data_9IP7
# 
_entry.id   9IP7 
# 
_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   9IP7         pdb_00009ip7 10.2210/pdb9ip7/pdb 
WWPDB D_1300049144 ?            ?                   
EMDB  EMD-60764    ?            ?                   
# 
_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                        9IP7 
_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 HL-type bispecific diabody Ex3) complex' 
_pdbx_database_related.db_id          EMD-60764 
_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 HL-type bispecific diabody Ex3'                                              27093.129 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 
;DIVMTQSPLSLPVTPGEPASISCRSSQNIVHNNGITYLEWYLQKPGQSPQLLIYKVSDRFSGVPDRFSGSGSGTDFTLKI
SRVEAEDVGVYYCFQGSHIPPTFGQGTKVEIKRAAAAGGGGSGGGGSGGGGSGGGGSQVQLVQSGAEVKKPGASVKVSCK
ASGYTFTSYWMHWVRQAPGQGLEWMGNIWPGSGGTNYAEKFKNRVTMTRDTSISTAYMELSRLRSDDTAVYYCARSGGPY
FFDYWGQGTLVTVSS
;
;DIVMTQSPLSLPVTPGEPASISCRSSQNIVHNNGITYLEWYLQKPGQSPQLLIYKVSDRFSGVPDRFSGSGSGTDFTLKI
SRVEAEDVGVYYCFQGSHIPPTFGQGTKVEIKRAAAAGGGGSGGGGSGGGGSGGGGSQVQLVQSGAEVKKPGASVKVSCK
ASGYTFTSYWMHWVRQAPGQGLEWMGNIWPGSGGTNYAEKFKNRVTMTRDTSISTAYMELSRLRSDDTAVYYCARSGGPY
FFDYWGQGTLVTVSS
;
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   ASP n 
2 2   ILE n 
2 3   VAL n 
2 4   MET n 
2 5   THR n 
2 6   GLN n 
2 7   SER n 
2 8   PRO n 
2 9   LEU n 
2 10  SER n 
2 11  LEU n 
2 12  PRO n 
2 13  VAL n 
2 14  THR n 
2 15  PRO n 
2 16  GLY n 
2 17  GLU n 
2 18  PRO n 
2 19  ALA n 
2 20  SER n 
2 21  ILE n 
2 22  SER n 
2 23  CYS n 
2 24  ARG n 
2 25  SER n 
2 26  SER n 
2 27  GLN n 
2 28  ASN n 
2 29  ILE n 
2 30  VAL n 
2 31  HIS n 
2 32  ASN n 
2 33  ASN n 
2 34  GLY n 
2 35  ILE n 
2 36  THR n 
2 37  TYR n 
2 38  LEU n 
2 39  GLU n 
2 40  TRP n 
2 41  TYR n 
2 42  LEU n 
2 43  GLN n 
2 44  LYS n 
2 45  PRO n 
2 46  GLY n 
2 47  GLN n 
2 48  SER n 
2 49  PRO n 
2 50  GLN n 
2 51  LEU n 
2 52  LEU n 
2 53  ILE n 
2 54  TYR n 
2 55  LYS n 
2 56  VAL n 
2 57  SER n 
2 58  ASP n 
2 59  ARG n 
2 60  PHE n 
2 61  SER n 
2 62  GLY n 
2 63  VAL n 
2 64  PRO n 
2 65  ASP n 
2 66  ARG n 
2 67  PHE n 
2 68  SER n 
2 69  GLY n 
2 70  SER n 
2 71  GLY n 
2 72  SER n 
2 73  GLY n 
2 74  THR n 
2 75  ASP n 
2 76  PHE n 
2 77  THR n 
2 78  LEU n 
2 79  LYS n 
2 80  ILE n 
2 81  SER n 
2 82  ARG n 
2 83  VAL n 
2 84  GLU n 
2 85  ALA n 
2 86  GLU n 
2 87  ASP n 
2 88  VAL n 
2 89  GLY n 
2 90  VAL n 
2 91  TYR n 
2 92  TYR n 
2 93  CYS n 
2 94  PHE n 
2 95  GLN n 
2 96  GLY n 
2 97  SER n 
2 98  HIS n 
2 99  ILE n 
2 100 PRO n 
2 101 PRO n 
2 102 THR n 
2 103 PHE n 
2 104 GLY n 
2 105 GLN n 
2 106 GLY n 
2 107 THR n 
2 108 LYS n 
2 109 VAL n 
2 110 GLU n 
2 111 ILE n 
2 112 LYS n 
2 113 ARG n 
2 114 ALA n 
2 115 ALA n 
2 116 ALA n 
2 117 ALA n 
2 118 GLY n 
2 119 GLY n 
2 120 GLY n 
2 121 GLY n 
2 122 SER n 
2 123 GLY n 
2 124 GLY n 
2 125 GLY n 
2 126 GLY n 
2 127 SER n 
2 128 GLY n 
2 129 GLY n 
2 130 GLY n 
2 131 GLY n 
2 132 SER n 
2 133 GLY n 
2 134 GLY n 
2 135 GLY n 
2 136 GLY n 
2 137 SER n 
2 138 GLN n 
2 139 VAL n 
2 140 GLN n 
2 141 LEU n 
2 142 VAL n 
2 143 GLN n 
2 144 SER n 
2 145 GLY n 
2 146 ALA n 
2 147 GLU n 
2 148 VAL n 
2 149 LYS n 
2 150 LYS n 
2 151 PRO n 
2 152 GLY n 
2 153 ALA n 
2 154 SER n 
2 155 VAL n 
2 156 LYS n 
2 157 VAL n 
2 158 SER n 
2 159 CYS n 
2 160 LYS n 
2 161 ALA n 
2 162 SER n 
2 163 GLY n 
2 164 TYR n 
2 165 THR n 
2 166 PHE n 
2 167 THR n 
2 168 SER n 
2 169 TYR n 
2 170 TRP n 
2 171 MET n 
2 172 HIS n 
2 173 TRP n 
2 174 VAL n 
2 175 ARG n 
2 176 GLN n 
2 177 ALA n 
2 178 PRO n 
2 179 GLY n 
2 180 GLN n 
2 181 GLY n 
2 182 LEU n 
2 183 GLU n 
2 184 TRP n 
2 185 MET n 
2 186 GLY n 
2 187 ASN n 
2 188 ILE n 
2 189 TRP n 
2 190 PRO n 
2 191 GLY n 
2 192 SER n 
2 193 GLY n 
2 194 GLY n 
2 195 THR n 
2 196 ASN n 
2 197 TYR n 
2 198 ALA n 
2 199 GLU n 
2 200 LYS n 
2 201 PHE n 
2 202 LYS n 
2 203 ASN n 
2 204 ARG n 
2 205 VAL n 
2 206 THR n 
2 207 MET n 
2 208 THR n 
2 209 ARG n 
2 210 ASP n 
2 211 THR n 
2 212 SER n 
2 213 ILE n 
2 214 SER n 
2 215 THR n 
2 216 ALA n 
2 217 TYR n 
2 218 MET n 
2 219 GLU n 
2 220 LEU n 
2 221 SER n 
2 222 ARG n 
2 223 LEU n 
2 224 ARG n 
2 225 SER n 
2 226 ASP n 
2 227 ASP n 
2 228 THR n 
2 229 ALA n 
2 230 VAL n 
2 231 TYR n 
2 232 TYR n 
2 233 CYS n 
2 234 ALA n 
2 235 ARG n 
2 236 SER n 
2 237 GLY n 
2 238 GLY n 
2 239 PRO n 
2 240 TYR n 
2 241 PHE n 
2 242 PHE n 
2 243 ASP n 
2 244 TYR n 
2 245 TRP n 
2 246 GLY n 
2 247 GLN n 
2 248 GLY n 
2 249 THR n 
2 250 LEU n 
2 251 VAL n 
2 252 THR n 
2 253 VAL n 
2 254 SER n 
2 255 SER 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' 1 255 ?     ? ?                         ? ? ? ? ? ? '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  ?   ?   ?   A . n 
A 1 20  PHE 20  20  ?   ?   ?   A . n 
A 1 21  GLU 21  21  ?   ?   ?   A . n 
A 1 22  ASP 22  22  ?   ?   ?   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  ?   ?   ?   A . n 
A 1 47  GLN 47  47  ?   ?   ?   A . n 
A 1 48  ARG 48  48  ?   ?   ?   A . n 
A 1 49  ASN 49  49  ?   ?   ?   A . n 
A 1 50  TYR 50  50  ?   ?   ?   A . n 
A 1 51  ASP 51  51  ?   ?   ?   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  ?   ?   ?   A . n 
A 1 71  THR 71  71  ?   ?   ?   A . n 
A 1 72  VAL 72  72  ?   ?   ?   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 ?   ?   ?   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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 217 THR 217 217 ?   ?   ?   A . n 
A 1 218 GLY 218 218 ?   ?   ?   A . n 
A 1 219 PRO 219 219 ?   ?   ?   A . n 
A 1 220 ARG 220 220 ?   ?   ?   A . n 
A 1 221 GLU 221 221 ?   ?   ?   A . n 
A 1 222 SER 222 222 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 589 ALA 589 589 ?   ?   ?   A . n 
A 1 590 GLY 590 590 ?   ?   ?   A . n 
A 1 591 HIS 591 591 ?   ?   ?   A . n 
A 1 592 VAL 592 592 ?   ?   ?   A . n 
A 1 593 CYS 593 593 ?   ?   ?   A . n 
A 1 594 HIS 594 594 ?   ?   ?   A . n 
A 1 595 LEU 595 595 ?   ?   ?   A . n 
A 1 596 CYS 596 596 ?   ?   ?   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   ASP 1   131 131 ASP ASP D . n 
B 2 2   ILE 2   132 132 ILE ILE D . n 
B 2 3   VAL 3   133 133 VAL VAL D . n 
B 2 4   MET 4   134 134 MET MET D . n 
B 2 5   THR 5   135 135 THR THR D . n 
B 2 6   GLN 6   136 136 GLN GLN D . n 
B 2 7   SER 7   137 137 SER SER D . n 
B 2 8   PRO 8   138 138 PRO PRO D . n 
B 2 9   LEU 9   139 139 LEU LEU D . n 
B 2 10  SER 10  140 140 SER SER D . n 
B 2 11  LEU 11  141 141 LEU LEU D . n 
B 2 12  PRO 12  142 142 PRO PRO D . n 
B 2 13  VAL 13  143 143 VAL VAL D . n 
B 2 14  THR 14  144 144 THR THR D . n 
B 2 15  PRO 15  145 145 PRO PRO D . n 
B 2 16  GLY 16  146 146 GLY GLY D . n 
B 2 17  GLU 17  147 147 GLU GLU D . n 
B 2 18  PRO 18  148 148 PRO PRO D . n 
B 2 19  ALA 19  149 149 ALA ALA D . n 
B 2 20  SER 20  150 150 SER SER D . n 
B 2 21  ILE 21  151 151 ILE ILE D . n 
B 2 22  SER 22  152 152 SER SER D . n 
B 2 23  CYS 23  153 153 CYS CYS D . n 
B 2 24  ARG 24  154 154 ARG ARG D . n 
B 2 25  SER 25  155 155 SER SER D . n 
B 2 26  SER 26  156 156 SER SER D . n 
B 2 27  GLN 27  157 157 GLN GLN D . n 
B 2 28  ASN 28  158 158 ASN ASN D . n 
B 2 29  ILE 29  159 159 ILE ILE D . n 
B 2 30  VAL 30  160 160 VAL VAL D . n 
B 2 31  HIS 31  161 161 HIS HIS D . n 
B 2 32  ASN 32  162 162 ASN ASN D . n 
B 2 33  ASN 33  163 163 ASN ASN D . n 
B 2 34  GLY 34  164 164 GLY GLY D . n 
B 2 35  ILE 35  165 165 ILE ILE D . n 
B 2 36  THR 36  166 166 THR THR D . n 
B 2 37  TYR 37  167 167 TYR TYR D . n 
B 2 38  LEU 38  168 168 LEU LEU D . n 
B 2 39  GLU 39  169 169 GLU GLU D . n 
B 2 40  TRP 40  170 170 TRP TRP D . n 
B 2 41  TYR 41  171 171 TYR TYR D . n 
B 2 42  LEU 42  172 172 LEU LEU D . n 
B 2 43  GLN 43  173 173 GLN GLN D . n 
B 2 44  LYS 44  174 174 LYS LYS D . n 
B 2 45  PRO 45  175 175 PRO PRO D . n 
B 2 46  GLY 46  176 176 GLY GLY D . n 
B 2 47  GLN 47  177 177 GLN GLN D . n 
B 2 48  SER 48  178 178 SER SER D . n 
B 2 49  PRO 49  179 179 PRO PRO D . n 
B 2 50  GLN 50  180 180 GLN GLN D . n 
B 2 51  LEU 51  181 181 LEU LEU D . n 
B 2 52  LEU 52  182 182 LEU LEU D . n 
B 2 53  ILE 53  183 183 ILE ILE D . n 
B 2 54  TYR 54  184 184 TYR TYR D . n 
B 2 55  LYS 55  185 185 LYS LYS D . n 
B 2 56  VAL 56  186 186 VAL VAL D . n 
B 2 57  SER 57  187 187 SER SER D . n 
B 2 58  ASP 58  188 188 ASP ASP D . n 
B 2 59  ARG 59  189 189 ARG ARG D . n 
B 2 60  PHE 60  190 190 PHE PHE D . n 
B 2 61  SER 61  191 191 SER SER D . n 
B 2 62  GLY 62  192 192 GLY GLY D . n 
B 2 63  VAL 63  193 193 VAL VAL D . n 
B 2 64  PRO 64  194 194 PRO PRO D . n 
B 2 65  ASP 65  195 195 ASP ASP D . n 
B 2 66  ARG 66  196 196 ARG ARG D . n 
B 2 67  PHE 67  197 197 PHE PHE D . n 
B 2 68  SER 68  198 198 SER SER D . n 
B 2 69  GLY 69  199 199 GLY GLY D . n 
B 2 70  SER 70  200 200 SER SER D . n 
B 2 71  GLY 71  201 201 GLY GLY D . n 
B 2 72  SER 72  202 202 SER SER D . n 
B 2 73  GLY 73  203 203 GLY GLY D . n 
B 2 74  THR 74  204 204 THR THR D . n 
B 2 75  ASP 75  205 205 ASP ASP D . n 
B 2 76  PHE 76  206 206 PHE PHE D . n 
B 2 77  THR 77  207 207 THR THR D . n 
B 2 78  LEU 78  208 208 LEU LEU D . n 
B 2 79  LYS 79  209 209 LYS LYS D . n 
B 2 80  ILE 80  210 210 ILE ILE D . n 
B 2 81  SER 81  211 211 SER SER D . n 
B 2 82  ARG 82  212 212 ARG ARG D . n 
B 2 83  VAL 83  213 213 VAL VAL D . n 
B 2 84  GLU 84  214 214 GLU GLU D . n 
B 2 85  ALA 85  215 215 ALA ALA D . n 
B 2 86  GLU 86  216 216 GLU GLU D . n 
B 2 87  ASP 87  217 217 ASP ASP D . n 
B 2 88  VAL 88  218 218 VAL VAL D . n 
B 2 89  GLY 89  219 219 GLY GLY D . n 
B 2 90  VAL 90  220 220 VAL VAL D . n 
B 2 91  TYR 91  221 221 TYR TYR D . n 
B 2 92  TYR 92  222 222 TYR TYR D . n 
B 2 93  CYS 93  223 223 CYS CYS D . n 
B 2 94  PHE 94  224 224 PHE PHE D . n 
B 2 95  GLN 95  225 225 GLN GLN D . n 
B 2 96  GLY 96  226 226 GLY GLY D . n 
B 2 97  SER 97  227 227 SER SER D . n 
B 2 98  HIS 98  228 228 HIS HIS D . n 
B 2 99  ILE 99  229 229 ILE ILE D . n 
B 2 100 PRO 100 230 230 PRO PRO D . n 
B 2 101 PRO 101 231 231 PRO PRO D . n 
B 2 102 THR 102 232 232 THR THR D . n 
B 2 103 PHE 103 233 233 PHE PHE D . n 
B 2 104 GLY 104 234 234 GLY GLY D . n 
B 2 105 GLN 105 235 235 GLN GLN D . n 
B 2 106 GLY 106 236 236 GLY GLY D . n 
B 2 107 THR 107 237 237 THR THR D . n 
B 2 108 LYS 108 238 238 LYS LYS D . n 
B 2 109 VAL 109 239 239 VAL VAL D . n 
B 2 110 GLU 110 240 240 GLU GLU D . n 
B 2 111 ILE 111 241 241 ILE ILE D . n 
B 2 112 LYS 112 242 242 LYS LYS D . n 
B 2 113 ARG 113 243 ?   ?   ?   D . n 
B 2 114 ALA 114 244 ?   ?   ?   D . n 
B 2 115 ALA 115 245 ?   ?   ?   D . n 
B 2 116 ALA 116 246 ?   ?   ?   D . n 
B 2 117 ALA 117 247 ?   ?   ?   D . n 
B 2 118 GLY 118 248 ?   ?   ?   D . n 
B 2 119 GLY 119 249 ?   ?   ?   D . n 
B 2 120 GLY 120 250 ?   ?   ?   D . n 
B 2 121 GLY 121 251 ?   ?   ?   D . n 
B 2 122 SER 122 252 ?   ?   ?   D . n 
B 2 123 GLY 123 253 ?   ?   ?   D . n 
B 2 124 GLY 124 254 ?   ?   ?   D . n 
B 2 125 GLY 125 255 ?   ?   ?   D . n 
B 2 126 GLY 126 256 ?   ?   ?   D . n 
B 2 127 SER 127 257 ?   ?   ?   D . n 
B 2 128 GLY 128 258 ?   ?   ?   D . n 
B 2 129 GLY 129 259 ?   ?   ?   D . n 
B 2 130 GLY 130 260 ?   ?   ?   D . n 
B 2 131 GLY 131 261 ?   ?   ?   D . n 
B 2 132 SER 132 262 ?   ?   ?   D . n 
B 2 133 GLY 133 263 ?   ?   ?   D . n 
B 2 134 GLY 134 264 ?   ?   ?   D . n 
B 2 135 GLY 135 265 ?   ?   ?   D . n 
B 2 136 GLY 136 266 ?   ?   ?   D . n 
B 2 137 SER 137 267 ?   ?   ?   D . n 
B 2 138 GLN 138 268 268 GLN GLN D . n 
B 2 139 VAL 139 269 269 VAL VAL D . n 
B 2 140 GLN 140 270 270 GLN GLN D . n 
B 2 141 LEU 141 271 271 LEU LEU D . n 
B 2 142 VAL 142 272 272 VAL VAL D . n 
B 2 143 GLN 143 273 273 GLN GLN D . n 
B 2 144 SER 144 274 274 SER SER D . n 
B 2 145 GLY 145 275 275 GLY GLY D . n 
B 2 146 ALA 146 276 276 ALA ALA D . n 
B 2 147 GLU 147 277 277 GLU GLU D . n 
B 2 148 VAL 148 278 278 VAL VAL D . n 
B 2 149 LYS 149 279 279 LYS LYS D . n 
B 2 150 LYS 150 280 280 LYS LYS D . n 
B 2 151 PRO 151 281 281 PRO PRO D . n 
B 2 152 GLY 152 282 282 GLY GLY D . n 
B 2 153 ALA 153 283 283 ALA ALA D . n 
B 2 154 SER 154 284 284 SER SER D . n 
B 2 155 VAL 155 285 285 VAL VAL D . n 
B 2 156 LYS 156 286 286 LYS LYS D . n 
B 2 157 VAL 157 287 287 VAL VAL D . n 
B 2 158 SER 158 288 288 SER SER D . n 
B 2 159 CYS 159 289 289 CYS CYS D . n 
B 2 160 LYS 160 290 290 LYS LYS D . n 
B 2 161 ALA 161 291 291 ALA ALA D . n 
B 2 162 SER 162 292 292 SER SER D . n 
B 2 163 GLY 163 293 293 GLY GLY D . n 
B 2 164 TYR 164 294 294 TYR TYR D . n 
B 2 165 THR 165 295 295 THR THR D . n 
B 2 166 PHE 166 296 296 PHE PHE D . n 
B 2 167 THR 167 297 297 THR THR D . n 
B 2 168 SER 168 298 298 SER SER D . n 
B 2 169 TYR 169 299 299 TYR TYR D . n 
B 2 170 TRP 170 300 300 TRP TRP D . n 
B 2 171 MET 171 301 301 MET MET D . n 
B 2 172 HIS 172 302 302 HIS HIS D . n 
B 2 173 TRP 173 303 303 TRP TRP D . n 
B 2 174 VAL 174 304 304 VAL VAL D . n 
B 2 175 ARG 175 305 305 ARG ARG D . n 
B 2 176 GLN 176 306 306 GLN GLN D . n 
B 2 177 ALA 177 307 307 ALA ALA D . n 
B 2 178 PRO 178 308 308 PRO PRO D . n 
B 2 179 GLY 179 309 309 GLY GLY D . n 
B 2 180 GLN 180 310 310 GLN GLN D . n 
B 2 181 GLY 181 311 311 GLY GLY D . n 
B 2 182 LEU 182 312 312 LEU LEU D . n 
B 2 183 GLU 183 313 313 GLU GLU D . n 
B 2 184 TRP 184 314 314 TRP TRP D . n 
B 2 185 MET 185 315 315 MET MET D . n 
B 2 186 GLY 186 316 316 GLY GLY D . n 
B 2 187 ASN 187 317 317 ASN ASN D . n 
B 2 188 ILE 188 318 318 ILE ILE D . n 
B 2 189 TRP 189 319 319 TRP TRP D . n 
B 2 190 PRO 190 320 320 PRO PRO D . n 
B 2 191 GLY 191 321 321 GLY GLY D . n 
B 2 192 SER 192 322 322 SER SER D . n 
B 2 193 GLY 193 323 323 GLY GLY D . n 
B 2 194 GLY 194 324 324 GLY GLY D . n 
B 2 195 THR 195 325 325 THR THR D . n 
B 2 196 ASN 196 326 326 ASN ASN D . n 
B 2 197 TYR 197 327 327 TYR TYR D . n 
B 2 198 ALA 198 328 328 ALA ALA D . n 
B 2 199 GLU 199 329 329 GLU GLU D . n 
B 2 200 LYS 200 330 330 LYS LYS D . n 
B 2 201 PHE 201 331 331 PHE PHE D . n 
B 2 202 LYS 202 332 332 LYS LYS D . n 
B 2 203 ASN 203 333 333 ASN ASN D . n 
B 2 204 ARG 204 334 334 ARG ARG D . n 
B 2 205 VAL 205 335 335 VAL VAL D . n 
B 2 206 THR 206 336 336 THR THR D . n 
B 2 207 MET 207 337 337 MET MET D . n 
B 2 208 THR 208 338 338 THR THR D . n 
B 2 209 ARG 209 339 339 ARG ARG D . n 
B 2 210 ASP 210 340 340 ASP ASP D . n 
B 2 211 THR 211 341 341 THR THR D . n 
B 2 212 SER 212 342 342 SER SER D . n 
B 2 213 ILE 213 343 343 ILE ILE D . n 
B 2 214 SER 214 344 344 SER SER D . n 
B 2 215 THR 215 345 345 THR THR D . n 
B 2 216 ALA 216 346 346 ALA ALA D . n 
B 2 217 TYR 217 347 347 TYR TYR D . n 
B 2 218 MET 218 348 348 MET MET D . n 
B 2 219 GLU 219 349 349 GLU GLU D . n 
B 2 220 LEU 220 350 350 LEU LEU D . n 
B 2 221 SER 221 351 351 SER SER D . n 
B 2 222 ARG 222 352 352 ARG ARG D . n 
B 2 223 LEU 223 353 353 LEU LEU D . n 
B 2 224 ARG 224 354 354 ARG ARG D . n 
B 2 225 SER 225 355 355 SER SER D . n 
B 2 226 ASP 226 356 356 ASP ASP D . n 
B 2 227 ASP 227 357 357 ASP ASP D . n 
B 2 228 THR 228 358 358 THR THR D . n 
B 2 229 ALA 229 359 359 ALA ALA D . n 
B 2 230 VAL 230 360 360 VAL VAL D . n 
B 2 231 TYR 231 361 361 TYR TYR D . n 
B 2 232 TYR 232 362 362 TYR TYR D . n 
B 2 233 CYS 233 363 363 CYS CYS D . n 
B 2 234 ALA 234 364 364 ALA ALA D . n 
B 2 235 ARG 235 365 365 ARG ARG D . n 
B 2 236 SER 236 366 366 SER SER D . n 
B 2 237 GLY 237 367 367 GLY GLY D . n 
B 2 238 GLY 238 368 368 GLY GLY D . n 
B 2 239 PRO 239 369 369 PRO PRO D . n 
B 2 240 TYR 240 370 370 TYR TYR D . n 
B 2 241 PHE 241 371 371 PHE PHE D . n 
B 2 242 PHE 242 372 372 PHE PHE D . n 
B 2 243 ASP 243 373 373 ASP ASP D . n 
B 2 244 TYR 244 374 374 TYR TYR D . n 
B 2 245 TRP 245 375 375 TRP TRP D . n 
B 2 246 GLY 246 376 376 GLY GLY D . n 
B 2 247 GLN 247 377 377 GLN GLN D . n 
B 2 248 GLY 248 378 378 GLY GLY D . n 
B 2 249 THR 249 379 379 THR THR D . n 
B 2 250 LEU 250 380 380 LEU LEU D . n 
B 2 251 VAL 251 381 381 VAL VAL D . n 
B 2 252 THR 252 382 382 THR THR D . n 
B 2 253 VAL 253 383 383 VAL VAL D . n 
B 2 254 SER 254 384 384 SER SER D . n 
B 2 255 SER 255 385 385 SER SER 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                     9IP7 
_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                         9IP7 
_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                   9IP7 
_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                                 9IP7 
_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                            3.21 
_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                     9IP7 
_struct.title                        'Local refinement structure of sEGFR and 528 Fv (from HL-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        9IP7 
_struct_keywords.text            
'bispecific antibody, diabody, EGFR, HL, 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 9IP7       9IP7   ? 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 9IP7 A 1 ? 621 ? P00533 25  ? 645 ? 1   621 
2 2 9IP7 D 1 ? 255 ? 9IP7   131 ? 385 ? 131 385 
# 
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 9IP7 HIS A 622 ? UNP P00533 ? ? 'expression tag' 622 1 
1 9IP7 HIS A 623 ? UNP P00533 ? ? 'expression tag' 623 2 
1 9IP7 HIS A 624 ? UNP P00533 ? ? 'expression tag' 624 3 
1 9IP7 HIS A 625 ? UNP P00533 ? ? 'expression tag' 625 4 
1 9IP7 HIS A 626 ? UNP P00533 ? ? 'expression tag' 626 5 
1 9IP7 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 24  ? PHE A 31  ? PHE A 24  PHE A 31  1 ? 8  
HELX_P HELX_P2  AA2 ILE A 318 ? LYS A 322 ? ILE A 318 LYS A 322 5 ? 5  
HELX_P HELX_P3  AA3 LEU A 348 ? GLY A 354 ? LEU A 348 GLY A 354 1 ? 7  
HELX_P HELX_P4  AA4 ASP A 364 ? VAL A 374 ? ASP A 364 VAL A 374 5 ? 11 
HELX_P HELX_P5  AA5 LEU A 393 ? GLU A 397 ? LEU A 393 GLU A 397 5 ? 5  
HELX_P HELX_P6  AA6 LYS A 407 ? GLY A 410 ? LYS A 407 GLY A 410 5 ? 4  
HELX_P HELX_P7  AA7 GLY A 471 ? THR A 478 ? GLY A 471 THR A 478 1 ? 8  
HELX_P HELX_P8  AA8 THR B 165 ? TYR B 169 ? THR D 295 TYR D 299 5 ? 5  
HELX_P HELX_P9  AA9 ALA B 198 ? LYS B 202 ? ALA D 328 LYS D 332 5 ? 5  
HELX_P HELX_P10 AB1 ARG B 224 ? THR B 228 ? ARG D 354 THR D 358 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 ? ? ? ? ? ? ? 2.018 ? ?               
disulf2  disulf ?    ? A CYS 212 SG  ? ? ? 1_555 A CYS 224 SG ? ? A CYS 212 A CYS 224 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf3  disulf ?    ? A CYS 227 SG  ? ? ? 1_555 A CYS 236 SG ? ? A CYS 227 A CYS 236 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf4  disulf ?    ? A CYS 240 SG  ? ? ? 1_555 A CYS 267 SG ? ? A CYS 240 A CYS 267 1_555 ? ? ? ? ? ? ? 2.026 ? ?               
disulf5  disulf ?    ? A CYS 271 SG  ? ? ? 1_555 A CYS 283 SG ? ? A CYS 271 A CYS 283 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf6  disulf ?    ? A CYS 287 SG  ? ? ? 1_555 A CYS 302 SG ? ? A CYS 287 A CYS 302 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf7  disulf ?    ? A CYS 305 SG  ? ? ? 1_555 A CYS 309 SG ? ? A CYS 305 A CYS 309 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf8  disulf ?    ? A CYS 313 SG  ? ? ? 1_555 A CYS 338 SG ? ? A CYS 313 A CYS 338 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf9  disulf ?    ? A CYS 446 SG  ? ? ? 1_555 A CYS 475 SG ? ? A CYS 446 A CYS 475 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
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 ? ? ? ? ? ? ? 2.029 ? ?               
disulf13 disulf ?    ? A CYS 515 SG  ? ? ? 1_555 A CYS 531 SG ? ? A CYS 515 A CYS 531 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf14 disulf ?    ? A CYS 534 SG  ? ? ? 1_555 A CYS 547 SG ? ? A CYS 534 A CYS 547 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf15 disulf ?    ? A CYS 538 SG  ? ? ? 1_555 A CYS 555 SG ? ? A CYS 538 A CYS 555 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf16 disulf ?    ? A CYS 558 SG  ? ? ? 1_555 A CYS 567 SG ? ? A CYS 558 A CYS 567 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf17 disulf ?    ? B CYS 23  SG  ? ? ? 1_555 B CYS 93  SG ? ? D CYS 153 D CYS 223 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf18 disulf ?    ? B CYS 159 SG  ? ? ? 1_555 B CYS 233 SG ? ? D CYS 289 D CYS 363 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
covale1  covale one  ? A ASN 328 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 328 B NAG 1   1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
covale2  covale one  ? A ASN 337 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 337 A NAG 701 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale3  covale one  ? A ASN 420 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 420 C NAG 1   1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
covale4  covale one  ? A ASN 504 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 504 A NAG 702 1_555 ? ? ? ? ? ? ? 1.444 ? 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 ? ? ? ? ? ? ? 1.393 ? ?               
# 
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 B 23  ? CYS B 93  ? CYS D 153 ? 1_555 CYS D 223 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS B 159 ? CYS B 233 ? CYS D 289 ? 1_555 CYS D 363 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 36  ? VAL A 37  ? VAL A 36  VAL A 37  
AA1 2 GLU A 60  ? VAL A 61  ? GLU A 60  VAL A 61  
AA1 3 ILE A 82  ? ILE A 83  ? ILE A 82  ILE A 83  
AA2 1 VAL A 65  ? LEU A 66  ? VAL A 65  LEU A 66  
AA2 2 LEU A 95  ? ALA A 96  ? LEU A 95  ALA A 96  
AA3 1 TYR A 246 ? ASN A 247 ? TYR A 246 ASN A 247 
AA3 2 GLN A 252 ? MET A 253 ? GLN A 252 MET A 253 
AA4 1 TYR A 261 ? PHE A 263 ? TYR A 261 PHE A 263 
AA4 2 THR A 266 ? VAL A 268 ? THR A 266 VAL A 268 
AA5 1 SER A 291 ? MET A 294 ? SER A 291 MET A 294 
AA5 2 LYS A 301 ? LYS A 304 ? LYS A 301 LYS A 304 
AA6 1 VAL A 312 ? CYS A 313 ? VAL A 312 CYS A 313 
AA6 2 SER A 340 ? ILE A 341 ? SER A 340 ILE A 341 
AA6 3 GLU A 376 ? ILE A 377 ? GLU A 376 ILE A 377 
AA7 1 HIS A 346 ? ILE A 347 ? HIS A 346 ILE A 347 
AA7 2 LEU A 381 ? ILE A 383 ? LEU A 381 ILE A 383 
AA7 3 PHE A 412 ? VAL A 416 ? PHE A 412 VAL A 416 
AA7 4 ASP A 436 ? VAL A 437 ? ASP A 436 VAL A 437 
AA8 1 GLU A 524 ? VAL A 526 ? GLU A 524 VAL A 526 
AA8 2 CYS A 531 ? GLN A 533 ? CYS A 531 GLN A 533 
AA9 1 ILE A 562 ? ASP A 563 ? ILE A 562 ASP A 563 
AA9 2 HIS A 566 ? CYS A 567 ? HIS A 566 CYS A 567 
AB1 1 MET B 4   ? GLN B 6   ? MET D 134 GLN D 136 
AB1 2 ALA B 19  ? SER B 25  ? ALA D 149 SER D 155 
AB1 3 ASP B 75  ? ILE B 80  ? ASP D 205 ILE D 210 
AB1 4 PHE B 67  ? SER B 72  ? PHE D 197 SER D 202 
AB2 1 GLN B 50  ? ILE B 53  ? GLN D 180 ILE D 183 
AB2 2 LEU B 38  ? GLN B 43  ? LEU D 168 GLN D 173 
AB2 3 GLY B 89  ? GLN B 95  ? GLY D 219 GLN D 225 
AB2 4 THR B 107 ? VAL B 109 ? THR D 237 VAL D 239 
AB3 1 GLN B 140 ? GLN B 143 ? GLN D 270 GLN D 273 
AB3 2 CYS B 159 ? SER B 162 ? CYS D 289 SER D 292 
AB4 1 GLU B 147 ? LYS B 149 ? GLU D 277 LYS D 279 
AB4 2 LEU B 250 ? VAL B 253 ? LEU D 380 VAL D 383 
AB4 3 ALA B 229 ? VAL B 230 ? ALA D 359 VAL D 360 
AB5 1 VAL B 155 ? VAL B 157 ? VAL D 285 VAL D 287 
AB5 2 THR B 215 ? LEU B 220 ? THR D 345 LEU D 350 
AB5 3 VAL B 205 ? ASP B 210 ? VAL D 335 ASP D 340 
AB6 1 VAL B 174 ? GLN B 176 ? VAL D 304 GLN D 306 
AB6 2 LEU B 182 ? TRP B 184 ? LEU D 312 TRP D 314 
# 
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 VAL A 37  ? N VAL A 37  O GLU A 60  ? O GLU A 60  
AA1 2 3 N VAL A 61  ? N VAL A 61  O ILE A 82  ? O ILE A 82  
AA2 1 2 O VAL A 65  ? O VAL A 65  N ALA A 96  ? N ALA A 96  
AA3 1 2 N ASN A 247 ? N ASN A 247 O GLN A 252 ? O GLN A 252 
AA4 1 2 N TYR A 261 ? N TYR A 261 O VAL A 268 ? O VAL A 268 
AA5 1 2 N TYR A 292 ? N TYR A 292 O LYS A 303 ? O LYS A 303 
AA6 1 2 N CYS A 313 ? N CYS A 313 O SER A 340 ? O SER A 340 
AA6 2 3 N ILE A 341 ? N ILE A 341 O GLU A 376 ? O GLU A 376 
AA7 1 2 N ILE A 347 ? N ILE A 347 O LEU A 382 ? O LEU A 382 
AA7 2 3 N LEU A 381 ? N LEU A 381 O ALA A 415 ? O ALA A 415 
AA7 3 4 N SER A 413 ? N SER A 413 O ASP A 436 ? O ASP A 436 
AA8 1 2 N PHE A 525 ? N PHE A 525 O ILE A 532 ? O ILE A 532 
AA9 1 2 N ASP A 563 ? N ASP A 563 O HIS A 566 ? O HIS A 566 
AB1 1 2 N THR B 5   ? N THR D 135 O ARG B 24  ? O ARG D 154 
AB1 2 3 N ALA B 19  ? N ALA D 149 O ILE B 80  ? O ILE D 210 
AB1 3 4 O THR B 77  ? O THR D 207 N SER B 70  ? N SER D 200 
AB2 1 2 O GLN B 50  ? O GLN D 180 N LEU B 42  ? N LEU D 172 
AB2 2 3 N GLU B 39  ? N GLU D 169 O PHE B 94  ? O PHE D 224 
AB2 3 4 N GLY B 89  ? N GLY D 219 O VAL B 109 ? O VAL D 239 
AB3 1 2 N VAL B 142 ? N VAL D 272 O LYS B 160 ? O LYS D 290 
AB4 1 2 N GLU B 147 ? N GLU D 277 O LEU B 250 ? O LEU D 380 
AB4 2 3 O VAL B 251 ? O VAL D 381 N ALA B 229 ? N ALA D 359 
AB5 1 2 N VAL B 155 ? N VAL D 285 O LEU B 220 ? O LEU D 350 
AB5 2 3 O THR B 215 ? O THR D 345 N ASP B 210 ? N ASP D 340 
AB6 1 2 N ARG B 175 ? N ARG D 305 O GLU B 183 ? O GLU D 313 
# 
_pdbx_entry_details.entry_id                   9IP7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 33  ? ? -110.51 -77.24  
2  1 CYS A 34  ? ? 38.06   61.69   
3  1 ASN A 91  ? ? -163.28 119.33  
4  1 LEU A 95  ? ? -109.70 77.09   
5  1 GLU A 118 ? ? -162.97 103.91  
6  1 ARG A 125 ? ? -105.75 66.57   
7  1 ASN A 129 ? ? -114.66 73.40   
8  1 ASN A 134 ? ? 69.49   -6.08   
9  1 SER A 150 ? ? -95.07  30.08   
10 1 GLU A 233 ? ? -124.74 -54.35  
11 1 ALA A 234 ? ? -138.15 -31.83  
12 1 ASP A 297 ? ? -128.32 -160.00 
13 1 PHE A 321 ? ? -95.51  31.72   
14 1 ASN A 328 ? ? -78.42  -159.52 
15 1 LYS A 333 ? ? 72.22   -49.00  
16 1 HIS A 409 ? ? 56.87   14.63   
17 1 LEU A 429 ? ? -34.66  114.94  
18 1 GLN A 480 ? ? -82.37  48.75   
19 1 PRO A 488 ? ? -59.59  -5.24   
20 1 ASN A 528 ? ? 37.19   51.52   
21 1 ASN A 544 ? ? -125.33 -167.78 
22 1 LYS A 585 ? ? 60.86   -119.01 
23 1 SER D 187 ? ? -146.61 37.43   
24 1 ASP D 188 ? ? -107.45 -158.17 
25 1 GLU D 240 ? ? -126.93 -168.77 
26 1 CYS D 363 ? ? -100.90 74.18   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9IP7 
_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                    9IP7 
_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                  3.21 
_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               781005 
_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 
'HL-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 'HL-type bispecific diabody Ex3' ? ? ? 2      
# 
_em_imaging.entry_id                        9IP7 
_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              9IP7 
_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                9IP7 
_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 THR 19  ? A THR 19  
15  1 Y 1 A PHE 20  ? A PHE 20  
16  1 Y 1 A GLU 21  ? A GLU 21  
17  1 Y 1 A ASP 22  ? A ASP 22  
18  1 Y 1 A VAL 46  ? A VAL 46  
19  1 Y 1 A GLN 47  ? A GLN 47  
20  1 Y 1 A ARG 48  ? A ARG 48  
21  1 Y 1 A ASN 49  ? A ASN 49  
22  1 Y 1 A TYR 50  ? A TYR 50  
23  1 Y 1 A ASP 51  ? A ASP 51  
24  1 Y 1 A ASN 70  ? A ASN 70  
25  1 Y 1 A THR 71  ? A THR 71  
26  1 Y 1 A VAL 72  ? A VAL 72  
27  1 Y 1 A ASN 100 ? A ASN 100 
28  1 Y 1 A TYR 101 ? A TYR 101 
29  1 Y 1 A ASP 102 ? A ASP 102 
30  1 Y 1 A ALA 103 ? A ALA 103 
31  1 Y 1 A ASN 104 ? A ASN 104 
32  1 Y 1 A LYS 105 ? A LYS 105 
33  1 Y 1 A THR 106 ? A THR 106 
34  1 Y 1 A GLY 107 ? A GLY 107 
35  1 Y 1 A PHE 156 ? A PHE 156 
36  1 Y 1 A GLN 157 ? A GLN 157 
37  1 Y 1 A ASN 158 ? A ASN 158 
38  1 Y 1 A HIS 159 ? A HIS 159 
39  1 Y 1 A LEU 160 ? A LEU 160 
40  1 Y 1 A GLY 161 ? A GLY 161 
41  1 Y 1 A SER 162 ? A SER 162 
42  1 Y 1 A CYS 163 ? A CYS 163 
43  1 Y 1 A GLN 164 ? A GLN 164 
44  1 Y 1 A LYS 165 ? A LYS 165 
45  1 Y 1 A CYS 166 ? A CYS 166 
46  1 Y 1 A ASP 167 ? A ASP 167 
47  1 Y 1 A PRO 168 ? A PRO 168 
48  1 Y 1 A SER 169 ? A SER 169 
49  1 Y 1 A CYS 170 ? A CYS 170 
50  1 Y 1 A PRO 171 ? A PRO 171 
51  1 Y 1 A ASN 172 ? A ASN 172 
52  1 Y 1 A ILE 190 ? A ILE 190 
53  1 Y 1 A CYS 191 ? A CYS 191 
54  1 Y 1 A ALA 192 ? A ALA 192 
55  1 Y 1 A GLN 193 ? A GLN 193 
56  1 Y 1 A GLN 194 ? A GLN 194 
57  1 Y 1 A CYS 195 ? A CYS 195 
58  1 Y 1 A SER 196 ? A SER 196 
59  1 Y 1 A GLY 197 ? A GLY 197 
60  1 Y 1 A ARG 198 ? A ARG 198 
61  1 Y 1 A CYS 199 ? A CYS 199 
62  1 Y 1 A ARG 200 ? A ARG 200 
63  1 Y 1 A GLY 201 ? A GLY 201 
64  1 Y 1 A LYS 202 ? A LYS 202 
65  1 Y 1 A SER 203 ? A SER 203 
66  1 Y 1 A PRO 204 ? A PRO 204 
67  1 Y 1 A SER 205 ? A SER 205 
68  1 Y 1 A ASP 206 ? A ASP 206 
69  1 Y 1 A CYS 207 ? A CYS 207 
70  1 Y 1 A CYS 208 ? A CYS 208 
71  1 Y 1 A HIS 209 ? A HIS 209 
72  1 Y 1 A ASN 210 ? A ASN 210 
73  1 Y 1 A CYS 216 ? A CYS 216 
74  1 Y 1 A THR 217 ? A THR 217 
75  1 Y 1 A GLY 218 ? A GLY 218 
76  1 Y 1 A PRO 219 ? A PRO 219 
77  1 Y 1 A ARG 220 ? A ARG 220 
78  1 Y 1 A GLU 221 ? A GLU 221 
79  1 Y 1 A SER 222 ? A SER 222 
80  1 Y 1 A ASP 588 ? A ASP 588 
81  1 Y 1 A ALA 589 ? A ALA 589 
82  1 Y 1 A GLY 590 ? A GLY 590 
83  1 Y 1 A HIS 591 ? A HIS 591 
84  1 Y 1 A VAL 592 ? A VAL 592 
85  1 Y 1 A CYS 593 ? A CYS 593 
86  1 Y 1 A HIS 594 ? A HIS 594 
87  1 Y 1 A LEU 595 ? A LEU 595 
88  1 Y 1 A CYS 596 ? A CYS 596 
89  1 Y 1 A HIS 597 ? A HIS 597 
90  1 Y 1 A PRO 598 ? A PRO 598 
91  1 Y 1 A ASN 599 ? A ASN 599 
92  1 Y 1 A CYS 600 ? A CYS 600 
93  1 Y 1 A THR 601 ? A THR 601 
94  1 Y 1 A TYR 602 ? A TYR 602 
95  1 Y 1 A GLY 603 ? A GLY 603 
96  1 Y 1 A CYS 604 ? A CYS 604 
97  1 Y 1 A THR 605 ? A THR 605 
98  1 Y 1 A GLY 606 ? A GLY 606 
99  1 Y 1 A PRO 607 ? A PRO 607 
100 1 Y 1 A GLY 608 ? A GLY 608 
101 1 Y 1 A LEU 609 ? A LEU 609 
102 1 Y 1 A GLU 610 ? A GLU 610 
103 1 Y 1 A GLY 611 ? A GLY 611 
104 1 Y 1 A CYS 612 ? A CYS 612 
105 1 Y 1 A PRO 613 ? A PRO 613 
106 1 Y 1 A THR 614 ? A THR 614 
107 1 Y 1 A ASN 615 ? A ASN 615 
108 1 Y 1 A GLY 616 ? A GLY 616 
109 1 Y 1 A PRO 617 ? A PRO 617 
110 1 Y 1 A LYS 618 ? A LYS 618 
111 1 Y 1 A ILE 619 ? A ILE 619 
112 1 Y 1 A PRO 620 ? A PRO 620 
113 1 Y 1 A SER 621 ? A SER 621 
114 1 Y 1 A HIS 622 ? A HIS 622 
115 1 Y 1 A HIS 623 ? A HIS 623 
116 1 Y 1 A HIS 624 ? A HIS 624 
117 1 Y 1 A HIS 625 ? A HIS 625 
118 1 Y 1 A HIS 626 ? A HIS 626 
119 1 Y 1 A HIS 627 ? A HIS 627 
120 1 Y 1 D ARG 243 ? B ARG 113 
121 1 Y 1 D ALA 244 ? B ALA 114 
122 1 Y 1 D ALA 245 ? B ALA 115 
123 1 Y 1 D ALA 246 ? B ALA 116 
124 1 Y 1 D ALA 247 ? B ALA 117 
125 1 Y 1 D GLY 248 ? B GLY 118 
126 1 Y 1 D GLY 249 ? B GLY 119 
127 1 Y 1 D GLY 250 ? B GLY 120 
128 1 Y 1 D GLY 251 ? B GLY 121 
129 1 Y 1 D SER 252 ? B SER 122 
130 1 Y 1 D GLY 253 ? B GLY 123 
131 1 Y 1 D GLY 254 ? B GLY 124 
132 1 Y 1 D GLY 255 ? B GLY 125 
133 1 Y 1 D GLY 256 ? B GLY 126 
134 1 Y 1 D SER 257 ? B SER 127 
135 1 Y 1 D GLY 258 ? B GLY 128 
136 1 Y 1 D GLY 259 ? B GLY 129 
137 1 Y 1 D GLY 260 ? B GLY 130 
138 1 Y 1 D GLY 261 ? B GLY 131 
139 1 Y 1 D SER 262 ? B SER 132 
140 1 Y 1 D GLY 263 ? B GLY 133 
141 1 Y 1 D GLY 264 ? B GLY 134 
142 1 Y 1 D GLY 265 ? B GLY 135 
143 1 Y 1 D GLY 266 ? B GLY 136 
144 1 Y 1 D SER 267 ? B SER 137 
# 
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           9IP7 
_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 HL-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                    9IP7 
_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   ? 163.570 127.093 184.635 1.00 97.74  ? 4   LYS A N   1 
ATOM   2    C CA  . LYS A 1 4   ? 162.302 126.582 184.130 1.00 103.41 ? 4   LYS A CA  1 
ATOM   3    C C   . LYS A 1 4   ? 162.034 127.082 182.714 1.00 101.18 ? 4   LYS A C   1 
ATOM   4    O O   . LYS A 1 4   ? 161.777 128.267 182.505 1.00 96.13  ? 4   LYS A O   1 
ATOM   5    C CB  . LYS A 1 4   ? 161.155 126.986 185.059 1.00 105.99 ? 4   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 4   ? 161.270 126.422 186.465 1.00 107.60 ? 4   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 4   ? 160.153 125.433 186.755 1.00 105.21 ? 4   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 4   ? 159.630 125.582 188.173 1.00 107.63 ? 4   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 4   ? 158.366 124.823 188.378 1.00 93.77  ? 4   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 5   ? 162.103 126.169 181.748 1.00 100.92 ? 5   LYS A N   1 
ATOM   11   C CA  . LYS A 1 5   ? 161.869 126.526 180.356 1.00 104.53 ? 5   LYS A CA  1 
ATOM   12   C C   . LYS A 1 5   ? 160.454 127.064 180.177 1.00 98.83  ? 5   LYS A C   1 
ATOM   13   O O   . LYS A 1 5   ? 159.488 126.506 180.704 1.00 100.95 ? 5   LYS A O   1 
ATOM   14   C CB  . LYS A 1 5   ? 162.091 125.306 179.459 1.00 104.10 ? 5   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 5   ? 162.078 125.574 177.958 1.00 107.31 ? 5   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 5   ? 162.694 126.915 177.597 1.00 110.18 ? 5   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 5   ? 162.216 127.380 176.231 1.00 99.29  ? 5   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 5   ? 162.669 128.763 175.921 1.00 100.05 ? 5   LYS A NZ  1 
ATOM   19   N N   . VAL A 1 6   ? 160.339 128.158 179.430 1.00 97.58  ? 6   VAL A N   1 
ATOM   20   C CA  . VAL A 1 6   ? 159.071 128.836 179.197 1.00 94.04  ? 6   VAL A CA  1 
ATOM   21   C C   . VAL A 1 6   ? 158.866 128.968 177.695 1.00 95.39  ? 6   VAL A C   1 
ATOM   22   O O   . VAL A 1 6   ? 159.788 129.361 176.971 1.00 95.72  ? 6   VAL A O   1 
ATOM   23   C CB  . VAL A 1 6   ? 159.030 130.218 179.876 1.00 99.40  ? 6   VAL A CB  1 
ATOM   24   C CG1 . VAL A 1 6   ? 157.723 130.922 179.571 1.00 88.07  ? 6   VAL A CG1 1 
ATOM   25   C CG2 . VAL A 1 6   ? 159.223 130.076 181.377 1.00 91.69  ? 6   VAL A CG2 1 
ATOM   26   N N   . CYS A 1 7   ? 157.662 128.644 177.229 1.00 96.81  ? 7   CYS A N   1 
ATOM   27   C CA  . CYS A 1 7   ? 157.330 128.668 175.812 1.00 99.17  ? 7   CYS A CA  1 
ATOM   28   C C   . CYS A 1 7   ? 155.985 129.358 175.618 1.00 97.56  ? 7   CYS A C   1 
ATOM   29   O O   . CYS A 1 7   ? 155.437 129.975 176.537 1.00 98.54  ? 7   CYS A O   1 
ATOM   30   C CB  . CYS A 1 7   ? 157.300 127.250 175.230 1.00 98.95  ? 7   CYS A CB  1 
ATOM   31   S SG  . CYS A 1 7   ? 156.649 125.997 176.351 1.00 101.01 ? 7   CYS A SG  1 
ATOM   32   N N   . GLN A 1 8   ? 155.452 129.266 174.396 1.00 96.45  ? 8   GLN A N   1 
ATOM   33   C CA  . GLN A 1 8   ? 154.156 129.925 174.086 1.00 97.04  ? 8   GLN A CA  1 
ATOM   34   C C   . GLN A 1 8   ? 153.013 129.103 174.702 1.00 85.33  ? 8   GLN A C   1 
ATOM   35   O O   . GLN A 1 8   ? 153.014 127.875 174.477 1.00 81.38  ? 8   GLN A O   1 
ATOM   36   C CB  . GLN A 1 8   ? 153.995 130.076 172.573 1.00 96.43  ? 8   GLN A CB  1 
ATOM   37   C CG  . GLN A 1 8   ? 152.740 130.832 172.151 1.00 96.64  ? 8   GLN A CG  1 
ATOM   38   C CD  . GLN A 1 8   ? 151.573 129.928 171.818 1.00 92.08  ? 8   GLN A CD  1 
ATOM   39   O OE1 . GLN A 1 8   ? 151.677 128.697 171.854 1.00 85.11  ? 8   GLN A OE1 1 
ATOM   40   N NE2 . GLN A 1 8   ? 150.447 130.536 171.478 1.00 94.95  ? 8   GLN A NE2 1 
ATOM   41   N N   . HIS A 1 23  ? 155.035 122.482 162.653 1.00 150.31 ? 23  HIS A N   1 
ATOM   42   C CA  . HIS A 1 23  ? 153.760 122.670 163.399 1.00 146.47 ? 23  HIS A CA  1 
ATOM   43   C C   . HIS A 1 23  ? 153.812 121.857 164.697 1.00 144.87 ? 23  HIS A C   1 
ATOM   44   O O   . HIS A 1 23  ? 154.362 122.350 165.707 1.00 142.35 ? 23  HIS A O   1 
ATOM   45   C CB  . HIS A 1 23  ? 152.562 122.277 162.529 1.00 146.56 ? 23  HIS A CB  1 
ATOM   46   C CG  . HIS A 1 23  ? 152.406 123.119 161.306 1.00 146.15 ? 23  HIS A CG  1 
ATOM   47   N ND1 . HIS A 1 23  ? 152.797 124.439 161.255 1.00 145.70 ? 23  HIS A ND1 1 
ATOM   48   C CD2 . HIS A 1 23  ? 151.904 122.835 160.098 1.00 145.82 ? 23  HIS A CD2 1 
ATOM   49   C CE1 . HIS A 1 23  ? 152.537 124.926 160.051 1.00 143.82 ? 23  HIS A CE1 1 
ATOM   50   N NE2 . HIS A 1 23  ? 151.994 123.968 159.331 1.00 146.83 ? 23  HIS A NE2 1 
ATOM   51   N N   . PHE A 1 24  ? 153.255 120.642 164.670 1.00 147.93 ? 24  PHE A N   1 
ATOM   52   C CA  . PHE A 1 24  ? 153.289 119.767 165.873 1.00 145.61 ? 24  PHE A CA  1 
ATOM   53   C C   . PHE A 1 24  ? 154.747 119.480 166.228 1.00 142.91 ? 24  PHE A C   1 
ATOM   54   O O   . PHE A 1 24  ? 155.110 119.563 167.414 1.00 139.72 ? 24  PHE A O   1 
ATOM   55   C CB  . PHE A 1 24  ? 152.513 118.461 165.677 1.00 146.52 ? 24  PHE A CB  1 
ATOM   56   C CG  . PHE A 1 24  ? 152.882 117.382 166.687 1.00 148.07 ? 24  PHE A CG  1 
ATOM   57   C CD1 . PHE A 1 24  ? 152.318 117.373 167.957 1.00 147.40 ? 24  PHE A CD1 1 
ATOM   58   C CD2 . PHE A 1 24  ? 153.785 116.376 166.362 1.00 150.35 ? 24  PHE A CD2 1 
ATOM   59   C CE1 . PHE A 1 24  ? 152.653 116.390 168.874 1.00 144.69 ? 24  PHE A CE1 1 
ATOM   60   C CE2 . PHE A 1 24  ? 154.118 115.397 167.284 1.00 149.61 ? 24  PHE A CE2 1 
ATOM   61   C CZ  . PHE A 1 24  ? 153.552 115.405 168.536 1.00 143.87 ? 24  PHE A CZ  1 
ATOM   62   N N   . LEU A 1 25  ? 155.563 119.155 165.221 1.00 146.90 ? 25  LEU A N   1 
ATOM   63   C CA  . LEU A 1 25  ? 156.997 118.858 165.468 1.00 150.71 ? 25  LEU A CA  1 
ATOM   64   C C   . LEU A 1 25  ? 157.651 120.095 166.103 1.00 150.21 ? 25  LEU A C   1 
ATOM   65   O O   . LEU A 1 25  ? 158.470 119.924 167.031 1.00 148.88 ? 25  LEU A O   1 
ATOM   66   C CB  . LEU A 1 25  ? 157.681 118.456 164.162 1.00 155.94 ? 25  LEU A CB  1 
ATOM   67   C CG  . LEU A 1 25  ? 159.087 117.860 164.290 1.00 153.24 ? 25  LEU A CG  1 
ATOM   68   C CD1 . LEU A 1 25  ? 159.325 116.847 163.184 1.00 153.27 ? 25  LEU A CD1 1 
ATOM   69   C CD2 . LEU A 1 25  ? 160.156 118.940 164.249 1.00 146.89 ? 25  LEU A CD2 1 
ATOM   70   N N   . SER A 1 26  ? 157.292 121.289 165.623 1.00 150.22 ? 26  SER A N   1 
ATOM   71   C CA  . SER A 1 26  ? 157.868 122.542 166.175 1.00 145.97 ? 26  SER A CA  1 
ATOM   72   C C   . SER A 1 26  ? 157.547 122.642 167.674 1.00 143.82 ? 26  SER A C   1 
ATOM   73   O O   . SER A 1 26  ? 158.492 122.826 168.470 1.00 140.82 ? 26  SER A O   1 
ATOM   74   C CB  . SER A 1 26  ? 157.360 123.747 165.427 1.00 144.89 ? 26  SER A CB  1 
ATOM   75   O OG  . SER A 1 26  ? 157.586 123.608 164.031 1.00 142.55 ? 26  SER A OG  1 
ATOM   76   N N   . LEU A 1 27  ? 156.267 122.502 168.038 1.00 143.57 ? 27  LEU A N   1 
ATOM   77   C CA  . LEU A 1 27  ? 155.867 122.575 169.469 1.00 137.86 ? 27  LEU A CA  1 
ATOM   78   C C   . LEU A 1 27  ? 156.420 121.340 170.202 1.00 138.32 ? 27  LEU A C   1 
ATOM   79   O O   . LEU A 1 27  ? 156.777 121.467 171.388 1.00 132.80 ? 27  LEU A O   1 
ATOM   80   C CB  . LEU A 1 27  ? 154.353 122.731 169.637 1.00 139.11 ? 27  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 27  ? 153.467 121.606 169.092 1.00 139.09 ? 27  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 27  ? 153.147 120.567 170.153 1.00 132.58 ? 27  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 27  ? 152.188 122.171 168.499 1.00 138.00 ? 27  LEU A CD2 1 
ATOM   84   N N   . GLN A 1 28  ? 156.510 120.201 169.510 1.00 141.35 ? 28  GLN A N   1 
ATOM   85   C CA  . GLN A 1 28  ? 157.068 118.969 170.123 1.00 138.33 ? 28  GLN A CA  1 
ATOM   86   C C   . GLN A 1 28  ? 158.507 119.246 170.582 1.00 142.79 ? 28  GLN A C   1 
ATOM   87   O O   . GLN A 1 28  ? 158.870 118.811 171.697 1.00 142.97 ? 28  GLN A O   1 
ATOM   88   C CB  . GLN A 1 28  ? 157.023 117.823 169.113 1.00 137.29 ? 28  GLN A CB  1 
ATOM   89   C CG  . GLN A 1 28  ? 157.889 116.624 169.481 1.00 143.99 ? 28  GLN A CG  1 
ATOM   90   C CD  . GLN A 1 28  ? 157.991 115.603 168.370 1.00 149.22 ? 28  GLN A CD  1 
ATOM   91   O OE1 . GLN A 1 28  ? 157.429 115.774 167.282 1.00 148.22 ? 28  GLN A OE1 1 
ATOM   92   N NE2 . GLN A 1 28  ? 158.719 114.527 168.633 1.00 152.62 ? 28  GLN A NE2 1 
ATOM   93   N N   . ARG A 1 29  ? 159.286 119.957 169.762 1.00 144.28 ? 29  ARG A N   1 
ATOM   94   C CA  . ARG A 1 29  ? 160.713 120.203 170.100 1.00 139.78 ? 29  ARG A CA  1 
ATOM   95   C C   . ARG A 1 29  ? 160.848 121.499 170.918 1.00 134.78 ? 29  ARG A C   1 
ATOM   96   O O   . ARG A 1 29  ? 161.959 121.755 171.430 1.00 130.03 ? 29  ARG A O   1 
ATOM   97   C CB  . ARG A 1 29  ? 161.562 120.251 168.824 1.00 138.61 ? 29  ARG A CB  1 
ATOM   98   C CG  . ARG A 1 29  ? 161.533 118.949 168.037 1.00 142.25 ? 29  ARG A CG  1 
ATOM   99   C CD  . ARG A 1 29  ? 161.663 117.739 168.950 1.00 141.81 ? 29  ARG A CD  1 
ATOM   100  N NE  . ARG A 1 29  ? 162.860 117.794 169.797 1.00 139.90 ? 29  ARG A NE  1 
ATOM   101  C CZ  . ARG A 1 29  ? 163.164 116.893 170.721 1.00 136.08 ? 29  ARG A CZ  1 
ATOM   102  N NH1 . ARG A 1 29  ? 162.372 115.853 170.914 1.00 135.68 ? 29  ARG A NH1 1 
ATOM   103  N NH2 . ARG A 1 29  ? 164.255 117.037 171.451 1.00 131.62 ? 29  ARG A NH2 1 
ATOM   104  N N   . MET A 1 30  ? 159.770 122.281 171.033 1.00 136.17 ? 30  MET A N   1 
ATOM   105  C CA  . MET A 1 30  ? 159.821 123.504 171.877 1.00 138.89 ? 30  MET A CA  1 
ATOM   106  C C   . MET A 1 30  ? 159.227 123.182 173.259 1.00 129.63 ? 30  MET A C   1 
ATOM   107  O O   . MET A 1 30  ? 159.617 123.851 174.239 1.00 128.32 ? 30  MET A O   1 
ATOM   108  C CB  . MET A 1 30  ? 159.064 124.671 171.230 1.00 141.89 ? 30  MET A CB  1 
ATOM   109  C CG  . MET A 1 30  ? 157.597 124.752 171.603 1.00 140.24 ? 30  MET A CG  1 
ATOM   110  S SD  . MET A 1 30  ? 156.785 126.233 170.969 1.00 136.20 ? 30  MET A SD  1 
ATOM   111  C CE  . MET A 1 30  ? 157.128 126.074 169.211 1.00 113.84 ? 30  MET A CE  1 
ATOM   112  N N   . PHE A 1 31  ? 158.337 122.186 173.329 1.00 122.03 ? 31  PHE A N   1 
ATOM   113  C CA  . PHE A 1 31  ? 157.706 121.802 174.622 1.00 118.96 ? 31  PHE A CA  1 
ATOM   114  C C   . PHE A 1 31  ? 158.478 120.633 175.234 1.00 120.02 ? 31  PHE A C   1 
ATOM   115  O O   . PHE A 1 31  ? 158.078 120.153 176.318 1.00 119.02 ? 31  PHE A O   1 
ATOM   116  C CB  . PHE A 1 31  ? 156.227 121.433 174.461 1.00 121.71 ? 31  PHE A CB  1 
ATOM   117  C CG  . PHE A 1 31  ? 155.253 122.603 174.417 1.00 113.92 ? 31  PHE A CG  1 
ATOM   118  C CD1 . PHE A 1 31  ? 154.907 123.201 173.212 1.00 112.10 ? 31  PHE A CD1 1 
ATOM   119  C CD2 . PHE A 1 31  ? 154.673 123.092 175.582 1.00 97.51  ? 31  PHE A CD2 1 
ATOM   120  C CE1 . PHE A 1 31  ? 154.016 124.263 173.176 1.00 103.58 ? 31  PHE A CE1 1 
ATOM   121  C CE2 . PHE A 1 31  ? 153.783 124.153 175.540 1.00 91.00  ? 31  PHE A CE2 1 
ATOM   122  C CZ  . PHE A 1 31  ? 153.456 124.735 174.338 1.00 92.19  ? 31  PHE A CZ  1 
ATOM   123  N N   . ASN A 1 32  ? 159.542 120.179 174.563 1.00 126.23 ? 32  ASN A N   1 
ATOM   124  C CA  . ASN A 1 32  ? 160.293 118.998 175.073 1.00 126.54 ? 32  ASN A CA  1 
ATOM   125  C C   . ASN A 1 32  ? 160.495 119.153 176.585 1.00 121.42 ? 32  ASN A C   1 
ATOM   126  O O   . ASN A 1 32  ? 160.345 118.145 177.308 1.00 113.54 ? 32  ASN A O   1 
ATOM   127  C CB  . ASN A 1 32  ? 161.599 118.797 174.311 1.00 130.24 ? 32  ASN A CB  1 
ATOM   128  C CG  . ASN A 1 32  ? 162.357 120.088 174.107 1.00 129.72 ? 32  ASN A CG  1 
ATOM   129  O OD1 . ASN A 1 32  ? 161.925 121.148 174.573 1.00 125.24 ? 32  ASN A OD1 1 
ATOM   130  N ND2 . ASN A 1 32  ? 163.486 120.021 173.417 1.00 129.41 ? 32  ASN A ND2 1 
ATOM   131  N N   . ASN A 1 33  ? 160.813 120.367 177.043 1.00 119.84 ? 33  ASN A N   1 
ATOM   132  C CA  . ASN A 1 33  ? 160.975 120.625 178.501 1.00 118.02 ? 33  ASN A CA  1 
ATOM   133  C C   . ASN A 1 33  ? 159.814 121.508 178.967 1.00 118.10 ? 33  ASN A C   1 
ATOM   134  O O   . ASN A 1 33  ? 158.876 120.967 179.593 1.00 117.25 ? 33  ASN A O   1 
ATOM   135  C CB  . ASN A 1 33  ? 162.337 121.236 178.812 1.00 118.80 ? 33  ASN A CB  1 
ATOM   136  C CG  . ASN A 1 33  ? 162.649 121.247 180.290 1.00 122.07 ? 33  ASN A CG  1 
ATOM   137  O OD1 . ASN A 1 33  ? 163.590 120.577 180.729 1.00 129.23 ? 33  ASN A OD1 1 
ATOM   138  N ND2 . ASN A 1 33  ? 161.881 121.990 181.073 1.00 116.47 ? 33  ASN A ND2 1 
ATOM   139  N N   . CYS A 1 34  ? 159.879 122.810 178.672 1.00 113.88 ? 34  CYS A N   1 
ATOM   140  C CA  . CYS A 1 34  ? 158.786 123.748 179.043 1.00 103.29 ? 34  CYS A CA  1 
ATOM   141  C C   . CYS A 1 34  ? 158.214 123.385 180.422 1.00 95.44  ? 34  CYS A C   1 
ATOM   142  O O   . CYS A 1 34  ? 157.005 123.074 180.498 1.00 94.48  ? 34  CYS A O   1 
ATOM   143  C CB  . CYS A 1 34  ? 157.684 123.726 177.993 1.00 100.76 ? 34  CYS A CB  1 
ATOM   144  S SG  . CYS A 1 34  ? 158.130 124.633 176.492 1.00 108.00 ? 34  CYS A SG  1 
ATOM   145  N N   . GLU A 1 35  ? 159.046 123.444 181.464 1.00 95.23  ? 35  GLU A N   1 
ATOM   146  C CA  . GLU A 1 35  ? 158.577 123.134 182.809 1.00 93.64  ? 35  GLU A CA  1 
ATOM   147  C C   . GLU A 1 35  ? 157.368 123.981 183.188 1.00 87.02  ? 35  GLU A C   1 
ATOM   148  O O   . GLU A 1 35  ? 156.435 123.485 183.829 1.00 91.88  ? 35  GLU A O   1 
ATOM   149  C CB  . GLU A 1 35  ? 159.707 123.330 183.818 1.00 93.24  ? 35  GLU A CB  1 
ATOM   150  C CG  . GLU A 1 35  ? 159.717 122.309 184.944 1.00 93.64  ? 35  GLU A CG  1 
ATOM   151  C CD  . GLU A 1 35  ? 160.538 121.079 184.610 1.00 101.63 ? 35  GLU A CD  1 
ATOM   152  O OE1 . GLU A 1 35  ? 161.006 120.968 183.458 1.00 103.74 ? 35  GLU A OE1 1 
ATOM   153  O OE2 . GLU A 1 35  ? 160.717 120.222 185.501 1.00 104.38 ? 35  GLU A OE2 1 
ATOM   154  N N   . VAL A 1 36  ? 157.372 125.256 182.807 1.00 83.33  ? 36  VAL A N   1 
ATOM   155  C CA  . VAL A 1 36  ? 156.265 126.173 183.055 1.00 77.41  ? 36  VAL A CA  1 
ATOM   156  C C   . VAL A 1 36  ? 156.029 126.977 181.786 1.00 80.50  ? 36  VAL A C   1 
ATOM   157  O O   . VAL A 1 36  ? 156.971 127.551 181.230 1.00 92.53  ? 36  VAL A O   1 
ATOM   158  C CB  . VAL A 1 36  ? 156.552 127.111 184.244 1.00 68.69  ? 36  VAL A CB  1 
ATOM   159  C CG1 . VAL A 1 36  ? 155.524 128.230 184.303 1.00 60.04  ? 36  VAL A CG1 1 
ATOM   160  C CG2 . VAL A 1 36  ? 156.573 126.331 185.548 1.00 68.50  ? 36  VAL A CG2 1 
ATOM   161  N N   . VAL A 1 37  ? 154.781 127.025 181.331 1.00 72.22  ? 37  VAL A N   1 
ATOM   162  C CA  . VAL A 1 37  ? 154.427 127.711 180.093 1.00 76.51  ? 37  VAL A CA  1 
ATOM   163  C C   . VAL A 1 37  ? 153.679 128.991 180.439 1.00 80.53  ? 37  VAL A C   1 
ATOM   164  O O   . VAL A 1 37  ? 152.591 128.947 181.025 1.00 80.27  ? 37  VAL A O   1 
ATOM   165  C CB  . VAL A 1 37  ? 153.589 126.812 179.172 1.00 78.56  ? 37  VAL A CB  1 
ATOM   166  C CG1 . VAL A 1 37  ? 153.489 127.423 177.785 1.00 84.72  ? 37  VAL A CG1 1 
ATOM   167  C CG2 . VAL A 1 37  ? 154.198 125.424 179.095 1.00 80.94  ? 37  VAL A CG2 1 
ATOM   168  N N   . LEU A 1 38  ? 154.265 130.136 180.076 1.00 88.31  ? 38  LEU A N   1 
ATOM   169  C CA  . LEU A 1 38  ? 153.592 131.419 180.247 1.00 85.78  ? 38  LEU A CA  1 
ATOM   170  C C   . LEU A 1 38  ? 152.434 131.605 179.280 1.00 84.12  ? 38  LEU A C   1 
ATOM   171  O O   . LEU A 1 38  ? 151.552 132.430 179.541 1.00 83.61  ? 38  LEU A O   1 
ATOM   172  C CB  . LEU A 1 38  ? 154.584 132.567 180.072 1.00 85.14  ? 38  LEU A CB  1 
ATOM   173  C CG  . LEU A 1 38  ? 155.198 133.171 181.332 1.00 91.89  ? 38  LEU A CG  1 
ATOM   174  C CD1 . LEU A 1 38  ? 154.207 134.157 181.919 1.00 79.03  ? 38  LEU A CD1 1 
ATOM   175  C CD2 . LEU A 1 38  ? 155.562 132.102 182.348 1.00 94.95  ? 38  LEU A CD2 1 
ATOM   176  N N   . GLY A 1 39  ? 152.416 130.869 178.175 1.00 84.32  ? 39  GLY A N   1 
ATOM   177  C CA  . GLY A 1 39  ? 151.349 131.007 177.208 1.00 90.72  ? 39  GLY A CA  1 
ATOM   178  C C   . GLY A 1 39  ? 150.266 129.970 177.401 1.00 94.37  ? 39  GLY A C   1 
ATOM   179  O O   . GLY A 1 39  ? 149.475 130.056 178.344 1.00 87.35  ? 39  GLY A O   1 
ATOM   180  N N   . ASN A 1 40  ? 150.199 129.003 176.479 1.00 89.65  ? 40  ASN A N   1 
ATOM   181  C CA  . ASN A 1 40  ? 149.120 127.979 176.534 1.00 71.03  ? 40  ASN A CA  1 
ATOM   182  C C   . ASN A 1 40  ? 149.677 126.609 176.137 1.00 69.58  ? 40  ASN A C   1 
ATOM   183  O O   . ASN A 1 40  ? 150.523 126.561 175.218 1.00 77.89  ? 40  ASN A O   1 
ATOM   184  C CB  . ASN A 1 40  ? 147.961 128.339 175.612 1.00 78.24  ? 40  ASN A CB  1 
ATOM   185  C CG  . ASN A 1 40  ? 147.343 129.675 175.945 1.00 85.30  ? 40  ASN A CG  1 
ATOM   186  O OD1 . ASN A 1 40  ? 146.805 129.857 177.043 1.00 88.59  ? 40  ASN A OD1 1 
ATOM   187  N ND2 . ASN A 1 40  ? 147.397 130.616 175.014 1.00 79.34  ? 40  ASN A ND2 1 
ATOM   188  N N   . LEU A 1 41  ? 149.215 125.539 176.792 1.00 72.88  ? 41  LEU A N   1 
ATOM   189  C CA  . LEU A 1 41  ? 149.642 124.171 176.396 1.00 80.04  ? 41  LEU A CA  1 
ATOM   190  C C   . LEU A 1 41  ? 148.877 123.787 175.122 1.00 69.24  ? 41  LEU A C   1 
ATOM   191  O O   . LEU A 1 41  ? 147.881 123.038 175.226 1.00 67.55  ? 41  LEU A O   1 
ATOM   192  C CB  . LEU A 1 41  ? 149.405 123.184 177.538 1.00 81.29  ? 41  LEU A CB  1 
ATOM   193  C CG  . LEU A 1 41  ? 150.019 121.792 177.362 1.00 75.83  ? 41  LEU A CG  1 
ATOM   194  C CD1 . LEU A 1 41  ? 151.320 121.871 176.585 1.00 83.55  ? 41  LEU A CD1 1 
ATOM   195  C CD2 . LEU A 1 41  ? 150.263 121.172 178.723 1.00 78.34  ? 41  LEU A CD2 1 
ATOM   196  N N   . GLU A 1 42  ? 149.326 124.283 173.967 1.00 69.85  ? 42  GLU A N   1 
ATOM   197  C CA  . GLU A 1 42  ? 148.622 124.035 172.711 1.00 79.24  ? 42  GLU A CA  1 
ATOM   198  C C   . GLU A 1 42  ? 149.138 122.759 172.041 1.00 93.51  ? 42  GLU A C   1 
ATOM   199  O O   . GLU A 1 42  ? 149.556 122.745 170.884 1.00 99.12  ? 42  GLU A O   1 
ATOM   200  C CB  . GLU A 1 42  ? 148.759 125.239 171.788 1.00 79.92  ? 42  GLU A CB  1 
ATOM   201  C CG  . GLU A 1 42  ? 148.027 126.475 172.273 1.00 86.16  ? 42  GLU A CG  1 
ATOM   202  C CD  . GLU A 1 42  ? 148.549 127.745 171.635 1.00 92.02  ? 42  GLU A CD  1 
ATOM   203  O OE1 . GLU A 1 42  ? 148.955 127.695 170.455 1.00 93.63  ? 42  GLU A OE1 1 
ATOM   204  O OE2 . GLU A 1 42  ? 148.555 128.794 172.313 1.00 91.94  ? 42  GLU A OE2 1 
ATOM   205  N N   . ILE A 1 43  ? 149.124 121.658 172.815 1.00 95.62  ? 43  ILE A N   1 
ATOM   206  C CA  . ILE A 1 43  ? 149.525 120.320 172.279 1.00 97.95  ? 43  ILE A CA  1 
ATOM   207  C C   . ILE A 1 43  ? 148.422 119.910 171.299 1.00 91.01  ? 43  ILE A C   1 
ATOM   208  O O   . ILE A 1 43  ? 147.336 119.535 171.760 1.00 85.94  ? 43  ILE A O   1 
ATOM   209  C CB  . ILE A 1 43  ? 149.775 119.265 173.380 1.00 96.48  ? 43  ILE A CB  1 
ATOM   210  C CG1 . ILE A 1 43  ? 149.963 117.877 172.761 1.00 92.91  ? 43  ILE A CG1 1 
ATOM   211  C CG2 . ILE A 1 43  ? 148.684 119.242 174.457 1.00 93.84  ? 43  ILE A CG2 1 
ATOM   212  C CD1 . ILE A 1 43  ? 150.649 116.875 173.670 1.00 95.35  ? 43  ILE A CD1 1 
ATOM   213  N N   . THR A 1 44  ? 148.691 119.974 170.001 1.00 98.30  ? 44  THR A N   1 
ATOM   214  C CA  . THR A 1 44  ? 147.705 119.724 168.961 1.00 106.58 ? 44  THR A CA  1 
ATOM   215  C C   . THR A 1 44  ? 148.214 118.655 168.009 1.00 112.68 ? 44  THR A C   1 
ATOM   216  O O   . THR A 1 44  ? 149.386 118.665 167.619 1.00 118.40 ? 44  THR A O   1 
ATOM   217  C CB  . THR A 1 44  ? 147.388 121.007 168.185 1.00 107.80 ? 44  THR A CB  1 
ATOM   218  O OG1 . THR A 1 44  ? 148.608 121.690 167.871 1.00 109.02 ? 44  THR A OG1 1 
ATOM   219  C CG2 . THR A 1 44  ? 146.502 121.924 169.014 1.00 101.46 ? 44  THR A CG2 1 
ATOM   220  N N   . TYR A 1 45  ? 147.320 117.748 167.602 1.00 109.65 ? 45  TYR A N   1 
ATOM   221  C CA  . TYR A 1 45  ? 147.695 116.707 166.607 1.00 109.14 ? 45  TYR A CA  1 
ATOM   222  C C   . TYR A 1 45  ? 148.896 115.921 167.135 1.00 108.49 ? 45  TYR A C   1 
ATOM   223  O O   . TYR A 1 45  ? 149.962 115.977 166.482 1.00 116.16 ? 45  TYR A O   1 
ATOM   224  C CB  . TYR A 1 45  ? 147.989 117.375 165.259 1.00 113.23 ? 45  TYR A CB  1 
ATOM   225  C CG  . TYR A 1 45  ? 147.167 118.622 164.957 1.00 108.99 ? 45  TYR A CG  1 
ATOM   226  C CD1 . TYR A 1 45  ? 145.809 118.684 165.249 1.00 108.49 ? 45  TYR A CD1 1 
ATOM   227  C CD2 . TYR A 1 45  ? 147.763 119.752 164.411 1.00 107.87 ? 45  TYR A CD2 1 
ATOM   228  C CE1 . TYR A 1 45  ? 145.066 119.823 164.988 1.00 107.17 ? 45  TYR A CE1 1 
ATOM   229  C CE2 . TYR A 1 45  ? 147.031 120.897 164.145 1.00 108.16 ? 45  TYR A CE2 1 
ATOM   230  C CZ  . TYR A 1 45  ? 145.679 120.933 164.434 1.00 108.24 ? 45  TYR A CZ  1 
ATOM   231  O OH  . TYR A 1 45  ? 144.952 122.058 164.173 1.00 104.85 ? 45  TYR A OH  1 
ATOM   232  N N   . LEU A 1 52  ? 155.336 112.826 170.137 1.00 118.78 ? 52  LEU A N   1 
ATOM   233  C CA  . LEU A 1 52  ? 155.023 111.562 170.794 1.00 120.70 ? 52  LEU A CA  1 
ATOM   234  C C   . LEU A 1 52  ? 155.665 111.492 172.173 1.00 124.17 ? 52  LEU A C   1 
ATOM   235  O O   . LEU A 1 52  ? 156.849 111.177 172.299 1.00 126.45 ? 52  LEU A O   1 
ATOM   236  C CB  . LEU A 1 52  ? 155.484 110.383 169.936 1.00 114.14 ? 52  LEU A CB  1 
ATOM   237  C CG  . LEU A 1 52  ? 154.890 110.303 168.529 1.00 114.15 ? 52  LEU A CG  1 
ATOM   238  C CD1 . LEU A 1 52  ? 155.865 109.639 167.570 1.00 105.88 ? 52  LEU A CD1 1 
ATOM   239  C CD2 . LEU A 1 52  ? 153.563 109.561 168.549 1.00 116.35 ? 52  LEU A CD2 1 
ATOM   240  N N   . SER A 1 53  ? 154.869 111.789 173.203 1.00 125.55 ? 53  SER A N   1 
ATOM   241  C CA  . SER A 1 53  ? 155.327 111.785 174.592 1.00 121.57 ? 53  SER A CA  1 
ATOM   242  C C   . SER A 1 53  ? 156.530 112.703 174.790 1.00 118.02 ? 53  SER A C   1 
ATOM   243  O O   . SER A 1 53  ? 157.445 112.390 175.555 1.00 115.28 ? 53  SER A O   1 
ATOM   244  C CB  . SER A 1 53  ? 155.652 110.365 175.067 1.00 120.11 ? 53  SER A CB  1 
ATOM   245  O OG  . SER A 1 53  ? 156.976 110.000 174.716 1.00 124.08 ? 53  SER A OG  1 
ATOM   246  N N   . PHE A 1 54  ? 156.534 113.846 174.101 1.00 116.80 ? 54  PHE A N   1 
ATOM   247  C CA  . PHE A 1 54  ? 157.656 114.771 174.194 1.00 119.24 ? 54  PHE A CA  1 
ATOM   248  C C   . PHE A 1 54  ? 157.625 115.605 175.468 1.00 117.27 ? 54  PHE A C   1 
ATOM   249  O O   . PHE A 1 54  ? 158.643 116.209 175.820 1.00 119.61 ? 54  PHE A O   1 
ATOM   250  C CB  . PHE A 1 54  ? 157.683 115.691 172.971 1.00 123.22 ? 54  PHE A CB  1 
ATOM   251  C CG  . PHE A 1 54  ? 156.427 116.496 172.786 1.00 117.03 ? 54  PHE A CG  1 
ATOM   252  C CD1 . PHE A 1 54  ? 155.366 115.989 172.056 1.00 118.32 ? 54  PHE A CD1 1 
ATOM   253  C CD2 . PHE A 1 54  ? 156.309 117.761 173.337 1.00 119.27 ? 54  PHE A CD2 1 
ATOM   254  C CE1 . PHE A 1 54  ? 154.211 116.726 171.883 1.00 119.39 ? 54  PHE A CE1 1 
ATOM   255  C CE2 . PHE A 1 54  ? 155.156 118.500 173.167 1.00 119.91 ? 54  PHE A CE2 1 
ATOM   256  C CZ  . PHE A 1 54  ? 154.106 117.983 172.438 1.00 112.30 ? 54  PHE A CZ  1 
ATOM   257  N N   . LEU A 1 55  ? 156.492 115.656 176.163 1.00 111.99 ? 55  LEU A N   1 
ATOM   258  C CA  . LEU A 1 55  ? 156.345 116.467 177.364 1.00 107.73 ? 55  LEU A CA  1 
ATOM   259  C C   . LEU A 1 55  ? 156.119 115.567 178.571 1.00 104.72 ? 55  LEU A C   1 
ATOM   260  O O   . LEU A 1 55  ? 155.278 114.661 178.532 1.00 106.56 ? 55  LEU A O   1 
ATOM   261  C CB  . LEU A 1 55  ? 155.199 117.470 177.209 1.00 107.69 ? 55  LEU A CB  1 
ATOM   262  C CG  . LEU A 1 55  ? 153.757 116.962 177.157 1.00 104.74 ? 55  LEU A CG  1 
ATOM   263  C CD1 . LEU A 1 55  ? 153.076 117.188 178.495 1.00 103.18 ? 55  LEU A CD1 1 
ATOM   264  C CD2 . LEU A 1 55  ? 152.985 117.633 176.034 1.00 103.30 ? 55  LEU A CD2 1 
ATOM   265  N N   . LYS A 1 56  ? 156.889 115.805 179.633 1.00 104.26 ? 56  LYS A N   1 
ATOM   266  C CA  . LYS A 1 56  ? 156.734 115.064 180.879 1.00 104.13 ? 56  LYS A CA  1 
ATOM   267  C C   . LYS A 1 56  ? 156.697 115.942 182.117 1.00 99.40  ? 56  LYS A C   1 
ATOM   268  O O   . LYS A 1 56  ? 156.184 115.489 183.144 1.00 97.59  ? 56  LYS A O   1 
ATOM   269  C CB  . LYS A 1 56  ? 157.873 114.046 181.054 1.00 104.82 ? 56  LYS A CB  1 
ATOM   270  C CG  . LYS A 1 56  ? 158.047 113.043 179.929 1.00 104.69 ? 56  LYS A CG  1 
ATOM   271  C CD  . LYS A 1 56  ? 157.196 111.807 180.152 1.00 102.08 ? 56  LYS A CD  1 
ATOM   272  C CE  . LYS A 1 56  ? 157.028 111.037 178.860 1.00 108.60 ? 56  LYS A CE  1 
ATOM   273  N NZ  . LYS A 1 56  ? 156.663 111.948 177.748 1.00 111.50 ? 56  LYS A NZ  1 
ATOM   274  N N   . THR A 1 57  ? 157.212 117.171 182.068 1.00 98.18  ? 57  THR A N   1 
ATOM   275  C CA  . THR A 1 57  ? 157.452 117.958 183.271 1.00 98.64  ? 57  THR A CA  1 
ATOM   276  C C   . THR A 1 57  ? 156.856 119.356 183.163 1.00 98.93  ? 57  THR A C   1 
ATOM   277  O O   . THR A 1 57  ? 157.409 120.312 183.712 1.00 102.39 ? 57  THR A O   1 
ATOM   278  C CB  . THR A 1 57  ? 158.948 118.048 183.571 1.00 103.05 ? 57  THR A CB  1 
ATOM   279  O OG1 . THR A 1 57  ? 159.646 118.481 182.396 1.00 102.58 ? 57  THR A OG1 1 
ATOM   280  C CG2 . THR A 1 57  ? 159.490 116.695 184.007 1.00 104.14 ? 57  THR A CG2 1 
ATOM   281  N N   . ILE A 1 58  ? 155.725 119.496 182.475 1.00 94.02  ? 58  ILE A N   1 
ATOM   282  C CA  . ILE A 1 58  ? 155.064 120.792 182.378 1.00 84.89  ? 58  ILE A CA  1 
ATOM   283  C C   . ILE A 1 58  ? 154.299 121.025 183.672 1.00 79.00  ? 58  ILE A C   1 
ATOM   284  O O   . ILE A 1 58  ? 153.129 120.650 183.788 1.00 83.08  ? 58  ILE A O   1 
ATOM   285  C CB  . ILE A 1 58  ? 154.127 120.860 181.160 1.00 80.18  ? 58  ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 58  ? 154.840 120.354 179.904 1.00 86.20  ? 58  ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 58  ? 153.624 122.277 180.963 1.00 78.49  ? 58  ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 58  ? 154.211 120.820 178.607 1.00 79.09  ? 58  ILE A CD1 1 
ATOM   289  N N   . GLN A 1 59  ? 154.952 121.656 184.650 1.00 78.19  ? 59  GLN A N   1 
ATOM   290  C CA  . GLN A 1 59  ? 154.379 121.747 185.989 1.00 78.79  ? 59  GLN A CA  1 
ATOM   291  C C   . GLN A 1 59  ? 153.138 122.632 186.006 1.00 80.25  ? 59  GLN A C   1 
ATOM   292  O O   . GLN A 1 59  ? 152.036 122.169 186.320 1.00 92.92  ? 59  GLN A O   1 
ATOM   293  C CB  . GLN A 1 59  ? 155.429 122.265 186.973 1.00 81.94  ? 59  GLN A CB  1 
ATOM   294  C CG  . GLN A 1 59  ? 154.877 122.607 188.345 1.00 85.71  ? 59  GLN A CG  1 
ATOM   295  C CD  . GLN A 1 59  ? 155.754 122.090 189.467 1.00 95.99  ? 59  GLN A CD  1 
ATOM   296  O OE1 . GLN A 1 59  ? 156.337 121.011 189.366 1.00 89.56  ? 59  GLN A OE1 1 
ATOM   297  N NE2 . GLN A 1 59  ? 155.852 122.860 190.545 1.00 100.42 ? 59  GLN A NE2 1 
ATOM   298  N N   . GLU A 1 60  ? 153.294 123.909 185.667 1.00 68.09  ? 60  GLU A N   1 
ATOM   299  C CA  . GLU A 1 60  ? 152.189 124.856 185.687 1.00 61.51  ? 60  GLU A CA  1 
ATOM   300  C C   . GLU A 1 60  ? 152.121 125.591 184.358 1.00 66.39  ? 60  GLU A C   1 
ATOM   301  O O   . GLU A 1 60  ? 153.149 126.005 183.816 1.00 81.99  ? 60  GLU A O   1 
ATOM   302  C CB  . GLU A 1 60  ? 152.340 125.863 186.834 1.00 60.25  ? 60  GLU A CB  1 
ATOM   303  C CG  . GLU A 1 60  ? 151.270 126.940 186.856 1.00 72.40  ? 60  GLU A CG  1 
ATOM   304  C CD  . GLU A 1 60  ? 151.765 128.252 187.431 1.00 84.60  ? 60  GLU A CD  1 
ATOM   305  O OE1 . GLU A 1 60  ? 152.499 128.222 188.440 1.00 92.88  ? 60  GLU A OE1 1 
ATOM   306  O OE2 . GLU A 1 60  ? 151.414 129.315 186.876 1.00 75.96  ? 60  GLU A OE2 1 
ATOM   307  N N   . VAL A 1 61  ? 150.908 125.751 183.836 1.00 59.18  ? 61  VAL A N   1 
ATOM   308  C CA  . VAL A 1 61  ? 150.670 126.476 182.593 1.00 63.84  ? 61  VAL A CA  1 
ATOM   309  C C   . VAL A 1 61  ? 149.876 127.730 182.931 1.00 71.08  ? 61  VAL A C   1 
ATOM   310  O O   . VAL A 1 61  ? 148.780 127.646 183.498 1.00 71.93  ? 61  VAL A O   1 
ATOM   311  C CB  . VAL A 1 61  ? 149.932 125.611 181.559 1.00 64.73  ? 61  VAL A CB  1 
ATOM   312  C CG1 . VAL A 1 61  ? 149.218 126.486 180.544 1.00 74.80  ? 61  VAL A CG1 1 
ATOM   313  C CG2 . VAL A 1 61  ? 150.904 124.680 180.859 1.00 67.37  ? 61  VAL A CG2 1 
ATOM   314  N N   . ALA A 1 62  ? 150.432 128.892 182.590 1.00 77.99  ? 62  ALA A N   1 
ATOM   315  C CA  . ALA A 1 62  ? 149.766 130.173 182.828 1.00 70.31  ? 62  ALA A CA  1 
ATOM   316  C C   . ALA A 1 62  ? 148.932 130.544 181.602 1.00 71.34  ? 62  ALA A C   1 
ATOM   317  O O   . ALA A 1 62  ? 149.251 131.445 180.826 1.00 74.60  ? 62  ALA A O   1 
ATOM   318  C CB  . ALA A 1 62  ? 150.787 131.250 183.167 1.00 76.66  ? 62  ALA A CB  1 
ATOM   319  N N   . GLY A 1 63  ? 147.832 129.805 181.428 1.00 71.60  ? 63  GLY A N   1 
ATOM   320  C CA  . GLY A 1 63  ? 146.942 130.028 180.272 1.00 74.08  ? 63  GLY A CA  1 
ATOM   321  C C   . GLY A 1 63  ? 145.972 128.867 180.167 1.00 81.62  ? 63  GLY A C   1 
ATOM   322  O O   . GLY A 1 63  ? 145.699 128.246 181.213 1.00 86.04  ? 63  GLY A O   1 
ATOM   323  N N   . TYR A 1 64  ? 145.421 128.566 178.989 1.00 79.67  ? 64  TYR A N   1 
ATOM   324  C CA  . TYR A 1 64  ? 144.550 127.367 178.827 1.00 74.23  ? 64  TYR A CA  1 
ATOM   325  C C   . TYR A 1 64  ? 145.357 126.293 178.113 1.00 72.11  ? 64  TYR A C   1 
ATOM   326  O O   . TYR A 1 64  ? 146.491 126.598 177.709 1.00 76.48  ? 64  TYR A O   1 
ATOM   327  C CB  . TYR A 1 64  ? 143.250 127.732 178.107 1.00 87.56  ? 64  TYR A CB  1 
ATOM   328  C CG  . TYR A 1 64  ? 143.294 127.759 176.587 1.00 93.02  ? 64  TYR A CG  1 
ATOM   329  C CD1 . TYR A 1 64  ? 143.767 128.867 175.898 1.00 94.57  ? 64  TYR A CD1 1 
ATOM   330  C CD2 . TYR A 1 64  ? 142.809 126.691 175.845 1.00 88.10  ? 64  TYR A CD2 1 
ATOM   331  C CE1 . TYR A 1 64  ? 143.788 128.899 174.514 1.00 95.14  ? 64  TYR A CE1 1 
ATOM   332  C CE2 . TYR A 1 64  ? 142.820 126.712 174.461 1.00 88.86  ? 64  TYR A CE2 1 
ATOM   333  C CZ  . TYR A 1 64  ? 143.314 127.818 173.794 1.00 96.97  ? 64  TYR A CZ  1 
ATOM   334  O OH  . TYR A 1 64  ? 143.324 127.840 172.431 1.00 97.18  ? 64  TYR A OH  1 
ATOM   335  N N   . VAL A 1 65  ? 144.828 125.070 178.028 1.00 73.40  ? 65  VAL A N   1 
ATOM   336  C CA  . VAL A 1 65  ? 145.547 123.920 177.402 1.00 75.69  ? 65  VAL A CA  1 
ATOM   337  C C   . VAL A 1 65  ? 144.724 123.457 176.192 1.00 75.39  ? 65  VAL A C   1 
ATOM   338  O O   . VAL A 1 65  ? 143.698 122.771 176.399 1.00 80.44  ? 65  VAL A O   1 
ATOM   339  C CB  . VAL A 1 65  ? 145.807 122.783 178.415 1.00 72.23  ? 65  VAL A CB  1 
ATOM   340  C CG1 . VAL A 1 65  ? 144.635 122.548 179.360 1.00 75.64  ? 65  VAL A CG1 1 
ATOM   341  C CG2 . VAL A 1 65  ? 146.227 121.479 177.746 1.00 70.95  ? 65  VAL A CG2 1 
ATOM   342  N N   . LEU A 1 66  ? 145.137 123.846 174.983 1.00 78.12  ? 66  LEU A N   1 
ATOM   343  C CA  . LEU A 1 66  ? 144.448 123.408 173.744 1.00 94.13  ? 66  LEU A CA  1 
ATOM   344  C C   . LEU A 1 66  ? 144.969 122.005 173.409 1.00 100.96 ? 66  LEU A C   1 
ATOM   345  O O   . LEU A 1 66  ? 145.774 121.882 172.458 1.00 101.73 ? 66  LEU A O   1 
ATOM   346  C CB  . LEU A 1 66  ? 144.704 124.407 172.617 1.00 97.77  ? 66  LEU A CB  1 
ATOM   347  C CG  . LEU A 1 66  ? 143.895 124.199 171.333 1.00 109.33 ? 66  LEU A CG  1 
ATOM   348  C CD1 . LEU A 1 66  ? 142.401 124.369 171.558 1.00 105.34 ? 66  LEU A CD1 1 
ATOM   349  C CD2 . LEU A 1 66  ? 144.390 125.157 170.270 1.00 112.84 ? 66  LEU A CD2 1 
ATOM   350  N N   . ILE A 1 67  ? 144.536 120.993 174.167 1.00 99.63  ? 67  ILE A N   1 
ATOM   351  C CA  . ILE A 1 67  ? 145.038 119.597 173.972 1.00 95.10  ? 67  ILE A CA  1 
ATOM   352  C C   . ILE A 1 67  ? 144.130 118.889 172.954 1.00 98.20  ? 67  ILE A C   1 
ATOM   353  O O   . ILE A 1 67  ? 142.936 118.708 173.258 1.00 101.51 ? 67  ILE A O   1 
ATOM   354  C CB  . ILE A 1 67  ? 145.162 118.837 175.310 1.00 92.98  ? 67  ILE A CB  1 
ATOM   355  C CG1 . ILE A 1 67  ? 145.515 117.368 175.078 1.00 88.68  ? 67  ILE A CG1 1 
ATOM   356  C CG2 . ILE A 1 67  ? 143.917 118.988 176.188 1.00 93.89  ? 67  ILE A CG2 1 
ATOM   357  C CD1 . ILE A 1 67  ? 146.402 116.775 176.156 1.00 87.11  ? 67  ILE A CD1 1 
ATOM   358  N N   . ALA A 1 68  ? 144.666 118.522 171.787 1.00 104.17 ? 68  ALA A N   1 
ATOM   359  C CA  . ALA A 1 68  ? 143.900 117.847 170.712 1.00 108.86 ? 68  ALA A CA  1 
ATOM   360  C C   . ALA A 1 68  ? 144.635 116.570 170.306 1.00 107.92 ? 68  ALA A C   1 
ATOM   361  O O   . ALA A 1 68  ? 144.900 116.394 169.100 1.00 109.54 ? 68  ALA A O   1 
ATOM   362  C CB  . ALA A 1 68  ? 143.725 118.792 169.545 1.00 104.92 ? 68  ALA A CB  1 
ATOM   363  N N   . LEU A 1 69  ? 144.930 115.695 171.271 1.00 102.59 ? 69  LEU A N   1 
ATOM   364  C CA  . LEU A 1 69  ? 145.686 114.441 171.004 1.00 100.87 ? 69  LEU A CA  1 
ATOM   365  C C   . LEU A 1 69  ? 146.705 114.698 169.880 1.00 99.55  ? 69  LEU A C   1 
ATOM   366  O O   . LEU A 1 69  ? 147.628 115.508 170.122 1.00 95.86  ? 69  LEU A O   1 
ATOM   367  C CB  . LEU A 1 69  ? 144.736 113.294 170.657 1.00 110.32 ? 69  LEU A CB  1 
ATOM   368  C CG  . LEU A 1 69  ? 143.972 113.390 169.334 1.00 114.40 ? 69  LEU A CG  1 
ATOM   369  C CD1 . LEU A 1 69  ? 143.780 112.000 168.767 1.00 103.78 ? 69  LEU A CD1 1 
ATOM   370  C CD2 . LEU A 1 69  ? 142.625 114.064 169.515 1.00 118.51 ? 69  LEU A CD2 1 
ATOM   371  N N   . GLU A 1 73  ? 146.803 108.373 171.327 1.00 139.37 ? 73  GLU A N   1 
ATOM   372  C CA  . GLU A 1 73  ? 146.128 107.806 172.523 1.00 139.24 ? 73  GLU A CA  1 
ATOM   373  C C   . GLU A 1 73  ? 147.078 107.884 173.726 1.00 133.31 ? 73  GLU A C   1 
ATOM   374  O O   . GLU A 1 73  ? 146.592 108.205 174.833 1.00 132.96 ? 73  GLU A O   1 
ATOM   375  C CB  . GLU A 1 73  ? 145.722 106.352 172.281 1.00 145.54 ? 73  GLU A CB  1 
ATOM   376  C CG  . GLU A 1 73  ? 144.661 105.846 173.254 1.00 146.76 ? 73  GLU A CG  1 
ATOM   377  C CD  . GLU A 1 73  ? 143.250 105.899 172.699 1.00 144.71 ? 73  GLU A CD  1 
ATOM   378  O OE1 . GLU A 1 73  ? 142.809 107.001 172.313 1.00 139.49 ? 73  GLU A OE1 1 
ATOM   379  O OE2 . GLU A 1 73  ? 142.588 104.841 172.661 1.00 145.63 ? 73  GLU A OE2 1 
ATOM   380  N N   . ARG A 1 74  ? 148.371 107.620 173.504 1.00 130.22 ? 74  ARG A N   1 
ATOM   381  C CA  . ARG A 1 74  ? 149.360 107.615 174.616 1.00 128.83 ? 74  ARG A CA  1 
ATOM   382  C C   . ARG A 1 74  ? 150.071 108.974 174.703 1.00 130.87 ? 74  ARG A C   1 
ATOM   383  O O   . ARG A 1 74  ? 151.066 109.170 173.970 1.00 133.55 ? 74  ARG A O   1 
ATOM   384  C CB  . ARG A 1 74  ? 150.384 106.484 174.457 1.00 129.64 ? 74  ARG A CB  1 
ATOM   385  C CG  . ARG A 1 74  ? 151.431 106.488 175.562 1.00 130.25 ? 74  ARG A CG  1 
ATOM   386  C CD  . ARG A 1 74  ? 150.773 106.485 176.931 1.00 134.09 ? 74  ARG A CD  1 
ATOM   387  N NE  . ARG A 1 74  ? 151.536 107.208 177.953 1.00 133.94 ? 74  ARG A NE  1 
ATOM   388  C CZ  . ARG A 1 74  ? 151.134 107.348 179.209 1.00 133.67 ? 74  ARG A CZ  1 
ATOM   389  N NH1 . ARG A 1 74  ? 149.990 106.813 179.596 1.00 131.50 ? 74  ARG A NH1 1 
ATOM   390  N NH2 . ARG A 1 74  ? 151.877 108.017 180.072 1.00 130.43 ? 74  ARG A NH2 1 
ATOM   391  N N   . ILE A 1 75  ? 149.570 109.876 175.548 1.00 129.16 ? 75  ILE A N   1 
ATOM   392  C CA  . ILE A 1 75  ? 150.221 111.200 175.787 1.00 121.26 ? 75  ILE A CA  1 
ATOM   393  C C   . ILE A 1 75  ? 150.242 111.410 177.310 1.00 120.19 ? 75  ILE A C   1 
ATOM   394  O O   . ILE A 1 75  ? 149.177 111.670 177.883 1.00 120.15 ? 75  ILE A O   1 
ATOM   395  C CB  . ILE A 1 75  ? 149.499 112.346 175.053 1.00 111.85 ? 75  ILE A CB  1 
ATOM   396  C CG1 . ILE A 1 75  ? 149.125 111.976 173.615 1.00 112.98 ? 75  ILE A CG1 1 
ATOM   397  C CG2 . ILE A 1 75  ? 150.337 113.623 175.113 1.00 108.56 ? 75  ILE A CG2 1 
ATOM   398  C CD1 . ILE A 1 75  ? 148.396 113.075 172.863 1.00 104.64 ? 75  ILE A CD1 1 
ATOM   399  N N   . PRO A 1 76  ? 151.390 111.310 178.008 1.00 122.77 ? 76  PRO A N   1 
ATOM   400  C CA  . PRO A 1 76  ? 151.380 111.398 179.464 1.00 120.61 ? 76  PRO A CA  1 
ATOM   401  C C   . PRO A 1 76  ? 150.666 112.612 180.042 1.00 113.13 ? 76  PRO A C   1 
ATOM   402  O O   . PRO A 1 76  ? 149.677 112.397 180.770 1.00 119.35 ? 76  PRO A O   1 
ATOM   403  C CB  . PRO A 1 76  ? 152.877 111.394 179.842 1.00 122.46 ? 76  PRO A CB  1 
ATOM   404  C CG  . PRO A 1 76  ? 153.607 111.630 178.544 1.00 124.76 ? 76  PRO A CG  1 
ATOM   405  C CD  . PRO A 1 76  ? 152.707 111.116 177.446 1.00 124.36 ? 76  PRO A CD  1 
ATOM   406  N N   . LEU A 1 77  ? 151.142 113.832 179.753 1.00 101.34 ? 77  LEU A N   1 
ATOM   407  C CA  . LEU A 1 77  ? 150.565 115.063 180.354 1.00 99.20  ? 77  LEU A CA  1 
ATOM   408  C C   . LEU A 1 77  ? 150.524 114.864 181.878 1.00 100.14 ? 77  LEU A C   1 
ATOM   409  O O   . LEU A 1 77  ? 149.686 115.519 182.536 1.00 97.85  ? 77  LEU A O   1 
ATOM   410  C CB  . LEU A 1 77  ? 149.179 115.299 179.751 1.00 101.43 ? 77  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 77  ? 149.021 116.482 178.791 1.00 97.72  ? 77  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 77  ? 149.530 117.782 179.387 1.00 89.13  ? 77  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 77  ? 149.683 116.187 177.456 1.00 98.25  ? 77  LEU A CD2 1 
ATOM   414  N N   . GLU A 1 78  ? 151.418 114.038 182.437 1.00 103.10 ? 78  GLU A N   1 
ATOM   415  C CA  . GLU A 1 78  ? 151.375 113.672 183.876 1.00 104.57 ? 78  GLU A CA  1 
ATOM   416  C C   . GLU A 1 78  ? 151.621 114.853 184.814 1.00 97.31  ? 78  GLU A C   1 
ATOM   417  O O   . GLU A 1 78  ? 150.913 114.904 185.840 1.00 100.02 ? 78  GLU A O   1 
ATOM   418  C CB  . GLU A 1 78  ? 152.417 112.574 184.094 1.00 109.04 ? 78  GLU A CB  1 
ATOM   419  C CG  . GLU A 1 78  ? 152.131 111.315 183.279 1.00 115.13 ? 78  GLU A CG  1 
ATOM   420  C CD  . GLU A 1 78  ? 153.260 110.302 183.230 1.00 125.66 ? 78  GLU A CD  1 
