data_9DPL
# 
_entry.id   9DPL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DPL         pdb_00009dpl 10.2210/pdb9dpl/pdb 
WWPDB D_1000287983 ?            ?                   
EMDB  EMD-47106    ?            ?                   
# 
_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       2025-03-12 
_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                        9DPL 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2' 
_pdbx_database_related.db_id          EMD-47106 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yong.xiong@yale.edu 
_pdbx_contact_author.name_first         Yong 
_pdbx_contact_author.name_last          Xiong 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9625-9313 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Devarkar, S.C.' 1 0000-0002-9271-243X 
'Xiong, Y.'      2 0000-0001-9625-9313 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            53 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkaf114 
_citation.pdbx_database_id_PubMed   40036503 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Devarkar, S.C.'     1 0000-0002-9271-243X 
primary 'Budding, C.R.'      2 ?                   
primary 'Pathirage, C.'      3 ?                   
primary 'Kavoor, A.'         4 ?                   
primary 'Herbert, C.'        5 ?                   
primary 'Limbach, P.A.'      6 ?                   
primary 'Musier-Forsyth, K.' 7 ?                   
primary 'Xiong, Y.'          8 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Lysine--tRNA ligase'                                                   68143.953 2 2.7.7.-,6.1.1.6 ? 
'Human KRS' ? 
2 polymer     nat 'tRNA-Lys3 (Cellular modified)'                                         24833.062 1 ?               ? ? ? 
3 polymer     syn 'Aminoacyl tRNA synthase complex-interacting multifunctional protein 2' 4082.798  2 ?               ? ? ? 
4 non-polymer syn LYSINE                                                                  147.195   2 ?               ? ? ? 
5 non-polymer syn 'ADENOSINE MONOPHOSPHATE'                                               347.221   2 ?               ? ? ? 
6 non-polymer syn 'SODIUM ION'                                                            22.990    2 ?               ? ? ? 
7 non-polymer syn 'MAGNESIUM ION'                                                         24.305    2 ?               ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Lysyl-tRNA synthetase,LysRS'                                 
3 'Multisynthase complex auxiliary component p38,Protein JTV-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  
;MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIR
SQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANS
RNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGR
QFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEEL
EKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD
SNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
;
;MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIR
SQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANS
RNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGR
QFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEEL
EKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD
SNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
;
A,B ? 
2 polyribonucleotide no yes 
;GCCCGGAUA(2MG)CUCAG(H2U)CGG(H2U)AGAGCA(PSU)CAGACU(70U)UU(12A)A(PSU)CUGAGG(7MG)
(H2U)(5MC)(5MC)AGGG(2MU)(PSU)CA(1MA)GUCCCUGUUCGGGCGCCA
;
GCCCGGAUAGCUCAGUCGGUAGAGCAUCAGACUUUUAAUCUGAGGGUCCAGGGUUCAAGUCCCUGUUCGGGCGCCA C   ? 
3 'polypeptide(L)'   no no  MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYG MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYG D,E ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 LYSINE                    LYS 
5 'ADENOSINE MONOPHOSPHATE' AMP 
6 'SODIUM ION'              NA  
7 'MAGNESIUM ION'           MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ALA n 
1 4   VAL n 
1 5   GLN n 
1 6   ALA n 
1 7   ALA n 
1 8   GLU n 
1 9   VAL n 
1 10  LYS n 
1 11  VAL n 
1 12  ASP n 
1 13  GLY n 
1 14  SER n 
1 15  GLU n 
1 16  PRO n 
1 17  LYS n 
1 18  LEU n 
1 19  SER n 
1 20  LYS n 
1 21  ASN n 
1 22  GLU n 
1 23  LEU n 
1 24  LYS n 
1 25  ARG n 
1 26  ARG n 
1 27  LEU n 
1 28  LYS n 
1 29  ALA n 
1 30  GLU n 
1 31  LYS n 
1 32  LYS n 
1 33  VAL n 
1 34  ALA n 
1 35  GLU n 
1 36  LYS n 
1 37  GLU n 
1 38  ALA n 
1 39  LYS n 
1 40  GLN n 
1 41  LYS n 
1 42  GLU n 
1 43  LEU n 
1 44  SER n 
1 45  GLU n 
1 46  LYS n 
1 47  GLN n 
1 48  LEU n 
1 49  SER n 
1 50  GLN n 
1 51  ALA n 
1 52  THR n 
1 53  ALA n 
1 54  ALA n 
1 55  ALA n 
1 56  THR n 
1 57  ASN n 
1 58  HIS n 
1 59  THR n 
1 60  THR n 
1 61  ASP n 
1 62  ASN n 
1 63  GLY n 
1 64  VAL n 
1 65  GLY n 
1 66  PRO n 
1 67  GLU n 
1 68  GLU n 
1 69  GLU n 
1 70  SER n 
1 71  VAL n 
1 72  ASP n 
1 73  PRO n 
1 74  ASN n 
1 75  GLN n 
1 76  TYR n 
1 77  TYR n 
1 78  LYS n 
1 79  ILE n 
1 80  ARG n 
1 81  SER n 
1 82  GLN n 
1 83  ALA n 
1 84  ILE n 
1 85  HIS n 
1 86  GLN n 
1 87  LEU n 
1 88  LYS n 
1 89  VAL n 
1 90  ASN n 
1 91  GLY n 
1 92  GLU n 
1 93  ASP n 
1 94  PRO n 
1 95  TYR n 
1 96  PRO n 
1 97  HIS n 
1 98  LYS n 
1 99  PHE n 
1 100 HIS n 
1 101 VAL n 
1 102 ASP n 
1 103 ILE n 
1 104 SER n 
1 105 LEU n 
1 106 THR n 
1 107 ASP n 
1 108 PHE n 
1 109 ILE n 
1 110 GLN n 
1 111 LYS n 
1 112 TYR n 
1 113 SER n 
1 114 HIS n 
1 115 LEU n 
1 116 GLN n 
1 117 PRO n 
1 118 GLY n 
1 119 ASP n 
1 120 HIS n 
1 121 LEU n 
1 122 THR n 
1 123 ASP n 
1 124 ILE n 
1 125 THR n 
1 126 LEU n 
1 127 LYS n 
1 128 VAL n 
1 129 ALA n 
1 130 GLY n 
1 131 ARG n 
1 132 ILE n 
1 133 HIS n 
1 134 ALA n 
1 135 LYS n 
1 136 ARG n 
1 137 ALA n 
1 138 SER n 
1 139 GLY n 
1 140 GLY n 
1 141 LYS n 
1 142 LEU n 
1 143 ILE n 
1 144 PHE n 
1 145 TYR n 
1 146 ASP n 
1 147 LEU n 
1 148 ARG n 
1 149 GLY n 
1 150 GLU n 
1 151 GLY n 
1 152 VAL n 
1 153 LYS n 
1 154 LEU n 
1 155 GLN n 
1 156 VAL n 
1 157 MET n 
1 158 ALA n 
1 159 ASN n 
1 160 SER n 
1 161 ARG n 
1 162 ASN n 
1 163 TYR n 
1 164 LYS n 
1 165 SER n 
1 166 GLU n 
1 167 GLU n 
1 168 GLU n 
1 169 PHE n 
1 170 ILE n 
1 171 HIS n 
1 172 ILE n 
1 173 ASN n 
1 174 ASN n 
1 175 LYS n 
1 176 LEU n 
1 177 ARG n 
1 178 ARG n 
1 179 GLY n 
1 180 ASP n 
1 181 ILE n 
1 182 ILE n 
1 183 GLY n 
1 184 VAL n 
1 185 GLN n 
1 186 GLY n 
1 187 ASN n 
1 188 PRO n 
1 189 GLY n 
1 190 LYS n 
1 191 THR n 
1 192 LYS n 
1 193 LYS n 
1 194 GLY n 
1 195 GLU n 
1 196 LEU n 
1 197 SER n 
1 198 ILE n 
1 199 ILE n 
1 200 PRO n 
1 201 TYR n 
1 202 GLU n 
1 203 ILE n 
1 204 THR n 
1 205 LEU n 
1 206 LEU n 
1 207 SER n 
1 208 PRO n 
1 209 CYS n 
1 210 LEU n 
1 211 HIS n 
1 212 MET n 
1 213 LEU n 
1 214 PRO n 
1 215 HIS n 
1 216 LEU n 
1 217 HIS n 
1 218 PHE n 
1 219 GLY n 
1 220 LEU n 
1 221 LYS n 
1 222 ASP n 
1 223 LYS n 
1 224 GLU n 
1 225 THR n 
1 226 ARG n 
1 227 TYR n 
1 228 ARG n 
1 229 GLN n 
1 230 ARG n 
1 231 TYR n 
1 232 LEU n 
1 233 ASP n 
1 234 LEU n 
1 235 ILE n 
1 236 LEU n 
1 237 ASN n 
1 238 ASP n 
1 239 PHE n 
1 240 VAL n 
1 241 ARG n 
1 242 GLN n 
1 243 LYS n 
1 244 PHE n 
1 245 ILE n 
1 246 ILE n 
1 247 ARG n 
1 248 SER n 
1 249 LYS n 
1 250 ILE n 
1 251 ILE n 
1 252 THR n 
1 253 TYR n 
1 254 ILE n 
1 255 ARG n 
1 256 SER n 
1 257 PHE n 
1 258 LEU n 
1 259 ASP n 
1 260 GLU n 
1 261 LEU n 
1 262 GLY n 
1 263 PHE n 
1 264 LEU n 
1 265 GLU n 
1 266 ILE n 
1 267 GLU n 
1 268 THR n 
1 269 PRO n 
1 270 MET n 
1 271 MET n 
1 272 ASN n 
1 273 ILE n 
1 274 ILE n 
1 275 PRO n 
1 276 GLY n 
1 277 GLY n 
1 278 ALA n 
1 279 VAL n 
1 280 ALA n 
1 281 LYS n 
1 282 PRO n 
1 283 PHE n 
1 284 ILE n 
1 285 THR n 
1 286 TYR n 
1 287 HIS n 
1 288 ASN n 
1 289 GLU n 
1 290 LEU n 
1 291 ASP n 
1 292 MET n 
1 293 ASN n 
1 294 LEU n 
1 295 TYR n 
1 296 MET n 
1 297 ARG n 
1 298 ILE n 
1 299 ALA n 
1 300 PRO n 
1 301 GLU n 
1 302 LEU n 
1 303 TYR n 
1 304 HIS n 
1 305 LYS n 
1 306 MET n 
1 307 LEU n 
1 308 VAL n 
1 309 VAL n 
1 310 GLY n 
1 311 GLY n 
1 312 ILE n 
1 313 ASP n 
1 314 ARG n 
1 315 VAL n 
1 316 TYR n 
1 317 GLU n 
1 318 ILE n 
1 319 GLY n 
1 320 ARG n 
1 321 GLN n 
1 322 PHE n 
1 323 ARG n 
1 324 ASN n 
1 325 GLU n 
1 326 GLY n 
1 327 ILE n 
1 328 ASP n 
1 329 LEU n 
1 330 THR n 
1 331 HIS n 
1 332 ASN n 
1 333 PRO n 
1 334 GLU n 
1 335 PHE n 
1 336 THR n 
1 337 THR n 
1 338 CYS n 
1 339 GLU n 
1 340 PHE n 
1 341 TYR n 
1 342 MET n 
1 343 ALA n 
1 344 TYR n 
1 345 ALA n 
1 346 ASP n 
1 347 TYR n 
1 348 HIS n 
1 349 ASP n 
1 350 LEU n 
1 351 MET n 
1 352 GLU n 
1 353 ILE n 
1 354 THR n 
1 355 GLU n 
1 356 LYS n 
1 357 MET n 
1 358 VAL n 
1 359 SER n 
1 360 GLY n 
1 361 MET n 
1 362 VAL n 
1 363 LYS n 
1 364 HIS n 
1 365 ILE n 
1 366 THR n 
1 367 GLY n 
1 368 SER n 
1 369 TYR n 
1 370 LYS n 
1 371 VAL n 
1 372 THR n 
1 373 TYR n 
1 374 HIS n 
1 375 PRO n 
1 376 ASP n 
1 377 GLY n 
1 378 PRO n 
1 379 GLU n 
1 380 GLY n 
1 381 GLN n 
1 382 ALA n 
1 383 TYR n 
1 384 ASP n 
1 385 VAL n 
1 386 ASP n 
1 387 PHE n 
1 388 THR n 
1 389 PRO n 
1 390 PRO n 
1 391 PHE n 
1 392 ARG n 
1 393 ARG n 
1 394 ILE n 
1 395 ASN n 
1 396 MET n 
1 397 VAL n 
1 398 GLU n 
1 399 GLU n 
1 400 LEU n 
1 401 GLU n 
1 402 LYS n 
1 403 ALA n 
1 404 LEU n 
1 405 GLY n 
1 406 MET n 
1 407 LYS n 
1 408 LEU n 
1 409 PRO n 
1 410 GLU n 
1 411 THR n 
1 412 ASN n 
1 413 LEU n 
1 414 PHE n 
1 415 GLU n 
1 416 THR n 
1 417 GLU n 
1 418 GLU n 
1 419 THR n 
1 420 ARG n 
1 421 LYS n 
1 422 ILE n 
1 423 LEU n 
1 424 ASP n 
1 425 ASP n 
1 426 ILE n 
1 427 CYS n 
1 428 VAL n 
1 429 ALA n 
1 430 LYS n 
1 431 ALA n 
1 432 VAL n 
1 433 GLU n 
1 434 CYS n 
1 435 PRO n 
1 436 PRO n 
1 437 PRO n 
1 438 ARG n 
1 439 THR n 
1 440 THR n 
1 441 ALA n 
1 442 ARG n 
1 443 LEU n 
1 444 LEU n 
1 445 ASP n 
1 446 LYS n 
1 447 LEU n 
1 448 VAL n 
1 449 GLY n 
1 450 GLU n 
1 451 PHE n 
1 452 LEU n 
1 453 GLU n 
1 454 VAL n 
1 455 THR n 
1 456 CYS n 
1 457 ILE n 
1 458 ASN n 
1 459 PRO n 
1 460 THR n 
1 461 PHE n 
1 462 ILE n 
1 463 CYS n 
1 464 ASP n 
1 465 HIS n 
1 466 PRO n 
1 467 GLN n 
1 468 ILE n 
1 469 MET n 
1 470 SER n 
1 471 PRO n 
1 472 LEU n 
1 473 ALA n 
1 474 LYS n 
1 475 TRP n 
1 476 HIS n 
1 477 ARG n 
1 478 SER n 
1 479 LYS n 
1 480 GLU n 
1 481 GLY n 
1 482 LEU n 
1 483 THR n 
1 484 GLU n 
1 485 ARG n 
1 486 PHE n 
1 487 GLU n 
1 488 LEU n 
1 489 PHE n 
1 490 VAL n 
1 491 MET n 
1 492 LYS n 
1 493 LYS n 
1 494 GLU n 
1 495 ILE n 
1 496 CYS n 
1 497 ASN n 
1 498 ALA n 
1 499 TYR n 
1 500 THR n 
1 501 GLU n 
1 502 LEU n 
1 503 ASN n 
1 504 ASP n 
1 505 PRO n 
1 506 MET n 
1 507 ARG n 
1 508 GLN n 
1 509 ARG n 
1 510 GLN n 
1 511 LEU n 
1 512 PHE n 
1 513 GLU n 
1 514 GLU n 
1 515 GLN n 
1 516 ALA n 
1 517 LYS n 
1 518 ALA n 
1 519 LYS n 
1 520 ALA n 
1 521 ALA n 
1 522 GLY n 
1 523 ASP n 
1 524 ASP n 
1 525 GLU n 
1 526 ALA n 
1 527 MET n 
1 528 PHE n 
1 529 ILE n 
1 530 ASP n 
1 531 GLU n 
1 532 ASN n 
1 533 PHE n 
1 534 CYS n 
1 535 THR n 
1 536 ALA n 
1 537 LEU n 
1 538 GLU n 
1 539 TYR n 
1 540 GLY n 
1 541 LEU n 
1 542 PRO n 
1 543 PRO n 
1 544 THR n 
1 545 ALA n 
1 546 GLY n 
1 547 TRP n 
1 548 GLY n 
1 549 MET n 
1 550 GLY n 
1 551 ILE n 
1 552 ASP n 
1 553 ARG n 
1 554 VAL n 
1 555 ALA n 
1 556 MET n 
1 557 PHE n 
1 558 LEU n 
1 559 THR n 
1 560 ASP n 
1 561 SER n 
1 562 ASN n 
1 563 ASN n 
1 564 ILE n 
1 565 LYS n 
1 566 GLU n 
1 567 VAL n 
1 568 LEU n 
1 569 LEU n 
1 570 PHE n 
1 571 PRO n 
1 572 ALA n 
1 573 MET n 
1 574 LYS n 
1 575 PRO n 
1 576 GLU n 
1 577 ASP n 
1 578 LYS n 
1 579 LYS n 
1 580 GLU n 
1 581 ASN n 
1 582 VAL n 
1 583 ALA n 
1 584 THR n 
1 585 THR n 
1 586 ASP n 
1 587 THR n 
1 588 LEU n 
1 589 GLU n 
1 590 SER n 
1 591 THR n 
1 592 THR n 
1 593 VAL n 
1 594 GLY n 
1 595 THR n 
1 596 SER n 
1 597 VAL n 
2 1   G   n 
2 2   C   n 
2 3   C   n 
2 4   C   n 
2 5   G   n 
2 6   G   n 
2 7   A   n 
2 8   U   n 
2 9   A   n 
2 10  2MG n 
2 11  C   n 
2 12  U   n 
2 13  C   n 
2 14  A   n 
2 15  G   n 
2 16  H2U n 
2 17  C   n 
2 18  G   n 
2 19  G   n 
2 20  H2U n 
2 21  A   n 
2 22  G   n 
2 23  A   n 
2 24  G   n 
2 25  C   n 
2 26  A   n 
2 27  PSU n 
2 28  C   n 
2 29  A   n 
2 30  G   n 
2 31  A   n 
2 32  C   n 
2 33  U   n 
2 34  70U n 
2 35  U   n 
2 36  U   n 
2 37  12A n 
2 38  A   n 
2 39  PSU n 
2 40  C   n 
2 41  U   n 
2 42  G   n 
2 43  A   n 
2 44  G   n 
2 45  G   n 
2 46  7MG n 
2 47  H2U n 
2 48  5MC n 
2 49  5MC n 
2 50  A   n 
2 51  G   n 
2 52  G   n 
2 53  G   n 
2 54  2MU n 
2 55  PSU n 
2 56  C   n 
2 57  A   n 
2 58  1MA n 
2 59  G   n 
2 60  U   n 
2 61  C   n 
2 62  C   n 
2 63  C   n 
2 64  U   n 
2 65  G   n 
2 66  U   n 
2 67  U   n 
2 68  C   n 
2 69  G   n 
2 70  G   n 
2 71  G   n 
2 72  C   n 
2 73  G   n 
2 74  C   n 
2 75  C   n 
2 76  A   n 
3 1   MET n 
3 2   PRO n 
3 3   MET n 
3 4   TYR n 
3 5   GLN n 
3 6   VAL n 
3 7   LYS n 
3 8   PRO n 
3 9   TYR n 
3 10  HIS n 
3 11  GLY n 
3 12  GLY n 
3 13  GLY n 
3 14  ALA n 
3 15  PRO n 
3 16  LEU n 
3 17  ARG n 
3 18  VAL n 
3 19  GLU n 
3 20  LEU n 
3 21  PRO n 
3 22  THR n 
3 23  CYS n 
3 24  MET n 
3 25  TYR n 
3 26  ARG n 
3 27  LEU n 
3 28  PRO n 
3 29  ASN n 
3 30  VAL n 
3 31  HIS n 
3 32  GLY n 
3 33  ARG n 
3 34  SER n 
3 35  TYR n 
3 36  GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   597 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KARS, KIAA0070' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_entity_src_nat.entity_id                  2 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           76 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Homo sapiens' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9606 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       36 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.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 
12A 'RNA linking'       n "2-METHYLTHIO-N6-(AMINOCARBONYL-L-THREONYL)-ADENOSINE-5'-MONOPHOSPHATE" ? 'C16 H23 N6 O11 P S' 538.426 
1MA 'RNA linking'       n "6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE"                            ? 'C11 H16 N5 O7 P'    361.248 
2MG 'RNA linking'       n "2N-METHYLGUANOSINE-5'-MONOPHOSPHATE"                                   ? 'C11 H16 N5 O8 P'    377.247 
2MU 'RNA linking'       n "2',5-DIMETHYLURIDINE-5'-MONOPHOSPHATE"                                 ? 'C11 H17 N2 O9 P'    352.234 
5MC 'RNA linking'       n "5-METHYLCYTIDINE-5'-MONOPHOSPHATE"                                     ? 'C10 H16 N3 O8 P'    337.223 
70U 'RNA linking'       n "5-(O-METHYLACETO)-2-THIO-2-DEOXY-URIDINE-5'-MONOPHOSPHATE"             ? 'C12 H17 N2 O10 P S' 412.310 
7MG 'RNA linking'       n "7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE"                           ? 'C11 H18 N5 O8 P'    379.263 
A   'RNA linking'       y "ADENOSINE-5'-MONOPHOSPHATE"                                            ? 'C10 H14 N5 O7 P'    347.221 
ALA 'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'         89.093  
AMP non-polymer         . 'ADENOSINE MONOPHOSPHATE'                                               ? 'C10 H14 N5 O7 P'    347.221 
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 
C   'RNA linking'       y "CYTIDINE-5'-MONOPHOSPHATE"                                             ? 'C9 H14 N3 O8 P'     323.197 
CYS 'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'       121.158 
G   'RNA linking'       y "GUANOSINE-5'-MONOPHOSPHATE"                                            ? 'C10 H14 N5 O8 P'    363.221 
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  
H2U 'RNA linking'       n "5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE"                                   ? 'C9 H15 N2 O9 P'     326.197 
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 
MG  non-polymer         . 'MAGNESIUM ION'                                                         ? 'Mg 2'               24.305  
NA  non-polymer         . 'SODIUM ION'                                                            ? 'Na 1'               22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'         115.130 
PSU 'RNA linking'       n "PSEUDOURIDINE-5'-MONOPHOSPHATE"                                        ? 'C9 H13 N2 O9 P'     324.181 
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 
U   'RNA linking'       y "URIDINE-5'-MONOPHOSPHATE"                                              ? 'C9 H13 N2 O9 P'     324.181 
VAL 'L-peptide linking' y VALINE                                                                  ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   VAL 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   VAL 9   9   ?   ?   ?   A . n 
A 1 10  LYS 10  10  ?   ?   ?   A . n 
A 1 11  VAL 11  11  ?   ?   ?   A . n 
A 1 12  ASP 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  SER 44  44  ?   ?   ?   A . n 
A 1 45  GLU 45  45  ?   ?   ?   A . n 
A 1 46  LYS 46  46  ?   ?   ?   A . n 
A 1 47  GLN 47  47  ?   ?   ?   A . n 
A 1 48  LEU 48  48  ?   ?   ?   A . n 
A 1 49  SER 49  49  ?   ?   ?   A . n 
A 1 50  GLN 50  50  ?   ?   ?   A . n 
A 1 51  ALA 51  51  ?   ?   ?   A . n 
A 1 52  THR 52  52  ?   ?   ?   A . n 
A 1 53  ALA 53  53  ?   ?   ?   A . n 
A 1 54  ALA 54  54  ?   ?   ?   A . n 
A 1 55  ALA 55  55  ?   ?   ?   A . n 
A 1 56  THR 56  56  ?   ?   ?   A . n 
A 1 57  ASN 57  57  ?   ?   ?   A . n 
A 1 58  HIS 58  58  ?   ?   ?   A . n 
A 1 59  THR 59  59  ?   ?   ?   A . n 
A 1 60  THR 60  60  ?   ?   ?   A . n 
A 1 61  ASP 61  61  ?   ?   ?   A . n 
A 1 62  ASN 62  62  ?   ?   ?   A . n 
A 1 63  GLY 63  63  ?   ?   ?   A . n 
A 1 64  VAL 64  64  ?   ?   ?   A . n 
A 1 65  GLY 65  65  ?   ?   ?   A . n 
A 1 66  PRO 66  66  ?   ?   ?   A . n 
A 1 67  GLU 67  67  ?   ?   ?   A . n 
A 1 68  GLU 68  68  ?   ?   ?   A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  HIS 85  85  85  HIS HIS A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  HIS 97  97  97  HIS HIS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 TYR 112 112 112 TYR TYR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 HIS 211 211 211 HIS HIS A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 HIS 215 215 215 HIS HIS A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 TYR 231 231 231 TYR TYR A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 THR 252 252 252 THR THR A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 PHE 257 257 257 PHE PHE A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 MET 270 270 270 MET MET A . n 
A 1 271 MET 271 271 271 MET MET A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 TYR 286 286 286 TYR TYR A . n 
A 1 287 HIS 287 287 287 HIS HIS A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 MET 292 292 292 MET MET A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 TYR 303 303 303 TYR TYR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ASP 313 313 313 ASP ASP A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 GLU 317 317 317 GLU GLU 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 ARG 320 320 320 ARG ARG A . n 
A 1 321 GLN 321 321 321 GLN GLN A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 PRO 333 333 333 PRO PRO A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 CYS 338 338 338 CYS CYS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 MET 342 342 342 MET MET A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 TYR 344 344 344 TYR TYR A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 TYR 347 347 347 TYR TYR A . n 
A 1 348 HIS 348 348 348 HIS HIS A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 MET 351 351 351 MET MET A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 ILE 353 353 353 ILE ILE A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 GLU 355 355 355 GLU GLU A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 MET 357 357 357 MET MET A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 MET 361 361 361 MET MET A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 LYS 363 363 363 LYS LYS A . n 
A 1 364 HIS 364 364 364 HIS HIS A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 HIS 374 374 374 HIS HIS A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 GLN 381 381 381 GLN GLN A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 ASP 384 384 384 ASP ASP A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 ASP 386 386 386 ASP ASP A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 THR 388 388 388 THR THR A . n 
A 1 389 PRO 389 389 389 PRO PRO A . n 
A 1 390 PRO 390 390 390 PRO PRO A . n 
A 1 391 PHE 391 391 391 PHE PHE A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 MET 396 396 396 MET MET A . n 
A 1 397 VAL 397 397 397 VAL VAL A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 LYS 402 402 402 LYS LYS A . n 
A 1 403 ALA 403 403 403 ALA ALA A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 GLY 405 405 405 GLY GLY A . n 
A 1 406 MET 406 406 406 MET MET A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 GLU 410 410 410 GLU GLU A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 PHE 414 414 414 PHE PHE A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 THR 416 416 416 THR THR A . n 
A 1 417 GLU 417 417 417 GLU GLU A . n 
A 1 418 GLU 418 418 418 GLU GLU A . n 
A 1 419 THR 419 419 419 THR THR A . n 
A 1 420 ARG 420 420 420 ARG ARG A . n 
A 1 421 LYS 421 421 421 LYS LYS A . n 
A 1 422 ILE 422 422 422 ILE ILE A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 CYS 427 427 427 CYS CYS A . n 
A 1 428 VAL 428 428 428 VAL VAL A . n 
A 1 429 ALA 429 429 429 ALA ALA A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 ALA 431 431 431 ALA ALA A . n 
A 1 432 VAL 432 432 432 VAL VAL A . n 
A 1 433 GLU 433 433 433 GLU GLU A . n 
A 1 434 CYS 434 434 434 CYS CYS A . n 
A 1 435 PRO 435 435 435 PRO PRO A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 PRO 437 437 437 PRO PRO A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 THR 439 439 439 THR THR A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 ALA 441 441 441 ALA ALA A . n 
A 1 442 ARG 442 442 442 ARG ARG A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 ASP 445 445 445 ASP ASP A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 PHE 451 451 451 PHE PHE A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 GLU 453 453 453 GLU GLU A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 THR 455 455 455 THR THR A . n 
A 1 456 CYS 456 456 456 CYS CYS A . n 
A 1 457 ILE 457 457 457 ILE ILE A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 THR 460 460 460 THR THR A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 ILE 462 462 462 ILE ILE A . n 
A 1 463 CYS 463 463 463 CYS CYS A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 HIS 465 465 465 HIS HIS A . n 
A 1 466 PRO 466 466 466 PRO PRO A . n 
A 1 467 GLN 467 467 467 GLN GLN A . n 
A 1 468 ILE 468 468 468 ILE ILE A . n 
A 1 469 MET 469 469 469 MET MET A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PRO 471 471 471 PRO PRO A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 LYS 474 474 474 LYS LYS A . n 
A 1 475 TRP 475 475 475 TRP TRP A . n 
A 1 476 HIS 476 476 476 HIS HIS A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 SER 478 478 478 SER SER A . n 
A 1 479 LYS 479 479 479 LYS LYS A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 GLY 481 481 481 GLY GLY A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 THR 483 483 483 THR THR A . n 
A 1 484 GLU 484 484 484 GLU GLU A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 PHE 486 486 486 PHE PHE A . n 
A 1 487 GLU 487 487 487 GLU GLU A . n 
A 1 488 LEU 488 488 488 LEU LEU A . n 
A 1 489 PHE 489 489 489 PHE PHE A . n 
A 1 490 VAL 490 490 490 VAL VAL A . n 
A 1 491 MET 491 491 491 MET MET A . n 
A 1 492 LYS 492 492 492 LYS LYS A . n 
A 1 493 LYS 493 493 493 LYS LYS A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 ILE 495 495 495 ILE ILE A . n 
A 1 496 CYS 496 496 496 CYS CYS A . n 
A 1 497 ASN 497 497 497 ASN ASN A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 TYR 499 499 499 TYR TYR A . n 
A 1 500 THR 500 500 500 THR THR A . n 
A 1 501 GLU 501 501 501 GLU GLU A . n 
A 1 502 LEU 502 502 502 LEU LEU A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 ASP 504 504 504 ASP ASP A . n 
A 1 505 PRO 505 505 505 PRO PRO A . n 
A 1 506 MET 506 506 506 MET MET A . n 
A 1 507 ARG 507 507 507 ARG ARG A . n 
A 1 508 GLN 508 508 508 GLN GLN A . n 
A 1 509 ARG 509 509 509 ARG ARG A . n 
A 1 510 GLN 510 510 510 GLN GLN A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 GLU 513 513 513 GLU GLU A . n 
A 1 514 GLU 514 514 514 GLU GLU A . n 
A 1 515 GLN 515 515 515 GLN GLN A . n 
A 1 516 ALA 516 516 516 ALA ALA A . n 
A 1 517 LYS 517 517 517 LYS LYS A . n 
A 1 518 ALA 518 518 518 ALA ALA A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ALA 520 520 520 ALA ALA A . n 
A 1 521 ALA 521 521 521 ALA ALA A . n 
A 1 522 GLY 522 522 522 GLY GLY A . n 
A 1 523 ASP 523 523 523 ASP ASP A . n 
A 1 524 ASP 524 524 524 ASP ASP A . n 
A 1 525 GLU 525 525 525 GLU GLU A . n 
A 1 526 ALA 526 526 526 ALA ALA A . n 
A 1 527 MET 527 527 527 MET MET A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 ILE 529 529 529 ILE ILE A . n 
A 1 530 ASP 530 530 530 ASP ASP A . n 
A 1 531 GLU 531 531 531 GLU GLU A . n 
A 1 532 ASN 532 532 532 ASN ASN A . n 
A 1 533 PHE 533 533 533 PHE PHE A . n 
A 1 534 CYS 534 534 534 CYS CYS A . n 
A 1 535 THR 535 535 535 THR THR A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 TYR 539 539 539 TYR TYR A . n 
A 1 540 GLY 540 540 540 GLY GLY A . n 
A 1 541 LEU 541 541 541 LEU LEU A . n 
A 1 542 PRO 542 542 542 PRO PRO A . n 
A 1 543 PRO 543 543 543 PRO PRO A . n 
A 1 544 THR 544 544 544 THR THR A . n 
A 1 545 ALA 545 545 545 ALA ALA A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 TRP 547 547 547 TRP TRP A . n 
A 1 548 GLY 548 548 548 GLY GLY A . n 
A 1 549 MET 549 549 549 MET MET A . n 
A 1 550 GLY 550 550 550 GLY GLY A . n 
A 1 551 ILE 551 551 551 ILE ILE A . n 
A 1 552 ASP 552 552 552 ASP ASP A . n 
A 1 553 ARG 553 553 553 ARG ARG A . n 
A 1 554 VAL 554 554 554 VAL VAL A . n 
A 1 555 ALA 555 555 555 ALA ALA A . n 
A 1 556 MET 556 556 556 MET MET A . n 
A 1 557 PHE 557 557 557 PHE PHE A . n 
A 1 558 LEU 558 558 558 LEU LEU A . n 
A 1 559 THR 559 559 559 THR THR A . n 
A 1 560 ASP 560 560 560 ASP ASP A . n 
A 1 561 SER 561 561 561 SER SER A . n 
A 1 562 ASN 562 562 562 ASN ASN A . n 
A 1 563 ASN 563 563 563 ASN ASN A . n 
A 1 564 ILE 564 564 564 ILE ILE A . n 
A 1 565 LYS 565 565 565 LYS LYS A . n 
A 1 566 GLU 566 566 566 GLU GLU A . n 
A 1 567 VAL 567 567 567 VAL VAL A . n 
A 1 568 LEU 568 568 568 LEU LEU A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 PHE 570 570 570 PHE PHE A . n 
A 1 571 PRO 571 571 571 PRO PRO A . n 
A 1 572 ALA 572 572 572 ALA ALA A . n 
A 1 573 MET 573 573 573 MET MET A . n 
A 1 574 LYS 574 574 574 LYS LYS A . n 
A 1 575 PRO 575 575 575 PRO PRO A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 ASP 577 577 577 ASP ASP A . n 
A 1 578 LYS 578 578 578 LYS LYS A . n 
A 1 579 LYS 579 579 579 LYS LYS A . n 
A 1 580 GLU 580 580 ?   ?   ?   A . n 
A 1 581 ASN 581 581 ?   ?   ?   A . n 
A 1 582 VAL 582 582 ?   ?   ?   A . n 
A 1 583 ALA 583 583 ?   ?   ?   A . n 
A 1 584 THR 584 584 ?   ?   ?   A . n 
A 1 585 THR 585 585 ?   ?   ?   A . n 
A 1 586 ASP 586 586 ?   ?   ?   A . n 
A 1 587 THR 587 587 ?   ?   ?   A . n 
A 1 588 LEU 588 588 ?   ?   ?   A . n 
A 1 589 GLU 589 589 ?   ?   ?   A . n 
A 1 590 SER 590 590 ?   ?   ?   A . n 
A 1 591 THR 591 591 ?   ?   ?   A . n 
A 1 592 THR 592 592 ?   ?   ?   A . n 
A 1 593 VAL 593 593 ?   ?   ?   A . n 
A 1 594 GLY 594 594 ?   ?   ?   A . n 
A 1 595 THR 595 595 ?   ?   ?   A . n 
A 1 596 SER 596 596 ?   ?   ?   A . n 
A 1 597 VAL 597 597 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   VAL 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   ALA 6   6   ?   ?   ?   B . n 
B 1 7   ALA 7   7   ?   ?   ?   B . n 
B 1 8   GLU 8   8   ?   ?   ?   B . n 
B 1 9   VAL 9   9   ?   ?   ?   B . n 
B 1 10  LYS 10  10  ?   ?   ?   B . n 
B 1 11  VAL 11  11  ?   ?   ?   B . n 
B 1 12  ASP 12  12  ?   ?   ?   B . n 
B 1 13  GLY 13  13  ?   ?   ?   B . n 
B 1 14  SER 14  14  ?   ?   ?   B . n 
B 1 15  GLU 15  15  ?   ?   ?   B . n 
B 1 16  PRO 16  16  ?   ?   ?   B . n 
B 1 17  LYS 17  17  ?   ?   ?   B . n 
B 1 18  LEU 18  18  ?   ?   ?   B . n 
B 1 19  SER 19  19  ?   ?   ?   B . n 
B 1 20  LYS 20  20  ?   ?   ?   B . n 
B 1 21  ASN 21  21  ?   ?   ?   B . n 
B 1 22  GLU 22  22  ?   ?   ?   B . n 
B 1 23  LEU 23  23  ?   ?   ?   B . n 
B 1 24  LYS 24  24  ?   ?   ?   B . n 
B 1 25  ARG 25  25  ?   ?   ?   B . n 
B 1 26  ARG 26  26  ?   ?   ?   B . n 
B 1 27  LEU 27  27  ?   ?   ?   B . n 
B 1 28  LYS 28  28  ?   ?   ?   B . n 
B 1 29  ALA 29  29  ?   ?   ?   B . n 
B 1 30  GLU 30  30  ?   ?   ?   B . n 
B 1 31  LYS 31  31  ?   ?   ?   B . n 
B 1 32  LYS 32  32  ?   ?   ?   B . n 
B 1 33  VAL 33  33  ?   ?   ?   B . n 
B 1 34  ALA 34  34  ?   ?   ?   B . n 
B 1 35  GLU 35  35  ?   ?   ?   B . n 
B 1 36  LYS 36  36  ?   ?   ?   B . n 
B 1 37  GLU 37  37  ?   ?   ?   B . n 
B 1 38  ALA 38  38  ?   ?   ?   B . n 
B 1 39  LYS 39  39  ?   ?   ?   B . n 
B 1 40  GLN 40  40  ?   ?   ?   B . n 
B 1 41  LYS 41  41  ?   ?   ?   B . n 
B 1 42  GLU 42  42  ?   ?   ?   B . n 
B 1 43  LEU 43  43  ?   ?   ?   B . n 
B 1 44  SER 44  44  ?   ?   ?   B . n 
B 1 45  GLU 45  45  ?   ?   ?   B . n 
B 1 46  LYS 46  46  ?   ?   ?   B . n 
B 1 47  GLN 47  47  ?   ?   ?   B . n 
B 1 48  LEU 48  48  ?   ?   ?   B . n 
B 1 49  SER 49  49  ?   ?   ?   B . n 
B 1 50  GLN 50  50  ?   ?   ?   B . n 
B 1 51  ALA 51  51  ?   ?   ?   B . n 
B 1 52  THR 52  52  ?   ?   ?   B . n 
B 1 53  ALA 53  53  ?   ?   ?   B . n 
B 1 54  ALA 54  54  ?   ?   ?   B . n 
B 1 55  ALA 55  55  ?   ?   ?   B . n 
B 1 56  THR 56  56  ?   ?   ?   B . n 
B 1 57  ASN 57  57  ?   ?   ?   B . n 
B 1 58  HIS 58  58  ?   ?   ?   B . n 
B 1 59  THR 59  59  ?   ?   ?   B . n 
B 1 60  THR 60  60  ?   ?   ?   B . n 
B 1 61  ASP 61  61  ?   ?   ?   B . n 
B 1 62  ASN 62  62  ?   ?   ?   B . n 
B 1 63  GLY 63  63  ?   ?   ?   B . n 
B 1 64  VAL 64  64  ?   ?   ?   B . n 
B 1 65  GLY 65  65  ?   ?   ?   B . n 
B 1 66  PRO 66  66  ?   ?   ?   B . n 
B 1 67  GLU 67  67  ?   ?   ?   B . n 
B 1 68  GLU 68  68  ?   ?   ?   B . n 
B 1 69  GLU 69  69  ?   ?   ?   B . n 
B 1 70  SER 70  70  ?   ?   ?   B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLN 75  75  75  GLN GLN B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  HIS 85  85  85  HIS HIS B . n 
B 1 86  GLN 86  86  86  GLN GLN B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  ASP 93  93  93  ASP ASP B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  TYR 95  95  95  TYR TYR B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  HIS 97  97  97  HIS HIS B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  PHE 99  99  99  PHE PHE B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ASP 107 107 107 ASP ASP B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 TYR 112 112 112 TYR TYR B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 HIS 114 114 114 HIS HIS B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 PRO 117 117 117 PRO PRO B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 ASP 119 119 119 ASP ASP B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 ASP 123 123 123 ASP ASP B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 HIS 133 133 133 HIS HIS B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 TYR 145 145 145 TYR TYR B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 VAL 156 156 156 VAL VAL B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 ALA 158 158 158 ALA ALA B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 TYR 163 163 163 TYR TYR B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 GLU 168 168 168 GLU GLU B . n 
B 1 169 PHE 169 169 169 PHE PHE B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ASN 173 173 173 ASN ASN B . n 
B 1 174 ASN 174 174 174 ASN ASN B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 LEU 176 176 176 LEU LEU B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 ARG 178 178 178 ARG ARG B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 ASN 187 187 187 ASN ASN B . n 
B 1 188 PRO 188 188 188 PRO PRO B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 LYS 190 190 190 LYS LYS B . n 
B 1 191 THR 191 191 191 THR THR B . n 
B 1 192 LYS 192 192 192 LYS LYS B . n 
B 1 193 LYS 193 193 193 LYS LYS B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 LEU 196 196 196 LEU LEU B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 THR 204 204 204 THR THR B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 HIS 211 211 211 HIS HIS B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 HIS 215 215 215 HIS HIS B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 HIS 217 217 217 HIS HIS B . n 
B 1 218 PHE 218 218 218 PHE PHE B . n 
B 1 219 GLY 219 219 219 GLY GLY B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 ARG 230 230 230 ARG ARG B . n 
