data_9IPB
# 
_entry.id   9IPB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IPB         pdb_00009ipb 10.2210/pdb9ipb/pdb 
WWPDB D_1300049128 ?            ?                   
EMDB  EMD-60768    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IPB 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Local refinement structure of sEGFR and 528 Fv (from LH-type bispecific diabody Ex3) complex' 
_pdbx_database_related.db_id          EMD-60768 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yoshikazu.tanaka@tohoku.ac.jp 
_pdbx_contact_author.name_first         Yoshikazu 
_pdbx_contact_author.name_last          Tanaka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7893-3236 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sato, K.'     1 0009-0007-9952-4638 
'Uehara, S.'   2 ?                   
'Tsugita, A.'  3 ?                   
'Matsui, T.'   4 ?                   
'Asano, R.'    5 ?                   
'Makabe, K.'   6 ?                   
'Yokoyama, T.' 7 ?                   
'Tanaka, Y.'   8 ?                   
# 
_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 Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Bispecific antibody-antigen complex structures reveal activity enhancement by domain rearrangement' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sato, K.'     1  0009-0007-9952-4638 
primary 'Uehara, S.'   2  ?                   
primary 'Tsugita, A.'  3  ?                   
primary 'Ishii, M.'    4  ?                   
primary 'Ishiyama, S.' 5  ?                   
primary 'Maejima, A.'  6  ?                   
primary 'Nakahara, I.' 7  ?                   
primary 'Nazuka, M.'   8  ?                   
primary 'Matsui, T.'   9  ?                   
primary 'Christos, G.' 10 ?                   
primary 'Yokoyama, T.' 11 ?                   
primary 'Kumagai, I.'  12 ?                   
primary 'Makabe, K.'   13 ?                   
primary 'Asano, R.'    14 ?                   
primary 'Tanaka, Y.'   15 ?                   
# 
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 'Epidermal growth factor receptor'                                                        69496.062 1 2.7.10.1 ? 
? ? 
2 polymer     man '528 Fv from LH-type bispecific diabody Ex3'                                              26651.629 1 ?        
Y52W ? ? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2 ?        ? 
? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                                                  221.208   2 ?        ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1' 
# 
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 
;LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENL
QIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHL
GSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTC
PPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGE
FKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLE
IIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQ
VCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAH
YIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSHHHHHH
;
;LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENL
QIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHL
GSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTC
PPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGE
FKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLE
IIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQ
VCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAH
YIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSHHHHHH
;
A ? 
2 'polypeptide(L)' no no 
;QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYWMHWVRQAPGQGLEWMGNIWPGSGGTNYAEKFKNRVTMTRDTSISTAY
MELSRLRSDDTAVYYCARSGGPYFFDYWGQGTLVTVSSGGGGSGGGGSGGGGSGGGGSDIVMTQSPLSLPVTPGEPASIS
CRSSQNIVHNNGITYLEWYLQKPGQSPQLLIYKVSDRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCFQGSHIPPT
FGQGTKVEIK
;
;QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYWMHWVRQAPGQGLEWMGNIWPGSGGTNYAEKFKNRVTMTRDTSISTAY
MELSRLRSDDTAVYYCARSGGPYFFDYWGQGTLVTVSSGGGGSGGGGSGGGGSGGGGSDIVMTQSPLSLPVTPGEPASIS
CRSSQNIVHNNGITYLEWYLQKPGQSPQLLIYKVSDRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCFQGSHIPPT
FGQGTKVEIK
;
D ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   GLU n 
1 3   GLU n 
1 4   LYS n 
1 5   LYS n 
1 6   VAL n 
1 7   CYS n 
1 8   GLN n 
1 9   GLY n 
1 10  THR n 
1 11  SER n 
1 12  ASN n 
1 13  LYS n 
1 14  LEU n 
1 15  THR n 
1 16  GLN n 
1 17  LEU n 
1 18  GLY n 
1 19  THR n 
1 20  PHE n 
1 21  GLU n 
1 22  ASP n 
1 23  HIS n 
1 24  PHE n 
1 25  LEU n 
1 26  SER n 
1 27  LEU n 
1 28  GLN n 
1 29  ARG n 
1 30  MET n 
1 31  PHE n 
1 32  ASN n 
1 33  ASN n 
1 34  CYS n 
1 35  GLU n 
1 36  VAL n 
1 37  VAL n 
1 38  LEU n 
1 39  GLY n 
1 40  ASN n 
1 41  LEU n 
1 42  GLU n 
1 43  ILE n 
1 44  THR n 
1 45  TYR n 
1 46  VAL n 
1 47  GLN n 
1 48  ARG n 
1 49  ASN n 
1 50  TYR n 
1 51  ASP n 
1 52  LEU n 
1 53  SER n 
1 54  PHE n 
1 55  LEU n 
1 56  LYS n 
1 57  THR n 
1 58  ILE n 
1 59  GLN n 
1 60  GLU n 
1 61  VAL n 
1 62  ALA n 
1 63  GLY n 
1 64  TYR n 
1 65  VAL n 
1 66  LEU n 
1 67  ILE n 
1 68  ALA n 
1 69  LEU n 
1 70  ASN n 
1 71  THR n 
1 72  VAL n 
1 73  GLU n 
1 74  ARG n 
1 75  ILE n 
1 76  PRO n 
1 77  LEU n 
1 78  GLU n 
1 79  ASN n 
1 80  LEU n 
1 81  GLN n 
1 82  ILE n 
1 83  ILE n 
1 84  ARG n 
1 85  GLY n 
1 86  ASN n 
1 87  MET n 
1 88  TYR n 
1 89  TYR n 
1 90  GLU n 
1 91  ASN n 
1 92  SER n 
1 93  TYR n 
1 94  ALA n 
1 95  LEU n 
1 96  ALA n 
1 97  VAL n 
1 98  LEU n 
1 99  SER n 
1 100 ASN n 
1 101 TYR n 
1 102 ASP n 
1 103 ALA n 
1 104 ASN n 
1 105 LYS n 
1 106 THR n 
1 107 GLY n 
1 108 LEU n 
1 109 LYS n 
1 110 GLU n 
1 111 LEU n 
1 112 PRO n 
1 113 MET n 
1 114 ARG n 
1 115 ASN n 
1 116 LEU n 
1 117 GLN n 
1 118 GLU n 
1 119 ILE n 
1 120 LEU n 
1 121 HIS n 
1 122 GLY n 
1 123 ALA n 
1 124 VAL n 
1 125 ARG n 
1 126 PHE n 
1 127 SER n 
1 128 ASN n 
1 129 ASN n 
1 130 PRO n 
1 131 ALA n 
1 132 LEU n 
1 133 CYS n 
1 134 ASN n 
1 135 VAL n 
1 136 GLU n 
1 137 SER n 
1 138 ILE n 
1 139 GLN n 
1 140 TRP n 
1 141 ARG n 
1 142 ASP n 
1 143 ILE n 
1 144 VAL n 
1 145 SER n 
1 146 SER n 
1 147 ASP n 
1 148 PHE n 
1 149 LEU n 
1 150 SER n 
1 151 ASN n 
1 152 MET n 
1 153 SER n 
1 154 MET n 
1 155 ASP n 
1 156 PHE n 
1 157 GLN n 
1 158 ASN n 
1 159 HIS n 
1 160 LEU n 
1 161 GLY n 
1 162 SER n 
1 163 CYS n 
1 164 GLN n 
1 165 LYS n 
1 166 CYS n 
1 167 ASP n 
1 168 PRO n 
1 169 SER n 
1 170 CYS n 
1 171 PRO n 
1 172 ASN n 
1 173 GLY n 
1 174 SER n 
1 175 CYS n 
1 176 TRP n 
1 177 GLY n 
1 178 ALA n 
1 179 GLY n 
1 180 GLU n 
1 181 GLU n 
1 182 ASN n 
1 183 CYS n 
1 184 GLN n 
1 185 LYS n 
1 186 LEU n 
1 187 THR n 
1 188 LYS n 
1 189 ILE n 
1 190 ILE n 
1 191 CYS n 
1 192 ALA n 
1 193 GLN n 
1 194 GLN n 
1 195 CYS n 
1 196 SER n 
1 197 GLY n 
1 198 ARG n 
1 199 CYS n 
1 200 ARG n 
1 201 GLY n 
1 202 LYS n 
1 203 SER n 
1 204 PRO n 
1 205 SER n 
1 206 ASP n 
1 207 CYS n 
1 208 CYS n 
1 209 HIS n 
1 210 ASN n 
1 211 GLN n 
1 212 CYS n 
1 213 ALA n 
1 214 ALA n 
1 215 GLY n 
1 216 CYS n 
1 217 THR n 
1 218 GLY n 
1 219 PRO n 
1 220 ARG n 
1 221 GLU n 
1 222 SER n 
1 223 ASP n 
1 224 CYS n 
1 225 LEU n 
1 226 VAL n 
1 227 CYS n 
1 228 ARG n 
1 229 LYS n 
1 230 PHE n 
1 231 ARG n 
1 232 ASP n 
1 233 GLU n 
1 234 ALA n 
1 235 THR n 
1 236 CYS n 
1 237 LYS n 
1 238 ASP n 
1 239 THR n 
1 240 CYS n 
1 241 PRO n 
1 242 PRO n 
1 243 LEU n 
1 244 MET n 
1 245 LEU n 
1 246 TYR n 
1 247 ASN n 
1 248 PRO n 
1 249 THR n 
1 250 THR n 
1 251 TYR n 
1 252 GLN n 
1 253 MET n 
1 254 ASP n 
1 255 VAL n 
1 256 ASN n 
1 257 PRO n 
1 258 GLU n 
1 259 GLY n 
1 260 LYS n 
1 261 TYR n 
1 262 SER n 
1 263 PHE n 
1 264 GLY n 
1 265 ALA n 
1 266 THR n 
1 267 CYS n 
1 268 VAL n 
1 269 LYS n 
1 270 LYS n 
1 271 CYS n 
1 272 PRO n 
1 273 ARG n 
1 274 ASN n 
1 275 TYR n 
1 276 VAL n 
1 277 VAL n 
1 278 THR n 
1 279 ASP n 
1 280 HIS n 
1 281 GLY n 
1 282 SER n 
1 283 CYS n 
1 284 VAL n 
1 285 ARG n 
1 286 ALA n 
1 287 CYS n 
1 288 GLY n 
1 289 ALA n 
1 290 ASP n 
1 291 SER n 
1 292 TYR n 
1 293 GLU n 
1 294 MET n 
1 295 GLU n 
1 296 GLU n 
1 297 ASP n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 LYS n 
1 302 CYS n 
1 303 LYS n 
1 304 LYS n 
1 305 CYS n 
1 306 GLU n 
1 307 GLY n 
1 308 PRO n 
1 309 CYS n 
1 310 ARG n 
1 311 LYS n 
1 312 VAL n 
1 313 CYS n 
1 314 ASN n 
1 315 GLY n 
1 316 ILE n 
1 317 GLY n 
1 318 ILE n 
1 319 GLY n 
1 320 GLU n 
1 321 PHE n 
1 322 LYS n 
1 323 ASP n 
1 324 SER n 
1 325 LEU n 
1 326 SER n 
1 327 ILE n 
1 328 ASN n 
1 329 ALA n 
1 330 THR n 
1 331 ASN n 
1 332 ILE n 
1 333 LYS n 
1 334 HIS n 
1 335 PHE n 
1 336 LYS n 
1 337 ASN n 
1 338 CYS n 
1 339 THR n 
1 340 SER n 
1 341 ILE n 
1 342 SER n 
1 343 GLY n 
1 344 ASP n 
1 345 LEU n 
1 346 HIS n 
1 347 ILE n 
1 348 LEU n 
1 349 PRO n 
1 350 VAL n 
1 351 ALA n 
1 352 PHE n 
1 353 ARG n 
1 354 GLY n 
1 355 ASP n 
1 356 SER n 
1 357 PHE n 
1 358 THR n 
1 359 HIS n 
1 360 THR n 
1 361 PRO n 
1 362 PRO n 
1 363 LEU n 
1 364 ASP n 
1 365 PRO n 
1 366 GLN n 
1 367 GLU n 
1 368 LEU n 
1 369 ASP n 
1 370 ILE n 
1 371 LEU n 
1 372 LYS n 
1 373 THR n 
1 374 VAL n 
1 375 LYS n 
1 376 GLU n 
1 377 ILE n 
1 378 THR n 
1 379 GLY n 
1 380 PHE n 
1 381 LEU n 
1 382 LEU n 
1 383 ILE n 
1 384 GLN n 
1 385 ALA n 
1 386 TRP n 
1 387 PRO n 
1 388 GLU n 
1 389 ASN n 
1 390 ARG n 
1 391 THR n 
1 392 ASP n 
1 393 LEU n 
1 394 HIS n 
1 395 ALA n 
1 396 PHE n 
1 397 GLU n 
1 398 ASN n 
1 399 LEU n 
1 400 GLU n 
1 401 ILE n 
1 402 ILE n 
1 403 ARG n 
1 404 GLY n 
1 405 ARG n 
1 406 THR n 
1 407 LYS n 
1 408 GLN n 
1 409 HIS n 
1 410 GLY n 
1 411 GLN n 
1 412 PHE n 
1 413 SER n 
1 414 LEU n 
1 415 ALA n 
1 416 VAL n 
1 417 VAL n 
1 418 SER n 
1 419 LEU n 
1 420 ASN n 
1 421 ILE n 
1 422 THR n 
1 423 SER n 
1 424 LEU n 
1 425 GLY n 
1 426 LEU n 
1 427 ARG n 
1 428 SER n 
1 429 LEU n 
1 430 LYS n 
1 431 GLU n 
1 432 ILE n 
1 433 SER n 
1 434 ASP n 
1 435 GLY n 
1 436 ASP n 
1 437 VAL n 
1 438 ILE n 
1 439 ILE n 
1 440 SER n 
1 441 GLY n 
1 442 ASN n 
1 443 LYS n 
1 444 ASN n 
1 445 LEU n 
1 446 CYS n 
1 447 TYR n 
1 448 ALA n 
1 449 ASN n 
1 450 THR n 
1 451 ILE n 
1 452 ASN n 
1 453 TRP n 
1 454 LYS n 
1 455 LYS n 
1 456 LEU n 
1 457 PHE n 
1 458 GLY n 
1 459 THR n 
1 460 SER n 
1 461 GLY n 
1 462 GLN n 
1 463 LYS n 
1 464 THR n 
1 465 LYS n 
1 466 ILE n 
1 467 ILE n 
1 468 SER n 
1 469 ASN n 
1 470 ARG n 
1 471 GLY n 
1 472 GLU n 
1 473 ASN n 
1 474 SER n 
1 475 CYS n 
1 476 LYS n 
1 477 ALA n 
1 478 THR n 
1 479 GLY n 
1 480 GLN n 
1 481 VAL n 
1 482 CYS n 
1 483 HIS n 
1 484 ALA n 
1 485 LEU n 
1 486 CYS n 
1 487 SER n 
1 488 PRO n 
1 489 GLU n 
1 490 GLY n 
1 491 CYS n 
1 492 TRP n 
1 493 GLY n 
1 494 PRO n 
1 495 GLU n 
1 496 PRO n 
1 497 ARG n 
1 498 ASP n 
1 499 CYS n 
1 500 VAL n 
1 501 SER n 
1 502 CYS n 
1 503 ARG n 
1 504 ASN n 
1 505 VAL n 
1 506 SER n 
1 507 ARG n 
1 508 GLY n 
1 509 ARG n 
1 510 GLU n 
1 511 CYS n 
1 512 VAL n 
1 513 ASP n 
1 514 LYS n 
1 515 CYS n 
1 516 ASN n 
1 517 LEU n 
1 518 LEU n 
1 519 GLU n 
1 520 GLY n 
1 521 GLU n 
1 522 PRO n 
1 523 ARG n 
1 524 GLU n 
1 525 PHE n 
1 526 VAL n 
1 527 GLU n 
1 528 ASN n 
1 529 SER n 
1 530 GLU n 
1 531 CYS n 
1 532 ILE n 
1 533 GLN n 
1 534 CYS n 
1 535 HIS n 
1 536 PRO n 
1 537 GLU n 
1 538 CYS n 
1 539 LEU n 
1 540 PRO n 
1 541 GLN n 
1 542 ALA n 
1 543 MET n 
1 544 ASN n 
1 545 ILE n 
1 546 THR n 
1 547 CYS n 
1 548 THR n 
1 549 GLY n 
1 550 ARG n 
1 551 GLY n 
1 552 PRO n 
1 553 ASP n 
1 554 ASN n 
1 555 CYS n 
1 556 ILE n 
1 557 GLN n 
1 558 CYS n 
1 559 ALA n 
1 560 HIS n 
1 561 TYR n 
1 562 ILE n 
1 563 ASP n 
1 564 GLY n 
1 565 PRO n 
1 566 HIS n 
1 567 CYS n 
1 568 VAL n 
1 569 LYS n 
1 570 THR n 
1 571 CYS n 
1 572 PRO n 
1 573 ALA n 
1 574 GLY n 
1 575 VAL n 
1 576 MET n 
1 577 GLY n 
1 578 GLU n 
1 579 ASN n 
1 580 ASN n 
1 581 THR n 
1 582 LEU n 
1 583 VAL n 
1 584 TRP n 
1 585 LYS n 
1 586 TYR n 
1 587 ALA n 
1 588 ASP n 
1 589 ALA n 
1 590 GLY n 
1 591 HIS n 
1 592 VAL n 
1 593 CYS n 
1 594 HIS n 
1 595 LEU n 
1 596 CYS n 
1 597 HIS n 
1 598 PRO n 
1 599 ASN n 
1 600 CYS n 
1 601 THR n 
1 602 TYR n 
1 603 GLY n 
1 604 CYS n 
1 605 THR n 
1 606 GLY n 
1 607 PRO n 
1 608 GLY n 
1 609 LEU n 
1 610 GLU n 
1 611 GLY n 
1 612 CYS n 
1 613 PRO n 
1 614 THR n 
1 615 ASN n 
1 616 GLY n 
1 617 PRO n 
1 618 LYS n 
1 619 ILE n 
1 620 PRO n 
1 621 SER n 
1 622 HIS n 
1 623 HIS n 
1 624 HIS n 
1 625 HIS n 
1 626 HIS n 
1 627 HIS n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   ALA n 
2 10  GLU n 
2 11  VAL n 
2 12  LYS n 
2 13  LYS n 
2 14  PRO n 
2 15  GLY n 
2 16  ALA n 
2 17  SER n 
2 18  VAL n 
2 19  LYS n 
2 20  VAL n 
2 21  SER n 
2 22  CYS n 
2 23  LYS n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  TYR n 
2 28  THR n 
2 29  PHE n 
2 30  THR n 
2 31  SER n 
2 32  TYR n 
2 33  TRP n 
2 34  MET n 
2 35  HIS n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  GLN n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  MET n 
2 49  GLY n 
2 50  ASN n 
2 51  ILE n 
2 52  TRP n 
2 53  PRO n 
2 54  GLY n 
2 55  SER n 
2 56  GLY n 
2 57  GLY n 
2 58  THR n 
2 59  ASN n 
2 60  TYR n 
2 61  ALA n 
2 62  GLU n 
2 63  LYS n 
2 64  PHE n 
2 65  LYS n 
2 66  ASN n 
2 67  ARG n 
2 68  VAL n 
2 69  THR n 
2 70  MET n 
2 71  THR n 
2 72  ARG n 
2 73  ASP n 
2 74  THR n 
2 75  SER n 
2 76  ILE n 
2 77  SER n 
2 78  THR n 
2 79  ALA n 
2 80  TYR n 
2 81  MET n 
2 82  GLU n 
2 83  LEU n 
2 84  SER n 
2 85  ARG n 
2 86  LEU n 
2 87  ARG n 
2 88  SER n 
2 89  ASP n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  ARG n 
2 99  SER n 
2 100 GLY n 
2 101 GLY n 
2 102 PRO n 
2 103 TYR n 
2 104 PHE n 
2 105 PHE n 
2 106 ASP n 
2 107 TYR n 
2 108 TRP n 
2 109 GLY n 
2 110 GLN n 
2 111 GLY n 
2 112 THR n 
2 113 LEU n 
2 114 VAL n 
2 115 THR n 
2 116 VAL n 
2 117 SER n 
2 118 SER n 
2 119 GLY n 
2 120 GLY n 
2 121 GLY n 
2 122 GLY n 
2 123 SER n 
2 124 GLY n 
2 125 GLY n 
2 126 GLY n 
2 127 GLY n 
2 128 SER n 
2 129 GLY n 
2 130 GLY n 
2 131 GLY n 
2 132 GLY n 
2 133 SER n 
2 134 GLY n 
2 135 GLY n 
2 136 GLY n 
2 137 GLY n 
2 138 SER n 
2 139 ASP n 
2 140 ILE n 
2 141 VAL n 
2 142 MET n 
2 143 THR n 
2 144 GLN n 
2 145 SER n 
2 146 PRO n 
2 147 LEU n 
2 148 SER n 
2 149 LEU n 
2 150 PRO n 
2 151 VAL n 
2 152 THR n 
2 153 PRO n 
2 154 GLY n 
2 155 GLU n 
2 156 PRO n 
2 157 ALA n 
2 158 SER n 
2 159 ILE n 
2 160 SER n 
2 161 CYS n 
2 162 ARG n 
2 163 SER n 
2 164 SER n 
2 165 GLN n 
2 166 ASN n 
2 167 ILE n 
2 168 VAL n 
2 169 HIS n 
2 170 ASN n 
2 171 ASN n 
2 172 GLY n 
2 173 ILE n 
2 174 THR n 
2 175 TYR n 
2 176 LEU n 
2 177 GLU n 
2 178 TRP n 
2 179 TYR n 
2 180 LEU n 
2 181 GLN n 
2 182 LYS n 
2 183 PRO n 
2 184 GLY n 
2 185 GLN n 
2 186 SER n 
2 187 PRO n 
2 188 GLN n 
2 189 LEU n 
2 190 LEU n 
2 191 ILE n 
2 192 TYR n 
2 193 LYS n 
2 194 VAL n 
2 195 SER n 
2 196 ASP n 
2 197 ARG n 
2 198 PHE n 
2 199 SER n 
2 200 GLY n 
2 201 VAL n 
2 202 PRO n 
2 203 ASP n 
2 204 ARG n 
2 205 PHE n 
2 206 SER n 
2 207 GLY n 
2 208 SER n 
2 209 GLY n 
2 210 SER n 
2 211 GLY n 
2 212 THR n 
2 213 ASP n 
2 214 PHE n 
2 215 THR n 
2 216 LEU n 
2 217 LYS n 
2 218 ILE n 
2 219 SER n 
2 220 ARG n 
2 221 VAL n 
2 222 GLU n 
2 223 ALA n 
2 224 GLU n 
2 225 ASP n 
2 226 VAL n 
2 227 GLY n 
2 228 VAL n 
2 229 TYR n 
2 230 TYR n 
2 231 CYS n 
2 232 PHE n 
2 233 GLN n 
2 234 GLY n 
2 235 SER n 
2 236 HIS n 
2 237 ILE n 
2 238 PRO n 
2 239 PRO n 
2 240 THR n 
2 241 PHE n 
2 242 GLY n 
2 243 GLN n 
2 244 GLY n 
2 245 THR n 
2 246 LYS n 
2 247 VAL n 
2 248 GLU n 
2 249 ILE n 
2 250 LYS 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' 1 627 human ? 'EGFR, ERBB, ERBB1, HER1' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Cricetulus griseus'         10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 250 ?     ? ?                         ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Brevibacillus choshinensis' 54911 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_branch.entity_id   3 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                            'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'       LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  3 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  NAG 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  NAG 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   LEU 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   CYS 7   7   7   CYS CYS A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   GLY 9   9   ?   ?   ?   A . n 
A 1 10  THR 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  ?   ?   ?   A . n 
A 1 12  ASN 12  12  ?   ?   ?   A . n 
A 1 13  LYS 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  THR 15  15  ?   ?   ?   A . n 
A 1 16  GLN 16  16  ?   ?   ?   A . n 
A 1 17  LEU 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  HIS 23  23  23  HIS HIS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  CYS 34  34  34  CYS CYS A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  MET 87  87  87  MET MET A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 TYR 101 101 ?   ?   ?   A . n 
A 1 102 ASP 102 102 ?   ?   ?   A . n 
A 1 103 ALA 103 103 ?   ?   ?   A . n 
A 1 104 ASN 104 104 ?   ?   ?   A . n 
A 1 105 LYS 105 105 ?   ?   ?   A . n 
A 1 106 THR 106 106 ?   ?   ?   A . n 
A 1 107 GLY 107 107 ?   ?   ?   A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 MET 113 113 113 MET MET A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 GLN 139 139 139 GLN GLN A . n 
A 1 140 TRP 140 140 140 TRP TRP A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 PHE 156 156 ?   ?   ?   A . n 
A 1 157 GLN 157 157 ?   ?   ?   A . n 
A 1 158 ASN 158 158 ?   ?   ?   A . n 
A 1 159 HIS 159 159 ?   ?   ?   A . n 
A 1 160 LEU 160 160 ?   ?   ?   A . n 
A 1 161 GLY 161 161 ?   ?   ?   A . n 
A 1 162 SER 162 162 ?   ?   ?   A . n 
A 1 163 CYS 163 163 ?   ?   ?   A . n 
A 1 164 GLN 164 164 ?   ?   ?   A . n 
A 1 165 LYS 165 165 ?   ?   ?   A . n 
A 1 166 CYS 166 166 ?   ?   ?   A . n 
A 1 167 ASP 167 167 ?   ?   ?   A . n 
A 1 168 PRO 168 168 ?   ?   ?   A . n 
A 1 169 SER 169 169 ?   ?   ?   A . n 
A 1 170 CYS 170 170 ?   ?   ?   A . n 
A 1 171 PRO 171 171 ?   ?   ?   A . n 
A 1 172 ASN 172 172 ?   ?   ?   A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 CYS 175 175 175 CYS CYS A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 ILE 190 190 ?   ?   ?   A . n 
A 1 191 CYS 191 191 ?   ?   ?   A . n 
A 1 192 ALA 192 192 ?   ?   ?   A . n 
A 1 193 GLN 193 193 ?   ?   ?   A . n 
A 1 194 GLN 194 194 ?   ?   ?   A . n 
A 1 195 CYS 195 195 ?   ?   ?   A . n 
A 1 196 SER 196 196 ?   ?   ?   A . n 
A 1 197 GLY 197 197 ?   ?   ?   A . n 
A 1 198 ARG 198 198 ?   ?   ?   A . n 
A 1 199 CYS 199 199 ?   ?   ?   A . n 
A 1 200 ARG 200 200 ?   ?   ?   A . n 
A 1 201 GLY 201 201 ?   ?   ?   A . n 
A 1 202 LYS 202 202 ?   ?   ?   A . n 
A 1 203 SER 203 203 ?   ?   ?   A . n 
A 1 204 PRO 204 204 ?   ?   ?   A . n 
A 1 205 SER 205 205 ?   ?   ?   A . n 
A 1 206 ASP 206 206 ?   ?   ?   A . n 
A 1 207 CYS 207 207 ?   ?   ?   A . n 
A 1 208 CYS 208 208 ?   ?   ?   A . n 
A 1 209 HIS 209 209 ?   ?   ?   A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 CYS 216 216 216 CYS CYS A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 CYS 224 224 224 CYS CYS A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 CYS 227 227 227 CYS CYS A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 CYS 236 236 236 CYS CYS A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 CYS 240 240 240 CYS CYS A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 TYR 246 246 246 TYR TYR A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 MET 253 253 253 MET MET A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 CYS 267 267 267 CYS CYS A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 CYS 271 271 271 CYS CYS A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 HIS 280 280 280 HIS HIS A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 CYS 283 283 283 CYS CYS A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ARG 285 285 285 ARG ARG A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 CYS 287 287 287 CYS CYS A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 GLU 295 295 295 GLU GLU A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 CYS 302 302 302 CYS CYS A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 CYS 305 305 305 CYS CYS A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 CYS 309 309 309 CYS CYS A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 CYS 313 313 313 CYS CYS A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 HIS 334 334 334 HIS HIS A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 CYS 338 338 338 CYS CYS A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 ASP 344 344 344 ASP ASP A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 HIS 346 346 346 HIS HIS A . n 
A 1 347 ILE 347 347 347 ILE ILE A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 PHE 352 352 352 PHE PHE A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 HIS 359 359 359 HIS HIS A . n 
A 1 360 THR 360 360 360 THR THR A . n 
A 1 361 PRO 361 361 361 PRO PRO A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 GLN 366 366 366 GLN GLN A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ILE 370 370 370 ILE ILE A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 THR 373 373 373 THR THR A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 PHE 380 380 380 PHE PHE A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 GLN 384 384 384 GLN GLN A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 TRP 386 386 386 TRP TRP A . n 
A 1 387 PRO 387 387 387 PRO PRO A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ASN 389 389 389 ASN ASN A . n 
A 1 390 ARG 390 390 390 ARG ARG A . n 
A 1 391 THR 391 391 391 THR THR A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 HIS 394 394 394 HIS HIS A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 LEU 399 399 399 LEU LEU A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 ARG 403 403 403 ARG ARG A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 GLN 408 408 408 GLN GLN A . n 
A 1 409 HIS 409 409 409 HIS HIS A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLN 411 411 411 GLN GLN A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 VAL 416 416 416 VAL VAL A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 ASN 420 420 420 ASN ASN A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 SER 423 423 423 SER SER A . n 
A 1 424 LEU 424 424 424 LEU LEU A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 ARG 427 427 427 ARG ARG A . n 
A 1 428 SER 428 428 428 SER SER A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 ASP 436 436 436 ASP ASP A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 ILE 438 438 438 ILE ILE A . n 
A 1 439 ILE 439 439 439 ILE ILE A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 CYS 446 446 446 CYS CYS A . n 
A 1 447 TYR 447 447 447 TYR TYR A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 ASN 449 449 449 ASN ASN A . n 
A 1 450 THR 450 450 450 THR THR A . n 
A 1 451 ILE 451 451 451 ILE ILE A . n 
A 1 452 ASN 452 452 452 ASN ASN A . n 
A 1 453 TRP 453 453 453 TRP TRP A . n 
A 1 454 LYS 454 454 454 LYS LYS A . n 
A 1 455 LYS 455 455 455 LYS LYS A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 PHE 457 457 457 PHE PHE A . n 
A 1 458 GLY 458 458 458 GLY GLY A . n 
A 1 459 THR 459 459 459 THR THR A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 GLN 462 462 462 GLN GLN A . n 
A 1 463 LYS 463 463 463 LYS LYS A . n 
A 1 464 THR 464 464 464 THR THR A . n 
A 1 465 LYS 465 465 465 LYS LYS A . n 
A 1 466 ILE 466 466 466 ILE ILE A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 SER 468 468 468 SER SER A . n 
A 1 469 ASN 469 469 469 ASN ASN A . n 
A 1 470 ARG 470 470 470 ARG ARG A . n 
A 1 471 GLY 471 471 471 GLY GLY A . n 
A 1 472 GLU 472 472 472 GLU GLU A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 SER 474 474 474 SER SER A . n 
A 1 475 CYS 475 475 475 CYS CYS A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 ALA 477 477 477 ALA ALA A . n 
A 1 478 THR 478 478 478 THR THR A . n 
A 1 479 GLY 479 479 479 GLY GLY A . n 
A 1 480 GLN 480 480 480 GLN GLN A . n 
A 1 481 VAL 481 481 481 VAL VAL A . n 
A 1 482 CYS 482 482 482 CYS CYS A . n 
A 1 483 HIS 483 483 483 HIS HIS A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 CYS 486 486 486 CYS CYS A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 PRO 488 488 488 PRO PRO A . n 
A 1 489 GLU 489 489 489 GLU GLU A . n 
A 1 490 GLY 490 490 490 GLY GLY A . n 
A 1 491 CYS 491 491 491 CYS CYS A . n 
A 1 492 TRP 492 492 492 TRP TRP A . n 
A 1 493 GLY 493 493 493 GLY GLY A . n 
A 1 494 PRO 494 494 494 PRO PRO A . n 
A 1 495 GLU 495 495 495 GLU GLU A . n 
A 1 496 PRO 496 496 496 PRO PRO A . n 
A 1 497 ARG 497 497 497 ARG ARG A . n 
A 1 498 ASP 498 498 498 ASP ASP A . n 
A 1 499 CYS 499 499 499 CYS CYS A . n 
A 1 500 VAL 500 500 500 VAL VAL A . n 
A 1 501 SER 501 501 501 SER SER A . n 
A 1 502 CYS 502 502 502 CYS CYS A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 ASN 504 504 504 ASN ASN A . n 
A 1 505 VAL 505 505 505 VAL VAL A . n 
A 1 506 SER 506 506 506 SER SER A . n 
A 1 507 ARG 507 507 507 ARG ARG A . n 
A 1 508 GLY 508 508 508 GLY GLY A . n 
A 1 509 ARG 509 509 509 ARG ARG A . n 
A 1 510 GLU 510 510 510 GLU GLU A . n 
A 1 511 CYS 511 511 511 CYS CYS A . n 
A 1 512 VAL 512 512 512 VAL VAL A . n 
A 1 513 ASP 513 513 513 ASP ASP A . n 
A 1 514 LYS 514 514 514 LYS LYS A . n 
A 1 515 CYS 515 515 515 CYS CYS A . n 
A 1 516 ASN 516 516 516 ASN ASN A . n 
A 1 517 LEU 517 517 517 LEU LEU A . n 
A 1 518 LEU 518 518 518 LEU LEU A . n 
A 1 519 GLU 519 519 519 GLU GLU A . n 
A 1 520 GLY 520 520 520 GLY GLY A . n 
A 1 521 GLU 521 521 521 GLU GLU A . n 
A 1 522 PRO 522 522 522 PRO PRO A . n 
A 1 523 ARG 523 523 523 ARG ARG A . n 
A 1 524 GLU 524 524 524 GLU GLU A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 VAL 526 526 526 VAL VAL A . n 
A 1 527 GLU 527 527 527 GLU GLU A . n 
A 1 528 ASN 528 528 528 ASN ASN A . n 
A 1 529 SER 529 529 529 SER SER A . n 
A 1 530 GLU 530 530 530 GLU GLU A . n 
A 1 531 CYS 531 531 531 CYS CYS A . n 
A 1 532 ILE 532 532 532 ILE ILE A . n 
A 1 533 GLN 533 533 533 GLN GLN A . n 
A 1 534 CYS 534 534 534 CYS CYS A . n 
A 1 535 HIS 535 535 535 HIS HIS A . n 
A 1 536 PRO 536 536 536 PRO PRO A . n 
A 1 537 GLU 537 537 537 GLU GLU A . n 
A 1 538 CYS 538 538 538 CYS CYS A . n 
A 1 539 LEU 539 539 539 LEU LEU A . n 
A 1 540 PRO 540 540 540 PRO PRO A . n 
A 1 541 GLN 541 541 541 GLN GLN A . n 
A 1 542 ALA 542 542 542 ALA ALA A . n 
A 1 543 MET 543 543 543 MET MET A . n 
A 1 544 ASN 544 544 544 ASN ASN A . n 
A 1 545 ILE 545 545 545 ILE ILE A . n 
A 1 546 THR 546 546 546 THR THR A . n 
A 1 547 CYS 547 547 547 CYS CYS A . n 
A 1 548 THR 548 548 548 THR THR A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 ARG 550 550 550 ARG ARG A . n 
A 1 551 GLY 551 551 551 GLY GLY A . n 
A 1 552 PRO 552 552 552 PRO PRO A . n 
A 1 553 ASP 553 553 553 ASP ASP A . n 
A 1 554 ASN 554 554 554 ASN ASN A . n 
A 1 555 CYS 555 555 555 CYS CYS A . n 
A 1 556 ILE 556 556 556 ILE ILE A . n 
A 1 557 GLN 557 557 557 GLN GLN A . n 
A 1 558 CYS 558 558 558 CYS CYS A . n 
A 1 559 ALA 559 559 559 ALA ALA A . n 
A 1 560 HIS 560 560 560 HIS HIS A . n 
A 1 561 TYR 561 561 561 TYR TYR A . n 
A 1 562 ILE 562 562 562 ILE ILE A . n 
A 1 563 ASP 563 563 563 ASP ASP A . n 
A 1 564 GLY 564 564 564 GLY GLY A . n 
A 1 565 PRO 565 565 565 PRO PRO A . n 
A 1 566 HIS 566 566 566 HIS HIS A . n 
A 1 567 CYS 567 567 567 CYS CYS A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 LYS 569 569 569 LYS LYS A . n 
A 1 570 THR 570 570 570 THR THR A . n 
A 1 571 CYS 571 571 571 CYS CYS A . n 
A 1 572 PRO 572 572 572 PRO PRO A . n 
A 1 573 ALA 573 573 573 ALA ALA A . n 
A 1 574 GLY 574 574 574 GLY GLY A . n 
A 1 575 VAL 575 575 575 VAL VAL A . n 
A 1 576 MET 576 576 576 MET MET A . n 
A 1 577 GLY 577 577 577 GLY GLY A . n 
A 1 578 GLU 578 578 578 GLU GLU A . n 
A 1 579 ASN 579 579 579 ASN ASN A . n 
A 1 580 ASN 580 580 580 ASN ASN A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 LEU 582 582 582 LEU LEU A . n 
A 1 583 VAL 583 583 583 VAL VAL A . n 
A 1 584 TRP 584 584 584 TRP TRP A . n 
A 1 585 LYS 585 585 585 LYS LYS A . n 
A 1 586 TYR 586 586 586 TYR TYR A . n 
A 1 587 ALA 587 587 587 ALA ALA A . n 
A 1 588 ASP 588 588 588 ASP ASP A . n 
A 1 589 ALA 589 589 589 ALA ALA A . n 
A 1 590 GLY 590 590 590 GLY GLY A . n 
A 1 591 HIS 591 591 591 HIS HIS A . n 
A 1 592 VAL 592 592 592 VAL VAL A . n 
A 1 593 CYS 593 593 593 CYS CYS A . n 
A 1 594 HIS 594 594 594 HIS HIS A . n 
A 1 595 LEU 595 595 595 LEU LEU A . n 
A 1 596 CYS 596 596 596 CYS CYS A . n 
A 1 597 HIS 597 597 ?   ?   ?   A . n 
A 1 598 PRO 598 598 ?   ?   ?   A . n 
A 1 599 ASN 599 599 ?   ?   ?   A . n 
A 1 600 CYS 600 600 ?   ?   ?   A . n 
A 1 601 THR 601 601 ?   ?   ?   A . n 
A 1 602 TYR 602 602 ?   ?   ?   A . n 
A 1 603 GLY 603 603 ?   ?   ?   A . n 
A 1 604 CYS 604 604 ?   ?   ?   A . n 
A 1 605 THR 605 605 ?   ?   ?   A . n 
A 1 606 GLY 606 606 ?   ?   ?   A . n 
A 1 607 PRO 607 607 ?   ?   ?   A . n 
A 1 608 GLY 608 608 ?   ?   ?   A . n 
A 1 609 LEU 609 609 ?   ?   ?   A . n 
A 1 610 GLU 610 610 ?   ?   ?   A . n 
A 1 611 GLY 611 611 ?   ?   ?   A . n 
A 1 612 CYS 612 612 ?   ?   ?   A . n 
A 1 613 PRO 613 613 ?   ?   ?   A . n 
A 1 614 THR 614 614 ?   ?   ?   A . n 
A 1 615 ASN 615 615 ?   ?   ?   A . n 
A 1 616 GLY 616 616 ?   ?   ?   A . n 
A 1 617 PRO 617 617 ?   ?   ?   A . n 
A 1 618 LYS 618 618 ?   ?   ?   A . n 
A 1 619 ILE 619 619 ?   ?   ?   A . n 
A 1 620 PRO 620 620 ?   ?   ?   A . n 
A 1 621 SER 621 621 ?   ?   ?   A . n 
A 1 622 HIS 622 622 ?   ?   ?   A . n 
A 1 623 HIS 623 623 ?   ?   ?   A . n 
A 1 624 HIS 624 624 ?   ?   ?   A . n 
A 1 625 HIS 625 625 ?   ?   ?   A . n 
A 1 626 HIS 626 626 ?   ?   ?   A . n 
A 1 627 HIS 627 627 ?   ?   ?   A . n 
B 2 1   GLN 1   117 117 GLN GLN D . n 
B 2 2   VAL 2   118 118 VAL VAL D . n 
B 2 3   GLN 3   119 119 GLN GLN D . n 
B 2 4   LEU 4   120 120 LEU LEU D . n 
B 2 5   VAL 5   121 121 VAL VAL D . n 
B 2 6   GLN 6   122 122 GLN GLN D . n 
B 2 7   SER 7   123 123 SER SER D . n 
B 2 8   GLY 8   124 124 GLY GLY D . n 
B 2 9   ALA 9   125 125 ALA ALA D . n 
B 2 10  GLU 10  126 126 GLU GLU D . n 
B 2 11  VAL 11  127 127 VAL VAL D . n 
B 2 12  LYS 12  128 128 LYS LYS D . n 
B 2 13  LYS 13  129 129 LYS LYS D . n 
B 2 14  PRO 14  130 130 PRO PRO D . n 
B 2 15  GLY 15  131 131 GLY GLY D . n 
B 2 16  ALA 16  132 132 ALA ALA D . n 
B 2 17  SER 17  133 133 SER SER D . n 
B 2 18  VAL 18  134 134 VAL VAL D . n 
B 2 19  LYS 19  135 135 LYS LYS D . n 
B 2 20  VAL 20  136 136 VAL VAL D . n 
B 2 21  SER 21  137 137 SER SER D . n 
B 2 22  CYS 22  138 138 CYS CYS D . n 
B 2 23  LYS 23  139 139 LYS LYS D . n 
B 2 24  ALA 24  140 140 ALA ALA D . n 
B 2 25  SER 25  141 141 SER SER D . n 
B 2 26  GLY 26  142 142 GLY GLY D . n 
B 2 27  TYR 27  143 143 TYR TYR D . n 
B 2 28  THR 28  144 144 THR THR D . n 
B 2 29  PHE 29  145 145 PHE PHE D . n 
B 2 30  THR 30  146 146 THR THR D . n 
B 2 31  SER 31  147 147 SER SER D . n 
B 2 32  TYR 32  148 148 TYR TYR D . n 
B 2 33  TRP 33  149 149 TRP TRP D . n 
B 2 34  MET 34  150 150 MET MET D . n 
B 2 35  HIS 35  151 151 HIS HIS D . n 
B 2 36  TRP 36  152 152 TRP TRP D . n 
B 2 37  VAL 37  153 153 VAL VAL D . n 
B 2 38  ARG 38  154 154 ARG ARG D . n 
B 2 39  GLN 39  155 155 GLN GLN D . n 
B 2 40  ALA 40  156 156 ALA ALA D . n 
B 2 41  PRO 41  157 157 PRO PRO D . n 
B 2 42  GLY 42  158 158 GLY GLY D . n 
B 2 43  GLN 43  159 159 GLN GLN D . n 
B 2 44  GLY 44  160 160 GLY GLY D . n 
B 2 45  LEU 45  161 161 LEU LEU D . n 
B 2 46  GLU 46  162 162 GLU GLU D . n 
B 2 47  TRP 47  163 163 TRP TRP D . n 
B 2 48  MET 48  164 164 MET MET D . n 
B 2 49  GLY 49  165 165 GLY GLY D . n 
B 2 50  ASN 50  166 166 ASN ASN D . n 
B 2 51  ILE 51  167 167 ILE ILE D . n 
B 2 52  TRP 52  168 168 TRP TRP D . n 
B 2 53  PRO 53  169 169 PRO PRO D . n 
B 2 54  GLY 54  170 170 GLY GLY D . n 
B 2 55  SER 55  171 171 SER SER D . n 
B 2 56  GLY 56  172 172 GLY GLY D . n 
B 2 57  GLY 57  173 173 GLY GLY D . n 
B 2 58  THR 58  174 174 THR THR D . n 
B 2 59  ASN 59  175 175 ASN ASN D . n 
B 2 60  TYR 60  176 176 TYR TYR D . n 
B 2 61  ALA 61  177 177 ALA ALA D . n 
B 2 62  GLU 62  178 178 GLU GLU D . n 
B 2 63  LYS 63  179 179 LYS LYS D . n 
B 2 64  PHE 64  180 180 PHE PHE D . n 
B 2 65  LYS 65  181 181 LYS LYS D . n 
B 2 66  ASN 66  182 182 ASN ASN D . n 
B 2 67  ARG 67  183 183 ARG ARG D . n 
B 2 68  VAL 68  184 184 VAL VAL D . n 
B 2 69  THR 69  185 185 THR THR D . n 
B 2 70  MET 70  186 186 MET MET D . n 
B 2 71  THR 71  187 187 THR THR D . n 
B 2 72  ARG 72  188 188 ARG ARG D . n 
B 2 73  ASP 73  189 189 ASP ASP D . n 
B 2 74  THR 74  190 190 THR THR D . n 
B 2 75  SER 75  191 191 SER SER D . n 
B 2 76  ILE 76  192 192 ILE ILE D . n 
B 2 77  SER 77  193 193 SER SER D . n 
B 2 78  THR 78  194 194 THR THR D . n 
B 2 79  ALA 79  195 195 ALA ALA D . n 
B 2 80  TYR 80  196 196 TYR TYR D . n 
B 2 81  MET 81  197 197 MET MET D . n 
B 2 82  GLU 82  198 198 GLU GLU D . n 
B 2 83  LEU 83  199 199 LEU LEU D . n 
B 2 84  SER 84  200 200 SER SER D . n 
B 2 85  ARG 85  201 201 ARG ARG D . n 
B 2 86  LEU 86  202 202 LEU LEU D . n 
B 2 87  ARG 87  203 203 ARG ARG D . n 
B 2 88  SER 88  204 204 SER SER D . n 
B 2 89  ASP 89  205 205 ASP ASP D . n 
B 2 90  ASP 90  206 206 ASP ASP D . n 
B 2 91  THR 91  207 207 THR THR D . n 
B 2 92  ALA 92  208 208 ALA ALA D . n 
B 2 93  VAL 93  209 209 VAL VAL D . n 
B 2 94  TYR 94  210 210 TYR TYR D . n 
B 2 95  TYR 95  211 211 TYR TYR D . n 
B 2 96  CYS 96  212 212 CYS CYS D . n 
B 2 97  ALA 97  213 213 ALA ALA D . n 
B 2 98  ARG 98  214 214 ARG ARG D . n 
B 2 99  SER 99  215 215 SER SER D . n 
B 2 100 GLY 100 216 216 GLY GLY D . n 
B 2 101 GLY 101 217 217 GLY GLY D . n 
B 2 102 PRO 102 218 218 PRO PRO D . n 
B 2 103 TYR 103 219 219 TYR TYR D . n 
B 2 104 PHE 104 220 220 PHE PHE D . n 
B 2 105 PHE 105 221 221 PHE PHE D . n 
B 2 106 ASP 106 222 222 ASP ASP D . n 
B 2 107 TYR 107 223 223 TYR TYR D . n 
B 2 108 TRP 108 224 224 TRP TRP D . n 
B 2 109 GLY 109 225 225 GLY GLY D . n 
B 2 110 GLN 110 226 226 GLN GLN D . n 
B 2 111 GLY 111 227 227 GLY GLY D . n 
B 2 112 THR 112 228 228 THR THR D . n 
B 2 113 LEU 113 229 229 LEU LEU D . n 
B 2 114 VAL 114 230 230 VAL VAL D . n 
B 2 115 THR 115 231 231 THR THR D . n 
B 2 116 VAL 116 232 232 VAL VAL D . n 
B 2 117 SER 117 233 233 SER SER D . n 
B 2 118 SER 118 234 234 SER SER D . n 
B 2 119 GLY 119 235 ?   ?   ?   D . n 
B 2 120 GLY 120 236 ?   ?   ?   D . n 
B 2 121 GLY 121 237 ?   ?   ?   D . n 
B 2 122 GLY 122 238 ?   ?   ?   D . n 
B 2 123 SER 123 239 ?   ?   ?   D . n 
B 2 124 GLY 124 240 ?   ?   ?   D . n 
B 2 125 GLY 125 241 ?   ?   ?   D . n 
B 2 126 GLY 126 242 ?   ?   ?   D . n 
B 2 127 GLY 127 243 ?   ?   ?   D . n 
B 2 128 SER 128 244 ?   ?   ?   D . n 
B 2 129 GLY 129 245 ?   ?   ?   D . n 
B 2 130 GLY 130 246 ?   ?   ?   D . n 
B 2 131 GLY 131 247 ?   ?   ?   D . n 
B 2 132 GLY 132 248 ?   ?   ?   D . n 
B 2 133 SER 133 249 ?   ?   ?   D . n 
B 2 134 GLY 134 250 ?   ?   ?   D . n 
B 2 135 GLY 135 251 ?   ?   ?   D . n 
B 2 136 GLY 136 252 ?   ?   ?   D . n 
B 2 137 GLY 137 253 ?   ?   ?   D . n 
B 2 138 SER 138 254 ?   ?   ?   D . n 
B 2 139 ASP 139 255 255 ASP ASP D . n 
B 2 140 ILE 140 256 256 ILE ILE D . n 
B 2 141 VAL 141 257 257 VAL VAL D . n 
B 2 142 MET 142 258 258 MET MET D . n 
B 2 143 THR 143 259 259 THR THR D . n 
B 2 144 GLN 144 260 260 GLN GLN D . n 
B 2 145 SER 145 261 261 SER SER D . n 
B 2 146 PRO 146 262 262 PRO PRO D . n 
B 2 147 LEU 147 263 263 LEU LEU D . n 
B 2 148 SER 148 264 264 SER SER D . n 
B 2 149 LEU 149 265 265 LEU LEU D . n 
B 2 150 PRO 150 266 266 PRO PRO D . n 
B 2 151 VAL 151 267 267 VAL VAL D . n 
B 2 152 THR 152 268 268 THR THR D . n 
B 2 153 PRO 153 269 269 PRO PRO D . n 
B 2 154 GLY 154 270 270 GLY GLY D . n 
B 2 155 GLU 155 271 271 GLU GLU D . n 
B 2 156 PRO 156 272 272 PRO PRO D . n 
B 2 157 ALA 157 273 273 ALA ALA D . n 
B 2 158 SER 158 274 274 SER SER D . n 
B 2 159 ILE 159 275 275 ILE ILE D . n 
B 2 160 SER 160 276 276 SER SER D . n 
B 2 161 CYS 161 277 277 CYS CYS D . n 
B 2 162 ARG 162 278 278 ARG ARG D . n 
B 2 163 SER 163 279 279 SER SER D . n 
B 2 164 SER 164 280 280 SER SER D . n 
B 2 165 GLN 165 281 281 GLN GLN D . n 
B 2 166 ASN 166 282 282 ASN ASN D . n 
B 2 167 ILE 167 283 283 ILE ILE D . n 
B 2 168 VAL 168 284 284 VAL VAL D . n 
B 2 169 HIS 169 285 285 HIS HIS D . n 
B 2 170 ASN 170 286 286 ASN ASN D . n 
B 2 171 ASN 171 287 287 ASN ASN D . n 
B 2 172 GLY 172 288 288 GLY GLY D . n 
B 2 173 ILE 173 289 289 ILE ILE D . n 
B 2 174 THR 174 290 290 THR THR D . n 
B 2 175 TYR 175 291 291 TYR TYR D . n 
B 2 176 LEU 176 292 292 LEU LEU D . n 
B 2 177 GLU 177 293 293 GLU GLU D . n 
B 2 178 TRP 178 294 294 TRP TRP D . n 
B 2 179 TYR 179 295 295 TYR TYR D . n 
B 2 180 LEU 180 296 296 LEU LEU D . n 
B 2 181 GLN 181 297 297 GLN GLN D . n 
B 2 182 LYS 182 298 298 LYS LYS D . n 
B 2 183 PRO 183 299 299 PRO PRO D . n 
B 2 184 GLY 184 300 300 GLY GLY D . n 
B 2 185 GLN 185 301 301 GLN GLN D . n 
B 2 186 SER 186 302 302 SER SER D . n 
B 2 187 PRO 187 303 303 PRO PRO D . n 
B 2 188 GLN 188 304 304 GLN GLN D . n 
B 2 189 LEU 189 305 305 LEU LEU D . n 
B 2 190 LEU 190 306 306 LEU LEU D . n 
B 2 191 ILE 191 307 307 ILE ILE D . n 
B 2 192 TYR 192 308 308 TYR TYR D . n 
B 2 193 LYS 193 309 309 LYS LYS D . n 
B 2 194 VAL 194 310 310 VAL VAL D . n 
B 2 195 SER 195 311 311 SER SER D . n 
B 2 196 ASP 196 312 312 ASP ASP D . n 
B 2 197 ARG 197 313 313 ARG ARG D . n 
B 2 198 PHE 198 314 314 PHE PHE D . n 
B 2 199 SER 199 315 315 SER SER D . n 
B 2 200 GLY 200 316 316 GLY GLY D . n 
B 2 201 VAL 201 317 317 VAL VAL D . n 
B 2 202 PRO 202 318 318 PRO PRO D . n 
B 2 203 ASP 203 319 319 ASP ASP D . n 
B 2 204 ARG 204 320 320 ARG ARG D . n 
B 2 205 PHE 205 321 321 PHE PHE D . n 
B 2 206 SER 206 322 322 SER SER D . n 
B 2 207 GLY 207 323 323 GLY GLY D . n 
B 2 208 SER 208 324 324 SER SER D . n 
B 2 209 GLY 209 325 325 GLY GLY D . n 
B 2 210 SER 210 326 326 SER SER D . n 
B 2 211 GLY 211 327 327 GLY GLY D . n 
B 2 212 THR 212 328 328 THR THR D . n 
B 2 213 ASP 213 329 329 ASP ASP D . n 
B 2 214 PHE 214 330 330 PHE PHE D . n 
B 2 215 THR 215 331 331 THR THR D . n 
B 2 216 LEU 216 332 332 LEU LEU D . n 
B 2 217 LYS 217 333 333 LYS LYS D . n 
B 2 218 ILE 218 334 334 ILE ILE D . n 
B 2 219 SER 219 335 335 SER SER D . n 
B 2 220 ARG 220 336 336 ARG ARG D . n 
B 2 221 VAL 221 337 337 VAL VAL D . n 
B 2 222 GLU 222 338 338 GLU GLU D . n 
B 2 223 ALA 223 339 339 ALA ALA D . n 
B 2 224 GLU 224 340 340 GLU GLU D . n 
B 2 225 ASP 225 341 341 ASP ASP D . n 
B 2 226 VAL 226 342 342 VAL VAL D . n 
B 2 227 GLY 227 343 343 GLY GLY D . n 
B 2 228 VAL 228 344 344 VAL VAL D . n 
B 2 229 TYR 229 345 345 TYR TYR D . n 
B 2 230 TYR 230 346 346 TYR TYR D . n 
B 2 231 CYS 231 347 347 CYS CYS D . n 
B 2 232 PHE 232 348 348 PHE PHE D . n 
B 2 233 GLN 233 349 349 GLN GLN D . n 
B 2 234 GLY 234 350 350 GLY GLY D . n 
B 2 235 SER 235 351 351 SER SER D . n 
B 2 236 HIS 236 352 352 HIS HIS D . n 
B 2 237 ILE 237 353 353 ILE ILE D . n 
B 2 238 PRO 238 354 354 PRO PRO D . n 
B 2 239 PRO 239 355 355 PRO PRO D . n 
B 2 240 THR 240 356 356 THR THR D . n 
B 2 241 PHE 241 357 357 PHE PHE D . n 
B 2 242 GLY 242 358 358 GLY GLY D . n 
B 2 243 GLN 243 359 359 GLN GLN D . n 
B 2 244 GLY 244 360 360 GLY GLY D . n 
B 2 245 THR 245 361 361 THR THR D . n 
B 2 246 LYS 246 362 362 LYS LYS D . n 
B 2 247 VAL 247 363 363 VAL VAL D . n 
B 2 248 GLU 248 364 364 GLU GLU D . n 
B 2 249 ILE 249 365 365 ILE ILE D . n 
B 2 250 LYS 250 366 366 LYS LYS D . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 3 NAG 1 B NAG 1 B NAG 1 n 
C 3 NAG 2 B NAG 2 B NAG 2 n 
D 3 NAG 1 C NAG 1 C NAG 1 n 
D 3 NAG 2 C NAG 2 C NAG 2 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 4 NAG 1 701 1337 NAG NAG A . 
F 4 NAG 1 702 1504 NAG NAG A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IPB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9IPB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IPB 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IPB 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_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                            2.93 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                    ? 
# 
_struct.entry_id                     9IPB 
_struct.title                        'Local refinement structure of sEGFR and 528 Fv (from LH-type bispecific diabody Ex3) complex' 
_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        9IPB 
_struct_keywords.text            
'bispecific antibody, diabody, EGFR, LH, Ex3, 528, local refinement, ANTITUMOR PROTEIN, ANTITUMOR PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'ANTITUMOR PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 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 EGFR_HUMAN P00533 ? 1 
;LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENL
QIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHL
GSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTC
PPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGE
FKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLE
IIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQ
VCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAH
YIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS
;
25 
2 PDB 9IPB       9IPB   ? 2 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IPB A 1 ? 621 ? P00533 25  ? 645 ? 1   621 
2 2 9IPB D 1 ? 250 ? 9IPB   117 ? 366 ? 117 366 
# 
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 9IPB HIS A 622 ? UNP P00533 ? ? 'expression tag' 622 1 
1 9IPB HIS A 623 ? UNP P00533 ? ? 'expression tag' 623 2 
1 9IPB HIS A 624 ? UNP P00533 ? ? 'expression tag' 624 3 
1 9IPB HIS A 625 ? UNP P00533 ? ? 'expression tag' 625 4 
1 9IPB HIS A 626 ? UNP P00533 ? ? 'expression tag' 626 5 
1 9IPB HIS A 627 ? UNP P00533 ? ? 'expression tag' 627 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 PHE A 20  ? MET A 30  ? PHE A 20  MET A 30  1 ? 11 
HELX_P HELX_P2  AA2 GLN A 139 ? VAL A 144 ? GLN A 139 VAL A 144 1 ? 6  
HELX_P HELX_P3  AA3 ASP A 147 ? ASN A 151 ? ASP A 147 ASN A 151 5 ? 5  
HELX_P HELX_P4  AA4 ILE A 318 ? LYS A 322 ? ILE A 318 LYS A 322 5 ? 5  
HELX_P HELX_P5  AA5 LEU A 348 ? GLY A 354 ? LEU A 348 GLY A 354 1 ? 7  
HELX_P HELX_P6  AA6 ASP A 364 ? VAL A 374 ? ASP A 364 VAL A 374 5 ? 11 
HELX_P HELX_P7  AA7 LEU A 393 ? GLU A 397 ? LEU A 393 GLU A 397 5 ? 5  
HELX_P HELX_P8  AA8 LYS A 407 ? GLY A 410 ? LYS A 407 GLY A 410 5 ? 4  
HELX_P HELX_P9  AA9 ASN A 452 ? PHE A 457 ? ASN A 452 PHE A 457 1 ? 6  
HELX_P HELX_P10 AB1 GLY A 471 ? THR A 478 ? GLY A 471 THR A 478 1 ? 8  
HELX_P HELX_P11 AB2 GLU A 495 ? CYS A 499 ? GLU A 495 CYS A 499 5 ? 5  
HELX_P HELX_P12 AB3 GLU A 578 ? ASN A 580 ? GLU A 578 ASN A 580 5 ? 3  
HELX_P HELX_P13 AB4 THR B 28  ? TYR B 32  ? THR D 144 TYR D 148 5 ? 5  
HELX_P HELX_P14 AB5 ARG B 87  ? THR B 91  ? ARG D 203 THR D 207 5 ? 5  
HELX_P HELX_P15 AB6 GLU B 222 ? VAL B 226 ? GLU D 338 VAL D 342 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 7   SG  ? ? ? 1_555 A CYS 34  SG ? ? A CYS 7   A CYS 34  1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf2  disulf ?    ? A CYS 212 SG  ? ? ? 1_555 A CYS 224 SG ? ? A CYS 212 A CYS 224 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf3  disulf ?    ? A CYS 227 SG  ? ? ? 1_555 A CYS 236 SG ? ? A CYS 227 A CYS 236 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf4  disulf ?    ? A CYS 240 SG  ? ? ? 1_555 A CYS 267 SG ? ? A CYS 240 A CYS 267 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf5  disulf ?    ? A CYS 271 SG  ? ? ? 1_555 A CYS 283 SG ? ? A CYS 271 A CYS 283 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf6  disulf ?    ? A CYS 287 SG  ? ? ? 1_555 A CYS 302 SG ? ? A CYS 287 A CYS 302 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf7  disulf ?    ? A CYS 305 SG  ? ? ? 1_555 A CYS 309 SG ? ? A CYS 305 A CYS 309 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf8  disulf ?    ? A CYS 313 SG  ? ? ? 1_555 A CYS 338 SG ? ? A CYS 313 A CYS 338 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf9  disulf ?    ? A CYS 446 SG  ? ? ? 1_555 A CYS 475 SG ? ? A CYS 446 A CYS 475 1_555 ? ? ? ? ? ? ? 2.024 ? ?               
disulf10 disulf ?    ? A CYS 482 SG  ? ? ? 1_555 A CYS 491 SG ? ? A CYS 482 A CYS 491 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf11 disulf ?    ? A CYS 486 SG  ? ? ? 1_555 A CYS 499 SG ? ? A CYS 486 A CYS 499 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf12 disulf ?    ? A CYS 502 SG  ? ? ? 1_555 A CYS 511 SG ? ? A CYS 502 A CYS 511 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf13 disulf ?    ? A CYS 515 SG  ? ? ? 1_555 A CYS 531 SG ? ? A CYS 515 A CYS 531 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf14 disulf ?    ? A CYS 534 SG  ? ? ? 1_555 A CYS 547 SG ? ? A CYS 534 A CYS 547 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf15 disulf ?    ? A CYS 538 SG  ? ? ? 1_555 A CYS 555 SG ? ? A CYS 538 A CYS 555 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf16 disulf ?    ? A CYS 558 SG  ? ? ? 1_555 A CYS 567 SG ? ? A CYS 558 A CYS 567 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
disulf17 disulf ?    ? A CYS 571 SG  ? ? ? 1_555 A CYS 593 SG ? ? A CYS 571 A CYS 593 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf18 disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? D CYS 138 D CYS 212 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf19 disulf ?    ? B CYS 161 SG  ? ? ? 1_555 B CYS 231 SG ? ? D CYS 277 D CYS 347 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
covale1  covale one  ? A ASN 328 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 328 B NAG 1   1_555 ? ? ? ? ? ? ? 1.456 ? N-Glycosylation 
covale2  covale one  ? A ASN 337 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 337 A NAG 701 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale3  covale one  ? A ASN 420 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 420 C NAG 1   1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale4  covale one  ? A ASN 504 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 504 A NAG 702 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale5  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? B NAG 1   B NAG 2   1_555 ? ? ? ? ? ? ? 1.434 ? ?               
covale6  covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.443 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  NAG C .   ? ASN A 328 ? NAG B 1   ? 1_555 ASN A 328 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN A 420 ? NAG C 1   ? 1_555 ASN A 420 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN A 337 ? NAG A 701 ? 1_555 ASN A 337 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN A 504 ? NAG A 702 ? 1_555 ASN A 504 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  CYS A 7   ? CYS A 34  ? CYS A 7   ? 1_555 CYS A 34  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS A 212 ? CYS A 224 ? CYS A 212 ? 1_555 CYS A 224 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS A 227 ? CYS A 236 ? CYS A 227 ? 1_555 CYS A 236 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS A 240 ? CYS A 267 ? CYS A 240 ? 1_555 CYS A 267 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS A 271 ? CYS A 283 ? CYS A 271 ? 1_555 CYS A 283 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS A 287 ? CYS A 302 ? CYS A 287 ? 1_555 CYS A 302 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 305 ? CYS A 309 ? CYS A 305 ? 1_555 CYS A 309 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 313 ? CYS A 338 ? CYS A 313 ? 1_555 CYS A 338 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 446 ? CYS A 475 ? CYS A 446 ? 1_555 CYS A 475 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 482 ? CYS A 491 ? CYS A 482 ? 1_555 CYS A 491 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 486 ? CYS A 499 ? CYS A 486 ? 1_555 CYS A 499 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 502 ? CYS A 511 ? CYS A 502 ? 1_555 CYS A 511 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 515 ? CYS A 531 ? CYS A 515 ? 1_555 CYS A 531 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS A 534 ? CYS A 547 ? CYS A 534 ? 1_555 CYS A 547 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS A 538 ? CYS A 555 ? CYS A 538 ? 1_555 CYS A 555 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS A 558 ? CYS A 567 ? CYS A 558 ? 1_555 CYS A 567 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS A 571 ? CYS A 593 ? CYS A 571 ? 1_555 CYS A 593 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS B 22  ? CYS B 96  ? CYS D 138 ? 1_555 CYS D 212 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS B 161 ? CYS B 231 ? CYS D 277 ? 1_555 CYS D 347 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 5 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
# 
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 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA9 1 2 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? 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 6   ? CYS A 7   ? VAL A 6   CYS A 7   
AA1 2 VAL A 36  ? VAL A 37  ? VAL A 36  VAL A 37  
AA1 3 GLU A 60  ? VAL A 61  ? GLU A 60  VAL A 61  
AA1 4 ILE A 82  ? ILE A 83  ? ILE A 82  ILE A 83  
AA1 5 GLU A 118 ? ILE A 119 ? GLU A 118 ILE A 119 
AA2 1 LEU A 41  ? VAL A 46  ? LEU A 41  VAL A 46  
AA2 2 VAL A 65  ? ASN A 70  ? VAL A 65  ASN A 70  
AA2 3 TYR A 93  ? LEU A 98  ? TYR A 93  LEU A 98  
AA2 4 ALA A 123 ? SER A 127 ? ALA A 123 SER A 127 
AA3 1 PHE A 230 ? ARG A 231 ? PHE A 230 ARG A 231 
AA3 2 CYS A 236 ? LYS A 237 ? CYS A 236 LYS A 237 
AA4 1 MET A 244 ? TYR A 246 ? MET A 244 TYR A 246 
AA4 2 MET A 253 ? VAL A 255 ? MET A 253 VAL A 255 
AA5 1 TYR A 261 ? PHE A 263 ? TYR A 261 PHE A 263 
AA5 2 THR A 266 ? VAL A 268 ? THR A 266 VAL A 268 
AA6 1 VAL A 276 ? VAL A 277 ? VAL A 276 VAL A 277 
AA6 2 CYS A 283 ? VAL A 284 ? CYS A 283 VAL A 284 
AA7 1 SER A 291 ? GLU A 295 ? SER A 291 GLU A 295 
AA7 2 ARG A 300 ? LYS A 304 ? ARG A 300 LYS A 304 
AA8 1 LEU A 345 ? ILE A 347 ? LEU A 345 ILE A 347 
AA8 2 LEU A 381 ? ILE A 383 ? LEU A 381 ILE A 383 
AA8 3 PHE A 412 ? VAL A 417 ? PHE A 412 VAL A 417 
AA8 4 ASP A 436 ? SER A 440 ? ASP A 436 SER A 440 
AA9 1 GLU A 376 ? ILE A 377 ? GLU A 376 ILE A 377 
AA9 2 ILE A 401 ? ILE A 402 ? ILE A 401 ILE A 402 
AB1 1 GLU A 524 ? VAL A 526 ? GLU A 524 VAL A 526 
AB1 2 CYS A 531 ? GLN A 533 ? CYS A 531 GLN A 533 
AB2 1 HIS A 566 ? CYS A 567 ? HIS A 566 CYS A 567 
AB2 2 ILE A 562 ? ASP A 563 ? ILE A 562 ASP A 563 
AB2 3 VAL A 592 ? LEU A 595 ? VAL A 592 LEU A 595 
AB2 4 LEU A 582 ? ALA A 587 ? LEU A 582 ALA A 587 
AB2 5 ALA A 573 ? MET A 576 ? ALA A 573 MET A 576 
AB3 1 GLN B 3   ? GLN B 6   ? GLN D 119 GLN D 122 
AB3 2 VAL B 18  ? SER B 25  ? VAL D 134 SER D 141 
AB3 3 THR B 78  ? LEU B 83  ? THR D 194 LEU D 199 
AB3 4 VAL B 68  ? THR B 69  ? VAL D 184 THR D 185 
AB4 1 GLN B 3   ? GLN B 6   ? GLN D 119 GLN D 122 
AB4 2 VAL B 18  ? SER B 25  ? VAL D 134 SER D 141 
AB4 3 THR B 78  ? LEU B 83  ? THR D 194 LEU D 199 
AB4 4 ARG B 72  ? ASP B 73  ? ARG D 188 ASP D 189 
AB5 1 GLU B 10  ? LYS B 12  ? GLU D 126 LYS D 128 
AB5 2 THR B 112 ? VAL B 116 ? THR D 228 VAL D 232 
AB5 3 ALA B 92  ? CYS B 96  ? ALA D 208 CYS D 212 
AB5 4 TRP B 36  ? GLN B 39  ? TRP D 152 GLN D 155 
AB5 5 LEU B 45  ? TRP B 47  ? LEU D 161 TRP D 163 
AB6 1 GLY B 49  ? ASN B 50  ? GLY D 165 ASN D 166 
AB6 2 ASN B 59  ? TYR B 60  ? ASN D 175 TYR D 176 
AB7 1 MET B 142 ? THR B 143 ? MET D 258 THR D 259 
AB7 2 ALA B 157 ? SER B 163 ? ALA D 273 SER D 279 
AB7 3 ASP B 213 ? ILE B 218 ? ASP D 329 ILE D 334 
AB7 4 PHE B 205 ? SER B 210 ? PHE D 321 SER D 326 
AB8 1 PRO B 150 ? VAL B 151 ? PRO D 266 VAL D 267 
AB8 2 THR B 245 ? ILE B 249 ? THR D 361 ILE D 365 
AB8 3 GLY B 227 ? GLN B 233 ? GLY D 343 GLN D 349 
AB8 4 LEU B 176 ? GLN B 181 ? LEU D 292 GLN D 297 
AB8 5 GLN B 188 ? ILE B 191 ? GLN D 304 ILE D 307 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N CYS A 7   ? N CYS A 7   O VAL A 36  ? O VAL A 36  
AA1 2 3 N VAL A 37  ? N VAL A 37  O GLU A 60  ? O GLU A 60  
AA1 3 4 N VAL A 61  ? N VAL A 61  O ILE A 82  ? O ILE A 82  
AA1 4 5 N ILE A 83  ? N ILE A 83  O GLU A 118 ? O GLU A 118 
AA2 1 2 N LEU A 41  ? N LEU A 41  O LEU A 66  ? O LEU A 66  
AA2 2 3 N VAL A 65  ? N VAL A 65  O ALA A 94  ? O ALA A 94  
AA2 3 4 N LEU A 95  ? N LEU A 95  O ARG A 125 ? O ARG A 125 
AA3 1 2 N PHE A 230 ? N PHE A 230 O LYS A 237 ? O LYS A 237 
AA4 1 2 N LEU A 245 ? N LEU A 245 O ASP A 254 ? O ASP A 254 
AA5 1 2 N PHE A 263 ? N PHE A 263 O THR A 266 ? O THR A 266 
AA6 1 2 N VAL A 276 ? N VAL A 276 O VAL A 284 ? O VAL A 284 
AA7 1 2 N MET A 294 ? N MET A 294 O LYS A 301 ? O LYS A 301 
AA8 1 2 N LEU A 345 ? N LEU A 345 O LEU A 382 ? O LEU A 382 
AA8 2 3 N LEU A 381 ? N LEU A 381 O SER A 413 ? O SER A 413 
AA8 3 4 N LEU A 414 ? N LEU A 414 O ILE A 438 ? O ILE A 438 
AA9 1 2 N ILE A 377 ? N ILE A 377 O ILE A 401 ? O ILE A 401 
AB1 1 2 N PHE A 525 ? N PHE A 525 O ILE A 532 ? O ILE A 532 
AB2 1 2 O HIS A 566 ? O HIS A 566 N ASP A 563 ? N ASP A 563 
AB2 2 3 N ILE A 562 ? N ILE A 562 O CYS A 593 ? O CYS A 593 
AB2 3 4 O HIS A 594 ? O HIS A 594 N TYR A 586 ? N TYR A 586 
AB2 4 5 O VAL A 583 ? O VAL A 583 N VAL A 575 ? N VAL A 575 
AB3 1 2 N VAL B 5   ? N VAL D 121 O LYS B 23  ? O LYS D 139 
AB3 2 3 N VAL B 18  ? N VAL D 134 O LEU B 83  ? O LEU D 199 
AB3 3 4 O GLU B 82  ? O GLU D 198 N THR B 69  ? N THR D 185 
AB4 1 2 N VAL B 5   ? N VAL D 121 O LYS B 23  ? O LYS D 139 
AB4 2 3 N VAL B 18  ? N VAL D 134 O LEU B 83  ? O LEU D 199 
AB4 3 4 O THR B 78  ? O THR D 194 N ASP B 73  ? N ASP D 189 
AB5 1 2 N GLU B 10  ? N GLU D 126 O THR B 115 ? O THR D 231 
AB5 2 3 O THR B 112 ? O THR D 228 N TYR B 94  ? N TYR D 210 
AB5 3 4 O TYR B 95  ? O TYR D 211 N VAL B 37  ? N VAL D 153 
AB5 4 5 N ARG B 38  ? N ARG D 154 O GLU B 46  ? O GLU D 162 
AB6 1 2 N ASN B 50  ? N ASN D 166 O ASN B 59  ? O ASN D 175 
AB7 1 2 N THR B 143 ? N THR D 259 O ARG B 162 ? O ARG D 278 
AB7 2 3 N ILE B 159 ? N ILE D 275 O LEU B 216 ? O LEU D 332 
AB7 3 4 O THR B 215 ? O THR D 331 N SER B 208 ? N SER D 324 
AB8 1 2 N VAL B 151 ? N VAL D 267 O GLU B 248 ? O GLU D 364 
AB8 2 3 O VAL B 247 ? O VAL D 363 N GLY B 227 ? N GLY D 343 
AB8 3 4 O PHE B 232 ? O PHE D 348 N GLU B 177 ? N GLU D 293 
AB8 4 5 N TRP B 178 ? N TRP D 294 O LEU B 190 ? O LEU D 306 
# 
_pdbx_entry_details.entry_id                   9IPB 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    114 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE1 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    181 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.53 
# 
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 PHE A 31  ? ? -143.18 -6.53   
2  1 TYR A 45  ? ? 70.55   58.39   
3  1 LEU A 77  ? ? -158.42 35.96   
4  1 ILE A 143 ? ? -91.16  -66.85  
5  1 GLU A 181 ? ? 69.43   -63.71  
6  1 LYS A 185 ? ? 39.31   68.61   
7  1 THR A 187 ? ? -148.80 -16.82  
8  1 ALA A 213 ? ? -90.65  -60.06  
9  1 PRO A 219 ? ? -78.64  48.27   
10 1 GLU A 233 ? ? -146.86 -31.69  
11 1 ALA A 234 ? ? -153.91 -31.06  
12 1 ARG A 273 ? ? 58.98   -149.05 
13 1 GLU A 296 ? ? -87.18  -74.62  
14 1 ASP A 297 ? ? -78.27  -168.23 
15 1 LYS A 333 ? ? 90.75   -21.60  
16 1 ASN A 337 ? ? 37.97   41.64   
17 1 GLN A 411 ? ? -149.78 -65.11  
18 1 LEU A 426 ? ? -106.66 53.64   
19 1 SER A 433 ? ? -72.18  -70.86  
20 1 ASP A 434 ? ? -90.21  -60.87  
21 1 LYS A 463 ? ? -125.86 -169.89 
22 1 LYS A 465 ? ? -115.69 53.35   
23 1 PRO A 488 ? ? -48.81  -10.98  
24 1 ASP A 498 ? ? -91.82  55.35   
25 1 ASN A 544 ? ? -128.21 -153.39 
26 1 TYR D 291 ? ? -92.90  53.23   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9IPB 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9IPB 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.93 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               1085217 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX 
'LH-type bispecific antibody Ex3 composed of 528 and OKT3 Fvs in ternary complex with sEGFR and CD3gamma-epsilon' ? ? ? '1, 2' 
2 1 RECOMBINANT        COMPLEX 'Soluble Epidermal Growth Factor Receptor (sEGFR)' ? ? ? 1      
3 1 RECOMBINANT        COMPLEX 'LH-type bispecific diabody Ex3' ? ? ? 2      
# 
_em_imaging.entry_id                        9IPB 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'JEOL CRYO ARM 300' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             900 
_em_imaging.nominal_defocus_max             2400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9IPB 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9IPB 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A LEU 1   ? A LEU 1   
2   1 Y 1 A GLU 2   ? A GLU 2   
3   1 Y 1 A GLU 3   ? A GLU 3   
4   1 Y 1 A GLY 9   ? A GLY 9   
5   1 Y 1 A THR 10  ? A THR 10  
6   1 Y 1 A SER 11  ? A SER 11  
7   1 Y 1 A ASN 12  ? A ASN 12  
8   1 Y 1 A LYS 13  ? A LYS 13  
9   1 Y 1 A LEU 14  ? A LEU 14  
10  1 Y 1 A THR 15  ? A THR 15  
11  1 Y 1 A GLN 16  ? A GLN 16  
12  1 Y 1 A LEU 17  ? A LEU 17  
13  1 Y 1 A GLY 18  ? A GLY 18  
14  1 Y 1 A TYR 101 ? A TYR 101 
15  1 Y 1 A ASP 102 ? A ASP 102 
16  1 Y 1 A ALA 103 ? A ALA 103 
17  1 Y 1 A ASN 104 ? A ASN 104 
18  1 Y 1 A LYS 105 ? A LYS 105 
19  1 Y 1 A THR 106 ? A THR 106 
20  1 Y 1 A GLY 107 ? A GLY 107 
21  1 Y 1 A PHE 156 ? A PHE 156 
22  1 Y 1 A GLN 157 ? A GLN 157 
23  1 Y 1 A ASN 158 ? A ASN 158 
24  1 Y 1 A HIS 159 ? A HIS 159 
25  1 Y 1 A LEU 160 ? A LEU 160 
26  1 Y 1 A GLY 161 ? A GLY 161 
27  1 Y 1 A SER 162 ? A SER 162 
28  1 Y 1 A CYS 163 ? A CYS 163 
29  1 Y 1 A GLN 164 ? A GLN 164 
30  1 Y 1 A LYS 165 ? A LYS 165 
31  1 Y 1 A CYS 166 ? A CYS 166 
32  1 Y 1 A ASP 167 ? A ASP 167 
33  1 Y 1 A PRO 168 ? A PRO 168 
34  1 Y 1 A SER 169 ? A SER 169 
35  1 Y 1 A CYS 170 ? A CYS 170 
36  1 Y 1 A PRO 171 ? A PRO 171 
37  1 Y 1 A ASN 172 ? A ASN 172 
38  1 Y 1 A ILE 190 ? A ILE 190 
39  1 Y 1 A CYS 191 ? A CYS 191 
40  1 Y 1 A ALA 192 ? A ALA 192 
41  1 Y 1 A GLN 193 ? A GLN 193 
42  1 Y 1 A GLN 194 ? A GLN 194 
43  1 Y 1 A CYS 195 ? A CYS 195 
44  1 Y 1 A SER 196 ? A SER 196 
45  1 Y 1 A GLY 197 ? A GLY 197 
46  1 Y 1 A ARG 198 ? A ARG 198 
47  1 Y 1 A CYS 199 ? A CYS 199 
48  1 Y 1 A ARG 200 ? A ARG 200 
49  1 Y 1 A GLY 201 ? A GLY 201 
50  1 Y 1 A LYS 202 ? A LYS 202 
51  1 Y 1 A SER 203 ? A SER 203 
52  1 Y 1 A PRO 204 ? A PRO 204 
53  1 Y 1 A SER 205 ? A SER 205 
54  1 Y 1 A ASP 206 ? A ASP 206 
55  1 Y 1 A CYS 207 ? A CYS 207 
56  1 Y 1 A CYS 208 ? A CYS 208 
57  1 Y 1 A HIS 209 ? A HIS 209 
58  1 Y 1 A HIS 597 ? A HIS 597 
59  1 Y 1 A PRO 598 ? A PRO 598 
60  1 Y 1 A ASN 599 ? A ASN 599 
61  1 Y 1 A CYS 600 ? A CYS 600 
62  1 Y 1 A THR 601 ? A THR 601 
63  1 Y 1 A TYR 602 ? A TYR 602 
64  1 Y 1 A GLY 603 ? A GLY 603 
65  1 Y 1 A CYS 604 ? A CYS 604 
66  1 Y 1 A THR 605 ? A THR 605 
67  1 Y 1 A GLY 606 ? A GLY 606 
68  1 Y 1 A PRO 607 ? A PRO 607 
69  1 Y 1 A GLY 608 ? A GLY 608 
70  1 Y 1 A LEU 609 ? A LEU 609 
71  1 Y 1 A GLU 610 ? A GLU 610 
72  1 Y 1 A GLY 611 ? A GLY 611 
73  1 Y 1 A CYS 612 ? A CYS 612 
74  1 Y 1 A PRO 613 ? A PRO 613 
75  1 Y 1 A THR 614 ? A THR 614 
76  1 Y 1 A ASN 615 ? A ASN 615 
77  1 Y 1 A GLY 616 ? A GLY 616 
78  1 Y 1 A PRO 617 ? A PRO 617 
79  1 Y 1 A LYS 618 ? A LYS 618 
80  1 Y 1 A ILE 619 ? A ILE 619 
81  1 Y 1 A PRO 620 ? A PRO 620 
82  1 Y 1 A SER 621 ? A SER 621 
83  1 Y 1 A HIS 622 ? A HIS 622 
84  1 Y 1 A HIS 623 ? A HIS 623 
85  1 Y 1 A HIS 624 ? A HIS 624 
86  1 Y 1 A HIS 625 ? A HIS 625 
87  1 Y 1 A HIS 626 ? A HIS 626 
88  1 Y 1 A HIS 627 ? A HIS 627 
89  1 Y 1 D GLY 235 ? B GLY 119 
90  1 Y 1 D GLY 236 ? B GLY 120 
91  1 Y 1 D GLY 237 ? B GLY 121 
92  1 Y 1 D GLY 238 ? B GLY 122 
93  1 Y 1 D SER 239 ? B SER 123 
94  1 Y 1 D GLY 240 ? B GLY 124 
95  1 Y 1 D GLY 241 ? B GLY 125 
96  1 Y 1 D GLY 242 ? B GLY 126 
97  1 Y 1 D GLY 243 ? B GLY 127 
98  1 Y 1 D SER 244 ? B SER 128 
99  1 Y 1 D GLY 245 ? B GLY 129 
100 1 Y 1 D GLY 246 ? B GLY 130 
101 1 Y 1 D GLY 247 ? B GLY 131 
102 1 Y 1 D GLY 248 ? B GLY 132 
103 1 Y 1 D SER 249 ? B SER 133 
104 1 Y 1 D GLY 250 ? B GLY 134 
105 1 Y 1 D GLY 251 ? B GLY 135 
106 1 Y 1 D GLY 252 ? B GLY 136 
107 1 Y 1 D GLY 253 ? B GLY 137 
108 1 Y 1 D SER 254 ? B SER 138 
# 
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 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-10 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9IPB 
_em_admin.last_update        2025-05-28 
_em_admin.map_release_date   2025-05-28 
_em_admin.title              'Local refinement structure of sEGFR and 528 Fv (from LH-type bispecific diabody Ex3) complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 2 2 9606  'Homo sapiens'        ? ? ? ? ? 
? ? 3 3 32630 'synthetic construct' ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 2 2 10029 'Cricetulus griseus'         ? ? 
