000 1.000 56.91000  ? 69   GLN B CG  1 
ATOM   4345  C CD  . GLN B 1 50  ? 31.44800  -46.23400 -23.83900 1.000 71.02000  ? 69   GLN B CD  1 
ATOM   4346  O OE1 . GLN B 1 50  ? 31.78900  -47.32900 -23.38000 1.000 70.29000  ? 69   GLN B OE1 1 
ATOM   4347  N NE2 . GLN B 1 50  ? 31.57900  -45.92500 -25.12900 1.000 61.83000  ? 69   GLN B NE2 1 
ATOM   4348  N N   . VAL B 1 51  ? 30.82400  -45.27300 -18.29600 1.000 48.74000  ? 70   VAL B N   1 
ATOM   4349  C CA  . VAL B 1 51  ? 30.48100  -45.91300 -17.02800 1.000 46.50000  ? 70   VAL B CA  1 
ATOM   4350  C C   . VAL B 1 51  ? 30.36300  -44.87700 -15.91500 1.000 56.49000  ? 70   VAL B C   1 
ATOM   4351  O O   . VAL B 1 51  ? 29.66000  -45.09700 -14.92100 1.000 56.35000  ? 70   VAL B O   1 
ATOM   4352  C CB  . VAL B 1 51  ? 31.50500  -47.00400 -16.65800 1.000 49.25000  ? 70   VAL B CB  1 
ATOM   4353  C CG1 . VAL B 1 51  ? 31.55000  -48.08900 -17.72800 1.000 36.24000  ? 70   VAL B CG1 1 
ATOM   4354  C CG2 . VAL B 1 51  ? 32.89100  -46.40500 -16.44100 1.000 49.98000  ? 70   VAL B CG2 1 
ATOM   4355  N N   . ALA B 1 52  ? 31.05900  -43.74500 -16.05800 1.000 60.54000  ? 71   ALA B N   1 
ATOM   4356  C CA  . ALA B 1 52  ? 30.91900  -42.67600 -15.07100 1.000 54.71000  ? 71   ALA B CA  1 
ATOM   4357  C C   . ALA B 1 52  ? 29.54600  -42.02800 -15.15600 1.000 60.77000  ? 71   ALA B C   1 
ATOM   4358  O O   . ALA B 1 52  ? 28.96400  -41.65900 -14.12900 1.000 61.55000  ? 71   ALA B O   1 
ATOM   4359  C CB  . ALA B 1 52  ? 32.01100  -41.62500 -15.25900 1.000 50.45000  ? 71   ALA B CB  1 
ATOM   4360  N N   . ALA B 1 53  ? 29.01800  -41.87500 -16.37800 1.000 60.68000  ? 72   ALA B N   1 
ATOM   4361  C CA  . ALA B 1 53  ? 27.68900  -41.29700 -16.55800 1.000 65.69000  ? 72   ALA B CA  1 
ATOM   4362  C C   . ALA B 1 53  ? 26.62300  -42.10200 -15.82800 1.000 65.36000  ? 72   ALA B C   1 
ATOM   4363  O O   . ALA B 1 53  ? 25.63400  -41.53300 -15.35100 1.000 70.71000  ? 72   ALA B O   1 
ATOM   4364  C CB  . ALA B 1 53  ? 27.35800  -41.19700 -18.05100 1.000 60.19000  ? 72   ALA B CB  1 
ATOM   4365  N N   . THR B 1 54  ? 26.80500  -43.41900 -15.72500 1.000 63.42000  ? 73   THR B N   1 
ATOM   4366  C CA  . THR B 1 54  ? 25.90400  -44.27300 -14.96900 1.000 62.19000  ? 73   THR B CA  1 
ATOM   4367  C C   . THR B 1 54  ? 26.29100  -44.35700 -13.49800 1.000 67.71000  ? 73   THR B C   1 
ATOM   4368  O O   . THR B 1 54  ? 25.85900  -45.28400 -12.80200 1.000 76.00000  ? 73   THR B O   1 
ATOM   4369  C CB  . THR B 1 54  ? 25.86800  -45.67700 -15.57700 1.000 66.43000  ? 73   THR B CB  1 
ATOM   4370  O OG1 . THR B 1 54  ? 27.07900  -46.37300 -15.25200 1.000 69.76000  ? 73   THR B OG1 1 
ATOM   4371  C CG2 . THR B 1 54  ? 25.76500  -45.58100 -17.09100 1.000 58.69000  ? 73   THR B CG2 1 
ATOM   4372  N N   . GLY B 1 55  ? 27.10300  -43.41700 -13.01600 1.000 67.47000  ? 74   GLY B N   1 
ATOM   4373  C CA  . GLY B 1 55  ? 27.53900  -43.42400 -11.62900 1.000 60.78000  ? 74   GLY B CA  1 
ATOM   4374  C C   . GLY B 1 55  ? 28.40800  -44.60400 -11.26400 1.000 62.06000  ? 74   GLY B C   1 
ATOM   4375  O O   . GLY B 1 55  ? 28.43900  -45.00800 -10.09700 1.000 69.81000  ? 74   GLY B O   1 
ATOM   4376  N N   . ASP B 1 56  ? 29.12400  -45.16500 -12.22800 1.000 69.39000  ? 75   ASP B N   1 
ATOM   4377  C CA  . ASP B 1 56  ? 29.96600  -46.33200 -12.00100 1.000 73.98000  ? 75   ASP B CA  1 
ATOM   4378  C C   . ASP B 1 56  ? 31.41100  -45.98500 -12.41900 1.000 65.87000  ? 75   ASP B C   1 
ATOM   4379  O O   . ASP B 1 56  ? 31.73800  -44.82300 -12.68700 1.000 61.87000  ? 75   ASP B O   1 
ATOM   4380  C CB  . ASP B 1 56  ? 29.33500  -47.52200 -12.73500 1.000 67.55000  ? 75   ASP B CB  1 
ATOM   4381  C CG  . ASP B 1 56  ? 29.70100  -48.86000 -12.12300 1.000 79.10000  ? 75   ASP B CG  1 
ATOM   4382  O OD1 . ASP B 1 56  ? 30.62400  -48.91300 -11.28000 1.000 74.52000  ? 75   ASP B OD1 1 
ATOM   4383  O OD2 . ASP B 1 56  ? 29.00000  -49.84900 -12.43600 1.000 86.48000  ? 75   ASP B OD2 1 
ATOM   4384  N N   . GLY B 1 57  ? 32.29500  -46.98400 -12.43400 1.000 59.76000  ? 76   GLY B N   1 
ATOM   4385  C CA  . GLY B 1 57  ? 33.66900  -46.76100 -12.83500 1.000 49.41000  ? 76   GLY B CA  1 
ATOM   4386  C C   . GLY B 1 57  ? 34.63000  -46.68200 -11.66300 1.000 53.45000  ? 76   GLY B C   1 
ATOM   4387  O O   . GLY B 1 57  ? 34.29300  -47.07100 -10.53900 1.000 54.10000  ? 76   GLY B O   1 
ATOM   4388  N N   . PRO B 1 58  ? 35.84400  -46.17300 -11.89900 1.000 43.50000  ? 77   PRO B N   1 
ATOM   4389  C CA  . PRO B 1 58  ? 36.86700  -46.12900 -10.84600 1.000 38.50000  ? 77   PRO B CA  1 
ATOM   4390  C C   . PRO B 1 58  ? 36.68700  -44.90200 -9.96300  1.000 36.16000  ? 77   PRO B C   1 
ATOM   4391  O O   . PRO B 1 58  ? 35.96100  -43.96800 -10.30100 1.000 41.88000  ? 77   PRO B O   1 
ATOM   4392  C CB  . PRO B 1 58  ? 38.17100  -46.03100 -11.64300 1.000 43.20000  ? 77   PRO B CB  1 
ATOM   4393  C CG  . PRO B 1 58  ? 37.77300  -45.20900 -12.83300 1.000 39.10000  ? 77   PRO B CG  1 
ATOM   4394  C CD  . PRO B 1 58  ? 36.34700  -45.61400 -13.16700 1.000 45.00000  ? 77   PRO B CD  1 
ATOM   4395  N N   . ASP B 1 59  ? 37.36700  -44.89800 -8.81300  1.000 37.49000  ? 78   ASP B N   1 
ATOM   4396  C CA  . ASP B 1 59  ? 37.31500  -43.65900 -8.04200  1.000 40.35000  ? 78   ASP B CA  1 
ATOM   4397  C C   . ASP B 1 59  ? 38.30000  -42.64500 -8.59400  1.000 38.07000  ? 78   ASP B C   1 
ATOM   4398  O O   . ASP B 1 59  ? 38.06100  -41.43500 -8.52600  1.000 41.67000  ? 78   ASP B O   1 
ATOM   4399  C CB  . ASP B 1 59  ? 37.60100  -43.86000 -6.54700  1.000 41.67000  ? 78   ASP B CB  1 
ATOM   4400  C CG  . ASP B 1 59  ? 36.75700  -44.93900 -5.91500  1.000 47.65000  ? 78   ASP B CG  1 
ATOM   4401  O OD1 . ASP B 1 59  ? 36.20400  -45.78100 -6.63700  1.000 56.98000  ? 78   ASP B OD1 1 
ATOM   4402  O OD2 . ASP B 1 59  ? 36.47500  -44.82000 -4.70300  1.000 62.19000  ? 78   ASP B OD2 1 
ATOM   4403  N N   . ILE B 1 60  ? 39.41600  -43.12600 -9.12700  1.000 38.06000  ? 79   ILE B N   1 
ATOM   4404  C CA  . ILE B 1 60  ? 40.46700  -42.28600 -9.67600  1.000 34.69000  ? 79   ILE B CA  1 
ATOM   4405  C C   . ILE B 1 60  ? 40.78700  -42.79600 -11.07200 1.000 38.81000  ? 79   ILE B C   1 
ATOM   4406  O O   . ILE B 1 60  ? 40.80800  -44.00900 -11.30700 1.000 39.81000  ? 79   ILE B O   1 
ATOM   4407  C CB  . ILE B 1 60  ? 41.70900  -42.30000 -8.76100  1.000 32.86000  ? 79   ILE B CB  1 
ATOM   4408  C CG1 . ILE B 1 60  ? 41.36200  -41.73000 -7.38600  1.000 32.78000  ? 79   ILE B CG1 1 
ATOM   4409  C CG2 . ILE B 1 60  ? 42.81600  -41.49700 -9.34800  1.000 34.73000  ? 79   ILE B CG2 1 
ATOM   4410  C CD1 . ILE B 1 60  ? 42.47200  -41.90500 -6.36300  1.000 34.29000  ? 79   ILE B CD1 1 
ATOM   4411  N N   . ILE B 1 61  ? 40.99000  -41.87300 -12.01000 1.000 37.14000  ? 80   ILE B N   1 
ATOM   4412  C CA  . ILE B 1 61  ? 41.43900  -42.19800 -13.36000 1.000 37.69000  ? 80   ILE B CA  1 
ATOM   4413  C C   . ILE B 1 61  ? 42.70600  -41.41200 -13.65100 1.000 36.24000  ? 80   ILE B C   1 
ATOM   4414  O O   . ILE B 1 61  ? 42.74600  -40.19900 -13.41300 1.000 36.67000  ? 80   ILE B O   1 
ATOM   4415  C CB  . ILE B 1 61  ? 40.35300  -41.90200 -14.41400 1.000 38.16000  ? 80   ILE B CB  1 
ATOM   4416  C CG1 . ILE B 1 61  ? 40.89200  -42.15400 -15.82800 1.000 39.82000  ? 80   ILE B CG1 1 
ATOM   4417  C CG2 . ILE B 1 61  ? 39.76800  -40.49600 -14.25200 1.000 34.37000  ? 80   ILE B CG2 1 
ATOM   4418  C CD1 . ILE B 1 61  ? 39.80900  -42.14400 -16.90800 1.000 34.58000  ? 80   ILE B CD1 1 
ATOM   4419  N N   . PHE B 1 62  ? 43.74300  -42.09700 -14.15200 1.000 38.38000  ? 81   PHE B N   1 
ATOM   4420  C CA  . PHE B 1 62  ? 44.93500  -41.42300 -14.66500 1.000 35.48000  ? 81   PHE B CA  1 
ATOM   4421  C C   . PHE B 1 62  ? 44.90300  -41.38400 -16.18600 1.000 43.44000  ? 81   PHE B C   1 
ATOM   4422  O O   . PHE B 1 62  ? 44.66800  -42.41100 -16.83400 1.000 42.87000  ? 81   PHE B O   1 
ATOM   4423  C CB  . PHE B 1 62  ? 46.27000  -42.06800 -14.26400 1.000 36.17000  ? 81   PHE B CB  1 
ATOM   4424  C CG  . PHE B 1 62  ? 46.57000  -42.05100 -12.78900 1.000 37.17000  ? 81   PHE B CG  1 
ATOM   4425  C CD1 . PHE B 1 62  ? 45.60100  -42.30400 -11.83700 1.000 37.31000  ? 81   PHE B CD1 1 
ATOM   4426  C CD2 . PHE B 1 62  ? 47.77800  -41.54000 -12.36700 1.000 32.74000  ? 81   PHE B CD2 1 
ATOM   4427  C CE1 . PHE B 1 62  ? 45.90500  -42.24000 -10.49400 1.000 33.78000  ? 81   PHE B CE1 1 
ATOM   4428  C CE2 . PHE B 1 62  ? 48.07600  -41.43000 -11.03200 1.000 36.63000  ? 81   PHE B CE2 1 
ATOM   4429  C CZ  . PHE B 1 62  ? 47.14000  -41.77700 -10.09400 1.000 38.01000  ? 81   PHE B CZ  1 
ATOM   4430  N N   . TRP B 1 63  ? 45.18700  -40.21200 -16.75200 1.000 41.45000  ? 82   TRP B N   1 
ATOM   4431  C CA  . TRP B 1 63  ? 45.26700  -40.09000 -18.20000 1.000 37.50000  ? 82   TRP B CA  1 
ATOM   4432  C C   . TRP B 1 63  ? 45.84600  -38.72500 -18.53500 1.000 38.32000  ? 82   TRP B C   1 
ATOM   4433  O O   . TRP B 1 63  ? 45.92300  -37.83900 -17.67800 1.000 35.00000  ? 82   TRP B O   1 
ATOM   4434  C CB  . TRP B 1 63  ? 43.89500  -40.26600 -18.85200 1.000 34.63000  ? 82   TRP B CB  1 
ATOM   4435  C CG  . TRP B 1 63  ? 43.97700  -40.63100 -20.27700 1.000 37.97000  ? 82   TRP B CG  1 
ATOM   4436  C CD1 . TRP B 1 63  ? 43.84700  -39.80000 -21.35100 1.000 35.27000  ? 82   TRP B CD1 1 
ATOM   4437  C CD2 . TRP B 1 63  ? 44.18500  -41.94400 -20.80100 1.000 40.16000  ? 82   TRP B CD2 1 
ATOM   4438  N NE1 . TRP B 1 63  ? 43.97700  -40.51800 -22.51600 1.000 37.61000  ? 82   TRP B NE1 1 
ATOM   4439  C CE2 . TRP B 1 63  ? 44.18600  -41.83600 -22.20500 1.000 40.13000  ? 82   TRP B CE2 1 
ATOM   4440  C CE3 . TRP B 1 63  ? 44.37500  -43.20100 -20.21800 1.000 41.60000  ? 82   TRP B CE3 1 
ATOM   4441  C CZ2 . TRP B 1 63  ? 44.37300  -42.93600 -23.03700 1.000 39.72000  ? 82   TRP B CZ2 1 
ATOM   4442  C CZ3 . TRP B 1 63  ? 44.56300  -44.29500 -21.04400 1.000 41.83000  ? 82   TRP B CZ3 1 
ATOM   4443  C CH2 . TRP B 1 63  ? 44.56000  -44.15500 -22.44100 1.000 45.87000  ? 82   TRP B CH2 1 
ATOM   4444  N N   . ALA B 1 64  ? 46.26400  -38.57300 -19.79300 1.000 35.23000  ? 83   ALA B N   1 
ATOM   4445  C CA  . ALA B 1 64  ? 46.69500  -37.27500 -20.30000 1.000 34.97000  ? 83   ALA B CA  1 
ATOM   4446  C C   . ALA B 1 64  ? 45.61500  -36.22200 -20.07400 1.000 34.77000  ? 83   ALA B C   1 
ATOM   4447  O O   . ALA B 1 64  ? 44.42600  -36.47400 -20.29900 1.000 33.82000  ? 83   ALA B O   1 
ATOM   4448  C CB  . ALA B 1 64  ? 47.02000  -37.37900 -21.79100 1.000 30.71000  ? 83   ALA B CB  1 
ATOM   4449  N N   . HIS B 1 65  ? 46.04600  -35.03000 -19.65300 1.000 30.08000  ? 84   HIS B N   1 
ATOM   4450  C CA  . HIS B 1 65  ? 45.10800  -33.98800 -19.24600 1.000 33.54000  ? 84   HIS B CA  1 
ATOM   4451  C C   . HIS B 1 65  ? 44.14400  -33.59200 -20.35200 1.000 36.15000  ? 84   HIS B C   1 
ATOM   4452  O O   . HIS B 1 65  ? 43.02600  -33.16100 -20.05500 1.000 41.29000  ? 84   HIS B O   1 
ATOM   4453  C CB  . HIS B 1 65  ? 45.85600  -32.73900 -18.82000 1.000 31.31000  ? 84   HIS B CB  1 
ATOM   4454  C CG  . HIS B 1 65  ? 46.50900  -32.03500 -19.96400 1.000 35.35000  ? 84   HIS B CG  1 
ATOM   4455  N ND1 . HIS B 1 65  ? 47.68300  -32.47800 -20.53000 1.000 34.36000  ? 84   HIS B ND1 1 
ATOM   4456  C CD2 . HIS B 1 65  ? 46.13600  -30.94500 -20.67400 1.000 34.68000  ? 84   HIS B CD2 1 
ATOM   4457  C CE1 . HIS B 1 65  ? 48.01900  -31.67700 -21.52500 1.000 32.67000  ? 84   HIS B CE1 1 
ATOM   4458  N NE2 . HIS B 1 65  ? 47.09700  -30.73900 -21.63400 1.000 30.88000  ? 84   HIS B NE2 1 
ATOM   4459  N N   . ASP B 1 66  ? 44.55900  -33.67600 -21.62200 1.000 30.36000  ? 85   ASP B N   1 
ATOM   4460  C CA  . ASP B 1 66  ? 43.70600  -33.16200 -22.69200 1.000 37.36000  ? 85   ASP B CA  1 
ATOM   4461  C C   . ASP B 1 66  ? 42.39300  -33.91900 -22.77200 1.000 39.00000  ? 85   ASP B C   1 
ATOM   4462  O O   . ASP B 1 66  ? 41.35900  -33.33100 -23.10200 1.000 40.12000  ? 85   ASP B O   1 
ATOM   4463  C CB  . ASP B 1 66  ? 44.38600  -33.18500 -24.07100 1.000 33.11000  ? 85   ASP B CB  1 
ATOM   4464  C CG  . ASP B 1 66  ? 44.98700  -34.54600 -24.43300 1.000 38.72000  ? 85   ASP B CG  1 
ATOM   4465  O OD1 . ASP B 1 66  ? 45.49900  -35.26600 -23.55600 1.000 45.43000  ? 85   ASP B OD1 1 
ATOM   4466  O OD2 . ASP B 1 66  ? 44.83200  -34.95700 -25.59800 1.000 47.72000  ? 85   ASP B OD2 1 
ATOM   4467  N N   . ARG B 1 67  ? 42.40600  -35.21200 -22.47500 1.000 39.64000  ? 86   ARG B N   1 
ATOM   4468  C CA  . ARG B 1 67  ? 41.16700  -35.96900 -22.54100 1.000 33.88000  ? 86   ARG B CA  1 
ATOM   4469  C C   . ARG B 1 67  ? 40.20300  -35.55500 -21.43000 1.000 41.48000  ? 86   ARG B C   1 
ATOM   4470  O O   . ARG B 1 67  ? 38.98100  -35.66400 -21.59700 1.000 41.99000  ? 86   ARG B O   1 
ATOM   4471  C CB  . ARG B 1 67  ? 41.49300  -37.46200 -22.48000 1.000 37.98000  ? 86   ARG B CB  1 
ATOM   4472  C CG  . ARG B 1 67  ? 40.32900  -38.35600 -22.78100 1.000 48.24000  ? 86   ARG B CG  1 
ATOM   4473  C CD  . ARG B 1 67  ? 39.88000  -38.17200 -24.23100 1.000 48.98000  ? 86   ARG B CD  1 
ATOM   4474  N NE  . ARG B 1 67  ? 38.63900  -38.89700 -24.47600 1.000 50.49000  ? 86   ARG B NE  1 
ATOM   4475  C CZ  . ARG B 1 67  ? 37.45200  -38.45800 -24.07500 1.000 49.66000  ? 86   ARG B CZ  1 
ATOM   4476  N NH1 . ARG B 1 67  ? 37.33200  -37.33500 -23.38100 1.000 38.91000  ? 86   ARG B NH1 1 
ATOM   4477  N NH2 . ARG B 1 67  ? 36.36400  -39.17100 -24.35900 1.000 58.71000  ? 86   ARG B NH2 1 
ATOM   4478  N N   . PHE B 1 68  ? 40.72300  -35.04600 -20.30600 1.000 35.82000  ? 87   PHE B N   1 
ATOM   4479  C CA  . PHE B 1 68  ? 39.85300  -34.68200 -19.19000 1.000 38.20000  ? 87   PHE B CA  1 
ATOM   4480  C C   . PHE B 1 68  ? 38.96500  -33.48300 -19.48300 1.000 40.26000  ? 87   PHE B C   1 
ATOM   4481  O O   . PHE B 1 68  ? 38.02400  -33.23700 -18.71900 1.000 40.32000  ? 87   PHE B O   1 
ATOM   4482  C CB  . PHE B 1 68  ? 40.65700  -34.38300 -17.92200 1.000 37.04000  ? 87   PHE B CB  1 
ATOM   4483  C CG  . PHE B 1 68  ? 41.26700  -35.59400 -17.28800 1.000 36.86000  ? 87   PHE B CG  1 
ATOM   4484  C CD1 . PHE B 1 68  ? 41.00000  -36.86200 -17.77900 1.000 37.28000  ? 87   PHE B CD1 1 
ATOM   4485  C CD2 . PHE B 1 68  ? 42.06000  -35.47100 -16.16600 1.000 35.03000  ? 87   PHE B CD2 1 
ATOM   4486  C CE1 . PHE B 1 68  ? 41.54800  -37.98200 -17.18400 1.000 35.98000  ? 87   PHE B CE1 1 
ATOM   4487  C CE2 . PHE B 1 68  ? 42.61100  -36.58500 -15.56400 1.000 39.02000  ? 87   PHE B CE2 1 
ATOM   4488  C CZ  . PHE B 1 68  ? 42.35000  -37.84400 -16.07200 1.000 39.09000  ? 87   PHE B CZ  1 
ATOM   4489  N N   . GLY B 1 69  ? 39.23700  -32.72500 -20.54500 1.000 41.08000  ? 88   GLY B N   1 
ATOM   4490  C CA  . GLY B 1 69  ? 38.36400  -31.61000 -20.87200 1.000 45.66000  ? 88   GLY B CA  1 
ATOM   4491  C C   . GLY B 1 69  ? 36.95400  -32.05600 -21.21000 1.000 44.12000  ? 88   GLY B C   1 
ATOM   4492  O O   . GLY B 1 69  ? 35.97800  -31.45600 -20.75900 1.000 43.55000  ? 88   GLY B O   1 
ATOM   4493  N N   . GLY B 1 70  ? 36.83200  -33.12000 -22.00600 1.000 46.74000  ? 89   GLY B N   1 
ATOM   4494  C CA  . GLY B 1 70  ? 35.51900  -33.66800 -22.29700 1.000 39.76000  ? 89   GLY B CA  1 
ATOM   4495  C C   . GLY B 1 70  ? 34.83900  -34.24800 -21.07200 1.000 45.02000  ? 89   GLY B C   1 
ATOM   4496  O O   . GLY B 1 70  ? 33.61200  -34.19100 -20.95000 1.000 45.68000  ? 89   GLY B O   1 
ATOM   4497  N N   . TYR B 1 71  ? 35.62300  -34.84000 -20.16200 1.000 42.84000  ? 90   TYR B N   1 
ATOM   4498  C CA  . TYR B 1 71  ? 35.05400  -35.40300 -18.94000 1.000 41.47000  ? 90   TYR B CA  1 
ATOM   4499  C C   . TYR B 1 71  ? 34.41700  -34.30800 -18.10300 1.000 39.78000  ? 90   TYR B C   1 
ATOM   4500  O O   . TYR B 1 71  ? 33.26500  -34.42300 -17.67100 1.000 45.21000  ? 90   TYR B O   1 
ATOM   4501  C CB  . TYR B 1 71  ? 36.12900  -36.12400 -18.12300 1.000 37.09000  ? 90   TYR B CB  1 
ATOM   4502  C CG  . TYR B 1 71  ? 36.75600  -37.30900 -18.81300 1.000 37.05000  ? 90   TYR B CG  1 
ATOM   4503  C CD1 . TYR B 1 71  ? 36.21000  -37.83500 -19.97300 1.000 37.84000  ? 90   TYR B CD1 1 
ATOM   4504  C CD2 . TYR B 1 71  ? 37.89800  -37.90400 -18.29900 1.000 38.70000  ? 90   TYR B CD2 1 
ATOM   4505  C CE1 . TYR B 1 71  ? 36.79900  -38.90800 -20.60800 1.000 42.71000  ? 90   TYR B CE1 1 
ATOM   4506  C CE2 . TYR B 1 71  ? 38.49000  -38.98300 -18.92400 1.000 32.26000  ? 90   TYR B CE2 1 
ATOM   4507  C CZ  . TYR B 1 71  ? 37.93500  -39.48100 -20.07800 1.000 38.95000  ? 90   TYR B CZ  1 
ATOM   4508  O OH  . TYR B 1 71  ? 38.50900  -40.55400 -20.72100 1.000 39.51000  ? 90   TYR B OH  1 
ATOM   4509  N N   . ALA B 1 72  ? 35.15600  -33.22000 -17.89000 1.000 36.52000  ? 91   ALA B N   1 
ATOM   4510  C CA  . ALA B 1 72  ? 34.64600  -32.10300 -17.10900 1.000 41.38000  ? 91   ALA B CA  1 
ATOM   4511  C C   . ALA B 1 72  ? 33.46500  -31.43500 -17.79400 1.000 45.60000  ? 91   ALA B C   1 
ATOM   4512  O O   . ALA B 1 72  ? 32.53100  -30.99900 -17.11300 1.000 45.49000  ? 91   ALA B O   1 
ATOM   4513  C CB  . ALA B 1 72  ? 35.75400  -31.08400 -16.85400 1.000 38.11000  ? 91   ALA B CB  1 
ATOM   4514  N N   . GLN B 1 73  ? 33.48500  -31.33600 -19.12800 1.000 46.44000  ? 92   GLN B N   1 
ATOM   4515  C CA  . GLN B 1 73  ? 32.33200  -30.77700 -19.82300 1.000 53.12000  ? 92   GLN B CA  1 
ATOM   4516  C C   . GLN B 1 73  ? 31.06000  -31.51000 -19.42500 1.000 54.37000  ? 92   GLN B C   1 
ATOM   4517  O O   . GLN B 1 73  ? 29.99600  -30.89700 -19.27600 1.000 53.04000  ? 92   GLN B O   1 
ATOM   4518  C CB  . GLN B 1 73  ? 32.48900  -30.85600 -21.34000 1.000 54.73000  ? 92   GLN B CB  1 
ATOM   4519  C CG  . GLN B 1 73  ? 31.28000  -30.19700 -21.96500 1.000 58.90000  ? 92   GLN B CG  1 
ATOM   4520  C CD  . GLN B 1 73  ? 31.42100  -28.69300 -22.01700 1.000 64.46000  ? 92   GLN B CD  1 
ATOM   4521  O OE1 . GLN B 1 73  ? 32.05900  -28.15600 -22.92100 1.000 66.28000  ? 92   GLN B OE1 1 
ATOM   4522  N NE2 . GLN B 1 73  ? 31.00500  -28.02500 -20.93900 1.000 71.88000  ? 92   GLN B NE2 1 
ATOM   4523  N N   . SER B 1 74  ? 31.16200  -32.82300 -19.23600 1.000 52.47000  ? 93   SER B N   1 
ATOM   4524  C CA  . SER B 1 74  ? 30.05000  -33.68300 -18.87800 1.000 46.29000  ? 93   SER B CA  1 
ATOM   4525  C C   . SER B 1 74  ? 29.87700  -33.81300 -17.37100 1.000 44.21000  ? 93   SER B C   1 
ATOM   4526  O O   . SER B 1 74  ? 29.07900  -34.64000 -16.92300 1.000 45.23000  ? 93   SER B O   1 
ATOM   4527  C CB  . SER B 1 74  ? 30.25300  -35.06100 -19.49900 1.000 44.43000  ? 93   SER B CB  1 
ATOM   4528  O OG  . SER B 1 74  ? 30.37600  -34.94400 -20.90500 1.000 50.46000  ? 93   SER B OG  1 
ATOM   4529  N N   . GLY B 1 75  ? 30.61800  -33.03500 -16.58400 1.000 46.71000  ? 94   GLY B N   1 
ATOM   4530  C CA  . GLY B 1 75  ? 30.50600  -33.11200 -15.14100 1.000 40.32000  ? 94   GLY B CA  1 
ATOM   4531  C C   . GLY B 1 75  ? 30.97900  -34.41700 -14.54400 1.000 44.76000  ? 94   GLY B C   1 
ATOM   4532  O O   . GLY B 1 75  ? 30.53400  -34.78800 -13.45000 1.000 43.66000  ? 94   GLY B O   1 
ATOM   4533  N N   . LEU B 1 76  ? 31.86900  -35.13200 -15.23300 1.000 38.59000  ? 95   LEU B N   1 
ATOM   4534  C CA  . LEU B 1 76  ? 32.27000  -36.45900 -14.80100 1.000 34.55000  ? 95   LEU B CA  1 
ATOM   4535  C C   . LEU B 1 76  ? 33.42000  -36.43800 -13.81300 1.000 42.51000  ? 95   LEU B C   1 
ATOM   4536  O O   . LEU B 1 76  ? 33.75300  -37.49000 -13.26000 1.000 45.28000  ? 95   LEU B O   1 
ATOM   4537  C CB  . LEU B 1 76  ? 32.65900  -37.30700 -16.00500 1.000 36.52000  ? 95   LEU B CB  1 
ATOM   4538  C CG  . LEU B 1 76  ? 31.52200  -37.51100 -17.00100 1.000 44.95000  ? 95   LEU B CG  1 
ATOM   4539  C CD1 . LEU B 1 76  ? 32.00600  -38.31300 -18.20200 1.000 44.25000  ? 95   LEU B CD1 1 
ATOM   4540  C CD2 . LEU B 1 76  ? 30.31300  -38.16400 -16.33900 1.000 36.79000  ? 95   LEU B CD2 1 
ATOM   4541  N N   . LEU B 1 77  ? 34.03400  -35.28200 -13.58200 1.000 37.46000  ? 96   LEU B N   1 
ATOM   4542  C CA  . LEU B 1 77  ? 35.19000  -35.17300 -12.71200 1.000 37.53000  ? 96   LEU B CA  1 
ATOM   4543  C C   . LEU B 1 77  ? 34.86100  -34.27200 -11.53600 1.000 38.93000  ? 96   LEU B C   1 
ATOM   4544  O O   . LEU B 1 77  ? 34.22000  -33.23000 -11.70200 1.000 38.82000  ? 96   LEU B O   1 
ATOM   4545  C CB  . LEU B 1 77  ? 36.40400  -34.62600 -13.45800 1.000 35.17000  ? 96   LEU B CB  1 
ATOM   4546  C CG  . LEU B 1 77  ? 37.04300  -35.53800 -14.50600 1.000 37.92000  ? 96   LEU B CG  1 
ATOM   4547  C CD1 . LEU B 1 77  ? 38.15200  -34.79500 -15.22000 1.000 33.93000  ? 96   LEU B CD1 1 
ATOM   4548  C CD2 . LEU B 1 77  ? 37.57400  -36.81400 -13.88200 1.000 31.53000  ? 96   LEU B CD2 1 
ATOM   4549  N N   . ALA B 1 78  ? 35.29700  -34.68900 -10.35100 1.000 38.19000  ? 97   ALA B N   1 
ATOM   4550  C CA  . ALA B 1 78  ? 35.14700  -33.86200 -9.16600  1.000 38.26000  ? 97   ALA B CA  1 
ATOM   4551  C C   . ALA B 1 78  ? 36.06900  -32.65800 -9.24500  1.000 39.26000  ? 97   ALA B C   1 
ATOM   4552  O O   . ALA B 1 78  ? 37.17500  -32.73100 -9.78300  1.000 41.27000  ? 97   ALA B O   1 
ATOM   4553  C CB  . ALA B 1 78  ? 35.46000  -34.67100 -7.90500  1.000 35.78000  ? 97   ALA B CB  1 
ATOM   4554  N N   . GLU B 1 79  ? 35.60300  -31.54400 -8.71500  1.000 40.15000  ? 98   GLU B N   1 
ATOM   4555  C CA  . GLU B 1 79  ? 36.42000  -30.35000 -8.61600  1.000 39.48000  ? 98   GLU B CA  1 
ATOM   4556  C C   . GLU B 1 79  ? 37.31400  -30.50200 -7.39000  1.000 45.66000  ? 98   GLU B C   1 
ATOM   4557  O O   . GLU B 1 79  ? 36.81500  -30.69700 -6.27800  1.000 49.62000  ? 98   GLU B O   1 
ATOM   4558  C CB  . GLU B 1 79  ? 35.49100  -29.13900 -8.52200  1.000 42.94000  ? 98   GLU B CB  1 
ATOM   4559  C CG  . GLU B 1 79  ? 36.08600  -27.74700 -8.65800  1.000 57.53000  ? 98   GLU B CG  1 
ATOM   4560  C CD  . GLU B 1 79  ? 34.98700  -26.67600 -8.76900  1.000 72.49000  ? 98   GLU B CD  1 
ATOM   4561  O OE1 . GLU B 1 79  ? 33.78300  -27.04800 -8.73100  1.000 63.39000  ? 98   GLU B OE1 1 
ATOM   4562  O OE2 . GLU B 1 79  ? 35.32600  -25.47100 -8.89000  1.000 70.70000  ? 98   GLU B OE2 1 
ATOM   4563  N N   . ILE B 1 80  ? 38.63200  -30.47700 -7.58900  1.000 40.27000  ? 99   ILE B N   1 
ATOM   4564  C CA  . ILE B 1 80  ? 39.55900  -30.78100 -6.50400  1.000 44.66000  ? 99   ILE B CA  1 
ATOM   4565  C C   . ILE B 1 80  ? 39.93200  -29.48600 -5.80200  1.000 47.12000  ? 99   ILE B C   1 
ATOM   4566  O O   . ILE B 1 80  ? 39.73600  -28.38400 -6.32400  1.000 46.09000  ? 99   ILE B O   1 
ATOM   4567  C CB  . ILE B 1 80  ? 40.83500  -31.53500 -6.95700  1.000 35.63000  ? 99   ILE B CB  1 
ATOM   4568  C CG1 . ILE B 1 80  ? 41.66700  -30.66500 -7.89600  1.000 34.23000  ? 99   ILE B CG1 1 
ATOM   4569  C CG2 . ILE B 1 80  ? 40.46800  -32.87500 -7.57600  1.000 37.24000  ? 99   ILE B CG2 1 
ATOM   4570  C CD1 . ILE B 1 80  ? 43.10100  -31.13200 -8.05300  1.000 33.58000  ? 99   ILE B CD1 1 
ATOM   4571  N N   . THR B 1 81  ? 40.46900  -29.61800 -4.58900  1.000 39.18000  ? 100  THR B N   1 
ATOM   4572  C CA  . THR B 1 81  ? 40.75500  -28.46300 -3.73900  1.000 45.47000  ? 100  THR B CA  1 
ATOM   4573  C C   . THR B 1 81  ? 42.07300  -28.62600 -2.97900  1.000 46.60000  ? 100  THR B C   1 
ATOM   4574  O O   . THR B 1 81  ? 42.09800  -28.68000 -1.74500  1.000 43.80000  ? 100  THR B O   1 
ATOM   4575  C CB  . THR B 1 81  ? 39.57700  -28.21700 -2.78900  1.000 54.45000  ? 100  THR B CB  1 
ATOM   4576  O OG1 . THR B 1 81  ? 39.84600  -27.07500 -1.96800  1.000 70.21000  ? 100  THR B OG1 1 
ATOM   4577  C CG2 . THR B 1 81  ? 39.26200  -29.47000 -1.93200  1.000 49.07000  ? 100  THR B CG2 1 
ATOM   4578  N N   . PRO B 1 82  ? 43.20200  -28.66200 -3.68700  1.000 45.64000  ? 101  PRO B N   1 
ATOM   4579  C CA  . PRO B 1 82  ? 44.49000  -28.66600 -2.98300  1.000 42.46000  ? 101  PRO B CA  1 
ATOM   4580  C C   . PRO B 1 82  ? 44.78100  -27.30800 -2.36300  1.000 36.09000  ? 101  PRO B C   1 
ATOM   4581  O O   . PRO B 1 82  ? 44.43500  -26.25900 -2.90900  1.000 39.65000  ? 101  PRO B O   1 
ATOM   4582  C CB  . PRO B 1 82  ? 45.49900  -28.99800 -4.08800  1.000 40.96000  ? 101  PRO B CB  1 
ATOM   4583  C CG  . PRO B 1 82  ? 44.85500  -28.48200 -5.32100  1.000 40.01000  ? 101  PRO B CG  1 
ATOM   4584  C CD  . PRO B 1 82  ? 43.38200  -28.68400 -5.15000  1.000 42.02000  ? 101  PRO B CD  1 
ATOM   4585  N N   . ALA B 1 83  ? 45.43300  -27.33400 -1.21000  1.000 34.68000  ? 102  ALA B N   1 
ATOM   4586  C CA  . ALA B 1 83  ? 45.79300  -26.09700 -0.53800  1.000 35.84000  ? 102  ALA B CA  1 
ATOM   4587  C C   . ALA B 1 83  ? 46.85300  -25.33700 -1.33800  1.000 40.40000  ? 102  ALA B C   1 
ATOM   4588  O O   . ALA B 1 83  ? 47.58800  -25.90600 -2.15500  1.000 40.43000  ? 102  ALA B O   1 
ATOM   4589  C CB  . ALA B 1 83  ? 46.29200  -26.39000 0.88000   1.000 26.07000  ? 102  ALA B CB  1 
ATOM   4590  N N   . ALA B 1 84  ? 46.91700  -24.02500 -1.09100  1.000 40.76000  ? 103  ALA B N   1 
ATOM   4591  C CA  . ALA B 1 84  ? 47.84800  -23.16800 -1.81900  1.000 37.82000  ? 103  ALA B CA  1 
ATOM   4592  C C   . ALA B 1 84  ? 49.28100  -23.67100 -1.69000  1.000 39.70000  ? 103  ALA B C   1 
ATOM   4593  O O   . ALA B 1 84  ? 50.01500  -23.75700 -2.68200  1.000 48.03000  ? 103  ALA B O   1 
ATOM   4594  C CB  . ALA B 1 84  ? 47.73100  -21.72900 -1.31500  1.000 41.47000  ? 103  ALA B CB  1 
ATOM   4595  N N   . ALA B 1 85  ? 49.69400  -24.01600 -0.46800  1.000 40.53000  ? 104  ALA B N   1 
ATOM   4596  C CA  . ALA B 1 85  ? 51.05200  -24.50700 -0.25400  1.000 39.46000  ? 104  ALA B CA  1 
ATOM   4597  C C   . ALA B 1 85  ? 51.29900  -25.80200 -1.01200  1.000 43.31000  ? 104  ALA B C   1 
ATOM   4598  O O   . ALA B 1 85  ? 52.38200  -25.99800 -1.58100  1.000 43.49000  ? 104  ALA B O   1 
ATOM   4599  C CB  . ALA B 1 85  ? 51.31300  -24.70500 1.23600   1.000 39.19000  ? 104  ALA B CB  1 
ATOM   4600  N N   . PHE B 1 86  ? 50.30800  -26.69900 -1.02900  1.000 37.38000  ? 105  PHE B N   1 
ATOM   4601  C CA  . PHE B 1 86  ? 50.45400  -27.92800 -1.79900  1.000 38.47000  ? 105  PHE B CA  1 
ATOM   4602  C C   . PHE B 1 86  ? 50.69500  -27.61900 -3.27000  1.000 42.58000  ? 105  PHE B C   1 
ATOM   4603  O O   . PHE B 1 86  ? 51.53300  -28.25500 -3.92000  1.000 42.59000  ? 105  PHE B O   1 
ATOM   4604  C CB  . PHE B 1 86  ? 49.21400  -28.80500 -1.64000  1.000 40.13000  ? 105  PHE B CB  1 
ATOM   4605  C CG  . PHE B 1 86  ? 49.32700  -30.13800 -2.31500  1.000 38.29000  ? 105  PHE B CG  1 
ATOM   4606  C CD1 . PHE B 1 86  ? 49.95800  -31.19300 -1.68200  1.000 35.19000  ? 105  PHE B CD1 1 
ATOM   4607  C CD2 . PHE B 1 86  ? 48.82700  -30.33000 -3.59500  1.000 44.77000  ? 105  PHE B CD2 1 
ATOM   4608  C CE1 . PHE B 1 86  ? 50.06800  -32.42800 -2.30100  1.000 40.67000  ? 105  PHE B CE1 1 
ATOM   4609  C CE2 . PHE B 1 86  ? 48.94100  -31.56000 -4.22900  1.000 41.23000  ? 105  PHE B CE2 1 
ATOM   4610  C CZ  . PHE B 1 86  ? 49.56200  -32.61200 -3.58100  1.000 38.96000  ? 105  PHE B CZ  1 
ATOM   4611  N N   . GLN B 1 87  ? 49.97500  -26.63700 -3.81300  1.000 42.51000  ? 106  GLN B N   1 
ATOM   4612  C CA  . GLN B 1 87  ? 50.13200  -26.33700 -5.22800  1.000 41.04000  ? 106  GLN B CA  1 
ATOM   4613  C C   . GLN B 1 87  ? 51.53800  -25.84200 -5.53100  1.000 42.78000  ? 106  GLN B C   1 
ATOM   4614  O O   . GLN B 1 87  ? 52.07400  -26.13300 -6.60200  1.000 45.63000  ? 106  GLN B O   1 
ATOM   4615  C CB  . GLN B 1 87  ? 49.09100  -25.31700 -5.69100  1.000 36.34000  ? 106  GLN B CB  1 
ATOM   4616  C CG  . GLN B 1 87  ? 47.64500  -25.74200 -5.46100  1.000 44.79000  ? 106  GLN B CG  1 
ATOM   4617  C CD  . GLN B 1 87  ? 46.66000  -24.82200 -6.15700  1.000 43.38000  ? 106  GLN B CD  1 
ATOM   4618  O OE1 . GLN B 1 87  ? 47.02000  -24.09300 -7.07900  1.000 57.77000  ? 106  GLN B OE1 1 
ATOM   4619  N NE2 . GLN B 1 87  ? 45.44900  -24.75900 -5.63300  1.000 41.29000  ? 106  GLN B NE2 1 
ATOM   4620  N N   . ASP B 1 88  ? 52.16600  -25.09700 -4.61000  1.000 41.71000  ? 107  ASP B N   1 
ATOM   4621  C CA  . ASP B 1 88  ? 53.54000  -24.69300 -4.92500  1.000 45.93000  ? 107  ASP B CA  1 
ATOM   4622  C C   . ASP B 1 88  ? 54.52300  -25.85400 -4.98600  1.000 40.82000  ? 107  ASP B C   1 
ATOM   4623  O O   . ASP B 1 88  ? 55.64800  -25.65600 -5.44700  1.000 43.49000  ? 107  ASP B O   1 
ATOM   4624  C CB  . ASP B 1 88  ? 54.16800  -23.67800 -3.96300  1.000 52.54000  ? 107  ASP B CB  1 
ATOM   4625  C CG  . ASP B 1 88  ? 53.69500  -22.26300 -4.20400  1.000 60.84000  ? 107  ASP B CG  1 
ATOM   4626  O OD1 . ASP B 1 88  ? 52.73700  -22.07800 -4.98400  1.000 66.79000  ? 107  ASP B OD1 1 
ATOM   4627  O OD2 . ASP B 1 88  ? 54.47200  -21.34600 -3.81900  1.000 83.57000  ? 107  ASP B OD2 1 
ATOM   4628  N N   . LYS B 1 89  ? 54.16500  -27.03000 -4.48800  1.000 40.04000  ? 108  LYS B N   1 
ATOM   4629  C CA  . LYS B 1 89  ? 55.03000  -28.18800 -4.64000  1.000 39.20000  ? 108  LYS B CA  1 
ATOM   4630  C C   . LYS B 1 89  ? 55.10500  -28.66900 -6.08400  1.000 43.13000  ? 108  LYS B C   1 
ATOM   4631  O O   . LYS B 1 89  ? 55.95400  -29.51000 -6.40200  1.000 36.34000  ? 108  LYS B O   1 
ATOM   4632  C CB  . LYS B 1 89  ? 54.50800  -29.30100 -3.73700  1.000 40.18000  ? 108  LYS B CB  1 
ATOM   4633  C CG  . LYS B 1 89  ? 54.63700  -28.95100 -2.27900  1.000 42.62000  ? 108  LYS B CG  1 
ATOM   4634  C CD  . LYS B 1 89  ? 53.70800  -29.77400 -1.41000  1.000 44.61000  ? 108  LYS B CD  1 
ATOM   4635  C CE  . LYS B 1 89  ? 54.14400  -31.20800 -1.27200  1.000 50.48000  ? 108  LYS B CE  1 
ATOM   4636  N NZ  . LYS B 1 89  ? 53.33400  -31.85300 -0.20200  1.000 43.24000  ? 108  LYS B NZ  1 
ATOM   4637  N N   . LEU B 1 90  ? 54.23400  -28.16200 -6.95000  1.000 39.34000  ? 109  LEU B N   1 
ATOM   4638  C CA  . LEU B 1 90  ? 54.15600  -28.54100 -8.34900  1.000 38.20000  ? 109  LEU B CA  1 
ATOM   4639  C C   . LEU B 1 90  ? 54.45400  -27.33300 -9.22200  1.000 43.40000  ? 109  LEU B C   1 
ATOM   4640  O O   . LEU B 1 90  ? 54.23000  -26.18600 -8.81400  1.000 42.53000  ? 109  LEU B O   1 
ATOM   4641  C CB  . LEU B 1 90  ? 52.76800  -29.09300 -8.68500  1.000 42.61000  ? 109  LEU B CB  1 
ATOM   4642  C CG  . LEU B 1 90  ? 52.47100  -30.57400 -8.45200  1.000 37.22000  ? 109  LEU B CG  1 
ATOM   4643  C CD1 . LEU B 1 90  ? 52.56600  -30.95300 -6.99800  1.000 35.90000  ? 109  LEU B CD1 1 
ATOM   4644  C CD2 . LEU B 1 90  ? 51.06900  -30.86900 -8.96900  1.000 38.09000  ? 109  LEU B CD2 1 
ATOM   4645  N N   . TYR B 1 91  ? 54.96900  -27.60000 -10.42700 1.000 40.72000  ? 110  TYR B N   1 
ATOM   4646  C CA  . TYR B 1 91  ? 55.30700  -26.51100 -11.34100 1.000 40.13000  ? 110  TYR B CA  1 
ATOM   4647  C C   . TYR B 1 91  ? 54.03800  -25.78500 -11.75500 1.000 32.25000  ? 110  TYR B C   1 
ATOM   4648  O O   . TYR B 1 91  ? 53.04300  -26.43600 -12.09200 1.000 36.23000  ? 110  TYR B O   1 
ATOM   4649  C CB  . TYR B 1 91  ? 56.02800  -27.01300 -12.57700 1.000 34.89000  ? 110  TYR B CB  1 
ATOM   4650  C CG  . TYR B 1 91  ? 57.40500  -27.52900 -12.28900 1.000 34.62000  ? 110  TYR B CG  1 
ATOM   4651  C CD1 . TYR B 1 91  ? 58.48100  -26.65400 -12.13700 1.000 36.03000  ? 110  TYR B CD1 1 
ATOM   4652  C CD2 . TYR B 1 91  ? 57.63400  -28.89100 -12.17500 1.000 31.96000  ? 110  TYR B CD2 1 
ATOM   4653  C CE1 . TYR B 1 91  ? 59.75200  -27.12900 -11.87200 1.000 35.64000  ? 110  TYR B CE1 1 
ATOM   4654  C CE2 . TYR B 1 91  ? 58.89500  -29.37700 -11.91600 1.000 42.59000  ? 110  TYR B CE2 1 
ATOM   4655  C CZ  . TYR B 1 91  ? 59.95000  -28.49500 -11.76100 1.000 38.38000  ? 110  TYR B CZ  1 
ATOM   4656  O OH  . TYR B 1 91  ? 61.19500  -29.00400 -11.50300 1.000 43.85000  ? 110  TYR B OH  1 
ATOM   4657  N N   . PRO B 1 92  ? 54.02900  -24.45200 -11.72900 1.000 39.77000  ? 111  PRO B N   1 
ATOM   4658  C CA  . PRO B 1 92  ? 52.77300  -23.72600 -11.98300 1.000 42.71000  ? 111  PRO B CA  1 
ATOM   4659  C C   . PRO B 1 92  ? 52.14600  -24.07100 -13.31600 1.000 39.43000  ? 111  PRO B C   1 
ATOM   4660  O O   . PRO B 1 92  ? 50.91400  -24.18900 -13.39700 1.000 44.98000  ? 111  PRO B O   1 
ATOM   4661  C CB  . PRO B 1 92  ? 53.20300  -22.25400 -11.91800 1.000 42.05000  ? 111  PRO B CB  1 
ATOM   4662  C CG  . PRO B 1 92  ? 54.41700  -22.25800 -11.07200 1.000 45.55000  ? 111  PRO B CG  1 
ATOM   4663  C CD  . PRO B 1 92  ? 55.13000  -23.54900 -11.35000 1.000 41.11000  ? 111  PRO B CD  1 
ATOM   4664  N N   . PHE B 1 93  ? 52.95200  -24.26600 -14.36600 1.000 34.91000  ? 112  PHE B N   1 
ATOM   4665  C CA  . PHE B 1 93  ? 52.35500  -24.49100 -15.67600 1.000 35.03000  ? 112  PHE B CA  1 
ATOM   4666  C C   . PHE B 1 93  ? 51.62300  -25.82200 -15.72100 1.000 37.46000  ? 112  PHE B C   1 
ATOM   4667  O O   . PHE B 1 93  ? 50.64100  -25.95600 -16.45700 1.000 40.31000  ? 112  PHE B O   1 
ATOM   4668  C CB  . PHE B 1 93  ? 53.41000  -24.39800 -16.78400 1.000 40.05000  ? 112  PHE B CB  1 
ATOM   4669  C CG  . PHE B 1 93  ? 54.26800  -25.62500 -16.94900 1.000 43.66000  ? 112  PHE B CG  1 
ATOM   4670  C CD1 . PHE B 1 93  ? 55.39300  -25.82500 -16.16300 1.000 34.81000  ? 112  PHE B CD1 1 
ATOM   4671  C CD2 . PHE B 1 93  ? 53.98000  -26.55100 -17.94700 1.000 41.96000  ? 112  PHE B CD2 1 
ATOM   4672  C CE1 . PHE B 1 93  ? 56.18800  -26.95300 -16.34200 1.000 37.97000  ? 112  PHE B CE1 1 
ATOM   4673  C CE2 . PHE B 1 93  ? 54.77200  -27.67600 -18.13300 1.000 43.09000  ? 112  PHE B CE2 1 
ATOM   4674  C CZ  . PHE B 1 93  ? 55.88000  -27.87700 -17.33100 1.000 36.02000  ? 112  PHE B CZ  1 
ATOM   4675  N N   . THR B 1 94  ? 52.03300  -26.79700 -14.90200 1.000 33.59000  ? 113  THR B N   1 
ATOM   4676  C CA  . THR B 1 94  ? 51.29600  -28.05800 -14.87800 1.000 33.55000  ? 113  THR B CA  1 
ATOM   4677  C C   . THR B 1 94  ? 49.87800  -27.87100 -14.35100 1.000 32.72000  ? 113  THR B C   1 
ATOM   4678  O O   . THR B 1 94  ? 48.97200  -28.59900 -14.76700 1.000 31.54000  ? 113  THR B O   1 
ATOM   4679  C CB  . THR B 1 94  ? 52.02000  -29.11700 -14.04100 1.000 35.35000  ? 113  THR B CB  1 
ATOM   4680  O OG1 . THR B 1 94  ? 52.05300  -28.71400 -12.66200 1.000 31.36000  ? 113  THR B OG1 1 
ATOM   4681  C CG2 . THR B 1 94  ? 53.44500  -29.36000 -14.56900 1.000 32.53000  ? 113  THR B CG2 1 
ATOM   4682  N N   . TRP B 1 95  ? 49.65900  -26.92000 -13.43200 1.000 35.73000  ? 114  TRP B N   1 
ATOM   4683  C CA  . TRP B 1 95  ? 48.29200  -26.68200 -12.97100 1.000 41.19000  ? 114  TRP B CA  1 
ATOM   4684  C C   . TRP B 1 95  ? 47.42200  -26.11500 -14.08500 1.000 42.09000  ? 114  TRP B C   1 
ATOM   4685  O O   . TRP B 1 95  ? 46.21700  -26.39100 -14.12100 1.000 40.99000  ? 114  TRP B O   1 
ATOM   4686  C CB  . TRP B 1 95  ? 48.24000  -25.75200 -11.74600 1.000 39.99000  ? 114  TRP B CB  1 
ATOM   4687  C CG  . TRP B 1 95  ? 48.73400  -26.36500 -10.45200 1.000 37.98000  ? 114  TRP B CG  1 
ATOM   4688  C CD1 . TRP B 1 95  ? 49.88000  -26.05600 -9.78600  1.000 37.30000  ? 114  TRP B CD1 1 
ATOM   4689  C CD2 . TRP B 1 95  ? 48.10800  -27.41500 -9.70000  1.000 36.01000  ? 114  TRP B CD2 1 
ATOM   4690  N NE1 . TRP B 1 95  ? 50.00100  -26.82900 -8.65400  1.000 34.63000  ? 114  TRP B NE1 1 
ATOM   4691  C CE2 . TRP B 1 95  ? 48.92900  -27.67900 -8.58600  1.000 36.97000  ? 114  TRP B CE2 1 
ATOM   4692  C CE3 . TRP B 1 95  ? 46.93600  -28.15700 -9.86100  1.000 32.69000  ? 114  TRP B CE3 1 
ATOM   4693  C CZ2 . TRP B 1 95  ? 48.61000  -28.65000 -7.63400  1.000 38.71000  ? 114  TRP B CZ2 1 
ATOM   4694  C CZ3 . TRP B 1 95  ? 46.62400  -29.12300 -8.91900  1.000 34.72000  ? 114  TRP B CZ3 1 
ATOM   4695  C CH2 . TRP B 1 95  ? 47.45700  -29.36000 -7.82000  1.000 33.50000  ? 114  TRP B CH2 1 
ATOM   4696  N N   . ASP B 1 96  ? 48.00500  -25.33900 -15.00700 1.000 41.35000  ? 115  ASP B N   1 
ATOM   4697  C CA  . ASP B 1 96  ? 47.20500  -24.85200 -16.12700 1.000 41.51000  ? 115  ASP B CA  1 
ATOM   4698  C C   . ASP B 1 96  ? 46.62400  -26.00600 -16.93200 1.000 40.17000  ? 115  ASP B C   1 
ATOM   4699  O O   . ASP B 1 96  ? 45.48200  -25.92100 -17.40000 1.000 42.28000  ? 115  ASP B O   1 
ATOM   4700  C CB  . ASP B 1 96  ? 48.02600  -23.94200 -17.03800 1.000 36.45000  ? 115  ASP B CB  1 
ATOM   4701  C CG  . ASP B 1 96  ? 48.39100  -22.63200 -16.37900 1.000 45.05000  ? 115  ASP B CG  1 
ATOM   4702  O OD1 . ASP B 1 96  ? 47.71200  -22.23500 -15.41400 1.000 55.28000  ? 115  ASP B OD1 1 
ATOM   4703  O OD2 . ASP B 1 96  ? 49.34100  -21.97400 -16.85200 1.000 58.66000  ? 115  ASP B OD2 1 
ATOM   4704  N N   . ALA B 1 97  ? 47.37300  -27.10400 -17.06900 1.000 37.17000  ? 116  ALA B N   1 
ATOM   4705  C CA  . ALA B 1 97  ? 46.89500  -28.23900 -17.85200 1.000 35.17000  ? 116  ALA B CA  1 
ATOM   4706  C C   . ALA B 1 97  ? 45.63700  -28.87200 -17.27500 1.000 34.87000  ? 116  ALA B C   1 
ATOM   4707  O O   . ALA B 1 97  ? 44.91500  -29.54900 -18.01200 1.000 35.16000  ? 116  ALA B O   1 
ATOM   4708  C CB  . ALA B 1 97  ? 47.98700  -29.30100 -17.96600 1.000 27.96000  ? 116  ALA B CB  1 
ATOM   4709  N N   . VAL B 1 98  ? 45.36000  -28.68500 -15.98400 1.000 37.25000  ? 117  VAL B N   1 
ATOM   4710  C CA  . VAL B 1 98  ? 44.23900  -29.35000 -15.32500 1.000 30.42000  ? 117  VAL B CA  1 
ATOM   4711  C C   . VAL B 1 98  ? 43.18000  -28.34800 -14.86500 1.000 38.86000  ? 117  VAL B C   1 
ATOM   4712  O O   . VAL B 1 98  ? 42.38700  -28.65000 -13.97100 1.000 39.33000  ? 117  VAL B O   1 
ATOM   4713  C CB  . VAL B 1 98  ? 44.71100  -30.22900 -14.15800 1.000 34.02000  ? 117  VAL B CB  1 
ATOM   4714  C CG1 . VAL B 1 98  ? 45.57900  -31.36200 -14.67000 1.000 33.40000  ? 117  VAL B CG1 1 
ATOM   4715  C CG2 . VAL B 1 98  ? 45.45400  -29.38700 -13.11800 1.000 29.82000  ? 117  VAL B CG2 1 
ATOM   4716  N N   . ARG B 1 99  ? 43.16400  -27.15300 -15.44900 1.000 39.26000  ? 118  ARG B N   1 
ATOM   4717  C CA  . ARG B 1 99  ? 42.03200  -26.25500 -15.30000 1.000 40.89000  ? 118  ARG B CA  1 
ATOM   4718  C C   . ARG B 1 99  ? 41.07700  -26.48800 -16.45300 1.000 40.58000  ? 118  ARG B C   1 
ATOM   4719  O O   . ARG B 1 99  ? 41.49700  -26.57200 -17.60900 1.000 38.50000  ? 118  ARG B O   1 
ATOM   4720  C CB  . ARG B 1 99  ? 42.47000  -24.79700 -15.31400 1.000 42.55000  ? 118  ARG B CB  1 
ATOM   4721  C CG  . ARG B 1 99  ? 43.42400  -24.45400 -14.23200 1.000 44.27000  ? 118  ARG B CG  1 
ATOM   4722  C CD  . ARG B 1 99  ? 43.91900  -23.04400 -14.40500 1.000 56.18000  ? 118  ARG B CD  1 
ATOM   4723  N NE  . ARG B 1 99  ? 45.13300  -22.85500 -13.62600 1.000 62.90000  ? 118  ARG B NE  1 
ATOM   4724  C CZ  . ARG B 1 99  ? 45.14500  -22.53000 -12.34400 1.000 55.73000  ? 118  ARG B CZ  1 
ATOM   4725  N NH1 . ARG B 1 99  ? 44.02200  -22.30500 -11.68000 1.000 59.99000  ? 118  ARG B NH1 1 
ATOM   4726  N NH2 . ARG B 1 99  ? 46.31000  -22.43800 -11.71100 1.000 56.03000  ? 118  ARG B NH2 1 
ATOM   4727  N N   . TYR B 1 100 ? 39.79100  -26.60200 -16.14400 1.000 39.20000  ? 119  TYR B N   1 
ATOM   4728  C CA  . TYR B 1 100 ? 38.78500  -26.62400 -17.19300 1.000 41.46000  ? 119  TYR B CA  1 
ATOM   4729  C C   . TYR B 1 100 ? 37.78500  -25.52300 -16.90000 1.000 41.97000  ? 119  TYR B C   1 
ATOM   4730  O O   . TYR B 1 100 ? 37.13700  -25.53000 -15.84900 1.000 52.16000  ? 119  TYR B O   1 
ATOM   4731  C CB  . TYR B 1 100 ? 38.08500  -27.97600 -17.30300 1.000 31.78000  ? 119  TYR B CB  1 
ATOM   4732  C CG  . TYR B 1 100 ? 37.22500  -28.05000 -18.53300 1.000 49.30000  ? 119  TYR B CG  1 
ATOM   4733  C CD1 . TYR B 1 100 ? 37.78700  -28.33100 -19.77400 1.000 43.35000  ? 119  TYR B CD1 1 
ATOM   4734  C CD2 . TYR B 1 100 ? 35.86300  -27.78600 -18.47000 1.000 45.65000  ? 119  TYR B CD2 1 
ATOM   4735  C CE1 . TYR B 1 100 ? 37.01500  -28.38900 -20.91000 1.000 45.70000  ? 119  TYR B CE1 1 
ATOM   4736  C CE2 . TYR B 1 100 ? 35.08200  -27.83800 -19.60500 1.000 44.23000  ? 119  TYR B CE2 1 
ATOM   4737  C CZ  . TYR B 1 100 ? 35.66000  -28.14000 -20.82200 1.000 51.15000  ? 119  TYR B CZ  1 
ATOM   4738  O OH  . TYR B 1 100 ? 34.88700  -28.19700 -21.96300 1.000 56.07000  ? 119  TYR B OH  1 
ATOM   4739  N N   . ASN B 1 101 ? 37.69400  -24.56600 -17.81100 1.000 39.40000  ? 120  ASN B N   1 
ATOM   4740  C CA  . ASN B 1 101 ? 36.79200  -23.43500 -17.66600 1.000 49.19000  ? 120  ASN B CA  1 
ATOM   4741  C C   . ASN B 1 101 ? 36.94600  -22.79500 -16.28900 1.000 45.72000  ? 120  ASN B C   1 
ATOM   4742  O O   . ASN B 1 101 ? 35.96300  -22.43900 -15.63800 1.000 51.51000  ? 120  ASN B O   1 
ATOM   4743  C CB  . ASN B 1 101 ? 35.34000  -23.85300 -17.89500 1.000 52.57000  ? 120  ASN B CB  1 
ATOM   4744  C CG  . ASN B 1 101 ? 34.46900  -22.69100 -18.31600 1.000 50.83000  ? 120  ASN B CG  1 
ATOM   4745  O OD1 . ASN B 1 101 ? 34.97400  -21.66000 -18.76200 1.000 49.56000  ? 120  ASN B OD1 1 
ATOM   4746  N ND2 . ASN B 1 101 ? 33.16600  -22.81500 -18.09300 1.000 54.91000  ? 120  ASN B ND2 1 
ATOM   4747  N N   . GLY B 1 102 ? 38.19400  -22.68600 -15.82500 1.000 43.71000  ? 121  GLY B N   1 
ATOM   4748  C CA  . GLY B 1 102 ? 38.50000  -22.06800 -14.55100 1.000 43.64000  ? 121  GLY B CA  1 
ATOM   4749  C C   . GLY B 1 102 ? 38.50600  -22.99700 -13.35700 1.000 43.81000  ? 121  GLY B C   1 
ATOM   4750  O O   . GLY B 1 102 ? 38.85500  -22.55800 -12.25000 1.000 52.55000  ? 121  GLY B O   1 
ATOM   4751  N N   . LYS B 1 103 ? 38.14900  -24.26400 -13.53800 1.000 43.41000  ? 122  LYS B N   1 
ATOM   4752  C CA  . LYS B 1 103 ? 38.02100  -25.20800 -12.43400 1.000 48.95000  ? 122  LYS B CA  1 
ATOM   4753  C C   . LYS B 1 103 ? 39.21400  -26.15300 -12.41000 1.000 41.72000  ? 122  LYS B C   1 
ATOM   4754  O O   . LYS B 1 103 ? 39.54900  -26.74700 -13.44000 1.000 43.74000  ? 122  LYS B O   1 
ATOM   4755  C CB  . LYS B 1 103 ? 36.75400  -26.04800 -12.57900 1.000 49.84000  ? 122  LYS B CB  1 
ATOM   4756  C CG  . LYS B 1 103 ? 35.44100  -25.31800 -12.53600 1.000 56.15000  ? 122  LYS B CG  1 
ATOM   4757  C CD  . LYS B 1 103 ? 34.39600  -26.40800 -12.40000 1.000 61.39000  ? 122  LYS B CD  1 
ATOM   4758  C CE  . LYS B 1 103 ? 33.00200  -25.89400 -12.18400 1.000 68.63000  ? 122  LYS B CE  1 
ATOM   4759  N NZ  . LYS B 1 103 ? 32.11900  -27.07800 -11.96600 1.000 69.84000  ? 122  LYS B NZ  1 
ATOM   4760  N N   . LEU B 1 104 ? 39.81900  -26.33800 -11.23400 1.000 39.29000  ? 123  LEU B N   1 
ATOM   4761  C CA  . LEU B 1 104 ? 40.82200  -27.38900 -11.08300 1.000 37.63000  ? 123  LEU B CA  1 
ATOM   4762  C C   . LEU B 1 104 ? 40.13500  -28.74200 -10.99600 1.000 36.23000  ? 123  LEU B C   1 
ATOM   4763  O O   . LEU B 1 104 ? 39.37100  -28.99300 -10.05900 1.000 39.22000  ? 123  LEU B O   1 
ATOM   4764  C CB  . LEU B 1 104 ? 41.68600  -27.18200 -9.84300  1.000 37.15000  ? 123  LEU B CB  1 
ATOM   4765  C CG  . LEU B 1 104 ? 42.78700  -26.13100 -9.75700  1.000 39.22000  ? 123  LEU B CG  1 
ATOM   4766  C CD1 . LEU B 1 104 ? 43.46600  -26.25400 -8.39200  1.000 39.10000  ? 123  LEU B CD1 1 
ATOM   4767  C CD2 . LEU B 1 104 ? 43.80000  -26.30100 -10.87700 1.000 33.39000  ? 123  LEU B CD2 1 
ATOM   4768  N N   . ILE B 1 105 ? 40.44300  -29.63500 -11.93200 1.000 29.90000  ? 124  ILE B N   1 
ATOM   4769  C CA  . ILE B 1 105 ? 39.67900  -30.87200 -12.02500 1.000 32.30000  ? 124  ILE B CA  1 
ATOM   4770  C C   . ILE B 1 105 ? 40.53200  -32.13500 -12.02800 1.000 35.26000  ? 124  ILE B C   1 
ATOM   4771  O O   . ILE B 1 105 ? 40.00200  -33.22700 -12.27100 1.000 32.16000  ? 124  ILE B O   1 
ATOM   4772  C CB  . ILE B 1 105 ? 38.76500  -30.83100 -13.26400 1.000 37.89000  ? 124  ILE B CB  1 
ATOM   4773  C CG1 . ILE B 1 105 ? 39.55200  -30.37700 -14.50100 1.000 31.97000  ? 124  ILE B CG1 1 
ATOM   4774  C CG2 . ILE B 1 105 ? 37.55100  -29.94200 -12.99800 1.000 32.63000  ? 124  ILE B CG2 1 
ATOM   4775  C CD1 . ILE B 1 105 ? 40.23300  -31.47500 -15.25100 1.000 31.94000  ? 124  ILE B CD1 1 
ATOM   4776  N N   . ALA B 1 106 ? 41.83700  -32.01400 -11.76100 1.000 31.32000  ? 125  ALA B N   1 
ATOM   4777  C CA  . ALA B 1 106 ? 42.69700  -33.19500 -11.67600 1.000 28.71000  ? 125  ALA B CA  1 
ATOM   4778  C C   . ALA B 1 106 ? 44.01100  -32.80600 -11.01900 1.000 33.44000  ? 125  ALA B C   1 
ATOM   4779  O O   . ALA B 1 106 ? 44.33200  -31.62100 -10.90300 1.000 37.90000  ? 125  ALA B O   1 
ATOM   4780  C CB  . ALA B 1 106 ? 42.95800  -33.81500 -13.05000 1.000 34.20000  ? 125  ALA B CB  1 
ATOM   4781  N N   . TYR B 1 107 ? 44.79500  -33.82200 -10.61400 1.000 34.65000  ? 126  TYR B N   1 
ATOM   4782  C CA  . TYR B 1 107 ? 46.12500  -33.46300 -10.12900 1.000 34.86000  ? 126  TYR B CA  1 
ATOM   4783  C C   . TYR B 1 107 ? 47.17500  -33.78100 -11.17600 1.000 32.58000  ? 126  TYR B C   1 
ATOM   4784  O O   . TYR B 1 107 ? 47.21600  -34.90800 -11.68700 1.000 34.21000  ? 126  TYR B O   1 
ATOM   4785  C CB  . TYR B 1 107 ? 46.55300  -34.13700 -8.81500  1.000 34.01000  ? 126  TYR B CB  1 
ATOM   4786  C CG  . TYR B 1 107 ? 45.66600  -34.01600 -7.60300  1.000 33.94000  ? 126  TYR B CG  1 
ATOM   4787  C CD1 . TYR B 1 107 ? 44.32200  -34.34600 -7.63500  1.000 34.18000  ? 126  TYR B CD1 1 
ATOM   4788  C CD2 . TYR B 1 107 ? 46.13500  -33.32100 -6.49600  1.000 33.03000  ? 126  TYR B CD2 1 
ATOM   4789  C CE1 . TYR B 1 107 ? 43.53400  -34.19200 -6.51400  1.000 28.12000  ? 126  TYR B CE1 1 
ATOM   4790  C CE2 . TYR B 1 107 ? 45.35000  -33.11200 -5.40000  1.000 37.66000  ? 126  TYR B CE2 1 
ATOM   4791  C CZ  . TYR B 1 107 ? 44.04900  -33.54100 -5.41000  1.000 34.14000  ? 126  TYR B CZ  1 
ATOM   4792  O OH  . TYR B 1 107 ? 43.29200  -33.31600 -4.29000  1.000 38.01000  ? 126  TYR B OH  1 
ATOM   4793  N N   . PRO B 1 108 ? 48.05700  -32.83200 -11.48000 1.000 32.85000  ? 127  PRO B N   1 
ATOM   4794  C CA  . PRO B 1 108 ? 49.16300  -33.11100 -12.40500 1.000 33.52000  ? 127  PRO B CA  1 
ATOM   4795  C C   . PRO B 1 108 ? 50.12600  -34.13500 -11.82200 1.000 36.75000  ? 127  PRO B C   1 
ATOM   4796  O O   . PRO B 1 108 ? 50.47200  -34.08700 -10.64000 1.000 37.37000  ? 127  PRO B O   1 
ATOM   4797  C CB  . PRO B 1 108 ? 49.84100  -31.74400 -12.56300 1.000 35.54000  ? 127  PRO B CB  1 
ATOM   4798  C CG  . PRO B 1 108 ? 48.80400  -30.73200 -12.08700 1.000 36.42000  ? 127  PRO B CG  1 
ATOM   4799  C CD  . PRO B 1 108 ? 48.06700  -31.44300 -10.99700 1.000 31.55000  ? 127  PRO B CD  1 
ATOM   4800  N N   . ILE B 1 109 ? 50.58100  -35.05000 -12.67200 1.000 33.27000  ? 128  ILE B N   1 
ATOM   4801  C CA  . ILE B 1 109 ? 51.49600  -36.09800 -12.24200 1.000 33.17000  ? 128  ILE B CA  1 
ATOM   4802  C C   . ILE B 1 109 ? 52.81700  -35.99700 -12.99800 1.000 39.18000  ? 128  ILE B C   1 
ATOM   4803  O O   . ILE B 1 109 ? 53.86800  -35.75800 -12.39600 1.000 35.71000  ? 128  ILE B O   1 
ATOM   4804  C CB  . ILE B 1 109 ? 50.86900  -37.48900 -12.43200 1.000 36.80000  ? 128  ILE B CB  1 
ATOM   4805  C CG1 . ILE B 1 109 ? 49.52900  -37.56500 -11.70700 1.000 35.32000  ? 128  ILE B CG1 1 
ATOM   4806  C CG2 . ILE B 1 109 ? 51.81600  -38.55100 -11.91000 1.000 34.55000  ? 128  ILE B CG2 1 
ATOM   4807  C CD1 . ILE B 1 109 ? 49.65700  -37.33700 -10.19700 1.000 35.11000  ? 128  ILE B CD1 1 
ATOM   4808  N N   . ALA B 1 110 ? 52.77500  -36.17200 -14.32000 1.000 38.90000  ? 129  ALA B N   1 
ATOM   4809  C CA  . ALA B 1 110 ? 53.98200  -36.22100 -15.13800 1.000 36.86000  ? 129  ALA B CA  1 
ATOM   4810  C C   . ALA B 1 110 ? 53.82400  -35.36700 -16.39300 1.000 38.91000  ? 129  ALA B C   1 
ATOM   4811  O O   . ALA B 1 110 ? 52.71900  -34.99000 -16.79900 1.000 33.10000  ? 129  ALA B O   1 
ATOM   4812  C CB  . ALA B 1 110 ? 54.35200  -37.66200 -15.52700 1.000 30.00000  ? 129  ALA B CB  1 
ATOM   4813  N N   . VAL B 1 111 ? 54.97000  -35.08100 -17.00200 1.000 30.66000  ? 130  VAL B N   1 
ATOM   4814  C CA  . VAL B 1 111 ? 55.09800  -34.12900 -18.09500 1.000 35.64000  ? 130  VAL B CA  1 
ATOM   4815  C C   . VAL B 1 111 ? 55.83200  -34.79000 -19.25400 1.000 38.85000  ? 130  VAL B C   1 
ATOM   4816  O O   . VAL B 1 111 ? 56.91600  -35.35500 -19.06400 1.000 35.74000  ? 130  VAL B O   1 
ATOM   4817  C CB  . VAL B 1 111 ? 55.85000  -32.86700 -17.62400 1.000 37.75000  ? 130  VAL B CB  1 
ATOM   4818  C CG1 . VAL B 1 111 ? 56.26900  -32.05600 -18.79800 1.000 34.52000  ? 130  VAL B CG1 1 
ATOM   4819  C CG2 . VAL B 1 111 ? 54.97200  -32.03200 -16.70500 1.000 37.90000  ? 130  VAL B CG2 1 
ATOM   4820  N N   . GLU B 1 112 ? 55.26000  -34.71500 -20.45400 1.000 32.66000  ? 131  GLU B N   1 
ATOM   4821  C CA  . GLU B 1 112 ? 55.99300  -35.15400 -21.63200 1.000 36.51000  ? 131  GLU B CA  1 
ATOM   4822  C C   . GLU B 1 112 ? 55.85300  -34.14700 -22.76000 1.000 34.88000  ? 131  GLU B C   1 
ATOM   4823  O O   . GLU B 1 112 ? 54.81400  -33.49700 -22.92200 1.000 33.37000  ? 131  GLU B O   1 
ATOM   4824  C CB  . GLU B 1 112 ? 55.54300  -36.52200 -22.15300 1.000 34.78000  ? 131  GLU B CB  1 
ATOM   4825  C CG  . GLU B 1 112 ? 54.21300  -36.50500 -22.85300 1.000 40.70000  ? 131  GLU B CG  1 
ATOM   4826  C CD  . GLU B 1 112 ? 53.87800  -37.84400 -23.47800 1.000 47.76000  ? 131  GLU B CD  1 
ATOM   4827  O OE1 . GLU B 1 112 ? 54.67500  -38.79800 -23.32100 1.000 48.43000  ? 131  GLU B OE1 1 
ATOM   4828  O OE2 . GLU B 1 112 ? 52.83300  -37.92100 -24.15300 1.000 48.22000  ? 131  GLU B OE2 1 
ATOM   4829  N N   . ALA B 1 113 ? 56.91500  -34.05800 -23.55500 1.000 29.73000  ? 132  ALA B N   1 
ATOM   4830  C CA  . ALA B 1 113 ? 56.94000  -33.26600 -24.77300 1.000 29.95000  ? 132  ALA B CA  1 
ATOM   4831  C C   . ALA B 1 113 ? 58.01700  -33.84800 -25.67500 1.000 31.44000  ? 132  ALA B C   1 
ATOM   4832  O O   . ALA B 1 113 ? 58.86500  -34.62600 -25.22600 1.000 35.37000  ? 132  ALA B O   1 
ATOM   4833  C CB  . ALA B 1 113 ? 57.20700  -31.78500 -24.47700 1.000 29.17000  ? 132  ALA B CB  1 
ATOM   4834  N N   . LEU B 1 114 ? 57.96900  -33.47300 -26.95600 1.000 33.33000  ? 133  LEU B N   1 
ATOM   4835  C CA  . LEU B 1 114 ? 59.02900  -33.84700 -27.88700 1.000 33.59000  ? 133  LEU B CA  1 
ATOM   4836  C C   . LEU B 1 114 ? 60.34500  -33.19700 -27.48900 1.000 34.67000  ? 133  LEU B C   1 
ATOM   4837  O O   . LEU B 1 114 ? 60.37300  -32.16000 -26.81900 1.000 30.50000  ? 133  LEU B O   1 
ATOM   4838  C CB  . LEU B 1 114 ? 58.67900  -33.42000 -29.31100 1.000 33.03000  ? 133  LEU B CB  1 
ATOM   4839  C CG  . LEU B 1 114 ? 57.53400  -34.12400 -30.03100 1.000 31.02000  ? 133  LEU B CG  1 
ATOM   4840  C CD1 . LEU B 1 114 ? 57.26100  -33.35900 -31.28300 1.000 24.17000  ? 133  LEU B CD1 1 
ATOM   4841  C CD2 . LEU B 1 114 ? 57.90700  -35.55900 -30.33900 1.000 30.66000  ? 133  LEU B CD2 1 
ATOM   4842  N N   . SER B 1 115 ? 61.44800  -33.81500 -27.91200 1.000 35.27000  ? 134  SER B N   1 
ATOM   4843  C CA  . SER B 1 115 ? 62.76100  -33.19800 -27.80000 1.000 30.81000  ? 134  SER B CA  1 
ATOM   4844  C C   . SER B 1 115 ? 63.55100  -33.44500 -29.06900 1.000 34.04000  ? 134  SER B C   1 
ATOM   4845  O O   . SER B 1 115 ? 63.10400  -34.14100 -29.98600 1.000 37.14000  ? 134  SER B O   1 
ATOM   4846  C CB  . SER B 1 115 ? 63.55700  -33.72200 -26.59700 1.000 32.85000  ? 134  SER B CB  1 
ATOM   4847  O OG  . SER B 1 115 ? 63.01700  -33.26900 -25.37300 1.000 32.81000  ? 134  SER B OG  1 
ATOM   4848  N N   . LEU B 1 116 ? 64.74300  -32.85800 -29.10700 1.000 31.80000  ? 135  LEU B N   1 
ATOM   4849  C CA  . LEU B 1 116 ? 65.72200  -33.18200 -30.13400 1.000 29.47000  ? 135  LEU B CA  1 
ATOM   4850  C C   . LEU B 1 116 ? 66.56100  -34.37200 -29.68000 1.000 33.51000  ? 135  LEU B C   1 
ATOM   4851  O O   . LEU B 1 116 ? 67.19500  -34.33200 -28.61800 1.000 38.50000  ? 135  LEU B O   1 
ATOM   4852  C CB  . LEU B 1 116 ? 66.60400  -31.97200 -30.42500 1.000 33.25000  ? 135  LEU B CB  1 
ATOM   4853  C CG  . LEU B 1 116 ? 67.65700  -32.12200 -31.51500 1.000 27.10000  ? 135  LEU B CG  1 
ATOM   4854  C CD1 . LEU B 1 116 ? 66.99400  -32.52200 -32.81900 1.000 26.34000  ? 135  LEU B CD1 1 
ATOM   4855  C CD2 . LEU B 1 116 ? 68.34700  -30.79000 -31.67900 1.000 27.68000  ? 135  LEU B CD2 1 
ATOM   4856  N N   . ILE B 1 117 ? 66.56600  -35.43100 -30.47700 1.000 32.12000  ? 136  ILE B N   1 
ATOM   4857  C CA  . ILE B 1 117 ? 67.32400  -36.63500 -30.17600 1.000 29.51000  ? 136  ILE B CA  1 
ATOM   4858  C C   . ILE B 1 117 ? 68.45100  -36.71800 -31.18600 1.000 32.74000  ? 136  ILE B C   1 
ATOM   4859  O O   . ILE B 1 117 ? 68.21200  -36.63100 -32.39900 1.000 33.68000  ? 136  ILE B O   1 
ATOM   4860  C CB  . ILE B 1 117 ? 66.43300  -37.88800 -30.21000 1.000 28.47000  ? 136  ILE B CB  1 
ATOM   4861  C CG1 . ILE B 1 117 ? 65.28800  -37.74100 -29.20300 1.000 28.03000  ? 136  ILE B CG1 1 
ATOM   4862  C CG2 . ILE B 1 117 ? 67.25800  -39.12600 -29.90500 1.000 30.81000  ? 136  ILE B CG2 1 
ATOM   4863  C CD1 . ILE B 1 117 ? 64.28100  -38.86200 -29.23600 1.000 31.52000  ? 136  ILE B CD1 1 
ATOM   4864  N N   . TYR B 1 118 ? 69.68000  -36.85600 -30.69300 1.000 36.31000  ? 137  TYR B N   1 
ATOM   4865  C CA  . TYR B 1 118 ? 70.83500  -36.69700 -31.55500 1.000 31.71000  ? 137  TYR B CA  1 
ATOM   4866  C C   . TYR B 1 118 ? 71.83500  -37.79400 -31.25900 1.000 35.67000  ? 137  TYR B C   1 
ATOM   4867  O O   . TYR B 1 118 ? 71.88400  -38.32600 -30.14800 1.000 36.68000  ? 137  TYR B O   1 
ATOM   4868  C CB  . TYR B 1 118 ? 71.45800  -35.31500 -31.39200 1.000 31.29000  ? 137  TYR B CB  1 
ATOM   4869  C CG  . TYR B 1 118 ? 72.12600  -35.07200 -30.06300 1.000 40.71000  ? 137  TYR B CG  1 
ATOM   4870  C CD1 . TYR B 1 118 ? 71.37900  -34.71200 -28.94000 1.000 36.18000  ? 137  TYR B CD1 1 
ATOM   4871  C CD2 . TYR B 1 118 ? 73.51600  -35.13900 -29.94000 1.000 36.93000  ? 137  TYR B CD2 1 
ATOM   4872  C CE1 . TYR B 1 118 ? 71.99600  -34.46800 -27.71100 1.000 35.23000  ? 137  TYR B CE1 1 
ATOM   4873  C CE2 . TYR B 1 118 ? 74.14300  -34.88600 -28.72500 1.000 35.44000  ? 137  TYR B CE2 1 
ATOM   4874  C CZ  . TYR B 1 118 ? 73.38300  -34.56000 -27.61200 1.000 39.58000  ? 137  TYR B CZ  1 
ATOM   4875  O OH  . TYR B 1 118 ? 74.02000  -34.31700 -26.41100 1.000 39.54000  ? 137  TYR B OH  1 
ATOM   4876  N N   . ASN B 1 119 ? 72.60900  -38.13500 -32.28700 1.000 38.68000  ? 138  ASN B N   1 
ATOM   4877  C CA  . ASN B 1 119 ? 73.62000  -39.18400 -32.22400 1.000 37.62000  ? 138  ASN B CA  1 
ATOM   4878  C C   . ASN B 1 119 ? 74.94600  -38.55600 -31.80500 1.000 42.06000  ? 138  ASN B C   1 
ATOM   4879  O O   . ASN B 1 119 ? 75.54600  -37.77700 -32.55600 1.000 42.93000  ? 138  ASN B O   1 
ATOM   4880  C CB  . ASN B 1 119 ? 73.70100  -39.90100 -33.57100 1.000 37.94000  ? 138  ASN B CB  1 
ATOM   4881  C CG  . ASN B 1 119 ? 74.65800  -41.07500 -33.57000 1.000 37.63000  ? 138  ASN B CG  1 
ATOM   4882  O OD1 . ASN B 1 119 ? 75.53600  -41.18300 -32.72000 1.000 47.54000  ? 138  ASN B OD1 1 
ATOM   4883  N ND2 . ASN B 1 119 ? 74.43400  -42.01100 -34.48600 1.000 35.37000  ? 138  ASN B ND2 1 
ATOM   4884  N N   . LYS B 1 120 ? 75.40200  -38.91100 -30.59900 1.000 42.07000  ? 139  LYS B N   1 
ATOM   4885  C CA  . LYS B 1 120 ? 76.59000  -38.28300 -30.02800 1.000 45.31000  ? 139  LYS B CA  1 
ATOM   4886  C C   . LYS B 1 120 ? 77.83000  -38.57600 -30.85500 1.000 38.49000  ? 139  LYS B C   1 
ATOM   4887  O O   . LYS B 1 120 ? 78.72900  -37.73400 -30.95200 1.000 40.80000  ? 139  LYS B O   1 
ATOM   4888  C CB  . LYS B 1 120 ? 76.78300  -38.74700 -28.58400 1.000 45.96000  ? 139  LYS B CB  1 
ATOM   4889  C CG  . LYS B 1 120 ? 75.78100  -38.14500 -27.61200 1.000 35.58000  ? 139  LYS B CG  1 
ATOM   4890  C CD  . LYS B 1 120 ? 76.05600  -38.57100 -26.18900 1.000 32.83000  ? 139  LYS B CD  1 
ATOM   4891  C CE  . LYS B 1 120 ? 75.13900  -37.83500 -25.23800 1.000 39.47000  ? 139  LYS B CE  1 
ATOM   4892  N NZ  . LYS B 1 120 ? 75.34800  -38.21700 -23.81200 1.000 49.50000  ? 139  LYS B NZ  1 
ATOM   4893  N N   . ASP B 1 121 ? 77.90100  -39.76800 -31.44500 1.000 37.47000  ? 140  ASP B N   1 
ATOM   4894  C CA  . ASP B 1 121 ? 79.06700  -40.14200 -32.24200 1.000 35.16000  ? 140  ASP B CA  1 
ATOM   4895  C C   . ASP B 1 121 ? 79.12800  -39.33200 -33.53000 1.000 38.33000  ? 140  ASP B C   1 
ATOM   4896  O O   . ASP B 1 121 ? 80.18700  -38.81800 -33.90500 1.000 53.09000  ? 140  ASP B O   1 
ATOM   4897  C CB  . ASP B 1 121 ? 79.01800  -41.64000 -32.53300 1.000 32.81000  ? 140  ASP B CB  1 
ATOM   4898  C CG  . ASP B 1 121 ? 79.05800  -42.47200 -31.26000 1.000 48.73000  ? 140  ASP B CG  1 
ATOM   4899  O OD1 . ASP B 1 121 ? 79.85100  -42.14900 -30.34700 1.000 41.70000  ? 140  ASP B OD1 1 
ATOM   4900  O OD2 . ASP B 1 121 ? 78.22400  -43.39500 -31.12900 1.000 53.79000  ? 140  ASP B OD2 1 
ATOM   4901  N N   . LEU B 1 122 ? 77.99400  -39.19600 -34.21900 1.000 41.74000  ? 141  LEU B N   1 
ATOM   4902  C CA  . LEU B 1 122 ? 77.94300  -38.41800 -35.45400 1.000 45.07000  ? 141  LEU B CA  1 
ATOM   4903  C C   . LEU B 1 122 ? 77.93600  -36.92100 -35.19200 1.000 45.00000  ? 141  LEU B C   1 
ATOM   4904  O O   . LEU B 1 122 ? 78.38400  -36.14100 -36.04200 1.000 40.45000  ? 141  LEU B O   1 
ATOM   4905  C CB  . LEU B 1 122 ? 76.69100  -38.78700 -36.24700 1.000 39.72000  ? 141  LEU B CB  1 
ATOM   4906  C CG  . LEU B 1 122 ? 76.60100  -40.24000 -36.69500 1.000 39.94000  ? 141  LEU B CG  1 
ATOM   4907  C CD1 . LEU B 1 122 ? 75.21600  -40.49600 -37.24700 1.000 36.72000  ? 141  LEU B CD1 1 
ATOM   4908  C CD2 . LEU B 1 122 ? 77.67000  -40.54900 -37.73000 1.000 39.33000  ? 141  LEU B CD2 1 
ATOM   4909  N N   . LEU B 1 123 ? 77.41800  -36.50100 -34.04100 1.000 43.21000  ? 142  LEU B N   1 
ATOM   4910  C CA  . LEU B 1 123 ? 77.13200  -35.09100 -33.79000 1.000 42.92000  ? 142  LEU B CA  1 
ATOM   4911  C C   . LEU B 1 123 ? 77.32900  -34.82900 -32.30700 1.000 41.81000  ? 142  LEU B C   1 
ATOM   4912  O O   . LEU B 1 123 ? 76.37700  -34.83700 -31.52000 1.000 41.35000  ? 142  LEU B O   1 
ATOM   4913  C CB  . LEU B 1 123 ? 75.71100  -34.73800 -34.23000 1.000 41.93000  ? 142  LEU B CB  1 
ATOM   4914  C CG  . LEU B 1 123 ? 75.30000  -33.27500 -34.37300 1.000 39.96000  ? 142  LEU B CG  1 
ATOM   4915  C CD1 . LEU B 1 123 ? 76.08400  -32.66300 -35.50500 1.000 41.03000  ? 142  LEU B CD1 1 
ATOM   4916  C CD2 . LEU B 1 123 ? 73.79900  -33.16200 -34.64700 1.000 36.45000  ? 142  LEU B CD2 1 
ATOM   4917  N N   . PRO B 1 124 ? 78.56900  -34.61900 -31.87800 1.000 39.59000  ? 143  PRO B N   1 
ATOM   4918  C CA  . PRO B 1 124 ? 78.79100  -34.30600 -30.46000 1.000 46.56000  ? 143  PRO B CA  1 
ATOM   4919  C C   . PRO B 1 124 ? 78.08100  -33.04100 -30.01300 1.000 42.52000  ? 143  PRO B C   1 
ATOM   4920  O O   . PRO B 1 124 ? 77.62000  -32.96600 -28.86500 1.000 44.15000  ? 143  PRO B O   1 
ATOM   4921  C CB  . PRO B 1 124 ? 80.31600  -34.15800 -30.37100 1.000 43.47000  ? 143  PRO B CB  1 
ATOM   4922  C CG  . PRO B 1 124 ? 80.84000  -34.91600 -31.55000 1.000 45.41000  ? 143  PRO B CG  1 
ATOM   4923  C CD  . PRO B 1 124 ? 79.82800  -34.71400 -32.63100 1.000 39.54000  ? 143  PRO B CD  1 
ATOM   4924  N N   . ASN B 1 125 ? 77.96000  -32.05500 -30.90300 1.000 33.05000  ? 144  ASN B N   1 
ATOM   4925  C CA  . ASN B 1 125 ? 77.49000  -30.71400 -30.57000 1.000 34.70000  ? 144  ASN B CA  1 
ATOM   4926  C C   . ASN B 1 125 ? 76.28700  -30.39100 -31.45200 1.000 42.92000  ? 144  ASN B C   1 
ATOM   4927  O O   . ASN B 1 125 ? 76.42500  -29.72700 -32.49200 1.000 37.08000  ? 144  ASN B O   1 
ATOM   4928  C CB  . ASN B 1 125 ? 78.61400  -29.70500 -30.77200 1.000 41.27000  ? 144  ASN B CB  1 
ATOM   4929  C CG  . ASN B 1 125 ? 79.81700  -30.00400 -29.89500 1.000 51.12000  ? 144  ASN B CG  1 
ATOM   4930  O OD1 . ASN B 1 125 ? 79.67500  -30.33700 -28.71900 1.000 51.64000  ? 144  ASN B OD1 1 
ATOM   4931  N ND2 . ASN B 1 125 ? 81.01100  -29.91600 -30.47600 1.000 54.68000  ? 144  ASN B ND2 1 
ATOM   4932  N N   . PRO B 1 126 ? 75.09100  -30.82700 -31.06000 1.000 46.15000  ? 145  PRO B N   1 
ATOM   4933  C CA  . PRO B 1 126 ? 73.93700  -30.68500 -31.93900 1.000 36.52000  ? 145  PRO B CA  1 
ATOM   4934  C C   . PRO B 1 126 ? 73.60900  -29.19400 -32.16800 1.000 37.38000  ? 145  PRO B C   1 
ATOM   4935  O O   . PRO B 1 126 ? 73.95200  -28.35000 -31.33400 1.000 35.21000  ? 145  PRO B O   1 
ATOM   4936  C CB  . PRO B 1 126 ? 72.81200  -31.39500 -31.18000 1.000 33.44000  ? 145  PRO B CB  1 
ATOM   4937  C CG  . PRO B 1 126 ? 73.21600  -31.34600 -29.74300 1.000 33.72000  ? 145  PRO B CG  1 
ATOM   4938  C CD  . PRO B 1 126 ? 74.73800  -31.43400 -29.76000 1.000 38.51000  ? 145  PRO B CD  1 
ATOM   4939  N N   . PRO B 1 127 ? 72.97400  -28.88600 -33.29800 1.000 38.74000  ? 146  PRO B N   1 
ATOM   4940  C CA  . PRO B 1 127 ? 72.69400  -27.47500 -33.60400 1.000 41.86000  ? 146  PRO B CA  1 
ATOM   4941  C C   . PRO B 1 127 ? 71.71600  -26.85600 -32.61400 1.000 41.26000  ? 146  PRO B C   1 
ATOM   4942  O O   . PRO B 1 127 ? 70.81300  -27.52100 -32.10200 1.000 39.09000  ? 146  PRO B O   1 
ATOM   4943  C CB  . PRO B 1 127 ? 72.09500  -27.53400 -35.00100 1.000 43.97000  ? 146  PRO B CB  1 
ATOM   4944  C CG  . PRO B 1 127 ? 71.46200  -28.88800 -35.07100 1.000 40.88000  ? 146  PRO B CG  1 
ATOM   4945  C CD  . PRO B 1 127 ? 72.36500  -29.78800 -34.27000 1.000 37.51000  ? 146  PRO B CD  1 
ATOM   4946  N N   . LYS B 1 128 ? 71.89600  -25.55500 -32.36200 1.000 40.78000  ? 147  LYS B N   1 
ATOM   4947  C CA  . LYS B 1 128 ? 70.96600  -24.81000 -31.52500 1.000 40.48000  ? 147  LYS B CA  1 
ATOM   4948  C C   . LYS B 1 128 ? 69.84800  -24.15200 -32.31800 1.000 43.31000  ? 147  LYS B C   1 
ATOM   4949  O O   . LYS B 1 128 ? 68.80000  -23.83400 -31.74000 1.000 40.37000  ? 147  LYS B O   1 
ATOM   4950  C CB  . LYS B 1 128 ? 71.69400  -23.72700 -30.71400 1.000 42.54000  ? 147  LYS B CB  1 
ATOM   4951  C CG  . LYS B 1 128 ? 72.62800  -24.27100 -29.65500 1.000 41.05000  ? 147  LYS B CG  1 
ATOM   4952  C CD  . LYS B 1 128 ? 71.82500  -25.03500 -28.62500 1.000 47.91000  ? 147  LYS B CD  1 
ATOM   4953  C CE  . LYS B 1 128 ? 72.69300  -25.59900 -27.51800 1.000 52.12000  ? 147  LYS B CE  1 
ATOM   4954  N NZ  . LYS B 1 128 ? 71.87600  -26.49000 -26.64200 1.000 55.30000  ? 147  LYS B NZ  1 
ATOM   4955  N N   . THR B 1 129 ? 70.03600  -23.94300 -33.61500 1.000 38.66000  ? 148  THR B N   1 
ATOM   4956  C CA  . THR B 1 129 ? 69.04000  -23.28500 -34.44200 1.000 40.42000  ? 148  THR B CA  1 
ATOM   4957  C C   . THR B 1 129 ? 68.61100  -24.21300 -35.57000 1.000 36.89000  ? 148  THR B C   1 
ATOM   4958  O O   . THR B 1 129 ? 69.38400  -25.05500 -36.03500 1.000 34.17000  ? 148  THR B O   1 
ATOM   4959  C CB  . THR B 1 129 ? 69.57500  -21.97200 -35.03900 1.000 40.59000  ? 148  THR B CB  1 
ATOM   4960  O OG1 . THR B 1 129 ? 70.58700  -22.26200 -36.00700 1.000 40.24000  ? 148  THR B OG1 1 
ATOM   4961  C CG2 . THR B 1 129 ? 70.17500  -21.09400 -33.94800 1.000 37.59000  ? 148  THR B CG2 1 
ATOM   4962  N N   . TRP B 1 130 ? 67.35100  -24.06400 -35.98500 1.000 39.79000  ? 149  TRP B N   1 
ATOM   4963  C CA  . TRP B 1 130 ? 66.90400  -24.70000 -37.22000 1.000 37.67000  ? 149  TRP B CA  1 
ATOM   4964  C C   . TRP B 1 130 ? 67.69400  -24.18500 -38.41100 1.000 38.75000  ? 149  TRP B C   1 
ATOM   4965  O O   . TRP B 1 130 ? 68.03400  -24.95000 -39.32200 1.000 39.53000  ? 149  TRP B O   1 
ATOM   4966  C CB  . TRP B 1 130 ? 65.41100  -24.45600 -37.43600 1.000 30.35000  ? 149  TRP B CB  1 
ATOM   4967  C CG  . TRP B 1 130 ? 64.49900  -25.34800 -36.63800 1.000 34.77000  ? 149  TRP B CG  1 
ATOM   4968  C CD1 . TRP B 1 130 ? 63.91400  -25.07500 -35.42600 1.000 37.02000  ? 149  TRP B CD1 1 
ATOM   4969  C CD2 . TRP B 1 130 ? 64.03600  -26.64900 -37.02100 1.000 32.03000  ? 149  TRP B CD2 1 
ATOM   4970  N NE1 . TRP B 1 130 ? 63.12400  -26.13500 -35.02700 1.000 33.71000  ? 149  TRP B NE1 1 
ATOM   4971  C CE2 . TRP B 1 130 ? 63.18300  -27.11300 -35.98900 1.000 35.24000  ? 149  TRP B CE2 1 
ATOM   4972  C CE3 . TRP B 1 130 ? 64.25800  -27.47100 -38.13600 1.000 31.94000  ? 149  TRP B CE3 1 
ATOM   4973  C CZ2 . TRP B 1 130 ? 62.56000  -28.36400 -36.03800 1.000 28.56000  ? 149  TRP B CZ2 1 
ATOM   4974  C CZ3 . TRP B 1 130 ? 63.63600  -28.71100 -38.18400 1.000 30.08000  ? 149  TRP B CZ3 1 
ATOM   4975  C CH2 . TRP B 1 130 ? 62.80000  -29.14600 -37.14000 1.000 29.51000  ? 149  TRP B CH2 1 
ATOM   4976  N N   . GLU B 1 131 ? 68.00200  -22.88900 -38.41100 1.000 36.20000  ? 150  GLU B N   1 
ATOM   4977  C CA  . GLU B 1 131 ? 68.63400  -22.25300 -39.55600 1.000 40.39000  ? 150  GLU B CA  1 
ATOM   4978  C C   . GLU B 1 131 ? 69.99200  -22.85500 -39.89600 1.000 45.28000  ? 150  GLU B C   1 
ATOM   4979  O O   . GLU B 1 131 ? 70.44100  -22.73800 -41.04400 1.000 48.25000  ? 150  GLU B O   1 
ATOM   4980  C CB  . GLU B 1 131 ? 68.78600  -20.76000 -39.28700 1.000 40.92000  ? 150  GLU B CB  1 
ATOM   4981  C CG  . GLU B 1 131 ? 67.48400  -19.97900 -39.26100 1.000 40.85000  ? 150  GLU B CG  1 
ATOM   4982  C CD  . GLU B 1 131 ? 66.73700  -20.06400 -37.92700 1.000 44.40000  ? 150  GLU B CD  1 
ATOM   4983  O OE1 . GLU B 1 131 ? 67.12100  -20.86400 -37.03700 1.000 36.69000  ? 150  GLU B OE1 1 
ATOM   4984  O OE2 . GLU B 1 131 ? 65.80500  -19.25400 -37.74100 1.000 43.95000  ? 150  GLU B OE2 1 
ATOM   4985  N N   . GLU B 1 132 ? 70.65500  -23.49500 -38.94100 1.000 40.56000  ? 151  GLU B N   1 
ATOM   4986  C CA  . GLU B 1 132 ? 71.99300  -23.98900 -39.20200 1.000 41.86000  ? 151  GLU B CA  1 
ATOM   4987  C C   . GLU B 1 132 ? 71.98400  -25.45400 -39.63500 1.000 48.13000  ? 151  GLU B C   1 
ATOM   4988  O O   . GLU B 1 132 ? 73.05000  -26.00700 -39.93500 1.000 44.08000  ? 151  GLU B O   1 
ATOM   4989  C CB  . GLU B 1 132 ? 72.87200  -23.76300 -37.95300 1.000 44.52000  ? 151  GLU B CB  1 
ATOM   4990  C CG  . GLU B 1 132 ? 73.03000  -24.89100 -36.96900 1.000 50.45000  ? 151  GLU B CG  1 
ATOM   4991  C CD  . GLU B 1 132 ? 73.51900  -24.39900 -35.58100 1.000 60.13000  ? 151  GLU B CD  1 
ATOM   4992  O OE1 . GLU B 1 132 ? 73.07700  -23.30200 -35.15600 1.000 56.40000  ? 151  GLU B OE1 1 
ATOM   4993  O OE2 . GLU B 1 132 ? 74.45300  -25.03400 -35.00800 1.000 55.30000  ? 151  GLU B OE2 1 
ATOM   4994  N N   . ILE B 1 133 ? 70.80500  -26.07600 -39.71300 1.000 41.46000  ? 152  ILE B N   1 
ATOM   4995  C CA  . ILE B 1 133 ? 70.65400  -27.46900 -40.13500 1.000 41.62000  ? 152  ILE B CA  1 
ATOM   4996  C C   . ILE B 1 133 ? 70.88200  -27.67000 -41.63500 1.000 39.30000  ? 152  ILE B C   1 
ATOM   4997  O O   . ILE B 1 133 ? 71.41500  -28.72200 -42.01600 1.000 40.75000  ? 152  ILE B O   1 
ATOM   4998  C CB  . ILE B 1 133 ? 69.28700  -28.01900 -39.69500 1.000 39.21000  ? 152  ILE B CB  1 
ATOM   4999  C CG1 . ILE B 1 133 ? 69.27800  -28.21300 -38.18500 1.000 40.08000  ? 152  ILE B CG1 1 
ATOM   5000  C CG2 . ILE B 1 133 ? 68.95400  -29.34500 -40.37500 1.000 34.42000  ? 152  ILE B CG2 1 
ATOM   5001  C CD1 . ILE B 1 133 ? 67.93500  -28.58100 -37.63800 1.000 41.81000  ? 152  ILE B CD1 1 
ATOM   5002  N N   . PRO B 1 134 ? 70.49900  -26.74400 -42.53100 1.000 38.81000  ? 153  PRO B N   1 
ATOM   5003  C CA  . PRO B 1 134 ? 70.89700  -26.92600 -43.94400 1.000 42.67000  ? 153  PRO B CA  1 
ATOM   5004  C C   . PRO B 1 134 ? 72.39000  -27.13300 -44.11200 1.000 43.05000  ? 153  PRO B C   1 
ATOM   5005  O O   . PRO B 1 134 ? 72.81000  -28.11200 -44.74600 1.000 45.86000  ? 153  PRO B O   1 
ATOM   5006  C CB  . PRO B 1 134 ? 70.41800  -25.63300 -44.61200 1.000 46.02000  ? 153  PRO B CB  1 
ATOM   5007  C CG  . PRO B 1 134 ? 69.27500  -25.18200 -43.76500 1.000 45.06000  ? 153  PRO B CG  1 
ATOM   5008  C CD  . PRO B 1 134 ? 69.66600  -25.53900 -42.36200 1.000 36.27000  ? 153  PRO B CD  1 
ATOM   5009  N N   . ALA B 1 135 ? 73.20300  -26.24300 -43.52900 1.000 46.06000  ? 154  ALA B N   1 
ATOM   5010  C CA  . ALA B 1 135 ? 74.65600  -26.37200 -43.60000 1.000 38.13000  ? 154  ALA B CA  1 
ATOM   5011  C C   . ALA B 1 135 ? 75.13900  -27.66700 -42.95800 1.000 39.25000  ? 154  ALA B C   1 
ATOM   5012  O O   . ALA B 1 135 ? 76.02900  -28.33600 -43.49000 1.000 48.11000  ? 154  ALA B O   1 
ATOM   5013  C CB  . ALA B 1 135 ? 75.31800  -25.16900 -42.93100 1.000 37.21000  ? 154  ALA B CB  1 
ATOM   5014  N N   . LEU B 1 136 ? 74.57100  -28.03300 -41.80900 1.000 45.56000  ? 155  LEU B N   1 
ATOM   5015  C CA  . LEU B 1 136 ? 74.94200  -29.29200 -41.17000 1.000 41.30000  ? 155  LEU B CA  1 
ATOM   5016  C C   . LEU B 1 136 ? 74.64800  -30.48500 -42.06800 1.000 42.47000  ? 155  LEU B C   1 
ATOM   5017  O O   . LEU B 1 136 ? 75.37000  -31.48700 -42.02800 1.000 46.09000  ? 155  LEU B O   1 
ATOM   5018  C CB  . LEU B 1 136 ? 74.20500  -29.44200 -39.84000 1.000 37.12000  ? 155  LEU B CB  1 
ATOM   5019  C CG  . LEU B 1 136 ? 74.54000  -30.72200 -39.07000 1.000 43.25000  ? 155  LEU B CG  1 
ATOM   5020  C CD1 . LEU B 1 136 ? 76.03200  -30.77300 -38.73700 1.000 39.50000  ? 155  LEU B CD1 1 
ATOM   5021  C CD2 . LEU B 1 136 ? 73.71300  -30.83500 -37.79800 1.000 41.41000  ? 155  LEU B CD2 1 
ATOM   5022  N N   . ASP B 1 137 ? 73.59800  -30.39700 -42.88400 1.000 43.38000  ? 156  ASP B N   1 
ATOM   5023  C CA  . ASP B 1 137 ? 73.25000  -31.51100 -43.75800 1.000 44.21000  ? 156  ASP B CA  1 
ATOM   5024  C C   . ASP B 1 137 ? 74.22700  -31.62500 -44.92600 1.000 42.75000  ? 156  ASP B C   1 
ATOM   5025  O O   . ASP B 1 137 ? 74.58000  -32.73800 -45.33100 1.000 41.02000  ? 156  ASP B O   1 
ATOM   5026  C CB  . ASP B 1 137 ? 71.80600  -31.35100 -44.23800 1.000 40.98000  ? 156  ASP B CB  1 
ATOM   5027  C CG  . ASP B 1 137 ? 71.28100  -32.58000 -44.94100 1.000 41.36000  ? 156  ASP B CG  1 
ATOM   5028  O OD1 . ASP B 1 137 ? 71.08600  -33.62600 -44.26800 1.000 34.15000  ? 156  ASP B OD1 1 
ATOM   5029  O OD2 . ASP B 1 137 ? 71.03300  -32.48500 -46.16600 1.000 40.51000  ? 156  ASP B OD2 1 
ATOM   5030  N N   . LYS B 1 138 ? 74.69500  -30.49100 -45.46700 1.000 43.51000  ? 157  LYS B N   1 
ATOM   5031  C CA  . LYS B 1 138 ? 75.76000  -30.53500 -46.46800 1.000 51.81000  ? 157  LYS B CA  1 
ATOM   5032  C C   . LYS B 1 138 ? 76.94500  -31.34700 -45.95200 1.000 45.94000  ? 157  LYS B C   1 
ATOM   5033  O O   . LYS B 1 138 ? 77.40400  -32.29000 -46.60600 1.000 51.08000  ? 157  LYS B O   1 
ATOM   5034  C CB  . LYS B 1 138 ? 76.23400  -29.11900 -46.82800 1.000 58.52000  ? 157  LYS B CB  1 
ATOM   5035  C CG  . LYS B 1 138 ? 75.18400  -28.17200 -47.40500 1.000 62.67000  ? 157  LYS B CG  1 
ATOM   5036  C CD  . LYS B 1 138 ? 74.72100  -28.57400 -48.80500 1.000 73.19000  ? 157  LYS B CD  1 
ATOM   5037  C CE  . LYS B 1 138 ? 73.58200  -27.65200 -49.34300 1.000 66.14000  ? 157  LYS B CE  1 
ATOM   5038  N NZ  . LYS B 1 138 ? 73.98500  -26.21800 -49.54900 1.000 72.90000  ? 157  LYS B NZ  1 
ATOM   5039  N N   . GLU B 1 139 ? 77.42300  -31.01300 -44.75100 1.000 40.91000  ? 158  GLU B N   1 
ATOM   5040  C CA  . GLU B 1 139 ? 78.61800  -31.65200 -44.20900 1.000 49.40000  ? 158  GLU B CA  1 
ATOM   5041  C C   . GLU B 1 139 ? 78.40500  -33.14700 -44.02100 1.000 50.61000  ? 158  GLU B C   1 
ATOM   5042  O O   . GLU B 1 139 ? 79.23900  -33.96600 -44.42800 1.000 51.99000  ? 158  GLU B O   1 
ATOM   5043  C CB  . GLU B 1 139 ? 78.99600  -31.00700 -42.87900 1.000 43.54000  ? 158  GLU B CB  1 
ATOM   5044  C CG  . GLU B 1 139 ? 79.38500  -29.54700 -42.96200 1.000 52.25000  ? 158  GLU B CG  1 
ATOM   5045  C CD  . GLU B 1 139 ? 79.83700  -28.99700 -41.61800 1.000 72.45000  ? 158  GLU B CD  1 
ATOM   5046  O OE1 . GLU B 1 139 ? 79.77200  -29.74500 -40.61100 1.000 69.98000  ? 158  GLU B OE1 1 
ATOM   5047  O OE2 . GLU B 1 139 ? 80.25900  -27.82100 -41.57000 1.000 80.66000  ? 158  GLU B OE2 1 
ATOM   5048  N N   . LEU B 1 140 ? 77.28600  -33.51800 -43.39700 1.000 49.23000  ? 159  LEU B N   1 
ATOM   5049  C CA  . LEU B 1 140 ? 77.01600  -34.92300 -43.11600 1.000 45.34000  ? 159  LEU B CA  1 
ATOM   5050  C C   . LEU B 1 140 ? 76.71500  -35.71300 -44.38500 1.000 42.36000  ? 159  LEU B C   1 
ATOM   5051  O O   . LEU B 1 140 ? 76.96800  -36.92100 -44.42400 1.000 41.93000  ? 159  LEU B O   1 
ATOM   5052  C CB  . LEU B 1 140 ? 75.86700  -35.03000 -42.11300 1.000 45.94000  ? 159  LEU B CB  1 
ATOM   5053  C CG  . LEU B 1 140 ? 76.19800  -34.67400 -40.66300 1.000 41.46000  ? 159  LEU B CG  1 
ATOM   5054  C CD1 . LEU B 1 140 ? 74.93400  -34.47200 -39.86200 1.000 37.61000  ? 159  LEU B CD1 1 
ATOM   5055  C CD2 . LEU B 1 140 ? 77.00800  -35.80400 -40.04900 1.000 39.64000  ? 159  LEU B CD2 1 
ATOM   5056  N N   . LYS B 1 141 ? 76.17300  -35.06400 -45.42600 1.000 38.80000  ? 160  LYS B N   1 