B 1 231 TYR 231 231 231 TYR TYR B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 ASP 233 233 233 ASP ASP B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 ILE 235 235 235 ILE ILE B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 PHE 239 239 239 PHE PHE B . n 
B 1 240 VAL 240 240 240 VAL VAL B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 LYS 243 243 243 LYS LYS B . n 
B 1 244 PHE 244 244 244 PHE PHE B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 SER 248 248 248 SER SER B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 ILE 250 250 250 ILE ILE B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 THR 252 252 252 THR THR B . n 
B 1 253 TYR 253 253 253 TYR TYR B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 PHE 257 257 257 PHE PHE B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 GLU 260 260 260 GLU GLU B . n 
B 1 261 LEU 261 261 261 LEU LEU B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 PHE 263 263 263 PHE PHE B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 ILE 266 266 266 ILE ILE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 PRO 269 269 269 PRO PRO B . n 
B 1 270 MET 270 270 270 MET MET B . n 
B 1 271 MET 271 271 271 MET MET B . n 
B 1 272 ASN 272 272 272 ASN ASN B . n 
B 1 273 ILE 273 273 273 ILE ILE B . n 
B 1 274 ILE 274 274 274 ILE ILE B . n 
B 1 275 PRO 275 275 275 PRO PRO B . n 
B 1 276 GLY 276 276 276 GLY GLY B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 PRO 282 282 282 PRO PRO B . n 
B 1 283 PHE 283 283 283 PHE PHE B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 TYR 286 286 286 TYR TYR B . n 
B 1 287 HIS 287 287 287 HIS HIS B . n 
B 1 288 ASN 288 288 288 ASN ASN B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 MET 292 292 292 MET MET B . n 
B 1 293 ASN 293 293 293 ASN ASN B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 MET 296 296 296 MET MET B . n 
B 1 297 ARG 297 297 297 ARG ARG B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 GLU 301 301 301 GLU GLU B . n 
B 1 302 LEU 302 302 302 LEU LEU B . n 
B 1 303 TYR 303 303 303 TYR TYR B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 MET 306 306 306 MET MET B . n 
B 1 307 LEU 307 307 307 LEU LEU B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 GLY 310 310 310 GLY GLY B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 ILE 312 312 312 ILE ILE B . n 
B 1 313 ASP 313 313 313 ASP ASP B . n 
B 1 314 ARG 314 314 314 ARG ARG B . n 
B 1 315 VAL 315 315 315 VAL VAL B . n 
B 1 316 TYR 316 316 316 TYR TYR B . n 
B 1 317 GLU 317 317 317 GLU GLU B . n 
B 1 318 ILE 318 318 318 ILE ILE B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ARG 320 320 320 ARG ARG B . n 
B 1 321 GLN 321 321 321 GLN GLN B . n 
B 1 322 PHE 322 322 322 PHE PHE B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 ASN 324 324 324 ASN ASN B . n 
B 1 325 GLU 325 325 325 GLU GLU B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 THR 330 330 330 THR THR B . n 
B 1 331 HIS 331 331 331 HIS HIS B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 PRO 333 333 333 PRO PRO B . n 
B 1 334 GLU 334 334 334 GLU GLU B . n 
B 1 335 PHE 335 335 335 PHE PHE B . n 
B 1 336 THR 336 336 336 THR THR B . n 
B 1 337 THR 337 337 337 THR THR B . n 
B 1 338 CYS 338 338 338 CYS CYS B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 PHE 340 340 340 PHE PHE B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 MET 342 342 342 MET MET B . n 
B 1 343 ALA 343 343 343 ALA ALA B . n 
B 1 344 TYR 344 344 344 TYR TYR B . n 
B 1 345 ALA 345 345 345 ALA ALA B . n 
B 1 346 ASP 346 346 346 ASP ASP B . n 
B 1 347 TYR 347 347 347 TYR TYR B . n 
B 1 348 HIS 348 348 348 HIS HIS B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 LEU 350 350 350 LEU LEU B . n 
B 1 351 MET 351 351 351 MET MET B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 ILE 353 353 353 ILE ILE B . n 
B 1 354 THR 354 354 354 THR THR B . n 
B 1 355 GLU 355 355 355 GLU GLU B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 MET 357 357 357 MET MET B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 SER 359 359 359 SER SER B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 MET 361 361 361 MET MET B . n 
B 1 362 VAL 362 362 362 VAL VAL B . n 
B 1 363 LYS 363 363 363 LYS LYS B . n 
B 1 364 HIS 364 364 364 HIS HIS B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 GLY 367 367 367 GLY GLY B . n 
B 1 368 SER 368 368 368 SER SER B . n 
B 1 369 TYR 369 369 369 TYR TYR B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 THR 372 372 372 THR THR B . n 
B 1 373 TYR 373 373 373 TYR TYR B . n 
B 1 374 HIS 374 374 374 HIS HIS B . n 
B 1 375 PRO 375 375 375 PRO PRO B . n 
B 1 376 ASP 376 376 376 ASP ASP B . n 
B 1 377 GLY 377 377 377 GLY GLY B . n 
B 1 378 PRO 378 378 378 PRO PRO B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 GLY 380 380 380 GLY GLY B . n 
B 1 381 GLN 381 381 381 GLN GLN B . n 
B 1 382 ALA 382 382 382 ALA ALA B . n 
B 1 383 TYR 383 383 383 TYR TYR B . n 
B 1 384 ASP 384 384 384 ASP ASP B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 ASP 386 386 386 ASP ASP B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 THR 388 388 388 THR THR B . n 
B 1 389 PRO 389 389 389 PRO PRO B . n 
B 1 390 PRO 390 390 390 PRO PRO B . n 
B 1 391 PHE 391 391 391 PHE PHE B . n 
B 1 392 ARG 392 392 392 ARG ARG B . n 
B 1 393 ARG 393 393 393 ARG ARG B . n 
B 1 394 ILE 394 394 394 ILE ILE B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 MET 396 396 396 MET MET B . n 
B 1 397 VAL 397 397 397 VAL VAL B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 LEU 400 400 400 LEU LEU B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 LYS 402 402 402 LYS LYS B . n 
B 1 403 ALA 403 403 403 ALA ALA B . n 
B 1 404 LEU 404 404 404 LEU LEU B . n 
B 1 405 GLY 405 405 405 GLY GLY B . n 
B 1 406 MET 406 406 406 MET MET B . n 
B 1 407 LYS 407 407 407 LYS LYS B . n 
B 1 408 LEU 408 408 408 LEU LEU B . n 
B 1 409 PRO 409 409 409 PRO PRO B . n 
B 1 410 GLU 410 410 410 GLU GLU B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 LEU 413 413 413 LEU LEU B . n 
B 1 414 PHE 414 414 414 PHE PHE B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 THR 416 416 416 THR THR B . n 
B 1 417 GLU 417 417 417 GLU GLU B . n 
B 1 418 GLU 418 418 418 GLU GLU B . n 
B 1 419 THR 419 419 419 THR THR B . n 
B 1 420 ARG 420 420 420 ARG ARG B . n 
B 1 421 LYS 421 421 421 LYS LYS B . n 
B 1 422 ILE 422 422 422 ILE ILE B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 ASP 424 424 424 ASP ASP B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 ILE 426 426 426 ILE ILE B . n 
B 1 427 CYS 427 427 427 CYS CYS B . n 
B 1 428 VAL 428 428 428 VAL VAL B . n 
B 1 429 ALA 429 429 429 ALA ALA B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 ALA 431 431 431 ALA ALA B . n 
B 1 432 VAL 432 432 432 VAL VAL B . n 
B 1 433 GLU 433 433 433 GLU GLU B . n 
B 1 434 CYS 434 434 434 CYS CYS B . n 
B 1 435 PRO 435 435 435 PRO PRO B . n 
B 1 436 PRO 436 436 436 PRO PRO B . n 
B 1 437 PRO 437 437 437 PRO PRO B . n 
B 1 438 ARG 438 438 438 ARG ARG B . n 
B 1 439 THR 439 439 439 THR THR B . n 
B 1 440 THR 440 440 440 THR THR B . n 
B 1 441 ALA 441 441 441 ALA ALA B . n 
B 1 442 ARG 442 442 442 ARG ARG B . n 
B 1 443 LEU 443 443 443 LEU LEU B . n 
B 1 444 LEU 444 444 444 LEU LEU B . n 
B 1 445 ASP 445 445 445 ASP ASP B . n 
B 1 446 LYS 446 446 446 LYS LYS B . n 
B 1 447 LEU 447 447 447 LEU LEU B . n 
B 1 448 VAL 448 448 448 VAL VAL B . n 
B 1 449 GLY 449 449 449 GLY GLY B . n 
B 1 450 GLU 450 450 450 GLU GLU B . n 
B 1 451 PHE 451 451 451 PHE PHE B . n 
B 1 452 LEU 452 452 452 LEU LEU B . n 
B 1 453 GLU 453 453 453 GLU GLU B . n 
B 1 454 VAL 454 454 454 VAL VAL B . n 
B 1 455 THR 455 455 455 THR THR B . n 
B 1 456 CYS 456 456 456 CYS CYS B . n 
B 1 457 ILE 457 457 457 ILE ILE B . n 
B 1 458 ASN 458 458 458 ASN ASN B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 THR 460 460 460 THR THR B . n 
B 1 461 PHE 461 461 461 PHE PHE B . n 
B 1 462 ILE 462 462 462 ILE ILE B . n 
B 1 463 CYS 463 463 463 CYS CYS B . n 
B 1 464 ASP 464 464 464 ASP ASP B . n 
B 1 465 HIS 465 465 465 HIS HIS B . n 
B 1 466 PRO 466 466 466 PRO PRO B . n 
B 1 467 GLN 467 467 467 GLN GLN B . n 
B 1 468 ILE 468 468 468 ILE ILE B . n 
B 1 469 MET 469 469 469 MET MET B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PRO 471 471 471 PRO PRO B . n 
B 1 472 LEU 472 472 472 LEU LEU B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 LYS 474 474 474 LYS LYS B . n 
B 1 475 TRP 475 475 475 TRP TRP B . n 
B 1 476 HIS 476 476 476 HIS HIS B . n 
B 1 477 ARG 477 477 477 ARG ARG B . n 
B 1 478 SER 478 478 478 SER SER B . n 
B 1 479 LYS 479 479 479 LYS LYS B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 GLY 481 481 481 GLY GLY B . n 
B 1 482 LEU 482 482 482 LEU LEU B . n 
B 1 483 THR 483 483 483 THR THR B . n 
B 1 484 GLU 484 484 484 GLU GLU B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 PHE 486 486 486 PHE PHE B . n 
B 1 487 GLU 487 487 487 GLU GLU B . n 
B 1 488 LEU 488 488 488 LEU LEU B . n 
B 1 489 PHE 489 489 489 PHE PHE B . n 
B 1 490 VAL 490 490 490 VAL VAL B . n 
B 1 491 MET 491 491 491 MET MET B . n 
B 1 492 LYS 492 492 492 LYS LYS B . n 
B 1 493 LYS 493 493 493 LYS LYS B . n 
B 1 494 GLU 494 494 494 GLU GLU B . n 
B 1 495 ILE 495 495 495 ILE ILE B . n 
B 1 496 CYS 496 496 496 CYS CYS B . n 
B 1 497 ASN 497 497 497 ASN ASN B . n 
B 1 498 ALA 498 498 498 ALA ALA B . n 
B 1 499 TYR 499 499 499 TYR TYR B . n 
B 1 500 THR 500 500 500 THR THR B . n 
B 1 501 GLU 501 501 501 GLU GLU B . n 
B 1 502 LEU 502 502 502 LEU LEU B . n 
B 1 503 ASN 503 503 503 ASN ASN B . n 
B 1 504 ASP 504 504 504 ASP ASP B . n 
B 1 505 PRO 505 505 505 PRO PRO B . n 
B 1 506 MET 506 506 506 MET MET B . n 
B 1 507 ARG 507 507 507 ARG ARG B . n 
B 1 508 GLN 508 508 508 GLN GLN B . n 
B 1 509 ARG 509 509 509 ARG ARG B . n 
B 1 510 GLN 510 510 510 GLN GLN B . n 
B 1 511 LEU 511 511 511 LEU LEU B . n 
B 1 512 PHE 512 512 512 PHE PHE B . n 
B 1 513 GLU 513 513 513 GLU GLU B . n 
B 1 514 GLU 514 514 514 GLU GLU B . n 
B 1 515 GLN 515 515 515 GLN GLN B . n 
B 1 516 ALA 516 516 516 ALA ALA B . n 
B 1 517 LYS 517 517 517 LYS LYS B . n 
B 1 518 ALA 518 518 518 ALA ALA B . n 
B 1 519 LYS 519 519 519 LYS LYS B . n 
B 1 520 ALA 520 520 520 ALA ALA B . n 
B 1 521 ALA 521 521 521 ALA ALA B . n 
B 1 522 GLY 522 522 522 GLY GLY B . n 
B 1 523 ASP 523 523 523 ASP ASP B . n 
B 1 524 ASP 524 524 524 ASP ASP B . n 
B 1 525 GLU 525 525 525 GLU GLU B . n 
B 1 526 ALA 526 526 526 ALA ALA B . n 
B 1 527 MET 527 527 527 MET MET B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 ILE 529 529 529 ILE ILE B . n 
B 1 530 ASP 530 530 530 ASP ASP B . n 
B 1 531 GLU 531 531 531 GLU GLU B . n 
B 1 532 ASN 532 532 532 ASN ASN B . n 
B 1 533 PHE 533 533 533 PHE PHE B . n 
B 1 534 CYS 534 534 534 CYS CYS B . n 
B 1 535 THR 535 535 535 THR THR B . n 
B 1 536 ALA 536 536 536 ALA ALA B . n 
B 1 537 LEU 537 537 537 LEU LEU B . n 
B 1 538 GLU 538 538 538 GLU GLU B . n 
B 1 539 TYR 539 539 539 TYR TYR B . n 
B 1 540 GLY 540 540 540 GLY GLY B . n 
B 1 541 LEU 541 541 541 LEU LEU B . n 
B 1 542 PRO 542 542 542 PRO PRO B . n 
B 1 543 PRO 543 543 543 PRO PRO B . n 
B 1 544 THR 544 544 544 THR THR B . n 
B 1 545 ALA 545 545 545 ALA ALA B . n 
B 1 546 GLY 546 546 546 GLY GLY B . n 
B 1 547 TRP 547 547 547 TRP TRP B . n 
B 1 548 GLY 548 548 548 GLY GLY B . n 
B 1 549 MET 549 549 549 MET MET B . n 
B 1 550 GLY 550 550 550 GLY GLY B . n 
B 1 551 ILE 551 551 551 ILE ILE B . n 
B 1 552 ASP 552 552 552 ASP ASP B . n 
B 1 553 ARG 553 553 553 ARG ARG B . n 
B 1 554 VAL 554 554 554 VAL VAL B . n 
B 1 555 ALA 555 555 555 ALA ALA B . n 
B 1 556 MET 556 556 556 MET MET B . n 
B 1 557 PHE 557 557 557 PHE PHE B . n 
B 1 558 LEU 558 558 558 LEU LEU B . n 
B 1 559 THR 559 559 559 THR THR B . n 
B 1 560 ASP 560 560 560 ASP ASP B . n 
B 1 561 SER 561 561 561 SER SER B . n 
B 1 562 ASN 562 562 562 ASN ASN B . n 
B 1 563 ASN 563 563 563 ASN ASN B . n 
B 1 564 ILE 564 564 564 ILE ILE B . n 
B 1 565 LYS 565 565 565 LYS LYS B . n 
B 1 566 GLU 566 566 566 GLU GLU B . n 
B 1 567 VAL 567 567 567 VAL VAL B . n 
B 1 568 LEU 568 568 568 LEU LEU B . n 
B 1 569 LEU 569 569 569 LEU LEU B . n 
B 1 570 PHE 570 570 570 PHE PHE B . n 
B 1 571 PRO 571 571 571 PRO PRO B . n 
B 1 572 ALA 572 572 572 ALA ALA B . n 
B 1 573 MET 573 573 573 MET MET B . n 
B 1 574 LYS 574 574 574 LYS LYS B . n 
B 1 575 PRO 575 575 575 PRO PRO B . n 
B 1 576 GLU 576 576 576 GLU GLU B . n 
B 1 577 ASP 577 577 577 ASP ASP B . n 
B 1 578 LYS 578 578 ?   ?   ?   B . n 
B 1 579 LYS 579 579 ?   ?   ?   B . n 
B 1 580 GLU 580 580 ?   ?   ?   B . n 
B 1 581 ASN 581 581 ?   ?   ?   B . n 
B 1 582 VAL 582 582 ?   ?   ?   B . n 
B 1 583 ALA 583 583 ?   ?   ?   B . n 
B 1 584 THR 584 584 ?   ?   ?   B . n 
B 1 585 THR 585 585 ?   ?   ?   B . n 
B 1 586 ASP 586 586 ?   ?   ?   B . n 
B 1 587 THR 587 587 ?   ?   ?   B . n 
B 1 588 LEU 588 588 ?   ?   ?   B . n 
B 1 589 GLU 589 589 ?   ?   ?   B . n 
B 1 590 SER 590 590 ?   ?   ?   B . n 
B 1 591 THR 591 591 ?   ?   ?   B . n 
B 1 592 THR 592 592 ?   ?   ?   B . n 
B 1 593 VAL 593 593 ?   ?   ?   B . n 
B 1 594 GLY 594 594 ?   ?   ?   B . n 
B 1 595 THR 595 595 ?   ?   ?   B . n 
B 1 596 SER 596 596 ?   ?   ?   B . n 
B 1 597 VAL 597 597 ?   ?   ?   B . n 
C 2 1   G   1   1   1   G   G   C . n 
C 2 2   C   2   2   2   C   C   C . n 
C 2 3   C   3   3   3   C   C   C . n 
C 2 4   C   4   4   4   C   C   C . n 
C 2 5   G   5   5   5   G   G   C . n 
C 2 6   G   6   6   6   G   G   C . n 
C 2 7   A   7   7   7   A   A   C . n 
C 2 8   U   8   8   8   U   U   C . n 
C 2 9   A   9   9   9   A   A   C . n 
C 2 10  2MG 10  10  10  2MG 2MG C . n 
C 2 11  C   11  11  11  C   C   C . n 
C 2 12  U   12  12  12  U   U   C . n 
C 2 13  C   13  13  13  C   C   C . n 
C 2 14  A   14  14  14  A   A   C . n 
C 2 15  G   15  15  15  G   G   C . n 
C 2 16  H2U 16  16  16  H2U H2U C . n 
C 2 17  C   17  17  17  C   C   C . n 
C 2 18  G   18  18  18  G   G   C . n 
C 2 19  G   19  19  19  G   G   C . n 
C 2 20  H2U 20  20  20  H2U H2U C . n 
C 2 21  A   21  21  21  A   A   C . n 
C 2 22  G   22  22  22  G   G   C . n 
C 2 23  A   23  23  23  A   A   C . n 
C 2 24  G   24  24  24  G   G   C . n 
C 2 25  C   25  25  25  C   C   C . n 
C 2 26  A   26  26  26  A   A   C . n 
C 2 27  PSU 27  27  27  PSU PSU C . n 
C 2 28  C   28  28  28  C   C   C . n 
C 2 29  A   29  29  29  A   A   C . n 
C 2 30  G   30  30  30  G   G   C . n 
C 2 31  A   31  31  31  A   A   C . n 
C 2 32  C   32  32  32  C   C   C . n 
C 2 33  U   33  33  33  U   U   C . n 
C 2 34  70U 34  34  34  70U 70U C . n 
C 2 35  U   35  35  35  U   U   C . n 
C 2 36  U   36  36  36  U   U   C . n 
C 2 37  12A 37  37  37  12A 12A C . n 
C 2 38  A   38  38  38  A   A   C . n 
C 2 39  PSU 39  39  39  PSU PSU C . n 
C 2 40  C   40  40  40  C   C   C . n 
C 2 41  U   41  41  41  U   U   C . n 
C 2 42  G   42  42  42  G   G   C . n 
C 2 43  A   43  43  43  A   A   C . n 
C 2 44  G   44  44  44  G   G   C . n 
C 2 45  G   45  45  45  G   G   C . n 
C 2 46  7MG 46  46  46  7MG 7MG C . n 
C 2 47  H2U 47  47  47  H2U H2U C . n 
C 2 48  5MC 48  48  48  5MC 5MC C . n 
C 2 49  5MC 49  49  49  5MC 5MC C . n 
C 2 50  A   50  50  50  A   A   C . n 
C 2 51  G   51  51  51  G   G   C . n 
C 2 52  G   52  52  52  G   G   C . n 
C 2 53  G   53  53  53  G   G   C . n 
C 2 54  2MU 54  54  54  2MU 2MU C . n 
C 2 55  PSU 55  55  55  PSU PSU C . n 
C 2 56  C   56  56  56  C   C   C . n 
C 2 57  A   57  57  57  A   A   C . n 
C 2 58  1MA 58  58  58  1MA 1MA C . n 
C 2 59  G   59  59  59  G   G   C . n 
C 2 60  U   60  60  60  U   U   C . n 
C 2 61  C   61  61  61  C   C   C . n 
C 2 62  C   62  62  62  C   C   C . n 
C 2 63  C   63  63  63  C   C   C . n 
C 2 64  U   64  64  64  U   U   C . n 
C 2 65  G   65  65  65  G   G   C . n 
C 2 66  U   66  66  66  U   U   C . n 
C 2 67  U   67  67  67  U   U   C . n 
C 2 68  C   68  68  68  C   C   C . n 
C 2 69  G   69  69  69  G   G   C . n 
C 2 70  G   70  70  70  G   G   C . n 
C 2 71  G   71  71  71  G   G   C . n 
C 2 72  C   72  72  72  C   C   C . n 
C 2 73  G   73  73  73  G   G   C . n 
C 2 74  C   74  74  74  C   C   C . n 
C 2 75  C   75  75  75  C   C   C . n 
C 2 76  A   76  76  76  A   A   C . n 
D 3 1   MET 1   1   1   MET MET D . n 
D 3 2   PRO 2   2   2   PRO PRO D . n 
D 3 3   MET 3   3   3   MET MET D . n 
D 3 4   TYR 4   4   4   TYR TYR D . n 
D 3 5   GLN 5   5   5   GLN GLN D . n 
D 3 6   VAL 6   6   6   VAL VAL D . n 
D 3 7   LYS 7   7   7   LYS LYS D . n 
D 3 8   PRO 8   8   8   PRO PRO D . n 
D 3 9   TYR 9   9   9   TYR TYR D . n 
D 3 10  HIS 10  10  10  HIS HIS D . n 
D 3 11  GLY 11  11  11  GLY GLY D . n 
D 3 12  GLY 12  12  12  GLY GLY D . n 
D 3 13  GLY 13  13  13  GLY GLY D . n 
D 3 14  ALA 14  14  14  ALA ALA D . n 
D 3 15  PRO 15  15  15  PRO PRO D . n 
D 3 16  LEU 16  16  16  LEU LEU D . n 
D 3 17  ARG 17  17  17  ARG ARG D . n 
D 3 18  VAL 18  18  18  VAL VAL D . n 
D 3 19  GLU 19  19  19  GLU GLU D . n 
D 3 20  LEU 20  20  20  LEU LEU D . n 
D 3 21  PRO 21  21  21  PRO PRO D . n 
D 3 22  THR 22  22  ?   ?   ?   D . n 
D 3 23  CYS 23  23  ?   ?   ?   D . n 
D 3 24  MET 24  24  ?   ?   ?   D . n 
D 3 25  TYR 25  25  ?   ?   ?   D . n 
D 3 26  ARG 26  26  ?   ?   ?   D . n 
D 3 27  LEU 27  27  ?   ?   ?   D . n 
D 3 28  PRO 28  28  ?   ?   ?   D . n 
D 3 29  ASN 29  29  ?   ?   ?   D . n 
D 3 30  VAL 30  30  ?   ?   ?   D . n 
D 3 31  HIS 31  31  ?   ?   ?   D . n 
D 3 32  GLY 32  32  ?   ?   ?   D . n 
D 3 33  ARG 33  33  ?   ?   ?   D . n 
D 3 34  SER 34  34  ?   ?   ?   D . n 
D 3 35  TYR 35  35  ?   ?   ?   D . n 
D 3 36  GLY 36  36  ?   ?   ?   D . n 
E 3 1   MET 1   1   1   MET MET E . n 
E 3 2   PRO 2   2   2   PRO PRO E . n 
E 3 3   MET 3   3   3   MET MET E . n 
E 3 4   TYR 4   4   4   TYR TYR E . n 
E 3 5   GLN 5   5   5   GLN GLN E . n 
E 3 6   VAL 6   6   6   VAL VAL E . n 
E 3 7   LYS 7   7   7   LYS LYS E . n 
E 3 8   PRO 8   8   8   PRO PRO E . n 
E 3 9   TYR 9   9   9   TYR TYR E . n 
E 3 10  HIS 10  10  10  HIS HIS E . n 
E 3 11  GLY 11  11  11  GLY GLY E . n 
E 3 12  GLY 12  12  12  GLY GLY E . n 
E 3 13  GLY 13  13  13  GLY GLY E . n 
E 3 14  ALA 14  14  14  ALA ALA E . n 
E 3 15  PRO 15  15  15  PRO PRO E . n 
E 3 16  LEU 16  16  16  LEU LEU E . n 
E 3 17  ARG 17  17  17  ARG ARG E . n 
E 3 18  VAL 18  18  18  VAL VAL E . n 
E 3 19  GLU 19  19  19  GLU GLU E . n 
E 3 20  LEU 20  20  20  LEU LEU E . n 
E 3 21  PRO 21  21  21  PRO PRO E . n 
E 3 22  THR 22  22  ?   ?   ?   E . n 
E 3 23  CYS 23  23  ?   ?   ?   E . n 
E 3 24  MET 24  24  ?   ?   ?   E . n 
E 3 25  TYR 25  25  ?   ?   ?   E . n 
E 3 26  ARG 26  26  ?   ?   ?   E . n 
E 3 27  LEU 27  27  ?   ?   ?   E . n 
E 3 28  PRO 28  28  ?   ?   ?   E . n 
E 3 29  ASN 29  29  ?   ?   ?   E . n 
E 3 30  VAL 30  30  ?   ?   ?   E . n 
E 3 31  HIS 31  31  ?   ?   ?   E . n 
E 3 32  GLY 32  32  ?   ?   ?   E . n 
E 3 33  ARG 33  33  ?   ?   ?   E . n 
E 3 34  SER 34  34  ?   ?   ?   E . n 
E 3 35  TYR 35  35  ?   ?   ?   E . n 
E 3 36  GLY 36  36  ?   ?   ?   E . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 LYS ? ? LYS ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AMP ? ? AMP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
F 4 LYS 1 601 601 LYS LYS A . 
G 5 AMP 1 602 801 AMP AMP A . 
H 4 LYS 1 601 601 LYS LYS B . 
I 5 AMP 1 602 786 AMP AMP B . 
J 6 NA  1 101 202 NA  NA  C . 
K 6 NA  1 102 203 NA  NA  C . 
L 7 MG  1 103 78  MG  MG  C . 
M 7 MG  1 104 201 MG  MG  C . 
# 
_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                     9DPL 
_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                         9DPL 
_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                   9DPL 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9DPL 
_struct.title                        'Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2' 
_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        9DPL 
_struct_keywords.text            'Aminoacylation, tRNA, multi-tRNA synthetase complex, LysRS, TRANSLATION' 
_struct_keywords.pdbx_keywords   TRANSLATION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
L N N 7 ? 
M N N 7 ? 
# 
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 SYK_HUMAN   Q15046 ? 1 
;MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIR
SQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANS
RNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGR
QFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEEL
EKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD
SNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
;
1 
2 PDB 9DPL        9DPL   ? 2 ? 1 
3 UNP AIMP2_HUMAN Q13155 ? 3 MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYG 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 9DPL A 1 ? 597 ? Q15046 1 ? 597 ? 1 597 
2 1 9DPL B 1 ? 597 ? Q15046 1 ? 597 ? 1 597 
3 2 9DPL C 1 ? 76  ? 9DPL   1 ? 76  ? 1 76  
4 3 9DPL D 1 ? 36  ? Q13155 1 ? 36  ? 1 36  
5 3 9DPL E 1 ? 36  ? Q13155 1 ? 36  ? 1 36  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 19  ? LYS A 41  ? SER A 19  LYS A 41  1 ? 23 
HELX_P HELX_P2  AA2 GLN A 75  ? ASN A 90  ? GLN A 75  ASN A 90  1 ? 16 
HELX_P HELX_P3  AA3 SER A 104 ? SER A 113 ? SER A 104 SER A 113 1 ? 10 
HELX_P HELX_P4  AA4 SER A 165 ? LEU A 176 ? SER A 165 LEU A 176 1 ? 12 
HELX_P HELX_P5  AA5 ASP A 222 ? GLN A 229 ? ASP A 222 GLN A 229 1 ? 8  
HELX_P HELX_P6  AA6 GLN A 229 ? ASN A 237 ? GLN A 229 ASN A 237 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 238 ? GLY A 262 ? ASP A 238 GLY A 262 1 ? 25 
HELX_P HELX_P8  AA8 PRO A 300 ? GLY A 311 ? PRO A 300 GLY A 311 1 ? 12 
HELX_P HELX_P9  AA9 ASP A 346 ? GLY A 367 ? ASP A 346 GLY A 367 1 ? 22 
HELX_P HELX_P10 AB1 MET A 396 ? GLY A 405 ? MET A 396 GLY A 405 1 ? 10 
HELX_P HELX_P11 AB2 THR A 416 ? LYS A 430 ? THR A 416 LYS A 430 1 ? 15 
HELX_P HELX_P12 AB3 THR A 439 ? LEU A 452 ? THR A 439 LEU A 452 1 ? 14 
HELX_P HELX_P13 AB4 PRO A 466 ? SER A 470 ? PRO A 466 SER A 470 5 ? 5  
HELX_P HELX_P14 AB5 ASP A 504 ? ALA A 521 ? ASP A 504 ALA A 521 1 ? 18 
HELX_P HELX_P15 AB6 ASP A 524 ? PHE A 528 ? ASP A 524 PHE A 528 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 530 ? GLY A 540 ? ASP A 530 GLY A 540 1 ? 11 
HELX_P HELX_P17 AB8 ILE A 551 ? ASP A 560 ? ILE A 551 ASP A 560 1 ? 10 
HELX_P HELX_P18 AB9 ASN A 563 ? VAL A 567 ? ASN A 563 VAL A 567 5 ? 5  
HELX_P HELX_P19 AC1 ASP B 72  ? ASN B 90  ? ASP B 72  ASN B 90  1 ? 19 
HELX_P HELX_P20 AC2 SER B 104 ? TYR B 112 ? SER B 104 TYR B 112 1 ? 9  
HELX_P HELX_P21 AC3 SER B 165 ? ASN B 174 ? SER B 165 ASN B 174 1 ? 10 
HELX_P HELX_P22 AC4 ASP B 222 ? GLN B 229 ? ASP B 222 GLN B 229 1 ? 8  
HELX_P HELX_P23 AC5 GLN B 229 ? ASN B 237 ? GLN B 229 ASN B 237 1 ? 9  
HELX_P HELX_P24 AC6 ASP B 238 ? GLY B 262 ? ASP B 238 GLY B 262 1 ? 25 
HELX_P HELX_P25 AC7 PRO B 300 ? GLY B 311 ? PRO B 300 GLY B 311 1 ? 12 
HELX_P HELX_P26 AC8 ASP B 346 ? GLY B 367 ? ASP B 346 GLY B 367 1 ? 22 
HELX_P HELX_P27 AC9 MET B 396 ? GLY B 405 ? MET B 396 GLY B 405 1 ? 10 
HELX_P HELX_P28 AD1 GLU B 410 ? PHE B 414 ? GLU B 410 PHE B 414 5 ? 5  
HELX_P HELX_P29 AD2 GLU B 417 ? LYS B 430 ? GLU B 417 LYS B 430 1 ? 14 
HELX_P HELX_P30 AD3 THR B 439 ? LEU B 452 ? THR B 439 LEU B 452 1 ? 14 
HELX_P HELX_P31 AD4 GLU B 453 ? CYS B 456 ? GLU B 453 CYS B 456 5 ? 4  
HELX_P HELX_P32 AD5 PRO B 466 ? SER B 470 ? PRO B 466 SER B 470 5 ? 5  
HELX_P HELX_P33 AD6 ASP B 504 ? ALA B 521 ? ASP B 504 ALA B 521 1 ? 18 
HELX_P HELX_P34 AD7 ASP B 530 ? GLU B 538 ? ASP B 530 GLU B 538 1 ? 9  
HELX_P HELX_P35 AD8 ASP B 552 ? ASP B 560 ? ASP B 552 ASP B 560 1 ? 9  
HELX_P HELX_P36 AD9 ASN B 563 ? LEU B 568 ? ASN B 563 LEU B 568 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? C A   9  "O3'" ? ? ? 1_555 C 2MG 10 P  ? ? C A   9  C 2MG 10 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale2  covale both ? C 2MG 10 "O3'" ? ? ? 1_555 C C   11 P  ? ? C 2MG 10 C C   11 1_555 ? ? ? ? ? ? ?                       
1.607 ? ? 
covale3  covale both ? C G   15 "O3'" ? ? ? 1_555 C H2U 16 P  ? ? C G   15 C H2U 16 1_555 ? ? ? ? ? ? ?                       
1.605 ? ? 
covale4  covale both ? C H2U 16 "O3'" ? ? ? 1_555 C C   17 P  ? ? C H2U 16 C C   17 1_555 ? ? ? ? ? ? ?                       
1.609 ? ? 
covale5  covale both ? C G   19 "O3'" ? ? ? 1_555 C H2U 20 P  ? ? C G   19 C H2U 20 1_555 ? ? ? ? ? ? ?                       
1.605 ? ? 
covale6  covale both ? C H2U 20 "O3'" ? ? ? 1_555 C A   21 P  ? ? C H2U 20 C A   21 1_555 ? ? ? ? ? ? ?                       
1.605 ? ? 
covale7  covale both ? C A   26 "O3'" ? ? ? 1_555 C PSU 27 P  ? ? C A   26 C PSU 27 1_555 ? ? ? ? ? ? ?                       
1.603 ? ? 
covale8  covale both ? C PSU 27 "O3'" ? ? ? 1_555 C C   28 P  ? ? C PSU 27 C C   28 1_555 ? ? ? ? ? ? ?                       
1.604 ? ? 
covale9  covale both ? C U   33 "O3'" ? ? ? 1_555 C 70U 34 P  ? ? C U   33 C 70U 34 1_555 ? ? ? ? ? ? ?                       
1.604 ? ? 
covale10 covale both ? C 70U 34 "O3'" ? ? ? 1_555 C U   35 P  ? ? C 70U 34 C U   35 1_555 ? ? ? ? ? ? ?                       
1.605 ? ? 
covale11 covale both ? C U   36 "O3'" ? ? ? 1_555 C 12A 37 P  ? ? C U   36 C 12A 37 1_555 ? ? ? ? ? ? ?                       
1.610 ? ? 
covale12 covale both ? C 12A 37 "O3'" ? ? ? 1_555 C A   38 P  ? ? C 12A 37 C A   38 1_555 ? ? ? ? ? ? ?                       
1.608 ? ? 
covale13 covale both ? C A   38 "O3'" ? ? ? 1_555 C PSU 39 P  ? ? C A   38 C PSU 39 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale14 covale both ? C PSU 39 "O3'" ? ? ? 1_555 C C   40 P  ? ? C PSU 39 C C   40 1_555 ? ? ? ? ? ? ?                       
1.605 ? ? 
covale15 covale both ? C G   45 "O3'" ? ? ? 1_555 C 7MG 46 P  ? ? C G   45 C 7MG 46 1_555 ? ? ? ? ? ? ?                       
1.607 ? ? 
covale16 covale both ? C 7MG 46 "O3'" ? ? ? 1_555 C H2U 47 P  ? ? C 7MG 46 C H2U 47 1_555 ? ? ? ? ? ? ?                       
1.608 ? ? 
covale17 covale both ? C H2U 47 "O3'" ? ? ? 1_555 C 5MC 48 P  ? ? C H2U 47 C 5MC 48 1_555 ? ? ? ? ? ? ?                       
1.609 ? ? 
covale18 covale both ? C 5MC 48 "O3'" ? ? ? 1_555 C 5MC 49 P  ? ? C 5MC 48 C 5MC 49 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale19 covale both ? C 5MC 49 "O3'" ? ? ? 1_555 C A   50 P  ? ? C 5MC 49 C A   50 1_555 ? ? ? ? ? ? ?                       
1.610 ? ? 
covale20 covale both ? C G   53 "O3'" ? ? ? 1_555 C 2MU 54 P  ? ? C G   53 C 2MU 54 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale21 covale both ? C 2MU 54 "O3'" ? ? ? 1_555 C PSU 55 P  ? ? C 2MU 54 C PSU 55 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale22 covale both ? C PSU 55 "O3'" ? ? ? 1_555 C C   56 P  ? ? C PSU 55 C C   56 1_555 ? ? ? ? ? ? ?                       
1.606 ? ? 
covale23 covale both ? C A   57 "O3'" ? ? ? 1_555 C 1MA 58 P  ? ? C A   57 C 1MA 58 1_555 ? ? ? ? ? ? ?                       
1.603 ? ? 
covale24 covale both ? C 1MA 58 "O3'" ? ? ? 1_555 C G   59 P  ? ? C 1MA 58 C G   59 1_555 ? ? ? ? ? ? ?                       
1.604 ? ? 
hydrog1  hydrog ?    ? C G   1  N1    ? ? ? 1_555 C C   72 N3 ? ? C G   1  C C   72 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog2  hydrog ?    ? C G   1  N2    ? ? ? 1_555 C C   72 O2 ? ? C G   1  C C   72 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog3  hydrog ?    ? C G   1  O6    ? ? ? 1_555 C C   72 N4 ? ? C G   1  C C   72 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog4  hydrog ?    ? C C   2  N3    ? ? ? 1_555 C G   71 N1 ? ? C C   2  C G   71 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog5  hydrog ?    ? C C   2  N4    ? ? ? 1_555 C G   71 O6 ? ? C C   2  C G   71 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog6  hydrog ?    ? C C   2  O2    ? ? ? 1_555 C G   71 N2 ? ? C C   2  C G   71 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog7  hydrog ?    ? C C   3  N3    ? ? ? 1_555 C G   70 N1 ? ? C C   3  C G   70 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog8  hydrog ?    ? C C   3  N4    ? ? ? 1_555 C G   70 O6 ? ? C C   3  C G   70 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog9  hydrog ?    ? C C   3  O2    ? ? ? 1_555 C G   70 N2 ? ? C C   3  C G   70 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog10 hydrog ?    ? C C   4  N3    ? ? ? 1_555 C G   69 N1 ? ? C C   4  C G   69 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog11 hydrog ?    ? C C   4  N4    ? ? ? 1_555 C G   69 O6 ? ? C C   4  C G   69 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog12 hydrog ?    ? C C   4  O2    ? ? ? 1_555 C G   69 N2 ? ? C C   4  C G   69 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog13 hydrog ?    ? C G   5  N1    ? ? ? 1_555 C C   68 N3 ? ? C G   5  C C   68 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog14 hydrog ?    ? C G   5  N2    ? ? ? 1_555 C C   68 O2 ? ? C G   5  C C   68 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog15 hydrog ?    ? C G   5  O6    ? ? ? 1_555 C C   68 N4 ? ? C G   5  C C   68 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog16 hydrog ?    ? C G   6  N1    ? ? ? 1_555 C U   67 O2 ? ? C G   6  C U   67 1_555 ? ? ? ? ? ? TYPE_28_PAIR            ? ? 
? 
hydrog17 hydrog ?    ? C G   6  O6    ? ? ? 1_555 C U   67 N3 ? ? C G   6  C U   67 1_555 ? ? ? ? ? ? TYPE_28_PAIR            ? ? 
? 
hydrog18 hydrog ?    ? C A   7  N1    ? ? ? 1_555 C U   66 N3 ? ? C A   7  C U   66 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog19 hydrog ?    ? C A   7  N6    ? ? ? 1_555 C U   66 O4 ? ? C A   7  C U   66 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog20 hydrog ?    ? C U   8  N3    ? ? ? 1_555 C A   14 N7 ? ? C U   8  C A   14 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN'    ? ? 
? 
hydrog21 hydrog ?    ? C U   8  O2    ? ? ? 1_555 C A   14 N6 ? ? C U   8  C A   14 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN'    ? ? 
? 
hydrog22 hydrog ?    ? C A   9  N6    ? ? ? 1_555 C A   23 N7 ? ? C A   9  C A   23 1_555 ? ? ? ? ? ? TYPE_2_PAIR             ? ? 
? 
hydrog23 hydrog ?    ? C A   9  N7    ? ? ? 1_555 C A   23 N6 ? ? C A   9  C A   23 1_555 ? ? ? ? ? ? TYPE_2_PAIR             ? ? 
? 
hydrog24 hydrog ?    ? C 2MG 10 N1    ? ? ? 1_555 C C   25 N3 ? ? C 2MG 10 C C   25 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog25 hydrog ?    ? C 2MG 10 N2    ? ? ? 1_555 C C   25 O2 ? ? C 2MG 10 C C   25 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog26 hydrog ?    ? C 2MG 10 O6    ? ? ? 1_555 C C   25 N4 ? ? C 2MG 10 C C   25 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog27 hydrog ?    ? C 2MG 10 N7    ? ? ? 1_555 C G   45 N2 ? ? C 2MG 10 C G   45 1_555 ? ? ? ? ? ? TYPE_6_PAIR             ? ? 
? 
hydrog28 hydrog ?    ? C 2MG 10 O6    ? ? ? 1_555 C G   45 N1 ? ? C 2MG 10 C G   45 1_555 ? ? ? ? ? ? TYPE_6_PAIR             ? ? 
? 
hydrog29 hydrog ?    ? C C   11 N3    ? ? ? 1_555 C G   24 N1 ? ? C C   11 C G   24 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog30 hydrog ?    ? C C   11 N4    ? ? ? 1_555 C G   24 O6 ? ? C C   11 C G   24 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog31 hydrog ?    ? C C   11 O2    ? ? ? 1_555 C G   24 N2 ? ? C C   11 C G   24 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog32 hydrog ?    ? C U   12 N3    ? ? ? 1_555 C A   23 N1 ? ? C U   12 C A   23 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog33 hydrog ?    ? C U   12 O4    ? ? ? 1_555 C A   23 N6 ? ? C U   12 C A   23 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog34 hydrog ?    ? C C   13 N3    ? ? ? 1_555 C G   22 N1 ? ? C C   13 C G   22 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog35 hydrog ?    ? C C   13 N4    ? ? ? 1_555 C G   22 O6 ? ? C C   13 C G   22 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog36 hydrog ?    ? C C   13 O2    ? ? ? 1_555 C G   22 N2 ? ? C C   13 C G   22 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog37 hydrog ?    ? C A   14 N6    ? ? ? 1_555 C A   21 N3 ? ? C A   14 C A   21 1_555 ? ? ? ? ? ? 'A-A MISPAIR'           ? ? 
? 
hydrog38 hydrog ?    ? C G   15 N1    ? ? ? 1_555 C 5MC 48 O2 ? ? C G   15 C 5MC 48 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog39 hydrog ?    ? C G   15 N2    ? ? ? 1_555 C 5MC 48 N3 ? ? C G   15 C 5MC 48 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog40 hydrog ?    ? C G   18 N2    ? ? ? 1_555 C PSU 55 O4 ? ? C G   18 C PSU 55 1_555 ? ? ? ? ? ? 'G-PSU MISPAIR'         ? ? 
? 
hydrog41 hydrog ?    ? C G   19 N1    ? ? ? 1_555 C C   56 N3 ? ? C G   19 C C   56 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog42 hydrog ?    ? C G   19 N2    ? ? ? 1_555 C C   56 O2 ? ? C G   19 C C   56 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog43 hydrog ?    ? C G   19 O6    ? ? ? 1_555 C C   56 N4 ? ? C G   19 C C   56 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog44 hydrog ?    ? C G   22 N7    ? ? ? 1_555 C 7MG 46 N1 ? ? C G   22 C 7MG 46 1_555 ? ? ? ? ? ? TYPE_7_PAIR             ? ? 