? 3 3 54911 'Brevibacillus choshinensis' ? ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
# 
_atom_sites.entry_id                    9IPB 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 4   ? 165.449 126.785 186.412 1.00 61.63  ? 4   LYS A N   1 
ATOM   2    C CA  . LYS A 1 4   ? 164.602 126.079 185.460 1.00 56.14  ? 4   LYS A CA  1 
ATOM   3    C C   . LYS A 1 4   ? 164.718 126.737 184.091 1.00 54.29  ? 4   LYS A C   1 
ATOM   4    O O   . LYS A 1 4   ? 164.506 127.947 183.959 1.00 53.39  ? 4   LYS A O   1 
ATOM   5    C CB  . LYS A 1 4   ? 163.151 126.079 185.937 1.00 49.10  ? 4   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 4   ? 162.920 125.316 187.231 1.00 48.81  ? 4   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 4   ? 161.465 125.398 187.663 1.00 48.04  ? 4   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 4   ? 161.236 124.670 188.977 1.00 46.12  ? 4   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 4   ? 159.822 124.781 189.430 1.00 47.37  ? 4   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 5   ? 165.057 125.945 183.077 1.00 53.95  ? 5   LYS A N   1 
ATOM   11   C CA  . LYS A 1 5   ? 165.147 126.468 181.721 1.00 55.54  ? 5   LYS A CA  1 
ATOM   12   C C   . LYS A 1 5   ? 163.772 126.909 181.239 1.00 52.44  ? 5   LYS A C   1 
ATOM   13   O O   . LYS A 1 5   ? 162.752 126.308 181.585 1.00 49.76  ? 5   LYS A O   1 
ATOM   14   C CB  . LYS A 1 5   ? 165.729 125.414 180.779 1.00 57.84  ? 5   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 5   ? 166.407 125.990 179.545 1.00 63.94  ? 5   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 5   ? 165.469 126.004 178.348 1.00 65.56  ? 5   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 5   ? 166.073 126.763 177.179 1.00 70.60  ? 5   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 5   ? 165.059 127.057 176.130 1.00 75.89  ? 5   LYS A NZ  1 
ATOM   19   N N   . VAL A 1 6   ? 163.746 127.969 180.434 1.00 55.82  ? 6   VAL A N   1 
ATOM   20   C CA  . VAL A 1 6   ? 162.502 128.621 180.052 1.00 55.90  ? 6   VAL A CA  1 
ATOM   21   C C   . VAL A 1 6   ? 162.433 128.765 178.538 1.00 63.09  ? 6   VAL A C   1 
ATOM   22   O O   . VAL A 1 6   ? 163.456 128.796 177.848 1.00 68.04  ? 6   VAL A O   1 
ATOM   23   C CB  . VAL A 1 6   ? 162.361 129.999 180.732 1.00 49.01  ? 6   VAL A CB  1 
ATOM   24   C CG1 . VAL A 1 6   ? 162.144 129.835 182.228 1.00 44.01  ? 6   VAL A CG1 1 
ATOM   25   C CG2 . VAL A 1 6   ? 163.586 130.855 180.455 1.00 51.75  ? 6   VAL A CG2 1 
ATOM   26   N N   . CYS A 1 7   ? 161.206 128.849 178.024 1.00 61.86  ? 7   CYS A N   1 
ATOM   27   C CA  . CYS A 1 7   ? 160.951 129.104 176.615 1.00 64.62  ? 7   CYS A CA  1 
ATOM   28   C C   . CYS A 1 7   ? 159.803 130.095 176.482 1.00 61.19  ? 7   CYS A C   1 
ATOM   29   O O   . CYS A 1 7   ? 158.965 130.223 177.378 1.00 56.34  ? 7   CYS A O   1 
ATOM   30   C CB  . CYS A 1 7   ? 160.628 127.814 175.847 1.00 68.91  ? 7   CYS A CB  1 
ATOM   31   S SG  . CYS A 1 7   ? 159.263 126.850 176.523 1.00 79.88  ? 7   CYS A SG  1 
ATOM   32   N N   . GLN A 1 8   ? 159.772 130.795 175.347 1.00 66.09  ? 8   GLN A N   1 
ATOM   33   C CA  . GLN A 1 8   ? 158.821 131.884 175.152 1.00 63.98  ? 8   GLN A CA  1 
ATOM   34   C C   . GLN A 1 8   ? 157.388 131.412 174.941 1.00 60.45  ? 8   GLN A C   1 
ATOM   35   O O   . GLN A 1 8   ? 156.462 132.192 175.184 1.00 60.38  ? 8   GLN A O   1 
ATOM   36   C CB  . GLN A 1 8   ? 159.251 132.742 173.961 1.00 69.12  ? 8   GLN A CB  1 
ATOM   37   C CG  . GLN A 1 8   ? 160.420 133.672 174.244 1.00 80.10  ? 8   GLN A CG  1 
ATOM   38   C CD  . GLN A 1 8   ? 161.767 132.991 174.083 1.00 81.75  ? 8   GLN A CD  1 
ATOM   39   O OE1 . GLN A 1 8   ? 161.919 131.808 174.387 1.00 78.52  ? 8   GLN A OE1 1 
ATOM   40   N NE2 . GLN A 1 8   ? 162.751 133.738 173.598 1.00 86.00  ? 8   GLN A NE2 1 
ATOM   41   N N   . THR A 1 19  ? 155.098 121.414 156.872 1.00 105.95 ? 19  THR A N   1 
ATOM   42   C CA  . THR A 1 19  ? 154.842 119.985 156.925 1.00 104.57 ? 19  THR A CA  1 
ATOM   43   C C   . THR A 1 19  ? 154.782 119.518 158.375 1.00 100.13 ? 19  THR A C   1 
ATOM   44   O O   . THR A 1 19  ? 155.221 120.210 159.298 1.00 98.82  ? 19  THR A O   1 
ATOM   45   C CB  . THR A 1 19  ? 155.921 119.208 156.169 1.00 104.25 ? 19  THR A CB  1 
ATOM   46   O OG1 . THR A 1 19  ? 157.104 119.122 156.975 1.00 103.24 ? 19  THR A OG1 1 
ATOM   47   C CG2 . THR A 1 19  ? 156.257 119.900 154.857 1.00 99.34  ? 19  THR A CG2 1 
ATOM   48   N N   . PHE A 1 20  ? 154.217 118.324 158.571 1.00 95.80  ? 20  PHE A N   1 
ATOM   49   C CA  . PHE A 1 20  ? 154.177 117.746 159.911 1.00 99.02  ? 20  PHE A CA  1 
ATOM   50   C C   . PHE A 1 20  ? 155.587 117.498 160.432 1.00 102.13 ? 20  PHE A C   1 
ATOM   51   O O   . PHE A 1 20  ? 155.862 117.681 161.626 1.00 101.80 ? 20  PHE A O   1 
ATOM   52   C CB  . PHE A 1 20  ? 153.362 116.452 159.903 1.00 91.13  ? 20  PHE A CB  1 
ATOM   53   C CG  . PHE A 1 20  ? 151.872 116.667 159.960 1.00 85.75  ? 20  PHE A CG  1 
ATOM   54   C CD1 . PHE A 1 20  ? 151.320 117.901 159.659 1.00 84.37  ? 20  PHE A CD1 1 
ATOM   55   C CD2 . PHE A 1 20  ? 151.024 115.632 160.317 1.00 79.32  ? 20  PHE A CD2 1 
ATOM   56   C CE1 . PHE A 1 20  ? 149.953 118.097 159.710 1.00 76.21  ? 20  PHE A CE1 1 
ATOM   57   C CE2 . PHE A 1 20  ? 149.656 115.822 160.372 1.00 77.11  ? 20  PHE A CE2 1 
ATOM   58   C CZ  . PHE A 1 20  ? 149.120 117.056 160.068 1.00 76.33  ? 20  PHE A CZ  1 
ATOM   59   N N   . GLU A 1 21  ? 156.498 117.089 159.545 1.00 101.97 ? 21  GLU A N   1 
ATOM   60   C CA  . GLU A 1 21  ? 157.898 116.937 159.925 1.00 101.53 ? 21  GLU A CA  1 
ATOM   61   C C   . GLU A 1 21  ? 158.494 118.264 160.379 1.00 103.23 ? 21  GLU A C   1 
ATOM   62   O O   . GLU A 1 21  ? 159.184 118.323 161.403 1.00 101.88 ? 21  GLU A O   1 
ATOM   63   C CB  . GLU A 1 21  ? 158.694 116.363 158.752 1.00 101.46 ? 21  GLU A CB  1 
ATOM   64   C CG  . GLU A 1 21  ? 160.189 116.253 158.997 1.00 104.22 ? 21  GLU A CG  1 
ATOM   65   C CD  . GLU A 1 21  ? 160.632 114.829 159.265 1.00 105.14 ? 21  GLU A CD  1 
ATOM   66   O OE1 . GLU A 1 21  ? 159.870 113.896 158.935 1.00 100.56 ? 21  GLU A OE1 1 
ATOM   67   O OE2 . GLU A 1 21  ? 161.743 114.642 159.804 1.00 106.03 ? 21  GLU A OE2 1 
ATOM   68   N N   . ASP A 1 22  ? 158.233 119.341 159.634 1.00 106.44 ? 22  ASP A N   1 
ATOM   69   C CA  . ASP A 1 22  ? 158.740 120.656 160.020 1.00 108.17 ? 22  ASP A CA  1 
ATOM   70   C C   . ASP A 1 22  ? 158.115 121.128 161.327 1.00 107.61 ? 22  ASP A C   1 
ATOM   71   O O   . ASP A 1 22  ? 158.795 121.735 162.168 1.00 103.36 ? 22  ASP A O   1 
ATOM   72   C CB  . ASP A 1 22  ? 158.476 121.667 158.905 1.00 104.56 ? 22  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 22  ? 159.211 121.326 157.624 1.00 101.90 ? 22  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 22  ? 160.318 120.755 157.706 1.00 105.13 ? 22  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 22  ? 158.679 121.629 156.535 1.00 98.04  ? 22  ASP A OD2 1 
ATOM   76   N N   . HIS A 1 23  ? 156.828 120.825 161.511 1.00 104.29 ? 23  HIS A N   1 
ATOM   77   C CA  . HIS A 1 23  ? 156.149 121.194 162.781 1.00 103.12 ? 23  HIS A CA  1 
ATOM   78   C C   . HIS A 1 23  ? 156.864 120.515 163.953 1.00 103.18 ? 23  HIS A C   1 
ATOM   79   O O   . HIS A 1 23  ? 157.283 121.225 164.891 1.00 100.85 ? 23  HIS A O   1 
ATOM   80   C CB  . HIS A 1 23  ? 154.667 120.809 162.747 1.00 97.53  ? 23  HIS A CB  1 
ATOM   81   C CG  . HIS A 1 23  ? 154.127 120.491 164.101 1.00 93.70  ? 23  HIS A CG  1 
ATOM   82   N ND1 . HIS A 1 23  ? 154.018 119.205 164.584 1.00 86.06  ? 23  HIS A ND1 1 
ATOM   83   C CD2 . HIS A 1 23  ? 153.669 121.292 165.070 1.00 85.31  ? 23  HIS A CD2 1 
ATOM   84   C CE1 . HIS A 1 23  ? 153.514 119.240 165.809 1.00 87.97  ? 23  HIS A CE1 1 
ATOM   85   N NE2 . HIS A 1 23  ? 153.292 120.498 166.122 1.00 86.08  ? 23  HIS A NE2 1 
ATOM   86   N N   . PHE A 1 24  ? 157.010 119.188 163.902 1.00 96.21  ? 24  PHE A N   1 
ATOM   87   C CA  . PHE A 1 24  ? 157.609 118.452 165.049 1.00 90.87  ? 24  PHE A CA  1 
ATOM   88   C C   . PHE A 1 24  ? 158.983 119.034 165.362 1.00 94.57  ? 24  PHE A C   1 
ATOM   89   O O   . PHE A 1 24  ? 159.290 119.259 166.550 1.00 96.48  ? 24  PHE A O   1 
ATOM   90   C CB  . PHE A 1 24  ? 157.699 116.953 164.755 1.00 92.76  ? 24  PHE A CB  1 
ATOM   91   C CG  . PHE A 1 24  ? 158.615 116.188 165.701 1.00 96.97  ? 24  PHE A CG  1 
ATOM   92   C CD1 . PHE A 1 24  ? 158.148 115.723 166.923 1.00 95.35  ? 24  PHE A CD1 1 
ATOM   93   C CD2 . PHE A 1 24  ? 159.939 115.928 165.364 1.00 97.26  ? 24  PHE A CD2 1 
ATOM   94   C CE1 . PHE A 1 24  ? 158.982 115.028 167.784 1.00 88.94  ? 24  PHE A CE1 1 
ATOM   95   C CE2 . PHE A 1 24  ? 160.766 115.227 166.226 1.00 95.30  ? 24  PHE A CE2 1 
ATOM   96   C CZ  . PHE A 1 24  ? 160.287 114.781 167.434 1.00 87.21  ? 24  PHE A CZ  1 
ATOM   97   N N   . LEU A 1 25  ? 159.792 119.275 164.329 1.00 99.84  ? 25  LEU A N   1 
ATOM   98   C CA  . LEU A 1 25  ? 161.170 119.780 164.559 1.00 104.03 ? 25  LEU A CA  1 
ATOM   99   C C   . LEU A 1 25  ? 161.093 121.103 165.333 1.00 101.86 ? 25  LEU A C   1 
ATOM   100  O O   . LEU A 1 25  ? 161.735 121.201 166.399 1.00 105.42 ? 25  LEU A O   1 
ATOM   101  C CB  . LEU A 1 25  ? 161.891 119.955 163.223 1.00 109.89 ? 25  LEU A CB  1 
ATOM   102  C CG  . LEU A 1 25  ? 162.084 118.682 162.394 1.00 110.64 ? 25  LEU A CG  1 
ATOM   103  C CD1 . LEU A 1 25  ? 162.667 119.002 161.028 1.00 105.91 ? 25  LEU A CD1 1 
ATOM   104  C CD2 . LEU A 1 25  ? 162.950 117.673 163.125 1.00 101.64 ? 25  LEU A CD2 1 
ATOM   105  N N   . SER A 1 26  ? 160.312 122.064 164.832 1.00 99.82  ? 26  SER A N   1 
ATOM   106  C CA  . SER A 1 26  ? 160.215 123.395 165.488 1.00 102.65 ? 26  SER A CA  1 
ATOM   107  C C   . SER A 1 26  ? 159.657 123.237 166.909 1.00 99.06  ? 26  SER A C   1 
ATOM   108  O O   . SER A 1 26  ? 160.229 123.841 167.841 1.00 92.19  ? 26  SER A O   1 
ATOM   109  C CB  . SER A 1 26  ? 159.364 124.335 164.675 1.00 103.81 ? 26  SER A CB  1 
ATOM   110  O OG  . SER A 1 26  ? 158.061 123.800 164.487 1.00 102.49 ? 26  SER A OG  1 
ATOM   111  N N   . LEU A 1 27  ? 158.572 122.475 167.056 1.00 95.68  ? 27  LEU A N   1 
ATOM   112  C CA  . LEU A 1 27  ? 157.952 122.270 168.389 1.00 87.89  ? 27  LEU A CA  1 
ATOM   113  C C   . LEU A 1 27  ? 159.005 121.697 169.348 1.00 90.27  ? 27  LEU A C   1 
ATOM   114  O O   . LEU A 1 27  ? 159.216 122.297 170.422 1.00 92.27  ? 27  LEU A O   1 
ATOM   115  C CB  . LEU A 1 27  ? 156.752 121.338 168.245 1.00 76.30  ? 27  LEU A CB  1 
ATOM   116  C CG  . LEU A 1 27  ? 155.900 121.142 169.502 1.00 64.72  ? 27  LEU A CG  1 
ATOM   117  C CD1 . LEU A 1 27  ? 155.412 122.480 170.029 1.00 70.49  ? 27  LEU A CD1 1 
ATOM   118  C CD2 . LEU A 1 27  ? 154.723 120.252 169.163 1.00 58.43  ? 27  LEU A CD2 1 
ATOM   119  N N   . GLN A 1 28  ? 159.647 120.591 168.967 1.00 90.20  ? 28  GLN A N   1 
ATOM   120  C CA  . GLN A 1 28  ? 160.638 119.936 169.859 1.00 87.70  ? 28  GLN A CA  1 
ATOM   121  C C   . GLN A 1 28  ? 161.789 120.920 170.126 1.00 94.33  ? 28  GLN A C   1 
ATOM   122  O O   . GLN A 1 28  ? 162.286 120.947 171.265 1.00 96.21  ? 28  GLN A O   1 
ATOM   123  C CB  . GLN A 1 28  ? 161.139 118.651 169.199 1.00 91.17  ? 28  GLN A CB  1 
ATOM   124  C CG  . GLN A 1 28  ? 162.437 118.808 168.414 1.00 93.27  ? 28  GLN A CG  1 
ATOM   125  C CD  . GLN A 1 28  ? 162.894 117.530 167.747 1.00 95.66  ? 28  GLN A CD  1 
ATOM   126  O OE1 . GLN A 1 28  ? 163.072 117.467 166.526 1.00 97.84  ? 28  GLN A OE1 1 
ATOM   127  N NE2 . GLN A 1 28  ? 163.087 116.494 168.550 1.00 92.47  ? 28  GLN A NE2 1 
ATOM   128  N N   . ARG A 1 29  ? 162.187 121.686 169.121 1.00 97.04  ? 29  ARG A N   1 
ATOM   129  C CA  . ARG A 1 29  ? 163.277 122.635 169.273 1.00 98.53  ? 29  ARG A CA  1 
ATOM   130  C C   . ARG A 1 29  ? 162.968 123.723 170.291 1.00 100.89 ? 29  ARG A C   1 
ATOM   131  O O   . ARG A 1 29  ? 163.833 124.117 171.073 1.00 101.74 ? 29  ARG A O   1 
ATOM   132  C CB  . ARG A 1 29  ? 163.619 123.274 167.927 1.00 101.65 ? 29  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 29  ? 164.797 124.228 167.993 1.00 106.75 ? 29  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 29  ? 165.961 123.585 168.728 1.00 112.31 ? 29  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 29  ? 167.130 124.457 168.781 1.00 114.95 ? 29  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 29  ? 167.323 125.392 169.705 1.00 112.94 ? 29  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 29  ? 166.420 125.584 170.657 1.00 110.67 ? 29  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 29  ? 168.419 126.138 169.675 1.00 106.70 ? 29  ARG A NH2 1 
ATOM   139  N N   . MET A 1 30  ? 161.730 124.205 170.281 1.00 101.89 ? 30  MET A N   1 
ATOM   140  C CA  . MET A 1 30  ? 161.322 125.302 171.198 1.00 102.44 ? 30  MET A CA  1 
ATOM   141  C C   . MET A 1 30  ? 160.801 124.707 172.514 1.00 91.87  ? 30  MET A C   1 
ATOM   142  O O   . MET A 1 30  ? 160.300 125.484 173.354 1.00 87.70  ? 30  MET A O   1 
ATOM   143  C CB  . MET A 1 30  ? 160.226 126.159 170.555 1.00 98.35  ? 30  MET A CB  1 
ATOM   144  C CG  . MET A 1 30  ? 160.133 127.571 171.100 1.00 93.30  ? 30  MET A CG  1 
ATOM   145  S SD  . MET A 1 30  ? 158.913 128.561 170.214 1.00 98.09  ? 30  MET A SD  1 
ATOM   146  C CE  . MET A 1 30  ? 157.467 127.504 170.367 1.00 89.83  ? 30  MET A CE  1 
ATOM   147  N N   . PHE A 1 31  ? 160.915 123.389 172.694 1.00 83.84  ? 31  PHE A N   1 
ATOM   148  C CA  . PHE A 1 31  ? 160.322 122.781 173.915 1.00 71.69  ? 31  PHE A CA  1 
ATOM   149  C C   . PHE A 1 31  ? 161.172 121.645 174.473 1.00 71.98  ? 31  PHE A C   1 
ATOM   150  O O   . PHE A 1 31  ? 160.813 121.160 175.566 1.00 65.76  ? 31  PHE A O   1 
ATOM   151  C CB  . PHE A 1 31  ? 158.911 122.260 173.624 1.00 71.44  ? 31  PHE A CB  1 
ATOM   152  C CG  . PHE A 1 31  ? 157.812 123.307 173.732 1.00 70.99  ? 31  PHE A CG  1 
ATOM   153  C CD1 . PHE A 1 31  ? 157.184 123.557 174.947 1.00 59.35  ? 31  PHE A CD1 1 
ATOM   154  C CD2 . PHE A 1 31  ? 157.406 124.037 172.621 1.00 72.38  ? 31  PHE A CD2 1 
ATOM   155  C CE1 . PHE A 1 31  ? 156.184 124.510 175.045 1.00 53.33  ? 31  PHE A CE1 1 
ATOM   156  C CE2 . PHE A 1 31  ? 156.405 124.988 172.726 1.00 65.55  ? 31  PHE A CE2 1 
ATOM   157  C CZ  . PHE A 1 31  ? 155.796 125.223 173.936 1.00 57.46  ? 31  PHE A CZ  1 
ATOM   158  N N   . ASN A 1 32  ? 162.243 121.216 173.791 1.00 86.63  ? 32  ASN A N   1 
ATOM   159  C CA  . ASN A 1 32  ? 162.955 120.085 174.387 1.00 92.15  ? 32  ASN A CA  1 
ATOM   160  C C   . ASN A 1 32  ? 163.587 120.452 175.724 1.00 83.10  ? 32  ASN A C   1 
ATOM   161  O O   . ASN A 1 32  ? 163.466 119.706 176.702 1.00 77.52  ? 32  ASN A O   1 
ATOM   162  C CB  . ASN A 1 32  ? 164.021 119.560 173.426 1.00 89.15  ? 32  ASN A CB  1 
ATOM   163  C CG  . ASN A 1 32  ? 164.997 120.638 172.994 1.00 94.29  ? 32  ASN A CG  1 
ATOM   164  O OD1 . ASN A 1 32  ? 164.668 121.824 172.993 1.00 91.70  ? 32  ASN A OD1 1 
ATOM   165  N ND2 . ASN A 1 32  ? 166.205 120.230 172.623 1.00 92.44  ? 32  ASN A ND2 1 
ATOM   166  N N   . ASN A 1 33  ? 164.266 121.594 175.787 1.00 79.48  ? 33  ASN A N   1 
ATOM   167  C CA  . ASN A 1 33  ? 164.955 122.003 177.001 1.00 76.83  ? 33  ASN A CA  1 
ATOM   168  C C   . ASN A 1 33  ? 164.066 122.782 177.959 1.00 76.75  ? 33  ASN A C   1 
ATOM   169  O O   . ASN A 1 33  ? 164.483 123.037 179.094 1.00 71.24  ? 33  ASN A O   1 
ATOM   170  C CB  . ASN A 1 33  ? 166.186 122.843 176.648 1.00 81.13  ? 33  ASN A CB  1 
ATOM   171  C CG  . ASN A 1 33  ? 165.980 123.682 175.402 1.00 87.63  ? 33  ASN A CG  1 
ATOM   172  O OD1 . ASN A 1 33  ? 164.876 124.159 175.136 1.00 85.29  ? 33  ASN A OD1 1 
ATOM   173  N ND2 . ASN A 1 33  ? 167.044 123.865 174.629 1.00 92.94  ? 33  ASN A ND2 1 
ATOM   174  N N   . CYS A 1 34  ? 162.859 123.153 177.540 1.00 73.40  ? 34  CYS A N   1 
ATOM   175  C CA  . CYS A 1 34  ? 162.000 123.988 178.367 1.00 56.64  ? 34  CYS A CA  1 
ATOM   176  C C   . CYS A 1 34  ? 161.556 123.250 179.623 1.00 46.40  ? 34  CYS A C   1 
ATOM   177  O O   . CYS A 1 34  ? 161.301 122.043 179.601 1.00 43.91  ? 34  CYS A O   1 
ATOM   178  C CB  . CYS A 1 34  ? 160.777 124.444 177.574 1.00 48.19  ? 34  CYS A CB  1 
ATOM   179  S SG  . CYS A 1 34  ? 160.050 125.981 178.179 1.00 59.66  ? 34  CYS A SG  1 
ATOM   180  N N   . GLU A 1 35  ? 161.470 123.992 180.726 1.00 42.43  ? 35  GLU A N   1 
ATOM   181  C CA  . GLU A 1 35  ? 160.959 123.466 181.984 1.00 34.16  ? 35  GLU A CA  1 
ATOM   182  C C   . GLU A 1 35  ? 159.798 124.330 182.455 1.00 31.11  ? 35  GLU A C   1 
ATOM   183  O O   . GLU A 1 35  ? 158.846 123.832 183.063 1.00 31.61  ? 35  GLU A O   1 
ATOM   184  C CB  . GLU A 1 35  ? 162.067 123.417 183.038 1.00 37.58  ? 35  GLU A CB  1 
ATOM   185  C CG  . GLU A 1 35  ? 161.617 122.917 184.399 1.00 35.86  ? 35  GLU A CG  1 
ATOM   186  C CD  . GLU A 1 35  ? 162.716 122.180 185.137 1.00 50.01  ? 35  GLU A CD  1 
ATOM   187  O OE1 . GLU A 1 35  ? 163.655 121.691 184.474 1.00 50.80  ? 35  GLU A OE1 1 
ATOM   188  O OE2 . GLU A 1 35  ? 162.644 122.091 186.381 1.00 62.35  ? 35  GLU A OE2 1 
ATOM   189  N N   . VAL A 1 36  ? 159.873 125.628 182.173 1.00 33.59  ? 36  VAL A N   1 
ATOM   190  C CA  . VAL A 1 36  ? 158.810 126.580 182.476 1.00 30.28  ? 36  VAL A CA  1 
ATOM   191  C C   . VAL A 1 36  ? 158.516 127.348 181.196 1.00 33.79  ? 36  VAL A C   1 
ATOM   192  O O   . VAL A 1 36  ? 159.412 127.988 180.633 1.00 41.22  ? 36  VAL A O   1 
ATOM   193  C CB  . VAL A 1 36  ? 159.192 127.539 183.612 1.00 30.64  ? 36  VAL A CB  1 
ATOM   194  C CG1 . VAL A 1 36  ? 158.161 128.648 183.736 1.00 30.83  ? 36  VAL A CG1 1 
ATOM   195  C CG2 . VAL A 1 36  ? 159.329 126.783 184.924 1.00 33.14  ? 36  VAL A CG2 1 
ATOM   196  N N   . VAL A 1 37  ? 157.286 127.222 180.692 1.00 30.07  ? 37  VAL A N   1 
ATOM   197  C CA  . VAL A 1 37  ? 156.900 127.908 179.422 1.00 33.64  ? 37  VAL A CA  1 
ATOM   198  C C   . VAL A 1 37  ? 156.271 129.260 179.784 1.00 34.59  ? 37  VAL A C   1 
ATOM   199  O O   . VAL A 1 37  ? 155.245 129.258 180.489 1.00 32.68  ? 37  VAL A O   1 
ATOM   200  C CB  . VAL A 1 37  ? 155.927 127.062 178.579 1.00 31.90  ? 37  VAL A CB  1 
ATOM   201  C CG1 . VAL A 1 37  ? 155.681 127.678 177.207 1.00 39.45  ? 37  VAL A CG1 1 
ATOM   202  C CG2 . VAL A 1 37  ? 156.392 125.618 178.447 1.00 27.32  ? 37  VAL A CG2 1 
ATOM   203  N N   . LEU A 1 38  ? 156.869 130.361 179.326 1.00 42.89  ? 38  LEU A N   1 
ATOM   204  C CA  . LEU A 1 38  ? 156.350 131.712 179.666 1.00 39.21  ? 38  LEU A CA  1 
ATOM   205  C C   . LEU A 1 38  ? 155.129 132.018 178.787 1.00 42.13  ? 38  LEU A C   1 
ATOM   206  O O   . LEU A 1 38  ? 154.425 133.009 179.077 1.00 44.67  ? 38  LEU A O   1 
ATOM   207  C CB  . LEU A 1 38  ? 157.436 132.773 179.499 1.00 46.37  ? 38  LEU A CB  1 
ATOM   208  C CG  . LEU A 1 38  ? 158.491 132.837 180.607 1.00 43.39  ? 38  LEU A CG  1 
ATOM   209  C CD1 . LEU A 1 38  ? 157.858 132.706 181.981 1.00 32.12  ? 38  LEU A CD1 1 
ATOM   210  C CD2 . LEU A 1 38  ? 159.556 131.783 180.401 1.00 41.58  ? 38  LEU A CD2 1 
ATOM   211  N N   . GLY A 1 39  ? 154.893 131.200 177.757 1.00 46.56  ? 39  GLY A N   1 
ATOM   212  C CA  . GLY A 1 39  ? 153.763 131.437 176.841 1.00 43.10  ? 39  GLY A CA  1 
ATOM   213  C C   . GLY A 1 39  ? 152.766 130.298 176.862 1.00 39.56  ? 39  GLY A C   1 
ATOM   214  O O   . GLY A 1 39  ? 152.395 129.863 177.969 1.00 36.77  ? 39  GLY A O   1 
ATOM   215  N N   . ASN A 1 40  ? 152.357 129.816 175.687 1.00 38.67  ? 40  ASN A N   1 
ATOM   216  C CA  . ASN A 1 40  ? 151.336 128.782 175.604 1.00 33.41  ? 40  ASN A CA  1 
ATOM   217  C C   . ASN A 1 40  ? 151.930 127.532 174.974 1.00 34.95  ? 40  ASN A C   1 
ATOM   218  O O   . ASN A 1 40  ? 152.545 127.602 173.905 1.00 43.97  ? 40  ASN A O   1 
ATOM   219  C CB  . ASN A 1 40  ? 150.136 129.271 174.793 1.00 40.63  ? 40  ASN A CB  1 
ATOM   220  C CG  . ASN A 1 40  ? 149.817 130.729 175.051 1.00 50.71  ? 40  ASN A CG  1 
ATOM   221  O OD1 . ASN A 1 40  ? 149.388 131.098 176.144 1.00 52.24  ? 40  ASN A OD1 1 
ATOM   222  N ND2 . ASN A 1 40  ? 150.027 131.568 174.043 1.00 56.13  ? 40  ASN A ND2 1 
ATOM   223  N N   . LEU A 1 41  ? 151.744 126.395 175.638 1.00 26.34  ? 41  LEU A N   1 
ATOM   224  C CA  . LEU A 1 41  ? 152.211 125.113 175.124 1.00 22.78  ? 41  LEU A CA  1 
ATOM   225  C C   . LEU A 1 41  ? 151.194 124.604 174.111 1.00 31.36  ? 41  LEU A C   1 
ATOM   226  O O   . LEU A 1 41  ? 150.064 124.261 174.471 1.00 35.71  ? 41  LEU A O   1 
ATOM   227  C CB  . LEU A 1 41  ? 152.408 124.126 176.272 1.00 20.40  ? 41  LEU A CB  1 
ATOM   228  C CG  . LEU A 1 41  ? 152.323 122.621 176.014 1.00 20.95  ? 41  LEU A CG  1 
ATOM   229  C CD1 . LEU A 1 41  ? 153.407 122.162 175.059 1.00 35.31  ? 41  LEU A CD1 1 
ATOM   230  C CD2 . LEU A 1 41  ? 152.415 121.863 177.325 1.00 24.96  ? 41  LEU A CD2 1 
ATOM   231  N N   . GLU A 1 42  ? 151.579 124.606 172.832 1.00 39.57  ? 42  GLU A N   1 
ATOM   232  C CA  . GLU A 1 42  ? 150.622 124.214 171.765 1.00 34.73  ? 42  GLU A CA  1 
ATOM   233  C C   . GLU A 1 42  ? 151.189 123.041 170.953 1.00 37.74  ? 42  GLU A C   1 
ATOM   234  O O   . GLU A 1 42  ? 152.024 123.293 170.059 1.00 46.03  ? 42  GLU A O   1 
ATOM   235  C CB  . GLU A 1 42  ? 150.348 125.423 170.873 1.00 37.53  ? 42  GLU A CB  1 
ATOM   236  C CG  . GLU A 1 42  ? 149.843 126.636 171.647 1.00 38.17  ? 42  GLU A CG  1 
ATOM   237  C CD  . GLU A 1 42  ? 149.858 127.922 170.842 1.00 51.35  ? 42  GLU A CD  1 
ATOM   238  O OE1 . GLU A 1 42  ? 150.253 127.871 169.659 1.00 60.23  ? 42  GLU A OE1 1 
ATOM   239  O OE2 . GLU A 1 42  ? 149.484 128.975 171.398 1.00 53.32  ? 42  GLU A OE2 1 
ATOM   240  N N   . ILE A 1 43  ? 150.737 121.818 171.240 1.00 33.52  ? 43  ILE A N   1 
ATOM   241  C CA  . ILE A 1 43  ? 151.181 120.616 170.471 1.00 40.22  ? 43  ILE A CA  1 
ATOM   242  C C   . ILE A 1 43  ? 150.101 120.305 169.425 1.00 53.44  ? 43  ILE A C   1 
ATOM   243  O O   . ILE A 1 43  ? 149.091 119.683 169.810 1.00 54.67  ? 43  ILE A O   1 
ATOM   244  C CB  . ILE A 1 43  ? 151.393 119.437 171.435 1.00 39.80  ? 43  ILE A CB  1 
ATOM   245  C CG1 . ILE A 1 43  ? 151.913 119.918 172.786 1.00 35.01  ? 43  ILE A CG1 1 
ATOM   246  C CG2 . ILE A 1 43  ? 152.303 118.376 170.819 1.00 49.60  ? 43  ILE A CG2 1 
ATOM   247  C CD1 . ILE A 1 43  ? 151.970 118.838 173.849 1.00 33.96  ? 43  ILE A CD1 1 
ATOM   248  N N   . THR A 1 44  ? 150.293 120.713 168.163 1.00 60.20  ? 44  THR A N   1 
ATOM   249  C CA  . THR A 1 44  ? 149.219 120.541 167.154 1.00 56.21  ? 44  THR A CA  1 
ATOM   250  C C   . THR A 1 44  ? 149.795 120.106 165.823 1.00 64.54  ? 44  THR A C   1 
ATOM   251  O O   . THR A 1 44  ? 150.846 120.658 165.447 1.00 71.10  ? 44  THR A O   1 
ATOM   252  C CB  . THR A 1 44  ? 148.454 121.855 167.002 1.00 50.73  ? 44  THR A CB  1 
ATOM   253  O OG1 . THR A 1 44  ? 149.432 122.794 166.566 1.00 53.90  ? 44  THR A OG1 1 
ATOM   254  C CG2 . THR A 1 44  ? 147.823 122.339 168.294 1.00 44.62  ? 44  THR A CG2 1 
ATOM   255  N N   . TYR A 1 45  ? 149.136 119.172 165.123 1.00 65.50  ? 45  TYR A N   1 
ATOM   256  C CA  . TYR A 1 45  ? 149.562 118.753 163.756 1.00 70.18  ? 45  TYR A CA  1 
ATOM   257  C C   . TYR A 1 45  ? 150.862 117.953 163.809 1.00 77.99  ? 45  TYR A C   1 
ATOM   258  O O   . TYR A 1 45  ? 151.857 118.378 163.183 1.00 85.93  ? 45  TYR A O   1 
ATOM   259  C CB  . TYR A 1 45  ? 149.630 119.979 162.837 1.00 68.61  ? 45  TYR A CB  1 
ATOM   260  C CG  . TYR A 1 45  ? 148.358 120.815 162.863 1.00 69.04  ? 45  TYR A CG  1 
ATOM   261  C CD1 . TYR A 1 45  ? 147.114 120.222 163.046 1.00 60.78  ? 45  TYR A CD1 1 
ATOM   262  C CD2 . TYR A 1 45  ? 148.403 122.197 162.732 1.00 71.86  ? 45  TYR A CD2 1 
ATOM   263  C CE1 . TYR A 1 45  ? 145.954 120.975 163.082 1.00 61.38  ? 45  TYR A CE1 1 
ATOM   264  C CE2 . TYR A 1 45  ? 147.249 122.962 162.766 1.00 70.23  ? 45  TYR A CE2 1 
ATOM   265  C CZ  . TYR A 1 45  ? 146.021 122.349 162.941 1.00 68.57  ? 45  TYR A CZ  1 
ATOM   266  O OH  . TYR A 1 45  ? 144.879 123.095 162.976 1.00 70.13  ? 45  TYR A OH  1 
ATOM   267  N N   . VAL A 1 46  ? 150.843 116.843 164.552 1.00 74.79  ? 46  VAL A N   1 
ATOM   268  C CA  . VAL A 1 46  ? 152.030 115.939 164.594 1.00 83.64  ? 46  VAL A CA  1 
ATOM   269  C C   . VAL A 1 46  ? 151.611 114.624 163.921 1.00 90.16  ? 46  VAL A C   1 
ATOM   270  O O   . VAL A 1 46  ? 150.496 114.139 164.214 1.00 90.45  ? 46  VAL A O   1 
ATOM   271  C CB  . VAL A 1 46  ? 152.590 115.705 166.010 1.00 83.38  ? 46  VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 46  ? 151.556 115.090 166.943 1.00 72.45  ? 46  VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 46  ? 153.862 114.867 165.977 1.00 97.49  ? 46  VAL A CG2 1 
ATOM   274  N N   . GLN A 1 47  ? 152.456 114.084 163.044 1.00 89.53  ? 47  GLN A N   1 
ATOM   275  C CA  . GLN A 1 47  ? 152.135 112.875 162.299 1.00 92.67  ? 47  GLN A CA  1 
ATOM   276  C C   . GLN A 1 47  ? 152.374 111.628 163.149 1.00 92.30  ? 47  GLN A C   1 
ATOM   277  O O   . GLN A 1 47  ? 152.864 111.690 164.279 1.00 91.31  ? 47  GLN A O   1 
ATOM   278  C CB  . GLN A 1 47  ? 152.945 112.816 161.006 1.00 95.71  ? 47  GLN A CB  1 
ATOM   279  C CG  . GLN A 1 47  ? 154.428 112.574 161.210 1.00 97.30  ? 47  GLN A CG  1 
ATOM   280  C CD  . GLN A 1 47  ? 155.218 113.863 161.276 1.00 93.01  ? 47  GLN A CD  1 
ATOM   281  O OE1 . GLN A 1 47  ? 155.052 114.661 162.199 1.00 91.08  ? 47  GLN A OE1 1 
ATOM   282  N NE2 . GLN A 1 47  ? 156.086 114.076 160.294 1.00 92.64  ? 47  GLN A NE2 1 
ATOM   283  N N   . ARG A 1 48  ? 152.027 110.473 162.582 1.00 93.68  ? 48  ARG A N   1 
ATOM   284  C CA  . ARG A 1 48  ? 152.061 109.215 163.317 1.00 91.07  ? 48  ARG A CA  1 
ATOM   285  C C   . ARG A 1 48  ? 153.489 108.810 163.661 1.00 93.90  ? 48  ARG A C   1 
ATOM   286  O O   . ARG A 1 48  ? 154.390 108.890 162.820 1.00 96.41  ? 48  ARG A O   1 
ATOM   287  C CB  . ARG A 1 48  ? 151.395 108.110 162.498 1.00 92.23  ? 48  ARG A CB  1 
ATOM   288  C CG  . ARG A 1 48  ? 149.897 108.271 162.311 1.00 85.21  ? 48  ARG A CG  1 
ATOM   289  C CD  . ARG A 1 48  ? 149.170 108.228 163.642 1.00 87.02  ? 48  ARG A CD  1 
ATOM   290  N NE  . ARG A 1 48  ? 149.508 107.040 164.416 1.00 89.27  ? 48  ARG A NE  1 
ATOM   291  C CZ  . ARG A 1 48  ? 148.760 105.946 164.477 1.00 81.96  ? 48  ARG A CZ  1 
ATOM   292  N NH1 . ARG A 1 48  ? 147.618 105.853 163.817 1.00 67.30  ? 48  ARG A NH1 1 
ATOM   293  N NH2 . ARG A 1 48  ? 149.169 104.921 165.219 1.00 84.18  ? 48  ARG A NH2 1 
ATOM   294  N N   . ASN A 1 49  ? 153.684 108.366 164.905 1.00 93.38  ? 49  ASN A N   1 
ATOM   295  C CA  . ASN A 1 49  ? 154.925 107.722 165.346 1.00 98.53  ? 49  ASN A CA  1 
ATOM   296  C C   . ASN A 1 49  ? 156.153 108.582 165.057 1.00 100.77 ? 49  ASN A C   1 
ATOM   297  O O   . ASN A 1 49  ? 157.186 108.093 164.594 1.00 96.54  ? 49  ASN A O   1 
ATOM   298  C CB  . ASN A 1 49  ? 155.073 106.337 164.714 1.00 98.64  ? 49  ASN A CB  1 
ATOM   299  C CG  . ASN A 1 49  ? 153.757 105.591 164.631 1.00 97.43  ? 49  ASN A CG  1 
ATOM   300  O OD1 . ASN A 1 49  ? 153.153 105.488 163.564 1.00 92.85  ? 49  ASN A OD1 1 
ATOM   301  N ND2 . ASN A 1 49  ? 153.304 105.064 165.764 1.00 95.01  ? 49  ASN A ND2 1 
ATOM   302  N N   . TYR A 1 50  ? 156.042 109.880 165.333 1.00 101.43 ? 50  TYR A N   1 
ATOM   303  C CA  . TYR A 1 50  ? 157.166 110.787 165.178 1.00 100.52 ? 50  TYR A CA  1 
ATOM   304  C C   . TYR A 1 50  ? 157.490 111.551 166.455 1.00 96.58  ? 50  TYR A C   1 
ATOM   305  O O   . TYR A 1 50  ? 158.538 112.203 166.516 1.00 92.50  ? 50  TYR A O   1 
ATOM   306  C CB  . TYR A 1 50  ? 156.900 111.777 164.031 1.00 96.52  ? 50  TYR A CB  1 
ATOM   307  C CG  . TYR A 1 50  ? 158.128 112.512 163.539 1.00 97.39  ? 50  TYR A CG  1 
ATOM   308  C CD1 . TYR A 1 50  ? 159.387 111.929 163.614 1.00 97.61  ? 50  TYR A CD1 1 
ATOM   309  C CD2 . TYR A 1 50  ? 158.026 113.775 162.970 1.00 95.06  ? 50  TYR A CD2 1 
ATOM   310  C CE1 . TYR A 1 50  ? 160.511 112.592 163.159 1.00 99.15  ? 50  TYR A CE1 1 
ATOM   311  C CE2 . TYR A 1 50  ? 159.143 114.442 162.504 1.00 96.15  ? 50  TYR A CE2 1 
ATOM   312  C CZ  . TYR A 1 50  ? 160.383 113.848 162.606 1.00 98.20  ? 50  TYR A CZ  1 
ATOM   313  O OH  . TYR A 1 50  ? 161.500 114.509 162.151 1.00 97.37  ? 50  TYR A OH  1 
ATOM   314  N N   . ASP A 1 51  ? 156.634 111.481 167.471 1.00 93.18  ? 51  ASP A N   1 
ATOM   315  C CA  . ASP A 1 51  ? 156.925 112.081 168.765 1.00 98.34  ? 51  ASP A CA  1 
ATOM   316  C C   . ASP A 1 51  ? 157.730 111.106 169.614 1.00 92.57  ? 51  ASP A C   1 
ATOM   317  O O   . ASP A 1 51  ? 157.331 109.951 169.794 1.00 90.50  ? 51  ASP A O   1 
ATOM   318  C CB  . ASP A 1 51  ? 155.626 112.456 169.480 1.00 99.81  ? 51  ASP A CB  1 
ATOM   319  C CG  . ASP A 1 51  ? 155.104 113.819 169.071 1.00 94.67  ? 51  ASP A CG  1 
ATOM   320  O OD1 . ASP A 1 51  ? 155.916 114.673 168.665 1.00 92.23  ? 51  ASP A OD1 1 
ATOM   321  O OD2 . ASP A 1 51  ? 153.879 114.041 169.159 1.00 95.83  ? 51  ASP A OD2 1 
ATOM   322  N N   . LEU A 1 52  ? 158.868 111.567 170.137 1.00 86.82  ? 52  LEU A N   1 
ATOM   323  C CA  . LEU A 1 52  ? 159.722 110.714 170.963 1.00 88.57  ? 52  LEU A CA  1 
ATOM   324  C C   . LEU A 1 52  ? 160.406 111.595 172.006 1.00 94.01  ? 52  LEU A C   1 
ATOM   325  O O   . LEU A 1 52  ? 161.467 112.166 171.736 1.00 96.92  ? 52  LEU A O   1 
ATOM   326  C CB  . LEU A 1 52  ? 160.738 109.967 170.109 1.00 86.89  ? 52  LEU A CB  1 
ATOM   327  C CG  . LEU A 1 52  ? 161.708 109.039 170.844 1.00 87.73  ? 52  LEU A CG  1 
ATOM   328  C CD1 . LEU A 1 52  ? 160.958 108.109 171.786 1.00 87.06  ? 52  LEU A CD1 1 
ATOM   329  C CD2 . LEU A 1 52  ? 162.546 108.245 169.853 1.00 88.21  ? 52  LEU A CD2 1 
ATOM   330  N N   . SER A 1 53  ? 159.760 111.738 173.174 1.00 96.66  ? 53  SER A N   1 
ATOM   331  C CA  . SER A 1 53  ? 160.294 112.551 174.299 1.00 87.31  ? 53  SER A CA  1 
ATOM   332  C C   . SER A 1 53  ? 160.730 113.940 173.809 1.00 82.21  ? 53  SER A C   1 
ATOM   333  O O   . SER A 1 53  ? 161.755 114.444 174.317 1.00 79.33  ? 53  SER A O   1 
ATOM   334  C CB  . SER A 1 53  ? 161.422 111.827 174.988 1.00 85.92  ? 53  SER A CB  1 
ATOM   335  O OG  . SER A 1 53  ? 161.041 110.499 175.317 1.00 86.60  ? 53  SER A OG  1 
ATOM   336  N N   . PHE A 1 54  ? 159.983 114.550 172.883 1.00 79.97  ? 54  PHE A N   1 
ATOM   337  C CA  . PHE A 1 54  ? 160.305 115.921 172.393 1.00 81.46  ? 54  PHE A CA  1 
ATOM   338  C C   . PHE A 1 54  ? 160.040 116.933 173.517 1.00 78.66  ? 54  PHE A C   1 
ATOM   339  O O   . PHE A 1 54  ? 160.847 117.871 173.671 1.00 73.21  ? 54  PHE A O   1 
ATOM   340  C CB  . PHE A 1 54  ? 159.566 116.267 171.094 1.00 81.01  ? 54  PHE A CB  1 
ATOM   341  C CG  . PHE A 1 54  ? 158.044 116.286 171.135 1.00 77.09  ? 54  PHE A CG  1 
ATOM   342  C CD1 . PHE A 1 54  ? 157.327 115.362 171.887 1.00 70.94  ? 54  PHE A CD1 1 
ATOM   343  C CD2 . PHE A 1 54  ? 157.332 117.241 170.419 1.00 77.79  ? 54  PHE A CD2 1 
ATOM   344  C CE1 . PHE A 1 54  ? 155.943 115.393 171.919 1.00 68.91  ? 54  PHE A CE1 1 
ATOM   345  C CE2 . PHE A 1 54  ? 155.948 117.267 170.453 1.00 74.83  ? 54  PHE A CE2 1 
ATOM   346  C CZ  . PHE A 1 54  ? 155.258 116.347 171.204 1.00 71.54  ? 54  PHE A CZ  1 
ATOM   347  N N   . LEU A 1 55  ? 158.938 116.764 174.260 1.00 79.91  ? 55  LEU A N   1 
ATOM   348  C CA  . LEU A 1 55  ? 158.606 117.679 175.389 1.00 61.58  ? 55  LEU A CA  1 
ATOM   349  C C   . LEU A 1 55  ? 158.098 116.859 176.587 1.00 48.98  ? 55  LEU A C   1 
ATOM   350  O O   . LEU A 1 55  ? 156.895 116.573 176.642 1.00 46.08  ? 55  LEU A O   1 
ATOM   351  C CB  . LEU A 1 55  ? 157.621 118.773 174.972 1.00 57.36  ? 55  LEU A CB  1 
ATOM   352  C CG  . LEU A 1 55  ? 156.646 118.439 173.840 1.00 47.82  ? 55  LEU A CG  1 
ATOM   353  C CD1 . LEU A 1 55  ? 155.431 117.705 174.368 1.00 46.22  ? 55  LEU A CD1 1 
ATOM   354  C CD2 . LEU A 1 55  ? 156.230 119.706 173.114 1.00 45.54  ? 55  LEU A CD2 1 
ATOM   355  N N   . LYS A 1 56  ? 158.989 116.504 177.509 1.00 42.77  ? 56  LYS A N   1 
ATOM   356  C CA  . LYS A 1 56  ? 158.637 115.699 178.710 1.00 46.52  ? 56  LYS A CA  1 
ATOM   357  C C   . LYS A 1 56  ? 159.074 116.423 179.992 1.00 45.99  ? 56  LYS A C   1 
ATOM   358  O O   . LYS A 1 56  ? 158.498 116.105 181.056 1.00 45.38  ? 56  LYS A O   1 
ATOM   359  C CB  . LYS A 1 56  ? 159.330 114.338 178.578 1.00 54.45  ? 56  LYS A CB  1 
ATOM   360  C CG  . LYS A 1 56  ? 159.291 113.411 179.790 1.00 50.42  ? 56  LYS A CG  1 
ATOM   361  C CD  . LYS A 1 56  ? 157.917 112.816 180.062 1.00 49.39  ? 56  LYS A CD  1 
ATOM   362  C CE  . LYS A 1 56  ? 157.831 112.017 181.315 1.00 54.08  ? 56  LYS A CE  1 
ATOM   363  N NZ  . LYS A 1 56  ? 156.766 111.019 181.197 1.00 54.76  ? 56  LYS A NZ  1 
ATOM   364  N N   . THR A 1 57  ? 160.008 117.377 179.911 1.00 44.78  ? 57  THR A N   1 
ATOM   365  C CA  . THR A 1 57  ? 160.577 118.073 181.091 1.00 39.52  ? 57  THR A CA  1 
ATOM   366  C C   . THR A 1 57  ? 159.746 119.277 181.478 1.00 35.37  ? 57  THR A C   1 
ATOM   367  O O   . THR A 1 57  ? 160.059 119.878 182.526 1.00 40.75  ? 57  THR A O   1 
ATOM   368  C CB  . THR A 1 57  ? 162.010 118.481 180.760 1.00 49.15  ? 57  THR A CB  1 
ATOM   369  O OG1 . THR A 1 57  ? 161.954 119.110 179.483 1.00 52.02  ? 57  THR A OG1 1 
ATOM   370  C CG2 . THR A 1 57  ? 162.947 117.289 180.693 1.00 48.84  ? 57  THR A CG2 1 
ATOM   371  N N   . ILE A 1 58  ? 158.728 119.632 180.689 1.00 36.78  ? 58  ILE A N   1 
ATOM   372  C CA  . ILE A 1 58  ? 157.916 120.857 180.960 1.00 24.74  ? 58  ILE A CA  1 
ATOM   373  C C   . ILE A 1 58  ? 157.222 120.675 182.317 1.00 21.96  ? 58  ILE A C   1 
ATOM   374  O O   . ILE A 1 58  ? 156.583 119.618 182.497 1.00 24.23  ? 58  ILE A O   1 
ATOM   375  C CB  . ILE A 1 58  ? 156.902 121.153 179.837 1.00 17.28  ? 58  ILE A CB  1 
ATOM   376  C CG1 . ILE A 1 58  ? 157.531 121.080 178.445 1.00 33.69  ? 58  ILE A CG1 1 
ATOM   377  C CG2 . ILE A 1 58  ? 156.233 122.508 180.071 1.00 17.42  ? 58  ILE A CG2 1 
ATOM   378  C CD1 . ILE A 1 58  ? 156.536 121.246 177.312 1.00 33.81  ? 58  ILE A CD1 1 
ATOM   379  N N   . GLN A 1 59  ? 157.359 121.640 183.233 1.00 20.55  ? 59  GLN A N   1 
ATOM   380  C CA  . GLN A 1 59  ? 156.717 121.614 184.537 1.00 20.28  ? 59  GLN A CA  1 
ATOM   381  C C   . GLN A 1 59  ? 155.826 122.819 184.799 1.00 14.82  ? 59  GLN A C   1 
ATOM   382  O O   . GLN A 1 59  ? 155.183 122.870 185.853 1.00 16.19  ? 59  GLN A O   1 
ATOM   383  C CB  . GLN A 1 59  ? 157.736 121.535 185.685 1.00 22.25  ? 59  GLN A CB  1 
ATOM   384  C CG  . GLN A 1 59  ? 158.476 120.213 185.775 1.00 26.90  ? 59  GLN A CG  1 
ATOM   385  C CD  . GLN A 1 59  ? 159.527 120.210 186.865 1.00 34.60  ? 59  GLN A CD  1 
ATOM   386  O OE1 . GLN A 1 59  ? 159.254 120.577 188.008 1.00 42.03  ? 59  GLN A OE1 1 
ATOM   387  N NE2 . GLN A 1 59  ? 160.738 119.792 186.516 1.00 38.52  ? 59  GLN A NE2 1 
ATOM   388  N N   . GLU A 1 60  ? 155.761 123.781 183.881 1.00 15.99  ? 60  GLU A N   1 
ATOM   389  C CA  . GLU A 1 60  ? 155.006 125.004 184.120 1.00 17.05  ? 60  GLU A CA  1 
ATOM   390  C C   . GLU A 1 60  ? 154.757 125.708 182.796 1.00 20.20  ? 60  GLU A C   1 
ATOM   391  O O   . GLU A 1 60  ? 155.695 125.925 182.025 1.00 26.07  ? 60  GLU A O   1 
ATOM   392  C CB  . GLU A 1 60  ? 155.763 125.928 185.079 1.00 24.92  ? 60  GLU A CB  1 
ATOM   393  C CG  . GLU A 1 60  ? 155.109 127.276 185.293 1.00 32.07  ? 60  GLU A CG  1 
ATOM   394  C CD  . GLU A 1 60  ? 154.401 127.364 186.625 1.00 35.32  ? 60  GLU A CD  1 
ATOM   395  O OE1 . GLU A 1 60  ? 154.996 126.957 187.645 1.00 40.60  ? 60  GLU A OE1 1 
ATOM   396  O OE2 . GLU A 1 60  ? 153.246 127.833 186.653 1.00 26.97  ? 60  GLU A OE2 1 
ATOM   397  N N   . VAL A 1 61  ? 153.485 126.032 182.544 1.00 19.55  ? 61  VAL A N   1 
ATOM   398  C CA  . VAL A 1 61  ? 153.116 126.773 181.303 1.00 20.54  ? 61  VAL A CA  1 
ATOM   399  C C   . VAL A 1 61  ? 152.395 128.058 181.736 1.00 22.18  ? 61  VAL A C   1 
ATOM   400  O O   . VAL A 1 61  ? 151.289 127.948 182.304 1.00 23.21  ? 61  VAL A O   1 
ATOM   401  C CB  . VAL A 1 61  ? 152.241 125.940 180.345 1.00 17.39  ? 61  VAL A CB  1 
ATOM   402  C CG1 . VAL A 1 61  ? 151.872 126.725 179.093 1.00 19.76  ? 61  VAL A CG1 1 
ATOM   403  C CG2 . VAL A 1 61  ? 152.908 124.623 179.970 1.00 14.62  ? 61  VAL A CG2 1 
ATOM   404  N N   . ALA A 1 62  ? 153.010 129.218 181.496 1.00 25.22  ? 62  ALA A N   1 
ATOM   405  C CA  . ALA A 1 62  ? 152.366 130.510 181.828 1.00 22.91  ? 62  ALA A CA  1 
ATOM   406  C C   . ALA A 1 62  ? 151.417 130.888 180.695 1.00 32.35  ? 62  ALA A C   1 
ATOM   407  O O   . ALA A 1 62  ? 151.688 131.876 179.981 1.00 37.98  ? 62  ALA A O   1 
ATOM   408  C CB  . ALA A 1 62  ? 153.418 131.570 182.042 1.00 26.98  ? 62  ALA A CB  1 
ATOM   409  N N   . GLY A 1 63  ? 150.342 130.116 180.528 1.00 26.06  ? 63  GLY A N   1 
ATOM   410  C CA  . GLY A 1 63  ? 149.387 130.370 179.438 1.00 21.26  ? 63  GLY A CA  1 
ATOM   411  C C   . GLY A 1 63  ? 148.405 129.227 179.331 1.00 22.72  ? 63  GLY A C   1 
ATOM   412  O O   . GLY A 1 63  ? 147.855 128.824 180.373 1.00 17.77  ? 63  GLY A O   1 
ATOM   413  N N   . TYR A 1 64  ? 148.195 128.717 178.118 1.00 24.89  ? 64  TYR A N   1 
ATOM   414  C CA  . TYR A 1 64  ? 147.281 127.604 177.924 1.00 20.98  ? 64  TYR A CA  1 
ATOM   415  C C   . TYR A 1 64  ? 147.996 126.455 177.227 1.00 19.80  ? 64  TYR A C   1 
ATOM   416  O O   . TYR A 1 64  ? 148.948 126.661 176.469 1.00 23.87  ? 64  TYR A O   1 
ATOM   417  C CB  . TYR A 1 64  ? 146.043 128.024 177.114 1.00 25.38  ? 64  TYR A CB  1 
ATOM   418  C CG  . TYR A 1 64  ? 146.329 128.527 175.716 1.00 31.99  ? 64  TYR A CG  1 
ATOM   419  C CD1 . TYR A 1 64  ? 146.435 127.647 174.645 1.00 35.37  ? 64  TYR A CD1 1 
ATOM   420  C CD2 . TYR A 1 64  ? 146.475 129.883 175.463 1.00 37.29  ? 64  TYR A CD2 1 
ATOM   421  C CE1 . TYR A 1 64  ? 146.691 128.104 173.367 1.00 39.83  ? 64  TYR A CE1 1 
ATOM   422  C CE2 . TYR A 1 64  ? 146.725 130.350 174.188 1.00 43.02  ? 64  TYR A CE2 1 
ATOM   423  C CZ  . TYR A 1 64  ? 146.836 129.457 173.145 1.00 48.05  ? 64  TYR A CZ  1 
ATOM   424  O OH  . TYR A 1 64  ? 147.090 129.920 171.875 1.00 62.22  ? 64  TYR A OH  1 
ATOM   425  N N   . VAL A 1 65  ? 147.619 125.209 177.542 1.00 15.24  ? 65  VAL A N   1 
ATOM   426  C CA  . VAL A 1 65  ? 148.197 123.985 176.909 1.00 15.56  ? 65  VAL A CA  1 
ATOM   427  C C   . VAL A 1 65  ? 147.221 123.485 175.833 1.00 24.85  ? 65  VAL A C   1 
ATOM   428  O O   . VAL A 1 65  ? 146.234 122.832 176.218 1.00 28.26  ? 65  VAL A O   1 
ATOM   429  C CB  . VAL A 1 65  ? 148.472 122.892 177.958 1.00 12.01  ? 65  VAL A CB  1 
ATOM   430  C CG1 . VAL A 1 65  ? 148.918 121.582 177.321 1.00 13.63  ? 65  VAL A CG1 1 
ATOM   431  C CG2 . VAL A 1 65  ? 149.494 123.356 178.987 1.00 19.53  ? 65  VAL A CG2 1 
ATOM   432  N N   . LEU A 1 66  ? 147.474 123.774 174.553 1.00 29.51  ? 66  LEU A N   1 
ATOM   433  C CA  . LEU A 1 66  ? 146.601 123.356 173.423 1.00 26.81  ? 66  LEU A CA  1 
ATOM   434  C C   . LEU A 1 66  ? 147.164 122.104 172.735 1.00 28.52  ? 66  LEU A C   1 
ATOM   435  O O   . LEU A 1 66  ? 148.065 122.260 171.891 1.00 32.82  ? 66  LEU A O   1 
ATOM   436  C CB  . LEU A 1 66  ? 146.517 124.537 172.459 1.00 30.68  ? 66  LEU A CB  1 
ATOM   437  C CG  . LEU A 1 66  ? 145.798 124.297 171.128 1.00 38.72  ? 66  LEU A CG  1 
ATOM   438  C CD1 . LEU A 1 66  ? 144.317 124.032 171.321 1.00 43.31  ? 66  LEU A CD1 1 
ATOM   439  C CD2 . LEU A 1 66  ? 146.017 125.492 170.225 1.00 46.67  ? 66  LEU A CD2 1 
ATOM   440  N N   . ILE A 1 67  ? 146.632 120.926 173.062 1.00 24.25  ? 67  ILE A N   1 
ATOM   441  C CA  . ILE A 1 67  ? 147.056 119.676 172.365 1.00 31.64  ? 67  ILE A CA  1 
ATOM   442  C C   . ILE A 1 67  ? 145.935 119.323 171.378 1.00 44.15  ? 67  ILE A C   1 
ATOM   443  O O   . ILE A 1 67  ? 144.960 118.675 171.811 1.00 46.19  ? 67  ILE A O   1 
ATOM   444  C CB  . ILE A 1 67  ? 147.312 118.550 173.380 1.00 33.11  ? 67  ILE A CB  1 
ATOM   445  C CG1 . ILE A 1 67  ? 148.192 119.032 174.530 1.00 29.88  ? 67  ILE A CG1 1 
ATOM   446  C CG2 . ILE A 1 67  ? 147.898 117.316 172.694 1.00 39.97  ? 67  ILE A CG2 1 
ATOM   447  C CD1 . ILE A 1 67  ? 148.378 118.013 175.637 1.00 22.74  ? 67  ILE A CD1 1 
ATOM   448  N N   . ALA A 1 68  ? 146.058 119.741 170.114 1.00 46.39  ? 68  ALA A N   1 
ATOM   449  C CA  . ALA A 1 68  ? 144.948 119.536 169.151 1.00 39.97  ? 68  ALA A CA  1 
ATOM   450  C C   . ALA A 1 68  ? 145.413 118.749 167.926 1.00 61.20  ? 68  ALA A C   1 
ATOM   451  O O   . ALA A 1 68  ? 146.574 118.933 167.508 1.00 69.19  ? 68  ALA A O   1 
ATOM   452  C CB  . ALA A 1 68  ? 144.390 120.880 168.748 1.00 33.22  ? 68  ALA A CB  1 
ATOM   453  N N   . LEU A 1 69  ? 144.541 117.897 167.375 1.00 63.29  ? 69  LEU A N   1 
ATOM   454  C CA  . LEU A 1 69  ? 144.866 117.142 166.134 1.00 54.09  ? 69  LEU A CA  1 
ATOM   455  C C   . LEU A 1 69  ? 146.237 116.458 166.263 1.00 55.00  ? 69  LEU A C   1 
ATOM   456  O O   . LEU A 1 69  ? 147.078 116.645 165.357 1.00 53.11  ? 69  LEU A O   1 
ATOM   457  C CB  . LEU A 1 69  ? 144.809 118.080 164.929 1.00 52.66  ? 69  LEU A CB  1 
ATOM   458  C CG  . LEU A 1 69  ? 143.427 118.643 164.584 1.00 55.82  ? 69  LEU A CG  1 
ATOM   459  C CD1 . LEU A 1 69  ? 143.180 120.000 165.219 1.00 47.81  ? 69  LEU A CD1 1 
ATOM   460  C CD2 . LEU A 1 69  ? 143.210 118.701 163.082 1.00 62.48  ? 69  LEU A CD2 1 
ATOM   461  N N   . ASN A 1 70  ? 146.447 115.698 167.340 1.00 60.55  ? 70  ASN A N   1 
ATOM   462  C CA  . ASN A 1 70  ? 147.721 114.948 167.519 1.00 67.42  ? 70  ASN A CA  1 
ATOM   463  C C   . ASN A 1 70  ? 147.470 113.475 167.189 1.00 72.26  ? 70  ASN A C   1 
ATOM   464  O O   . ASN A 1 70  ? 146.711 112.821 167.936 1.00 69.80  ? 70  ASN A O   1 
ATOM   465  C CB  . ASN A 1 70  ? 148.292 115.111 168.923 1.00 63.79  ? 70  ASN A CB  1 
ATOM   466  C CG  . ASN A 1 70  ? 148.864 116.488 169.155 1.00 63.85  ? 70  ASN A CG  1 
ATOM   467  O OD1 . ASN A 1 70  ? 150.064 116.626 169.417 1.00 68.95  ? 70  ASN A OD1 1 
ATOM   468  N ND2 . ASN A 1 70  ? 148.033 117.514 169.066 1.00 54.48  ? 70  ASN A ND2 1 
ATOM   469  N N   . THR A 1 71  ? 148.086 112.972 166.118 1.00 79.77  ? 71  THR A N   1 
ATOM   470  C CA  . THR A 1 71  ? 147.840 111.578 165.692 1.00 79.31  ? 71  THR A CA  1 
ATOM   471  C C   . THR A 1 71  ? 148.685 110.636 166.523 1.00 80.62  ? 71  THR A C   1 
ATOM   472  O O   . THR A 1 71  ? 148.349 109.432 166.569 1.00 78.05  ? 71  THR A O   1 
ATOM   473  C CB  . THR A 1 71  ? 148.148 111.457 164.201 1.00 83.85  ? 71  THR A CB  1 
ATOM   474  O OG1 . THR A 1 71  ? 149.550 111.687 164.111 1.00 86.94  ? 71  THR A OG1 1 
ATOM   475  C CG2 . THR A 1 71  ? 147.394 112.474 163.365 1.00 77.91  ? 71  THR A CG2 1 
ATOM   476  N N   . VAL A 1 72  ? 149.736 111.151 167.168 1.00 80.02  ? 72  VAL A N   1 
ATOM   477  C CA  . VAL A 1 72  ? 150.665 110.286 167.958 1.00 79.13  ? 72  VAL A CA  1 
ATOM   478  C C   . VAL A 1 72  ? 149.883 109.556 169.058 1.00 72.01  ? 72  VAL A C   1 
ATOM   479  O O   . VAL A 1 72  ? 148.887 110.123 169.556 1.00 70.81  ? 72  VAL A O   1 
ATOM   480  C CB  . VAL A 1 72  ? 151.814 111.112 168.559 1.00 71.24  ? 72  VAL A CB  1 
ATOM   481  C CG1 . VAL A 1 72  ? 152.796 111.561 167.486 1.00 81.00  ? 72  VAL A CG1 1 
ATOM   482  C CG2 . VAL A 1 72  ? 151.286 112.300 169.353 1.00 68.87  ? 72  VAL A CG2 1 
ATOM   483  N N   . GLU A 1 73  ? 150.331 108.354 169.428 1.00 73.08  ? 73  GLU A N   1 
ATOM   484  C CA  . GLU A 1 73  ? 149.636 107.589 170.456 1.00 74.97  ? 73  GLU A CA  1 
ATOM   485  C C   . GLU A 1 73  ? 149.808 108.204 171.839 1.00 69.61  ? 73  GLU A C   1 
ATOM   486  O O   . GLU A 1 73  ? 148.918 108.070 172.687 1.00 69.50  ? 73  GLU A O   1 
ATOM   487  C CB  . GLU A 1 73  ? 150.131 106.143 170.459 1.00 78.63  ? 73  GLU A CB  1 
ATOM   488  C CG  . GLU A 1 73  ? 149.142 105.152 171.048 1.00 76.16  ? 73  GLU A CG  1 
ATOM   489  C CD  . GLU A 1 73  ? 149.821 104.054 171.841 1.00 79.89  ? 73  GLU A CD  1 
ATOM   490  O OE1 . GLU A 1 73  ? 150.557 104.377 172.798 1.00 74.29  ? 73  GLU A OE1 1 
ATOM   491  O OE2 . GLU A 1 73  ? 149.620 102.867 171.509 1.00 74.32  ? 73  GLU A OE2 1 
ATOM   492  N N   . ARG A 1 74  ? 150.948 108.850 172.092 1.00 65.88  ? 74  ARG A N   1 
ATOM   493  C CA  . ARG A 1 74  ? 151.180 109.347 173.475 1.00 58.27  ? 74  ARG A CA  1 
ATOM   494  C C   . ARG A 1 74  ? 151.902 110.700 173.475 1.00 54.90  ? 74  ARG A C   1 
ATOM   495  O O   . ARG A 1 74  ? 153.044 110.761 172.971 1.00 57.29  ? 74  ARG A O   1 
ATOM   496  C CB  . ARG A 1 74  ? 151.992 108.328 174.282 1.00 51.96  ? 74  ARG A CB  1 
ATOM   497  C CG  . ARG A 1 74  ? 152.368 108.796 175.680 1.00 41.58  ? 74  ARG A CG  1 
ATOM   498  C CD  . ARG A 1 74  ? 153.069 107.699 176.464 1.00 40.42  ? 74  ARG A CD  1 
ATOM   499  N NE  . ARG A 1 74  ? 153.668 108.192 177.709 1.00 49.14  ? 74  ARG A NE  1 
ATOM   500  C CZ  . ARG A 1 74  ? 153.345 107.764 178.921 1.00 54.07  ? 74  ARG A CZ  1 
ATOM   501  N NH1 . ARG A 1 74  ? 152.245 107.056 179.099 1.00 54.21  ? 74  ARG A NH1 1 
ATOM   502  N NH2 . ARG A 1 74  ? 154.116 108.054 179.954 1.00 57.42  ? 74  ARG A NH2 1 
ATOM   503  N N   . ILE A 1 75  ? 151.258 111.736 174.019 1.00 52.01  ? 75  ILE A N   1 
ATOM   504  C CA  . ILE A 1 75  ? 151.945 113.053 174.173 1.00 49.11  ? 75  ILE A CA  1 
ATOM   505  C C   . ILE A 1 75  ? 152.476 113.104 175.613 1.00 46.93  ? 75  ILE A C   1 
ATOM   506  O O   . ILE A 1 75  ? 151.651 113.145 176.553 1.00 41.02  ? 75  ILE A O   1 
ATOM   507  C CB  . ILE A 1 75  ? 151.002 114.228 173.864 1.00 51.77  ? 75  ILE A CB  1 
ATOM   508  C CG1 . ILE A 1 75  ? 150.863 114.446 172.363 1.00 54.01  ? 75  ILE A CG1 1 
ATOM   509  C CG2 . ILE A 1 75  ? 151.471 115.502 174.566 1.00 42.11  ? 75  ILE A CG2 1 
ATOM   510  C CD1 . ILE A 1 75  ? 152.159 114.837 171.681 1.00 58.00  ? 75  ILE A CD1 1 
ATOM   511  N N   . PRO A 1 76  ? 153.807 113.051 175.829 1.00 47.23  ? 76  PRO A N   1 
ATOM   512  C CA  . PRO A 1 76  ? 154.340 113.027 177.180 1.00 40.20  ? 76  PRO A CA  1 
ATOM   513  C C   . PRO A 1 76  ? 154.226 114.409 177.794 1.00 44.46  ? 76  PRO A C   1 
ATOM   514  O O   . PRO A 1 76  ? 154.636 115.382 177.141 1.00 45.47  ? 76  PRO A O   1 
ATOM   515  C CB  . PRO A 1 76  ? 155.791 112.586 176.961 1.00 44.45  ? 76  PRO A CB  1 
ATOM   516  C CG  . PRO A 1 76  ? 156.125 113.084 175.572 1.00 49.84  ? 76  PRO A CG  1 
ATOM   517  C CD  . PRO A 1 76  ? 154.823 113.015 174.791 1.00 52.72  ? 76  PRO A CD  1 
ATOM   518  N N   . LEU A 1 77  ? 153.645 114.506 178.990 1.00 49.71  ? 77  LEU A N   1 
ATOM   519  C CA  . LEU A 1 77  ? 153.536 115.800 179.716 1.00 38.85  ? 77  LEU A CA  1 
ATOM   520  C C   . LEU A 1 77  ? 153.340 115.437 181.191 1.00 35.42  ? 77  LEU A C   1 
ATOM   521  O O   . LEU A 1 77  ? 152.580 116.140 181.888 1.00 27.12  ? 77  LEU A O   1 
ATOM   522  C CB  . LEU A 1 77  ? 152.397 116.677 179.197 1.00 32.37  ? 77  LEU A CB  1 
ATOM   523  C CG  . LEU A 1 77  ? 152.747 117.627 178.048 1.00 34.01  ? 77  LEU A CG  1 
ATOM   524  C CD1 . LEU A 1 77  ? 151.534 118.432 177.628 1.00 37.12  ? 77  LEU A CD1 1 
ATOM   525  C CD2 . LEU A 1 77  ? 153.893 118.541 178.439 1.00 23.85  ? 77  LEU A CD2 1 
ATOM   526  N N   . GLU A 1 78  ? 153.998 114.363 181.629 1.00 42.74  ? 78  GLU A N   1 
ATOM   527  C CA  . GLU A 1 78  ? 153.826 113.880 183.021 1.00 40.41  ? 78  GLU A CA  1 
ATOM   528  C C   . GLU A 1 78  ? 154.334 114.932 184.010 1.00 37.76  ? 78  GLU A C   1 
ATOM   529  O O   . GLU A 1 78  ? 153.596 115.218 184.963 1.00 36.13  ? 78  GLU A O   1 
ATOM   530  C CB  . GLU A 1 78  ? 154.594 112.568 183.159 1.00 46.41  ? 78  GLU A CB  1 
ATOM   531  C CG  . GLU A 1 78  ? 153.958 111.585 184.136 1.00 49.36  ? 78  GLU A CG  1 
ATOM   532  C CD  . GLU A 1 78  ? 154.458 110.170 183.914 1.00 52.47  ? 78  GLU A CD  1 
ATOM   533  O OE1 . GLU A 1 78  ? 154.234 109.638 182.806 1.00 52.16  ? 78  GLU A OE1 1 
ATOM   534  O OE2 . GLU A 1 78  ? 155.078 109.605 184.837 1.00 56.41  ? 78  GLU A OE2 1 
ATOM   535  N N   . ASN A 1 79  ? 155.520 115.498 183.772 1.00 39.43  ? 79  ASN A N   1 
ATOM   536  C CA  . ASN A 1 79  ? 156.133 116.453 184.742 1.00 34.53  ? 79  ASN A CA  1 
ATOM   537  C C   . ASN A 1 79  ? 155.286 117.721 184.891 1.00 27.15  ? 79  ASN A C   1 
ATOM   538  O O   . ASN A 1 79  ? 155.393 118.362 185.956 1.00 31.92  ? 79  ASN A O   1 
ATOM   539  C CB  . ASN A 1 79  ? 157.565 116.793 184.345 1.00 34.63  ? 79  ASN A CB  1 
ATOM   540  C CG  . ASN A 1 79  ? 158.452 115.572 184.329 1.00 41.21  ? 79  ASN A CG  1 
ATOM   541  O OD1 . ASN A 1 79  ? 158.183 114.616 183.593 1.00 50.56  ? 79  ASN A OD1 1 
ATOM   542  N ND2 . ASN A 1 79  ? 159.506 115.581 185.131 1.00 38.42  ? 79  ASN A ND2 1 
ATOM   543  N N   . LEU A 1 80  ? 154.478 118.072 183.888 1.00 23.72  ? 80  LEU A N   1 
ATOM   544  C CA  . LEU A 1 80  ? 153.725 119.321 183.937 1.00 19.26  ? 80  LEU A CA  1 
ATOM   545  C C   . LEU A 1 80  ? 152.993 119.465 185.263 1.00 17.53  ? 80  LEU A C   1 
ATOM   546  O O   . LEU A 1 80  ? 152.075 118.695 185.557 1.00 17.65  ? 80  LEU A O   1 
ATOM   547  C CB  . LEU A 1 80  ? 152.731 119.403 182.778 1.00 14.66  ? 80  LEU A CB  1 
ATOM   548  C CG  . LEU A 1 80  ? 152.348 120.831 182.395 1.00 7.41   ? 80  LEU A CG  1 
ATOM   549  C CD1 . LEU A 1 80  ? 153.521 121.513 181.727 1.00 12.03  ? 80  LEU A CD1 1 
ATOM   550  C CD2 . LEU A 1 80  ? 151.131 120.855 181.493 1.00 9.80   ? 80  LEU A CD2 1 
ATOM   551  N N   . GLN A 1 81  ? 153.388 120.454 186.062 1.00 16.74  ? 81  GLN A N   1 
ATOM   552  C CA  . GLN A 1 81  ? 152.839 120.626 187.400 1.00 19.15  ? 81  GLN A CA  1 
ATOM   553  C C   . GLN A 1 81  ? 151.632 121.555 187.427 1.00 15.10  ? 81  GLN A C   1 
ATOM   554  O O   . GLN A 1 81  ? 150.687 121.313 188.186 1.00 17.05  ? 81  GLN A O   1 
ATOM   555  C CB  . GLN A 1 81  ? 153.921 121.160 188.343 1.00 20.64  ? 81  GLN A CB  1 
ATOM   556  C CG  . GLN A 1 81  ? 153.624 120.952 189.817 1.00 20.47  ? 81  GLN A CG  1 
ATOM   557  C CD  . GLN A 1 81  ? 154.026 119.577 190.301 1.00 25.59  ? 81  GLN A CD  1 
ATOM   558  O OE1 . GLN A 1 81  ? 153.178 118.751 190.638 1.00 33.76  ? 81  GLN A OE1 1 
ATOM   559  N NE2 . GLN A 1 81  ? 155.328 119.321 190.337 1.00 28.83  ? 81  GLN A NE2 1 
ATOM   560  N N   . ILE A 1 82  ? 151.637 122.610 186.617 1.00 8.97   ? 82  ILE A N   1 
ATOM   561  C CA  . ILE A 1 82  ? 150.583 123.616 186.676 1.00 11.20  ? 82  ILE A CA  1 
ATOM   562  C C   . ILE A 1 82  ? 150.592 124.407 185.376 1.00 14.34  ? 82  ILE A C   1 
ATOM   563  O O   . ILE A 1 82  ? 151.652 124.692 184.812 1.00 13.47  ? 82  ILE A O   1 
ATOM   564  C CB  . ILE A 1 82  ? 150.764 124.536 187.907 1.00 16.46  ? 82  ILE A CB  1 
ATOM   565  C CG1 . ILE A 1 82  ? 149.737 125.670 187.904 1.00 15.10  ? 82  ILE A CG1 1 
ATOM   566  C CG2 . ILE A 1 82  ? 152.171 125.095 187.948 1.00 18.45  ? 82  ILE A CG2 1 
ATOM   567  C CD1 . ILE A 1 82  ? 149.899 126.635 189.047 1.00 13.66  ? 82  ILE A CD1 1 
ATOM   568  N N   . ILE A 1 83  ? 149.398 124.753 184.903 1.00 18.14  ? 83  ILE A N   1 
ATOM   569  C CA  . ILE A 1 83  ? 149.212 125.697 183.807 1.00 14.63  ? 83  ILE A CA  1 
ATOM   570  C C   . ILE A 1 83  ? 148.695 126.994 184.414 1.00 16.15  ? 83  ILE A C   1 
ATOM   571  O O   . ILE A 1 83  ? 147.659 127.000 185.091 1.00 14.63  ? 83  ILE A O   1 
ATOM   572  C CB  . ILE A 1 83  ? 148.245 125.156 182.743 1.00 9.94   ? 83  ILE A CB  1 
ATOM   573  C CG1 . ILE A 1 83  ? 148.385 123.639 182.619 1.00 7.88   ? 83  ILE A CG1 1 
ATOM   574  C CG2 . ILE A 1 83  ? 148.506 125.815 181.402 1.00 9.89   ? 83  ILE A CG2 1 
ATOM   575  C CD1 . ILE A 1 83  ? 147.329 122.998 181.756 1.00 5.63   ? 83  ILE A CD1 1 
ATOM   576  N N   . ARG A 1 84  ? 149.421 128.090 184.182 1.00 19.45  ? 84  ARG A N   1 
ATOM   577  C CA  . ARG A 1 84  ? 149.089 129.351 184.837 1.00 16.28  ? 84  ARG A CA  1 
ATOM   578  C C   . ARG A 1 84  ? 147.744 129.888 184.365 1.00 25.67  ? 84  ARG A C   1 
ATOM   579  O O   . ARG A 1 84  ? 146.890 130.256 185.180 1.00 38.08  ? 84  ARG A O   1 
ATOM   580  C CB  . ARG A 1 84  ? 150.192 130.380 184.586 1.00 18.70  ? 84  ARG A CB  1 
ATOM   581  C CG  . ARG A 1 84  ? 151.499 130.083 185.297 1.00 22.78  ? 84  ARG A CG  1 
ATOM   582  C CD  . ARG A 1 84  ? 151.472 130.561 186.738 1.00 19.35  ? 84  ARG A CD  1 
ATOM   583  N NE  . ARG A 1 84  ? 152.638 130.101 187.484 1.00 16.12  ? 84  ARG A NE  1 
ATOM   584  C CZ  . ARG A 1 84  ? 152.652 129.881 188.791 1.00 20.88  ? 84  ARG A CZ  1 
ATOM   585  N NH1 . ARG A 1 84  ? 151.576 130.071 189.536 1.00 30.63  ? 84  ARG A NH1 1 
ATOM   586  N NH2 . ARG A 1 84  ? 153.775 129.459 189.366 1.00 20.58  ? 84  ARG A NH2 1 
ATOM   587  N N   . GLY A 1 85  ? 147.534 129.938 183.054 1.00 23.12  ? 85  GLY A N   1 
ATOM   588  C CA  . GLY A 1 85  ? 146.322 130.515 182.513 1.00 22.72  ? 85  GLY A CA  1 
ATOM   589  C C   . GLY A 1 85  ? 146.405 131.984 182.174 1.00 26.92  ? 85  GLY A C   1 
ATOM   590  O O   . GLY A 1 85  ? 145.366 132.653 182.136 1.00 30.94  ? 85  GLY A O   1 
ATOM   591  N N   . ASN A 1 86  ? 147.608 132.512 181.933 1.00 25.06  ? 86  ASN A N   1 
ATOM   592  C CA  . ASN A 1 86  ? 147.747 133.915 181.560 1.00 21.12  ? 86  ASN A CA  1 
ATOM   593  C C   . ASN A 1 86  ? 147.057 134.228 180.240 1.00 26.76  ? 86  ASN A C   1 
ATOM   594  O O   . ASN A 1 86  ? 146.703 135.387 179.997 1.00 41.32  ? 86  ASN A O   1 
ATOM   595  C CB  . ASN A 1 86  ? 149.226 134.293 181.480 1.00 21.21  ? 86  ASN A CB  1 
ATOM   596  C CG  . ASN A 1 86  ? 149.904 134.279 182.834 1.00 31.09  ? 86  ASN A CG  1 
ATOM   597  O OD1 . ASN A 1 86  ? 149.284 133.961 183.849 1.00 26.28  ? 86  ASN A OD1 1 
ATOM   598  N ND2 . ASN A 1 86  ? 151.186 134.626 182.858 1.00 40.57  ? 86  ASN A ND2 1 
ATOM   599  N N   . MET A 1 87  ? 146.864 133.228 179.386 1.00 24.70  ? 87  MET A N   1 
ATOM   600  C CA  . MET A 1 87  ? 146.121 133.368 178.144 1.00 30.90  ? 87  MET A CA  1 
ATOM   601  C C   . MET A 1 87  ? 145.107 132.234 178.056 1.00 35.81  ? 87  MET A C   1 
ATOM   602  O O   . MET A 1 87  ? 145.031 131.371 178.935 1.00 38.06  ? 87  MET A O   1 
ATOM   603  C CB  . MET A 1 87  ? 147.059 133.368 176.930 1.00 39.05  ? 87  MET A CB  1 
ATOM   604  C CG  . MET A 1 87  ? 147.495 134.755 176.488 1.00 49.98  ? 87  MET A CG  1 
ATOM   605  S SD  . MET A 1 87  ? 148.190 134.770 174.824 1.00 69.07  ? 87  MET A SD  1 
ATOM   606  C CE  . MET A 1 87  ? 149.942 134.794 175.192 1.00 46.51  ? 87  MET A CE  1 
ATOM   607  N N   . TYR A 1 88  ? 144.315 132.239 176.987 1.00 40.84  ? 88  TYR A N   1 
ATOM   608  C CA  . TYR A 1 88  ? 143.309 131.211 176.776 1.00 41.27  ? 88  TYR A CA  1 
ATOM   609  C C   . TYR A 1 88  ? 143.264 130.842 175.301 1.00 46.56  ? 88  TYR A C   1 
ATOM   610  O O   . TYR A 1 88  ? 143.623 131.642 174.434 1.00 49.56  ? 88  TYR A O   1 
ATOM   611  C CB  . TYR A 1 88  ? 141.922 131.669 177.244 1.00 45.52  ? 88  TYR A CB  1 
ATOM   612  C CG  . TYR A 1 88  ? 141.887 132.164 178.672 1.00 41.87  ? 88  TYR A CG  1 
ATOM   613  C CD1 . TYR A 1 88  ? 141.896 131.274 179.737 1.00 36.13  ? 88  TYR A CD1 1 
ATOM   614  C CD2 . TYR A 1 88  ? 141.838 133.522 178.954 1.00 43.59  ? 88  TYR A CD2 1 
ATOM   615  C CE1 . TYR A 1 88  ? 141.859 131.722 181.042 1.00 35.53  ? 88  TYR A CE1 1 
ATOM   616  C CE2 . TYR A 1 88  ? 141.802 133.980 180.256 1.00 44.22  ? 88  TYR A CE2 1 
ATOM   617  C CZ  . TYR A 1 88  ? 141.813 133.076 181.296 1.00 42.15  ? 88  TYR A CZ  1 
ATOM   618  O OH  . TYR A 1 88  ? 141.777 133.529 182.594 1.00 41.71  ? 88  TYR A OH  1 
ATOM   619  N N   . TYR A 1 89  ? 142.819 129.614 175.028 1.00 50.11  ? 89  TYR A N   1 
ATOM   620  C CA  . TYR A 1 89  ? 142.709 129.153 173.648 1.00 56.65  ? 89  TYR A CA  1 
ATOM   621  C C   . TYR A 1 89  ? 141.624 129.926 172.905 1.00 63.60  ? 89  TYR A C   1 
ATOM   622  O O   . TYR A 1 89  ? 141.902 130.622 171.922 1.00 63.46  ? 89  TYR A O   1 
ATOM   623  C CB  . TYR A 1 89  ? 142.438 127.645 173.630 1.00 51.38  ? 89  TYR A CB  1 
ATOM   624  C CG  . TYR A 1 89  ? 141.768 127.121 172.380 1.00 60.55  ? 89  TYR A CG  1 
ATOM   625  C CD1 . TYR A 1 89  ? 142.352 127.282 171.130 1.00 60.92  ? 89  TYR A CD1 1 
ATOM   626  C CD2 . TYR A 1 89  ? 140.558 126.446 172.454 1.00 64.22  ? 89  TYR A CD2 1 
ATOM   627  C CE1 . TYR A 1 89  ? 141.740 126.799 169.990 1.00 66.60  ? 89  TYR A CE1 1 
ATOM   628  C CE2 . TYR A 1 89  ? 139.940 125.958 171.321 1.00 67.23  ? 89  TYR A CE2 1 
ATOM   629  C CZ  . TYR A 1 89  ? 140.534 126.137 170.092 1.00 70.30  ? 89  TYR A CZ  1 
ATOM   630  O OH  . TYR A 1 89  ? 139.917 125.650 168.964 1.00 71.15  ? 89  TYR A OH  1 
ATOM   631  N N   . GLU A 1 90  ? 140.379 129.825 173.367 1.00 67.05  ? 90  GLU A N   1 
ATOM   632  C CA  . GLU A 1 90  ? 139.301 130.667 172.859 1.00 61.48  ? 90  GLU A CA  1 
ATOM   633  C C   . GLU A 1 90  ? 138.751 131.581 173.944 1.00 60.18  ? 90  GLU A C   1 
ATOM   634  O O   . GLU A 1 90  ? 138.757 132.805 173.775 1.00 63.12  ? 90  GLU A O   1 
ATOM   635  C CB  . GLU A 1 90  ? 138.186 129.799 172.260 1.00 59.53  ? 90  GLU A CB  1 
ATOM   636  C CG  . GLU A 1 90  ? 138.461 129.335 170.838 1.00 63.80  ? 90  GLU A CG  1 
ATOM   637  C CD  . GLU A 1 90  ? 137.555 128.197 170.410 1.00 71.20  ? 90  GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 90  ? 136.840 127.647 171.273 1.00 75.21  ? 90  GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 90  ? 137.560 127.853 169.209 1.00 71.80  ? 90  GLU A OE2 1 
ATOM   640  N N   . ASN A 1 91  ? 138.286 131.023 175.060 1.00 60.20  ? 91  ASN A N   1 
ATOM   641  C CA  . ASN A 1 91  ? 137.837 131.815 176.203 1.00 60.72  ? 91  ASN A CA  1 
ATOM   642  C C   . ASN A 1 91  ? 137.752 130.887 177.402 1.00 58.57  ? 91  ASN A C   1 
ATOM   643  O O   . ASN A 1 91  ? 137.051 129.871 177.343 1.00 58.83  ? 91  ASN A O   1 
ATOM   644  C CB  . ASN A 1 91  ? 136.484 132.471 175.928 1.00 66.59  ? 91  ASN A CB  1 
ATOM   645  C CG  . ASN A 1 91  ? 136.001 133.316 177.091 1.00 71.78  ? 91  ASN A CG  1 
ATOM   646  O OD1 . ASN A 1 91  ? 136.798 133.935 177.796 1.00 68.53  ? 91  ASN A OD1 1 
ATOM   647  N ND2 . ASN A 1 91  ? 134.689 133.348 177.296 1.00 72.70  ? 91  ASN A ND2 1 
ATOM   648  N N   . SER A 1 92  ? 138.448 131.240 178.485 1.00 52.49  ? 92  SER A N   1 
ATOM   649  C CA  . SER A 1 92  ? 138.531 130.397 179.680 1.00 51.80  ? 92  SER A CA  1 
ATOM   650  C C   . SER A 1 92  ? 138.977 128.983 179.317 1.00 56.77  ? 92  SER A C   1 
ATOM   651  O O   . SER A 1 92  ? 138.441 127.989 179.812 1.00 57.56  ? 92  SER A O   1 
ATOM   652  C CB  . SER A 1 92  ? 137.204 130.378 180.442 1.00 57.48  ? 92  SER A CB  1 
ATOM   653  O OG  . SER A 1 92  ? 136.173 129.801 179.663 1.00 56.06  ? 92  SER A OG  1 
ATOM   654  N N   . TYR A 1 93  ? 139.972 128.895 178.438 1.00 55.99  ? 93  TYR A N   1 
ATOM   655  C CA  . TYR A 1 93  ? 140.470 127.628 177.909 1.00 43.27  ? 93  TYR A CA  1 
ATOM   656  C C   . TYR A 1 93  ? 141.960 127.532 178.219 1.00 40.24  ? 93  TYR A C   1 
ATOM   657  O O   . TYR A 1 93  ? 142.789 128.061 177.472 1.00 44.45  ? 93  TYR A O   1 
ATOM   658  C CB  . TYR A 1 93  ? 140.223 127.532 176.408 1.00 47.50  ? 93  TYR A CB  1 
ATOM   659  C CG  . TYR A 1 93  ? 138.858 127.018 176.019 1.00 55.66  ? 93  TYR A CG  1 
ATOM   660  C CD1 . TYR A 1 93  ? 138.126 126.201 176.869 1.00 50.00  ? 93  TYR A CD1 1 
ATOM   661  C CD2 . TYR A 1 93  ? 138.304 127.351 174.792 1.00 61.96  ? 93  TYR A CD2 1 
ATOM   662  C CE1 . TYR A 1 93  ? 136.877 125.733 176.504 1.00 56.90  ? 93  TYR A CE1 1 
ATOM   663  C CE2 . TYR A 1 93  ? 137.063 126.891 174.420 1.00 65.34  ? 93  TYR A CE2 1 
ATOM   664  C CZ  . TYR A 1 93  ? 136.352 126.084 175.276 1.00 66.40  ? 93  TYR A CZ  1 
ATOM   665  O OH  . TYR A 1 93  ? 135.112 125.631 174.892 1.00 63.02  ? 93  TYR A OH  1 
ATOM   666  N N   . ALA A 1 94  ? 142.303 126.857 179.314 1.00 32.68  ? 94  ALA A N   1 
ATOM   667  C CA  . ALA A 1 94  ? 143.704 126.631 179.645 1.00 20.49  ? 94  ALA A CA  1 
ATOM   668  C C   . ALA A 1 94  ? 144.205 125.302 179.093 1.00 16.14  ? 94  ALA A C   1 
ATOM   669  O O   . ALA A 1 94  ? 145.275 125.242 178.480 1.00 20.81  ? 94  ALA A O   1 
ATOM   670  C CB  . ALA A 1 94  ? 143.906 126.686 181.159 1.00 18.82  ? 94  ALA A CB  1 
ATOM   671  N N   . LEU A 1 95  ? 143.447 124.231 179.297 1.00 12.18  ? 95  LEU A N   1 
ATOM   672  C CA  . LEU A 1 95  ? 143.777 122.921 178.750 1.00 12.70  ? 95  LEU A CA  1 
ATOM   673  C C   . LEU A 1 95  ? 142.843 122.653 177.577 1.00 22.05  ? 95  LEU A C   1 
ATOM   674  O O   . LEU A 1 95  ? 141.639 122.459 177.764 1.00 33.30  ? 95  LEU A O   1 
ATOM   675  C CB  . LEU A 1 95  ? 143.655 121.839 179.819 1.00 16.12  ? 95  LEU A CB  1 
ATOM   676  C CG  . LEU A 1 95  ? 144.179 120.449 179.461 1.00 16.52  ? 95  LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 95  ? 145.453 120.544 178.646 1.00 16.66  ? 95  LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 95  ? 144.421 119.650 180.723 1.00 13.50  ? 95  LEU A CD2 1 
ATOM   679  N N   . ALA A 1 96  ? 143.371 122.684 176.350 1.00 22.95  ? 96  ALA A N   1 
ATOM   680  C CA  . ALA A 1 96  ? 142.572 122.454 175.122 1.00 21.12  ? 96  ALA A CA  1 
ATOM   681  C C   . ALA A 1 96  ? 143.034 121.170 174.436 1.00 20.76  ? 96  ALA A C   1 
ATOM   682  O O   . ALA A 1 96  ? 143.831 121.263 173.482 1.00 23.00  ? 96  ALA A O   1 
ATOM   683  C CB  . ALA A 1 96  ? 142.692 123.650 174.208 1.00 29.53  ? 96  ALA A CB  1 
ATOM   684  N N   . VAL A 1 97  ? 142.565 120.012 174.905 1.00 21.63  ? 97  VAL A N   1 
ATOM   685  C CA  . VAL A 1 97  ? 142.890 118.700 174.266 1.00 30.94  ? 97  VAL A CA  1 
ATOM   686  C C   . VAL A 1 97  ? 141.697 118.369 173.359 1.00 45.62  ? 97  VAL A C   1 
ATOM   687  O O   . VAL A 1 97  ? 140.609 118.084 173.908 1.00 49.86  ? 97  VAL A O   1 
ATOM   688  C CB  . VAL A 1 97  ? 143.194 117.576 175.278 1.00 33.03  ? 97  VAL A CB  1 
ATOM   689  C CG1 . VAL A 1 97  ? 144.540 117.795 175.958 1.00 35.54  ? 97  VAL A CG1 1 
ATOM   690  C CG2 . VAL A 1 97  ? 142.103 117.384 176.325 1.00 30.11  ? 97  VAL A CG2 1 
ATOM   691  N N   . LEU A 1 98  ? 141.866 118.435 172.033 1.00 46.94  ? 98  LEU A N   1 
ATOM   692  C CA  . LEU A 1 98  ? 140.696 118.272 171.128 1.00 45.97  ? 98  LEU A CA  1 
ATOM   693  C C   . LEU A 1 98  ? 141.072 117.838 169.705 1.00 51.25  ? 98  LEU A C   1 
ATOM   694  O O   . LEU A 1 98  ? 142.117 118.295 169.238 1.00 50.70  ? 98  LEU A O   1 
ATOM   695  C CB  . LEU A 1 98  ? 139.955 119.610 171.123 1.00 43.83  ? 98  LEU A CB  1 
ATOM   696  C CG  . LEU A 1 98  ? 140.798 120.890 171.037 1.00 39.59  ? 98  LEU A CG  1 
ATOM   697  C CD1 . LEU A 1 98  ? 141.045 121.330 169.608 1.00 37.64  ? 98  LEU A CD1 1 
ATOM   698  C CD2 . LEU A 1 98  ? 140.123 122.002 171.819 1.00 52.03  ? 98  LEU A CD2 1 
ATOM   699  N N   . SER A 1 99  ? 140.258 116.996 169.051 1.00 57.01  ? 99  SER A N   1 
ATOM   700  C CA  . SER A 1 99  ? 140.434 116.582 167.661 1.00 57.55  ? 99  SER A CA  1 
ATOM   701  C C   . SER A 1 99  ? 141.683 115.737 167.437 1.00 55.50  ? 99  SER A C   1 
ATOM   702  O O   . SER A 1 99  ? 142.084 115.531 166.286 1.00 55.10  ? 99  SER A O   1 
ATOM   703  C CB  . SER A 1 99  ? 140.449 117.792 166.717 1.00 59.45  ? 99  SER A CB  1 
ATOM   704  O OG  . SER A 1 99  ? 139.188 118.439 166.696 1.00 58.49  ? 99  SER A OG  1 
ATOM   705  N N   . ASN A 1 100 ? 142.300 115.279 168.528 1.00 58.88  ? 100 ASN A N   1 
ATOM   706  C CA  . ASN A 1 100 ? 143.557 114.487 168.425 1.00 56.46  ? 100 ASN A CA  1 
ATOM   707  C C   . ASN A 1 100 ? 143.260 113.152 167.736 1.00 58.30  ? 100 ASN A C   1 
ATOM   708  O O   . ASN A 1 100 ? 143.793 112.132 168.221 1.00 60.92  ? 100 ASN A O   1 
ATOM   709  C CB  . ASN A 1 100 ? 144.199 114.301 169.795 1.00 52.78  ? 100 ASN A CB  1 
ATOM   710  C CG  . ASN A 1 100 ? 144.572 115.616 170.435 1.00 52.03  ? 100 ASN A CG  1 
ATOM   711  O OD1 . ASN A 1 100 ? 145.407 116.351 169.899 1.00 52.67  ? 100 ASN A OD1 1 
ATOM   712  N ND2 . ASN A 1 100 ? 143.977 115.924 171.577 1.00 49.88  ? 100 ASN A ND2 1 
ATOM   713  N N   . LEU A 1 108 ? 145.240 110.495 169.553 1.00 64.09  ? 108 LEU A N   1 
ATOM   714  C CA  . LEU A 1 108 ? 145.989 110.477 170.838 1.00 63.92  ? 108 LEU A CA  1 
ATOM   715  C C   . LEU A 1 108 ? 145.331 109.475 171.797 1.00 62.17  ? 108 LEU A C   1 
ATOM   716  O O   . LEU A 1 108 ? 144.119 109.620 172.061 1.00 66.15  ? 108 LEU A O   1 
ATOM   717  C CB  . LEU A 1 108 ? 146.045 111.879 171.441 1.00 61.54  ? 108 LEU A CB  1 
ATOM   718  C CG  . LEU A 1 108 ? 146.633 111.986 172.852 1.00 53.00  ? 108 LEU A CG  1 
ATOM   719  C CD1 . LEU A 1 108 ? 148.102 111.608 172.845 1.00 46.76  ? 108 LEU A CD1 1 
ATOM   720  C CD2 . LEU A 1 108 ? 146.442 113.386 173.406 1.00 43.36  ? 108 LEU A CD2 1 
ATOM   721  N N   . LYS A 1 109 ? 146.101 108.506 172.293 1.00 61.15  ? 109 LYS A N   1 
ATOM   722  C CA  . LYS A 1 109 ? 145.584 107.506 173.219 1.00 66.41  ? 109 LYS A CA  1 
ATOM   723  C C   . LYS A 1 109 ? 145.964 107.784 174.668 1.00 64.23  ? 109 LYS A C   1 
ATOM   724  O O   . LYS A 1 109 ? 145.102 107.752 175.551 1.00 63.61  ? 109 LYS A O   1 
ATOM   725  C CB  . LYS A 1 109 ? 146.078 106.112 172.810 1.00 75.26  ? 109 LYS A CB  1 
ATOM   726  C CG  . LYS A 1 109 ? 145.779 105.018 173.823 1.00 75.51  ? 109 LYS A CG  1 
ATOM   727  C CD  . LYS A 1 109 ? 144.425 104.378 173.566 1.00 75.31  ? 109 LYS A CD  1 
ATOM   728  C CE  . LYS A 1 109 ? 144.488 102.867 173.712 1.00 74.21  ? 109 LYS A CE  1 
ATOM   729  N NZ  . LYS A 1 109 ? 143.535 102.181 172.795 1.00 78.00  ? 109 LYS A NZ  1 
ATOM   730  N N   . GLU A 1 110 ? 147.240 108.053 174.933 1.00 64.12  ? 110 GLU A N   1 
ATOM   731  C CA  . GLU A 1 110 ? 147.737 108.259 176.288 1.00 57.09  ? 110 GLU A CA  1 
ATOM   732  C C   . GLU A 1 110 ? 148.184 109.704 176.447 1.00 52.99  ? 110 GLU A C   1 
ATOM   733  O O   . GLU A 1 110 ? 149.034 110.182 175.688 1.00 50.75  ? 110 GLU A O   1 
ATOM   734  C CB  . GLU A 1 110 ? 148.892 107.304 176.598 1.00 57.65  ? 110 GLU A CB  1 
ATOM   735  C CG  . GLU A 1 110 ? 148.457 105.881 176.903 1.00 68.53  ? 110 GLU A CG  1 
ATOM   736  C CD  . GLU A 1 110 ? 149.551 105.072 177.570 1.00 75.22  ? 110 GLU A CD  1 
ATOM   737  O OE1 . GLU A 1 110 ? 150.224 105.614 178.471 1.00 75.77  ? 110 GLU A OE1 1 
ATOM   738  O OE2 . GLU A 1 110 ? 149.737 103.895 177.195 1.00 70.05  ? 110 GLU A OE2 1 
ATOM   739  N N   . LEU A 1 111 ? 147.612 110.415 177.429 1.00 54.30  ? 111 LEU A N   1 
ATOM   740  C CA  . LEU A 1 111 ? 148.047 111.796 177.776 1.00 46.15  ? 111 LEU A CA  1 
ATOM   741  C C   . LEU A 1 111 ? 148.228 111.798 179.299 1.00 42.62  ? 111 LEU A C   1 
ATOM   742  O O   . LEU A 1 111 ? 147.297 112.241 180.000 1.00 47.29  ? 111 LEU A O   1 
ATOM   743  C CB  . LEU A 1 111 ? 147.065 112.874 177.322 1.00 36.43  ? 111 LEU A CB  1 
ATOM   744  C CG  . LEU A 1 111 ? 147.465 114.323 177.621 1.00 23.25  ? 111 LEU A CG  1 
ATOM   745  C CD1 . LEU A 1 111 ? 148.736 114.723 176.899 1.00 24.86  ? 111 LEU A CD1 1 
ATOM   746  C CD2 . LEU A 1 111 ? 146.341 115.266 177.257 1.00 26.61  ? 111 LEU A CD2 1 
ATOM   747  N N   . PRO A 1 112 ? 149.362 111.303 179.843 1.00 40.71  ? 112 PRO A N   1 
ATOM   748  C CA  . PRO A 1 112 ? 149.547 111.180 181.287 1.00 40.72  ? 112 PRO A CA  1 
ATOM   749  C C   . PRO A 1 112 ? 149.998 112.430 182.021 1.00 46.10  ? 112 PRO A C   1 
ATOM   750  O O   . PRO A 1 112 ? 151.164 112.499 182.449 1.00 57.30  ? 112 PRO A O   1 
ATOM   751  C CB  . PRO A 1 112 ? 150.598 110.065 181.355 1.00 46.49  ? 112 PRO A CB  1 
ATOM   752  C CG  . PRO A 1 112 ? 151.503 110.352 180.183 1.00 48.22  ? 112 PRO A CG  1 
ATOM   753  C CD  . PRO A 1 112 ? 150.570 110.883 179.112 1.00 43.66  ? 112 PRO A CD  1 
ATOM   754  N N   . MET A 1 113 ? 149.146 113.449 182.121 1.00 40.35  ? 113 MET A N   1 
ATOM   755  C CA  . MET A 1 113 ? 149.605 114.701 182.776 1.00 30.47  ? 113 MET A CA  1 
ATOM   756  C C   . MET A 1 113 ? 149.555 114.449 184.289 1.00 36.37  ? 113 MET A C   1 
ATOM   757  O O   . MET A 1 113 ? 148.924 115.248 185.000 1.00 44.25  ? 113 MET A O   1 
ATOM   758  C CB  . MET A 1 113 ? 148.739 115.889 182.351 1.00 28.44  ? 113 MET A CB  1 
ATOM   759  C CG  . MET A 1 113 ? 148.464 115.918 180.863 1.00 24.99  ? 113 MET A CG  1 
ATOM   760  S SD  . MET A 1 113 ? 147.549 117.378 180.335 1.00 7.95   ? 113 MET A SD  1 
ATOM   761  C CE  . MET A 1 113 ? 148.894 118.561 180.201 1.00 17.34  ? 113 MET A CE  1 
ATOM   762  N N   . ARG A 1 114 ? 150.254 113.428 184.776 1.00 40.34  ? 114 ARG A N   1 
ATOM   763  C CA  . ARG A 1 114 ? 150.144 113.026 186.179 1.00 41.92  ? 114 ARG A CA  1 
ATOM   764  C C   . ARG A 1 114 ? 150.483 114.110 187.189 1.00 43.53  ? 114 ARG A C   1 
ATOM   765  O O   . ARG A 1 114 ? 149.797 114.249 188.201 1.00 45.25  ? 114 ARG A O   1 
ATOM   766  C CB  . ARG A 1 114 ? 151.014 111.792 186.442 1.00 46.44  ? 114 ARG A CB  1 
ATOM   767  C CG  . ARG A 1 114 ? 150.990 111.311 187.883 1.00 56.08  ? 114 ARG A CG  1 
ATOM   768  C CD  . ARG A 1 114 ? 152.002 110.199 188.109 1.00 65.56  ? 114 ARG A CD  1 
ATOM   769  N NE  . ARG A 1 114 ? 153.366 110.638 187.829 1.00 68.55  ? 114 ARG A NE  1 
ATOM   770  C CZ  . ARG A 1 114 ? 154.442 109.869 187.965 1.00 68.24  ? 114 ARG A CZ  1 
ATOM   771  N NH1 . ARG A 1 114 ? 154.315 108.616 188.381 1.00 71.59  ? 114 ARG A NH1 1 
ATOM   772  N NH2 . ARG A 1 114 ? 155.644 110.352 187.687 1.00 58.78  ? 114 ARG A NH2 1 
ATOM   773  N N   . ASN A 1 115 ? 151.528 114.879 186.929 1.00 42.58  ? 115 ASN A N   1 
ATOM   774  C CA  . ASN A 1 115 ? 151.879 115.957 187.843 1.00 35.79  ? 115 ASN A CA  1 
ATOM   775  C C   . ASN A 1 115 ? 150.915 117.133 187.773 1.00 34.71  ? 115 ASN A C   1 
ATOM   776  O O   . ASN A 1 115 ? 150.996 118.027 188.622 1.00 42.22  ? 115 ASN A O   1 
ATOM   777  C CB  . ASN A 1 115 ? 153.303 116.439 187.561 1.00 34.85  ? 115 ASN A CB  1 
ATOM   778  C CG  . ASN A 1 115 ? 154.353 115.451 188.027 1.00 41.06  ? 115 ASN A CG  1 
ATOM   779  O OD1 . ASN A 1 115 ? 154.754 115.457 189.190 1.00 40.45  ? 115 ASN A OD1 1 
ATOM   780  N ND2 . ASN A 1 115 ? 154.802 114.593 187.119 1.00 42.10  ? 115 ASN A ND2 1 
ATOM   781  N N   . LEU A 1 116 ? 150.066 117.194 186.736 1.00 26.98  ? 116 LEU A N   1 
ATOM   782  C CA  . LEU A 1 116 ? 149.097 118.310 186.562 1.00 23.08  ? 116 LEU A CA  1 
ATOM   783  C C   . LEU A 1 116 ? 148.106 118.251 187.726 1.00 28.09  ? 116 LEU A C   1 
ATOM   784  O O   . LEU A 1 116 ? 147.213 117.378 187.692 1.00 29.65  ? 116 LEU A O   1 
ATOM   785  C CB  . LEU A 1 116 ? 148.368 118.263 185.220 1.00 21.57  ? 116 LEU A CB  1 
ATOM   786  C CG  . LEU A 1 116 ? 147.438 119.440 184.913 1.00 11.01  ? 116 LEU A CG  1 
ATOM   787  C CD1 . LEU A 1 116 ? 148.207 120.713 184.625 1.00 9.11   ? 116 LEU A CD1 1 
ATOM   788  C CD2 . LEU A 1 116 ? 146.526 119.088 183.755 1.00 20.56  ? 116 LEU A CD2 1 
ATOM   789  N N   . GLN A 1 117 ? 148.275 119.129 188.715 1.00 32.13  ? 117 GLN A N   1 
ATOM   790  C CA  . GLN A 1 117 ? 147.397 119.157 189.911 1.00 32.13  ? 117 GLN A CA  1 
ATOM   791  C C   . GLN A 1 117 ? 146.707 120.522 190.014 1.00 31.90  ? 117 GLN A C   1 
ATOM   792  O O   . GLN A 1 117 ? 145.870 120.675 190.929 1.00 43.53  ? 117 GLN A O   1 
ATOM   793  C CB  . GLN A 1 117 ? 148.254 118.848 191.137 1.00 34.58  ? 117 GLN A CB  1 
ATOM   794  C CG  . GLN A 1 117 ? 148.626 117.376 191.272 1.00 41.39  ? 117 GLN A CG  1 
ATOM   795  C CD  . GLN A 1 117 ? 149.994 117.164 191.882 1.00 35.81  ? 117 GLN A CD  1 
ATOM   796  O OE1 . GLN A 1 117 ? 150.296 117.653 192.976 1.00 36.21  ? 117 GLN A OE1 1 
ATOM   797  N NE2 . GLN A 1 117 ? 150.839 116.432 191.171 1.00 37.89  ? 117 GLN A NE2 1 
ATOM   798  N N   . GLU A 1 118 ? 147.029 121.470 189.127 1.00 25.52  ? 118 GLU A N   1 
ATOM   799  C CA  . GLU A 1 118 ? 146.464 122.839 189.233 1.00 28.54  ? 118 GLU A CA  1 
ATOM   800  C C   . GLU A 1 118 ? 146.349 123.553 187.883 1.00 27.26  ? 118 GLU A C   1 
ATOM   801  O O   . GLU A 1 118 ? 147.309 123.463 187.100 1.00 23.46  ? 118 GLU A O   1 
ATOM   802  C CB  . GLU A 1 118 ? 147.361 123.684 190.136 1.00 28.19  ? 118 GLU A CB  1 
ATOM   803  C CG  . GLU A 1 118 ? 146.834 125.095 190.382 1.00 35.08  ? 118 GLU A CG  1 
ATOM   804  C CD  . GLU A 1 118 ? 145.451 125.146 191.004 1.00 47.00  ? 118 GLU A CD  1 
ATOM   805  O OE1 . GLU A 1 118 ? 145.283 124.608 192.118 1.00 48.03  ? 118 GLU A OE1 1 
ATOM   806  O OE2 . GLU A 1 118 ? 144.543 125.724 190.372 1.00 44.23  ? 118 GLU A OE2 1 
ATOM   807  N N   . ILE A 1 119 ? 145.219 124.212 187.617 1.00 30.37  ? 119 ILE A N   1 
ATOM   808  C CA  . ILE A 1 119 ? 145.039 125.082 186.415 1.00 24.00  ? 119 ILE A CA  1 
ATOM   809  C C   . ILE A 1 119 ? 144.429 126.370 186.987 1.00 30.27  ? 119 ILE A C   1 
ATOM   810  O O   . ILE A 1 119 ? 143.194 126.396 187.161 1.00 40.51  ? 119 ILE A O   1 
ATOM   811  C CB  . ILE A 1 119 ? 144.193 124.410 185.316 1.00 24.70  ? 119 ILE A CB  1 
ATOM   812  C CG1 . ILE A 1 119 ? 144.968 123.282 184.634 1.00 22.50  ? 119 ILE A CG1 1 
ATOM   813  C CG2 . ILE A 1 119 ? 143.697 125.433 184.294 1.00 23.20  ? 119 ILE A CG2 1 
ATOM   814  C CD1 . ILE A 1 119 ? 144.120 122.369 183.767 1.00 12.80  ? 119 ILE A CD1 1 
ATOM   815  N N   . LEU A 1 120 ? 145.244 127.379 187.310 1.00 27.04  ? 120 LEU A N   1 
ATOM   816  C CA  . LEU A 1 120 ? 144.796 128.593 187.984 1.00 27.43  ? 120 LEU A CA  1 
ATOM   817  C C   . LEU A 1 120 ? 143.646 129.250 187.231 1.00 38.78  ? 120 LEU A C   1 
ATOM   818  O O   . LEU A 1 120 ? 142.536 129.389 187.758 1.00 44.25  ? 120 LEU A O   1 
ATOM   819  C CB  . LEU A 1 120 ? 145.969 129.562 188.141 1.00 21.76  ? 120 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 120 ? 147.121 129.075 189.020 1.00 17.38  ? 120 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 120 ? 148.234 130.108 189.065 1.00 17.96  ? 120 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 120 ? 146.628 128.747 190.419 1.00 21.27  ? 120 LEU A CD2 1 
ATOM   823  N N   . HIS A 1 121 ? 143.893 129.660 185.990 1.00 30.95  ? 121 HIS A N   1 
ATOM   824  C CA  . HIS A 1 121 ? 142.905 130.352 185.175 1.00 27.95  ? 121 HIS A CA  1 
ATOM   825  C C   . HIS A 1 121 ? 142.618 129.532 183.928 1.00 32.39  ? 121 HIS A C   1 
ATOM   826  O O   . HIS A 1 121 ? 143.545 129.117 183.227 1.00 36.24  ? 121 HIS A O   1 
ATOM   827  C CB  . HIS A 1 121 ? 143.396 131.751 184.794 1.00 34.32  ? 121 HIS A CB  1 
ATOM   828  C CG  . HIS A 1 121 ? 143.995 132.512 185.936 1.00 40.28  ? 121 HIS A CG  1 
ATOM   829  N ND1 . HIS A 1 121 ? 143.470 132.476 187.210 1.00 44.01  ? 121 HIS A ND1 1 
ATOM   830  C CD2 . HIS A 1 121 ? 145.075 133.326 185.997 1.00 35.66  ? 121 HIS A CD2 1 
ATOM   831  C CE1 . HIS A 1 121 ? 144.200 133.236 188.006 1.00 39.38  ? 121 HIS A CE1 1 
ATOM   832  N NE2 . HIS A 1 121 ? 145.180 133.763 187.295 1.00 36.29  ? 121 HIS A NE2 1 
ATOM   833  N N   . GLY A 1 122 ? 141.341 129.303 183.655 1.00 37.73  ? 122 GLY A N   1 
ATOM   834  C CA  . GLY A 1 122 ? 140.913 128.549 182.494 1.00 33.44  ? 122 GLY A CA  1 
ATOM   835  C C   . GLY A 1 122 ? 140.310 127.209 182.883 1.00 32.38  ? 122 GLY A C   1 
ATOM   836  O O   . GLY A 1 122 ? 140.294 126.809 184.048 1.00 31.80  ? 122 GLY A O   1 
ATOM   837  N N   . ALA A 1 123 ? 139.809 126.516 181.863 1.00 29.30  ? 123 ALA A N   1 
ATOM   838  C CA  . ALA A 1 123 ? 139.177 125.218 182.037 1.00 36.99  ? 123 ALA A CA  1 
ATOM   839  C C   . ALA A 1 123 ? 139.656 124.278 180.940 1.00 39.32  ? 123 ALA A C   1 
ATOM   840  O O   . ALA A 1 123 ? 140.268 124.698 179.955 1.00 44.00  ? 123 ALA A O   1 
ATOM   841  C CB  . ALA A 1 123 ? 137.649 125.329 182.026 1.00 45.38  ? 123 ALA A CB  1 
ATOM   842  N N   . VAL A 1 124 ? 139.367 122.992 181.119 1.00 35.24  ? 124 VAL A N   1 
ATOM   843  C CA  . VAL A 1 124 ? 139.799 121.948 180.197 1.00 31.89  ? 124 VAL A CA  1 
ATOM   844  C C   . VAL A 1 124 ? 138.659 121.635 179.237 1.00 40.84  ? 124 VAL A C   1 
ATOM   845  O O   . VAL A 1 124 ? 137.510 121.456 179.659 1.00 50.01  ? 124 VAL A O   1 
ATOM   846  C CB  . VAL A 1 124 ? 140.253 120.687 180.954 1.00 45.10  ? 124 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 124 ? 139.246 120.313 182.026 1.00 50.58  ? 124 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 124 ? 140.468 119.532 179.989 1.00 47.36  ? 124 VAL A CG2 1 
ATOM   849  N N   . ARG A 1 125 ? 138.991 121.601 177.942 1.00 43.54  ? 125 ARG A N   1 
ATOM   850  C CA  . ARG A 1 125 ? 137.976 121.311 176.899 1.00 52.59  ? 125 ARG A CA  1 
ATOM   851  C C   . ARG A 1 125 ? 138.206 119.899 176.350 1.00 54.44  ? 125 ARG A C   1 
ATOM   852  O O   . ARG A 1 125 ? 139.348 119.600 175.939 1.00 50.78  ? 125 ARG A O   1 
ATOM   853  C CB  . ARG A 1 125 ? 138.065 122.339 175.767 1.00 53.49  ? 125 ARG A CB  1 
ATOM   854  C CG  . ARG A 1 125 ? 137.118 122.072 174.607 1.00 58.40  ? 125 ARG A CG  1 
ATOM   855  C CD  . ARG A 1 125 ? 137.229 123.154 173.547 1.00 63.64  ? 125 ARG A CD  1 
ATOM   856  N NE  . ARG A 1 125 ? 136.381 122.885 172.381 1.00 70.76  ? 125 ARG A NE  1 
ATOM   857  C CZ  . ARG A 1 125 ? 136.290 123.677 171.321 1.00 70.02  ? 125 ARG A CZ  1 
ATOM   858  N NH1 . ARG A 1 125 ? 136.808 124.892 171.356 1.00 67.97  ? 125 ARG A NH1 1 
ATOM   859  N NH2 . ARG A 1 125 ? 135.679 123.252 170.230 1.00 67.16  ? 125 ARG A NH2 1 