ATOM   421  O OE1 . GLU A 1 78  ? 154.312 110.540 183.860 1.00 127.56 ? 78  GLU A OE1 1 
ATOM   422  O OE2 . GLU A 1 78  ? 153.084 109.271 182.548 1.00 126.03 ? 78  GLU A OE2 1 
ATOM   423  N N   . ASN A 1 79  ? 152.555 115.754 184.506 1.00 96.44  ? 79  ASN A N   1 
ATOM   424  C CA  . ASN A 1 79  ? 152.915 116.810 185.440 1.00 98.48  ? 79  ASN A CA  1 
ATOM   425  C C   . ASN A 1 79  ? 152.110 118.088 185.250 1.00 95.08  ? 79  ASN A C   1 
ATOM   426  O O   . ASN A 1 79  ? 152.344 119.058 185.977 1.00 95.81  ? 79  ASN A O   1 
ATOM   427  C CB  . ASN A 1 79  ? 154.405 117.131 185.286 1.00 100.67 ? 79  ASN A CB  1 
ATOM   428  C CG  . ASN A 1 79  ? 155.209 116.758 186.516 1.00 102.39 ? 79  ASN A CG  1 
ATOM   429  O OD1 . ASN A 1 79  ? 156.424 116.574 186.445 1.00 100.33 ? 79  ASN A OD1 1 
ATOM   430  N ND2 . ASN A 1 79  ? 154.534 116.646 187.654 1.00 103.60 ? 79  ASN A ND2 1 
ATOM   431  N N   . LEU A 1 80  ? 151.171 118.120 184.306 1.00 88.89  ? 80  LEU A N   1 
ATOM   432  C CA  . LEU A 1 80  ? 150.343 119.307 184.119 1.00 84.80  ? 80  LEU A CA  1 
ATOM   433  C C   . LEU A 1 80  ? 149.446 119.479 185.336 1.00 85.73  ? 80  LEU A C   1 
ATOM   434  O O   . LEU A 1 80  ? 148.472 118.742 185.509 1.00 103.05 ? 80  LEU A O   1 
ATOM   435  C CB  . LEU A 1 80  ? 149.518 119.198 182.841 1.00 81.39  ? 80  LEU A CB  1 
ATOM   436  C CG  . LEU A 1 80  ? 148.632 120.417 182.576 1.00 71.46  ? 80  LEU A CG  1 
ATOM   437  C CD1 . LEU A 1 80  ? 149.465 121.684 182.576 1.00 72.83  ? 80  LEU A CD1 1 
ATOM   438  C CD2 . LEU A 1 80  ? 147.882 120.278 181.267 1.00 78.13  ? 80  LEU A CD2 1 
ATOM   439  N N   . GLN A 1 81  ? 149.777 120.451 186.184 1.00 72.16  ? 81  GLN A N   1 
ATOM   440  C CA  . GLN A 1 81  ? 149.074 120.669 187.441 1.00 78.51  ? 81  GLN A CA  1 
ATOM   441  C C   . GLN A 1 81  ? 148.033 121.776 187.354 1.00 81.12  ? 81  GLN A C   1 
ATOM   442  O O   . GLN A 1 81  ? 146.877 121.571 187.734 1.00 100.72 ? 81  GLN A O   1 
ATOM   443  C CB  . GLN A 1 81  ? 150.076 120.998 188.554 1.00 75.04  ? 81  GLN A CB  1 
ATOM   444  C CG  . GLN A 1 81  ? 151.085 119.905 188.839 1.00 79.03  ? 81  GLN A CG  1 
ATOM   445  C CD  . GLN A 1 81  ? 151.622 119.976 190.253 1.00 83.56  ? 81  GLN A CD  1 
ATOM   446  O OE1 . GLN A 1 81  ? 151.806 121.061 190.801 1.00 83.92  ? 81  GLN A OE1 1 
ATOM   447  N NE2 . GLN A 1 81  ? 151.878 118.819 190.850 1.00 89.29  ? 81  GLN A NE2 1 
ATOM   448  N N   . ILE A 1 82  ? 148.489 122.961 186.954 1.00 70.96  ? 82  ILE A N   1 
ATOM   449  C CA  . ILE A 1 82  ? 147.598 124.148 186.980 1.00 73.76  ? 82  ILE A CA  1 
ATOM   450  C C   . ILE A 1 82  ? 147.338 124.667 185.570 1.00 76.18  ? 82  ILE A C   1 
ATOM   451  O O   . ILE A 1 82  ? 148.246 124.577 184.740 1.00 85.13  ? 82  ILE A O   1 
ATOM   452  C CB  . ILE A 1 82  ? 148.222 125.242 187.870 1.00 74.45  ? 82  ILE A CB  1 
ATOM   453  C CG1 . ILE A 1 82  ? 148.110 124.910 189.363 1.00 78.38  ? 82  ILE A CG1 1 
ATOM   454  C CG2 . ILE A 1 82  ? 147.638 126.621 187.555 1.00 84.40  ? 82  ILE A CG2 1 
ATOM   455  C CD1 . ILE A 1 82  ? 146.690 124.760 189.875 1.00 90.76  ? 82  ILE A CD1 1 
ATOM   456  N N   . ILE A 1 83  ? 146.093 125.094 185.286 1.00 71.45  ? 83  ILE A N   1 
ATOM   457  C CA  . ILE A 1 83  ? 145.683 125.704 183.979 1.00 75.62  ? 83  ILE A CA  1 
ATOM   458  C C   . ILE A 1 83  ? 145.046 127.047 184.359 1.00 87.72  ? 83  ILE A C   1 
ATOM   459  O O   . ILE A 1 83  ? 143.860 127.032 184.723 1.00 98.84  ? 83  ILE A O   1 
ATOM   460  C CB  . ILE A 1 83  ? 144.753 124.766 183.183 1.00 80.51  ? 83  ILE A CB  1 
ATOM   461  C CG1 . ILE A 1 83  ? 145.518 123.556 182.644 1.00 72.44  ? 83  ILE A CG1 1 
ATOM   462  C CG2 . ILE A 1 83  ? 144.027 125.499 182.055 1.00 87.55  ? 83  ILE A CG2 1 
ATOM   463  C CD1 . ILE A 1 83  ? 146.610 123.901 181.646 1.00 70.25  ? 83  ILE A CD1 1 
ATOM   464  N N   . ARG A 1 84  ? 145.743 128.168 184.175 1.00 84.18  ? 84  ARG A N   1 
ATOM   465  C CA  . ARG A 1 84  ? 145.345 129.469 184.701 1.00 81.60  ? 84  ARG A CA  1 
ATOM   466  C C   . ARG A 1 84  ? 144.306 130.184 183.848 1.00 83.71  ? 84  ARG A C   1 
ATOM   467  O O   . ARG A 1 84  ? 143.706 131.156 184.321 1.00 92.95  ? 84  ARG A O   1 
ATOM   468  C CB  . ARG A 1 84  ? 146.571 130.371 184.859 1.00 85.30  ? 84  ARG A CB  1 
ATOM   469  C CG  . ARG A 1 84  ? 147.672 129.774 185.718 1.00 83.46  ? 84  ARG A CG  1 
ATOM   470  C CD  . ARG A 1 84  ? 147.697 130.401 187.099 1.00 81.71  ? 84  ARG A CD  1 
ATOM   471  N NE  . ARG A 1 84  ? 148.864 129.977 187.862 1.00 81.73  ? 84  ARG A NE  1 
ATOM   472  C CZ  . ARG A 1 84  ? 149.290 130.571 188.967 1.00 89.06  ? 84  ARG A CZ  1 
ATOM   473  N NH1 . ARG A 1 84  ? 148.660 131.617 189.475 1.00 97.23  ? 84  ARG A NH1 1 
ATOM   474  N NH2 . ARG A 1 84  ? 150.373 130.103 189.580 1.00 88.98  ? 84  ARG A NH2 1 
ATOM   475  N N   . GLY A 1 85  ? 144.082 129.741 182.615 1.00 81.98  ? 85  GLY A N   1 
ATOM   476  C CA  . GLY A 1 85  ? 143.042 130.335 181.791 1.00 90.66  ? 85  GLY A CA  1 
ATOM   477  C C   . GLY A 1 85  ? 143.249 131.796 181.462 1.00 89.65  ? 85  GLY A C   1 
ATOM   478  O O   . GLY A 1 85  ? 142.272 132.549 181.384 1.00 94.83  ? 85  GLY A O   1 
ATOM   479  N N   . ASN A 1 86  ? 144.498 132.225 181.268 1.00 83.73  ? 86  ASN A N   1 
ATOM   480  C CA  . ASN A 1 86  ? 144.741 133.598 180.841 1.00 82.23  ? 86  ASN A CA  1 
ATOM   481  C C   . ASN A 1 86  ? 144.233 133.852 179.428 1.00 86.54  ? 86  ASN A C   1 
ATOM   482  O O   . ASN A 1 86  ? 144.029 135.011 179.053 1.00 88.76  ? 86  ASN A O   1 
ATOM   483  C CB  . ASN A 1 86  ? 146.231 133.928 180.935 1.00 81.46  ? 86  ASN A CB  1 
ATOM   484  C CG  . ASN A 1 86  ? 146.681 134.185 182.362 1.00 80.44  ? 86  ASN A CG  1 
ATOM   485  O OD1 . ASN A 1 86  ? 145.932 133.957 183.312 1.00 79.97  ? 86  ASN A OD1 1 
ATOM   486  N ND2 . ASN A 1 86  ? 147.908 134.666 182.518 1.00 77.37  ? 86  ASN A ND2 1 
ATOM   487  N N   . MET A 1 87  ? 144.054 132.763 178.675 1.00 90.55  ? 87  MET A N   1 
ATOM   488  C CA  . MET A 1 87  ? 143.492 132.849 177.305 1.00 94.56  ? 87  MET A CA  1 
ATOM   489  C C   . MET A 1 87  ? 142.483 131.702 177.176 1.00 99.84  ? 87  MET A C   1 
ATOM   490  O O   . MET A 1 87  ? 142.486 130.823 178.065 1.00 101.23 ? 87  MET A O   1 
ATOM   491  C CB  . MET A 1 87  ? 144.582 132.682 176.242 1.00 93.75  ? 87  MET A CB  1 
ATOM   492  C CG  . MET A 1 87  ? 145.644 133.763 176.258 1.00 93.98  ? 87  MET A CG  1 
ATOM   493  S SD  . MET A 1 87  ? 144.971 135.405 175.932 1.00 96.91  ? 87  MET A SD  1 
ATOM   494  C CE  . MET A 1 87  ? 144.177 135.133 174.342 1.00 97.82  ? 87  MET A CE  1 
ATOM   495  N N   . TYR A 1 88  ? 141.636 131.726 176.149 1.00 106.44 ? 88  TYR A N   1 
ATOM   496  C CA  . TYR A 1 88  ? 140.625 130.658 175.945 1.00 114.20 ? 88  TYR A CA  1 
ATOM   497  C C   . TYR A 1 88  ? 140.446 130.417 174.465 1.00 118.38 ? 88  TYR A C   1 
ATOM   498  O O   . TYR A 1 88  ? 140.706 131.342 173.666 1.00 117.42 ? 88  TYR A O   1 
ATOM   499  C CB  . TYR A 1 88  ? 139.276 131.029 176.565 1.00 116.45 ? 88  TYR A CB  1 
ATOM   500  C CG  . TYR A 1 88  ? 139.341 131.474 178.018 1.00 110.14 ? 88  TYR A CG  1 
ATOM   501  C CD1 . TYR A 1 88  ? 139.349 130.552 179.057 1.00 108.75 ? 88  TYR A CD1 1 
ATOM   502  C CD2 . TYR A 1 88  ? 139.380 132.822 178.345 1.00 105.84 ? 88  TYR A CD2 1 
ATOM   503  C CE1 . TYR A 1 88  ? 139.399 130.959 180.380 1.00 105.41 ? 88  TYR A CE1 1 
ATOM   504  C CE2 . TYR A 1 88  ? 139.431 133.242 179.663 1.00 103.37 ? 88  TYR A CE2 1 
ATOM   505  C CZ  . TYR A 1 88  ? 139.438 132.308 180.681 1.00 103.99 ? 88  TYR A CZ  1 
ATOM   506  O OH  . TYR A 1 88  ? 139.486 132.736 181.975 1.00 102.88 ? 88  TYR A OH  1 
ATOM   507  N N   . TYR A 1 89  ? 140.012 129.214 174.094 1.00 119.78 ? 89  TYR A N   1 
ATOM   508  C CA  . TYR A 1 89  ? 139.724 128.891 172.701 1.00 127.88 ? 89  TYR A CA  1 
ATOM   509  C C   . TYR A 1 89  ? 138.575 129.743 172.174 1.00 131.73 ? 89  TYR A C   1 
ATOM   510  O O   . TYR A 1 89  ? 138.750 130.542 171.247 1.00 129.85 ? 89  TYR A O   1 
ATOM   511  C CB  . TYR A 1 89  ? 139.403 127.400 172.566 1.00 127.63 ? 89  TYR A CB  1 
ATOM   512  C CG  . TYR A 1 89  ? 139.482 126.869 171.151 1.00 130.02 ? 89  TYR A CG  1 
ATOM   513  C CD1 . TYR A 1 89  ? 140.106 127.597 170.146 1.00 129.62 ? 89  TYR A CD1 1 
ATOM   514  C CD2 . TYR A 1 89  ? 138.930 125.638 170.822 1.00 124.51 ? 89  TYR A CD2 1 
ATOM   515  C CE1 . TYR A 1 89  ? 140.178 127.113 168.853 1.00 126.72 ? 89  TYR A CE1 1 
ATOM   516  C CE2 . TYR A 1 89  ? 138.998 125.146 169.532 1.00 124.82 ? 89  TYR A CE2 1 
ATOM   517  C CZ  . TYR A 1 89  ? 139.623 125.888 168.553 1.00 127.72 ? 89  TYR A CZ  1 
ATOM   518  O OH  . TYR A 1 89  ? 139.692 125.402 167.267 1.00 135.83 ? 89  TYR A OH  1 
ATOM   519  N N   . GLU A 1 90  ? 137.385 129.585 172.756 1.00 131.77 ? 90  GLU A N   1 
ATOM   520  C CA  . GLU A 1 90  ? 136.237 130.410 172.396 1.00 133.78 ? 90  GLU A CA  1 
ATOM   521  C C   . GLU A 1 90  ? 135.758 131.259 173.566 1.00 136.09 ? 90  GLU A C   1 
ATOM   522  O O   . GLU A 1 90  ? 135.729 132.489 173.457 1.00 138.85 ? 90  GLU A O   1 
ATOM   523  C CB  . GLU A 1 90  ? 135.100 129.523 171.872 1.00 132.86 ? 90  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 90  ? 135.568 128.356 171.018 1.00 131.71 ? 90  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 90  ? 136.154 128.801 169.693 1.00 136.91 ? 90  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 90  ? 135.730 129.857 169.178 1.00 131.36 ? 90  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 90  ? 137.038 128.094 169.166 1.00 141.92 ? 90  GLU A OE2 1 
ATOM   528  N N   . ASN A 1 91  ? 135.388 130.639 174.685 1.00 132.59 ? 91  ASN A N   1 
ATOM   529  C CA  . ASN A 1 91  ? 134.953 131.372 175.873 1.00 132.17 ? 91  ASN A CA  1 
ATOM   530  C C   . ASN A 1 91  ? 135.010 130.424 177.058 1.00 130.28 ? 91  ASN A C   1 
ATOM   531  O O   . ASN A 1 91  ? 134.273 129.433 177.086 1.00 132.93 ? 91  ASN A O   1 
ATOM   532  C CB  . ASN A 1 91  ? 133.528 131.900 175.696 1.00 137.99 ? 91  ASN A CB  1 
ATOM   533  C CG  . ASN A 1 91  ? 132.965 132.494 176.972 1.00 139.80 ? 91  ASN A CG  1 
ATOM   534  O OD1 . ASN A 1 91  ? 132.220 131.838 177.700 1.00 149.41 ? 91  ASN A OD1 1 
ATOM   535  N ND2 . ASN A 1 91  ? 133.320 133.743 177.250 1.00 133.90 ? 91  ASN A ND2 1 
ATOM   536  N N   . SER A 1 92  ? 135.825 130.755 178.069 1.00 128.64 ? 92  SER A N   1 
ATOM   537  C CA  . SER A 1 92  ? 136.016 129.884 179.262 1.00 125.76 ? 92  SER A CA  1 
ATOM   538  C C   . SER A 1 92  ? 136.283 128.447 178.789 1.00 118.30 ? 92  SER A C   1 
ATOM   539  O O   . SER A 1 92  ? 135.632 127.516 179.307 1.00 110.39 ? 92  SER A O   1 
ATOM   540  C CB  . SER A 1 92  ? 134.865 130.003 180.252 1.00 126.93 ? 92  SER A CB  1 
ATOM   541  O OG  . SER A 1 92  ? 133.666 130.447 179.635 1.00 132.74 ? 92  SER A OG  1 
ATOM   542  N N   . TYR A 1 93  ? 137.189 128.276 177.820 1.00 117.07 ? 93  TYR A N   1 
ATOM   543  C CA  . TYR A 1 93  ? 137.604 126.936 177.321 1.00 115.69 ? 93  TYR A CA  1 
ATOM   544  C C   . TYR A 1 93  ? 138.988 126.663 177.895 1.00 109.46 ? 93  TYR A C   1 
ATOM   545  O O   . TYR A 1 93  ? 139.986 126.907 177.181 1.00 96.97  ? 93  TYR A O   1 
ATOM   546  C CB  . TYR A 1 93  ? 137.571 126.942 175.788 1.00 122.73 ? 93  TYR A CB  1 
ATOM   547  C CG  . TYR A 1 93  ? 136.223 126.650 175.141 1.00 126.33 ? 93  TYR A CG  1 
ATOM   548  C CD1 . TYR A 1 93  ? 135.028 126.813 175.832 1.00 126.29 ? 93  TYR A CD1 1 
ATOM   549  C CD2 . TYR A 1 93  ? 136.147 126.240 173.816 1.00 127.46 ? 93  TYR A CD2 1 
ATOM   550  C CE1 . TYR A 1 93  ? 133.806 126.555 175.236 1.00 132.45 ? 93  TYR A CE1 1 
ATOM   551  C CE2 . TYR A 1 93  ? 134.932 125.978 173.207 1.00 132.71 ? 93  TYR A CE2 1 
ATOM   552  C CZ  . TYR A 1 93  ? 133.758 126.135 173.920 1.00 137.07 ? 93  TYR A CZ  1 
ATOM   553  O OH  . TYR A 1 93  ? 132.551 125.890 173.334 1.00 139.72 ? 93  TYR A OH  1 
ATOM   554  N N   . ALA A 1 94  ? 139.067 126.201 179.147 1.00 111.76 ? 94  ALA A N   1 
ATOM   555  C CA  . ALA A 1 94  ? 140.361 125.973 179.836 1.00 98.91  ? 94  ALA A CA  1 
ATOM   556  C C   . ALA A 1 94  ? 141.000 124.670 179.352 1.00 93.87  ? 94  ALA A C   1 
ATOM   557  O O   . ALA A 1 94  ? 142.134 124.731 178.841 1.00 106.90 ? 94  ALA A O   1 
ATOM   558  C CB  . ALA A 1 94  ? 140.145 125.962 181.329 1.00 91.02  ? 94  ALA A CB  1 
ATOM   559  N N   . LEU A 1 95  ? 140.301 123.537 179.469 1.00 80.81  ? 95  LEU A N   1 
ATOM   560  C CA  . LEU A 1 95  ? 140.820 122.228 178.992 1.00 90.89  ? 95  LEU A CA  1 
ATOM   561  C C   . LEU A 1 95  ? 140.012 121.801 177.758 1.00 101.34 ? 95  LEU A C   1 
ATOM   562  O O   . LEU A 1 95  ? 139.134 120.924 177.904 1.00 115.69 ? 95  LEU A O   1 
ATOM   563  C CB  . LEU A 1 95  ? 140.741 121.221 180.137 1.00 100.80 ? 95  LEU A CB  1 
ATOM   564  C CG  . LEU A 1 95  ? 141.291 119.815 179.874 1.00 102.52 ? 95  LEU A CG  1 
ATOM   565  C CD1 . LEU A 1 95  ? 142.716 119.822 179.353 1.00 97.77  ? 95  LEU A CD1 1 
ATOM   566  C CD2 . LEU A 1 95  ? 141.210 119.011 181.157 1.00 96.03  ? 95  LEU A CD2 1 
ATOM   567  N N   . ALA A 1 96  ? 140.292 122.395 176.593 1.00 95.23  ? 96  ALA A N   1 
ATOM   568  C CA  . ALA A 1 96  ? 139.570 122.091 175.333 1.00 104.58 ? 96  ALA A CA  1 
ATOM   569  C C   . ALA A 1 96  ? 140.101 120.787 174.735 1.00 109.44 ? 96  ALA A C   1 
ATOM   570  O O   . ALA A 1 96  ? 141.334 120.690 174.548 1.00 108.12 ? 96  ALA A O   1 
ATOM   571  C CB  . ALA A 1 96  ? 139.722 123.247 174.369 1.00 97.33  ? 96  ALA A CB  1 
ATOM   572  N N   . VAL A 1 97  ? 139.217 119.821 174.456 1.00 112.57 ? 97  VAL A N   1 
ATOM   573  C CA  . VAL A 1 97  ? 139.610 118.508 173.852 1.00 111.52 ? 97  VAL A CA  1 
ATOM   574  C C   . VAL A 1 97  ? 138.622 118.170 172.725 1.00 119.92 ? 97  VAL A C   1 
ATOM   575  O O   . VAL A 1 97  ? 137.570 118.844 172.655 1.00 123.37 ? 97  VAL A O   1 
ATOM   576  C CB  . VAL A 1 97  ? 139.665 117.368 174.887 1.00 112.30 ? 97  VAL A CB  1 
ATOM   577  C CG1 . VAL A 1 97  ? 140.930 117.424 175.731 1.00 107.26 ? 97  VAL A CG1 1 
ATOM   578  C CG2 . VAL A 1 97  ? 138.435 117.352 175.780 1.00 117.09 ? 97  VAL A CG2 1 
ATOM   579  N N   . LEU A 1 98  ? 138.941 117.185 171.875 1.00 123.48 ? 98  LEU A N   1 
ATOM   580  C CA  . LEU A 1 98  ? 138.067 116.772 170.785 1.00 129.08 ? 98  LEU A CA  1 
ATOM   581  C C   . LEU A 1 98  ? 138.554 115.441 170.233 1.00 128.72 ? 98  LEU A C   1 
ATOM   582  O O   . LEU A 1 98  ? 139.750 115.136 170.285 1.00 128.18 ? 98  LEU A O   1 
ATOM   583  C CB  . LEU A 1 98  ? 138.006 117.831 169.673 1.00 129.67 ? 98  LEU A CB  1 
ATOM   584  C CG  . LEU A 1 98  ? 139.269 118.601 169.265 1.00 124.19 ? 98  LEU A CG  1 
ATOM   585  C CD1 . LEU A 1 98  ? 140.270 117.727 168.520 1.00 124.02 ? 98  LEU A CD1 1 
ATOM   586  C CD2 . LEU A 1 98  ? 138.896 119.818 168.431 1.00 116.46 ? 98  LEU A CD2 1 
ATOM   587  N N   . SER A 1 99  ? 137.613 114.660 169.705 1.00 132.11 ? 99  SER A N   1 
ATOM   588  C CA  . SER A 1 99  ? 137.894 113.367 169.079 1.00 132.72 ? 99  SER A CA  1 
ATOM   589  C C   . SER A 1 99  ? 138.788 112.474 169.937 1.00 131.66 ? 99  SER A C   1 
ATOM   590  O O   . SER A 1 99  ? 139.484 111.599 169.422 1.00 125.96 ? 99  SER A O   1 
ATOM   591  C CB  . SER A 1 99  ? 138.533 113.572 167.702 1.00 124.00 ? 99  SER A CB  1 
ATOM   592  O OG  . SER A 1 99  ? 139.850 114.078 167.816 1.00 119.54 ? 99  SER A OG  1 
ATOM   593  N N   . LEU A 1 108 ? 141.983 109.348 173.684 1.00 140.96 ? 108 LEU A N   1 
ATOM   594  C CA  . LEU A 1 108 ? 143.198 109.538 174.518 1.00 137.78 ? 108 LEU A CA  1 
ATOM   595  C C   . LEU A 1 108 ? 143.046 108.751 175.832 1.00 139.41 ? 108 LEU A C   1 
ATOM   596  O O   . LEU A 1 108 ? 143.101 109.377 176.910 1.00 140.01 ? 108 LEU A O   1 
ATOM   597  C CB  . LEU A 1 108 ? 143.411 111.029 174.785 1.00 131.64 ? 108 LEU A CB  1 
ATOM   598  C CG  . LEU A 1 108 ? 144.098 111.835 173.682 1.00 126.71 ? 108 LEU A CG  1 
ATOM   599  C CD1 . LEU A 1 108 ? 144.019 113.310 174.029 1.00 121.96 ? 108 LEU A CD1 1 
ATOM   600  C CD2 . LEU A 1 108 ? 145.540 111.401 173.501 1.00 123.53 ? 108 LEU A CD2 1 
ATOM   601  N N   . LYS A 1 109 ? 142.846 107.433 175.770 1.00 136.13 ? 109 LYS A N   1 
ATOM   602  C CA  . LYS A 1 109 ? 142.687 106.643 176.987 1.00 135.27 ? 109 LYS A CA  1 
ATOM   603  C C   . LYS A 1 109 ? 143.947 106.706 177.842 1.00 135.42 ? 109 LYS A C   1 
ATOM   604  O O   . LYS A 1 109 ? 143.876 106.874 179.065 1.00 139.68 ? 109 LYS A O   1 
ATOM   605  C CB  . LYS A 1 109 ? 142.344 105.196 176.632 1.00 138.18 ? 109 LYS A CB  1 
ATOM   606  C CG  . LYS A 1 109 ? 142.849 104.168 177.634 1.00 140.54 ? 109 LYS A CG  1 
ATOM   607  C CD  . LYS A 1 109 ? 143.980 103.333 177.057 1.00 139.07 ? 109 LYS A CD  1 
ATOM   608  C CE  . LYS A 1 109 ? 144.596 102.437 178.118 1.00 136.79 ? 109 LYS A CE  1 
ATOM   609  N NZ  . LYS A 1 109 ? 145.730 101.637 177.581 1.00 137.86 ? 109 LYS A NZ  1 
ATOM   610  N N   . GLU A 1 110 ? 145.114 106.575 177.190 1.00 133.00 ? 110 GLU A N   1 
ATOM   611  C CA  . GLU A 1 110 ? 146.434 106.614 177.880 1.00 133.98 ? 110 GLU A CA  1 
ATOM   612  C C   . GLU A 1 110 ? 146.867 108.080 178.013 1.00 133.82 ? 110 GLU A C   1 
ATOM   613  O O   . GLU A 1 110 ? 147.983 108.422 177.565 1.00 133.37 ? 110 GLU A O   1 
ATOM   614  C CB  . GLU A 1 110 ? 147.412 105.742 177.093 1.00 133.30 ? 110 GLU A CB  1 
ATOM   615  C CG  . GLU A 1 110 ? 147.652 104.385 177.743 1.00 137.86 ? 110 GLU A CG  1 
ATOM   616  C CD  . GLU A 1 110 ? 148.666 103.526 177.011 1.00 142.28 ? 110 GLU A CD  1 
ATOM   617  O OE1 . GLU A 1 110 ? 148.437 103.223 175.822 1.00 146.80 ? 110 GLU A OE1 1 
ATOM   618  O OE2 . GLU A 1 110 ? 149.688 103.167 177.631 1.00 141.75 ? 110 GLU A OE2 1 
ATOM   619  N N   . LEU A 1 111 ? 145.994 108.930 178.570 1.00 132.86 ? 111 LEU A N   1 
ATOM   620  C CA  . LEU A 1 111 ? 146.276 110.376 178.763 1.00 126.90 ? 111 LEU A CA  1 
ATOM   621  C C   . LEU A 1 111 ? 146.138 110.678 180.260 1.00 122.59 ? 111 LEU A C   1 
ATOM   622  O O   . LEU A 1 111 ? 145.112 111.276 180.649 1.00 115.07 ? 111 LEU A O   1 
ATOM   623  C CB  . LEU A 1 111 ? 145.305 111.198 177.918 1.00 123.33 ? 111 LEU A CB  1 
ATOM   624  C CG  . LEU A 1 111 ? 145.460 112.721 177.962 1.00 119.85 ? 111 LEU A CG  1 
ATOM   625  C CD1 . LEU A 1 111 ? 146.416 113.216 176.902 1.00 118.35 ? 111 LEU A CD1 1 
ATOM   626  C CD2 . LEU A 1 111 ? 144.101 113.371 177.799 1.00 120.03 ? 111 LEU A CD2 1 
ATOM   627  N N   . PRO A 1 112 ? 147.089 110.240 181.115 1.00 126.73 ? 112 PRO A N   1 
ATOM   628  C CA  . PRO A 1 112 ? 146.983 110.453 182.550 1.00 118.87 ? 112 PRO A CA  1 
ATOM   629  C C   . PRO A 1 112 ? 147.340 111.851 183.005 1.00 108.62 ? 112 PRO A C   1 
ATOM   630  O O   . PRO A 1 112 ? 148.509 112.045 183.388 1.00 111.14 ? 112 PRO A O   1 
ATOM   631  C CB  . PRO A 1 112 ? 147.965 109.391 183.089 1.00 124.39 ? 112 PRO A CB  1 
ATOM   632  C CG  . PRO A 1 112 ? 149.054 109.344 182.045 1.00 124.62 ? 112 PRO A CG  1 
ATOM   633  C CD  . PRO A 1 112 ? 148.293 109.495 180.742 1.00 128.02 ? 112 PRO A CD  1 
ATOM   634  N N   . MET A 1 113 ? 146.423 112.817 182.889 1.00 103.31 ? 113 MET A N   1 
ATOM   635  C CA  . MET A 1 113 ? 146.608 114.142 183.466 1.00 102.62 ? 113 MET A CA  1 
ATOM   636  C C   . MET A 1 113 ? 146.256 114.102 184.948 1.00 100.05 ? 113 MET A C   1 
ATOM   637  O O   . MET A 1 113 ? 145.404 114.864 185.414 1.00 104.55 ? 113 MET A O   1 
ATOM   638  C CB  . MET A 1 113 ? 145.759 115.182 182.731 1.00 103.34 ? 113 MET A CB  1 
ATOM   639  C CG  . MET A 1 113 ? 145.865 115.112 181.216 1.00 106.22 ? 113 MET A CG  1 
ATOM   640  S SD  . MET A 1 113 ? 144.432 115.783 180.351 1.00 112.92 ? 113 MET A SD  1 
ATOM   641  C CE  . MET A 1 113 ? 143.138 114.685 180.917 1.00 108.60 ? 113 MET A CE  1 
ATOM   642  N N   . ARG A 1 114 ? 146.919 113.213 185.692 1.00 100.75 ? 114 ARG A N   1 
ATOM   643  C CA  . ARG A 1 114 ? 146.567 112.989 187.089 1.00 103.89 ? 114 ARG A CA  1 
ATOM   644  C C   . ARG A 1 114 ? 146.824 114.220 187.946 1.00 105.71 ? 114 ARG A C   1 
ATOM   645  O O   . ARG A 1 114 ? 146.158 114.412 188.969 1.00 110.15 ? 114 ARG A O   1 
ATOM   646  C CB  . ARG A 1 114 ? 147.342 111.788 187.629 1.00 108.52 ? 114 ARG A CB  1 
ATOM   647  C CG  . ARG A 1 114 ? 148.847 111.901 187.460 1.00 109.98 ? 114 ARG A CG  1 
ATOM   648  C CD  . ARG A 1 114 ? 149.540 110.589 187.780 1.00 116.36 ? 114 ARG A CD  1 
ATOM   649  N NE  . ARG A 1 114 ? 149.669 109.744 186.598 1.00 119.49 ? 114 ARG A NE  1 
ATOM   650  C CZ  . ARG A 1 114 ? 150.814 109.492 185.978 1.00 121.27 ? 114 ARG A CZ  1 
ATOM   651  N NH1 . ARG A 1 114 ? 151.957 110.007 186.401 1.00 123.90 ? 114 ARG A NH1 1 
ATOM   652  N NH2 . ARG A 1 114 ? 150.812 108.705 184.906 1.00 121.60 ? 114 ARG A NH2 1 
ATOM   653  N N   . ASN A 1 115 ? 147.779 115.062 187.554 1.00 103.26 ? 115 ASN A N   1 
ATOM   654  C CA  . ASN A 1 115 ? 148.041 116.290 188.291 1.00 102.04 ? 115 ASN A CA  1 
ATOM   655  C C   . ASN A 1 115 ? 147.091 117.418 187.915 1.00 99.06  ? 115 ASN A C   1 
ATOM   656  O O   . ASN A 1 115 ? 147.032 118.421 188.633 1.00 95.93  ? 115 ASN A O   1 
ATOM   657  C CB  . ASN A 1 115 ? 149.474 116.758 188.033 1.00 101.15 ? 115 ASN A CB  1 
ATOM   658  C CG  . ASN A 1 115 ? 150.491 116.019 188.882 1.00 99.48  ? 115 ASN A CG  1 
ATOM   659  O OD1 . ASN A 1 115 ? 151.628 115.803 188.463 1.00 97.68  ? 115 ASN A OD1 1 
ATOM   660  N ND2 . ASN A 1 115 ? 150.086 115.629 190.084 1.00 96.07  ? 115 ASN A ND2 1 
ATOM   661  N N   . LEU A 1 116 ? 146.338 117.275 186.823 1.00 96.68  ? 116 LEU A N   1 
ATOM   662  C CA  . LEU A 1 116 ? 145.385 118.296 186.391 1.00 88.11  ? 116 LEU A CA  1 
ATOM   663  C C   . LEU A 1 116 ? 144.201 118.264 187.352 1.00 98.24  ? 116 LEU A C   1 
ATOM   664  O O   . LEU A 1 116 ? 143.119 117.758 187.049 1.00 110.21 ? 116 LEU A O   1 
ATOM   665  C CB  . LEU A 1 116 ? 144.948 118.050 184.952 1.00 82.54  ? 116 LEU A CB  1 
ATOM   666  C CG  . LEU A 1 116 ? 144.528 119.257 184.114 1.00 79.57  ? 116 LEU A CG  1 
ATOM   667  C CD1 . LEU A 1 116 ? 145.300 120.497 184.523 1.00 84.60  ? 116 LEU A CD1 1 
ATOM   668  C CD2 . LEU A 1 116 ? 144.721 118.966 182.636 1.00 78.44  ? 116 LEU A CD2 1 
ATOM   669  N N   . GLN A 1 117 ? 144.398 118.770 188.576 1.00 97.84  ? 117 GLN A N   1 
ATOM   670  C CA  . GLN A 1 117 ? 143.356 118.661 189.634 1.00 113.77 ? 117 GLN A CA  1 
ATOM   671  C C   . GLN A 1 117 ? 142.890 120.047 190.099 1.00 119.01 ? 117 GLN A C   1 
ATOM   672  O O   . GLN A 1 117 ? 142.170 120.101 191.120 1.00 120.40 ? 117 GLN A O   1 
ATOM   673  C CB  . GLN A 1 117 ? 143.933 117.834 190.784 1.00 115.79 ? 117 GLN A CB  1 
ATOM   674  C CG  . GLN A 1 117 ? 145.098 118.499 191.507 1.00 111.23 ? 117 GLN A CG  1 
ATOM   675  C CD  . GLN A 1 117 ? 146.132 117.509 191.997 1.00 112.53 ? 117 GLN A CD  1 
ATOM   676  O OE1 . GLN A 1 117 ? 145.840 116.617 192.800 1.00 118.84 ? 117 GLN A OE1 1 
ATOM   677  N NE2 . GLN A 1 117 ? 147.356 117.657 191.510 1.00 102.52 ? 117 GLN A NE2 1 
ATOM   678  N N   . GLU A 1 118 ? 143.276 121.118 189.401 1.00 115.76 ? 118 GLU A N   1 
ATOM   679  C CA  . GLU A 1 118 ? 142.767 122.474 189.737 1.00 111.80 ? 118 GLU A CA  1 
ATOM   680  C C   . GLU A 1 118 ? 143.011 123.431 188.564 1.00 97.16  ? 118 GLU A C   1 
ATOM   681  O O   . GLU A 1 118 ? 144.146 123.936 188.439 1.00 93.85  ? 118 GLU A O   1 
ATOM   682  C CB  . GLU A 1 118 ? 143.377 123.028 191.027 1.00 109.21 ? 118 GLU A CB  1 
ATOM   683  C CG  . GLU A 1 118 ? 142.342 123.266 192.123 1.00 117.23 ? 118 GLU A CG  1 
ATOM   684  C CD  . GLU A 1 118 ? 141.115 124.054 191.698 1.00 125.90 ? 118 GLU A CD  1 
ATOM   685  O OE1 . GLU A 1 118 ? 141.274 125.213 191.263 1.00 123.79 ? 118 GLU A OE1 1 
ATOM   686  O OE2 . GLU A 1 118 ? 139.998 123.504 191.803 1.00 126.81 ? 118 GLU A OE2 1 
ATOM   687  N N   . ILE A 1 119 ? 141.962 123.748 187.805 1.00 93.99  ? 119 ILE A N   1 
ATOM   688  C CA  . ILE A 1 119 ? 142.019 124.625 186.605 1.00 85.92  ? 119 ILE A CA  1 
ATOM   689  C C   . ILE A 1 119 ? 141.575 125.988 187.129 1.00 95.45  ? 119 ILE A C   1 
ATOM   690  O O   . ILE A 1 119 ? 140.365 126.150 187.408 1.00 107.54 ? 119 ILE A O   1 
ATOM   691  C CB  . ILE A 1 119 ? 141.124 124.094 185.470 1.00 86.40  ? 119 ILE A CB  1 
ATOM   692  C CG1 . ILE A 1 119 ? 141.607 122.735 184.952 1.00 86.43  ? 119 ILE A CG1 1 
ATOM   693  C CG2 . ILE A 1 119 ? 141.007 125.115 184.339 1.00 83.30  ? 119 ILE A CG2 1 
ATOM   694  C CD1 . ILE A 1 119 ? 140.620 122.030 184.038 1.00 88.51  ? 119 ILE A CD1 1 
ATOM   695  N N   . LEU A 1 120 ? 142.509 126.915 187.271 1.00 103.63 ? 120 LEU A N   1 
ATOM   696  C CA  . LEU A 1 120 ? 142.234 128.225 187.899 1.00 104.78 ? 120 LEU A CA  1 
ATOM   697  C C   . LEU A 1 120 ? 141.619 129.220 186.916 1.00 100.79 ? 120 LEU A C   1 
ATOM   698  O O   . LEU A 1 120 ? 142.093 129.271 185.762 1.00 98.40  ? 120 LEU A O   1 
ATOM   699  C CB  . LEU A 1 120 ? 143.591 128.720 188.397 1.00 102.01 ? 120 LEU A CB  1 
ATOM   700  C CG  . LEU A 1 120 ? 144.465 127.702 189.140 1.00 108.98 ? 120 LEU A CG  1 
ATOM   701  C CD1 . LEU A 1 120 ? 145.690 128.360 189.748 1.00 104.94 ? 120 LEU A CD1 1 
ATOM   702  C CD2 . LEU A 1 120 ? 143.701 126.940 190.204 1.00 106.18 ? 120 LEU A CD2 1 
ATOM   703  N N   . HIS A 1 121 ? 140.595 129.958 187.339 1.00 98.21  ? 121 HIS A N   1 
ATOM   704  C CA  . HIS A 1 121 ? 139.996 131.034 186.546 1.00 101.01 ? 121 HIS A CA  1 
ATOM   705  C C   . HIS A 1 121 ? 139.636 130.563 185.140 1.00 104.90 ? 121 HIS A C   1 
ATOM   706  O O   . HIS A 1 121 ? 139.879 131.253 184.149 1.00 104.53 ? 121 HIS A O   1 
ATOM   707  C CB  . HIS A 1 121 ? 140.915 132.255 186.495 1.00 101.99 ? 121 HIS A CB  1 
ATOM   708  C CG  . HIS A 1 121 ? 141.035 132.975 187.802 1.00 104.22 ? 121 HIS A CG  1 
ATOM   709  N ND1 . HIS A 1 121 ? 140.255 132.666 188.895 1.00 107.22 ? 121 HIS A ND1 1 
ATOM   710  C CD2 . HIS A 1 121 ? 141.844 133.988 188.191 1.00 98.15  ? 121 HIS A CD2 1 
ATOM   711  C CE1 . HIS A 1 121 ? 140.575 133.461 189.900 1.00 102.91 ? 121 HIS A CE1 1 
ATOM   712  N NE2 . HIS A 1 121 ? 141.538 134.271 189.500 1.00 96.27  ? 121 HIS A NE2 1 
ATOM   713  N N   . GLY A 1 122 ? 139.090 129.347 185.032 1.00 107.30 ? 122 GLY A N   1 
ATOM   714  C CA  . GLY A 1 122 ? 138.709 128.780 183.723 1.00 108.54 ? 122 GLY A CA  1 
ATOM   715  C C   . GLY A 1 122 ? 137.640 127.722 183.885 1.00 109.02 ? 122 GLY A C   1 
ATOM   716  O O   . GLY A 1 122 ? 137.434 127.290 185.036 1.00 108.49 ? 122 GLY A O   1 
ATOM   717  N N   . ALA A 1 123 ? 136.978 127.320 182.795 1.00 107.55 ? 123 ALA A N   1 
ATOM   718  C CA  . ALA A 1 123 ? 135.931 126.270 182.819 1.00 107.97 ? 123 ALA A CA  1 
ATOM   719  C C   . ALA A 1 123 ? 136.368 125.121 181.910 1.00 105.50 ? 123 ALA A C   1 
ATOM   720  O O   . ALA A 1 123 ? 136.650 125.372 180.720 1.00 110.59 ? 123 ALA A O   1 
ATOM   721  C CB  . ALA A 1 123 ? 134.601 126.848 182.394 1.00 121.76 ? 123 ALA A CB  1 
ATOM   722  N N   . VAL A 1 124 ? 136.434 123.902 182.448 1.00 101.39 ? 124 VAL A N   1 
ATOM   723  C CA  . VAL A 1 124 ? 136.888 122.713 181.664 1.00 105.03 ? 124 VAL A CA  1 
ATOM   724  C C   . VAL A 1 124 ? 135.961 122.531 180.450 1.00 108.70 ? 124 VAL A C   1 
ATOM   725  O O   . VAL A 1 124 ? 134.730 122.452 180.663 1.00 113.92 ? 124 VAL A O   1 
ATOM   726  C CB  . VAL A 1 124 ? 136.941 121.454 182.556 1.00 112.95 ? 124 VAL A CB  1 
ATOM   727  C CG1 . VAL A 1 124 ? 135.582 121.084 183.136 1.00 118.35 ? 124 VAL A CG1 1 
ATOM   728  C CG2 . VAL A 1 124 ? 137.544 120.258 181.832 1.00 114.89 ? 124 VAL A CG2 1 
ATOM   729  N N   . ARG A 1 125 ? 136.523 122.509 179.233 1.00 110.80 ? 125 ARG A N   1 
ATOM   730  C CA  . ARG A 1 125 ? 135.731 122.237 178.000 1.00 116.08 ? 125 ARG A CA  1 
ATOM   731  C C   . ARG A 1 125 ? 136.094 120.809 177.574 1.00 117.82 ? 125 ARG A C   1 
ATOM   732  O O   . ARG A 1 125 ? 136.717 120.635 176.503 1.00 120.65 ? 125 ARG A O   1 
ATOM   733  C CB  . ARG A 1 125 ? 136.033 123.311 176.947 1.00 116.77 ? 125 ARG A CB  1 
ATOM   734  C CG  . ARG A 1 125 ? 135.461 123.112 175.550 1.00 120.50 ? 125 ARG A CG  1 
ATOM   735  C CD  . ARG A 1 125 ? 133.965 122.852 175.506 1.00 130.52 ? 125 ARG A CD  1 
ATOM   736  N NE  . ARG A 1 125 ? 133.527 122.711 174.113 1.00 135.54 ? 125 ARG A NE  1 
ATOM   737  C CZ  . ARG A 1 125 ? 132.284 122.476 173.714 1.00 137.95 ? 125 ARG A CZ  1 
ATOM   738  N NH1 . ARG A 1 125 ? 131.338 122.224 174.600 1.00 134.26 ? 125 ARG A NH1 1 
ATOM   739  N NH2 . ARG A 1 125 ? 131.992 122.492 172.426 1.00 137.67 ? 125 ARG A NH2 1 
ATOM   740  N N   . PHE A 1 126 ? 135.716 119.820 178.382 1.00 117.12 ? 126 PHE A N   1 
ATOM   741  C CA  . PHE A 1 126 ? 136.134 118.440 178.145 1.00 125.34 ? 126 PHE A CA  1 
ATOM   742  C C   . PHE A 1 126 ? 135.039 117.767 177.320 1.00 132.31 ? 126 PHE A C   1 
ATOM   743  O O   . PHE A 1 126 ? 134.173 117.049 177.826 1.00 137.85 ? 126 PHE A O   1 
ATOM   744  C CB  . PHE A 1 126 ? 136.395 117.721 179.463 1.00 128.93 ? 126 PHE A CB  1 
ATOM   745  C CG  . PHE A 1 126 ? 136.695 116.261 179.313 1.00 135.22 ? 126 PHE A CG  1 
ATOM   746  C CD1 . PHE A 1 126 ? 137.902 115.850 178.775 1.00 133.25 ? 126 PHE A CD1 1 
ATOM   747  C CD2 . PHE A 1 126 ? 135.791 115.299 179.725 1.00 138.50 ? 126 PHE A CD2 1 
ATOM   748  C CE1 . PHE A 1 126 ? 138.197 114.512 178.633 1.00 137.56 ? 126 PHE A CE1 1 
ATOM   749  C CE2 . PHE A 1 126 ? 136.081 113.959 179.585 1.00 139.44 ? 126 PHE A CE2 1 
ATOM   750  C CZ  . PHE A 1 126 ? 137.286 113.565 179.040 1.00 140.17 ? 126 PHE A CZ  1 
ATOM   751  N N   . SER A 1 127 ? 135.075 118.029 176.018 1.00 130.04 ? 127 SER A N   1 
ATOM   752  C CA  . SER A 1 127 ? 134.038 117.596 175.094 1.00 136.24 ? 127 SER A CA  1 
ATOM   753  C C   . SER A 1 127 ? 134.613 116.661 174.038 1.00 137.50 ? 127 SER A C   1 
ATOM   754  O O   . SER A 1 127 ? 135.788 116.755 173.676 1.00 135.77 ? 127 SER A O   1 
ATOM   755  C CB  . SER A 1 127 ? 133.383 118.798 174.408 1.00 136.57 ? 127 SER A CB  1 
ATOM   756  O OG  . SER A 1 127 ? 134.356 119.622 173.791 1.00 131.80 ? 127 SER A OG  1 
ATOM   757  N N   . ASN A 1 128 ? 133.760 115.763 173.541 1.00 140.61 ? 128 ASN A N   1 
ATOM   758  C CA  . ASN A 1 128 ? 134.104 114.841 172.460 1.00 143.11 ? 128 ASN A CA  1 
ATOM   759  C C   . ASN A 1 128 ? 135.305 113.970 172.845 1.00 143.86 ? 128 ASN A C   1 
ATOM   760  O O   . ASN A 1 128 ? 136.397 114.062 172.281 1.00 140.62 ? 128 ASN A O   1 
ATOM   761  C CB  . ASN A 1 128 ? 134.367 115.603 171.155 1.00 140.83 ? 128 ASN A CB  1 
ATOM   762  C CG  . ASN A 1 128 ? 134.404 114.690 169.945 1.00 142.43 ? 128 ASN A CG  1 
ATOM   763  O OD1 . ASN A 1 128 ? 134.964 115.040 168.906 1.00 142.08 ? 128 ASN A OD1 1 
ATOM   764  N ND2 . ASN A 1 128 ? 133.804 113.512 170.074 1.00 142.89 ? 128 ASN A ND2 1 
ATOM   765  N N   . ASN A 1 129 ? 135.068 113.124 173.846 1.00 147.86 ? 129 ASN A N   1 
ATOM   766  C CA  . ASN A 1 129 ? 136.073 112.170 174.298 1.00 149.11 ? 129 ASN A CA  1 
ATOM   767  C C   . ASN A 1 129 ? 135.604 110.746 174.026 1.00 150.43 ? 129 ASN A C   1 
ATOM   768  O O   . ASN A 1 129 ? 135.228 110.028 174.961 1.00 151.44 ? 129 ASN A O   1 
ATOM   769  C CB  . ASN A 1 129 ? 136.362 112.356 175.788 1.00 149.18 ? 129 ASN A CB  1 
ATOM   770  C CG  . ASN A 1 129 ? 135.119 112.688 176.585 1.00 147.77 ? 129 ASN A CG  1 
ATOM   771  O OD1 . ASN A 1 129 ? 134.449 113.687 176.325 1.00 144.50 ? 129 ASN A OD1 1 
ATOM   772  N ND2 . ASN A 1 129 ? 134.800 111.847 177.562 1.00 146.51 ? 129 ASN A ND2 1 
ATOM   773  N N   . PRO A 1 130 ? 135.609 110.297 172.766 1.00 150.24 ? 130 PRO A N   1 
ATOM   774  C CA  . PRO A 1 130 ? 135.101 108.952 172.465 1.00 153.12 ? 130 PRO A CA  1 
ATOM   775  C C   . PRO A 1 130 ? 136.050 107.844 172.893 1.00 154.43 ? 130 PRO A C   1 
ATOM   776  O O   . PRO A 1 130 ? 135.615 106.824 173.437 1.00 153.15 ? 130 PRO A O   1 
ATOM   777  C CB  . PRO A 1 130 ? 134.922 108.982 170.942 1.00 151.63 ? 130 PRO A CB  1 
ATOM   778  C CG  . PRO A 1 130 ? 135.935 109.966 170.465 1.00 145.40 ? 130 PRO A CG  1 
ATOM   779  C CD  . PRO A 1 130 ? 136.161 110.964 171.573 1.00 144.93 ? 130 PRO A CD  1 
ATOM   780  N N   . ALA A 1 131 ? 137.348 108.031 172.654 1.00 153.05 ? 131 ALA A N   1 
ATOM   781  C CA  . ALA A 1 131 ? 138.345 107.011 172.944 1.00 149.45 ? 131 ALA A CA  1 
ATOM   782  C C   . ALA A 1 131 ? 138.958 107.137 174.331 1.00 147.90 ? 131 ALA A C   1 
ATOM   783  O O   . ALA A 1 131 ? 139.706 106.244 174.742 1.00 147.80 ? 131 ALA A O   1 
ATOM   784  C CB  . ALA A 1 131 ? 139.461 107.048 171.892 1.00 145.78 ? 131 ALA A CB  1 
ATOM   785  N N   . LEU A 1 132 ? 138.666 108.211 175.060 1.00 147.58 ? 132 LEU A N   1 
ATOM   786  C CA  . LEU A 1 132 ? 139.225 108.380 176.394 1.00 146.37 ? 132 LEU A CA  1 
ATOM   787  C C   . LEU A 1 132 ? 138.551 107.427 177.373 1.00 145.80 ? 132 LEU A C   1 
ATOM   788  O O   . LEU A 1 132 ? 137.322 107.397 177.484 1.00 144.60 ? 132 LEU A O   1 
ATOM   789  C CB  . LEU A 1 132 ? 139.065 109.827 176.856 1.00 143.76 ? 132 LEU A CB  1 
ATOM   790  C CG  . LEU A 1 132 ? 140.117 110.810 176.335 1.00 143.68 ? 132 LEU A CG  1 
ATOM   791  C CD1 . LEU A 1 132 ? 139.703 111.418 175.002 1.00 144.14 ? 132 LEU A CD1 1 
ATOM   792  C CD2 . LEU A 1 132 ? 140.390 111.898 177.365 1.00 142.52 ? 132 LEU A CD2 1 
ATOM   793  N N   . CYS A 1 133 ? 139.362 106.648 178.085 1.00 144.03 ? 133 CYS A N   1 
ATOM   794  C CA  . CYS A 1 133 ? 138.875 105.650 179.024 1.00 143.95 ? 133 CYS A CA  1 
ATOM   795  C C   . CYS A 1 133 ? 139.345 105.983 180.434 1.00 147.94 ? 133 CYS A C   1 
ATOM   796  O O   . CYS A 1 133 ? 140.341 106.686 180.630 1.00 146.65 ? 133 CYS A O   1 
ATOM   797  C CB  . CYS A 1 133 ? 139.344 104.242 178.633 1.00 141.79 ? 133 CYS A CB  1 
ATOM   798  S SG  . CYS A 1 133 ? 138.146 102.932 178.979 1.00 128.44 ? 133 CYS A SG  1 
ATOM   799  N N   . ASN A 1 134 ? 138.581 105.489 181.413 1.00 151.28 ? 134 ASN A N   1 
ATOM   800  C CA  . ASN A 1 134 ? 138.832 105.669 182.842 1.00 151.85 ? 134 ASN A CA  1 
ATOM   801  C C   . ASN A 1 134 ? 138.596 107.122 183.249 1.00 150.86 ? 134 ASN A C   1 
ATOM   802  O O   . ASN A 1 134 ? 138.596 107.452 184.439 1.00 147.96 ? 134 ASN A O   1 
ATOM   803  C CB  . ASN A 1 134 ? 140.251 105.202 183.204 1.00 150.73 ? 134 ASN A CB  1 
ATOM   804  C CG  . ASN A 1 134 ? 140.549 105.297 184.693 1.00 152.17 ? 134 ASN A CG  1 
ATOM   805  O OD1 . ASN A 1 134 ? 140.875 106.365 185.211 1.00 154.62 ? 134 ASN A OD1 1 
ATOM   806  N ND2 . ASN A 1 134 ? 140.438 104.171 185.388 1.00 146.49 ? 134 ASN A ND2 1 
ATOM   807  N N   . VAL A 1 135 ? 138.338 107.990 182.270 1.00 148.87 ? 135 VAL A N   1 
ATOM   808  C CA  . VAL A 1 135 ? 138.028 109.380 182.577 1.00 145.35 ? 135 VAL A CA  1 
ATOM   809  C C   . VAL A 1 135 ? 136.541 109.578 182.841 1.00 145.25 ? 135 VAL A C   1 
ATOM   810  O O   . VAL A 1 135 ? 136.165 110.526 183.541 1.00 143.69 ? 135 VAL A O   1 
ATOM   811  C CB  . VAL A 1 135 ? 138.516 110.302 181.446 1.00 140.78 ? 135 VAL A CB  1 
ATOM   812  C CG1 . VAL A 1 135 ? 137.553 110.276 180.268 1.00 142.53 ? 135 VAL A CG1 1 
ATOM   813  C CG2 . VAL A 1 135 ? 138.709 111.722 181.959 1.00 139.65 ? 135 VAL A CG2 1 
ATOM   814  N N   . GLU A 1 136 ? 135.685 108.700 182.312 1.00 146.15 ? 136 GLU A N   1 
ATOM   815  C CA  . GLU A 1 136 ? 134.255 108.813 182.573 1.00 148.66 ? 136 GLU A CA  1 
ATOM   816  C C   . GLU A 1 136 ? 133.935 108.540 184.037 1.00 149.06 ? 136 GLU A C   1 
ATOM   817  O O   . GLU A 1 136 ? 133.067 109.198 184.622 1.00 146.55 ? 136 GLU A O   1 
ATOM   818  C CB  . GLU A 1 136 ? 133.481 107.859 181.664 1.00 151.06 ? 136 GLU A CB  1 
ATOM   819  C CG  . GLU A 1 136 ? 133.836 107.978 180.189 1.00 149.81 ? 136 GLU A CG  1 
ATOM   820  C CD  . GLU A 1 136 ? 133.470 109.329 179.605 1.00 146.45 ? 136 GLU A CD  1 
ATOM   821  O OE1 . GLU A 1 136 ? 132.262 109.603 179.448 1.00 142.97 ? 136 GLU A OE1 1 
ATOM   822  O OE2 . GLU A 1 136 ? 134.391 110.116 179.299 1.00 144.41 ? 136 GLU A OE2 1 
ATOM   823  N N   . SER A 1 137 ? 134.624 107.569 184.643 1.00 149.87 ? 137 SER A N   1 
ATOM   824  C CA  . SER A 1 137 ? 134.350 107.218 186.033 1.00 148.16 ? 137 SER A CA  1 
ATOM   825  C C   . SER A 1 137 ? 134.667 108.374 186.974 1.00 145.92 ? 137 SER A C   1 
ATOM   826  O O   . SER A 1 137 ? 133.908 108.647 187.911 1.00 143.48 ? 137 SER A O   1 
ATOM   827  C CB  . SER A 1 137 ? 135.147 105.974 186.424 1.00 146.47 ? 137 SER A CB  1 
ATOM   828  O OG  . SER A 1 137 ? 135.161 105.026 185.371 1.00 144.98 ? 137 SER A OG  1 
ATOM   829  N N   . ILE A 1 138 ? 135.779 109.063 186.743 1.00 146.24 ? 138 ILE A N   1 
ATOM   830  C CA  . ILE A 1 138 ? 136.182 110.170 187.602 1.00 146.49 ? 138 ILE A CA  1 
ATOM   831  C C   . ILE A 1 138 ? 135.387 111.414 187.232 1.00 142.61 ? 138 ILE A C   1 
ATOM   832  O O   . ILE A 1 138 ? 135.109 111.669 186.053 1.00 140.75 ? 138 ILE A O   1 
ATOM   833  C CB  . ILE A 1 138 ? 137.700 110.413 187.496 1.00 145.82 ? 138 ILE A CB  1 
ATOM   834  C CG1 . ILE A 1 138 ? 138.131 111.589 188.376 1.00 139.03 ? 138 ILE A CG1 1 
ATOM   835  C CG2 . ILE A 1 138 ? 138.113 110.641 186.052 1.00 146.42 ? 138 ILE A CG2 1 
ATOM   836  C CD1 . ILE A 1 138 ? 137.759 111.431 189.834 1.00 140.27 ? 138 ILE A CD1 1 
ATOM   837  N N   . GLN A 1 139 ? 135.002 112.185 188.245 1.00 139.75 ? 139 GLN A N   1 
ATOM   838  C CA  . GLN A 1 139 ? 134.317 113.446 188.011 1.00 140.42 ? 139 GLN A CA  1 
ATOM   839  C C   . GLN A 1 139 ? 135.252 114.441 187.333 1.00 140.70 ? 139 GLN A C   1 
ATOM   840  O O   . GLN A 1 139 ? 136.479 114.331 187.409 1.00 141.62 ? 139 GLN A O   1 
ATOM   841  C CB  . GLN A 1 139 ? 133.793 114.023 189.326 1.00 138.59 ? 139 GLN A CB  1 
ATOM   842  C CG  . GLN A 1 139 ? 134.799 114.004 190.467 1.00 137.58 ? 139 GLN A CG  1 
ATOM   843  C CD  . GLN A 1 139 ? 135.827 115.113 190.357 1.00 139.95 ? 139 GLN A CD  1 
ATOM   844  O OE1 . GLN A 1 139 ? 135.538 116.194 189.843 1.00 136.06 ? 139 GLN A OE1 1 
ATOM   845  N NE2 . GLN A 1 139 ? 137.038 114.848 190.835 1.00 140.03 ? 139 GLN A NE2 1 
ATOM   846  N N   . TRP A 1 140 ? 134.655 115.422 186.662 1.00 138.30 ? 140 TRP A N   1 
ATOM   847  C CA  . TRP A 1 140 ? 135.394 116.405 185.882 1.00 135.51 ? 140 TRP A CA  1 
ATOM   848  C C   . TRP A 1 140 ? 135.216 117.821 186.413 1.00 134.17 ? 140 TRP A C   1 
ATOM   849  O O   . TRP A 1 140 ? 135.614 118.780 185.743 1.00 130.65 ? 140 TRP A O   1 
ATOM   850  C CB  . TRP A 1 140 ? 134.955 116.324 184.420 1.00 136.40 ? 140 TRP A CB  1 
ATOM   851  C CG  . TRP A 1 140 ? 135.136 114.957 183.839 1.00 143.25 ? 140 TRP A CG  1 
ATOM   852  C CD1 . TRP A 1 140 ? 136.076 114.034 184.193 1.00 143.55 ? 140 TRP A CD1 1 
ATOM   853  C CD2 . TRP A 1 140 ? 134.314 114.331 182.848 1.00 149.58 ? 140 TRP A CD2 1 
ATOM   854  N NE1 . TRP A 1 140 ? 135.912 112.885 183.458 1.00 146.69 ? 140 TRP A NE1 1 
ATOM   855  C CE2 . TRP A 1 140 ? 134.834 113.042 182.627 1.00 149.66 ? 140 TRP A CE2 1 
ATOM   856  C CE3 . TRP A 1 140 ? 133.197 114.741 182.116 1.00 148.03 ? 140 TRP A CE3 1 
ATOM   857  C CZ2 . TRP A 1 140 ? 134.274 112.159 181.705 1.00 148.13 ? 140 TRP A CZ2 1 
ATOM   858  C CZ3 . TRP A 1 140 ? 132.644 113.864 181.200 1.00 149.15 ? 140 TRP A CZ3 1 
ATOM   859  C CH2 . TRP A 1 140 ? 133.183 112.589 181.003 1.00 148.29 ? 140 TRP A CH2 1 
ATOM   860  N N   . ARG A 1 141 ? 134.631 117.975 187.600 1.00 135.31 ? 141 ARG A N   1 
ATOM   861  C CA  . ARG A 1 141 ? 134.305 119.288 188.142 1.00 131.61 ? 141 ARG A CA  1 
ATOM   862  C C   . ARG A 1 141 ? 135.232 119.732 189.264 1.00 127.14 ? 141 ARG A C   1 
ATOM   863  O O   . ARG A 1 141 ? 135.434 120.938 189.438 1.00 126.06 ? 141 ARG A O   1 
ATOM   864  C CB  . ARG A 1 141 ? 132.859 119.302 188.652 1.00 138.26 ? 141 ARG A CB  1 
ATOM   865  C CG  . ARG A 1 141 ? 131.817 119.505 187.562 1.00 139.10 ? 141 ARG A CG  1 
ATOM   866  C CD  . ARG A 1 141 ? 131.400 118.186 186.930 1.00 139.19 ? 141 ARG A CD  1 
ATOM   867  N NE  . ARG A 1 141 ? 130.512 118.386 185.791 1.00 138.27 ? 141 ARG A NE  1 
ATOM   868  C CZ  . ARG A 1 141 ? 130.913 118.442 184.528 1.00 137.78 ? 141 ARG A CZ  1 
ATOM   869  N NH1 . ARG A 1 141 ? 132.189 118.316 184.202 1.00 136.83 ? 141 ARG A NH1 1 
ATOM   870  N NH2 . ARG A 1 141 ? 130.011 118.630 183.568 1.00 136.99 ? 141 ARG A NH2 1 
ATOM   871  N N   . ASP A 1 142 ? 135.800 118.797 190.030 1.00 126.91 ? 142 ASP A N   1 
ATOM   872  C CA  . ASP A 1 142 ? 136.710 119.175 191.105 1.00 128.80 ? 142 ASP A CA  1 
ATOM   873  C C   . ASP A 1 142 ? 138.019 119.746 190.574 1.00 129.38 ? 142 ASP A C   1 
ATOM   874  O O   . ASP A 1 142 ? 138.749 120.399 191.327 1.00 124.64 ? 142 ASP A O   1 
ATOM   875  C CB  . ASP A 1 142 ? 136.985 117.972 192.010 1.00 126.76 ? 142 ASP A CB  1 
ATOM   876  C CG  . ASP A 1 142 ? 137.903 118.308 193.168 1.00 129.30 ? 142 ASP A CG  1 
ATOM   877  O OD1 . ASP A 1 142 ? 137.537 119.179 193.985 1.00 127.85 ? 142 ASP A OD1 1 
ATOM   878  O OD2 . ASP A 1 142 ? 138.992 117.704 193.261 1.00 132.23 ? 142 ASP A OD2 1 
ATOM   879  N N   . ILE A 1 143 ? 138.323 119.533 189.295 1.00 127.19 ? 143 ILE A N   1 
ATOM   880  C CA  . ILE A 1 143 ? 139.516 120.097 188.675 1.00 117.25 ? 143 ILE A CA  1 
ATOM   881  C C   . ILE A 1 143 ? 139.257 121.556 188.322 1.00 116.13 ? 143 ILE A C   1 
ATOM   882  O O   . ILE A 1 143 ? 140.122 122.233 187.755 1.00 114.45 ? 143 ILE A O   1 
ATOM   883  C CB  . ILE A 1 143 ? 139.934 119.288 187.434 1.00 111.51 ? 143 ILE A CB  1 
ATOM   884  C CG1 . ILE A 1 143 ? 139.008 119.596 186.255 1.00 112.86 ? 143 ILE A CG1 1 
ATOM   885  C CG2 . ILE A 1 143 ? 139.924 117.801 187.744 1.00 112.65 ? 143 ILE A CG2 1 
ATOM   886  C CD1 . ILE A 1 143 ? 139.277 118.754 185.025 1.00 108.92 ? 143 ILE A CD1 1 
ATOM   887  N N   . VAL A 1 144 ? 138.063 122.046 188.651 1.00 117.03 ? 144 VAL A N   1 
ATOM   888  C CA  . VAL A 1 144 ? 137.653 123.417 188.378 1.00 112.51 ? 144 VAL A CA  1 
ATOM   889  C C   . VAL A 1 144 ? 137.096 124.020 189.660 1.00 116.73 ? 144 VAL A C   1 
ATOM   890  O O   . VAL A 1 144 ? 136.576 123.309 190.526 1.00 117.82 ? 144 VAL A O   1 
ATOM   891  C CB  . VAL A 1 144 ? 136.609 123.479 187.238 1.00 114.27 ? 144 VAL A CB  1 
ATOM   892  C CG1 . VAL A 1 144 ? 136.327 124.911 186.834 1.00 115.24 ? 144 VAL A CG1 1 
ATOM   893  C CG2 . VAL A 1 144 ? 137.095 122.691 186.040 1.00 109.69 ? 144 VAL A CG2 1 
ATOM   894  N N   . SER A 1 145 ? 137.213 125.341 189.784 1.00 121.25 ? 145 SER A N   1 
ATOM   895  C CA  . SER A 1 145 ? 136.735 126.069 190.953 1.00 125.32 ? 145 SER A CA  1 
ATOM   896  C C   . SER A 1 145 ? 135.819 127.200 190.508 1.00 130.89 ? 145 SER A C   1 
ATOM   897  O O   . SER A 1 145 ? 136.251 128.103 189.784 1.00 133.90 ? 145 SER A O   1 
ATOM   898  C CB  . SER A 1 145 ? 137.905 126.619 191.772 1.00 125.13 ? 145 SER A CB  1 
ATOM   899  O OG  . SER A 1 145 ? 138.335 127.871 191.267 1.00 122.90 ? 145 SER A OG  1 
ATOM   900  N N   . SER A 1 146 ? 134.558 127.143 190.944 1.00 130.54 ? 146 SER A N   1 
ATOM   901  C CA  . SER A 1 146 ? 133.589 128.228 190.763 1.00 129.41 ? 146 SER A CA  1 
ATOM   902  C C   . SER A 1 146 ? 133.369 128.580 189.293 1.00 126.76 ? 146 SER A C   1 
ATOM   903  O O   . SER A 1 146 ? 133.124 129.741 188.955 1.00 121.22 ? 146 SER A O   1 
ATOM   904  C CB  . SER A 1 146 ? 134.004 129.474 191.549 1.00 125.19 ? 146 SER A CB  1 
ATOM   905  O OG  . SER A 1 146 ? 134.536 129.124 192.815 1.00 118.80 ? 146 SER A OG  1 
ATOM   906  N N   . ASP A 1 147 ? 133.452 127.592 188.405 1.00 125.66 ? 147 ASP A N   1 
ATOM   907  C CA  . ASP A 1 147 ? 133.178 127.807 186.987 1.00 126.57 ? 147 ASP A CA  1 
ATOM   908  C C   . ASP A 1 147 ? 132.369 126.649 186.421 1.00 128.81 ? 147 ASP A C   1 
ATOM   909  O O   . ASP A 1 147 ? 132.535 126.259 185.261 1.00 126.96 ? 147 ASP A O   1 
ATOM   910  C CB  . ASP A 1 147 ? 134.471 128.002 186.196 1.00 125.35 ? 147 ASP A CB  1 
ATOM   911  C CG  . ASP A 1 147 ? 134.334 129.048 185.107 1.00 125.56 ? 147 ASP A CG  1 
ATOM   912  O OD1 . ASP A 1 147 ? 133.208 129.233 184.598 1.00 126.29 ? 147 ASP A OD1 1 
ATOM   913  O OD2 . ASP A 1 147 ? 135.350 129.687 184.761 1.00 121.18 ? 147 ASP A OD2 1 
ATOM   914  N N   . PHE A 1 148 ? 131.479 126.083 187.236 1.00 129.00 ? 148 PHE A N   1 
ATOM   915  C CA  . PHE A 1 148 ? 130.650 124.966 186.803 1.00 129.02 ? 148 PHE A CA  1 
ATOM   916  C C   . PHE A 1 148 ? 129.517 125.388 185.878 1.00 133.40 ? 148 PHE A C   1 
ATOM   917  O O   . PHE A 1 148 ? 128.927 124.526 185.218 1.00 132.78 ? 148 PHE A O   1 
ATOM   918  C CB  . PHE A 1 148 ? 130.074 124.234 188.017 1.00 128.25 ? 148 PHE A CB  1 
ATOM   919  C CG  . PHE A 1 148 ? 130.958 124.283 189.229 1.00 129.65 ? 148 PHE A CG  1 
ATOM   920  C CD1 . PHE A 1 148 ? 131.987 123.370 189.386 1.00 131.32 ? 148 PHE A CD1 1 
ATOM   921  C CD2 . PHE A 1 148 ? 130.757 125.237 190.212 1.00 128.33 ? 148 PHE A CD2 1 
ATOM   922  C CE1 . PHE A 1 148 ? 132.803 123.410 190.502 1.00 130.59 ? 148 PHE A CE1 1 
ATOM   923  C CE2 . PHE A 1 148 ? 131.570 125.282 191.330 1.00 129.34 ? 148 PHE A CE2 1 
ATOM   924  C CZ  . PHE A 1 148 ? 132.594 124.367 191.475 1.00 129.99 ? 148 PHE A CZ  1 
ATOM   925  N N   . LEU A 1 149 ? 129.196 126.682 185.815 1.00 138.95 ? 149 LEU A N   1 
ATOM   926  C CA  . LEU A 1 149 ? 128.170 127.141 184.884 1.00 141.91 ? 149 LEU A CA  1 
ATOM   927  C C   . LEU A 1 149 ? 128.597 126.911 183.440 1.00 140.88 ? 149 LEU A C   1 
ATOM   928  O O   . LEU A 1 149 ? 127.782 126.518 182.597 1.00 141.80 ? 149 LEU A O   1 
ATOM   929  C CB  . LEU A 1 149 ? 127.856 128.618 185.130 1.00 143.35 ? 149 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 149 ? 129.016 129.617 185.087 1.00 142.60 ? 149 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 149 ? 129.021 130.388 183.773 1.00 141.44 ? 149 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 149 ? 128.949 130.570 186.270 1.00 143.25 ? 149 LEU A CD2 1 
ATOM   933  N N   . SER A 1 150 ? 129.871 127.158 183.133 1.00 136.44 ? 150 SER A N   1 
ATOM   934  C CA  . SER A 1 150 ? 130.429 126.915 181.810 1.00 132.36 ? 150 SER A CA  1 
ATOM   935  C C   . SER A 1 150 ? 131.106 125.553 181.716 1.00 134.83 ? 150 SER A C   1 
ATOM   936  O O   . SER A 1 150 ? 132.067 125.387 180.956 1.00 136.89 ? 150 SER A O   1 
ATOM   937  C CB  . SER A 1 150 ? 131.412 128.023 181.439 1.00 123.63 ? 150 SER A CB  1 
ATOM   938  O OG  . SER A 1 150 ? 131.861 127.875 180.104 1.00 122.89 ? 150 SER A OG  1 
ATOM   939  N N   . ASN A 1 151 ? 130.629 124.576 182.482 1.00 134.72 ? 151 ASN A N   1 
ATOM   940  C CA  . ASN A 1 151 ? 131.186 123.227 182.499 1.00 133.88 ? 151 ASN A CA  1 
ATOM   941  C C   . ASN A 1 151 ? 130.222 122.285 181.783 1.00 135.63 ? 151 ASN A C   1 
ATOM   942  O O   . ASN A 1 151 ? 129.391 121.626 182.410 1.00 136.41 ? 151 ASN A O   1 
ATOM   943  C CB  . ASN A 1 151 ? 131.441 122.776 183.948 1.00 133.28 ? 151 ASN A CB  1 
ATOM   944  C CG  . ASN A 1 151 ? 132.349 121.562 184.037 1.00 133.74 ? 151 ASN A CG  1 
ATOM   945  O OD1 . ASN A 1 151 ? 132.432 120.758 183.109 1.00 136.68 ? 151 ASN A OD1 1 
ATOM   946  N ND2 . ASN A 1 151 ? 133.030 121.421 185.168 1.00 130.42 ? 151 ASN A ND2 1 
ATOM   947  N N   . MET A 1 152 ? 130.339 122.214 180.457 1.00 134.56 ? 152 MET A N   1 
ATOM   948  C CA  . MET A 1 152 ? 129.656 121.175 179.700 1.00 140.18 ? 152 MET A CA  1 
ATOM   949  C C   . MET A 1 152 ? 130.662 120.097 179.323 1.00 139.18 ? 152 MET A C   1 
ATOM   950  O O   . MET A 1 152 ? 131.833 120.381 179.055 1.00 136.41 ? 152 MET A O   1 
ATOM   951  C CB  . MET A 1 152 ? 128.977 121.675 178.413 1.00 142.47 ? 152 MET A CB  1 
ATOM   952  C CG  . MET A 1 152 ? 129.849 122.376 177.365 1.00 140.45 ? 152 MET A CG  1 
ATOM   953  S SD  . MET A 1 152 ? 130.946 123.732 177.800 1.00 134.92 ? 152 MET A SD  1 
ATOM   954  C CE  . MET A 1 152 ? 129.845 124.735 178.788 1.00 131.67 ? 152 MET A CE  1 
ATOM   955  N N   . SER A 1 153 ? 130.193 118.852 179.294 1.00 142.11 ? 153 SER A N   1 
ATOM   956  C CA  . SER A 1 153 ? 131.081 117.726 179.036 1.00 145.93 ? 153 SER A CA  1 
ATOM   957  C C   . SER A 1 153 ? 130.288 116.571 178.446 1.00 151.25 ? 153 SER A C   1 
ATOM   958  O O   . SER A 1 153 ? 129.273 116.158 179.015 1.00 151.65 ? 153 SER A O   1 
ATOM   959  C CB  . SER A 1 153 ? 131.780 117.291 180.325 1.00 144.75 ? 153 SER A CB  1 
ATOM   960  O OG  . SER A 1 153 ? 130.895 116.555 181.150 1.00 146.74 ? 153 SER A OG  1 
ATOM   961  N N   . MET A 1 154 ? 130.757 116.051 177.313 1.00 150.49 ? 154 MET A N   1 
ATOM   962  C CA  . MET A 1 154 ? 130.140 114.890 176.688 1.00 148.80 ? 154 MET A CA  1 
ATOM   963  C C   . MET A 1 154 ? 131.155 114.238 175.762 1.00 145.80 ? 154 MET A C   1 
ATOM   964  O O   . MET A 1 154 ? 132.127 114.866 175.335 1.00 142.89 ? 154 MET A O   1 
ATOM   965  C CB  . MET A 1 154 ? 128.870 115.270 175.920 1.00 152.10 ? 154 MET A CB  1 
ATOM   966  C CG  . MET A 1 154 ? 129.126 116.050 174.644 1.00 154.28 ? 154 MET A CG  1 
ATOM   967  S SD  . MET A 1 154 ? 130.117 117.529 174.920 1.00 160.65 ? 154 MET A SD  1 
ATOM   968  C CE  . MET A 1 154 ? 128.937 118.584 175.756 1.00 148.73 ? 154 MET A CE  1 
ATOM   969  N N   . ASP A 1 155 ? 130.912 112.968 175.453 1.00 146.89 ? 155 ASP A N   1 
ATOM   970  C CA  . ASP A 1 155 ? 131.806 112.209 174.587 1.00 146.38 ? 155 ASP A CA  1 
ATOM   971  C C   . ASP A 1 155 ? 131.477 112.450 173.117 1.00 143.08 ? 155 ASP A C   1 
ATOM   972  O O   . ASP A 1 155 ? 132.259 112.109 172.230 1.00 140.54 ? 155 ASP A O   1 
ATOM   973  C CB  . ASP A 1 155 ? 131.723 110.715 174.908 1.00 146.33 ? 155 ASP A CB  1 
ATOM   974  C CG  . ASP A 1 155 ? 132.334 110.375 176.253 1.00 149.55 ? 155 ASP A CG  1 
ATOM   975  O OD1 . ASP A 1 155 ? 132.431 111.282 177.106 1.00 149.35 ? 155 ASP A OD1 1 
ATOM   976  O OD2 . ASP A 1 155 ? 132.717 109.204 176.458 1.00 150.46 ? 155 ASP A OD2 1 
ATOM   977  N N   . GLY A 1 173 ? 137.910 106.649 195.750 1.00 144.02 ? 173 GLY A N   1 
ATOM   978  C CA  . GLY A 1 173 ? 136.586 106.514 195.172 1.00 140.59 ? 173 GLY A CA  1 
ATOM   979  C C   . GLY A 1 173 ? 136.609 106.143 193.702 1.00 142.03 ? 173 GLY A C   1 
ATOM   980  O O   . GLY A 1 173 ? 136.149 105.068 193.317 1.00 139.44 ? 173 GLY A O   1 
ATOM   981  N N   . SER A 1 174 ? 137.145 107.040 192.877 1.00 141.10 ? 174 SER A N   1 
ATOM   982  C CA  . SER A 1 174 ? 137.235 106.831 191.439 1.00 140.66 ? 174 SER A CA  1 
ATOM   983  C C   . SER A 1 174 ? 138.638 107.180 190.967 1.00 143.95 ? 174 SER A C   1 
ATOM   984  O O   . SER A 1 174 ? 139.177 108.227 191.337 1.00 140.49 ? 174 SER A O   1 
ATOM   985  C CB  . SER A 1 174 ? 136.196 107.674 190.693 1.00 138.49 ? 174 SER A CB  1 
ATOM   986  O OG  . SER A 1 174 ? 136.122 108.983 191.230 1.00 140.19 ? 174 SER A OG  1 
ATOM   987  N N   . CYS A 1 175 ? 139.222 106.303 190.154 1.00 149.01 ? 175 CYS A N   1 
ATOM   988  C CA  . CYS A 1 175 ? 140.557 106.539 189.626 1.00 148.33 ? 175 CYS A CA  1 
ATOM   989  C C   . CYS A 1 175 ? 140.527 107.630 188.561 1.00 143.62 ? 175 CYS A C   1 
ATOM   990  O O   . CYS A 1 175 ? 139.519 107.839 187.882 1.00 142.41 ? 175 CYS A O   1 
ATOM   991  C CB  . CYS A 1 175 ? 141.134 105.250 189.042 1.00 149.04 ? 175 CYS A CB  1 
ATOM   992  S SG  . CYS A 1 175 ? 142.544 105.495 187.944 1.00 155.05 ? 175 CYS A SG  1 
ATOM   993  N N   . TRP A 1 176 ? 141.655 108.325 188.411 1.00 139.50 ? 176 TRP A N   1 
ATOM   994  C CA  . TRP A 1 176 ? 141.713 109.497 187.541 1.00 137.42 ? 176 TRP A CA  1 
ATOM   995  C C   . TRP A 1 176 ? 142.067 109.127 186.102 1.00 135.30 ? 176 TRP A C   1 
ATOM   996  O O   . TRP A 1 176 ? 141.278 109.365 185.182 1.00 134.83 ? 176 TRP A O   1 
ATOM   997  C CB  . TRP A 1 176 ? 142.724 110.510 188.093 1.00 131.45 ? 176 TRP A CB  1 
ATOM   998  C CG  . TRP A 1 176 ? 142.416 111.937 187.731 1.00 123.54 ? 176 TRP A CG  1 
ATOM   999  C CD1 . TRP A 1 176 ? 141.948 112.907 188.567 1.00 123.02 ? 176 TRP A CD1 1 
ATOM   1000 C CD2 . TRP A 1 176 ? 142.548 112.550 186.442 1.00 115.36 ? 176 TRP A CD2 1 
ATOM   1001 N NE1 . TRP A 1 176 ? 141.783 114.085 187.883 1.00 114.59 ? 176 TRP A NE1 1 
ATOM   1002 C CE2 . TRP A 1 176 ? 142.143 113.893 186.576 1.00 109.95 ? 176 TRP A CE2 1 
ATOM   1003 C CE3 . TRP A 1 176 ? 142.970 112.096 185.189 1.00 115.50 ? 176 TRP A CE3 1 
ATOM   1004 C CZ2 . TRP A 1 176 ? 142.147 114.784 185.508 1.00 104.92 ? 176 TRP A CZ2 1 
ATOM   1005 C CZ3 . TRP A 1 176 ? 142.971 112.982 184.129 1.00 111.46 ? 176 TRP A CZ3 1 
ATOM   1006 C CH2 . TRP A 1 176 ? 142.562 114.310 184.295 1.00 103.54 ? 176 TRP A CH2 1 
ATOM   1007 N N   . GLY A 1 177 ? 143.243 108.542 185.894 1.00 133.86 ? 177 GLY A N   1 
ATOM   1008 C CA  . GLY A 1 177 ? 143.718 108.288 184.548 1.00 136.07 ? 177 GLY A CA  1 
ATOM   1009 C C   . GLY A 1 177 ? 143.978 106.828 184.244 1.00 151.08 ? 177 GLY A C   1 
ATOM   1010 O O   . GLY A 1 177 ? 143.607 105.948 185.026 1.00 156.97 ? 177 GLY A O   1 
ATOM   1011 N N   . ALA A 1 178 ? 144.617 106.562 183.106 1.00 151.00 ? 178 ALA A N   1 
ATOM   1012 C CA  . ALA A 1 178 ? 144.903 105.190 182.710 1.00 152.15 ? 178 ALA A CA  1 
ATOM   1013 C C   . ALA A 1 178 ? 145.797 104.510 183.738 1.00 153.10 ? 178 ALA A C   1 
ATOM   1014 O O   . ALA A 1 178 ? 146.767 105.094 184.229 1.00 152.66 ? 178 ALA A O   1 
ATOM   1015 C CB  . ALA A 1 178 ? 145.566 105.162 181.333 1.00 146.27 ? 178 ALA A CB  1 
ATOM   1016 N N   . GLY A 1 179 ? 145.462 103.265 184.065 1.00 151.26 ? 179 GLY A N   1 
ATOM   1017 C CA  . GLY A 1 179 ? 146.191 102.534 185.081 1.00 151.26 ? 179 GLY A CA  1 
ATOM   1018 C C   . GLY A 1 179 ? 145.678 102.820 186.476 1.00 149.06 ? 179 GLY A C   1 
ATOM   1019 O O   . GLY A 1 179 ? 145.458 103.979 186.839 1.00 146.00 ? 179 GLY A O   1 
ATOM   1020 N N   . GLU A 1 180 ? 145.482 101.766 187.270 1.00 150.56 ? 180 GLU A N   1 
ATOM   1021 C CA  . GLU A 1 180 ? 144.958 101.925 188.621 1.00 149.69 ? 180 GLU A CA  1 
ATOM   1022 C C   . GLU A 1 180 ? 145.975 102.519 189.586 1.00 149.46 ? 180 GLU A C   1 
ATOM   1023 O O   . GLU A 1 180 ? 145.604 102.859 190.715 1.00 148.21 ? 180 GLU A O   1 
ATOM   1024 C CB  . GLU A 1 180 ? 144.467 100.576 189.152 1.00 150.20 ? 180 GLU A CB  1 
ATOM   1025 C CG  . GLU A 1 180 ? 143.262 100.023 188.408 1.00 153.58 ? 180 GLU A CG  1 
ATOM   1026 C CD  . GLU A 1 180 ? 142.362 99.185  189.295 1.00 151.50 ? 180 GLU A CD  1 
ATOM   1027 O OE1 . GLU A 1 180 ? 142.735 98.940  190.462 1.00 151.74 ? 180 GLU A OE1 1 
ATOM   1028 O OE2 . GLU A 1 180 ? 141.281 98.772  188.826 1.00 145.41 ? 180 GLU A OE2 1 
ATOM   1029 N N   . GLU A 1 181 ? 147.239 102.649 189.177 1.00 151.36 ? 181 GLU A N   1 
ATOM   1030 C CA  . GLU A 1 181 ? 148.262 103.195 190.062 1.00 151.84 ? 181 GLU A CA  1 
ATOM   1031 C C   . GLU A 1 181 ? 148.043 104.671 190.370 1.00 154.32 ? 181 GLU A C   1 
ATOM   1032 O O   . GLU A 1 181 ? 148.577 105.165 191.369 1.00 153.36 ? 181 GLU A O   1 
ATOM   1033 C CB  . GLU A 1 181 ? 149.649 102.992 189.449 1.00 148.95 ? 181 GLU A CB  1 
ATOM   1034 C CG  . GLU A 1 181 ? 150.002 103.984 188.350 1.00 153.24 ? 181 GLU A CG  1 
ATOM   1035 C CD  . GLU A 1 181 ? 149.348 103.644 187.025 1.00 152.81 ? 181 GLU A CD  1 
ATOM   1036 O OE1 . GLU A 1 181 ? 148.961 102.472 186.836 1.00 155.56 ? 181 GLU A OE1 1 
ATOM   1037 O OE2 . GLU A 1 181 ? 149.223 104.549 186.173 1.00 149.55 ? 181 GLU A OE2 1 
ATOM   1038 N N   . ASN A 1 182 ? 147.279 105.382 189.547 1.00 156.69 ? 182 ASN A N   1 
ATOM   1039 C CA  . ASN A 1 182 ? 147.031 106.802 189.743 1.00 152.75 ? 182 ASN A CA  1 
ATOM   1040 C C   . ASN A 1 182 ? 145.663 107.021 190.377 1.00 151.15 ? 182 ASN A C   1 
ATOM   1041 O O   . ASN A 1 182 ? 144.742 106.217 190.209 1.00 152.99 ? 182 ASN A O   1 
ATOM   1042 C CB  . ASN A 1 182 ? 147.122 107.560 188.416 1.00 145.54 ? 182 ASN A CB  1 
ATOM   1043 C CG  . ASN A 1 182 ? 145.943 107.288 187.503 1.00 144.76 ? 182 ASN A CG  1 
ATOM   1044 O OD1 . ASN A 1 182 ? 144.908 107.950 187.590 1.00 143.53 ? 182 ASN A OD1 1 
ATOM   1045 N ND2 . ASN A 1 182 ? 146.094 106.309 186.618 1.00 145.04 ? 182 ASN A ND2 1 
ATOM   1046 N N   . CYS A 1 183 ? 145.540 108.125 191.111 1.00 142.64 ? 183 CYS A N   1 
ATOM   1047 C CA  . CYS A 1 183 ? 144.306 108.470 191.800 1.00 140.56 ? 183 CYS A CA  1 
ATOM   1048 C C   . CYS A 1 183 ? 144.044 109.960 191.637 1.00 139.96 ? 183 CYS A C   1 
ATOM   1049 O O   . CYS A 1 183 ? 144.923 110.730 191.241 1.00 140.52 ? 183 CYS A O   1 
ATOM   1050 C CB  . CYS A 1 183 ? 144.362 108.089 193.285 1.00 144.05 ? 183 CYS A CB  1 
ATOM   1051 S SG  . CYS A 1 183 ? 142.770 107.591 193.983 1.00 160.77 ? 183 CYS A SG  1 
ATOM   1052 N N   . GLN A 1 184 ? 142.809 110.364 191.946 1.00 140.29 ? 184 GLN A N   1 
ATOM   1053 C CA  . GLN A 1 184 ? 142.415 111.755 191.748 1.00 137.41 ? 184 GLN A CA  1 
ATOM   1054 C C   . GLN A 1 184 ? 142.993 112.661 192.831 1.00 133.56 ? 184 GLN A C   1 
ATOM   1055 O O   . GLN A 1 184 ? 143.212 113.853 192.584 1.00 129.35 ? 184 GLN A O   1 
ATOM   1056 C CB  . GLN A 1 184 ? 140.885 111.844 191.676 1.00 136.77 ? 184 GLN A CB  1 
ATOM   1057 C CG  . GLN A 1 184 ? 140.262 113.237 191.780 1.00 133.96 ? 184 GLN A CG  1 
ATOM   1058 C CD  . GLN A 1 184 ? 140.158 113.744 193.201 1.00 136.24 ? 184 GLN A CD  1 
ATOM   1059 O OE1 . GLN A 1 184 ? 140.053 112.961 194.143 1.00 139.43 ? 184 GLN A OE1 1 
ATOM   1060 N NE2 . GLN A 1 184 ? 140.178 115.062 193.362 1.00 134.89 ? 184 GLN A NE2 1 
ATOM   1061 N N   . LYS A 1 185 ? 143.264 112.114 194.019 1.00 132.20 ? 185 LYS A N   1 
ATOM   1062 C CA  . LYS A 1 185 ? 143.905 112.844 195.117 1.00 130.78 ? 185 LYS A CA  1 
ATOM   1063 C C   . LYS A 1 185 ? 143.093 114.080 195.519 1.00 136.34 ? 185 LYS A C   1 
ATOM   1064 O O   . LYS A 1 185 ? 143.521 115.224 195.353 1.00 137.07 ? 185 LYS A O   1 
ATOM   1065 C CB  . LYS A 1 185 ? 145.348 113.224 194.762 1.00 130.34 ? 185 LYS A CB  1 
ATOM   1066 C CG  . LYS A 1 185 ? 146.102 112.174 193.958 1.00 128.33 ? 185 LYS A CG  1 
ATOM   1067 C CD  . LYS A 1 185 ? 147.524 112.622 193.662 1.00 119.88 ? 185 LYS A CD  1 
ATOM   1068 C CE  . LYS A 1 185 ? 147.592 113.423 192.372 1.00 113.11 ? 185 LYS A CE  1 
ATOM   1069 N NZ  . LYS A 1 185 ? 148.948 113.375 191.757 1.00 105.71 ? 185 LYS A NZ  1 
ATOM   1070 N N   . LEU A 1 186 ? 141.899 113.822 196.049 1.00 138.28 ? 186 LEU A N   1 
ATOM   1071 C CA  . LEU A 1 186 ? 141.034 114.901 196.511 1.00 139.04 ? 186 LEU A CA  1 
ATOM   1072 C C   . LEU A 1 186 ? 141.695 115.677 197.644 1.00 137.84 ? 186 LEU A C   1 
ATOM   1073 O O   . LEU A 1 186 ? 142.313 115.097 198.542 1.00 136.52 ? 186 LEU A O   1 
ATOM   1074 C CB  . LEU A 1 186 ? 139.690 114.338 196.974 1.00 139.58 ? 186 LEU A CB  1 
ATOM   1075 C CG  . LEU A 1 186 ? 138.614 115.344 197.385 1.00 136.97 ? 186 LEU A CG  1 
ATOM   1076 C CD1 . LEU A 1 186 ? 138.420 116.399 196.307 1.00 133.55 ? 186 LEU A CD1 1 
ATOM   1077 C CD2 . LEU A 1 186 ? 137.305 114.631 197.684 1.00 131.99 ? 186 LEU A CD2 1 
ATOM   1078 N N   . THR A 1 187 ? 141.562 117.002 197.595 1.00 135.27 ? 187 THR A N   1 
ATOM   1079 C CA  . THR A 1 187 ? 142.126 117.877 198.616 1.00 134.85 ? 187 THR A CA  1 
ATOM   1080 C C   . THR A 1 187 ? 141.165 118.937 199.132 1.00 136.04 ? 187 THR A C   1 
ATOM   1081 O O   . THR A 1 187 ? 141.416 119.486 200.212 1.00 136.93 ? 187 THR A O   1 
ATOM   1082 C CB  . THR A 1 187 ? 143.386 118.579 198.088 1.00 135.00 ? 187 THR A CB  1 
ATOM   1083 O OG1 . THR A 1 187 ? 143.886 119.481 199.083 1.00 134.30 ? 187 THR A OG1 1 
ATOM   1084 C CG2 . THR A 1 187 ? 143.071 119.355 196.818 1.00 139.00 ? 187 THR A CG2 1 
ATOM   1085 N N   . LYS A 1 188 ? 140.087 119.246 198.414 1.00 135.42 ? 188 LYS A N   1 
ATOM   1086 C CA  . LYS A 1 188 ? 139.142 120.278 198.825 1.00 137.44 ? 188 LYS A CA  1 
ATOM   1087 C C   . LYS A 1 188 ? 137.862 119.701 199.418 1.00 140.73 ? 188 LYS A C   1 
ATOM   1088 O O   . LYS A 1 188 ? 137.418 120.144 200.482 1.00 140.83 ? 188 LYS A O   1 
ATOM   1089 C CB  . LYS A 1 188 ? 138.803 121.182 197.633 1.00 132.53 ? 188 LYS A CB  1 
ATOM   1090 C CG  . LYS A 1 188 ? 139.995 121.938 197.070 1.00 132.33 ? 188 LYS A CG  1 
ATOM   1091 C CD  . LYS A 1 188 ? 140.715 122.722 198.156 1.00 136.85 ? 188 LYS A CD  1 
ATOM   1092 C CE  . LYS A 1 188 ? 142.033 123.284 197.650 1.00 136.32 ? 188 LYS A CE  1 
ATOM   1093 N NZ  . LYS A 1 188 ? 142.958 123.621 198.768 1.00 127.86 ? 188 LYS A NZ  1 
ATOM   1094 N N   . ILE A 1 189 ? 137.259 118.722 198.753 1.00 139.25 ? 189 ILE A N   1 
ATOM   1095 C CA  . ILE A 1 189 ? 136.021 118.123 199.233 1.00 136.86 ? 189 ILE A CA  1 
ATOM   1096 C C   . ILE A 1 189 ? 136.323 116.953 200.161 1.00 133.14 ? 189 ILE A C   1 
ATOM   1097 O O   . ILE A 1 189 ? 137.485 116.643 200.427 1.00 128.65 ? 189 ILE A O   1 
ATOM   1098 C CB  . ILE A 1 189 ? 135.129 117.674 198.063 1.00 135.99 ? 189 ILE A CB  1 
ATOM   1099 C CG1 . ILE A 1 189 ? 135.316 118.605 196.863 1.00 134.48 ? 189 ILE A CG1 1 
ATOM   1100 C CG2 . ILE A 1 189 ? 133.670 117.636 198.490 1.00 134.58 ? 189 ILE A CG2 1 
ATOM   1101 C CD1 . ILE A 1 189 ? 134.629 118.123 195.604 1.00 124.90 ? 189 ILE A CD1 1 
ATOM   1102 N N   . GLN A 1 211 ? 148.171 129.670 199.090 1.00 135.63 ? 211 GLN A N   1 
ATOM   1103 C CA  . GLN A 1 211 ? 146.969 128.862 198.926 1.00 130.29 ? 211 GLN A CA  1 
ATOM   1104 C C   . GLN A 1 211 ? 147.167 127.859 197.795 1.00 127.01 ? 211 GLN A C   1 
ATOM   1105 O O   . GLN A 1 211 ? 147.143 128.220 196.619 1.00 124.60 ? 211 GLN A O   1 
ATOM   1106 C CB  . GLN A 1 211 ? 145.748 129.752 198.645 1.00 129.32 ? 211 GLN A CB  1 
ATOM   1107 C CG  . GLN A 1 211 ? 145.376 130.777 199.726 1.00 130.21 ? 211 GLN A CG  1 
ATOM   1108 C CD  . GLN A 1 211 ? 146.473 131.779 200.033 1.00 132.39 ? 211 GLN A CD  1 
ATOM   1109 O OE1 . GLN A 1 211 ? 146.841 131.982 201.190 1.00 129.50 ? 211 GLN A OE1 1 
ATOM   1110 N NE2 . GLN A 1 211 ? 147.004 132.413 198.993 1.00 134.25 ? 211 GLN A NE2 1 
ATOM   1111 N N   . CYS A 1 212 ? 147.317 126.575 198.139 1.00 133.29 ? 212 CYS A N   1 
ATOM   1112 C CA  . CYS A 1 212 ? 147.583 125.514 197.132 1.00 137.79 ? 212 CYS A CA  1 
ATOM   1113 C C   . CYS A 1 212 ? 146.279 125.168 196.402 1.00 135.77 ? 212 CYS A C   1 
ATOM   1114 O O   . CYS A 1 212 ? 145.221 125.183 197.070 1.00 138.38 ? 212 CYS A O   1 
ATOM   1115 C CB  . CYS A 1 212 ? 148.159 124.254 197.771 1.00 140.71 ? 212 CYS A CB  1 
ATOM   1116 S SG  . CYS A 1 212 ? 148.989 124.517 199.362 1.00 148.61 ? 212 CYS A SG  1 
ATOM   1117 N N   . ALA A 1 213 ? 146.346 124.871 195.100 1.00 132.94 ? 213 ALA A N   1 
ATOM   1118 C CA  . ALA A 1 213 ? 145.157 124.534 194.280 1.00 129.32 ? 213 ALA A CA  1 
ATOM   1119 C C   . ALA A 1 213 ? 145.285 123.107 193.742 1.00 126.62 ? 213 ALA A C   1 
ATOM   1120 O O   . ALA A 1 213 ? 144.452 122.261 194.134 1.00 119.46 ? 213 ALA A O   1 
ATOM   1121 C CB  . ALA A 1 213 ? 145.008 125.544 193.165 1.00 121.66 ? 213 ALA A CB  1 
ATOM   1122 N N   . ALA A 1 214 ? 146.292 122.831 192.906 1.00 127.07 ? 214 ALA A N   1 
ATOM   1123 C CA  . ALA A 1 214 ? 146.485 121.497 192.287 1.00 125.28 ? 214 ALA A CA  1 
ATOM   1124 C C   . ALA A 1 214 ? 147.073 120.534 193.318 1.00 130.26 ? 214 ALA A C   1 
ATOM   1125 O O   . ALA A 1 214 ? 148.300 120.294 193.272 1.00 127.18 ? 214 ALA A O   1 
ATOM   1126 C CB  . ALA A 1 214 ? 147.364 121.615 191.062 1.00 108.60 ? 214 ALA A CB  1 
ATOM   1127 N N   . GLY A 1 215 ? 146.235 120.001 194.214 1.00 132.51 ? 215 GLY A N   1 
ATOM   1128 C CA  . GLY A 1 215 ? 146.678 119.060 195.262 1.00 133.98 ? 215 GLY A CA  1 
ATOM   1129 C C   . GLY A 1 215 ? 146.704 119.734 196.621 1.00 139.40 ? 215 GLY A C   1 
ATOM   1130 O O   . GLY A 1 215 ? 146.461 120.960 196.652 1.00 134.22 ? 215 GLY A O   1 
ATOM   1131 N N   . ASP A 1 223 ? 153.608 127.053 202.503 1.00 143.91 ? 223 ASP A N   1 
ATOM   1132 C CA  . ASP A 1 223 ? 154.549 126.887 201.401 1.00 142.37 ? 223 ASP A CA  1 
ATOM   1133 C C   . ASP A 1 223 ? 153.998 125.924 200.356 1.00 139.85 ? 223 ASP A C   1 
ATOM   1134 O O   . ASP A 1 223 ? 154.454 124.786 200.242 1.00 134.80 ? 223 ASP A O   1 
ATOM   1135 C CB  . ASP A 1 223 ? 155.899 126.391 201.920 1.00 142.33 ? 223 ASP A CB  1 
ATOM   1136 C CG  . ASP A 1 223 ? 156.576 127.396 202.831 1.00 145.23 ? 223 ASP A CG  1 
ATOM   1137 O OD1 . ASP A 1 223 ? 155.859 128.167 203.502 1.00 138.34 ? 223 ASP A OD1 1 
ATOM   1138 O OD2 . ASP A 1 223 ? 157.824 127.416 202.875 1.00 151.65 ? 223 ASP A OD2 1 
ATOM   1139 N N   . CYS A 1 224 ? 153.011 126.391 199.598 1.00 141.93 ? 224 CYS A N   1 
ATOM   1140 C CA  . CYS A 1 224 ? 152.390 125.566 198.574 1.00 141.20 ? 224 CYS A CA  1 
ATOM   1141 C C   . CYS A 1 224 ? 153.357 125.311 197.424 1.00 136.99 ? 224 CYS A C   1 
ATOM   1142 O O   . CYS A 1 224 ? 154.194 126.152 197.086 1.00 137.82 ? 224 CYS A O   1 
ATOM   1143 C CB  . CYS A 1 224 ? 151.123 126.235 198.048 1.00 145.04 ? 224 CYS A CB  1 
ATOM   1144 S SG  . CYS A 1 224 ? 149.799 126.379 199.266 1.00 158.18 ? 224 CYS A SG  1 
ATOM   1145 N N   . LEU A 1 225 ? 153.236 124.125 196.823 1.00 131.96 ? 225 LEU A N   1 
ATOM   1146 C CA  . LEU A 1 225 ? 154.045 123.809 195.651 1.00 130.07 ? 225 LEU A CA  1 
ATOM   1147 C C   . LEU A 1 225 ? 153.707 124.732 194.486 1.00 126.97 ? 225 LEU A C   1 
ATOM   1148 O O   . LEU A 1 225 ? 154.604 125.189 193.767 1.00 125.88 ? 225 LEU A O   1 
ATOM   1149 C CB  . LEU A 1 225 ? 153.857 122.340 195.261 1.00 124.40 ? 225 LEU A CB  1 
ATOM   1150 C CG  . LEU A 1 225 ? 152.439 121.805 195.046 1.00 118.88 ? 225 LEU A CG  1 
ATOM   1151 C CD1 . LEU A 1 225 ? 152.425 120.788 193.919 1.00 110.27 ? 225 LEU A CD1 1 
ATOM   1152 C CD2 . LEU A 1 225 ? 151.889 121.188 196.323 1.00 121.56 ? 225 LEU A CD2 1 
ATOM   1153 N N   . VAL A 1 226 ? 152.409 125.004 194.292 1.00 122.06 ? 226 VAL A N   1 
ATOM   1154 C CA  . VAL A 1 226 ? 151.931 125.942 193.231 1.00 117.51 ? 226 VAL A CA  1 
ATOM   1155 C C   . VAL A 1 226 ? 150.997 126.933 193.936 1.00 124.83 ? 226 VAL A C   1 
ATOM   1156 O O   . VAL A 1 226 ? 150.098 126.457 194.663 1.00 128.73 ? 226 VAL A O   1 
ATOM   1157 C CB  . VAL A 1 226 ? 151.228 125.249 192.048 1.00 107.57 ? 226 VAL A CB  1 
ATOM   1158 C CG1 . VAL A 1 226 ? 151.052 126.199 190.869 1.00 103.82 ? 226 VAL A CG1 1 
ATOM   1159 C CG2 . VAL A 1 226 ? 151.968 123.994 191.605 1.00 106.14 ? 226 VAL A CG2 1 
ATOM   1160 N N   . CYS A 1 227 ? 151.184 128.241 193.739 1.00 127.15 ? 227 CYS A N   1 
ATOM   1161 C CA  . CYS A 1 227 ? 150.417 129.261 194.436 1.00 121.60 ? 227 CYS A CA  1 
ATOM   1162 C C   . CYS A 1 227 ? 149.185 129.688 193.640 1.00 120.42 ? 227 CYS A C   1 
ATOM   1163 O O   . CYS A 1 227 ? 149.004 129.340 192.471 1.00 118.77 ? 227 CYS A O   1 
ATOM   1164 C CB  . CYS A 1 227 ? 151.290 130.478 194.733 1.00 122.04 ? 227 CYS A CB  1 
ATOM   1165 S SG  . CYS A 1 227 ? 150.382 131.850 195.484 1.00 132.94 ? 227 CYS A SG  1 
ATOM   1166 N N   . ARG A 1 228 ? 148.328 130.462 194.311 1.00 121.42 ? 228 ARG A N   1 
ATOM   1167 C CA  . ARG A 1 228 ? 147.127 130.999 193.680 1.00 118.42 ? 228 ARG A CA  1 
ATOM   1168 C C   . ARG A 1 228 ? 147.484 131.953 192.547 1.00 112.32 ? 228 ARG A C   1 
ATOM   1169 O O   . ARG A 1 228 ? 147.020 131.791 191.412 1.00 112.81 ? 228 ARG A O   1 
ATOM   1170 C CB  . ARG A 1 228 ? 146.285 131.711 194.741 1.00 116.48 ? 228 ARG A CB  1 
ATOM   1171 C CG  . ARG A 1 228 ? 145.163 130.887 195.364 1.00 113.15 ? 228 ARG A CG  1 
ATOM   1172 C CD  . ARG A 1 228 ? 144.125 130.380 194.375 1.00 111.17 ? 228 ARG A CD  1 
ATOM   1173 N NE  . ARG A 1 228 ? 143.639 131.450 193.513 1.00 111.65 ? 228 ARG A NE  1 
ATOM   1174 C CZ  . ARG A 1 228 ? 143.376 131.319 192.221 1.00 107.82 ? 228 ARG A CZ  1 
ATOM   1175 N NH1 . ARG A 1 228 ? 143.488 130.155 191.609 1.00 100.33 ? 228 ARG A NH1 1 
ATOM   1176 N NH2 . ARG A 1 228 ? 142.968 132.379 191.532 1.00 108.12 ? 228 ARG A NH2 1 
ATOM   1177 N N   . LYS A 1 229 ? 148.315 132.955 192.837 1.00 107.66 ? 229 LYS A N   1 
ATOM   1178 C CA  . LYS A 1 229 ? 148.737 133.933 191.840 1.00 108.59 ? 229 LYS A CA  1 
ATOM   1179 C C   . LYS A 1 229 ? 150.241 133.916 191.605 1.00 110.66 ? 229 LYS A C   1 
ATOM   1180 O O   . LYS A 1 229 ? 150.677 133.732 190.465 1.00 110.48 ? 229 LYS A O   1 
ATOM   1181 C CB  . LYS A 1 229 ? 148.279 135.336 192.256 1.00 117.34 ? 229 LYS A CB  1 
ATOM   1182 C CG  . LYS A 1 229 ? 146.866 135.703 191.830 1.00 115.83 ? 229 LYS A CG  1 
ATOM   1183 C CD  . LYS A 1 229 ? 146.704 135.599 190.322 1.00 103.05 ? 229 LYS A CD  1 
ATOM   1184 C CE  . LYS A 1 229 ? 145.252 135.754 189.906 1.00 100.93 ? 229 LYS A CE  1 
ATOM   1185 N NZ  . LYS A 1 229 ? 144.373 134.753 190.563 1.00 103.46 ? 229 LYS A NZ  1 
ATOM   1186 N N   . PHE A 1 230 ? 151.051 134.100 192.647 1.00 115.14 ? 230 PHE A N   1 
ATOM   1187 C CA  . PHE A 1 230 ? 152.486 134.276 192.484 1.00 113.44 ? 230 PHE A CA  1 
ATOM   1188 C C   . PHE A 1 230 ? 153.235 133.471 193.535 1.00 119.06 ? 230 PHE A C   1 
ATOM   1189 O O   . PHE A 1 230 ? 152.911 133.533 194.724 1.00 127.72 ? 230 PHE A O   1 