? 
hydrog45 hydrog ?    ? C G   22 O6    ? ? ? 1_555 C 7MG 46 N2 ? ? C G   22 C 7MG 46 1_555 ? ? ? ? ? ? TYPE_7_PAIR             ? ? 
? 
hydrog46 hydrog ?    ? C C   25 N4    ? ? ? 1_555 C G   45 O6 ? ? C C   25 C G   45 1_555 ? ? ? ? ? ? 'C-G PAIR'              ? ? 
? 
hydrog47 hydrog ?    ? C A   26 N1    ? ? ? 1_555 C G   44 N1 ? ? C A   26 C G   44 1_555 ? ? ? ? ? ? TYPE_8_PAIR             ? ? 
? 
hydrog48 hydrog ?    ? C A   26 N6    ? ? ? 1_555 C G   44 O6 ? ? C A   26 C G   44 1_555 ? ? ? ? ? ? TYPE_8_PAIR             ? ? 
? 
hydrog49 hydrog ?    ? C PSU 27 N3    ? ? ? 1_555 C A   43 N1 ? ? C PSU 27 C A   43 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog50 hydrog ?    ? C PSU 27 O2    ? ? ? 1_555 C A   43 N6 ? ? C PSU 27 C A   43 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog51 hydrog ?    ? C C   28 N3    ? ? ? 1_555 C G   42 N1 ? ? C C   28 C G   42 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog52 hydrog ?    ? C C   28 N4    ? ? ? 1_555 C G   42 O6 ? ? C C   28 C G   42 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog53 hydrog ?    ? C C   28 O2    ? ? ? 1_555 C G   42 N2 ? ? C C   28 C G   42 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog54 hydrog ?    ? C A   29 N1    ? ? ? 1_555 C U   41 N3 ? ? C A   29 C U   41 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog55 hydrog ?    ? C A   29 N6    ? ? ? 1_555 C U   41 O4 ? ? C A   29 C U   41 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog56 hydrog ?    ? C G   30 N1    ? ? ? 1_555 C C   40 N3 ? ? C G   30 C C   40 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog57 hydrog ?    ? C G   30 N2    ? ? ? 1_555 C C   40 O2 ? ? C G   30 C C   40 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog58 hydrog ?    ? C G   30 O6    ? ? ? 1_555 C C   40 N4 ? ? C G   30 C C   40 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog59 hydrog ?    ? C A   31 N1    ? ? ? 1_555 C PSU 39 N3 ? ? C A   31 C PSU 39 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog60 hydrog ?    ? C A   31 N6    ? ? ? 1_555 C PSU 39 O2 ? ? C A   31 C PSU 39 1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ? ? 
? 
hydrog61 hydrog ?    ? C C   32 O2    ? ? ? 1_555 C A   38 N6 ? ? C C   32 C A   38 1_555 ? ? ? ? ? ? 'C-A MISPAIR'           ? ? 
? 
hydrog62 hydrog ?    ? C 5MC 49 N3    ? ? ? 1_555 C G   65 N1 ? ? C 5MC 49 C G   65 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog63 hydrog ?    ? C 5MC 49 N4    ? ? ? 1_555 C G   65 O6 ? ? C 5MC 49 C G   65 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog64 hydrog ?    ? C 5MC 49 O2    ? ? ? 1_555 C G   65 N2 ? ? C 5MC 49 C G   65 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog65 hydrog ?    ? C A   50 N1    ? ? ? 1_555 C U   64 N3 ? ? C A   50 C U   64 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog66 hydrog ?    ? C A   50 N6    ? ? ? 1_555 C U   64 O4 ? ? C A   50 C U   64 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog67 hydrog ?    ? C G   51 N1    ? ? ? 1_555 C C   63 N3 ? ? C G   51 C C   63 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog68 hydrog ?    ? C G   51 N2    ? ? ? 1_555 C C   63 O2 ? ? C G   51 C C   63 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog69 hydrog ?    ? C G   51 O6    ? ? ? 1_555 C C   63 N4 ? ? C G   51 C C   63 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog70 hydrog ?    ? C G   52 N1    ? ? ? 1_555 C C   62 N3 ? ? C G   52 C C   62 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog71 hydrog ?    ? C G   52 N2    ? ? ? 1_555 C C   62 O2 ? ? C G   52 C C   62 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog72 hydrog ?    ? C G   52 O6    ? ? ? 1_555 C C   62 N4 ? ? C G   52 C C   62 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog73 hydrog ?    ? C G   53 N1    ? ? ? 1_555 C C   61 N3 ? ? C G   53 C C   61 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog74 hydrog ?    ? C G   53 N2    ? ? ? 1_555 C C   61 O2 ? ? C G   53 C C   61 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog75 hydrog ?    ? C G   53 O6    ? ? ? 1_555 C C   61 N4 ? ? C G   53 C C   61 1_555 ? ? ? ? ? ? WATSON-CRICK            ? ? 
? 
hydrog76 hydrog ?    ? C 2MU 54 N3    ? ? ? 1_555 C 1MA 58 N7 ? ? C 2MU 54 C 1MA 58 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN'    ? ? 
? 
hydrog77 hydrog ?    ? C 2MU 54 O2    ? ? ? 1_555 C 1MA 58 N6 ? ? C 2MU 54 C 1MA 58 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN'    ? ? 
? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
hydrog ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 436 A . ? PRO 436 A PRO 437 A ? PRO 437 A 1 2.47 
2 PRO 436 B . ? PRO 436 B PRO 437 B ? PRO 437 B 1 1.96 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 8 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 8 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 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 LEU A 126 ? ALA A 137 ? LEU A 126 ALA A 137 
AA1 2 LEU A 142 ? GLY A 149 ? LEU A 142 GLY A 149 
AA1 3 VAL A 152 ? ASN A 159 ? VAL A 152 ASN A 159 
AA1 4 LEU A 196 ? SER A 207 ? LEU A 196 SER A 207 
AA1 5 ILE A 181 ? LYS A 190 ? ILE A 181 LYS A 190 
AA1 6 LEU A 126 ? ALA A 137 ? LEU A 126 ALA A 137 
AA2 1 LEU A 264 ? GLU A 265 ? LEU A 264 GLU A 265 
AA2 2 ARG A 314 ? PHE A 322 ? ARG A 314 PHE A 322 
AA2 3 GLU A 334 ? ALA A 343 ? GLU A 334 ALA A 343 
AA2 4 THR A 544 ? GLY A 550 ? THR A 544 GLY A 550 
AA2 5 LYS A 493 ? THR A 500 ? LYS A 493 THR A 500 
AA2 6 ARG A 485 ? VAL A 490 ? ARG A 485 VAL A 490 
AA2 7 THR A 460 ? CYS A 463 ? THR A 460 CYS A 463 
AA2 8 ARG A 392 ? ASN A 395 ? ARG A 392 ASN A 395 
AA3 1 MET A 271 ? ASN A 272 ? MET A 271 ASN A 272 
AA3 2 MET A 292 ? MET A 296 ? MET A 292 MET A 296 
AA3 3 ILE A 284 ? HIS A 287 ? ILE A 284 HIS A 287 
AA4 1 LYS A 370 ? TYR A 373 ? LYS A 370 TYR A 373 
AA4 2 TYR A 383 ? ASP A 386 ? TYR A 383 ASP A 386 
AA5 1 LEU B 126 ? ALA B 137 ? LEU B 126 ALA B 137 
AA5 2 LEU B 142 ? ARG B 148 ? LEU B 142 ARG B 148 
AA5 3 LYS B 153 ? ASN B 159 ? LYS B 153 ASN B 159 
AA5 4 LEU B 196 ? SER B 207 ? LEU B 196 SER B 207 
AA5 5 ILE B 181 ? LYS B 190 ? ILE B 181 LYS B 190 
AA5 6 LEU B 126 ? ALA B 137 ? LEU B 126 ALA B 137 
AA6 1 LEU B 264 ? GLU B 265 ? LEU B 264 GLU B 265 
AA6 2 VAL B 315 ? PHE B 322 ? VAL B 315 PHE B 322 
AA6 3 GLU B 334 ? ALA B 343 ? GLU B 334 ALA B 343 
AA6 4 THR B 544 ? GLY B 550 ? THR B 544 GLY B 550 
AA6 5 LYS B 493 ? THR B 500 ? LYS B 493 THR B 500 
AA6 6 ARG B 485 ? VAL B 490 ? ARG B 485 VAL B 490 
AA6 7 THR B 460 ? CYS B 463 ? THR B 460 CYS B 463 
AA6 8 ARG B 392 ? ASN B 395 ? ARG B 392 ASN B 395 
AA7 1 MET B 271 ? ASN B 272 ? MET B 271 ASN B 272 
AA7 2 ASN B 293 ? MET B 296 ? ASN B 293 MET B 296 
AA7 3 ILE B 284 ? TYR B 286 ? ILE B 284 TYR B 286 
AA8 1 LYS B 370 ? TYR B 373 ? LYS B 370 TYR B 373 
AA8 2 TYR B 383 ? ASP B 386 ? TYR B 383 ASP B 386 
# 
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 ARG A 131 ? N ARG A 131 O ARG A 148 ? O ARG A 148 
AA1 2 3 N TYR A 145 ? N TYR A 145 O VAL A 156 ? O VAL A 156 
AA1 3 4 N GLN A 155 ? N GLN A 155 O ILE A 198 ? O ILE A 198 
AA1 4 5 O TYR A 201 ? O TYR A 201 N GLN A 185 ? N GLN A 185 
AA1 5 6 O ILE A 182 ? O ILE A 182 N GLY A 130 ? N GLY A 130 
AA2 1 2 N LEU A 264 ? N LEU A 264 O TYR A 316 ? O TYR A 316 
AA2 2 3 N GLU A 317 ? N GLU A 317 O GLU A 339 ? O GLU A 339 
AA2 3 4 N PHE A 340 ? N PHE A 340 O TRP A 547 ? O TRP A 547 
AA2 4 5 O GLY A 550 ? O GLY A 550 N ILE A 495 ? N ILE A 495 
AA2 5 6 O ALA A 498 ? O ALA A 498 N PHE A 486 ? N PHE A 486 
AA2 6 7 O PHE A 489 ? O PHE A 489 N THR A 460 ? N THR A 460 
AA2 7 8 O PHE A 461 ? O PHE A 461 N ARG A 392 ? N ARG A 392 
AA3 1 2 N ASN A 272 ? N ASN A 272 O TYR A 295 ? O TYR A 295 
AA3 2 3 O MET A 292 ? O MET A 292 N HIS A 287 ? N HIS A 287 
AA4 1 2 N TYR A 373 ? N TYR A 373 O TYR A 383 ? O TYR A 383 
AA5 1 2 N HIS B 133 ? N HIS B 133 O ASP B 146 ? O ASP B 146 
AA5 2 3 N ILE B 143 ? N ILE B 143 O ALA B 158 ? O ALA B 158 
AA5 3 4 N GLN B 155 ? N GLN B 155 O ILE B 198 ? O ILE B 198 
AA5 4 5 O TYR B 201 ? O TYR B 201 N GLN B 185 ? N GLN B 185 
AA5 5 6 O ILE B 182 ? O ILE B 182 N GLY B 130 ? N GLY B 130 
AA6 1 2 N LEU B 264 ? N LEU B 264 O TYR B 316 ? O TYR B 316 
AA6 2 3 N VAL B 315 ? N VAL B 315 O TYR B 341 ? O TYR B 341 
AA6 3 4 N MET B 342 ? N MET B 342 O ALA B 545 ? O ALA B 545 
AA6 4 5 O GLY B 546 ? O GLY B 546 N TYR B 499 ? N TYR B 499 
AA6 5 6 O LYS B 493 ? O LYS B 493 N VAL B 490 ? N VAL B 490 
AA6 6 7 O PHE B 489 ? O PHE B 489 N THR B 460 ? N THR B 460 
AA6 7 8 O PHE B 461 ? O PHE B 461 N ILE B 394 ? N ILE B 394 
AA7 1 2 N ASN B 272 ? N ASN B 272 O TYR B 295 ? O TYR B 295 
AA7 2 3 O LEU B 294 ? O LEU B 294 N THR B 285 ? N THR B 285 
AA8 1 2 N TYR B 373 ? N TYR B 373 O TYR B 383 ? O TYR B 383 
# 
_pdbx_entry_details.entry_id                   9DPL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 17  ? ? 52.91   12.91   
2  1 LEU A 18  ? ? 48.06   -135.87 
3  1 GLU A 325 ? ? -126.69 -169.85 
4  1 PRO A 409 ? ? -59.35  170.08  
5  1 ARG A 438 ? ? -94.27  57.46   
6  1 LEU A 472 ? ? 55.79   16.53   
7  1 ASP A 523 ? ? 57.23   -142.13 
8  1 GLU B 92  ? ? -119.72 50.16   
9  1 ASP B 93  ? ? -39.48  117.90  
10 1 GLU B 150 ? ? -91.23  31.11   
11 1 ASN B 324 ? ? -93.09  54.72   
12 1 ASP B 552 ? ? -135.96 -37.29  
13 1 ASN B 562 ? ? -91.40  50.59   
14 1 ALA E 14  ? ? 48.40   74.06   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DPL 
_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                    9DPL 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.80 
_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               232412 
_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            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_imaging.entry_id                        9DPL 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_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                      2.7 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           81000 
_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            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9DPL 
_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                9DPL 
_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 MET 1   ? A MET 1   
2   1 Y 1 A ALA 2   ? A ALA 2   
3   1 Y 1 A ALA 3   ? A ALA 3   
4   1 Y 1 A VAL 4   ? A VAL 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A ALA 6   ? A ALA 6   
7   1 Y 1 A ALA 7   ? A ALA 7   
8   1 Y 1 A GLU 8   ? A GLU 8   
9   1 Y 1 A VAL 9   ? A VAL 9   
10  1 Y 1 A LYS 10  ? A LYS 10  
11  1 Y 1 A VAL 11  ? A VAL 11  
12  1 Y 1 A ASP 12  ? A ASP 12  
13  1 Y 1 A GLY 13  ? A GLY 13  
14  1 Y 1 A SER 44  ? A SER 44  
15  1 Y 1 A GLU 45  ? A GLU 45  
16  1 Y 1 A LYS 46  ? A LYS 46  
17  1 Y 1 A GLN 47  ? A GLN 47  
18  1 Y 1 A LEU 48  ? A LEU 48  
19  1 Y 1 A SER 49  ? A SER 49  
20  1 Y 1 A GLN 50  ? A GLN 50  
21  1 Y 1 A ALA 51  ? A ALA 51  
22  1 Y 1 A THR 52  ? A THR 52  
23  1 Y 1 A ALA 53  ? A ALA 53  
24  1 Y 1 A ALA 54  ? A ALA 54  
25  1 Y 1 A ALA 55  ? A ALA 55  
26  1 Y 1 A THR 56  ? A THR 56  
27  1 Y 1 A ASN 57  ? A ASN 57  
28  1 Y 1 A HIS 58  ? A HIS 58  
29  1 Y 1 A THR 59  ? A THR 59  
30  1 Y 1 A THR 60  ? A THR 60  
31  1 Y 1 A ASP 61  ? A ASP 61  
32  1 Y 1 A ASN 62  ? A ASN 62  
33  1 Y 1 A GLY 63  ? A GLY 63  
34  1 Y 1 A VAL 64  ? A VAL 64  
35  1 Y 1 A GLY 65  ? A GLY 65  
36  1 Y 1 A PRO 66  ? A PRO 66  
37  1 Y 1 A GLU 67  ? A GLU 67  
38  1 Y 1 A GLU 68  ? A GLU 68  
39  1 Y 1 A GLU 580 ? A GLU 580 
40  1 Y 1 A ASN 581 ? A ASN 581 
41  1 Y 1 A VAL 582 ? A VAL 582 
42  1 Y 1 A ALA 583 ? A ALA 583 
43  1 Y 1 A THR 584 ? A THR 584 
44  1 Y 1 A THR 585 ? A THR 585 
45  1 Y 1 A ASP 586 ? A ASP 586 
46  1 Y 1 A THR 587 ? A THR 587 
47  1 Y 1 A LEU 588 ? A LEU 588 
48  1 Y 1 A GLU 589 ? A GLU 589 
49  1 Y 1 A SER 590 ? A SER 590 
50  1 Y 1 A THR 591 ? A THR 591 
51  1 Y 1 A THR 592 ? A THR 592 
52  1 Y 1 A VAL 593 ? A VAL 593 
53  1 Y 1 A GLY 594 ? A GLY 594 
54  1 Y 1 A THR 595 ? A THR 595 
55  1 Y 1 A SER 596 ? A SER 596 
56  1 Y 1 A VAL 597 ? A VAL 597 
57  1 Y 1 B MET 1   ? B MET 1   
58  1 Y 1 B ALA 2   ? B ALA 2   
59  1 Y 1 B ALA 3   ? B ALA 3   
60  1 Y 1 B VAL 4   ? B VAL 4   
61  1 Y 1 B GLN 5   ? B GLN 5   
62  1 Y 1 B ALA 6   ? B ALA 6   
63  1 Y 1 B ALA 7   ? B ALA 7   
64  1 Y 1 B GLU 8   ? B GLU 8   
65  1 Y 1 B VAL 9   ? B VAL 9   
66  1 Y 1 B LYS 10  ? B LYS 10  
67  1 Y 1 B VAL 11  ? B VAL 11  
68  1 Y 1 B ASP 12  ? B ASP 12  
69  1 Y 1 B GLY 13  ? B GLY 13  
70  1 Y 1 B SER 14  ? B SER 14  
71  1 Y 1 B GLU 15  ? B GLU 15  
72  1 Y 1 B PRO 16  ? B PRO 16  
73  1 Y 1 B LYS 17  ? B LYS 17  
74  1 Y 1 B LEU 18  ? B LEU 18  
75  1 Y 1 B SER 19  ? B SER 19  
76  1 Y 1 B LYS 20  ? B LYS 20  
77  1 Y 1 B ASN 21  ? B ASN 21  
78  1 Y 1 B GLU 22  ? B GLU 22  
79  1 Y 1 B LEU 23  ? B LEU 23  
80  1 Y 1 B LYS 24  ? B LYS 24  
81  1 Y 1 B ARG 25  ? B ARG 25  
82  1 Y 1 B ARG 26  ? B ARG 26  
83  1 Y 1 B LEU 27  ? B LEU 27  
84  1 Y 1 B LYS 28  ? B LYS 28  
85  1 Y 1 B ALA 29  ? B ALA 29  
86  1 Y 1 B GLU 30  ? B GLU 30  
87  1 Y 1 B LYS 31  ? B LYS 31  
88  1 Y 1 B LYS 32  ? B LYS 32  
89  1 Y 1 B VAL 33  ? B VAL 33  
90  1 Y 1 B ALA 34  ? B ALA 34  
91  1 Y 1 B GLU 35  ? B GLU 35  
92  1 Y 1 B LYS 36  ? B LYS 36  
93  1 Y 1 B GLU 37  ? B GLU 37  
94  1 Y 1 B ALA 38  ? B ALA 38  
95  1 Y 1 B LYS 39  ? B LYS 39  
96  1 Y 1 B GLN 40  ? B GLN 40  
97  1 Y 1 B LYS 41  ? B LYS 41  
98  1 Y 1 B GLU 42  ? B GLU 42  
99  1 Y 1 B LEU 43  ? B LEU 43  
100 1 Y 1 B SER 44  ? B SER 44  
101 1 Y 1 B GLU 45  ? B GLU 45  
102 1 Y 1 B LYS 46  ? B LYS 46  
103 1 Y 1 B GLN 47  ? B GLN 47  
104 1 Y 1 B LEU 48  ? B LEU 48  
105 1 Y 1 B SER 49  ? B SER 49  
106 1 Y 1 B GLN 50  ? B GLN 50  
107 1 Y 1 B ALA 51  ? B ALA 51  
108 1 Y 1 B THR 52  ? B THR 52  
109 1 Y 1 B ALA 53  ? B ALA 53  
110 1 Y 1 B ALA 54  ? B ALA 54  
111 1 Y 1 B ALA 55  ? B ALA 55  
112 1 Y 1 B THR 56  ? B THR 56  
113 1 Y 1 B ASN 57  ? B ASN 57  
114 1 Y 1 B HIS 58  ? B HIS 58  
115 1 Y 1 B THR 59  ? B THR 59  
116 1 Y 1 B THR 60  ? B THR 60  
117 1 Y 1 B ASP 61  ? B ASP 61  
118 1 Y 1 B ASN 62  ? B ASN 62  
119 1 Y 1 B GLY 63  ? B GLY 63  
120 1 Y 1 B VAL 64  ? B VAL 64  
121 1 Y 1 B GLY 65  ? B GLY 65  
122 1 Y 1 B PRO 66  ? B PRO 66  
123 1 Y 1 B GLU 67  ? B GLU 67  
124 1 Y 1 B GLU 68  ? B GLU 68  
125 1 Y 1 B GLU 69  ? B GLU 69  
126 1 Y 1 B SER 70  ? B SER 70  
127 1 Y 1 B LYS 578 ? B LYS 578 
128 1 Y 1 B LYS 579 ? B LYS 579 
129 1 Y 1 B GLU 580 ? B GLU 580 
130 1 Y 1 B ASN 581 ? B ASN 581 
131 1 Y 1 B VAL 582 ? B VAL 582 
132 1 Y 1 B ALA 583 ? B ALA 583 
133 1 Y 1 B THR 584 ? B THR 584 
134 1 Y 1 B THR 585 ? B THR 585 
135 1 Y 1 B ASP 586 ? B ASP 586 
136 1 Y 1 B THR 587 ? B THR 587 
137 1 Y 1 B LEU 588 ? B LEU 588 
138 1 Y 1 B GLU 589 ? B GLU 589 
139 1 Y 1 B SER 590 ? B SER 590 
140 1 Y 1 B THR 591 ? B THR 591 
141 1 Y 1 B THR 592 ? B THR 592 
142 1 Y 1 B VAL 593 ? B VAL 593 
143 1 Y 1 B GLY 594 ? B GLY 594 
144 1 Y 1 B THR 595 ? B THR 595 
145 1 Y 1 B SER 596 ? B SER 596 
146 1 Y 1 B VAL 597 ? B VAL 597 
147 1 Y 1 D THR 22  ? D THR 22  
148 1 Y 1 D CYS 23  ? D CYS 23  
149 1 Y 1 D MET 24  ? D MET 24  
150 1 Y 1 D TYR 25  ? D TYR 25  
151 1 Y 1 D ARG 26  ? D ARG 26  
152 1 Y 1 D LEU 27  ? D LEU 27  
153 1 Y 1 D PRO 28  ? D PRO 28  
154 1 Y 1 D ASN 29  ? D ASN 29  
155 1 Y 1 D VAL 30  ? D VAL 30  
156 1 Y 1 D HIS 31  ? D HIS 31  
157 1 Y 1 D GLY 32  ? D GLY 32  
158 1 Y 1 D ARG 33  ? D ARG 33  
159 1 Y 1 D SER 34  ? D SER 34  
160 1 Y 1 D TYR 35  ? D TYR 35  
161 1 Y 1 D GLY 36  ? D GLY 36  
162 1 Y 1 E THR 22  ? E THR 22  
163 1 Y 1 E CYS 23  ? E CYS 23  
164 1 Y 1 E MET 24  ? E MET 24  
165 1 Y 1 E TYR 25  ? E TYR 25  
166 1 Y 1 E ARG 26  ? E ARG 26  
167 1 Y 1 E LEU 27  ? E LEU 27  
168 1 Y 1 E PRO 28  ? E PRO 28  
169 1 Y 1 E ASN 29  ? E ASN 29  
170 1 Y 1 E VAL 30  ? E VAL 30  
171 1 Y 1 E HIS 31  ? E HIS 31  
172 1 Y 1 E GLY 32  ? E GLY 32  
173 1 Y 1 E ARG 33  ? E ARG 33  
174 1 Y 1 E SER 34  ? E SER 34  
175 1 Y 1 E TYR 35  ? E TYR 35  
176 1 Y 1 E GLY 36  ? E GLY 36  
# 
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 
12A OP3    O  N N 1   
12A P      P  N N 2   
12A OP1    O  N N 3   
12A OP2    O  N N 4   
12A "O5'"  O  N N 5   
12A "C5'"  C  N N 6   
12A "C4'"  C  N R 7   
12A "O4'"  O  N N 8   
12A "C3'"  C  N S 9   
12A "O3'"  O  N N 10  
12A "C2'"  C  N R 11  
12A "O2'"  O  N N 12  
12A "C1'"  C  N R 13  
12A N9     N  Y N 14  
12A C8     C  Y N 15  
12A N7     N  Y N 16  
12A C5     C  Y N 17  
12A C6     C  Y N 18  
12A N6     N  N N 19  
12A N1     N  Y N 20  
12A C2     C  Y N 21  
12A N3     N  Y N 22  
12A C4     C  Y N 23  
12A S2     S  N N 24  
12A C2M    C  N N 25  
12A CC     C  N N 26  
12A OO     O  N N 27  
12A N      N  N N 28  
12A CA     C  N S 29  
12A C      C  N N 30  
12A O      O  N N 31  
12A OXT    O  N N 32  
12A CB     C  N R 33  
12A OG1    O  N N 34  
12A CG2    C  N N 35  
12A HOP3   H  N N 36  
12A HOP2   H  N N 37  
12A "H5'"  H  N N 38  
12A "H5''" H  N N 39  
12A "H4'"  H  N N 40  
12A "H3'"  H  N N 41  
12A "HO3'" H  N N 42  
12A "H2'"  H  N N 43  
12A "HO2'" H  N N 44  
12A "H1'"  H  N N 45  
12A H8     H  N N 46  
12A HN6    H  N N 47  
12A H2M1   H  N N 48  
12A H2M2   H  N N 49  
12A H2M3   H  N N 50  
12A H      H  N N 51  
12A HA     H  N N 52  
12A HXT    H  N N 53  
12A HB     H  N N 54  
12A HG1    H  N N 55  
12A HG21   H  N N 56  
12A HG22   H  N N 57  
12A HG23   H  N N 58  
1MA P      P  N N 59  
1MA OP1    O  N N 60  
1MA OP2    O  N N 61  
1MA OP3    O  N N 62  
1MA "O5'"  O  N N 63  
1MA "C5'"  C  N N 64  
1MA "C4'"  C  N R 65  
1MA "O4'"  O  N N 66  
1MA "C3'"  C  N S 67  
1MA "O3'"  O  N N 68  
1MA "C2'"  C  N R 69  
1MA "O2'"  O  N N 70  
1MA "C1'"  C  N R 71  
1MA N9     N  Y N 72  
1MA C8     C  Y N 73  
1MA N7     N  Y N 74  
1MA C5     C  Y N 75  
1MA C6     C  N N 76  
1MA N6     N  N N 77  
1MA N1     N  N N 78  
1MA CM1    C  N N 79  
1MA C2     C  N N 80  
1MA N3     N  N N 81  
1MA C4     C  Y N 82  
1MA HOP2   H  N N 83  
1MA HOP3   H  N N 84  
1MA "H5'"  H  N N 85  
1MA "H5''" H  N N 86  
1MA "H4'"  H  N N 87  
1MA "H3'"  H  N N 88  
1MA "HO3'" H  N N 89  
1MA "H2'"  H  N N 90  
1MA "HO2'" H  N N 91  
1MA "H1'"  H  N N 92  
1MA H8     H  N N 93  
1MA HN61   H  N N 94  
1MA HM11   H  N N 95  
1MA HM12   H  N N 96  
1MA HM13   H  N N 97  
1MA H2     H  N N 98  
2MG P      P  N N 99  
2MG OP1    O  N N 100 
2MG OP2    O  N N 101 
2MG OP3    O  N N 102 
2MG "O5'"  O  N N 103 
2MG "C5'"  C  N N 104 
2MG "C4'"  C  N R 105 
2MG "O4'"  O  N N 106 
2MG "C3'"  C  N S 107 
2MG "O3'"  O  N N 108 
2MG "C2'"  C  N R 109 
2MG "O2'"  O  N N 110 
2MG "C1'"  C  N R 111 
2MG N9     N  Y N 112 
2MG C8     C  Y N 113 
2MG N7     N  Y N 114 
2MG C5     C  Y N 115 
2MG C6     C  N N 116 
2MG O6     O  N N 117 
2MG N1     N  N N 118 
2MG C2     C  N N 119 
2MG N2     N  N N 120 
2MG CM2    C  N N 121 
2MG N3     N  N N 122 
2MG C4     C  Y N 123 
2MG HOP2   H  N N 124 
2MG HOP3   H  N N 125 
2MG "H5'"  H  N N 126 
2MG "H5''" H  N N 127 
2MG "H4'"  H  N N 128 
2MG "H3'"  H  N N 129 
2MG "HO3'" H  N N 130 
2MG "H2'"  H  N N 131 
2MG "HO2'" H  N N 132 
2MG "H1'"  H  N N 133 
2MG H8     H  N N 134 
2MG HN1    H  N N 135 
2MG HN2    H  N N 136 
2MG HM21   H  N N 137 
2MG HM22   H  N N 138 
2MG HM23   H  N N 139 
2MU N1     N  N N 140 
2MU C2     C  N N 141 
2MU N3     N  N N 142 
2MU C4     C  N N 143 
2MU C5     C  N N 144 
2MU C5M    C  N N 145 
2MU C6     C  N N 146 
2MU O2     O  N N 147 
2MU O4     O  N N 148 
2MU "C1'"  C  N R 149 
2MU "C2'"  C  N R 150 
2MU "O2'"  O  N N 151 
2MU "C3'"  C  N R 152 
2MU "C4'"  C  N R 153 
2MU "O3'"  O  N N 154 
2MU "O4'"  O  N N 155 
2MU "C5'"  C  N N 156 
2MU "O5'"  O  N N 157 
2MU "C6'"  C  N N 158 
2MU P      P  N N 159 
2MU OP1    O  N N 160 
2MU OP2    O  N N 161 
2MU OP3    O  N N 162 
2MU HN3    H  N N 163 
2MU HM51   H  N N 164 
2MU HM52   H  N N 165 
2MU HM53   H  N N 166 
2MU H6     H  N N 167 
2MU "H1'"  H  N N 168 
2MU "H2'"  H  N N 169 
2MU "H3'"  H  N N 170 
2MU "H4'"  H  N N 171 
2MU "HO3'" H  N N 172 
2MU "H5'"  H  N N 173 
2MU "H5''" H  N N 174 
2MU "H6'1" H  N N 175 
2MU "H6'2" H  N N 176 
2MU "H6'3" H  N N 177 
2MU HOP2   H  N N 178 
2MU HOP3   H  N N 179 
5MC P      P  N N 180 
5MC OP1    O  N N 181 
5MC OP2    O  N N 182 
5MC OP3    O  N N 183 
5MC "O5'"  O  N N 184 
5MC "C5'"  C  N N 185 
5MC "C4'"  C  N R 186 
5MC "O4'"  O  N N 187 
5MC "C3'"  C  N S 188 
5MC "O3'"  O  N N 189 
5MC "C2'"  C  N R 190 
5MC "O2'"  O  N N 191 
5MC "C1'"  C  N R 192 
5MC N1     N  N N 193 
5MC C2     C  N N 194 
5MC O2     O  N N 195 
5MC N3     N  N N 196 
5MC C4     C  N N 197 
5MC N4     N  N N 198 
5MC C5     C  N N 199 
5MC C6     C  N N 200 
5MC CM5    C  N N 201 
5MC HOP2   H  N N 202 
5MC HOP3   H  N N 203 
5MC "H5'"  H  N N 204 
5MC "H5''" H  N N 205 
5MC "H4'"  H  N N 206 
5MC "H3'"  H  N N 207 
5MC "HO3'" H  N N 208 
5MC "H2'"  H  N N 209 
5MC "HO2'" H  N N 210 
5MC "H1'"  H  N N 211 
5MC HN41   H  N N 212 
5MC HN42   H  N N 213 
5MC H6     H  N N 214 
5MC HM51   H  N N 215 
5MC HM52   H  N N 216 
5MC HM53   H  N N 217 
70U N1     N  N N 218 
70U C2     C  N N 219 
70U S2     S  N N 220 
70U N3     N  N N 221 
70U C4     C  N N 222 
70U O4     O  N N 223 
70U C5     C  N N 224 
70U C6     C  N N 225 
70U C5M    C  N N 226 
70U C8     C  N N 227 
70U O8     O  N N 228 
70U O9     O  N N 229 
70U C9     C  N N 230 
70U "C1'"  C  N R 231 
70U "O2'"  O  N N 232 
70U "C2'"  C  N R 233 
70U "O3'"  O  N N 234 
70U "C3'"  C  N S 235 
70U "C4'"  C  N R 236 
70U "O4'"  O  N N 237 
70U "C5'"  C  N N 238 
70U "O5'"  O  N N 239 
70U P      P  N N 240 
70U OP1    O  N N 241 
70U OP2    O  N N 242 
70U OP3    O  N N 243 
70U HN3    H  N N 244 
70U H6     H  N N 245 
70U H71    H  N N 246 
70U H72    H  N N 247 
70U H91    H  N N 248 
70U H92    H  N N 249 
70U H93    H  N N 250 
70U "H1'"  H  N N 251 
70U "HO2'" H  N N 252 
70U "H2'"  H  N N 253 
70U "HO3'" H  N N 254 
70U "H3'"  H  N N 255 
70U "H4'"  H  N N 256 
70U "H5'"  H  N N 257 
70U "H5''" H  N N 258 
70U HOP2   H  N N 259 
70U HOP3   H  N N 260 
7MG P      P  N N 261 
7MG OP1    O  N N 262 
7MG OP2    O  N N 263 
7MG OP3    O  N N 264 
7MG "O5'"  O  N N 265 
7MG "C5'"  C  N N 266 
7MG "C4'"  C  N R 267 
7MG "O4'"  O  N N 268 
7MG "C3'"  C  N S 269 
7MG "O3'"  O  N N 270 
7MG "C2'"  C  N R 271 
7MG "O2'"  O  N N 272 
7MG "C1'"  C  N R 273 
7MG N9     N  N N 274 
7MG C8     C  N N 275 
7MG N7     N  N N 276 
7MG C5     C  N N 277 
7MG C6     C  N N 278 
7MG O6     O  N N 279 
7MG N1     N  N N 280 
7MG C2     C  N N 281 
7MG N2     N  N N 282 
7MG N3     N  N N 283 
7MG C4     C  N N 284 
7MG CM7    C  N N 285 
7MG HOP2   H  N N 286 
7MG HOP3   H  N N 287 
7MG "H5'"  H  N N 288 
7MG "H5''" H  N N 289 
7MG "H4'"  H  N N 290 
7MG "H3'"  H  N N 291 
7MG "HO3'" H  N N 292 
7MG "H2'"  H  N N 293 
7MG "HO2'" H  N N 294 
7MG "H1'"  H  N N 295 
7MG H81    H  N N 296 
7MG H82    H  N N 297 
7MG HN1    H  N N 298 
7MG HN21   H  N N 299 
7MG HN22   H  N N 300 
7MG HM71   H  N N 301 
7MG HM72   H  N N 302 
7MG HM73   H  N N 303 
A   OP3    O  N N 304 
A   P      P  N N 305 
A   OP1    O  N N 306 
A   OP2    O  N N 307 
A   "O5'"  O  N N 308 
A   "C5'"  C  N N 309 
A   "C4'"  C  N R 310 
A   "O4'"  O  N N 311 
A   "C3'"  C  N S 312 
A   "O3'"  O  N N 313 
A   "C2'"  C  N R 314 
A   "O2'"  O  N N 315 
A   "C1'"  C  N R 316 
A   N9     N  Y N 317 
A   C8     C  Y N 318 
A   N7     N  Y N 319 
A   C5     C  Y N 320 
A   C6     C  Y N 321 
A   N6     N  N N 322 
A   N1     N  Y N 323 
A   C2     C  Y N 324 
A   N3     N  Y N 325 
A   C4     C  Y N 326 
A   HOP3   H  N N 327 
A   HOP2   H  N N 328 
A   "H5'"  H  N N 329 
A   "H5''" H  N N 330 
A   "H4'"  H  N N 331 
A   "H3'"  H  N N 332 
A   "HO3'" H  N N 333 
A   "H2'"  H  N N 334 
A   "HO2'" H  N N 335 
A   "H1'"  H  N N 336 
A   H8     H  N N 337 
A   H61    H  N N 338 
A   H62    H  N N 339 
A   H2     H  N N 340 
ALA N      N  N N 341 
ALA CA     C  N S 342 
ALA C      C  N N 343 
ALA O      O  N N 344 
ALA CB     C  N N 345 
ALA OXT    O  N N 346 
ALA H      H  N N 347 
ALA H2     H  N N 348 
ALA HA     H  N N 349 
ALA HB1    H  N N 350 
ALA HB2    H  N N 351 
ALA HB3    H  N N 352 
ALA HXT    H  N N 353 
AMP P      P  N N 354 
AMP O1P    O  N N 355 
AMP O2P    O  N N 356 
AMP O3P    O  N N 357 
AMP "O5'"  O  N N 358 
AMP "C5'"  C  N N 359 
AMP "C4'"  C  N R 360 
AMP "O4'"  O  N N 361 
AMP "C3'"  C  N S 362 
AMP "O3'"  O  N N 363 
AMP "C2'"  C  N R 364 
AMP "O2'"  O  N N 365 
AMP "C1'"  C  N R 366 
AMP N9     N  Y N 367 
AMP C8     C  Y N 368 
AMP N7     N  Y N 369 
AMP C5     C  Y N 370 
AMP C6     C  Y N 371 
AMP N6     N  N N 372 
AMP N1     N  Y N 373 
AMP C2     C  Y N 374 
AMP N3     N  Y N 375 
AMP C4     C  Y N 376 
AMP HOP2   H  N N 377 
AMP HOP3   H  N N 378 
AMP "H5'1" H  N N 379 
AMP "H5'2" H  N N 380 
AMP "H4'"  H  N N 381 
AMP "H3'"  H  N N 382 
AMP "HO3'" H  N N 383 
AMP "H2'"  H  N N 384 
AMP "HO2'" H  N N 385 
AMP "H1'"  H  N N 386 
AMP H8     H  N N 387 
AMP HN61   H  N N 388 
AMP HN62   H  N N 389 
AMP H2     H  N N 390 
ARG N      N  N N 391 
ARG CA     C  N S 392 
ARG C      C  N N 393 
ARG O      O  N N 394 
ARG CB     C  N N 395 
ARG CG     C  N N 396 
ARG CD     C  N N 397 
ARG NE     N  N N 398 
ARG CZ     C  N N 399 
ARG NH1    N  N N 400 
ARG NH2    N  N N 401 
ARG OXT    O  N N 402 
ARG H      H  N N 403 
ARG H2     H  N N 404 
ARG HA     H  N N 405 
ARG HB2    H  N N 406 
ARG HB3    H  N N 407 
ARG HG2    H  N N 408 
ARG HG3    H  N N 409 
ARG HD2    H  N N 410 
ARG HD3    H  N N 411 
ARG HE     H  N N 412 
ARG HH11   H  N N 413 
ARG HH12   H  N N 414 
ARG HH21   H  N N 415 
ARG HH22   H  N N 416 
ARG HXT    H  N N 417 
ASN N      N  N N 418 
ASN CA     C  N S 419 
ASN C      C  N N 420 
ASN O      O  N N 421 
ASN CB     C  N N 422 
ASN CG     C  N N 423 
ASN OD1    O  N N 424 
ASN ND2    N  N N 425 
ASN OXT    O  N N 426 
ASN H      H  N N 427 
ASN H2     H  N N 428 
ASN HA     H  N N 429 
ASN HB2    H  N N 430 
ASN HB3    H  N N 431 
ASN HD21   H  N N 432 
ASN HD22   H  N N 433 
ASN HXT    H  N N 434 
ASP N      N  N N 435 
ASP CA     C  N S 436 
ASP C      C  N N 437 
ASP O      O  N N 438 
ASP CB     C  N N 439 
ASP CG     C  N N 440 
ASP OD1    O  N N 441 
ASP OD2    O  N N 442 
ASP OXT    O  N N 443 
ASP H      H  N N 444 
ASP H2     H  N N 445 
ASP HA     H  N N 446 
ASP HB2    H  N N 447 
ASP HB3    H  N N 448 
ASP HD2    H  N N 449 
ASP HXT    H  N N 450 
C   OP3    O  N N 451 
C   P      P  N N 452 
C   OP1    O  N N 453 
C   OP2    O  N N 454 
C   "O5'"  O  N N 455 
C   "C5'"  C  N N 456 
C   "C4'"  C  N R 457 
C   "O4'"  O  N N 458 
C   "C3'"  C  N S 459 
C   "O3'"  O  N N 460 
C   "C2'"  C  N R 461 
C   "O2'"  O  N N 462 
C   "C1'"  C  N R 463 
C   N1     N  N N 464 
C   C2     C  N N 465 
C   O2     O  N N 466 
C   N3     N  N N 467 
C   C4     C  N N 468 
C   N4     N  N N 469 
C   C5     C  N N 470 
C   C6     C  N N 471 
C   HOP3   H  N N 472 
C   HOP2   H  N N 473 
C   "H5'"  H  N N 474 
C   "H5''" H  N N 475 
C   "H4'"  H  N N 476 
C   "H3'"  H  N N 477 
C   "HO3'" H  N N 478 
C   "H2'"  H  N N 479 
C   "HO2'" H  N N 480 
C   "H1'"  H  N N 481 
C   H41    H  N N 482 
C   H42    H  N N 483 
C   H5     H  N N 484 
C   H6     H  N N 485 
CYS N      N  N N 486 
CYS CA     C  N R 487 
CYS C      C  N N 488 
CYS O      O  N N 489 
CYS CB     C  N N 490 
CYS SG     S  N N 491 
CYS OXT    O  N N 492 
CYS H      H  N N 493 
CYS H2     H  N N 494 
CYS HA     H  N N 495 
CYS HB2    H  N N 496 
CYS HB3    H  N N 497 
CYS HG     H  N N 498 
CYS HXT    H  N N 499 
G   OP3    O  N N 500 
G   P      P  N N 501 
G   OP1    O  N N 502 
G   OP2    O  N N 503 
G   "O5'"  O  N N 504 
G   "C5'"  C  N N 505 
G   "C4'"  C  N R 506 
G   "O4'"  O  N N 507 
G   "C3'"  C  N S 508 
G   "O3'"  O  N N 509 
G   "C2'"  C  N R 510 
G   "O2'"  O  N N 511 
G   "C1'"  C  N R 512 
G   N9     N  Y N 513 
G   C8     C  Y N 514 
G   N7     N  Y N 515 
G   C5     C  Y N 516 
G   C6     C  N N 517 
G   O6     O  N N 518 
G   N1     N  N N 519 
G   C2     C  N N 520 
G   N2     N  N N 521 
G   N3     N  N N 522 
G   C4     C  Y N 523 
G   HOP3   H  N N 524 
G   HOP2   H  N N 525 
G   "H5'"  H  N N 526 
G   "H5''" H  N N 527 
G   "H4'"  H  N N 528 
G   "H3'"  H  N N 529 
G   "HO3'" H  N N 530 
G   "H2'"  H  N N 531 
G   "HO2'" H  N N 532 
G   "H1'"  H  N N 533 
G   H8     H  N N 534 
G   H1     H  N N 535 
G   H21    H  N N 536 
G   H22    H  N N 537 
GLN N      N  N N 538 
GLN CA     C  N S 539 
GLN C      C  N N 540 
GLN O      O  N N 541 
GLN CB     C  N N 542 
GLN CG     C  N N 543 
GLN CD     C  N N 544 
GLN OE1    O  N N 545 
GLN NE2    N  N N 546 
GLN OXT    O  N N 547 
GLN H      H  N N 548 
GLN H2     H  N N 549 
GLN HA     H  N N 550 
GLN HB2    H  N N 551 
GLN HB3    H  N N 552 
GLN HG2    H  N N 553 
GLN HG3    H  N N 554 
GLN HE21   H  N N 555 
GLN HE22   H  N N 556 
GLN HXT    H  N N 557 
GLU N      N  N N 558 
GLU CA     C  N S 559 
GLU C      C  N N 560 
GLU O      O  N N 561 
GLU CB     C  N N 562 
GLU CG     C  N N 563 
GLU CD     C  N N 564 
GLU OE1    O  N N 565 
GLU OE2    O  N N 566 
GLU OXT    O  N N 567 
GLU H      H  N N 568 