ATOM   5057  C CA  . LYS B 1 141 ? 75.95300  -35.77000 -46.69000 1.000 45.08000  ? 160  LYS B CA  1 
ATOM   5058  C C   . LYS B 1 141 ? 77.26500  -36.18300 -47.34400 1.000 45.00000  ? 160  LYS B C   1 
ATOM   5059  O O   . LYS B 1 141 ? 77.34900  -37.26300 -47.93700 1.000 45.23000  ? 160  LYS B O   1 
ATOM   5060  C CB  . LYS B 1 141 ? 75.11400  -34.92200 -47.65000 1.000 41.58000  ? 160  LYS B CB  1 
ATOM   5061  C CG  . LYS B 1 141 ? 73.64500  -34.81000 -47.24900 1.000 44.30000  ? 160  LYS B CG  1 
ATOM   5062  C CD  . LYS B 1 141 ? 72.88600  -36.09600 -47.51600 1.000 46.21000  ? 160  LYS B CD  1 
ATOM   5063  C CE  . LYS B 1 141 ? 71.46900  -36.03400 -46.93500 1.000 46.35000  ? 160  LYS B CE  1 
ATOM   5064  N NZ  . LYS B 1 141 ? 70.60700  -34.98700 -47.53900 1.000 39.20000  ? 160  LYS B NZ  1 
ATOM   5065  N N   . ALA B 1 142 ? 78.30200  -35.35200 -47.23800 1.000 47.47000  ? 161  ALA B N   1 
ATOM   5066  C CA  . ALA B 1 142 ? 79.60700  -35.72100 -47.77100 1.000 45.56000  ? 161  ALA B CA  1 
ATOM   5067  C C   . ALA B 1 142 ? 80.24500  -36.88200 -47.01300 1.000 50.58000  ? 161  ALA B C   1 
ATOM   5068  O O   . ALA B 1 142 ? 81.14200  -37.53700 -47.55100 1.000 62.15000  ? 161  ALA B O   1 
ATOM   5069  C CB  . ALA B 1 142 ? 80.53800  -34.51000 -47.75200 1.000 47.13000  ? 161  ALA B CB  1 
ATOM   5070  N N   . LYS B 1 143 ? 79.81500  -37.15500 -45.78500 1.000 49.86000  ? 162  LYS B N   1 
ATOM   5071  C CA  . LYS B 1 143 ? 80.27700  -38.32700 -45.05600 1.000 45.14000  ? 162  LYS B CA  1 
ATOM   5072  C C   . LYS B 1 143 ? 79.30300  -39.49100 -45.16700 1.000 42.70000  ? 162  LYS B C   1 
ATOM   5073  O O   . LYS B 1 143 ? 79.48800  -40.50900 -44.49600 1.000 49.87000  ? 162  LYS B O   1 
ATOM   5074  C CB  . LYS B 1 143 ? 80.52200  -37.96700 -43.59000 1.000 41.69000  ? 162  LYS B CB  1 
ATOM   5075  C CG  . LYS B 1 143 ? 81.57200  -36.88700 -43.43700 1.000 48.97000  ? 162  LYS B CG  1 
ATOM   5076  C CD  . LYS B 1 143 ? 81.78700  -36.49100 -42.00100 1.000 55.02000  ? 162  LYS B CD  1 
ATOM   5077  C CE  . LYS B 1 143 ? 82.78300  -35.34700 -41.92000 1.000 63.81000  ? 162  LYS B CE  1 
ATOM   5078  N NZ  . LYS B 1 143 ? 82.21700  -34.10300 -42.52700 1.000 64.82000  ? 162  LYS B NZ  1 
ATOM   5079  N N   . GLY B 1 144 ? 78.27500  -39.36400 -46.00000 1.000 39.69000  ? 163  GLY B N   1 
ATOM   5080  C CA  . GLY B 1 144 ? 77.32700  -40.44100 -46.19100 1.000 44.36000  ? 163  GLY B CA  1 
ATOM   5081  C C   . GLY B 1 144 ? 76.18100  -40.48700 -45.21000 1.000 47.88000  ? 163  GLY B C   1 
ATOM   5082  O O   . GLY B 1 144 ? 75.61200  -41.56400 -45.00500 1.000 51.62000  ? 163  GLY B O   1 
ATOM   5083  N N   . LYS B 1 145 ? 75.82700  -39.36000 -44.59300 1.000 43.36000  ? 164  LYS B N   1 
ATOM   5084  C CA  . LYS B 1 145 ? 74.76900  -39.29900 -43.59300 1.000 44.70000  ? 164  LYS B CA  1 
ATOM   5085  C C   . LYS B 1 145 ? 73.84200  -38.12600 -43.90700 1.000 44.48000  ? 164  LYS B C   1 
ATOM   5086  O O   . LYS B 1 145 ? 74.06700  -37.35700 -44.84700 1.000 43.16000  ? 164  LYS B O   1 
ATOM   5087  C CB  . LYS B 1 145 ? 75.36100  -39.17100 -42.18400 1.000 37.45000  ? 164  LYS B CB  1 
ATOM   5088  C CG  . LYS B 1 145 ? 76.31900  -40.29400 -41.80200 1.000 40.91000  ? 164  LYS B CG  1 
ATOM   5089  C CD  . LYS B 1 145 ? 75.61900  -41.64200 -41.70300 1.000 36.47000  ? 164  LYS B CD  1 
ATOM   5090  C CE  . LYS B 1 145 ? 76.60100  -42.74200 -41.34000 1.000 30.57000  ? 164  LYS B CE  1 
ATOM   5091  N NZ  . LYS B 1 145 ? 75.94800  -44.08000 -41.25800 1.000 33.90000  ? 164  LYS B NZ  1 
ATOM   5092  N N   . SER B 1 146 ? 72.79200  -37.98100 -43.10500 1.000 39.10000  ? 165  SER B N   1 
ATOM   5093  C CA  . SER B 1 146 ? 71.91900  -36.81800 -43.17600 1.000 37.34000  ? 165  SER B CA  1 
ATOM   5094  C C   . SER B 1 146 ? 71.79900  -36.20700 -41.78800 1.000 37.06000  ? 165  SER B C   1 
ATOM   5095  O O   . SER B 1 146 ? 72.04600  -36.86800 -40.77600 1.000 42.68000  ? 165  SER B O   1 
ATOM   5096  C CB  . SER B 1 146 ? 70.54100  -37.17900 -43.73100 1.000 37.19000  ? 165  SER B CB  1 
ATOM   5097  O OG  . SER B 1 146 ? 69.88600  -38.11700 -42.89700 1.000 42.16000  ? 165  SER B OG  1 
ATOM   5098  N N   . ALA B 1 147 ? 71.45600  -34.91900 -41.75000 1.000 32.79000  ? 166  ALA B N   1 
ATOM   5099  C CA  . ALA B 1 147 ? 71.32900  -34.22900 -40.46900 1.000 34.99000  ? 166  ALA B CA  1 
ATOM   5100  C C   . ALA B 1 147 ? 70.13400  -34.73700 -39.65900 1.000 38.14000  ? 166  ALA B C   1 
ATOM   5101  O O   . ALA B 1 147 ? 70.29000  -35.13400 -38.49600 1.000 37.67000  ? 166  ALA B O   1 
ATOM   5102  C CB  . ALA B 1 147 ? 71.22400  -32.72100 -40.69800 1.000 31.10000  ? 166  ALA B CB  1 
ATOM   5103  N N   . LEU B 1 148 ? 68.94100  -34.75900 -40.26200 1.000 33.52000  ? 167  LEU B N   1 
ATOM   5104  C CA  . LEU B 1 148 ? 67.69500  -34.79800 -39.50700 1.000 32.70000  ? 167  LEU B CA  1 
ATOM   5105  C C   . LEU B 1 148 ? 66.61900  -35.60200 -40.22000 1.000 37.66000  ? 167  LEU B C   1 
ATOM   5106  O O   . LEU B 1 148 ? 66.36600  -35.38800 -41.40700 1.000 39.37000  ? 167  LEU B O   1 
ATOM   5107  C CB  . LEU B 1 148 ? 67.18000  -33.37500 -39.26600 1.000 36.94000  ? 167  LEU B CB  1 
ATOM   5108  C CG  . LEU B 1 148 ? 65.79400  -33.20100 -38.62100 1.000 34.45000  ? 167  LEU B CG  1 
ATOM   5109  C CD1 . LEU B 1 148 ? 65.73300  -33.75100 -37.20100 1.000 34.28000  ? 167  LEU B CD1 1 
ATOM   5110  C CD2 . LEU B 1 148 ? 65.39900  -31.74100 -38.64700 1.000 30.35000  ? 167  LEU B CD2 1 
ATOM   5111  N N   . MET B 1 149 ? 65.96100  -36.49600 -39.48400 1.000 36.77000  ? 168  MET B N   1 
ATOM   5112  C CA  . MET B 1 149 ? 64.77100  -37.17300 -39.98200 1.000 35.64000  ? 168  MET B CA  1 
ATOM   5113  C C   . MET B 1 149 ? 63.73000  -37.27400 -38.88000 1.000 42.55000  ? 168  MET B C   1 
ATOM   5114  O O   . MET B 1 149 ? 63.99500  -37.84700 -37.81900 1.000 40.26000  ? 168  MET B O   1 
ATOM   5115  C CB  . MET B 1 149 ? 65.09400  -38.56500 -40.51800 1.000 34.66000  ? 168  MET B CB  1 
ATOM   5116  C CG  . MET B 1 149 ? 65.86900  -38.51000 -41.80900 1.000 48.12000  ? 168  MET B CG  1 
ATOM   5117  S SD  . MET B 1 149 ? 66.00400  -40.13100 -42.55100 1.000 54.36000  ? 168  MET B SD  1 
ATOM   5118  C CE  . MET B 1 149 ? 64.29200  -40.33700 -43.00300 1.000 44.83000  ? 168  MET B CE  1 
ATOM   5119  N N   . PHE B 1 150 ? 62.53800  -36.74800 -39.14300 1.000 36.89000  ? 169  PHE B N   1 
ATOM   5120  C CA  . PHE B 1 150 ? 61.43300  -36.94100 -38.22200 1.000 36.71000  ? 169  PHE B CA  1 
ATOM   5121  C C   . PHE B 1 150 ? 60.12500  -37.03300 -38.99700 1.000 31.49000  ? 169  PHE B C   1 
ATOM   5122  O O   . PHE B 1 150 ? 60.03500  -36.65000 -40.16700 1.000 33.06000  ? 169  PHE B O   1 
ATOM   5123  C CB  . PHE B 1 150 ? 61.38800  -35.82700 -37.16800 1.000 34.59000  ? 169  PHE B CB  1 
ATOM   5124  C CG  . PHE B 1 150 ? 61.03700  -34.47600 -37.71400 1.000 36.52000  ? 169  PHE B CG  1 
ATOM   5125  C CD1 . PHE B 1 150 ? 62.00000  -33.69900 -38.34300 1.000 32.35000  ? 169  PHE B CD1 1 
ATOM   5126  C CD2 . PHE B 1 150 ? 59.76300  -33.94900 -37.53100 1.000 31.14000  ? 169  PHE B CD2 1 
ATOM   5127  C CE1 . PHE B 1 150 ? 61.69100  -32.44100 -38.83000 1.000 34.44000  ? 169  PHE B CE1 1 
ATOM   5128  C CE2 . PHE B 1 150 ? 59.44600  -32.68600 -38.00700 1.000 35.60000  ? 169  PHE B CE2 1 
ATOM   5129  C CZ  . PHE B 1 150 ? 60.41600  -31.92700 -38.65600 1.000 34.01000  ? 169  PHE B CZ  1 
ATOM   5130  N N   . ASN B 1 151 ? 59.11600  -37.57400 -38.31800 1.000 40.08000  ? 170  ASN B N   1 
ATOM   5131  C CA  . ASN B 1 151 ? 57.78200  -37.78100 -38.87200 1.000 36.07000  ? 170  ASN B CA  1 
ATOM   5132  C C   . ASN B 1 151 ? 57.19300  -36.47600 -39.38300 1.000 30.67000  ? 170  ASN B C   1 
ATOM   5133  O O   . ASN B 1 151 ? 56.94100  -35.56600 -38.59300 1.000 34.60000  ? 170  ASN B O   1 
ATOM   5134  C CB  . ASN B 1 151 ? 56.87700  -38.37600 -37.79900 1.000 37.13000  ? 170  ASN B CB  1 
ATOM   5135  C CG  . ASN B 1 151 ? 55.54500  -38.81500 -38.33700 1.000 38.57000  ? 170  ASN B CG  1 
ATOM   5136  O OD1 . ASN B 1 151 ? 55.27400  -38.70400 -39.53000 1.000 38.79000  ? 170  ASN B OD1 1 
ATOM   5137  N ND2 . ASN B 1 151 ? 54.68600  -39.30800 -37.44500 1.000 39.45000  ? 170  ASN B ND2 1 
ATOM   5138  N N   . LEU B 1 152 ? 56.98700  -36.37100 -40.69300 1.000 34.71000  ? 171  LEU B N   1 
ATOM   5139  C CA  . LEU B 1 152 ? 56.41000  -35.18600 -41.31100 1.000 30.65000  ? 171  LEU B CA  1 
ATOM   5140  C C   . LEU B 1 152 ? 54.93800  -35.37000 -41.67200 1.000 36.62000  ? 171  LEU B C   1 
ATOM   5141  O O   . LEU B 1 152 ? 54.32300  -34.44300 -42.21200 1.000 38.89000  ? 171  LEU B O   1 
ATOM   5142  C CB  . LEU B 1 152 ? 57.21100  -34.82600 -42.57200 1.000 33.00000  ? 171  LEU B CB  1 
ATOM   5143  C CG  . LEU B 1 152 ? 58.69700  -34.50100 -42.35400 1.000 38.37000  ? 171  LEU B CG  1 
ATOM   5144  C CD1 . LEU B 1 152 ? 59.42300  -34.31000 -43.66500 1.000 27.66000  ? 171  LEU B CD1 1 
ATOM   5145  C CD2 . LEU B 1 152 ? 58.87800  -33.27400 -41.47200 1.000 34.19000  ? 171  LEU B CD2 1 
ATOM   5146  N N   . GLN B 1 153 ? 54.36300  -36.54200 -41.40000 1.000 34.01000  ? 172  GLN B N   1 
ATOM   5147  C CA  . GLN B 1 153 ? 52.97500  -36.79300 -41.77700 1.000 42.86000  ? 172  GLN B CA  1 
ATOM   5148  C C   . GLN B 1 153 ? 51.98600  -36.25900 -40.74900 1.000 40.54000  ? 172  GLN B C   1 
ATOM   5149  O O   . GLN B 1 153 ? 50.86000  -35.91200 -41.11300 1.000 40.92000  ? 172  GLN B O   1 
ATOM   5150  C CB  . GLN B 1 153 ? 52.74900  -38.29500 -41.97900 1.000 38.34000  ? 172  GLN B CB  1 
ATOM   5151  C CG  . GLN B 1 153 ? 53.77900  -38.88800 -42.90100 1.000 38.75000  ? 172  GLN B CG  1 
ATOM   5152  C CD  . GLN B 1 153 ? 53.80300  -38.19000 -44.24200 1.000 38.19000  ? 172  GLN B CD  1 
ATOM   5153  O OE1 . GLN B 1 153 ? 52.76300  -37.95600 -44.85800 1.000 41.35000  ? 172  GLN B OE1 1 
ATOM   5154  N NE2 . GLN B 1 153 ? 54.98800  -37.79400 -44.66900 1.000 39.82000  ? 172  GLN B NE2 1 
ATOM   5155  N N   . GLU B 1 154 ? 52.38100  -36.17700 -39.47800 1.000 39.24000  ? 173  GLU B N   1 
ATOM   5156  C CA  . GLU B 1 154 ? 51.46100  -35.86400 -38.39200 1.000 37.03000  ? 173  GLU B CA  1 
ATOM   5157  C C   . GLU B 1 154 ? 51.79400  -34.50800 -37.78500 1.000 41.49000  ? 173  GLU B C   1 
ATOM   5158  O O   . GLU B 1 154 ? 52.94800  -34.28600 -37.38100 1.000 37.13000  ? 173  GLU B O   1 
ATOM   5159  C CB  . GLU B 1 154 ? 51.52100  -36.95200 -37.32600 1.000 34.88000  ? 173  GLU B CB  1 
ATOM   5160  C CG  . GLU B 1 154 ? 51.19900  -38.34200 -37.85900 1.000 48.52000  ? 173  GLU B CG  1 
ATOM   5161  C CD  . GLU B 1 154 ? 49.80100  -38.44400 -38.46900 1.000 57.16000  ? 173  GLU B CD  1 
ATOM   5162  O OE1 . GLU B 1 154 ? 48.89200  -37.69200 -38.04000 1.000 57.18000  ? 173  GLU B OE1 1 
ATOM   5163  O OE2 . GLU B 1 154 ? 49.60800  -39.29500 -39.36800 1.000 52.03000  ? 173  GLU B OE2 1 
ATOM   5164  N N   . PRO B 1 155 ? 50.83000  -33.58500 -37.68100 1.000 38.88000  ? 174  PRO B N   1 
ATOM   5165  C CA  . PRO B 1 155 ? 51.16100  -32.21800 -37.25500 1.000 38.38000  ? 174  PRO B CA  1 
ATOM   5166  C C   . PRO B 1 155 ? 51.69800  -32.14900 -35.84200 1.000 36.97000  ? 174  PRO B C   1 
ATOM   5167  O O   . PRO B 1 155 ? 52.36300  -31.16500 -35.49700 1.000 37.45000  ? 174  PRO B O   1 
ATOM   5168  C CB  . PRO B 1 155 ? 49.82100  -31.47900 -37.35500 1.000 38.04000  ? 174  PRO B CB  1 
ATOM   5169  C CG  . PRO B 1 155 ? 48.93300  -32.37600 -38.09700 1.000 42.24000  ? 174  PRO B CG  1 
ATOM   5170  C CD  . PRO B 1 155 ? 49.37900  -33.76400 -37.79200 1.000 39.21000  ? 174  PRO B CD  1 
ATOM   5171  N N   . TYR B 1 156 ? 51.40000  -33.14300 -35.00300 1.000 32.98000  ? 175  TYR B N   1 
ATOM   5172  C CA  . TYR B 1 156 ? 52.00100  -33.17800 -33.67500 1.000 38.46000  ? 175  TYR B CA  1 
ATOM   5173  C C   . TYR B 1 156 ? 53.51800  -33.03000 -33.76000 1.000 36.50000  ? 175  TYR B C   1 
ATOM   5174  O O   . TYR B 1 156 ? 54.12100  -32.30800 -32.95900 1.000 32.90000  ? 175  TYR B O   1 
ATOM   5175  C CB  . TYR B 1 156 ? 51.62600  -34.47600 -32.96700 1.000 36.94000  ? 175  TYR B CB  1 
ATOM   5176  C CG  . TYR B 1 156 ? 52.25200  -34.65800 -31.60500 1.000 38.02000  ? 175  TYR B CG  1 
ATOM   5177  C CD1 . TYR B 1 156 ? 51.70700  -34.06300 -30.47400 1.000 35.87000  ? 175  TYR B CD1 1 
ATOM   5178  C CD2 . TYR B 1 156 ? 53.40700  -35.42500 -31.45600 1.000 38.22000  ? 175  TYR B CD2 1 
ATOM   5179  C CE1 . TYR B 1 156 ? 52.28500  -34.23300 -29.22700 1.000 31.17000  ? 175  TYR B CE1 1 
ATOM   5180  C CE2 . TYR B 1 156 ? 53.99800  -35.59900 -30.21700 1.000 39.30000  ? 175  TYR B CE2 1 
ATOM   5181  C CZ  . TYR B 1 156 ? 53.43400  -35.00100 -29.10300 1.000 39.45000  ? 175  TYR B CZ  1 
ATOM   5182  O OH  . TYR B 1 156 ? 54.02700  -35.17400 -27.86800 1.000 36.51000  ? 175  TYR B OH  1 
ATOM   5183  N N   . PHE B 1 157 ? 54.15600  -33.66700 -34.74900 1.000 31.74000  ? 176  PHE B N   1 
ATOM   5184  C CA  . PHE B 1 157 ? 55.61000  -33.55900 -34.77800 1.000 30.27000  ? 176  PHE B CA  1 
ATOM   5185  C C   . PHE B 1 157 ? 56.12600  -32.31200 -35.48800 1.000 34.05000  ? 176  PHE B C   1 
ATOM   5186  O O   . PHE B 1 157 ? 57.22800  -31.85200 -35.17400 1.000 35.59000  ? 176  PHE B O   1 
ATOM   5187  C CB  . PHE B 1 157 ? 56.30500  -34.74800 -35.44500 1.000 28.57000  ? 176  PHE B CB  1 
ATOM   5188  C CG  . PHE B 1 157 ? 56.09400  -36.07400 -34.77300 1.000 31.21000  ? 176  PHE B CG  1 
ATOM   5189  C CD1 . PHE B 1 157 ? 54.84200  -36.56300 -34.47300 1.000 34.30000  ? 176  PHE B CD1 1 
ATOM   5190  C CD2 . PHE B 1 157 ? 57.19300  -36.71200 -34.21900 1.000 37.75000  ? 176  PHE B CD2 1 
ATOM   5191  C CE1 . PHE B 1 157 ? 54.70300  -37.77800 -33.82500 1.000 35.82000  ? 176  PHE B CE1 1 
ATOM   5192  C CE2 . PHE B 1 157 ? 57.06400  -37.89600 -33.53000 1.000 35.96000  ? 176  PHE B CE2 1 
ATOM   5193  C CZ  . PHE B 1 157 ? 55.81300  -38.43000 -33.32800 1.000 40.10000  ? 176  PHE B CZ  1 
ATOM   5194  N N   . THR B 1 158 ? 55.39100  -31.77000 -36.45200 1.000 32.26000  ? 177  THR B N   1 
ATOM   5195  C CA  . THR B 1 158 ? 55.85300  -30.58800 -37.17500 1.000 35.24000  ? 177  THR B CA  1 
ATOM   5196  C C   . THR B 1 158 ? 55.44000  -29.28800 -36.50900 1.000 34.45000  ? 177  THR B C   1 
ATOM   5197  O O   . THR B 1 158 ? 56.02600  -28.23600 -36.80400 1.000 33.45000  ? 177  THR B O   1 
ATOM   5198  C CB  . THR B 1 158 ? 55.31700  -30.57700 -38.61200 1.000 36.04000  ? 177  THR B CB  1 
ATOM   5199  O OG1 . THR B 1 158 ? 53.88800  -30.67400 -38.58000 1.000 42.03000  ? 177  THR B OG1 1 
ATOM   5200  C CG2 . THR B 1 158 ? 55.89300  -31.72900 -39.43400 1.000 33.67000  ? 177  THR B CG2 1 
ATOM   5201  N N   . TRP B 1 159 ? 54.44400  -29.33800 -35.62800 1.000 39.41000  ? 178  TRP B N   1 
ATOM   5202  C CA  . TRP B 1 159 ? 53.95500  -28.12000 -34.99900 1.000 34.52000  ? 178  TRP B CA  1 
ATOM   5203  C C   . TRP B 1 159 ? 55.00400  -27.36800 -34.17900 1.000 32.77000  ? 178  TRP B C   1 
ATOM   5204  O O   . TRP B 1 159 ? 54.91300  -26.12700 -34.13400 1.000 31.87000  ? 178  TRP B O   1 
ATOM   5205  C CB  . TRP B 1 159 ? 52.73400  -28.44400 -34.13200 1.000 34.78000  ? 178  TRP B CB  1 
ATOM   5206  C CG  . TRP B 1 159 ? 52.07700  -27.20600 -33.65100 1.000 37.00000  ? 178  TRP B CG  1 
ATOM   5207  C CD1 . TRP B 1 159 ? 52.11000  -26.68800 -32.38900 1.000 36.00000  ? 178  TRP B CD1 1 
ATOM   5208  C CD2 . TRP B 1 159 ? 51.33300  -26.28000 -34.45100 1.000 33.04000  ? 178  TRP B CD2 1 
ATOM   5209  N NE1 . TRP B 1 159 ? 51.40000  -25.50500 -32.34900 1.000 39.06000  ? 178  TRP B NE1 1 
ATOM   5210  C CE2 . TRP B 1 159 ? 50.91600  -25.23600 -33.60200 1.000 33.58000  ? 178  TRP B CE2 1 
ATOM   5211  C CE3 . TRP B 1 159 ? 50.95800  -26.24700 -35.80100 1.000 39.95000  ? 178  TRP B CE3 1 
ATOM   5212  C CZ2 . TRP B 1 159 ? 50.14600  -24.16500 -34.05800 1.000 37.28000  ? 178  TRP B CZ2 1 
ATOM   5213  C CZ3 . TRP B 1 159 ? 50.19400  -25.18300 -36.25400 1.000 36.20000  ? 178  TRP B CZ3 1 
ATOM   5214  C CH2 . TRP B 1 159 ? 49.79500  -24.15600 -35.38200 1.000 36.45000  ? 178  TRP B CH2 1 
ATOM   5215  N N   . PRO B 1 160 ? 55.96700  -28.01100 -33.49500 1.000 29.41000  ? 179  PRO B N   1 
ATOM   5216  C CA  . PRO B 1 160 ? 56.95800  -27.21300 -32.75300 1.000 33.50000  ? 179  PRO B CA  1 
ATOM   5217  C C   . PRO B 1 160 ? 57.64900  -26.16400 -33.60400 1.000 30.81000  ? 179  PRO B C   1 
ATOM   5218  O O   . PRO B 1 160 ? 57.79900  -25.01900 -33.16200 1.000 29.64000  ? 179  PRO B O   1 
ATOM   5219  C CB  . PRO B 1 160 ? 57.94500  -28.27500 -32.24800 1.000 34.97000  ? 179  PRO B CB  1 
ATOM   5220  C CG  . PRO B 1 160 ? 57.14400  -29.50100 -32.13300 1.000 25.47000  ? 179  PRO B CG  1 
ATOM   5221  C CD  . PRO B 1 160 ? 56.17700  -29.45600 -33.27600 1.000 30.63000  ? 179  PRO B CD  1 
ATOM   5222  N N   . LEU B 1 161 ? 58.04100  -26.51200 -34.82700 1.000 31.37000  ? 180  LEU B N   1 
ATOM   5223  C CA  . LEU B 1 161 ? 58.61200  -25.52600 -35.73600 1.000 31.02000  ? 180  LEU B CA  1 
ATOM   5224  C C   . LEU B 1 161 ? 57.58900  -24.46200 -36.11700 1.000 32.16000  ? 180  LEU B C   1 
ATOM   5225  O O   . LEU B 1 161 ? 57.87500  -23.26100 -36.04000 1.000 34.36000  ? 180  LEU B O   1 
ATOM   5226  C CB  . LEU B 1 161 ? 59.15900  -26.22900 -36.98100 1.000 37.40000  ? 180  LEU B CB  1 
ATOM   5227  C CG  . LEU B 1 161 ? 59.70400  -25.39000 -38.14400 1.000 30.32000  ? 180  LEU B CG  1 
ATOM   5228  C CD1 . LEU B 1 161 ? 60.80300  -24.46600 -37.67700 1.000 37.19000  ? 180  LEU B CD1 1 
ATOM   5229  C CD2 . LEU B 1 161 ? 60.22700  -26.32400 -39.23600 1.000 30.55000  ? 180  LEU B CD2 1 
ATOM   5230  N N   . ILE B 1 162 ? 56.38300  -24.88100 -36.51900 1.000 36.72000  ? 181  ILE B N   1 
ATOM   5231  C CA  . ILE B 1 162 ? 55.39100  -23.93300 -37.03200 1.000 33.45000  ? 181  ILE B CA  1 
ATOM   5232  C C   . ILE B 1 162 ? 54.98300  -22.92500 -35.96400 1.000 32.23000  ? 181  ILE B C   1 
ATOM   5233  O O   . ILE B 1 162 ? 54.67400  -21.76800 -36.27200 1.000 34.36000  ? 181  ILE B O   1 
ATOM   5234  C CB  . ILE B 1 162 ? 54.17100  -24.69300 -37.58300 1.000 31.73000  ? 181  ILE B CB  1 
ATOM   5235  C CG1 . ILE B 1 162 ? 54.58700  -25.59800 -38.73700 1.000 37.02000  ? 181  ILE B CG1 1 
ATOM   5236  C CG2 . ILE B 1 162 ? 53.10400  -23.72500 -38.06800 1.000 31.77000  ? 181  ILE B CG2 1 
ATOM   5237  C CD1 . ILE B 1 162 ? 53.50300  -26.57400 -39.16900 1.000 32.80000  ? 181  ILE B CD1 1 
ATOM   5238  N N   . ALA B 1 163 ? 54.97700  -23.33900 -34.69900 1.000 27.06000  ? 182  ALA B N   1 
ATOM   5239  C CA  . ALA B 1 163 ? 54.48300  -22.48500 -33.63300 1.000 36.91000  ? 182  ALA B CA  1 
ATOM   5240  C C   . ALA B 1 163 ? 55.52700  -21.51000 -33.12300 1.000 39.91000  ? 182  ALA B C   1 
ATOM   5241  O O   . ALA B 1 163 ? 55.15700  -20.48200 -32.54200 1.000 38.51000  ? 182  ALA B O   1 
ATOM   5242  C CB  . ALA B 1 163 ? 53.98100  -23.33900 -32.46800 1.000 39.45000  ? 182  ALA B CB  1 
ATOM   5243  N N   . ALA B 1 164 ? 56.81200  -21.81100 -33.33900 1.000 34.72000  ? 183  ALA B N   1 
ATOM   5244  C CA  . ALA B 1 164 ? 57.90100  -21.09400 -32.67900 1.000 37.23000  ? 183  ALA B CA  1 
ATOM   5245  C C   . ALA B 1 164 ? 57.79700  -19.58300 -32.86000 1.000 33.74000  ? 183  ALA B C   1 
ATOM   5246  O O   . ALA B 1 164 ? 58.04700  -18.82000 -31.92200 1.000 38.23000  ? 183  ALA B O   1 
ATOM   5247  C CB  . ALA B 1 164 ? 59.24600  -21.60800 -33.20300 1.000 32.04000  ? 183  ALA B CB  1 
ATOM   5248  N N   . ASP B 1 165 ? 57.44000  -19.13100 -34.06000 1.000 35.66000  ? 184  ASP B N   1 
ATOM   5249  C CA  . ASP B 1 165 ? 57.41100  -17.70700 -34.36800 1.000 37.00000  ? 184  ASP B CA  1 
ATOM   5250  C C   . ASP B 1 165 ? 56.00600  -17.11200 -34.27700 1.000 41.81000  ? 184  ASP B C   1 
ATOM   5251  O O   . ASP B 1 165 ? 55.82000  -15.93500 -34.60400 1.000 45.13000  ? 184  ASP B O   1 
ATOM   5252  C CB  . ASP B 1 165 ? 58.05000  -17.47000 -35.74500 1.000 45.86000  ? 184  ASP B CB  1 
ATOM   5253  C CG  . ASP B 1 165 ? 58.27700  -15.99000 -36.05500 1.000 49.24000  ? 184  ASP B CG  1 
ATOM   5254  O OD1 . ASP B 1 165 ? 59.03200  -15.32600 -35.30700 1.000 46.48000  ? 184  ASP B OD1 1 
ATOM   5255  O OD2 . ASP B 1 165 ? 57.76000  -15.51800 -37.09300 1.000 46.87000  ? 184  ASP B OD2 1 
ATOM   5256  N N   . GLY B 1 166 ? 55.02100  -17.87700 -33.79400 1.000 38.82000  ? 185  GLY B N   1 
ATOM   5257  C CA  . GLY B 1 166 ? 53.73500  -17.28300 -33.46600 1.000 33.13000  ? 185  GLY B CA  1 
ATOM   5258  C C   . GLY B 1 166 ? 52.49900  -18.12500 -33.70600 1.000 34.21000  ? 185  GLY B C   1 
ATOM   5259  O O   . GLY B 1 166 ? 51.38900  -17.67200 -33.42200 1.000 39.53000  ? 185  GLY B O   1 
ATOM   5260  N N   . GLY B 1 167 ? 52.65800  -19.33500 -34.23300 1.000 40.97000  ? 186  GLY B N   1 
ATOM   5261  C CA  . GLY B 1 167 ? 51.52300  -20.22100 -34.38100 1.000 34.13000  ? 186  GLY B CA  1 
ATOM   5262  C C   . GLY B 1 167 ? 51.03200  -20.75800 -33.04900 1.000 32.79000  ? 186  GLY B C   1 
ATOM   5263  O O   . GLY B 1 167 ? 51.80400  -20.98400 -32.12100 1.000 37.75000  ? 186  GLY B O   1 
ATOM   5264  N N   . TYR B 1 168 ? 49.71500  -20.94900 -32.96100 1.000 40.21000  ? 187  TYR B N   1 
ATOM   5265  C CA  . TYR B 1 168 ? 49.06600  -21.59700 -31.82600 1.000 36.35000  ? 187  TYR B CA  1 
ATOM   5266  C C   . TYR B 1 168 ? 47.77000  -22.21100 -32.32500 1.000 34.70000  ? 187  TYR B C   1 
ATOM   5267  O O   . TYR B 1 168 ? 47.28400  -21.86600 -33.40400 1.000 36.56000  ? 187  TYR B O   1 
ATOM   5268  C CB  . TYR B 1 168 ? 48.81600  -20.61700 -30.66900 1.000 31.32000  ? 187  TYR B CB  1 
ATOM   5269  C CG  . TYR B 1 168 ? 48.01300  -19.39400 -31.06600 1.000 36.33000  ? 187  TYR B CG  1 
ATOM   5270  C CD1 . TYR B 1 168 ? 46.62300  -19.38300 -30.99200 1.000 32.41000  ? 187  TYR B CD1 1 
ATOM   5271  C CD2 . TYR B 1 168 ? 48.65600  -18.24200 -31.51900 1.000 33.15000  ? 187  TYR B CD2 1 
ATOM   5272  C CE1 . TYR B 1 168 ? 45.89300  -18.25800 -31.36100 1.000 31.68000  ? 187  TYR B CE1 1 
ATOM   5273  C CE2 . TYR B 1 168 ? 47.93800  -17.11500 -31.88100 1.000 31.24000  ? 187  TYR B CE2 1 
ATOM   5274  C CZ  . TYR B 1 168 ? 46.55700  -17.12900 -31.80600 1.000 37.28000  ? 187  TYR B CZ  1 
ATOM   5275  O OH  . TYR B 1 168 ? 45.85000  -16.00600 -32.17800 1.000 33.00000  ? 187  TYR B OH  1 
ATOM   5276  N N   . ALA B 1 169 ? 47.22600  -23.15200 -31.55000 1.000 35.67000  ? 188  ALA B N   1 
ATOM   5277  C CA  . ALA B 1 169 ? 45.96300  -23.77900 -31.94400 1.000 33.05000  ? 188  ALA B CA  1 
ATOM   5278  C C   . ALA B 1 169 ? 44.76400  -22.93000 -31.52600 1.000 36.56000  ? 188  ALA B C   1 
ATOM   5279  O O   . ALA B 1 169 ? 44.06300  -22.36200 -32.37000 1.000 40.96000  ? 188  ALA B O   1 
ATOM   5280  C CB  . ALA B 1 169 ? 45.86800  -25.18700 -31.34600 1.000 34.17000  ? 188  ALA B CB  1 
ATOM   5281  N N   . PHE B 1 170 ? 44.54200  -22.79300 -30.22400 1.000 35.16000  ? 189  PHE B N   1 
ATOM   5282  C CA  . PHE B 1 170 ? 43.48200  -21.94300 -29.70100 1.000 34.83000  ? 189  PHE B CA  1 
ATOM   5283  C C   . PHE B 1 170 ? 44.09600  -21.02700 -28.65600 1.000 39.90000  ? 189  PHE B C   1 
ATOM   5284  O O   . PHE B 1 170 ? 44.89100  -21.47600 -27.82400 1.000 38.42000  ? 189  PHE B O   1 
ATOM   5285  C CB  . PHE B 1 170 ? 42.33800  -22.75600 -29.06800 1.000 35.63000  ? 189  PHE B CB  1 
ATOM   5286  C CG  . PHE B 1 170 ? 41.62700  -23.67800 -30.02600 1.000 37.89000  ? 189  PHE B CG  1 
ATOM   5287  C CD1 . PHE B 1 170 ? 40.70600  -23.18600 -30.93800 1.000 39.16000  ? 189  PHE B CD1 1 
ATOM   5288  C CD2 . PHE B 1 170 ? 41.85300  -25.04800 -29.98500 1.000 39.63000  ? 189  PHE B CD2 1 
ATOM   5289  C CE1 . PHE B 1 170 ? 40.04900  -24.04100 -31.81700 1.000 41.37000  ? 189  PHE B CE1 1 
ATOM   5290  C CE2 . PHE B 1 170 ? 41.19100  -25.90700 -30.85100 1.000 40.20000  ? 189  PHE B CE2 1 
ATOM   5291  C CZ  . PHE B 1 170 ? 40.29100  -25.40200 -31.77000 1.000 35.67000  ? 189  PHE B CZ  1 
ATOM   5292  N N   . LYS B 1 171 ? 43.74000  -19.74500 -28.70800 1.000 36.11000  ? 190  LYS B N   1 
ATOM   5293  C CA  . LYS B 1 171 ? 44.32200  -18.78200 -27.78500 1.000 39.39000  ? 190  LYS B CA  1 
ATOM   5294  C C   . LYS B 1 171 ? 43.95000  -19.15300 -26.35700 1.000 42.94000  ? 190  LYS B C   1 
ATOM   5295  O O   . LYS B 1 171 ? 42.80000  -19.49900 -26.07500 1.000 41.98000  ? 190  LYS B O   1 
ATOM   5296  C CB  . LYS B 1 171 ? 43.83200  -17.37200 -28.10600 1.000 42.04000  ? 190  LYS B CB  1 
ATOM   5297  C CG  . LYS B 1 171 ? 44.60700  -16.30400 -27.38500 1.000 42.96000  ? 190  LYS B CG  1 
ATOM   5298  C CD  . LYS B 1 171 ? 46.00500  -16.26800 -27.99800 1.000 55.50000  ? 190  LYS B CD  1 
ATOM   5299  C CE  . LYS B 1 171 ? 46.88300  -15.15300 -27.46200 1.000 53.01000  ? 190  LYS B CE  1 
ATOM   5300  N NZ  . LYS B 1 171 ? 48.24000  -15.24400 -28.08600 1.000 52.37000  ? 190  LYS B NZ  1 
ATOM   5301  N N   . TYR B 1 172 ? 44.93300  -19.12500 -25.46600 1.000 47.33000  ? 191  TYR B N   1 
ATOM   5302  C CA  . TYR B 1 172 ? 44.71400  -19.42600 -24.06000 1.000 44.71000  ? 191  TYR B CA  1 
ATOM   5303  C C   . TYR B 1 172 ? 44.73200  -18.14600 -23.24200 1.000 46.26000  ? 191  TYR B C   1 
ATOM   5304  O O   . TYR B 1 172 ? 45.52800  -17.23900 -23.50200 1.000 48.31000  ? 191  TYR B O   1 
ATOM   5305  C CB  . TYR B 1 172 ? 45.77400  -20.38600 -23.51800 1.000 44.12000  ? 191  TYR B CB  1 
ATOM   5306  C CG  . TYR B 1 172 ? 45.57900  -20.71000 -22.05700 1.000 48.26000  ? 191  TYR B CG  1 
ATOM   5307  C CD1 . TYR B 1 172 ? 44.56300  -21.56700 -21.65000 1.000 46.69000  ? 191  TYR B CD1 1 
ATOM   5308  C CD2 . TYR B 1 172 ? 46.40200  -20.15400 -21.07800 1.000 55.21000  ? 191  TYR B CD2 1 
ATOM   5309  C CE1 . TYR B 1 172 ? 44.37100  -21.86800 -20.30800 1.000 50.41000  ? 191  TYR B CE1 1 
ATOM   5310  C CE2 . TYR B 1 172 ? 46.21700  -20.44900 -19.72900 1.000 51.69000  ? 191  TYR B CE2 1 
ATOM   5311  C CZ  . TYR B 1 172 ? 45.19900  -21.30800 -19.35100 1.000 56.05000  ? 191  TYR B CZ  1 
ATOM   5312  O OH  . TYR B 1 172 ? 45.00200  -21.61700 -18.02000 1.000 55.68000  ? 191  TYR B OH  1 
ATOM   5313  N N   . ALA B 1 173 ? 43.84100  -18.07700 -22.25800 1.000 50.53000  ? 192  ALA B N   1 
ATOM   5314  C CA  . ALA B 1 173 ? 43.85000  -16.96900 -21.30700 1.000 52.61000  ? 192  ALA B CA  1 
ATOM   5315  C C   . ALA B 1 173 ? 43.05400  -17.39800 -20.08100 1.000 54.20000  ? 192  ALA B C   1 
ATOM   5316  O O   . ALA B 1 173 ? 41.84500  -17.62800 -20.18100 1.000 54.96000  ? 192  ALA B O   1 
ATOM   5317  C CB  . ALA B 1 173 ? 43.26900  -15.70400 -21.93300 1.000 43.40000  ? 192  ALA B CB  1 
ATOM   5318  N N   . ALA B 1 174 ? 43.74100  -17.54900 -18.94700 1.000 59.30000  ? 193  ALA B N   1 
ATOM   5319  C CA  . ALA B 1 174 ? 43.09900  -17.63900 -17.63200 1.000 58.93000  ? 193  ALA B CA  1 
ATOM   5320  C C   . ALA B 1 174 ? 42.11800  -18.81000 -17.53800 1.000 53.17000  ? 193  ALA B C   1 
ATOM   5321  O O   . ALA B 1 174 ? 40.95500  -18.64400 -17.16900 1.000 63.90000  ? 193  ALA B O   1 
ATOM   5322  C CB  . ALA B 1 174 ? 42.39700  -16.32000 -17.29300 1.000 66.48000  ? 193  ALA B CB  1 
ATOM   5323  N N   . GLY B 1 175 ? 42.59200  -20.00700 -17.87600 1.000 57.14000  ? 194  GLY B N   1 
ATOM   5324  C CA  . GLY B 1 175 ? 41.78900  -21.21000 -17.75400 1.000 55.52000  ? 194  GLY B CA  1 
ATOM   5325  C C   . GLY B 1 175 ? 40.74300  -21.41100 -18.83000 1.000 58.96000  ? 194  GLY B C   1 
ATOM   5326  O O   . GLY B 1 175 ? 39.88100  -22.29200 -18.68500 1.000 51.90000  ? 194  GLY B O   1 
ATOM   5327  N N   . LYS B 1 176 ? 40.78500  -20.63300 -19.91100 1.000 50.33000  ? 195  LYS B N   1 
ATOM   5328  C CA  . LYS B 1 176 ? 39.73300  -20.69700 -20.91100 1.000 50.75000  ? 195  LYS B CA  1 
ATOM   5329  C C   . LYS B 1 176 ? 40.34500  -20.63300 -22.29900 1.000 42.67000  ? 195  LYS B C   1 
ATOM   5330  O O   . LYS B 1 176 ? 41.15400  -19.74500 -22.58100 1.000 46.94000  ? 195  LYS B O   1 
ATOM   5331  C CB  . LYS B 1 176 ? 38.73800  -19.55000 -20.70300 1.000 42.79000  ? 195  LYS B CB  1 
ATOM   5332  C CG  . LYS B 1 176 ? 37.45500  -19.67500 -21.48800 1.000 53.14000  ? 195  LYS B CG  1 
ATOM   5333  C CD  . LYS B 1 176 ? 36.51500  -18.52400 -21.17700 1.000 50.74000  ? 195  LYS B CD  1 
ATOM   5334  C CE  . LYS B 1 176 ? 35.17100  -18.76400 -21.80800 1.000 50.01000  ? 195  LYS B CE  1 
ATOM   5335  N NZ  . LYS B 1 176 ? 35.29400  -18.81200 -23.28700 1.000 62.09000  ? 195  LYS B NZ  1 
ATOM   5336  N N   . TYR B 1 177 ? 39.95800  -21.56500 -23.16000 1.000 41.18000  ? 196  TYR B N   1 
ATOM   5337  C CA  . TYR B 1 177 ? 40.31700  -21.48700 -24.56800 1.000 36.47000  ? 196  TYR B CA  1 
ATOM   5338  C C   . TYR B 1 177 ? 39.22900  -20.77400 -25.36100 1.000 38.70000  ? 196  TYR B C   1 
ATOM   5339  O O   . TYR B 1 177 ? 38.03500  -20.94000 -25.09800 1.000 44.04000  ? 196  TYR B O   1 
ATOM   5340  C CB  . TYR B 1 177 ? 40.56900  -22.87900 -25.14300 1.000 39.64000  ? 196  TYR B CB  1 
ATOM   5341  C CG  . TYR B 1 177 ? 41.84500  -23.47100 -24.61500 1.000 38.64000  ? 196  TYR B CG  1 
ATOM   5342  C CD1 . TYR B 1 177 ? 43.07200  -23.04200 -25.10200 1.000 36.03000  ? 196  TYR B CD1 1 
ATOM   5343  C CD2 . TYR B 1 177 ? 41.83300  -24.43200 -23.61300 1.000 40.10000  ? 196  TYR B CD2 1 
ATOM   5344  C CE1 . TYR B 1 177 ? 44.25100  -23.55900 -24.61400 1.000 40.28000  ? 196  TYR B CE1 1 
ATOM   5345  C CE2 . TYR B 1 177 ? 43.01600  -24.95600 -23.11400 1.000 37.30000  ? 196  TYR B CE2 1 
ATOM   5346  C CZ  . TYR B 1 177 ? 44.21900  -24.51400 -23.62100 1.000 39.42000  ? 196  TYR B CZ  1 
ATOM   5347  O OH  . TYR B 1 177 ? 45.40400  -25.02300 -23.14600 1.000 42.38000  ? 196  TYR B OH  1 
ATOM   5348  N N   . ASP B 1 178 ? 39.65700  -19.96500 -26.31800 1.000 36.01000  ? 197  ASP B N   1 
ATOM   5349  C CA  . ASP B 1 178 ? 38.77400  -19.22300 -27.21400 1.000 37.13000  ? 197  ASP B CA  1 
ATOM   5350  C C   . ASP B 1 178 ? 38.78500  -19.93100 -28.56700 1.000 45.55000  ? 197  ASP B C   1 
ATOM   5351  O O   . ASP B 1 178 ? 39.72800  -19.76900 -29.34600 1.000 44.67000  ? 197  ASP B O   1 
ATOM   5352  C CB  . ASP B 1 178 ? 39.25200  -17.77700 -27.32000 1.000 38.17000  ? 197  ASP B CB  1 
ATOM   5353  C CG  . ASP B 1 178 ? 38.41900  -16.93600 -28.27800 1.000 45.63000  ? 197  ASP B CG  1 
ATOM   5354  O OD1 . ASP B 1 178 ? 37.44900  -17.44700 -28.87800 1.000 42.61000  ? 197  ASP B OD1 1 
ATOM   5355  O OD2 . ASP B 1 178 ? 38.77300  -15.74600 -28.46100 1.000 47.39000  ? 197  ASP B OD2 1 
ATOM   5356  N N   . ILE B 1 179 ? 37.72900  -20.69800 -28.87100 1.000 42.74000  ? 198  ILE B N   1 
ATOM   5357  C CA  . ILE B 1 179 ? 37.74000  -21.45600 -30.12400 1.000 41.62000  ? 198  ILE B CA  1 
ATOM   5358  C C   . ILE B 1 179 ? 37.53400  -20.54100 -31.31100 1.000 34.68000  ? 198  ILE B C   1 
ATOM   5359  O O   . ILE B 1 179 ? 37.62400  -20.98800 -32.45400 1.000 43.65000  ? 198  ILE B O   1 
ATOM   5360  C CB  . ILE B 1 179 ? 36.70000  -22.59500 -30.19900 1.000 35.66000  ? 198  ILE B CB  1 
ATOM   5361  C CG1 . ILE B 1 179 ? 35.28100  -22.10400 -29.95700 1.000 37.23000  ? 198  ILE B CG1 1 
ATOM   5362  C CG2 . ILE B 1 179 ? 37.04000  -23.71500 -29.30400 1.000 47.22000  ? 198  ILE B CG2 1 
ATOM   5363  C CD1 . ILE B 1 179 ? 34.28600  -23.20800 -30.22400 1.000 42.94000  ? 198  ILE B CD1 1 
ATOM   5364  N N   . LYS B 1 180 ? 37.25200  -19.27200 -31.07600 1.000 40.13000  ? 199  LYS B N   1 
ATOM   5365  C CA  . LYS B 1 180 ? 37.22100  -18.35300 -32.20300 1.000 45.99000  ? 199  LYS B CA  1 
ATOM   5366  C C   . LYS B 1 180 ? 38.58900  -17.76300 -32.53300 1.000 42.57000  ? 199  LYS B C   1 
ATOM   5367  O O   . LYS B 1 180 ? 38.71500  -17.06100 -33.54100 1.000 42.47000  ? 199  LYS B O   1 
ATOM   5368  C CB  . LYS B 1 180 ? 36.22700  -17.21800 -31.95000 1.000 43.00000  ? 199  LYS B CB  1 
ATOM   5369  C CG  . LYS B 1 180 ? 34.77300  -17.66700 -31.91500 1.000 48.72000  ? 199  LYS B CG  1 
ATOM   5370  C CD  . LYS B 1 180 ? 33.87300  -16.45300 -31.90100 1.000 52.11000  ? 199  LYS B CD  1 
ATOM   5371  C CE  . LYS B 1 180 ? 33.93600  -15.77900 -33.27400 1.000 52.18000  ? 199  LYS B CE  1 
ATOM   5372  N NZ  . LYS B 1 180 ? 33.03200  -14.60700 -33.41000 1.000 59.11000  ? 199  LYS B NZ  1 
ATOM   5373  N N   . ASP B 1 181 ? 39.61000  -18.02800 -31.72800 1.000 37.36000  ? 200  ASP B N   1 
ATOM   5374  C CA  . ASP B 1 181 ? 40.91800  -17.40600 -31.90500 1.000 40.99000  ? 200  ASP B CA  1 
ATOM   5375  C C   . ASP B 1 181 ? 41.91500  -18.51300 -32.24200 1.000 40.65000  ? 200  ASP B C   1 
ATOM   5376  O O   . ASP B 1 181 ? 42.55900  -19.08600 -31.35900 1.000 39.65000  ? 200  ASP B O   1 
ATOM   5377  C CB  . ASP B 1 181 ? 41.31900  -16.61600 -30.66500 1.000 41.69000  ? 200  ASP B CB  1 
ATOM   5378  C CG  . ASP B 1 181 ? 42.54300  -15.74100 -30.89700 1.000 50.99000  ? 200  ASP B CG  1 
ATOM   5379  O OD1 . ASP B 1 181 ? 43.13700  -15.81900 -31.99500 1.000 46.64000  ? 200  ASP B OD1 1 
ATOM   5380  O OD2 . ASP B 1 181 ? 42.90000  -14.95900 -29.98400 1.000 58.32000  ? 200  ASP B OD2 1 
ATOM   5381  N N   . VAL B 1 182 ? 42.02600  -18.81100 -33.53700 1.000 37.52000  ? 201  VAL B N   1 
ATOM   5382  C CA  . VAL B 1 182 ? 42.90300  -19.85600 -34.04300 1.000 39.32000  ? 201  VAL B CA  1 
ATOM   5383  C C   . VAL B 1 182 ? 44.11200  -19.20400 -34.69100 1.000 39.95000  ? 201  VAL B C   1 
ATOM   5384  O O   . VAL B 1 182 ? 43.97600  -18.25400 -35.47400 1.000 38.73000  ? 201  VAL B O   1 
ATOM   5385  C CB  . VAL B 1 182 ? 42.16000  -20.76800 -35.03600 1.000 39.82000  ? 201  VAL B CB  1 
ATOM   5386  C CG1 . VAL B 1 182 ? 43.13300  -21.70800 -35.72700 1.000 37.70000  ? 201  VAL B CG1 1 
ATOM   5387  C CG2 . VAL B 1 182 ? 41.08900  -21.56800 -34.30300 1.000 41.28000  ? 201  VAL B CG2 1 
ATOM   5388  N N   . GLY B 1 183 ? 45.29600  -19.71100 -34.36100 1.000 35.41000  ? 202  GLY B N   1 
ATOM   5389  C CA  . GLY B 1 183 ? 46.54100  -19.14900 -34.84800 1.000 39.18000  ? 202  GLY B CA  1 
ATOM   5390  C C   . GLY B 1 183 ? 47.23900  -20.00200 -35.89200 1.000 41.97000  ? 202  GLY B C   1 
ATOM   5391  O O   . GLY B 1 183 ? 48.44500  -20.24500 -35.79200 1.000 40.90000  ? 202  GLY B O   1 
ATOM   5392  N N   . VAL B 1 184 ? 46.49000  -20.48700 -36.87800 1.000 44.93000  ? 203  VAL B N   1 
ATOM   5393  C CA  . VAL B 1 184 ? 47.04100  -21.39800 -37.88000 1.000 39.83000  ? 203  VAL B CA  1 
ATOM   5394  C C   . VAL B 1 184 ? 47.60500  -20.65400 -39.08700 1.000 44.22000  ? 203  VAL B C   1 
ATOM   5395  O O   . VAL B 1 184 ? 48.63700  -21.05200 -39.63000 1.000 51.28000  ? 203  VAL B O   1 
ATOM   5396  C CB  . VAL B 1 184 ? 45.97400  -22.43400 -38.29700 1.000 35.29000  ? 203  VAL B CB  1 
ATOM   5397  C CG1 . VAL B 1 184 ? 46.36400  -23.11600 -39.58300 1.000 30.96000  ? 203  VAL B CG1 1 
ATOM   5398  C CG2 . VAL B 1 184 ? 45.83000  -23.49000 -37.21700 1.000 30.35000  ? 203  VAL B CG2 1 
ATOM   5399  N N   . ASP B 1 185 ? 46.98800  -19.56300 -39.54400 1.000 36.90000  ? 204  ASP B N   1 
ATOM   5400  C CA  . ASP B 1 185 ? 47.49400  -18.87100 -40.72500 1.000 38.20000  ? 204  ASP B CA  1 
ATOM   5401  C C   . ASP B 1 185 ? 48.08000  -17.49700 -40.41300 1.000 41.77000  ? 204  ASP B C   1 
ATOM   5402  O O   . ASP B 1 185 ? 48.01900  -16.59000 -41.24700 1.000 48.47000  ? 204  ASP B O   1 
ATOM   5403  C CB  . ASP B 1 185 ? 46.41800  -18.72500 -41.80000 1.000 46.38000  ? 204  ASP B CB  1 
ATOM   5404  C CG  . ASP B 1 185 ? 45.29900  -17.78600 -41.39500 1.000 50.14000  ? 204  ASP B CG  1 
ATOM   5405  O OD1 . ASP B 1 185 ? 45.23200  -17.37200 -40.21500 1.000 51.59000  ? 204  ASP B OD1 1 
ATOM   5406  O OD2 . ASP B 1 185 ? 44.49800  -17.43200 -42.28300 1.000 60.93000  ? 204  ASP B OD2 1 
ATOM   5407  N N   . ASN B 1 186 ? 48.66300  -17.32000 -39.24100 1.000 39.06000  ? 205  ASN B N   1 
ATOM   5408  C CA  . ASN B 1 186 ? 49.29600  -16.04500 -38.96000 1.000 36.72000  ? 205  ASN B CA  1 
ATOM   5409  C C   . ASN B 1 186 ? 50.73400  -16.06600 -39.48800 1.000 44.31000  ? 205  ASN B C   1 
ATOM   5410  O O   . ASN B 1 186 ? 51.24300  -17.10000 -39.92800 1.000 41.66000  ? 205  ASN B O   1 
ATOM   5411  C CB  . ASN B 1 186 ? 49.19500  -15.74700 -37.46400 1.000 35.22000  ? 205  ASN B CB  1 
ATOM   5412  C CG  . ASN B 1 186 ? 49.94100  -16.76000 -36.59400 1.000 45.66000  ? 205  ASN B CG  1 
ATOM   5413  O OD1 . ASN B 1 186 ? 50.93000  -17.37100 -37.01300 1.000 43.89000  ? 205  ASN B OD1 1 
ATOM   5414  N ND2 . ASN B 1 186 ? 49.40400  -17.00600 -35.40100 1.000 38.79000  ? 205  ASN B ND2 1 
ATOM   5415  N N   . ALA B 1 187 ? 51.38600  -14.90100 -39.45200 1.000 40.29000  ? 206  ALA B N   1 
ATOM   5416  C CA  . ALA B 1 187 ? 52.69800  -14.77200 -40.07700 1.000 41.23000  ? 206  ALA B CA  1 
ATOM   5417  C C   . ALA B 1 187 ? 53.71400  -15.72500 -39.45100 1.000 45.96000  ? 206  ALA B C   1 
ATOM   5418  O O   . ALA B 1 187 ? 54.58400  -16.26300 -40.14800 1.000 39.92000  ? 206  ALA B O   1 
ATOM   5419  C CB  . ALA B 1 187 ? 53.18300  -13.32700 -39.97500 1.000 42.13000  ? 206  ALA B CB  1 
ATOM   5420  N N   . GLY B 1 188 ? 53.62200  -15.94200 -38.13700 1.000 41.11000  ? 207  GLY B N   1 
ATOM   5421  C CA  . GLY B 1 188 ? 54.52800  -16.87900 -37.49100 1.000 35.70000  ? 207  GLY B CA  1 
ATOM   5422  C C   . GLY B 1 188 ? 54.38000  -18.29000 -38.02700 1.000 36.71000  ? 207  GLY B C   1 
ATOM   5423  O O   . GLY B 1 188 ? 55.36600  -18.95300 -38.35500 1.000 44.11000  ? 207  GLY B O   1 
ATOM   5424  N N   . ALA B 1 189 ? 53.14200  -18.76500 -38.13900 1.000 38.80000  ? 208  ALA B N   1 
ATOM   5425  C CA  . ALA B 1 189 ? 52.91500  -20.11300 -38.65300 1.000 36.91000  ? 208  ALA B CA  1 
ATOM   5426  C C   . ALA B 1 189 ? 53.38000  -20.23400 -40.09400 1.000 38.30000  ? 208  ALA B C   1 
ATOM   5427  O O   . ALA B 1 189 ? 53.90400  -21.27900 -40.50100 1.000 41.59000  ? 208  ALA B O   1 
ATOM   5428  C CB  . ALA B 1 189 ? 51.43800  -20.47900 -38.53600 1.000 37.56000  ? 208  ALA B CB  1 
ATOM   5429  N N   . LYS B 1 190 ? 53.19500  -19.17700 -40.88300 1.000 36.52000  ? 209  LYS B N   1 
ATOM   5430  C CA  . LYS B 1 190 ? 53.67400  -19.19400 -42.26000 1.000 39.33000  ? 209  LYS B CA  1 
ATOM   5431  C C   . LYS B 1 190 ? 55.19800  -19.22400 -42.30600 1.000 39.67000  ? 209  LYS B C   1 
ATOM   5432  O O   . LYS B 1 190 ? 55.79300  -20.02600 -43.03500 1.000 41.39000  ? 209  LYS B O   1 
ATOM   5433  C CB  . LYS B 1 190 ? 53.12000  -17.98700 -43.01100 1.000 38.93000  ? 209  LYS B CB  1 
ATOM   5434  C CG  . LYS B 1 190 ? 51.59200  -18.00400 -43.13600 1.000 40.34000  ? 209  LYS B CG  1 
ATOM   5435  C CD  . LYS B 1 190 ? 51.09600  -16.80400 -43.91300 1.000 39.00000  ? 209  LYS B CD  1 
ATOM   5436  C CE  . LYS B 1 190 ? 49.57700  -16.78900 -44.01500 1.000 49.29000  ? 209  LYS B CE  1 
ATOM   5437  N NZ  . LYS B 1 190 ? 49.12600  -15.63600 -44.84800 1.000 48.85000  ? 209  LYS B NZ  1 
ATOM   5438  N N   . ALA B 1 191 ? 55.85100  -18.38300 -41.50600 1.000 33.51000  ? 210  ALA B N   1 
ATOM   5439  C CA  . ALA B 1 191 ? 57.31200  -18.39100 -41.46400 1.000 44.13000  ? 210  ALA B CA  1 
ATOM   5440  C C   . ALA B 1 191 ? 57.84600  -19.78000 -41.12900 1.000 43.04000  ? 210  ALA B C   1 
ATOM   5441  O O   . ALA B 1 191 ? 58.72700  -20.30300 -41.82200 1.000 40.33000  ? 210  ALA B O   1 
ATOM   5442  C CB  . ALA B 1 191 ? 57.82100  -17.36400 -40.44900 1.000 39.01000  ? 210  ALA B CB  1 
ATOM   5443  N N   . GLY B 1 192 ? 57.31000  -20.40200 -40.07600 1.000 41.84000  ? 211  GLY B N   1 
ATOM   5444  C CA  . GLY B 1 192 ? 57.82000  -21.70100 -39.66300 1.000 36.01000  ? 211  GLY B CA  1 
ATOM   5445  C C   . GLY B 1 192 ? 57.59200  -22.78200 -40.70400 1.000 38.84000  ? 211  GLY B C   1 
ATOM   5446  O O   . GLY B 1 192 ? 58.48800  -23.58000 -40.99200 1.000 33.97000  ? 211  GLY B O   1 
ATOM   5447  N N   . LEU B 1 193 ? 56.38100  -22.83800 -41.26600 1.000 35.34000  ? 212  LEU B N   1 
ATOM   5448  C CA  . LEU B 1 193 ? 56.09400  -23.84800 -42.27400 1.000 32.52000  ? 212  LEU B CA  1 
ATOM   5449  C C   . LEU B 1 193 ? 56.86300  -23.57100 -43.55200 1.000 37.04000  ? 212  LEU B C   1 
ATOM   5450  O O   . LEU B 1 193 ? 57.31500  -24.50500 -44.22500 1.000 36.72000  ? 212  LEU B O   1 
ATOM   5451  C CB  . LEU B 1 193 ? 54.59800  -23.90800 -42.55600 1.000 34.12000  ? 212  LEU B CB  1 
ATOM   5452  C CG  . LEU B 1 193 ? 54.14900  -24.95800 -43.56800 1.000 38.54000  ? 212  LEU B CG  1 
ATOM   5453  C CD1 . LEU B 1 193 ? 54.56700  -26.34900 -43.10300 1.000 30.87000  ? 212  LEU B CD1 1 
ATOM   5454  C CD2 . LEU B 1 193 ? 52.63800  -24.86200 -43.74500 1.000 38.35000  ? 212  LEU B CD2 1 
ATOM   5455  N N   . THR B 1 194 ? 57.01500  -22.29300 -43.90700 1.000 34.97000  ? 213  THR B N   1 
ATOM   5456  C CA  . THR B 1 194 ? 57.89200  -21.94500 -45.01600 1.000 34.40000  ? 213  THR B CA  1 
ATOM   5457  C C   . THR B 1 194 ? 59.27100  -22.54600 -44.82800 1.000 40.21000  ? 213  THR B C   1 
ATOM   5458  O O   . THR B 1 194 ? 59.85200  -23.09800 -45.77200 1.000 37.96000  ? 213  THR B O   1 
ATOM   5459  C CB  . THR B 1 194 ? 57.99400  -20.42800 -45.16700 1.000 36.93000  ? 213  THR B CB  1 
ATOM   5460  O OG1 . THR B 1 194 ? 56.76700  -19.91500 -45.69100 1.000 45.00000  ? 213  THR B OG1 1 
ATOM   5461  C CG2 . THR B 1 194 ? 59.14500  -20.03900 -46.08300 1.000 39.88000  ? 213  THR B CG2 1 
ATOM   5462  N N   . PHE B 1 195 ? 59.79500  -22.45000 -43.61300 1.000 34.79000  ? 214  PHE B N   1 
ATOM   5463  C CA  . PHE B 1 195 ? 61.12900  -23.02500 -43.34400 1.000 37.88000  ? 214  PHE B CA  1 
ATOM   5464  C C   . PHE B 1 195 ? 61.07300  -24.54800 -43.46200 1.000 34.76000  ? 214  PHE B C   1 
ATOM   5465  O O   . PHE B 1 195 ? 62.03800  -25.13300 -43.89500 1.000 35.48000  ? 214  PHE B O   1 
ATOM   5466  C CB  . PHE B 1 195 ? 61.69700  -22.54400 -42.01300 1.000 38.68000  ? 214  PHE B CB  1 
ATOM   5467  C CG  . PHE B 1 195 ? 63.09900  -23.03100 -41.79100 1.000 37.28000  ? 214  PHE B CG  1 
ATOM   5468  C CD1 . PHE B 1 195 ? 63.33500  -24.32800 -41.38600 1.000 38.76000  ? 214  PHE B CD1 1 
ATOM   5469  C CD2 . PHE B 1 195 ? 64.17500  -22.21000 -42.03100 1.000 33.41000  ? 214  PHE B CD2 1 
ATOM   5470  C CE1 . PHE B 1 195 ? 64.62300  -24.79200 -41.21200 1.000 37.31000  ? 214  PHE B CE1 1 
ATOM   5471  C CE2 . PHE B 1 195 ? 65.46200  -22.67400 -41.84600 1.000 42.46000  ? 214  PHE B CE2 1 
ATOM   5472  C CZ  . PHE B 1 195 ? 65.68200  -23.96100 -41.43800 1.000 36.96000  ? 214  PHE B CZ  1 
ATOM   5473  N N   . LEU B 1 196 ? 59.96700  -25.16000 -43.06700 1.000 32.65000  ? 215  LEU B N   1 
ATOM   5474  C CA  . LEU B 1 196 ? 59.86200  -26.60200 -43.22800 1.000 31.28000  ? 215  LEU B CA  1 
ATOM   5475  C C   . LEU B 1 196 ? 59.87800  -27.00400 -44.70300 1.000 38.06000  ? 215  LEU B C   1 
ATOM   5476  O O   . LEU B 1 196 ? 60.59600  -27.94000 -45.08600 1.000 38.45000  ? 215  LEU B O   1 
ATOM   5477  C CB  . LEU B 1 196 ? 58.60500  -27.12100 -42.54700 1.000 34.36000  ? 215  LEU B CB  1 
ATOM   5478  C CG  . LEU B 1 196 ? 58.55800  -28.63900 -42.59500 1.000 33.92000  ? 215  LEU B CG  1 
ATOM   5479  C CD1 . LEU B 1 196 ? 59.78500  -29.14300 -41.87200 1.000 39.45000  ? 215  LEU B CD1 1 
ATOM   5480  C CD2 . LEU B 1 196 ? 57.31100  -29.16100 -41.92500 1.000 42.35000  ? 215  LEU B CD2 1 
ATOM   5481  N N   . VAL B 1 197 ? 59.11100  -26.31000 -45.55300 1.000 32.84000  ? 216  VAL B N   1 
ATOM   5482  C CA  . VAL B 1 197 ? 58.99000  -26.75400 -46.94000 1.000 37.35000  ? 216  VAL B CA  1 
ATOM   5483  C C   . VAL B 1 197 ? 60.30100  -26.53000 -47.68600 1.000 41.25000  ? 216  VAL B C   1 
ATOM   5484  O O   . VAL B 1 197 ? 60.67700  -27.32400 -48.55400 1.000 37.92000  ? 216  VAL B O   1 
ATOM   5485  C CB  . VAL B 1 197 ? 57.80600  -26.07000 -47.65300 1.000 42.07000  ? 216  VAL B CB  1 
ATOM   5486  C CG1 . VAL B 1 197 ? 56.50100  -26.33500 -46.91600 1.000 40.09000  ? 216  VAL B CG1 1 
ATOM   5487  C CG2 . VAL B 1 197 ? 58.05200  -24.57600 -47.84900 1.000 46.75000  ? 216  VAL B CG2 1 
ATOM   5488  N N   . ASP B 1 198 ? 61.01400  -25.44800 -47.36700 1.000 42.19000  ? 217  ASP B N   1 
ATOM   5489  C CA  . ASP B 1 198 ? 62.29100  -25.20800 -48.01900 1.000 37.49000  ? 217  ASP B CA  1 
ATOM   5490  C C   . ASP B 1 198 ? 63.30500  -26.28300 -47.65900 1.000 39.91000  ? 217  ASP B C   1 
ATOM   5491  O O   . ASP B 1 198 ? 64.12300  -26.67200 -48.49800 1.000 42.44000  ? 217  ASP B O   1 
ATOM   5492  C CB  . ASP B 1 198 ? 62.81900  -23.82100 -47.67200 1.000 34.73000  ? 217  ASP B CB  1 
ATOM   5493  C CG  . ASP B 1 198 ? 61.97300  -22.72100 -48.26900 1.000 50.58000  ? 217  ASP B CG  1 
ATOM   5494  O OD1 . ASP B 1 198 ? 61.12300  -23.03300 -49.13100 1.000 53.99000  ? 217  ASP B OD1 1 
ATOM   5495  O OD2 . ASP B 1 198 ? 62.21700  -21.53600 -47.95400 1.000 61.13000  ? 217  ASP B OD2 1 
ATOM   5496  N N   . LEU B 1 199 ? 63.28000  -26.77300 -46.41900 1.000 41.79000  ? 218  LEU B N   1 
ATOM   5497  C CA  . LEU B 1 199 ? 64.14000  -27.90600 -46.08500 1.000 41.25000  ? 218  LEU B CA  1 
ATOM   5498  C C   . LEU B 1 199 ? 63.89200  -29.06300 -47.03800 1.000 38.57000  ? 218  LEU B C   1 
ATOM   5499  O O   . LEU B 1 199 ? 64.82700  -29.76200 -47.43700 1.000 38.63000  ? 218  LEU B O   1 
ATOM   5500  C CB  . LEU B 1 199 ? 63.90800  -28.36200 -44.64200 1.000 33.83000  ? 218  LEU B CB  1 
ATOM   5501  C CG  . LEU B 1 199 ? 64.41200  -27.48400 -43.50400 1.000 38.28000  ? 218  LEU B CG  1 
ATOM   5502  C CD1 . LEU B 1 199 ? 63.98400  -28.06300 -42.16600 1.000 30.89000  ? 218  LEU B CD1 1 
ATOM   5503  C CD2 . LEU B 1 199 ? 65.92600  -27.36500 -43.58500 1.000 43.31000  ? 218  LEU B CD2 1 
ATOM   5504  N N   . ILE B 1 200 ? 62.62900  -29.27500 -47.41100 1.000 39.45000  ? 219  ILE B N   1 
ATOM   5505  C CA  . ILE B 1 200 ? 62.27500  -30.37300 -48.30000 1.000 41.72000  ? 219  ILE B CA  1 
ATOM   5506  C C   . ILE B 1 200 ? 62.67200  -30.06200 -49.73800 1.000 40.86000  ? 219  ILE B C   1 
ATOM   5507  O O   . ILE B 1 200 ? 63.17700  -30.93400 -50.45600 1.000 42.04000  ? 219  ILE B O   1 
ATOM   5508  C CB  . ILE B 1 200 ? 60.77400  -30.68000 -48.16700 1.000 44.22000  ? 219  ILE B CB  1 
ATOM   5509  C CG1 . ILE B 1 200 ? 60.46800  -31.16800 -46.75200 1.000 40.01000  ? 219  ILE B CG1 1 
ATOM   5510  C CG2 . ILE B 1 200 ? 60.32700  -31.69900 -49.21000 1.000 38.12000  ? 219  ILE B CG2 1 
ATOM   5511  C CD1 . ILE B 1 200 ? 58.99700  -31.26400 -46.46100 1.000 44.25000  ? 219  ILE B CD1 1 
ATOM   5512  N N   . LYS B 1 201 ? 62.45400  -28.82300 -50.18300 1.000 35.47000  ? 220  LYS B N   1 
ATOM   5513  C CA  . LYS B 1 201 ? 62.82400  -28.46600 -51.54600 1.000 39.61000  ? 220  LYS B CA  1 
ATOM   5514  C C   . LYS B 1 201 ? 64.33000  -28.57800 -51.74600 1.000 44.50000  ? 220  LYS B C   1 
ATOM   5515  O O   . LYS B 1 201 ? 64.79100  -29.06400 -52.78500 1.000 55.29000  ? 220  LYS B O   1 
ATOM   5516  C CB  . LYS B 1 201 ? 62.34100  -27.05400 -51.87300 1.000 34.97000  ? 220  LYS B CB  1 
ATOM   5517  C CG  . LYS B 1 201 ? 60.83500  -26.91900 -51.94400 1.000 43.57000  ? 220  LYS B CG  1 
ATOM   5518  C CD  . LYS B 1 201 ? 60.45400  -25.47700 -52.21400 1.000 46.69000  ? 220  LYS B CD  1 
ATOM   5519  C CE  . LYS B 1 201 ? 58.96000  -25.30600 -52.33400 1.000 51.31000  ? 220  LYS B CE  1 
ATOM   5520  N NZ  . LYS B 1 201 ? 58.62800  -23.87200 -52.57200 1.000 63.24000  ? 220  LYS B NZ  1 
ATOM   5521  N N   . ASN B 1 202 ? 65.11100  -28.14800 -50.76000 1.000 39.19000  ? 221  ASN B N   1 
ATOM   5522  C CA  . ASN B 1 202 ? 66.56300  -28.22500 -50.83700 1.000 44.51000  ? 221  ASN B CA  1 
ATOM   5523  C C   . ASN B 1 202 ? 67.11200  -29.61500 -50.50400 1.000 43.37000  ? 221  ASN B C   1 
ATOM   5524  O O   . ASN B 1 202 ? 68.33000  -29.75900 -50.33300 1.000 42.38000  ? 221  ASN B O   1 
ATOM   5525  C CB  . ASN B 1 202 ? 67.18300  -27.18200 -49.91000 1.000 46.49000  ? 221  ASN B CB  1 
ATOM   5526  C CG  . ASN B 1 202 ? 66.80100  -25.77300 -50.30200 1.000 50.44000  ? 221  ASN B CG  1 
ATOM   5527  O OD1 . ASN B 1 202 ? 66.64300  -25.46200 -51.48600 1.000 53.69000  ? 221  ASN B OD1 1 
ATOM   5528  N ND2 . ASN B 1 202 ? 66.67300  -24.90300 -49.31000 1.000 51.09000  ? 221  ASN B ND2 1 
ATOM   5529  N N   . LYS B 1 203 ? 66.24100  -30.62100 -50.39400 1.000 43.31000  ? 222  LYS B N   1 
ATOM   5530  C CA  . LYS B 1 203 ? 66.58800  -32.03800 -50.29100 1.000 41.75000  ? 222  LYS B CA  1 
ATOM   5531  C C   . LYS B 1 203 ? 67.16700  -32.42500 -48.93800 1.000 42.86000  ? 222  LYS B C   1 
ATOM   5532  O O   . LYS B 1 203 ? 67.67800  -33.54400 -48.79300 1.000 43.67000  ? 222  LYS B O   1 
ATOM   5533  C CB  . LYS B 1 203 ? 67.56800  -32.46400 -51.38900 1.000 38.70000  ? 222  LYS B CB  1 
ATOM   5534  C CG  . LYS B 1 203 ? 67.03800  -32.34800 -52.81300 1.000 55.07000  ? 222  LYS B CG  1 
ATOM   5535  C CD  . LYS B 1 203 ? 66.01200  -33.43100 -53.09100 1.000 54.85000  ? 222  LYS B CD  1 
ATOM   5536  C CE  . LYS B 1 203 ? 65.67200  -33.51400 -54.56700 1.000 58.66000  ? 222  LYS B CE  1 
ATOM   5537  N NZ  . LYS B 1 203 ? 64.67900  -34.60100 -54.82800 1.000 68.44000  ? 222  LYS B NZ  1 
ATOM   5538  N N   . HIS B 1 204 ? 67.10500  -31.54100 -47.93700 1.000 44.87000  ? 223  HIS B N   1 
ATOM   5539  C CA  . HIS B 1 204 ? 67.56700  -31.92600 -46.60400 1.000 43.10000  ? 223  HIS B CA  1 
ATOM   5540  C C   . HIS B 1 204 ? 66.59500  -32.86700 -45.91900 1.000 38.75000  ? 223  HIS B C   1 
ATOM   5541  O O   . HIS B 1 204 ? 67.01200  -33.64100 -45.04900 1.000 46.93000  ? 223  HIS B O   1 
ATOM   5542  C CB  . HIS B 1 204 ? 67.81400  -30.68700 -45.74300 1.000 37.65000  ? 223  HIS B CB  1 
ATOM   5543  C CG  . HIS B 1 204 ? 68.68600  -29.66900 -46.40100 1.000 39.18000  ? 223  HIS B CG  1 
ATOM   5544  N ND1 . HIS B 1 204 ? 70.00400  -29.91200 -46.72600 1.000 38.91000  ? 223  HIS B ND1 1 
ATOM   5545  C CD2 . HIS B 1 204 ? 68.43000  -28.39700 -46.78700 1.000 37.45000  ? 223  HIS B CD2 1 
ATOM   5546  C CE1 . HIS B 1 204 ? 70.51900  -28.83600 -47.29600 1.000 42.49000  ? 223  HIS B CE1 1 
ATOM   5547  N NE2 . HIS B 1 204 ? 69.58500  -27.90200 -47.34500 1.000 40.52000  ? 223  HIS B NE2 1 
ATOM   5548  N N   . MET B 1 205 ? 65.31500  -32.84000 -46.30200 1.000 40.21000  ? 224  MET B N   1 
ATOM   5549  C CA  . MET B 1 205 ? 64.35500  -33.83700 -45.85400 1.000 43.33000  ? 224  MET B CA  1 
ATOM   5550  C C   . MET B 1 205 ? 63.41600  -34.20700 -46.99200 1.000 44.47000  ? 224  MET B C   1 
ATOM   5551  O O   . MET B 1 205 ? 63.14400  -33.39400 -47.89100 1.000 43.59000  ? 224  MET B O   1 
ATOM   5552  C CB  . MET B 1 205 ? 63.53100  -33.33700 -44.65300 1.000 44.98000  ? 224  MET B CB  1 
ATOM   5553  C CG  . MET B 1 205 ? 64.32800  -33.02400 -43.39600 1.000 42.04000  ? 224  MET B CG  1 
ATOM   5554  S SD  . MET B 1 205 ? 63.21600  -32.75000 -41.99700 1.000 42.23000  ? 224  MET B SD  1 
ATOM   5555  C CE  . MET B 1 205 ? 62.43800  -31.23500 -42.53000 1.000 32.20000  ? 224  MET B CE  1 
ATOM   5556  N N   . ASN B 1 206 ? 62.91200  -35.44900 -46.92700 1.000 45.21000  ? 225  ASN B N   1 
ATOM   5557  C CA  . ASN B 1 206 ? 61.89900  -36.00600 -47.82700 1.000 42.52000  ? 225  ASN B CA  1 
ATOM   5558  C C   . ASN B 1 206 ? 60.50600  -35.80900 -47.24000 1.000 51.35000  ? 225  ASN B C   1 
ATOM   5559  O O   . ASN B 1 206 ? 60.26600  -36.20000 -46.09000 1.000 51.10000  ? 225  ASN B O   1 
ATOM   5560  C CB  . ASN B 1 206 ? 62.06100  -37.51200 -48.00400 1.000 51.56000  ? 225  ASN B CB  1 
ATOM   5561  C CG  . ASN B 1 206 ? 61.18100  -38.04300 -49.13700 1.000 67.29000  ? 225  ASN B CG  1 
ATOM   5562  O OD1 . ASN B 1 206 ? 60.71700  -39.21100 -49.09700 1.000 68.23000  ? 225  ASN B OD1 1 
ATOM   5563  N ND2 . ASN B 1 206 ? 61.09600  -37.28300 -50.22400 1.000 67.24000  ? 225  ASN B ND2 1 
ATOM   5564  N N   . ALA B 1 207 ? 59.56600  -35.30100 -48.04800 1.000 53.78000  ? 226  ALA B N   1 
ATOM   5565  C CA  . ALA B 1 207 ? 58.23200  -35.06000 -47.53100 1.000 46.71000  ? 226  ALA B CA  1 
ATOM   5566  C C   . ALA B 1 207 ? 57.45000  -36.34000 -47.23400 1.000 49.58000  ? 226  ALA B C   1 
ATOM   5567  O O   . ALA B 1 207 ? 56.39900  -36.27700 -46.57600 1.000 43.73000  ? 226  ALA B O   1 
ATOM   5568  C CB  . ALA B 1 207 ? 57.43300  -34.22500 -48.55300 1.000 43.32000  ? 226  ALA B CB  1 
ATOM   5569  N N   . ASP B 1 208 ? 57.92200  -37.49000 -47.68900 1.000 46.10000  ? 227  ASP B N   1 
ATOM   5570  C CA  . ASP B 1 208 ? 57.25900  -38.76400 -47.45800 1.000 49.64000  ? 227  ASP B CA  1 
ATOM   5571  C C   . ASP B 1 208 ? 57.69700  -39.44600 -46.17400 1.000 45.86000  ? 227  ASP B C   1 
ATOM   5572  O O   . ASP B 1 208 ? 57.14000  -40.48500 -45.80200 1.000 41.31000  ? 227  ASP B O   1 
ATOM   5573  C CB  . ASP B 1 208 ? 57.51400  -39.69900 -48.65600 1.000 54.36000  ? 227  ASP B CB  1 
ATOM   5574  C CG  . ASP B 1 208 ? 56.67300  -39.31700 -49.86700 1.000 70.93000  ? 227  ASP B CG  1 
ATOM   5575  O OD1 . ASP B 1 208 ? 55.45200  -39.08000 -49.68800 1.000 72.04000  ? 227  ASP B OD1 1 
ATOM   5576  O OD2 . ASP B 1 208 ? 57.25600  -39.18500 -50.96500 1.000 76.27000  ? 227  ASP B OD2 1 
ATOM   5577  N N   . THR B 1 209 ? 58.66700  -38.87600 -45.46900 1.000 43.41000  ? 228  THR B N   1 
ATOM   5578  C CA  . THR B 1 209 ? 59.19100  -39.51400 -44.26600 1.000 38.88000  ? 228  THR B CA  1 
ATOM   5579  C C   . THR B 1 209 ? 58.13700  -39.56300 -43.17200 1.000 39.63000  ? 228  THR B C   1 
ATOM   5580  O O   . THR B 1 209 ? 57.53600  -38.53300 -42.82300 1.000 38.82000  ? 228  THR B O   1 
ATOM   5581  C CB  . THR B 1 209 ? 60.40100  -38.74000 -43.75100 1.000 36.91000  ? 228  THR B CB  1 
ATOM   5582  O OG1 . THR B 1 209 ? 61.40700  -38.70900 -44.78100 1.000 48.98000  ? 228  THR B OG1 1 
ATOM   5583  C CG2 . THR B 1 209 ? 60.95700  -39.43900 -42.54400 1.000 37.50000  ? 228  THR B CG2 1 
ATOM   5584  N N   . ASP B 1 210 ? 57.92000  -40.74600 -42.61500 1.000 36.14000  ? 229  ASP B N   1 
ATOM   5585  C CA  . ASP B 1 210 ? 56.91100  -40.94900 -41.57800 1.000 40.98000  ? 229  ASP B CA  1 
ATOM   5586  C C   . ASP B 1 210 ? 57.59100  -41.43200 -40.29600 1.000 43.60000  ? 229  ASP B C   1 
ATOM   5587  O O   . ASP B 1 210 ? 58.81800  -41.39800 -40.16700 1.000 40.53000  ? 229  ASP B O   1 
ATOM   5588  C CB  . ASP B 1 210 ? 55.80900  -41.90800 -42.05800 1.000 47.21000  ? 229  ASP B CB  1 
ATOM   5589  C CG  . ASP B 1 210 ? 56.29200  -43.34100 -42.25100 1.000 53.81000  ? 229  ASP B CG  1 
ATOM   5590  O OD1 . ASP B 1 210 ? 57.45900  -43.65800 -41.93400 1.000 51.78000  ? 229  ASP B OD1 1 
ATOM   5591  O OD2 . ASP B 1 210 ? 55.48700  -44.15200 -42.77000 1.000 52.85000  ? 229  ASP B OD2 1 
ATOM   5592  N N   . TYR B 1 211 ? 56.78900  -41.81200 -39.31800 1.000 40.14000  ? 230  TYR B N   1 
ATOM   5593  C CA  . TYR B 1 211 ? 57.35400  -42.19300 -38.00700 1.000 40.46000  ? 230  TYR B CA  1 
ATOM   5594  C C   . TYR B 1 211 ? 58.22800  -43.44900 -38.09300 1.000 45.72000  ? 230  TYR B C   1 
ATOM   5595  O O   . TYR B 1 211 ? 59.29200  -43.46000 -37.51000 1.000 41.86000  ? 230  TYR B O   1 
ATOM   5596  C CB  . TYR B 1 211 ? 56.23500  -42.28100 -36.97600 1.000 34.73000  ? 230  TYR B CB  1 
ATOM   5597  C CG  . TYR B 1 211 ? 56.69400  -42.60600 -35.58800 1.000 32.77000  ? 230  TYR B CG  1 
ATOM   5598  C CD1 . TYR B 1 211 ? 57.20400  -43.85000 -35.29600 1.000 38.27000  ? 230  TYR B CD1 1 
ATOM   5599  C CD2 . TYR B 1 211 ? 56.63800  -41.66900 -34.57800 1.000 33.82000  ? 230  TYR B CD2 1 
ATOM   5600  C CE1 . TYR B 1 211 ? 57.63400  -44.16600 -34.02800 1.000 38.95000  ? 230  TYR B CE1 1 
ATOM   5601  C CE2 . TYR B 1 211 ? 57.06300  -41.96900 -33.30100 1.000 37.09000  ? 230  TYR B CE2 1 
ATOM   5602  C CZ  . TYR B 1 211 ? 57.56200  -43.22200 -33.02900 1.000 36.42000  ? 230  TYR B CZ  1 
ATOM   5603  O OH  . TYR B 1 211 ? 57.99100  -43.54600 -31.78700 1.000 45.51000  ? 230  TYR B OH  1 
ATOM   5604  N N   . SER B 1 212 ? 57.79300  -44.48700 -38.79000 1.000 43.81000  ? 231  SER B N   1 
ATOM   5605  C CA  . SER B 1 212 ? 58.63800  -45.67900 -38.80700 1.000 47.12000  ? 231  SER B CA  1 
ATOM   5606  C C   . SER B 1 212 ? 59.91400  -45.46300 -39.63100 1.000 41.47000  ? 231  SER B C   1 
ATOM   5607  O O   . SER B 1 212 ? 60.96200  -46.03500 -39.30300 1.000 45.16000  ? 231  SER B O   1 
ATOM   5608  C CB  . SER B 1 212 ? 57.86400  -46.89100 -39.32800 1.000 38.48000  ? 231  SER B CB  1 
ATOM   5609  O OG  . SER B 1 212 ? 57.73400  -46.83300 -40.73000 1.000 62.86000  ? 231  SER B OG  1 
ATOM   5610  N N   . ILE B 1 213 ? 59.85400  -44.65000 -40.69300 1.000 41.20000  ? 232  ILE B N   1 
ATOM   5611  C CA  . ILE B 1 213 ? 61.03800  -44.39900 -41.51600 1.000 37.10000  ? 232  ILE B CA  1 
ATOM   5612  C C   . ILE B 1 213 ? 62.09200  -43.62600 -40.73300 1.000 40.84000  ? 232  ILE B C   1 
ATOM   5613  O O   . ILE B 1 213 ? 63.26900  -44.01000 -40.69800 1.000 40.74000  ? 232  ILE B O   1 
ATOM   5614  C CB  . ILE B 1 213 ? 60.65800  -43.65400 -42.80900 1.000 42.93000  ? 232  ILE B CB  1 
ATOM   5615  C CG1 . ILE B 1 213 ? 59.80800  -44.53400 -43.72600 1.000 45.51000  ? 232  ILE B CG1 1 
ATOM   5616  C CG2 . ILE B 1 213 ? 61.90800  -43.15200 -43.54300 1.000 34.24000  ? 232  ILE B CG2 1 
ATOM   5617  C CD1 . ILE B 1 213 ? 59.21000  -43.77300 -44.89200 1.000 41.72000  ? 232  ILE B CD1 1 
ATOM   5618  N N   . ALA B 1 214 ? 61.69200  -42.51300 -40.11100 1.000 42.54000  ? 233  ALA B N   1 
ATOM   5619  C CA  . ALA B 1 214 ? 62.63800  -41.73700 -39.31800 1.000 37.27000  ? 233  ALA B CA  1 
ATOM   5620  C C   . ALA B 1 214 ? 63.20100  -42.56900 -38.18000 1.000 43.55000  ? 233  ALA B C   1 
ATOM   5621  O O   . ALA B 1 214 ? 64.40600  -42.51500 -37.89900 1.000 39.27000  ? 233  ALA B O   1 
ATOM   5622  C CB  . ALA B 1 214 ? 61.97400  -40.47500 -38.77400 1.000 33.74000  ? 233  ALA B CB  1 
ATOM   5623  N N   . GLU B 1 215 ? 62.34700  -43.35900 -37.52100 1.000 40.76000  ? 234  GLU B N   1 
ATOM   5624  C CA  . GLU B 1 215 ? 62.80600  -44.16400 -36.39700 1.000 38.71000  ? 234  GLU B CA  1 
ATOM   5625  C C   . GLU B 1 215 ? 63.87300  -45.15900 -36.83900 1.000 38.61000  ? 234  GLU B C   1 
ATOM   5626  O O   . GLU B 1 215 ? 64.88900  -45.34100 -36.16100 1.000 34.57000  ? 234  GLU B O   1 
ATOM   5627  C CB  . GLU B 1 215 ? 61.64100  -44.91200 -35.76300 1.000 32.21000  ? 234  GLU B CB  1 
ATOM   5628  C CG  . GLU B 1 215 ? 62.01900  -45.45800 -34.41000 1.000 41.12000  ? 234  GLU B CG  1 
ATOM   5629  C CD  . GLU B 1 215 ? 61.03900  -46.45300 -33.86600 1.000 46.92000  ? 234  GLU B CD  1 
ATOM   5630  O OE1 . GLU B 1 215 ? 60.18700  -46.94200 -34.64200 1.000 53.51000  ? 234  GLU B OE1 1 
ATOM   5631  O OE2 . GLU B 1 215 ? 61.10700  -46.71900 -32.64600 1.000 43.69000  ? 234  GLU B OE2 1 
ATOM   5632  N N   . ALA B 1 216 ? 63.64400  -45.82800 -37.97000 1.000 39.42000  ? 235  ALA B N   1 
ATOM   5633  C CA  . ALA B 1 216 ? 64.62700  -46.77400 -38.48500 1.000 43.33000  ? 235  ALA B CA  1 
ATOM   5634  C C   . ALA B 1 216 ? 65.92100  -46.06900 -38.85700 1.000 42.68000  ? 235  ALA B C   1 
ATOM   5635  O O   . ALA B 1 216 ? 67.01600  -46.56900 -38.57200 1.000 38.86000  ? 235  ALA B O   1 
ATOM   5636  C CB  . ALA B 1 216 ? 64.06100  -47.51500 -39.69700 1.000 40.63000  ? 235  ALA B CB  1 
ATOM   5637  N N   . ALA B 1 217 ? 65.81400  -44.90100 -39.49100 1.000 39.69000  ? 236  ALA B N   1 
ATOM   5638  C CA  . ALA B 1 217 ? 67.00400  -44.19700 -39.94600 1.000 40.86000  ? 236  ALA B CA  1 
ATOM   5639  C C   . ALA B 1 217 ? 67.88400  -43.79300 -38.77000 1.000 39.94000  ? 236  ALA B C   1 
ATOM   5640  O O   . ALA B 1 217 ? 69.10400  -43.99100 -38.79700 1.000 37.08000  ? 236  ALA B O   1 
ATOM   5641  C CB  . ALA B 1 217 ? 66.60100  -42.97500 -40.76700 1.000 41.23000  ? 236  ALA B CB  1 
ATOM   5642  N N   . PHE B 1 218 ? 67.28100  -43.23600 -37.71600 1.000 38.01000  ? 237  PHE B N   1 
ATOM   5643  C CA  . PHE B 1 218 ? 68.07100  -42.84800 -36.55500 1.000 37.57000  ? 237  PHE B CA  1 
ATOM   5644  C C   . PHE B 1 218 ? 68.62600  -44.07300 -35.84000 1.000 40.18000  ? 237  PHE B C   1 
ATOM   5645  O O   . PHE B 1 218 ? 69.81800  -44.12300 -35.50500 1.000 38.15000  ? 237  PHE B O   1 
ATOM   5646  C CB  . PHE B 1 218 ? 67.25000  -42.00500 -35.57900 1.000 34.76000  ? 237  PHE B CB  1 
ATOM   5647  C CG  . PHE B 1 218 ? 68.07700  -41.42200 -34.47100 1.000 35.23000  ? 237  PHE B CG  1 
ATOM   5648  C CD1 . PHE B 1 218 ? 68.83800  -40.28100 -34.69200 1.000 35.90000  ? 237  PHE B CD1 1 
ATOM   5649  C CD2 . PHE B 1 218 ? 68.15600  -42.04900 -33.23800 1.000 40.29000  ? 237  PHE B CD2 1 
ATOM   5650  C CE1 . PHE B 1 218 ? 69.63600  -39.74800 -33.68600 1.000 35.81000  ? 237  PHE B CE1 1 
ATOM   5651  C CE2 . PHE B 1 218 ? 68.95200  -41.52500 -32.23100 1.000 35.89000  ? 237  PHE B CE2 1 
ATOM   5652  C CZ  . PHE B 1 218 ? 69.69300  -40.37000 -32.45900 1.000 35.51000  ? 237  PHE B CZ  1 
ATOM   5653  N N   . ASN B 1 219 ? 67.77900  -45.08000 -35.60100 1.000 33.59000  ? 238  ASN B N   1 
ATOM   5654  C CA  . ASN B 1 219 ? 68.24500  -46.21700 -34.82000 1.000 36.38000  ? 238  ASN B CA  1 
ATOM   5655  C C   . ASN B 1 219 ? 69.22200  -47.11400 -35.57900 1.000 36.54000  ? 238  ASN B C   1 
ATOM   5656  O O   . ASN B 1 219 ? 69.76400  -48.04300 -34.97600 1.000 36.91000  ? 238  ASN B O   1 
ATOM   5657  C CB  . ASN B 1 219 ? 67.06100  -47.04200 -34.31000 1.000 35.32000  ? 238  ASN B CB  1 
ATOM   5658  C CG  . ASN B 1 219 ? 66.16700  -46.24800 -33.37300 1.000 38.49000  ? 238  ASN B CG  1 
ATOM   5659  O OD1 . ASN B 1 219 ? 66.58700  -45.23300 -32.82600 1.000 45.48000  ? 238  ASN B OD1 1 
ATOM   5660  N ND2 . ASN B 1 219 ? 64.98200  -46.76400 -33.09700 1.000 37.82000  ? 238  ASN B ND2 1 
ATOM   5661  N N   . LYS B 1 220 ? 69.43700  -46.87800 -36.87500 1.000 41.37000  ? 239  LYS B N   1 
ATOM   5662  C CA  . LYS B 1 220 ? 70.46100  -47.55600 -37.66500 1.000 39.04000  ? 239  LYS B CA  1 
ATOM   5663  C C   . LYS B 1 220 ? 71.70900  -46.70800 -37.86900 1.000 40.90000  ? 239  LYS B C   1 
ATOM   5664  O O   . LYS B 1 220 ? 72.65400  -47.16900 -38.51600 1.000 42.07000  ? 239  LYS B O   1 
ATOM   5665  C CB  . LYS B 1 220 ? 69.91100  -47.94700 -39.04200 1.000 40.76000  ? 239  LYS B CB  1 
ATOM   5666  C CG  . LYS B 1 220 ? 69.02600  -49.18600 -39.15100 1.000 48.83000  ? 239  LYS B CG  1 
ATOM   5667  C CD  . LYS B 1 220 ? 68.43400  -49.18900 -40.57400 1.000 62.61000  ? 239  LYS B CD  1 
ATOM   5668  C CE  . LYS B 1 220 ? 67.60200  -50.41100 -40.94900 1.000 62.87000  ? 239  LYS B CE  1 
ATOM   5669  N NZ  . LYS B 1 220 ? 68.45800  -51.57800 -41.31500 1.000 75.07000  ? 239  LYS B NZ  1 
ATOM   5670  N N   . GLY B 1 221 ? 71.73100  -45.47900 -37.35900 1.000 42.18000  ? 240  GLY B N   1 
ATOM   5671  C CA  . GLY B 1 221 ? 72.89000  -44.62600 -37.52600 1.000 36.29000  ? 240  GLY B CA  1 
ATOM   5672  C C   . GLY B 1 221 ? 72.98800  -43.92300 -38.85700 1.000 39.25000  ? 240  GLY B C   1 
ATOM   5673  O O   . GLY B 1 221 ? 74.08600  -43.50000 -39.24100 1.000 41.62000  ? 240  GLY B O   1 
ATOM   5674  N N   . GLU B 1 222 ? 71.87500  -43.77300 -39.57700 1.000 36.91000  ? 241  GLU B N   1 
ATOM   5675  C CA  . GLU B 1 222 ? 71.89100  -43.18200 -40.91000 1.000 34.22000  ? 241  GLU B CA  1 
ATOM   5676  C C   . GLU B 1 222 ? 71.65200  -41.68000 -40.90500 1.000 36.26000  ? 241  GLU B C   1 
ATOM   5677  O O   . GLU B 1 222 ? 72.00300  -41.00300 -41.87600 1.000 36.44000  ? 241  GLU B O   1 
ATOM   5678  C CB  . GLU B 1 222 ? 70.83700  -43.85800 -41.78400 1.000 37.30000  ? 241  GLU B CB  1 
ATOM   5679  C CG  . GLU B 1 222 ? 71.09300  -45.34100 -41.96000 1.000 44.88000  ? 241  GLU B CG  1 
ATOM   5680  C CD  . GLU B 1 222 ? 70.06700  -46.01800 -42.82600 1.000 46.40000  ? 241  GLU B CD  1 
ATOM   5681  O OE1 . GLU B 1 222 ? 69.10700  -45.33600 -43.24800 1.000 54.80000  ? 241  GLU B OE1 1 
ATOM   5682  O OE2 . GLU B 1 222 ? 70.21200  -47.24000 -43.06900 1.000 46.71000  ? 241  GLU B OE2 1 
ATOM   5683  N N   . THR B 1 223 ? 71.06200  -41.14400 -39.84700 1.000 40.96000  ? 242  THR B N   1 
ATOM   5684  C CA  . THR B 1 223 ? 70.83200  -39.71400 -39.72800 1.000 40.56000  ? 242  THR B CA  1 
ATOM   5685  C C   . THR B 1 223 ? 71.27500  -39.28600 -38.33800 1.000 32.43000  ? 242  THR B C   1 
ATOM   5686  O O   . THR B 1 223 ? 71.25100  -40.07700 -37.39000 1.000 33.61000  ? 242  THR B O   1 
ATOM   5687  C CB  . THR B 1 223 ? 69.33600  -39.34900 -40.00800 1.000 41.13000  ? 242  THR B CB  1 
ATOM   5688  O OG1 . THR B 1 223 ? 69.15800  -37.92500 -40.02000 1.000 36.22000  ? 242  THR B OG1 1 
ATOM   5689  C CG2 . THR B 1 223 ? 68.40600  -39.98600 -38.98600 1.000 37.96000  ? 242  THR B CG2 1 
ATOM   5690  N N   . ALA B 1 224 ? 71.73300  -38.04100 -38.23200 1.000 33.08000  ? 243  ALA B N   1 
ATOM   5691  C CA  . ALA B 1 224 ? 72.31700  -37.59200 -36.97500 1.000 35.73000  ? 243  ALA B CA  1 
ATOM   5692  C C   . ALA B 1 224 ? 71.27300  -37.23000 -35.93200 1.000 37.28000  ? 243  ALA B C   1 
ATOM   5693  O O   . ALA B 1 224 ? 71.58400  -37.25200 -34.73300 1.000 35.73000  ? 243  ALA B O   1 
ATOM   5694  C CB  . ALA B 1 224 ? 73.23700  -36.39000 -37.21300 1.000 32.67000  ? 243  ALA B CB  1 
ATOM   5695  N N   . MET B 1 225 ? 70.05500  -36.89000 -36.35300 1.000 29.78000  ? 244  MET B N   1 
ATOM   5696  C CA  . MET B 1 225 ? 69.06800  -36.34300 -35.43700 1.000 36.07000  ? 244  MET B CA  1 
ATOM   5697  C C   . MET B 1 225 ? 67.68700  -36.87600 -35.78000 1.000 36.75000  ? 244  MET B C   1 
ATOM   5698  O O   . MET B 1 225 ? 67.39900  -37.21800 -36.93100 1.000 33.28000  ? 244  MET B O   1 
ATOM   5699  C CB  . MET B 1 225 ? 69.04400  -34.80700 -35.48700 1.000 34.01000  ? 244  MET B CB  1 
ATOM   5700  C CG  . MET B 1 225 ? 70.34800  -34.15000 -35.10000 1.000 32.26000  ? 244  MET B CG  1 
ATOM   5701  S SD  . MET B 1 225 ? 70.23900  -32.35400 -35.11500 1.000 37.27000  ? 244  MET B SD  1 
ATOM   5702  C CE  . MET B 1 225 ? 70.13500  -32.03100 -36.87500 1.000 34.66000  ? 244  MET B CE  1 
ATOM   5703  N N   . THR B 1 226 ? 66.83600  -36.95000 -34.76100 1.000 35.46000  ? 245  THR B N   1 
ATOM   5704  C CA  . THR B 1 226 ? 65.40100  -37.10300 -34.95500 1.000 30.33000  ? 245  THR B CA  1 
ATOM   5705  C C   . THR B 1 226 ? 64.69400  -36.28000 -33.89100 1.000 35.19000  ? 245  THR B C   1 
ATOM   5706  O O   . THR B 1 226 ? 65.30600  -35.82400 -32.92000 1.000 34.70000  ? 245  THR B O   1 
ATOM   5707  C CB  . THR B 1 226 ? 64.96000  -38.57100 -34.89500 1.000 27.65000  ? 245  THR B CB  1 
ATOM   5708  O OG1 . THR B 1 226 ? 63.58300  -38.67000 -35.27700 1.000 33.95000  ? 245  THR B OG1 1 
ATOM   5709  C CG2 . THR B 1 226 ? 65.11400  -39.12600 -33.49000 1.000 32.22000  ? 245  THR B CG2 1 
ATOM   5710  N N   . ILE B 1 227 ? 63.39800  -36.07300 -34.08500 1.000 32.18000  ? 246  ILE B N   1 
ATOM   5711  C CA  . ILE B 1 227 ? 62.56000  -35.37500 -33.11900 1.000 29.64000  ? 246  ILE B CA  1 
ATOM   5712  C C   . ILE B 1 227 ? 61.54200  -36.37400 -32.61900 1.000 33.07000  ? 246  ILE B C   1 
ATOM   5713  O O   . ILE B 1 227 ? 60.70700  -36.85400 -33.39700 1.000 29.27000  ? 246  ILE B O   1 
ATOM   5714  C CB  . ILE B 1 227 ? 61.87500  -34.14800 -33.73500 1.000 31.08000  ? 246  ILE B CB  1 
ATOM   5715  C CG1 . ILE B 1 227 ? 62.92100  -33.09300 -34.08800 1.000 32.64000  ? 246  ILE B CG1 1 
ATOM   5716  C CG2 . ILE B 1 227 ? 60.81500  -33.59800 -32.79400 1.000 27.80000  ? 246  ILE B CG2 1 
ATOM   5717  C CD1 . ILE B 1 227 ? 62.38200  -31.94500 -34.90100 1.000 32.57000  ? 246  ILE B CD1 1 
ATOM   5718  N N   . ASN B 1 228 ? 61.61200  -36.70600 -31.33500 1.000 28.46000  ? 247  ASN B N   1 
ATOM   5719  C CA  . ASN B 1 228 ? 60.73100  -37.75400 -30.84700 1.000 27.95000  ? 247  ASN B CA  1 
ATOM   5720  C C   . ASN B 1 228 ? 60.63700  -37.63200 -29.33200 1.000 37.24000  ? 247  ASN B C   1 
ATOM   5721  O O   . ASN B 1 228 ? 61.33500  -36.82600 -28.70800 1.000 32.51000  ? 247  ASN B O   1 
ATOM   5722  C CB  . ASN B 1 228 ? 61.23300  -39.11700 -31.34000 1.000 26.20000  ? 247  ASN B CB  1 
ATOM   5723  C CG  . ASN B 1 228 ? 60.13000  -40.13700 -31.45800 1.000 34.41000  ? 247  ASN B CG  1 
ATOM   5724  O OD1 . ASN B 1 228 ? 59.04600  -39.95900 -30.90700 1.000 37.47000  ? 247  ASN B OD1 1 
ATOM   5725  N ND2 . ASN B 1 228 ? 60.36100  -41.16500 -32.27500 1.000 31.78000  ? 247  ASN B ND2 1 
ATOM   5726  N N   . GLY B 1 229 ? 59.72400  -38.40900 -28.75200 1.000 34.26000  ? 248  GLY B N   1 
ATOM   5727  C CA  . GLY B 1 229 ? 59.44100  -38.30400 -27.34500 1.000 31.38000  ? 248  GLY B CA  1 
ATOM   5728  C C   . GLY B 1 229 ? 59.94300  -39.47900 -26.53300 1.000 35.74000  ? 248  GLY B C   1 
ATOM   5729  O O   . GLY B 1 229 ? 60.49100  -40.44900 -27.06900 1.000 39.31000  ? 248  GLY B O   1 
ATOM   5730  N N   . PRO B 1 230 ? 59.72300  -39.42100 -25.21300 1.000 37.03000  ? 249  PRO B N   1 
ATOM   5731  C CA  . PRO B 1 230 ? 60.28400  -40.44800 -24.31500 1.000 36.99000  ? 249  PRO B CA  1 
ATOM   5732  C C   . PRO B 1 230 ? 59.79000  -41.85100 -24.59500 1.000 34.65000  ? 249  PRO B C   1 
ATOM   5733  O O   . PRO B 1 230 ? 60.45000  -42.81600 -24.20000 1.000 38.83000  ? 249  PRO B O   1 
ATOM   5734  C CB  . PRO B 1 230 ? 59.83600  -39.97800 -22.92200 1.000 32.46000  ? 249  PRO B CB  1 
ATOM   5735  C CG  . PRO B 1 230 ? 59.54900  -38.51500 -23.07400 1.000 36.08000  ? 249  PRO B CG  1 
ATOM   5736  C CD  . PRO B 1 230 ? 58.99900  -38.37500 -24.46900 1.000 37.51000  ? 249  PRO B CD  1 
ATOM   5737  N N   . TRP B 1 231 ? 58.64200  -42.00100 -25.24500 1.000 35.42000  ? 250  TRP B N   1 
ATOM   5738  C CA  . TRP B 1 231 ? 58.16700  -43.32500 -25.62700 1.000 39.27000  ? 250  TRP B CA  1 
ATOM   5739  C C   . TRP B 1 231 ? 59.09800  -44.01500 -26.62300 1.000 43.89000  ? 250  TRP B C   1 
ATOM   5740  O O   . TRP B 1 231 ? 58.96900  -45.22800 -26.83900 1.000 37.65000  ? 250  TRP B O   1 
ATOM   5741  C CB  . TRP B 1 231 ? 56.77000  -43.20200 -26.23300 1.000 35.71000  ? 250  TRP B CB  1 
ATOM   5742  C CG  . TRP B 1 231 ? 56.76200  -42.24700 -27.38000 1.000 36.11000  ? 250  TRP B CG  1 
ATOM   5743  C CD1 . TRP B 1 231 ? 57.10300  -42.51800 -28.67200 1.000 36.44000  ? 250  TRP B CD1 1 
ATOM   5744  C CD2 . TRP B 1 231 ? 56.39200  -40.86200 -27.34400 1.000 36.38000  ? 250  TRP B CD2 1 
ATOM   5745  N NE1 . TRP B 1 231 ? 56.97200  -41.38700 -29.44400 1.000 38.33000  ? 250  TRP B NE1 1 
ATOM   5746  C CE2 . TRP B 1 231 ? 56.53700  -40.35700 -28.65000 1.000 39.49000  ? 250  TRP B CE2 1 
ATOM   5747  C CE3 . TRP B 1 231 ? 55.95700  -40.00200 -26.33600 1.000 35.16000  ? 250  TRP B CE3 1 
ATOM   5748  C CZ2 . TRP B 1 231 ? 56.25500  -39.03000 -28.97000 1.000 38.18000  ? 250  TRP B CZ2 1 
ATOM   5749  C CZ3 . TRP B 1 231 ? 55.68300  -38.68700 -26.65500 1.000 31.46000  ? 250  TRP B CZ3 1 
ATOM   5750  C CH2 . TRP B 1 231 ? 55.83000  -38.21400 -27.95700 1.000 34.17000  ? 250  TRP B CH2 1 
ATOM   5751  N N   . ALA B 1 232 ? 60.00600  -43.26900 -27.25900 1.000 40.93000  ? 251  ALA B N   1 
ATOM   5752  C CA  . ALA B 1 232 ? 60.89200  -43.82300 -28.27100 1.000 36.46000  ? 251  ALA B CA  1 
ATOM   5753  C C   . ALA B 1 232 ? 62.26600  -44.20300 -27.73300 1.000 44.89000  ? 251  ALA B C   1 
ATOM   5754  O O   . ALA B 1 232 ? 63.06200  -44.80000 -28.47300 1.000 39.32000  ? 251  ALA B O   1 
ATOM   5755  C CB  . ALA B 1 232 ? 61.05200  -42.81800 -29.41400 1.000 37.46000  ? 251  ALA B CB  1 
ATOM   5756  N N   . TRP B 1 233 ? 62.56100  -43.87800 -26.46900 1.000 43.45000  ? 252  TRP B N   1 
ATOM   5757  C CA  . TRP B 1 233 ? 63.89900  -44.12400 -25.93200 1.000 42.95000  ? 252  TRP B CA  1 
ATOM   5758  C C   . TRP B 1 233 ? 64.19200  -45.61300 -25.82500 1.000 44.35000  ? 252  TRP B C   1 
ATOM   5759  O O   . TRP B 1 233 ? 65.33100  -46.04500 -26.03500 1.000 40.17000  ? 252  TRP B O   1 
ATOM   5760  C CB  . TRP B 1 233 ? 64.04200  -43.48000 -24.56300 1.000 35.88000  ? 252  TRP B CB  1 
ATOM   5761  C CG  . TRP B 1 233 ? 63.89600  -42.01200 -24.57100 1.000 33.91000  ? 252  TRP B CG  1 
ATOM   5762  C CD1 . TRP B 1 233 ? 63.80200  -41.19600 -25.65900 1.000 34.16000  ? 252  TRP B CD1 1 
ATOM   5763  C CD2 . TRP B 1 233 ? 63.80100  -41.16900 -23.42100 1.000 32.09000  ? 252  TRP B CD2 1 
ATOM   5764  N NE1 . TRP B 1 233 ? 63.65900  -39.88800 -25.25400 1.000 32.44000  ? 252  TRP B NE1 1 
ATOM   5765  C CE2 . TRP B 1 233 ? 63.66400  -39.84600 -23.88300 1.000 33.82000  ? 252  TRP B CE2 1 
ATOM   5766  C CE3 . TRP B 1 233 ? 63.82300  -41.40500 -22.04000 1.000 32.00000  ? 252  TRP B CE3 1 
ATOM   5767  C CZ2 . TRP B 1 233 ? 63.54500  -38.76100 -23.01300 1.000 33.02000  ? 252  TRP B CZ2 1 