ATOM   860  N N   . PHE A 1 126 ? 137.159 119.075 176.338 1.00 58.63  ? 126 PHE A N   1 
ATOM   861  C CA  . PHE A 1 126 ? 137.261 117.677 175.839 1.00 59.14  ? 126 PHE A CA  1 
ATOM   862  C C   . PHE A 1 126 ? 136.347 117.500 174.635 1.00 67.62  ? 126 PHE A C   1 
ATOM   863  O O   . PHE A 1 126 ? 135.112 117.597 174.805 1.00 70.85  ? 126 PHE A O   1 
ATOM   864  C CB  . PHE A 1 126 ? 136.817 116.697 176.926 1.00 67.55  ? 126 PHE A CB  1 
ATOM   865  C CG  . PHE A 1 126 ? 137.936 115.992 177.678 1.00 66.22  ? 126 PHE A CG  1 
ATOM   866  C CD1 . PHE A 1 126 ? 139.165 116.609 177.879 1.00 61.35  ? 126 PHE A CD1 1 
ATOM   867  C CD2 . PHE A 1 126 ? 137.753 114.709 178.181 1.00 63.12  ? 126 PHE A CD2 1 
ATOM   868  C CE1 . PHE A 1 126 ? 140.178 115.959 178.564 1.00 58.25  ? 126 PHE A CE1 1 
ATOM   869  C CE2 . PHE A 1 126 ? 138.770 114.064 178.864 1.00 61.89  ? 126 PHE A CE2 1 
ATOM   870  C CZ  . PHE A 1 126 ? 139.978 114.690 179.054 1.00 68.18  ? 126 PHE A CZ  1 
ATOM   871  N N   . SER A 1 127 ? 136.923 117.237 173.456 1.00 70.90  ? 127 SER A N   1 
ATOM   872  C CA  . SER A 1 127 ? 136.099 117.116 172.224 1.00 72.20  ? 127 SER A CA  1 
ATOM   873  C C   . SER A 1 127 ? 136.845 116.354 171.120 1.00 67.19  ? 127 SER A C   1 
ATOM   874  O O   . SER A 1 127 ? 138.080 116.507 171.030 1.00 62.31  ? 127 SER A O   1 
ATOM   875  C CB  . SER A 1 127 ? 135.663 118.474 171.734 1.00 69.24  ? 127 SER A CB  1 
ATOM   876  O OG  . SER A 1 127 ? 136.785 119.302 171.466 1.00 57.33  ? 127 SER A OG  1 
ATOM   877  N N   . ASN A 1 128 ? 136.121 115.563 170.321 1.00 70.54  ? 128 ASN A N   1 
ATOM   878  C CA  . ASN A 1 128 ? 136.729 114.845 169.163 1.00 73.44  ? 128 ASN A CA  1 
ATOM   879  C C   . ASN A 1 128 ? 137.971 114.054 169.587 1.00 70.03  ? 128 ASN A C   1 
ATOM   880  O O   . ASN A 1 128 ? 138.987 114.137 168.868 1.00 66.89  ? 128 ASN A O   1 
ATOM   881  C CB  . ASN A 1 128 ? 137.045 115.799 168.016 1.00 75.34  ? 128 ASN A CB  1 
ATOM   882  C CG  . ASN A 1 128 ? 135.818 116.527 167.522 1.00 75.35  ? 128 ASN A CG  1 
ATOM   883  O OD1 . ASN A 1 128 ? 135.176 117.254 168.287 1.00 78.25  ? 128 ASN A OD1 1 
ATOM   884  N ND2 . ASN A 1 128 ? 135.477 116.347 166.255 1.00 69.60  ? 128 ASN A ND2 1 
ATOM   885  N N   . ASN A 1 129 ? 137.890 113.297 170.684 1.00 72.82  ? 129 ASN A N   1 
ATOM   886  C CA  . ASN A 1 129 ? 139.029 112.429 171.096 1.00 66.32  ? 129 ASN A CA  1 
ATOM   887  C C   . ASN A 1 129 ? 138.509 111.005 171.325 1.00 67.10  ? 129 ASN A C   1 
ATOM   888  O O   . ASN A 1 129 ? 138.363 110.613 172.503 1.00 71.87  ? 129 ASN A O   1 
ATOM   889  C CB  . ASN A 1 129 ? 139.753 112.981 172.321 1.00 65.55  ? 129 ASN A CB  1 
ATOM   890  C CG  . ASN A 1 129 ? 140.749 114.062 171.976 1.00 58.67  ? 129 ASN A CG  1 
ATOM   891  O OD1 . ASN A 1 129 ? 140.992 114.336 170.796 1.00 51.35  ? 129 ASN A OD1 1 
ATOM   892  N ND2 . ASN A 1 129 ? 141.352 114.671 172.986 1.00 57.03  ? 129 ASN A ND2 1 
ATOM   893  N N   . PRO A 1 130 ? 138.218 110.217 170.264 1.00 70.99  ? 130 PRO A N   1 
ATOM   894  C CA  . PRO A 1 130 ? 137.782 108.821 170.427 1.00 71.90  ? 130 PRO A CA  1 
ATOM   895  C C   . PRO A 1 130 ? 138.875 107.903 170.942 1.00 66.06  ? 130 PRO A C   1 
ATOM   896  O O   . PRO A 1 130 ? 138.583 106.968 171.698 1.00 60.27  ? 130 PRO A O   1 
ATOM   897  C CB  . PRO A 1 130 ? 137.334 108.431 169.012 1.00 68.54  ? 130 PRO A CB  1 
ATOM   898  C CG  . PRO A 1 130 ? 138.130 109.312 168.113 1.00 68.77  ? 130 PRO A CG  1 
ATOM   899  C CD  . PRO A 1 130 ? 138.306 110.612 168.847 1.00 71.61  ? 130 PRO A CD  1 
ATOM   900  N N   . ALA A 1 131 ? 140.130 108.142 170.557 1.00 66.90  ? 131 ALA A N   1 
ATOM   901  C CA  . ALA A 1 131 ? 141.218 107.269 170.979 1.00 69.05  ? 131 ALA A CA  1 
ATOM   902  C C   . ALA A 1 131 ? 141.672 107.559 172.403 1.00 68.79  ? 131 ALA A C   1 
ATOM   903  O O   . ALA A 1 131 ? 142.347 106.723 173.013 1.00 71.26  ? 131 ALA A O   1 
ATOM   904  C CB  . ALA A 1 131 ? 142.401 107.400 170.018 1.00 67.28  ? 131 ALA A CB  1 
ATOM   905  N N   . LEU A 1 132 ? 141.315 108.719 172.947 1.00 69.92  ? 132 LEU A N   1 
ATOM   906  C CA  . LEU A 1 132 ? 141.766 109.095 174.280 1.00 67.65  ? 132 LEU A CA  1 
ATOM   907  C C   . LEU A 1 132 ? 141.052 108.254 175.331 1.00 73.05  ? 132 LEU A C   1 
ATOM   908  O O   . LEU A 1 132 ? 139.824 108.305 175.451 1.00 78.96  ? 132 LEU A O   1 
ATOM   909  C CB  . LEU A 1 132 ? 141.520 110.582 174.521 1.00 56.86  ? 132 LEU A CB  1 
ATOM   910  C CG  . LEU A 1 132 ? 142.124 111.152 175.803 1.00 59.84  ? 132 LEU A CG  1 
ATOM   911  C CD1 . LEU A 1 132 ? 143.536 110.629 175.987 1.00 60.36  ? 132 LEU A CD1 1 
ATOM   912  C CD2 . LEU A 1 132 ? 142.116 112.671 175.770 1.00 66.65  ? 132 LEU A CD2 1 
ATOM   913  N N   . CYS A 1 133 ? 141.824 107.482 176.093 1.00 70.71  ? 133 CYS A N   1 
ATOM   914  C CA  . CYS A 1 133 ? 141.287 106.606 177.120 1.00 74.62  ? 133 CYS A CA  1 
ATOM   915  C C   . CYS A 1 133 ? 141.997 106.868 178.441 1.00 74.78  ? 133 CYS A C   1 
ATOM   916  O O   . CYS A 1 133 ? 143.105 107.410 178.478 1.00 78.67  ? 133 CYS A O   1 
ATOM   917  C CB  . CYS A 1 133 ? 141.428 105.127 176.730 1.00 77.45  ? 133 CYS A CB  1 
ATOM   918  S SG  . CYS A 1 133 ? 143.063 104.424 177.044 1.00 92.35  ? 133 CYS A SG  1 
ATOM   919  N N   . ASN A 1 134 ? 141.337 106.492 179.545 1.00 71.39  ? 134 ASN A N   1 
ATOM   920  C CA  . ASN A 1 134 ? 141.935 106.612 180.911 1.00 69.89  ? 134 ASN A CA  1 
ATOM   921  C C   . ASN A 1 134 ? 142.035 108.077 181.360 1.00 73.36  ? 134 ASN A C   1 
ATOM   922  O O   . ASN A 1 134 ? 142.512 108.307 182.483 1.00 78.07  ? 134 ASN A O   1 
ATOM   923  C CB  . ASN A 1 134 ? 143.252 105.847 181.026 1.00 76.04  ? 134 ASN A CB  1 
ATOM   924  C CG  . ASN A 1 134 ? 143.381 105.153 182.361 1.00 85.62  ? 134 ASN A CG  1 
ATOM   925  O OD1 . ASN A 1 134 ? 142.534 105.336 183.243 1.00 85.07  ? 134 ASN A OD1 1 
ATOM   926  N ND2 . ASN A 1 134 ? 144.427 104.358 182.535 1.00 87.83  ? 134 ASN A ND2 1 
ATOM   927  N N   . VAL A 1 135 ? 141.590 109.029 180.541 1.00 70.19  ? 135 VAL A N   1 
ATOM   928  C CA  . VAL A 1 135 ? 141.589 110.427 180.957 1.00 62.53  ? 135 VAL A CA  1 
ATOM   929  C C   . VAL A 1 135 ? 140.181 110.936 181.255 1.00 61.98  ? 135 VAL A C   1 
ATOM   930  O O   . VAL A 1 135 ? 140.035 111.918 181.999 1.00 63.92  ? 135 VAL A O   1 
ATOM   931  C CB  . VAL A 1 135 ? 142.278 111.306 179.891 1.00 52.11  ? 135 VAL A CB  1 
ATOM   932  C CG1 . VAL A 1 135 ? 142.473 112.725 180.393 1.00 44.79  ? 135 VAL A CG1 1 
ATOM   933  C CG2 . VAL A 1 135 ? 143.618 110.702 179.518 1.00 55.94  ? 135 VAL A CG2 1 
ATOM   934  N N   . GLU A 1 136 ? 139.154 110.260 180.736 1.00 67.09  ? 136 GLU A N   1 
ATOM   935  C CA  . GLU A 1 136 ? 137.755 110.658 181.055 1.00 72.95  ? 136 GLU A CA  1 
ATOM   936  C C   . GLU A 1 136 ? 137.496 110.482 182.561 1.00 79.49  ? 136 GLU A C   1 
ATOM   937  O O   . GLU A 1 136 ? 136.599 111.176 183.086 1.00 82.25  ? 136 GLU A O   1 
ATOM   938  C CB  . GLU A 1 136 ? 136.762 109.850 180.219 1.00 72.73  ? 136 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 136 ? 136.419 110.508 178.886 1.00 78.58  ? 136 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 136 ? 135.454 111.679 178.977 1.00 76.60  ? 136 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 136 ? 135.780 112.683 179.644 1.00 72.91  ? 136 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 136 ? 134.364 111.581 178.376 1.00 75.49  ? 136 GLU A OE2 1 
ATOM   943  N N   . SER A 1 137 ? 138.248 109.601 183.225 1.00 79.45  ? 137 SER A N   1 
ATOM   944  C CA  . SER A 1 137 ? 138.072 109.349 184.648 1.00 79.96  ? 137 SER A CA  1 
ATOM   945  C C   . SER A 1 137 ? 138.908 110.274 185.523 1.00 68.42  ? 137 SER A C   1 
ATOM   946  O O   . SER A 1 137 ? 138.892 110.124 186.749 1.00 69.15  ? 137 SER A O   1 
ATOM   947  C CB  . SER A 1 137 ? 138.413 107.891 184.970 1.00 84.88  ? 137 SER A CB  1 
ATOM   948  O OG  . SER A 1 137 ? 138.106 107.581 186.318 1.00 89.77  ? 137 SER A OG  1 
ATOM   949  N N   . ILE A 1 138 ? 139.657 111.193 184.906 1.00 67.00  ? 138 ILE A N   1 
ATOM   950  C CA  . ILE A 1 138 ? 140.561 112.110 185.664 1.00 66.26  ? 138 ILE A CA  1 
ATOM   951  C C   . ILE A 1 138 ? 139.708 113.048 186.524 1.00 71.12  ? 138 ILE A C   1 
ATOM   952  O O   . ILE A 1 138 ? 138.592 113.401 186.087 1.00 70.48  ? 138 ILE A O   1 
ATOM   953  C CB  . ILE A 1 138 ? 141.508 112.879 184.720 1.00 53.94  ? 138 ILE A CB  1 
ATOM   954  C CG1 . ILE A 1 138 ? 142.757 112.058 184.408 1.00 53.90  ? 138 ILE A CG1 1 
ATOM   955  C CG2 . ILE A 1 138 ? 141.872 114.258 185.273 1.00 53.67  ? 138 ILE A CG2 1 
ATOM   956  C CD1 . ILE A 1 138 ? 143.507 111.588 185.642 1.00 63.51  ? 138 ILE A CD1 1 
ATOM   957  N N   . GLN A 1 139 ? 140.230 113.438 187.686 1.00 73.30  ? 139 GLN A N   1 
ATOM   958  C CA  . GLN A 1 139 ? 139.502 114.326 188.624 1.00 68.12  ? 139 GLN A CA  1 
ATOM   959  C C   . GLN A 1 139 ? 139.862 115.777 188.278 1.00 61.82  ? 139 GLN A C   1 
ATOM   960  O O   . GLN A 1 139 ? 140.767 116.338 188.931 1.00 63.46  ? 139 GLN A O   1 
ATOM   961  C CB  . GLN A 1 139 ? 139.885 113.924 190.047 1.00 66.12  ? 139 GLN A CB  1 
ATOM   962  C CG  . GLN A 1 139 ? 139.964 112.420 190.296 1.00 68.55  ? 139 GLN A CG  1 
ATOM   963  C CD  . GLN A 1 139 ? 138.630 111.709 190.230 1.00 68.15  ? 139 GLN A CD  1 
ATOM   964  O OE1 . GLN A 1 139 ? 138.559 110.477 190.299 1.00 61.50  ? 139 GLN A OE1 1 
ATOM   965  N NE2 . GLN A 1 139 ? 137.556 112.472 190.092 1.00 72.55  ? 139 GLN A NE2 1 
ATOM   966  N N   . TRP A 1 140 ? 139.178 116.362 187.291 1.00 60.36  ? 140 TRP A N   1 
ATOM   967  C CA  . TRP A 1 140 ? 139.458 117.751 186.847 1.00 55.25  ? 140 TRP A CA  1 
ATOM   968  C C   . TRP A 1 140 ? 139.025 118.734 187.930 1.00 60.32  ? 140 TRP A C   1 
ATOM   969  O O   . TRP A 1 140 ? 139.413 119.915 187.850 1.00 61.76  ? 140 TRP A O   1 
ATOM   970  C CB  . TRP A 1 140 ? 138.744 118.037 185.521 1.00 52.04  ? 140 TRP A CB  1 
ATOM   971  C CG  . TRP A 1 140 ? 139.166 117.107 184.417 1.00 52.05  ? 140 TRP A CG  1 
ATOM   972  C CD1 . TRP A 1 140 ? 138.502 116.018 183.937 1.00 48.83  ? 140 TRP A CD1 1 
ATOM   973  C CD2 . TRP A 1 140 ? 140.407 117.175 183.688 1.00 46.63  ? 140 TRP A CD2 1 
ATOM   974  N NE1 . TRP A 1 140 ? 139.227 115.422 182.939 1.00 47.04  ? 140 TRP A NE1 1 
ATOM   975  C CE2 . TRP A 1 140 ? 140.402 116.106 182.769 1.00 44.78  ? 140 TRP A CE2 1 
ATOM   976  C CE3 . TRP A 1 140 ? 141.506 118.037 183.720 1.00 40.13  ? 140 TRP A CE3 1 
ATOM   977  C CZ2 . TRP A 1 140 ? 141.460 115.879 181.893 1.00 43.03  ? 140 TRP A CZ2 1 
ATOM   978  C CZ3 . TRP A 1 140 ? 142.551 117.808 182.857 1.00 36.38  ? 140 TRP A CZ3 1 
ATOM   979  C CH2 . TRP A 1 140 ? 142.525 116.746 181.954 1.00 40.44  ? 140 TRP A CH2 1 
ATOM   980  N N   . ARG A 1 141 ? 138.247 118.269 188.908 1.00 67.21  ? 141 ARG A N   1 
ATOM   981  C CA  . ARG A 1 141 ? 137.793 119.132 190.026 1.00 69.99  ? 141 ARG A CA  1 
ATOM   982  C C   . ARG A 1 141 ? 139.015 119.608 190.822 1.00 66.79  ? 141 ARG A C   1 
ATOM   983  O O   . ARG A 1 141 ? 139.002 120.773 191.267 1.00 67.88  ? 141 ARG A O   1 
ATOM   984  C CB  . ARG A 1 141 ? 136.813 118.378 190.928 1.00 75.56  ? 141 ARG A CB  1 
ATOM   985  C CG  . ARG A 1 141 ? 135.520 117.980 190.230 1.00 72.86  ? 141 ARG A CG  1 
ATOM   986  C CD  . ARG A 1 141 ? 134.301 118.545 190.934 1.00 81.20  ? 141 ARG A CD  1 
ATOM   987  N NE  . ARG A 1 141 ? 134.275 118.182 192.356 1.00 92.43  ? 141 ARG A NE  1 
ATOM   988  C CZ  . ARG A 1 141 ? 134.296 119.033 193.376 1.00 95.34  ? 141 ARG A CZ  1 
ATOM   989  N NH1 . ARG A 1 141 ? 134.646 120.295 193.198 1.00 93.53  ? 141 ARG A NH1 1 
ATOM   990  N NH2 . ARG A 1 141 ? 133.993 118.610 194.589 1.00 88.69  ? 141 ARG A NH2 1 
ATOM   991  N N   . ASP A 1 142 ? 140.023 118.748 190.991 1.00 63.43  ? 142 ASP A N   1 
ATOM   992  C CA  . ASP A 1 142 ? 141.247 119.090 191.769 1.00 60.40  ? 142 ASP A CA  1 
ATOM   993  C C   . ASP A 1 142 ? 142.151 120.006 190.939 1.00 51.60  ? 142 ASP A C   1 
ATOM   994  O O   . ASP A 1 142 ? 142.900 120.796 191.551 1.00 53.98  ? 142 ASP A O   1 
ATOM   995  C CB  . ASP A 1 142 ? 141.964 117.831 192.233 1.00 58.84  ? 142 ASP A CB  1 
ATOM   996  C CG  . ASP A 1 142 ? 143.481 117.928 192.325 1.00 58.85  ? 142 ASP A CG  1 
ATOM   997  O OD1 . ASP A 1 142 ? 143.970 118.798 193.072 1.00 65.17  ? 142 ASP A OD1 1 
ATOM   998  O OD2 . ASP A 1 142 ? 144.160 117.125 191.655 1.00 56.09  ? 142 ASP A OD2 1 
ATOM   999  N N   . ILE A 1 143 ? 142.066 119.942 189.609 1.00 48.44  ? 143 ILE A N   1 
ATOM   1000 C CA  . ILE A 1 143 ? 142.968 120.734 188.719 1.00 48.48  ? 143 ILE A CA  1 
ATOM   1001 C C   . ILE A 1 143 ? 142.298 122.082 188.409 1.00 44.19  ? 143 ILE A C   1 
ATOM   1002 O O   . ILE A 1 143 ? 142.827 123.114 188.868 1.00 35.91  ? 143 ILE A O   1 
ATOM   1003 C CB  . ILE A 1 143 ? 143.310 119.960 187.430 1.00 43.48  ? 143 ILE A CB  1 
ATOM   1004 C CG1 . ILE A 1 143 ? 143.417 118.454 187.670 1.00 44.40  ? 143 ILE A CG1 1 
ATOM   1005 C CG2 . ILE A 1 143 ? 144.581 120.521 186.795 1.00 33.47  ? 143 ILE A CG2 1 
ATOM   1006 C CD1 . ILE A 1 143 ? 143.852 117.671 186.448 1.00 43.41  ? 143 ILE A CD1 1 
ATOM   1007 N N   . VAL A 1 144 ? 141.185 122.076 187.672 1.00 48.63  ? 144 VAL A N   1 
ATOM   1008 C CA  . VAL A 1 144 ? 140.466 123.329 187.292 1.00 44.63  ? 144 VAL A CA  1 
ATOM   1009 C C   . VAL A 1 144 ? 140.086 124.067 188.583 1.00 55.76  ? 144 VAL A C   1 
ATOM   1010 O O   . VAL A 1 144 ? 139.531 123.401 189.484 1.00 58.94  ? 144 VAL A O   1 
ATOM   1011 C CB  . VAL A 1 144 ? 139.236 123.051 186.407 1.00 49.42  ? 144 VAL A CB  1 
ATOM   1012 C CG1 . VAL A 1 144 ? 138.394 124.301 186.180 1.00 57.26  ? 144 VAL A CG1 1 
ATOM   1013 C CG2 . VAL A 1 144 ? 139.631 122.431 185.073 1.00 40.92  ? 144 VAL A CG2 1 
ATOM   1014 N N   . SER A 1 145 ? 140.349 125.374 188.664 1.00 59.06  ? 145 SER A N   1 
ATOM   1015 C CA  . SER A 1 145 ? 140.072 126.190 189.842 1.00 61.89  ? 145 SER A CA  1 
ATOM   1016 C C   . SER A 1 145 ? 139.060 127.272 189.487 1.00 65.06  ? 145 SER A C   1 
ATOM   1017 O O   . SER A 1 145 ? 139.398 128.243 188.801 1.00 64.36  ? 145 SER A O   1 
ATOM   1018 C CB  . SER A 1 145 ? 141.358 126.808 190.389 1.00 54.71  ? 145 SER A CB  1 
ATOM   1019 O OG  . SER A 1 145 ? 141.912 127.730 189.467 1.00 48.05  ? 145 SER A OG  1 
ATOM   1020 N N   . SER A 1 146 ? 137.823 127.098 189.950 1.00 70.82  ? 146 SER A N   1 
ATOM   1021 C CA  . SER A 1 146 ? 136.764 128.104 189.918 1.00 74.51  ? 146 SER A CA  1 
ATOM   1022 C C   . SER A 1 146 ? 136.380 128.542 188.509 1.00 74.18  ? 146 SER A C   1 
ATOM   1023 O O   . SER A 1 146 ? 135.694 129.559 188.350 1.00 69.80  ? 146 SER A O   1 
ATOM   1024 C CB  . SER A 1 146 ? 137.140 129.335 190.754 1.00 67.08  ? 146 SER A CB  1 
ATOM   1025 O OG  . SER A 1 146 ? 137.140 129.029 192.138 1.00 75.75  ? 146 SER A OG  1 
ATOM   1026 N N   . ASP A 1 147 ? 136.797 127.811 187.479 1.00 70.03  ? 147 ASP A N   1 
ATOM   1027 C CA  . ASP A 1 147 ? 136.447 128.123 186.097 1.00 59.01  ? 147 ASP A CA  1 
ATOM   1028 C C   . ASP A 1 147 ? 135.600 127.015 185.480 1.00 61.95  ? 147 ASP A C   1 
ATOM   1029 O O   . ASP A 1 147 ? 135.769 126.655 184.314 1.00 63.43  ? 147 ASP A O   1 
ATOM   1030 C CB  . ASP A 1 147 ? 137.699 128.373 185.262 1.00 53.39  ? 147 ASP A CB  1 
ATOM   1031 C CG  . ASP A 1 147 ? 138.057 129.844 185.177 1.00 50.95  ? 147 ASP A CG  1 
ATOM   1032 O OD1 . ASP A 1 147 ? 137.983 130.535 186.214 1.00 49.80  ? 147 ASP A OD1 1 
ATOM   1033 O OD2 . ASP A 1 147 ? 138.408 130.311 184.073 1.00 48.47  ? 147 ASP A OD2 1 
ATOM   1034 N N   . PHE A 1 148 ? 134.672 126.465 186.265 1.00 70.03  ? 148 PHE A N   1 
ATOM   1035 C CA  . PHE A 1 148 ? 133.815 125.382 185.800 1.00 74.39  ? 148 PHE A CA  1 
ATOM   1036 C C   . PHE A 1 148 ? 132.731 125.852 184.841 1.00 75.91  ? 148 PHE A C   1 
ATOM   1037 O O   . PHE A 1 148 ? 132.032 125.009 184.268 1.00 72.10  ? 148 PHE A O   1 
ATOM   1038 C CB  . PHE A 1 148 ? 133.172 124.680 186.996 1.00 77.31  ? 148 PHE A CB  1 
ATOM   1039 C CG  . PHE A 1 148 ? 134.110 123.781 187.744 1.00 79.48  ? 148 PHE A CG  1 
ATOM   1040 C CD1 . PHE A 1 148 ? 134.643 122.656 187.139 1.00 77.04  ? 148 PHE A CD1 1 
ATOM   1041 C CD2 . PHE A 1 148 ? 134.466 124.066 189.051 1.00 80.29  ? 148 PHE A CD2 1 
ATOM   1042 C CE1 . PHE A 1 148 ? 135.509 121.829 187.825 1.00 75.92  ? 148 PHE A CE1 1 
ATOM   1043 C CE2 . PHE A 1 148 ? 135.332 123.243 189.742 1.00 80.15  ? 148 PHE A CE2 1 
ATOM   1044 C CZ  . PHE A 1 148 ? 135.853 122.124 189.128 1.00 77.60  ? 148 PHE A CZ  1 
ATOM   1045 N N   . LEU A 1 149 ? 132.569 127.166 184.660 1.00 77.62  ? 149 LEU A N   1 
ATOM   1046 C CA  . LEU A 1 149 ? 131.522 127.675 183.779 1.00 77.60  ? 149 LEU A CA  1 
ATOM   1047 C C   . LEU A 1 149 ? 131.711 127.204 182.343 1.00 75.40  ? 149 LEU A C   1 
ATOM   1048 O O   . LEU A 1 149 ? 130.734 127.087 181.595 1.00 80.22  ? 149 LEU A O   1 
ATOM   1049 C CB  . LEU A 1 149 ? 131.486 129.203 183.839 1.00 80.43  ? 149 LEU A CB  1 
ATOM   1050 C CG  . LEU A 1 149 ? 132.822 129.941 183.707 1.00 77.98  ? 149 LEU A CG  1 
ATOM   1051 C CD1 . LEU A 1 149 ? 133.100 130.335 182.261 1.00 72.72  ? 149 LEU A CD1 1 
ATOM   1052 C CD2 . LEU A 1 149 ? 132.853 131.163 184.613 1.00 61.69  ? 149 LEU A CD2 1 
ATOM   1053 N N   . SER A 1 150 ? 132.949 126.931 181.942 1.00 69.12  ? 150 SER A N   1 
ATOM   1054 C CA  . SER A 1 150 ? 133.271 126.462 180.598 1.00 69.61  ? 150 SER A CA  1 
ATOM   1055 C C   . SER A 1 150 ? 134.090 125.183 180.671 1.00 64.24  ? 150 SER A C   1 
ATOM   1056 O O   . SER A 1 150 ? 135.135 125.041 180.032 1.00 60.22  ? 150 SER A O   1 
ATOM   1057 C CB  . SER A 1 150 ? 134.009 127.537 179.808 1.00 67.77  ? 150 SER A CB  1 
ATOM   1058 O OG  . SER A 1 150 ? 133.133 128.584 179.430 1.00 74.00  ? 150 SER A OG  1 
ATOM   1059 N N   . ASN A 1 151 ? 133.625 124.230 181.475 1.00 65.53  ? 151 ASN A N   1 
ATOM   1060 C CA  . ASN A 1 151 ? 134.298 122.942 181.635 1.00 63.15  ? 151 ASN A CA  1 
ATOM   1061 C C   . ASN A 1 151 ? 133.456 121.874 180.943 1.00 63.46  ? 151 ASN A C   1 
ATOM   1062 O O   . ASN A 1 151 ? 132.618 121.219 181.564 1.00 67.52  ? 151 ASN A O   1 
ATOM   1063 C CB  . ASN A 1 151 ? 134.510 122.622 183.109 1.00 69.74  ? 151 ASN A CB  1 
ATOM   1064 C CG  . ASN A 1 151 ? 135.876 122.031 183.383 1.00 69.77  ? 151 ASN A CG  1 
ATOM   1065 O OD1 . ASN A 1 151 ? 136.796 122.179 182.581 1.00 70.88  ? 151 ASN A OD1 1 
ATOM   1066 N ND2 . ASN A 1 151 ? 136.014 121.352 184.515 1.00 63.09  ? 151 ASN A ND2 1 
ATOM   1067 N N   . MET A 1 152 ? 133.683 121.697 179.643 1.00 65.65  ? 152 MET A N   1 
ATOM   1068 C CA  . MET A 1 152 ? 133.023 120.635 178.884 1.00 71.30  ? 152 MET A CA  1 
ATOM   1069 C C   . MET A 1 152 ? 133.952 119.426 178.761 1.00 71.58  ? 152 MET A C   1 
ATOM   1070 O O   . MET A 1 152 ? 134.449 119.070 177.691 1.00 71.05  ? 152 MET A O   1 
ATOM   1071 C CB  . MET A 1 152 ? 132.560 121.154 177.521 1.00 71.56  ? 152 MET A CB  1 
ATOM   1072 C CG  . MET A 1 152 ? 133.633 121.778 176.638 1.00 60.44  ? 152 MET A CG  1 
ATOM   1073 S SD  . MET A 1 152 ? 134.650 122.970 177.518 1.00 72.05  ? 152 MET A SD  1 
ATOM   1074 C CE  . MET A 1 152 ? 133.612 124.422 177.362 1.00 62.39  ? 152 MET A CE  1 
ATOM   1075 N N   . SER A 1 153 ? 134.169 118.779 179.906 1.00 75.16  ? 153 SER A N   1 
ATOM   1076 C CA  . SER A 1 153 ? 134.974 117.560 179.967 1.00 74.61  ? 153 SER A CA  1 
ATOM   1077 C C   . SER A 1 153 ? 134.127 116.345 179.576 1.00 77.88  ? 153 SER A C   1 
ATOM   1078 O O   . SER A 1 153 ? 133.929 115.403 180.343 1.00 76.35  ? 153 SER A O   1 
ATOM   1079 C CB  . SER A 1 153 ? 135.580 117.395 181.354 1.00 66.43  ? 153 SER A CB  1 
ATOM   1080 O OG  . SER A 1 153 ? 136.767 118.158 181.483 1.00 58.29  ? 153 SER A OG  1 
ATOM   1081 N N   . MET A 1 154 ? 133.636 116.376 178.334 1.00 76.91  ? 154 MET A N   1 
ATOM   1082 C CA  . MET A 1 154 ? 132.809 115.250 177.828 1.00 84.77  ? 154 MET A CA  1 
ATOM   1083 C C   . MET A 1 154 ? 133.377 114.786 176.478 1.00 80.26  ? 154 MET A C   1 
ATOM   1084 O O   . MET A 1 154 ? 133.074 115.434 175.454 1.00 76.61  ? 154 MET A O   1 
ATOM   1085 C CB  . MET A 1 154 ? 131.353 115.691 177.647 1.00 91.06  ? 154 MET A CB  1 
ATOM   1086 C CG  . MET A 1 154 ? 130.716 116.231 178.912 1.00 92.96  ? 154 MET A CG  1 
ATOM   1087 S SD  . MET A 1 154 ? 129.183 117.127 178.594 1.00 105.70 ? 154 MET A SD  1 
ATOM   1088 C CE  . MET A 1 154 ? 129.807 118.446 177.543 1.00 83.45  ? 154 MET A CE  1 
ATOM   1089 N N   . ASP A 1 155 ? 134.173 113.712 176.484 1.00 82.53  ? 155 ASP A N   1 
ATOM   1090 C CA  . ASP A 1 155 ? 134.742 113.167 175.221 1.00 83.42  ? 155 ASP A CA  1 
ATOM   1091 C C   . ASP A 1 155 ? 134.137 111.786 174.948 1.00 79.34  ? 155 ASP A C   1 
ATOM   1092 O O   . ASP A 1 155 ? 134.806 110.792 175.305 1.00 76.94  ? 155 ASP A O   1 
ATOM   1093 C CB  . ASP A 1 155 ? 136.261 113.121 175.262 1.00 82.08  ? 155 ASP A CB  1 
ATOM   1094 C CG  . ASP A 1 155 ? 136.956 113.876 174.140 1.00 79.86  ? 155 ASP A CG  1 
ATOM   1095 O OD1 . ASP A 1 155 ? 136.613 113.620 172.967 1.00 79.99  ? 155 ASP A OD1 1 
ATOM   1096 O OD2 . ASP A 1 155 ? 137.844 114.697 174.446 1.00 75.71  ? 155 ASP A OD2 1 
ATOM   1097 N N   . GLY A 1 173 ? 138.789 105.806 190.424 1.00 88.77  ? 173 GLY A N   1 
ATOM   1098 C CA  . GLY A 1 173 ? 139.240 105.766 189.046 1.00 83.04  ? 173 GLY A CA  1 
ATOM   1099 C C   . GLY A 1 173 ? 140.187 106.895 188.694 1.00 86.12  ? 173 GLY A C   1 
ATOM   1100 O O   . GLY A 1 173 ? 140.364 107.229 187.522 1.00 82.82  ? 173 GLY A O   1 
ATOM   1101 N N   . SER A 1 174 ? 140.800 107.486 189.715 1.00 90.05  ? 174 SER A N   1 
ATOM   1102 C CA  . SER A 1 174 ? 141.732 108.594 189.523 1.00 87.02  ? 174 SER A CA  1 
ATOM   1103 C C   . SER A 1 174 ? 143.047 108.047 188.983 1.00 93.64  ? 174 SER A C   1 
ATOM   1104 O O   . SER A 1 174 ? 143.921 107.626 189.745 1.00 89.27  ? 174 SER A O   1 
ATOM   1105 C CB  . SER A 1 174 ? 141.942 109.343 190.834 1.00 84.22  ? 174 SER A CB  1 
ATOM   1106 O OG  . SER A 1 174 ? 142.523 108.502 191.815 1.00 83.12  ? 174 SER A OG  1 
ATOM   1107 N N   . CYS A 1 175 ? 143.196 108.071 187.656 1.00 94.10  ? 175 CYS A N   1 
ATOM   1108 C CA  . CYS A 1 175 ? 144.449 107.581 187.021 1.00 91.19  ? 175 CYS A CA  1 
ATOM   1109 C C   . CYS A 1 175 ? 144.585 108.202 185.624 1.00 78.50  ? 175 CYS A C   1 
ATOM   1110 O O   . CYS A 1 175 ? 143.668 108.001 184.812 1.00 73.61  ? 175 CYS A O   1 
ATOM   1111 C CB  . CYS A 1 175 ? 144.440 106.062 186.902 1.00 96.54  ? 175 CYS A CB  1 
ATOM   1112 S SG  . CYS A 1 175 ? 145.802 105.404 185.905 1.00 115.00 ? 175 CYS A SG  1 
ATOM   1113 N N   . TRP A 1 176 ? 145.675 108.927 185.353 1.00 73.19  ? 176 TRP A N   1 
ATOM   1114 C CA  . TRP A 1 176 ? 145.859 109.605 184.045 1.00 60.62  ? 176 TRP A CA  1 
ATOM   1115 C C   . TRP A 1 176 ? 146.029 108.566 182.944 1.00 67.97  ? 176 TRP A C   1 
ATOM   1116 O O   . TRP A 1 176 ? 145.542 108.831 181.824 1.00 64.27  ? 176 TRP A O   1 
ATOM   1117 C CB  . TRP A 1 176 ? 147.056 110.560 184.072 1.00 50.06  ? 176 TRP A CB  1 
ATOM   1118 C CG  . TRP A 1 176 ? 146.745 111.909 184.657 1.00 47.33  ? 176 TRP A CG  1 
ATOM   1119 C CD1 . TRP A 1 176 ? 146.897 112.281 185.956 1.00 53.84  ? 176 TRP A CD1 1 
ATOM   1120 C CD2 . TRP A 1 176 ? 146.206 113.059 183.971 1.00 45.79  ? 176 TRP A CD2 1 
ATOM   1121 N NE1 . TRP A 1 176 ? 146.528 113.586 186.127 1.00 57.64  ? 176 TRP A NE1 1 
ATOM   1122 C CE2 . TRP A 1 176 ? 146.087 114.086 184.931 1.00 48.31  ? 176 TRP A CE2 1 
ATOM   1123 C CE3 . TRP A 1 176 ? 145.816 113.322 182.655 1.00 46.17  ? 176 TRP A CE3 1 
ATOM   1124 C CZ2 . TRP A 1 176 ? 145.600 115.349 184.612 1.00 37.97  ? 176 TRP A CZ2 1 
ATOM   1125 C CZ3 . TRP A 1 176 ? 145.329 114.571 182.342 1.00 38.75  ? 176 TRP A CZ3 1 
ATOM   1126 C CH2 . TRP A 1 176 ? 145.227 115.570 183.308 1.00 33.33  ? 176 TRP A CH2 1 
ATOM   1127 N N   . GLY A 1 177 ? 146.686 107.436 183.226 1.00 75.65  ? 177 GLY A N   1 
ATOM   1128 C CA  . GLY A 1 177 ? 146.814 106.360 182.224 1.00 80.49  ? 177 GLY A CA  1 
ATOM   1129 C C   . GLY A 1 177 ? 148.045 105.509 182.457 1.00 86.39  ? 177 GLY A C   1 
ATOM   1130 O O   . GLY A 1 177 ? 148.524 105.475 183.610 1.00 81.25  ? 177 GLY A O   1 
ATOM   1131 N N   . ALA A 1 178 ? 148.522 104.820 181.415 1.00 90.79  ? 178 ALA A N   1 
ATOM   1132 C CA  . ALA A 1 178 ? 149.762 104.015 181.523 1.00 92.66  ? 178 ALA A CA  1 
ATOM   1133 C C   . ALA A 1 178 ? 149.697 103.103 182.750 1.00 96.93  ? 178 ALA A C   1 
ATOM   1134 O O   . ALA A 1 178 ? 150.680 103.070 183.520 1.00 92.04  ? 178 ALA A O   1 
ATOM   1135 C CB  . ALA A 1 178 ? 150.964 104.933 181.581 1.00 82.88  ? 178 ALA A CB  1 
ATOM   1136 N N   . GLY A 1 179 ? 148.587 102.378 182.924 1.00 96.06  ? 179 GLY A N   1 
ATOM   1137 C CA  . GLY A 1 179 ? 148.489 101.455 184.043 1.00 93.40  ? 179 GLY A CA  1 
ATOM   1138 C C   . GLY A 1 179 ? 148.628 102.173 185.371 1.00 95.02  ? 179 GLY A C   1 
ATOM   1139 O O   . GLY A 1 179 ? 147.975 103.190 185.627 1.00 92.04  ? 179 GLY A O   1 
ATOM   1140 N N   . GLU A 1 180 ? 149.541 101.684 186.214 1.00 93.61  ? 180 GLU A N   1 
ATOM   1141 C CA  . GLU A 1 180 ? 149.773 102.328 187.536 1.00 90.29  ? 180 GLU A CA  1 
ATOM   1142 C C   . GLU A 1 180 ? 150.791 103.470 187.378 1.00 86.86  ? 180 GLU A C   1 
ATOM   1143 O O   . GLU A 1 180 ? 151.024 103.888 186.223 1.00 84.70  ? 180 GLU A O   1 
ATOM   1144 C CB  . GLU A 1 180 ? 150.232 101.278 188.548 1.00 85.75  ? 180 GLU A CB  1 
ATOM   1145 C CG  . GLU A 1 180 ? 149.966 101.674 189.997 1.00 89.57  ? 180 GLU A CG  1 
ATOM   1146 C CD  . GLU A 1 180 ? 148.572 102.227 190.233 1.00 90.23  ? 180 GLU A CD  1 
ATOM   1147 O OE1 . GLU A 1 180 ? 147.591 101.490 189.996 1.00 90.63  ? 180 GLU A OE1 1 
ATOM   1148 O OE2 . GLU A 1 180 ? 148.469 103.400 190.649 1.00 82.78  ? 180 GLU A OE2 1 
ATOM   1149 N N   . GLU A 1 181 ? 151.350 103.967 188.489 1.00 88.72  ? 181 GLU A N   1 
ATOM   1150 C CA  . GLU A 1 181 ? 152.351 105.071 188.460 1.00 86.47  ? 181 GLU A CA  1 
ATOM   1151 C C   . GLU A 1 181 ? 151.664 106.381 188.039 1.00 86.73  ? 181 GLU A C   1 
ATOM   1152 O O   . GLU A 1 181 ? 151.626 107.316 188.866 1.00 82.73  ? 181 GLU A O   1 
ATOM   1153 C CB  . GLU A 1 181 ? 153.530 104.747 187.540 1.00 84.07  ? 181 GLU A CB  1 
ATOM   1154 C CG  . GLU A 1 181 ? 154.880 105.183 188.103 1.00 87.10  ? 181 GLU A CG  1 
ATOM   1155 C CD  . GLU A 1 181 ? 155.227 106.657 187.990 1.00 92.28  ? 181 GLU A CD  1 
ATOM   1156 O OE1 . GLU A 1 181 ? 154.428 107.431 187.423 1.00 82.79  ? 181 GLU A OE1 1 
ATOM   1157 O OE2 . GLU A 1 181 ? 156.313 107.034 188.477 1.00 95.98  ? 181 GLU A OE2 1 
ATOM   1158 N N   . ASN A 1 182 ? 151.139 106.441 186.812 1.00 88.92  ? 182 ASN A N   1 
ATOM   1159 C CA  . ASN A 1 182 ? 150.467 107.677 186.320 1.00 77.22  ? 182 ASN A CA  1 
ATOM   1160 C C   . ASN A 1 182 ? 149.072 107.772 186.950 1.00 76.83  ? 182 ASN A C   1 
ATOM   1161 O O   . ASN A 1 182 ? 148.119 107.219 186.362 1.00 78.83  ? 182 ASN A O   1 
ATOM   1162 C CB  . ASN A 1 182 ? 150.468 107.735 184.797 1.00 69.61  ? 182 ASN A CB  1 
ATOM   1163 C CG  . ASN A 1 182 ? 151.872 107.704 184.243 1.00 67.22  ? 182 ASN A CG  1 
ATOM   1164 O OD1 . ASN A 1 182 ? 152.840 107.662 185.010 1.00 69.30  ? 182 ASN A OD1 1 
ATOM   1165 N ND2 . ASN A 1 182 ? 152.009 107.726 182.926 1.00 64.72  ? 182 ASN A ND2 1 
ATOM   1166 N N   . CYS A 1 183 ? 148.957 108.452 188.094 1.00 75.00  ? 183 CYS A N   1 
ATOM   1167 C CA  . CYS A 1 183 ? 147.643 108.630 188.765 1.00 82.82  ? 183 CYS A CA  1 
ATOM   1168 C C   . CYS A 1 183 ? 147.324 110.132 188.873 1.00 85.09  ? 183 CYS A C   1 
ATOM   1169 O O   . CYS A 1 183 ? 148.254 110.948 188.702 1.00 82.06  ? 183 CYS A O   1 
ATOM   1170 C CB  . CYS A 1 183 ? 147.659 107.985 190.145 1.00 88.83  ? 183 CYS A CB  1 
ATOM   1171 S SG  . CYS A 1 183 ? 146.246 108.438 191.185 1.00 93.14  ? 183 CYS A SG  1 
ATOM   1172 N N   . GLN A 1 184 ? 146.062 110.498 189.127 1.00 81.73  ? 184 GLN A N   1 
ATOM   1173 C CA  . GLN A 1 184 ? 145.646 111.919 189.277 1.00 71.74  ? 184 GLN A CA  1 
ATOM   1174 C C   . GLN A 1 184 ? 146.186 112.477 190.604 1.00 75.52  ? 184 GLN A C   1 
ATOM   1175 O O   . GLN A 1 184 ? 146.116 113.710 190.782 1.00 78.08  ? 184 GLN A O   1 
ATOM   1176 C CB  . GLN A 1 184 ? 144.121 112.019 189.209 1.00 77.09  ? 184 GLN A CB  1 
ATOM   1177 C CG  . GLN A 1 184 ? 143.537 113.408 189.458 1.00 74.24  ? 184 GLN A CG  1 
ATOM   1178 C CD  . GLN A 1 184 ? 144.202 114.509 188.659 1.00 72.89  ? 184 GLN A CD  1 
ATOM   1179 O OE1 . GLN A 1 184 ? 144.311 114.439 187.432 1.00 75.95  ? 184 GLN A OE1 1 
ATOM   1180 N NE2 . GLN A 1 184 ? 144.661 115.543 189.348 1.00 62.36  ? 184 GLN A NE2 1 
ATOM   1181 N N   . LYS A 1 185 ? 146.706 111.629 191.500 1.00 77.14  ? 185 LYS A N   1 
ATOM   1182 C CA  . LYS A 1 185 ? 147.301 112.092 192.787 1.00 75.03  ? 185 LYS A CA  1 
ATOM   1183 C C   . LYS A 1 185 ? 146.437 113.239 193.342 1.00 80.09  ? 185 LYS A C   1 
ATOM   1184 O O   . LYS A 1 185 ? 146.919 114.394 193.375 1.00 78.83  ? 185 LYS A O   1 
ATOM   1185 C CB  . LYS A 1 185 ? 148.795 112.429 192.644 1.00 72.04  ? 185 LYS A CB  1 
ATOM   1186 C CG  . LYS A 1 185 ? 149.219 113.393 191.543 1.00 69.18  ? 185 LYS A CG  1 
ATOM   1187 C CD  . LYS A 1 185 ? 150.520 113.010 190.851 1.00 64.04  ? 185 LYS A CD  1 
ATOM   1188 C CE  . LYS A 1 185 ? 151.706 113.003 191.761 1.00 54.16  ? 185 LYS A CE  1 
ATOM   1189 N NZ  . LYS A 1 185 ? 152.930 112.664 191.031 1.00 49.30  ? 185 LYS A NZ  1 
ATOM   1190 N N   . LEU A 1 186 ? 145.210 112.924 193.770 1.00 83.63  ? 186 LEU A N   1 
ATOM   1191 C CA  . LEU A 1 186 ? 144.273 113.967 194.267 1.00 87.37  ? 186 LEU A CA  1 
ATOM   1192 C C   . LEU A 1 186 ? 144.889 114.747 195.439 1.00 88.21  ? 186 LEU A C   1 
ATOM   1193 O O   . LEU A 1 186 ? 145.590 114.123 196.265 1.00 89.01  ? 186 LEU A O   1 
ATOM   1194 C CB  . LEU A 1 186 ? 142.943 113.328 194.664 1.00 85.55  ? 186 LEU A CB  1 
ATOM   1195 C CG  . LEU A 1 186 ? 141.923 113.164 193.534 1.00 81.65  ? 186 LEU A CG  1 
ATOM   1196 C CD1 . LEU A 1 186 ? 140.632 112.564 194.061 1.00 80.43  ? 186 LEU A CD1 1 
ATOM   1197 C CD2 . LEU A 1 186 ? 141.662 114.513 192.888 1.00 76.62  ? 186 LEU A CD2 1 
ATOM   1198 N N   . THR A 1 187 ? 144.620 116.054 195.508 1.00 81.37  ? 187 THR A N   1 
ATOM   1199 C CA  . THR A 1 187 ? 145.120 116.895 196.589 1.00 80.19  ? 187 THR A CA  1 
ATOM   1200 C C   . THR A 1 187 ? 144.207 118.056 196.957 1.00 81.39  ? 187 THR A C   1 
ATOM   1201 O O   . THR A 1 187 ? 144.380 118.623 198.043 1.00 85.13  ? 187 THR A O   1 
ATOM   1202 C CB  . THR A 1 187 ? 146.507 117.457 196.237 1.00 80.48  ? 187 THR A CB  1 
ATOM   1203 O OG1 . THR A 1 187 ? 147.114 118.012 197.410 1.00 80.70  ? 187 THR A OG1 1 
ATOM   1204 C CG2 . THR A 1 187 ? 146.396 118.535 195.168 1.00 73.42  ? 187 THR A CG2 1 
ATOM   1205 N N   . LYS A 1 188 ? 143.251 118.430 196.108 1.00 79.18  ? 188 LYS A N   1 
ATOM   1206 C CA  . LYS A 1 188 ? 142.352 119.545 196.381 1.00 78.42  ? 188 LYS A CA  1 
ATOM   1207 C C   . LYS A 1 188 ? 140.934 119.098 196.707 1.00 81.53  ? 188 LYS A C   1 
ATOM   1208 O O   . LYS A 1 188 ? 140.280 119.705 197.561 1.00 85.04  ? 188 LYS A O   1 
ATOM   1209 C CB  . LYS A 1 188 ? 142.324 120.502 195.185 1.00 69.43  ? 188 LYS A CB  1 
ATOM   1210 C CG  . LYS A 1 188 ? 141.485 121.752 195.385 1.00 65.99  ? 188 LYS A CG  1 
ATOM   1211 C CD  . LYS A 1 188 ? 140.660 122.058 194.145 1.00 62.46  ? 188 LYS A CD  1 
ATOM   1212 C CE  . LYS A 1 188 ? 140.686 123.540 193.810 1.00 50.94  ? 188 LYS A CE  1 
ATOM   1213 N NZ  . LYS A 1 188 ? 140.262 123.796 192.405 1.00 48.71  ? 188 LYS A NZ  1 
ATOM   1214 N N   . ILE A 1 189 ? 140.446 118.050 196.053 1.00 77.17  ? 189 ILE A N   1 
ATOM   1215 C CA  . ILE A 1 189 ? 139.098 117.557 196.299 1.00 84.73  ? 189 ILE A CA  1 
ATOM   1216 C C   . ILE A 1 189 ? 139.142 116.311 197.174 1.00 86.33  ? 189 ILE A C   1 
ATOM   1217 O O   . ILE A 1 189 ? 138.425 116.214 198.170 1.00 91.55  ? 189 ILE A O   1 
ATOM   1218 C CB  . ILE A 1 189 ? 138.364 117.270 194.979 1.00 88.86  ? 189 ILE A CB  1 
ATOM   1219 C CG1 . ILE A 1 189 ? 138.512 118.455 194.022 1.00 80.82  ? 189 ILE A CG1 1 
ATOM   1220 C CG2 . ILE A 1 189 ? 136.896 116.963 195.240 1.00 88.37  ? 189 ILE A CG2 1 
ATOM   1221 C CD1 . ILE A 1 189 ? 137.677 119.659 194.401 1.00 73.86  ? 189 ILE A CD1 1 
ATOM   1222 N N   . ASN A 1 210 ? 148.812 130.203 201.948 1.00 68.55  ? 210 ASN A N   1 
ATOM   1223 C CA  . ASN A 1 210 ? 147.882 129.988 200.845 1.00 75.66  ? 210 ASN A CA  1 
ATOM   1224 C C   . ASN A 1 210 ? 148.488 130.430 199.519 1.00 67.34  ? 210 ASN A C   1 
ATOM   1225 O O   . ASN A 1 210 ? 147.774 130.862 198.614 1.00 59.34  ? 210 ASN A O   1 
ATOM   1226 C CB  . ASN A 1 210 ? 146.571 130.735 201.095 1.00 76.27  ? 210 ASN A CB  1 
ATOM   1227 C CG  . ASN A 1 210 ? 145.359 129.958 200.622 1.00 70.40  ? 210 ASN A CG  1 
ATOM   1228 O OD1 . ASN A 1 210 ? 145.310 129.495 199.482 1.00 66.16  ? 210 ASN A OD1 1 
ATOM   1229 N ND2 . ASN A 1 210 ? 144.371 129.811 201.497 1.00 70.44  ? 210 ASN A ND2 1 
ATOM   1230 N N   . GLN A 1 211 ? 149.812 130.321 199.407 1.00 62.79  ? 211 GLN A N   1 
ATOM   1231 C CA  . GLN A 1 211 ? 150.525 130.703 198.195 1.00 55.45  ? 211 GLN A CA  1 
ATOM   1232 C C   . GLN A 1 211 ? 151.115 129.499 197.466 1.00 52.47  ? 211 GLN A C   1 
ATOM   1233 O O   . GLN A 1 211 ? 151.969 129.664 196.589 1.00 46.83  ? 211 GLN A O   1 
ATOM   1234 C CB  . GLN A 1 211 ? 151.616 131.723 198.523 1.00 54.16  ? 211 GLN A CB  1 
ATOM   1235 C CG  . GLN A 1 211 ? 151.871 132.722 197.407 1.00 55.97  ? 211 GLN A CG  1 
ATOM   1236 C CD  . GLN A 1 211 ? 150.806 133.799 197.335 1.00 57.12  ? 211 GLN A CD  1 
ATOM   1237 O OE1 . GLN A 1 211 ? 150.699 134.511 196.339 1.00 54.52  ? 211 GLN A OE1 1 
ATOM   1238 N NE2 . GLN A 1 211 ? 150.020 133.930 198.397 1.00 57.90  ? 211 GLN A NE2 1 
ATOM   1239 N N   . CYS A 1 212 ? 150.676 128.293 197.812 1.00 51.35  ? 212 CYS A N   1 
ATOM   1240 C CA  . CYS A 1 212 ? 151.085 127.078 197.121 1.00 49.67  ? 212 CYS A CA  1 
ATOM   1241 C C   . CYS A 1 212 ? 149.937 126.597 196.244 1.00 50.51  ? 212 CYS A C   1 
ATOM   1242 O O   . CYS A 1 212 ? 148.810 126.436 196.722 1.00 55.07  ? 212 CYS A O   1 
ATOM   1243 C CB  . CYS A 1 212 ? 151.493 125.993 198.117 1.00 53.18  ? 212 CYS A CB  1 
ATOM   1244 S SG  . CYS A 1 212 ? 152.798 126.500 199.259 1.00 65.33  ? 212 CYS A SG  1 
ATOM   1245 N N   . ALA A 1 213 ? 150.227 126.369 194.963 1.00 42.15  ? 213 ALA A N   1 
ATOM   1246 C CA  . ALA A 1 213 ? 149.183 126.077 193.986 1.00 45.89  ? 213 ALA A CA  1 
ATOM   1247 C C   . ALA A 1 213 ? 148.909 124.580 193.862 1.00 52.99  ? 213 ALA A C   1 
ATOM   1248 O O   . ALA A 1 213 ? 147.788 124.126 194.109 1.00 50.29  ? 213 ALA A O   1 
ATOM   1249 C CB  . ALA A 1 213 ? 149.566 126.670 192.626 1.00 41.72  ? 213 ALA A CB  1 
ATOM   1250 N N   . ALA A 1 214 ? 149.924 123.802 193.482 1.00 45.16  ? 214 ALA A N   1 
ATOM   1251 C CA  . ALA A 1 214 ? 149.717 122.374 193.264 1.00 41.11  ? 214 ALA A CA  1 
ATOM   1252 C C   . ALA A 1 214 ? 149.617 121.626 194.588 1.00 57.56  ? 214 ALA A C   1 
ATOM   1253 O O   . ALA A 1 214 ? 148.606 120.975 194.874 1.00 60.19  ? 214 ALA A O   1 
ATOM   1254 C CB  . ALA A 1 214 ? 150.846 121.805 192.404 1.00 38.49  ? 214 ALA A CB  1 
ATOM   1255 N N   . GLY A 1 215 ? 150.657 121.710 195.408 1.00 64.63  ? 215 GLY A N   1 
ATOM   1256 C CA  . GLY A 1 215 ? 150.663 121.024 196.678 1.00 67.98  ? 215 GLY A CA  1 
ATOM   1257 C C   . GLY A 1 215 ? 151.697 121.612 197.610 1.00 68.99  ? 215 GLY A C   1 
ATOM   1258 O O   . GLY A 1 215 ? 152.330 122.627 197.308 1.00 64.28  ? 215 GLY A O   1 
ATOM   1259 N N   . CYS A 1 216 ? 151.862 120.957 198.755 1.00 74.76  ? 216 CYS A N   1 
ATOM   1260 C CA  . CYS A 1 216 ? 152.796 121.398 199.778 1.00 81.52  ? 216 CYS A CA  1 
ATOM   1261 C C   . CYS A 1 216 ? 153.667 120.232 200.221 1.00 87.20  ? 216 CYS A C   1 
ATOM   1262 O O   . CYS A 1 216 ? 153.235 119.077 200.224 1.00 84.24  ? 216 CYS A O   1 
ATOM   1263 C CB  . CYS A 1 216 ? 152.065 121.989 200.992 1.00 81.75  ? 216 CYS A CB  1 
ATOM   1264 S SG  . CYS A 1 216 ? 151.146 123.508 200.650 1.00 55.17  ? 216 CYS A SG  1 
ATOM   1265 N N   . THR A 1 217 ? 154.905 120.552 200.595 1.00 89.61  ? 217 THR A N   1 
ATOM   1266 C CA  . THR A 1 217 ? 155.829 119.560 201.129 1.00 92.20  ? 217 THR A CA  1 
ATOM   1267 C C   . THR A 1 217 ? 156.241 119.970 202.537 1.00 97.27  ? 217 THR A C   1 
ATOM   1268 O O   . THR A 1 217 ? 157.421 119.906 202.897 1.00 98.32  ? 217 THR A O   1 
ATOM   1269 C CB  . THR A 1 217 ? 157.053 119.412 200.221 1.00 89.67  ? 217 THR A CB  1 
ATOM   1270 O OG1 . THR A 1 217 ? 156.654 119.567 198.853 1.00 79.49  ? 217 THR A OG1 1 
ATOM   1271 C CG2 . THR A 1 217 ? 157.683 118.035 200.393 1.00 87.79  ? 217 THR A CG2 1 
ATOM   1272 N N   . GLY A 1 218 ? 155.269 120.401 203.336 1.00 97.18  ? 218 GLY A N   1 
ATOM   1273 C CA  . GLY A 1 218 ? 155.527 120.895 204.666 1.00 104.68 ? 218 GLY A CA  1 
ATOM   1274 C C   . GLY A 1 218 ? 154.797 122.197 204.925 1.00 108.81 ? 218 GLY A C   1 
ATOM   1275 O O   . GLY A 1 218 ? 154.503 122.964 204.002 1.00 102.99 ? 218 GLY A O   1 
ATOM   1276 N N   . PRO A 1 219 ? 154.487 122.476 206.198 1.00 115.14 ? 219 PRO A N   1 
ATOM   1277 C CA  . PRO A 1 219 ? 153.741 123.686 206.568 1.00 112.76 ? 219 PRO A CA  1 
ATOM   1278 C C   . PRO A 1 219 ? 154.599 124.951 206.594 1.00 108.76 ? 219 PRO A C   1 
ATOM   1279 O O   . PRO A 1 219 ? 154.564 125.729 207.549 1.00 101.46 ? 219 PRO A O   1 
ATOM   1280 C CB  . PRO A 1 219 ? 153.204 123.337 207.959 1.00 109.00 ? 219 PRO A CB  1 
ATOM   1281 C CG  . PRO A 1 219 ? 154.235 122.426 208.527 1.00 107.03 ? 219 PRO A CG  1 
ATOM   1282 C CD  . PRO A 1 219 ? 154.800 121.639 207.370 1.00 109.55 ? 219 PRO A CD  1 
ATOM   1283 N N   . ARG A 1 220 ? 155.376 125.157 205.533 1.00 109.92 ? 220 ARG A N   1 
ATOM   1284 C CA  . ARG A 1 220 ? 156.227 126.329 205.404 1.00 102.25 ? 220 ARG A CA  1 
ATOM   1285 C C   . ARG A 1 220 ? 156.128 126.864 203.984 1.00 98.07  ? 220 ARG A C   1 
ATOM   1286 O O   . ARG A 1 220 ? 156.104 126.090 203.023 1.00 96.82  ? 220 ARG A O   1 
ATOM   1287 C CB  . ARG A 1 220 ? 157.688 126.002 205.746 1.00 99.25  ? 220 ARG A CB  1 
ATOM   1288 C CG  . ARG A 1 220 ? 158.618 127.205 205.738 1.00 96.76  ? 220 ARG A CG  1 
ATOM   1289 C CD  . ARG A 1 220 ? 158.226 128.216 206.803 1.00 93.02  ? 220 ARG A CD  1 
ATOM   1290 N NE  . ARG A 1 220 ? 157.644 129.422 206.225 1.00 92.08  ? 220 ARG A NE  1 
ATOM   1291 C CZ  . ARG A 1 220 ? 156.627 130.090 206.751 1.00 91.20  ? 220 ARG A CZ  1 
ATOM   1292 N NH1 . ARG A 1 220 ? 156.050 129.699 207.875 1.00 91.54  ? 220 ARG A NH1 1 
ATOM   1293 N NH2 . ARG A 1 220 ? 156.177 131.179 206.133 1.00 86.20  ? 220 ARG A NH2 1 
ATOM   1294 N N   . GLU A 1 221 ? 156.070 128.191 203.860 1.00 94.31  ? 221 GLU A N   1 
ATOM   1295 C CA  . GLU A 1 221 ? 155.995 128.812 202.543 1.00 90.91  ? 221 GLU A CA  1 
ATOM   1296 C C   . GLU A 1 221 ? 157.303 128.699 201.773 1.00 92.83  ? 221 GLU A C   1 
ATOM   1297 O O   . GLU A 1 221 ? 157.314 128.921 200.558 1.00 89.55  ? 221 GLU A O   1 
ATOM   1298 C CB  . GLU A 1 221 ? 155.597 130.283 202.677 1.00 85.44  ? 221 GLU A CB  1 
ATOM   1299 C CG  . GLU A 1 221 ? 154.197 130.499 203.226 1.00 83.90  ? 221 GLU A CG  1 
ATOM   1300 C CD  . GLU A 1 221 ? 153.124 129.917 202.329 1.00 80.95  ? 221 GLU A CD  1 
ATOM   1301 O OE1 . GLU A 1 221 ? 152.986 130.390 201.181 1.00 79.13  ? 221 GLU A OE1 1 
ATOM   1302 O OE2 . GLU A 1 221 ? 152.417 128.986 202.770 1.00 78.70  ? 221 GLU A OE2 1 
ATOM   1303 N N   . SER A 1 222 ? 158.402 128.358 202.448 1.00 94.35  ? 222 SER A N   1 
ATOM   1304 C CA  . SER A 1 222 ? 159.698 128.242 201.794 1.00 94.44  ? 222 SER A CA  1 
ATOM   1305 C C   . SER A 1 222 ? 159.858 126.948 201.006 1.00 93.38  ? 222 SER A C   1 
ATOM   1306 O O   . SER A 1 222 ? 160.812 126.832 200.230 1.00 90.98  ? 222 SER A O   1 
ATOM   1307 C CB  . SER A 1 222 ? 160.820 128.350 202.830 1.00 94.86  ? 222 SER A CB  1 
ATOM   1308 O OG  . SER A 1 222 ? 160.701 129.540 203.590 1.00 91.79  ? 222 SER A OG  1 
ATOM   1309 N N   . ASP A 1 223 ? 158.961 125.979 201.182 1.00 87.87  ? 223 ASP A N   1 
ATOM   1310 C CA  . ASP A 1 223 ? 159.058 124.684 200.511 1.00 86.73  ? 223 ASP A CA  1 
ATOM   1311 C C   . ASP A 1 223 ? 157.696 124.336 199.916 1.00 85.62  ? 223 ASP A C   1 
ATOM   1312 O O   . ASP A 1 223 ? 156.798 123.878 200.628 1.00 89.12  ? 223 ASP A O   1 
ATOM   1313 C CB  . ASP A 1 223 ? 159.531 123.601 201.477 1.00 96.47  ? 223 ASP A CB  1 
ATOM   1314 C CG  . ASP A 1 223 ? 159.704 122.253 200.805 1.00 93.68  ? 223 ASP A CG  1 
ATOM   1315 O OD1 . ASP A 1 223 ? 159.853 122.217 199.565 1.00 88.41  ? 223 ASP A OD1 1 
ATOM   1316 O OD2 . ASP A 1 223 ? 159.690 121.227 201.517 1.00 88.29  ? 223 ASP A OD2 1 
ATOM   1317 N N   . CYS A 1 224 ? 157.550 124.553 198.611 1.00 84.60  ? 224 CYS A N   1 
ATOM   1318 C CA  . CYS A 1 224 ? 156.351 124.158 197.889 1.00 76.57  ? 224 CYS A CA  1 
ATOM   1319 C C   . CYS A 1 224 ? 156.722 123.897 196.437 1.00 67.90  ? 224 CYS A C   1 
ATOM   1320 O O   . CYS A 1 224 ? 157.731 124.399 195.935 1.00 71.67  ? 224 CYS A O   1 
ATOM   1321 C CB  . CYS A 1 224 ? 155.248 125.219 197.991 1.00 69.39  ? 224 CYS A CB  1 
ATOM   1322 S SG  . CYS A 1 224 ? 154.056 124.908 199.318 1.00 85.32  ? 224 CYS A SG  1 
ATOM   1323 N N   . LEU A 1 225 ? 155.893 123.093 195.767 1.00 57.74  ? 225 LEU A N   1 
ATOM   1324 C CA  . LEU A 1 225 ? 156.192 122.687 194.397 1.00 47.28  ? 225 LEU A CA  1 
ATOM   1325 C C   . LEU A 1 225 ? 156.212 123.886 193.457 1.00 47.06  ? 225 LEU A C   1 
ATOM   1326 O O   . LEU A 1 225 ? 157.247 124.213 192.865 1.00 42.57  ? 225 LEU A O   1 
ATOM   1327 C CB  . LEU A 1 225 ? 155.177 121.643 193.927 1.00 42.62  ? 225 LEU A CB  1 
ATOM   1328 C CG  . LEU A 1 225 ? 154.590 120.721 194.996 1.00 50.43  ? 225 LEU A CG  1 
ATOM   1329 C CD1 . LEU A 1 225 ? 153.402 119.951 194.443 1.00 41.93  ? 225 LEU A CD1 1 
ATOM   1330 C CD2 . LEU A 1 225 ? 155.649 119.765 195.524 1.00 54.96  ? 225 LEU A CD2 1 
ATOM   1331 N N   . VAL A 1 226 ? 155.073 124.555 193.306 1.00 49.34  ? 226 VAL A N   1 
ATOM   1332 C CA  . VAL A 1 226 ? 154.952 125.724 192.443 1.00 42.00  ? 226 VAL A CA  1 
ATOM   1333 C C   . VAL A 1 226 ? 154.237 126.822 193.216 1.00 44.09  ? 226 VAL A C   1 
ATOM   1334 O O   . VAL A 1 226 ? 153.197 126.576 193.836 1.00 45.34  ? 226 VAL A O   1 
ATOM   1335 C CB  . VAL A 1 226 ? 154.201 125.400 191.137 1.00 31.09  ? 226 VAL A CB  1 
ATOM   1336 C CG1 . VAL A 1 226 ? 155.140 124.749 190.135 1.00 25.94  ? 226 VAL A CG1 1 
ATOM   1337 C CG2 . VAL A 1 226 ? 153.015 124.498 191.419 1.00 25.02  ? 226 VAL A CG2 1 
ATOM   1338 N N   . CYS A 1 227 ? 154.798 128.026 193.184 1.00 40.12  ? 227 CYS A N   1 
ATOM   1339 C CA  . CYS A 1 227 ? 154.201 129.159 193.874 1.00 42.86  ? 227 CYS A CA  1 
ATOM   1340 C C   . CYS A 1 227 ? 152.979 129.659 193.118 1.00 40.86  ? 227 CYS A C   1 
ATOM   1341 O O   . CYS A 1 227 ? 152.958 129.679 191.884 1.00 35.77  ? 227 CYS A O   1 
ATOM   1342 C CB  . CYS A 1 227 ? 155.222 130.283 194.032 1.00 52.14  ? 227 CYS A CB  1 
ATOM   1343 S SG  . CYS A 1 227 ? 156.418 129.995 195.354 1.00 92.73  ? 227 CYS A SG  1 
ATOM   1344 N N   . ARG A 1 228 ? 151.953 130.059 193.872 1.00 42.18  ? 228 ARG A N   1 
ATOM   1345 C CA  . ARG A 1 228 ? 150.708 130.502 193.252 1.00 33.96  ? 228 ARG A CA  1 
ATOM   1346 C C   . ARG A 1 228 ? 150.915 131.764 192.424 1.00 31.52  ? 228 ARG A C   1 
ATOM   1347 O O   . ARG A 1 228 ? 150.405 131.868 191.303 1.00 30.48  ? 228 ARG A O   1 
ATOM   1348 C CB  . ARG A 1 228 ? 149.642 130.731 194.323 1.00 39.28  ? 228 ARG A CB  1 
ATOM   1349 C CG  . ARG A 1 228 ? 148.311 131.217 193.777 1.00 30.42  ? 228 ARG A CG  1 
ATOM   1350 C CD  . ARG A 1 228 ? 147.165 130.841 194.701 1.00 34.98  ? 228 ARG A CD  1 
ATOM   1351 N NE  . ARG A 1 228 ? 147.004 129.396 194.810 1.00 46.16  ? 228 ARG A NE  1 
ATOM   1352 C CZ  . ARG A 1 228 ? 145.834 128.772 194.823 1.00 48.36  ? 228 ARG A CZ  1 
ATOM   1353 N NH1 . ARG A 1 228 ? 144.694 129.438 194.734 1.00 45.53  ? 228 ARG A NH1 1 
ATOM   1354 N NH2 . ARG A 1 228 ? 145.806 127.447 194.927 1.00 41.18  ? 228 ARG A NH2 1 
ATOM   1355 N N   . LYS A 1 229 ? 151.659 132.734 192.955 1.00 37.21  ? 229 LYS A N   1 
ATOM   1356 C CA  . LYS A 1 229 ? 151.888 133.993 192.260 1.00 34.07  ? 229 LYS A CA  1 
ATOM   1357 C C   . LYS A 1 229 ? 153.350 134.193 191.882 1.00 35.29  ? 229 LYS A C   1 
ATOM   1358 O O   . LYS A 1 229 ? 153.664 134.349 190.699 1.00 32.68  ? 229 LYS A O   1 
ATOM   1359 C CB  . LYS A 1 229 ? 151.394 135.163 193.123 1.00 38.53  ? 229 LYS A CB  1 
ATOM   1360 C CG  . LYS A 1 229 ? 149.885 135.204 193.312 1.00 38.34  ? 229 LYS A CG  1 
ATOM   1361 C CD  . LYS A 1 229 ? 149.193 135.892 192.147 1.00 37.09  ? 229 LYS A CD  1 
ATOM   1362 C CE  . LYS A 1 229 ? 149.826 137.239 191.841 1.00 29.30  ? 229 LYS A CE  1 
ATOM   1363 N NZ  . LYS A 1 229 ? 149.931 137.484 190.376 1.00 28.42  ? 229 LYS A NZ  1 
ATOM   1364 N N   . PHE A 1 230 ? 154.262 134.182 192.854 1.00 37.65  ? 230 PHE A N   1 
ATOM   1365 C CA  . PHE A 1 230 ? 155.665 134.459 192.579 1.00 38.05  ? 230 PHE A CA  1 
ATOM   1366 C C   . PHE A 1 230 ? 156.542 133.696 193.560 1.00 45.90  ? 230 PHE A C   1 
ATOM   1367 O O   . PHE A 1 230 ? 156.101 133.291 194.638 1.00 49.51  ? 230 PHE A O   1 
ATOM   1368 C CB  . PHE A 1 230 ? 155.978 135.961 192.655 1.00 31.18  ? 230 PHE A CB  1 
ATOM   1369 C CG  . PHE A 1 230 ? 155.124 136.807 191.755 1.00 28.37  ? 230 PHE A CG  1 
ATOM   1370 C CD1 . PHE A 1 230 ? 155.438 136.954 190.417 1.00 29.63  ? 230 PHE A CD1 1 
ATOM   1371 C CD2 . PHE A 1 230 ? 154.008 137.457 192.250 1.00 36.90  ? 230 PHE A CD2 1 
ATOM   1372 C CE1 . PHE A 1 230 ? 154.651 137.729 189.589 1.00 25.40  ? 230 PHE A CE1 1 
ATOM   1373 C CE2 . PHE A 1 230 ? 153.220 138.236 191.427 1.00 36.41  ? 230 PHE A CE2 1 
ATOM   1374 C CZ  . PHE A 1 230 ? 153.543 138.372 190.095 1.00 27.84  ? 230 PHE A CZ  1 
ATOM   1375 N N   . ARG A 1 231 ? 157.807 133.499 193.183 1.00 48.04  ? 231 ARG A N   1 
ATOM   1376 C CA  . ARG A 1 231 ? 158.776 132.839 194.095 1.00 50.41  ? 231 ARG A CA  1 
ATOM   1377 C C   . ARG A 1 231 ? 160.064 133.673 194.083 1.00 59.79  ? 231 ARG A C   1 
ATOM   1378 O O   . ARG A 1 231 ? 160.756 133.669 193.043 1.00 61.46  ? 231 ARG A O   1 
ATOM   1379 C CB  . ARG A 1 231 ? 159.074 131.400 193.662 1.00 56.01  ? 231 ARG A CB  1 
ATOM   1380 C CG  . ARG A 1 231 ? 160.221 130.749 194.422 1.00 61.89  ? 231 ARG A CG  1 
ATOM   1381 C CD  . ARG A 1 231 ? 160.152 129.231 194.398 1.00 58.98  ? 231 ARG A CD  1 
ATOM   1382 N NE  . ARG A 1 231 ? 159.016 128.739 195.184 1.00 58.32  ? 231 ARG A NE  1 
ATOM   1383 C CZ  . ARG A 1 231 ? 158.700 127.462 195.362 1.00 59.92  ? 231 ARG A CZ  1 
ATOM   1384 N NH1 . ARG A 1 231 ? 159.481 126.511 194.883 1.00 66.29  ? 231 ARG A NH1 1 
ATOM   1385 N NH2 . ARG A 1 231 ? 157.602 127.143 196.022 1.00 61.43  ? 231 ARG A NH2 1 
ATOM   1386 N N   . ASP A 1 232 ? 160.351 134.413 195.156 1.00 63.35  ? 232 ASP A N   1 
ATOM   1387 C CA  . ASP A 1 232 ? 161.550 135.293 195.172 1.00 64.43  ? 232 ASP A CA  1 
ATOM   1388 C C   . ASP A 1 232 ? 162.774 134.428 194.865 1.00 66.02  ? 232 ASP A C   1 
ATOM   1389 O O   . ASP A 1 232 ? 163.447 134.717 193.855 1.00 61.66  ? 232 ASP A O   1 
ATOM   1390 C CB  . ASP A 1 232 ? 161.699 136.075 196.464 1.00 71.05  ? 232 ASP A CB  1 
ATOM   1391 C CG  . ASP A 1 232 ? 161.552 135.249 197.727 1.00 79.46  ? 232 ASP A CG  1 
ATOM   1392 O OD1 . ASP A 1 232 ? 160.489 134.631 197.865 1.00 75.54  ? 232 ASP A OD1 1 
ATOM   1393 O OD2 . ASP A 1 232 ? 162.500 135.226 198.538 1.00 82.42  ? 232 ASP A OD2 1 
ATOM   1394 N N   . GLU A 1 233 ? 163.043 133.401 195.679 1.00 70.52  ? 233 GLU A N   1 
ATOM   1395 C CA  . GLU A 1 233 ? 164.203 132.501 195.454 1.00 74.20  ? 233 GLU A CA  1 
ATOM   1396 C C   . GLU A 1 233 ? 163.811 131.095 195.925 1.00 73.10  ? 233 GLU A C   1 
ATOM   1397 O O   . GLU A 1 233 ? 164.304 130.111 195.333 1.00 72.81  ? 233 GLU A O   1 
ATOM   1398 C CB  . GLU A 1 233 ? 165.436 133.005 196.206 1.00 81.40  ? 233 GLU A CB  1 
ATOM   1399 C CG  . GLU A 1 233 ? 166.071 134.241 195.576 1.00 84.29  ? 233 GLU A CG  1 
ATOM   1400 C CD  . GLU A 1 233 ? 167.190 134.868 196.387 1.00 87.19  ? 233 GLU A CD  1 
ATOM   1401 O OE1 . GLU A 1 233 ? 168.192 134.172 196.650 1.00 83.74  ? 233 GLU A OE1 1 
ATOM   1402 O OE2 . GLU A 1 233 ? 167.059 136.055 196.753 1.00 94.61  ? 233 GLU A OE2 1 
ATOM   1403 N N   . ALA A 1 234 ? 162.953 131.015 196.947 1.00 74.88  ? 234 ALA A N   1 
ATOM   1404 C CA  . ALA A 1 234 ? 162.506 129.703 197.471 1.00 81.12  ? 234 ALA A CA  1 
ATOM   1405 C C   . ALA A 1 234 ? 161.132 129.840 198.127 1.00 77.95  ? 234 ALA A C   1 
ATOM   1406 O O   . ALA A 1 234 ? 160.354 128.863 198.099 1.00 78.82  ? 234 ALA A O   1 
ATOM   1407 C CB  . ALA A 1 234 ? 163.527 129.167 198.449 1.00 84.28  ? 234 ALA A CB  1 
ATOM   1408 N N   . THR A 1 235 ? 160.839 131.008 198.704 1.00 76.97  ? 235 THR A N   1 
ATOM   1409 C CA  . THR A 1 235 ? 159.560 131.171 199.433 1.00 82.04  ? 235 THR A CA  1 
ATOM   1410 C C   . THR A 1 235 ? 158.505 131.734 198.506 1.00 80.69  ? 235 THR A C   1 
ATOM   1411 O O   . THR A 1 235 ? 158.862 132.533 197.612 1.00 69.05  ? 235 THR A O   1 
ATOM   1412 C CB  . THR A 1 235 ? 159.752 132.026 200.687 1.00 82.99  ? 235 THR A CB  1 
ATOM   1413 O OG1 . THR A 1 235 ? 158.525 132.732 200.853 1.00 80.59  ? 235 THR A OG1 1 
ATOM   1414 C CG2 . THR A 1 235 ? 160.905 133.004 200.563 1.00 77.32  ? 235 THR A CG2 1 
ATOM   1415 N N   . CYS A 1 236 ? 157.249 131.336 198.711 1.00 83.95  ? 236 CYS A N   1 
ATOM   1416 C CA  . CYS A 1 236 ? 156.145 131.783 197.873 1.00 72.40  ? 236 CYS A CA  1 
ATOM   1417 C C   . CYS A 1 236 ? 155.667 133.148 198.354 1.00 70.57  ? 236 CYS A C   1 
ATOM   1418 O O   . CYS A 1 236 ? 155.205 133.284 199.492 1.00 67.33  ? 236 CYS A O   1 
ATOM   1419 C CB  . CYS A 1 236 ? 155.005 130.768 197.905 1.00 69.92  ? 236 CYS A CB  1 
ATOM   1420 S SG  . CYS A 1 236 ? 155.294 129.302 196.895 1.00 71.28  ? 236 CYS A SG  1 
ATOM   1421 N N   . LYS A 1 237 ? 155.804 134.145 197.474 1.00 67.87  ? 237 LYS A N   1 
ATOM   1422 C CA  . LYS A 1 237 ? 155.427 135.534 197.832 1.00 59.79  ? 237 LYS A CA  1 
ATOM   1423 C C   . LYS A 1 237 ? 154.191 135.965 197.035 1.00 55.76  ? 237 LYS A C   1 
ATOM   1424 O O   . LYS A 1 237 ? 154.083 135.578 195.853 1.00 59.76  ? 237 LYS A O   1 
ATOM   1425 C CB  . LYS A 1 237 ? 156.598 136.462 197.501 1.00 53.22  ? 237 LYS A CB  1 
ATOM   1426 C CG  . LYS A 1 237 ? 157.885 136.166 198.253 1.00 66.01  ? 237 LYS A CG  1 
ATOM   1427 C CD  . LYS A 1 237 ? 157.699 136.245 199.762 1.00 69.50  ? 237 LYS A CD  1 
ATOM   1428 C CE  . LYS A 1 237 ? 158.995 136.153 200.499 1.00 71.81  ? 237 LYS A CE  1 
ATOM   1429 N NZ  . LYS A 1 237 ? 159.917 137.213 200.086 1.00 68.83  ? 237 LYS A NZ  1 
ATOM   1430 N N   . ASP A 1 238 ? 153.298 136.731 197.662 1.00 49.23  ? 238 ASP A N   1 
ATOM   1431 C CA  . ASP A 1 238 ? 152.124 137.252 196.972 1.00 47.03  ? 238 ASP A CA  1 
ATOM   1432 C C   . ASP A 1 238 ? 152.516 138.172 195.825 1.00 45.22  ? 238 ASP A C   1 
ATOM   1433 O O   . ASP A 1 238 ? 151.825 138.217 194.802 1.00 45.61  ? 238 ASP A O   1 
ATOM   1434 C CB  . ASP A 1 238 ? 151.214 137.987 197.956 1.00 52.92  ? 238 ASP A CB  1 
ATOM   1435 C CG  . ASP A 1 238 ? 149.777 138.058 197.479 1.00 57.72  ? 238 ASP A CG  1 
ATOM   1436 O OD1 . ASP A 1 238 ? 149.478 138.910 196.616 1.00 56.75  ? 238 ASP A OD1 1 
ATOM   1437 O OD2 . ASP A 1 238 ? 148.947 137.261 197.964 1.00 58.56  ? 238 ASP A OD2 1 
ATOM   1438 N N   . THR A 1 239 ? 153.612 138.909 195.978 1.00 46.56  ? 239 THR A N   1 
ATOM   1439 C CA  . THR A 1 239 ? 154.116 139.774 194.922 1.00 47.43  ? 239 THR A CA  1 
ATOM   1440 C C   . THR A 1 239 ? 155.618 139.924 195.103 1.00 57.24  ? 239 THR A C   1 
ATOM   1441 O O   . THR A 1 239 ? 156.161 139.661 196.179 1.00 68.13  ? 239 THR A O   1 
ATOM   1442 C CB  . THR A 1 239 ? 153.432 141.144 194.934 1.00 48.62  ? 239 THR A CB  1 
ATOM   1443 O OG1 . THR A 1 239 ? 154.005 141.974 193.916 1.00 49.80  ? 239 THR A OG1 1 
ATOM   1444 C CG2 . THR A 1 239 ? 153.606 141.815 196.288 1.00 46.76  ? 239 THR A CG2 1 
ATOM   1445 N N   . CYS A 1 240 ? 156.302 140.360 194.041 1.00 58.47  ? 240 CYS A N   1 
ATOM   1446 C CA  . CYS A 1 240 ? 157.781 140.487 194.058 1.00 65.74  ? 240 CYS A CA  1 
ATOM   1447 C C   . CYS A 1 240 ? 158.197 141.713 194.882 1.00 64.43  ? 240 CYS A C   1 
ATOM   1448 O O   . CYS A 1 240 ? 157.443 142.710 194.883 1.00 65.76  ? 240 CYS A O   1 
ATOM   1449 C CB  . CYS A 1 240 ? 158.322 140.566 192.636 1.00 61.94  ? 240 CYS A CB  1 
ATOM   1450 S SG  . CYS A 1 240 ? 158.196 138.987 191.758 1.00 68.05  ? 240 CYS A SG  1 
ATOM   1451 N N   . PRO A 1 241 ? 159.354 141.681 195.578 1.00 66.51  ? 241 PRO A N   1 
ATOM   1452 C CA  . PRO A 1 241 ? 159.758 142.796 196.419 1.00 77.30  ? 241 PRO A CA  1 
ATOM   1453 C C   . PRO A 1 241 ? 159.654 144.105 195.646 1.00 84.34  ? 241 PRO A C   1 
ATOM   1454 O O   . PRO A 1 241 ? 160.254 144.199 194.555 1.00 86.15  ? 241 PRO A O   1 
ATOM   1455 C CB  . PRO A 1 241 ? 161.191 142.399 196.779 1.00 80.41  ? 241 PRO A CB  1 
ATOM   1456 C CG  . PRO A 1 241 ? 161.140 140.899 196.815 1.00 77.86  ? 241 PRO A CG  1 
ATOM   1457 C CD  . PRO A 1 241 ? 160.310 140.578 195.591 1.00 70.64  ? 241 PRO A CD  1 
ATOM   1458 N N   . PRO A 1 242 ? 158.923 145.133 196.141 1.00 85.44  ? 242 PRO A N   1 
ATOM   1459 C CA  . PRO A 1 242 ? 158.709 146.354 195.371 1.00 77.79  ? 242 PRO A CA  1 
ATOM   1460 C C   . PRO A 1 242 ? 159.999 147.008 194.921 1.00 77.87  ? 242 PRO A C   1 
ATOM   1461 O O   . PRO A 1 242 ? 160.992 146.923 195.659 1.00 85.24  ? 242 PRO A O   1 
ATOM   1462 C CB  . PRO A 1 242 ? 157.932 147.244 196.351 1.00 80.76  ? 242 PRO A CB  1 
ATOM   1463 C CG  . PRO A 1 242 ? 157.227 146.258 197.244 1.00 82.12  ? 242 PRO A CG  1 
ATOM   1464 C CD  . PRO A 1 242 ? 158.262 145.169 197.438 1.00 86.19  ? 242 PRO A CD  1 
ATOM   1465 N N   . LEU A 1 243 ? 159.986 147.652 193.752 1.00 73.44  ? 243 LEU A N   1 
ATOM   1466 C CA  . LEU A 1 243 ? 161.187 148.337 193.208 1.00 80.91  ? 243 LEU A CA  1 
ATOM   1467 C C   . LEU A 1 243 ? 161.275 149.742 193.819 1.00 91.45  ? 243 LEU A C   1 
ATOM   1468 O O   . LEU A 1 243 ? 162.343 150.332 193.680 1.00 93.20  ? 243 LEU A O   1 
ATOM   1469 C CB  . LEU A 1 243 ? 161.101 148.375 191.685 1.00 81.00  ? 243 LEU A CB  1 
ATOM   1470 C CG  . LEU A 1 243 ? 160.926 147.022 190.986 1.00 82.01  ? 243 LEU A CG  1 
ATOM   1471 C CD1 . LEU A 1 243 ? 160.827 147.227 189.489 1.00 79.46  ? 243 LEU A CD1 1 
ATOM   1472 C CD2 . LEU A 1 243 ? 162.042 146.046 191.316 1.00 77.16  ? 243 LEU A CD2 1 
ATOM   1473 N N   . MET A 1 244 ? 160.185 150.297 194.359 1.00 93.83  ? 244 MET A N   1 
ATOM   1474 C CA  . MET A 1 244 ? 160.181 151.570 195.065 1.00 94.39  ? 244 MET A CA  1 
ATOM   1475 C C   . MET A 1 244 ? 159.831 151.341 196.529 1.00 94.68  ? 244 MET A C   1 
ATOM   1476 O O   . MET A 1 244 ? 158.808 150.722 196.839 1.00 91.59  ? 244 MET A O   1 
ATOM   1477 C CB  . MET A 1 244 ? 159.187 152.542 194.429 1.00 90.66  ? 244 MET A CB  1 
ATOM   1478 C CG  . MET A 1 244 ? 159.308 152.655 192.919 1.00 88.33  ? 244 MET A CG  1 
ATOM   1479 S SD  . MET A 1 244 ? 160.793 153.536 192.402 1.00 105.25 ? 244 MET A SD  1 
ATOM   1480 C CE  . MET A 1 244 ? 161.571 152.305 191.360 1.00 93.26  ? 244 MET A CE  1 
ATOM   1481 N N   . LEU A 1 245 ? 160.713 151.839 197.401 1.00 101.49 ? 245 LEU A N   1 
ATOM   1482 C CA  . LEU A 1 245 ? 160.493 151.713 198.861 1.00 102.41 ? 245 LEU A CA  1 
ATOM   1483 C C   . LEU A 1 245 ? 160.242 153.112 199.434 1.00 101.76 ? 245 LEU A C   1 
ATOM   1484 O O   . LEU A 1 245 ? 160.932 154.061 199.006 1.00 99.47  ? 245 LEU A O   1 
ATOM   1485 C CB  . LEU A 1 245 ? 161.701 151.047 199.514 1.00 101.22 ? 245 LEU A CB  1 
ATOM   1486 C CG  . LEU A 1 245 ? 161.401 150.220 200.767 1.00 98.96  ? 245 LEU A CG  1 
ATOM   1487 C CD1 . LEU A 1 245 ? 160.479 149.077 200.388 1.00 95.80  ? 245 LEU A CD1 1 
ATOM   1488 C CD2 . LEU A 1 245 ? 162.677 149.695 201.399 1.00 99.08  ? 245 LEU A CD2 1 
ATOM   1489 N N   . TYR A 1 246 ? 159.265 153.216 200.341 1.00 101.14 ? 246 TYR A N   1 
ATOM   1490 C CA  . TYR A 1 246 ? 158.921 154.507 200.988 1.00 102.62 ? 246 TYR A CA  1 
ATOM   1491 C C   . TYR A 1 246 ? 159.777 154.653 202.227 1.00 105.02 ? 246 TYR A C   1 
ATOM   1492 O O   . TYR A 1 246 ? 159.971 153.645 202.940 1.00 104.21 ? 246 TYR A O   1 
ATOM   1493 C CB  . TYR A 1 246 ? 157.439 154.567 201.362 1.00 101.68 ? 246 TYR A CB  1 
ATOM   1494 C CG  . TYR A 1 246 ? 157.039 155.887 202.001 1.00 101.08 ? 246 TYR A CG  1 
ATOM   1495 C CD1 . TYR A 1 246 ? 156.620 156.958 201.223 1.00 100.64 ? 246 TYR A CD1 1 
ATOM   1496 C CD2 . TYR A 1 246 ? 157.098 156.067 203.378 1.00 105.09 ? 246 TYR A CD2 1 
ATOM   1497 C CE1 . TYR A 1 246 ? 156.260 158.165 201.794 1.00 103.34 ? 246 TYR A CE1 1 
ATOM   1498 C CE2 . TYR A 1 246 ? 156.740 157.269 203.962 1.00 108.25 ? 246 TYR A CE2 1 
ATOM   1499 C CZ  . TYR A 1 246 ? 156.324 158.320 203.166 1.00 106.14 ? 246 TYR A CZ  1 
ATOM   1500 O OH  . TYR A 1 246 ? 155.965 159.508 203.725 1.00 100.26 ? 246 TYR A OH  1 
ATOM   1501 N N   . ASN A 1 247 ? 160.276 155.861 202.480 1.00 106.57 ? 247 ASN A N   1 
ATOM   1502 C CA  . ASN A 1 247 ? 161.138 156.140 203.659 1.00 106.95 ? 247 ASN A CA  1 
ATOM   1503 C C   . ASN A 1 247 ? 160.596 157.394 204.348 1.00 105.88 ? 247 ASN A C   1 
ATOM   1504 O O   . ASN A 1 247 ? 160.669 158.472 203.723 1.00 105.65 ? 247 ASN A O   1 
ATOM   1505 C CB  . ASN A 1 247 ? 162.607 156.273 203.269 1.00 103.77 ? 247 ASN A CB  1 
ATOM   1506 C CG  . ASN A 1 247 ? 162.828 156.993 201.958 1.00 104.01 ? 247 ASN A CG  1 
ATOM   1507 O OD1 . ASN A 1 247 ? 161.901 157.572 201.383 1.00 102.87 ? 247 ASN A OD1 1 
ATOM   1508 N ND2 . ASN A 1 247 ? 164.061 156.986 201.475 1.00 102.66 ? 247 ASN A ND2 1 
ATOM   1509 N N   . PRO A 1 248 ? 160.036 157.332 205.577 1.00 105.63 ? 248 PRO A N   1 
ATOM   1510 C CA  . PRO A 1 248 ? 159.466 158.547 206.182 1.00 101.21 ? 248 PRO A CA  1 
ATOM   1511 C C   . PRO A 1 248 ? 160.442 159.707 206.257 1.00 100.15 ? 248 PRO A C   1 
ATOM   1512 O O   . PRO A 1 248 ? 160.003 160.859 206.349 1.00 98.71  ? 248 PRO A O   1 
ATOM   1513 C CB  . PRO A 1 248 ? 159.043 158.079 207.582 1.00 103.31 ? 248 PRO A CB  1 
ATOM   1514 C CG  . PRO A 1 248 ? 158.926 156.589 207.473 1.00 103.83 ? 248 PRO A CG  1 
ATOM   1515 C CD  . PRO A 1 248 ? 159.974 156.177 206.486 1.00 105.71 ? 248 PRO A CD  1 
ATOM   1516 N N   . THR A 1 249 ? 161.751 159.442 206.235 1.00 104.05 ? 249 THR A N   1 
ATOM   1517 C CA  . THR A 1 249 ? 162.727 160.527 206.260 1.00 100.09 ? 249 THR A CA  1 
ATOM   1518 C C   . THR A 1 249 ? 162.627 161.391 205.008 1.00 102.98 ? 249 THR A C   1 
ATOM   1519 O O   . THR A 1 249 ? 162.667 162.625 205.089 1.00 104.36 ? 249 THR A O   1 
ATOM   1520 C CB  . THR A 1 249 ? 164.139 159.957 206.408 1.00 97.70  ? 249 THR A CB  1 
ATOM   1521 O OG1 . THR A 1 249 ? 164.289 159.380 207.712 1.00 96.58  ? 249 THR A OG1 1 
ATOM   1522 C CG2 . THR A 1 249 ? 165.184 161.047 206.222 1.00 88.99  ? 249 THR A CG2 1 
ATOM   1523 N N   . THR A 1 250 ? 162.473 160.774 203.833 1.00 106.40 ? 250 THR A N   1 
ATOM   1524 C CA  . THR A 1 250 ? 162.398 161.508 202.546 1.00 104.87 ? 250 THR A CA  1 
ATOM   1525 C C   . THR A 1 250 ? 160.950 161.814 202.230 1.00 99.87  ? 250 THR A C   1 
ATOM   1526 O O   . THR A 1 250 ? 160.713 162.616 201.300 1.00 100.69 ? 250 THR A O   1 
ATOM   1527 C CB  . THR A 1 250 ? 163.054 160.686 201.441 1.00 107.04 ? 250 THR A CB  1 
ATOM   1528 O OG1 . THR A 1 250 ? 164.096 159.951 202.074 1.00 111.57 ? 250 THR A OG1 1 
ATOM   1529 C CG2 . THR A 1 250 ? 163.637 161.556 200.344 1.00 98.60  ? 250 THR A CG2 1 
ATOM   1530 N N   . TYR A 1 251 ? 160.010 161.208 202.959 1.00 97.18  ? 251 TYR A N   1 
ATOM   1531 C CA  . TYR A 1 251 ? 158.554 161.447 202.760 1.00 97.46  ? 251 TYR A CA  1 
ATOM   1532 C C   . TYR A 1 251 ? 158.182 161.171 201.303 1.00 101.66 ? 251 TYR A C   1 
ATOM   1533 O O   . TYR A 1 251 ? 157.314 161.889 200.761 1.00 100.96 ? 251 TYR A O   1 
ATOM   1534 C CB  . TYR A 1 251 ? 158.192 162.879 203.169 1.00 99.04  ? 251 TYR A CB  1 
ATOM   1535 C CG  . TYR A 1 251 ? 158.426 163.192 204.638 1.00 97.53  ? 251 TYR A CG  1 
ATOM   1536 C CD1 . TYR A 1 251 ? 157.439 162.953 205.584 1.00 96.51  ? 251 TYR A CD1 1 
ATOM   1537 C CD2 . TYR A 1 251 ? 159.625 163.739 205.072 1.00 97.70  ? 251 TYR A CD2 1 
ATOM   1538 C CE1 . TYR A 1 251 ? 157.641 163.240 206.923 1.00 93.33  ? 251 TYR A CE1 1 
ATOM   1539 C CE2 . TYR A 1 251 ? 159.840 164.031 206.408 1.00 95.49  ? 251 TYR A CE2 1 
ATOM   1540 C CZ  . TYR A 1 251 ? 158.845 163.780 207.335 1.00 89.47  ? 251 TYR A CZ  1 
ATOM   1541 O OH  . TYR A 1 251 ? 159.051 164.066 208.653 1.00 74.98  ? 251 TYR A OH  1 
ATOM   1542 N N   . GLN A 1 252 ? 158.808 160.168 200.678 1.00 102.71 ? 252 GLN A N   1 
ATOM   1543 C CA  . GLN A 1 252 ? 158.549 159.847 199.248 1.00 99.14  ? 252 GLN A CA  1 
ATOM   1544 C C   . GLN A 1 252 ? 159.046 158.426 198.938 1.00 101.67 ? 252 GLN A C   1 
ATOM   1545 O O   . GLN A 1 252 ? 159.411 157.718 199.899 1.00 100.79 ? 252 GLN A O   1 
ATOM   1546 C CB  . GLN A 1 252 ? 159.213 160.895 198.354 1.00 93.91  ? 252 GLN A CB  1 
ATOM   1547 C CG  . GLN A 1 252 ? 160.736 160.828 198.331 1.00 99.82  ? 252 GLN A CG  1 
ATOM   1548 C CD  . GLN A 1 252 ? 161.362 161.941 197.520 1.00 99.97  ? 252 GLN A CD  1 
ATOM   1549 O OE1 . GLN A 1 252 ? 160.681 162.853 197.038 1.00 99.50  ? 252 GLN A OE1 1 
ATOM   1550 N NE2 . GLN A 1 252 ? 162.675 161.876 197.364 1.00 102.43 ? 252 GLN A NE2 1 
ATOM   1551 N N   . MET A 1 253 ? 159.071 158.034 197.658 1.00 100.81 ? 253 MET A N   1 
ATOM   1552 C CA  . MET A 1 253 ? 159.493 156.670 197.241 1.00 99.70  ? 253 MET A CA  1 
ATOM   1553 C C   . MET A 1 253 ? 160.981 156.678 196.854 1.00 100.80 ? 253 MET A C   1 
ATOM   1554 O O   . MET A 1 253 ? 161.458 157.738 196.394 1.00 95.23  ? 253 MET A O   1 
ATOM   1555 C CB  . MET A 1 253 ? 158.647 156.174 196.065 1.00 97.75  ? 253 MET A CB  1 
ATOM   1556 C CG  . MET A 1 253 ? 157.159 156.165 196.349 1.00 93.28  ? 253 MET A CG  1 
ATOM   1557 S SD  . MET A 1 253 ? 156.724 155.119 197.753 1.00 91.40  ? 253 MET A SD  1 
ATOM   1558 C CE  . MET A 1 253 ? 155.141 155.843 198.202 1.00 83.86  ? 253 MET A CE  1 
ATOM   1559 N N   . ASP A 1 254 ? 161.680 155.553 197.029 1.00 101.25 ? 254 ASP A N   1 
ATOM   1560 C CA  . ASP A 1 254 ? 163.143 155.438 196.770 1.00 103.80 ? 254 ASP A CA  1 
ATOM   1561 C C   . ASP A 1 254 ? 163.437 154.037 196.221 1.00 100.26 ? 254 ASP A C   1 
ATOM   1562 O O   . ASP A 1 254 ? 162.759 153.080 196.646 1.00 99.27  ? 254 ASP A O   1 
ATOM   1563 C CB  . ASP A 1 254 ? 163.948 155.764 198.018 1.00 106.43 ? 254 ASP A CB  1 
ATOM   1564 C CG  . ASP A 1 254 ? 165.445 155.946 197.807 1.00 106.17 ? 254 ASP A CG  1 
ATOM   1565 O OD1 . ASP A 1 254 ? 166.100 154.977 197.368 1.00 104.41 ? 254 ASP A OD1 1 
ATOM   1566 O OD2 . ASP A 1 254 ? 165.943 157.057 198.081 1.00 101.27 ? 254 ASP A OD2 1 
ATOM   1567 N N   . VAL A 1 255 ? 164.418 153.924 195.321 1.00 99.43  ? 255 VAL A N   1 
ATOM   1568 C CA  . VAL A 1 255 ? 164.757 152.605 194.705 1.00 98.24  ? 255 VAL A CA  1 
ATOM   1569 C C   . VAL A 1 255 ? 165.039 151.593 195.827 1.00 98.25  ? 255 VAL A C   1 
ATOM   1570 O O   . VAL A 1 255 ? 165.807 151.936 196.752 1.00 94.13  ? 255 VAL A O   1 
ATOM   1571 C CB  . VAL A 1 255 ? 165.953 152.725 193.741 1.00 97.15  ? 255 VAL A CB  1 
ATOM   1572 C CG1 . VAL A 1 255 ? 166.348 151.373 193.158 1.00 94.31  ? 255 VAL A CG1 1 
ATOM   1573 C CG2 . VAL A 1 255 ? 165.680 153.730 192.630 1.00 92.85  ? 255 VAL A CG2 1 
ATOM   1574 N N   . ASN A 1 256 ? 164.447 150.399 195.740 1.00 94.64  ? 256 ASN A N   1 
ATOM   1575 C CA  . ASN A 1 256 ? 164.623 149.362 196.795 1.00 90.97  ? 256 ASN A CA  1 
ATOM   1576 C C   . ASN A 1 256 ? 165.683 148.357 196.338 1.00 90.28  ? 256 ASN A C   1 
ATOM   1577 O O   . ASN A 1 256 ? 165.450 147.668 195.321 1.00 85.86  ? 256 ASN A O   1 
ATOM   1578 C CB  . ASN A 1 256 ? 163.300 148.675 197.110 1.00 88.05  ? 256 ASN A CB  1 
ATOM   1579 C CG  . ASN A 1 256 ? 163.390 147.732 198.285 1.00 84.37  ? 256 ASN A CG  1 
ATOM   1580 O OD1 . ASN A 1 256 ? 164.431 147.650 198.946 1.00 84.68  ? 256 ASN A OD1 1 
ATOM   1581 N ND2 . ASN A 1 256 ? 162.306 147.028 198.571 1.00 83.29  ? 256 ASN A ND2 1 
ATOM   1582 N N   . PRO A 1 257 ? 166.831 148.237 197.040 1.00 89.90  ? 257 PRO A N   1 
ATOM   1583 C CA  . PRO A 1 257 ? 167.845 147.255 196.679 1.00 88.56  ? 257 PRO A CA  1 
ATOM   1584 C C   . PRO A 1 257 ? 167.321 145.826 196.744 1.00 89.64  ? 257 PRO A C   1 
ATOM   1585 O O   . PRO A 1 257 ? 167.532 145.062 195.780 1.00 90.70  ? 257 PRO A O   1 
ATOM   1586 C CB  . PRO A 1 257 ? 168.954 147.510 197.714 1.00 84.12  ? 257 PRO A CB  1 
ATOM   1587 C CG  . PRO A 1 257 ? 168.714 148.931 198.168 1.00 83.21  ? 257 PRO A CG  1 
ATOM   1588 C CD  . PRO A 1 257 ? 167.203 149.064 198.175 1.00 85.03  ? 257 PRO A CD  1 
ATOM   1589 N N   . GLU A 1 258 ? 166.681 145.444 197.854 1.00 87.64  ? 258 GLU A N   1 
ATOM   1590 C CA  . GLU A 1 258 ? 166.181 144.053 198.023 1.00 84.20  ? 258 GLU A CA  1 
ATOM   1591 C C   . GLU A 1 258 ? 165.001 143.869 197.058 1.00 84.36  ? 258 GLU A C   1 
ATOM   1592 O O   . GLU A 1 258 ? 164.592 142.708 196.846 1.00 79.93  ? 258 GLU A O   1 
ATOM   1593 C CB  . GLU A 1 258 ? 165.873 143.775 199.496 1.00 81.03  ? 258 GLU A CB  1 
ATOM   1594 C CG  . GLU A 1 258 ? 164.586 144.409 200.011 1.00 80.28  ? 258 GLU A CG  1 
ATOM   1595 C CD  . GLU A 1 258 ? 163.351 143.542 199.866 1.00 83.22  ? 258 GLU A CD  1 
ATOM   1596 O OE1 . GLU A 1 258 ? 163.394 142.356 200.257 1.00 78.83  ? 258 GLU A OE1 1 
ATOM   1597 O OE2 . GLU A 1 258 ? 162.327 144.073 199.399 1.00 87.01  ? 258 GLU A OE2 1 
ATOM   1598 N N   . GLY A 1 259 ? 164.477 144.963 196.496 1.00 84.46  ? 259 GLY A N   1 
ATOM   1599 C CA  . GLY A 1 259 ? 163.412 144.887 195.478 1.00 76.50  ? 259 GLY A CA  1 
ATOM   1600 C C   . GLY A 1 259 ? 163.900 144.107 194.275 1.00 79.13  ? 259 GLY A C   1 
ATOM   1601 O O   . GLY A 1 259 ? 165.011 144.421 193.799 1.00 79.44  ? 259 GLY A O   1 
ATOM   1602 N N   . LYS A 1 260 ? 163.118 143.136 193.793 1.00 76.85  ? 260 LYS A N   1 
ATOM   1603 C CA  . LYS A 1 260 ? 163.513 142.276 192.645 1.00 65.58  ? 260 LYS A CA  1 
ATOM   1604 C C   . LYS A 1 260 ? 162.480 142.402 191.522 1.00 62.96  ? 260 LYS A C   1 
ATOM   1605 O O   . LYS A 1 260 ? 161.280 142.533 191.848 1.00 63.25  ? 260 LYS A O   1 
ATOM   1606 C CB  . LYS A 1 260 ? 163.612 140.808 193.069 1.00 64.14  ? 260 LYS A CB  1 
ATOM   1607 C CG  . LYS A 1 260 ? 164.906 140.423 193.762 1.00 67.55  ? 260 LYS A CG  1 
ATOM   1608 C CD  . LYS A 1 260 ? 165.089 138.918 193.917 1.00 63.28  ? 260 LYS A CD  1 
ATOM   1609 C CE  . LYS A 1 260 ? 163.972 138.262 194.666 1.00 62.06  ? 260 LYS A CE  1 
ATOM   1610 N NZ  . LYS A 1 260 ? 163.831 138.801 196.021 1.00 64.06  ? 260 LYS A NZ  1 
ATOM   1611 N N   . TYR A 1 261 ? 162.913 142.358 190.258 1.00 66.90  ? 261 TYR A N   1 
ATOM   1612 C CA  . TYR A 1 261 ? 161.981 142.390 189.108 1.00 62.41  ? 261 TYR A CA  1 
ATOM   1613 C C   . TYR A 1 261 ? 161.198 141.097 189.080 1.00 61.98  ? 261 TYR A C   1 
ATOM   1614 O O   . TYR A 1 261 ? 161.599 140.114 189.738 1.00 65.08  ? 261 TYR A O   1 
ATOM   1615 C CB  . TYR A 1 261 ? 162.791 142.535 187.819 1.00 62.30  ? 261 TYR A CB  1 
ATOM   1616 C CG  . TYR A 1 261 ? 163.671 143.774 187.759 1.00 68.42  ? 261 TYR A CG  1 
ATOM   1617 C CD1 . TYR A 1 261 ? 163.201 145.007 188.188 1.00 69.73  ? 261 TYR A CD1 1 
ATOM   1618 C CD2 . TYR A 1 261 ? 164.981 143.702 187.303 1.00 80.04  ? 261 TYR A CD2 1 
ATOM   1619 C CE1 . TYR A 1 261 ? 163.997 146.138 188.140 1.00 77.60  ? 261 TYR A CE1 1 
ATOM   1620 C CE2 . TYR A 1 261 ? 165.789 144.825 187.256 1.00 84.33  ? 261 TYR A CE2 1 
ATOM   1621 C CZ  . TYR A 1 261 ? 165.296 146.047 187.676 1.00 85.43  ? 261 TYR A CZ  1 
ATOM   1622 O OH  . TYR A 1 261 ? 166.079 147.163 187.637 1.00 95.62  ? 261 TYR A OH  1 
ATOM   1623 N N   . SER A 1 262 ? 160.110 141.084 188.325 1.00 57.83  ? 262 SER A N   1 
ATOM   1624 C CA  . SER A 1 262 ? 159.255 139.913 188.181 1.00 52.90  ? 262 SER A CA  1 
ATOM   1625 C C   . SER A 1 262 ? 159.559 139.226 186.855 1.00 56.11  ? 262 SER A C   1 
ATOM   1626 O O   . SER A 1 262 ? 159.428 139.837 185.790 1.00 60.51  ? 262 SER A O   1 
ATOM   1627 C CB  . SER A 1 262 ? 157.780 140.303 188.258 1.00 47.60  ? 262 SER A CB  1 
ATOM   1628 O OG  . SER A 1 262 ? 156.956 139.154 188.264 1.00 37.54  ? 262 SER A OG  1 
ATOM   1629 N N   . PHE A 1 263 ? 159.959 137.962 186.926 1.00 48.02  ? 263 PHE A N   1 
ATOM   1630 C CA  . PHE A 1 263 ? 160.253 137.146 185.751 1.00 40.62  ? 263 PHE A CA  1 
ATOM   1631 C C   . PHE A 1 263 ? 159.189 136.055 185.680 1.00 36.66  ? 263 PHE A C   1 
ATOM   1632 O O   . PHE A 1 263 ? 159.365 134.959 186.212 1.00 47.54  ? 263 PHE A O   1 
ATOM   1633 C CB  . PHE A 1 263 ? 161.659 136.557 185.829 1.00 47.19  ? 263 PHE A CB  1 
ATOM   1634 C CG  . PHE A 1 263 ? 162.031 135.713 184.644 1.00 50.49  ? 263 PHE A CG  1 
ATOM   1635 C CD1 . PHE A 1 263 ? 161.584 136.040 183.375 1.00 51.09  ? 263 PHE A CD1 1 
ATOM   1636 C CD2 . PHE A 1 263 ? 162.827 134.592 184.800 1.00 43.60  ? 263 PHE A CD2 1 
ATOM   1637 C CE1 . PHE A 1 263 ? 161.925 135.264 182.286 1.00 48.21  ? 263 PHE A CE1 1 
ATOM   1638 C CE2 . PHE A 1 263 ? 163.171 133.813 183.714 1.00 41.13  ? 263 PHE A CE2 1 
ATOM   1639 C CZ  . PHE A 1 263 ? 162.720 134.150 182.455 1.00 45.73  ? 263 PHE A CZ  1 
ATOM   1640 N N   . GLY A 1 264 ? 158.080 136.362 185.012 1.00 30.64  ? 264 GLY A N   1 
ATOM   1641 C CA  . GLY A 1 264 ? 156.983 135.421 184.925 1.00 30.33  ? 264 GLY A CA  1 
ATOM   1642 C C   . GLY A 1 264 ? 156.374 135.123 186.278 1.00 25.03  ? 264 GLY A C   1 
ATOM   1643 O O   . GLY A 1 264 ? 155.703 135.975 186.867 1.00 33.34  ? 264 GLY A O   1 
ATOM   1644 N N   . ALA A 1 265 ? 156.604 133.911 186.784 1.00 22.66  ? 265 ALA A N   1 
ATOM   1645 C CA  . ALA A 1 265 ? 156.082 133.487 188.076 1.00 28.70  ? 265 ALA A CA  1 
ATOM   1646 C C   . ALA A 1 265 ? 157.164 133.424 189.149 1.00 35.66  ? 265 ALA A C   1 
ATOM   1647 O O   . ALA A 1 265 ? 156.990 132.737 190.159 1.00 36.01  ? 265 ALA A O   1 
ATOM   1648 C CB  . ALA A 1 265 ? 155.384 132.133 187.948 1.00 33.41  ? 265 ALA A CB  1 
ATOM   1649 N N   . THR A 1 266 ? 158.278 134.129 188.923 1.00 41.12  ? 266 THR A N   1 
ATOM   1650 C CA  . THR A 1 266 ? 159.380 134.154 189.912 1.00 38.87  ? 266 THR A CA  1 
ATOM   1651 C C   . THR A 1 266 ? 159.957 135.552 189.979 1.00 42.57  ? 266 THR A C   1 
ATOM   1652 O O   . THR A 1 266 ? 159.802 136.302 188.992 1.00 42.30  ? 266 THR A O   1 
ATOM   1653 C CB  . THR A 1 266 ? 160.443 133.121 189.540 1.00 43.90  ? 266 THR A CB  1 
ATOM   1654 O OG1 . THR A 1 266 ? 161.375 133.143 190.615 1.00 56.73  ? 266 THR A OG1 1 
ATOM   1655 C CG2 . THR A 1 266 ? 161.160 133.448 188.243 1.00 45.32  ? 266 THR A CG2 1 
ATOM   1656 N N   . CYS A 1 267 ? 160.577 135.938 191.098 1.00 50.94  ? 267 CYS A N   1 
ATOM   1657 C CA  . CYS A 1 267 ? 161.168 137.293 191.262 1.00 49.82  ? 267 CYS A CA  1 
ATOM   1658 C C   . CYS A 1 267 ? 162.682 137.202 191.047 1.00 52.30  ? 267 CYS A C   1 
ATOM   1659 O O   . CYS A 1 267 ? 163.297 136.295 191.640 1.00 56.39  ? 267 CYS A O   1 
ATOM   1660 C CB  . CYS A 1 267 ? 160.834 137.882 192.624 1.00 51.34  ? 267 CYS A CB  1 
ATOM   1661 S SG  . CYS A 1 267 ? 159.085 137.693 193.045 1.00 62.95  ? 267 CYS A SG  1 
ATOM   1662 N N   . VAL A 1 268 ? 163.252 138.087 190.228 1.00 52.47  ? 268 VAL A N   1 
ATOM   1663 C CA  . VAL A 1 268 ? 164.710 138.050 189.902 1.00 63.84  ? 268 VAL A CA  1 
ATOM   1664 C C   . VAL A 1 268 ? 165.324 139.438 190.149 1.00 66.99  ? 268 VAL A C   1 
ATOM   1665 O O   . VAL A 1 268 ? 164.699 140.439 189.742 1.00 67.02  ? 268 VAL A O   1 
ATOM   1666 C CB  . VAL A 1 268 ? 164.921 137.600 188.444 1.00 68.45  ? 268 VAL A CB  1 
ATOM   1667 C CG1 . VAL A 1 268 ? 164.640 136.113 188.260 1.00 61.09  ? 268 VAL A CG1 1 
ATOM   1668 C CG2 . VAL A 1 268 ? 164.097 138.428 187.466 1.00 60.83  ? 268 VAL A CG2 1 
ATOM   1669 N N   . LYS A 1 269 ? 166.497 139.502 190.790 1.00 67.86  ? 269 LYS A N   1 
ATOM   1670 C CA  . LYS A 1 269 ? 167.136 140.803 190.961 1.00 72.04  ? 269 LYS A CA  1 
ATOM   1671 C C   . LYS A 1 269 ? 167.368 141.474 189.614 1.00 72.83  ? 269 LYS A C   1 
ATOM   1672 O O   . LYS A 1 269 ? 167.166 142.686 189.470 1.00 76.59  ? 269 LYS A O   1 
ATOM   1673 C CB  . LYS A 1 269 ? 168.453 140.649 191.721 1.00 74.72  ? 269 LYS A CB  1 
ATOM   1674 C CG  . LYS A 1 269 ? 168.906 141.910 192.439 1.00 77.48  ? 269 LYS A CG  1 
ATOM   1675 C CD  . LYS A 1 269 ? 168.310 142.000 193.834 1.00 73.45  ? 269 LYS A CD  1 
ATOM   1676 C CE  . LYS A 1 269 ? 168.650 140.771 194.661 1.00 71.14  ? 269 LYS A CE  1 
ATOM   1677 N NZ  . LYS A 1 269 ? 168.642 141.065 196.121 1.00 78.00  ? 269 LYS A NZ  1 
ATOM   1678 N N   . LYS A 1 270 ? 167.803 140.705 188.620 1.00 75.32  ? 270 LYS A N   1 
ATOM   1679 C CA  . LYS A 1 270 ? 167.877 141.168 187.244 1.00 81.95  ? 270 LYS A CA  1 
ATOM   1680 C C   . LYS A 1 270 ? 167.444 140.031 186.331 1.00 82.41  ? 270 LYS A C   1 
ATOM   1681 O O   . LYS A 1 270 ? 167.661 138.854 186.634 1.00 82.79  ? 270 LYS A O   1 
ATOM   1682 C CB  . LYS A 1 270 ? 169.288 141.660 186.880 1.00 88.02  ? 270 LYS A CB  1 
ATOM   1683 C CG  . LYS A 1 270 ? 170.254 140.572 186.439 1.00 91.30  ? 270 LYS A CG  1 
ATOM   1684 C CD  . LYS A 1 270 ? 171.558 141.169 185.936 1.00 88.82  ? 270 LYS A CD  1 
ATOM   1685 C CE  . LYS A 1 270 ? 172.745 140.295 186.305 1.00 92.16  ? 270 LYS A CE  1 
ATOM   1686 N NZ  . LYS A 1 270 ? 173.124 140.451 187.736 1.00 90.54  ? 270 LYS A NZ  1 
ATOM   1687 N N   . CYS A 1 271 ? 166.814 140.389 185.224 1.00 83.27  ? 271 CYS A N   1 
ATOM   1688 C CA  . CYS A 1 271 ? 166.299 139.362 184.325 1.00 90.82  ? 271 CYS A CA  1 
ATOM   1689 C C   . CYS A 1 271 ? 167.350 139.004 183.282 1.00 91.53  ? 271 CYS A C   1 
ATOM   1690 O O   . CYS A 1 271 ? 167.805 139.886 182.543 1.00 89.75  ? 271 CYS A O   1 
ATOM   1691 C CB  . CYS A 1 271 ? 165.022 139.832 183.645 1.00 93.51  ? 271 CYS A CB  1 
ATOM   1692 S SG  . CYS A 1 271 ? 163.921 140.764 184.739 1.00 75.64  ? 271 CYS A SG  1 
ATOM   1693 N N   . PRO A 1 272 ? 167.752 137.743 183.193 1.00 91.60  ? 272 PRO A N   1 
ATOM   1694 C CA  . PRO A 1 272 ? 168.818 137.347 182.269 1.00 95.75  ? 272 PRO A CA  1 
ATOM   1695 C C   . PRO A 1 272 ? 168.318 137.333 180.828 1.00 99.52  ? 272 PRO A C   1 
ATOM   1696 O O   . PRO A 1 272 ? 167.149 137.588 180.544 1.00 93.59  ? 272 PRO A O   1 
ATOM   1697 C CB  . PRO A 1 272 ? 169.199 135.937 182.744 1.00 87.83  ? 272 PRO A CB  1 
ATOM   1698 C CG  . PRO A 1 272 ? 168.455 135.720 184.044 1.00 89.75  ? 272 PRO A CG  1 
ATOM   1699 C CD  . PRO A 1 272 ? 167.260 136.605 183.983 1.00 85.86  ? 272 PRO A CD  1 
ATOM   1700 N N   . ARG A 1 273 ? 169.240 137.027 179.920 1.00 103.05 ? 273 ARG A N   1 
ATOM   1701 C CA  . ARG A 1 273 ? 168.978 136.958 178.476 1.00 103.02 ? 273 ARG A CA  1 
ATOM   1702 C C   . ARG A 1 273 ? 168.468 138.333 178.027 1.00 104.34 ? 273 ARG A C   1 
ATOM   1703 O O   . ARG A 1 273 ? 168.850 139.363 178.597 1.00 99.40  ? 273 ARG A O   1 
ATOM   1704 C CB  . ARG A 1 273 ? 168.048 135.788 178.177 1.00 98.96  ? 273 ARG A CB  1 
ATOM   1705 C CG  . ARG A 1 273 ? 168.062 135.312 176.728 1.00 101.25 ? 273 ARG A CG  1 
ATOM   1706 C CD  . ARG A 1 273 ? 167.243 134.043 176.557 1.00 104.57 ? 273 ARG A CD  1 
ATOM   1707 N NE  . ARG A 1 273 ? 165.817 134.287 176.738 1.00 107.68 ? 273 ARG A NE  1 
ATOM   1708 C CZ  . ARG A 1 273 ? 165.015 134.776 175.803 1.00 102.40 ? 273 ARG A CZ  1 
ATOM   1709 N NH1 . ARG A 1 273 ? 165.465 135.083 174.597 1.00 101.80 ? 273 ARG A NH1 1 
ATOM   1710 N NH2 . ARG A 1 273 ? 163.729 134.962 176.084 1.00 99.80  ? 273 ARG A NH2 1 
ATOM   1711 N N   . ASN A 1 274 ? 167.610 138.374 177.008 1.00 104.19 ? 274 ASN A N   1 
ATOM   1712 C CA  . ASN A 1 274 ? 167.082 139.632 176.483 1.00 102.69 ? 274 ASN A CA  1 
ATOM   1713 C C   . ASN A 1 274 ? 165.668 139.828 177.023 1.00 97.92  ? 274 ASN A C   1 
ATOM   1714 O O   . ASN A 1 274 ? 164.669 139.511 176.376 1.00 96.67  ? 274 ASN A O   1 
ATOM   1715 C CB  . ASN A 1 274 ? 167.115 139.634 174.958 1.00 101.54 ? 274 ASN A CB  1 
ATOM   1716 C CG  . ASN A 1 274 ? 168.521 139.764 174.406 1.00 105.97 ? 274 ASN A CG  1 
ATOM   1717 O OD1 . ASN A 1 274 ? 169.426 140.242 175.090 1.00 108.57 ? 274 ASN A OD1 1 
ATOM   1718 N ND2 . ASN A 1 274 ? 168.711 139.340 173.163 1.00 102.27 ? 274 ASN A ND2 1 
ATOM   1719 N N   . TYR A 1 275 ? 165.580 140.375 178.240 1.00 93.70  ? 275 TYR A N   1 
ATOM   1720 C CA  . TYR A 1 275 ? 164.247 140.672 178.836 1.00 88.64  ? 275 TYR A CA  1 
ATOM   1721 C C   . TYR A 1 275 ? 164.201 142.156 179.207 1.00 87.94  ? 275 TYR A C   1 
ATOM   1722 O O   . TYR A 1 275 ? 165.257 142.719 179.569 1.00 91.39  ? 275 TYR A O   1 
ATOM   1723 C CB  . TYR A 1 275 ? 163.967 139.754 180.030 1.00 85.99  ? 275 TYR A CB  1 
ATOM   1724 C CG  . TYR A 1 275 ? 163.433 138.380 179.650 1.00 83.69  ? 275 TYR A CG  1 
ATOM   1725 C CD1 . TYR A 1 275 ? 164.289 137.304 179.453 1.00 87.43  ? 275 TYR A CD1 1 