ATOM   1190 C CB  . PHE A 1 230 ? 152.874 135.757 192.589 1.00 111.37 ? 230 PHE A CB  1 
ATOM   1191 C CG  . PHE A 1 230 ? 152.426 136.588 191.419 1.00 107.87 ? 230 PHE A CG  1 
ATOM   1192 C CD1 . PHE A 1 230 ? 152.612 136.145 190.122 1.00 103.13 ? 230 PHE A CD1 1 
ATOM   1193 C CD2 . PHE A 1 230 ? 151.810 137.811 191.621 1.00 108.02 ? 230 PHE A CD2 1 
ATOM   1194 C CE1 . PHE A 1 230 ? 152.196 136.911 189.048 1.00 101.90 ? 230 PHE A CE1 1 
ATOM   1195 C CE2 . PHE A 1 230 ? 151.393 138.580 190.551 1.00 108.86 ? 230 PHE A CE2 1 
ATOM   1196 C CZ  . PHE A 1 230 ? 151.586 138.128 189.263 1.00 105.96 ? 230 PHE A CZ  1 
ATOM   1197 N N   . ARG A 1 231 ? 154.248 132.729 193.091 1.00 116.73 ? 231 ARG A N   1 
ATOM   1198 C CA  . ARG A 1 231 ? 155.096 131.925 193.973 1.00 122.18 ? 231 ARG A CA  1 
ATOM   1199 C C   . ARG A 1 231 ? 156.535 132.332 193.669 1.00 121.43 ? 231 ARG A C   1 
ATOM   1200 O O   . ARG A 1 231 ? 157.115 131.872 192.682 1.00 120.78 ? 231 ARG A O   1 
ATOM   1201 C CB  . ARG A 1 231 ? 154.857 130.433 193.749 1.00 122.47 ? 231 ARG A CB  1 
ATOM   1202 C CG  . ARG A 1 231 ? 155.586 129.469 194.695 1.00 125.92 ? 231 ARG A CG  1 
ATOM   1203 C CD  . ARG A 1 231 ? 157.032 129.215 194.293 1.00 125.98 ? 231 ARG A CD  1 
ATOM   1204 N NE  . ARG A 1 231 ? 157.154 128.890 192.877 1.00 126.26 ? 231 ARG A NE  1 
ATOM   1205 C CZ  . ARG A 1 231 ? 158.270 129.019 192.172 1.00 125.87 ? 231 ARG A CZ  1 
ATOM   1206 N NH1 . ARG A 1 231 ? 159.386 129.471 192.720 1.00 123.93 ? 231 ARG A NH1 1 
ATOM   1207 N NH2 . ARG A 1 231 ? 158.264 128.691 190.883 1.00 124.42 ? 231 ARG A NH2 1 
ATOM   1208 N N   . ASP A 1 232 ? 157.100 133.203 194.506 1.00 120.76 ? 232 ASP A N   1 
ATOM   1209 C CA  . ASP A 1 232 ? 158.433 133.735 194.248 1.00 121.42 ? 232 ASP A CA  1 
ATOM   1210 C C   . ASP A 1 232 ? 159.496 132.642 194.255 1.00 126.65 ? 232 ASP A C   1 
ATOM   1211 O O   . ASP A 1 232 ? 160.076 132.331 193.210 1.00 128.62 ? 232 ASP A O   1 
ATOM   1212 C CB  . ASP A 1 232 ? 158.779 134.813 195.278 1.00 120.19 ? 232 ASP A CB  1 
ATOM   1213 C CG  . ASP A 1 232 ? 158.789 134.282 196.696 1.00 126.15 ? 232 ASP A CG  1 
ATOM   1214 O OD1 . ASP A 1 232 ? 158.454 133.095 196.890 1.00 127.60 ? 232 ASP A OD1 1 
ATOM   1215 O OD2 . ASP A 1 232 ? 159.130 135.053 197.618 1.00 129.66 ? 232 ASP A OD2 1 
ATOM   1216 N N   . GLU A 1 233 ? 159.722 132.001 195.407 1.00 128.80 ? 233 GLU A N   1 
ATOM   1217 C CA  . GLU A 1 233 ? 160.704 130.891 195.521 1.00 133.30 ? 233 GLU A CA  1 
ATOM   1218 C C   . GLU A 1 233 ? 159.974 129.668 196.095 1.00 133.30 ? 233 GLU A C   1 
ATOM   1219 O O   . GLU A 1 233 ? 159.980 128.612 195.425 1.00 135.59 ? 233 GLU A O   1 
ATOM   1220 C CB  . GLU A 1 233 ? 161.865 131.287 196.432 1.00 133.70 ? 233 GLU A CB  1 
ATOM   1221 C CG  . GLU A 1 233 ? 162.485 132.637 196.083 1.00 134.42 ? 233 GLU A CG  1 
ATOM   1222 C CD  . GLU A 1 233 ? 163.078 132.722 194.688 1.00 136.82 ? 233 GLU A CD  1 
ATOM   1223 O OE1 . GLU A 1 233 ? 163.972 131.908 194.377 1.00 138.20 ? 233 GLU A OE1 1 
ATOM   1224 O OE2 . GLU A 1 233 ? 162.655 133.609 193.918 1.00 130.36 ? 233 GLU A OE2 1 
ATOM   1225 N N   . ALA A 1 234 ? 159.315 129.831 197.248 1.00 132.80 ? 234 ALA A N   1 
ATOM   1226 C CA  . ALA A 1 234 ? 158.584 128.706 197.882 1.00 136.61 ? 234 ALA A CA  1 
ATOM   1227 C C   . ALA A 1 234 ? 157.232 129.174 198.429 1.00 136.56 ? 234 ALA A C   1 
ATOM   1228 O O   . ALA A 1 234 ? 156.282 128.361 198.431 1.00 138.82 ? 234 ALA A O   1 
ATOM   1229 C CB  . ALA A 1 234 ? 159.435 128.095 198.974 1.00 138.00 ? 234 ALA A CB  1 
ATOM   1230 N N   . THR A 1 235 ? 157.138 130.431 198.877 1.00 134.13 ? 235 THR A N   1 
ATOM   1231 C CA  . THR A 1 235 ? 155.905 130.913 199.476 1.00 135.14 ? 235 THR A CA  1 
ATOM   1232 C C   . THR A 1 235 ? 154.880 131.247 198.397 1.00 132.98 ? 235 THR A C   1 
ATOM   1233 O O   . THR A 1 235 ? 155.208 131.428 197.222 1.00 132.37 ? 235 THR A O   1 
ATOM   1234 C CB  . THR A 1 235 ? 156.170 132.146 200.340 1.00 135.07 ? 235 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 235 ? 156.606 133.229 199.509 1.00 137.27 ? 235 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 235 ? 157.243 131.849 201.375 1.00 136.67 ? 235 THR A CG2 1 
ATOM   1237 N N   . CYS A 1 236 ? 153.621 131.331 198.815 1.00 135.31 ? 236 CYS A N   1 
ATOM   1238 C CA  . CYS A 1 236 ? 152.516 131.652 197.923 1.00 135.93 ? 236 CYS A CA  1 
ATOM   1239 C C   . CYS A 1 236 ? 152.008 133.052 198.233 1.00 135.96 ? 236 CYS A C   1 
ATOM   1240 O O   . CYS A 1 236 ? 151.710 133.367 199.390 1.00 135.78 ? 236 CYS A O   1 
ATOM   1241 C CB  . CYS A 1 236 ? 151.385 130.631 198.063 1.00 138.89 ? 236 CYS A CB  1 
ATOM   1242 S SG  . CYS A 1 236 ? 149.829 131.146 197.307 1.00 149.14 ? 236 CYS A SG  1 
ATOM   1243 N N   . LYS A 1 237 ? 151.911 133.887 197.200 1.00 137.15 ? 237 LYS A N   1 
ATOM   1244 C CA  . LYS A 1 237 ? 151.459 135.261 197.353 1.00 136.19 ? 237 LYS A CA  1 
ATOM   1245 C C   . LYS A 1 237 ? 150.490 135.610 196.234 1.00 134.41 ? 237 LYS A C   1 
ATOM   1246 O O   . LYS A 1 237 ? 150.613 135.120 195.108 1.00 131.15 ? 237 LYS A O   1 
ATOM   1247 C CB  . LYS A 1 237 ? 152.634 136.249 197.347 1.00 131.91 ? 237 LYS A CB  1 
ATOM   1248 C CG  . LYS A 1 237 ? 153.554 136.135 198.549 1.00 133.95 ? 237 LYS A CG  1 
ATOM   1249 C CD  . LYS A 1 237 ? 154.650 137.186 198.501 1.00 132.54 ? 237 LYS A CD  1 
ATOM   1250 C CE  . LYS A 1 237 ? 155.562 137.086 199.712 1.00 132.62 ? 237 LYS A CE  1 
ATOM   1251 N NZ  . LYS A 1 237 ? 154.815 137.281 200.985 1.00 132.54 ? 237 LYS A NZ  1 
ATOM   1252 N N   . ASP A 1 238 ? 149.519 136.466 196.557 1.00 135.68 ? 238 ASP A N   1 
ATOM   1253 C CA  . ASP A 1 238 ? 148.595 136.958 195.543 1.00 132.55 ? 238 ASP A CA  1 
ATOM   1254 C C   . ASP A 1 238 ? 149.238 138.015 194.656 1.00 134.45 ? 238 ASP A C   1 
ATOM   1255 O O   . ASP A 1 238 ? 148.856 138.157 193.489 1.00 133.24 ? 238 ASP A O   1 
ATOM   1256 C CB  . ASP A 1 238 ? 147.338 137.525 196.204 1.00 130.62 ? 238 ASP A CB  1 
ATOM   1257 C CG  . ASP A 1 238 ? 147.651 138.363 197.427 1.00 132.83 ? 238 ASP A CG  1 
ATOM   1258 O OD1 . ASP A 1 238 ? 148.588 138.005 198.170 1.00 130.99 ? 238 ASP A OD1 1 
ATOM   1259 O OD2 . ASP A 1 238 ? 146.961 139.381 197.644 1.00 132.94 ? 238 ASP A OD2 1 
ATOM   1260 N N   . THR A 1 239 ? 150.201 138.766 195.186 1.00 136.01 ? 239 THR A N   1 
ATOM   1261 C CA  . THR A 1 239 ? 150.903 139.787 194.424 1.00 131.39 ? 239 THR A CA  1 
ATOM   1262 C C   . THR A 1 239 ? 152.374 139.778 194.810 1.00 127.81 ? 239 THR A C   1 
ATOM   1263 O O   . THR A 1 239 ? 152.712 139.687 195.993 1.00 130.11 ? 239 THR A O   1 
ATOM   1264 C CB  . THR A 1 239 ? 150.313 141.183 194.667 1.00 136.50 ? 239 THR A CB  1 
ATOM   1265 O OG1 . THR A 1 239 ? 149.963 141.323 196.049 1.00 141.94 ? 239 THR A OG1 1 
ATOM   1266 C CG2 . THR A 1 239 ? 149.075 141.399 193.808 1.00 137.19 ? 239 THR A CG2 1 
ATOM   1267 N N   . CYS A 1 240 ? 153.241 139.871 193.806 1.00 126.27 ? 240 CYS A N   1 
ATOM   1268 C CA  . CYS A 1 240 ? 154.665 139.977 194.057 1.00 122.65 ? 240 CYS A CA  1 
ATOM   1269 C C   . CYS A 1 240 ? 154.981 141.331 194.687 1.00 118.27 ? 240 CYS A C   1 
ATOM   1270 O O   . CYS A 1 240 ? 154.230 142.294 194.515 1.00 124.35 ? 240 CYS A O   1 
ATOM   1271 C CB  . CYS A 1 240 ? 155.448 139.806 192.759 1.00 116.63 ? 240 CYS A CB  1 
ATOM   1272 S SG  . CYS A 1 240 ? 155.698 138.095 192.240 1.00 116.12 ? 240 CYS A SG  1 
ATOM   1273 N N   . PRO A 1 241 ? 156.075 141.425 195.438 1.00 116.39 ? 241 PRO A N   1 
ATOM   1274 C CA  . PRO A 1 241 ? 156.497 142.725 195.972 1.00 129.66 ? 241 PRO A CA  1 
ATOM   1275 C C   . PRO A 1 241 ? 156.735 143.713 194.845 1.00 136.24 ? 241 PRO A C   1 
ATOM   1276 O O   . PRO A 1 241 ? 157.493 143.426 193.906 1.00 134.51 ? 241 PRO A O   1 
ATOM   1277 C CB  . PRO A 1 241 ? 157.800 142.403 196.722 1.00 128.20 ? 241 PRO A CB  1 
ATOM   1278 C CG  . PRO A 1 241 ? 158.198 141.033 196.270 1.00 121.99 ? 241 PRO A CG  1 
ATOM   1279 C CD  . PRO A 1 241 ? 156.934 140.329 195.911 1.00 118.96 ? 241 PRO A CD  1 
ATOM   1280 N N   . PRO A 1 242 ? 156.100 144.883 194.899 1.00 142.93 ? 242 PRO A N   1 
ATOM   1281 C CA  . PRO A 1 242 ? 156.152 145.805 193.758 1.00 135.54 ? 242 PRO A CA  1 
ATOM   1282 C C   . PRO A 1 242 ? 157.561 146.314 193.498 1.00 132.57 ? 242 PRO A C   1 
ATOM   1283 O O   . PRO A 1 242 ? 158.384 146.433 194.408 1.00 137.53 ? 242 PRO A O   1 
ATOM   1284 C CB  . PRO A 1 242 ? 155.216 146.947 194.178 1.00 133.43 ? 242 PRO A CB  1 
ATOM   1285 C CG  . PRO A 1 242 ? 154.387 146.387 195.296 1.00 138.80 ? 242 PRO A CG  1 
ATOM   1286 C CD  . PRO A 1 242 ? 155.270 145.406 195.995 1.00 142.83 ? 242 PRO A CD  1 
ATOM   1287 N N   . LEU A 1 243 ? 157.831 146.615 192.226 1.00 125.96 ? 243 LEU A N   1 
ATOM   1288 C CA  . LEU A 1 243 ? 159.117 147.171 191.828 1.00 131.77 ? 243 LEU A CA  1 
ATOM   1289 C C   . LEU A 1 243 ? 159.371 148.546 192.429 1.00 140.23 ? 243 LEU A C   1 
ATOM   1290 O O   . LEU A 1 243 ? 160.525 148.988 192.458 1.00 144.36 ? 243 LEU A O   1 
ATOM   1291 C CB  . LEU A 1 243 ? 159.207 147.251 190.300 1.00 129.67 ? 243 LEU A CB  1 
ATOM   1292 C CG  . LEU A 1 243 ? 158.055 147.913 189.536 1.00 121.18 ? 243 LEU A CG  1 
ATOM   1293 C CD1 . LEU A 1 243 ? 158.577 148.614 188.292 1.00 111.18 ? 243 LEU A CD1 1 
ATOM   1294 C CD2 . LEU A 1 243 ? 156.986 146.897 189.154 1.00 102.67 ? 243 LEU A CD2 1 
ATOM   1295 N N   . MET A 1 244 ? 158.331 149.225 192.906 1.00 142.29 ? 244 MET A N   1 
ATOM   1296 C CA  . MET A 1 244 ? 158.461 150.546 193.501 1.00 145.56 ? 244 MET A CA  1 
ATOM   1297 C C   . MET A 1 244 ? 157.586 150.606 194.746 1.00 144.86 ? 244 MET A C   1 
ATOM   1298 O O   . MET A 1 244 ? 156.488 150.043 194.770 1.00 144.31 ? 244 MET A O   1 
ATOM   1299 C CB  . MET A 1 244 ? 158.098 151.634 192.481 1.00 147.88 ? 244 MET A CB  1 
ATOM   1300 C CG  . MET A 1 244 ? 156.659 152.104 192.511 1.00 147.21 ? 244 MET A CG  1 
ATOM   1301 S SD  . MET A 1 244 ? 156.142 152.784 190.922 1.00 149.80 ? 244 MET A SD  1 
ATOM   1302 C CE  . MET A 1 244 ? 157.620 153.670 190.434 1.00 150.96 ? 244 MET A CE  1 
ATOM   1303 N N   . LEU A 1 245 ? 158.093 151.265 195.787 1.00 145.89 ? 245 LEU A N   1 
ATOM   1304 C CA  . LEU A 1 245 ? 157.473 151.240 197.104 1.00 148.66 ? 245 LEU A CA  1 
ATOM   1305 C C   . LEU A 1 245 ? 157.424 152.641 197.693 1.00 154.10 ? 245 LEU A C   1 
ATOM   1306 O O   . LEU A 1 245 ? 158.418 153.372 197.662 1.00 155.22 ? 245 LEU A O   1 
ATOM   1307 C CB  . LEU A 1 245 ? 158.242 150.315 198.052 1.00 146.74 ? 245 LEU A CB  1 
ATOM   1308 C CG  . LEU A 1 245 ? 157.480 149.700 199.223 1.00 150.28 ? 245 LEU A CG  1 
ATOM   1309 C CD1 . LEU A 1 245 ? 156.803 148.412 198.789 1.00 153.33 ? 245 LEU A CD1 1 
ATOM   1310 C CD2 . LEU A 1 245 ? 158.423 149.451 200.386 1.00 148.98 ? 245 LEU A CD2 1 
ATOM   1311 N N   . TYR A 1 246 ? 156.264 152.974 198.271 1.00 155.84 ? 246 TYR A N   1 
ATOM   1312 C CA  . TYR A 1 246 ? 156.084 154.303 198.911 1.00 158.12 ? 246 TYR A CA  1 
ATOM   1313 C C   . TYR A 1 246 ? 157.041 154.428 200.084 1.00 155.33 ? 246 TYR A C   1 
ATOM   1314 O O   . TYR A 1 246 ? 157.185 153.464 200.867 1.00 154.29 ? 246 TYR A O   1 
ATOM   1315 C CB  . TYR A 1 246 ? 154.632 154.474 199.367 1.00 156.97 ? 246 TYR A CB  1 
ATOM   1316 C CG  . TYR A 1 246 ? 154.421 155.557 200.417 1.00 155.07 ? 246 TYR A CG  1 
ATOM   1317 C CD1 . TYR A 1 246 ? 154.559 156.902 200.098 1.00 151.36 ? 246 TYR A CD1 1 
ATOM   1318 C CD2 . TYR A 1 246 ? 154.087 155.234 201.727 1.00 155.24 ? 246 TYR A CD2 1 
ATOM   1319 C CE1 . TYR A 1 246 ? 154.374 157.892 201.048 1.00 151.21 ? 246 TYR A CE1 1 
ATOM   1320 C CE2 . TYR A 1 246 ? 153.896 156.215 202.685 1.00 152.93 ? 246 TYR A CE2 1 
ATOM   1321 C CZ  . TYR A 1 246 ? 154.039 157.548 202.345 1.00 151.50 ? 246 TYR A CZ  1 
ATOM   1322 O OH  . TYR A 1 246 ? 153.852 158.520 203.284 1.00 150.68 ? 246 TYR A OH  1 
ATOM   1323 N N   . ASN A 1 247 ? 157.679 155.589 200.208 1.00 150.84 ? 247 ASN A N   1 
ATOM   1324 C CA  . ASN A 1 247 ? 158.620 155.846 201.298 1.00 150.43 ? 247 ASN A CA  1 
ATOM   1325 C C   . ASN A 1 247 ? 158.110 156.984 202.170 1.00 152.05 ? 247 ASN A C   1 
ATOM   1326 O O   . ASN A 1 247 ? 158.163 158.154 201.747 1.00 154.79 ? 247 ASN A O   1 
ATOM   1327 C CB  . ASN A 1 247 ? 160.006 156.180 200.746 1.00 154.63 ? 247 ASN A CB  1 
ATOM   1328 C CG  . ASN A 1 247 ? 161.107 155.973 201.767 1.00 157.94 ? 247 ASN A CG  1 
ATOM   1329 O OD1 . ASN A 1 247 ? 160.866 156.005 202.974 1.00 159.68 ? 247 ASN A OD1 1 
ATOM   1330 N ND2 . ASN A 1 247 ? 162.326 155.760 201.286 1.00 155.35 ? 247 ASN A ND2 1 
ATOM   1331 N N   . PRO A 1 248 ? 157.609 156.706 203.375 1.00 152.04 ? 248 PRO A N   1 
ATOM   1332 C CA  . PRO A 1 248 ? 157.167 157.800 204.254 1.00 153.87 ? 248 PRO A CA  1 
ATOM   1333 C C   . PRO A 1 248 ? 158.295 158.708 204.712 1.00 153.08 ? 248 PRO A C   1 
ATOM   1334 O O   . PRO A 1 248 ? 158.025 159.846 205.116 1.00 148.07 ? 248 PRO A O   1 
ATOM   1335 C CB  . PRO A 1 248 ? 156.526 157.061 205.435 1.00 154.21 ? 248 PRO A CB  1 
ATOM   1336 C CG  . PRO A 1 248 ? 157.222 155.741 205.465 1.00 155.28 ? 248 PRO A CG  1 
ATOM   1337 C CD  . PRO A 1 248 ? 157.503 155.390 204.028 1.00 150.95 ? 248 PRO A CD  1 
ATOM   1338 N N   . THR A 1 249 ? 159.546 158.242 204.673 1.00 157.58 ? 249 THR A N   1 
ATOM   1339 C CA  . THR A 1 249 ? 160.664 159.079 205.099 1.00 160.47 ? 249 THR A CA  1 
ATOM   1340 C C   . THR A 1 249 ? 160.836 160.285 204.183 1.00 157.87 ? 249 THR A C   1 
ATOM   1341 O O   . THR A 1 249 ? 161.090 161.399 204.656 1.00 155.98 ? 249 THR A O   1 
ATOM   1342 C CB  . THR A 1 249 ? 161.952 158.258 205.145 1.00 163.80 ? 249 THR A CB  1 
ATOM   1343 O OG1 . THR A 1 249 ? 161.679 156.968 205.706 1.00 164.02 ? 249 THR A OG1 1 
ATOM   1344 C CG2 . THR A 1 249 ? 163.002 158.962 205.991 1.00 161.91 ? 249 THR A CG2 1 
ATOM   1345 N N   . THR A 1 250 ? 160.703 160.085 202.875 1.00 157.08 ? 250 THR A N   1 
ATOM   1346 C CA  . THR A 1 250 ? 160.828 161.163 201.904 1.00 154.45 ? 250 THR A CA  1 
ATOM   1347 C C   . THR A 1 250 ? 159.493 161.813 201.570 1.00 148.65 ? 250 THR A C   1 
ATOM   1348 O O   . THR A 1 250 ? 159.449 162.686 200.697 1.00 143.86 ? 250 THR A O   1 
ATOM   1349 C CB  . THR A 1 250 ? 161.479 160.646 200.617 1.00 153.37 ? 250 THR A CB  1 
ATOM   1350 O OG1 . THR A 1 250 ? 160.471 160.111 199.750 1.00 151.51 ? 250 THR A OG1 1 
ATOM   1351 C CG2 . THR A 1 250 ? 162.498 159.562 200.935 1.00 154.39 ? 250 THR A CG2 1 
ATOM   1352 N N   . TYR A 1 251 ? 158.412 161.403 202.237 1.00 148.20 ? 251 TYR A N   1 
ATOM   1353 C CA  . TYR A 1 251 ? 157.073 161.951 202.015 1.00 146.05 ? 251 TYR A CA  1 
ATOM   1354 C C   . TYR A 1 251 ? 156.638 161.797 200.560 1.00 144.66 ? 251 TYR A C   1 
ATOM   1355 O O   . TYR A 1 251 ? 155.853 162.598 200.047 1.00 144.73 ? 251 TYR A O   1 
ATOM   1356 C CB  . TYR A 1 251 ? 156.981 163.422 202.441 1.00 145.43 ? 251 TYR A CB  1 
ATOM   1357 C CG  . TYR A 1 251 ? 157.364 163.700 203.882 1.00 153.54 ? 251 TYR A CG  1 
ATOM   1358 C CD1 . TYR A 1 251 ? 158.685 163.603 204.307 1.00 158.73 ? 251 TYR A CD1 1 
ATOM   1359 C CD2 . TYR A 1 251 ? 156.403 164.054 204.818 1.00 153.55 ? 251 TYR A CD2 1 
ATOM   1360 C CE1 . TYR A 1 251 ? 159.035 163.856 205.619 1.00 161.07 ? 251 TYR A CE1 1 
ATOM   1361 C CE2 . TYR A 1 251 ? 156.744 164.310 206.133 1.00 159.56 ? 251 TYR A CE2 1 
ATOM   1362 C CZ  . TYR A 1 251 ? 158.061 164.209 206.527 1.00 161.74 ? 251 TYR A CZ  1 
ATOM   1363 O OH  . TYR A 1 251 ? 158.404 164.461 207.835 1.00 159.00 ? 251 TYR A OH  1 
ATOM   1364 N N   . GLN A 1 252 ? 157.141 160.764 199.889 1.00 146.94 ? 252 GLN A N   1 
ATOM   1365 C CA  . GLN A 1 252 ? 156.851 160.547 198.481 1.00 148.80 ? 252 GLN A CA  1 
ATOM   1366 C C   . GLN A 1 252 ? 156.783 159.054 198.209 1.00 152.00 ? 252 GLN A C   1 
ATOM   1367 O O   . GLN A 1 252 ? 157.308 158.237 198.969 1.00 152.74 ? 252 GLN A O   1 
ATOM   1368 C CB  . GLN A 1 252 ? 157.906 161.198 197.576 1.00 145.79 ? 252 GLN A CB  1 
ATOM   1369 C CG  . GLN A 1 252 ? 157.777 162.704 197.440 1.00 143.53 ? 252 GLN A CG  1 
ATOM   1370 C CD  . GLN A 1 252 ? 157.829 163.163 195.997 1.00 140.06 ? 252 GLN A CD  1 
ATOM   1371 O OE1 . GLN A 1 252 ? 156.807 163.518 195.410 1.00 133.57 ? 252 GLN A OE1 1 
ATOM   1372 N NE2 . GLN A 1 252 ? 159.023 163.157 195.417 1.00 140.57 ? 252 GLN A NE2 1 
ATOM   1373 N N   . MET A 1 253 ? 156.124 158.708 197.107 1.00 153.49 ? 253 MET A N   1 
ATOM   1374 C CA  . MET A 1 253 ? 156.052 157.325 196.649 1.00 154.73 ? 253 MET A CA  1 
ATOM   1375 C C   . MET A 1 253 ? 157.328 157.040 195.865 1.00 154.40 ? 253 MET A C   1 
ATOM   1376 O O   . MET A 1 253 ? 157.516 157.553 194.757 1.00 153.58 ? 253 MET A O   1 
ATOM   1377 C CB  . MET A 1 253 ? 154.783 157.123 195.820 1.00 153.69 ? 253 MET A CB  1 
ATOM   1378 C CG  . MET A 1 253 ? 154.390 155.680 195.482 1.00 152.89 ? 253 MET A CG  1 
ATOM   1379 S SD  . MET A 1 253 ? 155.602 154.645 194.649 1.00 159.13 ? 253 MET A SD  1 
ATOM   1380 C CE  . MET A 1 253 ? 155.800 155.552 193.116 1.00 155.94 ? 253 MET A CE  1 
ATOM   1381 N N   . ASP A 1 254 ? 158.221 156.250 196.455 1.00 152.51 ? 254 ASP A N   1 
ATOM   1382 C CA  . ASP A 1 254 ? 159.562 156.036 195.937 1.00 152.13 ? 254 ASP A CA  1 
ATOM   1383 C C   . ASP A 1 254 ? 159.671 154.673 195.253 1.00 152.69 ? 254 ASP A C   1 
ATOM   1384 O O   . ASP A 1 254 ? 158.675 153.982 195.018 1.00 151.19 ? 254 ASP A O   1 
ATOM   1385 C CB  . ASP A 1 254 ? 160.582 156.179 197.069 1.00 151.39 ? 254 ASP A CB  1 
ATOM   1386 C CG  . ASP A 1 254 ? 160.673 157.597 197.594 1.00 152.62 ? 254 ASP A CG  1 
ATOM   1387 O OD1 . ASP A 1 254 ? 159.707 158.365 197.407 1.00 152.69 ? 254 ASP A OD1 1 
ATOM   1388 O OD2 . ASP A 1 254 ? 161.711 157.944 198.193 1.00 153.81 ? 254 ASP A OD2 1 
ATOM   1389 N N   . VAL A 1 255 ? 160.900 154.289 194.909 1.00 156.43 ? 255 VAL A N   1 
ATOM   1390 C CA  . VAL A 1 255 ? 161.183 152.977 194.339 1.00 156.89 ? 255 VAL A CA  1 
ATOM   1391 C C   . VAL A 1 255 ? 161.370 151.976 195.473 1.00 155.08 ? 255 VAL A C   1 
ATOM   1392 O O   . VAL A 1 255 ? 161.557 152.363 196.632 1.00 155.03 ? 255 VAL A O   1 
ATOM   1393 C CB  . VAL A 1 255 ? 162.421 153.024 193.423 1.00 157.21 ? 255 VAL A CB  1 
ATOM   1394 C CG1 . VAL A 1 255 ? 163.697 152.834 194.232 1.00 151.18 ? 255 VAL A CG1 1 
ATOM   1395 C CG2 . VAL A 1 255 ? 162.314 151.980 192.319 1.00 154.37 ? 255 VAL A CG2 1 
ATOM   1396 N N   . ASN A 1 256 ? 161.314 150.683 195.149 1.00 151.97 ? 256 ASN A N   1 
ATOM   1397 C CA  . ASN A 1 256 ? 161.451 149.634 196.148 1.00 150.12 ? 256 ASN A CA  1 
ATOM   1398 C C   . ASN A 1 256 ? 162.858 149.066 196.105 1.00 150.62 ? 256 ASN A C   1 
ATOM   1399 O O   . ASN A 1 256 ? 163.262 148.526 195.063 1.00 148.40 ? 256 ASN A O   1 
ATOM   1400 C CB  . ASN A 1 256 ? 160.431 148.527 195.906 1.00 148.86 ? 256 ASN A CB  1 
ATOM   1401 C CG  . ASN A 1 256 ? 160.406 147.501 197.025 1.00 146.90 ? 256 ASN A CG  1 
ATOM   1402 O OD1 . ASN A 1 256 ? 160.933 147.737 198.112 1.00 144.36 ? 256 ASN A OD1 1 
ATOM   1403 N ND2 . ASN A 1 256 ? 159.788 146.356 196.763 1.00 141.33 ? 256 ASN A ND2 1 
ATOM   1404 N N   . PRO A 1 257 ? 163.639 149.169 197.185 1.00 149.28 ? 257 PRO A N   1 
ATOM   1405 C CA  . PRO A 1 257 ? 164.947 148.492 197.198 1.00 150.24 ? 257 PRO A CA  1 
ATOM   1406 C C   . PRO A 1 257 ? 164.833 146.989 197.016 1.00 148.95 ? 257 PRO A C   1 
ATOM   1407 O O   . PRO A 1 257 ? 165.717 146.367 196.415 1.00 146.05 ? 257 PRO A O   1 
ATOM   1408 C CB  . PRO A 1 257 ? 165.521 148.862 198.575 1.00 147.91 ? 257 PRO A CB  1 
ATOM   1409 C CG  . PRO A 1 257 ? 164.748 150.071 199.009 1.00 144.02 ? 257 PRO A CG  1 
ATOM   1410 C CD  . PRO A 1 257 ? 163.378 149.902 198.435 1.00 146.16 ? 257 PRO A CD  1 
ATOM   1411 N N   . GLU A 1 258 ? 163.755 146.388 197.525 1.00 148.24 ? 258 GLU A N   1 
ATOM   1412 C CA  . GLU A 1 258 ? 163.472 144.971 197.344 1.00 143.78 ? 258 GLU A CA  1 
ATOM   1413 C C   . GLU A 1 258 ? 162.528 144.724 196.167 1.00 140.41 ? 258 GLU A C   1 
ATOM   1414 O O   . GLU A 1 258 ? 161.850 143.690 196.110 1.00 136.65 ? 258 GLU A O   1 
ATOM   1415 C CB  . GLU A 1 258 ? 162.919 144.396 198.655 1.00 142.33 ? 258 GLU A CB  1 
ATOM   1416 C CG  . GLU A 1 258 ? 162.886 142.870 198.782 1.00 136.70 ? 258 GLU A CG  1 
ATOM   1417 C CD  . GLU A 1 258 ? 161.487 142.290 198.665 1.00 135.45 ? 258 GLU A CD  1 
ATOM   1418 O OE1 . GLU A 1 258 ? 160.537 143.061 198.416 1.00 141.66 ? 258 GLU A OE1 1 
ATOM   1419 O OE2 . GLU A 1 258 ? 161.337 141.061 198.826 1.00 129.65 ? 258 GLU A OE2 1 
ATOM   1420 N N   . GLY A 1 259 ? 162.482 145.653 195.211 1.00 141.05 ? 259 GLY A N   1 
ATOM   1421 C CA  . GLY A 1 259 ? 161.601 145.547 194.063 1.00 135.89 ? 259 GLY A CA  1 
ATOM   1422 C C   . GLY A 1 259 ? 161.773 144.257 193.291 1.00 127.90 ? 259 GLY A C   1 
ATOM   1423 O O   . GLY A 1 259 ? 162.897 143.860 192.968 1.00 127.45 ? 259 GLY A O   1 
ATOM   1424 N N   . LYS A 1 260 ? 160.657 143.570 193.016 1.00 122.45 ? 260 LYS A N   1 
ATOM   1425 C CA  . LYS A 1 260 ? 160.692 142.258 192.322 1.00 118.67 ? 260 LYS A CA  1 
ATOM   1426 C C   . LYS A 1 260 ? 159.701 142.266 191.153 1.00 113.93 ? 260 LYS A C   1 
ATOM   1427 O O   . LYS A 1 260 ? 158.492 142.469 191.402 1.00 113.94 ? 260 LYS A O   1 
ATOM   1428 C CB  . LYS A 1 260 ? 160.346 141.174 193.345 1.00 119.77 ? 260 LYS A CB  1 
ATOM   1429 C CG  . LYS A 1 260 ? 161.359 140.051 193.442 1.00 112.70 ? 260 LYS A CG  1 
ATOM   1430 C CD  . LYS A 1 260 ? 161.600 139.523 194.849 1.00 114.41 ? 260 LYS A CD  1 
ATOM   1431 C CE  . LYS A 1 260 ? 162.126 140.561 195.789 1.00 125.43 ? 260 LYS A CE  1 
ATOM   1432 N NZ  . LYS A 1 260 ? 163.231 141.346 195.230 1.00 127.69 ? 260 LYS A NZ  1 
ATOM   1433 N N   . TYR A 1 261 ? 160.179 141.996 189.930 1.00 108.50 ? 261 TYR A N   1 
ATOM   1434 C CA  . TYR A 1 261 ? 159.313 141.950 188.719 1.00 100.40 ? 261 TYR A CA  1 
ATOM   1435 C C   . TYR A 1 261 ? 158.498 140.662 188.752 1.00 104.92 ? 261 TYR A C   1 
ATOM   1436 O O   . TYR A 1 261 ? 159.023 139.590 188.959 1.00 111.37 ? 261 TYR A O   1 
ATOM   1437 C CB  . TYR A 1 261 ? 160.148 142.057 187.439 1.00 96.24  ? 261 TYR A CB  1 
ATOM   1438 C CG  . TYR A 1 261 ? 161.055 143.277 187.387 1.00 106.21 ? 261 TYR A CG  1 
ATOM   1439 C CD1 . TYR A 1 261 ? 160.584 144.503 186.937 1.00 109.36 ? 261 TYR A CD1 1 
ATOM   1440 C CD2 . TYR A 1 261 ? 162.384 143.199 187.782 1.00 112.27 ? 261 TYR A CD2 1 
ATOM   1441 C CE1 . TYR A 1 261 ? 161.405 145.617 186.891 1.00 107.36 ? 261 TYR A CE1 1 
ATOM   1442 C CE2 . TYR A 1 261 ? 163.217 144.304 187.736 1.00 113.17 ? 261 TYR A CE2 1 
ATOM   1443 C CZ  . TYR A 1 261 ? 162.726 145.516 187.287 1.00 107.83 ? 261 TYR A CZ  1 
ATOM   1444 O OH  . TYR A 1 261 ? 163.535 146.613 187.235 1.00 105.40 ? 261 TYR A OH  1 
ATOM   1445 N N   . SER A 1 262 ? 157.208 140.732 188.486 1.00 103.64 ? 262 SER A N   1 
ATOM   1446 C CA  . SER A 1 262 ? 156.314 139.579 188.588 1.00 94.50  ? 262 SER A CA  1 
ATOM   1447 C C   . SER A 1 262 ? 156.332 138.803 187.274 1.00 86.04  ? 262 SER A C   1 
ATOM   1448 O O   . SER A 1 262 ? 155.428 138.904 186.446 1.00 90.21  ? 262 SER A O   1 
ATOM   1449 C CB  . SER A 1 262 ? 154.905 140.039 188.947 1.00 92.18  ? 262 SER A CB  1 
ATOM   1450 O OG  . SER A 1 262 ? 154.939 141.067 189.920 1.00 80.57  ? 262 SER A OG  1 
ATOM   1451 N N   . PHE A 1 263 ? 157.373 137.982 187.082 1.00 81.89  ? 263 PHE A N   1 
ATOM   1452 C CA  . PHE A 1 263 ? 157.549 137.213 185.817 1.00 93.54  ? 263 PHE A CA  1 
ATOM   1453 C C   . PHE A 1 263 ? 156.827 135.871 185.916 1.00 98.12  ? 263 PHE A C   1 
ATOM   1454 O O   . PHE A 1 263 ? 157.370 134.972 186.583 1.00 100.92 ? 263 PHE A O   1 
ATOM   1455 C CB  . PHE A 1 263 ? 159.056 137.088 185.581 1.00 101.85 ? 263 PHE A CB  1 
ATOM   1456 C CG  . PHE A 1 263 ? 159.452 136.304 184.338 1.00 112.93 ? 263 PHE A CG  1 
ATOM   1457 C CD1 . PHE A 1 263 ? 158.648 136.296 183.203 1.00 104.71 ? 263 PHE A CD1 1 
ATOM   1458 C CD2 . PHE A 1 263 ? 160.632 135.573 184.313 1.00 116.40 ? 263 PHE A CD2 1 
ATOM   1459 C CE1 . PHE A 1 263 ? 159.020 135.578 182.078 1.00 105.58 ? 263 PHE A CE1 1 
ATOM   1460 C CE2 . PHE A 1 263 ? 160.996 134.857 183.185 1.00 118.33 ? 263 PHE A CE2 1 
ATOM   1461 C CZ  . PHE A 1 263 ? 160.192 134.861 182.071 1.00 112.18 ? 263 PHE A CZ  1 
ATOM   1462 N N   . GLY A 1 264 ? 155.693 135.704 185.227 1.00 98.68  ? 264 GLY A N   1 
ATOM   1463 C CA  . GLY A 1 264 ? 154.879 134.506 185.284 1.00 91.69  ? 264 GLY A CA  1 
ATOM   1464 C C   . GLY A 1 264 ? 154.169 134.330 186.607 1.00 91.95  ? 264 GLY A C   1 
ATOM   1465 O O   . GLY A 1 264 ? 153.190 135.022 186.897 1.00 91.07  ? 264 GLY A O   1 
ATOM   1466 N N   . ALA A 1 265 ? 154.652 133.386 187.413 1.00 94.00  ? 265 ALA A N   1 
ATOM   1467 C CA  . ALA A 1 265 ? 154.153 133.185 188.765 1.00 96.17  ? 265 ALA A CA  1 
ATOM   1468 C C   . ALA A 1 265 ? 155.248 133.333 189.812 1.00 95.37  ? 265 ALA A C   1 
ATOM   1469 O O   . ALA A 1 265 ? 155.037 132.957 190.969 1.00 100.28 ? 265 ALA A O   1 
ATOM   1470 C CB  . ALA A 1 265 ? 153.489 131.811 188.891 1.00 102.55 ? 265 ALA A CB  1 
ATOM   1471 N N   . THR A 1 266 ? 156.410 133.873 189.428 1.00 91.74  ? 266 THR A N   1 
ATOM   1472 C CA  . THR A 1 266 ? 157.576 133.997 190.334 1.00 100.75 ? 266 THR A CA  1 
ATOM   1473 C C   . THR A 1 266 ? 158.113 135.409 190.325 1.00 104.46 ? 266 THR A C   1 
ATOM   1474 O O   . THR A 1 266 ? 158.378 135.937 189.224 1.00 107.15 ? 266 THR A O   1 
ATOM   1475 C CB  . THR A 1 266 ? 158.653 132.985 189.936 1.00 104.99 ? 266 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 266 ? 159.827 133.413 190.618 1.00 113.84 ? 266 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 266 ? 158.932 132.944 188.444 1.00 96.97  ? 266 THR A CG2 1 
ATOM   1478 N N   . CYS A 1 267 ? 158.260 136.015 191.503 1.00 105.74 ? 267 CYS A N   1 
ATOM   1479 C CA  . CYS A 1 267 ? 158.857 137.365 191.642 1.00 104.29 ? 267 CYS A CA  1 
ATOM   1480 C C   . CYS A 1 267 ? 160.358 137.253 191.346 1.00 107.97 ? 267 CYS A C   1 
ATOM   1481 O O   . CYS A 1 267 ? 160.965 136.260 191.805 1.00 111.84 ? 267 CYS A O   1 
ATOM   1482 C CB  . CYS A 1 267 ? 158.584 137.903 193.039 1.00 108.55 ? 267 CYS A CB  1 
ATOM   1483 S SG  . CYS A 1 267 ? 156.961 137.396 193.662 1.00 110.09 ? 267 CYS A SG  1 
ATOM   1484 N N   . VAL A 1 268 ? 160.927 138.211 190.612 1.00 108.85 ? 268 VAL A N   1 
ATOM   1485 C CA  . VAL A 1 268 ? 162.369 138.187 190.222 1.00 113.89 ? 268 VAL A CA  1 
ATOM   1486 C C   . VAL A 1 268 ? 162.994 139.544 190.582 1.00 115.82 ? 268 VAL A C   1 
ATOM   1487 O O   . VAL A 1 268 ? 162.546 140.567 190.028 1.00 116.47 ? 268 VAL A O   1 
ATOM   1488 C CB  . VAL A 1 268 ? 162.516 137.853 188.724 1.00 114.81 ? 268 VAL A CB  1 
ATOM   1489 C CG1 . VAL A 1 268 ? 161.981 136.464 188.399 1.00 108.95 ? 268 VAL A CG1 1 
ATOM   1490 C CG2 . VAL A 1 268 ? 161.845 138.885 187.825 1.00 112.74 ? 268 VAL A CG2 1 
ATOM   1491 N N   . LYS A 1 269 ? 163.978 139.558 191.486 1.00 117.48 ? 269 LYS A N   1 
ATOM   1492 C CA  . LYS A 1 269 ? 164.657 140.817 191.888 1.00 121.71 ? 269 LYS A CA  1 
ATOM   1493 C C   . LYS A 1 269 ? 164.940 141.615 190.611 1.00 124.30 ? 269 LYS A C   1 
ATOM   1494 O O   . LYS A 1 269 ? 164.619 142.824 190.594 1.00 124.59 ? 269 LYS A O   1 
ATOM   1495 C CB  . LYS A 1 269 ? 165.936 140.492 192.667 1.00 121.87 ? 269 LYS A CB  1 
ATOM   1496 C CG  . LYS A 1 269 ? 166.855 141.672 192.948 1.00 125.34 ? 269 LYS A CG  1 
ATOM   1497 C CD  . LYS A 1 269 ? 166.320 142.656 193.980 1.00 128.93 ? 269 LYS A CD  1 
ATOM   1498 C CE  . LYS A 1 269 ? 166.523 142.172 195.376 1.00 129.35 ? 269 LYS A CE  1 
ATOM   1499 N NZ  . LYS A 1 269 ? 166.447 143.290 196.316 1.00 133.30 ? 269 LYS A NZ  1 
ATOM   1500 N N   . LYS A 1 270 ? 165.514 140.967 189.593 1.00 120.78 ? 270 LYS A N   1 
ATOM   1501 C CA  . LYS A 1 270 ? 165.780 141.608 188.279 1.00 118.47 ? 270 LYS A CA  1 
ATOM   1502 C C   . LYS A 1 270 ? 165.049 140.776 187.218 1.00 110.30 ? 270 LYS A C   1 
ATOM   1503 O O   . LYS A 1 270 ? 165.077 139.534 187.335 1.00 113.76 ? 270 LYS A O   1 
ATOM   1504 C CB  . LYS A 1 270 ? 167.286 141.701 188.010 1.00 120.64 ? 270 LYS A CB  1 
ATOM   1505 C CG  . LYS A 1 270 ? 168.016 140.368 187.919 1.00 122.94 ? 270 LYS A CG  1 
ATOM   1506 C CD  . LYS A 1 270 ? 168.132 139.815 186.505 1.00 127.68 ? 270 LYS A CD  1 
ATOM   1507 C CE  . LYS A 1 270 ? 168.057 138.326 186.487 1.00 127.96 ? 270 LYS A CE  1 
ATOM   1508 N NZ  . LYS A 1 270 ? 168.557 137.785 185.222 1.00 122.36 ? 270 LYS A NZ  1 
ATOM   1509 N N   . CYS A 1 271 ? 164.413 141.416 186.230 1.00 102.40 ? 271 CYS A N   1 
ATOM   1510 C CA  . CYS A 1 271 ? 163.630 140.710 185.179 1.00 114.87 ? 271 CYS A CA  1 
ATOM   1511 C C   . CYS A 1 271 ? 164.580 139.821 184.359 1.00 116.99 ? 271 CYS A C   1 
ATOM   1512 O O   . CYS A 1 271 ? 165.431 140.389 183.639 1.00 113.58 ? 271 CYS A O   1 
ATOM   1513 C CB  . CYS A 1 271 ? 162.885 141.704 184.294 1.00 121.73 ? 271 CYS A CB  1 
ATOM   1514 S SG  . CYS A 1 271 ? 161.917 140.916 182.980 1.00 128.80 ? 271 CYS A SG  1 
ATOM   1515 N N   . PRO A 1 272 ? 164.487 138.471 184.426 1.00 123.11 ? 272 PRO A N   1 
ATOM   1516 C CA  . PRO A 1 272 ? 165.422 137.596 183.730 1.00 127.50 ? 272 PRO A CA  1 
ATOM   1517 C C   . PRO A 1 272 ? 164.973 137.148 182.353 1.00 129.10 ? 272 PRO A C   1 
ATOM   1518 O O   . PRO A 1 272 ? 163.903 137.606 181.907 1.00 121.81 ? 272 PRO A O   1 
ATOM   1519 C CB  . PRO A 1 272 ? 165.445 136.428 184.718 1.00 130.74 ? 272 PRO A CB  1 
ATOM   1520 C CG  . PRO A 1 272 ? 163.991 136.268 185.076 1.00 126.95 ? 272 PRO A CG  1 
ATOM   1521 C CD  . PRO A 1 272 ? 163.498 137.703 185.169 1.00 123.57 ? 272 PRO A CD  1 
ATOM   1522 N N   . ARG A 1 273 ? 165.736 136.262 181.705 1.00 132.03 ? 273 ARG A N   1 
ATOM   1523 C CA  . ARG A 1 273 ? 165.416 135.750 180.371 1.00 129.15 ? 273 ARG A CA  1 
ATOM   1524 C C   . ARG A 1 273 ? 165.305 136.878 179.349 1.00 126.74 ? 273 ARG A C   1 
ATOM   1525 O O   . ARG A 1 273 ? 164.436 136.860 178.476 1.00 121.08 ? 273 ARG A O   1 
ATOM   1526 C CB  . ARG A 1 273 ? 164.137 134.909 180.392 1.00 127.94 ? 273 ARG A CB  1 
ATOM   1527 C CG  . ARG A 1 273 ? 164.026 133.967 181.583 1.00 124.95 ? 273 ARG A CG  1 
ATOM   1528 C CD  . ARG A 1 273 ? 163.157 132.762 181.259 1.00 124.22 ? 273 ARG A CD  1 
ATOM   1529 N NE  . ARG A 1 273 ? 163.666 132.007 180.121 1.00 125.44 ? 273 ARG A NE  1 
ATOM   1530 C CZ  . ARG A 1 273 ? 164.160 130.778 180.198 1.00 117.55 ? 273 ARG A CZ  1 
ATOM   1531 N NH1 . ARG A 1 273 ? 164.229 130.133 181.351 1.00 111.00 ? 273 ARG A NH1 1 
ATOM   1532 N NH2 . ARG A 1 273 ? 164.594 130.183 179.091 1.00 114.54 ? 273 ARG A NH2 1 
ATOM   1533 N N   . ASN A 1 274 ? 166.192 137.872 179.475 1.00 128.15 ? 274 ASN A N   1 
ATOM   1534 C CA  . ASN A 1 274 ? 166.283 139.022 178.563 1.00 130.01 ? 274 ASN A CA  1 
ATOM   1535 C C   . ASN A 1 274 ? 164.913 139.624 178.252 1.00 128.96 ? 274 ASN A C   1 
ATOM   1536 O O   . ASN A 1 274 ? 164.693 140.185 177.177 1.00 127.90 ? 274 ASN A O   1 
ATOM   1537 C CB  . ASN A 1 274 ? 167.028 138.660 177.269 1.00 132.16 ? 274 ASN A CB  1 
ATOM   1538 C CG  . ASN A 1 274 ? 166.320 137.597 176.450 1.00 131.14 ? 274 ASN A CG  1 
ATOM   1539 O OD1 . ASN A 1 274 ? 165.365 137.884 175.728 1.00 127.80 ? 274 ASN A OD1 1 
ATOM   1540 N ND2 . ASN A 1 274 ? 166.788 136.360 176.559 1.00 130.97 ? 274 ASN A ND2 1 
ATOM   1541 N N   . TYR A 1 275 ? 163.979 139.543 179.207 1.00 128.28 ? 275 TYR A N   1 
ATOM   1542 C CA  . TYR A 1 275 ? 162.610 140.101 179.022 1.00 122.11 ? 275 TYR A CA  1 
ATOM   1543 C C   . TYR A 1 275 ? 162.633 141.580 179.399 1.00 113.76 ? 275 TYR A C   1 
ATOM   1544 O O   . TYR A 1 275 ? 163.640 142.019 179.999 1.00 114.23 ? 275 TYR A O   1 
ATOM   1545 C CB  . TYR A 1 275 ? 161.587 139.334 179.863 1.00 118.62 ? 275 TYR A CB  1 
ATOM   1546 C CG  . TYR A 1 275 ? 160.855 138.199 179.158 1.00 123.17 ? 275 TYR A CG  1 
ATOM   1547 C CD1 . TYR A 1 275 ? 161.437 137.491 178.115 1.00 122.27 ? 275 TYR A CD1 1 
ATOM   1548 C CD2 . TYR A 1 275 ? 159.574 137.832 179.547 1.00 118.09 ? 275 TYR A CD2 1 
ATOM   1549 C CE1 . TYR A 1 275 ? 160.768 136.460 177.479 1.00 115.52 ? 275 TYR A CE1 1 
ATOM   1550 C CE2 . TYR A 1 275 ? 158.891 136.805 178.918 1.00 106.00 ? 275 TYR A CE2 1 
ATOM   1551 C CZ  . TYR A 1 275 ? 159.491 136.117 177.881 1.00 104.50 ? 275 TYR A CZ  1 
ATOM   1552 O OH  . TYR A 1 275 ? 158.829 135.103 177.253 1.00 95.50  ? 275 TYR A OH  1 
ATOM   1553 N N   . VAL A 1 276 ? 161.568 142.322 179.078 1.00 105.67 ? 276 VAL A N   1 
ATOM   1554 C CA  . VAL A 1 276 ? 161.501 143.790 179.356 1.00 102.33 ? 276 VAL A CA  1 
ATOM   1555 C C   . VAL A 1 276 ? 160.652 144.015 180.617 1.00 98.94  ? 276 VAL A C   1 
ATOM   1556 O O   . VAL A 1 276 ? 160.118 143.017 181.142 1.00 105.62 ? 276 VAL A O   1 
ATOM   1557 C CB  . VAL A 1 276 ? 160.940 144.591 178.164 1.00 104.10 ? 276 VAL A CB  1 
ATOM   1558 C CG1 . VAL A 1 276 ? 161.511 144.110 176.836 1.00 110.66 ? 276 VAL A CG1 1 
ATOM   1559 C CG2 . VAL A 1 276 ? 159.415 144.584 178.128 1.00 103.17 ? 276 VAL A CG2 1 
ATOM   1560 N N   . VAL A 1 277 ? 160.537 145.265 181.079 1.00 87.07  ? 277 VAL A N   1 
ATOM   1561 C CA  . VAL A 1 277 ? 159.710 145.614 182.275 1.00 79.23  ? 277 VAL A CA  1 
ATOM   1562 C C   . VAL A 1 277 ? 158.379 146.193 181.772 1.00 84.61  ? 277 VAL A C   1 
ATOM   1563 O O   . VAL A 1 277 ? 158.341 147.409 181.489 1.00 90.50  ? 277 VAL A O   1 
ATOM   1564 C CB  . VAL A 1 277 ? 160.442 146.598 183.206 1.00 76.79  ? 277 VAL A CB  1 
ATOM   1565 C CG1 . VAL A 1 277 ? 159.585 146.983 184.406 1.00 81.06  ? 277 VAL A CG1 1 
ATOM   1566 C CG2 . VAL A 1 277 ? 161.791 146.055 183.658 1.00 80.18  ? 277 VAL A CG2 1 
ATOM   1567 N N   . THR A 1 278 ? 157.325 145.378 181.687 1.00 88.98  ? 278 THR A N   1 
ATOM   1568 C CA  . THR A 1 278 ? 156.006 145.798 181.160 1.00 92.25  ? 278 THR A CA  1 
ATOM   1569 C C   . THR A 1 278 ? 155.352 146.787 182.105 1.00 86.07  ? 278 THR A C   1 
ATOM   1570 O O   . THR A 1 278 ? 155.791 146.853 183.274 1.00 83.00  ? 278 THR A O   1 
ATOM   1571 C CB  . THR A 1 278 ? 155.160 144.542 180.967 1.00 94.52  ? 278 THR A CB  1 
ATOM   1572 O OG1 . THR A 1 278 ? 156.035 143.646 180.291 1.00 87.23  ? 278 THR A OG1 1 
ATOM   1573 C CG2 . THR A 1 278 ? 153.907 144.785 180.146 1.00 95.61  ? 278 THR A CG2 1 
ATOM   1574 N N   . ASP A 1 279 ? 154.337 147.529 181.643 1.00 92.26  ? 279 ASP A N   1 
ATOM   1575 C CA  . ASP A 1 279 ? 153.611 148.492 182.466 1.00 99.86  ? 279 ASP A CA  1 
ATOM   1576 C C   . ASP A 1 279 ? 153.026 147.829 183.706 1.00 103.15 ? 279 ASP A C   1 
ATOM   1577 O O   . ASP A 1 279 ? 153.093 148.387 184.807 1.00 111.18 ? 279 ASP A O   1 
ATOM   1578 C CB  . ASP A 1 279 ? 152.510 149.157 181.641 1.00 100.18 ? 279 ASP A CB  1 
ATOM   1579 C CG  . ASP A 1 279 ? 153.058 149.973 180.486 1.00 98.97  ? 279 ASP A CG  1 
ATOM   1580 O OD1 . ASP A 1 279 ? 154.141 149.624 179.970 1.00 94.72  ? 279 ASP A OD1 1 
ATOM   1581 O OD2 . ASP A 1 279 ? 152.406 150.962 180.094 1.00 105.74 ? 279 ASP A OD2 1 
ATOM   1582 N N   . HIS A 1 280 ? 152.445 146.638 183.547 1.00 96.18  ? 280 HIS A N   1 
ATOM   1583 C CA  . HIS A 1 280 ? 151.910 145.909 184.691 1.00 99.28  ? 280 HIS A CA  1 
ATOM   1584 C C   . HIS A 1 280 ? 153.011 145.419 185.623 1.00 99.50  ? 280 HIS A C   1 
ATOM   1585 O O   . HIS A 1 280 ? 152.746 145.180 186.806 1.00 103.24 ? 280 HIS A O   1 
ATOM   1586 C CB  . HIS A 1 280 ? 151.057 144.732 184.203 1.00 97.56  ? 280 HIS A CB  1 
ATOM   1587 C CG  . HIS A 1 280 ? 150.709 143.742 185.272 1.00 107.60 ? 280 HIS A CG  1 
ATOM   1588 N ND1 . HIS A 1 280 ? 151.593 142.783 185.719 1.00 102.90 ? 280 HIS A ND1 1 
ATOM   1589 C CD2 . HIS A 1 280 ? 149.571 143.563 185.983 1.00 118.78 ? 280 HIS A CD2 1 
ATOM   1590 C CE1 . HIS A 1 280 ? 151.016 142.057 186.659 1.00 106.22 ? 280 HIS A CE1 1 
ATOM   1591 N NE2 . HIS A 1 280 ? 149.788 142.509 186.838 1.00 120.79 ? 280 HIS A NE2 1 
ATOM   1592 N N   . GLY A 1 281 ? 154.217 145.212 185.081 1.00 93.37  ? 281 GLY A N   1 
ATOM   1593 C CA  . GLY A 1 281 ? 155.338 144.638 185.849 1.00 84.71  ? 281 GLY A CA  1 
ATOM   1594 C C   . GLY A 1 281 ? 155.525 143.195 185.426 1.00 86.42  ? 281 GLY A C   1 
ATOM   1595 O O   . GLY A 1 281 ? 156.504 142.571 185.885 1.00 86.23  ? 281 GLY A O   1 
ATOM   1596 N N   . SER A 1 282 ? 154.638 142.690 184.559 1.00 93.75  ? 282 SER A N   1 
ATOM   1597 C CA  . SER A 1 282 ? 154.693 141.284 184.078 1.00 97.18  ? 282 SER A CA  1 
ATOM   1598 C C   . SER A 1 282 ? 155.626 141.194 182.865 1.00 90.81  ? 282 SER A C   1 
ATOM   1599 O O   . SER A 1 282 ? 155.163 141.491 181.744 1.00 91.73  ? 282 SER A O   1 
ATOM   1600 C CB  . SER A 1 282 ? 153.313 140.759 183.758 1.00 96.68  ? 282 SER A CB  1 
ATOM   1601 O OG  . SER A 1 282 ? 152.648 141.566 182.795 1.00 91.43  ? 282 SER A OG  1 
ATOM   1602 N N   . CYS A 1 283 ? 156.876 140.775 183.069 1.00 85.09  ? 283 CYS A N   1 
ATOM   1603 C CA  . CYS A 1 283 ? 157.893 140.698 181.986 1.00 92.00  ? 283 CYS A CA  1 
ATOM   1604 C C   . CYS A 1 283 ? 157.287 140.082 180.711 1.00 102.29 ? 283 CYS A C   1 
ATOM   1605 O O   . CYS A 1 283 ? 156.627 139.025 180.833 1.00 110.45 ? 283 CYS A O   1 
ATOM   1606 C CB  . CYS A 1 283 ? 159.101 139.906 182.473 1.00 100.25 ? 283 CYS A CB  1 
ATOM   1607 S SG  . CYS A 1 283 ? 160.049 140.749 183.768 1.00 112.85 ? 283 CYS A SG  1 
ATOM   1608 N N   . VAL A 1 284 ? 157.499 140.709 179.546 1.00 97.30  ? 284 VAL A N   1 
ATOM   1609 C CA  . VAL A 1 284 ? 156.989 140.204 178.231 1.00 98.20  ? 284 VAL A CA  1 
ATOM   1610 C C   . VAL A 1 284 ? 158.085 140.444 177.179 1.00 103.48 ? 284 VAL A C   1 
ATOM   1611 O O   . VAL A 1 284 ? 158.858 141.407 177.369 1.00 102.48 ? 284 VAL A O   1 
ATOM   1612 C CB  . VAL A 1 284 ? 155.672 140.890 177.821 1.00 92.73  ? 284 VAL A CB  1 
ATOM   1613 C CG1 . VAL A 1 284 ? 155.899 142.320 177.342 1.00 94.29  ? 284 VAL A CG1 1 
ATOM   1614 C CG2 . VAL A 1 284 ? 154.935 140.096 176.752 1.00 90.54  ? 284 VAL A CG2 1 
ATOM   1615 N N   . ARG A 1 285 ? 158.176 139.612 176.132 1.00 109.19 ? 285 ARG A N   1 
ATOM   1616 C CA  . ARG A 1 285 ? 159.269 139.759 175.136 1.00 113.41 ? 285 ARG A CA  1 
ATOM   1617 C C   . ARG A 1 285 ? 158.778 140.569 173.920 1.00 114.86 ? 285 ARG A C   1 
ATOM   1618 O O   . ARG A 1 285 ? 159.564 140.719 172.960 1.00 112.89 ? 285 ARG A O   1 
ATOM   1619 C CB  . ARG A 1 285 ? 159.788 138.374 174.735 1.00 111.43 ? 285 ARG A CB  1 
ATOM   1620 C CG  . ARG A 1 285 ? 161.212 138.402 174.197 1.00 115.87 ? 285 ARG A CG  1 
ATOM   1621 C CD  . ARG A 1 285 ? 162.105 139.257 175.082 1.00 116.02 ? 285 ARG A CD  1 
ATOM   1622 N NE  . ARG A 1 285 ? 163.468 139.371 174.553 1.00 121.44 ? 285 ARG A NE  1 
ATOM   1623 C CZ  . ARG A 1 285 ? 164.041 140.515 174.208 1.00 121.12 ? 285 ARG A CZ  1 
ATOM   1624 N NH1 . ARG A 1 285 ? 163.374 141.649 174.326 1.00 117.31 ? 285 ARG A NH1 1 
ATOM   1625 N NH2 . ARG A 1 285 ? 165.281 140.521 173.752 1.00 124.49 ? 285 ARG A NH2 1 
ATOM   1626 N N   . ALA A 1 286 ? 157.542 141.082 173.958 1.00 111.87 ? 286 ALA A N   1 
ATOM   1627 C CA  . ALA A 1 286 ? 157.054 141.904 172.852 1.00 103.49 ? 286 ALA A CA  1 
ATOM   1628 C C   . ALA A 1 286 ? 156.072 142.920 173.428 1.00 96.77  ? 286 ALA A C   1 
ATOM   1629 O O   . ALA A 1 286 ? 154.908 142.593 173.674 1.00 94.78  ? 286 ALA A O   1 
ATOM   1630 C CB  . ALA A 1 286 ? 156.405 141.048 171.773 1.00 103.58 ? 286 ALA A CB  1 
ATOM   1631 N N   . CYS A 1 287 ? 156.549 144.143 173.639 1.00 99.23  ? 287 CYS A N   1 
ATOM   1632 C CA  . CYS A 1 287 ? 155.732 145.243 174.134 1.00 108.87 ? 287 CYS A CA  1 
ATOM   1633 C C   . CYS A 1 287 ? 155.616 146.340 173.082 1.00 111.57 ? 287 CYS A C   1 
ATOM   1634 O O   . CYS A 1 287 ? 155.590 147.531 173.396 1.00 111.71 ? 287 CYS A O   1 
ATOM   1635 C CB  . CYS A 1 287 ? 156.300 145.802 175.437 1.00 107.03 ? 287 CYS A CB  1 
ATOM   1636 S SG  . CYS A 1 287 ? 155.080 146.617 176.491 1.00 96.84  ? 287 CYS A SG  1 
ATOM   1637 N N   . GLY A 1 288 ? 155.547 145.943 171.816 1.00 111.08 ? 288 GLY A N   1 
ATOM   1638 C CA  . GLY A 1 288 ? 155.451 146.865 170.706 1.00 107.78 ? 288 GLY A CA  1 
ATOM   1639 C C   . GLY A 1 288 ? 154.048 147.290 170.337 1.00 110.13 ? 288 GLY A C   1 
ATOM   1640 O O   . GLY A 1 288 ? 153.874 148.004 169.343 1.00 111.64 ? 288 GLY A O   1 
ATOM   1641 N N   . ALA A 1 289 ? 153.039 146.877 171.099 1.00 111.17 ? 289 ALA A N   1 
ATOM   1642 C CA  . ALA A 1 289 ? 151.652 147.223 170.823 1.00 113.27 ? 289 ALA A CA  1 
ATOM   1643 C C   . ALA A 1 289 ? 151.210 148.324 171.779 1.00 115.01 ? 289 ALA A C   1 
ATOM   1644 O O   . ALA A 1 289 ? 151.204 148.126 172.999 1.00 112.81 ? 289 ALA A O   1 
ATOM   1645 C CB  . ALA A 1 289 ? 150.747 145.999 170.957 1.00 110.68 ? 289 ALA A CB  1 
ATOM   1646 N N   . ASP A 1 290 ? 150.843 149.480 171.220 1.00 120.00 ? 290 ASP A N   1 
ATOM   1647 C CA  . ASP A 1 290 ? 150.368 150.630 171.991 1.00 122.09 ? 290 ASP A CA  1 
ATOM   1648 C C   . ASP A 1 290 ? 151.387 151.076 173.036 1.00 116.26 ? 290 ASP A C   1 
ATOM   1649 O O   . ASP A 1 290 ? 151.019 151.589 174.096 1.00 115.95 ? 290 ASP A O   1 
ATOM   1650 C CB  . ASP A 1 290 ? 149.018 150.335 172.652 1.00 125.07 ? 290 ASP A CB  1 
ATOM   1651 C CG  . ASP A 1 290 ? 148.155 151.574 172.797 1.00 123.42 ? 290 ASP A CG  1 
ATOM   1652 O OD1 . ASP A 1 290 ? 148.703 152.694 172.731 1.00 118.82 ? 290 ASP A OD1 1 
ATOM   1653 O OD2 . ASP A 1 290 ? 146.928 151.426 172.977 1.00 122.24 ? 290 ASP A OD2 1 
ATOM   1654 N N   . SER A 1 291 ? 152.667 150.893 172.746 1.00 115.35 ? 291 SER A N   1 
ATOM   1655 C CA  . SER A 1 291 ? 153.747 151.237 173.668 1.00 117.92 ? 291 SER A CA  1 
ATOM   1656 C C   . SER A 1 291 ? 155.048 151.249 172.873 1.00 116.10 ? 291 SER A C   1 
ATOM   1657 O O   . SER A 1 291 ? 155.043 151.116 171.643 1.00 115.27 ? 291 SER A O   1 
ATOM   1658 C CB  . SER A 1 291 ? 153.798 150.264 174.847 1.00 119.61 ? 291 SER A CB  1 
ATOM   1659 O OG  . SER A 1 291 ? 154.659 149.174 174.572 1.00 119.89 ? 291 SER A OG  1 
ATOM   1660 N N   . TYR A 1 292 ? 156.168 151.410 173.575 1.00 113.20 ? 292 TYR A N   1 
ATOM   1661 C CA  . TYR A 1 292 ? 157.476 151.395 172.937 1.00 115.45 ? 292 TYR A CA  1 
ATOM   1662 C C   . TYR A 1 292 ? 158.519 150.978 173.964 1.00 113.62 ? 292 TYR A C   1 
ATOM   1663 O O   . TYR A 1 292 ? 158.275 151.001 175.173 1.00 111.43 ? 292 TYR A O   1 
ATOM   1664 C CB  . TYR A 1 292 ? 157.827 152.757 172.323 1.00 120.49 ? 292 TYR A CB  1 
ATOM   1665 C CG  . TYR A 1 292 ? 158.589 153.685 173.243 1.00 122.23 ? 292 TYR A CG  1 
ATOM   1666 C CD1 . TYR A 1 292 ? 157.939 154.389 174.246 1.00 122.66 ? 292 TYR A CD1 1 
ATOM   1667 C CD2 . TYR A 1 292 ? 159.958 153.867 173.096 1.00 117.06 ? 292 TYR A CD2 1 
ATOM   1668 C CE1 . TYR A 1 292 ? 158.633 155.240 175.085 1.00 122.51 ? 292 TYR A CE1 1 
ATOM   1669 C CE2 . TYR A 1 292 ? 160.660 154.714 173.930 1.00 114.99 ? 292 TYR A CE2 1 
ATOM   1670 C CZ  . TYR A 1 292 ? 159.993 155.399 174.923 1.00 121.37 ? 292 TYR A CZ  1 
ATOM   1671 O OH  . TYR A 1 292 ? 160.689 156.246 175.755 1.00 124.13 ? 292 TYR A OH  1 
ATOM   1672 N N   . GLU A 1 293 ? 159.690 150.598 173.463 1.00 115.52 ? 293 GLU A N   1 
ATOM   1673 C CA  . GLU A 1 293 ? 160.759 150.044 174.283 1.00 116.03 ? 293 GLU A CA  1 
ATOM   1674 C C   . GLU A 1 293 ? 161.760 151.135 174.644 1.00 121.48 ? 293 GLU A C   1 
ATOM   1675 O O   . GLU A 1 293 ? 162.226 151.870 173.767 1.00 128.45 ? 293 GLU A O   1 
ATOM   1676 C CB  . GLU A 1 293 ? 161.455 148.903 173.540 1.00 119.56 ? 293 GLU A CB  1 
ATOM   1677 C CG  . GLU A 1 293 ? 160.830 147.535 173.769 1.00 124.87 ? 293 GLU A CG  1 
ATOM   1678 C CD  . GLU A 1 293 ? 159.535 147.347 173.003 1.00 119.45 ? 293 GLU A CD  1 
ATOM   1679 O OE1 . GLU A 1 293 ? 159.303 148.092 172.028 1.00 118.22 ? 293 GLU A OE1 1 
ATOM   1680 O OE2 . GLU A 1 293 ? 158.749 146.451 173.375 1.00 111.85 ? 293 GLU A OE2 1 
ATOM   1681 N N   . MET A 1 294 ? 162.127 151.232 175.925 1.00 121.33 ? 294 MET A N   1 
ATOM   1682 C CA  . MET A 1 294 ? 163.012 152.321 176.416 1.00 127.27 ? 294 MET A CA  1 
ATOM   1683 C C   . MET A 1 294 ? 164.005 151.754 177.441 1.00 124.12 ? 294 MET A C   1 
ATOM   1684 O O   . MET A 1 294 ? 163.558 151.045 178.359 1.00 124.77 ? 294 MET A O   1 
ATOM   1685 C CB  . MET A 1 294 ? 162.139 153.417 177.038 1.00 126.83 ? 294 MET A CB  1 
ATOM   1686 C CG  . MET A 1 294 ? 162.878 154.467 177.843 1.00 124.52 ? 294 MET A CG  1 
ATOM   1687 S SD  . MET A 1 294 ? 163.488 153.887 179.439 1.00 127.84 ? 294 MET A SD  1 
ATOM   1688 C CE  . MET A 1 294 ? 162.055 153.179 180.264 1.00 123.99 ? 294 MET A CE  1 
ATOM   1689 N N   . GLU A 1 295 ? 165.295 152.075 177.309 1.00 119.95 ? 295 GLU A N   1 
ATOM   1690 C CA  . GLU A 1 295 ? 166.333 151.595 178.260 1.00 121.55 ? 295 GLU A CA  1 
ATOM   1691 C C   . GLU A 1 295 ? 166.715 152.741 179.211 1.00 124.90 ? 295 GLU A C   1 
ATOM   1692 O O   . GLU A 1 295 ? 167.564 153.571 178.818 1.00 127.68 ? 295 GLU A O   1 
ATOM   1693 C CB  . GLU A 1 295 ? 167.544 151.056 177.500 1.00 123.25 ? 295 GLU A CB  1 
ATOM   1694 C CG  . GLU A 1 295 ? 168.538 150.335 178.405 1.00 123.77 ? 295 GLU A CG  1 
ATOM   1695 C CD  . GLU A 1 295 ? 169.640 149.581 177.684 1.00 124.00 ? 295 GLU A CD  1 
ATOM   1696 O OE1 . GLU A 1 295 ? 169.671 149.604 176.436 1.00 125.15 ? 295 GLU A OE1 1 
ATOM   1697 O OE2 . GLU A 1 295 ? 170.472 148.964 178.381 1.00 124.56 ? 295 GLU A OE2 1 
ATOM   1698 N N   . GLU A 1 296 ? 166.116 152.783 180.406 1.00 126.10 ? 296 GLU A N   1 
ATOM   1699 C CA  . GLU A 1 296 ? 166.433 153.825 181.422 1.00 129.54 ? 296 GLU A CA  1 
ATOM   1700 C C   . GLU A 1 296 ? 167.507 153.272 182.366 1.00 132.71 ? 296 GLU A C   1 
ATOM   1701 O O   . GLU A 1 296 ? 168.283 154.088 182.910 1.00 139.84 ? 296 GLU A O   1 
ATOM   1702 C CB  . GLU A 1 296 ? 165.217 154.255 182.245 1.00 122.86 ? 296 GLU A CB  1 
ATOM   1703 C CG  . GLU A 1 296 ? 164.437 153.096 182.860 1.00 119.22 ? 296 GLU A CG  1 
ATOM   1704 C CD  . GLU A 1 296 ? 163.293 153.524 183.760 1.00 120.34 ? 296 GLU A CD  1 
ATOM   1705 O OE1 . GLU A 1 296 ? 162.392 154.240 183.276 1.00 123.56 ? 296 GLU A OE1 1 
ATOM   1706 O OE2 . GLU A 1 296 ? 163.300 153.131 184.945 1.00 119.56 ? 296 GLU A OE2 1 
ATOM   1707 N N   . ASP A 1 297 ? 167.542 151.949 182.554 1.00 126.71 ? 297 ASP A N   1 
ATOM   1708 C CA  . ASP A 1 297 ? 168.536 151.290 183.444 1.00 125.44 ? 297 ASP A CA  1 
ATOM   1709 C C   . ASP A 1 297 ? 169.221 150.166 182.664 1.00 127.93 ? 297 ASP A C   1 
ATOM   1710 O O   . ASP A 1 297 ? 169.160 150.204 181.419 1.00 128.77 ? 297 ASP A O   1 
ATOM   1711 C CB  . ASP A 1 297 ? 167.877 150.780 184.715 1.00 128.50 ? 297 ASP A CB  1 
ATOM   1712 C CG  . ASP A 1 297 ? 166.857 151.716 185.346 1.00 129.98 ? 297 ASP A CG  1 
ATOM   1713 O OD1 . ASP A 1 297 ? 167.230 152.866 185.657 1.00 133.48 ? 297 ASP A OD1 1 
ATOM   1714 O OD2 . ASP A 1 297 ? 165.701 151.281 185.529 1.00 123.61 ? 297 ASP A OD2 1 
ATOM   1715 N N   . GLY A 1 298 ? 169.836 149.197 183.351 1.00 130.51 ? 298 GLY A N   1 
ATOM   1716 C CA  . GLY A 1 298 ? 170.481 148.066 182.714 1.00 133.43 ? 298 GLY A CA  1 
ATOM   1717 C C   . GLY A 1 298 ? 169.526 147.058 182.110 1.00 130.67 ? 298 GLY A C   1 
ATOM   1718 O O   . GLY A 1 298 ? 169.983 146.126 181.440 1.00 126.26 ? 298 GLY A O   1 
ATOM   1719 N N   . VAL A 1 299 ? 168.223 147.221 182.326 1.00 130.47 ? 299 VAL A N   1 
ATOM   1720 C CA  . VAL A 1 299 ? 167.210 146.317 181.795 1.00 127.34 ? 299 VAL A CA  1 
ATOM   1721 C C   . VAL A 1 299 ? 166.284 147.104 180.876 1.00 121.46 ? 299 VAL A C   1 
ATOM   1722 O O   . VAL A 1 299 ? 165.838 148.205 181.221 1.00 116.62 ? 299 VAL A O   1 
ATOM   1723 C CB  . VAL A 1 299 ? 166.425 145.614 182.921 1.00 127.99 ? 299 VAL A CB  1 
ATOM   1724 C CG1 . VAL A 1 299 ? 165.696 146.621 183.803 1.00 123.24 ? 299 VAL A CG1 1 
ATOM   1725 C CG2 . VAL A 1 299 ? 165.451 144.600 182.336 1.00 122.85 ? 299 VAL A CG2 1 
ATOM   1726 N N   . ARG A 1 300 ? 166.039 146.527 179.694 1.00 120.17 ? 300 ARG A N   1 
ATOM   1727 C CA  . ARG A 1 300 ? 165.112 147.165 178.727 1.00 116.83 ? 300 ARG A CA  1 
ATOM   1728 C C   . ARG A 1 300 ? 163.743 147.282 179.406 1.00 113.75 ? 300 ARG A C   1 
ATOM   1729 O O   . ARG A 1 300 ? 163.315 146.309 180.062 1.00 112.72 ? 300 ARG A O   1 
ATOM   1730 C CB  . ARG A 1 300 ? 165.064 146.372 177.416 1.00 112.91 ? 300 ARG A CB  1 
ATOM   1731 C CG  . ARG A 1 300 ? 164.036 146.836 176.392 1.00 108.67 ? 300 ARG A CG  1 
ATOM   1732 C CD  . ARG A 1 300 ? 163.960 148.348 176.226 1.00 111.63 ? 300 ARG A CD  1 
ATOM   1733 N NE  . ARG A 1 300 ? 165.191 149.009 175.777 1.00 116.10 ? 300 ARG A NE  1 
ATOM   1734 C CZ  . ARG A 1 300 ? 165.758 148.866 174.586 1.00 120.67 ? 300 ARG A CZ  1 
ATOM   1735 N NH1 . ARG A 1 300 ? 165.196 148.101 173.667 1.00 123.17 ? 300 ARG A NH1 1 
ATOM   1736 N NH2 . ARG A 1 300 ? 166.882 149.505 174.313 1.00 122.04 ? 300 ARG A NH2 1 
ATOM   1737 N N   . LYS A 1 301 ? 163.102 148.436 179.261 1.00 112.23 ? 301 LYS A N   1 
ATOM   1738 C CA  . LYS A 1 301 ? 161.789 148.694 179.907 1.00 106.45 ? 301 LYS A CA  1 
ATOM   1739 C C   . LYS A 1 301 ? 160.785 149.234 178.879 1.00 108.17 ? 301 LYS A C   1 
ATOM   1740 O O   . LYS A 1 301 ? 161.117 150.207 178.191 1.00 108.15 ? 301 LYS A O   1 
ATOM   1741 C CB  . LYS A 1 301 ? 161.988 149.666 181.073 1.00 95.90  ? 301 LYS A CB  1 
ATOM   1742 C CG  . LYS A 1 301 ? 160.707 150.096 181.771 1.00 93.72  ? 301 LYS A CG  1 
ATOM   1743 C CD  . LYS A 1 301 ? 160.935 150.829 183.086 1.00 96.19  ? 301 LYS A CD  1 
ATOM   1744 C CE  . LYS A 1 301 ? 161.665 150.000 184.092 1.00 94.64  ? 301 LYS A CE  1 
ATOM   1745 N NZ  . LYS A 1 301 ? 161.528 150.552 185.440 1.00 111.96 ? 301 LYS A NZ  1 
ATOM   1746 N N   . CYS A 1 302 ? 159.574 148.686 178.841 1.00 106.54 ? 302 CYS A N   1 
ATOM   1747 C CA  . CYS A 1 302 ? 158.534 149.068 177.894 1.00 108.78 ? 302 CYS A CA  1 
ATOM   1748 C C   . CYS A 1 302 ? 157.733 150.236 178.462 1.00 111.90 ? 302 CYS A C   1 
ATOM   1749 O O   . CYS A 1 302 ? 157.119 150.114 179.528 1.00 104.06 ? 302 CYS A O   1 
ATOM   1750 C CB  . CYS A 1 302 ? 157.615 147.885 177.591 1.00 102.38 ? 302 CYS A CB  1 
ATOM   1751 S SG  . CYS A 1 302 ? 155.965 148.362 177.032 1.00 117.70 ? 302 CYS A SG  1 
ATOM   1752 N N   . LYS A 1 303 ? 157.737 151.359 177.751 1.00 119.67 ? 303 LYS A N   1 
ATOM   1753 C CA  . LYS A 1 303 ? 156.994 152.549 178.140 1.00 120.98 ? 303 LYS A CA  1 
ATOM   1754 C C   . LYS A 1 303 ? 155.907 152.857 177.119 1.00 119.39 ? 303 LYS A C   1 
ATOM   1755 O O   . LYS A 1 303 ? 155.879 152.313 176.012 1.00 116.08 ? 303 LYS A O   1 
ATOM   1756 C CB  . LYS A 1 303 ? 157.924 153.758 178.297 1.00 115.01 ? 303 LYS A CB  1 
ATOM   1757 C CG  . LYS A 1 303 ? 157.834 154.429 179.656 1.00 111.44 ? 303 LYS A CG  1 
ATOM   1758 C CD  . LYS A 1 303 ? 159.059 155.278 179.935 1.00 114.48 ? 303 LYS A CD  1 
ATOM   1759 C CE  . LYS A 1 303 ? 158.975 155.942 181.298 1.00 114.39 ? 303 LYS A CE  1 
ATOM   1760 N NZ  . LYS A 1 303 ? 157.797 156.846 181.400 1.00 116.71 ? 303 LYS A NZ  1 
ATOM   1761 N N   . LYS A 1 304 ? 155.009 153.757 177.510 1.00 121.55 ? 304 LYS A N   1 
ATOM   1762 C CA  . LYS A 1 304 ? 153.874 154.112 176.672 1.00 122.52 ? 304 LYS A CA  1 
ATOM   1763 C C   . LYS A 1 304 ? 154.328 154.825 175.404 1.00 119.96 ? 304 LYS A C   1 
ATOM   1764 O O   . LYS A 1 304 ? 155.305 155.579 175.399 1.00 115.70 ? 304 LYS A O   1 
ATOM   1765 C CB  . LYS A 1 304 ? 152.897 154.997 177.444 1.00 122.80 ? 304 LYS A CB  1 
ATOM   1766 C CG  . LYS A 1 304 ? 152.007 154.241 178.417 1.00 123.20 ? 304 LYS A CG  1 
ATOM   1767 C CD  . LYS A 1 304 ? 151.387 153.017 177.765 1.00 120.71 ? 304 LYS A CD  1 
ATOM   1768 C CE  . LYS A 1 304 ? 150.315 153.407 176.760 1.00 125.66 ? 304 LYS A CE  1 
ATOM   1769 N NZ  . LYS A 1 304 ? 149.505 152.235 176.331 1.00 125.63 ? 304 LYS A NZ  1 
ATOM   1770 N N   . CYS A 1 305 ? 153.597 154.580 174.321 1.00 122.58 ? 305 CYS A N   1 
ATOM   1771 C CA  . CYS A 1 305 ? 153.881 155.184 173.022 1.00 124.76 ? 305 CYS A CA  1 
ATOM   1772 C C   . CYS A 1 305 ? 153.406 156.630 173.060 1.00 128.03 ? 305 CYS A C   1 
ATOM   1773 O O   . CYS A 1 305 ? 152.222 156.913 172.860 1.00 131.73 ? 305 CYS A O   1 
ATOM   1774 C CB  . CYS A 1 305 ? 153.195 154.392 171.913 1.00 132.65 ? 305 CYS A CB  1 
ATOM   1775 S SG  . CYS A 1 305 ? 153.543 154.927 170.221 1.00 141.78 ? 305 CYS A SG  1 
ATOM   1776 N N   . GLU A 1 306 ? 154.329 157.553 173.326 1.00 128.51 ? 306 GLU A N   1 
ATOM   1777 C CA  . GLU A 1 306 ? 153.993 158.973 173.397 1.00 125.73 ? 306 GLU A CA  1 
ATOM   1778 C C   . GLU A 1 306 ? 153.547 159.454 172.021 1.00 116.87 ? 306 GLU A C   1 
ATOM   1779 O O   . GLU A 1 306 ? 154.367 159.618 171.112 1.00 116.18 ? 306 GLU A O   1 
ATOM   1780 C CB  . GLU A 1 306 ? 155.184 159.775 173.917 1.00 125.74 ? 306 GLU A CB  1 
ATOM   1781 C CG  . GLU A 1 306 ? 156.526 159.421 173.283 1.00 128.10 ? 306 GLU A CG  1 
ATOM   1782 C CD  . GLU A 1 306 ? 157.011 160.479 172.312 1.00 132.59 ? 306 GLU A CD  1 
ATOM   1783 O OE1 . GLU A 1 306 ? 156.577 161.644 172.434 1.00 138.82 ? 306 GLU A OE1 1 
ATOM   1784 O OE2 . GLU A 1 306 ? 157.825 160.146 171.425 1.00 129.15 ? 306 GLU A OE2 1 
ATOM   1785 N N   . GLY A 1 307 ? 152.246 159.683 171.868 1.00 112.00 ? 307 GLY A N   1 
ATOM   1786 C CA  . GLY A 1 307 ? 151.672 159.899 170.563 1.00 109.22 ? 307 GLY A CA  1 
ATOM   1787 C C   . GLY A 1 307 ? 151.989 158.718 169.673 1.00 109.67 ? 307 GLY A C   1 
ATOM   1788 O O   . GLY A 1 307 ? 151.782 157.559 170.046 1.00 112.77 ? 307 GLY A O   1 
ATOM   1789 N N   . PRO A 1 308 ? 152.492 158.985 168.476 1.00 110.27 ? 308 PRO A N   1 
ATOM   1790 C CA  . PRO A 1 308 ? 153.109 157.911 167.691 1.00 108.58 ? 308 PRO A CA  1 
ATOM   1791 C C   . PRO A 1 308 ? 154.581 157.756 168.037 1.00 109.80 ? 308 PRO A C   1 
ATOM   1792 O O   . PRO A 1 308 ? 155.339 158.730 167.983 1.00 105.01 ? 308 PRO A O   1 
ATOM   1793 C CB  . PRO A 1 308 ? 152.917 158.376 166.240 1.00 103.92 ? 308 PRO A CB  1 
ATOM   1794 C CG  . PRO A 1 308 ? 152.000 159.584 166.314 1.00 101.79 ? 308 PRO A CG  1 
ATOM   1795 C CD  . PRO A 1 308 ? 152.247 160.179 167.658 1.00 111.58 ? 308 PRO A CD  1 
ATOM   1796 N N   . CYS A 1 309 ? 155.000 156.546 168.395 1.00 108.92 ? 309 CYS A N   1 
ATOM   1797 C CA  . CYS A 1 309 ? 156.393 156.302 168.734 1.00 110.83 ? 309 CYS A CA  1 
ATOM   1798 C C   . CYS A 1 309 ? 157.186 155.912 167.488 1.00 100.59 ? 309 CYS A C   1 
ATOM   1799 O O   . CYS A 1 309 ? 156.647 155.788 166.385 1.00 96.64  ? 309 CYS A O   1 
ATOM   1800 C CB  . CYS A 1 309 ? 156.494 155.244 169.830 1.00 117.66 ? 309 CYS A CB  1 
ATOM   1801 S SG  . CYS A 1 309 ? 155.252 153.949 169.717 1.00 136.62 ? 309 CYS A SG  1 
ATOM   1802 N N   . ARG A 1 310 ? 158.489 155.714 167.678 1.00 95.65  ? 310 ARG A N   1 
ATOM   1803 C CA  . ARG A 1 310 ? 159.410 155.571 166.558 1.00 83.04  ? 310 ARG A CA  1 
ATOM   1804 C C   . ARG A 1 310 ? 159.055 154.367 165.695 1.00 84.07  ? 310 ARG A C   1 
ATOM   1805 O O   . ARG A 1 310 ? 158.749 153.284 166.200 1.00 94.22  ? 310 ARG A O   1 
ATOM   1806 C CB  . ARG A 1 310 ? 160.843 155.440 167.072 1.00 90.56  ? 310 ARG A CB  1 
ATOM   1807 C CG  . ARG A 1 310 ? 161.483 156.759 167.470 1.00 92.12  ? 310 ARG A CG  1 
ATOM   1808 C CD  . ARG A 1 310 ? 162.099 157.462 166.273 1.00 94.54  ? 310 ARG A CD  1 
ATOM   1809 N NE  . ARG A 1 310 ? 163.365 156.862 165.872 1.00 93.62  ? 310 ARG A NE  1 
ATOM   1810 C CZ  . ARG A 1 310 ? 163.497 155.981 164.890 1.00 90.40  ? 310 ARG A CZ  1 
ATOM   1811 N NH1 . ARG A 1 310 ? 162.454 155.570 164.187 1.00 80.84  ? 310 ARG A NH1 1 
ATOM   1812 N NH2 . ARG A 1 310 ? 164.704 155.502 164.606 1.00 83.46  ? 310 ARG A NH2 1 
ATOM   1813 N N   . LYS A 1 311 ? 159.092 154.570 164.377 1.00 70.50  ? 311 LYS A N   1 
ATOM   1814 C CA  . LYS A 1 311 ? 158.848 153.495 163.418 1.00 77.46  ? 311 LYS A CA  1 
ATOM   1815 C C   . LYS A 1 311 ? 159.618 153.839 162.146 1.00 67.61  ? 311 LYS A C   1 
ATOM   1816 O O   . LYS A 1 311 ? 159.138 154.625 161.325 1.00 70.98  ? 311 LYS A O   1 
ATOM   1817 C CB  . LYS A 1 311 ? 157.360 153.327 163.144 1.00 74.04  ? 311 LYS A CB  1 
ATOM   1818 C CG  . LYS A 1 311 ? 157.036 152.340 162.034 1.00 69.26  ? 311 LYS A CG  1 
ATOM   1819 C CD  . LYS A 1 311 ? 155.627 151.789 162.177 1.00 70.08  ? 311 LYS A CD  1 
ATOM   1820 C CE  . LYS A 1 311 ? 154.950 151.642 160.824 1.00 71.47  ? 311 LYS A CE  1 
ATOM   1821 N NZ  . LYS A 1 311 ? 155.624 150.629 159.966 1.00 78.30  ? 311 LYS A NZ  1 
ATOM   1822 N N   . VAL A 1 312 ? 160.811 153.256 161.996 1.00 68.76  ? 312 VAL A N   1 
ATOM   1823 C CA  . VAL A 1 312 ? 161.592 153.477 160.785 1.00 64.23  ? 312 VAL A CA  1 
ATOM   1824 C C   . VAL A 1 312 ? 160.818 152.940 159.594 1.00 62.42  ? 312 VAL A C   1 
ATOM   1825 O O   . VAL A 1 312 ? 160.327 151.805 159.609 1.00 65.59  ? 312 VAL A O   1 
ATOM   1826 C CB  . VAL A 1 312 ? 162.974 152.819 160.905 1.00 70.97  ? 312 VAL A CB  1 
ATOM   1827 C CG1 . VAL A 1 312 ? 163.702 152.867 159.571 1.00 56.56  ? 312 VAL A CG1 1 
ATOM   1828 C CG2 . VAL A 1 312 ? 163.795 153.501 161.985 1.00 71.38  ? 312 VAL A CG2 1 
ATOM   1829 N N   . CYS A 1 313 ? 160.702 153.757 158.552 1.00 55.19  ? 313 CYS A N   1 
ATOM   1830 C CA  . CYS A 1 313 ? 159.831 153.435 157.435 1.00 54.88  ? 313 CYS A CA  1 
ATOM   1831 C C   . CYS A 1 313 ? 160.509 153.861 156.144 1.00 48.93  ? 313 CYS A C   1 
ATOM   1832 O O   . CYS A 1 313 ? 161.120 154.929 156.083 1.00 49.29  ? 313 CYS A O   1 
ATOM   1833 C CB  . CYS A 1 313 ? 158.479 154.132 157.597 1.00 56.05  ? 313 CYS A CB  1 
ATOM   1834 S SG  . CYS A 1 313 ? 157.261 153.778 156.332 1.00 72.99  ? 313 CYS A SG  1 
ATOM   1835 N N   . ASN A 1 314 ? 160.405 153.021 155.119 1.00 52.42  ? 314 ASN A N   1 
ATOM   1836 C CA  . ASN A 1 314 ? 161.060 153.316 153.854 1.00 59.55  ? 314 ASN A CA  1 
ATOM   1837 C C   . ASN A 1 314 ? 160.365 154.469 153.142 1.00 60.89  ? 314 ASN A C   1 
ATOM   1838 O O   . ASN A 1 314 ? 159.135 154.565 153.130 1.00 59.96  ? 314 ASN A O   1 
ATOM   1839 C CB  . ASN A 1 314 ? 161.074 152.078 152.959 1.00 66.33  ? 314 ASN A CB  1 
ATOM   1840 C CG  . ASN A 1 314 ? 162.288 151.203 153.198 1.00 70.91  ? 314 ASN A CG  1 
ATOM   1841 O OD1 . ASN A 1 314 ? 163.373 151.698 153.504 1.00 70.10  ? 314 ASN A OD1 1 
ATOM   1842 N ND2 . ASN A 1 314 ? 162.112 149.896 153.057 1.00 68.55  ? 314 ASN A ND2 1 
ATOM   1843 N N   . GLY A 1 315 ? 161.148 155.341 152.489 1.00 62.28  ? 315 GLY A N   1 
ATOM   1844 C CA  . GLY A 1 315 ? 160.602 156.500 151.746 1.00 51.48  ? 315 GLY A CA  1 
ATOM   1845 C C   . GLY A 1 315 ? 160.594 156.246 150.249 1.00 57.26  ? 315 GLY A C   1 
ATOM   1846 O O   . GLY A 1 315 ? 160.978 155.129 149.851 1.00 65.80  ? 315 GLY A O   1 
ATOM   1847 N N   . ILE A 1 316 ? 160.206 157.237 149.437 1.00 48.07  ? 316 ILE A N   1 
ATOM   1848 C CA  . ILE A 1 316 ? 160.090 157.061 147.953 1.00 46.72  ? 316 ILE A CA  1 
ATOM   1849 C C   . ILE A 1 316 ? 161.497 157.086 147.333 1.00 50.17  ? 316 ILE A C   1 
ATOM   1850 O O   . ILE A 1 316 ? 162.089 158.181 147.302 1.00 48.50  ? 316 ILE A O   1 
ATOM   1851 C CB  . ILE A 1 316 ? 159.160 158.126 147.335 1.00 35.08  ? 316 ILE A CB  1 
ATOM   1852 C CG1 . ILE A 1 316 ? 157.811 158.218 148.061 1.00 35.60  ? 316 ILE A CG1 1 
ATOM   1853 C CG2 . ILE A 1 316 ? 158.970 157.881 145.838 1.00 43.73  ? 316 ILE A CG2 1 
ATOM   1854 C CD1 . ILE A 1 316 ? 157.042 156.909 148.130 1.00 41.52  ? 316 ILE A CD1 1 
ATOM   1855 N N   . GLY A 1 317 ? 161.995 155.950 146.826 1.00 57.59  ? 317 GLY A N   1 
ATOM   1856 C CA  . GLY A 1 317 ? 163.311 155.817 146.249 1.00 54.24  ? 317 GLY A CA  1 
ATOM   1857 C C   . GLY A 1 317 ? 164.253 154.914 147.019 1.00 63.32  ? 317 GLY A C   1 
ATOM   1858 O O   . GLY A 1 317 ? 165.295 154.528 146.479 1.00 68.23  ? 317 GLY A O   1 
ATOM   1859 N N   . ILE A 1 318 ? 163.916 154.566 148.259 1.00 67.26  ? 318 ILE A N   1 
ATOM   1860 C CA  . ILE A 1 318 ? 164.731 153.682 149.083 1.00 64.27  ? 318 ILE A CA  1 
ATOM   1861 C C   . ILE A 1 318 ? 163.838 152.583 149.640 1.00 57.66  ? 318 ILE A C   1 
ATOM   1862 O O   . ILE A 1 318 ? 162.819 152.869 150.277 1.00 55.29  ? 318 ILE A O   1 
ATOM   1863 C CB  . ILE A 1 318 ? 165.428 154.447 150.224 1.00 68.53  ? 318 ILE A CB  1 
ATOM   1864 C CG1 . ILE A 1 318 ? 166.631 155.222 149.686 1.00 74.19  ? 318 ILE A CG1 1 
ATOM   1865 C CG2 . ILE A 1 318 ? 165.861 153.491 151.322 1.00 62.11  ? 318 ILE A CG2 1 
ATOM   1866 C CD1 . ILE A 1 318 ? 167.366 156.017 150.741 1.00 70.73  ? 318 ILE A CD1 1 
ATOM   1867 N N   . GLY A 1 319 ? 164.222 151.330 149.402 1.00 63.22  ? 319 GLY A N   1 
ATOM   1868 C CA  . GLY A 1 319 ? 163.461 150.199 149.897 1.00 70.66  ? 319 GLY A CA  1 
ATOM   1869 C C   . GLY A 1 319 ? 162.538 149.599 148.857 1.00 68.87  ? 319 GLY A C   1 
ATOM   1870 O O   . GLY A 1 319 ? 162.885 149.536 147.674 1.00 68.36  ? 319 GLY A O   1 
ATOM   1871 N N   . GLU A 1 320 ? 161.357 149.150 149.287 1.00 69.54  ? 320 GLU A N   1 
ATOM   1872 C CA  . GLU A 1 320 ? 160.379 148.616 148.346 1.00 70.65  ? 320 GLU A CA  1 
ATOM   1873 C C   . GLU A 1 320 ? 159.867 149.683 147.388 1.00 72.41  ? 320 GLU A C   1 
ATOM   1874 O O   . GLU A 1 320 ? 159.368 149.345 146.310 1.00 71.88  ? 320 GLU A O   1 
ATOM   1875 C CB  . GLU A 1 320 ? 159.208 147.984 149.099 1.00 68.34  ? 320 GLU A CB  1 
ATOM   1876 C CG  . GLU A 1 320 ? 158.588 148.883 150.155 1.00 69.57  ? 320 GLU A CG  1 
ATOM   1877 C CD  . GLU A 1 320 ? 159.200 148.682 151.526 1.00 77.20  ? 320 GLU A CD  1 
ATOM   1878 O OE1 . GLU A 1 320 ? 160.406 148.966 151.686 1.00 74.90  ? 320 GLU A OE1 1 
ATOM   1879 O OE2 . GLU A 1 320 ? 158.476 148.242 152.443 1.00 88.47  ? 320 GLU A OE2 1 
ATOM   1880 N N   . PHE A 1 321 ? 159.978 150.960 147.759 1.00 72.71  ? 321 PHE A N   1 
ATOM   1881 C CA  . PHE A 1 321 ? 159.629 152.071 146.884 1.00 64.43  ? 321 PHE A CA  1 
ATOM   1882 C C   . PHE A 1 321 ? 160.837 152.628 146.145 1.00 56.87  ? 321 PHE A C   1 
ATOM   1883 O O   . PHE A 1 321 ? 160.883 153.832 145.864 1.00 58.10  ? 321 PHE A O   1 
ATOM   1884 C CB  . PHE A 1 321 ? 158.943 153.181 147.682 1.00 56.19  ? 321 PHE A CB  1 
ATOM   1885 C CG  . PHE A 1 321 ? 158.117 152.684 148.831 1.00 64.86  ? 321 PHE A CG  1 
ATOM   1886 C CD1 . PHE A 1 321 ? 156.971 151.943 148.607 1.00 67.18  ? 321 PHE A CD1 1 
ATOM   1887 C CD2 . PHE A 1 321 ? 158.479 152.968 150.135 1.00 62.06  ? 321 PHE A CD2 1 
ATOM   1888 C CE1 . PHE A 1 321 ? 156.205 151.491 149.663 1.00 65.89  ? 321 PHE A CE1 1 
ATOM   1889 C CE2 . PHE A 1 321 ? 157.718 152.518 151.194 1.00 65.64  ? 321 PHE A CE2 1 
ATOM   1890 C CZ  . PHE A 1 321 ? 156.580 151.778 150.957 1.00 65.59  ? 321 PHE A CZ  1 
ATOM   1891 N N   . LYS A 1 322 ? 161.819 151.779 145.829 1.00 54.96  ? 322 LYS A N   1 
ATOM   1892 C CA  . LYS A 1 322 ? 163.047 152.257 145.202 1.00 61.96  ? 322 LYS A CA  1 
ATOM   1893 C C   . LYS A 1 322 ? 162.763 152.920 143.861 1.00 64.99  ? 322 LYS A C   1 
ATOM   1894 O O   . LYS A 1 322 ? 163.349 153.959 143.537 1.00 69.30  ? 322 LYS A O   1 
ATOM   1895 C CB  . LYS A 1 322 ? 164.032 151.098 145.035 1.00 68.61  ? 322 LYS A CB  1 
ATOM   1896 C CG  . LYS A 1 322 ? 164.927 151.200 143.810 1.00 67.24  ? 322 LYS A CG  1 
ATOM   1897 C CD  . LYS A 1 322 ? 165.754 149.938 143.625 1.00 71.47  ? 322 LYS A CD  1 
ATOM   1898 C CE  . LYS A 1 322 ? 164.866 148.714 143.469 1.00 74.54  ? 322 LYS A CE  1 
ATOM   1899 N NZ  . LYS A 1 322 ? 164.078 148.758 142.207 1.00 69.02  ? 322 LYS A NZ  1 
ATOM   1900 N N   . ASP A 1 323 ? 161.826 152.342 143.104 1.00 60.69  ? 323 ASP A N   1 
ATOM   1901 C CA  . ASP A 1 323 ? 161.509 152.877 141.750 1.00 58.89  ? 323 ASP A CA  1 
ATOM   1902 C C   . ASP A 1 323 ? 160.134 153.555 141.762 1.00 62.62  ? 323 ASP A C   1 
ATOM   1903 O O   . ASP A 1 323 ? 159.634 153.884 140.665 1.00 64.86  ? 323 ASP A O   1 
ATOM   1904 C CB  . ASP A 1 323 ? 161.639 151.789 140.696 1.00 66.34  ? 323 ASP A CB  1 
ATOM   1905 C CG  . ASP A 1 323 ? 161.119 150.418 141.104 1.00 69.04  ? 323 ASP A CG  1 
ATOM   1906 O OD1 . ASP A 1 323 ? 160.566 150.306 142.218 1.00 62.48  ? 323 ASP A OD1 1 
ATOM   1907 O OD2 . ASP A 1 323 ? 161.286 149.469 140.309 1.00 72.53  ? 323 ASP A OD2 1 
ATOM   1908 N N   . SER A 1 324 ? 159.542 153.755 142.943 1.00 59.92  ? 324 SER A N   1 
ATOM   1909 C CA  . SER A 1 324 ? 158.260 154.503 143.019 1.00 46.22  ? 324 SER A CA  1 
ATOM   1910 C C   . SER A 1 324 ? 158.540 155.983 142.726 1.00 45.77  ? 324 SER A C   1 
ATOM   1911 O O   . SER A 1 324 ? 159.666 156.436 143.023 1.00 49.55  ? 324 SER A O   1 
ATOM   1912 C CB  . SER A 1 324 ? 157.594 154.325 144.356 1.00 48.44  ? 324 SER A CB  1 
ATOM   1913 O OG  . SER A 1 324 ? 157.252 152.964 144.573 1.00 57.11  ? 324 SER A OG  1 
ATOM   1914 N N   . LEU A 1 325 ? 157.568 156.703 142.162 1.00 18.16  ? 325 LEU A N   1 
ATOM   1915 C CA  . LEU A 1 325 ? 157.807 158.119 141.773 1.00 10.33  ? 325 LEU A CA  1 
ATOM   1916 C C   . LEU A 1 325 ? 157.075 159.058 142.743 1.00 11.39  ? 325 LEU A C   1 
ATOM   1917 O O   . LEU A 1 325 ? 157.381 160.269 142.723 1.00 14.41  ? 325 LEU A O   1 
ATOM   1918 C CB  . LEU A 1 325 ? 157.355 158.344 140.333 1.00 8.69   ? 325 LEU A CB  1 
ATOM   1919 C CG  . LEU A 1 325 ? 157.847 157.312 139.316 1.00 12.09  ? 325 LEU A CG  1 
ATOM   1920 C CD1 . LEU A 1 325 ? 156.681 156.518 138.754 1.00 13.23  ? 325 LEU A CD1 1 
ATOM   1921 C CD2 . LEU A 1 325 ? 158.634 157.987 138.210 1.00 12.57  ? 325 LEU A CD2 1 
ATOM   1922 N N   . SER A 1 326 ? 156.160 158.524 143.556 1.00 7.78   ? 326 SER A N   1 
ATOM   1923 C CA  . SER A 1 326 ? 155.355 159.385 144.461 1.00 8.40   ? 326 SER A CA  1 
ATOM   1924 C C   . SER A 1 326 ? 154.603 158.537 145.490 1.00 10.41  ? 326 SER A C   1 
ATOM   1925 O O   . SER A 1 326 ? 154.810 157.305 145.508 1.00 14.00  ? 326 SER A O   1 
ATOM   1926 C CB  . SER A 1 326 ? 154.381 160.215 143.673 1.00 10.16  ? 326 SER A CB  1 
ATOM   1927 O OG  . SER A 1 326 ? 153.446 159.388 142.996 1.00 12.35  ? 326 SER A OG  1 
ATOM   1928 N N   . ILE A 1 327 ? 153.811 159.162 146.362 1.00 9.19   ? 327 ILE A N   1 
ATOM   1929 C CA  . ILE A 1 327 ? 152.984 158.404 147.345 1.00 12.01  ? 327 ILE A CA  1 
ATOM   1930 C C   . ILE A 1 327 ? 151.589 158.244 146.718 1.00 14.78  ? 327 ILE A C   1 
ATOM   1931 O O   . ILE A 1 327 ? 150.693 159.034 147.078 1.00 31.06  ? 327 ILE A O   1 
ATOM   1932 C CB  . ILE A 1 327 ? 152.957 159.100 148.719 1.00 9.11   ? 327 ILE A CB  1 
ATOM   1933 C CG1 . ILE A 1 327 ? 154.367 159.443 149.206 1.00 7.79   ? 327 ILE A CG1 1 
ATOM   1934 C CG2 . ILE A 1 327 ? 152.202 158.251 149.743 1.00 14.10  ? 327 ILE A CG2 1 
ATOM   1935 C CD1 . ILE A 1 327 ? 154.406 160.214 150.514 1.00 8.04   ? 327 ILE A CD1 1 
ATOM   1936 N N   . ASN A 1 328 ? 151.416 157.282 145.800 1.00 12.40  ? 328 ASN A N   1 
ATOM   1937 C CA  . ASN A 1 328 ? 150.109 157.062 145.121 1.00 13.00  ? 328 ASN A CA  1 
ATOM   1938 C C   . ASN A 1 328 ? 149.156 156.300 146.048 1.00 24.73  ? 328 ASN A C   1 
ATOM   1939 O O   . ASN A 1 328 ? 149.365 156.344 147.278 1.00 25.69  ? 328 ASN A O   1 
ATOM   1940 C CB  . ASN A 1 328 ? 150.269 156.379 143.768 1.00 19.46  ? 328 ASN A CB  1 
ATOM   1941 C CG  . ASN A 1 328 ? 151.603 155.696 143.591 1.00 16.43  ? 328 ASN A CG  1 
ATOM   1942 O OD1 . ASN A 1 328 ? 152.654 156.301 143.830 1.00 14.80  ? 328 ASN A OD1 1 
ATOM   1943 N ND2 . ASN A 1 328 ? 151.571 154.439 143.171 1.00 19.39  ? 328 ASN A ND2 1 
ATOM   1944 N N   . ALA A 1 329 ? 148.131 155.665 145.473 1.00 29.73  ? 329 ALA A N   1 
ATOM   1945 C CA  . ALA A 1 329 ? 147.153 154.898 146.280 1.00 27.40  ? 329 ALA A CA  1 
ATOM   1946 C C   . ALA A 1 329 ? 147.663 153.468 146.468 1.00 27.47  ? 329 ALA A C   1 
ATOM   1947 O O   . ALA A 1 329 ? 146.907 152.619 146.988 1.00 29.29  ? 329 ALA A O   1 
ATOM   1948 C CB  . ALA A 1 329 ? 145.797 154.923 145.610 1.00 26.92  ? 329 ALA A CB  1 
ATOM   1949 N N   . THR A 1 330 ? 148.908 153.211 146.055 1.00 23.60  ? 330 THR A N   1 
ATOM   1950 C CA  . THR A 1 330 ? 149.499 151.865 146.212 1.00 29.82  ? 330 THR A CA  1 
ATOM   1951 C C   . THR A 1 330 ? 150.472 151.890 147.371 1.00 31.25  ? 330 THR A C   1 
ATOM   1952 O O   . THR A 1 330 ? 150.320 151.054 148.288 1.00 31.96  ? 330 THR A O   1 
ATOM   1953 C CB  . THR A 1 330 ? 150.173 151.441 144.909 1.00 27.79  ? 330 THR A CB  1 
ATOM   1954 O OG1 . THR A 1 330 ? 149.195 151.651 143.896 1.00 31.87  ? 330 THR A OG1 1 
ATOM   1955 C CG2 . THR A 1 330 ? 150.596 149.984 144.919 1.00 22.42  ? 330 THR A CG2 1 
ATOM   1956 N N   . ASN A 1 331 ? 151.431 152.821 147.347 1.00 43.47  ? 331 ASN A N   1 
ATOM   1957 C CA  . ASN A 1 331 ? 152.411 152.949 148.462 1.00 46.49  ? 331 ASN A CA  1 
ATOM   1958 C C   . ASN A 1 331 ? 151.740 153.637 149.656 1.00 49.15  ? 331 ASN A C   1 