ATOM   5768  C CZ3 . TRP B 1 233 ? 63.71300  -40.33200 -21.18400 1.000 27.76000  ? 252  TRP B CZ3 1 
ATOM   5769  C CH2 . TRP B 1 233 ? 63.57400  -39.02300 -21.67100 1.000 27.52000  ? 252  TRP B CH2 1 
ATOM   5770  N N   . SER B 1 234 ? 63.17900  -46.41100 -25.48800 1.000 42.26000  ? 253  SER B N   1 
ATOM   5771  C CA  . SER B 1 234 ? 63.40300  -47.83600 -25.29400 1.000 43.07000  ? 253  SER B CA  1 
ATOM   5772  C C   . SER B 1 234 ? 63.97000  -48.47300 -26.55600 1.000 45.03000  ? 253  SER B C   1 
ATOM   5773  O O   . SER B 1 234 ? 64.97000  -49.19900 -26.49900 1.000 45.53000  ? 253  SER B O   1 
ATOM   5774  C CB  . SER B 1 234 ? 62.10200  -48.51400 -24.86900 1.000 41.81000  ? 253  SER B CB  1 
ATOM   5775  O OG  . SER B 1 234 ? 62.30400  -49.89400 -24.62800 1.000 49.37000  ? 253  SER B OG  1 
ATOM   5776  N N   . ASN B 1 235 ? 63.36900  -48.17400 -27.71400 1.000 44.37000  ? 254  ASN B N   1 
ATOM   5777  C CA  . ASN B 1 235 ? 63.86800  -48.75100 -28.95800 1.000 41.63000  ? 254  ASN B CA  1 
ATOM   5778  C C   . ASN B 1 235 ? 65.28400  -48.28600 -29.25000 1.000 41.94000  ? 254  ASN B C   1 
ATOM   5779  O O   . ASN B 1 235 ? 66.10500  -49.06500 -29.74600 1.000 43.06000  ? 254  ASN B O   1 
ATOM   5780  C CB  . ASN B 1 235 ? 62.96100  -48.41100 -30.14300 1.000 46.12000  ? 254  ASN B CB  1 
ATOM   5781  C CG  . ASN B 1 235 ? 61.62200  -49.11900 -30.08100 1.000 47.85000  ? 254  ASN B CG  1 
ATOM   5782  O OD1 . ASN B 1 235 ? 61.50000  -50.20500 -29.51400 1.000 51.02000  ? 254  ASN B OD1 1 
ATOM   5783  N ND2 . ASN B 1 235 ? 60.62300  -48.53500 -30.73300 1.000 46.46000  ? 254  ASN B ND2 1 
ATOM   5784  N N   . ILE B 1 236 ? 65.59100  -47.01500 -28.97200 1.000 43.71000  ? 255  ILE B N   1 
ATOM   5785  C CA  . ILE B 1 236 ? 66.95200  -46.54200 -29.21300 1.000 43.90000  ? 255  ILE B CA  1 
ATOM   5786  C C   . ILE B 1 236 ? 67.91600  -47.23200 -28.26200 1.000 42.25000  ? 255  ILE B C   1 
ATOM   5787  O O   . ILE B 1 236 ? 69.01600  -47.63000 -28.65700 1.000 43.92000  ? 255  ILE B O   1 
ATOM   5788  C CB  . ILE B 1 236 ? 67.06100  -45.01400 -29.07400 1.000 42.40000  ? 255  ILE B CB  1 
ATOM   5789  C CG1 . ILE B 1 236 ? 65.97100  -44.29400 -29.85900 1.000 38.06000  ? 255  ILE B CG1 1 
ATOM   5790  C CG2 . ILE B 1 236 ? 68.38700  -44.56500 -29.64700 1.000 37.04000  ? 255  ILE B CG2 1 
ATOM   5791  C CD1 . ILE B 1 236 ? 65.93000  -42.80300 -29.56300 1.000 34.47000  ? 255  ILE B CD1 1 
ATOM   5792  N N   . ASP B 1 237 ? 67.51400  -47.38800 -26.99400 1.000 40.32000  ? 256  ASP B N   1 
ATOM   5793  C CA  . ASP B 1 237 ? 68.31500  -48.14800 -26.04000 1.000 45.70000  ? 256  ASP B CA  1 
ATOM   5794  C C   . ASP B 1 237 ? 68.69100  -49.50700 -26.61700 1.000 46.87000  ? 256  ASP B C   1 
ATOM   5795  O O   . ASP B 1 237 ? 69.85900  -49.90900 -26.59900 1.000 49.35000  ? 256  ASP B O   1 
ATOM   5796  C CB  . ASP B 1 237 ? 67.54700  -48.35000 -24.72800 1.000 44.85000  ? 256  ASP B CB  1 
ATOM   5797  C CG  . ASP B 1 237 ? 67.32900  -47.06400 -23.95300 1.000 45.37000  ? 256  ASP B CG  1 
ATOM   5798  O OD1 . ASP B 1 237 ? 68.12000  -46.11300 -24.12300 1.000 48.62000  ? 256  ASP B OD1 1 
ATOM   5799  O OD2 . ASP B 1 237 ? 66.37000  -47.01800 -23.14800 1.000 44.60000  ? 256  ASP B OD2 1 
ATOM   5800  N N   . THR B 1 238 ? 67.70000  -50.22300 -27.14700 1.000 48.74000  ? 257  THR B N   1 
ATOM   5801  C CA  . THR B 1 238 ? 67.95700  -51.53500 -27.72200 1.000 46.36000  ? 257  THR B CA  1 
ATOM   5802  C C   . THR B 1 238 ? 68.93500  -51.46100 -28.88600 1.000 41.96000  ? 257  THR B C   1 
ATOM   5803  O O   . THR B 1 238 ? 69.75400  -52.36800 -29.06200 1.000 42.25000  ? 257  THR B O   1 
ATOM   5804  C CB  . THR B 1 238 ? 66.63900  -52.16800 -28.16400 1.000 42.70000  ? 257  THR B CB  1 
ATOM   5805  O OG1 . THR B 1 238 ? 65.79400  -52.36000 -27.01900 1.000 47.67000  ? 257  THR B OG1 1 
ATOM   5806  C CG2 . THR B 1 238 ? 66.88800  -53.49900 -28.84300 1.000 38.21000  ? 257  THR B CG2 1 
ATOM   5807  N N   . SER B 1 239 ? 68.88800  -50.38800 -29.67500 1.000 41.15000  ? 258  SER B N   1 
ATOM   5808  C CA  . SER B 1 239 ? 69.69500  -50.34600 -30.89000 1.000 42.42000  ? 258  SER B CA  1 
ATOM   5809  C C   . SER B 1 239 ? 71.17400  -50.17000 -30.60000 1.000 41.67000  ? 258  SER B C   1 
ATOM   5810  O O   . SER B 1 239 ? 71.99100  -50.41500 -31.49100 1.000 46.22000  ? 258  SER B O   1 
ATOM   5811  C CB  . SER B 1 239 ? 69.26100  -49.20500 -31.80400 1.000 39.60000  ? 258  SER B CB  1 
ATOM   5812  O OG  . SER B 1 239 ? 69.74700  -47.97700 -31.28800 1.000 43.31000  ? 258  SER B OG  1 
ATOM   5813  N N   . ALA B 1 240 ? 71.52500  -49.71200 -29.40100 1.000 43.44000  ? 259  ALA B N   1 
ATOM   5814  C CA  . ALA B 1 240 ? 72.88700  -49.41600 -28.94300 1.000 49.23000  ? 259  ALA B CA  1 
ATOM   5815  C C   . ALA B 1 240 ? 73.47100  -48.14600 -29.55500 1.000 42.82000  ? 259  ALA B C   1 
ATOM   5816  O O   . ALA B 1 240 ? 74.66600  -47.90900 -29.39500 1.000 51.44000  ? 259  ALA B O   1 
ATOM   5817  C CB  . ALA B 1 240 ? 73.86400  -50.57200 -29.19100 1.000 46.53000  ? 259  ALA B CB  1 
ATOM   5818  N N   . VAL B 1 241 ? 72.68300  -47.32100 -30.24300 1.000 43.16000  ? 260  VAL B N   1 
ATOM   5819  C CA  . VAL B 1 241 ? 73.14300  -45.98600 -30.61000 1.000 38.31000  ? 260  VAL B CA  1 
ATOM   5820  C C   . VAL B 1 241 ? 73.38000  -45.17200 -29.34300 1.000 36.62000  ? 260  VAL B C   1 
ATOM   5821  O O   . VAL B 1 241 ? 72.61200  -45.26400 -28.37400 1.000 37.55000  ? 260  VAL B O   1 
ATOM   5822  C CB  . VAL B 1 241 ? 72.11100  -45.29900 -31.52600 1.000 41.98000  ? 260  VAL B CB  1 
ATOM   5823  C CG1 . VAL B 1 241 ? 72.54000  -43.88000 -31.87700 1.000 37.62000  ? 260  VAL B CG1 1 
ATOM   5824  C CG2 . VAL B 1 241 ? 71.86900  -46.12100 -32.77700 1.000 36.39000  ? 260  VAL B CG2 1 
ATOM   5825  N N   . ASN B 1 242 ? 74.45200  -44.37900 -29.33300 1.000 34.93000  ? 261  ASN B N   1 
ATOM   5826  C CA  . ASN B 1 242 ? 74.70400  -43.46100 -28.22300 1.000 37.31000  ? 261  ASN B CA  1 
ATOM   5827  C C   . ASN B 1 242 ? 73.98100  -42.16000 -28.53400 1.000 34.63000  ? 261  ASN B C   1 
ATOM   5828  O O   . ASN B 1 242 ? 74.43400  -41.36200 -29.35300 1.000 37.87000  ? 261  ASN B O   1 
ATOM   5829  C CB  . ASN B 1 242 ? 76.19500  -43.23100 -28.00000 1.000 39.06000  ? 261  ASN B CB  1 
ATOM   5830  C CG  . ASN B 1 242 ? 76.92200  -44.49100 -27.58000 1.000 48.40000  ? 261  ASN B CG  1 
ATOM   5831  O OD1 . ASN B 1 242 ? 77.89100  -44.91200 -28.22700 1.000 50.98000  ? 261  ASN B OD1 1 
ATOM   5832  N ND2 . ASN B 1 242 ? 76.43000  -45.13100 -26.51300 1.000 38.88000  ? 261  ASN B ND2 1 
ATOM   5833  N N   . TYR B 1 243 ? 72.85800  -41.93200 -27.87600 1.000 36.85000  ? 262  TYR B N   1 
ATOM   5834  C CA  . TYR B 1 243 ? 72.03400  -40.78400 -28.19800 1.000 35.32000  ? 262  TYR B CA  1 
ATOM   5835  C C   . TYR B 1 243 ? 71.96700  -39.83400 -27.01400 1.000 34.57000  ? 262  TYR B C   1 
ATOM   5836  O O   . TYR B 1 243 ? 72.04300  -40.24400 -25.85000 1.000 39.08000  ? 262  TYR B O   1 
ATOM   5837  C CB  . TYR B 1 243 ? 70.62300  -41.21300 -28.60300 1.000 42.00000  ? 262  TYR B CB  1 
ATOM   5838  C CG  . TYR B 1 243 ? 69.81600  -41.82100 -27.48100 1.000 38.73000  ? 262  TYR B CG  1 
ATOM   5839  C CD1 . TYR B 1 243 ? 69.97900  -43.15500 -27.13200 1.000 36.18000  ? 262  TYR B CD1 1 
ATOM   5840  C CD2 . TYR B 1 243 ? 68.86600  -41.07500 -26.79800 1.000 39.01000  ? 262  TYR B CD2 1 
ATOM   5841  C CE1 . TYR B 1 243 ? 69.23800  -43.72700 -26.12400 1.000 36.80000  ? 262  TYR B CE1 1 
ATOM   5842  C CE2 . TYR B 1 243 ? 68.11600  -41.64000 -25.78300 1.000 38.66000  ? 262  TYR B CE2 1 
ATOM   5843  C CZ  . TYR B 1 243 ? 68.30800  -42.96800 -25.45200 1.000 40.26000  ? 262  TYR B CZ  1 
ATOM   5844  O OH  . TYR B 1 243 ? 67.56800  -43.54000 -24.44000 1.000 41.04000  ? 262  TYR B OH  1 
ATOM   5845  N N   . GLY B 1 244 ? 71.84300  -38.55400 -27.33400 1.000 35.50000  ? 263  GLY B N   1 
ATOM   5846  C CA  . GLY B 1 244 ? 71.54900  -37.55300 -26.34200 1.000 34.88000  ? 263  GLY B CA  1 
ATOM   5847  C C   . GLY B 1 244 ? 70.17300  -36.99000 -26.60500 1.000 34.45000  ? 263  GLY B C   1 
ATOM   5848  O O   . GLY B 1 244 ? 69.67200  -37.06200 -27.73300 1.000 34.74000  ? 263  GLY B O   1 
ATOM   5849  N N   . VAL B 1 245 ? 69.54200  -36.44800 -25.56900 1.000 35.28000  ? 264  VAL B N   1 
ATOM   5850  C CA  . VAL B 1 245 ? 68.25400  -35.78100 -25.69000 1.000 29.56000  ? 264  VAL B CA  1 
ATOM   5851  C C   . VAL B 1 245 ? 68.45500  -34.36000 -25.18700 1.000 28.46000  ? 264  VAL B C   1 
ATOM   5852  O O   . VAL B 1 245 ? 69.08600  -34.15200 -24.14500 1.000 42.27000  ? 264  VAL B O   1 
ATOM   5853  C CB  . VAL B 1 245 ? 67.16400  -36.51700 -24.89800 1.000 29.61000  ? 264  VAL B CB  1 
ATOM   5854  C CG1 . VAL B 1 245 ? 65.82200  -35.84900 -25.09200 1.000 34.41000  ? 264  VAL B CG1 1 
ATOM   5855  C CG2 . VAL B 1 245 ? 67.10700  -37.98300 -25.31300 1.000 29.33000  ? 264  VAL B CG2 1 
ATOM   5856  N N   . THR B 1 246 ? 67.97900  -33.38100 -25.94600 1.000 29.28000  ? 265  THR B N   1 
ATOM   5857  C CA  . THR B 1 246 ? 68.30600  -31.99500 -25.65200 1.000 30.14000  ? 265  THR B CA  1 
ATOM   5858  C C   . THR B 1 246 ? 67.16900  -31.07800 -26.09600 1.000 34.75000  ? 265  THR B C   1 
ATOM   5859  O O   . THR B 1 246 ? 66.17100  -31.50900 -26.68900 1.000 36.67000  ? 265  THR B O   1 
ATOM   5860  C CB  . THR B 1 246 ? 69.61700  -31.59100 -26.32800 1.000 32.95000  ? 265  THR B CB  1 
ATOM   5861  O OG1 . THR B 1 246 ? 69.95400  -30.25200 -25.94900 1.000 32.22000  ? 265  THR B OG1 1 
ATOM   5862  C CG2 . THR B 1 246 ? 69.46600  -31.66200 -27.82600 1.000 33.16000  ? 265  THR B CG2 1 
ATOM   5863  N N   . VAL B 1 247 ? 67.34000  -29.78900 -25.79000 1.000 32.50000  ? 266  VAL B N   1 
ATOM   5864  C CA  . VAL B 1 247 ? 66.36600  -28.77600 -26.16500 1.000 34.53000  ? 266  VAL B CA  1 
ATOM   5865  C C   . VAL B 1 247 ? 66.22700  -28.73100 -27.67900 1.000 36.93000  ? 266  VAL B C   1 
ATOM   5866  O O   . VAL B 1 247 ? 67.21400  -28.83800 -28.41800 1.000 39.45000  ? 266  VAL B O   1 
ATOM   5867  C CB  . VAL B 1 247 ? 66.80000  -27.41500 -25.59200 1.000 35.67000  ? 266  VAL B CB  1 
ATOM   5868  C CG1 . VAL B 1 247 ? 68.17000  -27.00500 -26.17600 1.000 35.65000  ? 266  VAL B CG1 1 
ATOM   5869  C CG2 . VAL B 1 247 ? 65.75800  -26.35200 -25.88100 1.000 27.07000  ? 266  VAL B CG2 1 
ATOM   5870  N N   . LEU B 1 248 ? 64.99200  -28.58300 -28.14600 1.000 35.27000  ? 267  LEU B N   1 
ATOM   5871  C CA  . LEU B 1 248 ? 64.74100  -28.45300 -29.57100 1.000 33.31000  ? 267  LEU B CA  1 
ATOM   5872  C C   . LEU B 1 248 ? 65.42800  -27.19500 -30.09800 1.000 33.93000  ? 267  LEU B C   1 
ATOM   5873  O O   . LEU B 1 248 ? 65.67500  -26.25600 -29.33500 1.000 37.60000  ? 267  LEU B O   1 
ATOM   5874  C CB  . LEU B 1 248 ? 63.24000  -28.37700 -29.82200 1.000 27.91000  ? 267  LEU B CB  1 
ATOM   5875  C CG  . LEU B 1 248 ? 62.48200  -29.67400 -29.59200 1.000 32.99000  ? 267  LEU B CG  1 
ATOM   5876  C CD1 . LEU B 1 248 ? 61.00200  -29.38400 -29.47000 1.000 33.46000  ? 267  LEU B CD1 1 
ATOM   5877  C CD2 . LEU B 1 248 ? 62.73600  -30.58600 -30.77900 1.000 30.69000  ? 267  LEU B CD2 1 
ATOM   5878  N N   . PRO B 1 249 ? 65.76200  -27.15100 -31.39100 1.000 34.86000  ? 268  PRO B N   1 
ATOM   5879  C CA  . PRO B 1 249 ? 66.35000  -25.93100 -31.95000 1.000 31.58000  ? 268  PRO B CA  1 
ATOM   5880  C C   . PRO B 1 249 ? 65.38300  -24.76100 -31.85600 1.000 35.86000  ? 268  PRO B C   1 
ATOM   5881  O O   . PRO B 1 249 ? 64.16300  -24.92700 -31.86000 1.000 31.80000  ? 268  PRO B O   1 
ATOM   5882  C CB  . PRO B 1 249 ? 66.61400  -26.30100 -33.41600 1.000 33.70000  ? 268  PRO B CB  1 
ATOM   5883  C CG  . PRO B 1 249 ? 66.61800  -27.78500 -33.45600 1.000 32.13000  ? 268  PRO B CG  1 
ATOM   5884  C CD  . PRO B 1 249 ? 65.62700  -28.20300 -32.41400 1.000 32.97000  ? 268  PRO B CD  1 
ATOM   5885  N N   . THR B 1 250 ? 65.94700  -23.56700 -31.76800 1.000 35.06000  ? 269  THR B N   1 
ATOM   5886  C CA  . THR B 1 250 ? 65.16900  -22.35500 -31.93000 1.000 33.06000  ? 269  THR B CA  1 
ATOM   5887  C C   . THR B 1 250 ? 64.87100  -22.10500 -33.40700 1.000 36.27000  ? 269  THR B C   1 
ATOM   5888  O O   . THR B 1 250 ? 65.52300  -22.64600 -34.30900 1.000 32.80000  ? 269  THR B O   1 
ATOM   5889  C CB  . THR B 1 250 ? 65.92700  -21.16400 -31.35100 1.000 40.32000  ? 269  THR B CB  1 
ATOM   5890  O OG1 . THR B 1 250 ? 67.17800  -21.03600 -32.04900 1.000 36.54000  ? 269  THR B OG1 1 
ATOM   5891  C CG2 . THR B 1 250 ? 66.18900  -21.36500 -29.84100 1.000 31.21000  ? 269  THR B CG2 1 
ATOM   5892  N N   . PHE B 1 251 ? 63.85700  -21.27700 -33.65500 1.000 39.40000  ? 270  PHE B N   1 
ATOM   5893  C CA  . PHE B 1 251 ? 63.58500  -20.77000 -34.99400 1.000 41.33000  ? 270  PHE B CA  1 
ATOM   5894  C C   . PHE B 1 251 ? 63.39300  -19.26500 -34.91000 1.000 36.52000  ? 270  PHE B C   1 
ATOM   5895  O O   . PHE B 1 251 ? 62.65000  -18.78900 -34.05400 1.000 35.33000  ? 270  PHE B O   1 
ATOM   5896  C CB  . PHE B 1 251 ? 62.36100  -21.43000 -35.63500 1.000 37.78000  ? 270  PHE B CB  1 
ATOM   5897  C CG  . PHE B 1 251 ? 62.00700  -20.82600 -36.96500 1.000 40.22000  ? 270  PHE B CG  1 
ATOM   5898  C CD1 . PHE B 1 251 ? 62.88700  -20.89900 -38.02400 1.000 40.76000  ? 270  PHE B CD1 1 
ATOM   5899  C CD2 . PHE B 1 251 ? 60.78300  -20.20000 -37.15900 1.000 42.49000  ? 270  PHE B CD2 1 
ATOM   5900  C CE1 . PHE B 1 251 ? 62.56800  -20.33500 -39.25200 1.000 47.32000  ? 270  PHE B CE1 1 
ATOM   5901  C CE2 . PHE B 1 251 ? 60.45500  -19.63900 -38.38200 1.000 36.37000  ? 270  PHE B CE2 1 
ATOM   5902  C CZ  . PHE B 1 251 ? 61.34500  -19.70700 -39.42900 1.000 39.99000  ? 270  PHE B CZ  1 
ATOM   5903  N N   . LYS B 1 252 ? 64.07700  -18.52700 -35.78300 1.000 41.18000  ? 271  LYS B N   1 
ATOM   5904  C CA  . LYS B 1 252 ? 64.08300  -17.07900 -35.76200 1.000 41.69000  ? 271  LYS B CA  1 
ATOM   5905  C C   . LYS B 1 252 ? 64.37600  -16.56600 -34.35400 1.000 43.11000  ? 271  LYS B C   1 
ATOM   5906  O O   . LYS B 1 252 ? 63.81300  -15.56500 -33.89500 1.000 42.87000  ? 271  LYS B O   1 
ATOM   5907  C CB  . LYS B 1 252 ? 62.77200  -16.49400 -36.29900 1.000 44.26000  ? 271  LYS B CB  1 
ATOM   5908  C CG  . LYS B 1 252 ? 62.60500  -16.68300 -37.80600 1.000 38.25000  ? 271  LYS B CG  1 
ATOM   5909  C CD  . LYS B 1 252 ? 61.28700  -16.16300 -38.30700 1.000 41.13000  ? 271  LYS B CD  1 
ATOM   5910  C CE  . LYS B 1 252 ? 61.24700  -14.64500 -38.28700 1.000 47.18000  ? 271  LYS B CE  1 
ATOM   5911  N NZ  . LYS B 1 252 ? 59.95400  -14.10800 -38.83400 1.000 53.12000  ? 271  LYS B NZ  1 
ATOM   5912  N N   . GLY B 1 253 ? 65.24600  -17.27300 -33.64500 1.000 38.86000  ? 272  GLY B N   1 
ATOM   5913  C CA  . GLY B 1 253 ? 65.65900  -16.89000 -32.32500 1.000 44.48000  ? 272  GLY B CA  1 
ATOM   5914  C C   . GLY B 1 253 ? 64.73700  -17.32100 -31.20200 1.000 41.72000  ? 272  GLY B C   1 
ATOM   5915  O O   . GLY B 1 253 ? 65.12200  -17.19600 -30.02600 1.000 48.05000  ? 272  GLY B O   1 
ATOM   5916  N N   . GLN B 1 254 ? 63.56700  -17.83700 -31.51000 1.000 40.89000  ? 273  GLN B N   1 
ATOM   5917  C CA  . GLN B 1 254 ? 62.59300  -18.15500 -30.47100 1.000 39.06000  ? 273  GLN B CA  1 
ATOM   5918  C C   . GLN B 1 254 ? 62.47700  -19.67700 -30.35100 1.000 38.50000  ? 273  GLN B C   1 
ATOM   5919  O O   . GLN B 1 254 ? 62.68200  -20.38800 -31.34200 1.000 41.46000  ? 273  GLN B O   1 
ATOM   5920  C CB  . GLN B 1 254 ? 61.24700  -17.55800 -30.86000 1.000 39.06000  ? 273  GLN B CB  1 
ATOM   5921  C CG  . GLN B 1 254 ? 61.45800  -16.20900 -31.50400 1.000 40.02000  ? 273  GLN B CG  1 
ATOM   5922  C CD  . GLN B 1 254 ? 60.24800  -15.71300 -32.25800 1.000 52.39000  ? 273  GLN B CD  1 
ATOM   5923  O OE1 . GLN B 1 254 ? 59.12300  -16.17800 -32.04200 1.000 61.59000  ? 273  GLN B OE1 1 
ATOM   5924  N NE2 . GLN B 1 254 ? 60.50200  -14.91500 -33.30500 1.000 51.10000  ? 273  GLN B NE2 1 
ATOM   5925  N N   . PRO B 1 255 ? 62.20100  -20.21300 -29.18400 1.000 37.81000  ? 274  PRO B N   1 
ATOM   5926  C CA  . PRO B 1 255 ? 62.22100  -21.68100 -29.03900 1.000 38.51000  ? 274  PRO B CA  1 
ATOM   5927  C C   . PRO B 1 255 ? 61.07600  -22.35500 -29.76800 1.000 40.53000  ? 274  PRO B C   1 
ATOM   5928  O O   . PRO B 1 255 ? 59.96500  -21.81500 -29.89500 1.000 39.72000  ? 274  PRO B O   1 
ATOM   5929  C CB  . PRO B 1 255 ? 62.09600  -21.89000 -27.52100 1.000 37.97000  ? 274  PRO B CB  1 
ATOM   5930  C CG  . PRO B 1 255 ? 61.45000  -20.65100 -27.02200 1.000 34.01000  ? 274  PRO B CG  1 
ATOM   5931  C CD  . PRO B 1 255 ? 61.92600  -19.52800 -27.89700 1.000 38.61000  ? 274  PRO B CD  1 
ATOM   5932  N N   . SER B 1 256 ? 61.34400  -23.56700 -30.24400 1.000 36.40000  ? 275  SER B N   1 
ATOM   5933  C CA  . SER B 1 256 ? 60.27200  -24.42400 -30.72600 1.000 31.72000  ? 275  SER B CA  1 
ATOM   5934  C C   . SER B 1 256 ? 59.30700  -24.73000 -29.59500 1.000 37.56000  ? 275  SER B C   1 
ATOM   5935  O O   . SER B 1 256 ? 59.71400  -24.86900 -28.44300 1.000 35.20000  ? 275  SER B O   1 
ATOM   5936  C CB  . SER B 1 256 ? 60.83900  -25.75300 -31.28500 1.000 31.97000  ? 275  SER B CB  1 
ATOM   5937  O OG  . SER B 1 256 ? 61.53500  -25.53800 -32.50000 1.000 35.15000  ? 275  SER B OG  1 
ATOM   5938  N N   . LYS B 1 257 ? 58.01700  -24.83500 -29.93300 1.000 36.15000  ? 276  LYS B N   1 
ATOM   5939  C CA  . LYS B 1 257 ? 56.93000  -24.90400 -28.96100 1.000 39.36000  ? 276  LYS B CA  1 
ATOM   5940  C C   . LYS B 1 257 ? 56.16800  -26.21600 -29.12200 1.000 32.40000  ? 276  LYS B C   1 
ATOM   5941  O O   . LYS B 1 257 ? 55.09300  -26.24800 -29.73500 1.000 37.43000  ? 276  LYS B O   1 
ATOM   5942  C CB  . LYS B 1 257 ? 56.00000  -23.70000 -29.11500 1.000 35.65000  ? 276  LYS B CB  1 
ATOM   5943  C CG  . LYS B 1 257 ? 56.62700  -22.40100 -28.62800 1.000 36.58000  ? 276  LYS B CG  1 
ATOM   5944  C CD  . LYS B 1 257 ? 55.81000  -21.18200 -29.00700 1.000 36.12000  ? 276  LYS B CD  1 
ATOM   5945  C CE  . LYS B 1 257 ? 54.49100  -21.13400 -28.27800 1.000 48.16000  ? 276  LYS B CE  1 
ATOM   5946  N NZ  . LYS B 1 257 ? 54.65500  -20.90700 -26.82900 1.000 49.61000  ? 276  LYS B NZ  1 
ATOM   5947  N N   . PRO B 1 258 ? 56.68600  -27.31700 -28.58200 1.000 34.04000  ? 277  PRO B N   1 
ATOM   5948  C CA  . PRO B 1 258 ? 55.97200  -28.59300 -28.68500 1.000 27.80000  ? 277  PRO B CA  1 
ATOM   5949  C C   . PRO B 1 258 ? 54.73700  -28.60400 -27.80500 1.000 37.97000  ? 277  PRO B C   1 
ATOM   5950  O O   . PRO B 1 258 ? 54.62200  -27.84000 -26.84200 1.000 41.91000  ? 277  PRO B O   1 
ATOM   5951  C CB  . PRO B 1 258 ? 57.00000  -29.61600 -28.20000 1.000 30.80000  ? 277  PRO B CB  1 
ATOM   5952  C CG  . PRO B 1 258 ? 57.90200  -28.82100 -27.27400 1.000 34.04000  ? 277  PRO B CG  1 
ATOM   5953  C CD  . PRO B 1 258 ? 57.97000  -27.44200 -27.86300 1.000 31.67000  ? 277  PRO B CD  1 
ATOM   5954  N N   . PHE B 1 259 ? 53.80000  -29.48600 -28.15200 1.000 34.36000  ? 278  PHE B N   1 
ATOM   5955  C CA  . PHE B 1 259 ? 52.64900  -29.70300 -27.28600 1.000 32.67000  ? 278  PHE B CA  1 
ATOM   5956  C C   . PHE B 1 259 ? 53.05000  -30.50700 -26.06100 1.000 35.71000  ? 278  PHE B C   1 
ATOM   5957  O O   . PHE B 1 259 ? 53.83200  -31.45800 -26.14900 1.000 36.29000  ? 278  PHE B O   1 
ATOM   5958  C CB  . PHE B 1 259 ? 51.51600  -30.41900 -28.01900 1.000 32.36000  ? 278  PHE B CB  1 
ATOM   5959  C CG  . PHE B 1 259 ? 50.78000  -29.55200 -28.98700 1.000 35.67000  ? 278  PHE B CG  1 
ATOM   5960  C CD1 . PHE B 1 259 ? 49.98500  -28.51200 -28.52400 1.000 32.56000  ? 278  PHE B CD1 1 
ATOM   5961  C CD2 . PHE B 1 259 ? 50.83500  -29.79800 -30.34700 1.000 31.49000  ? 278  PHE B CD2 1 
ATOM   5962  C CE1 . PHE B 1 259 ? 49.29100  -27.70600 -29.39500 1.000 34.51000  ? 278  PHE B CE1 1 
ATOM   5963  C CE2 . PHE B 1 259 ? 50.12200  -29.00000 -31.23200 1.000 39.98000  ? 278  PHE B CE2 1 
ATOM   5964  C CZ  . PHE B 1 259 ? 49.34900  -27.95200 -30.75500 1.000 32.07000  ? 278  PHE B CZ  1 
ATOM   5965  N N   . VAL B 1 260 ? 52.49200  -30.12900 -24.91500 1.000 32.30000  ? 279  VAL B N   1 
ATOM   5966  C CA  . VAL B 1 260 ? 52.83100  -30.73300 -23.63600 1.000 32.33000  ? 279  VAL B CA  1 
ATOM   5967  C C   . VAL B 1 260 ? 51.63400  -31.55300 -23.18100 1.000 26.50000  ? 279  VAL B C   1 
ATOM   5968  O O   . VAL B 1 260 ? 50.53500  -31.01200 -23.01300 1.000 31.06000  ? 279  VAL B O   1 
ATOM   5969  C CB  . VAL B 1 260 ? 53.20100  -29.66700 -22.59500 1.000 30.91000  ? 279  VAL B CB  1 
ATOM   5970  C CG1 . VAL B 1 260 ? 53.63000  -30.31100 -21.27800 1.000 29.31000  ? 279  VAL B CG1 1 
ATOM   5971  C CG2 . VAL B 1 260 ? 54.27100  -28.73300 -23.13500 1.000 31.18000  ? 279  VAL B CG2 1 
ATOM   5972  N N   . GLY B 1 261 ? 51.84200  -32.85100 -22.99000 1.000 26.61000  ? 280  GLY B N   1 
ATOM   5973  C CA  . GLY B 1 261 ? 50.86500  -33.71000 -22.34600 1.000 27.45000  ? 280  GLY B CA  1 
ATOM   5974  C C   . GLY B 1 261 ? 51.23000  -33.91300 -20.88000 1.000 37.45000  ? 280  GLY B C   1 
ATOM   5975  O O   . GLY B 1 261 ? 52.37100  -34.23300 -20.55700 1.000 38.41000  ? 280  GLY B O   1 
ATOM   5976  N N   . VAL B 1 262 ? 50.24700  -33.71000 -20.01300 1.000 37.86000  ? 281  VAL B N   1 
ATOM   5977  C CA  . VAL B 1 262 ? 50.43500  -33.77200 -18.57000 1.000 34.99000  ? 281  VAL B CA  1 
ATOM   5978  C C   . VAL B 1 262 ? 49.61700  -34.94800 -18.05600 1.000 37.95000  ? 281  VAL B C   1 
ATOM   5979  O O   . VAL B 1 262 ? 48.38600  -34.87300 -18.00000 1.000 35.23000  ? 281  VAL B O   1 
ATOM   5980  C CB  . VAL B 1 262 ? 50.01300  -32.46300 -17.88900 1.000 34.77000  ? 281  VAL B CB  1 
ATOM   5981  C CG1 . VAL B 1 262 ? 50.07800  -32.59600 -16.37200 1.000 29.81000  ? 281  VAL B CG1 1 
ATOM   5982  C CG2 . VAL B 1 262 ? 50.88400  -31.30500 -18.37300 1.000 26.92000  ? 281  VAL B CG2 1 
ATOM   5983  N N   . LEU B 1 263 ? 50.29000  -36.04300 -17.69800 1.000 37.77000  ? 282  LEU B N   1 
ATOM   5984  C CA  . LEU B 1 263 ? 49.60200  -37.15700 -17.05800 1.000 34.49000  ? 282  LEU B CA  1 
ATOM   5985  C C   . LEU B 1 263 ? 48.93400  -36.65500 -15.78500 1.000 37.42000  ? 282  LEU B C   1 
ATOM   5986  O O   . LEU B 1 263 ? 49.55100  -35.93400 -15.00000 1.000 42.49000  ? 282  LEU B O   1 
ATOM   5987  C CB  . LEU B 1 263 ? 50.59000  -38.28000 -16.74400 1.000 34.28000  ? 282  LEU B CB  1 
ATOM   5988  C CG  . LEU B 1 263 ? 50.00300  -39.51200 -16.05300 1.000 39.44000  ? 282  LEU B CG  1 
ATOM   5989  C CD1 . LEU B 1 263 ? 48.97100  -40.18800 -16.94300 1.000 39.95000  ? 282  LEU B CD1 1 
ATOM   5990  C CD2 . LEU B 1 263 ? 51.09300  -40.49700 -15.63600 1.000 31.26000  ? 282  LEU B CD2 1 
ATOM   5991  N N   . SER B 1 264 ? 47.66700  -37.00700 -15.58400 1.000 35.55000  ? 283  SER B N   1 
ATOM   5992  C CA  . SER B 1 264 ? 46.89700  -36.36800 -14.52600 1.000 35.87000  ? 283  SER B CA  1 
ATOM   5993  C C   . SER B 1 264 ? 46.00200  -37.36500 -13.80100 1.000 34.70000  ? 283  SER B C   1 
ATOM   5994  O O   . SER B 1 264 ? 45.52800  -38.34600 -14.38000 1.000 36.88000  ? 283  SER B O   1 
ATOM   5995  C CB  . SER B 1 264 ? 46.05800  -35.21800 -15.09400 1.000 35.47000  ? 283  SER B CB  1 
ATOM   5996  O OG  . SER B 1 264 ? 46.89600  -34.19400 -15.58300 1.000 36.65000  ? 283  SER B OG  1 
ATOM   5997  N N   . ALA B 1 265 ? 45.75500  -37.08800 -12.52700 1.000 30.69000  ? 284  ALA B N   1 
ATOM   5998  C CA  . ALA B 1 265 ? 44.88000  -37.91100 -11.70300 1.000 34.71000  ? 284  ALA B CA  1 
ATOM   5999  C C   . ALA B 1 265 ? 43.59100  -37.14600 -11.43900 1.000 35.55000  ? 284  ALA B C   1 
ATOM   6000  O O   . ALA B 1 265 ? 43.61300  -36.09800 -10.78500 1.000 35.11000  ? 284  ALA B O   1 
ATOM   6001  C CB  . ALA B 1 265 ? 45.56200  -38.28800 -10.39000 1.000 34.67000  ? 284  ALA B CB  1 
ATOM   6002  N N   . GLY B 1 266 ? 42.47600  -37.66900 -11.94100 1.000 31.56000  ? 285  GLY B N   1 
ATOM   6003  C CA  . GLY B 1 266 ? 41.17300  -37.06100 -11.74600 1.000 37.15000  ? 285  GLY B CA  1 
ATOM   6004  C C   . GLY B 1 266 ? 40.29700  -37.92400 -10.85800 1.000 35.19000  ? 285  GLY B C   1 
ATOM   6005  O O   . GLY B 1 266 ? 40.39000  -39.15500 -10.87800 1.000 36.48000  ? 285  GLY B O   1 
ATOM   6006  N N   . ILE B 1 267 ? 39.43800  -37.27300 -10.07700 1.000 29.91000  ? 286  ILE B N   1 
ATOM   6007  C CA  . ILE B 1 267 ? 38.54400  -37.95100 -9.14600  1.000 33.31000  ? 286  ILE B CA  1 
ATOM   6008  C C   . ILE B 1 267 ? 37.13400  -37.98600 -9.73500  1.000 40.31000  ? 286  ILE B C   1 
ATOM   6009  O O   . ILE B 1 267 ? 36.58500  -36.94800 -10.13500 1.000 34.47000  ? 286  ILE B O   1 
ATOM   6010  C CB  . ILE B 1 267 ? 38.56400  -37.26100 -7.77200  1.000 43.08000  ? 286  ILE B CB  1 
ATOM   6011  C CG1 . ILE B 1 267 ? 39.95400  -37.36300 -7.15000  1.000 37.55000  ? 286  ILE B CG1 1 
ATOM   6012  C CG2 . ILE B 1 267 ? 37.50600  -37.86000 -6.84400  1.000 42.39000  ? 286  ILE B CG2 1 
ATOM   6013  C CD1 . ILE B 1 267 ? 40.14400  -36.47700 -5.94700  1.000 38.51000  ? 286  ILE B CD1 1 
ATOM   6014  N N   . ASN B 1 268 ? 36.55100  -39.18400 -9.79000  1.000 39.56000  ? 287  ASN B N   1 
ATOM   6015  C CA  . ASN B 1 268 ? 35.22300  -39.37100 -10.36300 1.000 38.16000  ? 287  ASN B CA  1 
ATOM   6016  C C   . ASN B 1 268 ? 34.17600  -38.58600 -9.58200  1.000 38.71000  ? 287  ASN B C   1 
ATOM   6017  O O   . ASN B 1 268 ? 34.10200  -38.67300 -8.35400  1.000 41.20000  ? 287  ASN B O   1 
ATOM   6018  C CB  . ASN B 1 268 ? 34.89100  -40.86700 -10.38300 1.000 36.02000  ? 287  ASN B CB  1 
ATOM   6019  C CG  . ASN B 1 268 ? 33.57800  -41.18500 -11.07900 1.000 48.45000  ? 287  ASN B CG  1 
ATOM   6020  O OD1 . ASN B 1 268 ? 32.76500  -40.30000 -11.35900 1.000 51.03000  ? 287  ASN B OD1 1 
ATOM   6021  N ND2 . ASN B 1 268 ? 33.38700  -42.46100 -11.40600 1.000 48.39000  ? 287  ASN B ND2 1 
ATOM   6022  N N   . ALA B 1 269 ? 33.36300  -37.81300 -10.30800 1.000 39.17000  ? 288  ALA B N   1 
ATOM   6023  C CA  . ALA B 1 269 ? 32.33100  -37.00200 -9.66400  1.000 41.90000  ? 288  ALA B CA  1 
ATOM   6024  C C   . ALA B 1 269 ? 31.30000  -37.85800 -8.94200  1.000 36.20000  ? 288  ALA B C   1 
ATOM   6025  O O   . ALA B 1 269 ? 30.68400  -37.39800 -7.97500  1.000 36.47000  ? 288  ALA B O   1 
ATOM   6026  C CB  . ALA B 1 269 ? 31.64400  -36.10900 -10.69400 1.000 40.36000  ? 288  ALA B CB  1 
ATOM   6027  N N   . ALA B 1 270 ? 31.10500  -39.09700 -9.37700  1.000 37.92000  ? 289  ALA B N   1 
ATOM   6028  C CA  . ALA B 1 270 ? 30.16600  -40.00200 -8.72500  1.000 41.37000  ? 289  ALA B CA  1 
ATOM   6029  C C   . ALA B 1 270 ? 30.79400  -40.80800 -7.59500  1.000 46.47000  ? 289  ALA B C   1 
ATOM   6030  O O   . ALA B 1 270 ? 30.13000  -41.69300 -7.04400  1.000 50.49000  ? 289  ALA B O   1 
ATOM   6031  C CB  . ALA B 1 270 ? 29.56300  -40.96900 -9.74800  1.000 39.76000  ? 289  ALA B CB  1 
ATOM   6032  N N   . SER B 1 271 ? 32.04800  -40.55000 -7.25200  1.000 45.00000  ? 290  SER B N   1 
ATOM   6033  C CA  . SER B 1 271 ? 32.71400  -41.34200 -6.22300  1.000 50.03000  ? 290  SER B CA  1 
ATOM   6034  C C   . SER B 1 271 ? 32.19000  -40.97600 -4.83600  1.000 44.68000  ? 290  SER B C   1 
ATOM   6035  O O   . SER B 1 271 ? 32.05300  -39.78700 -4.52400  1.000 39.78000  ? 290  SER B O   1 
ATOM   6036  C CB  . SER B 1 271 ? 34.22600  -41.13200 -6.27900  1.000 41.40000  ? 290  SER B CB  1 
ATOM   6037  O OG  . SER B 1 271 ? 34.86800  -41.83500 -5.22500  1.000 43.79000  ? 290  SER B OG  1 
ATOM   6038  N N   . PRO B 1 272 ? 31.90200  -41.95800 -3.97700  1.000 50.28000  ? 291  PRO B N   1 
ATOM   6039  C CA  . PRO B 1 272 ? 31.58600  -41.65900 -2.57700  1.000 47.60000  ? 291  PRO B CA  1 
ATOM   6040  C C   . PRO B 1 272 ? 32.82300  -41.45900 -1.72200  1.000 50.46000  ? 291  PRO B C   1 
ATOM   6041  O O   . PRO B 1 272 ? 32.68900  -41.23100 -0.51300  1.000 44.82000  ? 291  PRO B O   1 
ATOM   6042  C CB  . PRO B 1 272 ? 30.82900  -42.91200 -2.13000  1.000 43.20000  ? 291  PRO B CB  1 
ATOM   6043  C CG  . PRO B 1 272 ? 31.48700  -44.00800 -2.90800  1.000 49.90000  ? 291  PRO B CG  1 
ATOM   6044  C CD  . PRO B 1 272 ? 31.84200  -43.40500 -4.25400  1.000 52.15000  ? 291  PRO B CD  1 
ATOM   6045  N N   . ASN B 1 273 ? 34.00800  -41.55100 -2.33300  1.000 44.13000  ? 292  ASN B N   1 
ATOM   6046  C CA  . ASN B 1 273 ? 35.28300  -41.65600 -1.64200  1.000 42.16000  ? 292  ASN B CA  1 
ATOM   6047  C C   . ASN B 1 273 ? 36.19400  -40.48100 -1.97900  1.000 42.49000  ? 292  ASN B C   1 
ATOM   6048  O O   . ASN B 1 273 ? 37.40800  -40.65400 -2.10600  1.000 47.92000  ? 292  ASN B O   1 
ATOM   6049  C CB  . ASN B 1 273 ? 35.97100  -42.96800 -2.01300  1.000 43.67000  ? 292  ASN B CB  1 
ATOM   6050  C CG  . ASN B 1 273 ? 35.18400  -44.18400 -1.56900  1.000 51.90000  ? 292  ASN B CG  1 
ATOM   6051  O OD1 . ASN B 1 273 ? 34.67800  -44.24400 -0.44600  1.000 54.66000  ? 292  ASN B OD1 1 
ATOM   6052  N ND2 . ASN B 1 273 ? 35.06700  -45.16300 -2.46000  1.000 49.95000  ? 292  ASN B ND2 1 
ATOM   6053  N N   . LYS B 1 274 ? 35.63300  -39.28500 -2.15400  1.000 40.44000  ? 293  LYS B N   1 
ATOM   6054  C CA  . LYS B 1 274 ? 36.43300  -38.17300 -2.65500  1.000 36.26000  ? 293  LYS B CA  1 
ATOM   6055  C C   . LYS B 1 274 ? 37.57700  -37.81100 -1.70700  1.000 46.35000  ? 293  LYS B C   1 
ATOM   6056  O O   . LYS B 1 274 ? 38.71600  -37.61400 -2.15100  1.000 47.88000  ? 293  LYS B O   1 
ATOM   6057  C CB  . LYS B 1 274 ? 35.54800  -36.95700 -2.91300  1.000 41.75000  ? 293  LYS B CB  1 
ATOM   6058  C CG  . LYS B 1 274 ? 34.63300  -37.13200 -4.11200  1.000 46.43000  ? 293  LYS B CG  1 
ATOM   6059  C CD  . LYS B 1 274 ? 33.83400  -35.86900 -4.39900  1.000 55.50000  ? 293  LYS B CD  1 
ATOM   6060  C CE  . LYS B 1 274 ? 32.95700  -36.06100 -5.62000  1.000 46.40000  ? 293  LYS B CE  1 
ATOM   6061  N NZ  . LYS B 1 274 ? 31.96800  -37.12000 -5.30900  1.000 48.32000  ? 293  LYS B NZ  1 
ATOM   6062  N N   . GLU B 1 275 ? 37.30100  -37.70400 -0.39800  1.000 48.57000  ? 294  GLU B N   1 
ATOM   6063  C CA  . GLU B 1 275 ? 38.37700  -37.35300 0.52700   1.000 52.90000  ? 294  GLU B CA  1 
ATOM   6064  C C   . GLU B 1 275 ? 39.43000  -38.45300 0.59600   1.000 49.28000  ? 294  GLU B C   1 
ATOM   6065  O O   . GLU B 1 275 ? 40.63600  -38.16700 0.58100   1.000 46.72000  ? 294  GLU B O   1 
ATOM   6066  C CB  . GLU B 1 275 ? 37.82200  -37.03200 1.90600   1.000 47.63000  ? 294  GLU B CB  1 
ATOM   6067  C CG  . GLU B 1 275 ? 37.18600  -35.64800 1.97800   1.000 69.56000  ? 294  GLU B CG  1 
ATOM   6068  C CD  . GLU B 1 275 ? 38.19200  -34.50100 1.74100   1.000 89.79000  ? 294  GLU B CD  1 
ATOM   6069  O OE1 . GLU B 1 275 ? 39.38700  -34.62300 2.11200   1.000 91.61000  ? 294  GLU B OE1 1 
ATOM   6070  O OE2 . GLU B 1 275 ? 37.77500  -33.47300 1.16600   1.000 93.16000  ? 294  GLU B OE2 1 
ATOM   6071  N N   . LEU B 1 276 ? 38.99100  -39.71700 0.65100   1.000 43.09000  ? 295  LEU B N   1 
ATOM   6072  C CA  . LEU B 1 276 ? 39.93100  -40.83200 0.57400   1.000 48.57000  ? 295  LEU B CA  1 
ATOM   6073  C C   . LEU B 1 276 ? 40.80400  -40.72700 -0.66400  1.000 43.47000  ? 295  LEU B C   1 
ATOM   6074  O O   . LEU B 1 276 ? 42.02000  -40.90100 -0.58400  1.000 40.62000  ? 295  LEU B O   1 
ATOM   6075  C CB  . LEU B 1 276 ? 39.18100  -42.16800 0.58900   1.000 49.05000  ? 295  LEU B CB  1 
ATOM   6076  C CG  . LEU B 1 276 ? 38.58000  -42.61000 1.92000   1.000 54.49000  ? 295  LEU B CG  1 
ATOM   6077  C CD1 . LEU B 1 276 ? 37.70400  -43.84200 1.73900   1.000 49.51000  ? 295  LEU B CD1 1 
ATOM   6078  C CD2 . LEU B 1 276 ? 39.69000  -42.88500 2.92200   1.000 53.46000  ? 295  LEU B CD2 1 
ATOM   6079  N N   . ALA B 1 277 ? 40.19600  -40.43400 -1.82200  1.000 41.62000  ? 296  ALA B N   1 
ATOM   6080  C CA  . ALA B 1 277 ? 40.97200  -40.20900 -3.03900  1.000 39.26000  ? 296  ALA B CA  1 
ATOM   6081  C C   . ALA B 1 277 ? 41.86500  -38.98400 -2.89600  1.000 41.64000  ? 296  ALA B C   1 
ATOM   6082  O O   . ALA B 1 277 ? 43.02500  -38.99500 -3.33300  1.000 39.94000  ? 296  ALA B O   1 
ATOM   6083  C CB  . ALA B 1 277 ? 40.04300  -40.05800 -4.24400  1.000 35.15000  ? 296  ALA B CB  1 
ATOM   6084  N N   . LYS B 1 278 ? 41.34400  -37.91900 -2.28100  1.000 37.99000  ? 297  LYS B N   1 
ATOM   6085  C CA  . LYS B 1 278 ? 42.17500  -36.75000 -2.01800  1.000 39.99000  ? 297  LYS B CA  1 
ATOM   6086  C C   . LYS B 1 278 ? 43.36700  -37.10300 -1.14300  1.000 45.78000  ? 297  LYS B C   1 
ATOM   6087  O O   . LYS B 1 278 ? 44.50500  -36.70600 -1.43000  1.000 42.43000  ? 297  LYS B O   1 
ATOM   6088  C CB  . LYS B 1 278 ? 41.35500  -35.65400 -1.35100  1.000 37.86000  ? 297  LYS B CB  1 
ATOM   6089  C CG  . LYS B 1 278 ? 42.22300  -34.51700 -0.88700  1.000 42.98000  ? 297  LYS B CG  1 
ATOM   6090  C CD  . LYS B 1 278 ? 41.43800  -33.31500 -0.46200  1.000 43.89000  ? 297  LYS B CD  1 
ATOM   6091  C CE  . LYS B 1 278 ? 42.40100  -32.20400 -0.12000  1.000 46.44000  ? 297  LYS B CE  1 
ATOM   6092  N NZ  . LYS B 1 278 ? 41.72000  -30.90200 0.04200   1.000 56.97000  ? 297  LYS B NZ  1 
ATOM   6093  N N   . GLU B 1 279 ? 43.11900  -37.84800 -0.06800  1.000 42.44000  ? 298  GLU B N   1 
ATOM   6094  C CA  . GLU B 1 279 ? 44.18500  -38.22300 0.84600   1.000 42.14000  ? 298  GLU B CA  1 
ATOM   6095  C C   . GLU B 1 279 ? 45.24000  -39.06300 0.13600   1.000 40.50000  ? 298  GLU B C   1 
ATOM   6096  O O   . GLU B 1 279 ? 46.44700  -38.82900 0.28700   1.000 43.65000  ? 298  GLU B O   1 
ATOM   6097  C CB  . GLU B 1 279 ? 43.58300  -38.97200 2.03900   1.000 37.01000  ? 298  GLU B CB  1 
ATOM   6098  C CG  . GLU B 1 279 ? 44.58800  -39.40200 3.09200   1.000 48.40000  ? 298  GLU B CG  1 
ATOM   6099  C CD  . GLU B 1 279 ? 43.93200  -40.03800 4.30800   1.000 55.30000  ? 298  GLU B CD  1 
ATOM   6100  O OE1 . GLU B 1 279 ? 42.68300  -40.09300 4.35600   1.000 61.53000  ? 298  GLU B OE1 1 
ATOM   6101  O OE2 . GLU B 1 279 ? 44.66700  -40.49600 5.21000   1.000 54.19000  ? 298  GLU B OE2 1 
ATOM   6102  N N   . PHE B 1 280 ? 44.80000  -40.04100 -0.65700  1.000 36.55000  ? 299  PHE B N   1 
ATOM   6103  C CA  . PHE B 1 280 ? 45.73900  -40.87600 -1.39600  1.000 39.16000  ? 299  PHE B CA  1 
ATOM   6104  C C   . PHE B 1 280 ? 46.62600  -40.03600 -2.30600  1.000 40.08000  ? 299  PHE B C   1 
ATOM   6105  O O   . PHE B 1 280 ? 47.86000  -40.13000 -2.25500  1.000 37.53000  ? 299  PHE B O   1 
ATOM   6106  C CB  . PHE B 1 280 ? 44.97900  -41.91800 -2.21800  1.000 39.45000  ? 299  PHE B CB  1 
ATOM   6107  C CG  . PHE B 1 280 ? 45.87300  -42.79200 -3.03700  1.000 39.47000  ? 299  PHE B CG  1 
ATOM   6108  C CD1 . PHE B 1 280 ? 46.56800  -43.84000 -2.45000  1.000 44.54000  ? 299  PHE B CD1 1 
ATOM   6109  C CD2 . PHE B 1 280 ? 46.06400  -42.54000 -4.38500  1.000 36.54000  ? 299  PHE B CD2 1 
ATOM   6110  C CE1 . PHE B 1 280 ? 47.41500  -44.64300 -3.20000  1.000 43.80000  ? 299  PHE B CE1 1 
ATOM   6111  C CE2 . PHE B 1 280 ? 46.91200  -43.34000 -5.14500  1.000 35.37000  ? 299  PHE B CE2 1 
ATOM   6112  C CZ  . PHE B 1 280 ? 47.58700  -44.39200 -4.55100  1.000 36.63000  ? 299  PHE B CZ  1 
ATOM   6113  N N   . LEU B 1 281 ? 46.01300  -39.19300 -3.13900  1.000 37.20000  ? 300  LEU B N   1 
ATOM   6114  C CA  . LEU B 1 281 ? 46.78500  -38.43600 -4.12000  1.000 38.98000  ? 300  LEU B CA  1 
ATOM   6115  C C   . LEU B 1 281 ? 47.70400  -37.42200 -3.44300  1.000 43.98000  ? 300  LEU B C   1 
ATOM   6116  O O   . LEU B 1 281 ? 48.88600  -37.30700 -3.79200  1.000 39.04000  ? 300  LEU B O   1 
ATOM   6117  C CB  . LEU B 1 281 ? 45.83400  -37.75300 -5.10100  1.000 31.06000  ? 300  LEU B CB  1 
ATOM   6118  C CG  . LEU B 1 281 ? 45.01200  -38.76100 -5.91200  1.000 34.13000  ? 300  LEU B CG  1 
ATOM   6119  C CD1 . LEU B 1 281 ? 43.85700  -38.09400 -6.66600  1.000 32.26000  ? 300  LEU B CD1 1 
ATOM   6120  C CD2 . LEU B 1 281 ? 45.92700  -39.51300 -6.87500  1.000 30.55000  ? 300  LEU B CD2 1 
ATOM   6121  N N   . GLU B 1 282 ? 47.18500  -36.68600 -2.45800  1.000 43.66000  ? 301  GLU B N   1 
ATOM   6122  C CA  . GLU B 1 282 ? 47.98200  -35.61800 -1.86800  1.000 41.07000  ? 301  GLU B CA  1 
ATOM   6123  C C   . GLU B 1 282 ? 48.97700  -36.12600 -0.83300  1.000 43.20000  ? 301  GLU B C   1 
ATOM   6124  O O   . GLU B 1 282 ? 50.03100  -35.51000 -0.64800  1.000 46.04000  ? 301  GLU B O   1 
ATOM   6125  C CB  . GLU B 1 282 ? 47.08600  -34.55700 -1.22200  1.000 39.93000  ? 301  GLU B CB  1 
ATOM   6126  C CG  . GLU B 1 282 ? 46.19500  -33.79700 -2.19200  1.000 39.30000  ? 301  GLU B CG  1 
ATOM   6127  C CD  . GLU B 1 282 ? 45.51400  -32.59500 -1.55100  1.000 48.47000  ? 301  GLU B CD  1 
ATOM   6128  O OE1 . GLU B 1 282 ? 45.75000  -32.34000 -0.34600  1.000 46.23000  ? 301  GLU B OE1 1 
ATOM   6129  O OE2 . GLU B 1 282 ? 44.72700  -31.91400 -2.25000  1.000 46.17000  ? 301  GLU B OE2 1 
ATOM   6130  N N   . ASN B 1 283 ? 48.67200  -37.20700 -0.12400  1.000 41.99000  ? 302  ASN B N   1 
ATOM   6131  C CA  . ASN B 1 283 ? 49.56900  -37.57400 0.95800   1.000 46.87000  ? 302  ASN B CA  1 
ATOM   6132  C C   . ASN B 1 283 ? 50.40700  -38.80800 0.66200   1.000 40.94000  ? 302  ASN B C   1 
ATOM   6133  O O   . ASN B 1 283 ? 51.34400  -39.08100 1.41700   1.000 38.54000  ? 302  ASN B O   1 
ATOM   6134  C CB  . ASN B 1 283 ? 48.81500  -37.79700 2.27600   1.000 50.82000  ? 302  ASN B CB  1 
ATOM   6135  C CG  . ASN B 1 283 ? 47.98300  -36.59100 2.69200   1.000 52.73000  ? 302  ASN B CG  1 
ATOM   6136  O OD1 . ASN B 1 283 ? 48.11500  -35.49900 2.13500   1.000 50.86000  ? 302  ASN B OD1 1 
ATOM   6137  N ND2 . ASN B 1 283 ? 47.23900  -36.74900 3.78800   1.000 54.61000  ? 302  ASN B ND2 1 
ATOM   6138  N N   . TYR B 1 284 ? 50.07500  -39.60100 -0.35900  1.000 40.67000  ? 303  TYR B N   1 
ATOM   6139  C CA  . TYR B 1 284 ? 50.93800  -40.74100 -0.63900  1.000 43.10000  ? 303  TYR B CA  1 
ATOM   6140  C C   . TYR B 1 284 ? 51.53400  -40.71000 -2.03600  1.000 39.96000  ? 303  TYR B C   1 
ATOM   6141  O O   . TYR B 1 284 ? 52.73600  -40.94300 -2.18700  1.000 38.86000  ? 303  TYR B O   1 
ATOM   6142  C CB  . TYR B 1 284 ? 50.24000  -42.10100 -0.41700  1.000 43.71000  ? 303  TYR B CB  1 
ATOM   6143  C CG  . TYR B 1 284 ? 49.79500  -42.34100 1.00100   1.000 44.70000  ? 303  TYR B CG  1 
ATOM   6144  C CD1 . TYR B 1 284 ? 49.12700  -41.36600 1.72200   1.000 49.36000  ? 303  TYR B CD1 1 
ATOM   6145  C CD2 . TYR B 1 284 ? 50.29700  -43.42500 1.70500   1.000 47.52000  ? 303  TYR B CD2 1 
ATOM   6146  C CE1 . TYR B 1 284 ? 48.78000  -41.55200 3.03800   1.000 51.91000  ? 303  TYR B CE1 1 
ATOM   6147  C CE2 . TYR B 1 284 ? 49.98600  -43.61500 3.03800   1.000 57.32000  ? 303  TYR B CE2 1 
ATOM   6148  C CZ  . TYR B 1 284 ? 49.22400  -42.67100 3.70200   1.000 52.95000  ? 303  TYR B CZ  1 
ATOM   6149  O OH  . TYR B 1 284 ? 48.90100  -42.84100 5.03100   1.000 57.56000  ? 303  TYR B OH  1 
ATOM   6150  N N   . LEU B 1 285 ? 50.73000  -40.44900 -3.06500  1.000 41.29000  ? 304  LEU B N   1 
ATOM   6151  C CA  . LEU B 1 285 ? 51.24400  -40.50400 -4.42600  1.000 36.61000  ? 304  LEU B CA  1 
ATOM   6152  C C   . LEU B 1 285 ? 52.14000  -39.31300 -4.73400  1.000 39.34000  ? 304  LEU B C   1 
ATOM   6153  O O   . LEU B 1 285 ? 53.27100  -39.48100 -5.20100  1.000 40.38000  ? 304  LEU B O   1 
ATOM   6154  C CB  . LEU B 1 285 ? 50.08800  -40.58300 -5.41800  1.000 36.11000  ? 304  LEU B CB  1 
ATOM   6155  C CG  . LEU B 1 285 ? 50.60300  -40.66800 -6.85300  1.000 39.04000  ? 304  LEU B CG  1 
ATOM   6156  C CD1 . LEU B 1 285 ? 51.53400  -41.86100 -7.00400  1.000 35.77000  ? 304  LEU B CD1 1 
ATOM   6157  C CD2 . LEU B 1 285 ? 49.44400  -40.80400 -7.78600  1.000 39.87000  ? 304  LEU B CD2 1 
ATOM   6158  N N   . LEU B 1 286 ? 51.65700  -38.10000 -4.47000  1.000 40.40000  ? 305  LEU B N   1 
ATOM   6159  C CA  . LEU B 1 286 ? 52.37600  -36.88100 -4.84600  1.000 39.55000  ? 305  LEU B CA  1 
ATOM   6160  C C   . LEU B 1 286 ? 53.45100  -36.52100 -3.82200  1.000 41.41000  ? 305  LEU B C   1 
ATOM   6161  O O   . LEU B 1 286 ? 53.51800  -35.41600 -3.28200  1.000 41.68000  ? 305  LEU B O   1 
ATOM   6162  C CB  . LEU B 1 286 ? 51.39500  -35.73800 -5.06700  1.000 40.30000  ? 305  LEU B CB  1 
ATOM   6163  C CG  . LEU B 1 286 ? 50.77800  -35.87500 -6.45400  1.000 42.63000  ? 305  LEU B CG  1 
ATOM   6164  C CD1 . LEU B 1 286 ? 49.58500  -34.94100 -6.70700  1.000 40.65000  ? 305  LEU B CD1 1 
ATOM   6165  C CD2 . LEU B 1 286 ? 51.88800  -35.57600 -7.42300  1.000 32.95000  ? 305  LEU B CD2 1 
ATOM   6166  N N   . THR B 1 287 ? 54.32900  -37.49200 -3.59700  1.000 44.46000  ? 306  THR B N   1 
ATOM   6167  C CA  . THR B 1 287 ? 55.47900  -37.35600 -2.71700  1.000 43.25000  ? 306  THR B CA  1 
ATOM   6168  C C   . THR B 1 287 ? 56.64700  -38.03700 -3.40000  1.000 41.84000  ? 306  THR B C   1 
ATOM   6169  O O   . THR B 1 287 ? 56.45000  -38.87000 -4.28700  1.000 43.09000  ? 306  THR B O   1 
ATOM   6170  C CB  . THR B 1 287 ? 55.26200  -38.01500 -1.34800  1.000 42.49000  ? 306  THR B CB  1 
ATOM   6171  O OG1 . THR B 1 287 ? 55.15600  -39.43700 -1.51700  1.000 44.65000  ? 306  THR B OG1 1 
ATOM   6172  C CG2 . THR B 1 287 ? 53.99500  -37.50200 -0.69800  1.000 33.78000  ? 306  THR B CG2 1 
ATOM   6173  N N   . ASP B 1 288 ? 57.86600  -37.70300 -2.97000  1.000 41.31000  ? 307  ASP B N   1 
ATOM   6174  C CA  . ASP B 1 288 ? 59.03300  -38.33300 -3.57600  1.000 44.43000  ? 307  ASP B CA  1 
ATOM   6175  C C   . ASP B 1 288 ? 58.92000  -39.84500 -3.55700  1.000 47.00000  ? 307  ASP B C   1 
ATOM   6176  O O   . ASP B 1 288 ? 59.23400  -40.52400 -4.52400  1.000 44.34000  ? 307  ASP B O   1 
ATOM   6177  C CB  . ASP B 1 288 ? 60.31200  -37.92200 -2.85200  1.000 44.10000  ? 307  ASP B CB  1 
ATOM   6178  C CG  . ASP B 1 288 ? 60.61500  -36.44900 -2.97700  1.000 48.93000  ? 307  ASP B CG  1 
ATOM   6179  O OD1 . ASP B 1 288 ? 60.00000  -35.78300 -3.84000  1.000 44.28000  ? 307  ASP B OD1 1 
ATOM   6180  O OD2 . ASP B 1 288 ? 61.49900  -35.95100 -2.24500  1.000 53.08000  ? 307  ASP B OD2 1 
ATOM   6181  N N   . GLU B 1 289 ? 58.53600  -40.37500 -2.39900  1.000 42.81000  ? 308  GLU B N   1 
ATOM   6182  C CA  . GLU B 1 289 ? 58.44000  -41.84000 -2.16800  1.000 52.40000  ? 308  GLU B CA  1 
ATOM   6183  C C   . GLU B 1 289 ? 57.32500  -42.44300 -3.03100  1.000 45.27000  ? 308  GLU B C   1 
ATOM   6184  O O   . GLU B 1 289 ? 57.49700  -43.54800 -3.52400  1.000 35.64000  ? 308  GLU B O   1 
ATOM   6185  C CB  . GLU B 1 289 ? 58.36100  -42.12900 -0.66900  1.000 55.93000  ? 308  GLU B CB  1 
ATOM   6186  C CG  . GLU B 1 289 ? 57.43000  -41.19500 0.07400   1.000 66.26000  ? 308  GLU B CG  1 
ATOM   6187  C CD  . GLU B 1 289 ? 58.00700  -39.92800 0.68500   1.000 70.03000  ? 308  GLU B CD  1 
ATOM   6188  O OE1 . GLU B 1 289 ? 58.62800  -39.14900 -0.03700  1.000 68.08000  ? 308  GLU B OE1 1 
ATOM   6189  O OE2 . GLU B 1 289 ? 57.79700  -39.71200 1.88400   1.000 79.09000  ? 308  GLU B OE2 1 
ATOM   6190  N N   . GLY B 1 290 ? 56.20000  -41.74900 -3.13900  1.000 39.31000  ? 309  GLY B N   1 
ATOM   6191  C CA  . GLY B 1 290 ? 55.14000  -42.16800 -4.09300  1.000 38.39000  ? 309  GLY B CA  1 
ATOM   6192  C C   . GLY B 1 290 ? 55.49200  -42.24800 -5.58300  1.000 44.05000  ? 309  GLY B C   1 
ATOM   6193  O O   . GLY B 1 290 ? 55.35700  -43.31000 -6.20700  1.000 36.40000  ? 309  GLY B O   1 
ATOM   6194  N N   . LEU B 1 291 ? 55.90500  -41.11600 -6.15900  1.000 40.49000  ? 310  LEU B N   1 
ATOM   6195  C CA  . LEU B 1 291 ? 56.27600  -41.09700 -7.56700  1.000 36.09000  ? 310  LEU B CA  1 
ATOM   6196  C C   . LEU B 1 291 ? 57.42500  -42.05900 -7.84900  1.000 37.78000  ? 310  LEU B C   1 
ATOM   6197  O O   . LEU B 1 291 ? 57.42400  -42.75400 -8.87100  1.000 39.27000  ? 310  LEU B O   1 
ATOM   6198  C CB  . LEU B 1 291 ? 56.63800  -39.67900 -7.98800  1.000 27.52000  ? 310  LEU B CB  1 
ATOM   6199  C CG  . LEU B 1 291 ? 55.49400  -38.66200 -7.94700  1.000 33.37000  ? 310  LEU B CG  1 
ATOM   6200  C CD1 . LEU B 1 291 ? 55.97300  -37.28000 -8.35300  1.000 30.20000  ? 310  LEU B CD1 1 
ATOM   6201  C CD2 . LEU B 1 291 ? 54.31200  -39.10900 -8.81300  1.000 31.44000  ? 310  LEU B CD2 1 
ATOM   6202  N N   . GLU B 1 292 ? 58.41300  -42.12000 -6.95300  1.000 37.99000  ? 311  GLU B N   1 
ATOM   6203  C CA  . GLU B 1 292 ? 59.51100  -43.06600 -7.12900  1.000 41.83000  ? 311  GLU B CA  1 
ATOM   6204  C C   . GLU B 1 292 ? 59.00900  -44.49700 -7.26600  1.000 41.99000  ? 311  GLU B C   1 
ATOM   6205  O O   . GLU B 1 292 ? 59.51600  -45.26200 -8.09800  1.000 37.26000  ? 311  GLU B O   1 
ATOM   6206  C CB  . GLU B 1 292 ? 60.48300  -42.96700 -5.95900  1.000 48.44000  ? 311  GLU B CB  1 
ATOM   6207  C CG  . GLU B 1 292 ? 61.54800  -44.03800 -5.97000  1.000 48.11000  ? 311  GLU B CG  1 
ATOM   6208  C CD  . GLU B 1 292 ? 62.50200  -43.88600 -4.82200  1.000 64.30000  ? 311  GLU B CD  1 
ATOM   6209  O OE1 . GLU B 1 292 ? 62.39400  -42.86800 -4.10100  1.000 68.60000  ? 311  GLU B OE1 1 
ATOM   6210  O OE2 . GLU B 1 292 ? 63.32900  -44.80100 -4.61300  1.000 80.27000  ? 311  GLU B OE2 1 
ATOM   6211  N N   . ALA B 1 293 ? 58.01700  -44.87800 -6.45700  1.000 37.79000  ? 312  ALA B N   1 
ATOM   6212  C CA  . ALA B 1 293 ? 57.47000  -46.22800 -6.54300  1.000 39.85000  ? 312  ALA B CA  1 
ATOM   6213  C C   . ALA B 1 293 ? 56.83500  -46.47800 -7.90400  1.000 41.66000  ? 312  ALA B C   1 
ATOM   6214  O O   . ALA B 1 293 ? 56.99400  -47.55900 -8.48600  1.000 41.25000  ? 312  ALA B O   1 
ATOM   6215  C CB  . ALA B 1 293 ? 56.44900  -46.45100 -5.42700  1.000 38.49000  ? 312  ALA B CB  1 
ATOM   6216  N N   . VAL B 1 294 ? 56.10300  -45.49600 -8.42400  1.000 36.04000  ? 313  VAL B N   1 
ATOM   6217  C CA  . VAL B 1 294 ? 55.57000  -45.61900 -9.77300  1.000 36.92000  ? 313  VAL B CA  1 
ATOM   6218  C C   . VAL B 1 294 ? 56.70600  -45.61600 -10.78100 1.000 42.07000  ? 313  VAL B C   1 
ATOM   6219  O O   . VAL B 1 294 ? 56.75100  -46.44500 -11.69500 1.000 41.65000  ? 313  VAL B O   1 
ATOM   6220  C CB  . VAL B 1 294 ? 54.58200  -44.48200 -10.06500 1.000 31.05000  ? 313  VAL B CB  1 
ATOM   6221  C CG1 . VAL B 1 294 ? 54.09200  -44.58500 -11.50100 1.000 34.31000  ? 313  VAL B CG1 1 
ATOM   6222  C CG2 . VAL B 1 294 ? 53.45100  -44.50600 -9.07700  1.000 30.81000  ? 313  VAL B CG2 1 
ATOM   6223  N N   . ASN B 1 295 ? 57.64200  -44.67300 -10.61300 1.000 40.03000  ? 314  ASN B N   1 
ATOM   6224  C CA  . ASN B 1 295 ? 58.74700  -44.48500 -11.54400 1.000 37.47000  ? 314  ASN B CA  1 
ATOM   6225  C C   . ASN B 1 295 ? 59.54700  -45.76600 -11.70500 1.000 38.62000  ? 314  ASN B C   1 
ATOM   6226  O O   . ASN B 1 295 ? 59.89600  -46.16700 -12.81800 1.000 42.57000  ? 314  ASN B O   1 
ATOM   6227  C CB  . ASN B 1 295 ? 59.68700  -43.40400 -11.02000 1.000 38.96000  ? 314  ASN B CB  1 
ATOM   6228  C CG  . ASN B 1 295 ? 60.61800  -42.89200 -12.07600 1.000 38.16000  ? 314  ASN B CG  1 
ATOM   6229  O OD1 . ASN B 1 295 ? 60.30000  -42.89300 -13.25400 1.000 43.77000  ? 314  ASN B OD1 1 
ATOM   6230  N ND2 . ASN B 1 295 ? 61.83500  -42.57700 -11.67100 1.000 52.09000  ? 314  ASN B ND2 1 
ATOM   6231  N N   . LYS B 1 296 ? 59.88700  -46.39200 -10.58200 1.000 38.83000  ? 315  LYS B N   1 
ATOM   6232  C CA  . LYS B 1 296 ? 60.68000  -47.61000 -10.60400 1.000 42.41000  ? 315  LYS B CA  1 
ATOM   6233  C C   . LYS B 1 296 ? 60.02200  -48.69500 -11.43300 1.000 46.12000  ? 315  LYS B C   1 
ATOM   6234  O O   . LYS B 1 296 ? 60.72200  -49.47600 -12.07800 1.000 46.12000  ? 315  LYS B O   1 
ATOM   6235  C CB  . LYS B 1 296 ? 60.90100  -48.10300 -9.18100  1.000 40.43000  ? 315  LYS B CB  1 
ATOM   6236  C CG  . LYS B 1 296 ? 61.91900  -47.30900 -8.40400  1.000 52.86000  ? 315  LYS B CG  1 
ATOM   6237  C CD  . LYS B 1 296 ? 61.82600  -47.67300 -6.93400  1.000 63.22000  ? 315  LYS B CD  1 
ATOM   6238  C CE  . LYS B 1 296 ? 62.56300  -48.96500 -6.61300  1.000 73.02000  ? 315  LYS B CE  1 
ATOM   6239  N NZ  . LYS B 1 296 ? 61.85100  -50.18400 -7.10200  1.000 76.73000  ? 315  LYS B NZ  1 
ATOM   6240  N N   . ASP B 1 297 ? 58.68900  -48.75500 -11.44000 1.000 38.97000  ? 316  ASP B N   1 
ATOM   6241  C CA  . ASP B 1 297 ? 57.99400  -49.73400 -12.27200 1.000 42.90000  ? 316  ASP B CA  1 
ATOM   6242  C C   . ASP B 1 297 ? 58.19500  -49.42400 -13.75200 1.000 43.29000  ? 316  ASP B C   1 
ATOM   6243  O O   . ASP B 1 297 ? 58.71600  -50.25100 -14.51000 1.000 48.30000  ? 316  ASP B O   1 
ATOM   6244  C CB  . ASP B 1 297 ? 56.49900  -49.75900 -11.92700 1.000 43.80000  ? 316  ASP B CB  1 
ATOM   6245  C CG  . ASP B 1 297 ? 55.76700  -50.93000 -12.57200 1.000 45.65000  ? 316  ASP B CG  1 
ATOM   6246  O OD1 . ASP B 1 297 ? 56.42000  -51.76600 -13.22600 1.000 50.71000  ? 316  ASP B OD1 1 
ATOM   6247  O OD2 . ASP B 1 297 ? 54.53100  -51.00800 -12.44600 1.000 44.56000  ? 316  ASP B OD2 1 
ATOM   6248  N N   . LYS B 1 298 ? 57.76000  -48.23800 -14.18300 1.000 40.57000  ? 317  LYS B N   1 
ATOM   6249  C CA  . LYS B 1 298 ? 57.97200  -47.72400 -15.53000 1.000 44.08000  ? 317  LYS B CA  1 
ATOM   6250  C C   . LYS B 1 298 ? 58.16200  -46.21700 -15.42600 1.000 46.30000  ? 317  LYS B C   1 
ATOM   6251  O O   . LYS B 1 298 ? 57.34700  -45.53600 -14.77600 1.000 44.45000  ? 317  LYS B O   1 
ATOM   6252  C CB  . LYS B 1 298 ? 56.82900  -48.07000 -16.48800 1.000 39.69000  ? 317  LYS B CB  1 
ATOM   6253  C CG  . LYS B 1 298 ? 57.01800  -49.44500 -17.12100 1.000 49.06000  ? 317  LYS B CG  1 
ATOM   6254  C CD  . LYS B 1 298 ? 55.87600  -49.87400 -18.02900 1.000 56.10000  ? 317  LYS B CD  1 
ATOM   6255  C CE  . LYS B 1 298 ? 54.76100  -50.48100 -17.18300 1.000 52.38000  ? 317  LYS B CE  1 
ATOM   6256  N NZ  . LYS B 1 298 ? 53.67600  -51.09100 -17.99300 1.000 50.12000  ? 317  LYS B NZ  1 
ATOM   6257  N N   . PRO B 1 299 ? 59.20500  -45.67700 -16.05500 1.000 41.77000  ? 318  PRO B N   1 
ATOM   6258  C CA  . PRO B 1 299 ? 59.57400  -44.27400 -15.82800 1.000 42.28000  ? 318  PRO B CA  1 
ATOM   6259  C C   . PRO B 1 299 ? 58.44300  -43.32000 -16.18800 1.000 41.41000  ? 318  PRO B C   1 
ATOM   6260  O O   . PRO B 1 299 ? 57.83800  -43.41700 -17.25700 1.000 43.62000  ? 318  PRO B O   1 
ATOM   6261  C CB  . PRO B 1 299 ? 60.78600  -44.07300 -16.74800 1.000 34.75000  ? 318  PRO B CB  1 
ATOM   6262  C CG  . PRO B 1 299 ? 61.26500  -45.44900 -17.06500 1.000 39.01000  ? 318  PRO B CG  1 
ATOM   6263  C CD  . PRO B 1 299 ? 60.05600  -46.31500 -17.07100 1.000 35.83000  ? 318  PRO B CD  1 
ATOM   6264  N N   . LEU B 1 300 ? 58.17800  -42.37400 -15.29000 1.000 40.15000  ? 319  LEU B N   1 
ATOM   6265  C CA  . LEU B 1 300 ? 57.18800  -41.34300 -15.55700 1.000 39.47000  ? 319  LEU B CA  1 
ATOM   6266  C C   . LEU B 1 300 ? 57.67500  -40.29600 -16.54900 1.000 41.59000  ? 319  LEU B C   1 
ATOM   6267  O O   . LEU B 1 300 ? 56.85000  -39.53700 -17.06800 1.000 41.29000  ? 319  LEU B O   1 
ATOM   6268  C CB  . LEU B 1 300 ? 56.78800  -40.64600 -14.25600 1.000 30.81000  ? 319  LEU B CB  1 
ATOM   6269  C CG  . LEU B 1 300 ? 56.03100  -41.50200 -13.24800 1.000 34.34000  ? 319  LEU B CG  1 
ATOM   6270  C CD1 . LEU B 1 300 ? 55.83900  -40.74900 -11.93500 1.000 28.13000  ? 319  LEU B CD1 1 
ATOM   6271  C CD2 . LEU B 1 300 ? 54.69600  -41.92400 -13.83900 1.000 36.12000  ? 319  LEU B CD2 1 
ATOM   6272  N N   . GLY B 1 301 ? 58.98100  -40.24100 -16.83100 1.000 34.86000  ? 320  GLY B N   1 
ATOM   6273  C CA  . GLY B 1 301 ? 59.54400  -39.12000 -17.56000 1.000 30.01000  ? 320  GLY B CA  1 
ATOM   6274  C C   . GLY B 1 301 ? 59.80600  -37.95900 -16.62700 1.000 33.65000  ? 320  GLY B C   1 
ATOM   6275  O O   . GLY B 1 301 ? 60.22900  -38.17000 -15.48800 1.000 34.11000  ? 320  GLY B O   1 
ATOM   6276  N N   . ALA B 1 302 ? 59.58600  -36.73400 -17.09500 1.000 33.78000  ? 321  ALA B N   1 
ATOM   6277  C CA  . ALA B 1 302 ? 59.58500  -35.58500 -16.20000 1.000 36.18000  ? 321  ALA B CA  1 
ATOM   6278  C C   . ALA B 1 302 ? 58.31100  -35.59400 -15.35800 1.000 38.50000  ? 321  ALA B C   1 
ATOM   6279  O O   . ALA B 1 302 ? 57.27400  -36.12500 -15.77100 1.000 39.07000  ? 321  ALA B O   1 
ATOM   6280  C CB  . ALA B 1 302 ? 59.69700  -34.28200 -16.99900 1.000 30.79000  ? 321  ALA B CB  1 
ATOM   6281  N N   . VAL B 1 303 ? 58.39000  -35.01600 -14.15800 1.000 37.16000  ? 322  VAL B N   1 
ATOM   6282  C CA  . VAL B 1 303 ? 57.26100  -35.04900 -13.23700 1.000 31.19000  ? 322  VAL B CA  1 
ATOM   6283  C C   . VAL B 1 303 ? 56.91100  -33.63600 -12.78400 1.000 30.85000  ? 322  VAL B C   1 
ATOM   6284  O O   . VAL B 1 303 ? 57.73000  -32.71600 -12.80800 1.000 36.96000  ? 322  VAL B O   1 
ATOM   6285  C CB  . VAL B 1 303 ? 57.53300  -35.96300 -12.03000 1.000 36.34000  ? 322  VAL B CB  1 
ATOM   6286  C CG1 . VAL B 1 303 ? 57.73100  -37.39200 -12.50300 1.000 37.39000  ? 322  VAL B CG1 1 
ATOM   6287  C CG2 . VAL B 1 303 ? 58.74500  -35.48400 -11.24700 1.000 37.99000  ? 322  VAL B CG2 1 
ATOM   6288  N N   . ALA B 1 304 ? 55.66100  -33.47200 -12.37300 1.000 32.74000  ? 323  ALA B N   1 
ATOM   6289  C CA  . ALA B 1 304 ? 55.16700  -32.16500 -11.96000 1.000 37.39000  ? 323  ALA B CA  1 
ATOM   6290  C C   . ALA B 1 304 ? 55.63200  -31.77000 -10.56500 1.000 35.90000  ? 323  ALA B C   1 
ATOM   6291  O O   . ALA B 1 304 ? 55.58000  -30.58200 -10.22200 1.000 35.27000  ? 323  ALA B O   1 
ATOM   6292  C CB  . ALA B 1 304 ? 53.63500  -32.14200 -12.01100 1.000 35.51000  ? 323  ALA B CB  1 
ATOM   6293  N N   . LEU B 1 305 ? 56.08600  -32.73000 -9.76200  1.000 30.81000  ? 324  LEU B N   1 
ATOM   6294  C CA  . LEU B 1 305 ? 56.48700  -32.46400 -8.38400  1.000 35.39000  ? 324  LEU B CA  1 
ATOM   6295  C C   . LEU B 1 305 ? 57.92200  -31.95400 -8.38800  1.000 37.28000  ? 324  LEU B C   1 
ATOM   6296  O O   . LEU B 1 305 ? 58.83900  -32.67700 -8.79200  1.000 37.29000  ? 324  LEU B O   1 
ATOM   6297  C CB  . LEU B 1 305 ? 56.35100  -33.73200 -7.55000  1.000 32.22000  ? 324  LEU B CB  1 
ATOM   6298  C CG  . LEU B 1 305 ? 56.57400  -33.60300 -6.05200  1.000 36.97000  ? 324  LEU B CG  1 
ATOM   6299  C CD1 . LEU B 1 305 ? 55.52100  -32.68000 -5.46200  1.000 36.57000  ? 324  LEU B CD1 1 
ATOM   6300  C CD2 . LEU B 1 305 ? 56.49100  -34.98400 -5.44100  1.000 32.88000  ? 324  LEU B CD2 1 
ATOM   6301  N N   . LYS B 1 306 ? 58.11700  -30.71200 -7.93400  1.000 34.48000  ? 325  LYS B N   1 
ATOM   6302  C CA  . LYS B 1 306 ? 59.41800  -30.06100 -8.05200  1.000 34.15000  ? 325  LYS B CA  1 
ATOM   6303  C C   . LYS B 1 306 ? 60.51700  -30.86900 -7.38100  1.000 40.83000  ? 325  LYS B C   1 
ATOM   6304  O O   . LYS B 1 306 ? 61.59300  -31.07000 -7.95500  1.000 42.05000  ? 325  LYS B O   1 
ATOM   6305  C CB  . LYS B 1 306 ? 59.35800  -28.66600 -7.44600  1.000 29.41000  ? 325  LYS B CB  1 
ATOM   6306  C CG  . LYS B 1 306 ? 58.49000  -27.71100 -8.21100  1.000 34.41000  ? 325  LYS B CG  1 
ATOM   6307  C CD  . LYS B 1 306 ? 58.49000  -26.38700 -7.50500  1.000 37.15000  ? 325  LYS B CD  1 
ATOM   6308  C CE  . LYS B 1 306 ? 57.56600  -25.41100 -8.16700  1.000 42.03000  ? 325  LYS B CE  1 
ATOM   6309  N NZ  . LYS B 1 306 ? 57.52000  -24.16400 -7.36500  1.000 46.50000  ? 325  LYS B NZ  1 
ATOM   6310  N N   . SER B 1 307 ? 60.26000  -31.34600 -6.16200  1.000 36.41000  ? 326  SER B N   1 
ATOM   6311  C CA  . SER B 1 307 ? 61.29600  -32.03900 -5.40600  1.000 39.17000  ? 326  SER B CA  1 
ATOM   6312  C C   . SER B 1 307 ? 61.78000  -33.28300 -6.14800  1.000 40.34000  ? 326  SER B C   1 
ATOM   6313  O O   . SER B 1 307 ? 62.98300  -33.45200 -6.37100  1.000 45.39000  ? 326  SER B O   1 
ATOM   6314  C CB  . SER B 1 307 ? 60.78500  -32.38300 -3.99700  1.000 38.93000  ? 326  SER B CB  1 
ATOM   6315  O OG  . SER B 1 307 ? 59.72300  -33.33400 -3.99500  1.000 33.09000  ? 326  SER B OG  1 
ATOM   6316  N N   . TYR B 1 308 ? 60.85800  -34.14800 -6.57700  1.000 38.92000  ? 327  TYR B N   1 
ATOM   6317  C CA  . TYR B 1 308 ? 61.30100  -35.37400 -7.23000  1.000 42.52000  ? 327  TYR B CA  1 
ATOM   6318  C C   . TYR B 1 308 ? 61.83900  -35.10300 -8.63300  1.000 44.67000  ? 327  TYR B C   1 
ATOM   6319  O O   . TYR B 1 308 ? 62.75000  -35.80500 -9.08900  1.000 40.06000  ? 327  TYR B O   1 
ATOM   6320  C CB  . TYR B 1 308 ? 60.16900  -36.39900 -7.25200  1.000 35.30000  ? 327  TYR B CB  1 
ATOM   6321  C CG  . TYR B 1 308 ? 60.60700  -37.76600 -7.72800  1.000 39.20000  ? 327  TYR B CG  1 
ATOM   6322  C CD1 . TYR B 1 308 ? 61.63600  -38.43900 -7.07900  1.000 35.12000  ? 327  TYR B CD1 1 
ATOM   6323  C CD2 . TYR B 1 308 ? 59.93300  -38.42700 -8.74900  1.000 35.81000  ? 327  TYR B CD2 1 
ATOM   6324  C CE1 . TYR B 1 308 ? 62.04100  -39.70100 -7.48000  1.000 30.91000  ? 327  TYR B CE1 1 
ATOM   6325  C CE2 . TYR B 1 308 ? 60.32300  -39.69700 -9.15400  1.000 39.89000  ? 327  TYR B CE2 1 
ATOM   6326  C CZ  . TYR B 1 308 ? 61.38200  -40.32700 -8.51200  1.000 45.16000  ? 327  TYR B CZ  1 
ATOM   6327  O OH  . TYR B 1 308 ? 61.77600  -41.58700 -8.90100  1.000 46.05000  ? 327  TYR B OH  1 
ATOM   6328  N N   . GLU B 1 309 ? 61.31400  -34.08300 -9.32200  1.000 40.40000  ? 328  GLU B N   1 
ATOM   6329  C CA  . GLU B 1 309 ? 61.83200  -33.73300 -10.64500 1.000 44.30000  ? 328  GLU B CA  1 
ATOM   6330  C C   . GLU B 1 309 ? 63.29500  -33.31600 -10.57200 1.000 42.72000  ? 328  GLU B C   1 
ATOM   6331  O O   . GLU B 1 309 ? 64.08500  -33.64900 -11.46000 1.000 42.19000  ? 328  GLU B O   1 
ATOM   6332  C CB  . GLU B 1 309 ? 60.96600  -32.63100 -11.27400 1.000 38.51000  ? 328  GLU B CB  1 
ATOM   6333  C CG  . GLU B 1 309 ? 61.48600  -31.99000 -12.56100 1.000 34.24000  ? 328  GLU B CG  1 
ATOM   6334  C CD  . GLU B 1 309 ? 61.68200  -32.96000 -13.71800 1.000 40.64000  ? 328  GLU B CD  1 
ATOM   6335  O OE1 . GLU B 1 309 ? 61.06300  -34.04200 -13.73100 1.000 46.16000  ? 328  GLU B OE1 1 
ATOM   6336  O OE2 . GLU B 1 309 ? 62.45800  -32.62400 -14.63600 1.000 37.33000  ? 328  GLU B OE2 1 
ATOM   6337  N N   . GLU B 1 310 ? 63.67400  -32.59200 -9.52000  1.000 45.03000  ? 329  GLU B N   1 
ATOM   6338  C CA  . GLU B 1 310 ? 65.06600  -32.19100 -9.36400  1.000 46.10000  ? 329  GLU B CA  1 
ATOM   6339  C C   . GLU B 1 310 ? 65.97800  -33.39600 -9.20800  1.000 46.47000  ? 329  GLU B C   1 
ATOM   6340  O O   . GLU B 1 310 ? 67.13600  -33.36400 -9.64100  1.000 46.43000  ? 329  GLU B O   1 
ATOM   6341  C CB  . GLU B 1 310 ? 65.19500  -31.25200 -8.17000  1.000 44.61000  ? 329  GLU B CB  1 
ATOM   6342  C CG  . GLU B 1 310 ? 64.51700  -29.93300 -8.44500  1.000 51.54000  ? 329  GLU B CG  1 
ATOM   6343  C CD  . GLU B 1 310 ? 64.40600  -29.05800 -7.21900  1.000 56.64000  ? 329  GLU B CD  1 
ATOM   6344  O OE1 . GLU B 1 310 ? 64.82000  -29.50800 -6.12800  1.000 73.10000  ? 329  GLU B OE1 1 
ATOM   6345  O OE2 . GLU B 1 310 ? 63.82200  -27.95400 -7.33100  1.000 63.34000  ? 329  GLU B OE2 1 
ATOM   6346  N N   . GLU B 1 311 ? 65.48600  -34.46500 -8.59200  1.000 44.28000  ? 330  GLU B N   1 
ATOM   6347  C CA  . GLU B 1 311 ? 66.31800  -35.65300 -8.50000  1.000 42.69000  ? 330  GLU B CA  1 
ATOM   6348  C C   . GLU B 1 311 ? 66.38800  -36.36800 -9.84600  1.000 45.48000  ? 330  GLU B C   1 
ATOM   6349  O O   . GLU B 1 311 ? 67.47200  -36.77500 -10.28500 1.000 46.71000  ? 330  GLU B O   1 
ATOM   6350  C CB  . GLU B 1 311 ? 65.79100  -36.57900 -7.41000  1.000 45.95000  ? 330  GLU B CB  1 
ATOM   6351  C CG  . GLU B 1 311 ? 66.87900  -37.50100 -6.92600  1.000 43.99000  ? 330  GLU B CG  1 
ATOM   6352  C CD  . GLU B 1 311 ? 67.98100  -36.70200 -6.25000  1.000 66.00000  ? 330  GLU B CD  1 
ATOM   6353  O OE1 . GLU B 1 311 ? 67.65400  -35.63700 -5.66800  1.000 60.21000  ? 330  GLU B OE1 1 
ATOM   6354  O OE2 . GLU B 1 311 ? 69.17000  -37.09200 -6.36000  1.000 76.30000  ? 330  GLU B OE2 1 
ATOM   6355  N N   . LEU B 1 312 ? 65.24300  -36.49400 -10.52800 1.000 38.63000  ? 331  LEU B N   1 
ATOM   6356  C CA  . LEU B 1 312 ? 65.21200  -37.14600 -11.83300 1.000 35.46000  ? 331  LEU B CA  1 
ATOM   6357  C C   . LEU B 1 312 ? 66.03200  -36.38100 -12.85900 1.000 37.06000  ? 331  LEU B C   1 
ATOM   6358  O O   . LEU B 1 312 ? 66.69000  -36.99000 -13.71100 1.000 38.25000  ? 331  LEU B O   1 
ATOM   6359  C CB  . LEU B 1 312 ? 63.77600  -37.28200 -12.32600 1.000 37.36000  ? 331  LEU B CB  1 
ATOM   6360  C CG  . LEU B 1 312 ? 62.86500  -38.23600 -11.57400 1.000 38.44000  ? 331  LEU B CG  1 
ATOM   6361  C CD1 . LEU B 1 312 ? 61.48500  -38.20200 -12.20500 1.000 36.73000  ? 331  LEU B CD1 1 
ATOM   6362  C CD2 . LEU B 1 312 ? 63.45100  -39.63400 -11.59000 1.000 33.40000  ? 331  LEU B CD2 1 
ATOM   6363  N N   . ALA B 1 313 ? 66.00100  -35.04500 -12.80100 1.000 36.77000  ? 332  ALA B N   1 
ATOM   6364  C CA  . ALA B 1 313 ? 66.62000  -34.22000 -13.83500 1.000 39.57000  ? 332  ALA B CA  1 
ATOM   6365  C C   . ALA B 1 313 ? 68.14100  -34.31200 -13.85000 1.000 44.73000  ? 332  ALA B C   1 
ATOM   6366  O O   . ALA B 1 313 ? 68.76700  -33.72000 -14.73500 1.000 47.93000  ? 332  ALA B O   1 
ATOM   6367  C CB  . ALA B 1 313 ? 66.19700  -32.76000 -13.66400 1.000 42.88000  ? 332  ALA B CB  1 
ATOM   6368  N N   . LYS B 1 314 ? 68.75100  -35.02100 -12.89500 1.000 43.78000  ? 333  LYS B N   1 
ATOM   6369  C CA  . LYS B 1 314 ? 70.16000  -35.36800 -13.03300 1.000 44.60000  ? 333  LYS B CA  1 
ATOM   6370  C C   . LYS B 1 314 ? 70.40400  -36.16200 -14.31300 1.000 46.65000  ? 333  LYS B C   1 
ATOM   6371  O O   . LYS B 1 314 ? 71.52000  -36.15000 -14.84700 1.000 52.93000  ? 333  LYS B O   1 
ATOM   6372  C CB  . LYS B 1 314 ? 70.62900  -36.14700 -11.80400 1.000 51.57000  ? 333  LYS B CB  1 
ATOM   6373  C CG  . LYS B 1 314 ? 70.65000  -35.31200 -10.50900 1.000 60.30000  ? 333  LYS B CG  1 
ATOM   6374  C CD  . LYS B 1 314 ? 71.06700  -36.14800 -9.30600  1.000 61.45000  ? 333  LYS B CD  1 
ATOM   6375  C CE  . LYS B 1 314 ? 71.22600  -35.29300 -8.06600  1.000 63.29000  ? 333  LYS B CE  1 
ATOM   6376  N NZ  . LYS B 1 314 ? 69.92500  -34.75800 -7.61600  1.000 58.73000  ? 333  LYS B NZ  1 
ATOM   6377  N N   . ASP B 1 315 ? 69.37800  -36.85200 -14.81700 1.000 39.78000  ? 334  ASP B N   1 
ATOM   6378  C CA  . ASP B 1 315 ? 69.41400  -37.40000 -16.16800 1.000 37.96000  ? 334  ASP B CA  1 
ATOM   6379  C C   . ASP B 1 315 ? 69.16300  -36.27800 -17.17100 1.000 37.87000  ? 334  ASP B C   1 
ATOM   6380  O O   . ASP B 1 315 ? 68.08200  -35.67900 -17.15900 1.000 40.53000  ? 334  ASP B O   1 
ATOM   6381  C CB  . ASP B 1 315 ? 68.37000  -38.50800 -16.31700 1.000 33.44000  ? 334  ASP B CB  1 
ATOM   6382  C CG  . ASP B 1 315 ? 68.37500  -39.15900 -17.70200 1.000 40.05000  ? 334  ASP B CG  1 
ATOM   6383  O OD1 . ASP B 1 315 ? 69.08900  -38.67400 -18.61300 1.000 39.14000  ? 334  ASP B OD1 1 
ATOM   6384  O OD2 . ASP B 1 315 ? 67.66300  -40.17800 -17.88100 1.000 35.60000  ? 334  ASP B OD2 1 
ATOM   6385  N N   . PRO B 1 316 ? 70.11700  -35.95800 -18.04200 1.000 38.44000  ? 335  PRO B N   1 
ATOM   6386  C CA  . PRO B 1 316 ? 69.90000  -34.83700 -18.96800 1.000 33.90000  ? 335  PRO B CA  1 
ATOM   6387  C C   . PRO B 1 316 ? 68.76000  -35.07200 -19.94600 1.000 38.29000  ? 335  PRO B C   1 
ATOM   6388  O O   . PRO B 1 316 ? 68.18400  -34.09600 -20.44800 1.000 36.65000  ? 335  PRO B O   1 
ATOM   6389  C CB  . PRO B 1 316 ? 71.25400  -34.69900 -19.67600 1.000 32.38000  ? 335  PRO B CB  1 
ATOM   6390  C CG  . PRO B 1 316 ? 71.90900  -36.05000 -19.51100 1.000 35.03000  ? 335  PRO B CG  1 
ATOM   6391  C CD  . PRO B 1 316 ? 71.45500  -36.56400 -18.19300 1.000 35.30000  ? 335  PRO B CD  1 
ATOM   6392  N N   . ARG B 1 317 ? 68.40400  -36.33000 -20.22500 1.000 36.20000  ? 336  ARG B N   1 
ATOM   6393  C CA  . ARG B 1 317 ? 67.25200  -36.58900 -21.07900 1.000 31.35000  ? 336  ARG B CA  1 
ATOM   6394  C C   . ARG B 1 317 ? 65.97900  -36.06100 -20.43200 1.000 36.20000  ? 336  ARG B C   1 
ATOM   6395  O O   . ARG B 1 317 ? 65.16800  -35.38900 -21.08200 1.000 33.12000  ? 336  ARG B O   1 
ATOM   6396  C CB  . ARG B 1 317 ? 67.13000  -38.08600 -21.35500 1.000 30.73000  ? 336  ARG B CB  1 
ATOM   6397  C CG  . ARG B 1 317 ? 68.35000  -38.72800 -22.02500 1.000 31.34000  ? 336  ARG B CG  1 
ATOM   6398  C CD  . ARG B 1 317 ? 68.08700  -40.21400 -22.20200 1.000 29.50000  ? 336  ARG B CD  1 
ATOM   6399  N NE  . ARG B 1 317 ? 67.89300  -40.83400 -20.89800 1.000 37.23000  ? 336  ARG B NE  1 
ATOM   6400  C CZ  . ARG B 1 317 ? 67.40500  -42.04900 -20.69800 1.000 37.75000  ? 336  ARG B CZ  1 
ATOM   6401  N NH1 . ARG B 1 317 ? 67.06100  -42.83200 -21.70900 1.000 36.65000  ? 336  ARG B NH1 1 
ATOM   6402  N NH2 . ARG B 1 317 ? 67.23600  -42.48200 -19.45200 1.000 33.84000  ? 336  ARG B NH2 1 
ATOM   6403  N N   . ILE B 1 318 ? 65.80400  -36.32900 -19.13700 1.000 37.76000  ? 337  ILE B N   1 
ATOM   6404  C CA  . ILE B 1 318 ? 64.62800  -35.83500 -18.43400 1.000 34.00000  ? 337  ILE B CA  1 
ATOM   6405  C C   . ILE B 1 318 ? 64.67500  -34.32000 -18.32200 1.000 35.86000  ? 337  ILE B C   1 
ATOM   6406  O O   . ILE B 1 318 ? 63.65900  -33.63800 -18.50800 1.000 36.60000  ? 337  ILE B O   1 
ATOM   6407  C CB  . ILE B 1 318 ? 64.50700  -36.51200 -17.05600 1.000 36.48000  ? 337  ILE B CB  1 
ATOM   6408  C CG1 . ILE B 1 318 ? 64.17900  -37.99900 -17.23200 1.000 35.76000  ? 337  ILE B CG1 1 
ATOM   6409  C CG2 . ILE B 1 318 ? 63.47400  -35.79600 -16.17800 1.000 34.28000  ? 337  ILE B CG2 1 
ATOM   6410  C CD1 . ILE B 1 318 ? 64.32500  -38.80300 -15.96500 1.000 41.42000  ? 337  ILE B CD1 1 
ATOM   6411  N N   . ALA B 1 319 ? 65.85500  -33.76700 -18.03700 1.000 34.22000  ? 338  ALA B N   1 
ATOM   6412  C CA  . ALA B 1 319 ? 65.98600  -32.31700 -17.94600 1.000 35.77000  ? 338  ALA B CA  1 
ATOM   6413  C C   . ALA B 1 319 ? 65.56000  -31.65300 -19.24400 1.000 35.48000  ? 338  ALA B C   1 
ATOM   6414  O O   . ALA B 1 319 ? 64.91200  -30.59800 -19.23100 1.000 35.51000  ? 338  ALA B O   1 
ATOM   6415  C CB  . ALA B 1 319 ? 67.42600  -31.93500 -17.60300 1.000 29.91000  ? 338  ALA B CB  1 
ATOM   6416  N N   . ALA B 1 320 ? 65.91200  -32.26200 -20.37600 1.000 33.26000  ? 339  ALA B N   1 
ATOM   6417  C CA  . ALA B 1 320 ? 65.53100  -31.70800 -21.66700 1.000 33.53000  ? 339  ALA B CA  1 
ATOM   6418  C C   . ALA B 1 320 ? 64.02400  -31.78200 -21.88500 1.000 34.66000  ? 339  ALA B C   1 
ATOM   6419  O O   . ALA B 1 320 ? 63.41300  -30.82600 -22.38300 1.000 32.13000  ? 339  ALA B O   1 
ATOM   6420  C CB  . ALA B 1 320 ? 66.27600  -32.44100 -22.77400 1.000 32.46000  ? 339  ALA B CB  1 
ATOM   6421  N N   . THR B 1 321 ? 63.40600  -32.91100 -21.53000 1.000 31.79000  ? 340  THR B N   1 
ATOM   6422  C CA  . THR B 1 321 ? 61.96300  -33.03400 -21.69000 1.000 31.32000  ? 340  THR B CA  1 
ATOM   6423  C C   . THR B 1 321 ? 61.25000  -31.91800 -20.94400 1.000 31.62000  ? 340  THR B C   1 
ATOM   6424  O O   . THR B 1 321 ? 60.34900  -31.26400 -21.48100 1.000 32.58000  ? 340  THR B O   1 
ATOM   6425  C CB  . THR B 1 321 ? 61.48500  -34.39100 -21.18000 1.000 31.81000  ? 340  THR B CB  1 
ATOM   6426  O OG1 . THR B 1 321 ? 62.20200  -35.43500 -21.85000 1.000 29.91000  ? 340  THR B OG1 1 
ATOM   6427  C CG2 . THR B 1 321 ? 59.97200  -34.54600 -21.43400 1.000 23.27000  ? 340  THR B CG2 1 
ATOM   6428  N N   . MET B 1 322 ? 61.66400  -31.67400 -19.70100 1.000 31.54000  ? 341  MET B N   1 
ATOM   6429  C CA  . MET B 1 322 ? 61.08200  -30.58900 -18.92500 1.000 32.40000  ? 341  MET B CA  1 
ATOM   6430  C C   . MET B 1 322 ? 61.35500  -29.24400 -19.57700 1.000 33.13000  ? 341  MET B C   1 
ATOM   6431  O O   . MET B 1 322 ? 60.46100  -28.39400 -19.65100 1.000 37.35000  ? 341  MET B O   1 
ATOM   6432  C CB  . MET B 1 322 ? 61.62100  -30.62900 -17.49400 1.000 34.51000  ? 341  MET B CB  1 
ATOM   6433  C CG  . MET B 1 322 ? 61.11000  -29.51700 -16.60300 1.000 31.81000  ? 341  MET B CG  1 
ATOM   6434  S SD  . MET B 1 322 ? 59.31000  -29.51600 -16.53200 1.000 40.92000  ? 341  MET B SD  1 
ATOM   6435  C CE  . MET B 1 322 ? 59.00000  -31.02500 -15.62700 1.000 35.62000  ? 341  MET B CE  1 
ATOM   6436  N N   . GLU B 1 323 ? 62.57800  -29.03800 -20.07300 1.000 33.89000  ? 342  GLU B N   1 
ATOM   6437  C CA  . GLU B 1 323 ? 62.90400  -27.76200 -20.69900 1.000 33.00000  ? 342  GLU B CA  1 
ATOM   6438  C C   . GLU B 1 323 ? 62.05100  -27.52800 -21.94000 1.000 34.82000  ? 342  GLU B C   1 
ATOM   6439  O O   . GLU B 1 323 ? 61.53100  -26.42700 -22.15800 1.000 33.71000  ? 342  GLU B O   1 
ATOM   6440  C CB  . GLU B 1 323 ? 64.39200  -27.69900 -21.05100 1.000 31.62000  ? 342  GLU B CB  1 
ATOM   6441  C CG  . GLU B 1 323 ? 64.78100  -26.34500 -21.65400 1.000 38.82000  ? 342  GLU B CG  1 
ATOM   6442  C CD  . GLU B 1 323 ? 66.27500  -26.18900 -21.92100 1.000 48.53000  ? 342  GLU B CD  1 
ATOM   6443  O OE1 . GLU B 1 323 ? 67.03600  -27.15400 -21.68300 1.000 46.74000  ? 342  GLU B OE1 1 
ATOM   6444  O OE2 . GLU B 1 323 ? 66.68400  -25.08400 -22.35000 1.000 50.09000  ? 342  GLU B OE2 1 
ATOM   6445  N N   . ASN B 1 324 ? 61.90500  -28.55000 -22.77900 1.000 30.62000  ? 343  ASN B N   1 
ATOM   6446  C CA  . ASN B 1 324 ? 61.03500  -28.38500 -23.93100 1.000 33.41000  ? 343  ASN B CA  1 
ATOM   6447  C C   . ASN B 1 324 ? 59.58900  -28.20700 -23.48800 1.000 33.80000  ? 343  ASN B C   1 
ATOM   6448  O O   . ASN B 1 324 ? 58.84000  -27.42800 -24.08800 1.000 32.84000  ? 343  ASN B O   1 
ATOM   6449  C CB  . ASN B 1 324 ? 61.19900  -29.56500 -24.89100 1.000 32.67000  ? 343  ASN B CB  1 
ATOM   6450  C CG  . ASN B 1 324 ? 62.49400  -29.47700 -25.70500 1.000 34.30000  ? 343  ASN B CG  1 
ATOM   6451  O OD1 . ASN B 1 324 ? 62.84500  -28.41000 -26.21700 1.000 30.71000  ? 343  ASN B OD1 1 
ATOM   6452  N ND2 . ASN B 1 324 ? 63.21400  -30.59400 -25.81000 1.000 27.05000  ? 343  ASN B ND2 1 
ATOM   6453  N N   . ALA B 1 325 ? 59.18400  -28.89500 -22.42000 1.000 34.30000  ? 344  ALA B N   1 
ATOM   6454  C CA  . ALA B 1 325 ? 57.81800  -28.74000 -21.93000 1.000 36.55000  ? 344  ALA B CA  1 
ATOM   6455  C C   . ALA B 1 325 ? 57.56300  -27.31800 -21.45800 1.000 36.21000  ? 344  ALA B C   1 
ATOM   6456  O O   . ALA B 1 325 ? 56.54900  -26.70700 -21.81100 1.000 35.07000  ? 344  ALA B O   1 
ATOM   6457  C CB  . ALA B 1 325 ? 57.54700  -29.73000 -20.80900 1.000 25.25000  ? 344  ALA B CB  1 
ATOM   6458  N N   . GLN B 1 326 ? 58.49200  -26.76600 -20.67200 1.000 32.07000  ? 345  GLN B N   1 
ATOM   6459  C CA  . GLN B 1 326 ? 58.32100  -25.41100 -20.16000 1.000 36.39000  ? 345  GLN B CA  1 
ATOM   6460  C C   . GLN B 1 326 ? 58.30700  -24.37800 -21.27600 1.000 37.68000  ? 345  GLN B C   1 
ATOM   6461  O O   . GLN B 1 326 ? 57.63400  -23.35000 -21.15500 1.000 45.67000  ? 345  GLN B O   1 
ATOM   6462  C CB  . GLN B 1 326 ? 59.41500  -25.10200 -19.14000 1.000 38.06000  ? 345  GLN B CB  1 
ATOM   6463  C CG  . GLN B 1 326 ? 59.14200  -25.69100 -17.75900 1.000 42.59000  ? 345  GLN B CG  1 
ATOM   6464  C CD  . GLN B 1 326 ? 60.34400  -25.62900 -16.84700 1.000 51.39000  ? 345  GLN B CD  1 
ATOM   6465  O OE1 . GLN B 1 326 ? 61.46900  -25.40100 -17.30100 1.000 62.69000  ? 345  GLN B OE1 1 
ATOM   6466  N NE2 . GLN B 1 326 ? 60.11400  -25.79200 -15.54700 1.000 49.83000  ? 345  GLN B NE2 1 
ATOM   6467  N N   . LYS B 1 327 ? 59.01800  -24.63600 -22.36600 1.000 29.86000  ? 346  LYS B N   1 
ATOM   6468  C CA  . LYS B 1 327 ? 59.05000  -23.71700 -23.49100 1.000 37.04000  ? 346  LYS B CA  1 
ATOM   6469  C C   . LYS B 1 327 ? 57.90500  -23.94100 -24.46600 1.000 38.11000  ? 346  LYS B C   1 
ATOM   6470  O O   . LYS B 1 327 ? 57.71600  -23.12800 -25.38000 1.000 31.86000  ? 346  LYS B O   1 
ATOM   6471  C CB  . LYS B 1 327 ? 60.40100  -23.84300 -24.21700 1.000 33.52000  ? 346  LYS B CB  1 
ATOM   6472  C CG  . LYS B 1 327 ? 61.57400  -23.34000 -23.36700 1.000 31.53000  ? 346  LYS B CG  1 
ATOM   6473  C CD  . LYS B 1 327 ? 62.94000  -23.50900 -24.02600 1.000 33.43000  ? 346  LYS B CD  1 
ATOM   6474  C CE  . LYS B 1 327 ? 64.02200  -22.92200 -23.13000 1.000 38.08000  ? 346  LYS B CE  1 
ATOM   6475  N NZ  . LYS B 1 327 ? 65.40300  -23.08000 -23.66200 1.000 47.18000  ? 346  LYS B NZ  1 
ATOM   6476  N N   . GLY B 1 328 ? 57.14600  -25.01000 -24.29100 1.000 27.63000  ? 347  GLY B N   1 
ATOM   6477  C CA  . GLY B 1 328 ? 56.11200  -25.38700 -25.22100 1.000 33.80000  ? 347  GLY B CA  1 
ATOM   6478  C C   . GLY B 1 328 ? 54.73700  -24.85600 -24.87100 1.000 42.79000  ? 347  GLY B C   1 
ATOM   6479  O O   . GLY B 1 328 ? 54.56700  -23.91400 -24.09100 1.000 41.30000  ? 347  GLY B O   1 