ATOM   1726 C CD2 . TYR A 1 275 ? 162.072 138.165 179.479 1.00 80.92  ? 275 TYR A CD2 1 
ATOM   1727 C CE1 . TYR A 1 275 ? 163.806 136.054 179.107 1.00 85.65  ? 275 TYR A CE1 1 
ATOM   1728 C CE2 . TYR A 1 275 ? 161.576 136.920 179.130 1.00 78.96  ? 275 TYR A CE2 1 
ATOM   1729 C CZ  . TYR A 1 275 ? 162.446 135.862 178.943 1.00 81.00  ? 275 TYR A CZ  1 
ATOM   1730 O OH  . TYR A 1 275 ? 161.962 134.632 178.601 1.00 71.70  ? 275 TYR A OH  1 
ATOM   1731 N N   . VAL A 1 276 ? 163.019 142.775 179.122 1.00 85.31  ? 276 VAL A N   1 
ATOM   1732 C CA  . VAL A 1 276 ? 162.900 144.242 179.384 1.00 82.10  ? 276 VAL A CA  1 
ATOM   1733 C C   . VAL A 1 276 ? 161.922 144.480 180.544 1.00 76.55  ? 276 VAL A C   1 
ATOM   1734 O O   . VAL A 1 276 ? 160.741 144.100 180.406 1.00 78.66  ? 276 VAL A O   1 
ATOM   1735 C CB  . VAL A 1 276 ? 162.437 144.966 178.107 1.00 84.51  ? 276 VAL A CB  1 
ATOM   1736 C CG1 . VAL A 1 276 ? 163.614 145.406 177.249 1.00 88.77  ? 276 VAL A CG1 1 
ATOM   1737 C CG2 . VAL A 1 276 ? 161.472 144.114 177.294 1.00 84.26  ? 276 VAL A CG2 1 
ATOM   1738 N N   . VAL A 1 277 ? 162.395 145.109 181.623 1.00 71.92  ? 277 VAL A N   1 
ATOM   1739 C CA  . VAL A 1 277 ? 161.528 145.362 182.814 1.00 69.96  ? 277 VAL A CA  1 
ATOM   1740 C C   . VAL A 1 277 ? 160.422 146.352 182.421 1.00 73.57  ? 277 VAL A C   1 
ATOM   1741 O O   . VAL A 1 277 ? 160.755 147.419 181.869 1.00 81.71  ? 277 VAL A O   1 
ATOM   1742 C CB  . VAL A 1 277 ? 162.347 145.887 184.007 1.00 69.87  ? 277 VAL A CB  1 
ATOM   1743 C CG1 . VAL A 1 277 ? 161.475 146.112 185.235 1.00 68.89  ? 277 VAL A CG1 1 
ATOM   1744 C CG2 . VAL A 1 277 ? 163.508 144.960 184.338 1.00 74.61  ? 277 VAL A CG2 1 
ATOM   1745 N N   . THR A 1 278 ? 159.163 146.012 182.701 1.00 73.29  ? 278 THR A N   1 
ATOM   1746 C CA  . THR A 1 278 ? 158.037 146.920 182.399 1.00 79.57  ? 278 THR A CA  1 
ATOM   1747 C C   . THR A 1 278 ? 157.821 147.835 183.583 1.00 84.69  ? 278 THR A C   1 
ATOM   1748 O O   . THR A 1 278 ? 158.612 147.752 184.547 1.00 84.65  ? 278 THR A O   1 
ATOM   1749 C CB  . THR A 1 278 ? 156.786 146.104 182.086 1.00 79.09  ? 278 THR A CB  1 
ATOM   1750 O OG1 . THR A 1 278 ? 156.526 145.370 183.279 1.00 79.17  ? 278 THR A OG1 1 
ATOM   1751 C CG2 . THR A 1 278 ? 156.989 145.156 180.920 1.00 77.42  ? 278 THR A CG2 1 
ATOM   1752 N N   . ASP A 1 279 ? 156.784 148.674 183.531 1.00 86.54  ? 279 ASP A N   1 
ATOM   1753 C CA  . ASP A 1 279 ? 156.574 149.667 184.622 1.00 89.59  ? 279 ASP A CA  1 
ATOM   1754 C C   . ASP A 1 279 ? 156.145 148.957 185.910 1.00 93.81  ? 279 ASP A C   1 
ATOM   1755 O O   . ASP A 1 279 ? 156.571 149.407 186.995 1.00 99.50  ? 279 ASP A O   1 
ATOM   1756 C CB  . ASP A 1 279 ? 155.590 150.742 184.190 1.00 91.69  ? 279 ASP A CB  1 
ATOM   1757 C CG  . ASP A 1 279 ? 155.984 151.514 182.940 1.00 96.17  ? 279 ASP A CG  1 
ATOM   1758 O OD1 . ASP A 1 279 ? 157.062 151.216 182.384 1.00 95.48  ? 279 ASP A OD1 1 
ATOM   1759 O OD2 . ASP A 1 279 ? 155.211 152.406 182.533 1.00 99.05  ? 279 ASP A OD2 1 
ATOM   1760 N N   . HIS A 1 280 ? 155.346 147.893 185.804 1.00 84.73  ? 280 HIS A N   1 
ATOM   1761 C CA  . HIS A 1 280 ? 154.826 147.221 186.988 1.00 85.76  ? 280 HIS A CA  1 
ATOM   1762 C C   . HIS A 1 280 ? 155.805 146.212 187.583 1.00 84.06  ? 280 HIS A C   1 
ATOM   1763 O O   . HIS A 1 280 ? 155.383 145.345 188.359 1.00 79.97  ? 280 HIS A O   1 
ATOM   1764 C CB  . HIS A 1 280 ? 153.487 146.530 186.687 1.00 84.14  ? 280 HIS A CB  1 
ATOM   1765 C CG  . HIS A 1 280 ? 153.406 145.881 185.336 1.00 87.93  ? 280 HIS A CG  1 
ATOM   1766 N ND1 . HIS A 1 280 ? 153.675 146.548 184.159 1.00 88.81  ? 280 HIS A ND1 1 
ATOM   1767 C CD2 . HIS A 1 280 ? 153.076 144.617 184.981 1.00 84.89  ? 280 HIS A CD2 1 
ATOM   1768 C CE1 . HIS A 1 280 ? 153.516 145.724 183.140 1.00 84.25  ? 280 HIS A CE1 1 
ATOM   1769 N NE2 . HIS A 1 280 ? 153.153 144.545 183.611 1.00 76.07  ? 280 HIS A NE2 1 
ATOM   1770 N N   . GLY A 1 281 ? 157.090 146.298 187.242 1.00 80.09  ? 281 GLY A N   1 
ATOM   1771 C CA  . GLY A 1 281 ? 158.107 145.463 187.837 1.00 73.80  ? 281 GLY A CA  1 
ATOM   1772 C C   . GLY A 1 281 ? 158.408 144.180 187.093 1.00 70.94  ? 281 GLY A C   1 
ATOM   1773 O O   . GLY A 1 281 ? 159.456 143.572 187.337 1.00 66.03  ? 281 GLY A O   1 
ATOM   1774 N N   . SER A 1 282 ? 157.528 143.750 186.196 1.00 75.97  ? 282 SER A N   1 
ATOM   1775 C CA  . SER A 1 282 ? 157.740 142.528 185.437 1.00 63.48  ? 282 SER A CA  1 
ATOM   1776 C C   . SER A 1 282 ? 158.586 142.808 184.203 1.00 65.31  ? 282 SER A C   1 
ATOM   1777 O O   . SER A 1 282 ? 158.513 143.885 183.607 1.00 72.93  ? 282 SER A O   1 
ATOM   1778 C CB  . SER A 1 282 ? 156.404 141.907 185.025 1.00 61.05  ? 282 SER A CB  1 
ATOM   1779 O OG  . SER A 1 282 ? 155.659 142.795 184.211 1.00 68.81  ? 282 SER A OG  1 
ATOM   1780 N N   . CYS A 1 283 ? 159.431 141.834 183.853 1.00 65.30  ? 283 CYS A N   1 
ATOM   1781 C CA  . CYS A 1 283 ? 160.284 141.982 182.646 1.00 72.32  ? 283 CYS A CA  1 
ATOM   1782 C C   . CYS A 1 283 ? 159.802 141.011 181.563 1.00 69.55  ? 283 CYS A C   1 
ATOM   1783 O O   . CYS A 1 283 ? 160.235 139.841 181.580 1.00 70.90  ? 283 CYS A O   1 
ATOM   1784 C CB  . CYS A 1 283 ? 161.755 141.737 182.956 1.00 70.17  ? 283 CYS A CB  1 
ATOM   1785 S SG  . CYS A 1 283 ? 162.065 140.333 184.054 1.00 58.06  ? 283 CYS A SG  1 
ATOM   1786 N N   . VAL A 1 284 ? 158.943 141.492 180.664 1.00 66.45  ? 284 VAL A N   1 
ATOM   1787 C CA  . VAL A 1 284 ? 158.394 140.624 179.583 1.00 76.91  ? 284 VAL A CA  1 
ATOM   1788 C C   . VAL A 1 284 ? 159.466 140.451 178.497 1.00 87.30  ? 284 VAL A C   1 
ATOM   1789 O O   . VAL A 1 284 ? 160.524 141.110 178.598 1.00 86.75  ? 284 VAL A O   1 
ATOM   1790 C CB  . VAL A 1 284 ? 157.106 141.245 179.017 1.00 80.46  ? 284 VAL A CB  1 
ATOM   1791 C CG1 . VAL A 1 284 ? 155.967 141.192 180.028 1.00 70.48  ? 284 VAL A CG1 1 
ATOM   1792 C CG2 . VAL A 1 284 ? 157.337 142.675 178.550 1.00 79.78  ? 284 VAL A CG2 1 
ATOM   1793 N N   . ARG A 1 285 ? 159.200 139.599 177.504 1.00 86.75  ? 285 ARG A N   1 
ATOM   1794 C CA  . ARG A 1 285 ? 160.186 139.342 176.459 1.00 85.56  ? 285 ARG A CA  1 
ATOM   1795 C C   . ARG A 1 285 ? 160.496 140.604 175.660 1.00 85.78  ? 285 ARG A C   1 
ATOM   1796 O O   . ARG A 1 285 ? 161.662 140.888 175.364 1.00 84.38  ? 285 ARG A O   1 
ATOM   1797 C CB  . ARG A 1 285 ? 159.687 138.229 175.537 1.00 85.95  ? 285 ARG A CB  1 
ATOM   1798 C CG  . ARG A 1 285 ? 160.522 138.031 174.282 1.00 92.76  ? 285 ARG A CG  1 
ATOM   1799 C CD  . ARG A 1 285 ? 161.910 137.510 174.616 1.00 95.06  ? 285 ARG A CD  1 
ATOM   1800 N NE  . ARG A 1 285 ? 162.734 137.351 173.423 1.00 93.18  ? 285 ARG A NE  1 
ATOM   1801 C CZ  . ARG A 1 285 ? 163.477 138.312 172.892 1.00 97.05  ? 285 ARG A CZ  1 
ATOM   1802 N NH1 . ARG A 1 285 ? 163.527 139.522 173.425 1.00 98.27  ? 285 ARG A NH1 1 
ATOM   1803 N NH2 . ARG A 1 285 ? 164.188 138.053 171.799 1.00 98.28  ? 285 ARG A NH2 1 
ATOM   1804 N N   . ALA A 1 286 ? 159.469 141.374 175.306 1.00 84.46  ? 286 ALA A N   1 
ATOM   1805 C CA  . ALA A 1 286 ? 159.654 142.599 174.541 1.00 87.98  ? 286 ALA A CA  1 
ATOM   1806 C C   . ALA A 1 286 ? 158.696 143.667 175.046 1.00 90.95  ? 286 ALA A C   1 
ATOM   1807 O O   . ALA A 1 286 ? 157.640 143.361 175.606 1.00 84.67  ? 286 ALA A O   1 
ATOM   1808 C CB  . ALA A 1 286 ? 159.437 142.366 173.040 1.00 86.81  ? 286 ALA A CB  1 
ATOM   1809 N N   . CYS A 1 287 ? 159.089 144.922 174.809 1.00 94.35  ? 287 CYS A N   1 
ATOM   1810 C CA  . CYS A 1 287 ? 158.253 146.063 175.250 1.00 91.46  ? 287 CYS A CA  1 
ATOM   1811 C C   . CYS A 1 287 ? 156.956 146.093 174.443 1.00 90.63  ? 287 CYS A C   1 
ATOM   1812 O O   . CYS A 1 287 ? 156.964 145.637 173.279 1.00 94.38  ? 287 CYS A O   1 
ATOM   1813 C CB  . CYS A 1 287 ? 159.004 147.379 175.100 1.00 94.95  ? 287 CYS A CB  1 
ATOM   1814 S SG  . CYS A 1 287 ? 160.279 147.585 176.367 1.00 104.69 ? 287 CYS A SG  1 
ATOM   1815 N N   . GLY A 1 288 ? 155.899 146.627 175.042 1.00 90.13  ? 288 GLY A N   1 
ATOM   1816 C CA  . GLY A 1 288 ? 154.601 146.691 174.408 1.00 95.96  ? 288 GLY A CA  1 
ATOM   1817 C C   . GLY A 1 288 ? 154.559 147.710 173.283 1.00 102.83 ? 288 GLY A C   1 
ATOM   1818 O O   . GLY A 1 288 ? 155.540 148.376 172.950 1.00 106.15 ? 288 GLY A O   1 
ATOM   1819 N N   . ALA A 1 289 ? 153.375 147.817 172.675 1.00 104.24 ? 289 ALA A N   1 
ATOM   1820 C CA  . ALA A 1 289 ? 153.191 148.757 171.573 1.00 101.88 ? 289 ALA A CA  1 
ATOM   1821 C C   . ALA A 1 289 ? 153.346 150.198 172.042 1.00 102.74 ? 289 ALA A C   1 
ATOM   1822 O O   . ALA A 1 289 ? 153.903 151.036 171.323 1.00 100.78 ? 289 ALA A O   1 
ATOM   1823 C CB  . ALA A 1 289 ? 151.822 148.546 170.927 1.00 90.49  ? 289 ALA A CB  1 
ATOM   1824 N N   . ASP A 1 290 ? 152.861 150.506 173.241 1.00 102.59 ? 290 ASP A N   1 
ATOM   1825 C CA  . ASP A 1 290 ? 152.924 151.853 173.789 1.00 102.74 ? 290 ASP A CA  1 
ATOM   1826 C C   . ASP A 1 290 ? 154.233 152.142 174.513 1.00 106.06 ? 290 ASP A C   1 
ATOM   1827 O O   . ASP A 1 290 ? 154.415 153.259 175.009 1.00 106.92 ? 290 ASP A O   1 
ATOM   1828 C CB  . ASP A 1 290 ? 151.746 152.088 174.741 1.00 102.49 ? 290 ASP A CB  1 
ATOM   1829 C CG  . ASP A 1 290 ? 151.388 153.555 174.876 1.00 101.05 ? 290 ASP A CG  1 
ATOM   1830 O OD1 . ASP A 1 290 ? 151.361 154.259 173.845 1.00 101.01 ? 290 ASP A OD1 1 
ATOM   1831 O OD2 . ASP A 1 290 ? 151.133 154.004 176.013 1.00 101.38 ? 290 ASP A OD2 1 
ATOM   1832 N N   . SER A 1 291 ? 155.143 151.175 174.587 1.00 103.86 ? 291 SER A N   1 
ATOM   1833 C CA  . SER A 1 291 ? 156.405 151.338 175.290 1.00 97.97  ? 291 SER A CA  1 
ATOM   1834 C C   . SER A 1 291 ? 157.571 151.112 174.336 1.00 97.71  ? 291 SER A C   1 
ATOM   1835 O O   . SER A 1 291 ? 157.427 150.497 173.276 1.00 99.04  ? 291 SER A O   1 
ATOM   1836 C CB  . SER A 1 291 ? 156.507 150.373 176.478 1.00 97.82  ? 291 SER A CB  1 
ATOM   1837 O OG  . SER A 1 291 ? 155.467 150.603 177.413 1.00 98.92  ? 291 SER A OG  1 
ATOM   1838 N N   . TYR A 1 292 ? 158.749 151.597 174.738 1.00 95.68  ? 292 TYR A N   1 
ATOM   1839 C CA  . TYR A 1 292 ? 159.969 151.395 173.909 1.00 96.75  ? 292 TYR A CA  1 
ATOM   1840 C C   . TYR A 1 292 ? 161.080 150.850 174.802 1.00 97.32  ? 292 TYR A C   1 
ATOM   1841 O O   . TYR A 1 292 ? 160.989 150.987 176.041 1.00 95.71  ? 292 TYR A O   1 
ATOM   1842 C CB  . TYR A 1 292 ? 160.386 152.700 173.226 1.00 99.69  ? 292 TYR A CB  1 
ATOM   1843 C CG  . TYR A 1 292 ? 160.850 153.804 174.167 1.00 103.15 ? 292 TYR A CG  1 
ATOM   1844 C CD1 . TYR A 1 292 ? 159.957 154.741 174.670 1.00 103.55 ? 292 TYR A CD1 1 
ATOM   1845 C CD2 . TYR A 1 292 ? 162.183 153.912 174.545 1.00 96.14  ? 292 TYR A CD2 1 
ATOM   1846 C CE1 . TYR A 1 292 ? 160.373 155.748 175.524 1.00 97.72  ? 292 TYR A CE1 1 
ATOM   1847 C CE2 . TYR A 1 292 ? 162.611 154.913 175.400 1.00 95.95  ? 292 TYR A CE2 1 
ATOM   1848 C CZ  . TYR A 1 292 ? 161.704 155.834 175.891 1.00 97.67  ? 292 TYR A CZ  1 
ATOM   1849 O OH  . TYR A 1 292 ? 162.119 156.824 176.733 1.00 98.50  ? 292 TYR A OH  1 
ATOM   1850 N N   . GLU A 1 293 ? 162.108 150.253 174.193 1.00 98.21  ? 293 GLU A N   1 
ATOM   1851 C CA  . GLU A 1 293 ? 163.224 149.662 174.975 1.00 100.24 ? 293 GLU A CA  1 
ATOM   1852 C C   . GLU A 1 293 ? 164.279 150.739 175.259 1.00 106.84 ? 293 GLU A C   1 
ATOM   1853 O O   . GLU A 1 293 ? 164.749 151.374 174.290 1.00 109.11 ? 293 GLU A O   1 
ATOM   1854 C CB  . GLU A 1 293 ? 163.882 148.502 174.227 1.00 98.36  ? 293 GLU A CB  1 
ATOM   1855 C CG  . GLU A 1 293 ? 163.021 147.245 174.142 1.00 100.69 ? 293 GLU A CG  1 
ATOM   1856 C CD  . GLU A 1 293 ? 161.918 147.246 173.099 1.00 99.46  ? 293 GLU A CD  1 
ATOM   1857 O OE1 . GLU A 1 293 ? 161.762 148.258 172.384 1.00 100.68 ? 293 GLU A OE1 1 
ATOM   1858 O OE2 . GLU A 1 293 ? 161.214 146.219 172.999 1.00 91.14  ? 293 GLU A OE2 1 
ATOM   1859 N N   . MET A 1 294 ? 164.631 150.936 176.531 1.00 108.89 ? 294 MET A N   1 
ATOM   1860 C CA  . MET A 1 294 ? 165.704 151.902 176.887 1.00 108.68 ? 294 MET A CA  1 
ATOM   1861 C C   . MET A 1 294 ? 166.520 151.318 178.049 1.00 111.64 ? 294 MET A C   1 
ATOM   1862 O O   . MET A 1 294 ? 165.905 150.929 179.064 1.00 109.28 ? 294 MET A O   1 
ATOM   1863 C CB  . MET A 1 294 ? 165.120 153.260 177.291 1.00 108.69 ? 294 MET A CB  1 
ATOM   1864 C CG  . MET A 1 294 ? 166.139 154.209 177.889 1.00 118.16 ? 294 MET A CG  1 
ATOM   1865 S SD  . MET A 1 294 ? 167.623 154.385 176.879 1.00 142.58 ? 294 MET A SD  1 
ATOM   1866 C CE  . MET A 1 294 ? 168.684 155.273 178.027 1.00 122.83 ? 294 MET A CE  1 
ATOM   1867 N N   . GLU A 1 295 ? 167.846 151.255 177.899 1.00 115.84 ? 295 GLU A N   1 
ATOM   1868 C CA  . GLU A 1 295 ? 168.705 150.651 178.950 1.00 112.62 ? 295 GLU A CA  1 
ATOM   1869 C C   . GLU A 1 295 ? 169.457 151.760 179.698 1.00 112.93 ? 295 GLU A C   1 
ATOM   1870 O O   . GLU A 1 295 ? 170.447 152.282 179.140 1.00 115.12 ? 295 GLU A O   1 
ATOM   1871 C CB  . GLU A 1 295 ? 169.684 149.660 178.322 1.00 107.98 ? 295 GLU A CB  1 
ATOM   1872 C CG  . GLU A 1 295 ? 170.603 148.990 179.338 1.00 110.11 ? 295 GLU A CG  1 
ATOM   1873 C CD  . GLU A 1 295 ? 172.076 149.246 179.079 1.00 117.22 ? 295 GLU A CD  1 
ATOM   1874 O OE1 . GLU A 1 295 ? 172.560 148.848 177.999 1.00 123.46 ? 295 GLU A OE1 1 
ATOM   1875 O OE2 . GLU A 1 295 ? 172.738 149.850 179.949 1.00 116.49 ? 295 GLU A OE2 1 
ATOM   1876 N N   . GLU A 1 296 ? 169.004 152.107 180.905 1.00 111.21 ? 296 GLU A N   1 
ATOM   1877 C CA  . GLU A 1 296 ? 169.732 153.109 181.726 1.00 111.54 ? 296 GLU A CA  1 
ATOM   1878 C C   . GLU A 1 296 ? 170.798 152.362 182.534 1.00 113.41 ? 296 GLU A C   1 
ATOM   1879 O O   . GLU A 1 296 ? 171.991 152.457 182.172 1.00 111.28 ? 296 GLU A O   1 
ATOM   1880 C CB  . GLU A 1 296 ? 168.777 153.859 182.654 1.00 108.35 ? 296 GLU A CB  1 
ATOM   1881 C CG  . GLU A 1 296 ? 167.545 154.408 181.941 1.00 112.24 ? 296 GLU A CG  1 
ATOM   1882 C CD  . GLU A 1 296 ? 166.331 153.504 182.031 1.00 111.50 ? 296 GLU A CD  1 
ATOM   1883 O OE1 . GLU A 1 296 ? 165.872 153.251 183.164 1.00 108.75 ? 296 GLU A OE1 1 
ATOM   1884 O OE2 . GLU A 1 296 ? 165.847 153.051 180.975 1.00 113.54 ? 296 GLU A OE2 1 
ATOM   1885 N N   . ASP A 1 297 ? 170.380 151.641 183.577 1.00 117.47 ? 297 ASP A N   1 
ATOM   1886 C CA  . ASP A 1 297 ? 171.306 150.838 184.361 1.00 115.68 ? 297 ASP A CA  1 
ATOM   1887 C C   . ASP A 1 297 ? 171.605 149.551 183.593 1.00 116.97 ? 297 ASP A C   1 
ATOM   1888 O O   . ASP A 1 297 ? 171.277 149.420 182.410 1.00 115.66 ? 297 ASP A O   1 
ATOM   1889 C CB  . ASP A 1 297 ? 170.739 150.560 185.756 1.00 113.30 ? 297 ASP A CB  1 
ATOM   1890 C CG  . ASP A 1 297 ? 169.243 150.321 185.741 1.00 112.93 ? 297 ASP A CG  1 
ATOM   1891 O OD1 . ASP A 1 297 ? 168.638 150.401 184.652 1.00 115.00 ? 297 ASP A OD1 1 
ATOM   1892 O OD2 . ASP A 1 297 ? 168.672 150.055 186.819 1.00 110.64 ? 297 ASP A OD2 1 
ATOM   1893 N N   . GLY A 1 298 ? 172.240 148.600 184.273 1.00 115.01 ? 298 GLY A N   1 
ATOM   1894 C CA  . GLY A 1 298 ? 172.625 147.345 183.655 1.00 113.28 ? 298 GLY A CA  1 
ATOM   1895 C C   . GLY A 1 298 ? 171.482 146.563 183.035 1.00 111.90 ? 298 GLY A C   1 
ATOM   1896 O O   . GLY A 1 298 ? 171.710 145.686 182.197 1.00 111.08 ? 298 GLY A O   1 
ATOM   1897 N N   . VAL A 1 299 ? 170.248 146.926 183.401 1.00 110.31 ? 299 VAL A N   1 
ATOM   1898 C CA  . VAL A 1 299 ? 169.044 146.243 182.835 1.00 108.09 ? 299 VAL A CA  1 
ATOM   1899 C C   . VAL A 1 299 ? 168.187 147.278 182.085 1.00 106.18 ? 299 VAL A C   1 
ATOM   1900 O O   . VAL A 1 299 ? 167.958 148.374 182.640 1.00 101.87 ? 299 VAL A O   1 
ATOM   1901 C CB  . VAL A 1 299 ? 168.243 145.534 183.945 1.00 105.55 ? 299 VAL A CB  1 
ATOM   1902 C CG1 . VAL A 1 299 ? 167.960 146.455 185.126 1.00 102.81 ? 299 VAL A CG1 1 
ATOM   1903 C CG2 . VAL A 1 299 ? 166.958 144.907 183.418 1.00 97.52  ? 299 VAL A CG2 1 
ATOM   1904 N N   . ARG A 1 300 ? 167.736 146.937 180.873 1.00 106.24 ? 300 ARG A N   1 
ATOM   1905 C CA  . ARG A 1 300 ? 166.883 147.857 180.074 1.00 103.16 ? 300 ARG A CA  1 
ATOM   1906 C C   . ARG A 1 300 ? 165.461 147.880 180.655 1.00 94.62  ? 300 ARG A C   1 
ATOM   1907 O O   . ARG A 1 300 ? 165.059 146.876 181.283 1.00 94.63  ? 300 ARG A O   1 
ATOM   1908 C CB  . ARG A 1 300 ? 166.877 147.414 178.607 1.00 97.28  ? 300 ARG A CB  1 
ATOM   1909 C CG  . ARG A 1 300 ? 167.065 145.915 178.423 1.00 91.98  ? 300 ARG A CG  1 
ATOM   1910 C CD  . ARG A 1 300 ? 167.089 145.550 176.949 1.00 92.91  ? 300 ARG A CD  1 
ATOM   1911 N NE  . ARG A 1 300 ? 168.005 146.410 176.193 1.00 103.93 ? 300 ARG A NE  1 
ATOM   1912 C CZ  . ARG A 1 300 ? 168.196 146.334 174.883 1.00 100.86 ? 300 ARG A CZ  1 
ATOM   1913 N NH1 . ARG A 1 300 ? 167.500 145.472 174.163 1.00 89.49  ? 300 ARG A NH1 1 
ATOM   1914 N NH2 . ARG A 1 300 ? 169.078 147.123 174.297 1.00 95.03  ? 300 ARG A NH2 1 
ATOM   1915 N N   . LYS A 1 301 ? 164.733 148.980 180.442 1.00 89.91  ? 301 LYS A N   1 
ATOM   1916 C CA  . LYS A 1 301 ? 163.359 149.109 180.993 1.00 87.62  ? 301 LYS A CA  1 
ATOM   1917 C C   . LYS A 1 301 ? 162.395 149.528 179.873 1.00 93.45  ? 301 LYS A C   1 
ATOM   1918 O O   . LYS A 1 301 ? 162.843 150.208 178.925 1.00 98.36  ? 301 LYS A O   1 
ATOM   1919 C CB  . LYS A 1 301 ? 163.346 150.111 182.151 1.00 86.28  ? 301 LYS A CB  1 
ATOM   1920 C CG  . LYS A 1 301 ? 164.356 149.807 183.247 1.00 88.74  ? 301 LYS A CG  1 
ATOM   1921 C CD  . LYS A 1 301 ? 164.221 150.684 184.484 1.00 84.52  ? 301 LYS A CD  1 
ATOM   1922 C CE  . LYS A 1 301 ? 165.297 150.394 185.480 1.00 87.39  ? 301 LYS A CE  1 
ATOM   1923 N NZ  . LYS A 1 301 ? 165.346 148.968 185.811 1.00 86.86  ? 301 LYS A NZ  1 
ATOM   1924 N N   . CYS A 1 302 ? 161.125 149.130 179.984 1.00 91.16  ? 302 CYS A N   1 
ATOM   1925 C CA  . CYS A 1 302 ? 160.110 149.484 178.958 1.00 88.34  ? 302 CYS A CA  1 
ATOM   1926 C C   . CYS A 1 302 ? 159.552 150.884 179.249 1.00 96.37  ? 302 CYS A C   1 
ATOM   1927 O O   . CYS A 1 302 ? 158.447 150.971 179.827 1.00 96.84  ? 302 CYS A O   1 
ATOM   1928 C CB  . CYS A 1 302 ? 158.961 148.485 178.962 1.00 83.93  ? 302 CYS A CB  1 
ATOM   1929 S SG  . CYS A 1 302 ? 159.347 146.961 178.066 1.00 95.17  ? 302 CYS A SG  1 
ATOM   1930 N N   . LYS A 1 303 ? 160.279 151.929 178.847 1.00 97.24  ? 303 LYS A N   1 
ATOM   1931 C CA  . LYS A 1 303 ? 159.827 153.320 179.108 1.00 97.75  ? 303 LYS A CA  1 
ATOM   1932 C C   . LYS A 1 303 ? 158.641 153.641 178.184 1.00 99.91  ? 303 LYS A C   1 
ATOM   1933 O O   . LYS A 1 303 ? 158.658 153.181 177.024 1.00 100.12 ? 303 LYS A O   1 
ATOM   1934 C CB  . LYS A 1 303 ? 160.997 154.290 178.916 1.00 98.11  ? 303 LYS A CB  1 
ATOM   1935 C CG  . LYS A 1 303 ? 162.316 153.804 179.498 1.00 97.88  ? 303 LYS A CG  1 
ATOM   1936 C CD  . LYS A 1 303 ? 163.237 154.938 179.926 1.00 106.10 ? 303 LYS A CD  1 
ATOM   1937 C CE  . LYS A 1 303 ? 162.800 155.559 181.213 1.00 107.85 ? 303 LYS A CE  1 
ATOM   1938 N NZ  . LYS A 1 303 ? 162.823 154.583 182.306 1.00 104.93 ? 303 LYS A NZ  1 
ATOM   1939 N N   . LYS A 1 304 ? 157.655 154.392 178.684 1.00 97.84  ? 304 LYS A N   1 
ATOM   1940 C CA  . LYS A 1 304 ? 156.479 154.717 177.889 1.00 97.83  ? 304 LYS A CA  1 
ATOM   1941 C C   . LYS A 1 304 ? 156.855 155.614 176.716 1.00 99.23  ? 304 LYS A C   1 
ATOM   1942 O O   . LYS A 1 304 ? 157.669 156.532 176.850 1.00 100.78 ? 304 LYS A O   1 
ATOM   1943 C CB  . LYS A 1 304 ? 155.424 155.402 178.758 1.00 96.33  ? 304 LYS A CB  1 
ATOM   1944 C CG  . LYS A 1 304 ? 153.992 155.142 178.319 1.00 93.18  ? 304 LYS A CG  1 
ATOM   1945 C CD  . LYS A 1 304 ? 153.718 153.654 178.176 1.00 96.53  ? 304 LYS A CD  1 
ATOM   1946 C CE  . LYS A 1 304 ? 153.596 152.980 179.532 1.00 96.53  ? 304 LYS A CE  1 
ATOM   1947 N NZ  . LYS A 1 304 ? 152.739 151.765 179.473 1.00 96.74  ? 304 LYS A NZ  1 
ATOM   1948 N N   . CYS A 1 305 ? 156.257 155.340 175.560 1.00 98.21  ? 305 CYS A N   1 
ATOM   1949 C CA  . CYS A 1 305 ? 156.511 156.148 174.376 1.00 96.88  ? 305 CYS A CA  1 
ATOM   1950 C C   . CYS A 1 305 ? 155.961 157.557 174.561 1.00 105.14 ? 305 CYS A C   1 
ATOM   1951 O O   . CYS A 1 305 ? 154.853 157.747 175.070 1.00 109.70 ? 305 CYS A O   1 
ATOM   1952 C CB  . CYS A 1 305 ? 155.879 155.504 173.141 1.00 98.14  ? 305 CYS A CB  1 
ATOM   1953 S SG  . CYS A 1 305 ? 156.582 153.913 172.645 1.00 122.65 ? 305 CYS A SG  1 
ATOM   1954 N N   . GLU A 1 306 ? 156.745 158.548 174.144 1.00 104.31 ? 306 GLU A N   1 
ATOM   1955 C CA  . GLU A 1 306 ? 156.300 159.941 174.145 1.00 100.71 ? 306 GLU A CA  1 
ATOM   1956 C C   . GLU A 1 306 ? 155.352 160.114 172.966 1.00 92.02  ? 306 GLU A C   1 
ATOM   1957 O O   . GLU A 1 306 ? 155.748 160.508 171.868 1.00 88.25  ? 306 GLU A O   1 
ATOM   1958 C CB  . GLU A 1 306 ? 157.488 160.891 174.064 1.00 100.24 ? 306 GLU A CB  1 
ATOM   1959 C CG  . GLU A 1 306 ? 158.650 160.368 173.234 1.00 102.17 ? 306 GLU A CG  1 
ATOM   1960 C CD  . GLU A 1 306 ? 159.777 161.373 173.109 1.00 101.15 ? 306 GLU A CD  1 
ATOM   1961 O OE1 . GLU A 1 306 ? 159.532 162.575 173.343 1.00 99.16  ? 306 GLU A OE1 1 
ATOM   1962 O OE2 . GLU A 1 306 ? 160.909 160.962 172.777 1.00 98.66  ? 306 GLU A OE2 1 
ATOM   1963 N N   . GLY A 1 307 ? 154.076 159.820 173.201 1.00 87.07  ? 307 GLY A N   1 
ATOM   1964 C CA  . GLY A 1 307 ? 153.115 159.718 172.132 1.00 87.14  ? 307 GLY A CA  1 
ATOM   1965 C C   . GLY A 1 307 ? 153.484 158.586 171.196 1.00 96.00  ? 307 GLY A C   1 
ATOM   1966 O O   . GLY A 1 307 ? 153.761 157.462 171.627 1.00 96.94  ? 307 GLY A O   1 
ATOM   1967 N N   . PRO A 1 308 ? 153.496 158.858 169.890 1.00 96.71  ? 308 PRO A N   1 
ATOM   1968 C CA  . PRO A 1 308 ? 153.986 157.858 168.929 1.00 85.98  ? 308 PRO A CA  1 
ATOM   1969 C C   . PRO A 1 308 ? 155.508 157.845 168.915 1.00 85.82  ? 308 PRO A C   1 
ATOM   1970 O O   . PRO A 1 308 ? 156.144 158.822 168.513 1.00 78.68  ? 308 PRO A O   1 
ATOM   1971 C CB  . PRO A 1 308 ? 153.409 158.339 167.594 1.00 73.26  ? 308 PRO A CB  1 
ATOM   1972 C CG  . PRO A 1 308 ? 153.245 159.813 167.765 1.00 69.27  ? 308 PRO A CG  1 
ATOM   1973 C CD  . PRO A 1 308 ? 152.969 160.063 169.226 1.00 83.10  ? 308 PRO A CD  1 
ATOM   1974 N N   . CYS A 1 309 ? 156.093 156.736 169.357 1.00 81.76  ? 309 CYS A N   1 
ATOM   1975 C CA  . CYS A 1 309 ? 157.541 156.643 169.484 1.00 83.81  ? 309 CYS A CA  1 
ATOM   1976 C C   . CYS A 1 309 ? 158.163 156.253 168.143 1.00 59.40  ? 309 CYS A C   1 
ATOM   1977 O O   . CYS A 1 309 ? 157.501 156.224 167.102 1.00 57.31  ? 309 CYS A O   1 
ATOM   1978 C CB  . CYS A 1 309 ? 157.916 155.678 170.605 1.00 95.78  ? 309 CYS A CB  1 
ATOM   1979 S SG  . CYS A 1 309 ? 156.972 154.143 170.664 1.00 115.82 ? 309 CYS A SG  1 
ATOM   1980 N N   . ARG A 1 310 ? 159.457 155.945 168.165 1.00 44.10  ? 310 ARG A N   1 
ATOM   1981 C CA  . ARG A 1 310 ? 160.238 155.821 166.941 1.00 30.16  ? 310 ARG A CA  1 
ATOM   1982 C C   . ARG A 1 310 ? 159.856 154.559 166.175 1.00 34.36  ? 310 ARG A C   1 
ATOM   1983 O O   . ARG A 1 310 ? 159.944 153.447 166.706 1.00 43.25  ? 310 ARG A O   1 
ATOM   1984 C CB  . ARG A 1 310 ? 161.727 155.813 167.277 1.00 34.25  ? 310 ARG A CB  1 
ATOM   1985 C CG  . ARG A 1 310 ? 162.639 155.692 166.072 1.00 29.48  ? 310 ARG A CG  1 
ATOM   1986 C CD  . ARG A 1 310 ? 163.719 156.760 166.099 1.00 26.99  ? 310 ARG A CD  1 
ATOM   1987 N NE  . ARG A 1 310 ? 164.960 156.298 165.489 1.00 26.21  ? 310 ARG A NE  1 
ATOM   1988 C CZ  . ARG A 1 310 ? 166.042 157.049 165.336 1.00 23.62  ? 310 ARG A CZ  1 
ATOM   1989 N NH1 . ARG A 1 310 ? 166.073 158.309 165.737 1.00 15.52  ? 310 ARG A NH1 1 
ATOM   1990 N NH2 . ARG A 1 310 ? 167.121 156.521 164.764 1.00 18.85  ? 310 ARG A NH2 1 
ATOM   1991 N N   . LYS A 1 311 ? 159.430 154.738 164.924 1.00 32.25  ? 311 LYS A N   1 
ATOM   1992 C CA  . LYS A 1 311 ? 159.193 153.645 163.979 1.00 31.94  ? 311 LYS A CA  1 
ATOM   1993 C C   . LYS A 1 311 ? 159.818 154.074 162.656 1.00 21.54  ? 311 LYS A C   1 
ATOM   1994 O O   . LYS A 1 311 ? 159.149 154.674 161.812 1.00 22.51  ? 311 LYS A O   1 
ATOM   1995 C CB  . LYS A 1 311 ? 157.705 153.339 163.832 1.00 31.32  ? 311 LYS A CB  1 
ATOM   1996 C CG  . LYS A 1 311 ? 157.399 152.267 162.796 1.00 33.74  ? 311 LYS A CG  1 
ATOM   1997 C CD  . LYS A 1 311 ? 156.018 151.672 162.994 1.00 39.37  ? 311 LYS A CD  1 
ATOM   1998 C CE  . LYS A 1 311 ? 155.539 150.972 161.734 1.00 41.91  ? 311 LYS A CE  1 
ATOM   1999 N NZ  . LYS A 1 311 ? 155.478 151.902 160.572 1.00 37.27  ? 311 LYS A NZ  1 
ATOM   2000 N N   . VAL A 1 312 ? 161.098 153.758 162.472 1.00 23.40  ? 312 VAL A N   1 
ATOM   2001 C CA  . VAL A 1 312 ? 161.843 154.243 161.314 1.00 20.45  ? 312 VAL A CA  1 
ATOM   2002 C C   . VAL A 1 312 ? 161.360 153.497 160.074 1.00 25.38  ? 312 VAL A C   1 
ATOM   2003 O O   . VAL A 1 312 ? 161.533 152.281 159.962 1.00 29.32  ? 312 VAL A O   1 
ATOM   2004 C CB  . VAL A 1 312 ? 163.354 154.076 161.507 1.00 19.14  ? 312 VAL A CB  1 
ATOM   2005 C CG1 . VAL A 1 312 ? 164.093 154.429 160.226 1.00 22.21  ? 312 VAL A CG1 1 
ATOM   2006 C CG2 . VAL A 1 312 ? 163.838 154.938 162.658 1.00 21.59  ? 312 VAL A CG2 1 
ATOM   2007 N N   . CYS A 1 313 ? 160.757 154.225 159.141 1.00 24.16  ? 313 CYS A N   1 
ATOM   2008 C CA  . CYS A 1 313 ? 160.381 153.696 157.840 1.00 27.30  ? 313 CYS A CA  1 
ATOM   2009 C C   . CYS A 1 313 ? 161.243 154.336 156.760 1.00 22.60  ? 313 CYS A C   1 
ATOM   2010 O O   . CYS A 1 313 ? 161.927 155.336 156.986 1.00 23.31  ? 313 CYS A O   1 
ATOM   2011 C CB  . CYS A 1 313 ? 158.897 153.942 157.547 1.00 25.16  ? 313 CYS A CB  1 
ATOM   2012 S SG  . CYS A 1 313 ? 157.815 153.832 158.981 1.00 28.37  ? 313 CYS A SG  1 
ATOM   2013 N N   . ASN A 1 314 ? 161.199 153.743 155.573 1.00 22.93  ? 314 ASN A N   1 
ATOM   2014 C CA  . ASN A 1 314 ? 161.958 154.243 154.438 1.00 25.92  ? 314 ASN A CA  1 
ATOM   2015 C C   . ASN A 1 314 ? 161.128 155.252 153.657 1.00 30.96  ? 314 ASN A C   1 
ATOM   2016 O O   . ASN A 1 314 ? 159.925 155.064 153.456 1.00 33.09  ? 314 ASN A O   1 
ATOM   2017 C CB  . ASN A 1 314 ? 162.387 153.095 153.524 1.00 27.09  ? 314 ASN A CB  1 
ATOM   2018 C CG  . ASN A 1 314 ? 163.811 152.648 153.783 1.00 28.87  ? 314 ASN A CG  1 
ATOM   2019 O OD1 . ASN A 1 314 ? 164.704 152.879 152.970 1.00 38.27  ? 314 ASN A OD1 1 
ATOM   2020 N ND2 . ASN A 1 314 ? 164.030 152.003 154.923 1.00 34.83  ? 314 ASN A ND2 1 
ATOM   2021 N N   . GLY A 1 315 ? 161.781 156.312 153.178 1.00 26.00  ? 315 GLY A N   1 
ATOM   2022 C CA  . GLY A 1 315 ? 161.060 157.357 152.429 1.00 17.26  ? 315 GLY A CA  1 
ATOM   2023 C C   . GLY A 1 315 ? 161.082 157.091 150.939 1.00 19.13  ? 315 GLY A C   1 
ATOM   2024 O O   . GLY A 1 315 ? 161.346 155.939 150.548 1.00 26.54  ? 315 GLY A O   1 
ATOM   2025 N N   . ILE A 1 316 ? 160.814 158.121 150.134 1.00 21.17  ? 316 ILE A N   1 
ATOM   2026 C CA  . ILE A 1 316 ? 160.776 157.962 148.650 1.00 22.80  ? 316 ILE A CA  1 
ATOM   2027 C C   . ILE A 1 316 ? 162.211 158.058 148.109 1.00 23.75  ? 316 ILE A C   1 
ATOM   2028 O O   . ILE A 1 316 ? 162.869 159.088 148.363 1.00 25.27  ? 316 ILE A O   1 
ATOM   2029 C CB  . ILE A 1 316 ? 159.829 158.990 147.997 1.00 13.99  ? 316 ILE A CB  1 
ATOM   2030 C CG1 . ILE A 1 316 ? 158.365 158.561 148.096 1.00 9.49   ? 316 ILE A CG1 1 
ATOM   2031 C CG2 . ILE A 1 316 ? 160.225 159.260 146.546 1.00 17.86  ? 316 ILE A CG2 1 
ATOM   2032 C CD1 . ILE A 1 316 ? 157.801 158.567 149.505 1.00 10.35  ? 316 ILE A CD1 1 
ATOM   2033 N N   . GLY A 1 317 ? 162.678 157.017 147.418 1.00 29.89  ? 317 GLY A N   1 
ATOM   2034 C CA  . GLY A 1 317 ? 164.005 157.007 146.825 1.00 34.12  ? 317 GLY A CA  1 
ATOM   2035 C C   . GLY A 1 317 ? 164.867 155.844 147.279 1.00 40.19  ? 317 GLY A C   1 
ATOM   2036 O O   . GLY A 1 317 ? 165.750 155.407 146.533 1.00 42.70  ? 317 GLY A O   1 
ATOM   2037 N N   . ILE A 1 318 ? 164.630 155.337 148.486 1.00 37.44  ? 318 ILE A N   1 
ATOM   2038 C CA  . ILE A 1 318 ? 165.390 154.217 149.030 1.00 33.60  ? 318 ILE A CA  1 
ATOM   2039 C C   . ILE A 1 318 ? 164.424 153.232 149.672 1.00 29.97  ? 318 ILE A C   1 
ATOM   2040 O O   . ILE A 1 318 ? 163.441 153.631 150.306 1.00 28.56  ? 318 ILE A O   1 
ATOM   2041 C CB  . ILE A 1 318 ? 166.455 154.683 150.045 1.00 34.65  ? 318 ILE A CB  1 
ATOM   2042 C CG1 . ILE A 1 318 ? 165.831 155.585 151.111 1.00 26.85  ? 318 ILE A CG1 1 
ATOM   2043 C CG2 . ILE A 1 318 ? 167.598 155.395 149.335 1.00 39.71  ? 318 ILE A CG2 1 
ATOM   2044 C CD1 . ILE A 1 318 ? 166.836 156.152 152.088 1.00 29.41  ? 318 ILE A CD1 1 
ATOM   2045 N N   . GLY A 1 319 ? 164.703 151.942 149.502 1.00 29.46  ? 319 GLY A N   1 
ATOM   2046 C CA  . GLY A 1 319 ? 163.878 150.902 150.084 1.00 30.32  ? 319 GLY A CA  1 
ATOM   2047 C C   . GLY A 1 319 ? 162.804 150.397 149.145 1.00 36.90  ? 319 GLY A C   1 
ATOM   2048 O O   . GLY A 1 319 ? 163.020 150.316 147.932 1.00 38.67  ? 319 GLY A O   1 
ATOM   2049 N N   . GLU A 1 320 ? 161.640 150.046 149.696 1.00 33.16  ? 320 GLU A N   1 
ATOM   2050 C CA  . GLU A 1 320 ? 160.527 149.602 148.865 1.00 32.02  ? 320 GLU A CA  1 
ATOM   2051 C C   . GLU A 1 320 ? 160.018 150.708 147.951 1.00 35.12  ? 320 GLU A C   1 
ATOM   2052 O O   . GLU A 1 320 ? 159.426 150.412 146.908 1.00 30.33  ? 320 GLU A O   1 
ATOM   2053 C CB  . GLU A 1 320 ? 159.390 149.082 149.745 1.00 27.93  ? 320 GLU A CB  1 
ATOM   2054 C CG  . GLU A 1 320 ? 158.785 150.133 150.659 1.00 29.93  ? 320 GLU A CG  1 
ATOM   2055 C CD  . GLU A 1 320 ? 157.746 149.557 151.600 1.00 35.69  ? 320 GLU A CD  1 
ATOM   2056 O OE1 . GLU A 1 320 ? 157.249 148.443 151.329 1.00 30.30  ? 320 GLU A OE1 1 
ATOM   2057 O OE2 . GLU A 1 320 ? 157.427 150.217 152.610 1.00 39.94  ? 320 GLU A OE2 1 
ATOM   2058 N N   . PHE A 1 321 ? 160.232 151.972 148.320 1.00 36.09  ? 321 PHE A N   1 
ATOM   2059 C CA  . PHE A 1 321 ? 159.860 153.114 147.495 1.00 25.28  ? 321 PHE A CA  1 
ATOM   2060 C C   . PHE A 1 321 ? 161.052 153.687 146.738 1.00 28.51  ? 321 PHE A C   1 
ATOM   2061 O O   . PHE A 1 321 ? 161.125 154.902 146.522 1.00 26.11  ? 321 PHE A O   1 
ATOM   2062 C CB  . PHE A 1 321 ? 159.207 154.197 148.353 1.00 22.96  ? 321 PHE A CB  1 
ATOM   2063 C CG  . PHE A 1 321 ? 158.365 153.659 149.470 1.00 24.29  ? 321 PHE A CG  1 
ATOM   2064 C CD1 . PHE A 1 321 ? 157.100 153.156 149.221 1.00 24.37  ? 321 PHE A CD1 1 
ATOM   2065 C CD2 . PHE A 1 321 ? 158.836 153.658 150.771 1.00 23.23  ? 321 PHE A CD2 1 
ATOM   2066 C CE1 . PHE A 1 321 ? 156.321 152.662 150.248 1.00 25.21  ? 321 PHE A CE1 1 
ATOM   2067 C CE2 . PHE A 1 321 ? 158.061 153.164 151.801 1.00 25.09  ? 321 PHE A CE2 1 
ATOM   2068 C CZ  . PHE A 1 321 ? 156.803 152.666 151.539 1.00 28.69  ? 321 PHE A CZ  1 
ATOM   2069 N N   . LYS A 1 322 ? 161.998 152.833 146.341 1.00 33.19  ? 322 LYS A N   1 
ATOM   2070 C CA  . LYS A 1 322 ? 163.168 153.312 145.614 1.00 35.96  ? 322 LYS A CA  1 
ATOM   2071 C C   . LYS A 1 322 ? 162.783 153.892 144.258 1.00 38.92  ? 322 LYS A C   1 
ATOM   2072 O O   . LYS A 1 322 ? 163.304 154.937 143.854 1.00 40.06  ? 322 LYS A O   1 
ATOM   2073 C CB  . LYS A 1 322 ? 164.180 152.178 145.448 1.00 36.32  ? 322 LYS A CB  1 
ATOM   2074 C CG  . LYS A 1 322 ? 165.447 152.575 144.705 1.00 32.56  ? 322 LYS A CG  1 
ATOM   2075 C CD  . LYS A 1 322 ? 166.314 151.366 144.379 1.00 38.93  ? 322 LYS A CD  1 
ATOM   2076 C CE  . LYS A 1 322 ? 165.477 150.123 144.110 1.00 36.96  ? 322 LYS A CE  1 
ATOM   2077 N NZ  . LYS A 1 322 ? 164.881 150.136 142.746 1.00 33.70  ? 322 LYS A NZ  1 
ATOM   2078 N N   . ASP A 1 323 ? 161.876 153.229 143.543 1.00 32.78  ? 323 ASP A N   1 
ATOM   2079 C CA  . ASP A 1 323 ? 161.431 153.684 142.234 1.00 27.43  ? 323 ASP A CA  1 
ATOM   2080 C C   . ASP A 1 323 ? 160.153 154.510 142.293 1.00 31.64  ? 323 ASP A C   1 
ATOM   2081 O O   . ASP A 1 323 ? 159.683 154.971 141.249 1.00 33.14  ? 323 ASP A O   1 
ATOM   2082 C CB  . ASP A 1 323 ? 161.229 152.485 141.303 1.00 36.66  ? 323 ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 323 ? 162.472 151.628 141.178 1.00 47.88  ? 323 ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 323 ? 163.417 152.048 140.478 1.00 45.68  ? 323 ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 323 ? 162.506 150.534 141.780 1.00 54.11  ? 323 ASP A OD2 1 
ATOM   2086 N N   . SER A 1 324 ? 159.582 154.705 143.478 1.00 28.56  ? 324 SER A N   1 
ATOM   2087 C CA  . SER A 1 324 ? 158.379 155.515 143.609 1.00 13.91  ? 324 SER A CA  1 
ATOM   2088 C C   . SER A 1 324 ? 158.694 156.994 143.407 1.00 20.93  ? 324 SER A C   1 
ATOM   2089 O O   . SER A 1 324 ? 159.791 157.468 143.712 1.00 23.54  ? 324 SER A O   1 
ATOM   2090 C CB  . SER A 1 324 ? 157.739 155.304 144.978 1.00 12.38  ? 324 SER A CB  1 
ATOM   2091 O OG  . SER A 1 324 ? 157.363 153.952 145.160 1.00 21.70  ? 324 SER A OG  1 
ATOM   2092 N N   . LEU A 1 325 ? 157.712 157.728 142.882 1.00 18.16  ? 325 LEU A N   1 
ATOM   2093 C CA  . LEU A 1 325 ? 157.884 159.151 142.614 1.00 10.33  ? 325 LEU A CA  1 
ATOM   2094 C C   . LEU A 1 325 ? 157.363 160.028 143.743 1.00 11.39  ? 325 LEU A C   1 
ATOM   2095 O O   . LEU A 1 325 ? 157.975 161.054 144.063 1.00 14.41  ? 325 LEU A O   1 
ATOM   2096 C CB  . LEU A 1 325 ? 157.183 159.537 141.312 1.00 8.69   ? 325 LEU A CB  1 
ATOM   2097 C CG  . LEU A 1 325 ? 157.483 158.685 140.079 1.00 12.09  ? 325 LEU A CG  1 
ATOM   2098 C CD1 . LEU A 1 325 ? 156.363 158.814 139.064 1.00 13.23  ? 325 LEU A CD1 1 
ATOM   2099 C CD2 . LEU A 1 325 ? 158.819 159.087 139.459 1.00 12.57  ? 325 LEU A CD2 1 
ATOM   2100 N N   . SER A 1 326 ? 156.238 159.652 144.344 1.00 7.78   ? 326 SER A N   1 
ATOM   2101 C CA  . SER A 1 326 ? 155.600 160.459 145.369 1.00 8.40   ? 326 SER A CA  1 
ATOM   2102 C C   . SER A 1 326 ? 154.917 159.530 146.359 1.00 10.41  ? 326 SER A C   1 
ATOM   2103 O O   . SER A 1 326 ? 155.066 158.307 146.302 1.00 14.00  ? 326 SER A O   1 
ATOM   2104 C CB  . SER A 1 326 ? 154.592 161.436 144.759 1.00 10.16  ? 326 SER A CB  1 
ATOM   2105 O OG  . SER A 1 326 ? 153.267 160.943 144.877 1.00 12.35  ? 326 SER A OG  1 
ATOM   2106 N N   . ILE A 1 327 ? 154.154 160.127 147.273 1.00 9.19   ? 327 ILE A N   1 
ATOM   2107 C CA  . ILE A 1 327 ? 153.348 159.373 148.236 1.00 12.01  ? 327 ILE A CA  1 
ATOM   2108 C C   . ILE A 1 327 ? 151.956 159.260 147.624 1.00 14.78  ? 327 ILE A C   1 
ATOM   2109 O O   . ILE A 1 327 ? 151.052 160.041 147.913 1.00 31.06  ? 327 ILE A O   1 
ATOM   2110 C CB  . ILE A 1 327 ? 153.327 160.031 149.610 1.00 9.11   ? 327 ILE A CB  1 
ATOM   2111 C CG1 . ILE A 1 327 ? 154.747 160.153 150.158 1.00 7.79   ? 327 ILE A CG1 1 
ATOM   2112 C CG2 . ILE A 1 327 ? 152.468 159.223 150.584 1.00 14.10  ? 327 ILE A CG2 1 
ATOM   2113 C CD1 . ILE A 1 327 ? 154.815 160.694 151.567 1.00 8.04   ? 327 ILE A CD1 1 
ATOM   2114 N N   . ASN A 1 328 ? 151.789 158.267 146.761 1.00 12.40  ? 328 ASN A N   1 
ATOM   2115 C CA  . ASN A 1 328 ? 150.495 157.975 146.173 1.00 13.00  ? 328 ASN A CA  1 
ATOM   2116 C C   . ASN A 1 328 ? 149.746 156.969 147.046 1.00 24.73  ? 328 ASN A C   1 
ATOM   2117 O O   . ASN A 1 328 ? 150.149 156.664 148.173 1.00 25.69  ? 328 ASN A O   1 
ATOM   2118 C CB  . ASN A 1 328 ? 150.683 157.539 144.726 1.00 19.46  ? 328 ASN A CB  1 
ATOM   2119 C CG  . ASN A 1 328 ? 151.958 156.730 144.507 1.00 16.43  ? 328 ASN A CG  1 
ATOM   2120 O OD1 . ASN A 1 328 ? 153.052 157.230 144.760 1.00 14.80  ? 328 ASN A OD1 1 
ATOM   2121 N ND2 . ASN A 1 328 ? 151.824 155.498 144.014 1.00 19.39  ? 328 ASN A ND2 1 
ATOM   2122 N N   . ALA A 1 329 ? 148.616 156.466 146.543 1.00 29.73  ? 329 ALA A N   1 
ATOM   2123 C CA  . ALA A 1 329 ? 147.696 155.714 147.394 1.00 27.40  ? 329 ALA A CA  1 
ATOM   2124 C C   . ALA A 1 329 ? 148.319 154.416 147.894 1.00 27.47  ? 329 ALA A C   1 
ATOM   2125 O O   . ALA A 1 329 ? 148.092 154.015 149.040 1.00 29.29  ? 329 ALA A O   1 
ATOM   2126 C CB  . ALA A 1 329 ? 146.398 155.435 146.645 1.00 26.92  ? 329 ALA A CB  1 
ATOM   2127 N N   . THR A 1 330 ? 149.078 153.729 147.040 1.00 23.60  ? 330 THR A N   1 
ATOM   2128 C CA  . THR A 1 330 ? 149.799 152.543 147.491 1.00 29.82  ? 330 THR A CA  1 
ATOM   2129 C C   . THR A 1 330 ? 150.843 152.900 148.545 1.00 31.25  ? 330 THR A C   1 
ATOM   2130 O O   . THR A 1 330 ? 151.038 152.152 149.511 1.00 31.96  ? 330 THR A O   1 
ATOM   2131 C CB  . THR A 1 330 ? 150.447 151.846 146.299 1.00 27.79  ? 330 THR A CB  1 
ATOM   2132 O OG1 . THR A 1 330 ? 151.546 152.634 145.842 1.00 31.87  ? 330 THR A OG1 1 
ATOM   2133 C CG2 . THR A 1 330 ? 149.448 151.710 145.171 1.00 22.42  ? 330 THR A CG2 1 
ATOM   2134 N N   . ASN A 1 331 ? 151.525 154.038 148.378 1.00 26.10  ? 331 ASN A N   1 
ATOM   2135 C CA  . ASN A 1 331 ? 152.486 154.479 149.385 1.00 25.81  ? 331 ASN A CA  1 
ATOM   2136 C C   . ASN A 1 331 ? 151.802 154.747 150.718 1.00 38.94  ? 331 ASN A C   1 
ATOM   2137 O O   . ASN A 1 331 ? 152.336 154.408 151.780 1.00 38.26  ? 331 ASN A O   1 
ATOM   2138 C CB  . ASN A 1 331 ? 153.218 155.733 148.906 1.00 18.05  ? 331 ASN A CB  1 
ATOM   2139 C CG  . ASN A 1 331 ? 154.481 155.414 148.140 1.00 16.60  ? 331 ASN A CG  1 
ATOM   2140 O OD1 . ASN A 1 331 ? 154.571 154.393 147.461 1.00 23.10  ? 331 ASN A OD1 1 
ATOM   2141 N ND2 . ASN A 1 331 ? 155.470 156.284 148.252 1.00 14.37  ? 331 ASN A ND2 1 
ATOM   2142 N N   . ILE A 1 332 ? 150.701 155.494 150.692 1.00 39.54  ? 332 ILE A N   1 
ATOM   2143 C CA  . ILE A 1 332 ? 149.981 155.854 151.944 1.00 35.87  ? 332 ILE A CA  1 
ATOM   2144 C C   . ILE A 1 332 ? 149.647 154.547 152.671 1.00 44.44  ? 332 ILE A C   1 
ATOM   2145 O O   . ILE A 1 332 ? 149.439 153.544 151.959 1.00 46.13  ? 332 ILE A O   1 
ATOM   2146 C CB  . ILE A 1 332 ? 148.739 156.706 151.622 1.00 34.31  ? 332 ILE A CB  1 
ATOM   2147 C CG1 . ILE A 1 332 ? 149.032 158.207 151.737 1.00 36.76  ? 332 ILE A CG1 1 
ATOM   2148 C CG2 . ILE A 1 332 ? 147.536 156.303 152.474 1.00 38.71  ? 332 ILE A CG2 1 
ATOM   2149 C CD1 . ILE A 1 332 ? 149.555 158.654 153.092 1.00 32.53  ? 332 ILE A CD1 1 
ATOM   2150 N N   . LYS A 1 333 ? 149.642 154.546 154.006 1.00 49.08  ? 333 LYS A N   1 
ATOM   2151 C CA  . LYS A 1 333 ? 149.335 153.351 154.847 1.00 49.93  ? 333 LYS A CA  1 
ATOM   2152 C C   . LYS A 1 333 ? 150.653 152.621 155.136 1.00 44.87  ? 333 LYS A C   1 
ATOM   2153 O O   . LYS A 1 333 ? 150.689 151.873 156.133 1.00 48.04  ? 333 LYS A O   1 
ATOM   2154 C CB  . LYS A 1 333 ? 148.301 152.373 154.272 1.00 49.10  ? 333 LYS A CB  1 
ATOM   2155 C CG  . LYS A 1 333 ? 146.984 152.990 153.823 1.00 53.22  ? 333 LYS A CG  1 
ATOM   2156 C CD  . LYS A 1 333 ? 146.411 154.014 154.794 1.00 51.88  ? 333 LYS A CD  1 
ATOM   2157 C CE  . LYS A 1 333 ? 145.069 154.492 154.360 1.00 55.35  ? 333 LYS A CE  1 
ATOM   2158 N NZ  . LYS A 1 333 ? 144.587 155.557 155.240 1.00 55.14  ? 333 LYS A NZ  1 
ATOM   2159 N N   . HIS A 1 334 ? 151.690 152.828 154.321 1.00 40.74  ? 334 HIS A N   1 
ATOM   2160 C CA  . HIS A 1 334 ? 153.031 152.251 154.592 1.00 36.13  ? 334 HIS A CA  1 
ATOM   2161 C C   . HIS A 1 334 ? 153.717 153.206 155.562 1.00 39.16  ? 334 HIS A C   1 
ATOM   2162 O O   . HIS A 1 334 ? 154.787 152.831 156.086 1.00 39.54  ? 334 HIS A O   1 
ATOM   2163 C CB  . HIS A 1 334 ? 153.860 152.081 153.317 1.00 42.17  ? 334 HIS A CB  1 
ATOM   2164 C CG  . HIS A 1 334 ? 153.284 151.140 152.312 1.00 52.48  ? 334 HIS A CG  1 
ATOM   2165 N ND1 . HIS A 1 334 ? 154.088 150.430 151.447 1.00 45.27  ? 334 HIS A ND1 1 
ATOM   2166 C CD2 . HIS A 1 334 ? 152.026 150.785 152.021 1.00 50.71  ? 334 HIS A CD2 1 
ATOM   2167 C CE1 . HIS A 1 334 ? 153.332 149.677 150.664 1.00 39.50  ? 334 HIS A CE1 1 
ATOM   2168 N NE2 . HIS A 1 334 ? 152.075 149.876 150.996 1.00 40.60  ? 334 HIS A NE2 1 
ATOM   2169 N N   . PHE A 1 335 ? 153.134 154.395 155.785 1.00 45.51  ? 335 PHE A N   1 
ATOM   2170 C CA  . PHE A 1 335 ? 153.677 155.369 156.723 1.00 40.23  ? 335 PHE A CA  1 
ATOM   2171 C C   . PHE A 1 335 ? 152.799 155.523 157.960 1.00 44.04  ? 335 PHE A C   1 
ATOM   2172 O O   . PHE A 1 335 ? 152.918 156.519 158.680 1.00 50.73  ? 335 PHE A O   1 
ATOM   2173 C CB  . PHE A 1 335 ? 153.864 156.724 156.039 1.00 32.23  ? 335 PHE A CB  1 
ATOM   2174 C CG  . PHE A 1 335 ? 154.753 156.681 154.829 1.00 34.07  ? 335 PHE A CG  1 
ATOM   2175 C CD1 . PHE A 1 335 ? 156.129 156.767 154.961 1.00 25.39  ? 335 PHE A CD1 1 
ATOM   2176 C CD2 . PHE A 1 335 ? 154.212 156.566 153.560 1.00 31.03  ? 335 PHE A CD2 1 
ATOM   2177 C CE1 . PHE A 1 335 ? 156.949 156.732 153.849 1.00 22.16  ? 335 PHE A CE1 1 
ATOM   2178 C CE2 . PHE A 1 335 ? 155.027 156.530 152.445 1.00 24.38  ? 335 PHE A CE2 1 
ATOM   2179 C CZ  . PHE A 1 335 ? 156.397 156.613 152.590 1.00 24.83  ? 335 PHE A CZ  1 
ATOM   2180 N N   . LYS A 1 336 ? 151.906 154.567 158.208 1.00 41.54  ? 336 LYS A N   1 
ATOM   2181 C CA  . LYS A 1 336 ? 151.040 154.640 159.376 1.00 46.04  ? 336 LYS A CA  1 
ATOM   2182 C C   . LYS A 1 336 ? 151.867 154.553 160.652 1.00 50.54  ? 336 LYS A C   1 
ATOM   2183 O O   . LYS A 1 336 ? 152.864 153.829 160.710 1.00 52.54  ? 336 LYS A O   1 
ATOM   2184 C CB  . LYS A 1 336 ? 150.003 153.518 159.338 1.00 51.43  ? 336 LYS A CB  1 
ATOM   2185 C CG  . LYS A 1 336 ? 148.563 154.001 159.355 1.00 51.90  ? 336 LYS A CG  1 
ATOM   2186 C CD  . LYS A 1 336 ? 148.228 154.704 160.659 1.00 50.49  ? 336 LYS A CD  1 
ATOM   2187 C CE  . LYS A 1 336 ? 146.806 155.240 160.645 1.00 42.09  ? 336 LYS A CE  1 
ATOM   2188 N NZ  . LYS A 1 336 ? 146.497 156.035 161.865 1.00 41.70  ? 336 LYS A NZ  1 
ATOM   2189 N N   . ASN A 1 337 ? 151.455 155.326 161.664 1.00 44.39  ? 337 ASN A N   1 
ATOM   2190 C CA  . ASN A 1 337 ? 152.119 155.466 162.961 1.00 40.12  ? 337 ASN A CA  1 
ATOM   2191 C C   . ASN A 1 337 ? 153.640 155.465 162.835 1.00 39.50  ? 337 ASN A C   1 
ATOM   2192 O O   . ASN A 1 337 ? 154.340 154.868 163.659 1.00 45.27  ? 337 ASN A O   1 
ATOM   2193 C CB  . ASN A 1 337 ? 151.640 154.388 163.953 1.00 53.64  ? 337 ASN A CB  1 
ATOM   2194 C CG  . ASN A 1 337 ? 151.907 152.956 163.486 1.00 66.92  ? 337 ASN A CG  1 
ATOM   2195 O OD1 . ASN A 1 337 ? 152.985 152.637 162.993 1.00 60.32  ? 337 ASN A OD1 1 
ATOM   2196 N ND2 . ASN A 1 337 ? 150.919 152.081 163.659 1.00 73.51  ? 337 ASN A ND2 1 
ATOM   2197 N N   . CYS A 1 338 ? 154.158 156.157 161.825 1.00 34.13  ? 338 CYS A N   1 
ATOM   2198 C CA  . CYS A 1 338 ? 155.569 156.108 161.475 1.00 29.65  ? 338 CYS A CA  1 
ATOM   2199 C C   . CYS A 1 338 ? 156.254 157.424 161.818 1.00 24.01  ? 338 CYS A C   1 
ATOM   2200 O O   . CYS A 1 338 ? 155.689 158.503 161.617 1.00 33.74  ? 338 CYS A O   1 
ATOM   2201 C CB  . CYS A 1 338 ? 155.750 155.801 159.989 1.00 33.58  ? 338 CYS A CB  1 
ATOM   2202 S SG  . CYS A 1 338 ? 157.465 155.774 159.452 1.00 35.72  ? 338 CYS A SG  1 
ATOM   2203 N N   . THR A 1 339 ? 157.478 157.323 162.330 1.00 20.69  ? 339 THR A N   1 
ATOM   2204 C CA  . THR A 1 339 ? 158.268 158.475 162.734 1.00 18.99  ? 339 THR A CA  1 
ATOM   2205 C C   . THR A 1 339 ? 159.690 158.295 162.222 1.00 23.68  ? 339 THR A C   1 
ATOM   2206 O O   . THR A 1 339 ? 160.163 157.168 162.057 1.00 30.73  ? 339 THR A O   1 
ATOM   2207 C CB  . THR A 1 339 ? 158.262 158.641 164.262 1.00 21.76  ? 339 THR A CB  1 
ATOM   2208 O OG1 . THR A 1 339 ? 156.914 158.575 164.744 1.00 23.53  ? 339 THR A OG1 1 
ATOM   2209 C CG2 . THR A 1 339 ? 158.865 159.973 164.672 1.00 21.85  ? 339 THR A CG2 1 
ATOM   2210 N N   . SER A 1 340 ? 160.368 159.416 161.971 1.00 21.87  ? 340 SER A N   1 
ATOM   2211 C CA  . SER A 1 340 ? 161.751 159.423 161.491 1.00 21.89  ? 340 SER A CA  1 
ATOM   2212 C C   . SER A 1 340 ? 161.870 158.674 160.160 1.00 15.56  ? 340 SER A C   1 
ATOM   2213 O O   . SER A 1 340 ? 162.506 157.624 160.051 1.00 21.71  ? 340 SER A O   1 
ATOM   2214 C CB  . SER A 1 340 ? 162.704 158.840 162.542 1.00 16.29  ? 340 SER A CB  1 
ATOM   2215 O OG  . SER A 1 340 ? 164.012 158.692 162.017 1.00 9.38   ? 340 SER A OG  1 
ATOM   2216 N N   . ILE A 1 341 ? 161.213 159.247 159.147 1.00 14.02  ? 341 ILE A N   1 
ATOM   2217 C CA  . ILE A 1 341 ? 161.307 158.710 157.794 1.00 12.67  ? 341 ILE A CA  1 
ATOM   2218 C C   . ILE A 1 341 ? 162.769 158.659 157.381 1.00 14.48  ? 341 ILE A C   1 
ATOM   2219 O O   . ILE A 1 341 ? 163.512 159.637 157.538 1.00 16.24  ? 341 ILE A O   1 
ATOM   2220 C CB  . ILE A 1 341 ? 160.474 159.559 156.818 1.00 9.17   ? 341 ILE A CB  1 
ATOM   2221 C CG1 . ILE A 1 341 ? 159.101 158.932 156.576 1.00 11.42  ? 341 ILE A CG1 1 
ATOM   2222 C CG2 . ILE A 1 341 ? 161.187 159.723 155.483 1.00 11.29  ? 341 ILE A CG2 1 
ATOM   2223 C CD1 . ILE A 1 341 ? 158.303 158.705 157.825 1.00 19.62  ? 341 ILE A CD1 1 
ATOM   2224 N N   . SER A 1 342 ? 163.197 157.508 156.869 1.00 16.04  ? 342 SER A N   1 
ATOM   2225 C CA  . SER A 1 342 ? 164.564 157.322 156.385 1.00 16.21  ? 342 SER A CA  1 
ATOM   2226 C C   . SER A 1 342 ? 164.534 157.490 154.870 1.00 22.42  ? 342 SER A C   1 
ATOM   2227 O O   . SER A 1 342 ? 164.294 156.542 154.123 1.00 26.05  ? 342 SER A O   1 
ATOM   2228 C CB  . SER A 1 342 ? 165.113 155.962 156.799 1.00 20.48  ? 342 SER A CB  1 
ATOM   2229 O OG  . SER A 1 342 ? 166.502 155.872 156.532 1.00 24.85  ? 342 SER A OG  1 
ATOM   2230 N N   . GLY A 1 343 ? 164.759 158.726 154.425 1.00 18.02  ? 343 GLY A N   1 
ATOM   2231 C CA  . GLY A 1 343 ? 164.685 159.025 152.985 1.00 17.40  ? 343 GLY A CA  1 
ATOM   2232 C C   . GLY A 1 343 ? 163.916 160.313 152.781 1.00 21.88  ? 343 GLY A C   1 
ATOM   2233 O O   . GLY A 1 343 ? 163.699 161.031 153.777 1.00 18.64  ? 343 GLY A O   1 
ATOM   2234 N N   . ASP A 1 344 ? 163.502 160.594 151.547 1.00 20.51  ? 344 ASP A N   1 
ATOM   2235 C CA  . ASP A 1 344 ? 162.804 161.873 151.255 1.00 13.18  ? 344 ASP A CA  1 
ATOM   2236 C C   . ASP A 1 344 ? 161.292 161.670 151.347 1.00 11.52  ? 344 ASP A C   1 
ATOM   2237 O O   . ASP A 1 344 ? 160.851 160.506 151.363 1.00 11.55  ? 344 ASP A O   1 
ATOM   2238 C CB  . ASP A 1 344 ? 163.210 162.405 149.893 1.00 16.74  ? 344 ASP A CB  1 
ATOM   2239 C CG  . ASP A 1 344 ? 164.639 162.087 149.482 1.00 29.31  ? 344 ASP A CG  1 
ATOM   2240 O OD1 . ASP A 1 344 ? 165.559 162.470 150.231 1.00 28.54  ? 344 ASP A OD1 1 
ATOM   2241 O OD2 . ASP A 1 344 ? 164.818 161.462 148.416 1.00 42.30  ? 344 ASP A OD2 1 
ATOM   2242 N N   . LEU A 1 345 ? 160.529 162.762 151.407 1.00 10.63  ? 345 LEU A N   1 
ATOM   2243 C CA  . LEU A 1 345 ? 159.047 162.661 151.413 1.00 8.86   ? 345 LEU A CA  1 
ATOM   2244 C C   . LEU A 1 345 ? 158.512 163.553 150.283 1.00 8.01   ? 345 LEU A C   1 
ATOM   2245 O O   . LEU A 1 345 ? 158.558 164.789 150.436 1.00 10.43  ? 345 LEU A O   1 
ATOM   2246 C CB  . LEU A 1 345 ? 158.492 163.063 152.777 1.00 7.42   ? 345 LEU A CB  1 
ATOM   2247 C CG  . LEU A 1 345 ? 157.470 162.105 153.393 1.00 8.59   ? 345 LEU A CG  1 
ATOM   2248 C CD1 . LEU A 1 345 ? 158.028 160.694 153.414 1.00 11.17  ? 345 LEU A CD1 1 
ATOM   2249 C CD2 . LEU A 1 345 ? 157.105 162.554 154.796 1.00 9.13   ? 345 LEU A CD2 1 
ATOM   2250 N N   . HIS A 1 346 ? 158.047 162.949 149.187 1.00 5.77   ? 346 HIS A N   1 
ATOM   2251 C CA  . HIS A 1 346 ? 157.582 163.739 148.019 1.00 4.31   ? 346 HIS A CA  1 
ATOM   2252 C C   . HIS A 1 346 ? 156.058 163.684 147.927 1.00 6.15   ? 346 HIS A C   1 
ATOM   2253 O O   . HIS A 1 346 ? 155.501 162.572 148.002 1.00 7.86   ? 346 HIS A O   1 
ATOM   2254 C CB  . HIS A 1 346 ? 158.155 163.192 146.709 1.00 9.01   ? 346 HIS A CB  1 
ATOM   2255 C CG  . HIS A 1 346 ? 159.635 163.013 146.660 1.00 11.95  ? 346 HIS A CG  1 
ATOM   2256 N ND1 . HIS A 1 346 ? 160.324 163.100 145.470 1.00 11.74  ? 346 HIS A ND1 1 
ATOM   2257 C CD2 . HIS A 1 346 ? 160.549 162.738 147.596 1.00 15.54  ? 346 HIS A CD2 1 
ATOM   2258 C CE1 . HIS A 1 346 ? 161.612 162.891 145.695 1.00 16.70  ? 346 HIS A CE1 1 
ATOM   2259 N NE2 . HIS A 1 346 ? 161.771 162.668 146.979 1.00 17.26  ? 346 HIS A NE2 1 
ATOM   2260 N N   . ILE A 1 347 ? 155.406 164.841 147.793 1.00 6.45   ? 347 ILE A N   1 
ATOM   2261 C CA  . ILE A 1 347 ? 153.927 164.866 147.578 1.00 4.64   ? 347 ILE A CA  1 
ATOM   2262 C C   . ILE A 1 347 ? 153.710 165.581 146.240 1.00 6.01   ? 347 ILE A C   1 
ATOM   2263 O O   . ILE A 1 347 ? 153.657 166.826 146.245 1.00 8.73   ? 347 ILE A O   1 
ATOM   2264 C CB  . ILE A 1 347 ? 153.178 165.524 148.750 1.00 3.86   ? 347 ILE A CB  1 
ATOM   2265 C CG1 . ILE A 1 347 ? 153.554 164.899 150.096 1.00 3.53   ? 347 ILE A CG1 1 
ATOM   2266 C CG2 . ILE A 1 347 ? 151.670 165.470 148.518 1.00 6.65   ? 347 ILE A CG2 1 
ATOM   2267 C CD1 . ILE A 1 347 ? 154.707 165.580 150.809 1.00 4.46   ? 347 ILE A CD1 1 
ATOM   2268 N N   . LEU A 1 348 ? 153.620 164.825 145.145 1.00 3.92   ? 348 LEU A N   1 
ATOM   2269 C CA  . LEU A 1 348 ? 153.508 165.378 143.807 1.00 4.08   ? 348 LEU A CA  1 
ATOM   2270 C C   . LEU A 1 348 ? 152.056 165.386 143.354 1.00 6.96   ? 348 LEU A C   1 
ATOM   2271 O O   . LEU A 1 348 ? 151.197 164.736 143.956 1.00 9.30   ? 348 LEU A O   1 
ATOM   2272 C CB  . LEU A 1 348 ? 154.373 164.566 142.840 1.00 6.55   ? 348 LEU A CB  1 
ATOM   2273 C CG  . LEU A 1 348 ? 155.857 164.458 143.194 1.00 5.57   ? 348 LEU A CG  1 
ATOM   2274 C CD1 . LEU A 1 348 ? 156.617 163.726 142.103 1.00 4.40   ? 348 LEU A CD1 1 
ATOM   2275 C CD2 . LEU A 1 348 ? 156.454 165.833 143.434 1.00 5.39   ? 348 LEU A CD2 1 
ATOM   2276 N N   . PRO A 1 349 ? 151.737 166.134 142.292 1.00 6.58   ? 349 PRO A N   1 
ATOM   2277 C CA  . PRO A 1 349 ? 150.349 166.142 141.799 1.00 6.50   ? 349 PRO A CA  1 
ATOM   2278 C C   . PRO A 1 349 ? 149.830 164.777 141.381 1.00 9.71   ? 349 PRO A C   1 
ATOM   2279 O O   . PRO A 1 349 ? 148.614 164.555 141.424 1.00 16.21  ? 349 PRO A O   1 
ATOM   2280 C CB  . PRO A 1 349 ? 150.412 167.110 140.611 1.00 8.02   ? 349 PRO A CB  1 
ATOM   2281 C CG  . PRO A 1 349 ? 151.527 168.028 140.949 1.00 5.44   ? 349 PRO A CG  1 
ATOM   2282 C CD  . PRO A 1 349 ? 152.550 167.178 141.642 1.00 5.70   ? 349 PRO A CD  1 
ATOM   2283 N N   . VAL A 1 350 ? 150.737 163.868 141.014 1.00 8.06   ? 350 VAL A N   1 
ATOM   2284 C CA  . VAL A 1 350 ? 150.338 162.496 140.576 1.00 9.82   ? 350 VAL A CA  1 
ATOM   2285 C C   . VAL A 1 350 ? 149.654 161.769 141.742 1.00 14.27  ? 350 VAL A C   1 
ATOM   2286 O O   . VAL A 1 350 ? 148.875 160.838 141.471 1.00 30.00  ? 350 VAL A O   1 
ATOM   2287 C CB  . VAL A 1 350 ? 151.532 161.674 140.057 1.00 10.50  ? 350 VAL A CB  1 
ATOM   2288 C CG1 . VAL A 1 350 ? 151.516 161.532 138.541 1.00 15.37  ? 350 VAL A CG1 1 
ATOM   2289 C CG2 . VAL A 1 350 ? 152.863 162.219 140.557 1.00 10.23  ? 350 VAL A CG2 1 
ATOM   2290 N N   . ALA A 1 351 ? 149.954 162.159 142.982 1.00 9.85   ? 351 ALA A N   1 
ATOM   2291 C CA  . ALA A 1 351 ? 149.348 161.495 144.131 1.00 12.52  ? 351 ALA A CA  1 
ATOM   2292 C C   . ALA A 1 351 ? 147.836 161.682 144.134 1.00 16.45  ? 351 ALA A C   1 
ATOM   2293 O O   . ALA A 1 351 ? 147.078 160.708 144.207 1.00 22.97  ? 351 ALA A O   1 
ATOM   2294 C CB  . ALA A 1 351 ? 149.964 162.024 145.426 1.00 11.21  ? 351 ALA A CB  1 
ATOM   2295 N N   . PHE A 1 352 ? 147.379 162.929 144.029 1.00 15.49  ? 352 PHE A N   1 
ATOM   2296 C CA  . PHE A 1 352 ? 145.954 163.229 144.061 1.00 14.63  ? 352 PHE A CA  1 
ATOM   2297 C C   . PHE A 1 352 ? 145.282 163.093 142.704 1.00 19.26  ? 352 PHE A C   1 
ATOM   2298 O O   . PHE A 1 352 ? 144.069 162.858 142.651 1.00 29.30  ? 352 PHE A O   1 
ATOM   2299 C CB  . PHE A 1 352 ? 145.728 164.642 144.603 1.00 12.76  ? 352 PHE A CB  1 
ATOM   2300 C CG  . PHE A 1 352 ? 146.617 164.989 145.757 1.00 9.94   ? 352 PHE A CG  1 
ATOM   2301 C CD1 . PHE A 1 352 ? 146.310 164.559 147.034 1.00 11.61  ? 352 PHE A CD1 1 
ATOM   2302 C CD2 . PHE A 1 352 ? 147.766 165.735 145.565 1.00 8.34   ? 352 PHE A CD2 1 
ATOM   2303 C CE1 . PHE A 1 352 ? 147.126 164.869 148.097 1.00 11.37  ? 352 PHE A CE1 1 
ATOM   2304 C CE2 . PHE A 1 352 ? 148.587 166.048 146.626 1.00 8.53   ? 352 PHE A CE2 1 
ATOM   2305 C CZ  . PHE A 1 352 ? 148.266 165.615 147.894 1.00 10.09  ? 352 PHE A CZ  1 
ATOM   2306 N N   . ARG A 1 353 ? 146.043 163.191 141.612 1.00 19.97  ? 353 ARG A N   1 
ATOM   2307 C CA  . ARG A 1 353 ? 145.466 162.997 140.254 1.00 17.43  ? 353 ARG A CA  1 
ATOM   2308 C C   . ARG A 1 353 ? 145.387 161.511 139.928 1.00 18.34  ? 353 ARG A C   1 
ATOM   2309 O O   . ARG A 1 353 ? 144.456 161.103 139.207 1.00 30.42  ? 353 ARG A O   1 
ATOM   2310 C CB  . ARG A 1 353 ? 146.347 163.552 139.135 1.00 13.40  ? 353 ARG A CB  1 
ATOM   2311 C CG  . ARG A 1 353 ? 145.752 163.371 137.747 1.00 10.95  ? 353 ARG A CG  1 
ATOM   2312 C CD  . ARG A 1 353 ? 146.791 163.638 136.683 1.00 18.59  ? 353 ARG A CD  1 
ATOM   2313 N NE  . ARG A 1 353 ? 147.920 164.379 137.252 1.00 15.89  ? 353 ARG A NE  1 
ATOM   2314 C CZ  . ARG A 1 353 ? 149.179 163.995 137.151 1.00 14.14  ? 353 ARG A CZ  1 
ATOM   2315 N NH1 . ARG A 1 353 ? 149.480 162.898 136.483 1.00 9.69   ? 353 ARG A NH1 1 
ATOM   2316 N NH2 . ARG A 1 353 ? 150.130 164.716 137.712 1.00 13.12  ? 353 ARG A NH2 1 
ATOM   2317 N N   . GLY A 1 354 ? 146.308 160.727 140.468 1.00 16.56  ? 354 GLY A N   1 
ATOM   2318 C CA  . GLY A 1 354 ? 146.389 159.326 140.123 1.00 16.83  ? 354 GLY A CA  1 
ATOM   2319 C C   . GLY A 1 354 ? 147.307 159.085 138.939 1.00 19.50  ? 354 GLY A C   1 
ATOM   2320 O O   . GLY A 1 354 ? 147.580 159.969 138.128 1.00 23.29  ? 354 GLY A O   1 
ATOM   2321 N N   . ASP A 1 355 ? 147.802 157.856 138.853 1.00 16.53  ? 355 ASP A N   1 
ATOM   2322 C CA  . ASP A 1 355 ? 148.685 157.455 137.770 1.00 8.97   ? 355 ASP A CA  1 
ATOM   2323 C C   . ASP A 1 355 ? 148.195 156.148 137.172 1.00 14.04  ? 355 ASP A C   1 
ATOM   2324 O O   . ASP A 1 355 ? 147.813 155.226 137.899 1.00 17.81  ? 355 ASP A O   1 
ATOM   2325 C CB  . ASP A 1 355 ? 150.128 157.303 138.251 1.00 10.91  ? 355 ASP A CB  1 
ATOM   2326 C CG  . ASP A 1 355 ? 151.134 157.546 137.149 1.00 8.70   ? 355 ASP A CG  1 
ATOM   2327 O OD1 . ASP A 1 355 ? 150.764 158.173 136.136 1.00 7.01   ? 355 ASP A OD1 1 
ATOM   2328 O OD2 . ASP A 1 355 ? 152.294 157.113 137.297 1.00 10.06  ? 355 ASP A OD2 1 
ATOM   2329 N N   . SER A 1 356 ? 148.197 156.075 135.841 1.00 15.55  ? 356 SER A N   1 
ATOM   2330 C CA  . SER A 1 356 ? 147.739 154.841 135.158 1.00 7.33   ? 356 SER A CA  1 
ATOM   2331 C C   . SER A 1 356 ? 148.939 153.920 134.895 1.00 10.31  ? 356 SER A C   1 
ATOM   2332 O O   . SER A 1 356 ? 148.793 152.703 135.112 1.00 16.86  ? 356 SER A O   1 
ATOM   2333 C CB  . SER A 1 356 ? 146.989 155.168 133.902 1.00 7.20   ? 356 SER A CB  1 
ATOM   2334 O OG  . SER A 1 356 ? 147.655 156.177 133.159 1.00 9.40   ? 356 SER A OG  1 
ATOM   2335 N N   . PHE A 1 357 ? 150.077 154.469 134.462 1.00 10.03  ? 357 PHE A N   1 
ATOM   2336 C CA  . PHE A 1 357 ? 151.209 153.607 134.141 1.00 5.61   ? 357 PHE A CA  1 
ATOM   2337 C C   . PHE A 1 357 ? 151.658 152.806 135.355 1.00 9.66   ? 357 PHE A C   1 
ATOM   2338 O O   . PHE A 1 357 ? 151.962 151.613 135.243 1.00 20.99  ? 357 PHE A O   1 
ATOM   2339 C CB  . PHE A 1 357 ? 152.370 154.429 133.591 1.00 4.63   ? 357 PHE A CB  1 
ATOM   2340 C CG  . PHE A 1 357 ? 153.615 153.626 133.363 1.00 5.95   ? 357 PHE A CG  1 
ATOM   2341 C CD1 . PHE A 1 357 ? 153.743 152.829 132.238 1.00 9.48   ? 357 PHE A CD1 1 
ATOM   2342 C CD2 . PHE A 1 357 ? 154.654 153.659 134.275 1.00 7.70   ? 357 PHE A CD2 1 
ATOM   2343 C CE1 . PHE A 1 357 ? 154.884 152.087 132.026 1.00 13.06  ? 357 PHE A CE1 1 
ATOM   2344 C CE2 . PHE A 1 357 ? 155.795 152.918 134.069 1.00 7.90   ? 357 PHE A CE2 1 
ATOM   2345 C CZ  . PHE A 1 357 ? 155.910 152.131 132.943 1.00 15.97  ? 357 PHE A CZ  1 
ATOM   2346 N N   . THR A 1 358 ? 151.714 153.443 136.519 1.00 8.86   ? 358 THR A N   1 
ATOM   2347 C CA  . THR A 1 358 ? 152.040 152.750 137.755 1.00 10.35  ? 358 THR A CA  1 
ATOM   2348 C C   . THR A 1 358 ? 150.820 152.107 138.400 1.00 17.22  ? 358 THR A C   1 
ATOM   2349 O O   . THR A 1 358 ? 150.953 151.487 139.460 1.00 24.52  ? 358 THR A O   1 
ATOM   2350 C CB  . THR A 1 358 ? 152.711 153.711 138.740 1.00 9.41   ? 358 THR A CB  1 
ATOM   2351 O OG1 . THR A 1 358 ? 151.764 154.693 139.174 1.00 16.34  ? 358 THR A OG1 1 
ATOM   2352 C CG2 . THR A 1 358 ? 153.890 154.410 138.080 1.00 8.36   ? 358 THR A CG2 1 
ATOM   2353 N N   . HIS A 1 359 ? 149.643 152.239 137.781 1.00 13.70  ? 359 HIS A N   1 
ATOM   2354 C CA  . HIS A 1 359 ? 148.419 151.571 138.230 1.00 13.29  ? 359 HIS A CA  1 
ATOM   2355 C C   . HIS A 1 359 ? 148.059 151.959 139.661 1.00 13.28  ? 359 HIS A C   1 
ATOM   2356 O O   . HIS A 1 359 ? 147.772 151.106 140.502 1.00 21.53  ? 359 HIS A O   1 
ATOM   2357 C CB  . HIS A 1 359 ? 148.545 150.053 138.097 1.00 16.78  ? 359 HIS A CB  1 
ATOM   2358 C CG  . HIS A 1 359 ? 149.201 149.618 136.826 1.00 12.67  ? 359 HIS A CG  1 
ATOM   2359 N ND1 . HIS A 1 359 ? 150.471 149.086 136.789 1.00 9.74   ? 359 HIS A ND1 1 
ATOM   2360 C CD2 . HIS A 1 359 ? 148.765 149.644 135.546 1.00 8.60   ? 359 HIS A CD2 1 
ATOM   2361 C CE1 . HIS A 1 359 ? 150.790 148.801 135.539 1.00 11.28  ? 359 HIS A CE1 1 
ATOM   2362 N NE2 . HIS A 1 359 ? 149.771 149.129 134.765 1.00 11.56  ? 359 HIS A NE2 1 
ATOM   2363 N N   . THR A 1 360 ? 148.074 153.260 139.942 1.00 12.39  ? 360 THR A N   1 
ATOM   2364 C CA  . THR A 1 360 ? 147.799 153.751 141.283 1.00 17.79  ? 360 THR A CA  1 
ATOM   2365 C C   . THR A 1 360 ? 146.579 154.657 141.276 1.00 19.41  ? 360 THR A C   1 
ATOM   2366 O O   . THR A 1 360 ? 146.537 155.628 140.507 1.00 16.90  ? 360 THR A O   1 
ATOM   2367 C CB  . THR A 1 360 ? 149.011 154.492 141.833 1.00 16.73  ? 360 THR A CB  1 
ATOM   2368 O OG1 . THR A 1 360 ? 149.261 155.656 141.037 1.00 17.32  ? 360 THR A OG1 1 
ATOM   2369 C CG2 . THR A 1 360 ? 150.218 153.590 141.770 1.00 18.22  ? 360 THR A CG2 1 
ATOM   2370 N N   . PRO A 1 361 ? 145.577 154.383 142.104 1.00 21.22  ? 361 PRO A N   1 
ATOM   2371 C CA  . PRO A 1 361 ? 144.395 155.244 142.159 1.00 21.31  ? 361 PRO A CA  1 
ATOM   2372 C C   . PRO A 1 361 ? 144.738 156.591 142.766 1.00 27.47  ? 361 PRO A C   1 
ATOM   2373 O O   . PRO A 1 361 ? 145.723 156.711 143.510 1.00 35.27  ? 361 PRO A O   1 
ATOM   2374 C CB  . PRO A 1 361 ? 143.428 154.456 143.054 1.00 28.16  ? 361 PRO A CB  1 
ATOM   2375 C CG  . PRO A 1 361 ? 144.318 153.634 143.921 1.00 30.21  ? 361 PRO A CG  1 
ATOM   2376 C CD  . PRO A 1 361 ? 145.502 153.271 143.069 1.00 24.81  ? 361 PRO A CD  1 
ATOM   2377 N N   . PRO A 1 362 ? 143.963 157.632 142.460 1.00 30.49  ? 362 PRO A N   1 
ATOM   2378 C CA  . PRO A 1 362 ? 144.224 158.944 143.064 1.00 25.67  ? 362 PRO A CA  1 
ATOM   2379 C C   . PRO A 1 362 ? 144.133 158.884 144.581 1.00 28.99  ? 362 PRO A C   1 
ATOM   2380 O O   . PRO A 1 362 ? 143.271 158.208 145.146 1.00 34.68  ? 362 PRO A O   1 
ATOM   2381 C CB  . PRO A 1 362 ? 143.128 159.836 142.468 1.00 23.18  ? 362 PRO A CB  1 
ATOM   2382 C CG  . PRO A 1 362 ? 142.082 158.892 141.971 1.00 28.89  ? 362 PRO A CG  1 
ATOM   2383 C CD  . PRO A 1 362 ? 142.819 157.668 141.536 1.00 32.03  ? 362 PRO A CD  1 
ATOM   2384 N N   . LEU A 1 363 ? 145.035 159.607 145.240 1.00 29.43  ? 363 LEU A N   1 
ATOM   2385 C CA  . LEU A 1 363 ? 145.095 159.620 146.698 1.00 31.03  ? 363 LEU A CA  1 
ATOM   2386 C C   . LEU A 1 363 ? 144.043 160.585 147.228 1.00 34.85  ? 363 LEU A C   1 
ATOM   2387 O O   . LEU A 1 363 ? 144.119 161.794 146.985 1.00 35.02  ? 363 LEU A O   1 
ATOM   2388 C CB  . LEU A 1 363 ? 146.490 160.013 147.174 1.00 27.00  ? 363 LEU A CB  1 
ATOM   2389 C CG  . LEU A 1 363 ? 146.626 160.432 148.637 1.00 26.37  ? 363 LEU A CG  1 
ATOM   2390 C CD1 . LEU A 1 363 ? 146.372 159.247 149.547 1.00 27.25  ? 363 LEU A CD1 1 
ATOM   2391 C CD2 . LEU A 1 363 ? 148.000 161.027 148.898 1.00 20.72  ? 363 LEU A CD2 1 
ATOM   2392 N N   . ASP A 1 364 ? 143.056 160.053 147.940 1.00 37.76  ? 364 ASP A N   1 
ATOM   2393 C CA  . ASP A 1 364 ? 142.064 160.906 148.571 1.00 39.48  ? 364 ASP A CA  1 
ATOM   2394 C C   . ASP A 1 364 ? 142.732 161.749 149.656 1.00 44.49  ? 364 ASP A C   1 
ATOM   2395 O O   . ASP A 1 364 ? 143.566 161.240 150.411 1.00 47.03  ? 364 ASP A O   1 
ATOM   2396 C CB  . ASP A 1 364 ? 140.935 160.064 149.167 1.00 49.19  ? 364 ASP A CB  1 
ATOM   2397 C CG  . ASP A 1 364 ? 139.700 160.882 149.484 1.00 65.71  ? 364 ASP A CG  1 
ATOM   2398 O OD1 . ASP A 1 364 ? 139.119 161.473 148.550 1.00 71.12  ? 364 ASP A OD1 1 
ATOM   2399 O OD2 . ASP A 1 364 ? 139.305 160.929 150.667 1.00 65.17  ? 364 ASP A OD2 1 
ATOM   2400 N N   . PRO A 1 365 ? 142.398 163.038 149.749 1.00 44.52  ? 365 PRO A N   1 
ATOM   2401 C CA  . PRO A 1 365 ? 143.124 163.922 150.677 1.00 36.96  ? 365 PRO A CA  1 
ATOM   2402 C C   . PRO A 1 365 ? 143.039 163.505 152.135 1.00 43.63  ? 365 PRO A C   1 
ATOM   2403 O O   . PRO A 1 365 ? 143.931 163.864 152.914 1.00 45.75  ? 365 PRO A O   1 
ATOM   2404 C CB  . PRO A 1 365 ? 142.458 165.286 150.449 1.00 37.31  ? 365 PRO A CB  1 
ATOM   2405 C CG  . PRO A 1 365 ? 141.900 165.204 149.067 1.00 38.78  ? 365 PRO A CG  1 
ATOM   2406 C CD  . PRO A 1 365 ? 141.448 163.783 148.906 1.00 44.22  ? 365 PRO A CD  1 
ATOM   2407 N N   . GLN A 1 366 ? 142.002 162.766 152.535 1.00 51.20  ? 366 GLN A N   1 
ATOM   2408 C CA  . GLN A 1 366 ? 141.857 162.391 153.937 1.00 52.60  ? 366 GLN A CA  1 
ATOM   2409 C C   . GLN A 1 366 ? 142.924 161.407 154.399 1.00 46.48  ? 366 GLN A C   1 
ATOM   2410 O O   . GLN A 1 366 ? 143.144 161.277 155.608 1.00 43.32  ? 366 GLN A O   1 
ATOM   2411 C CB  . GLN A 1 366 ? 140.465 161.805 154.184 1.00 55.93  ? 366 GLN A CB  1 
ATOM   2412 C CG  . GLN A 1 366 ? 139.350 162.512 153.428 1.00 57.67  ? 366 GLN A CG  1 
ATOM   2413 C CD  . GLN A 1 366 ? 139.032 163.887 153.989 1.00 65.97  ? 366 GLN A CD  1 
ATOM   2414 O OE1 . GLN A 1 366 ? 139.385 164.200 155.125 1.00 63.13  ? 366 GLN A OE1 1 
ATOM   2415 N NE2 . GLN A 1 366 ? 138.374 164.718 153.188 1.00 64.30  ? 366 GLN A NE2 1 
ATOM   2416 N N   . GLU A 1 367 ? 143.591 160.713 153.477 1.00 43.34  ? 367 GLU A N   1 
ATOM   2417 C CA  . GLU A 1 367 ? 144.659 159.795 153.853 1.00 39.55  ? 367 GLU A CA  1 
ATOM   2418 C C   . GLU A 1 367 ? 145.995 160.493 154.065 1.00 40.87  ? 367 GLU A C   1 
ATOM   2419 O O   . GLU A 1 367 ? 146.958 159.837 154.473 1.00 38.41  ? 367 GLU A O   1 
ATOM   2420 C CB  . GLU A 1 367 ? 144.818 158.698 152.797 1.00 43.74  ? 367 GLU A CB  1 
ATOM   2421 C CG  . GLU A 1 367 ? 143.804 157.573 152.910 1.00 50.31  ? 367 GLU A CG  1 
ATOM   2422 C CD  . GLU A 1 367 ? 142.665 157.719 151.925 1.00 56.68  ? 367 GLU A CD  1 
ATOM   2423 O OE1 . GLU A 1 367 ? 142.898 158.277 150.833 1.00 52.63  ? 367 GLU A OE1 1 
ATOM   2424 O OE2 . GLU A 1 367 ? 141.539 157.279 152.241 1.00 59.20  ? 367 GLU A OE2 1 
ATOM   2425 N N   . LEU A 1 368 ? 146.080 161.798 153.798 1.00 42.63  ? 368 LEU A N   1 
ATOM   2426 C CA  . LEU A 1 368 ? 147.316 162.529 154.043 1.00 37.00  ? 368 LEU A CA  1 
ATOM   2427 C C   . LEU A 1 368 ? 147.597 162.707 155.529 1.00 38.26  ? 368 LEU A C   1 
ATOM   2428 O O   . LEU A 1 368 ? 148.726 163.046 155.897 1.00 38.16  ? 368 LEU A O   1 
ATOM   2429 C CB  . LEU A 1 368 ? 147.266 163.894 153.359 1.00 27.04  ? 368 LEU A CB  1 
ATOM   2430 C CG  . LEU A 1 368 ? 147.844 163.955 151.947 1.00 22.30  ? 368 LEU A CG  1 
ATOM   2431 C CD1 . LEU A 1 368 ? 147.903 165.391 151.475 1.00 17.02  ? 368 LEU A CD1 1 
ATOM   2432 C CD2 . LEU A 1 368 ? 149.221 163.315 151.900 1.00 21.18  ? 368 LEU A CD2 1 
ATOM   2433 N N   . ASP A 1 369 ? 146.601 162.479 156.387 1.00 40.23  ? 369 ASP A N   1 
ATOM   2434 C CA  . ASP A 1 369 ? 146.800 162.576 157.827 1.00 35.32  ? 369 ASP A CA  1 
ATOM   2435 C C   . ASP A 1 369 ? 147.660 161.446 158.376 1.00 35.91  ? 369 ASP A C   1 
ATOM   2436 O O   . ASP A 1 369 ? 148.023 161.485 159.556 1.00 38.83  ? 369 ASP A O   1 
ATOM   2437 C CB  . ASP A 1 369 ? 145.448 162.598 158.542 1.00 43.97  ? 369 ASP A CB  1 
ATOM   2438 C CG  . ASP A 1 369 ? 144.464 163.551 157.894 1.00 52.90  ? 369 ASP A CG  1 
ATOM   2439 O OD1 . ASP A 1 369 ? 144.895 164.378 157.063 1.00 51.47  ? 369 ASP A OD1 1 
ATOM   2440 O OD2 . ASP A 1 369 ? 143.259 163.475 158.215 1.00 61.51  ? 369 ASP A OD2 1 
ATOM   2441 N N   . ILE A 1 370 ? 147.976 160.440 157.557 1.00 33.16  ? 370 ILE A N   1 
ATOM   2442 C CA  . ILE A 1 370 ? 148.899 159.389 157.971 1.00 34.31  ? 370 ILE A CA  1 
ATOM   2443 C C   . ILE A 1 370 ? 150.268 159.976 158.292 1.00 32.70  ? 370 ILE A C   1 
ATOM   2444 O O   . ILE A 1 370 ? 150.959 159.505 159.204 1.00 33.25  ? 370 ILE A O   1 
ATOM   2445 C CB  . ILE A 1 370 ? 148.975 158.299 156.880 1.00 40.82  ? 370 ILE A CB  1 
ATOM   2446 C CG1 . ILE A 1 370 ? 147.959 157.186 157.153 1.00 39.59  ? 370 ILE A CG1 1 
ATOM   2447 C CG2 . ILE A 1 370 ? 150.381 157.729 156.757 1.00 41.17  ? 370 ILE A CG2 1 
ATOM   2448 C CD1 . ILE A 1 370 ? 146.519 157.591 156.925 1.00 40.43  ? 370 ILE A CD1 1 
ATOM   2449 N N   . LEU A 1 371 ? 150.668 161.027 157.576 1.00 30.89  ? 371 LEU A N   1 
ATOM   2450 C CA  . LEU A 1 371 ? 151.959 161.669 157.783 1.00 23.89  ? 371 LEU A CA  1 
ATOM   2451 C C   . LEU A 1 371 ? 152.003 162.543 159.030 1.00 18.59  ? 371 LEU A C   1 
ATOM   2452 O O   . LEU A 1 371 ? 153.064 163.098 159.335 1.00 17.98  ? 371 LEU A O   1 
ATOM   2453 C CB  . LEU A 1 371 ? 152.331 162.509 156.558 1.00 22.70  ? 371 LEU A CB  1 
ATOM   2454 C CG  . LEU A 1 371 ? 152.412 161.767 155.224 1.00 17.88  ? 371 LEU A CG  1 
ATOM   2455 C CD1 . LEU A 1 371 ? 152.223 162.732 154.066 1.00 19.39  ? 371 LEU A CD1 1 
ATOM   2456 C CD2 . LEU A 1 371 ? 153.735 161.031 155.102 1.00 15.39  ? 371 LEU A CD2 1 
ATOM   2457 N N   . LYS A 1 372 ? 150.888 162.689 159.749 1.00 22.28  ? 372 LYS A N   1 
ATOM   2458 C CA  . LYS A 1 372 ? 150.882 163.470 160.980 1.00 24.01  ? 372 LYS A CA  1 
ATOM   2459 C C   . LYS A 1 372 ? 151.784 162.883 162.056 1.00 28.82  ? 372 LYS A C   1 
ATOM   2460 O O   . LYS A 1 372 ? 152.140 163.597 162.999 1.00 33.09  ? 372 LYS A O   1 
ATOM   2461 C CB  . LYS A 1 372 ? 149.455 163.590 161.519 1.00 28.52  ? 372 LYS A CB  1 
ATOM   2462 C CG  . LYS A 1 372 ? 148.679 164.778 160.976 1.00 30.51  ? 372 LYS A CG  1 
ATOM   2463 C CD  . LYS A 1 372 ? 147.204 164.675 161.326 1.00 40.81  ? 372 LYS A CD  1 
ATOM   2464 C CE  . LYS A 1 372 ? 146.453 165.939 160.943 1.00 49.22  ? 372 LYS A CE  1 
ATOM   2465 N NZ  . LYS A 1 372 ? 145.847 166.605 162.129 1.00 42.92  ? 372 LYS A NZ  1 
ATOM   2466 N N   . THR A 1 373 ? 152.156 161.609 161.941 1.00 29.33  ? 373 THR A N   1 
ATOM   2467 C CA  . THR A 1 373 ? 153.042 160.968 162.901 1.00 21.89  ? 373 THR A CA  1 
ATOM   2468 C C   . THR A 1 373 ? 154.511 161.297 162.670 1.00 20.98  ? 373 THR A C   1 
ATOM   2469 O O   . THR A 1 373 ? 155.301 161.241 163.620 1.00 28.02  ? 373 THR A O   1 
ATOM   2470 C CB  . THR A 1 373 ? 152.846 159.448 162.852 1.00 27.29  ? 373 THR A CB  1 
ATOM   2471 O OG1 . THR A 1 373 ? 151.447 159.149 162.780 1.00 34.85  ? 373 THR A OG1 1 
ATOM   2472 C CG2 . THR A 1 373 ? 153.429 158.789 164.087 1.00 31.39  ? 373 THR A CG2 1 
ATOM   2473 N N   . VAL A 1 374 ? 154.890 161.652 161.444 1.00 20.28  ? 374 VAL A N   1 
ATOM   2474 C CA  . VAL A 1 374 ? 156.286 161.893 161.091 1.00 15.15  ? 374 VAL A CA  1 
ATOM   2475 C C   . VAL A 1 374 ? 156.825 163.089 161.864 1.00 13.02  ? 374 VAL A C   1 
ATOM   2476 O O   . VAL A 1 374 ? 156.357 164.219 161.688 1.00 26.06  ? 374 VAL A O   1 
ATOM   2477 C CB  . VAL A 1 374 ? 156.441 162.110 159.575 1.00 13.91  ? 374 VAL A CB  1 
ATOM   2478 C CG1 . VAL A 1 374 ? 157.910 162.141 159.191 1.00 11.39  ? 374 VAL A CG1 1 
ATOM   2479 C CG2 . VAL A 1 374 ? 155.701 161.028 158.808 1.00 15.83  ? 374 VAL A CG2 1 
ATOM   2480 N N   . LYS A 1 375 ? 157.812 162.845 162.724 1.00 9.94   ? 375 LYS A N   1 
ATOM   2481 C CA  . LYS A 1 375 ? 158.453 163.896 163.502 1.00 10.66  ? 375 LYS A CA  1 
ATOM   2482 C C   . LYS A 1 375 ? 159.893 164.152 163.084 1.00 8.89   ? 375 LYS A C   1 
ATOM   2483 O O   . LYS A 1 375 ? 160.562 164.986 163.701 1.00 15.38  ? 375 LYS A O   1 
ATOM   2484 C CB  . LYS A 1 375 ? 158.407 163.551 164.995 1.00 13.83  ? 375 LYS A CB  1 
ATOM   2485 C CG  . LYS A 1 375 ? 157.101 163.913 165.680 1.00 22.32  ? 375 LYS A CG  1 
ATOM   2486 C CD  . LYS A 1 375 ? 156.508 162.722 166.413 1.00 35.93  ? 375 LYS A CD  1 
ATOM   2487 C CE  . LYS A 1 375 ? 155.222 163.101 167.130 1.00 46.24  ? 375 LYS A CE  1 
ATOM   2488 N NZ  . LYS A 1 375 ? 154.020 162.859 166.285 1.00 37.15  ? 375 LYS A NZ  1 
ATOM   2489 N N   . GLU A 1 376 ? 160.358 163.469 162.036 1.00 10.00  ? 376 GLU A N   1 
ATOM   2490 C CA  . GLU A 1 376 ? 161.723 163.686 161.495 1.00 11.89  ? 376 GLU A CA  1 
ATOM   2491 C C   . GLU A 1 376 ? 161.785 163.124 160.072 1.00 10.45  ? 376 GLU A C   1 
ATOM   2492 O O   . GLU A 1 376 ? 161.038 162.176 159.800 1.00 12.52  ? 376 GLU A O   1 
ATOM   2493 C CB  . GLU A 1 376 ? 162.799 163.022 162.353 1.00 15.19  ? 376 GLU A CB  1 
ATOM   2494 C CG  . GLU A 1 376 ? 164.202 163.162 161.769 1.00 18.82  ? 376 GLU A CG  1 
ATOM   2495 C CD  . GLU A 1 376 ? 165.311 162.620 162.649 1.00 32.65  ? 376 GLU A CD  1 
ATOM   2496 O OE1 . GLU A 1 376 ? 165.022 162.157 163.772 1.00 38.63  ? 376 GLU A OE1 1 
ATOM   2497 O OE2 . GLU A 1 376 ? 166.471 162.646 162.192 1.00 35.15  ? 376 GLU A OE2 1 
ATOM   2498 N N   . ILE A 1 377 ? 162.591 163.717 159.193 1.00 9.51   ? 377 ILE A N   1 
ATOM   2499 C CA  . ILE A 1 377 ? 162.791 163.216 157.801 1.00 11.59  ? 377 ILE A CA  1 
ATOM   2500 C C   . ILE A 1 377 ? 164.292 163.348 157.521 1.00 16.63  ? 377 ILE A C   1 
ATOM   2501 O O   . ILE A 1 377 ? 164.754 164.496 157.380 1.00 21.05  ? 377 ILE A O   1 
ATOM   2502 C CB  . ILE A 1 377 ? 161.931 163.984 156.777 1.00 9.48   ? 377 ILE A CB  1 
ATOM   2503 C CG1 . ILE A 1 377 ? 160.439 163.905 157.111 1.00 6.76   ? 377 ILE A CG1 1 
ATOM   2504 C CG2 . ILE A 1 377 ? 162.213 163.498 155.354 1.00 10.67  ? 377 ILE A CG2 1 
ATOM   2505 C CD1 . ILE A 1 377 ? 159.556 164.786 156.245 1.00 6.59   ? 377 ILE A CD1 1 
ATOM   2506 N N   . THR A 1 378 ? 165.030 162.239 157.455 1.00 18.77  ? 378 THR A N   1 
ATOM   2507 C CA  . THR A 1 378 ? 166.495 162.267 157.260 1.00 18.62  ? 378 THR A CA  1 
ATOM   2508 C C   . THR A 1 378 ? 166.784 162.789 155.870 1.00 22.28  ? 378 THR A C   1 
ATOM   2509 O O   . THR A 1 378 ? 167.895 163.314 155.677 1.00 24.77  ? 378 THR A O   1 
ATOM   2510 C CB  . THR A 1 378 ? 167.102 160.888 157.507 1.00 19.79  ? 378 THR A CB  1 
ATOM   2511 O OG1 . THR A 1 378 ? 166.591 160.050 156.479 1.00 24.44  ? 378 THR A OG1 1 
ATOM   2512 C CG2 . THR A 1 378 ? 166.747 160.334 158.876 1.00 21.58  ? 378 THR A CG2 1 
ATOM   2513 N N   . GLY A 1 379 ? 165.841 162.674 154.927 1.00 19.13  ? 379 GLY A N   1 
ATOM   2514 C CA  . GLY A 1 379 ? 166.000 163.248 153.577 1.00 17.31  ? 379 GLY A CA  1 
ATOM   2515 C C   . GLY A 1 379 ? 165.399 164.637 153.504 1.00 18.68  ? 379 GLY A C   1 
ATOM   2516 O O   . GLY A 1 379 ? 165.615 165.419 154.448 1.00 18.56  ? 379 GLY A O   1 
ATOM   2517 N N   . PHE A 1 380 ? 164.656 164.933 152.433 1.00 21.30  ? 380 PHE A N   1 
ATOM   2518 C CA  . PHE A 1 380 ? 164.043 166.278 152.261 1.00 13.68  ? 380 PHE A CA  1 
ATOM   2519 C C   . PHE A 1 380 ? 162.517 166.159 152.217 1.00 9.80   ? 380 PHE A C   1 
ATOM   2520 O O   . PHE A 1 380 ? 162.001 165.041 152.024 1.00 13.73  ? 380 PHE A O   1 
ATOM   2521 C CB  . PHE A 1 380 ? 164.618 166.939 151.006 1.00 16.15  ? 380 PHE A CB  1 
ATOM   2522 C CG  . PHE A 1 380 ? 164.135 166.413 149.662 1.00 23.88  ? 380 PHE A CG  1 
ATOM   2523 C CD1 . PHE A 1 380 ? 162.991 166.927 149.064 1.00 23.91  ? 380 PHE A CD1 1 
ATOM   2524 C CD2 . PHE A 1 380 ? 164.848 165.436 148.980 1.00 28.52  ? 380 PHE A CD2 1 
ATOM   2525 C CE1 . PHE A 1 380 ? 162.563 166.454 147.835 1.00 19.19  ? 380 PHE A CE1 1 
ATOM   2526 C CE2 . PHE A 1 380 ? 164.417 164.971 147.749 1.00 28.44  ? 380 PHE A CE2 1 
ATOM   2527 C CZ  . PHE A 1 380 ? 163.276 165.480 147.180 1.00 24.44  ? 380 PHE A CZ  1 
ATOM   2528 N N   . LEU A 1 381 ? 161.812 167.279 152.406 1.00 8.53   ? 381 LEU A N   1 
ATOM   2529 C CA  . LEU A 1 381 ? 160.326 167.281 152.316 1.00 7.87   ? 381 LEU A CA  1 
ATOM   2530 C C   . LEU A 1 381 ? 159.910 168.107 151.089 1.00 9.95   ? 381 LEU A C   1 
ATOM   2531 O O   . LEU A 1 381 ? 160.121 169.335 151.105 1.00 11.64  ? 381 LEU A O   1 
ATOM   2532 C CB  . LEU A 1 381 ? 159.693 167.830 153.593 1.00 4.95   ? 381 LEU A CB  1 
ATOM   2533 C CG  . LEU A 1 381 ? 158.164 167.920 153.594 1.00 3.29   ? 381 LEU A CG  1 
ATOM   2534 C CD1 . LEU A 1 381 ? 157.557 166.547 153.395 1.00 5.32   ? 381 LEU A CD1 1 
ATOM   2535 C CD2 . LEU A 1 381 ? 157.660 168.548 154.879 1.00 6.22   ? 381 LEU A CD2 1 
ATOM   2536 N N   . LEU A 1 382 ? 159.347 167.454 150.070 1.00 6.77   ? 382 LEU A N   1 
ATOM   2537 C CA  . LEU A 1 382 ? 158.880 168.171 148.857 1.00 5.87   ? 382 LEU A CA  1 
ATOM   2538 C C   . LEU A 1 382 ? 157.350 168.116 148.814 1.00 5.95   ? 382 LEU A C   1 
ATOM   2539 O O   . LEU A 1 382 ? 156.804 167.004 148.687 1.00 6.38   ? 382 LEU A O   1 
ATOM   2540 C CB  . LEU A 1 382 ? 159.494 167.530 147.616 1.00 6.39   ? 382 LEU A CB  1 
ATOM   2541 C CG  . LEU A 1 382 ? 158.945 167.991 146.264 1.00 7.79   ? 382 LEU A CG  1 
ATOM   2542 C CD1 . LEU A 1 382 ? 159.254 169.458 146.032 1.00 9.63   ? 382 LEU A CD1 1 
ATOM   2543 C CD2 . LEU A 1 382 ? 159.551 167.135 145.168 1.00 11.42  ? 382 LEU A CD2 1 
ATOM   2544 N N   . ILE A 1 383 ? 156.691 169.270 148.926 1.00 5.56   ? 383 ILE A N   1 
ATOM   2545 C CA  . ILE A 1 383 ? 155.204 169.314 148.821 1.00 4.72   ? 383 ILE A CA  1 
ATOM   2546 C C   . ILE A 1 383 ? 154.856 170.124 147.565 1.00 7.55   ? 383 ILE A C   1 
ATOM   2547 O O   . ILE A 1 383 ? 154.678 171.351 147.683 1.00 10.97  ? 383 ILE A O   1 
ATOM   2548 C CB  . ILE A 1 383 ? 154.587 169.910 150.096 1.00 3.28   ? 383 ILE A CB  1 
ATOM   2549 C CG1 . ILE A 1 383 ? 155.291 169.390 151.344 1.00 3.58   ? 383 ILE A CG1 1 
ATOM   2550 C CG2 . ILE A 1 383 ? 153.083 169.648 150.141 1.00 5.20   ? 383 ILE A CG2 1 
ATOM   2551 C CD1 . ILE A 1 383 ? 154.958 170.157 152.608 1.00 4.44   ? 383 ILE A CD1 1 
ATOM   2552 N N   . GLN A 1 384 ? 154.787 169.458 146.411 1.00 6.90   ? 384 GLN A N   1 
ATOM   2553 C CA  . GLN A 1 384 ? 154.504 170.158 145.134 1.00 5.58   ? 384 GLN A CA  1 
ATOM   2554 C C   . GLN A 1 384 ? 152.992 170.164 144.888 1.00 7.39   ? 384 GLN A C   1 
ATOM   2555 O O   . GLN A 1 384 ? 152.553 170.819 143.922 1.00 13.82  ? 384 GLN A O   1 
ATOM   2556 C CB  . GLN A 1 384 ? 155.233 169.470 143.982 1.00 4.98   ? 384 GLN A CB  1 
ATOM   2557 C CG  . GLN A 1 384 ? 156.618 170.037 143.697 1.00 6.61   ? 384 GLN A CG  1 
ATOM   2558 C CD  . GLN A 1 384 ? 157.299 169.363 142.528 1.00 12.94  ? 384 GLN A CD  1 
ATOM   2559 O OE1 . GLN A 1 384 ? 158.411 168.837 142.642 1.00 16.25  ? 384 GLN A OE1 1 
ATOM   2560 N NE2 . GLN A 1 384 ? 156.634 169.380 141.382 1.00 22.86  ? 384 GLN A NE2 1 
ATOM   2561 N N   . ALA A 1 385 ? 152.235 169.463 145.733 1.00 4.94   ? 385 ALA A N   1 
ATOM   2562 C CA  . ALA A 1 385 ? 150.789 169.427 145.570 1.00 4.38   ? 385 ALA A CA  1 
ATOM   2563 C C   . ALA A 1 385 ? 150.140 169.165 146.918 1.00 6.88   ? 385 ALA A C   1 
ATOM   2564 O O   . ALA A 1 385 ? 150.573 168.275 147.655 1.00 10.15  ? 385 ALA A O   1 
ATOM   2565 C CB  . ALA A 1 385 ? 150.371 168.353 144.565 1.00 5.97   ? 385 ALA A CB  1 
ATOM   2566 N N   . TRP A 1 386 ? 149.112 169.942 147.231 1.00 8.17   ? 386 TRP A N   1 
ATOM   2567 C CA  . TRP A 1 386 ? 148.314 169.771 148.431 1.00 8.67   ? 386 TRP A CA  1 
ATOM   2568 C C   . TRP A 1 386 ? 146.843 169.889 148.069 1.00 13.58  ? 386 TRP A C   1 
ATOM   2569 O O   . TRP A 1 386 ? 146.491 170.590 147.115 1.00 21.35  ? 386 TRP A O   1 
ATOM   2570 C CB  . TRP A 1 386 ? 148.670 170.823 149.491 1.00 11.34  ? 386 TRP A CB  1 
ATOM   2571 C CG  . TRP A 1 386 ? 148.481 170.359 150.903 1.00 11.46  ? 386 TRP A CG  1 
ATOM   2572 C CD1 . TRP A 1 386 ? 147.603 170.860 151.819 1.00 15.11  ? 386 TRP A CD1 1 
ATOM   2573 C CD2 . TRP A 1 386 ? 149.192 169.306 151.563 1.00 10.61  ? 386 TRP A CD2 1 
ATOM   2574 N NE1 . TRP A 1 386 ? 147.720 170.182 153.006 1.00 16.79  ? 386 TRP A NE1 1 
ATOM   2575 C CE2 . TRP A 1 386 ? 148.689 169.222 152.875 1.00 13.06  ? 386 TRP A CE2 1 
ATOM   2576 C CE3 . TRP A 1 386 ? 150.202 168.423 151.171 1.00 13.87  ? 386 TRP A CE3 1 
ATOM   2577 C CZ2 . TRP A 1 386 ? 149.163 168.293 153.797 1.00 14.13  ? 386 TRP A CZ2 1 
ATOM   2578 C CZ3 . TRP A 1 386 ? 150.672 167.504 152.086 1.00 12.49  ? 386 TRP A CZ3 1 
ATOM   2579 C CH2 . TRP A 1 386 ? 150.152 167.445 153.383 1.00 14.60  ? 386 TRP A CH2 1 
ATOM   2580 N N   . PRO A 1 387 ? 145.965 169.197 148.793 1.00 15.16  ? 387 PRO A N   1 
ATOM   2581 C CA  . PRO A 1 387 ? 144.528 169.399 148.585 1.00 15.98  ? 387 PRO A CA  1 
ATOM   2582 C C   . PRO A 1 387 ? 144.155 170.860 148.779 1.00 21.04  ? 387 PRO A C   1 
ATOM   2583 O O   . PRO A 1 387 ? 144.596 171.514 149.727 1.00 24.01  ? 387 PRO A O   1 
ATOM   2584 C CB  . PRO A 1 387 ? 143.877 168.503 149.647 1.00 16.29  ? 387 PRO A CB  1 
ATOM   2585 C CG  . PRO A 1 387 ? 145.005 167.901 150.443 1.00 16.51  ? 387 PRO A CG  1 
ATOM   2586 C CD  . PRO A 1 387 ? 146.244 168.026 149.637 1.00 13.44  ? 387 PRO A CD  1 
ATOM   2587 N N   . GLU A 1 388 ? 143.331 171.370 147.866 1.00 23.92  ? 388 GLU A N   1 
ATOM   2588 C CA  . GLU A 1 388 ? 143.006 172.789 147.849 1.00 28.35  ? 388 GLU A CA  1 
ATOM   2589 C C   . GLU A 1 388 ? 142.003 173.186 148.923 1.00 31.17  ? 388 GLU A C   1 
ATOM   2590 O O   . GLU A 1 388 ? 141.832 174.384 149.171 1.00 30.17  ? 388 GLU A O   1 