ATOM   1959 O O   . ASN A 1 331 ? 152.374 153.693 150.730 1.00 58.19  ? 331 ASN A O   1 
ATOM   1960 C CB  . ASN A 1 331 ? 153.676 153.684 148.032 1.00 46.71  ? 331 ASN A CB  1 
ATOM   1961 C CG  . ASN A 1 331 ? 153.451 154.520 146.797 1.00 44.17  ? 331 ASN A CG  1 
ATOM   1962 O OD1 . ASN A 1 331 ? 152.466 155.260 146.725 1.00 44.32  ? 331 ASN A OD1 1 
ATOM   1963 N ND2 . ASN A 1 331 ? 154.325 154.394 145.810 1.00 50.14  ? 331 ASN A ND2 1 
ATOM   1964 N N   . ILE A 1 332 ? 150.511 154.137 149.484 1.00 46.87  ? 332 ILE A N   1 
ATOM   1965 C CA  . ILE A 1 332 ? 149.780 154.730 150.645 1.00 52.53  ? 332 ILE A CA  1 
ATOM   1966 C C   . ILE A 1 332 ? 149.409 153.569 151.580 1.00 64.99  ? 332 ILE A C   1 
ATOM   1967 O O   . ILE A 1 332 ? 149.515 152.407 151.125 1.00 63.18  ? 332 ILE A O   1 
ATOM   1968 C CB  . ILE A 1 332 ? 148.536 155.508 150.184 1.00 50.87  ? 332 ILE A CB  1 
ATOM   1969 C CG1 . ILE A 1 332 ? 148.074 156.518 151.234 1.00 51.97  ? 332 ILE A CG1 1 
ATOM   1970 C CG2 . ILE A 1 332 ? 147.414 154.547 149.794 1.00 54.67  ? 332 ILE A CG2 1 
ATOM   1971 C CD1 . ILE A 1 332 ? 149.159 157.474 151.696 1.00 46.53  ? 332 ILE A CD1 1 
ATOM   1972 N N   . LYS A 1 333 ? 149.007 153.860 152.823 1.00 65.24  ? 333 LYS A N   1 
ATOM   1973 C CA  . LYS A 1 333 ? 148.721 152.789 153.819 1.00 63.67  ? 333 LYS A CA  1 
ATOM   1974 C C   . LYS A 1 333 ? 150.066 152.182 154.246 1.00 56.01  ? 333 LYS A C   1 
ATOM   1975 O O   . LYS A 1 333 ? 150.288 152.042 155.465 1.00 59.54  ? 333 LYS A O   1 
ATOM   1976 C CB  . LYS A 1 333 ? 147.754 151.719 153.295 1.00 66.91  ? 333 LYS A CB  1 
ATOM   1977 C CG  . LYS A 1 333 ? 146.382 152.221 152.867 1.00 68.16  ? 333 LYS A CG  1 
ATOM   1978 C CD  . LYS A 1 333 ? 145.539 152.742 154.024 1.00 65.08  ? 333 LYS A CD  1 
ATOM   1979 C CE  . LYS A 1 333 ? 145.323 151.709 155.085 1.00 71.21  ? 333 LYS A CE  1 
ATOM   1980 N NZ  . LYS A 1 333 ? 144.477 152.218 156.167 1.00 76.48  ? 333 LYS A NZ  1 
ATOM   1981 N N   . HIS A 1 334 ? 150.922 151.826 153.284 1.00 49.09  ? 334 HIS A N   1 
ATOM   1982 C CA  . HIS A 1 334 ? 152.282 151.344 153.640 1.00 54.20  ? 334 HIS A CA  1 
ATOM   1983 C C   . HIS A 1 334 ? 152.932 152.437 154.490 1.00 59.63  ? 334 HIS A C   1 
ATOM   1984 O O   . HIS A 1 334 ? 153.961 152.176 155.150 1.00 62.01  ? 334 HIS A O   1 
ATOM   1985 C CB  . HIS A 1 334 ? 153.216 151.144 152.442 1.00 48.35  ? 334 HIS A CB  1 
ATOM   1986 C CG  . HIS A 1 334 ? 152.764 150.127 151.446 1.00 54.71  ? 334 HIS A CG  1 
ATOM   1987 N ND1 . HIS A 1 334 ? 151.433 149.812 151.281 1.00 52.30  ? 334 HIS A ND1 1 
ATOM   1988 C CD2 . HIS A 1 334 ? 153.435 149.366 150.572 1.00 60.32  ? 334 HIS A CD2 1 
ATOM   1989 C CE1 . HIS A 1 334 ? 151.314 148.900 150.326 1.00 62.39  ? 334 HIS A CE1 1 
ATOM   1990 N NE2 . HIS A 1 334 ? 152.518 148.615 149.881 1.00 67.08  ? 334 HIS A NE2 1 
ATOM   1991 N N   . PHE A 1 335 ? 152.386 153.665 154.443 1.00 56.98  ? 335 PHE A N   1 
ATOM   1992 C CA  . PHE A 1 335 ? 152.887 154.806 155.258 1.00 58.11  ? 335 PHE A CA  1 
ATOM   1993 C C   . PHE A 1 335 ? 151.992 155.035 156.492 1.00 60.54  ? 335 PHE A C   1 
ATOM   1994 O O   . PHE A 1 335 ? 152.137 156.117 157.102 1.00 64.75  ? 335 PHE A O   1 
ATOM   1995 C CB  . PHE A 1 335 ? 152.959 156.074 154.397 1.00 50.60  ? 335 PHE A CB  1 
ATOM   1996 C CG  . PHE A 1 335 ? 154.152 156.158 153.454 1.00 46.70  ? 335 PHE A CG  1 
ATOM   1997 C CD1 . PHE A 1 335 ? 155.415 156.496 153.929 1.00 43.94  ? 335 PHE A CD1 1 
ATOM   1998 C CD2 . PHE A 1 335 ? 153.998 155.951 152.088 1.00 46.99  ? 335 PHE A CD2 1 
ATOM   1999 C CE1 . PHE A 1 335 ? 156.497 156.583 153.067 1.00 39.43  ? 335 PHE A CE1 1 
ATOM   2000 C CE2 . PHE A 1 335 ? 155.083 156.045 151.230 1.00 46.06  ? 335 PHE A CE2 1 
ATOM   2001 C CZ  . PHE A 1 335 ? 156.328 156.362 151.720 1.00 40.24  ? 335 PHE A CZ  1 
ATOM   2002 N N   . LYS A 1 336 ? 151.102 154.103 156.868 1.00 61.74  ? 336 LYS A N   1 
ATOM   2003 C CA  . LYS A 1 336 ? 150.321 154.263 158.086 1.00 68.75  ? 336 LYS A CA  1 
ATOM   2004 C C   . LYS A 1 336 ? 151.221 154.115 159.306 1.00 72.56  ? 336 LYS A C   1 
ATOM   2005 O O   . LYS A 1 336 ? 151.975 153.143 159.420 1.00 76.35  ? 336 LYS A O   1 
ATOM   2006 C CB  . LYS A 1 336 ? 149.190 153.238 158.132 1.00 74.49  ? 336 LYS A CB  1 
ATOM   2007 C CG  . LYS A 1 336 ? 148.369 153.283 159.408 1.00 78.76  ? 336 LYS A CG  1 
ATOM   2008 C CD  . LYS A 1 336 ? 147.355 154.413 159.371 1.00 81.38  ? 336 LYS A CD  1 
ATOM   2009 C CE  . LYS A 1 336 ? 146.211 154.098 158.421 1.00 88.06  ? 336 LYS A CE  1 
ATOM   2010 N NZ  . LYS A 1 336 ? 145.153 155.145 158.462 1.00 80.63  ? 336 LYS A NZ  1 
ATOM   2011 N N   . ASN A 1 337 ? 151.145 155.089 160.211 1.00 69.94  ? 337 ASN A N   1 
ATOM   2012 C CA  . ASN A 1 337 ? 151.962 155.146 161.421 1.00 75.11  ? 337 ASN A CA  1 
ATOM   2013 C C   . ASN A 1 337 ? 153.457 155.151 161.118 1.00 74.65  ? 337 ASN A C   1 
ATOM   2014 O O   . ASN A 1 337 ? 154.269 154.809 161.983 1.00 75.13  ? 337 ASN A O   1 
ATOM   2015 C CB  . ASN A 1 337 ? 151.623 153.998 162.379 1.00 84.07  ? 337 ASN A CB  1 
ATOM   2016 C CG  . ASN A 1 337 ? 151.433 154.471 163.807 1.00 88.02  ? 337 ASN A CG  1 
ATOM   2017 O OD1 . ASN A 1 337 ? 152.086 155.416 164.250 1.00 79.61  ? 337 ASN A OD1 1 
ATOM   2018 N ND2 . ASN A 1 337 ? 150.534 153.818 164.537 1.00 98.73  ? 337 ASN A ND2 1 
ATOM   2019 N N   . CYS A 1 338 ? 153.839 155.535 159.902 1.00 70.22  ? 338 CYS A N   1 
ATOM   2020 C CA  . CYS A 1 338 ? 155.246 155.617 159.517 1.00 63.14  ? 338 CYS A CA  1 
ATOM   2021 C C   . CYS A 1 338 ? 155.785 156.952 160.014 1.00 55.94  ? 338 CYS A C   1 
ATOM   2022 O O   . CYS A 1 338 ? 155.499 158.003 159.437 1.00 59.29  ? 338 CYS A O   1 
ATOM   2023 C CB  . CYS A 1 338 ? 155.397 155.482 158.006 1.00 62.72  ? 338 CYS A CB  1 
ATOM   2024 S SG  . CYS A 1 338 ? 155.534 153.781 157.398 1.00 71.46  ? 338 CYS A SG  1 
ATOM   2025 N N   . THR A 1 339 ? 156.570 156.918 161.090 1.00 54.77  ? 339 THR A N   1 
ATOM   2026 C CA  . THR A 1 339 ? 157.022 158.147 161.735 1.00 49.19  ? 339 THR A CA  1 
ATOM   2027 C C   . THR A 1 339 ? 158.295 158.694 161.095 1.00 42.46  ? 339 THR A C   1 
ATOM   2028 O O   . THR A 1 339 ? 158.306 159.819 160.587 1.00 49.25  ? 339 THR A O   1 
ATOM   2029 C CB  . THR A 1 339 ? 157.235 157.907 163.233 1.00 59.75  ? 339 THR A CB  1 
ATOM   2030 O OG1 . THR A 1 339 ? 155.964 157.822 163.887 1.00 68.75  ? 339 THR A OG1 1 
ATOM   2031 C CG2 . THR A 1 339 ? 158.034 159.045 163.848 1.00 50.25  ? 339 THR A CG2 1 
ATOM   2032 N N   . SER A 1 340 ? 159.370 157.914 161.107 1.00 42.38  ? 340 SER A N   1 
ATOM   2033 C CA  . SER A 1 340 ? 160.658 158.348 160.573 1.00 40.56  ? 340 SER A CA  1 
ATOM   2034 C C   . SER A 1 340 ? 160.837 157.725 159.195 1.00 43.68  ? 340 SER A C   1 
ATOM   2035 O O   . SER A 1 340 ? 161.285 156.583 159.072 1.00 55.77  ? 340 SER A O   1 
ATOM   2036 C CB  . SER A 1 340 ? 161.796 157.962 161.511 1.00 47.48  ? 340 SER A CB  1 
ATOM   2037 O OG  . SER A 1 340 ? 163.046 158.018 160.845 1.00 30.53  ? 340 SER A OG  1 
ATOM   2038 N N   . ILE A 1 341 ? 160.489 158.492 158.153 1.00 34.93  ? 341 ILE A N   1 
ATOM   2039 C CA  . ILE A 1 341 ? 160.624 158.028 156.739 1.00 39.19  ? 341 ILE A CA  1 
ATOM   2040 C C   . ILE A 1 341 ? 162.122 157.901 156.433 1.00 44.51  ? 341 ILE A C   1 
ATOM   2041 O O   . ILE A 1 341 ? 162.814 158.933 156.532 1.00 38.68  ? 341 ILE A O   1 
ATOM   2042 C CB  . ILE A 1 341 ? 159.892 158.994 155.786 1.00 33.76  ? 341 ILE A CB  1 
ATOM   2043 C CG1 . ILE A 1 341 ? 158.393 158.687 155.706 1.00 35.39  ? 341 ILE A CG1 1 
ATOM   2044 C CG2 . ILE A 1 341 ? 160.522 159.000 154.392 1.00 37.54  ? 341 ILE A CG2 1 
ATOM   2045 C CD1 . ILE A 1 341 ? 157.720 158.433 157.043 1.00 43.74  ? 341 ILE A CD1 1 
ATOM   2046 N N   . SER A 1 342 ? 162.604 156.709 156.065 1.00 55.79  ? 342 SER A N   1 
ATOM   2047 C CA  . SER A 1 342 ? 164.018 156.452 155.826 1.00 57.36  ? 342 SER A CA  1 
ATOM   2048 C C   . SER A 1 342 ? 164.485 156.932 154.461 1.00 58.26  ? 342 SER A C   1 
ATOM   2049 O O   . SER A 1 342 ? 165.683 156.848 154.170 1.00 67.59  ? 342 SER A O   1 
ATOM   2050 C CB  . SER A 1 342 ? 164.319 154.959 155.972 1.00 52.79  ? 342 SER A CB  1 
ATOM   2051 O OG  . SER A 1 342 ? 165.693 154.743 156.239 1.00 55.45  ? 342 SER A OG  1 
ATOM   2052 N N   . GLY A 1 343 ? 163.547 157.404 153.638 1.00 50.54  ? 343 GLY A N   1 
ATOM   2053 C CA  . GLY A 1 343 ? 163.897 157.888 152.290 1.00 50.54  ? 343 GLY A CA  1 
ATOM   2054 C C   . GLY A 1 343 ? 163.505 159.340 152.116 1.00 55.41  ? 343 GLY A C   1 
ATOM   2055 O O   . GLY A 1 343 ? 163.839 160.152 153.005 1.00 52.74  ? 343 GLY A O   1 
ATOM   2056 N N   . ASP A 1 344 ? 162.839 159.653 151.000 1.00 57.68  ? 344 ASP A N   1 
ATOM   2057 C CA  . ASP A 1 344 ? 162.432 161.052 150.693 1.00 44.85  ? 344 ASP A CA  1 
ATOM   2058 C C   . ASP A 1 344 ? 161.046 161.025 150.042 1.00 42.01  ? 344 ASP A C   1 
ATOM   2059 O O   . ASP A 1 344 ? 160.940 160.536 148.896 1.00 43.65  ? 344 ASP A O   1 
ATOM   2060 C CB  . ASP A 1 344 ? 163.485 161.757 149.852 1.00 42.39  ? 344 ASP A CB  1 
ATOM   2061 C CG  . ASP A 1 344 ? 164.239 160.878 148.863 1.00 47.16  ? 344 ASP A CG  1 
ATOM   2062 O OD1 . ASP A 1 344 ? 163.946 159.667 148.805 1.00 57.55  ? 344 ASP A OD1 1 
ATOM   2063 O OD2 . ASP A 1 344 ? 165.123 161.411 148.163 1.00 48.54  ? 344 ASP A OD2 1 
ATOM   2064 N N   . LEU A 1 345 ? 160.027 161.529 150.742 1.00 36.08  ? 345 LEU A N   1 
ATOM   2065 C CA  . LEU A 1 345 ? 158.631 161.506 150.229 1.00 30.16  ? 345 LEU A CA  1 
ATOM   2066 C C   . LEU A 1 345 ? 158.561 162.287 148.909 1.00 29.82  ? 345 LEU A C   1 
ATOM   2067 O O   . LEU A 1 345 ? 159.303 163.288 148.786 1.00 30.14  ? 345 LEU A O   1 
ATOM   2068 C CB  . LEU A 1 345 ? 157.688 162.079 151.286 1.00 29.71  ? 345 LEU A CB  1 
ATOM   2069 C CG  . LEU A 1 345 ? 157.618 161.309 152.610 1.00 29.95  ? 345 LEU A CG  1 
ATOM   2070 C CD1 . LEU A 1 345 ? 156.475 161.832 153.455 1.00 29.39  ? 345 LEU A CD1 1 
ATOM   2071 C CD2 . LEU A 1 345 ? 157.494 159.806 152.403 1.00 37.76  ? 345 LEU A CD2 1 
ATOM   2072 N N   . HIS A 1 346 ? 157.713 161.855 147.968 1.00 31.82  ? 346 HIS A N   1 
ATOM   2073 C CA  . HIS A 1 346 ? 157.600 162.490 146.625 1.00 28.21  ? 346 HIS A CA  1 
ATOM   2074 C C   . HIS A 1 346 ? 156.140 162.856 146.331 1.00 23.76  ? 346 HIS A C   1 
ATOM   2075 O O   . HIS A 1 346 ? 155.594 162.418 145.300 1.00 30.19  ? 346 HIS A O   1 
ATOM   2076 C CB  . HIS A 1 346 ? 158.177 161.550 145.560 1.00 34.06  ? 346 HIS A CB  1 
ATOM   2077 C CG  . HIS A 1 346 ? 159.644 161.687 145.349 1.00 29.77  ? 346 HIS A CG  1 
ATOM   2078 N ND1 . HIS A 1 346 ? 160.598 161.043 146.106 1.00 26.44  ? 346 HIS A ND1 1 
ATOM   2079 C CD2 . HIS A 1 346 ? 160.311 162.412 144.447 1.00 32.21  ? 346 HIS A CD2 1 
ATOM   2080 C CE1 . HIS A 1 346 ? 161.801 161.375 145.662 1.00 27.93  ? 346 HIS A CE1 1 
ATOM   2081 N NE2 . HIS A 1 346 ? 161.648 162.202 144.651 1.00 28.39  ? 346 HIS A NE2 1 
ATOM   2082 N N   . ILE A 1 347 ? 155.510 163.654 147.194 1.00 23.37  ? 347 ILE A N   1 
ATOM   2083 C CA  . ILE A 1 347 ? 154.122 164.131 146.912 1.00 20.63  ? 347 ILE A CA  1 
ATOM   2084 C C   . ILE A 1 347 ? 154.163 164.759 145.512 1.00 20.33  ? 347 ILE A C   1 
ATOM   2085 O O   . ILE A 1 347 ? 154.911 165.743 145.367 1.00 23.18  ? 347 ILE A O   1 
ATOM   2086 C CB  . ILE A 1 347 ? 153.627 165.111 147.992 1.00 19.70  ? 347 ILE A CB  1 
ATOM   2087 C CG1 . ILE A 1 347 ? 153.250 164.381 149.283 1.00 23.54  ? 347 ILE A CG1 1 
ATOM   2088 C CG2 . ILE A 1 347 ? 152.467 165.960 147.472 1.00 16.31  ? 347 ILE A CG2 1 
ATOM   2089 C CD1 . ILE A 1 347 ? 154.413 164.110 150.219 1.00 24.13  ? 347 ILE A CD1 1 
ATOM   2090 N N   . LEU A 1 348 ? 153.436 164.215 144.526 1.00 26.68  ? 348 LEU A N   1 
ATOM   2091 C CA  . LEU A 1 348 ? 153.483 164.689 143.153 1.00 24.84  ? 348 LEU A CA  1 
ATOM   2092 C C   . LEU A 1 348 ? 152.073 164.826 142.604 1.00 22.61  ? 348 LEU A C   1 
ATOM   2093 O O   . LEU A 1 348 ? 151.135 164.211 143.120 1.00 24.35  ? 348 LEU A O   1 
ATOM   2094 C CB  . LEU A 1 348 ? 154.290 163.723 142.274 1.00 27.23  ? 348 LEU A CB  1 
ATOM   2095 C CG  . LEU A 1 348 ? 155.626 164.220 141.725 1.00 27.44  ? 348 LEU A CG  1 
ATOM   2096 C CD1 . LEU A 1 348 ? 156.558 164.607 142.854 1.00 30.13  ? 348 LEU A CD1 1 
ATOM   2097 C CD2 . LEU A 1 348 ? 156.259 163.158 140.851 1.00 23.02  ? 348 LEU A CD2 1 
ATOM   2098 N N   . PRO A 1 349 ? 151.886 165.641 141.562 1.00 18.53  ? 349 PRO A N   1 
ATOM   2099 C CA  . PRO A 1 349 ? 150.562 165.709 140.925 1.00 23.99  ? 349 PRO A CA  1 
ATOM   2100 C C   . PRO A 1 349 ? 150.101 164.382 140.351 1.00 30.22  ? 349 PRO A C   1 
ATOM   2101 O O   . PRO A 1 349 ? 148.890 164.132 140.287 1.00 39.91  ? 349 PRO A O   1 
ATOM   2102 C CB  . PRO A 1 349 ? 150.756 166.764 139.826 1.00 25.69  ? 349 PRO A CB  1 
ATOM   2103 C CG  . PRO A 1 349 ? 151.936 167.560 140.265 1.00 22.99  ? 349 PRO A CG  1 
ATOM   2104 C CD  . PRO A 1 349 ? 152.834 166.591 140.958 1.00 21.14  ? 349 PRO A CD  1 
ATOM   2105 N N   . VAL A 1 350 ? 151.052 163.528 139.959 1.00 25.07  ? 350 VAL A N   1 
ATOM   2106 C CA  . VAL A 1 350 ? 150.728 162.187 139.389 1.00 22.62  ? 350 VAL A CA  1 
ATOM   2107 C C   . VAL A 1 350 ? 150.100 161.320 140.490 1.00 31.53  ? 350 VAL A C   1 
ATOM   2108 O O   . VAL A 1 350 ? 149.386 160.363 140.130 1.00 37.94  ? 350 VAL A O   1 
ATOM   2109 C CB  . VAL A 1 350 ? 151.972 161.511 138.784 1.00 21.19  ? 350 VAL A CB  1 
ATOM   2110 C CG1 . VAL A 1 350 ? 153.001 161.134 139.844 1.00 24.12  ? 350 VAL A CG1 1 
ATOM   2111 C CG2 . VAL A 1 350 ? 151.607 160.286 137.955 1.00 24.54  ? 350 VAL A CG2 1 
ATOM   2112 N N   . ALA A 1 351 ? 150.350 161.621 141.770 1.00 32.48  ? 351 ALA A N   1 
ATOM   2113 C CA  . ALA A 1 351 ? 149.735 160.865 142.855 1.00 33.34  ? 351 ALA A CA  1 
ATOM   2114 C C   . ALA A 1 351 ? 148.237 161.129 142.924 1.00 35.42  ? 351 ALA A C   1 
ATOM   2115 O O   . ALA A 1 351 ? 147.432 160.192 142.957 1.00 43.99  ? 351 ALA A O   1 
ATOM   2116 C CB  . ALA A 1 351 ? 150.402 161.218 144.183 1.00 25.32  ? 351 ALA A CB  1 
ATOM   2117 N N   . PHE A 1 352 ? 147.844 162.404 142.937 1.00 32.14  ? 352 PHE A N   1 
ATOM   2118 C CA  . PHE A 1 352 ? 146.428 162.741 143.028 1.00 31.48  ? 352 PHE A CA  1 
ATOM   2119 C C   . PHE A 1 352 ? 145.706 162.448 141.722 1.00 39.18  ? 352 PHE A C   1 
ATOM   2120 O O   . PHE A 1 352 ? 144.565 161.974 141.731 1.00 50.67  ? 352 PHE A O   1 
ATOM   2121 C CB  . PHE A 1 352 ? 146.265 164.206 143.421 1.00 31.37  ? 352 PHE A CB  1 
ATOM   2122 C CG  . PHE A 1 352 ? 146.880 164.538 144.741 1.00 30.81  ? 352 PHE A CG  1 
ATOM   2123 C CD1 . PHE A 1 352 ? 146.154 164.409 145.909 1.00 35.31  ? 352 PHE A CD1 1 
ATOM   2124 C CD2 . PHE A 1 352 ? 148.192 164.961 144.817 1.00 28.04  ? 352 PHE A CD2 1 
ATOM   2125 C CE1 . PHE A 1 352 ? 146.722 164.705 147.125 1.00 32.26  ? 352 PHE A CE1 1 
ATOM   2126 C CE2 . PHE A 1 352 ? 148.765 165.256 146.030 1.00 35.42  ? 352 PHE A CE2 1 
ATOM   2127 C CZ  . PHE A 1 352 ? 148.030 165.130 147.185 1.00 36.26  ? 352 PHE A CZ  1 
ATOM   2128 N N   . ARG A 1 353 ? 146.350 162.729 140.589 1.00 35.30  ? 353 ARG A N   1 
ATOM   2129 C CA  . ARG A 1 353 ? 145.778 162.350 139.306 1.00 31.71  ? 353 ARG A CA  1 
ATOM   2130 C C   . ARG A 1 353 ? 145.738 160.841 139.125 1.00 28.96  ? 353 ARG A C   1 
ATOM   2131 O O   . ARG A 1 353 ? 144.920 160.342 138.345 1.00 31.99  ? 353 ARG A O   1 
ATOM   2132 C CB  . ARG A 1 353 ? 146.574 162.990 138.170 1.00 34.78  ? 353 ARG A CB  1 
ATOM   2133 C CG  . ARG A 1 353 ? 145.901 162.919 136.813 1.00 34.89  ? 353 ARG A CG  1 
ATOM   2134 C CD  . ARG A 1 353 ? 146.920 163.085 135.702 1.00 38.57  ? 353 ARG A CD  1 
ATOM   2135 N NE  . ARG A 1 353 ? 148.125 163.759 136.171 1.00 37.39  ? 353 ARG A NE  1 
ATOM   2136 C CZ  . ARG A 1 353 ? 149.342 163.237 136.120 1.00 40.25  ? 353 ARG A CZ  1 
ATOM   2137 N NH1 . ARG A 1 353 ? 149.557 162.030 135.624 1.00 38.02  ? 353 ARG A NH1 1 
ATOM   2138 N NH2 . ARG A 1 353 ? 150.370 163.945 136.578 1.00 41.50  ? 353 ARG A NH2 1 
ATOM   2139 N N   . GLY A 1 354 ? 146.636 160.124 139.803 1.00 31.70  ? 354 GLY A N   1 
ATOM   2140 C CA  . GLY A 1 354 ? 146.717 158.663 139.610 1.00 39.62  ? 354 GLY A CA  1 
ATOM   2141 C C   . GLY A 1 354 ? 147.519 158.343 138.364 1.00 37.05  ? 354 GLY A C   1 
ATOM   2142 O O   . GLY A 1 354 ? 147.589 159.208 137.470 1.00 44.09  ? 354 GLY A O   1 
ATOM   2143 N N   . ASP A 1 355 ? 148.122 157.155 138.304 1.00 29.34  ? 355 ASP A N   1 
ATOM   2144 C CA  . ASP A 1 355 ? 148.985 156.803 137.144 1.00 27.42  ? 355 ASP A CA  1 
ATOM   2145 C C   . ASP A 1 355 ? 148.501 155.483 136.539 1.00 31.17  ? 355 ASP A C   1 
ATOM   2146 O O   . ASP A 1 355 ? 148.329 154.507 137.298 1.00 38.11  ? 355 ASP A O   1 
ATOM   2147 C CB  . ASP A 1 355 ? 150.451 156.761 137.539 1.00 32.84  ? 355 ASP A CB  1 
ATOM   2148 C CG  . ASP A 1 355 ? 151.441 156.624 136.392 1.00 43.83  ? 355 ASP A CG  1 
ATOM   2149 O OD1 . ASP A 1 355 ? 150.994 156.590 135.226 1.00 47.36  ? 355 ASP A OD1 1 
ATOM   2150 O OD2 . ASP A 1 355 ? 152.654 156.551 136.677 1.00 45.12  ? 355 ASP A OD2 1 
ATOM   2151 N N   . SER A 1 356 ? 148.294 155.462 135.222 1.00 26.78  ? 356 SER A N   1 
ATOM   2152 C CA  . SER A 1 356 ? 147.818 154.232 134.541 1.00 20.35  ? 356 SER A CA  1 
ATOM   2153 C C   . SER A 1 356 ? 148.988 153.255 134.368 1.00 20.93  ? 356 SER A C   1 
ATOM   2154 O O   . SER A 1 356 ? 148.801 152.055 134.661 1.00 26.55  ? 356 SER A O   1 
ATOM   2155 C CB  . SER A 1 356 ? 147.188 154.564 133.218 1.00 26.01  ? 356 SER A CB  1 
ATOM   2156 O OG  . SER A 1 356 ? 148.116 155.236 132.377 1.00 27.42  ? 356 SER A OG  1 
ATOM   2157 N N   . PHE A 1 357 ? 150.155 153.752 133.950 1.00 26.56  ? 357 PHE A N   1 
ATOM   2158 C CA  . PHE A 1 357 ? 151.308 152.849 133.671 1.00 23.97  ? 357 PHE A CA  1 
ATOM   2159 C C   . PHE A 1 357 ? 151.657 152.063 134.928 1.00 32.75  ? 357 PHE A C   1 
ATOM   2160 O O   . PHE A 1 357 ? 151.855 150.837 134.840 1.00 49.40  ? 357 PHE A O   1 
ATOM   2161 C CB  . PHE A 1 357 ? 152.533 153.595 133.131 1.00 16.41  ? 357 PHE A CB  1 
ATOM   2162 C CG  . PHE A 1 357 ? 153.792 152.741 133.077 1.00 15.03  ? 357 PHE A CG  1 
ATOM   2163 C CD1 . PHE A 1 357 ? 154.002 151.849 132.033 1.00 22.26  ? 357 PHE A CD1 1 
ATOM   2164 C CD2 . PHE A 1 357 ? 154.768 152.843 134.061 1.00 26.04  ? 357 PHE A CD2 1 
ATOM   2165 C CE1 . PHE A 1 357 ? 155.146 151.071 131.988 1.00 23.82  ? 357 PHE A CE1 1 
ATOM   2166 C CE2 . PHE A 1 357 ? 155.912 152.065 134.007 1.00 23.37  ? 357 PHE A CE2 1 
ATOM   2167 C CZ  . PHE A 1 357 ? 156.100 151.183 132.971 1.00 22.92  ? 357 PHE A CZ  1 
ATOM   2168 N N   . THR A 1 358 ? 151.742 152.744 136.067 1.00 32.00  ? 358 THR A N   1 
ATOM   2169 C CA  . THR A 1 358 ? 152.148 152.056 137.313 1.00 36.05  ? 358 THR A CA  1 
ATOM   2170 C C   . THR A 1 358 ? 150.941 151.402 137.957 1.00 37.41  ? 358 THR A C   1 
ATOM   2171 O O   . THR A 1 358 ? 151.080 150.929 139.104 1.00 42.20  ? 358 THR A O   1 
ATOM   2172 C CB  . THR A 1 358 ? 152.828 153.052 138.249 1.00 38.90  ? 358 THR A CB  1 
ATOM   2173 O OG1 . THR A 1 358 ? 151.824 154.006 138.577 1.00 46.75  ? 358 THR A OG1 1 
ATOM   2174 C CG2 . THR A 1 358 ? 154.008 153.748 137.597 1.00 38.91  ? 358 THR A CG2 1 
ATOM   2175 N N   . HIS A 1 359 ? 149.797 151.328 137.267 1.00 35.89  ? 359 HIS A N   1 
ATOM   2176 C CA  . HIS A 1 359 ? 148.593 150.601 137.758 1.00 34.06  ? 359 HIS A CA  1 
ATOM   2177 C C   . HIS A 1 359 ? 148.206 151.075 139.162 1.00 36.61  ? 359 HIS A C   1 
ATOM   2178 O O   . HIS A 1 359 ? 148.127 150.219 140.073 1.00 46.93  ? 359 HIS A O   1 
ATOM   2179 C CB  . HIS A 1 359 ? 148.848 149.088 137.733 1.00 35.22  ? 359 HIS A CB  1 
ATOM   2180 C CG  . HIS A 1 359 ? 149.560 148.602 136.514 1.00 37.74  ? 359 HIS A CG  1 
ATOM   2181 N ND1 . HIS A 1 359 ? 150.558 147.653 136.585 1.00 43.99  ? 359 HIS A ND1 1 
ATOM   2182 C CD2 . HIS A 1 359 ? 149.464 148.939 135.224 1.00 35.07  ? 359 HIS A CD2 1 
ATOM   2183 C CE1 . HIS A 1 359 ? 151.027 147.418 135.369 1.00 40.97  ? 359 HIS A CE1 1 
ATOM   2184 N NE2 . HIS A 1 359 ? 150.378 148.190 134.528 1.00 38.69  ? 359 HIS A NE2 1 
ATOM   2185 N N   . THR A 1 360 ? 147.963 152.375 139.350 1.00 34.22  ? 360 THR A N   1 
ATOM   2186 C CA  . THR A 1 360 ? 147.527 152.938 140.650 1.00 34.32  ? 360 THR A CA  1 
ATOM   2187 C C   . THR A 1 360 ? 146.350 153.870 140.409 1.00 38.71  ? 360 THR A C   1 
ATOM   2188 O O   . THR A 1 360 ? 146.408 154.655 139.439 1.00 39.81  ? 360 THR A O   1 
ATOM   2189 C CB  . THR A 1 360 ? 148.707 153.622 141.345 1.00 33.74  ? 360 THR A CB  1 
ATOM   2190 O OG1 . THR A 1 360 ? 148.230 153.918 142.654 1.00 35.90  ? 360 THR A OG1 1 
ATOM   2191 C CG2 . THR A 1 360 ? 149.173 154.892 140.654 1.00 33.73  ? 360 THR A CG2 1 
ATOM   2192 N N   . PRO A 1 361 ? 145.269 153.813 141.222 1.00 36.39  ? 361 PRO A N   1 
ATOM   2193 C CA  . PRO A 1 361 ? 144.140 154.722 141.070 1.00 33.68  ? 361 PRO A CA  1 
ATOM   2194 C C   . PRO A 1 361 ? 144.386 156.080 141.719 1.00 39.30  ? 361 PRO A C   1 
ATOM   2195 O O   . PRO A 1 361 ? 145.343 156.201 142.511 1.00 37.56  ? 361 PRO A O   1 
ATOM   2196 C CB  . PRO A 1 361 ? 143.022 153.938 141.764 1.00 42.01  ? 361 PRO A CB  1 
ATOM   2197 C CG  . PRO A 1 361 ? 143.734 153.250 142.902 1.00 46.09  ? 361 PRO A CG  1 
ATOM   2198 C CD  . PRO A 1 361 ? 145.077 152.863 142.311 1.00 41.37  ? 361 PRO A CD  1 
ATOM   2199 N N   . PRO A 1 362 ? 143.578 157.125 141.422 1.00 42.78  ? 362 PRO A N   1 
ATOM   2200 C CA  . PRO A 1 362 ? 143.835 158.463 141.965 1.00 39.68  ? 362 PRO A CA  1 
ATOM   2201 C C   . PRO A 1 362 ? 143.832 158.447 143.486 1.00 42.41  ? 362 PRO A C   1 
ATOM   2202 O O   . PRO A 1 362 ? 143.026 157.760 144.118 1.00 52.43  ? 362 PRO A O   1 
ATOM   2203 C CB  . PRO A 1 362 ? 142.682 159.306 141.405 1.00 36.08  ? 362 PRO A CB  1 
ATOM   2204 C CG  . PRO A 1 362 ? 141.664 158.323 140.923 1.00 44.89  ? 362 PRO A CG  1 
ATOM   2205 C CD  . PRO A 1 362 ? 142.428 157.113 140.505 1.00 44.85  ? 362 PRO A CD  1 
ATOM   2206 N N   . LEU A 1 363 ? 144.782 159.191 144.065 1.00 44.62  ? 363 LEU A N   1 
ATOM   2207 C CA  . LEU A 1 363 ? 144.923 159.226 145.544 1.00 52.93  ? 363 LEU A CA  1 
ATOM   2208 C C   . LEU A 1 363 ? 143.817 160.090 146.155 1.00 60.72  ? 363 LEU A C   1 
ATOM   2209 O O   . LEU A 1 363 ? 143.676 161.260 145.739 1.00 57.55  ? 363 LEU A O   1 
ATOM   2210 C CB  . LEU A 1 363 ? 146.303 159.758 145.928 1.00 49.70  ? 363 LEU A CB  1 
ATOM   2211 C CG  . LEU A 1 363 ? 146.547 159.978 147.424 1.00 39.31  ? 363 LEU A CG  1 
ATOM   2212 C CD1 . LEU A 1 363 ? 146.571 158.658 148.172 1.00 48.14  ? 363 LEU A CD1 1 
ATOM   2213 C CD2 . LEU A 1 363 ? 147.837 160.744 147.644 1.00 38.26  ? 363 LEU A CD2 1 
ATOM   2214 N N   . ASP A 1 364 ? 143.068 159.529 147.101 1.00 63.84  ? 364 ASP A N   1 
ATOM   2215 C CA  . ASP A 1 364 ? 142.027 160.270 147.796 1.00 61.74  ? 364 ASP A CA  1 
ATOM   2216 C C   . ASP A 1 364 ? 142.666 161.315 148.703 1.00 61.94  ? 364 ASP A C   1 
ATOM   2217 O O   . ASP A 1 364 ? 143.581 160.986 149.467 1.00 64.81  ? 364 ASP A O   1 
ATOM   2218 C CB  . ASP A 1 364 ? 141.147 159.326 148.610 1.00 62.21  ? 364 ASP A CB  1 
ATOM   2219 C CG  . ASP A 1 364 ? 139.737 159.852 148.787 1.00 74.53  ? 364 ASP A CG  1 
ATOM   2220 O OD1 . ASP A 1 364 ? 139.112 160.232 147.774 1.00 85.20  ? 364 ASP A OD1 1 
ATOM   2221 O OD2 . ASP A 1 364 ? 139.253 159.886 149.938 1.00 73.60  ? 364 ASP A OD2 1 
ATOM   2222 N N   . PRO A 1 365 ? 142.234 162.576 148.639 1.00 54.24  ? 365 PRO A N   1 
ATOM   2223 C CA  . PRO A 1 365 ? 142.815 163.591 149.531 1.00 48.39  ? 365 PRO A CA  1 
ATOM   2224 C C   . PRO A 1 365 ? 142.681 163.249 151.002 1.00 54.20  ? 365 PRO A C   1 
ATOM   2225 O O   . PRO A 1 365 ? 143.551 163.623 151.796 1.00 55.88  ? 365 PRO A O   1 
ATOM   2226 C CB  . PRO A 1 365 ? 142.029 164.858 149.170 1.00 46.84  ? 365 PRO A CB  1 
ATOM   2227 C CG  . PRO A 1 365 ? 141.593 164.636 147.764 1.00 46.17  ? 365 PRO A CG  1 
ATOM   2228 C CD  . PRO A 1 365 ? 141.309 163.165 147.657 1.00 57.57  ? 365 PRO A CD  1 
ATOM   2229 N N   . GLN A 1 366 ? 141.614 162.549 151.392 1.00 61.27  ? 366 GLN A N   1 
ATOM   2230 C CA  . GLN A 1 366 ? 141.465 162.138 152.783 1.00 64.12  ? 366 GLN A CA  1 
ATOM   2231 C C   . GLN A 1 366 ? 142.488 161.085 153.186 1.00 61.71  ? 366 GLN A C   1 
ATOM   2232 O O   . GLN A 1 366 ? 142.726 160.898 154.384 1.00 61.28  ? 366 GLN A O   1 
ATOM   2233 C CB  . GLN A 1 366 ? 140.049 161.616 153.027 1.00 63.62  ? 366 GLN A CB  1 
ATOM   2234 C CG  . GLN A 1 366 ? 138.964 162.406 152.310 1.00 61.80  ? 366 GLN A CG  1 
ATOM   2235 C CD  . GLN A 1 366 ? 138.579 163.680 153.040 1.00 66.38  ? 366 GLN A CD  1 
ATOM   2236 O OE1 . GLN A 1 366 ? 139.286 164.135 153.939 1.00 72.74  ? 366 GLN A OE1 1 
ATOM   2237 N NE2 . GLN A 1 366 ? 137.452 164.264 152.652 1.00 62.37  ? 366 GLN A NE2 1 
ATOM   2238 N N   . GLU A 1 367 ? 143.093 160.392 152.219 1.00 58.29  ? 367 GLU A N   1 
ATOM   2239 C CA  . GLU A 1 367 ? 144.152 159.439 152.525 1.00 55.24  ? 367 GLU A CA  1 
ATOM   2240 C C   . GLU A 1 367 ? 145.467 160.120 152.873 1.00 47.84  ? 367 GLU A C   1 
ATOM   2241 O O   . GLU A 1 367 ? 146.388 159.444 153.343 1.00 46.20  ? 367 GLU A O   1 
ATOM   2242 C CB  . GLU A 1 367 ? 144.362 158.487 151.347 1.00 54.72  ? 367 GLU A CB  1 
ATOM   2243 C CG  . GLU A 1 367 ? 143.670 157.143 151.500 1.00 67.00  ? 367 GLU A CG  1 
ATOM   2244 C CD  . GLU A 1 367 ? 143.702 156.323 150.225 1.00 78.06  ? 367 GLU A CD  1 
ATOM   2245 O OE1 . GLU A 1 367 ? 143.011 156.702 149.256 1.00 82.00  ? 367 GLU A OE1 1 
ATOM   2246 O OE2 . GLU A 1 367 ? 144.415 155.298 150.192 1.00 75.01  ? 367 GLU A OE2 1 
ATOM   2247 N N   . LEU A 1 368 ? 145.579 161.431 152.649 1.00 48.04  ? 368 LEU A N   1 
ATOM   2248 C CA  . LEU A 1 368 ? 146.799 162.149 152.993 1.00 51.78  ? 368 LEU A CA  1 
ATOM   2249 C C   . LEU A 1 368 ? 147.004 162.254 154.496 1.00 48.47  ? 368 LEU A C   1 
ATOM   2250 O O   . LEU A 1 368 ? 148.131 162.499 154.937 1.00 47.59  ? 368 LEU A O   1 
ATOM   2251 C CB  . LEU A 1 368 ? 146.780 163.549 152.382 1.00 48.29  ? 368 LEU A CB  1 
ATOM   2252 C CG  . LEU A 1 368 ? 147.196 163.674 150.918 1.00 35.71  ? 368 LEU A CG  1 
ATOM   2253 C CD1 . LEU A 1 368 ? 147.475 165.124 150.598 1.00 30.88  ? 368 LEU A CD1 1 
ATOM   2254 C CD2 . LEU A 1 368 ? 148.411 162.816 150.623 1.00 30.08  ? 368 LEU A CD2 1 
ATOM   2255 N N   . ASP A 1 369 ? 145.948 162.071 155.290 1.00 49.12  ? 369 ASP A N   1 
ATOM   2256 C CA  . ASP A 1 369 ? 146.082 162.102 156.740 1.00 49.26  ? 369 ASP A CA  1 
ATOM   2257 C C   . ASP A 1 369 ? 146.931 160.957 157.270 1.00 46.95  ? 369 ASP A C   1 
ATOM   2258 O O   . ASP A 1 369 ? 147.325 160.990 158.439 1.00 50.11  ? 369 ASP A O   1 
ATOM   2259 C CB  . ASP A 1 369 ? 144.701 162.074 157.395 1.00 60.21  ? 369 ASP A CB  1 
ATOM   2260 C CG  . ASP A 1 369 ? 143.784 163.159 156.866 1.00 64.07  ? 369 ASP A CG  1 
ATOM   2261 O OD1 . ASP A 1 369 ? 144.294 164.226 156.464 1.00 58.88  ? 369 ASP A OD1 1 
ATOM   2262 O OD2 . ASP A 1 369 ? 142.554 162.946 156.852 1.00 64.66  ? 369 ASP A OD2 1 
ATOM   2263 N N   . ILE A 1 370 ? 147.205 159.945 156.444 1.00 43.96  ? 370 ILE A N   1 
ATOM   2264 C CA  . ILE A 1 370 ? 148.144 158.896 156.828 1.00 40.59  ? 370 ILE A CA  1 
ATOM   2265 C C   . ILE A 1 370 ? 149.528 159.488 157.063 1.00 38.50  ? 370 ILE A C   1 
ATOM   2266 O O   . ILE A 1 370 ? 150.249 159.079 157.982 1.00 44.25  ? 370 ILE A O   1 
ATOM   2267 C CB  . ILE A 1 370 ? 148.163 157.792 155.754 1.00 48.71  ? 370 ILE A CB  1 
ATOM   2268 C CG1 . ILE A 1 370 ? 146.961 156.862 155.928 1.00 51.74  ? 370 ILE A CG1 1 
ATOM   2269 C CG2 . ILE A 1 370 ? 149.456 157.006 155.801 1.00 55.68  ? 370 ILE A CG2 1 
ATOM   2270 C CD1 . ILE A 1 370 ? 146.653 156.030 154.705 1.00 53.28  ? 370 ILE A CD1 1 
ATOM   2271 N N   . LEU A 1 371 ? 149.889 160.493 156.258 1.00 39.42  ? 371 LEU A N   1 
ATOM   2272 C CA  . LEU A 1 371 ? 151.229 161.126 156.353 1.00 36.42  ? 371 LEU A CA  1 
ATOM   2273 C C   . LEU A 1 371 ? 151.285 162.084 157.557 1.00 32.47  ? 371 LEU A C   1 
ATOM   2274 O O   . LEU A 1 371 ? 152.381 162.640 157.791 1.00 28.01  ? 371 LEU A O   1 
ATOM   2275 C CB  . LEU A 1 371 ? 151.536 161.860 155.047 1.00 33.08  ? 371 LEU A CB  1 
ATOM   2276 C CG  . LEU A 1 371 ? 151.555 161.008 153.773 1.00 33.20  ? 371 LEU A CG  1 
ATOM   2277 C CD1 . LEU A 1 371 ? 151.697 161.903 152.555 1.00 34.49  ? 371 LEU A CD1 1 
ATOM   2278 C CD2 . LEU A 1 371 ? 152.663 159.969 153.790 1.00 37.35  ? 371 LEU A CD2 1 
ATOM   2279 N N   . LYS A 1 372 ? 150.187 162.272 158.305 1.00 35.60  ? 372 LYS A N   1 
ATOM   2280 C CA  . LYS A 1 372 ? 150.219 163.132 159.482 1.00 36.66  ? 372 LYS A CA  1 
ATOM   2281 C C   . LYS A 1 372 ? 151.112 162.571 160.579 1.00 42.41  ? 372 LYS A C   1 
ATOM   2282 O O   . LYS A 1 372 ? 151.499 163.311 161.489 1.00 48.51  ? 372 LYS A O   1 
ATOM   2283 C CB  . LYS A 1 372 ? 148.803 163.336 160.020 1.00 36.87  ? 372 LYS A CB  1 
ATOM   2284 C CG  . LYS A 1 372 ? 148.369 164.787 160.107 1.00 41.72  ? 372 LYS A CG  1 
ATOM   2285 C CD  . LYS A 1 372 ? 146.859 164.897 160.228 1.00 43.87  ? 372 LYS A CD  1 
ATOM   2286 C CE  . LYS A 1 372 ? 146.240 165.434 158.949 1.00 42.87  ? 372 LYS A CE  1 
ATOM   2287 N NZ  . LYS A 1 372 ? 145.029 166.257 159.220 1.00 52.74  ? 372 LYS A NZ  1 
ATOM   2288 N N   . THR A 1 373 ? 151.443 161.282 160.512 1.00 41.63  ? 373 THR A N   1 
ATOM   2289 C CA  . THR A 1 373 ? 152.278 160.646 161.521 1.00 37.60  ? 373 THR A CA  1 
ATOM   2290 C C   . THR A 1 373 ? 153.757 160.977 161.365 1.00 40.32  ? 373 THR A C   1 
ATOM   2291 O O   . THR A 1 373 ? 154.517 160.810 162.325 1.00 47.87  ? 373 THR A O   1 
ATOM   2292 C CB  . THR A 1 373 ? 152.082 159.130 161.463 1.00 45.12  ? 373 THR A CB  1 
ATOM   2293 O OG1 . THR A 1 373 ? 150.708 158.837 161.185 1.00 43.20  ? 373 THR A OG1 1 
ATOM   2294 C CG2 . THR A 1 373 ? 152.463 158.492 162.779 1.00 61.46  ? 373 THR A CG2 1 
ATOM   2295 N N   . VAL A 1 374 ? 154.169 161.378 160.156 1.00 36.39  ? 374 VAL A N   1 
ATOM   2296 C CA  . VAL A 1 374 ? 155.611 161.633 159.853 1.00 32.62  ? 374 VAL A CA  1 
ATOM   2297 C C   . VAL A 1 374 ? 156.155 162.707 160.805 1.00 37.85  ? 374 VAL A C   1 
ATOM   2298 O O   . VAL A 1 374 ? 155.496 163.764 160.923 1.00 38.58  ? 374 VAL A O   1 
ATOM   2299 C CB  . VAL A 1 374 ? 155.832 162.041 158.382 1.00 28.12  ? 374 VAL A CB  1 
ATOM   2300 C CG1 . VAL A 1 374 ? 157.300 162.330 158.087 1.00 29.27  ? 374 VAL A CG1 1 
ATOM   2301 C CG2 . VAL A 1 374 ? 155.300 160.993 157.413 1.00 37.69  ? 374 VAL A CG2 1 
ATOM   2302 N N   . LYS A 1 375 ? 157.297 162.454 161.454 1.00 35.08  ? 375 LYS A N   1 
ATOM   2303 C CA  . LYS A 1 375 ? 157.961 163.442 162.343 1.00 31.73  ? 375 LYS A CA  1 
ATOM   2304 C C   . LYS A 1 375 ? 159.425 163.643 161.918 1.00 30.75  ? 375 LYS A C   1 
ATOM   2305 O O   . LYS A 1 375 ? 160.084 164.514 162.531 1.00 42.11  ? 375 LYS A O   1 
ATOM   2306 C CB  . LYS A 1 375 ? 157.864 162.972 163.798 1.00 32.57  ? 375 LYS A CB  1 
ATOM   2307 C CG  . LYS A 1 375 ? 156.441 162.754 164.287 1.00 38.59  ? 375 LYS A CG  1 
ATOM   2308 C CD  . LYS A 1 375 ? 156.264 162.889 165.794 1.00 52.15  ? 375 LYS A CD  1 
ATOM   2309 C CE  . LYS A 1 375 ? 156.494 164.277 166.307 1.00 54.75  ? 375 LYS A CE  1 
ATOM   2310 N NZ  . LYS A 1 375 ? 155.560 165.248 165.731 1.00 51.85  ? 375 LYS A NZ  1 
ATOM   2311 N N   . GLU A 1 376 ? 159.921 162.902 160.917 1.00 26.89  ? 376 GLU A N   1 
ATOM   2312 C CA  . GLU A 1 376 ? 161.304 163.030 160.484 1.00 29.56  ? 376 GLU A CA  1 
ATOM   2313 C C   . GLU A 1 376 ? 161.420 162.457 159.081 1.00 29.81  ? 376 GLU A C   1 
ATOM   2314 O O   . GLU A 1 376 ? 160.797 161.440 158.770 1.00 39.31  ? 376 GLU A O   1 
ATOM   2315 C CB  . GLU A 1 376 ? 162.265 162.308 161.436 1.00 35.54  ? 376 GLU A CB  1 
ATOM   2316 C CG  . GLU A 1 376 ? 163.715 162.301 160.971 1.00 39.63  ? 376 GLU A CG  1 
ATOM   2317 C CD  . GLU A 1 376 ? 164.571 161.298 161.720 1.00 56.40  ? 376 GLU A CD  1 
ATOM   2318 O OE1 . GLU A 1 376 ? 164.339 160.080 161.567 1.00 57.58  ? 376 GLU A OE1 1 
ATOM   2319 O OE2 . GLU A 1 376 ? 165.480 161.729 162.460 1.00 61.31  ? 376 GLU A OE2 1 
ATOM   2320 N N   . ILE A 1 377 ? 162.136 163.168 158.215 1.00 24.58  ? 377 ILE A N   1 
ATOM   2321 C CA  . ILE A 1 377 ? 162.413 162.667 156.842 1.00 31.60  ? 377 ILE A CA  1 
ATOM   2322 C C   . ILE A 1 377 ? 163.925 162.812 156.662 1.00 41.79  ? 377 ILE A C   1 
ATOM   2323 O O   . ILE A 1 377 ? 164.379 163.978 156.651 1.00 45.23  ? 377 ILE A O   1 
ATOM   2324 C CB  . ILE A 1 377 ? 161.596 163.420 155.774 1.00 25.06  ? 377 ILE A CB  1 
ATOM   2325 C CG1 . ILE A 1 377 ? 160.100 163.115 155.912 1.00 20.27  ? 377 ILE A CG1 1 
ATOM   2326 C CG2 . ILE A 1 377 ? 162.117 163.112 154.368 1.00 34.62  ? 377 ILE A CG2 1 
ATOM   2327 C CD1 . ILE A 1 377 ? 159.211 163.802 154.889 1.00 19.76  ? 377 ILE A CD1 1 
ATOM   2328 N N   . THR A 1 378 ? 164.678 161.709 156.682 1.00 39.85  ? 378 THR A N   1 
ATOM   2329 C CA  . THR A 1 378 ? 166.112 161.723 156.397 1.00 48.85  ? 378 THR A CA  1 
ATOM   2330 C C   . THR A 1 378 ? 166.340 161.768 154.883 1.00 52.58  ? 378 THR A C   1 
ATOM   2331 O O   . THR A 1 378 ? 166.952 160.890 154.275 1.00 64.22  ? 378 THR A O   1 
ATOM   2332 C CB  . THR A 1 378 ? 166.804 160.527 157.039 1.00 56.94  ? 378 THR A CB  1 
ATOM   2333 O OG1 . THR A 1 378 ? 168.116 160.375 156.484 1.00 69.13  ? 378 THR A OG1 1 
ATOM   2334 C CG2 . THR A 1 378 ? 166.014 159.259 156.810 1.00 45.85  ? 378 THR A CG2 1 
ATOM   2335 N N   . GLY A 1 379 ? 165.828 162.837 154.283 1.00 43.19  ? 379 GLY A N   1 
ATOM   2336 C CA  . GLY A 1 379 ? 165.906 163.051 152.854 1.00 46.18  ? 379 GLY A CA  1 
ATOM   2337 C C   . GLY A 1 379 ? 165.411 164.436 152.502 1.00 44.73  ? 379 GLY A C   1 
ATOM   2338 O O   . GLY A 1 379 ? 165.753 165.409 153.179 1.00 46.36  ? 379 GLY A O   1 
ATOM   2339 N N   . PHE A 1 380 ? 164.604 164.550 151.438 1.00 43.05  ? 380 PHE A N   1 
ATOM   2340 C CA  . PHE A 1 380 ? 163.973 165.839 151.042 1.00 45.08  ? 380 PHE A CA  1 
ATOM   2341 C C   . PHE A 1 380 ? 162.466 165.605 150.927 1.00 42.66  ? 380 PHE A C   1 
ATOM   2342 O O   . PHE A 1 380 ? 162.068 164.598 150.302 1.00 48.44  ? 380 PHE A O   1 
ATOM   2343 C CB  . PHE A 1 380 ? 164.547 166.398 149.733 1.00 45.89  ? 380 PHE A CB  1 
ATOM   2344 C CG  . PHE A 1 380 ? 164.242 165.627 148.455 1.00 45.46  ? 380 PHE A CG  1 
ATOM   2345 C CD1 . PHE A 1 380 ? 165.177 164.760 147.906 1.00 49.60  ? 380 PHE A CD1 1 
ATOM   2346 C CD2 . PHE A 1 380 ? 163.029 165.782 147.793 1.00 38.59  ? 380 PHE A CD2 1 
ATOM   2347 C CE1 . PHE A 1 380 ? 164.913 164.075 146.735 1.00 50.61  ? 380 PHE A CE1 1 
ATOM   2348 C CE2 . PHE A 1 380 ? 162.764 165.080 146.628 1.00 38.66  ? 380 PHE A CE2 1 
ATOM   2349 C CZ  . PHE A 1 380 ? 163.708 164.232 146.102 1.00 42.81  ? 380 PHE A CZ  1 
ATOM   2350 N N   . LEU A 1 381 ? 161.647 166.477 151.524 1.00 32.54  ? 381 LEU A N   1 
ATOM   2351 C CA  . LEU A 1 381 ? 160.168 166.380 151.402 1.00 23.73  ? 381 LEU A CA  1 
ATOM   2352 C C   . LEU A 1 381 ? 159.740 167.243 150.207 1.00 30.30  ? 381 LEU A C   1 
ATOM   2353 O O   . LEU A 1 381 ? 159.618 168.472 150.391 1.00 30.55  ? 381 LEU A O   1 
ATOM   2354 C CB  . LEU A 1 381 ? 159.458 166.820 152.682 1.00 19.82  ? 381 LEU A CB  1 
ATOM   2355 C CG  . LEU A 1 381 ? 157.936 166.982 152.581 1.00 18.86  ? 381 LEU A CG  1 
ATOM   2356 C CD1 . LEU A 1 381 ? 157.244 165.741 152.042 1.00 27.08  ? 381 LEU A CD1 1 
ATOM   2357 C CD2 . LEU A 1 381 ? 157.363 167.350 153.931 1.00 18.74  ? 381 LEU A CD2 1 
ATOM   2358 N N   . LEU A 1 382 ? 159.521 166.627 149.043 1.00 31.13  ? 382 LEU A N   1 
ATOM   2359 C CA  . LEU A 1 382 ? 159.096 167.357 147.821 1.00 30.15  ? 382 LEU A CA  1 
ATOM   2360 C C   . LEU A 1 382 ? 157.566 167.344 147.750 1.00 27.71  ? 382 LEU A C   1 
ATOM   2361 O O   . LEU A 1 382 ? 157.003 166.227 147.696 1.00 32.48  ? 382 LEU A O   1 
ATOM   2362 C CB  . LEU A 1 382 ? 159.717 166.701 146.591 1.00 25.09  ? 382 LEU A CB  1 
ATOM   2363 C CG  . LEU A 1 382 ? 159.152 167.130 145.233 1.00 22.63  ? 382 LEU A CG  1 
ATOM   2364 C CD1 . LEU A 1 382 ? 159.481 168.582 144.951 1.00 26.51  ? 382 LEU A CD1 1 
ATOM   2365 C CD2 . LEU A 1 382 ? 159.676 166.230 144.134 1.00 29.93  ? 382 LEU A CD2 1 
ATOM   2366 N N   . ILE A 1 383 ? 156.920 168.515 147.756 1.00 21.17  ? 383 ILE A N   1 
ATOM   2367 C CA  . ILE A 1 383 ? 155.470 168.606 147.651 1.00 16.70  ? 383 ILE A CA  1 
ATOM   2368 C C   . ILE A 1 383 ? 155.159 169.447 146.424 1.00 19.22  ? 383 ILE A C   1 
ATOM   2369 O O   . ILE A 1 383 ? 155.479 170.641 146.382 1.00 20.79  ? 383 ILE A O   1 
ATOM   2370 C CB  . ILE A 1 383 ? 154.844 169.213 148.912 1.00 16.09  ? 383 ILE A CB  1 
ATOM   2371 C CG1 . ILE A 1 383 ? 155.234 168.398 150.140 1.00 19.31  ? 383 ILE A CG1 1 
ATOM   2372 C CG2 . ILE A 1 383 ? 153.338 169.270 148.780 1.00 18.57  ? 383 ILE A CG2 1 
ATOM   2373 C CD1 . ILE A 1 383 ? 154.803 169.024 151.436 1.00 22.73  ? 383 ILE A CD1 1 
ATOM   2374 N N   . GLN A 1 384 ? 154.536 168.833 145.421 1.00 17.90  ? 384 GLN A N   1 
ATOM   2375 C CA  . GLN A 1 384 ? 154.173 169.535 144.203 1.00 18.53  ? 384 GLN A CA  1 
ATOM   2376 C C   . GLN A 1 384 ? 152.674 169.630 143.976 1.00 22.12  ? 384 GLN A C   1 
ATOM   2377 O O   . GLN A 1 384 ? 152.254 170.317 143.039 1.00 28.30  ? 384 GLN A O   1 
ATOM   2378 C CB  . GLN A 1 384 ? 154.819 168.863 142.983 1.00 20.05  ? 384 GLN A CB  1 
ATOM   2379 C CG  . GLN A 1 384 ? 156.305 168.627 143.132 1.00 23.96  ? 384 GLN A CG  1 
ATOM   2380 C CD  . GLN A 1 384 ? 157.087 169.077 141.918 1.00 29.26  ? 384 GLN A CD  1 
ATOM   2381 O OE1 . GLN A 1 384 ? 158.018 169.874 142.026 1.00 34.79  ? 384 GLN A OE1 1 
ATOM   2382 N NE2 . GLN A 1 384 ? 156.712 168.568 140.751 1.00 33.30  ? 384 GLN A NE2 1 
ATOM   2383 N N   . ALA A 1 385 ? 151.860 168.969 144.794 1.00 17.36  ? 385 ALA A N   1 
ATOM   2384 C CA  . ALA A 1 385 ? 150.415 169.030 144.642 1.00 20.18  ? 385 ALA A CA  1 
ATOM   2385 C C   . ALA A 1 385 ? 149.761 168.753 145.984 1.00 17.54  ? 385 ALA A C   1 
ATOM   2386 O O   . ALA A 1 385 ? 150.205 167.880 146.732 1.00 14.91  ? 385 ALA A O   1 
ATOM   2387 C CB  . ALA A 1 385 ? 149.914 168.029 143.598 1.00 32.34  ? 385 ALA A CB  1 
ATOM   2388 N N   . TRP A 1 386 ? 148.709 169.506 146.277 1.00 21.51  ? 386 TRP A N   1 
ATOM   2389 C CA  . TRP A 1 386 ? 147.920 169.364 147.487 1.00 24.70  ? 386 TRP A CA  1 
ATOM   2390 C C   . TRP A 1 386 ? 146.452 169.471 147.110 1.00 34.58  ? 386 TRP A C   1 
ATOM   2391 O O   . TRP A 1 386 ? 146.115 170.125 146.116 1.00 41.26  ? 386 TRP A O   1 
ATOM   2392 C CB  . TRP A 1 386 ? 148.271 170.445 148.520 1.00 24.86  ? 386 TRP A CB  1 
ATOM   2393 C CG  . TRP A 1 386 ? 148.386 169.952 149.931 1.00 24.16  ? 386 TRP A CG  1 
ATOM   2394 C CD1 . TRP A 1 386 ? 147.761 170.467 151.026 1.00 27.00  ? 386 TRP A CD1 1 
ATOM   2395 C CD2 . TRP A 1 386 ? 149.186 168.860 150.403 1.00 20.74  ? 386 TRP A CD2 1 
ATOM   2396 N NE1 . TRP A 1 386 ? 148.112 169.761 152.148 1.00 25.98  ? 386 TRP A NE1 1 
ATOM   2397 C CE2 . TRP A 1 386 ? 148.986 168.769 151.792 1.00 22.23  ? 386 TRP A CE2 1 
ATOM   2398 C CE3 . TRP A 1 386 ? 150.048 167.950 149.787 1.00 24.01  ? 386 TRP A CE3 1 
ATOM   2399 C CZ2 . TRP A 1 386 ? 149.615 167.808 152.572 1.00 20.70  ? 386 TRP A CZ2 1 
ATOM   2400 C CZ3 . TRP A 1 386 ? 150.670 166.996 150.564 1.00 30.47  ? 386 TRP A CZ3 1 
ATOM   2401 C CH2 . TRP A 1 386 ? 150.451 166.932 151.941 1.00 23.55  ? 386 TRP A CH2 1 
ATOM   2402 N N   . PRO A 1 387 ? 145.563 168.829 147.865 1.00 33.90  ? 387 PRO A N   1 
ATOM   2403 C CA  . PRO A 1 387 ? 144.130 168.995 147.602 1.00 47.04  ? 387 PRO A CA  1 
ATOM   2404 C C   . PRO A 1 387 ? 143.728 170.460 147.690 1.00 54.25  ? 387 PRO A C   1 
ATOM   2405 O O   . PRO A 1 387 ? 144.129 171.181 148.606 1.00 55.36  ? 387 PRO A O   1 
ATOM   2406 C CB  . PRO A 1 387 ? 143.463 168.156 148.700 1.00 43.56  ? 387 PRO A CB  1 
ATOM   2407 C CG  . PRO A 1 387 ? 144.540 167.875 149.704 1.00 33.38  ? 387 PRO A CG  1 
ATOM   2408 C CD  . PRO A 1 387 ? 145.817 167.857 148.939 1.00 27.22  ? 387 PRO A CD  1 
ATOM   2409 N N   . GLU A 1 388 ? 142.923 170.897 146.720 1.00 52.18  ? 388 GLU A N   1 
ATOM   2410 C CA  . GLU A 1 388 ? 142.533 172.301 146.665 1.00 58.79  ? 388 GLU A CA  1 
ATOM   2411 C C   . GLU A 1 388 ? 141.606 172.677 147.813 1.00 67.42  ? 388 GLU A C   1 
ATOM   2412 O O   . GLU A 1 388 ? 141.545 173.849 148.200 1.00 71.76  ? 388 GLU A O   1 
ATOM   2413 C CB  . GLU A 1 388 ? 141.877 172.608 145.321 1.00 67.80  ? 388 GLU A CB  1 
ATOM   2414 C CG  . GLU A 1 388 ? 142.782 172.361 144.127 1.00 65.62  ? 388 GLU A CG  1 
ATOM   2415 C CD  . GLU A 1 388 ? 144.046 173.198 144.172 1.00 69.70  ? 388 GLU A CD  1 
ATOM   2416 O OE1 . GLU A 1 388 ? 144.001 174.367 143.735 1.00 71.24  ? 388 GLU A OE1 1 
ATOM   2417 O OE2 . GLU A 1 388 ? 145.085 172.688 144.642 1.00 63.67  ? 388 GLU A OE2 1 
ATOM   2418 N N   . ASN A 1 389 ? 140.881 171.706 148.369 1.00 66.99  ? 389 ASN A N   1 
ATOM   2419 C CA  . ASN A 1 389 ? 140.044 171.970 149.532 1.00 71.85  ? 389 ASN A CA  1 
ATOM   2420 C C   . ASN A 1 389 ? 140.857 172.192 150.801 1.00 69.44  ? 389 ASN A C   1 
ATOM   2421 O O   . ASN A 1 389 ? 140.285 172.601 151.817 1.00 66.37  ? 389 ASN A O   1 
ATOM   2422 C CB  . ASN A 1 389 ? 139.059 170.820 149.741 1.00 82.43  ? 389 ASN A CB  1 
ATOM   2423 C CG  . ASN A 1 389 ? 138.140 170.619 148.552 1.00 97.46  ? 389 ASN A CG  1 
ATOM   2424 O OD1 . ASN A 1 389 ? 138.527 170.856 147.408 1.00 95.44  ? 389 ASN A OD1 1 
ATOM   2425 N ND2 . ASN A 1 389 ? 136.915 170.180 148.818 1.00 105.42 ? 389 ASN A ND2 1 
ATOM   2426 N N   . ARG A 1 390 ? 142.160 171.931 150.769 1.00 60.04  ? 390 ARG A N   1 
ATOM   2427 C CA  . ARG A 1 390 ? 143.039 172.160 151.907 1.00 50.39  ? 390 ARG A CA  1 
ATOM   2428 C C   . ARG A 1 390 ? 143.851 173.425 151.669 1.00 49.00  ? 390 ARG A C   1 
ATOM   2429 O O   . ARG A 1 390 ? 144.499 173.565 150.628 1.00 47.02  ? 390 ARG A O   1 
ATOM   2430 C CB  . ARG A 1 390 ? 143.967 170.966 152.129 1.00 42.03  ? 390 ARG A CB  1 
ATOM   2431 C CG  . ARG A 1 390 ? 143.265 169.732 152.662 1.00 45.57  ? 390 ARG A CG  1 
ATOM   2432 C CD  . ARG A 1 390 ? 143.510 169.558 154.151 1.00 47.25  ? 390 ARG A CD  1 
ATOM   2433 N NE  . ARG A 1 390 ? 144.823 168.987 154.425 1.00 38.39  ? 390 ARG A NE  1 
ATOM   2434 C CZ  . ARG A 1 390 ? 145.118 167.699 154.318 1.00 41.58  ? 390 ARG A CZ  1 
ATOM   2435 N NH1 . ARG A 1 390 ? 144.212 166.810 153.944 1.00 50.73  ? 390 ARG A NH1 1 
ATOM   2436 N NH2 . ARG A 1 390 ? 146.353 167.291 154.593 1.00 37.86  ? 390 ARG A NH2 1 
ATOM   2437 N N   . THR A 1 391 ? 143.811 174.340 152.635 1.00 47.47  ? 391 THR A N   1 
ATOM   2438 C CA  . THR A 1 391 ? 144.485 175.625 152.527 1.00 42.27  ? 391 THR A CA  1 
ATOM   2439 C C   . THR A 1 391 ? 145.872 175.622 153.156 1.00 41.30  ? 391 THR A C   1 
ATOM   2440 O O   . THR A 1 391 ? 146.519 176.673 153.205 1.00 43.39  ? 391 THR A O   1 
ATOM   2441 C CB  . THR A 1 391 ? 143.630 176.724 153.160 1.00 44.81  ? 391 THR A CB  1 
ATOM   2442 O OG1 . THR A 1 391 ? 143.231 176.322 154.476 1.00 48.78  ? 391 THR A OG1 1 
ATOM   2443 C CG2 . THR A 1 391 ? 142.391 176.983 152.317 1.00 52.87  ? 391 THR A CG2 1 
ATOM   2444 N N   . ASP A 1 392 ? 146.340 174.476 153.642 1.00 34.12  ? 392 ASP A N   1 
ATOM   2445 C CA  . ASP A 1 392 ? 147.672 174.381 154.221 1.00 25.96  ? 392 ASP A CA  1 
ATOM   2446 C C   . ASP A 1 392 ? 148.111 172.925 154.197 1.00 27.06  ? 392 ASP A C   1 
ATOM   2447 O O   . ASP A 1 392 ? 147.356 172.033 153.805 1.00 32.61  ? 392 ASP A O   1 
ATOM   2448 C CB  . ASP A 1 392 ? 147.708 174.943 155.644 1.00 36.89  ? 392 ASP A CB  1 
ATOM   2449 C CG  . ASP A 1 392 ? 146.693 174.289 156.552 1.00 44.21  ? 392 ASP A CG  1 
ATOM   2450 O OD1 . ASP A 1 392 ? 145.498 174.274 156.195 1.00 43.47  ? 392 ASP A OD1 1 
ATOM   2451 O OD2 . ASP A 1 392 ? 147.092 173.793 157.625 1.00 47.82  ? 392 ASP A OD2 1 
ATOM   2452 N N   . LEU A 1 393 ? 149.354 172.697 154.620 1.00 29.95  ? 393 LEU A N   1 
ATOM   2453 C CA  . LEU A 1 393 ? 149.929 171.352 154.670 1.00 23.98  ? 393 LEU A CA  1 
ATOM   2454 C C   . LEU A 1 393 ? 149.577 170.691 156.003 1.00 30.12  ? 393 LEU A C   1 
ATOM   2455 O O   . LEU A 1 393 ? 150.413 170.488 156.885 1.00 33.96  ? 393 LEU A O   1 
ATOM   2456 C CB  . LEU A 1 393 ? 151.435 171.411 154.449 1.00 14.46  ? 393 LEU A CB  1 
ATOM   2457 C CG  . LEU A 1 393 ? 151.876 171.986 153.106 1.00 11.17  ? 393 LEU A CG  1 
ATOM   2458 C CD1 . LEU A 1 393 ? 153.321 172.433 153.152 1.00 9.62   ? 393 LEU A CD1 1 
ATOM   2459 C CD2 . LEU A 1 393 ? 151.685 170.944 152.030 1.00 25.42  ? 393 LEU A CD2 1 
ATOM   2460 N N   . HIS A 1 394 ? 148.294 170.346 156.133 1.00 32.24  ? 394 HIS A N   1 
ATOM   2461 C CA  . HIS A 1 394 ? 147.822 169.706 157.356 1.00 34.97  ? 394 HIS A CA  1 
ATOM   2462 C C   . HIS A 1 394 ? 148.408 168.312 157.531 1.00 36.88  ? 394 HIS A C   1 
ATOM   2463 O O   . HIS A 1 394 ? 148.599 167.863 158.667 1.00 43.77  ? 394 HIS A O   1 
ATOM   2464 C CB  . HIS A 1 394 ? 146.296 169.640 157.364 1.00 42.15  ? 394 HIS A CB  1 
ATOM   2465 C CG  . HIS A 1 394 ? 145.641 170.852 157.950 1.00 58.56  ? 394 HIS A CG  1 
ATOM   2466 N ND1 . HIS A 1 394 ? 145.960 171.338 159.200 1.00 65.43  ? 394 HIS A ND1 1 
ATOM   2467 C CD2 . HIS A 1 394 ? 144.680 171.671 157.461 1.00 59.22  ? 394 HIS A CD2 1 
ATOM   2468 C CE1 . HIS A 1 394 ? 145.225 172.406 159.455 1.00 66.92  ? 394 HIS A CE1 1 
ATOM   2469 N NE2 . HIS A 1 394 ? 144.443 172.631 158.415 1.00 64.18  ? 394 HIS A NE2 1 
ATOM   2470 N N   . ALA A 1 395 ? 148.699 167.615 156.433 1.00 35.87  ? 395 ALA A N   1 
ATOM   2471 C CA  . ALA A 1 395 ? 149.269 166.277 156.527 1.00 36.40  ? 395 ALA A CA  1 
ATOM   2472 C C   . ALA A 1 395 ? 150.705 166.283 157.026 1.00 31.89  ? 395 ALA A C   1 
ATOM   2473 O O   . ALA A 1 395 ? 151.249 165.210 157.303 1.00 36.32  ? 395 ALA A O   1 
ATOM   2474 C CB  . ALA A 1 395 ? 149.201 165.575 155.172 1.00 33.42  ? 395 ALA A CB  1 
ATOM   2475 N N   . PHE A 1 396 ? 151.329 167.465 157.099 1.00 27.11  ? 396 PHE A N   1 
ATOM   2476 C CA  . PHE A 1 396 ? 152.726 167.601 157.598 1.00 23.64  ? 396 PHE A CA  1 
ATOM   2477 C C   . PHE A 1 396 ? 152.742 168.566 158.782 1.00 32.51  ? 396 PHE A C   1 
ATOM   2478 O O   . PHE A 1 396 ? 153.771 169.251 158.974 1.00 32.21  ? 396 PHE A O   1 
ATOM   2479 C CB  . PHE A 1 396 ? 153.637 168.024 156.441 1.00 22.70  ? 396 PHE A CB  1 
ATOM   2480 C CG  . PHE A 1 396 ? 153.906 166.903 155.447 1.00 18.35  ? 396 PHE A CG  1 
ATOM   2481 C CD1 . PHE A 1 396 ? 154.840 165.917 155.738 1.00 18.07  ? 396 PHE A CD1 1 
ATOM   2482 C CD2 . PHE A 1 396 ? 153.241 166.841 154.228 1.00 24.14  ? 396 PHE A CD2 1 
ATOM   2483 C CE1 . PHE A 1 396 ? 155.093 164.892 154.844 1.00 23.56  ? 396 PHE A CE1 1 
ATOM   2484 C CE2 . PHE A 1 396 ? 153.502 165.813 153.334 1.00 30.27  ? 396 PHE A CE2 1 
ATOM   2485 C CZ  . PHE A 1 396 ? 154.424 164.842 153.646 1.00 31.50  ? 396 PHE A CZ  1 
ATOM   2486 N N   . GLU A 1 397 ? 151.659 168.633 159.567 1.00 44.17  ? 397 GLU A N   1 
ATOM   2487 C CA  . GLU A 1 397 ? 151.641 169.454 160.768 1.00 40.59  ? 397 GLU A CA  1 
ATOM   2488 C C   . GLU A 1 397 ? 152.449 168.849 161.907 1.00 40.57  ? 397 GLU A C   1 
ATOM   2489 O O   . GLU A 1 397 ? 152.681 169.535 162.907 1.00 41.77  ? 397 GLU A O   1 
ATOM   2490 C CB  . GLU A 1 397 ? 150.201 169.681 161.224 1.00 43.65  ? 397 GLU A CB  1 
ATOM   2491 C CG  . GLU A 1 397 ? 149.590 168.511 161.972 1.00 46.63  ? 397 GLU A CG  1 
ATOM   2492 C CD  . GLU A 1 397 ? 148.083 168.619 162.086 1.00 54.73  ? 397 GLU A CD  1 
ATOM   2493 O OE1 . GLU A 1 397 ? 147.605 169.438 162.898 1.00 61.19  ? 397 GLU A OE1 1 
ATOM   2494 O OE2 . GLU A 1 397 ? 147.376 167.887 161.364 1.00 54.22  ? 397 GLU A OE2 1 
ATOM   2495 N N   . ASN A 1 398 ? 152.904 167.601 161.753 1.00 38.16  ? 398 ASN A N   1 
ATOM   2496 C CA  . ASN A 1 398 ? 153.747 166.923 162.778 1.00 34.74  ? 398 ASN A CA  1 
ATOM   2497 C C   . ASN A 1 398 ? 155.155 166.716 162.211 1.00 33.45  ? 398 ASN A C   1 
ATOM   2498 O O   . ASN A 1 398 ? 156.022 166.233 162.969 1.00 41.00  ? 398 ASN A O   1 
ATOM   2499 C CB  . ASN A 1 398 ? 153.078 165.634 163.233 1.00 38.32  ? 398 ASN A CB  1 
ATOM   2500 C CG  . ASN A 1 398 ? 151.695 165.905 163.773 1.00 48.59  ? 398 ASN A CG  1 
ATOM   2501 O OD1 . ASN A 1 398 ? 151.554 166.509 164.842 1.00 58.39  ? 398 ASN A OD1 1 
ATOM   2502 N ND2 . ASN A 1 398 ? 150.667 165.482 163.052 1.00 46.34  ? 398 ASN A ND2 1 
ATOM   2503 N N   . LEU A 1 399 ? 155.382 167.076 160.943 1.00 27.61  ? 399 LEU A N   1 
ATOM   2504 C CA  . LEU A 1 399 ? 156.725 166.973 160.313 1.00 26.38  ? 399 LEU A CA  1 
ATOM   2505 C C   . LEU A 1 399 ? 157.622 168.060 160.920 1.00 26.17  ? 399 LEU A C   1 
ATOM   2506 O O   . LEU A 1 399 ? 157.283 169.251 160.744 1.00 25.07  ? 399 LEU A O   1 
ATOM   2507 C CB  . LEU A 1 399 ? 156.599 167.123 158.799 1.00 18.55  ? 399 LEU A CB  1 
ATOM   2508 C CG  . LEU A 1 399 ? 157.913 167.148 158.013 1.00 12.25  ? 399 LEU A CG  1 
ATOM   2509 C CD1 . LEU A 1 399 ? 158.119 165.853 157.257 1.00 18.39  ? 399 LEU A CD1 1 
ATOM   2510 C CD2 . LEU A 1 399 ? 157.946 168.336 157.071 1.00 12.75  ? 399 LEU A CD2 1 
ATOM   2511 N N   . GLU A 1 400 ? 158.713 167.672 161.587 1.00 25.46  ? 400 GLU A N   1 
ATOM   2512 C CA  . GLU A 1 400 ? 159.611 168.637 162.278 1.00 22.30  ? 400 GLU A CA  1 
ATOM   2513 C C   . GLU A 1 400 ? 161.024 168.610 161.676 1.00 26.56  ? 400 GLU A C   1 
ATOM   2514 O O   . GLU A 1 400 ? 161.697 169.660 161.750 1.00 32.85  ? 400 GLU A O   1 
ATOM   2515 C CB  . GLU A 1 400 ? 159.676 168.277 163.760 1.00 27.70  ? 400 GLU A CB  1 
ATOM   2516 C CG  . GLU A 1 400 ? 158.333 168.400 164.473 1.00 34.59  ? 400 GLU A CG  1 
ATOM   2517 C CD  . GLU A 1 400 ? 158.233 167.669 165.799 1.00 40.70  ? 400 GLU A CD  1 
ATOM   2518 O OE1 . GLU A 1 400 ? 159.229 167.047 166.227 1.00 39.42  ? 400 GLU A OE1 1 
ATOM   2519 O OE2 . GLU A 1 400 ? 157.143 167.720 166.404 1.00 41.60  ? 400 GLU A OE2 1 
ATOM   2520 N N   . ILE A 1 401 ? 161.459 167.478 161.112 1.00 25.48  ? 401 ILE A N   1 
ATOM   2521 C CA  . ILE A 1 401 ? 162.852 167.328 160.584 1.00 26.03  ? 401 ILE A CA  1 
ATOM   2522 C C   . ILE A 1 401 ? 162.817 167.008 159.083 1.00 27.76  ? 401 ILE A C   1 
ATOM   2523 O O   . ILE A 1 401 ? 161.938 166.212 158.685 1.00 37.52  ? 401 ILE A O   1 
ATOM   2524 C CB  . ILE A 1 401 ? 163.605 166.245 161.377 1.00 37.25  ? 401 ILE A CB  1 
ATOM   2525 C CG1 . ILE A 1 401 ? 163.854 166.689 162.816 1.00 35.53  ? 401 ILE A CG1 1 
ATOM   2526 C CG2 . ILE A 1 401 ? 164.903 165.846 160.673 1.00 47.91  ? 401 ILE A CG2 1 
ATOM   2527 C CD1 . ILE A 1 401 ? 164.394 165.596 163.718 1.00 35.13  ? 401 ILE A CD1 1 
ATOM   2528 N N   . ILE A 1 402 ? 163.698 167.622 158.281 1.00 21.72  ? 402 ILE A N   1 
ATOM   2529 C CA  . ILE A 1 402 ? 163.806 167.338 156.854 1.00 24.60  ? 402 ILE A CA  1 
ATOM   2530 C C   . ILE A 1 402 ? 165.274 167.108 156.515 1.00 40.16  ? 402 ILE A C   1 
ATOM   2531 O O   . ILE A 1 402 ? 165.756 167.568 155.473 1.00 45.52  ? 402 ILE A O   1 
ATOM   2532 C CB  . ILE A 1 402 ? 163.202 168.462 155.992 1.00 21.06  ? 402 ILE A CB  1 
ATOM   2533 C CG1 . ILE A 1 402 ? 161.919 168.994 156.620 1.00 24.78  ? 402 ILE A CG1 1 
ATOM   2534 C CG2 . ILE A 1 402 ? 162.874 167.950 154.598 1.00 22.25  ? 402 ILE A CG2 1 
ATOM   2535 C CD1 . ILE A 1 402 ? 161.134 169.907 155.706 1.00 22.49  ? 402 ILE A CD1 1 
ATOM   2536 N N   . ARG A 1 403 ? 166.002 166.453 157.421 1.00 41.27  ? 403 ARG A N   1 
ATOM   2537 C CA  . ARG A 1 403 ? 167.423 166.167 157.254 1.00 43.63  ? 403 ARG A CA  1 
ATOM   2538 C C   . ARG A 1 403 ? 167.738 165.742 155.829 1.00 52.98  ? 403 ARG A C   1 
ATOM   2539 O O   . ARG A 1 403 ? 167.240 164.720 155.348 1.00 53.21  ? 403 ARG A O   1 
ATOM   2540 C CB  . ARG A 1 403 ? 167.842 165.060 158.223 1.00 40.87  ? 403 ARG A CB  1 
ATOM   2541 C CG  . ARG A 1 403 ? 168.383 165.540 159.553 1.00 48.07  ? 403 ARG A CG  1 
ATOM   2542 C CD  . ARG A 1 403 ? 168.512 164.382 160.529 1.00 47.83  ? 403 ARG A CD  1 
ATOM   2543 N NE  . ARG A 1 403 ? 168.006 164.713 161.855 1.00 44.79  ? 403 ARG A NE  1 
ATOM   2544 C CZ  . ARG A 1 403 ? 168.647 165.472 162.734 1.00 45.50  ? 403 ARG A CZ  1 
ATOM   2545 N NH1 . ARG A 1 403 ? 169.829 165.999 162.462 1.00 43.61  ? 403 ARG A NH1 1 
ATOM   2546 N NH2 . ARG A 1 403 ? 168.088 165.705 163.918 1.00 48.79  ? 403 ARG A NH2 1 
ATOM   2547 N N   . GLY A 1 404 ? 168.585 166.519 155.159 1.00 55.62  ? 404 GLY A N   1 
ATOM   2548 C CA  . GLY A 1 404 ? 168.821 166.334 153.742 1.00 57.77  ? 404 GLY A CA  1 
ATOM   2549 C C   . GLY A 1 404 ? 169.893 165.322 153.398 1.00 60.16  ? 404 GLY A C   1 
ATOM   2550 O O   . GLY A 1 404 ? 170.902 165.669 152.777 1.00 56.80  ? 404 GLY A O   1 
ATOM   2551 N N   . ARG A 1 405 ? 169.692 164.066 153.801 1.00 59.56  ? 405 ARG A N   1 
ATOM   2552 C CA  . ARG A 1 405 ? 170.590 163.005 153.360 1.00 56.41  ? 405 ARG A CA  1 
ATOM   2553 C C   . ARG A 1 405 ? 170.520 162.836 151.848 1.00 58.17  ? 405 ARG A C   1 
ATOM   2554 O O   . ARG A 1 405 ? 171.547 162.658 151.184 1.00 65.66  ? 405 ARG A O   1 
ATOM   2555 C CB  . ARG A 1 405 ? 170.246 161.697 154.071 1.00 52.31  ? 405 ARG A CB  1 
ATOM   2556 C CG  . ARG A 1 405 ? 171.028 161.464 155.356 1.00 55.11  ? 405 ARG A CG  1 
ATOM   2557 C CD  . ARG A 1 405 ? 170.599 162.429 156.449 1.00 57.80  ? 405 ARG A CD  1 
ATOM   2558 N NE  . ARG A 1 405 ? 171.353 162.238 157.682 1.00 68.42  ? 405 ARG A NE  1 
ATOM   2559 C CZ  . ARG A 1 405 ? 170.964 161.463 158.685 1.00 70.40  ? 405 ARG A CZ  1 
ATOM   2560 N NH1 . ARG A 1 405 ? 169.831 160.783 158.633 1.00 63.17  ? 405 ARG A NH1 1 
ATOM   2561 N NH2 . ARG A 1 405 ? 171.730 161.369 159.767 1.00 73.11  ? 405 ARG A NH2 1 
ATOM   2562 N N   . THR A 1 406 ? 169.314 162.891 151.290 1.00 54.92  ? 406 THR A N   1 
ATOM   2563 C CA  . THR A 1 406 ? 169.094 162.979 149.855 1.00 55.91  ? 406 THR A CA  1 
ATOM   2564 C C   . THR A 1 406 ? 168.338 164.267 149.567 1.00 62.91  ? 406 THR A C   1 
ATOM   2565 O O   . THR A 1 406 ? 167.376 164.598 150.266 1.00 71.31  ? 406 THR A O   1 
ATOM   2566 C CB  . THR A 1 406 ? 168.307 161.776 149.331 1.00 55.73  ? 406 THR A CB  1 
ATOM   2567 O OG1 . THR A 1 406 ? 168.724 160.593 150.022 1.00 64.24  ? 406 THR A OG1 1 
ATOM   2568 C CG2 . THR A 1 406 ? 168.544 161.596 147.840 1.00 55.83  ? 406 THR A CG2 1 
ATOM   2569 N N   . LYS A 1 407 ? 168.777 165.001 148.550 1.00 55.63  ? 407 LYS A N   1 
ATOM   2570 C CA  . LYS A 1 407 ? 168.254 166.332 148.283 1.00 51.80  ? 407 LYS A CA  1 
ATOM   2571 C C   . LYS A 1 407 ? 167.809 166.446 146.833 1.00 49.04  ? 407 LYS A C   1 
ATOM   2572 O O   . LYS A 1 407 ? 168.478 165.944 145.926 1.00 52.86  ? 407 LYS A O   1 
ATOM   2573 C CB  . LYS A 1 407 ? 169.306 167.402 148.596 1.00 55.45  ? 407 LYS A CB  1 
ATOM   2574 C CG  . LYS A 1 407 ? 170.172 167.076 149.807 1.00 51.07  ? 407 LYS A CG  1 
ATOM   2575 C CD  . LYS A 1 407 ? 171.286 168.089 150.008 1.00 49.82  ? 407 LYS A CD  1 
ATOM   2576 C CE  . LYS A 1 407 ? 170.906 169.454 149.471 1.00 47.93  ? 407 LYS A CE  1 
ATOM   2577 N NZ  . LYS A 1 407 ? 171.789 170.529 149.999 1.00 53.92  ? 407 LYS A NZ  1 
ATOM   2578 N N   . GLN A 1 408 ? 166.673 167.108 146.623 1.00 50.15  ? 408 GLN A N   1 
ATOM   2579 C CA  . GLN A 1 408 ? 166.185 167.353 145.273 1.00 55.12  ? 408 GLN A CA  1 
ATOM   2580 C C   . GLN A 1 408 ? 167.089 168.355 144.568 1.00 59.72  ? 408 GLN A C   1 
ATOM   2581 O O   . GLN A 1 408 ? 167.391 169.422 145.110 1.00 60.68  ? 408 GLN A O   1 
ATOM   2582 C CB  . GLN A 1 408 ? 164.750 167.874 145.310 1.00 52.05  ? 408 GLN A CB  1 
ATOM   2583 C CG  . GLN A 1 408 ? 164.205 168.295 143.956 1.00 50.93  ? 408 GLN A CG  1 
ATOM   2584 C CD  . GLN A 1 408 ? 163.750 169.740 143.935 1.00 52.24  ? 408 GLN A CD  1 
ATOM   2585 O OE1 . GLN A 1 408 ? 164.031 170.504 144.857 1.00 47.11  ? 408 GLN A OE1 1 
ATOM   2586 N NE2 . GLN A 1 408 ? 163.041 170.122 142.880 1.00 54.81  ? 408 GLN A NE2 1 
ATOM   2587 N N   . HIS A 1 409 ? 167.527 168.003 143.359 1.00 66.39  ? 409 HIS A N   1 
ATOM   2588 C CA  . HIS A 1 409 ? 168.446 168.813 142.562 1.00 69.29  ? 409 HIS A CA  1 
ATOM   2589 C C   . HIS A 1 409 ? 169.748 169.109 143.300 1.00 67.54  ? 409 HIS A C   1 
ATOM   2590 O O   . HIS A 1 409 ? 170.509 169.992 142.893 1.00 71.14  ? 409 HIS A O   1 
ATOM   2591 C CB  . HIS A 1 409 ? 167.788 170.122 142.110 1.00 62.91  ? 409 HIS A CB  1 
ATOM   2592 C CG  . HIS A 1 409 ? 166.703 169.934 141.097 1.00 74.91  ? 409 HIS A CG  1 
ATOM   2593 N ND1 . HIS A 1 409 ? 166.499 168.741 140.437 1.00 76.06  ? 409 HIS A ND1 1 
ATOM   2594 C CD2 . HIS A 1 409 ? 165.760 170.787 140.630 1.00 75.59  ? 409 HIS A CD2 1 
ATOM   2595 C CE1 . HIS A 1 409 ? 165.479 168.867 139.608 1.00 73.47  ? 409 HIS A CE1 1 
ATOM   2596 N NE2 . HIS A 1 409 ? 165.013 170.099 139.706 1.00 76.44  ? 409 HIS A NE2 1 
ATOM   2597 N N   . GLY A 1 410 ? 170.018 168.387 144.385 1.00 61.58  ? 410 GLY A N   1 
ATOM   2598 C CA  . GLY A 1 410 ? 171.242 168.568 145.135 1.00 62.53  ? 410 GLY A CA  1 
ATOM   2599 C C   . GLY A 1 410 ? 171.303 169.813 145.988 1.00 59.99  ? 410 GLY A C   1 
ATOM   2600 O O   . GLY A 1 410 ? 172.364 170.107 146.545 1.00 64.95  ? 410 GLY A O   1 
ATOM   2601 N N   . GLN A 1 411 ? 170.205 170.560 146.111 1.00 50.96  ? 411 GLN A N   1 
ATOM   2602 C CA  . GLN A 1 411 ? 170.247 171.806 146.865 1.00 50.10  ? 411 GLN A CA  1 
ATOM   2603 C C   . GLN A 1 411 ? 169.091 171.944 147.850 1.00 53.75  ? 411 GLN A C   1 
ATOM   2604 O O   . GLN A 1 411 ? 169.232 172.608 148.881 1.00 61.37  ? 411 GLN A O   1 
ATOM   2605 C CB  . GLN A 1 411 ? 170.251 173.000 145.907 1.00 51.08  ? 411 GLN A CB  1 
ATOM   2606 C CG  . GLN A 1 411 ? 169.495 172.758 144.613 1.00 53.83  ? 411 GLN A CG  1 
ATOM   2607 C CD  . GLN A 1 411 ? 169.621 173.914 143.641 1.00 58.24  ? 411 GLN A CD  1 
ATOM   2608 O OE1 . GLN A 1 411 ? 169.924 175.040 144.035 1.00 52.17  ? 411 GLN A OE1 1 
ATOM   2609 N NE2 . GLN A 1 411 ? 169.387 173.641 142.363 1.00 62.51  ? 411 GLN A NE2 1 
ATOM   2610 N N   . PHE A 1 412 ? 167.954 171.319 147.559 1.00 47.42  ? 412 PHE A N   1 
ATOM   2611 C CA  . PHE A 1 412 ? 166.715 171.583 148.277 1.00 34.93  ? 412 PHE A CA  1 
ATOM   2612 C C   . PHE A 1 412 ? 166.272 170.372 149.086 1.00 38.35  ? 412 PHE A C   1 
ATOM   2613 O O   . PHE A 1 412 ? 166.324 169.236 148.606 1.00 49.10  ? 412 PHE A O   1 
ATOM   2614 C CB  . PHE A 1 412 ? 165.603 171.982 147.307 1.00 32.49  ? 412 PHE A CB  1 
ATOM   2615 C CG  . PHE A 1 412 ? 165.890 173.240 146.546 1.00 38.68  ? 412 PHE A CG  1 
ATOM   2616 C CD1 . PHE A 1 412 ? 166.325 174.376 147.204 1.00 42.45  ? 412 PHE A CD1 1 
ATOM   2617 C CD2 . PHE A 1 412 ? 165.731 173.287 145.173 1.00 42.35  ? 412 PHE A CD2 1 
ATOM   2618 C CE1 . PHE A 1 412 ? 166.590 175.537 146.508 1.00 45.43  ? 412 PHE A CE1 1 
ATOM   2619 C CE2 . PHE A 1 412 ? 165.994 174.445 144.471 1.00 46.18  ? 412 PHE A CE2 1 
ATOM   2620 C CZ  . PHE A 1 412 ? 166.425 175.572 145.139 1.00 47.99  ? 412 PHE A CZ  1 
ATOM   2621 N N   . SER A 1 413 ? 165.831 170.629 150.315 1.00 37.01  ? 413 SER A N   1 
ATOM   2622 C CA  . SER A 1 413 ? 165.222 169.619 151.170 1.00 35.59  ? 413 SER A CA  1 
ATOM   2623 C C   . SER A 1 413 ? 163.715 169.788 151.279 1.00 39.19  ? 413 SER A C   1 
ATOM   2624 O O   . SER A 1 413 ? 162.970 168.820 151.111 1.00 44.85  ? 413 SER A O   1 
ATOM   2625 C CB  . SER A 1 413 ? 165.855 169.660 152.566 1.00 37.16  ? 413 SER A CB  1 
ATOM   2626 O OG  . SER A 1 413 ? 166.190 170.986 152.922 1.00 36.60  ? 413 SER A OG  1 
ATOM   2627 N N   . LEU A 1 414 ? 163.243 170.998 151.560 1.00 32.69  ? 414 LEU A N   1 
ATOM   2628 C CA  . LEU A 1 414 ? 161.821 171.313 151.530 1.00 22.56  ? 414 LEU A CA  1 
ATOM   2629 C C   . LEU A 1 414 ? 161.523 172.018 150.215 1.00 24.07  ? 414 LEU A C   1 
ATOM   2630 O O   . LEU A 1 414 ? 162.042 173.109 149.962 1.00 28.20  ? 414 LEU A O   1 
ATOM   2631 C CB  . LEU A 1 414 ? 161.424 172.186 152.719 1.00 18.42  ? 414 LEU A CB  1 
ATOM   2632 C CG  . LEU A 1 414 ? 159.965 172.640 152.759 1.00 16.32  ? 414 LEU A CG  1 
ATOM   2633 C CD1 . LEU A 1 414 ? 159.047 171.448 152.934 1.00 23.21  ? 414 LEU A CD1 1 
ATOM   2634 C CD2 . LEU A 1 414 ? 159.744 173.649 153.868 1.00 12.50  ? 414 LEU A CD2 1 
ATOM   2635 N N   . ALA A 1 415 ? 160.694 171.397 149.382 1.00 18.71  ? 415 ALA A N   1 
ATOM   2636 C CA  . ALA A 1 415 ? 160.467 171.854 148.016 1.00 22.28  ? 415 ALA A CA  1 
ATOM   2637 C C   . ALA A 1 415 ? 158.981 172.028 147.742 1.00 26.09  ? 415 ALA A C   1 
ATOM   2638 O O   . ALA A 1 415 ? 158.450 171.559 146.734 1.00 34.12  ? 415 ALA A O   1 
ATOM   2639 C CB  . ALA A 1 415 ? 161.093 170.891 147.015 1.00 26.34  ? 415 ALA A CB  1 
ATOM   2640 N N   . VAL A 1 416 ? 158.284 172.711 148.648 1.00 20.59  ? 416 VAL A N   1 
ATOM   2641 C CA  . VAL A 1 416 ? 156.878 173.040 148.448 1.00 14.89  ? 416 VAL A CA  1 
ATOM   2642 C C   . VAL A 1 416 ? 156.772 173.948 147.230 1.00 18.76  ? 416 VAL A C   1 
ATOM   2643 O O   . VAL A 1 416 ? 157.173 175.114 147.281 1.00 25.66  ? 416 VAL A O   1 
ATOM   2644 C CB  . VAL A 1 416 ? 156.288 173.709 149.703 1.00 12.22  ? 416 VAL A CB  1 
ATOM   2645 C CG1 . VAL A 1 416 ? 154.907 174.258 149.422 1.00 20.96  ? 416 VAL A CG1 1 
ATOM   2646 C CG2 . VAL A 1 416 ? 156.249 172.723 150.855 1.00 11.24  ? 416 VAL A CG2 1 
ATOM   2647 N N   . VAL A 1 417 ? 156.228 173.431 146.131 1.00 18.82  ? 417 VAL A N   1 
ATOM   2648 C CA  . VAL A 1 417 ? 156.265 174.119 144.845 1.00 19.86  ? 417 VAL A CA  1 
ATOM   2649 C C   . VAL A 1 417 ? 154.879 174.085 144.216 1.00 29.26  ? 417 VAL A C   1 
ATOM   2650 O O   . VAL A 1 417 ? 154.290 173.009 144.064 1.00 33.84  ? 417 VAL A O   1 
ATOM   2651 C CB  . VAL A 1 417 ? 157.300 173.490 143.895 1.00 26.50  ? 417 VAL A CB  1 
ATOM   2652 C CG1 . VAL A 1 417 ? 156.955 173.789 142.451 1.00 30.55  ? 417 VAL A CG1 1 
ATOM   2653 C CG2 . VAL A 1 417 ? 158.691 173.995 144.213 1.00 30.65  ? 417 VAL A CG2 1 
ATOM   2654 N N   . SER A 1 418 ? 154.367 175.260 143.849 1.00 38.22  ? 418 SER A N   1 
ATOM   2655 C CA  . SER A 1 418 ? 153.156 175.418 143.041 1.00 37.89  ? 418 SER A CA  1 
ATOM   2656 C C   . SER A 1 418 ? 151.967 174.704 143.691 1.00 45.30  ? 418 SER A C   1 
ATOM   2657 O O   . SER A 1 418 ? 151.346 173.798 143.129 1.00 46.49  ? 418 SER A O   1 
ATOM   2658 C CB  . SER A 1 418 ? 153.389 174.924 141.604 1.00 40.43  ? 418 SER A CB  1 
ATOM   2659 O OG  . SER A 1 418 ? 153.290 173.514 141.514 1.00 32.95  ? 418 SER A OG  1 
ATOM   2660 N N   . LEU A 1 419 ? 151.665 175.156 144.899 1.00 43.16  ? 419 LEU A N   1 
ATOM   2661 C CA  . LEU A 1 419 ? 150.554 174.648 145.692 1.00 36.11  ? 419 LEU A CA  1 
ATOM   2662 C C   . LEU A 1 419 ? 149.470 175.710 145.796 1.00 47.32  ? 419 LEU A C   1 
ATOM   2663 O O   . LEU A 1 419 ? 149.629 176.849 145.348 1.00 45.37  ? 419 LEU A O   1 
ATOM   2664 C CB  . LEU A 1 419 ? 151.020 174.217 147.085 1.00 19.68  ? 419 LEU A CB  1 
ATOM   2665 C CG  . LEU A 1 419 ? 151.447 172.771 147.309 1.00 12.27  ? 419 LEU A CG  1 
ATOM   2666 C CD1 . LEU A 1 419 ? 152.877 172.561 146.905 1.00 14.59  ? 419 LEU A CD1 1 
ATOM   2667 C CD2 . LEU A 1 419 ? 151.255 172.419 148.765 1.00 15.10  ? 419 LEU A CD2 1 
ATOM   2668 N N   . ASN A 1 420 ? 148.349 175.321 146.394 1.00 49.09  ? 420 ASN A N   1 
ATOM   2669 C CA  . ASN A 1 420 ? 147.248 176.257 146.604 1.00 48.67  ? 420 ASN A CA  1 
ATOM   2670 C C   . ASN A 1 420 ? 147.021 176.477 148.087 1.00 46.55  ? 420 ASN A C   1 
ATOM   2671 O O   . ASN A 1 420 ? 145.874 176.543 148.536 1.00 53.46  ? 420 ASN A O   1 
ATOM   2672 C CB  . ASN A 1 420 ? 145.954 175.751 145.958 1.00 63.52  ? 420 ASN A CB  1 
ATOM   2673 C CG  . ASN A 1 420 ? 145.088 176.887 145.431 1.00 67.72  ? 420 ASN A CG  1 
ATOM   2674 O OD1 . ASN A 1 420 ? 145.596 177.886 144.916 1.00 71.06  ? 420 ASN A OD1 1 
ATOM   2675 N ND2 . ASN A 1 420 ? 143.770 176.750 145.596 1.00 66.67  ? 420 ASN A ND2 1 
ATOM   2676 N N   . ILE A 1 421 ? 148.102 176.597 148.850 1.00 42.85  ? 421 ILE A N   1 
ATOM   2677 C CA  . ILE A 1 421 ? 148.023 176.707 150.298 1.00 38.13  ? 421 ILE A CA  1 
ATOM   2678 C C   . ILE A 1 421 ? 147.942 178.182 150.657 1.00 40.34  ? 421 ILE A C   1 
ATOM   2679 O O   . ILE A 1 421 ? 148.781 178.984 150.229 1.00 41.49  ? 421 ILE A O   1 
ATOM   2680 C CB  . ILE A 1 421 ? 149.221 176.032 150.981 1.00 27.55  ? 421 ILE A CB  1 
ATOM   2681 C CG1 . ILE A 1 421 ? 150.540 176.442 150.324 1.00 26.76  ? 421 ILE A CG1 1 
ATOM   2682 C CG2 . ILE A 1 421 ? 149.078 174.517 150.917 1.00 38.30  ? 421 ILE A CG2 1 
ATOM   2683 C CD1 . ILE A 1 421 ? 151.736 175.681 150.851 1.00 26.57  ? 421 ILE A CD1 1 
ATOM   2684 N N   . THR A 1 422 ? 146.912 178.550 151.419 1.00 40.93  ? 422 THR A N   1 
ATOM   2685 C CA  . THR A 1 422 ? 146.835 179.915 151.924 1.00 42.44  ? 422 THR A CA  1 
ATOM   2686 C C   . THR A 1 422 ? 147.906 180.157 152.977 1.00 43.59  ? 422 THR A C   1 
ATOM   2687 O O   . THR A 1 422 ? 148.583 181.190 152.957 1.00 51.98  ? 422 THR A O   1 
ATOM   2688 C CB  . THR A 1 422 ? 145.441 180.190 152.485 1.00 49.82  ? 422 THR A CB  1 
ATOM   2689 O OG1 . THR A 1 422 ? 144.497 180.261 151.408 1.00 57.39  ? 422 THR A OG1 1 
ATOM   2690 C CG2 . THR A 1 422 ? 145.424 181.507 153.242 1.00 49.29  ? 422 THR A CG2 1 
ATOM   2691 N N   . SER A 1 423 ? 148.090 179.205 153.886 1.00 34.48  ? 423 SER A N   1 
ATOM   2692 C CA  . SER A 1 423 ? 149.152 179.246 154.878 1.00 26.06  ? 423 SER A CA  1 
ATOM   2693 C C   . SER A 1 423 ? 150.107 178.089 154.630 1.00 28.70  ? 423 SER A C   1 
ATOM   2694 O O   . SER A 1 423 ? 149.716 177.052 154.089 1.00 41.61  ? 423 SER A O   1 
ATOM   2695 C CB  . SER A 1 423 ? 148.593 179.166 156.300 1.00 35.52  ? 423 SER A CB  1 
ATOM   2696 O OG  . SER A 1 423 ? 147.560 178.201 156.391 1.00 34.09  ? 423 SER A OG  1 
ATOM   2697 N N   . LEU A 1 424 ? 151.370 178.275 155.020 1.00 24.09  ? 424 LEU A N   1 
ATOM   2698 C CA  . LEU A 1 424 ? 152.363 177.232 154.784 1.00 19.42  ? 424 LEU A CA  1 
ATOM   2699 C C   . LEU A 1 424 ? 152.020 175.961 155.550 1.00 17.19  ? 424 LEU A C   1 
ATOM   2700 O O   . LEU A 1 424 ? 152.128 174.855 155.010 1.00 21.81  ? 424 LEU A O   1 
ATOM   2701 C CB  . LEU A 1 424 ? 153.755 177.737 155.156 1.00 20.65  ? 424 LEU A CB  1 
ATOM   2702 C CG  . LEU A 1 424 ? 154.926 176.925 154.610 1.00 14.36  ? 424 LEU A CG  1 
ATOM   2703 C CD1 . LEU A 1 424 ? 154.630 176.438 153.208 1.00 14.68  ? 424 LEU A CD1 1 
ATOM   2704 C CD2 . LEU A 1 424 ? 156.165 177.785 154.606 1.00 17.40  ? 424 LEU A CD2 1 
ATOM   2705 N N   . GLY A 1 425 ? 151.604 176.097 156.807 1.00 18.41  ? 425 GLY A N   1 
ATOM   2706 C CA  . GLY A 1 425 ? 151.024 174.998 157.546 1.00 20.37  ? 425 GLY A CA  1 
ATOM   2707 C C   . GLY A 1 425 ? 151.998 174.106 158.281 1.00 25.21  ? 425 GLY A C   1 
ATOM   2708 O O   . GLY A 1 425 ? 151.567 173.335 159.146 1.00 39.03  ? 425 GLY A O   1 
ATOM   2709 N N   . LEU A 1 426 ? 153.294 174.182 157.978 1.00 23.48  ? 426 LEU A N   1 
ATOM   2710 C CA  . LEU A 1 426 ? 154.292 173.356 158.658 1.00 24.29  ? 426 LEU A CA  1 
ATOM   2711 C C   . LEU A 1 426 ? 154.579 173.949 160.038 1.00 33.25  ? 426 LEU A C   1 
ATOM   2712 O O   . LEU A 1 426 ? 155.674 174.424 160.341 1.00 35.57  ? 426 LEU A O   1 
ATOM   2713 C CB  . LEU A 1 426 ? 155.561 173.253 157.825 1.00 17.67  ? 426 LEU A CB  1 
ATOM   2714 C CG  . LEU A 1 426 ? 155.461 172.561 156.470 1.00 10.79  ? 426 LEU A CG  1 
ATOM   2715 C CD1 . LEU A 1 426 ? 156.580 173.023 155.565 1.00 9.72   ? 426 LEU A CD1 1 
ATOM   2716 C CD2 . LEU A 1 426 ? 155.516 171.066 156.652 1.00 12.94  ? 426 LEU A CD2 1 
ATOM   2717 N N   . ARG A 1 427 ? 153.558 173.901 160.894 1.00 40.77  ? 427 ARG A N   1 
ATOM   2718 C CA  . ARG A 1 427 ? 153.643 174.549 162.196 1.00 35.29  ? 427 ARG A CA  1 
ATOM   2719 C C   . ARG A 1 427 ? 154.610 173.861 163.150 1.00 33.13  ? 427 ARG A C   1 
ATOM   2720 O O   . ARG A 1 427 ? 154.933 174.440 164.193 1.00 32.71  ? 427 ARG A O   1 
ATOM   2721 C CB  . ARG A 1 427 ? 152.254 174.626 162.829 1.00 34.36  ? 427 ARG A CB  1 
ATOM   2722 C CG  . ARG A 1 427 ? 151.775 173.338 163.470 1.00 36.66  ? 427 ARG A CG  1 
ATOM   2723 C CD  . ARG A 1 427 ? 150.313 173.450 163.854 1.00 39.83  ? 427 ARG A CD  1 
ATOM   2724 N NE  . ARG A 1 427 ? 149.544 174.154 162.835 1.00 48.22  ? 427 ARG A NE  1 
ATOM   2725 C CZ  . ARG A 1 427 ? 148.723 173.568 161.975 1.00 61.04  ? 427 ARG A CZ  1 
ATOM   2726 N NH1 . ARG A 1 427 ? 148.504 172.265 162.008 1.00 61.53  ? 427 ARG A NH1 1 
ATOM   2727 N NH2 . ARG A 1 427 ? 148.097 174.310 161.067 1.00 63.54  ? 427 ARG A NH2 1 
ATOM   2728 N N   . SER A 1 428 ? 155.078 172.660 162.771 1.00 22.77  ? 428 SER A N   1 
ATOM   2729 C CA  . SER A 1 428 ? 156.061 171.872 163.558 1.00 22.07  ? 428 SER A CA  1 