ATOM   6480  N N   . GLU B 1 329 ? 53.73900  -25.49000 -25.47700 1.000 40.11000  ? 348  GLU B N   1 
ATOM   6481  C CA  . GLU B 1 329 ? 52.33600  -25.12700 -25.37800 1.000 38.16000  ? 348  GLU B CA  1 
ATOM   6482  C C   . GLU B 1 329 ? 51.60200  -26.30300 -24.75700 1.000 38.71000  ? 348  GLU B C   1 
ATOM   6483  O O   . GLU B 1 329 ? 51.69200  -27.42700 -25.26400 1.000 31.49000  ? 348  GLU B O   1 
ATOM   6484  C CB  . GLU B 1 329 ? 51.79200  -24.81600 -26.77800 1.000 39.57000  ? 348  GLU B CB  1 
ATOM   6485  C CG  . GLU B 1 329 ? 50.31100  -24.43100 -26.91000 1.000 43.60000  ? 348  GLU B CG  1 
ATOM   6486  C CD  . GLU B 1 329 ? 49.85400  -24.34100 -28.39600 1.000 56.65000  ? 348  GLU B CD  1 
ATOM   6487  O OE1 . GLU B 1 329 ? 50.67900  -24.61700 -29.31500 1.000 49.83000  ? 348  GLU B OE1 1 
ATOM   6488  O OE2 . GLU B 1 329 ? 48.66400  -24.01800 -28.64800 1.000 43.07000  ? 348  GLU B OE2 1 
ATOM   6489  N N   . ILE B 1 330 ? 50.89900  -26.05700 -23.64400 1.000 34.92000  ? 349  ILE B N   1 
ATOM   6490  C CA  . ILE B 1 330 ? 50.04900  -27.09400 -23.06900 1.000 33.26000  ? 349  ILE B CA  1 
ATOM   6491  C C   . ILE B 1 330 ? 49.00200  -27.48500 -24.10100 1.000 36.37000  ? 349  ILE B C   1 
ATOM   6492  O O   . ILE B 1 330 ? 48.35700  -26.61600 -24.70800 1.000 38.17000  ? 349  ILE B O   1 
ATOM   6493  C CB  . ILE B 1 330 ? 49.39000  -26.58300 -21.77800 1.000 39.08000  ? 349  ILE B CB  1 
ATOM   6494  C CG1 . ILE B 1 330 ? 50.44800  -26.33100 -20.70300 1.000 36.28000  ? 349  ILE B CG1 1 
ATOM   6495  C CG2 . ILE B 1 330 ? 48.29900  -27.52900 -21.30100 1.000 35.58000  ? 349  ILE B CG2 1 
ATOM   6496  C CD1 . ILE B 1 330 ? 51.20200  -27.58800 -20.30400 1.000 42.36000  ? 349  ILE B CD1 1 
ATOM   6497  N N   . MET B 1 331 ? 48.85100  -28.78400 -24.33400 1.000 32.28000  ? 350  MET B N   1 
ATOM   6498  C CA  . MET B 1 331 ? 47.81700  -29.29300 -25.23400 1.000 30.60000  ? 350  MET B CA  1 
ATOM   6499  C C   . MET B 1 331 ? 46.45900  -28.77400 -24.78900 1.000 33.66000  ? 350  MET B C   1 
ATOM   6500  O O   . MET B 1 331 ? 46.06900  -29.00600 -23.63100 1.000 29.57000  ? 350  MET B O   1 
ATOM   6501  C CB  . MET B 1 331 ? 47.78800  -30.82000 -25.20100 1.000 33.48000  ? 350  MET B CB  1 
ATOM   6502  C CG  . MET B 1 331 ? 46.76000  -31.42400 -26.12600 1.000 30.78000  ? 350  MET B CG  1 
ATOM   6503  S SD  . MET B 1 331 ? 47.27500  -31.58600 -27.82100 1.000 54.71000  ? 350  MET B SD  1 
ATOM   6504  C CE  . MET B 1 331 ? 48.16500  -33.14800 -27.70300 1.000 54.59000  ? 350  MET B CE  1 
ATOM   6505  N N   . PRO B 1 332 ? 45.71600  -28.07800 -25.64300 1.000 31.66000  ? 351  PRO B N   1 
ATOM   6506  C CA  . PRO B 1 332 ? 44.39100  -27.58300 -25.23900 1.000 34.86000  ? 351  PRO B CA  1 
ATOM   6507  C C   . PRO B 1 332 ? 43.45000  -28.73400 -24.92700 1.000 35.65000  ? 351  PRO B C   1 
ATOM   6508  O O   . PRO B 1 332 ? 43.32900  -29.69800 -25.69300 1.000 37.54000  ? 351  PRO B O   1 
ATOM   6509  C CB  . PRO B 1 332 ? 43.91100  -26.79800 -26.47200 1.000 33.05000  ? 351  PRO B CB  1 
ATOM   6510  C CG  . PRO B 1 332 ? 45.17000  -26.42300 -27.16900 1.000 29.81000  ? 351  PRO B CG  1 
ATOM   6511  C CD  . PRO B 1 332 ? 46.08200  -27.59000 -26.98500 1.000 37.86000  ? 351  PRO B CD  1 
ATOM   6512  N N   . ASN B 1 333 ? 42.76300  -28.63900 -23.79600 1.000 33.14000  ? 352  ASN B N   1 
ATOM   6513  C CA  . ASN B 1 333 ? 41.88100  -29.69800 -23.32400 1.000 42.71000  ? 352  ASN B CA  1 
ATOM   6514  C C   . ASN B 1 333 ? 40.43300  -29.55000 -23.80900 1.000 41.22000  ? 352  ASN B C   1 
ATOM   6515  O O   . ASN B 1 333 ? 39.54700  -30.23600 -23.28800 1.000 43.76000  ? 352  ASN B O   1 
ATOM   6516  C CB  . ASN B 1 333 ? 41.89800  -29.77600 -21.78600 1.000 37.84000  ? 352  ASN B CB  1 
ATOM   6517  C CG  . ASN B 1 333 ? 41.41100  -28.49100 -21.11200 1.000 41.91000  ? 352  ASN B CG  1 
ATOM   6518  O OD1 . ASN B 1 333 ? 40.97100  -27.54700 -21.77900 1.000 43.03000  ? 352  ASN B OD1 1 
ATOM   6519  N ND2 . ASN B 1 333 ? 41.48800  -28.45500 -19.78100 1.000 35.79000  ? 352  ASN B ND2 1 
ATOM   6520  N N   . ILE B 1 334 ? 40.16000  -28.69200 -24.78300 1.000 36.77000  ? 353  ILE B N   1 
ATOM   6521  C CA  . ILE B 1 334 ? 38.80600  -28.64600 -25.33400 1.000 39.56000  ? 353  ILE B CA  1 
ATOM   6522  C C   . ILE B 1 334 ? 38.68900  -29.68300 -26.44400 1.000 37.98000  ? 353  ILE B C   1 
ATOM   6523  O O   . ILE B 1 334 ? 39.62000  -29.84300 -27.24300 1.000 41.58000  ? 353  ILE B O   1 
ATOM   6524  C CB  . ILE B 1 334 ? 38.44200  -27.23800 -25.82800 1.000 35.56000  ? 353  ILE B CB  1 
ATOM   6525  C CG1 . ILE B 1 334 ? 39.46200  -26.77000 -26.85800 1.000 38.92000  ? 353  ILE B CG1 1 
ATOM   6526  C CG2 . ILE B 1 334 ? 38.31700  -26.26200 -24.66100 1.000 31.89000  ? 353  ILE B CG2 1 
ATOM   6527  C CD1 . ILE B 1 334 ? 39.13300  -25.45600 -27.44900 1.000 35.04000  ? 353  ILE B CD1 1 
ATOM   6528  N N   . PRO B 1 335 ? 37.57200  -30.41200 -26.52600 1.000 44.01000  ? 354  PRO B N   1 
ATOM   6529  C CA  . PRO B 1 335 ? 37.46800  -31.48700 -27.52900 1.000 46.12000  ? 354  PRO B CA  1 
ATOM   6530  C C   . PRO B 1 335 ? 37.50800  -30.98700 -28.96000 1.000 42.32000  ? 354  PRO B C   1 
ATOM   6531  O O   . PRO B 1 335 ? 37.74100  -31.78800 -29.87600 1.000 40.68000  ? 354  PRO B O   1 
ATOM   6532  C CB  . PRO B 1 335 ? 36.12300  -32.14500 -27.20500 1.000 42.50000  ? 354  PRO B CB  1 
ATOM   6533  C CG  . PRO B 1 335 ? 35.34200  -31.07000 -26.51500 1.000 43.03000  ? 354  PRO B CG  1 
ATOM   6534  C CD  . PRO B 1 335 ? 36.33800  -30.26400 -25.73700 1.000 38.55000  ? 354  PRO B CD  1 
ATOM   6535  N N   . GLN B 1 336 ? 37.29800  -29.69200 -29.17800 1.000 39.88000  ? 355  GLN B N   1 
ATOM   6536  C CA  . GLN B 1 336 ? 37.36300  -29.10700 -30.51000 1.000 40.50000  ? 355  GLN B CA  1 
ATOM   6537  C C   . GLN B 1 336 ? 38.77100  -29.16100 -31.09300 1.000 39.68000  ? 355  GLN B C   1 
ATOM   6538  O O   . GLN B 1 336 ? 38.97400  -28.76400 -32.24400 1.000 40.53000  ? 355  GLN B O   1 
ATOM   6539  C CB  . GLN B 1 336 ? 36.87500  -27.65700 -30.48700 1.000 40.33000  ? 355  GLN B CB  1 
ATOM   6540  C CG  . GLN B 1 336 ? 35.37200  -27.45300 -30.29100 1.000 33.58000  ? 355  GLN B CG  1 
ATOM   6541  C CD  . GLN B 1 336 ? 34.93500  -27.50500 -28.83300 1.000 38.85000  ? 355  GLN B CD  1 
ATOM   6542  O OE1 . GLN B 1 336 ? 35.75700  -27.60500 -27.92100 1.000 40.81000  ? 355  GLN B OE1 1 
ATOM   6543  N NE2 . GLN B 1 336 ? 33.63400  -27.36600 -28.60700 1.000 37.33000  ? 355  GLN B NE2 1 
ATOM   6544  N N   . MET B 1 337 ? 39.75400  -29.65000 -30.32900 1.000 39.08000  ? 356  MET B N   1 
ATOM   6545  C CA  . MET B 1 337 ? 41.07800  -29.85600 -30.91400 1.000 45.83000  ? 356  MET B CA  1 
ATOM   6546  C C   . MET B 1 337 ? 41.01500  -30.76800 -32.12400 1.000 41.47000  ? 356  MET B C   1 
ATOM   6547  O O   . MET B 1 337 ? 41.89300  -30.70200 -32.99000 1.000 40.55000  ? 356  MET B O   1 
ATOM   6548  C CB  . MET B 1 337 ? 42.06400  -30.43000 -29.89400 1.000 39.96000  ? 356  MET B CB  1 
ATOM   6549  C CG  . MET B 1 337 ? 42.71900  -29.39500 -29.01500 1.000 41.86000  ? 356  MET B CG  1 
ATOM   6550  S SD  . MET B 1 337 ? 43.71900  -28.24200 -29.99200 1.000 38.28000  ? 356  MET B SD  1 
ATOM   6551  C CE  . MET B 1 337 ? 45.09300  -29.27400 -30.49900 1.000 36.68000  ? 356  MET B CE  1 
ATOM   6552  N N   . SER B 1 338 ? 39.99100  -31.62000 -32.20200 1.000 39.84000  ? 357  SER B N   1 
ATOM   6553  C CA  . SER B 1 338 ? 39.81200  -32.46700 -33.37500 1.000 39.93000  ? 357  SER B CA  1 
ATOM   6554  C C   . SER B 1 338 ? 39.80300  -31.64500 -34.65900 1.000 34.15000  ? 357  SER B C   1 
ATOM   6555  O O   . SER B 1 338 ? 40.34100  -32.07500 -35.68100 1.000 40.30000  ? 357  SER B O   1 
ATOM   6556  C CB  . SER B 1 338 ? 38.51700  -33.26800 -33.23200 1.000 42.82000  ? 357  SER B CB  1 
ATOM   6557  O OG  . SER B 1 338 ? 37.38900  -32.41100 -33.17900 1.000 43.66000  ? 357  SER B OG  1 
ATOM   6558  N N   . ALA B 1 339 ? 39.19100  -30.45800 -34.62600 1.000 39.12000  ? 358  ALA B N   1 
ATOM   6559  C CA  . ALA B 1 339 ? 39.18700  -29.59200 -35.80100 1.000 33.41000  ? 358  ALA B CA  1 
ATOM   6560  C C   . ALA B 1 339 ? 40.59100  -29.12600 -36.14300 1.000 32.03000  ? 358  ALA B C   1 
ATOM   6561  O O   . ALA B 1 339 ? 40.96300  -29.08000 -37.31800 1.000 39.31000  ? 358  ALA B O   1 
ATOM   6562  C CB  . ALA B 1 339 ? 38.27700  -28.38800 -35.57100 1.000 33.83000  ? 358  ALA B CB  1 
ATOM   6563  N N   . PHE B 1 340 ? 41.38400  -28.77000 -35.12800 1.000 37.39000  ? 359  PHE B N   1 
ATOM   6564  C CA  . PHE B 1 340 ? 42.75900  -28.33500 -35.36400 1.000 34.25000  ? 359  PHE B CA  1 
ATOM   6565  C C   . PHE B 1 340 ? 43.57700  -29.43100 -36.03400 1.000 33.56000  ? 359  PHE B C   1 
ATOM   6566  O O   . PHE B 1 340 ? 44.23000  -29.18700 -37.05200 1.000 36.52000  ? 359  PHE B O   1 
ATOM   6567  C CB  . PHE B 1 340 ? 43.41400  -27.91600 -34.04700 1.000 40.66000  ? 359  PHE B CB  1 
ATOM   6568  C CG  . PHE B 1 340 ? 44.87600  -27.54800 -34.17900 1.000 33.39000  ? 359  PHE B CG  1 
ATOM   6569  C CD1 . PHE B 1 340 ? 45.26100  -26.28800 -34.62100 1.000 29.61000  ? 359  PHE B CD1 1 
ATOM   6570  C CD2 . PHE B 1 340 ? 45.86000  -28.48200 -33.87700 1.000 30.63000  ? 359  PHE B CD2 1 
ATOM   6571  C CE1 . PHE B 1 340 ? 46.60700  -25.96700 -34.74700 1.000 35.42000  ? 359  PHE B CE1 1 
ATOM   6572  C CE2 . PHE B 1 340 ? 47.20000  -28.17600 -34.00300 1.000 32.58000  ? 359  PHE B CE2 1 
ATOM   6573  C CZ  . PHE B 1 340 ? 47.58000  -26.91700 -34.43800 1.000 35.93000  ? 359  PHE B CZ  1 
ATOM   6574  N N   . TRP B 1 341 ? 43.55700  -30.64800 -35.48000 1.000 37.11000  ? 360  TRP B N   1 
ATOM   6575  C CA  . TRP B 1 341 ? 44.38800  -31.70800 -36.04300 1.000 41.87000  ? 360  TRP B CA  1 
ATOM   6576  C C   . TRP B 1 341 ? 43.98100  -32.00800 -37.48100 1.000 42.16000  ? 360  TRP B C   1 
ATOM   6577  O O   . TRP B 1 341 ? 44.83400  -32.11700 -38.37300 1.000 40.59000  ? 360  TRP B O   1 
ATOM   6578  C CB  . TRP B 1 341 ? 44.30500  -32.98700 -35.20500 1.000 41.49000  ? 360  TRP B CB  1 
ATOM   6579  C CG  . TRP B 1 341 ? 44.78000  -32.88000 -33.78700 1.000 43.05000  ? 360  TRP B CG  1 
ATOM   6580  C CD1 . TRP B 1 341 ? 44.02700  -33.03300 -32.65600 1.000 42.09000  ? 360  TRP B CD1 1 
ATOM   6581  C CD2 . TRP B 1 341 ? 46.09900  -32.54100 -33.34400 1.000 44.70000  ? 360  TRP B CD2 1 
ATOM   6582  N NE1 . TRP B 1 341 ? 44.80600  -32.85000 -31.53900 1.000 43.25000  ? 360  TRP B NE1 1 
ATOM   6583  C CE2 . TRP B 1 341 ? 46.07800  -32.53600 -31.93400 1.000 39.33000  ? 360  TRP B CE2 1 
ATOM   6584  C CE3 . TRP B 1 341 ? 47.29900  -32.25200 -33.99900 1.000 39.27000  ? 360  TRP B CE3 1 
ATOM   6585  C CZ2 . TRP B 1 341 ? 47.20300  -32.24600 -31.17500 1.000 43.60000  ? 360  TRP B CZ2 1 
ATOM   6586  C CZ3 . TRP B 1 341 ? 48.41200  -31.96700 -33.24100 1.000 40.94000  ? 360  TRP B CZ3 1 
ATOM   6587  C CH2 . TRP B 1 341 ? 48.36100  -31.96800 -31.84800 1.000 42.33000  ? 360  TRP B CH2 1 
ATOM   6588  N N   . TYR B 1 342 ? 42.67300  -32.13700 -37.71800 1.000 36.80000  ? 361  TYR B N   1 
ATOM   6589  C CA  . TYR B 1 342 ? 42.16700  -32.49100 -39.04100 1.000 37.38000  ? 361  TYR B CA  1 
ATOM   6590  C C   . TYR B 1 342 ? 42.60800  -31.46800 -40.08200 1.000 36.46000  ? 361  TYR B C   1 
ATOM   6591  O O   . TYR B 1 342 ? 43.13200  -31.82600 -41.14300 1.000 41.33000  ? 361  TYR B O   1 
ATOM   6592  C CB  . TYR B 1 342 ? 40.63700  -32.59200 -38.98500 1.000 41.36000  ? 361  TYR B CB  1 
ATOM   6593  C CG  . TYR B 1 342 ? 39.97600  -33.14000 -40.24100 1.000 49.66000  ? 361  TYR B CG  1 
ATOM   6594  C CD1 . TYR B 1 342 ? 39.89000  -34.51000 -40.46500 1.000 50.68000  ? 361  TYR B CD1 1 
ATOM   6595  C CD2 . TYR B 1 342 ? 39.44700  -32.28700 -41.20500 1.000 47.73000  ? 361  TYR B CD2 1 
ATOM   6596  C CE1 . TYR B 1 342 ? 39.28600  -35.01800 -41.61000 1.000 50.02000  ? 361  TYR B CE1 1 
ATOM   6597  C CE2 . TYR B 1 342 ? 38.85000  -32.78500 -42.35300 1.000 50.50000  ? 361  TYR B CE2 1 
ATOM   6598  C CZ  . TYR B 1 342 ? 38.77200  -34.15200 -42.55100 1.000 56.84000  ? 361  TYR B CZ  1 
ATOM   6599  O OH  . TYR B 1 342 ? 38.17400  -34.65000 -43.69200 1.000 68.70000  ? 361  TYR B OH  1 
ATOM   6600  N N   . ALA B 1 343 ? 42.42100  -30.18100 -39.78100 1.000 38.17000  ? 362  ALA B N   1 
ATOM   6601  C CA  . ALA B 1 343 ? 42.74500  -29.12700 -40.73600 1.000 33.20000  ? 362  ALA B CA  1 
ATOM   6602  C C   . ALA B 1 343 ? 44.24800  -29.00600 -40.94400 1.000 36.84000  ? 362  ALA B C   1 
ATOM   6603  O O   . ALA B 1 343 ? 44.72500  -28.92500 -42.08200 1.000 39.20000  ? 362  ALA B O   1 
ATOM   6604  C CB  . ALA B 1 343 ? 42.16200  -27.79500 -40.25600 1.000 33.51000  ? 362  ALA B CB  1 
ATOM   6605  N N   . VAL B 1 344 ? 45.01200  -28.98000 -39.84900 1.000 37.07000  ? 363  VAL B N   1 
ATOM   6606  C CA  . VAL B 1 344 ? 46.44100  -28.71400 -39.95800 1.000 35.24000  ? 363  VAL B CA  1 
ATOM   6607  C C   . VAL B 1 344 ? 47.17100  -29.89600 -40.58100 1.000 36.28000  ? 363  VAL B C   1 
ATOM   6608  O O   . VAL B 1 344 ? 48.20400  -29.71200 -41.23500 1.000 35.90000  ? 363  VAL B O   1 
ATOM   6609  C CB  . VAL B 1 344 ? 47.00900  -28.32700 -38.58000 1.000 38.39000  ? 363  VAL B CB  1 
ATOM   6610  C CG1 . VAL B 1 344 ? 48.53200  -28.17700 -38.62800 1.000 29.78000  ? 363  VAL B CG1 1 
ATOM   6611  C CG2 . VAL B 1 344 ? 46.38700  -27.03300 -38.11700 1.000 31.17000  ? 363  VAL B CG2 1 
ATOM   6612  N N   . ARG B 1 345 ? 46.65500  -31.11800 -40.41000 1.000 37.81000  ? 364  ARG B N   1 
ATOM   6613  C CA  . ARG B 1 345 ? 47.28000  -32.27500 -41.04700 1.000 34.95000  ? 364  ARG B CA  1 
ATOM   6614  C C   . ARG B 1 345 ? 47.30200  -32.12000 -42.56300 1.000 35.01000  ? 364  ARG B C   1 
ATOM   6615  O O   . ARG B 1 345 ? 48.32400  -32.36500 -43.21400 1.000 37.52000  ? 364  ARG B O   1 
ATOM   6616  C CB  . ARG B 1 345 ? 46.54100  -33.55500 -40.66300 1.000 37.42000  ? 364  ARG B CB  1 
ATOM   6617  C CG  . ARG B 1 345 ? 47.28200  -34.79100 -41.10800 1.000 37.97000  ? 364  ARG B CG  1 
ATOM   6618  C CD  . ARG B 1 345 ? 46.53200  -36.08200 -40.87400 1.000 35.33000  ? 364  ARG B CD  1 
ATOM   6619  N NE  . ARG B 1 345 ? 47.44700  -37.20100 -41.07300 1.000 57.30000  ? 364  ARG B NE  1 
ATOM   6620  C CZ  . ARG B 1 345 ? 47.75500  -37.74400 -42.24700 1.000 58.74000  ? 364  ARG B CZ  1 
ATOM   6621  N NH1 . ARG B 1 345 ? 47.18500  -37.33900 -43.37400 1.000 53.90000  ? 364  ARG B NH1 1 
ATOM   6622  N NH2 . ARG B 1 345 ? 48.66800  -38.71400 -42.29100 1.000 51.96000  ? 364  ARG B NH2 1 
ATOM   6623  N N   . THR B 1 346 ? 46.17400  -31.71700 -43.14400 1.000 36.91000  ? 365  THR B N   1 
ATOM   6624  C CA  . THR B 1 346 ? 46.11500  -31.54000 -44.58700 1.000 37.78000  ? 365  THR B CA  1 
ATOM   6625  C C   . THR B 1 346 ? 47.05800  -30.43700 -45.04200 1.000 39.43000  ? 365  THR B C   1 
ATOM   6626  O O   . THR B 1 346 ? 47.74700  -30.57700 -46.06300 1.000 33.48000  ? 365  THR B O   1 
ATOM   6627  C CB  . THR B 1 346 ? 44.67900  -31.23000 -45.01000 1.000 39.34000  ? 365  THR B CB  1 
ATOM   6628  O OG1 . THR B 1 346 ? 43.84800  -32.34300 -44.67400 1.000 40.40000  ? 365  THR B OG1 1 
ATOM   6629  C CG2 . THR B 1 346 ? 44.58500  -30.95500 -46.52000 1.000 29.78000  ? 365  THR B CG2 1 
ATOM   6630  N N   . ALA B 1 347 ? 47.09700  -29.32600 -44.30400 1.000 34.00000  ? 366  ALA B N   1 
ATOM   6631  C CA  . ALA B 1 347 ? 47.86700  -28.18100 -44.76800 1.000 35.69000  ? 366  ALA B CA  1 
ATOM   6632  C C   . ALA B 1 347 ? 49.34700  -28.52100 -44.85300 1.000 33.52000  ? 366  ALA B C   1 
ATOM   6633  O O   . ALA B 1 347 ? 50.00900  -28.21900 -45.85200 1.000 37.44000  ? 366  ALA B O   1 
ATOM   6634  C CB  . ALA B 1 347 ? 47.63300  -26.98500 -43.85000 1.000 32.88000  ? 366  ALA B CB  1 
ATOM   6635  N N   . VAL B 1 348 ? 49.88100  -29.17100 -43.82100 1.000 34.87000  ? 367  VAL B N   1 
ATOM   6636  C CA  . VAL B 1 348 ? 51.31100  -29.46100 -43.81300 1.000 41.31000  ? 367  VAL B CA  1 
ATOM   6637  C C   . VAL B 1 348 ? 51.65600  -30.42900 -44.93300 1.000 37.08000  ? 367  VAL B C   1 
ATOM   6638  O O   . VAL B 1 348 ? 52.63500  -30.23200 -45.65900 1.000 31.15000  ? 367  VAL B O   1 
ATOM   6639  C CB  . VAL B 1 348 ? 51.74700  -29.99400 -42.43600 1.000 37.89000  ? 367  VAL B CB  1 
ATOM   6640  C CG1 . VAL B 1 348 ? 53.22300  -30.37100 -42.45900 1.000 34.08000  ? 367  VAL B CG1 1 
ATOM   6641  C CG2 . VAL B 1 348 ? 51.48300  -28.95400 -41.36800 1.000 34.43000  ? 367  VAL B CG2 1 
ATOM   6642  N N   . ILE B 1 349 ? 50.83900  -31.46800 -45.11500 1.000 35.63000  ? 368  ILE B N   1 
ATOM   6643  C CA  . ILE B 1 349 ? 51.10000  -32.44600 -46.16600 1.000 39.41000  ? 368  ILE B CA  1 
ATOM   6644  C C   . ILE B 1 349 ? 51.00700  -31.81200 -47.54900 1.000 35.18000  ? 368  ILE B C   1 
ATOM   6645  O O   . ILE B 1 349 ? 51.85600  -32.06200 -48.41100 1.000 38.59000  ? 368  ILE B O   1 
ATOM   6646  C CB  . ILE B 1 349 ? 50.15500  -33.65000 -46.01200 1.000 43.37000  ? 368  ILE B CB  1 
ATOM   6647  C CG1 . ILE B 1 349 ? 50.68800  -34.56400 -44.89900 1.000 39.56000  ? 368  ILE B CG1 1 
ATOM   6648  C CG2 . ILE B 1 349 ? 49.95200  -34.36600 -47.34400 1.000 34.52000  ? 368  ILE B CG2 1 
ATOM   6649  C CD1 . ILE B 1 349 ? 49.73200  -35.63000 -44.46600 1.000 40.72000  ? 368  ILE B CD1 1 
ATOM   6650  N N   . ASN B 1 350 ? 49.99000  -30.98000 -47.79100 1.000 34.72000  ? 369  ASN B N   1 
ATOM   6651  C CA  . ASN B 1 350 ? 49.89900  -30.35000 -49.10400 1.000 37.53000  ? 369  ASN B CA  1 
ATOM   6652  C C   . ASN B 1 350 ? 51.06400  -29.40200 -49.34500 1.000 40.32000  ? 369  ASN B C   1 
ATOM   6653  O O   . ASN B 1 350 ? 51.57400  -29.31400 -50.46800 1.000 43.14000  ? 369  ASN B O   1 
ATOM   6654  C CB  . ASN B 1 350 ? 48.58400  -29.58700 -49.28800 1.000 35.24000  ? 369  ASN B CB  1 
ATOM   6655  C CG  . ASN B 1 350 ? 47.38500  -30.49500 -49.38600 1.000 34.35000  ? 369  ASN B CG  1 
ATOM   6656  O OD1 . ASN B 1 350 ? 47.50500  -31.67600 -49.70600 1.000 36.47000  ? 369  ASN B OD1 1 
ATOM   6657  N ND2 . ASN B 1 350 ? 46.20100  -29.91600 -49.21700 1.000 41.24000  ? 369  ASN B ND2 1 
ATOM   6658  N N   . ALA B 1 351 ? 51.47100  -28.65100 -48.32100 1.000 34.35000  ? 370  ALA B N   1 
ATOM   6659  C CA  . ALA B 1 351 ? 52.56000  -27.70500 -48.52000 1.000 36.64000  ? 370  ALA B CA  1 
ATOM   6660  C C   . ALA B 1 351 ? 53.88600  -28.43400 -48.69000 1.000 43.25000  ? 370  ALA B C   1 
ATOM   6661  O O   . ALA B 1 351 ? 54.69000  -28.08500 -49.56700 1.000 35.37000  ? 370  ALA B O   1 
ATOM   6662  C CB  . ALA B 1 351 ? 52.61700  -26.72600 -47.35100 1.000 35.20000  ? 370  ALA B CB  1 
ATOM   6663  N N   . ALA B 1 352 ? 54.10800  -29.47000 -47.87200 1.000 39.77000  ? 371  ALA B N   1 
ATOM   6664  C CA  . ALA B 1 352 ? 55.35600  -30.22300 -47.91600 1.000 36.83000  ? 371  ALA B CA  1 
ATOM   6665  C C   . ALA B 1 352 ? 55.55200  -30.88500 -49.27300 1.000 39.07000  ? 371  ALA B C   1 
ATOM   6666  O O   . ALA B 1 352 ? 56.67800  -30.98200 -49.77100 1.000 42.28000  ? 371  ALA B O   1 
ATOM   6667  C CB  . ALA B 1 352 ? 55.37200  -31.26800 -46.80200 1.000 34.12000  ? 371  ALA B CB  1 
ATOM   6668  N N   . SER B 1 353 ? 54.46800  -31.33700 -49.88800 1.000 40.92000  ? 372  SER B N   1 
ATOM   6669  C CA  . SER B 1 353 ? 54.52500  -32.02100 -51.16900 1.000 37.84000  ? 372  SER B CA  1 
ATOM   6670  C C   . SER B 1 353 ? 54.48600  -31.06800 -52.35400 1.000 40.36000  ? 372  SER B C   1 
ATOM   6671  O O   . SER B 1 353 ? 54.48400  -31.52700 -53.50300 1.000 36.76000  ? 372  SER B O   1 
ATOM   6672  C CB  . SER B 1 353 ? 53.35800  -32.99600 -51.27200 1.000 40.26000  ? 372  SER B CB  1 
ATOM   6673  O OG  . SER B 1 353 ? 52.14400  -32.25900 -51.28600 1.000 43.50000  ? 372  SER B OG  1 
ATOM   6674  N N   . GLY B 1 354 ? 54.41000  -29.76500 -52.11000 1.000 36.60000  ? 373  GLY B N   1 
ATOM   6675  C CA  . GLY B 1 354 ? 54.29800  -28.84300 -53.21700 1.000 34.08000  ? 373  GLY B CA  1 
ATOM   6676  C C   . GLY B 1 354 ? 52.95100  -28.85100 -53.90800 1.000 44.89000  ? 373  GLY B C   1 
ATOM   6677  O O   . GLY B 1 354 ? 52.77700  -28.13900 -54.90300 1.000 44.64000  ? 373  GLY B O   1 
ATOM   6678  N N   . ARG B 1 355 ? 51.97200  -29.53900 -53.35400 1.000 44.09000  ? 374  ARG B N   1 
ATOM   6679  C CA  . ARG B 1 355 ? 50.65200  -29.45200 -54.00100 1.000 35.98000  ? 374  ARG B CA  1 
ATOM   6680  C C   . ARG B 1 355 ? 50.03000  -28.10600 -53.65300 1.000 40.10000  ? 374  ARG B C   1 
ATOM   6681  O O   . ARG B 1 355 ? 49.16300  -27.69200 -54.37700 1.000 34.74000  ? 374  ARG B O   1 
ATOM   6682  C CB  . ARG B 1 355 ? 49.76300  -30.61200 -53.57200 1.000 40.79000  ? 374  ARG B CB  1 
ATOM   6683  C CG  . ARG B 1 355 ? 50.25600  -31.93300 -54.12600 1.000 42.57000  ? 374  ARG B CG  1 
ATOM   6684  C CD  . ARG B 1 355 ? 49.38300  -33.09400 -53.78100 1.000 46.48000  ? 374  ARG B CD  1 
ATOM   6685  N NE  . ARG B 1 355 ? 50.07300  -33.99400 -52.88900 1.000 52.41000  ? 374  ARG B NE  1 
ATOM   6686  C CZ  . ARG B 1 355 ? 49.63300  -34.26100 -51.69000 1.000 46.17000  ? 374  ARG B CZ  1 
ATOM   6687  N NH1 . ARG B 1 355 ? 48.53200  -33.68300 -51.27900 1.000 56.27000  ? 374  ARG B NH1 1 
ATOM   6688  N NH2 . ARG B 1 355 ? 50.28200  -35.09700 -50.91000 1.000 48.81000  ? 374  ARG B NH2 1 
ATOM   6689  N N   . GLN B 1 356 ? 50.53000  -27.41800 -52.63100 1.000 41.69000  ? 375  GLN B N   1 
ATOM   6690  C CA  . GLN B 1 356 ? 49.85100  -26.19400 -52.23900 1.000 39.09000  ? 375  GLN B CA  1 
ATOM   6691  C C   . GLN B 1 356 ? 50.88200  -25.21700 -51.68500 1.000 44.01000  ? 375  GLN B C   1 
ATOM   6692  O O   . GLN B 1 356 ? 51.93200  -25.62800 -51.18400 1.000 45.43000  ? 375  GLN B O   1 
ATOM   6693  C CB  . GLN B 1 356 ? 48.74000  -26.54600 -51.22500 1.000 41.04000  ? 375  GLN B CB  1 
ATOM   6694  C CG  . GLN B 1 356 ? 47.56100  -25.59000 -51.20300 1.000 46.87000  ? 375  GLN B CG  1 
ATOM   6695  C CD  . GLN B 1 356 ? 46.38000  -26.11800 -50.38600 1.000 46.66000  ? 375  GLN B CD  1 
ATOM   6696  O OE1 . GLN B 1 356 ? 46.45900  -27.14100 -49.71000 1.000 45.96000  ? 375  GLN B OE1 1 
ATOM   6697  N NE2 . GLN B 1 356 ? 45.25400  -25.41200 -50.48600 1.000 41.64000  ? 375  GLN B NE2 1 
ATOM   6698  N N   . THR B 1 357 ? 50.60900  -23.92200 -51.81800 1.000 39.53000  ? 376  THR B N   1 
ATOM   6699  C CA  . THR B 1 357 ? 51.54900  -22.99100 -51.22100 1.000 32.81000  ? 376  THR B CA  1 
ATOM   6700  C C   . THR B 1 357 ? 51.35900  -22.96300 -49.71100 1.000 40.82000  ? 376  THR B C   1 
ATOM   6701  O O   . THR B 1 357 ? 50.31800  -23.36200 -49.18300 1.000 39.13000  ? 376  THR B O   1 
ATOM   6702  C CB  . THR B 1 357 ? 51.38700  -21.57500 -51.76900 1.000 34.60000  ? 376  THR B CB  1 
ATOM   6703  O OG1 . THR B 1 357 ? 50.08900  -21.08300 -51.43600 1.000 38.04000  ? 376  THR B OG1 1 
ATOM   6704  C CG2 . THR B 1 357 ? 51.58500  -21.53700 -53.27800 1.000 35.37000  ? 376  THR B CG2 1 
ATOM   6705  N N   . VAL B 1 358 ? 52.38500  -22.47500 -49.00900 1.000 38.08000  ? 377  VAL B N   1 
ATOM   6706  C CA  . VAL B 1 358 ? 52.24500  -22.30500 -47.56800 1.000 35.59000  ? 377  VAL B CA  1 
ATOM   6707  C C   . VAL B 1 358 ? 51.07100  -21.37700 -47.27300 1.000 37.45000  ? 377  VAL B C   1 
ATOM   6708  O O   . VAL B 1 358 ? 50.22500  -21.66700 -46.41300 1.000 39.64000  ? 377  VAL B O   1 
ATOM   6709  C CB  . VAL B 1 358 ? 53.56900  -21.80200 -46.95400 1.000 31.67000  ? 377  VAL B CB  1 
ATOM   6710  C CG1 . VAL B 1 358 ? 53.38000  -21.43800 -45.48600 1.000 31.38000  ? 377  VAL B CG1 1 
ATOM   6711  C CG2 . VAL B 1 358 ? 54.64400  -22.87400 -47.09000 1.000 27.64000  ? 377  VAL B CG2 1 
ATOM   6712  N N   . ASP B 1 359 ? 50.95600  -20.29000 -48.03600 1.000 38.55000  ? 378  ASP B N   1 
ATOM   6713  C CA  . ASP B 1 359 ? 49.84900  -19.35000 -47.86300 1.000 43.58000  ? 378  ASP B CA  1 
ATOM   6714  C C   . ASP B 1 359 ? 48.46100  -19.98500 -48.05700 1.000 43.63000  ? 378  ASP B C   1 
ATOM   6715  O O   . ASP B 1 359 ? 47.64200  -19.91500 -47.13600 1.000 44.38000  ? 378  ASP B O   1 
ATOM   6716  C CB  . ASP B 1 359 ? 50.07600  -18.12700 -48.75800 1.000 48.48000  ? 378  ASP B CB  1 
ATOM   6717  C CG  . ASP B 1 359 ? 50.82500  -17.00000 -48.03400 1.000 65.28000  ? 378  ASP B CG  1 
ATOM   6718  O OD1 . ASP B 1 359 ? 50.45400  -16.69000 -46.88100 1.000 69.83000  ? 378  ASP B OD1 1 
ATOM   6719  O OD2 . ASP B 1 359 ? 51.83300  -16.49500 -48.57400 1.000 67.49000  ? 378  ASP B OD2 1 
ATOM   6720  N N   . GLU B 1 360 ? 48.20500  -20.62500 -49.18000 1.000 39.91000  ? 379  GLU B N   1 
ATOM   6721  C CA  . GLU B 1 360 ? 46.84600  -21.18000 -49.33100 1.000 43.33000  ? 379  GLU B CA  1 
ATOM   6722  C C   . GLU B 1 360 ? 46.59000  -22.27800 -48.30500 1.000 42.84000  ? 379  GLU B C   1 
ATOM   6723  O O   . GLU B 1 360 ? 45.49700  -22.32900 -47.79700 1.000 44.28000  ? 379  GLU B O   1 
ATOM   6724  C CB  . GLU B 1 360 ? 46.63800  -21.73900 -50.73600 1.000 51.84000  ? 379  GLU B CB  1 
ATOM   6725  C CG  . GLU B 1 360 ? 46.44600  -20.65600 -51.77800 1.000 65.02000  ? 379  GLU B CG  1 
ATOM   6726  C CD  . GLU B 1 360 ? 45.02000  -20.26200 -52.10700 1.000 71.58000  ? 379  GLU B CD  1 
ATOM   6727  O OE1 . GLU B 1 360 ? 44.35600  -19.68700 -51.24200 1.000 60.45000  ? 379  GLU B OE1 1 
ATOM   6728  O OE2 . GLU B 1 360 ? 44.59800  -20.51300 -53.24500 1.000 84.02000  ? 379  GLU B OE2 1 
ATOM   6729  N N   . ALA B 1 361 ? 47.60600  -23.04400 -47.94300 1.000 36.72000  ? 380  ALA B N   1 
ATOM   6730  C CA  . ALA B 1 361 ? 47.35900  -24.22000 -47.15000 1.000 39.99000  ? 380  ALA B CA  1 
ATOM   6731  C C   . ALA B 1 361 ? 47.02100  -23.82400 -45.73500 1.000 37.53000  ? 380  ALA B C   1 
ATOM   6732  O O   . ALA B 1 361 ? 46.08700  -24.37300 -45.14500 1.000 35.44000  ? 380  ALA B O   1 
ATOM   6733  C CB  . ALA B 1 361 ? 48.57100  -25.15600 -47.19300 1.000 35.16000  ? 380  ALA B CB  1 
ATOM   6734  N N   . LEU B 1 362 ? 47.71700  -22.82100 -45.21500 1.000 38.74000  ? 381  LEU B N   1 
ATOM   6735  C CA  . LEU B 1 362 ? 47.40600  -22.30900 -43.89700 1.000 44.00000  ? 381  LEU B CA  1 
ATOM   6736  C C   . LEU B 1 362 ? 46.16000  -21.44900 -43.92600 1.000 40.96000  ? 381  LEU B C   1 
ATOM   6737  O O   . LEU B 1 362 ? 45.37500  -21.48400 -42.97000 1.000 40.22000  ? 381  LEU B O   1 
ATOM   6738  C CB  . LEU B 1 362 ? 48.58700  -21.52800 -43.33000 1.000 39.86000  ? 381  LEU B CB  1 
ATOM   6739  C CG  . LEU B 1 362 ? 49.76200  -22.44300 -43.01500 1.000 32.88000  ? 381  LEU B CG  1 
ATOM   6740  C CD1 . LEU B 1 362 ? 50.96400  -21.67200 -42.50500 1.000 40.33000  ? 381  LEU B CD1 1 
ATOM   6741  C CD2 . LEU B 1 362 ? 49.31700  -23.48700 -42.01600 1.000 33.85000  ? 381  LEU B CD2 1 
ATOM   6742  N N   . LYS B 1 363 ? 45.94400  -20.69000 -45.00500 1.000 37.90000  ? 382  LYS B N   1 
ATOM   6743  C CA  . LYS B 1 363 ? 44.68700  -19.95900 -45.10300 1.000 41.33000  ? 382  LYS B CA  1 
ATOM   6744  C C   . LYS B 1 363 ? 43.50500  -20.91800 -45.09500 1.000 38.38000  ? 382  LYS B C   1 
ATOM   6745  O O   . LYS B 1 363 ? 42.52200  -20.68400 -44.38300 1.000 47.74000  ? 382  LYS B O   1 
ATOM   6746  C CB  . LYS B 1 363 ? 44.64700  -19.05700 -46.34300 1.000 49.88000  ? 382  LYS B CB  1 
ATOM   6747  C CG  . LYS B 1 363 ? 43.29400  -18.34500 -46.44800 1.000 46.89000  ? 382  LYS B CG  1 
ATOM   6748  C CD  . LYS B 1 363 ? 43.01400  -17.48400 -47.69900 1.000 67.07000  ? 382  LYS B CD  1 
ATOM   6749  C CE  . LYS B 1 363 ? 43.46900  -16.02600 -47.61500 1.000 72.76000  ? 382  LYS B CE  1 
ATOM   6750  N NZ  . LYS B 1 363 ? 42.77000  -15.26100 -48.70600 1.000 80.73000  ? 382  LYS B NZ  1 
ATOM   6751  N N   . ASP B 1 364 ? 43.58900  -22.02600 -45.84300 1.000 37.17000  ? 383  ASP B N   1 
ATOM   6752  C CA  . ASP B 1 364 ? 42.47300  -22.97700 -45.85900 1.000 37.16000  ? 383  ASP B CA  1 
ATOM   6753  C C   . ASP B 1 364 ? 42.32600  -23.68400 -44.51800 1.000 41.84000  ? 383  ASP B C   1 
ATOM   6754  O O   . ASP B 1 364 ? 41.20200  -23.95100 -44.07700 1.000 42.50000  ? 383  ASP B O   1 
ATOM   6755  C CB  . ASP B 1 364 ? 42.63800  -24.01100 -46.97200 1.000 33.32000  ? 383  ASP B CB  1 
ATOM   6756  C CG  . ASP B 1 364 ? 42.50400  -23.40800 -48.36300 1.000 51.05000  ? 383  ASP B CG  1 
ATOM   6757  O OD1 . ASP B 1 364 ? 41.90500  -22.31300 -48.48100 1.000 54.59000  ? 383  ASP B OD1 1 
ATOM   6758  O OD2 . ASP B 1 364 ? 42.96200  -24.04000 -49.34300 1.000 50.92000  ? 383  ASP B OD2 1 
ATOM   6759  N N   . ALA B 1 365 ? 43.44800  -24.00900 -43.86400 1.000 35.94000  ? 384  ALA B N   1 
ATOM   6760  C CA  . ALA B 1 365 ? 43.39100  -24.74700 -42.60500 1.000 33.62000  ? 384  ALA B CA  1 
ATOM   6761  C C   . ALA B 1 365 ? 42.82100  -23.88700 -41.48800 1.000 35.92000  ? 384  ALA B C   1 
ATOM   6762  O O   . ALA B 1 365 ? 42.08700  -24.38600 -40.62600 1.000 34.64000  ? 384  ALA B O   1 
ATOM   6763  C CB  . ALA B 1 365 ? 44.78200  -25.26000 -42.22400 1.000 37.27000  ? 384  ALA B CB  1 
ATOM   6764  N N   . GLN B 1 366 ? 43.17000  -22.59900 -41.48000 1.000 34.45000  ? 385  GLN B N   1 
ATOM   6765  C CA  . GLN B 1 366 ? 42.55300  -21.64700 -40.56300 1.000 36.73000  ? 385  GLN B CA  1 
ATOM   6766  C C   . GLN B 1 366 ? 41.03600  -21.68100 -40.68700 1.000 38.73000  ? 385  GLN B C   1 
ATOM   6767  O O   . GLN B 1 366 ? 40.31600  -21.82300 -39.68900 1.000 36.35000  ? 385  GLN B O   1 
ATOM   6768  C CB  . GLN B 1 366 ? 43.08700  -20.25000 -40.87600 1.000 42.99000  ? 385  GLN B CB  1 
ATOM   6769  C CG  . GLN B 1 366 ? 42.50200  -19.09100 -40.08900 1.000 41.74000  ? 385  GLN B CG  1 
ATOM   6770  C CD  . GLN B 1 366 ? 42.93800  -19.07000 -38.65600 1.000 39.51000  ? 385  GLN B CD  1 
ATOM   6771  O OE1 . GLN B 1 366 ? 44.03500  -19.51500 -38.32300 1.000 40.69000  ? 385  GLN B OE1 1 
ATOM   6772  N NE2 . GLN B 1 366 ? 42.11800  -18.47500 -37.80400 1.000 38.50000  ? 385  GLN B NE2 1 
ATOM   6773  N N   . THR B 1 367 ? 40.53800  -21.58200 -41.92100 1.000 41.34000  ? 386  THR B N   1 
ATOM   6774  C CA  . THR B 1 367 ? 39.10100  -21.57200 -42.17200 1.000 36.58000  ? 386  THR B CA  1 
ATOM   6775  C C   . THR B 1 367 ? 38.45600  -22.89100 -41.77400 1.000 34.91000  ? 386  THR B C   1 
ATOM   6776  O O   . THR B 1 367 ? 37.44100  -22.91100 -41.07000 1.000 41.64000  ? 386  THR B O   1 
ATOM   6777  C CB  . THR B 1 367 ? 38.85300  -21.27300 -43.64900 1.000 49.55000  ? 386  THR B CB  1 
ATOM   6778  O OG1 . THR B 1 367 ? 39.31900  -19.94900 -43.94200 1.000 56.18000  ? 386  THR B OG1 1 
ATOM   6779  C CG2 . THR B 1 367 ? 37.38300  -21.40100 -43.99800 1.000 54.32000  ? 386  THR B CG2 1 
ATOM   6780  N N   . ALA B 1 368 ? 39.04100  -24.01000 -42.20100 1.000 35.90000  ? 387  ALA B N   1 
ATOM   6781  C CA  . ALA B 1 368 ? 38.46400  -25.31000 -41.88000 1.000 33.40000  ? 387  ALA B CA  1 
ATOM   6782  C C   . ALA B 1 368 ? 38.47900  -25.56800 -40.37700 1.000 34.73000  ? 387  ALA B C   1 
ATOM   6783  O O   . ALA B 1 368 ? 37.53300  -26.14700 -39.83300 1.000 38.24000  ? 387  ALA B O   1 
ATOM   6784  C CB  . ALA B 1 368 ? 39.20700  -26.41600 -42.63300 1.000 23.36000  ? 387  ALA B CB  1 
ATOM   6785  N N   . ALA B 1 369 ? 39.54100  -25.14700 -39.68500 1.000 39.08000  ? 388  ALA B N   1 
ATOM   6786  C CA  . ALA B 1 369 ? 39.62600  -25.39000 -38.24500 1.000 38.04000  ? 388  ALA B CA  1 
ATOM   6787  C C   . ALA B 1 369 ? 38.55700  -24.60700 -37.49700 1.000 36.27000  ? 388  ALA B C   1 
ATOM   6788  O O   . ALA B 1 369 ? 37.84500  -25.16300 -36.65100 1.000 37.60000  ? 388  ALA B O   1 
ATOM   6789  C CB  . ALA B 1 369 ? 41.02200  -25.03900 -37.72300 1.000 35.21000  ? 388  ALA B CB  1 
ATOM   6790  N N   . ARG B 1 370 ? 38.42600  -23.31000 -37.80700 1.000 39.01000  ? 389  ARG B N   1 
ATOM   6791  C CA  . ARG B 1 370 ? 37.32800  -22.50200 -37.27100 1.000 44.13000  ? 389  ARG B CA  1 
ATOM   6792  C C   . ARG B 1 370 ? 35.96600  -23.16100 -37.52300 1.000 40.47000  ? 389  ARG B C   1 
ATOM   6793  O O   . ARG B 1 370 ? 35.16600  -23.34100 -36.59700 1.000 41.79000  ? 389  ARG B O   1 
ATOM   6794  C CB  . ARG B 1 370 ? 37.36100  -21.10500 -37.89800 1.000 40.22000  ? 389  ARG B CB  1 
ATOM   6795  C CG  . ARG B 1 370 ? 38.54300  -20.19900 -37.56900 1.000 34.41000  ? 389  ARG B CG  1 
ATOM   6796  C CD  . ARG B 1 370 ? 38.43300  -19.59900 -36.19100 1.000 48.98000  ? 389  ARG B CD  1 
ATOM   6797  N NE  . ARG B 1 370 ? 37.15600  -18.92000 -35.98800 1.000 56.70000  ? 389  ARG B NE  1 
ATOM   6798  C CZ  . ARG B 1 370 ? 36.86800  -17.70200 -36.43200 1.000 59.71000  ? 389  ARG B CZ  1 
ATOM   6799  N NH1 . ARG B 1 370 ? 37.72100  -17.01700 -37.18000 1.000 56.83000  ? 389  ARG B NH1 1 
ATOM   6800  N NH2 . ARG B 1 370 ? 35.68800  -17.16500 -36.13200 1.000 57.06000  ? 389  ARG B NH2 1 
ATOM   6801  N N   . ALA B 1 371 ? 35.69400  -23.54700 -38.77100 1.000 38.52000  ? 390  ALA B N   1 
ATOM   6802  C CA  . ALA B 1 371 ? 34.36600  -24.05300 -39.10700 1.000 36.56000  ? 390  ALA B CA  1 
ATOM   6803  C C   . ALA B 1 371 ? 34.05500  -25.36000 -38.38100 1.000 35.47000  ? 390  ALA B C   1 
ATOM   6804  O O   . ALA B 1 371 ? 32.98000  -25.50500 -37.78900 1.000 43.02000  ? 390  ALA B O   1 
ATOM   6805  C CB  . ALA B 1 371 ? 34.23800  -24.22800 -40.62100 1.000 33.84000  ? 390  ALA B CB  1 
ATOM   6806  N N   . PHE B 1 372 ? 34.97700  -26.32800 -38.41900 1.000 34.02000  ? 391  PHE B N   1 
ATOM   6807  C CA  . PHE B 1 372 ? 34.75100  -27.59800 -37.72800 1.000 39.21000  ? 391  PHE B CA  1 
ATOM   6808  C C   . PHE B 1 372 ? 34.64800  -27.41200 -36.21800 1.000 39.08000  ? 391  PHE B C   1 
ATOM   6809  O O   . PHE B 1 372 ? 33.85700  -28.09500 -35.55800 1.000 43.08000  ? 391  PHE B O   1 
ATOM   6810  C CB  . PHE B 1 372 ? 35.86300  -28.60500 -38.04400 1.000 39.56000  ? 391  PHE B CB  1 
ATOM   6811  C CG  . PHE B 1 372 ? 35.72300  -29.29100 -39.36900 1.000 43.50000  ? 391  PHE B CG  1 
ATOM   6812  C CD1 . PHE B 1 372 ? 34.79800  -30.31600 -39.53200 1.000 54.01000  ? 391  PHE B CD1 1 
ATOM   6813  C CD2 . PHE B 1 372 ? 36.52800  -28.94800 -40.43500 1.000 42.56000  ? 391  PHE B CD2 1 
ATOM   6814  C CE1 . PHE B 1 372 ? 34.66000  -30.96200 -40.74500 1.000 52.26000  ? 391  PHE B CE1 1 
ATOM   6815  C CE2 . PHE B 1 372 ? 36.40000  -29.59400 -41.65200 1.000 51.43000  ? 391  PHE B CE2 1 
ATOM   6816  C CZ  . PHE B 1 372 ? 35.46200  -30.60200 -41.80600 1.000 52.88000  ? 391  PHE B CZ  1 
ATOM   6817  N N   . ALA B 1 373 ? 35.46600  -26.52500 -35.64300 1.000 39.21000  ? 392  ALA B N   1 
ATOM   6818  C CA  . ALA B 1 373 ? 35.40800  -26.31100 -34.20100 1.000 41.13000  ? 392  ALA B CA  1 
ATOM   6819  C C   . ALA B 1 373 ? 34.07300  -25.70600 -33.79800 1.000 44.04000  ? 392  ALA B C   1 
ATOM   6820  O O   . ALA B 1 373 ? 33.47800  -26.11700 -32.79400 1.000 38.65000  ? 392  ALA B O   1 
ATOM   6821  C CB  . ALA B 1 373 ? 36.55700  -25.41500 -33.75000 1.000 26.60000  ? 392  ALA B CB  1 
ATOM   6822  N N   . ALA B 1 374 ? 33.58600  -24.73600 -34.57600 1.000 41.38000  ? 393  ALA B N   1 
ATOM   6823  C CA  . ALA B 1 374 ? 32.26200  -24.17800 -34.33200 1.000 41.61000  ? 393  ALA B CA  1 
ATOM   6824  C C   . ALA B 1 374 ? 31.18100  -25.23700 -34.46100 1.000 39.12000  ? 393  ALA B C   1 
ATOM   6825  O O   . ALA B 1 374 ? 30.19400  -25.21000 -33.72000 1.000 42.54000  ? 393  ALA B O   1 
ATOM   6826  C CB  . ALA B 1 374 ? 31.98800  -23.03000 -35.29900 1.000 35.80000  ? 393  ALA B CB  1 
ATOM   6827  N N   . ALA B 1 375 ? 31.34700  -26.17900 -35.38500 1.000 41.52000  ? 394  ALA B N   1 
ATOM   6828  C CA  . ALA B 1 375 ? 30.28400  -27.13900 -35.65500 1.000 46.09000  ? 394  ALA B CA  1 
ATOM   6829  C C   . ALA B 1 375 ? 30.17000  -28.19900 -34.56600 1.000 44.18000  ? 394  ALA B C   1 
ATOM   6830  O O   . ALA B 1 375 ? 29.07300  -28.72500 -34.33600 1.000 53.36000  ? 394  ALA B O   1 
ATOM   6831  C CB  . ALA B 1 375 ? 30.50800  -27.79500 -37.02000 1.000 42.07000  ? 394  ALA B CB  1 
ATOM   6832  N N   . GLY B 1 376 ? 31.26900  -28.52100 -33.90200 1.000 46.77000  ? 395  GLY B N   1 
ATOM   6833  C CA  . GLY B 1 376 ? 31.23300  -29.44200 -32.78500 1.000 41.78000  ? 395  GLY B CA  1 
ATOM   6834  C C   . GLY B 1 376 ? 32.50800  -30.25400 -32.69300 1.000 51.18000  ? 395  GLY B C   1 
ATOM   6835  O O   . GLY B 1 376 ? 33.45200  -30.08300 -33.45900 1.000 55.50000  ? 395  GLY B O   1 
ATOM   6836  N N   . LYS B 1 377 ? 32.49100  -31.16300 -31.72000 1.000 57.99000  ? 396  LYS B N   1 
ATOM   6837  C CA  . LYS B 1 377 ? 33.55700  -32.11400 -31.42400 1.000 53.95000  ? 396  LYS B CA  1 
ATOM   6838  C C   . LYS B 1 377 ? 33.82100  -33.10500 -32.55200 1.000 58.34000  ? 396  LYS B C   1 
ATOM   6839  O O   . LYS B 1 377 ? 34.97000  -33.49700 -32.76900 1.000 60.96000  ? 396  LYS B O   1 
ATOM   6840  C CB  . LYS B 1 377 ? 33.14700  -32.86400 -30.16400 1.000 52.53000  ? 396  LYS B CB  1 
ATOM   6841  C CG  . LYS B 1 377 ? 33.99400  -34.02600 -29.76700 1.000 66.59000  ? 396  LYS B CG  1 
ATOM   6842  C CD  . LYS B 1 377 ? 33.57300  -34.40600 -28.36800 1.000 64.92000  ? 396  LYS B CD  1 
ATOM   6843  C CE  . LYS B 1 377 ? 34.34900  -35.57800 -27.82100 1.000 73.11000  ? 396  LYS B CE  1 
ATOM   6844  N NZ  . LYS B 1 377 ? 34.02900  -35.67600 -26.36600 1.000 65.74000  ? 396  LYS B NZ  1 
ATOM   6845  N N   . GLU B 1 378 ? 32.79000  -33.50300 -33.28300 1.000 65.02000  ? 397  GLU B N   1 
ATOM   6846  C CA  . GLU B 1 378 ? 32.88200  -34.59200 -34.24200 1.000 65.04000  ? 397  GLU B CA  1 
ATOM   6847  C C   . GLU B 1 378 ? 33.29800  -34.02700 -35.59300 1.000 60.52000  ? 397  GLU B C   1 
ATOM   6848  O O   . GLU B 1 378 ? 32.63900  -33.11400 -36.11500 1.000 55.17000  ? 397  GLU B O   1 
ATOM   6849  C CB  . GLU B 1 378 ? 31.52600  -35.28900 -34.36300 1.000 75.13000  ? 397  GLU B CB  1 
ATOM   6850  C CG  . GLU B 1 378 ? 31.00300  -35.88000 -33.05900 1.000 83.39000  ? 397  GLU B CG  1 
ATOM   6851  C CD  . GLU B 1 378 ? 29.56400  -36.36600 -33.17500 1.000 110.80000 ? 397  GLU B CD  1 
ATOM   6852  O OE1 . GLU B 1 378 ? 28.93600  -36.13400 -34.23200 1.000 114.13000 ? 397  GLU B OE1 1 
ATOM   6853  O OE2 . GLU B 1 378 ? 29.05600  -36.96400 -32.19800 1.000 122.24000 ? 397  GLU B OE2 1 
ATOM   6854  N N   . ILE B 1 379 ? 34.36900  -34.57500 -36.16600 1.000 55.32000  ? 398  ILE B N   1 
ATOM   6855  C CA  . ILE B 1 379 ? 34.77400  -34.17200 -37.50600 1.000 55.63000  ? 398  ILE B CA  1 
ATOM   6856  C C   . ILE B 1 379 ? 33.89900  -34.94100 -38.48800 1.000 53.09000  ? 398  ILE B C   1 
ATOM   6857  O O   . ILE B 1 379 ? 34.18700  -36.08200 -38.84800 1.000 50.94000  ? 398  ILE B O   1 
ATOM   6858  C CB  . ILE B 1 379 ? 36.26100  -34.41400 -37.76900 1.000 51.70000  ? 398  ILE B CB  1 
ATOM   6859  C CG1 . ILE B 1 379 ? 37.10100  -33.63100 -36.77900 1.000 51.42000  ? 398  ILE B CG1 1 
ATOM   6860  C CG2 . ILE B 1 379 ? 36.60600  -33.98400 -39.19100 1.000 53.74000  ? 398  ILE B CG2 1 
ATOM   6861  C CD1 . ILE B 1 379 ? 36.84800  -32.14100 -36.84100 1.000 48.99000  ? 398  ILE B CD1 1 
ATOM   6862  N N   . GLU B 1 380 ? 32.80600  -34.32100 -38.90600 1.000 60.50000  ? 399  GLU B N   1 
ATOM   6863  C CA  . GLU B 1 380 ? 31.96200  -34.92300 -39.92200 1.000 61.96000  ? 399  GLU B CA  1 
ATOM   6864  C C   . GLU B 1 380 ? 31.43400  -33.82400 -40.81600 1.000 48.49000  ? 399  GLU B C   1 
ATOM   6865  O O   . GLU B 1 380 ? 30.98600  -32.77700 -40.34200 1.000 53.95000  ? 399  GLU B O   1 
ATOM   6866  C CB  . GLU B 1 380 ? 30.79200  -35.71000 -39.32200 1.000 59.59000  ? 399  GLU B CB  1 
ATOM   6867  C CG  . GLU B 1 380 ? 29.96400  -36.40700 -40.40200 1.000 66.57000  ? 399  GLU B CG  1 
ATOM   6868  C CD  . GLU B 1 380 ? 28.81600  -37.24000 -39.85500 1.000 72.96000  ? 399  GLU B CD  1 
ATOM   6869  O OE1 . GLU B 1 380 ? 28.61900  -37.27000 -38.61700 1.000 77.13000  ? 399  GLU B OE1 1 
ATOM   6870  O OE2 . GLU B 1 380 ? 28.10900  -37.86700 -40.67800 1.000 71.05000  ? 399  GLU B OE2 1 
ATOM   6871  N N   . ILE B 1 381 ? 31.50800  -34.06500 -42.11000 1.000 45.36000  ? 400  ILE B N   1 
ATOM   6872  C CA  . ILE B 1 381 ? 30.79500  -33.27000 -43.08700 1.000 57.10000  ? 400  ILE B CA  1 
ATOM   6873  C C   . ILE B 1 381 ? 29.92400  -34.22900 -43.87700 1.000 60.59000  ? 400  ILE B C   1 
ATOM   6874  O O   . ILE B 1 381 ? 30.41100  -35.24300 -44.38700 1.000 60.31000  ? 400  ILE B O   1 
ATOM   6875  C CB  . ILE B 1 381 ? 31.75800  -32.44600 -43.96300 1.000 51.95000  ? 400  ILE B CB  1 
ATOM   6876  C CG1 . ILE B 1 381 ? 30.95900  -31.50500 -44.87600 1.000 54.22000  ? 400  ILE B CG1 1 
ATOM   6877  C CG2 . ILE B 1 381 ? 32.79700  -33.35800 -44.65900 1.000 50.78000  ? 400  ILE B CG2 1 
ATOM   6878  C CD1 . ILE B 1 381 ? 31.73300  -30.27700 -45.30500 1.000 62.51000  ? 400  ILE B CD1 1 
ATOM   6879  N N   . LYS B 1 382 ? 28.62800  -33.94700 -43.90700 1.000 50.80000  ? 401  LYS B N   1 
ATOM   6880  C CA  . LYS B 1 382 ? 27.64400  -34.85000 -44.47700 1.000 50.57000  ? 401  LYS B CA  1 
ATOM   6881  C C   . LYS B 1 382 ? 27.22300  -34.31000 -45.83000 1.000 49.81000  ? 401  LYS B C   1 
ATOM   6882  O O   . LYS B 1 382 ? 27.02400  -33.09800 -45.99100 1.000 51.79000  ? 401  LYS B O   1 
ATOM   6883  C CB  . LYS B 1 382 ? 26.44700  -35.01000 -43.53800 1.000 49.12000  ? 401  LYS B CB  1 
ATOM   6884  C CG  . LYS B 1 382 ? 25.38600  -36.01900 -43.97800 1.000 54.55000  ? 401  LYS B CG  1 
ATOM   6885  C CD  . LYS B 1 382 ? 24.35400  -36.24600 -42.86500 1.000 57.96000  ? 401  LYS B CD  1 
ATOM   6886  C CE  . LYS B 1 382 ? 24.81700  -37.27100 -41.82100 1.000 61.74000  ? 401  LYS B CE  1 
ATOM   6887  N NZ  . LYS B 1 382 ? 24.74700  -38.66200 -42.37300 1.000 66.03000  ? 401  LYS B NZ  1 
ATOM   6888  N N   . LYS B 1 383 ? 27.14100  -35.19100 -46.81300 1.000 53.04000  ? 402  LYS B N   1 
ATOM   6889  C CA  . LYS B 1 383 ? 26.77500  -34.70300 -48.12600 1.000 58.77000  ? 402  LYS B CA  1 
ATOM   6890  C C   . LYS B 1 383 ? 25.27900  -34.41200 -48.19000 1.000 53.36000  ? 402  LYS B C   1 
ATOM   6891  O O   . LYS B 1 383 ? 24.45800  -35.05200 -47.51800 1.000 45.92000  ? 402  LYS B O   1 
ATOM   6892  C CB  . LYS B 1 383 ? 27.24400  -35.68100 -49.20300 1.000 60.62000  ? 402  LYS B CB  1 
ATOM   6893  C CG  . LYS B 1 383 ? 28.79400  -35.73800 -49.28000 1.000 69.02000  ? 402  LYS B CG  1 
ATOM   6894  C CD  . LYS B 1 383 ? 29.28700  -36.48600 -50.54600 1.000 79.38000  ? 402  LYS B CD  1 
ATOM   6895  C CE  . LYS B 1 383 ? 30.84400  -36.42900 -50.73300 1.000 78.49000  ? 402  LYS B CE  1 
ATOM   6896  N NZ  . LYS B 1 383 ? 31.68600  -36.85400 -49.54600 1.000 74.63000  ? 402  LYS B NZ  1 
ATOM   6897  N N   . LEU B 1 384 ? 24.95200  -33.38200 -48.96100 1.000 52.83000  ? 403  LEU B N   1 
ATOM   6898  C CA  . LEU B 1 384 ? 23.60000  -32.83400 -48.96500 1.000 54.24000  ? 403  LEU B CA  1 
ATOM   6899  C C   . LEU B 1 384 ? 22.53500  -33.88200 -49.25600 1.000 54.44000  ? 403  LEU B C   1 
ATOM   6900  O O   . LEU B 1 384 ? 21.52200  -33.91000 -48.53300 1.000 49.26000  ? 403  LEU B O   1 
ATOM   6901  C CB  . LEU B 1 384 ? 23.55100  -31.66300 -49.94900 1.000 52.72000  ? 403  LEU B CB  1 
ATOM   6902  C CG  . LEU B 1 384 ? 22.24900  -30.88800 -50.00500 1.000 52.81000  ? 403  LEU B CG  1 
ATOM   6903  C CD1 . LEU B 1 384 ? 21.94300  -30.35300 -48.61900 1.000 49.89000  ? 403  LEU B CD1 1 
ATOM   6904  C CD2 . LEU B 1 384 ? 22.38600  -29.75400 -51.01400 1.000 49.10000  ? 403  LEU B CD2 1 
ATOM   6905  N N   . PRO B 1 385 ? 22.67900  -34.76000 -50.26400 1.000 61.09000  ? 404  PRO B N   1 
ATOM   6906  C CA  . PRO B 1 385 ? 21.62600  -35.77200 -50.48900 1.000 57.76000  ? 404  PRO B CA  1 
ATOM   6907  C C   . PRO B 1 385 ? 21.35400  -36.66700 -49.28500 1.000 50.93000  ? 404  PRO B C   1 
ATOM   6908  O O   . PRO B 1 385 ? 20.18100  -36.97900 -49.01000 1.000 57.13000  ? 404  PRO B O   1 
ATOM   6909  C CB  . PRO B 1 385 ? 22.16300  -36.56500 -51.69000 1.000 51.22000  ? 404  PRO B CB  1 
ATOM   6910  C CG  . PRO B 1 385 ? 23.04100  -35.58900 -52.41000 1.000 45.05000  ? 404  PRO B CG  1 
ATOM   6911  C CD  . PRO B 1 385 ? 23.69700  -34.78800 -51.33600 1.000 44.54000  ? 404  PRO B CD  1 
ATOM   6912  N N   . GLU B 1 386 ? 22.39600  -37.08500 -48.55800 1.000 47.85000  ? 405  GLU B N   1 
ATOM   6913  C CA  . GLU B 1 386 ? 22.18200  -37.97000 -47.41800 1.000 49.40000  ? 405  GLU B CA  1 
ATOM   6914  C C   . GLU B 1 386 ? 21.49800  -37.23300 -46.28800 1.000 39.58000  ? 405  GLU B C   1 
ATOM   6915  O O   . GLU B 1 386 ? 20.66900  -37.81600 -45.58100 1.000 40.69000  ? 405  GLU B O   1 
ATOM   6916  C CB  . GLU B 1 386 ? 23.52000  -38.49800 -46.91400 1.000 55.84000  ? 405  GLU B CB  1 
ATOM   6917  C CG  . GLU B 1 386 ? 24.39100  -38.94100 -48.05100 1.000 69.87000  ? 405  GLU B CG  1 
ATOM   6918  C CD  . GLU B 1 386 ? 25.82000  -39.17700 -47.61000 1.000 82.20000  ? 405  GLU B CD  1 
ATOM   6919  O OE1 . GLU B 1 386 ? 26.06800  -39.23800 -46.38200 1.000 72.92000  ? 405  GLU B OE1 1 
ATOM   6920  O OE2 . GLU B 1 386 ? 26.70400  -39.14500 -48.50700 1.000 93.89000  ? 405  GLU B OE2 1 
ATOM   6921  N N   . PHE B 1 387 ? 21.84300  -35.95900 -46.10100 1.000 41.21000  ? 406  PHE B N   1 
ATOM   6922  C CA  . PHE B 1 387 ? 21.16700  -35.15400 -45.09600 1.000 45.76000  ? 406  PHE B CA  1 
ATOM   6923  C C   . PHE B 1 387 ? 19.71000  -34.93700 -45.47400 1.000 48.54000  ? 406  PHE B C   1 
ATOM   6924  O O   . PHE B 1 387 ? 18.81000  -35.09200 -44.64200 1.000 46.95000  ? 406  PHE B O   1 
ATOM   6925  C CB  . PHE B 1 387 ? 21.87800  -33.82100 -44.91000 1.000 39.63000  ? 406  PHE B CB  1 
ATOM   6926  C CG  . PHE B 1 387 ? 21.15700  -32.90900 -43.96700 1.000 37.57000  ? 406  PHE B CG  1 
ATOM   6927  C CD1 . PHE B 1 387 ? 21.07700  -33.22300 -42.62300 1.000 38.65000  ? 406  PHE B CD1 1 
ATOM   6928  C CD2 . PHE B 1 387 ? 20.54900  -31.75100 -44.42000 1.000 40.73000  ? 406  PHE B CD2 1 
ATOM   6929  C CE1 . PHE B 1 387 ? 20.40100  -32.39100 -41.73600 1.000 42.49000  ? 406  PHE B CE1 1 
ATOM   6930  C CE2 . PHE B 1 387 ? 19.86800  -30.91200 -43.54700 1.000 41.82000  ? 406  PHE B CE2 1 
ATOM   6931  C CZ  . PHE B 1 387 ? 19.79400  -31.23000 -42.19800 1.000 39.08000  ? 406  PHE B CZ  1 
ATOM   6932  N N   . GLU B 1 388 ? 19.46100  -34.56100 -46.72800 1.000 45.95000  ? 407  GLU B N   1 
ATOM   6933  C CA  . GLU B 1 388 ? 18.08800  -34.41900 -47.18200 1.000 49.38000  ? 407  GLU B CA  1 
ATOM   6934  C C   . GLU B 1 388 ? 17.33100  -35.73900 -47.10500 1.000 50.30000  ? 407  GLU B C   1 
ATOM   6935  O O   . GLU B 1 388 ? 16.12000  -35.73700 -46.85400 1.000 51.36000  ? 407  GLU B O   1 
ATOM   6936  C CB  . GLU B 1 388 ? 18.06900  -33.81400 -48.58900 1.000 52.20000  ? 407  GLU B CB  1 
ATOM   6937  C CG  . GLU B 1 388 ? 18.22300  -32.28900 -48.55900 1.000 50.30000  ? 407  GLU B CG  1 
ATOM   6938  C CD  . GLU B 1 388 ? 18.30500  -31.65700 -49.92800 1.000 61.56000  ? 407  GLU B CD  1 
ATOM   6939  O OE1 . GLU B 1 388 ? 18.57300  -32.38800 -50.90100 1.000 72.96000  ? 407  GLU B OE1 1 
ATOM   6940  O OE2 . GLU B 1 388 ? 18.06300  -30.43300 -50.04100 1.000 64.93000  ? 407  GLU B OE2 1 
ATOM   6941  N N   . ALA B 1 389 ? 18.01700  -36.87400 -47.27200 1.000 42.26000  ? 408  ALA B N   1 
ATOM   6942  C CA  . ALA B 1 389 ? 17.35000  -38.15200 -47.04000 1.000 41.86000  ? 408  ALA B CA  1 
ATOM   6943  C C   . ALA B 1 389 ? 16.88600  -38.26200 -45.59400 1.000 44.55000  ? 408  ALA B C   1 
ATOM   6944  O O   . ALA B 1 389 ? 15.80600  -38.79700 -45.31200 1.000 54.24000  ? 408  ALA B O   1 
ATOM   6945  C CB  . ALA B 1 389 ? 18.27700  -39.31200 -47.39500 1.000 34.43000  ? 408  ALA B CB  1 
ATOM   6946  N N   . MET B 1 390 ? 17.69500  -37.75800 -44.66400 1.000 48.38000  ? 409  MET B N   1 
ATOM   6947  C CA  . MET B 1 390 ? 17.30300  -37.72100 -43.26000 1.000 50.96000  ? 409  MET B CA  1 
ATOM   6948  C C   . MET B 1 390 ? 16.07100  -36.85500 -43.04100 1.000 47.92000  ? 409  MET B C   1 
ATOM   6949  O O   . MET B 1 390 ? 15.14600  -37.24700 -42.32300 1.000 46.28000  ? 409  MET B O   1 
ATOM   6950  C CB  . MET B 1 390 ? 18.46600  -37.20800 -42.41400 1.000 47.38000  ? 409  MET B CB  1 
ATOM   6951  C CG  . MET B 1 390 ? 19.51100  -38.24200 -42.14500 1.000 51.02000  ? 409  MET B CG  1 
ATOM   6952  S SD  . MET B 1 390 ? 20.84500  -37.60800 -41.11100 1.000 60.97000  ? 409  MET B SD  1 
ATOM   6953  C CE  . MET B 1 390 ? 21.55700  -39.17900 -40.62600 1.000 64.44000  ? 409  MET B CE  1 
ATOM   6954  N N   . VAL B 1 391 ? 16.05200  -35.66000 -43.63400 1.000 46.22000  ? 410  VAL B N   1 
ATOM   6955  C CA  . VAL B 1 391 ? 14.95400  -34.73000 -43.39400 1.000 47.28000  ? 410  VAL B CA  1 
ATOM   6956  C C   . VAL B 1 391 ? 13.65100  -35.30300 -43.92800 1.000 50.83000  ? 410  VAL B C   1 
ATOM   6957  O O   . VAL B 1 391 ? 12.61100  -35.26100 -43.25900 1.000 45.08000  ? 410  VAL B O   1 
ATOM   6958  C CB  . VAL B 1 391 ? 15.27000  -33.36500 -44.02800 1.000 43.64000  ? 410  VAL B CB  1 
ATOM   6959  C CG1 . VAL B 1 391 ? 14.12600  -32.39800 -43.80200 1.000 41.64000  ? 410  VAL B CG1 1 
ATOM   6960  C CG2 . VAL B 1 391 ? 16.58300  -32.80900 -43.48000 1.000 43.88000  ? 410  VAL B CG2 1 
ATOM   6961  N N   . ASN B 1 392 ? 13.69500  -35.87900 -45.12600 1.000 50.37000  ? 411  ASN B N   1 
ATOM   6962  C CA  . ASN B 1 392 ? 12.49900  -36.42800 -45.74000 1.000 51.19000  ? 411  ASN B CA  1 
ATOM   6963  C C   . ASN B 1 392 ? 11.99600  -37.66700 -45.01300 1.000 51.44000  ? 411  ASN B C   1 
ATOM   6964  O O   . ASN B 1 392 ? 10.88900  -38.12900 -45.30500 1.000 53.55000  ? 411  ASN B O   1 
ATOM   6965  C CB  . ASN B 1 392 ? 12.77400  -36.73400 -47.21100 1.000 45.21000  ? 411  ASN B CB  1 
ATOM   6966  C CG  . ASN B 1 392 ? 13.14200  -35.48900 -47.99400 1.000 48.60000  ? 411  ASN B CG  1 
ATOM   6967  O OD1 . ASN B 1 392 ? 12.65600  -34.39700 -47.69900 1.000 50.86000  ? 411  ASN B OD1 1 
ATOM   6968  N ND2 . ASN B 1 392 ? 13.98200  -35.64800 -49.01000 1.000 53.68000  ? 411  ASN B ND2 1 
ATOM   6969  N N   . ALA B 1 393 ? 12.78300  -38.21300 -44.08700 1.000 47.90000  ? 412  ALA B N   1 
ATOM   6970  C CA  . ALA B 1 393 ? 12.36200  -39.30000 -43.21900 1.000 36.64000  ? 412  ALA B CA  1 
ATOM   6971  C C   . ALA B 1 393 ? 11.94800  -38.82200 -41.83200 1.000 43.74000  ? 412  ALA B C   1 
ATOM   6972  O O   . ALA B 1 393 ? 11.59700  -39.65200 -40.98100 1.000 41.43000  ? 412  ALA B O   1 
ATOM   6973  C CB  . ALA B 1 393 ? 13.48600  -40.33300 -43.10000 1.000 41.46000  ? 412  ALA B CB  1 
ATOM   6974  N N   . GLY B 1 394 ? 11.97800  -37.51300 -41.58000 1.000 36.72000  ? 413  GLY B N   1 
ATOM   6975  C CA  . GLY B 1 394 ? 11.65500  -37.02000 -40.25500 1.000 39.64000  ? 413  GLY B CA  1 
ATOM   6976  C C   . GLY B 1 394 ? 12.71600  -37.29600 -39.22000 1.000 42.95000  ? 413  GLY B C   1 
ATOM   6977  O O   . GLY B 1 394 ? 12.42600  -37.26700 -38.02100 1.000 45.98000  ? 413  GLY B O   1 
ATOM   6978  N N   . ASN B 1 395 ? 13.94300  -37.56800 -39.66200 1.000 47.65000  ? 414  ASN B N   1 
ATOM   6979  C CA  . ASN B 1 395 ? 15.08300  -37.83600 -38.78900 1.000 47.22000  ? 414  ASN B CA  1 
ATOM   6980  C C   . ASN B 1 395 ? 15.81900  -36.52800 -38.53400 1.000 44.13000  ? 414  ASN B C   1 
ATOM   6981  O O   . ASN B 1 395 ? 16.48300  -35.99600 -39.42800 1.000 43.45000  ? 414  ASN B O   1 
ATOM   6982  C CB  . ASN B 1 395 ? 15.98000  -38.88700 -39.44100 1.000 46.11000  ? 414  ASN B CB  1 
ATOM   6983  C CG  . ASN B 1 395 ? 17.17700  -39.27500 -38.59300 1.000 46.34000  ? 414  ASN B CG  1 
ATOM   6984  O OD1 . ASN B 1 395 ? 17.56500  -38.58400 -37.64600 1.000 48.26000  ? 414  ASN B OD1 1 
ATOM   6985  N ND2 . ASN B 1 395 ? 17.73700  -40.43600 -38.90100 1.000 49.68000  ? 414  ASN B ND2 1 
ATOM   6986  N N   . THR B 1 396 ? 15.71600  -36.01900 -37.30600 1.000 38.88000  ? 415  THR B N   1 
ATOM   6987  C CA  . THR B 1 396 ? 16.25900  -34.71700 -36.94300 1.000 41.72000  ? 415  THR B CA  1 
ATOM   6988  C C   . THR B 1 396 ? 17.47600  -34.82200 -36.03100 1.000 48.46000  ? 415  THR B C   1 
ATOM   6989  O O   . THR B 1 396 ? 17.79600  -33.86500 -35.31900 1.000 48.80000  ? 415  THR B O   1 
ATOM   6990  C CB  . THR B 1 396 ? 15.18000  -33.86300 -36.27500 1.000 46.71000  ? 415  THR B CB  1 
ATOM   6991  O OG1 . THR B 1 396 ? 14.71200  -34.52000 -35.08800 1.000 43.56000  ? 415  THR B OG1 1 
ATOM   6992  C CG2 . THR B 1 396 ? 14.00600  -33.65100 -37.21800 1.000 47.27000  ? 415  THR B CG2 1 
ATOM   6993  N N   . THR B 1 397 ? 18.16800  -35.96000 -36.03900 1.000 44.49000  ? 416  THR B N   1 
ATOM   6994  C CA  . THR B 1 397 ? 19.26700  -36.15200 -35.10400 1.000 42.55000  ? 416  THR B CA  1 
ATOM   6995  C C   . THR B 1 397 ? 20.54800  -35.41100 -35.49200 1.000 47.48000  ? 416  THR B C   1 
ATOM   6996  O O   . THR B 1 397 ? 21.32500  -35.06200 -34.59900 1.000 46.95000  ? 416  THR B O   1 
ATOM   6997  C CB  . THR B 1 397 ? 19.54900  -37.64900 -34.93100 1.000 42.12000  ? 416  THR B CB  1 
ATOM   6998  O OG1 . THR B 1 397 ? 19.81200  -38.24800 -36.20800 1.000 43.39000  ? 416  THR B OG1 1 
ATOM   6999  C CG2 . THR B 1 397 ? 18.35400  -38.33300 -34.29100 1.000 45.21000  ? 416  THR B CG2 1 
ATOM   7000  N N   . TYR B 1 398 ? 20.79300  -35.13600 -36.77300 1.000 47.55000  ? 417  TYR B N   1 
ATOM   7001  C CA  . TYR B 1 398 ? 22.10600  -34.63000 -37.16800 1.000 48.02000  ? 417  TYR B CA  1 
ATOM   7002  C C   . TYR B 1 398 ? 22.24700  -33.13700 -36.89300 1.000 51.04000  ? 417  TYR B C   1 
ATOM   7003  O O   . TYR B 1 398 ? 21.40900  -32.33200 -37.31100 1.000 45.77000  ? 417  TYR B O   1 
ATOM   7004  C CB  . TYR B 1 398 ? 22.39100  -34.88900 -38.64500 1.000 46.91000  ? 417  TYR B CB  1 
ATOM   7005  C CG  . TYR B 1 398 ? 23.76000  -34.38000 -39.08200 1.000 55.36000  ? 417  TYR B CG  1 
ATOM   7006  C CD1 . TYR B 1 398 ? 24.91800  -35.13000 -38.86600 1.000 50.71000  ? 417  TYR B CD1 1 
ATOM   7007  C CD2 . TYR B 1 398 ? 23.89700  -33.12800 -39.68000 1.000 53.83000  ? 417  TYR B CD2 1 
ATOM   7008  C CE1 . TYR B 1 398 ? 26.16700  -34.65700 -39.26300 1.000 50.73000  ? 417  TYR B CE1 1 
ATOM   7009  C CE2 . TYR B 1 398 ? 25.14000  -32.64600 -40.07400 1.000 52.97000  ? 417  TYR B CE2 1 
ATOM   7010  C CZ  . TYR B 1 398 ? 26.26900  -33.41000 -39.86700 1.000 56.02000  ? 417  TYR B CZ  1 
ATOM   7011  O OH  . TYR B 1 398 ? 27.49600  -32.91300 -40.26800 1.000 52.07000  ? 417  TYR B OH  1 
ATOM   7012  N N   . THR B 1 399 ? 23.34100  -32.77500 -36.22500 1.000 51.46000  ? 418  THR B N   1 
ATOM   7013  C CA  . THR B 1 399 ? 23.78400  -31.39800 -36.05800 1.000 48.14000  ? 418  THR B CA  1 
ATOM   7014  C C   . THR B 1 399 ? 25.20700  -31.33300 -36.57900 1.000 47.21000  ? 418  THR B C   1 
ATOM   7015  O O   . THR B 1 399 ? 26.04000  -32.14600 -36.16900 1.000 49.84000  ? 418  THR B O   1 
ATOM   7016  C CB  . THR B 1 399 ? 23.77300  -30.98100 -34.59000 1.000 42.47000  ? 418  THR B CB  1 
ATOM   7017  O OG1 . THR B 1 399 ? 22.52900  -31.35100 -33.99700 1.000 57.78000  ? 418  THR B OG1 1 
ATOM   7018  C CG2 . THR B 1 399 ? 23.94300  -29.48000 -34.46700 1.000 39.56000  ? 418  THR B CG2 1 
ATOM   7019  N N   . GLY B 1 400 ? 25.49500  -30.39300 -37.46400 1.000 48.63000  ? 419  GLY B N   1 
ATOM   7020  C CA  . GLY B 1 400 ? 26.85800  -30.21300 -37.92000 1.000 46.37000  ? 419  GLY B CA  1 
ATOM   7021  C C   . GLY B 1 400 ? 26.92500  -29.63200 -39.31800 1.000 43.84000  ? 419  GLY B C   1 
ATOM   7022  O O   . GLY B 1 400 ? 25.96100  -29.07100 -39.83500 1.000 45.04000  ? 419  GLY B O   1 
ATOM   7023  N N   . LEU B 1 401 ? 28.11300  -29.75600 -39.90600 1.000 47.77000  ? 420  LEU B N   1 
ATOM   7024  C CA  . LEU B 1 401 ? 28.35400  -29.22500 -41.23900 1.000 45.64000  ? 420  LEU B CA  1 
ATOM   7025  C C   . LEU B 1 401 ? 27.69800  -30.10800 -42.29500 1.000 43.84000  ? 420  LEU B C   1 
ATOM   7026  O O   . LEU B 1 401 ? 27.64900  -31.33500 -42.16800 1.000 48.16000  ? 420  LEU B O   1 
ATOM   7027  C CB  . LEU B 1 401 ? 29.85900  -29.10900 -41.50900 1.000 43.14000  ? 420  LEU B CB  1 
ATOM   7028  C CG  . LEU B 1 401 ? 30.69900  -28.12900 -40.67600 1.000 42.01000  ? 420  LEU B CG  1 
ATOM   7029  C CD1 . LEU B 1 401 ? 32.17400  -28.21700 -41.06200 1.000 45.34000  ? 420  LEU B CD1 1 
ATOM   7030  C CD2 . LEU B 1 401 ? 30.20500  -26.69700 -40.79700 1.000 42.75000  ? 420  LEU B CD2 1 
ATOM   7031  N N   . VAL B 1 402 ? 27.17600  -29.47200 -43.33500 1.000 41.16000  ? 421  VAL B N   1 
ATOM   7032  C CA  . VAL B 1 402 ? 26.64500  -30.16400 -44.50200 1.000 47.36000  ? 421  VAL B CA  1 
ATOM   7033  C C   . VAL B 1 402 ? 27.29800  -29.55200 -45.72500 1.000 47.43000  ? 421  VAL B C   1 
ATOM   7034  O O   . VAL B 1 402 ? 27.29600  -28.32400 -45.88700 1.000 47.47000  ? 421  VAL B O   1 
ATOM   7035  C CB  . VAL B 1 402 ? 25.10600  -30.07300 -44.59500 1.000 48.44000  ? 421  VAL B CB  1 
ATOM   7036  C CG1 . VAL B 1 402 ? 24.62200  -30.58600 -45.94200 1.000 45.60000  ? 421  VAL B CG1 1 
ATOM   7037  C CG2 . VAL B 1 402 ? 24.45800  -30.88800 -43.48900 1.000 47.29000  ? 421  VAL B CG2 1 
ATOM   7038  N N   . GLU B 1 403 ? 27.85900  -30.40200 -46.57700 1.000 50.64000  ? 422  GLU B N   1 
ATOM   7039  C CA  . GLU B 1 403 ? 28.63300  -29.91800 -47.70800 1.000 52.23000  ? 422  GLU B CA  1 
ATOM   7040  C C   . GLU B 1 403 ? 27.75900  -29.07800 -48.62800 1.000 58.30000  ? 422  GLU B C   1 
ATOM   7041  O O   . GLU B 1 403 ? 26.69300  -29.52500 -49.06800 1.000 55.07000  ? 422  GLU B O   1 
ATOM   7042  C CB  . GLU B 1 403 ? 29.23800  -31.10000 -48.46000 1.000 55.45000  ? 422  GLU B CB  1 
ATOM   7043  C CG  . GLU B 1 403 ? 30.12100  -30.70700 -49.62200 1.000 63.22000  ? 422  GLU B CG  1 
ATOM   7044  C CD  . GLU B 1 403 ? 30.74200  -31.90800 -50.29400 1.000 68.02000  ? 422  GLU B CD  1 
ATOM   7045  O OE1 . GLU B 1 403 ? 30.52300  -33.03800 -49.80700 1.000 67.84000  ? 422  GLU B OE1 1 
ATOM   7046  O OE2 . GLU B 1 403 ? 31.42600  -31.72500 -51.32100 1.000 73.08000  ? 422  GLU B OE2 1 
ATOM   7047  N N   . GLY B 1 404 ? 28.19800  -27.84400 -48.88600 1.000 60.65000  ? 423  GLY B N   1 
ATOM   7048  C CA  . GLY B 1 404 ? 27.53100  -26.95800 -49.80800 1.000 54.18000  ? 423  GLY B CA  1 
ATOM   7049  C C   . GLY B 1 404 ? 26.62800  -25.93300 -49.15300 1.000 56.96000  ? 423  GLY B C   1 
ATOM   7050  O O   . GLY B 1 404 ? 26.34900  -24.89300 -49.75900 1.000 63.08000  ? 423  GLY B O   1 
ATOM   7051  N N   . ILE B 1 405 ? 26.15600  -26.19800 -47.93800 1.000 49.81000  ? 424  ILE B N   1 
ATOM   7052  C CA  . ILE B 1 405 ? 25.25900  -25.26700 -47.26800 1.000 50.26000  ? 424  ILE B CA  1 
ATOM   7053  C C   . ILE B 1 405 ? 25.82400  -24.75000 -45.95400 1.000 55.38000  ? 424  ILE B C   1 
ATOM   7054  O O   . ILE B 1 405 ? 25.43300  -23.65300 -45.52000 1.000 52.91000  ? 424  ILE B O   1 
ATOM   7055  C CB  . ILE B 1 405 ? 23.86700  -25.89300 -47.03800 1.000 50.34000  ? 424  ILE B CB  1 
ATOM   7056  C CG1 . ILE B 1 405 ? 23.85300  -26.85400 -45.86400 1.000 50.21000  ? 424  ILE B CG1 1 
ATOM   7057  C CG2 . ILE B 1 405 ? 23.46600  -26.74600 -48.22700 1.000 55.93000  ? 424  ILE B CG2 1 
ATOM   7058  C CD1 . ILE B 1 405 ? 22.43600  -27.33000 -45.53200 1.000 51.02000  ? 424  ILE B CD1 1 
ATOM   7059  N N   . GLY B 1 406 ? 26.75100  -25.46700 -45.31900 1.000 49.19000  ? 425  GLY B N   1 
ATOM   7060  C CA  . GLY B 1 406 ? 27.34300  -24.99800 -44.08200 1.000 45.39000  ? 425  GLY B CA  1 
ATOM   7061  C C   . GLY B 1 406 ? 26.92600  -25.79600 -42.86200 1.000 44.57000  ? 425  GLY B C   1 
ATOM   7062  O O   . GLY B 1 406 ? 26.98700  -27.03000 -42.85300 1.000 40.40000  ? 425  GLY B O   1 
ATOM   7063  N N   . TYR B 1 407 ? 26.48200  -25.09700 -41.82600 1.000 41.93000  ? 426  TYR B N   1 
ATOM   7064  C CA  . TYR B 1 407 ? 26.13400  -25.71300 -40.55600 1.000 44.56000  ? 426  TYR B CA  1 
ATOM   7065  C C   . TYR B 1 407 ? 24.62000  -25.77000 -40.39200 1.000 43.19000  ? 426  TYR B C   1 
ATOM   7066  O O   . TYR B 1 407 ? 23.91000  -24.79800 -40.68000 1.000 35.23000  ? 426  TYR B O   1 
ATOM   7067  C CB  . TYR B 1 407 ? 26.78200  -24.93700 -39.40700 1.000 43.33000  ? 426  TYR B CB  1 
ATOM   7068  C CG  . TYR B 1 407 ? 26.48100  -25.45100 -38.01600 1.000 44.42000  ? 426  TYR B CG  1 
ATOM   7069  C CD1 . TYR B 1 407 ? 26.98600  -26.66800 -37.57800 1.000 43.36000  ? 426  TYR B CD1 1 
ATOM   7070  C CD2 . TYR B 1 407 ? 25.73500  -24.68800 -37.12000 1.000 46.83000  ? 426  TYR B CD2 1 
ATOM   7071  C CE1 . TYR B 1 407 ? 26.72600  -27.12900 -36.30100 1.000 40.92000  ? 426  TYR B CE1 1 
ATOM   7072  C CE2 . TYR B 1 407 ? 25.46900  -25.13800 -35.84300 1.000 43.95000  ? 426  TYR B CE2 1 
ATOM   7073  C CZ  . TYR B 1 407 ? 25.96700  -26.35900 -35.44000 1.000 47.80000  ? 426  TYR B CZ  1 
ATOM   7074  O OH  . TYR B 1 407 ? 25.70600  -26.80900 -34.16800 1.000 49.73000  ? 426  TYR B OH  1 
ATOM   7075  N N   . VAL B 1 408 ? 24.12800  -26.92400 -39.94500 1.000 43.00000  ? 427  VAL B N   1 
ATOM   7076  C CA  . VAL B 1 408 ? 22.71000  -27.11400 -39.66300 1.000 44.84000  ? 427  VAL B CA  1 
ATOM   7077  C C   . VAL B 1 408 ? 22.54200  -27.46700 -38.19200 1.000 43.51000  ? 427  VAL B C   1 
ATOM   7078  O O   . VAL B 1 408 ? 23.38800  -28.14900 -37.60200 1.000 47.08000  ? 427  VAL B O   1 
ATOM   7079  C CB  . VAL B 1 408 ? 22.06500  -28.20000 -40.55200 1.000 33.73000  ? 427  VAL B CB  1 
ATOM   7080  C CG1 . VAL B 1 408 ? 22.20700  -27.83800 -42.00600 1.000 40.85000  ? 427  VAL B CG1 1 
ATOM   7081  C CG2 . VAL B 1 408 ? 22.65600  -29.57100 -40.26600 1.000 34.50000  ? 427  VAL B CG2 1 
ATOM   7082  N N   . TYR B 1 409 ? 21.45400  -26.98000 -37.60000 1.000 42.33000  ? 428  TYR B N   1 
ATOM   7083  C CA  . TYR B 1 409 ? 21.04200  -27.37400 -36.26300 1.000 40.80000  ? 428  TYR B CA  1 
ATOM   7084  C C   . TYR B 1 409 ? 19.53200  -27.20200 -36.17000 1.000 44.07000  ? 428  TYR B C   1 
ATOM   7085  O O   . TYR B 1 409 ? 18.90800  -26.54200 -37.00500 1.000 41.93000  ? 428  TYR B O   1 
ATOM   7086  C CB  . TYR B 1 409 ? 21.76400  -26.56800 -35.17800 1.000 36.47000  ? 428  TYR B CB  1 
ATOM   7087  C CG  . TYR B 1 409 ? 21.38600  -25.09900 -35.09500 1.000 37.94000  ? 428  TYR B CG  1 
ATOM   7088  C CD1 . TYR B 1 409 ? 21.96500  -24.16500 -35.93600 1.000 36.88000  ? 428  TYR B CD1 1 
ATOM   7089  C CD2 . TYR B 1 409 ? 20.49900  -24.64200 -34.13300 1.000 39.70000  ? 428  TYR B CD2 1 
ATOM   7090  C CE1 . TYR B 1 409 ? 21.64200  -22.82000 -35.85100 1.000 38.27000  ? 428  TYR B CE1 1 
ATOM   7091  C CE2 . TYR B 1 409 ? 20.16500  -23.29600 -34.04000 1.000 38.43000  ? 428  TYR B CE2 1 
ATOM   7092  C CZ  . TYR B 1 409 ? 20.73900  -22.39200 -34.90200 1.000 44.58000  ? 428  TYR B CZ  1 
ATOM   7093  O OH  . TYR B 1 409 ? 20.42000  -21.05600 -34.81500 1.000 45.97000  ? 428  TYR B OH  1 
ATOM   7094  N N   . TRP B 1 410 ? 18.95300  -27.79900 -35.13400 1.000 44.97000  ? 429  TRP B N   1 
ATOM   7095  C CA  . TRP B 1 410 ? 17.51300  -27.86800 -34.96400 1.000 41.60000  ? 429  TRP B CA  1 
ATOM   7096  C C   . TRP B 1 410 ? 17.10800  -27.18500 -33.66400 1.000 40.41000  ? 429  TRP B C   1 
ATOM   7097  O O   . TRP B 1 410 ? 17.79500  -27.30900 -32.64700 1.000 43.87000  ? 429  TRP B O   1 
ATOM   7098  C CB  . TRP B 1 410 ? 17.05000  -29.32000 -34.92900 1.000 39.18000  ? 429  TRP B CB  1 
ATOM   7099  C CG  . TRP B 1 410 ? 17.31800  -30.09700 -36.17000 1.000 45.12000  ? 429  TRP B CG  1 
ATOM   7100  C CD1 . TRP B 1 410 ? 18.43600  -30.83600 -36.44200 1.000 41.49000  ? 429  TRP B CD1 1 
ATOM   7101  C CD2 . TRP B 1 410 ? 16.43400  -30.28000 -37.28500 1.000 46.03000  ? 429  TRP B CD2 1 
ATOM   7102  N NE1 . TRP B 1 410 ? 18.31400  -31.44300 -37.66700 1.000 44.67000  ? 429  TRP B NE1 1 
ATOM   7103  C CE2 . TRP B 1 410 ? 17.09700  -31.11700 -38.20800 1.000 42.64000  ? 429  TRP B CE2 1 
ATOM   7104  C CE3 . TRP B 1 410 ? 15.15400  -29.80500 -37.60000 1.000 49.97000  ? 429  TRP B CE3 1 
ATOM   7105  C CZ2 . TRP B 1 410 ? 16.52400  -31.49400 -39.42300 1.000 43.13000  ? 429  TRP B CZ2 1 
ATOM   7106  C CZ3 . TRP B 1 410 ? 14.58600  -30.17900 -38.81900 1.000 42.66000  ? 429  TRP B CZ3 1 
ATOM   7107  C CH2 . TRP B 1 410 ? 15.27300  -31.01700 -39.71000 1.000 42.28000  ? 429  TRP B CH2 1 
ATOM   7108  N N   . THR B 1 411 ? 15.99000  -26.47200 -33.69800 1.000 40.33000  ? 430  THR B N   1 
ATOM   7109  C CA  . THR B 1 411 ? 15.32600  -25.99700 -32.49400 1.000 40.85000  ? 430  THR B CA  1 
ATOM   7110  C C   . THR B 1 411 ? 13.92500  -26.59000 -32.42700 1.000 42.48000  ? 430  THR B C   1 
ATOM   7111  O O   . THR B 1 411 ? 13.29000  -26.86600 -33.45100 1.000 41.71000  ? 430  THR B O   1 
ATOM   7112  C CB  . THR B 1 411 ? 15.25200  -24.46800 -32.44200 1.000 42.60000  ? 430  THR B CB  1 
ATOM   7113  O OG1 . THR B 1 411 ? 14.63300  -23.98100 -33.63700 1.000 44.06000  ? 430  THR B OG1 1 
ATOM   7114  C CG2 . THR B 1 411 ? 16.63900  -23.87100 -32.28800 1.000 41.69000  ? 430  THR B CG2 1 
ATOM   7115  N N   . THR B 1 412 ? 13.45200  -26.79400 -31.20800 1.000 39.26000  ? 431  THR B N   1 
ATOM   7116  C CA  . THR B 1 412 ? 12.23300  -27.54100 -30.96400 1.000 41.54000  ? 431  THR B CA  1 
ATOM   7117  C C   . THR B 1 412 ? 11.19700  -26.66000 -30.28400 1.000 46.10000  ? 431  THR B C   1 
ATOM   7118  O O   . THR B 1 412 ? 11.52000  -25.87600 -29.38600 1.000 41.53000  ? 431  THR B O   1 
ATOM   7119  C CB  . THR B 1 412 ? 12.52100  -28.77000 -30.10900 1.000 41.02000  ? 431  THR B CB  1 
ATOM   7120  O OG1 . THR B 1 412 ? 13.43900  -29.61600 -30.80800 1.000 41.76000  ? 431  THR B OG1 1 
ATOM   7121  C CG2 . THR B 1 412 ? 11.24500  -29.55200 -29.82800 1.000 37.74000  ? 431  THR B CG2 1 
ATOM   7122  N N   . GLU B 1 413 ? 9.95300   -26.78900 -30.73200 1.000 40.47000  ? 432  GLU B N   1 
ATOM   7123  C CA  . GLU B 1 413 ? 8.82200   -26.15100 -30.09000 1.000 38.49000  ? 432  GLU B CA  1 
ATOM   7124  C C   . GLU B 1 413 ? 7.66200   -27.13200 -30.09000 1.000 39.71000  ? 432  GLU B C   1 
ATOM   7125  O O   . GLU B 1 413 ? 7.53500   -27.96900 -30.99300 1.000 36.01000  ? 432  GLU B O   1 
ATOM   7126  C CB  . GLU B 1 413 ? 8.40000   -24.84600 -30.78700 1.000 36.09000  ? 432  GLU B CB  1 
ATOM   7127  C CG  . GLU B 1 413 ? 7.21300   -24.22700 -30.08900 1.000 38.41000  ? 432  GLU B CG  1 
ATOM   7128  C CD  . GLU B 1 413 ? 7.58500   -23.66700 -28.74100 1.000 43.79000  ? 432  GLU B CD  1 
ATOM   7129  O OE1 . GLU B 1 413 ? 8.54200   -22.86800 -28.68300 1.000 53.81000  ? 432  GLU B OE1 1 
ATOM   7130  O OE2 . GLU B 1 413 ? 7.01600   -24.12000 -27.72400 1.000 45.33000  ? 432  GLU B OE2 1 
ATOM   7131  N N   . THR B 1 414 ? 6.82400   -27.03200 -29.06200 1.000 38.31000  ? 433  THR B N   1 
ATOM   7132  C CA  . THR B 1 414 ? 5.58100   -27.78700 -28.99300 1.000 45.24000  ? 433  THR B CA  1 
ATOM   7133  C C   . THR B 1 414 ? 4.40200   -26.88900 -29.35700 1.000 37.69000  ? 433  THR B C   1 
ATOM   7134  O O   . THR B 1 414 ? 4.25800   -25.78600 -28.81600 1.000 40.21000  ? 433  THR B O   1 
ATOM   7135  C CB  . THR B 1 414 ? 5.40300   -28.39200 -27.60200 1.000 41.57000  ? 433  THR B CB  1 
ATOM   7136  O OG1 . THR B 1 414 ? 6.49400   -29.29100 -27.35900 1.000 40.64000  ? 433  THR B OG1 1 
ATOM   7137  C CG2 . THR B 1 414 ? 4.09800   -29.16300 -27.51000 1.000 39.69000  ? 433  THR B CG2 1 
ATOM   7138  N N   . LEU B 1 415 ? 3.57300   -27.35900 -30.28200 1.000 43.10000  ? 434  LEU B N   1 
ATOM   7139  C CA  . LEU B 1 415 ? 2.35400   -26.66500 -30.68000 1.000 41.90000  ? 434  LEU B CA  1 
ATOM   7140  C C   . LEU B 1 415 ? 1.15800   -27.30400 -29.97900 1.000 40.33000  ? 434  LEU B C   1 
ATOM   7141  O O   . LEU B 1 415 ? 1.10400   -28.52800 -29.83500 1.000 41.44000  ? 434  LEU B O   1 
ATOM   7142  C CB  . LEU B 1 415 ? 2.17800   -26.74300 -32.19700 1.000 40.94000  ? 434  LEU B CB  1 
ATOM   7143  C CG  . LEU B 1 415 ? 3.32000   -26.19900 -33.07500 1.000 44.41000  ? 434  LEU B CG  1 
ATOM   7144  C CD1 . LEU B 1 415 ? 3.03500   -26.44100 -34.56600 1.000 34.11000  ? 434  LEU B CD1 1 
ATOM   7145  C CD2 . LEU B 1 415 ? 3.59900   -24.72900 -32.80300 1.000 38.42000  ? 434  LEU B CD2 1 
ATOM   7146  N N   . TYR B 1 416 ? 0.20500   -26.48700 -29.52800 1.000 40.33000  ? 435  TYR B N   1 
ATOM   7147  C CA  . TYR B 1 416 ? -1.06200  -27.01800 -29.02700 1.000 37.87000  ? 435  TYR B CA  1 
ATOM   7148  C C   . TYR B 1 416 ? -2.20100  -26.67400 -29.97000 1.000 38.50000  ? 435  TYR B C   1 
ATOM   7149  O O   . TYR B 1 416 ? -2.23700  -25.57900 -30.53900 1.000 39.16000  ? 435  TYR B O   1 
ATOM   7150  C CB  . TYR B 1 416 ? -1.46700  -26.50900 -27.64000 1.000 41.40000  ? 435  TYR B CB  1 
ATOM   7151  C CG  . TYR B 1 416 ? -0.58800  -26.94000 -26.49100 1.000 45.40000  ? 435  TYR B CG  1 
ATOM   7152  C CD1 . TYR B 1 416 ? 0.77100   -27.14000 -26.65500 1.000 41.66000  ? 435  TYR B CD1 1 
ATOM   7153  C CD2 . TYR B 1 416 ? -1.16600  -27.37100 -25.30500 1.000 41.13000  ? 435  TYR B CD2 1 
ATOM   7154  C CE1 . TYR B 1 416 ? 1.55300   -27.58000 -25.61000 1.000 46.54000  ? 435  TYR B CE1 1 
ATOM   7155  C CE2 . TYR B 1 416 ? -0.40000  -27.84200 -24.26600 1.000 54.02000  ? 435  TYR B CE2 1 
ATOM   7156  C CZ  . TYR B 1 416 ? 0.96000   -27.94200 -24.42700 1.000 50.82000  ? 435  TYR B CZ  1 
ATOM   7157  O OH  . TYR B 1 416 ? 1.73700   -28.39800 -23.40400 1.000 61.73000  ? 435  TYR B OH  1 
ATOM   7158  N N   . PHE B 1 417 ? -3.14900  -27.59900 -30.12100 1.000 41.11000  ? 436  PHE B N   1 
ATOM   7159  C CA  . PHE B 1 417 ? -4.35700  -27.27500 -30.86100 1.000 39.84000  ? 436  PHE B CA  1 
ATOM   7160  C C   . PHE B 1 417 ? -5.59600  -27.71500 -30.09200 1.000 40.13000  ? 436  PHE B C   1 
ATOM   7161  O O   . PHE B 1 417 ? -5.55000  -28.63400 -29.26800 1.000 34.81000  ? 436  PHE B O   1 
ATOM   7162  C CB  . PHE B 1 417 ? -4.46600  -27.89600 -32.27900 1.000 37.35000  ? 436  PHE B CB  1 
ATOM   7163  C CG  . PHE B 1 417 ? -3.25600  -27.71500 -33.15400 1.000 39.46000  ? 436  PHE B CG  1 
ATOM   7164  C CD1 . PHE B 1 417 ? -1.97800  -28.06700 -32.73800 1.000 43.54000  ? 436  PHE B CD1 1 
ATOM   7165  C CD2 . PHE B 1 417 ? -3.38400  -26.96300 -34.31000 1.000 38.76000  ? 436  PHE B CD2 1 
ATOM   7166  C CE1 . PHE B 1 417 ? -0.88200  -27.85600 -33.56100 1.000 39.91000  ? 436  PHE B CE1 1 
ATOM   7167  C CE2 . PHE B 1 417 ? -2.29500  -26.70800 -35.12100 1.000 37.61000  ? 436  PHE B CE2 1 
ATOM   7168  C CZ  . PHE B 1 417 ? -1.03900  -27.15400 -34.74600 1.000 43.71000  ? 436  PHE B CZ  1 
ATOM   7169  N N   . ILE B 1 418 ? -6.71300  -27.04000 -30.38600 1.000 37.18000  ? 437  ILE B N   1 
ATOM   7170  C CA  . ILE B 1 418 ? -8.04000  -27.42500 -29.91000 1.000 40.97000  ? 437  ILE B CA  1 
ATOM   7171  C C   . ILE B 1 418 ? -8.81600  -28.05300 -31.05000 1.000 37.90000  ? 437  ILE B C   1 
ATOM   7172  O O   . ILE B 1 418 ? -8.74800  -27.59900 -32.19800 1.000 35.97000  ? 437  ILE B O   1 
ATOM   7173  C CB  . ILE B 1 418 ? -8.80200  -26.21500 -29.33900 1.000 41.66000  ? 437  ILE B CB  1 
ATOM   7174  C CG1 . ILE B 1 418 ? -10.11600 -26.67500 -28.71700 1.000 40.21000  ? 437  ILE B CG1 1 
ATOM   7175  C CG2 . ILE B 1 418 ? -9.05300  -25.17000 -30.42500 1.000 36.25000  ? 437  ILE B CG2 1 
ATOM   7176  C CD1 . ILE B 1 418 ? -10.75400 -25.65100 -27.81800 1.000 43.70000  ? 437  ILE B CD1 1 
ATOM   7177  N N   . ARG B 1 419 ? -9.55800  -29.09700 -30.74800 1.000 40.93000  ? 438  ARG B N   1 
ATOM   7178  C CA  . ARG B 1 419 ? -10.46600 -29.61700 -31.75700 1.000 43.60000  ? 438  ARG B CA  1 
ATOM   7179  C C   . ARG B 1 419 ? -11.71300 -28.77800 -31.83400 1.000 42.04000  ? 438  ARG B C   1 
ATOM   7180  O O   . ARG B 1 419 ? -12.46700 -28.66200 -30.86400 1.000 44.30000  ? 438  ARG B O   1 
ATOM   7181  C CB  . ARG B 1 419 ? -10.77500 -31.08700 -31.52400 1.000 38.91000  ? 438  ARG B CB  1 
ATOM   7182  C CG  . ARG B 1 419 ? -11.98200 -31.65500 -32.25400 1.000 43.98000  ? 438  ARG B CG  1 
ATOM   7183  C CD  . ARG B 1 419 ? -11.34700 -32.71700 -33.13700 1.000 47.80000  ? 438  ARG B CD  1 
ATOM   7184  N NE  . ARG B 1 419 ? -11.75000 -34.09300 -32.90800 1.000 47.39000  ? 438  ARG B NE  1 
ATOM   7185  C CZ  . ARG B 1 419 ? -12.65700 -34.78600 -33.57100 1.000 46.16000  ? 438  ARG B CZ  1 
ATOM   7186  N NH1 . ARG B 1 419 ? -13.42100 -34.23400 -34.49000 1.000 43.94000  ? 438  ARG B NH1 1 
ATOM   7187  N NH2 . ARG B 1 419 ? -12.77000 -36.09000 -33.32600 1.000 58.82000  ? 438  ARG B NH2 1 
ATOM   7188  N N   . THR B 1 420 ? -11.92400 -28.18200 -32.99600 1.000 43.81000  ? 439  THR B N   1 
ATOM   7189  C CA  . THR B 1 420 ? -13.10400 -27.39900 -33.32100 1.000 45.16000  ? 439  THR B CA  1 
ATOM   7190  C C   . THR B 1 420 ? -14.23000 -28.28400 -33.82700 1.000 50.06000  ? 439  THR B C   1 
ATOM   7191  O O   . THR B 1 420 ? -15.32200 -27.79200 -34.11200 1.000 58.15000  ? 439  THR B O   1 