GLU H2     H  N N 569 
GLU HA     H  N N 570 
GLU HB2    H  N N 571 
GLU HB3    H  N N 572 
GLU HG2    H  N N 573 
GLU HG3    H  N N 574 
GLU HE2    H  N N 575 
GLU HXT    H  N N 576 
GLY N      N  N N 577 
GLY CA     C  N N 578 
GLY C      C  N N 579 
GLY O      O  N N 580 
GLY OXT    O  N N 581 
GLY H      H  N N 582 
GLY H2     H  N N 583 
GLY HA2    H  N N 584 
GLY HA3    H  N N 585 
GLY HXT    H  N N 586 
H2U P      P  N N 587 
H2U OP1    O  N N 588 
H2U OP2    O  N N 589 
H2U OP3    O  N N 590 
H2U "O5'"  O  N N 591 
H2U "C5'"  C  N N 592 
H2U "C4'"  C  N R 593 
H2U "O4'"  O  N N 594 
H2U "C3'"  C  N S 595 
H2U "O3'"  O  N N 596 
H2U "C1'"  C  N R 597 
H2U "C2'"  C  N R 598 
H2U "O2'"  O  N N 599 
H2U N1     N  N N 600 
H2U C2     C  N N 601 
H2U O2     O  N N 602 
H2U N3     N  N N 603 
H2U C4     C  N N 604 
H2U O4     O  N N 605 
H2U C5     C  N N 606 
H2U C6     C  N N 607 
H2U HOP2   H  N N 608 
H2U HOP3   H  N N 609 
H2U "H5'"  H  N N 610 
H2U "H5''" H  N N 611 
H2U "H4'"  H  N N 612 
H2U "H3'"  H  N N 613 
H2U "HO3'" H  N N 614 
H2U "H1'"  H  N N 615 
H2U "H2'"  H  N N 616 
H2U "HO2'" H  N N 617 
H2U HN3    H  N N 618 
H2U H51    H  N N 619 
H2U H52    H  N N 620 
H2U H61    H  N N 621 
H2U H62    H  N N 622 
HIS N      N  N N 623 
HIS CA     C  N S 624 
HIS C      C  N N 625 
HIS O      O  N N 626 
HIS CB     C  N N 627 
HIS CG     C  Y N 628 
HIS ND1    N  Y N 629 
HIS CD2    C  Y N 630 
HIS CE1    C  Y N 631 
HIS NE2    N  Y N 632 
HIS OXT    O  N N 633 
HIS H      H  N N 634 
HIS H2     H  N N 635 
HIS HA     H  N N 636 
HIS HB2    H  N N 637 
HIS HB3    H  N N 638 
HIS HD1    H  N N 639 
HIS HD2    H  N N 640 
HIS HE1    H  N N 641 
HIS HE2    H  N N 642 
HIS HXT    H  N N 643 
ILE N      N  N N 644 
ILE CA     C  N S 645 
ILE C      C  N N 646 
ILE O      O  N N 647 
ILE CB     C  N S 648 
ILE CG1    C  N N 649 
ILE CG2    C  N N 650 
ILE CD1    C  N N 651 
ILE OXT    O  N N 652 
ILE H      H  N N 653 
ILE H2     H  N N 654 
ILE HA     H  N N 655 
ILE HB     H  N N 656 
ILE HG12   H  N N 657 
ILE HG13   H  N N 658 
ILE HG21   H  N N 659 
ILE HG22   H  N N 660 
ILE HG23   H  N N 661 
ILE HD11   H  N N 662 
ILE HD12   H  N N 663 
ILE HD13   H  N N 664 
ILE HXT    H  N N 665 
LEU N      N  N N 666 
LEU CA     C  N S 667 
LEU C      C  N N 668 
LEU O      O  N N 669 
LEU CB     C  N N 670 
LEU CG     C  N N 671 
LEU CD1    C  N N 672 
LEU CD2    C  N N 673 
LEU OXT    O  N N 674 
LEU H      H  N N 675 
LEU H2     H  N N 676 
LEU HA     H  N N 677 
LEU HB2    H  N N 678 
LEU HB3    H  N N 679 
LEU HG     H  N N 680 
LEU HD11   H  N N 681 
LEU HD12   H  N N 682 
LEU HD13   H  N N 683 
LEU HD21   H  N N 684 
LEU HD22   H  N N 685 
LEU HD23   H  N N 686 
LEU HXT    H  N N 687 
LYS N      N  N N 688 
LYS CA     C  N S 689 
LYS C      C  N N 690 
LYS O      O  N N 691 
LYS CB     C  N N 692 
LYS CG     C  N N 693 
LYS CD     C  N N 694 
LYS CE     C  N N 695 
LYS NZ     N  N N 696 
LYS OXT    O  N N 697 
LYS H      H  N N 698 
LYS H2     H  N N 699 
LYS HA     H  N N 700 
LYS HB2    H  N N 701 
LYS HB3    H  N N 702 
LYS HG2    H  N N 703 
LYS HG3    H  N N 704 
LYS HD2    H  N N 705 
LYS HD3    H  N N 706 
LYS HE2    H  N N 707 
LYS HE3    H  N N 708 
LYS HZ1    H  N N 709 
LYS HZ2    H  N N 710 
LYS HZ3    H  N N 711 
LYS HXT    H  N N 712 
MET N      N  N N 713 
MET CA     C  N S 714 
MET C      C  N N 715 
MET O      O  N N 716 
MET CB     C  N N 717 
MET CG     C  N N 718 
MET SD     S  N N 719 
MET CE     C  N N 720 
MET OXT    O  N N 721 
MET H      H  N N 722 
MET H2     H  N N 723 
MET HA     H  N N 724 
MET HB2    H  N N 725 
MET HB3    H  N N 726 
MET HG2    H  N N 727 
MET HG3    H  N N 728 
MET HE1    H  N N 729 
MET HE2    H  N N 730 
MET HE3    H  N N 731 
MET HXT    H  N N 732 
MG  MG     MG N N 733 
NA  NA     NA N N 734 
PHE N      N  N N 735 
PHE CA     C  N S 736 
PHE C      C  N N 737 
PHE O      O  N N 738 
PHE CB     C  N N 739 
PHE CG     C  Y N 740 
PHE CD1    C  Y N 741 
PHE CD2    C  Y N 742 
PHE CE1    C  Y N 743 
PHE CE2    C  Y N 744 
PHE CZ     C  Y N 745 
PHE OXT    O  N N 746 
PHE H      H  N N 747 
PHE H2     H  N N 748 
PHE HA     H  N N 749 
PHE HB2    H  N N 750 
PHE HB3    H  N N 751 
PHE HD1    H  N N 752 
PHE HD2    H  N N 753 
PHE HE1    H  N N 754 
PHE HE2    H  N N 755 
PHE HZ     H  N N 756 
PHE HXT    H  N N 757 
PRO N      N  N N 758 
PRO CA     C  N S 759 
PRO C      C  N N 760 
PRO O      O  N N 761 
PRO CB     C  N N 762 
PRO CG     C  N N 763 
PRO CD     C  N N 764 
PRO OXT    O  N N 765 
PRO H      H  N N 766 
PRO HA     H  N N 767 
PRO HB2    H  N N 768 
PRO HB3    H  N N 769 
PRO HG2    H  N N 770 
PRO HG3    H  N N 771 
PRO HD2    H  N N 772 
PRO HD3    H  N N 773 
PRO HXT    H  N N 774 
PSU N1     N  N N 775 
PSU C2     C  N N 776 
PSU N3     N  N N 777 
PSU C4     C  N N 778 
PSU C5     C  N N 779 
PSU C6     C  N N 780 
PSU O2     O  N N 781 
PSU O4     O  N N 782 
PSU "C1'"  C  N S 783 
PSU "C2'"  C  N R 784 
PSU "O2'"  O  N N 785 
PSU "C3'"  C  N S 786 
PSU "C4'"  C  N R 787 
PSU "O3'"  O  N N 788 
PSU "O4'"  O  N N 789 
PSU "C5'"  C  N N 790 
PSU "O5'"  O  N N 791 
PSU P      P  N N 792 
PSU OP1    O  N N 793 
PSU OP2    O  N N 794 
PSU OP3    O  N N 795 
PSU HN1    H  N N 796 
PSU HN3    H  N N 797 
PSU H6     H  N N 798 
PSU "H1'"  H  N N 799 
PSU "H2'"  H  N N 800 
PSU "HO2'" H  N N 801 
PSU "H3'"  H  N N 802 
PSU "H4'"  H  N N 803 
PSU "HO3'" H  N N 804 
PSU "H5'"  H  N N 805 
PSU "H5''" H  N N 806 
PSU HOP2   H  N N 807 
PSU HOP3   H  N N 808 
SER N      N  N N 809 
SER CA     C  N S 810 
SER C      C  N N 811 
SER O      O  N N 812 
SER CB     C  N N 813 
SER OG     O  N N 814 
SER OXT    O  N N 815 
SER H      H  N N 816 
SER H2     H  N N 817 
SER HA     H  N N 818 
SER HB2    H  N N 819 
SER HB3    H  N N 820 
SER HG     H  N N 821 
SER HXT    H  N N 822 
THR N      N  N N 823 
THR CA     C  N S 824 
THR C      C  N N 825 
THR O      O  N N 826 
THR CB     C  N R 827 
THR OG1    O  N N 828 
THR CG2    C  N N 829 
THR OXT    O  N N 830 
THR H      H  N N 831 
THR H2     H  N N 832 
THR HA     H  N N 833 
THR HB     H  N N 834 
THR HG1    H  N N 835 
THR HG21   H  N N 836 
THR HG22   H  N N 837 
THR HG23   H  N N 838 
THR HXT    H  N N 839 
TRP N      N  N N 840 
TRP CA     C  N S 841 
TRP C      C  N N 842 
TRP O      O  N N 843 
TRP CB     C  N N 844 
TRP CG     C  Y N 845 
TRP CD1    C  Y N 846 
TRP CD2    C  Y N 847 
TRP NE1    N  Y N 848 
TRP CE2    C  Y N 849 
TRP CE3    C  Y N 850 
TRP CZ2    C  Y N 851 
TRP CZ3    C  Y N 852 
TRP CH2    C  Y N 853 
TRP OXT    O  N N 854 
TRP H      H  N N 855 
TRP H2     H  N N 856 
TRP HA     H  N N 857 
TRP HB2    H  N N 858 
TRP HB3    H  N N 859 
TRP HD1    H  N N 860 
TRP HE1    H  N N 861 
TRP HE3    H  N N 862 
TRP HZ2    H  N N 863 
TRP HZ3    H  N N 864 
TRP HH2    H  N N 865 
TRP HXT    H  N N 866 
TYR N      N  N N 867 
TYR CA     C  N S 868 
TYR C      C  N N 869 
TYR O      O  N N 870 
TYR CB     C  N N 871 
TYR CG     C  Y N 872 
TYR CD1    C  Y N 873 
TYR CD2    C  Y N 874 
TYR CE1    C  Y N 875 
TYR CE2    C  Y N 876 
TYR CZ     C  Y N 877 
TYR OH     O  N N 878 
TYR OXT    O  N N 879 
TYR H      H  N N 880 
TYR H2     H  N N 881 
TYR HA     H  N N 882 
TYR HB2    H  N N 883 
TYR HB3    H  N N 884 
TYR HD1    H  N N 885 
TYR HD2    H  N N 886 
TYR HE1    H  N N 887 
TYR HE2    H  N N 888 
TYR HH     H  N N 889 
TYR HXT    H  N N 890 
U   OP3    O  N N 891 
U   P      P  N N 892 
U   OP1    O  N N 893 
U   OP2    O  N N 894 
U   "O5'"  O  N N 895 
U   "C5'"  C  N N 896 
U   "C4'"  C  N R 897 
U   "O4'"  O  N N 898 
U   "C3'"  C  N S 899 
U   "O3'"  O  N N 900 
U   "C2'"  C  N R 901 
U   "O2'"  O  N N 902 
U   "C1'"  C  N R 903 
U   N1     N  N N 904 
U   C2     C  N N 905 
U   O2     O  N N 906 
U   N3     N  N N 907 
U   C4     C  N N 908 
U   O4     O  N N 909 
U   C5     C  N N 910 
U   C6     C  N N 911 
U   HOP3   H  N N 912 
U   HOP2   H  N N 913 
U   "H5'"  H  N N 914 
U   "H5''" H  N N 915 
U   "H4'"  H  N N 916 
U   "H3'"  H  N N 917 
U   "HO3'" H  N N 918 
U   "H2'"  H  N N 919 
U   "HO2'" H  N N 920 
U   "H1'"  H  N N 921 
U   H3     H  N N 922 
U   H5     H  N N 923 
U   H6     H  N N 924 
VAL N      N  N N 925 
VAL CA     C  N S 926 
VAL C      C  N N 927 
VAL O      O  N N 928 
VAL CB     C  N N 929 
VAL CG1    C  N N 930 
VAL CG2    C  N N 931 
VAL OXT    O  N N 932 
VAL H      H  N N 933 
VAL H2     H  N N 934 
VAL HA     H  N N 935 
VAL HB     H  N N 936 
VAL HG11   H  N N 937 
VAL HG12   H  N N 938 
VAL HG13   H  N N 939 
VAL HG21   H  N N 940 
VAL HG22   H  N N 941 
VAL HG23   H  N N 942 
VAL HXT    H  N N 943 
# 
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 
12A OP3   P      sing N N 1   
12A OP3   HOP3   sing N N 2   
12A P     OP1    doub N N 3   
12A P     OP2    sing N N 4   
12A P     "O5'"  sing N N 5   
12A OP2   HOP2   sing N N 6   
12A "O5'" "C5'"  sing N N 7   
12A "C5'" "C4'"  sing N N 8   
12A "C5'" "H5'"  sing N N 9   
12A "C5'" "H5''" sing N N 10  
12A "C4'" "O4'"  sing N N 11  
12A "C4'" "C3'"  sing N N 12  
12A "C4'" "H4'"  sing N N 13  
12A "O4'" "C1'"  sing N N 14  
12A "C3'" "O3'"  sing N N 15  
12A "C3'" "C2'"  sing N N 16  
12A "C3'" "H3'"  sing N N 17  
12A "O3'" "HO3'" sing N N 18  
12A "C2'" "O2'"  sing N N 19  
12A "C2'" "C1'"  sing N N 20  
12A "C2'" "H2'"  sing N N 21  
12A "O2'" "HO2'" sing N N 22  
12A "C1'" N9     sing N N 23  
12A "C1'" "H1'"  sing N N 24  
12A N9    C8     sing Y N 25  
12A N9    C4     sing Y N 26  
12A C8    N7     doub Y N 27  
12A C8    H8     sing N N 28  
12A N7    C5     sing Y N 29  
12A C5    C6     sing Y N 30  
12A C5    C4     doub Y N 31  
12A C6    N6     sing N N 32  
12A C6    N1     doub Y N 33  
12A N6    CC     sing N N 34  
12A N6    HN6    sing N N 35  
12A N1    C2     sing Y N 36  
12A C2    N3     doub Y N 37  
12A C2    S2     sing N N 38  
12A N3    C4     sing Y N 39  
12A S2    C2M    sing N N 40  
12A C2M   H2M1   sing N N 41  
12A C2M   H2M2   sing N N 42  
12A C2M   H2M3   sing N N 43  
12A CC    OO     doub N N 44  
12A CC    N      sing N N 45  
12A N     CA     sing N N 46  
12A N     H      sing N N 47  
12A CA    C      sing N N 48  
12A CA    CB     sing N N 49  
12A CA    HA     sing N N 50  
12A C     O      doub N N 51  
12A C     OXT    sing N N 52  
12A OXT   HXT    sing N N 53  
12A CB    OG1    sing N N 54  
12A CB    CG2    sing N N 55  
12A CB    HB     sing N N 56  
12A OG1   HG1    sing N N 57  
12A CG2   HG21   sing N N 58  
12A CG2   HG22   sing N N 59  
12A CG2   HG23   sing N N 60  
1MA P     OP1    doub N N 61  
1MA P     OP2    sing N N 62  
1MA P     OP3    sing N N 63  
1MA P     "O5'"  sing N N 64  
1MA OP2   HOP2   sing N N 65  
1MA OP3   HOP3   sing N N 66  
1MA "O5'" "C5'"  sing N N 67  
1MA "C5'" "C4'"  sing N N 68  
1MA "C5'" "H5'"  sing N N 69  
1MA "C5'" "H5''" sing N N 70  
1MA "C4'" "O4'"  sing N N 71  
1MA "C4'" "C3'"  sing N N 72  
1MA "C4'" "H4'"  sing N N 73  
1MA "O4'" "C1'"  sing N N 74  
1MA "C3'" "O3'"  sing N N 75  
1MA "C3'" "C2'"  sing N N 76  
1MA "C3'" "H3'"  sing N N 77  
1MA "O3'" "HO3'" sing N N 78  
1MA "C2'" "O2'"  sing N N 79  
1MA "C2'" "C1'"  sing N N 80  
1MA "C2'" "H2'"  sing N N 81  
1MA "O2'" "HO2'" sing N N 82  
1MA "C1'" N9     sing N N 83  
1MA "C1'" "H1'"  sing N N 84  
1MA N9    C8     sing Y N 85  
1MA N9    C4     sing Y N 86  
1MA C8    N7     doub Y N 87  
1MA C8    H8     sing N N 88  
1MA N7    C5     sing Y N 89  
1MA C5    C6     sing N N 90  
1MA C5    C4     doub Y N 91  
1MA C6    N6     doub N N 92  
1MA C6    N1     sing N N 93  
1MA N6    HN61   sing N N 94  
1MA N1    CM1    sing N N 95  
1MA N1    C2     sing N N 96  
1MA CM1   HM11   sing N N 97  
1MA CM1   HM12   sing N N 98  
1MA CM1   HM13   sing N N 99  
1MA C2    N3     doub N N 100 
1MA C2    H2     sing N N 101 
1MA N3    C4     sing N N 102 
2MG P     OP1    doub N N 103 
2MG P     OP2    sing N N 104 
2MG P     OP3    sing N N 105 
2MG P     "O5'"  sing N N 106 
2MG OP2   HOP2   sing N N 107 
2MG OP3   HOP3   sing N N 108 
2MG "O5'" "C5'"  sing N N 109 
2MG "C5'" "C4'"  sing N N 110 
2MG "C5'" "H5'"  sing N N 111 
2MG "C5'" "H5''" sing N N 112 
2MG "C4'" "O4'"  sing N N 113 
2MG "C4'" "C3'"  sing N N 114 
2MG "C4'" "H4'"  sing N N 115 
2MG "O4'" "C1'"  sing N N 116 
2MG "C3'" "O3'"  sing N N 117 
2MG "C3'" "C2'"  sing N N 118 
2MG "C3'" "H3'"  sing N N 119 
2MG "O3'" "HO3'" sing N N 120 
2MG "C2'" "O2'"  sing N N 121 
2MG "C2'" "C1'"  sing N N 122 
2MG "C2'" "H2'"  sing N N 123 
2MG "O2'" "HO2'" sing N N 124 
2MG "C1'" N9     sing N N 125 
2MG "C1'" "H1'"  sing N N 126 
2MG N9    C8     sing Y N 127 
2MG N9    C4     sing Y N 128 
2MG C8    N7     doub Y N 129 
2MG C8    H8     sing N N 130 
2MG N7    C5     sing Y N 131 
2MG C5    C6     sing N N 132 
2MG C5    C4     doub Y N 133 
2MG C6    O6     doub N N 134 
2MG C6    N1     sing N N 135 
2MG N1    C2     sing N N 136 
2MG N1    HN1    sing N N 137 
2MG C2    N2     sing N N 138 
2MG C2    N3     doub N N 139 
2MG N2    CM2    sing N N 140 
2MG N2    HN2    sing N N 141 
2MG CM2   HM21   sing N N 142 
2MG CM2   HM22   sing N N 143 
2MG CM2   HM23   sing N N 144 
2MG N3    C4     sing N N 145 
2MU N1    C2     sing N N 146 
2MU N1    C6     sing N N 147 
2MU N1    "C1'"  sing N N 148 
2MU C2    N3     sing N N 149 
2MU C2    O2     doub N N 150 
2MU N3    C4     sing N N 151 
2MU N3    HN3    sing N N 152 
2MU C4    C5     sing N N 153 
2MU C4    O4     doub N N 154 
2MU C5    C5M    sing N N 155 
2MU C5    C6     doub N N 156 
2MU C5M   HM51   sing N N 157 
2MU C5M   HM52   sing N N 158 
2MU C5M   HM53   sing N N 159 
2MU C6    H6     sing N N 160 
2MU "C1'" "C2'"  sing N N 161 
2MU "C1'" "O4'"  sing N N 162 
2MU "C1'" "H1'"  sing N N 163 
2MU "C2'" "O2'"  sing N N 164 
2MU "C2'" "C3'"  sing N N 165 
2MU "C2'" "H2'"  sing N N 166 
2MU "O2'" "C6'"  sing N N 167 
2MU "C3'" "C4'"  sing N N 168 
2MU "C3'" "O3'"  sing N N 169 
2MU "C3'" "H3'"  sing N N 170 
2MU "C4'" "O4'"  sing N N 171 
2MU "C4'" "C5'"  sing N N 172 
2MU "C4'" "H4'"  sing N N 173 
2MU "O3'" "HO3'" sing N N 174 
2MU "C5'" "O5'"  sing N N 175 
2MU "C5'" "H5'"  sing N N 176 
2MU "C5'" "H5''" sing N N 177 
2MU "O5'" P      sing N N 178 
2MU "C6'" "H6'1" sing N N 179 
2MU "C6'" "H6'2" sing N N 180 
2MU "C6'" "H6'3" sing N N 181 
2MU P     OP1    doub N N 182 
2MU P     OP2    sing N N 183 
2MU P     OP3    sing N N 184 
2MU OP2   HOP2   sing N N 185 
2MU OP3   HOP3   sing N N 186 
5MC P     OP1    doub N N 187 
5MC P     OP2    sing N N 188 
5MC P     OP3    sing N N 189 
5MC P     "O5'"  sing N N 190 
5MC OP2   HOP2   sing N N 191 
5MC OP3   HOP3   sing N N 192 
5MC "O5'" "C5'"  sing N N 193 
5MC "C5'" "C4'"  sing N N 194 
5MC "C5'" "H5'"  sing N N 195 
5MC "C5'" "H5''" sing N N 196 
5MC "C4'" "O4'"  sing N N 197 
5MC "C4'" "C3'"  sing N N 198 
5MC "C4'" "H4'"  sing N N 199 
5MC "O4'" "C1'"  sing N N 200 
5MC "C3'" "O3'"  sing N N 201 
5MC "C3'" "C2'"  sing N N 202 
5MC "C3'" "H3'"  sing N N 203 
5MC "O3'" "HO3'" sing N N 204 
5MC "C2'" "O2'"  sing N N 205 
5MC "C2'" "C1'"  sing N N 206 
5MC "C2'" "H2'"  sing N N 207 
5MC "O2'" "HO2'" sing N N 208 
5MC "C1'" N1     sing N N 209 
5MC "C1'" "H1'"  sing N N 210 
5MC N1    C2     sing N N 211 
5MC N1    C6     sing N N 212 
5MC C2    O2     doub N N 213 
5MC C2    N3     sing N N 214 
5MC N3    C4     doub N N 215 
5MC C4    N4     sing N N 216 
5MC C4    C5     sing N N 217 
5MC N4    HN41   sing N N 218 
5MC N4    HN42   sing N N 219 
5MC C5    C6     doub N N 220 
5MC C5    CM5    sing N N 221 
5MC C6    H6     sing N N 222 
5MC CM5   HM51   sing N N 223 
5MC CM5   HM52   sing N N 224 
5MC CM5   HM53   sing N N 225 
70U N1    C2     sing N N 226 
70U N1    C6     sing N N 227 
70U N1    "C1'"  sing N N 228 
70U C2    S2     doub N N 229 
70U C2    N3     sing N N 230 
70U N3    C4     sing N N 231 
70U N3    HN3    sing N N 232 
70U C4    O4     doub N N 233 
70U C4    C5     sing N N 234 
70U C5    C6     doub N N 235 
70U C5    C5M    sing N N 236 
70U C6    H6     sing N N 237 
70U C5M   C8     sing N N 238 
70U C5M   H71    sing N N 239 
70U C5M   H72    sing N N 240 
70U C8    O8     doub N N 241 
70U C8    O9     sing N N 242 
70U O9    C9     sing N N 243 
70U C9    H91    sing N N 244 
70U C9    H92    sing N N 245 
70U C9    H93    sing N N 246 
70U "C1'" "C2'"  sing N N 247 
70U "C1'" "O4'"  sing N N 248 
70U "C1'" "H1'"  sing N N 249 
70U "O2'" "C2'"  sing N N 250 
70U "O2'" "HO2'" sing N N 251 
70U "C2'" "C3'"  sing N N 252 
70U "C2'" "H2'"  sing N N 253 
70U "O3'" "C3'"  sing N N 254 
70U "O3'" "HO3'" sing N N 255 
70U "C3'" "C4'"  sing N N 256 
70U "C3'" "H3'"  sing N N 257 
70U "C4'" "O4'"  sing N N 258 
70U "C4'" "C5'"  sing N N 259 
70U "C4'" "H4'"  sing N N 260 
70U "C5'" "O5'"  sing N N 261 
70U "C5'" "H5'"  sing N N 262 
70U "C5'" "H5''" sing N N 263 
70U "O5'" P      sing N N 264 
70U P     OP1    doub N N 265 
70U P     OP2    sing N N 266 
70U P     OP3    sing N N 267 
70U OP2   HOP2   sing N N 268 
70U OP3   HOP3   sing N N 269 
7MG P     OP1    doub N N 270 
7MG P     OP2    sing N N 271 
7MG P     OP3    sing N N 272 
7MG P     "O5'"  sing N N 273 
7MG OP2   HOP2   sing N N 274 
7MG OP3   HOP3   sing N N 275 
7MG "O5'" "C5'"  sing N N 276 
7MG "C5'" "C4'"  sing N N 277 
7MG "C5'" "H5'"  sing N N 278 
7MG "C5'" "H5''" sing N N 279 
7MG "C4'" "O4'"  sing N N 280 
7MG "C4'" "C3'"  sing N N 281 
7MG "C4'" "H4'"  sing N N 282 
7MG "O4'" "C1'"  sing N N 283 
7MG "C3'" "O3'"  sing N N 284 
7MG "C3'" "C2'"  sing N N 285 
7MG "C3'" "H3'"  sing N N 286 
7MG "O3'" "HO3'" sing N N 287 
7MG "C2'" "O2'"  sing N N 288 
7MG "C2'" "C1'"  sing N N 289 
7MG "C2'" "H2'"  sing N N 290 
7MG "O2'" "HO2'" sing N N 291 
7MG "C1'" N9     sing N N 292 
7MG "C1'" "H1'"  sing N N 293 
7MG N9    C8     sing N N 294 
7MG N9    C4     sing N N 295 
7MG C8    N7     sing N N 296 
7MG C8    H81    sing N N 297 
7MG C8    H82    sing N N 298 
7MG N7    C5     sing N N 299 
7MG N7    CM7    sing N N 300 
7MG C5    C6     sing N N 301 
7MG C5    C4     doub N N 302 
7MG C6    O6     doub N N 303 
7MG C6    N1     sing N N 304 
7MG N1    C2     sing N N 305 
7MG N1    HN1    sing N N 306 
7MG C2    N2     sing N N 307 
7MG C2    N3     doub N N 308 
7MG N2    HN21   sing N N 309 
7MG N2    HN22   sing N N 310 
7MG N3    C4     sing N N 311 
7MG CM7   HM71   sing N N 312 
7MG CM7   HM72   sing N N 313 
7MG CM7   HM73   sing N N 314 
A   OP3   P      sing N N 315 
A   OP3   HOP3   sing N N 316 
A   P     OP1    doub N N 317 
A   P     OP2    sing N N 318 
A   P     "O5'"  sing N N 319 
A   OP2   HOP2   sing N N 320 
A   "O5'" "C5'"  sing N N 321 
A   "C5'" "C4'"  sing N N 322 
A   "C5'" "H5'"  sing N N 323 
A   "C5'" "H5''" sing N N 324 
A   "C4'" "O4'"  sing N N 325 
A   "C4'" "C3'"  sing N N 326 
A   "C4'" "H4'"  sing N N 327 
A   "O4'" "C1'"  sing N N 328 
A   "C3'" "O3'"  sing N N 329 
A   "C3'" "C2'"  sing N N 330 
A   "C3'" "H3'"  sing N N 331 
A   "O3'" "HO3'" sing N N 332 
A   "C2'" "O2'"  sing N N 333 
A   "C2'" "C1'"  sing N N 334 
A   "C2'" "H2'"  sing N N 335 
A   "O2'" "HO2'" sing N N 336 
A   "C1'" N9     sing N N 337 
A   "C1'" "H1'"  sing N N 338 
A   N9    C8     sing Y N 339 
A   N9    C4     sing Y N 340 
A   C8    N7     doub Y N 341 
A   C8    H8     sing N N 342 
A   N7    C5     sing Y N 343 
A   C5    C6     sing Y N 344 
A   C5    C4     doub Y N 345 
A   C6    N6     sing N N 346 
A   C6    N1     doub Y N 347 
A   N6    H61    sing N N 348 
A   N6    H62    sing N N 349 
A   N1    C2     sing Y N 350 
A   C2    N3     doub Y N 351 
A   C2    H2     sing N N 352 
A   N3    C4     sing Y N 353 
ALA N     CA     sing N N 354 
ALA N     H      sing N N 355 
ALA N     H2     sing N N 356 
ALA CA    C      sing N N 357 
ALA CA    CB     sing N N 358 
ALA CA    HA     sing N N 359 
ALA C     O      doub N N 360 
ALA C     OXT    sing N N 361 
ALA CB    HB1    sing N N 362 
ALA CB    HB2    sing N N 363 
ALA CB    HB3    sing N N 364 
ALA OXT   HXT    sing N N 365 
AMP P     O1P    doub N N 366 
AMP P     O2P    sing N N 367 
AMP P     O3P    sing N N 368 
AMP P     "O5'"  sing N N 369 
AMP O2P   HOP2   sing N N 370 
AMP O3P   HOP3   sing N N 371 
AMP "O5'" "C5'"  sing N N 372 
AMP "C5'" "C4'"  sing N N 373 
AMP "C5'" "H5'1" sing N N 374 
AMP "C5'" "H5'2" sing N N 375 
AMP "C4'" "O4'"  sing N N 376 
AMP "C4'" "C3'"  sing N N 377 
AMP "C4'" "H4'"  sing N N 378 
AMP "O4'" "C1'"  sing N N 379 
AMP "C3'" "O3'"  sing N N 380 
AMP "C3'" "C2'"  sing N N 381 
AMP "C3'" "H3'"  sing N N 382 
AMP "O3'" "HO3'" sing N N 383 
AMP "C2'" "O2'"  sing N N 384 
AMP "C2'" "C1'"  sing N N 385 
AMP "C2'" "H2'"  sing N N 386 
AMP "O2'" "HO2'" sing N N 387 
AMP "C1'" N9     sing N N 388 
AMP "C1'" "H1'"  sing N N 389 
AMP N9    C8     sing Y N 390 
AMP N9    C4     sing Y N 391 
AMP C8    N7     doub Y N 392 
AMP C8    H8     sing N N 393 
AMP N7    C5     sing Y N 394 
AMP C5    C6     sing Y N 395 
AMP C5    C4     doub Y N 396 
AMP C6    N6     sing N N 397 
AMP C6    N1     doub Y N 398 
AMP N6    HN61   sing N N 399 
AMP N6    HN62   sing N N 400 
AMP N1    C2     sing Y N 401 
AMP C2    N3     doub Y N 402 
AMP C2    H2     sing N N 403 
AMP N3    C4     sing Y N 404 
ARG N     CA     sing N N 405 
ARG N     H      sing N N 406 
ARG N     H2     sing N N 407 
ARG CA    C      sing N N 408 
ARG CA    CB     sing N N 409 
ARG CA    HA     sing N N 410 
ARG C     O      doub N N 411 
ARG C     OXT    sing N N 412 
ARG CB    CG     sing N N 413 
ARG CB    HB2    sing N N 414 
ARG CB    HB3    sing N N 415 
ARG CG    CD     sing N N 416 
ARG CG    HG2    sing N N 417 
ARG CG    HG3    sing N N 418 
ARG CD    NE     sing N N 419 
ARG CD    HD2    sing N N 420 
ARG CD    HD3    sing N N 421 
ARG NE    CZ     sing N N 422 
ARG NE    HE     sing N N 423 
ARG CZ    NH1    sing N N 424 
ARG CZ    NH2    doub N N 425 
ARG NH1   HH11   sing N N 426 
ARG NH1   HH12   sing N N 427 
ARG NH2   HH21   sing N N 428 
ARG NH2   HH22   sing N N 429 
ARG OXT   HXT    sing N N 430 
ASN N     CA     sing N N 431 
ASN N     H      sing N N 432 
ASN N     H2     sing N N 433 
ASN CA    C      sing N N 434 
ASN CA    CB     sing N N 435 
ASN CA    HA     sing N N 436 
ASN C     O      doub N N 437 
ASN C     OXT    sing N N 438 
ASN CB    CG     sing N N 439 
ASN CB    HB2    sing N N 440 
ASN CB    HB3    sing N N 441 
ASN CG    OD1    doub N N 442 
ASN CG    ND2    sing N N 443 
ASN ND2   HD21   sing N N 444 
ASN ND2   HD22   sing N N 445 
ASN OXT   HXT    sing N N 446 
ASP N     CA     sing N N 447 
ASP N     H      sing N N 448 
ASP N     H2     sing N N 449 
ASP CA    C      sing N N 450 
ASP CA    CB     sing N N 451 
ASP CA    HA     sing N N 452 
ASP C     O      doub N N 453 
ASP C     OXT    sing N N 454 
ASP CB    CG     sing N N 455 
ASP CB    HB2    sing N N 456 
ASP CB    HB3    sing N N 457 
ASP CG    OD1    doub N N 458 
ASP CG    OD2    sing N N 459 
ASP OD2   HD2    sing N N 460 
ASP OXT   HXT    sing N N 461 
C   OP3   P      sing N N 462 
C   OP3   HOP3   sing N N 463 
C   P     OP1    doub N N 464 
C   P     OP2    sing N N 465 
C   P     "O5'"  sing N N 466 
C   OP2   HOP2   sing N N 467 
C   "O5'" "C5'"  sing N N 468 
C   "C5'" "C4'"  sing N N 469 
C   "C5'" "H5'"  sing N N 470 
C   "C5'" "H5''" sing N N 471 
C   "C4'" "O4'"  sing N N 472 
C   "C4'" "C3'"  sing N N 473 
C   "C4'" "H4'"  sing N N 474 
C   "O4'" "C1'"  sing N N 475 
C   "C3'" "O3'"  sing N N 476 
C   "C3'" "C2'"  sing N N 477 
C   "C3'" "H3'"  sing N N 478 
C   "O3'" "HO3'" sing N N 479 
C   "C2'" "O2'"  sing N N 480 
C   "C2'" "C1'"  sing N N 481 
C   "C2'" "H2'"  sing N N 482 
C   "O2'" "HO2'" sing N N 483 
C   "C1'" N1     sing N N 484 
C   "C1'" "H1'"  sing N N 485 
C   N1    C2     sing N N 486 
C   N1    C6     sing N N 487 
C   C2    O2     doub N N 488 
C   C2    N3     sing N N 489 
C   N3    C4     doub N N 490 
C   C4    N4     sing N N 491 
C   C4    C5     sing N N 492 
C   N4    H41    sing N N 493 
C   N4    H42    sing N N 494 
C   C5    C6     doub N N 495 
C   C5    H5     sing N N 496 
C   C6    H6     sing N N 497 
CYS N     CA     sing N N 498 
CYS N     H      sing N N 499 
CYS N     H2     sing N N 500 
CYS CA    C      sing N N 501 
CYS CA    CB     sing N N 502 
CYS CA    HA     sing N N 503 
CYS C     O      doub N N 504 
CYS C     OXT    sing N N 505 
CYS CB    SG     sing N N 506 
CYS CB    HB2    sing N N 507 
CYS CB    HB3    sing N N 508 
CYS SG    HG     sing N N 509 
CYS OXT   HXT    sing N N 510 
G   OP3   P      sing N N 511 
G   OP3   HOP3   sing N N 512 
G   P     OP1    doub N N 513 
G   P     OP2    sing N N 514 
G   P     "O5'"  sing N N 515 
G   OP2   HOP2   sing N N 516 
G   "O5'" "C5'"  sing N N 517 
G   "C5'" "C4'"  sing N N 518 
G   "C5'" "H5'"  sing N N 519 
G   "C5'" "H5''" sing N N 520 
G   "C4'" "O4'"  sing N N 521 
G   "C4'" "C3'"  sing N N 522 
G   "C4'" "H4'"  sing N N 523 
G   "O4'" "C1'"  sing N N 524 
G   "C3'" "O3'"  sing N N 525 
G   "C3'" "C2'"  sing N N 526 
G   "C3'" "H3'"  sing N N 527 
G   "O3'" "HO3'" sing N N 528 
G   "C2'" "O2'"  sing N N 529 
G   "C2'" "C1'"  sing N N 530 
G   "C2'" "H2'"  sing N N 531 
G   "O2'" "HO2'" sing N N 532 
G   "C1'" N9     sing N N 533 
G   "C1'" "H1'"  sing N N 534 
G   N9    C8     sing Y N 535 
G   N9    C4     sing Y N 536 
G   C8    N7     doub Y N 537 
G   C8    H8     sing N N 538 
G   N7    C5     sing Y N 539 
G   C5    C6     sing N N 540 
G   C5    C4     doub Y N 541 
G   C6    O6     doub N N 542 
G   C6    N1     sing N N 543 
G   N1    C2     sing N N 544 
G   N1    H1     sing N N 545 
G   C2    N2     sing N N 546 
G   C2    N3     doub N N 547 
G   N2    H21    sing N N 548 
G   N2    H22    sing N N 549 
G   N3    C4     sing N N 550 
GLN N     CA     sing N N 551 
GLN N     H      sing N N 552 
GLN N     H2     sing N N 553 
GLN CA    C      sing N N 554 
GLN CA    CB     sing N N 555 
GLN CA    HA     sing N N 556 
GLN C     O      doub N N 557 
GLN C     OXT    sing N N 558 
GLN CB    CG     sing N N 559 
GLN CB    HB2    sing N N 560 
GLN CB    HB3    sing N N 561 
GLN CG    CD     sing N N 562 
GLN CG    HG2    sing N N 563 
GLN CG    HG3    sing N N 564 
GLN CD    OE1    doub N N 565 
GLN CD    NE2    sing N N 566 
GLN NE2   HE21   sing N N 567 
GLN NE2   HE22   sing N N 568 
GLN OXT   HXT    sing N N 569 
GLU N     CA     sing N N 570 
GLU N     H      sing N N 571 
GLU N     H2     sing N N 572 
GLU CA    C      sing N N 573 
GLU CA    CB     sing N N 574 
GLU CA    HA     sing N N 575 
GLU C     O      doub N N 576 
GLU C     OXT    sing N N 577 
GLU CB    CG     sing N N 578 
GLU CB    HB2    sing N N 579 
GLU CB    HB3    sing N N 580 
GLU CG    CD     sing N N 581 
GLU CG    HG2    sing N N 582 
GLU CG    HG3    sing N N 583 
GLU CD    OE1    doub N N 584 
GLU CD    OE2    sing N N 585 
GLU OE2   HE2    sing N N 586 
GLU OXT   HXT    sing N N 587 
GLY N     CA     sing N N 588 
GLY N     H      sing N N 589 
GLY N     H2     sing N N 590 
GLY CA    C      sing N N 591 
GLY CA    HA2    sing N N 592 
GLY CA    HA3    sing N N 593 
GLY C     O      doub N N 594 
GLY C     OXT    sing N N 595 
GLY OXT   HXT    sing N N 596 
H2U P     OP1    doub N N 597 
H2U P     OP2    sing N N 598 
H2U P     OP3    sing N N 599 
H2U P     "O5'"  sing N N 600 
H2U OP2   HOP2   sing N N 601 
H2U OP3   HOP3   sing N N 602 
H2U "O5'" "C5'"  sing N N 603 
H2U "C5'" "C4'"  sing N N 604 
H2U "C5'" "H5'"  sing N N 605 
H2U "C5'" "H5''" sing N N 606 
H2U "C4'" "O4'"  sing N N 607 
H2U "C4'" "C3'"  sing N N 608 
H2U "C4'" "H4'"  sing N N 609 
H2U "O4'" "C1'"  sing N N 610 
H2U "C3'" "O3'"  sing N N 611 
H2U "C3'" "C2'"  sing N N 612 
H2U "C3'" "H3'"  sing N N 613 
H2U "O3'" "HO3'" sing N N 614 
H2U "C1'" "C2'"  sing N N 615 
H2U "C1'" N1     sing N N 616 
H2U "C1'" "H1'"  sing N N 617 
H2U "C2'" "O2'"  sing N N 618 
H2U "C2'" "H2'"  sing N N 619 
H2U "O2'" "HO2'" sing N N 620 
H2U N1    C2     sing N N 621 
H2U N1    C6     sing N N 622 
H2U C2    O2     doub N N 623 
H2U C2    N3     sing N N 624 
H2U N3    C4     sing N N 625 
H2U N3    HN3    sing N N 626 
H2U C4    O4     doub N N 627 
H2U C4    C5     sing N N 628 
H2U C5    C6     sing N N 629 
H2U C5    H51    sing N N 630 
H2U C5    H52    sing N N 631 
H2U C6    H61    sing N N 632 
H2U C6    H62    sing N N 633 
HIS N     CA     sing N N 634 
HIS N     H      sing N N 635 
HIS N     H2     sing N N 636 
HIS CA    C      sing N N 637 
HIS CA    CB     sing N N 638 
HIS CA    HA     sing N N 639 
HIS C     O      doub N N 640 
HIS C     OXT    sing N N 641 
HIS CB    CG     sing N N 642 
HIS CB    HB2    sing N N 643 
HIS CB    HB3    sing N N 644 
HIS CG    ND1    sing Y N 645 
HIS CG    CD2    doub Y N 646 
HIS ND1   CE1    doub Y N 647 
HIS ND1   HD1    sing N N 648 
HIS CD2   NE2    sing Y N 649 
HIS CD2   HD2    sing N N 650 
HIS CE1   NE2    sing Y N 651 
HIS CE1   HE1    sing N N 652 
HIS NE2   HE2    sing N N 653 
HIS OXT   HXT    sing N N 654 
ILE N     CA     sing N N 655 
ILE N     H      sing N N 656 
ILE N     H2     sing N N 657 
ILE CA    C      sing N N 658 
ILE CA    CB     sing N N 659 