ATOM   2730 C C   . SER A 1 428 ? 157.463 172.052 162.970 1.00 19.84  ? 428 SER A C   1 
ATOM   2731 O O   . SER A 1 428 ? 158.415 172.199 163.767 1.00 24.26  ? 428 SER A O   1 
ATOM   2732 C CB  . SER A 1 428 ? 155.708 170.415 163.534 1.00 38.47  ? 428 SER A CB  1 
ATOM   2733 O OG  . SER A 1 428 ? 155.292 169.951 164.807 1.00 45.99  ? 428 SER A OG  1 
ATOM   2734 N N   . LEU A 1 429 ? 157.589 172.016 161.638 1.00 18.99  ? 429 LEU A N   1 
ATOM   2735 C CA  . LEU A 1 429 ? 158.914 172.095 160.968 1.00 23.90  ? 429 LEU A CA  1 
ATOM   2736 C C   . LEU A 1 429 ? 159.829 173.021 161.779 1.00 24.84  ? 429 LEU A C   1 
ATOM   2737 O O   . LEU A 1 429 ? 159.518 174.230 161.859 1.00 28.79  ? 429 LEU A O   1 
ATOM   2738 C CB  . LEU A 1 429 ? 158.774 172.568 159.524 1.00 17.38  ? 429 LEU A CB  1 
ATOM   2739 C CG  . LEU A 1 429 ? 160.078 172.650 158.723 1.00 9.50   ? 429 LEU A CG  1 
ATOM   2740 C CD1 . LEU A 1 429 ? 160.987 171.454 158.947 1.00 14.98  ? 429 LEU A CD1 1 
ATOM   2741 C CD2 . LEU A 1 429 ? 159.741 172.778 157.259 1.00 14.98  ? 429 LEU A CD2 1 
ATOM   2742 N N   . LYS A 1 430 ? 160.904 172.473 162.349 1.00 25.12  ? 430 LYS A N   1 
ATOM   2743 C CA  . LYS A 1 430 ? 161.833 173.258 163.203 1.00 27.91  ? 430 LYS A CA  1 
ATOM   2744 C C   . LYS A 1 430 ? 163.298 172.979 162.836 1.00 28.44  ? 430 LYS A C   1 
ATOM   2745 O O   . LYS A 1 430 ? 164.156 173.769 163.289 1.00 31.05  ? 430 LYS A O   1 
ATOM   2746 C CB  . LYS A 1 430 ? 161.566 172.908 164.673 1.00 37.41  ? 430 LYS A CB  1 
ATOM   2747 C CG  . LYS A 1 430 ? 161.497 171.420 165.010 1.00 32.80  ? 430 LYS A CG  1 
ATOM   2748 C CD  . LYS A 1 430 ? 162.838 170.750 165.277 1.00 37.36  ? 430 LYS A CD  1 
ATOM   2749 C CE  . LYS A 1 430 ? 162.755 169.268 165.131 1.00 40.30  ? 430 LYS A CE  1 
ATOM   2750 N NZ  . LYS A 1 430 ? 163.974 168.603 165.590 1.00 45.75  ? 430 LYS A NZ  1 
ATOM   2751 N N   . GLU A 1 431 ? 163.587 171.923 162.064 1.00 30.38  ? 431 GLU A N   1 
ATOM   2752 C CA  . GLU A 1 431 ? 164.996 171.538 161.780 1.00 33.61  ? 431 GLU A CA  1 
ATOM   2753 C C   . GLU A 1 431 ? 165.208 171.109 160.323 1.00 27.85  ? 431 GLU A C   1 
ATOM   2754 O O   . GLU A 1 431 ? 165.069 169.900 160.057 1.00 30.29  ? 431 GLU A O   1 
ATOM   2755 C CB  . GLU A 1 431 ? 165.418 170.402 162.714 1.00 43.26  ? 431 GLU A CB  1 
ATOM   2756 C CG  . GLU A 1 431 ? 166.891 170.026 162.575 1.00 49.65  ? 431 GLU A CG  1 
ATOM   2757 C CD  . GLU A 1 431 ? 167.380 168.949 163.523 1.00 59.97  ? 431 GLU A CD  1 
ATOM   2758 O OE1 . GLU A 1 431 ? 166.572 168.410 164.307 1.00 53.49  ? 431 GLU A OE1 1 
ATOM   2759 O OE2 . GLU A 1 431 ? 168.592 168.656 163.476 1.00 74.47  ? 431 GLU A OE2 1 
ATOM   2760 N N   . ILE A 1 432 ? 165.546 172.031 159.416 1.00 25.48  ? 432 ILE A N   1 
ATOM   2761 C CA  . ILE A 1 432 ? 165.929 171.685 158.054 1.00 27.72  ? 432 ILE A CA  1 
ATOM   2762 C C   . ILE A 1 432 ? 167.453 171.639 158.054 1.00 48.33  ? 432 ILE A C   1 
ATOM   2763 O O   . ILE A 1 432 ? 168.120 172.675 158.010 1.00 48.85  ? 432 ILE A O   1 
ATOM   2764 C CB  . ILE A 1 432 ? 165.379 172.684 157.035 1.00 23.26  ? 432 ILE A CB  1 
ATOM   2765 C CG1 . ILE A 1 432 ? 163.858 172.581 156.967 1.00 16.41  ? 432 ILE A CG1 1 
ATOM   2766 C CG2 . ILE A 1 432 ? 165.972 172.431 155.671 1.00 34.46  ? 432 ILE A CG2 1 
ATOM   2767 C CD1 . ILE A 1 432 ? 163.221 173.655 156.132 1.00 17.15  ? 432 ILE A CD1 1 
ATOM   2768 N N   . SER A 1 433 ? 168.008 170.429 158.113 1.00 48.57  ? 433 SER A N   1 
ATOM   2769 C CA  . SER A 1 433 ? 169.420 170.270 158.442 1.00 44.84  ? 433 SER A CA  1 
ATOM   2770 C C   . SER A 1 433 ? 170.330 170.630 157.273 1.00 50.54  ? 433 SER A C   1 
ATOM   2771 O O   . SER A 1 433 ? 171.136 171.562 157.366 1.00 56.08  ? 433 SER A O   1 
ATOM   2772 C CB  . SER A 1 433 ? 169.688 168.837 158.905 1.00 46.28  ? 433 SER A CB  1 
ATOM   2773 O OG  . SER A 1 433 ? 169.337 168.669 160.267 1.00 44.71  ? 433 SER A OG  1 
ATOM   2774 N N   . ASP A 1 434 ? 170.216 169.903 156.163 1.00 51.76  ? 434 ASP A N   1 
ATOM   2775 C CA  . ASP A 1 434 ? 171.209 169.982 155.097 1.00 60.23  ? 434 ASP A CA  1 
ATOM   2776 C C   . ASP A 1 434 ? 170.782 170.866 153.932 1.00 59.21  ? 434 ASP A C   1 
ATOM   2777 O O   . ASP A 1 434 ? 171.499 171.804 153.575 1.00 63.59  ? 434 ASP A O   1 
ATOM   2778 C CB  . ASP A 1 434 ? 171.535 168.574 154.585 1.00 59.72  ? 434 ASP A CB  1 
ATOM   2779 C CG  . ASP A 1 434 ? 173.007 168.395 154.276 1.00 68.36  ? 434 ASP A CG  1 
ATOM   2780 O OD1 . ASP A 1 434 ? 173.776 169.361 154.465 1.00 67.18  ? 434 ASP A OD1 1 
ATOM   2781 O OD2 . ASP A 1 434 ? 173.395 167.289 153.846 1.00 66.48  ? 434 ASP A OD2 1 
ATOM   2782 N N   . GLY A 1 435 ? 169.632 170.590 153.329 1.00 48.87  ? 435 GLY A N   1 
ATOM   2783 C CA  . GLY A 1 435 ? 169.268 171.257 152.098 1.00 46.24  ? 435 GLY A CA  1 
ATOM   2784 C C   . GLY A 1 435 ? 168.702 172.649 152.297 1.00 44.57  ? 435 GLY A C   1 
ATOM   2785 O O   . GLY A 1 435 ? 168.442 173.104 153.409 1.00 48.29  ? 435 GLY A O   1 
ATOM   2786 N N   . ASP A 1 436 ? 168.513 173.334 151.172 1.00 45.41  ? 436 ASP A N   1 
ATOM   2787 C CA  . ASP A 1 436 ? 167.880 174.642 151.143 1.00 42.54  ? 436 ASP A CA  1 
ATOM   2788 C C   . ASP A 1 436 ? 166.366 174.461 151.046 1.00 37.78  ? 436 ASP A C   1 
ATOM   2789 O O   . ASP A 1 436 ? 165.849 173.343 151.096 1.00 40.23  ? 436 ASP A O   1 
ATOM   2790 C CB  . ASP A 1 436 ? 168.428 175.470 149.985 1.00 42.26  ? 436 ASP A CB  1 
ATOM   2791 C CG  . ASP A 1 436 ? 169.926 175.670 150.069 1.00 53.48  ? 436 ASP A CG  1 
ATOM   2792 O OD1 . ASP A 1 436 ? 170.640 174.697 150.388 1.00 59.04  ? 436 ASP A OD1 1 
ATOM   2793 O OD2 . ASP A 1 436 ? 170.391 176.801 149.816 1.00 59.58  ? 436 ASP A OD2 1 
ATOM   2794 N N   . VAL A 1 437 ? 165.636 175.564 150.906 1.00 38.46  ? 437 VAL A N   1 
ATOM   2795 C CA  . VAL A 1 437 ? 164.183 175.537 150.787 1.00 30.27  ? 437 VAL A CA  1 
ATOM   2796 C C   . VAL A 1 437 ? 163.773 176.329 149.557 1.00 35.29  ? 437 VAL A C   1 
ATOM   2797 O O   . VAL A 1 437 ? 164.217 177.467 149.369 1.00 42.63  ? 437 VAL A O   1 
ATOM   2798 C CB  . VAL A 1 437 ? 163.487 176.112 152.034 1.00 26.88  ? 437 VAL A CB  1 
ATOM   2799 C CG1 . VAL A 1 437 ? 162.028 175.722 152.025 1.00 28.98  ? 437 VAL A CG1 1 
ATOM   2800 C CG2 . VAL A 1 437 ? 164.162 175.625 153.296 1.00 26.73  ? 437 VAL A CG2 1 
ATOM   2801 N N   . ILE A 1 438 ? 162.924 175.734 148.726 1.00 27.37  ? 438 ILE A N   1 
ATOM   2802 C CA  . ILE A 1 438 ? 162.304 176.426 147.604 1.00 27.03  ? 438 ILE A CA  1 
ATOM   2803 C C   . ILE A 1 438 ? 160.802 176.398 147.824 1.00 29.64  ? 438 ILE A C   1 
ATOM   2804 O O   . ILE A 1 438 ? 160.205 175.322 147.943 1.00 33.65  ? 438 ILE A O   1 
ATOM   2805 C CB  . ILE A 1 438 ? 162.673 175.792 146.254 1.00 30.13  ? 438 ILE A CB  1 
ATOM   2806 C CG1 . ILE A 1 438 ? 161.715 176.273 145.164 1.00 31.47  ? 438 ILE A CG1 1 
ATOM   2807 C CG2 . ILE A 1 438 ? 162.641 174.283 146.344 1.00 35.44  ? 438 ILE A CG2 1 
ATOM   2808 C CD1 . ILE A 1 438 ? 162.076 175.786 143.782 1.00 35.41  ? 438 ILE A CD1 1 
ATOM   2809 N N   . ILE A 1 439 ? 160.193 177.578 147.898 1.00 29.69  ? 439 ILE A N   1 
ATOM   2810 C CA  . ILE A 1 439 ? 158.747 177.714 148.055 1.00 24.85  ? 439 ILE A CA  1 
ATOM   2811 C C   . ILE A 1 439 ? 158.288 178.675 146.962 1.00 32.32  ? 439 ILE A C   1 
ATOM   2812 O O   . ILE A 1 439 ? 158.269 179.895 147.150 1.00 41.37  ? 439 ILE A O   1 
ATOM   2813 C CB  . ILE A 1 439 ? 158.348 178.213 149.446 1.00 21.75  ? 439 ILE A CB  1 
ATOM   2814 C CG1 . ILE A 1 439 ? 159.011 177.344 150.515 1.00 18.14  ? 439 ILE A CG1 1 
ATOM   2815 C CG2 . ILE A 1 439 ? 156.840 178.200 149.597 1.00 25.79  ? 439 ILE A CG2 1 
ATOM   2816 C CD1 . ILE A 1 439 ? 158.296 177.331 151.826 1.00 15.46  ? 439 ILE A CD1 1 
ATOM   2817 N N   . SER A 1 440 ? 157.909 178.126 145.812 1.00 31.33  ? 440 SER A N   1 
ATOM   2818 C CA  . SER A 1 440 ? 157.572 178.916 144.641 1.00 37.90  ? 440 SER A CA  1 
ATOM   2819 C C   . SER A 1 440 ? 156.278 178.405 144.029 1.00 46.84  ? 440 SER A C   1 
ATOM   2820 O O   . SER A 1 440 ? 155.919 177.236 144.183 1.00 52.22  ? 440 SER A O   1 
ATOM   2821 C CB  . SER A 1 440 ? 158.693 178.871 143.598 1.00 42.60  ? 440 SER A CB  1 
ATOM   2822 O OG  . SER A 1 440 ? 158.792 177.584 143.018 1.00 43.17  ? 440 SER A OG  1 
ATOM   2823 N N   . GLY A 1 441 ? 155.578 179.297 143.334 1.00 48.47  ? 441 GLY A N   1 
ATOM   2824 C CA  . GLY A 1 441 ? 154.313 178.956 142.722 1.00 51.61  ? 441 GLY A CA  1 
ATOM   2825 C C   . GLY A 1 441 ? 153.128 178.973 143.659 1.00 52.07  ? 441 GLY A C   1 
ATOM   2826 O O   . GLY A 1 441 ? 152.003 178.720 143.211 1.00 52.94  ? 441 GLY A O   1 
ATOM   2827 N N   . ASN A 1 442 ? 153.339 179.264 144.941 1.00 50.13  ? 442 ASN A N   1 
ATOM   2828 C CA  . ASN A 1 442 ? 152.257 179.359 145.918 1.00 47.85  ? 442 ASN A CA  1 
ATOM   2829 C C   . ASN A 1 442 ? 151.590 180.715 145.740 1.00 61.06  ? 442 ASN A C   1 
ATOM   2830 O O   . ASN A 1 442 ? 151.862 181.668 146.470 1.00 65.97  ? 442 ASN A O   1 
ATOM   2831 C CB  . ASN A 1 442 ? 152.792 179.186 147.334 1.00 38.47  ? 442 ASN A CB  1 
ATOM   2832 C CG  . ASN A 1 442 ? 153.753 178.027 147.457 1.00 30.38  ? 442 ASN A CG  1 
ATOM   2833 O OD1 . ASN A 1 442 ? 154.844 178.049 146.889 1.00 30.55  ? 442 ASN A OD1 1 
ATOM   2834 N ND2 . ASN A 1 442 ? 153.364 177.016 148.220 1.00 25.46  ? 442 ASN A ND2 1 
ATOM   2835 N N   . LYS A 1 443 ? 150.697 180.801 144.751 1.00 65.53  ? 443 LYS A N   1 
ATOM   2836 C CA  . LYS A 1 443 ? 150.088 182.079 144.402 1.00 65.48  ? 443 LYS A CA  1 
ATOM   2837 C C   . LYS A 1 443 ? 149.270 182.674 145.540 1.00 65.05  ? 443 LYS A C   1 
ATOM   2838 O O   . LYS A 1 443 ? 149.007 183.881 145.530 1.00 66.08  ? 443 LYS A O   1 
ATOM   2839 C CB  . LYS A 1 443 ? 149.209 181.917 143.162 1.00 69.18  ? 443 LYS A CB  1 
ATOM   2840 C CG  . LYS A 1 443 ? 149.828 181.058 142.073 1.00 70.00  ? 443 LYS A CG  1 
ATOM   2841 C CD  . LYS A 1 443 ? 149.671 181.704 140.707 1.00 77.00  ? 443 LYS A CD  1 
ATOM   2842 C CE  . LYS A 1 443 ? 150.331 180.869 139.622 1.00 79.99  ? 443 LYS A CE  1 
ATOM   2843 N NZ  . LYS A 1 443 ? 151.774 181.200 139.470 1.00 83.47  ? 443 LYS A NZ  1 
ATOM   2844 N N   . ASN A 1 444 ? 148.865 181.866 146.520 1.00 58.18  ? 444 ASN A N   1 
ATOM   2845 C CA  . ASN A 1 444 ? 148.022 182.341 147.609 1.00 57.99  ? 444 ASN A CA  1 
ATOM   2846 C C   . ASN A 1 444 ? 148.651 182.146 148.983 1.00 55.40  ? 444 ASN A C   1 
ATOM   2847 O O   . ASN A 1 444 ? 147.932 182.173 149.988 1.00 55.18  ? 444 ASN A O   1 
ATOM   2848 C CB  . ASN A 1 444 ? 146.657 181.651 147.557 1.00 59.91  ? 444 ASN A CB  1 
ATOM   2849 C CG  . ASN A 1 444 ? 146.043 181.684 146.173 1.00 61.41  ? 444 ASN A CG  1 
ATOM   2850 O OD1 . ASN A 1 444 ? 145.732 180.645 145.593 1.00 55.16  ? 444 ASN A OD1 1 
ATOM   2851 N ND2 . ASN A 1 444 ? 145.866 182.884 145.634 1.00 68.82  ? 444 ASN A ND2 1 
ATOM   2852 N N   . LEU A 1 445 ? 149.965 181.961 149.062 1.00 53.55  ? 445 LEU A N   1 
ATOM   2853 C CA  . LEU A 1 445 ? 150.668 181.822 150.332 1.00 47.87  ? 445 LEU A CA  1 
ATOM   2854 C C   . LEU A 1 445 ? 151.531 183.056 150.551 1.00 48.48  ? 445 LEU A C   1 
ATOM   2855 O O   . LEU A 1 445 ? 152.395 183.368 149.725 1.00 57.12  ? 445 LEU A O   1 
ATOM   2856 C CB  . LEU A 1 445 ? 151.521 180.555 150.350 1.00 42.93  ? 445 LEU A CB  1 
ATOM   2857 C CG  . LEU A 1 445 ? 152.725 180.505 151.292 1.00 37.12  ? 445 LEU A CG  1 
ATOM   2858 C CD1 . LEU A 1 445 ? 152.284 180.538 152.745 1.00 39.39  ? 445 LEU A CD1 1 
ATOM   2859 C CD2 . LEU A 1 445 ? 153.543 179.260 151.012 1.00 37.76  ? 445 LEU A CD2 1 
ATOM   2860 N N   . CYS A 1 446 ? 151.300 183.752 151.659 1.00 40.63  ? 446 CYS A N   1 
ATOM   2861 C CA  . CYS A 1 446 ? 152.022 184.978 151.976 1.00 50.21  ? 446 CYS A CA  1 
ATOM   2862 C C   . CYS A 1 446 ? 153.003 184.827 153.127 1.00 48.29  ? 446 CYS A C   1 
ATOM   2863 O O   . CYS A 1 446 ? 154.079 185.428 153.096 1.00 49.48  ? 446 CYS A O   1 
ATOM   2864 C CB  . CYS A 1 446 ? 151.031 186.100 152.306 1.00 65.36  ? 446 CYS A CB  1 
ATOM   2865 S SG  . CYS A 1 446 ? 151.714 187.429 153.322 1.00 83.37  ? 446 CYS A SG  1 
ATOM   2866 N N   . TYR A 1 447 ? 152.665 184.023 154.137 1.00 42.34  ? 447 TYR A N   1 
ATOM   2867 C CA  . TYR A 1 447 ? 153.479 183.925 155.341 1.00 35.34  ? 447 TYR A CA  1 
ATOM   2868 C C   . TYR A 1 447 ? 154.803 183.209 155.117 1.00 40.92  ? 447 TYR A C   1 
ATOM   2869 O O   . TYR A 1 447 ? 155.637 183.199 156.028 1.00 42.35  ? 447 TYR A O   1 
ATOM   2870 C CB  . TYR A 1 447 ? 152.701 183.214 156.447 1.00 36.22  ? 447 TYR A CB  1 
ATOM   2871 C CG  . TYR A 1 447 ? 151.209 183.439 156.408 1.00 39.91  ? 447 TYR A CG  1 
ATOM   2872 C CD1 . TYR A 1 447 ? 150.384 182.630 155.641 1.00 41.62  ? 447 TYR A CD1 1 
ATOM   2873 C CD2 . TYR A 1 447 ? 150.624 184.453 157.150 1.00 47.46  ? 447 TYR A CD2 1 
ATOM   2874 C CE1 . TYR A 1 447 ? 149.023 182.828 155.608 1.00 47.12  ? 447 TYR A CE1 1 
ATOM   2875 C CE2 . TYR A 1 447 ? 149.262 184.660 157.124 1.00 53.79  ? 447 TYR A CE2 1 
ATOM   2876 C CZ  . TYR A 1 447 ? 148.466 183.844 156.350 1.00 58.35  ? 447 TYR A CZ  1 
ATOM   2877 O OH  . TYR A 1 447 ? 147.106 184.041 156.319 1.00 80.00  ? 447 TYR A OH  1 
ATOM   2878 N N   . ALA A 1 448 ? 155.014 182.606 153.945 1.00 48.15  ? 448 ALA A N   1 
ATOM   2879 C CA  . ALA A 1 448 ? 156.265 181.897 153.694 1.00 38.22  ? 448 ALA A CA  1 
ATOM   2880 C C   . ALA A 1 448 ? 157.461 182.833 153.791 1.00 40.84  ? 448 ALA A C   1 
ATOM   2881 O O   . ALA A 1 448 ? 158.490 182.478 154.376 1.00 44.34  ? 448 ALA A O   1 
ATOM   2882 C CB  . ALA A 1 448 ? 156.223 181.227 152.322 1.00 34.51  ? 448 ALA A CB  1 
ATOM   2883 N N   . ASN A 1 449 ? 157.346 184.034 153.224 1.00 40.75  ? 449 ASN A N   1 
ATOM   2884 C CA  . ASN A 1 449 ? 158.429 185.004 153.315 1.00 35.71  ? 449 ASN A CA  1 
ATOM   2885 C C   . ASN A 1 449 ? 158.568 185.588 154.713 1.00 35.01  ? 449 ASN A C   1 
ATOM   2886 O O   . ASN A 1 449 ? 159.646 186.082 155.058 1.00 42.16  ? 449 ASN A O   1 
ATOM   2887 C CB  . ASN A 1 449 ? 158.212 186.129 152.304 1.00 33.89  ? 449 ASN A CB  1 
ATOM   2888 C CG  . ASN A 1 449 ? 157.301 187.218 152.834 1.00 53.84  ? 449 ASN A CG  1 
ATOM   2889 O OD1 . ASN A 1 449 ? 157.763 188.271 153.274 1.00 66.46  ? 449 ASN A OD1 1 
ATOM   2890 N ND2 . ASN A 1 449 ? 155.998 186.969 152.796 1.00 53.61  ? 449 ASN A ND2 1 
ATOM   2891 N N   . THR A 1 450 ? 157.510 185.524 155.526 1.00 32.30  ? 450 THR A N   1 
ATOM   2892 C CA  . THR A 1 450 ? 157.541 186.174 156.861 1.00 37.44  ? 450 THR A CA  1 
ATOM   2893 C C   . THR A 1 450 ? 158.476 185.432 157.791 1.00 32.69  ? 450 THR A C   1 
ATOM   2894 O O   . THR A 1 450 ? 159.093 186.093 158.653 1.00 39.21  ? 450 THR A O   1 
ATOM   2895 C CB  . THR A 1 450 ? 156.119 186.216 157.417 1.00 39.86  ? 450 THR A CB  1 
ATOM   2896 O OG1 . THR A 1 450 ? 155.338 186.835 156.399 1.00 55.67  ? 450 THR A OG1 1 
ATOM   2897 C CG2 . THR A 1 450 ? 156.015 187.008 158.708 1.00 46.92  ? 450 THR A CG2 1 
ATOM   2898 N N   . ILE A 1 451 ? 158.604 184.118 157.624 1.00 36.29  ? 451 ILE A N   1 
ATOM   2899 C CA  . ILE A 1 451 ? 159.425 183.264 158.537 1.00 40.37  ? 451 ILE A CA  1 
ATOM   2900 C C   . ILE A 1 451 ? 160.906 183.662 158.458 1.00 42.05  ? 451 ILE A C   1 
ATOM   2901 O O   . ILE A 1 451 ? 161.323 184.122 157.375 1.00 42.46  ? 451 ILE A O   1 
ATOM   2902 C CB  . ILE A 1 451 ? 159.197 181.780 158.194 1.00 33.63  ? 451 ILE A CB  1 
ATOM   2903 C CG1 . ILE A 1 451 ? 157.770 181.352 158.520 1.00 30.30  ? 451 ILE A CG1 1 
ATOM   2904 C CG2 . ILE A 1 451 ? 160.221 180.876 158.882 1.00 32.49  ? 451 ILE A CG2 1 
ATOM   2905 C CD1 . ILE A 1 451 ? 157.310 180.120 157.765 1.00 24.86  ? 451 ILE A CD1 1 
ATOM   2906 N N   . ASN A 1 452 ? 161.638 183.555 159.575 1.00 46.11  ? 452 ASN A N   1 
ATOM   2907 C CA  . ASN A 1 452 ? 163.113 183.768 159.555 1.00 47.49  ? 452 ASN A CA  1 
ATOM   2908 C C   . ASN A 1 452 ? 163.711 182.371 159.411 1.00 48.77  ? 452 ASN A C   1 
ATOM   2909 O O   . ASN A 1 452 ? 163.633 181.599 160.389 1.00 50.47  ? 452 ASN A O   1 
ATOM   2910 C CB  . ASN A 1 452 ? 163.621 184.484 160.798 1.00 50.24  ? 452 ASN A CB  1 
ATOM   2911 C CG  . ASN A 1 452 ? 165.129 184.478 160.874 1.00 52.65  ? 452 ASN A CG  1 
ATOM   2912 O OD1 . ASN A 1 452 ? 165.702 183.934 161.825 1.00 53.44  ? 452 ASN A OD1 1 
ATOM   2913 N ND2 . ASN A 1 452 ? 165.786 185.065 159.885 1.00 51.14  ? 452 ASN A ND2 1 
ATOM   2914 N N   . TRP A 1 453 ? 164.283 182.052 158.252 1.00 45.09  ? 453 TRP A N   1 
ATOM   2915 C CA  . TRP A 1 453 ? 164.717 180.684 158.009 1.00 40.32  ? 453 TRP A CA  1 
ATOM   2916 C C   . TRP A 1 453 ? 166.164 180.431 158.403 1.00 44.78  ? 453 TRP A C   1 
ATOM   2917 O O   . TRP A 1 453 ? 166.673 179.334 158.156 1.00 49.77  ? 453 TRP A O   1 
ATOM   2918 C CB  . TRP A 1 453 ? 164.514 180.307 156.537 1.00 34.40  ? 453 TRP A CB  1 
ATOM   2919 C CG  . TRP A 1 453 ? 163.092 180.427 156.082 1.00 32.24  ? 453 TRP A CG  1 
ATOM   2920 C CD1 . TRP A 1 453 ? 162.329 181.555 156.063 1.00 34.30  ? 453 TRP A CD1 1 
ATOM   2921 C CD2 . TRP A 1 453 ? 162.242 179.362 155.645 1.00 24.09  ? 453 TRP A CD2 1 
ATOM   2922 N NE1 . TRP A 1 453 ? 161.068 181.267 155.605 1.00 28.42  ? 453 TRP A NE1 1 
ATOM   2923 C CE2 . TRP A 1 453 ? 160.988 179.925 155.347 1.00 21.95  ? 453 TRP A CE2 1 
ATOM   2924 C CE3 . TRP A 1 453 ? 162.425 177.990 155.464 1.00 27.52  ? 453 TRP A CE3 1 
ATOM   2925 C CZ2 . TRP A 1 453 ? 159.925 179.165 154.876 1.00 20.82  ? 453 TRP A CZ2 1 
ATOM   2926 C CZ3 . TRP A 1 453 ? 161.367 177.239 155.001 1.00 21.44  ? 453 TRP A CZ3 1 
ATOM   2927 C CH2 . TRP A 1 453 ? 160.134 177.827 154.711 1.00 18.43  ? 453 TRP A CH2 1 
ATOM   2928 N N   . LYS A 1 454 ? 166.843 181.411 159.000 1.00 47.85  ? 454 LYS A N   1 
ATOM   2929 C CA  . LYS A 1 454 ? 168.166 181.149 159.550 1.00 57.08  ? 454 LYS A CA  1 
ATOM   2930 C C   . LYS A 1 454 ? 168.102 180.248 160.776 1.00 47.79  ? 454 LYS A C   1 
ATOM   2931 O O   . LYS A 1 454 ? 169.091 179.580 161.094 1.00 44.17  ? 454 LYS A O   1 
ATOM   2932 C CB  . LYS A 1 454 ? 168.863 182.464 159.901 1.00 68.52  ? 454 LYS A CB  1 
ATOM   2933 C CG  . LYS A 1 454 ? 168.677 183.563 158.864 1.00 63.43  ? 454 LYS A CG  1 
ATOM   2934 C CD  . LYS A 1 454 ? 169.537 183.317 157.636 1.00 68.02  ? 454 LYS A CD  1 
ATOM   2935 C CE  . LYS A 1 454 ? 168.688 183.176 156.384 1.00 65.60  ? 454 LYS A CE  1 
ATOM   2936 N NZ  . LYS A 1 454 ? 169.403 182.426 155.313 1.00 54.94  ? 454 LYS A NZ  1 
ATOM   2937 N N   . LYS A 1 455 ? 166.937 180.204 161.427 1.00 41.98  ? 455 LYS A N   1 
ATOM   2938 C CA  . LYS A 1 455 ? 166.761 179.351 162.631 1.00 43.62  ? 455 LYS A CA  1 
ATOM   2939 C C   . LYS A 1 455 ? 166.553 177.894 162.192 1.00 48.46  ? 455 LYS A C   1 
ATOM   2940 O O   . LYS A 1 455 ? 167.092 176.992 162.868 1.00 59.76  ? 455 LYS A O   1 
ATOM   2941 C CB  . LYS A 1 455 ? 165.577 179.871 163.454 1.00 53.31  ? 455 LYS A CB  1 
ATOM   2942 C CG  . LYS A 1 455 ? 164.459 178.872 163.720 1.00 55.08  ? 455 LYS A CG  1 
ATOM   2943 C CD  . LYS A 1 455 ? 163.186 179.516 164.254 1.00 54.20  ? 455 LYS A CD  1 
ATOM   2944 C CE  . LYS A 1 455 ? 162.636 180.548 163.321 1.00 51.18  ? 455 LYS A CE  1 
ATOM   2945 N NZ  . LYS A 1 455 ? 162.241 179.976 162.032 1.00 46.79  ? 455 LYS A NZ  1 
ATOM   2946 N N   . LEU A 1 456 ? 165.810 177.677 161.103 1.00 45.48  ? 456 LEU A N   1 
ATOM   2947 C CA  . LEU A 1 456 ? 165.533 176.325 160.628 1.00 36.70  ? 456 LEU A CA  1 
ATOM   2948 C C   . LEU A 1 456 ? 166.791 175.650 160.096 1.00 38.36  ? 456 LEU A C   1 
ATOM   2949 O O   . LEU A 1 456 ? 166.993 174.448 160.303 1.00 36.59  ? 456 LEU A O   1 
ATOM   2950 C CB  . LEU A 1 456 ? 164.456 176.361 159.544 1.00 26.92  ? 456 LEU A CB  1 
ATOM   2951 C CG  . LEU A 1 456 ? 163.100 176.965 159.902 1.00 20.16  ? 456 LEU A CG  1 
ATOM   2952 C CD1 . LEU A 1 456 ? 162.067 176.560 158.874 1.00 12.65  ? 456 LEU A CD1 1 
ATOM   2953 C CD2 . LEU A 1 456 ? 162.670 176.533 161.288 1.00 28.01  ? 456 LEU A CD2 1 
ATOM   2954 N N   . PHE A 1 457 ? 167.641 176.405 159.408 1.00 45.50  ? 457 PHE A N   1 
ATOM   2955 C CA  . PHE A 1 457 ? 168.792 175.828 158.729 1.00 50.18  ? 457 PHE A CA  1 
ATOM   2956 C C   . PHE A 1 457 ? 169.782 175.239 159.725 1.00 52.73  ? 457 PHE A C   1 
ATOM   2957 O O   . PHE A 1 457 ? 170.054 175.822 160.777 1.00 54.33  ? 457 PHE A O   1 
ATOM   2958 C CB  . PHE A 1 457 ? 169.475 176.893 157.876 1.00 56.96  ? 457 PHE A CB  1 
ATOM   2959 C CG  . PHE A 1 457 ? 168.706 177.261 156.642 1.00 55.49  ? 457 PHE A CG  1 
ATOM   2960 C CD1 . PHE A 1 457 ? 167.588 176.538 156.267 1.00 44.92  ? 457 PHE A CD1 1 
ATOM   2961 C CD2 . PHE A 1 457 ? 169.089 178.341 155.869 1.00 57.09  ? 457 PHE A CD2 1 
ATOM   2962 C CE1 . PHE A 1 457 ? 166.878 176.876 155.140 1.00 40.31  ? 457 PHE A CE1 1 
ATOM   2963 C CE2 . PHE A 1 457 ? 168.380 178.681 154.738 1.00 55.87  ? 457 PHE A CE2 1 
ATOM   2964 C CZ  . PHE A 1 457 ? 167.274 177.947 154.375 1.00 43.32  ? 457 PHE A CZ  1 
ATOM   2965 N N   . GLY A 1 458 ? 170.322 174.072 159.383 1.00 58.58  ? 458 GLY A N   1 
ATOM   2966 C CA  . GLY A 1 458 ? 171.288 173.405 160.233 1.00 65.02  ? 458 GLY A CA  1 
ATOM   2967 C C   . GLY A 1 458 ? 172.724 173.621 159.801 1.00 75.42  ? 458 GLY A C   1 
ATOM   2968 O O   . GLY A 1 458 ? 173.656 173.243 160.518 1.00 77.32  ? 458 GLY A O   1 
ATOM   2969 N N   . THR A 1 459 ? 172.917 174.227 158.632 1.00 77.81  ? 459 THR A N   1 
ATOM   2970 C CA  . THR A 1 459 ? 174.246 174.499 158.105 1.00 79.06  ? 459 THR A CA  1 
ATOM   2971 C C   . THR A 1 459 ? 174.248 175.869 157.441 1.00 75.87  ? 459 THR A C   1 
ATOM   2972 O O   . THR A 1 459 ? 173.197 176.440 157.137 1.00 73.03  ? 459 THR A O   1 
ATOM   2973 C CB  . THR A 1 459 ? 174.698 173.419 157.113 1.00 81.64  ? 459 THR A CB  1 
ATOM   2974 O OG1 . THR A 1 459 ? 173.583 173.003 156.315 1.00 73.87  ? 459 THR A OG1 1 
ATOM   2975 C CG2 . THR A 1 459 ? 175.265 172.217 157.852 1.00 85.68  ? 459 THR A CG2 1 
ATOM   2976 N N   . SER A 1 460 ? 175.450 176.397 157.216 1.00 79.98  ? 460 SER A N   1 
ATOM   2977 C CA  . SER A 1 460 ? 175.619 177.731 156.657 1.00 92.07  ? 460 SER A CA  1 
ATOM   2978 C C   . SER A 1 460 ? 175.562 177.762 155.135 1.00 91.32  ? 460 SER A C   1 
ATOM   2979 O O   . SER A 1 460 ? 175.577 178.853 154.555 1.00 84.37  ? 460 SER A O   1 
ATOM   2980 C CB  . SER A 1 460 ? 176.948 178.333 157.125 1.00 97.59  ? 460 SER A CB  1 
ATOM   2981 O OG  . SER A 1 460 ? 177.989 178.044 156.208 1.00 103.79 ? 460 SER A OG  1 
ATOM   2982 N N   . GLY A 1 461 ? 175.498 176.608 154.477 1.00 88.39  ? 461 GLY A N   1 
ATOM   2983 C CA  . GLY A 1 461 ? 175.468 176.569 153.028 1.00 84.83  ? 461 GLY A CA  1 
ATOM   2984 C C   . GLY A 1 461 ? 174.065 176.532 152.458 1.00 83.24  ? 461 GLY A C   1 
ATOM   2985 O O   . GLY A 1 461 ? 173.867 176.156 151.299 1.00 81.39  ? 461 GLY A O   1 
ATOM   2986 N N   . GLN A 1 462 ? 173.083 176.922 153.264 1.00 73.85  ? 462 GLN A N   1 
ATOM   2987 C CA  . GLN A 1 462 ? 171.678 176.847 152.894 1.00 60.07  ? 462 GLN A CA  1 
ATOM   2988 C C   . GLN A 1 462 ? 171.100 178.244 152.715 1.00 56.32  ? 462 GLN A C   1 
ATOM   2989 O O   . GLN A 1 462 ? 171.424 179.162 153.474 1.00 64.17  ? 462 GLN A O   1 
ATOM   2990 C CB  . GLN A 1 462 ? 170.881 176.086 153.954 1.00 57.85  ? 462 GLN A CB  1 
ATOM   2991 C CG  . GLN A 1 462 ? 171.625 174.907 154.550 1.00 60.79  ? 462 GLN A CG  1 
ATOM   2992 C CD  . GLN A 1 462 ? 170.851 174.232 155.661 1.00 57.31  ? 462 GLN A CD  1 
ATOM   2993 O OE1 . GLN A 1 462 ? 171.173 174.383 156.838 1.00 62.73  ? 462 GLN A OE1 1 
ATOM   2994 N NE2 . GLN A 1 462 ? 169.818 173.487 155.292 1.00 53.40  ? 462 GLN A NE2 1 
ATOM   2995 N N   . LYS A 1 463 ? 170.244 178.397 151.707 1.00 50.98  ? 463 LYS A N   1 
ATOM   2996 C CA  . LYS A 1 463 ? 169.582 179.668 151.445 1.00 52.21  ? 463 LYS A CA  1 
ATOM   2997 C C   . LYS A 1 463 ? 168.235 179.398 150.793 1.00 51.67  ? 463 LYS A C   1 
ATOM   2998 O O   . LYS A 1 463 ? 168.150 178.616 149.843 1.00 53.60  ? 463 LYS A O   1 
ATOM   2999 C CB  . LYS A 1 463 ? 170.440 180.565 150.546 1.00 47.99  ? 463 LYS A CB  1 
ATOM   3000 C CG  . LYS A 1 463 ? 169.793 181.896 150.199 1.00 47.43  ? 463 LYS A CG  1 
ATOM   3001 C CD  . LYS A 1 463 ? 169.849 182.860 151.372 1.00 47.49  ? 463 LYS A CD  1 
ATOM   3002 C CE  . LYS A 1 463 ? 168.501 183.521 151.612 1.00 43.50  ? 463 LYS A CE  1 
ATOM   3003 N NZ  . LYS A 1 463 ? 167.648 182.730 152.542 1.00 40.09  ? 463 LYS A NZ  1 
ATOM   3004 N N   . THR A 1 464 ? 167.194 180.055 151.297 1.00 47.99  ? 464 THR A N   1 
ATOM   3005 C CA  . THR A 1 464 ? 165.846 179.846 150.791 1.00 42.82  ? 464 THR A CA  1 
ATOM   3006 C C   . THR A 1 464 ? 165.689 180.419 149.385 1.00 47.99  ? 464 THR A C   1 
ATOM   3007 O O   . THR A 1 464 ? 166.492 181.230 148.917 1.00 63.31  ? 464 THR A O   1 
ATOM   3008 C CB  . THR A 1 464 ? 164.818 180.486 151.721 1.00 43.84  ? 464 THR A CB  1 
ATOM   3009 O OG1 . THR A 1 464 ? 165.273 181.788 152.110 1.00 54.64  ? 464 THR A OG1 1 
ATOM   3010 C CG2 . THR A 1 464 ? 164.612 179.632 152.956 1.00 39.28  ? 464 THR A CG2 1 
ATOM   3011 N N   . LYS A 1 465 ? 164.630 179.981 148.711 1.00 37.19  ? 465 LYS A N   1 
ATOM   3012 C CA  . LYS A 1 465 ? 164.279 180.439 147.370 1.00 42.44  ? 465 LYS A CA  1 
ATOM   3013 C C   . LYS A 1 465 ? 162.792 180.768 147.302 1.00 49.14  ? 465 LYS A C   1 
ATOM   3014 O O   . LYS A 1 465 ? 162.081 180.388 146.370 1.00 50.78  ? 465 LYS A O   1 
ATOM   3015 C CB  . LYS A 1 465 ? 164.656 179.395 146.324 1.00 47.32  ? 465 LYS A CB  1 
ATOM   3016 C CG  . LYS A 1 465 ? 164.841 179.950 144.921 1.00 53.32  ? 465 LYS A CG  1 
ATOM   3017 C CD  . LYS A 1 465 ? 165.369 178.888 143.974 1.00 52.97  ? 465 LYS A CD  1 
ATOM   3018 C CE  . LYS A 1 465 ? 165.365 179.381 142.538 1.00 59.59  ? 465 LYS A CE  1 
ATOM   3019 N NZ  . LYS A 1 465 ? 164.228 180.306 142.278 1.00 61.53  ? 465 LYS A NZ  1 
ATOM   3020 N N   . ILE A 1 466 ? 162.304 181.493 148.306 1.00 48.23  ? 466 ILE A N   1 
ATOM   3021 C CA  . ILE A 1 466 ? 160.885 181.825 148.417 1.00 40.33  ? 466 ILE A CA  1 
ATOM   3022 C C   . ILE A 1 466 ? 160.598 182.973 147.454 1.00 46.56  ? 466 ILE A C   1 
ATOM   3023 O O   . ILE A 1 466 ? 160.833 184.139 147.773 1.00 46.61  ? 466 ILE A O   1 
ATOM   3024 C CB  . ILE A 1 466 ? 160.498 182.184 149.852 1.00 38.71  ? 466 ILE A CB  1 
ATOM   3025 C CG1 . ILE A 1 466 ? 161.268 181.308 150.839 1.00 33.23  ? 466 ILE A CG1 1 
ATOM   3026 C CG2 . ILE A 1 466 ? 159.000 182.037 150.045 1.00 42.68  ? 466 ILE A CG2 1 
ATOM   3027 C CD1 . ILE A 1 466 ? 160.762 181.399 152.252 1.00 31.95  ? 466 ILE A CD1 1 
ATOM   3028 N N   . ILE A 1 467 ? 160.080 182.645 146.269 1.00 51.21  ? 467 ILE A N   1 
ATOM   3029 C CA  . ILE A 1 467 ? 159.723 183.637 145.264 1.00 53.59  ? 467 ILE A CA  1 
ATOM   3030 C C   . ILE A 1 467 ? 158.432 183.210 144.579 1.00 58.51  ? 467 ILE A C   1 
ATOM   3031 O O   . ILE A 1 467 ? 158.013 182.054 144.659 1.00 59.77  ? 467 ILE A O   1 
ATOM   3032 C CB  . ILE A 1 467 ? 160.847 183.845 144.223 1.00 56.70  ? 467 ILE A CB  1 
ATOM   3033 C CG1 . ILE A 1 467 ? 161.139 182.544 143.467 1.00 55.89  ? 467 ILE A CG1 1 
ATOM   3034 C CG2 . ILE A 1 467 ? 162.106 184.376 144.893 1.00 51.31  ? 467 ILE A CG2 1 
ATOM   3035 C CD1 . ILE A 1 467 ? 162.073 182.703 142.284 1.00 54.98  ? 467 ILE A CD1 1 
ATOM   3036 N N   . SER A 1 468 ? 157.804 184.170 143.899 1.00 61.16  ? 468 SER A N   1 
ATOM   3037 C CA  . SER A 1 468 ? 156.577 183.941 143.132 1.00 69.05  ? 468 SER A CA  1 
ATOM   3038 C C   . SER A 1 468 ? 155.410 183.517 144.020 1.00 71.00  ? 468 SER A C   1 
ATOM   3039 O O   . SER A 1 468 ? 154.497 182.821 143.571 1.00 65.23  ? 468 SER A O   1 
ATOM   3040 C CB  . SER A 1 468 ? 156.798 182.912 142.018 1.00 64.46  ? 468 SER A CB  1 
ATOM   3041 O OG  . SER A 1 468 ? 158.034 183.130 141.361 1.00 68.01  ? 468 SER A OG  1 
ATOM   3042 N N   . ASN A 1 469 ? 155.427 183.930 145.284 1.00 73.08  ? 469 ASN A N   1 
ATOM   3043 C CA  . ASN A 1 469 ? 154.296 183.723 146.175 1.00 65.26  ? 469 ASN A CA  1 
ATOM   3044 C C   . ASN A 1 469 ? 153.283 184.850 145.974 1.00 72.92  ? 469 ASN A C   1 
ATOM   3045 O O   . ASN A 1 469 ? 153.379 185.642 145.034 1.00 82.94  ? 469 ASN A O   1 
ATOM   3046 C CB  . ASN A 1 469 ? 154.760 183.644 147.629 1.00 51.82  ? 469 ASN A CB  1 
ATOM   3047 C CG  . ASN A 1 469 ? 155.775 182.548 147.861 1.00 43.63  ? 469 ASN A CG  1 
ATOM   3048 O OD1 . ASN A 1 469 ? 156.590 182.247 146.994 1.00 45.15  ? 469 ASN A OD1 1 
ATOM   3049 N ND2 . ASN A 1 469 ? 155.733 181.946 149.041 1.00 43.10  ? 469 ASN A ND2 1 
ATOM   3050 N N   . ARG A 1 470 ? 152.292 184.927 146.858 1.00 63.61  ? 470 ARG A N   1 
ATOM   3051 C CA  . ARG A 1 470 ? 151.380 186.061 146.857 1.00 70.44  ? 470 ARG A CA  1 
ATOM   3052 C C   . ARG A 1 470 ? 152.135 187.335 147.214 1.00 79.00  ? 470 ARG A C   1 
ATOM   3053 O O   . ARG A 1 470 ? 153.032 187.325 148.062 1.00 75.28  ? 470 ARG A O   1 
ATOM   3054 C CB  . ARG A 1 470 ? 150.234 185.820 147.843 1.00 71.54  ? 470 ARG A CB  1 
ATOM   3055 C CG  . ARG A 1 470 ? 149.810 187.043 148.642 1.00 76.95  ? 470 ARG A CG  1 
ATOM   3056 C CD  . ARG A 1 470 ? 148.554 186.766 149.449 1.00 79.31  ? 470 ARG A CD  1 
ATOM   3057 N NE  . ARG A 1 470 ? 147.398 186.528 148.593 1.00 84.48  ? 470 ARG A NE  1 
ATOM   3058 C CZ  . ARG A 1 470 ? 146.682 187.485 148.019 1.00 89.25  ? 470 ARG A CZ  1 
ATOM   3059 N NH1 . ARG A 1 470 ? 146.971 188.764 148.193 1.00 90.60  ? 470 ARG A NH1 1 
ATOM   3060 N NH2 . ARG A 1 470 ? 145.649 187.149 147.251 1.00 85.96  ? 470 ARG A NH2 1 
ATOM   3061 N N   . GLY A 1 471 ? 151.778 188.433 146.550 1.00 86.58  ? 471 GLY A N   1 
ATOM   3062 C CA  . GLY A 1 471 ? 152.444 189.703 146.766 1.00 92.07  ? 471 GLY A CA  1 
ATOM   3063 C C   . GLY A 1 471 ? 152.418 190.161 148.209 1.00 97.06  ? 471 GLY A C   1 
ATOM   3064 O O   . GLY A 1 471 ? 151.367 190.141 148.856 1.00 98.24  ? 471 GLY A O   1 
ATOM   3065 N N   . GLU A 1 472 ? 153.579 190.571 148.724 1.00 102.02 ? 472 GLU A N   1 
ATOM   3066 C CA  . GLU A 1 472 ? 153.669 190.975 150.124 1.00 105.84 ? 472 GLU A CA  1 
ATOM   3067 C C   . GLU A 1 472 ? 152.840 192.224 150.399 1.00 107.58 ? 472 GLU A C   1 
ATOM   3068 O O   . GLU A 1 472 ? 152.177 192.319 151.437 1.00 112.14 ? 472 GLU A O   1 
ATOM   3069 C CB  . GLU A 1 472 ? 155.130 191.205 150.510 1.00 108.28 ? 472 GLU A CB  1 
ATOM   3070 C CG  . GLU A 1 472 ? 156.069 190.089 150.082 1.00 102.38 ? 472 GLU A CG  1 
ATOM   3071 C CD  . GLU A 1 472 ? 156.754 190.379 148.761 1.00 101.29 ? 472 GLU A CD  1 
ATOM   3072 O OE1 . GLU A 1 472 ? 156.254 191.239 148.006 1.00 106.00 ? 472 GLU A OE1 1 
ATOM   3073 O OE2 . GLU A 1 472 ? 157.792 189.746 148.477 1.00 87.42  ? 472 GLU A OE2 1 
ATOM   3074 N N   . ASN A 1 473 ? 152.873 193.197 149.485 1.00 104.30 ? 473 ASN A N   1 
ATOM   3075 C CA  . ASN A 1 473 ? 152.116 194.429 149.687 1.00 109.98 ? 473 ASN A CA  1 
ATOM   3076 C C   . ASN A 1 473 ? 150.618 194.144 149.695 1.00 107.29 ? 473 ASN A C   1 
ATOM   3077 O O   . ASN A 1 473 ? 149.885 194.628 150.567 1.00 108.53 ? 473 ASN A O   1 
ATOM   3078 C CB  . ASN A 1 473 ? 152.483 195.441 148.596 1.00 120.94 ? 473 ASN A CB  1 
ATOM   3079 C CG  . ASN A 1 473 ? 151.663 196.726 148.663 1.00 126.59 ? 473 ASN A CG  1 
ATOM   3080 O OD1 . ASN A 1 473 ? 150.901 196.957 149.602 1.00 126.47 ? 473 ASN A OD1 1 
ATOM   3081 N ND2 . ASN A 1 473 ? 151.823 197.571 147.652 1.00 125.29 ? 473 ASN A ND2 1 
ATOM   3082 N N   . SER A 1 474 ? 150.147 193.346 148.733 1.00 105.72 ? 474 SER A N   1 
ATOM   3083 C CA  . SER A 1 474 ? 148.735 192.976 148.704 1.00 109.76 ? 474 SER A CA  1 
ATOM   3084 C C   . SER A 1 474 ? 148.359 192.164 149.934 1.00 105.77 ? 474 SER A C   1 
ATOM   3085 O O   . SER A 1 474 ? 147.262 192.324 150.483 1.00 105.19 ? 474 SER A O   1 
ATOM   3086 C CB  . SER A 1 474 ? 148.423 192.194 147.429 1.00 112.99 ? 474 SER A CB  1 
ATOM   3087 O OG  . SER A 1 474 ? 148.999 190.901 147.470 1.00 99.57  ? 474 SER A OG  1 
ATOM   3088 N N   . CYS A 1 475 ? 149.256 191.280 150.375 1.00 102.81 ? 475 CYS A N   1 
ATOM   3089 C CA  . CYS A 1 475 ? 149.008 190.496 151.580 1.00 98.91  ? 475 CYS A CA  1 
ATOM   3090 C C   . CYS A 1 475 ? 148.847 191.389 152.804 1.00 97.42  ? 475 CYS A C   1 
ATOM   3091 O O   . CYS A 1 475 ? 147.944 191.176 153.622 1.00 97.94  ? 475 CYS A O   1 
ATOM   3092 C CB  . CYS A 1 475 ? 150.148 189.503 151.789 1.00 96.64  ? 475 CYS A CB  1 
ATOM   3093 S SG  . CYS A 1 475 ? 150.208 188.783 153.430 1.00 97.41  ? 475 CYS A SG  1 
ATOM   3094 N N   . LYS A 1 476 ? 149.719 192.387 152.952 1.00 102.09 ? 476 LYS A N   1 
ATOM   3095 C CA  . LYS A 1 476 ? 149.603 193.310 154.077 1.00 103.15 ? 476 LYS A CA  1 
ATOM   3096 C C   . LYS A 1 476 ? 148.328 194.138 153.978 1.00 107.22 ? 476 LYS A C   1 
ATOM   3097 O O   . LYS A 1 476 ? 147.662 194.392 154.988 1.00 108.56 ? 476 LYS A O   1 
ATOM   3098 C CB  . LYS A 1 476 ? 150.828 194.223 154.142 1.00 106.29 ? 476 LYS A CB  1 
ATOM   3099 C CG  . LYS A 1 476 ? 152.161 193.521 154.398 1.00 107.39 ? 476 LYS A CG  1 
ATOM   3100 C CD  . LYS A 1 476 ? 152.003 192.210 155.154 1.00 104.70 ? 476 LYS A CD  1 
ATOM   3101 C CE  . LYS A 1 476 ? 153.347 191.527 155.354 1.00 100.62 ? 476 LYS A CE  1 
ATOM   3102 N NZ  . LYS A 1 476 ? 153.985 191.167 154.058 1.00 96.26  ? 476 LYS A NZ  1 
ATOM   3103 N N   . ALA A 1 477 ? 147.976 194.572 152.765 1.00 108.62 ? 477 ALA A N   1 
ATOM   3104 C CA  . ALA A 1 477 ? 146.790 195.404 152.587 1.00 107.05 ? 477 ALA A CA  1 
ATOM   3105 C C   . ALA A 1 477 ? 145.511 194.632 152.890 1.00 108.55 ? 477 ALA A C   1 
ATOM   3106 O O   . ALA A 1 477 ? 144.577 195.179 153.487 1.00 106.18 ? 477 ALA A O   1 
ATOM   3107 C CB  . ALA A 1 477 ? 146.753 195.967 151.167 1.00 107.01 ? 477 ALA A CB  1 
ATOM   3108 N N   . THR A 1 478 ? 145.448 193.363 152.490 1.00 109.14 ? 478 THR A N   1 
ATOM   3109 C CA  . THR A 1 478 ? 144.245 192.562 152.674 1.00 106.43 ? 478 THR A CA  1 
ATOM   3110 C C   . THR A 1 478 ? 144.121 191.987 154.078 1.00 103.67 ? 478 THR A C   1 
ATOM   3111 O O   . THR A 1 478 ? 143.129 191.309 154.366 1.00 102.68 ? 478 THR A O   1 
ATOM   3112 C CB  . THR A 1 478 ? 144.203 191.421 151.653 1.00 104.53 ? 478 THR A CB  1 
ATOM   3113 O OG1 . THR A 1 478 ? 142.888 190.853 151.623 1.00 113.20 ? 478 THR A OG1 1 
ATOM   3114 C CG2 . THR A 1 478 ? 145.204 190.338 152.020 1.00 94.14  ? 478 THR A CG2 1 
ATOM   3115 N N   . GLY A 1 479 ? 145.092 192.236 154.952 1.00 102.21 ? 479 GLY A N   1 
ATOM   3116 C CA  . GLY A 1 479 ? 145.029 191.712 156.299 1.00 94.33  ? 479 GLY A CA  1 
ATOM   3117 C C   . GLY A 1 479 ? 145.432 190.265 156.437 1.00 90.74  ? 479 GLY A C   1 
ATOM   3118 O O   . GLY A 1 479 ? 145.191 189.666 157.490 1.00 90.37  ? 479 GLY A O   1 
ATOM   3119 N N   . GLN A 1 480 ? 146.046 189.678 155.408 1.00 94.59  ? 480 GLN A N   1 
ATOM   3120 C CA  . GLN A 1 480 ? 146.497 188.295 155.491 1.00 87.59  ? 480 GLN A CA  1 
ATOM   3121 C C   . GLN A 1 480 ? 147.845 188.220 156.195 1.00 81.98  ? 480 GLN A C   1 
ATOM   3122 O O   . GLN A 1 480 ? 148.765 187.543 155.728 1.00 72.47  ? 480 GLN A O   1 
ATOM   3123 C CB  . GLN A 1 480 ? 146.589 187.677 154.094 1.00 82.07  ? 480 GLN A CB  1 
ATOM   3124 C CG  . GLN A 1 480 ? 146.456 186.166 154.060 1.00 69.88  ? 480 GLN A CG  1 
ATOM   3125 C CD  . GLN A 1 480 ? 145.050 185.697 154.361 1.00 81.45  ? 480 GLN A CD  1 
ATOM   3126 O OE1 . GLN A 1 480 ? 144.084 186.435 154.175 1.00 91.07  ? 480 GLN A OE1 1 
ATOM   3127 N NE2 . GLN A 1 480 ? 144.927 184.461 154.830 1.00 76.51  ? 480 GLN A NE2 1 
ATOM   3128 N N   . VAL A 1 481 ? 147.955 188.880 157.341 1.00 87.26  ? 481 VAL A N   1 
ATOM   3129 C CA  . VAL A 1 481 ? 149.155 188.851 158.163 1.00 82.10  ? 481 VAL A CA  1 
ATOM   3130 C C   . VAL A 1 481 ? 148.793 188.158 159.466 1.00 87.29  ? 481 VAL A C   1 
ATOM   3131 O O   . VAL A 1 481 ? 147.675 188.318 159.972 1.00 89.57  ? 481 VAL A O   1 
ATOM   3132 C CB  . VAL A 1 481 ? 149.729 190.263 158.399 1.00 84.50  ? 481 VAL A CB  1 
ATOM   3133 C CG1 . VAL A 1 481 ? 149.035 190.968 159.558 1.00 85.40  ? 481 VAL A CG1 1 
ATOM   3134 C CG2 . VAL A 1 481 ? 151.230 190.194 158.635 1.00 82.58  ? 481 VAL A CG2 1 
ATOM   3135 N N   . CYS A 1 482 ? 149.710 187.345 159.976 1.00 90.79  ? 482 CYS A N   1 
ATOM   3136 C CA  . CYS A 1 482 ? 149.409 186.564 161.160 1.00 77.06  ? 482 CYS A CA  1 
ATOM   3137 C C   . CYS A 1 482 ? 149.317 187.459 162.392 1.00 73.97  ? 482 CYS A C   1 
ATOM   3138 O O   . CYS A 1 482 ? 149.542 188.670 162.341 1.00 77.31  ? 482 CYS A O   1 
ATOM   3139 C CB  . CYS A 1 482 ? 150.451 185.469 161.352 1.00 76.14  ? 482 CYS A CB  1 
ATOM   3140 S SG  . CYS A 1 482 ? 152.142 185.958 161.005 1.00 95.47  ? 482 CYS A SG  1 
ATOM   3141 N N   . HIS A 1 483 ? 148.976 186.828 163.512 1.00 68.26  ? 483 HIS A N   1 
ATOM   3142 C CA  . HIS A 1 483 ? 148.620 187.558 164.720 1.00 76.68  ? 483 HIS A CA  1 
ATOM   3143 C C   . HIS A 1 483 ? 149.752 188.470 165.169 1.00 73.29  ? 483 HIS A C   1 
ATOM   3144 O O   . HIS A 1 483 ? 150.932 188.122 165.069 1.00 79.82  ? 483 HIS A O   1 
ATOM   3145 C CB  . HIS A 1 483 ? 148.192 186.564 165.799 1.00 75.14  ? 483 HIS A CB  1 
ATOM   3146 C CG  . HIS A 1 483 ? 146.748 186.180 165.732 1.00 82.45  ? 483 HIS A CG  1 
ATOM   3147 N ND1 . HIS A 1 483 ? 145.913 186.229 166.827 1.00 77.50  ? 483 HIS A ND1 1 
ATOM   3148 C CD2 . HIS A 1 483 ? 145.989 185.742 164.700 1.00 87.02  ? 483 HIS A CD2 1 
ATOM   3149 C CE1 . HIS A 1 483 ? 144.703 185.837 166.473 1.00 78.98  ? 483 HIS A CE1 1 
ATOM   3150 N NE2 . HIS A 1 483 ? 144.722 185.536 165.187 1.00 83.11  ? 483 HIS A NE2 1 
ATOM   3151 N N   . ALA A 1 484 ? 149.383 189.655 165.659 1.00 64.84  ? 484 ALA A N   1 
ATOM   3152 C CA  . ALA A 1 484 ? 150.345 190.507 166.342 1.00 68.96  ? 484 ALA A CA  1 
ATOM   3153 C C   . ALA A 1 484 ? 150.854 189.865 167.622 1.00 67.54  ? 484 ALA A C   1 
ATOM   3154 O O   . ALA A 1 484 ? 151.870 190.313 168.164 1.00 66.33  ? 484 ALA A O   1 
ATOM   3155 C CB  . ALA A 1 484 ? 149.720 191.868 166.652 1.00 76.73  ? 484 ALA A CB  1 
ATOM   3156 N N   . LEU A 1 485 ? 150.172 188.833 168.109 1.00 65.41  ? 485 LEU A N   1 
ATOM   3157 C CA  . LEU A 1 485 ? 150.613 188.053 169.260 1.00 60.37  ? 485 LEU A CA  1 
ATOM   3158 C C   . LEU A 1 485 ? 151.618 186.993 168.811 1.00 58.02  ? 485 LEU A C   1 
ATOM   3159 O O   . LEU A 1 485 ? 151.465 185.802 169.062 1.00 61.60  ? 485 LEU A O   1 
ATOM   3160 C CB  . LEU A 1 485 ? 149.399 187.426 169.935 1.00 59.40  ? 485 LEU A CB  1 
ATOM   3161 C CG  . LEU A 1 485 ? 149.348 186.955 171.396 1.00 71.28  ? 485 LEU A CG  1 
ATOM   3162 C CD1 . LEU A 1 485 ? 147.913 186.550 171.707 1.00 66.17  ? 485 LEU A CD1 1 
ATOM   3163 C CD2 . LEU A 1 485 ? 150.324 185.856 171.789 1.00 68.13  ? 485 LEU A CD2 1 
ATOM   3164 N N   . CYS A 1 486 ? 152.648 187.435 168.092 1.00 58.17  ? 486 CYS A N   1 
ATOM   3165 C CA  . CYS A 1 486 ? 153.687 186.548 167.592 1.00 48.82  ? 486 CYS A CA  1 
ATOM   3166 C C   . CYS A 1 486 ? 154.970 187.345 167.427 1.00 51.85  ? 486 CYS A C   1 
ATOM   3167 O O   . CYS A 1 486 ? 154.933 188.536 167.108 1.00 58.91  ? 486 CYS A O   1 
ATOM   3168 C CB  . CYS A 1 486 ? 153.295 185.892 166.262 1.00 43.53  ? 486 CYS A CB  1 
ATOM   3169 S SG  . CYS A 1 486 ? 152.189 184.465 166.415 1.00 58.68  ? 486 CYS A SG  1 
ATOM   3170 N N   . SER A 1 487 ? 156.107 186.686 167.657 1.00 53.38  ? 487 SER A N   1 
ATOM   3171 C CA  . SER A 1 487 ? 157.420 187.365 167.527 1.00 58.64  ? 487 SER A CA  1 
ATOM   3172 C C   . SER A 1 487 ? 157.683 187.680 166.049 1.00 60.66  ? 487 SER A C   1 
ATOM   3173 O O   . SER A 1 487 ? 157.203 186.911 165.187 1.00 59.74  ? 487 SER A O   1 
ATOM   3174 C CB  . SER A 1 487 ? 158.518 186.517 168.115 1.00 59.43  ? 487 SER A CB  1 
ATOM   3175 O OG  . SER A 1 487 ? 159.803 187.023 167.784 1.00 61.88  ? 487 SER A OG  1 
ATOM   3176 N N   . PRO A 1 488 ? 158.427 188.757 165.711 1.00 59.59  ? 488 PRO A N   1 
ATOM   3177 C CA  . PRO A 1 488 ? 158.763 189.042 164.321 1.00 50.75  ? 488 PRO A CA  1 
ATOM   3178 C C   . PRO A 1 488 ? 159.548 187.906 163.678 1.00 44.80  ? 488 PRO A C   1 
ATOM   3179 O O   . PRO A 1 488 ? 159.808 187.970 162.460 1.00 47.63  ? 488 PRO A O   1 
ATOM   3180 C CB  . PRO A 1 488 ? 159.598 190.329 164.424 1.00 53.16  ? 488 PRO A CB  1 
ATOM   3181 C CG  . PRO A 1 488 ? 159.159 190.950 165.729 1.00 50.45  ? 488 PRO A CG  1 
ATOM   3182 C CD  . PRO A 1 488 ? 158.915 189.762 166.641 1.00 53.32  ? 488 PRO A CD  1 
ATOM   3183 N N   . GLU A 1 489 ? 159.910 186.888 164.464 1.00 45.32  ? 489 GLU A N   1 
ATOM   3184 C CA  . GLU A 1 489 ? 160.700 185.739 163.949 1.00 46.41  ? 489 GLU A CA  1 
ATOM   3185 C C   . GLU A 1 489 ? 159.988 185.116 162.737 1.00 40.25  ? 489 GLU A C   1 
ATOM   3186 O O   . GLU A 1 489 ? 160.686 184.535 161.883 1.00 39.68  ? 489 GLU A O   1 
ATOM   3187 C CB  . GLU A 1 489 ? 160.900 184.738 165.086 1.00 48.43  ? 489 GLU A CB  1 
ATOM   3188 C CG  . GLU A 1 489 ? 162.121 183.842 164.900 1.00 53.25  ? 489 GLU A CG  1 
ATOM   3189 C CD  . GLU A 1 489 ? 162.603 183.234 166.204 1.00 64.92  ? 489 GLU A CD  1 
ATOM   3190 O OE1 . GLU A 1 489 ? 162.970 184.010 167.111 1.00 67.07  ? 489 GLU A OE1 1 
ATOM   3191 O OE2 . GLU A 1 489 ? 162.602 181.992 166.321 1.00 74.72  ? 489 GLU A OE2 1 
ATOM   3192 N N   . GLY A 1 490 ? 158.658 185.217 162.668 1.00 34.86  ? 490 GLY A N   1 
ATOM   3193 C CA  . GLY A 1 490 ? 157.934 184.713 161.484 1.00 35.33  ? 490 GLY A CA  1 
ATOM   3194 C C   . GLY A 1 490 ? 156.708 183.917 161.872 1.00 37.35  ? 490 GLY A C   1 
ATOM   3195 O O   . GLY A 1 490 ? 156.386 183.885 163.077 1.00 48.48  ? 490 GLY A O   1 
ATOM   3196 N N   . CYS A 1 491 ? 156.053 183.287 160.892 1.00 30.40  ? 491 CYS A N   1 
ATOM   3197 C CA  . CYS A 1 491 ? 154.847 182.520 161.165 1.00 24.09  ? 491 CYS A CA  1 
ATOM   3198 C C   . CYS A 1 491 ? 154.492 181.666 159.958 1.00 27.91  ? 491 CYS A C   1 
ATOM   3199 O O   . CYS A 1 491 ? 154.663 182.096 158.817 1.00 41.70  ? 491 CYS A O   1 
ATOM   3200 C CB  . CYS A 1 491 ? 153.687 183.451 161.530 1.00 28.20  ? 491 CYS A CB  1 
ATOM   3201 S SG  . CYS A 1 491 ? 152.907 184.285 160.147 1.00 58.17  ? 491 CYS A SG  1 
ATOM   3202 N N   . TRP A 1 492 ? 154.001 180.455 160.222 1.00 31.64  ? 492 TRP A N   1 
ATOM   3203 C CA  . TRP A 1 492 ? 153.572 179.547 159.169 1.00 25.06  ? 492 TRP A CA  1 
ATOM   3204 C C   . TRP A 1 492 ? 152.145 179.801 158.708 1.00 28.86  ? 492 TRP A C   1 
ATOM   3205 O O   . TRP A 1 492 ? 151.720 179.205 157.713 1.00 34.65  ? 492 TRP A O   1 
ATOM   3206 C CB  . TRP A 1 492 ? 153.686 178.094 159.638 1.00 25.71  ? 492 TRP A CB  1 
ATOM   3207 C CG  . TRP A 1 492 ? 155.038 177.706 160.140 1.00 29.45  ? 492 TRP A CG  1 
ATOM   3208 C CD1 . TRP A 1 492 ? 155.456 177.689 161.436 1.00 31.46  ? 492 TRP A CD1 1 
ATOM   3209 C CD2 . TRP A 1 492 ? 156.146 177.253 159.356 1.00 23.55  ? 492 TRP A CD2 1 
ATOM   3210 N NE1 . TRP A 1 492 ? 156.759 177.265 161.508 1.00 25.69  ? 492 TRP A NE1 1 
ATOM   3211 C CE2 . TRP A 1 492 ? 157.206 176.992 160.242 1.00 23.35  ? 492 TRP A CE2 1 
ATOM   3212 C CE3 . TRP A 1 492 ? 156.346 177.048 157.990 1.00 20.16  ? 492 TRP A CE3 1 
ATOM   3213 C CZ2 . TRP A 1 492 ? 158.444 176.536 159.807 1.00 27.45  ? 492 TRP A CZ2 1 
ATOM   3214 C CZ3 . TRP A 1 492 ? 157.577 176.597 157.561 1.00 17.42  ? 492 TRP A CZ3 1 
ATOM   3215 C CH2 . TRP A 1 492 ? 158.609 176.347 158.464 1.00 23.61  ? 492 TRP A CH2 1 
ATOM   3216 N N   . GLY A 1 493 ? 151.397 180.654 159.401 1.00 34.56  ? 493 GLY A N   1 
ATOM   3217 C CA  . GLY A 1 493 ? 150.016 180.895 159.064 1.00 37.95  ? 493 GLY A CA  1 
ATOM   3218 C C   . GLY A 1 493 ? 149.369 181.931 159.957 1.00 47.68  ? 493 GLY A C   1 
ATOM   3219 O O   . GLY A 1 493 ? 149.974 182.430 160.909 1.00 46.35  ? 493 GLY A O   1 
ATOM   3220 N N   . PRO A 1 494 ? 148.110 182.266 159.672 1.00 51.51  ? 494 PRO A N   1 
ATOM   3221 C CA  . PRO A 1 494 ? 147.447 183.347 160.413 1.00 57.30  ? 494 PRO A CA  1 
ATOM   3222 C C   . PRO A 1 494 ? 147.042 182.943 161.821 1.00 62.74  ? 494 PRO A C   1 
ATOM   3223 O O   . PRO A 1 494 ? 147.005 183.783 162.726 1.00 62.23  ? 494 PRO A O   1 
ATOM   3224 C CB  . PRO A 1 494 ? 146.222 183.657 159.546 1.00 57.22  ? 494 PRO A CB  1 
ATOM   3225 C CG  . PRO A 1 494 ? 145.913 182.366 158.869 1.00 48.23  ? 494 PRO A CG  1 
ATOM   3226 C CD  . PRO A 1 494 ? 147.220 181.641 158.678 1.00 50.89  ? 494 PRO A CD  1 
ATOM   3227 N N   . GLU A 1 495 ? 146.731 181.665 162.014 1.00 56.58  ? 495 GLU A N   1 
ATOM   3228 C CA  . GLU A 1 495 ? 146.294 181.196 163.317 1.00 54.55  ? 495 GLU A CA  1 
ATOM   3229 C C   . GLU A 1 495 ? 147.439 181.283 164.325 1.00 48.26  ? 495 GLU A C   1 
ATOM   3230 O O   . GLU A 1 495 ? 148.609 181.151 163.960 1.00 47.81  ? 495 GLU A O   1 
ATOM   3231 C CB  . GLU A 1 495 ? 145.789 179.759 163.223 1.00 61.22  ? 495 GLU A CB  1 
ATOM   3232 C CG  . GLU A 1 495 ? 144.860 179.503 162.047 1.00 65.49  ? 495 GLU A CG  1 
ATOM   3233 C CD  . GLU A 1 495 ? 144.941 178.078 161.535 1.00 76.84  ? 495 GLU A CD  1 
ATOM   3234 O OE1 . GLU A 1 495 ? 144.224 177.209 162.074 1.00 87.86  ? 495 GLU A OE1 1 
ATOM   3235 O OE2 . GLU A 1 495 ? 145.719 177.826 160.591 1.00 67.67  ? 495 GLU A OE2 1 
ATOM   3236 N N   . PRO A 1 496 ? 147.127 181.516 165.602 1.00 50.90  ? 496 PRO A N   1 
ATOM   3237 C CA  . PRO A 1 496 ? 148.192 181.571 166.616 1.00 44.34  ? 496 PRO A CA  1 
ATOM   3238 C C   . PRO A 1 496 ? 148.921 180.255 166.795 1.00 48.59  ? 496 PRO A C   1 
ATOM   3239 O O   . PRO A 1 496 ? 150.026 180.248 167.352 1.00 55.16  ? 496 PRO A O   1 
ATOM   3240 C CB  . PRO A 1 496 ? 147.444 181.979 167.892 1.00 49.87  ? 496 PRO A CB  1 
ATOM   3241 C CG  . PRO A 1 496 ? 146.041 181.539 167.662 1.00 65.49  ? 496 PRO A CG  1 
ATOM   3242 C CD  . PRO A 1 496 ? 145.791 181.709 166.191 1.00 65.88  ? 496 PRO A CD  1 
ATOM   3243 N N   . ARG A 1 497 ? 148.335 179.139 166.357 1.00 49.50  ? 497 ARG A N   1 
ATOM   3244 C CA  . ARG A 1 497 ? 149.049 177.867 166.388 1.00 44.43  ? 497 ARG A CA  1 
ATOM   3245 C C   . ARG A 1 497 ? 150.272 177.909 165.484 1.00 45.45  ? 497 ARG A C   1 
ATOM   3246 O O   . ARG A 1 497 ? 151.336 177.390 165.841 1.00 47.88  ? 497 ARG A O   1 
ATOM   3247 C CB  . ARG A 1 497 ? 148.117 176.732 165.967 1.00 48.63  ? 497 ARG A CB  1 
ATOM   3248 C CG  . ARG A 1 497 ? 146.836 176.655 166.771 1.00 56.62  ? 497 ARG A CG  1 
ATOM   3249 C CD  . ARG A 1 497 ? 146.005 175.445 166.388 1.00 70.12  ? 497 ARG A CD  1 
ATOM   3250 N NE  . ARG A 1 497 ? 145.547 175.509 165.006 1.00 70.86  ? 497 ARG A NE  1 
ATOM   3251 C CZ  . ARG A 1 497 ? 145.904 174.651 164.062 1.00 72.23  ? 497 ARG A CZ  1 
ATOM   3252 N NH1 . ARG A 1 497 ? 146.716 173.640 164.319 1.00 67.39  ? 497 ARG A NH1 1 
ATOM   3253 N NH2 . ARG A 1 497 ? 145.430 174.808 162.829 1.00 69.73  ? 497 ARG A NH2 1 
ATOM   3254 N N   . ASP A 1 498 ? 150.101 178.505 164.295 1.00 45.50  ? 498 ASP A N   1 
ATOM   3255 C CA  . ASP A 1 498 ? 151.186 178.587 163.280 1.00 35.97  ? 498 ASP A CA  1 
ATOM   3256 C C   . ASP A 1 498 ? 152.048 179.819 163.549 1.00 33.68  ? 498 ASP A C   1 
ATOM   3257 O O   . ASP A 1 498 ? 151.719 180.894 163.001 1.00 40.01  ? 498 ASP A O   1 
ATOM   3258 C CB  . ASP A 1 498 ? 150.625 178.667 161.871 1.00 38.56  ? 498 ASP A CB  1 
ATOM   3259 C CG  . ASP A 1 498 ? 149.719 177.519 161.456 1.00 46.14  ? 498 ASP A CG  1 
ATOM   3260 O OD1 . ASP A 1 498 ? 150.093 176.798 160.507 1.00 48.88  ? 498 ASP A OD1 1 
ATOM   3261 O OD2 . ASP A 1 498 ? 148.643 177.374 162.073 1.00 52.66  ? 498 ASP A OD2 1 
ATOM   3262 N N   . CYS A 1 499 ? 153.102 179.685 164.354 1.00 26.37  ? 499 CYS A N   1 
ATOM   3263 C CA  . CYS A 1 499 ? 154.019 180.789 164.627 1.00 32.56  ? 499 CYS A CA  1 
ATOM   3264 C C   . CYS A 1 499 ? 155.305 180.197 165.174 1.00 44.74  ? 499 CYS A C   1 
ATOM   3265 O O   . CYS A 1 499 ? 155.267 179.448 166.155 1.00 51.96  ? 499 CYS A O   1 
ATOM   3266 C CB  . CYS A 1 499 ? 153.411 181.784 165.620 1.00 32.46  ? 499 CYS A CB  1 
ATOM   3267 S SG  . CYS A 1 499 ? 152.693 183.263 164.859 1.00 46.74  ? 499 CYS A SG  1 
ATOM   3268 N N   . VAL A 1 500 ? 156.429 180.472 164.496 1.00 41.05  ? 500 VAL A N   1 
ATOM   3269 C CA  . VAL A 1 500 ? 157.763 179.923 164.890 1.00 42.58  ? 500 VAL A CA  1 
ATOM   3270 C C   . VAL A 1 500 ? 158.095 180.425 166.302 1.00 42.30  ? 500 VAL A C   1 
ATOM   3271 O O   . VAL A 1 500 ? 158.618 179.617 167.099 1.00 50.38  ? 500 VAL A O   1 
ATOM   3272 C CB  . VAL A 1 500 ? 158.849 180.316 163.866 1.00 41.55  ? 500 VAL A CB  1 
ATOM   3273 C CG1 . VAL A 1 500 ? 158.547 179.762 162.479 1.00 36.67  ? 500 VAL A CG1 1 
ATOM   3274 C CG2 . VAL A 1 500 ? 159.075 181.823 163.793 1.00 42.87  ? 500 VAL A CG2 1 
ATOM   3275 N N   . SER A 1 501 ? 157.760 181.685 166.587 1.00 35.61  ? 501 SER A N   1 
ATOM   3276 C CA  . SER A 1 501 ? 157.988 182.269 167.933 1.00 47.81  ? 501 SER A CA  1 
ATOM   3277 C C   . SER A 1 501 ? 156.845 183.246 168.227 1.00 53.18  ? 501 SER A C   1 
ATOM   3278 O O   . SER A 1 501 ? 156.311 183.829 167.259 1.00 59.83  ? 501 SER A O   1 
ATOM   3279 C CB  . SER A 1 501 ? 159.330 182.942 168.021 1.00 55.74  ? 501 SER A CB  1 
ATOM   3280 O OG  . SER A 1 501 ? 160.379 181.986 167.950 1.00 55.46  ? 501 SER A OG  1 
ATOM   3281 N N   . CYS A 1 502 ? 156.484 183.418 169.499 1.00 49.40  ? 502 CYS A N   1 
ATOM   3282 C CA  . CYS A 1 502 ? 155.357 184.266 169.847 1.00 54.93  ? 502 CYS A CA  1 
ATOM   3283 C C   . CYS A 1 502 ? 155.799 185.363 170.804 1.00 57.71  ? 502 CYS A C   1 
ATOM   3284 O O   . CYS A 1 502 ? 156.683 185.161 171.642 1.00 60.24  ? 502 CYS A O   1 
ATOM   3285 C CB  . CYS A 1 502 ? 154.217 183.435 170.444 1.00 48.96  ? 502 CYS A CB  1 
ATOM   3286 S SG  . CYS A 1 502 ? 153.519 182.263 169.242 1.00 51.66  ? 502 CYS A SG  1 
ATOM   3287 N N   . ARG A 1 503 ? 155.177 186.536 170.653 1.00 55.27  ? 503 ARG A N   1 
ATOM   3288 C CA  . ARG A 1 503 ? 155.605 187.723 171.389 1.00 52.12  ? 503 ARG A CA  1 
ATOM   3289 C C   . ARG A 1 503 ? 155.542 187.494 172.892 1.00 51.16  ? 503 ARG A C   1 
ATOM   3290 O O   . ARG A 1 503 ? 156.521 187.722 173.611 1.00 51.98  ? 503 ARG A O   1 
ATOM   3291 C CB  . ARG A 1 503 ? 154.738 188.917 170.991 1.00 52.38  ? 503 ARG A CB  1 
ATOM   3292 C CG  . ARG A 1 503 ? 155.385 190.272 171.219 1.00 50.71  ? 503 ARG A CG  1 
ATOM   3293 C CD  . ARG A 1 503 ? 154.557 191.386 170.597 1.00 54.75  ? 503 ARG A CD  1 
ATOM   3294 N NE  . ARG A 1 503 ? 153.148 191.025 170.488 1.00 62.62  ? 503 ARG A NE  1 
ATOM   3295 C CZ  . ARG A 1 503 ? 152.246 191.230 171.438 1.00 71.55  ? 503 ARG A CZ  1 
ATOM   3296 N NH1 . ARG A 1 503 ? 152.570 191.795 172.589 1.00 79.08  ? 503 ARG A NH1 1 
ATOM   3297 N NH2 . ARG A 1 503 ? 150.986 190.858 171.228 1.00 65.26  ? 503 ARG A NH2 1 
ATOM   3298 N N   . ASN A 1 504 ? 154.397 187.042 173.384 1.00 54.68  ? 504 ASN A N   1 
ATOM   3299 C CA  . ASN A 1 504 ? 154.248 186.685 174.784 1.00 53.17  ? 504 ASN A CA  1 
ATOM   3300 C C   . ASN A 1 504 ? 154.573 185.202 174.953 1.00 52.69  ? 504 ASN A C   1 
ATOM   3301 O O   . ASN A 1 504 ? 155.131 184.559 174.061 1.00 63.02  ? 504 ASN A O   1 
ATOM   3302 C CB  . ASN A 1 504 ? 152.842 187.026 175.271 1.00 52.96  ? 504 ASN A CB  1 
ATOM   3303 C CG  . ASN A 1 504 ? 152.673 188.499 175.586 1.00 63.58  ? 504 ASN A CG  1 
ATOM   3304 O OD1 . ASN A 1 504 ? 152.251 189.281 174.734 1.00 67.04  ? 504 ASN A OD1 1 
ATOM   3305 N ND2 . ASN A 1 504 ? 152.998 188.883 176.817 1.00 69.01  ? 504 ASN A ND2 1 
ATOM   3306 N N   . VAL A 1 505 ? 154.229 184.644 176.110 1.00 43.09  ? 505 VAL A N   1 
ATOM   3307 C CA  . VAL A 1 505 ? 154.458 183.231 176.383 1.00 45.76  ? 505 VAL A CA  1 
ATOM   3308 C C   . VAL A 1 505 ? 153.526 182.384 175.526 1.00 46.29  ? 505 VAL A C   1 
ATOM   3309 O O   . VAL A 1 505 ? 152.559 182.894 174.952 1.00 56.11  ? 505 VAL A O   1 
ATOM   3310 C CB  . VAL A 1 505 ? 154.269 182.932 177.877 1.00 55.86  ? 505 VAL A CB  1 
ATOM   3311 C CG1 . VAL A 1 505 ? 154.938 184.012 178.707 1.00 64.55  ? 505 VAL A CG1 1 
ATOM   3312 C CG2 . VAL A 1 505 ? 152.799 182.875 178.198 1.00 58.70  ? 505 VAL A CG2 1 
ATOM   3313 N N   . SER A 1 506 ? 153.809 181.086 175.437 1.00 53.02  ? 506 SER A N   1 
ATOM   3314 C CA  . SER A 1 506 ? 153.094 180.180 174.550 1.00 51.79  ? 506 SER A CA  1 
ATOM   3315 C C   . SER A 1 506 ? 152.438 179.061 175.346 1.00 51.48  ? 506 SER A C   1 
ATOM   3316 O O   . SER A 1 506 ? 153.034 178.520 176.281 1.00 60.88  ? 506 SER A O   1 
ATOM   3317 C CB  . SER A 1 506 ? 154.037 179.582 173.502 1.00 52.05  ? 506 SER A CB  1 
ATOM   3318 O OG  . SER A 1 506 ? 154.932 180.562 173.008 1.00 65.61  ? 506 SER A OG  1 
ATOM   3319 N N   . ARG A 1 507 ? 151.206 178.716 174.967 1.00 49.82  ? 507 ARG A N   1 
ATOM   3320 C CA  . ARG A 1 507 ? 150.458 177.641 175.618 1.00 52.20  ? 507 ARG A CA  1 
ATOM   3321 C C   . ARG A 1 507 ? 150.508 176.408 174.720 1.00 53.37  ? 507 ARG A C   1 
ATOM   3322 O O   . ARG A 1 507 ? 149.605 176.135 173.930 1.00 57.28  ? 507 ARG A O   1 
ATOM   3323 C CB  . ARG A 1 507 ? 149.026 178.080 175.910 1.00 60.10  ? 507 ARG A CB  1 
ATOM   3324 C CG  . ARG A 1 507 ? 148.175 177.013 176.582 1.00 61.86  ? 507 ARG A CG  1 
ATOM   3325 C CD  . ARG A 1 507 ? 146.747 177.483 176.806 1.00 59.97  ? 507 ARG A CD  1 
ATOM   3326 N NE  . ARG A 1 507 ? 146.684 178.822 177.378 1.00 64.79  ? 507 ARG A NE  1 
ATOM   3327 C CZ  . ARG A 1 507 ? 145.584 179.371 177.876 1.00 75.21  ? 507 ARG A CZ  1 
ATOM   3328 N NH1 . ARG A 1 507 ? 144.431 178.723 177.882 1.00 78.36  ? 507 ARG A NH1 1 
ATOM   3329 N NH2 . ARG A 1 507 ? 145.643 180.600 178.380 1.00 73.96  ? 507 ARG A NH2 1 
ATOM   3330 N N   . GLY A 1 508 ? 151.595 175.652 174.855 1.00 59.33  ? 508 GLY A N   1 
ATOM   3331 C CA  . GLY A 1 508 ? 151.783 174.441 174.082 1.00 61.20  ? 508 GLY A CA  1 
ATOM   3332 C C   . GLY A 1 508 ? 151.824 174.679 172.587 1.00 61.56  ? 508 GLY A C   1 
ATOM   3333 O O   . GLY A 1 508 ? 152.751 175.314 172.075 1.00 68.15  ? 508 GLY A O   1 
ATOM   3334 N N   . ARG A 1 509 ? 150.822 174.161 171.875 1.00 61.11  ? 509 ARG A N   1 
ATOM   3335 C CA  . ARG A 1 509 ? 150.748 174.377 170.434 1.00 60.63  ? 509 ARG A CA  1 
ATOM   3336 C C   . ARG A 1 509 ? 150.528 175.848 170.104 1.00 55.21  ? 509 ARG A C   1 
ATOM   3337 O O   . ARG A 1 509 ? 151.150 176.383 169.179 1.00 50.66  ? 509 ARG A O   1 
ATOM   3338 C CB  . ARG A 1 509 ? 149.632 173.521 169.836 1.00 58.60  ? 509 ARG A CB  1 
ATOM   3339 C CG  . ARG A 1 509 ? 149.687 173.390 168.325 1.00 59.24  ? 509 ARG A CG  1 
ATOM   3340 C CD  . ARG A 1 509 ? 151.079 173.004 167.859 1.00 57.60  ? 509 ARG A CD  1 
ATOM   3341 N NE  . ARG A 1 509 ? 151.042 171.983 166.820 1.00 59.06  ? 509 ARG A NE  1 
ATOM   3342 C CZ  . ARG A 1 509 ? 152.089 171.265 166.438 1.00 54.74  ? 509 ARG A CZ  1 
ATOM   3343 N NH1 . ARG A 1 509 ? 153.279 171.431 166.992 1.00 44.56  ? 509 ARG A NH1 1 
ATOM   3344 N NH2 . ARG A 1 509 ? 151.940 170.359 165.476 1.00 56.23  ? 509 ARG A NH2 1 
ATOM   3345 N N   . GLU A 1 510 ? 149.651 176.516 170.848 1.00 53.44  ? 510 GLU A N   1 
ATOM   3346 C CA  . GLU A 1 510 ? 149.291 177.899 170.578 1.00 50.63  ? 510 GLU A CA  1 
ATOM   3347 C C   . GLU A 1 510 ? 150.194 178.842 171.369 1.00 51.83  ? 510 GLU A C   1 
ATOM   3348 O O   . GLU A 1 510 ? 151.179 178.432 171.987 1.00 53.23  ? 510 GLU A O   1 
ATOM   3349 C CB  . GLU A 1 510 ? 147.822 178.139 170.920 1.00 53.95  ? 510 GLU A CB  1 
ATOM   3350 C CG  . GLU A 1 510 ? 146.857 177.156 170.292 1.00 65.49  ? 510 GLU A CG  1 
ATOM   3351 C CD  . GLU A 1 510 ? 145.575 177.822 169.836 1.00 72.93  ? 510 GLU A CD  1 
ATOM   3352 O OE1 . GLU A 1 510 ? 145.405 179.029 170.105 1.00 66.24  ? 510 GLU A OE1 1 
ATOM   3353 O OE2 . GLU A 1 510 ? 144.737 177.138 169.211 1.00 78.27  ? 510 GLU A OE2 1 
ATOM   3354 N N   . CYS A 1 511 ? 149.858 180.130 171.349 1.00 49.96  ? 511 CYS A N   1 
ATOM   3355 C CA  . CYS A 1 511 ? 150.495 181.108 172.226 1.00 49.95  ? 511 CYS A CA  1 
ATOM   3356 C C   . CYS A 1 511 ? 149.445 182.145 172.590 1.00 47.25  ? 511 CYS A C   1 
ATOM   3357 O O   . CYS A 1 511 ? 149.108 183.004 171.772 1.00 53.09  ? 511 CYS A O   1 
ATOM   3358 C CB  . CYS A 1 511 ? 151.708 181.756 171.569 1.00 52.29  ? 511 CYS A CB  1 
ATOM   3359 S SG  . CYS A 1 511 ? 151.583 182.029 169.801 1.00 70.47  ? 511 CYS A SG  1 
ATOM   3360 N N   . VAL A 1 512 ? 148.921 182.047 173.806 1.00 48.18  ? 512 VAL A N   1 
ATOM   3361 C CA  . VAL A 1 512 ? 147.884 182.948 174.289 1.00 59.84  ? 512 VAL A CA  1 
ATOM   3362 C C   . VAL A 1 512 ? 148.487 184.309 174.607 1.00 57.37  ? 512 VAL A C   1 
ATOM   3363 O O   . VAL A 1 512 ? 149.712 184.473 174.607 1.00 54.50  ? 512 VAL A O   1 
ATOM   3364 C CB  . VAL A 1 512 ? 147.171 182.357 175.517 1.00 68.24  ? 512 VAL A CB  1 
ATOM   3365 C CG1 . VAL A 1 512 ? 146.171 181.300 175.082 1.00 62.15  ? 512 VAL A CG1 1 
ATOM   3366 C CG2 . VAL A 1 512 ? 148.188 181.766 176.478 1.00 60.43  ? 512 VAL A CG2 1 
ATOM   3367 N N   . ASP A 1 513 ? 147.623 185.296 174.863 1.00 60.38  ? 513 ASP A N   1 
ATOM   3368 C CA  . ASP A 1 513 ? 148.089 186.633 175.216 1.00 56.97  ? 513 ASP A CA  1 
ATOM   3369 C C   . ASP A 1 513 ? 148.998 186.610 176.436 1.00 57.29  ? 513 ASP A C   1 
ATOM   3370 O O   . ASP A 1 513 ? 149.925 187.421 176.533 1.00 58.46  ? 513 ASP A O   1 
ATOM   3371 C CB  . ASP A 1 513 ? 146.892 187.552 175.462 1.00 62.43  ? 513 ASP A CB  1 
ATOM   3372 C CG  . ASP A 1 513 ? 147.206 189.009 175.191 1.00 76.19  ? 513 ASP A CG  1 
ATOM   3373 O OD1 . ASP A 1 513 ? 148.085 189.570 175.878 1.00 75.94  ? 513 ASP A OD1 1 
ATOM   3374 O OD2 . ASP A 1 513 ? 146.571 189.596 174.289 1.00 81.36  ? 513 ASP A OD2 1 
ATOM   3375 N N   . LYS A 1 514 ? 148.752 185.694 177.369 1.00 54.39  ? 514 LYS A N   1 
ATOM   3376 C CA  . LYS A 1 514 ? 149.575 185.549 178.560 1.00 53.97  ? 514 LYS A CA  1 
ATOM   3377 C C   . LYS A 1 514 ? 149.204 184.247 179.248 1.00 56.89  ? 514 LYS A C   1 
ATOM   3378 O O   . LYS A 1 514 ? 148.088 183.746 179.087 1.00 57.60  ? 514 LYS A O   1 
ATOM   3379 C CB  . LYS A 1 514 ? 149.387 186.729 179.522 1.00 67.12  ? 514 LYS A CB  1 
ATOM   3380 C CG  . LYS A 1 514 ? 147.935 187.122 179.735 1.00 67.10  ? 514 LYS A CG  1 
ATOM   3381 C CD  . LYS A 1 514 ? 147.817 188.382 180.574 1.00 68.15  ? 514 LYS A CD  1 
ATOM   3382 C CE  . LYS A 1 514 ? 146.419 188.529 181.148 1.00 79.77  ? 514 LYS A CE  1 
ATOM   3383 N NZ  . LYS A 1 514 ? 145.435 187.674 180.430 1.00 84.69  ? 514 LYS A NZ  1 
ATOM   3384 N N   . CYS A 1 515 ? 150.124 183.705 180.052 1.00 65.33  ? 515 CYS A N   1 
ATOM   3385 C CA  . CYS A 1 515 ? 149.798 182.481 180.830 1.00 67.19  ? 515 CYS A CA  1 
ATOM   3386 C C   . CYS A 1 515 ? 148.640 182.784 181.792 1.00 72.17  ? 515 CYS A C   1 
ATOM   3387 O O   . CYS A 1 515 ? 148.482 183.965 182.174 1.00 73.20  ? 515 CYS A O   1 
ATOM   3388 C CB  . CYS A 1 515 ? 150.987 182.005 181.653 1.00 64.96  ? 515 CYS A CB  1 
ATOM   3389 S SG  . CYS A 1 515 ? 151.985 180.735 180.834 1.00 87.33  ? 515 CYS A SG  1 
ATOM   3390 N N   . ASN A 1 516 ? 147.882 181.758 182.187 1.00 70.62  ? 516 ASN A N   1 
ATOM   3391 C CA  . ASN A 1 516 ? 146.779 181.960 183.166 1.00 72.69  ? 516 ASN A CA  1 
ATOM   3392 C C   . ASN A 1 516 ? 147.385 182.079 184.567 1.00 76.67  ? 516 ASN A C   1 
ATOM   3393 O O   . ASN A 1 516 ? 147.119 181.196 185.409 1.00 79.06  ? 516 ASN A O   1 
ATOM   3394 C CB  . ASN A 1 516 ? 145.738 180.850 183.078 1.00 70.46  ? 516 ASN A CB  1 
ATOM   3395 C CG  . ASN A 1 516 ? 145.122 180.760 181.703 1.00 73.24  ? 516 ASN A CG  1 
ATOM   3396 O OD1 . ASN A 1 516 ? 145.199 179.712 181.055 1.00 73.82  ? 516 ASN A OD1 1 
ATOM   3397 N ND2 . ASN A 1 516 ? 144.510 181.841 181.243 1.00 77.17  ? 516 ASN A ND2 1 
ATOM   3398 N N   . LEU A 1 517 ? 148.171 183.133 184.802 1.00 70.84  ? 517 LEU A N   1 
ATOM   3399 C CA  . LEU A 1 517 ? 148.837 183.316 186.117 1.00 69.58  ? 517 LEU A CA  1 
ATOM   3400 C C   . LEU A 1 517 ? 147.778 183.654 187.178 1.00 81.33  ? 517 LEU A C   1 
ATOM   3401 O O   . LEU A 1 517 ? 147.793 183.016 188.254 1.00 91.87  ? 517 LEU A O   1 
ATOM   3402 C CB  . LEU A 1 517 ? 149.901 184.405 186.003 1.00 63.84  ? 517 LEU A CB  1 
ATOM   3403 C CG  . LEU A 1 517 ? 151.019 184.133 184.991 1.00 63.01  ? 517 LEU A CG  1 
ATOM   3404 C CD1 . LEU A 1 517 ? 152.012 185.282 184.948 1.00 65.42  ? 517 LEU A CD1 1 
ATOM   3405 C CD2 . LEU A 1 517 ? 151.725 182.825 185.305 1.00 59.19  ? 517 LEU A CD2 1 
ATOM   3406 N N   . LEU A 1 518 ? 146.898 184.617 186.882 1.00 85.74  ? 518 LEU A N   1 
ATOM   3407 C CA  . LEU A 1 518 ? 145.875 185.033 187.881 1.00 85.38  ? 518 LEU A CA  1 
ATOM   3408 C C   . LEU A 1 518 ? 144.454 184.833 187.330 1.00 80.48  ? 518 LEU A C   1 
ATOM   3409 O O   . LEU A 1 518 ? 143.557 184.542 188.151 1.00 79.54  ? 518 LEU A O   1 
ATOM   3410 C CB  . LEU A 1 518 ? 146.140 186.488 188.260 1.00 84.49  ? 518 LEU A CB  1 
ATOM   3411 C CG  . LEU A 1 518 ? 147.470 186.766 188.968 1.00 82.18  ? 518 LEU A CG  1 
ATOM   3412 C CD1 . LEU A 1 518 ? 147.633 188.253 189.201 1.00 74.22  ? 518 LEU A CD1 1 
ATOM   3413 C CD2 . LEU A 1 518 ? 147.586 186.012 190.279 1.00 86.97  ? 518 LEU A CD2 1 
ATOM   3414 N N   . GLU A 1 519 ? 144.250 184.993 186.019 1.00 80.52  ? 519 GLU A N   1 
ATOM   3415 C CA  . GLU A 1 519 ? 142.911 184.847 185.387 1.00 84.36  ? 519 GLU A CA  1 
ATOM   3416 C C   . GLU A 1 519 ? 142.949 183.722 184.346 1.00 79.93  ? 519 GLU A C   1 
ATOM   3417 O O   . GLU A 1 519 ? 143.925 183.685 183.568 1.00 78.41  ? 519 GLU A O   1 
ATOM   3418 C CB  . GLU A 1 519 ? 142.464 186.152 184.729 1.00 87.49  ? 519 GLU A CB  1 
ATOM   3419 C CG  . GLU A 1 519 ? 141.699 187.074 185.674 1.00 80.34  ? 519 GLU A CG  1 
ATOM   3420 C CD  . GLU A 1 519 ? 142.543 187.859 186.663 1.00 88.18  ? 519 GLU A CD  1 
ATOM   3421 O OE1 . GLU A 1 519 ? 143.786 187.770 186.610 1.00 85.55  ? 519 GLU A OE1 1 
ATOM   3422 O OE2 . GLU A 1 519 ? 141.942 188.566 187.498 1.00 95.28  ? 519 GLU A OE2 1 
ATOM   3423 N N   . GLY A 1 520 ? 141.925 182.862 184.323 1.00 73.31  ? 520 GLY A N   1 
ATOM   3424 C CA  . GLY A 1 520 ? 141.843 181.743 183.362 1.00 77.38  ? 520 GLY A CA  1 
ATOM   3425 C C   . GLY A 1 520 ? 141.395 180.468 184.045 1.00 75.97  ? 520 GLY A C   1 
ATOM   3426 O O   . GLY A 1 520 ? 141.483 180.415 185.288 1.00 75.45  ? 520 GLY A O   1 
ATOM   3427 N N   . GLU A 1 521 ? 140.902 179.490 183.281 1.00 78.14  ? 521 GLU A N   1 
ATOM   3428 C CA  . GLU A 1 521 ? 140.488 178.173 183.836 1.00 80.60  ? 521 GLU A CA  1 
ATOM   3429 C C   . GLU A 1 521 ? 141.722 177.262 183.977 1.00 85.06  ? 521 GLU A C   1 
ATOM   3430 O O   . GLU A 1 521 ? 141.883 176.667 185.066 1.00 90.47  ? 521 GLU A O   1 
ATOM   3431 C CB  . GLU A 1 521 ? 139.414 177.536 182.953 1.00 86.61  ? 521 GLU A CB  1 
ATOM   3432 C CG  . GLU A 1 521 ? 139.009 176.133 183.397 1.00 97.26  ? 521 GLU A CG  1 
ATOM   3433 C CD  . GLU A 1 521 ? 138.556 176.042 184.843 1.00 101.01 ? 521 GLU A CD  1 
ATOM   3434 O OE1 . GLU A 1 521 ? 137.570 176.721 185.198 1.00 101.66 ? 521 GLU A OE1 1 
ATOM   3435 O OE2 . GLU A 1 521 ? 139.191 175.292 185.613 1.00 99.72  ? 521 GLU A OE2 1 
ATOM   3436 N N   . PRO A 1 522 ? 142.604 177.122 182.958 1.00 81.23  ? 522 PRO A N   1 
ATOM   3437 C CA  . PRO A 1 522 ? 143.747 176.228 183.063 1.00 76.95  ? 522 PRO A CA  1 
ATOM   3438 C C   . PRO A 1 522 ? 144.620 176.630 184.235 1.00 71.67  ? 522 PRO A C   1 
ATOM   3439 O O   . PRO A 1 522 ? 145.236 175.736 184.849 1.00 64.63  ? 522 PRO A O   1 
ATOM   3440 C CB  . PRO A 1 522 ? 144.491 176.377 181.727 1.00 72.96  ? 522 PRO A CB  1 
ATOM   3441 C CG  . PRO A 1 522 ? 143.459 176.955 180.791 1.00 73.23  ? 522 PRO A CG  1 
ATOM   3442 C CD  . PRO A 1 522 ? 142.563 177.803 181.673 1.00 73.31  ? 522 PRO A CD  1 
ATOM   3443 N N   . ARG A 1 523 ? 144.682 177.930 184.538 1.00 73.18  ? 523 ARG A N   1 
ATOM   3444 C CA  . ARG A 1 523 ? 145.555 178.445 185.626 1.00 70.31  ? 523 ARG A CA  1 
ATOM   3445 C C   . ARG A 1 523 ? 146.920 177.759 185.488 1.00 70.15  ? 523 ARG A C   1 
ATOM   3446 O O   . ARG A 1 523 ? 147.276 176.950 186.375 1.00 80.65  ? 523 ARG A O   1 
ATOM   3447 C CB  . ARG A 1 523 ? 144.908 178.256 187.003 1.00 75.72  ? 523 ARG A CB  1 
ATOM   3448 C CG  . ARG A 1 523 ? 143.730 179.191 187.233 1.00 82.57  ? 523 ARG A CG  1 
ATOM   3449 C CD  . ARG A 1 523 ? 144.109 180.660 187.075 1.00 84.49  ? 523 ARG A CD  1 
ATOM   3450 N NE  . ARG A 1 523 ? 143.378 181.553 187.980 1.00 81.73  ? 523 ARG A NE  1 
ATOM   3451 C CZ  . ARG A 1 523 ? 143.518 181.586 189.301 1.00 87.13  ? 523 ARG A CZ  1 
ATOM   3452 N NH1 . ARG A 1 523 ? 144.510 180.938 189.884 1.00 91.23  ? 523 ARG A NH1 1 
ATOM   3453 N NH2 . ARG A 1 523 ? 142.670 182.277 190.040 1.00 91.36  ? 523 ARG A NH2 1 
ATOM   3454 N N   . GLU A 1 524 ? 147.639 178.066 184.408 1.00 68.93  ? 524 GLU A N   1 
ATOM   3455 C CA  . GLU A 1 524 ? 148.977 177.476 184.146 1.00 65.79  ? 524 GLU A CA  1 
ATOM   3456 C C   . GLU A 1 524 ? 150.049 178.406 184.733 1.00 60.52  ? 524 GLU A C   1 
ATOM   3457 O O   . GLU A 1 524 ? 149.673 179.289 185.536 1.00 61.97  ? 524 GLU A O   1 
ATOM   3458 C CB  . GLU A 1 524 ? 149.113 177.270 182.637 1.00 71.60  ? 524 GLU A CB  1 
ATOM   3459 C CG  . GLU A 1 524 ? 149.053 178.568 181.835 1.00 73.79  ? 524 GLU A CG  1 
ATOM   3460 C CD  . GLU A 1 524 ? 148.126 178.579 180.629 1.00 72.75  ? 524 GLU A CD  1 
ATOM   3461 O OE1 . GLU A 1 524 ? 147.529 177.540 180.278 1.00 72.14  ? 524 GLU A OE1 1 
ATOM   3462 O OE2 . GLU A 1 524 ? 147.995 179.670 180.040 1.00 68.64  ? 524 GLU A OE2 1 
ATOM   3463 N N   . PHE A 1 525 ? 151.320 178.224 184.364 1.00 59.28  ? 525 PHE A N   1 
ATOM   3464 C CA  . PHE A 1 525 ? 152.419 179.042 184.854 1.00 61.67  ? 525 PHE A CA  1 
ATOM   3465 C C   . PHE A 1 525 ? 153.497 179.119 183.782 1.00 64.06  ? 525 PHE A C   1 
ATOM   3466 O O   . PHE A 1 525 ? 153.574 178.272 182.889 1.00 63.55  ? 525 PHE A O   1 
ATOM   3467 C CB  . PHE A 1 525 ? 152.995 178.493 186.163 1.00 64.91  ? 525 PHE A CB  1 
ATOM   3468 C CG  . PHE A 1 525 ? 154.022 177.415 185.971 1.00 67.98  ? 525 PHE A CG  1 
ATOM   3469 C CD1 . PHE A 1 525 ? 153.640 176.127 185.646 1.00 66.88  ? 525 PHE A CD1 1 
ATOM   3470 C CD2 . PHE A 1 525 ? 155.370 177.689 186.120 1.00 69.06  ? 525 PHE A CD2 1 
ATOM   3471 C CE1 . PHE A 1 525 ? 154.580 175.134 185.470 1.00 61.74  ? 525 PHE A CE1 1 
ATOM   3472 C CE2 . PHE A 1 525 ? 156.315 176.699 185.945 1.00 68.44  ? 525 PHE A CE2 1 
ATOM   3473 C CZ  . PHE A 1 525 ? 155.919 175.420 185.619 1.00 65.42  ? 525 PHE A CZ  1 
ATOM   3474 N N   . VAL A 1 526 ? 154.335 180.144 183.888 1.00 62.91  ? 526 VAL A N   1 
ATOM   3475 C CA  . VAL A 1 526 ? 155.347 180.418 182.874 1.00 58.28  ? 526 VAL A CA  1 
ATOM   3476 C C   . VAL A 1 526 ? 156.579 179.563 183.138 1.00 63.75  ? 526 VAL A C   1 
ATOM   3477 O O   . VAL A 1 526 ? 157.102 179.531 184.258 1.00 68.75  ? 526 VAL A O   1 
ATOM   3478 C CB  . VAL A 1 526 ? 155.707 181.911 182.855 1.00 69.48  ? 526 VAL A CB  1 
ATOM   3479 C CG1 . VAL A 1 526 ? 154.677 182.692 182.064 1.00 72.64  ? 526 VAL A CG1 1 
ATOM   3480 C CG2 . VAL A 1 526 ? 155.812 182.452 184.274 1.00 71.70  ? 526 VAL A CG2 1 
ATOM   3481 N N   . GLU A 1 527 ? 157.046 178.870 182.102 1.00 67.84  ? 527 GLU A N   1 
ATOM   3482 C CA  . GLU A 1 527 ? 158.279 178.094 182.165 1.00 68.49  ? 527 GLU A CA  1 
ATOM   3483 C C   . GLU A 1 527 ? 159.044 178.322 180.872 1.00 68.98  ? 527 GLU A C   1 
ATOM   3484 O O   . GLU A 1 527 ? 158.571 177.930 179.802 1.00 72.79  ? 527 GLU A O   1 
ATOM   3485 C CB  . GLU A 1 527 ? 157.993 176.604 182.368 1.00 68.77  ? 527 GLU A CB  1 
ATOM   3486 C CG  . GLU A 1 527 ? 159.239 175.744 182.503 1.00 69.02  ? 527 GLU A CG  1 
ATOM   3487 C CD  . GLU A 1 527 ? 159.742 175.667 183.931 1.00 73.50  ? 527 GLU A CD  1 
ATOM   3488 O OE1 . GLU A 1 527 ? 160.191 176.704 184.462 1.00 70.85  ? 527 GLU A OE1 1 
ATOM   3489 O OE2 . GLU A 1 527 ? 159.688 174.568 184.523 1.00 70.92  ? 527 GLU A OE2 1 
ATOM   3490 N N   . ASN A 1 528 ? 160.220 178.950 180.981 1.00 64.27  ? 528 ASN A N   1 
ATOM   3491 C CA  . ASN A 1 528 ? 161.058 179.353 179.851 1.00 66.68  ? 528 ASN A CA  1 
ATOM   3492 C C   . ASN A 1 528 ? 160.227 179.837 178.666 1.00 70.91  ? 528 ASN A C   1 
ATOM   3493 O O   . ASN A 1 528 ? 160.417 179.381 177.533 1.00 76.63  ? 528 ASN A O   1 
ATOM   3494 C CB  . ASN A 1 528 ? 162.013 178.221 179.435 1.00 73.09  ? 528 ASN A CB  1 
ATOM   3495 C CG  . ASN A 1 528 ? 161.300 176.996 178.881 1.00 74.99  ? 528 ASN A CG  1 
ATOM   3496 O OD1 . ASN A 1 528 ? 160.658 176.246 179.615 1.00 73.95  ? 528 ASN A OD1 1 
ATOM   3497 N ND2 . ASN A 1 528 ? 161.415 176.790 177.575 1.00 72.97  ? 528 ASN A ND2 1 
ATOM   3498 N N   . SER A 1 529 ? 159.312 180.773 178.926 1.00 67.29  ? 529 SER A N   1 
ATOM   3499 C CA  . SER A 1 529 ? 158.404 181.319 177.918 1.00 68.26  ? 529 SER A CA  1 