ATOM   7192  C CB  . THR B 1 420 ? -12.75300 -26.34300 -34.36800 1.000 45.78000  ? 439  THR B CB  1 
ATOM   7193  O OG1 . THR B 1 420 ? -12.38300 -27.00200 -35.59800 1.000 37.24000  ? 439  THR B OG1 1 
ATOM   7194  C CG2 . THR B 1 420 ? -11.56600 -25.50400 -33.88700 1.000 42.47000  ? 439  THR B CG2 1 
ATOM   7195  N N   . ASN B 1 421 ? -14.01000 -29.59400 -33.85400 1.000 52.75000  ? 440  ASN B N   1 
ATOM   7196  C CA  . ASN B 1 421 ? -14.85700 -30.52600 -34.57200 1.000 53.22000  ? 440  ASN B CA  1 
ATOM   7197  C C   . ASN B 1 421 ? -15.32000 -31.68700 -33.70000 1.000 50.65000  ? 440  ASN B C   1 
ATOM   7198  O O   . ASN B 1 421 ? -15.60900 -32.76600 -34.23900 1.000 46.16000  ? 440  ASN B O   1 
ATOM   7199  C CB  . ASN B 1 421 ? -14.00600 -31.15100 -35.68100 1.000 46.39000  ? 440  ASN B CB  1 
ATOM   7200  C CG  . ASN B 1 421 ? -14.80400 -31.55100 -36.87300 1.000 50.15000  ? 440  ASN B CG  1 
ATOM   7201  O OD1 . ASN B 1 421 ? -14.31300 -32.30400 -37.72500 1.000 51.78000  ? 440  ASN B OD1 1 
ATOM   7202  N ND2 . ASN B 1 421 ? -15.93900 -30.91400 -37.05600 1.000 64.31000  ? 440  ASN B ND2 1 
ATOM   7203  N N   . PRO B 1 422 ? -15.48900 -31.52100 -32.38200 1.000 44.14000  ? 441  PRO B N   1 
ATOM   7204  C CA  . PRO B 1 422 ? -15.46200 -32.73000 -31.52500 1.000 50.40000  ? 441  PRO B CA  1 
ATOM   7205  C C   . PRO B 1 422 ? -16.72500 -33.54900 -31.64500 1.000 52.44000  ? 441  PRO B C   1 
ATOM   7206  O O   . PRO B 1 422 ? -16.68900 -34.77900 -31.42900 1.000 46.73000  ? 441  PRO B O   1 
ATOM   7207  C CB  . PRO B 1 422 ? -15.26000 -32.16300 -30.10500 1.000 42.28000  ? 441  PRO B CB  1 
ATOM   7208  C CG  . PRO B 1 422 ? -15.88800 -30.83800 -30.16900 1.000 45.55000  ? 441  PRO B CG  1 
ATOM   7209  C CD  . PRO B 1 422 ? -15.68200 -30.29800 -31.56300 1.000 41.82000  ? 441  PRO B CD  1 
ATOM   7210  N N   . GLU B 1 423 ? -17.83500 -32.92400 -31.99300 1.000 46.74000  ? 442  GLU B N   1 
ATOM   7211  C CA  . GLU B 1 423 ? -19.10700 -33.60500 -32.10500 1.000 50.18000  ? 442  GLU B CA  1 
ATOM   7212  C C   . GLU B 1 423 ? -19.63100 -33.70000 -33.53400 1.000 53.12000  ? 442  GLU B C   1 
ATOM   7213  O O   . GLU B 1 423 ? -20.73500 -34.22200 -33.74000 1.000 56.89000  ? 442  GLU B O   1 
ATOM   7214  C CB  . GLU B 1 423 ? -20.13000 -32.88800 -31.20500 1.000 50.37000  ? 442  GLU B CB  1 
ATOM   7215  C CG  . GLU B 1 423 ? -19.95400 -33.27900 -29.75600 1.000 50.00000  ? 442  GLU B CG  1 
ATOM   7216  C CD  . GLU B 1 423 ? -20.73900 -32.41400 -28.78900 1.000 53.87000  ? 442  GLU B CD  1 
ATOM   7217  O OE1 . GLU B 1 423 ? -21.05000 -31.24600 -29.12100 1.000 50.34000  ? 442  GLU B OE1 1 
ATOM   7218  O OE2 . GLU B 1 423 ? -21.10500 -32.93600 -27.71500 1.000 56.04000  ? 442  GLU B OE2 1 
ATOM   7219  N N   . GLN B 1 424 ? -18.88000 -33.22000 -34.52800 1.000 59.54000  ? 443  GLN B N   1 
ATOM   7220  C CA  . GLN B 1 424 ? -19.34900 -33.35700 -35.89800 1.000 45.47000  ? 443  GLN B CA  1 
ATOM   7221  C C   . GLN B 1 424 ? -19.39300 -34.83200 -36.26900 1.000 48.89000  ? 443  GLN B C   1 
ATOM   7222  O O   . GLN B 1 424 ? -18.56200 -35.63200 -35.82600 1.000 55.93000  ? 443  GLN B O   1 
ATOM   7223  C CB  . GLN B 1 424 ? -18.47600 -32.59100 -36.87600 1.000 44.62000  ? 443  GLN B CB  1 
ATOM   7224  C CG  . GLN B 1 424 ? -19.06000 -32.57400 -38.28000 1.000 46.80000  ? 443  GLN B CG  1 
ATOM   7225  C CD  . GLN B 1 424 ? -18.16300 -31.92600 -39.32000 1.000 58.25000  ? 443  GLN B CD  1 
ATOM   7226  O OE1 . GLN B 1 424 ? -17.00800 -31.59600 -39.05700 1.000 53.20000  ? 443  GLN B OE1 1 
ATOM   7227  N NE2 . GLN B 1 424 ? -18.70600 -31.74300 -40.53200 1.000 59.06000  ? 443  GLN B NE2 1 
ATOM   7228  N N   . LEU B 1 425 ? -20.39300 -35.18200 -37.06800 1.000 49.59000  ? 444  LEU B N   1 
ATOM   7229  C CA  . LEU B 1 425 ? -20.73800 -36.56400 -37.35800 1.000 43.19000  ? 444  LEU B CA  1 
ATOM   7230  C C   . LEU B 1 425 ? -19.85400 -37.12700 -38.45800 1.000 41.61000  ? 444  LEU B C   1 
ATOM   7231  O O   . LEU B 1 425 ? -19.79800 -36.56800 -39.55800 1.000 40.93000  ? 444  LEU B O   1 
ATOM   7232  C CB  . LEU B 1 425 ? -22.20400 -36.63200 -37.77500 1.000 41.51000  ? 444  LEU B CB  1 
ATOM   7233  C CG  . LEU B 1 425 ? -22.74200 -37.94500 -38.32600 1.000 43.23000  ? 444  LEU B CG  1 
ATOM   7234  C CD1 . LEU B 1 425 ? -22.64500 -39.06000 -37.30200 1.000 39.34000  ? 444  LEU B CD1 1 
ATOM   7235  C CD2 . LEU B 1 425 ? -24.17600 -37.72200 -38.77500 1.000 46.03000  ? 444  LEU B CD2 1 
ATOM   7236  N N   . TRP B 1 426 ? -19.16800 -38.23300 -38.15800 1.000 40.82000  ? 445  TRP B N   1 
ATOM   7237  C CA  . TRP B 1 426 ? -18.46300 -39.02400 -39.16400 1.000 38.98000  ? 445  TRP B CA  1 
ATOM   7238  C C   . TRP B 1 426 ? -17.50600 -38.17000 -40.00400 1.000 41.43000  ? 445  TRP B C   1 
ATOM   7239  O O   . TRP B 1 426 ? -17.48400 -38.24900 -41.23300 1.000 43.99000  ? 445  TRP B O   1 
ATOM   7240  C CB  . TRP B 1 426 ? -19.48100 -39.71800 -40.06100 1.000 37.26000  ? 445  TRP B CB  1 
ATOM   7241  C CG  . TRP B 1 426 ? -20.27100 -40.79800 -39.40100 1.000 42.31000  ? 445  TRP B CG  1 
ATOM   7242  C CD1 . TRP B 1 426 ? -19.89900 -41.55000 -38.32300 1.000 39.13000  ? 445  TRP B CD1 1 
ATOM   7243  C CD2 . TRP B 1 426 ? -21.61500 -41.18400 -39.71900 1.000 35.97000  ? 445  TRP B CD2 1 
ATOM   7244  N NE1 . TRP B 1 426 ? -20.91100 -42.42200 -37.98800 1.000 41.96000  ? 445  TRP B NE1 1 
ATOM   7245  C CE2 . TRP B 1 426 ? -21.98000 -42.20800 -38.82000 1.000 41.62000  ? 445  TRP B CE2 1 
ATOM   7246  C CE3 . TRP B 1 426 ? -22.54100 -40.76900 -40.68300 1.000 46.11000  ? 445  TRP B CE3 1 
ATOM   7247  C CZ2 . TRP B 1 426 ? -23.23600 -42.83600 -38.86300 1.000 44.62000  ? 445  TRP B CZ2 1 
ATOM   7248  C CZ3 . TRP B 1 426 ? -23.79400 -41.39400 -40.72800 1.000 45.06000  ? 445  TRP B CZ3 1 
ATOM   7249  C CH2 . TRP B 1 426 ? -24.12500 -42.41700 -39.82400 1.000 37.11000  ? 445  TRP B CH2 1 
ATOM   7250  N N   . ALA B 1 427 ? -16.70500 -37.33900 -39.34400 1.000 34.22000  ? 446  ALA B N   1 
ATOM   7251  C CA  . ALA B 1 427 ? -15.93300 -36.33200 -40.06800 1.000 37.43000  ? 446  ALA B CA  1 
ATOM   7252  C C   . ALA B 1 427 ? -14.43500 -36.47100 -39.80700 1.000 37.34000  ? 446  ALA B C   1 
ATOM   7253  O O   . ALA B 1 427 ? -13.99000 -37.10200 -38.84300 1.000 34.64000  ? 446  ALA B O   1 
ATOM   7254  C CB  . ALA B 1 427 ? -16.38600 -34.91500 -39.71700 1.000 33.20000  ? 446  ALA B CB  1 
ATOM   7255  N N   . ILE B 1 428 ? -13.66300 -35.85600 -40.69100 1.000 40.66000  ? 447  ILE B N   1 
ATOM   7256  C CA  . ILE B 1 428 ? -12.22600 -35.67700 -40.46900 1.000 41.33000  ? 447  ILE B CA  1 
ATOM   7257  C C   . ILE B 1 428 ? -12.01800 -34.70900 -39.31200 1.000 42.39000  ? 447  ILE B C   1 
ATOM   7258  O O   . ILE B 1 428 ? -12.56100 -33.59100 -39.34000 1.000 41.97000  ? 447  ILE B O   1 
ATOM   7259  C CB  . ILE B 1 428 ? -11.55000 -35.17400 -41.74800 1.000 44.01000  ? 447  ILE B CB  1 
ATOM   7260  C CG1 . ILE B 1 428 ? -11.39500 -36.32700 -42.73500 1.000 46.15000  ? 447  ILE B CG1 1 
ATOM   7261  C CG2 . ILE B 1 428 ? -10.22400 -34.50900 -41.45300 1.000 49.53000  ? 447  ILE B CG2 1 
ATOM   7262  C CD1 . ILE B 1 428 ? -10.56500 -37.46100 -42.15500 1.000 50.53000  ? 447  ILE B CD1 1 
ATOM   7263  N N   . PRO B 1 429 ? -11.26300 -35.09200 -38.28300 1.000 44.76000  ? 448  PRO B N   1 
ATOM   7264  C CA  . PRO B 1 429 ? -11.02600 -34.18600 -37.15300 1.000 37.92000  ? 448  PRO B CA  1 
ATOM   7265  C C   . PRO B 1 429 ? -10.38300 -32.89600 -37.61400 1.000 40.61000  ? 448  PRO B C   1 
ATOM   7266  O O   . PRO B 1 429 ? -9.49000  -32.89600 -38.45900 1.000 45.21000  ? 448  PRO B O   1 
ATOM   7267  C CB  . PRO B 1 429 ? -10.07900 -34.98200 -36.25600 1.000 36.50000  ? 448  PRO B CB  1 
ATOM   7268  C CG  . PRO B 1 429 ? -10.33300 -36.40900 -36.62200 1.000 41.87000  ? 448  PRO B CG  1 
ATOM   7269  C CD  . PRO B 1 429 ? -10.64000 -36.41000 -38.08500 1.000 38.50000  ? 448  PRO B CD  1 
ATOM   7270  N N   . LYS B 1 430 ? -10.84500 -31.78400 -37.06100 1.000 41.20000  ? 449  LYS B N   1 
ATOM   7271  C CA  . LYS B 1 430 ? -10.24400 -30.50500 -37.39300 1.000 42.34000  ? 449  LYS B CA  1 
ATOM   7272  C C   . LYS B 1 430 ? -9.77500  -29.79900 -36.13400 1.000 39.37000  ? 449  LYS B C   1 
ATOM   7273  O O   . LYS B 1 430 ? -10.40800 -29.88700 -35.07500 1.000 36.95000  ? 449  LYS B O   1 
ATOM   7274  C CB  . LYS B 1 430 ? -11.19600 -29.62300 -38.17400 1.000 35.61000  ? 449  LYS B CB  1 
ATOM   7275  C CG  . LYS B 1 430 ? -11.81500 -30.41600 -39.27700 1.000 54.11000  ? 449  LYS B CG  1 
ATOM   7276  C CD  . LYS B 1 430 ? -12.07500 -29.58800 -40.47800 1.000 61.60000  ? 449  LYS B CD  1 
ATOM   7277  C CE  . LYS B 1 430 ? -12.86000 -30.36900 -41.46800 1.000 63.15000  ? 449  LYS B CE  1 
ATOM   7278  N NZ  . LYS B 1 430 ? -14.24500 -29.97500 -41.18400 1.000 83.34000  ? 449  LYS B NZ  1 
ATOM   7279  N N   . TYR B 1 431 ? -8.65900  -29.10100 -36.26400 1.000 38.79000  ? 450  TYR B N   1 
ATOM   7280  C CA  . TYR B 1 431 ? -7.97300  -28.51700 -35.12800 1.000 39.05000  ? 450  TYR B CA  1 
ATOM   7281  C C   . TYR B 1 431 ? -7.62900  -27.07600 -35.44700 1.000 38.22000  ? 450  TYR B C   1 
ATOM   7282  O O   . TYR B 1 431 ? -7.53700  -26.67400 -36.61200 1.000 33.27000  ? 450  TYR B O   1 
ATOM   7283  C CB  . TYR B 1 431 ? -6.70400  -29.29700 -34.77700 1.000 33.78000  ? 450  TYR B CB  1 
ATOM   7284  C CG  . TYR B 1 431 ? -6.98300  -30.71200 -34.34100 1.000 35.33000  ? 450  TYR B CG  1 
ATOM   7285  C CD1 . TYR B 1 431 ? -7.36300  -31.00200 -33.03300 1.000 42.20000  ? 450  TYR B CD1 1 
ATOM   7286  C CD2 . TYR B 1 431 ? -6.88500  -31.75800 -35.24100 1.000 33.84000  ? 450  TYR B CD2 1 
ATOM   7287  C CE1 . TYR B 1 431 ? -7.62100  -32.30900 -32.63100 1.000 40.90000  ? 450  TYR B CE1 1 
ATOM   7288  C CE2 . TYR B 1 431 ? -7.14100  -33.05700 -34.85500 1.000 36.41000  ? 450  TYR B CE2 1 
ATOM   7289  C CZ  . TYR B 1 431 ? -7.50400  -33.33300 -33.55600 1.000 39.33000  ? 450  TYR B CZ  1 
ATOM   7290  O OH  . TYR B 1 431 ? -7.74900  -34.63800 -33.19500 1.000 36.81000  ? 450  TYR B OH  1 
ATOM   7291  N N   . GLN B 1 432 ? -7.46900  -26.29900 -34.38600 1.000 36.67000  ? 451  GLN B N   1 
ATOM   7292  C CA  . GLN B 1 432 ? -7.04400  -24.91700 -34.49700 1.000 40.02000  ? 451  GLN B CA  1 
ATOM   7293  C C   . GLN B 1 432 ? -6.05000  -24.60400 -33.39200 1.000 39.76000  ? 451  GLN B C   1 
ATOM   7294  O O   . GLN B 1 432 ? -6.31600  -24.87000 -32.21500 1.000 42.26000  ? 451  GLN B O   1 
ATOM   7295  C CB  . GLN B 1 432 ? -8.24700  -23.98600 -34.45800 1.000 38.06000  ? 451  GLN B CB  1 
ATOM   7296  C CG  . GLN B 1 432 ? -7.92100  -22.52600 -34.29800 1.000 44.16000  ? 451  GLN B CG  1 
ATOM   7297  C CD  . GLN B 1 432 ? -9.13000  -21.65300 -34.55100 1.000 46.37000  ? 451  GLN B CD  1 
ATOM   7298  O OE1 . GLN B 1 432 ? -10.09300 -22.08600 -35.17900 1.000 56.09000  ? 451  GLN B OE1 1 
ATOM   7299  N NE2 . GLN B 1 432 ? -9.13300  -20.46200 -33.97000 1.000 54.37000  ? 451  GLN B NE2 1 
ATOM   7300  N N   . GLN B 1 433 ? -4.91300  -24.03600 -33.78900 1.000 37.29000  ? 452  GLN B N   1 
ATOM   7301  C CA  . GLN B 1 433 ? -3.82100  -23.75700 -32.87100 1.000 39.05000  ? 452  GLN B CA  1 
ATOM   7302  C C   . GLN B 1 433 ? -4.23100  -22.73100 -31.82400 1.000 37.58000  ? 452  GLN B C   1 
ATOM   7303  O O   . GLN B 1 433 ? -4.95600  -21.77600 -32.12400 1.000 38.57000  ? 452  GLN B O   1 
ATOM   7304  C CB  . GLN B 1 433 ? -2.61800  -23.25200 -33.67500 1.000 38.45000  ? 452  GLN B CB  1 
ATOM   7305  C CG  . GLN B 1 433 ? -1.37000  -23.03900 -32.87100 1.000 38.92000  ? 452  GLN B CG  1 
ATOM   7306  C CD  . GLN B 1 433 ? -0.22700  -22.53600 -33.72600 1.000 48.25000  ? 452  GLN B CD  1 
ATOM   7307  O OE1 . GLN B 1 433 ? -0.38900  -22.29400 -34.92600 1.000 54.66000  ? 452  GLN B OE1 1 
ATOM   7308  N NE2 . GLN B 1 433 ? 0.93900   -22.37000 -33.11300 1.000 42.72000  ? 452  GLN B NE2 1 
ATOM   7309  N N   . ILE B 1 434 ? -3.74500  -22.91800 -30.59400 1.000 38.10000  ? 453  ILE B N   1 
ATOM   7310  C CA  . ILE B 1 434 ? -4.07300  -22.05900 -29.45600 1.000 37.02000  ? 453  ILE B CA  1 
ATOM   7311  C C   . ILE B 1 434 ? -2.80600  -21.51300 -28.79500 1.000 42.40000  ? 453  ILE B C   1 
ATOM   7312  O O   . ILE B 1 434 ? -1.75400  -22.18100 -28.78300 1.000 40.25000  ? 453  ILE B O   1 
ATOM   7313  C CB  . ILE B 1 434 ? -4.97500  -22.81000 -28.46100 1.000 34.72000  ? 453  ILE B CB  1 
ATOM   7314  C CG1 . ILE B 1 434 ? -4.42600  -24.20800 -28.17400 1.000 33.56000  ? 453  ILE B CG1 1 
ATOM   7315  C CG2 . ILE B 1 434 ? -6.42400  -22.87100 -28.97900 1.000 39.03000  ? 453  ILE B CG2 1 
ATOM   7316  C CD1 . ILE B 1 434 ? -5.15900  -24.96600 -27.09700 1.000 30.90000  ? 453  ILE B CD1 1 
ATOM   7317  N N   . PRO B 1 435 ? -2.85000  -20.29500 -28.24900 1.000 48.72000  ? 454  PRO B N   1 
ATOM   7318  C CA  . PRO B 1 435 ? -1.61200  -19.64100 -27.75900 1.000 43.56000  ? 454  PRO B CA  1 
ATOM   7319  C C   . PRO B 1 435 ? -1.19900  -20.08900 -26.35400 1.000 54.32000  ? 454  PRO B C   1 
ATOM   7320  O O   . PRO B 1 435 ? -1.99000  -20.68000 -25.58100 1.000 45.79000  ? 454  PRO B O   1 
ATOM   7321  C CB  . PRO B 1 435 ? -1.98400  -18.15800 -27.77000 1.000 40.04000  ? 454  PRO B CB  1 
ATOM   7322  C CG  . PRO B 1 435 ? -3.46500  -18.12700 -27.62700 1.000 43.74000  ? 454  PRO B CG  1 
ATOM   7323  C CD  . PRO B 1 435 ? -4.00000  -19.35400 -28.29900 1.000 37.16000  ? 454  PRO B CD  1 
ATOM   7324  N N   . PHE B 1 436 ? 0.05400   -19.75100 -26.00700 1.000 52.01000  ? 455  PHE B N   1 
ATOM   7325  C CA  . PHE B 1 436 ? 0.93200   -20.34800 -25.00600 1.000 55.43000  ? 455  PHE B CA  1 
ATOM   7326  C C   . PHE B 1 436 ? 0.31000   -20.84300 -23.70400 1.000 70.07000  ? 455  PHE B C   1 
ATOM   7327  O O   . PHE B 1 436 ? 0.61900   -21.96700 -23.30100 1.000 84.10000  ? 455  PHE B O   1 
ATOM   7328  C CB  . PHE B 1 436 ? 2.10300   -19.39800 -24.64200 1.000 53.28000  ? 455  PHE B CB  1 
ATOM   7329  C CG  . PHE B 1 436 ? 2.74000   -19.68900 -23.30500 1.000 38.10000  ? 455  PHE B CG  1 
ATOM   7330  C CD1 . PHE B 1 436 ? 3.28600   -20.95100 -23.02200 1.000 45.82000  ? 455  PHE B CD1 1 
ATOM   7331  C CD2 . PHE B 1 436 ? 2.90300   -18.69100 -22.38700 1.000 41.19000  ? 455  PHE B CD2 1 
ATOM   7332  C CE1 . PHE B 1 436 ? 3.89100   -21.18000 -21.78800 1.000 47.42000  ? 455  PHE B CE1 1 
ATOM   7333  C CE2 . PHE B 1 436 ? 3.52400   -18.91800 -21.17000 1.000 48.90000  ? 455  PHE B CE2 1 
ATOM   7334  C CZ  . PHE B 1 436 ? 4.01800   -20.16300 -20.87600 1.000 44.20000  ? 455  PHE B CZ  1 
ATOM   7335  N N   . PRO B 1 437 ? -0.45200  -20.07300 -22.94300 1.000 43.14000  ? 456  PRO B N   1 
ATOM   7336  C CA  . PRO B 1 437 ? -0.99100  -20.69200 -21.70500 1.000 50.60000  ? 456  PRO B CA  1 
ATOM   7337  C C   . PRO B 1 437 ? -1.86000  -21.90400 -22.01700 1.000 52.05000  ? 456  PRO B C   1 
ATOM   7338  O O   . PRO B 1 437 ? -1.85100  -22.88500 -21.25900 1.000 46.22000  ? 456  PRO B O   1 
ATOM   7339  C CB  . PRO B 1 437 ? -1.73200  -19.53600 -21.04100 1.000 65.04000  ? 456  PRO B CB  1 
ATOM   7340  C CG  . PRO B 1 437 ? -1.01100  -18.31300 -21.57300 1.000 57.29000  ? 456  PRO B CG  1 
ATOM   7341  C CD  . PRO B 1 437 ? -0.67200  -18.60200 -22.97500 1.000 57.27000  ? 456  PRO B CD  1 
ATOM   7342  N N   . TYR B 1 438 ? -2.57700  -21.86900 -23.13800 1.000 48.45000  ? 457  TYR B N   1 
ATOM   7343  C CA  . TYR B 1 438 ? -3.37700  -22.94600 -23.70800 1.000 45.99000  ? 457  TYR B CA  1 
ATOM   7344  C C   . TYR B 1 438 ? -4.58500  -23.38300 -22.89500 1.000 42.97000  ? 457  TYR B C   1 
ATOM   7345  O O   . TYR B 1 438 ? -5.31900  -24.28000 -23.32200 1.000 49.70000  ? 457  TYR B O   1 
ATOM   7346  C CB  . TYR B 1 438 ? -2.56400  -24.22100 -23.92700 1.000 44.29000  ? 457  TYR B CB  1 
ATOM   7347  C CG  . TYR B 1 438 ? -1.17300  -24.06100 -24.46000 1.000 44.15000  ? 457  TYR B CG  1 
ATOM   7348  C CD1 . TYR B 1 438 ? -0.93500  -23.49700 -25.69400 1.000 48.28000  ? 457  TYR B CD1 1 
ATOM   7349  C CD2 . TYR B 1 438 ? -0.10500  -24.58400 -23.75300 1.000 50.40000  ? 457  TYR B CD2 1 
ATOM   7350  C CE1 . TYR B 1 438 ? 0.34600   -23.38000 -26.18800 1.000 47.61000  ? 457  TYR B CE1 1 
ATOM   7351  C CE2 . TYR B 1 438 ? 1.19200   -24.48000 -24.24000 1.000 52.13000  ? 457  TYR B CE2 1 
ATOM   7352  C CZ  . TYR B 1 438 ? 1.41300   -23.87000 -25.45100 1.000 52.82000  ? 457  TYR B CZ  1 
ATOM   7353  O OH  . TYR B 1 438 ? 2.69900   -23.76200 -25.93000 1.000 46.85000  ? 457  TYR B OH  1 
ATOM   7354  N N   . PHE B 1 439 ? -4.79800  -22.82000 -21.71700 1.000 44.86000  ? 458  PHE B N   1 
ATOM   7355  C CA  . PHE B 1 439 ? -5.82400  -23.36400 -20.81900 1.000 40.54000  ? 458  PHE B CA  1 
ATOM   7356  C C   . PHE B 1 439 ? -7.18900  -23.25500 -21.49900 1.000 43.81000  ? 458  PHE B C   1 
ATOM   7357  O O   . PHE B 1 439 ? -7.60300  -22.16400 -21.92500 1.000 43.33000  ? 458  PHE B O   1 
ATOM   7358  C CB  . PHE B 1 439 ? -5.83800  -22.63100 -19.47400 1.000 45.79000  ? 458  PHE B CB  1 
ATOM   7359  C CG  . PHE B 1 439 ? -4.54600  -22.72600 -18.69200 1.000 47.50000  ? 458  PHE B CG  1 
ATOM   7360  C CD1 . PHE B 1 439 ? -4.07200  -23.95000 -18.25200 1.000 41.78000  ? 458  PHE B CD1 1 
ATOM   7361  C CD2 . PHE B 1 439 ? -3.87200  -21.57500 -18.31300 1.000 46.62000  ? 458  PHE B CD2 1 
ATOM   7362  C CE1 . PHE B 1 439 ? -2.89100  -24.02700 -17.51400 1.000 39.53000  ? 458  PHE B CE1 1 
ATOM   7363  C CE2 . PHE B 1 439 ? -2.70700  -21.64600 -17.55800 1.000 42.56000  ? 458  PHE B CE2 1 
ATOM   7364  C CZ  . PHE B 1 439 ? -2.21800  -22.87200 -17.16000 1.000 37.02000  ? 458  PHE B CZ  1 
ATOM   7365  N N   . GLN B 1 440 ? -7.85500  -24.38600 -21.65600 1.000 46.46000  ? 459  GLN B N   1 
ATOM   7366  C CA  . GLN B 1 440 ? -9.19900  -24.46400 -22.21500 1.000 45.08000  ? 459  GLN B CA  1 
ATOM   7367  C C   . GLN B 1 440 ? -10.12500 -25.14000 -21.20400 1.000 43.54000  ? 459  GLN B C   1 
ATOM   7368  O O   . GLN B 1 440 ? -9.66300  -25.75300 -20.23500 1.000 39.81000  ? 459  GLN B O   1 
ATOM   7369  C CB  . GLN B 1 440 ? -9.20400  -25.24900 -23.54300 1.000 35.80000  ? 459  GLN B CB  1 
ATOM   7370  C CG  . GLN B 1 440 ? -8.23800  -24.69500 -24.58100 1.000 41.40000  ? 459  GLN B CG  1 
ATOM   7371  C CD  . GLN B 1 440 ? -8.61800  -23.31300 -25.09400 1.000 46.32000  ? 459  GLN B CD  1 
ATOM   7372  O OE1 . GLN B 1 440 ? -9.78900  -23.04100 -25.38200 1.000 35.40000  ? 459  GLN B OE1 1 
ATOM   7373  N NE2 . GLN B 1 440 ? -7.62600  -22.42100 -25.18700 1.000 39.91000  ? 459  GLN B NE2 1 
ATOM   7374  N N   . ARG B 1 441 ? -11.44200 -25.02200 -21.43500 1.000 43.61000  ? 460  ARG B N   1 
ATOM   7375  C CA  . ARG B 1 441 ? -12.42100 -25.77200 -20.65000 1.000 41.51000  ? 460  ARG B CA  1 
ATOM   7376  C C   . ARG B 1 441 ? -12.06200 -27.24700 -20.66800 1.000 41.95000  ? 460  ARG B C   1 
ATOM   7377  O O   . ARG B 1 441 ? -11.49100 -27.76200 -21.63000 1.000 46.41000  ? 460  ARG B O   1 
ATOM   7378  C CB  . ARG B 1 441 ? -13.82800 -25.60500 -21.21000 1.000 48.31000  ? 460  ARG B CB  1 
ATOM   7379  C CG  . ARG B 1 441 ? -14.39400 -24.21000 -21.16300 1.000 46.21000  ? 460  ARG B CG  1 
ATOM   7380  C CD  . ARG B 1 441 ? -14.82900 -23.83300 -19.76500 1.000 47.98000  ? 460  ARG B CD  1 
ATOM   7381  N NE  . ARG B 1 441 ? -15.40400 -22.49400 -19.75200 1.000 50.56000  ? 460  ARG B NE  1 
ATOM   7382  C CZ  . ARG B 1 441 ? -15.77100 -21.83700 -18.66000 1.000 52.92000  ? 460  ARG B CZ  1 
ATOM   7383  N NH1 . ARG B 1 441 ? -15.67100 -22.38200 -17.45700 1.000 53.75000  ? 460  ARG B NH1 1 
ATOM   7384  N NH2 . ARG B 1 441 ? -16.24700 -20.60000 -18.77900 1.000 59.17000  ? 460  ARG B NH2 1 
ATOM   7385  N N   . LYS B 1 442 ? -12.40100 -27.94700 -19.60500 1.000 48.67000  ? 461  LYS B N   1 
ATOM   7386  C CA  . LYS B 1 442 ? -11.96000 -29.33000 -19.56600 1.000 52.42000  ? 461  LYS B CA  1 
ATOM   7387  C C   . LYS B 1 442 ? -12.71100 -30.20600 -20.55500 1.000 50.19000  ? 461  LYS B C   1 
ATOM   7388  O O   . LYS B 1 442 ? -12.23300 -31.29200 -20.89400 1.000 57.70000  ? 461  LYS B O   1 
ATOM   7389  C CB  . LYS B 1 442 ? -12.07300 -29.84700 -18.15900 1.000 56.16000  ? 461  LYS B CB  1 
ATOM   7390  C CG  . LYS B 1 442 ? -11.06200 -29.27200 -17.31800 1.000 57.36000  ? 461  LYS B CG  1 
ATOM   7391  C CD  . LYS B 1 442 ? -11.57900 -29.68800 -15.90800 1.000 77.33000  ? 461  LYS B CD  1 
ATOM   7392  C CE  . LYS B 1 442 ? -13.00800 -29.23600 -15.40100 1.000 75.03000  ? 461  LYS B CE  1 
ATOM   7393  N NZ  . LYS B 1 442 ? -12.89500 -27.74800 -14.98100 1.000 73.06000  ? 461  LYS B NZ  1 
ATOM   7394  N N   . ASP B 1 443 ? -13.82700 -29.73500 -21.09800 1.000 46.18000  ? 462  ASP B N   1 
ATOM   7395  C CA  . ASP B 1 443 ? -14.45100 -30.54200 -22.13400 1.000 57.76000  ? 462  ASP B CA  1 
ATOM   7396  C C   . ASP B 1 443 ? -13.77000 -30.38900 -23.49200 1.000 52.00000  ? 462  ASP B C   1 
ATOM   7397  O O   . ASP B 1 443 ? -14.04500 -31.18600 -24.39600 1.000 54.53000  ? 462  ASP B O   1 
ATOM   7398  C CB  . ASP B 1 443 ? -15.95700 -30.22200 -22.24800 1.000 51.34000  ? 462  ASP B CB  1 
ATOM   7399  C CG  . ASP B 1 443 ? -16.24600 -28.83000 -22.79800 1.000 62.65000  ? 462  ASP B CG  1 
ATOM   7400  O OD1 . ASP B 1 443 ? -15.30800 -28.03400 -23.03600 1.000 64.59000  ? 462  ASP B OD1 1 
ATOM   7401  O OD2 . ASP B 1 443 ? -17.44000 -28.53500 -23.01900 1.000 77.67000  ? 462  ASP B OD2 1 
ATOM   7402  N N   . ALA B 1 444 ? -12.88700 -29.40300 -23.65300 1.000 47.20000  ? 463  ALA B N   1 
ATOM   7403  C CA  . ALA B 1 444 ? -12.18900 -29.21400 -24.92100 1.000 44.11000  ? 463  ALA B CA  1 
ATOM   7404  C C   . ALA B 1 444 ? -11.19300 -30.33900 -25.15600 1.000 39.89000  ? 463  ALA B C   1 
ATOM   7405  O O   . ALA B 1 444 ? -10.54900 -30.82100 -24.22200 1.000 42.66000  ? 463  ALA B O   1 
ATOM   7406  C CB  . ALA B 1 444 ? -11.46000 -27.87300 -24.93800 1.000 43.58000  ? 463  ALA B CB  1 
ATOM   7407  N N   . ILE B 1 445 ? -11.05500 -30.74900 -26.41000 1.000 36.51000  ? 464  ILE B N   1 
ATOM   7408  C CA  . ILE B 1 445 ? -10.06200 -31.74900 -26.78500 1.000 41.37000  ? 464  ILE B CA  1 
ATOM   7409  C C   . ILE B 1 445 ? -8.79000  -31.04200 -27.23900 1.000 39.04000  ? 464  ILE B C   1 
ATOM   7410  O O   . ILE B 1 445 ? -8.81500  -30.22600 -28.16600 1.000 41.63000  ? 464  ILE B O   1 
ATOM   7411  C CB  . ILE B 1 445 ? -10.60000 -32.69200 -27.87100 1.000 42.16000  ? 464  ILE B CB  1 
ATOM   7412  C CG1 . ILE B 1 445 ? -11.72600 -33.54800 -27.29500 1.000 39.30000  ? 464  ILE B CG1 1 
ATOM   7413  C CG2 . ILE B 1 445 ? -9.50400  -33.58500 -28.40000 1.000 34.58000  ? 464  ILE B CG2 1 
ATOM   7414  C CD1 . ILE B 1 445 ? -12.40500 -34.40900 -28.32900 1.000 42.15000  ? 464  ILE B CD1 1 
ATOM   7415  N N   . ILE B 1 446 ? -7.68000  -31.36000 -26.57600 1.000 39.54000  ? 465  ILE B N   1 
ATOM   7416  C CA  . ILE B 1 446 ? -6.38900  -30.71500 -26.78400 1.000 35.52000  ? 465  ILE B CA  1 
ATOM   7417  C C   . ILE B 1 446 ? -5.45000  -31.72700 -27.42200 1.000 42.23000  ? 465  ILE B C   1 
ATOM   7418  O O   . ILE B 1 446 ? -5.44400  -32.90500 -27.04400 1.000 37.84000  ? 465  ILE B O   1 
ATOM   7419  C CB  . ILE B 1 446 ? -5.80400  -30.17600 -25.46700 1.000 37.53000  ? 465  ILE B CB  1 
ATOM   7420  C CG1 . ILE B 1 446 ? -6.75300  -29.15300 -24.83900 1.000 36.91000  ? 465  ILE B CG1 1 
ATOM   7421  C CG2 . ILE B 1 446 ? -4.43500  -29.55700 -25.70100 1.000 40.21000  ? 465  ILE B CG2 1 
ATOM   7422  C CD1 . ILE B 1 446 ? -6.99600  -27.95200 -25.70700 1.000 39.83000  ? 465  ILE B CD1 1 
ATOM   7423  N N   . GLU B 1 447 ? -4.66900  -31.26000 -28.39500 1.000 45.95000  ? 466  GLU B N   1 
ATOM   7424  C CA  . GLU B 1 447 ? -3.77700  -32.06100 -29.22000 1.000 44.65000  ? 466  GLU B CA  1 
ATOM   7425  C C   . GLU B 1 447 ? -2.45400  -31.31500 -29.30800 1.000 43.50000  ? 466  GLU B C   1 
ATOM   7426  O O   . GLU B 1 447 ? -2.44600  -30.11000 -29.58000 1.000 40.71000  ? 466  GLU B O   1 
ATOM   7427  C CB  . GLU B 1 447 ? -4.43400  -32.24000 -30.59400 1.000 48.26000  ? 466  GLU B CB  1 
ATOM   7428  C CG  . GLU B 1 447 ? -3.71200  -32.94000 -31.75300 1.000 57.10000  ? 466  GLU B CG  1 
ATOM   7429  C CD  . GLU B 1 447 ? -3.57000  -34.44200 -31.61000 1.000 63.81000  ? 466  GLU B CD  1 
ATOM   7430  O OE1 . GLU B 1 447 ? -4.05800  -35.01000 -30.59800 1.000 57.79000  ? 466  GLU B OE1 1 
ATOM   7431  O OE2 . GLU B 1 447 ? -3.09800  -35.05900 -32.60500 1.000 65.17000  ? 466  GLU B OE2 1 
ATOM   7432  N N   . THR B 1 448 ? -1.34300  -32.00100 -29.05100 1.000 48.59000  ? 467  THR B N   1 
ATOM   7433  C CA  . THR B 1 448 ? -0.03700  -31.35700 -29.11800 1.000 42.36000  ? 467  THR B CA  1 
ATOM   7434  C C   . THR B 1 448 ? 0.81600   -32.00900 -30.19100 1.000 42.77000  ? 467  THR B C   1 
ATOM   7435  O O   . THR B 1 448 ? 0.77500   -33.22800 -30.37900 1.000 47.15000  ? 467  THR B O   1 
ATOM   7436  C CB  . THR B 1 448 ? 0.71600   -31.40200 -27.78700 1.000 40.65000  ? 467  THR B CB  1 
ATOM   7437  O OG1 . THR B 1 448 ? 0.97200   -32.76000 -27.41700 1.000 46.34000  ? 467  THR B OG1 1 
ATOM   7438  C CG2 . THR B 1 448 ? -0.07700  -30.70100 -26.69500 1.000 48.20000  ? 467  THR B CG2 1 
ATOM   7439  N N   . LYS B 1 449 ? 1.58300   -31.18300 -30.89100 1.000 46.34000  ? 468  LYS B N   1 
ATOM   7440  C CA  . LYS B 1 449 ? 2.54100   -31.63200 -31.89100 1.000 46.56000  ? 468  LYS B CA  1 
ATOM   7441  C C   . LYS B 1 449 ? 3.92500   -31.11200 -31.52200 1.000 47.84000  ? 468  LYS B C   1 
ATOM   7442  O O   . LYS B 1 449 ? 4.05800   -30.02600 -30.94500 1.000 44.85000  ? 468  LYS B O   1 
ATOM   7443  C CB  . LYS B 1 449 ? 2.15300   -31.14900 -33.30000 1.000 40.33000  ? 468  LYS B CB  1 
ATOM   7444  C CG  . LYS B 1 449 ? 0.78800   -31.62300 -33.78600 1.000 42.45000  ? 468  LYS B CG  1 
ATOM   7445  C CD  . LYS B 1 449 ? 0.74500   -33.13700 -33.94600 1.000 52.13000  ? 468  LYS B CD  1 
ATOM   7446  C CE  . LYS B 1 449 ? -0.59100  -33.59400 -34.50900 1.000 55.58000  ? 468  LYS B CE  1 
ATOM   7447  N NZ  . LYS B 1 449 ? -0.78200  -35.07500 -34.52800 1.000 59.48000  ? 468  LYS B NZ  1 
ATOM   7448  N N   . THR B 1 450 ? 4.95100   -31.89100 -31.84000 1.000 45.40000  ? 469  THR B N   1 
ATOM   7449  C CA  . THR B 1 450 ? 6.32700   -31.47700 -31.62200 1.000 39.94000  ? 469  THR B CA  1 
ATOM   7450  C C   . THR B 1 450 ? 6.91500   -31.02800 -32.95500 1.000 44.59000  ? 469  THR B C   1 
ATOM   7451  O O   . THR B 1 450 ? 6.83400   -31.75900 -33.94900 1.000 42.76000  ? 469  THR B O   1 
ATOM   7452  C CB  . THR B 1 450 ? 7.14500   -32.61700 -31.01300 1.000 49.13000  ? 469  THR B CB  1 
ATOM   7453  O OG1 . THR B 1 450 ? 6.51400   -33.07600 -29.80600 1.000 45.11000  ? 469  THR B OG1 1 
ATOM   7454  C CG2 . THR B 1 450 ? 8.56700   -32.14000 -30.68300 1.000 42.57000  ? 469  THR B CG2 1 
ATOM   7455  N N   . LEU B 1 451 ? 7.48700   -29.82000 -32.97500 1.000 38.42000  ? 470  LEU B N   1 
ATOM   7456  C CA  . LEU B 1 451 ? 7.93400   -29.15900 -34.20000 1.000 37.66000  ? 470  LEU B CA  1 
ATOM   7457  C C   . LEU B 1 451 ? 9.44000   -28.93400 -34.11900 1.000 46.00000  ? 470  LEU B C   1 
ATOM   7458  O O   . LEU B 1 451 ? 9.91300   -28.16000 -33.27800 1.000 47.35000  ? 470  LEU B O   1 
ATOM   7459  C CB  . LEU B 1 451 ? 7.21400   -27.82500 -34.38800 1.000 37.23000  ? 470  LEU B CB  1 
ATOM   7460  C CG  . LEU B 1 451 ? 7.35300   -27.13200 -35.74600 1.000 44.78000  ? 470  LEU B CG  1 
ATOM   7461  C CD1 . LEU B 1 451 ? 6.43200   -27.77700 -36.78900 1.000 37.36000  ? 470  LEU B CD1 1 
ATOM   7462  C CD2 . LEU B 1 451 ? 7.13800   -25.62500 -35.65200 1.000 44.33000  ? 470  LEU B CD2 1 
ATOM   7463  N N   . HIS B 1 452 ? 10.19100  -29.58900 -34.99600 1.000 43.97000  ? 471  HIS B N   1 
ATOM   7464  C CA  . HIS B 1 452 ? 11.63900  -29.42500 -35.07400 1.000 37.11000  ? 471  HIS B CA  1 
ATOM   7465  C C   . HIS B 1 452 ? 11.94100  -28.53600 -36.27400 1.000 39.69000  ? 471  HIS B C   1 
ATOM   7466  O O   . HIS B 1 452 ? 11.73200  -28.94800 -37.42000 1.000 43.58000  ? 471  HIS B O   1 
ATOM   7467  C CB  . HIS B 1 452 ? 12.31200  -30.78300 -35.22600 1.000 39.43000  ? 471  HIS B CB  1 
ATOM   7468  C CG  . HIS B 1 452 ? 11.93800  -31.76300 -34.15900 1.000 39.73000  ? 471  HIS B CG  1 
ATOM   7469  N ND1 . HIS B 1 452 ? 12.45900  -31.71900 -32.88600 1.000 43.48000  ? 471  HIS B ND1 1 
ATOM   7470  C CD2 . HIS B 1 452 ? 11.09000  -32.81800 -34.17900 1.000 40.76000  ? 471  HIS B CD2 1 
ATOM   7471  C CE1 . HIS B 1 452 ? 11.95100  -32.70500 -32.16800 1.000 41.81000  ? 471  HIS B CE1 1 
ATOM   7472  N NE2 . HIS B 1 452 ? 11.11800  -33.38800 -32.93000 1.000 42.59000  ? 471  HIS B NE2 1 
ATOM   7473  N N   . THR B 1 453 ? 12.43100  -27.32600 -36.02600 1.000 37.27000  ? 472  THR B N   1 
ATOM   7474  C CA  . THR B 1 453 ? 12.68500  -26.37400 -37.10500 1.000 39.57000  ? 472  THR B CA  1 
ATOM   7475  C C   . THR B 1 453 ? 14.16200  -26.39900 -37.48800 1.000 43.19000  ? 472  THR B C   1 
ATOM   7476  O O   . THR B 1 453 ? 15.03600  -26.40700 -36.61500 1.000 44.06000  ? 472  THR B O   1 
ATOM   7477  C CB  . THR B 1 453 ? 12.25700  -24.96100 -36.70800 1.000 40.02000  ? 472  THR B CB  1 
ATOM   7478  O OG1 . THR B 1 453 ? 10.86300  -24.96900 -36.38900 1.000 45.32000  ? 472  THR B OG1 1 
ATOM   7479  C CG2 . THR B 1 453 ? 12.48900  -23.98200 -37.85200 1.000 42.57000  ? 472  THR B CG2 1 
ATOM   7480  N N   . LEU B 1 454 ? 14.43100  -26.41800 -38.79400 1.000 41.60000  ? 473  LEU B N   1 
ATOM   7481  C CA  . LEU B 1 454 ? 15.78700  -26.50700 -39.32000 1.000 42.49000  ? 473  LEU B CA  1 
ATOM   7482  C C   . LEU B 1 454 ? 16.41800  -25.12800 -39.48200 1.000 47.25000  ? 473  LEU B C   1 
ATOM   7483  O O   . LEU B 1 454 ? 15.78000  -24.18400 -39.95900 1.000 46.94000  ? 473  LEU B O   1 
ATOM   7484  C CB  . LEU B 1 454 ? 15.79300  -27.24400 -40.66100 1.000 42.36000  ? 473  LEU B CB  1 
ATOM   7485  C CG  . LEU B 1 454 ? 17.13100  -27.41600 -41.39000 1.000 39.91000  ? 473  LEU B CG  1 
ATOM   7486  C CD1 . LEU B 1 454 ? 18.15000  -28.18000 -40.55900 1.000 37.91000  ? 473  LEU B CD1 1 
ATOM   7487  C CD2 . LEU B 1 454 ? 16.88800  -28.14000 -42.69700 1.000 45.17000  ? 473  LEU B CD2 1 
ATOM   7488  N N   . HIS B 1 455 ? 17.68100  -25.02800 -39.07800 1.000 45.73000  ? 474  HIS B N   1 
ATOM   7489  C CA  . HIS B 1 455 ? 18.48700  -23.81900 -39.16700 1.000 46.13000  ? 474  HIS B CA  1 
ATOM   7490  C C   . HIS B 1 455 ? 19.67000  -24.08700 -40.08100 1.000 45.22000  ? 474  HIS B C   1 
ATOM   7491  O O   . HIS B 1 455 ? 20.22200  -25.19100 -40.08000 1.000 42.62000  ? 474  HIS B O   1 
ATOM   7492  C CB  . HIS B 1 455 ? 18.98700  -23.42300 -37.79100 1.000 44.07000  ? 474  HIS B CB  1 
ATOM   7493  C CG  . HIS B 1 455 ? 17.90300  -23.01800 -36.84300 1.000 47.96000  ? 474  HIS B CG  1 
ATOM   7494  N ND1 . HIS B 1 455 ? 17.56500  -21.70200 -36.61200 1.000 50.08000  ? 474  HIS B ND1 1 
ATOM   7495  C CD2 . HIS B 1 455 ? 17.03100  -23.76300 -36.12300 1.000 47.80000  ? 474  HIS B CD2 1 
ATOM   7496  C CE1 . HIS B 1 455 ? 16.57800  -21.65300 -35.73500 1.000 52.34000  ? 474  HIS B CE1 1 
ATOM   7497  N NE2 . HIS B 1 455 ? 16.22200  -22.89000 -35.43600 1.000 50.72000  ? 474  HIS B NE2 1 
ATOM   7498  N N   . VAL B 1 456 ? 20.04900  -23.08800 -40.87300 1.000 49.88000  ? 475  VAL B N   1 
ATOM   7499  C CA  . VAL B 1 456 ? 21.15500  -23.21800 -41.81600 1.000 47.15000  ? 475  VAL B CA  1 
ATOM   7500  C C   . VAL B 1 456 ? 22.06400  -22.00600 -41.67400 1.000 45.40000  ? 475  VAL B C   1 
ATOM   7501  O O   . VAL B 1 456 ? 21.60100  -20.86100 -41.74500 1.000 50.22000  ? 475  VAL B O   1 
ATOM   7502  C CB  . VAL B 1 456 ? 20.66300  -23.36700 -43.26300 1.000 49.70000  ? 475  VAL B CB  1 
ATOM   7503  C CG1 . VAL B 1 456 ? 21.82100  -23.21500 -44.24300 1.000 46.90000  ? 475  VAL B CG1 1 
ATOM   7504  C CG2 . VAL B 1 456 ? 20.00100  -24.72700 -43.43300 1.000 45.15000  ? 475  VAL B CG2 1 
ATOM   7505  N N   . LEU B 1 457 ? 23.34900  -22.25500 -41.46600 1.000 43.65000  ? 476  LEU B N   1 
ATOM   7506  C CA  . LEU B 1 457 ? 24.34700  -21.19900 -41.38400 1.000 47.78000  ? 476  LEU B CA  1 
ATOM   7507  C C   . LEU B 1 457 ? 25.46500  -21.49300 -42.37400 1.000 50.45000  ? 476  LEU B C   1 
ATOM   7508  O O   . LEU B 1 457 ? 26.05800  -22.57700 -42.34500 1.000 48.60000  ? 476  LEU B O   1 
ATOM   7509  C CB  . LEU B 1 457 ? 24.89700  -21.08300 -39.95900 1.000 42.72000  ? 476  LEU B CB  1 
ATOM   7510  C CG  . LEU B 1 457 ? 23.91600  -20.54400 -38.91700 1.000 48.82000  ? 476  LEU B CG  1 
ATOM   7511  C CD1 . LEU B 1 457 ? 24.44400  -20.75800 -37.51100 1.000 45.91000  ? 476  LEU B CD1 1 
ATOM   7512  C CD2 . LEU B 1 457 ? 23.67600  -19.06900 -39.17000 1.000 51.16000  ? 476  LEU B CD2 1 
ATOM   7513  N N   . SER B 1 458 ? 25.74500  -20.53500 -43.25200 1.000 47.95000  ? 477  SER B N   1 
ATOM   7514  C CA  . SER B 1 458 ? 26.94000  -20.63900 -44.07500 1.000 52.39000  ? 477  SER B CA  1 
ATOM   7515  C C   . SER B 1 458 ? 28.16300  -20.58800 -43.17400 1.000 47.28000  ? 477  SER B C   1 
ATOM   7516  O O   . SER B 1 458 ? 28.12300  -19.99600 -42.09100 1.000 49.52000  ? 477  SER B O   1 
ATOM   7517  C CB  . SER B 1 458 ? 26.98900  -19.50600 -45.10200 1.000 58.03000  ? 477  SER B CB  1 
ATOM   7518  O OG  . SER B 1 458 ? 27.16500  -18.24700 -44.46500 1.000 58.35000  ? 477  SER B OG  1 
ATOM   7519  N N   . LYS B 1 459 ? 29.25100  -21.23800 -43.61400 1.000 53.37000  ? 478  LYS B N   1 
ATOM   7520  C CA  . LYS B 1 459 ? 30.49900  -21.20300 -42.85100 1.000 57.31000  ? 478  LYS B CA  1 
ATOM   7521  C C   . LYS B 1 459 ? 30.79800  -19.77200 -42.43700 1.000 61.37000  ? 478  LYS B C   1 
ATOM   7522  O O   . LYS B 1 459 ? 31.26500  -19.50800 -41.33000 1.000 60.29000  ? 478  LYS B O   1 
ATOM   7523  C CB  . LYS B 1 459 ? 31.69500  -21.73700 -43.65700 1.000 52.31000  ? 478  LYS B CB  1 
ATOM   7524  C CG  . LYS B 1 459 ? 31.69000  -23.21400 -44.02400 1.000 57.27000  ? 478  LYS B CG  1 
ATOM   7525  C CD  . LYS B 1 459 ? 33.05200  -23.57600 -44.64700 1.000 61.24000  ? 478  LYS B CD  1 
ATOM   7526  C CE  . LYS B 1 459 ? 33.07100  -24.95300 -45.31200 1.000 64.42000  ? 478  LYS B CE  1 
ATOM   7527  N NZ  . LYS B 1 459 ? 32.88800  -26.09600 -44.37700 1.000 61.06000  ? 478  LYS B NZ  1 
ATOM   7528  N N   . ASP B 1 460 ? 30.50000  -18.84800 -43.33500 1.000 59.66000  ? 479  ASP B N   1 
ATOM   7529  C CA  . ASP B 1 460 ? 30.87300  -17.45900 -43.14700 1.000 58.70000  ? 479  ASP B CA  1 
ATOM   7530  C C   . ASP B 1 460 ? 29.94600  -16.78400 -42.13600 1.000 59.13000  ? 479  ASP B C   1 
ATOM   7531  O O   . ASP B 1 460 ? 30.37300  -15.92300 -41.35500 1.000 58.45000  ? 479  ASP B O   1 
ATOM   7532  C CB  . ASP B 1 460 ? 30.87600  -16.82300 -44.53600 1.000 60.38000  ? 479  ASP B CB  1 
ATOM   7533  C CG  . ASP B 1 460 ? 31.80000  -15.64600 -44.63700 1.000 75.60000  ? 479  ASP B CG  1 
ATOM   7534  O OD1 . ASP B 1 460 ? 31.86100  -14.84500 -43.67000 1.000 79.27000  ? 479  ASP B OD1 1 
ATOM   7535  O OD2 . ASP B 1 460 ? 32.60900  -15.66300 -45.60000 1.000 89.47000  ? 479  ASP B OD2 1 
ATOM   7536  N N   . GLU B 1 461 ? 28.67000  -17.17400 -42.14000 1.000 56.93000  ? 480  GLU B N   1 
ATOM   7537  C CA  . GLU B 1 461 ? 27.73800  -16.81200 -41.07200 1.000 50.47000  ? 480  GLU B CA  1 
ATOM   7538  C C   . GLU B 1 461 ? 28.12900  -17.41900 -39.72800 1.000 51.76000  ? 480  GLU B C   1 
ATOM   7539  O O   . GLU B 1 461 ? 28.08400  -16.74400 -38.69000 1.000 44.07000  ? 480  GLU B O   1 
ATOM   7540  C CB  . GLU B 1 461 ? 26.34000  -17.29100 -41.43900 1.000 55.03000  ? 480  GLU B CB  1 
ATOM   7541  C CG  . GLU B 1 461 ? 25.50900  -16.33500 -42.23100 1.000 60.04000  ? 480  GLU B CG  1 
ATOM   7542  C CD  . GLU B 1 461 ? 24.24300  -17.00500 -42.73700 1.000 68.23000  ? 480  GLU B CD  1 
ATOM   7543  O OE1 . GLU B 1 461 ? 24.32900  -18.20300 -43.09100 1.000 65.52000  ? 480  GLU B OE1 1 
ATOM   7544  O OE2 . GLU B 1 461 ? 23.15300  -16.38100 -42.63300 1.000 74.93000  ? 480  GLU B OE2 1 
ATOM   7545  N N   . LEU B 1 462 ? 28.46900  -18.70900 -39.73000 1.000 53.54000  ? 481  LEU B N   1 
ATOM   7546  C CA  . LEU B 1 462 ? 28.87100  -19.40700 -38.51300 1.000 48.86000  ? 481  LEU B CA  1 
ATOM   7547  C C   . LEU B 1 462 ? 30.09600  -18.76600 -37.87100 1.000 51.83000  ? 481  LEU B C   1 
ATOM   7548  O O   . LEU B 1 462 ? 30.21700  -18.72300 -36.64100 1.000 63.26000  ? 481  LEU B O   1 
ATOM   7549  C CB  . LEU B 1 462 ? 29.15000  -20.86600 -38.85800 1.000 47.96000  ? 481  LEU B CB  1 
ATOM   7550  C CG  . LEU B 1 462 ? 29.59600  -21.86200 -37.79700 1.000 45.09000  ? 481  LEU B CG  1 
ATOM   7551  C CD1 . LEU B 1 462 ? 28.50700  -22.06900 -36.76800 1.000 46.45000  ? 481  LEU B CD1 1 
ATOM   7552  C CD2 . LEU B 1 462 ? 29.96200  -23.16900 -38.48200 1.000 47.72000  ? 481  LEU B CD2 1 
ATOM   7553  N N   . LEU B 1 463 ? 31.02500  -18.27500 -38.68800 1.000 51.61000  ? 482  LEU B N   1 
ATOM   7554  C CA  . LEU B 1 463 ? 32.24400  -17.69600 -38.14700 1.000 58.81000  ? 482  LEU B CA  1 
ATOM   7555  C C   . LEU B 1 463 ? 32.01700  -16.32900 -37.51700 1.000 58.21000  ? 482  LEU B C   1 
ATOM   7556  O O   . LEU B 1 463 ? 32.78200  -15.94700 -36.62900 1.000 63.89000  ? 482  LEU B O   1 
ATOM   7557  C CB  . LEU B 1 463 ? 33.31300  -17.61000 -39.24500 1.000 63.48000  ? 482  LEU B CB  1 
ATOM   7558  C CG  . LEU B 1 463 ? 33.77400  -18.99300 -39.70700 1.000 67.05000  ? 482  LEU B CG  1 
ATOM   7559  C CD1 . LEU B 1 463 ? 34.79900  -18.92500 -40.83800 1.000 62.71000  ? 482  LEU B CD1 1 
ATOM   7560  C CD2 . LEU B 1 463 ? 34.29900  -19.77000 -38.51600 1.000 61.16000  ? 482  LEU B CD2 1 
ATOM   7561  N N   . LYS B 1 464 ? 30.99600  -15.58100 -37.94400 1.000 61.36000  ? 483  LYS B N   1 
ATOM   7562  C CA  . LYS B 1 464 ? 30.70200  -14.32000 -37.26900 1.000 63.06000  ? 483  LYS B CA  1 
ATOM   7563  C C   . LYS B 1 464 ? 29.96400  -14.48600 -35.94900 1.000 62.69000  ? 483  LYS B C   1 
ATOM   7564  O O   . LYS B 1 464 ? 29.86300  -13.50600 -35.20200 1.000 68.92000  ? 483  LYS B O   1 
ATOM   7565  C CB  . LYS B 1 464 ? 29.86300  -13.36500 -38.12300 1.000 63.72000  ? 483  LYS B CB  1 
ATOM   7566  C CG  . LYS B 1 464 ? 30.56800  -12.55600 -39.20000 1.000 76.15000  ? 483  LYS B CG  1 
ATOM   7567  C CD  . LYS B 1 464 ? 29.53900  -11.55700 -39.76800 1.000 79.42000  ? 483  LYS B CD  1 
ATOM   7568  C CE  . LYS B 1 464 ? 29.34800  -10.27200 -38.90600 1.000 81.50000  ? 483  LYS B CE  1 
ATOM   7569  N NZ  . LYS B 1 464 ? 30.40300  -9.21500  -39.17000 1.000 85.28000  ? 483  LYS B NZ  1 
ATOM   7570  N N   . LEU B 1 465 ? 29.40200  -15.65400 -35.64600 1.000 57.98000  ? 484  LEU B N   1 
ATOM   7571  C CA  . LEU B 1 465 ? 28.64600  -15.77200 -34.40200 1.000 55.92000  ? 484  LEU B CA  1 
ATOM   7572  C C   . LEU B 1 465 ? 29.58900  -15.82700 -33.20100 1.000 65.14000  ? 484  LEU B C   1 
ATOM   7573  O O   . LEU B 1 465 ? 30.73900  -16.26300 -33.30700 1.000 62.52000  ? 484  LEU B O   1 
ATOM   7574  C CB  . LEU B 1 465 ? 27.74300  -17.01200 -34.40600 1.000 54.83000  ? 484  LEU B CB  1 
ATOM   7575  C CG  . LEU B 1 465 ? 26.60500  -17.14700 -35.42500 1.000 48.59000  ? 484  LEU B CG  1 
ATOM   7576  C CD1 . LEU B 1 465 ? 25.84400  -18.44300 -35.21300 1.000 48.09000  ? 484  LEU B CD1 1 
ATOM   7577  C CD2 . LEU B 1 465 ? 25.65400  -15.97900 -35.41800 1.000 49.22000  ? 484  LEU B CD2 1 
ATOM   7578  N N   . ASP B 1 466 ? 29.08200  -15.37900 -32.05200 1.000 68.39000  ? 485  ASP B N   1 
ATOM   7579  C CA  . ASP B 1 466 ? 29.79400  -15.38800 -30.76700 1.000 68.54000  ? 485  ASP B CA  1 
ATOM   7580  C C   . ASP B 1 466 ? 29.35400  -16.56300 -29.90400 1.000 65.83000  ? 485  ASP B C   1 
ATOM   7581  O O   . ASP B 1 466 ? 28.37300  -16.50300 -29.16500 1.000 74.53000  ? 485  ASP B O   1 
ATOM   7582  C CB  . ASP B 1 466 ? 29.61400  -14.04300 -30.06700 1.000 71.58000  ? 485  ASP B CB  1 
ATOM   7583  C CG  . ASP B 1 466 ? 30.88800  -13.20800 -30.09500 1.000 82.87000  ? 485  ASP B CG  1 
ATOM   7584  O OD1 . ASP B 1 466 ? 31.89200  -13.70800 -29.54100 1.000 78.90000  ? 485  ASP B OD1 1 
ATOM   7585  O OD2 . ASP B 1 466 ? 30.91600  -12.14400 -30.75600 1.000 86.68000  ? 485  ASP B OD2 1 
ATOM   7586  N N   . TYR B 1 467 ? 30.12400  -17.64200 -29.99600 1.000 64.36000  ? 486  TYR B N   1 
ATOM   7587  C CA  . TYR B 1 467 ? 29.95700  -18.88700 -29.26800 1.000 63.04000  ? 486  TYR B CA  1 
ATOM   7588  C C   . TYR B 1 467 ? 31.24500  -19.18300 -28.50300 1.000 63.28000  ? 486  TYR B C   1 
ATOM   7589  O O   . TYR B 1 467 ? 32.25400  -18.49500 -28.66800 1.000 57.84000  ? 486  TYR B O   1 
ATOM   7590  C CB  . TYR B 1 467 ? 29.62000  -20.01400 -30.25200 1.000 59.26000  ? 486  TYR B CB  1 
ATOM   7591  C CG  . TYR B 1 467 ? 30.62800  -20.10000 -31.37100 1.000 57.83000  ? 486  TYR B CG  1 
ATOM   7592  C CD1 . TYR B 1 467 ? 30.49200  -19.31100 -32.51000 1.000 57.76000  ? 486  TYR B CD1 1 
ATOM   7593  C CD2 . TYR B 1 467 ? 31.72700  -20.94300 -31.28500 1.000 60.53000  ? 486  TYR B CD2 1 
ATOM   7594  C CE1 . TYR B 1 467 ? 31.41900  -19.36100 -33.54100 1.000 55.63000  ? 486  TYR B CE1 1 
ATOM   7595  C CE2 . TYR B 1 467 ? 32.66400  -21.00400 -32.32000 1.000 53.49000  ? 486  TYR B CE2 1 
ATOM   7596  C CZ  . TYR B 1 467 ? 32.50500  -20.21100 -33.44100 1.000 57.57000  ? 486  TYR B CZ  1 
ATOM   7597  O OH  . TYR B 1 467 ? 33.42900  -20.26700 -34.46600 1.000 67.14000  ? 486  TYR B OH  1 
ATOM   7598  N N   . ASP B 1 468 ? 31.22100  -20.20100 -27.63900 1.000 59.00000  ? 487  ASP B N   1 
ATOM   7599  C CA  . ASP B 1 468 ? 32.45400  -20.62700 -26.99300 1.000 51.79000  ? 487  ASP B CA  1 
ATOM   7600  C C   . ASP B 1 468 ? 32.49400  -22.15000 -26.95100 1.000 54.50000  ? 487  ASP B C   1 
ATOM   7601  O O   . ASP B 1 468 ? 31.53300  -22.83500 -27.31500 1.000 58.29000  ? 487  ASP B O   1 
ATOM   7602  C CB  . ASP B 1 468 ? 32.64800  -19.99800 -25.59200 1.000 52.92000  ? 487  ASP B CB  1 
ATOM   7603  C CG  . ASP B 1 468 ? 31.93400  -20.74100 -24.45200 1.000 52.21000  ? 487  ASP B CG  1 
ATOM   7604  O OD1 . ASP B 1 468 ? 31.26600  -21.77500 -24.65700 1.000 56.32000  ? 487  ASP B OD1 1 
ATOM   7605  O OD2 . ASP B 1 468 ? 32.07100  -20.27800 -23.29700 1.000 50.56000  ? 487  ASP B OD2 1 
ATOM   7606  N N   . ALA B 1 469 ? 33.62900  -22.67500 -26.48300 1.000 45.76000  ? 488  ALA B N   1 
ATOM   7607  C CA  . ALA B 1 469 ? 33.85300  -24.11500 -26.42600 1.000 49.27000  ? 488  ALA B CA  1 
ATOM   7608  C C   . ALA B 1 469 ? 32.98900  -24.80700 -25.38100 1.000 48.27000  ? 488  ALA B C   1 
ATOM   7609  O O   . ALA B 1 469 ? 32.77400  -26.02000 -25.47800 1.000 49.79000  ? 488  ALA B O   1 
ATOM   7610  C CB  . ALA B 1 469 ? 35.32600  -24.39900 -26.12600 1.000 39.83000  ? 488  ALA B CB  1 
ATOM   7611  N N   . TYR B 1 470 ? 32.49800  -24.06800 -24.38600 1.000 49.88000  ? 489  TYR B N   1 
ATOM   7612  C CA  . TYR B 1 470 ? 31.93800  -24.65300 -23.17600 1.000 48.38000  ? 489  TYR B CA  1 
ATOM   7613  C C   . TYR B 1 470 ? 30.41500  -24.68400 -23.18300 1.000 53.47000  ? 489  TYR B C   1 
ATOM   7614  O O   . TYR B 1 470 ? 29.82400  -25.51600 -22.48700 1.000 51.04000  ? 489  TYR B O   1 
ATOM   7615  C CB  . TYR B 1 470 ? 32.45700  -23.86800 -21.96400 1.000 46.58000  ? 489  TYR B CB  1 
ATOM   7616  C CG  . TYR B 1 470 ? 33.97100  -23.77500 -21.98200 1.000 48.05000  ? 489  TYR B CG  1 
ATOM   7617  C CD1 . TYR B 1 470 ? 34.77000  -24.79500 -21.47600 1.000 48.75000  ? 489  TYR B CD1 1 
ATOM   7618  C CD2 . TYR B 1 470 ? 34.60300  -22.68000 -22.56700 1.000 44.22000  ? 489  TYR B CD2 1 
ATOM   7619  C CE1 . TYR B 1 470 ? 36.16000  -24.70700 -21.52400 1.000 47.58000  ? 489  TYR B CE1 1 
ATOM   7620  C CE2 . TYR B 1 470 ? 35.97700  -22.58000 -22.62200 1.000 41.19000  ? 489  TYR B CE2 1 
ATOM   7621  C CZ  . TYR B 1 470 ? 36.75500  -23.59300 -22.10300 1.000 44.74000  ? 489  TYR B CZ  1 
ATOM   7622  O OH  . TYR B 1 470 ? 38.12600  -23.48700 -22.16800 1.000 40.69000  ? 489  TYR B OH  1 
ATOM   7623  N N   . TYR B 1 471 ? 29.77400  -23.82200 -23.97200 1.000 50.84000  ? 490  TYR B N   1 
ATOM   7624  C CA  . TYR B 1 471 ? 28.32300  -23.75700 -24.09400 1.000 50.04000  ? 490  TYR B CA  1 
ATOM   7625  C C   . TYR B 1 471 ? 27.95100  -23.66400 -25.55900 1.000 54.97000  ? 490  TYR B C   1 
ATOM   7626  O O   . TYR B 1 471 ? 28.41500  -22.76000 -26.26200 1.000 55.61000  ? 490  TYR B O   1 
ATOM   7627  C CB  . TYR B 1 471 ? 27.76700  -22.56200 -23.33100 1.000 43.82000  ? 490  TYR B CB  1 
ATOM   7628  C CG  . TYR B 1 471 ? 28.07600  -22.69500 -21.87500 1.000 53.08000  ? 490  TYR B CG  1 
ATOM   7629  C CD1 . TYR B 1 471 ? 27.32300  -23.54200 -21.06600 1.000 59.81000  ? 490  TYR B CD1 1 
ATOM   7630  C CD2 . TYR B 1 471 ? 29.15000  -22.02700 -21.31300 1.000 45.37000  ? 490  TYR B CD2 1 
ATOM   7631  C CE1 . TYR B 1 471 ? 27.61600  -23.70200 -19.72700 1.000 53.90000  ? 490  TYR B CE1 1 
ATOM   7632  C CE2 . TYR B 1 471 ? 29.44900  -22.17400 -19.97200 1.000 49.87000  ? 490  TYR B CE2 1 
ATOM   7633  C CZ  . TYR B 1 471 ? 28.68200  -23.01300 -19.18400 1.000 53.13000  ? 490  TYR B CZ  1 
ATOM   7634  O OH  . TYR B 1 471 ? 28.97300  -23.16600 -17.84700 1.000 59.45000  ? 490  TYR B OH  1 
ATOM   7635  N N   . ALA B 1 472 ? 27.12000  -24.59700 -26.01600 1.000 60.48000  ? 491  ALA B N   1 
ATOM   7636  C CA  . ALA B 1 472 ? 26.67000  -24.56100 -27.40000 1.000 58.96000  ? 491  ALA B CA  1 
ATOM   7637  C C   . ALA B 1 472 ? 25.74100  -23.37200 -27.60500 1.000 52.79000  ? 491  ALA B C   1 
ATOM   7638  O O   . ALA B 1 472 ? 24.75600  -23.20900 -26.87800 1.000 55.32000  ? 491  ALA B O   1 
ATOM   7639  C CB  . ALA B 1 472 ? 25.97100  -25.85900 -27.77200 1.000 50.45000  ? 491  ALA B CB  1 
ATOM   7640  N N   . PHE B 1 473 ? 26.07100  -22.52300 -28.57200 1.000 53.48000  ? 492  PHE B N   1 
ATOM   7641  C CA  . PHE B 1 473 ? 25.26100  -21.31000 -28.83900 1.000 57.75000  ? 492  PHE B CA  1 
ATOM   7642  C C   . PHE B 1 473 ? 23.82000  -21.69500 -29.20100 1.000 53.12000  ? 492  PHE B C   1 
ATOM   7643  O O   . PHE B 1 473 ? 22.91800  -20.95900 -28.86300 1.000 58.82000  ? 492  PHE B O   1 
ATOM   7644  C CB  . PHE B 1 473 ? 25.92400  -20.45700 -29.92600 1.000 54.32000  ? 492  PHE B CB  1 
ATOM   7645  C CG  . PHE B 1 473 ? 25.53000  -20.84800 -31.32500 1.000 60.65000  ? 492  PHE B CG  1 
ATOM   7646  C CD1 . PHE B 1 473 ? 26.13700  -21.91900 -31.95000 1.000 61.49000  ? 492  PHE B CD1 1 
ATOM   7647  C CD2 . PHE B 1 473 ? 24.43800  -20.26700 -31.94000 1.000 53.37000  ? 492  PHE B CD2 1 
ATOM   7648  C CE1 . PHE B 1 473 ? 25.73300  -22.32800 -33.20700 1.000 54.68000  ? 492  PHE B CE1 1 
ATOM   7649  C CE2 . PHE B 1 473 ? 24.03200  -20.67800 -33.19500 1.000 49.30000  ? 492  PHE B CE2 1 
ATOM   7650  C CZ  . PHE B 1 473 ? 24.67900  -21.71000 -33.82400 1.000 54.78000  ? 492  PHE B CZ  1 
ATOM   7651  N N   . TYR B 1 474 ? 23.62100  -22.89200 -29.76900 1.000 51.24000  ? 493  TYR B N   1 
ATOM   7652  C CA  . TYR B 1 474 ? 22.28600  -23.31700 -30.25200 1.000 53.15000  ? 493  TYR B CA  1 
ATOM   7653  C C   . TYR B 1 474 ? 21.32600  -23.48600 -29.08000 1.000 51.62000  ? 493  TYR B C   1 
ATOM   7654  O O   . TYR B 1 474 ? 20.14800  -23.26300 -29.23800 1.000 53.47000  ? 493  TYR B O   1 
ATOM   7655  C CB  . TYR B 1 474 ? 22.37500  -24.49800 -31.22200 1.000 51.74000  ? 493  TYR B CB  1 
ATOM   7656  C CG  . TYR B 1 474 ? 22.95600  -25.77300 -30.67700 1.000 57.92000  ? 493  TYR B CG  1 
ATOM   7657  C CD1 . TYR B 1 474 ? 22.31100  -26.49600 -29.69900 1.000 61.82000  ? 493  TYR B CD1 1 
ATOM   7658  C CD2 . TYR B 1 474 ? 24.12700  -26.29600 -31.18600 1.000 57.37000  ? 493  TYR B CD2 1 
ATOM   7659  C CE1 . TYR B 1 474 ? 22.83700  -27.66700 -29.19200 1.000 71.53000  ? 493  TYR B CE1 1 
ATOM   7660  C CE2 . TYR B 1 474 ? 24.66300  -27.47300 -30.70400 1.000 60.37000  ? 493  TYR B CE2 1 
ATOM   7661  C CZ  . TYR B 1 474 ? 24.01700  -28.16200 -29.70100 1.000 72.93000  ? 493  TYR B CZ  1 
ATOM   7662  O OH  . TYR B 1 474 ? 24.54200  -29.31200 -29.20100 1.000 79.09000  ? 493  TYR B OH  1 
ATOM   7663  N N   . GLY B 1 475 ? 21.84900  -23.84000 -27.92400 1.000 51.06000  ? 494  GLY B N   1 
ATOM   7664  C CA  . GLY B 1 475 ? 20.98200  -23.98700 -26.76800 1.000 46.86000  ? 494  GLY B CA  1 
ATOM   7665  C C   . GLY B 1 475 ? 20.30300  -22.68900 -26.37300 1.000 51.86000  ? 494  GLY B C   1 
ATOM   7666  O O   . GLY B 1 475 ? 19.08700  -22.64900 -26.17100 1.000 55.49000  ? 494  GLY B O   1 
ATOM   7667  N N   . ILE B 1 476 ? 21.08000  -21.61000 -26.24700 1.000 52.52000  ? 495  ILE B N   1 
ATOM   7668  C CA  . ILE B 1 476 ? 20.49700  -20.32000 -25.88500 1.000 45.02000  ? 495  ILE B CA  1 
ATOM   7669  C C   . ILE B 1 476 ? 19.62400  -19.79000 -27.01800 1.000 45.74000  ? 495  ILE B C   1 
ATOM   7670  O O   . ILE B 1 476 ? 18.59300  -19.15200 -26.77600 1.000 43.24000  ? 495  ILE B O   1 
ATOM   7671  C CB  . ILE B 1 476 ? 21.59700  -19.31700 -25.47800 1.000 51.49000  ? 495  ILE B CB  1 
ATOM   7672  C CG1 . ILE B 1 476 ? 20.97800  -18.03300 -24.90600 1.000 51.76000  ? 495  ILE B CG1 1 
ATOM   7673  C CG2 . ILE B 1 476 ? 22.52700  -18.98500 -26.63100 1.000 46.94000  ? 495  ILE B CG2 1 
ATOM   7674  C CD1 . ILE B 1 476 ? 20.24800  -18.23800 -23.58500 1.000 45.79000  ? 495  ILE B CD1 1 
ATOM   7675  N N   . VAL B 1 477 ? 20.00900  -20.05000 -28.27100 1.000 47.01000  ? 496  VAL B N   1 
ATOM   7676  C CA  . VAL B 1 477 ? 19.14000  -19.68600 -29.38500 1.000 48.86000  ? 496  VAL B CA  1 
ATOM   7677  C C   . VAL B 1 477 ? 17.77100  -20.32900 -29.20600 1.000 43.48000  ? 496  VAL B C   1 
ATOM   7678  O O   . VAL B 1 477 ? 16.73300  -19.67300 -29.35700 1.000 42.13000  ? 496  VAL B O   1 
ATOM   7679  C CB  . VAL B 1 477 ? 19.78600  -20.07300 -30.73100 1.000 47.85000  ? 496  VAL B CB  1 
ATOM   7680  C CG1 . VAL B 1 477 ? 18.76900  -19.99800 -31.85500 1.000 38.35000  ? 496  VAL B CG1 1 
ATOM   7681  C CG2 . VAL B 1 477 ? 20.94200  -19.14400 -31.04700 1.000 37.00000  ? 496  VAL B CG2 1 
ATOM   7682  N N   . GLU B 1 478 ? 17.74800  -21.61600 -28.84900 1.000 42.95000  ? 497  GLU B N   1 
ATOM   7683  C CA  . GLU B 1 478 ? 16.46600  -22.28200 -28.66100 1.000 47.01000  ? 497  GLU B CA  1 
ATOM   7684  C C   . GLU B 1 478 ? 15.67500  -21.62800 -27.54100 1.000 43.85000  ? 497  GLU B C   1 
ATOM   7685  O O   . GLU B 1 478 ? 14.46000  -21.43900 -27.66000 1.000 47.14000  ? 497  GLU B O   1 
ATOM   7686  C CB  . GLU B 1 478 ? 16.65400  -23.75900 -28.34600 1.000 48.54000  ? 497  GLU B CB  1 
ATOM   7687  C CG  . GLU B 1 478 ? 15.43300  -24.57900 -28.72900 1.000 45.62000  ? 497  GLU B CG  1 
ATOM   7688  C CD  . GLU B 1 478 ? 15.52700  -26.02300 -28.29400 1.000 50.53000  ? 497  GLU B CD  1 
ATOM   7689  O OE1 . GLU B 1 478 ? 16.18700  -26.30100 -27.27100 1.000 54.10000  ? 497  GLU B OE1 1 
ATOM   7690  O OE2 . GLU B 1 478 ? 15.04700  -26.89400 -29.05500 1.000 49.75000  ? 497  GLU B OE2 1 
ATOM   7691  N N   . GLU B 1 479 ? 16.33500  -21.28300 -26.43400 1.000 44.38000  ? 498  GLU B N   1 
ATOM   7692  C CA  . GLU B 1 479 ? 15.57100  -20.69300 -25.33900 1.000 50.31000  ? 498  GLU B CA  1 
ATOM   7693  C C   . GLU B 1 479 ? 15.04800  -19.30700 -25.68000 1.000 45.00000  ? 498  GLU B C   1 
ATOM   7694  O O   . GLU B 1 479 ? 13.99400  -18.90900 -25.17200 1.000 49.89000  ? 498  GLU B O   1 
ATOM   7695  C CB  . GLU B 1 479 ? 16.38800  -20.65400 -24.04700 1.000 50.62000  ? 498  GLU B CB  1 
ATOM   7696  C CG  . GLU B 1 479 ? 16.45000  -22.02000 -23.39900 1.000 58.86000  ? 498  GLU B CG  1 
ATOM   7697  C CD  . GLU B 1 479 ? 16.79400  -21.96000 -21.92900 1.000 74.04000  ? 498  GLU B CD  1 
ATOM   7698  O OE1 . GLU B 1 479 ? 17.15300  -20.86900 -21.43000 1.000 71.04000  ? 498  GLU B OE1 1 
ATOM   7699  O OE2 . GLU B 1 479 ? 16.64800  -23.00700 -21.26100 1.000 83.09000  ? 498  GLU B OE2 1 
ATOM   7700  N N   . MET B 1 480 ? 15.76600  -18.55900 -26.51700 1.000 43.68000  ? 499  MET B N   1 
ATOM   7701  C CA  . MET B 1 480 ? 15.26700  -17.27000 -26.97500 1.000 42.82000  ? 499  MET B CA  1 
ATOM   7702  C C   . MET B 1 480 ? 14.01000  -17.45600 -27.80900 1.000 41.83000  ? 499  MET B C   1 
ATOM   7703  O O   . MET B 1 480 ? 13.00300  -16.77000 -27.60000 1.000 42.86000  ? 499  MET B O   1 
ATOM   7704  C CB  . MET B 1 480 ? 16.36400  -16.56800 -27.77300 1.000 46.31000  ? 499  MET B CB  1 
ATOM   7705  C CG  . MET B 1 480 ? 16.18100  -15.08700 -27.97700 1.000 55.58000  ? 499  MET B CG  1 
ATOM   7706  S SD  . MET B 1 480 ? 16.11400  -14.33100 -26.35800 1.000 67.94000  ? 499  MET B SD  1 
ATOM   7707  C CE  . MET B 1 480 ? 17.67700  -14.91000 -25.68600 1.000 48.54000  ? 499  MET B CE  1 
ATOM   7708  N N   . LEU B 1 481 ? 14.03800  -18.42300 -28.72900 1.000 46.04000  ? 500  LEU B N   1 
ATOM   7709  C CA  . LEU B 1 481 ? 12.88900  -18.67200 -29.59100 1.000 42.32000  ? 500  LEU B CA  1 
ATOM   7710  C C   . LEU B 1 481 ? 11.68300  -19.12500 -28.78300 1.000 41.44000  ? 500  LEU B C   1 
ATOM   7711  O O   . LEU B 1 481 ? 10.54900  -18.73400 -29.08100 1.000 48.83000  ? 500  LEU B O   1 
ATOM   7712  C CB  . LEU B 1 481 ? 13.24700  -19.70800 -30.65200 1.000 36.98000  ? 500  LEU B CB  1 
ATOM   7713  C CG  . LEU B 1 481 ? 14.32100  -19.30900 -31.66400 1.000 41.61000  ? 500  LEU B CG  1 
ATOM   7714  C CD1 . LEU B 1 481 ? 14.57500  -20.48400 -32.58700 1.000 43.73000  ? 500  LEU B CD1 1 
ATOM   7715  C CD2 . LEU B 1 481 ? 13.93000  -18.06600 -32.45100 1.000 37.70000  ? 500  LEU B CD2 1 
ATOM   7716  N N   . LYS B 1 482 ? 11.90200  -19.94400 -27.75100 1.000 37.76000  ? 501  LYS B N   1 
ATOM   7717  C CA  . LYS B 1 482 ? 10.79400  -20.31400 -26.87600 1.000 37.67000  ? 501  LYS B CA  1 
ATOM   7718  C C   . LYS B 1 482 ? 10.30100  -19.12700 -26.07100 1.000 38.86000  ? 501  LYS B C   1 
ATOM   7719  O O   . LYS B 1 482 ? 9.09600   -18.98700 -25.83800 1.000 42.26000  ? 501  LYS B O   1 
ATOM   7720  C CB  . LYS B 1 482 ? 11.19400  -21.45600 -25.95400 1.000 40.93000  ? 501  LYS B CB  1 
ATOM   7721  C CG  . LYS B 1 482 ? 11.13400  -22.79900 -26.62700 1.000 45.46000  ? 501  LYS B CG  1 
ATOM   7722  C CD  . LYS B 1 482 ? 11.65200  -23.89200 -25.72600 1.000 51.53000  ? 501  LYS B CD  1 
ATOM   7723  C CE  . LYS B 1 482 ? 11.53000  -25.22900 -26.42700 1.000 58.03000  ? 501  LYS B CE  1 
ATOM   7724  N NZ  . LYS B 1 482 ? 12.28500  -26.31100 -25.73600 1.000 61.80000  ? 501  LYS B NZ  1 
ATOM   7725  N N   . PHE B 1 483 ? 11.20600  -18.25900 -25.63000 1.000 41.18000  ? 502  PHE B N   1 
ATOM   7726  C CA  . PHE B 1 483 ? 10.75500  -17.11600 -24.84700 1.000 41.64000  ? 502  PHE B CA  1 
ATOM   7727  C C   . PHE B 1 483 ? 9.89200   -16.17500 -25.68000 1.000 40.42000  ? 502  PHE B C   1 
ATOM   7728  O O   . PHE B 1 483 ? 8.80900   -15.77100 -25.24700 1.000 38.90000  ? 502  PHE B O   1 
ATOM   7729  C CB  . PHE B 1 483 ? 11.93800  -16.36400 -24.23800 1.000 43.57000  ? 502  PHE B CB  1 
ATOM   7730  C CG  . PHE B 1 483 ? 11.52300  -15.09800 -23.56600 1.000 42.01000  ? 502  PHE B CG  1 
ATOM   7731  C CD1 . PHE B 1 483 ? 10.78600  -15.13300 -22.39700 1.000 40.94000  ? 502  PHE B CD1 1 
ATOM   7732  C CD2 . PHE B 1 483 ? 11.81400  -13.87300 -24.13500 1.000 43.69000  ? 502  PHE B CD2 1 
ATOM   7733  C CE1 . PHE B 1 483 ? 10.36500  -13.96300 -21.79000 1.000 47.97000  ? 502  PHE B CE1 1 
ATOM   7734  C CE2 . PHE B 1 483 ? 11.40100  -12.70200 -23.53600 1.000 48.05000  ? 502  PHE B CE2 1 
ATOM   7735  C CZ  . PHE B 1 483 ? 10.67300  -12.74500 -22.36000 1.000 45.47000  ? 502  PHE B CZ  1 
ATOM   7736  N N   . ILE B 1 484 ? 10.35500  -15.81400 -26.87700 1.000 43.02000  ? 503  ILE B N   1 
ATOM   7737  C CA  . ILE B 1 484 ? 9.62100   -14.83800 -27.67900 1.000 43.30000  ? 503  ILE B CA  1 
ATOM   7738  C C   . ILE B 1 484 ? 8.31000   -15.43100 -28.18400 1.000 41.25000  ? 503  ILE B C   1 
ATOM   7739  O O   . ILE B 1 484 ? 7.28800   -14.73600 -28.25800 1.000 46.93000  ? 503  ILE B O   1 
ATOM   7740  C CB  . ILE B 1 484 ? 10.50300  -14.30400 -28.82500 1.000 44.55000  ? 503  ILE B CB  1 
ATOM   7741  C CG1 . ILE B 1 484 ? 10.88500  -15.42400 -29.79500 1.000 47.68000  ? 503  ILE B CG1 1 
ATOM   7742  C CG2 . ILE B 1 484 ? 11.77300  -13.66500 -28.26400 1.000 40.37000  ? 503  ILE B CG2 1 
ATOM   7743  C CD1 . ILE B 1 484 ? 11.57700  -14.92800 -31.04200 1.000 48.48000  ? 503  ILE B CD1 1 
ATOM   7744  N N   . HIS B 1 485 ? 8.31700   -16.71800 -28.53900 1.000 40.84000  ? 504  HIS B N   1 
ATOM   7745  C CA  . HIS B 1 485 ? 7.07900   -17.41100 -28.88000 1.000 36.91000  ? 504  HIS B CA  1 
ATOM   7746  C C   . HIS B 1 485 ? 6.04200   -17.23200 -27.77900 1.000 43.12000  ? 504  HIS B C   1 
ATOM   7747  O O   . HIS B 1 485 ? 4.88000   -16.90100 -28.04300 1.000 45.82000  ? 504  HIS B O   1 
ATOM   7748  C CB  . HIS B 1 485 ? 7.37400   -18.89500 -29.11400 1.000 35.13000  ? 504  HIS B CB  1 
ATOM   7749  C CG  . HIS B 1 485 ? 6.16200   -19.72900 -29.39300 1.000 49.57000  ? 504  HIS B CG  1 
ATOM   7750  N ND1 . HIS B 1 485 ? 5.52500   -19.74200 -30.61600 1.000 47.63000  ? 504  HIS B ND1 1 
ATOM   7751  C CD2 . HIS B 1 485 ? 5.47200   -20.58700 -28.60200 1.000 46.20000  ? 504  HIS B CD2 1 
ATOM   7752  C CE1 . HIS B 1 485 ? 4.49700   -20.57100 -30.56800 1.000 46.57000  ? 504  HIS B CE1 1 
ATOM   7753  N NE2 . HIS B 1 485 ? 4.44200   -21.09600 -29.35700 1.000 53.40000  ? 504  HIS B NE2 1 
ATOM   7754  N N   . ARG B 1 486 ? 6.46400   -17.42500 -26.52800 1.000 40.38000  ? 505  ARG B N   1 
ATOM   7755  C CA  . ARG B 1 486 ? 5.55100   -17.34900 -25.39500 1.000 36.94000  ? 505  ARG B CA  1 
ATOM   7756  C C   . ARG B 1 486 ? 5.22700   -15.91000 -25.01800 1.000 40.27000  ? 505  ARG B C   1 
ATOM   7757  O O   . ARG B 1 486 ? 4.10800   -15.61600 -24.58500 1.000 47.17000  ? 505  ARG B O   1 
ATOM   7758  C CB  . ARG B 1 486 ? 6.16900   -18.09700 -24.22200 1.000 41.43000  ? 505  ARG B CB  1 
ATOM   7759  C CG  . ARG B 1 486 ? 6.12200   -19.58600 -24.43400 1.000 40.67000  ? 505  ARG B CG  1 
ATOM   7760  C CD  . ARG B 1 486 ? 7.16100   -20.32300 -23.61300 1.000 47.52000  ? 505  ARG B CD  1 
ATOM   7761  N NE  . ARG B 1 486 ? 7.01600   -21.76200 -23.79200 1.000 48.37000  ? 505  ARG B NE  1 
ATOM   7762  C CZ  . ARG B 1 486 ? 7.39500   -22.42300 -24.87900 1.000 46.42000  ? 505  ARG B CZ  1 
ATOM   7763  N NH1 . ARG B 1 486 ? 7.85300   -21.79300 -25.95000 1.000 40.86000  ? 505  ARG B NH1 1 
ATOM   7764  N NH2 . ARG B 1 486 ? 7.26200   -23.74400 -24.91200 1.000 50.47000  ? 505  ARG B NH2 1 
ATOM   7765  N N   . ALA B 1 487 ? 6.18800   -15.00000 -25.14600 1.000 41.74000  ? 506  ALA B N   1 
ATOM   7766  C CA  . ALA B 1 487 ? 5.89900   -13.61000 -24.81500 1.000 45.73000  ? 506  ALA B CA  1 
ATOM   7767  C C   . ALA B 1 487 ? 4.82800   -13.05000 -25.73600 1.000 41.70000  ? 506  ALA B C   1 
ATOM   7768  O O   . ALA B 1 487 ? 3.93600   -12.31500 -25.30000 1.000 48.58000  ? 506  ALA B O   1 
ATOM   7769  C CB  . ALA B 1 487 ? 7.17400   -12.77600 -24.89600 1.000 33.70000  ? 506  ALA B CB  1 
ATOM   7770  N N   . ASP B 1 488 ? 4.90700   -13.39000 -27.01600 1.000 47.57000  ? 507  ASP B N   1 
ATOM   7771  C CA  . ASP B 1 488 ? 3.91200   -12.95000 -27.98600 1.000 53.08000  ? 507  ASP B CA  1 
ATOM   7772  C C   . ASP B 1 488 ? 2.58800   -13.68700 -27.80600 1.000 47.44000  ? 507  ASP B C   1 
ATOM   7773  O O   . ASP B 1 488 ? 1.51600   -13.08000 -27.91000 1.000 54.57000  ? 507  ASP B O   1 
ATOM   7774  C CB  . ASP B 1 488 ? 4.48600   -13.14600 -29.38800 1.000 51.34000  ? 507  ASP B CB  1 
ATOM   7775  C CG  . ASP B 1 488 ? 3.53700   -12.73800 -30.47600 1.000 62.63000  ? 507  ASP B CG  1 
ATOM   7776  O OD1 . ASP B 1 488 ? 3.20300   -11.53300 -30.54800 1.000 68.74000  ? 507  ASP B OD1 1 
ATOM   7777  O OD2 . ASP B 1 488 ? 3.18100   -13.61400 -31.29900 1.000 62.42000  ? 507  ASP B OD2 1 
ATOM   7778  N N   . ALA B 1 489 ? 2.63800   -14.98900 -27.52400 1.000 48.18000  ? 508  ALA B N   1 
ATOM   7779  C CA  . ALA B 1 489 ? 1.41000   -15.77400 -27.43200 1.000 49.16000  ? 508  ALA B CA  1 
ATOM   7780  C C   . ALA B 1 489 ? 0.54900   -15.35300 -26.24900 1.000 46.75000  ? 508  ALA B C   1 
ATOM   7781  O O   . ALA B 1 489 ? -0.67600  -15.24100 -26.37800 1.000 49.18000  ? 508  ALA B O   1 
ATOM   7782  C CB  . ALA B 1 489 ? 1.74300   -17.26100 -27.34100 1.000 49.76000  ? 508  ALA B CB  1 
ATOM   7783  N N   . ILE B 1 490 ? 1.16400   -15.12400 -25.08400 1.000 46.90000  ? 509  ILE B N   1 
ATOM   7784  C CA  . ILE B 1 490 ? 0.37900   -14.91000 -23.86900 1.000 47.79000  ? 509  ILE B CA  1 
ATOM   7785  C C   . ILE B 1 490 ? -0.43900  -13.62800 -23.96200 1.000 54.78000  ? 509  ILE B C   1 
ATOM   7786  O O   . ILE B 1 490 ? -1.55000  -13.55300 -23.41700 1.000 49.85000  ? 509  ILE B O   1 
ATOM   7787  C CB  . ILE B 1 490 ? 1.28300   -14.92300 -22.62000 1.000 50.29000  ? 509  ILE B CB  1 
ATOM   7788  C CG1 . ILE B 1 490 ? 0.41900   -14.99200 -21.35700 1.000 44.32000  ? 509  ILE B CG1 1 
ATOM   7789  C CG2 . ILE B 1 490 ? 2.21200   -13.70700 -22.60400 1.000 45.85000  ? 509  ILE B CG2 1 
ATOM   7790  C CD1 . ILE B 1 490 ? 1.14800   -15.43400 -20.12300 1.000 41.35000  ? 509  ILE B CD1 1 
ATOM   7791  N N   . LYS B 1 491 ? 0.08100   -12.60600 -24.65400 1.000 53.74000  ? 510  LYS B N   1 
ATOM   7792  C CA  . LYS B 1 491 ? -0.73200  -11.42600 -24.92700 1.000 55.70000  ? 510  LYS B CA  1 
ATOM   7793  C C   . LYS B 1 491 ? -1.95200  -11.80800 -25.75300 1.000 56.85000  ? 510  LYS B C   1 
ATOM   7794  O O   . LYS B 1 491 ? -3.06100  -11.31400 -25.51400 1.000 57.26000  ? 510  LYS B O   1 
ATOM   7795  C CB  . LYS B 1 491 ? 0.09900   -10.35400 -25.64200 1.000 60.49000  ? 510  LYS B CB  1 
ATOM   7796  C CG  . LYS B 1 491 ? 1.19900   -9.72300  -24.78100 1.000 62.79000  ? 510  LYS B CG  1 
ATOM   7797  C CD  . LYS B 1 491 ? 1.98600   -8.66100  -25.54700 1.000 76.09000  ? 510  LYS B CD  1 
ATOM   7798  C CE  . LYS B 1 491 ? 1.20100   -7.35700  -25.70400 1.000 79.45000  ? 510  LYS B CE  1 
ATOM   7799  N NZ  . LYS B 1 491 ? 1.07200   -6.60700  -24.41500 1.000 81.91000  ? 510  LYS B NZ  1 
ATOM   7800  N N   . SER B 1 492 ? -1.76800  -12.71400 -26.71100 1.000 53.96000  ? 511  SER B N   1 
ATOM   7801  C CA  . SER B 1 492 ? -2.88200  -13.18100 -27.52400 1.000 52.60000  ? 511  SER B CA  1 
ATOM   7802  C C   . SER B 1 492 ? -3.86400  -14.02300 -26.71100 1.000 51.82000  ? 511  SER B C   1 
ATOM   7803  O O   . SER B 1 492 ? -5.06100  -14.03400 -27.00400 1.000 44.37000  ? 511  SER B O   1 
ATOM   7804  C CB  . SER B 1 492 ? -2.33700  -13.96900 -28.72000 1.000 45.47000  ? 511  SER B CB  1 
ATOM   7805  O OG  . SER B 1 492 ? -3.37800  -14.51500 -29.49900 1.000 67.89000  ? 511  SER B OG  1 
ATOM   7806  N N   . TYR B 1 493 ? -3.38600  -14.73500 -25.69400 1.000 56.64000  ? 512  TYR B N   1 
ATOM   7807  C CA  . TYR B 1 493 ? -4.26200  -15.63900 -24.95800 1.000 46.23000  ? 512  TYR B CA  1 
ATOM   7808  C C   . TYR B 1 493 ? -5.17300  -14.90000 -23.97800 1.000 47.39000  ? 512  TYR B C   1 
ATOM   7809  O O   . TYR B 1 493 ? -6.33900  -15.27200 -23.82400 1.000 56.24000  ? 512  TYR B O   1 
ATOM   7810  C CB  . TYR B 1 493 ? -3.42300  -16.68400 -24.21800 1.000 47.23000  ? 512  TYR B CB  1 
ATOM   7811  C CG  . TYR B 1 493 ? -4.23700  -17.56400 -23.30000 1.000 46.45000  ? 512  TYR B CG  1 
ATOM   7812  C CD1 . TYR B 1 493 ? -4.99000  -18.62200 -23.80000 1.000 46.65000  ? 512  TYR B CD1 1 
ATOM   7813  C CD2 . TYR B 1 493 ? -4.27600  -17.31400 -21.93600 1.000 46.06000  ? 512  TYR B CD2 1 
ATOM   7814  C CE1 . TYR B 1 493 ? -5.74400  -19.41900 -22.96600 1.000 46.20000  ? 512  TYR B CE1 1 
ATOM   7815  C CE2 . TYR B 1 493 ? -5.02900  -18.09600 -21.09100 1.000 49.73000  ? 512  TYR B CE2 1 
ATOM   7816  C CZ  . TYR B 1 493 ? -5.76500  -19.14700 -21.61400 1.000 53.18000  ? 512  TYR B CZ  1 
ATOM   7817  O OH  . TYR B 1 493 ? -6.51400  -19.93200 -20.77900 1.000 44.70000  ? 512  TYR B OH  1 
ATOM   7818  N N   . CYS B 1 494 ? -4.65500  -13.87200 -23.29600 1.000 50.11000  ? 513  CYS B N   1 
ATOM   7819  C CA  . CYS B 1 494 ? -5.37000  -13.19700 -22.21900 1.000 52.54000  ? 513  CYS B CA  1 
ATOM   7820  C C   . CYS B 1 494 ? -4.62300  -11.96400 -21.74200 1.000 57.52000  ? 513  CYS B C   1 
ATOM   7821  O O   . CYS B 1 494 ? -3.42100  -12.03700 -21.48900 1.000 63.35000  ? 513  CYS B O   1 
ATOM   7822  C CB  . CYS B 1 494 ? -5.56300  -14.17400 -21.04700 1.000 46.28000  ? 513  CYS B CB  1 
ATOM   7823  S SG  . CYS B 1 494 ? -6.48300  -13.54400 -19.61500 1.000 53.53000  ? 513  CYS B SG  1 
ATOM   7824  N N   . GLU B 1 495 ? -5.30600  -10.83400 -21.59700 1.000 64.49000  ? 514  GLU B N   1 
ATOM   7825  C CA  . GLU B 1 495 ? -4.58500  -9.64200  -21.13700 1.000 64.74000  ? 514  GLU B CA  1 
ATOM   7826  C C   . GLU B 1 495 ? -4.59200  -9.47700  -19.62700 1.000 55.67000  ? 514  GLU B C   1 
ATOM   7827  O O   . GLU B 1 495 ? -4.05100  -8.49300  -19.13100 1.000 53.07000  ? 514  GLU B O   1 
ATOM   7828  C CB  . GLU B 1 495 ? -5.08400  -8.33900  -21.79700 1.000 78.33000  ? 514  GLU B CB  1 
ATOM   7829  C CG  . GLU B 1 495 ? -6.33700  -7.59900  -21.20600 1.000 93.50000  ? 514  GLU B CG  1 
ATOM   7830  C CD  . GLU B 1 495 ? -7.58000  -7.71200  -22.06200 1.000 105.95000 ? 514  GLU B CD  1 
ATOM   7831  O OE1 . GLU B 1 495 ? -7.71200  -8.67600  -22.85500 1.000 106.33000 ? 514  GLU B OE1 1 
ATOM   7832  O OE2 . GLU B 1 495 ? -8.42900  -6.78800  -21.94700 1.000 120.15000 ? 514  GLU B OE2 1 
ATOM   7833  N N   . ILE B 1 496 ? -5.16800  -10.41000 -18.89300 1.000 51.79000  ? 515  ILE B N   1 
ATOM   7834  C CA  . ILE B 1 496 ? -5.20200  -10.28100 -17.42000 1.000 53.65000  ? 515  ILE B CA  1 
ATOM   7835  C C   . ILE B 1 496 ? -3.80400  -10.46000 -16.83900 1.000 52.00000  ? 515  ILE B C   1 
ATOM   7836  O O   . ILE B 1 496 ? -3.14400  -11.47900 -17.11700 1.000 52.92000  ? 515  ILE B O   1 
ATOM   7837  C CB  . ILE B 1 496 ? -6.15500  -11.31100 -16.79000 1.000 46.07000  ? 515  ILE B CB  1 
ATOM   7838  C CG1 . ILE B 1 496 ? -7.59800  -10.99800 -17.22800 1.000 47.48000  ? 515  ILE B CG1 1 
ATOM   7839  C CG2 . ILE B 1 496 ? -6.06700  -11.28700 -15.29700 1.000 42.14000  ? 515  ILE B CG2 1 
ATOM   7840  C CD1 . ILE B 1 496 ? -8.59700  -12.03700 -16.78200 1.000 50.20000  ? 515  ILE B CD1 1 
ATOM   7841  N N   . PRO B 1 497 ? -3.31500  -9.51300  -16.03500 1.000 51.72000  ? 516  PRO B N   1 
ATOM   7842  C CA  . PRO B 1 497 ? -1.95300  -9.62900  -15.48800 1.000 52.79000  ? 516  PRO B CA  1 
ATOM   7843  C C   . PRO B 1 497 ? -1.78700  -10.90100 -14.66400 1.000 50.05000  ? 516  PRO B C   1 
ATOM   7844  O O   . PRO B 1 497 ? -2.68600  -11.31000 -13.92100 1.000 46.42000  ? 516  PRO B O   1 
ATOM   7845  C CB  . PRO B 1 497 ? -1.81400  -8.37200  -14.61900 1.000 50.51000  ? 516  PRO B CB  1 
ATOM   7846  C CG  . PRO B 1 497 ? -2.80600  -7.40300  -15.20600 1.000 55.36000  ? 516  PRO B CG  1 
ATOM   7847  C CD  . PRO B 1 497 ? -3.96500  -8.24700  -15.66400 1.000 49.39000  ? 516  PRO B CD  1 
ATOM   7848  N N   . LEU B 1 498 ? -0.63700  -11.53000 -14.82200 1.000 46.44000  ? 517  LEU B N   1 
ATOM   7849  C CA  . LEU B 1 498 ? -0.35100  -12.75300 -14.09500 1.000 47.78000  ? 517  LEU B CA  1 
ATOM   7850  C C   . LEU B 1 498 ? -0.06200  -12.46100 -12.62300 1.000 50.30000  ? 517  LEU B C   1 
ATOM   7851  O O   . LEU B 1 498 ? 0.57600   -11.45300 -12.29600 1.000 50.21000  ? 517  LEU B O   1 
ATOM   7852  C CB  . LEU B 1 498 ? 0.83600   -13.46600 -14.72500 1.000 49.94000  ? 517  LEU B CB  1 
ATOM   7853  C CG  . LEU B 1 498 ? 0.59500   -14.12700 -16.07000 1.000 40.68000  ? 517  LEU B CG  1 
ATOM   7854  C CD1 . LEU B 1 498 ? 1.94300   -14.32900 -16.66000 1.000 47.10000  ? 517  LEU B CD1 1 
ATOM   7855  C CD2 . LEU B 1 498 ? -0.10000  -15.46500 -15.88100 1.000 38.44000  ? 517  LEU B CD2 1 
ATOM   7856  N N   . PRO B 1 499 ? -0.49800  -13.33000 -11.71800 1.000 47.35000  ? 518  PRO B N   1 
ATOM   7857  C CA  . PRO B 1 499 ? -0.26100  -13.15300 -10.27000 1.000 45.00000  ? 518  PRO B CA  1 
ATOM   7858  C C   . PRO B 1 499 ? 1.16700   -13.50700 -9.86700  1.000 49.50000  ? 518  PRO B C   1 
ATOM   7859  O O   . PRO B 1 499 ? 1.42700   -14.49100 -9.16800  1.000 48.85000  ? 518  PRO B O   1 
ATOM   7860  C CB  . PRO B 1 499 ? -1.29500  -14.10000 -9.65600  1.000 44.57000  ? 518  PRO B CB  1 
ATOM   7861  C CG  . PRO B 1 499 ? -1.44300  -15.18500 -10.67300 1.000 43.04000  ? 518  PRO B CG  1 
ATOM   7862  C CD  . PRO B 1 499 ? -1.30400  -14.52600 -12.01200 1.000 45.37000  ? 518  PRO B CD  1 
ATOM   7863  N N   . ILE B 1 500 ? 2.11100   -12.66900 -10.29600 1.000 48.02000  ? 519  ILE B N   1 
ATOM   7864  C CA  . ILE B 1 500 ? 3.54400   -12.91700 -10.14800 1.000 51.24000  ? 519  ILE B CA  1 
ATOM   7865  C C   . ILE B 1 500 ? 4.02700   -12.35700 -8.82000  1.000 51.84000  ? 519  ILE B C   1 
ATOM   7866  O O   . ILE B 1 500 ? 3.71300   -11.21500 -8.46600  1.000 57.14000  ? 519  ILE B O   1 
ATOM   7867  C CB  . ILE B 1 500 ? 4.32100   -12.29000 -11.31600 1.000 50.84000  ? 519  ILE B CB  1 
ATOM   7868  C CG1 . ILE B 1 500 ? 3.91200   -12.95700 -12.62800 1.000 49.36000  ? 519  ILE B CG1 1 
ATOM   7869  C CG2 . ILE B 1 500 ? 5.81400   -12.38400 -11.07700 1.000 49.37000  ? 519  ILE B CG2 1 
ATOM   7870  C CD1 . ILE B 1 500 ? 4.24100   -12.15300 -13.85800 1.000 56.97000  ? 519  ILE B CD1 1 
ATOM   7871  N N   . ILE B 1 501 ? 4.79700   -13.15700 -8.09000  1.000 55.04000  ? 520  ILE B N   1 
ATOM   7872  C CA  . ILE B 1 501 ? 5.42200   -12.74800 -6.83700  1.000 60.30000  ? 520  ILE B CA  1 
ATOM   7873  C C   . ILE B 1 501 ? 6.89100   -12.44100 -7.11000  1.000 60.11000  ? 520  ILE B C   1 
ATOM   7874  O O   . ILE B 1 501 ? 7.70000   -13.35500 -7.31100  1.000 55.32000  ? 520  ILE B O   1 
ATOM   7875  C CB  . ILE B 1 501 ? 5.26600   -13.82700 -5.75800  1.000 49.58000  ? 520  ILE B CB  1 
ATOM   7876  C CG1 . ILE B 1 501 ? 3.80200   -13.92800 -5.33600  1.000 57.35000  ? 520  ILE B CG1 1 
ATOM   7877  C CG2 . ILE B 1 501 ? 6.17800   -13.55600 -4.57500  1.000 58.92000  ? 520  ILE B CG2 1 
ATOM   7878  C CD1 . ILE B 1 501 ? 3.49300   -15.14600 -4.51600  1.000 60.73000  ? 520  ILE B CD1 1 
ATOM   7879  N N   . LYS B 1 502 ? 7.23100   -11.14400 -7.12100  1.000 68.82000  ? 521  LYS B N   1 
ATOM   7880  C CA  . LYS B 1 502 ? 8.60700   -10.66000 -7.26800  1.000 64.62000  ? 521  LYS B CA  1 
ATOM   7881  C C   . LYS B 1 502 ? 9.12700   -10.30000 -5.88500  1.000 73.85000  ? 521  LYS B C   1 
ATOM   7882  O O   . LYS B 1 502 ? 8.88300   -9.19700  -5.38900  1.000 82.23000  ? 521  LYS B O   1 
ATOM   7883  C CB  . LYS B 1 502 ? 8.69100   -9.43100  -8.17100  1.000 67.45000  ? 521  LYS B CB  1 
ATOM   7884  C CG  . LYS B 1 502 ? 8.45100   -9.61900  -9.65100  1.000 71.69000  ? 521  LYS B CG  1 
ATOM   7885  C CD  . LYS B 1 502 ? 8.53300   -8.25400  -10.33400 1.000 71.88000  ? 521  LYS B CD  1 
ATOM   7886  C CE  . LYS B 1 502 ? 9.96000   -7.70300  -10.24400 1.000 82.92000  ? 521  LYS B CE  1 
ATOM   7887  N NZ  . LYS B 1 502 ? 10.14800  -6.40400  -10.95100 1.000 81.55000  ? 521  LYS B NZ  1 
ATOM   7888  N N   . SER B 1 503 ? 9.85400   -11.21400 -5.26400  1.000 73.17000  ? 522  SER B N   1 
ATOM   7889  C CA  . SER B 1 503 ? 10.64000  -10.87900 -4.09000  1.000 77.90000  ? 522  SER B CA  1 
ATOM   7890  C C   . SER B 1 503 ? 12.10700  -11.04600 -4.43400  1.000 71.15000  ? 522  SER B C   1 
ATOM   7891  O O   . SER B 1 503 ? 12.50900  -12.10800 -4.92200  1.000 69.48000  ? 522  SER B O   1 
ATOM   7892  C CB  . SER B 1 503 ? 10.26300  -11.75200 -2.89100  1.000 87.24000  ? 522  SER B CB  1 
ATOM   7893  O OG  . SER B 1 503 ? 8.96100   -11.44600 -2.42400  1.000 74.46000  ? 522  SER B OG  1 
ATOM   7894  N N   . LYS B 1 504 ? 12.88100  -9.98500  -4.20500  1.000 80.80000  ? 523  LYS B N   1 
ATOM   7895  C CA  . LYS B 1 504 ? 14.34500  -9.98600  -4.31800  1.000 97.08000  ? 523  LYS B CA  1 
ATOM   7896  C C   . LYS B 1 504 ? 14.84500  -8.54500  -4.24200  1.000 99.71000  ? 523  LYS B C   1 
ATOM   7897  O O   . LYS B 1 504 ? 14.39800  -7.68400  -5.00500  1.000 103.84000 ? 523  LYS B O   1 
ATOM   7898  C CB  . LYS B 1 504 ? 14.82300  -10.63900 -5.62200  1.000 88.67000  ? 523  LYS B CB  1 
ATOM   7899  C CG  . LYS B 1 504 ? 16.31200  -10.92900 -5.68400  1.000 77.03000  ? 523  LYS B CG  1 
ATOM   7900  C CD  . LYS B 1 504 ? 16.64500  -11.72700 -6.93500  1.000 66.36000  ? 523  LYS B CD  1 
ATOM   7901  C CE  . LYS B 1 504 ? 16.62600  -10.87200 -8.19200  1.000 67.93000  ? 523  LYS B CE  1 
ATOM   7902  N NZ  . LYS B 1 504 ? 17.03900  -11.67000 -9.37700  1.000 68.07000  ? 523  LYS B NZ  1 
ATOM   7903  N N   . GLY C 2 2   ? 7.77000   -20.36100 3.84200   1.000 59.19000  ? 566  GLY C N   1 