ATOM   2591 C CB  . GLU A 1 388 ? 142.477 173.182 146.469 1.00 35.45  ? 388 GLU A CB  1 
ATOM   2592 C CG  . GLU A 1 388 ? 143.520 173.095 145.366 1.00 34.62  ? 388 GLU A CG  1 
ATOM   2593 C CD  . GLU A 1 388 ? 142.955 173.419 143.999 1.00 50.91  ? 388 GLU A CD  1 
ATOM   2594 O OE1 . GLU A 1 388 ? 141.716 173.526 143.875 1.00 53.02  ? 388 GLU A OE1 1 
ATOM   2595 O OE2 . GLU A 1 388 ? 143.749 173.568 143.046 1.00 51.34  ? 388 GLU A OE2 1 
ATOM   2596 N N   . ASN A 1 389 ? 141.345 172.225 149.565 1.00 31.45  ? 389 ASN A N   1 
ATOM   2597 C CA  . ASN A 1 389 ? 140.398 172.516 150.632 1.00 27.60  ? 389 ASN A CA  1 
ATOM   2598 C C   . ASN A 1 389 ? 141.069 172.679 151.990 1.00 30.63  ? 389 ASN A C   1 
ATOM   2599 O O   . ASN A 1 389 ? 140.390 173.025 152.962 1.00 32.48  ? 389 ASN A O   1 
ATOM   2600 C CB  . ASN A 1 389 ? 139.331 171.418 150.707 1.00 29.10  ? 389 ASN A CB  1 
ATOM   2601 C CG  . ASN A 1 389 ? 139.788 170.211 151.501 1.00 37.41  ? 389 ASN A CG  1 
ATOM   2602 O OD1 . ASN A 1 389 ? 140.483 169.338 150.982 1.00 33.10  ? 389 ASN A OD1 1 
ATOM   2603 N ND2 . ASN A 1 389 ? 139.392 170.151 152.768 1.00 38.03  ? 389 ASN A ND2 1 
ATOM   2604 N N   . ARG A 1 390 ? 142.374 172.439 152.082 1.00 29.88  ? 390 ARG A N   1 
ATOM   2605 C CA  . ARG A 1 390 ? 143.132 172.629 153.311 1.00 29.54  ? 390 ARG A CA  1 
ATOM   2606 C C   . ARG A 1 390 ? 144.003 173.869 153.175 1.00 32.17  ? 390 ARG A C   1 
ATOM   2607 O O   . ARG A 1 390 ? 144.709 174.032 152.174 1.00 28.73  ? 390 ARG A O   1 
ATOM   2608 C CB  . ARG A 1 390 ? 143.993 171.404 153.626 1.00 20.30  ? 390 ARG A CB  1 
ATOM   2609 C CG  . ARG A 1 390 ? 143.217 170.100 153.697 1.00 19.87  ? 390 ARG A CG  1 
ATOM   2610 C CD  . ARG A 1 390 ? 144.150 168.902 153.742 1.00 26.63  ? 390 ARG A CD  1 
ATOM   2611 N NE  . ARG A 1 390 ? 144.808 168.759 155.035 1.00 40.44  ? 390 ARG A NE  1 
ATOM   2612 C CZ  . ARG A 1 390 ? 145.197 167.602 155.553 1.00 44.18  ? 390 ARG A CZ  1 
ATOM   2613 N NH1 . ARG A 1 390 ? 145.007 166.460 154.914 1.00 40.79  ? 390 ARG A NH1 1 
ATOM   2614 N NH2 . ARG A 1 390 ? 145.793 167.591 156.742 1.00 38.34  ? 390 ARG A NH2 1 
ATOM   2615 N N   . THR A 1 391 ? 143.951 174.738 154.182 1.00 30.69  ? 391 THR A N   1 
ATOM   2616 C CA  . THR A 1 391 ? 144.653 176.014 154.151 1.00 25.15  ? 391 THR A CA  1 
ATOM   2617 C C   . THR A 1 391 ? 146.076 175.932 154.687 1.00 27.71  ? 391 THR A C   1 
ATOM   2618 O O   . THR A 1 391 ? 146.782 176.946 154.675 1.00 31.75  ? 391 THR A O   1 
ATOM   2619 C CB  . THR A 1 391 ? 143.873 177.063 154.949 1.00 29.28  ? 391 THR A CB  1 
ATOM   2620 O OG1 . THR A 1 391 ? 143.629 176.572 156.273 1.00 37.30  ? 391 THR A OG1 1 
ATOM   2621 C CG2 . THR A 1 391 ? 142.544 177.363 154.274 1.00 29.62  ? 391 THR A CG2 1 
ATOM   2622 N N   . ASP A 1 392 ? 146.513 174.767 155.159 1.00 25.99  ? 392 ASP A N   1 
ATOM   2623 C CA  . ASP A 1 392 ? 147.867 174.624 155.675 1.00 20.48  ? 392 ASP A CA  1 
ATOM   2624 C C   . ASP A 1 392 ? 148.258 173.155 155.652 1.00 17.59  ? 392 ASP A C   1 
ATOM   2625 O O   . ASP A 1 392 ? 147.409 172.268 155.537 1.00 20.95  ? 392 ASP A O   1 
ATOM   2626 C CB  . ASP A 1 392 ? 147.995 175.193 157.091 1.00 23.32  ? 392 ASP A CB  1 
ATOM   2627 C CG  . ASP A 1 392 ? 147.069 174.517 158.075 1.00 27.86  ? 392 ASP A CG  1 
ATOM   2628 O OD1 . ASP A 1 392 ? 146.061 173.924 157.636 1.00 36.50  ? 392 ASP A OD1 1 
ATOM   2629 O OD2 . ASP A 1 392 ? 147.347 174.585 159.289 1.00 22.31  ? 392 ASP A OD2 1 
ATOM   2630 N N   . LEU A 1 393 ? 149.565 172.913 155.767 1.00 17.50  ? 393 LEU A N   1 
ATOM   2631 C CA  . LEU A 1 393 ? 150.109 171.556 155.805 1.00 17.55  ? 393 LEU A CA  1 
ATOM   2632 C C   . LEU A 1 393 ? 149.910 170.970 157.203 1.00 21.36  ? 393 LEU A C   1 
ATOM   2633 O O   . LEU A 1 393 ? 150.834 170.851 158.011 1.00 19.11  ? 393 LEU A O   1 
ATOM   2634 C CB  . LEU A 1 393 ? 151.578 171.558 155.404 1.00 11.40  ? 393 LEU A CB  1 
ATOM   2635 C CG  . LEU A 1 393 ? 151.996 172.533 154.303 1.00 5.55   ? 393 LEU A CG  1 
ATOM   2636 C CD1 . LEU A 1 393 ? 153.477 172.847 154.405 1.00 5.42   ? 393 LEU A CD1 1 
ATOM   2637 C CD2 . LEU A 1 393 ? 151.667 171.961 152.939 1.00 8.83   ? 393 LEU A CD2 1 
ATOM   2638 N N   . HIS A 1 394 ? 148.659 170.598 157.484 1.00 24.60  ? 394 HIS A N   1 
ATOM   2639 C CA  . HIS A 1 394 ? 148.333 169.979 158.763 1.00 24.59  ? 394 HIS A CA  1 
ATOM   2640 C C   . HIS A 1 394 ? 148.890 168.570 158.897 1.00 25.86  ? 394 HIS A C   1 
ATOM   2641 O O   . HIS A 1 394 ? 148.933 168.046 160.014 1.00 32.18  ? 394 HIS A O   1 
ATOM   2642 C CB  . HIS A 1 394 ? 146.817 169.954 158.970 1.00 30.05  ? 394 HIS A CB  1 
ATOM   2643 C CG  . HIS A 1 394 ? 146.299 171.103 159.779 1.00 38.21  ? 394 HIS A CG  1 
ATOM   2644 N ND1 . HIS A 1 394 ? 147.020 171.678 160.803 1.00 28.46  ? 394 HIS A ND1 1 
ATOM   2645 C CD2 . HIS A 1 394 ? 145.127 171.779 159.719 1.00 40.03  ? 394 HIS A CD2 1 
ATOM   2646 C CE1 . HIS A 1 394 ? 146.317 172.659 161.338 1.00 26.11  ? 394 HIS A CE1 1 
ATOM   2647 N NE2 . HIS A 1 394 ? 145.165 172.743 160.697 1.00 34.27  ? 394 HIS A NE2 1 
ATOM   2648 N N   . ALA A 1 395 ? 149.306 167.942 157.796 1.00 28.25  ? 395 ALA A N   1 
ATOM   2649 C CA  . ALA A 1 395 ? 149.937 166.633 157.889 1.00 23.56  ? 395 ALA A CA  1 
ATOM   2650 C C   . ALA A 1 395 ? 151.351 166.715 158.444 1.00 24.65  ? 395 ALA A C   1 
ATOM   2651 O O   . ALA A 1 395 ? 151.859 165.717 158.963 1.00 36.03  ? 395 ALA A O   1 
ATOM   2652 C CB  . ALA A 1 395 ? 149.955 165.956 156.520 1.00 17.96  ? 395 ALA A CB  1 
ATOM   2653 N N   . PHE A 1 396 ? 151.997 167.877 158.346 1.00 17.07  ? 396 PHE A N   1 
ATOM   2654 C CA  . PHE A 1 396 ? 153.360 168.058 158.827 1.00 13.85  ? 396 PHE A CA  1 
ATOM   2655 C C   . PHE A 1 396 ? 153.435 169.029 159.997 1.00 18.51  ? 396 PHE A C   1 
ATOM   2656 O O   . PHE A 1 396 ? 154.484 169.638 160.228 1.00 19.41  ? 396 PHE A O   1 
ATOM   2657 C CB  . PHE A 1 396 ? 154.260 168.521 157.683 1.00 13.00  ? 396 PHE A CB  1 
ATOM   2658 C CG  . PHE A 1 396 ? 154.264 167.587 156.511 1.00 10.93  ? 396 PHE A CG  1 
ATOM   2659 C CD1 . PHE A 1 396 ? 154.781 166.309 156.634 1.00 11.98  ? 396 PHE A CD1 1 
ATOM   2660 C CD2 . PHE A 1 396 ? 153.739 167.979 155.293 1.00 8.61   ? 396 PHE A CD2 1 
ATOM   2661 C CE1 . PHE A 1 396 ? 154.781 165.443 155.562 1.00 10.33  ? 396 PHE A CE1 1 
ATOM   2662 C CE2 . PHE A 1 396 ? 153.738 167.117 154.217 1.00 10.54  ? 396 PHE A CE2 1 
ATOM   2663 C CZ  . PHE A 1 396 ? 154.259 165.847 154.353 1.00 11.41  ? 396 PHE A CZ  1 
ATOM   2664 N N   . GLU A 1 397 ? 152.338 169.189 160.740 1.00 22.92  ? 397 GLU A N   1 
ATOM   2665 C CA  . GLU A 1 397 ? 152.367 170.044 161.920 1.00 14.37  ? 397 GLU A CA  1 
ATOM   2666 C C   . GLU A 1 397 ? 153.248 169.458 163.014 1.00 16.36  ? 397 GLU A C   1 
ATOM   2667 O O   . GLU A 1 397 ? 153.810 170.207 163.819 1.00 15.41  ? 397 GLU A O   1 
ATOM   2668 C CB  . GLU A 1 397 ? 150.949 170.266 162.446 1.00 19.20  ? 397 GLU A CB  1 
ATOM   2669 C CG  . GLU A 1 397 ? 150.201 168.984 162.770 1.00 25.74  ? 397 GLU A CG  1 
ATOM   2670 C CD  . GLU A 1 397 ? 148.876 169.241 163.461 1.00 39.52  ? 397 GLU A CD  1 
ATOM   2671 O OE1 . GLU A 1 397 ? 148.220 170.252 163.136 1.00 33.68  ? 397 GLU A OE1 1 
ATOM   2672 O OE2 . GLU A 1 397 ? 148.491 168.430 164.329 1.00 56.12  ? 397 GLU A OE2 1 
ATOM   2673 N N   . ASN A 1 398 ? 153.375 168.132 163.063 1.00 28.57  ? 398 ASN A N   1 
ATOM   2674 C CA  . ASN A 1 398 ? 154.190 167.465 164.068 1.00 20.26  ? 398 ASN A CA  1 
ATOM   2675 C C   . ASN A 1 398 ? 155.630 167.244 163.626 1.00 15.50  ? 398 ASN A C   1 
ATOM   2676 O O   . ASN A 1 398 ? 156.447 166.803 164.441 1.00 16.95  ? 398 ASN A O   1 
ATOM   2677 C CB  . ASN A 1 398 ? 153.567 166.117 164.444 1.00 18.77  ? 398 ASN A CB  1 
ATOM   2678 C CG  . ASN A 1 398 ? 152.259 166.269 165.193 1.00 31.56  ? 398 ASN A CG  1 
ATOM   2679 O OD1 . ASN A 1 398 ? 152.122 167.135 166.057 1.00 39.50  ? 398 ASN A OD1 1 
ATOM   2680 N ND2 . ASN A 1 398 ? 151.288 165.425 164.865 1.00 33.04  ? 398 ASN A ND2 1 
ATOM   2681 N N   . LEU A 1 399 ? 155.961 167.536 162.371 1.00 15.42  ? 399 LEU A N   1 
ATOM   2682 C CA  . LEU A 1 399 ? 157.328 167.366 161.900 1.00 11.73  ? 399 LEU A CA  1 
ATOM   2683 C C   . LEU A 1 399 ? 158.248 168.352 162.607 1.00 11.65  ? 399 LEU A C   1 
ATOM   2684 O O   . LEU A 1 399 ? 157.966 169.552 162.658 1.00 13.83  ? 399 LEU A O   1 
ATOM   2685 C CB  . LEU A 1 399 ? 157.397 167.566 160.387 1.00 11.05  ? 399 LEU A CB  1 
ATOM   2686 C CG  . LEU A 1 399 ? 158.788 167.505 159.758 1.00 5.50   ? 399 LEU A CG  1 
ATOM   2687 C CD1 . LEU A 1 399 ? 159.372 166.110 159.882 1.00 9.32   ? 399 LEU A CD1 1 
ATOM   2688 C CD2 . LEU A 1 399 ? 158.730 167.934 158.307 1.00 6.02   ? 399 LEU A CD2 1 
ATOM   2689 N N   . GLU A 1 400 ? 159.350 167.843 163.151 1.00 9.29   ? 400 GLU A N   1 
ATOM   2690 C CA  . GLU A 1 400 ? 160.266 168.640 163.959 1.00 10.75  ? 400 GLU A CA  1 
ATOM   2691 C C   . GLU A 1 400 ? 161.623 168.859 163.312 1.00 9.44   ? 400 GLU A C   1 
ATOM   2692 O O   . GLU A 1 400 ? 162.136 169.979 163.337 1.00 13.76  ? 400 GLU A O   1 
ATOM   2693 C CB  . GLU A 1 400 ? 160.466 167.983 165.328 1.00 15.91  ? 400 GLU A CB  1 
ATOM   2694 C CG  . GLU A 1 400 ? 159.224 167.981 166.204 1.00 22.29  ? 400 GLU A CG  1 
ATOM   2695 C CD  . GLU A 1 400 ? 159.438 167.261 167.518 1.00 38.63  ? 400 GLU A CD  1 
ATOM   2696 O OE1 . GLU A 1 400 ? 160.487 166.601 167.672 1.00 54.78  ? 400 GLU A OE1 1 
ATOM   2697 O OE2 . GLU A 1 400 ? 158.558 167.356 168.400 1.00 35.27  ? 400 GLU A OE2 1 
ATOM   2698 N N   . ILE A 1 401 ? 162.183 167.833 162.664 1.00 10.54  ? 401 ILE A N   1 
ATOM   2699 C CA  . ILE A 1 401 ? 163.537 167.939 162.034 1.00 13.44  ? 401 ILE A CA  1 
ATOM   2700 C C   . ILE A 1 401 ? 163.477 167.521 160.559 1.00 11.09  ? 401 ILE A C   1 
ATOM   2701 O O   . ILE A 1 401 ? 162.711 166.595 160.249 1.00 14.75  ? 401 ILE A O   1 
ATOM   2702 C CB  . ILE A 1 401 ? 164.578 167.103 162.801 1.00 19.71  ? 401 ILE A CB  1 
ATOM   2703 C CG1 . ILE A 1 401 ? 164.566 167.411 164.294 1.00 22.12  ? 401 ILE A CG1 1 
ATOM   2704 C CG2 . ILE A 1 401 ? 165.968 167.297 162.199 1.00 24.76  ? 401 ILE A CG2 1 
ATOM   2705 C CD1 . ILE A 1 401 ? 163.707 166.466 165.112 1.00 25.08  ? 401 ILE A CD1 1 
ATOM   2706 N N   . ILE A 1 402 ? 164.232 168.196 159.689 1.00 11.69  ? 402 ILE A N   1 
ATOM   2707 C CA  . ILE A 1 402 ? 164.340 167.830 158.243 1.00 13.35  ? 402 ILE A CA  1 
ATOM   2708 C C   . ILE A 1 402 ? 165.845 167.785 157.950 1.00 19.67  ? 402 ILE A C   1 
ATOM   2709 O O   . ILE A 1 402 ? 166.361 168.752 157.354 1.00 29.34  ? 402 ILE A O   1 
ATOM   2710 C CB  . ILE A 1 402 ? 163.576 168.806 157.327 1.00 13.84  ? 402 ILE A CB  1 
ATOM   2711 C CG1 . ILE A 1 402 ? 162.141 169.027 157.806 1.00 9.53   ? 402 ILE A CG1 1 
ATOM   2712 C CG2 . ILE A 1 402 ? 163.622 168.325 155.877 1.00 11.32  ? 402 ILE A CG2 1 
ATOM   2713 C CD1 . ILE A 1 402 ? 161.360 170.052 157.002 1.00 7.48   ? 402 ILE A CD1 1 
ATOM   2714 N N   . ARG A 1 403 ? 166.520 166.714 158.366 1.00 21.85  ? 403 ARG A N   1 
ATOM   2715 C CA  . ARG A 1 403 ? 167.997 166.601 158.230 1.00 22.69  ? 403 ARG A CA  1 
ATOM   2716 C C   . ARG A 1 403 ? 168.458 167.075 156.844 1.00 24.17  ? 403 ARG A C   1 
ATOM   2717 O O   . ARG A 1 403 ? 169.455 167.804 156.790 1.00 26.75  ? 403 ARG A O   1 
ATOM   2718 C CB  . ARG A 1 403 ? 168.429 165.156 158.495 1.00 24.97  ? 403 ARG A CB  1 
ATOM   2719 C CG  . ARG A 1 403 ? 168.049 164.609 159.863 1.00 25.86  ? 403 ARG A CG  1 
ATOM   2720 C CD  . ARG A 1 403 ? 168.648 165.422 160.993 1.00 29.10  ? 403 ARG A CD  1 
ATOM   2721 N NE  . ARG A 1 403 ? 168.308 164.842 162.296 1.00 35.73  ? 403 ARG A NE  1 
ATOM   2722 C CZ  . ARG A 1 403 ? 168.587 165.364 163.484 1.00 38.24  ? 403 ARG A CZ  1 
ATOM   2723 N NH1 . ARG A 1 403 ? 169.375 166.420 163.598 1.00 41.14  ? 403 ARG A NH1 1 
ATOM   2724 N NH2 . ARG A 1 403 ? 168.048 164.833 164.565 1.00 35.23  ? 403 ARG A NH2 1 
ATOM   2725 N N   . GLY A 1 404 ? 167.802 166.648 155.768 1.00 20.40  ? 404 GLY A N   1 
ATOM   2726 C CA  . GLY A 1 404 ? 168.145 167.119 154.413 1.00 23.19  ? 404 GLY A CA  1 
ATOM   2727 C C   . GLY A 1 404 ? 169.296 166.331 153.825 1.00 32.22  ? 404 GLY A C   1 
ATOM   2728 O O   . GLY A 1 404 ? 169.714 166.678 152.708 1.00 38.31  ? 404 GLY A O   1 
ATOM   2729 N N   . ARG A 1 405 ? 169.790 165.309 154.528 1.00 32.11  ? 405 ARG A N   1 
ATOM   2730 C CA  . ARG A 1 405 ? 170.938 164.483 154.061 1.00 28.86  ? 405 ARG A CA  1 
ATOM   2731 C C   . ARG A 1 405 ? 170.862 164.349 152.531 1.00 36.37  ? 405 ARG A C   1 
ATOM   2732 O O   . ARG A 1 405 ? 171.893 164.623 151.880 1.00 49.61  ? 405 ARG A O   1 
ATOM   2733 C CB  . ARG A 1 405 ? 170.935 163.141 154.802 1.00 21.67  ? 405 ARG A CB  1 
ATOM   2734 C CG  . ARG A 1 405 ? 171.153 163.296 156.301 1.00 30.16  ? 405 ARG A CG  1 
ATOM   2735 C CD  . ARG A 1 405 ? 170.731 162.076 157.095 1.00 34.88  ? 405 ARG A CD  1 
ATOM   2736 N NE  . ARG A 1 405 ? 170.565 162.403 158.515 1.00 42.29  ? 405 ARG A NE  1 
ATOM   2737 C CZ  . ARG A 1 405 ? 170.200 161.563 159.478 1.00 43.17  ? 405 ARG A CZ  1 
ATOM   2738 N NH1 . ARG A 1 405 ? 169.912 160.301 159.212 1.00 38.65  ? 405 ARG A NH1 1 
ATOM   2739 N NH2 . ARG A 1 405 ? 170.119 161.994 160.723 1.00 43.68  ? 405 ARG A NH2 1 
ATOM   2740 N N   . THR A 1 406 ? 169.712 163.952 151.976 1.00 29.03  ? 406 THR A N   1 
ATOM   2741 C CA  . THR A 1 406 ? 169.500 163.885 150.519 1.00 29.45  ? 406 THR A CA  1 
ATOM   2742 C C   . THR A 1 406 ? 168.510 164.977 150.206 1.00 36.99  ? 406 THR A C   1 
ATOM   2743 O O   . THR A 1 406 ? 167.337 164.823 150.597 1.00 40.74  ? 406 THR A O   1 
ATOM   2744 C CB  . THR A 1 406 ? 168.968 162.505 150.144 1.00 31.32  ? 406 THR A CB  1 
ATOM   2745 O OG1 . THR A 1 406 ? 167.901 162.258 151.052 1.00 26.53  ? 406 THR A OG1 1 
ATOM   2746 C CG2 . THR A 1 406 ? 170.017 161.418 150.290 1.00 35.13  ? 406 THR A CG2 1 
ATOM   2747 N N   . LYS A 1 407 ? 168.951 166.062 149.565 1.00 39.68  ? 407 LYS A N   1 
ATOM   2748 C CA  . LYS A 1 407 ? 168.046 167.221 149.350 1.00 35.62  ? 407 LYS A CA  1 
ATOM   2749 C C   . LYS A 1 407 ? 167.599 167.302 147.883 1.00 37.80  ? 407 LYS A C   1 
ATOM   2750 O O   . LYS A 1 407 ? 168.325 166.787 147.009 1.00 45.81  ? 407 LYS A O   1 
ATOM   2751 C CB  . LYS A 1 407 ? 168.772 168.497 149.788 1.00 39.48  ? 407 LYS A CB  1 
ATOM   2752 C CG  . LYS A 1 407 ? 170.266 168.317 150.009 1.00 41.14  ? 407 LYS A CG  1 
ATOM   2753 C CD  . LYS A 1 407 ? 170.954 169.541 150.596 1.00 43.63  ? 407 LYS A CD  1 
ATOM   2754 C CE  . LYS A 1 407 ? 172.359 169.240 151.008 1.00 38.06  ? 407 LYS A CE  1 
ATOM   2755 N NZ  . LYS A 1 407 ? 172.408 168.116 151.946 1.00 35.02  ? 407 LYS A NZ  1 
ATOM   2756 N N   . GLN A 1 408 ? 166.445 167.928 147.636 1.00 36.80  ? 408 GLN A N   1 
ATOM   2757 C CA  . GLN A 1 408 ? 165.935 168.093 146.251 1.00 40.79  ? 408 GLN A CA  1 
ATOM   2758 C C   . GLN A 1 408 ? 166.982 168.852 145.425 1.00 47.25  ? 408 GLN A C   1 
ATOM   2759 O O   . GLN A 1 408 ? 167.493 169.876 145.923 1.00 46.02  ? 408 GLN A O   1 
ATOM   2760 C CB  . GLN A 1 408 ? 164.612 168.856 146.277 1.00 37.97  ? 408 GLN A CB  1 
ATOM   2761 C CG  . GLN A 1 408 ? 163.884 168.890 144.938 1.00 33.94  ? 408 GLN A CG  1 
ATOM   2762 C CD  . GLN A 1 408 ? 162.805 169.948 144.876 1.00 42.25  ? 408 GLN A CD  1 
ATOM   2763 O OE1 . GLN A 1 408 ? 162.586 170.702 145.829 1.00 45.02  ? 408 GLN A OE1 1 
ATOM   2764 N NE2 . GLN A 1 408 ? 162.123 170.018 143.742 1.00 41.71  ? 408 GLN A NE2 1 
ATOM   2765 N N   . HIS A 1 409 ? 167.278 168.371 144.215 1.00 53.83  ? 409 HIS A N   1 
ATOM   2766 C CA  . HIS A 1 409 ? 168.315 169.015 143.362 1.00 59.95  ? 409 HIS A CA  1 
ATOM   2767 C C   . HIS A 1 409 ? 169.570 169.233 144.211 1.00 62.88  ? 409 HIS A C   1 
ATOM   2768 O O   . HIS A 1 409 ? 170.298 170.221 143.973 1.00 62.43  ? 409 HIS A O   1 
ATOM   2769 C CB  . HIS A 1 409 ? 167.807 170.313 142.725 1.00 59.23  ? 409 HIS A CB  1 
ATOM   2770 C CG  . HIS A 1 409 ? 166.681 170.115 141.768 1.00 64.05  ? 409 HIS A CG  1 
ATOM   2771 N ND1 . HIS A 1 409 ? 165.359 170.208 142.141 1.00 61.54  ? 409 HIS A ND1 1 
ATOM   2772 C CD2 . HIS A 1 409 ? 166.677 169.829 140.461 1.00 64.24  ? 409 HIS A CD2 1 
ATOM   2773 C CE1 . HIS A 1 409 ? 164.590 169.979 141.087 1.00 64.14  ? 409 HIS A CE1 1 
ATOM   2774 N NE2 . HIS A 1 409 ? 165.371 169.746 140.055 1.00 71.86  ? 409 HIS A NE2 1 
ATOM   2775 N N   . GLY A 1 410 ? 169.813 168.343 145.178 1.00 60.04  ? 410 GLY A N   1 
ATOM   2776 C CA  . GLY A 1 410 ? 170.972 168.494 146.080 1.00 50.00  ? 410 GLY A CA  1 
ATOM   2777 C C   . GLY A 1 410 ? 170.986 169.871 146.711 1.00 53.33  ? 410 GLY A C   1 
ATOM   2778 O O   . GLY A 1 410 ? 172.092 170.421 146.889 1.00 60.51  ? 410 GLY A O   1 
ATOM   2779 N N   . GLN A 1 411 ? 169.809 170.408 147.054 1.00 47.23  ? 411 GLN A N   1 
ATOM   2780 C CA  . GLN A 1 411 ? 169.748 171.794 147.588 1.00 37.03  ? 411 GLN A CA  1 
ATOM   2781 C C   . GLN A 1 411 ? 168.579 171.970 148.566 1.00 35.55  ? 411 GLN A C   1 
ATOM   2782 O O   . GLN A 1 411 ? 168.855 172.214 149.757 1.00 37.64  ? 411 GLN A O   1 
ATOM   2783 C CB  . GLN A 1 411 ? 169.586 172.793 146.444 1.00 37.95  ? 411 GLN A CB  1 
ATOM   2784 C CG  . GLN A 1 411 ? 169.525 174.246 146.903 1.00 38.60  ? 411 GLN A CG  1 
ATOM   2785 C CD  . GLN A 1 411 ? 169.423 175.230 145.759 1.00 45.05  ? 411 GLN A CD  1 
ATOM   2786 O OE1 . GLN A 1 411 ? 169.400 174.852 144.583 1.00 46.40  ? 411 GLN A OE1 1 
ATOM   2787 N NE2 . GLN A 1 411 ? 169.360 176.509 146.097 1.00 46.33  ? 411 GLN A NE2 1 
ATOM   2788 N N   . PHE A 1 412 ? 167.334 171.853 148.095 1.00 37.38  ? 412 PHE A N   1 
ATOM   2789 C CA  . PHE A 1 412 ? 166.165 172.154 148.972 1.00 27.37  ? 412 PHE A CA  1 
ATOM   2790 C C   . PHE A 1 412 ? 165.795 170.958 149.843 1.00 27.20  ? 412 PHE A C   1 
ATOM   2791 O O   . PHE A 1 412 ? 165.573 169.859 149.304 1.00 27.85  ? 412 PHE A O   1 
ATOM   2792 C CB  . PHE A 1 412 ? 164.993 172.629 148.108 1.00 22.03  ? 412 PHE A CB  1 
ATOM   2793 C CG  . PHE A 1 412 ? 165.383 173.625 147.025 1.00 24.97  ? 412 PHE A CG  1 
ATOM   2794 C CD1 . PHE A 1 412 ? 165.552 174.972 147.322 1.00 25.98  ? 412 PHE A CD1 1 
ATOM   2795 C CD2 . PHE A 1 412 ? 165.559 173.215 145.709 1.00 32.47  ? 412 PHE A CD2 1 
ATOM   2796 C CE1 . PHE A 1 412 ? 165.899 175.879 146.335 1.00 26.06  ? 412 PHE A CE1 1 
ATOM   2797 C CE2 . PHE A 1 412 ? 165.906 174.127 144.725 1.00 37.75  ? 412 PHE A CE2 1 
ATOM   2798 C CZ  . PHE A 1 412 ? 166.073 175.455 145.039 1.00 33.00  ? 412 PHE A CZ  1 
ATOM   2799 N N   . SER A 1 413 ? 165.719 171.175 151.159 1.00 23.15  ? 413 SER A N   1 
ATOM   2800 C CA  . SER A 1 413 ? 165.302 170.102 152.097 1.00 15.87  ? 413 SER A CA  1 
ATOM   2801 C C   . SER A 1 413 ? 163.840 170.337 152.494 1.00 16.29  ? 413 SER A C   1 
ATOM   2802 O O   . SER A 1 413 ? 163.182 169.370 152.924 1.00 16.06  ? 413 SER A O   1 
ATOM   2803 C CB  . SER A 1 413 ? 166.198 170.061 153.297 1.00 20.75  ? 413 SER A CB  1 
ATOM   2804 O OG  . SER A 1 413 ? 166.199 171.318 153.959 1.00 25.61  ? 413 SER A OG  1 
ATOM   2805 N N   . LEU A 1 414 ? 163.360 171.578 152.379 1.00 13.88  ? 414 LEU A N   1 
ATOM   2806 C CA  . LEU A 1 414 ? 161.926 171.873 152.637 1.00 7.45   ? 414 LEU A CA  1 
ATOM   2807 C C   . LEU A 1 414 ? 161.409 172.651 151.422 1.00 8.06   ? 414 LEU A C   1 
ATOM   2808 O O   . LEU A 1 414 ? 161.883 173.781 151.201 1.00 13.15  ? 414 LEU A O   1 
ATOM   2809 C CB  . LEU A 1 414 ? 161.711 172.655 153.930 1.00 9.07   ? 414 LEU A CB  1 
ATOM   2810 C CG  . LEU A 1 414 ? 160.278 173.129 154.194 1.00 7.65   ? 414 LEU A CG  1 
ATOM   2811 C CD1 . LEU A 1 414 ? 159.332 171.955 154.367 1.00 6.01   ? 414 LEU A CD1 1 
ATOM   2812 C CD2 . LEU A 1 414 ? 160.224 174.045 155.402 1.00 10.19  ? 414 LEU A CD2 1 
ATOM   2813 N N   . ALA A 1 415 ? 160.490 172.062 150.656 1.00 9.83   ? 415 ALA A N   1 
ATOM   2814 C CA  . ALA A 1 415 ? 160.030 172.726 149.415 1.00 8.83   ? 415 ALA A CA  1 
ATOM   2815 C C   . ALA A 1 415 ? 158.504 172.739 149.333 1.00 10.92  ? 415 ALA A C   1 
ATOM   2816 O O   . ALA A 1 415 ? 157.935 171.769 148.796 1.00 13.52  ? 415 ALA A O   1 
ATOM   2817 C CB  . ALA A 1 415 ? 160.639 172.037 148.218 1.00 10.17  ? 415 ALA A CB  1 
ATOM   2818 N N   . VAL A 1 416 ? 157.863 173.790 149.852 1.00 9.91   ? 416 VAL A N   1 
ATOM   2819 C CA  . VAL A 1 416 ? 156.386 173.940 149.696 1.00 5.91   ? 416 VAL A CA  1 
ATOM   2820 C C   . VAL A 1 416 ? 156.189 174.750 148.409 1.00 9.74   ? 416 VAL A C   1 
ATOM   2821 O O   . VAL A 1 416 ? 156.383 175.980 148.458 1.00 14.18  ? 416 VAL A O   1 
ATOM   2822 C CB  . VAL A 1 416 ? 155.784 174.642 150.923 1.00 5.64   ? 416 VAL A CB  1 
ATOM   2823 C CG1 . VAL A 1 416 ? 154.267 174.721 150.845 1.00 7.83   ? 416 VAL A CG1 1 
ATOM   2824 C CG2 . VAL A 1 416 ? 156.222 173.975 152.219 1.00 7.22   ? 416 VAL A CG2 1 
ATOM   2825 N N   . VAL A 1 417 ? 155.831 174.098 147.300 1.00 9.04   ? 417 VAL A N   1 
ATOM   2826 C CA  . VAL A 1 417 ? 155.797 174.840 146.005 1.00 12.85  ? 417 VAL A CA  1 
ATOM   2827 C C   . VAL A 1 417 ? 154.423 174.793 145.321 1.00 15.93  ? 417 VAL A C   1 
ATOM   2828 O O   . VAL A 1 417 ? 153.807 173.711 145.320 1.00 21.29  ? 417 VAL A O   1 
ATOM   2829 C CB  . VAL A 1 417 ? 156.897 174.276 145.085 1.00 13.74  ? 417 VAL A CB  1 
ATOM   2830 C CG1 . VAL A 1 417 ? 156.895 174.943 143.715 1.00 20.94  ? 417 VAL A CG1 1 
ATOM   2831 C CG2 . VAL A 1 417 ? 158.277 174.377 145.723 1.00 13.58  ? 417 VAL A CG2 1 
ATOM   2832 N N   . SER A 1 418 ? 153.969 175.925 144.776 1.00 16.13  ? 418 SER A N   1 
ATOM   2833 C CA  . SER A 1 418 ? 152.730 176.012 144.000 1.00 20.87  ? 418 SER A CA  1 
ATOM   2834 C C   . SER A 1 418 ? 151.569 175.311 144.707 1.00 19.35  ? 418 SER A C   1 
ATOM   2835 O O   . SER A 1 418 ? 150.987 174.347 144.205 1.00 20.90  ? 418 SER A O   1 
ATOM   2836 C CB  . SER A 1 418 ? 152.936 175.451 142.589 1.00 28.62  ? 418 SER A CB  1 
ATOM   2837 O OG  . SER A 1 418 ? 154.071 176.032 141.971 1.00 37.81  ? 418 SER A OG  1 
ATOM   2838 N N   . LEU A 1 419 ? 151.257 175.826 145.894 1.00 18.94  ? 419 LEU A N   1 
ATOM   2839 C CA  . LEU A 1 419 ? 150.134 175.249 146.665 1.00 17.86  ? 419 LEU A CA  1 
ATOM   2840 C C   . LEU A 1 419 ? 149.072 176.329 146.875 1.00 20.58  ? 419 LEU A C   1 
ATOM   2841 O O   . LEU A 1 419 ? 149.319 177.495 146.506 1.00 23.35  ? 419 LEU A O   1 
ATOM   2842 C CB  . LEU A 1 419 ? 150.610 174.684 148.002 1.00 15.14  ? 419 LEU A CB  1 
ATOM   2843 C CG  . LEU A 1 419 ? 151.642 173.556 147.942 1.00 9.00   ? 419 LEU A CG  1 
ATOM   2844 C CD1 . LEU A 1 419 ? 151.758 172.904 149.304 1.00 6.90   ? 419 LEU A CD1 1 
ATOM   2845 C CD2 . LEU A 1 419 ? 151.225 172.539 146.909 1.00 9.69   ? 419 LEU A CD2 1 
ATOM   2846 N N   . ASN A 1 420 ? 147.940 175.945 147.446 1.00 22.63  ? 420 ASN A N   1 
ATOM   2847 C CA  . ASN A 1 420 ? 146.830 176.848 147.721 1.00 29.94  ? 420 ASN A CA  1 
ATOM   2848 C C   . ASN A 1 420 ? 146.551 176.894 149.218 1.00 31.04  ? 420 ASN A C   1 
ATOM   2849 O O   . ASN A 1 420 ? 145.397 176.785 149.647 1.00 33.31  ? 420 ASN A O   1 
ATOM   2850 C CB  . ASN A 1 420 ? 145.579 176.420 146.948 1.00 30.63  ? 420 ASN A CB  1 
ATOM   2851 C CG  . ASN A 1 420 ? 144.542 177.521 146.868 1.00 38.21  ? 420 ASN A CG  1 
ATOM   2852 O OD1 . ASN A 1 420 ? 144.796 178.587 146.308 1.00 42.74  ? 420 ASN A OD1 1 
ATOM   2853 N ND2 . ASN A 1 420 ? 143.366 177.270 147.432 1.00 40.27  ? 420 ASN A ND2 1 
ATOM   2854 N N   . ILE A 1 421 ? 147.603 177.049 150.018 1.00 24.04  ? 421 ILE A N   1 
ATOM   2855 C CA  . ILE A 1 421 ? 147.511 177.013 151.472 1.00 22.84  ? 421 ILE A CA  1 
ATOM   2856 C C   . ILE A 1 421 ? 147.674 178.426 152.013 1.00 26.36  ? 421 ILE A C   1 
ATOM   2857 O O   . ILE A 1 421 ? 148.527 179.188 151.544 1.00 26.78  ? 421 ILE A O   1 
ATOM   2858 C CB  . ILE A 1 421 ? 148.566 176.069 152.081 1.00 18.13  ? 421 ILE A CB  1 
ATOM   2859 C CG1 . ILE A 1 421 ? 149.908 176.237 151.371 1.00 15.21  ? 421 ILE A CG1 1 
ATOM   2860 C CG2 . ILE A 1 421 ? 148.096 174.626 151.998 1.00 16.88  ? 421 ILE A CG2 1 
ATOM   2861 C CD1 . ILE A 1 421 ? 151.082 175.705 152.155 1.00 11.99  ? 421 ILE A CD1 1 
ATOM   2862 N N   . THR A 1 422 ? 146.840 178.778 152.994 1.00 27.16  ? 422 THR A N   1 
ATOM   2863 C CA  . THR A 1 422 ? 146.933 180.098 153.610 1.00 20.39  ? 422 THR A CA  1 
ATOM   2864 C C   . THR A 1 422 ? 148.163 180.211 154.504 1.00 29.32  ? 422 THR A C   1 
ATOM   2865 O O   . THR A 1 422 ? 148.884 181.214 154.453 1.00 41.27  ? 422 THR A O   1 
ATOM   2866 C CB  . THR A 1 422 ? 145.659 180.393 154.405 1.00 25.43  ? 422 THR A CB  1 
ATOM   2867 O OG1 . THR A 1 422 ? 144.588 180.691 153.500 1.00 32.61  ? 422 THR A OG1 1 
ATOM   2868 C CG2 . THR A 1 422 ? 145.866 181.576 155.340 1.00 32.13  ? 422 THR A CG2 1 
ATOM   2869 N N   . SER A 1 423 ? 148.390 179.193 155.340 1.00 27.40  ? 423 SER A N   1 
ATOM   2870 C CA  . SER A 1 423 ? 149.559 179.196 156.257 1.00 21.45  ? 423 SER A CA  1 
ATOM   2871 C C   . SER A 1 423 ? 150.429 177.965 155.976 1.00 22.75  ? 423 SER A C   1 
ATOM   2872 O O   . SER A 1 423 ? 149.977 177.088 155.216 1.00 26.92  ? 423 SER A O   1 
ATOM   2873 C CB  . SER A 1 423 ? 149.111 179.231 157.687 1.00 19.94  ? 423 SER A CB  1 
ATOM   2874 O OG  . SER A 1 423 ? 148.117 178.247 157.933 1.00 19.98  ? 423 SER A OG  1 
ATOM   2875 N N   . LEU A 1 424 ? 151.630 177.909 156.556 1.00 25.28  ? 424 LEU A N   1 
ATOM   2876 C CA  . LEU A 1 424 ? 152.508 176.721 156.382 1.00 12.62  ? 424 LEU A CA  1 
ATOM   2877 C C   . LEU A 1 424 ? 152.048 175.614 157.345 1.00 9.85   ? 424 LEU A C   1 
ATOM   2878 O O   . LEU A 1 424 ? 152.041 174.445 156.928 1.00 14.01  ? 424 LEU A O   1 
ATOM   2879 C CB  . LEU A 1 424 ? 153.972 177.090 156.606 1.00 14.68  ? 424 LEU A CB  1 
ATOM   2880 C CG  . LEU A 1 424 ? 154.640 177.887 155.484 1.00 10.81  ? 424 LEU A CG  1 
ATOM   2881 C CD1 . LEU A 1 424 ? 155.899 178.547 156.012 1.00 14.54  ? 424 LEU A CD1 1 
ATOM   2882 C CD2 . LEU A 1 424 ? 154.969 176.945 154.341 1.00 5.92   ? 424 LEU A CD2 1 
ATOM   2883 N N   . GLY A 1 425 ? 151.677 175.968 158.576 1.00 10.87  ? 425 GLY A N   1 
ATOM   2884 C CA  . GLY A 1 425 ? 151.274 174.934 159.514 1.00 14.16  ? 425 GLY A CA  1 
ATOM   2885 C C   . GLY A 1 425 ? 152.390 174.000 159.933 1.00 16.63  ? 425 GLY A C   1 
ATOM   2886 O O   . GLY A 1 425 ? 152.146 172.807 160.151 1.00 18.63  ? 425 GLY A O   1 
ATOM   2887 N N   . LEU A 1 426 ? 153.625 174.505 160.010 1.00 13.04  ? 426 LEU A N   1 
ATOM   2888 C CA  . LEU A 1 426 ? 154.777 173.678 160.464 1.00 8.04   ? 426 LEU A CA  1 
ATOM   2889 C C   . LEU A 1 426 ? 155.161 174.127 161.878 1.00 11.51  ? 426 LEU A C   1 
ATOM   2890 O O   . LEU A 1 426 ? 156.350 174.417 162.100 1.00 16.68  ? 426 LEU A O   1 
ATOM   2891 C CB  . LEU A 1 426 ? 155.938 173.810 159.483 1.00 7.90   ? 426 LEU A CB  1 
ATOM   2892 C CG  . LEU A 1 426 ? 155.624 173.485 158.020 1.00 6.93   ? 426 LEU A CG  1 
ATOM   2893 C CD1 . LEU A 1 426 ? 156.827 173.769 157.140 1.00 9.80   ? 426 LEU A CD1 1 
ATOM   2894 C CD2 . LEU A 1 426 ? 155.190 172.040 157.875 1.00 6.67   ? 426 LEU A CD2 1 
ATOM   2895 N N   . ARG A 1 427 ? 154.199 174.146 162.801 1.00 12.44  ? 427 ARG A N   1 
ATOM   2896 C CA  . ARG A 1 427 ? 154.420 174.653 164.154 1.00 12.40  ? 427 ARG A CA  1 
ATOM   2897 C C   . ARG A 1 427 ? 155.595 173.968 164.845 1.00 16.70  ? 427 ARG A C   1 
ATOM   2898 O O   . ARG A 1 427 ? 156.448 174.631 165.445 1.00 21.84  ? 427 ARG A O   1 
ATOM   2899 C CB  . ARG A 1 427 ? 153.150 174.465 164.985 1.00 16.25  ? 427 ARG A CB  1 
ATOM   2900 C CG  . ARG A 1 427 ? 151.864 174.559 164.190 1.00 13.71  ? 427 ARG A CG  1 
ATOM   2901 C CD  . ARG A 1 427 ? 150.684 174.020 164.986 1.00 19.45  ? 427 ARG A CD  1 
ATOM   2902 N NE  . ARG A 1 427 ? 150.607 172.564 164.951 1.00 23.49  ? 427 ARG A NE  1 
ATOM   2903 C CZ  . ARG A 1 427 ? 151.007 171.768 165.933 1.00 24.36  ? 427 ARG A CZ  1 
ATOM   2904 N NH1 . ARG A 1 427 ? 151.530 172.253 167.046 1.00 23.66  ? 427 ARG A NH1 1 
ATOM   2905 N NH2 . ARG A 1 427 ? 150.878 170.452 165.795 1.00 24.26  ? 427 ARG A NH2 1 
ATOM   2906 N N   . SER A 1 428 ? 155.655 172.639 164.774 1.00 14.54  ? 428 SER A N   1 
ATOM   2907 C CA  . SER A 1 428 ? 156.684 171.901 165.495 1.00 11.10  ? 428 SER A CA  1 
ATOM   2908 C C   . SER A 1 428 ? 158.031 171.893 164.785 1.00 10.35  ? 428 SER A C   1 
ATOM   2909 O O   . SER A 1 428 ? 159.010 171.415 165.367 1.00 14.68  ? 428 SER A O   1 
ATOM   2910 C CB  . SER A 1 428 ? 156.231 170.460 165.737 1.00 16.18  ? 428 SER A CB  1 
ATOM   2911 O OG  . SER A 1 428 ? 154.905 170.422 166.235 1.00 19.25  ? 428 SER A OG  1 
ATOM   2912 N N   . LEU A 1 429 ? 158.109 172.400 163.557 1.00 10.25  ? 429 LEU A N   1 
ATOM   2913 C CA  . LEU A 1 429 ? 159.379 172.424 162.842 1.00 9.86   ? 429 LEU A CA  1 
ATOM   2914 C C   . LEU A 1 429 ? 160.362 173.343 163.554 1.00 8.68   ? 429 LEU A C   1 
ATOM   2915 O O   . LEU A 1 429 ? 160.089 174.532 163.745 1.00 14.97  ? 429 LEU A O   1 
ATOM   2916 C CB  . LEU A 1 429 ? 159.168 172.879 161.400 1.00 8.16   ? 429 LEU A CB  1 
ATOM   2917 C CG  . LEU A 1 429 ? 160.403 172.861 160.499 1.00 4.56   ? 429 LEU A CG  1 
ATOM   2918 C CD1 . LEU A 1 429 ? 160.797 171.435 160.164 1.00 5.75   ? 429 LEU A CD1 1 
ATOM   2919 C CD2 . LEU A 1 429 ? 160.155 173.659 159.231 1.00 8.59   ? 429 LEU A CD2 1 
ATOM   2920 N N   . LYS A 1 430 ? 161.504 172.785 163.951 1.00 8.60   ? 430 LYS A N   1 
ATOM   2921 C CA  . LYS A 1 430 ? 162.512 173.531 164.691 1.00 13.36  ? 430 LYS A CA  1 
ATOM   2922 C C   . LYS A 1 430 ? 163.920 173.407 164.133 1.00 15.11  ? 430 LYS A C   1 
ATOM   2923 O O   . LYS A 1 430 ? 164.734 174.305 164.378 1.00 19.48  ? 430 LYS A O   1 
ATOM   2924 C CB  . LYS A 1 430 ? 162.530 173.092 166.163 1.00 14.94  ? 430 LYS A CB  1 
ATOM   2925 C CG  . LYS A 1 430 ? 162.553 171.585 166.355 1.00 19.41  ? 430 LYS A CG  1 
ATOM   2926 C CD  . LYS A 1 430 ? 162.867 171.214 167.794 1.00 29.95  ? 430 LYS A CD  1 
ATOM   2927 C CE  . LYS A 1 430 ? 163.580 169.874 167.875 1.00 31.46  ? 430 LYS A CE  1 
ATOM   2928 N NZ  . LYS A 1 430 ? 164.846 169.872 167.091 1.00 27.13  ? 430 LYS A NZ  1 
ATOM   2929 N N   . GLU A 1 431 ? 164.241 172.343 163.401 1.00 13.54  ? 431 GLU A N   1 
ATOM   2930 C CA  . GLU A 1 431 ? 165.588 172.127 162.892 1.00 14.64  ? 431 GLU A CA  1 
ATOM   2931 C C   . GLU A 1 431 ? 165.529 171.734 161.424 1.00 14.40  ? 431 GLU A C   1 
ATOM   2932 O O   . GLU A 1 431 ? 164.746 170.860 161.041 1.00 15.03  ? 431 GLU A O   1 
ATOM   2933 C CB  . GLU A 1 431 ? 166.316 171.047 163.699 1.00 19.75  ? 431 GLU A CB  1 
ATOM   2934 C CG  . GLU A 1 431 ? 167.631 170.588 163.087 1.00 25.95  ? 431 GLU A CG  1 
ATOM   2935 C CD  . GLU A 1 431 ? 168.816 171.412 163.554 1.00 30.31  ? 431 GLU A CD  1 
ATOM   2936 O OE1 . GLU A 1 431 ? 168.784 172.650 163.395 1.00 20.03  ? 431 GLU A OE1 1 
ATOM   2937 O OE2 . GLU A 1 431 ? 169.781 170.819 164.079 1.00 38.41  ? 431 GLU A OE2 1 
ATOM   2938 N N   . ILE A 1 432 ? 166.323 172.419 160.595 1.00 16.33  ? 432 ILE A N   1 
ATOM   2939 C CA  . ILE A 1 432 ? 166.514 172.052 159.160 1.00 16.83  ? 432 ILE A CA  1 
ATOM   2940 C C   . ILE A 1 432 ? 168.042 171.985 159.097 1.00 24.40  ? 432 ILE A C   1 
ATOM   2941 O O   . ILE A 1 432 ? 168.665 173.064 159.077 1.00 33.64  ? 432 ILE A O   1 
ATOM   2942 C CB  . ILE A 1 432 ? 165.895 173.098 158.223 1.00 14.61  ? 432 ILE A CB  1 
ATOM   2943 C CG1 . ILE A 1 432 ? 164.402 173.260 158.495 1.00 11.59  ? 432 ILE A CG1 1 
ATOM   2944 C CG2 . ILE A 1 432 ? 166.167 172.754 156.761 1.00 20.49  ? 432 ILE A CG2 1 
ATOM   2945 C CD1 . ILE A 1 432 ? 163.819 174.571 158.004 1.00 15.02  ? 432 ILE A CD1 1 
ATOM   2946 N N   . SER A 1 433 ? 168.614 170.784 159.174 1.00 20.04  ? 433 SER A N   1 
ATOM   2947 C CA  . SER A 1 433 ? 170.082 170.632 159.323 1.00 25.97  ? 433 SER A CA  1 
ATOM   2948 C C   . SER A 1 433 ? 170.870 170.973 158.056 1.00 33.59  ? 433 SER A C   1 
ATOM   2949 O O   . SER A 1 433 ? 171.507 172.037 158.065 1.00 38.96  ? 433 SER A O   1 
ATOM   2950 C CB  . SER A 1 433 ? 170.390 169.233 159.784 1.00 32.19  ? 433 SER A CB  1 
ATOM   2951 O OG  . SER A 1 433 ? 169.635 168.908 160.942 1.00 31.19  ? 433 SER A OG  1 
ATOM   2952 N N   . ASP A 1 434 ? 170.807 170.155 157.006 1.00 30.74  ? 434 ASP A N   1 
ATOM   2953 C CA  . ASP A 1 434 ? 171.702 170.328 155.827 1.00 32.91  ? 434 ASP A CA  1 
ATOM   2954 C C   . ASP A 1 434 ? 171.132 171.232 154.735 1.00 36.57  ? 434 ASP A C   1 
ATOM   2955 O O   . ASP A 1 434 ? 171.796 172.246 154.444 1.00 47.25  ? 434 ASP A O   1 
ATOM   2956 C CB  . ASP A 1 434 ? 172.052 168.985 155.208 1.00 37.22  ? 434 ASP A CB  1 
ATOM   2957 C CG  . ASP A 1 434 ? 172.708 167.982 156.146 1.00 42.64  ? 434 ASP A CG  1 
ATOM   2958 O OD1 . ASP A 1 434 ? 173.785 168.304 156.688 1.00 53.65  ? 434 ASP A OD1 1 
ATOM   2959 O OD2 . ASP A 1 434 ? 172.137 166.885 156.323 1.00 30.78  ? 434 ASP A OD2 1 
ATOM   2960 N N   . GLY A 1 435 ? 169.991 170.902 154.124 1.00 30.59  ? 435 GLY A N   1 
ATOM   2961 C CA  . GLY A 1 435 ? 169.502 171.654 152.949 1.00 26.59  ? 435 GLY A CA  1 
ATOM   2962 C C   . GLY A 1 435 ? 168.828 172.965 153.284 1.00 27.30  ? 435 GLY A C   1 
ATOM   2963 O O   . GLY A 1 435 ? 168.576 173.213 154.476 1.00 41.10  ? 435 GLY A O   1 
ATOM   2964 N N   . ASP A 1 436 ? 168.525 173.765 152.258 1.00 23.07  ? 436 ASP A N   1 
ATOM   2965 C CA  . ASP A 1 436 ? 167.879 175.089 152.471 1.00 25.85  ? 436 ASP A CA  1 
ATOM   2966 C C   . ASP A 1 436 ? 166.355 174.937 152.433 1.00 21.46  ? 436 ASP A C   1 
ATOM   2967 O O   . ASP A 1 436 ? 165.868 173.795 152.577 1.00 19.25  ? 436 ASP A O   1 
ATOM   2968 C CB  . ASP A 1 436 ? 168.388 176.119 151.474 1.00 30.70  ? 436 ASP A CB  1 
ATOM   2969 C CG  . ASP A 1 436 ? 168.080 175.853 150.008 1.00 34.06  ? 436 ASP A CG  1 
ATOM   2970 O OD1 . ASP A 1 436 ? 167.464 174.813 149.719 1.00 34.77  ? 436 ASP A OD1 1 
ATOM   2971 O OD2 . ASP A 1 436 ? 168.456 176.695 149.166 1.00 36.32  ? 436 ASP A OD2 1 
ATOM   2972 N N   . VAL A 1 437 ? 165.635 176.048 152.249 1.00 19.75  ? 437 VAL A N   1 
ATOM   2973 C CA  . VAL A 1 437 ? 164.141 176.018 152.242 1.00 13.24  ? 437 VAL A CA  1 
ATOM   2974 C C   . VAL A 1 437 ? 163.618 176.859 151.069 1.00 15.81  ? 437 VAL A C   1 
ATOM   2975 O O   . VAL A 1 437 ? 164.074 178.006 150.922 1.00 27.16  ? 437 VAL A O   1 
ATOM   2976 C CB  . VAL A 1 437 ? 163.590 176.546 153.578 1.00 12.61  ? 437 VAL A CB  1 
ATOM   2977 C CG1 . VAL A 1 437 ? 162.118 176.924 153.483 1.00 13.86  ? 437 VAL A CG1 1 
ATOM   2978 C CG2 . VAL A 1 437 ? 163.820 175.564 154.718 1.00 18.37  ? 437 VAL A CG2 1 
ATOM   2979 N N   . ILE A 1 438 ? 162.702 176.312 150.268 1.00 13.44  ? 438 ILE A N   1 
ATOM   2980 C CA  . ILE A 1 438 ? 162.076 177.111 149.172 1.00 12.57  ? 438 ILE A CA  1 
ATOM   2981 C C   . ILE A 1 438 ? 160.554 177.063 149.356 1.00 15.13  ? 438 ILE A C   1 
ATOM   2982 O O   . ILE A 1 438 ? 159.977 175.960 149.282 1.00 18.23  ? 438 ILE A O   1 
ATOM   2983 C CB  . ILE A 1 438 ? 162.492 176.614 147.775 1.00 14.27  ? 438 ILE A CB  1 
ATOM   2984 C CG1 . ILE A 1 438 ? 161.792 177.406 146.671 1.00 15.36  ? 438 ILE A CG1 1 
ATOM   2985 C CG2 . ILE A 1 438 ? 162.257 175.112 147.620 1.00 21.57  ? 438 ILE A CG2 1 
ATOM   2986 C CD1 . ILE A 1 438 ? 162.138 176.944 145.268 1.00 22.21  ? 438 ILE A CD1 1 
ATOM   2987 N N   . ILE A 1 439 ? 159.936 178.210 149.626 1.00 14.97  ? 439 ILE A N   1 
ATOM   2988 C CA  . ILE A 1 439 ? 158.448 178.248 149.721 1.00 13.03  ? 439 ILE A CA  1 
ATOM   2989 C C   . ILE A 1 439 ? 157.953 179.238 148.661 1.00 17.23  ? 439 ILE A C   1 
ATOM   2990 O O   . ILE A 1 439 ? 157.902 180.446 148.963 1.00 23.94  ? 439 ILE A O   1 
ATOM   2991 C CB  . ILE A 1 439 ? 157.998 178.625 151.141 1.00 14.30  ? 439 ILE A CB  1 
ATOM   2992 C CG1 . ILE A 1 439 ? 158.798 177.864 152.189 1.00 17.24  ? 439 ILE A CG1 1 
ATOM   2993 C CG2 . ILE A 1 439 ? 156.498 178.397 151.303 1.00 14.63  ? 439 ILE A CG2 1 
ATOM   2994 C CD1 . ILE A 1 439 ? 158.413 178.194 153.617 1.00 18.60  ? 439 ILE A CD1 1 
ATOM   2995 N N   . SER A 1 440 ? 157.608 178.744 147.470 1.00 18.12  ? 440 SER A N   1 
ATOM   2996 C CA  . SER A 1 440 ? 157.237 179.665 146.366 1.00 20.51  ? 440 SER A CA  1 
ATOM   2997 C C   . SER A 1 440 ? 155.966 179.195 145.651 1.00 23.13  ? 440 SER A C   1 
ATOM   2998 O O   . SER A 1 440 ? 155.619 178.006 145.787 1.00 25.59  ? 440 SER A O   1 
ATOM   2999 C CB  . SER A 1 440 ? 158.376 179.788 145.394 1.00 25.19  ? 440 SER A CB  1 
ATOM   3000 O OG  . SER A 1 440 ? 158.699 178.523 144.835 1.00 34.96  ? 440 SER A OG  1 
ATOM   3001 N N   . GLY A 1 441 ? 155.307 180.092 144.916 1.00 24.72  ? 441 GLY A N   1 
ATOM   3002 C CA  . GLY A 1 441 ? 154.130 179.745 144.154 1.00 28.96  ? 441 GLY A CA  1 
ATOM   3003 C C   . GLY A 1 441 ? 152.836 179.707 144.936 1.00 29.29  ? 441 GLY A C   1 
ATOM   3004 O O   . GLY A 1 441 ? 151.763 179.666 144.321 1.00 34.48  ? 441 GLY A O   1 
ATOM   3005 N N   . ASN A 1 442 ? 152.932 179.730 146.269 1.00 21.40  ? 442 ASN A N   1 
ATOM   3006 C CA  . ASN A 1 442 ? 151.721 179.719 147.136 1.00 20.81  ? 442 ASN A CA  1 
ATOM   3007 C C   . ASN A 1 442 ? 151.061 181.098 147.076 1.00 28.94  ? 442 ASN A C   1 
ATOM   3008 O O   . ASN A 1 442 ? 151.419 181.956 147.907 1.00 37.68  ? 442 ASN A O   1 
ATOM   3009 C CB  . ASN A 1 442 ? 152.061 179.307 148.562 1.00 23.12  ? 442 ASN A CB  1 
ATOM   3010 C CG  . ASN A 1 442 ? 152.946 178.086 148.614 1.00 23.65  ? 442 ASN A CG  1 
ATOM   3011 O OD1 . ASN A 1 442 ? 154.061 178.101 148.083 1.00 23.34  ? 442 ASN A OD1 1 
ATOM   3012 N ND2 . ASN A 1 442 ? 152.476 177.027 149.254 1.00 19.38  ? 442 ASN A ND2 1 
ATOM   3013 N N   . LYS A 1 443 ? 150.120 181.299 146.150 1.00 31.41  ? 443 LYS A N   1 
ATOM   3014 C CA  . LYS A 1 443 ? 149.504 182.606 145.960 1.00 33.99  ? 443 LYS A CA  1 
ATOM   3015 C C   . LYS A 1 443 ? 148.680 183.057 147.158 1.00 33.33  ? 443 LYS A C   1 
ATOM   3016 O O   . LYS A 1 443 ? 148.303 184.232 147.217 1.00 39.10  ? 443 LYS A O   1 
ATOM   3017 C CB  . LYS A 1 443 ? 148.626 182.594 144.708 1.00 30.70  ? 443 LYS A CB  1 
ATOM   3018 C CG  . LYS A 1 443 ? 149.230 181.840 143.533 1.00 33.88  ? 443 LYS A CG  1 
ATOM   3019 C CD  . LYS A 1 443 ? 149.931 182.783 142.568 1.00 35.12  ? 443 LYS A CD  1 
ATOM   3020 C CE  . LYS A 1 443 ? 151.421 182.870 142.864 1.00 40.71  ? 443 LYS A CE  1 
ATOM   3021 N NZ  . LYS A 1 443 ? 152.206 183.246 141.656 1.00 40.20  ? 443 LYS A NZ  1 
ATOM   3022 N N   . ASN A 1 444 ? 148.387 182.165 148.102 1.00 30.69  ? 444 ASN A N   1 
ATOM   3023 C CA  . ASN A 1 444 ? 147.587 182.503 149.268 1.00 31.35  ? 444 ASN A CA  1 
ATOM   3024 C C   . ASN A 1 444 ? 148.359 182.409 150.576 1.00 31.86  ? 444 ASN A C   1 
ATOM   3025 O O   . ASN A 1 444 ? 147.775 182.642 151.640 1.00 29.94  ? 444 ASN A O   1 
ATOM   3026 C CB  . ASN A 1 444 ? 146.349 181.601 149.336 1.00 30.11  ? 444 ASN A CB  1 
ATOM   3027 C CG  . ASN A 1 444 ? 145.415 181.804 148.160 1.00 35.69  ? 444 ASN A CG  1 
ATOM   3028 O OD1 . ASN A 1 444 ? 144.392 182.478 148.274 1.00 46.99  ? 444 ASN A OD1 1 
ATOM   3029 N ND2 . ASN A 1 444 ? 145.763 181.218 147.021 1.00 32.67  ? 444 ASN A ND2 1 
ATOM   3030 N N   . LEU A 1 445 ? 149.661 182.112 150.484 1.00 31.16  ? 445 LEU A N   1 
ATOM   3031 C CA  . LEU A 1 445 ? 150.507 181.989 151.701 1.00 26.15  ? 445 LEU A CA  1 
ATOM   3032 C C   . LEU A 1 445 ? 150.743 183.389 152.275 1.00 32.61  ? 445 LEU A C   1 
ATOM   3033 O O   . LEU A 1 445 ? 151.238 184.252 151.527 1.00 41.17  ? 445 LEU A O   1 
ATOM   3034 C CB  . LEU A 1 445 ? 151.825 181.275 151.413 1.00 24.26  ? 445 LEU A CB  1 
ATOM   3035 C CG  . LEU A 1 445 ? 152.468 180.591 152.622 1.00 18.91  ? 445 LEU A CG  1 
ATOM   3036 C CD1 . LEU A 1 445 ? 151.602 179.441 153.093 1.00 19.13  ? 445 LEU A CD1 1 
ATOM   3037 C CD2 . LEU A 1 445 ? 153.855 180.105 152.276 1.00 19.00  ? 445 LEU A CD2 1 
ATOM   3038 N N   . CYS A 1 446 ? 150.447 183.585 153.559 1.00 30.49  ? 446 CYS A N   1 
ATOM   3039 C CA  . CYS A 1 446 ? 150.529 184.911 154.154 1.00 35.94  ? 446 CYS A CA  1 
ATOM   3040 C C   . CYS A 1 446 ? 151.629 184.977 155.208 1.00 45.80  ? 446 CYS A C   1 
ATOM   3041 O O   . CYS A 1 446 ? 152.526 185.821 155.119 1.00 63.29  ? 446 CYS A O   1 
ATOM   3042 C CB  . CYS A 1 446 ? 149.155 185.267 154.742 1.00 39.04  ? 446 CYS A CB  1 
ATOM   3043 S SG  . CYS A 1 446 ? 148.734 187.015 155.060 1.00 56.59  ? 446 CYS A SG  1 
ATOM   3044 N N   . TYR A 1 447 ? 151.598 184.086 156.200 1.00 37.44  ? 447 TYR A N   1 
ATOM   3045 C CA  . TYR A 1 447 ? 152.596 184.074 157.270 1.00 33.09  ? 447 TYR A CA  1 
ATOM   3046 C C   . TYR A 1 447 ? 153.750 183.165 156.856 1.00 43.38  ? 447 TYR A C   1 
ATOM   3047 O O   . TYR A 1 447 ? 153.872 182.018 157.293 1.00 49.65  ? 447 TYR A O   1 
ATOM   3048 C CB  . TYR A 1 447 ? 151.977 183.619 158.586 1.00 36.11  ? 447 TYR A CB  1 
ATOM   3049 C CG  . TYR A 1 447 ? 150.558 184.088 158.814 1.00 36.54  ? 447 TYR A CG  1 
ATOM   3050 C CD1 . TYR A 1 447 ? 149.478 183.329 158.383 1.00 31.93  ? 447 TYR A CD1 1 
ATOM   3051 C CD2 . TYR A 1 447 ? 150.299 185.279 159.475 1.00 50.02  ? 447 TYR A CD2 1 
ATOM   3052 C CE1 . TYR A 1 447 ? 148.179 183.749 158.594 1.00 43.36  ? 447 TYR A CE1 1 
ATOM   3053 C CE2 . TYR A 1 447 ? 149.003 185.708 159.692 1.00 51.88  ? 447 TYR A CE2 1 
ATOM   3054 C CZ  . TYR A 1 447 ? 147.947 184.939 159.249 1.00 56.27  ? 447 TYR A CZ  1 
ATOM   3055 O OH  . TYR A 1 447 ? 146.655 185.364 159.462 1.00 60.81  ? 447 TYR A OH  1 
ATOM   3056 N N   . ALA A 1 448 ? 154.615 183.696 155.995 1.00 44.85  ? 448 ALA A N   1 
ATOM   3057 C CA  . ALA A 1 448 ? 155.773 182.956 155.508 1.00 36.33  ? 448 ALA A CA  1 
ATOM   3058 C C   . ALA A 1 448 ? 157.089 183.627 155.860 1.00 32.55  ? 448 ALA A C   1 
ATOM   3059 O O   . ALA A 1 448 ? 158.000 182.966 156.371 1.00 37.44  ? 448 ALA A O   1 
ATOM   3060 C CB  . ALA A 1 448 ? 155.674 182.763 153.987 1.00 33.53  ? 448 ALA A CB  1 
ATOM   3061 N N   . ASN A 1 449 ? 157.218 184.928 155.601 1.00 27.84  ? 449 ASN A N   1 
ATOM   3062 C CA  . ASN A 1 449 ? 158.467 185.635 155.845 1.00 31.58  ? 449 ASN A CA  1 
ATOM   3063 C C   . ASN A 1 449 ? 158.670 186.007 157.308 1.00 38.45  ? 449 ASN A C   1 
ATOM   3064 O O   . ASN A 1 449 ? 159.770 186.437 157.671 1.00 39.78  ? 449 ASN A O   1 
ATOM   3065 C CB  . ASN A 1 449 ? 158.502 186.910 155.000 1.00 33.90  ? 449 ASN A CB  1 
ATOM   3066 C CG  . ASN A 1 449 ? 158.398 186.627 153.515 1.00 29.19  ? 449 ASN A CG  1 
ATOM   3067 O OD1 . ASN A 1 449 ? 157.372 186.895 152.891 1.00 30.05  ? 449 ASN A OD1 1 
ATOM   3068 N ND2 . ASN A 1 449 ? 159.463 186.083 152.942 1.00 30.28  ? 449 ASN A ND2 1 
ATOM   3069 N N   . THR A 1 450 ? 157.646 185.808 158.141 1.00 35.75  ? 450 THR A N   1 
ATOM   3070 C CA  . THR A 1 450 ? 157.735 186.189 159.567 1.00 32.32  ? 450 THR A CA  1 
ATOM   3071 C C   . THR A 1 450 ? 158.751 185.322 160.276 1.00 31.54  ? 450 THR A C   1 
ATOM   3072 O O   . THR A 1 450 ? 159.506 185.868 161.108 1.00 42.64  ? 450 THR A O   1 
ATOM   3073 C CB  . THR A 1 450 ? 156.354 186.044 160.204 1.00 34.37  ? 450 THR A CB  1 
ATOM   3074 O OG1 . THR A 1 450 ? 156.129 184.641 160.294 1.00 34.92  ? 450 THR A OG1 1 
ATOM   3075 C CG2 . THR A 1 450 ? 155.260 186.694 159.377 1.00 45.99  ? 450 THR A CG2 1 
ATOM   3076 N N   . ILE A 1 451 ? 158.795 184.027 159.964 1.00 32.99  ? 451 ILE A N   1 
ATOM   3077 C CA  . ILE A 1 451 ? 159.663 183.088 160.664 1.00 33.83  ? 451 ILE A CA  1 
ATOM   3078 C C   . ILE A 1 451 ? 161.120 183.405 160.369 1.00 37.13  ? 451 ILE A C   1 
ATOM   3079 O O   . ILE A 1 451 ? 161.511 183.608 159.213 1.00 38.78  ? 451 ILE A O   1 
ATOM   3080 C CB  . ILE A 1 451 ? 159.316 181.645 160.270 1.00 18.27  ? 451 ILE A CB  1 
ATOM   3081 C CG1 . ILE A 1 451 ? 157.805 181.419 160.338 1.00 18.69  ? 451 ILE A CG1 1 
ATOM   3082 C CG2 . ILE A 1 451 ? 160.045 180.656 161.163 1.00 17.51  ? 451 ILE A CG2 1 
ATOM   3083 C CD1 . ILE A 1 451 ? 157.166 181.176 158.991 1.00 21.84  ? 451 ILE A CD1 1 
ATOM   3084 N N   . ASN A 1 452 ? 161.933 183.452 161.423 1.00 38.72  ? 452 ASN A N   1 
ATOM   3085 C CA  . ASN A 1 452 ? 163.377 183.632 161.289 1.00 37.34  ? 452 ASN A CA  1 
ATOM   3086 C C   . ASN A 1 452 ? 163.969 182.297 160.862 1.00 40.28  ? 452 ASN A C   1 
ATOM   3087 O O   . ASN A 1 452 ? 164.258 181.425 161.683 1.00 43.42  ? 452 ASN A O   1 
ATOM   3088 C CB  . ASN A 1 452 ? 163.986 184.127 162.595 1.00 44.85  ? 452 ASN A CB  1 
ATOM   3089 C CG  . ASN A 1 452 ? 165.488 184.303 162.506 1.00 45.54  ? 452 ASN A CG  1 
ATOM   3090 O OD1 . ASN A 1 452 ? 166.016 184.720 161.476 1.00 42.74  ? 452 ASN A OD1 1 
ATOM   3091 N ND2 . ASN A 1 452 ? 166.186 183.984 163.590 1.00 47.09  ? 452 ASN A ND2 1 
ATOM   3092 N N   . TRP A 1 453 ? 164.133 182.117 159.552 1.00 43.09  ? 453 TRP A N   1 
ATOM   3093 C CA  . TRP A 1 453 ? 164.603 180.796 159.063 1.00 37.07  ? 453 TRP A CA  1 
ATOM   3094 C C   . TRP A 1 453 ? 166.024 180.509 159.559 1.00 32.36  ? 453 TRP A C   1 
ATOM   3095 O O   . TRP A 1 453 ? 166.364 179.319 159.711 1.00 37.32  ? 453 TRP A O   1 
ATOM   3096 C CB  . TRP A 1 453 ? 164.483 180.713 157.536 1.00 33.25  ? 453 TRP A CB  1 
ATOM   3097 C CG  . TRP A 1 453 ? 163.045 180.631 157.102 1.00 30.71  ? 453 TRP A CG  1 
ATOM   3098 C CD1 . TRP A 1 453 ? 162.249 181.653 156.675 1.00 28.83  ? 453 TRP A CD1 1 
ATOM   3099 C CD2 . TRP A 1 453 ? 162.210 179.454 157.126 1.00 23.36  ? 453 TRP A CD2 1 
ATOM   3100 N NE1 . TRP A 1 453 ? 160.990 181.190 156.401 1.00 23.76  ? 453 TRP A NE1 1 
ATOM   3101 C CE2 . TRP A 1 453 ? 160.934 179.849 156.672 1.00 23.65  ? 453 TRP A CE2 1 
ATOM   3102 C CE3 . TRP A 1 453 ? 162.418 178.116 157.474 1.00 22.85  ? 453 TRP A CE3 1 
ATOM   3103 C CZ2 . TRP A 1 453 ? 159.876 178.951 156.561 1.00 26.23  ? 453 TRP A CZ2 1 
ATOM   3104 C CZ3 . TRP A 1 453 ? 161.370 177.230 157.366 1.00 23.72  ? 453 TRP A CZ3 1 
ATOM   3105 C CH2 . TRP A 1 453 ? 160.118 177.644 156.915 1.00 21.68  ? 453 TRP A CH2 1 
ATOM   3106 N N   . LYS A 1 454 ? 166.817 181.550 159.819 1.00 43.95  ? 454 LYS A N   1 
ATOM   3107 C CA  . LYS A 1 454 ? 168.188 181.297 160.246 1.00 44.39  ? 454 LYS A CA  1 
ATOM   3108 C C   . LYS A 1 454 ? 168.249 180.558 161.576 1.00 40.40  ? 454 LYS A C   1 
ATOM   3109 O O   . LYS A 1 454 ? 169.282 179.957 161.889 1.00 39.85  ? 454 LYS A O   1 
ATOM   3110 C CB  . LYS A 1 454 ? 168.963 182.612 160.345 1.00 50.32  ? 454 LYS A CB  1 
ATOM   3111 C CG  . LYS A 1 454 ? 168.497 183.694 159.381 1.00 52.28  ? 454 LYS A CG  1 
ATOM   3112 C CD  . LYS A 1 454 ? 168.770 183.310 157.933 1.00 62.84  ? 454 LYS A CD  1 
ATOM   3113 C CE  . LYS A 1 454 ? 167.574 183.618 157.046 1.00 60.46  ? 454 LYS A CE  1 
ATOM   3114 N NZ  . LYS A 1 454 ? 167.880 183.404 155.604 1.00 54.96  ? 454 LYS A NZ  1 
ATOM   3115 N N   . LYS A 1 455 ? 167.171 180.589 162.362 1.00 38.49  ? 455 LYS A N   1 
ATOM   3116 C CA  . LYS A 1 455 ? 167.164 179.878 163.636 1.00 37.73  ? 455 LYS A CA  1 
ATOM   3117 C C   . LYS A 1 455 ? 167.033 178.375 163.432 1.00 36.30  ? 455 LYS A C   1 
ATOM   3118 O O   . LYS A 1 455 ? 167.671 177.588 164.141 1.00 35.25  ? 455 LYS A O   1 
ATOM   3119 C CB  . LYS A 1 455 ? 166.032 180.399 164.520 1.00 46.01  ? 455 LYS A CB  1 
ATOM   3120 C CG  . LYS A 1 455 ? 166.129 179.968 165.974 1.00 48.05  ? 455 LYS A CG  1 
ATOM   3121 C CD  . LYS A 1 455 ? 164.789 180.098 166.678 1.00 43.32  ? 455 LYS A CD  1 
ATOM   3122 C CE  . LYS A 1 455 ? 163.750 179.185 166.051 1.00 41.49  ? 455 LYS A CE  1 
ATOM   3123 N NZ  . LYS A 1 455 ? 164.125 177.749 166.168 1.00 27.79  ? 455 LYS A NZ  1 
ATOM   3124 N N   . LEU A 1 456 ? 166.208 177.956 162.470 1.00 34.58  ? 456 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 456 ? 166.020 176.531 162.221 1.00 23.09  ? 456 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 456 ? 167.222 175.917 161.517 1.00 22.63  ? 456 LEU A C   1 
ATOM   3127 O O   . LEU A 1 456 ? 167.513 174.732 161.711 1.00 23.43  ? 456 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 456 ? 164.755 176.304 161.395 1.00 18.57  ? 456 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 456 ? 163.466 176.945 161.910 1.00 18.91  ? 456 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 456 ? 163.126 178.187 161.108 1.00 25.67  ? 456 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 456 ? 162.324 175.949 161.856 1.00 15.97  ? 456 LEU A CD2 1 
ATOM   3132 N N   . PHE A 1 457 ? 167.925 176.698 160.702 1.00 24.40  ? 457 PHE A N   1 
ATOM   3133 C CA  . PHE A 1 457 ? 169.041 176.171 159.931 1.00 28.28  ? 457 PHE A CA  1 
ATOM   3134 C C   . PHE A 1 457 ? 170.202 175.790 160.842 1.00 32.29  ? 457 PHE A C   1 
ATOM   3135 O O   . PHE A 1 457 ? 170.465 176.449 161.852 1.00 37.90  ? 457 PHE A O   1 
ATOM   3136 C CB  . PHE A 1 457 ? 169.500 177.198 158.898 1.00 31.62  ? 457 PHE A CB  1 
ATOM   3137 C CG  . PHE A 1 457 ? 168.500 177.447 157.806 1.00 37.29  ? 457 PHE A CG  1 
ATOM   3138 C CD1 . PHE A 1 457 ? 167.506 176.521 157.535 1.00 31.17  ? 457 PHE A CD1 1 
ATOM   3139 C CD2 . PHE A 1 457 ? 168.552 178.606 157.053 1.00 38.63  ? 457 PHE A CD2 1 
ATOM   3140 C CE1 . PHE A 1 457 ? 166.585 176.747 156.534 1.00 28.98  ? 457 PHE A CE1 1 
ATOM   3141 C CE2 . PHE A 1 457 ? 167.632 178.838 156.049 1.00 36.10  ? 457 PHE A CE2 1 
ATOM   3142 C CZ  . PHE A 1 457 ? 166.648 177.907 155.790 1.00 27.70  ? 457 PHE A CZ  1 
ATOM   3143 N N   . GLY A 1 458 ? 170.898 174.717 160.476 1.00 34.82  ? 458 GLY A N   1 
ATOM   3144 C CA  . GLY A 1 458 ? 172.051 174.264 161.228 1.00 38.25  ? 458 GLY A CA  1 
ATOM   3145 C C   . GLY A 1 458 ? 173.360 174.597 160.542 1.00 41.64  ? 458 GLY A C   1 
ATOM   3146 O O   . GLY A 1 458 ? 174.373 174.842 161.203 1.00 44.79  ? 458 GLY A O   1 
ATOM   3147 N N   . THR A 1 459 ? 173.348 174.607 159.213 1.00 44.50  ? 459 THR A N   1 
ATOM   3148 C CA  . THR A 1 459 ? 174.517 174.950 158.417 1.00 49.56  ? 459 THR A CA  1 
ATOM   3149 C C   . THR A 1 459 ? 174.440 176.413 157.999 1.00 55.09  ? 459 THR A C   1 
ATOM   3150 O O   . THR A 1 459 ? 173.380 176.900 157.597 1.00 55.80  ? 459 THR A O   1 
ATOM   3151 C CB  . THR A 1 459 ? 174.617 174.055 157.179 1.00 52.31  ? 459 THR A CB  1 
ATOM   3152 O OG1 . THR A 1 459 ? 174.595 172.679 157.579 1.00 47.49  ? 459 THR A OG1 1 
ATOM   3153 C CG2 . THR A 1 459 ? 175.907 174.331 156.419 1.00 51.53  ? 459 THR A CG2 1 
ATOM   3154 N N   . SER A 1 460 ? 175.573 177.112 158.106 1.00 59.61  ? 460 SER A N   1 
ATOM   3155 C CA  . SER A 1 460 ? 175.607 178.534 157.782 1.00 69.74  ? 460 SER A CA  1 
ATOM   3156 C C   . SER A 1 460 ? 175.331 178.804 156.308 1.00 66.94  ? 460 SER A C   1 
ATOM   3157 O O   . SER A 1 460 ? 174.887 179.905 155.966 1.00 58.79  ? 460 SER A O   1 
ATOM   3158 C CB  . SER A 1 460 ? 176.961 179.127 158.175 1.00 64.37  ? 460 SER A CB  1 
ATOM   3159 O OG  . SER A 1 460 ? 177.163 179.052 159.575 1.00 63.84  ? 460 SER A OG  1 
ATOM   3160 N N   . GLY A 1 461 ? 175.581 177.832 155.431 1.00 63.90  ? 461 GLY A N   1 
ATOM   3161 C CA  . GLY A 1 461 ? 175.367 178.031 154.010 1.00 59.38  ? 461 GLY A CA  1 
ATOM   3162 C C   . GLY A 1 461 ? 173.932 177.920 153.545 1.00 62.88  ? 461 GLY A C   1 
ATOM   3163 O O   . GLY A 1 461 ? 173.653 178.205 152.377 1.00 62.96  ? 461 GLY A O   1 
ATOM   3164 N N   . GLN A 1 462 ? 173.020 177.512 154.423 1.00 58.42  ? 462 GLN A N   1 
ATOM   3165 C CA  . GLN A 1 462 ? 171.620 177.379 154.043 1.00 48.76  ? 462 GLN A CA  1 
ATOM   3166 C C   . GLN A 1 462 ? 170.994 178.747 153.802 1.00 49.59  ? 462 GLN A C   1 
ATOM   3167 O O   . GLN A 1 462 ? 171.264 179.711 154.524 1.00 57.16  ? 462 GLN A O   1 
ATOM   3168 C CB  . GLN A 1 462 ? 170.845 176.630 155.125 1.00 40.07  ? 462 GLN A CB  1 
ATOM   3169 C CG  . GLN A 1 462 ? 171.435 175.278 155.484 1.00 37.95  ? 462 GLN A CG  1 
ATOM   3170 C CD  . GLN A 1 462 ? 170.792 174.672 156.714 1.00 35.94  ? 462 GLN A CD  1 
ATOM   3171 O OE1 . GLN A 1 462 ? 171.321 174.775 157.819 1.00 41.51  ? 462 GLN A OE1 1 
ATOM   3172 N NE2 . GLN A 1 462 ? 169.643 174.035 156.527 1.00 32.84  ? 462 GLN A NE2 1 
ATOM   3173 N N   . LYS A 1 463 ? 170.124 178.811 152.791 1.00 40.84  ? 463 LYS A N   1 
ATOM   3174 C CA  . LYS A 1 463 ? 169.407 180.074 152.485 1.00 38.44  ? 463 LYS A CA  1 
ATOM   3175 C C   . LYS A 1 463 ? 167.901 179.783 152.468 1.00 34.54  ? 463 LYS A C   1 
ATOM   3176 O O   . LYS A 1 463 ? 167.508 178.682 152.897 1.00 30.26  ? 463 LYS A O   1 
ATOM   3177 C CB  . LYS A 1 463 ? 169.850 180.617 151.125 1.00 41.04  ? 463 LYS A CB  1 
ATOM   3178 C CG  . LYS A 1 463 ? 169.915 179.570 150.023 1.00 41.39  ? 463 LYS A CG  1 
ATOM   3179 C CD  . LYS A 1 463 ? 169.679 180.124 148.623 1.00 44.72  ? 463 LYS A CD  1 
ATOM   3180 C CE  . LYS A 1 463 ? 168.250 180.508 148.402 1.00 45.37  ? 463 LYS A CE  1 
ATOM   3181 N NZ  . LYS A 1 463 ? 167.358 179.355 148.545 1.00 35.02  ? 463 LYS A NZ  1 
ATOM   3182 N N   . THR A 1 464 ? 167.092 180.739 152.010 1.00 32.77  ? 464 THR A N   1 
ATOM   3183 C CA  . THR A 1 464 ? 165.634 180.526 151.904 1.00 23.66  ? 464 THR A CA  1 
ATOM   3184 C C   . THR A 1 464 ? 165.147 181.256 150.675 1.00 29.05  ? 464 THR A C   1 
ATOM   3185 O O   . THR A 1 464 ? 165.569 182.414 150.476 1.00 40.08  ? 464 THR A O   1 
ATOM   3186 C CB  . THR A 1 464 ? 164.931 181.017 153.168 1.00 28.92  ? 464 THR A CB  1 
ATOM   3187 O OG1 . THR A 1 464 ? 165.554 180.353 154.261 1.00 31.31  ? 464 THR A OG1 1 
ATOM   3188 C CG2 . THR A 1 464 ? 163.449 180.689 153.175 1.00 24.20  ? 464 THR A CG2 1 
ATOM   3189 N N   . LYS A 1 465 ? 164.296 180.615 149.872 1.00 23.48  ? 465 LYS A N   1 
ATOM   3190 C CA  . LYS A 1 465 ? 163.829 181.243 148.610 1.00 22.35  ? 465 LYS A CA  1 
ATOM   3191 C C   . LYS A 1 465 ? 162.314 181.487 148.690 1.00 22.20  ? 465 LYS A C   1 
ATOM   3192 O O   . LYS A 1 465 ? 161.597 181.042 147.770 1.00 26.40  ? 465 LYS A O   1 
ATOM   3193 C CB  . LYS A 1 465 ? 164.191 180.358 147.412 1.00 26.92  ? 465 LYS A CB  1 
ATOM   3194 C CG  . LYS A 1 465 ? 164.209 181.054 146.060 1.00 34.43  ? 465 LYS A CG  1 
ATOM   3195 C CD  . LYS A 1 465 ? 164.633 180.131 144.925 1.00 36.64  ? 465 LYS A CD  1 
ATOM   3196 C CE  . LYS A 1 465 ? 165.995 179.556 145.149 1.00 37.47  ? 465 LYS A CE  1 
ATOM   3197 N NZ  . LYS A 1 465 ? 166.425 178.735 144.015 1.00 33.00  ? 465 LYS A NZ  1 
ATOM   3198 N N   . ILE A 1 466 ? 161.846 182.168 149.740 1.00 23.35  ? 466 ILE A N   1 
ATOM   3199 C CA  . ILE A 1 466 ? 160.393 182.513 149.805 1.00 24.60  ? 466 ILE A CA  1 
ATOM   3200 C C   . ILE A 1 466 ? 160.123 183.641 148.799 1.00 25.67  ? 466 ILE A C   1 
ATOM   3201 O O   . ILE A 1 466 ? 160.496 184.795 149.096 1.00 28.99  ? 466 ILE A O   1 
ATOM   3202 C CB  . ILE A 1 466 ? 159.961 182.891 151.232 1.00 23.40  ? 466 ILE A CB  1 
ATOM   3203 C CG1 . ILE A 1 466 ? 160.246 181.765 152.216 1.00 25.11  ? 466 ILE A CG1 1 
ATOM   3204 C CG2 . ILE A 1 466 ? 158.489 183.300 151.263 1.00 22.73  ? 466 ILE A CG2 1 
ATOM   3205 C CD1 . ILE A 1 466 ? 159.576 181.944 153.564 1.00 26.38  ? 466 ILE A CD1 1 
ATOM   3206 N N   . ILE A 1 467 ? 159.509 183.316 147.662 1.00 25.10  ? 467 ILE A N   1 
ATOM   3207 C CA  . ILE A 1 467 ? 159.227 184.284 146.609 1.00 31.01  ? 467 ILE A CA  1 
ATOM   3208 C C   . ILE A 1 467 ? 157.873 183.971 145.990 1.00 32.58  ? 467 ILE A C   1 
ATOM   3209 O O   . ILE A 1 467 ? 157.434 182.818 145.959 1.00 31.86  ? 467 ILE A O   1 
ATOM   3210 C CB  . ILE A 1 467 ? 160.321 184.290 145.517 1.00 33.47  ? 467 ILE A CB  1 
ATOM   3211 C CG1 . ILE A 1 467 ? 160.698 182.857 145.135 1.00 30.24  ? 467 ILE A CG1 1 
ATOM   3212 C CG2 . ILE A 1 467 ? 161.541 185.076 145.976 1.00 33.27  ? 467 ILE A CG2 1 
ATOM   3213 C CD1 . ILE A 1 467 ? 161.777 182.770 144.078 1.00 31.02  ? 467 ILE A CD1 1 
ATOM   3214 N N   . SER A 1 468 ? 157.212 185.017 145.491 1.00 36.03  ? 468 SER A N   1 
ATOM   3215 C CA  . SER A 1 468 ? 155.961 184.905 144.742 1.00 40.11  ? 468 SER A CA  1 
ATOM   3216 C C   . SER A 1 468 ? 154.816 184.347 145.585 1.00 35.08  ? 468 SER A C   1 
ATOM   3217 O O   . SER A 1 468 ? 153.904 183.709 145.055 1.00 32.50  ? 468 SER A O   1 
ATOM   3218 C CB  . SER A 1 468 ? 156.141 184.062 143.474 1.00 41.59  ? 468 SER A CB  1 
ATOM   3219 O OG  . SER A 1 468 ? 154.893 183.597 142.991 1.00 47.12  ? 468 SER A OG  1 
ATOM   3220 N N   . ASN A 1 469 ? 154.859 184.597 146.893 1.00 37.56  ? 469 ASN A N   1 
ATOM   3221 C CA  . ASN A 1 469 ? 153.694 184.223 147.736 1.00 37.55  ? 469 ASN A CA  1 
ATOM   3222 C C   . ASN A 1 469 ? 152.865 185.501 147.895 1.00 43.02  ? 469 ASN A C   1 
ATOM   3223 O O   . ASN A 1 469 ? 153.237 186.521 147.278 1.00 53.30  ? 469 ASN A O   1 
ATOM   3224 C CB  . ASN A 1 469 ? 154.109 183.612 149.069 1.00 39.62  ? 469 ASN A CB  1 
ATOM   3225 C CG  . ASN A 1 469 ? 155.163 182.544 148.913 1.00 30.96  ? 469 ASN A CG  1 
ATOM   3226 O OD1 . ASN A 1 469 ? 156.283 182.836 148.484 1.00 31.19  ? 469 ASN A OD1 1 
ATOM   3227 N ND2 . ASN A 1 469 ? 154.838 181.313 149.277 1.00 30.40  ? 469 ASN A ND2 1 
ATOM   3228 N N   . ARG A 1 470 ? 151.798 185.462 148.689 1.00 43.12  ? 470 ARG A N   1 
ATOM   3229 C CA  . ARG A 1 470 ? 150.963 186.635 148.906 1.00 43.86  ? 470 ARG A CA  1 
ATOM   3230 C C   . ARG A 1 470 ? 151.806 187.754 149.504 1.00 49.39  ? 470 ARG A C   1 
ATOM   3231 O O   . ARG A 1 470 ? 152.572 187.531 150.446 1.00 52.84  ? 470 ARG A O   1 
ATOM   3232 C CB  . ARG A 1 470 ? 149.790 186.294 149.824 1.00 39.64  ? 470 ARG A CB  1 
ATOM   3233 C CG  . ARG A 1 470 ? 148.961 187.493 150.252 1.00 42.86  ? 470 ARG A CG  1 
ATOM   3234 C CD  . ARG A 1 470 ? 147.480 187.155 150.291 1.00 38.20  ? 470 ARG A CD  1 
ATOM   3235 N NE  . ARG A 1 470 ? 147.206 185.982 151.112 1.00 43.54  ? 470 ARG A NE  1 
ATOM   3236 C CZ  . ARG A 1 470 ? 146.041 185.730 151.693 1.00 53.88  ? 470 ARG A CZ  1 
ATOM   3237 N NH1 . ARG A 1 470 ? 145.014 186.553 151.567 1.00 58.28  ? 470 ARG A NH1 1 
ATOM   3238 N NH2 . ARG A 1 470 ? 145.904 184.623 152.418 1.00 49.29  ? 470 ARG A NH2 1 
ATOM   3239 N N   . GLY A 1 471 ? 151.669 188.957 148.949 1.00 50.92  ? 471 GLY A N   1 
ATOM   3240 C CA  . GLY A 1 471 ? 152.520 190.055 149.366 1.00 52.21  ? 471 GLY A CA  1 
ATOM   3241 C C   . GLY A 1 471 ? 152.311 190.418 150.823 1.00 64.38  ? 471 GLY A C   1 
ATOM   3242 O O   . GLY A 1 471 ? 151.206 190.324 151.360 1.00 68.14  ? 471 GLY A O   1 
ATOM   3243 N N   . GLU A 1 472 ? 153.403 190.838 151.468 1.00 68.60  ? 472 GLU A N   1 
ATOM   3244 C CA  . GLU A 1 472 ? 153.335 191.215 152.877 1.00 63.79  ? 472 GLU A CA  1 
ATOM   3245 C C   . GLU A 1 472 ? 152.410 192.407 153.083 1.00 65.95  ? 472 GLU A C   1 
ATOM   3246 O O   . GLU A 1 472 ? 151.684 192.474 154.082 1.00 66.11  ? 472 GLU A O   1 
ATOM   3247 C CB  . GLU A 1 472 ? 154.735 191.524 153.408 1.00 58.34  ? 472 GLU A CB  1 
ATOM   3248 C CG  . GLU A 1 472 ? 155.818 190.594 152.888 1.00 62.63  ? 472 GLU A CG  1 
ATOM   3249 C CD  . GLU A 1 472 ? 157.173 190.879 153.505 1.00 65.26  ? 472 GLU A CD  1 
ATOM   3250 O OE1 . GLU A 1 472 ? 157.540 192.068 153.616 1.00 71.75  ? 472 GLU A OE1 1 
ATOM   3251 O OE2 . GLU A 1 472 ? 157.872 189.915 153.881 1.00 53.35  ? 472 GLU A OE2 1 
ATOM   3252 N N   . ASN A 1 473 ? 152.433 193.365 152.153 1.00 67.44  ? 473 ASN A N   1 
ATOM   3253 C CA  . ASN A 1 473 ? 151.517 194.497 152.231 1.00 69.27  ? 473 ASN A CA  1 
ATOM   3254 C C   . ASN A 1 473 ? 150.068 194.026 152.208 1.00 63.90  ? 473 ASN A C   1 
ATOM   3255 O O   . ASN A 1 473 ? 149.267 194.405 153.067 1.00 62.05  ? 473 ASN A O   1 
ATOM   3256 C CB  . ASN A 1 473 ? 151.791 195.472 151.087 1.00 72.06  ? 473 ASN A CB  1 
ATOM   3257 C CG  . ASN A 1 473 ? 153.273 195.686 150.849 1.00 71.47  ? 473 ASN A CG  1 
ATOM   3258 O OD1 . ASN A 1 473 ? 153.835 195.188 149.873 1.00 67.74  ? 473 ASN A OD1 1 
ATOM   3259 N ND2 . ASN A 1 473 ? 153.915 196.426 151.746 1.00 67.67  ? 473 ASN A ND2 1 
ATOM   3260 N N   . SER A 1 474 ? 149.719 193.171 151.244 1.00 63.91  ? 474 SER A N   1 
ATOM   3261 C CA  . SER A 1 474 ? 148.377 192.596 151.225 1.00 67.19  ? 474 SER A CA  1 
ATOM   3262 C C   . SER A 1 474 ? 148.151 191.667 152.412 1.00 64.40  ? 474 SER A C   1 
ATOM   3263 O O   . SER A 1 474 ? 147.029 191.587 152.930 1.00 64.58  ? 474 SER A O   1 
ATOM   3264 C CB  . SER A 1 474 ? 148.141 191.851 149.911 1.00 58.16  ? 474 SER A CB  1 
ATOM   3265 O OG  . SER A 1 474 ? 149.070 190.794 149.748 1.00 58.42  ? 474 SER A OG  1 
ATOM   3266 N N   . CYS A 1 475 ? 149.204 190.977 152.861 1.00 64.49  ? 475 CYS A N   1 
ATOM   3267 C CA  . CYS A 1 475 ? 149.087 190.070 153.999 1.00 61.57  ? 475 CYS A CA  1 
ATOM   3268 C C   . CYS A 1 475 ? 148.617 190.812 155.244 1.00 66.70  ? 475 CYS A C   1 
ATOM   3269 O O   . CYS A 1 475 ? 147.741 190.334 155.975 1.00 68.27  ? 475 CYS A O   1 
ATOM   3270 C CB  . CYS A 1 475 ? 150.436 189.387 154.248 1.00 58.28  ? 475 CYS A CB  1 
ATOM   3271 S SG  . CYS A 1 475 ? 150.446 188.025 155.444 1.00 72.88  ? 475 CYS A SG  1 
ATOM   3272 N N   . LYS A 1 476 ? 149.194 191.987 155.503 1.00 66.82  ? 476 LYS A N   1 
ATOM   3273 C CA  . LYS A 1 476 ? 148.756 192.807 156.626 1.00 64.62  ? 476 LYS A CA  1 
ATOM   3274 C C   . LYS A 1 476 ? 147.509 193.623 156.310 1.00 72.40  ? 476 LYS A C   1 
ATOM   3275 O O   . LYS A 1 476 ? 146.796 194.018 157.239 1.00 76.86  ? 476 LYS A O   1 
ATOM   3276 C CB  . LYS A 1 476 ? 149.891 193.734 157.075 1.00 59.02  ? 476 LYS A CB  1 
ATOM   3277 C CG  . LYS A 1 476 ? 150.302 194.773 156.048 1.00 63.54  ? 476 LYS A CG  1 
ATOM   3278 C CD  . LYS A 1 476 ? 151.465 195.611 156.549 1.00 63.08  ? 476 LYS A CD  1 
ATOM   3279 C CE  . LYS A 1 476 ? 152.683 194.746 156.819 1.00 65.23  ? 476 LYS A CE  1 
ATOM   3280 N NZ  . LYS A 1 476 ? 153.661 194.802 155.699 1.00 58.16  ? 476 LYS A NZ  1 
ATOM   3281 N N   . ALA A 1 477 ? 147.227 193.880 155.030 1.00 68.58  ? 477 ALA A N   1 
ATOM   3282 C CA  . ALA A 1 477 ? 146.033 194.639 154.673 1.00 66.90  ? 477 ALA A CA  1 
ATOM   3283 C C   . ALA A 1 477 ? 144.764 193.829 154.903 1.00 74.85  ? 477 ALA A C   1 
ATOM   3284 O O   . ALA A 1 477 ? 143.754 194.368 155.370 1.00 75.60  ? 477 ALA A O   1 
ATOM   3285 C CB  . ALA A 1 477 ? 146.117 195.098 153.217 1.00 63.19  ? 477 ALA A CB  1 
ATOM   3286 N N   . THR A 1 478 ? 144.790 192.536 154.582 1.00 75.52  ? 478 THR A N   1 
ATOM   3287 C CA  . THR A 1 478 ? 143.606 191.700 154.751 1.00 75.22  ? 478 THR A CA  1 
ATOM   3288 C C   . THR A 1 478 ? 143.366 191.299 156.202 1.00 71.75  ? 478 THR A C   1 
ATOM   3289 O O   . THR A 1 478 ? 142.528 190.427 156.457 1.00 73.58  ? 478 THR A O   1 
ATOM   3290 C CB  . THR A 1 478 ? 143.708 190.439 153.886 1.00 74.74  ? 478 THR A CB  1 
ATOM   3291 O OG1 . THR A 1 478 ? 142.566 189.607 154.124 1.00 78.55  ? 478 THR A OG1 1 
ATOM   3292 C CG2 . THR A 1 478 ? 144.959 189.655 154.237 1.00 68.33  ? 478 THR A CG2 1 
ATOM   3293 N N   . GLY A 1 479 ? 144.074 191.906 157.151 1.00 66.75  ? 479 GLY A N   1 
ATOM   3294 C CA  . GLY A 1 479 ? 143.926 191.552 158.547 1.00 66.92  ? 479 GLY A CA  1 
ATOM   3295 C C   . GLY A 1 479 ? 144.582 190.252 158.943 1.00 67.43  ? 479 GLY A C   1 
ATOM   3296 O O   . GLY A 1 479 ? 144.370 189.787 160.068 1.00 67.54  ? 479 GLY A O   1 
ATOM   3297 N N   . GLN A 1 480 ? 145.370 189.650 158.056 1.00 69.66  ? 480 GLN A N   1 
ATOM   3298 C CA  . GLN A 1 480 ? 146.012 188.367 158.330 1.00 67.41  ? 480 GLN A CA  1 
ATOM   3299 C C   . GLN A 1 480 ? 147.426 188.601 158.861 1.00 64.11  ? 480 GLN A C   1 
ATOM   3300 O O   . GLN A 1 480 ? 148.433 188.411 158.178 1.00 59.24  ? 480 GLN A O   1 
ATOM   3301 C CB  . GLN A 1 480 ? 146.016 187.501 157.075 1.00 64.56  ? 480 GLN A CB  1 
ATOM   3302 C CG  . GLN A 1 480 ? 144.680 186.860 156.751 1.00 63.26  ? 480 GLN A CG  1 
ATOM   3303 C CD  . GLN A 1 480 ? 144.836 185.522 156.059 1.00 60.79  ? 480 GLN A CD  1 
ATOM   3304 O OE1 . GLN A 1 480 ? 145.025 185.456 154.845 1.00 70.60  ? 480 GLN A OE1 1 
ATOM   3305 N NE2 . GLN A 1 480 ? 144.756 184.444 156.830 1.00 57.74  ? 480 GLN A NE2 1 
ATOM   3306 N N   . VAL A 1 481 ? 147.474 189.030 160.118 1.00 69.51  ? 481 VAL A N   1 
ATOM   3307 C CA  . VAL A 1 481 ? 148.716 189.243 160.850 1.00 66.54  ? 481 VAL A CA  1 
ATOM   3308 C C   . VAL A 1 481 ? 148.661 188.385 162.106 1.00 62.06  ? 481 VAL A C   1 
ATOM   3309 O O   . VAL A 1 481 ? 147.616 188.309 162.762 1.00 71.63  ? 481 VAL A O   1 
ATOM   3310 C CB  . VAL A 1 481 ? 148.924 190.731 161.193 1.00 62.36  ? 481 VAL A CB  1 
ATOM   3311 C CG1 . VAL A 1 481 ? 149.804 190.893 162.424 1.00 54.65  ? 481 VAL A CG1 1 
ATOM   3312 C CG2 . VAL A 1 481 ? 149.532 191.462 160.008 1.00 62.25  ? 481 VAL A CG2 1 
ATOM   3313 N N   . CYS A 1 482 ? 149.776 187.729 162.426 1.00 45.94  ? 482 CYS A N   1 
ATOM   3314 C CA  . CYS A 1 482 ? 149.821 186.798 163.544 1.00 45.36  ? 482 CYS A CA  1 
ATOM   3315 C C   . CYS A 1 482 ? 149.460 187.503 164.851 1.00 44.75  ? 482 CYS A C   1 
ATOM   3316 O O   . CYS A 1 482 ? 149.442 188.734 164.950 1.00 49.77  ? 482 CYS A O   1 
ATOM   3317 C CB  . CYS A 1 482 ? 151.200 186.157 163.647 1.00 51.76  ? 482 CYS A CB  1 
ATOM   3318 S SG  . CYS A 1 482 ? 151.341 184.965 164.994 1.00 62.76  ? 482 CYS A SG  1 
ATOM   3319 N N   . HIS A 1 483 ? 149.181 186.697 165.873 1.00 34.87  ? 483 HIS A N   1 
ATOM   3320 C CA  . HIS A 1 483 ? 148.707 187.228 167.142 1.00 34.70  ? 483 HIS A CA  1 
ATOM   3321 C C   . HIS A 1 483 ? 149.771 188.093 167.803 1.00 33.20  ? 483 HIS A C   1 
ATOM   3322 O O   . HIS A 1 483 ? 150.974 187.904 167.602 1.00 34.76  ? 483 HIS A O   1 
ATOM   3323 C CB  . HIS A 1 483 ? 148.308 186.089 168.080 1.00 25.70  ? 483 HIS A CB  1 
ATOM   3324 C CG  . HIS A 1 483 ? 146.847 185.766 168.051 1.00 35.16  ? 483 HIS A CG  1 
ATOM   3325 N ND1 . HIS A 1 483 ? 146.056 185.795 169.179 1.00 44.38  ? 483 HIS A ND1 1 
ATOM   3326 C CD2 . HIS A 1 483 ? 146.034 185.406 167.030 1.00 38.99  ? 483 HIS A CD2 1 
ATOM   3327 C CE1 . HIS A 1 483 ? 144.818 185.467 168.855 1.00 50.11  ? 483 HIS A CE1 1 
ATOM   3328 N NE2 . HIS A 1 483 ? 144.778 185.226 167.556 1.00 42.39  ? 483 HIS A NE2 1 
ATOM   3329 N N   . ALA A 1 484 ? 149.310 189.068 168.591 1.00 31.04  ? 484 ALA A N   1 
ATOM   3330 C CA  . ALA A 1 484 ? 150.234 189.895 169.357 1.00 33.22  ? 484 ALA A CA  1 
ATOM   3331 C C   . ALA A 1 484 ? 151.037 189.059 170.343 1.00 38.34  ? 484 ALA A C   1 
ATOM   3332 O O   . ALA A 1 484 ? 152.171 189.416 170.679 1.00 43.73  ? 484 ALA A O   1 
ATOM   3333 C CB  . ALA A 1 484 ? 149.470 190.998 170.090 1.00 41.26  ? 484 ALA A CB  1 
ATOM   3334 N N   . LEU A 1 485 ? 150.458 187.930 170.772 1.00 37.93  ? 485 LEU A N   1 
ATOM   3335 C CA  . LEU A 1 485 ? 151.158 187.003 171.700 1.00 30.84  ? 485 LEU A CA  1 
ATOM   3336 C C   . LEU A 1 485 ? 152.181 186.189 170.900 1.00 29.53  ? 485 LEU A C   1 
ATOM   3337 O O   . LEU A 1 485 ? 152.030 184.952 170.843 1.00 32.80  ? 485 LEU A O   1 
ATOM   3338 C CB  . LEU A 1 485 ? 150.121 186.090 172.345 1.00 30.17  ? 485 LEU A CB  1 
ATOM   3339 C CG  . LEU A 1 485 ? 148.803 186.749 172.761 1.00 38.09  ? 485 LEU A CG  1 
ATOM   3340 C CD1 . LEU A 1 485 ? 147.827 185.701 173.265 1.00 37.57  ? 485 LEU A CD1 1 
ATOM   3341 C CD2 . LEU A 1 485 ? 149.046 187.806 173.820 1.00 37.07  ? 485 LEU A CD2 1 
ATOM   3342 N N   . CYS A 1 486 ? 153.139 186.861 170.264 1.00 31.03  ? 486 CYS A N   1 
ATOM   3343 C CA  . CYS A 1 486 ? 154.122 186.148 169.415 1.00 33.74  ? 486 CYS A CA  1 
ATOM   3344 C C   . CYS A 1 486 ? 155.407 186.978 169.341 1.00 38.49  ? 486 CYS A C   1 
ATOM   3345 O O   . CYS A 1 486 ? 155.364 188.083 168.764 1.00 46.17  ? 486 CYS A O   1 
ATOM   3346 C CB  . CYS A 1 486 ? 153.569 185.931 168.013 1.00 31.84  ? 486 CYS A CB  1 
ATOM   3347 S SG  . CYS A 1 486 ? 154.131 184.395 167.235 1.00 42.54  ? 486 CYS A SG  1 
ATOM   3348 N N   . SER A 1 487 ? 156.499 186.460 169.902 1.00 37.25  ? 487 SER A N   1 
ATOM   3349 C CA  . SER A 1 487 ? 157.800 187.170 169.845 1.00 38.83  ? 487 SER A CA  1 
ATOM   3350 C C   . SER A 1 487 ? 158.150 187.438 168.377 1.00 41.19  ? 487 SER A C   1 
ATOM   3351 O O   . SER A 1 487 ? 157.775 186.613 167.517 1.00 43.44  ? 487 SER A O   1 
ATOM   3352 C CB  . SER A 1 487 ? 158.870 186.367 170.531 1.00 41.49  ? 487 SER A CB  1 
ATOM   3353 O OG  . SER A 1 487 ? 160.154 186.951 170.361 1.00 41.71  ? 487 SER A OG  1 
ATOM   3354 N N   . PRO A 1 488 ? 158.865 188.535 168.050 1.00 43.92  ? 488 PRO A N   1 
ATOM   3355 C CA  . PRO A 1 488 ? 159.268 188.797 166.675 1.00 47.87  ? 488 PRO A CA  1 
ATOM   3356 C C   . PRO A 1 488 ? 159.915 187.602 165.979 1.00 49.91  ? 488 PRO A C   1 
ATOM   3357 O O   . PRO A 1 488 ? 160.100 187.660 164.747 1.00 48.13  ? 488 PRO A O   1 
ATOM   3358 C CB  . PRO A 1 488 ? 160.256 189.960 166.852 1.00 43.94  ? 488 PRO A CB  1 
ATOM   3359 C CG  . PRO A 1 488 ? 159.732 190.696 168.060 1.00 43.08  ? 488 PRO A CG  1 
ATOM   3360 C CD  . PRO A 1 488 ? 159.260 189.584 168.979 1.00 45.31  ? 488 PRO A CD  1 
ATOM   3361 N N   . GLU A 1 489 ? 160.248 186.549 166.735 1.00 43.71  ? 489 GLU A N   1 
ATOM   3362 C CA  . GLU A 1 489 ? 160.907 185.352 166.150 1.00 42.47  ? 489 GLU A CA  1 
ATOM   3363 C C   . GLU A 1 489 ? 160.139 184.930 164.890 1.00 41.94  ? 489 GLU A C   1 
ATOM   3364 O O   . GLU A 1 489 ? 160.800 184.623 163.874 1.00 43.10  ? 489 GLU A O   1 
ATOM   3365 C CB  . GLU A 1 489 ? 160.984 184.220 167.173 1.00 38.65  ? 489 GLU A CB  1 
ATOM   3366 C CG  . GLU A 1 489 ? 161.946 184.518 168.319 1.00 40.98  ? 489 GLU A CG  1 
ATOM   3367 C CD  . GLU A 1 489 ? 162.594 183.284 168.919 1.00 46.67  ? 489 GLU A CD  1 
ATOM   3368 O OE1 . GLU A 1 489 ? 162.314 182.170 168.429 1.00 42.71  ? 489 GLU A OE1 1 
ATOM   3369 O OE2 . GLU A 1 489 ? 163.378 183.438 169.878 1.00 45.43  ? 489 GLU A OE2 1 
ATOM   3370 N N   . GLY A 1 490 ? 158.805 184.920 164.948 1.00 36.43  ? 490 GLY A N   1 
ATOM   3371 C CA  . GLY A 1 490 ? 158.024 184.620 163.733 1.00 32.47  ? 490 GLY A CA  1 
ATOM   3372 C C   . GLY A 1 490 ? 156.703 183.956 164.045 1.00 35.41  ? 490 GLY A C   1 
ATOM   3373 O O   . GLY A 1 490 ? 156.403 183.773 165.241 1.00 38.33  ? 490 GLY A O   1 
ATOM   3374 N N   . CYS A 1 491 ? 155.942 183.609 163.005 1.00 35.64  ? 491 CYS A N   1 
ATOM   3375 C CA  . CYS A 1 491 ? 154.643 182.917 163.188 1.00 29.28  ? 491 CYS A CA  1 
ATOM   3376 C C   . CYS A 1 491 ? 154.440 181.954 162.017 1.00 24.69  ? 491 CYS A C   1 
ATOM   3377 O O   . CYS A 1 491 ? 154.773 182.330 160.877 1.00 27.06  ? 491 CYS A O   1 
ATOM   3378 C CB  . CYS A 1 491 ? 153.482 183.897 163.165 1.00 32.20  ? 491 CYS A CB  1 
ATOM   3379 S SG  . CYS A 1 491 ? 152.004 183.307 164.029 1.00 38.34  ? 491 CYS A SG  1 
ATOM   3380 N N   . TRP A 1 492 ? 153.897 180.769 162.293 1.00 25.00  ? 492 TRP A N   1 
ATOM   3381 C CA  . TRP A 1 492 ? 153.626 179.804 161.197 1.00 19.80  ? 492 TRP A CA  1 
ATOM   3382 C C   . TRP A 1 492 ? 152.210 179.987 160.646 1.00 22.57  ? 492 TRP A C   1 
ATOM   3383 O O   . TRP A 1 492 ? 151.953 179.510 159.524 1.00 23.26  ? 492 TRP A O   1 
ATOM   3384 C CB  . TRP A 1 492 ? 153.831 178.368 161.696 1.00 15.66  ? 492 TRP A CB  1 
ATOM   3385 C CG  . TRP A 1 492 ? 155.255 178.050 162.060 1.00 16.59  ? 492 TRP A CG  1 
ATOM   3386 C CD1 . TRP A 1 492 ? 155.818 178.082 163.302 1.00 17.51  ? 492 TRP A CD1 1 
ATOM   3387 C CD2 . TRP A 1 492 ? 156.309 177.669 161.150 1.00 13.19  ? 492 TRP A CD2 1 
ATOM   3388 N NE1 . TRP A 1 492 ? 157.140 177.735 163.232 1.00 13.68  ? 492 TRP A NE1 1 
ATOM   3389 C CE2 . TRP A 1 492 ? 157.472 177.480 161.927 1.00 12.14  ? 492 TRP A CE2 1 
ATOM   3390 C CE3 . TRP A 1 492 ? 156.381 177.468 159.768 1.00 9.58   ? 492 TRP A CE3 1 
ATOM   3391 C CZ2 . TRP A 1 492 ? 158.687 177.101 161.363 1.00 11.55  ? 492 TRP A CZ2 1 
ATOM   3392 C CZ3 . TRP A 1 492 ? 157.584 177.095 159.213 1.00 9.21   ? 492 TRP A CZ3 1 
ATOM   3393 C CH2 . TRP A 1 492 ? 158.719 176.916 160.001 1.00 11.20  ? 492 TRP A CH2 1 
ATOM   3394 N N   . GLY A 1 493 ? 151.328 180.656 161.395 1.00 26.50  ? 493 GLY A N   1 
ATOM   3395 C CA  . GLY A 1 493 ? 149.924 180.789 160.962 1.00 25.68  ? 493 GLY A CA  1 
ATOM   3396 C C   . GLY A 1 493 ? 149.214 181.967 161.597 1.00 33.20  ? 493 GLY A C   1 
ATOM   3397 O O   . GLY A 1 493 ? 149.903 182.921 162.007 1.00 38.86  ? 493 GLY A O   1 
ATOM   3398 N N   . PRO A 1 494 ? 147.867 181.949 161.706 1.00 33.93  ? 494 PRO A N   1 
ATOM   3399 C CA  . PRO A 1 494 ? 147.097 183.097 162.199 1.00 38.83  ? 494 PRO A CA  1 
ATOM   3400 C C   . PRO A 1 494 ? 146.818 183.069 163.695 1.00 36.99  ? 494 PRO A C   1 
ATOM   3401 O O   . PRO A 1 494 ? 146.308 184.050 164.245 1.00 33.76  ? 494 PRO A O   1 
ATOM   3402 C CB  . PRO A 1 494 ? 145.796 182.996 161.397 1.00 41.96  ? 494 PRO A CB  1 
ATOM   3403 C CG  . PRO A 1 494 ? 145.626 181.518 161.155 1.00 33.73  ? 494 PRO A CG  1 
ATOM   3404 C CD  . PRO A 1 494 ? 146.991 180.863 161.234 1.00 31.34  ? 494 PRO A CD  1 
ATOM   3405 N N   . GLU A 1 495 ? 147.141 181.970 164.364 1.00 33.90  ? 495 GLU A N   1 
ATOM   3406 C CA  . GLU A 1 495 ? 146.802 181.769 165.763 1.00 28.97  ? 495 GLU A CA  1 
ATOM   3407 C C   . GLU A 1 495 ? 148.062 181.597 166.603 1.00 27.52  ? 495 GLU A C   1 
ATOM   3408 O O   . GLU A 1 495 ? 149.131 181.272 166.075 1.00 28.13  ? 495 GLU A O   1 
ATOM   3409 C CB  . GLU A 1 495 ? 145.886 180.547 165.930 1.00 27.21  ? 495 GLU A CB  1 
ATOM   3410 C CG  . GLU A 1 495 ? 146.202 179.389 165.009 1.00 32.87  ? 495 GLU A CG  1 
ATOM   3411 C CD  . GLU A 1 495 ? 145.751 178.058 165.576 1.00 45.04  ? 495 GLU A CD  1 
ATOM   3412 O OE1 . GLU A 1 495 ? 145.338 178.023 166.754 1.00 44.19  ? 495 GLU A OE1 1 
ATOM   3413 O OE2 . GLU A 1 495 ? 145.810 177.047 164.844 1.00 52.64  ? 495 GLU A OE2 1 
ATOM   3414 N N   . PRO A 1 496 ? 147.975 181.822 167.920 1.00 30.16  ? 496 PRO A N   1 
ATOM   3415 C CA  . PRO A 1 496 ? 149.173 181.688 168.768 1.00 22.07  ? 496 PRO A CA  1 
ATOM   3416 C C   . PRO A 1 496 ? 149.769 180.293 168.777 1.00 30.74  ? 496 PRO A C   1 
ATOM   3417 O O   . PRO A 1 496 ? 150.936 180.141 169.159 1.00 37.98  ? 496 PRO A O   1 
ATOM   3418 C CB  . PRO A 1 496 ? 148.666 182.083 170.162 1.00 24.79  ? 496 PRO A CB  1 
ATOM   3419 C CG  . PRO A 1 496 ? 147.446 182.886 169.918 1.00 32.64  ? 496 PRO A CG  1 
ATOM   3420 C CD  . PRO A 1 496 ? 146.819 182.327 168.681 1.00 36.92  ? 496 PRO A CD  1 
ATOM   3421 N N   . ARG A 1 497 ? 149.008 179.268 168.388 1.00 34.34  ? 497 ARG A N   1 
ATOM   3422 C CA  . ARG A 1 497 ? 149.566 177.922 168.322 1.00 25.98  ? 497 ARG A CA  1 
ATOM   3423 C C   . ARG A 1 497 ? 150.701 177.845 167.309 1.00 21.45  ? 497 ARG A C   1 
ATOM   3424 O O   . ARG A 1 497 ? 151.691 177.138 167.528 1.00 23.54  ? 497 ARG A O   1 
ATOM   3425 C CB  . ARG A 1 497 ? 148.472 176.913 167.976 1.00 29.45  ? 497 ARG A CB  1 
ATOM   3426 C CG  . ARG A 1 497 ? 147.895 176.184 169.176 1.00 34.62  ? 497 ARG A CG  1 
ATOM   3427 C CD  . ARG A 1 497 ? 147.291 174.852 168.768 1.00 44.23  ? 497 ARG A CD  1 
ATOM   3428 N NE  . ARG A 1 497 ? 146.767 174.885 167.408 1.00 49.84  ? 497 ARG A NE  1 
ATOM   3429 C CZ  . ARG A 1 497 ? 146.653 173.822 166.623 1.00 45.31  ? 497 ARG A CZ  1 
ATOM   3430 N NH1 . ARG A 1 497 ? 147.017 172.618 167.033 1.00 36.28  ? 497 ARG A NH1 1 
ATOM   3431 N NH2 . ARG A 1 497 ? 146.163 173.972 165.396 1.00 43.18  ? 497 ARG A NH2 1 
ATOM   3432 N N   . ASP A 1 498 ? 150.552 178.595 166.215 1.00 19.62  ? 498 ASP A N   1 
ATOM   3433 C CA  . ASP A 1 498 ? 151.575 178.594 165.138 1.00 23.79  ? 498 ASP A CA  1 
ATOM   3434 C C   . ASP A 1 498 ? 152.582 179.711 165.403 1.00 22.91  ? 498 ASP A C   1 
ATOM   3435 O O   . ASP A 1 498 ? 152.781 180.551 164.508 1.00 22.84  ? 498 ASP A O   1 
ATOM   3436 C CB  . ASP A 1 498 ? 150.922 178.743 163.776 1.00 29.55  ? 498 ASP A CB  1 
ATOM   3437 C CG  . ASP A 1 498 ? 149.574 178.058 163.609 1.00 37.05  ? 498 ASP A CG  1 
ATOM   3438 O OD1 . ASP A 1 498 ? 149.502 176.836 163.848 1.00 35.24  ? 498 ASP A OD1 1 
ATOM   3439 O OD2 . ASP A 1 498 ? 148.613 178.750 163.221 1.00 36.94  ? 498 ASP A OD2 1 
ATOM   3440 N N   . CYS A 1 499 ? 153.195 179.714 166.585 1.00 26.09  ? 499 CYS A N   1 
ATOM   3441 C CA  . CYS A 1 499 ? 154.146 180.755 166.951 1.00 19.59  ? 499 CYS A CA  1 
ATOM   3442 C C   . CYS A 1 499 ? 155.500 180.127 167.239 1.00 31.51  ? 499 CYS A C   1 
ATOM   3443 O O   . CYS A 1 499 ? 155.593 179.176 168.021 1.00 35.65  ? 499 CYS A O   1 
ATOM   3444 C CB  . CYS A 1 499 ? 153.660 181.542 168.171 1.00 17.81  ? 499 CYS A CB  1 
ATOM   3445 S SG  . CYS A 1 499 ? 152.724 183.041 167.789 1.00 29.32  ? 499 CYS A SG  1 
ATOM   3446 N N   . VAL A 1 500 ? 156.545 180.651 166.592 1.00 30.35  ? 500 VAL A N   1 
ATOM   3447 C CA  . VAL A 1 500 ? 157.927 180.164 166.874 1.00 26.70  ? 500 VAL A CA  1 
ATOM   3448 C C   . VAL A 1 500 ? 158.226 180.480 168.345 1.00 34.33  ? 500 VAL A C   1 
ATOM   3449 O O   . VAL A 1 500 ? 158.633 179.551 169.076 1.00 41.87  ? 500 VAL A O   1 
ATOM   3450 C CB  . VAL A 1 500 ? 158.936 180.836 165.927 1.00 20.40  ? 500 VAL A CB  1 
ATOM   3451 C CG1 . VAL A 1 500 ? 160.361 180.374 166.195 1.00 25.99  ? 500 VAL A CG1 1 
ATOM   3452 C CG2 . VAL A 1 500 ? 158.563 180.623 164.466 1.00 18.13  ? 500 VAL A CG2 1 
ATOM   3453 N N   . SER A 1 501 ? 158.011 181.730 168.764 1.00 28.03  ? 501 SER A N   1 
ATOM   3454 C CA  . SER A 1 501 ? 158.198 182.125 170.151 1.00 26.76  ? 501 SER A CA  1 
ATOM   3455 C C   . SER A 1 501 ? 157.199 183.226 170.465 1.00 32.79  ? 501 SER A C   1 