ILE CA    HA     sing N N 660 
ILE C     O      doub N N 661 
ILE C     OXT    sing N N 662 
ILE CB    CG1    sing N N 663 
ILE CB    CG2    sing N N 664 
ILE CB    HB     sing N N 665 
ILE CG1   CD1    sing N N 666 
ILE CG1   HG12   sing N N 667 
ILE CG1   HG13   sing N N 668 
ILE CG2   HG21   sing N N 669 
ILE CG2   HG22   sing N N 670 
ILE CG2   HG23   sing N N 671 
ILE CD1   HD11   sing N N 672 
ILE CD1   HD12   sing N N 673 
ILE CD1   HD13   sing N N 674 
ILE OXT   HXT    sing N N 675 
LEU N     CA     sing N N 676 
LEU N     H      sing N N 677 
LEU N     H2     sing N N 678 
LEU CA    C      sing N N 679 
LEU CA    CB     sing N N 680 
LEU CA    HA     sing N N 681 
LEU C     O      doub N N 682 
LEU C     OXT    sing N N 683 
LEU CB    CG     sing N N 684 
LEU CB    HB2    sing N N 685 
LEU CB    HB3    sing N N 686 
LEU CG    CD1    sing N N 687 
LEU CG    CD2    sing N N 688 
LEU CG    HG     sing N N 689 
LEU CD1   HD11   sing N N 690 
LEU CD1   HD12   sing N N 691 
LEU CD1   HD13   sing N N 692 
LEU CD2   HD21   sing N N 693 
LEU CD2   HD22   sing N N 694 
LEU CD2   HD23   sing N N 695 
LEU OXT   HXT    sing N N 696 
LYS N     CA     sing N N 697 
LYS N     H      sing N N 698 
LYS N     H2     sing N N 699 
LYS CA    C      sing N N 700 
LYS CA    CB     sing N N 701 
LYS CA    HA     sing N N 702 
LYS C     O      doub N N 703 
LYS C     OXT    sing N N 704 
LYS CB    CG     sing N N 705 
LYS CB    HB2    sing N N 706 
LYS CB    HB3    sing N N 707 
LYS CG    CD     sing N N 708 
LYS CG    HG2    sing N N 709 
LYS CG    HG3    sing N N 710 
LYS CD    CE     sing N N 711 
LYS CD    HD2    sing N N 712 
LYS CD    HD3    sing N N 713 
LYS CE    NZ     sing N N 714 
LYS CE    HE2    sing N N 715 
LYS CE    HE3    sing N N 716 
LYS NZ    HZ1    sing N N 717 
LYS NZ    HZ2    sing N N 718 
LYS NZ    HZ3    sing N N 719 
LYS OXT   HXT    sing N N 720 
MET N     CA     sing N N 721 
MET N     H      sing N N 722 
MET N     H2     sing N N 723 
MET CA    C      sing N N 724 
MET CA    CB     sing N N 725 
MET CA    HA     sing N N 726 
MET C     O      doub N N 727 
MET C     OXT    sing N N 728 
MET CB    CG     sing N N 729 
MET CB    HB2    sing N N 730 
MET CB    HB3    sing N N 731 
MET CG    SD     sing N N 732 
MET CG    HG2    sing N N 733 
MET CG    HG3    sing N N 734 
MET SD    CE     sing N N 735 
MET CE    HE1    sing N N 736 
MET CE    HE2    sing N N 737 
MET CE    HE3    sing N N 738 
MET OXT   HXT    sing N N 739 
PHE N     CA     sing N N 740 
PHE N     H      sing N N 741 
PHE N     H2     sing N N 742 
PHE CA    C      sing N N 743 
PHE CA    CB     sing N N 744 
PHE CA    HA     sing N N 745 
PHE C     O      doub N N 746 
PHE C     OXT    sing N N 747 
PHE CB    CG     sing N N 748 
PHE CB    HB2    sing N N 749 
PHE CB    HB3    sing N N 750 
PHE CG    CD1    doub Y N 751 
PHE CG    CD2    sing Y N 752 
PHE CD1   CE1    sing Y N 753 
PHE CD1   HD1    sing N N 754 
PHE CD2   CE2    doub Y N 755 
PHE CD2   HD2    sing N N 756 
PHE CE1   CZ     doub Y N 757 
PHE CE1   HE1    sing N N 758 
PHE CE2   CZ     sing Y N 759 
PHE CE2   HE2    sing N N 760 
PHE CZ    HZ     sing N N 761 
PHE OXT   HXT    sing N N 762 
PRO N     CA     sing N N 763 
PRO N     CD     sing N N 764 
PRO N     H      sing N N 765 
PRO CA    C      sing N N 766 
PRO CA    CB     sing N N 767 
PRO CA    HA     sing N N 768 
PRO C     O      doub N N 769 
PRO C     OXT    sing N N 770 
PRO CB    CG     sing N N 771 
PRO CB    HB2    sing N N 772 
PRO CB    HB3    sing N N 773 
PRO CG    CD     sing N N 774 
PRO CG    HG2    sing N N 775 
PRO CG    HG3    sing N N 776 
PRO CD    HD2    sing N N 777 
PRO CD    HD3    sing N N 778 
PRO OXT   HXT    sing N N 779 
PSU N1    C2     sing N N 780 
PSU N1    C6     sing N N 781 
PSU N1    HN1    sing N N 782 
PSU C2    N3     sing N N 783 
PSU C2    O2     doub N N 784 
PSU N3    C4     sing N N 785 
PSU N3    HN3    sing N N 786 
PSU C4    C5     sing N N 787 
PSU C4    O4     doub N N 788 
PSU C5    C6     doub N N 789 
PSU C5    "C1'"  sing N N 790 
PSU C6    H6     sing N N 791 
PSU "C1'" "C2'"  sing N N 792 
PSU "C1'" "O4'"  sing N N 793 
PSU "C1'" "H1'"  sing N N 794 
PSU "C2'" "O2'"  sing N N 795 
PSU "C2'" "C3'"  sing N N 796 
PSU "C2'" "H2'"  sing N N 797 
PSU "O2'" "HO2'" sing N N 798 
PSU "C3'" "C4'"  sing N N 799 
PSU "C3'" "O3'"  sing N N 800 
PSU "C3'" "H3'"  sing N N 801 
PSU "C4'" "O4'"  sing N N 802 
PSU "C4'" "C5'"  sing N N 803 
PSU "C4'" "H4'"  sing N N 804 
PSU "O3'" "HO3'" sing N N 805 
PSU "C5'" "O5'"  sing N N 806 
PSU "C5'" "H5'"  sing N N 807 
PSU "C5'" "H5''" sing N N 808 
PSU "O5'" P      sing N N 809 
PSU P     OP1    doub N N 810 
PSU P     OP2    sing N N 811 
PSU P     OP3    sing N N 812 
PSU OP2   HOP2   sing N N 813 
PSU OP3   HOP3   sing N N 814 
SER N     CA     sing N N 815 
SER N     H      sing N N 816 
SER N     H2     sing N N 817 
SER CA    C      sing N N 818 
SER CA    CB     sing N N 819 
SER CA    HA     sing N N 820 
SER C     O      doub N N 821 
SER C     OXT    sing N N 822 
SER CB    OG     sing N N 823 
SER CB    HB2    sing N N 824 
SER CB    HB3    sing N N 825 
SER OG    HG     sing N N 826 
SER OXT   HXT    sing N N 827 
THR N     CA     sing N N 828 
THR N     H      sing N N 829 
THR N     H2     sing N N 830 
THR CA    C      sing N N 831 
THR CA    CB     sing N N 832 
THR CA    HA     sing N N 833 
THR C     O      doub N N 834 
THR C     OXT    sing N N 835 
THR CB    OG1    sing N N 836 
THR CB    CG2    sing N N 837 
THR CB    HB     sing N N 838 
THR OG1   HG1    sing N N 839 
THR CG2   HG21   sing N N 840 
THR CG2   HG22   sing N N 841 
THR CG2   HG23   sing N N 842 
THR OXT   HXT    sing N N 843 
TRP N     CA     sing N N 844 
TRP N     H      sing N N 845 
TRP N     H2     sing N N 846 
TRP CA    C      sing N N 847 
TRP CA    CB     sing N N 848 
TRP CA    HA     sing N N 849 
TRP C     O      doub N N 850 
TRP C     OXT    sing N N 851 
TRP CB    CG     sing N N 852 
TRP CB    HB2    sing N N 853 
TRP CB    HB3    sing N N 854 
TRP CG    CD1    doub Y N 855 
TRP CG    CD2    sing Y N 856 
TRP CD1   NE1    sing Y N 857 
TRP CD1   HD1    sing N N 858 
TRP CD2   CE2    doub Y N 859 
TRP CD2   CE3    sing Y N 860 
TRP NE1   CE2    sing Y N 861 
TRP NE1   HE1    sing N N 862 
TRP CE2   CZ2    sing Y N 863 
TRP CE3   CZ3    doub Y N 864 
TRP CE3   HE3    sing N N 865 
TRP CZ2   CH2    doub Y N 866 
TRP CZ2   HZ2    sing N N 867 
TRP CZ3   CH2    sing Y N 868 
TRP CZ3   HZ3    sing N N 869 
TRP CH2   HH2    sing N N 870 
TRP OXT   HXT    sing N N 871 
TYR N     CA     sing N N 872 
TYR N     H      sing N N 873 
TYR N     H2     sing N N 874 
TYR CA    C      sing N N 875 
TYR CA    CB     sing N N 876 
TYR CA    HA     sing N N 877 
TYR C     O      doub N N 878 
TYR C     OXT    sing N N 879 
TYR CB    CG     sing N N 880 
TYR CB    HB2    sing N N 881 
TYR CB    HB3    sing N N 882 
TYR CG    CD1    doub Y N 883 
TYR CG    CD2    sing Y N 884 
TYR CD1   CE1    sing Y N 885 
TYR CD1   HD1    sing N N 886 
TYR CD2   CE2    doub Y N 887 
TYR CD2   HD2    sing N N 888 
TYR CE1   CZ     doub Y N 889 
TYR CE1   HE1    sing N N 890 
TYR CE2   CZ     sing Y N 891 
TYR CE2   HE2    sing N N 892 
TYR CZ    OH     sing N N 893 
TYR OH    HH     sing N N 894 
TYR OXT   HXT    sing N N 895 
U   OP3   P      sing N N 896 
U   OP3   HOP3   sing N N 897 
U   P     OP1    doub N N 898 
U   P     OP2    sing N N 899 
U   P     "O5'"  sing N N 900 
U   OP2   HOP2   sing N N 901 
U   "O5'" "C5'"  sing N N 902 
U   "C5'" "C4'"  sing N N 903 
U   "C5'" "H5'"  sing N N 904 
U   "C5'" "H5''" sing N N 905 
U   "C4'" "O4'"  sing N N 906 
U   "C4'" "C3'"  sing N N 907 
U   "C4'" "H4'"  sing N N 908 
U   "O4'" "C1'"  sing N N 909 
U   "C3'" "O3'"  sing N N 910 
U   "C3'" "C2'"  sing N N 911 
U   "C3'" "H3'"  sing N N 912 
U   "O3'" "HO3'" sing N N 913 
U   "C2'" "O2'"  sing N N 914 
U   "C2'" "C1'"  sing N N 915 
U   "C2'" "H2'"  sing N N 916 
U   "O2'" "HO2'" sing N N 917 
U   "C1'" N1     sing N N 918 
U   "C1'" "H1'"  sing N N 919 
U   N1    C2     sing N N 920 
U   N1    C6     sing N N 921 
U   C2    O2     doub N N 922 
U   C2    N3     sing N N 923 
U   N3    C4     sing N N 924 
U   N3    H3     sing N N 925 
U   C4    O4     doub N N 926 
U   C4    C5     sing N N 927 
U   C5    C6     doub N N 928 
U   C5    H5     sing N N 929 
U   C6    H6     sing N N 930 
VAL N     CA     sing N N 931 
VAL N     H      sing N N 932 
VAL N     H2     sing N N 933 
VAL CA    C      sing N N 934 
VAL CA    CB     sing N N 935 
VAL CA    HA     sing N N 936 
VAL C     O      doub N N 937 
VAL C     OXT    sing N N 938 
VAL CB    CG1    sing N N 939 
VAL CB    CG2    sing N N 940 
VAL CB    HB     sing N N 941 
VAL CG1   HG11   sing N N 942 
VAL CG1   HG12   sing N N 943 
VAL CG1   HG13   sing N N 944 
VAL CG2   HG21   sing N N 945 
VAL CG2   HG22   sing N N 946 
VAL CG2   HG23   sing N N 947 
VAL OXT   HXT    sing N N 948 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-22 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DPL 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2' 
# 
_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' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_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         50 
_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 
'MODEL FITTING'                 ? 1  ? ? ? 'UCSF ChimeraX' 1.7/v10 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?               ?       
'PARTICLE SELECTION'            ? 3  1 1 1 ?               ?       
'VOLUME SELECTION'              ? 4  1 1 1 ?               ?       
CLASSIFICATION                  ? 5  1 1 1 ?               ?       
MASKING                         ? 6  1 1 1 ?               ?       
RECONSTRUCTION                  ? 7  1 1 1 ?               ?       
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?               ?       
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?               ?       
'CTF CORRECTION'                ? 10 1 1 1 ?               ?       
'LAYERLINE INDEXING'            ? 11 1 1 1 ?               ?       
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?               ?       
'MODEL REFINEMENT'              ? 13 1 1 1 ?               ?       
'SERIES ALIGNMENT'              ? 14 1 1 1 ?               ?       
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?               ?       
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?               ?       
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?               ?       
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?               ?       
OTHER                           ? 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 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9DPL 'double helix'        
9DPL 'a-form double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 C G   1  1_555 C C   72 1_555 -0.789 -0.231 0.044  6.230   -2.890  6.027    1  C_G1:C72_C      C 1  ? C 72 ? 19 1 
1 C C   2  1_555 C G   71 1_555 0.425  -0.143 -0.361 4.724   -10.700 4.123    2  C_C2:G71_C      C 2  ? C 71 ? 19 1 
1 C C   3  1_555 C G   70 1_555 0.821  -0.370 -0.044 0.599   -11.497 -0.159   3  C_C3:G70_C      C 3  ? C 70 ? 19 1 
1 C C   4  1_555 C G   69 1_555 0.713  -0.320 -0.005 3.156   -11.180 -0.622   4  C_C4:G69_C      C 4  ? C 69 ? 19 1 
1 C G   5  1_555 C C   68 1_555 -1.219 -0.553 -0.051 -5.484  -18.598 0.585    5  C_G5:C68_C      C 5  ? C 68 ? 19 1 
1 C G   6  1_555 C U   67 1_555 -1.663 -0.464 0.145  -3.966  -15.836 -1.085   6  C_G6:U67_C      C 6  ? C 67 ? 28 1 
1 C A   7  1_555 C U   66 1_555 0.723  -0.195 0.231  -0.287  -11.058 -0.076   7  C_A7:U66_C      C 7  ? C 66 ? 20 1 
1 C 5MC 49 1_555 C G   65 1_555 0.772  -0.436 -0.222 9.324   -13.772 -2.566   8  C_5MC49:G65_C   C 49 ? C 65 ? 19 1 
1 C A   50 1_555 C U   64 1_555 0.831  -0.222 0.244  1.011   -10.336 2.016    9  C_A50:U64_C     C 50 ? C 64 ? 20 1 
1 C G   51 1_555 C C   63 1_555 -1.112 -0.506 -0.085 -3.983  -10.807 0.353    10 C_G51:C63_C     C 51 ? C 63 ? 19 1 
1 C G   52 1_555 C C   62 1_555 0.225  -0.153 -0.541 -8.347  -10.778 1.191    11 C_G52:C62_C     C 52 ? C 62 ? 19 1 
1 C G   53 1_555 C C   61 1_555 -0.441 -0.330 -0.931 -21.943 -11.767 -1.083   12 C_G53:C61_C     C 53 ? C 61 ? 19 1 
1 C 2MU 54 1_555 C 1MA 58 1_555 4.269  -2.164 0.174  -4.106  14.770  -100.264 13 C_2MU54:1MA58_C C 54 ? C 58 ? 24 4 
1 C PSU 55 1_555 C G   18 1_555 0.312  -5.715 0.314  17.262  5.855   -93.308  14 C_PSU55:G18_C   C 55 ? C 18 ? ?  2 
1 C A   38 1_555 C C   32 1_555 -3.697 -0.917 -0.204 -1.816  1.244   -13.963  15 C_A38:C32_C     C 38 ? C 32 ? ?  1 
1 C PSU 39 1_555 C A   31 1_555 -0.222 -0.155 -0.105 7.577   -8.324  -4.637   16 C_PSU39:A31_C   C 39 ? C 31 ? 21 1 
1 C C   40 1_555 C G   30 1_555 0.383  -0.208 -0.174 5.854   -13.487 1.103    17 C_C40:G30_C     C 40 ? C 30 ? 19 1 
1 C U   41 1_555 C A   29 1_555 0.373  -0.239 -0.097 1.273   -12.344 1.803    18 C_U41:A29_C     C 41 ? C 29 ? 20 1 
1 C G   42 1_555 C C   28 1_555 0.908  -0.202 0.112  -5.374  -15.406 0.851    19 C_G42:C28_C     C 42 ? C 28 ? 19 1 
1 C A   43 1_555 C PSU 27 1_555 0.097  0.054  0.178  -13.575 -23.029 -2.120   20 C_A43:PSU27_C   C 43 ? C 27 ? 21 1 
1 C G   44 1_555 C A   26 1_555 0.261  1.482  -0.042 -18.544 -21.969 -20.013  21 C_G44:A26_C     C 44 ? C 26 ? 8  1 
1 C 2MG 10 1_555 C C   25 1_555 -1.191 -0.305 -0.395 -7.562  -11.679 6.119    22 C_2MG10:C25_C   C 10 ? C 25 ? 19 1 
1 C C   11 1_555 C G   24 1_555 0.586  -0.290 -0.168 -9.270  -12.154 1.654    23 C_C11:G24_C     C 11 ? C 24 ? 19 1 
1 C U   12 1_555 C A   23 1_555 -0.383 -0.116 0.211  -14.414 -9.009  1.809    24 C_U12:A23_C     C 12 ? C 23 ? 20 1 
1 C C   13 1_555 C G   22 1_555 0.189  -0.128 0.317  -12.838 1.494   -0.356   25 C_C13:G22_C     C 13 ? C 22 ? 19 1 
1 C A   14 1_555 C U   8  1_555 -4.272 -2.258 0.104  1.776   6.830   -96.494  26 C_A14:U8_C      C 14 ? C 8  ? 24 4 
1 C G   15 1_555 C 5MC 48 1_555 0.350  3.181  -0.410 7.444   -8.105  159.979  27 C_G15:5MC48_C   C 15 ? C 48 ? 22 2 
1 C G   19 1_555 C C   56 1_555 -1.134 -0.586 0.386  -15.820 -13.843 -3.827   28 C_G19:C56_C     C 19 ? C 56 ? 19 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 C G   1  1_555 C C   72 1_555 C C   2  1_555 C G   71 1_555 -0.639 -1.604 3.449 0.901  2.898  34.874  -3.117 1.202  3.292 4.824 
-1.499  35.002  1  CC_G1C2:G71C72_CC         C 1  ? C 72 ? C 2  ? C 71 ? 
1 C C   2  1_555 C G   71 1_555 C C   3  1_555 C G   70 1_555 -0.131 -1.518 3.446 -1.105 6.772  34.242  -3.568 0.049  3.101 11.360 
1.854   34.902  2  CC_C2C3:G70G71_CC         C 2  ? C 71 ? C 3  ? C 70 ? 
1 C C   3  1_555 C G   70 1_555 C C   4  1_555 C G   69 1_555 -0.634 -1.804 3.258 0.090  7.592  25.877  -5.655 1.382  2.629 16.507 
-0.195  26.949  3  CC_C3C4:G69G70_CC         C 3  ? C 70 ? C 4  ? C 69 ? 
1 C C   4  1_555 C G   69 1_555 C G   5  1_555 C C   68 1_555 1.165  -1.958 3.370 3.227  12.899 26.430  -6.360 -1.655 2.307 26.208 
-6.557  29.533  4  CC_C4G5:C68G69_CC         C 4  ? C 69 ? C 5  ? C 68 ? 
1 C G   5  1_555 C C   68 1_555 C G   6  1_555 C U   67 1_555 -0.451 -1.908 3.171 -3.454 4.724  27.998  -4.861 0.184  2.851 9.631 
7.042   28.591  5  CC_G5G6:U67C68_CC         C 5  ? C 68 ? C 6  ? C 67 ? 
1 C G   6  1_555 C U   67 1_555 C A   7  1_555 C U   66 1_555 -0.095 -0.533 3.270 -1.425 7.327  42.222  -1.451 -0.010 3.141 10.076 
1.960   42.847  6  CC_G6A7:U66U67_CC         C 6  ? C 67 ? C 7  ? C 66 ? 
1 C A   7  1_555 C U   66 1_555 C 5MC 49 1_555 C G   65 1_555 -0.036 -2.097 3.068 5.330  1.029  37.749  -3.332 0.681  2.980 1.581 
-8.186  38.123  7  CC_A75MC49:G65U66_CC      C 7  ? C 66 ? C 49 ? C 65 ? 
1 C 5MC 49 1_555 C G   65 1_555 C A   50 1_555 C U   64 1_555 -0.561 -1.312 3.399 -2.472 8.857  32.829  -3.643 0.566  2.988 15.301 
4.270   34.059  8  CC_5MC49A50:U64G65_CC     C 49 ? C 65 ? C 50 ? C 64 ? 
1 C A   50 1_555 C U   64 1_555 C G   51 1_555 C C   63 1_555 -0.149 -2.054 3.158 2.209  8.993  24.003  -6.775 0.866  2.232 20.666 
-5.076  25.703  9  CC_A50G51:C63U64_CC       C 50 ? C 64 ? C 51 ? C 63 ? 
1 C G   51 1_555 C C   63 1_555 C G   52 1_555 C C   62 1_555 0.077  -1.575 3.452 1.356  10.121 36.084  -3.772 0.057  2.921 15.950 
-2.137  37.455  10 CC_G51G52:C62C63_CC       C 51 ? C 63 ? C 52 ? C 62 ? 
1 C G   52 1_555 C C   62 1_555 C G   53 1_555 C C   61 1_555 0.531  -1.744 3.803 2.325  8.249  28.452  -5.306 -0.501 3.214 16.320 
-4.600  29.689  11 CC_G52G53:C61C62_CC       C 52 ? C 62 ? C 53 ? C 61 ? 
1 C G   53 1_555 C C   61 1_555 C 2MU 54 1_555 C 1MA 58 1_555 -2.608 -1.912 3.096 -3.267 1.497  89.403  -1.388 1.789  3.145 1.064 
2.322   89.460  12 CC_G532MU54:1MA58C61_CC   C 53 ? C 61 ? C 54 ? C 58 ? 
1 C 2MU 54 1_555 C 1MA 58 1_555 C PSU 55 1_555 C G   18 1_555 2.438  -2.240 3.379 5.434  6.288  49.007  -3.144 -2.490 3.322 7.517 
-6.496  49.664  13 CC_2MU54PSU55:G181MA58_CC C 54 ? C 58 ? C 55 ? C 18 ? 
1 C A   38 1_555 C C   32 1_555 C PSU 39 1_555 C A   31 1_555 0.352  -1.047 3.233 -5.111 6.763  42.714  -2.039 -0.949 2.982 9.176 
6.935   43.509  14 CC_A38PSU39:A31C32_CC     C 38 ? C 32 ? C 39 ? C 31 ? 
1 C PSU 39 1_555 C A   31 1_555 C C   40 1_555 C G   30 1_555 0.031  -1.802 3.440 -2.063 7.598  34.037  -4.147 -0.362 2.974 12.768 
3.466   34.909  15 CC_PSU39C40:G30A31_CC     C 39 ? C 31 ? C 40 ? C 30 ? 
1 C C   40 1_555 C G   30 1_555 C U   41 1_555 C A   29 1_555 -0.607 -1.910 3.463 -2.249 12.107 28.890  -5.709 0.718  2.518 22.993 
4.272   31.353  16 CC_C40U41:A29G30_CC       C 40 ? C 30 ? C 41 ? C 29 ? 
1 C U   41 1_555 C A   29 1_555 C G   42 1_555 C C   28 1_555 0.155  -1.453 3.461 0.762  13.273 33.263  -4.243 -0.144 2.706 22.119 
-1.269  35.752  17 CC_U41G42:C28A29_CC       C 41 ? C 29 ? C 42 ? C 28 ? 
1 C G   42 1_555 C C   28 1_555 C A   43 1_555 C PSU 27 1_555 -0.126 -2.110 3.359 4.401  12.522 30.572  -5.577 0.885  2.302 22.466 
-7.896  33.266  18 CC_G42A43:PSU27C28_CC     C 42 ? C 28 ? C 43 ? C 27 ? 
1 C A   43 1_555 C PSU 27 1_555 C G   44 1_555 C A   26 1_555 -1.237 -1.237 3.274 2.558  6.980  33.590  -3.129 2.473  2.868 11.897 
-4.360  34.380  19 CC_A43G44:A26PSU27_CC     C 43 ? C 27 ? C 44 ? C 26 ? 
1 C G   44 1_555 C A   26 1_555 C 2MG 10 1_555 C C   25 1_555 -3.615 -2.377 3.339 12.329 4.140  69.121  -2.202 3.545  2.616 3.617 
-10.771 70.184  20 CC_G442MG10:C25A26_CC     C 44 ? C 26 ? C 10 ? C 25 ? 
1 C 2MG 10 1_555 C C   25 1_555 C C   11 1_555 C G   24 1_555 -1.259 -1.340 3.330 -1.672 4.128  42.919  -2.230 1.547  3.238 5.624 
2.278   43.139  21 CC_2MG10C11:G24C25_CC     C 10 ? C 25 ? C 11 ? C 24 ? 
1 C C   11 1_555 C G   24 1_555 C U   12 1_555 C A   23 1_555 0.125  -1.429 3.374 -0.576 10.693 29.359  -4.603 -0.337 2.698 20.267 
1.092   31.211  22 CC_C11U12:A23G24_CC       C 11 ? C 24 ? C 12 ? C 23 ? 
1 C U   12 1_555 C A   23 1_555 C C   13 1_555 C G   22 1_555 1.703  -2.191 3.234 6.565  2.174  27.018  -5.081 -1.928 3.363 4.558 
-13.766 27.873  23 CC_U12C13:G22A23_CC       C 12 ? C 23 ? C 13 ? C 22 ? 
1 C C   13 1_555 C G   22 1_555 C A   14 1_555 C U   8  1_555 -1.486 -0.533 3.089 5.064  -0.280 61.490  -0.508 1.668  2.973 -0.274 
-4.943  61.678  24 CC_C13A14:U8G22_CC        C 13 ? C 22 ? C 14 ? C 8  ? 
1 C A   14 1_555 C U   8  1_555 C G   15 1_555 C 5MC 48 1_555 1.931  -3.124 3.624 1.369  12.930 -68.586 2.184  1.749  4.051 
-11.371 1.204   -69.659 25 CC_A14G15:5MC48U8_CC      C 14 ? C 8  ? C 15 ? C 48 ? 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'AI157890-01A1 (R21 grant)' 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9DPL 
_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  
MG 
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . SER A 1 14  ? 176.071 150.000 172.391 1.00 25974. ? 14  SER A N     1 
ATOM   2     C  CA    . SER A 1 14  ? 175.357 150.397 171.149 1.00 25976. ? 14  SER A CA    1 
ATOM   3     C  C     . SER A 1 14  ? 175.362 151.926 171.012 1.00 25984. ? 14  SER A C     1 
ATOM   4     O  O     . SER A 1 14  ? 176.395 152.548 171.346 1.00 25984. ? 14  SER A O     1 
ATOM   5     C  CB    . SER A 1 14  ? 173.951 149.853 171.132 1.00 25975. ? 14  SER A CB    1 
ATOM   6     O  OG    . SER A 1 14  ? 173.957 148.433 171.194 1.00 25972. ? 14  SER A OG    1 
ATOM   7     N  N     . GLU A 1 15  ? 174.251 152.503 170.545 1.00 26478. ? 15  GLU A N     1 
ATOM   8     C  CA    . GLU A 1 15  ? 174.155 153.977 170.387 1.00 26478. ? 15  GLU A CA    1 
ATOM   9     C  C     . GLU A 1 15  ? 174.401 154.643 171.750 1.00 26468. ? 15  GLU A C     1 
ATOM   10    O  O     . GLU A 1 15  ? 173.772 154.216 172.742 1.00 26457. ? 15  GLU A O     1 
ATOM   11    C  CB    . GLU A 1 15  ? 172.786 154.358 169.820 1.00 26463. ? 15  GLU A CB    1 
ATOM   12    C  CG    . GLU A 1 15  ? 172.544 155.864 169.769 1.00 26475. ? 15  GLU A CG    1 
ATOM   13    C  CD    . GLU A 1 15  ? 173.309 156.627 168.703 1.00 26476. ? 15  GLU A CD    1 
ATOM   14    O  OE1   . GLU A 1 15  ? 174.037 155.992 167.910 1.00 26467. ? 15  GLU A OE1   1 
ATOM   15    O  OE2   . GLU A 1 15  ? 173.179 157.868 168.672 1.00 26486. ? 15  GLU A OE2   1 
ATOM   16    N  N     . PRO A 1 16  ? 175.287 155.659 171.845 1.00 26616. ? 16  PRO A N     1 
ATOM   17    C  CA    . PRO A 1 16  ? 175.507 156.358 173.103 1.00 26612. ? 16  PRO A CA    1 
ATOM   18    C  C     . PRO A 1 16  ? 174.201 156.908 173.657 1.00 26580. ? 16  PRO A C     1 
ATOM   19    O  O     . PRO A 1 16  ? 173.481 157.605 172.912 1.00 26585. ? 16  PRO A O     1 
ATOM   20    C  CB    . PRO A 1 16  ? 176.501 157.472 172.731 1.00 26622. ? 16  PRO A CB    1 
ATOM   21    C  CG    . PRO A 1 16  ? 176.394 157.579 171.225 1.00 26627. ? 16  PRO A CG    1 
ATOM   22    C  CD    . PRO A 1 16  ? 176.104 156.164 170.758 1.00 26628. ? 16  PRO A CD    1 
ATOM   23    N  N     . LYS A 1 17  ? 173.902 156.603 174.925 1.00 24869. ? 17  LYS A N     1 
ATOM   24    C  CA    . LYS A 1 17  ? 172.664 157.093 175.572 1.00 24844. ? 17  LYS A CA    1 
ATOM   25    C  C     . LYS A 1 17  ? 171.494 156.707 174.663 1.00 24790. ? 17  LYS A C     1 
ATOM   26    O  O     . LYS A 1 17  ? 170.376 157.234 174.853 1.00 24762. ? 17  LYS A O     1 
ATOM   27    C  CB    . LYS A 1 17  ? 172.788 158.606 175.754 1.00 24835. ? 17  LYS A CB    1 
ATOM   28    C  CG    . LYS A 1 17  ? 174.100 159.074 176.362 1.00 24844. ? 17  LYS A CG    1 
ATOM   29    C  CD    . LYS A 1 17  ? 174.278 160.583 176.249 1.00 24840. ? 17  LYS A CD    1 
ATOM   30    C  CE    . LYS A 1 17  ? 174.112 161.056 174.840 1.00 24844. ? 17  LYS A CE    1 
ATOM   31    N  NZ    . LYS A 1 17  ? 175.079 160.434 173.932 1.00 24852. ? 17  LYS A NZ    1 
ATOM   32    N  N     . LEU A 1 18  ? 171.766 155.832 173.697 1.00 23685. ? 18  LEU A N     1 
ATOM   33    C  CA    . LEU A 1 18  ? 170.687 155.366 172.799 1.00 23641. ? 18  LEU A CA    1 
ATOM   34    C  C     . LEU A 1 18  ? 169.917 156.594 172.307 1.00 23586. ? 18  LEU A C     1 
ATOM   35    O  O     . LEU A 1 18  ? 170.560 157.588 171.926 1.00 23621. ? 18  LEU A O     1 
ATOM   36    C  CB    . LEU A 1 18  ? 169.787 154.392 173.551 1.00 23595. ? 18  LEU A CB    1 
ATOM   37    C  CG    . LEU A 1 18  ? 170.383 153.016 173.860 1.00 23624. ? 18  LEU A CG    1 
ATOM   38    C  CD1   . LEU A 1 18  ? 171.390 153.070 174.994 1.00 23639. ? 18  LEU A CD1   1 
ATOM   39    C  CD2   . LEU A 1 18  ? 169.271 152.036 174.185 1.00 23603. ? 18  LEU A CD2   1 
ATOM   40    N  N     . SER A 1 19  ? 168.595 156.511 172.305 1.00 20112. ? 19  SER A N     1 
ATOM   41    C  CA    . SER A 1 19  ? 167.783 157.678 171.917 1.00 19973. ? 19  SER A CA    1 
ATOM   42    C  C     . SER A 1 19  ? 166.871 157.962 173.096 1.00 19968. ? 19  SER A C     1 
ATOM   43    O  O     . SER A 1 19  ? 166.486 156.991 173.769 1.00 20008. ? 19  SER A O     1 
ATOM   44    C  CB    . SER A 1 19  ? 166.972 157.369 170.726 1.00 19794. ? 19  SER A CB    1 
ATOM   45    O  OG    . SER A 1 19  ? 165.923 156.478 171.071 1.00 19841. ? 19  SER A OG    1 
ATOM   46    N  N     . LYS A 1 20  ? 166.517 159.219 173.317 1.00 19641. ? 20  LYS A N     1 
ATOM   47    C  CA    . LYS A 1 20  ? 165.543 159.465 174.406 1.00 19664. ? 20  LYS A CA    1 
ATOM   48    C  C     . LYS A 1 20  ? 164.430 158.406 174.290 1.00 19693. ? 20  LYS A C     1 
ATOM   49    O  O     . LYS A 1 20  ? 164.077 157.796 175.319 1.00 19711. ? 20  LYS A O     1 
ATOM   50    C  CB    . LYS A 1 20  ? 165.004 160.894 174.317 1.00 19592. ? 20  LYS A CB    1 
ATOM   51    C  CG    . LYS A 1 20  ? 164.101 161.299 175.465 1.00 19640. ? 20  LYS A CG    1 
ATOM   52    C  CD    . LYS A 1 20  ? 164.774 161.063 176.810 1.00 19686. ? 20  LYS A CD    1 
ATOM   53    C  CE    . LYS A 1 20  ? 163.839 161.282 177.951 1.00 19680. ? 20  LYS A CE    1 
ATOM   54    N  NZ    . LYS A 1 20  ? 163.291 162.640 177.939 1.00 19717. ? 20  LYS A NZ    1 
ATOM   55    N  N     . ASN A 1 21  ? 163.931 158.166 173.077 1.00 19465. ? 21  ASN A N     1 
ATOM   56    C  CA    . ASN A 1 21  ? 162.839 157.183 172.868 1.00 19454. ? 21  ASN A CA    1 
ATOM   57    C  C     . ASN A 1 21  ? 163.247 155.832 173.446 1.00 19491. ? 21  ASN A C     1 
ATOM   58    O  O     . ASN A 1 21  ? 162.618 155.365 174.406 1.00 19487. ? 21  ASN A O     1 
ATOM   59    C  CB    . ASN A 1 21  ? 162.559 156.962 171.389 1.00 19405. ? 21  ASN A CB    1 
ATOM   60    C  CG    . ASN A 1 21  ? 162.421 158.245 170.608 1.00 19268. ? 21  ASN A CG    1 
ATOM   61    O  OD1   . ASN A 1 21  ? 163.143 158.451 169.627 1.00 19065. ? 21  ASN A OD1   1 
ATOM   62    N  ND2   . ASN A 1 21  ? 161.489 159.099 171.002 1.00 19267. ? 21  ASN A ND2   1 
ATOM   63    N  N     . GLU A 1 22  ? 164.232 155.203 172.824 1.00 19750. ? 22  GLU A N     1 
ATOM   64    C  CA    . GLU A 1 22  ? 164.684 153.889 173.318 1.00 19774. ? 22  GLU A CA    1 
ATOM   65    C  C     . GLU A 1 22  ? 164.747 153.974 174.839 1.00 19778. ? 22  GLU A C     1 
ATOM   66    O  O     . GLU A 1 22  ? 164.098 153.153 175.512 1.00 19779. ? 22  GLU A O     1 
ATOM   67    C  CB    . GLU A 1 22  ? 166.034 153.575 172.685 1.00 19782. ? 22  GLU A CB    1 
ATOM   68    C  CG    . GLU A 1 22  ? 165.957 153.400 171.170 1.00 19756. ? 22  GLU A CG    1 
ATOM   69    C  CD    . GLU A 1 22  ? 165.021 152.323 170.647 1.00 19671. ? 22  GLU A CD    1 
ATOM   70    O  OE1   . GLU A 1 22  ? 164.960 151.238 171.254 1.00 19626. ? 22  GLU A OE1   1 
ATOM   71    O  OE2   . GLU A 1 22  ? 164.344 152.565 169.626 1.00 19595. ? 22  GLU A OE2   1 
ATOM   72    N  N     . LEU A 1 23  ? 165.498 154.945 175.348 1.00 19770. ? 23  LEU A N     1 
ATOM   73    C  CA    . LEU A 1 23  ? 165.649 155.020 176.816 1.00 19770. ? 23  LEU A CA    1 
ATOM   74    C  C     . LEU A 1 23  ? 164.233 155.005 177.381 1.00 19765. ? 23  LEU A C     1 
ATOM   75    O  O     . LEU A 1 23  ? 163.917 154.128 178.206 1.00 19770. ? 23  LEU A O     1 
ATOM   76    C  CB    . LEU A 1 23  ? 166.385 156.283 177.247 1.00 19775. ? 23  LEU A CB    1 
ATOM   77    C  CG    . LEU A 1 23  ? 167.851 156.390 176.822 1.00 19788. ? 23  LEU A CG    1 
ATOM   78    C  CD1   . LEU A 1 23  ? 168.454 157.632 177.448 1.00 19791. ? 23  LEU A CD1   1 
ATOM   79    C  CD2   . LEU A 1 23  ? 168.627 155.153 177.235 1.00 19795. ? 23  LEU A CD2   1 
ATOM   80    N  N     . LYS A 1 24  ? 163.407 155.924 176.898 1.00 19426. ? 24  LYS A N     1 
ATOM   81    C  CA    . LYS A 1 24  ? 162.043 156.011 177.441 1.00 19422. ? 24  LYS A CA    1 
ATOM   82    C  C     . LYS A 1 24  ? 161.424 154.624 177.359 1.00 19429. ? 24  LYS A C     1 
ATOM   83    O  O     . LYS A 1 24  ? 160.990 154.099 178.400 1.00 19429. ? 24  LYS A O     1 
ATOM   84    C  CB    . LYS A 1 24  ? 161.230 156.944 176.553 1.00 19397. ? 24  LYS A CB    1 
ATOM   85    C  CG    . LYS A 1 24  ? 161.403 158.427 176.783 1.00 19358. ? 24  LYS A CG    1 
ATOM   86    C  CD    . LYS A 1 24  ? 160.588 159.180 175.741 1.00 19313. ? 24  LYS A CD    1 
ATOM   87    C  CE    . LYS A 1 24  ? 160.395 160.601 176.126 1.00 19205. ? 24  LYS A CE    1 
ATOM   88    N  NZ    . LYS A 1 24  ? 159.595 161.329 175.140 1.00 19045. ? 24  LYS A NZ    1 
ATOM   89    N  N     . ARG A 1 25  ? 161.433 154.028 176.173 1.00 19608. ? 25  ARG A N     1 
ATOM   90    C  CA    . ARG A 1 25  ? 160.732 152.733 176.019 1.00 19612. ? 25  ARG A CA    1 
ATOM   91    C  C     . ARG A 1 25  ? 161.257 151.768 177.078 1.00 19623. ? 25  ARG A C     1 
ATOM   92    O  O     . ARG A 1 25  ? 160.444 151.041 177.681 1.00 19618. ? 25  ARG A O     1 
ATOM   93    C  CB    . ARG A 1 25  ? 160.973 152.168 174.620 1.00 19610. ? 25  ARG A CB    1 
ATOM   94    C  CG    . ARG A 1 25  ? 160.436 153.057 173.509 1.00 19606. ? 25  ARG A CG    1 
ATOM   95    C  CD    . ARG A 1 25  ? 160.727 152.455 172.149 1.00 19606. ? 25  ARG A CD    1 
ATOM   96    N  NE    . ARG A 1 25  ? 159.964 151.217 171.966 1.00 19578. ? 25  ARG A NE    1 
ATOM   97    C  CZ    . ARG A 1 25  ? 160.503 150.010 171.880 1.00 19392. ? 25  ARG A CZ    1 
ATOM   98    N  NH1   . ARG A 1 25  ? 161.754 149.819 172.255 1.00 19276. ? 25  ARG A NH1   1 
ATOM   99    N  NH2   . ARG A 1 25  ? 159.787 148.997 171.431 1.00 19341. ? 25  ARG A NH2   1 
ATOM   100   N  N     . ARG A 1 26  ? 162.564 151.788 177.310 1.00 20228. ? 26  ARG A N     1 