ATOM   7904  C CA  . GLY C 2 2   ? 8.25700   -21.48800 4.61300   1.000 81.70000  ? 566  GLY C CA  1 
ATOM   7905  C C   . GLY C 2 2   ? 7.16100   -22.26300 5.32600   1.000 87.02000  ? 566  GLY C C   1 
ATOM   7906  O O   . GLY C 2 2   ? 7.03900   -22.19600 6.55200   1.000 84.08000  ? 566  GLY C O   1 
ATOM   7907  N N   . ASP C 2 3   ? 6.37300   -23.00800 4.55300   1.000 88.37000  ? 567  ASP C N   1 
ATOM   7908  C CA  . ASP C 2 3   ? 5.28100   -23.80200 5.09600   1.000 94.28000  ? 567  ASP C CA  1 
ATOM   7909  C C   . ASP C 2 3   ? 5.74000   -25.20200 5.50000   1.000 95.69000  ? 567  ASP C C   1 
ATOM   7910  O O   . ASP C 2 3   ? 4.92000   -26.01600 5.94600   1.000 90.78000  ? 567  ASP C O   1 
ATOM   7911  C CB  . ASP C 2 3   ? 4.13500   -23.86400 4.07400   1.000 93.56000  ? 567  ASP C CB  1 
ATOM   7912  C CG  . ASP C 2 3   ? 2.79700   -24.23800 4.70000   1.000 106.16000 ? 567  ASP C CG  1 
ATOM   7913  O OD1 . ASP C 2 3   ? 2.74500   -24.53600 5.91600   1.000 106.60000 ? 567  ASP C OD1 1 
ATOM   7914  O OD2 . ASP C 2 3   ? 1.78400   -24.17800 3.97300   1.000 109.41000 ? 567  ASP C OD2 1 
ATOM   7915  N N   . GLY C 2 4   ? 7.03800   -25.48500 5.37700   1.000 84.85000  ? 568  GLY C N   1 
ATOM   7916  C CA  . GLY C 2 4   ? 7.63900   -26.66100 5.97800   1.000 74.99000  ? 568  GLY C CA  1 
ATOM   7917  C C   . GLY C 2 4   ? 8.42500   -27.56600 5.05100   1.000 78.30000  ? 568  GLY C C   1 
ATOM   7918  O O   . GLY C 2 4   ? 9.51600   -28.01300 5.41400   1.000 79.59000  ? 568  GLY C O   1 
ATOM   7919  N N   . LEU C 2 5   ? 7.92200   -27.82700 3.84900   1.000 71.96000  ? 569  LEU C N   1 
ATOM   7920  C CA  . LEU C 2 5   ? 8.69400   -28.60900 2.88400   1.000 64.60000  ? 569  LEU C CA  1 
ATOM   7921  C C   . LEU C 2 5   ? 8.59900   -28.07600 1.46300   1.000 60.95000  ? 569  LEU C C   1 
ATOM   7922  O O   . LEU C 2 5   ? 9.46000   -28.40400 0.63400   1.000 54.28000  ? 569  LEU C O   1 
ATOM   7923  C CB  . LEU C 2 5   ? 8.25100   -30.08000 2.92000   1.000 68.46000  ? 569  LEU C CB  1 
ATOM   7924  C CG  . LEU C 2 5   ? 9.00400   -31.13400 2.10900   1.000 63.64000  ? 569  LEU C CG  1 
ATOM   7925  C CD1 . LEU C 2 5   ? 10.47200  -31.07700 2.41200   1.000 57.10000  ? 569  LEU C CD1 1 
ATOM   7926  C CD2 . LEU C 2 5   ? 8.47600   -32.51100 2.46800   1.000 65.52000  ? 569  LEU C CD2 1 
ATOM   7927  N N   . SER C 2 6   ? 7.60600   -27.24800 1.16100   1.000 56.78000  ? 570  SER C N   1 
ATOM   7928  C CA  . SER C 2 6   ? 7.48400   -26.62500 -0.14200  1.000 56.74000  ? 570  SER C CA  1 
ATOM   7929  C C   . SER C 2 6   ? 8.55600   -25.55900 -0.35200  1.000 57.47000  ? 570  SER C C   1 
ATOM   7930  O O   . SER C 2 6   ? 9.06600   -24.95600 0.59600   1.000 60.58000  ? 570  SER C O   1 
ATOM   7931  C CB  . SER C 2 6   ? 6.09100   -26.02300 -0.28300  1.000 61.41000  ? 570  SER C CB  1 
ATOM   7932  O OG  . SER C 2 6   ? 5.84100   -25.10900 0.76800   1.000 75.05000  ? 570  SER C OG  1 
ATOM   7933  N N   . LEU C 2 7   ? 8.91600   -25.36500 -1.62000  1.000 57.12000  ? 571  LEU C N   1 
ATOM   7934  C CA  . LEU C 2 7   ? 9.88700   -24.40400 -2.14100  1.000 50.48000  ? 571  LEU C CA  1 
ATOM   7935  C C   . LEU C 2 7   ? 11.31700  -24.63000 -1.67800  1.000 48.82000  ? 571  LEU C C   1 
ATOM   7936  O O   . LEU C 2 7   ? 12.14500  -23.71300 -1.81000  1.000 49.45000  ? 571  LEU C O   1 
ATOM   7937  C CB  . LEU C 2 7   ? 9.52900   -22.94600 -1.83900  1.000 45.01000  ? 571  LEU C CB  1 
ATOM   7938  C CG  . LEU C 2 7   ? 8.27900   -22.48000 -2.55600  1.000 53.74000  ? 571  LEU C CG  1 
ATOM   7939  C CD1 . LEU C 2 7   ? 8.28100   -20.95700 -2.64100  1.000 57.51000  ? 571  LEU C CD1 1 
ATOM   7940  C CD2 . LEU C 2 7   ? 8.14000   -23.16600 -3.90400  1.000 52.29000  ? 571  LEU C CD2 1 
ATOM   7941  N N   . ILE C 2 8   ? 11.65200  -25.79700 -1.16200  1.000 43.50000  ? 572  ILE C N   1 
ATOM   7942  C CA  . ILE C 2 8   ? 13.06500  -26.11000 -1.02200  1.000 44.83000  ? 572  ILE C CA  1 
ATOM   7943  C C   . ILE C 2 8   ? 13.58000  -26.51900 -2.39400  1.000 50.40000  ? 572  ILE C C   1 
ATOM   7944  O O   . ILE C 2 8   ? 12.81400  -26.94200 -3.27000  1.000 48.67000  ? 572  ILE C O   1 
ATOM   7945  C CB  . ILE C 2 8   ? 13.30400  -27.19700 0.04600   1.000 49.54000  ? 572  ILE C CB  1 
ATOM   7946  C CG1 . ILE C 2 8   ? 12.80800  -28.56500 -0.42000  1.000 47.78000  ? 572  ILE C CG1 1 
ATOM   7947  C CG2 . ILE C 2 8   ? 12.57800  -26.83200 1.34400   1.000 47.70000  ? 572  ILE C CG2 1 
ATOM   7948  C CD1 . ILE C 2 8   ? 13.88200  -29.42000 -1.06900  1.000 45.95000  ? 572  ILE C CD1 1 
ATOM   7949  N N   . SER C 2 9   ? 14.88400  -26.37800 -2.60000  1.000 47.40000  ? 573  SER C N   1 
ATOM   7950  C CA  . SER C 2 9   ? 15.49200  -26.72800 -3.87400  1.000 41.80000  ? 573  SER C CA  1 
ATOM   7951  C C   . SER C 2 9   ? 16.69200  -27.63200 -3.66400  1.000 46.16000  ? 573  SER C C   1 
ATOM   7952  O O   . SER C 2 9   ? 17.38800  -27.55400 -2.64200  1.000 46.93000  ? 573  SER C O   1 
ATOM   7953  C CB  . SER C 2 9   ? 15.90700  -25.48000 -4.65100  1.000 44.90000  ? 573  SER C CB  1 
ATOM   7954  O OG  . SER C 2 9   ? 14.76700  -24.71000 -5.00600  1.000 45.65000  ? 573  SER C OG  1 
ATOM   7955  N N   . ILE C 2 10  ? 16.92600  -28.49800 -4.65000  1.000 41.52000  ? 574  ILE C N   1 
ATOM   7956  C CA  . ILE C 2 10  ? 18.10000  -29.35600 -4.68500  1.000 41.88000  ? 574  ILE C CA  1 
ATOM   7957  C C   . ILE C 2 10  ? 18.94300  -28.93700 -5.87300  1.000 47.37000  ? 574  ILE C C   1 
ATOM   7958  O O   . ILE C 2 10  ? 18.40900  -28.64200 -6.95800  1.000 43.52000  ? 574  ILE C O   1 
ATOM   7959  C CB  . ILE C 2 10  ? 17.72600  -30.84500 -4.78900  1.000 41.28000  ? 574  ILE C CB  1 
ATOM   7960  C CG1 . ILE C 2 10  ? 16.88100  -31.26900 -3.57400  1.000 43.36000  ? 574  ILE C CG1 1 
ATOM   7961  C CG2 . ILE C 2 10  ? 18.97000  -31.72700 -4.97200  1.000 34.27000  ? 574  ILE C CG2 1 
ATOM   7962  C CD1 . ILE C 2 10  ? 17.56500  -31.05900 -2.23400  1.000 38.96000  ? 574  ILE C CD1 1 
ATOM   7963  N N   . ILE C 2 11  ? 20.26300  -28.89800 -5.67200  1.000 49.73000  ? 575  ILE C N   1 
ATOM   7964  C CA  . ILE C 2 11  ? 21.22100  -28.56000 -6.72100  1.000 45.08000  ? 575  ILE C CA  1 
ATOM   7965  C C   . ILE C 2 11  ? 21.92700  -29.83600 -7.14800  1.000 49.53000  ? 575  ILE C C   1 
ATOM   7966  O O   . ILE C 2 11  ? 22.50600  -30.54900 -6.31600  1.000 53.87000  ? 575  ILE C O   1 
ATOM   7967  C CB  . ILE C 2 11  ? 22.21900  -27.50800 -6.21500  1.000 52.63000  ? 575  ILE C CB  1 
ATOM   7968  C CG1 . ILE C 2 11  ? 21.49000  -26.16900 -6.08100  1.000 52.23000  ? 575  ILE C CG1 1 
ATOM   7969  C CG2 . ILE C 2 11  ? 23.43500  -27.42100 -7.12000  1.000 50.20000  ? 575  ILE C CG2 1 
ATOM   7970  C CD1 . ILE C 2 11  ? 22.24600  -25.11900 -5.30600  1.000 57.74000  ? 575  ILE C CD1 1 
ATOM   7971  N N   . ASP C 2 12  ? 21.87700  -30.13700 -8.45000  1.000 48.57000  ? 576  ASP C N   1 
ATOM   7972  C CA  . ASP C 2 12  ? 22.48800  -31.36200 -8.96900  1.000 57.85000  ? 576  ASP C CA  1 
ATOM   7973  C C   . ASP C 2 12  ? 23.99700  -31.31900 -8.90500  1.000 57.39000  ? 576  ASP C C   1 
ATOM   7974  O O   . ASP C 2 12  ? 24.63600  -32.32200 -8.57400  1.000 60.65000  ? 576  ASP C O   1 
ATOM   7975  C CB  . ASP C 2 12  ? 22.05500  -31.63400 -10.41000 1.000 54.92000  ? 576  ASP C CB  1 
ATOM   7976  C CG  . ASP C 2 12  ? 20.69000  -32.28700 -10.49000 1.000 65.18000  ? 576  ASP C CG  1 
ATOM   7977  O OD1 . ASP C 2 12  ? 20.28300  -32.91900 -9.50000  1.000 58.52000  ? 576  ASP C OD1 1 
ATOM   7978  O OD2 . ASP C 2 12  ? 20.07300  -32.20400 -11.57200 1.000 65.52000  ? 576  ASP C OD2 1 
ATOM   7979  N N   . GLU C 2 13  ? 24.60400  -30.17800 -9.25400  1.000 58.30000  ? 577  GLU C N   1 
ATOM   7980  C CA  . GLU C 2 13  ? 26.04700  -30.09000 -9.44100  1.000 62.55000  ? 577  GLU C CA  1 
ATOM   7981  C C   . GLU C 2 13  ? 26.66800  -29.65900 -8.12300  1.000 60.89000  ? 577  GLU C C   1 
ATOM   7982  O O   . GLU C 2 13  ? 26.55000  -28.49400 -7.72800  1.000 61.52000  ? 577  GLU C O   1 
ATOM   7983  C CB  . GLU C 2 13  ? 26.40700  -29.09800 -10.54300 1.000 56.52000  ? 577  GLU C CB  1 
ATOM   7984  C CG  . GLU C 2 13  ? 25.88000  -29.42300 -11.92700 1.000 56.34000  ? 577  GLU C CG  1 
ATOM   7985  C CD  . GLU C 2 13  ? 24.42500  -28.98400 -12.10600 1.000 61.39000  ? 577  GLU C CD  1 
ATOM   7986  O OE1 . GLU C 2 13  ? 23.82300  -28.45700 -11.13700 1.000 55.21000  ? 577  GLU C OE1 1 
ATOM   7987  O OE2 . GLU C 2 13  ? 23.89000  -29.14900 -13.22400 1.000 69.35000  ? 577  GLU C OE2 1 
ATOM   7988  N N   . VAL C 2 14  ? 27.32500  -30.58100 -7.45200  1.000 62.47000  ? 578  VAL C N   1 
ATOM   7989  C CA  . VAL C 2 14  ? 28.06300  -30.23300 -6.24700  1.000 68.90000  ? 578  VAL C CA  1 
ATOM   7990  C C   . VAL C 2 14  ? 29.37600  -29.58600 -6.64700  1.000 68.54000  ? 578  VAL C C   1 
ATOM   7991  O O   . VAL C 2 14  ? 30.03900  -30.02600 -7.59100  1.000 68.69000  ? 578  VAL C O   1 
ATOM   7992  C CB  . VAL C 2 14  ? 28.27700  -31.47000 -5.35500  1.000 67.01000  ? 578  VAL C CB  1 
ATOM   7993  C CG1 . VAL C 2 14  ? 28.94600  -32.57700 -6.14600  1.000 63.63000  ? 578  VAL C CG1 1 
ATOM   7994  C CG2 . VAL C 2 14  ? 29.13900  -31.10200 -4.16800  1.000 68.15000  ? 578  VAL C CG2 1 
ATOM   7995  N N   . GLY C 2 15  ? 29.73200  -28.50700 -5.95600  1.000 67.72000  ? 579  GLY C N   1 
ATOM   7996  C CA  . GLY C 2 15  ? 30.99900  -27.85700 -6.20500  1.000 69.85000  ? 579  GLY C CA  1 
ATOM   7997  C C   . GLY C 2 15  ? 31.37600  -26.88400 -5.10700  1.000 73.72000  ? 579  GLY C C   1 
ATOM   7998  O O   . GLY C 2 15  ? 30.50300  -26.23700 -4.51000  1.000 74.12000  ? 579  GLY C O   1 
ATOM   7999  N N   . ASN C 2 16  ? 32.67400  -26.78300 -4.82400  1.000 74.06000  ? 580  ASN C N   1 
ATOM   8000  C CA  . ASN C 2 16  ? 33.16800  -25.71500 -3.97200  1.000 71.17000  ? 580  ASN C CA  1 
ATOM   8001  C C   . ASN C 2 16  ? 33.05800  -24.36600 -4.67200  1.000 64.31000  ? 580  ASN C C   1 
ATOM   8002  O O   . ASN C 2 16  ? 32.84700  -24.26300 -5.88500  1.000 60.35000  ? 580  ASN C O   1 
ATOM   8003  C CB  . ASN C 2 16  ? 34.62500  -25.92000 -3.58400  1.000 63.78000  ? 580  ASN C CB  1 
ATOM   8004  C CG  . ASN C 2 16  ? 35.40000  -26.60100 -4.67100  1.000 77.15000  ? 580  ASN C CG  1 
ATOM   8005  O OD1 . ASN C 2 16  ? 34.88500  -27.53700 -5.29600  1.000 80.91000  ? 580  ASN C OD1 1 
ATOM   8006  N ND2 . ASN C 2 16  ? 36.51600  -25.99800 -5.07100  1.000 77.57000  ? 580  ASN C ND2 1 
ATOM   8007  N N   . GLY C 2 17  ? 33.23500  -23.32300 -3.88400  1.000 61.06000  ? 581  GLY C N   1 
ATOM   8008  C CA  . GLY C 2 17  ? 33.09600  -21.97100 -4.36700  1.000 57.49000  ? 581  GLY C CA  1 
ATOM   8009  C C   . GLY C 2 17  ? 31.79200  -21.34900 -3.91000  1.000 59.41000  ? 581  GLY C C   1 
ATOM   8010  O O   . GLY C 2 17  ? 30.80800  -22.02900 -3.61000  1.000 65.20000  ? 581  GLY C O   1 
ATOM   8011  N N   . GLU C 2 18  ? 31.80000  -20.02700 -3.85900  1.000 58.08000  ? 582  GLU C N   1 
ATOM   8012  C CA  . GLU C 2 18  ? 30.68800  -19.24900 -3.34100  1.000 57.23000  ? 582  GLU C CA  1 
ATOM   8013  C C   . GLU C 2 18  ? 29.83800  -18.75200 -4.49800  1.000 51.87000  ? 582  GLU C C   1 
ATOM   8014  O O   . GLU C 2 18  ? 30.36700  -18.17000 -5.45200  1.000 51.72000  ? 582  GLU C O   1 
ATOM   8015  C CB  . GLU C 2 18  ? 31.22600  -18.07800 -2.52500  1.000 51.04000  ? 582  GLU C CB  1 
ATOM   8016  C CG  . GLU C 2 18  ? 32.01500  -18.55500 -1.34000  1.000 54.78000  ? 582  GLU C CG  1 
ATOM   8017  C CD  . GLU C 2 18  ? 32.63200  -17.42700 -0.56000  1.000 63.70000  ? 582  GLU C CD  1 
ATOM   8018  O OE1 . GLU C 2 18  ? 32.56200  -16.27000 -1.02800  1.000 59.38000  ? 582  GLU C OE1 1 
ATOM   8019  O OE2 . GLU C 2 18  ? 33.18800  -17.70100 0.52300   1.000 73.17000  ? 582  GLU C OE2 1 
ATOM   8020  N N   . TYR C 2 19  ? 28.52900  -18.99000 -4.42900  1.000 47.75000  ? 583  TYR C N   1 
ATOM   8021  C CA  . TYR C 2 19  ? 27.63900  -18.51100 -5.47900  1.000 46.76000  ? 583  TYR C CA  1 
ATOM   8022  C C   . TYR C 2 19  ? 26.73400  -17.44600 -4.87500  1.000 48.90000  ? 583  TYR C C   1 
ATOM   8023  O O   . TYR C 2 19  ? 25.86300  -17.74300 -4.05000  1.000 49.54000  ? 583  TYR C O   1 
ATOM   8024  C CB  . TYR C 2 19  ? 26.83200  -19.61600 -6.17000  1.000 45.11000  ? 583  TYR C CB  1 
ATOM   8025  C CG  . TYR C 2 19  ? 27.66500  -20.74000 -6.76600  1.000 46.89000  ? 583  TYR C CG  1 
ATOM   8026  C CD1 . TYR C 2 19  ? 28.65600  -21.37600 -6.03600  1.000 51.29000  ? 583  TYR C CD1 1 
ATOM   8027  C CD2 . TYR C 2 19  ? 27.65100  -20.95300 -8.13900  1.000 50.70000  ? 583  TYR C CD2 1 
ATOM   8028  C CE1 . TYR C 2 19  ? 29.45200  -22.35300 -6.60300  1.000 52.78000  ? 583  TYR C CE1 1 
ATOM   8029  C CE2 . TYR C 2 19  ? 28.46600  -21.90000 -8.73100  1.000 50.66000  ? 583  TYR C CE2 1 
ATOM   8030  C CZ  . TYR C 2 19  ? 29.36900  -22.59800 -7.95600  1.000 53.01000  ? 583  TYR C CZ  1 
ATOM   8031  O OH  . TYR C 2 19  ? 30.18000  -23.54200 -8.54600  1.000 56.14000  ? 583  TYR C OH  1 
ATOM   8032  N N   . TRP C 2 20  ? 26.96600  -16.20800 -5.28700  1.000 49.45000  ? 584  TRP C N   1 
ATOM   8033  C CA  . TRP C 2 20  ? 26.29400  -15.03100 -4.76500  1.000 52.87000  ? 584  TRP C CA  1 
ATOM   8034  C C   . TRP C 2 20  ? 25.10000  -14.64600 -5.63200  1.000 51.13000  ? 584  TRP C C   1 
ATOM   8035  O O   . TRP C 2 20  ? 25.03500  -14.97200 -6.82100  1.000 49.87000  ? 584  TRP C O   1 
ATOM   8036  C CB  . TRP C 2 20  ? 27.29100  -13.87200 -4.68500  1.000 53.34000  ? 584  TRP C CB  1 
ATOM   8037  C CG  . TRP C 2 20  ? 28.27900  -14.06000 -3.58400  1.000 57.35000  ? 584  TRP C CG  1 
ATOM   8038  C CD1 . TRP C 2 20  ? 29.47400  -14.72500 -3.64700  1.000 54.09000  ? 584  TRP C CD1 1 
ATOM   8039  C CD2 . TRP C 2 20  ? 28.17500  -13.54500 -2.25500  1.000 56.62000  ? 584  TRP C CD2 1 
ATOM   8040  N NE1 . TRP C 2 20  ? 30.10500  -14.67300 -2.42800  1.000 55.51000  ? 584  TRP C NE1 1 
ATOM   8041  C CE2 . TRP C 2 20  ? 29.33000  -13.95100 -1.55800  1.000 57.87000  ? 584  TRP C CE2 1 
ATOM   8042  C CE3 . TRP C 2 20  ? 27.21400  -12.78400 -1.58400  1.000 57.25000  ? 584  TRP C CE3 1 
ATOM   8043  C CZ2 . TRP C 2 20  ? 29.54800  -13.62200 -0.22300  1.000 48.99000  ? 584  TRP C CZ2 1 
ATOM   8044  C CZ3 . TRP C 2 20  ? 27.43100  -12.46000 -0.26400  1.000 58.76000  ? 584  TRP C CZ3 1 
ATOM   8045  C CH2 . TRP C 2 20  ? 28.58900  -12.87800 0.40400   1.000 57.00000  ? 584  TRP C CH2 1 
ATOM   8046  N N   . SER C 2 21  ? 24.15200  -13.94300 -5.01900  1.000 52.28000  ? 585  SER C N   1 
ATOM   8047  C CA  . SER C 2 21  ? 22.94100  -13.54100 -5.71700  1.000 55.11000  ? 585  SER C CA  1 
ATOM   8048  C C   . SER C 2 21  ? 23.27400  -12.53400 -6.81300  1.000 55.52000  ? 585  SER C C   1 
ATOM   8049  O O   . SER C 2 21  ? 24.37500  -11.98000 -6.87300  1.000 52.46000  ? 585  SER C O   1 
ATOM   8050  C CB  . SER C 2 21  ? 21.93000  -12.93700 -4.74700  1.000 53.34000  ? 585  SER C CB  1 
ATOM   8051  O OG  . SER C 2 21  ? 22.38000  -11.67500 -4.29400  1.000 56.37000  ? 585  SER C OG  1 
ATOM   8052  N N   . ALA C 2 22  ? 22.29300  -12.29800 -7.68800  1.000 54.69000  ? 586  ALA C N   1 
ATOM   8053  C CA  . ALA C 2 22  ? 22.50400  -11.39300 -8.81400  1.000 56.48000  ? 586  ALA C CA  1 
ATOM   8054  C C   . ALA C 2 22  ? 22.97200  -10.02000 -8.34900  1.000 60.86000  ? 586  ALA C C   1 
ATOM   8055  O O   . ALA C 2 22  ? 23.85700  -9.41900  -8.96500  1.000 70.48000  ? 586  ALA C O   1 
ATOM   8056  C CB  . ALA C 2 22  ? 21.22100  -11.27200 -9.63800  1.000 57.57000  ? 586  ALA C CB  1 
ATOM   8057  N N   . ALA C 2 23  ? 22.40700  -9.51700  -7.25000  1.000 62.01000  ? 587  ALA C N   1 
ATOM   8058  C CA  . ALA C 2 23  ? 22.83600  -8.22400  -6.72800  1.000 64.22000  ? 587  ALA C CA  1 
ATOM   8059  C C   . ALA C 2 23  ? 24.21000  -8.28700  -6.07000  1.000 72.60000  ? 587  ALA C C   1 
ATOM   8060  O O   . ALA C 2 23  ? 24.88500  -7.25500  -5.97200  1.000 75.02000  ? 587  ALA C O   1 
ATOM   8061  C CB  . ALA C 2 23  ? 21.80800  -7.68800  -5.73300  1.000 68.22000  ? 587  ALA C CB  1 
ATOM   8062  N N   . GLY C 2 24  ? 24.64200  -9.46700  -5.62300  1.000 71.17000  ? 588  GLY C N   1 
ATOM   8063  C CA  . GLY C 2 24  ? 25.93600  -9.63000  -4.98900  1.000 68.18000  ? 588  GLY C CA  1 
ATOM   8064  C C   . GLY C 2 24  ? 25.93300  -9.56700  -3.47600  1.000 68.44000  ? 588  GLY C C   1 
ATOM   8065  O O   . GLY C 2 24  ? 27.00100  -9.71000  -2.86600  1.000 67.05000  ? 588  GLY C O   1 
ATOM   8066  N N   . ASP C 2 25  ? 24.77200  -9.36600  -2.85200  1.000 65.60000  ? 589  ASP C N   1 
ATOM   8067  C CA  . ASP C 2 25  ? 24.69000  -9.20300  -1.40600  1.000 64.94000  ? 589  ASP C CA  1 
ATOM   8068  C C   . ASP C 2 25  ? 24.42600  -10.50200 -0.64700  1.000 67.46000  ? 589  ASP C C   1 
ATOM   8069  O O   . ASP C 2 25  ? 24.93000  -10.65900 0.47300   1.000 69.16000  ? 589  ASP C O   1 
ATOM   8070  C CB  . ASP C 2 25  ? 23.61200  -8.16300  -1.07300  1.000 61.74000  ? 589  ASP C CB  1 
ATOM   8071  C CG  . ASP C 2 25  ? 22.33900  -8.37000  -1.87100  1.000 69.26000  ? 589  ASP C CG  1 
ATOM   8072  O OD1 . ASP C 2 25  ? 22.36000  -9.19800  -2.81000  1.000 74.08000  ? 589  ASP C OD1 1 
ATOM   8073  O OD2 . ASP C 2 25  ? 21.31300  -7.72300  -1.56200  1.000 68.71000  ? 589  ASP C OD2 1 
ATOM   8074  N N   . ILE C 2 26  ? 23.66400  -11.44000 -1.21500  1.000 62.58000  ? 590  ILE C N   1 
ATOM   8075  C CA  . ILE C 2 26  ? 23.28200  -12.67000 -0.52200  1.000 61.23000  ? 590  ILE C CA  1 
ATOM   8076  C C   . ILE C 2 26  ? 24.13800  -13.82000 -1.02900  1.000 58.77000  ? 590  ILE C C   1 
ATOM   8077  O O   . ILE C 2 26  ? 24.36900  -13.95200 -2.23900  1.000 56.45000  ? 590  ILE C O   1 
ATOM   8078  C CB  . ILE C 2 26  ? 21.78500  -13.00000 -0.70400  1.000 57.14000  ? 590  ILE C CB  1 
ATOM   8079  C CG1 . ILE C 2 26  ? 20.88800  -11.94200 -0.06000  1.000 57.31000  ? 590  ILE C CG1 1 
ATOM   8080  C CG2 . ILE C 2 26  ? 21.46500  -14.37600 -0.13800  1.000 58.97000  ? 590  ILE C CG2 1 
ATOM   8081  C CD1 . ILE C 2 26  ? 20.39300  -10.90100 -1.02400  1.000 60.18000  ? 590  ILE C CD1 1 
ATOM   8082  N N   . LEU C 2 27  ? 24.61300  -14.65600 -0.10700  1.000 55.06000  ? 591  LEU C N   1 
ATOM   8083  C CA  . LEU C 2 27  ? 25.27800  -15.89900 -0.47500  1.000 52.25000  ? 591  LEU C CA  1 
ATOM   8084  C C   . LEU C 2 27  ? 24.20600  -16.96900 -0.64500  1.000 59.37000  ? 591  LEU C C   1 
ATOM   8085  O O   . LEU C 2 27  ? 23.58300  -17.39700 0.33300   1.000 58.82000  ? 591  LEU C O   1 
ATOM   8086  C CB  . LEU C 2 27  ? 26.30300  -16.31700 0.57100   1.000 47.66000  ? 591  LEU C CB  1 
ATOM   8087  C CG  . LEU C 2 27  ? 27.15600  -17.51100 0.12200   1.000 58.55000  ? 591  LEU C CG  1 
ATOM   8088  C CD1 . LEU C 2 27  ? 28.04100  -17.13100 -1.07300  1.000 52.24000  ? 591  LEU C CD1 1 
ATOM   8089  C CD2 . LEU C 2 27  ? 27.98900  -18.08600 1.25800   1.000 51.35000  ? 591  LEU C CD2 1 
ATOM   8090  N N   . LEU C 2 28  ? 23.98200  -17.39500 -1.88600  1.000 59.76000  ? 592  LEU C N   1 
ATOM   8091  C CA  . LEU C 2 28  ? 22.96700  -18.41300 -2.12600  1.000 55.07000  ? 592  LEU C CA  1 
ATOM   8092  C C   . LEU C 2 28  ? 23.39600  -19.75800 -1.55200  1.000 52.30000  ? 592  LEU C C   1 
ATOM   8093  O O   . LEU C 2 28  ? 22.64500  -20.39800 -0.80700  1.000 61.86000  ? 592  LEU C O   1 
ATOM   8094  C CB  . LEU C 2 28  ? 22.68500  -18.51500 -3.62300  1.000 52.52000  ? 592  LEU C CB  1 
ATOM   8095  C CG  . LEU C 2 28  ? 22.04300  -17.25100 -4.20300  1.000 59.17000  ? 592  LEU C CG  1 
ATOM   8096  C CD1 . LEU C 2 28  ? 21.95900  -17.34500 -5.71500  1.000 56.87000  ? 592  LEU C CD1 1 
ATOM   8097  C CD2 . LEU C 2 28  ? 20.66200  -17.02100 -3.60000  1.000 53.52000  ? 592  LEU C CD2 1 
ATOM   8098  N N   . PHE C 2 29  ? 24.61600  -20.18100 -1.85000  1.000 54.30000  ? 593  PHE C N   1 
ATOM   8099  C CA  . PHE C 2 29  ? 25.11500  -21.46500 -1.38400  1.000 61.37000  ? 593  PHE C CA  1 
ATOM   8100  C C   . PHE C 2 29  ? 26.61600  -21.50900 -1.61600  1.000 60.09000  ? 593  PHE C C   1 
ATOM   8101  O O   . PHE C 2 29  ? 27.13800  -20.81800 -2.49800  1.000 54.06000  ? 593  PHE C O   1 
ATOM   8102  C CB  . PHE C 2 29  ? 24.41700  -22.62800 -2.09400  1.000 50.77000  ? 593  PHE C CB  1 
ATOM   8103  C CG  . PHE C 2 29  ? 24.50400  -22.55700 -3.58700  1.000 50.35000  ? 593  PHE C CG  1 
ATOM   8104  C CD1 . PHE C 2 29  ? 23.55600  -21.85000 -4.30800  1.000 51.59000  ? 593  PHE C CD1 1 
ATOM   8105  C CD2 . PHE C 2 29  ? 25.52500  -23.19500 -4.27300  1.000 53.80000  ? 593  PHE C CD2 1 
ATOM   8106  C CE1 . PHE C 2 29  ? 23.62500  -21.76900 -5.68400  1.000 48.37000  ? 593  PHE C CE1 1 
ATOM   8107  C CE2 . PHE C 2 29  ? 25.60100  -23.12400 -5.65600  1.000 54.58000  ? 593  PHE C CE2 1 
ATOM   8108  C CZ  . PHE C 2 29  ? 24.64500  -22.41200 -6.36300  1.000 50.74000  ? 593  PHE C CZ  1 
ATOM   8109  N N   . ALA C 2 30  ? 27.29900  -22.31900 -0.81200  1.000 61.36000  ? 594  ALA C N   1 
ATOM   8110  C CA  . ALA C 2 30  ? 28.74900  -22.41700 -0.88100  1.000 57.41000  ? 594  ALA C CA  1 
ATOM   8111  C C   . ALA C 2 30  ? 29.17500  -23.75800 -0.30400  1.000 60.19000  ? 594  ALA C C   1 
ATOM   8112  O O   . ALA C 2 30  ? 28.35800  -24.50600 0.24200   1.000 59.89000  ? 594  ALA C O   1 
ATOM   8113  C CB  . ALA C 2 30  ? 29.41600  -21.26000 -0.13300  1.000 53.20000  ? 594  ALA C CB  1 
ATOM   8114  N N   . ALA C 2 31  ? 30.47000  -24.05900 -0.45500  1.000 60.42000  ? 595  ALA C N   1 
ATOM   8115  C CA  . ALA C 2 31  ? 31.11300  -25.18500 0.22500   1.000 57.35000  ? 595  ALA C CA  1 
ATOM   8116  C C   . ALA C 2 31  ? 30.34900  -26.49100 0.01100   1.000 55.83000  ? 595  ALA C C   1 
ATOM   8117  O O   . ALA C 2 31  ? 30.18600  -27.30300 0.92300   1.000 60.19000  ? 595  ALA C O   1 
ATOM   8118  C CB  . ALA C 2 31  ? 31.28200  -24.89200 1.72000   1.000 55.25000  ? 595  ALA C CB  1 
ATOM   8119  N N   . GLY C 2 32  ? 29.86300  -26.69500 -1.20600  1.000 59.20000  ? 596  GLY C N   1 
ATOM   8120  C CA  . GLY C 2 32  ? 29.17100  -27.92800 -1.51600  1.000 56.95000  ? 596  GLY C CA  1 
ATOM   8121  C C   . GLY C 2 32  ? 27.79000  -28.09400 -0.91800  1.000 60.43000  ? 596  GLY C C   1 
ATOM   8122  O O   . GLY C 2 32  ? 27.30300  -29.22600 -0.84800  1.000 67.37000  ? 596  GLY C O   1 
ATOM   8123  N N   . LYS C 2 33  ? 27.13900  -27.01200 -0.47700  1.000 52.45000  ? 597  LYS C N   1 
ATOM   8124  C CA  . LYS C 2 33  ? 25.70800  -27.09000 -0.18800  1.000 55.68000  ? 597  LYS C CA  1 
ATOM   8125  C C   . LYS C 2 33  ? 24.93900  -27.48200 -1.44300  1.000 57.20000  ? 597  LYS C C   1 
ATOM   8126  O O   . LYS C 2 33  ? 25.14600  -26.90500 -2.51500  1.000 51.42000  ? 597  LYS C O   1 
ATOM   8127  C CB  . LYS C 2 33  ? 25.16500  -25.75900 0.34600   1.000 55.72000  ? 597  LYS C CB  1 
ATOM   8128  C CG  . LYS C 2 33  ? 25.37600  -25.50600 1.83000   1.000 65.47000  ? 597  LYS C CG  1 
ATOM   8129  C CD  . LYS C 2 33  ? 24.58900  -24.27200 2.28800   1.000 62.60000  ? 597  LYS C CD  1 
ATOM   8130  C CE  . LYS C 2 33  ? 25.29800  -22.98500 1.87300   1.000 70.44000  ? 597  LYS C CE  1 
ATOM   8131  N NZ  . LYS C 2 33  ? 24.62000  -21.75000 2.37200   1.000 57.89000  ? 597  LYS C NZ  1 
ATOM   8132  N N   . THR C 2 34  ? 24.04000  -28.46300 -1.30400  1.000 54.77000  ? 598  THR C N   1 
ATOM   8133  C CA  . THR C 2 34  ? 23.21300  -28.90600 -2.41700  1.000 54.28000  ? 598  THR C CA  1 
ATOM   8134  C C   . THR C 2 34  ? 21.72600  -28.69500 -2.17400  1.000 57.49000  ? 598  THR C C   1 
ATOM   8135  O O   . THR C 2 34  ? 20.92000  -29.01000 -3.05900  1.000 55.45000  ? 598  THR C O   1 
ATOM   8136  C CB  . THR C 2 34  ? 23.45400  -30.38900 -2.71800  1.000 59.11000  ? 598  THR C CB  1 
ATOM   8137  O OG1 . THR C 2 34  ? 22.86100  -31.18300 -1.69100  1.000 63.99000  ? 598  THR C OG1 1 
ATOM   8138  C CG2 . THR C 2 34  ? 24.94400  -30.68800 -2.74700  1.000 63.55000  ? 598  THR C CG2 1 
ATOM   8139  N N   . LYS C 2 35  ? 21.33400  -28.19400 -1.00400  1.000 59.30000  ? 599  LYS C N   1 
ATOM   8140  C CA  . LYS C 2 35  ? 19.93000  -28.00700 -0.65100  1.000 45.55000  ? 599  LYS C CA  1 
ATOM   8141  C C   . LYS C 2 35  ? 19.71100  -26.56300 -0.22800  1.000 48.33000  ? 599  LYS C C   1 
ATOM   8142  O O   . LYS C 2 35  ? 20.26700  -26.12100 0.78300   1.000 50.72000  ? 599  LYS C O   1 
ATOM   8143  C CB  . LYS C 2 35  ? 19.52100  -28.95400 0.47500   1.000 49.94000  ? 599  LYS C CB  1 
ATOM   8144  C CG  . LYS C 2 35  ? 18.06800  -28.83400 0.89000   1.000 53.57000  ? 599  LYS C CG  1 
ATOM   8145  C CD  . LYS C 2 35  ? 17.78300  -29.75500 2.05100   1.000 52.27000  ? 599  LYS C CD  1 
ATOM   8146  C CE  . LYS C 2 35  ? 16.36800  -29.61300 2.54500   1.000 54.70000  ? 599  LYS C CE  1 
ATOM   8147  N NZ  . LYS C 2 35  ? 16.18200  -30.48400 3.73900   1.000 66.87000  ? 599  LYS C NZ  1 
ATOM   8148  N N   . LEU C 2 36  ? 18.90000  -25.83700 -0.99000  1.000 52.17000  ? 600  LEU C N   1 
ATOM   8149  C CA  . LEU C 2 36  ? 18.56100  -24.46800 -0.63700  1.000 50.70000  ? 600  LEU C CA  1 
ATOM   8150  C C   . LEU C 2 36  ? 17.27900  -24.41800 0.18300   1.000 49.56000  ? 600  LEU C C   1 
ATOM   8151  O O   . LEU C 2 36  ? 16.38200  -25.25200 0.02800   1.000 47.10000  ? 600  LEU C O   1 
ATOM   8152  C CB  . LEU C 2 36  ? 18.36700  -23.60000 -1.87500  1.000 49.95000  ? 600  LEU C CB  1 
ATOM   8153  C CG  . LEU C 2 36  ? 19.52900  -23.40400 -2.82000  1.000 44.05000  ? 600  LEU C CG  1 
ATOM   8154  C CD1 . LEU C 2 36  ? 19.08400  -22.46800 -3.94700  1.000 51.54000  ? 600  LEU C CD1 1 
ATOM   8155  C CD2 . LEU C 2 36  ? 20.71600  -22.86700 -2.05800  1.000 55.96000  ? 600  LEU C CD2 1 
ATOM   8156  N N   . SER C 2 37  ? 17.19400  -23.40600 1.03700   1.000 51.89000  ? 601  SER C N   1 
ATOM   8157  C CA  . SER C 2 37  ? 15.99200  -23.14100 1.79700   1.000 54.49000  ? 601  SER C CA  1 
ATOM   8158  C C   . SER C 2 37  ? 14.95600  -22.49500 0.88000   1.000 49.59000  ? 601  SER C C   1 
ATOM   8159  O O   . SER C 2 37  ? 15.27300  -22.08000 -0.23400  1.000 50.44000  ? 601  SER C O   1 
ATOM   8160  C CB  . SER C 2 37  ? 16.31400  -22.24200 2.99100   1.000 50.04000  ? 601  SER C CB  1 
ATOM   8161  O OG  . SER C 2 37  ? 16.68300  -20.94400 2.56000   1.000 54.98000  ? 601  SER C OG  1 
ATOM   8162  N N   . PRO C 2 38  ? 13.69400  -22.42300 1.31600   1.000 50.35000  ? 602  PRO C N   1 
ATOM   8163  C CA  . PRO C 2 38  ? 12.70100  -21.65600 0.54500   1.000 53.94000  ? 602  PRO C CA  1 
ATOM   8164  C C   . PRO C 2 38  ? 13.12100  -20.21900 0.30900   1.000 54.48000  ? 602  PRO C C   1 
ATOM   8165  O O   . PRO C 2 38  ? 12.86300  -19.65500 -0.76200  1.000 56.73000  ? 602  PRO C O   1 
ATOM   8166  C CB  . PRO C 2 38  ? 11.43900  -21.76300 1.41700   1.000 44.93000  ? 602  PRO C CB  1 
ATOM   8167  C CG  . PRO C 2 38  ? 11.61300  -23.04300 2.14400   1.000 44.50000  ? 602  PRO C CG  1 
ATOM   8168  C CD  . PRO C 2 38  ? 13.07600  -23.14100 2.44600   1.000 47.20000  ? 602  PRO C CD  1 
ATOM   8169  N N   . TYR C 2 39  ? 13.79500  -19.61400 1.27900   1.000 55.64000  ? 603  TYR C N   1 
ATOM   8170  C CA  . TYR C 2 39  ? 14.24800  -18.23900 1.11100   1.000 54.86000  ? 603  TYR C CA  1 
ATOM   8171  C C   . TYR C 2 39  ? 15.28300  -18.09800 -0.01900  1.000 58.01000  ? 603  TYR C C   1 
ATOM   8172  O O   . TYR C 2 39  ? 15.14800  -17.21300 -0.86600  1.000 56.15000  ? 603  TYR C O   1 
ATOM   8173  C CB  . TYR C 2 39  ? 14.75800  -17.71200 2.46300   1.000 69.94000  ? 603  TYR C CB  1 
ATOM   8174  C CG  . TYR C 2 39  ? 15.36700  -16.31900 2.43700   1.000 75.10000  ? 603  TYR C CG  1 
ATOM   8175  C CD1 . TYR C 2 39  ? 14.58000  -15.16500 2.33500   1.000 71.42000  ? 603  TYR C CD1 1 
ATOM   8176  C CD2 . TYR C 2 39  ? 16.74200  -16.16500 2.52000   1.000 69.90000  ? 603  TYR C CD2 1 
ATOM   8177  C CE1 . TYR C 2 39  ? 15.16500  -13.90000 2.30800   1.000 67.57000  ? 603  TYR C CE1 1 
ATOM   8178  C CE2 . TYR C 2 39  ? 17.32800  -14.92200 2.49500   1.000 78.06000  ? 603  TYR C CE2 1 
ATOM   8179  C CZ  . TYR C 2 39  ? 16.53900  -13.79100 2.39500   1.000 82.19000  ? 603  TYR C CZ  1 
ATOM   8180  O OH  . TYR C 2 39  ? 17.12700  -12.54600 2.36100   1.000 96.22000  ? 603  TYR C OH  1 
ATOM   8181  N N   . MET C 2 40  ? 16.31400  -18.94700 -0.08000  1.000 53.39000  ? 604  MET C N   1 
ATOM   8182  C CA  . MET C 2 40  ? 17.24400  -18.79300 -1.20500  1.000 53.65000  ? 604  MET C CA  1 
ATOM   8183  C C   . MET C 2 40  ? 16.55800  -19.06900 -2.52200  1.000 55.21000  ? 604  MET C C   1 
ATOM   8184  O O   . MET C 2 40  ? 16.78700  -18.36700 -3.51600  1.000 57.29000  ? 604  MET C O   1 
ATOM   8185  C CB  . MET C 2 40  ? 18.42200  -19.73800 -1.09900  1.000 57.76000  ? 604  MET C CB  1 
ATOM   8186  C CG  . MET C 2 40  ? 19.19300  -19.56900 0.09600   1.000 68.07000  ? 604  MET C CG  1 
ATOM   8187  S SD  . MET C 2 40  ? 19.68400  -17.86100 0.08100   1.000 69.24000  ? 604  MET C SD  1 
ATOM   8188  C CE  . MET C 2 40  ? 20.56400  -17.80400 1.65500   1.000 68.73000  ? 604  MET C CE  1 
ATOM   8189  N N   . THR C 2 41  ? 15.72900  -20.10900 -2.54500  1.000 53.52000  ? 605  THR C N   1 
ATOM   8190  C CA  . THR C 2 41  ? 15.08000  -20.47700 -3.78800  1.000 51.48000  ? 605  THR C CA  1 
ATOM   8191  C C   . THR C 2 41  ? 14.42100  -19.25600 -4.39700  1.000 51.07000  ? 605  THR C C   1 
ATOM   8192  O O   . THR C 2 41  ? 14.70300  -18.89400 -5.54300  1.000 54.33000  ? 605  THR C O   1 
ATOM   8193  C CB  . THR C 2 41  ? 14.07700  -21.61000 -3.55200  1.000 54.30000  ? 605  THR C CB  1 
ATOM   8194  O OG1 . THR C 2 41  ? 14.78700  -22.80300 -3.18400  1.000 50.45000  ? 605  THR C OG1 1 
ATOM   8195  C CG2 . THR C 2 41  ? 13.25500  -21.85700 -4.81200  1.000 43.01000  ? 605  THR C CG2 1 
ATOM   8196  N N   . VAL C 2 42  ? 13.66300  -18.52600 -3.58000  1.000 47.45000  ? 606  VAL C N   1 
ATOM   8197  C CA  . VAL C 2 42  ? 12.93100  -17.35900 -4.04800  1.000 50.36000  ? 606  VAL C CA  1 
ATOM   8198  C C   . VAL C 2 42  ? 13.88100  -16.25300 -4.49000  1.000 46.91000  ? 606  VAL C C   1 
ATOM   8199  O O   . VAL C 2 42  ? 13.56700  -15.48600 -5.40700  1.000 48.21000  ? 606  VAL C O   1 
ATOM   8200  C CB  . VAL C 2 42  ? 11.96100  -16.90400 -2.94000  1.000 46.75000  ? 606  VAL C CB  1 
ATOM   8201  C CG1 . VAL C 2 42  ? 11.31700  -15.58100 -3.28900  1.000 52.66000  ? 606  VAL C CG1 1 
ATOM   8202  C CG2 . VAL C 2 42  ? 10.89000  -17.96600 -2.73900  1.000 45.17000  ? 606  VAL C CG2 1 
ATOM   8203  N N   . ILE C 2 43  ? 15.04600  -16.14100 -3.85900  1.000 48.99000  ? 607  ILE C N   1 
ATOM   8204  C CA  . ILE C 2 43  ? 15.98900  -15.10700 -4.26500  1.000 50.52000  ? 607  ILE C CA  1 
ATOM   8205  C C   . ILE C 2 43  ? 16.69000  -15.47700 -5.55500  1.000 52.83000  ? 607  ILE C C   1 
ATOM   8206  O O   . ILE C 2 43  ? 16.84200  -14.64300 -6.45400  1.000 55.79000  ? 607  ILE C O   1 
ATOM   8207  C CB  . ILE C 2 43  ? 16.98100  -14.83500 -3.12800  1.000 53.94000  ? 607  ILE C CB  1 
ATOM   8208  C CG1 . ILE C 2 43  ? 16.27700  -14.00300 -2.07300  1.000 56.53000  ? 607  ILE C CG1 1 
ATOM   8209  C CG2 . ILE C 2 43  ? 18.26300  -14.18600 -3.64700  1.000 53.31000  ? 607  ILE C CG2 1 
ATOM   8210  C CD1 . ILE C 2 43  ? 16.99900  -13.98000 -0.80100  1.000 68.63000  ? 607  ILE C CD1 1 
ATOM   8211  N N   . SER C 2 44  ? 17.13800  -16.72000 -5.67800  1.000 50.70000  ? 608  SER C N   1 
ATOM   8212  C CA  . SER C 2 44  ? 17.81200  -17.10600 -6.90800  1.000 51.74000  ? 608  SER C CA  1 
ATOM   8213  C C   . SER C 2 44  ? 16.85400  -17.06100 -8.09600  1.000 53.10000  ? 608  SER C C   1 
ATOM   8214  O O   . SER C 2 44  ? 17.23800  -16.63400 -9.19200  1.000 51.02000  ? 608  SER C O   1 
ATOM   8215  C CB  . SER C 2 44  ? 18.46100  -18.48100 -6.73600  1.000 49.34000  ? 608  SER C CB  1 
ATOM   8216  O OG  . SER C 2 44  ? 17.52000  -19.48900 -6.44400  1.000 50.55000  ? 608  SER C OG  1 
ATOM   8217  N N   . LEU C 2 45  ? 15.59100  -17.46300 -7.89300  1.000 53.83000  ? 609  LEU C N   1 
ATOM   8218  C CA  . LEU C 2 45  ? 14.63500  -17.48800 -8.99900  1.000 51.08000  ? 609  LEU C CA  1 
ATOM   8219  C C   . LEU C 2 45  ? 14.06900  -16.10900 -9.31700  1.000 46.88000  ? 609  LEU C C   1 
ATOM   8220  O O   . LEU C 2 45  ? 13.69500  -15.84900 -10.46400 1.000 48.40000  ? 609  LEU C O   1 
ATOM   8221  C CB  . LEU C 2 45  ? 13.49900  -18.45900 -8.69500  1.000 49.83000  ? 609  LEU C CB  1 
ATOM   8222  C CG  . LEU C 2 45  ? 13.98200  -19.89600 -8.49700  1.000 54.59000  ? 609  LEU C CG  1 
ATOM   8223  C CD1 . LEU C 2 45  ? 12.81900  -20.81400 -8.16100  1.000 46.44000  ? 609  LEU C CD1 1 
ATOM   8224  C CD2 . LEU C 2 45  ? 14.76400  -20.39600 -9.70900  1.000 45.31000  ? 609  LEU C CD2 1 
ATOM   8225  N N   . GLY C 2 46  ? 13.99200  -15.22300 -8.33900  1.000 45.74000  ? 610  GLY C N   1 
ATOM   8226  C CA  . GLY C 2 46  ? 13.55300  -13.85900 -8.61900  1.000 50.47000  ? 610  GLY C CA  1 
ATOM   8227  C C   . GLY C 2 46  ? 12.06600  -13.65800 -8.66300  1.000 52.69000  ? 610  GLY C C   1 
ATOM   8228  O O   . GLY C 2 46  ? 11.54100  -12.77800 -7.97500  1.000 62.45000  ? 610  GLY C O   1 
ATOM   8229  N N   . THR C 2 47  ? 11.36100  -14.45600 -9.45700  1.000 51.55000  ? 611  THR C N   1 
ATOM   8230  C CA  . THR C 2 47  ? 9.91100   -14.39900 -9.51900  1.000 56.86000  ? 611  THR C CA  1 
ATOM   8231  C C   . THR C 2 47  ? 9.31800   -15.75900 -9.18100  1.000 53.28000  ? 611  THR C C   1 
ATOM   8232  O O   . THR C 2 47  ? 9.99200   -16.79100 -9.23400  1.000 52.75000  ? 611  THR C O   1 
ATOM   8233  C CB  . THR C 2 47  ? 9.42600   -13.95900 -10.89700 1.000 52.69000  ? 611  THR C CB  1 
ATOM   8234  O OG1 . THR C 2 47  ? 9.95300   -14.84800 -11.88500 1.000 56.93000  ? 611  THR C OG1 1 
ATOM   8235  C CG2 . THR C 2 47  ? 9.88200   -12.54700 -11.19200 1.000 58.04000  ? 611  THR C CG2 1 
ATOM   8236  N N   . TRP C 2 48  ? 8.04100   -15.74700 -8.81800  1.000 47.24000  ? 612  TRP C N   1 
ATOM   8237  C CA  . TRP C 2 48  ? 7.36600   -16.97900 -8.45500  1.000 51.12000  ? 612  TRP C CA  1 
ATOM   8238  C C   . TRP C 2 48  ? 5.88700   -16.83900 -8.76300  1.000 49.99000  ? 612  TRP C C   1 
ATOM   8239  O O   . TRP C 2 48  ? 5.37200   -15.74000 -8.99400  1.000 51.82000  ? 612  TRP C O   1 
ATOM   8240  C CB  . TRP C 2 48  ? 7.57400   -17.33800 -6.97700  1.000 55.20000  ? 612  TRP C CB  1 
ATOM   8241  C CG  . TRP C 2 48  ? 7.05300   -18.69600 -6.65900  1.000 50.50000  ? 612  TRP C CG  1 
ATOM   8242  C CD1 . TRP C 2 48  ? 5.92900   -19.00700 -5.95100  1.000 57.76000  ? 612  TRP C CD1 1 
ATOM   8243  C CD2 . TRP C 2 48  ? 7.60500   -19.93900 -7.10400  1.000 54.06000  ? 612  TRP C CD2 1 
ATOM   8244  N NE1 . TRP C 2 48  ? 5.76300   -20.37700 -5.90100  1.000 57.48000  ? 612  TRP C NE1 1 
ATOM   8245  C CE2 . TRP C 2 48  ? 6.78100   -20.96800 -6.60300  1.000 55.33000  ? 612  TRP C CE2 1 
ATOM   8246  C CE3 . TRP C 2 48  ? 8.73200   -20.28400 -7.86300  1.000 52.41000  ? 612  TRP C CE3 1 
ATOM   8247  C CZ2 . TRP C 2 48  ? 7.04400   -22.31300 -6.84100  1.000 48.72000  ? 612  TRP C CZ2 1 
ATOM   8248  C CZ3 . TRP C 2 48  ? 8.99500   -21.62200 -8.08900  1.000 49.84000  ? 612  TRP C CZ3 1 
ATOM   8249  C CH2 . TRP C 2 48  ? 8.15500   -22.62000 -7.57900  1.000 47.21000  ? 612  TRP C CH2 1 
ATOM   8250  N N   . MET C 2 49  ? 5.21100   -17.97800 -8.78900  1.000 52.50000  ? 613  MET C N   1 
ATOM   8251  C CA  . MET C 2 49  ? 3.76400   -17.99100 -8.89000  1.000 47.90000  ? 613  MET C CA  1 
ATOM   8252  C C   . MET C 2 49  ? 3.27500   -19.26300 -8.21400  1.000 47.10000  ? 613  MET C C   1 
ATOM   8253  O O   . MET C 2 49  ? 3.84600   -20.33800 -8.41900  1.000 48.26000  ? 613  MET C O   1 
ATOM   8254  C CB  . MET C 2 49  ? 3.34800   -17.91400 -10.36000 1.000 48.73000  ? 613  MET C CB  1 
ATOM   8255  C CG  . MET C 2 49  ? 1.89800   -17.65200 -10.62700 1.000 52.76000  ? 613  MET C CG  1 
ATOM   8256  S SD  . MET C 2 49  ? 1.62100   -17.59300 -12.41400 1.000 59.88000  ? 613  MET C SD  1 
ATOM   8257  C CE  . MET C 2 49  ? 2.38900   -16.05000 -12.85400 1.000 49.82000  ? 613  MET C CE  1 
ATOM   8258  N N   . TYR C 2 50  ? 2.25000   -19.13200 -7.38000  1.000 53.41000  ? 614  TYR C N   1 
ATOM   8259  C CA  . TYR C 2 50  ? 1.65700   -20.28900 -6.72700  1.000 47.28000  ? 614  TYR C CA  1 
ATOM   8260  C C   . TYR C 2 50  ? 0.57900   -20.90800 -7.60300  1.000 48.81000  ? 614  TYR C C   1 
ATOM   8261  O O   . TYR C 2 50  ? -0.15900  -20.19900 -8.29600  1.000 51.03000  ? 614  TYR C O   1 
ATOM   8262  C CB  . TYR C 2 50  ? 1.08900   -19.91400 -5.36200  1.000 49.04000  ? 614  TYR C CB  1 
ATOM   8263  C CG  . TYR C 2 50  ? 2.17900   -19.71600 -4.35400  1.000 52.19000  ? 614  TYR C CG  1 
ATOM   8264  C CD1 . TYR C 2 50  ? 2.89200   -20.81000 -3.87400  1.000 56.58000  ? 614  TYR C CD1 1 
ATOM   8265  C CD2 . TYR C 2 50  ? 2.49700   -18.45700 -3.86800  1.000 50.98000  ? 614  TYR C CD2 1 
ATOM   8266  C CE1 . TYR C 2 50  ? 3.90400   -20.66000 -2.95100  1.000 53.63000  ? 614  TYR C CE1 1 
ATOM   8267  C CE2 . TYR C 2 50  ? 3.50500   -18.29400 -2.93400  1.000 61.08000  ? 614  TYR C CE2 1 
ATOM   8268  C CZ  . TYR C 2 50  ? 4.20800   -19.40300 -2.48000  1.000 65.69000  ? 614  TYR C CZ  1 
ATOM   8269  O OH  . TYR C 2 50  ? 5.22100   -19.25900 -1.55500  1.000 69.89000  ? 614  TYR C OH  1 
ATOM   8270  N N   . GLU C 2 51  ? 0.50400   -22.24500 -7.57300  1.000 43.16000  ? 615  GLU C N   1 
ATOM   8271  C CA  . GLU C 2 51  ? -0.44400  -22.94900 -8.43100  1.000 43.49000  ? 615  GLU C CA  1 
ATOM   8272  C C   . GLU C 2 51  ? -1.86700  -22.44700 -8.21300  1.000 54.03000  ? 615  GLU C C   1 
ATOM   8273  O O   . GLU C 2 51  ? -2.62700  -22.27500 -9.17400  1.000 52.21000  ? 615  GLU C O   1 
ATOM   8274  C CB  . GLU C 2 51  ? -0.41100  -24.45400 -8.18100  1.000 39.14000  ? 615  GLU C CB  1 
ATOM   8275  C CG  . GLU C 2 51  ? 0.86500   -25.20700 -8.48300  1.000 38.33000  ? 615  GLU C CG  1 
ATOM   8276  C CD  . GLU C 2 51  ? 1.76100   -25.32900 -7.26500  1.000 46.41000  ? 615  GLU C CD  1 
ATOM   8277  O OE1 . GLU C 2 51  ? 1.55600   -24.58800 -6.28400  1.000 46.99000  ? 615  GLU C OE1 1 
ATOM   8278  O OE2 . GLU C 2 51  ? 2.59900   -26.25200 -7.24200  1.000 51.38000  ? 615  GLU C OE2 1 
ATOM   8279  N N   . THR C 2 52  ? -2.25200  -22.21600 -6.95500  1.000 49.39000  ? 616  THR C N   1 
ATOM   8280  C CA  . THR C 2 52  ? -3.62600  -21.80400 -6.69600  1.000 53.94000  ? 616  THR C CA  1 
ATOM   8281  C C   . THR C 2 52  ? -3.92100  -20.46100 -7.34700  1.000 55.85000  ? 616  THR C C   1 
ATOM   8282  O O   . THR C 2 52  ? -4.99700  -20.27400 -7.92900  1.000 58.75000  ? 616  THR C O   1 
ATOM   8283  C CB  . THR C 2 52  ? -3.90700  -21.74200 -5.19200  1.000 55.14000  ? 616  THR C CB  1 
ATOM   8284  O OG1 . THR C 2 52  ? -3.07200  -20.74900 -4.58200  1.000 60.76000  ? 616  THR C OG1 1 
ATOM   8285  C CG2 . THR C 2 52  ? -3.64600  -23.09900 -4.54300  1.000 51.98000  ? 616  THR C CG2 1 
ATOM   8286  N N   . ASP C 2 53  ? -2.97300  -19.51700 -7.28500  1.000 50.42000  ? 617  ASP C N   1 
ATOM   8287  C CA  . ASP C 2 53  ? -3.20400  -18.23500 -7.94800  1.000 51.47000  ? 617  ASP C CA  1 
ATOM   8288  C C   . ASP C 2 53  ? -3.23800  -18.40800 -9.46000  1.000 49.90000  ? 617  ASP C C   1 
ATOM   8289  O O   . ASP C 2 53  ? -4.06300  -17.79000 -10.14500 1.000 48.98000  ? 617  ASP C O   1 
ATOM   8290  C CB  . ASP C 2 53  ? -2.14200  -17.20500 -7.55500  1.000 47.17000  ? 617  ASP C CB  1 
ATOM   8291  C CG  . ASP C 2 53  ? -2.13100  -16.90900 -6.07000  1.000 55.79000  ? 617  ASP C CG  1 
ATOM   8292  O OD1 . ASP C 2 53  ? -3.05200  -17.35900 -5.35300  1.000 62.87000  ? 617  ASP C OD1 1 
ATOM   8293  O OD2 . ASP C 2 53  ? -1.24200  -16.14700 -5.63000  1.000 62.05000  ? 617  ASP C OD2 1 
ATOM   8294  N N   . LEU C 2 54  ? -2.35800  -19.25600 -9.99300  1.000 49.52000  ? 618  LEU C N   1 
ATOM   8295  C CA  . LEU C 2 54  ? -2.37700  -19.53000 -11.42200 1.000 45.91000  ? 618  LEU C CA  1 
ATOM   8296  C C   . LEU C 2 54  ? -3.73400  -20.04500 -11.85900 1.000 44.37000  ? 618  LEU C C   1 
ATOM   8297  O O   . LEU C 2 54  ? -4.25500  -19.63200 -12.89700 1.000 47.18000  ? 618  LEU C O   1 
ATOM   8298  C CB  . LEU C 2 54  ? -1.28200  -20.54000 -11.77800 1.000 47.77000  ? 618  LEU C CB  1 
ATOM   8299  C CG  . LEU C 2 54  ? -1.14300  -20.91000 -13.26600 1.000 47.04000  ? 618  LEU C CG  1 
ATOM   8300  C CD1 . LEU C 2 54  ? -0.55100  -19.78300 -14.11100 1.000 44.32000  ? 618  LEU C CD1 1 
ATOM   8301  C CD2 . LEU C 2 54  ? -0.37100  -22.20800 -13.46000 1.000 47.25000  ? 618  LEU C CD2 1 
ATOM   8302  N N   . MET C 2 55  ? -4.33300  -20.94900 -11.08300 1.000 48.57000  ? 619  MET C N   1 
ATOM   8303  C CA  . MET C 2 55  ? -5.61300  -21.52900 -11.48700 1.000 49.15000  ? 619  MET C CA  1 
ATOM   8304  C C   . MET C 2 55  ? -6.71500  -20.49500 -11.49900 1.000 45.16000  ? 619  MET C C   1 
ATOM   8305  O O   . MET C 2 55  ? -7.54000  -20.47500 -12.41300 1.000 50.34000  ? 619  MET C O   1 
ATOM   8306  C CB  . MET C 2 55  ? -5.96200  -22.72400 -10.60000 1.000 46.52000  ? 619  MET C CB  1 
ATOM   8307  C CG  . MET C 2 55  ? -4.96300  -23.87400 -10.76800 1.000 61.96000  ? 619  MET C CG  1 
ATOM   8308  S SD  . MET C 2 55  ? -4.79600  -24.36400 -12.52600 1.000 70.04000  ? 619  MET C SD  1 
ATOM   8309  C CE  . MET C 2 55  ? -3.45800  -25.55700 -12.48400 1.000 55.72000  ? 619  MET C CE  1 
ATOM   8310  N N   . GLN C 2 56  ? -6.74600  -19.59700 -10.51400 1.000 42.47000  ? 620  GLN C N   1 
ATOM   8311  C CA  . GLN C 2 56  ? -7.72600  -18.51300 -10.58100 1.000 43.47000  ? 620  GLN C CA  1 
ATOM   8312  C C   . GLN C 2 56  ? -7.48300  -17.63600 -11.79000 1.000 48.45000  ? 620  GLN C C   1 
ATOM   8313  O O   . GLN C 2 56  ? -8.43000  -17.13700 -12.40100 1.000 53.25000  ? 620  GLN C O   1 
ATOM   8314  C CB  . GLN C 2 56  ? -7.70400  -17.67600 -9.29500  1.000 46.65000  ? 620  GLN C CB  1 
ATOM   8315  C CG  . GLN C 2 56  ? -8.28400  -18.41900 -8.12100  1.000 51.91000  ? 620  GLN C CG  1 
ATOM   8316  C CD  . GLN C 2 56  ? -9.76200  -18.72500 -8.32000  1.000 66.85000  ? 620  GLN C CD  1 
ATOM   8317  O OE1 . GLN C 2 56  ? -10.53500 -17.87500 -8.78100  1.000 66.03000  ? 620  GLN C OE1 1 
ATOM   8318  N NE2 . GLN C 2 56  ? -10.15400 -19.96200 -8.01400  1.000 64.98000  ? 620  GLN C NE2 1 
ATOM   8319  N N   . TRP C 2 57  ? -6.21700  -17.46300 -12.17200 1.000 41.94000  ? 621  TRP C N   1 
ATOM   8320  C CA  . TRP C 2 57  ? -5.90100  -16.70800 -13.36700 1.000 42.64000  ? 621  TRP C CA  1 
ATOM   8321  C C   . TRP C 2 57  ? -6.43800  -17.39700 -14.62000 1.000 45.72000  ? 621  TRP C C   1 
ATOM   8322  O O   . TRP C 2 57  ? -6.95600  -16.72200 -15.52200 1.000 42.13000  ? 621  TRP C O   1 
ATOM   8323  C CB  . TRP C 2 57  ? -4.38900  -16.51000 -13.47700 1.000 43.86000  ? 621  TRP C CB  1 
ATOM   8324  C CG  . TRP C 2 57  ? -3.99200  -15.63800 -14.61600 1.000 37.93000  ? 621  TRP C CG  1 
ATOM   8325  C CD1 . TRP C 2 57  ? -4.01000  -14.27200 -14.65800 1.000 37.16000  ? 621  TRP C CD1 1 
ATOM   8326  C CD2 . TRP C 2 57  ? -3.60200  -16.07700 -15.91600 1.000 39.00000  ? 621  TRP C CD2 1 
ATOM   8327  N NE1 . TRP C 2 57  ? -3.60000  -13.83500 -15.89700 1.000 41.47000  ? 621  TRP C NE1 1 
ATOM   8328  C CE2 . TRP C 2 57  ? -3.35200  -14.92500 -16.69100 1.000 39.20000  ? 621  TRP C CE2 1 
ATOM   8329  C CE3 . TRP C 2 57  ? -3.42700  -17.33800 -16.49800 1.000 40.24000  ? 621  TRP C CE3 1 
ATOM   8330  C CZ2 . TRP C 2 57  ? -2.93500  -14.99700 -18.01800 1.000 37.82000  ? 621  TRP C CZ2 1 
ATOM   8331  C CZ3 . TRP C 2 57  ? -3.01300  -17.41000 -17.81100 1.000 37.28000  ? 621  TRP C CZ3 1 
ATOM   8332  C CH2 . TRP C 2 57  ? -2.76900  -16.24800 -18.56000 1.000 43.32000  ? 621  TRP C CH2 1 
ATOM   8333  N N   . ARG C 2 58  ? -6.30200  -18.73300 -14.72100 1.000 47.62000  ? 622  ARG C N   1 
ATOM   8334  C CA  . ARG C 2 58  ? -6.83500  -19.39500 -15.91300 1.000 46.58000  ? 622  ARG C CA  1 
ATOM   8335  C C   . ARG C 2 58  ? -8.35400  -19.34000 -15.92000 1.000 44.40000  ? 622  ARG C C   1 
ATOM   8336  O O   . ARG C 2 58  ? -8.95300  -19.10900 -16.97700 1.000 43.96000  ? 622  ARG C O   1 
ATOM   8337  C CB  . ARG C 2 58  ? -6.36600  -20.85200 -16.07100 1.000 41.78000  ? 622  ARG C CB  1 
ATOM   8338  C CG  . ARG C 2 58  ? -6.96700  -21.88300 -15.13100 1.000 53.65000  ? 622  ARG C CG  1 
ATOM   8339  C CD  . ARG C 2 58  ? -6.65900  -23.35300 -15.52200 1.000 45.30000  ? 622  ARG C CD  1 
ATOM   8340  N NE  . ARG C 2 58  ? -7.54600  -23.92200 -16.53700 1.000 49.45000  ? 622  ARG C NE  1 
ATOM   8341  C CZ  . ARG C 2 58  ? -8.73700  -24.45600 -16.27700 1.000 51.98000  ? 622  ARG C CZ  1 
ATOM   8342  N NH1 . ARG C 2 58  ? -9.27800  -24.39100 -15.07100 1.000 43.94000  ? 622  ARG C NH1 1 
ATOM   8343  N NH2 . ARG C 2 58  ? -9.40900  -25.06200 -17.25500 1.000 50.98000  ? 622  ARG C NH2 1 
ATOM   8344  N N   . LEU C 2 59  ? -8.99600  -19.52400 -14.75500 1.000 44.64000  ? 623  LEU C N   1 
ATOM   8345  C CA  . LEU C 2 59  ? -10.44900 -19.37300 -14.70700 1.000 49.54000  ? 623  LEU C CA  1 
ATOM   8346  C C   . LEU C 2 59  ? -10.86100 -17.97700 -15.14400 1.000 49.66000  ? 623  LEU C C   1 
ATOM   8347  O O   . LEU C 2 59  ? -11.81400 -17.81700 -15.91500 1.000 46.72000  ? 623  LEU C O   1 
ATOM   8348  C CB  . LEU C 2 59  ? -11.01700 -19.64400 -13.31500 1.000 46.94000  ? 623  LEU C CB  1 
ATOM   8349  C CG  . LEU C 2 59  ? -11.41000 -21.04500 -12.82200 1.000 46.85000  ? 623  LEU C CG  1 
ATOM   8350  C CD1 . LEU C 2 59  ? -12.13300 -21.85900 -13.89400 1.000 50.07000  ? 623  LEU C CD1 1 
ATOM   8351  C CD2 . LEU C 2 59  ? -10.28900 -21.82500 -12.17300 1.000 62.44000  ? 623  LEU C CD2 1 
ATOM   8352  N N   . ALA C 2 60  ? -10.14900 -16.95500 -14.66800 1.000 48.49000  ? 624  ALA C N   1 
ATOM   8353  C CA  . ALA C 2 60  ? -10.44400 -15.59600 -15.10000 1.000 49.46000  ? 624  ALA C CA  1 
ATOM   8354  C C   . ALA C 2 60  ? -10.32100 -15.47200 -16.61100 1.000 46.67000  ? 624  ALA C C   1 
ATOM   8355  O O   . ALA C 2 60  ? -11.21600 -14.94100 -17.27800 1.000 47.87000  ? 624  ALA C O   1 
ATOM   8356  C CB  . ALA C 2 60  ? -9.51200  -14.60800 -14.40200 1.000 42.29000  ? 624  ALA C CB  1 
ATOM   8357  N N   . CYS C 2 61  ? -9.22000  -15.97700 -17.17000 1.000 50.43000  ? 625  CYS C N   1 
ATOM   8358  C CA  . CYS C 2 61  ? -8.98200  -15.84700 -18.60500 1.000 45.05000  ? 625  CYS C CA  1 
ATOM   8359  C C   . CYS C 2 61  ? -9.98200  -16.65500 -19.42000 1.000 44.15000  ? 625  CYS C C   1 
ATOM   8360  O O   . CYS C 2 61  ? -10.48100 -16.17600 -20.44400 1.000 42.83000  ? 625  CYS C O   1 
ATOM   8361  C CB  . CYS C 2 61  ? -7.55800  -16.27800 -18.93200 1.000 41.53000  ? 625  CYS C CB  1 
ATOM   8362  S SG  . CYS C 2 61  ? -6.33600  -15.11800 -18.32200 1.000 43.96000  ? 625  CYS C SG  1 
ATOM   8363  N N   . ILE C 2 62  ? -10.26200 -17.89100 -18.99900 1.000 44.45000  ? 626  ILE C N   1 
ATOM   8364  C CA  . ILE C 2 62  ? -11.21200 -18.72500 -19.73000 1.000 45.65000  ? 626  ILE C CA  1 
ATOM   8365  C C   . ILE C 2 62  ? -12.59900 -18.09800 -19.70500 1.000 51.81000  ? 626  ILE C C   1 
ATOM   8366  O O   . ILE C 2 62  ? -13.25900 -17.97400 -20.74400 1.000 54.30000  ? 626  ILE C O   1 
ATOM   8367  C CB  . ILE C 2 62  ? -11.23000 -20.15200 -19.15800 1.000 42.67000  ? 626  ILE C CB  1 
ATOM   8368  C CG1 . ILE C 2 62  ? -9.92500  -20.87300 -19.48200 1.000 44.75000  ? 626  ILE C CG1 1 
ATOM   8369  C CG2 . ILE C 2 62  ? -12.41200 -20.92600 -19.70300 1.000 45.94000  ? 626  ILE C CG2 1 
ATOM   8370  C CD1 . ILE C 2 62  ? -9.78900  -22.20000 -18.77500 1.000 44.50000  ? 626  ILE C CD1 1 
ATOM   8371  N N   . ASN C 2 63  ? -13.06300 -17.69200 -18.51700 1.000 48.55000  ? 627  ASN C N   1 
ATOM   8372  C CA  . ASN C 2 63  ? -14.38000 -17.06600 -18.42300 1.000 52.76000  ? 627  ASN C CA  1 
ATOM   8373  C C   . ASN C 2 63  ? -14.45300 -15.80300 -19.27200 1.000 53.79000  ? 627  ASN C C   1 
ATOM   8374  O O   . ASN C 2 63  ? -15.45200 -15.57200 -19.96500 1.000 50.92000  ? 627  ASN C O   1 
ATOM   8375  C CB  . ASN C 2 63  ? -14.73300 -16.77100 -16.96400 1.000 50.14000  ? 627  ASN C CB  1 
ATOM   8376  C CG  . ASN C 2 63  ? -15.23900 -18.00000 -16.22900 1.000 54.31000  ? 627  ASN C CG  1 
ATOM   8377  O OD1 . ASN C 2 63  ? -16.02700 -18.77800 -16.77400 1.000 55.37000  ? 627  ASN C OD1 1 
ATOM   8378  N ND2 . ASN C 2 63  ? -14.80000 -18.18000 -14.98800 1.000 46.99000  ? 627  ASN C ND2 1 
ATOM   8379  N N   . TYR C 2 64  ? -13.39500 -14.98800 -19.25600 1.000 48.89000  ? 628  TYR C N   1 
ATOM   8380  C CA  . TYR C 2 64  ? -13.36500 -13.82100 -20.13200 1.000 53.71000  ? 628  TYR C CA  1 
ATOM   8381  C C   . TYR C 2 64  ? -13.37400 -14.23300 -21.60000 1.000 54.98000  ? 628  TYR C C   1 
ATOM   8382  O O   . TYR C 2 64  ? -14.07600 -13.63000 -22.42200 1.000 57.09000  ? 628  TYR C O   1 
ATOM   8383  C CB  . TYR C 2 64  ? -12.15200 -12.95500 -19.79900 1.000 52.87000  ? 628  TYR C CB  1 
ATOM   8384  C CG  . TYR C 2 64  ? -12.01300 -11.69600 -20.63300 1.000 57.00000  ? 628  TYR C CG  1 
ATOM   8385  C CD1 . TYR C 2 64  ? -13.03100 -10.75200 -20.67400 1.000 56.74000  ? 628  TYR C CD1 1 
ATOM   8386  C CD2 . TYR C 2 64  ? -10.82200 -11.39400 -21.28100 1.000 63.96000  ? 628  TYR C CD2 1 
ATOM   8387  C CE1 . TYR C 2 64  ? -12.90000 -9.58500  -21.41000 1.000 54.02000  ? 628  TYR C CE1 1 
ATOM   8388  C CE2 . TYR C 2 64  ? -10.67900 -10.22000 -22.01000 1.000 69.33000  ? 628  TYR C CE2 1 
ATOM   8389  C CZ  . TYR C 2 64  ? -11.72600 -9.32100  -22.07000 1.000 61.57000  ? 628  TYR C CZ  1 
ATOM   8390  O OH  . TYR C 2 64  ? -11.59600 -8.15500  -22.79200 1.000 71.52000  ? 628  TYR C OH  1 
ATOM   8391  N N   . SER C 2 65  ? -12.60600 -15.26400 -21.95000 1.000 53.21000  ? 629  SER C N   1 
ATOM   8392  C CA  . SER C 2 65  ? -12.61700 -15.74600 -23.32400 1.000 52.50000  ? 629  SER C CA  1 
ATOM   8393  C C   . SER C 2 65  ? -14.00700 -16.21500 -23.72100 1.000 52.83000  ? 629  SER C C   1 
ATOM   8394  O O   . SER C 2 65  ? -14.46800 -15.93800 -24.83200 1.000 54.38000  ? 629  SER C O   1 
ATOM   8395  C CB  . SER C 2 65  ? -11.60000 -16.87300 -23.49500 1.000 47.30000  ? 629  SER C CB  1 
ATOM   8396  O OG  . SER C 2 65  ? -11.62600 -17.37100 -24.81900 1.000 52.82000  ? 629  SER C OG  1 
ATOM   8397  N N   . ASP C 2 66  ? -14.67900 -16.90000 -22.80600 1.000 48.49000  ? 630  ASP C N   1 
ATOM   8398  C CA  . ASP C 2 66  ? -16.04600 -17.42000 -23.04400 1.000 53.35000  ? 630  ASP C CA  1 
ATOM   8399  C C   . ASP C 2 66  ? -17.04400 -16.26800 -23.20500 1.000 64.14000  ? 630  ASP C C   1 
ATOM   8400  O O   . ASP C 2 66  ? -18.03000 -16.43600 -23.92200 1.000 59.06000  ? 630  ASP C O   1 
ATOM   8401  C CB  . ASP C 2 66  ? -16.48200 -18.31000 -21.88800 1.000 49.90000  ? 630  ASP C CB  1 
ATOM   8402  C CG  . ASP C 2 66  ? -16.07000 -19.74800 -22.07800 1.000 51.09000  ? 630  ASP C CG  1 
ATOM   8403  O OD1 . ASP C 2 66  ? -15.52100 -20.03900 -23.12600 1.000 60.03000  ? 630  ASP C OD1 1 
ATOM   8404  O OD2 . ASP C 2 66  ? -16.28300 -20.54300 -21.16700 1.000 55.32000  ? 630  ASP C OD2 1 
ATOM   8405  N N   . TYR C 2 67  ? -16.79900 -15.14000 -22.54900 1.000 60.39000  ? 631  TYR C N   1 
ATOM   8406  C CA  . TYR C 2 67  ? -17.72800 -13.99300 -22.63200 1.000 56.50000  ? 631  TYR C CA  1 
ATOM   8407  C C   . TYR C 2 67  ? -17.51300 -13.25900 -23.95400 1.000 60.79000  ? 631  TYR C C   1 
ATOM   8408  O O   . TYR C 2 67  ? -18.45600 -12.70900 -24.49200 1.000 58.08000  ? 631  TYR C O   1 
ATOM   8409  C CB  . TYR C 2 67  ? -17.56000 -13.13100 -21.38600 1.000 57.58000  ? 631  TYR C CB  1 
ATOM   8410  C CG  . TYR C 2 67  ? -18.13000 -11.74500 -21.46800 1.000 67.07000  ? 631  TYR C CG  1 
ATOM   8411  C CD1 . TYR C 2 67  ? -17.48200 -10.75400 -22.17000 1.000 69.33000  ? 631  TYR C CD1 1 
ATOM   8412  C CD2 . TYR C 2 67  ? -19.29300 -11.41500 -20.80500 1.000 75.29000  ? 631  TYR C CD2 1 
ATOM   8413  C CE1 . TYR C 2 67  ? -17.99300 -9.47200  -22.23900 1.000 76.75000  ? 631  TYR C CE1 1 
ATOM   8414  C CE2 . TYR C 2 67  ? -19.81900 -10.13900 -20.85900 1.000 77.18000  ? 631  TYR C CE2 1 
ATOM   8415  C CZ  . TYR C 2 67  ? -19.16700 -9.16600  -21.58600 1.000 79.79000  ? 631  TYR C CZ  1 
ATOM   8416  O OH  . TYR C 2 67  ? -19.67000 -7.90500  -21.65200 1.000 87.71000  ? 631  TYR C OH  1 
ATOM   8417  N N   . LYS C 2 68  ? -16.29100 -13.27600 -24.46900 1.000 64.67000  ? 632  LYS C N   1 
ATOM   8418  C CA  . LYS C 2 68  ? -16.01800 -12.59000 -25.75100 1.000 60.14000  ? 632  LYS C CA  1 
ATOM   8419  C C   . LYS C 2 68  ? -16.59100 -13.42600 -26.89200 1.000 57.05000  ? 632  LYS C C   1 
ATOM   8420  O O   . LYS C 2 68  ? -17.11100 -12.83300 -27.82100 1.000 56.21000  ? 632  LYS C O   1 
ATOM   8421  C CB  . LYS C 2 68  ? -14.52100 -12.34800 -25.93000 1.000 56.58000  ? 632  LYS C CB  1 
ATOM   8422  C CG  . LYS C 2 68  ? -13.82900 -11.68900 -24.75200 1.000 61.21000  ? 632  LYS C CG  1 
ATOM   8423  C CD  . LYS C 2 68  ? -12.55200 -10.99300 -25.15000 1.000 63.22000  ? 632  LYS C CD  1 
ATOM   8424  C CE  . LYS C 2 68  ? -11.30200 -11.75100 -24.77400 1.000 61.83000  ? 632  LYS C CE  1 
ATOM   8425  N NZ  . LYS C 2 68  ? -10.22900 -11.52800 -25.76300 1.000 65.40000  ? 632  LYS C NZ  1 
ATOM   8426  N N   . LYS C 2 69  ? -16.45900 -14.74900 -26.81800 1.000 56.79000  ? 633  LYS C N   1 
ATOM   8427  C CA  . LYS C 2 69  ? -17.01200 -15.62600 -27.85100 1.000 57.18000  ? 633  LYS C CA  1 
ATOM   8428  C C   . LYS C 2 69  ? -18.53300 -15.53500 -27.89200 1.000 60.97000  ? 633  LYS C C   1 
ATOM   8429  O O   . LYS C 2 69  ? -19.13100 -15.37400 -28.96300 1.000 58.48000  ? 633  LYS C O   1 
ATOM   8430  C CB  . LYS C 2 69  ? -16.58900 -17.07600 -27.60400 1.000 48.53000  ? 633  LYS C CB  1 
ATOM   8431  C CG  . LYS C 2 69  ? -15.12700 -17.38600 -27.85500 1.000 53.49000  ? 633  LYS C CG  1 
ATOM   8432  C CD  . LYS C 2 69  ? -14.84700 -18.84000 -27.50500 1.000 51.31000  ? 633  LYS C CD  1 
ATOM   8433  C CE  . LYS C 2 69  ? -13.40300 -19.22200 -27.75900 1.000 50.36000  ? 633  LYS C CE  1 
ATOM   8434  N NZ  . LYS C 2 69  ? -13.16800 -20.63700 -27.35300 1.000 58.07000  ? 633  LYS C NZ  1 
ATOM   8435  N N   . THR C 2 70  ? -19.17800 -15.65000 -26.72300 1.000 58.27000  ? 634  THR C N   1 
ATOM   8436  C CA  . THR C 2 70  ? -20.63300 -15.54400 -26.63600 1.000 56.33000  ? 634  THR C CA  1 
ATOM   8437  C C   . THR C 2 70  ? -21.11800 -14.21900 -27.18400 1.000 55.31000  ? 634  THR C C   1 
ATOM   8438  O O   . THR C 2 70  ? -22.20300 -14.13400 -27.76100 1.000 63.39000  ? 634  THR C O   1 
ATOM   8439  C CB  . THR C 2 70  ? -21.08900 -15.71700 -25.18700 1.000 59.69000  ? 634  THR C CB  1 
ATOM   8440  O OG1 . THR C 2 70  ? -20.54500 -16.91000 -24.64500 1.000 70.02000  ? 634  THR C OG1 1 
ATOM   8441  C CG2 . THR C 2 70  ? -22.60600 -15.81500 -25.11500 1.000 65.31000  ? 634  THR C CG2 1 
ATOM   8442  N N   . LEU C 2 71  ? -20.32200 -13.16600 -27.01200 1.000 61.67000  ? 635  LEU C N   1 
ATOM   8443  C CA  . LEU C 2 71  ? -20.70700 -11.85100 -27.48700 1.000 61.23000  ? 635  LEU C CA  1 
ATOM   8444  C C   . LEU C 2 71  ? -20.53500 -11.71900 -29.00100 1.000 59.52000  ? 635  LEU C C   1 
ATOM   8445  O O   . LEU C 2 71  ? -21.35200 -11.07300 -29.66600 1.000 66.81000  ? 635  LEU C O   1 
ATOM   8446  C CB  . LEU C 2 71  ? -19.90100 -10.79600 -26.71500 1.000 60.89000  ? 635  LEU C CB  1 
ATOM   8447  C CG  . LEU C 2 71  ? -20.23900 -9.32500  -26.81800 1.000 69.11000  ? 635  LEU C CG  1 
ATOM   8448  C CD1 . LEU C 2 71  ? -20.20600 -8.75300  -25.41900 1.000 75.11000  ? 635  LEU C CD1 1 
ATOM   8449  C CD2 . LEU C 2 71  ? -19.18900 -8.63100  -27.65600 1.000 65.65000  ? 635  LEU C CD2 1 
ATOM   8450  N N   . ILE C 2 72  ? -19.50700 -12.34500 -29.57000 1.000 56.48000  ? 636  ILE C N   1 
ATOM   8451  C CA  . ILE C 2 72  ? -19.41300 -12.42800 -31.02500 1.000 64.01000  ? 636  ILE C CA  1 
ATOM   8452  C C   . ILE C 2 72  ? -20.62800 -13.13300 -31.61400 1.000 63.85000  ? 636  ILE C C   1 
ATOM   8453  O O   . ILE C 2 72  ? -21.16000 -12.70700 -32.64700 1.000 68.78000  ? 636  ILE C O   1 
ATOM   8454  C CB  . ILE C 2 72  ? -18.10300 -13.11100 -31.46600 1.000 63.82000  ? 636  ILE C CB  1 
ATOM   8455  C CG1 . ILE C 2 72  ? -16.94100 -12.11800 -31.42700 1.000 58.62000  ? 636  ILE C CG1 1 
ATOM   8456  C CG2 . ILE C 2 72  ? -18.26100 -13.79900 -32.83400 1.000 69.63000  ? 636  ILE C CG2 1 
ATOM   8457  C CD1 . ILE C 2 72  ? -15.60600 -12.75900 -31.68600 1.000 54.70000  ? 636  ILE C CD1 1 
ATOM   8458  N N   . LYS C 2 73  ? -21.08500 -14.22200 -30.99500 1.000 65.62000  ? 637  LYS C N   1 
ATOM   8459  C CA  . LYS C 2 73  ? -22.24200 -14.89500 -31.58000 1.000 65.50000  ? 637  LYS C CA  1 
ATOM   8460  C C   . LYS C 2 73  ? -23.48700 -14.01900 -31.49500 1.000 64.85000  ? 637  LYS C C   1 
ATOM   8461  O O   . LYS C 2 73  ? -24.37300 -14.09900 -32.35100 1.000 63.84000  ? 637  LYS C O   1 
ATOM   8462  C CB  . LYS C 2 73  ? -22.48500 -16.24200 -30.90400 1.000 61.17000  ? 637  LYS C CB  1 
ATOM   8463  C CG  . LYS C 2 73  ? -23.71200 -17.00800 -31.37500 1.000 75.49000  ? 637  LYS C CG  1 
ATOM   8464  C CD  . LYS C 2 73  ? -23.74900 -18.30200 -30.67100 1.000 82.53000  ? 637  LYS C CD  1 
ATOM   8465  C CE  . LYS C 2 73  ? -24.15500 -17.94600 -29.30500 1.000 87.60000  ? 637  LYS C CE  1 
ATOM   8466  N NZ  . LYS C 2 73  ? -24.76400 -18.94600 -28.39600 1.000 93.24000  ? 637  LYS C NZ  1 
ATOM   8467  N N   . TYR C 2 74  ? -23.57400 -13.26100 -30.41200 1.000 60.89000  ? 638  TYR C N   1 
ATOM   8468  C CA  . TYR C 2 74  ? -24.72700 -12.36500 -30.18200 1.000 61.70000  ? 638  TYR C CA  1 
ATOM   8469  C C   . TYR C 2 74  ? -24.78200 -11.32500 -31.29600 1.000 63.72000  ? 638  TYR C C   1 
ATOM   8470  O O   . TYR C 2 74  ? -25.85400 -11.09700 -31.81200 1.000 65.63000  ? 638  TYR C O   1 
ATOM   8471  C CB  . TYR C 2 74  ? -24.61600 -11.73200 -28.80200 1.000 66.84000  ? 638  TYR C CB  1 
ATOM   8472  C CG  . TYR C 2 74  ? -25.87000 -11.05700 -28.32700 1.000 73.82000  ? 638  TYR C CG  1 
ATOM   8473  C CD1 . TYR C 2 74  ? -26.18100 -9.77000  -28.71800 1.000 78.46000  ? 638  TYR C CD1 1 
ATOM   8474  C CD2 . TYR C 2 74  ? -26.73900 -11.70800 -27.47800 1.000 77.73000  ? 638  TYR C CD2 1 
ATOM   8475  C CE1 . TYR C 2 74  ? -27.33100 -9.14400  -28.28100 1.000 79.10000  ? 638  TYR C CE1 1 
ATOM   8476  C CE2 . TYR C 2 74  ? -27.89200 -11.09600 -27.03300 1.000 84.91000  ? 638  TYR C CE2 1 
ATOM   8477  C CZ  . TYR C 2 74  ? -28.18700 -9.81200  -27.43400 1.000 84.17000  ? 638  TYR C CZ  1 
ATOM   8478  O OH  . TYR C 2 74  ? -29.32400 -9.21900  -26.98100 1.000 92.18000  ? 638  TYR C OH  1 
ATOM   8479  N N   . ARG C 2 75  ? -23.65400 -10.70500 -31.63100 1.000 69.23000  ? 639  ARG C N   1 
ATOM   8480  C CA  . ARG C 2 75  ? -23.67500 -9.76500  -32.74400 1.000 70.12000  ? 639  ARG C CA  1 
ATOM   8481  C C   . ARG C 2 75  ? -24.12800 -10.44500 -34.04600 1.000 69.98000  ? 639  ARG C C   1 
ATOM   8482  O O   . ARG C 2 75  ? -24.88200 -9.84700  -34.82400 1.000 74.65000  ? 639  ARG C O   1 
ATOM   8483  C CB  . ARG C 2 75  ? -22.31700 -9.11600  -32.93800 1.000 83.93000  ? 639  ARG C CB  1 
ATOM   8484  C CG  . ARG C 2 75  ? -22.27900 -8.15300  -34.15800 1.000 97.94000  ? 639  ARG C CG  1 
ATOM   8485  C CD  . ARG C 2 75  ? -20.86100 -7.92500  -34.55800 1.000 105.48000 ? 639  ARG C CD  1 
ATOM   8486  N NE  . ARG C 2 75  ? -20.30700 -9.24900  -34.84200 1.000 111.36000 ? 639  ARG C NE  1 
ATOM   8487  C CZ  . ARG C 2 75  ? -19.01500 -9.54500  -34.86300 1.000 116.83000 ? 639  ARG C CZ  1 
ATOM   8488  N NH1 . ARG C 2 75  ? -18.08700 -8.63400  -34.60800 1.000 118.75000 ? 639  ARG C NH1 1 
ATOM   8489  N NH2 . ARG C 2 75  ? -18.64400 -10.78900 -35.12700 1.000 108.28000 ? 639  ARG C NH2 1 
ATOM   8490  N N   . GLU C 2 76  ? -23.69500 -11.68700 -34.32600 1.000 67.60000  ? 640  GLU C N   1 
ATOM   8491  C CA  . GLU C 2 76  ? -24.15300 -12.34400 -35.55500 1.000 68.43000  ? 640  GLU C CA  1 
ATOM   8492  C C   . GLU C 2 76  ? -25.66000 -12.54100 -35.53800 1.000 67.68000  ? 640  GLU C C   1 
ATOM   8493  O O   . GLU C 2 76  ? -26.32200 -12.34600 -36.55700 1.000 70.57000  ? 640  GLU C O   1 
ATOM   8494  C CB  . GLU C 2 76  ? -23.45300 -13.69200 -35.76600 1.000 69.23000  ? 640  GLU C CB  1 
ATOM   8495  C CG  . GLU C 2 76  ? -21.95900 -13.59300 -35.93600 1.000 80.48000  ? 640  GLU C CG  1 
ATOM   8496  C CD  . GLU C 2 76  ? -21.33200 -14.92800 -36.26200 1.000 98.27000  ? 640  GLU C CD  1 
ATOM   8497  O OE1 . GLU C 2 76  ? -22.07600 -15.93700 -36.29800 1.000 97.55000  ? 640  GLU C OE1 1 
ATOM   8498  O OE2 . GLU C 2 76  ? -20.09600 -14.97600 -36.45300 1.000 119.14000 ? 640  GLU C OE2 1 
ATOM   8499  N N   . LEU C 2 77  ? -26.21800 -12.93900 -34.39300 1.000 64.38000  ? 641  LEU C N   1 
ATOM   8500  C CA  . LEU C 2 77  ? -27.66900 -12.99000 -34.26400 1.000 63.63000  ? 641  LEU C CA  1 
ATOM   8501  C C   . LEU C 2 77  ? -28.28900 -11.60100 -34.38600 1.000 66.11000  ? 641  LEU C C   1 
ATOM   8502  O O   . LEU C 2 77  ? -29.40900 -11.46300 -34.89100 1.000 65.04000  ? 641  LEU C O   1 
ATOM   8503  C CB  . LEU C 2 77  ? -28.05700 -13.61200 -32.92900 1.000 54.94000  ? 641  LEU C CB  1 
ATOM   8504  C CG  . LEU C 2 77  ? -27.54600 -15.02200 -32.64900 1.000 49.30000  ? 641  LEU C CG  1 
ATOM   8505  C CD1 . LEU C 2 77  ? -27.94300 -15.44800 -31.24200 1.000 54.77000  ? 641  LEU C CD1 1 
ATOM   8506  C CD2 . LEU C 2 77  ? -28.04400 -16.00400 -33.68500 1.000 42.04000  ? 641  LEU C CD2 1 
ATOM   8507  N N   . GLN C 2 78  ? -27.58700 -10.56900 -33.91600 1.000 69.01000  ? 642  GLN C N   1 
ATOM   8508  C CA  . GLN C 2 78  ? -28.11100 -9.21100  -34.00200 1.000 72.10000  ? 642  GLN C CA  1 
ATOM   8509  C C   . GLN C 2 78  ? -28.18700 -8.75200  -35.45300 1.000 72.19000  ? 642  GLN C C   1 
ATOM   8510  O O   . GLN C 2 78  ? -29.18200 -8.14300  -35.86300 1.000 72.95000  ? 642  GLN C O   1 
ATOM   8511  C CB  . GLN C 2 78  ? -27.24200 -8.25600  -33.18400 1.000 77.37000  ? 642  GLN C CB  1 
ATOM   8512  C CG  . GLN C 2 78  ? -27.91300 -6.94400  -32.80000 1.000 81.28000  ? 642  GLN C CG  1 
ATOM   8513  C CD  . GLN C 2 78  ? -27.89100 -5.89400  -33.88900 1.000 86.51000  ? 642  GLN C CD  1 
ATOM   8514  O OE1 . GLN C 2 78  ? -27.00000 -5.87400  -34.73300 1.000 86.89000  ? 642  GLN C OE1 1 
ATOM   8515  N NE2 . GLN C 2 78  ? -28.88200 -4.99800  -33.86500 1.000 88.50000  ? 642  GLN C NE2 1 
ATOM   8516  N N   . LYS C 2 79  ? -27.14700 -9.03800  -36.24300 1.000 72.99000  ? 643  LYS C N   1 
ATOM   8517  C CA  . LYS C 2 79  ? -27.21700 -8.79100  -37.68000 1.000 76.65000  ? 643  LYS C CA  1 
ATOM   8518  C C   . LYS C 2 79  ? -28.47400 -9.40000  -38.27500 1.000 76.32000  ? 643  LYS C C   1 
ATOM   8519  O O   . LYS C 2 79  ? -29.22100 -8.73600  -39.00200 1.000 74.44000  ? 643  LYS C O   1 
ATOM   8520  C CB  . LYS C 2 79  ? -26.01900 -9.40300  -38.40500 1.000 67.48000  ? 643  LYS C CB  1 
ATOM   8521  C CG  . LYS C 2 79  ? -26.14200 -9.30100  -39.95200 1.000 78.55000  ? 643  LYS C CG  1 
ATOM   8522  C CD  . LYS C 2 79  ? -25.63500 -7.96100  -40.47500 1.000 91.70000  ? 643  LYS C CD  1 
ATOM   8523  C CE  . LYS C 2 79  ? -25.73600 -7.75800  -42.01400 1.000 98.70000  ? 643  LYS C CE  1 
ATOM   8524  N NZ  . LYS C 2 79  ? -27.10900 -7.44000  -42.57700 1.000 112.26000 ? 643  LYS C NZ  1 
ATOM   8525  N N   . LYS C 2 80  ? -28.69000 -10.69300 -38.01800 1.000 70.77000  ? 644  LYS C N   1 
ATOM   8526  C CA  . LYS C 2 80  ? -29.86100 -11.35400 -38.57200 1.000 66.68000  ? 644  LYS C CA  1 
ATOM   8527  C C   . LYS C 2 80  ? -31.11500 -10.60700 -38.18000 1.000 64.33000  ? 644  LYS C C   1 
ATOM   8528  O O   . LYS C 2 80  ? -31.94600 -10.27200 -39.02800 1.000 70.15000  ? 644  LYS C O   1 
ATOM   8529  C CB  . LYS C 2 80  ? -29.96300 -12.79900 -38.08800 1.000 65.14000  ? 644  LYS C CB  1 
ATOM   8530  C CG  . LYS C 2 80  ? -28.74500 -13.65100 -38.25400 1.000 63.00000  ? 644  LYS C CG  1 
ATOM   8531  C CD  . LYS C 2 80  ? -28.20900 -13.63900 -39.65600 1.000 58.17000  ? 644  LYS C CD  1 
ATOM   8532  C CE  . LYS C 2 80  ? -27.47000 -14.91900 -39.85000 1.000 64.17000  ? 644  LYS C CE  1 
ATOM   8533  N NZ  . LYS C 2 80  ? -26.43400 -15.02400 -38.80400 1.000 76.84000  ? 644  LYS C NZ  1 
ATOM   8534  N N   . PHE C 2 81  ? -31.24900 -10.31300 -36.88800 1.000 64.79000  ? 645  PHE C N   1 
ATOM   8535  C CA  . PHE C 2 81  ? -32.49200 -9.75700  -36.37600 1.000 66.39000  ? 645  PHE C CA  1 
ATOM   8536  C C   . PHE C 2 81  ? -32.81100 -8.43800  -37.05800 1.000 71.55000  ? 645  PHE C C   1 
ATOM   8537  O O   . PHE C 2 81  ? -33.90200 -8.25600  -37.60900 1.000 73.75000  ? 645  PHE C O   1 
ATOM   8538  C CB  . PHE C 2 81  ? -32.39900 -9.59700  -34.85600 1.000 66.88000  ? 645  PHE C CB  1 
ATOM   8539  C CG  . PHE C 2 81  ? -33.73100 -9.49200  -34.16700 1.000 64.84000  ? 645  PHE C CG  1 
ATOM   8540  C CD1 . PHE C 2 81  ? -34.56400 -10.60400 -34.08500 1.000 71.25000  ? 645  PHE C CD1 1 
ATOM   8541  C CD2 . PHE C 2 81  ? -34.13500 -8.31700  -33.55900 1.000 62.80000  ? 645  PHE C CD2 1 
ATOM   8542  C CE1 . PHE C 2 81  ? -35.79600 -10.53400 -33.44300 1.000 65.77000  ? 645  PHE C CE1 1 
ATOM   8543  C CE2 . PHE C 2 81  ? -35.36200 -8.24300  -32.90700 1.000 67.76000  ? 645  PHE C CE2 1 
ATOM   8544  C CZ  . PHE C 2 81  ? -36.19300 -9.35500  -32.84800 1.000 65.13000  ? 645  PHE C CZ  1 
ATOM   8545  N N   . GLU C 2 82  ? -31.85000 -7.51000  -37.07400 1.000 74.86000  ? 646  GLU C N   1 
ATOM   8546  C CA  . GLU C 2 82  ? -32.14300 -6.19000  -37.62000 1.000 83.48000  ? 646  GLU C CA  1 
ATOM   8547  C C   . GLU C 2 82  ? -32.46300 -6.28000  -39.10300 1.000 83.41000  ? 646  GLU C C   1 
ATOM   8548  O O   . GLU C 2 82  ? -33.27400 -5.50200  -39.61800 1.000 88.57000  ? 646  GLU C O   1 
ATOM   8549  C CB  . GLU C 2 82  ? -30.97400 -5.22900  -37.34500 1.000 82.99000  ? 646  GLU C CB  1 
ATOM   8550  C CG  . GLU C 2 82  ? -31.46300 -3.88100  -36.80600 1.000 101.85000 ? 646  GLU C CG  1 
ATOM   8551  C CD  . GLU C 2 82  ? -31.95600 -2.89400  -37.84500 1.000 115.78000 ? 646  GLU C CD  1 
ATOM   8552  O OE1 . GLU C 2 82  ? -31.23000 -2.60500  -38.81700 1.000 124.87000 ? 646  GLU C OE1 1 
ATOM   8553  O OE2 . GLU C 2 82  ? -33.13000 -2.48000  -37.70300 1.000 114.43000 ? 646  GLU C OE2 1 
ATOM   8554  N N   . SER C 2 83  ? -31.87300 -7.26700  -39.79900 1.000 79.17000  ? 647  SER C N   1 
ATOM   8555  C CA  . SER C 2 83  ? -32.07900 -7.48600  -41.22600 1.000 79.35000  ? 647  SER C CA  1 
ATOM   8556  C C   . SER C 2 83  ? -33.37500 -8.22600  -41.53500 1.000 71.42000  ? 647  SER C C   1 
ATOM   8557  O O   . SER C 2 83  ? -33.51900 -8.78000  -42.63400 1.000 72.11000  ? 647  SER C O   1 
ATOM   8558  C CB  . SER C 2 83  ? -30.91700 -8.28100  -41.83000 1.000 72.50000  ? 647  SER C CB  1 
ATOM   8559  O OG  . SER C 2 83  ? -31.02200 -9.65100  -41.48400 1.000 70.10000  ? 647  SER C OG  1 
ATOM   8560  N N   . GLY C 2 84  ? -34.31200 -8.28100  -40.58900 1.000 75.42000  ? 648  GLY C N   1 
ATOM   8561  C CA  . GLY C 2 84  ? -35.57500 -8.94700  -40.76500 1.000 75.72000  ? 648  GLY C CA  1 
ATOM   8562  C C   . GLY C 2 84  ? -35.62300 -10.36500 -40.21800 1.000 74.59000  ? 648  GLY C C   1 
ATOM   8563  O O   . GLY C 2 84  ? -36.70500 -10.82500 -39.82600 1.000 70.78000  ? 648  GLY C O   1 
ATOM   8564  N N   . ASP C 2 85  ? -34.47800 -11.06400 -40.17300 1.000 75.21000  ? 649  ASP C N   1 
ATOM   8565  C CA  . ASP C 2 85  ? -34.45900 -12.44700 -39.71000 1.000 64.10000  ? 649  ASP C CA  1 
ATOM   8566  C C   . ASP C 2 85  ? -34.95300 -12.52900 -38.28400 1.000 62.42000  ? 649  ASP C C   1 
ATOM   8567  O O   . ASP C 2 85  ? -34.35700 -12.02700 -37.32700 1.000 66.23000  ? 649  ASP C O   1 
ATOM   8568  C CB  . ASP C 2 85  ? -33.09400 -13.10800 -39.81900 1.000 61.12000  ? 649  ASP C CB  1 
ATOM   8569  C CG  . ASP C 2 85  ? -33.14300 -14.59100 -39.44900 1.000 62.78000  ? 649  ASP C CG  1 
ATOM   8570  O OD1 . ASP C 2 85  ? -34.23200 -15.11100 -39.11000 1.000 60.50000  ? 649  ASP C OD1 1 
ATOM   8571  O OD2 . ASP C 2 85  ? -32.07800 -15.23700 -39.48000 1.000 69.06000  ? 649  ASP C OD2 1 
ATOM   8572  N N   . LYS C 2 86  ? -36.06400 -13.20900 -38.16900 1.000 64.75000  ? 650  LYS C N   1 
ATOM   8573  C CA  . LYS C 2 86  ? -36.97300 -13.06900 -37.05100 1.000 64.72000  ? 650  LYS C CA  1 
ATOM   8574  C C   . LYS C 2 86  ? -36.97500 -14.30100 -36.17400 1.000 55.94000  ? 650  LYS C C   1 
ATOM   8575  O O   . LYS C 2 86  ? -37.52800 -14.26000 -35.08000 1.000 56.66000  ? 650  LYS C O   1 
ATOM   8576  C CB  . LYS C 2 86  ? -38.37300 -12.74200 -37.61500 1.000 61.87000  ? 650  LYS C CB  1 
ATOM   8577  C CG  . LYS C 2 86  ? -39.17200 -13.87200 -38.19200 1.000 68.15000  ? 650  LYS C CG  1 
ATOM   8578  C CD  . LYS C 2 86  ? -38.32600 -14.84700 -39.03600 1.000 55.03000  ? 650  LYS C CD  1 
ATOM   8579  C CE  . LYS C 2 86  ? -39.12700 -15.73800 -39.99600 1.000 56.31000  ? 650  LYS C CE  1 
ATOM   8580  N NZ  . LYS C 2 86  ? -38.66000 -17.20300 -39.94000 1.000 43.47000  ? 650  LYS C NZ  1 
ATOM   8581  N N   . SER C 2 87  ? -36.27700 -15.35600 -36.61200 1.000 50.92000  ? 651  SER C N   1 
ATOM   8582  C CA  . SER C 2 87  ? -36.12100 -16.63800 -35.94000 1.000 48.24000  ? 651  SER C CA  1 
ATOM   8583  C C   . SER C 2 87  ? -35.13100 -16.61700 -34.78700 1.000 52.89000  ? 651  SER C C   1 
ATOM   8584  O O   . SER C 2 87  ? -35.18800 -17.51600 -33.94200 1.000 48.88000  ? 651  SER C O   1 
ATOM   8585  C CB  . SER C 2 87  ? -35.66200 -17.69300 -36.94000 1.000 47.53000  ? 651  SER C CB  1 
ATOM   8586  O OG  . SER C 2 87  ? -34.37500 -17.40400 -37.46400 1.000 44.04000  ? 651  SER C OG  1 
ATOM   8587  N N   . VAL C 2 88  ? -34.19400 -15.66100 -34.75500 1.000 58.55000  ? 652  VAL C N   1 
ATOM   8588  C CA  . VAL C 2 88  ? -33.09100 -15.71900 -33.79600 1.000 54.15000  ? 652  VAL C CA  1 
ATOM   8589  C C   . VAL C 2 88  ? -33.40500 -15.03600 -32.47100 1.000 52.75000  ? 652  VAL C C   1 
ATOM   8590  O O   . VAL C 2 88  ? -32.55000 -15.03500 -31.57500 1.000 53.56000  ? 652  VAL C O   1 
ATOM   8591  C CB  . VAL C 2 88  ? -31.81000 -15.08500 -34.37500 1.000 50.87000  ? 652  VAL C CB  1 
ATOM   8592  C CG1 . VAL C 2 88  ? -31.37500 -15.80700 -35.64700 1.000 49.01000  ? 652  VAL C CG1 1 
ATOM   8593  C CG2 . VAL C 2 88  ? -32.02300 -13.60000 -34.62100 1.000 53.43000  ? 652  VAL C CG2 1 
ATOM   8594  N N   . GLU C 2 89  ? -34.60500 -14.47100 -32.30900 1.000 56.83000  ? 653  GLU C N   1 
ATOM   8595  C CA  . GLU C 2 89  ? -34.87300 -13.63400 -31.13800 1.000 66.22000  ? 653  GLU C CA  1 
ATOM   8596  C C   . GLU C 2 89  ? -34.72300 -14.40900 -29.83500 1.000 59.00000  ? 653  GLU C C   1 
ATOM   8597  O O   . GLU C 2 89  ? -34.23800 -13.86600 -28.83600 1.000 56.57000  ? 653  GLU C O   1 
ATOM   8598  C CB  . GLU C 2 89  ? -36.27100 -13.01100 -31.21700 1.000 61.81000  ? 653  GLU C CB  1 
ATOM   8599  C CG  . GLU C 2 89  ? -36.58700 -12.12400 -30.00600 1.000 65.41000  ? 653  GLU C CG  1 
ATOM   8600  C CD  . GLU C 2 89  ? -37.88000 -11.34300 -30.13700 1.000 72.32000  ? 653  GLU C CD  1 
ATOM   8601  O OE1 . GLU C 2 89  ? -38.51100 -11.41100 -31.21200 1.000 77.87000  ? 653  GLU C OE1 1 
ATOM   8602  O OE2 . GLU C 2 89  ? -38.27300 -10.67800 -29.15100 1.000 71.82000  ? 653  GLU C OE2 1 
ATOM   8603  N N   . GLU C 2 90  ? -35.14900 -15.66700 -29.81100 1.000 53.88000  ? 654  GLU C N   1 
ATOM   8604  C CA  . GLU C 2 90  ? -35.02600 -16.42400 -28.57300 1.000 58.53000  ? 654  GLU C CA  1 
ATOM   8605  C C   . GLU C 2 90  ? -33.61500 -16.97400 -28.35600 1.000 58.00000  ? 654  GLU C C   1 
ATOM   8606  O O   . GLU C 2 90  ? -33.17800 -17.08100 -27.20300 1.000 54.19000  ? 654  GLU C O   1 
ATOM   8607  C CB  . GLU C 2 90  ? -36.07900 -17.53500 -28.53500 1.000 54.64000  ? 654  GLU C CB  1 
ATOM   8608  C CG  . GLU C 2 90  ? -36.06200 -18.39200 -27.27500 1.000 54.53000  ? 654  GLU C CG  1 
ATOM   8609  C CD  . GLU C 2 90  ? -36.19700 -17.59100 -25.98100 1.000 69.07000  ? 654  GLU C CD  1 
ATOM   8610  O OE1 . GLU C 2 90  ? -36.66600 -16.42800 -26.00700 1.000 65.99000  ? 654  GLU C OE1 1 
ATOM   8611  O OE2 . GLU C 2 90  ? -35.85600 -18.15700 -24.91700 1.000 73.51000  ? 654  GLU C OE2 1 
ATOM   8612  N N   . LYS C 2 91  ? -32.88600 -17.32700 -29.42400 1.000 52.25000  ? 655  LYS C N   1 
ATOM   8613  C CA  . LYS C 2 91  ? -31.46200 -17.60500 -29.25400 1.000 54.48000  ? 655  LYS C CA  1 
ATOM   8614  C C   . LYS C 2 91  ? -30.71900 -16.37100 -28.78400 1.000 56.75000  ? 655  LYS C C   1 
ATOM   8615  O O   . LYS C 2 91  ? -29.65500 -16.48400 -28.16800 1.000 61.92000  ? 655  LYS C O   1 