ATOM   3456 O O   . SER A 1 501 ? 156.667 183.880 169.565 1.00 41.19  ? 501 SER A O   1 
ATOM   3457 C CB  . SER A 1 501 ? 159.631 182.592 170.425 1.00 38.66  ? 501 SER A CB  1 
ATOM   3458 O OG  . SER A 1 501 ? 159.938 182.512 171.806 1.00 44.16  ? 501 SER A OG  1 
ATOM   3459 N N   . CYS A 1 502 ? 156.949 183.429 171.754 1.00 32.24  ? 502 CYS A N   1 
ATOM   3460 C CA  . CYS A 1 502 ? 155.892 184.323 172.195 1.00 39.02  ? 502 CYS A CA  1 
ATOM   3461 C C   . CYS A 1 502 ? 156.424 185.315 173.220 1.00 39.90  ? 502 CYS A C   1 
ATOM   3462 O O   . CYS A 1 502 ? 157.516 185.152 173.770 1.00 43.25  ? 502 CYS A O   1 
ATOM   3463 C CB  . CYS A 1 502 ? 154.709 183.528 172.751 1.00 41.63  ? 502 CYS A CB  1 
ATOM   3464 S SG  . CYS A 1 502 ? 154.217 182.184 171.643 1.00 54.51  ? 502 CYS A SG  1 
ATOM   3465 N N   . ARG A 1 503 ? 155.625 186.359 173.458 1.00 37.97  ? 503 ARG A N   1 
ATOM   3466 C CA  . ARG A 1 503 ? 156.111 187.534 174.175 1.00 40.94  ? 503 ARG A CA  1 
ATOM   3467 C C   . ARG A 1 503 ? 156.516 187.201 175.605 1.00 50.45  ? 503 ARG A C   1 
ATOM   3468 O O   . ARG A 1 503 ? 157.635 187.511 176.031 1.00 51.07  ? 503 ARG A O   1 
ATOM   3469 C CB  . ARG A 1 503 ? 155.041 188.626 174.165 1.00 41.27  ? 503 ARG A CB  1 
ATOM   3470 C CG  . ARG A 1 503 ? 155.057 189.511 172.932 1.00 40.95  ? 503 ARG A CG  1 
ATOM   3471 C CD  . ARG A 1 503 ? 153.989 190.586 173.027 1.00 45.97  ? 503 ARG A CD  1 
ATOM   3472 N NE  . ARG A 1 503 ? 152.868 190.163 173.858 1.00 52.51  ? 503 ARG A NE  1 
ATOM   3473 C CZ  . ARG A 1 503 ? 151.784 190.892 174.084 1.00 50.58  ? 503 ARG A CZ  1 
ATOM   3474 N NH1 . ARG A 1 503 ? 151.637 192.094 173.553 1.00 48.20  ? 503 ARG A NH1 1 
ATOM   3475 N NH2 . ARG A 1 503 ? 150.824 190.402 174.863 1.00 48.71  ? 503 ARG A NH2 1 
ATOM   3476 N N   . ASN A 1 504 ? 155.640 186.522 176.350 1.00 46.13  ? 504 ASN A N   1 
ATOM   3477 C CA  . ASN A 1 504 ? 155.971 186.303 177.787 1.00 45.91  ? 504 ASN A CA  1 
ATOM   3478 C C   . ASN A 1 504 ? 156.002 184.828 178.180 1.00 38.90  ? 504 ASN A C   1 
ATOM   3479 O O   . ASN A 1 504 ? 156.999 184.417 178.810 1.00 51.01  ? 504 ASN A O   1 
ATOM   3480 C CB  . ASN A 1 504 ? 154.955 186.965 178.709 1.00 49.18  ? 504 ASN A CB  1 
ATOM   3481 C CG  . ASN A 1 504 ? 154.576 188.352 178.256 1.00 58.55  ? 504 ASN A CG  1 
ATOM   3482 O OD1 . ASN A 1 504 ? 153.930 188.510 177.214 1.00 52.49  ? 504 ASN A OD1 1 
ATOM   3483 N ND2 . ASN A 1 504 ? 154.958 189.361 179.028 1.00 68.58  ? 504 ASN A ND2 1 
ATOM   3484 N N   . VAL A 1 505 ? 154.969 184.062 177.837 1.00 27.70  ? 505 VAL A N   1 
ATOM   3485 C CA  . VAL A 1 505 ? 154.858 182.696 178.326 1.00 27.44  ? 505 VAL A CA  1 
ATOM   3486 C C   . VAL A 1 505 ? 154.365 181.806 177.191 1.00 29.05  ? 505 VAL A C   1 
ATOM   3487 O O   . VAL A 1 505 ? 154.208 182.246 176.050 1.00 31.36  ? 505 VAL A O   1 
ATOM   3488 C CB  . VAL A 1 505 ? 153.916 182.590 179.542 1.00 28.41  ? 505 VAL A CB  1 
ATOM   3489 C CG1 . VAL A 1 505 ? 154.421 183.457 180.685 1.00 35.43  ? 505 VAL A CG1 1 
ATOM   3490 C CG2 . VAL A 1 505 ? 152.509 182.991 179.146 1.00 37.17  ? 505 VAL A CG2 1 
ATOM   3491 N N   . SER A 1 506 ? 154.129 180.535 177.514 1.00 26.35  ? 506 SER A N   1 
ATOM   3492 C CA  . SER A 1 506 ? 153.601 179.573 176.549 1.00 21.41  ? 506 SER A CA  1 
ATOM   3493 C C   . SER A 1 506 ? 153.013 178.396 177.308 1.00 24.24  ? 506 SER A C   1 
ATOM   3494 O O   . SER A 1 506 ? 153.719 177.756 178.093 1.00 35.05  ? 506 SER A O   1 
ATOM   3495 C CB  . SER A 1 506 ? 154.694 179.101 175.588 1.00 23.98  ? 506 SER A CB  1 
ATOM   3496 O OG  . SER A 1 506 ? 155.201 180.174 174.813 1.00 36.76  ? 506 SER A OG  1 
ATOM   3497 N N   . ARG A 1 507 ? 151.730 178.110 177.080 1.00 23.25  ? 507 ARG A N   1 
ATOM   3498 C CA  . ARG A 1 507 ? 151.077 176.932 177.653 1.00 21.59  ? 507 ARG A CA  1 
ATOM   3499 C C   . ARG A 1 507 ? 151.133 175.816 176.614 1.00 27.22  ? 507 ARG A C   1 
ATOM   3500 O O   . ARG A 1 507 ? 150.189 175.578 175.860 1.00 36.45  ? 507 ARG A O   1 
ATOM   3501 C CB  . ARG A 1 507 ? 149.644 177.247 178.068 1.00 24.87  ? 507 ARG A CB  1 
ATOM   3502 C CG  . ARG A 1 507 ? 149.477 178.539 178.840 1.00 34.58  ? 507 ARG A CG  1 
ATOM   3503 C CD  . ARG A 1 507 ? 148.298 178.451 179.795 1.00 39.20  ? 507 ARG A CD  1 
ATOM   3504 N NE  . ARG A 1 507 ? 148.112 179.683 180.551 1.00 50.44  ? 507 ARG A NE  1 
ATOM   3505 C CZ  . ARG A 1 507 ? 146.937 180.259 180.767 1.00 54.82  ? 507 ARG A CZ  1 
ATOM   3506 N NH1 . ARG A 1 507 ? 145.815 179.735 180.302 1.00 58.06  ? 507 ARG A NH1 1 
ATOM   3507 N NH2 . ARG A 1 507 ? 146.887 181.390 181.465 1.00 51.01  ? 507 ARG A NH2 1 
ATOM   3508 N N   . GLY A 1 508 ? 152.262 175.119 176.585 1.00 28.49  ? 508 GLY A N   1 
ATOM   3509 C CA  . GLY A 1 508 ? 152.465 174.126 175.544 1.00 29.05  ? 508 GLY A CA  1 
ATOM   3510 C C   . GLY A 1 508 ? 152.745 174.816 174.225 1.00 32.94  ? 508 GLY A C   1 
ATOM   3511 O O   . GLY A 1 508 ? 153.546 175.754 174.151 1.00 40.05  ? 508 GLY A O   1 
ATOM   3512 N N   . ARG A 1 509 ? 152.088 174.350 173.162 1.00 32.13  ? 509 ARG A N   1 
ATOM   3513 C CA  . ARG A 1 509 ? 152.249 174.996 171.863 1.00 30.59  ? 509 ARG A CA  1 
ATOM   3514 C C   . ARG A 1 509 ? 151.580 176.366 171.848 1.00 33.26  ? 509 ARG A C   1 
ATOM   3515 O O   . ARG A 1 509 ? 152.175 177.354 171.404 1.00 34.01  ? 509 ARG A O   1 
ATOM   3516 C CB  . ARG A 1 509 ? 151.685 174.106 170.757 1.00 31.30  ? 509 ARG A CB  1 
ATOM   3517 C CG  . ARG A 1 509 ? 152.285 174.380 169.390 1.00 35.18  ? 509 ARG A CG  1 
ATOM   3518 C CD  . ARG A 1 509 ? 153.802 174.295 169.433 1.00 44.67  ? 509 ARG A CD  1 
ATOM   3519 N NE  . ARG A 1 509 ? 154.423 174.989 168.310 1.00 44.15  ? 509 ARG A NE  1 
ATOM   3520 C CZ  . ARG A 1 509 ? 154.675 176.290 168.280 1.00 35.69  ? 509 ARG A CZ  1 
ATOM   3521 N NH1 . ARG A 1 509 ? 154.373 177.076 169.300 1.00 29.77  ? 509 ARG A NH1 1 
ATOM   3522 N NH2 . ARG A 1 509 ? 155.246 176.815 167.201 1.00 26.60  ? 509 ARG A NH2 1 
ATOM   3523 N N   . GLU A 1 510 ? 150.342 176.442 172.329 1.00 36.85  ? 510 GLU A N   1 
ATOM   3524 C CA  . GLU A 1 510 ? 149.655 177.722 172.428 1.00 30.41  ? 510 GLU A CA  1 
ATOM   3525 C C   . GLU A 1 510 ? 150.276 178.566 173.531 1.00 24.73  ? 510 GLU A C   1 
ATOM   3526 O O   . GLU A 1 510 ? 150.651 178.055 174.588 1.00 30.26  ? 510 GLU A O   1 
ATOM   3527 C CB  . GLU A 1 510 ? 148.167 177.510 172.705 1.00 34.04  ? 510 GLU A CB  1 
ATOM   3528 C CG  . GLU A 1 510 ? 147.296 178.712 172.375 1.00 38.66  ? 510 GLU A CG  1 
ATOM   3529 C CD  . GLU A 1 510 ? 146.576 179.263 173.591 1.00 41.30  ? 510 GLU A CD  1 
ATOM   3530 O OE1 . GLU A 1 510 ? 146.784 178.726 174.699 1.00 44.93  ? 510 GLU A OE1 1 
ATOM   3531 O OE2 . GLU A 1 510 ? 145.804 180.232 173.439 1.00 35.65  ? 510 GLU A OE2 1 
ATOM   3532 N N   . CYS A 1 511 ? 150.387 179.868 173.283 1.00 22.72  ? 511 CYS A N   1 
ATOM   3533 C CA  . CYS A 1 511 ? 150.970 180.790 174.248 1.00 31.35  ? 511 CYS A CA  1 
ATOM   3534 C C   . CYS A 1 511 ? 149.972 181.888 174.580 1.00 34.16  ? 511 CYS A C   1 
ATOM   3535 O O   . CYS A 1 511 ? 149.596 182.679 173.709 1.00 36.19  ? 511 CYS A O   1 
ATOM   3536 C CB  . CYS A 1 511 ? 152.273 181.387 173.724 1.00 31.05  ? 511 CYS A CB  1 
ATOM   3537 S SG  . CYS A 1 511 ? 152.244 181.933 172.024 1.00 37.80  ? 511 CYS A SG  1 
ATOM   3538 N N   . VAL A 1 512 ? 149.638 181.981 175.867 1.00 32.08  ? 512 VAL A N   1 
ATOM   3539 C CA  . VAL A 1 512 ? 148.681 183.023 176.327 1.00 41.35  ? 512 VAL A CA  1 
ATOM   3540 C C   . VAL A 1 512 ? 149.434 184.339 176.562 1.00 38.93  ? 512 VAL A C   1 
ATOM   3541 O O   . VAL A 1 512 ? 150.664 184.372 176.334 1.00 33.85  ? 512 VAL A O   1 
ATOM   3542 C CB  . VAL A 1 512 ? 148.020 182.508 177.615 1.00 47.72  ? 512 VAL A CB  1 
ATOM   3543 C CG1 . VAL A 1 512 ? 147.155 181.283 177.346 1.00 37.10  ? 512 VAL A CG1 1 
ATOM   3544 C CG2 . VAL A 1 512 ? 149.061 182.201 178.682 1.00 46.22  ? 512 VAL A CG2 1 
ATOM   3545 N N   . ASP A 1 513 ? 148.715 185.382 176.987 1.00 41.20  ? 513 ASP A N   1 
ATOM   3546 C CA  . ASP A 1 513 ? 149.354 186.692 177.286 1.00 42.08  ? 513 ASP A CA  1 
ATOM   3547 C C   . ASP A 1 513 ? 150.273 186.530 178.495 1.00 43.58  ? 513 ASP A C   1 
ATOM   3548 O O   . ASP A 1 513 ? 151.373 187.121 178.487 1.00 45.33  ? 513 ASP A O   1 
ATOM   3549 C CB  . ASP A 1 513 ? 148.309 187.769 177.526 1.00 45.75  ? 513 ASP A CB  1 
ATOM   3550 C CG  . ASP A 1 513 ? 147.194 187.394 178.492 1.00 48.81  ? 513 ASP A CG  1 
ATOM   3551 O OD1 . ASP A 1 513 ? 147.195 186.241 178.974 1.00 41.02  ? 513 ASP A OD1 1 
ATOM   3552 O OD2 . ASP A 1 513 ? 146.334 188.259 178.757 1.00 53.64  ? 513 ASP A OD2 1 
ATOM   3553 N N   . LYS A 1 514 ? 149.834 185.755 179.490 1.00 47.38  ? 514 LYS A N   1 
ATOM   3554 C CA  . LYS A 1 514 ? 150.632 185.597 180.731 1.00 46.23  ? 514 LYS A CA  1 
ATOM   3555 C C   . LYS A 1 514 ? 150.171 184.355 181.504 1.00 42.95  ? 514 LYS A C   1 
ATOM   3556 O O   . LYS A 1 514 ? 148.988 183.977 181.374 1.00 41.89  ? 514 LYS A O   1 
ATOM   3557 C CB  . LYS A 1 514 ? 150.481 186.852 181.596 1.00 46.99  ? 514 LYS A CB  1 
ATOM   3558 C CG  . LYS A 1 514 ? 149.039 187.221 181.914 1.00 47.86  ? 514 LYS A CG  1 
ATOM   3559 C CD  . LYS A 1 514 ? 148.888 188.500 182.726 1.00 56.18  ? 514 LYS A CD  1 
ATOM   3560 C CE  . LYS A 1 514 ? 147.451 188.811 182.999 1.00 59.89  ? 514 LYS A CE  1 
ATOM   3561 N NZ  . LYS A 1 514 ? 146.788 187.710 183.702 1.00 64.63  ? 514 LYS A NZ  1 
ATOM   3562 N N   . CYS A 1 515 ? 151.075 183.753 182.279 1.00 48.04  ? 515 CYS A N   1 
ATOM   3563 C CA  . CYS A 1 515 ? 150.744 182.592 183.091 1.00 46.10  ? 515 CYS A CA  1 
ATOM   3564 C C   . CYS A 1 515 ? 149.742 182.971 184.176 1.00 45.97  ? 515 CYS A C   1 
ATOM   3565 O O   . CYS A 1 515 ? 149.581 184.140 184.535 1.00 48.18  ? 515 CYS A O   1 
ATOM   3566 C CB  . CYS A 1 515 ? 151.999 182.007 183.741 1.00 42.57  ? 515 CYS A CB  1 
ATOM   3567 S SG  . CYS A 1 515 ? 153.023 180.951 182.692 1.00 67.45  ? 515 CYS A SG  1 
ATOM   3568 N N   . ASN A 1 516 ? 149.063 181.955 184.707 1.00 44.55  ? 516 ASN A N   1 
ATOM   3569 C CA  . ASN A 1 516 ? 148.113 182.148 185.800 1.00 44.73  ? 516 ASN A CA  1 
ATOM   3570 C C   . ASN A 1 516 ? 148.860 182.309 187.127 1.00 44.48  ? 516 ASN A C   1 
ATOM   3571 O O   . ASN A 1 516 ? 148.711 181.531 188.069 1.00 46.34  ? 516 ASN A O   1 
ATOM   3572 C CB  . ASN A 1 516 ? 147.125 180.991 185.849 1.00 41.29  ? 516 ASN A CB  1 
ATOM   3573 C CG  . ASN A 1 516 ? 146.386 180.804 184.541 1.00 41.94  ? 516 ASN A CG  1 
ATOM   3574 O OD1 . ASN A 1 516 ? 146.299 181.723 183.728 1.00 45.48  ? 516 ASN A OD1 1 
ATOM   3575 N ND2 . ASN A 1 516 ? 145.850 179.609 184.330 1.00 43.14  ? 516 ASN A ND2 1 
ATOM   3576 N N   . LEU A 1 517 ? 149.698 183.343 187.195 1.00 36.33  ? 517 LEU A N   1 
ATOM   3577 C CA  . LEU A 1 517 ? 150.493 183.563 188.429 1.00 38.20  ? 517 LEU A CA  1 
ATOM   3578 C C   . LEU A 1 517 ? 149.551 183.957 189.580 1.00 51.10  ? 517 LEU A C   1 
ATOM   3579 O O   . LEU A 1 517 ? 149.778 183.477 190.711 1.00 61.45  ? 517 LEU A O   1 
ATOM   3580 C CB  . LEU A 1 517 ? 151.569 184.616 188.175 1.00 49.37  ? 517 LEU A CB  1 
ATOM   3581 C CG  . LEU A 1 517 ? 152.998 184.085 188.026 1.00 45.89  ? 517 LEU A CG  1 
ATOM   3582 C CD1 . LEU A 1 517 ? 153.057 182.921 187.054 1.00 37.78  ? 517 LEU A CD1 1 
ATOM   3583 C CD2 . LEU A 1 517 ? 153.940 185.191 187.589 1.00 46.40  ? 517 LEU A CD2 1 
ATOM   3584 N N   . LEU A 1 518 ? 148.537 184.786 189.304 1.00 54.01  ? 518 LEU A N   1 
ATOM   3585 C CA  . LEU A 1 518 ? 147.618 185.213 190.349 1.00 50.95  ? 518 LEU A CA  1 
ATOM   3586 C C   . LEU A 1 518 ? 146.193 184.717 190.158 1.00 49.89  ? 518 LEU A C   1 
ATOM   3587 O O   . LEU A 1 518 ? 145.510 184.463 191.153 1.00 53.06  ? 518 LEU A O   1 
ATOM   3588 C CB  . LEU A 1 518 ? 147.591 186.748 190.458 1.00 50.51  ? 518 LEU A CB  1 
ATOM   3589 C CG  . LEU A 1 518 ? 148.898 187.511 190.712 1.00 46.00  ? 518 LEU A CG  1 
ATOM   3590 C CD1 . LEU A 1 518 ? 149.731 186.823 191.787 1.00 51.66  ? 518 LEU A CD1 1 
ATOM   3591 C CD2 . LEU A 1 518 ? 149.708 187.735 189.437 1.00 44.40  ? 518 LEU A CD2 1 
ATOM   3592 N N   . GLU A 1 519 ? 145.724 184.577 188.920 1.00 47.85  ? 519 GLU A N   1 
ATOM   3593 C CA  . GLU A 1 519 ? 144.361 184.141 188.653 1.00 50.05  ? 519 GLU A CA  1 
ATOM   3594 C C   . GLU A 1 519 ? 144.351 183.172 187.481 1.00 49.38  ? 519 GLU A C   1 
ATOM   3595 O O   . GLU A 1 519 ? 145.011 183.407 186.465 1.00 51.43  ? 519 GLU A O   1 
ATOM   3596 C CB  . GLU A 1 519 ? 143.442 185.332 188.356 1.00 52.74  ? 519 GLU A CB  1 
ATOM   3597 C CG  . GLU A 1 519 ? 144.106 186.444 187.561 1.00 57.19  ? 519 GLU A CG  1 
ATOM   3598 C CD  . GLU A 1 519 ? 143.515 187.807 187.862 1.00 66.94  ? 519 GLU A CD  1 
ATOM   3599 O OE1 . GLU A 1 519 ? 142.342 188.041 187.503 1.00 78.33  ? 519 GLU A OE1 1 
ATOM   3600 O OE2 . GLU A 1 519 ? 144.223 188.646 188.458 1.00 64.37  ? 519 GLU A OE2 1 
ATOM   3601 N N   . GLY A 1 520 ? 143.598 182.093 187.626 1.00 48.78  ? 520 GLY A N   1 
ATOM   3602 C CA  . GLY A 1 520 ? 143.478 181.096 186.583 1.00 48.92  ? 520 GLY A CA  1 
ATOM   3603 C C   . GLY A 1 520 ? 142.915 179.804 187.122 1.00 52.93  ? 520 GLY A C   1 
ATOM   3604 O O   . GLY A 1 520 ? 142.929 179.534 188.324 1.00 54.15  ? 520 GLY A O   1 
ATOM   3605 N N   . GLU A 1 521 ? 142.402 178.987 186.204 1.00 54.89  ? 521 GLU A N   1 
ATOM   3606 C CA  . GLU A 1 521 ? 141.814 177.707 186.583 1.00 61.87  ? 521 GLU A CA  1 
ATOM   3607 C C   . GLU A 1 521 ? 142.893 176.663 186.873 1.00 65.32  ? 521 GLU A C   1 
ATOM   3608 O O   . GLU A 1 521 ? 142.871 176.060 187.954 1.00 64.83  ? 521 GLU A O   1 
ATOM   3609 C CB  . GLU A 1 521 ? 140.843 177.214 185.503 1.00 64.49  ? 521 GLU A CB  1 
ATOM   3610 C CG  . GLU A 1 521 ? 140.097 175.941 185.870 1.00 72.62  ? 521 GLU A CG  1 
ATOM   3611 C CD  . GLU A 1 521 ? 139.610 175.941 187.306 1.00 79.22  ? 521 GLU A CD  1 
ATOM   3612 O OE1 . GLU A 1 521 ? 138.703 176.737 187.627 1.00 72.81  ? 521 GLU A OE1 1 
ATOM   3613 O OE2 . GLU A 1 521 ? 140.133 175.144 188.113 1.00 79.07  ? 521 GLU A OE2 1 
ATOM   3614 N N   . PRO A 1 522 ? 143.850 176.406 185.969 1.00 63.90  ? 522 PRO A N   1 
ATOM   3615 C CA  . PRO A 1 522 ? 144.904 175.435 186.295 1.00 57.17  ? 522 PRO A CA  1 
ATOM   3616 C C   . PRO A 1 522 ? 146.070 176.028 187.068 1.00 54.35  ? 522 PRO A C   1 
ATOM   3617 O O   . PRO A 1 522 ? 146.878 175.261 187.612 1.00 53.69  ? 522 PRO A O   1 
ATOM   3618 C CB  . PRO A 1 522 ? 145.358 174.927 184.914 1.00 53.19  ? 522 PRO A CB  1 
ATOM   3619 C CG  . PRO A 1 522 ? 144.554 175.706 183.889 1.00 57.80  ? 522 PRO A CG  1 
ATOM   3620 C CD  . PRO A 1 522 ? 144.017 176.902 184.593 1.00 57.17  ? 522 PRO A CD  1 
ATOM   3621 N N   . ARG A 1 523 ? 146.115 177.359 187.188 1.00 50.32  ? 523 ARG A N   1 
ATOM   3622 C CA  . ARG A 1 523 ? 147.139 178.065 188.004 1.00 43.07  ? 523 ARG A CA  1 
ATOM   3623 C C   . ARG A 1 523 ? 148.555 177.665 187.582 1.00 42.47  ? 523 ARG A C   1 
ATOM   3624 O O   . ARG A 1 523 ? 149.248 177.002 188.381 1.00 46.52  ? 523 ARG A O   1 
ATOM   3625 C CB  . ARG A 1 523 ? 146.870 177.822 189.493 1.00 50.05  ? 523 ARG A CB  1 
ATOM   3626 C CG  . ARG A 1 523 ? 145.645 178.558 190.011 1.00 55.03  ? 523 ARG A CG  1 
ATOM   3627 C CD  . ARG A 1 523 ? 145.773 180.054 189.783 1.00 52.42  ? 523 ARG A CD  1 
ATOM   3628 N NE  . ARG A 1 523 ? 144.965 180.817 190.739 1.00 51.24  ? 523 ARG A NE  1 
ATOM   3629 C CZ  . ARG A 1 523 ? 145.439 181.599 191.700 1.00 51.82  ? 523 ARG A CZ  1 
ATOM   3630 N NH1 . ARG A 1 523 ? 146.735 181.834 191.805 1.00 53.16  ? 523 ARG A NH1 1 
ATOM   3631 N NH2 . ARG A 1 523 ? 144.609 182.134 192.575 1.00 57.53  ? 523 ARG A NH2 1 
ATOM   3632 N N   . GLU A 1 524 ? 148.974 178.058 186.382 1.00 44.02  ? 524 GLU A N   1 
ATOM   3633 C CA  . GLU A 1 524 ? 150.335 177.846 185.913 1.00 36.72  ? 524 GLU A CA  1 
ATOM   3634 C C   . GLU A 1 524 ? 151.335 178.621 186.768 1.00 31.53  ? 524 GLU A C   1 
ATOM   3635 O O   . GLU A 1 524 ? 151.002 179.607 187.430 1.00 36.91  ? 524 GLU A O   1 
ATOM   3636 C CB  . GLU A 1 524 ? 150.485 178.285 184.456 1.00 36.75  ? 524 GLU A CB  1 
ATOM   3637 C CG  . GLU A 1 524 ? 149.234 178.174 183.607 1.00 37.18  ? 524 GLU A CG  1 
ATOM   3638 C CD  . GLU A 1 524 ? 148.894 176.744 183.257 1.00 44.83  ? 524 GLU A CD  1 
ATOM   3639 O OE1 . GLU A 1 524 ? 149.762 176.045 182.694 1.00 46.29  ? 524 GLU A OE1 1 
ATOM   3640 O OE2 . GLU A 1 524 ? 147.756 176.319 183.533 1.00 49.53  ? 524 GLU A OE2 1 
ATOM   3641 N N   . PHE A 1 525 ? 152.581 178.153 186.749 1.00 27.86  ? 525 PHE A N   1 
ATOM   3642 C CA  . PHE A 1 525 ? 153.713 178.901 187.274 1.00 28.88  ? 525 PHE A CA  1 
ATOM   3643 C C   . PHE A 1 525 ? 154.744 179.037 186.164 1.00 24.69  ? 525 PHE A C   1 
ATOM   3644 O O   . PHE A 1 525 ? 154.977 178.092 185.404 1.00 26.46  ? 525 PHE A O   1 
ATOM   3645 C CB  . PHE A 1 525 ? 154.322 178.229 188.525 1.00 31.73  ? 525 PHE A CB  1 
ATOM   3646 C CG  . PHE A 1 525 ? 155.186 177.030 188.228 1.00 32.58  ? 525 PHE A CG  1 
ATOM   3647 C CD1 . PHE A 1 525 ? 156.541 177.175 187.970 1.00 34.51  ? 525 PHE A CD1 1 
ATOM   3648 C CD2 . PHE A 1 525 ? 154.645 175.757 188.226 1.00 33.90  ? 525 PHE A CD2 1 
ATOM   3649 C CE1 . PHE A 1 525 ? 157.331 176.077 187.699 1.00 30.20  ? 525 PHE A CE1 1 
ATOM   3650 C CE2 . PHE A 1 525 ? 155.432 174.655 187.958 1.00 29.01  ? 525 PHE A CE2 1 
ATOM   3651 C CZ  . PHE A 1 525 ? 156.776 174.816 187.693 1.00 27.51  ? 525 PHE A CZ  1 
ATOM   3652 N N   . VAL A 1 526 ? 155.344 180.212 186.062 1.00 27.56  ? 526 VAL A N   1 
ATOM   3653 C CA  . VAL A 1 526 ? 156.241 180.525 184.956 1.00 30.98  ? 526 VAL A CA  1 
ATOM   3654 C C   . VAL A 1 526 ? 157.650 180.054 185.285 1.00 39.84  ? 526 VAL A C   1 
ATOM   3655 O O   . VAL A 1 526 ? 158.112 180.154 186.429 1.00 44.59  ? 526 VAL A O   1 
ATOM   3656 C CB  . VAL A 1 526 ? 156.203 182.032 184.629 1.00 32.53  ? 526 VAL A CB  1 
ATOM   3657 C CG1 . VAL A 1 526 ? 156.919 182.849 185.697 1.00 35.48  ? 526 VAL A CG1 1 
ATOM   3658 C CG2 . VAL A 1 526 ? 156.810 182.292 183.259 1.00 31.82  ? 526 VAL A CG2 1 
ATOM   3659 N N   . GLU A 1 527 ? 158.324 179.501 184.277 1.00 44.93  ? 527 GLU A N   1 
ATOM   3660 C CA  . GLU A 1 527 ? 159.726 179.119 184.388 1.00 43.35  ? 527 GLU A CA  1 
ATOM   3661 C C   . GLU A 1 527 ? 160.288 178.967 182.983 1.00 45.36  ? 527 GLU A C   1 
ATOM   3662 O O   . GLU A 1 527 ? 159.689 178.284 182.146 1.00 46.85  ? 527 GLU A O   1 
ATOM   3663 C CB  . GLU A 1 527 ? 159.898 177.824 185.198 1.00 44.54  ? 527 GLU A CB  1 
ATOM   3664 C CG  . GLU A 1 527 ? 159.184 176.605 184.634 1.00 42.05  ? 527 GLU A CG  1 
ATOM   3665 C CD  . GLU A 1 527 ? 160.102 175.727 183.804 1.00 50.01  ? 527 GLU A CD  1 
ATOM   3666 O OE1 . GLU A 1 527 ? 161.334 175.914 183.881 1.00 57.18  ? 527 GLU A OE1 1 
ATOM   3667 O OE2 . GLU A 1 527 ? 159.592 174.851 183.075 1.00 45.60  ? 527 GLU A OE2 1 
ATOM   3668 N N   . ASN A 1 528 ? 161.422 179.621 182.726 1.00 49.78  ? 528 ASN A N   1 
ATOM   3669 C CA  . ASN A 1 528 ? 162.054 179.618 181.406 1.00 61.36  ? 528 ASN A CA  1 
ATOM   3670 C C   . ASN A 1 528 ? 161.073 180.065 180.323 1.00 58.88  ? 528 ASN A C   1 
ATOM   3671 O O   . ASN A 1 528 ? 161.049 179.525 179.215 1.00 56.37  ? 528 ASN A O   1 
ATOM   3672 C CB  . ASN A 1 528 ? 162.640 178.244 181.078 1.00 62.86  ? 528 ASN A CB  1 
ATOM   3673 C CG  . ASN A 1 528 ? 163.876 178.332 180.204 1.00 69.39  ? 528 ASN A CG  1 
ATOM   3674 O OD1 . ASN A 1 528 ? 163.890 177.837 179.077 1.00 65.35  ? 528 ASN A OD1 1 
ATOM   3675 N ND2 . ASN A 1 528 ? 164.922 178.967 180.721 1.00 71.47  ? 528 ASN A ND2 1 
ATOM   3676 N N   . SER A 1 529 ? 160.256 181.068 180.656 1.00 53.04  ? 529 SER A N   1 
ATOM   3677 C CA  . SER A 1 529 ? 159.255 181.624 179.742 1.00 44.46  ? 529 SER A CA  1 
ATOM   3678 C C   . SER A 1 529 ? 158.300 180.541 179.239 1.00 42.63  ? 529 SER A C   1 
ATOM   3679 O O   . SER A 1 529 ? 158.121 180.346 178.035 1.00 43.52  ? 529 SER A O   1 
ATOM   3680 C CB  . SER A 1 529 ? 159.924 182.357 178.576 1.00 46.73  ? 529 SER A CB  1 
ATOM   3681 O OG  . SER A 1 529 ? 159.162 182.232 177.387 1.00 47.64  ? 529 SER A OG  1 
ATOM   3682 N N   . GLU A 1 530 ? 157.684 179.829 180.180 1.00 36.54  ? 530 GLU A N   1 
ATOM   3683 C CA  . GLU A 1 530 ? 156.740 178.774 179.844 1.00 31.95  ? 530 GLU A CA  1 
ATOM   3684 C C   . GLU A 1 530 ? 155.778 178.575 181.005 1.00 30.54  ? 530 GLU A C   1 
ATOM   3685 O O   . GLU A 1 530 ? 156.174 178.667 182.169 1.00 39.63  ? 530 GLU A O   1 
ATOM   3686 C CB  . GLU A 1 530 ? 157.461 177.460 179.520 1.00 31.62  ? 530 GLU A CB  1 
ATOM   3687 C CG  . GLU A 1 530 ? 156.642 176.492 178.683 1.00 39.20  ? 530 GLU A CG  1 
ATOM   3688 C CD  . GLU A 1 530 ? 156.849 175.047 179.092 1.00 49.49  ? 530 GLU A CD  1 
ATOM   3689 O OE1 . GLU A 1 530 ? 157.962 174.711 179.548 1.00 51.58  ? 530 GLU A OE1 1 
ATOM   3690 O OE2 . GLU A 1 530 ? 155.897 174.249 178.962 1.00 46.36  ? 530 GLU A OE2 1 
ATOM   3691 N N   . CYS A 1 531 ? 154.518 178.301 180.679 1.00 27.42  ? 531 CYS A N   1 
ATOM   3692 C CA  . CYS A 1 531 ? 153.488 178.057 181.682 1.00 23.71  ? 531 CYS A CA  1 
ATOM   3693 C C   . CYS A 1 531 ? 153.472 176.576 182.033 1.00 30.48  ? 531 CYS A C   1 
ATOM   3694 O O   . CYS A 1 531 ? 153.219 175.731 181.167 1.00 31.13  ? 531 CYS A O   1 
ATOM   3695 C CB  . CYS A 1 531 ? 152.114 178.490 181.173 1.00 31.11  ? 531 CYS A CB  1 
ATOM   3696 S SG  . CYS A 1 531 ? 151.751 180.254 181.276 1.00 42.05  ? 531 CYS A SG  1 
ATOM   3697 N N   . ILE A 1 532 ? 153.735 176.263 183.297 1.00 31.38  ? 532 ILE A N   1 
ATOM   3698 C CA  . ILE A 1 532 ? 153.694 174.895 183.797 1.00 30.31  ? 532 ILE A CA  1 
ATOM   3699 C C   . ILE A 1 532 ? 152.586 174.809 184.834 1.00 31.56  ? 532 ILE A C   1 
ATOM   3700 O O   . ILE A 1 532 ? 152.626 175.509 185.853 1.00 36.70  ? 532 ILE A O   1 
ATOM   3701 C CB  . ILE A 1 532 ? 155.039 174.461 184.398 1.00 26.80  ? 532 ILE A CB  1 
ATOM   3702 C CG1 . ILE A 1 532 ? 156.193 174.930 183.512 1.00 32.38  ? 532 ILE A CG1 1 
ATOM   3703 C CG2 . ILE A 1 532 ? 155.072 172.952 184.595 1.00 32.74  ? 532 ILE A CG2 1 
ATOM   3704 C CD1 . ILE A 1 532 ? 156.497 173.997 182.364 1.00 37.10  ? 532 ILE A CD1 1 
ATOM   3705 N N   . GLN A 1 533 ? 151.601 173.955 184.577 1.00 35.88  ? 533 GLN A N   1 
ATOM   3706 C CA  . GLN A 1 533 ? 150.558 173.705 185.560 1.00 41.56  ? 533 GLN A CA  1 
ATOM   3707 C C   . GLN A 1 533 ? 151.153 172.916 186.719 1.00 46.10  ? 533 GLN A C   1 
ATOM   3708 O O   . GLN A 1 533 ? 151.558 171.761 186.549 1.00 54.40  ? 533 GLN A O   1 
ATOM   3709 C CB  . GLN A 1 533 ? 149.397 172.946 184.924 1.00 43.03  ? 533 GLN A CB  1 
ATOM   3710 C CG  . GLN A 1 533 ? 148.462 172.286 185.924 1.00 48.25  ? 533 GLN A CG  1 
ATOM   3711 C CD  . GLN A 1 533 ? 147.857 171.002 185.394 1.00 51.09  ? 533 GLN A CD  1 
ATOM   3712 O OE1 . GLN A 1 533 ? 147.415 170.938 184.248 1.00 50.72  ? 533 GLN A OE1 1 
ATOM   3713 N NE2 . GLN A 1 533 ? 147.838 169.969 186.228 1.00 55.07  ? 533 GLN A NE2 1 
ATOM   3714 N N   . CYS A 1 534 ? 151.215 173.546 187.893 1.00 40.35  ? 534 CYS A N   1 
ATOM   3715 C CA  . CYS A 1 534 ? 151.878 172.889 189.049 1.00 49.36  ? 534 CYS A CA  1 
ATOM   3716 C C   . CYS A 1 534 ? 151.014 171.756 189.617 1.00 61.79  ? 534 CYS A C   1 
ATOM   3717 O O   . CYS A 1 534 ? 149.891 171.549 189.111 1.00 69.93  ? 534 CYS A O   1 
ATOM   3718 C CB  . CYS A 1 534 ? 152.186 173.899 190.144 1.00 54.83  ? 534 CYS A CB  1 
ATOM   3719 S SG  . CYS A 1 534 ? 150.855 175.087 190.452 1.00 51.71  ? 534 CYS A SG  1 
ATOM   3720 N N   . HIS A 1 535 ? 151.519 171.069 190.644 1.00 66.23  ? 535 HIS A N   1 
ATOM   3721 C CA  . HIS A 1 535 ? 150.790 169.913 191.226 1.00 72.58  ? 535 HIS A CA  1 
ATOM   3722 C C   . HIS A 1 535 ? 149.354 170.327 191.553 1.00 79.69  ? 535 HIS A C   1 
ATOM   3723 O O   . HIS A 1 535 ? 149.136 171.388 192.176 1.00 79.67  ? 535 HIS A O   1 
ATOM   3724 C CB  . HIS A 1 535 ? 151.546 169.403 192.456 1.00 69.80  ? 535 HIS A CB  1 
ATOM   3725 C CG  . HIS A 1 535 ? 151.902 167.958 192.390 1.00 72.39  ? 535 HIS A CG  1 
ATOM   3726 N ND1 . HIS A 1 535 ? 151.071 166.966 192.863 1.00 81.59  ? 535 HIS A ND1 1 
ATOM   3727 C CD2 . HIS A 1 535 ? 152.986 167.338 191.913 1.00 78.72  ? 535 HIS A CD2 1 
ATOM   3728 C CE1 . HIS A 1 535 ? 151.644 165.788 192.671 1.00 90.07  ? 535 HIS A CE1 1 
ATOM   3729 N NE2 . HIS A 1 535 ? 152.809 165.991 192.095 1.00 88.60  ? 535 HIS A NE2 1 
ATOM   3730 N N   . PRO A 1 536 ? 148.348 169.515 191.169 1.00 78.44  ? 536 PRO A N   1 
ATOM   3731 C CA  . PRO A 1 536 ? 146.964 169.822 191.499 1.00 77.62  ? 536 PRO A CA  1 
ATOM   3732 C C   . PRO A 1 536 ? 146.770 170.005 192.997 1.00 83.51  ? 536 PRO A C   1 
ATOM   3733 O O   . PRO A 1 536 ? 145.866 170.763 193.399 1.00 87.64  ? 536 PRO A O   1 
ATOM   3734 C CB  . PRO A 1 536 ? 146.228 168.584 190.974 1.00 78.04  ? 536 PRO A CB  1 
ATOM   3735 C CG  . PRO A 1 536 ? 147.111 168.082 189.857 1.00 73.27  ? 536 PRO A CG  1 
ATOM   3736 C CD  . PRO A 1 536 ? 148.513 168.301 190.390 1.00 74.32  ? 536 PRO A CD  1 
ATOM   3737 N N   . GLU A 1 537 ? 147.596 169.332 193.803 1.00 83.27  ? 537 GLU A N   1 
ATOM   3738 C CA  . GLU A 1 537 ? 147.456 169.403 195.281 1.00 83.63  ? 537 GLU A CA  1 
ATOM   3739 C C   . GLU A 1 537 ? 147.552 170.864 195.734 1.00 86.06  ? 537 GLU A C   1 
ATOM   3740 O O   . GLU A 1 537 ? 146.829 171.240 196.678 1.00 91.84  ? 537 GLU A O   1 
ATOM   3741 C CB  . GLU A 1 537 ? 148.559 168.597 195.962 1.00 84.17  ? 537 GLU A CB  1 
ATOM   3742 C CG  . GLU A 1 537 ? 148.744 167.200 195.379 1.00 91.92  ? 537 GLU A CG  1 
ATOM   3743 C CD  . GLU A 1 537 ? 147.693 166.176 195.762 1.00 98.91  ? 537 GLU A CD  1 
ATOM   3744 O OE1 . GLU A 1 537 ? 146.748 166.518 196.503 1.00 104.39 ? 537 GLU A OE1 1 
ATOM   3745 O OE2 . GLU A 1 537 ? 147.836 165.019 195.317 1.00 94.69  ? 537 GLU A OE2 1 
ATOM   3746 N N   . CYS A 1 538 ? 148.412 171.648 195.086 1.00 82.15  ? 538 CYS A N   1 
ATOM   3747 C CA  . CYS A 1 538 ? 148.622 173.065 195.483 1.00 82.70  ? 538 CYS A CA  1 
ATOM   3748 C C   . CYS A 1 538 ? 147.359 173.888 195.173 1.00 85.15  ? 538 CYS A C   1 
ATOM   3749 O O   . CYS A 1 538 ? 147.042 174.043 193.974 1.00 88.49  ? 538 CYS A O   1 
ATOM   3750 C CB  . CYS A 1 538 ? 149.841 173.616 194.758 1.00 80.10  ? 538 CYS A CB  1 
ATOM   3751 S SG  . CYS A 1 538 ? 151.231 172.451 194.725 1.00 91.51  ? 538 CYS A SG  1 
ATOM   3752 N N   . LEU A 1 539 ? 146.665 174.374 196.209 1.00 83.24  ? 539 LEU A N   1 
ATOM   3753 C CA  . LEU A 1 539 ? 145.430 175.182 196.031 1.00 80.26  ? 539 LEU A CA  1 
ATOM   3754 C C   . LEU A 1 539 ? 145.793 176.523 195.378 1.00 80.40  ? 539 LEU A C   1 
ATOM   3755 O O   . LEU A 1 539 ? 146.951 176.959 195.533 1.00 85.26  ? 539 LEU A O   1 
ATOM   3756 C CB  . LEU A 1 539 ? 144.726 175.393 197.371 1.00 83.65  ? 539 LEU A CB  1 
ATOM   3757 C CG  . LEU A 1 539 ? 145.542 176.048 198.489 1.00 87.24  ? 539 LEU A CG  1 
ATOM   3758 C CD1 . LEU A 1 539 ? 145.494 177.561 198.418 1.00 84.93  ? 539 LEU A CD1 1 
ATOM   3759 C CD2 . LEU A 1 539 ? 145.043 175.556 199.832 1.00 89.73  ? 539 LEU A CD2 1 
ATOM   3760 N N   . PRO A 1 540 ? 144.865 177.197 194.664 1.00 76.16  ? 540 PRO A N   1 
ATOM   3761 C CA  . PRO A 1 540 ? 145.147 178.507 194.092 1.00 73.97  ? 540 PRO A CA  1 
ATOM   3762 C C   . PRO A 1 540 ? 145.409 179.552 195.166 1.00 73.07  ? 540 PRO A C   1 
ATOM   3763 O O   . PRO A 1 540 ? 144.713 179.511 196.200 1.00 73.07  ? 540 PRO A O   1 
ATOM   3764 C CB  . PRO A 1 540 ? 143.876 178.818 193.285 1.00 69.20  ? 540 PRO A CB  1 
ATOM   3765 C CG  . PRO A 1 540 ? 143.232 177.472 193.071 1.00 70.38  ? 540 PRO A CG  1 
ATOM   3766 C CD  . PRO A 1 540 ? 143.531 176.724 194.352 1.00 74.09  ? 540 PRO A CD  1 
ATOM   3767 N N   . GLN A 1 541 ? 146.355 180.468 194.932 1.00 71.24  ? 541 GLN A N   1 
ATOM   3768 C CA  . GLN A 1 541 ? 146.707 181.539 195.900 1.00 77.03  ? 541 GLN A CA  1 
ATOM   3769 C C   . GLN A 1 541 ? 146.579 182.892 195.190 1.00 79.60  ? 541 GLN A C   1 
ATOM   3770 O O   . GLN A 1 541 ? 147.286 183.084 194.180 1.00 78.23  ? 541 GLN A O   1 
ATOM   3771 C CB  . GLN A 1 541 ? 148.126 181.344 196.428 1.00 73.19  ? 541 GLN A CB  1 
ATOM   3772 C CG  . GLN A 1 541 ? 148.489 182.280 197.575 1.00 81.10  ? 541 GLN A CG  1 
ATOM   3773 C CD  . GLN A 1 541 ? 149.914 182.118 198.058 1.00 91.97  ? 541 GLN A CD  1 
ATOM   3774 O OE1 . GLN A 1 541 ? 150.357 182.797 198.991 1.00 94.73  ? 541 GLN A OE1 1 
ATOM   3775 N NE2 . GLN A 1 541 ? 150.653 181.218 197.426 1.00 93.62  ? 541 GLN A NE2 1 
ATOM   3776 N N   . ALA A 1 542 ? 145.735 183.796 195.694 1.00 75.09  ? 542 ALA A N   1 
ATOM   3777 C CA  . ALA A 1 542 ? 145.486 185.108 195.049 1.00 71.13  ? 542 ALA A CA  1 
ATOM   3778 C C   . ALA A 1 542 ? 146.512 186.138 195.520 1.00 79.45  ? 542 ALA A C   1 
ATOM   3779 O O   . ALA A 1 542 ? 146.886 187.010 194.706 1.00 76.34  ? 542 ALA A O   1 
ATOM   3780 C CB  . ALA A 1 542 ? 144.078 185.561 195.353 1.00 66.78  ? 542 ALA A CB  1 
ATOM   3781 N N   . MET A 1 543 ? 146.959 186.050 196.775 1.00 85.51  ? 543 MET A N   1 
ATOM   3782 C CA  . MET A 1 543 ? 147.899 187.052 197.346 1.00 84.86  ? 543 MET A CA  1 
ATOM   3783 C C   . MET A 1 543 ? 149.260 186.938 196.644 1.00 85.62  ? 543 MET A C   1 
ATOM   3784 O O   . MET A 1 543 ? 149.818 187.999 196.288 1.00 86.32  ? 543 MET A O   1 
ATOM   3785 C CB  . MET A 1 543 ? 148.075 186.845 198.854 1.00 79.02  ? 543 MET A CB  1 
ATOM   3786 C CG  . MET A 1 543 ? 148.225 188.139 199.627 1.00 80.69  ? 543 MET A CG  1 
ATOM   3787 S SD  . MET A 1 543 ? 149.856 188.885 199.446 1.00 91.34  ? 543 MET A SD  1 
ATOM   3788 C CE  . MET A 1 543 ? 150.711 188.000 200.756 1.00 87.22  ? 543 MET A CE  1 
ATOM   3789 N N   . ASN A 1 544 ? 149.768 185.717 196.454 1.00 81.77  ? 544 ASN A N   1 
ATOM   3790 C CA  . ASN A 1 544 ? 151.084 185.480 195.797 1.00 76.38  ? 544 ASN A CA  1 
ATOM   3791 C C   . ASN A 1 544 ? 150.889 184.460 194.672 1.00 75.01  ? 544 ASN A C   1 
ATOM   3792 O O   . ASN A 1 544 ? 149.759 184.393 194.144 1.00 76.02  ? 544 ASN A O   1 
ATOM   3793 C CB  . ASN A 1 544 ? 152.131 185.043 196.816 1.00 77.40  ? 544 ASN A CB  1 
ATOM   3794 C CG  . ASN A 1 544 ? 152.137 185.921 198.043 1.00 85.50  ? 544 ASN A CG  1 
ATOM   3795 O OD1 . ASN A 1 544 ? 151.927 185.430 199.157 1.00 87.82  ? 544 ASN A OD1 1 
ATOM   3796 N ND2 . ASN A 1 544 ? 152.380 187.211 197.864 1.00 84.45  ? 544 ASN A ND2 1 
ATOM   3797 N N   . ILE A 1 545 ? 151.933 183.704 194.315 1.00 70.82  ? 545 ILE A N   1 
ATOM   3798 C CA  . ILE A 1 545 ? 151.839 182.650 193.262 1.00 68.89  ? 545 ILE A CA  1 
ATOM   3799 C C   . ILE A 1 545 ? 151.612 181.301 193.958 1.00 68.94  ? 545 ILE A C   1 
ATOM   3800 O O   . ILE A 1 545 ? 152.519 180.874 194.705 1.00 78.69  ? 545 ILE A O   1 
ATOM   3801 C CB  . ILE A 1 545 ? 153.087 182.647 192.360 1.00 63.29  ? 545 ILE A CB  1 
ATOM   3802 C CG1 . ILE A 1 545 ? 153.334 184.018 191.733 1.00 58.68  ? 545 ILE A CG1 1 
ATOM   3803 C CG2 . ILE A 1 545 ? 152.978 181.558 191.293 1.00 62.80  ? 545 ILE A CG2 1 
ATOM   3804 C CD1 . ILE A 1 545 ? 154.714 184.181 191.125 1.00 64.49  ? 545 ILE A CD1 1 
ATOM   3805 N N   . THR A 1 546 ? 150.448 180.680 193.757 1.00 62.33  ? 546 THR A N   1 
ATOM   3806 C CA  . THR A 1 546 ? 150.080 179.374 194.356 1.00 64.04  ? 546 THR A CA  1 
ATOM   3807 C C   . THR A 1 546 ? 151.258 178.437 194.483 1.00 62.92  ? 546 THR A C   1 
ATOM   3808 O O   . THR A 1 546 ? 151.356 177.799 195.554 1.00 67.18  ? 546 THR A O   1 
ATOM   3809 C CB  . THR A 1 546 ? 149.005 178.721 193.489 1.00 66.69  ? 546 THR A CB  1 
ATOM   3810 O OG1 . THR A 1 546 ? 149.041 177.332 193.800 1.00 69.14  ? 546 THR A OG1 1 
ATOM   3811 C CG2 . THR A 1 546 ? 149.256 178.888 192.002 1.00 61.74  ? 546 THR A CG2 1 
ATOM   3812 N N   . CYS A 1 547 ? 152.129 178.332 193.473 1.00 56.72  ? 547 CYS A N   1 
ATOM   3813 C CA  . CYS A 1 547 ? 153.193 177.292 193.468 1.00 52.57  ? 547 CYS A CA  1 
ATOM   3814 C C   . CYS A 1 547 ? 154.542 177.891 193.041 1.00 55.24  ? 547 CYS A C   1 
ATOM   3815 O O   . CYS A 1 547 ? 154.574 178.570 191.995 1.00 55.53  ? 547 CYS A O   1 
ATOM   3816 C CB  . CYS A 1 547 ? 152.799 176.166 192.521 1.00 55.19  ? 547 CYS A CB  1 
ATOM   3817 S SG  . CYS A 1 547 ? 151.868 176.734 191.071 1.00 75.70  ? 547 CYS A SG  1 
ATOM   3818 N N   . THR A 1 548 ? 155.610 177.639 193.811 1.00 55.84  ? 548 THR A N   1 
ATOM   3819 C CA  . THR A 1 548 ? 156.933 178.124 193.432 1.00 48.76  ? 548 THR A CA  1 
ATOM   3820 C C   . THR A 1 548 ? 157.486 177.354 192.239 1.00 45.86  ? 548 THR A C   1 
ATOM   3821 O O   . THR A 1 548 ? 158.108 177.943 191.348 1.00 46.45  ? 548 THR A O   1 
ATOM   3822 C CB  . THR A 1 548 ? 157.888 178.027 194.621 1.00 50.96  ? 548 THR A CB  1 
ATOM   3823 O OG1 . THR A 1 548 ? 157.259 178.573 195.788 1.00 51.02  ? 548 THR A OG1 1 
ATOM   3824 C CG2 . THR A 1 548 ? 159.171 178.793 194.338 1.00 52.79  ? 548 THR A CG2 1 
ATOM   3825 N N   . GLY A 1 549 ? 157.270 176.045 192.202 1.00 41.65  ? 549 GLY A N   1 
ATOM   3826 C CA  . GLY A 1 549 ? 157.793 175.236 191.127 1.00 38.37  ? 549 GLY A CA  1 
ATOM   3827 C C   . GLY A 1 549 ? 157.042 173.930 190.997 1.00 45.20  ? 549 GLY A C   1 
ATOM   3828 O O   . GLY A 1 549 ? 155.988 173.732 191.605 1.00 51.31  ? 549 GLY A O   1 
ATOM   3829 N N   . ARG A 1 550 ? 157.603 173.038 190.186 1.00 48.62  ? 550 ARG A N   1 
ATOM   3830 C CA  . ARG A 1 550 ? 156.997 171.736 189.960 1.00 45.11  ? 550 ARG A CA  1 
ATOM   3831 C C   . ARG A 1 550 ? 157.132 170.855 191.199 1.00 53.39  ? 550 ARG A C   1 
ATOM   3832 O O   . ARG A 1 550 ? 157.945 171.106 192.092 1.00 63.06  ? 550 ARG A O   1 
ATOM   3833 C CB  . ARG A 1 550 ? 157.645 171.043 188.761 1.00 43.79  ? 550 ARG A CB  1 
ATOM   3834 C CG  . ARG A 1 550 ? 156.908 171.232 187.448 1.00 40.40  ? 550 ARG A CG  1 
ATOM   3835 C CD  . ARG A 1 550 ? 157.621 170.499 186.325 1.00 39.34  ? 550 ARG A CD  1 
ATOM   3836 N NE  . ARG A 1 550 ? 158.909 171.108 186.017 1.00 40.10  ? 550 ARG A NE  1 
ATOM   3837 C CZ  . ARG A 1 550 ? 159.214 171.668 184.855 1.00 42.78  ? 550 ARG A CZ  1 
ATOM   3838 N NH1 . ARG A 1 550 ? 158.352 171.691 183.852 1.00 40.14  ? 550 ARG A NH1 1 
ATOM   3839 N NH2 . ARG A 1 550 ? 160.415 172.215 184.693 1.00 45.93  ? 550 ARG A NH2 1 
ATOM   3840 N N   . GLY A 1 551 ? 156.319 169.805 191.239 1.00 47.26  ? 551 GLY A N   1 
ATOM   3841 C CA  . GLY A 1 551 ? 156.367 168.850 192.319 1.00 63.80  ? 551 GLY A CA  1 
ATOM   3842 C C   . GLY A 1 551 ? 155.428 169.206 193.451 1.00 66.32  ? 551 GLY A C   1 
ATOM   3843 O O   . GLY A 1 551 ? 154.967 170.345 193.576 1.00 64.14  ? 551 GLY A O   1 
ATOM   3844 N N   . PRO A 1 552 ? 155.084 168.265 194.364 1.00 74.99  ? 552 PRO A N   1 
ATOM   3845 C CA  . PRO A 1 552 ? 154.122 168.573 195.410 1.00 74.75  ? 552 PRO A CA  1 
ATOM   3846 C C   . PRO A 1 552 ? 154.809 169.230 196.596 1.00 76.24  ? 552 PRO A C   1 
ATOM   3847 O O   . PRO A 1 552 ? 154.154 169.428 197.637 1.00 76.91  ? 552 PRO A O   1 
ATOM   3848 C CB  . PRO A 1 552 ? 153.574 167.187 195.741 1.00 79.49  ? 552 PRO A CB  1 
ATOM   3849 C CG  . PRO A 1 552 ? 154.774 166.283 195.596 1.00 78.27  ? 552 PRO A CG  1 
ATOM   3850 C CD  . PRO A 1 552 ? 155.583 166.886 194.460 1.00 76.34  ? 552 PRO A CD  1 
ATOM   3851 N N   . ASP A 1 553 ? 156.092 169.574 196.443 1.00 76.04  ? 553 ASP A N   1 
ATOM   3852 C CA  . ASP A 1 553 ? 156.872 170.183 197.555 1.00 73.67  ? 553 ASP A CA  1 
ATOM   3853 C C   . ASP A 1 553 ? 157.325 171.588 197.159 1.00 68.15  ? 553 ASP A C   1 
ATOM   3854 O O   . ASP A 1 553 ? 158.285 172.094 197.778 1.00 70.52  ? 553 ASP A O   1 
ATOM   3855 C CB  . ASP A 1 553 ? 158.066 169.321 197.925 1.00 80.41  ? 553 ASP A CB  1 
ATOM   3856 C CG  . ASP A 1 553 ? 159.021 169.017 196.780 1.00 78.42  ? 553 ASP A CG  1 
ATOM   3857 O OD1 . ASP A 1 553 ? 158.569 168.408 195.788 1.00 78.17  ? 553 ASP A OD1 1 
ATOM   3858 O OD2 . ASP A 1 553 ? 160.205 169.396 196.889 1.00 72.54  ? 553 ASP A OD2 1 
ATOM   3859 N N   . ASN A 1 554 ? 156.665 172.194 196.171 1.00 62.03  ? 554 ASN A N   1 
ATOM   3860 C CA  . ASN A 1 554 ? 157.054 173.516 195.698 1.00 55.61  ? 554 ASN A CA  1 
ATOM   3861 C C   . ASN A 1 554 ? 155.859 174.461 195.642 1.00 55.42  ? 554 ASN A C   1 
ATOM   3862 O O   . ASN A 1 554 ? 155.725 175.267 194.719 1.00 56.55  ? 554 ASN A O   1 
ATOM   3863 C CB  . ASN A 1 554 ? 157.731 173.423 194.334 1.00 51.92  ? 554 ASN A CB  1 
ATOM   3864 C CG  . ASN A 1 554 ? 159.242 173.406 194.434 1.00 56.28  ? 554 ASN A CG  1 
ATOM   3865 O OD1 . ASN A 1 554 ? 159.829 174.108 195.257 1.00 61.59  ? 554 ASN A OD1 1 
ATOM   3866 N ND2 . ASN A 1 554 ? 159.882 172.602 193.593 1.00 58.13  ? 554 ASN A ND2 1 
ATOM   3867 N N   . CYS A 1 555 ? 154.979 174.353 196.642 1.00 62.90  ? 555 CYS A N   1 
ATOM   3868 C CA  . CYS A 1 555 ? 153.838 175.302 196.736 1.00 68.64  ? 555 CYS A CA  1 
ATOM   3869 C C   . CYS A 1 555 ? 153.654 175.720 198.204 1.00 79.54  ? 555 CYS A C   1 
ATOM   3870 O O   . CYS A 1 555 ? 153.992 174.906 199.091 1.00 81.27  ? 555 CYS A O   1 
ATOM   3871 C CB  . CYS A 1 555 ? 152.557 174.723 196.149 1.00 68.46  ? 555 CYS A CB  1 
ATOM   3872 S SG  . CYS A 1 555 ? 152.352 172.935 196.352 1.00 71.99  ? 555 CYS A SG  1 
ATOM   3873 N N   . ILE A 1 556 ? 153.139 176.932 198.438 1.00 79.54  ? 556 ILE A N   1 
ATOM   3874 C CA  . ILE A 1 556 ? 153.012 177.505 199.811 1.00 87.69  ? 556 ILE A CA  1 
ATOM   3875 C C   . ILE A 1 556 ? 151.780 176.909 200.497 1.00 87.47  ? 556 ILE A C   1 
ATOM   3876 O O   . ILE A 1 556 ? 151.839 176.721 201.732 1.00 95.38  ? 556 ILE A O   1 
ATOM   3877 C CB  . ILE A 1 556 ? 152.923 179.040 199.720 1.00 92.96  ? 556 ILE A CB  1 
ATOM   3878 C CG1 . ILE A 1 556 ? 154.120 179.634 198.976 1.00 94.43  ? 556 ILE A CG1 1 
ATOM   3879 C CG2 . ILE A 1 556 ? 152.753 179.669 201.102 1.00 94.65  ? 556 ILE A CG2 1 
ATOM   3880 C CD1 . ILE A 1 556 ? 153.850 179.967 197.519 1.00 79.76  ? 556 ILE A CD1 1 
ATOM   3881 N N   . GLN A 1 557 ? 150.719 176.624 199.742 1.00 77.90  ? 557 GLN A N   1 
ATOM   3882 C CA  . GLN A 1 557 ? 149.473 176.106 200.285 1.00 84.95  ? 557 GLN A CA  1 
ATOM   3883 C C   . GLN A 1 557 ? 149.034 174.877 199.502 1.00 84.59  ? 557 GLN A C   1 
ATOM   3884 O O   . GLN A 1 557 ? 149.068 174.871 198.268 1.00 83.39  ? 557 GLN A O   1 
ATOM   3885 C CB  . GLN A 1 557 ? 148.374 177.173 200.247 1.00 86.50  ? 557 GLN A CB  1 
ATOM   3886 C CG  . GLN A 1 557 ? 148.481 178.212 201.351 1.00 89.52  ? 557 GLN A CG  1 
ATOM   3887 C CD  . GLN A 1 557 ? 147.204 178.341 202.158 1.00 90.39  ? 557 GLN A CD  1 
ATOM   3888 O OE1 . GLN A 1 557 ? 146.119 178.013 201.680 1.00 83.51  ? 557 GLN A OE1 1 
ATOM   3889 N NE2 . GLN A 1 557 ? 147.329 178.823 203.389 1.00 87.89  ? 557 GLN A NE2 1 
ATOM   3890 N N   . CYS A 1 558 ? 148.642 173.831 200.238 1.00 86.75  ? 558 CYS A N   1 
ATOM   3891 C CA  . CYS A 1 558 ? 148.199 172.566 199.599 1.00 92.48  ? 558 CYS A CA  1 
ATOM   3892 C C   . CYS A 1 558 ? 146.713 172.334 199.905 1.00 91.50  ? 558 CYS A C   1 
ATOM   3893 O O   . CYS A 1 558 ? 146.356 172.307 201.102 1.00 90.58  ? 558 CYS A O   1 
ATOM   3894 C CB  . CYS A 1 558 ? 148.996 171.380 200.130 1.00 100.61 ? 558 CYS A CB  1 
ATOM   3895 S SG  . CYS A 1 558 ? 150.761 171.723 200.356 1.00 104.34 ? 558 CYS A SG  1 
ATOM   3896 N N   . ALA A 1 559 ? 145.888 172.175 198.869 1.00 92.93  ? 559 ALA A N   1 
ATOM   3897 C CA  . ALA A 1 559 ? 144.458 171.948 199.049 1.00 96.71  ? 559 ALA A CA  1 
ATOM   3898 C C   . ALA A 1 559 ? 144.200 170.694 199.874 1.00 100.08 ? 559 ALA A C   1 
ATOM   3899 O O   . ALA A 1 559 ? 143.321 170.681 200.743 1.00 98.35  ? 559 ALA A O   1 
ATOM   3900 C CB  . ALA A 1 559 ? 143.763 171.850 197.692 1.00 88.19  ? 559 ALA A CB  1 
ATOM   3901 N N   . HIS A 1 560 ? 144.955 169.633 199.616 1.00 97.27  ? 560 HIS A N   1 
ATOM   3902 C CA  . HIS A 1 560 ? 144.850 168.393 200.361 1.00 97.67  ? 560 HIS A CA  1 
ATOM   3903 C C   . HIS A 1 560 ? 145.939 168.351 201.431 1.00 104.65 ? 560 HIS A C   1 
ATOM   3904 O O   . HIS A 1 560 ? 146.651 169.332 201.667 1.00 104.06 ? 560 HIS A O   1 
ATOM   3905 C CB  . HIS A 1 560 ? 144.928 167.200 199.407 1.00 100.38 ? 560 HIS A CB  1 
ATOM   3906 C CG  . HIS A 1 560 ? 143.985 167.291 198.248 1.00 103.99 ? 560 HIS A CG  1 
ATOM   3907 N ND1 . HIS A 1 560 ? 144.268 168.018 197.112 1.00 101.74 ? 560 HIS A ND1 1 
ATOM   3908 C CD2 . HIS A 1 560 ? 142.762 166.745 198.049 1.00 107.06 ? 560 HIS A CD2 1 
ATOM   3909 C CE1 . HIS A 1 560 ? 143.261 167.917 196.264 1.00 99.21  ? 560 HIS A CE1 1 
ATOM   3910 N NE2 . HIS A 1 560 ? 142.334 167.149 196.808 1.00 105.41 ? 560 HIS A NE2 1 
ATOM   3911 N N   . TYR A 1 561 ? 146.078 167.173 202.039 1.00 110.66 ? 561 TYR A N   1 
ATOM   3912 C CA  . TYR A 1 561 ? 147.057 167.021 203.144 1.00 109.69 ? 561 TYR A CA  1 
ATOM   3913 C C   . TYR A 1 561 ? 148.472 167.150 202.619 1.00 104.80 ? 561 TYR A C   1 
ATOM   3914 O O   . TYR A 1 561 ? 148.718 166.910 201.421 1.00 104.80 ? 561 TYR A O   1 
ATOM   3915 C CB  . TYR A 1 561 ? 146.830 165.669 203.826 1.00 111.79 ? 561 TYR A CB  1 
ATOM   3916 C CG  . TYR A 1 561 ? 145.362 165.306 204.001 1.00 114.74 ? 561 TYR A CG  1 
ATOM   3917 C CD1 . TYR A 1 561 ? 144.619 165.815 205.058 1.00 114.65 ? 561 TYR A CD1 1 
ATOM   3918 C CD2 . TYR A 1 561 ? 144.726 164.444 203.117 1.00 113.16 ? 561 TYR A CD2 1 
ATOM   3919 C CE1 . TYR A 1 561 ? 143.284 165.488 205.223 1.00 116.55 ? 561 TYR A CE1 1 
ATOM   3920 C CE2 . TYR A 1 561 ? 143.392 164.108 203.272 1.00 113.99 ? 561 TYR A CE2 1 
ATOM   3921 C CZ  . TYR A 1 561 ? 142.669 164.631 204.329 1.00 118.26 ? 561 TYR A CZ  1 
ATOM   3922 O OH  . TYR A 1 561 ? 141.354 164.303 204.488 1.00 116.39 ? 561 TYR A OH  1 
ATOM   3923 N N   . ILE A 1 562 ? 149.402 167.526 203.501 1.00 106.93 ? 562 ILE A N   1 
ATOM   3924 C CA  . ILE A 1 562 ? 150.834 167.644 203.088 1.00 107.87 ? 562 ILE A CA  1 
ATOM   3925 C C   . ILE A 1 562 ? 151.670 166.610 203.861 1.00 107.23 ? 562 ILE A C   1 
ATOM   3926 O O   . ILE A 1 562 ? 151.682 166.662 205.109 1.00 105.19 ? 562 ILE A O   1 
ATOM   3927 C CB  . ILE A 1 562 ? 151.356 169.082 203.279 1.00 103.40 ? 562 ILE A CB  1 
ATOM   3928 C CG1 . ILE A 1 562 ? 152.850 169.177 202.975 1.00 94.60  ? 562 ILE A CG1 1 
ATOM   3929 C CG2 . ILE A 1 562 ? 151.024 169.620 204.671 1.00 105.31 ? 562 ILE A CG2 1 
ATOM   3930 C CD1 . ILE A 1 562 ? 153.408 170.586 203.045 1.00 93.30  ? 562 ILE A CD1 1 
ATOM   3931 N N   . ASP A 1 563 ? 152.321 165.693 203.141 1.00 103.75 ? 563 ASP A N   1 
ATOM   3932 C CA  . ASP A 1 563 ? 153.209 164.693 203.794 1.00 102.43 ? 563 ASP A CA  1 
ATOM   3933 C C   . ASP A 1 563 ? 154.615 165.288 203.875 1.00 96.42  ? 563 ASP A C   1 
ATOM   3934 O O   . ASP A 1 563 ? 155.265 165.407 202.815 1.00 94.07  ? 563 ASP A O   1 
ATOM   3935 C CB  . ASP A 1 563 ? 153.190 163.367 203.052 1.00 105.26 ? 563 ASP A CB  1 
ATOM   3936 C CG  . ASP A 1 563 ? 154.180 162.324 203.549 1.00 105.73 ? 563 ASP A CG  1 
ATOM   3937 O OD1 . ASP A 1 563 ? 154.101 161.962 204.741 1.00 105.86 ? 563 ASP A OD1 1 
ATOM   3938 O OD2 . ASP A 1 563 ? 155.016 161.880 202.737 1.00 101.98 ? 563 ASP A OD2 1 
ATOM   3939 N N   . GLY A 1 564 ? 155.060 165.655 205.078 1.00 95.46  ? 564 GLY A N   1 
ATOM   3940 C CA  . GLY A 1 564 ? 156.373 166.312 205.206 1.00 89.00  ? 564 GLY A CA  1 
ATOM   3941 C C   . GLY A 1 564 ? 156.414 167.544 204.328 1.00 86.77  ? 564 GLY A C   1 
ATOM   3942 O O   . GLY A 1 564 ? 155.613 168.467 204.575 1.00 93.26  ? 564 GLY A O   1 
ATOM   3943 N N   . PRO A 1 565 ? 157.302 167.617 203.314 1.00 81.24  ? 565 PRO A N   1 
ATOM   3944 C CA  . PRO A 1 565 ? 157.303 168.747 202.397 1.00 80.06  ? 565 PRO A CA  1 
ATOM   3945 C C   . PRO A 1 565 ? 156.391 168.562 201.194 1.00 86.34  ? 565 PRO A C   1 
ATOM   3946 O O   . PRO A 1 565 ? 156.106 169.565 200.515 1.00 87.64  ? 565 PRO A O   1 
ATOM   3947 C CB  . PRO A 1 565 ? 158.784 168.780 201.994 1.00 71.07  ? 565 PRO A CB  1 
ATOM   3948 C CG  . PRO A 1 565 ? 159.189 167.323 201.973 1.00 77.86  ? 565 PRO A CG  1 
ATOM   3949 C CD  . PRO A 1 565 ? 158.350 166.646 203.046 1.00 81.52  ? 565 PRO A CD  1 
ATOM   3950 N N   . HIS A 1 566 ? 155.934 167.340 200.886 1.00 88.61  ? 566 HIS A N   1 
ATOM   3951 C CA  . HIS A 1 566 ? 155.172 167.047 199.636 1.00 85.02  ? 566 HIS A CA  1 
ATOM   3952 C C   . HIS A 1 566 ? 153.652 166.957 199.831 1.00 89.22  ? 566 HIS A C   1 
ATOM   3953 O O   . HIS A 1 566 ? 153.248 165.947 200.399 1.00 93.70  ? 566 HIS A O   1 
ATOM   3954 C CB  . HIS A 1 566 ? 155.616 165.689 199.080 1.00 84.12  ? 566 HIS A CB  1 
ATOM   3955 C CG  . HIS A 1 566 ? 157.082 165.548 198.858 1.00 76.64  ? 566 HIS A CG  1 
ATOM   3956 N ND1 . HIS A 1 566 ? 157.726 165.943 197.706 1.00 74.34  ? 566 HIS A ND1 1 
ATOM   3957 C CD2 . HIS A 1 566 ? 158.024 165.033 199.655 1.00 78.87  ? 566 HIS A CD2 1 
ATOM   3958 C CE1 . HIS A 1 566 ? 159.019 165.678 197.821 1.00 80.24  ? 566 HIS A CE1 1 
ATOM   3959 N NE2 . HIS A 1 566 ? 159.222 165.125 198.997 1.00 82.33  ? 566 HIS A NE2 1 
ATOM   3960 N N   . CYS A 1 567 ? 152.844 167.848 199.232 1.00 87.95  ? 567 CYS A N   1 
ATOM   3961 C CA  . CYS A 1 567 ? 151.365 167.848 199.386 1.00 90.31  ? 567 CYS A CA  1 
ATOM   3962 C C   . CYS A 1 567 ? 150.802 166.595 198.696 1.00 95.40  ? 567 CYS A C   1 
ATOM   3963 O O   . CYS A 1 567 ? 151.174 166.357 197.530 1.00 96.09  ? 567 CYS A O   1 
ATOM   3964 C CB  . CYS A 1 567 ? 150.747 169.085 198.749 1.00 91.45  ? 567 CYS A CB  1 
ATOM   3965 S SG  . CYS A 1 567 ? 151.723 170.600 198.947 1.00 106.89 ? 567 CYS A SG  1 
ATOM   3966 N N   . VAL A 1 568 ? 149.944 165.825 199.374 1.00 97.15  ? 568 VAL A N   1 
ATOM   3967 C CA  . VAL A 1 568 ? 149.461 164.540 198.781 1.00 98.62  ? 568 VAL A CA  1 
ATOM   3968 C C   . VAL A 1 568 ? 147.931 164.445 198.886 1.00 102.42 ? 568 VAL A C   1 
ATOM   3969 O O   . VAL A 1 568 ? 147.369 165.031 199.835 1.00 104.87 ? 568 VAL A O   1 
ATOM   3970 C CB  . VAL A 1 568 ? 150.142 163.371 199.517 1.00 102.29 ? 568 VAL A CB  1 
ATOM   3971 C CG1 . VAL A 1 568 ? 151.602 163.216 199.109 1.00 97.25  ? 568 VAL A CG1 1 
ATOM   3972 C CG2 . VAL A 1 568 ? 150.022 163.513 201.030 1.00 104.01 ? 568 VAL A CG2 1 
ATOM   3973 N N   . LYS A 1 569 ? 147.283 163.732 197.956 1.00 105.60 ? 569 LYS A N   1 
ATOM   3974 C CA  . LYS A 1 569 ? 145.839 163.543 198.074 1.00 109.34 ? 569 LYS A CA  1 
ATOM   3975 C C   . LYS A 1 569 ? 145.472 162.983 199.442 1.00 113.83 ? 569 LYS A C   1 
ATOM   3976 O O   . LYS A 1 569 ? 144.610 163.529 200.141 1.00 114.43 ? 569 LYS A O   1 
ATOM   3977 C CB  . LYS A 1 569 ? 145.335 162.612 196.969 1.00 108.56 ? 569 LYS A CB  1 
ATOM   3978 C CG  . LYS A 1 569 ? 145.269 163.233 195.582 1.00 105.88 ? 569 LYS A CG  1 
ATOM   3979 C CD  . LYS A 1 569 ? 144.082 164.171 195.442 1.00 108.08 ? 569 LYS A CD  1 
ATOM   3980 C CE  . LYS A 1 569 ? 142.804 163.403 195.144 1.00 106.83 ? 569 LYS A CE  1 
ATOM   3981 N NZ  . LYS A 1 569 ? 141.699 164.309 194.725 1.00 100.47 ? 569 LYS A NZ  1 
ATOM   3982 N N   . THR A 1 570 ? 146.113 161.886 199.835 1.00 112.62 ? 570 THR A N   1 
ATOM   3983 C CA  . THR A 1 570 ? 145.928 161.283 201.146 1.00 113.24 ? 570 THR A CA  1 
ATOM   3984 C C   . THR A 1 570 ? 147.292 160.973 201.743 1.00 110.58 ? 570 THR A C   1 
ATOM   3985 O O   . THR A 1 570 ? 148.268 160.762 201.019 1.00 106.93 ? 570 THR A O   1 
ATOM   3986 C CB  . THR A 1 570 ? 145.094 159.987 201.085 1.00 116.00 ? 570 THR A CB  1 
ATOM   3987 O OG1 . THR A 1 570 ? 145.960 158.869 200.853 1.00 108.95 ? 570 THR A OG1 1 
ATOM   3988 C CG2 . THR A 1 570 ? 144.050 160.052 199.977 1.00 107.68 ? 570 THR A CG2 1 
ATOM   3989 N N   . CYS A 1 571 ? 147.350 160.950 203.069 1.00 111.43 ? 571 CYS A N   1 
ATOM   3990 C CA  . CYS A 1 571 ? 148.587 160.586 203.740 1.00 109.76 ? 571 CYS A CA  1 
ATOM   3991 C C   . CYS A 1 571 ? 148.950 159.144 203.392 1.00 108.80 ? 571 CYS A C   1 
ATOM   3992 O O   . CYS A 1 571 ? 148.059 158.299 203.244 1.00 106.38 ? 571 CYS A O   1 
ATOM   3993 C CB  . CYS A 1 571 ? 148.448 160.747 205.255 1.00 112.28 ? 571 CYS A CB  1 
ATOM   3994 S SG  . CYS A 1 571 ? 148.137 162.441 205.809 1.00 118.38 ? 571 CYS A SG  1 
ATOM   3995 N N   . PRO A 1 572 ? 150.240 158.827 203.241 1.00 108.22 ? 572 PRO A N   1 
ATOM   3996 C CA  . PRO A 1 572 ? 150.620 157.470 202.824 1.00 107.07 ? 572 PRO A CA  1 
ATOM   3997 C C   . PRO A 1 572 ? 150.227 156.416 203.846 1.00 108.94 ? 572 PRO A C   1 
ATOM   3998 O O   . PRO A 1 572 ? 150.786 156.360 204.946 1.00 110.38 ? 572 PRO A O   1 
ATOM   3999 C CB  . PRO A 1 572 ? 152.143 157.563 202.665 1.00 101.22 ? 572 PRO A CB  1 
ATOM   4000 C CG  . PRO A 1 572 ? 152.547 158.720 203.515 1.00 105.79 ? 572 PRO A CG  1 
ATOM   4001 C CD  . PRO A 1 572 ? 151.412 159.696 203.443 1.00 108.23 ? 572 PRO A CD  1 
ATOM   4002 N N   . ALA A 1 573 ? 149.262 155.573 203.484 1.00 109.20 ? 573 ALA A N   1 
ATOM   4003 C CA  . ALA A 1 573 ? 148.751 154.532 204.363 1.00 108.55 ? 573 ALA A CA  1 
ATOM   4004 C C   . ALA A 1 573 ? 148.711 153.215 203.605 1.00 104.41 ? 573 ALA A C   1 
ATOM   4005 O O   . ALA A 1 573 ? 148.197 153.156 202.483 1.00 95.73  ? 573 ALA A O   1 
ATOM   4006 C CB  . ALA A 1 573 ? 147.356 154.887 204.888 1.00 109.96 ? 573 ALA A CB  1 
ATOM   4007 N N   . GLY A 1 574 ? 149.253 152.164 204.217 1.00 107.48 ? 574 GLY A N   1 
ATOM   4008 C CA  . GLY A 1 574 ? 149.268 150.851 203.609 1.00 108.44 ? 574 GLY A CA  1 
ATOM   4009 C C   . GLY A 1 574 ? 150.374 150.615 202.606 1.00 109.46 ? 574 GLY A C   1 
ATOM   4010 O O   . GLY A 1 574 ? 150.436 149.523 202.027 1.00 111.16 ? 574 GLY A O   1 
ATOM   4011 N N   . VAL A 1 575 ? 151.245 151.592 202.379 1.00 106.25 ? 575 VAL A N   1 
ATOM   4012 C CA  . VAL A 1 575 ? 152.327 151.442 201.414 1.00 101.49 ? 575 VAL A CA  1 
ATOM   4013 C C   . VAL A 1 575 ? 153.483 150.689 202.058 1.00 105.92 ? 575 VAL A C   1 
ATOM   4014 O O   . VAL A 1 575 ? 153.728 150.788 203.265 1.00 107.05 ? 575 VAL A O   1 
ATOM   4015 C CB  . VAL A 1 575 ? 152.775 152.818 200.884 1.00 95.75  ? 575 VAL A CB  1 
ATOM   4016 C CG1 . VAL A 1 575 ? 153.501 152.664 199.558 1.00 95.24  ? 575 VAL A CG1 1 
ATOM   4017 C CG2 . VAL A 1 575 ? 151.579 153.746 200.739 1.00 100.29 ? 575 VAL A CG2 1 
ATOM   4018 N N   . MET A 1 576 ? 154.202 149.924 201.240 1.00 105.14 ? 576 MET A N   1 
ATOM   4019 C CA  . MET A 1 576 ? 155.342 149.163 201.732 1.00 105.93 ? 576 MET A CA  1 
ATOM   4020 C C   . MET A 1 576 ? 156.500 150.100 202.052 1.00 103.69 ? 576 MET A C   1 
ATOM   4021 O O   . MET A 1 576 ? 156.857 150.963 201.245 1.00 102.29 ? 576 MET A O   1 
ATOM   4022 C CB  . MET A 1 576 ? 155.766 148.121 200.697 1.00 105.22 ? 576 MET A CB  1 
ATOM   4023 C CG  . MET A 1 576 ? 157.220 147.689 200.795 1.00 102.51 ? 576 MET A CG  1 
ATOM   4024 S SD  . MET A 1 576 ? 157.581 146.639 202.217 1.00 114.41 ? 576 MET A SD  1 
ATOM   4025 C CE  . MET A 1 576 ? 156.046 145.731 202.399 1.00 107.84 ? 576 MET A CE  1 
ATOM   4026 N N   . GLY A 1 577 ? 157.088 149.928 203.234 1.00 102.77 ? 577 GLY A N   1 
ATOM   4027 C CA  . GLY A 1 577 ? 158.164 150.795 203.671 1.00 104.04 ? 577 GLY A CA  1 
ATOM   4028 C C   . GLY A 1 577 ? 159.460 150.070 203.970 1.00 101.75 ? 577 GLY A C   1 
ATOM   4029 O O   . GLY A 1 577 ? 159.718 148.990 203.431 1.00 105.85 ? 577 GLY A O   1 
ATOM   4030 N N   . GLU A 1 578 ? 160.283 150.661 204.832 1.00 99.64  ? 578 GLU A N   1 
ATOM   4031 C CA  . GLU A 1 578 ? 161.576 150.082 205.164 1.00 103.30 ? 578 GLU A CA  1 
ATOM   4032 C C   . GLU A 1 578 ? 161.410 148.806 205.983 1.00 105.18 ? 578 GLU A C   1 
ATOM   4033 O O   . GLU A 1 578 ? 160.419 148.621 206.695 1.00 108.61 ? 578 GLU A O   1 
ATOM   4034 C CB  . GLU A 1 578 ? 162.428 151.088 205.937 1.00 108.55 ? 578 GLU A CB  1 
ATOM   4035 C CG  . GLU A 1 578 ? 162.393 152.499 205.372 1.00 109.90 ? 578 GLU A CG  1 
ATOM   4036 C CD  . GLU A 1 578 ? 163.539 152.776 204.419 1.00 109.40 ? 578 GLU A CD  1 
ATOM   4037 O OE1 . GLU A 1 578 ? 164.684 152.932 204.894 1.00 105.94 ? 578 GLU A OE1 1 
ATOM   4038 O OE2 . GLU A 1 578 ? 163.295 152.840 203.196 1.00 106.84 ? 578 GLU A OE2 1 
ATOM   4039 N N   . ASN A 1 579 ? 162.402 147.920 205.867 1.00 103.84 ? 579 ASN A N   1 
ATOM   4040 C CA  . ASN A 1 579 ? 162.452 146.663 206.618 1.00 104.60 ? 579 ASN A CA  1 
ATOM   4041 C C   . ASN A 1 579 ? 161.224 145.792 206.365 1.00 106.25 ? 579 ASN A C   1 
ATOM   4042 O O   . ASN A 1 579 ? 160.775 145.066 207.256 1.00 105.91 ? 579 ASN A O   1 
ATOM   4043 C CB  . ASN A 1 579 ? 162.624 146.919 208.119 1.00 106.30 ? 579 ASN A CB  1 
ATOM   4044 C CG  . ASN A 1 579 ? 163.735 147.907 208.417 1.00 110.79 ? 579 ASN A CG  1 
ATOM   4045 O OD1 . ASN A 1 579 ? 164.846 147.784 207.902 1.00 112.62 ? 579 ASN A OD1 1 
ATOM   4046 N ND2 . ASN A 1 579 ? 163.439 148.895 209.254 1.00 103.54 ? 579 ASN A ND2 1 
ATOM   4047 N N   . ASN A 1 580 ? 160.683 145.857 205.147 1.00 106.68 ? 580 ASN A N   1 
ATOM   4048 C CA  . ASN A 1 580 ? 159.536 145.043 204.739 1.00 106.55 ? 580 ASN A CA  1 
ATOM   4049 C C   . ASN A 1 580 ? 158.354 145.223 205.690 1.00 108.65 ? 580 ASN A C   1 
ATOM   4050 O O   . ASN A 1 580 ? 157.660 144.268 206.043 1.00 105.96 ? 580 ASN A O   1 
ATOM   4051 C CB  . ASN A 1 580 ? 159.924 143.567 204.626 1.00 104.06 ? 580 ASN A CB  1 
ATOM   4052 C CG  . ASN A 1 580 ? 160.190 143.143 203.195 1.00 100.62 ? 580 ASN A CG  1 
ATOM   4053 O OD1 . ASN A 1 580 ? 159.332 142.550 202.541 1.00 101.13 ? 580 ASN A OD1 1 
ATOM   4054 N ND2 . ASN A 1 580 ? 161.384 143.446 202.700 1.00 100.34 ? 580 ASN A ND2 1 
ATOM   4055 N N   . THR A 1 581 ? 158.123 146.465 206.108 1.00 107.76 ? 581 THR A N   1 
ATOM   4056 C CA  . THR A 1 581 ? 157.035 146.795 207.020 1.00 107.63 ? 581 THR A CA  1 
ATOM   4057 C C   . THR A 1 581 ? 156.170 147.880 206.400 1.00 110.18 ? 581 THR A C   1 
ATOM   4058 O O   . THR A 1 581 ? 156.690 148.886 205.905 1.00 106.10 ? 581 THR A O   1 
ATOM   4059 C CB  . THR A 1 581 ? 157.568 147.259 208.381 1.00 106.31 ? 581 THR A CB  1 
ATOM   4060 O OG1 . THR A 1 581 ? 158.663 146.425 208.778 1.00 103.31 ? 581 THR A OG1 1 
ATOM   4061 C CG2 . THR A 1 581 ? 156.472 147.185 209.434 1.00 104.84 ? 581 THR A CG2 1 
ATOM   4062 N N   . LEU A 1 582 ? 154.857 147.674 206.425 1.00 117.26 ? 582 LEU A N   1 
ATOM   4063 C CA  . LEU A 1 582 ? 153.928 148.669 205.911 1.00 114.55 ? 582 LEU A CA  1 
ATOM   4064 C C   . LEU A 1 582 ? 153.947 149.919 206.783 1.00 112.81 ? 582 LEU A C   1 
ATOM   4065 O O   . LEU A 1 582 ? 154.106 149.851 208.004 1.00 111.67 ? 582 LEU A O   1 
ATOM   4066 C CB  . LEU A 1 582 ? 152.512 148.098 205.849 1.00 111.87 ? 582 LEU A CB  1 
ATOM   4067 C CG  . LEU A 1 582 ? 152.275 146.932 204.887 1.00 112.00 ? 582 LEU A CG  1 
ATOM   4068 C CD1 . LEU A 1 582 ? 150.831 146.461 204.962 1.00 112.51 ? 582 LEU A CD1 1 
ATOM   4069 C CD2 . LEU A 1 582 ? 152.640 147.326 203.465 1.00 108.14 ? 582 LEU A CD2 1 
ATOM   4070 N N   . VAL A 1 583 ? 153.782 151.072 206.140 1.00 112.35 ? 583 VAL A N   1 
ATOM   4071 C CA  . VAL A 1 583 ? 153.756 152.361 206.822 1.00 111.96 ? 583 VAL A CA  1 
ATOM   4072 C C   . VAL A 1 583 ? 152.382 152.986 206.623 1.00 110.25 ? 583 VAL A C   1 
ATOM   4073 O O   . VAL A 1 583 ? 151.787 152.869 205.544 1.00 108.86 ? 583 VAL A O   1 
ATOM   4074 C CB  . VAL A 1 583 ? 154.881 153.295 206.331 1.00 107.95 ? 583 VAL A CB  1 
ATOM   4075 C CG1 . VAL A 1 583 ? 156.201 152.543 206.270 1.00 107.06 ? 583 VAL A CG1 1 
ATOM   4076 C CG2 . VAL A 1 583 ? 154.554 153.892 204.971 1.00 105.74 ? 583 VAL A CG2 1 
ATOM   4077 N N   . TRP A 1 584 ? 151.859 153.599 207.680 1.00 107.89 ? 584 TRP A N   1 
ATOM   4078 C CA  . TRP A 1 584 ? 150.571 154.276 207.652 1.00 108.57 ? 584 TRP A CA  1 
ATOM   4079 C C   . TRP A 1 584 ? 150.722 155.653 208.280 1.00 110.28 ? 584 TRP A C   1 
ATOM   4080 O O   . TRP A 1 584 ? 151.410 155.811 209.293 1.00 111.88 ? 584 TRP A O   1 
ATOM   4081 C CB  . TRP A 1 584 ? 149.495 153.470 208.396 1.00 108.83 ? 584 TRP A CB  1 
ATOM   4082 C CG  . TRP A 1 584 ? 149.352 152.045 207.931 1.00 109.91 ? 584 TRP A CG  1 
ATOM   4083 C CD1 . TRP A 1 584 ? 150.266 151.039 208.067 1.00 110.70 ? 584 TRP A CD1 1 
ATOM   4084 C CD2 . TRP A 1 584 ? 148.225 151.471 207.256 1.00 113.35 ? 584 TRP A CD2 1 
ATOM   4085 N NE1 . TRP A 1 584 ? 149.780 149.878 207.519 1.00 111.52 ? 584 TRP A NE1 1 
ATOM   4086 C CE2 . TRP A 1 584 ? 148.528 150.116 207.015 1.00 114.89 ? 584 TRP A CE2 1 
ATOM   4087 C CE3 . TRP A 1 584 ? 146.990 151.970 206.834 1.00 113.47 ? 584 TRP A CE3 1 
ATOM   4088 C CZ2 . TRP A 1 584 ? 147.642 149.256 206.370 1.00 113.75 ? 584 TRP A CZ2 1 
ATOM   4089 C CZ3 . TRP A 1 584 ? 146.111 151.115 206.193 1.00 114.62 ? 584 TRP A CZ3 1 
ATOM   4090 C CH2 . TRP A 1 584 ? 146.442 149.773 205.967 1.00 113.17 ? 584 TRP A CH2 1 
ATOM   4091 N N   . LYS A 1 585 ? 150.081 156.651 207.675 1.00 110.34 ? 585 LYS A N   1 
ATOM   4092 C CA  . LYS A 1 585 ? 150.177 158.028 208.137 1.00 109.13 ? 585 LYS A CA  1 
ATOM   4093 C C   . LYS A 1 585 ? 148.788 158.638 208.245 1.00 111.69 ? 585 LYS A C   1 
ATOM   4094 O O   . LYS A 1 585 ? 147.899 158.331 207.446 1.00 113.66 ? 585 LYS A O   1 
ATOM   4095 C CB  . LYS A 1 585 ? 151.048 158.871 207.196 1.00 106.23 ? 585 LYS A CB  1 
ATOM   4096 C CG  . LYS A 1 585 ? 152.513 158.465 207.181 1.00 106.04 ? 585 LYS A CG  1 
ATOM   4097 C CD  . LYS A 1 585 ? 153.426 159.674 207.290 1.00 102.09 ? 585 LYS A CD  1 
ATOM   4098 C CE  . LYS A 1 585 ? 154.807 159.373 206.732 1.00 99.83  ? 585 LYS A CE  1 
ATOM   4099 N NZ  . LYS A 1 585 ? 155.844 160.282 207.293 1.00 97.25  ? 585 LYS A NZ  1 
ATOM   4100 N N   . TYR A 1 586 ? 148.613 159.502 209.238 1.00 116.48 ? 586 TYR A N   1 
ATOM   4101 C CA  . TYR A 1 586 ? 147.374 160.230 209.472 1.00 117.94 ? 586 TYR A CA  1 
ATOM   4102 C C   . TYR A 1 586 ? 147.634 161.726 209.318 1.00 119.66 ? 586 TYR A C   1 
ATOM   4103 O O   . TYR A 1 586 ? 148.772 162.168 209.150 1.00 119.89 ? 586 TYR A O   1 
ATOM   4104 C CB  . TYR A 1 586 ? 146.803 159.905 210.856 1.00 114.53 ? 586 TYR A CB  1 
ATOM   4105 C CG  . TYR A 1 586 ? 147.667 160.373 212.006 1.00 113.70 ? 586 TYR A CG  1 
ATOM   4106 C CD1 . TYR A 1 586 ? 148.763 159.628 212.425 1.00 112.61 ? 586 TYR A CD1 1 
ATOM   4107 C CD2 . TYR A 1 586 ? 147.386 161.556 212.676 1.00 114.91 ? 586 TYR A CD2 1 
ATOM   4108 C CE1 . TYR A 1 586 ? 149.555 160.050 213.476 1.00 112.56 ? 586 TYR A CE1 1 
ATOM   4109 C CE2 . TYR A 1 586 ? 148.173 161.986 213.728 1.00 117.75 ? 586 TYR A CE2 1 
ATOM   4110 C CZ  . TYR A 1 586 ? 149.255 161.229 214.123 1.00 114.57 ? 586 TYR A CZ  1 
ATOM   4111 O OH  . TYR A 1 586 ? 150.041 161.654 215.170 1.00 106.35 ? 586 TYR A OH  1 
ATOM   4112 N N   . ALA A 1 587 ? 146.562 162.511 209.386 1.00 121.53 ? 587 ALA A N   1 
ATOM   4113 C CA  . ALA A 1 587 ? 146.630 163.951 209.185 1.00 123.24 ? 587 ALA A CA  1 
ATOM   4114 C C   . ALA A 1 587 ? 146.185 164.680 210.444 1.00 123.38 ? 587 ALA A C   1 
ATOM   4115 O O   . ALA A 1 587 ? 145.210 164.286 211.092 1.00 125.13 ? 587 ALA A O   1 
ATOM   4116 C CB  . ALA A 1 587 ? 145.762 164.384 207.999 1.00 120.78 ? 587 ALA A CB  1 
ATOM   4117 N N   . ASP A 1 588 ? 146.906 165.745 210.784 1.00 122.84 ? 588 ASP A N   1 
ATOM   4118 C CA  . ASP A 1 588 ? 146.588 166.566 211.941 1.00 125.70 ? 588 ASP A CA  1 
ATOM   4119 C C   . ASP A 1 588 ? 145.622 167.678 211.532 1.00 123.54 ? 588 ASP A C   1 
ATOM   4120 O O   . ASP A 1 588 ? 145.111 167.707 210.409 1.00 120.00 ? 588 ASP A O   1 
ATOM   4121 C CB  . ASP A 1 588 ? 147.867 167.126 212.559 1.00 126.18 ? 588 ASP A CB  1 
ATOM   4122 C CG  . ASP A 1 588 ? 148.600 166.107 213.406 1.00 122.10 ? 588 ASP A CG  1 
ATOM   4123 O OD1 . ASP A 1 588 ? 147.981 165.088 213.778 1.00 119.81 ? 588 ASP A OD1 1 
ATOM   4124 O OD2 . ASP A 1 588 ? 149.794 166.324 213.701 1.00 119.25 ? 588 ASP A OD2 1 
ATOM   4125 N N   . ALA A 1 589 ? 145.360 168.610 212.451 1.00 124.88 ? 589 ALA A N   1 
ATOM   4126 C CA  . ALA A 1 589 ? 144.486 169.736 212.136 1.00 123.97 ? 589 ALA A CA  1 
ATOM   4127 C C   . ALA A 1 589 ? 145.112 170.661 211.101 1.00 122.83 ? 589 ALA A C   1 
ATOM   4128 O O   . ALA A 1 589 ? 144.391 171.337 210.358 1.00 115.42 ? 589 ALA A O   1 
ATOM   4129 C CB  . ALA A 1 589 ? 144.148 170.513 213.408 1.00 116.08 ? 589 ALA A CB  1 
ATOM   4130 N N   . GLY A 1 590 ? 146.439 170.705 211.035 1.00 124.50 ? 590 GLY A N   1 
ATOM   4131 C CA  . GLY A 1 590 ? 147.158 171.506 210.070 1.00 121.82 ? 590 GLY A CA  1 
ATOM   4132 C C   . GLY A 1 590 ? 147.412 170.827 208.743 1.00 121.46 ? 590 GLY A C   1 
ATOM   4133 O O   . GLY A 1 590 ? 148.256 171.299 207.974 1.00 120.14 ? 590 GLY A O   1 
ATOM   4134 N N   . HIS A 1 591 ? 146.720 169.722 208.463 1.00 122.43 ? 591 HIS A N   1 
ATOM   4135 C CA  . HIS A 1 591 ? 146.827 168.942 207.232 1.00 118.62 ? 591 HIS A CA  1 
ATOM   4136 C C   . HIS A 1 591 ? 148.198 168.307 207.048 1.00 117.52 ? 591 HIS A C   1 
ATOM   4137 O O   . HIS A 1 591 ? 148.502 167.818 205.953 1.00 113.05 ? 591 HIS A O   1 
ATOM   4138 C CB  . HIS A 1 591 ? 146.485 169.779 205.993 1.00 112.67 ? 591 HIS A CB  1 
ATOM   4139 C CG  . HIS A 1 591 ? 145.026 169.794 205.659 1.00 110.07 ? 591 HIS A CG  1 
ATOM   4140 N ND1 . HIS A 1 591 ? 144.533 170.355 204.500 1.00 108.23 ? 591 HIS A ND1 1 
ATOM   4141 C CD2 . HIS A 1 591 ? 143.952 169.317 206.331 1.00 110.04 ? 591 HIS A CD2 1 
ATOM   4142 C CE1 . HIS A 1 591 ? 143.219 170.222 204.473 1.00 104.95 ? 591 HIS A CE1 1 
ATOM   4143 N NE2 . HIS A 1 591 ? 142.841 169.595 205.572 1.00 104.72 ? 591 HIS A NE2 1 
ATOM   4144 N N   . VAL A 1 592 ? 149.033 168.291 208.081 1.00 119.45 ? 592 VAL A N   1 
ATOM   4145 C CA  . VAL A 1 592 ? 150.348 167.671 207.990 1.00 118.89 ? 592 VAL A CA  1 
ATOM   4146 C C   . VAL A 1 592 ? 150.216 166.174 208.239 1.00 120.75 ? 592 VAL A C   1 
ATOM   4147 O O   . VAL A 1 592 ? 149.491 165.737 209.141 1.00 118.83 ? 592 VAL A O   1 
ATOM   4148 C CB  . VAL A 1 592 ? 151.330 168.333 208.976 1.00 115.83 ? 592 VAL A CB  1 
ATOM   4149 C CG1 . VAL A 1 592 ? 150.818 168.231 210.408 1.00 116.90 ? 592 VAL A CG1 1 
ATOM   4150 C CG2 . VAL A 1 592 ? 152.716 167.717 208.849 1.00 110.20 ? 592 VAL A CG2 1 
ATOM   4151 N N   . CYS A 1 593 ? 150.901 165.379 207.420 1.00 115.91 ? 593 CYS A N   1 
ATOM   4152 C CA  . CYS A 1 593 ? 150.870 163.925 207.541 1.00 109.72 ? 593 CYS A CA  1 
ATOM   4153 C C   . CYS A 1 593 ? 151.967 163.494 208.507 1.00 111.02 ? 593 CYS A C   1 
ATOM   4154 O O   . CYS A 1 593 ? 153.158 163.649 208.216 1.00 110.21 ? 593 CYS A O   1 
ATOM   4155 C CB  . CYS A 1 593 ? 151.043 163.261 206.178 1.00 107.24 ? 593 CYS A CB  1 
ATOM   4156 S SG  . CYS A 1 593 ? 149.670 163.521 205.027 1.00 116.77 ? 593 CYS A SG  1 
ATOM   4157 N N   . HIS A 1 594 ? 151.567 162.955 209.654 1.00 114.81 ? 594 HIS A N   1 
ATOM   4158 C CA  . HIS A 1 594 ? 152.497 162.524 210.687 1.00 116.19 ? 594 HIS A CA  1 
ATOM   4159 C C   . HIS A 1 594 ? 152.622 161.006 210.682 1.00 111.55 ? 594 HIS A C   1 
ATOM   4160 O O   . HIS A 1 594 ? 151.632 160.291 210.499 1.00 107.37 ? 594 HIS A O   1 
ATOM   4161 C CB  . HIS A 1 594 ? 152.042 163.007 212.066 1.00 114.38 ? 594 HIS A CB  1 
ATOM   4162 C CG  . HIS A 1 594 ? 152.703 164.275 212.509 1.00 116.02 ? 594 HIS A CG  1 
ATOM   4163 N ND1 . HIS A 1 594 ? 152.122 165.141 213.411 1.00 120.40 ? 594 HIS A ND1 1 
ATOM   4164 C CD2 . HIS A 1 594 ? 153.895 164.824 212.176 1.00 118.64 ? 594 HIS A CD2 1 
ATOM   4165 C CE1 . HIS A 1 594 ? 152.928 166.168 213.613 1.00 123.58 ? 594 HIS A CE1 1 
ATOM   4166 N NE2 . HIS A 1 594 ? 154.010 166.000 212.876 1.00 124.60 ? 594 HIS A NE2 1 
ATOM   4167 N N   . LEU A 1 595 ? 153.845 160.522 210.880 1.00 109.88 ? 595 LEU A N   1 
ATOM   4168 C CA  . LEU A 1 595 ? 154.089 159.087 210.911 1.00 107.74 ? 595 LEU A CA  1 
ATOM   4169 C C   . LEU A 1 595 ? 153.452 158.468 212.149 1.00 107.95 ? 595 LEU A C   1 
ATOM   4170 O O   . LEU A 1 595 ? 153.502 159.035 213.244 1.00 110.56 ? 595 LEU A O   1 
ATOM   4171 C CB  . LEU A 1 595 ? 155.594 158.808 210.884 1.00 103.53 ? 595 LEU A CB  1 
ATOM   4172 C CG  . LEU A 1 595 ? 156.099 157.382 210.634 1.00 102.86 ? 595 LEU A CG  1 
ATOM   4173 C CD1 . LEU A 1 595 ? 156.164 156.558 211.916 1.00 93.73  ? 595 LEU A CD1 1 
ATOM   4174 C CD2 . LEU A 1 595 ? 155.240 156.684 209.588 1.00 105.49 ? 595 LEU A CD2 1 
ATOM   4175 N N   . CYS A 1 596 ? 152.851 157.297 211.969 1.00 102.17 ? 596 CYS A N   1 
ATOM   4176 C CA  . CYS A 1 596 ? 152.215 156.586 213.072 1.00 99.57  ? 596 CYS A CA  1 
ATOM   4177 C C   . CYS A 1 596 ? 153.256 155.917 213.963 1.00 98.51  ? 596 CYS A C   1 
ATOM   4178 O O   . CYS A 1 596 ? 153.696 154.801 213.688 1.00 91.62  ? 596 CYS A O   1 
ATOM   4179 C CB  . CYS A 1 596 ? 151.227 155.544 212.543 1.00 97.50  ? 596 CYS A CB  1 
ATOM   4180 S SG  . CYS A 1 596 ? 149.645 156.223 211.993 1.00 110.01 ? 596 CYS A SG  1 
ATOM   4181 N N   . GLN B 2 1   ? 145.312 175.317 126.736 1.00 43.18  ? 117 GLN D N   1 
ATOM   4182 C CA  . GLN B 2 1   ? 144.953 173.916 126.549 1.00 47.93  ? 117 GLN D CA  1 
ATOM   4183 C C   . GLN B 2 1   ? 146.195 173.049 126.375 1.00 48.00  ? 117 GLN D C   1 
ATOM   4184 O O   . GLN B 2 1   ? 147.248 173.532 125.957 1.00 47.09  ? 117 GLN D O   1 
ATOM   4185 C CB  . GLN B 2 1   ? 144.027 173.756 125.342 1.00 42.95  ? 117 GLN D CB  1 
ATOM   4186 C CG  . GLN B 2 1   ? 144.719 173.937 124.001 1.00 44.52  ? 117 GLN D CG  1 
ATOM   4187 C CD  . GLN B 2 1   ? 143.821 173.595 122.830 1.00 43.79  ? 117 GLN D CD  1 
ATOM   4188 O OE1 . GLN B 2 1   ? 142.596 173.652 122.934 1.00 39.46  ? 117 GLN D OE1 1 
ATOM   4189 N NE2 . GLN B 2 1   ? 144.428 173.234 121.705 1.00 43.63  ? 117 GLN D NE2 1 
ATOM   4190 N N   . VAL B 2 2   ? 146.063 171.763 126.700 1.00 39.37  ? 118 VAL D N   1 
ATOM   4191 C CA  . VAL B 2 2   ? 147.177 170.834 126.560 1.00 36.80  ? 118 VAL D CA  1 
ATOM   4192 C C   . VAL B 2 2   ? 147.404 170.538 125.085 1.00 40.31  ? 118 VAL D C   1 
ATOM   4193 O O   . VAL B 2 2   ? 146.469 170.187 124.354 1.00 43.67  ? 118 VAL D O   1 
ATOM   4194 C CB  . VAL B 2 2   ? 146.906 169.547 127.351 1.00 31.74  ? 118 VAL D CB  1 
ATOM   4195 C CG1 . VAL B 2 2   ? 148.071 168.585 127.206 1.00 31.47  ? 118 VAL D CG1 1 
ATOM   4196 C CG2 . VAL B 2 2   ? 146.650 169.869 128.814 1.00 28.20  ? 118 VAL D CG2 1 
ATOM   4197 N N   . GLN B 2 3   ? 148.650 170.677 124.639 1.00 36.16  ? 119 GLN D N   1 
ATOM   4198 C CA  . GLN B 2 3   ? 148.985 170.467 123.233 1.00 38.05  ? 119 GLN D CA  1 
ATOM   4199 C C   . GLN B 2 3   ? 150.416 169.955 123.160 1.00 38.42  ? 119 GLN D C   1 
ATOM   4200 O O   . GLN B 2 3   ? 151.349 170.663 123.551 1.00 39.84  ? 119 GLN D O   1 
ATOM   4201 C CB  . GLN B 2 3   ? 148.817 171.758 122.435 1.00 43.99  ? 119 GLN D CB  1 
ATOM   4202 C CG  . GLN B 2 3   ? 148.644 171.558 120.940 1.00 44.88  ? 119 GLN D CG  1 
ATOM   4203 C CD  . GLN B 2 3   ? 149.637 172.359 120.124 1.00 49.09  ? 119 GLN D CD  1 
ATOM   4204 O OE1 . GLN B 2 3   ? 150.075 173.432 120.538 1.00 48.76  ? 119 GLN D OE1 1 
ATOM   4205 N NE2 . GLN B 2 3   ? 149.984 171.848 118.950 1.00 49.64  ? 119 GLN D NE2 1 
ATOM   4206 N N   . LEU B 2 4   ? 150.575 168.693 122.745 1.00 37.36  ? 120 LEU D N   1 
ATOM   4207 C CA  . LEU B 2 4   ? 151.923 168.072 122.653 1.00 34.14  ? 120 LEU D CA  1 
ATOM   4208 C C   . LEU B 2 4   ? 152.365 168.116 121.184 1.00 31.84  ? 120 LEU D C   1 
ATOM   4209 O O   . LEU B 2 4   ? 151.584 167.664 120.323 1.00 28.40  ? 120 LEU D O   1 
ATOM   4210 C CB  . LEU B 2 4   ? 151.915 166.642 123.194 1.00 23.71  ? 120 LEU D CB  1 
ATOM   4211 C CG  . LEU B 2 4   ? 151.744 166.470 124.707 1.00 17.03  ? 120 LEU D CG  1 
ATOM   4212 C CD1 . LEU B 2 4   ? 150.319 166.719 125.159 1.00 19.69  ? 120 LEU D CD1 1 
ATOM   4213 C CD2 . LEU B 2 4   ? 152.182 165.078 125.116 1.00 12.37  ? 120 LEU D CD2 1 
ATOM   4214 N N   . VAL B 2 5   ? 153.558 168.649 120.911 1.00 33.00  ? 121 VAL D N   1 
ATOM   4215 C CA  . VAL B 2 5   ? 154.014 168.811 119.499 1.00 36.75  ? 121 VAL D CA  1 
ATOM   4216 C C   . VAL B 2 5   ? 155.287 167.982 119.279 1.00 36.64  ? 121 VAL D C   1 
ATOM   4217 O O   . VAL B 2 5   ? 156.227 168.128 120.081 1.00 35.91  ? 121 VAL D O   1 
ATOM   4218 C CB  . VAL B 2 5   ? 154.265 170.297 119.181 1.00 40.69  ? 121 VAL D CB  1 
ATOM   4219 C CG1 . VAL B 2 5   ? 154.515 170.526 117.696 1.00 34.40  ? 121 VAL D CG1 1 
ATOM   4220 C CG2 . VAL B 2 5   ? 153.134 171.186 119.682 1.00 34.54  ? 121 VAL D CG2 1 
ATOM   4221 N N   . GLN B 2 6   ? 155.315 167.169 118.221 1.00 36.01  ? 122 GLN D N   1 
ATOM   4222 C CA  . GLN B 2 6   ? 156.507 166.337 117.919 1.00 37.57  ? 122 GLN D CA  1 
ATOM   4223 C C   . GLN B 2 6   ? 157.251 166.929 116.716 1.00 42.37  ? 122 GLN D C   1 
ATOM   4224 O O   . GLN B 2 6   ? 156.654 167.767 116.008 1.00 52.44  ? 122 GLN D O   1 
ATOM   4225 C CB  . GLN B 2 6   ? 156.076 164.901 117.632 1.00 37.35  ? 122 GLN D CB  1 
ATOM   4226 C CG  . GLN B 2 6   ? 155.171 164.306 118.703 1.00 28.92  ? 122 GLN D CG  1 
ATOM   4227 C CD  . GLN B 2 6   ? 154.864 162.844 118.473 1.00 20.66  ? 122 GLN D CD  1 
ATOM   4228 O OE1 . GLN B 2 6   ? 153.702 162.433 118.401 1.00 21.56  ? 122 GLN D OE1 1 
ATOM   4229 N NE2 . GLN B 2 6   ? 155.913 162.042 118.370 1.00 23.05  ? 122 GLN D NE2 1 
ATOM   4230 N N   . SER B 2 7   ? 158.499 166.507 116.494 1.00 39.74  ? 123 SER D N   1 
ATOM   4231 C CA  . SER B 2 7   ? 159.280 167.004 115.367 1.00 46.24  ? 123 SER D CA  1 
ATOM   4232 C C   . SER B 2 7   ? 158.648 166.589 114.043 1.00 51.35  ? 123 SER D C   1 
ATOM   4233 O O   . SER B 2 7   ? 158.253 167.437 113.236 1.00 51.45  ? 123 SER D O   1 
ATOM   4234 C CB  . SER B 2 7   ? 160.722 166.499 115.462 1.00 47.92  ? 123 SER D CB  1 
ATOM   4235 O OG  . SER B 2 7   ? 160.758 165.101 115.692 1.00 47.93  ? 123 SER D OG  1 
ATOM   4236 N N   . GLY B 2 8   ? 158.547 165.285 113.805 1.00 53.37  ? 124 GLY D N   1 
ATOM   4237 C CA  . GLY B 2 8   ? 157.885 164.771 112.626 1.00 48.07  ? 124 GLY D CA  1 
ATOM   4238 C C   . GLY B 2 8   ? 158.744 164.860 111.378 1.00 60.03  ? 124 GLY D C   1 
ATOM   4239 O O   . GLY B 2 8   ? 159.762 165.552 111.322 1.00 63.76  ? 124 GLY D O   1 
ATOM   4240 N N   . ALA B 2 9   ? 158.305 164.132 110.349 1.00 59.73  ? 125 ALA D N   1 
ATOM   4241 C CA  . ALA B 2 9   ? 158.939 164.131 109.030 1.00 63.56  ? 125 ALA D CA  1 
ATOM   4242 C C   . ALA B 2 9   ? 160.424 163.775 109.128 1.00 69.96  ? 125 ALA D C   1 
ATOM   4243 O O   . ALA B 2 9   ? 161.309 164.569 108.803 1.00 69.04  ? 125 ALA D O   1 
ATOM   4244 C CB  . ALA B 2 9   ? 158.736 165.478 108.326 1.00 65.76  ? 125 ALA D CB  1 
ATOM   4245 N N   . GLU B 2 10  ? 160.684 162.554 109.587 1.00 69.05  ? 126 GLU D N   1 
ATOM   4246 C CA  . GLU B 2 10  ? 162.038 162.040 109.739 1.00 70.19  ? 126 GLU D CA  1 
ATOM   4247 C C   . GLU B 2 10  ? 162.241 160.862 108.797 1.00 70.31  ? 126 GLU D C   1 
ATOM   4248 O O   . GLU B 2 10  ? 161.408 159.952 108.745 1.00 66.17  ? 126 GLU D O   1 
ATOM   4249 C CB  . GLU B 2 10  ? 162.309 161.616 111.185 1.00 64.34  ? 126 GLU D CB  1 
ATOM   4250 C CG  . GLU B 2 10  ? 161.927 162.662 112.219 1.00 67.53  ? 126 GLU D CG  1 
ATOM   4251 C CD  . GLU B 2 10  ? 163.134 163.276 112.899 1.00 71.45  ? 126 GLU D CD  1 
ATOM   4252 O OE1 . GLU B 2 10  ? 164.258 162.776 112.682 1.00 72.23  ? 126 GLU D OE1 1 
ATOM   4253 O OE2 . GLU B 2 10  ? 162.960 164.258 113.651 1.00 62.00  ? 126 GLU D OE2 1 
ATOM   4254 N N   . VAL B 2 11  ? 163.342 160.889 108.050 1.00 77.40  ? 127 VAL D N   1 
ATOM   4255 C CA  . VAL B 2 11  ? 163.730 159.796 107.166 1.00 81.09  ? 127 VAL D CA  1 
ATOM   4256 C C   . VAL B 2 11  ? 165.177 159.435 107.472 1.00 82.06  ? 127 VAL D C   1 
ATOM   4257 O O   . VAL B 2 11  ? 166.043 160.316 107.529 1.00 76.48  ? 127 VAL D O   1 
ATOM   4258 C CB  . VAL B 2 11  ? 163.550 160.165 105.680 1.00 77.44  ? 127 VAL D CB  1 
ATOM   4259 C CG1 . VAL B 2 11  ? 164.118 161.549 105.392 1.00 76.31  ? 127 VAL D CG1 1 
ATOM   4260 C CG2 . VAL B 2 11  ? 164.196 159.116 104.786 1.00 76.96  ? 127 VAL D CG2 1 
ATOM   4261 N N   . LYS B 2 12  ? 165.436 158.145 107.681 1.00 80.67  ? 128 LYS D N   1 
ATOM   4262 C CA  . LYS B 2 12  ? 166.761 157.700 108.093 1.00 79.42  ? 128 LYS D CA  1 
ATOM   4263 C C   . LYS B 2 12  ? 167.256 156.541 107.238 1.00 83.86  ? 128 LYS D C   1 
ATOM   4264 O O   . LYS B 2 12  ? 166.641 156.199 106.223 1.00 84.32  ? 128 LYS D O   1 
ATOM   4265 C CB  . LYS B 2 12  ? 166.747 157.294 109.569 1.00 73.05  ? 128 LYS D CB  1 
ATOM   4266 C CG  . LYS B 2 12  ? 166.788 158.459 110.543 1.00 75.00  ? 128 LYS D CG  1 
ATOM   4267 C CD  . LYS B 2 12  ? 167.834 159.485 110.139 1.00 79.18  ? 128 LYS D CD  1 
ATOM   4268 C CE  . LYS B 2 12  ? 168.209 160.380 111.307 1.00 76.40  ? 128 LYS D CE  1 
ATOM   4269 N NZ  . LYS B 2 12  ? 169.467 159.933 111.965 1.00 74.01  ? 128 LYS D NZ  1 
ATOM   4270 N N   . LYS B 2 13  ? 168.365 155.933 107.647 1.00 84.22  ? 129 LYS D N   1 
ATOM   4271 C CA  . LYS B 2 13  ? 168.954 154.780 106.988 1.00 83.58  ? 129 LYS D CA  1 
ATOM   4272 C C   . LYS B 2 13  ? 169.150 153.663 108.001 1.00 84.69  ? 129 LYS D C   1 
ATOM   4273 O O   . LYS B 2 13  ? 169.265 153.926 109.202 1.00 85.18  ? 129 LYS D O   1 
ATOM   4274 C CB  . LYS B 2 13  ? 170.302 155.139 106.343 1.00 84.04  ? 129 LYS D CB  1 
ATOM   4275 C CG  . LYS B 2 13  ? 170.292 156.451 105.576 1.00 83.66  ? 129 LYS D CG  1 
ATOM   4276 C CD  . LYS B 2 13  ? 169.536 156.314 104.264 1.00 83.32  ? 129 LYS D CD  1 
ATOM   4277 C CE  . LYS B 2 13  ? 168.649 157.521 104.007 1.00 80.62  ? 129 LYS D CE  1 
ATOM   4278 N NZ  . LYS B 2 13  ? 167.386 157.143 103.315 1.00 69.55  ? 129 LYS D NZ  1 
ATOM   4279 N N   . PRO B 2 14  ? 169.170 152.407 107.551 1.00 88.97  ? 130 PRO D N   1 
ATOM   4280 C CA  . PRO B 2 14  ? 169.349 151.295 108.493 1.00 90.98  ? 130 PRO D CA  1 
ATOM   4281 C C   . PRO B 2 14  ? 170.677 151.396 109.230 1.00 89.69  ? 130 PRO D C   1 
ATOM   4282 O O   . PRO B 2 14  ? 171.694 151.804 108.666 1.00 90.73  ? 130 PRO D O   1 
ATOM   4283 C CB  . PRO B 2 14  ? 169.296 150.055 107.593 1.00 85.46  ? 130 PRO D CB  1 
ATOM   4284 C CG  . PRO B 2 14  ? 168.541 150.495 106.388 1.00 90.27  ? 130 PRO D CG  1 
ATOM   4285 C CD  . PRO B 2 14  ? 168.912 151.932 106.182 1.00 88.57  ? 130 PRO D CD  1 
ATOM   4286 N N   . GLY B 2 15  ? 170.655 151.016 110.505 1.00 84.83  ? 131 GLY D N   1 
ATOM   4287 C CA  . GLY B 2 15  ? 171.839 151.087 111.335 1.00 77.79  ? 131 GLY D CA  1 
ATOM   4288 C C   . GLY B 2 15  ? 172.165 152.460 111.874 1.00 80.28  ? 131 GLY D C   1 
ATOM   4289 O O   . GLY B 2 15  ? 173.226 152.630 112.485 1.00 78.98  ? 131 GLY D O   1 
ATOM   4290 N N   . ALA B 2 16  ? 171.295 153.444 111.670 1.00 82.07  ? 132 ALA D N   1 
ATOM   4291 C CA  . ALA B 2 16  ? 171.521 154.799 112.139 1.00 81.15  ? 132 ALA D CA  1 
ATOM   4292 C C   . ALA B 2 16  ? 170.715 155.051 113.412 1.00 82.07  ? 132 ALA D C   1 
ATOM   4293 O O   . ALA B 2 16  ? 170.070 154.150 113.958 1.00 84.22  ? 132 ALA D O   1 
ATOM   4294 C CB  . ALA B 2 16  ? 171.171 155.801 111.037 1.00 72.41  ? 132 ALA D CB  1 
ATOM   4295 N N   . SER B 2 17  ? 170.752 156.290 113.895 1.00 77.03  ? 133 SER D N   1 
ATOM   4296 C CA  . SER B 2 17  ? 170.046 156.689 115.103 1.00 73.86  ? 133 SER D CA  1 
ATOM   4297 C C   . SER B 2 17  ? 169.144 157.875 114.799 1.00 75.35  ? 133 SER D C   1 
ATOM   4298 O O   . SER B 2 17  ? 169.536 158.794 114.074 1.00 79.69  ? 133 SER D O   1 
ATOM   4299 C CB  . SER B 2 17  ? 171.025 157.055 116.226 1.00 71.77  ? 133 SER D CB  1 
ATOM   4300 O OG  . SER B 2 17  ? 170.484 156.743 117.497 1.00 73.79  ? 133 SER D OG  1 
ATOM   4301 N N   . VAL B 2 18  ? 167.937 157.849 115.358 1.00 69.78  ? 134 VAL D N   1 
ATOM   4302 C CA  . VAL B 2 18  ? 166.973 158.931 115.200 1.00 68.82  ? 134 VAL D CA  1 
ATOM   4303 C C   . VAL B 2 18  ? 166.512 159.379 116.580 1.00 63.81  ? 134 VAL D C   1 
ATOM   4304 O O   . VAL B 2 18  ? 166.286 158.554 117.473 1.00 62.75  ? 134 VAL D O   1 
ATOM   4305 C CB  . VAL B 2 18  ? 165.776 158.515 114.314 1.00 75.64  ? 134 VAL D CB  1 
ATOM   4306 C CG1 . VAL B 2 18  ? 164.888 157.494 115.016 1.00 68.00  ? 134 VAL D CG1 1 
ATOM   4307 C CG2 . VAL B 2 18  ? 164.970 159.738 113.903 1.00 67.39  ? 134 VAL D CG2 1 
ATOM   4308 N N   . LYS B 2 19  ? 166.416 160.693 116.765 1.00 57.51  ? 135 LYS D N   1 
ATOM   4309 C CA  . LYS B 2 19  ? 165.955 161.284 118.013 1.00 49.65  ? 135 LYS D CA  1 
ATOM   4310 C C   . LYS B 2 19  ? 164.885 162.315 117.694 1.00 55.70  ? 135 LYS D C   1 
ATOM   4311 O O   . LYS B 2 19  ? 165.129 163.245 116.919 1.00 64.99  ? 135 LYS D O   1 
ATOM   4312 C CB  . LYS B 2 19  ? 167.113 161.930 118.782 1.00 51.10  ? 135 LYS D CB  1 
ATOM   4313 C CG  . LYS B 2 19  ? 166.691 162.730 120.003 1.00 48.73  ? 135 LYS D CG  1 
ATOM   4314 C CD  . LYS B 2 19  ? 167.905 163.239 120.766 1.00 53.06  ? 135 LYS D CD  1 
ATOM   4315 C CE  . LYS B 2 19  ? 167.711 163.121 122.269 1.00 49.20  ? 135 LYS D CE  1 
ATOM   4316 N NZ  . LYS B 2 19  ? 167.970 161.742 122.765 1.00 45.74  ? 135 LYS D NZ  1 
ATOM   4317 N N   . VAL B 2 20  ? 163.708 162.152 118.291 1.00 53.42  ? 136 VAL D N   1 
ATOM   4318 C CA  . VAL B 2 20  ? 162.567 163.019 118.031 1.00 51.99  ? 136 VAL D CA  1 
ATOM   4319 C C   . VAL B 2 20  ? 162.131 163.664 119.339 1.00 40.21  ? 136 VAL D C   1 
ATOM   4320 O O   . VAL B 2 20  ? 162.243 163.060 120.412 1.00 35.75  ? 136 VAL D O   1 