ATOM   3500 C C   . SER A 1 529 ? 157.540 180.213 177.306 1.00 66.93  ? 529 SER A C   1 
ATOM   3501 O O   . SER A 1 529 ? 157.520 179.993 176.093 1.00 68.77  ? 529 SER A O   1 
ATOM   3502 C CB  . SER A 1 529 ? 159.173 182.087 176.837 1.00 61.10  ? 529 SER A CB  1 
ATOM   3503 O OG  . SER A 1 529 ? 158.508 182.012 175.589 1.00 61.17  ? 529 SER A OG  1 
ATOM   3504 N N   . GLU A 1 530 ? 156.820 179.515 178.181 1.00 58.86  ? 530 GLU A N   1 
ATOM   3505 C CA  . GLU A 1 530 ? 155.902 178.463 177.762 1.00 54.17  ? 530 GLU A CA  1 
ATOM   3506 C C   . GLU A 1 530 ? 154.895 178.228 178.876 1.00 67.59  ? 530 GLU A C   1 
ATOM   3507 O O   . GLU A 1 530 ? 155.282 178.094 180.040 1.00 78.83  ? 530 GLU A O   1 
ATOM   3508 C CB  . GLU A 1 530 ? 156.654 177.168 177.435 1.00 55.22  ? 530 GLU A CB  1 
ATOM   3509 C CG  . GLU A 1 530 ? 155.757 175.966 177.206 1.00 60.81  ? 530 GLU A CG  1 
ATOM   3510 C CD  . GLU A 1 530 ? 155.643 175.597 175.742 1.00 67.00  ? 530 GLU A CD  1 
ATOM   3511 O OE1 . GLU A 1 530 ? 156.270 176.279 174.905 1.00 71.14  ? 530 GLU A OE1 1 
ATOM   3512 O OE2 . GLU A 1 530 ? 154.927 174.623 175.428 1.00 58.09  ? 530 GLU A OE2 1 
ATOM   3513 N N   . CYS A 1 531 ? 153.614 178.182 178.520 1.00 64.67  ? 531 CYS A N   1 
ATOM   3514 C CA  . CYS A 1 531 ? 152.559 177.929 179.494 1.00 55.71  ? 531 CYS A CA  1 
ATOM   3515 C C   . CYS A 1 531 ? 152.495 176.439 179.797 1.00 52.38  ? 531 CYS A C   1 
ATOM   3516 O O   . CYS A 1 531 ? 152.202 175.631 178.910 1.00 51.38  ? 531 CYS A O   1 
ATOM   3517 C CB  . CYS A 1 531 ? 151.211 178.420 178.973 1.00 53.41  ? 531 CYS A CB  1 
ATOM   3518 S SG  . CYS A 1 531 ? 150.879 180.174 179.217 1.00 75.08  ? 531 CYS A SG  1 
ATOM   3519 N N   . ILE A 1 532 ? 152.763 176.077 181.046 1.00 49.87  ? 532 ILE A N   1 
ATOM   3520 C CA  . ILE A 1 532 ? 152.660 174.700 181.511 1.00 58.81  ? 532 ILE A CA  1 
ATOM   3521 C C   . ILE A 1 532 ? 151.514 174.638 182.509 1.00 68.99  ? 532 ILE A C   1 
ATOM   3522 O O   . ILE A 1 532 ? 151.562 175.289 183.559 1.00 74.77  ? 532 ILE A O   1 
ATOM   3523 C CB  . ILE A 1 532 ? 153.972 174.213 182.140 1.00 58.67  ? 532 ILE A CB  1 
ATOM   3524 C CG1 . ILE A 1 532 ? 155.073 174.137 181.081 1.00 68.15  ? 532 ILE A CG1 1 
ATOM   3525 C CG2 . ILE A 1 532 ? 153.773 172.862 182.804 1.00 66.24  ? 532 ILE A CG2 1 
ATOM   3526 C CD1 . ILE A 1 532 ? 154.891 173.009 180.090 1.00 72.24  ? 532 ILE A CD1 1 
ATOM   3527 N N   . GLN A 1 533 ? 150.483 173.866 182.180 1.00 67.58  ? 533 GLN A N   1 
ATOM   3528 C CA  . GLN A 1 533 ? 149.324 173.762 183.054 1.00 58.35  ? 533 GLN A CA  1 
ATOM   3529 C C   . GLN A 1 533 ? 149.718 173.102 184.369 1.00 59.30  ? 533 GLN A C   1 
ATOM   3530 O O   . GLN A 1 533 ? 150.421 172.089 184.380 1.00 63.14  ? 533 GLN A O   1 
ATOM   3531 C CB  . GLN A 1 533 ? 148.214 172.968 182.368 1.00 68.80  ? 533 GLN A CB  1 
ATOM   3532 C CG  . GLN A 1 533 ? 147.072 172.570 183.285 1.00 80.31  ? 533 GLN A CG  1 
ATOM   3533 C CD  . GLN A 1 533 ? 146.175 171.515 182.672 1.00 86.92  ? 533 GLN A CD  1 
ATOM   3534 O OE1 . GLN A 1 533 ? 146.177 171.312 181.458 1.00 93.28  ? 533 GLN A OE1 1 
ATOM   3535 N NE2 . GLN A 1 533 ? 145.401 170.835 183.510 1.00 84.37  ? 533 GLN A NE2 1 
ATOM   3536 N N   . CYS A 1 534 ? 149.268 173.710 185.473 1.00 62.04  ? 534 CYS A N   1 
ATOM   3537 C CA  . CYS A 1 534 ? 149.570 173.205 186.834 1.00 72.08  ? 534 CYS A CA  1 
ATOM   3538 C C   . CYS A 1 534 ? 148.821 171.889 187.067 1.00 86.32  ? 534 CYS A C   1 
ATOM   3539 O O   . CYS A 1 534 ? 147.814 171.649 186.374 1.00 83.98  ? 534 CYS A O   1 
ATOM   3540 C CB  . CYS A 1 534 ? 149.200 174.242 187.888 1.00 69.81  ? 534 CYS A CB  1 
ATOM   3541 S SG  . CYS A 1 534 ? 150.115 175.797 187.717 1.00 79.31  ? 534 CYS A SG  1 
ATOM   3542 N N   . HIS A 1 535 ? 149.257 171.096 188.038 1.00 95.51  ? 535 HIS A N   1 
ATOM   3543 C CA  . HIS A 1 535 ? 148.685 169.785 188.315 1.00 93.70  ? 535 HIS A CA  1 
ATOM   3544 C C   . HIS A 1 535 ? 147.205 169.928 188.657 1.00 98.74  ? 535 HIS A C   1 
ATOM   3545 O O   . HIS A 1 535 ? 146.843 170.788 189.468 1.00 99.76  ? 535 HIS A O   1 
ATOM   3546 C CB  . HIS A 1 535 ? 149.460 169.097 189.434 1.00 95.09  ? 535 HIS A CB  1 
ATOM   3547 C CG  . HIS A 1 535 ? 149.002 167.704 189.722 1.00 101.37 ? 535 HIS A CG  1 
ATOM   3548 N ND1 . HIS A 1 535 ? 148.030 167.419 190.658 1.00 105.07 ? 535 HIS A ND1 1 
ATOM   3549 C CD2 . HIS A 1 535 ? 149.380 166.514 189.199 1.00 106.83 ? 535 HIS A CD2 1 
ATOM   3550 C CE1 . HIS A 1 535 ? 147.836 166.113 190.703 1.00 111.25 ? 535 HIS A CE1 1 
ATOM   3551 N NE2 . HIS A 1 535 ? 148.643 165.541 189.829 1.00 111.04 ? 535 HIS A NE2 1 
ATOM   3552 N N   . PRO A 1 536 ? 146.327 169.114 188.067 1.00 103.12 ? 536 PRO A N   1 
ATOM   3553 C CA  . PRO A 1 536 ? 144.882 169.359 188.210 1.00 102.80 ? 536 PRO A CA  1 
ATOM   3554 C C   . PRO A 1 536 ? 144.363 169.249 189.632 1.00 105.53 ? 536 PRO A C   1 
ATOM   3555 O O   . PRO A 1 536 ? 143.297 169.803 189.925 1.00 109.25 ? 536 PRO A O   1 
ATOM   3556 C CB  . PRO A 1 536 ? 144.255 168.290 187.304 1.00 107.84 ? 536 PRO A CB  1 
ATOM   3557 C CG  . PRO A 1 536 ? 145.283 167.213 187.223 1.00 105.84 ? 536 PRO A CG  1 
ATOM   3558 C CD  . PRO A 1 536 ? 146.610 167.912 187.264 1.00 105.89 ? 536 PRO A CD  1 
ATOM   3559 N N   . GLU A 1 537 ? 145.070 168.559 190.526 1.00 106.47 ? 537 GLU A N   1 
ATOM   3560 C CA  . GLU A 1 537 ? 144.595 168.358 191.887 1.00 114.50 ? 537 GLU A CA  1 
ATOM   3561 C C   . GLU A 1 537 ? 145.037 169.463 192.841 1.00 118.54 ? 537 GLU A C   1 
ATOM   3562 O O   . GLU A 1 537 ? 145.040 169.251 194.059 1.00 122.90 ? 537 GLU A O   1 
ATOM   3563 C CB  . GLU A 1 537 ? 145.053 166.996 192.413 1.00 118.39 ? 537 GLU A CB  1 
ATOM   3564 C CG  . GLU A 1 537 ? 144.483 165.818 191.644 1.00 119.86 ? 537 GLU A CG  1 
ATOM   3565 C CD  . GLU A 1 537 ? 143.167 165.333 192.218 1.00 125.69 ? 537 GLU A CD  1 
ATOM   3566 O OE1 . GLU A 1 537 ? 143.130 164.985 193.416 1.00 125.03 ? 537 GLU A OE1 1 
ATOM   3567 O OE2 . GLU A 1 537 ? 142.168 165.299 191.469 1.00 129.08 ? 537 GLU A OE2 1 
ATOM   3568 N N   . CYS A 1 538 ? 145.407 170.631 192.323 1.00 115.07 ? 538 CYS A N   1 
ATOM   3569 C CA  . CYS A 1 538 ? 145.713 171.790 193.151 1.00 115.32 ? 538 CYS A CA  1 
ATOM   3570 C C   . CYS A 1 538 ? 144.788 172.935 192.762 1.00 110.00 ? 538 CYS A C   1 
ATOM   3571 O O   . CYS A 1 538 ? 144.672 173.276 191.580 1.00 108.93 ? 538 CYS A O   1 
ATOM   3572 C CB  . CYS A 1 538 ? 147.191 172.187 193.032 1.00 120.91 ? 538 CYS A CB  1 
ATOM   3573 S SG  . CYS A 1 538 ? 147.716 173.055 191.543 1.00 140.06 ? 538 CYS A SG  1 
ATOM   3574 N N   . LEU A 1 539 ? 144.118 173.507 193.758 1.00 108.76 ? 539 LEU A N   1 
ATOM   3575 C CA  . LEU A 1 539 ? 143.085 174.496 193.504 1.00 108.46 ? 539 LEU A CA  1 
ATOM   3576 C C   . LEU A 1 539 ? 143.699 175.823 193.057 1.00 107.38 ? 539 LEU A C   1 
ATOM   3577 O O   . LEU A 1 539 ? 144.778 176.205 193.517 1.00 111.33 ? 539 LEU A O   1 
ATOM   3578 C CB  . LEU A 1 539 ? 142.241 174.708 194.759 1.00 113.79 ? 539 LEU A CB  1 
ATOM   3579 C CG  . LEU A 1 539 ? 141.225 175.852 194.797 1.00 117.09 ? 539 LEU A CG  1 
ATOM   3580 C CD1 . LEU A 1 539 ? 139.867 175.382 194.301 1.00 118.13 ? 539 LEU A CD1 1 
ATOM   3581 C CD2 . LEU A 1 539 ? 141.116 176.426 196.201 1.00 116.80 ? 539 LEU A CD2 1 
ATOM   3582 N N   . PRO A 1 540 ? 143.065 176.576 192.129 1.00 102.91 ? 540 PRO A N   1 
ATOM   3583 C CA  . PRO A 1 540 ? 143.577 177.888 191.749 1.00 97.75  ? 540 PRO A CA  1 
ATOM   3584 C C   . PRO A 1 540 ? 143.677 178.870 192.906 1.00 100.06 ? 540 PRO A C   1 
ATOM   3585 O O   . PRO A 1 540 ? 142.838 178.776 193.826 1.00 94.61  ? 540 PRO A O   1 
ATOM   3586 C CB  . PRO A 1 540 ? 142.545 178.357 190.713 1.00 93.54  ? 540 PRO A CB  1 
ATOM   3587 C CG  . PRO A 1 540 ? 141.999 177.078 190.141 1.00 95.62  ? 540 PRO A CG  1 
ATOM   3588 C CD  . PRO A 1 540 ? 141.883 176.194 191.364 1.00 102.11 ? 540 PRO A CD  1 
ATOM   3589 N N   . GLN A 1 541 ? 144.657 179.780 192.873 1.00 106.93 ? 541 GLN A N   1 
ATOM   3590 C CA  . GLN A 1 541 ? 144.792 180.848 193.902 1.00 110.34 ? 541 GLN A CA  1 
ATOM   3591 C C   . GLN A 1 541 ? 144.460 182.184 193.219 1.00 111.17 ? 541 GLN A C   1 
ATOM   3592 O O   . GLN A 1 541 ? 145.136 182.502 192.217 1.00 106.06 ? 541 GLN A O   1 
ATOM   3593 C CB  . GLN A 1 541 ? 146.181 180.819 194.539 1.00 110.94 ? 541 GLN A CB  1 
ATOM   3594 C CG  . GLN A 1 541 ? 146.571 182.132 195.210 1.00 117.68 ? 541 GLN A CG  1 
ATOM   3595 C CD  . GLN A 1 541 ? 147.558 181.986 196.347 1.00 123.77 ? 541 GLN A CD  1 
ATOM   3596 O OE1 . GLN A 1 541 ? 147.906 180.882 196.776 1.00 129.46 ? 541 GLN A OE1 1 
ATOM   3597 N NE2 . GLN A 1 541 ? 147.999 183.120 196.873 1.00 115.49 ? 541 GLN A NE2 1 
ATOM   3598 N N   . ALA A 1 542 ? 143.491 182.946 193.738 1.00 112.38 ? 542 ALA A N   1 
ATOM   3599 C CA  . ALA A 1 542 ? 143.015 184.196 193.091 1.00 112.29 ? 542 ALA A CA  1 
ATOM   3600 C C   . ALA A 1 542 ? 143.756 185.428 193.617 1.00 115.37 ? 542 ALA A C   1 
ATOM   3601 O O   . ALA A 1 542 ? 143.485 186.526 193.081 1.00 117.64 ? 542 ALA A O   1 
ATOM   3602 C CB  . ALA A 1 542 ? 141.524 184.330 193.305 1.00 105.65 ? 542 ALA A CB  1 
ATOM   3603 N N   . MET A 1 543 ? 144.656 185.279 194.596 1.00 112.07 ? 543 MET A N   1 
ATOM   3604 C CA  . MET A 1 543 ? 145.439 186.393 195.121 1.00 113.56 ? 543 MET A CA  1 
ATOM   3605 C C   . MET A 1 543 ? 146.810 186.497 194.464 1.00 109.09 ? 543 MET A C   1 
ATOM   3606 O O   . MET A 1 543 ? 147.198 187.573 194.000 1.00 105.13 ? 543 MET A O   1 
ATOM   3607 C CB  . MET A 1 543 ? 145.592 186.253 196.642 1.00 115.79 ? 543 MET A CB  1 
ATOM   3608 C CG  . MET A 1 543 ? 146.725 187.070 197.250 1.00 117.75 ? 543 MET A CG  1 
ATOM   3609 S SD  . MET A 1 543 ? 146.628 188.831 196.867 1.00 113.57 ? 543 MET A SD  1 
ATOM   3610 C CE  . MET A 1 543 ? 148.357 189.291 196.945 1.00 95.60  ? 543 MET A CE  1 
ATOM   3611 N N   . ASN A 1 544 ? 147.549 185.392 194.412 1.00 105.89 ? 544 ASN A N   1 
ATOM   3612 C CA  . ASN A 1 544 ? 148.867 185.363 193.792 1.00 100.86 ? 544 ASN A CA  1 
ATOM   3613 C C   . ASN A 1 544 ? 148.913 184.270 192.734 1.00 101.14 ? 544 ASN A C   1 
ATOM   3614 O O   . ASN A 1 544 ? 147.867 183.743 192.342 1.00 103.52 ? 544 ASN A O   1 
ATOM   3615 C CB  . ASN A 1 544 ? 149.960 185.150 194.840 1.00 102.83 ? 544 ASN A CB  1 
ATOM   3616 C CG  . ASN A 1 544 ? 150.765 186.406 195.105 1.00 109.32 ? 544 ASN A CG  1 
ATOM   3617 O OD1 . ASN A 1 544 ? 150.267 187.520 194.944 1.00 102.81 ? 544 ASN A OD1 1 
ATOM   3618 N ND2 . ASN A 1 544 ? 152.018 186.233 195.509 1.00 118.15 ? 544 ASN A ND2 1 
ATOM   3619 N N   . ILE A 1 545 ? 150.113 183.943 192.249 1.00 93.93  ? 545 ILE A N   1 
ATOM   3620 C CA  . ILE A 1 545 ? 150.242 182.919 191.219 1.00 87.88  ? 545 ILE A CA  1 
ATOM   3621 C C   . ILE A 1 545 ? 149.629 181.604 191.689 1.00 91.08  ? 545 ILE A C   1 
ATOM   3622 O O   . ILE A 1 545 ? 149.649 181.267 192.879 1.00 88.69  ? 545 ILE A O   1 
ATOM   3623 C CB  . ILE A 1 545 ? 151.714 182.776 190.784 1.00 82.38  ? 545 ILE A CB  1 
ATOM   3624 C CG1 . ILE A 1 545 ? 152.714 182.832 191.958 1.00 85.39  ? 545 ILE A CG1 1 
ATOM   3625 C CG2 . ILE A 1 545 ? 152.064 183.842 189.763 1.00 80.09  ? 545 ILE A CG2 1 
ATOM   3626 C CD1 . ILE A 1 545 ? 152.582 181.792 193.048 1.00 86.45  ? 545 ILE A CD1 1 
ATOM   3627 N N   . THR A 1 546 ? 148.995 180.878 190.762 1.00 89.24  ? 546 THR A N   1 
ATOM   3628 C CA  . THR A 1 546 ? 148.280 179.618 191.078 1.00 85.29  ? 546 THR A CA  1 
ATOM   3629 C C   . THR A 1 546 ? 149.262 178.544 191.499 1.00 82.45  ? 546 THR A C   1 
ATOM   3630 O O   . THR A 1 546 ? 148.942 177.821 192.468 1.00 90.19  ? 546 THR A O   1 
ATOM   3631 C CB  . THR A 1 546 ? 147.451 179.196 189.865 1.00 82.59  ? 546 THR A CB  1 
ATOM   3632 O OG1 . THR A 1 546 ? 146.756 178.026 190.284 1.00 92.39  ? 546 THR A OG1 1 
ATOM   3633 C CG2 . THR A 1 546 ? 148.286 178.879 188.637 1.00 74.71  ? 546 THR A CG2 1 
ATOM   3634 N N   . CYS A 1 547 ? 150.398 178.404 190.806 1.00 76.15  ? 547 CYS A N   1 
ATOM   3635 C CA  . CYS A 1 547 ? 151.404 177.410 191.151 1.00 74.30  ? 547 CYS A CA  1 
ATOM   3636 C C   . CYS A 1 547 ? 152.749 177.866 190.608 1.00 68.94  ? 547 CYS A C   1 
ATOM   3637 O O   . CYS A 1 547 ? 152.835 178.340 189.471 1.00 72.88  ? 547 CYS A O   1 
ATOM   3638 C CB  . CYS A 1 547 ? 151.024 176.027 190.607 1.00 80.34  ? 547 CYS A CB  1 
ATOM   3639 S SG  . CYS A 1 547 ? 151.687 175.581 188.987 1.00 83.34  ? 547 CYS A SG  1 
ATOM   3640 N N   . THR A 1 548 ? 153.789 177.748 191.435 1.00 66.69  ? 548 THR A N   1 
ATOM   3641 C CA  . THR A 1 548 ? 155.112 178.209 191.028 1.00 64.50  ? 548 THR A CA  1 
ATOM   3642 C C   . THR A 1 548 ? 155.716 177.297 189.967 1.00 70.65  ? 548 THR A C   1 
ATOM   3643 O O   . THR A 1 548 ? 156.359 177.774 189.025 1.00 81.14  ? 548 THR A O   1 
ATOM   3644 C CB  . THR A 1 548 ? 156.031 178.304 192.245 1.00 61.28  ? 548 THR A CB  1 
ATOM   3645 O OG1 . THR A 1 548 ? 155.425 179.143 193.235 1.00 65.48  ? 548 THR A OG1 1 
ATOM   3646 C CG2 . THR A 1 548 ? 157.376 178.892 191.853 1.00 61.98  ? 548 THR A CG2 1 
ATOM   3647 N N   . GLY A 1 549 ? 155.520 175.983 190.100 1.00 62.52  ? 549 GLY A N   1 
ATOM   3648 C CA  . GLY A 1 549 ? 156.069 175.040 189.151 1.00 62.48  ? 549 GLY A CA  1 
ATOM   3649 C C   . GLY A 1 549 ? 155.117 173.885 188.918 1.00 74.37  ? 549 GLY A C   1 
ATOM   3650 O O   . GLY A 1 549 ? 154.168 173.670 189.675 1.00 82.14  ? 549 GLY A O   1 
ATOM   3651 N N   . ARG A 1 550 ? 155.388 173.143 187.847 1.00 79.05  ? 550 ARG A N   1 
ATOM   3652 C CA  . ARG A 1 550 ? 154.560 171.999 187.500 1.00 79.79  ? 550 ARG A CA  1 
ATOM   3653 C C   . ARG A 1 550 ? 154.712 170.893 188.538 1.00 77.52  ? 550 ARG A C   1 
ATOM   3654 O O   . ARG A 1 550 ? 155.743 170.769 189.204 1.00 79.17  ? 550 ARG A O   1 
ATOM   3655 C CB  . ARG A 1 550 ? 154.928 171.474 186.112 1.00 73.31  ? 550 ARG A CB  1 
ATOM   3656 C CG  . ARG A 1 550 ? 156.216 170.671 186.067 1.00 80.88  ? 550 ARG A CG  1 
ATOM   3657 C CD  . ARG A 1 550 ? 156.583 170.295 184.643 1.00 83.90  ? 550 ARG A CD  1 
ATOM   3658 N NE  . ARG A 1 550 ? 157.607 171.177 184.095 1.00 89.23  ? 550 ARG A NE  1 
ATOM   3659 C CZ  . ARG A 1 550 ? 157.722 171.483 182.810 1.00 88.35  ? 550 ARG A CZ  1 
ATOM   3660 N NH1 . ARG A 1 550 ? 156.891 170.992 181.906 1.00 85.40  ? 550 ARG A NH1 1 
ATOM   3661 N NH2 . ARG A 1 550 ? 158.697 172.301 182.423 1.00 82.08  ? 550 ARG A NH2 1 
ATOM   3662 N N   . GLY A 1 551 ? 153.664 170.087 188.676 1.00 75.09  ? 551 GLY A N   1 
ATOM   3663 C CA  . GLY A 1 551 ? 153.663 169.009 189.634 1.00 82.32  ? 551 GLY A CA  1 
ATOM   3664 C C   . GLY A 1 551 ? 152.925 169.373 190.905 1.00 91.80  ? 551 GLY A C   1 
ATOM   3665 O O   . GLY A 1 551 ? 152.817 170.546 191.276 1.00 91.53  ? 551 GLY A O   1 
ATOM   3666 N N   . PRO A 1 552 ? 152.392 168.363 191.595 1.00 95.51  ? 552 PRO A N   1 
ATOM   3667 C CA  . PRO A 1 552 ? 151.625 168.638 192.822 1.00 99.10  ? 552 PRO A CA  1 
ATOM   3668 C C   . PRO A 1 552 ? 152.441 169.294 193.920 1.00 95.37  ? 552 PRO A C   1 
ATOM   3669 O O   . PRO A 1 552 ? 151.875 170.019 194.747 1.00 99.71  ? 552 PRO A O   1 
ATOM   3670 C CB  . PRO A 1 552 ? 151.130 167.247 193.244 1.00 106.24 ? 552 PRO A CB  1 
ATOM   3671 C CG  . PRO A 1 552 ? 151.258 166.393 192.019 1.00 99.28  ? 552 PRO A CG  1 
ATOM   3672 C CD  . PRO A 1 552 ? 152.434 166.928 191.275 1.00 93.30  ? 552 PRO A CD  1 
ATOM   3673 N N   . ASP A 1 553 ? 153.754 169.055 193.960 1.00 92.04  ? 553 ASP A N   1 
ATOM   3674 C CA  . ASP A 1 553 ? 154.576 169.589 195.042 1.00 91.51  ? 553 ASP A CA  1 
ATOM   3675 C C   . ASP A 1 553 ? 154.617 171.112 194.992 1.00 92.62  ? 553 ASP A C   1 
ATOM   3676 O O   . ASP A 1 553 ? 154.447 171.778 196.020 1.00 93.87  ? 553 ASP A O   1 
ATOM   3677 C CB  . ASP A 1 553 ? 155.981 168.972 194.955 1.00 97.05  ? 553 ASP A CB  1 
ATOM   3678 C CG  . ASP A 1 553 ? 156.994 169.571 195.944 1.00 101.69 ? 553 ASP A CG  1 
ATOM   3679 O OD1 . ASP A 1 553 ? 156.942 170.767 196.296 1.00 93.29  ? 553 ASP A OD1 1 
ATOM   3680 O OD2 . ASP A 1 553 ? 157.876 168.804 196.385 1.00 114.45 ? 553 ASP A OD2 1 
ATOM   3681 N N   . ASN A 1 554 ? 154.815 171.681 193.805 1.00 93.73  ? 554 ASN A N   1 
ATOM   3682 C CA  . ASN A 1 554 ? 155.034 173.114 193.672 1.00 86.84  ? 554 ASN A CA  1 
ATOM   3683 C C   . ASN A 1 554 ? 153.751 173.933 193.670 1.00 89.56  ? 554 ASN A C   1 
ATOM   3684 O O   . ASN A 1 554 ? 153.829 175.165 193.720 1.00 90.80  ? 554 ASN A O   1 
ATOM   3685 C CB  . ASN A 1 554 ? 155.823 173.407 192.394 1.00 78.53  ? 554 ASN A CB  1 
ATOM   3686 C CG  . ASN A 1 554 ? 157.266 172.963 192.487 1.00 87.95  ? 554 ASN A CG  1 
ATOM   3687 O OD1 . ASN A 1 554 ? 157.816 172.828 193.580 1.00 92.24  ? 554 ASN A OD1 1 
ATOM   3688 N ND2 . ASN A 1 554 ? 157.891 172.738 191.339 1.00 87.04  ? 554 ASN A ND2 1 
ATOM   3689 N N   . CYS A 1 555 ? 152.583 173.297 193.608 1.00 95.00  ? 555 CYS A N   1 
ATOM   3690 C CA  . CYS A 1 555 ? 151.332 174.041 193.676 1.00 94.68  ? 555 CYS A CA  1 
ATOM   3691 C C   . CYS A 1 555 ? 151.188 174.687 195.050 1.00 92.94  ? 555 CYS A C   1 
ATOM   3692 O O   . CYS A 1 555 ? 151.357 174.026 196.078 1.00 98.36  ? 555 CYS A O   1 
ATOM   3693 C CB  . CYS A 1 555 ? 150.144 173.121 193.387 1.00 104.48 ? 555 CYS A CB  1 
ATOM   3694 S SG  . CYS A 1 555 ? 149.743 172.934 191.625 1.00 115.61 ? 555 CYS A SG  1 
ATOM   3695 N N   . ILE A 1 556 ? 150.876 175.983 195.065 1.00 92.47  ? 556 ILE A N   1 
ATOM   3696 C CA  . ILE A 1 556 ? 150.814 176.724 196.321 1.00 98.53  ? 556 ILE A CA  1 
ATOM   3697 C C   . ILE A 1 556 ? 149.446 176.642 196.990 1.00 108.95 ? 556 ILE A C   1 
ATOM   3698 O O   . ILE A 1 556 ? 149.343 176.888 198.201 1.00 114.77 ? 556 ILE A O   1 
ATOM   3699 C CB  . ILE A 1 556 ? 151.206 178.197 196.102 1.00 93.90  ? 556 ILE A CB  1 
ATOM   3700 C CG1 . ILE A 1 556 ? 151.710 178.819 197.407 1.00 90.21  ? 556 ILE A CG1 1 
ATOM   3701 C CG2 . ILE A 1 556 ? 150.037 178.992 195.539 1.00 97.33  ? 556 ILE A CG2 1 
ATOM   3702 C CD1 . ILE A 1 556 ? 151.898 180.319 197.340 1.00 85.65  ? 556 ILE A CD1 1 
ATOM   3703 N N   . GLN A 1 557 ? 148.397 176.298 196.248 1.00 111.28 ? 557 GLN A N   1 
ATOM   3704 C CA  . GLN A 1 557 ? 147.054 176.165 196.793 1.00 117.32 ? 557 GLN A CA  1 
ATOM   3705 C C   . GLN A 1 557 ? 146.525 174.778 196.464 1.00 116.38 ? 557 GLN A C   1 
ATOM   3706 O O   . GLN A 1 557 ? 146.596 174.340 195.312 1.00 108.60 ? 557 GLN A O   1 
ATOM   3707 C CB  . GLN A 1 557 ? 146.122 177.243 196.234 1.00 113.64 ? 557 GLN A CB  1 
ATOM   3708 C CG  . GLN A 1 557 ? 144.688 177.153 196.734 1.00 114.75 ? 557 GLN A CG  1 
ATOM   3709 C CD  . GLN A 1 557 ? 144.580 177.291 198.241 1.00 117.36 ? 557 GLN A CD  1 
ATOM   3710 O OE1 . GLN A 1 557 ? 145.357 178.011 198.869 1.00 119.53 ? 557 GLN A OE1 1 
ATOM   3711 N NE2 . GLN A 1 557 ? 143.612 176.600 198.830 1.00 113.42 ? 557 GLN A NE2 1 
ATOM   3712 N N   . CYS A 1 558 ? 145.995 174.092 197.476 1.00 123.72 ? 558 CYS A N   1 
ATOM   3713 C CA  . CYS A 1 558 ? 145.511 172.721 197.318 1.00 129.27 ? 558 CYS A CA  1 
ATOM   3714 C C   . CYS A 1 558 ? 144.258 172.546 198.171 1.00 129.52 ? 558 CYS A C   1 
ATOM   3715 O O   . CYS A 1 558 ? 144.350 172.301 199.378 1.00 129.04 ? 558 CYS A O   1 
ATOM   3716 C CB  . CYS A 1 558 ? 146.587 171.712 197.703 1.00 132.31 ? 558 CYS A CB  1 
ATOM   3717 S SG  . CYS A 1 558 ? 147.559 171.108 196.307 1.00 137.98 ? 558 CYS A SG  1 
ATOM   3718 N N   . ALA A 1 559 ? 143.088 172.678 197.540 1.00 128.00 ? 559 ALA A N   1 
ATOM   3719 C CA  . ALA A 1 559 ? 141.841 172.378 198.235 1.00 130.47 ? 559 ALA A CA  1 
ATOM   3720 C C   . ALA A 1 559 ? 141.713 170.890 198.526 1.00 135.79 ? 559 ALA A C   1 
ATOM   3721 O O   . ALA A 1 559 ? 141.160 170.507 199.563 1.00 137.74 ? 559 ALA A O   1 
ATOM   3722 C CB  . ALA A 1 559 ? 140.645 172.865 197.417 1.00 127.03 ? 559 ALA A CB  1 
ATOM   3723 N N   . HIS A 1 560 ? 142.211 170.043 197.628 1.00 132.62 ? 560 HIS A N   1 
ATOM   3724 C CA  . HIS A 1 560 ? 142.230 168.612 197.874 1.00 131.86 ? 560 HIS A CA  1 
ATOM   3725 C C   . HIS A 1 560 ? 143.251 168.281 198.961 1.00 136.01 ? 560 HIS A C   1 
ATOM   3726 O O   . HIS A 1 560 ? 144.031 169.131 199.402 1.00 134.81 ? 560 HIS A O   1 
ATOM   3727 C CB  . HIS A 1 560 ? 142.548 167.852 196.587 1.00 130.23 ? 560 HIS A CB  1 
ATOM   3728 C CG  . HIS A 1 560 ? 141.337 167.325 195.883 1.00 132.62 ? 560 HIS A CG  1 
ATOM   3729 N ND1 . HIS A 1 560 ? 140.270 166.767 196.554 1.00 132.03 ? 560 HIS A ND1 1 
ATOM   3730 C CD2 . HIS A 1 560 ? 141.023 167.274 194.567 1.00 132.77 ? 560 HIS A CD2 1 
ATOM   3731 C CE1 . HIS A 1 560 ? 139.351 166.393 195.682 1.00 131.10 ? 560 HIS A CE1 1 
ATOM   3732 N NE2 . HIS A 1 560 ? 139.783 166.689 194.469 1.00 134.37 ? 560 HIS A NE2 1 
ATOM   3733 N N   . TYR A 1 561 ? 143.241 167.025 199.396 1.00 137.58 ? 561 TYR A N   1 
ATOM   3734 C CA  . TYR A 1 561 ? 144.111 166.619 200.490 1.00 142.42 ? 561 TYR A CA  1 
ATOM   3735 C C   . TYR A 1 561 ? 145.576 166.685 200.072 1.00 146.23 ? 561 TYR A C   1 
ATOM   3736 O O   . TYR A 1 561 ? 145.914 166.625 198.887 1.00 142.06 ? 561 TYR A O   1 
ATOM   3737 C CB  . TYR A 1 561 ? 143.766 165.208 200.962 1.00 143.75 ? 561 TYR A CB  1 
ATOM   3738 C CG  . TYR A 1 561 ? 144.360 164.878 202.313 1.00 149.45 ? 561 TYR A CG  1 
ATOM   3739 C CD1 . TYR A 1 561 ? 144.314 165.797 203.352 1.00 145.57 ? 561 TYR A CD1 1 
ATOM   3740 C CD2 . TYR A 1 561 ? 144.969 163.653 202.548 1.00 149.92 ? 561 TYR A CD2 1 
ATOM   3741 C CE1 . TYR A 1 561 ? 144.857 165.506 204.589 1.00 147.85 ? 561 TYR A CE1 1 
ATOM   3742 C CE2 . TYR A 1 561 ? 145.516 163.354 203.782 1.00 148.71 ? 561 TYR A CE2 1 
ATOM   3743 C CZ  . TYR A 1 561 ? 145.456 164.282 204.798 1.00 149.57 ? 561 TYR A CZ  1 
ATOM   3744 O OH  . TYR A 1 561 ? 145.998 163.986 206.027 1.00 148.15 ? 561 TYR A OH  1 
ATOM   3745 N N   . ILE A 1 562 ? 146.448 166.818 201.068 1.00 148.88 ? 562 ILE A N   1 
ATOM   3746 C CA  . ILE A 1 562 ? 147.884 166.948 200.858 1.00 141.37 ? 562 ILE A CA  1 
ATOM   3747 C C   . ILE A 1 562 ? 148.600 165.889 201.683 1.00 143.51 ? 562 ILE A C   1 
ATOM   3748 O O   . ILE A 1 562 ? 148.199 165.590 202.813 1.00 142.38 ? 562 ILE A O   1 
ATOM   3749 C CB  . ILE A 1 562 ? 148.383 168.362 201.224 1.00 136.80 ? 562 ILE A CB  1 
ATOM   3750 C CG1 . ILE A 1 562 ? 148.011 168.709 202.667 1.00 138.04 ? 562 ILE A CG1 1 
ATOM   3751 C CG2 . ILE A 1 562 ? 147.807 169.391 200.270 1.00 138.51 ? 562 ILE A CG2 1 
ATOM   3752 C CD1 . ILE A 1 562 ? 149.160 169.252 203.482 1.00 135.90 ? 562 ILE A CD1 1 
ATOM   3753 N N   . ASP A 1 563 ? 149.640 165.301 201.076 1.00 143.60 ? 563 ASP A N   1 
ATOM   3754 C CA  . ASP A 1 563 ? 150.464 164.279 201.779 1.00 146.27 ? 563 ASP A CA  1 
ATOM   3755 C C   . ASP A 1 563 ? 151.751 164.956 202.248 1.00 142.39 ? 563 ASP A C   1 
ATOM   3756 O O   . ASP A 1 563 ? 152.606 165.267 201.390 1.00 140.31 ? 563 ASP A O   1 
ATOM   3757 C CB  . ASP A 1 563 ? 150.721 163.062 200.905 1.00 151.61 ? 563 ASP A CB  1 
ATOM   3758 C CG  . ASP A 1 563 ? 150.770 161.736 201.650 1.00 151.50 ? 563 ASP A CG  1 
ATOM   3759 O OD1 . ASP A 1 563 ? 150.022 161.596 202.640 1.00 152.32 ? 563 ASP A OD1 1 
ATOM   3760 O OD2 . ASP A 1 563 ? 151.558 160.859 201.238 1.00 148.19 ? 563 ASP A OD2 1 
ATOM   3761 N N   . GLY A 1 564 ? 151.890 165.165 203.555 1.00 142.40 ? 564 GLY A N   1 
ATOM   3762 C CA  . GLY A 1 564 ? 153.025 165.862 204.111 1.00 139.11 ? 564 GLY A CA  1 
ATOM   3763 C C   . GLY A 1 564 ? 153.107 167.288 203.605 1.00 138.88 ? 564 GLY A C   1 
ATOM   3764 O O   . GLY A 1 564 ? 152.137 168.049 203.669 1.00 137.36 ? 564 GLY A O   1 
ATOM   3765 N N   . PRO A 1 565 ? 154.273 167.680 203.095 1.00 139.04 ? 565 PRO A N   1 
ATOM   3766 C CA  . PRO A 1 565 ? 154.415 169.000 202.468 1.00 135.80 ? 565 PRO A CA  1 
ATOM   3767 C C   . PRO A 1 565 ? 154.041 169.039 200.994 1.00 131.13 ? 565 PRO A C   1 
ATOM   3768 O O   . PRO A 1 565 ? 154.100 170.116 200.391 1.00 126.34 ? 565 PRO A O   1 
ATOM   3769 C CB  . PRO A 1 565 ? 155.910 169.291 202.653 1.00 135.62 ? 565 PRO A CB  1 
ATOM   3770 C CG  . PRO A 1 565 ? 156.558 167.942 202.630 1.00 137.44 ? 565 PRO A CG  1 
ATOM   3771 C CD  . PRO A 1 565 ? 155.537 166.924 203.083 1.00 137.99 ? 565 PRO A CD  1 
ATOM   3772 N N   . HIS A 1 566 ? 153.662 167.908 200.408 1.00 131.54 ? 566 HIS A N   1 
ATOM   3773 C CA  . HIS A 1 566 ? 153.294 167.822 199.004 1.00 125.39 ? 566 HIS A CA  1 
ATOM   3774 C C   . HIS A 1 566 ? 151.799 167.570 198.865 1.00 128.05 ? 566 HIS A C   1 
ATOM   3775 O O   . HIS A 1 566 ? 151.127 167.127 199.800 1.00 132.21 ? 566 HIS A O   1 
ATOM   3776 C CB  . HIS A 1 566 ? 154.070 166.709 198.287 1.00 119.43 ? 566 HIS A CB  1 
ATOM   3777 C CG  . HIS A 1 566 ? 155.542 166.703 198.565 1.00 117.52 ? 566 HIS A CG  1 
ATOM   3778 N ND1 . HIS A 1 566 ? 156.188 167.729 199.222 1.00 113.97 ? 566 HIS A ND1 1 
ATOM   3779 C CD2 . HIS A 1 566 ? 156.496 165.789 198.270 1.00 120.62 ? 566 HIS A CD2 1 
ATOM   3780 C CE1 . HIS A 1 566 ? 157.474 167.447 199.320 1.00 115.50 ? 566 HIS A CE1 1 
ATOM   3781 N NE2 . HIS A 1 566 ? 157.688 166.275 198.751 1.00 122.79 ? 566 HIS A NE2 1 
ATOM   3782 N N   . CYS A 1 567 ? 151.284 167.862 197.676 1.00 122.41 ? 567 CYS A N   1 
ATOM   3783 C CA  . CYS A 1 567 ? 149.890 167.602 197.353 1.00 124.25 ? 567 CYS A CA  1 
ATOM   3784 C C   . CYS A 1 567 ? 149.746 166.224 196.720 1.00 129.11 ? 567 CYS A C   1 
ATOM   3785 O O   . CYS A 1 567 ? 150.669 165.712 196.082 1.00 133.58 ? 567 CYS A O   1 
ATOM   3786 C CB  . CYS A 1 567 ? 149.347 168.674 196.408 1.00 126.54 ? 567 CYS A CB  1 
ATOM   3787 S SG  . CYS A 1 567 ? 149.229 170.318 197.144 1.00 140.36 ? 567 CYS A SG  1 
ATOM   3788 N N   . VAL A 1 568 ? 148.574 165.621 196.911 1.00 133.28 ? 568 VAL A N   1 
ATOM   3789 C CA  . VAL A 1 568 ? 148.277 164.286 196.407 1.00 142.16 ? 568 VAL A CA  1 
ATOM   3790 C C   . VAL A 1 568 ? 146.776 164.189 196.156 1.00 140.94 ? 568 VAL A C   1 
ATOM   3791 O O   . VAL A 1 568 ? 145.998 165.051 196.570 1.00 139.87 ? 568 VAL A O   1 
ATOM   3792 C CB  . VAL A 1 568 ? 148.746 163.186 197.389 1.00 145.64 ? 568 VAL A CB  1 
ATOM   3793 C CG1 . VAL A 1 568 ? 147.720 162.982 198.493 1.00 145.39 ? 568 VAL A CG1 1 
ATOM   3794 C CG2 . VAL A 1 568 ? 149.037 161.883 196.651 1.00 139.04 ? 568 VAL A CG2 1 
ATOM   3795 N N   . LYS A 1 569 ? 146.365 163.128 195.457 1.00 140.81 ? 569 LYS A N   1 
ATOM   3796 C CA  . LYS A 1 569 ? 144.944 162.897 195.217 1.00 137.18 ? 569 LYS A CA  1 
ATOM   3797 C C   . LYS A 1 569 ? 144.212 162.613 196.523 1.00 141.73 ? 569 LYS A C   1 
ATOM   3798 O O   . LYS A 1 569 ? 143.306 163.355 196.919 1.00 138.59 ? 569 LYS A O   1 
ATOM   3799 C CB  . LYS A 1 569 ? 144.760 161.736 194.237 1.00 136.36 ? 569 LYS A CB  1 
ATOM   3800 C CG  . LYS A 1 569 ? 144.571 162.155 192.789 1.00 132.76 ? 569 LYS A CG  1 
ATOM   3801 C CD  . LYS A 1 569 ? 145.899 162.496 192.136 1.00 132.46 ? 569 LYS A CD  1 
ATOM   3802 C CE  . LYS A 1 569 ? 145.960 161.972 190.711 1.00 121.61 ? 569 LYS A CE  1 
ATOM   3803 N NZ  . LYS A 1 569 ? 147.354 161.938 190.191 1.00 107.82 ? 569 LYS A NZ  1 
ATOM   3804 N N   . THR A 1 570 ? 144.601 161.542 197.211 1.00 148.07 ? 570 THR A N   1 
ATOM   3805 C CA  . THR A 1 570 ? 143.992 161.143 198.471 1.00 149.99 ? 570 THR A CA  1 
ATOM   3806 C C   . THR A 1 570 ? 145.070 160.568 199.378 1.00 151.19 ? 570 THR A C   1 
ATOM   3807 O O   . THR A 1 570 ? 146.168 160.221 198.934 1.00 149.66 ? 570 THR A O   1 
ATOM   3808 C CB  . THR A 1 570 ? 142.869 160.116 198.264 1.00 146.64 ? 570 THR A CB  1 
ATOM   3809 O OG1 . THR A 1 570 ? 143.260 159.171 197.260 1.00 137.11 ? 570 THR A OG1 1 
ATOM   3810 C CG2 . THR A 1 570 ? 141.578 160.802 197.842 1.00 142.94 ? 570 THR A CG2 1 
ATOM   3811 N N   . CYS A 1 571 ? 144.745 160.469 200.662 1.00 150.18 ? 571 CYS A N   1 
ATOM   3812 C CA  . CYS A 1 571 ? 145.692 159.935 201.627 1.00 151.51 ? 571 CYS A CA  1 
ATOM   3813 C C   . CYS A 1 571 ? 146.009 158.478 201.297 1.00 154.50 ? 571 CYS A C   1 
ATOM   3814 O O   . CYS A 1 571 ? 145.105 157.707 200.952 1.00 151.74 ? 571 CYS A O   1 
ATOM   3815 C CB  . CYS A 1 571 ? 145.130 160.036 203.045 1.00 148.71 ? 571 CYS A CB  1 
ATOM   3816 S SG  . CYS A 1 571 ? 146.372 159.926 204.352 1.00 148.32 ? 571 CYS A SG  1 
ATOM   3817 N N   . PRO A 1 572 ? 147.275 158.066 201.386 1.00 155.66 ? 572 PRO A N   1 
ATOM   3818 C CA  . PRO A 1 572 ? 147.618 156.660 201.122 1.00 157.75 ? 572 PRO A CA  1 
ATOM   3819 C C   . PRO A 1 572 ? 147.101 155.765 202.238 1.00 159.21 ? 572 PRO A C   1 
ATOM   3820 O O   . PRO A 1 572 ? 147.482 155.917 203.401 1.00 156.04 ? 572 PRO A O   1 
ATOM   3821 C CB  . PRO A 1 572 ? 149.149 156.673 201.065 1.00 159.04 ? 572 PRO A CB  1 
ATOM   3822 C CG  . PRO A 1 572 ? 149.548 157.859 201.879 1.00 153.09 ? 572 PRO A CG  1 
ATOM   3823 C CD  . PRO A 1 572 ? 148.461 158.882 201.700 1.00 150.73 ? 572 PRO A CD  1 
ATOM   3824 N N   . ALA A 1 573 ? 146.216 154.837 201.881 1.00 162.95 ? 573 ALA A N   1 
ATOM   3825 C CA  . ALA A 1 573 ? 145.666 153.876 202.828 1.00 161.01 ? 573 ALA A CA  1 
ATOM   3826 C C   . ALA A 1 573 ? 146.029 152.443 202.476 1.00 157.18 ? 573 ALA A C   1 
ATOM   3827 O O   . ALA A 1 573 ? 146.566 151.718 203.323 1.00 156.67 ? 573 ALA A O   1 
ATOM   3828 C CB  . ALA A 1 573 ? 144.138 154.027 202.907 1.00 157.49 ? 573 ALA A CB  1 
ATOM   3829 N N   . GLY A 1 574 ? 145.752 152.013 201.249 1.00 156.43 ? 574 GLY A N   1 
ATOM   3830 C CA  . GLY A 1 574 ? 146.115 150.680 200.812 1.00 160.00 ? 574 GLY A CA  1 
ATOM   3831 C C   . GLY A 1 574 ? 147.464 150.643 200.127 1.00 165.29 ? 574 GLY A C   1 
ATOM   3832 O O   . GLY A 1 574 ? 147.558 150.313 198.941 1.00 167.26 ? 574 GLY A O   1 
ATOM   3833 N N   . VAL A 1 575 ? 148.520 150.980 200.866 1.00 164.69 ? 575 VAL A N   1 
ATOM   3834 C CA  . VAL A 1 575 ? 149.868 151.020 200.311 1.00 164.42 ? 575 VAL A CA  1 
ATOM   3835 C C   . VAL A 1 575 ? 150.710 149.927 200.954 1.00 165.66 ? 575 VAL A C   1 
ATOM   3836 O O   . VAL A 1 575 ? 150.247 149.220 201.856 1.00 165.30 ? 575 VAL A O   1 
ATOM   3837 C CB  . VAL A 1 575 ? 150.512 152.404 200.511 1.00 160.29 ? 575 VAL A CB  1 
ATOM   3838 C CG1 . VAL A 1 575 ? 149.948 153.398 199.508 1.00 157.96 ? 575 VAL A CG1 1 
ATOM   3839 C CG2 . VAL A 1 575 ? 150.290 152.891 201.934 1.00 157.19 ? 575 VAL A CG2 1 
ATOM   3840 N N   . MET A 1 576 ? 151.947 149.779 200.492 1.00 168.13 ? 576 MET A N   1 
ATOM   3841 C CA  . MET A 1 576 ? 152.846 148.742 200.970 1.00 168.42 ? 576 MET A CA  1 
ATOM   3842 C C   . MET A 1 576 ? 153.996 149.359 201.756 1.00 165.04 ? 576 MET A C   1 
ATOM   3843 O O   . MET A 1 576 ? 154.488 150.442 201.425 1.00 161.04 ? 576 MET A O   1 
ATOM   3844 C CB  . MET A 1 576 ? 153.399 147.914 199.806 1.00 167.82 ? 576 MET A CB  1 
ATOM   3845 C CG  . MET A 1 576 ? 152.381 147.596 198.723 1.00 167.72 ? 576 MET A CG  1 
ATOM   3846 S SD  . MET A 1 576 ? 151.806 149.065 197.849 1.00 166.50 ? 576 MET A SD  1 
ATOM   3847 C CE  . MET A 1 576 ? 153.321 149.607 197.063 1.00 161.00 ? 576 MET A CE  1 
ATOM   3848 N N   . GLY A 1 577 ? 154.420 148.656 202.804 1.00 167.74 ? 577 GLY A N   1 
ATOM   3849 C CA  . GLY A 1 577 ? 155.501 149.127 203.648 1.00 167.51 ? 577 GLY A CA  1 
ATOM   3850 C C   . GLY A 1 577 ? 156.679 148.177 203.700 1.00 166.03 ? 577 GLY A C   1 
ATOM   3851 O O   . GLY A 1 577 ? 157.098 147.644 202.669 1.00 164.78 ? 577 GLY A O   1 
ATOM   3852 N N   . GLU A 1 578 ? 157.221 147.956 204.901 1.00 167.78 ? 578 GLU A N   1 
ATOM   3853 C CA  . GLU A 1 578 ? 158.364 147.058 205.044 1.00 171.33 ? 578 GLU A CA  1 
ATOM   3854 C C   . GLU A 1 578 ? 158.006 145.638 204.625 1.00 168.25 ? 578 GLU A C   1 
ATOM   3855 O O   . GLU A 1 578 ? 158.796 144.961 203.956 1.00 164.02 ? 578 GLU A O   1 
ATOM   3856 C CB  . GLU A 1 578 ? 158.872 147.082 206.486 1.00 172.57 ? 578 GLU A CB  1 
ATOM   3857 C CG  . GLU A 1 578 ? 160.228 146.423 206.678 1.00 170.26 ? 578 GLU A CG  1 
ATOM   3858 C CD  . GLU A 1 578 ? 161.354 147.207 206.033 1.00 172.73 ? 578 GLU A CD  1 
ATOM   3859 O OE1 . GLU A 1 578 ? 161.340 148.452 206.122 1.00 173.04 ? 578 GLU A OE1 1 
ATOM   3860 O OE2 . GLU A 1 578 ? 162.253 146.577 205.437 1.00 172.76 ? 578 GLU A OE2 1 
ATOM   3861 N N   . ASN A 1 579 ? 156.821 145.172 205.007 1.00 167.18 ? 579 ASN A N   1 
ATOM   3862 C CA  . ASN A 1 579 ? 156.302 143.868 204.611 1.00 168.78 ? 579 ASN A CA  1 
ATOM   3863 C C   . ASN A 1 579 ? 154.925 144.034 203.983 1.00 169.51 ? 579 ASN A C   1 
ATOM   3864 O O   . ASN A 1 579 ? 153.963 143.340 204.322 1.00 168.93 ? 579 ASN A O   1 
ATOM   3865 C CB  . ASN A 1 579 ? 156.258 142.913 205.802 1.00 167.67 ? 579 ASN A CB  1 
ATOM   3866 C CG  . ASN A 1 579 ? 156.016 141.473 205.388 1.00 161.77 ? 579 ASN A CG  1 
ATOM   3867 O OD1 . ASN A 1 579 ? 156.018 141.147 204.201 1.00 162.19 ? 579 ASN A OD1 1 
ATOM   3868 N ND2 . ASN A 1 579 ? 155.806 140.603 206.369 1.00 150.90 ? 579 ASN A ND2 1 
ATOM   3869 N N   . ASN A 1 580 ? 154.825 144.985 203.051 1.00 171.44 ? 580 ASN A N   1 
ATOM   3870 C CA  . ASN A 1 580 ? 153.561 145.345 202.404 1.00 173.99 ? 580 ASN A CA  1 
ATOM   3871 C C   . ASN A 1 580 ? 152.511 145.754 203.435 1.00 173.82 ? 580 ASN A C   1 
ATOM   3872 O O   . ASN A 1 580 ? 151.333 145.409 203.322 1.00 172.89 ? 580 ASN A O   1 
ATOM   3873 C CB  . ASN A 1 580 ? 153.046 144.211 201.515 1.00 176.18 ? 580 ASN A CB  1 
ATOM   3874 C CG  . ASN A 1 580 ? 153.678 144.219 200.136 1.00 174.40 ? 580 ASN A CG  1 
ATOM   3875 O OD1 . ASN A 1 580 ? 154.887 144.407 199.997 1.00 172.89 ? 580 ASN A OD1 1 
ATOM   3876 N ND2 . ASN A 1 580 ? 152.862 144.016 199.109 1.00 167.55 ? 580 ASN A ND2 1 
ATOM   3877 N N   . THR A 1 581 ? 152.945 146.496 204.450 1.00 175.40 ? 581 THR A N   1 
ATOM   3878 C CA  . THR A 1 581 ? 152.045 146.968 205.491 1.00 175.40 ? 581 THR A CA  1 
ATOM   3879 C C   . THR A 1 581 ? 151.233 148.158 204.997 1.00 171.79 ? 581 THR A C   1 
ATOM   3880 O O   . THR A 1 581 ? 151.745 149.028 204.288 1.00 170.67 ? 581 THR A O   1 
ATOM   3881 C CB  . THR A 1 581 ? 152.832 147.360 206.742 1.00 170.99 ? 581 THR A CB  1 
ATOM   3882 O OG1 . THR A 1 581 ? 153.330 148.695 206.596 1.00 163.79 ? 581 THR A OG1 1 
ATOM   3883 C CG2 . THR A 1 581 ? 154.002 146.410 206.954 1.00 165.97 ? 581 THR A CG2 1 
ATOM   3884 N N   . LEU A 1 582 ? 149.959 148.193 205.381 1.00 167.51 ? 582 LEU A N   1 
ATOM   3885 C CA  . LEU A 1 582 ? 149.063 149.285 205.007 1.00 164.24 ? 582 LEU A CA  1 
ATOM   3886 C C   . LEU A 1 582 ? 149.407 150.502 205.856 1.00 161.04 ? 582 LEU A C   1 
ATOM   3887 O O   . LEU A 1 582 ? 149.063 150.569 207.038 1.00 158.74 ? 582 LEU A O   1 
ATOM   3888 C CB  . LEU A 1 582 ? 147.606 148.874 205.191 1.00 163.27 ? 582 LEU A CB  1 
ATOM   3889 C CG  . LEU A 1 582 ? 147.141 147.619 204.449 1.00 162.56 ? 582 LEU A CG  1 
ATOM   3890 C CD1 . LEU A 1 582 ? 145.628 147.483 204.523 1.00 158.41 ? 582 LEU A CD1 1 
ATOM   3891 C CD2 . LEU A 1 582 ? 147.610 147.639 203.002 1.00 167.34 ? 582 LEU A CD2 1 
ATOM   3892 N N   . VAL A 1 583 ? 150.121 151.452 205.244 1.00 162.55 ? 583 VAL A N   1 
ATOM   3893 C CA  . VAL A 1 583 ? 150.539 152.685 205.976 1.00 160.81 ? 583 VAL A CA  1 
ATOM   3894 C C   . VAL A 1 583 ? 149.310 153.587 206.156 1.00 154.35 ? 583 VAL A C   1 
ATOM   3895 O O   . VAL A 1 583 ? 148.858 154.174 205.151 1.00 154.04 ? 583 VAL A O   1 
ATOM   3896 C CB  . VAL A 1 583 ? 151.666 153.426 205.231 1.00 160.74 ? 583 VAL A CB  1 
ATOM   3897 C CG1 . VAL A 1 583 ? 152.229 154.579 206.052 1.00 152.47 ? 583 VAL A CG1 1 
ATOM   3898 C CG2 . VAL A 1 583 ? 152.776 152.477 204.794 1.00 164.52 ? 583 VAL A CG2 1 
ATOM   3899 N N   . TRP A 1 584 ? 148.799 153.686 207.385 1.00 151.94 ? 584 TRP A N   1 
ATOM   3900 C CA  . TRP A 1 584 ? 147.645 154.578 207.664 1.00 155.99 ? 584 TRP A CA  1 
ATOM   3901 C C   . TRP A 1 584 ? 148.057 156.028 207.401 1.00 157.45 ? 584 TRP A C   1 
ATOM   3902 O O   . TRP A 1 584 ? 147.179 156.837 207.024 1.00 158.00 ? 584 TRP A O   1 
ATOM   3903 C CB  . TRP A 1 584 ? 147.169 154.380 209.110 1.00 158.36 ? 584 TRP A CB  1 
ATOM   3904 C CG  . TRP A 1 584 ? 146.609 155.619 209.756 1.00 157.80 ? 584 TRP A CG  1 
ATOM   3905 C CD1 . TRP A 1 584 ? 147.208 156.393 210.706 1.00 154.13 ? 584 TRP A CD1 1 
ATOM   3906 C CD2 . TRP A 1 584 ? 145.322 156.222 209.501 1.00 156.43 ? 584 TRP A CD2 1 
ATOM   3907 N NE1 . TRP A 1 584 ? 146.392 157.435 211.055 1.00 149.44 ? 584 TRP A NE1 1 
ATOM   3908 C CE2 . TRP A 1 584 ? 145.229 157.356 210.335 1.00 150.11 ? 584 TRP A CE2 1 
ATOM   3909 C CE3 . TRP A 1 584 ? 144.251 155.917 208.655 1.00 151.49 ? 584 TRP A CE3 1 
ATOM   3910 C CZ2 . TRP A 1 584 ? 144.106 158.179 210.345 1.00 140.15 ? 584 TRP A CZ2 1 
ATOM   3911 C CZ3 . TRP A 1 584 ? 143.142 156.733 208.665 1.00 141.19 ? 584 TRP A CZ3 1 
ATOM   3912 C CH2 . TRP A 1 584 ? 143.072 157.847 209.500 1.00 136.21 ? 584 TRP A CH2 1 
ATOM   3913 N N   . LYS A 1 585 ? 149.347 156.337 207.575 1.00 153.67 ? 585 LYS A N   1 
ATOM   3914 C CA  . LYS A 1 585 ? 149.851 157.723 207.372 1.00 154.18 ? 585 LYS A CA  1 
ATOM   3915 C C   . LYS A 1 585 ? 149.132 158.654 208.363 1.00 153.63 ? 585 LYS A C   1 
ATOM   3916 O O   . LYS A 1 585 ? 149.283 158.440 209.585 1.00 152.92 ? 585 LYS A O   1 
ATOM   3917 C CB  . LYS A 1 585 ? 149.665 158.156 205.911 1.00 154.84 ? 585 LYS A CB  1 
ATOM   3918 C CG  . LYS A 1 585 ? 150.371 159.441 205.496 1.00 149.30 ? 585 LYS A CG  1 
ATOM   3919 C CD  . LYS A 1 585 ? 151.874 159.415 205.739 1.00 145.62 ? 585 LYS A CD  1 
ATOM   3920 C CE  . LYS A 1 585 ? 152.535 160.699 205.350 1.00 143.89 ? 585 LYS A CE  1 
ATOM   3921 N NZ  . LYS A 1 585 ? 153.992 160.615 205.478 1.00 145.79 ? 585 LYS A NZ  1 
ATOM   3922 N N   . TYR A 1 586 ? 148.392 159.645 207.859 1.00 154.11 ? 586 TYR A N   1 
ATOM   3923 C CA  . TYR A 1 586 ? 147.617 160.561 208.738 1.00 154.66 ? 586 TYR A CA  1 
ATOM   3924 C C   . TYR A 1 586 ? 146.141 160.446 208.378 1.00 150.01 ? 586 TYR A C   1 
ATOM   3925 O O   . TYR A 1 586 ? 145.788 159.613 207.515 1.00 149.21 ? 586 TYR A O   1 
ATOM   3926 C CB  . TYR A 1 586 ? 148.134 161.994 208.582 1.00 156.41 ? 586 TYR A CB  1 
ATOM   3927 C CG  . TYR A 1 586 ? 149.103 162.428 209.673 1.00 156.64 ? 586 TYR A CG  1 
ATOM   3928 C CD1 . TYR A 1 586 ? 150.309 161.766 209.865 1.00 155.08 ? 586 TYR A CD1 1 
ATOM   3929 C CD2 . TYR A 1 586 ? 148.808 163.496 210.511 1.00 152.23 ? 586 TYR A CD2 1 
ATOM   3930 C CE1 . TYR A 1 586 ? 151.194 162.155 210.857 1.00 153.36 ? 586 TYR A CE1 1 
ATOM   3931 C CE2 . TYR A 1 586 ? 149.685 163.894 211.506 1.00 152.19 ? 586 TYR A CE2 1 
ATOM   3932 C CZ  . TYR A 1 586 ? 150.881 163.222 211.679 1.00 156.62 ? 586 TYR A CZ  1 
ATOM   3933 O OH  . TYR A 1 586 ? 151.749 163.611 212.658 1.00 160.89 ? 586 TYR A OH  1 
ATOM   3934 N N   . ALA A 1 587 ? 145.295 161.257 209.019 1.00 146.73 ? 587 ALA A N   1 
ATOM   3935 C CA  . ALA A 1 587 ? 143.877 161.239 208.683 1.00 145.22 ? 587 ALA A CA  1 
ATOM   3936 C C   . ALA A 1 587 ? 143.623 161.921 207.343 1.00 144.09 ? 587 ALA A C   1 
ATOM   3937 O O   . ALA A 1 587 ? 142.727 161.527 206.596 1.00 145.27 ? 587 ALA A O   1 
ATOM   3938 C CB  . ALA A 1 587 ? 143.064 161.907 209.781 1.00 144.21 ? 587 ALA A CB  1 
ATOM   3939 N N   . ASP B 2 1   ? 154.312 138.606 126.082 1.00 77.17  ? 131 ASP D N   1 
ATOM   3940 C CA  . ASP B 2 1   ? 153.248 139.594 126.214 1.00 78.12  ? 131 ASP D CA  1 
ATOM   3941 C C   . ASP B 2 1   ? 151.885 138.920 126.319 1.00 78.36  ? 131 ASP D C   1 
ATOM   3942 O O   . ASP B 2 1   ? 151.791 137.730 126.617 1.00 79.29  ? 131 ASP D O   1 
ATOM   3943 C CB  . ASP B 2 1   ? 153.263 140.562 125.029 1.00 77.86  ? 131 ASP D CB  1 
ATOM   3944 C CG  . ASP B 2 1   ? 154.654 141.070 124.708 1.00 84.76  ? 131 ASP D CG  1 
ATOM   3945 O OD1 . ASP B 2 1   ? 155.588 140.788 125.489 1.00 82.71  ? 131 ASP D OD1 1 
ATOM   3946 O OD2 . ASP B 2 1   ? 154.814 141.753 123.674 1.00 89.38  ? 131 ASP D OD2 1 
ATOM   3947 N N   . ILE B 2 2   ? 150.831 139.692 126.072 1.00 74.41  ? 132 ILE D N   1 
ATOM   3948 C CA  . ILE B 2 2   ? 149.457 139.205 126.117 1.00 73.78  ? 132 ILE D CA  1 
ATOM   3949 C C   . ILE B 2 2   ? 148.880 139.341 124.716 1.00 74.36  ? 132 ILE D C   1 
ATOM   3950 O O   . ILE B 2 2   ? 148.857 140.442 124.153 1.00 73.59  ? 132 ILE D O   1 
ATOM   3951 C CB  . ILE B 2 2   ? 148.610 139.973 127.145 1.00 69.40  ? 132 ILE D CB  1 
ATOM   3952 C CG1 . ILE B 2 2   ? 148.757 139.354 128.536 1.00 75.27  ? 132 ILE D CG1 1 
ATOM   3953 C CG2 . ILE B 2 2   ? 147.146 139.983 126.741 1.00 67.85  ? 132 ILE D CG2 1 
ATOM   3954 C CD1 . ILE B 2 2   ? 150.095 139.608 129.195 1.00 75.50  ? 132 ILE D CD1 1 
ATOM   3955 N N   . VAL B 2 3   ? 148.424 138.227 124.150 1.00 76.55  ? 133 VAL D N   1 
ATOM   3956 C CA  . VAL B 2 3   ? 147.885 138.223 122.794 1.00 76.44  ? 133 VAL D CA  1 
ATOM   3957 C C   . VAL B 2 3   ? 146.474 138.799 122.846 1.00 72.46  ? 133 VAL D C   1 
ATOM   3958 O O   . VAL B 2 3   ? 145.547 138.153 123.340 1.00 70.85  ? 133 VAL D O   1 
ATOM   3959 C CB  . VAL B 2 3   ? 147.890 136.815 122.190 1.00 77.18  ? 133 VAL D CB  1 
ATOM   3960 C CG1 . VAL B 2 3   ? 147.635 136.881 120.691 1.00 72.27  ? 133 VAL D CG1 1 
ATOM   3961 C CG2 . VAL B 2 3   ? 149.210 136.118 122.485 1.00 76.81  ? 133 VAL D CG2 1 
ATOM   3962 N N   . MET B 2 4   ? 146.323 140.050 122.387 1.00 68.92  ? 134 MET D N   1 
ATOM   3963 C CA  . MET B 2 4   ? 145.016 140.759 122.410 1.00 68.55  ? 134 MET D CA  1 
ATOM   3964 C C   . MET B 2 4   ? 144.297 140.510 121.077 1.00 69.91  ? 134 MET D C   1 
ATOM   3965 O O   . MET B 2 4   ? 144.138 141.477 120.300 1.00 69.98  ? 134 MET D O   1 
ATOM   3966 C CB  . MET B 2 4   ? 145.227 142.262 122.624 1.00 62.67  ? 134 MET D CB  1 
ATOM   3967 C CG  . MET B 2 4   ? 145.791 142.614 123.986 1.00 59.71  ? 134 MET D CG  1 
ATOM   3968 S SD  . MET B 2 4   ? 144.573 142.418 125.301 1.00 62.96  ? 134 MET D SD  1 
ATOM   3969 C CE  . MET B 2 4   ? 143.480 143.809 124.971 1.00 53.82  ? 134 MET D CE  1 
ATOM   3970 N N   . THR B 2 5   ? 143.878 139.270 120.816 1.00 74.29  ? 135 THR D N   1 
ATOM   3971 C CA  . THR B 2 5   ? 143.215 138.917 119.568 1.00 75.93  ? 135 THR D CA  1 
ATOM   3972 C C   . THR B 2 5   ? 141.855 139.597 119.468 1.00 75.99  ? 135 THR D C   1 
ATOM   3973 O O   . THR B 2 5   ? 141.110 139.681 120.447 1.00 75.76  ? 135 THR D O   1 
ATOM   3974 C CB  . THR B 2 5   ? 143.050 137.401 119.466 1.00 77.84  ? 135 THR D CB  1 
ATOM   3975 O OG1 . THR B 2 5   ? 144.290 136.761 119.794 1.00 81.21  ? 135 THR D OG1 1 
ATOM   3976 C CG2 . THR B 2 5   ? 142.641 137.000 118.056 1.00 73.88  ? 135 THR D CG2 1 
ATOM   3977 N N   . GLN B 2 6   ? 141.545 140.127 118.276 1.00 76.94  ? 136 GLN D N   1 
ATOM   3978 C CA  . GLN B 2 6   ? 140.253 140.819 118.027 1.00 76.65  ? 136 GLN D CA  1 
ATOM   3979 C C   . GLN B 2 6   ? 139.387 139.927 117.130 1.00 79.11  ? 136 GLN D C   1 
ATOM   3980 O O   . GLN B 2 6   ? 139.894 139.484 116.077 1.00 79.52  ? 136 GLN D O   1 
ATOM   3981 C CB  . GLN B 2 6   ? 140.455 142.186 117.373 1.00 72.50  ? 136 GLN D CB  1 
ATOM   3982 C CG  . GLN B 2 6   ? 141.602 142.988 117.977 1.00 70.22  ? 136 GLN D CG  1 
ATOM   3983 C CD  . GLN B 2 6   ? 141.429 144.485 117.848 1.00 65.25  ? 136 GLN D CD  1 
ATOM   3984 O OE1 . GLN B 2 6   ? 142.244 145.178 117.230 1.00 60.81  ? 136 GLN D OE1 1 
ATOM   3985 N NE2 . GLN B 2 6   ? 140.367 145.007 118.445 1.00 65.24  ? 136 GLN D NE2 1 
ATOM   3986 N N   . SER B 2 7   ? 138.138 139.669 117.525 1.00 77.87  ? 137 SER D N   1 
ATOM   3987 C CA  . SER B 2 7   ? 137.235 138.821 116.750 1.00 76.69  ? 137 SER D CA  1 
ATOM   3988 C C   . SER B 2 7   ? 137.059 139.313 115.318 1.00 76.73  ? 137 SER D C   1 
ATOM   3989 O O   . SER B 2 7   ? 137.162 138.489 114.392 1.00 79.33  ? 137 SER D O   1 
ATOM   3990 C CB  . SER B 2 7   ? 135.892 138.688 117.478 1.00 78.50  ? 137 SER D CB  1 
ATOM   3991 O OG  . SER B 2 7   ? 136.080 138.377 118.847 1.00 79.68  ? 137 SER D OG  1 
ATOM   3992 N N   . PRO B 2 8   ? 136.782 140.613 115.059 1.00 75.45  ? 138 PRO D N   1 
ATOM   3993 C CA  . PRO B 2 8   ? 136.717 141.121 113.698 1.00 76.99  ? 138 PRO D CA  1 
ATOM   3994 C C   . PRO B 2 8   ? 138.049 141.728 113.300 1.00 78.82  ? 138 PRO D C   1 
ATOM   3995 O O   . PRO B 2 8   ? 138.799 142.164 114.198 1.00 79.70  ? 138 PRO D O   1 
ATOM   3996 C CB  . PRO B 2 8   ? 135.596 142.160 113.772 1.00 76.67  ? 138 PRO D CB  1 
ATOM   3997 C CG  . PRO B 2 8   ? 135.636 142.649 115.202 1.00 76.41  ? 138 PRO D CG  1 
ATOM   3998 C CD  . PRO B 2 8   ? 136.473 141.665 116.015 1.00 77.24  ? 138 PRO D CD  1 
ATOM   3999 N N   . LEU B 2 9   ? 138.358 141.735 112.002 1.00 79.51  ? 139 LEU D N   1 
ATOM   4000 C CA  . LEU B 2 9   ? 139.607 142.353 111.487 1.00 80.90  ? 139 LEU D CA  1 
ATOM   4001 C C   . LEU B 2 9   ? 139.252 143.145 110.223 1.00 85.27  ? 139 LEU D C   1 
ATOM   4002 O O   . LEU B 2 9   ? 138.603 142.557 109.331 1.00 87.37  ? 139 LEU D O   1 
ATOM   4003 C CB  . LEU B 2 9   ? 140.667 141.289 111.210 1.00 85.46  ? 139 LEU D CB  1 
ATOM   4004 C CG  . LEU B 2 9   ? 142.026 141.803 110.725 1.00 85.95  ? 139 LEU D CG  1 
ATOM   4005 C CD1 . LEU B 2 9   ? 142.507 142.992 111.534 1.00 81.24  ? 139 LEU D CD1 1 
ATOM   4006 C CD2 . LEU B 2 9   ? 143.051 140.689 110.770 1.00 83.75  ? 139 LEU D CD2 1 
ATOM   4007 N N   . SER B 2 10  ? 139.645 144.418 110.147 1.00 86.31  ? 140 SER D N   1 
ATOM   4008 C CA  . SER B 2 10  ? 139.298 145.286 108.991 1.00 88.79  ? 140 SER D CA  1 
ATOM   4009 C C   . SER B 2 10  ? 137.798 145.146 108.701 1.00 91.22  ? 140 SER D C   1 
ATOM   4010 O O   . SER B 2 10  ? 137.437 144.971 107.517 1.00 92.71  ? 140 SER D O   1 
ATOM   4011 C CB  . SER B 2 10  ? 140.136 144.958 107.782 1.00 87.10  ? 140 SER D CB  1 
ATOM   4012 O OG  . SER B 2 10  ? 141.517 145.129 108.065 1.00 84.59  ? 140 SER D OG  1 
ATOM   4013 N N   . LEU B 2 11  ? 136.965 145.213 109.743 1.00 91.41  ? 141 LEU D N   1 
ATOM   4014 C CA  . LEU B 2 11  ? 135.499 145.039 109.578 1.00 95.33  ? 141 LEU D CA  1 
ATOM   4015 C C   . LEU B 2 11  ? 134.892 146.296 108.942 1.00 101.72 ? 141 LEU D C   1 
ATOM   4016 O O   . LEU B 2 11  ? 135.029 147.383 109.544 1.00 99.30  ? 141 LEU D O   1 
ATOM   4017 C CB  . LEU B 2 11  ? 134.899 144.768 110.956 1.00 91.16  ? 141 LEU D CB  1 
ATOM   4018 C CG  . LEU B 2 11  ? 133.372 144.839 111.052 1.00 95.91  ? 141 LEU D CG  1 
ATOM   4019 C CD1 . LEU B 2 11  ? 132.718 143.720 110.262 1.00 96.33  ? 141 LEU D CD1 1 
ATOM   4020 C CD2 . LEU B 2 11  ? 132.921 144.812 112.502 1.00 92.22  ? 141 LEU D CD2 1 
ATOM   4021 N N   . PRO B 2 12  ? 134.228 146.214 107.767 1.00 107.25 ? 142 PRO D N   1 
ATOM   4022 C CA  . PRO B 2 12  ? 133.551 147.383 107.193 1.00 106.14 ? 142 PRO D CA  1 
ATOM   4023 C C   . PRO B 2 12  ? 132.131 147.528 107.716 1.00 107.48 ? 142 PRO D C   1 
ATOM   4024 O O   . PRO B 2 12  ? 131.384 146.547 107.778 1.00 104.94 ? 142 PRO D O   1 
ATOM   4025 C CB  . PRO B 2 12  ? 133.577 147.091 105.689 1.00 107.53 ? 142 PRO D CB  1 
ATOM   4026 C CG  . PRO B 2 12  ? 133.600 145.583 105.594 1.00 110.33 ? 142 PRO D CG  1 
ATOM   4027 C CD  . PRO B 2 12  ? 134.083 145.020 106.917 1.00 108.09 ? 142 PRO D CD  1 
ATOM   4028 N N   . VAL B 2 13  ? 131.747 148.744 108.099 1.00 108.41 ? 143 VAL D N   1 
ATOM   4029 C CA  . VAL B 2 13  ? 130.425 149.014 108.651 1.00 112.51 ? 143 VAL D CA  1 
ATOM   4030 C C   . VAL B 2 13  ? 129.784 150.151 107.868 1.00 112.37 ? 143 VAL D C   1 
ATOM   4031 O O   . VAL B 2 13  ? 130.402 151.203 107.673 1.00 111.37 ? 143 VAL D O   1 
ATOM   4032 C CB  . VAL B 2 13  ? 130.483 149.365 110.151 1.00 110.87 ? 143 VAL D CB  1 
ATOM   4033 C CG1 . VAL B 2 13  ? 129.105 149.227 110.776 1.00 110.38 ? 143 VAL D CG1 1 
ATOM   4034 C CG2 . VAL B 2 13  ? 131.480 148.474 110.871 1.00 104.93 ? 143 VAL D CG2 1 
ATOM   4035 N N   . THR B 2 14  ? 128.551 149.934 107.420 1.00 112.17 ? 144 THR D N   1 
ATOM   4036 C CA  . THR B 2 14  ? 127.780 150.995 106.797 1.00 114.34 ? 144 THR D CA  1 
ATOM   4037 C C   . THR B 2 14  ? 127.336 152.008 107.854 1.00 115.69 ? 144 THR D C   1 
ATOM   4038 O O   . THR B 2 14  ? 127.117 151.648 109.014 1.00 113.54 ? 144 THR D O   1 
ATOM   4039 C CB  . THR B 2 14  ? 126.563 150.416 106.077 1.00 113.96 ? 144 THR D CB  1 
ATOM   4040 O OG1 . THR B 2 14  ? 125.658 151.468 105.722 1.00 111.22 ? 144 THR D OG1 1 
ATOM   4041 C CG2 . THR B 2 14  ? 125.847 149.409 106.963 1.00 112.13 ? 144 THR D CG2 1 
ATOM   4042 N N   . PRO B 2 15  ? 127.209 153.283 107.482 1.00 115.55 ? 145 PRO D N   1 
ATOM   4043 C CA  . PRO B 2 15  ? 126.819 154.301 108.465 1.00 112.77 ? 145 PRO D CA  1 
ATOM   4044 C C   . PRO B 2 15  ? 125.450 154.021 109.068 1.00 111.51 ? 145 PRO D C   1 
ATOM   4045 O O   . PRO B 2 15  ? 124.563 153.456 108.424 1.00 110.98 ? 145 PRO D O   1 
ATOM   4046 C CB  . PRO B 2 15  ? 126.813 155.599 107.649 1.00 109.68 ? 145 PRO D CB  1 
ATOM   4047 C CG  . PRO B 2 15  ? 127.746 155.337 106.520 1.00 108.92 ? 145 PRO D CG  1 
ATOM   4048 C CD  . PRO B 2 15  ? 127.592 153.881 106.191 1.00 111.86 ? 145 PRO D CD  1 
ATOM   4049 N N   . GLY B 2 16  ? 125.289 154.430 110.322 1.00 109.77 ? 146 GLY D N   1 
ATOM   4050 C CA  . GLY B 2 16  ? 124.047 154.217 111.044 1.00 108.48 ? 146 GLY D CA  1 
ATOM   4051 C C   . GLY B 2 16  ? 123.729 152.769 111.349 1.00 107.76 ? 146 GLY D C   1 
ATOM   4052 O O   . GLY B 2 16  ? 122.576 152.346 111.192 1.00 107.37 ? 146 GLY D O   1 
ATOM   4053 N N   . GLU B 2 17  ? 124.721 151.996 111.781 1.00 108.47 ? 147 GLU D N   1 
ATOM   4054 C CA  . GLU B 2 17  ? 124.529 150.600 112.136 1.00 108.34 ? 147 GLU D CA  1 
ATOM   4055 C C   . GLU B 2 17  ? 125.274 150.297 113.427 1.00 104.19 ? 147 GLU D C   1 
ATOM   4056 O O   . GLU B 2 17  ? 126.298 150.925 113.718 1.00 102.70 ? 147 GLU D O   1 
ATOM   4057 C CB  . GLU B 2 17  ? 125.020 149.662 111.021 1.00 110.05 ? 147 GLU D CB  1 
ATOM   4058 C CG  . GLU B 2 17  ? 123.936 149.266 110.031 1.00 111.17 ? 147 GLU D CG  1 
ATOM   4059 C CD  . GLU B 2 17  ? 123.289 147.939 110.374 1.00 109.74 ? 147 GLU D CD  1 
ATOM   4060 O OE1 . GLU B 2 17  ? 123.908 147.148 111.116 1.00 108.86 ? 147 GLU D OE1 1 
ATOM   4061 O OE2 . GLU B 2 17  ? 122.160 147.688 109.902 1.00 109.04 ? 147 GLU D OE2 1 
ATOM   4062 N N   . PRO B 2 18  ? 124.783 149.340 114.221 1.00 102.59 ? 148 PRO D N   1 
ATOM   4063 C CA  . PRO B 2 18  ? 125.450 148.985 115.494 1.00 99.74  ? 148 PRO D CA  1 
ATOM   4064 C C   . PRO B 2 18  ? 126.699 148.124 115.307 1.00 98.85  ? 148 PRO D C   1 
ATOM   4065 O O   . PRO B 2 18  ? 126.690 146.897 115.404 1.00 97.82  ? 148 PRO D O   1 
ATOM   4066 C CB  . PRO B 2 18  ? 124.350 148.238 116.251 1.00 99.97  ? 148 PRO D CB  1 
ATOM   4067 C CG  . PRO B 2 18  ? 123.514 147.630 115.181 1.00 100.53 ? 148 PRO D CG  1 
ATOM   4068 C CD  . PRO B 2 18  ? 123.516 148.609 114.039 1.00 102.91 ? 148 PRO D CD  1 
ATOM   4069 N N   . ALA B 2 19  ? 127.815 148.792 115.024 1.00 99.24  ? 149 ALA D N   1 
ATOM   4070 C CA  . ALA B 2 19  ? 129.087 148.099 114.877 1.00 98.96  ? 149 ALA D CA  1 
ATOM   4071 C C   . ALA B 2 19  ? 129.542 147.525 116.213 1.00 92.56  ? 149 ALA D C   1 
ATOM   4072 O O   . ALA B 2 19  ? 129.351 148.136 117.267 1.00 91.30  ? 149 ALA D O   1 
ATOM   4073 C CB  . ALA B 2 19  ? 130.150 149.048 114.325 1.00 95.94  ? 149 ALA D CB  1 
ATOM   4074 N N   . SER B 2 20  ? 130.146 146.340 116.164 1.00 89.31  ? 150 SER D N   1 
ATOM   4075 C CA  . SER B 2 20  ? 130.629 145.667 117.365 1.00 87.19  ? 150 SER D CA  1 
ATOM   4076 C C   . SER B 2 20  ? 131.957 144.996 117.057 1.00 87.27  ? 150 SER D C   1 
ATOM   4077 O O   . SER B 2 20  ? 132.027 144.133 116.178 1.00 87.66  ? 150 SER D O   1 
ATOM   4078 C CB  . SER B 2 20  ? 129.613 144.639 117.870 1.00 87.46  ? 150 SER D CB  1 
ATOM   4079 O OG  . SER B 2 20  ? 130.045 144.052 119.085 1.00 83.39  ? 150 SER D OG  1 
ATOM   4080 N N   . ILE B 2 21  ? 133.001 145.390 117.781 1.00 82.39  ? 151 ILE D N   1 
ATOM   4081 C CA  . ILE B 2 21  ? 134.325 144.791 117.665 1.00 76.53  ? 151 ILE D CA  1 
ATOM   4082 C C   . ILE B 2 21  ? 134.648 144.127 118.993 1.00 73.54  ? 151 ILE D C   1 
ATOM   4083 O O   . ILE B 2 21  ? 134.671 144.793 120.035 1.00 72.53  ? 151 ILE D O   1 
ATOM   4084 C CB  . ILE B 2 21  ? 135.397 145.829 117.299 1.00 72.34  ? 151 ILE D CB  1 
ATOM   4085 C CG1 . ILE B 2 21  ? 135.142 146.391 115.901 1.00 73.97  ? 151 ILE D CG1 1 
ATOM   4086 C CG2 . ILE B 2 21  ? 136.780 145.213 117.380 1.00 69.21  ? 151 ILE D CG2 1 
ATOM   4087 C CD1 . ILE B 2 21  ? 134.999 147.891 115.869 1.00 73.19  ? 151 ILE D CD1 1 
ATOM   4088 N N   . SER B 2 22  ? 134.899 142.823 118.958 1.00 76.28  ? 152 SER D N   1 
ATOM   4089 C CA  . SER B 2 22  ? 135.187 142.042 120.152 1.00 78.10  ? 152 SER D CA  1 
ATOM   4090 C C   . SER B 2 22  ? 136.659 141.661 120.163 1.00 78.22  ? 152 SER D C   1 
ATOM   4091 O O   . SER B 2 22  ? 137.177 141.139 119.170 1.00 80.33  ? 152 SER D O   1 
ATOM   4092 C CB  . SER B 2 22  ? 134.313 140.788 120.211 1.00 81.51  ? 152 SER D CB  1 
ATOM   4093 O OG  . SER B 2 22  ? 135.007 139.712 120.819 1.00 80.42  ? 152 SER D OG  1 
ATOM   4094 N N   . CYS B 2 23  ? 137.329 141.924 121.281 1.00 76.24  ? 153 CYS D N   1 
ATOM   4095 C CA  . CYS B 2 23  ? 138.745 141.627 121.438 1.00 76.22  ? 153 CYS D CA  1 
ATOM   4096 C C   . CYS B 2 23  ? 138.943 140.732 122.651 1.00 78.30  ? 153 CYS D C   1 
ATOM   4097 O O   . CYS B 2 23  ? 138.391 141.002 123.722 1.00 78.34  ? 153 CYS D O   1 
ATOM   4098 C CB  . CYS B 2 23  ? 139.566 142.909 121.585 1.00 73.44  ? 153 CYS D CB  1 
ATOM   4099 S SG  . CYS B 2 23  ? 141.348 142.633 121.575 1.00 82.13  ? 153 CYS D SG  1 
ATOM   4100 N N   . ARG B 2 24  ? 139.749 139.678 122.500 1.00 78.19  ? 154 ARG D N   1 
ATOM   4101 C CA  . ARG B 2 24  ? 139.992 138.736 123.624 1.00 77.10  ? 154 ARG D CA  1 
ATOM   4102 C C   . ARG B 2 24  ? 141.486 138.731 123.978 1.00 75.49  ? 154 ARG D C   1 
ATOM   4103 O O   . ARG B 2 24  ? 142.314 138.866 123.054 1.00 76.78  ? 154 ARG D O   1 
ATOM   4104 C CB  . ARG B 2 24  ? 139.503 137.330 123.261 1.00 77.75  ? 154 ARG D CB  1 
ATOM   4105 C CG  . ARG B 2 24  ? 138.008 137.294 122.979 1.00 80.66  ? 154 ARG D CG  1 
ATOM   4106 C CD  . ARG B 2 24  ? 137.648 136.194 121.993 1.00 82.02  ? 154 ARG D CD  1 
ATOM   4107 N NE  . ARG B 2 24  ? 138.549 136.116 120.836 1.00 81.84  ? 154 ARG D NE  1 
ATOM   4108 C CZ  . ARG B 2 24  ? 138.750 137.060 119.922 1.00 81.71  ? 154 ARG D CZ  1 
ATOM   4109 N NH1 . ARG B 2 24  ? 138.320 138.293 120.120 1.00 81.34  ? 154 ARG D NH1 1 
ATOM   4110 N NH2 . ARG B 2 24  ? 139.388 136.763 118.805 1.00 81.14  ? 154 ARG D NH2 1 
ATOM   4111 N N   . SER B 2 25  ? 141.809 138.571 125.263 1.00 73.62  ? 155 SER D N   1 
ATOM   4112 C CA  . SER B 2 25  ? 143.225 138.596 125.709 1.00 73.45  ? 155 SER D CA  1 
ATOM   4113 C C   . SER B 2 25  ? 143.715 137.172 126.001 1.00 73.69  ? 155 SER D C   1 
ATOM   4114 O O   . SER B 2 25  ? 142.898 136.355 126.476 1.00 76.44  ? 155 SER D O   1 
ATOM   4115 C CB  . SER B 2 25  ? 143.375 139.459 126.923 1.00 74.83  ? 155 SER D CB  1 
ATOM   4116 O OG  . SER B 2 25  ? 142.523 139.001 127.964 1.00 77.59  ? 155 SER D OG  1 
ATOM   4117 N N   . SER B 2 26  ? 144.995 136.892 125.738 1.00 73.21  ? 156 SER D N   1 
ATOM   4118 C CA  . SER B 2 26  ? 145.551 135.556 126.078 1.00 78.04  ? 156 SER D CA  1 
ATOM   4119 C C   . SER B 2 26  ? 145.433 135.323 127.590 1.00 80.52  ? 156 SER D C   1 
ATOM   4120 O O   . SER B 2 26  ? 145.127 134.180 127.990 1.00 80.19  ? 156 SER D O   1 
ATOM   4121 C CB  . SER B 2 26  ? 146.978 135.430 125.622 1.00 78.91  ? 156 SER D CB  1 
ATOM   4122 O OG  . SER B 2 26  ? 147.811 136.351 126.312 1.00 78.22  ? 156 SER D OG  1 
ATOM   4123 N N   . GLN B 2 27  ? 145.667 136.367 128.390 1.00 81.03  ? 157 GLN D N   1 
ATOM   4124 C CA  . GLN B 2 27  ? 145.595 136.238 129.870 1.00 80.96  ? 157 GLN D CA  1 
ATOM   4125 C C   . GLN B 2 27  ? 144.477 137.145 130.406 1.00 82.74  ? 157 GLN D C   1 
ATOM   4126 O O   . GLN B 2 27  ? 144.096 138.098 129.695 1.00 83.08  ? 157 GLN D O   1 
ATOM   4127 C CB  . GLN B 2 27  ? 146.948 136.586 130.489 1.00 78.54  ? 157 GLN D CB  1 
ATOM   4128 C CG  . GLN B 2 27  ? 148.068 135.626 130.101 1.00 74.25  ? 157 GLN D CG  1 
ATOM   4129 C CD  . GLN B 2 27  ? 149.437 136.097 130.539 1.00 77.55  ? 157 GLN D CD  1 
ATOM   4130 O OE1 . GLN B 2 27  ? 149.684 136.347 131.724 1.00 81.03  ? 157 GLN D OE1 1 
ATOM   4131 N NE2 . GLN B 2 27  ? 150.340 136.231 129.580 1.00 78.15  ? 157 GLN D NE2 1 
ATOM   4132 N N   . ASN B 2 28  ? 143.977 136.857 131.611 1.00 81.79  ? 158 ASN D N   1 
ATOM   4133 C CA  . ASN B 2 28  ? 142.864 137.652 132.200 1.00 81.29  ? 158 ASN D CA  1 
ATOM   4134 C C   . ASN B 2 28  ? 143.326 139.093 132.435 1.00 84.72  ? 158 ASN D C   1 
ATOM   4135 O O   . ASN B 2 28  ? 144.307 139.285 133.185 1.00 83.71  ? 158 ASN D O   1 
ATOM   4136 C CB  . ASN B 2 28  ? 142.350 137.017 133.487 1.00 80.56  ? 158 ASN D CB  1 
ATOM   4137 C CG  . ASN B 2 28  ? 141.140 137.726 134.049 1.00 83.14  ? 158 ASN D CG  1 
ATOM   4138 O OD1 . ASN B 2 28  ? 140.645 138.691 133.457 1.00 82.81  ? 158 ASN D OD1 1 
ATOM   4139 N ND2 . ASN B 2 28  ? 140.645 137.262 135.187 1.00 81.24  ? 158 ASN D ND2 1 
ATOM   4140 N N   . ILE B 2 29  ? 142.641 140.065 131.825 1.00 86.06  ? 159 ILE D N   1 
ATOM   4141 C CA  . ILE B 2 29  ? 142.969 141.484 132.047 1.00 82.32  ? 159 ILE D CA  1 
ATOM   4142 C C   . ILE B 2 29  ? 142.295 141.875 133.356 1.00 82.51  ? 159 ILE D C   1 
ATOM   4143 O O   . ILE B 2 29  ? 141.219 142.474 133.398 1.00 79.88  ? 159 ILE D O   1 
ATOM   4144 C CB  . ILE B 2 29  ? 142.542 142.369 130.874 1.00 73.60  ? 159 ILE D CB  1 
ATOM   4145 C CG1 . ILE B 2 29  ? 143.048 141.791 129.555 1.00 71.06  ? 159 ILE D CG1 1 
ATOM   4146 C CG2 . ILE B 2 29  ? 143.054 143.784 131.057 1.00 65.81  ? 159 ILE D CG2 1 
ATOM   4147 C CD1 . ILE B 2 29  ? 142.579 142.563 128.352 1.00 65.67  ? 159 ILE D CD1 1 
ATOM   4148 N N   . VAL B 2 30  ? 142.960 141.538 134.459 1.00 84.35  ? 160 VAL D N   1 
ATOM   4149 C CA  . VAL B 2 30  ? 142.515 141.909 135.796 1.00 86.03  ? 160 VAL D CA  1 
ATOM   4150 C C   . VAL B 2 30  ? 143.756 142.173 136.637 1.00 90.26  ? 160 VAL D C   1 
ATOM   4151 O O   . VAL B 2 30  ? 144.613 141.295 136.790 1.00 85.43  ? 160 VAL D O   1 
ATOM   4152 C CB  . VAL B 2 30  ? 141.629 140.819 136.430 1.00 83.29  ? 160 VAL D CB  1 
ATOM   4153 C CG1 . VAL B 2 30  ? 141.664 140.919 137.949 1.00 84.91  ? 160 VAL D CG1 1 
ATOM   4154 C CG2 . VAL B 2 30  ? 140.197 140.928 135.928 1.00 77.21  ? 160 VAL D CG2 1 
ATOM   4155 N N   . HIS B 2 31  ? 143.869 143.382 137.174 1.00 92.43  ? 161 HIS D N   1 
ATOM   4156 C CA  . HIS B 2 31  ? 145.030 143.770 137.959 1.00 91.04  ? 161 HIS D CA  1 
ATOM   4157 C C   . HIS B 2 31  ? 144.752 143.567 139.446 1.00 92.68  ? 161 HIS D C   1 
ATOM   4158 O O   . HIS B 2 31  ? 143.618 143.335 139.870 1.00 91.68  ? 161 HIS D O   1 
ATOM   4159 C CB  . HIS B 2 31  ? 145.413 145.226 137.666 1.00 85.07  ? 161 HIS D CB  1 
ATOM   4160 C CG  . HIS B 2 31  ? 146.725 145.637 138.257 1.00 86.08  ? 161 HIS D CG  1 
ATOM   4161 N ND1 . HIS B 2 31  ? 146.823 146.328 139.445 1.00 89.21  ? 161 HIS D ND1 1 
ATOM   4162 C CD2 . HIS B 2 31  ? 147.994 145.442 137.829 1.00 83.87  ? 161 HIS D CD2 1 
ATOM   4163 C CE1 . HIS B 2 31  ? 148.096 146.546 139.721 1.00 88.91  ? 161 HIS D CE1 1 
ATOM   4164 N NE2 . HIS B 2 31  ? 148.828 146.019 138.756 1.00 86.49  ? 161 HIS D NE2 1 
ATOM   4165 N N   . ASN B 2 32  ? 145.823 143.651 140.240 1.00 92.20  ? 162 ASN D N   1 
ATOM   4166 C CA  . ASN B 2 32  ? 145.706 143.448 141.680 1.00 93.74  ? 162 ASN D CA  1 
ATOM   4167 C C   . ASN B 2 32  ? 144.780 144.479 142.315 1.00 95.00  ? 162 ASN D C   1 
ATOM   4168 O O   . ASN B 2 32  ? 143.998 144.150 143.215 1.00 94.25  ? 162 ASN D O   1 
ATOM   4169 C CB  . ASN B 2 32  ? 147.091 143.500 142.325 1.00 91.97  ? 162 ASN D CB  1 
ATOM   4170 C CG  . ASN B 2 32  ? 147.048 143.271 143.821 1.00 94.80  ? 162 ASN D CG  1 
ATOM   4171 O OD1 . ASN B 2 32  ? 146.150 142.605 144.335 1.00 97.55  ? 162 ASN D OD1 1 
ATOM   4172 N ND2 . ASN B 2 32  ? 148.023 143.825 144.531 1.00 92.89  ? 162 ASN D ND2 1 
ATOM   4173 N N   . ASN B 2 33  ? 144.849 145.732 141.860 1.00 93.83  ? 163 ASN D N   1 
ATOM   4174 C CA  . ASN B 2 33  ? 143.975 146.765 142.403 1.00 89.59  ? 163 ASN D CA  1 
ATOM   4175 C C   . ASN B 2 33  ? 142.522 146.591 141.979 1.00 90.52  ? 163 ASN D C   1 
ATOM   4176 O O   . ASN B 2 33  ? 141.653 147.293 142.508 1.00 92.34  ? 163 ASN D O   1 
ATOM   4177 C CB  . ASN B 2 33  ? 144.479 148.155 142.003 1.00 85.78  ? 163 ASN D CB  1 
ATOM   4178 C CG  . ASN B 2 33  ? 144.643 148.311 140.505 1.00 84.42  ? 163 ASN D CG  1 
ATOM   4179 O OD1 . ASN B 2 33  ? 144.344 147.399 139.736 1.00 86.10  ? 163 ASN D OD1 1 
ATOM   4180 N ND2 . ASN B 2 33  ? 145.123 149.474 140.084 1.00 81.32  ? 163 ASN D ND2 1 
ATOM   4181 N N   . GLY B 2 34  ? 142.237 145.684 141.044 1.00 88.42  ? 164 GLY D N   1 
ATOM   4182 C CA  . GLY B 2 34  ? 140.878 145.334 140.697 1.00 86.61  ? 164 GLY D CA  1 
ATOM   4183 C C   . GLY B 2 34  ? 140.276 146.091 139.534 1.00 88.99  ? 164 GLY D C   1 
ATOM   4184 O O   . GLY B 2 34  ? 139.159 145.758 139.115 1.00 91.01  ? 164 GLY D O   1 
ATOM   4185 N N   . ILE B 2 35  ? 141.019 147.059 138.986 1.00 88.74  ? 165 ILE D N   1 
ATOM   4186 C CA  . ILE B 2 35  ? 140.527 147.839 137.806 1.00 82.68  ? 165 ILE D CA  1 
ATOM   4187 C C   . ILE B 2 35  ? 141.080 147.213 136.514 1.00 76.66  ? 165 ILE D C   1 
ATOM   4188 O O   . ILE B 2 35  ? 142.309 146.997 136.436 1.00 73.09  ? 165 ILE D O   1 
ATOM   4189 C CB  . ILE B 2 35  ? 140.893 149.331 137.931 1.00 79.73  ? 165 ILE D CB  1 
ATOM   4190 C CG1 . ILE B 2 35  ? 140.577 150.102 136.651 1.00 67.91  ? 165 ILE D CG1 1 
ATOM   4191 C CG2 . ILE B 2 35  ? 142.353 149.513 138.343 1.00 75.80  ? 165 ILE D CG2 1 
ATOM   4192 C CD1 . ILE B 2 35  ? 140.999 151.559 136.698 1.00 61.27  ? 165 ILE D CD1 1 
ATOM   4193 N N   . THR B 2 36  ? 140.217 146.915 135.536 1.00 74.71  ? 166 THR D N   1 
ATOM   4194 C CA  . THR B 2 36  ? 140.627 146.292 134.251 1.00 72.88  ? 166 THR D CA  1 
ATOM   4195 C C   . THR B 2 36  ? 141.086 147.396 133.319 1.00 65.85  ? 166 THR D C   1 
ATOM   4196 O O   . THR B 2 36  ? 140.242 148.233 132.948 1.00 61.38  ? 166 THR D O   1 
ATOM   4197 C CB  . THR B 2 36  ? 139.503 145.443 133.646 1.00 69.08  ? 166 THR D CB  1 
ATOM   4198 O OG1 . THR B 2 36  ? 139.914 145.192 132.304 1.00 66.34  ? 166 THR D OG1 1 
ATOM   4199 C CG2 . THR B 2 36  ? 138.137 146.109 133.633 1.00 62.96  ? 166 THR D CG2 1 
ATOM   4200 N N   . TYR B 2 37  ? 142.369 147.412 132.943 1.00 64.36  ? 167 TYR D N   1 
ATOM   4201 C CA  . TYR B 2 37  ? 142.944 148.493 132.095 1.00 54.63  ? 167 TYR D CA  1 
ATOM   4202 C C   . TYR B 2 37  ? 142.772 148.126 130.627 1.00 52.05  ? 167 TYR D C   1 
ATOM   4203 O O   . TYR B 2 37  ? 143.752 147.683 129.996 1.00 56.16  ? 167 TYR D O   1 
ATOM   4204 C CB  . TYR B 2 37  ? 144.414 148.747 132.437 1.00 49.54  ? 167 TYR D CB  1 
ATOM   4205 C CG  . TYR B 2 37  ? 144.641 149.546 133.713 1.00 50.06  ? 167 TYR D CG  1 
ATOM   4206 C CD1 . TYR B 2 37  ? 144.595 150.935 133.703 1.00 49.00  ? 167 TYR D CD1 1 
ATOM   4207 C CD2 . TYR B 2 37  ? 144.920 148.915 134.918 1.00 56.35  ? 167 TYR D CD2 1 
ATOM   4208 C CE1 . TYR B 2 37  ? 144.801 151.671 134.857 1.00 49.55  ? 167 TYR D CE1 1 
ATOM   4209 C CE2 . TYR B 2 37  ? 145.133 149.640 136.078 1.00 54.25  ? 167 TYR D CE2 1 
ATOM   4210 C CZ  . TYR B 2 37  ? 145.072 151.022 136.048 1.00 51.82  ? 167 TYR D CZ  1 
ATOM   4211 O OH  . TYR B 2 37  ? 145.277 151.745 137.186 1.00 54.20  ? 167 TYR D OH  1 
ATOM   4212 N N   . LEU B 2 38  ? 141.552 148.276 130.100 1.00 45.47  ? 168 LEU D N   1 
ATOM   4213 C CA  . LEU B 2 38  ? 141.262 148.001 128.670 1.00 42.09  ? 168 LEU D CA  1 
ATOM   4214 C C   . LEU B 2 38  ? 140.832 149.322 128.021 1.00 39.30  ? 168 LEU D C   1 
ATOM   4215 O O   . LEU B 2 38  ? 139.945 149.980 128.601 1.00 44.85  ? 168 LEU D O   1 
ATOM   4216 C CB  . LEU B 2 38  ? 140.170 146.945 128.542 1.00 48.81  ? 168 LEU D CB  1 
ATOM   4217 C CG  . LEU B 2 38  ? 140.007 146.316 127.156 1.00 51.65  ? 168 LEU D CG  1 
ATOM   4218 C CD1 . LEU B 2 38  ? 140.627 144.935 127.125 1.00 53.83  ? 168 LEU D CD1 1 
ATOM   4219 C CD2 . LEU B 2 38  ? 138.546 146.265 126.758 1.00 52.88  ? 168 LEU D CD2 1 
ATOM   4220 N N   . GLU B 2 39  ? 141.455 149.692 126.898 1.00 32.28  ? 169 GLU D N   1 
ATOM   4221 C CA  . GLU B 2 39  ? 141.150 150.989 126.239 1.00 29.68  ? 169 GLU D CA  1 
ATOM   4222 C C   . GLU B 2 39  ? 140.994 150.768 124.727 1.00 28.95  ? 169 GLU D C   1 
ATOM   4223 O O   . GLU B 2 39  ? 141.598 149.808 124.203 1.00 35.43  ? 169 GLU D O   1 
ATOM   4224 C CB  . GLU B 2 39  ? 142.264 151.991 126.541 1.00 33.73  ? 169 GLU D CB  1 
ATOM   4225 C CG  . GLU B 2 39  ? 142.374 152.335 128.023 1.00 36.30  ? 169 GLU D CG  1 
ATOM   4226 C CD  . GLU B 2 39  ? 143.638 153.077 128.414 1.00 33.52  ? 169 GLU D CD  1 
ATOM   4227 O OE1 . GLU B 2 39  ? 143.877 154.173 127.870 1.00 31.72  ? 169 GLU D OE1 1 
ATOM   4228 O OE2 . GLU B 2 39  ? 144.380 152.557 129.272 1.00 35.26  ? 169 GLU D OE2 1 
ATOM   4229 N N   . TRP B 2 40  ? 140.212 151.622 124.062 1.00 27.51  ? 170 TRP D N   1 
ATOM   4230 C CA  . TRP B 2 40  ? 140.016 151.501 122.601 1.00 33.47  ? 170 TRP D CA  1 
ATOM   4231 C C   . TRP B 2 40  ? 140.459 152.807 121.966 1.00 34.88  ? 170 TRP D C   1 
ATOM   4232 O O   . TRP B 2 40  ? 139.778 153.833 122.158 1.00 43.23  ? 170 TRP D O   1 
ATOM   4233 C CB  . TRP B 2 40  ? 138.557 151.151 122.300 1.00 41.46  ? 170 TRP D CB  1 
ATOM   4234 C CG  . TRP B 2 40  ? 138.176 149.769 122.763 1.00 44.00  ? 170 TRP D CG  1 
ATOM   4235 C CD1 . TRP B 2 40  ? 137.764 149.402 124.011 1.00 45.18  ? 170 TRP D CD1 1 
ATOM   4236 C CD2 . TRP B 2 40  ? 138.139 148.568 121.961 1.00 46.38  ? 170 TRP D CD2 1 
ATOM   4237 N NE1 . TRP B 2 40  ? 137.492 148.061 124.048 1.00 45.22  ? 170 TRP D NE1 1 
ATOM   4238 C CE2 . TRP B 2 40  ? 137.707 147.523 122.807 1.00 48.17  ? 170 TRP D CE2 1 
ATOM   4239 C CE3 . TRP B 2 40  ? 138.427 148.277 120.624 1.00 50.25  ? 170 TRP D CE3 1 
ATOM   4240 C CZ2 . TRP B 2 40  ? 137.560 146.214 122.354 1.00 57.47  ? 170 TRP D CZ2 1 
ATOM   4241 C CZ3 . TRP B 2 40  ? 138.278 146.982 120.179 1.00 55.15  ? 170 TRP D CZ3 1 
ATOM   4242 C CH2 . TRP B 2 40  ? 137.849 145.968 121.032 1.00 59.86  ? 170 TRP D CH2 1 
ATOM   4243 N N   . TYR B 2 41  ? 141.588 152.761 121.249 1.00 32.43  ? 171 TYR D N   1 
ATOM   4244 C CA  . TYR B 2 41  ? 142.180 154.003 120.684 1.00 38.21  ? 171 TYR D CA  1 
ATOM   4245 C C   . TYR B 2 41  ? 141.813 154.192 119.224 1.00 41.38  ? 171 TYR D C   1 
ATOM   4246 O O   . TYR B 2 41  ? 142.170 153.335 118.386 1.00 46.05  ? 171 TYR D O   1 
ATOM   4247 C CB  . TYR B 2 41  ? 143.705 153.960 120.813 1.00 38.76  ? 171 TYR D CB  1 
ATOM   4248 C CG  . TYR B 2 41  ? 144.231 154.067 122.237 1.00 35.52  ? 171 TYR D CG  1 
ATOM   4249 C CD1 . TYR B 2 41  ? 144.560 155.298 122.791 1.00 38.22  ? 171 TYR D CD1 1 
ATOM   4250 C CD2 . TYR B 2 41  ? 144.396 152.935 123.024 1.00 34.15  ? 171 TYR D CD2 1 
ATOM   4251 C CE1 . TYR B 2 41  ? 145.041 155.400 124.085 1.00 36.46  ? 171 TYR D CE1 1 
ATOM   4252 C CE2 . TYR B 2 41  ? 144.876 153.024 124.319 1.00 34.74  ? 171 TYR D CE2 1 
ATOM   4253 C CZ  . TYR B 2 41  ? 145.199 154.259 124.851 1.00 35.86  ? 171 TYR D CZ  1 
ATOM   4254 O OH  . TYR B 2 41  ? 145.670 154.337 126.127 1.00 40.00  ? 171 TYR D OH  1 
ATOM   4255 N N   . LEU B 2 42  ? 141.121 155.288 118.923 1.00 43.75  ? 172 LEU D N   1 
ATOM   4256 C CA  . LEU B 2 42  ? 140.800 155.648 117.549 1.00 48.57  ? 172 LEU D CA  1 
ATOM   4257 C C   . LEU B 2 42  ? 142.029 156.244 116.881 1.00 52.30  ? 172 LEU D C   1 
ATOM   4258 O O   . LEU B 2 42  ? 142.555 157.264 117.337 1.00 54.39  ? 172 LEU D O   1 
ATOM   4259 C CB  . LEU B 2 42  ? 139.646 156.646 117.509 1.00 53.35  ? 172 LEU D CB  1 
ATOM   4260 C CG  . LEU B 2 42  ? 139.019 156.919 116.142 1.00 63.41  ? 172 LEU D CG  1 
ATOM   4261 C CD1 . LEU B 2 42  ? 137.997 155.862 115.799 1.00 67.55  ? 172 LEU D CD1 1 
ATOM   4262 C CD2 . LEU B 2 42  ? 138.388 158.300 116.110 1.00 65.07  ? 172 LEU D CD2 1 
ATOM   4263 N N   . GLN B 2 43  ? 142.481 155.618 115.802 1.00 55.24  ? 173 GLN D N   1 
ATOM   4264 C CA  . GLN B 2 43  ? 143.568 156.146 114.983 1.00 60.54  ? 173 GLN D CA  1 
ATOM   4265 C C   . GLN B 2 43  ? 143.002 156.415 113.594 1.00 68.36  ? 173 GLN D C   1 
ATOM   4266 O O   . GLN B 2 43  ? 142.835 155.489 112.794 1.00 72.19  ? 173 GLN D O   1 
ATOM   4267 C CB  . GLN B 2 43  ? 144.748 155.181 114.931 1.00 58.80  ? 173 GLN D CB  1 
ATOM   4268 C CG  . GLN B 2 43  ? 145.838 155.606 113.962 1.00 61.82  ? 173 GLN D CG  1 
ATOM   4269 C CD  . GLN B 2 43  ? 146.910 154.553 113.792 1.00 61.85  ? 173 GLN D CD  1 