ATOM   8616  C CB  . LYS C 2 91  ? -30.83000 -18.11800 -30.54800 1.000 51.72000  ? 655  LYS C CB  1 
ATOM   8617  C CG  . LYS C 2 91  ? -31.12500 -19.56700 -30.85300 1.000 57.08000  ? 655  LYS C CG  1 
ATOM   8618  C CD  . LYS C 2 91  ? -30.27400 -20.07700 -32.01400 1.000 50.73000  ? 655  LYS C CD  1 
ATOM   8619  C CE  . LYS C 2 91  ? -30.79700 -19.55300 -33.33300 1.000 53.01000  ? 655  LYS C CE  1 
ATOM   8620  N NZ  . LYS C 2 91  ? -30.11900 -20.17400 -34.50000 1.000 69.53000  ? 655  LYS C NZ  1 
ATOM   8621  N N   . MET C 2 92  ? -31.25000 -15.18800 -29.07800 1.000 55.96000  ? 656  MET C N   1 
ATOM   8622  C CA  . MET C 2 92  ? -30.64300 -13.97100 -28.56200 1.000 53.98000  ? 656  MET C CA  1 
ATOM   8623  C C   . MET C 2 92  ? -30.87900 -13.79800 -27.06500 1.000 67.71000  ? 656  MET C C   1 
ATOM   8624  O O   . MET C 2 92  ? -29.95300 -13.42400 -26.34000 1.000 70.03000  ? 656  MET C O   1 
ATOM   8625  C CB  . MET C 2 92  ? -31.13300 -12.76600 -29.36400 1.000 59.72000  ? 656  MET C CB  1 
ATOM   8626  C CG  . MET C 2 92  ? -30.26000 -12.40900 -30.55700 1.000 63.37000  ? 656  MET C CG  1 
ATOM   8627  S SD  . MET C 2 92  ? -31.18600 -11.35300 -31.64500 1.000 72.17000  ? 656  MET C SD  1 
ATOM   8628  C CE  . MET C 2 92  ? -31.48700 -10.09800 -30.43800 1.000 67.71000  ? 656  MET C CE  1 
ATOM   8629  N N   . ASN C 2 93  ? -32.07800 -14.09400 -26.58200 1.000 63.15000  ? 657  ASN C N   1 
ATOM   8630  C CA  . ASN C 2 93  ? -32.29700 -13.97900 -25.12300 1.000 62.41000  ? 657  ASN C CA  1 
ATOM   8631  C C   . ASN C 2 93  ? -31.36500 -14.96800 -24.42500 1.000 65.50000  ? 657  ASN C C   1 
ATOM   8632  O O   . ASN C 2 93  ? -30.59300 -14.54000 -23.58300 1.000 70.74000  ? 657  ASN C O   1 
ATOM   8633  C CB  . ASN C 2 93  ? -33.75400 -14.21000 -24.73800 1.000 70.64000  ? 657  ASN C CB  1 
ATOM   8634  C CG  . ASN C 2 93  ? -34.68200 -13.18200 -25.33900 1.000 79.54000  ? 657  ASN C CG  1 
ATOM   8635  O OD1 . ASN C 2 93  ? -34.24000 -12.14100 -25.80800 1.000 90.11000  ? 657  ASN C OD1 1 
ATOM   8636  N ND2 . ASN C 2 93  ? -35.96800 -13.46800 -25.33900 1.000 78.80000  ? 657  ASN C ND2 1 
ATOM   8637  N N   . GLU C 2 94  ? -31.43200 -16.24100 -24.79800 1.000 60.80000  ? 658  GLU C N   1 
ATOM   8638  C CA  . GLU C 2 94  ? -30.59600 -17.26600 -24.18600 1.000 62.68000  ? 658  GLU C CA  1 
ATOM   8639  C C   . GLU C 2 94  ? -29.12500 -16.88000 -24.21700 1.000 71.24000  ? 658  GLU C C   1 
ATOM   8640  O O   . GLU C 2 94  ? -28.44000 -16.92300 -23.18700 1.000 69.86000  ? 658  GLU C O   1 
ATOM   8641  C CB  . GLU C 2 94  ? -30.80200 -18.59200 -24.91900 1.000 64.71000  ? 658  GLU C CB  1 
ATOM   8642  C CG  . GLU C 2 94  ? -32.10900 -19.29500 -24.62100 1.000 73.37000  ? 658  GLU C CG  1 
ATOM   8643  C CD  . GLU C 2 94  ? -32.33700 -20.50100 -25.52500 1.000 75.73000  ? 658  GLU C CD  1 
ATOM   8644  O OE1 . GLU C 2 94  ? -31.65800 -20.59500 -26.57500 1.000 66.15000  ? 658  GLU C OE1 1 
ATOM   8645  O OE2 . GLU C 2 94  ? -33.14300 -21.38500 -25.14600 1.000 77.96000  ? 658  GLU C OE2 1 
ATOM   8646  N N   . CYS C 2 95  ? -28.62600 -16.49800 -25.40000 1.000 72.65000  ? 659  CYS C N   1 
ATOM   8647  C CA  . CYS C 2 95  ? -27.21600 -16.17200 -25.57700 1.000 67.50000  ? 659  CYS C CA  1 
ATOM   8648  C C   . CYS C 2 95  ? -26.80200 -15.08800 -24.61300 1.000 74.37000  ? 659  CYS C C   1 
ATOM   8649  O O   . CYS C 2 95  ? -25.64400 -15.02500 -24.17700 1.000 81.60000  ? 659  CYS C O   1 
ATOM   8650  C CB  . CYS C 2 95  ? -26.97300 -15.71900 -27.01300 1.000 59.75000  ? 659  CYS C CB  1 
ATOM   8651  S SG  . CYS C 2 95  ? -25.27700 -15.42500 -27.42800 1.000 80.02000  ? 659  CYS C SG  1 
ATOM   8652  N N   . HIS C 2 96  ? -27.75500 -14.23900 -24.24100 1.000 77.37000  ? 660  HIS C N   1 
ATOM   8653  C CA  . HIS C 2 96  ? -27.47400 -13.15900 -23.31900 1.000 73.90000  ? 660  HIS C CA  1 
ATOM   8654  C C   . HIS C 2 96  ? -27.30400 -13.63800 -21.87200 1.000 73.41000  ? 660  HIS C C   1 
ATOM   8655  O O   . HIS C 2 96  ? -26.35200 -13.22200 -21.21400 1.000 80.72000  ? 660  HIS C O   1 
ATOM   8656  C CB  . HIS C 2 96  ? -28.54600 -12.09100 -23.44000 1.000 84.20000  ? 660  HIS C CB  1 
ATOM   8657  C CG  . HIS C 2 96  ? -28.31300 -10.93400 -22.53100 1.000 85.40000  ? 660  HIS C CG  1 
ATOM   8658  N ND1 . HIS C 2 96  ? -27.21100 -10.11700 -22.63600 1.000 88.29000  ? 660  HIS C ND1 1 
ATOM   8659  C CD2 . HIS C 2 96  ? -29.07200 -10.42500 -21.51900 1.000 87.24000  ? 660  HIS C CD2 1 
ATOM   8660  C CE1 . HIS C 2 96  ? -27.29400 -9.18200  -21.70200 1.000 87.95000  ? 660  HIS C CE1 1 
ATOM   8661  N NE2 . HIS C 2 96  ? -28.40800 -9.33300  -21.01500 1.000 91.39000  ? 660  HIS C NE2 1 
ATOM   8662  N N   . LYS C 2 97  ? -28.19500 -14.49300 -21.31100 1.000 73.78000  ? 661  LYS C N   1 
ATOM   8663  C CA  . LYS C 2 97  ? -27.95000 -14.83500 -19.89700 1.000 74.69000  ? 661  LYS C CA  1 
ATOM   8664  C C   . LYS C 2 97  ? -26.69600 -15.69800 -19.76500 1.000 78.90000  ? 661  LYS C C   1 
ATOM   8665  O O   . LYS C 2 97  ? -26.09100 -15.76800 -18.68100 1.000 74.76000  ? 661  LYS C O   1 
ATOM   8666  C CB  . LYS C 2 97  ? -29.09900 -15.60800 -19.25300 1.000 75.49000  ? 661  LYS C CB  1 
ATOM   8667  C CG  . LYS C 2 97  ? -28.85900 -17.09200 -19.38000 1.000 78.80000  ? 661  LYS C CG  1 
ATOM   8668  C CD  . LYS C 2 97  ? -30.22500 -17.58500 -19.66300 1.000 90.20000  ? 661  LYS C CD  1 
ATOM   8669  C CE  . LYS C 2 97  ? -30.19600 -18.60500 -20.84500 1.000 86.13000  ? 661  LYS C CE  1 
ATOM   8670  N NZ  . LYS C 2 97  ? -30.12700 -20.14300 -20.49900 1.000 94.32000  ? 661  LYS C NZ  1 
ATOM   8671  N N   . ILE C 2 98  ? -26.18800 -16.20500 -20.89400 1.000 69.36000  ? 662  ILE C N   1 
ATOM   8672  C CA  . ILE C 2 98  ? -24.96700 -17.04400 -20.84100 1.000 70.88000  ? 662  ILE C CA  1 
ATOM   8673  C C   . ILE C 2 98  ? -23.81900 -16.05700 -20.69600 1.000 74.36000  ? 662  ILE C C   1 
ATOM   8674  O O   . ILE C 2 98  ? -22.93500 -16.25800 -19.87600 1.000 73.48000  ? 662  ILE C O   1 
ATOM   8675  C CB  . ILE C 2 98  ? -24.82900 -17.85300 -22.13700 1.000 64.38000  ? 662  ILE C CB  1 
ATOM   8676  C CG1 . ILE C 2 98  ? -25.83600 -18.99700 -22.20400 1.000 59.55000  ? 662  ILE C CG1 1 
ATOM   8677  C CG2 . ILE C 2 98  ? -23.41000 -18.35300 -22.30200 1.000 64.21000  ? 662  ILE C CG2 1 
ATOM   8678  C CD1 . ILE C 2 98  ? -25.72400 -19.81900 -23.45200 1.000 52.46000  ? 662  ILE C CD1 1 
ATOM   8679  N N   . LEU C 2 99  ? -23.91100 -14.99500 -21.48000 1.000 74.45000  ? 663  LEU C N   1 
ATOM   8680  C CA  . LEU C 2 99  ? -22.93500 -13.89100 -21.52900 1.000 72.47000  ? 663  LEU C CA  1 
ATOM   8681  C C   . LEU C 2 99  ? -22.70100 -13.34600 -20.12400 1.000 71.24000  ? 663  LEU C C   1 
ATOM   8682  O O   . LEU C 2 99  ? -21.56200 -13.16200 -19.75000 1.000 72.22000  ? 663  LEU C O   1 
ATOM   8683  C CB  . LEU C 2 99  ? -23.58700 -12.81400 -22.38600 1.000 69.51000  ? 663  LEU C CB  1 
ATOM   8684  C CG  . LEU C 2 99  ? -22.63700 -11.99100 -23.23000 1.000 70.64000  ? 663  LEU C CG  1 
ATOM   8685  C CD1 . LEU C 2 99  ? -22.92800 -12.22100 -24.69400 1.000 68.95000  ? 663  LEU C CD1 1 
ATOM   8686  C CD2 . LEU C 2 99  ? -22.79800 -10.52800 -22.88700 1.000 77.74000  ? 663  LEU C CD2 1 
ATOM   8687  N N   . ASN C 2 100 ? -23.72100 -13.10600 -19.35400 1.000 69.16000  ? 664  ASN C N   1 
ATOM   8688  C CA  . ASN C 2 100 ? -23.46600 -12.52700 -18.06200 1.000 78.04000  ? 664  ASN C CA  1 
ATOM   8689  C C   . ASN C 2 100 ? -23.00000 -13.57000 -17.05700 1.000 77.79000  ? 664  ASN C C   1 
ATOM   8690  O O   . ASN C 2 100 ? -22.16600 -13.27100 -16.22100 1.000 78.08000  ? 664  ASN C O   1 
ATOM   8691  C CB  . ASN C 2 100 ? -24.69200 -11.77200 -17.56100 1.000 77.39000  ? 664  ASN C CB  1 
ATOM   8692  C CG  . ASN C 2 100 ? -25.04900 -10.60800 -18.44900 1.000 88.07000  ? 664  ASN C CG  1 
ATOM   8693  O OD1 . ASN C 2 100 ? -26.12700 -10.57300 -19.03800 1.000 87.08000  ? 664  ASN C OD1 1 
ATOM   8694  N ND2 . ASN C 2 100 ? -24.14100 -9.65200  -18.56200 1.000 98.69000  ? 664  ASN C ND2 1 
ATOM   8695  N N   . SER C 2 101 ? -23.50300 -14.78600 -17.13000 1.000 68.27000  ? 665  SER C N   1 
ATOM   8696  C CA  . SER C 2 101 ? -22.97500 -15.78400 -16.20700 1.000 69.24000  ? 665  SER C CA  1 
ATOM   8697  C C   . SER C 2 101 ? -21.45200 -15.83900 -16.28700 1.000 75.30000  ? 665  SER C C   1 
ATOM   8698  O O   . SER C 2 101 ? -20.76300 -15.86400 -15.26100 1.000 68.78000  ? 665  SER C O   1 
ATOM   8699  C CB  . SER C 2 101 ? -23.57900 -17.15500 -16.50700 1.000 68.04000  ? 665  SER C CB  1 
ATOM   8700  O OG  . SER C 2 101 ? -23.12800 -17.63700 -17.76400 1.000 73.23000  ? 665  SER C OG  1 
ATOM   8701  N N   . HIS C 2 102 ? -20.91100 -15.83600 -17.50800 1.000 65.26000  ? 666  HIS C N   1 
ATOM   8702  C CA  . HIS C 2 102 ? -19.46300 -15.84900 -17.68800 1.000 67.00000  ? 666  HIS C CA  1 
ATOM   8703  C C   . HIS C 2 102 ? -18.82100 -14.61000 -17.07400 1.000 68.69000  ? 666  HIS C C   1 
ATOM   8704  O O   . HIS C 2 102 ? -17.79400 -14.70400 -16.39100 1.000 66.45000  ? 666  HIS C O   1 
ATOM   8705  C CB  . HIS C 2 102 ? -19.13500 -15.96400 -19.17600 1.000 61.45000  ? 666  HIS C CB  1 
ATOM   8706  C CG  . HIS C 2 102 ? -19.41300 -17.32000 -19.74500 1.000 62.15000  ? 666  HIS C CG  1 
ATOM   8707  N ND1 . HIS C 2 102 ? -19.64800 -17.53500 -21.08600 1.000 66.11000  ? 666  HIS C ND1 1 
ATOM   8708  C CD2 . HIS C 2 102 ? -19.44400 -18.53900 -19.15900 1.000 60.88000  ? 666  HIS C CD2 1 
ATOM   8709  C CE1 . HIS C 2 102 ? -19.85100 -18.82300 -21.29500 1.000 56.00000  ? 666  HIS C CE1 1 
ATOM   8710  N NE2 . HIS C 2 102 ? -19.72500 -19.45600 -20.14300 1.000 58.46000  ? 666  HIS C NE2 1 
ATOM   8711  N N   . TYR C 2 103 ? -19.41900 -13.43600 -17.30200 1.000 67.38000  ? 667  TYR C N   1 
ATOM   8712  C CA  . TYR C 2 103 ? -18.86700 -12.20100 -16.75200 1.000 70.73000  ? 667  TYR C CA  1 
ATOM   8713  C C   . TYR C 2 103 ? -18.83800 -12.25000 -15.23000 1.000 69.16000  ? 667  TYR C C   1 
ATOM   8714  O O   . TYR C 2 103 ? -17.87300 -11.80300 -14.60100 1.000 69.55000  ? 667  TYR C O   1 
ATOM   8715  C CB  . TYR C 2 103 ? -19.68400 -11.00100 -17.23600 1.000 73.86000  ? 667  TYR C CB  1 
ATOM   8716  C CG  . TYR C 2 103 ? -18.99700 -9.66100  -17.05700 1.000 79.57000  ? 667  TYR C CG  1 
ATOM   8717  C CD1 . TYR C 2 103 ? -18.03000 -9.24200  -17.96300 1.000 78.17000  ? 667  TYR C CD1 1 
ATOM   8718  C CD2 . TYR C 2 103 ? -19.30400 -8.82300  -15.98900 1.000 84.00000  ? 667  TYR C CD2 1 
ATOM   8719  C CE1 . TYR C 2 103 ? -17.38700 -8.02300  -17.82200 1.000 84.63000  ? 667  TYR C CE1 1 
ATOM   8720  C CE2 . TYR C 2 103 ? -18.66200 -7.59600  -15.83800 1.000 87.09000  ? 667  TYR C CE2 1 
ATOM   8721  C CZ  . TYR C 2 103 ? -17.70300 -7.20300  -16.76100 1.000 90.12000  ? 667  TYR C CZ  1 
ATOM   8722  O OH  . TYR C 2 103 ? -17.05100 -5.99400  -16.63400 1.000 92.06000  ? 667  TYR C OH  1 
ATOM   8723  N N   . ILE C 2 104 ? -19.88800 -12.79800 -14.62100 1.000 68.19000  ? 668  ILE C N   1 
ATOM   8724  C CA  . ILE C 2 104 ? -19.93000 -12.89000 -13.16900 1.000 65.84000  ? 668  ILE C CA  1 
ATOM   8725  C C   . ILE C 2 104 ? -18.87200 -13.84900 -12.65700 1.000 63.09000  ? 668  ILE C C   1 
ATOM   8726  O O   . ILE C 2 104 ? -18.25700 -13.61200 -11.61100 1.000 69.13000  ? 668  ILE C O   1 
ATOM   8727  C CB  . ILE C 2 104 ? -21.34400 -13.28500 -12.71900 1.000 59.76000  ? 668  ILE C CB  1 
ATOM   8728  C CG1 . ILE C 2 104 ? -22.28500 -12.15900 -13.12600 1.000 69.98000  ? 668  ILE C CG1 1 
ATOM   8729  C CG2 . ILE C 2 104 ? -21.37300 -13.65500 -11.23800 1.000 53.17000  ? 668  ILE C CG2 1 
ATOM   8730  C CD1 . ILE C 2 104 ? -21.78200 -10.79100 -12.68200 1.000 78.32000  ? 668  ILE C CD1 1 
ATOM   8731  N N   . GLU C 2 105 ? -18.64600 -14.94600 -13.37400 1.000 62.35000  ? 669  GLU C N   1 
ATOM   8732  C CA  . GLU C 2 105 ? -17.58200 -15.85400 -12.97700 1.000 63.73000  ? 669  GLU C CA  1 
ATOM   8733  C C   . GLU C 2 105 ? -16.23000 -15.16500 -13.07200 1.000 59.69000  ? 669  GLU C C   1 
ATOM   8734  O O   . GLU C 2 105 ? -15.40500 -15.27800 -12.15900 1.000 57.38000  ? 669  GLU C O   1 
ATOM   8735  C CB  . GLU C 2 105 ? -17.62600 -17.10700 -13.84400 1.000 63.22000  ? 669  GLU C CB  1 
ATOM   8736  C CG  . GLU C 2 105 ? -18.93600 -17.83100 -13.70500 1.000 67.23000  ? 669  GLU C CG  1 
ATOM   8737  C CD  . GLU C 2 105 ? -19.17300 -18.30400 -12.29300 1.000 62.77000  ? 669  GLU C CD  1 
ATOM   8738  O OE1 . GLU C 2 105 ? -18.21000 -18.77700 -11.65500 1.000 66.35000  ? 669  GLU C OE1 1 
ATOM   8739  O OE2 . GLU C 2 105 ? -20.31300 -18.15300 -11.80600 1.000 66.91000  ? 669  GLU C OE2 1 
ATOM   8740  N N   . MET C 2 106 ? -16.01800 -14.40500 -14.14900 1.000 60.84000  ? 670  MET C N   1 
ATOM   8741  C CA  . MET C 2 106 ? -14.77000 -13.67500 -14.33500 1.000 59.03000  ? 670  MET C CA  1 
ATOM   8742  C C   . MET C 2 106 ? -14.49600 -12.74800 -13.15700 1.000 60.86000  ? 670  MET C C   1 
ATOM   8743  O O   . MET C 2 106 ? -13.39000 -12.72900 -12.60700 1.000 60.02000  ? 670  MET C O   1 
ATOM   8744  C CB  . MET C 2 106 ? -14.83300 -12.86400 -15.62700 1.000 56.29000  ? 670  MET C CB  1 
ATOM   8745  C CG  . MET C 2 106 ? -13.50500 -12.28200 -16.03200 1.000 52.89000  ? 670  MET C CG  1 
ATOM   8746  S SD  . MET C 2 106 ? -13.60300 -11.11400 -17.39500 1.000 60.28000  ? 670  MET C SD  1 
ATOM   8747  C CE  . MET C 2 106 ? -14.05600 -9.60000  -16.55900 1.000 69.64000  ? 670  MET C CE  1 
ATOM   8748  N N   . GLN C 2 107 ? -15.50300 -11.96600 -12.76100 1.000 67.19000  ? 671  GLN C N   1 
ATOM   8749  C CA  . GLN C 2 107 ? -15.33700 -11.01900 -11.66200 1.000 69.28000  ? 671  GLN C CA  1 
ATOM   8750  C C   . GLN C 2 107 ? -15.07900 -11.74100 -10.33900 1.000 64.13000  ? 671  GLN C C   1 
ATOM   8751  O O   . GLN C 2 107 ? -14.23500 -11.30700 -9.54400  1.000 66.75000  ? 671  GLN C O   1 
ATOM   8752  C CB  . GLN C 2 107 ? -16.57300 -10.12100 -11.56800 1.000 59.80000  ? 671  GLN C CB  1 
ATOM   8753  C CG  . GLN C 2 107 ? -16.80100 -9.20200  -12.77100 1.000 73.02000  ? 671  GLN C CG  1 
ATOM   8754  C CD  . GLN C 2 107 ? -15.70300 -8.16400  -12.95600 1.000 81.38000  ? 671  GLN C CD  1 
ATOM   8755  O OE1 . GLN C 2 107 ? -14.94100 -8.21100  -13.91900 1.000 83.45000  ? 671  GLN C OE1 1 
ATOM   8756  N NE2 . GLN C 2 107 ? -15.61800 -7.22000  -12.02100 1.000 82.33000  ? 671  GLN C NE2 1 
ATOM   8757  N N   . LYS C 2 108 ? -15.79200 -12.85500 -10.09800 1.000 62.68000  ? 672  LYS C N   1 
ATOM   8758  C CA  . LYS C 2 108 ? -15.52800 -13.73200 -8.95300  1.000 63.04000  ? 672  LYS C CA  1 
ATOM   8759  C C   . LYS C 2 108 ? -14.08200 -14.22500 -8.96400  1.000 72.50000  ? 672  LYS C C   1 
ATOM   8760  O O   . LYS C 2 108 ? -13.41800 -14.24800 -7.91900  1.000 68.32000  ? 672  LYS C O   1 
ATOM   8761  C CB  . LYS C 2 108 ? -16.52100 -14.91200 -8.98200  1.000 66.88000  ? 672  LYS C CB  1 
ATOM   8762  C CG  . LYS C 2 108 ? -16.46900 -15.98000 -7.83100  1.000 81.57000  ? 672  LYS C CG  1 
ATOM   8763  C CD  . LYS C 2 108 ? -16.95500 -15.49700 -6.44100  1.000 83.56000  ? 672  LYS C CD  1 
ATOM   8764  C CE  . LYS C 2 108 ? -16.96100 -16.61000 -5.34100  1.000 85.93000  ? 672  LYS C CE  1 
ATOM   8765  N NZ  . LYS C 2 108 ? -17.87400 -17.80000 -5.56400  1.000 81.50000  ? 672  LYS C NZ  1 
ATOM   8766  N N   . ASN C 2 109 ? -13.56800 -14.59300 -10.14400 1.000 65.16000  ? 673  ASN C N   1 
ATOM   8767  C CA  . ASN C 2 109 ? -12.18400 -15.04100 -10.24800 1.000 63.72000  ? 673  ASN C CA  1 
ATOM   8768  C C   . ASN C 2 109 ? -11.20700 -13.88900 -10.05500 1.000 63.84000  ? 673  ASN C C   1 
ATOM   8769  O O   . ASN C 2 109 ? -10.21700 -14.02200 -9.32500  1.000 63.07000  ? 673  ASN C O   1 
ATOM   8770  C CB  . ASN C 2 109 ? -11.94100 -15.72300 -11.59200 1.000 63.22000  ? 673  ASN C CB  1 
ATOM   8771  C CG  . ASN C 2 109 ? -12.64800 -17.05500 -11.70800 1.000 62.11000  ? 673  ASN C CG  1 
ATOM   8772  O OD1 . ASN C 2 109 ? -13.46500 -17.26300 -12.60600 1.000 58.28000  ? 673  ASN C OD1 1 
ATOM   8773  N ND2 . ASN C 2 109 ? -12.34600 -17.96600 -10.78500 1.000 60.33000  ? 673  ASN C ND2 1 
ATOM   8774  N N   . LEU C 2 110 ? -11.45000 -12.75800 -10.72400 1.000 62.40000  ? 674  LEU C N   1 
ATOM   8775  C CA  . LEU C 2 110 ? -10.57700 -11.60300 -10.54100 1.000 60.23000  ? 674  LEU C CA  1 
ATOM   8776  C C   . LEU C 2 110 ? -10.60100 -11.12100 -9.09800  1.000 63.60000  ? 674  LEU C C   1 
ATOM   8777  O O   . LEU C 2 110 ? -9.57600  -10.67400 -8.57000  1.000 68.75000  ? 674  LEU C O   1 
ATOM   8778  C CB  . LEU C 2 110 ? -10.97100 -10.47300 -11.49000 1.000 57.78000  ? 674  LEU C CB  1 
ATOM   8779  C CG  . LEU C 2 110 ? -10.69300 -10.70900 -12.97400 1.000 56.93000  ? 674  LEU C CG  1 
ATOM   8780  C CD1 . LEU C 2 110 ? -11.08400 -9.49800  -13.82300 1.000 53.31000  ? 674  LEU C CD1 1 
ATOM   8781  C CD2 . LEU C 2 110 ? -9.23400  -11.07700 -13.17500 1.000 60.56000  ? 674  LEU C CD2 1 
ATOM   8782  N N   . GLY C 2 111 ? -11.76300 -11.19700 -8.44600  1.000 58.42000  ? 675  GLY C N   1 
ATOM   8783  C CA  . GLY C 2 111 ? -11.84500 -10.83300 -7.04200  1.000 62.56000  ? 675  GLY C CA  1 
ATOM   8784  C C   . GLY C 2 111 ? -10.96800 -11.68500 -6.14300  1.000 66.70000  ? 675  GLY C C   1 
ATOM   8785  O O   . GLY C 2 111 ? -10.51900 -11.22200 -5.09100  1.000 61.02000  ? 675  GLY C O   1 
ATOM   8786  N N   . ASN C 2 112 ? -10.70800 -12.93300 -6.53700  1.000 67.20000  ? 676  ASN C N   1 
ATOM   8787  C CA  . ASN C 2 112 ? -9.82300  -13.80600 -5.77600  1.000 63.14000  ? 676  ASN C CA  1 
ATOM   8788  C C   . ASN C 2 112 ? -8.34800  -13.48300 -5.98100  1.000 63.99000  ? 676  ASN C C   1 
ATOM   8789  O O   . ASN C 2 112 ? -7.49800  -14.17300 -5.40900  1.000 69.65000  ? 676  ASN C O   1 
ATOM   8790  C CB  . ASN C 2 112 ? -10.06900 -15.26800 -6.14700  1.000 58.98000  ? 676  ASN C CB  1 
ATOM   8791  C CG  . ASN C 2 112 ? -11.39700 -15.77700 -5.64500  1.000 66.96000  ? 676  ASN C CG  1 
ATOM   8792  O OD1 . ASN C 2 112 ? -11.79700 -15.48200 -4.52400  1.000 78.45000  ? 676  ASN C OD1 1 
ATOM   8793  N ND2 . ASN C 2 112 ? -12.09000 -16.55300 -6.47400  1.000 68.13000  ? 676  ASN C ND2 1 
ATOM   8794  N N   . LEU C 2 113 ? -8.01700  -12.47200 -6.77800  1.000 58.79000  ? 677  LEU C N   1 
ATOM   8795  C CA  . LEU C 2 113 ? -6.61900  -12.14100 -7.03000  1.000 63.38000  ? 677  LEU C CA  1 
ATOM   8796  C C   . LEU C 2 113 ? -6.29300  -10.75600 -6.49000  1.000 64.94000  ? 677  LEU C C   1 
ATOM   8797  O O   . LEU C 2 113 ? -7.06200  -9.81000  -6.67200  1.000 64.82000  ? 677  LEU C O   1 
ATOM   8798  C CB  . LEU C 2 113 ? -6.32100  -12.20400 -8.53100  1.000 68.12000  ? 677  LEU C CB  1 
ATOM   8799  C CG  . LEU C 2 113 ? -6.52900  -13.57100 -9.18800  1.000 60.46000  ? 677  LEU C CG  1 
ATOM   8800  C CD1 . LEU C 2 113 ? -6.26800  -13.49900 -10.68600 1.000 55.39000  ? 677  LEU C CD1 1 
ATOM   8801  C CD2 . LEU C 2 113 ? -5.65200  -14.62500 -8.52500  1.000 55.98000  ? 677  LEU C CD2 1 
ATOM   8802  N N   . ILE D 2 1   ? 15.29600  -14.64200 -47.99300 1.000 97.65000  ? 565  ILE D N   1 
ATOM   8803  C CA  . ILE D 2 1   ? 14.83100  -15.32200 -46.78400 1.000 111.42000 ? 565  ILE D CA  1 
ATOM   8804  C C   . ILE D 2 1   ? 14.34000  -16.76000 -47.02100 1.000 116.15000 ? 565  ILE D C   1 
ATOM   8805  O O   . ILE D 2 1   ? 14.54800  -17.63100 -46.17300 1.000 105.96000 ? 565  ILE D O   1 
ATOM   8806  C CB  . ILE D 2 1   ? 13.75600  -14.45400 -46.05600 1.000 101.93000 ? 565  ILE D CB  1 
ATOM   8807  C CG1 . ILE D 2 1   ? 14.43900  -13.49800 -45.06100 1.000 95.84000  ? 565  ILE D CG1 1 
ATOM   8808  C CG2 . ILE D 2 1   ? 12.62700  -15.29700 -45.46800 1.000 93.05000  ? 565  ILE D CG2 1 
ATOM   8809  C CD1 . ILE D 2 1   ? 13.50800  -12.53500 -44.34700 1.000 76.51000  ? 565  ILE D CD1 1 
ATOM   8810  N N   . GLY D 2 2   ? 13.72000  -17.01700 -48.17300 1.000 119.00000 ? 566  GLY D N   1 
ATOM   8811  C CA  . GLY D 2 2   ? 13.27600  -18.36200 -48.51400 1.000 110.29000 ? 566  GLY D CA  1 
ATOM   8812  C C   . GLY D 2 2   ? 14.32400  -19.26700 -49.16300 1.000 104.61000 ? 566  GLY D C   1 
ATOM   8813  O O   . GLY D 2 2   ? 14.26000  -19.52200 -50.37400 1.000 91.96000  ? 566  GLY D O   1 
ATOM   8814  N N   . ASP D 2 3   ? 15.29600  -19.72400 -48.36900 1.000 96.45000  ? 567  ASP D N   1 
ATOM   8815  C CA  . ASP D 2 3   ? 16.38900  -20.59700 -48.87800 1.000 91.68000  ? 567  ASP D CA  1 
ATOM   8816  C C   . ASP D 2 3   ? 15.90500  -22.05200 -48.90400 1.000 86.02000  ? 567  ASP D C   1 
ATOM   8817  O O   . ASP D 2 3   ? 14.88100  -22.34800 -48.27100 1.000 88.55000  ? 567  ASP D O   1 
ATOM   8818  C CB  . ASP D 2 3   ? 17.74500  -20.24400 -48.24400 1.000 86.01000  ? 567  ASP D CB  1 
ATOM   8819  C CG  . ASP D 2 3   ? 18.46000  -21.31500 -47.43500 1.000 86.44000  ? 567  ASP D CG  1 
ATOM   8820  O OD1 . ASP D 2 3   ? 18.31900  -22.49300 -47.74500 1.000 92.51000  ? 567  ASP D OD1 1 
ATOM   8821  O OD2 . ASP D 2 3   ? 19.19500  -20.94400 -46.51300 1.000 81.80000  ? 567  ASP D OD2 1 
ATOM   8822  N N   . GLY D 2 4   ? 16.63400  -22.91000 -49.60800 1.000 71.34000  ? 568  GLY D N   1 
ATOM   8823  C CA  . GLY D 2 4   ? 16.26000  -24.29800 -49.83700 1.000 65.44000  ? 568  GLY D CA  1 
ATOM   8824  C C   . GLY D 2 4   ? 15.89300  -25.03900 -48.55900 1.000 70.49000  ? 568  GLY D C   1 
ATOM   8825  O O   . GLY D 2 4   ? 14.91700  -25.79600 -48.52600 1.000 66.01000  ? 568  GLY D O   1 
ATOM   8826  N N   . LEU D 2 5   ? 16.67000  -24.85800 -47.48100 1.000 63.74000  ? 569  LEU D N   1 
ATOM   8827  C CA  . LEU D 2 5   ? 16.39600  -25.66500 -46.28800 1.000 53.71000  ? 569  LEU D CA  1 
ATOM   8828  C C   . LEU D 2 5   ? 16.08200  -24.89300 -45.00800 1.000 49.25000  ? 569  LEU D C   1 
ATOM   8829  O O   . LEU D 2 5   ? 15.48500  -25.49100 -44.10800 1.000 46.75000  ? 569  LEU D O   1 
ATOM   8830  C CB  . LEU D 2 5   ? 17.55300  -26.63100 -45.97900 1.000 55.24000  ? 569  LEU D CB  1 
ATOM   8831  C CG  . LEU D 2 5   ? 17.84400  -27.77000 -46.96600 1.000 56.04000  ? 569  LEU D CG  1 
ATOM   8832  C CD1 . LEU D 2 5   ? 18.93200  -27.33700 -47.93200 1.000 62.18000  ? 569  LEU D CD1 1 
ATOM   8833  C CD2 . LEU D 2 5   ? 18.15400  -29.11800 -46.31700 1.000 57.48000  ? 569  LEU D CD2 1 
ATOM   8834  N N   . SER D 2 6   ? 16.44500  -23.62000 -44.87500 1.000 49.82000  ? 570  SER D N   1 
ATOM   8835  C CA  . SER D 2 6   ? 16.16000  -22.92900 -43.62200 1.000 50.46000  ? 570  SER D CA  1 
ATOM   8836  C C   . SER D 2 6   ? 14.66300  -22.85800 -43.35700 1.000 49.23000  ? 570  SER D C   1 
ATOM   8837  O O   . SER D 2 6   ? 13.84900  -22.74600 -44.27100 1.000 57.32000  ? 570  SER D O   1 
ATOM   8838  C CB  . SER D 2 6   ? 16.74300  -21.51600 -43.60300 1.000 54.37000  ? 570  SER D CB  1 
ATOM   8839  O OG  . SER D 2 6   ? 18.12000  -21.52600 -43.28500 1.000 54.82000  ? 570  SER D OG  1 
ATOM   8840  N N   . LEU D 2 7   ? 14.31200  -22.94800 -42.07500 1.000 41.84000  ? 571  LEU D N   1 
ATOM   8841  C CA  . LEU D 2 7   ? 12.97000  -22.76000 -41.54300 1.000 39.62000  ? 571  LEU D CA  1 
ATOM   8842  C C   . LEU D 2 7   ? 11.98100  -23.82100 -41.98800 1.000 48.72000  ? 571  LEU D C   1 
ATOM   8843  O O   . LEU D 2 7   ? 10.77800  -23.67000 -41.74800 1.000 46.89000  ? 571  LEU D O   1 
ATOM   8844  C CB  . LEU D 2 7   ? 12.41400  -21.37400 -41.87900 1.000 43.21000  ? 571  LEU D CB  1 
ATOM   8845  C CG  . LEU D 2 7   ? 13.04700  -20.29300 -41.02200 1.000 51.60000  ? 571  LEU D CG  1 
ATOM   8846  C CD1 . LEU D 2 7   ? 12.60100  -18.90900 -41.45100 1.000 53.38000  ? 571  LEU D CD1 1 
ATOM   8847  C CD2 . LEU D 2 7   ? 12.62000  -20.57300 -39.61000 1.000 52.59000  ? 571  LEU D CD2 1 
ATOM   8848  N N   . ILE D 2 8   ? 12.42700  -24.89500 -42.60500 1.000 46.81000  ? 572  ILE D N   1 
ATOM   8849  C CA  . ILE D 2 8   ? 11.49600  -25.99600 -42.78700 1.000 48.28000  ? 572  ILE D CA  1 
ATOM   8850  C C   . ILE D 2 8   ? 11.37200  -26.69800 -41.44200 1.000 46.89000  ? 572  ILE D C   1 
ATOM   8851  O O   . ILE D 2 8   ? 12.29400  -26.66600 -40.62100 1.000 44.60000  ? 572  ILE D O   1 
ATOM   8852  C CB  . ILE D 2 8   ? 11.94600  -26.94700 -43.91900 1.000 46.85000  ? 572  ILE D CB  1 
ATOM   8853  C CG1 . ILE D 2 8   ? 13.09200  -27.86100 -43.49300 1.000 48.98000  ? 572  ILE D CG1 1 
ATOM   8854  C CG2 . ILE D 2 8   ? 12.37800  -26.14900 -45.13100 1.000 46.68000  ? 572  ILE D CG2 1 
ATOM   8855  C CD1 . ILE D 2 8   ? 12.60900  -29.22400 -42.99900 1.000 49.24000  ? 572  ILE D CD1 1 
ATOM   8856  N N   . SER D 2 9   ? 10.21700  -27.29900 -41.17800 1.000 48.04000  ? 573  SER D N   1 
ATOM   8857  C CA  . SER D 2 9   ? 9.99400   -27.94500 -39.89400 1.000 43.13000  ? 573  SER D CA  1 
ATOM   8858  C C   . SER D 2 9   ? 9.51900   -29.37300 -40.10500 1.000 43.28000  ? 573  SER D C   1 
ATOM   8859  O O   . SER D 2 9   ? 8.96500   -29.71400 -41.15300 1.000 44.02000  ? 573  SER D O   1 
ATOM   8860  C CB  . SER D 2 9   ? 8.99300   -27.18300 -39.04600 1.000 37.30000  ? 573  SER D CB  1 
ATOM   8861  O OG  . SER D 2 9   ? 9.49600   -25.90400 -38.70900 1.000 40.02000  ? 573  SER D OG  1 
ATOM   8862  N N   . ILE D 2 10  ? 9.78500   -30.21000 -39.10900 1.000 45.91000  ? 574  ILE D N   1 
ATOM   8863  C CA  . ILE D 2 10  ? 9.38500   -31.61100 -39.09800 1.000 45.08000  ? 574  ILE D CA  1 
ATOM   8864  C C   . ILE D 2 10  ? 8.50100   -31.84600 -37.88700 1.000 43.47000  ? 574  ILE D C   1 
ATOM   8865  O O   . ILE D 2 10  ? 8.86600   -31.47200 -36.76500 1.000 40.38000  ? 574  ILE D O   1 
ATOM   8866  C CB  . ILE D 2 10  ? 10.60300  -32.54600 -39.06000 1.000 40.34000  ? 574  ILE D CB  1 
ATOM   8867  C CG1 . ILE D 2 10  ? 11.41700  -32.38700 -40.33900 1.000 46.15000  ? 574  ILE D CG1 1 
ATOM   8868  C CG2 . ILE D 2 10  ? 10.16500  -33.97700 -38.84000 1.000 42.27000  ? 574  ILE D CG2 1 
ATOM   8869  C CD1 . ILE D 2 10  ? 10.63500  -32.72600 -41.58900 1.000 47.14000  ? 574  ILE D CD1 1 
ATOM   8870  N N   . ILE D 2 11  ? 7.35600   -32.47600 -38.11100 1.000 43.88000  ? 575  ILE D N   1 
ATOM   8871  C CA  . ILE D 2 11  ? 6.39400   -32.78900 -37.06200 1.000 42.68000  ? 575  ILE D CA  1 
ATOM   8872  C C   . ILE D 2 11  ? 6.51200   -34.25900 -36.71900 1.000 39.12000  ? 575  ILE D C   1 
ATOM   8873  O O   . ILE D 2 11  ? 6.40700   -35.11600 -37.60300 1.000 43.45000  ? 575  ILE D O   1 
ATOM   8874  C CB  . ILE D 2 11  ? 4.96900   -32.45600 -37.51900 1.000 43.84000  ? 575  ILE D CB  1 
ATOM   8875  C CG1 . ILE D 2 11  ? 4.81800   -30.94900 -37.65000 1.000 42.67000  ? 575  ILE D CG1 1 
ATOM   8876  C CG2 . ILE D 2 11  ? 3.94900   -33.08500 -36.59100 1.000 48.48000  ? 575  ILE D CG2 1 
ATOM   8877  C CD1 . ILE D 2 11  ? 3.67500   -30.58200 -38.51200 1.000 44.43000  ? 575  ILE D CD1 1 
ATOM   8878  N N   . ASP D 2 12  ? 6.71100   -34.55700 -35.43600 1.000 39.57000  ? 576  ASP D N   1 
ATOM   8879  C CA  . ASP D 2 12  ? 6.90700   -35.94800 -35.03800 1.000 47.31000  ? 576  ASP D CA  1 
ATOM   8880  C C   . ASP D 2 12  ? 5.61100   -36.76000 -35.11500 1.000 54.25000  ? 576  ASP D C   1 
ATOM   8881  O O   . ASP D 2 12  ? 5.63400   -37.92300 -35.53300 1.000 60.72000  ? 576  ASP D O   1 
ATOM   8882  C CB  . ASP D 2 12  ? 7.50700   -36.01000 -33.63500 1.000 42.35000  ? 576  ASP D CB  1 
ATOM   8883  C CG  . ASP D 2 12  ? 8.93800   -35.51500 -33.59500 1.000 47.59000  ? 576  ASP D CG  1 
ATOM   8884  O OD1 . ASP D 2 12  ? 9.62000   -35.59700 -34.64100 1.000 48.11000  ? 576  ASP D OD1 1 
ATOM   8885  O OD2 . ASP D 2 12  ? 9.39400   -35.05900 -32.52300 1.000 46.26000  ? 576  ASP D OD2 1 
ATOM   8886  N N   . GLU D 2 13  ? 4.47600   -36.17900 -34.72500 1.000 50.13000  ? 577  GLU D N   1 
ATOM   8887  C CA  . GLU D 2 13  ? 3.25500   -36.95600 -34.50300 1.000 59.10000  ? 577  GLU D CA  1 
ATOM   8888  C C   . GLU D 2 13  ? 2.38600   -36.93000 -35.75400 1.000 55.36000  ? 577  GLU D C   1 
ATOM   8889  O O   . GLU D 2 13  ? 1.79600   -35.90100 -36.09300 1.000 58.38000  ? 577  GLU D O   1 
ATOM   8890  C CB  . GLU D 2 13  ? 2.46900   -36.42400 -33.31000 1.000 50.91000  ? 577  GLU D CB  1 
ATOM   8891  C CG  . GLU D 2 13  ? 3.21300   -36.48100 -31.98800 1.000 42.85000  ? 577  GLU D CG  1 
ATOM   8892  C CD  . GLU D 2 13  ? 4.06800   -35.24900 -31.77200 1.000 45.73000  ? 577  GLU D CD  1 
ATOM   8893  O OE1 . GLU D 2 13  ? 4.09900   -34.38400 -32.67400 1.000 47.89000  ? 577  GLU D OE1 1 
ATOM   8894  O OE2 . GLU D 2 13  ? 4.68000   -35.12500 -30.69200 1.000 51.09000  ? 577  GLU D OE2 1 
ATOM   8895  N N   . VAL D 2 14  ? 2.27000   -38.06900 -36.41300 1.000 55.51000  ? 578  VAL D N   1 
ATOM   8896  C CA  . VAL D 2 14  ? 1.45400   -38.15500 -37.61600 1.000 62.36000  ? 578  VAL D CA  1 
ATOM   8897  C C   . VAL D 2 14  ? 0.01700   -38.42300 -37.19400 1.000 62.74000  ? 578  VAL D C   1 
ATOM   8898  O O   . VAL D 2 14  ? -0.24000  -39.20100 -36.26700 1.000 63.74000  ? 578  VAL D O   1 
ATOM   8899  C CB  . VAL D 2 14  ? 1.97800   -39.25900 -38.55300 1.000 68.36000  ? 578  VAL D CB  1 
ATOM   8900  C CG1 . VAL D 2 14  ? 1.37500   -39.11700 -39.95600 1.000 58.07000  ? 578  VAL D CG1 1 
ATOM   8901  C CG2 . VAL D 2 14  ? 3.50800   -39.29500 -38.56200 1.000 64.89000  ? 578  VAL D CG2 1 
ATOM   8902  N N   . GLY D 2 15  ? -0.93700  -37.78200 -37.86300 1.000 67.13000  ? 579  GLY D N   1 
ATOM   8903  C CA  . GLY D 2 15  ? -2.33500  -38.00100 -37.52800 1.000 62.05000  ? 579  GLY D CA  1 
ATOM   8904  C C   . GLY D 2 15  ? -3.26100  -37.55300 -38.63500 1.000 64.37000  ? 579  GLY D C   1 
ATOM   8905  O O   . GLY D 2 15  ? -2.89600  -36.74100 -39.48800 1.000 65.02000  ? 579  GLY D O   1 
ATOM   8906  N N   . ASN D 2 16  ? -4.47100  -38.09500 -38.62200 1.000 56.05000  ? 580  ASN D N   1 
ATOM   8907  C CA  . ASN D 2 16  ? -5.43000  -37.62600 -39.59800 1.000 63.91000  ? 580  ASN D CA  1 
ATOM   8908  C C   . ASN D 2 16  ? -5.95600  -36.26400 -39.18600 1.000 54.17000  ? 580  ASN D C   1 
ATOM   8909  O O   . ASN D 2 16  ? -5.96100  -35.89200 -38.00900 1.000 56.44000  ? 580  ASN D O   1 
ATOM   8910  C CB  . ASN D 2 16  ? -6.62700  -38.57100 -39.77700 1.000 56.91000  ? 580  ASN D CB  1 
ATOM   8911  C CG  . ASN D 2 16  ? -6.22200  -39.97900 -40.10700 1.000 58.50000  ? 580  ASN D CG  1 
ATOM   8912  O OD1 . ASN D 2 16  ? -5.06400  -40.23200 -40.46000 1.000 71.37000  ? 580  ASN D OD1 1 
ATOM   8913  N ND2 . ASN D 2 16  ? -7.20600  -40.87400 -40.16800 1.000 59.73000  ? 580  ASN D ND2 1 
ATOM   8914  N N   . GLY D 2 17  ? -6.43700  -35.52600 -40.16300 1.000 47.86000  ? 581  GLY D N   1 
ATOM   8915  C CA  . GLY D 2 17  ? -7.12200  -34.34200 -39.70600 1.000 50.35000  ? 581  GLY D CA  1 
ATOM   8916  C C   . GLY D 2 17  ? -6.36800  -33.08100 -40.06100 1.000 48.50000  ? 581  GLY D C   1 
ATOM   8917  O O   . GLY D 2 17  ? -5.14300  -33.07800 -40.24600 1.000 50.43000  ? 581  GLY D O   1 
ATOM   8918  N N   . GLU D 2 18  ? -7.11300  -31.99100 -40.14300 1.000 48.68000  ? 582  GLU D N   1 
ATOM   8919  C CA  . GLU D 2 18  ? -6.60100  -30.71500 -40.59800 1.000 46.27000  ? 582  GLU D CA  1 
ATOM   8920  C C   . GLU D 2 18  ? -6.14100  -29.91000 -39.39700 1.000 40.02000  ? 582  GLU D C   1 
ATOM   8921  O O   . GLU D 2 18  ? -6.90400  -29.73500 -38.44400 1.000 41.21000  ? 582  GLU D O   1 
ATOM   8922  C CB  . GLU D 2 18  ? -7.70200  -29.95100 -41.32800 1.000 40.92000  ? 582  GLU D CB  1 
ATOM   8923  C CG  . GLU D 2 18  ? -8.29000  -30.68000 -42.51100 1.000 49.44000  ? 582  GLU D CG  1 
ATOM   8924  C CD  . GLU D 2 18  ? -9.44700  -29.90800 -43.12500 1.000 56.23000  ? 582  GLU D CD  1 
ATOM   8925  O OE1 . GLU D 2 18  ? -9.84900  -28.87300 -42.54400 1.000 50.22000  ? 582  GLU D OE1 1 
ATOM   8926  O OE2 . GLU D 2 18  ? -9.95100  -30.33600 -44.18300 1.000 65.27000  ? 582  GLU D OE2 1 
ATOM   8927  N N   . TYR D 2 19  ? -4.91200  -29.39700 -39.44100 1.000 37.16000  ? 583  TYR D N   1 
ATOM   8928  C CA  . TYR D 2 19  ? -4.44200  -28.52900 -38.37000 1.000 39.60000  ? 583  TYR D CA  1 
ATOM   8929  C C   . TYR D 2 19  ? -4.39400  -27.10400 -38.90400 1.000 39.94000  ? 583  TYR D C   1 
ATOM   8930  O O   . TYR D 2 19  ? -3.53400  -26.75900 -39.72200 1.000 46.83000  ? 583  TYR D O   1 
ATOM   8931  C CB  . TYR D 2 19  ? -3.10600  -28.96200 -37.75300 1.000 33.47000  ? 583  TYR D CB  1 
ATOM   8932  C CG  . TYR D 2 19  ? -3.16000  -30.36100 -37.17300 1.000 39.23000  ? 583  TYR D CG  1 
ATOM   8933  C CD1 . TYR D 2 19  ? -3.62200  -31.43600 -37.92200 1.000 40.24000  ? 583  TYR D CD1 1 
ATOM   8934  C CD2 . TYR D 2 19  ? -3.07000  -30.54000 -35.79500 1.000 39.76000  ? 583  TYR D CD2 1 
ATOM   8935  C CE1 . TYR D 2 19  ? -3.74400  -32.69700 -37.37300 1.000 46.22000  ? 583  TYR D CE1 1 
ATOM   8936  C CE2 . TYR D 2 19  ? -3.24000  -31.78900 -35.22200 1.000 40.65000  ? 583  TYR D CE2 1 
ATOM   8937  C CZ  . TYR D 2 19  ? -3.57200  -32.86400 -36.01500 1.000 40.18000  ? 583  TYR D CZ  1 
ATOM   8938  O OH  . TYR D 2 19  ? -3.72600  -34.10500 -35.44900 1.000 47.38000  ? 583  TYR D OH  1 
ATOM   8939  N N   . TRP D 2 20  ? -5.32100  -26.28900 -38.42400 1.000 35.89000  ? 584  TRP D N   1 
ATOM   8940  C CA  . TRP D 2 20  ? -5.50700  -24.91600 -38.86000 1.000 42.33000  ? 584  TRP D CA  1 
ATOM   8941  C C   . TRP D 2 20  ? -4.74600  -23.94800 -37.96400 1.000 45.34000  ? 584  TRP D C   1 
ATOM   8942  O O   . TRP D 2 20  ? -4.55600  -24.19400 -36.76800 1.000 40.97000  ? 584  TRP D O   1 
ATOM   8943  C CB  . TRP D 2 20  ? -7.00200  -24.57600 -38.87100 1.000 39.28000  ? 584  TRP D CB  1 
ATOM   8944  C CG  . TRP D 2 20  ? -7.70700  -25.25500 -40.00800 1.000 43.41000  ? 584  TRP D CG  1 
ATOM   8945  C CD1 . TRP D 2 20  ? -8.21700  -26.52300 -40.02000 1.000 39.92000  ? 584  TRP D CD1 1 
ATOM   8946  C CD2 . TRP D 2 20  ? -7.98500  -24.69700 -41.29800 1.000 43.01000  ? 584  TRP D CD2 1 
ATOM   8947  N NE1 . TRP D 2 20  ? -8.77600  -26.79500 -41.24600 1.000 41.13000  ? 584  TRP D NE1 1 
ATOM   8948  C CE2 . TRP D 2 20  ? -8.65500  -25.68700 -42.04400 1.000 41.91000  ? 584  TRP D CE2 1 
ATOM   8949  C CE3 . TRP D 2 20  ? -7.72800  -23.45900 -41.89500 1.000 43.03000  ? 584  TRP D CE3 1 
ATOM   8950  C CZ2 . TRP D 2 20  ? -9.07100  -25.47800 -43.35300 1.000 38.66000  ? 584  TRP D CZ2 1 
ATOM   8951  C CZ3 . TRP D 2 20  ? -8.14700  -23.25300 -43.19100 1.000 48.20000  ? 584  TRP D CZ3 1 
ATOM   8952  C CH2 . TRP D 2 20  ? -8.81000  -24.25700 -43.90700 1.000 43.67000  ? 584  TRP D CH2 1 
ATOM   8953  N N   . SER D 2 21  ? -4.32000  -22.83500 -38.55900 1.000 46.17000  ? 585  SER D N   1 
ATOM   8954  C CA  . SER D 2 21  ? -3.56500  -21.82800 -37.83600 1.000 44.37000  ? 585  SER D CA  1 
ATOM   8955  C C   . SER D 2 21  ? -4.42900  -21.19000 -36.75100 1.000 48.61000  ? 585  SER D C   1 
ATOM   8956  O O   . SER D 2 21  ? -5.63800  -21.42400 -36.65300 1.000 46.81000  ? 585  SER D O   1 
ATOM   8957  C CB  . SER D 2 21  ? -3.04000  -20.75500 -38.79000 1.000 46.72000  ? 585  SER D CB  1 
ATOM   8958  O OG  . SER D 2 21  ? -4.09100  -19.96800 -39.31300 1.000 49.04000  ? 585  SER D OG  1 
ATOM   8959  N N   . ALA D 2 22  ? -3.77700  -20.36600 -35.92700 1.000 53.51000  ? 586  ALA D N   1 
ATOM   8960  C CA  . ALA D 2 22  ? -4.44400  -19.75900 -34.78000 1.000 51.47000  ? 586  ALA D CA  1 
ATOM   8961  C C   . ALA D 2 22  ? -5.66900  -18.95000 -35.20300 1.000 58.46000  ? 586  ALA D C   1 
ATOM   8962  O O   . ALA D 2 22  ? -6.74000  -19.05700 -34.59300 1.000 60.08000  ? 586  ALA D O   1 
ATOM   8963  C CB  . ALA D 2 22  ? -3.45200  -18.88200 -34.01400 1.000 47.01000  ? 586  ALA D CB  1 
ATOM   8964  N N   . ALA D 2 23  ? -5.53000  -18.13600 -36.25300 1.000 59.46000  ? 587  ALA D N   1 
ATOM   8965  C CA  . ALA D 2 23  ? -6.61700  -17.25700 -36.66600 1.000 55.45000  ? 587  ALA D CA  1 
ATOM   8966  C C   . ALA D 2 23  ? -7.71800  -17.97500 -37.44300 1.000 56.84000  ? 587  ALA D C   1 
ATOM   8967  O O   . ALA D 2 23  ? -8.78200  -17.38700 -37.65700 1.000 61.16000  ? 587  ALA D O   1 
ATOM   8968  C CB  . ALA D 2 23  ? -6.05400  -16.10600 -37.50500 1.000 58.22000  ? 587  ALA D CB  1 
ATOM   8969  N N   . GLY D 2 24  ? -7.49400  -19.21800 -37.86500 1.000 57.61000  ? 588  GLY D N   1 
ATOM   8970  C CA  . GLY D 2 24  ? -8.48500  -19.98500 -38.59300 1.000 49.31000  ? 588  GLY D CA  1 
ATOM   8971  C C   . GLY D 2 24  ? -8.42900  -19.85500 -40.10000 1.000 61.62000  ? 588  GLY D C   1 
ATOM   8972  O O   . GLY D 2 24  ? -9.18200  -20.55000 -40.79800 1.000 66.11000  ? 588  GLY D O   1 
ATOM   8973  N N   . ASP D 2 25  ? -7.55300  -19.00500 -40.62500 1.000 63.36000  ? 589  ASP D N   1 
ATOM   8974  C CA  . ASP D 2 25  ? -7.49900  -18.68900 -42.04600 1.000 60.46000  ? 589  ASP D CA  1 
ATOM   8975  C C   . ASP D 2 25  ? -6.51000  -19.55600 -42.83400 1.000 54.93000  ? 589  ASP D C   1 
ATOM   8976  O O   . ASP D 2 25  ? -6.77500  -19.89000 -43.99200 1.000 54.61000  ? 589  ASP D O   1 
ATOM   8977  C CB  . ASP D 2 25  ? -7.18600  -17.19700 -42.20400 1.000 63.14000  ? 589  ASP D CB  1 
ATOM   8978  C CG  . ASP D 2 25  ? -6.05800  -16.74100 -41.29600 1.000 68.13000  ? 589  ASP D CG  1 
ATOM   8979  O OD1 . ASP D 2 25  ? -5.55000  -17.58200 -40.53200 1.000 68.85000  ? 589  ASP D OD1 1 
ATOM   8980  O OD2 . ASP D 2 25  ? -5.71300  -15.53300 -41.30900 1.000 77.51000  ? 589  ASP D OD2 1 
ATOM   8981  N N   . ILE D 2 26  ? -5.38900  -19.95800 -42.24400 1.000 56.56000  ? 590  ILE D N   1 
ATOM   8982  C CA  . ILE D 2 26  ? -4.38700  -20.76400 -42.94000 1.000 48.12000  ? 590  ILE D CA  1 
ATOM   8983  C C   . ILE D 2 26  ? -4.47200  -22.20800 -42.47000 1.000 48.10000  ? 590  ILE D C   1 
ATOM   8984  O O   . ILE D 2 26  ? -4.54400  -22.48200 -41.26300 1.000 51.57000  ? 590  ILE D O   1 
ATOM   8985  C CB  . ILE D 2 26  ? -2.96200  -20.21900 -42.72100 1.000 47.60000  ? 590  ILE D CB  1 
ATOM   8986  C CG1 . ILE D 2 26  ? -2.80600  -18.80000 -43.26800 1.000 50.71000  ? 590  ILE D CG1 1 
ATOM   8987  C CG2 . ILE D 2 26  ? -1.94600  -21.15400 -43.34700 1.000 52.03000  ? 590  ILE D CG2 1 
ATOM   8988  C CD1 . ILE D 2 26  ? -2.91700  -17.72100 -42.21900 1.000 55.96000  ? 590  ILE D CD1 1 
ATOM   8989  N N   . LEU D 2 27  ? -4.44200  -23.13500 -43.42200 1.000 40.98000  ? 591  LEU D N   1 
ATOM   8990  C CA  . LEU D 2 27  ? -4.30500  -24.55600 -43.12500 1.000 40.00000  ? 591  LEU D CA  1 
ATOM   8991  C C   . LEU D 2 27  ? -2.82300  -24.88600 -43.02800 1.000 45.73000  ? 591  LEU D C   1 
ATOM   8992  O O   . LEU D 2 27  ? -2.12800  -24.94600 -44.04900 1.000 47.61000  ? 591  LEU D O   1 
ATOM   8993  C CB  . LEU D 2 27  ? -4.98200  -25.40400 -44.19800 1.000 42.34000  ? 591  LEU D CB  1 
ATOM   8994  C CG  . LEU D 2 27  ? -4.84500  -26.91500 -43.99800 1.000 45.03000  ? 591  LEU D CG  1 
ATOM   8995  C CD1 . LEU D 2 27  ? -5.50300  -27.35600 -42.70300 1.000 41.85000  ? 591  LEU D CD1 1 
ATOM   8996  C CD2 . LEU D 2 27  ? -5.42600  -27.66500 -45.17300 1.000 41.62000  ? 591  LEU D CD2 1 
ATOM   8997  N N   . LEU D 2 28  ? -2.33500  -25.09400 -41.80100 1.000 43.47000  ? 592  LEU D N   1 
ATOM   8998  C CA  . LEU D 2 28  ? -0.91800  -25.38600 -41.61400 1.000 40.68000  ? 592  LEU D CA  1 
ATOM   8999  C C   . LEU D 2 28  ? -0.55600  -26.72700 -42.23900 1.000 43.04000  ? 592  LEU D C   1 
ATOM   9000  O O   . LEU D 2 28  ? 0.41500   -26.82600 -42.99400 1.000 51.69000  ? 592  LEU D O   1 
ATOM   9001  C CB  . LEU D 2 28  ? -0.56100  -25.37100 -40.12400 1.000 44.62000  ? 592  LEU D CB  1 
ATOM   9002  C CG  . LEU D 2 28  ? -0.72500  -24.06400 -39.33900 1.000 48.84000  ? 592  LEU D CG  1 
ATOM   9003  C CD1 . LEU D 2 28  ? -0.48700  -24.29000 -37.84400 1.000 40.98000  ? 592  LEU D CD1 1 
ATOM   9004  C CD2 . LEU D 2 28  ? 0.18000   -22.95700 -39.87400 1.000 43.81000  ? 592  LEU D CD2 1 
ATOM   9005  N N   . PHE D 2 29  ? -1.33600  -27.76600 -41.95500 1.000 42.55000  ? 593  PHE D N   1 
ATOM   9006  C CA  . PHE D 2 29  ? -1.01300  -29.10300 -42.44300 1.000 45.90000  ? 593  PHE D CA  1 
ATOM   9007  C C   . PHE D 2 29  ? -2.16100  -30.05200 -42.13700 1.000 46.40000  ? 593  PHE D C   1 
ATOM   9008  O O   . PHE D 2 29  ? -2.88800  -29.87500 -41.15500 1.000 47.86000  ? 593  PHE D O   1 
ATOM   9009  C CB  . PHE D 2 29  ? 0.29800   -29.63400 -41.83100 1.000 44.08000  ? 593  PHE D CB  1 
ATOM   9010  C CG  . PHE D 2 29  ? 0.31300   -29.66300 -40.32000 1.000 45.70000  ? 593  PHE D CG  1 
ATOM   9011  C CD1 . PHE D 2 29  ? 0.71300   -28.54700 -39.60200 1.000 41.93000  ? 593  PHE D CD1 1 
ATOM   9012  C CD2 . PHE D 2 29  ? -0.03800  -30.81100 -39.62300 1.000 37.99000  ? 593  PHE D CD2 1 
ATOM   9013  C CE1 . PHE D 2 29  ? 0.73900   -28.56500 -38.22900 1.000 40.28000  ? 593  PHE D CE1 1 
ATOM   9014  C CE2 . PHE D 2 29  ? -0.01000  -30.83400 -38.24900 1.000 36.96000  ? 593  PHE D CE2 1 
ATOM   9015  C CZ  . PHE D 2 29  ? 0.37300   -29.71100 -37.54900 1.000 38.33000  ? 593  PHE D CZ  1 
ATOM   9016  N N   . ALA D 2 30  ? -2.29400  -31.07200 -42.98000 1.000 45.77000  ? 594  ALA D N   1 
ATOM   9017  C CA  . ALA D 2 30  ? -3.39200  -32.02100 -42.89000 1.000 44.33000  ? 594  ALA D CA  1 
ATOM   9018  C C   . ALA D 2 30  ? -2.93200  -33.32900 -43.51300 1.000 45.59000  ? 594  ALA D C   1 
ATOM   9019  O O   . ALA D 2 30  ? -1.79700  -33.44900 -43.97700 1.000 46.78000  ? 594  ALA D O   1 
ATOM   9020  C CB  . ALA D 2 30  ? -4.63800  -31.48800 -43.59400 1.000 47.70000  ? 594  ALA D CB  1 
ATOM   9021  N N   . ALA D 2 31  ? -3.82200  -34.31700 -43.49800 1.000 46.32000  ? 595  ALA D N   1 
ATOM   9022  C CA  . ALA D 2 31  ? -3.64800  -35.55200 -44.25900 1.000 50.72000  ? 595  ALA D CA  1 
ATOM   9023  C C   . ALA D 2 31  ? -2.29100  -36.19500 -43.99800 1.000 51.42000  ? 595  ALA D C   1 
ATOM   9024  O O   . ALA D 2 31  ? -1.63100  -36.68900 -44.91400 1.000 49.54000  ? 595  ALA D O   1 
ATOM   9025  C CB  . ALA D 2 31  ? -3.84800  -35.30200 -45.75700 1.000 45.69000  ? 595  ALA D CB  1 
ATOM   9026  N N   . GLY D 2 32  ? -1.86500  -36.18700 -42.73900 1.000 58.15000  ? 596  GLY D N   1 
ATOM   9027  C CA  . GLY D 2 32  ? -0.61500  -36.85100 -42.40800 1.000 56.67000  ? 596  GLY D CA  1 
ATOM   9028  C C   . GLY D 2 32  ? 0.60100   -36.24600 -43.06200 1.000 56.16000  ? 596  GLY D C   1 
ATOM   9029  O O   . GLY D 2 32  ? 1.62800   -36.91800 -43.19300 1.000 62.68000  ? 596  GLY D O   1 
ATOM   9030  N N   . LYS D 2 33  ? 0.48900   -35.00700 -43.53200 1.000 55.57000  ? 597  LYS D N   1 
ATOM   9031  C CA  . LYS D 2 33  ? 1.65800   -34.22200 -43.89100 1.000 52.17000  ? 597  LYS D CA  1 
ATOM   9032  C C   . LYS D 2 33  ? 2.53100   -34.05800 -42.65500 1.000 58.95000  ? 597  LYS D C   1 
ATOM   9033  O O   . LYS D 2 33  ? 2.02800   -33.72300 -41.57900 1.000 60.46000  ? 597  LYS D O   1 
ATOM   9034  C CB  . LYS D 2 33  ? 1.22600   -32.85400 -44.43600 1.000 52.90000  ? 597  LYS D CB  1 
ATOM   9035  C CG  . LYS D 2 33  ? 2.38500   -31.97500 -44.87500 1.000 63.38000  ? 597  LYS D CG  1 
ATOM   9036  C CD  . LYS D 2 33  ? 1.96300   -30.58100 -45.39400 1.000 70.94000  ? 597  LYS D CD  1 
ATOM   9037  C CE  . LYS D 2 33  ? 3.19600   -29.80100 -45.88600 1.000 84.70000  ? 597  LYS D CE  1 
ATOM   9038  N NZ  . LYS D 2 33  ? 3.00000   -28.37900 -46.29700 1.000 85.72000  ? 597  LYS D NZ  1 
ATOM   9039  N N   . THR D 2 34  ? 3.83000   -34.34100 -42.78500 1.000 55.18000  ? 598  THR D N   1 
ATOM   9040  C CA  . THR D 2 34  ? 4.74500   -34.24800 -41.65200 1.000 53.05000  ? 598  THR D CA  1 
ATOM   9041  C C   . THR D 2 34  ? 5.88300   -33.25000 -41.83900 1.000 52.88000  ? 598  THR D C   1 
ATOM   9042  O O   . THR D 2 34  ? 6.63900   -33.02300 -40.88900 1.000 53.01000  ? 598  THR D O   1 
ATOM   9043  C CB  . THR D 2 34  ? 5.32400   -35.63100 -41.30500 1.000 54.64000  ? 598  THR D CB  1 
ATOM   9044  O OG1 . THR D 2 34  ? 5.81000   -36.28200 -42.49200 1.000 57.49000  ? 598  THR D OG1 1 
ATOM   9045  C CG2 . THR D 2 34  ? 4.27800   -36.49900 -40.63500 1.000 54.72000  ? 598  THR D CG2 1 
ATOM   9046  N N   . LYS D 2 35  ? 6.01100   -32.62300 -43.00600 1.000 53.26000  ? 599  LYS D N   1 
ATOM   9047  C CA  . LYS D 2 35  ? 7.06800   -31.64900 -43.25800 1.000 50.16000  ? 599  LYS D CA  1 
ATOM   9048  C C   . LYS D 2 35  ? 6.44900   -30.31700 -43.66800 1.000 50.64000  ? 599  LYS D C   1 
ATOM   9049  O O   . LYS D 2 35  ? 5.80300   -30.23100 -44.71300 1.000 50.49000  ? 599  LYS D O   1 
ATOM   9050  C CB  . LYS D 2 35  ? 8.03700   -32.16200 -44.33000 1.000 49.59000  ? 599  LYS D CB  1 
ATOM   9051  C CG  . LYS D 2 35  ? 9.18800   -31.21200 -44.60700 1.000 48.21000  ? 599  LYS D CG  1 
ATOM   9052  C CD  . LYS D 2 35  ? 10.31600  -31.85900 -45.40000 1.000 53.07000  ? 599  LYS D CD  1 
ATOM   9053  C CE  . LYS D 2 35  ? 10.03400  -31.97400 -46.88800 1.000 58.85000  ? 599  LYS D CE  1 
ATOM   9054  N NZ  . LYS D 2 35  ? 11.25900  -32.44200 -47.61300 1.000 48.83000  ? 599  LYS D NZ  1 
ATOM   9055  N N   . LEU D 2 36  ? 6.65600   -29.28400 -42.85000 1.000 43.26000  ? 600  LEU D N   1 
ATOM   9056  C CA  . LEU D 2 36  ? 6.17200   -27.93200 -43.11500 1.000 44.77000  ? 600  LEU D CA  1 
ATOM   9057  C C   . LEU D 2 36  ? 7.11500   -27.14800 -44.01500 1.000 49.07000  ? 600  LEU D C   1 
ATOM   9058  O O   . LEU D 2 36  ? 8.33600   -27.29800 -43.94900 1.000 49.69000  ? 600  LEU D O   1 
ATOM   9059  C CB  . LEU D 2 36  ? 5.98900   -27.15700 -41.80700 1.000 45.61000  ? 600  LEU D CB  1 
ATOM   9060  C CG  . LEU D 2 36  ? 4.59500   -27.01700 -41.21400 1.000 45.79000  ? 600  LEU D CG  1 
ATOM   9061  C CD1 . LEU D 2 36  ? 3.95600   -28.35800 -41.09300 1.000 48.68000  ? 600  LEU D CD1 1 
ATOM   9062  C CD2 . LEU D 2 36  ? 4.70900   -26.37900 -39.83600 1.000 36.61000  ? 600  LEU D CD2 1 
ATOM   9063  N N   . SER D 2 37  ? 6.53200   -26.27600 -44.83900 1.000 54.13000  ? 601  SER D N   1 
ATOM   9064  C CA  . SER D 2 37  ? 7.33000   -25.33300 -45.59800 1.000 54.32000  ? 601  SER D CA  1 
ATOM   9065  C C   . SER D 2 37  ? 7.88000   -24.27900 -44.64600 1.000 48.86000  ? 601  SER D C   1 
ATOM   9066  O O   . SER D 2 37  ? 7.42900   -24.16700 -43.50500 1.000 52.19000  ? 601  SER D O   1 
ATOM   9067  C CB  . SER D 2 37  ? 6.50100   -24.65700 -46.69500 1.000 57.47000  ? 601  SER D CB  1 
ATOM   9068  O OG  . SER D 2 37  ? 5.57200   -23.73000 -46.14900 1.000 52.49000  ? 601  SER D OG  1 
ATOM   9069  N N   . PRO D 2 38  ? 8.88100   -23.51500 -45.07900 1.000 43.98000  ? 602  PRO D N   1 
ATOM   9070  C CA  . PRO D 2 38  ? 9.28100   -22.35400 -44.27200 1.000 47.64000  ? 602  PRO D CA  1 
ATOM   9071  C C   . PRO D 2 38  ? 8.13600   -21.40500 -43.99100 1.000 46.46000  ? 602  PRO D C   1 
ATOM   9072  O O   . PRO D 2 38  ? 8.05000   -20.86000 -42.88300 1.000 43.00000  ? 602  PRO D O   1 
ATOM   9073  C CB  . PRO D 2 38  ? 10.38100  -21.70700 -45.12300 1.000 47.64000  ? 602  PRO D CB  1 
ATOM   9074  C CG  . PRO D 2 38  ? 10.98800  -22.86600 -45.84900 1.000 47.93000  ? 602  PRO D CG  1 
ATOM   9075  C CD  . PRO D 2 38  ? 9.83800   -23.78400 -46.16800 1.000 48.71000  ? 602  PRO D CD  1 
ATOM   9076  N N   . TYR D 2 39  ? 7.24100   -21.19900 -44.96200 1.000 53.60000  ? 603  TYR D N   1 
ATOM   9077  C CA  . TYR D 2 39  ? 6.13100   -20.27400 -44.75400 1.000 52.55000  ? 603  TYR D CA  1 
ATOM   9078  C C   . TYR D 2 39  ? 5.19200   -20.77200 -43.65800 1.000 52.82000  ? 603  TYR D C   1 
ATOM   9079  O O   . TYR D 2 39  ? 4.75900   -19.99100 -42.80300 1.000 56.86000  ? 603  TYR D O   1 
ATOM   9080  C CB  . TYR D 2 39  ? 5.37300   -20.05100 -46.06700 1.000 61.83000  ? 603  TYR D CB  1 
ATOM   9081  C CG  . TYR D 2 39  ? 4.21500   -19.07900 -45.92900 1.000 68.06000  ? 603  TYR D CG  1 
ATOM   9082  C CD1 . TYR D 2 39  ? 4.43000   -17.70700 -45.82600 1.000 71.09000  ? 603  TYR D CD1 1 
ATOM   9083  C CD2 . TYR D 2 39  ? 2.90500   -19.53800 -45.88300 1.000 64.74000  ? 603  TYR D CD2 1 
ATOM   9084  C CE1 . TYR D 2 39  ? 3.36100   -16.82000 -45.68800 1.000 69.69000  ? 603  TYR D CE1 1 
ATOM   9085  C CE2 . TYR D 2 39  ? 1.83600   -18.66900 -45.75200 1.000 66.55000  ? 603  TYR D CE2 1 
ATOM   9086  C CZ  . TYR D 2 39  ? 2.06600   -17.31300 -45.64600 1.000 69.03000  ? 603  TYR D CZ  1 
ATOM   9087  O OH  . TYR D 2 39  ? 0.99000   -16.46200 -45.50500 1.000 71.84000  ? 603  TYR D OH  1 
ATOM   9088  N N   . MET D 2 40  ? 4.86700   -22.06700 -43.66600 1.000 47.77000  ? 604  MET D N   1 
ATOM   9089  C CA  . MET D 2 40  ? 3.98000   -22.62000 -42.64500 1.000 44.84000  ? 604  MET D CA  1 
ATOM   9090  C C   . MET D 2 40  ? 4.61900   -22.56000 -41.26000 1.000 50.54000  ? 604  MET D C   1 
ATOM   9091  O O   . MET D 2 40  ? 3.93400   -22.29100 -40.26000 1.000 45.71000  ? 604  MET D O   1 
ATOM   9092  C CB  . MET D 2 40  ? 3.62600   -24.05300 -43.03000 1.000 45.80000  ? 604  MET D CB  1 
ATOM   9093  C CG  . MET D 2 40  ? 2.79000   -24.16000 -44.29500 1.000 46.58000  ? 604  MET D CG  1 
ATOM   9094  S SD  . MET D 2 40  ? 1.09600   -23.59700 -44.03900 1.000 65.73000  ? 604  MET D SD  1 
ATOM   9095  C CE  . MET D 2 40  ? 1.11700   -21.96200 -44.71500 1.000 51.11000  ? 604  MET D CE  1 
ATOM   9096  N N   . THR D 2 41  ? 5.93400   -22.81100 -41.19500 1.000 46.40000  ? 605  THR D N   1 
ATOM   9097  C CA  . THR D 2 41  ? 6.68600   -22.71600 -39.94800 1.000 41.75000  ? 605  THR D CA  1 
ATOM   9098  C C   . THR D 2 41  ? 6.57300   -21.34000 -39.31800 1.000 41.88000  ? 605  THR D C   1 
ATOM   9099  O O   . THR D 2 41  ? 6.35300   -21.21800 -38.10900 1.000 42.65000  ? 605  THR D O   1 
ATOM   9100  C CB  . THR D 2 41  ? 8.15000   -23.06300 -40.21400 1.000 42.16000  ? 605  THR D CB  1 
ATOM   9101  O OG1 . THR D 2 41  ? 8.27900   -24.45000 -40.52900 1.000 40.80000  ? 605  THR D OG1 1 
ATOM   9102  C CG2 . THR D 2 41  ? 9.01900   -22.71500 -39.02900 1.000 39.89000  ? 605  THR D CG2 1 
ATOM   9103  N N   . VAL D 2 42  ? 6.72600   -20.29200 -40.11700 1.000 42.31000  ? 606  VAL D N   1 
ATOM   9104  C CA  . VAL D 2 42  ? 6.67900   -18.94600 -39.56500 1.000 45.21000  ? 606  VAL D CA  1 
ATOM   9105  C C   . VAL D 2 42  ? 5.29500   -18.64700 -39.01400 1.000 53.80000  ? 606  VAL D C   1 
ATOM   9106  O O   . VAL D 2 42  ? 5.16100   -17.93700 -38.00500 1.000 56.06000  ? 606  VAL D O   1 
ATOM   9107  C CB  . VAL D 2 42  ? 7.10900   -17.91800 -40.63500 1.000 52.26000  ? 606  VAL D CB  1 
ATOM   9108  C CG1 . VAL D 2 42  ? 6.98100   -16.49000 -40.10500 1.000 55.55000  ? 606  VAL D CG1 1 
ATOM   9109  C CG2 . VAL D 2 42  ? 8.54100   -18.19900 -41.07300 1.000 58.64000  ? 606  VAL D CG2 1 
ATOM   9110  N N   . ILE D 2 43  ? 4.25000   -19.18100 -39.64800 1.000 46.70000  ? 607  ILE D N   1 
ATOM   9111  C CA  . ILE D 2 43  ? 2.89900   -18.93800 -39.16100 1.000 44.15000  ? 607  ILE D CA  1 
ATOM   9112  C C   . ILE D 2 43  ? 2.62100   -19.72700 -37.89600 1.000 41.10000  ? 607  ILE D C   1 
ATOM   9113  O O   . ILE D 2 43  ? 2.00200   -19.21200 -36.96000 1.000 47.23000  ? 607  ILE D O   1 
ATOM   9114  C CB  . ILE D 2 43  ? 1.88000   -19.26000 -40.26300 1.000 55.48000  ? 607  ILE D CB  1 
ATOM   9115  C CG1 . ILE D 2 43  ? 2.06000   -18.26300 -41.39700 1.000 49.29000  ? 607  ILE D CG1 1 
ATOM   9116  C CG2 . ILE D 2 43  ? 0.44900   -19.22500 -39.73300 1.000 39.93000  ? 607  ILE D CG2 1 
ATOM   9117  C CD1 . ILE D 2 43  ? 1.28500   -18.61000 -42.56100 1.000 54.52000  ? 607  ILE D CD1 1 
ATOM   9118  N N   . SER D 2 44  ? 3.07100   -20.98100 -37.84600 1.000 39.89000  ? 608  SER D N   1 
ATOM   9119  C CA  . SER D 2 44  ? 2.88200   -21.78200 -36.64100 1.000 38.47000  ? 608  SER D CA  1 
ATOM   9120  C C   . SER D 2 44  ? 3.54900   -21.12500 -35.44300 1.000 48.10000  ? 608  SER D C   1 
ATOM   9121  O O   . SER D 2 44  ? 2.93400   -20.96600 -34.38200 1.000 49.27000  ? 608  SER D O   1 
ATOM   9122  C CB  . SER D 2 44  ? 3.45700   -23.17600 -36.86200 1.000 45.15000  ? 608  SER D CB  1 
ATOM   9123  O OG  . SER D 2 44  ? 2.87600   -23.77500 -38.00300 1.000 56.64000  ? 608  SER D OG  1 
ATOM   9124  N N   . LEU D 2 45  ? 4.81700   -20.72700 -35.59900 1.000 45.06000  ? 609  LEU D N   1 
ATOM   9125  C CA  . LEU D 2 45  ? 5.56500   -20.16400 -34.47900 1.000 44.94000  ? 609  LEU D CA  1 
ATOM   9126  C C   . LEU D 2 45  ? 5.17800   -18.71800 -34.19300 1.000 47.00000  ? 609  LEU D C   1 
ATOM   9127  O O   . LEU D 2 45  ? 5.25400   -18.27800 -33.04100 1.000 50.20000  ? 609  LEU D O   1 
ATOM   9128  C CB  . LEU D 2 45  ? 7.06600   -20.26600 -34.74400 1.000 45.01000  ? 609  LEU D CB  1 
ATOM   9129  C CG  . LEU D 2 45  ? 7.60200   -21.70100 -34.80800 1.000 46.07000  ? 609  LEU D CG  1 
ATOM   9130  C CD1 . LEU D 2 45  ? 9.03200   -21.71100 -35.27100 1.000 46.71000  ? 609  LEU D CD1 1 
ATOM   9131  C CD2 . LEU D 2 45  ? 7.48100   -22.37800 -33.45200 1.000 45.14000  ? 609  LEU D CD2 1 
ATOM   9132  N N   . GLY D 2 46  ? 4.77200   -17.97000 -35.20900 1.000 44.60000  ? 610  GLY D N   1 
ATOM   9133  C CA  . GLY D 2 46  ? 4.35400   -16.58800 -34.98500 1.000 47.19000  ? 610  GLY D CA  1 
ATOM   9134  C C   . GLY D 2 46  ? 5.47300   -15.59200 -34.84600 1.000 41.25000  ? 610  GLY D C   1 
ATOM   9135  O O   . GLY D 2 46  ? 5.43200   -14.52100 -35.45500 1.000 48.31000  ? 610  GLY D O   1 
ATOM   9136  N N   . THR D 2 47  ? 6.47800   -15.90900 -34.04800 1.000 44.15000  ? 611  THR D N   1 
ATOM   9137  C CA  . THR D 2 47  ? 7.66200   -15.07700 -33.92800 1.000 48.10000  ? 611  THR D CA  1 
ATOM   9138  C C   . THR D 2 47  ? 8.87800   -15.85000 -34.40700 1.000 46.75000  ? 611  THR D C   1 
ATOM   9139  O O   . THR D 2 47  ? 8.89200   -17.08400 -34.43300 1.000 49.04000  ? 611  THR D O   1 
ATOM   9140  C CB  . THR D 2 47  ? 7.90300   -14.61300 -32.48100 1.000 53.64000  ? 611  THR D CB  1 
ATOM   9141  O OG1 . THR D 2 47  ? 8.07200   -15.75500 -31.62600 1.000 48.89000  ? 611  THR D OG1 1 
ATOM   9142  C CG2 . THR D 2 47  ? 6.74700   -13.75700 -31.99000 1.000 51.18000  ? 611  THR D CG2 1 
ATOM   9143  N N   . TRP D 2 48  ? 9.90300   -15.10300 -34.79900 1.000 49.49000  ? 612  TRP D N   1 
ATOM   9144  C CA  . TRP D 2 48  ? 11.16800  -15.71200 -35.15900 1.000 50.46000  ? 612  TRP D CA  1 
ATOM   9145  C C   . TRP D 2 48  ? 12.27300  -14.71900 -34.85400 1.000 54.66000  ? 612  TRP D C   1 
ATOM   9146  O O   . TRP D 2 48  ? 12.03100  -13.51400 -34.73100 1.000 51.80000  ? 612  TRP D O   1 
ATOM   9147  C CB  . TRP D 2 48  ? 11.18800  -16.12800 -36.63400 1.000 50.35000  ? 612  TRP D CB  1 
ATOM   9148  C CG  . TRP D 2 48  ? 12.31000  -17.04100 -36.94200 1.000 51.90000  ? 612  TRP D CG  1 
ATOM   9149  C CD1 . TRP D 2 48  ? 13.41500  -16.77800 -37.69600 1.000 56.11000  ? 612  TRP D CD1 1 
ATOM   9150  C CD2 . TRP D 2 48  ? 12.46800  -18.37400 -36.44900 1.000 55.64000  ? 612  TRP D CD2 1 
ATOM   9151  N NE1 . TRP D 2 48  ? 14.23900  -17.88100 -37.72800 1.000 53.27000  ? 612  TRP D NE1 1 
ATOM   9152  C CE2 . TRP D 2 48  ? 13.67900  -18.87100 -36.96300 1.000 53.67000  ? 612  TRP D CE2 1 
ATOM   9153  C CE3 . TRP D 2 48  ? 11.69300  -19.20300 -35.62800 1.000 58.49000  ? 612  TRP D CE3 1 
ATOM   9154  C CZ2 . TRP D 2 48  ? 14.13400  -20.15700 -36.68500 1.000 58.44000  ? 612  TRP D CZ2 1 
ATOM   9155  C CZ3 . TRP D 2 48  ? 12.15200  -20.48300 -35.35000 1.000 56.42000  ? 612  TRP D CZ3 1 
ATOM   9156  C CH2 . TRP D 2 48  ? 13.35700  -20.94800 -35.88100 1.000 58.03000  ? 612  TRP D CH2 1 
ATOM   9157  N N   . MET D 2 49  ? 13.49000  -15.24000 -34.70100 1.000 47.51000  ? 613  MET D N   1 
ATOM   9158  C CA  . MET D 2 49  ? 14.65900  -14.38500 -34.60300 1.000 47.60000  ? 613  MET D CA  1 
ATOM   9159  C C   . MET D 2 49  ? 15.79400  -15.06000 -35.34900 1.000 50.14000  ? 613  MET D C   1 
ATOM   9160  O O   . MET D 2 49  ? 15.97200  -16.27800 -35.25500 1.000 52.86000  ? 613  MET D O   1 
ATOM   9161  C CB  . MET D 2 49  ? 15.05600  -14.12900 -33.14900 1.000 50.04000  ? 613  MET D CB  1 
ATOM   9162  C CG  . MET D 2 49  ? 15.90600  -12.88800 -32.93300 1.000 52.22000  ? 613  MET D CG  1 
ATOM   9163  S SD  . MET D 2 49  ? 16.28100  -12.74000 -31.17800 1.000 59.54000  ? 613  MET D SD  1 
ATOM   9164  C CE  . MET D 2 49  ? 14.60100  -12.70400 -30.54600 1.000 51.40000  ? 613  MET D CE  1 
ATOM   9165  N N   . TYR D 2 50  ? 16.54800  -14.27500 -36.10400 1.000 51.64000  ? 614  TYR D N   1 
ATOM   9166  C CA  . TYR D 2 50  ? 17.74000  -14.79600 -36.75100 1.000 48.49000  ? 614  TYR D CA  1 
ATOM   9167  C C   . TYR D 2 50  ? 18.94400  -14.68200 -35.83100 1.000 45.78000  ? 614  TYR D C   1 
ATOM   9168  O O   . TYR D 2 50  ? 19.15800  -13.65800 -35.17400 1.000 43.97000  ? 614  TYR D O   1 
ATOM   9169  C CB  . TYR D 2 50  ? 17.98600  -14.09500 -38.08500 1.000 44.03000  ? 614  TYR D CB  1 
ATOM   9170  C CG  . TYR D 2 50  ? 17.07200  -14.64900 -39.15200 1.000 51.70000  ? 614  TYR D CG  1 
ATOM   9171  C CD1 . TYR D 2 50  ? 17.36900  -15.85700 -39.77300 1.000 50.23000  ? 614  TYR D CD1 1 
ATOM   9172  C CD2 . TYR D 2 50  ? 15.89700  -14.00600 -39.50500 1.000 47.16000  ? 614  TYR D CD2 1 
ATOM   9173  C CE1 . TYR D 2 50  ? 16.54200  -16.39500 -40.72800 1.000 45.92000  ? 614  TYR D CE1 1 
ATOM   9174  C CE2 . TYR D 2 50  ? 15.06000  -14.53700 -40.47100 1.000 58.16000  ? 614  TYR D CE2 1 
ATOM   9175  C CZ  . TYR D 2 50  ? 15.38700  -15.73400 -41.07600 1.000 60.53000  ? 614  TYR D CZ  1 
ATOM   9176  O OH  . TYR D 2 50  ? 14.55300  -16.26900 -42.03400 1.000 68.30000  ? 614  TYR D OH  1 
ATOM   9177  N N   . GLU D 2 51  ? 19.71200  -15.77200 -35.77900 1.000 49.34000  ? 615  GLU D N   1 
ATOM   9178  C CA  . GLU D 2 51  ? 20.91200  -15.83400 -34.95200 1.000 44.92000  ? 615  GLU D CA  1 
ATOM   9179  C C   . GLU D 2 51  ? 21.84800  -14.66200 -35.21700 1.000 46.85000  ? 615  GLU D C   1 
ATOM   9180  O O   . GLU D 2 51  ? 22.44000  -14.11100 -34.28400 1.000 47.33000  ? 615  GLU D O   1 
ATOM   9181  C CB  . GLU D 2 51  ? 21.61200  -17.15900 -35.21500 1.000 38.29000  ? 615  GLU D CB  1 
ATOM   9182  C CG  . GLU D 2 51  ? 21.65700  -17.40600 -36.70200 1.000 57.35000  ? 615  GLU D CG  1 
ATOM   9183  C CD  . GLU D 2 51  ? 20.64200  -18.43800 -37.12400 1.000 46.15000  ? 615  GLU D CD  1 
ATOM   9184  O OE1 . GLU D 2 51  ? 20.15100  -19.14300 -36.22700 1.000 43.59000  ? 615  GLU D OE1 1 
ATOM   9185  O OE2 . GLU D 2 51  ? 20.26400  -18.47400 -38.31600 1.000 53.11000  ? 615  GLU D OE2 1 
ATOM   9186  N N   . THR D 2 52  ? 21.99500  -14.26000 -36.48100 1.000 49.20000  ? 616  THR D N   1 
ATOM   9187  C CA  . THR D 2 52  ? 22.82300  -13.09800 -36.78400 1.000 50.93000  ? 616  THR D CA  1 
ATOM   9188  C C   . THR D 2 52  ? 22.22300  -11.81400 -36.22400 1.000 54.23000  ? 616  THR D C   1 
ATOM   9189  O O   . THR D 2 52  ? 22.96300  -10.91200 -35.81700 1.000 54.44000  ? 616  THR D O   1 
ATOM   9190  C CB  . THR D 2 52  ? 23.03300  -12.98400 -38.29600 1.000 56.91000  ? 616  THR D CB  1 
ATOM   9191  O OG1 . THR D 2 52  ? 23.83400  -11.83000 -38.58400 1.000 67.63000  ? 616  THR D OG1 1 
ATOM   9192  C CG2 . THR D 2 52  ? 21.69900  -12.90200 -39.02800 1.000 52.50000  ? 616  THR D CG2 1 
ATOM   9193  N N   . ASP D 2 53  ? 20.89200  -11.70900 -36.19500 1.000 54.13000  ? 617  ASP D N   1 
ATOM   9194  C CA  . ASP D 2 53  ? 20.26700  -10.57300 -35.52900 1.000 48.52000  ? 617  ASP D CA  1 
ATOM   9195  C C   . ASP D 2 53  ? 20.45500  -10.66200 -34.02500 1.000 52.30000  ? 617  ASP D C   1 
ATOM   9196  O O   . ASP D 2 53  ? 20.74100  -9.65500  -33.36600 1.000 51.37000  ? 617  ASP D O   1 
ATOM   9197  C CB  . ASP D 2 53  ? 18.78500  -10.51000 -35.87200 1.000 52.64000  ? 617  ASP D CB  1 
ATOM   9198  C CG  . ASP D 2 53  ? 18.54200  -10.25400 -37.34000 1.000 60.76000  ? 617  ASP D CG  1 
ATOM   9199  O OD1 . ASP D 2 53  ? 19.42700  -9.64900  -37.98300 1.000 66.70000  ? 617  ASP D OD1 1 
ATOM   9200  O OD2 . ASP D 2 53  ? 17.46900  -10.65400 -37.84800 1.000 53.71000  ? 617  ASP D OD2 1 
ATOM   9201  N N   . LEU D 2 54  ? 20.30300  -11.86300 -33.46400 1.000 48.78000  ? 618  LEU D N   1 
ATOM   9202  C CA  . LEU D 2 54  ? 20.52300  -12.03000 -32.03300 1.000 50.84000  ? 618  LEU D CA  1 
ATOM   9203  C C   . LEU D 2 54  ? 21.93900  -11.62100 -31.64500 1.000 50.31000  ? 618  LEU D C   1 
ATOM   9204  O O   . LEU D 2 54  ? 22.15200  -11.07700 -30.55800 1.000 47.51000  ? 618  LEU D O   1 
ATOM   9205  C CB  . LEU D 2 54  ? 20.23400  -13.47500 -31.62100 1.000 45.37000  ? 618  LEU D CB  1 
ATOM   9206  C CG  . LEU D 2 54  ? 20.37500  -13.79900 -30.13100 1.000 46.41000  ? 618  LEU D CG  1 
ATOM   9207  C CD1 . LEU D 2 54  ? 19.38100  -13.01100 -29.29600 1.000 48.75000  ? 618  LEU D CD1 1 
ATOM   9208  C CD2 . LEU D 2 54  ? 20.21000  -15.29400 -29.87700 1.000 43.26000  ? 618  LEU D CD2 1 
ATOM   9209  N N   . MET D 2 55  ? 22.91800  -11.85000 -32.52600 1.000 46.50000  ? 619  MET D N   1 
ATOM   9210  C CA  . MET D 2 55  ? 24.29600  -11.51200 -32.17400 1.000 54.92000  ? 619  MET D CA  1 
ATOM   9211  C C   . MET D 2 55  ? 24.53700  -10.00600 -32.16600 1.000 50.07000  ? 619  MET D C   1 
ATOM   9212  O O   . MET D 2 55  ? 25.27200  -9.50200  -31.31000 1.000 54.46000  ? 619  MET D O   1 
ATOM   9213  C CB  . MET D 2 55  ? 25.27300  -12.23100 -33.09900 1.000 59.28000  ? 619  MET D CB  1 
ATOM   9214  C CG  . MET D 2 55  ? 25.20300  -13.73000 -32.87300 1.000 71.08000  ? 619  MET D CG  1 
ATOM   9215  S SD  . MET D 2 55  ? 25.60100  -14.18600 -31.16300 1.000 78.98000  ? 619  MET D SD  1 
ATOM   9216  C CE  . MET D 2 55  ? 24.93300  -15.85100 -31.09800 1.000 62.22000  ? 619  MET D CE  1 
ATOM   9217  N N   . GLN D 2 56  ? 23.94100  -9.26200  -33.09700 1.000 50.93000  ? 620  GLN D N   1 
ATOM   9218  C CA  . GLN D 2 56  ? 24.04400  -7.81100  -32.97800 1.000 52.28000  ? 620  GLN D CA  1 
ATOM   9219  C C   . GLN D 2 56  ? 23.35000  -7.31400  -31.71800 1.000 52.74000  ? 620  GLN D C   1 
ATOM   9220  O O   . GLN D 2 56  ? 23.86100  -6.41900  -31.03600 1.000 55.65000  ? 620  GLN D O   1 
ATOM   9221  C CB  . GLN D 2 56  ? 23.48500  -7.12100  -34.21800 1.000 57.63000  ? 620  GLN D CB  1 
ATOM   9222  C CG  . GLN D 2 56  ? 24.32700  -7.35300  -35.45400 1.000 72.88000  ? 620  GLN D CG  1 
ATOM   9223  C CD  . GLN D 2 56  ? 25.74300  -6.82300  -35.28600 1.000 78.20000  ? 620  GLN D CD  1 
ATOM   9224  O OE1 . GLN D 2 56  ? 25.97100  -5.78500  -34.66800 1.000 78.78000  ? 620  GLN D OE1 1 
ATOM   9225  N NE2 . GLN D 2 56  ? 26.70700  -7.55700  -35.82700 1.000 73.83000  ? 620  GLN D NE2 1 
ATOM   9226  N N   . TRP D 2 57  ? 22.19000  -7.88400  -31.38700 1.000 48.56000  ? 621  TRP D N   1 
ATOM   9227  C CA  . TRP D 2 57  ? 21.53400  -7.52700  -30.13600 1.000 49.36000  ? 621  TRP D CA  1 
ATOM   9228  C C   . TRP D 2 57  ? 22.44400  -7.83200  -28.96000 1.000 49.37000  ? 621  TRP D C   1 
ATOM   9229  O O   . TRP D 2 57  ? 22.60800  -7.01100  -28.05100 1.000 49.61000  ? 621  TRP D O   1 
ATOM   9230  C CB  . TRP D 2 57  ? 20.22500  -8.30600  -29.98600 1.000 49.15000  ? 621  TRP D CB  1 
ATOM   9231  C CG  . TRP D 2 57  ? 19.41000  -7.90200  -28.79000 1.000 42.65000  ? 621  TRP D CG  1 
ATOM   9232  C CD1 . TRP D 2 57  ? 18.59200  -6.81500  -28.68600 1.000 42.15000  ? 621  TRP D CD1 1 
ATOM   9233  C CD2 . TRP D 2 57  ? 19.40300  -8.53200  -27.50200 1.000 41.17000  ? 621  TRP D CD2 1 
ATOM   9234  N NE1 . TRP D 2 57  ? 18.03800  -6.75500  -27.43200 1.000 44.41000  ? 621  TRP D NE1 1 
ATOM   9235  C CE2 . TRP D 2 57  ? 18.52300  -7.79500  -26.68200 1.000 47.40000  ? 621  TRP D CE2 1 
ATOM   9236  C CE3 . TRP D 2 57  ? 20.03900  -9.65800  -26.96900 1.000 40.08000  ? 621  TRP D CE3 1 
ATOM   9237  C CZ2 . TRP D 2 57  ? 18.25900  -8.15000  -25.35400 1.000 42.56000  ? 621  TRP D CZ2 1 
ATOM   9238  C CZ3 . TRP D 2 57  ? 19.78400  -10.00800 -25.65200 1.000 44.27000  ? 621  TRP D CZ3 1 
ATOM   9239  C CH2 . TRP D 2 57  ? 18.90100  -9.25400  -24.85700 1.000 44.52000  ? 621  TRP D CH2 1 
ATOM   9240  N N   . ARG D 2 58  ? 23.05900  -9.01300  -28.98600 1.000 47.89000  ? 622  ARG D N   1 
ATOM   9241  C CA  . ARG D 2 58  ? 23.93200  -9.46100  -27.91100 1.000 49.64000  ? 622  ARG D CA  1 
ATOM   9242  C C   . ARG D 2 58  ? 25.13900  -8.54100  -27.74600 1.000 50.38000  ? 622  ARG D C   1 
ATOM   9243  O O   . ARG D 2 58  ? 25.49900  -8.16900  -26.62300 1.000 50.44000  ? 622  ARG D O   1 
ATOM   9244  C CB  . ARG D 2 58  ? 24.32800  -10.91200 -28.20700 1.000 53.12000  ? 622  ARG D CB  1 
ATOM   9245  C CG  . ARG D 2 58  ? 25.25500  -11.58500 -27.24500 1.000 51.78000  ? 622  ARG D CG  1 
ATOM   9246  C CD  . ARG D 2 58  ? 26.61700  -11.63400 -27.83100 1.000 57.08000  ? 622  ARG D CD  1 
ATOM   9247  N NE  . ARG D 2 58  ? 27.60100  -12.22900 -26.94100 1.000 59.29000  ? 622  ARG D NE  1 
ATOM   9248  C CZ  . ARG D 2 58  ? 28.90500  -12.05200 -27.09000 1.000 60.91000  ? 622  ARG D CZ  1 
ATOM   9249  N NH1 . ARG D 2 58  ? 29.38700  -11.31200 -28.07300 1.000 60.54000  ? 622  ARG D NH1 1 
ATOM   9250  N NH2 . ARG D 2 58  ? 29.74000  -12.57400 -26.19700 1.000 61.98000  ? 622  ARG D NH2 1 
ATOM   9251  N N   . LEU D 2 59  ? 25.75500  -8.13400  -28.85700 1.000 45.09000  ? 623  LEU D N   1 
ATOM   9252  C CA  . LEU D 2 59  ? 26.87200  -7.19700  -28.79500 1.000 52.54000  ? 623  LEU D CA  1 
ATOM   9253  C C   . LEU D 2 59  ? 26.43400  -5.84100  -28.25500 1.000 47.65000  ? 623  LEU D C   1 
ATOM   9254  O O   . LEU D 2 59  ? 27.08000  -5.27600  -27.36600 1.000 47.32000  ? 623  LEU D O   1 
ATOM   9255  C CB  . LEU D 2 59  ? 27.48600  -7.05900  -30.18600 1.000 62.24000  ? 623  LEU D CB  1 
ATOM   9256  C CG  . LEU D 2 59  ? 28.19400  -8.34100  -30.61900 1.000 62.65000  ? 623  LEU D CG  1 
ATOM   9257  C CD1 . LEU D 2 59  ? 28.44800  -8.34900  -32.11000 1.000 61.46000  ? 623  LEU D CD1 1 
ATOM   9258  C CD2 . LEU D 2 59  ? 29.50400  -8.45900  -29.85400 1.000 54.34000  ? 623  LEU D CD2 1 
ATOM   9259  N N   . ALA D 2 60  ? 25.32800  -5.30800  -28.77900 1.000 55.35000  ? 624  ALA D N   1 
ATOM   9260  C CA  . ALA D 2 60  ? 24.82300  -4.01700  -28.31500 1.000 57.99000  ? 624  ALA D CA  1 
ATOM   9261  C C   . ALA D 2 60  ? 24.52800  -4.04000  -26.82100 1.000 52.92000  ? 624  ALA D C   1 
ATOM   9262  O O   . ALA D 2 60  ? 24.84000  -3.08100  -26.10600 1.000 53.66000  ? 624  ALA D O   1 
ATOM   9263  C CB  . ALA D 2 60  ? 23.57000  -3.63100  -29.10400 1.000 54.74000  ? 624  ALA D CB  1 
ATOM   9264  N N   . CYS D 2 61  ? 23.93300  -5.12800  -26.32900 1.000 48.30000  ? 625  CYS D N   1 
ATOM   9265  C CA  . CYS D 2 61  ? 23.63100  -5.20900  -24.90200 1.000 56.60000  ? 625  CYS D CA  1 
ATOM   9266  C C   . CYS D 2 61  ? 24.89900  -5.24600  -24.05600 1.000 52.00000  ? 625  CYS D C   1 
ATOM   9267  O O   . CYS D 2 61  ? 24.96300  -4.60600  -23.00200 1.000 52.39000  ? 625  CYS D O   1 
ATOM   9268  C CB  . CYS D 2 61  ? 22.75700  -6.42400  -24.61000 1.000 53.36000  ? 625  CYS D CB  1 
ATOM   9269  S SG  . CYS D 2 61  ? 21.06800  -6.21700  -25.15500 1.000 47.48000  ? 625  CYS D SG  1 
ATOM   9270  N N   . ILE D 2 62  ? 25.91400  -5.99800  -24.48800 1.000 51.11000  ? 626  ILE D N   1 
ATOM   9271  C CA  . ILE D 2 62  ? 27.16200  -6.05300  -23.72700 1.000 53.50000  ? 626  ILE D CA  1 
ATOM   9272  C C   . ILE D 2 62  ? 27.82200  -4.68200  -23.68900 1.000 54.87000  ? 626  ILE D C   1 
ATOM   9273  O O   . ILE D 2 62  ? 28.18100  -4.17700  -22.61800 1.000 55.54000  ? 626  ILE D O   1 
ATOM   9274  C CB  . ILE D 2 62  ? 28.10500  -7.11600  -24.31300 1.000 44.58000  ? 626  ILE D CB  1 
ATOM   9275  C CG1 . ILE D 2 62  ? 27.51200  -8.51100  -24.09600 1.000 49.25000  ? 626  ILE D CG1 1 
ATOM   9276  C CG2 . ILE D 2 62  ? 29.47700  -7.00000  -23.68800 1.000 45.57000  ? 626  ILE D CG2 1 
ATOM   9277  C CD1 . ILE D 2 62  ? 28.19900  -9.59200  -24.86800 1.000 41.67000  ? 626  ILE D CD1 1 
ATOM   9278  N N   . ASN D 2 63  ? 27.96800  -4.05100  -24.85800 1.000 56.50000  ? 627  ASN D N   1 
ATOM   9279  C CA  . ASN D 2 63  ? 28.52100  -2.70000  -24.92500 1.000 60.65000  ? 627  ASN D CA  1 
ATOM   9280  C C   . ASN D 2 63  ? 27.74900  -1.74500  -24.02700 1.000 64.86000  ? 627  ASN D C   1 
ATOM   9281  O O   . ASN D 2 63  ? 28.34200  -0.90000  -23.34500 1.000 69.80000  ? 627  ASN D O   1 
ATOM   9282  C CB  . ASN D 2 63  ? 28.49900  -2.20700  -26.37200 1.000 62.18000  ? 627  ASN D CB  1 
ATOM   9283  C CG  . ASN D 2 63  ? 29.54400  -2.88300  -27.23300 1.000 68.04000  ? 627  ASN D CG  1 
ATOM   9284  O OD1 . ASN D 2 63  ? 30.71900  -2.94400  -26.87100 1.000 64.41000  ? 627  ASN D OD1 1 
ATOM   9285  N ND2 . ASN D 2 63  ? 29.11300  -3.43300  -28.36000 1.000 64.61000  ? 627  ASN D ND2 1 
ATOM   9286  N N   . TYR D 2 64  ? 26.42100  -1.87700  -24.00800 1.000 62.30000  ? 628  TYR D N   1 
ATOM   9287  C CA  . TYR D 2 64  ? 25.57600  -1.01900  -23.18400 1.000 63.33000  ? 628  TYR D CA  1 
ATOM   9288  C C   . TYR D 2 64  ? 25.79600  -1.29900  -21.70100 1.000 63.48000  ? 628  TYR D C   1 
ATOM   9289  O O   . TYR D 2 64  ? 25.95600  -0.37100  -20.89900 1.000 65.88000  ? 628  TYR D O   1 
ATOM   9290  C CB  . TYR D 2 64  ? 24.11900  -1.23100  -23.61000 1.000 70.67000  ? 628  TYR D CB  1 
ATOM   9291  C CG  . TYR D 2 64  ? 23.04300  -0.31800  -23.05000 1.000 75.73000  ? 628  TYR D CG  1 
ATOM   9292  C CD1 . TYR D 2 64  ? 23.08800  1.05700   -23.24800 1.000 76.40000  ? 628  TYR D CD1 1 
ATOM   9293  C CD2 . TYR D 2 64  ? 21.89800  -0.85000  -22.46200 1.000 75.04000  ? 628  TYR D CD2 1 
ATOM   9294  C CE1 . TYR D 2 64  ? 22.08000  1.88200   -22.79400 1.000 81.72000  ? 628  TYR D CE1 1 
ATOM   9295  C CE2 . TYR D 2 64  ? 20.87400  -0.03300  -22.02100 1.000 82.19000  ? 628  TYR D CE2 1 
ATOM   9296  C CZ  . TYR D 2 64  ? 20.97400  1.33500   -22.17600 1.000 87.38000  ? 628  TYR D CZ  1 
ATOM   9297  O OH  . TYR D 2 64  ? 19.95900  2.15600   -21.72200 1.000 88.78000  ? 628  TYR D OH  1 
ATOM   9298  N N   . SER D 2 65  ? 25.83600  -2.57800  -21.32100 1.000 63.33000  ? 629  SER D N   1 
ATOM   9299  C CA  . SER D 2 65  ? 26.09100  -2.92900  -19.92900 1.000 58.76000  ? 629  SER D CA  1 
ATOM   9300  C C   . SER D 2 65  ? 27.44100  -2.38900  -19.47100 1.000 70.67000  ? 629  SER D C   1 
ATOM   9301  O O   . SER D 2 65  ? 27.55900  -1.82900  -18.37500 1.000 73.69000  ? 629  SER D O   1 
ATOM   9302  C CB  . SER D 2 65  ? 26.03000  -4.44400  -19.75600 1.000 50.68000  ? 629  SER D CB  1 
ATOM   9303  O OG  . SER D 2 65  ? 26.29800  -4.80300  -18.40900 1.000 60.82000  ? 629  SER D OG  1 
ATOM   9304  N N   . ASP D 2 66  ? 28.47100  -2.53900  -20.31000 1.000 66.53000  ? 630  ASP D N   1 
ATOM   9305  C CA  . ASP D 2 66  ? 29.78300  -1.99300  -19.97000 1.000 71.82000  ? 630  ASP D CA  1 
ATOM   9306  C C   . ASP D 2 66  ? 29.72800  -0.48500  -19.77900 1.000 75.99000  ? 630  ASP D C   1 
ATOM   9307  O O   . ASP D 2 66  ? 30.30700  0.04600   -18.82300 1.000 80.07000  ? 630  ASP D O   1 
ATOM   9308  C CB  . ASP D 2 66  ? 30.82200  -2.34900  -21.03900 1.000 61.88000  ? 630  ASP D CB  1 
ATOM   9309  C CG  . ASP D 2 66  ? 31.33200  -3.77400  -20.90900 1.000 64.33000  ? 630  ASP D CG  1 
ATOM   9310  O OD1 . ASP D 2 66  ? 31.28400  -4.32400  -19.78500 1.000 63.30000  ? 630  ASP D OD1 1 
ATOM   9311  O OD2 . ASP D 2 66  ? 31.82000  -4.32500  -21.92300 1.000 65.77000  ? 630  ASP D OD2 1 
ATOM   9312  N N   . TYR D 2 67  ? 29.03900  0.22900   -20.66600 1.000 79.21000  ? 631  TYR D N   1 
ATOM   9313  C CA  . TYR D 2 67  ? 28.94800  1.66800   -20.47200 1.000 82.64000  ? 631  TYR D CA  1 
ATOM   9314  C C   . TYR D 2 67  ? 28.16300  2.02600   -19.22100 1.000 83.67000  ? 631  TYR D C   1 
ATOM   9315  O O   . TYR D 2 67  ? 28.49900  3.00800   -18.55400 1.000 91.80000  ? 631  TYR D O   1 
ATOM   9316  C CB  . TYR D 2 67  ? 28.42400  2.30100   -21.75900 1.000 82.67000  ? 631  TYR D CB  1 
ATOM   9317  C CG  . TYR D 2 67  ? 27.67500  3.60100   -21.68700 1.000 89.53000  ? 631  TYR D CG  1 
ATOM   9318  C CD1 . TYR D 2 67  ? 28.02300  4.63000   -20.80500 1.000 93.62000  ? 631  TYR D CD1 1 
ATOM   9319  C CD2 . TYR D 2 67  ? 26.75600  3.87900   -22.66900 1.000 96.15000  ? 631  TYR D CD2 1 
ATOM   9320  C CE1 . TYR D 2 67  ? 27.31300  5.83700   -20.81800 1.000 94.04000  ? 631  TYR D CE1 1 
ATOM   9321  C CE2 . TYR D 2 67  ? 26.08000  5.06400   -22.71000 1.000 100.64000 ? 631  TYR D CE2 1 
ATOM   9322  C CZ  . TYR D 2 67  ? 26.35100  6.03900   -21.79800 1.000 96.92000  ? 631  TYR D CZ  1 
ATOM   9323  O OH  . TYR D 2 67  ? 25.58000  7.16200   -21.92700 1.000 96.36000  ? 631  TYR D OH  1 
ATOM   9324  N N   . LYS D 2 68  ? 27.18600  1.22000   -18.83000 1.000 78.21000  ? 632  LYS D N   1 
ATOM   9325  C CA  . LYS D 2 68  ? 26.54600  1.47300   -17.54500 1.000 83.59000  ? 632  LYS D CA  1 
ATOM   9326  C C   . LYS D 2 68  ? 27.50300  1.24700   -16.36900 1.000 81.70000  ? 632  LYS D C   1 
ATOM   9327  O O   . LYS D 2 68  ? 27.50800  2.03200   -15.41300 1.000 86.45000  ? 632  LYS D O   1 