ATOM   4321 C CB  . VAL B 2 20  ? 161.401 162.253 117.368 1.00 51.71  ? 136 VAL D CB  1 
ATOM   4322 C CG1 . VAL B 2 20  ? 161.911 161.420 116.203 1.00 54.73  ? 136 VAL D CG1 1 
ATOM   4323 C CG2 . VAL B 2 20  ? 160.692 161.365 118.372 1.00 45.17  ? 136 VAL D CG2 1 
ATOM   4324 N N   . SER B 2 21  ? 161.663 164.904 119.249 1.00 40.70  ? 137 SER D N   1 
ATOM   4325 C CA  . SER B 2 21  ? 161.280 165.684 120.413 1.00 46.51  ? 137 SER D CA  1 
ATOM   4326 C C   . SER B 2 21  ? 159.769 165.635 120.625 1.00 40.40  ? 137 SER D C   1 
ATOM   4327 O O   . SER B 2 21  ? 159.011 165.140 119.790 1.00 38.72  ? 137 SER D O   1 
ATOM   4328 C CB  . SER B 2 21  ? 161.747 167.131 120.257 1.00 51.50  ? 137 SER D CB  1 
ATOM   4329 O OG  . SER B 2 21  ? 161.065 167.776 119.195 1.00 50.39  ? 137 SER D OG  1 
ATOM   4330 N N   . CYS B 2 22  ? 159.335 166.158 121.774 1.00 36.06  ? 138 CYS D N   1 
ATOM   4331 C CA  . CYS B 2 22  ? 157.911 166.289 122.092 1.00 33.38  ? 138 CYS D CA  1 
ATOM   4332 C C   . CYS B 2 22  ? 157.727 167.561 122.917 1.00 40.34  ? 138 CYS D C   1 
ATOM   4333 O O   . CYS B 2 22  ? 157.859 167.543 124.143 1.00 46.77  ? 138 CYS D O   1 
ATOM   4334 C CB  . CYS B 2 22  ? 157.386 165.067 122.829 1.00 32.26  ? 138 CYS D CB  1 
ATOM   4335 S SG  . CYS B 2 22  ? 155.626 165.167 123.207 1.00 37.59  ? 138 CYS D SG  1 
ATOM   4336 N N   . LYS B 2 23  ? 157.406 168.659 122.238 1.00 38.22  ? 139 LYS D N   1 
ATOM   4337 C CA  . LYS B 2 23  ? 157.161 169.934 122.906 1.00 36.68  ? 139 LYS D CA  1 
ATOM   4338 C C   . LYS B 2 23  ? 155.787 169.885 123.560 1.00 36.86  ? 139 LYS D C   1 
ATOM   4339 O O   . LYS B 2 23  ? 154.759 170.002 122.890 1.00 37.79  ? 139 LYS D O   1 
ATOM   4340 C CB  . LYS B 2 23  ? 157.261 171.085 121.911 1.00 42.64  ? 139 LYS D CB  1 
ATOM   4341 C CG  . LYS B 2 23  ? 156.841 172.436 122.473 1.00 46.30  ? 139 LYS D CG  1 
ATOM   4342 C CD  . LYS B 2 23  ? 157.986 173.109 123.209 1.00 41.24  ? 139 LYS D CD  1 
ATOM   4343 C CE  . LYS B 2 23  ? 157.488 174.248 124.083 1.00 39.20  ? 139 LYS D CE  1 
ATOM   4344 N NZ  . LYS B 2 23  ? 156.920 173.756 125.368 1.00 40.76  ? 139 LYS D NZ  1 
ATOM   4345 N N   . ALA B 2 24  ? 155.764 169.707 124.877 1.00 35.20  ? 140 ALA D N   1 
ATOM   4346 C CA  . ALA B 2 24  ? 154.524 169.612 125.636 1.00 40.98  ? 140 ALA D CA  1 
ATOM   4347 C C   . ALA B 2 24  ? 154.228 170.960 126.279 1.00 45.73  ? 140 ALA D C   1 
ATOM   4348 O O   . ALA B 2 24  ? 155.048 171.483 127.041 1.00 45.24  ? 140 ALA D O   1 
ATOM   4349 C CB  . ALA B 2 24  ? 154.619 168.518 126.697 1.00 34.26  ? 140 ALA D CB  1 
ATOM   4350 N N   . SER B 2 25  ? 153.057 171.514 125.976 1.00 38.19  ? 141 SER D N   1 
ATOM   4351 C CA  . SER B 2 25  ? 152.649 172.815 126.480 1.00 39.47  ? 141 SER D CA  1 
ATOM   4352 C C   . SER B 2 25  ? 151.235 172.725 127.037 1.00 37.71  ? 141 SER D C   1 
ATOM   4353 O O   . SER B 2 25  ? 150.535 171.724 126.866 1.00 40.70  ? 141 SER D O   1 
ATOM   4354 C CB  . SER B 2 25  ? 152.725 173.887 125.384 1.00 49.14  ? 141 SER D CB  1 
ATOM   4355 O OG  . SER B 2 25  ? 151.839 173.590 124.320 1.00 48.97  ? 141 SER D OG  1 
ATOM   4356 N N   . GLY B 2 26  ? 150.819 173.793 127.714 1.00 35.14  ? 142 GLY D N   1 
ATOM   4357 C CA  . GLY B 2 26  ? 149.497 173.865 128.296 1.00 30.20  ? 142 GLY D CA  1 
ATOM   4358 C C   . GLY B 2 26  ? 149.347 173.197 129.644 1.00 31.02  ? 142 GLY D C   1 
ATOM   4359 O O   . GLY B 2 26  ? 148.240 173.206 130.199 1.00 33.89  ? 142 GLY D O   1 
ATOM   4360 N N   . TYR B 2 27  ? 150.415 172.624 130.190 1.00 25.09  ? 143 TYR D N   1 
ATOM   4361 C CA  . TYR B 2 27  ? 150.351 171.943 131.476 1.00 25.43  ? 143 TYR D CA  1 
ATOM   4362 C C   . TYR B 2 27  ? 151.761 171.838 132.036 1.00 26.40  ? 143 TYR D C   1 
ATOM   4363 O O   . TYR B 2 27  ? 152.749 172.039 131.326 1.00 27.66  ? 143 TYR D O   1 
ATOM   4364 C CB  . TYR B 2 27  ? 149.705 170.561 131.343 1.00 27.19  ? 143 TYR D CB  1 
ATOM   4365 C CG  . TYR B 2 27  ? 150.584 169.540 130.657 1.00 24.32  ? 143 TYR D CG  1 
ATOM   4366 C CD1 . TYR B 2 27  ? 150.749 169.549 129.280 1.00 24.99  ? 143 TYR D CD1 1 
ATOM   4367 C CD2 . TYR B 2 27  ? 151.248 168.569 131.387 1.00 21.13  ? 143 TYR D CD2 1 
ATOM   4368 C CE1 . TYR B 2 27  ? 151.552 168.617 128.652 1.00 20.42  ? 143 TYR D CE1 1 
ATOM   4369 C CE2 . TYR B 2 27  ? 152.051 167.636 130.770 1.00 22.80  ? 143 TYR D CE2 1 
ATOM   4370 C CZ  . TYR B 2 27  ? 152.200 167.664 129.404 1.00 23.73  ? 143 TYR D CZ  1 
ATOM   4371 O OH  . TYR B 2 27  ? 153.001 166.731 128.791 1.00 30.87  ? 143 TYR D OH  1 
ATOM   4372 N N   . THR B 2 28  ? 151.864 171.440 133.311 1.00 29.03  ? 144 THR D N   1 
ATOM   4373 C CA  . THR B 2 28  ? 153.195 171.219 133.930 1.00 32.49  ? 144 THR D CA  1 
ATOM   4374 C C   . THR B 2 28  ? 153.800 169.961 133.340 1.00 30.12  ? 144 THR D C   1 
ATOM   4375 O O   . THR B 2 28  ? 153.337 168.859 133.703 1.00 27.61  ? 144 THR D O   1 
ATOM   4376 C CB  . THR B 2 28  ? 153.054 171.142 135.448 1.00 29.66  ? 144 THR D CB  1 
ATOM   4377 O OG1 . THR B 2 28  ? 154.171 170.376 135.888 1.00 26.89  ? 144 THR D OG1 1 
ATOM   4378 C CG2 . THR B 2 28  ? 151.759 170.478 135.882 1.00 26.13  ? 144 THR D CG2 1 
ATOM   4379 N N   . PHE B 2 29  ? 154.817 170.101 132.488 1.00 26.35  ? 145 PHE D N   1 
ATOM   4380 C CA  . PHE B 2 29  ? 155.393 168.933 131.766 1.00 23.05  ? 145 PHE D CA  1 
ATOM   4381 C C   . PHE B 2 29  ? 156.020 167.926 132.720 1.00 25.31  ? 145 PHE D C   1 
ATOM   4382 O O   . PHE B 2 29  ? 156.121 166.750 132.325 1.00 32.24  ? 145 PHE D O   1 
ATOM   4383 C CB  . PHE B 2 29  ? 156.376 169.524 130.751 1.00 29.72  ? 145 PHE D CB  1 
ATOM   4384 C CG  . PHE B 2 29  ? 157.473 168.611 130.219 1.00 34.90  ? 145 PHE D CG  1 
ATOM   4385 C CD1 . PHE B 2 29  ? 157.238 167.762 129.145 1.00 35.06  ? 145 PHE D CD1 1 
ATOM   4386 C CD2 . PHE B 2 29  ? 158.752 168.644 130.764 1.00 33.37  ? 145 PHE D CD2 1 
ATOM   4387 C CE1 . PHE B 2 29  ? 158.244 166.946 128.654 1.00 32.28  ? 145 PHE D CE1 1 
ATOM   4388 C CE2 . PHE B 2 29  ? 159.756 167.831 130.264 1.00 31.22  ? 145 PHE D CE2 1 
ATOM   4389 C CZ  . PHE B 2 29  ? 159.500 166.983 129.214 1.00 30.62  ? 145 PHE D CZ  1 
ATOM   4390 N N   . THR B 2 30  ? 156.404 168.340 133.928 1.00 25.25  ? 146 THR D N   1 
ATOM   4391 C CA  . THR B 2 30  ? 157.131 167.424 134.840 1.00 24.16  ? 146 THR D CA  1 
ATOM   4392 C C   . THR B 2 30  ? 156.178 166.650 135.723 1.00 18.95  ? 146 THR D C   1 
ATOM   4393 O O   . THR B 2 30  ? 156.669 165.824 136.514 1.00 18.56  ? 146 THR D O   1 
ATOM   4394 C CB  . THR B 2 30  ? 158.123 168.237 135.668 1.00 29.92  ? 146 THR D CB  1 
ATOM   4395 O OG1 . THR B 2 30  ? 157.325 169.171 136.387 1.00 36.32  ? 146 THR D OG1 1 
ATOM   4396 C CG2 . THR B 2 30  ? 159.131 168.967 134.800 1.00 30.54  ? 146 THR D CG2 1 
ATOM   4397 N N   . SER B 2 31  ? 154.872 166.887 135.604 1.00 18.44  ? 147 SER D N   1 
ATOM   4398 C CA  . SER B 2 31  ? 153.893 166.232 136.510 1.00 14.88  ? 147 SER D CA  1 
ATOM   4399 C C   . SER B 2 31  ? 153.183 165.076 135.798 1.00 15.04  ? 147 SER D C   1 
ATOM   4400 O O   . SER B 2 31  ? 152.230 164.528 136.385 1.00 13.85  ? 147 SER D O   1 
ATOM   4401 C CB  . SER B 2 31  ? 152.897 167.233 137.018 1.00 14.99  ? 147 SER D CB  1 
ATOM   4402 O OG  . SER B 2 31  ? 151.837 166.590 137.709 1.00 17.11  ? 147 SER D OG  1 
ATOM   4403 N N   . TYR B 2 32  ? 153.630 164.712 134.594 1.00 16.49  ? 148 TYR D N   1 
ATOM   4404 C CA  . TYR B 2 32  ? 152.907 163.676 133.812 1.00 15.28  ? 148 TYR D CA  1 
ATOM   4405 C C   . TYR B 2 32  ? 153.875 162.783 133.069 1.00 15.07  ? 148 TYR D C   1 
ATOM   4406 O O   . TYR B 2 32  ? 154.840 163.312 132.484 1.00 15.39  ? 148 TYR D O   1 
ATOM   4407 C CB  . TYR B 2 32  ? 152.029 164.366 132.766 1.00 13.72  ? 148 TYR D CB  1 
ATOM   4408 C CG  . TYR B 2 32  ? 150.776 165.057 133.284 1.00 14.17  ? 148 TYR D CG  1 
ATOM   4409 C CD1 . TYR B 2 32  ? 150.810 166.376 133.717 1.00 12.99  ? 148 TYR D CD1 1 
ATOM   4410 C CD2 . TYR B 2 32  ? 149.557 164.395 133.316 1.00 13.78  ? 148 TYR D CD2 1 
ATOM   4411 C CE1 . TYR B 2 32  ? 149.672 167.013 134.179 1.00 13.11  ? 148 TYR D CE1 1 
ATOM   4412 C CE2 . TYR B 2 32  ? 148.411 165.021 133.776 1.00 12.67  ? 148 TYR D CE2 1 
ATOM   4413 C CZ  . TYR B 2 32  ? 148.469 166.333 134.209 1.00 12.13  ? 148 TYR D CZ  1 
ATOM   4414 O OH  . TYR B 2 32  ? 147.344 166.956 134.665 1.00 12.18  ? 148 TYR D OH  1 
ATOM   4415 N N   . TRP B 2 33  ? 153.628 161.470 133.072 1.00 14.95  ? 149 TRP D N   1 
ATOM   4416 C CA  . TRP B 2 33  ? 154.443 160.559 132.279 1.00 8.13   ? 149 TRP D CA  1 
ATOM   4417 C C   . TRP B 2 33  ? 154.356 160.935 130.808 1.00 7.61   ? 149 TRP D C   1 
ATOM   4418 O O   . TRP B 2 33  ? 153.304 161.353 130.318 1.00 13.50  ? 149 TRP D O   1 
ATOM   4419 C CB  . TRP B 2 33  ? 153.979 159.115 132.468 1.00 6.58   ? 149 TRP D CB  1 
ATOM   4420 C CG  . TRP B 2 33  ? 154.331 158.506 133.785 1.00 6.93   ? 149 TRP D CG  1 
ATOM   4421 C CD1 . TRP B 2 33  ? 153.517 158.378 134.869 1.00 8.35   ? 149 TRP D CD1 1 
ATOM   4422 C CD2 . TRP B 2 33  ? 155.582 157.912 134.151 1.00 7.75   ? 149 TRP D CD2 1 
ATOM   4423 N NE1 . TRP B 2 33  ? 154.186 157.754 135.894 1.00 10.53  ? 149 TRP D NE1 1 
ATOM   4424 C CE2 . TRP B 2 33  ? 155.456 157.458 135.477 1.00 6.97   ? 149 TRP D CE2 1 
ATOM   4425 C CE3 . TRP B 2 33  ? 156.798 157.728 133.488 1.00 9.92   ? 149 TRP D CE3 1 
ATOM   4426 C CZ2 . TRP B 2 33  ? 156.499 156.830 136.152 1.00 6.38   ? 149 TRP D CZ2 1 
ATOM   4427 C CZ3 . TRP B 2 33  ? 157.832 157.105 134.161 1.00 10.53  ? 149 TRP D CZ3 1 
ATOM   4428 C CH2 . TRP B 2 33  ? 157.676 156.664 135.479 1.00 8.80   ? 149 TRP D CH2 1 
ATOM   4429 N N   . MET B 2 34  ? 155.468 160.788 130.100 1.00 6.47   ? 150 MET D N   1 
ATOM   4430 C CA  . MET B 2 34  ? 155.518 161.040 128.663 1.00 7.70   ? 150 MET D CA  1 
ATOM   4431 C C   . MET B 2 34  ? 155.779 159.705 127.973 1.00 7.99   ? 150 MET D C   1 
ATOM   4432 O O   . MET B 2 34  ? 156.925 159.312 127.752 1.00 10.49  ? 150 MET D O   1 
ATOM   4433 C CB  . MET B 2 34  ? 156.578 162.074 128.312 1.00 14.50  ? 150 MET D CB  1 
ATOM   4434 C CG  . MET B 2 34  ? 156.660 162.374 126.826 1.00 17.92  ? 150 MET D CG  1 
ATOM   4435 S SD  . MET B 2 34  ? 155.286 163.376 126.233 1.00 27.84  ? 150 MET D SD  1 
ATOM   4436 C CE  . MET B 2 34  ? 155.015 164.462 127.629 1.00 19.68  ? 150 MET D CE  1 
ATOM   4437 N N   . HIS B 2 35  ? 154.699 159.006 127.643 1.00 7.30   ? 151 HIS D N   1 
ATOM   4438 C CA  . HIS B 2 35  ? 154.797 157.724 126.971 1.00 7.09   ? 151 HIS D CA  1 
ATOM   4439 C C   . HIS B 2 35  ? 155.159 157.912 125.503 1.00 8.49   ? 151 HIS D C   1 
ATOM   4440 O O   . HIS B 2 35  ? 154.899 158.953 124.898 1.00 10.43  ? 151 HIS D O   1 
ATOM   4441 C CB  . HIS B 2 35  ? 153.483 156.959 127.087 1.00 6.75   ? 151 HIS D CB  1 
ATOM   4442 C CG  . HIS B 2 35  ? 153.153 156.542 128.484 1.00 5.43   ? 151 HIS D CG  1 
ATOM   4443 N ND1 . HIS B 2 35  ? 153.069 155.221 128.864 1.00 7.88   ? 151 HIS D ND1 1 
ATOM   4444 C CD2 . HIS B 2 35  ? 152.888 157.271 129.592 1.00 7.13   ? 151 HIS D CD2 1 
ATOM   4445 C CE1 . HIS B 2 35  ? 152.765 155.154 130.147 1.00 9.48   ? 151 HIS D CE1 1 
ATOM   4446 N NE2 . HIS B 2 35  ? 152.652 156.384 130.613 1.00 10.03  ? 151 HIS D NE2 1 
ATOM   4447 N N   . TRP B 2 36  ? 155.773 156.880 124.934 1.00 8.44   ? 152 TRP D N   1 
ATOM   4448 C CA  . TRP B 2 36  ? 156.096 156.851 123.516 1.00 8.08   ? 152 TRP D CA  1 
ATOM   4449 C C   . TRP B 2 36  ? 155.502 155.591 122.910 1.00 10.75  ? 152 TRP D C   1 
ATOM   4450 O O   . TRP B 2 36  ? 155.742 154.487 123.407 1.00 19.42  ? 152 TRP D O   1 
ATOM   4451 C CB  . TRP B 2 36  ? 157.609 156.911 123.291 1.00 10.24  ? 152 TRP D CB  1 
ATOM   4452 C CG  . TRP B 2 36  ? 158.173 158.279 123.521 1.00 13.78  ? 152 TRP D CG  1 
ATOM   4453 C CD1 . TRP B 2 36  ? 158.700 158.764 124.681 1.00 11.60  ? 152 TRP D CD1 1 
ATOM   4454 C CD2 . TRP B 2 36  ? 158.241 159.349 122.571 1.00 16.22  ? 152 TRP D CD2 1 
ATOM   4455 N NE1 . TRP B 2 36  ? 159.103 160.066 124.510 1.00 13.27  ? 152 TRP D NE1 1 
ATOM   4456 C CE2 . TRP B 2 36  ? 158.830 160.448 123.223 1.00 15.65  ? 152 TRP D CE2 1 
ATOM   4457 C CE3 . TRP B 2 36  ? 157.864 159.482 121.232 1.00 15.71  ? 152 TRP D CE3 1 
ATOM   4458 C CZ2 . TRP B 2 36  ? 159.052 161.663 122.582 1.00 18.37  ? 152 TRP D CZ2 1 
ATOM   4459 C CZ3 . TRP B 2 36  ? 158.085 160.688 120.598 1.00 17.55  ? 152 TRP D CZ3 1 
ATOM   4460 C CH2 . TRP B 2 36  ? 158.674 161.762 121.272 1.00 16.60  ? 152 TRP D CH2 1 
ATOM   4461 N N   . VAL B 2 37  ? 154.717 155.761 121.850 1.00 10.11  ? 153 VAL D N   1 
ATOM   4462 C CA  . VAL B 2 37  ? 153.992 154.670 121.212 1.00 10.77  ? 153 VAL D CA  1 
ATOM   4463 C C   . VAL B 2 37  ? 154.288 154.702 119.721 1.00 14.23  ? 153 VAL D C   1 
ATOM   4464 O O   . VAL B 2 37  ? 154.286 155.771 119.102 1.00 24.21  ? 153 VAL D O   1 
ATOM   4465 C CB  . VAL B 2 37  ? 152.473 154.773 121.471 1.00 8.78   ? 153 VAL D CB  1 
ATOM   4466 C CG1 . VAL B 2 37  ? 151.724 153.678 120.734 1.00 10.60  ? 153 VAL D CG1 1 
ATOM   4467 C CG2 . VAL B 2 37  ? 152.179 154.712 122.963 1.00 8.89   ? 153 VAL D CG2 1 
ATOM   4468 N N   . ARG B 2 38  ? 154.550 153.533 119.145 1.00 11.70  ? 154 ARG D N   1 
ATOM   4469 C CA  . ARG B 2 38  ? 154.834 153.405 117.724 1.00 13.32  ? 154 ARG D CA  1 
ATOM   4470 C C   . ARG B 2 38  ? 153.712 152.644 117.030 1.00 20.35  ? 154 ARG D C   1 
ATOM   4471 O O   . ARG B 2 38  ? 153.068 151.773 117.622 1.00 20.71  ? 154 ARG D O   1 
ATOM   4472 C CB  . ARG B 2 38  ? 156.171 152.695 117.487 1.00 17.80  ? 154 ARG D CB  1 
ATOM   4473 C CG  . ARG B 2 38  ? 156.194 151.243 117.928 1.00 25.83  ? 154 ARG D CG  1 
ATOM   4474 C CD  . ARG B 2 38  ? 157.029 150.391 116.989 1.00 29.75  ? 154 ARG D CD  1 
ATOM   4475 N NE  . ARG B 2 38  ? 158.266 151.056 116.601 1.00 32.88  ? 154 ARG D NE  1 
ATOM   4476 C CZ  . ARG B 2 38  ? 159.304 150.442 116.049 1.00 36.79  ? 154 ARG D CZ  1 
ATOM   4477 N NH1 . ARG B 2 38  ? 159.286 149.143 115.802 1.00 36.27  ? 154 ARG D NH1 1 
ATOM   4478 N NH2 . ARG B 2 38  ? 160.386 151.149 115.739 1.00 41.12  ? 154 ARG D NH2 1 
ATOM   4479 N N   . GLN B 2 39  ? 153.478 152.990 115.764 1.00 23.14  ? 155 GLN D N   1 
ATOM   4480 C CA  . GLN B 2 39  ? 152.444 152.362 114.939 1.00 24.49  ? 155 GLN D CA  1 
ATOM   4481 C C   . GLN B 2 39  ? 153.079 151.963 113.610 1.00 33.38  ? 155 GLN D C   1 
ATOM   4482 O O   . GLN B 2 39  ? 153.049 152.729 112.644 1.00 38.01  ? 155 GLN D O   1 
ATOM   4483 C CB  . GLN B 2 39  ? 151.261 153.301 114.737 1.00 25.04  ? 155 GLN D CB  1 
ATOM   4484 C CG  . GLN B 2 39  ? 149.976 152.601 114.330 1.00 29.25  ? 155 GLN D CG  1 
ATOM   4485 C CD  . GLN B 2 39  ? 149.028 153.515 113.583 1.00 27.54  ? 155 GLN D CD  1 
ATOM   4486 O OE1 . GLN B 2 39  ? 147.888 153.148 113.301 1.00 33.12  ? 155 GLN D OE1 1 
ATOM   4487 N NE2 . GLN B 2 39  ? 149.496 154.713 113.257 1.00 20.13  ? 155 GLN D NE2 1 
ATOM   4488 N N   . ALA B 2 40  ? 153.651 150.765 113.565 1.00 35.41  ? 156 ALA D N   1 
ATOM   4489 C CA  . ALA B 2 40  ? 154.255 150.283 112.334 1.00 41.60  ? 156 ALA D CA  1 
ATOM   4490 C C   . ALA B 2 40  ? 153.170 149.946 111.314 1.00 51.08  ? 156 ALA D C   1 
ATOM   4491 O O   . ALA B 2 40  ? 152.098 149.460 111.686 1.00 53.46  ? 156 ALA D O   1 
ATOM   4492 C CB  . ALA B 2 40  ? 155.120 149.054 112.604 1.00 44.45  ? 156 ALA D CB  1 
ATOM   4493 N N   . PRO B 2 41  ? 153.408 150.207 110.028 1.00 53.25  ? 157 PRO D N   1 
ATOM   4494 C CA  . PRO B 2 41  ? 152.433 149.808 109.007 1.00 59.02  ? 157 PRO D CA  1 
ATOM   4495 C C   . PRO B 2 41  ? 152.215 148.302 109.021 1.00 60.67  ? 157 PRO D C   1 
ATOM   4496 O O   . PRO B 2 41  ? 153.154 147.520 109.177 1.00 52.97  ? 157 PRO D O   1 
ATOM   4497 C CB  . PRO B 2 41  ? 153.079 150.274 107.697 1.00 61.39  ? 157 PRO D CB  1 
ATOM   4498 C CG  . PRO B 2 41  ? 154.022 151.360 108.106 1.00 55.34  ? 157 PRO D CG  1 
ATOM   4499 C CD  . PRO B 2 41  ? 154.537 150.957 109.454 1.00 49.44  ? 157 PRO D CD  1 
ATOM   4500 N N   . GLY B 2 42  ? 150.957 147.901 108.858 1.00 62.59  ? 158 GLY D N   1 
ATOM   4501 C CA  . GLY B 2 42  ? 150.589 146.506 108.956 1.00 61.12  ? 158 GLY D CA  1 
ATOM   4502 C C   . GLY B 2 42  ? 150.449 145.984 110.368 1.00 60.00  ? 158 GLY D C   1 
ATOM   4503 O O   . GLY B 2 42  ? 150.169 144.791 110.544 1.00 60.87  ? 158 GLY D O   1 
ATOM   4504 N N   . GLN B 2 43  ? 150.635 146.832 111.377 1.00 61.43  ? 159 GLN D N   1 
ATOM   4505 C CA  . GLN B 2 43  ? 150.523 146.433 112.771 1.00 57.34  ? 159 GLN D CA  1 
ATOM   4506 C C   . GLN B 2 43  ? 149.822 147.536 113.549 1.00 52.43  ? 159 GLN D C   1 
ATOM   4507 O O   . GLN B 2 43  ? 149.742 148.685 113.106 1.00 48.86  ? 159 GLN D O   1 
ATOM   4508 C CB  . GLN B 2 43  ? 151.896 146.142 113.393 1.00 50.57  ? 159 GLN D CB  1 
ATOM   4509 C CG  . GLN B 2 43  ? 152.542 144.853 112.917 1.00 52.35  ? 159 GLN D CG  1 
ATOM   4510 C CD  . GLN B 2 43  ? 153.868 144.581 113.600 1.00 53.69  ? 159 GLN D CD  1 
ATOM   4511 O OE1 . GLN B 2 43  ? 154.562 145.506 114.023 1.00 52.72  ? 159 GLN D OE1 1 
ATOM   4512 N NE2 . GLN B 2 43  ? 154.226 143.308 113.712 1.00 48.71  ? 159 GLN D NE2 1 
ATOM   4513 N N   . GLY B 2 44  ? 149.330 147.159 114.726 1.00 47.18  ? 160 GLY D N   1 
ATOM   4514 C CA  . GLY B 2 44  ? 148.640 148.142 115.568 1.00 37.98  ? 160 GLY D CA  1 
ATOM   4515 C C   . GLY B 2 44  ? 149.633 148.938 116.375 1.00 30.96  ? 160 GLY D C   1 
ATOM   4516 O O   . GLY B 2 44  ? 150.848 148.705 116.223 1.00 40.01  ? 160 GLY D O   1 
ATOM   4517 N N   . LEU B 2 45  ? 149.133 149.840 117.208 1.00 22.68  ? 161 LEU D N   1 
ATOM   4518 C CA  . LEU B 2 45  ? 149.980 150.675 118.048 1.00 18.47  ? 161 LEU D CA  1 
ATOM   4519 C C   . LEU B 2 45  ? 150.784 149.809 119.009 1.00 19.67  ? 161 LEU D C   1 
ATOM   4520 O O   . LEU B 2 45  ? 150.283 148.816 119.543 1.00 23.60  ? 161 LEU D O   1 
ATOM   4521 C CB  . LEU B 2 45  ? 149.132 151.680 118.826 1.00 14.76  ? 161 LEU D CB  1 
ATOM   4522 C CG  . LEU B 2 45  ? 148.475 152.807 118.029 1.00 16.95  ? 161 LEU D CG  1 
ATOM   4523 C CD1 . LEU B 2 45  ? 147.236 153.299 118.750 1.00 14.72  ? 161 LEU D CD1 1 
ATOM   4524 C CD2 . LEU B 2 45  ? 149.451 153.947 117.801 1.00 16.96  ? 161 LEU D CD2 1 
ATOM   4525 N N   . GLU B 2 46  ? 152.042 150.184 119.225 1.00 16.10  ? 162 GLU D N   1 
ATOM   4526 C CA  . GLU B 2 46  ? 152.947 149.414 120.069 1.00 17.30  ? 162 GLU D CA  1 
ATOM   4527 C C   . GLU B 2 46  ? 153.663 150.353 121.027 1.00 18.52  ? 162 GLU D C   1 
ATOM   4528 O O   . GLU B 2 46  ? 154.330 151.297 120.592 1.00 23.24  ? 162 GLU D O   1 
ATOM   4529 C CB  . GLU B 2 46  ? 153.955 148.635 119.223 1.00 22.72  ? 162 GLU D CB  1 
ATOM   4530 C CG  . GLU B 2 46  ? 154.595 147.468 119.947 1.00 24.69  ? 162 GLU D CG  1 
ATOM   4531 C CD  . GLU B 2 46  ? 156.037 147.259 119.545 1.00 29.70  ? 162 GLU D CD  1 
ATOM   4532 O OE1 . GLU B 2 46  ? 156.340 147.365 118.338 1.00 27.09  ? 162 GLU D OE1 1 
ATOM   4533 O OE2 . GLU B 2 46  ? 156.866 146.988 120.436 1.00 34.59  ? 162 GLU D OE2 1 
ATOM   4534 N N   . TRP B 2 47  ? 153.522 150.091 122.322 1.00 16.67  ? 163 TRP D N   1 
ATOM   4535 C CA  . TRP B 2 47  ? 154.213 150.874 123.336 1.00 12.73  ? 163 TRP D CA  1 
ATOM   4536 C C   . TRP B 2 47  ? 155.709 150.595 123.287 1.00 13.06  ? 163 TRP D C   1 
ATOM   4537 O O   . TRP B 2 47  ? 156.137 149.452 123.100 1.00 23.89  ? 163 TRP D O   1 
ATOM   4538 C CB  . TRP B 2 47  ? 153.654 150.540 124.716 1.00 16.66  ? 163 TRP D CB  1 
ATOM   4539 C CG  . TRP B 2 47  ? 154.158 151.393 125.831 1.00 15.66  ? 163 TRP D CG  1 
ATOM   4540 C CD1 . TRP B 2 47  ? 153.809 152.683 126.098 1.00 11.90  ? 163 TRP D CD1 1 
ATOM   4541 C CD2 . TRP B 2 47  ? 155.086 151.008 126.852 1.00 18.69  ? 163 TRP D CD2 1 
ATOM   4542 N NE1 . TRP B 2 47  ? 154.469 153.130 127.216 1.00 14.39  ? 163 TRP D NE1 1 
ATOM   4543 C CE2 . TRP B 2 47  ? 155.259 152.120 127.698 1.00 15.99  ? 163 TRP D CE2 1 
ATOM   4544 C CE3 . TRP B 2 47  ? 155.793 149.834 127.129 1.00 20.97  ? 163 TRP D CE3 1 
ATOM   4545 C CZ2 . TRP B 2 47  ? 156.106 152.092 128.804 1.00 15.45  ? 163 TRP D CZ2 1 
ATOM   4546 C CZ3 . TRP B 2 47  ? 156.633 149.808 128.226 1.00 23.15  ? 163 TRP D CZ3 1 
ATOM   4547 C CH2 . TRP B 2 47  ? 156.784 150.930 129.049 1.00 18.59  ? 163 TRP D CH2 1 
ATOM   4548 N N   . MET B 2 48  ? 156.513 151.647 123.456 1.00 12.79  ? 164 MET D N   1 
ATOM   4549 C CA  . MET B 2 48  ? 157.962 151.516 123.372 1.00 17.67  ? 164 MET D CA  1 
ATOM   4550 C C   . MET B 2 48  ? 158.693 152.150 124.551 1.00 18.60  ? 164 MET D C   1 
ATOM   4551 O O   . MET B 2 48  ? 159.920 152.291 124.497 1.00 20.01  ? 164 MET D O   1 
ATOM   4552 C CB  . MET B 2 48  ? 158.478 152.112 122.057 1.00 15.16  ? 164 MET D CB  1 
ATOM   4553 C CG  . MET B 2 48  ? 158.480 153.628 122.011 1.00 15.48  ? 164 MET D CG  1 
ATOM   4554 S SD  . MET B 2 48  ? 159.166 154.288 120.480 1.00 22.67  ? 164 MET D SD  1 
ATOM   4555 C CE  . MET B 2 48  ? 160.069 152.870 119.866 1.00 28.63  ? 164 MET D CE  1 
ATOM   4556 N N   . GLY B 2 49  ? 157.987 152.522 125.615 1.00 16.41  ? 165 GLY D N   1 
ATOM   4557 C CA  . GLY B 2 49  ? 158.636 153.088 126.780 1.00 13.73  ? 165 GLY D CA  1 
ATOM   4558 C C   . GLY B 2 49  ? 158.172 154.489 127.117 1.00 11.23  ? 165 GLY D C   1 
ATOM   4559 O O   . GLY B 2 49  ? 157.707 155.221 126.239 1.00 16.09  ? 165 GLY D O   1 
ATOM   4560 N N   . ASN B 2 50  ? 158.293 154.876 128.386 1.00 11.76  ? 166 ASN D N   1 
ATOM   4561 C CA  . ASN B 2 50  ? 157.911 156.218 128.809 1.00 10.10  ? 166 ASN D CA  1 
ATOM   4562 C C   . ASN B 2 50  ? 159.030 156.894 129.590 1.00 14.07  ? 166 ASN D C   1 
ATOM   4563 O O   . ASN B 2 50  ? 160.128 156.344 129.719 1.00 19.09  ? 166 ASN D O   1 
ATOM   4564 C CB  . ASN B 2 50  ? 156.627 156.178 129.643 1.00 8.94   ? 166 ASN D CB  1 
ATOM   4565 C CG  . ASN B 2 50  ? 156.784 155.404 130.936 1.00 9.35   ? 166 ASN D CG  1 
ATOM   4566 O OD1 . ASN B 2 50  ? 157.863 154.919 131.265 1.00 15.06  ? 166 ASN D OD1 1 
ATOM   4567 N ND2 . ASN B 2 50  ? 155.695 155.289 131.682 1.00 8.42   ? 166 ASN D ND2 1 
ATOM   4568 N N   . ILE B 2 51  ? 158.757 158.084 130.120 1.00 13.33  ? 167 ILE D N   1 
ATOM   4569 C CA  . ILE B 2 51  ? 159.738 158.836 130.892 1.00 13.68  ? 167 ILE D CA  1 
ATOM   4570 C C   . ILE B 2 51  ? 158.993 159.734 131.867 1.00 11.77  ? 167 ILE D C   1 
ATOM   4571 O O   . ILE B 2 51  ? 157.898 160.222 131.577 1.00 16.19  ? 167 ILE D O   1 
ATOM   4572 C CB  . ILE B 2 51  ? 160.678 159.653 129.971 1.00 16.18  ? 167 ILE D CB  1 
ATOM   4573 C CG1 . ILE B 2 51  ? 161.737 160.390 130.790 1.00 19.29  ? 167 ILE D CG1 1 
ATOM   4574 C CG2 . ILE B 2 51  ? 159.885 160.630 129.118 1.00 12.43  ? 167 ILE D CG2 1 
ATOM   4575 C CD1 . ILE B 2 51  ? 162.846 160.971 129.958 1.00 25.84  ? 167 ILE D CD1 1 
ATOM   4576 N N   . TRP B 2 52  ? 159.563 159.925 133.061 1.00 11.93  ? 168 TRP D N   1 
ATOM   4577 C CA  . TRP B 2 52  ? 158.963 160.861 134.048 1.00 13.77  ? 168 TRP D CA  1 
ATOM   4578 C C   . TRP B 2 52  ? 159.791 162.140 134.071 1.00 20.60  ? 168 TRP D C   1 
ATOM   4579 O O   . TRP B 2 52  ? 160.859 162.143 134.711 1.00 25.81  ? 168 TRP D O   1 
ATOM   4580 C CB  . TRP B 2 52  ? 158.908 160.235 135.443 1.00 14.98  ? 168 TRP D CB  1 
ATOM   4581 C CG  . TRP B 2 52  ? 158.372 161.173 136.489 1.00 15.85  ? 168 TRP D CG  1 
ATOM   4582 C CD1 . TRP B 2 52  ? 159.086 161.897 137.397 1.00 23.14  ? 168 TRP D CD1 1 
ATOM   4583 C CD2 . TRP B 2 52  ? 156.987 161.512 136.705 1.00 12.25  ? 168 TRP D CD2 1 
ATOM   4584 N NE1 . TRP B 2 52  ? 158.245 162.645 138.176 1.00 25.88  ? 168 TRP D NE1 1 
ATOM   4585 C CE2 . TRP B 2 52  ? 156.954 162.434 137.772 1.00 20.09  ? 168 TRP D CE2 1 
ATOM   4586 C CE3 . TRP B 2 52  ? 155.784 161.124 136.108 1.00 9.52   ? 168 TRP D CE3 1 
ATOM   4587 C CZ2 . TRP B 2 52  ? 155.762 162.970 138.250 1.00 21.64  ? 168 TRP D CZ2 1 
ATOM   4588 C CZ3 . TRP B 2 52  ? 154.608 161.656 136.582 1.00 9.92   ? 168 TRP D CZ3 1 
ATOM   4589 C CH2 . TRP B 2 52  ? 154.601 162.567 137.635 1.00 18.78  ? 168 TRP D CH2 1 
ATOM   4590 N N   . PRO B 2 53  ? 159.356 163.234 133.410 1.00 20.48  ? 169 PRO D N   1 
ATOM   4591 C CA  . PRO B 2 53  ? 160.170 164.456 133.300 1.00 22.17  ? 169 PRO D CA  1 
ATOM   4592 C C   . PRO B 2 53  ? 160.570 165.056 134.636 1.00 26.57  ? 169 PRO D C   1 
ATOM   4593 O O   . PRO B 2 53  ? 161.548 165.812 134.687 1.00 28.83  ? 169 PRO D O   1 
ATOM   4594 C CB  . PRO B 2 53  ? 159.263 165.407 132.511 1.00 25.26  ? 169 PRO D CB  1 
ATOM   4595 C CG  . PRO B 2 53  ? 158.319 164.511 131.778 1.00 17.69  ? 169 PRO D CG  1 
ATOM   4596 C CD  . PRO B 2 53  ? 158.077 163.357 132.696 1.00 15.95  ? 169 PRO D CD  1 
ATOM   4597 N N   . GLY B 2 54  ? 159.845 164.756 135.715 1.00 26.08  ? 170 GLY D N   1 
ATOM   4598 C CA  . GLY B 2 54  ? 160.207 165.308 137.009 1.00 23.28  ? 170 GLY D CA  1 
ATOM   4599 C C   . GLY B 2 54  ? 161.538 164.791 137.519 1.00 28.31  ? 170 GLY D C   1 
ATOM   4600 O O   . GLY B 2 54  ? 162.289 165.521 138.172 1.00 31.41  ? 170 GLY D O   1 
ATOM   4601 N N   . SER B 2 55  ? 161.850 163.527 137.230 1.00 27.11  ? 171 SER D N   1 
ATOM   4602 C CA  . SER B 2 55  ? 163.073 162.902 137.711 1.00 28.35  ? 171 SER D CA  1 
ATOM   4603 C C   . SER B 2 55  ? 163.896 162.227 136.625 1.00 27.89  ? 171 SER D C   1 
ATOM   4604 O O   . SER B 2 55  ? 165.049 161.871 136.889 1.00 28.36  ? 171 SER D O   1 
ATOM   4605 C CB  . SER B 2 55  ? 162.753 161.867 138.800 1.00 26.99  ? 171 SER D CB  1 
ATOM   4606 O OG  . SER B 2 55  ? 162.367 160.630 138.227 1.00 22.95  ? 171 SER D OG  1 
ATOM   4607 N N   . GLY B 2 56  ? 163.355 162.042 135.423 1.00 23.13  ? 172 GLY D N   1 
ATOM   4608 C CA  . GLY B 2 56  ? 164.088 161.366 134.372 1.00 23.74  ? 172 GLY D CA  1 
ATOM   4609 C C   . GLY B 2 56  ? 164.086 159.859 134.462 1.00 24.35  ? 172 GLY D C   1 
ATOM   4610 O O   . GLY B 2 56  ? 164.864 159.209 133.759 1.00 21.86  ? 172 GLY D O   1 
ATOM   4611 N N   . GLY B 2 57  ? 163.236 159.280 135.307 1.00 23.78  ? 173 GLY D N   1 
ATOM   4612 C CA  . GLY B 2 57  ? 163.174 157.839 135.447 1.00 15.88  ? 173 GLY D CA  1 
ATOM   4613 C C   . GLY B 2 57  ? 162.350 157.185 134.359 1.00 17.08  ? 173 GLY D C   1 
ATOM   4614 O O   . GLY B 2 57  ? 161.118 157.266 134.369 1.00 17.70  ? 173 GLY D O   1 
ATOM   4615 N N   . THR B 2 58  ? 163.020 156.528 133.419 1.00 16.72  ? 174 THR D N   1 
ATOM   4616 C CA  . THR B 2 58  ? 162.358 155.962 132.255 1.00 15.48  ? 174 THR D CA  1 
ATOM   4617 C C   . THR B 2 58  ? 162.109 154.470 132.429 1.00 16.25  ? 174 THR D C   1 
ATOM   4618 O O   . THR B 2 58  ? 162.882 153.756 133.073 1.00 23.56  ? 174 THR D O   1 
ATOM   4619 C CB  . THR B 2 58  ? 163.193 156.191 130.994 1.00 19.77  ? 174 THR D CB  1 
ATOM   4620 O OG1 . THR B 2 58  ? 164.154 155.137 130.860 1.00 24.05  ? 174 THR D OG1 1 
ATOM   4621 C CG2 . THR B 2 58  ? 163.921 157.519 131.071 1.00 24.58  ? 174 THR D CG2 1 
ATOM   4622 N N   . ASN B 2 59  ? 161.011 154.007 131.842 1.00 11.64  ? 175 ASN D N   1 
ATOM   4623 C CA  . ASN B 2 59  ? 160.712 152.593 131.702 1.00 14.56  ? 175 ASN D CA  1 
ATOM   4624 C C   . ASN B 2 59  ? 160.780 152.220 130.228 1.00 18.17  ? 175 ASN D C   1 
ATOM   4625 O O   . ASN B 2 59  ? 160.707 153.079 129.346 1.00 19.55  ? 175 ASN D O   1 
ATOM   4626 C CB  . ASN B 2 59  ? 159.336 152.258 132.281 1.00 10.32  ? 175 ASN D CB  1 
ATOM   4627 C CG  . ASN B 2 59  ? 159.168 152.759 133.699 1.00 11.45  ? 175 ASN D CG  1 
ATOM   4628 O OD1 . ASN B 2 59  ? 159.380 153.938 133.980 1.00 12.80  ? 175 ASN D OD1 1 
ATOM   4629 N ND2 . ASN B 2 59  ? 158.789 151.864 134.603 1.00 12.42  ? 175 ASN D ND2 1 
ATOM   4630 N N   . TYR B 2 60  ? 160.939 150.927 129.962 1.00 21.92  ? 176 TYR D N   1 
ATOM   4631 C CA  . TYR B 2 60  ? 161.260 150.490 128.615 1.00 20.77  ? 176 TYR D CA  1 
ATOM   4632 C C   . TYR B 2 60  ? 160.507 149.209 128.294 1.00 30.10  ? 176 TYR D C   1 
ATOM   4633 O O   . TYR B 2 60  ? 160.109 148.456 129.185 1.00 32.38  ? 176 TYR D O   1 
ATOM   4634 C CB  . TYR B 2 60  ? 162.767 150.271 128.467 1.00 26.11  ? 176 TYR D CB  1 
ATOM   4635 C CG  . TYR B 2 60  ? 163.531 151.553 128.258 1.00 26.35  ? 176 TYR D CG  1 
ATOM   4636 C CD1 . TYR B 2 60  ? 163.111 152.494 127.333 1.00 23.05  ? 176 TYR D CD1 1 
ATOM   4637 C CD2 . TYR B 2 60  ? 164.662 151.833 129.012 1.00 31.08  ? 176 TYR D CD2 1 
ATOM   4638 C CE1 . TYR B 2 60  ? 163.806 153.672 127.155 1.00 25.24  ? 176 TYR D CE1 1 
ATOM   4639 C CE2 . TYR B 2 60  ? 165.361 153.005 128.840 1.00 28.23  ? 176 TYR D CE2 1 
ATOM   4640 C CZ  . TYR B 2 60  ? 164.930 153.920 127.909 1.00 28.47  ? 176 TYR D CZ  1 
ATOM   4641 O OH  . TYR B 2 60  ? 165.627 155.090 127.737 1.00 33.58  ? 176 TYR D OH  1 
ATOM   4642 N N   . ALA B 2 61  ? 160.312 148.975 127.001 1.00 30.16  ? 177 ALA D N   1 
ATOM   4643 C CA  . ALA B 2 61  ? 159.786 147.709 126.519 1.00 33.33  ? 177 ALA D CA  1 
ATOM   4644 C C   . ALA B 2 61  ? 160.937 146.749 126.251 1.00 45.28  ? 177 ALA D C   1 
ATOM   4645 O O   . ALA B 2 61  ? 162.058 147.165 125.947 1.00 48.73  ? 177 ALA D O   1 
ATOM   4646 C CB  . ALA B 2 61  ? 158.957 147.909 125.250 1.00 29.97  ? 177 ALA D CB  1 
ATOM   4647 N N   . GLU B 2 62  ? 160.651 145.451 126.374 1.00 47.65  ? 178 GLU D N   1 
ATOM   4648 C CA  . GLU B 2 62  ? 161.695 144.449 126.185 1.00 49.28  ? 178 GLU D CA  1 
ATOM   4649 C C   . GLU B 2 62  ? 162.275 144.498 124.778 1.00 51.85  ? 178 GLU D C   1 
ATOM   4650 O O   . GLU B 2 62  ? 163.455 144.188 124.583 1.00 55.63  ? 178 GLU D O   1 
ATOM   4651 C CB  . GLU B 2 62  ? 161.153 143.052 126.490 1.00 50.68  ? 178 GLU D CB  1 
ATOM   4652 C CG  . GLU B 2 62  ? 160.119 143.008 127.605 1.00 53.45  ? 178 GLU D CG  1 
ATOM   4653 C CD  . GLU B 2 62  ? 158.704 143.216 127.102 1.00 58.41  ? 178 GLU D CD  1 
ATOM   4654 O OE1 . GLU B 2 62  ? 158.490 143.139 125.874 1.00 52.66  ? 178 GLU D OE1 1 
ATOM   4655 O OE2 . GLU B 2 62  ? 157.807 143.458 127.936 1.00 56.64  ? 178 GLU D OE2 1 
ATOM   4656 N N   . LYS B 2 63  ? 161.469 144.886 123.790 1.00 47.01  ? 179 LYS D N   1 
ATOM   4657 C CA  . LYS B 2 63  ? 161.944 144.982 122.417 1.00 46.59  ? 179 LYS D CA  1 
ATOM   4658 C C   . LYS B 2 63  ? 162.772 146.233 122.156 1.00 47.44  ? 179 LYS D C   1 
ATOM   4659 O O   . LYS B 2 63  ? 163.398 146.329 121.096 1.00 51.92  ? 179 LYS D O   1 
ATOM   4660 C CB  . LYS B 2 63  ? 160.760 144.939 121.449 1.00 42.68  ? 179 LYS D CB  1 
ATOM   4661 C CG  . LYS B 2 63  ? 159.567 144.154 121.968 1.00 39.79  ? 179 LYS D CG  1 
ATOM   4662 C CD  . LYS B 2 63  ? 158.383 144.235 121.016 1.00 42.07  ? 179 LYS D CD  1 
ATOM   4663 C CE  . LYS B 2 63  ? 158.827 144.220 119.561 1.00 41.15  ? 179 LYS D CE  1 
ATOM   4664 N NZ  . LYS B 2 63  ? 157.724 144.606 118.639 1.00 37.82  ? 179 LYS D NZ  1 
ATOM   4665 N N   . PHE B 2 64  ? 162.790 147.189 123.087 1.00 44.69  ? 180 PHE D N   1 
ATOM   4666 C CA  . PHE B 2 64  ? 163.565 148.410 122.922 1.00 45.86  ? 180 PHE D CA  1 
ATOM   4667 C C   . PHE B 2 64  ? 164.450 148.739 124.116 1.00 48.31  ? 180 PHE D C   1 
ATOM   4668 O O   . PHE B 2 64  ? 165.062 149.812 124.126 1.00 53.27  ? 180 PHE D O   1 
ATOM   4669 C CB  . PHE B 2 64  ? 162.642 149.610 122.654 1.00 41.52  ? 180 PHE D CB  1 
ATOM   4670 C CG  . PHE B 2 64  ? 161.577 149.352 121.628 1.00 38.84  ? 180 PHE D CG  1 
ATOM   4671 C CD1 . PHE B 2 64  ? 161.830 149.553 120.282 1.00 38.58  ? 180 PHE D CD1 1 
ATOM   4672 C CD2 . PHE B 2 64  ? 160.316 148.933 122.011 1.00 34.55  ? 180 PHE D CD2 1 
ATOM   4673 C CE1 . PHE B 2 64  ? 160.849 149.324 119.338 1.00 35.22  ? 180 PHE D CE1 1 
ATOM   4674 C CE2 . PHE B 2 64  ? 159.332 148.704 121.073 1.00 28.47  ? 180 PHE D CE2 1 
ATOM   4675 C CZ  . PHE B 2 64  ? 159.598 148.899 119.735 1.00 31.21  ? 180 PHE D CZ  1 
ATOM   4676 N N   . LYS B 2 65  ? 164.541 147.855 125.114 1.00 46.25  ? 181 LYS D N   1 
ATOM   4677 C CA  . LYS B 2 65  ? 165.248 148.197 126.346 1.00 49.57  ? 181 LYS D CA  1 
ATOM   4678 C C   . LYS B 2 65  ? 166.715 148.510 126.082 1.00 53.74  ? 181 LYS D C   1 
ATOM   4679 O O   . LYS B 2 65  ? 167.263 149.470 126.636 1.00 42.54  ? 181 LYS D O   1 
ATOM   4680 C CB  . LYS B 2 65  ? 165.116 147.060 127.358 1.00 45.29  ? 181 LYS D CB  1 
ATOM   4681 C CG  . LYS B 2 65  ? 165.593 147.420 128.755 1.00 45.73  ? 181 LYS D CG  1 
ATOM   4682 C CD  . LYS B 2 65  ? 164.453 147.378 129.760 1.00 44.03  ? 181 LYS D CD  1 
ATOM   4683 C CE  . LYS B 2 65  ? 164.835 148.075 131.056 1.00 43.06  ? 181 LYS D CE  1 
ATOM   4684 N NZ  . LYS B 2 65  ? 163.699 148.849 131.629 1.00 34.08  ? 181 LYS D NZ  1 
ATOM   4685 N N   . ASN B 2 66  ? 167.367 147.717 125.237 1.00 62.18  ? 182 ASN D N   1 
ATOM   4686 C CA  . ASN B 2 66  ? 168.771 147.913 124.906 1.00 64.12  ? 182 ASN D CA  1 
ATOM   4687 C C   . ASN B 2 66  ? 168.974 148.744 123.645 1.00 65.26  ? 182 ASN D C   1 
ATOM   4688 O O   . ASN B 2 66  ? 170.114 148.892 123.193 1.00 58.98  ? 182 ASN D O   1 
ATOM   4689 C CB  . ASN B 2 66  ? 169.467 146.558 124.750 1.00 64.03  ? 182 ASN D CB  1 
ATOM   4690 C CG  . ASN B 2 66  ? 168.606 145.542 124.026 1.00 63.66  ? 182 ASN D CG  1 
ATOM   4691 O OD1 . ASN B 2 66  ? 167.842 145.889 123.125 1.00 59.96  ? 182 ASN D OD1 1 
ATOM   4692 N ND2 . ASN B 2 66  ? 168.727 144.279 124.416 1.00 57.68  ? 182 ASN D ND2 1 
ATOM   4693 N N   . ARG B 2 67  ? 167.900 149.287 123.066 1.00 63.71  ? 183 ARG D N   1 
ATOM   4694 C CA  . ARG B 2 67  ? 167.984 149.981 121.790 1.00 60.24  ? 183 ARG D CA  1 
ATOM   4695 C C   . ARG B 2 67  ? 167.524 151.430 121.819 1.00 53.60  ? 183 ARG D C   1 
ATOM   4696 O O   . ARG B 2 67  ? 167.971 152.210 120.971 1.00 54.31  ? 183 ARG D O   1 
ATOM   4697 C CB  . ARG B 2 67  ? 167.165 149.235 120.724 1.00 61.63  ? 183 ARG D CB  1 
ATOM   4698 C CG  . ARG B 2 67  ? 167.763 149.309 119.335 1.00 65.86  ? 183 ARG D CG  1 
ATOM   4699 C CD  . ARG B 2 67  ? 167.347 148.119 118.492 1.00 65.48  ? 183 ARG D CD  1 
ATOM   4700 N NE  . ARG B 2 67  ? 165.971 147.714 118.750 1.00 56.16  ? 183 ARG D NE  1 
ATOM   4701 C CZ  . ARG B 2 67  ? 164.938 148.047 117.989 1.00 53.30  ? 183 ARG D CZ  1 
ATOM   4702 N NH1 . ARG B 2 67  ? 165.090 148.791 116.906 1.00 54.35  ? 183 ARG D NH1 1 
ATOM   4703 N NH2 . ARG B 2 67  ? 163.723 147.620 118.321 1.00 46.85  ? 183 ARG D NH2 1 
ATOM   4704 N N   . VAL B 2 68  ? 166.662 151.819 122.756 1.00 49.29  ? 184 VAL D N   1 
ATOM   4705 C CA  . VAL B 2 68  ? 166.091 153.159 122.789 1.00 48.80  ? 184 VAL D CA  1 
ATOM   4706 C C   . VAL B 2 68  ? 166.496 153.847 124.085 1.00 43.91  ? 184 VAL D C   1 
ATOM   4707 O O   . VAL B 2 68  ? 166.591 153.211 125.141 1.00 42.82  ? 184 VAL D O   1 
ATOM   4708 C CB  . VAL B 2 68  ? 164.553 153.135 122.630 1.00 45.97  ? 184 VAL D CB  1 
ATOM   4709 C CG1 . VAL B 2 68  ? 163.874 152.715 123.910 1.00 40.69  ? 184 VAL D CG1 1 
ATOM   4710 C CG2 . VAL B 2 68  ? 164.041 154.496 122.202 1.00 46.53  ? 184 VAL D CG2 1 
ATOM   4711 N N   . THR B 2 69  ? 166.783 155.144 123.986 1.00 40.77  ? 185 THR D N   1 
ATOM   4712 C CA  . THR B 2 69  ? 167.059 155.995 125.136 1.00 40.17  ? 185 THR D CA  1 
ATOM   4713 C C   . THR B 2 69  ? 166.172 157.227 125.052 1.00 39.63  ? 185 THR D C   1 
ATOM   4714 O O   . THR B 2 69  ? 166.147 157.905 124.021 1.00 45.27  ? 185 THR D O   1 
ATOM   4715 C CB  . THR B 2 69  ? 168.532 156.420 125.190 1.00 42.56  ? 185 THR D CB  1 
ATOM   4716 O OG1 . THR B 2 69  ? 168.709 157.622 124.431 1.00 49.76  ? 185 THR D OG1 1 
ATOM   4717 C CG2 . THR B 2 69  ? 169.437 155.330 124.631 1.00 41.21  ? 185 THR D CG2 1 
ATOM   4718 N N   . MET B 2 70  ? 165.452 157.520 126.132 1.00 33.03  ? 186 MET D N   1 
ATOM   4719 C CA  . MET B 2 70  ? 164.587 158.692 126.197 1.00 34.93  ? 186 MET D CA  1 
ATOM   4720 C C   . MET B 2 70  ? 165.061 159.612 127.311 1.00 35.81  ? 186 MET D C   1 
ATOM   4721 O O   . MET B 2 70  ? 165.232 159.174 128.454 1.00 31.28  ? 186 MET D O   1 
ATOM   4722 C CB  . MET B 2 70  ? 163.124 158.299 126.421 1.00 29.23  ? 186 MET D CB  1 
ATOM   4723 C CG  . MET B 2 70  ? 162.925 157.036 127.232 1.00 27.60  ? 186 MET D CG  1 
ATOM   4724 S SD  . MET B 2 70  ? 161.379 156.195 126.837 1.00 29.33  ? 186 MET D SD  1 
ATOM   4725 C CE  . MET B 2 70  ? 161.564 155.943 125.076 1.00 27.35  ? 186 MET D CE  1 
ATOM   4726 N N   . THR B 2 71  ? 165.266 160.883 126.976 1.00 39.09  ? 187 THR D N   1 
ATOM   4727 C CA  . THR B 2 71  ? 165.692 161.892 127.933 1.00 40.67  ? 187 THR D CA  1 
ATOM   4728 C C   . THR B 2 71  ? 164.779 163.105 127.827 1.00 37.13  ? 187 THR D C   1 
ATOM   4729 O O   . THR B 2 71  ? 164.282 163.435 126.747 1.00 35.73  ? 187 THR D O   1 
ATOM   4730 C CB  . THR B 2 71  ? 167.149 162.314 127.703 1.00 46.23  ? 187 THR D CB  1 
ATOM   4731 O OG1 . THR B 2 71  ? 167.387 162.476 126.299 1.00 53.02  ? 187 THR D OG1 1 
ATOM   4732 C CG2 . THR B 2 71  ? 168.099 161.262 128.254 1.00 39.03  ? 187 THR D CG2 1 
ATOM   4733 N N   . ARG B 2 72  ? 164.561 163.765 128.957 1.00 33.98  ? 188 ARG D N   1 
ATOM   4734 C CA  . ARG B 2 72  ? 163.681 164.921 129.020 1.00 37.65  ? 188 ARG D CA  1 
ATOM   4735 C C   . ARG B 2 72  ? 164.487 166.212 129.092 1.00 53.51  ? 188 ARG D C   1 
ATOM   4736 O O   . ARG B 2 72  ? 165.661 166.224 129.470 1.00 62.43  ? 188 ARG D O   1 
ATOM   4737 C CB  . ARG B 2 72  ? 162.740 164.822 130.225 1.00 33.75  ? 188 ARG D CB  1 
ATOM   4738 C CG  . ARG B 2 72  ? 163.380 164.245 131.479 1.00 33.00  ? 188 ARG D CG  1 
ATOM   4739 C CD  . ARG B 2 72  ? 164.097 165.318 132.283 1.00 36.32  ? 188 ARG D CD  1 
ATOM   4740 N NE  . ARG B 2 72  ? 164.118 165.021 133.709 1.00 35.72  ? 188 ARG D NE  1 
ATOM   4741 C CZ  . ARG B 2 72  ? 165.066 165.428 134.542 1.00 40.45  ? 188 ARG D CZ  1 
ATOM   4742 N NH1 . ARG B 2 72  ? 166.091 166.150 134.121 1.00 49.21  ? 188 ARG D NH1 1 
ATOM   4743 N NH2 . ARG B 2 72  ? 164.982 165.105 135.829 1.00 39.43  ? 188 ARG D NH2 1 
ATOM   4744 N N   . ASP B 2 73  ? 163.833 167.308 128.717 1.00 47.82  ? 189 ASP D N   1 
ATOM   4745 C CA  . ASP B 2 73  ? 164.391 168.654 128.814 1.00 48.82  ? 189 ASP D CA  1 
ATOM   4746 C C   . ASP B 2 73  ? 163.424 169.469 129.668 1.00 54.56  ? 189 ASP D C   1 
ATOM   4747 O O   . ASP B 2 73  ? 162.477 170.068 129.153 1.00 57.49  ? 189 ASP D O   1 
ATOM   4748 C CB  . ASP B 2 73  ? 164.597 169.274 127.436 1.00 54.61  ? 189 ASP D CB  1 
ATOM   4749 C CG  . ASP B 2 73  ? 165.743 170.264 127.409 1.00 68.25  ? 189 ASP D CG  1 
ATOM   4750 O OD1 . ASP B 2 73  ? 165.683 171.263 128.155 1.00 74.18  ? 189 ASP D OD1 1 
ATOM   4751 O OD2 . ASP B 2 73  ? 166.700 170.047 126.636 1.00 70.40  ? 189 ASP D OD2 1 
ATOM   4752 N N   . THR B 2 74  ? 163.669 169.478 130.980 1.00 54.90  ? 190 THR D N   1 
ATOM   4753 C CA  . THR B 2 74  ? 162.744 170.115 131.914 1.00 57.22  ? 190 THR D CA  1 
ATOM   4754 C C   . THR B 2 74  ? 162.626 171.613 131.659 1.00 61.50  ? 190 THR D C   1 
ATOM   4755 O O   . THR B 2 74  ? 161.522 172.170 131.697 1.00 59.59  ? 190 THR D O   1 
ATOM   4756 C CB  . THR B 2 74  ? 163.197 169.852 133.351 1.00 51.61  ? 190 THR D CB  1 
ATOM   4757 O OG1 . THR B 2 74  ? 163.270 168.439 133.582 1.00 46.22  ? 190 THR D OG1 1 
ATOM   4758 C CG2 . THR B 2 74  ? 162.238 170.482 134.345 1.00 52.67  ? 190 THR D CG2 1 
ATOM   4759 N N   . SER B 2 75  ? 163.752 172.282 131.397 1.00 64.16  ? 191 SER D N   1 
ATOM   4760 C CA  . SER B 2 75  ? 163.740 173.736 131.260 1.00 63.65  ? 191 SER D CA  1 
ATOM   4761 C C   . SER B 2 75  ? 162.888 174.184 130.078 1.00 63.71  ? 191 SER D C   1 
ATOM   4762 O O   . SER B 2 75  ? 162.124 175.150 130.186 1.00 62.50  ? 191 SER D O   1 
ATOM   4763 C CB  . SER B 2 75  ? 165.169 174.258 131.118 1.00 65.78  ? 191 SER D CB  1 
ATOM   4764 O OG  . SER B 2 75  ? 165.849 173.600 130.063 1.00 60.50  ? 191 SER D OG  1 
ATOM   4765 N N   . ILE B 2 76  ? 163.004 173.495 128.938 1.00 58.60  ? 192 ILE D N   1 
ATOM   4766 C CA  . ILE B 2 76  ? 162.254 173.872 127.744 1.00 57.79  ? 192 ILE D CA  1 
ATOM   4767 C C   . ILE B 2 76  ? 160.958 173.084 127.599 1.00 60.11  ? 192 ILE D C   1 
ATOM   4768 O O   . ILE B 2 76  ? 160.194 173.333 126.655 1.00 58.14  ? 192 ILE D O   1 
ATOM   4769 C CB  . ILE B 2 76  ? 163.138 173.710 126.488 1.00 59.58  ? 192 ILE D CB  1 
ATOM   4770 C CG1 . ILE B 2 76  ? 162.679 174.654 125.373 1.00 68.21  ? 192 ILE D CG1 1 
ATOM   4771 C CG2 . ILE B 2 76  ? 163.144 172.268 126.014 1.00 53.16  ? 192 ILE D CG2 1 
ATOM   4772 C CD1 . ILE B 2 76  ? 163.012 176.108 125.627 1.00 67.78  ? 192 ILE D CD1 1 
ATOM   4773 N N   . SER B 2 77  ? 160.677 172.154 128.515 1.00 56.61  ? 193 SER D N   1 
ATOM   4774 C CA  . SER B 2 77  ? 159.459 171.343 128.495 1.00 45.61  ? 193 SER D CA  1 
ATOM   4775 C C   . SER B 2 77  ? 159.340 170.563 127.184 1.00 42.62  ? 193 SER D C   1 
ATOM   4776 O O   . SER B 2 77  ? 158.423 170.764 126.385 1.00 43.29  ? 193 SER D O   1 
ATOM   4777 C CB  . SER B 2 77  ? 158.216 172.207 128.741 1.00 44.05  ? 193 SER D CB  1 
ATOM   4778 O OG  . SER B 2 77  ? 158.103 172.561 130.108 1.00 46.96  ? 193 SER D OG  1 
ATOM   4779 N N   . THR B 2 78  ? 160.296 169.661 126.975 1.00 44.50  ? 194 THR D N   1 
ATOM   4780 C CA  . THR B 2 78  ? 160.334 168.853 125.760 1.00 42.50  ? 194 THR D CA  1 
ATOM   4781 C C   . THR B 2 78  ? 160.995 167.521 126.073 1.00 40.26  ? 194 THR D C   1 
ATOM   4782 O O   . THR B 2 78  ? 162.157 167.488 126.487 1.00 45.20  ? 194 THR D O   1 
ATOM   4783 C CB  . THR B 2 78  ? 161.089 169.577 124.643 1.00 45.19  ? 194 THR D CB  1 
ATOM   4784 O OG1 . THR B 2 78  ? 160.287 170.652 124.139 1.00 48.47  ? 194 THR D OG1 1 
ATOM   4785 C CG2 . THR B 2 78  ? 161.413 168.620 123.512 1.00 40.90  ? 194 THR D CG2 1 
ATOM   4786 N N   . ALA B 2 79  ? 160.260 166.431 125.876 1.00 33.75  ? 195 ALA D N   1 
ATOM   4787 C CA  . ALA B 2 79  ? 160.803 165.093 126.048 1.00 35.59  ? 195 ALA D CA  1 
ATOM   4788 C C   . ALA B 2 79  ? 161.332 164.567 124.720 1.00 38.34  ? 195 ALA D C   1 
ATOM   4789 O O   . ALA B 2 79  ? 160.894 164.985 123.646 1.00 38.92  ? 195 ALA D O   1 
ATOM   4790 C CB  . ALA B 2 79  ? 159.744 164.143 126.604 1.00 29.49  ? 195 ALA D CB  1 
ATOM   4791 N N   . TYR B 2 80  ? 162.281 163.638 124.804 1.00 37.71  ? 196 TYR D N   1 
ATOM   4792 C CA  . TYR B 2 80  ? 162.968 163.124 123.630 1.00 36.78  ? 196 TYR D CA  1 
ATOM   4793 C C   . TYR B 2 80  ? 162.912 161.603 123.612 1.00 29.37  ? 196 TYR D C   1 
ATOM   4794 O O   . TYR B 2 80  ? 162.726 160.952 124.643 1.00 25.84  ? 196 TYR D O   1 
ATOM   4795 C CB  . TYR B 2 80  ? 164.429 163.593 123.587 1.00 42.75  ? 196 TYR D CB  1 
ATOM   4796 C CG  . TYR B 2 80  ? 164.590 165.086 123.415 1.00 44.43  ? 196 TYR D CG  1 
ATOM   4797 C CD1 . TYR B 2 80  ? 164.629 165.659 122.152 1.00 49.08  ? 196 TYR D CD1 1 
ATOM   4798 C CD2 . TYR B 2 80  ? 164.699 165.923 124.518 1.00 38.51  ? 196 TYR D CD2 1 
ATOM   4799 C CE1 . TYR B 2 80  ? 164.776 167.023 121.991 1.00 51.35  ? 196 TYR D CE1 1 
ATOM   4800 C CE2 . TYR B 2 80  ? 164.844 167.287 124.367 1.00 46.10  ? 196 TYR D CE2 1 
ATOM   4801 C CZ  . TYR B 2 80  ? 164.882 167.832 123.102 1.00 53.95  ? 196 TYR D CZ  1 
ATOM   4802 O OH  . TYR B 2 80  ? 165.027 169.191 122.945 1.00 58.99  ? 196 TYR D OH  1 
ATOM   4803 N N   . MET B 2 81  ? 163.074 161.045 122.413 1.00 28.70  ? 197 MET D N   1 
ATOM   4804 C CA  . MET B 2 81  ? 163.092 159.599 122.205 1.00 28.16  ? 197 MET D CA  1 
ATOM   4805 C C   . MET B 2 81  ? 164.153 159.295 121.158 1.00 39.77  ? 197 MET D C   1 
ATOM   4806 O O   . MET B 2 81  ? 163.998 159.667 119.991 1.00 46.56  ? 197 MET D O   1 
ATOM   4807 C CB  . MET B 2 81  ? 161.718 159.084 121.770 1.00 27.81  ? 197 MET D CB  1 
ATOM   4808 C CG  . MET B 2 81  ? 161.546 157.573 121.857 1.00 21.97  ? 197 MET D CG  1 
ATOM   4809 S SD  . MET B 2 81  ? 162.010 156.689 120.354 1.00 30.16  ? 197 MET D SD  1 
ATOM   4810 C CE  . MET B 2 81  ? 161.545 157.869 119.090 1.00 26.82  ? 197 MET D CE  1 
ATOM   4811 N N   . GLU B 2 82  ? 165.232 158.636 121.573 1.00 38.89  ? 198 GLU D N   1 
ATOM   4812 C CA  . GLU B 2 82  ? 166.355 158.324 120.696 1.00 41.90  ? 198 GLU D CA  1 
ATOM   4813 C C   . GLU B 2 82  ? 166.359 156.829 120.409 1.00 40.27  ? 198 GLU D C   1 
ATOM   4814 O O   . GLU B 2 82  ? 166.646 156.021 121.298 1.00 39.20  ? 198 GLU D O   1 
ATOM   4815 C CB  . GLU B 2 82  ? 167.675 158.763 121.326 1.00 50.98  ? 198 GLU D CB  1 
ATOM   4816 C CG  . GLU B 2 82  ? 168.900 158.415 120.499 1.00 53.96  ? 198 GLU D CG  1 
ATOM   4817 C CD  . GLU B 2 82  ? 170.171 159.024 121.054 1.00 54.67  ? 198 GLU D CD  1 
ATOM   4818 O OE1 . GLU B 2 82  ? 170.086 159.782 122.043 1.00 55.19  ? 198 GLU D OE1 1 
ATOM   4819 O OE2 . GLU B 2 82  ? 171.255 158.745 120.501 1.00 55.99  ? 198 GLU D OE2 1 
ATOM   4820 N N   . LEU B 2 83  ? 166.061 156.467 119.164 1.00 47.30  ? 199 LEU D N   1 
ATOM   4821 C CA  . LEU B 2 83  ? 166.083 155.083 118.707 1.00 56.24  ? 199 LEU D CA  1 
ATOM   4822 C C   . LEU B 2 83  ? 167.329 154.877 117.858 1.00 64.90  ? 199 LEU D C   1 
ATOM   4823 O O   . LEU B 2 83  ? 167.512 155.558 116.844 1.00 67.46  ? 199 LEU D O   1 
ATOM   4824 C CB  . LEU B 2 83  ? 164.821 154.750 117.910 1.00 56.96  ? 199 LEU D CB  1 
ATOM   4825 C CG  . LEU B 2 83  ? 164.438 153.276 117.751 1.00 57.84  ? 199 LEU D CG  1 
ATOM   4826 C CD1 . LEU B 2 83  ? 164.043 152.659 119.077 1.00 52.46  ? 199 LEU D CD1 1 
ATOM   4827 C CD2 . LEU B 2 83  ? 163.306 153.135 116.751 1.00 53.29  ? 199 LEU D CD2 1 
ATOM   4828 N N   . SER B 2 84  ? 168.178 153.943 118.273 1.00 67.23  ? 200 SER D N   1 
ATOM   4829 C CA  . SER B 2 84  ? 169.431 153.651 117.595 1.00 69.56  ? 200 SER D CA  1 
ATOM   4830 C C   . SER B 2 84  ? 169.352 152.296 116.904 1.00 76.45  ? 200 SER D C   1 
ATOM   4831 O O   . SER B 2 84  ? 168.450 151.493 117.159 1.00 69.81  ? 200 SER D O   1 
ATOM   4832 C CB  . SER B 2 84  ? 170.602 153.678 118.585 1.00 65.18  ? 200 SER D CB  1 
ATOM   4833 O OG  . SER B 2 84  ? 170.617 154.887 119.324 1.00 62.53  ? 200 SER D OG  1 
ATOM   4834 N N   . ARG B 2 85  ? 170.323 152.052 116.022 1.00 81.83  ? 201 ARG D N   1 
ATOM   4835 C CA  . ARG B 2 85  ? 170.416 150.805 115.261 1.00 77.77  ? 201 ARG D CA  1 
ATOM   4836 C C   . ARG B 2 85  ? 169.099 150.495 114.554 1.00 77.34  ? 201 ARG D C   1 
ATOM   4837 O O   . ARG B 2 85  ? 168.512 149.422 114.716 1.00 74.68  ? 201 ARG D O   1 
ATOM   4838 C CB  . ARG B 2 85  ? 170.845 149.645 116.160 1.00 73.61  ? 201 ARG D CB  1 
ATOM   4839 C CG  . ARG B 2 85  ? 171.963 149.990 117.129 1.00 71.95  ? 201 ARG D CG  1 
ATOM   4840 C CD  . ARG B 2 85  ? 172.675 148.740 117.615 1.00 76.21  ? 201 ARG D CD  1 
ATOM   4841 N NE  . ARG B 2 85  ? 171.806 147.895 118.425 1.00 75.14  ? 201 ARG D NE  1 
ATOM   4842 C CZ  . ARG B 2 85  ? 171.607 148.054 119.726 1.00 70.08  ? 201 ARG D CZ  1 
ATOM   4843 N NH1 . ARG B 2 85  ? 172.197 149.026 120.402 1.00 65.67  ? 201 ARG D NH1 1 
ATOM   4844 N NH2 . ARG B 2 85  ? 170.796 147.216 120.366 1.00 67.64  ? 201 ARG D NH2 1 
ATOM   4845 N N   . LEU B 2 86  ? 168.629 151.462 113.769 1.00 77.25  ? 202 LEU D N   1 
ATOM   4846 C CA  . LEU B 2 86  ? 167.348 151.327 113.089 1.00 72.59  ? 202 LEU D CA  1 
ATOM   4847 C C   . LEU B 2 86  ? 167.367 150.144 112.129 1.00 70.63  ? 202 LEU D C   1 
ATOM   4848 O O   . LEU B 2 86  ? 168.301 149.982 111.339 1.00 77.15  ? 202 LEU D O   1 
ATOM   4849 C CB  . LEU B 2 86  ? 167.017 152.616 112.339 1.00 71.78  ? 202 LEU D CB  1 
ATOM   4850 C CG  . LEU B 2 86  ? 166.655 153.813 113.220 1.00 71.64  ? 202 LEU D CG  1 
ATOM   4851 C CD1 . LEU B 2 86  ? 166.788 155.112 112.447 1.00 70.88  ? 202 LEU D CD1 1 
ATOM   4852 C CD2 . LEU B 2 86  ? 165.249 153.660 113.766 1.00 68.27  ? 202 LEU D CD2 1 
ATOM   4853 N N   . ARG B 2 87  ? 166.328 149.320 112.202 1.00 64.25  ? 203 ARG D N   1 
ATOM   4854 C CA  . ARG B 2 87  ? 166.189 148.141 111.366 1.00 63.83  ? 203 ARG D CA  1 
ATOM   4855 C C   . ARG B 2 87  ? 165.176 148.416 110.259 1.00 61.54  ? 203 ARG D C   1 
ATOM   4856 O O   . ARG B 2 87  ? 164.640 149.520 110.138 1.00 61.20  ? 203 ARG D O   1 
ATOM   4857 C CB  . ARG B 2 87  ? 165.778 146.942 112.219 1.00 62.45  ? 203 ARG D CB  1 
ATOM   4858 C CG  . ARG B 2 87  ? 166.487 146.855 113.557 1.00 66.76  ? 203 ARG D CG  1 
ATOM   4859 C CD  . ARG B 2 87  ? 165.710 145.970 114.512 1.00 74.14  ? 203 ARG D CD  1 
ATOM   4860 N NE  . ARG B 2 87  ? 164.943 144.957 113.799 1.00 86.64  ? 203 ARG D NE  1 
ATOM   4861 C CZ  . ARG B 2 87  ? 164.475 143.845 114.349 1.00 96.85  ? 203 ARG D CZ  1 
ATOM   4862 N NH1 . ARG B 2 87  ? 164.676 143.569 115.628 1.00 96.29  ? 203 ARG D NH1 1 
ATOM   4863 N NH2 . ARG B 2 87  ? 163.788 142.989 113.599 1.00 90.02  ? 203 ARG D NH2 1 
ATOM   4864 N N   . SER B 2 88  ? 164.897 147.399 109.442 1.00 63.77  ? 204 SER D N   1 
ATOM   4865 C CA  . SER B 2 88  ? 163.900 147.559 108.389 1.00 65.70  ? 204 SER D CA  1 
ATOM   4866 C C   . SER B 2 88  ? 162.492 147.656 108.961 1.00 65.77  ? 204 SER D C   1 
ATOM   4867 O O   . SER B 2 88  ? 161.621 148.291 108.355 1.00 64.44  ? 204 SER D O   1 
ATOM   4868 C CB  . SER B 2 88  ? 163.992 146.400 107.396 1.00 61.75  ? 204 SER D CB  1 
ATOM   4869 O OG  . SER B 2 88  ? 163.953 145.151 108.064 1.00 65.14  ? 204 SER D OG  1 
ATOM   4870 N N   . ASP B 2 89  ? 162.252 147.042 110.116 1.00 66.01  ? 205 ASP D N   1 
ATOM   4871 C CA  . ASP B 2 89  ? 160.946 147.063 110.761 1.00 61.39  ? 205 ASP D CA  1 
ATOM   4872 C C   . ASP B 2 89  ? 160.756 148.261 111.680 1.00 58.59  ? 205 ASP D C   1 
ATOM   4873 O O   . ASP B 2 89  ? 159.697 148.379 112.307 1.00 55.89  ? 205 ASP D O   1 
ATOM   4874 C CB  . ASP B 2 89  ? 160.732 145.770 111.554 1.00 65.22  ? 205 ASP D CB  1 
ATOM   4875 C CG  . ASP B 2 89  ? 160.670 144.545 110.664 1.00 70.69  ? 205 ASP D CG  1 
ATOM   4876 O OD1 . ASP B 2 89  ? 160.311 144.689 109.477 1.00 68.58  ? 205 ASP D OD1 1 
ATOM   4877 O OD2 . ASP B 2 89  ? 160.982 143.438 111.152 1.00 75.48  ? 205 ASP D OD2 1 
ATOM   4878 N N   . ASP B 2 90  ? 161.745 149.147 111.779 1.00 57.72  ? 206 ASP D N   1 
ATOM   4879 C CA  . ASP B 2 90  ? 161.653 150.303 112.661 1.00 48.85  ? 206 ASP D CA  1 
ATOM   4880 C C   . ASP B 2 90  ? 160.881 151.463 112.047 1.00 49.18  ? 206 ASP D C   1 
ATOM   4881 O O   . ASP B 2 90  ? 160.665 152.468 112.731 1.00 49.68  ? 206 ASP D O   1 
ATOM   4882 C CB  . ASP B 2 90  ? 163.054 150.773 113.062 1.00 52.41  ? 206 ASP D CB  1 
ATOM   4883 C CG  . ASP B 2 90  ? 163.534 150.134 114.350 1.00 55.42  ? 206 ASP D CG  1 
ATOM   4884 O OD1 . ASP B 2 90  ? 162.902 149.157 114.802 1.00 55.75  ? 206 ASP D OD1 1 
ATOM   4885 O OD2 . ASP B 2 90  ? 164.543 150.610 114.912 1.00 54.44  ? 206 ASP D OD2 1 
ATOM   4886 N N   . THR B 2 91  ? 160.466 151.357 110.787 1.00 53.86  ? 207 THR D N   1 
ATOM   4887 C CA  . THR B 2 91  ? 159.648 152.399 110.180 1.00 50.92  ? 207 THR D CA  1 
ATOM   4888 C C   . THR B 2 91  ? 158.241 152.346 110.765 1.00 47.31  ? 207 THR D C   1 
ATOM   4889 O O   . THR B 2 91  ? 157.570 151.311 110.700 1.00 53.29  ? 207 THR D O   1 
ATOM   4890 C CB  . THR B 2 91  ? 159.614 152.237 108.661 1.00 54.26  ? 207 THR D CB  1 
ATOM   4891 O OG1 . THR B 2 91  ? 158.985 153.381 108.069 1.00 50.58  ? 207 THR D OG1 1 
ATOM   4892 C CG2 . THR B 2 91  ? 158.864 150.973 108.262 1.00 53.86  ? 207 THR D CG2 1 
ATOM   4893 N N   . ALA B 2 92  ? 157.798 153.457 111.338 1.00 37.64  ? 208 ALA D N   1 
ATOM   4894 C CA  . ALA B 2 92  ? 156.526 153.516 112.051 1.00 29.38  ? 208 ALA D CA  1 
ATOM   4895 C C   . ALA B 2 92  ? 156.174 154.983 112.267 1.00 26.46  ? 208 ALA D C   1 
ATOM   4896 O O   . ALA B 2 92  ? 156.878 155.884 111.795 1.00 30.70  ? 208 ALA D O   1 
ATOM   4897 C CB  . ALA B 2 92  ? 156.599 152.752 113.374 1.00 31.34  ? 208 ALA D CB  1 
ATOM   4898 N N   . VAL B 2 93  ? 155.079 155.220 112.982 1.00 26.11  ? 209 VAL D N   1 
ATOM   4899 C CA  . VAL B 2 93  ? 154.676 156.554 113.410 1.00 26.72  ? 209 VAL D CA  1 
ATOM   4900 C C   . VAL B 2 93  ? 154.796 156.598 114.926 1.00 23.31  ? 209 VAL D C   1 
ATOM   4901 O O   . VAL B 2 93  ? 154.104 155.854 115.632 1.00 25.59  ? 209 VAL D O   1 
ATOM   4902 C CB  . VAL B 2 93  ? 153.250 156.895 112.955 1.00 25.67  ? 209 VAL D CB  1 
ATOM   4903 C CG1 . VAL B 2 93  ? 152.879 158.300 113.392 1.00 22.78  ? 209 VAL D CG1 1 
ATOM   4904 C CG2 . VAL B 2 93  ? 153.126 156.750 111.448 1.00 32.73  ? 209 VAL D CG2 1 
ATOM   4905 N N   . TYR B 2 94  ? 155.670 157.464 115.425 1.00 21.39  ? 210 TYR D N   1 
ATOM   4906 C CA  . TYR B 2 94  ? 155.985 157.529 116.845 1.00 16.87  ? 210 TYR D CA  1 
ATOM   4907 C C   . TYR B 2 94  ? 155.195 158.661 117.486 1.00 18.45  ? 210 TYR D C   1 
ATOM   4908 O O   . TYR B 2 94  ? 155.311 159.819 117.070 1.00 30.00  ? 210 TYR D O   1 
ATOM   4909 C CB  . TYR B 2 94  ? 157.486 157.723 117.055 1.00 17.66  ? 210 TYR D CB  1 
ATOM   4910 C CG  . TYR B 2 94  ? 158.312 156.579 116.517 1.00 21.38  ? 210 TYR D CG  1 
ATOM   4911 C CD1 . TYR B 2 94  ? 158.494 155.421 117.259 1.00 23.45  ? 210 TYR D CD1 1 
ATOM   4912 C CD2 . TYR B 2 94  ? 158.896 156.649 115.260 1.00 23.86  ? 210 TYR D CD2 1 
ATOM   4913 C CE1 . TYR B 2 94  ? 159.241 154.370 116.769 1.00 27.92  ? 210 TYR D CE1 1 
ATOM   4914 C CE2 . TYR B 2 94  ? 159.645 155.602 114.763 1.00 26.07  ? 210 TYR D CE2 1 
ATOM   4915 C CZ  . TYR B 2 94  ? 159.814 154.466 115.521 1.00 27.19  ? 210 TYR D CZ  1 
ATOM   4916 O OH  . TYR B 2 94  ? 160.559 153.420 115.029 1.00 39.15  ? 210 TYR D OH  1 
ATOM   4917 N N   . TYR B 2 95  ? 154.396 158.324 118.491 1.00 12.78  ? 211 TYR D N   1 
ATOM   4918 C CA  . TYR B 2 95  ? 153.570 159.282 119.208 1.00 11.54  ? 211 TYR D CA  1 
ATOM   4919 C C   . TYR B 2 95  ? 154.122 159.483 120.610 1.00 12.75  ? 211 TYR D C   1 
ATOM   4920 O O   . TYR B 2 95  ? 154.545 158.524 121.262 1.00 15.65  ? 211 TYR D O   1 
ATOM   4921 C CB  . TYR B 2 95  ? 152.120 158.801 119.302 1.00 13.07  ? 211 TYR D CB  1 
ATOM   4922 C CG  . TYR B 2 95  ? 151.434 158.585 117.974 1.00 20.57  ? 211 TYR D CG  1 
ATOM   4923 C CD1 . TYR B 2 95  ? 150.955 159.656 117.235 1.00 21.69  ? 211 TYR D CD1 1 
ATOM   4924 C CD2 . TYR B 2 95  ? 151.260 157.307 117.463 1.00 14.42  ? 211 TYR D CD2 1 
ATOM   4925 C CE1 . TYR B 2 95  ? 150.325 159.461 116.024 1.00 17.65  ? 211 TYR D CE1 1 
ATOM   4926 C CE2 . TYR B 2 95  ? 150.633 157.103 116.252 1.00 15.46  ? 211 TYR D CE2 1 
ATOM   4927 C CZ  . TYR B 2 95  ? 150.167 158.183 115.537 1.00 19.45  ? 211 TYR D CZ  1 
ATOM   4928 O OH  . TYR B 2 95  ? 149.541 157.984 114.329 1.00 26.42  ? 211 TYR D OH  1 
ATOM   4929 N N   . CYS B 2 96  ? 154.121 160.730 121.073 1.00 13.45  ? 212 CYS D N   1 
ATOM   4930 C CA  . CYS B 2 96  ? 154.439 161.037 122.465 1.00 10.83  ? 212 CYS D CA  1 
ATOM   4931 C C   . CYS B 2 96  ? 153.111 161.272 123.177 1.00 13.69  ? 212 CYS D C   1 
ATOM   4932 O O   . CYS B 2 96  ? 152.538 162.359 123.137 1.00 26.54  ? 212 CYS D O   1 
ATOM   4933 C CB  . CYS B 2 96  ? 155.385 162.229 122.582 1.00 14.03  ? 212 CYS D CB  1 
ATOM   4934 S SG  . CYS B 2 96  ? 154.783 163.811 121.957 1.00 27.80  ? 212 CYS D SG  1 
ATOM   4935 N N   . ALA B 2 97  ? 152.608 160.227 123.816 1.00 7.81   ? 213 ALA D N   1 
ATOM   4936 C CA  . ALA B 2 97  ? 151.347 160.319 124.533 1.00 6.46   ? 213 ALA D CA  1 
ATOM   4937 C C   . ALA B 2 97  ? 151.603 160.897 125.924 1.00 11.40  ? 213 ALA D C   1 
ATOM   4938 O O   . ALA B 2 97  ? 152.701 161.364 126.236 1.00 17.44  ? 213 ALA D O   1 
ATOM   4939 C CB  . ALA B 2 97  ? 150.674 158.954 124.572 1.00 5.94   ? 213 ALA D CB  1 
ATOM   4940 N N   . ARG B 2 98  ? 150.587 160.876 126.782 1.00 9.82   ? 214 ARG D N   1 
ATOM   4941 C CA  . ARG B 2 98  ? 150.703 161.476 128.108 1.00 6.36   ? 214 ARG D CA  1 
ATOM   4942 C C   . ARG B 2 98  ? 149.745 160.752 129.042 1.00 8.13   ? 214 ARG D C   1 
ATOM   4943 O O   . ARG B 2 98  ? 148.526 160.882 128.900 1.00 11.52  ? 214 ARG D O   1 
ATOM   4944 C CB  . ARG B 2 98  ? 150.402 162.970 128.056 1.00 8.08   ? 214 ARG D CB  1 
ATOM   4945 C CG  . ARG B 2 98  ? 150.636 163.704 129.359 1.00 9.64   ? 214 ARG D CG  1 
ATOM   4946 C CD  . ARG B 2 98  ? 149.848 164.999 129.397 1.00 9.71   ? 214 ARG D CD  1 
ATOM   4947 N NE  . ARG B 2 98  ? 148.533 164.813 129.997 1.00 8.15   ? 214 ARG D NE  1 
ATOM   4948 C CZ  . ARG B 2 98  ? 147.737 165.801 130.379 1.00 12.41  ? 214 ARG D CZ  1 
ATOM   4949 N NH1 . ARG B 2 98  ? 148.087 167.067 130.231 1.00 15.75  ? 214 ARG D NH1 1 
ATOM   4950 N NH2 . ARG B 2 98  ? 146.559 165.510 130.923 1.00 13.77  ? 214 ARG D NH2 1 
ATOM   4951 N N   . SER B 2 99  ? 150.292 159.999 129.991 1.00 6.77   ? 215 SER D N   1 
ATOM   4952 C CA  . SER B 2 99  ? 149.465 159.224 130.904 1.00 8.41   ? 215 SER D CA  1 
ATOM   4953 C C   . SER B 2 99  ? 148.651 160.138 131.810 1.00 13.62  ? 215 SER D C   1 
ATOM   4954 O O   . SER B 2 99  ? 149.148 161.151 132.310 1.00 15.36  ? 215 SER D O   1 
ATOM   4955 C CB  . SER B 2 99  ? 150.335 158.294 131.748 1.00 9.34   ? 215 SER D CB  1 
ATOM   4956 O OG  . SER B 2 99  ? 149.555 157.304 132.393 1.00 8.72   ? 215 SER D OG  1 
ATOM   4957 N N   . GLY B 2 100 ? 147.385 159.779 132.020 1.00 12.26  ? 216 GLY D N   1 
ATOM   4958 C CA  . GLY B 2 100 ? 146.543 160.557 132.942 1.00 9.60   ? 216 GLY D CA  1 
ATOM   4959 C C   . GLY B 2 100 ? 146.462 159.854 134.276 1.00 9.31   ? 216 GLY D C   1 
ATOM   4960 O O   . GLY B 2 100 ? 147.472 159.258 134.691 1.00 10.75  ? 216 GLY D O   1 
ATOM   4961 N N   . GLY B 2 101 ? 145.299 159.908 134.920 1.00 10.13  ? 217 GLY D N   1 
ATOM   4962 C CA  . GLY B 2 101 ? 145.118 159.233 136.217 1.00 12.83  ? 217 GLY D CA  1 
ATOM   4963 C C   . GLY B 2 101 ? 144.262 157.995 136.074 1.00 14.28  ? 217 GLY D C   1 
ATOM   4964 O O   . GLY B 2 101 ? 144.775 156.888 136.337 1.00 18.67  ? 217 GLY D O   1 
ATOM   4965 N N   . PRO B 2 102 ? 142.971 158.086 135.671 1.00 17.09  ? 218 PRO D N   1 
ATOM   4966 C CA  . PRO B 2 102 ? 142.181 156.885 135.447 1.00 17.55  ? 218 PRO D CA  1 
ATOM   4967 C C   . PRO B 2 102 ? 142.372 156.330 134.047 1.00 18.23  ? 218 PRO D C   1 
ATOM   4968 O O   . PRO B 2 102 ? 141.996 155.171 133.796 1.00 20.27  ? 218 PRO D O   1 
ATOM   4969 C CB  . PRO B 2 102 ? 140.757 157.397 135.681 1.00 20.47  ? 218 PRO D CB  1 
ATOM   4970 C CG  . PRO B 2 102 ? 140.786 158.818 135.179 1.00 16.32  ? 218 PRO D CG  1 
ATOM   4971 C CD  . PRO B 2 102 ? 142.193 159.313 135.453 1.00 15.17  ? 218 PRO D CD  1 
ATOM   4972 N N   . TYR B 2 103 ? 142.957 157.126 133.153 1.00 15.73  ? 219 TYR D N   1 
ATOM   4973 C CA  . TYR B 2 103 ? 143.095 156.688 131.742 1.00 12.03  ? 219 TYR D CA  1 
ATOM   4974 C C   . TYR B 2 103 ? 144.540 156.745 131.304 1.00 13.52  ? 219 TYR D C   1 
ATOM   4975 O O   . TYR B 2 103 ? 145.407 157.205 132.069 1.00 17.19  ? 219 TYR D O   1 
ATOM   4976 C CB  . TYR B 2 103 ? 142.297 157.601 130.810 1.00 13.22  ? 219 TYR D CB  1 
ATOM   4977 C CG  . TYR B 2 103 ? 142.155 159.048 131.257 1.00 14.59  ? 219 TYR D CG  1 
ATOM   4978 C CD1 . TYR B 2 103 ? 143.165 159.972 131.027 1.00 15.76  ? 219 TYR D CD1 1 
ATOM   4979 C CD2 . TYR B 2 103 ? 140.994 159.497 131.873 1.00 17.50  ? 219 TYR D CD2 1 
ATOM   4980 C CE1 . TYR B 2 103 ? 143.036 161.290 131.428 1.00 20.58  ? 219 TYR D CE1 1 
ATOM   4981 C CE2 . TYR B 2 103 ? 140.852 160.814 132.274 1.00 14.19  ? 219 TYR D CE2 1 
ATOM   4982 C CZ  . TYR B 2 103 ? 141.877 161.714 132.049 1.00 17.99  ? 219 TYR D CZ  1 
ATOM   4983 O OH  . TYR B 2 103 ? 141.748 163.016 132.438 1.00 22.96  ? 219 TYR D OH  1 
ATOM   4984 N N   . PHE B 2 104 ? 144.797 156.282 130.082 1.00 12.82  ? 220 PHE D N   1 
ATOM   4985 C CA  . PHE B 2 104 ? 146.168 156.357 129.514 1.00 9.26   ? 220 PHE D CA  1 
ATOM   4986 C C   . PHE B 2 104 ? 146.160 157.257 128.292 1.00 8.49   ? 220 PHE D C   1 
ATOM   4987 O O   . PHE B 2 104 ? 145.123 157.309 127.594 1.00 11.32  ? 220 PHE D O   1 
ATOM   4988 C CB  . PHE B 2 104 ? 146.649 154.986 129.035 1.00 11.32  ? 220 PHE D CB  1 
ATOM   4989 C CG  . PHE B 2 104 ? 147.392 154.116 130.040 1.00 9.03   ? 220 PHE D CG  1 
ATOM   4990 C CD1 . PHE B 2 104 ? 146.707 153.227 130.860 1.00 10.19  ? 220 PHE D CD1 1 
ATOM   4991 C CD2 . PHE B 2 104 ? 148.778 154.167 130.135 1.00 5.97   ? 220 PHE D CD2 1 
ATOM   4992 C CE1 . PHE B 2 104 ? 147.389 152.426 131.761 1.00 11.87  ? 220 PHE D CE1 1 
ATOM   4993 C CE2 . PHE B 2 104 ? 149.454 153.363 131.038 1.00 5.94   ? 220 PHE D CE2 1 
ATOM   4994 C CZ  . PHE B 2 104 ? 148.760 152.494 131.846 1.00 7.60   ? 220 PHE D CZ  1 
ATOM   4995 N N   . PHE B 2 105 ? 147.266 157.960 128.042 1.00 8.76   ? 221 PHE D N   1 
ATOM   4996 C CA  . PHE B 2 105 ? 147.393 158.764 126.797 1.00 8.42   ? 221 PHE D CA  1 
ATOM   4997 C C   . PHE B 2 105 ? 146.156 159.631 126.574 1.00 9.80   ? 221 PHE D C   1 
ATOM   4998 O O   . PHE B 2 105 ? 145.517 159.495 125.508 1.00 8.60   ? 221 PHE D O   1 
ATOM   4999 C CB  . PHE B 2 105 ? 147.595 157.786 125.636 1.00 7.45   ? 221 PHE D CB  1 
ATOM   5000 C CG  . PHE B 2 105 ? 148.456 156.564 125.929 1.00 9.55   ? 221 PHE D CG  1 
ATOM   5001 C CD1 . PHE B 2 105 ? 149.542 156.633 126.796 1.00 9.22   ? 221 PHE D CD1 1 
ATOM   5002 C CD2 . PHE B 2 105 ? 148.166 155.338 125.342 1.00 8.23   ? 221 PHE D CD2 1 
ATOM   5003 C CE1 . PHE B 2 105 ? 150.312 155.512 127.060 1.00 8.79   ? 221 PHE D CE1 1 
ATOM   5004 C CE2 . PHE B 2 105 ? 148.942 154.223 125.608 1.00 8.75   ? 221 PHE D CE2 1 
ATOM   5005 C CZ  . PHE B 2 105 ? 150.013 154.310 126.465 1.00 9.60   ? 221 PHE D CZ  1 
ATOM   5006 N N   . ASP B 2 106 ? 145.819 160.496 127.535 1.00 11.69  ? 222 ASP D N   1 
ATOM   5007 C CA  . ASP B 2 106 ? 144.691 161.441 127.336 1.00 11.89  ? 222 ASP D CA  1 
ATOM   5008 C C   . ASP B 2 106 ? 144.999 162.283 126.098 1.00 12.60  ? 222 ASP D C   1 
ATOM   5009 O O   . ASP B 2 106 ? 144.145 162.329 125.188 1.00 13.20  ? 222 ASP D O   1 
ATOM   5010 C CB  . ASP B 2 106 ? 144.503 162.311 128.564 1.00 12.12  ? 222 ASP D CB  1 
ATOM   5011 C CG  . ASP B 2 106 ? 145.779 162.638 129.325 1.00 12.12  ? 222 ASP D CG  1 
ATOM   5012 O OD1 . ASP B 2 106 ? 146.731 163.128 128.688 1.00 15.44  ? 222 ASP D OD1 1 
ATOM   5013 O OD2 . ASP B 2 106 ? 145.806 162.414 130.549 1.00 11.74  ? 222 ASP D OD2 1 
ATOM   5014 N N   . TYR B 2 107 ? 146.175 162.917 126.066 1.00 8.35   ? 223 TYR D N   1 
ATOM   5015 C CA  . TYR B 2 107 ? 146.566 163.747 124.936 1.00 10.51  ? 223 TYR D CA  1 
ATOM   5016 C C   . TYR B 2 107 ? 147.738 163.111 124.203 1.00 9.61   ? 223 TYR D C   1 
ATOM   5017 O O   . TYR B 2 107 ? 148.675 162.605 124.828 1.00 9.57   ? 223 TYR D O   1 
ATOM   5018 C CB  . TYR B 2 107 ? 146.934 165.170 125.377 1.00 14.17  ? 223 TYR D CB  1 
ATOM   5019 C CG  . TYR B 2 107 ? 145.862 165.878 126.180 1.00 15.68  ? 223 TYR D CG  1 
ATOM   5020 C CD1 . TYR B 2 107 ? 145.737 165.675 127.545 1.00 18.23  ? 223 TYR D CD1 1 
ATOM   5021 C CD2 . TYR B 2 107 ? 144.989 166.767 125.570 1.00 16.13  ? 223 TYR D CD2 1 
ATOM   5022 C CE1 . TYR B 2 107 ? 144.764 166.321 128.279 1.00 21.00  ? 223 TYR D CE1 1 
ATOM   5023 C CE2 . TYR B 2 107 ? 144.012 167.419 126.295 1.00 23.35  ? 223 TYR D CE2 1 
ATOM   5024 C CZ  . TYR B 2 107 ? 143.906 167.192 127.650 1.00 24.19  ? 223 TYR D CZ  1 
ATOM   5025 O OH  . TYR B 2 107 ? 142.937 167.839 128.381 1.00 34.96  ? 223 TYR D OH  1 
ATOM   5026 N N   . TRP B 2 108 ? 147.675 163.141 122.876 1.00 11.27  ? 224 TRP D N   1 
ATOM   5027 C CA  . TRP B 2 108 ? 148.685 162.553 122.012 1.00 8.82   ? 224 TRP D CA  1 
ATOM   5028 C C   . TRP B 2 108 ? 149.383 163.638 121.205 1.00 11.85  ? 224 TRP D C   1 
ATOM   5029 O O   . TRP B 2 108 ? 148.801 164.684 120.907 1.00 19.51  ? 224 TRP D O   1 
ATOM   5030 C CB  . TRP B 2 108 ? 148.065 161.541 121.042 1.00 6.62   ? 224 TRP D CB  1 
ATOM   5031 C CG  . TRP B 2 108 ? 147.519 160.306 121.678 1.00 6.32   ? 224 TRP D CG  1 
ATOM   5032 C CD1 . TRP B 2 108 ? 146.478 160.225 122.553 1.00 6.04   ? 224 TRP D CD1 1 
ATOM   5033 C CD2 . TRP B 2 108 ? 147.970 158.965 121.465 1.00 5.58   ? 224 TRP D CD2 1 
ATOM   5034 N NE1 . TRP B 2 108 ? 146.259 158.918 122.908 1.00 5.18   ? 224 TRP D NE1 1 
ATOM   5035 C CE2 . TRP B 2 108 ? 147.163 158.124 122.253 1.00 4.80   ? 224 TRP D CE2 1 
ATOM   5036 C CE3 . TRP B 2 108 ? 148.982 158.395 120.689 1.00 5.63   ? 224 TRP D CE3 1 
ATOM   5037 C CZ2 . TRP B 2 108 ? 147.337 156.743 122.288 1.00 4.83   ? 224 TRP D CZ2 1 
ATOM   5038 C CZ3 . TRP B 2 108 ? 149.152 157.025 120.725 1.00 6.58   ? 224 TRP D CZ3 1 
ATOM   5039 C CH2 . TRP B 2 108 ? 148.334 156.215 121.519 1.00 4.52   ? 224 TRP D CH2 1 
ATOM   5040 N N   . GLY B 2 109 ? 150.617 163.343 120.798 1.00 8.61   ? 225 GLY D N   1 
ATOM   5041 C CA  . GLY B 2 109 ? 151.332 164.277 119.916 1.00 13.67  ? 225 GLY D CA  1 
ATOM   5042 C C   . GLY B 2 109 ? 150.864 164.044 118.499 1.00 19.05  ? 225 GLY D C   1 
ATOM   5043 O O   . GLY B 2 109 ? 150.341 162.947 118.234 1.00 25.54  ? 225 GLY D O   1 
ATOM   5044 N N   . GLN B 2 110 ? 151.047 165.017 117.606 1.00 20.68  ? 226 GLN D N   1 
ATOM   5045 C CA  . GLN B 2 110 ? 150.502 164.873 116.232 1.00 18.70  ? 226 GLN D CA  1 
ATOM   5046 C C   . GLN B 2 110 ? 151.006 163.549 115.635 1.00 22.98  ? 226 GLN D C   1 
ATOM   5047 O O   . GLN B 2 110 ? 150.208 162.867 114.960 1.00 25.65  ? 226 GLN D O   1 
ATOM   5048 C CB  . GLN B 2 110 ? 150.862 166.097 115.384 1.00 20.61  ? 226 GLN D CB  1 
ATOM   5049 C CG  . GLN B 2 110 ? 152.180 165.995 114.625 1.00 19.52  ? 226 GLN D CG  1 
ATOM   5050 C CD  . GLN B 2 110 ? 153.389 166.331 115.468 1.00 25.26  ? 226 GLN D CD  1 
ATOM   5051 O OE1 . GLN B 2 110 ? 153.276 166.692 116.644 1.00 25.91  ? 226 GLN D OE1 1 
ATOM   5052 N NE2 . GLN B 2 110 ? 154.564 166.225 114.864 1.00 25.95  ? 226 GLN D NE2 1 
ATOM   5053 N N   . GLY B 2 111 ? 152.269 163.198 115.885 1.00 22.41  ? 227 GLY D N   1 
ATOM   5054 C CA  . GLY B 2 111 ? 152.843 161.962 115.325 1.00 16.50  ? 227 GLY D CA  1 
ATOM   5055 C C   . GLY B 2 111 ? 154.109 162.230 114.543 1.00 21.04  ? 227 GLY D C   1 
ATOM   5056 O O   . GLY B 2 111 ? 154.143 163.238 113.810 1.00 27.88  ? 227 GLY D O   1 
ATOM   5057 N N   . THR B 2 112 ? 155.119 161.374 114.694 1.00 21.02  ? 228 THR D N   1 
ATOM   5058 C CA  . THR B 2 112 ? 156.369 161.488 113.953 1.00 29.85  ? 228 THR D CA  1 
ATOM   5059 C C   . THR B 2 112 ? 156.567 160.216 113.144 1.00 34.61  ? 228 THR D C   1 
ATOM   5060 O O   . THR B 2 112 ? 156.719 159.131 113.715 1.00 38.41  ? 228 THR D O   1 
ATOM   5061 C CB  . THR B 2 112 ? 157.556 161.711 114.893 1.00 35.10  ? 228 THR D CB  1 
ATOM   5062 O OG1 . THR B 2 112 ? 157.470 163.017 115.475 1.00 37.45  ? 228 THR D OG1 1 
ATOM   5063 C CG2 . THR B 2 112 ? 158.866 161.587 114.133 1.00 43.10  ? 228 THR D CG2 1 
ATOM   5064 N N   . LEU B 2 113 ? 156.567 160.350 111.821 1.00 36.86  ? 229 LEU D N   1 
ATOM   5065 C CA  . LEU B 2 113 ? 156.751 159.216 110.924 1.00 38.49  ? 229 LEU D CA  1 
ATOM   5066 C C   . LEU B 2 113 ? 158.233 159.101 110.590 1.00 49.08  ? 229 LEU D C   1 
ATOM   5067 O O   . LEU B 2 113 ? 158.768 159.904 109.819 1.00 59.28  ? 229 LEU D O   1 
ATOM   5068 C CB  . LEU B 2 113 ? 155.909 159.383 109.662 1.00 40.79  ? 229 LEU D CB  1 
ATOM   5069 C CG  . LEU B 2 113 ? 156.238 158.475 108.475 1.00 42.81  ? 229 LEU D CG  1 
ATOM   5070 C CD1 . LEU B 2 113 ? 155.542 157.132 108.610 1.00 37.75  ? 229 LEU D CD1 1 
ATOM   5071 C CD2 . LEU B 2 113 ? 155.857 159.149 107.167 1.00 42.93  ? 229 LEU D CD2 1 
ATOM   5072 N N   . VAL B 2 114 ? 158.898 158.113 111.177 1.00 46.87  ? 230 VAL D N   1 
ATOM   5073 C CA  . VAL B 2 114 ? 160.311 157.856 110.913 1.00 56.06  ? 230 VAL D CA  1 
ATOM   5074 C C   . VAL B 2 114 ? 160.347 156.709 109.909 1.00 54.94  ? 230 VAL D C   1 
ATOM   5075 O O   . VAL B 2 114 ? 160.362 155.532 110.270 1.00 49.60  ? 230 VAL D O   1 
ATOM   5076 C CB  . VAL B 2 114 ? 161.085 157.540 112.191 1.00 57.34  ? 230 VAL D CB  1 
ATOM   5077 C CG1 . VAL B 2 114 ? 162.543 157.241 111.870 1.00 56.88  ? 230 VAL D CG1 1 
ATOM   5078 C CG2 . VAL B 2 114 ? 160.980 158.700 113.168 1.00 52.90  ? 230 VAL D CG2 1 
ATOM   5079 N N   . THR B 2 115 ? 160.356 157.062 108.627 1.00 58.72  ? 231 THR D N   1 
ATOM   5080 C CA  . THR B 2 115 ? 160.372 156.079 107.550 1.00 64.88  ? 231 THR D CA  1 
ATOM   5081 C C   . THR B 2 115 ? 161.818 155.683 107.279 1.00 71.96  ? 231 THR D C   1 
ATOM   5082 O O   . THR B 2 115 ? 162.621 156.503 106.823 1.00 73.41  ? 231 THR D O   1 
ATOM   5083 C CB  . THR B 2 115 ? 159.711 156.634 106.292 1.00 64.28  ? 231 THR D CB  1 
ATOM   5084 O OG1 . THR B 2 115 ? 158.304 156.790 106.518 1.00 59.47  ? 231 THR D OG1 1 
ATOM   5085 C CG2 . THR B 2 115 ? 159.926 155.687 105.121 1.00 59.93  ? 231 THR D CG2 1 
ATOM   5086 N N   . VAL B 2 116 ? 162.147 154.427 107.565 1.00 75.69  ? 232 VAL D N   1 
ATOM   5087 C CA  . VAL B 2 116 ? 163.490 153.896 107.378 1.00 75.51  ? 232 VAL D CA  1 
ATOM   5088 C C   . VAL B 2 116 ? 163.395 152.595 106.589 1.00 82.07  ? 232 VAL D C   1 
ATOM   5089 O O   . VAL B 2 116 ? 162.495 151.778 106.817 1.00 81.00  ? 232 VAL D O   1 
ATOM   5090 C CB  . VAL B 2 116 ? 164.214 153.703 108.731 1.00 71.82  ? 232 VAL D CB  1 
ATOM   5091 C CG1 . VAL B 2 116 ? 163.888 152.367 109.356 1.00 67.74  ? 232 VAL D CG1 1 
ATOM   5092 C CG2 . VAL B 2 116 ? 165.712 153.843 108.554 1.00 79.39  ? 232 VAL D CG2 1 
ATOM   5093 N N   . SER B 2 117 ? 164.287 152.438 105.613 1.00 88.49  ? 233 SER D N   1 
ATOM   5094 C CA  . SER B 2 117 ? 164.292 151.254 104.768 1.00 97.57  ? 233 SER D CA  1 
ATOM   5095 C C   . SER B 2 117 ? 165.677 151.075 104.165 1.00 98.57  ? 233 SER D C   1 
ATOM   5096 O O   . SER B 2 117 ? 166.475 152.013 104.100 1.00 92.40  ? 233 SER D O   1 
ATOM   5097 C CB  . SER B 2 117 ? 163.236 151.345 103.660 1.00 93.70  ? 233 SER D CB  1 
ATOM   5098 O OG  . SER B 2 117 ? 161.925 151.296 104.197 1.00 84.77  ? 233 SER D OG  1 
ATOM   5099 N N   . SER B 2 118 ? 165.946 149.855 103.711 1.00 103.31 ? 234 SER D N   1 
ATOM   5100 C CA  . SER B 2 118 ? 167.227 149.529 103.093 1.00 103.53 ? 234 SER D CA  1 
ATOM   5101 C C   . SER B 2 118 ? 167.349 150.165 101.713 1.00 106.99 ? 234 SER D C   1 
ATOM   5102 O O   . SER B 2 118 ? 168.222 151.000 101.478 1.00 105.56 ? 234 SER D O   1 
ATOM   5103 C CB  . SER B 2 118 ? 167.402 148.012 102.990 1.00 96.23  ? 234 SER D CB  1 
ATOM   5104 O OG  . SER B 2 118 ? 166.369 147.429 102.214 1.00 89.30  ? 234 SER D OG  1 
ATOM   5105 N N   . ASP B 2 139 ? 154.134 139.480 127.401 1.00 51.47  ? 255 ASP D N   1 
ATOM   5106 C CA  . ASP B 2 139 ? 153.246 140.551 126.967 1.00 53.89  ? 255 ASP D CA  1 
ATOM   5107 C C   . ASP B 2 139 ? 151.832 140.031 126.734 1.00 50.97  ? 255 ASP D C   1 
ATOM   5108 O O   . ASP B 2 139 ? 151.638 139.013 126.070 1.00 46.84  ? 255 ASP D O   1 
ATOM   5109 C CB  . ASP B 2 139 ? 153.779 141.207 125.692 1.00 53.10  ? 255 ASP D CB  1 
ATOM   5110 C CG  . ASP B 2 139 ? 155.168 141.783 125.870 1.00 56.86  ? 255 ASP D CG  1 
ATOM   5111 O OD1 . ASP B 2 139 ? 155.823 141.457 126.882 1.00 57.75  ? 255 ASP D OD1 1 
ATOM   5112 O OD2 . ASP B 2 139 ? 155.606 142.563 124.999 1.00 57.17  ? 255 ASP D OD2 1 
ATOM   5113 N N   . ILE B 2 140 ? 150.847 140.735 127.286 1.00 51.52  ? 256 ILE D N   1 
ATOM   5114 C CA  . ILE B 2 140 ? 149.448 140.359 127.107 1.00 52.47  ? 256 ILE D CA  1 
ATOM   5115 C C   . ILE B 2 140 ? 149.053 140.681 125.670 1.00 49.82  ? 256 ILE D C   1 
ATOM   5116 O O   . ILE B 2 140 ? 149.038 141.847 125.268 1.00 46.01  ? 256 ILE D O   1 
ATOM   5117 C CB  . ILE B 2 140 ? 148.538 141.078 128.109 1.00 47.48  ? 256 ILE D CB  1 
ATOM   5118 C CG1 . ILE B 2 140 ? 148.835 140.607 129.534 1.00 54.03  ? 256 ILE D CG1 1 
ATOM   5119 C CG2 . ILE B 2 140 ? 147.077 140.848 127.758 1.00 41.76  ? 256 ILE D CG2 1 
ATOM   5120 C CD1 . ILE B 2 140 ? 147.806 141.049 130.552 1.00 54.92  ? 256 ILE D CD1 1 
ATOM   5121 N N   . VAL B 2 141 ? 148.733 139.651 124.893 1.00 50.45  ? 257 VAL D N   1 
ATOM   5122 C CA  . VAL B 2 141 ? 148.335 139.839 123.502 1.00 50.36  ? 257 VAL D CA  1 
ATOM   5123 C C   . VAL B 2 141 ? 146.856 140.198 123.466 1.00 50.72  ? 257 VAL D C   1 
ATOM   5124 O O   . VAL B 2 141 ? 146.007 139.433 123.936 1.00 53.08  ? 257 VAL D O   1 
ATOM   5125 C CB  . VAL B 2 141 ? 148.621 138.583 122.667 1.00 55.23  ? 257 VAL D CB  1 
ATOM   5126 C CG1 . VAL B 2 141 ? 148.021 138.724 121.277 1.00 51.53  ? 257 VAL D CG1 1 
ATOM   5127 C CG2 . VAL B 2 141 ? 150.119 138.335 122.583 1.00 45.30  ? 257 VAL D CG2 1 
ATOM   5128 N N   . MET B 2 142 ? 146.578 141.407 122.962 1.00 51.26  ? 258 MET D N   1 
ATOM   5129 C CA  . MET B 2 142 ? 145.180 141.891 122.841 1.00 50.71  ? 258 MET D CA  1 
ATOM   5130 C C   . MET B 2 142 ? 144.778 141.783 121.369 1.00 47.79  ? 258 MET D C   1 
ATOM   5131 O O   . MET B 2 142 ? 145.367 142.504 120.539 1.00 46.54  ? 258 MET D O   1 
ATOM   5132 C CB  . MET B 2 142 ? 145.057 143.353 123.284 1.00 39.54  ? 258 MET D CB  1 
ATOM   5133 C CG  . MET B 2 142 ? 145.620 143.641 124.658 1.00 35.05  ? 258 MET D CG  1 
ATOM   5134 S SD  . MET B 2 142 ? 144.466 143.206 125.973 1.00 35.55  ? 258 MET D SD  1 
ATOM   5135 C CE  . MET B 2 142 ? 143.082 144.269 125.543 1.00 29.73  ? 258 MET D CE  1 
ATOM   5136 N N   . THR B 2 143 ? 143.803 140.927 121.056 1.00 55.27  ? 259 THR D N   1 
ATOM   5137 C CA  . THR B 2 143 ? 143.383 140.725 119.650 1.00 58.20  ? 259 THR D CA  1 
ATOM   5138 C C   . THR B 2 143 ? 141.911 141.046 119.513 1.00 57.60  ? 259 THR D C   1 
ATOM   5139 O O   . THR B 2 143 ? 141.113 140.536 120.319 1.00 59.57  ? 259 THR D O   1 
ATOM   5140 C CB  . THR B 2 143 ? 143.694 139.293 119.213 1.00 59.48  ? 259 THR D CB  1 
ATOM   5141 O OG1 . THR B 2 143 ? 142.886 139.074 118.061 1.00 50.87  ? 259 THR D OG1 1 
ATOM   5142 C CG2 . THR B 2 143 ? 143.359 138.265 120.279 1.00 55.40  ? 259 THR D CG2 1 
ATOM   5143 N N   . GLN B 2 144 ? 141.557 141.857 118.516 1.00 55.83  ? 260 GLN D N   1 
ATOM   5144 C CA  . GLN B 2 144 ? 140.137 142.225 118.290 1.00 52.00  ? 260 GLN D CA  1 
ATOM   5145 C C   . GLN B 2 144 ? 139.495 141.194 117.351 1.00 58.75  ? 260 GLN D C   1 
ATOM   5146 O O   . GLN B 2 144 ? 140.045 140.979 116.252 1.00 62.11  ? 260 GLN D O   1 
ATOM   5147 C CB  . GLN B 2 144 ? 140.136 143.653 117.749 1.00 50.95  ? 260 GLN D CB  1 
ATOM   5148 C CG  . GLN B 2 144 ? 140.711 144.665 118.733 1.00 44.82  ? 260 GLN D CG  1 
ATOM   5149 C CD  . GLN B 2 144 ? 140.827 146.058 118.160 1.00 37.53  ? 260 GLN D CD  1 
ATOM   5150 O OE1 . GLN B 2 144 ? 141.910 146.650 118.122 1.00 39.10  ? 260 GLN D OE1 1 
ATOM   5151 N NE2 . GLN B 2 144 ? 139.704 146.594 117.706 1.00 28.86  ? 260 GLN D NE2 1 
ATOM   5152 N N   . SER B 2 145 ? 138.389 140.575 117.775 1.00 62.68  ? 261 SER D N   1 
ATOM   5153 C CA  . SER B 2 145 ? 137.752 139.539 116.962 1.00 63.77  ? 261 SER D CA  1 
ATOM   5154 C C   . SER B 2 145 ? 137.361 140.033 115.573 1.00 64.66  ? 261 SER D C   1 
ATOM   5155 O O   . SER B 2 145 ? 137.655 139.330 114.591 1.00 63.31  ? 261 SER D O   1 
ATOM   5156 C CB  . SER B 2 145 ? 136.555 138.953 117.718 1.00 63.79  ? 261 SER D CB  1 
ATOM   5157 O OG  . SER B 2 145 ? 136.931 138.522 119.015 1.00 62.39  ? 261 SER D OG  1 
ATOM   5158 N N   . PRO B 2 146 ? 136.717 141.187 115.402 1.00 63.82  ? 262 PRO D N   1 
ATOM   5159 C CA  . PRO B 2 146 ? 136.517 141.719 114.052 1.00 62.82  ? 262 PRO D CA  1 
ATOM   5160 C C   . PRO B 2 146 ? 137.800 142.346 113.523 1.00 67.25  ? 262 PRO D C   1 
ATOM   5161 O O   . PRO B 2 146 ? 138.772 142.553 114.249 1.00 65.80  ? 262 PRO D O   1 
ATOM   5162 C CB  . PRO B 2 146 ? 135.415 142.775 114.228 1.00 50.46  ? 262 PRO D CB  1 
ATOM   5163 C CG  . PRO B 2 146 ? 134.888 142.584 115.617 1.00 52.01  ? 262 PRO D CG  1 
ATOM   5164 C CD  . PRO B 2 146 ? 136.017 142.013 116.401 1.00 59.05  ? 262 PRO D CD  1 
ATOM   5165 N N   . LEU B 2 147 ? 137.789 142.633 112.220 1.00 67.71  ? 263 LEU D N   1 
ATOM   5166 C CA  . LEU B 2 147 ? 138.961 143.278 111.579 1.00 66.10  ? 263 LEU D CA  1 
ATOM   5167 C C   . LEU B 2 147 ? 138.462 144.009 110.327 1.00 66.19  ? 263 LEU D C   1 
ATOM   5168 O O   . LEU B 2 147 ? 137.951 143.329 109.412 1.00 71.76  ? 263 LEU D O   1 
ATOM   5169 C CB  . LEU B 2 147 ? 140.050 142.258 111.252 1.00 74.24  ? 263 LEU D CB  1 
ATOM   5170 C CG  . LEU B 2 147 ? 141.489 142.704 111.528 1.00 71.50  ? 263 LEU D CG  1 
ATOM   5171 C CD1 . LEU B 2 147 ? 142.479 141.617 111.152 1.00 65.52  ? 263 LEU D CD1 1 
ATOM   5172 C CD2 . LEU B 2 147 ? 141.827 144.007 110.825 1.00 54.65  ? 263 LEU D CD2 1 
ATOM   5173 N N   . SER B 2 148 ? 138.580 145.333 110.305 1.00 60.48  ? 264 SER D N   1 
ATOM   5174 C CA  . SER B 2 148 ? 138.147 146.168 109.182 1.00 65.75  ? 264 SER D CA  1 
ATOM   5175 C C   . SER B 2 148 ? 136.668 145.953 108.871 1.00 66.56  ? 264 SER D C   1 
ATOM   5176 O O   . SER B 2 148 ? 136.267 145.807 107.714 1.00 66.85  ? 264 SER D O   1 
ATOM   5177 C CB  . SER B 2 148 ? 139.008 145.913 107.944 1.00 68.92  ? 264 SER D CB  1 
ATOM   5178 O OG  . SER B 2 148 ? 138.562 144.768 107.240 1.00 67.32  ? 264 SER D OG  1 
ATOM   5179 N N   . LEU B 2 149 ? 135.864 145.892 109.937 1.00 62.41  ? 265 LEU D N   1 
ATOM   5180 C CA  . LEU B 2 149 ? 134.413 145.619 109.771 1.00 69.00  ? 265 LEU D CA  1 
ATOM   5181 C C   . LEU B 2 149 ? 133.724 146.804 109.084 1.00 74.24  ? 265 LEU D C   1 
ATOM   5182 O O   . LEU B 2 149 ? 133.894 147.952 109.549 1.00 67.15  ? 265 LEU D O   1 
ATOM   5183 C CB  . LEU B 2 149 ? 133.777 145.316 111.127 1.00 68.16  ? 265 LEU D CB  1 
ATOM   5184 C CG  . LEU B 2 149 ? 133.833 146.431 112.175 1.00 63.68  ? 265 LEU D CG  1 
ATOM   5185 C CD1 . LEU B 2 149 ? 132.474 146.627 112.822 1.00 65.33  ? 265 LEU D CD1 1 
ATOM   5186 C CD2 . LEU B 2 149 ? 134.870 146.092 113.223 1.00 59.62  ? 265 LEU D CD2 1 