ATOM   101   C  CA    . ARG A 1 26  ? 163.150 150.806 178.250 1.00 20243. ? 26  ARG A CA    1 
ATOM   102   C  C     . ARG A 1 26  ? 162.492 150.934 179.623 1.00 20238. ? 26  ARG A C     1 
ATOM   103   O  O     . ARG A 1 26  ? 161.984 149.921 180.136 1.00 20245. ? 26  ARG A O     1 
ATOM   104   C  CB    . ARG A 1 26  ? 164.649 151.077 178.353 1.00 20253. ? 26  ARG A CB    1 
ATOM   105   C  CG    . ARG A 1 26  ? 165.401 150.530 177.150 1.00 20257. ? 26  ARG A CG    1 
ATOM   106   C  CD    . ARG A 1 26  ? 165.198 149.026 177.061 1.00 20258. ? 26  ARG A CD    1 
ATOM   107   N  NE    . ARG A 1 26  ? 165.879 148.406 175.919 1.00 20259. ? 26  ARG A NE    1 
ATOM   108   C  CZ    . ARG A 1 26  ? 167.191 148.376 175.724 1.00 20252. ? 26  ARG A CZ    1 
ATOM   109   N  NH1   . ARG A 1 26  ? 167.676 147.892 174.595 1.00 20253. ? 26  ARG A NH1   1 
ATOM   110   N  NH2   . ARG A 1 26  ? 168.017 148.820 176.654 1.00 20246. ? 26  ARG A NH2   1 
ATOM   111   N  N     . LEU A 1 27  ? 162.481 152.136 180.185 1.00 19873. ? 27  LEU A N     1 
ATOM   112   C  CA    . LEU A 1 27  ? 161.950 152.279 181.562 1.00 19872. ? 27  LEU A CA    1 
ATOM   113   C  C     . LEU A 1 27  ? 160.556 151.649 181.653 1.00 19870. ? 27  LEU A C     1 
ATOM   114   O  O     . LEU A 1 27  ? 160.361 150.745 182.479 1.00 19869. ? 27  LEU A O     1 
ATOM   115   C  CB    . LEU A 1 27  ? 161.908 153.759 181.923 1.00 19871. ? 27  LEU A CB    1 
ATOM   116   C  CG    . LEU A 1 27  ? 163.219 154.358 182.440 1.00 19870. ? 27  LEU A CG    1 
ATOM   117   C  CD1   . LEU A 1 27  ? 163.690 153.585 183.656 1.00 19873. ? 27  LEU A CD1   1 
ATOM   118   C  CD2   . LEU A 1 27  ? 164.304 154.395 181.379 1.00 19871. ? 27  LEU A CD2   1 
ATOM   119   N  N     . LYS A 1 28  ? 159.620 152.124 180.838 1.00 19822. ? 28  LYS A N     1 
ATOM   120   C  CA    . LYS A 1 28  ? 158.235 151.612 180.952 1.00 19822. ? 28  LYS A CA    1 
ATOM   121   C  C     . LYS A 1 28  ? 158.331 150.102 181.143 1.00 19824. ? 28  LYS A C     1 
ATOM   122   O  O     . LYS A 1 28  ? 157.778 149.580 182.126 1.00 19823. ? 28  LYS A O     1 
ATOM   123   C  CB    . LYS A 1 28  ? 157.431 151.945 179.695 1.00 19819. ? 28  LYS A CB    1 
ATOM   124   C  CG    . LYS A 1 28  ? 155.929 151.710 179.771 1.00 19821. ? 28  LYS A CG    1 
ATOM   125   C  CD    . LYS A 1 28  ? 155.499 150.251 179.673 1.00 19821. ? 28  LYS A CD    1 
ATOM   126   C  CE    . LYS A 1 28  ? 155.943 149.610 178.398 1.00 19822. ? 28  LYS A CE    1 
ATOM   127   N  NZ    . LYS A 1 28  ? 155.322 150.250 177.236 1.00 19803. ? 28  LYS A NZ    1 
ATOM   128   N  N     . ALA A 1 29  ? 159.012 149.444 180.212 1.00 19808. ? 29  ALA A N     1 
ATOM   129   C  CA    . ALA A 1 29  ? 159.162 147.984 180.330 1.00 19806. ? 29  ALA A CA    1 
ATOM   130   C  C     . ALA A 1 29  ? 159.541 147.670 181.769 1.00 19816. ? 29  ALA A C     1 
ATOM   131   O  O     . ALA A 1 29  ? 158.821 146.941 182.481 1.00 19817. ? 29  ALA A O     1 
ATOM   132   C  CB    . ALA A 1 29  ? 160.241 147.526 179.398 1.00 19804. ? 29  ALA A CB    1 
ATOM   133   N  N     . GLU A 1 30  ? 160.678 148.218 182.178 1.00 20146. ? 30  GLU A N     1 
ATOM   134   C  CA    . GLU A 1 30  ? 161.134 147.948 183.536 1.00 20154. ? 30  GLU A CA    1 
ATOM   135   C  C     . GLU A 1 30  ? 160.002 148.146 184.536 1.00 20154. ? 30  GLU A C     1 
ATOM   136   O  O     . GLU A 1 30  ? 159.770 147.305 185.411 1.00 20162. ? 30  GLU A O     1 
ATOM   137   C  CB    . GLU A 1 30  ? 162.327 148.849 183.868 1.00 20158. ? 30  GLU A CB    1 
ATOM   138   C  CG    . GLU A 1 30  ? 162.611 149.016 185.355 1.00 20162. ? 30  GLU A CG    1 
ATOM   139   C  CD    . GLU A 1 30  ? 161.878 150.195 185.967 1.00 20162. ? 30  GLU A CD    1 
ATOM   140   O  OE1   . GLU A 1 30  ? 161.427 151.078 185.208 1.00 20159. ? 30  GLU A OE1   1 
ATOM   141   O  OE2   . GLU A 1 30  ? 161.748 150.235 187.208 1.00 20166. ? 30  GLU A OE2   1 
ATOM   142   N  N     . LYS A 1 31  ? 159.276 149.258 184.407 1.00 20085. ? 31  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 31  ? 158.152 149.521 185.299 1.00 20091. ? 31  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 31  ? 157.079 148.454 185.140 1.00 20098. ? 31  LYS A C     1 
ATOM   145   O  O     . LYS A 1 31  ? 156.491 147.995 186.125 1.00 20110. ? 31  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 31  ? 157.587 150.919 185.025 1.00 20092. ? 31  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 31  ? 156.589 151.432 186.063 1.00 20098. ? 31  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 31  ? 155.159 151.004 185.754 1.00 20101. ? 31  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 31  ? 154.218 151.330 186.903 1.00 20084. ? 31  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 31  ? 152.861 150.751 186.693 1.00 20061. ? 31  LYS A NZ    1 
ATOM   151   N  N     . LYS A 1 32  ? 156.814 148.045 183.899 1.00 19872. ? 32  LYS A N     1 
ATOM   152   C  CA    . LYS A 1 32  ? 155.820 147.020 183.619 1.00 19875. ? 32  LYS A CA    1 
ATOM   153   C  C     . LYS A 1 32  ? 156.159 145.721 184.335 1.00 19893. ? 32  LYS A C     1 
ATOM   154   O  O     . LYS A 1 32  ? 155.323 145.168 185.057 1.00 19901. ? 32  LYS A O     1 
ATOM   155   C  CB    . LYS A 1 32  ? 155.718 146.776 182.112 1.00 19862. ? 32  LYS A CB    1 
ATOM   156   C  CG    . LYS A 1 32  ? 154.728 145.694 181.721 1.00 19861. ? 32  LYS A CG    1 
ATOM   157   C  CD    . LYS A 1 32  ? 154.603 145.583 180.210 1.00 19858. ? 32  LYS A CD    1 
ATOM   158   C  CE    . LYS A 1 32  ? 155.970 145.553 179.545 1.00 19861. ? 32  LYS A CE    1 
ATOM   159   N  NZ    . LYS A 1 32  ? 155.870 145.575 178.060 1.00 19861. ? 32  LYS A NZ    1 
ATOM   160   N  N     . VAL A 1 33  ? 157.390 145.238 184.155 1.00 20444. ? 33  VAL A N     1 
ATOM   161   C  CA    . VAL A 1 33  ? 157.767 143.956 184.745 1.00 20461. ? 33  VAL A CA    1 
ATOM   162   C  C     . VAL A 1 33  ? 157.826 144.062 186.266 1.00 20479. ? 33  VAL A C     1 
ATOM   163   O  O     . VAL A 1 33  ? 157.450 143.125 186.982 1.00 20500. ? 33  VAL A O     1 
ATOM   164   C  CB    . VAL A 1 33  ? 159.091 143.443 184.144 1.00 20463. ? 33  VAL A CB    1 
ATOM   165   C  CG1   . VAL A 1 33  ? 159.000 143.408 182.627 1.00 20461. ? 33  VAL A CG1   1 
ATOM   166   C  CG2   . VAL A 1 33  ? 160.271 144.296 184.581 1.00 20466. ? 33  VAL A CG2   1 
ATOM   167   N  N     . ALA A 1 34  ? 158.279 145.208 186.784 1.00 20768. ? 34  ALA A N     1 
ATOM   168   C  CA    . ALA A 1 34  ? 158.347 145.399 188.227 1.00 20787. ? 34  ALA A CA    1 
ATOM   169   C  C     . ALA A 1 34  ? 156.959 145.364 188.855 1.00 20806. ? 34  ALA A C     1 
ATOM   170   O  O     . ALA A 1 34  ? 156.730 144.677 189.857 1.00 20816. ? 34  ALA A O     1 
ATOM   171   C  CB    . ALA A 1 34  ? 159.053 146.721 188.543 1.00 20779. ? 34  ALA A CB    1 
ATOM   172   N  N     . GLU A 1 35  ? 156.015 146.097 188.261 1.00 21469. ? 35  GLU A N     1 
ATOM   173   C  CA    . GLU A 1 35  ? 154.646 146.084 188.761 1.00 21488. ? 35  GLU A CA    1 
ATOM   174   C  C     . GLU A 1 35  ? 154.039 144.694 188.638 1.00 21484. ? 35  GLU A C     1 
ATOM   175   O  O     . GLU A 1 35  ? 153.334 144.229 189.542 1.00 21500. ? 35  GLU A O     1 
ATOM   176   C  CB    . GLU A 1 35  ? 153.807 147.119 188.008 1.00 21490. ? 35  GLU A CB    1 
ATOM   177   C  CG    . GLU A 1 35  ? 152.312 147.060 188.295 1.00 21505. ? 35  GLU A CG    1 
ATOM   178   C  CD    . GLU A 1 35  ? 151.575 146.097 187.383 1.00 21510. ? 35  GLU A CD    1 
ATOM   179   O  OE1   . GLU A 1 35  ? 151.668 146.257 186.148 1.00 21508. ? 35  GLU A OE1   1 
ATOM   180   O  OE2   . GLU A 1 35  ? 150.909 145.177 187.902 1.00 21510. ? 35  GLU A OE2   1 
ATOM   181   N  N     . LYS A 1 36  ? 154.307 144.010 187.523 1.00 20811. ? 36  LYS A N     1 
ATOM   182   C  CA    . LYS A 1 36  ? 153.773 142.672 187.316 1.00 20812. ? 36  LYS A CA    1 
ATOM   183   C  C     . LYS A 1 36  ? 154.232 141.715 188.408 1.00 20840. ? 36  LYS A C     1 
ATOM   184   O  O     . LYS A 1 36  ? 153.416 141.020 189.025 1.00 20852. ? 36  LYS A O     1 
ATOM   185   C  CB    . LYS A 1 36  ? 154.190 142.157 185.935 1.00 20796. ? 36  LYS A CB    1 
ATOM   186   C  CG    . LYS A 1 36  ? 153.703 140.752 185.623 1.00 20797. ? 36  LYS A CG    1 
ATOM   187   C  CD    . LYS A 1 36  ? 152.185 140.662 185.663 1.00 20780. ? 36  LYS A CD    1 
ATOM   188   C  CE    . LYS A 1 36  ? 151.540 141.653 184.705 1.00 20727. ? 36  LYS A CE    1 
ATOM   189   N  NZ    . LYS A 1 36  ? 151.924 141.389 183.291 1.00 20675. ? 36  LYS A NZ    1 
ATOM   190   N  N     . GLU A 1 37  ? 155.541 141.677 188.668 1.00 21936. ? 37  GLU A N     1 
ATOM   191   C  CA    . GLU A 1 37  ? 156.056 140.762 189.682 1.00 21961. ? 37  GLU A CA    1 
ATOM   192   C  C     . GLU A 1 37  ? 155.594 141.172 191.075 1.00 21964. ? 37  GLU A C     1 
ATOM   193   O  O     . GLU A 1 37  ? 155.306 140.315 191.919 1.00 21977. ? 37  GLU A O     1 
ATOM   194   C  CB    . GLU A 1 37  ? 157.584 140.684 189.615 1.00 21966. ? 37  GLU A CB    1 
ATOM   195   C  CG    . GLU A 1 37  ? 158.304 142.010 189.766 1.00 21963. ? 37  GLU A CG    1 
ATOM   196   C  CD    . GLU A 1 37  ? 158.661 142.320 191.206 1.00 21974. ? 37  GLU A CD    1 
ATOM   197   O  OE1   . GLU A 1 37  ? 158.469 141.440 192.071 1.00 21982. ? 37  GLU A OE1   1 
ATOM   198   O  OE2   . GLU A 1 37  ? 159.128 143.446 191.474 1.00 21973. ? 37  GLU A OE2   1 
ATOM   199   N  N     . ALA A 1 38  ? 155.514 142.480 191.338 1.00 21784. ? 38  ALA A N     1 
ATOM   200   C  CA    . ALA A 1 38  ? 155.059 142.940 192.643 1.00 21787. ? 38  ALA A CA    1 
ATOM   201   C  C     . ALA A 1 38  ? 153.583 142.658 192.868 1.00 21791. ? 38  ALA A C     1 
ATOM   202   O  O     . ALA A 1 38  ? 153.140 142.605 194.020 1.00 21798. ? 38  ALA A O     1 
ATOM   203   C  CB    . ALA A 1 38  ? 155.335 144.437 192.797 1.00 21786. ? 38  ALA A CB    1 
ATOM   204   N  N     . LYS A 1 39  ? 152.810 142.483 191.798 1.00 21622. ? 39  LYS A N     1 
ATOM   205   C  CA    . LYS A 1 39  ? 151.389 142.194 191.938 1.00 21623. ? 39  LYS A CA    1 
ATOM   206   C  C     . LYS A 1 39  ? 151.110 140.695 192.008 1.00 21643. ? 39  LYS A C     1 
ATOM   207   O  O     . LYS A 1 39  ? 150.440 140.232 192.937 1.00 21654. ? 39  LYS A O     1 
ATOM   208   C  CB    . LYS A 1 39  ? 150.611 142.824 190.779 1.00 21612. ? 39  LYS A CB    1 
ATOM   209   C  CG    . LYS A 1 39  ? 149.140 142.442 190.733 1.00 21614. ? 39  LYS A CG    1 
ATOM   210   C  CD    . LYS A 1 39  ? 148.849 141.467 189.601 1.00 21614. ? 39  LYS A CD    1 
ATOM   211   C  CE    . LYS A 1 39  ? 149.476 141.927 188.296 1.00 21608. ? 39  LYS A CE    1 
ATOM   212   N  NZ    . LYS A 1 39  ? 149.226 140.957 187.194 1.00 21562. ? 39  LYS A NZ    1 
ATOM   213   N  N     . GLN A 1 40  ? 151.607 139.928 191.034 1.00 22587. ? 40  GLN A N     1 
ATOM   214   C  CA    . GLN A 1 40  ? 151.285 138.503 190.988 1.00 22614. ? 40  GLN A CA    1 
ATOM   215   C  C     . GLN A 1 40  ? 151.864 137.757 192.185 1.00 22627. ? 40  GLN A C     1 
ATOM   216   O  O     . GLN A 1 40  ? 151.205 136.876 192.749 1.00 22637. ? 40  GLN A O     1 
ATOM   217   C  CB    . GLN A 1 40  ? 151.768 137.887 189.672 1.00 22619. ? 40  GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 40  ? 153.259 138.007 189.405 1.00 22620. ? 40  GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 40  ? 154.044 136.811 189.896 1.00 22632. ? 40  GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 40  ? 153.539 135.688 189.921 1.00 22637. ? 40  GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 40  ? 155.291 137.044 190.286 1.00 22630. ? 40  GLN A NE2   1 
ATOM   222   N  N     . LYS A 1 41  ? 153.088 138.092 192.591 1.00 22506. ? 41  LYS A N     1 
ATOM   223   C  CA    . LYS A 1 41  ? 153.695 137.439 193.743 1.00 22514. ? 41  LYS A CA    1 
ATOM   224   C  C     . LYS A 1 41  ? 153.259 138.049 195.067 1.00 22523. ? 41  LYS A C     1 
ATOM   225   O  O     . LYS A 1 41  ? 153.590 137.497 196.122 1.00 22522. ? 41  LYS A O     1 
ATOM   226   C  CB    . LYS A 1 41  ? 155.223 137.474 193.631 1.00 22513. ? 41  LYS A CB    1 
ATOM   227   C  CG    . LYS A 1 41  ? 155.949 136.318 194.332 1.00 22514. ? 41  LYS A CG    1 
ATOM   228   C  CD    . LYS A 1 41  ? 155.385 134.928 194.016 1.00 22514. ? 41  LYS A CD    1 
ATOM   229   C  CE    . LYS A 1 41  ? 155.238 134.663 192.521 1.00 22514. ? 41  LYS A CE    1 
ATOM   230   N  NZ    . LYS A 1 41  ? 154.654 133.321 192.250 1.00 22513. ? 41  LYS A NZ    1 
ATOM   231   N  N     . GLU A 1 42  ? 152.529 139.166 195.042 1.00 23064. ? 42  GLU A N     1 
ATOM   232   C  CA    . GLU A 1 42  ? 151.955 139.691 196.275 1.00 23080. ? 42  GLU A CA    1 
ATOM   233   C  C     . GLU A 1 42  ? 150.947 138.717 196.867 1.00 23093. ? 42  GLU A C     1 
ATOM   234   O  O     . GLU A 1 42  ? 150.774 138.666 198.091 1.00 23097. ? 42  GLU A O     1 
ATOM   235   C  CB    . GLU A 1 42  ? 151.302 141.048 196.011 1.00 23076. ? 42  GLU A CB    1 
ATOM   236   C  CG    . GLU A 1 42  ? 150.623 141.670 197.218 1.00 23090. ? 42  GLU A CG    1 
ATOM   237   C  CD    . GLU A 1 42  ? 149.119 141.490 197.193 1.00 23097. ? 42  GLU A CD    1 
ATOM   238   O  OE1   . GLU A 1 42  ? 148.568 141.234 196.102 1.00 23096. ? 42  GLU A OE1   1 
ATOM   239   O  OE2   . GLU A 1 42  ? 148.487 141.602 198.265 1.00 23100. ? 42  GLU A OE2   1 
ATOM   240   N  N     . LEU A 1 43  ? 150.286 137.933 196.022 1.00 23442. ? 43  LEU A N     1 
ATOM   241   C  CA    . LEU A 1 43  ? 149.321 136.941 196.475 1.00 23457. ? 43  LEU A CA    1 
ATOM   242   C  C     . LEU A 1 43  ? 150.011 135.831 197.259 1.00 23462. ? 43  LEU A C     1 
ATOM   243   O  O     . LEU A 1 43  ? 151.131 135.434 196.935 1.00 23457. ? 43  LEU A O     1 
ATOM   244   C  CB    . LEU A 1 43  ? 148.562 136.350 195.284 1.00 23459. ? 43  LEU A CB    1 
ATOM   245   C  CG    . LEU A 1 43  ? 147.265 137.052 194.876 1.00 23463. ? 43  LEU A CG    1 
ATOM   246   C  CD1   . LEU A 1 43  ? 146.342 137.213 196.073 1.00 23469. ? 43  LEU A CD1   1 
ATOM   247   C  CD2   . LEU A 1 43  ? 147.553 138.399 194.225 1.00 23457. ? 43  LEU A CD2   1 
ATOM   248   N  N     . GLU A 1 69  ? 155.291 126.318 181.094 1.00 20821. ? 69  GLU A N     1 
ATOM   249   C  CA    . GLU A 1 69  ? 154.915 127.701 181.361 1.00 20813. ? 69  GLU A CA    1 
ATOM   250   C  C     . GLU A 1 69  ? 153.583 128.037 180.699 1.00 20770. ? 69  GLU A C     1 
ATOM   251   O  O     . GLU A 1 69  ? 153.350 127.690 179.542 1.00 20772. ? 69  GLU A O     1 
ATOM   252   C  CB    . GLU A 1 69  ? 156.006 128.657 180.873 1.00 20822. ? 69  GLU A CB    1 
ATOM   253   C  CG    . GLU A 1 69  ? 155.629 130.127 180.953 1.00 20813. ? 69  GLU A CG    1 
ATOM   254   C  CD    . GLU A 1 69  ? 155.218 130.546 182.350 1.00 20815. ? 69  GLU A CD    1 
ATOM   255   O  OE1   . GLU A 1 69  ? 156.049 130.430 183.275 1.00 20830. ? 69  GLU A OE1   1 
ATOM   256   O  OE2   . GLU A 1 69  ? 154.063 130.989 182.524 1.00 20801. ? 69  GLU A OE2   1 
ATOM   257   N  N     . SER A 1 70  ? 152.710 128.714 181.441 1.00 19002. ? 70  SER A N     1 
ATOM   258   C  CA    . SER A 1 70  ? 151.399 129.076 180.920 1.00 18951. ? 70  SER A CA    1 
ATOM   259   C  C     . SER A 1 70  ? 151.530 130.238 179.944 1.00 18893. ? 70  SER A C     1 
ATOM   260   O  O     . SER A 1 70  ? 151.918 131.345 180.331 1.00 18910. ? 70  SER A O     1 
ATOM   261   C  CB    . SER A 1 70  ? 150.458 129.441 182.065 1.00 18956. ? 70  SER A CB    1 
ATOM   262   O  OG    . SER A 1 70  ? 150.934 130.573 182.773 1.00 18967. ? 70  SER A OG    1 
ATOM   263   N  N     . VAL A 1 71  ? 151.209 129.985 178.680 1.00 15908. ? 71  VAL A N     1 
ATOM   264   C  CA    . VAL A 1 71  ? 151.228 131.028 177.661 1.00 15822. ? 71  VAL A CA    1 
ATOM   265   C  C     . VAL A 1 71  ? 150.013 131.923 177.857 1.00 15750. ? 71  VAL A C     1 
ATOM   266   O  O     . VAL A 1 71  ? 148.939 131.453 178.249 1.00 15770. ? 71  VAL A O     1 
ATOM   267   C  CB    . VAL A 1 71  ? 151.248 130.411 176.254 1.00 15787. ? 71  VAL A CB    1 
ATOM   268   C  CG1   . VAL A 1 71  ? 151.520 131.477 175.206 1.00 15731. ? 71  VAL A CG1   1 
ATOM   269   C  CG2   . VAL A 1 71  ? 152.284 129.306 176.177 1.00 15801. ? 71  VAL A CG2   1 
ATOM   270   N  N     . ASP A 1 72  ? 150.183 133.214 177.600 1.00 14245. ? 72  ASP A N     1 
ATOM   271   C  CA    . ASP A 1 72  ? 149.075 134.147 177.722 1.00 14171. ? 72  ASP A CA    1 
ATOM   272   C  C     . ASP A 1 72  ? 147.974 133.774 176.732 1.00 14137. ? 72  ASP A C     1 
ATOM   273   O  O     . ASP A 1 72  ? 148.276 133.351 175.608 1.00 14149. ? 72  ASP A O     1 
ATOM   274   C  CB    . ASP A 1 72  ? 149.550 135.577 177.474 1.00 14149. ? 72  ASP A CB    1 
ATOM   275   C  CG    . ASP A 1 72  ? 150.920 135.843 178.056 1.00 14173. ? 72  ASP A CG    1 
ATOM   276   O  OD1   . ASP A 1 72  ? 151.137 135.506 179.238 1.00 14194. ? 72  ASP A OD1   1 
ATOM   277   O  OD2   . ASP A 1 72  ? 151.780 136.387 177.332 1.00 14188. ? 72  ASP A OD2   1 
ATOM   278   N  N     . PRO A 1 73  ? 146.703 133.903 177.109 1.00 12769. ? 73  PRO A N     1 
ATOM   279   C  CA    . PRO A 1 73  ? 145.613 133.445 176.238 1.00 12632. ? 73  PRO A CA    1 
ATOM   280   C  C     . PRO A 1 73  ? 145.551 134.142 174.887 1.00 12618. ? 73  PRO A C     1 
ATOM   281   O  O     . PRO A 1 73  ? 145.027 133.571 173.926 1.00 12571. ? 73  PRO A O     1 
ATOM   282   C  CB    . PRO A 1 73  ? 144.366 133.750 177.075 1.00 12451. ? 73  PRO A CB    1 
ATOM   283   C  CG    . PRO A 1 73  ? 144.852 133.671 178.479 1.00 12546. ? 73  PRO A CG    1 
ATOM   284   C  CD    . PRO A 1 73  ? 146.203 134.320 178.428 1.00 12650. ? 73  PRO A CD    1 
ATOM   285   N  N     . ASN A 1 74  ? 146.071 135.369 174.790 1.00 12695. ? 74  ASN A N     1 
ATOM   286   C  CA    . ASN A 1 74  ? 146.017 136.082 173.519 1.00 12707. ? 74  ASN A CA    1 
ATOM   287   C  C     . ASN A 1 74  ? 146.902 135.445 172.458 1.00 12750. ? 74  ASN A C     1 
ATOM   288   O  O     . ASN A 1 74  ? 146.672 135.665 171.265 1.00 12750. ? 74  ASN A O     1 
ATOM   289   C  CB    . ASN A 1 74  ? 146.416 137.546 173.704 1.00 12584. ? 74  ASN A CB    1 
ATOM   290   C  CG    . ASN A 1 74  ? 147.774 137.701 174.346 1.00 12643. ? 74  ASN A CG    1 
ATOM   291   O  OD1   . ASN A 1 74  ? 148.392 136.723 174.759 1.00 12756. ? 74  ASN A OD1   1 
ATOM   292   N  ND2   . ASN A 1 74  ? 148.254 138.935 174.424 1.00 12486. ? 74  ASN A ND2   1 
ATOM   293   N  N     . GLN A 1 75  ? 147.906 134.666 172.861 1.00 12754. ? 75  GLN A N     1 
ATOM   294   C  CA    . GLN A 1 75  ? 148.782 133.970 171.921 1.00 12748. ? 75  GLN A CA    1 
ATOM   295   C  C     . GLN A 1 75  ? 148.106 132.662 171.527 1.00 12735. ? 75  GLN A C     1 
ATOM   296   O  O     . GLN A 1 75  ? 148.541 131.568 171.883 1.00 12742. ? 75  GLN A O     1 
ATOM   297   C  CB    . GLN A 1 75  ? 150.158 133.733 172.535 1.00 12754. ? 75  GLN A CB    1 
ATOM   298   C  CG    . GLN A 1 75  ? 150.790 134.967 173.148 1.00 12779. ? 75  GLN A CG    1 
ATOM   299   C  CD    . GLN A 1 75  ? 151.441 135.860 172.115 1.00 12749. ? 75  GLN A CD    1 
ATOM   300   O  OE1   . GLN A 1 75  ? 151.457 135.543 170.926 1.00 12746. ? 75  GLN A OE1   1 
ATOM   301   N  NE2   . GLN A 1 75  ? 151.980 136.986 172.562 1.00 12733. ? 75  GLN A NE2   1 
ATOM   302   N  N     . TYR A 1 76  ? 147.012 132.789 170.775 1.00 12726. ? 76  TYR A N     1 
ATOM   303   C  CA    . TYR A 1 76  ? 146.276 131.605 170.348 1.00 12716. ? 76  TYR A CA    1 
ATOM   304   C  C     . TYR A 1 76  ? 147.097 130.757 169.390 1.00 12737. ? 76  TYR A C     1 
ATOM   305   O  O     . TYR A 1 76  ? 146.974 129.527 169.384 1.00 12759. ? 76  TYR A O     1 
ATOM   306   C  CB    . TYR A 1 76  ? 144.954 132.007 169.701 1.00 12694. ? 76  TYR A CB    1 
ATOM   307   C  CG    . TYR A 1 76  ? 144.132 130.831 169.232 1.00 12628. ? 76  TYR A CG    1 
ATOM   308   C  CD1   . TYR A 1 76  ? 143.535 129.970 170.139 1.00 12544. ? 76  TYR A CD1   1 
ATOM   309   C  CD2   . TYR A 1 76  ? 143.953 130.581 167.881 1.00 12743. ? 76  TYR A CD2   1 
ATOM   310   C  CE1   . TYR A 1 76  ? 142.785 128.896 169.713 1.00 12583. ? 76  TYR A CE1   1 
ATOM   311   C  CE2   . TYR A 1 76  ? 143.205 129.511 167.448 1.00 12746. ? 76  TYR A CE2   1 
ATOM   312   C  CZ    . TYR A 1 76  ? 142.623 128.672 168.367 1.00 12675. ? 76  TYR A CZ    1 
ATOM   313   O  OH    . TYR A 1 76  ? 141.876 127.604 167.936 1.00 12732. ? 76  TYR A OH    1 
ATOM   314   N  N     . TYR A 1 77  ? 147.932 131.392 168.567 1.00 12736. ? 77  TYR A N     1 
ATOM   315   C  CA    . TYR A 1 77  ? 148.711 130.642 167.588 1.00 12737. ? 77  TYR A CA    1 
ATOM   316   C  C     . TYR A 1 77  ? 149.651 129.656 168.266 1.00 12743. ? 77  TYR A C     1 
ATOM   317   O  O     . TYR A 1 77  ? 149.743 128.494 167.861 1.00 12753. ? 77  TYR A O     1 
ATOM   318   C  CB    . TYR A 1 77  ? 149.493 131.597 166.688 1.00 12736. ? 77  TYR A CB    1 
ATOM   319   C  CG    . TYR A 1 77  ? 150.337 130.878 165.665 1.00 12736. ? 77  TYR A CG    1 
ATOM   320   C  CD1   . TYR A 1 77  ? 149.762 130.305 164.543 1.00 12755. ? 77  TYR A CD1   1 
ATOM   321   C  CD2   . TYR A 1 77  ? 151.710 130.765 165.826 1.00 12749. ? 77  TYR A CD2   1 
ATOM   322   C  CE1   . TYR A 1 77  ? 150.529 129.641 163.610 1.00 12759. ? 77  TYR A CE1   1 
ATOM   323   C  CE2   . TYR A 1 77  ? 152.485 130.104 164.897 1.00 12751. ? 77  TYR A CE2   1 
ATOM   324   C  CZ    . TYR A 1 77  ? 151.889 129.545 163.791 1.00 12750. ? 77  TYR A CZ    1 
ATOM   325   O  OH    . TYR A 1 77  ? 152.659 128.886 162.863 1.00 12761. ? 77  TYR A OH    1 
ATOM   326   N  N     . LYS A 1 78  ? 150.350 130.098 169.312 1.00 12739. ? 78  LYS A N     1 
ATOM   327   C  CA    . LYS A 1 78  ? 151.303 129.221 169.986 1.00 12739. ? 78  LYS A CA    1 
ATOM   328   C  C     . LYS A 1 78  ? 150.597 128.058 170.673 1.00 12741. ? 78  LYS A C     1 
ATOM   329   O  O     . LYS A 1 78  ? 151.030 126.904 170.566 1.00 12756. ? 78  LYS A O     1 
ATOM   330   C  CB    . LYS A 1 78  ? 152.128 130.021 170.991 1.00 12751. ? 78  LYS A CB    1 
ATOM   331   C  CG    . LYS A 1 78  ? 153.243 130.833 170.359 1.00 12748. ? 78  LYS A CG    1 
ATOM   332   C  CD    . LYS A 1 78  ? 153.949 131.703 171.385 1.00 12759. ? 78  LYS A CD    1 
ATOM   333   C  CE    . LYS A 1 78  ? 154.244 130.931 172.660 1.00 12757. ? 78  LYS A CE    1 
ATOM   334   N  NZ    . LYS A 1 78  ? 155.207 129.820 172.428 1.00 12753. ? 78  LYS A NZ    1 
ATOM   335   N  N     . ILE A 1 79  ? 149.503 128.343 171.381 1.00 12735. ? 79  ILE A N     1 
ATOM   336   C  CA    . ILE A 1 79  ? 148.774 127.294 172.090 1.00 12732. ? 79  ILE A CA    1 
ATOM   337   C  C     . ILE A 1 79  ? 148.213 126.279 171.103 1.00 12734. ? 79  ILE A C     1 
ATOM   338   O  O     . ILE A 1 79  ? 148.322 125.062 171.302 1.00 12743. ? 79  ILE A O     1 
ATOM   339   C  CB    . ILE A 1 79  ? 147.659 127.907 172.954 1.00 12739. ? 79  ILE A CB    1 
ATOM   340   C  CG1   . ILE A 1 79  ? 148.217 129.020 173.838 1.00 12768. ? 79  ILE A CG1   1 
ATOM   341   C  CG2   . ILE A 1 79  ? 146.991 126.838 173.797 1.00 12747. ? 79  ILE A CG2   1 
ATOM   342   C  CD1   . ILE A 1 79  ? 147.159 129.748 174.628 1.00 12726. ? 79  ILE A CD1   1 
ATOM   343   N  N     . ARG A 1 80  ? 147.604 126.768 170.023 1.00 12738. ? 80  ARG A N     1 
ATOM   344   C  CA    . ARG A 1 80  ? 147.028 125.870 169.030 1.00 12738. ? 80  ARG A CA    1 
ATOM   345   C  C     . ARG A 1 80  ? 148.107 125.054 168.331 1.00 12743. ? 80  ARG A C     1 
ATOM   346   O  O     . ARG A 1 80  ? 147.918 123.860 168.071 1.00 12758. ? 80  ARG A O     1 
ATOM   347   C  CB    . ARG A 1 80  ? 146.211 126.671 168.020 1.00 12748. ? 80  ARG A CB    1 
ATOM   348   C  CG    . ARG A 1 80  ? 145.280 125.829 167.174 1.00 12749. ? 80  ARG A CG    1 
ATOM   349   C  CD    . ARG A 1 80  ? 144.447 124.898 168.032 1.00 12737. ? 80  ARG A CD    1 
ATOM   350   N  NE    . ARG A 1 80  ? 143.416 124.224 167.254 1.00 12727. ? 80  ARG A NE    1 
ATOM   351   C  CZ    . ARG A 1 80  ? 142.672 123.224 167.705 1.00 12729. ? 80  ARG A CZ    1 
ATOM   352   N  NH1   . ARG A 1 80  ? 142.828 122.745 168.928 1.00 12736. ? 80  ARG A NH1   1 
ATOM   353   N  NH2   . ARG A 1 80  ? 141.753 122.689 166.908 1.00 12745. ? 80  ARG A NH2   1 
ATOM   354   N  N     . SER A 1 81  ? 149.248 125.676 168.020 1.00 12742. ? 81  SER A N     1 
ATOM   355   C  CA    . SER A 1 81  ? 150.333 124.953 167.371 1.00 12739. ? 81  SER A CA    1 
ATOM   356   C  C     . SER A 1 81  ? 150.886 123.861 168.273 1.00 12738. ? 81  SER A C     1 
ATOM   357   O  O     . SER A 1 81  ? 151.151 122.747 167.810 1.00 12745. ? 81  SER A O     1 
ATOM   358   C  CB    . SER A 1 81  ? 151.439 125.927 166.968 1.00 12744. ? 81  SER A CB    1 
ATOM   359   O  OG    . SER A 1 81  ? 150.919 126.988 166.189 1.00 12748. ? 81  SER A OG    1 
ATOM   360   N  N     . GLN A 1 82  ? 151.069 124.155 169.559 1.00 12732. ? 82  GLN A N     1 
ATOM   361   C  CA    . GLN A 1 82  ? 151.514 123.130 170.492 1.00 12727. ? 82  GLN A CA    1 
ATOM   362   C  C     . GLN A 1 82  ? 150.498 122.012 170.664 1.00 12726. ? 82  GLN A C     1 
ATOM   363   O  O     . GLN A 1 82  ? 150.896 120.846 170.749 1.00 12743. ? 82  GLN A O     1 
ATOM   364   C  CB    . GLN A 1 82  ? 151.837 123.750 171.851 1.00 12741. ? 82  GLN A CB    1 
ATOM   365   C  CG    . GLN A 1 82  ? 153.064 124.640 171.839 1.00 12744. ? 82  GLN A CG    1 
ATOM   366   C  CD    . GLN A 1 82  ? 153.225 125.429 173.121 1.00 12747. ? 82  GLN A CD    1 
ATOM   367   O  OE1   . GLN A 1 82  ? 152.424 125.301 174.047 1.00 12757. ? 82  GLN A OE1   1 
ATOM   368   N  NE2   . GLN A 1 82  ? 154.265 126.252 173.182 1.00 12758. ? 82  GLN A NE2   1 
ATOM   369   N  N     . ALA A 1 83  ? 149.204 122.331 170.710 1.00 12722. ? 83  ALA A N     1 
ATOM   370   C  CA    . ALA A 1 83  ? 148.190 121.285 170.765 1.00 12733. ? 83  ALA A CA    1 
ATOM   371   C  C     . ALA A 1 83  ? 148.217 120.404 169.524 1.00 12747. ? 83  ALA A C     1 
ATOM   372   O  O     . ALA A 1 83  ? 148.106 119.178 169.637 1.00 12762. ? 83  ALA A O     1 
ATOM   373   C  CB    . ALA A 1 83  ? 146.803 121.903 170.940 1.00 12745. ? 83  ALA A CB    1 
ATOM   374   N  N     . ILE A 1 84  ? 148.378 121.001 168.343 1.00 12747. ? 84  ILE A N     1 
ATOM   375   C  CA    . ILE A 1 84  ? 148.439 120.216 167.113 1.00 12739. ? 84  ILE A CA    1 
ATOM   376   C  C     . ILE A 1 84  ? 149.695 119.353 167.088 1.00 12746. ? 84  ILE A C     1 
ATOM   377   O  O     . ILE A 1 84  ? 149.664 118.200 166.643 1.00 12760. ? 84  ILE A O     1 
ATOM   378   C  CB    . ILE A 1 84  ? 148.358 121.143 165.888 1.00 12742. ? 84  ILE A CB    1 
ATOM   379   C  CG1   . ILE A 1 84  ? 146.992 121.828 165.830 1.00 12752. ? 84  ILE A CG1   1 
ATOM   380   C  CG2   . ILE A 1 84  ? 148.615 120.370 164.610 1.00 12750. ? 84  ILE A CG2   1 
ATOM   381   C  CD1   . ILE A 1 84  ? 145.835 120.910 166.138 1.00 12759. ? 84  ILE A CD1   1 
ATOM   382   N  N     . HIS A 1 85  ? 150.818 119.893 167.562 1.00 12748. ? 85  HIS A N     1 
ATOM   383   C  CA    . HIS A 1 85  ? 152.046 119.107 167.629 1.00 12741. ? 85  HIS A CA    1 
ATOM   384   C  C     . HIS A 1 85  ? 151.890 117.924 168.576 1.00 12746. ? 85  HIS A C     1 
ATOM   385   O  O     . HIS A 1 85  ? 152.323 116.807 168.265 1.00 12758. ? 85  HIS A O     1 
ATOM   386   C  CB    . HIS A 1 85  ? 153.206 120.001 168.062 1.00 12735. ? 85  HIS A CB    1 
ATOM   387   C  CG    . HIS A 1 85  ? 154.466 119.254 168.366 1.00 12736. ? 85  HIS A CG    1 
ATOM   388   N  ND1   . HIS A 1 85  ? 155.257 118.699 167.385 1.00 12743. ? 85  HIS A ND1   1 
ATOM   389   C  CD2   . HIS A 1 85  ? 155.075 118.977 169.543 1.00 12747. ? 85  HIS A CD2   1 
ATOM   390   C  CE1   . HIS A 1 85  ? 156.298 118.108 167.944 1.00 12751. ? 85  HIS A CE1   1 
ATOM   391   N  NE2   . HIS A 1 85  ? 156.211 118.262 169.252 1.00 12752. ? 85  HIS A NE2   1 
ATOM   392   N  N     . GLN A 1 86  ? 151.266 118.148 169.734 1.00 12745. ? 86  GLN A N     1 
ATOM   393   C  CA    . GLN A 1 86  ? 151.008 117.051 170.657 1.00 12748. ? 86  GLN A CA    1 
ATOM   394   C  C     . GLN A 1 86  ? 150.070 116.020 170.049 1.00 12760. ? 86  GLN A C     1 
ATOM   395   O  O     . GLN A 1 86  ? 150.222 114.820 170.298 1.00 12793. ? 86  GLN A O     1 
ATOM   396   C  CB    . GLN A 1 86  ? 150.434 117.585 171.967 1.00 12749. ? 86  GLN A CB    1 
ATOM   397   C  CG    . GLN A 1 86  ? 150.877 116.803 173.187 1.00 12747. ? 86  GLN A CG    1 
ATOM   398   C  CD    . GLN A 1 86  ? 152.352 116.976 173.482 1.00 12747. ? 86  GLN A CD    1 
ATOM   399   O  OE1   . GLN A 1 86  ? 152.978 117.940 173.040 1.00 12741. ? 86  GLN A OE1   1 
ATOM   400   N  NE2   . GLN A 1 86  ? 152.919 116.037 174.230 1.00 12751. ? 86  GLN A NE2   1 
ATOM   401   N  N     . LEU A 1 87  ? 149.088 116.465 169.264 1.00 12748. ? 87  LEU A N     1 
ATOM   402   C  CA    . LEU A 1 87  ? 148.238 115.522 168.545 1.00 12780. ? 87  LEU A CA    1 
ATOM   403   C  C     . LEU A 1 87  ? 149.051 114.702 167.553 1.00 12792. ? 87  LEU A C     1 
ATOM   404   O  O     . LEU A 1 87  ? 148.807 113.504 167.375 1.00 12846. ? 87  LEU A O     1 
ATOM   405   C  CB    . LEU A 1 87  ? 147.117 116.269 167.827 1.00 12769. ? 87  LEU A CB    1 
ATOM   406   C  CG    . LEU A 1 87  ? 145.981 116.793 168.702 1.00 12754. ? 87  LEU A CG    1 