ATOM   9328  C CB  . LYS D 2 68  ? 25.30100  0.60700   -17.41900 1.000 79.11000  ? 632  LYS D CB  1 
ATOM   9329  C CG  . LYS D 2 68  ? 24.11000  1.06100   -18.24900 1.000 72.20000  ? 632  LYS D CG  1 
ATOM   9330  C CD  . LYS D 2 68  ? 23.04100  -0.01200  -18.12800 1.000 72.69000  ? 632  LYS D CD  1 
ATOM   9331  C CE  . LYS D 2 68  ? 21.79600  0.20100   -18.98400 1.000 81.43000  ? 632  LYS D CE  1 
ATOM   9332  N NZ  . LYS D 2 68  ? 20.98600  1.45800   -18.76100 1.000 91.80000  ? 632  LYS D NZ  1 
ATOM   9333  N N   . LYS D 2 69  ? 28.30800  0.17900   -16.40400 1.000 82.57000  ? 633  LYS D N   1 
ATOM   9334  C CA  . LYS D 2 69  ? 29.21000  -0.10000  -15.28300 1.000 91.83000  ? 633  LYS D CA  1 
ATOM   9335  C C   . LYS D 2 69  ? 30.32200  0.93700   -15.19000 1.000 93.10000  ? 633  LYS D C   1 
ATOM   9336  O O   . LYS D 2 69  ? 30.57900  1.48900   -14.11400 1.000 97.72000  ? 633  LYS D O   1 
ATOM   9337  C CB  . LYS D 2 69  ? 29.81500  -1.49000  -15.42500 1.000 85.69000  ? 633  LYS D CB  1 
ATOM   9338  C CG  . LYS D 2 69  ? 28.87000  -2.65800  -15.35800 1.000 83.92000  ? 633  LYS D CG  1 
ATOM   9339  C CD  . LYS D 2 69  ? 29.73700  -3.84400  -15.71500 1.000 81.50000  ? 633  LYS D CD  1 
ATOM   9340  C CE  . LYS D 2 69  ? 28.96400  -5.08600  -16.04600 1.000 66.04000  ? 633  LYS D CE  1 
ATOM   9341  N NZ  . LYS D 2 69  ? 29.95500  -6.13700  -16.39600 1.000 64.74000  ? 633  LYS D NZ  1 
ATOM   9342  N N   . THR D 2 70  ? 31.00200  1.20900   -16.30700 1.000 88.80000  ? 634  THR D N   1 
ATOM   9343  C CA  . THR D 2 70  ? 32.02500  2.25100   -16.31000 1.000 91.74000  ? 634  THR D CA  1 
ATOM   9344  C C   . THR D 2 70  ? 31.44500  3.63100   -16.06900 1.000 96.68000  ? 634  THR D C   1 
ATOM   9345  O O   . THR D 2 70  ? 32.19900  4.55700   -15.75800 1.000 103.22000 ? 634  THR D O   1 
ATOM   9346  C CB  . THR D 2 70  ? 32.80700  2.23900   -17.63100 1.000 94.20000  ? 634  THR D CB  1 
ATOM   9347  O OG1 . THR D 2 70  ? 31.90100  2.41300   -18.73100 1.000 92.03000  ? 634  THR D OG1 1 
ATOM   9348  C CG2 . THR D 2 70  ? 33.58700  0.93800   -17.80100 1.000 89.36000  ? 634  THR D CG2 1 
ATOM   9349  N N   . LEU D 2 71  ? 30.12300  3.78600   -16.18600 1.000 97.96000  ? 635  LEU D N   1 
ATOM   9350  C CA  . LEU D 2 71  ? 29.45500  5.04300   -15.85000 1.000 100.75000 ? 635  LEU D CA  1 
ATOM   9351  C C   . LEU D 2 71  ? 29.39200  5.28100   -14.35500 1.000 106.45000 ? 635  LEU D C   1 
ATOM   9352  O O   . LEU D 2 71  ? 29.62600  6.40100   -13.89800 1.000 117.44000 ? 635  LEU D O   1 
ATOM   9353  C CB  . LEU D 2 71  ? 28.04500  5.09300   -16.42800 1.000 99.23000  ? 635  LEU D CB  1 
ATOM   9354  C CG  . LEU D 2 71  ? 27.19800  6.32400   -16.10400 1.000 96.09000  ? 635  LEU D CG  1 
ATOM   9355  C CD1 . LEU D 2 71  ? 26.31200  6.62000   -17.27900 1.000 94.71000  ? 635  LEU D CD1 1 
ATOM   9356  C CD2 . LEU D 2 71  ? 26.33600  6.07900   -14.86800 1.000 104.63000 ? 635  LEU D CD2 1 
ATOM   9357  N N   . ILE D 2 72  ? 29.02100  4.26800   -13.55700 1.000 102.66000 ? 636  ILE D N   1 
ATOM   9358  C CA  . ILE D 2 72  ? 28.82900  4.54400   -12.13700 1.000 106.61000 ? 636  ILE D CA  1 
ATOM   9359  C C   . ILE D 2 72  ? 30.09600  5.09200   -11.53900 1.000 116.30000 ? 636  ILE D C   1 
ATOM   9360  O O   . ILE D 2 72  ? 30.05400  5.91200   -10.61800 1.000 123.96000 ? 636  ILE D O   1 
ATOM   9361  C CB  . ILE D 2 72  ? 28.34600  3.31300   -11.33700 1.000 107.53000 ? 636  ILE D CB  1 
ATOM   9362  C CG1 . ILE D 2 72  ? 29.45000  2.24700   -11.33400 1.000 106.12000 ? 636  ILE D CG1 1 
ATOM   9363  C CG2 . ILE D 2 72  ? 26.98800  2.83000   -11.84600 1.000 96.55000  ? 636  ILE D CG2 1 
ATOM   9364  C CD1 . ILE D 2 72  ? 29.37100  1.28000   -10.18900 1.000 100.15000 ? 636  ILE D CD1 1 
ATOM   9365  N N   . LYS D 2 73  ? 31.23200  4.75700   -12.09900 1.000 118.77000 ? 637  LYS D N   1 
ATOM   9366  C CA  . LYS D 2 73  ? 32.43600  5.33900   -11.55900 1.000 123.65000 ? 637  LYS D CA  1 
ATOM   9367  C C   . LYS D 2 73  ? 32.41200  6.84100   -11.74900 1.000 127.31000 ? 637  LYS D C   1 
ATOM   9368  O O   . LYS D 2 73  ? 32.48900  7.59700   -10.78800 1.000 130.94000 ? 637  LYS D O   1 
ATOM   9369  C CB  . LYS D 2 73  ? 33.67600  4.73500   -12.19900 1.000 115.49000 ? 637  LYS D CB  1 
ATOM   9370  C CG  . LYS D 2 73  ? 33.93200  3.29500   -11.80100 1.000 121.08000 ? 637  LYS D CG  1 
ATOM   9371  C CD  . LYS D 2 73  ? 33.55800  2.34400   -12.92300 1.000 124.30000 ? 637  LYS D CD  1 
ATOM   9372  C CE  . LYS D 2 73  ? 34.73600  2.10800   -13.85500 1.000 116.20000 ? 637  LYS D CE  1 
ATOM   9373  N NZ  . LYS D 2 73  ? 34.76100  0.71600   -14.38100 1.000 123.93000 ? 637  LYS D NZ  1 
ATOM   9374  N N   . TYR D 2 74  ? 32.33100  7.26600   -13.00000 1.000 122.76000 ? 638  TYR D N   1 
ATOM   9375  C CA  . TYR D 2 74  ? 32.36400  8.68600   -13.29400 1.000 124.50000 ? 638  TYR D CA  1 
ATOM   9376  C C   . TYR D 2 74  ? 31.16200  9.34200   -12.71100 1.000 131.87000 ? 638  TYR D C   1 
ATOM   9377  O O   . TYR D 2 74  ? 31.14800  10.54800  -12.50000 1.000 136.20000 ? 638  TYR D O   1 
ATOM   9378  C CB  . TYR D 2 74  ? 32.41100  8.91500   -14.79000 1.000 125.94000 ? 638  TYR D CB  1 
ATOM   9379  C CG  . TYR D 2 74  ? 32.33900  10.35700  -15.21300 1.000 139.15000 ? 638  TYR D CG  1 
ATOM   9380  C CD1 . TYR D 2 74  ? 33.18700  11.30600  -14.66800 1.000 141.77000 ? 638  TYR D CD1 1 
ATOM   9381  C CD2 . TYR D 2 74  ? 31.42800  10.76800  -16.17200 1.000 139.00000 ? 638  TYR D CD2 1 
ATOM   9382  C CE1 . TYR D 2 74  ? 33.12300  12.62900  -15.05900 1.000 141.72000 ? 638  TYR D CE1 1 
ATOM   9383  C CE2 . TYR D 2 74  ? 31.35700  12.08600  -16.57200 1.000 141.85000 ? 638  TYR D CE2 1 
ATOM   9384  C CZ  . TYR D 2 74  ? 32.20600  13.01300  -16.01300 1.000 140.29000 ? 638  TYR D CZ  1 
ATOM   9385  O OH  . TYR D 2 74  ? 32.13400  14.32800  -16.41000 1.000 123.69000 ? 638  TYR D OH  1 
ATOM   9386  N N   . ARG D 2 75  ? 30.14100  8.56100   -12.41900 1.000 130.03000 ? 639  ARG D N   1 
ATOM   9387  C CA  . ARG D 2 75  ? 28.99300  9.13000   -11.75500 1.000 127.37000 ? 639  ARG D CA  1 
ATOM   9388  C C   . ARG D 2 75  ? 29.35400  9.21500   -10.30900 1.000 135.00000 ? 639  ARG D C   1 
ATOM   9389  O O   . ARG D 2 75  ? 28.50200  9.02500   -9.44600  1.000 136.12000 ? 639  ARG D O   1 
ATOM   9390  C CB  . ARG D 2 75  ? 27.76500  8.27100   -11.95200 1.000 118.96000 ? 639  ARG D CB  1 
ATOM   9391  C CG  . ARG D 2 75  ? 26.76100  8.89200   -12.89900 1.000 118.67000 ? 639  ARG D CG  1 
ATOM   9392  C CD  . ARG D 2 75  ? 25.40600  9.06300   -12.24200 1.000 115.36000 ? 639  ARG D CD  1 
ATOM   9393  N NE  . ARG D 2 75  ? 24.48300  8.00700   -12.63900 1.000 117.18000 ? 639  ARG D NE  1 
ATOM   9394  C CZ  . ARG D 2 75  ? 23.88100  7.94400   -13.82200 1.000 114.60000 ? 639  ARG D CZ  1 
ATOM   9395  N NH1 . ARG D 2 75  ? 24.10200  8.87600   -14.73600 1.000 107.83000 ? 639  ARG D NH1 1 
ATOM   9396  N NH2 . ARG D 2 75  ? 23.06100  6.93900   -14.09400 1.000 117.96000 ? 639  ARG D NH2 1 
ATOM   9397  N N   . GLU D 2 76  ? 30.61900  9.49700   -10.03700 1.000 139.77000 ? 640  GLU D N   1 
ATOM   9398  C CA  . GLU D 2 76  ? 31.09000  9.62200   -8.68400  1.000 142.38000 ? 640  GLU D CA  1 
ATOM   9399  C C   . GLU D 2 76  ? 32.51400  10.14600  -8.75400  1.000 145.16000 ? 640  GLU D C   1 
ATOM   9400  O O   . GLU D 2 76  ? 32.84100  10.96600  -9.61100  1.000 147.16000 ? 640  GLU D O   1 
ATOM   9401  C CB  . GLU D 2 76  ? 31.03600  8.27600   -7.97300  1.000 140.06000 ? 640  GLU D CB  1 
ATOM   9402  C CG  . GLU D 2 76  ? 32.38700  7.64200   -7.72000  1.000 139.14000 ? 640  GLU D CG  1 
ATOM   9403  C CD  . GLU D 2 76  ? 32.42400  6.19000   -8.13900  1.000 143.13000 ? 640  GLU D CD  1 
ATOM   9404  O OE1 . GLU D 2 76  ? 31.35200  5.55200   -8.17400  1.000 139.80000 ? 640  GLU D OE1 1 
ATOM   9405  O OE2 . GLU D 2 76  ? 33.52800  5.68900   -8.43500  1.000 145.47000 ? 640  GLU D OE2 1 
ATOM   9406  N N   . CYS D 2 95  ? 37.11500  8.84400   -17.98900 1.000 111.08000 ? 659  CYS D N   1 
ATOM   9407  C CA  . CYS D 2 95  ? 36.81700  7.57100   -18.64300 1.000 113.19000 ? 659  CYS D CA  1 
ATOM   9408  C C   . CYS D 2 95  ? 36.02200  7.81300   -19.91300 1.000 109.67000 ? 659  CYS D C   1 
ATOM   9409  O O   . CYS D 2 95  ? 35.42900  6.89000   -20.46000 1.000 107.78000 ? 659  CYS D O   1 
ATOM   9410  C CB  . CYS D 2 95  ? 36.03300  6.64600   -17.71600 1.000 117.83000 ? 659  CYS D CB  1 
ATOM   9411  S SG  . CYS D 2 95  ? 36.95400  6.06600   -16.26700 1.000 120.88000 ? 659  CYS D SG  1 
ATOM   9412  N N   . HIS D 2 96  ? 36.01700  9.07900   -20.34900 1.000 109.16000 ? 660  HIS D N   1 
ATOM   9413  C CA  . HIS D 2 96  ? 35.29900  9.49200   -21.54200 1.000 109.73000 ? 660  HIS D CA  1 
ATOM   9414  C C   . HIS D 2 96  ? 35.48100  8.52500   -22.69100 1.000 113.98000 ? 660  HIS D C   1 
ATOM   9415  O O   . HIS D 2 96  ? 34.50900  8.01900   -23.26500 1.000 108.26000 ? 660  HIS D O   1 
ATOM   9416  C CB  . HIS D 2 96  ? 35.75100  10.88500  -21.96500 1.000 104.60000 ? 660  HIS D CB  1 
ATOM   9417  C CG  . HIS D 2 96  ? 35.19100  11.97600  -21.12300 1.000 105.08000 ? 660  HIS D CG  1 
ATOM   9418  N ND1 . HIS D 2 96  ? 35.69400  13.26100  -21.14400 1.000 100.86000 ? 660  HIS D ND1 1 
ATOM   9419  C CD2 . HIS D 2 96  ? 34.14800  11.98900  -20.26100 1.000 110.79000 ? 660  HIS D CD2 1 
ATOM   9420  C CE1 . HIS D 2 96  ? 34.99600  14.01100  -20.31200 1.000 109.84000 ? 660  HIS D CE1 1 
ATOM   9421  N NE2 . HIS D 2 96  ? 34.05300  13.26600  -19.76800 1.000 112.80000 ? 660  HIS D NE2 1 
ATOM   9422  N N   . LYS D 2 97  ? 36.74300  8.27600   -23.05900 1.000 116.34000 ? 661  LYS D N   1 
ATOM   9423  C CA  . LYS D 2 97  ? 37.01100  7.48000   -24.23900 1.000 114.63000 ? 661  LYS D CA  1 
ATOM   9424  C C   . LYS D 2 97  ? 36.42000  6.08700   -24.08400 1.000 110.33000 ? 661  LYS D C   1 
ATOM   9425  O O   . LYS D 2 97  ? 35.86900  5.53600   -25.03800 1.000 110.02000 ? 661  LYS D O   1 
ATOM   9426  C CB  . LYS D 2 97  ? 38.51800  7.45800   -24.50800 1.000 122.53000 ? 661  LYS D CB  1 
ATOM   9427  C CG  . LYS D 2 97  ? 38.90900  7.05000   -25.91900 1.000 120.87000 ? 661  LYS D CG  1 
ATOM   9428  C CD  . LYS D 2 97  ? 40.39400  7.29100   -26.11800 1.000 120.30000 ? 661  LYS D CD  1 
ATOM   9429  C CE  . LYS D 2 97  ? 41.17700  6.19800   -25.42800 1.000 122.72000 ? 661  LYS D CE  1 
ATOM   9430  N NZ  . LYS D 2 97  ? 42.64800  6.24400   -25.64500 1.000 123.32000 ? 661  LYS D NZ  1 
ATOM   9431  N N   . ILE D 2 98  ? 36.46000  5.52400   -22.86600 1.000 107.71000 ? 662  ILE D N   1 
ATOM   9432  C CA  . ILE D 2 98  ? 35.75600  4.27200   -22.60900 1.000 109.26000 ? 662  ILE D CA  1 
ATOM   9433  C C   . ILE D 2 98  ? 34.26500  4.44100   -22.89000 1.000 102.54000 ? 662  ILE D C   1 
ATOM   9434  O O   . ILE D 2 98  ? 33.66000  3.68100   -23.65700 1.000 93.90000  ? 662  ILE D O   1 
ATOM   9435  C CB  . ILE D 2 98  ? 36.00200  3.79700   -21.16600 1.000 108.07000 ? 662  ILE D CB  1 
ATOM   9436  C CG1 . ILE D 2 98  ? 37.45400  3.87400   -20.74800 1.000 108.47000 ? 662  ILE D CG1 1 
ATOM   9437  C CG2 . ILE D 2 98  ? 35.65300  2.32600   -21.03700 1.000 105.44000 ? 662  ILE D CG2 1 
ATOM   9438  C CD1 . ILE D 2 98  ? 37.65000  3.48500   -19.28300 1.000 105.89000 ? 662  ILE D CD1 1 
ATOM   9439  N N   . LEU D 2 99  ? 33.65600  5.37800   -22.16100 1.000 103.30000 ? 663  LEU D N   1 
ATOM   9440  C CA  . LEU D 2 99  ? 32.19900  5.64100   -22.24200 1.000 94.38000  ? 663  LEU D CA  1 
ATOM   9441  C C   . LEU D 2 99  ? 31.82400  5.88600   -23.69600 1.000 98.26000  ? 663  LEU D C   1 
ATOM   9442  O O   . LEU D 2 99  ? 30.92900  5.21500   -24.22200 1.000 94.86000  ? 663  LEU D O   1 
ATOM   9443  C CB  . LEU D 2 99  ? 31.89800  6.88700   -21.41400 1.000 97.75000  ? 663  LEU D CB  1 
ATOM   9444  C CG  . LEU D 2 99  ? 31.36900  6.62500   -20.00900 1.000 101.53000 ? 663  LEU D CG  1 
ATOM   9445  C CD1 . LEU D 2 99  ? 32.24400  5.61600   -19.28600 1.000 103.02000 ? 663  LEU D CD1 1 
ATOM   9446  C CD2 . LEU D 2 99  ? 31.28300  7.91800   -19.22200 1.000 95.45000  ? 663  LEU D CD2 1 
ATOM   9447  N N   . ASN D 2 100 ? 32.54200  6.78900   -24.34700 1.000 98.20000  ? 664  ASN D N   1 
ATOM   9448  C CA  . ASN D 2 100 ? 32.19800  7.09200   -25.75600 1.000 98.04000  ? 664  ASN D CA  1 
ATOM   9449  C C   . ASN D 2 100 ? 32.60500  5.90100   -26.63000 1.000 96.81000  ? 664  ASN D C   1 
ATOM   9450  O O   . ASN D 2 100 ? 31.93000  5.64800   -27.63200 1.000 95.86000  ? 664  ASN D O   1 
ATOM   9451  C CB  . ASN D 2 100 ? 32.64900  8.50500   -26.13500 1.000 96.01000  ? 664  ASN D CB  1 
ATOM   9452  C CG  . ASN D 2 100 ? 33.22200  8.58900   -27.52500 1.000 92.56000  ? 664  ASN D CG  1 
ATOM   9453  O OD1 . ASN D 2 100 ? 32.73700  7.92700   -28.43300 1.000 93.63000  ? 664  ASN D OD1 1 
ATOM   9454  N ND2 . ASN D 2 100 ? 34.26000  9.38600   -27.69300 1.000 84.82000  ? 664  ASN D ND2 1 
ATOM   9455  N N   . SER D 2 101 ? 33.65900  5.18200   -26.24900 1.000 97.77000  ? 665  SER D N   1 
ATOM   9456  C CA  . SER D 2 101 ? 34.07100  3.97700   -27.00400 1.000 95.85000  ? 665  SER D CA  1 
ATOM   9457  C C   . SER D 2 101 ? 32.93800  2.96100   -26.91100 1.000 91.37000  ? 665  SER D C   1 
ATOM   9458  O O   . SER D 2 101 ? 32.57800  2.38100   -27.93000 1.000 89.38000  ? 665  SER D O   1 
ATOM   9459  C CB  . SER D 2 101 ? 35.33800  3.41600   -26.43300 1.000 99.35000  ? 665  SER D CB  1 
ATOM   9460  O OG  . SER D 2 101 ? 35.05600  2.48200   -25.40200 1.000 95.11000  ? 665  SER D OG  1 
ATOM   9461  N N   . HIS D 2 102 ? 32.39300  2.79400   -25.70900 1.000 92.67000  ? 666  HIS D N   1 
ATOM   9462  C CA  . HIS D 2 102 ? 31.28500  1.83800   -25.47400 1.000 86.48000  ? 666  HIS D CA  1 
ATOM   9463  C C   . HIS D 2 102 ? 30.07400  2.24500   -26.31500 1.000 86.20000  ? 666  HIS D C   1 
ATOM   9464  O O   . HIS D 2 102 ? 29.65800  1.43800   -27.14200 1.000 87.61000  ? 666  HIS D O   1 
ATOM   9465  C CB  . HIS D 2 102 ? 31.01600  1.70500   -23.97600 1.000 86.37000  ? 666  HIS D CB  1 
ATOM   9466  C CG  . HIS D 2 102 ? 32.03900  0.88700   -23.26400 1.000 82.40000  ? 666  HIS D CG  1 
ATOM   9467  N ND1 . HIS D 2 102 ? 32.61800  -0.22100  -23.82900 1.000 80.59000  ? 666  HIS D ND1 1 
ATOM   9468  C CD2 . HIS D 2 102 ? 32.58100  1.00300   -22.04000 1.000 84.56000  ? 666  HIS D CD2 1 
ATOM   9469  C CE1 . HIS D 2 102 ? 33.47500  -0.74600  -22.98600 1.000 74.48000  ? 666  HIS D CE1 1 
ATOM   9470  N NE2 . HIS D 2 102 ? 33.47200  -0.01700  -21.88800 1.000 80.43000  ? 666  HIS D NE2 1 
ATOM   9471  N N   . TYR D 2 103 ? 29.58900  3.47900   -26.18100 1.000 85.35000  ? 667  TYR D N   1 
ATOM   9472  C CA  . TYR D 2 103 ? 28.41300  3.90700   -26.98300 1.000 89.31000  ? 667  TYR D CA  1 
ATOM   9473  C C   . TYR D 2 103 ? 28.67300  3.76300   -28.48900 1.000 92.42000  ? 667  TYR D C   1 
ATOM   9474  O O   . TYR D 2 103 ? 27.77500  3.33700   -29.21100 1.000 88.10000  ? 667  TYR D O   1 
ATOM   9475  C CB  . TYR D 2 103 ? 27.94400  5.31800   -26.62100 1.000 94.23000  ? 667  TYR D CB  1 
ATOM   9476  C CG  . TYR D 2 103 ? 26.55000  5.60700   -27.11900 1.000 105.65000 ? 667  TYR D CG  1 
ATOM   9477  C CD1 . TYR D 2 103 ? 26.22300  5.39000   -28.44500 1.000 104.62000 ? 667  TYR D CD1 1 
ATOM   9478  C CD2 . TYR D 2 103 ? 25.54600  6.03600   -26.27400 1.000 103.48000 ? 667  TYR D CD2 1 
ATOM   9479  C CE1 . TYR D 2 103 ? 24.94900  5.59300   -28.93400 1.000 102.54000 ? 667  TYR D CE1 1 
ATOM   9480  C CE2 . TYR D 2 103 ? 24.26400  6.25600   -26.74800 1.000 110.54000 ? 667  TYR D CE2 1 
ATOM   9481  C CZ  . TYR D 2 103 ? 23.96400  6.02500   -28.07700 1.000 110.71000 ? 667  TYR D CZ  1 
ATOM   9482  O OH  . TYR D 2 103 ? 22.71400  6.22200   -28.57300 1.000 124.18000 ? 667  TYR D OH  1 
ATOM   9483  N N   . ILE D 2 104 ? 29.87000  4.09100   -28.96500 1.000 90.33000  ? 668  ILE D N   1 
ATOM   9484  C CA  . ILE D 2 104 ? 30.11800  3.98000   -30.43000 1.000 94.11000  ? 668  ILE D CA  1 
ATOM   9485  C C   . ILE D 2 104 ? 29.91900  2.53000   -30.86000 1.000 91.91000  ? 668  ILE D C   1 
ATOM   9486  O O   . ILE D 2 104 ? 29.28200  2.30400   -31.90100 1.000 85.54000  ? 668  ILE D O   1 
ATOM   9487  C CB  . ILE D 2 104 ? 31.53500  4.45000   -30.79700 1.000 97.04000  ? 668  ILE D CB  1 
ATOM   9488  C CG1 . ILE D 2 104 ? 31.65300  5.97200   -30.81700 1.000 93.15000  ? 668  ILE D CG1 1 
ATOM   9489  C CG2 . ILE D 2 104 ? 31.94000  3.84000   -32.12900 1.000 93.50000  ? 668  ILE D CG2 1 
ATOM   9490  C CD1 . ILE D 2 104 ? 30.36700  6.67400   -30.50100 1.000 96.57000  ? 668  ILE D CD1 1 
ATOM   9491  N N   . GLU D 2 105 ? 30.47000  1.59300   -30.09000 1.000 89.26000  ? 669  GLU D N   1 
ATOM   9492  C CA  . GLU D 2 105 ? 30.33100  0.16200   -30.44700 1.000 86.95000  ? 669  GLU D CA  1 
ATOM   9493  C C   . GLU D 2 105 ? 28.85600  -0.22000  -30.34900 1.000 82.61000  ? 669  GLU D C   1 
ATOM   9494  O O   . GLU D 2 105 ? 28.42500  -1.07700  -31.12000 1.000 79.13000  ? 669  GLU D O   1 
ATOM   9495  C CB  . GLU D 2 105 ? 31.25700  -0.70400  -29.59900 1.000 83.39000  ? 669  GLU D CB  1 
ATOM   9496  C CG  . GLU D 2 105 ? 32.01800  -1.72600  -30.41800 1.000 83.48000  ? 669  GLU D CG  1 
ATOM   9497  C CD  . GLU D 2 105 ? 32.75900  -1.14400  -31.60400 1.000 85.36000  ? 669  GLU D CD  1 
ATOM   9498  O OE1 . GLU D 2 105 ? 33.36100  -0.07800  -31.43900 1.000 85.77000  ? 669  GLU D OE1 1 
ATOM   9499  O OE2 . GLU D 2 105 ? 32.72900  -1.75900  -32.67700 1.000 75.54000  ? 669  GLU D OE2 1 
ATOM   9500  N N   . MET D 2 106 ? 28.11900  0.42600   -29.45100 1.000 82.93000  ? 670  MET D N   1 
ATOM   9501  C CA  . MET D 2 106 ? 26.69500  0.13900   -29.33200 1.000 83.39000  ? 670  MET D CA  1 
ATOM   9502  C C   . MET D 2 106 ? 25.91200  0.53800   -30.59600 1.000 82.98000  ? 670  MET D C   1 
ATOM   9503  O O   . MET D 2 106 ? 25.15800  -0.28100  -31.13100 1.000 71.66000  ? 670  MET D O   1 
ATOM   9504  C CB  . MET D 2 106 ? 26.13300  0.81900   -28.07800 1.000 83.63000  ? 670  MET D CB  1 
ATOM   9505  C CG  . MET D 2 106 ? 24.68500  0.47200   -27.80600 1.000 75.51000  ? 670  MET D CG  1 
ATOM   9506  S SD  . MET D 2 106 ? 24.03300  1.15500   -26.28000 1.000 86.40000  ? 670  MET D SD  1 
ATOM   9507  C CE  . MET D 2 106 ? 23.83200  2.89000   -26.64300 1.000 91.49000  ? 670  MET D CE  1 
ATOM   9508  N N   . GLN D 2 107 ? 26.06600  1.77600   -31.11700 1.000 85.05000  ? 671  GLN D N   1 
ATOM   9509  C CA  . GLN D 2 107 ? 25.35800  2.07400   -32.37800 1.000 80.15000  ? 671  GLN D CA  1 
ATOM   9510  C C   . GLN D 2 107 ? 25.80900  1.13300   -33.47000 1.000 79.79000  ? 671  GLN D C   1 
ATOM   9511  O O   . GLN D 2 107 ? 25.01800  0.73400   -34.33000 1.000 82.56000  ? 671  GLN D O   1 
ATOM   9512  C CB  . GLN D 2 107 ? 25.52900  3.52200   -32.88900 1.000 81.44000  ? 671  GLN D CB  1 
ATOM   9513  C CG  . GLN D 2 107 ? 24.89700  4.59700   -32.05800 1.000 92.46000  ? 671  GLN D CG  1 
ATOM   9514  C CD  . GLN D 2 107 ? 23.57600  4.10600   -31.58700 1.000 93.67000  ? 671  GLN D CD  1 
ATOM   9515  O OE1 . GLN D 2 107 ? 23.41600  3.75600   -30.41800 1.000 100.43000 ? 671  GLN D OE1 1 
ATOM   9516  N NE2 . GLN D 2 107 ? 22.59800  4.04700   -32.50400 1.000 90.43000  ? 671  GLN D NE2 1 
ATOM   9517  N N   . LYS D 2 108 ? 27.09100  0.80800   -33.47700 1.000 80.23000  ? 672  LYS D N   1 
ATOM   9518  C CA  . LYS D 2 108 ? 27.60600  -0.00900  -34.55900 1.000 88.85000  ? 672  LYS D CA  1 
ATOM   9519  C C   . LYS D 2 108 ? 26.79000  -1.28400  -34.66900 1.000 87.17000  ? 672  LYS D C   1 
ATOM   9520  O O   . LYS D 2 108 ? 26.41700  -1.69900  -35.76500 1.000 86.85000  ? 672  LYS D O   1 
ATOM   9521  C CB  . LYS D 2 108 ? 29.09900  -0.28100  -34.34400 1.000 90.13000  ? 672  LYS D CB  1 
ATOM   9522  C CG  . LYS D 2 108 ? 29.93200  0.98100   -34.62200 1.000 90.07000  ? 672  LYS D CG  1 
ATOM   9523  C CD  . LYS D 2 108 ? 31.33800  0.95300   -34.01600 1.000 95.42000  ? 672  LYS D CD  1 
ATOM   9524  C CE  . LYS D 2 108 ? 32.37500  0.38000   -34.95700 1.000 97.10000  ? 672  LYS D CE  1 
ATOM   9525  N NZ  . LYS D 2 108 ? 32.23800  -1.09500  -35.07000 1.000 89.38000  ? 672  LYS D NZ  1 
ATOM   9526  N N   . ASN D 2 109 ? 26.39100  -1.84400  -33.53100 1.000 87.18000  ? 673  ASN D N   1 
ATOM   9527  C CA  . ASN D 2 109 ? 25.47700  -2.98100  -33.53800 1.000 83.70000  ? 673  ASN D CA  1 
ATOM   9528  C C   . ASN D 2 109 ? 24.04000  -2.53900  -33.80600 1.000 84.17000  ? 673  ASN D C   1 
ATOM   9529  O O   . ASN D 2 109 ? 23.33400  -3.15300  -34.61600 1.000 82.68000  ? 673  ASN D O   1 
ATOM   9530  C CB  . ASN D 2 109 ? 25.58600  -3.73400  -32.21000 1.000 77.52000  ? 673  ASN D CB  1 
ATOM   9531  C CG  . ASN D 2 109 ? 27.01400  -4.18400  -31.92300 1.000 78.20000  ? 673  ASN D CG  1 
ATOM   9532  O OD1 . ASN D 2 109 ? 27.58800  -3.84400  -30.89300 1.000 77.72000  ? 673  ASN D OD1 1 
ATOM   9533  N ND2 . ASN D 2 109 ? 27.60400  -4.93600  -32.86100 1.000 75.83000  ? 673  ASN D ND2 1 
ATOM   9534  N N   . LEU D 2 110 ? 23.58700  -1.46800  -33.13300 1.000 82.15000  ? 674  LEU D N   1 
ATOM   9535  C CA  . LEU D 2 110 ? 22.20200  -1.01600  -33.28300 1.000 82.39000  ? 674  LEU D CA  1 
ATOM   9536  C C   . LEU D 2 110 ? 21.88900  -0.63400  -34.72500 1.000 83.72000  ? 674  LEU D C   1 
ATOM   9537  O O   . LEU D 2 110 ? 20.83100  -1.00300  -35.25600 1.000 81.64000  ? 674  LEU D O   1 
ATOM   9538  C CB  . LEU D 2 110 ? 21.93200  0.16000   -32.34900 1.000 77.66000  ? 674  LEU D CB  1 
ATOM   9539  C CG  . LEU D 2 110 ? 21.97600  -0.13600  -30.85400 1.000 73.70000  ? 674  LEU D CG  1 
ATOM   9540  C CD1 . LEU D 2 110 ? 21.91700  1.15400   -30.07100 1.000 68.48000  ? 674  LEU D CD1 1 
ATOM   9541  C CD2 . LEU D 2 110 ? 20.84400  -1.06600  -30.43200 1.000 67.50000  ? 674  LEU D CD2 1 
ATOM   9542  N N   . GLY D 2 111 ? 22.80000  0.09300   -35.38000 1.000 86.90000  ? 675  GLY D N   1 
ATOM   9543  C CA  . GLY D 2 111 ? 22.60400  0.39600   -36.78500 1.000 80.44000  ? 675  GLY D CA  1 
ATOM   9544  C C   . GLY D 2 111 ? 22.50400  -0.85200  -37.64100 1.000 86.10000  ? 675  GLY D C   1 
ATOM   9545  O O   . GLY D 2 111 ? 21.91300  -0.82100  -38.72600 1.000 89.74000  ? 675  GLY D O   1 
ATOM   9546  N N   . ASN D 2 112 ? 23.07200  -1.96800  -37.16700 1.000 86.35000  ? 676  ASN D N   1 
ATOM   9547  C CA  . ASN D 2 112 ? 22.97800  -3.24500  -37.85300 1.000 88.56000  ? 676  ASN D CA  1 
ATOM   9548  C C   . ASN D 2 112 ? 21.77100  -4.06900  -37.42900 1.000 92.30000  ? 676  ASN D C   1 
ATOM   9549  O O   . ASN D 2 112 ? 21.64500  -5.21200  -37.88100 1.000 87.97000  ? 676  ASN D O   1 
ATOM   9550  C CB  . ASN D 2 112 ? 24.26200  -4.05100  -37.61100 1.000 94.65000  ? 676  ASN D CB  1 
ATOM   9551  C CG  . ASN D 2 112 ? 25.47000  -3.48200  -38.32500 1.000 98.51000  ? 676  ASN D CG  1 
ATOM   9552  O OD1 . ASN D 2 112 ? 25.42700  -3.18200  -39.51800 1.000 106.00000 ? 676  ASN D OD1 1 
ATOM   9553  N ND2 . ASN D 2 112 ? 26.55800  -3.30100  -37.57600 1.000 97.17000  ? 676  ASN D ND2 1 
ATOM   9554  N N   . LEU D 2 113 ? 20.91200  -3.54200  -36.55600 1.000 92.02000  ? 677  LEU D N   1 
ATOM   9555  C CA  . LEU D 2 113 ? 19.62900  -4.20300  -36.27500 1.000 87.47000  ? 677  LEU D CA  1 
ATOM   9556  C C   . LEU D 2 113 ? 18.57500  -3.71600  -37.27800 1.000 90.55000  ? 677  LEU D C   1 
ATOM   9557  O O   . LEU D 2 113 ? 18.16900  -2.55200  -37.26500 1.000 91.52000  ? 677  LEU D O   1 
ATOM   9558  C CB  . LEU D 2 113 ? 19.13100  -3.95300  -34.84600 1.000 84.93000  ? 677  LEU D CB  1 
ATOM   9559  C CG  . LEU D 2 113 ? 19.65100  -4.72600  -33.61500 1.000 73.34000  ? 677  LEU D CG  1 
ATOM   9560  C CD1 . LEU D 2 113 ? 20.00400  -6.19000  -33.92700 1.000 62.16000  ? 677  LEU D CD1 1 
ATOM   9561  C CD2 . LEU D 2 113 ? 20.70300  -4.03200  -32.73800 1.000 68.28000  ? 677  LEU D CD2 1 
HETATM 9562  C C1  . GOL E 3 .   ? 1.75000   -68.76000 -32.58500 1.000 44.31000  ? 701  GOL A C1  1 
HETATM 9563  O O1  . GOL E 3 .   ? 1.82300   -68.00900 -33.73600 1.000 46.17000  ? 701  GOL A O1  1 
HETATM 9564  C C2  . GOL E 3 .   ? 2.93300   -68.28200 -31.82600 1.000 45.13000  ? 701  GOL A C2  1 
HETATM 9565  O O2  . GOL E 3 .   ? 3.22700   -67.00300 -32.24000 1.000 46.39000  ? 701  GOL A O2  1 
HETATM 9566  C C3  . GOL E 3 .   ? 2.51400   -68.35400 -30.32200 1.000 57.75000  ? 701  GOL A C3  1 
HETATM 9567  O O3  . GOL E 3 .   ? 3.25300   -69.37100 -29.69300 1.000 56.65000  ? 701  GOL A O3  1 
HETATM 9568  C C1  . GOL F 3 .   ? -13.19500 -60.56400 -12.83200 1.000 55.53000  ? 702  GOL A C1  1 
HETATM 9569  O O1  . GOL F 3 .   ? -12.48700 -61.68700 -12.37700 1.000 57.10000  ? 702  GOL A O1  1 
HETATM 9570  C C2  . GOL F 3 .   ? -13.20100 -60.61900 -14.37500 1.000 56.87000  ? 702  GOL A C2  1 
HETATM 9571  O O2  . GOL F 3 .   ? -14.00200 -61.65600 -14.88100 1.000 49.77000  ? 702  GOL A O2  1 
HETATM 9572  C C3  . GOL F 3 .   ? -13.66500 -59.21300 -14.82700 1.000 52.23000  ? 702  GOL A C3  1 
HETATM 9573  O O3  . GOL F 3 .   ? -13.76700 -59.26300 -16.24100 1.000 58.94000  ? 702  GOL A O3  1 
HETATM 9574  C C1  . GOL G 3 .   ? -10.92800 -60.14500 -23.22100 1.000 59.31000  ? 703  GOL A C1  1 
HETATM 9575  O O1  . GOL G 3 .   ? -11.86900 -61.11700 -22.89400 1.000 52.45000  ? 703  GOL A O1  1 
HETATM 9576  C C2  . GOL G 3 .   ? -11.10100 -59.83400 -24.73700 1.000 47.57000  ? 703  GOL A C2  1 
HETATM 9577  O O2  . GOL G 3 .   ? -11.98200 -58.75500 -24.96900 1.000 46.28000  ? 703  GOL A O2  1 
HETATM 9578  C C3  . GOL G 3 .   ? -9.63500  -59.66800 -25.38100 1.000 53.79000  ? 703  GOL A C3  1 
HETATM 9579  O O3  . GOL G 3 .   ? -8.66900  -59.23600 -24.42100 1.000 44.99000  ? 703  GOL A O3  1 
HETATM 9580  C C1  . GOL H 3 .   ? -11.46800 -55.94600 -13.43900 1.000 55.26000  ? 704  GOL A C1  1 
HETATM 9581  O O1  . GOL H 3 .   ? -11.39600 -55.38200 -14.71300 1.000 54.54000  ? 704  GOL A O1  1 
HETATM 9582  C C2  . GOL H 3 .   ? -11.08500 -54.82900 -12.41300 1.000 59.62000  ? 704  GOL A C2  1 
HETATM 9583  O O2  . GOL H 3 .   ? -12.13000 -54.57800 -11.50000 1.000 56.96000  ? 704  GOL A O2  1 
HETATM 9584  C C3  . GOL H 3 .   ? -9.78800  -55.35700 -11.71000 1.000 65.04000  ? 704  GOL A C3  1 
HETATM 9585  O O3  . GOL H 3 .   ? -9.02000  -54.24600 -11.35600 1.000 66.59000  ? 704  GOL A O3  1 
HETATM 9586  C C1  . GOL I 3 .   ? 58.37500  -22.03600 -15.98500 1.000 62.57000  ? 701  GOL B C1  1 
HETATM 9587  O O1  . GOL I 3 .   ? 58.12200  -22.03600 -17.36100 1.000 58.27000  ? 701  GOL B O1  1 
HETATM 9588  C C2  . GOL I 3 .   ? 57.34700  -22.99300 -15.36800 1.000 47.02000  ? 701  GOL B C2  1 
HETATM 9589  O O2  . GOL I 3 .   ? 57.72400  -23.45200 -14.12700 1.000 52.61000  ? 701  GOL B O2  1 
HETATM 9590  C C3  . GOL I 3 .   ? 56.11000  -22.17000 -15.24400 1.000 45.17000  ? 701  GOL B C3  1 
HETATM 9591  O O3  . GOL I 3 .   ? 55.49800  -22.69600 -14.13400 1.000 49.76000  ? 701  GOL B O3  1 
HETATM 9592  C C1  . GOL J 3 .   ? 50.82000  -38.63700 -31.40000 1.000 57.16000  ? 702  GOL B C1  1 
HETATM 9593  O O1  . GOL J 3 .   ? 50.97700  -38.66500 -32.81100 1.000 57.02000  ? 702  GOL B O1  1 
HETATM 9594  C C2  . GOL J 3 .   ? 52.14300  -39.16700 -30.73300 1.000 49.68000  ? 702  GOL B C2  1 
HETATM 9595  O O2  . GOL J 3 .   ? 52.21800  -38.83300 -29.37300 1.000 44.64000  ? 702  GOL B O2  1 
HETATM 9596  C C3  . GOL J 3 .   ? 52.12800  -40.71700 -30.97400 1.000 62.84000  ? 702  GOL B C3  1 
HETATM 9597  O O3  . GOL J 3 .   ? 53.11800  -41.30200 -30.16900 1.000 58.50000  ? 702  GOL B O3  1 
HETATM 9598  C C1  . GOL K 3 .   ? -18.40500 -27.84000 -35.33100 1.000 65.04000  ? 703  GOL B C1  1 
HETATM 9599  O O1  . GOL K 3 .   ? -18.40500 -26.55500 -34.75900 1.000 71.29000  ? 703  GOL B O1  1 
HETATM 9600  C C2  . GOL K 3 .   ? -19.32500 -28.75800 -34.45700 1.000 59.48000  ? 703  GOL B C2  1 
HETATM 9601  O O2  . GOL K 3 .   ? -19.84200 -29.81900 -35.18000 1.000 69.99000  ? 703  GOL B O2  1 
HETATM 9602  C C3  . GOL K 3 .   ? -18.43700 -29.25700 -33.32300 1.000 57.14000  ? 703  GOL B C3  1 
HETATM 9603  O O3  . GOL K 3 .   ? -18.76200 -30.59900 -33.13500 1.000 44.63000  ? 703  GOL B O3  1 
HETATM 9604  C C1  . GOL L 3 .   ? 47.64200  -42.46900 -20.74300 1.000 48.85000  ? 704  GOL B C1  1 
HETATM 9605  O O1  . GOL L 3 .   ? 48.04900  -43.57400 -21.47200 1.000 61.93000  ? 704  GOL B O1  1 
HETATM 9606  C C2  . GOL L 3 .   ? 48.14200  -41.24200 -21.51100 1.000 52.75000  ? 704  GOL B C2  1 
HETATM 9607  O O2  . GOL L 3 .   ? 47.08400  -40.47300 -21.98900 1.000 51.26000  ? 704  GOL B O2  1 
HETATM 9608  C C3  . GOL L 3 .   ? 49.04800  -40.50300 -20.49200 1.000 47.53000  ? 704  GOL B C3  1 
HETATM 9609  O O3  . GOL L 3 .   ? 50.06400  -39.87300 -21.20800 1.000 42.87000  ? 704  GOL B O3  1 
HETATM 9610  C C1  . GOL M 3 .   ? -15.39900 -4.67500  -25.16800 1.000 82.89000  ? 1101 GOL C C1  1 
HETATM 9611  O O1  . GOL M 3 .   ? -15.78600 -4.39800  -26.47300 1.000 82.48000  ? 1101 GOL C O1  1 
HETATM 9612  C C2  . GOL M 3 .   ? -16.53800 -5.50400  -24.51700 1.000 83.15000  ? 1101 GOL C C2  1 
HETATM 9613  O O2  . GOL M 3 .   ? -16.23600 -5.86100  -23.21000 1.000 86.20000  ? 1101 GOL C O2  1 
HETATM 9614  C C3  . GOL M 3 .   ? -17.80500 -4.60600  -24.59300 1.000 86.18000  ? 1101 GOL C C3  1 
HETATM 9615  O O3  . GOL M 3 .   ? -18.82800 -5.27500  -23.90000 1.000 85.22000  ? 1101 GOL C O3  1 
HETATM 9616  C C1  . GOL N 3 .   ? 3.58000   -12.21200 2.27300   1.000 83.01000  ? 1102 GOL C C1  1 
HETATM 9617  O O1  . GOL N 3 .   ? 4.90200   -11.77600 2.35800   1.000 72.64000  ? 1102 GOL C O1  1 
HETATM 9618  C C2  . GOL N 3 .   ? 3.60900   -13.73100 1.95100   1.000 89.04000  ? 1102 GOL C C2  1 
HETATM 9619  O O2  . GOL N 3 .   ? 2.51300   -14.38900 2.49500   1.000 83.54000  ? 1102 GOL C O2  1 
HETATM 9620  C C3  . GOL N 3 .   ? 3.63500   -13.82100 0.39300   1.000 80.91000  ? 1102 GOL C C3  1 
HETATM 9621  O O3  . GOL N 3 .   ? 3.78400   -15.17300 0.06900   1.000 68.83000  ? 1102 GOL C O3  1 
HETATM 9622  O O   . HOH O 4 .   ? 36.19600  -10.15800 -23.61300 1.000 52.38000  ? 801  HOH A O   1 
HETATM 9623  O O   . HOH O 4 .   ? 4.05400   -48.45200 -33.53900 1.000 45.43000  ? 802  HOH A O   1 
HETATM 9624  O O   . HOH O 4 .   ? -13.22800 -55.27200 -9.61600  1.000 38.11000  ? 803  HOH A O   1 
HETATM 9625  O O   . HOH O 4 .   ? 13.94900  -42.59300 0.61500   1.000 49.80000  ? 804  HOH A O   1 
HETATM 9626  O O   . HOH O 4 .   ? -32.84100 -58.97500 -24.85600 1.000 42.74000  ? 805  HOH A O   1 
HETATM 9627  O O   . HOH O 4 .   ? -17.07700 -44.80200 -20.09200 1.000 33.95000  ? 806  HOH A O   1 
HETATM 9628  O O   . HOH O 4 .   ? -26.43600 -77.98800 -2.12600  1.000 46.35000  ? 807  HOH A O   1 
HETATM 9629  O O   . HOH O 4 .   ? -7.91500  -71.37900 -43.01700 1.000 51.75000  ? 808  HOH A O   1 
HETATM 9630  O O   . HOH O 4 .   ? -22.95800 -48.82200 6.12900   1.000 38.22000  ? 809  HOH A O   1 
HETATM 9631  O O   . HOH O 4 .   ? -20.14500 -61.05600 -25.25700 1.000 34.17000  ? 810  HOH A O   1 
HETATM 9632  O O   . HOH O 4 .   ? -4.67000  -48.37600 -14.76800 1.000 50.27000  ? 811  HOH A O   1 
HETATM 9633  O O   . HOH O 4 .   ? -1.51900  -44.01200 -31.38900 1.000 33.24000  ? 812  HOH A O   1 
HETATM 9634  O O   . HOH O 4 .   ? -20.57700 -59.69500 -44.92600 1.000 67.53000  ? 813  HOH A O   1 
HETATM 9635  O O   . HOH O 4 .   ? -16.73300 -68.78700 -14.22200 1.000 38.33000  ? 814  HOH A O   1 
HETATM 9636  O O   . HOH O 4 .   ? -6.61300  -49.95700 -8.90300  1.000 38.58000  ? 815  HOH A O   1 
HETATM 9637  O O   . HOH O 4 .   ? -16.70900 -55.89400 -18.96900 1.000 32.02000  ? 816  HOH A O   1 
HETATM 9638  O O   . HOH O 4 .   ? 0.89100   -40.94600 -5.87500  1.000 55.07000  ? 817  HOH A O   1 
HETATM 9639  O O   . HOH O 4 .   ? -7.94100  -33.41800 -24.71600 1.000 37.71000  ? 818  HOH A O   1 
HETATM 9640  O O   . HOH O 4 .   ? -25.17300 -38.96900 -12.03800 1.000 42.48000  ? 819  HOH A O   1 
HETATM 9641  O O   . HOH O 4 .   ? 6.58000   -45.15400 1.21200   1.000 57.01000  ? 820  HOH A O   1 
HETATM 9642  O O   . HOH O 4 .   ? -9.06300  -50.80900 -2.31700  1.000 40.21000  ? 821  HOH A O   1 
HETATM 9643  O O   . HOH O 4 .   ? -5.51000  -48.48000 -35.17300 1.000 29.50000  ? 822  HOH A O   1 
HETATM 9644  O O   . HOH O 4 .   ? -11.22600 -54.43400 -51.17600 1.000 44.05000  ? 823  HOH A O   1 
HETATM 9645  O O   . HOH O 4 .   ? -26.19700 -67.20300 -31.90200 1.000 41.01000  ? 824  HOH A O   1 
HETATM 9646  O O   . HOH O 4 .   ? 43.32300  -22.30300 -5.97600  1.000 56.20000  ? 825  HOH A O   1 
HETATM 9647  O O   . HOH O 4 .   ? -29.36700 -46.67800 -15.63900 1.000 32.00000  ? 826  HOH A O   1 
HETATM 9648  O O   . HOH O 4 .   ? -10.79000 -54.73800 -7.30900  1.000 56.41000  ? 827  HOH A O   1 
HETATM 9649  O O   . HOH O 4 .   ? -25.32800 -46.87100 -22.08200 1.000 45.53000  ? 828  HOH A O   1 
HETATM 9650  O O   . HOH O 4 .   ? -23.28900 -48.83800 -23.53900 1.000 40.54000  ? 829  HOH A O   1 
HETATM 9651  O O   . HOH O 4 .   ? 6.86500   -40.64000 -9.24700  1.000 48.39000  ? 830  HOH A O   1 
HETATM 9652  O O   . HOH O 4 .   ? -31.32100 -53.16100 -16.43600 1.000 32.63000  ? 831  HOH A O   1 
HETATM 9653  O O   . HOH O 4 .   ? 7.94400   -32.99400 -11.05800 1.000 50.56000  ? 832  HOH A O   1 
HETATM 9654  O O   . HOH O 4 .   ? -24.47400 -64.09700 -0.63100  1.000 44.34000  ? 833  HOH A O   1 
HETATM 9655  O O   . HOH O 4 .   ? -11.87600 -56.83500 -52.22100 1.000 44.01000  ? 834  HOH A O   1 
HETATM 9656  O O   . HOH O 4 .   ? -18.33700 -69.66500 -21.04200 1.000 40.70000  ? 835  HOH A O   1 
HETATM 9657  O O   . HOH O 4 .   ? -27.75900 -64.45600 -0.87400  1.000 49.31000  ? 836  HOH A O   1 
HETATM 9658  O O   . HOH O 4 .   ? -29.92600 -57.69400 -27.68500 1.000 32.86000  ? 837  HOH A O   1 
HETATM 9659  O O   . HOH O 4 .   ? -30.95500 -63.72900 -2.07200  1.000 46.73000  ? 838  HOH A O   1 
HETATM 9660  O O   . HOH O 4 .   ? -2.49700  -68.44600 -35.85700 1.000 49.24000  ? 839  HOH A O   1 
HETATM 9661  O O   . HOH O 4 .   ? -36.41300 -50.17500 -10.51800 1.000 33.11000  ? 840  HOH A O   1 
HETATM 9662  O O   . HOH O 4 .   ? -29.12200 -72.17300 -9.38900  1.000 40.73000  ? 841  HOH A O   1 
HETATM 9663  O O   . HOH O 4 .   ? 3.75500   -56.94100 -42.58500 1.000 38.32000  ? 842  HOH A O   1 
HETATM 9664  O O   . HOH O 4 .   ? -9.88500  -47.40800 -26.49600 1.000 31.77000  ? 843  HOH A O   1 
HETATM 9665  O O   . HOH O 4 .   ? -26.08500 -74.04500 -22.60900 1.000 58.93000  ? 844  HOH A O   1 
HETATM 9666  O O   . HOH O 4 .   ? 1.79100   -60.26200 -49.62100 1.000 52.88000  ? 845  HOH A O   1 
HETATM 9667  O O   . HOH O 4 .   ? 19.74100  -13.78700 -7.41900  1.000 51.59000  ? 846  HOH A O   1 
HETATM 9668  O O   . HOH O 4 .   ? 16.69700  -25.90800 -17.02700 1.000 54.53000  ? 847  HOH A O   1 
HETATM 9669  O O   . HOH O 4 .   ? -8.99900  -35.87100 -18.33400 1.000 40.26000  ? 848  HOH A O   1 
HETATM 9670  O O   . HOH O 4 .   ? -19.71800 -56.09000 -17.11100 1.000 33.64000  ? 849  HOH A O   1 
HETATM 9671  O O   . HOH O 4 .   ? -17.73900 -67.14500 -43.21900 1.000 41.30000  ? 850  HOH A O   1 
HETATM 9672  O O   . HOH O 4 .   ? -3.30300  -69.06200 -48.55400 1.000 52.55000  ? 851  HOH A O   1 
HETATM 9673  O O   . HOH O 4 .   ? -0.71300  -44.41500 -20.70100 1.000 47.11000  ? 852  HOH A O   1 
HETATM 9674  O O   . HOH O 4 .   ? -22.33700 -71.82000 -23.68300 1.000 42.12000  ? 853  HOH A O   1 
HETATM 9675  O O   . HOH O 4 .   ? -7.85100  -54.66800 -53.53700 1.000 53.71000  ? 854  HOH A O   1 
HETATM 9676  O O   . HOH O 4 .   ? -9.94800  -41.74600 -23.73100 1.000 34.62000  ? 855  HOH A O   1 
HETATM 9677  O O   . HOH O 4 .   ? -23.75100 -63.87500 -18.79300 1.000 35.24000  ? 856  HOH A O   1 
HETATM 9678  O O   . HOH O 4 .   ? -3.09900  -38.32200 -13.84600 1.000 39.74000  ? 857  HOH A O   1 
HETATM 9679  O O   . HOH O 4 .   ? -14.26900 -46.51500 -45.06800 1.000 41.92000  ? 858  HOH A O   1 
HETATM 9680  O O   . HOH O 4 .   ? -14.44900 -61.33400 -52.37500 1.000 53.76000  ? 859  HOH A O   1 
HETATM 9681  O O   . HOH O 4 .   ? -15.65300 -54.21600 -2.70000  1.000 35.58000  ? 860  HOH A O   1 
HETATM 9682  O O   . HOH O 4 .   ? 17.11900  -42.65900 -7.54300  1.000 57.04000  ? 861  HOH A O   1 
HETATM 9683  O O   . HOH O 4 .   ? -13.60800 -44.26600 -24.90800 1.000 38.72000  ? 862  HOH A O   1 
HETATM 9684  O O   . HOH O 4 .   ? -23.77800 -61.51300 -20.47200 1.000 31.98000  ? 863  HOH A O   1 
HETATM 9685  O O   . HOH O 4 .   ? -20.68300 -65.72500 -30.64900 1.000 44.38000  ? 864  HOH A O   1 
HETATM 9686  O O   . HOH O 4 .   ? -24.10800 -54.04600 -39.93600 1.000 42.01000  ? 865  HOH A O   1 
HETATM 9687  O O   . HOH O 4 .   ? -19.01800 -74.85900 -11.07400 1.000 40.48000  ? 866  HOH A O   1 
HETATM 9688  O O   . HOH O 4 .   ? -13.22200 -65.92100 -31.08000 1.000 42.22000  ? 867  HOH A O   1 
HETATM 9689  O O   . HOH O 4 .   ? 13.68300  -24.51400 -9.95600  1.000 41.99000  ? 868  HOH A O   1 
HETATM 9690  O O   . HOH O 4 .   ? -17.79100 -54.59300 -4.59600  1.000 35.53000  ? 869  HOH A O   1 
HETATM 9691  O O   . HOH O 4 .   ? -20.26900 -70.74100 -14.05100 1.000 39.20000  ? 870  HOH A O   1 
HETATM 9692  O O   . HOH O 4 .   ? 9.331     -35.983   9.178     1.000 61.89000  ? 871  HOH A O   1 
HETATM 9693  O O   . HOH O 4 .   ? -1.73800  -42.30700 -7.77800  1.000 51.00000  ? 872  HOH A O   1 
HETATM 9694  O O   . HOH O 4 .   ? -17.55100 -33.36600 -17.07100 1.000 55.45000  ? 873  HOH A O   1 
HETATM 9695  O O   . HOH O 4 .   ? -10.00800 -40.08800 -35.78100 1.000 37.93000  ? 874  HOH A O   1 
HETATM 9696  O O   . HOH O 4 .   ? -17.22400 -71.21900 -17.53200 1.000 48.54000  ? 875  HOH A O   1 
HETATM 9697  O O   . HOH O 4 .   ? -14.36300 -45.23000 1.28700   1.000 36.94000  ? 876  HOH A O   1 
HETATM 9698  O O   . HOH O 4 .   ? -17.327   -52.672   -45.355   1.000 36.77000  ? 877  HOH A O   1 
HETATM 9699  O O   . HOH O 4 .   ? -7.84700  -49.24500 -47.59100 1.000 36.88000  ? 878  HOH A O   1 
HETATM 9700  O O   . HOH O 4 .   ? -27.69700 -46.64200 -8.46700  1.000 33.59000  ? 879  HOH A O   1 
HETATM 9701  O O   . HOH O 4 .   ? 2.01900   -44.91500 -22.14000 1.000 45.27000  ? 880  HOH A O   1 
HETATM 9702  O O   . HOH O 4 .   ? -28.52500 -57.98400 -29.98600 1.000 29.57000  ? 881  HOH A O   1 
HETATM 9703  O O   . HOH O 4 .   ? -17.773   -40.410   10.983    1.000 47.45000  ? 882  HOH A O   1 
HETATM 9704  O O   . HOH O 4 .   ? 18.39200  -18.39600 -15.05500 1.000 37.86000  ? 883  HOH A O   1 
HETATM 9705  O O   . HOH O 4 .   ? 20.72100  -17.06900 -13.64900 1.000 43.60000  ? 884  HOH A O   1 
HETATM 9706  O O   . HOH O 4 .   ? -6.93600  -60.60900 -28.76700 1.000 31.29000  ? 885  HOH A O   1 
HETATM 9707  O O   . HOH O 4 .   ? -15.28300 -34.59700 -5.85500  1.000 48.31000  ? 886  HOH A O   1 
HETATM 9708  O O   . HOH O 4 .   ? -22.22300 -62.98600 -24.91400 1.000 39.41000  ? 887  HOH A O   1 
HETATM 9709  O O   . HOH O 4 .   ? -33.87800 -52.17000 5.19700   1.000 60.07000  ? 888  HOH A O   1 
HETATM 9710  O O   . HOH O 4 .   ? -29.00300 -53.63600 -17.99300 1.000 24.72000  ? 889  HOH A O   1 
HETATM 9711  O O   . HOH O 4 .   ? -1.38500  -63.48900 -25.23900 1.000 44.43000  ? 890  HOH A O   1 
HETATM 9712  O O   . HOH O 4 .   ? 2.75600   -61.84100 -43.49000 1.000 44.79000  ? 891  HOH A O   1 
HETATM 9713  O O   . HOH O 4 .   ? -26.02400 -35.89400 -6.47200  1.000 42.94000  ? 892  HOH A O   1 
HETATM 9714  O O   . HOH O 4 .   ? -6.67200  -26.31400 -19.93100 1.000 56.12000  ? 893  HOH A O   1 
HETATM 9715  O O   . HOH O 4 .   ? -1.59200  -62.46600 -22.53300 1.000 38.43000  ? 894  HOH A O   1 
HETATM 9716  O O   . HOH O 4 .   ? -28.51700 -48.36400 4.81200   1.000 53.99000  ? 895  HOH A O   1 
HETATM 9717  O O   . HOH O 4 .   ? 1.76800   -42.66100 -12.98000 1.000 47.04000  ? 896  HOH A O   1 
HETATM 9718  O O   . HOH O 4 .   ? -13.76900 -65.04100 -28.53100 1.000 40.04000  ? 897  HOH A O   1 
HETATM 9719  O O   . HOH O 4 .   ? -40.653   -67.031   -11.149   1.000 46.84000  ? 898  HOH A O   1 
HETATM 9720  O O   . HOH O 4 .   ? -8.54200  -43.66000 -42.11100 1.000 44.62000  ? 899  HOH A O   1 
HETATM 9721  O O   . HOH O 4 .   ? -19.39300 -54.45700 -14.84100 1.000 30.54000  ? 900  HOH A O   1 
HETATM 9722  O O   . HOH O 4 .   ? -22.87000 -60.36900 5.92000   1.000 43.97000  ? 901  HOH A O   1 
HETATM 9723  O O   . HOH O 4 .   ? -30.52000 -55.09000 -27.65400 1.000 33.04000  ? 902  HOH A O   1 
HETATM 9724  O O   . HOH O 4 .   ? -1.56900  -69.34100 -27.63800 1.000 45.27000  ? 903  HOH A O   1 
HETATM 9725  O O   . HOH O 4 .   ? -31.31500 -47.81500 4.54500   1.000 57.93000  ? 904  HOH A O   1 
HETATM 9726  O O   . HOH O 4 .   ? -35.93300 -60.13900 -17.77500 1.000 39.12000  ? 905  HOH A O   1 
HETATM 9727  O O   . HOH O 4 .   ? -39.06100 -57.05100 -2.39700  1.000 43.72000  ? 906  HOH A O   1 
HETATM 9728  O O   . HOH O 4 .   ? -37.42100 -53.14800 -1.77300  1.000 38.66000  ? 907  HOH A O   1 
HETATM 9729  O O   . HOH O 4 .   ? -12.57500 -46.29200 -23.22000 1.000 34.72000  ? 908  HOH A O   1 
HETATM 9730  O O   . HOH O 4 .   ? 3.00800   -71.04100 -26.05000 1.000 62.21000  ? 909  HOH A O   1 
HETATM 9731  O O   . HOH O 4 .   ? -11.67400 -51.84800 4.02600   1.000 43.13000  ? 910  HOH A O   1 
HETATM 9732  O O   . HOH O 4 .   ? 21.16500  -34.32900 -6.89800  1.000 54.36000  ? 911  HOH A O   1 
HETATM 9733  O O   . HOH O 4 .   ? -33.33600 -52.56500 -18.48100 1.000 38.42000  ? 912  HOH A O   1 
HETATM 9734  O O   . HOH O 4 .   ? -32.37900 -62.06200 -24.15900 1.000 39.96000  ? 913  HOH A O   1 
HETATM 9735  O O   . HOH O 4 .   ? -19.86100 -40.19100 -28.28900 1.000 43.37000  ? 914  HOH A O   1 
HETATM 9736  O O   . HOH O 4 .   ? -19.90700 -40.39100 -18.22700 1.000 39.67000  ? 915  HOH A O   1 
HETATM 9737  O O   . HOH O 4 .   ? -26.76700 -76.61700 -18.26200 1.000 44.22000  ? 916  HOH A O   1 
HETATM 9738  O O   . HOH O 4 .   ? -15.55800 -35.01200 -9.29100  1.000 50.70000  ? 917  HOH A O   1 
HETATM 9739  O O   . HOH O 4 .   ? -36.28800 -47.90800 -4.94200  1.000 44.87000  ? 918  HOH A O   1 
HETATM 9740  O O   . HOH O 4 .   ? -2.98300  -65.18200 -46.26300 1.000 47.19000  ? 919  HOH A O   1 
HETATM 9741  O O   . HOH O 4 .   ? -23.804   -40.465   7.211     1.000 45.82000  ? 920  HOH A O   1 
HETATM 9742  O O   . HOH O 4 .   ? 17.83600  -37.29800 -8.28400  1.000 48.29000  ? 921  HOH A O   1 
HETATM 9743  O O   . HOH O 4 .   ? -9.198    -50.888   6.050     1.000 46.59000  ? 922  HOH A O   1 
HETATM 9744  O O   . HOH O 4 .   ? -25.06600 -47.53100 -29.68100 1.000 34.32000  ? 923  HOH A O   1 
HETATM 9745  O O   . HOH O 4 .   ? -27.39500 -38.74000 -9.11300  1.000 44.68000  ? 924  HOH A O   1 
HETATM 9746  O O   . HOH O 4 .   ? -21.71200 -67.08200 -10.83300 1.000 31.65000  ? 925  HOH A O   1 
HETATM 9747  O O   . HOH O 4 .   ? -14.40100 -62.28100 -45.43900 1.000 40.93000  ? 926  HOH A O   1 
HETATM 9748  O O   . HOH O 4 .   ? -2.16600  -67.33300 -40.62200 1.000 46.36000  ? 927  HOH A O   1 
HETATM 9749  O O   . HOH O 4 .   ? 0.90000   -49.05800 -22.55100 1.000 44.29000  ? 928  HOH A O   1 
HETATM 9750  O O   . HOH O 4 .   ? -20.27900 -46.49000 -14.96000 1.000 43.93000  ? 929  HOH A O   1 
HETATM 9751  O O   . HOH O 4 .   ? 6.32100   -51.89300 -34.36600 1.000 49.02000  ? 930  HOH A O   1 
HETATM 9752  O O   . HOH O 4 .   ? -30.47200 -51.65400 -25.02000 1.000 41.55000  ? 931  HOH A O   1 
HETATM 9753  O O   . HOH O 4 .   ? 4.10900   -67.15200 -37.14200 1.000 54.39000  ? 932  HOH A O   1 
HETATM 9754  O O   . HOH O 4 .   ? 17.83100  -15.37100 -15.04300 1.000 36.79000  ? 933  HOH A O   1 
HETATM 9755  O O   . HOH O 4 .   ? -15.89600 -36.29900 -1.45600  1.000 49.92000  ? 934  HOH A O   1 
HETATM 9756  O O   . HOH O 4 .   ? -13.00600 -61.49300 -9.49200  1.000 33.58000  ? 935  HOH A O   1 
HETATM 9757  O O   . HOH O 4 .   ? -14.20900 -71.13400 -39.54400 1.000 44.20000  ? 936  HOH A O   1 
HETATM 9758  O O   . HOH O 4 .   ? -22.03700 -46.12300 -35.74100 1.000 34.30000  ? 937  HOH A O   1 
HETATM 9759  O O   . HOH O 4 .   ? 8.60200   -21.57000 -20.85900 1.000 42.69000  ? 938  HOH A O   1 
HETATM 9760  O O   . HOH O 4 .   ? 1.36900   -47.03800 -44.29300 1.000 53.40000  ? 939  HOH A O   1 
HETATM 9761  O O   . HOH O 4 .   ? -12.68300 -61.27500 -19.96800 1.000 59.21000  ? 940  HOH A O   1 
HETATM 9762  O O   . HOH O 4 .   ? -23.51200 -54.91500 -42.54700 1.000 44.31000  ? 941  HOH A O   1 
HETATM 9763  O O   . HOH O 4 .   ? -13.21000 -65.87700 -5.86100  1.000 41.94000  ? 942  HOH A O   1 
HETATM 9764  O O   . HOH O 4 .   ? -33.32400 -50.97400 0.59200   1.000 44.25000  ? 943  HOH A O   1 
HETATM 9765  O O   . HOH O 4 .   ? -20.03400 -34.39600 -4.40900  1.000 69.03000  ? 944  HOH A O   1 
HETATM 9766  O O   . HOH O 4 .   ? 4.85400   -59.78800 -42.80500 1.000 45.64000  ? 945  HOH A O   1 
HETATM 9767  O O   . HOH O 4 .   ? 4.60800   -23.70300 -5.23200  1.000 47.97000  ? 946  HOH A O   1 
HETATM 9768  O O   . HOH O 4 .   ? -20.67400 -63.68200 -9.34900  1.000 26.00000  ? 947  HOH A O   1 
HETATM 9769  O O   . HOH O 4 .   ? -29.73300 -54.37300 -30.68600 1.000 45.88000  ? 948  HOH A O   1 
HETATM 9770  O O   . HOH O 4 .   ? -8.46400  -48.85700 -17.96600 1.000 40.11000  ? 949  HOH A O   1 
HETATM 9771  O O   . HOH O 4 .   ? 5.09900   -66.67800 -27.88900 1.000 42.38000  ? 950  HOH A O   1 
HETATM 9772  O O   . HOH O 4 .   ? -32.39500 -53.44400 -0.29000  1.000 40.27000  ? 951  HOH A O   1 
HETATM 9773  O O   . HOH O 4 .   ? 24.59000  -9.50700  -16.73500 1.000 49.88000  ? 952  HOH A O   1 
HETATM 9774  O O   . HOH O 4 .   ? -37.77200 -69.22200 -17.93500 1.000 46.39000  ? 953  HOH A O   1 
HETATM 9775  O O   . HOH O 4 .   ? -0.26100  -65.42300 -22.93100 1.000 49.73000  ? 954  HOH A O   1 
HETATM 9776  O O   . HOH O 4 .   ? -39.82400 -68.19700 -8.02000  1.000 57.36000  ? 955  HOH A O   1 
HETATM 9777  O O   . HOH O 4 .   ? -12.10500 -45.15000 -0.29900  1.000 34.60000  ? 956  HOH A O   1 
HETATM 9778  O O   . HOH O 4 .   ? 3.75700   -46.83900 -47.13700 1.000 62.86000  ? 957  HOH A O   1 
HETATM 9779  O O   . HOH O 4 .   ? 18.32800  -21.68800 -18.31700 1.000 53.36000  ? 958  HOH A O   1 
HETATM 9780  O O   . HOH O 4 .   ? 35.03300  -11.23000 -5.78800  1.000 53.25000  ? 959  HOH A O   1 
HETATM 9781  O O   . HOH O 4 .   ? 5.56000   -47.90100 -25.10100 1.000 47.15000  ? 960  HOH A O   1 
HETATM 9782  O O   . HOH O 4 .   ? 12.17000  -3.39100  -23.47200 1.000 68.62000  ? 961  HOH A O   1 
HETATM 9783  O O   . HOH O 4 .   ? -30.31200 -69.98000 -22.09800 1.000 42.89000  ? 962  HOH A O   1 
HETATM 9784  O O   . HOH O 4 .   ? 32.87200  -9.97700  -26.75300 1.000 44.82000  ? 963  HOH A O   1 
HETATM 9785  O O   . HOH O 4 .   ? -24.20900 -62.08800 -2.82900  1.000 43.43000  ? 964  HOH A O   1 
HETATM 9786  O O   . HOH O 4 .   ? -10.52900 -47.67200 5.05800   1.000 43.20000  ? 965  HOH A O   1 
HETATM 9787  O O   . HOH O 4 .   ? 4.43800   -25.53600 -2.70400  1.000 53.05000  ? 966  HOH A O   1 
HETATM 9788  O O   . HOH O 4 .   ? -9.72200  -51.18100 -16.00300 1.000 41.38000  ? 967  HOH A O   1 
HETATM 9789  O O   . HOH O 4 .   ? 7.97600   -11.26500 -14.92100 1.000 47.98000  ? 968  HOH A O   1 
HETATM 9790  O O   . HOH O 4 .   ? -15.24900 -58.41600 -25.93000 1.000 36.37000  ? 969  HOH A O   1 
HETATM 9791  O O   . HOH O 4 .   ? -2.29600  -34.40300 -14.62500 1.000 65.04000  ? 970  HOH A O   1 
HETATM 9792  O O   . HOH O 4 .   ? -17.95700 -38.95700 -30.16300 1.000 53.47000  ? 971  HOH A O   1 
HETATM 9793  O O   . HOH O 4 .   ? -19.18300 -67.42500 -24.08900 1.000 55.59000  ? 972  HOH A O   1 
HETATM 9794  O O   . HOH O 4 .   ? -13.43700 -63.07300 -6.10800  1.000 43.33000  ? 973  HOH A O   1 
HETATM 9795  O O   . HOH O 4 .   ? 10.29900  -8.60600  -20.89000 1.000 42.68000  ? 974  HOH A O   1 
HETATM 9796  O O   . HOH O 4 .   ? -0.45000  -47.38200 -46.71000 1.000 45.64000  ? 975  HOH A O   1 
HETATM 9797  O O   . HOH O 4 .   ? -29.181   -47.052   -23.508   1.000 43.60000  ? 976  HOH A O   1 
HETATM 9798  O O   . HOH O 4 .   ? 27.27600  -7.90300  -19.79600 1.000 54.12000  ? 977  HOH A O   1 
HETATM 9799  O O   . HOH O 4 .   ? -33.49200 -43.38500 -3.10200  1.000 54.48000  ? 978  HOH A O   1 
HETATM 9800  O O   . HOH O 4 .   ? -12.77300 -57.01600 -22.21100 1.000 46.35000  ? 979  HOH A O   1 
HETATM 9801  O O   . HOH O 4 .   ? -35.13000 -55.12500 -16.80600 1.000 46.04000  ? 980  HOH A O   1 
HETATM 9802  O O   . HOH O 4 .   ? 40.29300  -11.19400 -10.43500 1.000 48.33000  ? 981  HOH A O   1 
HETATM 9803  O O   . HOH O 4 .   ? -5.62800  -66.66200 -22.36400 1.000 47.54000  ? 982  HOH A O   1 
HETATM 9804  O O   . HOH O 4 .   ? -22.27400 -41.38300 -17.12100 1.000 52.41000  ? 983  HOH A O   1 
HETATM 9805  O O   . HOH O 4 .   ? -15.25200 -30.90200 -13.45400 1.000 78.23000  ? 984  HOH A O   1 
HETATM 9806  O O   . HOH O 4 .   ? 2.54500   -35.19300 -20.85200 1.000 54.48000  ? 985  HOH A O   1 
HETATM 9807  O O   . HOH O 4 .   ? -3.05300  -34.39100 2.57900   1.000 48.72000  ? 986  HOH A O   1 
HETATM 9808  O O   . HOH O 4 .   ? -32.86800 -48.49500 -0.40400  1.000 42.93000  ? 987  HOH A O   1 
HETATM 9809  O O   . HOH O 4 .   ? 0.01900   -36.86500 -13.74900 1.000 60.26000  ? 988  HOH A O   1 
HETATM 9810  O O   . HOH O 4 .   ? 27.03600  -28.04200 -18.33900 1.000 58.68000  ? 989  HOH A O   1 
HETATM 9811  O O   . HOH O 4 .   ? -26.38300 -52.25800 -40.84500 1.000 48.47000  ? 990  HOH A O   1 
HETATM 9812  O O   . HOH O 4 .   ? 1.88200   -37.19600 -26.83400 1.000 58.36000  ? 991  HOH A O   1 
HETATM 9813  O O   . HOH O 4 .   ? -11.82100 -67.16000 -8.27600  1.000 44.00000  ? 992  HOH A O   1 
HETATM 9814  O O   . HOH O 4 .   ? -27.29800 -54.26900 -43.12300 1.000 50.67000  ? 993  HOH A O   1 
HETATM 9815  O O   . HOH P 4 .   ? 60.37800  -19.18800 -42.76000 1.000 43.54000  ? 801  HOH B O   1 
HETATM 9816  O O   . HOH P 4 .   ? 74.93000  -24.52700 -50.78900 1.000 62.58000  ? 802  HOH B O   1 
HETATM 9817  O O   . HOH P 4 .   ? 47.50800  -22.68400 -27.10100 1.000 37.90000  ? 803  HOH B O   1 
HETATM 9818  O O   . HOH P 4 .   ? 55.27100  -22.29800 -22.49000 1.000 40.76000  ? 804  HOH B O   1 
HETATM 9819  O O   . HOH P 4 .   ? 33.75500  -32.47000 -13.92400 1.000 36.26000  ? 805  HOH B O   1 
HETATM 9820  O O   . HOH P 4 .   ? 78.70100  -34.08900 -37.26700 1.000 44.92000  ? 806  HOH B O   1 
HETATM 9821  O O   . HOH P 4 .   ? 65.19200  -50.65000 -31.33000 1.000 44.76000  ? 807  HOH B O   1 
HETATM 9822  O O   . HOH P 4 .   ? 71.31900  -42.21900 -35.63800 1.000 33.93000  ? 808  HOH B O   1 
HETATM 9823  O O   . HOH P 4 .   ? 14.78200  -37.50300 -35.62300 1.000 43.43000  ? 809  HOH B O   1 
HETATM 9824  O O   . HOH P 4 .   ? 75.32400  -47.97200 -27.03900 1.000 41.76000  ? 810  HOH B O   1 
HETATM 9825  O O   . HOH P 4 .   ? 18.66400  -34.89500 -39.27100 1.000 44.35000  ? 811  HOH B O   1 
HETATM 9826  O O   . HOH P 4 .   ? -14.89500 -36.31100 -30.77200 1.000 50.91000  ? 812  HOH B O   1 
HETATM 9827  O O   . HOH P 4 .   ? 58.46200  -42.09100 -19.24900 1.000 43.78000  ? 813  HOH B O   1 
HETATM 9828  O O   . HOH P 4 .   ? 69.29300  -31.98700 -21.11900 1.000 35.63000  ? 814  HOH B O   1 
HETATM 9829  O O   . HOH P 4 .   ? 57.35500  -20.88700 -36.53300 1.000 32.04000  ? 815  HOH B O   1 
HETATM 9830  O O   . HOH P 4 .   ? 55.54400  -15.27000 -42.21100 1.000 39.66000  ? 816  HOH B O   1 
HETATM 9831  O O   . HOH P 4 .   ? 50.76700  -33.50200 -41.72600 1.000 39.00000  ? 817  HOH B O   1 
HETATM 9832  O O   . HOH P 4 .   ? 65.87500  -45.03000 -21.63900 1.000 36.51000  ? 818  HOH B O   1 
HETATM 9833  O O   . HOH P 4 .   ? 60.08500  -35.13100 -50.99700 1.000 44.12000  ? 819  HOH B O   1 
HETATM 9834  O O   . HOH P 4 .   ? 35.87400  -20.78800 -26.36700 1.000 43.24000  ? 820  HOH B O   1 
HETATM 9835  O O   . HOH P 4 .   ? 39.08900  -34.78900 -10.25100 1.000 35.84000  ? 821  HOH B O   1 
HETATM 9836  O O   . HOH P 4 .   ? 60.42400  -47.03100 -27.89100 1.000 39.79000  ? 822  HOH B O   1 
HETATM 9837  O O   . HOH P 4 .   ? 76.17300  -44.88600 -31.44600 1.000 39.83000  ? 823  HOH B O   1 
HETATM 9838  O O   . HOH P 4 .   ? 35.99300  -29.92700 -33.73600 1.000 49.71000  ? 824  HOH B O   1 
HETATM 9839  O O   . HOH P 4 .   ? -20.29800 -36.75900 -33.71700 1.000 59.11000  ? 825  HOH B O   1 
HETATM 9840  O O   . HOH P 4 .   ? 55.13500  -23.24900 -7.78500  1.000 47.42000  ? 826  HOH B O   1 
HETATM 9841  O O   . HOH P 4 .   ? 55.19100  -32.53400 -28.08600 1.000 34.81000  ? 827  HOH B O   1 
HETATM 9842  O O   . HOH P 4 .   ? 54.49100  -25.34200 -50.79500 1.000 40.01000  ? 828  HOH B O   1 
HETATM 9843  O O   . HOH P 4 .   ? -6.74400  -36.18300 -35.04500 1.000 52.22000  ? 829  HOH B O   1 
HETATM 9844  O O   . HOH P 4 .   ? 68.34400  -43.07500 -44.31200 1.000 42.68000  ? 830  HOH B O   1 
HETATM 9845  O O   . HOH P 4 .   ? 61.01900  -40.93400 -15.34800 1.000 35.04000  ? 831  HOH B O   1 
HETATM 9846  O O   . HOH P 4 .   ? 45.58900  -29.54100 0.18400   1.000 42.12000  ? 832  HOH B O   1 
HETATM 9847  O O   . HOH P 4 .   ? 46.52100  -33.99800 -49.00300 1.000 42.80000  ? 833  HOH B O   1 
HETATM 9848  O O   . HOH P 4 .   ? 70.26900  -25.52800 -48.21200 1.000 42.71000  ? 834  HOH B O   1 
HETATM 9849  O O   . HOH P 4 .   ? 51.94600  -22.09500 -29.75200 1.000 43.73000  ? 835  HOH B O   1 
HETATM 9850  O O   . HOH P 4 .   ? 42.43900  -30.97300 -18.72200 1.000 29.17000  ? 836  HOH B O   1 
HETATM 9851  O O   . HOH P 4 .   ? 58.93900  -29.87000 -35.43300 1.000 36.78000  ? 837  HOH B O   1 
HETATM 9852  O O   . HOH P 4 .   ? 40.73300  -34.66600 -35.92300 1.000 48.47000  ? 838  HOH B O   1 
HETATM 9853  O O   . HOH P 4 .   ? 62.95600  -36.63400 -44.29600 1.000 45.73000  ? 839  HOH B O   1 
HETATM 9854  O O   . HOH P 4 .   ? -12.50100 -29.70100 -28.44100 1.000 46.00000  ? 840  HOH B O   1 
HETATM 9855  O O   . HOH P 4 .   ? 49.17900  -22.41100 -12.51000 1.000 42.32000  ? 841  HOH B O   1 
HETATM 9856  O O   . HOH P 4 .   ? 15.41000  -37.75500 -49.70400 1.000 53.70000  ? 842  HOH B O   1 
HETATM 9857  O O   . HOH P 4 .   ? 58.73300  -19.56200 -29.27700 1.000 35.00000  ? 843  HOH B O   1 
HETATM 9858  O O   . HOH P 4 .   ? 62.13600  -25.99700 -27.03800 1.000 30.67000  ? 844  HOH B O   1 
HETATM 9859  O O   . HOH P 4 .   ? 63.96200  -30.44100 -14.62800 1.000 47.03000  ? 845  HOH B O   1 
HETATM 9860  O O   . HOH P 4 .   ? 72.32900  -23.64500 -42.67500 1.000 52.04000  ? 846  HOH B O   1 
HETATM 9861  O O   . HOH P 4 .   ? 76.511    -43.859   -38.216   1.000 43.39000  ? 847  HOH B O   1 
HETATM 9862  O O   . HOH P 4 .   ? 9.76200   -18.42000 -31.60100 1.000 48.90000  ? 848  HOH B O   1 
HETATM 9863  O O   . HOH P 4 .   ? 38.84200  -32.62300 -24.22400 1.000 40.27000  ? 849  HOH B O   1 
HETATM 9864  O O   . HOH P 4 .   ? 33.51900  -49.35300 -6.74300  1.000 58.51000  ? 850  HOH B O   1 
HETATM 9865  O O   . HOH P 4 .   ? 0.29200   -23.28500 -30.07700 1.000 39.14000  ? 851  HOH B O   1 
HETATM 9866  O O   . HOH P 4 .   ? 2.98900   -23.32000 -28.54500 1.000 39.76000  ? 852  HOH B O   1 
HETATM 9867  O O   . HOH P 4 .   ? 62.54400  -37.33200 -26.38400 1.000 30.85000  ? 853  HOH B O   1 
HETATM 9868  O O   . HOH P 4 .   ? 68.84700  -33.54100 -42.81000 1.000 37.76000  ? 854  HOH B O   1 
HETATM 9869  O O   . HOH P 4 .   ? 69.32100  -27.63200 -29.54700 1.000 48.08000  ? 855  HOH B O   1 
HETATM 9870  O O   . HOH P 4 .   ? 60.71800  -47.96100 -37.45100 1.000 44.99000  ? 856  HOH B O   1 
HETATM 9871  O O   . HOH P 4 .   ? 54.74900  -41.54600 -46.44000 1.000 43.17000  ? 857  HOH B O   1 
HETATM 9872  O O   . HOH P 4 .   ? 56.23900  -13.32200 -37.44700 1.000 50.77000  ? 858  HOH B O   1 
HETATM 9873  O O   . HOH P 4 .   ? 50.18100  -37.16400 -21.21200 1.000 42.83000  ? 859  HOH B O   1 
HETATM 9874  O O   . HOH P 4 .   ? 54.63700  -45.01600 -15.26300 1.000 37.78000  ? 860  HOH B O   1 
HETATM 9875  O O   . HOH P 4 .   ? 39.49000  -25.33100 -20.71200 1.000 44.61000  ? 861  HOH B O   1 
HETATM 9876  O O   . HOH P 4 .   ? 40.69900  -32.55600 -3.92200  1.000 38.98000  ? 862  HOH B O   1 
HETATM 9877  O O   . HOH P 4 .   ? 45.13200  -37.59100 -24.95300 1.000 47.44000  ? 863  HOH B O   1 
HETATM 9878  O O   . HOH P 4 .   ? 32.84500  -30.41800 -36.59500 1.000 47.06000  ? 864  HOH B O   1 
HETATM 9879  O O   . HOH P 4 .   ? 17.19900  -19.45100 -38.12800 1.000 47.25000  ? 865  HOH B O   1 
HETATM 9880  O O   . HOH P 4 .   ? 47.67600  -23.96000 -24.70400 1.000 39.50000  ? 866  HOH B O   1 
HETATM 9881  O O   . HOH P 4 .   ? -12.70200 -25.43600 -16.44700 1.000 40.95000  ? 867  HOH B O   1 
HETATM 9882  O O   . HOH P 4 .   ? 80.650    -42.989   -44.278   1.000 40.67000  ? 868  HOH B O   1 
HETATM 9883  O O   . HOH P 4 .   ? 61.46000  -35.38500 -24.56600 1.000 31.18000  ? 869  HOH B O   1 
HETATM 9884  O O   . HOH P 4 .   ? 45.06800  -26.77400 -46.01200 1.000 42.80000  ? 870  HOH B O   1 
HETATM 9885  O O   . HOH P 4 .   ? 1.51700   -16.44200 -7.23000  1.000 57.34000  ? 871  HOH B O   1 
HETATM 9886  O O   . HOH P 4 .   ? 45.61500  -33.78800 1.99300   1.000 39.76000  ? 872  HOH B O   1 
HETATM 9887  O O   . HOH P 4 .   ? 12.13900  -23.34700 -30.29000 1.000 39.71000  ? 873  HOH B O   1 
HETATM 9888  O O   . HOH P 4 .   ? 43.81600  -55.23300 -10.53700 1.000 54.20000  ? 874  HOH B O   1 
HETATM 9889  O O   . HOH P 4 .   ? 67.90000  -24.61400 -29.15200 1.000 37.17000  ? 875  HOH B O   1 
HETATM 9890  O O   . HOH P 4 .   ? 51.16900  -23.49400 -22.58500 1.000 50.58000  ? 876  HOH B O   1 
HETATM 9891  O O   . HOH P 4 .   ? 68.98300  -21.70300 -43.18200 1.000 41.72000  ? 877  HOH B O   1 
HETATM 9892  O O   . HOH P 4 .   ? 60.65800  -45.59400 -24.30400 1.000 41.98000  ? 878  HOH B O   1 
HETATM 9893  O O   . HOH P 4 .   ? 68.20700  -36.01100 -46.53900 1.000 44.36000  ? 879  HOH B O   1 
HETATM 9894  O O   . HOH P 4 .   ? 32.87200  -38.44100 -0.76800  1.000 39.63000  ? 880  HOH B O   1 
HETATM 9895  O O   . HOH P 4 .   ? 47.04000  -43.53700 -17.83000 1.000 37.55000  ? 881  HOH B O   1 
HETATM 9896  O O   . HOH P 4 .   ? 55.86500  -22.37700 -18.99700 1.000 51.27000  ? 882  HOH B O   1 
HETATM 9897  O O   . HOH P 4 .   ? 66.85500  -19.56300 -34.41900 1.000 34.92000  ? 883  HOH B O   1 
HETATM 9898  O O   . HOH P 4 .   ? 80.85600  -44.00800 -28.49300 1.000 41.47000  ? 884  HOH B O   1 
HETATM 9899  O O   . HOH P 4 .   ? 64.76900  -29.37300 -16.70100 1.000 35.85000  ? 885  HOH B O   1 
HETATM 9900  O O   . HOH P 4 .   ? 43.10500  -26.94100 -49.47800 1.000 48.89000  ? 886  HOH B O   1 
HETATM 9901  O O   . HOH P 4 .   ? 63.12600  -45.12200 -31.27800 1.000 37.48000  ? 887  HOH B O   1 
HETATM 9902  O O   . HOH P 4 .   ? 23.75600  -22.09700 -47.18100 1.000 45.61000  ? 888  HOH B O   1 
HETATM 9903  O O   . HOH P 4 .   ? 3.51400   -16.84300 -30.51900 1.000 43.69000  ? 889  HOH B O   1 
HETATM 9904  O O   . HOH P 4 .   ? 11.91600  -23.84000 -32.82900 1.000 41.65000  ? 890  HOH B O   1 
HETATM 9905  O O   . HOH P 4 .   ? 71.56500  -19.78200 -36.98100 1.000 49.26000  ? 891  HOH B O   1 
HETATM 9906  O O   . HOH P 4 .   ? 32.92400  -19.96100 -19.77500 1.000 42.27000  ? 892  HOH B O   1 
HETATM 9907  O O   . HOH P 4 .   ? 75.84600  -25.64500 -39.47300 1.000 40.94000  ? 893  HOH B O   1 
HETATM 9908  O O   . HOH P 4 .   ? -15.09500 -34.31100 -42.62700 1.000 43.33000  ? 894  HOH B O   1 
HETATM 9909  O O   . HOH P 4 .   ? 46.39400  -31.98300 -52.32500 1.000 39.53000  ? 895  HOH B O   1 
HETATM 9910  O O   . HOH P 4 .   ? 45.61500  -16.81200 -37.32400 1.000 38.77000  ? 896  HOH B O   1 
HETATM 9911  O O   . HOH P 4 .   ? 77.89300  -37.29200 -22.88200 1.000 51.14000  ? 897  HOH B O   1 
HETATM 9912  O O   . HOH P 4 .   ? 39.05600  -50.95300 2.54700   1.000 45.58000  ? 898  HOH B O   1 
HETATM 9913  O O   . HOH P 4 .   ? 40.80900  -17.06400 -35.49600 1.000 36.41000  ? 899  HOH B O   1 
HETATM 9914  O O   . HOH P 4 .   ? 52.85800  -32.72800 -40.43300 1.000 37.14000  ? 900  HOH B O   1 
HETATM 9915  O O   . HOH P 4 .   ? 49.71100  -12.69600 -38.68300 1.000 51.85000  ? 901  HOH B O   1 
HETATM 9916  O O   . HOH P 4 .   ? 41.52700  -23.50000 -51.78800 1.000 52.16000  ? 902  HOH B O   1 
HETATM 9917  O O   . HOH P 4 .   ? 41.78900  -32.03100 -26.45900 1.000 47.52000  ? 903  HOH B O   1 
HETATM 9918  O O   . HOH P 4 .   ? 62.60800  -41.27500 -34.45500 1.000 29.62000  ? 904  HOH B O   1 
HETATM 9919  O O   . HOH P 4 .   ? -8.77000  -28.74000 -21.87600 1.000 51.09000  ? 905  HOH B O   1 
HETATM 9920  O O   . HOH P 4 .   ? 16.98900  -14.19100 -10.81900 1.000 48.23000  ? 906  HOH B O   1 
HETATM 9921  O O   . HOH P 4 .   ? 45.63000  -50.58500 -20.79700 1.000 43.08000  ? 907  HOH B O   1 
HETATM 9922  O O   . HOH P 4 .   ? 53.91900  -34.07300 -48.00100 1.000 41.25000  ? 908  HOH B O   1 
HETATM 9923  O O   . HOH P 4 .   ? 5.72100   -9.22400  -5.53400  1.000 58.33000  ? 909  HOH B O   1 
HETATM 9924  O O   . HOH P 4 .   ? 59.73400  -38.71800 -35.69900 1.000 30.81000  ? 910  HOH B O   1 
HETATM 9925  O O   . HOH P 4 .   ? 52.34300  -34.34300 -25.62500 1.000 34.14000  ? 911  HOH B O   1 
HETATM 9926  O O   . HOH P 4 .   ? 45.17400  -34.82800 -45.48800 1.000 47.35000  ? 912  HOH B O   1 
HETATM 9927  O O   . HOH P 4 .   ? 44.32400  -27.89800 -21.42300 1.000 40.05000  ? 913  HOH B O   1 
HETATM 9928  O O   . HOH P 4 .   ? 43.36200  -54.42600 -15.52600 1.000 42.10000  ? 914  HOH B O   1 
HETATM 9929  O O   . HOH P 4 .   ? 61.88400  -40.78700 -46.81300 1.000 51.88000  ? 915  HOH B O   1 
HETATM 9930  O O   . HOH P 4 .   ? 54.13100  -24.98500 -21.37700 1.000 43.64000  ? 916  HOH B O   1 
HETATM 9931  O O   . HOH P 4 .   ? 53.29500  -19.32900 -49.57300 1.000 46.53000  ? 917  HOH B O   1 
HETATM 9932  O O   . HOH P 4 .   ? 52.59700  -36.93200 -19.32900 1.000 39.49000  ? 918  HOH B O   1 
HETATM 9933  O O   . HOH P 4 .   ? 55.22700  -25.75900 -0.77900  1.000 53.72000  ? 919  HOH B O   1 
HETATM 9934  O O   . HOH P 4 .   ? 1.67900   -20.42400 -28.48900 1.000 48.27000  ? 920  HOH B O   1 
HETATM 9935  O O   . HOH P 4 .   ? 66.71200  -25.38400 -46.37600 1.000 41.07000  ? 921  HOH B O   1 
HETATM 9936  O O   . HOH P 4 .   ? 54.93200  -43.31800 -17.89800 1.000 41.11000  ? 922  HOH B O   1 
HETATM 9937  O O   . HOH P 4 .   ? 46.08800  -53.09600 -6.84700  1.000 46.10000  ? 923  HOH B O   1 
HETATM 9938  O O   . HOH P 4 .   ? 46.60300  -16.83500 -18.52600 1.000 48.50000  ? 924  HOH B O   1 
HETATM 9939  O O   . HOH P 4 .   ? 68.81900  -50.84400 -35.38000 1.000 52.73000  ? 925  HOH B O   1 
HETATM 9940  O O   . HOH P 4 .   ? 60.31300  -15.05700 -41.64500 1.000 51.82000  ? 926  HOH B O   1 
HETATM 9941  O O   . HOH P 4 .   ? 54.66400  -34.17500 -45.17100 1.000 40.53000  ? 927  HOH B O   1 
HETATM 9942  O O   . HOH P 4 .   ? 30.71500  -12.18700 -42.90800 1.000 66.82000  ? 928  HOH B O   1 
HETATM 9943  O O   . HOH P 4 .   ? 12.71100  -20.14400 -22.76200 1.000 43.27000  ? 929  HOH B O   1 
HETATM 9944  O O   . HOH P 4 .   ? 75.63900  -46.83300 -38.52500 1.000 48.49000  ? 930  HOH B O   1 
HETATM 9945  O O   . HOH P 4 .   ? 75.97100  -44.58900 -34.64500 1.000 35.02000  ? 931  HOH B O   1 
HETATM 9946  O O   . HOH P 4 .   ? 40.14200  -16.41500 -38.86600 1.000 45.05000  ? 932  HOH B O   1 
HETATM 9947  O O   . HOH P 4 .   ? 55.59200  -34.05700 -1.55700  1.000 45.35000  ? 933  HOH B O   1 
HETATM 9948  O O   . HOH P 4 .   ? 35.76000  -48.24700 -4.93500  1.000 56.30000  ? 934  HOH B O   1 
HETATM 9949  O O   . HOH P 4 .   ? 52.37000  -21.95700 -25.13800 1.000 37.86000  ? 935  HOH B O   1 
HETATM 9950  O O   . HOH P 4 .   ? 46.91100  -19.34100 -15.91000 1.000 58.73000  ? 936  HOH B O   1 
HETATM 9951  O O   . HOH P 4 .   ? 59.87900  -41.28400 -35.46000 1.000 34.18000  ? 937  HOH B O   1 
HETATM 9952  O O   . HOH P 4 .   ? 57.19000  -32.32900 -2.60400  1.000 34.53000  ? 938  HOH B O   1 
HETATM 9953  O O   . HOH P 4 .   ? 39.56300  -16.20700 -18.70600 1.000 53.08000  ? 939  HOH B O   1 
HETATM 9954  O O   . HOH P 4 .   ? 69.01200  -49.66700 -44.53600 1.000 52.27000  ? 940  HOH B O   1 
HETATM 9955  O O   . HOH P 4 .   ? 49.90800  -48.13400 10.25200  1.000 60.68000  ? 941  HOH B O   1 
HETATM 9956  O O   . HOH P 4 .   ? 71.37200  -36.29500 -23.08000 1.000 43.42000  ? 942  HOH B O   1 
HETATM 9957  O O   . HOH P 4 .   ? 54.81800  -44.66200 -39.63700 1.000 40.15000  ? 943  HOH B O   1 
HETATM 9958  O O   . HOH P 4 .   ? 46.77200  -14.88400 -34.92300 1.000 46.44000  ? 944  HOH B O   1 
HETATM 9959  O O   . HOH P 4 .   ? 44.67600  -35.42500 4.94100   1.000 46.76000  ? 945  HOH B O   1 
HETATM 9960  O O   . HOH P 4 .   ? 33.88900  -36.94700 -22.36000 1.000 58.55000  ? 946  HOH B O   1 
HETATM 9961  O O   . HOH P 4 .   ? 65.84600  -36.05600 -48.67100 1.000 47.43000  ? 947  HOH B O   1 
HETATM 9962  O O   . HOH P 4 .   ? 54.20900  -40.78100 -18.19800 1.000 41.64000  ? 948  HOH B O   1 
HETATM 9963  O O   . HOH P 4 .   ? 47.69600  -39.79200 5.64000   1.000 52.37000  ? 949  HOH B O   1 
HETATM 9964  O O   . HOH P 4 .   ? 49.29600  -35.47300 -35.05400 1.000 41.46000  ? 950  HOH B O   1 
HETATM 9965  O O   . HOH P 4 .   ? 52.45400  -37.28200 3.74000   1.000 55.26000  ? 951  HOH B O   1 
HETATM 9966  O O   . HOH P 4 .   ? 69.67400  -20.33400 -30.26700 1.000 45.02000  ? 952  HOH B O   1 
HETATM 9967  O O   . HOH P 4 .   ? 28.80200  -23.26600 -29.95100 1.000 60.48000  ? 953  HOH B O   1 
HETATM 9968  O O   . HOH P 4 .   ? 58.37000  -48.14400 -43.53200 1.000 54.71000  ? 954  HOH B O   1 
HETATM 9969  O O   . HOH P 4 .   ? 20.59400  -29.05700 -32.74100 1.000 49.20000  ? 955  HOH B O   1 
HETATM 9970  O O   . HOH P 4 .   ? 72.15200  -46.07500 -25.32300 1.000 49.67000  ? 956  HOH B O   1 
HETATM 9971  O O   . HOH P 4 .   ? 24.86700  -35.31300 -35.03800 1.000 46.38000  ? 957  HOH B O   1 
HETATM 9972  O O   . HOH P 4 .   ? 36.05400  -40.77000 1.42000   1.000 46.28000  ? 958  HOH B O   1 
HETATM 9973  O O   . HOH P 4 .   ? 57.02900  -38.99900 -20.23200 1.000 41.08000  ? 959  HOH B O   1 
HETATM 9974  O O   . HOH P 4 .   ? 52.09000  -14.29700 -35.83900 1.000 45.54000  ? 960  HOH B O   1 
HETATM 9975  O O   . HOH P 4 .   ? 68.57200  -23.45700 -47.12200 1.000 44.24000  ? 961  HOH B O   1 
HETATM 9976  O O   . HOH P 4 .   ? -15.00600 -26.80400 -37.49200 1.000 42.03000  ? 962  HOH B O   1 
HETATM 9977  O O   . HOH P 4 .   ? 66.54600  -36.95700 -44.26500 1.000 61.41000  ? 963  HOH B O   1 
HETATM 9978  O O   . HOH P 4 .   ? 54.32700  -46.16800 -24.75000 1.000 55.29000  ? 964  HOH B O   1 
HETATM 9979  O O   . HOH P 4 .   ? 53.54100  -42.21400 -39.29400 1.000 41.81000  ? 965  HOH B O   1 
HETATM 9980  O O   . HOH P 4 .   ? 64.74000  -44.74200 -43.53800 1.000 47.37000  ? 966  HOH B O   1 
HETATM 9981  O O   . HOH P 4 .   ? 7.85700   -11.48400 -28.50900 1.000 50.00000  ? 967  HOH B O   1 
HETATM 9982  O O   . HOH P 4 .   ? 29.72300  -40.09000 0.45600   1.000 57.11000  ? 968  HOH B O   1 
HETATM 9983  O O   . HOH P 4 .   ? 48.370    -22.516   2.185     1.000 32.67000  ? 969  HOH B O   1 
HETATM 9984  O O   . HOH P 4 .   ? 29.01800  -22.45400 -46.70300 1.000 46.68000  ? 970  HOH B O   1 
HETATM 9985  O O   . HOH P 4 .   ? 34.56200  -39.04100 1.17900   1.000 51.02000  ? 971  HOH B O   1 
HETATM 9986  O O   . HOH P 4 .   ? -7.53700  -19.38400 -26.58800 1.000 49.12000  ? 972  HOH B O   1 
HETATM 9987  O O   . HOH P 4 .   ? -20.91800 -36.05500 -28.92400 1.000 45.29000  ? 973  HOH B O   1 
HETATM 9988  O O   . HOH P 4 .   ? 52.66000  -41.26800 -35.57900 1.000 38.98000  ? 974  HOH B O   1 
HETATM 9989  O O   . HOH P 4 .   ? 15.46200  -42.49500 -40.35400 1.000 58.39000  ? 975  HOH B O   1 
HETATM 9990  O O   . HOH P 4 .   ? -4.22500  -27.37100 -22.39700 1.000 49.59000  ? 976  HOH B O   1 
HETATM 9991  O O   . HOH P 4 .   ? 53.91300  -44.13700 -31.89200 1.000 48.69000  ? 977  HOH B O   1 
HETATM 9992  O O   . HOH P 4 .   ? 82.34000  -40.65400 -46.37700 1.000 46.04000  ? 978  HOH B O   1 
HETATM 9993  O O   . HOH P 4 .   ? 36.29800  -25.63200 -44.60100 1.000 49.46000  ? 979  HOH B O   1 
HETATM 9994  O O   . HOH P 4 .   ? 30.36800  -19.42600 -46.79200 1.000 56.64000  ? 980  HOH B O   1 
HETATM 9995  O O   . HOH P 4 .   ? 59.05800  -20.07100 -24.12400 1.000 53.64000  ? 981  HOH B O   1 
HETATM 9996  O O   . HOH P 4 .   ? 72.51800  -38.30800 -6.93900  1.000 58.09000  ? 982  HOH B O   1 
HETATM 9997  O O   . HOH P 4 .   ? 45.84900  -35.68100 -37.37500 1.000 49.22000  ? 983  HOH B O   1 
HETATM 9998  O O   . HOH P 4 .   ? 29.96000  -24.71800 -47.04100 1.000 53.76000  ? 984  HOH B O   1 
HETATM 9999  O O   . HOH P 4 .   ? 70.32300  -26.70600 -51.42500 1.000 46.85000  ? 985  HOH B O   1 
HETATM 10000 O O   . HOH P 4 .   ? 71.75300  -39.20300 -22.19900 1.000 40.74000  ? 986  HOH B O   1 
HETATM 10001 O O   . HOH P 4 .   ? -17.00600 -31.02200 -26.93600 1.000 53.57000  ? 987  HOH B O   1 
HETATM 10002 O O   . HOH P 4 .   ? 37.39700  -39.74700 4.26800   1.000 51.81000  ? 988  HOH B O   1 
HETATM 10003 O O   . HOH P 4 .   ? 63.30100  -45.43600 -21.14200 1.000 34.42000  ? 989  HOH B O   1 
HETATM 10004 O O   . HOH P 4 .   ? 25.38000  -26.82600 -23.16800 1.000 48.90000  ? 990  HOH B O   1 
HETATM 10005 O O   . HOH P 4 .   ? 28.78400  -32.18400 -23.52000 1.000 45.73000  ? 991  HOH B O   1 
HETATM 10006 O O   . HOH P 4 .   ? 14.79000  -37.94500 -32.76300 1.000 51.43000  ? 992  HOH B O   1 
HETATM 10007 O O   . HOH P 4 .   ? 46.71700  -36.38600 -32.85700 1.000 52.09000  ? 993  HOH B O   1 
HETATM 10008 O O   . HOH P 4 .   ? 49.14600  -19.43600 -27.33800 1.000 39.76000  ? 994  HOH B O   1 
HETATM 10009 O O   . HOH P 4 .   ? 49.36400  -12.79000 -33.60600 1.000 47.65000  ? 995  HOH B O   1 
HETATM 10010 O O   . HOH P 4 .   ? 59.27900  -16.32500 -44.11700 1.000 52.35000  ? 996  HOH B O   1 
HETATM 10011 O O   . HOH P 4 .   ? -3.93900  -4.72500  -22.11400 1.000 112.35000 ? 997  HOH B O   1 
HETATM 10012 O O   . HOH P 4 .   ? -2.52100  -28.47900 -20.51200 1.000 54.42000  ? 998  HOH B O   1 
HETATM 10013 O O   . HOH P 4 .   ? 23.10300  -40.63700 -52.82500 1.000 52.27000  ? 999  HOH B O   1 
HETATM 10014 O O   . HOH Q 4 .   ? -34.83900 -17.80200 -31.73500 1.000 50.39000  ? 1201 HOH C O   1 
HETATM 10015 O O   . HOH Q 4 .   ? -28.38300 -18.69600 -27.89100 1.000 58.25000  ? 1202 HOH C O   1 
HETATM 10016 O O   . HOH Q 4 .   ? 18.30600  -34.56300 -9.37800  1.000 50.51000  ? 1203 HOH C O   1 
HETATM 10017 O O   . HOH Q 4 .   ? -0.56900  -23.13300 -5.06800  1.000 47.44000  ? 1204 HOH C O   1 
HETATM 10018 O O   . HOH Q 4 .   ? -8.15200  -24.00200 -12.59100 1.000 48.27000  ? 1205 HOH C O   1 
HETATM 10019 O O   . HOH Q 4 .   ? 22.55600  -33.21100 -5.11600  1.000 49.41000  ? 1206 HOH C O   1 
HETATM 10020 O O   . HOH Q 4 .   ? 27.25100  -27.08500 -5.12500  1.000 53.22000  ? 1207 HOH C O   1 
HETATM 10021 O O   . HOH Q 4 .   ? 11.99900  -29.68900 4.88100   1.000 58.02000  ? 1208 HOH C O   1 
HETATM 10022 O O   . HOH Q 4 .   ? 14.20000  -13.70000 -12.62400 1.000 51.29000  ? 1209 HOH C O   1 
HETATM 10023 O O   . HOH Q 4 .   ? 18.28800  -25.72400 3.63200   1.000 48.93000  ? 1210 HOH C O   1 
HETATM 10024 O O   . HOH Q 4 .   ? -15.61700 -21.10500 -29.87800 1.000 69.62000  ? 1211 HOH C O   1 
HETATM 10025 O O   . HOH Q 4 .   ? 7.33200   -16.54800 -3.24400  1.000 50.03000  ? 1212 HOH C O   1 
HETATM 10026 O O   . HOH Q 4 .   ? -37.43700 -13.93800 -42.29300 1.000 62.57000  ? 1213 HOH C O   1 
HETATM 10027 O O   . HOH Q 4 .   ? -8.47000  -6.90800  -9.66400  1.000 61.09000  ? 1214 HOH C O   1 
HETATM 10028 O O   . HOH R 4 .   ? 15.62000  -11.74100 -36.23400 1.000 47.71000  ? 701  HOH D O   1 
HETATM 10029 O O   . HOH R 4 .   ? 9.84100   -37.49600 -36.59500 1.000 46.87000  ? 702  HOH D O   1 
HETATM 10030 O O   . HOH R 4 .   ? 8.05000   -37.22600 -38.55000 1.000 40.54000  ? 703  HOH D O   1 
HETATM 10031 O O   . HOH R 4 .   ? 0.90800   -16.48900 -36.65700 1.000 45.96000  ? 704  HOH D O   1 
HETATM 10032 O O   . HOH R 4 .   ? 38.82000  11.02800  -16.70500 1.000 75.56000  ? 705  HOH D O   1 
HETATM 10033 O O   . HOH R 4 .   ? 8.47700   -37.28500 -41.25600 1.000 49.43000  ? 706  HOH D O   1 
HETATM 10034 O O   . HOH R 4 .   ? 1.78800   -18.91500 -32.24100 1.000 59.22000  ? 707  HOH D O   1 
HETATM 10035 O O   . HOH R 4 .   ? 28.03200  -15.08100 -25.19000 1.000 47.49000  ? 708  HOH D O   1 
HETATM 10036 O O   . HOH R 4 .   ? 0.16800   -34.84200 -39.09400 1.000 64.41000  ? 709  HOH D O   1 
HETATM 10037 O O   . HOH R 4 .   ? 11.35400  -15.19000 -40.97800 1.000 59.53000  ? 710  HOH D O   1 
HETATM 10038 O O   . HOH R 4 .   ? -12.62600 -26.15600 -42.63400 1.000 50.03000  ? 711  HOH D O   1 
HETATM 10039 O O   . HOH R 4 .   ? -11.81200 -24.00300 -40.71500 1.000 56.69000  ? 712  HOH D O   1 
# 