ATOM   4270 O OE1 . GLN B 2 43  ? 147.469 154.389 112.708 1.00 62.22  ? 173 GLN D OE1 1 
ATOM   4271 N NE2 . GLN B 2 43  ? 147.207 153.833 114.866 1.00 60.96  ? 173 GLN D NE2 1 
ATOM   4272 N N   . LYS B 2 44  ? 142.698 157.678 113.315 1.00 68.86  ? 174 LYS D N   1 
ATOM   4273 C CA  . LYS B 2 44  ? 142.220 158.047 111.995 1.00 76.93  ? 174 LYS D CA  1 
ATOM   4274 C C   . LYS B 2 44  ? 143.325 157.825 110.963 1.00 79.61  ? 174 LYS D C   1 
ATOM   4275 O O   . LYS B 2 44  ? 144.512 157.892 111.293 1.00 76.02  ? 174 LYS D O   1 
ATOM   4276 C CB  . LYS B 2 44  ? 141.773 159.506 111.976 1.00 79.15  ? 174 LYS D CB  1 
ATOM   4277 C CG  . LYS B 2 44  ? 140.735 159.854 113.028 1.00 80.24  ? 174 LYS D CG  1 
ATOM   4278 C CD  . LYS B 2 44  ? 139.326 159.663 112.497 1.00 83.64  ? 174 LYS D CD  1 
ATOM   4279 C CE  . LYS B 2 44  ? 138.400 160.762 112.990 1.00 81.77  ? 174 LYS D CE  1 
ATOM   4280 N NZ  . LYS B 2 44  ? 138.739 161.198 114.371 1.00 79.08  ? 174 LYS D NZ  1 
ATOM   4281 N N   . PRO B 2 45  ? 142.960 157.534 109.714 1.00 84.54  ? 175 PRO D N   1 
ATOM   4282 C CA  . PRO B 2 45  ? 143.980 157.317 108.675 1.00 85.69  ? 175 PRO D CA  1 
ATOM   4283 C C   . PRO B 2 45  ? 144.918 158.509 108.563 1.00 85.88  ? 175 PRO D C   1 
ATOM   4284 O O   . PRO B 2 45  ? 144.491 159.639 108.315 1.00 84.03  ? 175 PRO D O   1 
ATOM   4285 C CB  . PRO B 2 45  ? 143.148 157.123 107.402 1.00 83.83  ? 175 PRO D CB  1 
ATOM   4286 C CG  . PRO B 2 45  ? 141.832 156.621 107.889 1.00 83.85  ? 175 PRO D CG  1 
ATOM   4287 C CD  . PRO B 2 45  ? 141.596 157.296 109.210 1.00 82.83  ? 175 PRO D CD  1 
ATOM   4288 N N   . GLY B 2 46  ? 146.207 158.245 108.749 1.00 85.03  ? 176 GLY D N   1 
ATOM   4289 C CA  . GLY B 2 46  ? 147.192 159.315 108.761 1.00 81.28  ? 176 GLY D CA  1 
ATOM   4290 C C   . GLY B 2 46  ? 147.023 160.279 109.914 1.00 82.75  ? 176 GLY D C   1 
ATOM   4291 O O   . GLY B 2 46  ? 147.122 161.497 109.723 1.00 85.25  ? 176 GLY D O   1 
ATOM   4292 N N   . GLN B 2 47  ? 146.770 159.761 111.115 1.00 81.51  ? 177 GLN D N   1 
ATOM   4293 C CA  . GLN B 2 47  ? 146.549 160.607 112.277 1.00 78.30  ? 177 GLN D CA  1 
ATOM   4294 C C   . GLN B 2 47  ? 147.052 159.898 113.525 1.00 71.99  ? 177 GLN D C   1 
ATOM   4295 O O   . GLN B 2 47  ? 147.206 158.674 113.553 1.00 70.19  ? 177 GLN D O   1 
ATOM   4296 C CB  . GLN B 2 47  ? 145.068 160.970 112.436 1.00 79.09  ? 177 GLN D CB  1 
ATOM   4297 C CG  . GLN B 2 47  ? 144.691 162.322 111.861 1.00 80.33  ? 177 GLN D CG  1 
ATOM   4298 C CD  . GLN B 2 47  ? 143.605 163.008 112.663 1.00 80.64  ? 177 GLN D CD  1 
ATOM   4299 O OE1 . GLN B 2 47  ? 143.463 162.775 113.864 1.00 79.60  ? 177 GLN D OE1 1 
ATOM   4300 N NE2 . GLN B 2 47  ? 142.829 163.860 112.003 1.00 75.61  ? 177 GLN D NE2 1 
ATOM   4301 N N   . SER B 2 48  ? 147.312 160.691 114.559 1.00 66.33  ? 178 SER D N   1 
ATOM   4302 C CA  . SER B 2 48  ? 147.744 160.139 115.832 1.00 58.55  ? 178 SER D CA  1 
ATOM   4303 C C   . SER B 2 48  ? 146.572 159.458 116.534 1.00 53.07  ? 178 SER D C   1 
ATOM   4304 O O   . SER B 2 48  ? 145.466 160.005 116.567 1.00 53.49  ? 178 SER D O   1 
ATOM   4305 C CB  . SER B 2 48  ? 148.315 161.237 116.723 1.00 56.88  ? 178 SER D CB  1 
ATOM   4306 O OG  . SER B 2 48  ? 147.559 162.429 116.602 1.00 61.82  ? 178 SER D OG  1 
ATOM   4307 N N   . PRO B 2 49  ? 146.777 158.265 117.091 1.00 49.53  ? 179 PRO D N   1 
ATOM   4308 C CA  . PRO B 2 49  ? 145.691 157.590 117.809 1.00 47.53  ? 179 PRO D CA  1 
ATOM   4309 C C   . PRO B 2 49  ? 145.180 158.429 118.970 1.00 47.64  ? 179 PRO D C   1 
ATOM   4310 O O   . PRO B 2 49  ? 145.948 159.099 119.662 1.00 49.42  ? 179 PRO D O   1 
ATOM   4311 C CB  . PRO B 2 49  ? 146.346 156.295 118.299 1.00 44.69  ? 179 PRO D CB  1 
ATOM   4312 C CG  . PRO B 2 49  ? 147.426 156.039 117.317 1.00 50.25  ? 179 PRO D CG  1 
ATOM   4313 C CD  . PRO B 2 49  ? 147.950 157.393 116.922 1.00 53.38  ? 179 PRO D CD  1 
ATOM   4314 N N   . GLN B 2 50  ? 143.866 158.388 119.175 1.00 47.33  ? 180 GLN D N   1 
ATOM   4315 C CA  . GLN B 2 50  ? 143.220 159.108 120.261 1.00 45.06  ? 180 GLN D CA  1 
ATOM   4316 C C   . GLN B 2 50  ? 142.326 158.153 121.035 1.00 40.81  ? 180 GLN D C   1 
ATOM   4317 O O   . GLN B 2 50  ? 141.737 157.234 120.460 1.00 46.13  ? 180 GLN D O   1 
ATOM   4318 C CB  . GLN B 2 50  ? 142.407 160.301 119.742 1.00 49.71  ? 180 GLN D CB  1 
ATOM   4319 C CG  . GLN B 2 50  ? 141.265 159.933 118.811 1.00 52.88  ? 180 GLN D CG  1 
ATOM   4320 C CD  . GLN B 2 50  ? 141.104 160.919 117.672 1.00 60.64  ? 180 GLN D CD  1 
ATOM   4321 O OE1 . GLN B 2 50  ? 142.064 161.567 117.256 1.00 57.54  ? 180 GLN D OE1 1 
ATOM   4322 N NE2 . GLN B 2 50  ? 139.883 161.046 117.168 1.00 66.54  ? 180 GLN D NE2 1 
ATOM   4323 N N   . LEU B 2 51  ? 142.221 158.351 122.352 1.00 35.45  ? 181 LEU D N   1 
ATOM   4324 C CA  . LEU B 2 51  ? 141.458 157.392 123.199 1.00 37.36  ? 181 LEU D CA  1 
ATOM   4325 C C   . LEU B 2 51  ? 139.942 157.589 123.032 1.00 42.91  ? 181 LEU D C   1 
ATOM   4326 O O   . LEU B 2 51  ? 139.518 158.740 122.801 1.00 46.19  ? 181 LEU D O   1 
ATOM   4327 C CB  . LEU B 2 51  ? 141.900 157.567 124.650 1.00 36.35  ? 181 LEU D CB  1 
ATOM   4328 C CG  . LEU B 2 51  ? 141.324 156.576 125.665 1.00 36.20  ? 181 LEU D CG  1 
ATOM   4329 C CD1 . LEU B 2 51  ? 141.360 155.158 125.126 1.00 37.62  ? 181 LEU D CD1 1 
ATOM   4330 C CD2 . LEU B 2 51  ? 142.135 156.667 126.941 1.00 33.50  ? 181 LEU D CD2 1 
ATOM   4331 N N   . LEU B 2 52  ? 139.164 156.504 123.135 1.00 42.74  ? 182 LEU D N   1 
ATOM   4332 C CA  . LEU B 2 52  ? 137.681 156.589 123.053 1.00 43.63  ? 182 LEU D CA  1 
ATOM   4333 C C   . LEU B 2 52  ? 137.094 156.065 124.370 1.00 45.79  ? 182 LEU D C   1 
ATOM   4334 O O   . LEU B 2 52  ? 136.462 156.860 125.094 1.00 54.79  ? 182 LEU D O   1 
ATOM   4335 C CB  . LEU B 2 52  ? 137.152 155.769 121.878 1.00 45.25  ? 182 LEU D CB  1 
ATOM   4336 C CG  . LEU B 2 52  ? 137.695 156.120 120.491 1.00 52.35  ? 182 LEU D CG  1 
ATOM   4337 C CD1 . LEU B 2 52  ? 137.276 155.032 119.520 1.00 52.98  ? 182 LEU D CD1 1 
ATOM   4338 C CD2 . LEU B 2 52  ? 137.160 157.467 120.040 1.00 56.28  ? 182 LEU D CD2 1 
ATOM   4339 N N   . ILE B 2 53  ? 137.247 154.767 124.649 1.00 37.73  ? 183 ILE D N   1 
ATOM   4340 C CA  . ILE B 2 53  ? 136.727 154.146 125.904 1.00 40.87  ? 183 ILE D CA  1 
ATOM   4341 C C   . ILE B 2 53  ? 137.923 154.050 126.861 1.00 37.93  ? 183 ILE D C   1 
ATOM   4342 O O   . ILE B 2 53  ? 138.697 153.087 126.721 1.00 41.12  ? 183 ILE D O   1 
ATOM   4343 C CB  . ILE B 2 53  ? 136.079 152.772 125.629 1.00 42.60  ? 183 ILE D CB  1 
ATOM   4344 C CG1 . ILE B 2 53  ? 135.366 152.714 124.269 1.00 49.83  ? 183 ILE D CG1 1 
ATOM   4345 C CG2 . ILE B 2 53  ? 135.140 152.373 126.768 1.00 47.76  ? 183 ILE D CG2 1 
ATOM   4346 C CD1 . ILE B 2 53  ? 134.285 153.762 124.069 1.00 57.53  ? 183 ILE D CD1 1 
ATOM   4347 N N   . TYR B 2 54  ? 138.100 155.006 127.780 1.00 40.02  ? 184 TYR D N   1 
ATOM   4348 C CA  . TYR B 2 54  ? 139.303 155.021 128.661 1.00 39.50  ? 184 TYR D CA  1 
ATOM   4349 C C   . TYR B 2 54  ? 139.280 153.813 129.598 1.00 40.30  ? 184 TYR D C   1 
ATOM   4350 O O   . TYR B 2 54  ? 140.304 153.549 130.260 1.00 41.24  ? 184 TYR D O   1 
ATOM   4351 C CB  . TYR B 2 54  ? 139.447 156.359 129.397 1.00 42.61  ? 184 TYR D CB  1 
ATOM   4352 C CG  . TYR B 2 54  ? 138.656 156.557 130.682 1.00 40.30  ? 184 TYR D CG  1 
ATOM   4353 C CD1 . TYR B 2 54  ? 139.141 156.100 131.902 1.00 41.27  ? 184 TYR D CD1 1 
ATOM   4354 C CD2 . TYR B 2 54  ? 137.456 157.256 130.683 1.00 42.29  ? 184 TYR D CD2 1 
ATOM   4355 C CE1 . TYR B 2 54  ? 138.435 156.293 133.077 1.00 43.04  ? 184 TYR D CE1 1 
ATOM   4356 C CE2 . TYR B 2 54  ? 136.744 157.462 131.852 1.00 46.79  ? 184 TYR D CE2 1 
ATOM   4357 C CZ  . TYR B 2 54  ? 137.234 156.978 133.052 1.00 48.27  ? 184 TYR D CZ  1 
ATOM   4358 O OH  . TYR B 2 54  ? 136.534 157.175 134.207 1.00 57.22  ? 184 TYR D OH  1 
ATOM   4359 N N   . LYS B 2 55  ? 138.156 153.097 129.688 1.00 43.36  ? 185 LYS D N   1 
ATOM   4360 C CA  . LYS B 2 55  ? 138.081 151.852 130.497 1.00 48.15  ? 185 LYS D CA  1 
ATOM   4361 C C   . LYS B 2 55  ? 137.373 150.778 129.662 1.00 51.49  ? 185 LYS D C   1 
ATOM   4362 O O   . LYS B 2 55  ? 137.103 151.046 128.476 1.00 48.76  ? 185 LYS D O   1 
ATOM   4363 C CB  . LYS B 2 55  ? 137.351 152.131 131.813 1.00 50.94  ? 185 LYS D CB  1 
ATOM   4364 C CG  . LYS B 2 55  ? 137.755 151.286 133.016 1.00 51.49  ? 185 LYS D CG  1 
ATOM   4365 C CD  . LYS B 2 55  ? 139.255 151.090 133.199 1.00 43.54  ? 185 LYS D CD  1 
ATOM   4366 C CE  . LYS B 2 55  ? 140.034 152.358 133.314 1.00 40.80  ? 185 LYS D CE  1 
ATOM   4367 N NZ  . LYS B 2 55  ? 141.463 152.067 133.181 1.00 41.55  ? 185 LYS D NZ  1 
ATOM   4368 N N   . VAL B 2 56  ? 137.117 149.602 130.238 1.00 53.48  ? 186 VAL D N   1 
ATOM   4369 C CA  . VAL B 2 56  ? 136.361 148.528 129.525 1.00 55.48  ? 186 VAL D CA  1 
ATOM   4370 C C   . VAL B 2 56  ? 134.989 149.098 129.134 1.00 58.71  ? 186 VAL D C   1 
ATOM   4371 O O   . VAL B 2 56  ? 134.503 148.734 128.042 1.00 59.76  ? 186 VAL D O   1 
ATOM   4372 C CB  . VAL B 2 56  ? 136.201 147.239 130.354 1.00 62.02  ? 186 VAL D CB  1 
ATOM   4373 C CG1 . VAL B 2 56  ? 137.507 146.466 130.458 1.00 61.34  ? 186 VAL D CG1 1 
ATOM   4374 C CG2 . VAL B 2 56  ? 135.620 147.504 131.738 1.00 59.46  ? 186 VAL D CG2 1 
ATOM   4375 N N   . SER B 2 57  ? 134.410 149.966 129.978 1.00 58.97  ? 187 SER D N   1 
ATOM   4376 C CA  . SER B 2 57  ? 133.039 150.492 129.727 1.00 59.57  ? 187 SER D CA  1 
ATOM   4377 C C   . SER B 2 57  ? 132.888 151.940 130.225 1.00 57.93  ? 187 SER D C   1 
ATOM   4378 O O   . SER B 2 57  ? 131.797 152.266 130.743 1.00 55.67  ? 187 SER D O   1 
ATOM   4379 C CB  . SER B 2 57  ? 132.010 149.600 130.372 1.00 59.84  ? 187 SER D CB  1 
ATOM   4380 O OG  . SER B 2 57  ? 132.229 149.509 131.773 1.00 61.83  ? 187 SER D OG  1 
ATOM   4381 N N   . ASP B 2 58  ? 133.923 152.771 130.080 1.00 55.31  ? 188 ASP D N   1 
ATOM   4382 C CA  . ASP B 2 58  ? 133.853 154.211 130.471 1.00 51.05  ? 188 ASP D CA  1 
ATOM   4383 C C   . ASP B 2 58  ? 133.805 155.036 129.177 1.00 48.37  ? 188 ASP D C   1 
ATOM   4384 O O   . ASP B 2 58  ? 133.387 154.457 128.154 1.00 50.30  ? 188 ASP D O   1 
ATOM   4385 C CB  . ASP B 2 58  ? 134.969 154.561 131.442 1.00 48.66  ? 188 ASP D CB  1 
ATOM   4386 C CG  . ASP B 2 58  ? 134.756 154.059 132.863 1.00 50.99  ? 188 ASP D CG  1 
ATOM   4387 O OD1 . ASP B 2 58  ? 134.551 152.840 133.034 1.00 48.68  ? 188 ASP D OD1 1 
ATOM   4388 O OD2 . ASP B 2 58  ? 134.789 154.893 133.789 1.00 52.15  ? 188 ASP D OD2 1 
ATOM   4389 N N   . ARG B 2 59  ? 134.174 156.325 129.195 1.00 46.22  ? 189 ARG D N   1 
ATOM   4390 C CA  . ARG B 2 59  ? 134.227 157.126 127.946 1.00 50.37  ? 189 ARG D CA  1 
ATOM   4391 C C   . ARG B 2 59  ? 135.169 158.321 128.139 1.00 52.67  ? 189 ARG D C   1 
ATOM   4392 O O   . ARG B 2 59  ? 135.155 158.918 129.236 1.00 56.01  ? 189 ARG D O   1 
ATOM   4393 C CB  . ARG B 2 59  ? 132.825 157.583 127.530 1.00 57.22  ? 189 ARG D CB  1 
ATOM   4394 C CG  . ARG B 2 59  ? 132.762 158.202 126.143 1.00 59.08  ? 189 ARG D CG  1 
ATOM   4395 C CD  . ARG B 2 59  ? 131.321 158.377 125.700 1.00 68.69  ? 189 ARG D CD  1 
ATOM   4396 N NE  . ARG B 2 59  ? 130.619 157.091 125.611 1.00 72.74  ? 189 ARG D NE  1 
ATOM   4397 C CZ  . ARG B 2 59  ? 129.543 156.771 126.318 1.00 71.60  ? 189 ARG D CZ  1 
ATOM   4398 N NH1 . ARG B 2 59  ? 129.063 157.619 127.210 1.00 68.98  ? 189 ARG D NH1 1 
ATOM   4399 N NH2 . ARG B 2 59  ? 128.952 155.606 126.130 1.00 71.17  ? 189 ARG D NH2 1 
ATOM   4400 N N   . PHE B 2 60  ? 135.932 158.658 127.095 1.00 50.39  ? 190 PHE D N   1 
ATOM   4401 C CA  . PHE B 2 60  ? 136.919 159.766 127.187 1.00 51.88  ? 190 PHE D CA  1 
ATOM   4402 C C   . PHE B 2 60  ? 136.218 161.098 126.979 1.00 60.12  ? 190 PHE D C   1 
ATOM   4403 O O   . PHE B 2 60  ? 135.325 161.191 126.110 1.00 62.09  ? 190 PHE D O   1 
ATOM   4404 C CB  . PHE B 2 60  ? 138.007 159.553 126.131 1.00 46.65  ? 190 PHE D CB  1 
ATOM   4405 C CG  . PHE B 2 60  ? 139.182 160.516 126.216 1.00 47.34  ? 190 PHE D CG  1 
ATOM   4406 C CD1 . PHE B 2 60  ? 139.639 160.980 127.444 1.00 45.24  ? 190 PHE D CD1 1 
ATOM   4407 C CD2 . PHE B 2 60  ? 139.819 160.964 125.065 1.00 45.94  ? 190 PHE D CD2 1 
ATOM   4408 C CE1 . PHE B 2 60  ? 140.705 161.861 127.514 1.00 42.93  ? 190 PHE D CE1 1 
ATOM   4409 C CE2 . PHE B 2 60  ? 140.887 161.843 125.142 1.00 43.40  ? 190 PHE D CE2 1 
ATOM   4410 C CZ  . PHE B 2 60  ? 141.326 162.290 126.365 1.00 41.54  ? 190 PHE D CZ  1 
ATOM   4411 N N   . SER B 2 61  ? 136.608 162.110 127.755 1.00 59.62  ? 191 SER D N   1 
ATOM   4412 C CA  . SER B 2 61  ? 136.048 163.444 127.597 1.00 57.75  ? 191 SER D CA  1 
ATOM   4413 C C   . SER B 2 61  ? 136.295 163.950 126.182 1.00 59.35  ? 191 SER D C   1 
ATOM   4414 O O   . SER B 2 61  ? 137.406 163.847 125.655 1.00 62.04  ? 191 SER D O   1 
ATOM   4415 C CB  . SER B 2 61  ? 136.661 164.400 128.620 1.00 57.79  ? 191 SER D CB  1 
ATOM   4416 O OG  . SER B 2 61  ? 138.063 164.507 128.444 1.00 55.42  ? 191 SER D OG  1 
ATOM   4417 N N   . GLY B 2 62  ? 135.250 164.498 125.566 1.00 59.50  ? 192 GLY D N   1 
ATOM   4418 C CA  . GLY B 2 62  ? 135.309 164.918 124.186 1.00 64.21  ? 192 GLY D CA  1 
ATOM   4419 C C   . GLY B 2 62  ? 134.900 163.859 123.187 1.00 67.25  ? 192 GLY D C   1 
ATOM   4420 O O   . GLY B 2 62  ? 134.685 164.186 122.013 1.00 70.64  ? 192 GLY D O   1 
ATOM   4421 N N   . VAL B 2 63  ? 134.790 162.605 123.611 1.00 65.50  ? 193 VAL D N   1 
ATOM   4422 C CA  . VAL B 2 63  ? 134.309 161.526 122.756 1.00 70.59  ? 193 VAL D CA  1 
ATOM   4423 C C   . VAL B 2 63  ? 132.802 161.405 122.967 1.00 74.08  ? 193 VAL D C   1 
ATOM   4424 O O   . VAL B 2 63  ? 132.364 161.232 124.116 1.00 74.76  ? 193 VAL D O   1 
ATOM   4425 C CB  . VAL B 2 63  ? 135.018 160.202 123.065 1.00 67.39  ? 193 VAL D CB  1 
ATOM   4426 C CG1 . VAL B 2 63  ? 134.121 159.020 122.734 1.00 66.82  ? 193 VAL D CG1 1 
ATOM   4427 C CG2 . VAL B 2 63  ? 136.324 160.113 122.293 1.00 63.18  ? 193 VAL D CG2 1 
ATOM   4428 N N   . PRO B 2 64  ? 131.963 161.435 121.898 1.00 78.69  ? 194 PRO D N   1 
ATOM   4429 C CA  . PRO B 2 64  ? 130.515 161.388 122.058 1.00 80.44  ? 194 PRO D CA  1 
ATOM   4430 C C   . PRO B 2 64  ? 130.023 160.083 122.669 1.00 78.33  ? 194 PRO D C   1 
ATOM   4431 O O   . PRO B 2 64  ? 130.758 159.076 122.630 1.00 75.99  ? 194 PRO D O   1 
ATOM   4432 C CB  . PRO B 2 64  ? 129.979 161.581 120.626 1.00 81.30  ? 194 PRO D CB  1 
ATOM   4433 C CG  . PRO B 2 64  ? 131.129 162.217 119.886 1.00 81.76  ? 194 PRO D CG  1 
ATOM   4434 C CD  . PRO B 2 64  ? 132.335 161.519 120.479 1.00 79.05  ? 194 PRO D CD  1 
ATOM   4435 N N   . ASP B 2 65  ? 128.789 160.084 123.180 1.00 80.64  ? 195 ASP D N   1 
ATOM   4436 C CA  . ASP B 2 65  ? 128.220 158.879 123.847 1.00 78.70  ? 195 ASP D CA  1 
ATOM   4437 C C   . ASP B 2 65  ? 127.997 157.755 122.829 1.00 80.45  ? 195 ASP D C   1 
ATOM   4438 O O   . ASP B 2 65  ? 127.740 156.612 123.263 1.00 80.16  ? 195 ASP D O   1 
ATOM   4439 C CB  . ASP B 2 65  ? 126.936 159.218 124.588 1.00 80.42  ? 195 ASP D CB  1 
ATOM   4440 C CG  . ASP B 2 65  ? 125.870 159.919 123.758 1.00 83.16  ? 195 ASP D CG  1 
ATOM   4441 O OD1 . ASP B 2 65  ? 126.129 160.174 122.562 1.00 86.10  ? 195 ASP D OD1 1 
ATOM   4442 O OD2 . ASP B 2 65  ? 124.790 160.207 124.315 1.00 81.83  ? 195 ASP D OD2 1 
ATOM   4443 N N   . ARG B 2 66  ? 128.095 158.060 121.532 1.00 83.66  ? 196 ARG D N   1 
ATOM   4444 C CA  . ARG B 2 66  ? 127.821 157.037 120.487 1.00 84.11  ? 196 ARG D CA  1 
ATOM   4445 C C   . ARG B 2 66  ? 128.771 155.842 120.680 1.00 80.23  ? 196 ARG D C   1 
ATOM   4446 O O   . ARG B 2 66  ? 128.393 154.717 120.284 1.00 80.11  ? 196 ARG D O   1 
ATOM   4447 C CB  . ARG B 2 66  ? 127.961 157.633 119.081 1.00 86.00  ? 196 ARG D CB  1 
ATOM   4448 C CG  . ARG B 2 66  ? 129.385 157.639 118.547 1.00 83.56  ? 196 ARG D CG  1 
ATOM   4449 C CD  . ARG B 2 66  ? 129.457 158.200 117.141 1.00 87.40  ? 196 ARG D CD  1 
ATOM   4450 N NE  . ARG B 2 66  ? 129.254 159.651 117.112 1.00 92.41  ? 196 ARG D NE  1 
ATOM   4451 C CZ  . ARG B 2 66  ? 130.163 160.504 116.662 1.00 94.33  ? 196 ARG D CZ  1 
ATOM   4452 N NH1 . ARG B 2 66  ? 131.353 160.060 116.300 1.00 92.02  ? 196 ARG D NH1 1 
ATOM   4453 N NH2 . ARG B 2 66  ? 129.882 161.792 116.576 1.00 95.24  ? 196 ARG D NH2 1 
ATOM   4454 N N   . PHE B 2 67  ? 129.952 156.078 121.262 1.00 77.89  ? 197 PHE D N   1 
ATOM   4455 C CA  . PHE B 2 67  ? 130.924 154.980 121.514 1.00 72.67  ? 197 PHE D CA  1 
ATOM   4456 C C   . PHE B 2 67  ? 130.592 154.300 122.839 1.00 73.05  ? 197 PHE D C   1 
ATOM   4457 O O   . PHE B 2 67  ? 130.228 155.001 123.802 1.00 73.68  ? 197 PHE D O   1 
ATOM   4458 C CB  . PHE B 2 67  ? 132.363 155.506 121.484 1.00 71.06  ? 197 PHE D CB  1 
ATOM   4459 C CG  . PHE B 2 67  ? 132.796 156.107 120.153 1.00 73.57  ? 197 PHE D CG  1 
ATOM   4460 C CD1 . PHE B 2 67  ? 133.303 155.302 119.140 1.00 75.16  ? 197 PHE D CD1 1 
ATOM   4461 C CD2 . PHE B 2 67  ? 132.711 157.475 119.925 1.00 78.14  ? 197 PHE D CD2 1 
ATOM   4462 C CE1 . PHE B 2 67  ? 133.699 155.851 117.931 1.00 77.65  ? 197 PHE D CE1 1 
ATOM   4463 C CE2 . PHE B 2 67  ? 133.112 158.018 118.715 1.00 79.03  ? 197 PHE D CE2 1 
ATOM   4464 C CZ  . PHE B 2 67  ? 133.604 157.206 117.721 1.00 78.83  ? 197 PHE D CZ  1 
ATOM   4465 N N   . SER B 2 68  ? 130.710 152.973 122.890 1.00 73.26  ? 198 SER D N   1 
ATOM   4466 C CA  . SER B 2 68  ? 130.430 152.200 124.093 1.00 71.42  ? 198 SER D CA  1 
ATOM   4467 C C   . SER B 2 68  ? 131.406 151.035 124.154 1.00 69.34  ? 198 SER D C   1 
ATOM   4468 O O   . SER B 2 68  ? 132.140 150.762 123.202 1.00 71.04  ? 198 SER D O   1 
ATOM   4469 C CB  . SER B 2 68  ? 128.981 151.700 124.120 1.00 72.73  ? 198 SER D CB  1 
ATOM   4470 O OG  . SER B 2 68  ? 128.060 152.765 123.951 1.00 76.90  ? 198 SER D OG  1 
ATOM   4471 N N   . GLY B 2 69  ? 131.479 150.392 125.322 1.00 66.60  ? 199 GLY D N   1 
ATOM   4472 C CA  . GLY B 2 69  ? 132.368 149.235 125.525 1.00 67.75  ? 199 GLY D CA  1 
ATOM   4473 C C   . GLY B 2 69  ? 131.810 148.363 126.628 1.00 65.55  ? 199 GLY D C   1 
ATOM   4474 O O   . GLY B 2 69  ? 131.137 148.916 127.520 1.00 62.45  ? 199 GLY D O   1 
ATOM   4475 N N   . SER B 2 70  ? 132.043 147.053 126.564 1.00 69.79  ? 200 SER D N   1 
ATOM   4476 C CA  . SER B 2 70  ? 131.540 146.098 127.582 1.00 73.62  ? 200 SER D CA  1 
ATOM   4477 C C   . SER B 2 70  ? 132.355 144.807 127.488 1.00 75.11  ? 200 SER D C   1 
ATOM   4478 O O   . SER B 2 70  ? 132.651 144.442 126.392 1.00 74.26  ? 200 SER D O   1 
ATOM   4479 C CB  . SER B 2 70  ? 130.071 145.831 127.396 1.00 73.92  ? 200 SER D CB  1 
ATOM   4480 O OG  . SER B 2 70  ? 129.808 145.352 126.084 1.00 71.74  ? 200 SER D OG  1 
ATOM   4481 N N   . GLY B 2 71  ? 132.648 144.126 128.587 1.00 74.03  ? 201 GLY D N   1 
ATOM   4482 C CA  . GLY B 2 71  ? 133.425 142.904 128.637 1.00 75.22  ? 201 GLY D CA  1 
ATOM   4483 C C   . GLY B 2 71  ? 133.849 142.574 130.051 1.00 77.18  ? 201 GLY D C   1 
ATOM   4484 O O   . GLY B 2 71  ? 133.863 143.414 130.949 1.00 74.77  ? 201 GLY D O   1 
ATOM   4485 N N   . SER B 2 72  ? 134.253 141.315 130.243 1.00 79.72  ? 202 SER D N   1 
ATOM   4486 C CA  . SER B 2 72  ? 134.743 140.872 131.574 1.00 79.03  ? 202 SER D CA  1 
ATOM   4487 C C   . SER B 2 72  ? 135.739 139.721 131.374 1.00 81.51  ? 202 SER D C   1 
ATOM   4488 O O   . SER B 2 72  ? 135.670 139.056 130.318 1.00 82.64  ? 202 SER D O   1 
ATOM   4489 C CB  . SER B 2 72  ? 133.604 140.454 132.463 1.00 79.15  ? 202 SER D CB  1 
ATOM   4490 O OG  . SER B 2 72  ? 132.901 139.355 131.898 1.00 79.76  ? 202 SER D OG  1 
ATOM   4491 N N   . GLY B 2 73  ? 136.626 139.498 132.348 1.00 82.59  ? 203 GLY D N   1 
ATOM   4492 C CA  . GLY B 2 73  ? 137.596 138.391 132.251 1.00 85.18  ? 203 GLY D CA  1 
ATOM   4493 C C   . GLY B 2 73  ? 138.546 138.591 131.086 1.00 83.43  ? 203 GLY D C   1 
ATOM   4494 O O   . GLY B 2 73  ? 139.375 139.519 131.154 1.00 80.53  ? 203 GLY D O   1 
ATOM   4495 N N   . THR B 2 74  ? 138.447 137.742 130.059 1.00 83.09  ? 204 THR D N   1 
ATOM   4496 C CA  . THR B 2 74  ? 139.362 137.833 128.901 1.00 82.28  ? 204 THR D CA  1 
ATOM   4497 C C   . THR B 2 74  ? 138.596 138.320 127.689 1.00 81.56  ? 204 THR D C   1 
ATOM   4498 O O   . THR B 2 74  ? 139.251 138.786 126.733 1.00 80.15  ? 204 THR D O   1 
ATOM   4499 C CB  . THR B 2 74  ? 140.000 136.470 128.644 1.00 81.43  ? 204 THR D CB  1 
ATOM   4500 O OG1 . THR B 2 74  ? 138.914 135.612 128.312 1.00 83.56  ? 204 THR D OG1 1 
ATOM   4501 C CG2 . THR B 2 74  ? 140.739 135.934 129.857 1.00 79.66  ? 204 THR D CG2 1 
ATOM   4502 N N   . ASP B 2 75  ? 137.264 138.222 127.713 1.00 80.41  ? 205 ASP D N   1 
ATOM   4503 C CA  . ASP B 2 75  ? 136.455 138.600 126.520 1.00 80.03  ? 205 ASP D CA  1 
ATOM   4504 C C   . ASP B 2 75  ? 135.944 140.035 126.672 1.00 78.92  ? 205 ASP D C   1 
ATOM   4505 O O   . ASP B 2 75  ? 135.260 140.313 127.679 1.00 79.35  ? 205 ASP D O   1 
ATOM   4506 C CB  . ASP B 2 75  ? 135.328 137.610 126.271 1.00 81.86  ? 205 ASP D CB  1 
ATOM   4507 C CG  . ASP B 2 75  ? 134.648 137.729 124.914 1.00 83.40  ? 205 ASP D CG  1 
ATOM   4508 O OD1 . ASP B 2 75  ? 134.079 138.805 124.633 1.00 83.16  ? 205 ASP D OD1 1 
ATOM   4509 O OD2 . ASP B 2 75  ? 134.698 136.745 124.147 1.00 81.11  ? 205 ASP D OD2 1 
ATOM   4510 N N   . PHE B 2 76  ? 136.300 140.908 125.736 1.00 77.65  ? 206 PHE D N   1 
ATOM   4511 C CA  . PHE B 2 76  ? 135.831 142.314 125.770 1.00 76.30  ? 206 PHE D CA  1 
ATOM   4512 C C   . PHE B 2 76  ? 135.213 142.627 124.432 1.00 73.30  ? 206 PHE D C   1 
ATOM   4513 O O   . PHE B 2 76  ? 135.327 141.785 123.521 1.00 73.41  ? 206 PHE D O   1 
ATOM   4514 C CB  . PHE B 2 76  ? 137.011 143.213 126.146 1.00 72.54  ? 206 PHE D CB  1 
ATOM   4515 C CG  . PHE B 2 76  ? 137.584 142.895 127.520 1.00 70.74  ? 206 PHE D CG  1 
ATOM   4516 C CD1 . PHE B 2 76  ? 138.646 142.011 127.665 1.00 73.48  ? 206 PHE D CD1 1 
ATOM   4517 C CD2 . PHE B 2 76  ? 137.034 143.458 128.666 1.00 68.35  ? 206 PHE D CD2 1 
ATOM   4518 C CE1 . PHE B 2 76  ? 139.155 141.717 128.920 1.00 75.41  ? 206 PHE D CE1 1 
ATOM   4519 C CE2 . PHE B 2 76  ? 137.548 143.160 129.917 1.00 71.59  ? 206 PHE D CE2 1 
ATOM   4520 C CZ  . PHE B 2 76  ? 138.608 142.295 130.041 1.00 74.26  ? 206 PHE D CZ  1 
ATOM   4521 N N   . THR B 2 77  ? 134.482 143.732 124.339 1.00 70.00  ? 207 THR D N   1 
ATOM   4522 C CA  . THR B 2 77  ? 133.915 144.193 123.081 1.00 72.41  ? 207 THR D CA  1 
ATOM   4523 C C   . THR B 2 77  ? 133.648 145.688 123.155 1.00 69.79  ? 207 THR D C   1 
ATOM   4524 O O   . THR B 2 77  ? 133.564 146.276 124.236 1.00 68.80  ? 207 THR D O   1 
ATOM   4525 C CB  . THR B 2 77  ? 132.624 143.441 122.732 1.00 78.74  ? 207 THR D CB  1 
ATOM   4526 O OG1 . THR B 2 77  ? 132.189 143.819 121.420 1.00 80.17  ? 207 THR D OG1 1 
ATOM   4527 C CG2 . THR B 2 77  ? 131.528 143.762 123.738 1.00 77.07  ? 207 THR D CG2 1 
ATOM   4528 N N   . LEU B 2 78  ? 133.522 146.297 121.980 1.00 68.39  ? 208 LEU D N   1 
ATOM   4529 C CA  . LEU B 2 78  ? 133.197 147.707 121.839 1.00 66.28  ? 208 LEU D CA  1 
ATOM   4530 C C   . LEU B 2 78  ? 131.940 147.850 120.995 1.00 75.27  ? 208 LEU D C   1 
ATOM   4531 O O   . LEU B 2 78  ? 131.809 147.208 119.949 1.00 77.56  ? 208 LEU D O   1 
ATOM   4532 C CB  . LEU B 2 78  ? 134.356 148.479 121.200 1.00 64.54  ? 208 LEU D CB  1 
ATOM   4533 C CG  . LEU B 2 78  ? 134.248 150.004 121.154 1.00 67.06  ? 208 LEU D CG  1 
ATOM   4534 C CD1 . LEU B 2 78  ? 135.619 150.638 121.285 1.00 67.06  ? 208 LEU D CD1 1 
ATOM   4535 C CD2 . LEU B 2 78  ? 133.586 150.442 119.860 1.00 70.00  ? 208 LEU D CD2 1 
ATOM   4536 N N   . LYS B 2 79  ? 131.020 148.696 121.450 1.00 78.61  ? 209 LYS D N   1 
ATOM   4537 C CA  . LYS B 2 79  ? 129.740 148.898 120.786 1.00 79.32  ? 209 LYS D CA  1 
ATOM   4538 C C   . LYS B 2 79  ? 129.658 150.319 120.249 1.00 81.74  ? 209 LYS D C   1 
ATOM   4539 O O   . LYS B 2 79  ? 129.931 151.279 120.977 1.00 82.02  ? 209 LYS D O   1 
ATOM   4540 C CB  . LYS B 2 79  ? 128.576 148.627 121.743 1.00 76.79  ? 209 LYS D CB  1 
ATOM   4541 C CG  . LYS B 2 79  ? 128.035 147.211 121.672 1.00 82.45  ? 209 LYS D CG  1 
ATOM   4542 C CD  . LYS B 2 79  ? 127.741 146.808 120.236 1.00 85.88  ? 209 LYS D CD  1 
ATOM   4543 C CE  . LYS B 2 79  ? 126.372 147.296 119.794 1.00 87.39  ? 209 LYS D CE  1 
ATOM   4544 N NZ  . LYS B 2 79  ? 125.802 146.444 118.714 1.00 86.53  ? 209 LYS D NZ  1 
ATOM   4545 N N   . ILE B 2 80  ? 129.284 150.446 118.979 1.00 85.43  ? 210 ILE D N   1 
ATOM   4546 C CA  . ILE B 2 80  ? 129.069 151.743 118.337 1.00 87.31  ? 210 ILE D CA  1 
ATOM   4547 C C   . ILE B 2 80  ? 127.658 151.698 117.757 1.00 94.51  ? 210 ILE D C   1 
ATOM   4548 O O   . ILE B 2 80  ? 127.446 151.226 116.635 1.00 98.53  ? 210 ILE D O   1 
ATOM   4549 C CB  . ILE B 2 80  ? 130.107 152.047 117.254 1.00 87.19  ? 210 ILE D CB  1 
ATOM   4550 C CG1 . ILE B 2 80  ? 131.518 151.985 117.835 1.00 81.82  ? 210 ILE D CG1 1 
ATOM   4551 C CG2 . ILE B 2 80  ? 129.857 153.412 116.645 1.00 90.54  ? 210 ILE D CG2 1 
ATOM   4552 C CD1 . ILE B 2 80  ? 132.597 152.342 116.844 1.00 77.06  ? 210 ILE D CD1 1 
ATOM   4553 N N   . SER B 2 81  ? 126.681 152.187 118.525 1.00 95.14  ? 211 SER D N   1 
ATOM   4554 C CA  . SER B 2 81  ? 125.287 152.102 118.096 1.00 97.58  ? 211 SER D CA  1 
ATOM   4555 C C   . SER B 2 81  ? 125.048 152.896 116.818 1.00 99.41  ? 211 SER D C   1 
ATOM   4556 O O   . SER B 2 81  ? 124.371 152.420 115.900 1.00 99.97  ? 211 SER D O   1 
ATOM   4557 C CB  . SER B 2 81  ? 124.368 152.591 119.214 1.00 91.43  ? 211 SER D CB  1 
ATOM   4558 O OG  . SER B 2 81  ? 124.784 152.085 120.471 1.00 88.78  ? 211 SER D OG  1 
ATOM   4559 N N   . ARG B 2 82  ? 125.594 154.106 116.740 1.00 99.39  ? 212 ARG D N   1 
ATOM   4560 C CA  . ARG B 2 82  ? 125.501 154.944 115.553 1.00 101.48 ? 212 ARG D CA  1 
ATOM   4561 C C   . ARG B 2 82  ? 126.906 155.211 115.039 1.00 102.79 ? 212 ARG D C   1 
ATOM   4562 O O   . ARG B 2 82  ? 127.780 155.624 115.806 1.00 101.05 ? 212 ARG D O   1 
ATOM   4563 C CB  . ARG B 2 82  ? 124.786 156.262 115.860 1.00 101.49 ? 212 ARG D CB  1 
ATOM   4564 C CG  . ARG B 2 82  ? 123.850 156.197 117.056 1.00 101.80 ? 212 ARG D CG  1 
ATOM   4565 C CD  . ARG B 2 82  ? 123.092 157.501 117.237 1.00 103.32 ? 212 ARG D CD  1 
ATOM   4566 N NE  . ARG B 2 82  ? 123.960 158.575 117.706 1.00 103.20 ? 212 ARG D NE  1 
ATOM   4567 C CZ  . ARG B 2 82  ? 124.075 158.947 118.973 1.00 102.94 ? 212 ARG D CZ  1 
ATOM   4568 N NH1 . ARG B 2 82  ? 123.389 158.350 119.934 1.00 101.60 ? 212 ARG D NH1 1 
ATOM   4569 N NH2 . ARG B 2 82  ? 124.900 159.943 119.285 1.00 99.10  ? 212 ARG D NH2 1 
ATOM   4570 N N   . VAL B 2 83  ? 127.124 154.976 113.748 1.00 104.72 ? 213 VAL D N   1 
ATOM   4571 C CA  . VAL B 2 83  ? 128.436 155.126 113.131 1.00 106.39 ? 213 VAL D CA  1 
ATOM   4572 C C   . VAL B 2 83  ? 128.338 156.160 112.018 1.00 108.02 ? 213 VAL D C   1 
ATOM   4573 O O   . VAL B 2 83  ? 127.432 156.096 111.178 1.00 107.57 ? 213 VAL D O   1 
ATOM   4574 C CB  . VAL B 2 83  ? 128.974 153.782 112.602 1.00 106.61 ? 213 VAL D CB  1 
ATOM   4575 C CG1 . VAL B 2 83  ? 127.913 153.056 111.796 1.00 108.13 ? 213 VAL D CG1 1 
ATOM   4576 C CG2 . VAL B 2 83  ? 130.229 153.997 111.771 1.00 103.30 ? 213 VAL D CG2 1 
ATOM   4577 N N   . GLU B 2 84  ? 129.260 157.116 112.025 1.00 106.95 ? 214 GLU D N   1 
ATOM   4578 C CA  . GLU B 2 84  ? 129.340 158.171 111.025 1.00 107.59 ? 214 GLU D CA  1 
ATOM   4579 C C   . GLU B 2 84  ? 130.716 158.124 110.359 1.00 105.43 ? 214 GLU D C   1 
ATOM   4580 O O   . GLU B 2 84  ? 131.511 157.208 110.589 1.00 102.93 ? 214 GLU D O   1 
ATOM   4581 C CB  . GLU B 2 84  ? 129.060 159.534 111.663 1.00 109.29 ? 214 GLU D CB  1 
ATOM   4582 C CG  . GLU B 2 84  ? 128.343 160.520 110.752 1.00 110.12 ? 214 GLU D CG  1 
ATOM   4583 C CD  . GLU B 2 84  ? 126.835 160.389 110.819 1.00 109.62 ? 214 GLU D CD  1 
ATOM   4584 O OE1 . GLU B 2 84  ? 126.332 159.797 111.797 1.00 111.95 ? 214 GLU D OE1 1 
ATOM   4585 O OE2 . GLU B 2 84  ? 126.153 160.878 109.894 1.00 106.58 ? 214 GLU D OE2 1 
ATOM   4586 N N   . ALA B 2 85  ? 131.003 159.123 109.521 1.00 104.73 ? 215 ALA D N   1 
ATOM   4587 C CA  . ALA B 2 85  ? 132.312 159.173 108.827 1.00 101.90 ? 215 ALA D CA  1 
ATOM   4588 C C   . ALA B 2 85  ? 133.439 159.298 109.855 1.00 101.87 ? 215 ALA D C   1 
ATOM   4589 O O   . ALA B 2 85  ? 134.554 158.806 109.588 1.00 99.25  ? 215 ALA D O   1 
ATOM   4590 C CB  . ALA B 2 85  ? 132.331 160.324 107.846 1.00 99.59  ? 215 ALA D CB  1 
ATOM   4591 N N   . GLU B 2 86  ? 133.159 159.935 110.995 1.00 103.81 ? 216 GLU D N   1 
ATOM   4592 C CA  . GLU B 2 86  ? 134.195 160.142 112.041 1.00 101.98 ? 216 GLU D CA  1 
ATOM   4593 C C   . GLU B 2 86  ? 134.641 158.791 112.619 1.00 97.54  ? 216 GLU D C   1 
ATOM   4594 O O   . GLU B 2 86  ? 135.853 158.632 112.879 1.00 91.33  ? 216 GLU D O   1 
ATOM   4595 C CB  . GLU B 2 86  ? 133.630 161.025 113.153 1.00 99.66  ? 216 GLU D CB  1 
ATOM   4596 C CG  . GLU B 2 86  ? 134.531 161.105 114.383 1.00 97.87  ? 216 GLU D CG  1 
ATOM   4597 C CD  . GLU B 2 86  ? 133.881 161.771 115.581 1.00 98.13  ? 216 GLU D CD  1 
ATOM   4598 O OE1 . GLU B 2 86  ? 132.711 162.190 115.462 1.00 94.08  ? 216 GLU D OE1 1 
ATOM   4599 O OE2 . GLU B 2 86  ? 134.544 161.867 116.636 1.00 100.71 ? 216 GLU D OE2 1 
ATOM   4600 N N   . ASP B 2 87  ? 133.708 157.852 112.793 1.00 99.14  ? 217 ASP D N   1 
ATOM   4601 C CA  . ASP B 2 87  ? 134.043 156.554 113.445 1.00 95.82  ? 217 ASP D CA  1 
ATOM   4602 C C   . ASP B 2 87  ? 134.957 155.707 112.550 1.00 95.51  ? 217 ASP D C   1 
ATOM   4603 O O   . ASP B 2 87  ? 135.524 154.718 113.062 1.00 91.86  ? 217 ASP D O   1 
ATOM   4604 C CB  . ASP B 2 87  ? 132.782 155.806 113.845 1.00 97.54  ? 217 ASP D CB  1 
ATOM   4605 C CG  . ASP B 2 87  ? 131.760 156.632 114.611 1.00 99.50  ? 217 ASP D CG  1 
ATOM   4606 O OD1 . ASP B 2 87  ? 132.008 157.841 114.805 1.00 100.32 ? 217 ASP D OD1 1 
ATOM   4607 O OD2 . ASP B 2 87  ? 130.730 156.058 115.013 1.00 97.96  ? 217 ASP D OD2 1 
ATOM   4608 N N   . VAL B 2 88  ? 135.100 156.074 111.273 1.00 97.64  ? 218 VAL D N   1 
ATOM   4609 C CA  . VAL B 2 88  ? 136.026 155.330 110.365 1.00 96.98  ? 218 VAL D CA  1 
ATOM   4610 C C   . VAL B 2 88  ? 137.447 155.422 110.949 1.00 93.57  ? 218 VAL D C   1 
ATOM   4611 O O   . VAL B 2 88  ? 137.768 156.460 111.573 1.00 92.00  ? 218 VAL D O   1 
ATOM   4612 C CB  . VAL B 2 88  ? 135.974 155.839 108.910 1.00 99.53  ? 218 VAL D CB  1 
ATOM   4613 C CG1 . VAL B 2 88  ? 137.008 155.157 108.021 1.00 94.55  ? 218 VAL D CG1 1 
ATOM   4614 C CG2 . VAL B 2 88  ? 134.581 155.691 108.311 1.00 98.74  ? 218 VAL D CG2 1 
ATOM   4615 N N   . GLY B 2 89  ? 138.252 154.370 110.776 1.00 90.61  ? 219 GLY D N   1 
ATOM   4616 C CA  . GLY B 2 89  ? 139.618 154.357 111.334 1.00 83.76  ? 219 GLY D CA  1 
ATOM   4617 C C   . GLY B 2 89  ? 139.968 152.992 111.890 1.00 80.86  ? 219 GLY D C   1 
ATOM   4618 O O   . GLY B 2 89  ? 139.252 152.025 111.563 1.00 86.02  ? 219 GLY D O   1 
ATOM   4619 N N   . VAL B 2 90  ? 141.027 152.907 112.700 1.00 70.59  ? 220 VAL D N   1 
ATOM   4620 C CA  . VAL B 2 90  ? 141.456 151.630 113.257 1.00 67.68  ? 220 VAL D CA  1 
ATOM   4621 C C   . VAL B 2 90  ? 141.262 151.679 114.765 1.00 60.11  ? 220 VAL D C   1 
ATOM   4622 O O   . VAL B 2 90  ? 141.654 152.655 115.414 1.00 61.31  ? 220 VAL D O   1 
ATOM   4623 C CB  . VAL B 2 90  ? 142.922 151.316 112.905 1.00 70.19  ? 220 VAL D CB  1 
ATOM   4624 C CG1 . VAL B 2 90  ? 143.182 149.822 113.001 1.00 68.01  ? 220 VAL D CG1 1 
ATOM   4625 C CG2 . VAL B 2 90  ? 143.264 151.835 111.516 1.00 73.38  ? 220 VAL D CG2 1 
ATOM   4626 N N   . TYR B 2 91  ? 140.647 150.613 115.291 1.00 56.00  ? 221 TYR D N   1 
ATOM   4627 C CA  . TYR B 2 91  ? 140.406 150.513 116.753 1.00 52.47  ? 221 TYR D CA  1 
ATOM   4628 C C   . TYR B 2 91  ? 141.389 149.505 117.316 1.00 47.24  ? 221 TYR D C   1 
ATOM   4629 O O   . TYR B 2 91  ? 141.498 148.387 116.771 1.00 54.04  ? 221 TYR D O   1 
ATOM   4630 C CB  . TYR B 2 91  ? 138.961 150.122 117.083 1.00 56.25  ? 221 TYR D CB  1 
ATOM   4631 C CG  . TYR B 2 91  ? 137.912 151.156 116.696 1.00 61.45  ? 221 TYR D CG  1 
ATOM   4632 C CD1 . TYR B 2 91  ? 137.954 151.801 115.466 1.00 65.85  ? 221 TYR D CD1 1 
ATOM   4633 C CD2 . TYR B 2 91  ? 136.900 151.512 117.578 1.00 64.55  ? 221 TYR D CD2 1 
ATOM   4634 C CE1 . TYR B 2 91  ? 137.007 152.744 115.111 1.00 69.77  ? 221 TYR D CE1 1 
ATOM   4635 C CE2 . TYR B 2 91  ? 135.951 152.462 117.239 1.00 71.47  ? 221 TYR D CE2 1 
ATOM   4636 C CZ  . TYR B 2 91  ? 136.003 153.078 116.001 1.00 75.53  ? 221 TYR D CZ  1 
ATOM   4637 O OH  . TYR B 2 91  ? 135.076 154.016 115.650 1.00 79.37  ? 221 TYR D OH  1 
ATOM   4638 N N   . TYR B 2 92  ? 142.125 149.896 118.363 1.00 39.10  ? 222 TYR D N   1 
ATOM   4639 C CA  . TYR B 2 92  ? 143.159 149.021 118.978 1.00 42.22  ? 222 TYR D CA  1 
ATOM   4640 C C   . TYR B 2 92  ? 142.755 148.681 120.402 1.00 40.47  ? 222 TYR D C   1 
ATOM   4641 O O   . TYR B 2 92  ? 142.885 149.562 121.280 1.00 41.92  ? 222 TYR D O   1 
ATOM   4642 C CB  . TYR B 2 92  ? 144.520 149.722 118.968 1.00 42.35  ? 222 TYR D CB  1 
ATOM   4643 C CG  . TYR B 2 92  ? 145.100 149.986 117.586 1.00 45.76  ? 222 TYR D CG  1 
ATOM   4644 C CD1 . TYR B 2 92  ? 146.015 149.112 117.011 1.00 48.85  ? 222 TYR D CD1 1 
ATOM   4645 C CD2 . TYR B 2 92  ? 144.726 151.107 116.856 1.00 48.81  ? 222 TYR D CD2 1 
ATOM   4646 C CE1 . TYR B 2 92  ? 146.547 149.351 115.755 1.00 52.40  ? 222 TYR D CE1 1 
ATOM   4647 C CE2 . TYR B 2 92  ? 145.250 151.356 115.599 1.00 50.07  ? 222 TYR D CE2 1 
ATOM   4648 C CZ  . TYR B 2 92  ? 146.161 150.474 115.047 1.00 50.36  ? 222 TYR D CZ  1 
ATOM   4649 O OH  . TYR B 2 92  ? 146.680 150.717 113.808 1.00 51.99  ? 222 TYR D OH  1 
ATOM   4650 N N   . CYS B 2 93  ? 142.279 147.457 120.642 1.00 42.60  ? 223 CYS D N   1 
ATOM   4651 C CA  . CYS B 2 93  ? 141.949 147.003 121.988 1.00 44.07  ? 223 CYS D CA  1 
ATOM   4652 C C   . CYS B 2 93  ? 143.235 146.963 122.797 1.00 38.72  ? 223 CYS D C   1 
ATOM   4653 O O   . CYS B 2 93  ? 144.048 146.049 122.659 1.00 48.69  ? 223 CYS D O   1 
ATOM   4654 C CB  . CYS B 2 93  ? 141.271 145.639 121.949 1.00 57.04  ? 223 CYS D CB  1 
ATOM   4655 S SG  . CYS B 2 93  ? 142.130 144.403 120.961 1.00 75.61  ? 223 CYS D SG  1 
ATOM   4656 N N   . PHE B 2 94  ? 143.432 148.004 123.608 1.00 30.93  ? 224 PHE D N   1 
ATOM   4657 C CA  . PHE B 2 94  ? 144.702 148.115 124.369 1.00 33.81  ? 224 PHE D CA  1 
ATOM   4658 C C   . PHE B 2 94  ? 144.533 147.542 125.767 1.00 39.32  ? 224 PHE D C   1 
ATOM   4659 O O   . PHE B 2 94  ? 143.426 147.626 126.338 1.00 44.81  ? 224 PHE D O   1 
ATOM   4660 C CB  . PHE B 2 94  ? 145.109 149.591 124.386 1.00 35.98  ? 224 PHE D CB  1 
ATOM   4661 C CG  . PHE B 2 94  ? 146.187 149.934 125.403 1.00 34.74  ? 224 PHE D CG  1 
ATOM   4662 C CD1 . PHE B 2 94  ? 147.532 149.792 125.087 1.00 39.55  ? 224 PHE D CD1 1 
ATOM   4663 C CD2 . PHE B 2 94  ? 145.852 150.400 126.669 1.00 33.91  ? 224 PHE D CD2 1 
ATOM   4664 C CE1 . PHE B 2 94  ? 148.512 150.103 126.014 1.00 41.27  ? 224 PHE D CE1 1 
ATOM   4665 C CE2 . PHE B 2 94  ? 146.837 150.707 127.592 1.00 34.37  ? 224 PHE D CE2 1 
ATOM   4666 C CZ  . PHE B 2 94  ? 148.163 150.561 127.262 1.00 38.29  ? 224 PHE D CZ  1 
ATOM   4667 N N   . GLN B 2 95  ? 145.610 146.970 126.305 1.00 41.07  ? 225 GLN D N   1 
ATOM   4668 C CA  . GLN B 2 95  ? 145.598 146.409 127.681 1.00 43.43  ? 225 GLN D CA  1 
ATOM   4669 C C   . GLN B 2 95  ? 146.728 147.096 128.464 1.00 46.03  ? 225 GLN D C   1 
ATOM   4670 O O   . GLN B 2 95  ? 147.804 147.325 127.875 1.00 51.71  ? 225 GLN D O   1 
ATOM   4671 C CB  . GLN B 2 95  ? 145.761 144.889 127.678 1.00 47.11  ? 225 GLN D CB  1 
ATOM   4672 C CG  . GLN B 2 95  ? 147.116 144.389 127.186 1.00 48.21  ? 225 GLN D CG  1 
ATOM   4673 C CD  . GLN B 2 95  ? 148.144 144.244 128.287 1.00 52.21  ? 225 GLN D CD  1 
ATOM   4674 O OE1 . GLN B 2 95  ? 147.869 144.490 129.466 1.00 53.13  ? 225 GLN D OE1 1 
ATOM   4675 N NE2 . GLN B 2 95  ? 149.347 143.836 127.910 1.00 54.65  ? 225 GLN D NE2 1 
ATOM   4676 N N   . GLY B 2 96  ? 146.486 147.434 129.730 1.00 45.08  ? 226 GLY D N   1 
ATOM   4677 C CA  . GLY B 2 96  ? 147.533 148.073 130.548 1.00 46.51  ? 226 GLY D CA  1 
ATOM   4678 C C   . GLY B 2 96  ? 147.775 147.292 131.820 1.00 55.60  ? 226 GLY D C   1 
ATOM   4679 O O   . GLY B 2 96  ? 148.803 147.546 132.478 1.00 57.52  ? 226 GLY D O   1 
ATOM   4680 N N   . SER B 2 97  ? 146.877 146.361 132.147 1.00 56.45  ? 227 SER D N   1 
ATOM   4681 C CA  . SER B 2 97  ? 146.991 145.600 133.419 1.00 64.09  ? 227 SER D CA  1 
ATOM   4682 C C   . SER B 2 97  ? 148.318 144.829 133.467 1.00 65.73  ? 227 SER D C   1 
ATOM   4683 O O   . SER B 2 97  ? 148.896 144.722 134.569 1.00 69.54  ? 227 SER D O   1 
ATOM   4684 C CB  . SER B 2 97  ? 145.818 144.676 133.595 1.00 70.04  ? 227 SER D CB  1 
ATOM   4685 O OG  . SER B 2 97  ? 146.014 143.820 134.712 1.00 76.91  ? 227 SER D OG  1 
ATOM   4686 N N   . HIS B 2 98  ? 148.773 144.306 132.326 1.00 63.27  ? 228 HIS D N   1 
ATOM   4687 C CA  . HIS B 2 98  ? 150.019 143.490 132.298 1.00 62.85  ? 228 HIS D CA  1 
ATOM   4688 C C   . HIS B 2 98  ? 151.220 144.439 132.236 1.00 60.77  ? 228 HIS D C   1 
ATOM   4689 O O   . HIS B 2 98  ? 151.106 145.497 131.584 1.00 59.57  ? 228 HIS D O   1 
ATOM   4690 C CB  . HIS B 2 98  ? 149.918 142.456 131.173 1.00 64.35  ? 228 HIS D CB  1 
ATOM   4691 C CG  . HIS B 2 98  ? 148.636 141.690 131.247 1.00 70.88  ? 228 HIS D CG  1 
ATOM   4692 N ND1 . HIS B 2 98  ? 147.502 142.055 130.553 1.00 69.98  ? 228 HIS D ND1 1 
ATOM   4693 C CD2 . HIS B 2 98  ? 148.307 140.589 131.936 1.00 74.95  ? 228 HIS D CD2 1 
ATOM   4694 C CE1 . HIS B 2 98  ? 146.530 141.194 130.819 1.00 71.93  ? 228 HIS D CE1 1 
ATOM   4695 N NE2 . HIS B 2 98  ? 146.997 140.296 131.657 1.00 75.36  ? 228 HIS D NE2 1 
ATOM   4696 N N   . ILE B 2 99  ? 152.338 144.075 132.876 1.00 62.77  ? 229 ILE D N   1 
ATOM   4697 C CA  . ILE B 2 99  ? 153.459 145.017 132.955 1.00 63.42  ? 229 ILE D CA  1 
ATOM   4698 C C   . ILE B 2 99  ? 153.813 145.625 131.602 1.00 56.00  ? 229 ILE D C   1 
ATOM   4699 O O   . ILE B 2 99  ? 153.913 146.860 131.515 1.00 50.66  ? 229 ILE D O   1 
ATOM   4700 C CB  . ILE B 2 99  ? 154.663 144.349 133.643 1.00 66.96  ? 229 ILE D CB  1 
ATOM   4701 C CG1 . ILE B 2 99  ? 154.196 143.492 134.823 1.00 64.25  ? 229 ILE D CG1 1 
ATOM   4702 C CG2 . ILE B 2 99  ? 155.664 145.397 134.103 1.00 66.92  ? 229 ILE D CG2 1 
ATOM   4703 C CD1 . ILE B 2 99  ? 153.679 144.294 135.997 1.00 58.31  ? 229 ILE D CD1 1 
ATOM   4704 N N   . PRO B 2 100 ? 154.020 144.857 130.532 1.00 55.09  ? 230 PRO D N   1 
ATOM   4705 C CA  . PRO B 2 100 ? 154.206 145.479 129.221 1.00 50.21  ? 230 PRO D CA  1 
ATOM   4706 C C   . PRO B 2 100 ? 152.873 145.685 128.525 1.00 51.28  ? 230 PRO D C   1 
ATOM   4707 O O   . PRO B 2 100 ? 152.171 144.711 128.214 1.00 54.38  ? 230 PRO D O   1 
ATOM   4708 C CB  . PRO B 2 100 ? 155.082 144.467 128.469 1.00 48.32  ? 230 PRO D CB  1 
ATOM   4709 C CG  . PRO B 2 100 ? 154.806 143.151 129.122 1.00 55.56  ? 230 PRO D CG  1 
ATOM   4710 C CD  . PRO B 2 100 ? 154.106 143.387 130.438 1.00 56.87  ? 230 PRO D CD  1 
ATOM   4711 N N   . PRO B 2 101 ? 152.484 146.933 128.270 1.00 46.27  ? 231 PRO D N   1 
ATOM   4712 C CA  . PRO B 2 101 ? 151.255 147.174 127.508 1.00 42.64  ? 231 PRO D CA  1 
ATOM   4713 C C   . PRO B 2 101 ? 151.353 146.581 126.112 1.00 44.35  ? 231 PRO D C   1 
ATOM   4714 O O   . PRO B 2 101 ? 152.420 146.572 125.495 1.00 44.51  ? 231 PRO D O   1 
ATOM   4715 C CB  . PRO B 2 101 ? 151.162 148.701 127.467 1.00 32.60  ? 231 PRO D CB  1 
ATOM   4716 C CG  . PRO B 2 101 ? 151.903 149.145 128.673 1.00 34.18  ? 231 PRO D CG  1 
ATOM   4717 C CD  . PRO B 2 101 ? 153.042 148.181 128.814 1.00 40.05  ? 231 PRO D CD  1 
ATOM   4718 N N   . THR B 2 102 ? 150.227 146.076 125.616 1.00 42.62  ? 232 THR D N   1 
ATOM   4719 C CA  . THR B 2 102 ? 150.183 145.456 124.300 1.00 46.27  ? 232 THR D CA  1 
ATOM   4720 C C   . THR B 2 102 ? 148.880 145.829 123.614 1.00 43.63  ? 232 THR D C   1 
ATOM   4721 O O   . THR B 2 102 ? 147.803 145.673 124.196 1.00 42.57  ? 232 THR D O   1 
ATOM   4722 C CB  . THR B 2 102 ? 150.311 143.932 124.400 1.00 55.41  ? 232 THR D CB  1 
ATOM   4723 O OG1 . THR B 2 102 ? 151.691 143.577 124.550 1.00 65.93  ? 232 THR D OG1 1 
ATOM   4724 C CG2 . THR B 2 102 ? 149.771 143.269 123.146 1.00 58.83  ? 232 THR D CG2 1 
ATOM   4725 N N   . PHE B 2 103 ? 148.998 146.321 122.379 1.00 43.60  ? 233 PHE D N   1 
ATOM   4726 C CA  . PHE B 2 103 ? 147.792 146.690 121.594 1.00 42.42  ? 233 PHE D CA  1 
ATOM   4727 C C   . PHE B 2 103 ? 147.281 145.465 120.851 1.00 45.47  ? 233 PHE D C   1 
ATOM   4728 O O   . PHE B 2 103 ? 148.004 144.450 120.761 1.00 51.52  ? 233 PHE D O   1 
ATOM   4729 C CB  . PHE B 2 103 ? 148.128 147.807 120.603 1.00 43.37  ? 233 PHE D CB  1 
ATOM   4730 C CG  . PHE B 2 103 ? 148.212 149.207 121.196 1.00 41.78  ? 233 PHE D CG  1 
ATOM   4731 C CD1 . PHE B 2 103 ? 149.398 149.682 121.745 1.00 40.63  ? 233 PHE D CD1 1 
ATOM   4732 C CD2 . PHE B 2 103 ? 147.110 150.053 121.180 1.00 41.37  ? 233 PHE D CD2 1 
ATOM   4733 C CE1 . PHE B 2 103 ? 149.471 150.961 122.272 1.00 38.96  ? 233 PHE D CE1 1 
ATOM   4734 C CE2 . PHE B 2 103 ? 147.189 151.331 121.708 1.00 41.87  ? 233 PHE D CE2 1 
ATOM   4735 C CZ  . PHE B 2 103 ? 148.367 151.782 122.251 1.00 39.36  ? 233 PHE D CZ  1 
ATOM   4736 N N   . GLY B 2 104 ? 146.067 145.559 120.316 1.00 47.65  ? 234 GLY D N   1 
ATOM   4737 C CA  . GLY B 2 104 ? 145.450 144.456 119.552 1.00 55.13  ? 234 GLY D CA  1 
ATOM   4738 C C   . GLY B 2 104 ? 145.961 144.419 118.125 1.00 60.16  ? 234 GLY D C   1 
ATOM   4739 O O   . GLY B 2 104 ? 146.833 145.251 117.793 1.00 57.44  ? 234 GLY D O   1 
ATOM   4740 N N   . GLN B 2 105 ? 145.440 143.507 117.300 1.00 66.46  ? 235 GLN D N   1 
ATOM   4741 C CA  . GLN B 2 105 ? 145.899 143.346 115.894 1.00 69.14  ? 235 GLN D CA  1 
ATOM   4742 C C   . GLN B 2 105 ? 145.605 144.632 115.107 1.00 67.70  ? 235 GLN D C   1 
ATOM   4743 O O   . GLN B 2 105 ? 146.469 145.022 114.291 1.00 67.00  ? 235 GLN D O   1 
ATOM   4744 C CB  . GLN B 2 105 ? 145.254 142.108 115.268 1.00 70.82  ? 235 GLN D CB  1 
ATOM   4745 C CG  . GLN B 2 105 ? 143.768 142.264 114.955 1.00 71.51  ? 235 GLN D CG  1 
ATOM   4746 C CD  . GLN B 2 105 ? 143.077 140.964 114.608 1.00 75.78  ? 235 GLN D CD  1 
ATOM   4747 O OE1 . GLN B 2 105 ? 143.703 139.901 114.555 1.00 76.13  ? 235 GLN D OE1 1 
ATOM   4748 N NE2 . GLN B 2 105 ? 141.775 141.027 114.369 1.00 78.58  ? 235 GLN D NE2 1 
ATOM   4749 N N   . GLY B 2 106 ? 144.447 145.260 115.340 1.00 65.21  ? 236 GLY D N   1 
ATOM   4750 C CA  . GLY B 2 106 ? 144.042 146.487 114.624 1.00 64.76  ? 236 GLY D CA  1 
ATOM   4751 C C   . GLY B 2 106 ? 142.818 146.235 113.766 1.00 69.72  ? 236 GLY D C   1 
ATOM   4752 O O   . GLY B 2 106 ? 143.003 145.776 112.622 1.00 74.89  ? 236 GLY D O   1 
ATOM   4753 N N   . THR B 2 107 ? 141.617 146.541 114.269 1.00 64.14  ? 237 THR D N   1 
ATOM   4754 C CA  . THR B 2 107 ? 140.364 146.344 113.543 1.00 68.60  ? 237 THR D CA  1 
ATOM   4755 C C   . THR B 2 107 ? 140.057 147.634 112.789 1.00 70.53  ? 237 THR D C   1 
ATOM   4756 O O   . THR B 2 107 ? 139.395 148.533 113.310 1.00 74.02  ? 237 THR D O   1 
ATOM   4757 C CB  . THR B 2 107 ? 139.226 145.969 114.486 1.00 70.57  ? 237 THR D CB  1 
ATOM   4758 O OG1 . THR B 2 107 ? 139.703 145.046 115.470 1.00 69.54  ? 237 THR D OG1 1 
ATOM   4759 C CG2 . THR B 2 107 ? 138.085 145.331 113.712 1.00 78.62  ? 237 THR D CG2 1 
ATOM   4760 N N   . LYS B 2 108 ? 140.538 147.716 111.554 1.00 74.98  ? 238 LYS D N   1 
ATOM   4761 C CA  . LYS B 2 108 ? 140.336 148.899 110.722 1.00 79.97  ? 238 LYS D CA  1 
ATOM   4762 C C   . LYS B 2 108 ? 138.878 148.951 110.286 1.00 85.70  ? 238 LYS D C   1 
ATOM   4763 O O   . LYS B 2 108 ? 138.469 148.263 109.349 1.00 91.02  ? 238 LYS D O   1 
ATOM   4764 C CB  . LYS B 2 108 ? 141.272 148.868 109.520 1.00 83.91  ? 238 LYS D CB  1 
ATOM   4765 C CG  . LYS B 2 108 ? 141.037 149.986 108.516 1.00 88.68  ? 238 LYS D CG  1 
ATOM   4766 C CD  . LYS B 2 108 ? 142.148 150.041 107.480 1.00 93.45  ? 238 LYS D CD  1 
ATOM   4767 C CE  . LYS B 2 108 ? 142.100 151.337 106.689 1.00 94.02  ? 238 LYS D CE  1 
ATOM   4768 N NZ  . LYS B 2 108 ? 142.477 152.511 107.523 1.00 89.78  ? 238 LYS D NZ  1 
ATOM   4769 N N   . VAL B 2 109 ? 138.104 149.786 110.987 1.00 85.21  ? 239 VAL D N   1 
ATOM   4770 C CA  . VAL B 2 109 ? 136.659 149.951 110.653 1.00 90.89  ? 239 VAL D CA  1 
ATOM   4771 C C   . VAL B 2 109 ? 136.548 150.724 109.333 1.00 96.43  ? 239 VAL D C   1 
ATOM   4772 O O   . VAL B 2 109 ? 137.126 151.829 109.245 1.00 92.26  ? 239 VAL D O   1 
ATOM   4773 C CB  . VAL B 2 109 ? 135.906 150.669 111.788 1.00 87.62  ? 239 VAL D CB  1 
ATOM   4774 C CG1 . VAL B 2 109 ? 134.461 150.970 111.412 1.00 94.39  ? 239 VAL D CG1 1 
ATOM   4775 C CG2 . VAL B 2 109 ? 135.972 149.883 113.091 1.00 78.31  ? 239 VAL D CG2 1 
ATOM   4776 N N   . GLU B 2 110 ? 135.842 150.159 108.354 1.00 102.58 ? 240 GLU D N   1 
ATOM   4777 C CA  . GLU B 2 110 ? 135.663 150.799 107.058 1.00 104.75 ? 240 GLU D CA  1 
ATOM   4778 C C   . GLU B 2 110 ? 134.182 150.876 106.712 1.00 108.02 ? 240 GLU D C   1 
ATOM   4779 O O   . GLU B 2 110 ? 133.327 150.630 107.569 1.00 107.38 ? 240 GLU D O   1 
ATOM   4780 C CB  . GLU B 2 110 ? 136.433 150.038 105.976 1.00 102.82 ? 240 GLU D CB  1 
ATOM   4781 C CG  . GLU B 2 110 ? 137.941 150.056 106.171 1.00 99.08  ? 240 GLU D CG  1 
ATOM   4782 C CD  . GLU B 2 110 ? 138.550 148.668 106.123 1.00 99.41  ? 240 GLU D CD  1 
ATOM   4783 O OE1 . GLU B 2 110 ? 137.861 147.700 106.508 1.00 99.53  ? 240 GLU D OE1 1 
ATOM   4784 O OE2 . GLU B 2 110 ? 139.723 148.546 105.710 1.00 99.54  ? 240 GLU D OE2 1 
ATOM   4785 N N   . ILE B 2 111 ? 133.867 151.223 105.467 1.00 109.37 ? 241 ILE D N   1 
ATOM   4786 C CA  . ILE B 2 111 ? 132.491 151.331 104.999 1.00 109.99 ? 241 ILE D CA  1 
ATOM   4787 C C   . ILE B 2 111 ? 132.270 150.292 103.909 1.00 111.10 ? 241 ILE D C   1 
ATOM   4788 O O   . ILE B 2 111 ? 133.047 150.216 102.950 1.00 109.84 ? 241 ILE D O   1 
ATOM   4789 C CB  . ILE B 2 111 ? 132.176 152.745 104.477 1.00 109.12 ? 241 ILE D CB  1 
ATOM   4790 C CG1 . ILE B 2 111 ? 132.833 153.803 105.366 1.00 107.87 ? 241 ILE D CG1 1 
ATOM   4791 C CG2 . ILE B 2 111 ? 130.673 152.960 104.405 1.00 108.97 ? 241 ILE D CG2 1 
ATOM   4792 C CD1 . ILE B 2 111 ? 132.236 153.891 106.755 1.00 107.20 ? 241 ILE D CD1 1 
ATOM   4793 N N   . LYS B 2 112 ? 131.215 149.497 104.058 1.00 114.11 ? 242 LYS D N   1 
ATOM   4794 C CA  . LYS B 2 112 ? 130.877 148.478 103.071 1.00 114.22 ? 242 LYS D CA  1 
ATOM   4795 C C   . LYS B 2 112 ? 129.714 148.934 102.196 1.00 112.98 ? 242 LYS D C   1 
ATOM   4796 O O   . LYS B 2 112 ? 129.733 150.035 101.647 1.00 113.73 ? 242 LYS D O   1 
ATOM   4797 C CB  . LYS B 2 112 ? 130.531 147.154 103.756 1.00 112.44 ? 242 LYS D CB  1 
ATOM   4798 C CG  . LYS B 2 112 ? 129.211 147.163 104.510 1.00 111.70 ? 242 LYS D CG  1 
ATOM   4799 C CD  . LYS B 2 112 ? 129.108 145.971 105.450 1.00 109.33 ? 242 LYS D CD  1 
ATOM   4800 C CE  . LYS B 2 112 ? 127.860 146.048 106.313 1.00 107.45 ? 242 LYS D CE  1 
ATOM   4801 N NZ  . LYS B 2 112 ? 126.798 145.121 105.834 1.00 103.34 ? 242 LYS D NZ  1 
ATOM   4802 N N   . GLN B 2 138 ? 145.314 174.324 126.479 1.00 60.88  ? 268 GLN D N   1 
ATOM   4803 C CA  . GLN B 2 138 ? 145.379 173.053 125.768 1.00 65.09  ? 268 GLN D CA  1 
ATOM   4804 C C   . GLN B 2 138 ? 146.777 172.452 125.850 1.00 64.61  ? 268 GLN D C   1 
ATOM   4805 O O   . GLN B 2 138 ? 147.748 173.152 126.137 1.00 64.52  ? 268 GLN D O   1 
ATOM   4806 C CB  . GLN B 2 138 ? 144.968 173.233 124.306 1.00 65.19  ? 268 GLN D CB  1 
ATOM   4807 C CG  . GLN B 2 138 ? 144.061 172.136 123.778 1.00 64.31  ? 268 GLN D CG  1 
ATOM   4808 C CD  . GLN B 2 138 ? 144.828 171.038 123.072 1.00 65.67  ? 268 GLN D CD  1 
ATOM   4809 O OE1 . GLN B 2 138 ? 145.988 171.217 122.700 1.00 64.45  ? 268 GLN D OE1 1 
ATOM   4810 N NE2 . GLN B 2 138 ? 144.184 169.893 122.882 1.00 63.85  ? 268 GLN D NE2 1 
ATOM   4811 N N   . VAL B 2 139 ? 146.872 171.149 125.597 1.00 64.36  ? 269 VAL D N   1 
ATOM   4812 C CA  . VAL B 2 139 ? 148.131 170.416 125.655 1.00 64.61  ? 269 VAL D CA  1 
ATOM   4813 C C   . VAL B 2 139 ? 148.364 169.749 124.308 1.00 63.29  ? 269 VAL D C   1 
ATOM   4814 O O   . VAL B 2 139 ? 147.496 169.021 123.813 1.00 63.29  ? 269 VAL D O   1 
ATOM   4815 C CB  . VAL B 2 139 ? 148.127 169.368 126.781 1.00 60.65  ? 269 VAL D CB  1 
ATOM   4816 C CG1 . VAL B 2 139 ? 149.316 168.440 126.632 1.00 53.38  ? 269 VAL D CG1 1 
ATOM   4817 C CG2 . VAL B 2 139 ? 148.134 170.047 128.137 1.00 61.39  ? 269 VAL D CG2 1 
ATOM   4818 N N   . GLN B 2 140 ? 149.533 169.992 123.722 1.00 60.03  ? 270 GLN D N   1 
ATOM   4819 C CA  . GLN B 2 140 ? 149.912 169.352 122.473 1.00 61.24  ? 270 GLN D CA  1 
ATOM   4820 C C   . GLN B 2 140 ? 151.392 169.006 122.521 1.00 59.42  ? 270 GLN D C   1 
ATOM   4821 O O   . GLN B 2 140 ? 152.209 169.800 122.997 1.00 58.59  ? 270 GLN D O   1 
ATOM   4822 C CB  . GLN B 2 140 ? 149.619 170.252 121.265 1.00 64.13  ? 270 GLN D CB  1 
ATOM   4823 C CG  . GLN B 2 140 ? 149.693 169.562 119.900 1.00 65.48  ? 270 GLN D CG  1 
ATOM   4824 C CD  . GLN B 2 140 ? 149.436 168.063 119.960 1.00 64.52  ? 270 GLN D CD  1 
ATOM   4825 O OE1 . GLN B 2 140 ? 150.339 167.271 120.231 1.00 63.48  ? 270 GLN D OE1 1 
ATOM   4826 N NE2 . GLN B 2 140 ? 148.193 167.669 119.713 1.00 59.59  ? 270 GLN D NE2 1 
ATOM   4827 N N   . LEU B 2 141 ? 151.726 167.817 122.029 1.00 61.27  ? 271 LEU D N   1 
ATOM   4828 C CA  . LEU B 2 141 ? 153.098 167.325 121.980 1.00 61.77  ? 271 LEU D CA  1 
ATOM   4829 C C   . LEU B 2 141 ? 153.521 167.267 120.518 1.00 63.16  ? 271 LEU D C   1 
ATOM   4830 O O   . LEU B 2 141 ? 153.041 166.416 119.762 1.00 65.60  ? 271 LEU D O   1 
ATOM   4831 C CB  . LEU B 2 141 ? 153.211 165.952 122.640 1.00 57.64  ? 271 LEU D CB  1 
ATOM   4832 C CG  . LEU B 2 141 ? 153.228 165.861 124.168 1.00 51.00  ? 271 LEU D CG  1 
ATOM   4833 C CD1 . LEU B 2 141 ? 151.867 166.160 124.766 1.00 48.43  ? 271 LEU D CD1 1 
ATOM   4834 C CD2 . LEU B 2 141 ? 153.683 164.484 124.584 1.00 44.70  ? 271 LEU D CD2 1 
ATOM   4835 N N   . VAL B 2 142 ? 154.416 168.166 120.121 1.00 62.88  ? 272 VAL D N   1 
ATOM   4836 C CA  . VAL B 2 142 ? 154.863 168.270 118.737 1.00 65.43  ? 272 VAL D CA  1 
ATOM   4837 C C   . VAL B 2 142 ? 156.138 167.453 118.578 1.00 64.05  ? 272 VAL D C   1 
ATOM   4838 O O   . VAL B 2 142 ? 157.114 167.657 119.310 1.00 64.02  ? 272 VAL D O   1 
ATOM   4839 C CB  . VAL B 2 142 ? 155.080 169.734 118.323 1.00 65.94  ? 272 VAL D CB  1 
ATOM   4840 C CG1 . VAL B 2 142 ? 153.763 170.492 118.365 1.00 62.45  ? 272 VAL D CG1 1 
ATOM   4841 C CG2 . VAL B 2 142 ? 156.094 170.399 119.235 1.00 64.23  ? 272 VAL D CG2 1 
ATOM   4842 N N   . GLN B 2 143 ? 156.125 166.528 117.624 1.00 61.33  ? 273 GLN D N   1 
ATOM   4843 C CA  . GLN B 2 143 ? 157.246 165.637 117.377 1.00 60.68  ? 273 GLN D CA  1 
ATOM   4844 C C   . GLN B 2 143 ? 158.227 166.285 116.402 1.00 66.10  ? 273 GLN D C   1 
ATOM   4845 O O   . GLN B 2 143 ? 158.142 167.476 116.093 1.00 68.71  ? 273 GLN D O   1 
ATOM   4846 C CB  . GLN B 2 143 ? 156.738 164.294 116.858 1.00 61.02  ? 273 GLN D CB  1 
ATOM   4847 C CG  . GLN B 2 143 ? 156.827 163.163 117.863 1.00 57.89  ? 273 GLN D CG  1 
ATOM   4848 C CD  . GLN B 2 143 ? 156.261 161.864 117.328 1.00 54.68  ? 273 GLN D CD  1 
ATOM   4849 O OE1 . GLN B 2 143 ? 156.914 161.154 116.568 1.00 52.27  ? 273 GLN D OE1 1 
ATOM   4850 N NE2 . GLN B 2 143 ? 155.043 161.541 117.737 1.00 52.08  ? 273 GLN D NE2 1 
ATOM   4851 N N   . SER B 2 144 ? 159.178 165.496 115.913 1.00 67.33  ? 274 SER D N   1 
ATOM   4852 C CA  . SER B 2 144 ? 160.154 165.949 114.936 1.00 70.29  ? 274 SER D CA  1 
ATOM   4853 C C   . SER B 2 144 ? 159.623 165.684 113.528 1.00 73.84  ? 274 SER D C   1 
ATOM   4854 O O   . SER B 2 144 ? 158.436 165.414 113.327 1.00 74.01  ? 274 SER D O   1 
ATOM   4855 C CB  . SER B 2 144 ? 161.497 165.263 115.175 1.00 68.05  ? 274 SER D CB  1 
ATOM   4856 O OG  . SER B 2 144 ? 161.666 164.161 114.302 1.00 68.88  ? 274 SER D OG  1 
ATOM   4857 N N   . GLY B 2 145 ? 160.498 165.781 112.531 1.00 73.78  ? 275 GLY D N   1 
ATOM   4858 C CA  . GLY B 2 145 ? 160.149 165.447 111.170 1.00 71.30  ? 275 GLY D CA  1 
ATOM   4859 C C   . GLY B 2 145 ? 160.562 164.031 110.812 1.00 71.16  ? 275 GLY D C   1 
ATOM   4860 O O   . GLY B 2 145 ? 161.459 163.452 111.419 1.00 68.93  ? 275 GLY D O   1 
ATOM   4861 N N   . ALA B 2 146 ? 159.885 163.475 109.811 1.00 74.24  ? 276 ALA D N   1 
ATOM   4862 C CA  . ALA B 2 146 ? 160.198 162.130 109.353 1.00 73.40  ? 276 ALA D CA  1 
ATOM   4863 C C   . ALA B 2 146 ? 161.593 162.086 108.743 1.00 73.97  ? 276 ALA D C   1 
ATOM   4864 O O   . ALA B 2 146 ? 162.015 163.015 108.049 1.00 75.83  ? 276 ALA D O   1 
ATOM   4865 C CB  . ALA B 2 146 ? 159.163 161.660 108.332 1.00 67.75  ? 276 ALA D CB  1 
ATOM   4866 N N   . GLU B 2 147 ? 162.313 160.998 109.008 1.00 73.41  ? 277 GLU D N   1 
ATOM   4867 C CA  . GLU B 2 147 ? 163.668 160.833 108.507 1.00 77.54  ? 277 GLU D CA  1 
ATOM   4868 C C   . GLU B 2 147 ? 163.848 159.420 107.975 1.00 77.67  ? 277 GLU D C   1 
ATOM   4869 O O   . GLU B 2 147 ? 163.174 158.484 108.411 1.00 76.76  ? 277 GLU D O   1 
ATOM   4870 C CB  . GLU B 2 147 ? 164.714 161.117 109.594 1.00 74.27  ? 277 GLU D CB  1 
ATOM   4871 C CG  . GLU B 2 147 ? 164.533 160.301 110.862 1.00 69.92  ? 277 GLU D CG  1 
ATOM   4872 C CD  . GLU B 2 147 ? 163.666 161.003 111.887 1.00 69.97  ? 277 GLU D CD  1 
ATOM   4873 O OE1 . GLU B 2 147 ? 162.429 160.850 111.822 1.00 70.64  ? 277 GLU D OE1 1 
ATOM   4874 O OE2 . GLU B 2 147 ? 164.220 161.706 112.757 1.00 65.54  ? 277 GLU D OE2 1 
ATOM   4875 N N   . VAL B 2 148 ? 164.765 159.279 107.022 1.00 79.75  ? 278 VAL D N   1 
ATOM   4876 C CA  . VAL B 2 148 ? 165.115 157.990 106.437 1.00 83.19  ? 278 VAL D CA  1 
ATOM   4877 C C   . VAL B 2 148 ? 166.588 157.741 106.720 1.00 86.04  ? 278 VAL D C   1 
ATOM   4878 O O   . VAL B 2 148 ? 167.444 158.544 106.329 1.00 88.23  ? 278 VAL D O   1 
ATOM   4879 C CB  . VAL B 2 148 ? 164.828 157.947 104.929 1.00 82.77  ? 278 VAL D CB  1 
ATOM   4880 C CG1 . VAL B 2 148 ? 165.477 156.723 104.300 1.00 78.85  ? 278 VAL D CG1 1 
ATOM   4881 C CG2 . VAL B 2 148 ? 163.329 157.953 104.675 1.00 79.89  ? 278 VAL D CG2 1 
ATOM   4882 N N   . LYS B 2 149 ? 166.883 156.636 107.394 1.00 85.96  ? 279 LYS D N   1 
ATOM   4883 C CA  . LYS B 2 149 ? 168.240 156.296 107.797 1.00 85.19  ? 279 LYS D CA  1 
ATOM   4884 C C   . LYS B 2 149 ? 168.658 154.978 107.146 1.00 88.81  ? 279 LYS D C   1 
ATOM   4885 O O   . LYS B 2 149 ? 167.947 154.415 106.309 1.00 89.04  ? 279 LYS D O   1 
ATOM   4886 C CB  . LYS B 2 149 ? 168.347 156.227 109.323 1.00 81.66  ? 279 LYS D CB  1 
ATOM   4887 C CG  . LYS B 2 149 ? 167.358 157.111 110.066 1.00 80.10  ? 279 LYS D CG  1 
ATOM   4888 C CD  . LYS B 2 149 ? 167.694 158.584 109.896 1.00 79.25  ? 279 LYS D CD  1 
ATOM   4889 C CE  . LYS B 2 149 ? 169.103 158.889 110.375 1.00 82.68  ? 279 LYS D CE  1 
ATOM   4890 N NZ  . LYS B 2 149 ? 169.420 160.340 110.276 1.00 86.70  ? 279 LYS D NZ  1 
ATOM   4891 N N   . LYS B 2 150 ? 169.832 154.490 107.541 1.00 91.60  ? 280 LYS D N   1 
ATOM   4892 C CA  . LYS B 2 150 ? 170.401 153.247 107.055 1.00 90.55  ? 280 LYS D CA  1 
ATOM   4893 C C   . LYS B 2 150 ? 170.492 152.227 108.186 1.00 85.82  ? 280 LYS D C   1 
ATOM   4894 O O   . LYS B 2 150 ? 170.608 152.604 109.356 1.00 82.55  ? 280 LYS D O   1 
ATOM   4895 C CB  . LYS B 2 150 ? 171.799 153.472 106.462 1.00 91.31  ? 280 LYS D CB  1 
ATOM   4896 C CG  . LYS B 2 150 ? 171.932 154.742 105.637 1.00 91.10  ? 280 LYS D CG  1 
ATOM   4897 C CD  . LYS B 2 150 ? 172.566 155.866 106.442 1.00 91.62  ? 280 LYS D CD  1 
ATOM   4898 C CE  . LYS B 2 150 ? 172.114 157.227 105.939 1.00 94.84  ? 280 LYS D CE  1 
ATOM   4899 N NZ  . LYS B 2 150 ? 172.935 158.330 106.509 1.00 101.17 ? 280 LYS D NZ  1 
ATOM   4900 N N   . PRO B 2 151 ? 170.426 150.933 107.873 1.00 86.44  ? 281 PRO D N   1 
ATOM   4901 C CA  . PRO B 2 151 ? 170.515 149.917 108.929 1.00 85.13  ? 281 PRO D CA  1 
ATOM   4902 C C   . PRO B 2 151 ? 171.824 150.021 109.698 1.00 82.63  ? 281 PRO D C   1 
ATOM   4903 O O   . PRO B 2 151 ? 172.885 150.282 109.128 1.00 86.36  ? 281 PRO D O   1 
ATOM   4904 C CB  . PRO B 2 151 ? 170.418 148.596 108.159 1.00 87.31  ? 281 PRO D CB  1 
ATOM   4905 C CG  . PRO B 2 151 ? 169.686 148.947 106.909 1.00 91.88  ? 281 PRO D CG  1 
ATOM   4906 C CD  . PRO B 2 151 ? 170.125 150.339 106.560 1.00 90.14  ? 281 PRO D CD  1 
ATOM   4907 N N   . GLY B 2 152 ? 171.736 149.813 111.011 1.00 79.64  ? 282 GLY D N   1 
ATOM   4908 C CA  . GLY B 2 152 ? 172.880 149.912 111.887 1.00 78.87  ? 282 GLY D CA  1 
ATOM   4909 C C   . GLY B 2 152 ? 173.172 151.303 112.407 1.00 77.70  ? 282 GLY D C   1 
ATOM   4910 O O   . GLY B 2 152 ? 174.073 151.457 113.242 1.00 77.26  ? 282 GLY D O   1 
ATOM   4911 N N   . ALA B 2 153 ? 172.444 152.317 111.949 1.00 77.06  ? 283 ALA D N   1 
ATOM   4912 C CA  . ALA B 2 153 ? 172.657 153.684 112.395 1.00 76.11  ? 283 ALA D CA  1 
ATOM   4913 C C   . ALA B 2 153 ? 171.792 153.965 113.623 1.00 74.79  ? 283 ALA D C   1 
ATOM   4914 O O   . ALA B 2 153 ? 171.147 153.069 114.175 1.00 76.41  ? 283 ALA D O   1 
ATOM   4915 C CB  . ALA B 2 153 ? 172.370 154.662 111.258 1.00 77.26  ? 283 ALA D CB  1 
ATOM   4916 N N   . SER B 2 154 ? 171.772 155.220 114.066 1.00 71.91  ? 284 SER D N   1 
ATOM   4917 C CA  . SER B 2 154 ? 170.989 155.633 115.221 1.00 68.81  ? 284 SER D CA  1 
ATOM   4918 C C   . SER B 2 154 ? 170.147 156.847 114.860 1.00 68.94  ? 284 SER D C   1 
ATOM   4919 O O   . SER B 2 154 ? 170.615 157.754 114.165 1.00 71.28  ? 284 SER D O   1 
ATOM   4920 C CB  . SER B 2 154 ? 171.888 155.959 116.418 1.00 69.11  ? 284 SER D CB  1 
ATOM   4921 O OG  . SER B 2 154 ? 171.127 156.460 117.503 1.00 68.29  ? 284 SER D OG  1 
ATOM   4922 N N   . VAL B 2 155 ? 168.867 156.824 115.250 1.00 68.04  ? 285 VAL D N   1 
ATOM   4923 C CA  . VAL B 2 155 ? 167.914 157.922 114.902 1.00 66.03  ? 285 VAL D CA  1 
ATOM   4924 C C   . VAL B 2 155 ? 167.360 158.522 116.202 1.00 62.24  ? 285 VAL D C   1 
ATOM   4925 O O   . VAL B 2 155 ? 166.627 157.807 116.920 1.00 62.51  ? 285 VAL D O   1 
ATOM   4926 C CB  . VAL B 2 155 ? 166.783 157.436 113.970 1.00 68.11  ? 285 VAL D CB  1 
ATOM   4927 C CG1 . VAL B 2 155 ? 166.017 156.239 114.526 1.00 62.05  ? 285 VAL D CG1 1 
ATOM   4928 C CG2 . VAL B 2 155 ? 165.813 158.557 113.616 1.00 63.52  ? 285 VAL D CG2 1 
ATOM   4929 N N   . LYS B 2 156 ? 167.723 159.768 116.510 1.00 60.06  ? 286 LYS D N   1 
ATOM   4930 C CA  . LYS B 2 156 ? 167.153 160.463 117.692 1.00 56.92  ? 286 LYS D CA  1 
ATOM   4931 C C   . LYS B 2 156 ? 165.775 160.980 117.265 1.00 58.39  ? 286 LYS D C   1 
ATOM   4932 O O   . LYS B 2 156 ? 165.698 161.611 116.186 1.00 60.28  ? 286 LYS D O   1 
ATOM   4933 C CB  . LYS B 2 156 ? 168.049 161.603 118.184 1.00 58.81  ? 286 LYS D CB  1 
ATOM   4934 C CG  . LYS B 2 156 ? 167.591 162.261 119.481 1.00 57.87  ? 286 LYS D CG  1 
ATOM   4935 C CD  . LYS B 2 156 ? 167.387 163.765 119.372 1.00 58.01  ? 286 LYS D CD  1 
ATOM   4936 C CE  . LYS B 2 156 ? 166.152 164.120 118.613 1.00 60.27  ? 286 LYS D CE  1 
ATOM   4937 N NZ  . LYS B 2 156 ? 166.150 165.533 118.232 1.00 62.86  ? 286 LYS D NZ  1 
ATOM   4938 N N   . VAL B 2 157 ? 164.737 160.696 118.050 1.00 56.60  ? 287 VAL D N   1 
ATOM   4939 C CA  . VAL B 2 157 ? 163.345 161.127 117.727 1.00 55.01  ? 287 VAL D CA  1 
ATOM   4940 C C   . VAL B 2 157 ? 162.900 162.102 118.821 1.00 53.21  ? 287 VAL D C   1 
ATOM   4941 O O   . VAL B 2 157 ? 162.748 161.643 119.972 1.00 53.59  ? 287 VAL D O   1 
ATOM   4942 C CB  . VAL B 2 157 ? 162.414 159.907 117.627 1.00 49.66  ? 287 VAL D CB  1 
ATOM   4943 C CG1 . VAL B 2 157 ? 161.018 160.304 117.174 1.00 48.09  ? 287 VAL D CG1 1 
ATOM   4944 C CG2 . VAL B 2 157 ? 162.992 158.840 116.706 1.00 50.40  ? 287 VAL D CG2 1 
ATOM   4945 N N   . SER B 2 158 ? 162.692 163.382 118.493 1.00 54.62  ? 288 SER D N   1 
ATOM   4946 C CA  . SER B 2 158 ? 162.360 164.373 119.503 1.00 57.48  ? 288 SER D CA  1 
ATOM   4947 C C   . SER B 2 158 ? 160.850 164.482 119.670 1.00 60.52  ? 288 SER D C   1 
ATOM   4948 O O   . SER B 2 158 ? 160.074 164.129 118.779 1.00 63.59  ? 288 SER D O   1 
ATOM   4949 C CB  . SER B 2 158 ? 162.946 165.738 119.134 1.00 61.69  ? 288 SER D CB  1 
ATOM   4950 O OG  . SER B 2 158 ? 162.160 166.791 119.665 1.00 64.46  ? 288 SER D OG  1 
ATOM   4951 N N   . CYS B 2 159 ? 160.440 164.974 120.838 1.00 57.79  ? 289 CYS D N   1 
ATOM   4952 C CA  . CYS B 2 159 ? 159.020 165.198 121.117 1.00 59.48  ? 289 CYS D CA  1 
ATOM   4953 C C   . CYS B 2 159 ? 158.917 166.391 122.068 1.00 66.41  ? 289 CYS D C   1 
ATOM   4954 O O   . CYS B 2 159 ? 159.045 166.243 123.285 1.00 66.63  ? 289 CYS D O   1 
ATOM   4955 C CB  . CYS B 2 159 ? 158.362 163.959 121.701 1.00 59.13  ? 289 CYS D CB  1 
ATOM   4956 S SG  . CYS B 2 159 ? 156.622 164.188 122.112 1.00 72.96  ? 289 CYS D SG  1 
ATOM   4957 N N   . LYS B 2 160 ? 158.689 167.569 121.495 1.00 68.65  ? 290 LYS D N   1 
ATOM   4958 C CA  . LYS B 2 160 ? 158.490 168.764 122.301 1.00 64.29  ? 290 LYS D CA  1 
ATOM   4959 C C   . LYS B 2 160 ? 157.145 168.700 123.012 1.00 59.96  ? 290 LYS D C   1 
ATOM   4960 O O   . LYS B 2 160 ? 156.130 168.322 122.422 1.00 58.28  ? 290 LYS D O   1 
ATOM   4961 C CB  . LYS B 2 160 ? 158.567 170.014 121.424 1.00 64.43  ? 290 LYS D CB  1 
ATOM   4962 C CG  . LYS B 2 160 ? 158.969 171.279 122.163 1.00 64.69  ? 290 LYS D CG  1 
ATOM   4963 C CD  . LYS B 2 160 ? 158.117 172.464 121.746 1.00 65.52  ? 290 LYS D CD  1 
ATOM   4964 C CE  . LYS B 2 160 ? 158.313 173.634 122.693 1.00 61.17  ? 290 LYS D CE  1 
ATOM   4965 N NZ  . LYS B 2 160 ? 157.625 173.415 123.993 1.00 60.64  ? 290 LYS D NZ  1 
ATOM   4966 N N   . ALA B 2 161 ? 157.142 169.069 124.290 1.00 56.87  ? 291 ALA D N   1 
ATOM   4967 C CA  . ALA B 2 161 ? 155.940 169.057 125.111 1.00 57.24  ? 291 ALA D CA  1 
ATOM   4968 C C   . ALA B 2 161 ? 155.675 170.457 125.642 1.00 58.83  ? 291 ALA D C   1 
ATOM   4969 O O   . ALA B 2 161 ? 156.563 171.077 126.237 1.00 59.91  ? 291 ALA D O   1 
ATOM   4970 C CB  . ALA B 2 161 ? 156.072 168.067 126.268 1.00 48.98  ? 291 ALA D CB  1 
ATOM   4971 N N   . SER B 2 162 ? 154.458 170.949 125.428 1.00 57.29  ? 292 SER D N   1 
ATOM   4972 C CA  . SER B 2 162 ? 154.066 172.263 125.911 1.00 57.95  ? 292 SER D CA  1 
ATOM   4973 C C   . SER B 2 162 ? 152.586 172.244 126.261 1.00 59.35  ? 292 SER D C   1 
ATOM   4974 O O   . SER B 2 162 ? 151.811 171.463 125.705 1.00 59.22  ? 292 SER D O   1 
ATOM   4975 C CB  . SER B 2 162 ? 154.352 173.356 124.875 1.00 59.91  ? 292 SER D CB  1 
ATOM   4976 O OG  . SER B 2 162 ? 155.637 173.921 125.072 1.00 62.30  ? 292 SER D OG  1 
ATOM   4977 N N   . GLY B 2 163 ? 152.203 173.121 127.187 1.00 59.04  ? 293 GLY D N   1 
ATOM   4978 C CA  . GLY B 2 163 ? 150.835 173.220 127.645 1.00 56.32  ? 293 GLY D CA  1 
ATOM   4979 C C   . GLY B 2 163 ? 150.565 172.575 128.987 1.00 54.32  ? 293 GLY D C   1 
ATOM   4980 O O   . GLY B 2 163 ? 149.468 172.755 129.531 1.00 53.38  ? 293 GLY D O   1 
ATOM   4981 N N   . TYR B 2 164 ? 151.524 171.835 129.538 1.00 51.33  ? 294 TYR D N   1 
ATOM   4982 C CA  . TYR B 2 164 ? 151.334 171.164 130.814 1.00 48.64  ? 294 TYR D CA  1 
ATOM   4983 C C   . TYR B 2 164 ? 152.670 171.086 131.533 1.00 47.66  ? 294 TYR D C   1 
ATOM   4984 O O   . TYR B 2 164 ? 153.731 171.281 130.934 1.00 50.59  ? 294 TYR D O   1 
ATOM   4985 C CB  . TYR B 2 164 ? 150.736 169.763 130.629 1.00 50.21  ? 294 TYR D CB  1 
ATOM   4986 C CG  . TYR B 2 164 ? 151.721 168.722 130.141 1.00 45.79  ? 294 TYR D CG  1 
ATOM   4987 C CD1 . TYR B 2 164 ? 151.981 168.562 128.788 1.00 46.60  ? 294 TYR D CD1 1 
ATOM   4988 C CD2 . TYR B 2 164 ? 152.371 167.883 131.033 1.00 43.70  ? 294 TYR D CD2 1 
ATOM   4989 C CE1 . TYR B 2 164 ? 152.873 167.609 128.341 1.00 47.06  ? 294 TYR D CE1 1 
ATOM   4990 C CE2 . TYR B 2 164 ? 153.266 166.930 130.596 1.00 41.90  ? 294 TYR D CE2 1 
ATOM   4991 C CZ  . TYR B 2 164 ? 153.513 166.796 129.249 1.00 41.86  ? 294 TYR D CZ  1 
ATOM   4992 O OH  . TYR B 2 164 ? 154.403 165.844 128.814 1.00 40.70  ? 294 TYR D OH  1 
ATOM   4993 N N   . THR B 2 165 ? 152.607 170.800 132.833 1.00 45.51  ? 295 THR D N   1 
ATOM   4994 C CA  . THR B 2 165 ? 153.817 170.637 133.627 1.00 43.04  ? 295 THR D CA  1 
ATOM   4995 C C   . THR B 2 165 ? 154.588 169.423 133.133 1.00 42.11  ? 295 THR D C   1 
ATOM   4996 O O   . THR B 2 165 ? 154.189 168.283 133.392 1.00 42.84  ? 295 THR D O   1 
ATOM   4997 C CB  . THR B 2 165 ? 153.478 170.487 135.111 1.00 41.71  ? 295 THR D CB  1 
ATOM   4998 O OG1 . THR B 2 165 ? 152.719 171.621 135.547 1.00 44.91  ? 295 THR D OG1 1 
ATOM   4999 C CG2 . THR B 2 165 ? 154.746 170.385 135.941 1.00 38.61  ? 295 THR D CG2 1 
ATOM   5000 N N   . PHE B 2 166 ? 155.701 169.659 132.433 1.00 41.74  ? 296 PHE D N   1 
ATOM   5001 C CA  . PHE B 2 166 ? 156.388 168.574 131.739 1.00 40.78  ? 296 PHE D CA  1 
ATOM   5002 C C   . PHE B 2 166 ? 156.879 167.509 132.710 1.00 37.65  ? 296 PHE D C   1 
ATOM   5003 O O   . PHE B 2 166 ? 156.786 166.310 132.424 1.00 37.04  ? 296 PHE D O   1 
ATOM   5004 C CB  . PHE B 2 166 ? 157.553 169.125 130.920 1.00 42.76  ? 296 PHE D CB  1 
ATOM   5005 C CG  . PHE B 2 166 ? 158.235 168.092 130.073 1.00 47.46  ? 296 PHE D CG  1 
ATOM   5006 C CD1 . PHE B 2 166 ? 157.494 167.184 129.337 1.00 44.84  ? 296 PHE D CD1 1 
ATOM   5007 C CD2 . PHE B 2 166 ? 159.616 168.026 130.014 1.00 49.42  ? 296 PHE D CD2 1 
ATOM   5008 C CE1 . PHE B 2 166 ? 158.117 166.234 128.555 1.00 45.01  ? 296 PHE D CE1 1 
ATOM   5009 C CE2 . PHE B 2 166 ? 160.243 167.077 129.236 1.00 48.85  ? 296 PHE D CE2 1 
ATOM   5010 C CZ  . PHE B 2 166 ? 159.492 166.180 128.505 1.00 46.34  ? 296 PHE D CZ  1 
ATOM   5011 N N   . THR B 2 167 ? 157.404 167.920 133.858 1.00 36.03  ? 297 THR D N   1 
ATOM   5012 C CA  . THR B 2 167 ? 157.909 166.959 134.835 1.00 36.01  ? 297 THR D CA  1 
ATOM   5013 C C   . THR B 2 167 ? 156.796 166.481 135.761 1.00 36.99  ? 297 THR D C   1 
ATOM   5014 O O   . THR B 2 167 ? 156.938 166.449 136.982 1.00 39.11  ? 297 THR D O   1 
ATOM   5015 C CB  . THR B 2 167 ? 159.047 167.587 135.628 1.00 40.34  ? 297 THR D CB  1 
ATOM   5016 O OG1 . THR B 2 167 ? 158.765 168.975 135.844 1.00 44.67  ? 297 THR D OG1 1 
ATOM   5017 C CG2 . THR B 2 167 ? 160.345 167.476 134.857 1.00 41.23  ? 297 THR D CG2 1 
ATOM   5018 N N   . SER B 2 168 ? 155.686 166.039 135.156 1.00 33.71  ? 298 SER D N   1 
ATOM   5019 C CA  . SER B 2 168 ? 154.542 165.525 135.958 1.00 30.94  ? 298 SER D CA  1 
ATOM   5020 C C   . SER B 2 168 ? 153.789 164.423 135.196 1.00 31.16  ? 298 SER D C   1 
ATOM   5021 O O   . SER B 2 168 ? 152.755 163.957 135.719 1.00 36.22  ? 298 SER D O   1 
ATOM   5022 C CB  . SER B 2 168 ? 153.609 166.644 136.349 1.00 33.42  ? 298 SER D CB  1 
ATOM   5023 O OG  . SER B 2 168 ? 152.471 166.140 137.032 1.00 35.51  ? 298 SER D OG  1 
ATOM   5024 N N   . TYR B 2 169 ? 154.282 164.013 134.022 1.00 27.07  ? 299 TYR D N   1 
ATOM   5025 C CA  . TYR B 2 169 ? 153.582 163.017 133.226 1.00 24.63  ? 299 TYR D CA  1 
ATOM   5026 C C   . TYR B 2 169 ? 154.598 162.082 132.596 1.00 23.93  ? 299 TYR D C   1 
ATOM   5027 O O   . TYR B 2 169 ? 155.621 162.542 132.080 1.00 26.01  ? 299 TYR D O   1 
ATOM   5028 C CB  . TYR B 2 169 ? 152.745 163.675 132.126 1.00 29.79  ? 299 TYR D CB  1 
ATOM   5029 C CG  . TYR B 2 169 ? 151.388 164.166 132.566 1.00 33.83  ? 299 TYR D CG  1 
ATOM   5030 C CD1 . TYR B 2 169 ? 151.231 165.430 133.116 1.00 35.70  ? 299 TYR D CD1 1 
ATOM   5031 C CD2 . TYR B 2 169 ? 150.264 163.365 132.437 1.00 33.09  ? 299 TYR D CD2 1 
ATOM   5032 C CE1 . TYR B 2 169 ? 149.991 165.886 133.514 1.00 37.86  ? 299 TYR D CE1 1 
ATOM   5033 C CE2 . TYR B 2 169 ? 149.021 163.811 132.833 1.00 36.20  ? 299 TYR D CE2 1 
ATOM   5034 C CZ  . TYR B 2 169 ? 148.890 165.071 133.371 1.00 39.92  ? 299 TYR D CZ  1 
ATOM   5035 O OH  . TYR B 2 169 ? 147.653 165.520 133.770 1.00 38.56  ? 299 TYR D OH  1 
ATOM   5036 N N   . TRP B 2 170 ? 154.286 160.780 132.609 1.00 24.02  ? 300 TRP D N   1 
ATOM   5037 C CA  . TRP B 2 170 ? 155.140 159.786 131.920 1.00 19.47  ? 300 TRP D CA  1 
ATOM   5038 C C   . TRP B 2 170 ? 155.139 160.121 130.434 1.00 19.04  ? 300 TRP D C   1 
ATOM   5039 O O   . TRP B 2 170 ? 154.049 160.404 129.900 1.00 24.03  ? 300 TRP D O   1 