ATOM   407   C  CD1   . LEU A 1 87  ? 144.909 117.437 167.844 1.00 12744. ? 87  LEU A CD1   1 
ATOM   408   C  CD2   . LEU A 1 87  ? 145.400 115.671 169.538 1.00 12781. ? 87  LEU A CD2   1 
ATOM   409   N  N     . LYS A 1 88  ? 150.010 115.340 166.882 1.00 12764. ? 88  LYS A N     1 
ATOM   410   C  CA    . LYS A 1 88  ? 150.842 114.627 165.919 1.00 12766. ? 88  LYS A CA    1 
ATOM   411   C  C     . LYS A 1 88  ? 151.710 113.575 166.598 1.00 12783. ? 88  LYS A C     1 
ATOM   412   O  O     . LYS A 1 88  ? 151.843 112.455 166.092 1.00 12790. ? 88  LYS A O     1 
ATOM   413   C  CB    . LYS A 1 88  ? 151.719 115.613 165.149 1.00 12755. ? 88  LYS A CB    1 
ATOM   414   C  CG    . LYS A 1 88  ? 150.981 116.448 164.125 1.00 12755. ? 88  LYS A CG    1 
ATOM   415   C  CD    . LYS A 1 88  ? 151.942 117.367 163.397 1.00 12739. ? 88  LYS A CD    1 
ATOM   416   C  CE    . LYS A 1 88  ? 151.206 118.450 162.637 1.00 12731. ? 88  LYS A CE    1 
ATOM   417   N  NZ    . LYS A 1 88  ? 152.139 119.278 161.827 1.00 12735. ? 88  LYS A NZ    1 
ATOM   418   N  N     . VAL A 1 89  ? 152.314 113.914 167.740 1.00 13226. ? 89  VAL A N     1 
ATOM   419   C  CA    . VAL A 1 89  ? 153.302 113.012 168.327 1.00 13239. ? 89  VAL A CA    1 
ATOM   420   C  C     . VAL A 1 89  ? 152.652 111.758 168.903 1.00 13259. ? 89  VAL A C     1 
ATOM   421   O  O     . VAL A 1 89  ? 153.255 110.679 168.878 1.00 13263. ? 89  VAL A O     1 
ATOM   422   C  CB    . VAL A 1 89  ? 154.156 113.741 169.382 1.00 13226. ? 89  VAL A CB    1 
ATOM   423   C  CG1   . VAL A 1 89  ? 154.867 114.929 168.758 1.00 13223. ? 89  VAL A CG1   1 
ATOM   424   C  CG2   . VAL A 1 89  ? 153.313 114.176 170.565 1.00 13241. ? 89  VAL A CG2   1 
ATOM   425   N  N     . ASN A 1 90  ? 151.431 111.858 169.427 1.00 14117. ? 90  ASN A N     1 
ATOM   426   C  CA    . ASN A 1 90  ? 150.809 110.719 170.090 1.00 14156. ? 90  ASN A CA    1 
ATOM   427   C  C     . ASN A 1 90  ? 149.875 109.931 169.178 1.00 14170. ? 90  ASN A C     1 
ATOM   428   O  O     . ASN A 1 90  ? 149.063 109.145 169.674 1.00 14198. ? 90  ASN A O     1 
ATOM   429   C  CB    . ASN A 1 90  ? 150.062 111.171 171.351 1.00 14181. ? 90  ASN A CB    1 
ATOM   430   C  CG    . ASN A 1 90  ? 148.980 112.186 171.064 1.00 14183. ? 90  ASN A CG    1 
ATOM   431   O  OD1   . ASN A 1 90  ? 148.737 112.546 169.916 1.00 14167. ? 90  ASN A OD1   1 
ATOM   432   N  ND2   . ASN A 1 90  ? 148.323 112.660 172.116 1.00 14188. ? 90  ASN A ND2   1 
ATOM   433   N  N     . GLY A 1 91  ? 149.965 110.125 167.863 1.00 13852. ? 91  GLY A N     1 
ATOM   434   C  CA    . GLY A 1 91  ? 149.297 109.281 166.895 1.00 13856. ? 91  GLY A CA    1 
ATOM   435   C  C     . GLY A 1 91  ? 148.043 109.868 166.283 1.00 13867. ? 91  GLY A C     1 
ATOM   436   O  O     . GLY A 1 91  ? 147.588 109.367 165.247 1.00 13851. ? 91  GLY A O     1 
ATOM   437   N  N     . GLU A 1 92  ? 147.468 110.907 166.884 1.00 14750. ? 92  GLU A N     1 
ATOM   438   C  CA    . GLU A 1 92  ? 146.243 111.512 166.358 1.00 14763. ? 92  GLU A CA    1 
ATOM   439   C  C     . GLU A 1 92  ? 146.604 112.628 165.378 1.00 14719. ? 92  GLU A C     1 
ATOM   440   O  O     . GLU A 1 92  ? 146.538 113.820 165.679 1.00 14723. ? 92  GLU A O     1 
ATOM   441   C  CB    . GLU A 1 92  ? 145.371 112.026 167.495 1.00 14778. ? 92  GLU A CB    1 
ATOM   442   C  CG    . GLU A 1 92  ? 144.816 110.936 168.390 1.00 14798. ? 92  GLU A CG    1 
ATOM   443   C  CD    . GLU A 1 92  ? 145.007 111.243 169.860 1.00 14800. ? 92  GLU A CD    1 
ATOM   444   O  OE1   . GLU A 1 92  ? 145.509 112.341 170.177 1.00 14783. ? 92  GLU A OE1   1 
ATOM   445   O  OE2   . GLU A 1 92  ? 144.658 110.386 170.698 1.00 14804. ? 92  GLU A OE2   1 
ATOM   446   N  N     . ASP A 1 93  ? 146.989 112.213 164.178 1.00 12963. ? 93  ASP A N     1 
ATOM   447   C  CA    . ASP A 1 93  ? 147.376 113.175 163.157 1.00 12918. ? 93  ASP A CA    1 
ATOM   448   C  C     . ASP A 1 93  ? 146.149 113.952 162.693 1.00 12894. ? 93  ASP A C     1 
ATOM   449   O  O     . ASP A 1 93  ? 145.178 113.345 162.220 1.00 12890. ? 93  ASP A O     1 
ATOM   450   C  CB    . ASP A 1 93  ? 148.035 112.467 161.974 1.00 12901. ? 93  ASP A CB    1 
ATOM   451   C  CG    . ASP A 1 93  ? 148.458 113.429 160.882 1.00 12887. ? 93  ASP A CG    1 
ATOM   452   O  OD1   . ASP A 1 93  ? 149.311 114.299 161.153 1.00 12874. ? 93  ASP A OD1   1 
ATOM   453   O  OD2   . ASP A 1 93  ? 147.941 113.312 159.752 1.00 12887. ? 93  ASP A OD2   1 
ATOM   454   N  N     . PRO A 1 94  ? 146.148 115.278 162.806 1.00 12751. ? 94  PRO A N     1 
ATOM   455   C  CA    . PRO A 1 94  ? 144.961 116.072 162.463 1.00 12744. ? 94  PRO A CA    1 
ATOM   456   C  C     . PRO A 1 94  ? 144.819 116.424 160.989 1.00 12752. ? 94  PRO A C     1 
ATOM   457   O  O     . PRO A 1 94  ? 144.030 117.317 160.669 1.00 12777. ? 94  PRO A O     1 
ATOM   458   C  CB    . PRO A 1 94  ? 145.179 117.343 163.292 1.00 12752. ? 94  PRO A CB    1 
ATOM   459   C  CG    . PRO A 1 94  ? 146.651 117.506 163.291 1.00 12753. ? 94  PRO A CG    1 
ATOM   460   C  CD    . PRO A 1 94  ? 147.219 116.112 163.376 1.00 12761. ? 94  PRO A CD    1 
ATOM   461   N  N     . TYR A 1 95  ? 145.549 115.763 160.094 1.00 12756. ? 95  TYR A N     1 
ATOM   462   C  CA    . TYR A 1 95  ? 145.489 116.041 158.659 1.00 12746. ? 95  TYR A CA    1 
ATOM   463   C  C     . TYR A 1 95  ? 145.260 114.736 157.910 1.00 12735. ? 95  TYR A C     1 
ATOM   464   O  O     . TYR A 1 95  ? 146.185 114.191 157.293 1.00 12755. ? 95  TYR A O     1 
ATOM   465   C  CB    . TYR A 1 95  ? 146.763 116.735 158.180 1.00 12743. ? 95  TYR A CB    1 
ATOM   466   C  CG    . TYR A 1 95  ? 147.007 118.073 158.832 1.00 12732. ? 95  TYR A CG    1 
ATOM   467   C  CD1   . TYR A 1 95  ? 146.392 119.219 158.357 1.00 12733. ? 95  TYR A CD1   1 
ATOM   468   C  CD2   . TYR A 1 95  ? 147.853 118.189 159.923 1.00 12747. ? 95  TYR A CD2   1 
ATOM   469   C  CE1   . TYR A 1 95  ? 146.611 120.441 158.950 1.00 12727. ? 95  TYR A CE1   1 
ATOM   470   C  CE2   . TYR A 1 95  ? 148.079 119.409 160.522 1.00 12750. ? 95  TYR A CE2   1 
ATOM   471   C  CZ    . TYR A 1 95  ? 147.456 120.531 160.030 1.00 12734. ? 95  TYR A CZ    1 
ATOM   472   O  OH    . TYR A 1 95  ? 147.676 121.751 160.623 1.00 12755. ? 95  TYR A OH    1 
ATOM   473   N  N     . PRO A 1 96  ? 144.041 114.202 157.946 1.00 12711. ? 96  PRO A N     1 
ATOM   474   C  CA    . PRO A 1 96  ? 143.753 112.983 157.187 1.00 12717. ? 96  PRO A CA    1 
ATOM   475   C  C     . PRO A 1 96  ? 143.865 113.223 155.693 1.00 12709. ? 96  PRO A C     1 
ATOM   476   O  O     . PRO A 1 96  ? 143.593 114.316 155.191 1.00 12674. ? 96  PRO A O     1 
ATOM   477   C  CB    . PRO A 1 96  ? 142.313 112.643 157.588 1.00 12741. ? 96  PRO A CB    1 
ATOM   478   C  CG    . PRO A 1 96  ? 142.052 113.435 158.824 1.00 12748. ? 96  PRO A CG    1 
ATOM   479   C  CD    . PRO A 1 96  ? 142.863 114.674 158.686 1.00 12740. ? 96  PRO A CD    1 
ATOM   480   N  N     . HIS A 1 97  ? 144.276 112.177 154.978 1.00 12738. ? 97  HIS A N     1 
ATOM   481   C  CA    . HIS A 1 97  ? 144.491 112.305 153.541 1.00 12744. ? 97  HIS A CA    1 
ATOM   482   C  C     . HIS A 1 97  ? 143.172 112.401 152.786 1.00 12714. ? 97  HIS A C     1 
ATOM   483   O  O     . HIS A 1 97  ? 143.016 113.245 151.897 1.00 12663. ? 97  HIS A O     1 
ATOM   484   C  CB    . HIS A 1 97  ? 145.318 111.128 153.031 1.00 12746. ? 97  HIS A CB    1 
ATOM   485   C  CG    . HIS A 1 97  ? 146.787 111.280 153.262 1.00 12730. ? 97  HIS A CG    1 
ATOM   486   N  ND1   . HIS A 1 97  ? 147.460 110.593 154.249 1.00 12723. ? 97  HIS A ND1   1 
ATOM   487   C  CD2   . HIS A 1 97  ? 147.713 112.043 152.637 1.00 12742. ? 97  HIS A CD2   1 
ATOM   488   C  CE1   . HIS A 1 97  ? 148.737 110.925 154.219 1.00 12748. ? 97  HIS A CE1   1 
ATOM   489   N  NE2   . HIS A 1 97  ? 148.917 111.803 153.250 1.00 12752. ? 97  HIS A NE2   1 
ATOM   490   N  N     . LYS A 1 98  ? 142.209 111.545 153.124 1.00 12728. ? 98  LYS A N     1 
ATOM   491   C  CA    . LYS A 1 98  ? 140.963 111.463 152.374 1.00 12733. ? 98  LYS A CA    1 
ATOM   492   C  C     . LYS A 1 98  ? 139.780 111.361 153.322 1.00 12736. ? 98  LYS A C     1 
ATOM   493   O  O     . LYS A 1 98  ? 139.792 110.548 154.250 1.00 12744. ? 98  LYS A O     1 
ATOM   494   C  CB    . LYS A 1 98  ? 140.972 110.259 151.426 1.00 12741. ? 98  LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 98  ? 139.625 109.958 150.798 1.00 12744. ? 98  LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 98  ? 139.245 111.026 149.790 1.00 12751. ? 98  LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 98  ? 138.174 110.534 148.837 1.00 12746. ? 98  LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 98  ? 137.071 111.518 148.699 1.00 12730. ? 98  LYS A NZ    1 
ATOM   499   N  N     . PHE A 1 99  ? 138.763 112.183 153.079 1.00 12739. ? 99  PHE A N     1 
ATOM   500   C  CA    . PHE A 1 99  ? 137.477 112.076 153.752 1.00 12740. ? 99  PHE A CA    1 
ATOM   501   C  C     . PHE A 1 99  ? 136.397 111.947 152.692 1.00 12745. ? 99  PHE A C     1 
ATOM   502   O  O     . PHE A 1 99  ? 136.318 112.776 151.781 1.00 12763. ? 99  PHE A O     1 
ATOM   503   C  CB    . PHE A 1 99  ? 137.205 113.288 154.646 1.00 12741. ? 99  PHE A CB    1 
ATOM   504   C  CG    . PHE A 1 99  ? 135.892 113.223 155.366 1.00 12739. ? 99  PHE A CG    1 
ATOM   505   C  CD1   . PHE A 1 99  ? 135.690 112.307 156.381 1.00 12745. ? 99  PHE A CD1   1 
ATOM   506   C  CD2   . PHE A 1 99  ? 134.857 114.071 155.022 1.00 12749. ? 99  PHE A CD2   1 
ATOM   507   C  CE1   . PHE A 1 99  ? 134.484 112.241 157.040 1.00 12747. ? 99  PHE A CE1   1 
ATOM   508   C  CE2   . PHE A 1 99  ? 133.649 114.008 155.678 1.00 12747. ? 99  PHE A CE2   1 
ATOM   509   C  CZ    . PHE A 1 99  ? 133.463 113.091 156.688 1.00 12745. ? 99  PHE A CZ    1 
ATOM   510   N  N     . HIS A 1 100 ? 135.571 110.912 152.807 1.00 12735. ? 100 HIS A N     1 
ATOM   511   C  CA    . HIS A 1 100 ? 134.563 110.608 151.796 1.00 12743. ? 100 HIS A CA    1 
ATOM   512   C  C     . HIS A 1 100 ? 133.280 111.359 152.129 1.00 12746. ? 100 HIS A C     1 
ATOM   513   O  O     . HIS A 1 100 ? 132.579 111.012 153.084 1.00 12756. ? 100 HIS A O     1 
ATOM   514   C  CB    . HIS A 1 100 ? 134.315 109.106 151.720 1.00 12740. ? 100 HIS A CB    1 
ATOM   515   C  CG    . HIS A 1 100 ? 133.367 108.707 150.633 1.00 12740. ? 100 HIS A CG    1 
ATOM   516   N  ND1   . HIS A 1 100 ? 133.630 108.930 149.299 1.00 12697. ? 100 HIS A ND1   1 
ATOM   517   C  CD2   . HIS A 1 100 ? 132.156 108.105 150.682 1.00 12746. ? 100 HIS A CD2   1 
ATOM   518   C  CE1   . HIS A 1 100 ? 132.623 108.480 148.573 1.00 12674. ? 100 HIS A CE1   1 
ATOM   519   N  NE2   . HIS A 1 100 ? 131.715 107.974 149.388 1.00 12720. ? 100 HIS A NE2   1 
ATOM   520   N  N     . VAL A 1 101 ? 132.967 112.377 151.337 1.00 12739. ? 101 VAL A N     1 
ATOM   521   C  CA    . VAL A 1 101 ? 131.768 113.182 151.538 1.00 12714. ? 101 VAL A CA    1 
ATOM   522   C  C     . VAL A 1 101 ? 130.630 112.572 150.734 1.00 12679. ? 101 VAL A C     1 
ATOM   523   O  O     . VAL A 1 101 ? 130.751 112.373 149.520 1.00 12627. ? 101 VAL A O     1 
ATOM   524   C  CB    . VAL A 1 101 ? 132.012 114.641 151.127 1.00 12630. ? 101 VAL A CB    1 
ATOM   525   C  CG1   . VAL A 1 101 ? 130.706 115.404 151.100 1.00 12601. ? 101 VAL A CG1   1 
ATOM   526   C  CG2   . VAL A 1 101 ? 132.993 115.298 152.076 1.00 12701. ? 101 VAL A CG2   1 
ATOM   527   N  N     . ASP A 1 102 ? 129.522 112.273 151.410 1.00 12718. ? 102 ASP A N     1 
ATOM   528   C  CA    . ASP A 1 102 ? 128.388 111.651 150.739 1.00 12715. ? 102 ASP A CA    1 
ATOM   529   C  C     . ASP A 1 102 ? 127.512 112.680 150.038 1.00 12694. ? 102 ASP A C     1 
ATOM   530   O  O     . ASP A 1 102 ? 127.047 112.444 148.919 1.00 12692. ? 102 ASP A O     1 
ATOM   531   C  CB    . ASP A 1 102 ? 127.556 110.854 151.742 1.00 12746. ? 102 ASP A CB    1 
ATOM   532   C  CG    . ASP A 1 102 ? 128.084 109.454 151.952 1.00 12755. ? 102 ASP A CG    1 
ATOM   533   O  OD1   . ASP A 1 102 ? 129.209 109.167 151.496 1.00 12767. ? 102 ASP A OD1   1 
ATOM   534   O  OD2   . ASP A 1 102 ? 127.374 108.638 152.576 1.00 12761. ? 102 ASP A OD2   1 
ATOM   535   N  N     . ILE A 1 103 ? 127.276 113.824 150.680 1.00 12699. ? 103 ILE A N     1 
ATOM   536   C  CA    . ILE A 1 103 ? 126.340 114.821 150.183 1.00 12678. ? 103 ILE A CA    1 
ATOM   537   C  C     . ILE A 1 103 ? 126.861 116.206 150.540 1.00 12681. ? 103 ILE A C     1 
ATOM   538   O  O     . ILE A 1 103 ? 127.578 116.393 151.524 1.00 12712. ? 103 ILE A O     1 
ATOM   539   C  CB    . ILE A 1 103 ? 124.922 114.600 150.758 1.00 12734. ? 103 ILE A CB    1 
ATOM   540   C  CG1   . ILE A 1 103 ? 123.878 115.373 149.955 1.00 12744. ? 103 ILE A CG1   1 
ATOM   541   C  CG2   . ILE A 1 103 ? 124.867 114.984 152.226 1.00 12754. ? 103 ILE A CG2   1 
ATOM   542   C  CD1   . ILE A 1 103 ? 122.459 114.991 150.293 1.00 12748. ? 103 ILE A CD1   1 
ATOM   543   N  N     . SER A 1 104 ? 126.512 117.181 149.709 1.00 12640. ? 104 SER A N     1 
ATOM   544   C  CA    . SER A 1 104 ? 126.869 118.563 149.977 1.00 12674. ? 104 SER A CA    1 
ATOM   545   C  C     . SER A 1 104 ? 125.865 119.185 150.942 1.00 12749. ? 104 SER A C     1 
ATOM   546   O  O     . SER A 1 104 ? 124.749 118.697 151.120 1.00 12769. ? 104 SER A O     1 
ATOM   547   C  CB    . SER A 1 104 ? 126.936 119.363 148.679 1.00 12632. ? 104 SER A CB    1 
ATOM   548   O  OG    . SER A 1 104 ? 125.655 119.836 148.307 1.00 12705. ? 104 SER A OG    1 
ATOM   549   N  N     . LEU A 1 105 ? 126.280 120.278 151.581 1.00 12746. ? 105 LEU A N     1 
ATOM   550   C  CA    . LEU A 1 105 ? 125.417 120.961 152.534 1.00 12743. ? 105 LEU A CA    1 
ATOM   551   C  C     . LEU A 1 105 ? 124.154 121.519 151.894 1.00 12742. ? 105 LEU A C     1 
ATOM   552   O  O     . LEU A 1 105 ? 123.079 121.412 152.493 1.00 12751. ? 105 LEU A O     1 
ATOM   553   C  CB    . LEU A 1 105 ? 126.180 122.091 153.226 1.00 12749. ? 105 LEU A CB    1 
ATOM   554   C  CG    . LEU A 1 105 ? 127.331 121.683 154.145 1.00 12749. ? 105 LEU A CG    1 
ATOM   555   C  CD1   . LEU A 1 105 ? 127.853 122.885 154.909 1.00 12741. ? 105 LEU A CD1   1 
ATOM   556   C  CD2   . LEU A 1 105 ? 126.896 120.590 155.101 1.00 12760. ? 105 LEU A CD2   1 
ATOM   557   N  N     . THR A 1 106 ? 124.256 122.103 150.699 1.00 12740. ? 106 THR A N     1 
ATOM   558   C  CA    . THR A 1 106 ? 123.076 122.622 150.018 1.00 12735. ? 106 THR A CA    1 
ATOM   559   C  C     . THR A 1 106 ? 122.078 121.515 149.712 1.00 12740. ? 106 THR A C     1 
ATOM   560   O  O     . THR A 1 106 ? 120.871 121.687 149.920 1.00 12751. ? 106 THR A O     1 
ATOM   561   C  CB    . THR A 1 106 ? 123.484 123.331 148.729 1.00 12736. ? 106 THR A CB    1 
ATOM   562   O  OG1   . THR A 1 106 ? 124.541 124.257 149.006 1.00 12728. ? 106 THR A OG1   1 
ATOM   563   C  CG2   . THR A 1 106 ? 122.305 124.083 148.144 1.00 12748. ? 106 THR A CG2   1 
ATOM   564   N  N     . ASP A 1 107 ? 122.563 120.373 149.226 1.00 12743. ? 107 ASP A N     1 
ATOM   565   C  CA    . ASP A 1 107 ? 121.683 119.241 148.973 1.00 12738. ? 107 ASP A CA    1 
ATOM   566   C  C     . ASP A 1 107 ? 121.082 118.694 150.258 1.00 12737. ? 107 ASP A C     1 
ATOM   567   O  O     . ASP A 1 107 ? 119.924 118.270 150.258 1.00 12764. ? 107 ASP A O     1 
ATOM   568   C  CB    . ASP A 1 107 ? 122.440 118.140 148.233 1.00 12748. ? 107 ASP A CB    1 
ATOM   569   C  CG    . ASP A 1 107 ? 123.040 118.623 146.929 1.00 12718. ? 107 ASP A CG    1 
ATOM   570   O  OD1   . ASP A 1 107 ? 122.277 119.095 146.061 1.00 12673. ? 107 ASP A OD1   1 
ATOM   571   O  OD2   . ASP A 1 107 ? 124.275 118.529 146.770 1.00 12683. ? 107 ASP A OD2   1 
ATOM   572   N  N     . PHE A 1 108 ? 121.844 118.694 151.354 1.00 12733. ? 108 PHE A N     1 
ATOM   573   C  CA    . PHE A 1 108 ? 121.299 118.278 152.643 1.00 12744. ? 108 PHE A CA    1 
ATOM   574   C  C     . PHE A 1 108 ? 120.144 119.179 153.060 1.00 12758. ? 108 PHE A C     1 
ATOM   575   O  O     . PHE A 1 108 ? 119.070 118.699 153.451 1.00 12771. ? 108 PHE A O     1 
ATOM   576   C  CB    . PHE A 1 108 ? 122.409 118.295 153.697 1.00 12740. ? 108 PHE A CB    1 
ATOM   577   C  CG    . PHE A 1 108 ? 122.015 117.693 155.016 1.00 12733. ? 108 PHE A CG    1 
ATOM   578   C  CD1   . PHE A 1 108 ? 121.347 118.443 155.967 1.00 12739. ? 108 PHE A CD1   1 
ATOM   579   C  CD2   . PHE A 1 108 ? 122.332 116.382 155.312 1.00 12739. ? 108 PHE A CD2   1 
ATOM   580   C  CE1   . PHE A 1 108 ? 120.990 117.893 157.178 1.00 12744. ? 108 PHE A CE1   1 
ATOM   581   C  CE2   . PHE A 1 108 ? 121.980 115.828 156.524 1.00 12750. ? 108 PHE A CE2   1 
ATOM   582   C  CZ    . PHE A 1 108 ? 121.308 116.586 157.457 1.00 12755. ? 108 PHE A CZ    1 
ATOM   583   N  N     . ILE A 1 109 ? 120.348 120.495 152.973 1.00 12754. ? 109 ILE A N     1 
ATOM   584   C  CA    . ILE A 1 109 ? 119.298 121.442 153.333 1.00 12736. ? 109 ILE A CA    1 
ATOM   585   C  C     . ILE A 1 109 ? 118.077 121.242 152.448 1.00 12739. ? 109 ILE A C     1 
ATOM   586   O  O     . ILE A 1 109 ? 116.939 121.229 152.929 1.00 12751. ? 109 ILE A O     1 
ATOM   587   C  CB    . ILE A 1 109 ? 119.825 122.885 153.242 1.00 12725. ? 109 ILE A CB    1 
ATOM   588   C  CG1   . ILE A 1 109 ? 121.027 123.081 154.165 1.00 12734. ? 109 ILE A CG1   1 
ATOM   589   C  CG2   . ILE A 1 109 ? 118.725 123.873 153.581 1.00 12743. ? 109 ILE A CG2   1 
ATOM   590   C  CD1   . ILE A 1 109 ? 120.672 123.129 155.627 1.00 12762. ? 109 ILE A CD1   1 
ATOM   591   N  N     . GLN A 1 110 ? 118.295 121.082 151.142 1.00 12738. ? 110 GLN A N     1 
ATOM   592   C  CA    . GLN A 1 110 ? 117.180 120.906 150.218 1.00 12732. ? 110 GLN A CA    1 
ATOM   593   C  C     . GLN A 1 110 ? 116.409 119.623 150.507 1.00 12734. ? 110 GLN A C     1 
ATOM   594   O  O     . GLN A 1 110 ? 115.174 119.608 150.457 1.00 12743. ? 110 GLN A O     1 
ATOM   595   C  CB    . GLN A 1 110 ? 117.695 120.910 148.781 1.00 12739. ? 110 GLN A CB    1 
ATOM   596   C  CG    . GLN A 1 110 ? 116.605 120.877 147.730 1.00 12750. ? 110 GLN A CG    1 
ATOM   597   C  CD    . GLN A 1 110 ? 117.151 121.053 146.328 1.00 12752. ? 110 GLN A CD    1 
ATOM   598   O  OE1   . GLN A 1 110 ? 118.344 121.292 146.140 1.00 12747. ? 110 GLN A OE1   1 
ATOM   599   N  NE2   . GLN A 1 110 ? 116.279 120.936 145.334 1.00 12755. ? 110 GLN A NE2   1 
ATOM   600   N  N     . LYS A 1 111 ? 117.119 118.536 150.811 1.00 12739. ? 111 LYS A N     1 
ATOM   601   C  CA    . LYS A 1 111 ? 116.462 117.246 150.983 1.00 12740. ? 111 LYS A CA    1 
ATOM   602   C  C     . LYS A 1 111 ? 115.707 117.167 152.302 1.00 12739. ? 111 LYS A C     1 
ATOM   603   O  O     . LYS A 1 111 ? 114.595 116.631 152.351 1.00 12746. ? 111 LYS A O     1 
ATOM   604   C  CB    . LYS A 1 111 ? 117.489 116.120 150.898 1.00 12744. ? 111 LYS A CB    1 
ATOM   605   C  CG    . LYS A 1 111 ? 117.937 115.780 149.494 1.00 12744. ? 111 LYS A CG    1 
ATOM   606   C  CD    . LYS A 1 111 ? 118.303 114.310 149.380 1.00 12741. ? 111 LYS A CD    1 
ATOM   607   C  CE    . LYS A 1 111 ? 117.339 113.436 150.166 1.00 12743. ? 111 LYS A CE    1 
ATOM   608   N  NZ    . LYS A 1 111 ? 117.441 112.004 149.777 1.00 12752. ? 111 LYS A NZ    1 
ATOM   609   N  N     . TYR A 1 112 ? 116.291 117.681 153.385 1.00 12736. ? 112 TYR A N     1 
ATOM   610   C  CA    . TYR A 1 112 ? 115.755 117.428 154.717 1.00 12739. ? 112 TYR A CA    1 
ATOM   611   C  C     . TYR A 1 112 ? 115.165 118.671 155.373 1.00 12741. ? 112 TYR A C     1 
ATOM   612   O  O     . TYR A 1 112 ? 115.092 118.739 156.603 1.00 12747. ? 112 TYR A O     1 
ATOM   613   C  CB    . TYR A 1 112 ? 116.836 116.813 155.603 1.00 12751. ? 112 TYR A CB    1 
ATOM   614   C  CG    . TYR A 1 112 ? 117.345 115.501 155.066 1.00 12738. ? 112 TYR A CG    1 
ATOM   615   C  CD1   . TYR A 1 112 ? 116.582 114.349 155.167 1.00 12740. ? 112 TYR A CD1   1 
ATOM   616   C  CD2   . TYR A 1 112 ? 118.575 115.418 154.435 1.00 12742. ? 112 TYR A CD2   1 
ATOM   617   C  CE1   . TYR A 1 112 ? 117.035 113.150 154.669 1.00 12743. ? 112 TYR A CE1   1 
ATOM   618   C  CE2   . TYR A 1 112 ? 119.037 114.224 153.934 1.00 12744. ? 112 TYR A CE2   1 
ATOM   619   C  CZ    . TYR A 1 112 ? 118.263 113.092 154.054 1.00 12744. ? 112 TYR A CZ    1 
ATOM   620   O  OH    . TYR A 1 112 ? 118.719 111.897 153.554 1.00 12759. ? 112 TYR A OH    1 
ATOM   621   N  N     . SER A 1 113 ? 114.725 119.647 154.585 1.00 12738. ? 113 SER A N     1 
ATOM   622   C  CA    . SER A 1 113 ? 114.041 120.802 155.150 1.00 12734. ? 113 SER A CA    1 
ATOM   623   C  C     . SER A 1 113 ? 112.587 120.514 155.493 1.00 12739. ? 113 SER A C     1 
ATOM   624   O  O     . SER A 1 113 ? 111.930 121.367 156.097 1.00 12755. ? 113 SER A O     1 
ATOM   625   C  CB    . SER A 1 113 ? 114.113 121.986 154.186 1.00 12746. ? 113 SER A CB    1 
ATOM   626   O  OG    . SER A 1 113 ? 115.444 122.448 154.050 1.00 12754. ? 113 SER A OG    1 
ATOM   627   N  N     . HIS A 1 114 ? 112.074 119.344 155.127 1.00 12740. ? 114 HIS A N     1 
ATOM   628   C  CA    . HIS A 1 114 ? 110.683 118.986 155.357 1.00 12749. ? 114 HIS A CA    1 
ATOM   629   C  C     . HIS A 1 114 ? 110.460 118.273 156.683 1.00 12747. ? 114 HIS A C     1 
ATOM   630   O  O     . HIS A 1 114 ? 109.330 117.861 156.965 1.00 12755. ? 114 HIS A O     1 
ATOM   631   C  CB    . HIS A 1 114 ? 110.176 118.103 154.216 1.00 12753. ? 114 HIS A CB    1 
ATOM   632   C  CG    . HIS A 1 114 ? 110.732 116.715 154.239 1.00 12744. ? 114 HIS A CG    1 
ATOM   633   N  ND1   . HIS A 1 114 ? 111.985 116.408 153.755 1.00 12743. ? 114 HIS A ND1   1 
ATOM   634   C  CD2   . HIS A 1 114 ? 110.209 115.552 154.693 1.00 12744. ? 114 HIS A CD2   1 
ATOM   635   C  CE1   . HIS A 1 114 ? 112.209 115.115 153.907 1.00 12742. ? 114 HIS A CE1   1 
ATOM   636   N  NE2   . HIS A 1 114 ? 111.147 114.572 154.473 1.00 12742. ? 114 HIS A NE2   1 
ATOM   637   N  N     . LEU A 1 115 ? 111.499 118.108 157.495 1.00 12752. ? 115 LEU A N     1 
ATOM   638   C  CA    . LEU A 1 115 ? 111.364 117.404 158.761 1.00 12760. ? 115 LEU A CA    1 
ATOM   639   C  C     . LEU A 1 115 ? 110.689 118.287 159.801 1.00 12766. ? 115 LEU A C     1 
ATOM   640   O  O     . LEU A 1 115 ? 110.933 119.494 159.867 1.00 12760. ? 115 LEU A O     1 
ATOM   641   C  CB    . LEU A 1 115 ? 112.733 116.955 159.270 1.00 12758. ? 115 LEU A CB    1 
ATOM   642   C  CG    . LEU A 1 115 ? 113.417 115.838 158.484 1.00 12742. ? 115 LEU A CG    1 
ATOM   643   C  CD1   . LEU A 1 115 ? 114.792 115.560 159.055 1.00 12749. ? 115 LEU A CD1   1 
ATOM   644   C  CD2   . LEU A 1 115 ? 112.566 114.583 158.497 1.00 12749. ? 115 LEU A CD2   1 
ATOM   645   N  N     . GLN A 1 116 ? 109.830 117.676 160.609 1.00 12914. ? 116 GLN A N     1 
ATOM   646   C  CA    . GLN A 1 116 ? 109.194 118.365 161.717 1.00 12917. ? 116 GLN A CA    1 
ATOM   647   C  C     . GLN A 1 116 ? 110.158 118.474 162.893 1.00 12926. ? 116 GLN A C     1 
ATOM   648   O  O     . GLN A 1 116 ? 111.129 117.719 162.981 1.00 12940. ? 116 GLN A O     1 
ATOM   649   C  CB    . GLN A 1 116 ? 107.931 117.622 162.137 1.00 12920. ? 116 GLN A CB    1 
ATOM   650   C  CG    . GLN A 1 116 ? 107.061 117.186 160.977 1.00 12916. ? 116 GLN A CG    1 
ATOM   651   C  CD    . GLN A 1 116 ? 106.002 118.210 160.633 1.00 12910. ? 116 GLN A CD    1 
ATOM   652   O  OE1   . GLN A 1 116 ? 105.996 118.770 159.538 1.00 12916. ? 116 GLN A OE1   1 
ATOM   653   N  NE2   . GLN A 1 116 ? 105.098 118.462 161.571 1.00 12908. ? 116 GLN A NE2   1 
ATOM   654   N  N     . PRO A 1 117 ? 109.925 119.419 163.803 1.00 13109. ? 117 PRO A N     1 
ATOM   655   C  CA    . PRO A 1 117 ? 110.777 119.512 164.994 1.00 13114. ? 117 PRO A CA    1 
ATOM   656   C  C     . PRO A 1 117 ? 110.740 118.226 165.805 1.00 13116. ? 117 PRO A C     1 
ATOM   657   O  O     . PRO A 1 117 ? 109.696 117.587 165.946 1.00 13124. ? 117 PRO A O     1 
ATOM   658   C  CB    . PRO A 1 117 ? 110.174 120.686 165.770 1.00 13122. ? 117 PRO A CB    1 
ATOM   659   C  CG    . PRO A 1 117 ? 109.495 121.506 164.737 1.00 13124. ? 117 PRO A CG    1 
ATOM   660   C  CD    . PRO A 1 117 ? 108.972 120.539 163.721 1.00 13119. ? 117 PRO A CD    1 
ATOM   661   N  N     . GLY A 1 118 ? 111.898 117.850 166.339 1.00 12779. ? 118 GLY A N     1 
ATOM   662   C  CA    . GLY A 1 118 ? 112.024 116.635 167.113 1.00 12771. ? 118 GLY A CA    1 
ATOM   663   C  C     . GLY A 1 118 ? 112.255 115.376 166.309 1.00 12770. ? 118 GLY A C     1 
ATOM   664   O  O     . GLY A 1 118 ? 112.387 114.300 166.904 1.00 12766. ? 118 GLY A O     1 
ATOM   665   N  N     . ASP A 1 119 ? 112.305 115.468 164.984 1.00 13536. ? 119 ASP A N     1 
ATOM   666   C  CA    . ASP A 1 119 ? 112.512 114.287 164.159 1.00 13559. ? 119 ASP A CA    1 
ATOM   667   C  C     . ASP A 1 119 ? 113.965 113.832 164.221 1.00 13545. ? 119 ASP A C     1 
ATOM   668   O  O     . ASP A 1 119 ? 114.877 114.619 164.483 1.00 13555. ? 119 ASP A O     1 
ATOM   669   C  CB    . ASP A 1 119 ? 112.114 114.569 162.712 1.00 13573. ? 119 ASP A CB    1 
ATOM   670   C  CG    . ASP A 1 119 ? 110.618 114.732 162.542 1.00 13588. ? 119 ASP A CG    1 
ATOM   671   O  OD1   . ASP A 1 119 ? 109.870 114.359 163.469 1.00 13600. ? 119 ASP A OD1   1 
ATOM   672   O  OD2   . ASP A 1 119 ? 110.190 115.237 161.483 1.00 13584. ? 119 ASP A OD2   1 
ATOM   673   N  N     . HIS A 1 120 ? 114.173 112.539 163.974 1.00 12766. ? 120 HIS A N     1 
ATOM   674   C  CA    . HIS A 1 120 ? 115.515 111.959 164.001 1.00 12750. ? 120 HIS A CA    1 
ATOM   675   C  C     . HIS A 1 120 ? 115.498 110.721 163.109 1.00 12753. ? 120 HIS A C     1 
ATOM   676   O  O     . HIS A 1 120 ? 115.005 109.667 163.518 1.00 12767. ? 120 HIS A O     1 
ATOM   677   C  CB    . HIS A 1 120 ? 115.935 111.622 165.425 1.00 12756. ? 120 HIS A CB    1 
ATOM   678   C  CG    . HIS A 1 120 ? 117.349 111.149 165.542 1.00 12753. ? 120 HIS A CG    1 
ATOM   679   N  ND1   . HIS A 1 120 ? 118.358 111.610 164.726 1.00 12747. ? 120 HIS A ND1   1 
ATOM   680   C  CD2   . HIS A 1 120 ? 117.924 110.259 166.384 1.00 12760. ? 120 HIS A CD2   1 
ATOM   681   C  CE1   . HIS A 1 120 ? 119.493 111.022 165.057 1.00 12747. ? 120 HIS A CE1   1 
ATOM   682   N  NE2   . HIS A 1 120 ? 119.257 110.197 166.060 1.00 12754. ? 120 HIS A NE2   1 
ATOM   683   N  N     . LEU A 1 121 ? 116.037 110.857 161.897 1.00 12746. ? 121 LEU A N     1 
ATOM   684   C  CA    . LEU A 1 121 ? 116.048 109.769 160.919 1.00 12752. ? 121 LEU A CA    1 
ATOM   685   C  C     . LEU A 1 121 ? 117.182 108.809 161.266 1.00 12786. ? 121 LEU A C     1 
ATOM   686   O  O     . LEU A 1 121 ? 118.283 108.862 160.715 1.00 12788. ? 121 LEU A O     1 
ATOM   687   C  CB    . LEU A 1 121 ? 116.193 110.319 159.508 1.00 12747. ? 121 LEU A CB    1 
ATOM   688   C  CG    . LEU A 1 121 ? 115.030 111.169 158.999 1.00 12743. ? 121 LEU A CG    1 
ATOM   689   C  CD1   . LEU A 1 121 ? 115.268 111.587 157.561 1.00 12742. ? 121 LEU A CD1   1 
ATOM   690   C  CD2   . LEU A 1 121 ? 113.725 110.407 159.128 1.00 12754. ? 121 LEU A CD2   1 
ATOM   691   N  N     . THR A 1 122 ? 116.890 107.897 162.195 1.00 13609. ? 122 THR A N     1 
ATOM   692   C  CA    . THR A 1 122 ? 117.912 106.987 162.699 1.00 13632. ? 122 THR A CA    1 
ATOM   693   C  C     . THR A 1 122 ? 118.394 105.994 161.650 1.00 13654. ? 122 THR A C     1 
ATOM   694   O  O     . THR A 1 122 ? 119.439 105.367 161.847 1.00 13665. ? 122 THR A O     1 
ATOM   695   C  CB    . THR A 1 122 ? 117.383 106.222 163.912 1.00 13657. ? 122 THR A CB    1 
ATOM   696   O  OG1   . THR A 1 122 ? 116.212 105.487 163.539 1.00 13668. ? 122 THR A OG1   1 
ATOM   697   C  CG2   . THR A 1 122 ? 117.030 107.182 165.032 1.00 13652. ? 122 THR A CG2   1 
ATOM   698   N  N     . ASP A 1 123 ? 117.659 105.855 160.540 1.00 13901. ? 123 ASP A N     1 
ATOM   699   C  CA    . ASP A 1 123 ? 118.007 104.818 159.522 1.00 13912. ? 123 ASP A CA    1 
ATOM   700   C  C     . ASP A 1 123 ? 118.751 105.431 158.329 1.00 13892. ? 123 ASP A C     1 
ATOM   701   O  O     . ASP A 1 123 ? 118.999 104.691 157.353 1.00 13909. ? 123 ASP A O     1 
ATOM   702   C  CB    . ASP A 1 123 ? 116.766 104.061 159.077 1.00 13926. ? 123 ASP A CB    1 
ATOM   703   C  CG    . ASP A 1 123 ? 115.580 104.930 158.682 1.00 13927. ? 123 ASP A CG    1 
ATOM   704   O  OD1   . ASP A 1 123 ? 115.723 105.720 157.725 1.00 13925. ? 123 ASP A OD1   1 
ATOM   705   O  OD2   . ASP A 1 123 ? 114.525 104.814 159.340 1.00 13937. ? 123 ASP A OD2   1 
ATOM   706   N  N     . ILE A 1 124 ? 119.091 106.719 158.396 1.00 12969. ? 124 ILE A N     1 
ATOM   707   C  CA    . ILE A 1 124 ? 119.801 107.391 157.315 1.00 12932. ? 124 ILE A CA    1 
ATOM   708   C  C     . ILE A 1 124 ? 121.136 107.883 157.851 1.00 12918. ? 124 ILE A C     1 
ATOM   709   O  O     . ILE A 1 124 ? 121.179 108.603 158.855 1.00 12936. ? 124 ILE A O     1 
ATOM   710   C  CB    . ILE A 1 124 ? 118.985 108.562 156.738 1.00 12920. ? 124 ILE A CB    1 
ATOM   711   C  CG1   . ILE A 1 124 ? 117.639 108.064 156.208 1.00 12928. ? 124 ILE A CG1   1 
ATOM   712   C  CG2   . ILE A 1 124 ? 119.778 109.282 155.660 1.00 12911. ? 124 ILE A CG2   1 