ATOM   5187 N N   . PRO B 2 150 ? 132.980 146.585 107.980 1.00 81.72  ? 266 PRO D N   1 
ATOM   5188 C CA  . PRO B 2 150 ? 132.212 147.660 107.343 1.00 82.03  ? 266 PRO D CA  1 
ATOM   5189 C C   . PRO B 2 150 ? 130.792 147.741 107.881 1.00 85.42  ? 266 PRO D C   1 
ATOM   5190 O O   . PRO B 2 150 ? 130.153 146.733 108.188 1.00 86.17  ? 266 PRO D O   1 
ATOM   5191 C CB  . PRO B 2 150 ? 132.218 147.255 105.861 1.00 82.15  ? 266 PRO D CB  1 
ATOM   5192 C CG  . PRO B 2 150 ? 132.555 145.768 105.841 1.00 76.64  ? 266 PRO D CG  1 
ATOM   5193 C CD  . PRO B 2 150 ? 132.862 145.318 107.244 1.00 75.40  ? 266 PRO D CD  1 
ATOM   5194 N N   . VAL B 2 151 ? 130.293 148.972 107.996 1.00 84.66  ? 267 VAL D N   1 
ATOM   5195 C CA  . VAL B 2 151 ? 128.951 149.234 108.500 1.00 91.09  ? 267 VAL D CA  1 
ATOM   5196 C C   . VAL B 2 151 ? 128.309 150.333 107.663 1.00 89.68  ? 267 VAL D C   1 
ATOM   5197 O O   . VAL B 2 151 ? 128.958 150.991 106.850 1.00 89.92  ? 267 VAL D O   1 
ATOM   5198 C CB  . VAL B 2 151 ? 128.951 149.628 109.992 1.00 90.25  ? 267 VAL D CB  1 
ATOM   5199 C CG1 . VAL B 2 151 ? 129.002 148.387 110.867 1.00 85.40  ? 267 VAL D CG1 1 
ATOM   5200 C CG2 . VAL B 2 151 ? 130.120 150.550 110.296 1.00 83.39  ? 267 VAL D CG2 1 
ATOM   5201 N N   . THR B 2 152 ? 127.008 150.520 107.876 1.00 86.89  ? 268 THR D N   1 
ATOM   5202 C CA  . THR B 2 152 ? 126.217 151.534 107.200 1.00 90.33  ? 268 THR D CA  1 
ATOM   5203 C C   . THR B 2 152 ? 125.971 152.702 108.141 1.00 90.42  ? 268 THR D C   1 
ATOM   5204 O O   . THR B 2 152 ? 125.657 152.477 109.318 1.00 85.80  ? 268 THR D O   1 
ATOM   5205 C CB  . THR B 2 152 ? 124.878 150.944 106.730 1.00 88.82  ? 268 THR D CB  1 
ATOM   5206 O OG1 . THR B 2 152 ? 125.114 149.987 105.690 1.00 91.32  ? 268 THR D OG1 1 
ATOM   5207 C CG2 . THR B 2 152 ? 123.949 152.032 106.207 1.00 81.88  ? 268 THR D CG2 1 
ATOM   5208 N N   . PRO B 2 153 ? 126.124 153.954 107.677 1.00 93.93  ? 269 PRO D N   1 
ATOM   5209 C CA  . PRO B 2 153 ? 125.882 155.109 108.556 1.00 87.83  ? 269 PRO D CA  1 
ATOM   5210 C C   . PRO B 2 153 ? 124.514 155.076 109.218 1.00 85.85  ? 269 PRO D C   1 
ATOM   5211 O O   . PRO B 2 153 ? 123.482 155.148 108.543 1.00 83.76  ? 269 PRO D O   1 
ATOM   5212 C CB  . PRO B 2 153 ? 126.013 156.304 107.605 1.00 82.77  ? 269 PRO D CB  1 
ATOM   5213 C CG  . PRO B 2 153 ? 126.915 155.825 106.525 1.00 86.81  ? 269 PRO D CG  1 
ATOM   5214 C CD  . PRO B 2 153 ? 126.628 154.360 106.353 1.00 91.16  ? 269 PRO D CD  1 
ATOM   5215 N N   . GLY B 2 154 ? 124.501 154.969 110.544 1.00 85.87  ? 270 GLY D N   1 
ATOM   5216 C CA  . GLY B 2 154 ? 123.262 154.874 111.288 1.00 82.15  ? 270 GLY D CA  1 
ATOM   5217 C C   . GLY B 2 154 ? 123.102 153.536 111.978 1.00 79.75  ? 270 GLY D C   1 
ATOM   5218 O O   . GLY B 2 154 ? 122.620 153.467 113.113 1.00 76.19  ? 270 GLY D O   1 
ATOM   5219 N N   . GLU B 2 155 ? 123.503 152.465 111.300 1.00 81.37  ? 271 GLU D N   1 
ATOM   5220 C CA  . GLU B 2 155 ? 123.409 151.139 111.889 1.00 84.38  ? 271 GLU D CA  1 
ATOM   5221 C C   . GLU B 2 155 ? 124.447 150.982 112.998 1.00 82.61  ? 271 GLU D C   1 
ATOM   5222 O O   . GLU B 2 155 ? 125.614 151.342 112.814 1.00 84.29  ? 271 GLU D O   1 
ATOM   5223 C CB  . GLU B 2 155 ? 123.615 150.062 110.823 1.00 89.30  ? 271 GLU D CB  1 
ATOM   5224 C CG  . GLU B 2 155 ? 122.807 148.795 111.056 1.00 89.08  ? 271 GLU D CG  1 
ATOM   5225 C CD  . GLU B 2 155 ? 123.559 147.767 111.877 1.00 91.23  ? 271 GLU D CD  1 
ATOM   5226 O OE1 . GLU B 2 155 ? 124.768 147.574 111.629 1.00 94.07  ? 271 GLU D OE1 1 
ATOM   5227 O OE2 . GLU B 2 155 ? 122.943 147.152 112.772 1.00 85.66  ? 271 GLU D OE2 1 
ATOM   5228 N N   . PRO B 2 156 ? 124.055 150.458 114.159 1.00 83.56  ? 272 PRO D N   1 
ATOM   5229 C CA  . PRO B 2 156 ? 125.021 150.278 115.252 1.00 83.90  ? 272 PRO D CA  1 
ATOM   5230 C C   . PRO B 2 156 ? 126.075 149.239 114.894 1.00 83.22  ? 272 PRO D C   1 
ATOM   5231 O O   . PRO B 2 156 ? 125.776 148.220 114.268 1.00 79.46  ? 272 PRO D O   1 
ATOM   5232 C CB  . PRO B 2 156 ? 124.149 149.817 116.426 1.00 80.99  ? 272 PRO D CB  1 
ATOM   5233 C CG  . PRO B 2 156 ? 122.943 149.216 115.787 1.00 81.84  ? 272 PRO D CG  1 
ATOM   5234 C CD  . PRO B 2 156 ? 122.706 149.996 114.526 1.00 79.75  ? 272 PRO D CD  1 
ATOM   5235 N N   . ALA B 2 157 ? 127.311 149.507 115.299 1.00 71.92  ? 273 ALA D N   1 
ATOM   5236 C CA  . ALA B 2 157 ? 128.418 148.581 115.115 1.00 65.84  ? 273 ALA D CA  1 
ATOM   5237 C C   . ALA B 2 157 ? 128.862 148.019 116.460 1.00 63.02  ? 273 ALA D C   1 
ATOM   5238 O O   . ALA B 2 157 ? 128.446 148.478 117.526 1.00 65.23  ? 273 ALA D O   1 
ATOM   5239 C CB  . ALA B 2 157 ? 129.590 149.268 114.410 1.00 62.97  ? 273 ALA D CB  1 
ATOM   5240 N N   . SER B 2 158 ? 129.724 147.008 116.399 1.00 60.95  ? 274 SER D N   1 
ATOM   5241 C CA  . SER B 2 158 ? 130.227 146.368 117.612 1.00 64.38  ? 274 SER D CA  1 
ATOM   5242 C C   . SER B 2 158 ? 131.598 145.784 117.319 1.00 61.56  ? 274 SER D C   1 
ATOM   5243 O O   . SER B 2 158 ? 131.721 144.888 116.478 1.00 59.74  ? 274 SER D O   1 
ATOM   5244 C CB  . SER B 2 158 ? 129.267 145.282 118.096 1.00 67.83  ? 274 SER D CB  1 
ATOM   5245 O OG  . SER B 2 158 ? 129.619 144.833 119.393 1.00 65.54  ? 274 SER D OG  1 
ATOM   5246 N N   . ILE B 2 159 ? 132.620 146.286 118.006 1.00 54.99  ? 275 ILE D N   1 
ATOM   5247 C CA  . ILE B 2 159 ? 133.986 145.793 117.875 1.00 49.75  ? 275 ILE D CA  1 
ATOM   5248 C C   . ILE B 2 159 ? 134.331 145.029 119.144 1.00 45.62  ? 275 ILE D C   1 
ATOM   5249 O O   . ILE B 2 159 ? 134.382 145.612 120.234 1.00 52.09  ? 275 ILE D O   1 
ATOM   5250 C CB  . ILE B 2 159 ? 134.983 146.936 117.633 1.00 49.00  ? 275 ILE D CB  1 
ATOM   5251 C CG1 . ILE B 2 159 ? 134.669 147.653 116.320 1.00 46.06  ? 275 ILE D CG1 1 
ATOM   5252 C CG2 . ILE B 2 159 ? 136.404 146.404 117.623 1.00 38.66  ? 275 ILE D CG2 1 
ATOM   5253 C CD1 . ILE B 2 159 ? 134.153 149.059 116.506 1.00 36.09  ? 275 ILE D CD1 1 
ATOM   5254 N N   . SER B 2 160 ? 134.562 143.730 119.006 1.00 46.14  ? 276 SER D N   1 
ATOM   5255 C CA  . SER B 2 160 ? 134.969 142.899 120.127 1.00 52.69  ? 276 SER D CA  1 
ATOM   5256 C C   . SER B 2 160 ? 136.490 142.840 120.211 1.00 54.52  ? 276 SER D C   1 
ATOM   5257 O O   . SER B 2 160 ? 137.199 143.011 119.218 1.00 59.97  ? 276 SER D O   1 
ATOM   5258 C CB  . SER B 2 160 ? 134.395 141.489 119.994 1.00 55.66  ? 276 SER D CB  1 
ATOM   5259 O OG  . SER B 2 160 ? 135.061 140.585 120.859 1.00 56.57  ? 276 SER D OG  1 
ATOM   5260 N N   . CYS B 2 161 ? 136.989 142.602 121.421 1.00 52.78  ? 277 CYS D N   1 
ATOM   5261 C CA  . CYS B 2 161 ? 138.421 142.486 121.644 1.00 55.25  ? 277 CYS D CA  1 
ATOM   5262 C C   . CYS B 2 161 ? 138.689 141.364 122.635 1.00 62.98  ? 277 CYS D C   1 
ATOM   5263 O O   . CYS B 2 161 ? 138.001 141.243 123.652 1.00 66.02  ? 277 CYS D O   1 
ATOM   5264 C CB  . CYS B 2 161 ? 139.019 143.802 122.157 1.00 53.56  ? 277 CYS D CB  1 
ATOM   5265 S SG  . CYS B 2 161 ? 140.673 143.628 122.852 1.00 73.40  ? 277 CYS D SG  1 
ATOM   5266 N N   . ARG B 2 162 ? 139.695 140.550 122.330 1.00 63.50  ? 278 ARG D N   1 
ATOM   5267 C CA  . ARG B 2 162 ? 140.057 139.386 123.126 1.00 63.40  ? 278 ARG D CA  1 
ATOM   5268 C C   . ARG B 2 162 ? 141.460 139.592 123.676 1.00 63.53  ? 278 ARG D C   1 
ATOM   5269 O O   . ARG B 2 162 ? 142.370 139.974 122.933 1.00 62.73  ? 278 ARG D O   1 
ATOM   5270 C CB  . ARG B 2 162 ? 139.995 138.114 122.273 1.00 63.05  ? 278 ARG D CB  1 
ATOM   5271 C CG  . ARG B 2 162 ? 138.701 137.319 122.392 1.00 61.37  ? 278 ARG D CG  1 
ATOM   5272 C CD  . ARG B 2 162 ? 138.731 136.321 123.537 1.00 66.40  ? 278 ARG D CD  1 
ATOM   5273 N NE  . ARG B 2 162 ? 140.059 135.754 123.736 1.00 70.32  ? 278 ARG D NE  1 
ATOM   5274 C CZ  . ARG B 2 162 ? 140.523 135.333 124.904 1.00 67.12  ? 278 ARG D CZ  1 
ATOM   5275 N NH1 . ARG B 2 162 ? 139.778 135.369 125.996 1.00 67.10  ? 278 ARG D NH1 1 
ATOM   5276 N NH2 . ARG B 2 162 ? 141.761 134.852 124.976 1.00 63.58  ? 278 ARG D NH2 1 
ATOM   5277 N N   . SER B 2 163 ? 141.634 139.353 124.970 1.00 63.62  ? 279 SER D N   1 
ATOM   5278 C CA  . SER B 2 163 ? 142.938 139.463 125.604 1.00 58.58  ? 279 SER D CA  1 
ATOM   5279 C C   . SER B 2 163 ? 143.513 138.077 125.868 1.00 59.04  ? 279 SER D C   1 
ATOM   5280 O O   . SER B 2 163 ? 142.785 137.132 126.183 1.00 61.84  ? 279 SER D O   1 
ATOM   5281 C CB  . SER B 2 163 ? 142.849 140.256 126.909 1.00 61.16  ? 279 SER D CB  1 
ATOM   5282 O OG  . SER B 2 163 ? 142.029 139.600 127.857 1.00 66.23  ? 279 SER D OG  1 
ATOM   5283 N N   . SER B 2 164 ? 144.835 137.963 125.721 1.00 57.66  ? 280 SER D N   1 
ATOM   5284 C CA  . SER B 2 164 ? 145.492 136.675 125.922 1.00 58.76  ? 280 SER D CA  1 
ATOM   5285 C C   . SER B 2 164 ? 145.339 136.194 127.360 1.00 57.28  ? 280 SER D C   1 
ATOM   5286 O O   . SER B 2 164 ? 145.105 135.005 127.603 1.00 54.19  ? 280 SER D O   1 
ATOM   5287 C CB  . SER B 2 164 ? 146.968 136.772 125.536 1.00 53.69  ? 280 SER D CB  1 
ATOM   5288 O OG  . SER B 2 164 ? 147.722 137.411 126.549 1.00 55.40  ? 280 SER D OG  1 
ATOM   5289 N N   . GLN B 2 165 ? 145.469 137.099 128.322 1.00 59.87  ? 281 GLN D N   1 
ATOM   5290 C CA  . GLN B 2 165 ? 145.277 136.796 129.733 1.00 59.52  ? 281 GLN D CA  1 
ATOM   5291 C C   . GLN B 2 165 ? 144.182 137.693 130.301 1.00 63.40  ? 281 GLN D C   1 
ATOM   5292 O O   . GLN B 2 165 ? 143.555 138.479 129.586 1.00 61.42  ? 281 GLN D O   1 
ATOM   5293 C CB  . GLN B 2 165 ? 146.582 136.971 130.517 1.00 52.70  ? 281 GLN D CB  1 
ATOM   5294 C CG  . GLN B 2 165 ? 147.842 136.842 129.679 1.00 51.49  ? 281 GLN D CG  1 
ATOM   5295 C CD  . GLN B 2 165 ? 149.096 137.179 130.459 1.00 56.06  ? 281 GLN D CD  1 
ATOM   5296 O OE1 . GLN B 2 165 ? 149.039 137.470 131.654 1.00 56.38  ? 281 GLN D OE1 1 
ATOM   5297 N NE2 . GLN B 2 165 ? 150.240 137.143 129.785 1.00 51.93  ? 281 GLN D NE2 1 
ATOM   5298 N N   . ASN B 2 166 ? 143.951 137.565 131.604 1.00 65.15  ? 282 ASN D N   1 
ATOM   5299 C CA  . ASN B 2 166 ? 143.000 138.424 132.296 1.00 67.88  ? 282 ASN D CA  1 
ATOM   5300 C C   . ASN B 2 166 ? 143.686 139.738 132.647 1.00 73.54  ? 282 ASN D C   1 
ATOM   5301 O O   . ASN B 2 166 ? 144.671 139.750 133.394 1.00 70.25  ? 282 ASN D O   1 
ATOM   5302 C CB  . ASN B 2 166 ? 142.470 137.734 133.551 1.00 71.55  ? 282 ASN D CB  1 
ATOM   5303 C CG  . ASN B 2 166 ? 141.543 138.623 134.356 1.00 78.18  ? 282 ASN D CG  1 
ATOM   5304 O OD1 . ASN B 2 166 ? 140.669 139.289 133.803 1.00 78.49  ? 282 ASN D OD1 1 
ATOM   5305 N ND2 . ASN B 2 166 ? 141.730 138.636 135.671 1.00 79.72  ? 282 ASN D ND2 1 
ATOM   5306 N N   . ILE B 2 167 ? 143.170 140.840 132.112 1.00 77.61  ? 283 ILE D N   1 
ATOM   5307 C CA  . ILE B 2 167 ? 143.802 142.142 132.266 1.00 71.84  ? 283 ILE D CA  1 
ATOM   5308 C C   . ILE B 2 167 ? 143.199 142.927 133.433 1.00 72.22  ? 283 ILE D C   1 
ATOM   5309 O O   . ILE B 2 167 ? 143.388 144.138 133.525 1.00 69.61  ? 283 ILE D O   1 
ATOM   5310 C CB  . ILE B 2 167 ? 143.746 142.952 130.963 1.00 67.45  ? 283 ILE D CB  1 
ATOM   5311 C CG1 . ILE B 2 167 ? 142.317 143.414 130.680 1.00 55.12  ? 283 ILE D CG1 1 
ATOM   5312 C CG2 . ILE B 2 167 ? 144.277 142.127 129.804 1.00 62.60  ? 283 ILE D CG2 1 
ATOM   5313 C CD1 . ILE B 2 167 ? 142.242 144.753 129.992 1.00 39.97  ? 283 ILE D CD1 1 
ATOM   5314 N N   . VAL B 2 168 ? 142.476 142.258 134.326 1.00 75.66  ? 284 VAL D N   1 
ATOM   5315 C CA  . VAL B 2 168 ? 141.980 142.904 135.536 1.00 80.46  ? 284 VAL D CA  1 
ATOM   5316 C C   . VAL B 2 168 ? 143.156 143.035 136.499 1.00 85.80  ? 284 VAL D C   1 
ATOM   5317 O O   . VAL B 2 168 ? 143.659 142.036 137.019 1.00 80.08  ? 284 VAL D O   1 
ATOM   5318 C CB  . VAL B 2 168 ? 140.825 142.119 136.166 1.00 84.02  ? 284 VAL D CB  1 
ATOM   5319 C CG1 . VAL B 2 168 ? 140.444 142.726 137.508 1.00 84.02  ? 284 VAL D CG1 1 
ATOM   5320 C CG2 . VAL B 2 168 ? 139.628 142.098 135.229 1.00 76.09  ? 284 VAL D CG2 1 
ATOM   5321 N N   . HIS B 2 169 ? 143.600 144.267 136.731 1.00 85.57  ? 285 HIS D N   1 
ATOM   5322 C CA  . HIS B 2 169 ? 144.783 144.501 137.542 1.00 81.11  ? 285 HIS D CA  1 
ATOM   5323 C C   . HIS B 2 169 ? 144.513 144.163 139.006 1.00 81.71  ? 285 HIS D C   1 
ATOM   5324 O O   . HIS B 2 169 ? 143.366 144.067 139.452 1.00 83.45  ? 285 HIS D O   1 
ATOM   5325 C CB  . HIS B 2 169 ? 145.245 145.953 137.408 1.00 74.76  ? 285 HIS D CB  1 
ATOM   5326 C CG  . HIS B 2 169 ? 146.664 146.178 137.829 1.00 69.24  ? 285 HIS D CG  1 
ATOM   5327 N ND1 . HIS B 2 169 ? 147.740 145.754 137.079 1.00 60.44  ? 285 HIS D ND1 1 
ATOM   5328 C CD2 . HIS B 2 169 ? 147.184 146.784 138.923 1.00 69.69  ? 285 HIS D CD2 1 
ATOM   5329 C CE1 . HIS B 2 169 ? 148.861 146.087 137.693 1.00 55.40  ? 285 HIS D CE1 1 
ATOM   5330 N NE2 . HIS B 2 169 ? 148.552 146.714 138.814 1.00 61.93  ? 285 HIS D NE2 1 
ATOM   5331 N N   . ASN B 2 170 ? 145.603 143.975 139.755 1.00 80.50  ? 286 ASN D N   1 
ATOM   5332 C CA  . ASN B 2 170 ? 145.492 143.564 141.151 1.00 78.79  ? 286 ASN D CA  1 
ATOM   5333 C C   . ASN B 2 170 ? 144.784 144.611 142.001 1.00 78.45  ? 286 ASN D C   1 
ATOM   5334 O O   . ASN B 2 170 ? 144.150 144.268 143.005 1.00 75.87  ? 286 ASN D O   1 
ATOM   5335 C CB  . ASN B 2 170 ? 146.880 143.270 141.719 1.00 75.74  ? 286 ASN D CB  1 
ATOM   5336 C CG  . ASN B 2 170 ? 147.824 142.696 140.680 1.00 79.48  ? 286 ASN D CG  1 
ATOM   5337 O OD1 . ASN B 2 170 ? 147.494 141.733 139.989 1.00 86.02  ? 286 ASN D OD1 1 
ATOM   5338 N ND2 . ASN B 2 170 ? 149.007 143.288 140.564 1.00 74.51  ? 286 ASN D ND2 1 
ATOM   5339 N N   . ASN B 2 171 ? 144.875 145.887 141.621 1.00 79.91  ? 287 ASN D N   1 
ATOM   5340 C CA  . ASN B 2 171 ? 144.223 146.942 142.387 1.00 82.61  ? 287 ASN D CA  1 
ATOM   5341 C C   . ASN B 2 171 ? 142.708 146.939 142.228 1.00 89.48  ? 287 ASN D C   1 
ATOM   5342 O O   . ASN B 2 171 ? 142.025 147.666 142.957 1.00 82.72  ? 287 ASN D O   1 
ATOM   5343 C CB  . ASN B 2 171 ? 144.782 148.310 141.986 1.00 76.16  ? 287 ASN D CB  1 
ATOM   5344 C CG  . ASN B 2 171 ? 144.526 148.645 140.529 1.00 75.44  ? 287 ASN D CG  1 
ATOM   5345 O OD1 . ASN B 2 171 ? 144.121 147.789 139.743 1.00 76.69  ? 287 ASN D OD1 1 
ATOM   5346 N ND2 . ASN B 2 171 ? 144.762 149.899 140.161 1.00 67.64  ? 287 ASN D ND2 1 
ATOM   5347 N N   . GLY B 2 172 ? 142.170 146.146 141.304 1.00 87.75  ? 288 GLY D N   1 
ATOM   5348 C CA  . GLY B 2 172 ? 140.745 146.099 141.059 1.00 81.92  ? 288 GLY D CA  1 
ATOM   5349 C C   . GLY B 2 172 ? 140.265 146.954 139.908 1.00 85.53  ? 288 GLY D C   1 
ATOM   5350 O O   . GLY B 2 172 ? 139.069 146.922 139.594 1.00 87.00  ? 288 GLY D O   1 
ATOM   5351 N N   . ILE B 2 173 ? 141.152 147.713 139.271 1.00 83.87  ? 289 ILE D N   1 
ATOM   5352 C CA  . ILE B 2 173 ? 140.807 148.565 138.139 1.00 78.76  ? 289 ILE D CA  1 
ATOM   5353 C C   . ILE B 2 173 ? 141.429 147.969 136.886 1.00 76.74  ? 289 ILE D C   1 
ATOM   5354 O O   . ILE B 2 173 ? 142.649 147.774 136.822 1.00 71.18  ? 289 ILE D O   1 
ATOM   5355 C CB  . ILE B 2 173 ? 141.285 150.011 138.356 1.00 70.66  ? 289 ILE D CB  1 
ATOM   5356 C CG1 . ILE B 2 173 ? 140.344 150.749 139.311 1.00 69.24  ? 289 ILE D CG1 1 
ATOM   5357 C CG2 . ILE B 2 173 ? 141.384 150.746 137.029 1.00 56.38  ? 289 ILE D CG2 1 
ATOM   5358 C CD1 . ILE B 2 173 ? 141.045 151.750 140.204 1.00 62.82  ? 289 ILE D CD1 1 
ATOM   5359 N N   . THR B 2 174 ? 140.593 147.675 135.894 1.00 74.65  ? 290 THR D N   1 
ATOM   5360 C CA  . THR B 2 174 ? 141.065 147.173 134.611 1.00 68.93  ? 290 THR D CA  1 
ATOM   5361 C C   . THR B 2 174 ? 141.334 148.346 133.676 1.00 54.01  ? 290 THR D C   1 
ATOM   5362 O O   . THR B 2 174 ? 140.462 149.194 133.463 1.00 39.04  ? 290 THR D O   1 
ATOM   5363 C CB  . THR B 2 174 ? 140.050 146.209 133.993 1.00 73.34  ? 290 THR D CB  1 
ATOM   5364 O OG1 . THR B 2 174 ? 140.374 145.981 132.616 1.00 69.17  ? 290 THR D OG1 1 
ATOM   5365 C CG2 . THR B 2 174 ? 138.633 146.759 134.105 1.00 59.98  ? 290 THR D CG2 1 
ATOM   5366 N N   . TYR B 2 175 ? 142.546 148.400 133.136 1.00 53.96  ? 291 TYR D N   1 
ATOM   5367 C CA  . TYR B 2 175 ? 142.957 149.503 132.270 1.00 42.88  ? 291 TYR D CA  1 
ATOM   5368 C C   . TYR B 2 175 ? 142.698 149.162 130.804 1.00 35.01  ? 291 TYR D C   1 
ATOM   5369 O O   . TYR B 2 175 ? 143.575 149.240 129.944 1.00 31.42  ? 291 TYR D O   1 
ATOM   5370 C CB  . TYR B 2 175 ? 144.420 149.852 132.522 1.00 33.53  ? 291 TYR D CB  1 
ATOM   5371 C CG  . TYR B 2 175 ? 144.649 150.444 133.893 1.00 35.71  ? 291 TYR D CG  1 
ATOM   5372 C CD1 . TYR B 2 175 ? 144.163 151.704 134.212 1.00 36.31  ? 291 TYR D CD1 1 
ATOM   5373 C CD2 . TYR B 2 175 ? 145.326 149.735 134.875 1.00 44.04  ? 291 TYR D CD2 1 
ATOM   5374 C CE1 . TYR B 2 175 ? 144.358 152.248 135.465 1.00 44.01  ? 291 TYR D CE1 1 
ATOM   5375 C CE2 . TYR B 2 175 ? 145.525 150.271 136.132 1.00 46.90  ? 291 TYR D CE2 1 
ATOM   5376 C CZ  . TYR B 2 175 ? 145.039 151.528 136.421 1.00 48.74  ? 291 TYR D CZ  1 
ATOM   5377 O OH  . TYR B 2 175 ? 145.233 152.068 137.670 1.00 53.30  ? 291 TYR D OH  1 
ATOM   5378 N N   . LEU B 2 176 ? 141.455 148.777 130.534 1.00 30.96  ? 292 LEU D N   1 
ATOM   5379 C CA  . LEU B 2 176 ? 140.981 148.583 129.173 1.00 26.85  ? 292 LEU D CA  1 
ATOM   5380 C C   . LEU B 2 176 ? 140.594 149.931 128.584 1.00 20.50  ? 292 LEU D C   1 
ATOM   5381 O O   . LEU B 2 176 ? 139.917 150.732 129.231 1.00 25.20  ? 292 LEU D O   1 
ATOM   5382 C CB  . LEU B 2 176 ? 139.789 147.621 129.149 1.00 32.52  ? 292 LEU D CB  1 
ATOM   5383 C CG  . LEU B 2 176 ? 139.423 146.904 127.845 1.00 34.58  ? 292 LEU D CG  1 
ATOM   5384 C CD1 . LEU B 2 176 ? 138.682 147.815 126.880 1.00 29.75  ? 292 LEU D CD1 1 
ATOM   5385 C CD2 . LEU B 2 176 ? 140.666 146.342 127.181 1.00 31.66  ? 292 LEU D CD2 1 
ATOM   5386 N N   . GLU B 2 177 ? 141.067 150.182 127.369 1.00 13.81  ? 293 GLU D N   1 
ATOM   5387 C CA  . GLU B 2 177 ? 140.793 151.491 126.741 1.00 11.34  ? 293 GLU D CA  1 
ATOM   5388 C C   . GLU B 2 177 ? 140.569 151.295 125.244 1.00 11.18  ? 293 GLU D C   1 
ATOM   5389 O O   . GLU B 2 177 ? 141.098 150.318 124.685 1.00 20.98  ? 293 GLU D O   1 
ATOM   5390 C CB  . GLU B 2 177 ? 141.953 152.439 127.033 1.00 14.26  ? 293 GLU D CB  1 
ATOM   5391 C CG  . GLU B 2 177 ? 141.882 153.035 128.434 1.00 18.49  ? 293 GLU D CG  1 
ATOM   5392 C CD  . GLU B 2 177 ? 143.134 153.747 128.895 1.00 17.74  ? 293 GLU D CD  1 
ATOM   5393 O OE1 . GLU B 2 177 ? 143.553 154.695 128.203 1.00 13.85  ? 293 GLU D OE1 1 
ATOM   5394 O OE2 . GLU B 2 177 ? 143.676 153.359 129.949 1.00 20.06  ? 293 GLU D OE2 1 
ATOM   5395 N N   . TRP B 2 178 ? 139.797 152.185 124.639 1.00 9.35   ? 294 TRP D N   1 
ATOM   5396 C CA  . TRP B 2 178 ? 139.522 152.135 123.185 1.00 10.79  ? 294 TRP D CA  1 
ATOM   5397 C C   . TRP B 2 178 ? 139.974 153.448 122.568 1.00 10.88  ? 294 TRP D C   1 
ATOM   5398 O O   . TRP B 2 178 ? 139.524 154.514 123.024 1.00 12.86  ? 294 TRP D O   1 
ATOM   5399 C CB  . TRP B 2 178 ? 138.037 151.865 122.913 1.00 15.22  ? 294 TRP D CB  1 
ATOM   5400 C CG  . TRP B 2 178 ? 137.617 150.450 123.208 1.00 17.73  ? 294 TRP D CG  1 
ATOM   5401 C CD1 . TRP B 2 178 ? 137.132 149.961 124.385 1.00 19.39  ? 294 TRP D CD1 1 
ATOM   5402 C CD2 . TRP B 2 178 ? 137.654 149.333 122.294 1.00 22.88  ? 294 TRP D CD2 1 
ATOM   5403 N NE1 . TRP B 2 178 ? 136.863 148.624 124.269 1.00 23.06  ? 294 TRP D NE1 1 
ATOM   5404 C CE2 . TRP B 2 178 ? 137.173 148.210 123.000 1.00 25.65  ? 294 TRP D CE2 1 
ATOM   5405 C CE3 . TRP B 2 178 ? 138.042 149.175 120.959 1.00 23.28  ? 294 TRP D CE3 1 
ATOM   5406 C CZ2 . TRP B 2 178 ? 137.072 146.951 122.413 1.00 33.52  ? 294 TRP D CZ2 1 
ATOM   5407 C CZ3 . TRP B 2 178 ? 137.942 147.930 120.382 1.00 22.05  ? 294 TRP D CZ3 1 
ATOM   5408 C CH2 . TRP B 2 178 ? 137.463 146.836 121.099 1.00 30.74  ? 294 TRP D CH2 1 
ATOM   5409 N N   . TYR B 2 179 ? 140.848 153.369 121.576 1.00 9.30   ? 295 TYR D N   1 
ATOM   5410 C CA  . TYR B 2 179 ? 141.393 154.538 120.904 1.00 8.60   ? 295 TYR D CA  1 
ATOM   5411 C C   . TYR B 2 179 ? 140.927 154.541 119.458 1.00 9.58   ? 295 TYR D C   1 
ATOM   5412 O O   . TYR B 2 179 ? 141.024 153.520 118.770 1.00 15.40  ? 295 TYR D O   1 
ATOM   5413 C CB  . TYR B 2 179 ? 142.923 154.550 120.969 1.00 8.22   ? 295 TYR D CB  1 
ATOM   5414 C CG  . TYR B 2 179 ? 143.468 154.726 122.366 1.00 6.34   ? 295 TYR D CG  1 
ATOM   5415 C CD1 . TYR B 2 179 ? 143.549 153.653 123.240 1.00 7.12   ? 295 TYR D CD1 1 
ATOM   5416 C CD2 . TYR B 2 179 ? 143.895 155.967 122.813 1.00 6.91   ? 295 TYR D CD2 1 
ATOM   5417 C CE1 . TYR B 2 179 ? 144.041 153.810 124.515 1.00 9.27   ? 295 TYR D CE1 1 
ATOM   5418 C CE2 . TYR B 2 179 ? 144.388 156.133 124.089 1.00 6.23   ? 295 TYR D CE2 1 
ATOM   5419 C CZ  . TYR B 2 179 ? 144.459 155.051 124.935 1.00 6.28   ? 295 TYR D CZ  1 
ATOM   5420 O OH  . TYR B 2 179 ? 144.950 155.206 126.209 1.00 6.81   ? 295 TYR D OH  1 
ATOM   5421 N N   . LEU B 2 180 ? 140.413 155.692 119.026 1.00 8.68   ? 296 LEU D N   1 
ATOM   5422 C CA  . LEU B 2 180 ? 139.933 155.832 117.631 1.00 12.53  ? 296 LEU D CA  1 
ATOM   5423 C C   . LEU B 2 180 ? 140.922 156.696 116.841 1.00 13.74  ? 296 LEU D C   1 
ATOM   5424 O O   . LEU B 2 180 ? 140.922 157.927 117.026 1.00 16.39  ? 296 LEU D O   1 
ATOM   5425 C CB  . LEU B 2 180 ? 138.520 156.413 117.605 1.00 17.32  ? 296 LEU D CB  1 
ATOM   5426 C CG  . LEU B 2 180 ? 137.995 156.876 116.241 1.00 19.01  ? 296 LEU D CG  1 
ATOM   5427 C CD1 . LEU B 2 180 ? 138.102 155.787 115.191 1.00 22.79  ? 296 LEU D CD1 1 
ATOM   5428 C CD2 . LEU B 2 180 ? 136.562 157.357 116.366 1.00 24.74  ? 296 LEU D CD2 1 
ATOM   5429 N N   . GLN B 2 181 ? 141.751 156.064 116.019 1.00 13.00  ? 297 GLN D N   1 
ATOM   5430 C CA  . GLN B 2 181 ? 142.674 156.782 115.145 1.00 16.05  ? 297 GLN D CA  1 
ATOM   5431 C C   . GLN B 2 181 ? 141.908 157.135 113.877 1.00 25.56  ? 297 GLN D C   1 
ATOM   5432 O O   . GLN B 2 181 ? 141.786 156.334 112.950 1.00 28.79  ? 297 GLN D O   1 
ATOM   5433 C CB  . GLN B 2 181 ? 143.935 155.982 114.843 1.00 12.76  ? 297 GLN D CB  1 
ATOM   5434 C CG  . GLN B 2 181 ? 144.758 156.529 113.686 1.00 14.28  ? 297 GLN D CG  1 
ATOM   5435 C CD  . GLN B 2 181 ? 146.239 156.573 113.990 1.00 19.74  ? 297 GLN D CD  1 
ATOM   5436 O OE1 . GLN B 2 181 ? 146.936 157.512 113.609 1.00 22.71  ? 297 GLN D OE1 1 
ATOM   5437 N NE2 . GLN B 2 181 ? 146.731 155.549 114.680 1.00 20.21  ? 297 GLN D NE2 1 
ATOM   5438 N N   . LYS B 2 182 ? 141.359 158.345 113.851 1.00 26.53  ? 298 LYS D N   1 
ATOM   5439 C CA  . LYS B 2 182 ? 140.667 158.815 112.666 1.00 29.37  ? 298 LYS D CA  1 
ATOM   5440 C C   . LYS B 2 182 ? 141.673 159.061 111.542 1.00 35.32  ? 298 LYS D C   1 
ATOM   5441 O O   . LYS B 2 182 ? 142.849 159.331 111.802 1.00 38.90  ? 298 LYS D O   1 
ATOM   5442 C CB  . LYS B 2 182 ? 139.889 160.090 112.976 1.00 32.59  ? 298 LYS D CB  1 
ATOM   5443 C CG  . LYS B 2 182 ? 138.925 159.952 114.144 1.00 28.42  ? 298 LYS D CG  1 
ATOM   5444 C CD  . LYS B 2 182 ? 137.776 160.939 114.035 1.00 30.44  ? 298 LYS D CD  1 
ATOM   5445 C CE  . LYS B 2 182 ? 136.900 160.902 115.275 1.00 23.74  ? 298 LYS D CE  1 
ATOM   5446 N NZ  . LYS B 2 182 ? 136.260 162.217 115.548 1.00 28.51  ? 298 LYS D NZ  1 
ATOM   5447 N N   . PRO B 2 183 ? 141.241 158.953 110.285 1.00 40.36  ? 299 PRO D N   1 
ATOM   5448 C CA  . PRO B 2 183 ? 142.183 159.095 109.163 1.00 47.34  ? 299 PRO D CA  1 
ATOM   5449 C C   . PRO B 2 183 ? 142.871 160.451 109.168 1.00 48.14  ? 299 PRO D C   1 
ATOM   5450 O O   . PRO B 2 183 ? 142.232 161.496 109.021 1.00 40.22  ? 299 PRO D O   1 
ATOM   5451 C CB  . PRO B 2 183 ? 141.289 158.917 107.930 1.00 47.18  ? 299 PRO D CB  1 
ATOM   5452 C CG  . PRO B 2 183 ? 140.122 158.131 108.421 1.00 43.72  ? 299 PRO D CG  1 
ATOM   5453 C CD  . PRO B 2 183 ? 139.888 158.593 109.826 1.00 43.52  ? 299 PRO D CD  1 
ATOM   5454 N N   . GLY B 2 184 ? 144.192 160.426 109.340 1.00 39.50  ? 300 GLY D N   1 
ATOM   5455 C CA  . GLY B 2 184 ? 145.000 161.625 109.313 1.00 38.41  ? 300 GLY D CA  1 
ATOM   5456 C C   . GLY B 2 184 ? 145.289 162.255 110.658 1.00 45.22  ? 300 GLY D C   1 
ATOM   5457 O O   . GLY B 2 184 ? 146.003 163.265 110.706 1.00 45.40  ? 300 GLY D O   1 
ATOM   5458 N N   . GLN B 2 185 ? 144.767 161.702 111.751 1.00 43.49  ? 301 GLN D N   1 
ATOM   5459 C CA  . GLN B 2 185 ? 144.971 162.265 113.077 1.00 34.02  ? 301 GLN D CA  1 
ATOM   5460 C C   . GLN B 2 185 ? 145.460 161.190 114.038 1.00 26.13  ? 301 GLN D C   1 
ATOM   5461 O O   . GLN B 2 185 ? 145.339 159.989 113.783 1.00 23.19  ? 301 GLN D O   1 
ATOM   5462 C CB  . GLN B 2 185 ? 143.690 162.913 113.626 1.00 30.88  ? 301 GLN D CB  1 
ATOM   5463 C CG  . GLN B 2 185 ? 142.700 163.360 112.565 1.00 37.23  ? 301 GLN D CG  1 
ATOM   5464 C CD  . GLN B 2 185 ? 141.298 163.530 113.111 1.00 44.52  ? 301 GLN D CD  1 
ATOM   5465 O OE1 . GLN B 2 185 ? 141.111 163.939 114.257 1.00 48.98  ? 301 GLN D OE1 1 
ATOM   5466 N NE2 . GLN B 2 185 ? 140.301 163.231 112.287 1.00 41.01  ? 301 GLN D NE2 1 
ATOM   5467 N N   . SER B 2 186 ? 146.023 161.649 115.154 1.00 25.33  ? 302 SER D N   1 
ATOM   5468 C CA  . SER B 2 186 ? 146.541 160.758 116.176 1.00 21.19  ? 302 SER D CA  1 
ATOM   5469 C C   . SER B 2 186 ? 145.396 160.051 116.897 1.00 17.45  ? 302 SER D C   1 
ATOM   5470 O O   . SER B 2 186 ? 144.256 160.521 116.882 1.00 25.28  ? 302 SER D O   1 
ATOM   5471 C CB  . SER B 2 186 ? 147.389 161.540 117.176 1.00 17.31  ? 302 SER D CB  1 
ATOM   5472 O OG  . SER B 2 186 ? 146.701 162.686 117.642 1.00 17.08  ? 302 SER D OG  1 
ATOM   5473 N N   . PRO B 2 187 ? 145.672 158.904 117.520 1.00 9.58   ? 303 PRO D N   1 
ATOM   5474 C CA  . PRO B 2 187 ? 144.624 158.209 118.274 1.00 8.56   ? 303 PRO D CA  1 
ATOM   5475 C C   . PRO B 2 187 ? 144.068 159.080 119.389 1.00 11.25  ? 303 PRO D C   1 
ATOM   5476 O O   . PRO B 2 187 ? 144.782 159.872 120.007 1.00 15.46  ? 303 PRO D O   1 
ATOM   5477 C CB  . PRO B 2 187 ? 145.345 156.979 118.835 1.00 7.21   ? 303 PRO D CB  1 
ATOM   5478 C CG  . PRO B 2 187 ? 146.477 156.753 117.905 1.00 9.77   ? 303 PRO D CG  1 
ATOM   5479 C CD  . PRO B 2 187 ? 146.908 158.108 117.431 1.00 11.71  ? 303 PRO D CD  1 
ATOM   5480 N N   . GLN B 2 188 ? 142.769 158.934 119.632 1.00 12.53  ? 304 GLN D N   1 
ATOM   5481 C CA  . GLN B 2 188 ? 142.081 159.678 120.676 1.00 13.20  ? 304 GLN D CA  1 
ATOM   5482 C C   . GLN B 2 188 ? 141.311 158.710 121.559 1.00 10.82  ? 304 GLN D C   1 
ATOM   5483 O O   . GLN B 2 188 ? 140.721 157.742 121.072 1.00 13.19  ? 304 GLN D O   1 
ATOM   5484 C CB  . GLN B 2 188 ? 141.135 160.732 120.083 1.00 17.08  ? 304 GLN D CB  1 
ATOM   5485 C CG  . GLN B 2 188 ? 140.012 160.168 119.231 1.00 17.24  ? 304 GLN D CG  1 
ATOM   5486 C CD  . GLN B 2 188 ? 139.661 161.069 118.068 1.00 19.00  ? 304 GLN D CD  1 
ATOM   5487 O OE1 . GLN B 2 188 ? 140.421 161.184 117.107 1.00 24.46  ? 304 GLN D OE1 1 
ATOM   5488 N NE2 . GLN B 2 188 ? 138.505 161.716 118.148 1.00 14.04  ? 304 GLN D NE2 1 
ATOM   5489 N N   . LEU B 2 189 ? 141.370 158.909 122.877 1.00 7.74   ? 305 LEU D N   1 
ATOM   5490 C CA  . LEU B 2 189 ? 140.732 157.965 123.827 1.00 9.20   ? 305 LEU D CA  1 
ATOM   5491 C C   . LEU B 2 189 ? 139.209 158.087 123.708 1.00 17.83  ? 305 LEU D C   1 
ATOM   5492 O O   . LEU B 2 189 ? 138.720 159.234 123.667 1.00 22.08  ? 305 LEU D O   1 
ATOM   5493 C CB  . LEU B 2 189 ? 141.236 158.259 125.239 1.00 8.70   ? 305 LEU D CB  1 
ATOM   5494 C CG  . LEU B 2 189 ? 140.721 157.350 126.358 1.00 11.34  ? 305 LEU D CG  1 
ATOM   5495 C CD1 . LEU B 2 189 ? 140.867 155.876 126.041 1.00 14.92  ? 305 LEU D CD1 1 
ATOM   5496 C CD2 . LEU B 2 189 ? 141.460 157.691 127.633 1.00 8.28   ? 305 LEU D CD2 1 
ATOM   5497 N N   . LEU B 2 190 ? 138.499 156.959 123.633 1.00 14.28  ? 306 LEU D N   1 
ATOM   5498 C CA  . LEU B 2 190 ? 137.017 156.937 123.548 1.00 17.98  ? 306 LEU D CA  1 
ATOM   5499 C C   . LEU B 2 190 ? 136.492 156.411 124.887 1.00 26.00  ? 306 LEU D C   1 
ATOM   5500 O O   . LEU B 2 190 ? 135.743 157.151 125.534 1.00 38.39  ? 306 LEU D O   1 
ATOM   5501 C CB  . LEU B 2 190 ? 136.525 156.068 122.392 1.00 17.54  ? 306 LEU D CB  1 
ATOM   5502 C CG  . LEU B 2 190 ? 136.967 156.470 120.983 1.00 14.93  ? 306 LEU D CG  1 
ATOM   5503 C CD1 . LEU B 2 190 ? 136.262 155.559 120.000 1.00 18.36  ? 306 LEU D CD1 1 
ATOM   5504 C CD2 . LEU B 2 190 ? 136.697 157.925 120.653 1.00 13.56  ? 306 LEU D CD2 1 
ATOM   5505 N N   . ILE B 2 191 ? 136.899 155.202 125.280 1.00 18.14  ? 307 ILE D N   1 
ATOM   5506 C CA  . ILE B 2 191 ? 136.451 154.597 126.570 1.00 19.55  ? 307 ILE D CA  1 
ATOM   5507 C C   . ILE B 2 191 ? 137.665 154.557 127.506 1.00 17.24  ? 307 ILE D C   1 
ATOM   5508 O O   . ILE B 2 191 ? 138.523 153.678 127.309 1.00 20.62  ? 307 ILE D O   1 
ATOM   5509 C CB  . ILE B 2 191 ? 135.838 153.206 126.330 1.00 23.38  ? 307 ILE D CB  1 
ATOM   5510 C CG1 . ILE B 2 191 ? 134.961 153.191 125.083 1.00 23.40  ? 307 ILE D CG1 1 
ATOM   5511 C CG2 . ILE B 2 191 ? 135.065 152.729 127.558 1.00 33.13  ? 307 ILE D CG2 1 
ATOM   5512 C CD1 . ILE B 2 191 ? 133.739 154.087 125.179 1.00 29.39  ? 307 ILE D CD1 1 
ATOM   5513 N N   . TYR B 2 192 ? 137.724 155.456 128.491 1.00 22.97  ? 308 TYR D N   1 
ATOM   5514 C CA  . TYR B 2 192 ? 138.938 155.568 129.352 1.00 25.44  ? 308 TYR D CA  1 
ATOM   5515 C C   . TYR B 2 192 ? 139.053 154.373 130.300 1.00 25.93  ? 308 TYR D C   1 
ATOM   5516 O O   . TYR B 2 192 ? 140.161 154.136 130.824 1.00 25.09  ? 308 TYR D O   1 
ATOM   5517 C CB  . TYR B 2 192 ? 138.985 156.936 130.050 1.00 20.54  ? 308 TYR D CB  1 
ATOM   5518 C CG  . TYR B 2 192 ? 138.207 157.144 131.340 1.00 20.65  ? 308 TYR D CG  1 
ATOM   5519 C CD1 . TYR B 2 192 ? 138.710 156.706 132.559 1.00 18.84  ? 308 TYR D CD1 1 
ATOM   5520 C CD2 . TYR B 2 192 ? 137.017 157.857 131.350 1.00 27.02  ? 308 TYR D CD2 1 
ATOM   5521 C CE1 . TYR B 2 192 ? 138.018 156.914 133.739 1.00 25.03  ? 308 TYR D CE1 1 
ATOM   5522 C CE2 . TYR B 2 192 ? 136.319 158.079 132.525 1.00 33.66  ? 308 TYR D CE2 1 
ATOM   5523 C CZ  . TYR B 2 192 ? 136.822 157.607 133.724 1.00 36.41  ? 308 TYR D CZ  1 
ATOM   5524 O OH  . TYR B 2 192 ? 136.142 157.818 134.887 1.00 47.12  ? 308 TYR D OH  1 
ATOM   5525 N N   . LYS B 2 193 ? 137.962 153.650 130.532 1.00 26.37  ? 309 LYS D N   1 
ATOM   5526 C CA  . LYS B 2 193 ? 138.065 152.424 131.362 1.00 26.13  ? 309 LYS D CA  1 
ATOM   5527 C C   . LYS B 2 193 ? 137.377 151.287 130.605 1.00 33.04  ? 309 LYS D C   1 
ATOM   5528 O O   . LYS B 2 193 ? 137.149 151.436 129.389 1.00 31.53  ? 309 LYS D O   1 
ATOM   5529 C CB  . LYS B 2 193 ? 137.414 152.571 132.740 1.00 33.96  ? 309 LYS D CB  1 
ATOM   5530 C CG  . LYS B 2 193 ? 138.162 153.424 133.749 1.00 35.54  ? 309 LYS D CG  1 
ATOM   5531 C CD  . LYS B 2 193 ? 139.432 152.779 134.286 1.00 35.59  ? 309 LYS D CD  1 
ATOM   5532 C CE  . LYS B 2 193 ? 139.945 153.524 135.475 1.00 29.77  ? 309 LYS D CE  1 
ATOM   5533 N NZ  . LYS B 2 193 ? 138.946 153.583 136.545 1.00 21.42  ? 309 LYS D NZ  1 
ATOM   5534 N N   . VAL B 2 194 ? 137.055 150.199 131.300 1.00 40.58  ? 310 VAL D N   1 
ATOM   5535 C CA  . VAL B 2 194 ? 136.339 149.114 130.636 1.00 36.75  ? 310 VAL D CA  1 
ATOM   5536 C C   . VAL B 2 194 ? 135.004 149.615 130.098 1.00 39.96  ? 310 VAL D C   1 
ATOM   5537 O O   . VAL B 2 194 ? 134.569 149.222 129.008 1.00 44.07  ? 310 VAL D O   1 
ATOM   5538 C CB  . VAL B 2 194 ? 136.165 147.920 131.595 1.00 44.36  ? 310 VAL D CB  1 
ATOM   5539 C CG1 . VAL B 2 194 ? 135.515 148.361 132.901 1.00 46.78  ? 310 VAL D CG1 1 
ATOM   5540 C CG2 . VAL B 2 194 ? 135.359 146.817 130.934 1.00 50.49  ? 310 VAL D CG2 1 
ATOM   5541 N N   . SER B 2 195 ? 134.344 150.506 130.839 1.00 42.46  ? 311 SER D N   1 
ATOM   5542 C CA  . SER B 2 195 ? 133.088 151.101 130.402 1.00 40.30  ? 311 SER D CA  1 
ATOM   5543 C C   . SER B 2 195 ? 133.030 152.616 130.538 1.00 37.87  ? 311 SER D C   1 
ATOM   5544 O O   . SER B 2 195 ? 132.191 153.236 129.872 1.00 30.10  ? 311 SER D O   1 
ATOM   5545 C CB  . SER B 2 195 ? 131.909 150.495 131.177 1.00 34.64  ? 311 SER D CB  1 
ATOM   5546 O OG  . SER B 2 195 ? 132.256 150.264 132.531 1.00 40.93  ? 311 SER D OG  1 
ATOM   5547 N N   . ASP B 2 196 ? 133.920 153.189 131.354 1.00 38.62  ? 312 ASP D N   1 
ATOM   5548 C CA  . ASP B 2 196 ? 133.924 154.659 131.595 1.00 37.31  ? 312 ASP D CA  1 
ATOM   5549 C C   . ASP B 2 196 ? 134.342 155.383 130.314 1.00 28.12  ? 312 ASP D C   1 
ATOM   5550 O O   . ASP B 2 196 ? 135.492 155.195 129.880 1.00 27.66  ? 312 ASP D O   1 
ATOM   5551 C CB  . ASP B 2 196 ? 134.801 155.021 132.782 1.00 31.98  ? 312 ASP D CB  1 
ATOM   5552 C CG  . ASP B 2 196 ? 134.545 154.225 134.053 1.00 36.36  ? 312 ASP D CG  1 
ATOM   5553 O OD1 . ASP B 2 196 ? 133.675 153.331 134.021 1.00 48.18  ? 312 ASP D OD1 1 
ATOM   5554 O OD2 . ASP B 2 196 ? 135.219 154.508 135.065 1.00 32.04  ? 312 ASP D OD2 1 
ATOM   5555 N N   . ARG B 2 197 ? 133.442 156.187 129.747 1.00 30.39  ? 313 ARG D N   1 
ATOM   5556 C CA  . ARG B 2 197 ? 133.732 156.892 128.473 1.00 32.14  ? 313 ARG D CA  1 
ATOM   5557 C C   . ARG B 2 197 ? 134.527 158.169 128.769 1.00 34.05  ? 313 ARG D C   1 
ATOM   5558 O O   . ARG B 2 197 ? 134.389 158.700 129.889 1.00 40.73  ? 313 ARG D O   1 
ATOM   5559 C CB  . ARG B 2 197 ? 132.426 157.216 127.743 1.00 42.05  ? 313 ARG D CB  1 
ATOM   5560 C CG  . ARG B 2 197 ? 132.606 157.723 126.320 1.00 43.80  ? 313 ARG D CG  1 
ATOM   5561 C CD  . ARG B 2 197 ? 131.264 157.952 125.657 1.00 56.93  ? 313 ARG D CD  1 
ATOM   5562 N NE  . ARG B 2 197 ? 130.429 158.891 126.412 1.00 60.50  ? 313 ARG D NE  1 
ATOM   5563 C CZ  . ARG B 2 197 ? 129.261 158.572 126.951 1.00 66.61  ? 313 ARG D CZ  1 
ATOM   5564 N NH1 . ARG B 2 197 ? 128.874 157.309 126.980 1.00 68.21  ? 313 ARG D NH1 1 
ATOM   5565 N NH2 . ARG B 2 197 ? 128.487 159.512 127.463 1.00 66.64  ? 313 ARG D NH2 1 
ATOM   5566 N N   . PHE B 2 198 ? 135.300 158.651 127.795 1.00 31.36  ? 314 PHE D N   1 
ATOM   5567 C CA  . PHE B 2 198 ? 136.163 159.843 128.001 1.00 29.87  ? 314 PHE D CA  1 
ATOM   5568 C C   . PHE B 2 198 ? 135.350 161.122 127.870 1.00 34.43  ? 314 PHE D C   1 
ATOM   5569 O O   . PHE B 2 198 ? 134.151 161.030 127.536 1.00 35.00  ? 314 PHE D O   1 
ATOM   5570 C CB  . PHE B 2 198 ? 137.283 159.761 126.960 1.00 22.14  ? 314 PHE D CB  1 
ATOM   5571 C CG  . PHE B 2 198 ? 138.546 160.558 127.256 1.00 21.10  ? 314 PHE D CG  1 
ATOM   5572 C CD1 . PHE B 2 198 ? 139.134 160.539 128.516 1.00 22.49  ? 314 PHE D CD1 1 
ATOM   5573 C CD2 . PHE B 2 198 ? 139.131 161.343 126.271 1.00 18.00  ? 314 PHE D CD2 1 
ATOM   5574 C CE1 . PHE B 2 198 ? 140.282 161.271 128.770 1.00 17.05  ? 314 PHE D CE1 1 
ATOM   5575 C CE2 . PHE B 2 198 ? 140.278 162.073 126.533 1.00 15.38  ? 314 PHE D CE2 1 
ATOM   5576 C CZ  . PHE B 2 198 ? 140.850 162.036 127.781 1.00 13.45  ? 314 PHE D CZ  1 
ATOM   5577 N N   . SER B 2 199 ? 135.969 162.279 128.121 1.00 36.24  ? 315 SER D N   1 
ATOM   5578 C CA  . SER B 2 199 ? 135.327 163.582 128.027 1.00 32.45  ? 315 SER D CA  1 
ATOM   5579 C C   . SER B 2 199 ? 135.516 164.150 126.627 1.00 32.85  ? 315 SER D C   1 
ATOM   5580 O O   . SER B 2 199 ? 136.639 164.200 126.115 1.00 34.66  ? 315 SER D O   1 
ATOM   5581 C CB  . SER B 2 199 ? 135.902 164.543 129.068 1.00 27.89  ? 315 SER D CB  1 
ATOM   5582 O OG  . SER B 2 199 ? 137.068 165.182 128.579 1.00 22.13  ? 315 SER D OG  1 
ATOM   5583 N N   . GLY B 2 200 ? 134.415 164.579 126.013 1.00 35.44  ? 316 GLY D N   1 
ATOM   5584 C CA  . GLY B 2 200 ? 134.445 165.148 124.683 1.00 38.00  ? 316 GLY D CA  1 
ATOM   5585 C C   . GLY B 2 200 ? 134.027 164.214 123.570 1.00 42.66  ? 316 GLY D C   1 
ATOM   5586 O O   . GLY B 2 200 ? 134.034 164.629 122.404 1.00 38.00  ? 316 GLY D O   1 
ATOM   5587 N N   . VAL B 2 201 ? 133.664 162.974 123.883 1.00 46.28  ? 317 VAL D N   1 
ATOM   5588 C CA  . VAL B 2 201 ? 133.213 162.023 122.871 1.00 54.70  ? 317 VAL D CA  1 
ATOM   5589 C C   . VAL B 2 201 ? 131.725 161.764 123.075 1.00 59.91  ? 317 VAL D C   1 
ATOM   5590 O O   . VAL B 2 201 ? 131.238 161.818 124.214 1.00 58.84  ? 317 VAL D O   1 
ATOM   5591 C CB  . VAL B 2 201 ? 134.026 160.720 122.925 1.00 46.58  ? 317 VAL D CB  1 
ATOM   5592 C CG1 . VAL B 2 201 ? 135.419 160.945 122.360 1.00 44.48  ? 317 VAL D CG1 1 
ATOM   5593 C CG2 . VAL B 2 201 ? 134.106 160.203 124.347 1.00 41.23  ? 317 VAL D CG2 1 
ATOM   5594 N N   . PRO B 2 202 ? 130.969 161.487 122.015 1.00 55.83  ? 318 PRO D N   1 
ATOM   5595 C CA  . PRO B 2 202 ? 129.517 161.328 122.158 1.00 60.98  ? 318 PRO D CA  1 
ATOM   5596 C C   . PRO B 2 202 ? 129.158 160.057 122.914 1.00 65.67  ? 318 PRO D C   1 
ATOM   5597 O O   . PRO B 2 202 ? 129.980 159.169 123.145 1.00 61.47  ? 318 PRO D O   1 
ATOM   5598 C CB  . PRO B 2 202 ? 129.017 161.273 120.710 1.00 66.25  ? 318 PRO D CB  1 
ATOM   5599 C CG  . PRO B 2 202 ? 130.138 161.831 119.884 1.00 62.14  ? 318 PRO D CG  1 
ATOM   5600 C CD  . PRO B 2 202 ? 131.389 161.459 120.606 1.00 53.74  ? 318 PRO D CD  1 
ATOM   5601 N N   . ASP B 2 203 ? 127.883 159.985 123.297 1.00 68.60  ? 319 ASP D N   1 
ATOM   5602 C CA  . ASP B 2 203 ? 127.323 158.826 123.981 1.00 72.18  ? 319 ASP D CA  1 
ATOM   5603 C C   . ASP B 2 203 ? 127.179 157.616 123.068 1.00 73.46  ? 319 ASP D C   1 
ATOM   5604 O O   . ASP B 2 203 ? 126.799 156.541 123.545 1.00 68.05  ? 319 ASP D O   1 
ATOM   5605 C CB  . ASP B 2 203 ? 125.960 159.186 124.582 1.00 73.93  ? 319 ASP D CB  1 
ATOM   5606 C CG  . ASP B 2 203 ? 125.597 158.321 125.776 1.00 84.55  ? 319 ASP D CG  1 
ATOM   5607 O OD1 . ASP B 2 203 ? 126.383 157.415 126.122 1.00 82.06  ? 319 ASP D OD1 1 
ATOM   5608 O OD2 . ASP B 2 203 ? 124.523 158.550 126.370 1.00 87.22  ? 319 ASP D OD2 1 
ATOM   5609 N N   . ARG B 2 204 ? 127.461 157.769 121.772 1.00 71.14  ? 320 ARG D N   1 
ATOM   5610 C CA  . ARG B 2 204 ? 127.340 156.651 120.843 1.00 60.71  ? 320 ARG D CA  1 
ATOM   5611 C C   . ARG B 2 204 ? 128.272 155.509 121.228 1.00 61.15  ? 320 ARG D C   1 
ATOM   5612 O O   . ARG B 2 204 ? 127.877 154.338 121.201 1.00 64.57  ? 320 ARG D O   1 
ATOM   5613 C CB  . ARG B 2 204 ? 127.634 157.131 119.423 1.00 55.67  ? 320 ARG D CB  1 
ATOM   5614 C CG  . ARG B 2 204 ? 126.747 158.280 118.976 1.00 66.61  ? 320 ARG D CG  1 
ATOM   5615 C CD  . ARG B 2 204 ? 126.865 158.522 117.485 1.00 71.16  ? 320 ARG D CD  1 
ATOM   5616 N NE  . ARG B 2 204 ? 128.215 158.907 117.096 1.00 63.76  ? 320 ARG D NE  1 
ATOM   5617 C CZ  . ARG B 2 204 ? 128.669 160.153 117.104 1.00 70.98  ? 320 ARG D CZ  1 
ATOM   5618 N NH1 . ARG B 2 204 ? 127.901 161.166 117.471 1.00 70.54  ? 320 ARG D NH1 1 
ATOM   5619 N NH2 . ARG B 2 204 ? 129.923 160.389 116.730 1.00 67.58  ? 320 ARG D NH2 1 
ATOM   5620 N N   . PHE B 2 205 ? 129.511 155.830 121.593 1.00 56.29  ? 321 PHE D N   1 
ATOM   5621 C CA  . PHE B 2 205 ? 130.465 154.818 122.022 1.00 50.34  ? 321 PHE D CA  1 
ATOM   5622 C C   . PHE B 2 205 ? 130.155 154.383 123.448 1.00 50.73  ? 321 PHE D C   1 
ATOM   5623 O O   . PHE B 2 205 ? 129.940 155.221 124.329 1.00 54.66  ? 321 PHE D O   1 
ATOM   5624 C CB  . PHE B 2 205 ? 131.892 155.356 121.933 1.00 43.71  ? 321 PHE D CB  1 
ATOM   5625 C CG  . PHE B 2 205 ? 132.231 155.956 120.600 1.00 39.42  ? 321 PHE D CG  1 
ATOM   5626 C CD1 . PHE B 2 205 ? 132.674 155.158 119.561 1.00 33.48  ? 321 PHE D CD1 1 
ATOM   5627 C CD2 . PHE B 2 205 ? 132.110 157.318 120.388 1.00 43.19  ? 321 PHE D CD2 1 
ATOM   5628 C CE1 . PHE B 2 205 ? 132.987 155.707 118.335 1.00 32.21  ? 321 PHE D CE1 1 
ATOM   5629 C CE2 . PHE B 2 205 ? 132.423 157.872 119.165 1.00 40.57  ? 321 PHE D CE2 1 
ATOM   5630 C CZ  . PHE B 2 205 ? 132.862 157.066 118.138 1.00 35.26  ? 321 PHE D CZ  1 
ATOM   5631 N N   . SER B 2 206 ? 130.133 153.070 123.674 1.00 44.10  ? 322 SER D N   1 
ATOM   5632 C CA  . SER B 2 206 ? 129.846 152.527 125.003 1.00 44.00  ? 322 SER D CA  1 
ATOM   5633 C C   . SER B 2 206 ? 130.639 151.228 125.151 1.00 42.00  ? 322 SER D C   1 
ATOM   5634 O O   . SER B 2 206 ? 130.203 150.166 124.703 1.00 44.82  ? 322 SER D O   1 
ATOM   5635 C CB  . SER B 2 206 ? 128.355 152.302 125.204 1.00 53.32  ? 322 SER D CB  1 
ATOM   5636 O OG  . SER B 2 206 ? 127.908 151.169 124.481 1.00 57.22  ? 322 SER D OG  1 
ATOM   5637 N N   . GLY B 2 207 ? 131.807 151.332 125.779 1.00 46.94  ? 323 GLY D N   1 
ATOM   5638 C CA  . GLY B 2 207 ? 132.604 150.151 126.040 1.00 46.33  ? 323 GLY D CA  1 
ATOM   5639 C C   . GLY B 2 207 ? 131.915 149.210 127.010 1.00 42.53  ? 323 GLY D C   1 
ATOM   5640 O O   . GLY B 2 207 ? 131.191 149.625 127.915 1.00 46.06  ? 323 GLY D O   1 
ATOM   5641 N N   . SER B 2 208 ? 132.148 147.915 126.812 1.00 40.49  ? 324 SER D N   1 
ATOM   5642 C CA  . SER B 2 208 ? 131.503 146.897 127.625 1.00 50.05  ? 324 SER D CA  1 
ATOM   5643 C C   . SER B 2 208 ? 132.402 145.674 127.704 1.00 55.25  ? 324 SER D C   1 
ATOM   5644 O O   . SER B 2 208 ? 133.325 145.501 126.903 1.00 57.17  ? 324 SER D O   1 
ATOM   5645 C CB  . SER B 2 208 ? 130.126 146.519 127.065 1.00 48.41  ? 324 SER D CB  1 
ATOM   5646 O OG  . SER B 2 208 ? 130.238 145.950 125.773 1.00 46.10  ? 324 SER D OG  1 
ATOM   5647 N N   . GLY B 2 209 ? 132.125 144.829 128.689 1.00 59.70  ? 325 GLY D N   1 
ATOM   5648 C CA  . GLY B 2 209 ? 132.852 143.597 128.893 1.00 59.46  ? 325 GLY D CA  1 
ATOM   5649 C C   . GLY B 2 209 ? 133.369 143.485 130.308 1.00 68.29  ? 325 GLY D C   1 
ATOM   5650 O O   . GLY B 2 209 ? 133.252 144.398 131.123 1.00 66.44  ? 325 GLY D O   1 
ATOM   5651 N N   . SER B 2 210 ? 133.948 142.324 130.597 1.00 64.94  ? 326 SER D N   1 
ATOM   5652 C CA  . SER B 2 210 ? 134.536 142.057 131.900 1.00 63.23  ? 326 SER D CA  1 
ATOM   5653 C C   . SER B 2 210 ? 135.469 140.864 131.761 1.00 66.98  ? 326 SER D C   1 
ATOM   5654 O O   . SER B 2 210 ? 135.412 140.117 130.781 1.00 61.91  ? 326 SER D O   1 
ATOM   5655 C CB  . SER B 2 210 ? 133.462 141.798 132.962 1.00 58.36  ? 326 SER D CB  1 
ATOM   5656 O OG  . SER B 2 210 ? 132.793 142.997 133.313 1.00 60.87  ? 326 SER D OG  1 
ATOM   5657 N N   . GLY B 2 211 ? 136.333 140.695 132.757 1.00 73.21  ? 327 GLY D N   1 
ATOM   5658 C CA  . GLY B 2 211 ? 137.242 139.568 132.768 1.00 77.73  ? 327 GLY D CA  1 
ATOM   5659 C C   . GLY B 2 211 ? 138.238 139.581 131.629 1.00 76.41  ? 327 GLY D C   1 
ATOM   5660 O O   . GLY B 2 211 ? 139.176 140.383 131.623 1.00 75.39  ? 327 GLY D O   1 
ATOM   5661 N N   . THR B 2 212 ? 138.050 138.690 130.658 1.00 74.14  ? 328 THR D N   1 
ATOM   5662 C CA  . THR B 2 212 ? 138.997 138.524 129.565 1.00 74.08  ? 328 THR D CA  1 
ATOM   5663 C C   . THR B 2 212 ? 138.489 139.049 128.230 1.00 69.55  ? 328 THR D C   1 
ATOM   5664 O O   . THR B 2 212 ? 139.301 139.408 127.374 1.00 66.67  ? 328 THR D O   1 
ATOM   5665 C CB  . THR B 2 212 ? 139.370 137.043 129.417 1.00 76.62  ? 328 THR D CB  1 
ATOM   5666 O OG1 . THR B 2 212 ? 139.513 136.460 130.717 1.00 73.50  ? 328 THR D OG1 1 
ATOM   5667 C CG2 . THR B 2 212 ? 140.690 136.892 128.684 1.00 68.86  ? 328 THR D CG2 1 
ATOM   5668 N N   . ASP B 2 213 ? 137.175 139.112 128.031 1.00 66.83  ? 329 ASP D N   1 
ATOM   5669 C CA  . ASP B 2 213 ? 136.583 139.565 126.779 1.00 66.44  ? 329 ASP D CA  1 
ATOM   5670 C C   . ASP B 2 213 ? 136.007 140.963 126.955 1.00 67.44  ? 329 ASP D C   1 
ATOM   5671 O O   . ASP B 2 213 ? 135.262 141.216 127.908 1.00 67.84  ? 329 ASP D O   1 
ATOM   5672 C CB  . ASP B 2 213 ? 135.489 138.603 126.307 1.00 71.81  ? 329 ASP D CB  1 
ATOM   5673 C CG  . ASP B 2 213 ? 136.027 137.227 125.972 1.00 77.12  ? 329 ASP D CG  1 
ATOM   5674 O OD1 . ASP B 2 213 ? 137.174 136.921 126.358 1.00 76.30  ? 329 ASP D OD1 1 
ATOM   5675 O OD2 . ASP B 2 213 ? 135.302 136.453 125.313 1.00 74.09  ? 329 ASP D OD2 1 
ATOM   5676 N N   . PHE B 2 214 ? 136.354 141.863 126.037 1.00 65.90  ? 330 PHE D N   1 
ATOM   5677 C CA  . PHE B 2 214 ? 135.875 143.239 126.052 1.00 60.58  ? 330 PHE D CA  1 
ATOM   5678 C C   . PHE B 2 214 ? 135.389 143.615 124.661 1.00 52.62  ? 330 PHE D C   1 
ATOM   5679 O O   . PHE B 2 214 ? 136.103 143.409 123.675 1.00 53.07  ? 330 PHE D O   1 
ATOM   5680 C CB  . PHE B 2 214 ? 136.975 144.203 126.506 1.00 51.89  ? 330 PHE D CB  1 
ATOM   5681 C CG  . PHE B 2 214 ? 137.593 143.838 127.822 1.00 53.29  ? 330 PHE D CG  1 
ATOM   5682 C CD1 . PHE B 2 214 ? 137.037 144.282 129.008 1.00 51.56  ? 330 PHE D CD1 1 
ATOM   5683 C CD2 . PHE B 2 214 ? 138.731 143.051 127.874 1.00 57.36  ? 330 PHE D CD2 1 
ATOM   5684 C CE1 . PHE B 2 214 ? 137.602 143.947 130.222 1.00 56.84  ? 330 PHE D CE1 1 
ATOM   5685 C CE2 . PHE B 2 214 ? 139.299 142.713 129.084 1.00 60.16  ? 330 PHE D CE2 1 
ATOM   5686 C CZ  . PHE B 2 214 ? 138.735 143.163 130.260 1.00 57.86  ? 330 PHE D CZ  1 
ATOM   5687 N N   . THR B 2 215 ? 134.182 144.168 124.584 1.00 46.34  ? 331 THR D N   1 
ATOM   5688 C CA  . THR B 2 215 ? 133.577 144.569 123.322 1.00 50.20  ? 331 THR D CA  1 
ATOM   5689 C C   . THR B 2 215 ? 133.173 146.035 123.381 1.00 45.53  ? 331 THR D C   1 
ATOM   5690 O O   . THR B 2 215 ? 132.633 146.500 124.390 1.00 51.05  ? 331 THR D O   1 
ATOM   5691 C CB  . THR B 2 215 ? 132.346 143.713 122.990 1.00 56.51  ? 331 THR D CB  1 
ATOM   5692 O OG1 . THR B 2 215 ? 131.243 144.121 123.809 1.00 53.09  ? 331 THR D OG1 1 
ATOM   5693 C CG2 . THR B 2 215 ? 132.631 142.236 123.226 1.00 55.11  ? 331 THR D CG2 1 
ATOM   5694 N N   . LEU B 2 216 ? 133.432 146.757 122.296 1.00 41.46  ? 332 LEU D N   1 
ATOM   5695 C CA  . LEU B 2 216 ? 133.013 148.144 122.157 1.00 37.25  ? 332 LEU D CA  1 
ATOM   5696 C C   . LEU B 2 216 ? 131.769 148.203 121.283 1.00 51.54  ? 332 LEU D C   1 
ATOM   5697 O O   . LEU B 2 216 ? 131.774 147.700 120.155 1.00 51.31  ? 332 LEU D O   1 
ATOM   5698 C CB  . LEU B 2 216 ? 134.126 148.998 121.550 1.00 33.10  ? 332 LEU D CB  1 
ATOM   5699 C CG  . LEU B 2 216 ? 133.710 150.386 121.062 1.00 36.79  ? 332 LEU D CG  1 
ATOM   5700 C CD1 . LEU B 2 216 ? 133.660 151.370 122.218 1.00 34.34  ? 332 LEU D CD1 1 
ATOM   5701 C CD2 . LEU B 2 216 ? 134.652 150.876 119.979 1.00 36.33  ? 332 LEU D CD2 1 
ATOM   5702 N N   . LYS B 2 217 ? 130.709 148.815 121.804 1.00 53.52  ? 333 LYS D N   1 
ATOM   5703 C CA  . LYS B 2 217 ? 129.420 148.881 121.122 1.00 51.09  ? 333 LYS D CA  1 
ATOM   5704 C C   . LYS B 2 217 ? 129.121 150.333 120.774 1.00 54.98  ? 333 LYS D C   1 
ATOM   5705 O O   . LYS B 2 217 ? 128.885 151.154 121.666 1.00 53.70  ? 333 LYS D O   1 
ATOM   5706 C CB  . LYS B 2 217 ? 128.313 148.288 121.993 1.00 53.75  ? 333 LYS D CB  1 
ATOM   5707 C CG  . LYS B 2 217 ? 126.915 148.441 121.415 1.00 60.23  ? 333 LYS D CG  1 
ATOM   5708 C CD  . LYS B 2 217 ? 126.742 147.612 120.153 1.00 62.66  ? 333 LYS D CD  1 
ATOM   5709 C CE  . LYS B 2 217 ? 125.300 147.635 119.672 1.00 69.73  ? 333 LYS D CE  1 
ATOM   5710 N NZ  . LYS B 2 217 ? 125.136 146.937 118.367 1.00 76.39  ? 333 LYS D NZ  1 
ATOM   5711 N N   . ILE B 2 218 ? 129.131 150.645 119.483 1.00 59.73  ? 334 ILE D N   1 
ATOM   5712 C CA  . ILE B 2 218 ? 128.728 151.958 118.994 1.00 56.02  ? 334 ILE D CA  1 
ATOM   5713 C C   . ILE B 2 218 ? 127.234 151.912 118.702 1.00 67.34  ? 334 ILE D C   1 
ATOM   5714 O O   . ILE B 2 218 ? 126.771 151.073 117.922 1.00 66.45  ? 334 ILE D O   1 
ATOM   5715 C CB  . ILE B 2 218 ? 129.526 152.359 117.745 1.00 53.57  ? 334 ILE D CB  1 
ATOM   5716 C CG1 . ILE B 2 218 ? 131.004 152.006 117.921 1.00 46.67  ? 334 ILE D CG1 1 
ATOM   5717 C CG2 . ILE B 2 218 ? 129.356 153.843 117.458 1.00 54.19  ? 334 ILE D CG2 1 
ATOM   5718 C CD1 . ILE B 2 218 ? 131.770 151.927 116.620 1.00 46.00  ? 334 ILE D CD1 1 
ATOM   5719 N N   . SER B 2 219 ? 126.477 152.813 119.332 1.00 68.87  ? 335 SER D N   1 
ATOM   5720 C CA  . SER B 2 219 ? 125.024 152.770 119.207 1.00 71.44  ? 335 SER D CA  1 
ATOM   5721 C C   . SER B 2 219 ? 124.553 153.258 117.843 1.00 73.80  ? 335 SER D C   1 
ATOM   5722 O O   . SER B 2 219 ? 123.478 152.856 117.384 1.00 74.95  ? 335 SER D O   1 
ATOM   5723 C CB  . SER B 2 219 ? 124.378 153.598 120.318 1.00 63.73  ? 335 SER D CB  1 
ATOM   5724 O OG  . SER B 2 219 ? 124.302 152.858 121.524 1.00 66.34  ? 335 SER D OG  1 
ATOM   5725 N N   . ARG B 2 220 ? 125.329 154.116 117.185 1.00 74.25  ? 336 ARG D N   1 
ATOM   5726 C CA  . ARG B 2 220 ? 124.915 154.674 115.899 1.00 75.00  ? 336 ARG D CA  1 
ATOM   5727 C C   . ARG B 2 220 ? 126.165 155.119 115.152 1.00 74.72  ? 336 ARG D C   1 
ATOM   5728 O O   . ARG B 2 220 ? 126.836 156.061 115.581 1.00 82.62  ? 336 ARG D O   1 
ATOM   5729 C CB  . ARG B 2 220 ? 123.948 155.834 116.104 1.00 76.96  ? 336 ARG D CB  1 
ATOM   5730 C CG  . ARG B 2 220 ? 123.342 156.389 114.826 1.00 84.05  ? 336 ARG D CG  1 
ATOM   5731 C CD  . ARG B 2 220 ? 123.173 157.897 114.914 1.00 87.14  ? 336 ARG D CD  1 
ATOM   5732 N NE  . ARG B 2 220 ? 122.047 158.370 114.117 1.00 97.77  ? 336 ARG D NE  1 
ATOM   5733 C CZ  . ARG B 2 220 ? 122.125 158.718 112.840 1.00 96.56  ? 336 ARG D CZ  1 
ATOM   5734 N NH1 . ARG B 2 220 ? 123.267 158.657 112.176 1.00 94.81  ? 336 ARG D NH1 1 
ATOM   5735 N NH2 . ARG B 2 220 ? 121.029 159.139 112.215 1.00 91.15  ? 336 ARG D NH2 1 
ATOM   5736 N N   . VAL B 2 221 ? 126.475 154.446 114.045 1.00 72.49  ? 337 VAL D N   1 
ATOM   5737 C CA  . VAL B 2 221 ? 127.656 154.796 113.267 1.00 72.24  ? 337 VAL D CA  1 
ATOM   5738 C C   . VAL B 2 221 ? 127.373 156.048 112.450 1.00 74.87  ? 337 VAL D C   1 
ATOM   5739 O O   . VAL B 2 221 ? 126.382 156.118 111.711 1.00 80.89  ? 337 VAL D O   1 
ATOM   5740 C CB  . VAL B 2 221 ? 128.075 153.624 112.367 1.00 74.22  ? 337 VAL D CB  1 
ATOM   5741 C CG1 . VAL B 2 221 ? 128.976 154.110 111.241 1.00 73.07  ? 337 VAL D CG1 1 
ATOM   5742 C CG2 . VAL B 2 221 ? 128.773 152.556 113.187 1.00 67.66  ? 337 VAL D CG2 1 
ATOM   5743 N N   . GLU B 2 222 ? 128.240 157.045 112.583 1.00 72.90  ? 338 GLU D N   1 
ATOM   5744 C CA  . GLU B 2 222 ? 128.143 158.291 111.839 1.00 74.54  ? 338 GLU D CA  1 
ATOM   5745 C C   . GLU B 2 222 ? 129.296 158.389 110.845 1.00 70.62  ? 338 GLU D C   1 
ATOM   5746 O O   . GLU B 2 222 ? 130.175 157.524 110.784 1.00 62.60  ? 338 GLU D O   1 
ATOM   5747 C CB  . GLU B 2 222 ? 128.127 159.487 112.792 1.00 71.46  ? 338 GLU D CB  1 
ATOM   5748 C CG  . GLU B 2 222 ? 127.125 159.359 113.927 1.00 76.93  ? 338 GLU D CG  1 
ATOM   5749 C CD  . GLU B 2 222 ? 126.158 160.525 113.987 1.00 78.74  ? 338 GLU D CD  1 
ATOM   5750 O OE1 . GLU B 2 222 ? 126.051 161.264 112.986 1.00 85.96  ? 338 GLU D OE1 1 
ATOM   5751 O OE2 . GLU B 2 222 ? 125.504 160.703 115.036 1.00 73.68  ? 338 GLU D OE2 1 
ATOM   5752 N N   . ALA B 2 223 ? 129.280 159.463 110.052 1.00 74.85  ? 339 ALA D N   1 
ATOM   5753 C CA  . ALA B 2 223 ? 130.336 159.671 109.066 1.00 71.63  ? 339 ALA D CA  1 
ATOM   5754 C C   . ALA B 2 223 ? 131.686 159.896 109.737 1.00 64.71  ? 339 ALA D C   1 
ATOM   5755 O O   . ALA B 2 223 ? 132.713 159.400 109.260 1.00 63.02  ? 339 ALA D O   1 
ATOM   5756 C CB  . ALA B 2 223 ? 129.983 160.849 108.159 1.00 67.24  ? 339 ALA D CB  1 
ATOM   5757 N N   . GLU B 2 224 ? 131.704 160.644 110.841 1.00 61.27  ? 340 GLU D N   1 
ATOM   5758 C CA  . GLU B 2 224 ? 132.944 160.928 111.553 1.00 54.46  ? 340 GLU D CA  1 
ATOM   5759 C C   . GLU B 2 224 ? 133.494 159.719 112.298 1.00 55.59  ? 340 GLU D C   1 
ATOM   5760 O O   . GLU B 2 224 ? 134.638 159.769 112.762 1.00 57.39  ? 340 GLU D O   1 
ATOM   5761 C CB  . GLU B 2 224 ? 132.729 162.077 112.538 1.00 53.72  ? 340 GLU D CB  1 
ATOM   5762 C CG  . GLU B 2 224 ? 131.843 161.713 113.720 1.00 59.70  ? 340 GLU D CG  1 
ATOM   5763 C CD  . GLU B 2 224 ? 131.587 162.888 114.643 1.00 59.80  ? 340 GLU D CD  1 
ATOM   5764 O OE1 . GLU B 2 224 ? 131.861 164.036 114.236 1.00 60.68  ? 340 GLU D OE1 1 
ATOM   5765 O OE2 . GLU B 2 224 ? 131.111 162.662 115.775 1.00 52.61  ? 340 GLU D OE2 1 
ATOM   5766 N N   . ASP B 2 225 ? 132.718 158.642 112.422 1.00 61.09  ? 341 ASP D N   1 
ATOM   5767 C CA  . ASP B 2 225 ? 133.136 157.485 113.202 1.00 53.82  ? 341 ASP D CA  1 
ATOM   5768 C C   . ASP B 2 225 ? 134.108 156.579 112.461 1.00 46.25  ? 341 ASP D C   1 
ATOM   5769 O O   . ASP B 2 225 ? 134.623 155.631 113.065 1.00 44.10  ? 341 ASP D O   1 
ATOM   5770 C CB  . ASP B 2 225 ? 131.911 156.675 113.631 1.00 61.37  ? 341 ASP D CB  1 
ATOM   5771 C CG  . ASP B 2 225 ? 131.400 157.075 114.998 1.00 63.55  ? 341 ASP D CG  1 
ATOM   5772 O OD1 . ASP B 2 225 ? 131.766 158.173 115.468 1.00 61.27  ? 341 ASP D OD1 1 
ATOM   5773 O OD2 . ASP B 2 225 ? 130.636 156.294 115.603 1.00 63.25  ? 341 ASP D OD2 1 
ATOM   5774 N N   . VAL B 2 226 ? 134.367 156.835 111.178 1.00 50.78  ? 342 VAL D N   1 
ATOM   5775 C CA  . VAL B 2 226 ? 135.275 155.988 110.415 1.00 54.13  ? 342 VAL D CA  1 
ATOM   5776 C C   . VAL B 2 226 ? 136.692 156.134 110.952 1.00 55.70  ? 342 VAL D C   1 
ATOM   5777 O O   . VAL B 2 226 ? 137.167 157.244 111.231 1.00 52.02  ? 342 VAL D O   1 
ATOM   5778 C CB  . VAL B 2 226 ? 135.200 156.326 108.915 1.00 53.47  ? 342 VAL D CB  1 
ATOM   5779 C CG1 . VAL B 2 226 ? 133.828 155.974 108.366 1.00 58.43  ? 342 VAL D CG1 1 
ATOM   5780 C CG2 . VAL B 2 226 ? 135.505 157.797 108.674 1.00 54.37  ? 342 VAL D CG2 1 
ATOM   5781 N N   . GLY B 2 227 ? 137.368 155.009 111.115 1.00 44.66  ? 343 GLY D N   1 
ATOM   5782 C CA  . GLY B 2 227 ? 138.714 155.008 111.647 1.00 31.26  ? 343 GLY D CA  1 
ATOM   5783 C C   . GLY B 2 227 ? 139.048 153.659 112.243 1.00 32.82  ? 343 GLY D C   1 
ATOM   5784 O O   . GLY B 2 227 ? 138.237 152.733 112.248 1.00 38.89  ? 343 GLY D O   1 
ATOM   5785 N N   . VAL B 2 228 ? 140.272 153.571 112.752 1.00 25.26  ? 344 VAL D N   1 
ATOM   5786 C CA  . VAL B 2 228 ? 140.782 152.338 113.340 1.00 24.25  ? 344 VAL D CA  1 
ATOM   5787 C C   . VAL B 2 228 ? 140.587 152.406 114.848 1.00 16.93  ? 344 VAL D C   1 
ATOM   5788 O O   . VAL B 2 228 ? 141.062 153.339 115.503 1.00 18.27  ? 344 VAL D O   1 
ATOM   5789 C CB  . VAL B 2 228 ? 142.260 152.123 112.984 1.00 24.64  ? 344 VAL D CB  1 
ATOM   5790 C CG1 . VAL B 2 228 ? 142.806 150.903 113.703 1.00 27.42  ? 344 VAL D CG1 1 
ATOM   5791 C CG2 . VAL B 2 228 ? 142.429 151.982 111.480 1.00 27.11  ? 344 VAL D CG2 1 
ATOM   5792 N N   . TYR B 2 229 ? 139.887 151.420 115.400 1.00 17.11  ? 345 TYR D N   1 
ATOM   5793 C CA  . TYR B 2 229 ? 139.637 151.340 116.833 1.00 16.62  ? 345 TYR D CA  1 
ATOM   5794 C C   . TYR B 2 229 ? 140.592 150.321 117.440 1.00 20.53  ? 345 TYR D C   1 
ATOM   5795 O O   . TYR B 2 229 ? 140.625 149.164 117.009 1.00 22.87  ? 345 TYR D O   1 
ATOM   5796 C CB  . TYR B 2 229 ? 138.188 150.951 117.125 1.00 22.65  ? 345 TYR D CB  1 
ATOM   5797 C CG  . TYR B 2 229 ? 137.161 151.966 116.674 1.00 30.29  ? 345 TYR D CG  1 
ATOM   5798 C CD1 . TYR B 2 229 ? 136.869 152.141 115.328 1.00 33.15  ? 345 TYR D CD1 1 
ATOM   5799 C CD2 . TYR B 2 229 ? 136.466 152.733 117.598 1.00 25.98  ? 345 TYR D CD2 1 
ATOM   5800 C CE1 . TYR B 2 229 ? 135.929 153.062 114.916 1.00 32.71  ? 345 TYR D CE1 1 
ATOM   5801 C CE2 . TYR B 2 229 ? 135.524 153.656 117.194 1.00 24.08  ? 345 TYR D CE2 1 
ATOM   5802 C CZ  . TYR B 2 229 ? 135.259 153.816 115.853 1.00 30.35  ? 345 TYR D CZ  1 
ATOM   5803 O OH  . TYR B 2 229 ? 134.320 154.734 115.444 1.00 40.74  ? 345 TYR D OH  1 
ATOM   5804 N N   . TYR B 2 230 ? 141.323 150.757 118.474 1.00 19.35  ? 346 TYR D N   1 
ATOM   5805 C CA  . TYR B 2 230 ? 142.344 149.885 119.111 1.00 17.63  ? 346 TYR D CA  1 
ATOM   5806 C C   . TYR B 2 230 ? 141.991 149.604 120.553 1.00 13.07  ? 346 TYR D C   1 
ATOM   5807 O O   . TYR B 2 230 ? 141.945 150.545 121.361 1.00 12.30  ? 346 TYR D O   1 
ATOM   5808 C CB  . TYR B 2 230 ? 143.717 150.558 119.152 1.00 13.02  ? 346 TYR D CB  1 
ATOM   5809 C CG  . TYR B 2 230 ? 144.280 151.052 117.829 1.00 14.15  ? 346 TYR D CG  1 
ATOM   5810 C CD1 . TYR B 2 230 ? 145.074 150.233 117.038 1.00 16.95  ? 346 TYR D CD1 1 
ATOM   5811 C CD2 . TYR B 2 230 ? 144.038 152.346 117.390 1.00 13.31  ? 346 TYR D CD2 1 
ATOM   5812 C CE1 . TYR B 2 230 ? 145.601 150.683 115.840 1.00 18.85  ? 346 TYR D CE1 1 
ATOM   5813 C CE2 . TYR B 2 230 ? 144.558 152.808 116.195 1.00 16.20  ? 346 TYR D CE2 1 
ATOM   5814 C CZ  . TYR B 2 230 ? 145.344 151.975 115.420 1.00 22.07  ? 346 TYR D CZ  1 
ATOM   5815 O OH  . TYR B 2 230 ? 145.849 152.427 114.239 1.00 28.69  ? 346 TYR D OH  1 
ATOM   5816 N N   . CYS B 2 231 ? 141.753 148.338 120.881 1.00 17.57  ? 347 CYS D N   1 
ATOM   5817 C CA  . CYS B 2 231 ? 141.534 147.956 122.267 1.00 17.71  ? 347 CYS D CA  1 
ATOM   5818 C C   . CYS B 2 231 ? 142.887 147.902 122.962 1.00 18.53  ? 347 CYS D C   1 
ATOM   5819 O O   . CYS B 2 231 ? 143.823 147.262 122.472 1.00 29.88  ? 347 CYS D O   1 
ATOM   5820 C CB  . CYS B 2 231 ? 140.798 146.617 122.373 1.00 29.75  ? 347 CYS D CB  1 
ATOM   5821 S SG  . CYS B 2 231 ? 141.749 145.127 121.998 1.00 50.53  ? 347 CYS D SG  1 
ATOM   5822 N N   . PHE B 2 232 ? 142.996 148.602 124.084 1.00 16.06  ? 348 PHE D N   1 
ATOM   5823 C CA  . PHE B 2 232 ? 144.270 148.832 124.742 1.00 14.33  ? 348 PHE D CA  1 
ATOM   5824 C C   . PHE B 2 232 ? 144.207 148.346 126.181 1.00 14.14  ? 348 PHE D C   1 
ATOM   5825 O O   . PHE B 2 232 ? 143.191 148.519 126.860 1.00 20.82  ? 348 PHE D O   1 
ATOM   5826 C CB  . PHE B 2 232 ? 144.640 150.323 124.692 1.00 12.38  ? 348 PHE D CB  1 
ATOM   5827 C CG  . PHE B 2 232 ? 145.740 150.713 125.637 1.00 12.82  ? 348 PHE D CG  1 
ATOM   5828 C CD1 . PHE B 2 232 ? 147.061 150.650 125.239 1.00 15.34  ? 348 PHE D CD1 1 
ATOM   5829 C CD2 . PHE B 2 232 ? 145.453 151.145 126.923 1.00 12.13  ? 348 PHE D CD2 1 
ATOM   5830 C CE1 . PHE B 2 232 ? 148.072 151.005 126.101 1.00 13.05  ? 348 PHE D CE1 1 
ATOM   5831 C CE2 . PHE B 2 232 ? 146.462 151.498 127.789 1.00 11.06  ? 348 PHE D CE2 1 
ATOM   5832 C CZ  . PHE B 2 232 ? 147.772 151.430 127.377 1.00 11.80  ? 348 PHE D CZ  1 
ATOM   5833 N N   . GLN B 2 233 ? 145.295 147.736 126.639 1.00 15.00  ? 349 GLN D N   1 
ATOM   5834 C CA  . GLN B 2 233 ? 145.452 147.356 128.034 1.00 21.58  ? 349 GLN D CA  1 
ATOM   5835 C C   . GLN B 2 233 ? 146.677 148.049 128.610 1.00 26.72  ? 349 GLN D C   1 
ATOM   5836 O O   . GLN B 2 233 ? 147.696 148.204 127.929 1.00 28.15  ? 349 GLN D O   1 
ATOM   5837 C CB  . GLN B 2 233 ? 145.573 145.835 128.195 1.00 24.19  ? 349 GLN D CB  1 
ATOM   5838 C CG  . GLN B 2 233 ? 146.896 145.247 127.738 1.00 25.58  ? 349 GLN D CG  1 
ATOM   5839 C CD  . GLN B 2 233 ? 147.839 144.970 128.889 1.00 31.02  ? 349 GLN D CD  1 
ATOM   5840 O OE1 . GLN B 2 233 ? 147.415 144.843 130.037 1.00 34.97  ? 349 GLN D OE1 1 
ATOM   5841 N NE2 . GLN B 2 233 ? 149.128 144.876 128.588 1.00 32.64  ? 349 GLN D NE2 1 
ATOM   5842 N N   . GLY B 2 234 ? 146.563 148.487 129.858 1.00 22.75  ? 350 GLY D N   1 
ATOM   5843 C CA  . GLY B 2 234 ? 147.682 149.091 130.549 1.00 18.69  ? 350 GLY D CA  1 
ATOM   5844 C C   . GLY B 2 234 ? 147.923 148.439 131.891 1.00 27.21  ? 350 GLY D C   1 
ATOM   5845 O O   . GLY B 2 234 ? 148.772 148.887 132.666 1.00 26.69  ? 350 GLY D O   1 
ATOM   5846 N N   . SER B 2 235 ? 147.180 147.367 132.172 1.00 34.52  ? 351 SER D N   1 
ATOM   5847 C CA  . SER B 2 235 ? 147.273 146.688 133.457 1.00 36.12  ? 351 SER D CA  1 
ATOM   5848 C C   . SER B 2 235 ? 148.520 145.827 133.587 1.00 36.29  ? 351 SER D C   1 
ATOM   5849 O O   . SER B 2 235 ? 148.871 145.447 134.708 1.00 41.43  ? 351 SER D O   1 
ATOM   5850 C CB  . SER B 2 235 ? 146.032 145.826 133.681 1.00 38.55  ? 351 SER D CB  1 
ATOM   5851 O OG  . SER B 2 235 ? 144.975 146.587 134.238 1.00 44.29  ? 351 SER D OG  1 
ATOM   5852 N N   . HIS B 2 236 ? 149.189 145.508 132.486 1.00 33.56  ? 352 HIS D N   1 
ATOM   5853 C CA  . HIS B 2 236 ? 150.417 144.729 132.513 1.00 39.44  ? 352 HIS D CA  1 
ATOM   5854 C C   . HIS B 2 236 ? 151.617 145.658 132.393 1.00 41.37  ? 352 HIS D C   1 
ATOM   5855 O O   . HIS B 2 236 ? 151.484 146.849 132.103 1.00 37.43  ? 352 HIS D O   1 
ATOM   5856 C CB  . HIS B 2 236 ? 150.426 143.683 131.393 1.00 45.23  ? 352 HIS D CB  1 
ATOM   5857 C CG  . HIS B 2 236 ? 151.004 142.365 131.805 1.00 57.47  ? 352 HIS D CG  1 
ATOM   5858 N ND1 . HIS B 2 236 ? 150.597 141.697 132.940 1.00 57.95  ? 352 HIS D ND1 1 
ATOM   5859 C CD2 . HIS B 2 236 ? 151.959 141.593 131.235 1.00 56.75  ? 352 HIS D CD2 1 
ATOM   5860 C CE1 . HIS B 2 236 ? 151.276 140.570 133.051 1.00 58.41  ? 352 HIS D CE1 1 
ATOM   5861 N NE2 . HIS B 2 236 ? 152.109 140.482 132.030 1.00 58.93  ? 352 HIS D NE2 1 
ATOM   5862 N N   . ILE B 2 237 ? 152.805 145.095 132.630 1.00 51.86  ? 353 ILE D N   1 
ATOM   5863 C CA  . ILE B 2 237 ? 154.024 145.905 132.595 1.00 51.54  ? 353 ILE D CA  1 
ATOM   5864 C C   . ILE B 2 237 ? 154.241 146.544 131.228 1.00 41.44  ? 353 ILE D C   1 
ATOM   5865 O O   . ILE B 2 237 ? 154.449 147.767 131.171 1.00 35.06  ? 353 ILE D O   1 
ATOM   5866 C CB  . ILE B 2 237 ? 155.228 145.072 133.072 1.00 55.39  ? 353 ILE D CB  1 
ATOM   5867 C CG1 . ILE B 2 237 ? 155.062 144.687 134.544 1.00 51.74  ? 353 ILE D CG1 1 
ATOM   5868 C CG2 . ILE B 2 237 ? 156.526 145.837 132.861 1.00 51.11  ? 353 ILE D CG2 1 
ATOM   5869 C CD1 . ILE B 2 237 ? 156.044 143.636 135.013 1.00 42.22  ? 353 ILE D CD1 1 
ATOM   5870 N N   . PRO B 2 238 ? 154.220 145.813 130.113 1.00 41.59  ? 354 PRO D N   1 
ATOM   5871 C CA  . PRO B 2 238 ? 154.162 146.477 128.812 1.00 34.34  ? 354 PRO D CA  1 
ATOM   5872 C C   . PRO B 2 238 ? 152.724 146.692 128.376 1.00 37.81  ? 354 PRO D C   1 
ATOM   5873 O O   . PRO B 2 238 ? 151.980 145.722 128.166 1.00 40.96  ? 354 PRO D O   1 
ATOM   5874 C CB  . PRO B 2 238 ? 154.889 145.495 127.883 1.00 37.31  ? 354 PRO D CB  1 
ATOM   5875 C CG  . PRO B 2 238 ? 154.700 144.149 128.524 1.00 45.94  ? 354 PRO D CG  1 
ATOM   5876 C CD  . PRO B 2 238 ? 154.244 144.346 129.953 1.00 47.38  ? 354 PRO D CD  1 
ATOM   5877 N N   . PRO B 2 239 ? 152.288 147.942 128.235 1.00 31.73  ? 355 PRO D N   1 
ATOM   5878 C CA  . PRO B 2 239 ? 150.969 148.190 127.642 1.00 25.14  ? 355 PRO D CA  1 
ATOM   5879 C C   . PRO B 2 239 ? 150.938 147.735 126.190 1.00 29.21  ? 355 PRO D C   1 
ATOM   5880 O O   . PRO B 2 239 ? 151.871 147.981 125.424 1.00 24.76  ? 355 PRO D O   1 
ATOM   5881 C CB  . PRO B 2 239 ? 150.807 149.708 127.768 1.00 16.11  ? 355 PRO D CB  1 
ATOM   5882 C CG  . PRO B 2 239 ? 151.689 150.084 128.903 1.00 23.59  ? 355 PRO D CG  1 
ATOM   5883 C CD  . PRO B 2 239 ? 152.870 149.166 128.807 1.00 29.54  ? 355 PRO D CD  1 
ATOM   5884 N N   . THR B 2 240 ? 149.853 147.061 125.814 1.00 28.09  ? 356 THR D N   1 
ATOM   5885 C CA  . THR B 2 240 ? 149.704 146.523 124.470 1.00 32.02  ? 356 THR D CA  1 
ATOM   5886 C C   . THR B 2 240 ? 148.362 146.936 123.888 1.00 23.79  ? 356 THR D C   1 
ATOM   5887 O O   . THR B 2 240 ? 147.337 146.895 124.574 1.00 22.55  ? 356 THR D O   1 
ATOM   5888 C CB  . THR B 2 240 ? 149.822 144.990 124.456 1.00 38.28  ? 356 THR D CB  1 
ATOM   5889 O OG1 . THR B 2 240 ? 148.811 144.421 125.296 1.00 36.08  ? 356 THR D OG1 1 
ATOM   5890 C CG2 . THR B 2 240 ? 151.193 144.549 124.946 1.00 36.28  ? 356 THR D CG2 1 
ATOM   5891 N N   . PHE B 2 241 ? 148.378 147.335 122.619 1.00 22.07  ? 357 PHE D N   1 
ATOM   5892 C CA  . PHE B 2 241 ? 147.169 147.662 121.886 1.00 19.54  ? 357 PHE D CA  1 
ATOM   5893 C C   . PHE B 2 241 ? 146.686 146.437 121.113 1.00 24.83  ? 357 PHE D C   1 
ATOM   5894 O O   . PHE B 2 241 ? 147.315 145.376 121.117 1.00 36.29  ? 357 PHE D O   1 
ATOM   5895 C CB  . PHE B 2 241 ? 147.412 148.825 120.922 1.00 20.41  ? 357 PHE D CB  1 
ATOM   5896 C CG  . PHE B 2 241 ? 147.799 150.116 121.588 1.00 19.17  ? 357 PHE D CG  1 
ATOM   5897 C CD1 . PHE B 2 241 ? 149.065 150.289 122.124 1.00 17.03  ? 357 PHE D CD1 1 
ATOM   5898 C CD2 . PHE B 2 241 ? 146.904 151.171 121.649 1.00 15.71  ? 357 PHE D CD2 1 
ATOM   5899 C CE1 . PHE B 2 241 ? 149.422 151.479 122.725 1.00 13.45  ? 357 PHE D CE1 1 
ATOM   5900 C CE2 . PHE B 2 241 ? 147.256 152.363 122.247 1.00 14.48  ? 357 PHE D CE2 1 
ATOM   5901 C CZ  . PHE B 2 241 ? 148.516 152.518 122.785 1.00 12.33  ? 357 PHE D CZ  1 
ATOM   5902 N N   . GLY B 2 242 ? 145.540 146.593 120.444 1.00 20.64  ? 358 GLY D N   1 
ATOM   5903 C CA  . GLY B 2 242 ? 145.020 145.509 119.591 1.00 24.51  ? 358 GLY D CA  1 
ATOM   5904 C C   . GLY B 2 242 ? 145.381 145.799 118.150 1.00 29.35  ? 358 GLY D C   1 
ATOM   5905 O O   . GLY B 2 242 ? 145.911 146.899 117.895 1.00 31.98  ? 358 GLY D O   1 
ATOM   5906 N N   . GLN B 2 243 ? 145.117 144.868 117.231 1.00 32.73  ? 359 GLN D N   1 
ATOM   5907 C CA  . GLN B 2 243 ? 145.549 145.070 115.822 1.00 34.87  ? 359 GLN D CA  1 
ATOM   5908 C C   . GLN B 2 243 ? 144.815 146.292 115.240 1.00 39.29  ? 359 GLN D C   1 
ATOM   5909 O O   . GLN B 2 243 ? 145.452 147.050 114.479 1.00 38.24  ? 359 GLN D O   1 
ATOM   5910 C CB  . GLN B 2 243 ? 145.350 143.795 114.998 1.00 40.36  ? 359 GLN D CB  1 
ATOM   5911 C CG  . GLN B 2 243 ? 143.937 143.583 114.464 1.00 45.66  ? 359 GLN D CG  1 
ATOM   5912 C CD  . GLN B 2 243 ? 142.980 143.000 115.481 1.00 48.89  ? 359 GLN D CD  1 
ATOM   5913 O OE1 . GLN B 2 243 ? 143.343 142.728 116.631 1.00 43.29  ? 359 GLN D OE1 1 
ATOM   5914 N NE2 . GLN B 2 243 ? 141.741 142.795 115.057 1.00 50.11  ? 359 GLN D NE2 1 
ATOM   5915 N N   . GLY B 2 244 ? 143.536 146.474 115.584 1.00 36.39  ? 360 GLY D N   1 
ATOM   5916 C CA  . GLY B 2 244 ? 142.770 147.641 115.107 1.00 28.71  ? 360 GLY D CA  1 
ATOM   5917 C C   . GLY B 2 244 ? 141.788 147.278 114.013 1.00 39.23  ? 360 GLY D C   1 
ATOM   5918 O O   . GLY B 2 244 ? 142.237 146.730 112.986 1.00 51.09  ? 360 GLY D O   1 
ATOM   5919 N N   . THR B 2 245 ? 140.498 147.568 114.212 1.00 35.07  ? 361 THR D N   1 
ATOM   5920 C CA  . THR B 2 245 ? 139.483 147.314 113.197 1.00 43.03  ? 361 THR D CA  1 
ATOM   5921 C C   . THR B 2 245 ? 139.190 148.614 112.462 1.00 38.37  ? 361 THR D C   1 
ATOM   5922 O O   . THR B 2 245 ? 138.749 149.592 113.074 1.00 37.08  ? 361 THR D O   1 
ATOM   5923 C CB  . THR B 2 245 ? 138.201 146.760 113.816 1.00 45.89  ? 361 THR D CB  1 
ATOM   5924 O OG1 . THR B 2 245 ? 137.526 147.802 114.532 1.00 47.42  ? 361 THR D OG1 1 
ATOM   5925 C CG2 . THR B 2 245 ? 138.514 145.624 114.762 1.00 40.11  ? 361 THR D CG2 1 
ATOM   5926 N N   . LYS B 2 246 ? 139.426 148.620 111.153 1.00 44.30  ? 362 LYS D N   1 
ATOM   5927 C CA  . LYS B 2 246 ? 139.181 149.802 110.330 1.00 47.98  ? 362 LYS D CA  1 
ATOM   5928 C C   . LYS B 2 246 ? 137.690 149.879 110.035 1.00 56.29  ? 362 LYS D C   1 
ATOM   5929 O O   . LYS B 2 246 ? 137.198 149.333 109.046 1.00 62.41  ? 362 LYS D O   1 
ATOM   5930 C CB  . LYS B 2 246 ? 140.004 149.746 109.050 1.00 50.83  ? 362 LYS D CB  1 
ATOM   5931 C CG  . LYS B 2 246 ? 139.962 151.026 108.233 1.00 52.70  ? 362 LYS D CG  1 
ATOM   5932 C CD  . LYS B 2 246 ? 141.137 151.105 107.275 1.00 55.47  ? 362 LYS D CD  1 
ATOM   5933 C CE  . LYS B 2 246 ? 142.409 151.518 107.996 1.00 54.27  ? 362 LYS D CE  1 
ATOM   5934 N NZ  . LYS B 2 246 ? 142.656 152.982 107.889 1.00 57.22  ? 362 LYS D NZ  1 
ATOM   5935 N N   . VAL B 2 247 ? 136.957 150.568 110.909 1.00 48.64  ? 363 VAL D N   1 
ATOM   5936 C CA  . VAL B 2 247 ? 135.529 150.765 110.693 1.00 55.83  ? 363 VAL D CA  1 
ATOM   5937 C C   . VAL B 2 247 ? 135.332 151.700 109.509 1.00 60.30  ? 363 VAL D C   1 
ATOM   5938 O O   . VAL B 2 247 ? 135.877 152.810 109.475 1.00 58.78  ? 363 VAL D O   1 
ATOM   5939 C CB  . VAL B 2 247 ? 134.862 151.315 111.962 1.00 50.11  ? 363 VAL D CB  1 
ATOM   5940 C CG1 . VAL B 2 247 ? 133.524 151.955 111.628 1.00 51.24  ? 363 VAL D CG1 1 
ATOM   5941 C CG2 . VAL B 2 247 ? 134.687 150.208 112.989 1.00 50.09  ? 363 VAL D CG2 1 
ATOM   5942 N N   . GLU B 2 248 ? 134.552 151.252 108.528 1.00 64.77  ? 364 GLU D N   1 
ATOM   5943 C CA  . GLU B 2 248 ? 134.357 151.997 107.295 1.00 68.40  ? 364 GLU D CA  1 
ATOM   5944 C C   . GLU B 2 248 ? 132.882 152.000 106.927 1.00 72.12  ? 364 GLU D C   1 
ATOM   5945 O O   . GLU B 2 248 ? 132.126 151.105 107.315 1.00 74.04  ? 364 GLU D O   1 
ATOM   5946 C CB  . GLU B 2 248 ? 135.187 151.406 106.148 1.00 73.42  ? 364 GLU D CB  1 
ATOM   5947 C CG  . GLU B 2 248 ? 134.946 149.925 105.913 1.00 79.30  ? 364 GLU D CG  1 
ATOM   5948 C CD  . GLU B 2 248 ? 135.897 149.333 104.893 1.00 78.69  ? 364 GLU D CD  1 
ATOM   5949 O OE1 . GLU B 2 248 ? 136.509 150.110 104.129 1.00 80.88  ? 364 GLU D OE1 1 
ATOM   5950 O OE2 . GLU B 2 248 ? 136.034 148.093 104.855 1.00 73.85  ? 364 GLU D OE2 1 
ATOM   5951 N N   . ILE B 2 249 ? 132.482 153.018 106.174 1.00 70.75  ? 365 ILE D N   1 
ATOM   5952 C CA  . ILE B 2 249 ? 131.100 153.151 105.732 1.00 79.46  ? 365 ILE D CA  1 
ATOM   5953 C C   . ILE B 2 249 ? 130.870 152.264 104.517 1.00 85.95  ? 365 ILE D C   1 
ATOM   5954 O O   . ILE B 2 249 ? 131.698 152.208 103.600 1.00 85.36  ? 365 ILE D O   1 
ATOM   5955 C CB  . ILE B 2 249 ? 130.771 154.622 105.424 1.00 80.84  ? 365 ILE D CB  1 
ATOM   5956 C CG1 . ILE B 2 249 ? 131.892 155.260 104.600 1.00 77.68  ? 365 ILE D CG1 1 
ATOM   5957 C CG2 . ILE B 2 249 ? 130.549 155.398 106.712 1.00 75.95  ? 365 ILE D CG2 1 
ATOM   5958 C CD1 . ILE B 2 249 ? 131.588 156.670 104.145 1.00 69.06  ? 365 ILE D CD1 1 
ATOM   5959 N N   . LYS B 2 250 ? 129.743 151.560 104.510 1.00 93.05  ? 366 LYS D N   1 
ATOM   5960 C CA  . LYS B 2 250 ? 129.395 150.684 103.397 1.00 95.31  ? 366 LYS D CA  1 
ATOM   5961 C C   . LYS B 2 250 ? 128.796 151.478 102.241 1.00 85.13  ? 366 LYS D C   1 
ATOM   5962 O O   . LYS B 2 250 ? 129.399 152.433 101.752 1.00 83.37  ? 366 LYS D O   1 
ATOM   5963 C CB  . LYS B 2 250 ? 128.418 149.598 103.851 1.00 92.51  ? 366 LYS D CB  1 
ATOM   5964 C CG  . LYS B 2 250 ? 129.082 148.291 104.250 1.00 87.52  ? 366 LYS D CG  1 
ATOM   5965 C CD  . LYS B 2 250 ? 128.063 147.172 104.392 1.00 85.98  ? 366 LYS D CD  1 
ATOM   5966 C CE  . LYS B 2 250 ? 127.400 147.196 105.759 1.00 81.21  ? 366 LYS D CE  1 
ATOM   5967 N NZ  . LYS B 2 250 ? 127.392 145.851 106.396 1.00 76.92  ? 366 LYS D NZ  1 
HETATM 5968 C C1  . NAG C 3 .   ? 152.909 154.591 143.668 1.00 19.21  ? 1   NAG B C1  1 
HETATM 5969 C C2  . NAG C 3 .   ? 153.917 155.171 142.673 1.00 16.78  ? 1   NAG B C2  1 
HETATM 5970 C C3  . NAG C 3 .   ? 154.551 153.972 141.976 1.00 18.73  ? 1   NAG B C3  1 
HETATM 5971 C C4  . NAG C 3 .   ? 155.017 152.876 142.956 1.00 20.02  ? 1   NAG B C4  1 
HETATM 5972 C C5  . NAG C 3 .   ? 154.116 152.720 144.198 1.00 16.47  ? 1   NAG B C5  1 
HETATM 5973 C C6  . NAG C 3 .   ? 154.771 151.978 145.343 1.00 15.76  ? 1   NAG B C6  1 
HETATM 5974 C C7  . NAG C 3 .   ? 153.627 157.369 141.592 1.00 16.89  ? 1   NAG B C7  1 
HETATM 5975 C C8  . NAG C 3 .   ? 152.854 158.155 140.553 1.00 10.67  ? 1   NAG B C8  1 
HETATM 5976 N N2  . NAG C 3 .   ? 153.295 156.072 141.726 1.00 19.44  ? 1   NAG B N2  1 
HETATM 5977 O O3  . NAG C 3 .   ? 155.581 154.476 141.170 1.00 22.64  ? 1   NAG B O3  1 
HETATM 5978 O O4  . NAG C 3 .   ? 154.991 151.666 142.224 1.00 27.31  ? 1   NAG B O4  1 
HETATM 5979 O O5  . NAG C 3 .   ? 153.621 153.952 144.698 1.00 21.14  ? 1   NAG B O5  1 
HETATM 5980 O O6  . NAG C 3 .   ? 153.902 151.959 146.450 1.00 20.80  ? 1   NAG B O6  1 
HETATM 5981 O O7  . NAG C 3 .   ? 154.496 157.899 142.269 1.00 19.39  ? 1   NAG B O7  1 
HETATM 5982 C C1  . NAG C 3 .   ? 156.314 151.149 142.027 1.00 24.45  ? 2   NAG B C1  1 
HETATM 5983 C C2  . NAG C 3 .   ? 156.261 149.629 142.219 1.00 20.38  ? 2   NAG B C2  1 
HETATM 5984 C C3  . NAG C 3 .   ? 157.638 149.039 141.964 1.00 27.56  ? 2   NAG B C3  1 
HETATM 5985 C C4  . NAG C 3 .   ? 158.109 149.449 140.577 1.00 32.99  ? 2   NAG B C4  1 
HETATM 5986 C C5  . NAG C 3 .   ? 158.067 150.976 140.438 1.00 28.75  ? 2   NAG B C5  1 
HETATM 5987 C C6  . NAG C 3 .   ? 158.489 151.461 139.067 1.00 35.22  ? 2   NAG B C6  1 
HETATM 5988 C C7  . NAG C 3 .   ? 154.608 148.689 143.767 1.00 16.07  ? 2   NAG B C7  1 
HETATM 5989 C C8  . NAG C 3 .   ? 154.320 148.384 145.215 1.00 16.46  ? 2   NAG B C8  1 
HETATM 5990 N N2  . NAG C 3 .   ? 155.799 149.266 143.530 1.00 19.37  ? 2   NAG B N2  1 
HETATM 5991 O O3  . NAG C 3 .   ? 157.519 147.648 142.093 1.00 29.75  ? 2   NAG B O3  1 
HETATM 5992 O O4  . NAG C 3 .   ? 159.416 148.951 140.430 1.00 33.94  ? 2   NAG B O4  1 
HETATM 5993 O O5  . NAG C 3 .   ? 156.764 151.447 140.727 1.00 27.52  ? 2   NAG B O5  1 
HETATM 5994 O O6  . NAG C 3 .   ? 158.131 152.812 138.900 1.00 46.63  ? 2   NAG B O6  1 
HETATM 5995 O O7  . NAG C 3 .   ? 153.803 148.424 142.887 1.00 15.94  ? 2   NAG B O7  1 
HETATM 5996 C C1  . NAG D 3 .   ? 142.327 178.267 147.419 1.00 45.71  ? 1   NAG C C1  1 
HETATM 5997 C C2  . NAG D 3 .   ? 140.921 177.676 147.236 1.00 47.02  ? 1   NAG C C2  1 
HETATM 5998 C C3  . NAG D 3 .   ? 139.887 178.798 147.326 1.00 56.44  ? 1   NAG C C3  1 
HETATM 5999 C C4  . NAG D 3 .   ? 140.067 179.584 148.619 1.00 59.15  ? 1   NAG C C4  1 
HETATM 6000 C C5  . NAG D 3 .   ? 141.506 180.104 148.678 1.00 51.02  ? 1   NAG C C5  1 
HETATM 6001 C C6  . NAG D 3 .   ? 141.843 180.896 149.923 1.00 53.51  ? 1   NAG C C6  1 
HETATM 6002 C C7  . NAG D 3 .   ? 140.183 175.812 145.765 1.00 52.58  ? 1   NAG C C7  1 
HETATM 6003 C C8  . NAG D 3 .   ? 139.531 175.180 146.972 1.00 50.10  ? 1   NAG C C8  1 
HETATM 6004 N N2  . NAG D 3 .   ? 140.813 176.986 145.977 1.00 51.22  ? 1   NAG C N2  1 
HETATM 6005 O O3  . NAG D 3 .   ? 138.607 178.232 147.233 1.00 60.43  ? 1   NAG C O3  1 
HETATM 6006 O O4  . NAG D 3 .   ? 139.114 180.622 148.611 1.00 57.48  ? 1   NAG C O4  1 
HETATM 6007 O O5  . NAG D 3 .   ? 142.379 178.997 148.622 1.00 49.04  ? 1   NAG C O5  1 
HETATM 6008 O O6  . NAG D 3 .   ? 143.236 180.900 150.121 1.00 42.19  ? 1   NAG C O6  1 
HETATM 6009 O O7  . NAG D 3 .   ? 140.128 175.277 144.668 1.00 52.67  ? 1   NAG C O7  1 
HETATM 6010 C C1  . NAG D 3 .   ? 138.323 180.533 149.815 1.00 15.60  ? 2   NAG C C1  1 
HETATM 6011 C C2  . NAG D 3 .   ? 137.772 181.932 150.124 1.00 15.60  ? 2   NAG C C2  1 
HETATM 6012 C C3  . NAG D 3 .   ? 136.877 181.877 151.360 1.00 15.60  ? 2   NAG C C3  1 
HETATM 6013 C C4  . NAG D 3 .   ? 135.827 180.780 151.222 1.00 15.60  ? 2   NAG C C4  1 
HETATM 6014 C C5  . NAG D 3 .   ? 136.514 179.459 150.860 1.00 15.60  ? 2   NAG C C5  1 
HETATM 6015 C C6  . NAG D 3 .   ? 135.563 178.294 150.691 1.00 15.60  ? 2   NAG C C6  1 
HETATM 6016 C C7  . NAG D 3 .   ? 139.327 183.690 149.369 1.00 15.60  ? 2   NAG C C7  1 
HETATM 6017 C C8  . NAG D 3 .   ? 140.467 184.576 149.808 1.00 15.60  ? 2   NAG C C8  1 
HETATM 6018 N N2  . NAG D 3 .   ? 138.852 182.861 150.317 1.00 15.60  ? 2   NAG C N2  1 
HETATM 6019 O O3  . NAG D 3 .   ? 136.294 183.143 151.530 1.00 15.60  ? 2   NAG C O3  1 
HETATM 6020 O O4  . NAG D 3 .   ? 135.147 180.692 152.453 1.00 15.60  ? 2   NAG C O4  1 
HETATM 6021 O O5  . NAG D 3 .   ? 137.244 179.638 149.663 1.00 15.60  ? 2   NAG C O5  1 
HETATM 6022 O O6  . NAG D 3 .   ? 134.985 177.971 151.934 1.00 15.60  ? 2   NAG C O6  1 
HETATM 6023 O O7  . NAG D 3 .   ? 138.884 183.736 148.232 1.00 15.60  ? 2   NAG C O7  1 
HETATM 6024 C C1  . NAG E 4 .   ? 149.642 152.403 164.245 1.00 78.54  ? 701 NAG A C1  1 
HETATM 6025 C C2  . NAG E 4 .   ? 148.621 151.303 163.927 1.00 80.39  ? 701 NAG A C2  1 
HETATM 6026 C C3  . NAG E 4 .   ? 147.287 151.597 164.611 1.00 85.62  ? 701 NAG A C3  1 
HETATM 6027 C C4  . NAG E 4 .   ? 147.500 151.846 166.099 1.00 92.71  ? 701 NAG A C4  1 
HETATM 6028 C C5  . NAG E 4 .   ? 148.549 152.947 166.275 1.00 88.38  ? 701 NAG A C5  1 
HETATM 6029 C C6  . NAG E 4 .   ? 148.853 153.278 167.719 1.00 78.78  ? 701 NAG A C6  1 
HETATM 6030 C C7  . NAG E 4 .   ? 149.000 150.174 161.771 1.00 85.00  ? 701 NAG A C7  1 
HETATM 6031 C C8  . NAG E 4 .   ? 148.678 150.215 160.298 1.00 80.25  ? 701 NAG A C8  1 
HETATM 6032 N N2  . NAG E 4 .   ? 148.446 151.156 162.506 1.00 80.31  ? 701 NAG A N2  1 
HETATM 6033 O O3  . NAG E 4 .   ? 146.433 150.508 164.378 1.00 82.51  ? 701 NAG A O3  1 
HETATM 6034 O O4  . NAG E 4 .   ? 146.256 152.214 166.648 1.00 92.18  ? 701 NAG A O4  1 
HETATM 6035 O O5  . NAG E 4 .   ? 149.746 152.540 165.644 1.00 85.85  ? 701 NAG A O5  1 
HETATM 6036 O O6  . NAG E 4 .   ? 147.690 153.758 168.352 1.00 77.12  ? 701 NAG A O6  1 
HETATM 6037 O O7  . NAG E 4 .   ? 149.717 149.304 162.243 1.00 85.07  ? 701 NAG A O7  1 
HETATM 6038 C C1  . NAG F 4 .   ? 154.685 190.752 178.747 1.00 67.20  ? 702 NAG A C1  1 
HETATM 6039 C C2  . NAG F 4 .   ? 155.388 191.290 177.490 1.00 63.54  ? 702 NAG A C2  1 
HETATM 6040 C C3  . NAG F 4 .   ? 155.039 192.765 177.288 1.00 66.51  ? 702 NAG A C3  1 
HETATM 6041 C C4  . NAG F 4 .   ? 153.532 192.992 177.360 1.00 64.39  ? 702 NAG A C4  1 
HETATM 6042 C C5  . NAG F 4 .   ? 152.992 192.389 178.659 1.00 63.10  ? 702 NAG A C5  1 
HETATM 6043 C C6  . NAG F 4 .   ? 151.500 192.547 178.846 1.00 61.61  ? 702 NAG A C6  1 
HETATM 6044 C C7  . NAG F 4 .   ? 157.658 191.025 176.552 1.00 67.91  ? 702 NAG A C7  1 
HETATM 6045 C C8  . NAG F 4 .   ? 159.111 190.849 176.919 1.00 66.79  ? 702 NAG A C8  1 
HETATM 6046 N N2  . NAG F 4 .   ? 156.813 191.119 177.596 1.00 65.78  ? 702 NAG A N2  1 
HETATM 6047 O O3  . NAG F 4 .   ? 155.565 193.174 176.054 1.00 63.69  ? 702 NAG A O3  1 
HETATM 6048 O O4  . NAG F 4 .   ? 153.315 194.383 177.302 1.00 54.13  ? 702 NAG A O4  1 
HETATM 6049 O O5  . NAG F 4 .   ? 153.303 191.013 178.671 1.00 63.45  ? 702 NAG A O5  1 
HETATM 6050 O O6  . NAG F 4 .   ? 150.816 191.870 177.819 1.00 59.90  ? 702 NAG A O6  1 
HETATM 6051 O O7  . NAG F 4 .   ? 157.297 191.082 175.386 1.00 72.82  ? 702 NAG A O7  1 
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