ATOM   5040 C CB  . TRP B 2 170 ? 154.635 158.356 132.158 1.00 17.84  ? 300 TRP D CB  1 
ATOM   5041 C CG  . TRP B 2 170 ? 155.164 157.730 133.418 1.00 16.20  ? 300 TRP D CG  1 
ATOM   5042 C CD1 . TRP B 2 170 ? 154.544 157.644 134.630 1.00 17.21  ? 300 TRP D CD1 1 
ATOM   5043 C CD2 . TRP B 2 170 ? 156.463 157.125 133.586 1.00 16.21  ? 300 TRP D CD2 1 
ATOM   5044 N NE1 . TRP B 2 170 ? 155.360 157.019 135.536 1.00 16.51  ? 300 TRP D NE1 1 
ATOM   5045 C CE2 . TRP B 2 170 ? 156.542 156.691 134.926 1.00 14.18  ? 300 TRP D CE2 1 
ATOM   5046 C CE3 . TRP B 2 170 ? 157.553 156.910 132.738 1.00 19.21  ? 300 TRP D CE3 1 
ATOM   5047 C CZ2 . TRP B 2 170 ? 157.672 156.054 135.431 1.00 16.05  ? 300 TRP D CZ2 1 
ATOM   5048 C CZ3 . TRP B 2 170 ? 158.669 156.281 133.239 1.00 22.64  ? 300 TRP D CZ3 1 
ATOM   5049 C CH2 . TRP B 2 170 ? 158.727 155.862 134.568 1.00 21.63  ? 300 TRP D CH2 1 
ATOM   5050 N N   . MET B 2 171 ? 156.304 160.117 129.793 1.00 17.72  ? 301 MET D N   1 
ATOM   5051 C CA  . MET B 2 171 ? 156.442 160.400 128.366 1.00 19.60  ? 301 MET D CA  1 
ATOM   5052 C C   . MET B 2 171 ? 156.602 159.056 127.665 1.00 21.47  ? 301 MET D C   1 
ATOM   5053 O O   . MET B 2 171 ? 157.713 158.577 127.441 1.00 26.44  ? 301 MET D O   1 
ATOM   5054 C CB  . MET B 2 171 ? 157.621 161.329 128.102 1.00 23.09  ? 301 MET D CB  1 
ATOM   5055 C CG  . MET B 2 171 ? 157.956 161.514 126.632 1.00 28.91  ? 301 MET D CG  1 
ATOM   5056 S SD  . MET B 2 171 ? 156.661 162.358 125.710 1.00 34.00  ? 301 MET D SD  1 
ATOM   5057 C CE  . MET B 2 171 ? 156.124 163.561 126.925 1.00 34.35  ? 301 MET D CE  1 
ATOM   5058 N N   . HIS B 2 172 ? 155.478 158.431 127.333 1.00 19.47  ? 302 HIS D N   1 
ATOM   5059 C CA  . HIS B 2 172 ? 155.526 157.117 126.718 1.00 19.13  ? 302 HIS D CA  1 
ATOM   5060 C C   . HIS B 2 172 ? 155.991 157.222 125.273 1.00 20.66  ? 302 HIS D C   1 
ATOM   5061 O O   . HIS B 2 172 ? 155.855 158.259 124.622 1.00 27.65  ? 302 HIS D O   1 
ATOM   5062 C CB  . HIS B 2 172 ? 154.161 156.445 126.789 1.00 21.47  ? 302 HIS D CB  1 
ATOM   5063 C CG  . HIS B 2 172 ? 153.826 155.917 128.146 1.00 20.00  ? 302 HIS D CG  1 
ATOM   5064 N ND1 . HIS B 2 172 ? 153.621 154.579 128.394 1.00 18.66  ? 302 HIS D ND1 1 
ATOM   5065 C CD2 . HIS B 2 172 ? 153.671 156.548 129.332 1.00 20.79  ? 302 HIS D CD2 1 
ATOM   5066 C CE1 . HIS B 2 172 ? 153.348 154.409 129.675 1.00 19.85  ? 302 HIS D CE1 1 
ATOM   5067 N NE2 . HIS B 2 172 ? 153.373 155.588 130.266 1.00 20.63  ? 302 HIS D NE2 1 
ATOM   5068 N N   . TRP B 2 173 ? 156.578 156.144 124.753 1.00 18.52  ? 303 TRP D N   1 
ATOM   5069 C CA  . TRP B 2 173 ? 157.123 156.133 123.372 1.00 21.77  ? 303 TRP D CA  1 
ATOM   5070 C C   . TRP B 2 173 ? 156.577 154.913 122.641 1.00 24.01  ? 303 TRP D C   1 
ATOM   5071 O O   . TRP B 2 173 ? 157.282 153.886 122.572 1.00 32.53  ? 303 TRP D O   1 
ATOM   5072 C CB  . TRP B 2 173 ? 158.656 156.186 123.395 1.00 28.12  ? 303 TRP D CB  1 
ATOM   5073 C CG  . TRP B 2 173 ? 159.168 157.601 123.394 1.00 27.88  ? 303 TRP D CG  1 
ATOM   5074 C CD1 . TRP B 2 173 ? 159.511 158.364 124.472 1.00 27.14  ? 303 TRP D CD1 1 
ATOM   5075 C CD2 . TRP B 2 173 ? 159.337 158.445 122.235 1.00 29.21  ? 303 TRP D CD2 1 
ATOM   5076 N NE1 . TRP B 2 173 ? 159.906 159.611 124.065 1.00 28.09  ? 303 TRP D NE1 1 
ATOM   5077 C CE2 . TRP B 2 173 ? 159.804 159.692 122.701 1.00 30.83  ? 303 TRP D CE2 1 
ATOM   5078 C CE3 . TRP B 2 173 ? 159.147 158.264 120.862 1.00 33.59  ? 303 TRP D CE3 1 
ATOM   5079 C CZ2 . TRP B 2 173 ? 160.084 160.747 121.835 1.00 40.14  ? 303 TRP D CZ2 1 
ATOM   5080 C CZ3 . TRP B 2 173 ? 159.421 159.309 120.009 1.00 38.40  ? 303 TRP D CZ3 1 
ATOM   5081 C CH2 . TRP B 2 173 ? 159.879 160.534 120.492 1.00 42.51  ? 303 TRP D CH2 1 
ATOM   5082 N N   . VAL B 2 174 ? 155.349 155.013 122.134 1.00 24.34  ? 304 VAL D N   1 
ATOM   5083 C CA  . VAL B 2 174 ? 154.707 153.940 121.388 1.00 27.45  ? 304 VAL D CA  1 
ATOM   5084 C C   . VAL B 2 174 ? 155.227 153.951 119.958 1.00 32.13  ? 304 VAL D C   1 
ATOM   5085 O O   . VAL B 2 174 ? 155.678 154.980 119.446 1.00 38.08  ? 304 VAL D O   1 
ATOM   5086 C CB  . VAL B 2 174 ? 153.175 154.098 121.440 1.00 26.00  ? 304 VAL D CB  1 
ATOM   5087 C CG1 . VAL B 2 174 ? 152.486 152.821 121.008 1.00 31.26  ? 304 VAL D CG1 1 
ATOM   5088 C CG2 . VAL B 2 174 ? 152.738 154.486 122.836 1.00 30.49  ? 304 VAL D CG2 1 
ATOM   5089 N N   . ARG B 2 175 ? 155.178 152.794 119.304 1.00 30.41  ? 305 ARG D N   1 
ATOM   5090 C CA  . ARG B 2 175 ? 155.574 152.674 117.911 1.00 30.66  ? 305 ARG D CA  1 
ATOM   5091 C C   . ARG B 2 175 ? 154.534 151.859 117.161 1.00 35.15  ? 305 ARG D C   1 
ATOM   5092 O O   . ARG B 2 175 ? 153.831 151.030 117.746 1.00 41.25  ? 305 ARG D O   1 
ATOM   5093 C CB  . ARG B 2 175 ? 156.957 152.027 117.768 1.00 35.57  ? 305 ARG D CB  1 
ATOM   5094 C CG  . ARG B 2 175 ? 156.936 150.566 117.361 1.00 40.13  ? 305 ARG D CG  1 
ATOM   5095 C CD  . ARG B 2 175 ? 158.312 150.096 116.927 1.00 44.65  ? 305 ARG D CD  1 
ATOM   5096 N NE  . ARG B 2 175 ? 158.246 148.859 116.158 1.00 51.39  ? 305 ARG D NE  1 
ATOM   5097 C CZ  . ARG B 2 175 ? 159.213 148.416 115.368 1.00 55.92  ? 305 ARG D CZ  1 
ATOM   5098 N NH1 . ARG B 2 175 ? 160.342 149.088 115.215 1.00 58.12  ? 305 ARG D NH1 1 
ATOM   5099 N NH2 . ARG B 2 175 ? 159.044 147.270 114.714 1.00 54.56  ? 305 ARG D NH2 1 
ATOM   5100 N N   . GLN B 2 176 ? 154.434 152.108 115.858 1.00 37.65  ? 306 GLN D N   1 
ATOM   5101 C CA  . GLN B 2 176 ? 153.469 151.432 114.995 1.00 45.06  ? 306 GLN D CA  1 
ATOM   5102 C C   . GLN B 2 176 ? 154.204 150.928 113.758 1.00 51.40  ? 306 GLN D C   1 
ATOM   5103 O O   . GLN B 2 176 ? 154.409 151.679 112.800 1.00 58.04  ? 306 GLN D O   1 
ATOM   5104 C CB  . GLN B 2 176 ? 152.322 152.363 114.617 1.00 46.31  ? 306 GLN D CB  1 
ATOM   5105 C CG  . GLN B 2 176 ? 151.360 151.776 113.598 1.00 48.93  ? 306 GLN D CG  1 
ATOM   5106 C CD  . GLN B 2 176 ? 150.383 152.801 113.063 1.00 51.83  ? 306 GLN D CD  1 
ATOM   5107 O OE1 . GLN B 2 176 ? 150.507 153.994 113.335 1.00 52.62  ? 306 GLN D OE1 1 
ATOM   5108 N NE2 . GLN B 2 176 ? 149.403 152.339 112.296 1.00 55.60  ? 306 GLN D NE2 1 
ATOM   5109 N N   . ALA B 2 177 ? 154.608 149.667 113.782 1.00 52.12  ? 307 ALA D N   1 
ATOM   5110 C CA  . ALA B 2 177 ? 155.234 149.071 112.611 1.00 57.13  ? 307 ALA D CA  1 
ATOM   5111 C C   . ALA B 2 177 ? 154.204 148.946 111.494 1.00 61.96  ? 307 ALA D C   1 
ATOM   5112 O O   . ALA B 2 177 ? 153.101 148.441 111.731 1.00 61.70  ? 307 ALA D O   1 
ATOM   5113 C CB  . ALA B 2 177 ? 155.818 147.704 112.951 1.00 57.41  ? 307 ALA D CB  1 
ATOM   5114 N N   . PRO B 2 178 ? 154.511 149.405 110.281 1.00 66.15  ? 308 PRO D N   1 
ATOM   5115 C CA  . PRO B 2 178 ? 153.548 149.274 109.181 1.00 68.02  ? 308 PRO D CA  1 
ATOM   5116 C C   . PRO B 2 178 ? 153.193 147.817 108.929 1.00 69.31  ? 308 PRO D C   1 
ATOM   5117 O O   . PRO B 2 178 ? 154.044 146.928 108.999 1.00 67.95  ? 308 PRO D O   1 
ATOM   5118 C CB  . PRO B 2 178 ? 154.288 149.889 107.988 1.00 71.37  ? 308 PRO D CB  1 
ATOM   5119 C CG  . PRO B 2 178 ? 155.285 150.817 108.601 1.00 69.26  ? 308 PRO D CG  1 
ATOM   5120 C CD  . PRO B 2 178 ? 155.707 150.167 109.886 1.00 66.24  ? 308 PRO D CD  1 
ATOM   5121 N N   . GLY B 2 179 ? 151.917 147.579 108.633 1.00 69.49  ? 309 GLY D N   1 
ATOM   5122 C CA  . GLY B 2 179 ? 151.437 146.221 108.490 1.00 69.40  ? 309 GLY D CA  1 
ATOM   5123 C C   . GLY B 2 179 ? 151.348 145.455 109.789 1.00 69.14  ? 309 GLY D C   1 
ATOM   5124 O O   . GLY B 2 179 ? 151.346 144.221 109.772 1.00 66.28  ? 309 GLY D O   1 
ATOM   5125 N N   . GLN B 2 180 ? 151.275 146.154 110.919 1.00 70.19  ? 310 GLN D N   1 
ATOM   5126 C CA  . GLN B 2 180 ? 151.242 145.511 112.224 1.00 64.69  ? 310 GLN D CA  1 
ATOM   5127 C C   . GLN B 2 180 ? 150.586 146.457 113.217 1.00 62.28  ? 310 GLN D C   1 
ATOM   5128 O O   . GLN B 2 180 ? 150.459 147.659 112.967 1.00 61.55  ? 310 GLN D O   1 
ATOM   5129 C CB  . GLN B 2 180 ? 152.648 145.125 112.693 1.00 59.32  ? 310 GLN D CB  1 
ATOM   5130 C CG  . GLN B 2 180 ? 152.705 143.861 113.528 1.00 60.02  ? 310 GLN D CG  1 
ATOM   5131 C CD  . GLN B 2 180 ? 154.113 143.318 113.658 1.00 64.16  ? 310 GLN D CD  1 
ATOM   5132 O OE1 . GLN B 2 180 ? 154.959 143.542 112.793 1.00 65.08  ? 310 GLN D OE1 1 
ATOM   5133 N NE2 . GLN B 2 180 ? 154.374 142.603 114.746 1.00 60.00  ? 310 GLN D NE2 1 
ATOM   5134 N N   . GLY B 2 181 ? 150.148 145.885 114.342 1.00 57.20  ? 311 GLY D N   1 
ATOM   5135 C CA  . GLY B 2 181 ? 149.508 146.679 115.398 1.00 51.99  ? 311 GLY D CA  1 
ATOM   5136 C C   . GLY B 2 181 ? 150.541 147.475 116.159 1.00 47.54  ? 311 GLY D C   1 
ATOM   5137 O O   . GLY B 2 181 ? 151.746 147.186 116.000 1.00 50.62  ? 311 GLY D O   1 
ATOM   5138 N N   . LEU B 2 182 ? 150.099 148.435 116.962 1.00 42.93  ? 312 LEU D N   1 
ATOM   5139 C CA  . LEU B 2 182 ? 150.975 149.292 117.749 1.00 37.95  ? 312 LEU D CA  1 
ATOM   5140 C C   . LEU B 2 182 ? 151.781 148.460 118.737 1.00 37.71  ? 312 LEU D C   1 
ATOM   5141 O O   . LEU B 2 182 ? 151.243 147.579 119.413 1.00 40.68  ? 312 LEU D O   1 
ATOM   5142 C CB  . LEU B 2 182 ? 150.157 150.347 118.490 1.00 36.83  ? 312 LEU D CB  1 
ATOM   5143 C CG  . LEU B 2 182 ? 150.095 151.730 117.844 1.00 39.67  ? 312 LEU D CG  1 
ATOM   5144 C CD1 . LEU B 2 182 ? 149.291 151.674 116.563 1.00 45.71  ? 312 LEU D CD1 1 
ATOM   5145 C CD2 . LEU B 2 182 ? 149.498 152.738 118.800 1.00 36.79  ? 312 LEU D CD2 1 
ATOM   5146 N N   . GLU B 2 183 ? 153.078 148.741 118.817 1.00 33.58  ? 313 GLU D N   1 
ATOM   5147 C CA  . GLU B 2 183 ? 153.988 148.029 119.703 1.00 33.09  ? 313 GLU D CA  1 
ATOM   5148 C C   . GLU B 2 183 ? 154.590 149.019 120.685 1.00 30.42  ? 313 GLU D C   1 
ATOM   5149 O O   . GLU B 2 183 ? 155.226 149.995 120.276 1.00 33.28  ? 313 GLU D O   1 
ATOM   5150 C CB  . GLU B 2 183 ? 155.091 147.324 118.911 1.00 38.37  ? 313 GLU D CB  1 
ATOM   5151 C CG  . GLU B 2 183 ? 154.694 145.966 118.365 1.00 40.81  ? 313 GLU D CG  1 
ATOM   5152 C CD  . GLU B 2 183 ? 154.924 145.851 116.872 1.00 44.61  ? 313 GLU D CD  1 
ATOM   5153 O OE1 . GLU B 2 183 ? 155.626 146.717 116.309 1.00 46.02  ? 313 GLU D OE1 1 
ATOM   5154 O OE2 . GLU B 2 183 ? 154.405 144.894 116.262 1.00 47.35  ? 313 GLU D OE2 1 
ATOM   5155 N N   . TRP B 2 184 ? 154.388 148.769 121.973 1.00 29.28  ? 314 TRP D N   1 
ATOM   5156 C CA  . TRP B 2 184 ? 155.007 149.592 122.999 1.00 27.38  ? 314 TRP D CA  1 
ATOM   5157 C C   . TRP B 2 184 ? 156.520 149.430 122.959 1.00 30.81  ? 314 TRP D C   1 
ATOM   5158 O O   . TRP B 2 184 ? 157.037 148.347 122.673 1.00 37.91  ? 314 TRP D O   1 
ATOM   5159 C CB  . TRP B 2 184 ? 154.474 149.204 124.374 1.00 28.30  ? 314 TRP D CB  1 
ATOM   5160 C CG  . TRP B 2 184 ? 154.704 150.230 125.423 1.00 26.90  ? 314 TRP D CG  1 
ATOM   5161 C CD1 . TRP B 2 184 ? 154.236 151.507 125.437 1.00 24.20  ? 314 TRP D CD1 1 
ATOM   5162 C CD2 . TRP B 2 184 ? 155.462 150.066 126.624 1.00 29.64  ? 314 TRP D CD2 1 
ATOM   5163 N NE1 . TRP B 2 184 ? 154.655 152.152 126.573 1.00 23.58  ? 314 TRP D NE1 1 
ATOM   5164 C CE2 . TRP B 2 184 ? 155.411 151.287 127.319 1.00 25.36  ? 314 TRP D CE2 1 
ATOM   5165 C CE3 . TRP B 2 184 ? 156.180 149.004 127.180 1.00 32.95  ? 314 TRP D CE3 1 
ATOM   5166 C CZ2 . TRP B 2 184 ? 156.050 151.476 128.539 1.00 26.01  ? 314 TRP D CZ2 1 
ATOM   5167 C CZ3 . TRP B 2 184 ? 156.813 149.194 128.392 1.00 29.30  ? 314 TRP D CZ3 1 
ATOM   5168 C CH2 . TRP B 2 184 ? 156.744 150.419 129.058 1.00 25.40  ? 314 TRP D CH2 1 
ATOM   5169 N N   . MET B 2 185 ? 157.257 150.524 123.237 1.00 31.15  ? 315 MET D N   1 
ATOM   5170 C CA  . MET B 2 185 ? 158.751 150.512 123.223 1.00 31.72  ? 315 MET D CA  1 
ATOM   5171 C C   . MET B 2 185 ? 159.344 151.069 124.527 1.00 32.62  ? 315 MET D C   1 
ATOM   5172 O O   . MET B 2 185 ? 160.556 150.855 124.713 1.00 36.48  ? 315 MET D O   1 
ATOM   5173 C CB  . MET B 2 185 ? 159.331 151.375 122.099 1.00 31.55  ? 315 MET D CB  1 
ATOM   5174 C CG  . MET B 2 185 ? 158.860 151.024 120.709 1.00 39.79  ? 315 MET D CG  1 
ATOM   5175 S SD  . MET B 2 185 ? 159.988 151.709 119.478 1.00 49.66  ? 315 MET D SD  1 
ATOM   5176 C CE  . MET B 2 185 ? 159.924 153.458 119.894 1.00 35.08  ? 315 MET D CE  1 
ATOM   5177 N N   . GLY B 2 186 ? 158.619 151.884 125.303 1.00 29.34  ? 316 GLY D N   1 
ATOM   5178 C CA  . GLY B 2 186 ? 159.075 152.332 126.600 1.00 26.62  ? 316 GLY D CA  1 
ATOM   5179 C C   . GLY B 2 186 ? 158.501 153.693 126.918 1.00 25.10  ? 316 GLY D C   1 
ATOM   5180 O O   . GLY B 2 186 ? 157.722 154.261 126.155 1.00 31.08  ? 316 GLY D O   1 
ATOM   5181 N N   . ASN B 2 187 ? 158.907 154.206 128.074 1.00 21.20  ? 317 ASN D N   1 
ATOM   5182 C CA  . ASN B 2 187 ? 158.487 155.527 128.506 1.00 22.11  ? 317 ASN D CA  1 
ATOM   5183 C C   . ASN B 2 187 ? 159.657 156.186 129.221 1.00 23.72  ? 317 ASN D C   1 
ATOM   5184 O O   . ASN B 2 187 ? 160.760 155.636 129.286 1.00 29.29  ? 317 ASN D O   1 
ATOM   5185 C CB  . ASN B 2 187 ? 157.233 155.447 129.387 1.00 22.22  ? 317 ASN D CB  1 
ATOM   5186 C CG  . ASN B 2 187 ? 157.367 154.448 130.510 1.00 22.41  ? 317 ASN D CG  1 
ATOM   5187 O OD1 . ASN B 2 187 ? 158.470 154.072 130.899 1.00 25.11  ? 317 ASN D OD1 1 
ATOM   5188 N ND2 . ASN B 2 187 ? 156.235 154.013 131.044 1.00 17.95  ? 317 ASN D ND2 1 
ATOM   5189 N N   . ILE B 2 188 ? 159.412 157.378 129.754 1.00 22.63  ? 318 ILE D N   1 
ATOM   5190 C CA  . ILE B 2 188 ? 160.420 158.114 130.504 1.00 22.45  ? 318 ILE D CA  1 
ATOM   5191 C C   . ILE B 2 188 ? 159.700 159.140 131.361 1.00 23.08  ? 318 ILE D C   1 
ATOM   5192 O O   . ILE B 2 188 ? 158.766 159.803 130.905 1.00 26.72  ? 318 ILE D O   1 
ATOM   5193 C CB  . ILE B 2 188 ? 161.452 158.773 129.559 1.00 25.49  ? 318 ILE D CB  1 
ATOM   5194 C CG1 . ILE B 2 188 ? 162.242 159.854 130.291 1.00 30.74  ? 318 ILE D CG1 1 
ATOM   5195 C CG2 . ILE B 2 188 ? 160.766 159.356 128.341 1.00 27.12  ? 318 ILE D CG2 1 
ATOM   5196 C CD1 . ILE B 2 188 ? 163.380 160.408 129.485 1.00 38.18  ? 318 ILE D CD1 1 
ATOM   5197 N N   . TRP B 2 189 ? 160.135 159.263 132.612 1.00 25.50  ? 319 TRP D N   1 
ATOM   5198 C CA  . TRP B 2 189 ? 159.563 160.250 133.512 1.00 26.88  ? 319 TRP D CA  1 
ATOM   5199 C C   . TRP B 2 189 ? 160.469 161.469 133.540 1.00 30.09  ? 319 TRP D C   1 
ATOM   5200 O O   . TRP B 2 189 ? 161.583 161.385 134.077 1.00 36.32  ? 319 TRP D O   1 
ATOM   5201 C CB  . TRP B 2 189 ? 159.402 159.675 134.915 1.00 24.21  ? 319 TRP D CB  1 
ATOM   5202 C CG  . TRP B 2 189 ? 158.764 160.623 135.862 1.00 21.33  ? 319 TRP D CG  1 
ATOM   5203 C CD1 . TRP B 2 189 ? 159.393 161.456 136.733 1.00 26.33  ? 319 TRP D CD1 1 
ATOM   5204 C CD2 . TRP B 2 189 ? 157.363 160.839 136.041 1.00 20.12  ? 319 TRP D CD2 1 
ATOM   5205 N NE1 . TRP B 2 189 ? 158.472 162.182 137.444 1.00 26.64  ? 319 TRP D NE1 1 
ATOM   5206 C CE2 . TRP B 2 189 ? 157.216 161.819 137.037 1.00 25.35  ? 319 TRP D CE2 1 
ATOM   5207 C CE3 . TRP B 2 189 ? 156.217 160.299 135.455 1.00 21.34  ? 319 TRP D CE3 1 
ATOM   5208 C CZ2 . TRP B 2 189 ? 155.972 162.271 137.459 1.00 29.94  ? 319 TRP D CZ2 1 
ATOM   5209 C CZ3 . TRP B 2 189 ? 154.983 160.748 135.876 1.00 20.62  ? 319 TRP D CZ3 1 
ATOM   5210 C CH2 . TRP B 2 189 ? 154.870 161.722 136.868 1.00 25.02  ? 319 TRP D CH2 1 
ATOM   5211 N N   . PRO B 2 190 ? 160.049 162.610 132.992 1.00 26.55  ? 320 PRO D N   1 
ATOM   5212 C CA  . PRO B 2 190 ? 160.949 163.772 132.934 1.00 32.75  ? 320 PRO D CA  1 
ATOM   5213 C C   . PRO B 2 190 ? 161.392 164.276 134.294 1.00 38.97  ? 320 PRO D C   1 
ATOM   5214 O O   . PRO B 2 190 ? 162.434 164.936 134.380 1.00 44.03  ? 320 PRO D O   1 
ATOM   5215 C CB  . PRO B 2 190 ? 160.113 164.823 132.193 1.00 33.82  ? 320 PRO D CB  1 
ATOM   5216 C CG  . PRO B 2 190 ? 159.102 164.034 131.435 1.00 30.31  ? 320 PRO D CG  1 
ATOM   5217 C CD  . PRO B 2 190 ? 158.776 162.867 132.305 1.00 24.89  ? 320 PRO D CD  1 
ATOM   5218 N N   . GLY B 2 191 ? 160.637 163.996 135.357 1.00 38.73  ? 321 GLY D N   1 
ATOM   5219 C CA  . GLY B 2 191 ? 161.029 164.473 136.673 1.00 38.30  ? 321 GLY D CA  1 
ATOM   5220 C C   . GLY B 2 191 ? 162.348 163.891 137.143 1.00 36.56  ? 321 GLY D C   1 
ATOM   5221 O O   . GLY B 2 191 ? 163.190 164.604 137.694 1.00 38.61  ? 321 GLY D O   1 
ATOM   5222 N N   . SER B 2 192 ? 162.548 162.591 136.931 1.00 33.86  ? 322 SER D N   1 
ATOM   5223 C CA  . SER B 2 192 ? 163.760 161.916 137.364 1.00 36.65  ? 322 SER D CA  1 
ATOM   5224 C C   . SER B 2 192 ? 164.510 161.215 136.242 1.00 37.11  ? 322 SER D C   1 
ATOM   5225 O O   . SER B 2 192 ? 165.619 160.725 136.482 1.00 38.26  ? 322 SER D O   1 
ATOM   5226 C CB  . SER B 2 192 ? 163.439 160.890 138.463 1.00 36.22  ? 322 SER D CB  1 
ATOM   5227 O OG  . SER B 2 192 ? 162.636 161.465 139.479 1.00 34.21  ? 322 SER D OG  1 
ATOM   5228 N N   . GLY B 2 193 ? 163.952 161.151 135.037 1.00 34.60  ? 323 GLY D N   1 
ATOM   5229 C CA  . GLY B 2 193 ? 164.616 160.483 133.939 1.00 34.41  ? 323 GLY D CA  1 
ATOM   5230 C C   . GLY B 2 193 ? 164.504 158.977 133.938 1.00 33.05  ? 323 GLY D C   1 
ATOM   5231 O O   . GLY B 2 193 ? 165.181 158.325 133.137 1.00 33.39  ? 323 GLY D O   1 
ATOM   5232 N N   . GLY B 2 194 ? 163.682 158.402 134.812 1.00 32.03  ? 324 GLY D N   1 
ATOM   5233 C CA  . GLY B 2 194 ? 163.536 156.955 134.847 1.00 34.13  ? 324 GLY D CA  1 
ATOM   5234 C C   . GLY B 2 194 ? 162.832 156.445 133.603 1.00 31.53  ? 324 GLY D C   1 
ATOM   5235 O O   . GLY B 2 194 ? 161.759 156.935 133.233 1.00 32.16  ? 324 GLY D O   1 
ATOM   5236 N N   . THR B 2 195 ? 163.431 155.449 132.954 1.00 26.43  ? 325 THR D N   1 
ATOM   5237 C CA  . THR B 2 195 ? 162.909 154.877 131.724 1.00 26.22  ? 325 THR D CA  1 
ATOM   5238 C C   . THR B 2 195 ? 162.641 153.391 131.911 1.00 28.23  ? 325 THR D C   1 
ATOM   5239 O O   . THR B 2 195 ? 163.333 152.711 132.674 1.00 34.21  ? 325 THR D O   1 
ATOM   5240 C CB  . THR B 2 195 ? 163.885 155.068 130.562 1.00 29.31  ? 325 THR D CB  1 
ATOM   5241 O OG1 . THR B 2 195 ? 164.931 154.097 130.660 1.00 32.90  ? 325 THR D OG1 1 
ATOM   5242 C CG2 . THR B 2 195 ? 164.494 156.455 130.598 1.00 32.36  ? 325 THR D CG2 1 
ATOM   5243 N N   . ASN B 2 196 ? 161.627 152.888 131.203 1.00 28.24  ? 326 ASN D N   1 
ATOM   5244 C CA  . ASN B 2 196 ? 161.263 151.470 131.227 1.00 28.83  ? 326 ASN D CA  1 
ATOM   5245 C C   . ASN B 2 196 ? 161.137 150.987 129.787 1.00 31.45  ? 326 ASN D C   1 
ATOM   5246 O O   . ASN B 2 196 ? 160.034 150.960 129.237 1.00 33.05  ? 326 ASN D O   1 
ATOM   5247 C CB  . ASN B 2 196 ? 159.968 151.247 132.000 1.00 24.17  ? 326 ASN D CB  1 
ATOM   5248 C CG  . ASN B 2 196 ? 159.941 151.985 133.316 1.00 25.80  ? 326 ASN D CG  1 
ATOM   5249 O OD1 . ASN B 2 196 ? 159.859 153.211 133.350 1.00 24.45  ? 326 ASN D OD1 1 
ATOM   5250 N ND2 . ASN B 2 196 ? 160.005 151.241 134.413 1.00 28.86  ? 326 ASN D ND2 1 
ATOM   5251 N N   . TYR B 2 197 ? 162.254 150.587 129.185 1.00 32.49  ? 327 TYR D N   1 
ATOM   5252 C CA  . TYR B 2 197 ? 162.215 150.083 127.820 1.00 35.68  ? 327 TYR D CA  1 
ATOM   5253 C C   . TYR B 2 197 ? 161.508 148.734 127.761 1.00 38.42  ? 327 TYR D C   1 
ATOM   5254 O O   . TYR B 2 197 ? 161.532 147.950 128.712 1.00 39.81  ? 327 TYR D O   1 
ATOM   5255 C CB  . TYR B 2 197 ? 163.625 149.944 127.247 1.00 39.90  ? 327 TYR D CB  1 
ATOM   5256 C CG  . TYR B 2 197 ? 164.562 151.079 127.580 1.00 40.42  ? 327 TYR D CG  1 
ATOM   5257 C CD1 . TYR B 2 197 ? 164.302 152.369 127.149 1.00 42.55  ? 327 TYR D CD1 1 
ATOM   5258 C CD2 . TYR B 2 197 ? 165.723 150.852 128.305 1.00 45.35  ? 327 TYR D CD2 1 
ATOM   5259 C CE1 . TYR B 2 197 ? 165.163 153.407 127.444 1.00 47.71  ? 327 TYR D CE1 1 
ATOM   5260 C CE2 . TYR B 2 197 ? 166.590 151.882 128.604 1.00 43.91  ? 327 TYR D CE2 1 
ATOM   5261 C CZ  . TYR B 2 197 ? 166.307 153.157 128.171 1.00 46.97  ? 327 TYR D CZ  1 
ATOM   5262 O OH  . TYR B 2 197 ? 167.168 154.186 128.469 1.00 46.97  ? 327 TYR D OH  1 
ATOM   5263 N N   . ALA B 2 198 ? 160.870 148.471 126.624 1.00 39.16  ? 328 ALA D N   1 
ATOM   5264 C CA  . ALA B 2 198 ? 160.244 147.178 126.404 1.00 38.82  ? 328 ALA D CA  1 
ATOM   5265 C C   . ALA B 2 198 ? 161.308 146.101 126.220 1.00 51.18  ? 328 ALA D C   1 
ATOM   5266 O O   . ALA B 2 198 ? 162.477 146.385 125.946 1.00 54.56  ? 328 ALA D O   1 
ATOM   5267 C CB  . ALA B 2 198 ? 159.325 147.223 125.184 1.00 35.26  ? 328 ALA D CB  1 
ATOM   5268 N N   . GLU B 2 199 ? 160.886 144.845 126.380 1.00 55.74  ? 329 GLU D N   1 
ATOM   5269 C CA  . GLU B 2 199 ? 161.831 143.735 126.300 1.00 57.09  ? 329 GLU D CA  1 
ATOM   5270 C C   . GLU B 2 199 ? 162.462 143.641 124.917 1.00 54.89  ? 329 GLU D C   1 
ATOM   5271 O O   . GLU B 2 199 ? 163.667 143.392 124.793 1.00 57.46  ? 329 GLU D O   1 
ATOM   5272 C CB  . GLU B 2 199 ? 161.134 142.424 126.668 1.00 56.85  ? 329 GLU D CB  1 
ATOM   5273 C CG  . GLU B 2 199 ? 160.721 142.294 128.141 1.00 61.54  ? 329 GLU D CG  1 
ATOM   5274 C CD  . GLU B 2 199 ? 161.857 142.500 129.143 1.00 68.79  ? 329 GLU D CD  1 
ATOM   5275 O OE1 . GLU B 2 199 ? 163.041 142.556 128.747 1.00 66.94  ? 329 GLU D OE1 1 
ATOM   5276 O OE2 . GLU B 2 199 ? 161.555 142.610 130.350 1.00 71.61  ? 329 GLU D OE2 1 
ATOM   5277 N N   . LYS B 2 200 ? 161.666 143.837 123.865 1.00 53.21  ? 330 LYS D N   1 
ATOM   5278 C CA  . LYS B 2 200 ? 162.206 143.815 122.511 1.00 56.88  ? 330 LYS D CA  1 
ATOM   5279 C C   . LYS B 2 200 ? 163.166 144.968 122.250 1.00 55.47  ? 330 LYS D C   1 
ATOM   5280 O O   . LYS B 2 200 ? 163.988 144.877 121.332 1.00 58.13  ? 330 LYS D O   1 
ATOM   5281 C CB  . LYS B 2 200 ? 161.068 143.850 121.491 1.00 60.52  ? 330 LYS D CB  1 
ATOM   5282 C CG  . LYS B 2 200 ? 160.362 142.516 121.298 1.00 61.44  ? 330 LYS D CG  1 
ATOM   5283 C CD  . LYS B 2 200 ? 159.111 142.652 120.437 1.00 63.01  ? 330 LYS D CD  1 
ATOM   5284 C CE  . LYS B 2 200 ? 159.284 143.672 119.318 1.00 64.52  ? 330 LYS D CE  1 
ATOM   5285 N NZ  . LYS B 2 200 ? 160.391 143.317 118.385 1.00 63.98  ? 330 LYS D NZ  1 
ATOM   5286 N N   . PHE B 2 201 ? 163.083 146.045 123.033 1.00 53.02  ? 331 PHE D N   1 
ATOM   5287 C CA  . PHE B 2 201 ? 163.918 147.225 122.843 1.00 52.70  ? 331 PHE D CA  1 
ATOM   5288 C C   . PHE B 2 201 ? 164.782 147.517 124.066 1.00 53.38  ? 331 PHE D C   1 
ATOM   5289 O O   . PHE B 2 201 ? 165.228 148.654 124.245 1.00 50.91  ? 331 PHE D O   1 
ATOM   5290 C CB  . PHE B 2 201 ? 163.055 148.445 122.512 1.00 49.72  ? 331 PHE D CB  1 
ATOM   5291 C CG  . PHE B 2 201 ? 162.213 148.285 121.278 1.00 51.67  ? 331 PHE D CG  1 
ATOM   5292 C CD1 . PHE B 2 201 ? 161.025 147.576 121.317 1.00 52.47  ? 331 PHE D CD1 1 
ATOM   5293 C CD2 . PHE B 2 201 ? 162.603 148.860 120.081 1.00 50.82  ? 331 PHE D CD2 1 
ATOM   5294 C CE1 . PHE B 2 201 ? 160.249 147.433 120.184 1.00 52.98  ? 331 PHE D CE1 1 
ATOM   5295 C CE2 . PHE B 2 201 ? 161.831 148.722 118.945 1.00 50.24  ? 331 PHE D CE2 1 
ATOM   5296 C CZ  . PHE B 2 201 ? 160.652 148.007 118.997 1.00 52.52  ? 331 PHE D CZ  1 
ATOM   5297 N N   . LYS B 2 202 ? 165.022 146.515 124.914 1.00 54.70  ? 332 LYS D N   1 
ATOM   5298 C CA  . LYS B 2 202 ? 165.703 146.762 126.182 1.00 55.53  ? 332 LYS D CA  1 
ATOM   5299 C C   . LYS B 2 202 ? 167.139 147.228 125.972 1.00 56.48  ? 332 LYS D C   1 
ATOM   5300 O O   . LYS B 2 202 ? 167.610 148.138 126.664 1.00 55.43  ? 332 LYS D O   1 
ATOM   5301 C CB  . LYS B 2 202 ? 165.670 145.502 127.046 1.00 57.48  ? 332 LYS D CB  1 
ATOM   5302 C CG  . LYS B 2 202 ? 166.266 145.687 128.431 1.00 59.91  ? 332 LYS D CG  1 
ATOM   5303 C CD  . LYS B 2 202 ? 165.185 145.723 129.498 1.00 61.85  ? 332 LYS D CD  1 
ATOM   5304 C CE  . LYS B 2 202 ? 165.576 146.636 130.649 1.00 55.99  ? 332 LYS D CE  1 
ATOM   5305 N NZ  . LYS B 2 202 ? 164.385 147.199 131.344 1.00 49.74  ? 332 LYS D NZ  1 
ATOM   5306 N N   . ASN B 2 203 ? 167.851 146.620 125.024 1.00 57.04  ? 333 ASN D N   1 
ATOM   5307 C CA  . ASN B 2 203 ? 169.268 146.890 124.812 1.00 59.64  ? 333 ASN D CA  1 
ATOM   5308 C C   . ASN B 2 203 ? 169.536 147.545 123.461 1.00 60.73  ? 333 ASN D C   1 
ATOM   5309 O O   . ASN B 2 203 ? 170.612 147.371 122.884 1.00 61.39  ? 333 ASN D O   1 
ATOM   5310 C CB  . ASN B 2 203 ? 170.075 145.599 124.945 1.00 61.96  ? 333 ASN D CB  1 
ATOM   5311 C CG  . ASN B 2 203 ? 169.460 144.445 124.173 1.00 64.39  ? 333 ASN D CG  1 
ATOM   5312 O OD1 . ASN B 2 203 ? 169.018 144.607 123.036 1.00 63.39  ? 333 ASN D OD1 1 
ATOM   5313 N ND2 . ASN B 2 203 ? 169.428 143.271 124.792 1.00 68.01  ? 333 ASN D ND2 1 
ATOM   5314 N N   . ARG B 2 204 ? 168.571 148.303 122.945 1.00 59.66  ? 334 ARG D N   1 
ATOM   5315 C CA  . ARG B 2 204 ? 168.695 148.858 121.604 1.00 58.26  ? 334 ARG D CA  1 
ATOM   5316 C C   . ARG B 2 204 ? 168.371 150.346 121.574 1.00 55.05  ? 334 ARG D C   1 
ATOM   5317 O O   . ARG B 2 204 ? 168.879 151.079 120.719 1.00 55.78  ? 334 ARG D O   1 
ATOM   5318 C CB  . ARG B 2 204 ? 167.781 148.094 120.644 1.00 58.60  ? 334 ARG D CB  1 
ATOM   5319 C CG  . ARG B 2 204 ? 167.886 148.512 119.191 1.00 61.29  ? 334 ARG D CG  1 
ATOM   5320 C CD  . ARG B 2 204 ? 167.808 147.329 118.231 1.00 62.80  ? 334 ARG D CD  1 
ATOM   5321 N NE  . ARG B 2 204 ? 166.477 146.737 118.163 1.00 59.65  ? 334 ARG D NE  1 
ATOM   5322 C CZ  . ARG B 2 204 ? 166.043 145.757 118.945 1.00 59.53  ? 334 ARG D CZ  1 
ATOM   5323 N NH1 . ARG B 2 204 ? 166.827 145.193 119.849 1.00 56.60  ? 334 ARG D NH1 1 
ATOM   5324 N NH2 . ARG B 2 204 ? 164.794 145.322 118.807 1.00 61.07  ? 334 ARG D NH2 1 
ATOM   5325 N N   . VAL B 2 205 ? 167.540 150.806 122.507 1.00 53.92  ? 335 VAL D N   1 
ATOM   5326 C CA  . VAL B 2 205 ? 167.007 152.160 122.469 1.00 53.21  ? 335 VAL D CA  1 
ATOM   5327 C C   . VAL B 2 205 ? 167.451 152.923 123.710 1.00 48.22  ? 335 VAL D C   1 
ATOM   5328 O O   . VAL B 2 205 ? 167.857 152.345 124.720 1.00 46.84  ? 335 VAL D O   1 
ATOM   5329 C CB  . VAL B 2 205 ? 165.471 152.167 122.353 1.00 53.48  ? 335 VAL D CB  1 
ATOM   5330 C CG1 . VAL B 2 205 ? 165.021 151.188 121.290 1.00 52.31  ? 335 VAL D CG1 1 
ATOM   5331 C CG2 . VAL B 2 205 ? 164.844 151.822 123.686 1.00 53.12  ? 335 VAL D CG2 1 
ATOM   5332 N N   . THR B 2 206 ? 167.397 154.257 123.639 1.00 47.15  ? 336 THR D N   1 
ATOM   5333 C CA  . THR B 2 206 ? 167.765 155.142 124.764 1.00 49.59  ? 336 THR D CA  1 
ATOM   5334 C C   . THR B 2 206 ? 166.776 156.281 124.788 1.00 52.55  ? 336 THR D C   1 
ATOM   5335 O O   . THR B 2 206 ? 166.735 157.032 123.794 1.00 54.98  ? 336 THR D O   1 
ATOM   5336 C CB  . THR B 2 206 ? 169.200 155.638 124.597 1.00 56.45  ? 336 THR D CB  1 
ATOM   5337 O OG1 . THR B 2 206 ? 170.043 154.553 124.969 1.00 63.06  ? 336 THR D OG1 1 
ATOM   5338 C CG2 . THR B 2 206 ? 169.508 156.837 125.475 1.00 56.94  ? 336 THR D CG2 1 
ATOM   5339 N N   . MET B 2 207 ? 166.005 156.415 125.868 1.00 50.84  ? 337 MET D N   1 
ATOM   5340 C CA  . MET B 2 207 ? 164.988 157.490 125.999 1.00 46.36  ? 337 MET D CA  1 
ATOM   5341 C C   . MET B 2 207 ? 165.540 158.547 126.962 1.00 48.00  ? 337 MET D C   1 
ATOM   5342 O O   . MET B 2 207 ? 165.699 158.219 128.154 1.00 49.03  ? 337 MET D O   1 
ATOM   5343 C CB  . MET B 2 207 ? 163.657 156.915 126.494 1.00 39.57  ? 337 MET D CB  1 
ATOM   5344 C CG  . MET B 2 207 ? 163.069 155.894 125.540 1.00 41.02  ? 337 MET D CG  1 
ATOM   5345 S SD  . MET B 2 207 ? 161.402 155.355 125.967 1.00 46.98  ? 337 MET D SD  1 
ATOM   5346 C CE  . MET B 2 207 ? 161.170 154.176 124.630 1.00 37.12  ? 337 MET D CE  1 
ATOM   5347 N N   . THR B 2 208 ? 165.861 159.742 126.463 1.00 49.71  ? 338 THR D N   1 
ATOM   5348 C CA  . THR B 2 208 ? 166.402 160.852 127.276 1.00 51.38  ? 338 THR D CA  1 
ATOM   5349 C C   . THR B 2 208 ? 165.420 161.994 127.203 1.00 53.26  ? 338 THR D C   1 
ATOM   5350 O O   . THR B 2 208 ? 164.355 161.804 126.579 1.00 51.63  ? 338 THR D O   1 
ATOM   5351 C CB  . THR B 2 208 ? 167.780 161.249 126.752 1.00 55.27  ? 338 THR D CB  1 
ATOM   5352 O OG1 . THR B 2 208 ? 167.534 161.793 125.460 1.00 58.16  ? 338 THR D OG1 1 
ATOM   5353 C CG2 . THR B 2 208 ? 168.726 160.067 126.656 1.00 54.54  ? 338 THR D CG2 1 
ATOM   5354 N N   . ARG B 2 209 ? 165.736 163.137 127.817 1.00 55.69  ? 339 ARG D N   1 
ATOM   5355 C CA  . ARG B 2 209 ? 164.849 164.328 127.765 1.00 58.39  ? 339 ARG D CA  1 
ATOM   5356 C C   . ARG B 2 209 ? 165.634 165.589 128.157 1.00 63.43  ? 339 ARG D C   1 
ATOM   5357 O O   . ARG B 2 209 ? 166.681 165.449 128.826 1.00 64.32  ? 339 ARG D O   1 
ATOM   5358 C CB  . ARG B 2 209 ? 163.646 164.123 128.694 1.00 55.98  ? 339 ARG D CB  1 
ATOM   5359 C CG  . ARG B 2 209 ? 163.942 163.837 130.159 1.00 53.75  ? 339 ARG D CG  1 
ATOM   5360 C CD  . ARG B 2 209 ? 164.092 165.108 130.978 1.00 56.64  ? 339 ARG D CD  1 
ATOM   5361 N NE  . ARG B 2 209 ? 164.301 164.868 132.411 1.00 53.52  ? 339 ARG D NE  1 
ATOM   5362 C CZ  . ARG B 2 209 ? 165.336 164.236 132.948 1.00 51.09  ? 339 ARG D CZ  1 
ATOM   5363 N NH1 . ARG B 2 209 ? 166.384 163.921 132.208 1.00 50.38  ? 339 ARG D NH1 1 
ATOM   5364 N NH2 . ARG B 2 209 ? 165.325 163.933 134.233 1.00 48.54  ? 339 ARG D NH2 1 
ATOM   5365 N N   . ASP B 2 210 ? 165.152 166.766 127.750 1.00 64.79  ? 340 ASP D N   1 
ATOM   5366 C CA  . ASP B 2 210 ? 165.796 168.044 128.163 1.00 67.63  ? 340 ASP D CA  1 
ATOM   5367 C C   . ASP B 2 210 ? 164.759 168.850 128.949 1.00 69.33  ? 340 ASP D C   1 
ATOM   5368 O O   . ASP B 2 210 ? 163.944 169.545 128.306 1.00 71.70  ? 340 ASP D O   1 
ATOM   5369 C CB  . ASP B 2 210 ? 166.349 168.807 126.970 1.00 72.00  ? 340 ASP D CB  1 
ATOM   5370 C CG  . ASP B 2 210 ? 167.235 169.997 127.310 1.00 75.05  ? 340 ASP D CG  1 
ATOM   5371 O OD1 . ASP B 2 210 ? 166.746 170.918 127.997 1.00 76.13  ? 340 ASP D OD1 1 
ATOM   5372 O OD2 . ASP B 2 210 ? 168.407 169.995 126.881 1.00 74.33  ? 340 ASP D OD2 1 
ATOM   5373 N N   . THR B 2 211 ? 164.787 168.761 130.280 1.00 69.43  ? 341 THR D N   1 
ATOM   5374 C CA  . THR B 2 211 ? 163.756 169.434 131.102 1.00 72.19  ? 341 THR D CA  1 
ATOM   5375 C C   . THR B 2 211 ? 163.802 170.930 130.885 1.00 71.99  ? 341 THR D C   1 
ATOM   5376 O O   . THR B 2 211 ? 162.725 171.512 130.630 1.00 71.24  ? 341 THR D O   1 
ATOM   5377 C CB  . THR B 2 211 ? 163.955 169.078 132.575 1.00 69.74  ? 341 THR D CB  1 
ATOM   5378 O OG1 . THR B 2 211 ? 163.638 167.695 132.683 1.00 60.16  ? 341 THR D OG1 1 
ATOM   5379 C CG2 . THR B 2 211 ? 163.045 169.871 133.494 1.00 64.14  ? 341 THR D CG2 1 
ATOM   5380 N N   . SER B 2 212 ? 164.985 171.547 130.969 1.00 72.00  ? 342 SER D N   1 
ATOM   5381 C CA  . SER B 2 212 ? 165.035 173.004 130.895 1.00 75.20  ? 342 SER D CA  1 
ATOM   5382 C C   . SER B 2 212 ? 164.183 173.540 129.750 1.00 73.96  ? 342 SER D C   1 
ATOM   5383 O O   . SER B 2 212 ? 163.470 174.538 129.911 1.00 71.95  ? 342 SER D O   1 
ATOM   5384 C CB  . SER B 2 212 ? 166.483 173.469 130.745 1.00 77.71  ? 342 SER D CB  1 
ATOM   5385 O OG  . SER B 2 212 ? 167.206 172.614 129.877 1.00 77.23  ? 342 SER D OG  1 
ATOM   5386 N N   . ILE B 2 213 ? 164.239 172.892 128.589 1.00 72.12  ? 343 ILE D N   1 
ATOM   5387 C CA  . ILE B 2 213 ? 163.542 173.356 127.397 1.00 71.18  ? 343 ILE D CA  1 
ATOM   5388 C C   . ILE B 2 213 ? 162.397 172.425 127.005 1.00 69.42  ? 343 ILE D C   1 
ATOM   5389 O O   . ILE B 2 213 ? 161.773 172.620 125.956 1.00 69.51  ? 343 ILE D O   1 
ATOM   5390 C CB  . ILE B 2 213 ? 164.541 173.602 126.247 1.00 73.32  ? 343 ILE D CB  1 
ATOM   5391 C CG1 . ILE B 2 213 ? 165.089 172.309 125.625 1.00 69.65  ? 343 ILE D CG1 1 
ATOM   5392 C CG2 . ILE B 2 213 ? 165.691 174.483 126.721 1.00 75.14  ? 343 ILE D CG2 1 
ATOM   5393 C CD1 . ILE B 2 213 ? 164.315 171.763 124.470 1.00 68.72  ? 343 ILE D CD1 1 
ATOM   5394 N N   . SER B 2 214 ? 162.086 171.437 127.848 1.00 68.32  ? 344 SER D N   1 
ATOM   5395 C CA  . SER B 2 214 ? 160.814 170.707 127.815 1.00 64.60  ? 344 SER D CA  1 
ATOM   5396 C C   . SER B 2 214 ? 160.615 169.914 126.522 1.00 64.03  ? 344 SER D C   1 
ATOM   5397 O O   . SER B 2 214 ? 159.625 170.087 125.807 1.00 63.32  ? 344 SER D O   1 
ATOM   5398 C CB  . SER B 2 214 ? 159.638 171.656 128.054 1.00 59.73  ? 344 SER D CB  1 
ATOM   5399 O OG  . SER B 2 214 ? 159.387 171.818 129.439 1.00 61.28  ? 344 SER D OG  1 
ATOM   5400 N N   . THR B 2 215 ? 161.567 169.032 126.223 1.00 63.35  ? 345 THR D N   1 
ATOM   5401 C CA  . THR B 2 215 ? 161.361 167.966 125.252 1.00 60.57  ? 345 THR D CA  1 
ATOM   5402 C C   . THR B 2 215 ? 161.976 166.681 125.780 1.00 60.29  ? 345 THR D C   1 
ATOM   5403 O O   . THR B 2 215 ? 162.928 166.705 126.564 1.00 59.83  ? 345 THR D O   1 
ATOM   5404 C CB  . THR B 2 215 ? 161.965 168.258 123.868 1.00 64.72  ? 345 THR D CB  1 
ATOM   5405 O OG1 . THR B 2 215 ? 163.347 167.881 123.857 1.00 64.65  ? 345 THR D OG1 1 
ATOM   5406 C CG2 . THR B 2 215 ? 161.815 169.708 123.477 1.00 66.96  ? 345 THR D CG2 1 
ATOM   5407 N N   . ALA B 2 216 ? 161.418 165.557 125.338 1.00 59.10  ? 346 ALA D N   1 
ATOM   5408 C CA  . ALA B 2 216 ? 161.946 164.235 125.641 1.00 56.47  ? 346 ALA D CA  1 
ATOM   5409 C C   . ALA B 2 216 ? 162.333 163.565 124.333 1.00 54.54  ? 346 ALA D C   1 
ATOM   5410 O O   . ALA B 2 216 ? 161.489 163.394 123.447 1.00 53.20  ? 346 ALA D O   1 
ATOM   5411 C CB  . ALA B 2 216 ? 160.926 163.392 126.405 1.00 49.43  ? 346 ALA D CB  1 
ATOM   5412 N N   . TYR B 2 217 ? 163.593 163.137 124.207 1.00 53.22  ? 347 TYR D N   1 
ATOM   5413 C CA  . TYR B 2 217 ? 164.093 162.534 122.941 1.00 51.75  ? 347 TYR D CA  1 
ATOM   5414 C C   . TYR B 2 217 ? 164.029 161.014 123.023 1.00 45.70  ? 347 TYR D C   1 
ATOM   5415 O O   . TYR B 2 217 ? 163.705 160.481 124.108 1.00 45.95  ? 347 TYR D O   1 
ATOM   5416 C CB  . TYR B 2 217 ? 165.530 162.985 122.677 1.00 57.08  ? 347 TYR D CB  1 
ATOM   5417 C CG  . TYR B 2 217 ? 165.775 164.459 122.955 1.00 58.12  ? 347 TYR D CG  1 
ATOM   5418 C CD1 . TYR B 2 217 ? 165.581 165.419 121.971 1.00 59.20  ? 347 TYR D CD1 1 
ATOM   5419 C CD2 . TYR B 2 217 ? 166.198 164.886 124.207 1.00 56.71  ? 347 TYR D CD2 1 
ATOM   5420 C CE1 . TYR B 2 217 ? 165.807 166.761 122.222 1.00 61.99  ? 347 TYR D CE1 1 
ATOM   5421 C CE2 . TYR B 2 217 ? 166.422 166.224 124.472 1.00 61.80  ? 347 TYR D CE2 1 
ATOM   5422 C CZ  . TYR B 2 217 ? 166.230 167.165 123.476 1.00 64.92  ? 347 TYR D CZ  1 
ATOM   5423 O OH  . TYR B 2 217 ? 166.447 168.487 123.732 1.00 66.92  ? 347 TYR D OH  1 
ATOM   5424 N N   . MET B 2 218 ? 164.319 160.331 121.912 1.00 46.33  ? 348 MET D N   1 
ATOM   5425 C CA  . MET B 2 218 ? 164.301 158.845 121.863 1.00 45.45  ? 348 MET D CA  1 
ATOM   5426 C C   . MET B 2 218 ? 165.396 158.383 120.888 1.00 53.90  ? 348 MET D C   1 
ATOM   5427 O O   . MET B 2 218 ? 165.084 158.198 119.690 1.00 57.26  ? 348 MET D O   1 
ATOM   5428 C CB  . MET B 2 218 ? 162.908 158.349 121.454 1.00 43.09  ? 348 MET D CB  1 
ATOM   5429 C CG  . MET B 2 218 ? 162.683 156.862 121.659 1.00 40.37  ? 348 MET D CG  1 
ATOM   5430 S SD  . MET B 2 218 ? 163.127 155.858 120.228 1.00 46.26  ? 348 MET D SD  1 
ATOM   5431 C CE  . MET B 2 218 ? 161.873 156.380 119.051 1.00 48.24  ? 348 MET D CE  1 
ATOM   5432 N N   . GLU B 2 219 ? 166.630 158.220 121.374 1.00 56.34  ? 349 GLU D N   1 
ATOM   5433 C CA  . GLU B 2 219 ? 167.773 157.781 120.529 1.00 57.02  ? 349 GLU D CA  1 
ATOM   5434 C C   . GLU B 2 219 ? 167.717 156.259 120.350 1.00 56.10  ? 349 GLU D C   1 
ATOM   5435 O O   . GLU B 2 219 ? 168.197 155.541 121.252 1.00 55.92  ? 349 GLU D O   1 
ATOM   5436 C CB  . GLU B 2 219 ? 169.120 158.147 121.150 1.00 58.89  ? 349 GLU D CB  1 
ATOM   5437 C CG  . GLU B 2 219 ? 169.356 159.650 121.241 1.00 62.30  ? 349 GLU D CG  1 
ATOM   5438 C CD  . GLU B 2 219 ? 168.992 160.244 122.588 1.00 61.65  ? 349 GLU D CD  1 
ATOM   5439 O OE1 . GLU B 2 219 ? 169.629 159.870 123.595 1.00 63.07  ? 349 GLU D OE1 1 
ATOM   5440 O OE2 . GLU B 2 219 ? 168.065 161.073 122.629 1.00 58.65  ? 349 GLU D OE2 1 
ATOM   5441 N N   . LEU B 2 220 ? 167.167 155.790 119.229 1.00 57.70  ? 350 LEU D N   1 
ATOM   5442 C CA  . LEU B 2 220 ? 167.097 154.336 118.935 1.00 59.40  ? 350 LEU D CA  1 
ATOM   5443 C C   . LEU B 2 220 ? 168.358 153.946 118.153 1.00 64.57  ? 350 LEU D C   1 
ATOM   5444 O O   . LEU B 2 220 ? 168.422 154.281 116.951 1.00 68.84  ? 350 LEU D O   1 
ATOM   5445 C CB  . LEU B 2 220 ? 165.818 154.035 118.157 1.00 54.81  ? 350 LEU D CB  1 
ATOM   5446 C CG  . LEU B 2 220 ? 165.616 152.580 117.725 1.00 56.37  ? 350 LEU D CG  1 
ATOM   5447 C CD1 . LEU B 2 220 ? 164.142 152.228 117.745 1.00 51.64  ? 350 LEU D CD1 1 
ATOM   5448 C CD2 . LEU B 2 220 ? 166.207 152.332 116.350 1.00 65.95  ? 350 LEU D CD2 1 
ATOM   5449 N N   . SER B 2 221 ? 169.324 153.284 118.801 1.00 63.01  ? 351 SER D N   1 
ATOM   5450 C CA  . SER B 2 221 ? 170.553 152.865 118.149 1.00 66.74  ? 351 SER D CA  1 
ATOM   5451 C C   . SER B 2 221 ? 170.354 151.529 117.439 1.00 71.34  ? 351 SER D C   1 
ATOM   5452 O O   . SER B 2 221 ? 169.361 150.828 117.643 1.00 70.32  ? 351 SER D O   1 
ATOM   5453 C CB  . SER B 2 221 ? 171.689 152.766 119.166 1.00 67.88  ? 351 SER D CB  1 
ATOM   5454 O OG  . SER B 2 221 ? 171.226 152.233 120.394 1.00 67.16  ? 351 SER D OG  1 
ATOM   5455 N N   . ARG B 2 222 ? 171.323 151.183 116.592 1.00 73.09  ? 352 ARG D N   1 
ATOM   5456 C CA  . ARG B 2 222 ? 171.346 149.912 115.868 1.00 74.28  ? 352 ARG D CA  1 
ATOM   5457 C C   . ARG B 2 222 ? 170.045 149.690 115.096 1.00 76.52  ? 352 ARG D C   1 
ATOM   5458 O O   . ARG B 2 222 ? 169.290 148.748 115.344 1.00 74.60  ? 352 ARG D O   1 
ATOM   5459 C CB  . ARG B 2 222 ? 171.627 148.747 116.821 1.00 71.15  ? 352 ARG D CB  1 
ATOM   5460 C CG  . ARG B 2 222 ? 172.671 149.048 117.884 1.00 68.77  ? 352 ARG D CG  1 
ATOM   5461 C CD  . ARG B 2 222 ? 173.463 147.805 118.245 1.00 67.64  ? 352 ARG D CD  1 
ATOM   5462 N NE  . ARG B 2 222 ? 172.596 146.659 118.487 1.00 69.89  ? 352 ARG D NE  1 
ATOM   5463 C CZ  . ARG B 2 222 ? 172.257 146.218 119.691 1.00 69.43  ? 352 ARG D CZ  1 
ATOM   5464 N NH1 . ARG B 2 222 ? 172.691 146.811 120.791 1.00 67.51  ? 352 ARG D NH1 1 
ATOM   5465 N NH2 . ARG B 2 222 ? 171.464 145.156 119.793 1.00 67.71  ? 352 ARG D NH2 1 
ATOM   5466 N N   . LEU B 2 223 ? 169.791 150.588 114.149 1.00 78.33  ? 353 LEU D N   1 
ATOM   5467 C CA  . LEU B 2 223 ? 168.592 150.491 113.329 1.00 75.72  ? 353 LEU D CA  1 
ATOM   5468 C C   . LEU B 2 223 ? 168.649 149.255 112.441 1.00 78.54  ? 353 LEU D C   1 
ATOM   5469 O O   . LEU B 2 223 ? 169.716 148.860 111.964 1.00 80.44  ? 353 LEU D O   1 
ATOM   5470 C CB  . LEU B 2 223 ? 168.430 151.746 112.474 1.00 75.75  ? 353 LEU D CB  1 
ATOM   5471 C CG  . LEU B 2 223 ? 167.845 152.964 113.189 1.00 72.14  ? 353 LEU D CG  1 
ATOM   5472 C CD1 . LEU B 2 223 ? 168.400 154.250 112.599 1.00 72.45  ? 353 LEU D CD1 1 
ATOM   5473 C CD2 . LEU B 2 223 ? 166.329 152.944 113.113 1.00 73.98  ? 353 LEU D CD2 1 
ATOM   5474 N N   . ARG B 2 224 ? 167.489 148.641 112.225 1.00 76.37  ? 354 ARG D N   1 
ATOM   5475 C CA  . ARG B 2 224 ? 167.377 147.427 111.431 1.00 75.93  ? 354 ARG D CA  1 
ATOM   5476 C C   . ARG B 2 224 ? 166.315 147.620 110.357 1.00 74.21  ? 354 ARG D C   1 
ATOM   5477 O O   . ARG B 2 224 ? 165.608 148.630 110.323 1.00 76.04  ? 354 ARG D O   1 
ATOM   5478 C CB  . ARG B 2 224 ? 167.045 146.214 112.311 1.00 75.91  ? 354 ARG D CB  1 
ATOM   5479 C CG  . ARG B 2 224 ? 168.065 145.960 113.411 1.00 78.97  ? 354 ARG D CG  1 
ATOM   5480 C CD  . ARG B 2 224 ? 167.613 144.885 114.391 1.00 74.97  ? 354 ARG D CD  1 
ATOM   5481 N NE  . ARG B 2 224 ? 166.204 144.998 114.744 1.00 76.43  ? 354 ARG D NE  1 
ATOM   5482 C CZ  . ARG B 2 224 ? 165.254 144.179 114.313 1.00 79.71  ? 354 ARG D CZ  1 
ATOM   5483 N NH1 . ARG B 2 224 ? 165.528 143.171 113.501 1.00 80.45  ? 354 ARG D NH1 1 
ATOM   5484 N NH2 . ARG B 2 224 ? 163.999 144.376 114.707 1.00 78.79  ? 354 ARG D NH2 1 
ATOM   5485 N N   . SER B 2 225 ? 166.216 146.629 109.468 1.00 75.86  ? 355 SER D N   1 
ATOM   5486 C CA  . SER B 2 225 ? 165.280 146.722 108.351 1.00 77.90  ? 355 SER D CA  1 
ATOM   5487 C C   . SER B 2 225 ? 163.836 146.776 108.834 1.00 75.56  ? 355 SER D C   1 
ATOM   5488 O O   . SER B 2 225 ? 163.021 147.532 108.293 1.00 75.14  ? 355 SER D O   1 
ATOM   5489 C CB  . SER B 2 225 ? 165.483 145.544 107.399 1.00 76.62  ? 355 SER D CB  1 
ATOM   5490 O OG  . SER B 2 225 ? 164.257 145.151 106.806 1.00 69.26  ? 355 SER D OG  1 
ATOM   5491 N N   . ASP B 2 226 ? 163.500 145.983 109.848 1.00 73.50  ? 356 ASP D N   1 
ATOM   5492 C CA  . ASP B 2 226 ? 162.140 145.909 110.360 1.00 72.20  ? 356 ASP D CA  1 
ATOM   5493 C C   . ASP B 2 226 ? 161.871 146.914 111.472 1.00 71.08  ? 356 ASP D C   1 
ATOM   5494 O O   . ASP B 2 226 ? 160.794 146.877 112.076 1.00 69.49  ? 356 ASP D O   1 
ATOM   5495 C CB  . ASP B 2 226 ? 161.838 144.493 110.857 1.00 74.51  ? 356 ASP D CB  1 
ATOM   5496 C CG  . ASP B 2 226 ? 162.937 143.941 111.740 1.00 80.13  ? 356 ASP D CG  1 
ATOM   5497 O OD1 . ASP B 2 226 ? 164.117 144.011 111.338 1.00 81.95  ? 356 ASP D OD1 1 
ATOM   5498 O OD2 . ASP B 2 226 ? 162.620 143.436 112.838 1.00 79.96  ? 356 ASP D OD2 1 
ATOM   5499 N N   . ASP B 2 227 ? 162.818 147.805 111.758 1.00 71.63  ? 357 ASP D N   1 
ATOM   5500 C CA  . ASP B 2 227 ? 162.625 148.818 112.787 1.00 67.14  ? 357 ASP D CA  1 
ATOM   5501 C C   . ASP B 2 227 ? 161.887 150.046 112.276 1.00 61.83  ? 357 ASP D C   1 
ATOM   5502 O O   . ASP B 2 227 ? 161.676 150.986 113.051 1.00 60.95  ? 357 ASP D O   1 
ATOM   5503 C CB  . ASP B 2 227 ? 163.973 149.237 113.379 1.00 72.41  ? 357 ASP D CB  1 
ATOM   5504 C CG  . ASP B 2 227 ? 164.126 148.821 114.828 1.00 71.76  ? 357 ASP D CG  1 
ATOM   5505 O OD1 . ASP B 2 227 ? 163.244 148.096 115.335 1.00 70.36  ? 357 ASP D OD1 1 
ATOM   5506 O OD2 . ASP B 2 227 ? 165.125 149.219 115.463 1.00 68.77  ? 357 ASP D OD2 1 
ATOM   5507 N N   . THR B 2 228 ? 161.502 150.070 111.003 1.00 63.87  ? 358 THR D N   1 
ATOM   5508 C CA  . THR B 2 228 ? 160.716 151.180 110.482 1.00 65.75  ? 358 THR D CA  1 
ATOM   5509 C C   . THR B 2 228 ? 159.342 151.205 111.142 1.00 64.86  ? 358 THR D C   1 
ATOM   5510 O O   . THR B 2 228 ? 158.660 150.179 111.226 1.00 67.41  ? 358 THR D O   1 
ATOM   5511 C CB  . THR B 2 228 ? 160.584 151.077 108.961 1.00 70.46  ? 358 THR D CB  1 
ATOM   5512 O OG1 . THR B 2 228 ? 159.708 152.105 108.483 1.00 70.51  ? 358 THR D OG1 1 
ATOM   5513 C CG2 . THR B 2 228 ? 160.055 149.709 108.541 1.00 67.42  ? 358 THR D CG2 1 
ATOM   5514 N N   . ALA B 2 229 ? 158.942 152.379 111.619 1.00 59.34  ? 359 ALA D N   1 
ATOM   5515 C CA  . ALA B 2 229 ? 157.697 152.532 112.363 1.00 55.21  ? 359 ALA D CA  1 
ATOM   5516 C C   . ALA B 2 229 ? 157.414 154.020 112.520 1.00 50.90  ? 359 ALA D C   1 
ATOM   5517 O O   . ALA B 2 229 ? 158.187 154.873 112.072 1.00 55.56  ? 359 ALA D O   1 
ATOM   5518 C CB  . ALA B 2 229 ? 157.768 151.837 113.724 1.00 52.79  ? 359 ALA D CB  1 
ATOM   5519 N N   . VAL B 2 230 ? 156.293 154.323 113.165 1.00 49.09  ? 360 VAL D N   1 
ATOM   5520 C CA  . VAL B 2 230 ? 155.894 155.687 113.486 1.00 47.89  ? 360 VAL D CA  1 
ATOM   5521 C C   . VAL B 2 230 ? 155.915 155.803 115.003 1.00 42.94  ? 360 VAL D C   1 
ATOM   5522 O O   . VAL B 2 230 ? 155.031 155.274 115.686 1.00 44.32  ? 360 VAL D O   1 
ATOM   5523 C CB  . VAL B 2 230 ? 154.510 156.023 112.915 1.00 51.60  ? 360 VAL D CB  1 
ATOM   5524 C CG1 . VAL B 2 230 ? 154.070 157.400 113.367 1.00 52.88  ? 360 VAL D CG1 1 
ATOM   5525 C CG2 . VAL B 2 230 ? 154.525 155.934 111.398 1.00 50.83  ? 360 VAL D CG2 1 
ATOM   5526 N N   . TYR B 2 231 ? 156.988 156.421 115.520 1.00 40.31  ? 361 TYR D N   1 
ATOM   5527 C CA  . TYR B 2 231 ? 157.231 156.506 116.984 1.00 39.06  ? 361 TYR D CA  1 
ATOM   5528 C C   . TYR B 2 231 ? 156.412 157.604 117.630 1.00 39.75  ? 361 TYR D C   1 
ATOM   5529 O O   . TYR B 2 231 ? 156.957 158.705 117.854 1.00 43.76  ? 361 TYR D O   1 
ATOM   5530 C CB  . TYR B 2 231 ? 158.728 156.775 117.163 1.00 38.36  ? 361 TYR D CB  1 
ATOM   5531 C CG  . TYR B 2 231 ? 159.656 155.734 116.553 1.00 43.27  ? 361 TYR D CG  1 
ATOM   5532 C CD1 . TYR B 2 231 ? 160.737 156.115 115.769 1.00 49.32  ? 361 TYR D CD1 1 
ATOM   5533 C CD2 . TYR B 2 231 ? 159.472 154.378 116.785 1.00 43.43  ? 361 TYR D CD2 1 
ATOM   5534 C CE1 . TYR B 2 231 ? 161.597 155.180 115.220 1.00 51.18  ? 361 TYR D CE1 1 
ATOM   5535 C CE2 . TYR B 2 231 ? 160.326 153.431 116.246 1.00 44.25  ? 361 TYR D CE2 1 
ATOM   5536 C CZ  . TYR B 2 231 ? 161.390 153.834 115.459 1.00 47.95  ? 361 TYR D CZ  1 
ATOM   5537 O OH  . TYR B 2 231 ? 162.240 152.914 114.920 1.00 56.94  ? 361 TYR D OH  1 
ATOM   5538 N N   . TYR B 2 232 ? 155.148 157.334 117.952 1.00 37.55  ? 362 TYR D N   1 
ATOM   5539 C CA  . TYR B 2 232 ? 154.323 158.296 118.668 1.00 35.85  ? 362 TYR D CA  1 
ATOM   5540 C C   . TYR B 2 232 ? 154.833 158.480 120.090 1.00 32.71  ? 362 TYR D C   1 
ATOM   5541 O O   . TYR B 2 232 ? 155.173 157.512 120.773 1.00 35.13  ? 362 TYR D O   1 
ATOM   5542 C CB  . TYR B 2 232 ? 152.868 157.834 118.706 1.00 36.39  ? 362 TYR D CB  1 
ATOM   5543 C CG  . TYR B 2 232 ? 152.264 157.534 117.357 1.00 41.18  ? 362 TYR D CG  1 
ATOM   5544 C CD1 . TYR B 2 232 ? 151.629 158.524 116.625 1.00 47.00  ? 362 TYR D CD1 1 
ATOM   5545 C CD2 . TYR B 2 232 ? 152.321 156.259 116.820 1.00 43.15  ? 362 TYR D CD2 1 
ATOM   5546 C CE1 . TYR B 2 232 ? 151.073 158.253 115.393 1.00 51.49  ? 362 TYR D CE1 1 
ATOM   5547 C CE2 . TYR B 2 232 ? 151.769 155.978 115.590 1.00 48.46  ? 362 TYR D CE2 1 
ATOM   5548 C CZ  . TYR B 2 232 ? 151.145 156.978 114.880 1.00 53.51  ? 362 TYR D CZ  1 
ATOM   5549 O OH  . TYR B 2 232 ? 150.592 156.700 113.652 1.00 57.20  ? 362 TYR D OH  1 
ATOM   5550 N N   . CYS B 2 233 ? 154.891 159.732 120.536 1.00 31.12  ? 363 CYS D N   1 
ATOM   5551 C CA  . CYS B 2 233 ? 155.270 160.037 121.914 1.00 30.10  ? 363 CYS D CA  1 
ATOM   5552 C C   . CYS B 2 233 ? 154.019 160.334 122.738 1.00 29.89  ? 363 CYS D C   1 
ATOM   5553 O O   . CYS B 2 233 ? 153.715 161.472 123.093 1.00 35.11  ? 363 CYS D O   1 
ATOM   5554 C CB  . CYS B 2 233 ? 156.256 161.199 121.948 1.00 34.25  ? 363 CYS D CB  1 
ATOM   5555 S SG  . CYS B 2 233 ? 155.689 162.690 121.111 1.00 55.78  ? 363 CYS D SG  1 
ATOM   5556 N N   . ALA B 2 234 ? 153.280 159.268 123.051 1.00 26.88  ? 364 ALA D N   1 
ATOM   5557 C CA  . ALA B 2 234 ? 152.026 159.435 123.822 1.00 28.00  ? 364 ALA D CA  1 
ATOM   5558 C C   . ALA B 2 234 ? 152.342 159.846 125.262 1.00 25.53  ? 364 ALA D C   1 
ATOM   5559 O O   . ALA B 2 234 ? 153.462 159.570 125.743 1.00 27.70  ? 364 ALA D O   1 
ATOM   5560 C CB  . ALA B 2 234 ? 151.228 158.153 123.772 1.00 31.77  ? 364 ALA D CB  1 
ATOM   5561 N N   . ARG B 2 235 ? 151.380 160.479 125.938 1.00 22.49  ? 365 ARG D N   1 
ATOM   5562 C CA  . ARG B 2 235 ? 151.581 160.927 127.341 1.00 22.70  ? 365 ARG D CA  1 
ATOM   5563 C C   . ARG B 2 235 ? 150.587 160.188 128.243 1.00 26.23  ? 365 ARG D C   1 
ATOM   5564 O O   . ARG B 2 235 ? 149.372 160.335 128.007 1.00 30.06  ? 365 ARG D O   1 
ATOM   5565 C CB  . ARG B 2 235 ? 151.343 162.435 127.431 1.00 26.97  ? 365 ARG D CB  1 
ATOM   5566 C CG  . ARG B 2 235 ? 151.733 163.055 128.764 1.00 33.12  ? 365 ARG D CG  1 
ATOM   5567 C CD  . ARG B 2 235 ? 151.039 164.389 128.975 1.00 38.79  ? 365 ARG D CD  1 
ATOM   5568 N NE  . ARG B 2 235 ? 149.616 164.224 129.290 1.00 35.86  ? 365 ARG D NE  1 
ATOM   5569 C CZ  . ARG B 2 235 ? 148.797 165.222 129.586 1.00 40.45  ? 365 ARG D CZ  1 
ATOM   5570 N NH1 . ARG B 2 235 ? 149.201 166.472 129.450 1.00 44.67  ? 365 ARG D NH1 1 
ATOM   5571 N NH2 . ARG B 2 235 ? 147.577 164.968 130.023 1.00 39.99  ? 365 ARG D NH2 1 
ATOM   5572 N N   . SER B 2 236 ? 151.070 159.441 129.241 1.00 25.19  ? 366 SER D N   1 
ATOM   5573 C CA  . SER B 2 236 ? 150.162 158.646 130.057 1.00 24.65  ? 366 SER D CA  1 
ATOM   5574 C C   . SER B 2 236 ? 149.256 159.546 130.885 1.00 30.42  ? 366 SER D C   1 
ATOM   5575 O O   . SER B 2 236 ? 149.724 160.478 131.544 1.00 34.57  ? 366 SER D O   1 
ATOM   5576 C CB  . SER B 2 236 ? 150.953 157.714 130.972 1.00 21.99  ? 366 SER D CB  1 
ATOM   5577 O OG  . SER B 2 236 ? 150.203 157.364 132.119 1.00 24.73  ? 366 SER D OG  1 
ATOM   5578 N N   . GLY B 2 237 ? 147.958 159.246 130.849 1.00 31.24  ? 367 GLY D N   1 
ATOM   5579 C CA  . GLY B 2 237 ? 146.994 160.058 131.608 1.00 31.76  ? 367 GLY D CA  1 
ATOM   5580 C C   . GLY B 2 237 ? 146.852 159.572 133.033 1.00 30.50  ? 367 GLY D C   1 
ATOM   5581 O O   . GLY B 2 237 ? 147.706 158.776 133.479 1.00 29.37  ? 367 GLY D O   1 
ATOM   5582 N N   . GLY B 2 238 ? 145.809 160.027 133.722 1.00 31.80  ? 368 GLY D N   1 
ATOM   5583 C CA  . GLY B 2 238 ? 145.558 159.654 135.125 1.00 34.32  ? 368 GLY D CA  1 
ATOM   5584 C C   . GLY B 2 238 ? 145.097 158.216 135.238 1.00 35.67  ? 368 GLY D C   1 
ATOM   5585 O O   . GLY B 2 238 ? 145.916 157.381 135.679 1.00 37.17  ? 368 GLY D O   1 
ATOM   5586 N N   . PRO B 2 239 ? 143.842 157.866 134.870 1.00 34.09  ? 369 PRO D N   1 
ATOM   5587 C CA  . PRO B 2 239 ? 143.411 156.477 134.918 1.00 31.32  ? 369 PRO D CA  1 
ATOM   5588 C C   . PRO B 2 239 ? 143.508 155.750 133.577 1.00 32.27  ? 369 PRO D C   1 
ATOM   5589 O O   . PRO B 2 239 ? 143.039 154.601 133.492 1.00 31.21  ? 369 PRO D O   1 
ATOM   5590 C CB  . PRO B 2 239 ? 141.960 156.647 135.376 1.00 34.06  ? 369 PRO D CB  1 
ATOM   5591 C CG  . PRO B 2 239 ? 141.500 157.903 134.672 1.00 34.75  ? 369 PRO D CG  1 
ATOM   5592 C CD  . PRO B 2 239 ? 142.744 158.756 134.482 1.00 34.57  ? 369 PRO D CD  1 
ATOM   5593 N N   . TYR B 2 240 ? 144.070 156.408 132.562 1.00 35.13  ? 370 TYR D N   1 
ATOM   5594 C CA  . TYR B 2 240 ? 144.162 155.791 131.211 1.00 34.85  ? 370 TYR D CA  1 
ATOM   5595 C C   . TYR B 2 240 ? 145.538 156.091 130.624 1.00 34.31  ? 370 TYR D C   1 
ATOM   5596 O O   . TYR B 2 240 ? 146.192 157.061 131.060 1.00 34.37  ? 370 TYR D O   1 
ATOM   5597 C CB  . TYR B 2 240 ? 143.020 156.278 130.314 1.00 34.80  ? 370 TYR D CB  1 
ATOM   5598 C CG  . TYR B 2 240 ? 142.729 157.771 130.386 1.00 34.90  ? 370 TYR D CG  1 
ATOM   5599 C CD1 . TYR B 2 240 ? 143.436 158.678 129.609 1.00 35.27  ? 370 TYR D CD1 1 
ATOM   5600 C CD2 . TYR B 2 240 ? 141.727 158.267 131.210 1.00 37.04  ? 370 TYR D CD2 1 
ATOM   5601 C CE1 . TYR B 2 240 ? 143.168 160.035 129.667 1.00 38.83  ? 370 TYR D CE1 1 
ATOM   5602 C CE2 . TYR B 2 240 ? 141.448 159.622 131.275 1.00 35.91  ? 370 TYR D CE2 1 
ATOM   5603 C CZ  . TYR B 2 240 ? 142.173 160.509 130.502 1.00 37.40  ? 370 TYR D CZ  1 
ATOM   5604 O OH  . TYR B 2 240 ? 141.906 161.847 130.559 1.00 39.98  ? 370 TYR D OH  1 
ATOM   5605 N N   . PHE B 2 241 ? 145.971 155.275 129.663 1.00 31.78  ? 371 PHE D N   1 
ATOM   5606 C CA  . PHE B 2 241 ? 147.320 155.451 129.066 1.00 29.51  ? 371 PHE D CA  1 
ATOM   5607 C C   . PHE B 2 241 ? 147.236 156.359 127.854 1.00 29.60  ? 371 PHE D C   1 
ATOM   5608 O O   . PHE B 2 241 ? 146.129 156.508 127.291 1.00 35.50  ? 371 PHE D O   1 
ATOM   5609 C CB  . PHE B 2 241 ? 147.852 154.095 128.595 1.00 30.79  ? 371 PHE D CB  1 
ATOM   5610 C CG  . PHE B 2 241 ? 148.223 153.087 129.674 1.00 28.33  ? 371 PHE D CG  1 
ATOM   5611 C CD1 . PHE B 2 241 ? 147.242 152.430 130.408 1.00 30.36  ? 371 PHE D CD1 1 
ATOM   5612 C CD2 . PHE B 2 241 ? 149.552 152.752 129.906 1.00 25.36  ? 371 PHE D CD2 1 
ATOM   5613 C CE1 . PHE B 2 241 ? 147.583 151.498 131.374 1.00 31.73  ? 371 PHE D CE1 1 
ATOM   5614 C CE2 . PHE B 2 241 ? 149.886 151.813 130.868 1.00 26.60  ? 371 PHE D CE2 1 
ATOM   5615 C CZ  . PHE B 2 241 ? 148.903 151.190 131.600 1.00 29.93  ? 371 PHE D CZ  1 
ATOM   5616 N N   . PHE B 2 242 ? 148.358 156.973 127.472 1.00 28.54  ? 372 PHE D N   1 
ATOM   5617 C CA  . PHE B 2 242 ? 148.400 157.770 126.216 1.00 33.46  ? 372 PHE D CA  1 
ATOM   5618 C C   . PHE B 2 242 ? 147.234 158.756 126.150 1.00 35.68  ? 372 PHE D C   1 
ATOM   5619 O O   . PHE B 2 242 ? 146.503 158.752 125.135 1.00 35.94  ? 372 PHE D O   1 
ATOM   5620 C CB  . PHE B 2 242 ? 148.371 156.750 125.075 1.00 29.86  ? 372 PHE D CB  1 
ATOM   5621 C CG  . PHE B 2 242 ? 149.240 155.516 125.286 1.00 28.89  ? 372 PHE D CG  1 
ATOM   5622 C CD1 . PHE B 2 242 ? 150.465 155.599 125.940 1.00 27.70  ? 372 PHE D CD1 1 
ATOM   5623 C CD2 . PHE B 2 242 ? 148.817 154.267 124.847 1.00 33.24  ? 372 PHE D CD2 1 
ATOM   5624 C CE1 . PHE B 2 242 ? 151.243 154.470 126.136 1.00 28.24  ? 372 PHE D CE1 1 
ATOM   5625 C CE2 . PHE B 2 242 ? 149.601 153.143 125.046 1.00 31.34  ? 372 PHE D CE2 1 
ATOM   5626 C CZ  . PHE B 2 242 ? 150.811 153.245 125.689 1.00 30.91  ? 372 PHE D CZ  1 
ATOM   5627 N N   . ASP B 2 243 ? 147.062 159.580 127.187 1.00 32.79  ? 373 ASP D N   1 
ATOM   5628 C CA  . ASP B 2 243 ? 146.000 160.625 127.163 1.00 33.00  ? 373 ASP D CA  1 
ATOM   5629 C C   . ASP B 2 243 ? 146.211 161.513 125.932 1.00 40.38  ? 373 ASP D C   1 
ATOM   5630 O O   . ASP B 2 243 ? 145.232 161.729 125.184 1.00 45.99  ? 373 ASP D O   1 
ATOM   5631 C CB  . ASP B 2 243 ? 145.977 161.404 128.469 1.00 34.81  ? 373 ASP D CB  1 
ATOM   5632 C CG  . ASP B 2 243 ? 145.127 162.666 128.476 1.00 39.01  ? 373 ASP D CG  1 
ATOM   5633 O OD1 . ASP B 2 243 ? 143.944 162.580 128.091 1.00 38.53  ? 373 ASP D OD1 1 
ATOM   5634 O OD2 . ASP B 2 243 ? 145.647 163.717 128.898 1.00 38.35  ? 373 ASP D OD2 1 
ATOM   5635 N N   . TYR B 2 244 ? 147.437 162.003 125.732 1.00 39.97  ? 374 TYR D N   1 
ATOM   5636 C CA  . TYR B 2 244 ? 147.768 162.848 124.548 1.00 39.89  ? 374 TYR D CA  1 
ATOM   5637 C C   . TYR B 2 244 ? 148.781 162.105 123.680 1.00 38.76  ? 374 TYR D C   1 
ATOM   5638 O O   . TYR B 2 244 ? 149.289 161.059 124.129 1.00 40.73  ? 374 TYR D O   1 
ATOM   5639 C CB  . TYR B 2 244 ? 148.297 164.234 124.927 1.00 41.13  ? 374 TYR D CB  1 
ATOM   5640 C CG  . TYR B 2 244 ? 147.225 165.218 125.373 1.00 45.58  ? 374 TYR D CG  1 
ATOM   5641 C CD1 . TYR B 2 244 ? 146.499 165.954 124.445 1.00 45.84  ? 374 TYR D CD1 1 
ATOM   5642 C CD2 . TYR B 2 244 ? 146.953 165.424 126.718 1.00 46.14  ? 374 TYR D CD2 1 
ATOM   5643 C CE1 . TYR B 2 244 ? 145.523 166.853 124.843 1.00 46.18  ? 374 TYR D CE1 1 
ATOM   5644 C CE2 . TYR B 2 244 ? 145.982 166.321 127.129 1.00 46.64  ? 374 TYR D CE2 1 
ATOM   5645 C CZ  . TYR B 2 244 ? 145.266 167.039 126.189 1.00 47.59  ? 374 TYR D CZ  1 
ATOM   5646 O OH  . TYR B 2 244 ? 144.308 167.926 126.588 1.00 44.78  ? 374 TYR D OH  1 
ATOM   5647 N N   . TRP B 2 245 ? 149.083 162.630 122.489 1.00 38.66  ? 375 TRP D N   1 
ATOM   5648 C CA  . TRP B 2 245 ? 149.982 161.928 121.536 1.00 39.28  ? 375 TRP D CA  1 
ATOM   5649 C C   . TRP B 2 245 ? 150.765 162.937 120.697 1.00 44.29  ? 375 TRP D C   1 
ATOM   5650 O O   . TRP B 2 245 ? 150.366 164.121 120.667 1.00 51.80  ? 375 TRP D O   1 
ATOM   5651 C CB  . TRP B 2 245 ? 149.152 161.033 120.606 1.00 40.42  ? 375 TRP D CB  1 
ATOM   5652 C CG  . TRP B 2 245 ? 148.508 159.835 121.252 1.00 39.51  ? 375 TRP D CG  1 
ATOM   5653 C CD1 . TRP B 2 245 ? 147.442 159.826 122.103 1.00 38.62  ? 375 TRP D CD1 1 
ATOM   5654 C CD2 . TRP B 2 245 ? 148.853 158.450 121.031 1.00 38.68  ? 375 TRP D CD2 1 
ATOM   5655 N NE1 . TRP B 2 245 ? 147.122 158.542 122.454 1.00 39.80  ? 375 TRP D NE1 1 
ATOM   5656 C CE2 . TRP B 2 245 ? 147.965 157.676 121.808 1.00 38.28  ? 375 TRP D CE2 1 
ATOM   5657 C CE3 . TRP B 2 245 ? 149.823 157.794 120.266 1.00 41.36  ? 375 TRP D CE3 1 
ATOM   5658 C CZ2 . TRP B 2 245 ? 148.023 156.285 121.838 1.00 38.86  ? 375 TRP D CZ2 1 
ATOM   5659 C CZ3 . TRP B 2 245 ? 149.879 156.419 120.296 1.00 43.25  ? 375 TRP D CZ3 1 
ATOM   5660 C CH2 . TRP B 2 245 ? 148.989 155.676 121.070 1.00 41.18  ? 375 TRP D CH2 1 
ATOM   5661 N N   . GLY B 2 246 ? 151.840 162.492 120.037 1.00 43.20  ? 376 GLY D N   1 
ATOM   5662 C CA  . GLY B 2 246 ? 152.580 163.367 119.110 1.00 46.15  ? 376 GLY D CA  1 
ATOM   5663 C C   . GLY B 2 246 ? 152.121 163.072 117.696 1.00 51.37  ? 376 GLY D C   1 
ATOM   5664 O O   . GLY B 2 246 ? 151.441 162.042 117.511 1.00 48.50  ? 376 GLY D O   1 
ATOM   5665 N N   . GLN B 2 247 ? 152.478 163.914 116.723 1.00 54.99  ? 377 GLN D N   1 
ATOM   5666 C CA  . GLN B 2 247 ? 151.956 163.723 115.342 1.00 58.80  ? 377 GLN D CA  1 
ATOM   5667 C C   . GLN B 2 247 ? 152.411 162.358 114.795 1.00 58.38  ? 377 GLN D C   1 
ATOM   5668 O O   . GLN B 2 247 ? 151.620 161.726 114.063 1.00 56.90  ? 377 GLN D O   1 
ATOM   5669 C CB  . GLN B 2 247 ? 152.360 164.878 114.422 1.00 59.48  ? 377 GLN D CB  1 
ATOM   5670 C CG  . GLN B 2 247 ? 153.797 164.827 113.917 1.00 62.31  ? 377 GLN D CG  1 
ATOM   5671 C CD  . GLN B 2 247 ? 154.700 165.842 114.580 1.00 61.92  ? 377 GLN D CD  1 
ATOM   5672 O OE1 . GLN B 2 247 ? 154.302 166.552 115.510 1.00 60.66  ? 377 GLN D OE1 1 
ATOM   5673 N NE2 . GLN B 2 247 ? 155.937 165.912 114.110 1.00 62.18  ? 377 GLN D NE2 1 
ATOM   5674 N N   . GLY B 2 248 ? 153.627 161.923 115.135 1.00 56.43  ? 378 GLY D N   1 
ATOM   5675 C CA  . GLY B 2 248 ? 154.156 160.648 114.614 1.00 53.98  ? 378 GLY D CA  1 
ATOM   5676 C C   . GLY B 2 248 ? 155.335 160.880 113.692 1.00 57.24  ? 378 GLY D C   1 
ATOM   5677 O O   . GLY B 2 248 ? 155.166 161.616 112.698 1.00 63.27  ? 378 GLY D O   1 
ATOM   5678 N N   . THR B 2 249 ? 156.488 160.279 113.998 1.00 53.47  ? 379 THR D N   1 
ATOM   5679 C CA  . THR B 2 249 ? 157.692 160.482 113.194 1.00 58.31  ? 379 THR D CA  1 
ATOM   5680 C C   . THR B 2 249 ? 158.040 159.170 112.497 1.00 58.23  ? 379 THR D C   1 
ATOM   5681 O O   . THR B 2 249 ? 158.741 158.324 113.053 1.00 56.60  ? 379 THR D O   1 
ATOM   5682 C CB  . THR B 2 249 ? 158.848 160.957 114.060 1.00 58.96  ? 379 THR D CB  1 
ATOM   5683 O OG1 . THR B 2 249 ? 158.784 160.300 115.331 1.00 58.80  ? 379 THR D OG1 1 
ATOM   5684 C CG2 . THR B 2 249 ? 158.769 162.451 114.274 1.00 59.64  ? 379 THR D CG2 1 
ATOM   5685 N N   . LEU B 2 250 ? 157.549 159.008 111.271 1.00 59.62  ? 380 LEU D N   1 
ATOM   5686 C CA  . LEU B 2 250 ? 157.888 157.829 110.488 1.00 59.45  ? 380 LEU D CA  1 
ATOM   5687 C C   . LEU B 2 250 ? 159.387 157.794 110.222 1.00 61.77  ? 380 LEU D C   1 
ATOM   5688 O O   . LEU B 2 250 ? 159.978 158.791 109.799 1.00 68.66  ? 380 LEU D O   1 
ATOM   5689 C CB  . LEU B 2 250 ? 157.112 157.828 109.171 1.00 58.58  ? 380 LEU D CB  1 
ATOM   5690 C CG  . LEU B 2 250 ? 157.664 156.962 108.037 1.00 60.98  ? 380 LEU D CG  1 
ATOM   5691 C CD1 . LEU B 2 250 ? 157.577 155.487 108.390 1.00 64.27  ? 380 LEU D CD1 1 
ATOM   5692 C CD2 . LEU B 2 250 ? 156.924 157.245 106.741 1.00 61.91  ? 380 LEU D CD2 1 
ATOM   5693 N N   . VAL B 2 251 ? 160.003 156.642 110.475 1.00 59.42  ? 381 VAL D N   1 
ATOM   5694 C CA  . VAL B 2 251 ? 161.443 156.456 110.300 1.00 65.39  ? 381 VAL D CA  1 
ATOM   5695 C C   . VAL B 2 251 ? 161.617 155.229 109.409 1.00 68.30  ? 381 VAL D C   1 
ATOM   5696 O O   . VAL B 2 251 ? 161.669 154.094 109.890 1.00 68.84  ? 381 VAL D O   1 
ATOM   5697 C CB  . VAL B 2 251 ? 162.185 156.287 111.629 1.00 63.29  ? 381 VAL D CB  1 
ATOM   5698 C CG1 . VAL B 2 251 ? 163.669 156.061 111.386 1.00 65.42  ? 381 VAL D CG1 1 
ATOM   5699 C CG2 . VAL B 2 251 ? 161.965 157.500 112.519 1.00 61.21  ? 381 VAL D CG2 1 
ATOM   5700 N N   . THR B 2 252 ? 161.714 155.450 108.102 1.00 71.61  ? 382 THR D N   1 
ATOM   5701 C CA  . THR B 2 252 ? 161.885 154.366 107.143 1.00 75.87  ? 382 THR D CA  1 
ATOM   5702 C C   . THR B 2 252 ? 163.366 154.026 107.034 1.00 80.20  ? 382 THR D C   1 
ATOM   5703 O O   . THR B 2 252 ? 164.190 154.902 106.751 1.00 81.51  ? 382 THR D O   1 
ATOM   5704 C CB  . THR B 2 252 ? 161.321 154.754 105.777 1.00 78.02  ? 382 THR D CB  1 
ATOM   5705 O OG1 . THR B 2 252 ? 159.995 155.273 105.935 1.00 75.98  ? 382 THR D OG1 1 
ATOM   5706 C CG2 . THR B 2 252 ? 161.278 153.543 104.857 1.00 79.73  ? 382 THR D CG2 1 
ATOM   5707 N N   . VAL B 2 253 ? 163.701 152.758 107.256 1.00 83.77  ? 383 VAL D N   1 
ATOM   5708 C CA  . VAL B 2 253 ? 165.083 152.294 107.240 1.00 89.63  ? 383 VAL D CA  1 
ATOM   5709 C C   . VAL B 2 253 ? 165.189 151.124 106.275 1.00 92.83  ? 383 VAL D C   1 
ATOM   5710 O O   . VAL B 2 253 ? 164.455 150.137 106.405 1.00 87.73  ? 383 VAL D O   1 
ATOM   5711 C CB  . VAL B 2 253 ? 165.563 151.886 108.645 1.00 87.81  ? 383 VAL D CB  1 
ATOM   5712 C CG1 . VAL B 2 253 ? 166.818 151.037 108.552 1.00 85.39  ? 383 VAL D CG1 1 
ATOM   5713 C CG2 . VAL B 2 253 ? 165.810 153.118 109.495 1.00 82.68  ? 383 VAL D CG2 1 
ATOM   5714 N N   . SER B 2 254 ? 166.098 151.234 105.309 1.00 97.17  ? 384 SER D N   1 
ATOM   5715 C CA  . SER B 2 254 ? 166.329 150.171 104.342 1.00 99.25  ? 384 SER D CA  1 
ATOM   5716 C C   . SER B 2 254 ? 167.712 150.353 103.738 1.00 100.27 ? 384 SER D C   1 
ATOM   5717 O O   . SER B 2 254 ? 168.316 151.424 103.834 1.00 96.60  ? 384 SER D O   1 
ATOM   5718 C CB  . SER B 2 254 ? 165.257 150.161 103.247 1.00 98.71  ? 384 SER D CB  1 
ATOM   5719 O OG  . SER B 2 254 ? 165.758 149.592 102.050 1.00 96.99  ? 384 SER D OG  1 
ATOM   5720 N N   . SER B 2 255 ? 168.206 149.287 103.115 1.00 103.56 ? 385 SER D N   1 
ATOM   5721 C CA  . SER B 2 255 ? 169.506 149.321 102.456 1.00 104.28 ? 385 SER D CA  1 
ATOM   5722 C C   . SER B 2 255 ? 169.348 149.426 100.943 1.00 103.02 ? 385 SER D C   1 
ATOM   5723 O O   . SER B 2 255 ? 168.356 148.965 100.380 1.00 102.54 ? 385 SER D O   1 
ATOM   5724 C CB  . SER B 2 255 ? 170.324 148.078 102.813 1.00 101.99 ? 385 SER D CB  1 
ATOM   5725 O OG  . SER B 2 255 ? 171.000 148.249 104.047 1.00 100.57 ? 385 SER D OG  1 
HETATM 5726 C C1  . NAG C 3 .   ? 152.657 153.537 142.840 1.00 19.21  ? 1   NAG B C1  1 
HETATM 5727 C C2  . NAG C 3 .   ? 153.695 154.091 141.861 1.00 16.78  ? 1   NAG B C2  1 
HETATM 5728 C C3  . NAG C 3 .   ? 154.352 152.874 141.219 1.00 18.73  ? 1   NAG B C3  1 
HETATM 5729 C C4  . NAG C 3 .   ? 154.789 151.808 142.245 1.00 20.02  ? 1   NAG B C4  1 
HETATM 5730 C C5  . NAG C 3 .   ? 153.850 151.685 143.462 1.00 16.47  ? 1   NAG B C5  1 
HETATM 5731 C C6  . NAG C 3 .   ? 154.469 150.978 144.648 1.00 15.76  ? 1   NAG B C6  1 
HETATM 5732 C C7  . NAG C 3 .   ? 153.435 156.257 140.709 1.00 16.89  ? 1   NAG B C7  1 
HETATM 5733 C C8  . NAG C 3 .   ? 152.694 157.010 139.624 1.00 10.67  ? 1   NAG B C8  1 
HETATM 5734 N N2  . NAG C 3 .   ? 153.101 154.963 140.870 1.00 19.44  ? 1   NAG B N2  1 
HETATM 5735 O O3  . NAG C 3 .   ? 155.406 153.357 140.432 1.00 22.64  ? 1   NAG B O3  1 
HETATM 5736 O O4  . NAG C 3 .   ? 154.788 150.577 141.547 1.00 27.31  ? 1   NAG B O4  1 
HETATM 5737 O O5  . NAG C 3 .   ? 153.337 152.930 143.910 1.00 21.14  ? 1   NAG B O5  1 
HETATM 5738 O O6  . NAG C 3 .   ? 153.566 150.989 145.727 1.00 20.80  ? 1   NAG B O6  1 
HETATM 5739 O O7  . NAG C 3 .   ? 154.282 156.808 141.397 1.00 19.39  ? 1   NAG B O7  1 
HETATM 5740 C C1  . NAG C 3 .   ? 156.117 150.058 141.407 1.00 24.45  ? 2   NAG B C1  1 
HETATM 5741 C C2  . NAG C 3 .   ? 156.061 148.544 141.641 1.00 20.38  ? 2   NAG B C2  1 
HETATM 5742 C C3  . NAG C 3 .   ? 157.446 147.951 141.446 1.00 27.56  ? 2   NAG B C3  1 
HETATM 5743 C C4  . NAG C 3 .   ? 157.960 148.322 140.063 1.00 32.99  ? 2   NAG B C4  1 
HETATM 5744 C C5  . NAG C 3 .   ? 157.920 149.844 139.879 1.00 28.75  ? 2   NAG B C5  1 
HETATM 5745 C C6  . NAG C 3 .   ? 158.384 150.291 138.509 1.00 35.22  ? 2   NAG B C6  1 
HETATM 5746 C C7  . NAG C 3 .   ? 154.361 147.645 143.162 1.00 16.07  ? 2   NAG B C7  1 
HETATM 5747 C C8  . NAG C 3 .   ? 154.028 147.381 144.609 1.00 16.46  ? 2   NAG B C8  1 
HETATM 5748 N N2  . NAG C 3 .   ? 155.558 148.218 142.946 1.00 19.37  ? 2   NAG B N2  1 
HETATM 5749 O O3  . NAG C 3 .   ? 157.325 146.564 141.611 1.00 29.75  ? 2   NAG B O3  1 
HETATM 5750 O O4  . NAG C 3 .   ? 159.271 147.823 139.972 1.00 33.94  ? 2   NAG B O4  1 
HETATM 5751 O O5  . NAG C 3 .   ? 156.607 150.320 140.114 1.00 27.52  ? 2   NAG B O5  1 
HETATM 5752 O O6  . NAG C 3 .   ? 158.029 151.635 138.292 1.00 46.63  ? 2   NAG B O6  1 
HETATM 5753 O O7  . NAG C 3 .   ? 153.585 147.353 142.266 1.00 15.94  ? 2   NAG B O7  1 
HETATM 5754 C C1  . NAG D 3 .   ? 142.736 177.696 145.222 1.00 71.45  ? 1   NAG C C1  1 
HETATM 5755 C C2  . NAG D 3 .   ? 141.346 177.134 145.535 1.00 72.23  ? 1   NAG C C2  1 
HETATM 5756 C C3  . NAG D 3 .   ? 140.271 178.219 145.489 1.00 75.05  ? 1   NAG C C3  1 
HETATM 5757 C C4  . NAG D 3 .   ? 140.726 179.475 146.220 1.00 82.73  ? 1   NAG C C4  1 
HETATM 5758 C C5  . NAG D 3 .   ? 142.029 179.952 145.597 1.00 78.58  ? 1   NAG C C5  1 
HETATM 5759 C C6  . NAG D 3 .   ? 142.539 181.231 146.213 1.00 75.83  ? 1   NAG C C6  1 
HETATM 5760 C C7  . NAG D 3 .   ? 139.951 175.283 144.719 1.00 80.18  ? 1   NAG C C7  1 
HETATM 5761 C C8  . NAG D 3 .   ? 139.355 174.811 143.429 1.00 80.76  ? 1   NAG C C8  1 
HETATM 5762 N N2  . NAG D 3 .   ? 141.029 176.062 144.615 1.00 78.82  ? 1   NAG C N2  1 
HETATM 5763 O O3  . NAG D 3 .   ? 139.069 177.713 146.053 1.00 73.77  ? 1   NAG C O3  1 
HETATM 5764 O O4  . NAG D 3 .   ? 139.763 180.519 146.094 1.00 93.36  ? 1   NAG C O4  1 
HETATM 5765 O O5  . NAG D 3 .   ? 143.025 178.943 145.836 1.00 75.80  ? 1   NAG C O5  1 
HETATM 5766 O O6  . NAG D 3 .   ? 142.979 181.017 147.552 1.00 72.94  ? 1   NAG C O6  1 
HETATM 5767 O O7  . NAG D 3 .   ? 139.476 174.972 145.808 1.00 77.65  ? 1   NAG C O7  1 
HETATM 5768 C C1  . NAG D 3 .   ? 138.820 180.702 147.103 1.00 80.07  ? 2   NAG C C1  1 
HETATM 5769 C C2  . NAG D 3 .   ? 138.088 182.019 146.845 1.00 80.07  ? 2   NAG C C2  1 
HETATM 5770 C C3  . NAG D 3 .   ? 137.012 182.236 147.904 1.00 80.07  ? 2   NAG C C3  1 
HETATM 5771 C C4  . NAG D 3 .   ? 136.111 181.013 148.020 1.00 80.07  ? 2   NAG C C4  1 
HETATM 5772 C C5  . NAG D 3 .   ? 136.963 179.773 148.270 1.00 80.07  ? 2   NAG C C5  1 
HETATM 5773 C C6  . NAG D 3 .   ? 136.149 178.502 148.320 1.00 80.07  ? 2   NAG C C6  1 
HETATM 5774 C C7  . NAG D 3 .   ? 139.431 183.703 145.686 1.00 80.07  ? 2   NAG C C7  1 
HETATM 5775 C C8  . NAG D 3 .   ? 139.305 185.193 145.605 1.00 80.07  ? 2   NAG C C8  1 
HETATM 5776 N N2  . NAG D 3 .   ? 139.003 183.140 146.817 1.00 80.07  ? 2   NAG C N2  1 
HETATM 5777 O O3  . NAG D 3 .   ? 136.258 183.395 147.578 1.00 80.07  ? 2   NAG C O3  1 
HETATM 5778 O O4  . NAG D 3 .   ? 135.218 181.190 149.116 1.00 80.07  ? 2   NAG C O4  1 
HETATM 5779 O O5  . NAG D 3 .   ? 137.906 179.621 147.192 1.00 80.07  ? 2   NAG C O5  1 
HETATM 5780 O O6  . NAG D 3 .   ? 135.083 178.537 147.374 1.00 80.07  ? 2   NAG C O6  1 
HETATM 5781 O O7  . NAG D 3 .   ? 139.900 183.038 144.768 1.00 80.07  ? 2   NAG C O7  1 
HETATM 5782 C C1  . NAG E 4 .   ? 149.782 152.713 163.997 1.00 112.38 ? 701 NAG A C1  1 
HETATM 5783 C C2  . NAG E 4 .   ? 149.964 151.448 164.842 1.00 115.18 ? 701 NAG A C2  1 
HETATM 5784 C C3  . NAG E 4 .   ? 149.183 150.299 164.211 1.00 108.93 ? 701 NAG A C3  1 
HETATM 5785 C C4  . NAG E 4 .   ? 147.732 150.705 163.969 1.00 108.61 ? 701 NAG A C4  1 
HETATM 5786 C C5  . NAG E 4 .   ? 147.687 152.021 163.185 1.00 115.88 ? 701 NAG A C5  1 
HETATM 5787 C C6  . NAG E 4 .   ? 146.287 152.533 162.928 1.00 115.82 ? 701 NAG A C6  1 
HETATM 5788 C C7  . NAG E 4 .   ? 152.089 151.219 166.097 1.00 104.25 ? 701 NAG A C7  1 
HETATM 5789 C C8  . NAG E 4 .   ? 151.344 151.718 167.311 1.00 103.71 ? 701 NAG A C8  1 
HETATM 5790 N N2  . NAG E 4 .   ? 151.361 151.120 164.967 1.00 109.90 ? 701 NAG A N2  1 
HETATM 5791 O O3  . NAG E 4 .   ? 149.281 149.188 165.063 1.00 106.24 ? 701 NAG A O3  1 
HETATM 5792 O O4  . NAG E 4 .   ? 147.120 149.656 163.256 1.00 101.20 ? 701 NAG A O4  1 
HETATM 5793 O O5  . NAG E 4 .   ? 148.409 153.008 163.894 1.00 116.57 ? 701 NAG A O5  1 
HETATM 5794 O O6  . NAG E 4 .   ? 145.603 151.642 162.079 1.00 107.86 ? 701 NAG A O6  1 
HETATM 5795 O O7  . NAG E 4 .   ? 153.275 150.930 166.156 1.00 98.65  ? 701 NAG A O7  1 
HETATM 5796 C C1  . NAG F 4 .   ? 152.880 190.249 177.270 1.00 70.15  ? 702 NAG A C1  1 
HETATM 5797 C C2  . NAG F 4 .   ? 153.981 191.162 176.709 1.00 69.42  ? 702 NAG A C2  1 
HETATM 5798 C C3  . NAG F 4 .   ? 153.772 192.593 177.200 1.00 71.11  ? 702 NAG A C3  1 
HETATM 5799 C C4  . NAG F 4 .   ? 152.346 193.057 176.929 1.00 76.89  ? 702 NAG A C4  1 
HETATM 5800 C C5  . NAG F 4 .   ? 151.370 192.047 177.538 1.00 77.61  ? 702 NAG A C5  1 
HETATM 5801 C C6  . NAG F 4 .   ? 149.913 192.401 177.338 1.00 80.72  ? 702 NAG A C6  1 
HETATM 5802 C C7  . NAG F 4 .   ? 156.345 190.551 176.281 1.00 67.07  ? 702 NAG A C7  1 
HETATM 5803 C C8  . NAG F 4 .   ? 156.116 190.935 174.840 1.00 62.30  ? 702 NAG A C8  1 
HETATM 5804 N N2  . NAG F 4 .   ? 155.283 190.690 177.100 1.00 67.39  ? 702 NAG A N2  1 
HETATM 5805 O O3  . NAG F 4 .   ? 154.718 193.411 176.564 1.00 74.44  ? 702 NAG A O3  1 
HETATM 5806 O O4  . NAG F 4 .   ? 152.204 194.334 177.506 1.00 89.66  ? 702 NAG A O4  1 
HETATM 5807 O O5  . NAG F 4 .   ? 151.613 190.782 176.959 1.00 72.93  ? 702 NAG A O5  1 
HETATM 5808 O O6  . NAG F 4 .   ? 149.638 192.523 175.963 1.00 87.56  ? 702 NAG A O6  1 
HETATM 5809 O O7  . NAG F 4 .   ? 157.433 190.145 176.662 1.00 68.39  ? 702 NAG A O7  1 
# 