ATOM   713   C  CD1   . ILE A 1 124 ? 117.636 107.739 154.732 1.00 12929. ? 124 ILE A CD1   1 
ATOM   714   N  N     . THR A 1 125 ? 122.220 107.497 157.186 1.00 12745. ? 125 THR A N     1 
ATOM   715   C  CA    . THR A 1 125 ? 123.563 107.916 157.556 1.00 12741. ? 125 THR A CA    1 
ATOM   716   C  C     . THR A 1 125 ? 124.178 108.688 156.400 1.00 12737. ? 125 THR A C     1 
ATOM   717   O  O     . THR A 1 125 ? 124.171 108.214 155.259 1.00 12750. ? 125 THR A O     1 
ATOM   718   C  CB    . THR A 1 125 ? 124.440 106.715 157.916 1.00 12748. ? 125 THR A CB    1 
ATOM   719   O  OG1   . THR A 1 125 ? 123.714 105.833 158.780 1.00 12761. ? 125 THR A OG1   1 
ATOM   720   C  CG2   . THR A 1 125 ? 125.705 107.175 158.622 1.00 12755. ? 125 THR A CG2   1 
ATOM   721   N  N     . LEU A 1 126 ? 124.704 109.873 156.695 1.00 12728. ? 126 LEU A N     1 
ATOM   722   C  CA    . LEU A 1 126 ? 125.306 110.726 155.684 1.00 12728. ? 126 LEU A CA    1 
ATOM   723   C  C     . LEU A 1 126 ? 126.613 111.290 156.215 1.00 12733. ? 126 LEU A C     1 
ATOM   724   O  O     . LEU A 1 126 ? 126.837 111.367 157.425 1.00 12749. ? 126 LEU A O     1 
ATOM   725   C  CB    . LEU A 1 126 ? 124.370 111.868 155.273 1.00 12742. ? 126 LEU A CB    1 
ATOM   726   C  CG    . LEU A 1 126 ? 123.006 111.466 154.715 1.00 12750. ? 126 LEU A CG    1 
ATOM   727   C  CD1   . LEU A 1 126 ? 121.962 112.497 155.089 1.00 12752. ? 126 LEU A CD1   1 
ATOM   728   C  CD2   . LEU A 1 126 ? 123.078 111.295 153.210 1.00 12755. ? 126 LEU A CD2   1 
ATOM   729   N  N     . LYS A 1 127 ? 127.479 111.688 155.286 1.00 12741. ? 127 LYS A N     1 
ATOM   730   C  CA    . LYS A 1 127 ? 128.779 112.263 155.610 1.00 12741. ? 127 LYS A CA    1 
ATOM   731   C  C     . LYS A 1 127 ? 128.881 113.628 154.947 1.00 12732. ? 127 LYS A C     1 
ATOM   732   O  O     . LYS A 1 127 ? 128.786 113.734 153.721 1.00 12749. ? 127 LYS A O     1 
ATOM   733   C  CB    . LYS A 1 127 ? 129.913 111.349 155.151 1.00 12748. ? 127 LYS A CB    1 
ATOM   734   C  CG    . LYS A 1 127 ? 130.302 110.294 156.166 1.00 12742. ? 127 LYS A CG    1 
ATOM   735   C  CD    . LYS A 1 127 ? 131.767 109.931 156.051 1.00 12738. ? 127 LYS A CD    1 
ATOM   736   C  CE    . LYS A 1 127 ? 131.948 108.637 155.284 1.00 12741. ? 127 LYS A CE    1 
ATOM   737   N  NZ    . LYS A 1 127 ? 131.936 107.456 156.187 1.00 12754. ? 127 LYS A NZ    1 
ATOM   738   N  N     . VAL A 1 128 ? 129.074 114.667 155.753 1.00 12722. ? 128 VAL A N     1 
ATOM   739   C  CA    . VAL A 1 128 ? 129.231 116.030 155.270 1.00 12726. ? 128 VAL A CA    1 
ATOM   740   C  C     . VAL A 1 128 ? 130.546 116.575 155.812 1.00 12738. ? 128 VAL A C     1 
ATOM   741   O  O     . VAL A 1 128 ? 131.217 115.940 156.620 1.00 12757. ? 128 VAL A O     1 
ATOM   742   C  CB    . VAL A 1 128 ? 128.053 116.936 155.676 1.00 12731. ? 128 VAL A CB    1 
ATOM   743   C  CG1   . VAL A 1 128 ? 126.761 116.431 155.066 1.00 12749. ? 128 VAL A CG1   1 
ATOM   744   C  CG2   . VAL A 1 128 ? 127.936 117.003 157.186 1.00 12740. ? 128 VAL A CG2   1 
ATOM   745   N  N     . ALA A 1 129 ? 130.910 117.769 155.355 1.00 12736. ? 129 ALA A N     1 
ATOM   746   C  CA    . ALA A 1 129 ? 132.134 118.402 155.821 1.00 12739. ? 129 ALA A CA    1 
ATOM   747   C  C     . ALA A 1 129 ? 131.994 119.910 155.718 1.00 12737. ? 129 ALA A C     1 
ATOM   748   O  O     . ALA A 1 129 ? 131.280 120.423 154.854 1.00 12745. ? 129 ALA A O     1 
ATOM   749   C  CB    . ALA A 1 129 ? 133.350 117.929 155.022 1.00 12755. ? 129 ALA A CB    1 
ATOM   750   N  N     . GLY A 1 130 ? 132.687 120.616 156.602 1.00 12740. ? 130 GLY A N     1 
ATOM   751   C  CA    . GLY A 1 130 ? 132.640 122.066 156.567 1.00 12733. ? 130 GLY A CA    1 
ATOM   752   C  C     . GLY A 1 130 ? 133.451 122.667 157.691 1.00 12725. ? 130 GLY A C     1 
ATOM   753   O  O     . GLY A 1 130 ? 134.046 121.961 158.508 1.00 12753. ? 130 GLY A O     1 
ATOM   754   N  N     . ARG A 1 131 ? 133.449 123.995 157.729 1.00 12714. ? 131 ARG A N     1 
ATOM   755   C  CA    . ARG A 1 131 ? 134.216 124.757 158.704 1.00 12724. ? 131 ARG A CA    1 
ATOM   756   C  C     . ARG A 1 131 ? 133.332 125.157 159.878 1.00 12729. ? 131 ARG A C     1 
ATOM   757   O  O     . ARG A 1 131 ? 132.193 125.594 159.691 1.00 12769. ? 131 ARG A O     1 
ATOM   758   C  CB    . ARG A 1 131 ? 134.820 126.004 158.058 1.00 12736. ? 131 ARG A CB    1 
ATOM   759   C  CG    . ARG A 1 131 ? 135.792 126.753 158.944 1.00 12748. ? 131 ARG A CG    1 
ATOM   760   C  CD    . ARG A 1 131 ? 136.261 128.037 158.288 1.00 12733. ? 131 ARG A CD    1 
ATOM   761   N  NE    . ARG A 1 131 ? 137.116 127.780 157.137 1.00 12714. ? 131 ARG A NE    1 
ATOM   762   C  CZ    . ARG A 1 131 ? 138.418 127.545 157.207 1.00 12669. ? 131 ARG A CZ    1 
ATOM   763   N  NH1   . ARG A 1 131 ? 139.054 127.520 158.365 1.00 12659. ? 131 ARG A NH1   1 
ATOM   764   N  NH2   . ARG A 1 131 ? 139.099 127.328 156.086 1.00 12647. ? 131 ARG A NH2   1 
ATOM   765   N  N     . ILE A 1 132 ? 133.863 125.005 161.087 1.00 12721. ? 132 ILE A N     1 
ATOM   766   C  CA    . ILE A 1 132 ? 133.131 125.352 162.300 1.00 12719. ? 132 ILE A CA    1 
ATOM   767   C  C     . ILE A 1 132 ? 133.139 126.863 162.469 1.00 12725. ? 132 ILE A C     1 
ATOM   768   O  O     . ILE A 1 132 ? 134.200 127.496 162.448 1.00 12746. ? 132 ILE A O     1 
ATOM   769   C  CB    . ILE A 1 132 ? 133.750 124.665 163.526 1.00 12735. ? 132 ILE A CB    1 
ATOM   770   C  CG1   . ILE A 1 132 ? 133.644 123.148 163.407 1.00 12757. ? 132 ILE A CG1   1 
ATOM   771   C  CG2   . ILE A 1 132 ? 133.071 125.140 164.795 1.00 12754. ? 132 ILE A CG2   1 
ATOM   772   C  CD1   . ILE A 1 132 ? 134.254 122.417 164.577 1.00 12774. ? 132 ILE A CD1   1 
ATOM   773   N  N     . HIS A 1 133 ? 131.955 127.448 162.646 1.00 12729. ? 133 HIS A N     1 
ATOM   774   C  CA    . HIS A 1 133 ? 131.840 128.880 162.869 1.00 12733. ? 133 HIS A CA    1 
ATOM   775   C  C     . HIS A 1 133 ? 131.296 129.253 164.236 1.00 12737. ? 133 HIS A C     1 
ATOM   776   O  O     . HIS A 1 133 ? 131.420 130.416 164.629 1.00 12753. ? 133 HIS A O     1 
ATOM   777   C  CB    . HIS A 1 133 ? 130.956 129.524 161.792 1.00 12745. ? 133 HIS A CB    1 
ATOM   778   C  CG    . HIS A 1 133 ? 131.726 130.056 160.626 1.00 12735. ? 133 HIS A CG    1 
ATOM   779   N  ND1   . HIS A 1 133 ? 132.074 129.275 159.546 1.00 12743. ? 133 HIS A ND1   1 
ATOM   780   C  CD2   . HIS A 1 133 ? 132.224 131.289 160.374 1.00 12742. ? 133 HIS A CD2   1 
ATOM   781   C  CE1   . HIS A 1 133 ? 132.748 130.005 158.676 1.00 12747. ? 133 HIS A CE1   1 
ATOM   782   N  NE2   . HIS A 1 133 ? 132.853 131.230 159.155 1.00 12748. ? 133 HIS A NE2   1 
ATOM   783   N  N     . ALA A 1 134 ? 130.699 128.316 164.966 1.00 12722. ? 134 ALA A N     1 
ATOM   784   C  CA    . ALA A 1 134 ? 130.234 128.583 166.316 1.00 12721. ? 134 ALA A CA    1 
ATOM   785   C  C     . ALA A 1 134 ? 130.314 127.299 167.123 1.00 12728. ? 134 ALA A C     1 
ATOM   786   O  O     . ALA A 1 134 ? 130.247 126.198 166.571 1.00 12733. ? 134 ALA A O     1 
ATOM   787   C  CB    . ALA A 1 134 ? 128.805 129.132 166.326 1.00 12697. ? 134 ALA A CB    1 
ATOM   788   N  N     . LYS A 1 135 ? 130.465 127.451 168.437 1.00 12740. ? 135 LYS A N     1 
ATOM   789   C  CA    . LYS A 1 135 ? 130.541 126.316 169.360 1.00 12744. ? 135 LYS A CA    1 
ATOM   790   C  C     . LYS A 1 135 ? 129.814 126.723 170.640 1.00 12736. ? 135 LYS A C     1 
ATOM   791   O  O     . LYS A 1 135 ? 130.408 127.314 171.544 1.00 12741. ? 135 LYS A O     1 
ATOM   792   C  CB    . LYS A 1 135 ? 131.985 125.919 169.629 1.00 12753. ? 135 LYS A CB    1 
ATOM   793   C  CG    . LYS A 1 135 ? 132.143 124.624 170.403 1.00 12742. ? 135 LYS A CG    1 
ATOM   794   C  CD    . LYS A 1 135 ? 133.597 124.375 170.758 1.00 12745. ? 135 LYS A CD    1 
ATOM   795   C  CE    . LYS A 1 135 ? 133.761 123.093 171.552 1.00 12751. ? 135 LYS A CE    1 
ATOM   796   N  NZ    . LYS A 1 135 ? 135.150 122.938 172.060 1.00 12751. ? 135 LYS A NZ    1 
ATOM   797   N  N     . ARG A 1 136 ? 128.527 126.402 170.706 1.00 12736. ? 136 ARG A N     1 
ATOM   798   C  CA    . ARG A 1 136 ? 127.695 126.711 171.866 1.00 12701. ? 136 ARG A CA    1 
ATOM   799   C  C     . ARG A 1 136 ? 127.627 125.462 172.734 1.00 12705. ? 136 ARG A C     1 
ATOM   800   O  O     . ARG A 1 136 ? 127.011 124.464 172.356 1.00 12743. ? 136 ARG A O     1 
ATOM   801   C  CB    . ARG A 1 136 ? 126.307 127.170 171.434 1.00 12616. ? 136 ARG A CB    1 
ATOM   802   C  CG    . ARG A 1 136 ? 126.308 128.267 170.388 1.00 12553. ? 136 ARG A CG    1 
ATOM   803   C  CD    . ARG A 1 136 ? 124.898 128.586 169.929 1.00 12385. ? 136 ARG A CD    1 
ATOM   804   N  NE    . ARG A 1 136 ? 124.392 127.600 168.983 1.00 12435. ? 136 ARG A NE    1 
ATOM   805   C  CZ    . ARG A 1 136 ? 124.662 127.601 167.686 1.00 12560. ? 136 ARG A CZ    1 
ATOM   806   N  NH1   . ARG A 1 136 ? 125.438 128.522 167.143 1.00 12603. ? 136 ARG A NH1   1 
ATOM   807   N  NH2   . ARG A 1 136 ? 124.139 126.654 166.914 1.00 12588. ? 136 ARG A NH2   1 
ATOM   808   N  N     . ALA A 1 137 ? 128.269 125.515 173.896 1.00 12692. ? 137 ALA A N     1 
ATOM   809   C  CA    . ALA A 1 137 ? 128.291 124.385 174.821 1.00 12705. ? 137 ALA A CA    1 
ATOM   810   C  C     . ALA A 1 137 ? 127.143 124.554 175.805 1.00 12609. ? 137 ALA A C     1 
ATOM   811   O  O     . ALA A 1 137 ? 127.253 125.290 176.786 1.00 12478. ? 137 ALA A O     1 
ATOM   812   C  CB    . ALA A 1 137 ? 129.633 124.298 175.536 1.00 12716. ? 137 ALA A CB    1 
ATOM   813   N  N     . SER A 1 138 ? 126.035 123.866 175.544 1.00 12639. ? 138 SER A N     1 
ATOM   814   C  CA    . SER A 1 138 ? 124.881 123.896 176.429 1.00 12594. ? 138 SER A CA    1 
ATOM   815   C  C     . SER A 1 138 ? 125.013 122.927 177.593 1.00 12546. ? 138 SER A C     1 
ATOM   816   O  O     . SER A 1 138 ? 124.129 122.888 178.454 1.00 12458. ? 138 SER A O     1 
ATOM   817   C  CB    . SER A 1 138 ? 123.604 123.589 175.646 1.00 12673. ? 138 SER A CB    1 
ATOM   818   O  OG    . SER A 1 138 ? 122.457 123.913 176.411 1.00 12553. ? 138 SER A OG    1 
ATOM   819   N  N     . GLY A 1 139 ? 126.086 122.150 177.633 1.00 12770. ? 139 GLY A N     1 
ATOM   820   C  CA    . GLY A 1 139 ? 126.302 121.228 178.727 1.00 12759. ? 139 GLY A CA    1 
ATOM   821   C  C     . GLY A 1 139 ? 127.597 120.479 178.519 1.00 12867. ? 139 GLY A C     1 
ATOM   822   O  O     . GLY A 1 139 ? 128.305 120.691 177.533 1.00 12918. ? 139 GLY A O     1 
ATOM   823   N  N     . GLY A 1 140 ? 127.901 119.595 179.460 1.00 13104. ? 140 GLY A N     1 
ATOM   824   C  CA    . GLY A 1 140 ? 129.112 118.809 179.353 1.00 13182. ? 140 GLY A CA    1 
ATOM   825   C  C     . GLY A 1 140 ? 129.007 117.731 178.297 1.00 13209. ? 140 GLY A C     1 
ATOM   826   O  O     . GLY A 1 140 ? 130.022 117.228 177.807 1.00 13207. ? 140 GLY A O     1 
ATOM   827   N  N     . LYS A 1 141 ? 127.775 117.376 177.930 1.00 13148. ? 141 LYS A N     1 
ATOM   828   C  CA    . LYS A 1 141 ? 127.516 116.277 177.008 1.00 13132. ? 141 LYS A CA    1 
ATOM   829   C  C     . LYS A 1 141 ? 126.592 116.687 175.866 1.00 13078. ? 141 LYS A C     1 
ATOM   830   O  O     . LYS A 1 141 ? 126.013 115.822 175.204 1.00 13070. ? 141 LYS A O     1 
ATOM   831   C  CB    . LYS A 1 141 ? 126.933 115.085 177.769 1.00 13066. ? 141 LYS A CB    1 
ATOM   832   C  CG    . LYS A 1 141 ? 127.794 114.638 178.941 1.00 13137. ? 141 LYS A CG    1 
ATOM   833   C  CD    . LYS A 1 141 ? 127.078 113.647 179.842 1.00 13118. ? 141 LYS A CD    1 
ATOM   834   C  CE    . LYS A 1 141 ? 126.466 112.512 179.048 1.00 13104. ? 141 LYS A CE    1 
ATOM   835   N  NZ    . LYS A 1 141 ? 125.856 111.479 179.929 1.00 13114. ? 141 LYS A NZ    1 
ATOM   836   N  N     . LEU A 1 142 ? 126.440 117.987 175.624 1.00 12735. ? 142 LEU A N     1 
ATOM   837   C  CA    . LEU A 1 142 ? 125.599 118.475 174.533 1.00 12723. ? 142 LEU A CA    1 
ATOM   838   C  C     . LEU A 1 142 ? 126.204 119.771 174.013 1.00 12745. ? 142 LEU A C     1 
ATOM   839   O  O     . LEU A 1 142 ? 126.258 120.766 174.740 1.00 12758. ? 142 LEU A O     1 
ATOM   840   C  CB    . LEU A 1 142 ? 124.163 118.689 174.999 1.00 12648. ? 142 LEU A CB    1 
ATOM   841   C  CG    . LEU A 1 142 ? 123.207 119.302 173.976 1.00 12655. ? 142 LEU A CG    1 
ATOM   842   C  CD1   . LEU A 1 142 ? 123.105 118.429 172.742 1.00 12712. ? 142 LEU A CD1   1 
ATOM   843   C  CD2   . LEU A 1 142 ? 121.841 119.518 174.591 1.00 12464. ? 142 LEU A CD2   1 
ATOM   844   N  N     . ILE A 1 143 ? 126.656 119.758 172.762 1.00 12739. ? 143 ILE A N     1 
ATOM   845   C  CA    . ILE A 1 143 ? 127.297 120.915 172.151 1.00 12738. ? 143 ILE A CA    1 
ATOM   846   C  C     . ILE A 1 143 ? 126.652 121.166 170.795 1.00 12763. ? 143 ILE A C     1 
ATOM   847   O  O     . ILE A 1 143 ? 126.097 120.256 170.175 1.00 12780. ? 143 ILE A O     1 
ATOM   848   C  CB    . ILE A 1 143 ? 128.826 120.711 172.020 1.00 12726. ? 143 ILE A CB    1 
ATOM   849   C  CG1   . ILE A 1 143 ? 129.415 120.276 173.362 1.00 12742. ? 143 ILE A CG1   1 
ATOM   850   C  CG2   . ILE A 1 143 ? 129.518 121.981 171.560 1.00 12743. ? 143 ILE A CG2   1 
ATOM   851   C  CD1   . ILE A 1 143 ? 130.908 120.093 173.344 1.00 12767. ? 143 ILE A CD1   1 
ATOM   852   N  N     . PHE A 1 144 ? 126.700 122.418 170.343 1.00 12757. ? 144 PHE A N     1 
ATOM   853   C  CA    . PHE A 1 144 ? 126.139 122.811 169.057 1.00 12717. ? 144 PHE A CA    1 
ATOM   854   C  C     . PHE A 1 144 ? 127.219 123.485 168.225 1.00 12728. ? 144 PHE A C     1 
ATOM   855   O  O     . PHE A 1 144 ? 127.837 124.455 168.673 1.00 12744. ? 144 PHE A O     1 
ATOM   856   C  CB    . PHE A 1 144 ? 124.948 123.751 169.245 1.00 12684. ? 144 PHE A CB    1 
ATOM   857   C  CG    . PHE A 1 144 ? 123.789 123.123 169.956 1.00 12632. ? 144 PHE A CG    1 
ATOM   858   C  CD1   . PHE A 1 144 ? 122.881 122.338 169.272 1.00 12628. ? 144 PHE A CD1   1 
ATOM   859   C  CD2   . PHE A 1 144 ? 123.604 123.324 171.310 1.00 12600. ? 144 PHE A CD2   1 
ATOM   860   C  CE1   . PHE A 1 144 ? 121.813 121.765 169.927 1.00 12586. ? 144 PHE A CE1   1 
ATOM   861   C  CE2   . PHE A 1 144 ? 122.539 122.752 171.969 1.00 12553. ? 144 PHE A CE2   1 
ATOM   862   C  CZ    . PHE A 1 144 ? 121.644 121.971 171.276 1.00 12507. ? 144 PHE A CZ    1 
ATOM   863   N  N     . TYR A 1 145 ? 127.437 122.976 167.019 1.00 12728. ? 145 TYR A N     1 
ATOM   864   C  CA    . TYR A 1 145 ? 128.358 123.556 166.055 1.00 12740. ? 145 TYR A CA    1 
ATOM   865   C  C     . TYR A 1 145 ? 127.578 124.113 164.873 1.00 12756. ? 145 TYR A C     1 
ATOM   866   O  O     . TYR A 1 145 ? 126.456 123.691 164.590 1.00 12777. ? 145 TYR A O     1 
ATOM   867   C  CB    . TYR A 1 145 ? 129.368 122.519 165.555 1.00 12738. ? 145 TYR A CB    1 
ATOM   868   C  CG    . TYR A 1 145 ? 130.172 121.845 166.638 1.00 12732. ? 145 TYR A CG    1 
ATOM   869   C  CD1   . TYR A 1 145 ? 131.311 122.440 167.156 1.00 12746. ? 145 TYR A CD1   1 
ATOM   870   C  CD2   . TYR A 1 145 ? 129.798 120.606 167.132 1.00 12748. ? 145 TYR A CD2   1 
ATOM   871   C  CE1   . TYR A 1 145 ? 132.049 121.823 168.141 1.00 12743. ? 145 TYR A CE1   1 
ATOM   872   C  CE2   . TYR A 1 145 ? 130.529 119.983 168.115 1.00 12758. ? 145 TYR A CE2   1 
ATOM   873   C  CZ    . TYR A 1 145 ? 131.653 120.595 168.616 1.00 12750. ? 145 TYR A CZ    1 
ATOM   874   O  OH    . TYR A 1 145 ? 132.385 119.973 169.598 1.00 12749. ? 145 TYR A OH    1 
ATOM   875   N  N     . ASP A 1 146 ? 128.197 125.054 164.167 1.00 12747. ? 146 ASP A N     1 
ATOM   876   C  CA    . ASP A 1 146 ? 127.599 125.682 162.992 1.00 12737. ? 146 ASP A CA    1 
ATOM   877   C  C     . ASP A 1 146 ? 128.524 125.448 161.802 1.00 12731. ? 146 ASP A C     1 
ATOM   878   O  O     . ASP A 1 146 ? 129.435 126.240 161.551 1.00 12750. ? 146 ASP A O     1 
ATOM   879   C  CB    . ASP A 1 146 ? 127.369 127.166 163.232 1.00 12750. ? 146 ASP A CB    1 
ATOM   880   C  CG    . ASP A 1 146 ? 125.957 127.471 163.674 1.00 12746. ? 146 ASP A CG    1 
ATOM   881   O  OD1   . ASP A 1 146 ? 125.176 126.519 163.875 1.00 12735. ? 146 ASP A OD1   1 
ATOM   882   O  OD2   . ASP A 1 146 ? 125.628 128.665 163.826 1.00 12732. ? 146 ASP A OD2   1 
ATOM   883   N  N     . LEU A 1 147 ? 128.296 124.358 161.073 1.00 12727. ? 147 LEU A N     1 
ATOM   884   C  CA    . LEU A 1 147 ? 129.075 124.076 159.876 1.00 12736. ? 147 LEU A CA    1 
ATOM   885   C  C     . LEU A 1 147 ? 128.650 125.017 158.760 1.00 12733. ? 147 LEU A C     1 
ATOM   886   O  O     . LEU A 1 147 ? 127.514 124.948 158.285 1.00 12755. ? 147 LEU A O     1 
ATOM   887   C  CB    . LEU A 1 147 ? 128.873 122.628 159.445 1.00 12743. ? 147 LEU A CB    1 
ATOM   888   C  CG    . LEU A 1 147 ? 129.754 121.558 160.078 1.00 12738. ? 147 LEU A CG    1 
ATOM   889   C  CD1   . LEU A 1 147 ? 129.714 120.296 159.239 1.00 12740. ? 147 LEU A CD1   1 
ATOM   890   C  CD2   . LEU A 1 147 ? 131.172 122.064 160.225 1.00 12752. ? 147 LEU A CD2   1 
ATOM   891   N  N     . ARG A 1 148 ? 129.553 125.888 158.327 1.00 12727. ? 148 ARG A N     1 
ATOM   892   C  CA    . ARG A 1 148 ? 129.267 126.813 157.240 1.00 12729. ? 148 ARG A CA    1 
ATOM   893   C  C     . ARG A 1 148 ? 130.070 126.396 156.020 1.00 12738. ? 148 ARG A C     1 
ATOM   894   O  O     . ARG A 1 148 ? 131.295 126.264 156.094 1.00 12752. ? 148 ARG A O     1 
ATOM   895   C  CB    . ARG A 1 148 ? 129.586 128.253 157.638 1.00 12747. ? 148 ARG A CB    1 
ATOM   896   C  CG    . ARG A 1 148 ? 128.440 128.946 158.343 1.00 12751. ? 148 ARG A CG    1 
ATOM   897   C  CD    . ARG A 1 148 ? 128.516 130.450 158.176 1.00 12752. ? 148 ARG A CD    1 
ATOM   898   N  NE    . ARG A 1 148 ? 127.234 131.093 158.437 1.00 12738. ? 148 ARG A NE    1 
ATOM   899   C  CZ    . ARG A 1 148 ? 126.665 131.183 159.631 1.00 12746. ? 148 ARG A CZ    1 
ATOM   900   N  NH1   . ARG A 1 148 ? 127.248 130.696 160.715 1.00 12746. ? 148 ARG A NH1   1 
ATOM   901   N  NH2   . ARG A 1 148 ? 125.483 131.781 159.742 1.00 12764. ? 148 ARG A NH2   1 
ATOM   902   N  N     . GLY A 1 149 ? 129.378 126.184 154.908 1.00 12746. ? 149 GLY A N     1 
ATOM   903   C  CA    . GLY A 1 149 ? 130.037 125.794 153.677 1.00 12751. ? 149 GLY A CA    1 
ATOM   904   C  C     . GLY A 1 149 ? 129.116 125.998 152.501 1.00 12757. ? 149 GLY A C     1 
ATOM   905   O  O     . GLY A 1 149 ? 127.890 125.966 152.642 1.00 12777. ? 149 GLY A O     1 
ATOM   906   N  N     . GLU A 1 150 ? 129.712 126.222 151.332 1.00 12801. ? 150 GLU A N     1 
ATOM   907   C  CA    . GLU A 1 150 ? 129.005 126.416 150.071 1.00 12794. ? 150 GLU A CA    1 
ATOM   908   C  C     . GLU A 1 150 ? 128.036 127.587 150.117 1.00 12798. ? 150 GLU A C     1 
ATOM   909   O  O     . GLU A 1 150 ? 127.093 127.633 149.318 1.00 12805. ? 150 GLU A O     1 
ATOM   910   C  CB    . GLU A 1 150 ? 128.255 125.150 149.649 1.00 12808. ? 150 GLU A CB    1 
ATOM   911   C  CG    . GLU A 1 150 ? 129.146 123.932 149.517 1.00 12818. ? 150 GLU A CG    1 
ATOM   912   C  CD    . GLU A 1 150 ? 128.404 122.641 149.773 1.00 12822. ? 150 GLU A CD    1 
ATOM   913   O  OE1   . GLU A 1 150 ? 127.169 122.691 149.946 1.00 12831. ? 150 GLU A OE1   1 
ATOM   914   O  OE2   . GLU A 1 150 ? 129.056 121.577 149.808 1.00 12741. ? 150 GLU A OE2   1 
ATOM   915   N  N     . GLY A 1 151 ? 128.237 128.536 151.027 1.00 12740. ? 151 GLY A N     1 
ATOM   916   C  CA    . GLY A 1 151 ? 127.332 129.651 151.186 1.00 12745. ? 151 GLY A CA    1 
ATOM   917   C  C     . GLY A 1 151 ? 126.161 129.403 152.108 1.00 12746. ? 151 GLY A C     1 
ATOM   918   O  O     . GLY A 1 151 ? 125.347 130.314 152.301 1.00 12762. ? 151 GLY A O     1 
ATOM   919   N  N     . VAL A 1 152 ? 126.045 128.209 152.685 1.00 12745. ? 152 VAL A N     1 
ATOM   920   C  CA    . VAL A 1 152 ? 124.929 127.861 153.551 1.00 12736. ? 152 VAL A CA    1 
ATOM   921   C  C     . VAL A 1 152 ? 125.468 127.429 154.910 1.00 12740. ? 152 VAL A C     1 
ATOM   922   O  O     . VAL A 1 152 ? 126.675 127.299 155.118 1.00 12756. ? 152 VAL A O     1 
ATOM   923   C  CB    . VAL A 1 152 ? 124.034 126.762 152.945 1.00 12740. ? 152 VAL A CB    1 
ATOM   924   C  CG1   . VAL A 1 152 ? 123.620 127.132 151.534 1.00 12757. ? 152 VAL A CG1   1 
ATOM   925   C  CG2   . VAL A 1 152 ? 124.748 125.429 152.964 1.00 12748. ? 152 VAL A CG2   1 
ATOM   926   N  N     . LYS A 1 153 ? 124.541 127.213 155.842 1.00 12741. ? 153 LYS A N     1 
ATOM   927   C  CA    . LYS A 1 153 ? 124.852 126.831 157.211 1.00 12741. ? 153 LYS A CA    1 
ATOM   928   C  C     . LYS A 1 153 ? 124.031 125.614 157.609 1.00 12740. ? 153 LYS A C     1 
ATOM   929   O  O     . LYS A 1 153 ? 122.858 125.499 157.244 1.00 12756. ? 153 LYS A O     1 
ATOM   930   C  CB    . LYS A 1 153 ? 124.572 127.981 158.181 1.00 12737. ? 153 LYS A CB    1 
ATOM   931   C  CG    . LYS A 1 153 ? 124.907 127.670 159.624 1.00 12737. ? 153 LYS A CG    1 
ATOM   932   C  CD    . LYS A 1 153 ? 124.302 128.698 160.556 1.00 12736. ? 153 LYS A CD    1 
ATOM   933   C  CE    . LYS A 1 153 ? 122.802 128.507 160.681 1.00 12731. ? 153 LYS A CE    1 
ATOM   934   N  NZ    . LYS A 1 153 ? 122.464 127.377 161.588 1.00 12736. ? 153 LYS A NZ    1 
ATOM   935   N  N     . LEU A 1 154 ? 124.653 124.710 158.362 1.00 12742. ? 154 LEU A N     1 
ATOM   936   C  CA    . LEU A 1 154 ? 123.992 123.526 158.891 1.00 12735. ? 154 LEU A CA    1 
ATOM   937   C  C     . LEU A 1 154 ? 124.416 123.337 160.337 1.00 12736. ? 154 LEU A C     1 
ATOM   938   O  O     . LEU A 1 154 ? 125.608 123.389 160.646 1.00 12750. ? 154 LEU A O     1 
ATOM   939   C  CB    . LEU A 1 154 ? 124.344 122.284 158.069 1.00 12736. ? 154 LEU A CB    1 
ATOM   940   C  CG    . LEU A 1 154 ? 123.697 120.972 158.507 1.00 12739. ? 154 LEU A CG    1 
ATOM   941   C  CD1   . LEU A 1 154 ? 122.190 121.070 158.423 1.00 12757. ? 154 LEU A CD1   1 
ATOM   942   C  CD2   . LEU A 1 154 ? 124.208 119.819 157.668 1.00 12751. ? 154 LEU A CD2   1 
ATOM   943   N  N     . GLN A 1 155 ? 123.452 123.121 161.221 1.00 12744. ? 155 GLN A N     1 
ATOM   944   C  CA    . GLN A 1 155 ? 123.779 122.900 162.619 1.00 12742. ? 155 GLN A CA    1 
ATOM   945   C  C     . GLN A 1 155 ? 124.227 121.463 162.838 1.00 12748. ? 155 GLN A C     1 
ATOM   946   O  O     . GLN A 1 155 ? 123.862 120.555 162.089 1.00 12770. ? 155 GLN A O     1 
ATOM   947   C  CB    . GLN A 1 155 ? 122.583 123.211 163.515 1.00 12743. ? 155 GLN A CB    1 
ATOM   948   C  CG    . GLN A 1 155 ? 122.961 123.530 164.947 1.00 12720. ? 155 GLN A CG    1 
ATOM   949   C  CD    . GLN A 1 155 ? 121.756 123.730 165.836 1.00 12633. ? 155 GLN A CD    1 
ATOM   950   O  OE1   . GLN A 1 155 ? 121.569 124.796 166.418 1.00 12519. ? 155 GLN A OE1   1 
ATOM   951   N  NE2   . GLN A 1 155 ? 120.927 122.701 165.944 1.00 12666. ? 155 GLN A NE2   1 
ATOM   952   N  N     . VAL A 1 156 ? 125.043 121.267 163.869 1.00 12737. ? 156 VAL A N     1 
ATOM   953   C  CA    . VAL A 1 156 ? 125.488 119.946 164.296 1.00 12729. ? 156 VAL A CA    1 
ATOM   954   C  C     . VAL A 1 156 ? 125.256 119.878 165.797 1.00 12735. ? 156 VAL A C     1 
ATOM   955   O  O     . VAL A 1 156 ? 125.957 120.547 166.563 1.00 12748. ? 156 VAL A O     1 
ATOM   956   C  CB    . VAL A 1 156 ? 126.965 119.687 163.961 1.00 12738. ? 156 VAL A CB    1 
ATOM   957   C  CG1   . VAL A 1 156 ? 127.363 118.289 164.385 1.00 12751. ? 156 VAL A CG1   1 
ATOM   958   C  CG2   . VAL A 1 156 ? 127.241 119.902 162.481 1.00 12755. ? 156 VAL A CG2   1 
ATOM   959   N  N     . MET A 1 157 ? 124.268 119.097 166.224 1.00 12737. ? 157 MET A N     1 
ATOM   960   C  CA    . MET A 1 157 ? 123.995 118.928 167.648 1.00 12740. ? 157 MET A CA    1 
ATOM   961   C  C     . MET A 1 157 ? 124.657 117.625 168.100 1.00 12747. ? 157 MET A C     1 
ATOM   962   O  O     . MET A 1 157 ? 124.219 116.528 167.745 1.00 12752. ? 157 MET A O     1 
ATOM   963   C  CB    . MET A 1 157 ? 122.490 119.001 167.943 1.00 12740. ? 157 MET A CB    1 
ATOM   964   C  CG    . MET A 1 157 ? 121.984 118.758 169.354 1.00 12743. ? 157 MET A CG    1 
ATOM   965   S  SD    . MET A 1 157 ? 120.195 118.955 169.460 1.00 12645. ? 157 MET A SD    1 
ATOM   966   C  CE    . MET A 1 157 ? 119.657 117.469 168.624 1.00 12682. ? 157 MET A CE    1 
ATOM   967   N  N     . ALA A 1 158 ? 125.767 117.757 168.819 1.00 12746. ? 158 ALA A N     1 
ATOM   968   C  CA    . ALA A 1 158 ? 126.539 116.621 169.298 1.00 12739. ? 158 ALA A CA    1 
ATOM   969   C  C     . ALA A 1 158 ? 126.073 116.289 170.708 1.00 12744. ? 158 ALA A C     1 
ATOM   970   O  O     . ALA A 1 158 ? 126.268 117.080 171.636 1.00 12762. ? 158 ALA A O     1 
ATOM   971   C  CB    . ALA A 1 158 ? 128.034 116.928 169.270 1.00 12748. ? 158 ALA A CB    1 
ATOM   972   N  N     . ASN A 1 159 ? 125.442 115.129 170.857 1.00 12912. ? 159 ASN A N     1 
ATOM   973   C  CA    . ASN A 1 159 ? 125.007 114.611 172.145 1.00 12937. ? 159 ASN A CA    1 
ATOM   974   C  C     . ASN A 1 159 ? 125.679 113.265 172.366 1.00 12941. ? 159 ASN A C     1 
ATOM   975   O  O     . ASN A 1 159 ? 125.649 112.403 171.483 1.00 12943. ? 159 ASN A O     1 
ATOM   976   C  CB    . ASN A 1 159 ? 123.484 114.471 172.191 1.00 12922. ? 159 ASN A CB    1 
ATOM   977   C  CG    . ASN A 1 159 ? 122.949 114.370 173.605 1.00 12858. ? 159 ASN A CG    1 
ATOM   978   O  OD1   . ASN A 1 159 ? 123.712 114.274 174.564 1.00 12824. ? 159 ASN A OD1   1 
ATOM   979   N  ND2   . ASN A 1 159 ? 121.628 114.391 173.741 1.00 12799. ? 159 ASN A ND2   1 
ATOM   980   N  N     . SER A 1 160 ? 126.292 113.091 173.539 1.00 12772. ? 160 SER A N     1 
ATOM   981   C  CA    . SER A 1 160 ? 127.047 111.870 173.797 1.00 12766. ? 160 SER A CA    1 
ATOM   982   C  C     . SER A 1 160 ? 126.141 110.648 173.790 1.00 12762. ? 160 SER A C     1 
ATOM   983   O  O     . SER A 1 160 ? 126.603 109.524 173.569 1.00 12777. ? 160 SER A O     1 
ATOM   984   C  CB    . SER A 1 160 ? 127.782 111.973 175.131 1.00 12792. ? 160 SER A CB    1 
ATOM   985   O  OG    . SER A 1 160 ? 127.011 111.401 176.168 1.00 12781. ? 160 SER A OG    1 
ATOM   986   N  N     . ARG A 1 161 ? 124.846 110.848 174.041 1.00 13179. ? 161 ARG A N     1 
ATOM   987   C  CA    . ARG A 1 161 ? 123.904 109.737 174.002 1.00 13197. ? 161 ARG A CA    1 
ATOM   988   C  C     . ARG A 1 161 ? 123.833 109.116 172.615 1.00 13189. ? 161 ARG A C     1 
ATOM   989   O  O     . ARG A 1 161 ? 123.719 107.893 172.487 1.00 13200. ? 161 ARG A O     1 
ATOM   990   C  CB    . ARG A 1 161 ? 122.520 110.211 174.446 1.00 13194. ? 161 ARG A CB    1 
ATOM   991   C  CG    . ARG A 1 161 ? 121.609 109.097 174.923 1.00 13219. ? 161 ARG A CG    1 
ATOM   992   C  CD    . ARG A 1 161 ? 120.291 109.647 175.440 1.00 13220. ? 161 ARG A CD    1 
ATOM   993   N  NE    . ARG A 1 161 ? 120.474 110.535 176.582 1.00 13170. ? 161 ARG A NE    1 
ATOM   994   C  CZ    . ARG A 1 161 ? 120.021 111.780 176.644 1.00 13124. ? 161 ARG A CZ    1 
ATOM   995   N  NH1   . ARG A 1 161 ? 119.367 112.330 175.635 1.00 13102. ? 161 ARG A NH1   1 
ATOM   996   N  NH2   . ARG A 1 161 ? 120.230 112.491 177.748 1.00 13053. ? 161 ARG A NH2   1 
ATOM   997   N  N     . ASN A 1 162 ? 123.899 109.937 171.569 1.00 12765. ? 162 ASN A N     1 
ATOM   998   C  CA    . ASN A 1 162 ? 123.872 109.452 170.197 1.00 12759. ? 162 ASN A CA    1 
ATOM   999   C  C     . ASN A 1 162 ? 125.257 109.178 169.630 1.00 12759. ? 162 ASN A C     1 
ATOM   1000  O  O     . ASN A 1 162 ? 125.363 108.505 168.600 1.00 12767. ? 162 ASN A O     1 
ATOM   1001  C  CB    . ASN A 1 162 ? 123.148 110.456 169.296 1.00 12752. ? 162 ASN A CB    1 
ATOM   1002  C  CG    . ASN A 1 162 ? 121.758 110.783 169.792 1.00 12747. ? 162 ASN A CG    1 
ATOM   1003  O  OD1   . ASN A 1 162 ? 121.461 111.927 170.134 1.00 12743. ? 162 ASN A OD1   1 
ATOM   1004  N  ND2   . ASN A 1 162 ? 120.894 109.777 169.833 1.00 12750. ? 162 ASN A ND2   1 
ATOM   1005  N  N     . TYR A 1 163 ? 126.309 109.678 170.268 1.00 12748. ? 163 TYR A N     1 
ATOM   1006  C  CA    . TYR A 1 163 ? 127.668 109.408 169.833 1.00 12748. ? 163 TYR A CA    1 
ATOM   1007  C  C     . TYR A 1 163 ? 128.005 107.939 170.070 1.00 12750. ? 163 TYR A C     1 
ATOM   1008  O  O     . TYR A 1 163 ? 127.328 107.232 170.819 1.00 12763. ? 163 TYR A O     1 
ATOM   1009  C  CB    . TYR A 1 163 ? 128.650 110.317 170.569 1.00 12755. ? 163 TYR A CB    1 
ATOM   1010  C  CG    . TYR A 1 163 ? 129.850 110.732 169.753 1.00 12754. ? 163 TYR A CG    1 
ATOM   1011  C  CD1   . TYR A 1 163 ? 129.804 111.850 168.934 1.00 12751. ? 163 TYR A CD1   1 
ATOM   1012  C  CD2   . TYR A 1 163 ? 131.034 110.015 169.811 1.00 12768. ? 163 TYR A CD2   1 
ATOM   1013  C  CE1   . TYR A 1 163 ? 130.900 112.234 168.190 1.00 12744. ? 163 TYR A CE1   1 
ATOM   1014  C  CE2   . TYR A 1 163 ? 132.133 110.391 169.070 1.00 12766. ? 163 TYR A CE2   1 
ATOM   1015  C  CZ    . TYR A 1 163 ? 132.061 111.500 168.263 1.00 12745. ? 163 TYR A CZ    1 
ATOM   1016  O  OH    . TYR A 1 163 ? 133.158 111.875 167.526 1.00 12755. ? 163 TYR A OH    1 
ATOM   1017  N  N     . LYS A 1 164 ? 129.067 107.474 169.410 1.00 12745. ? 164 LYS A N     1 
ATOM   1018  C  CA    . LYS A 1 164 ? 129.428 106.065 169.521 1.00 12757. ? 164 LYS A CA    1 
ATOM   1019  C  C     . LYS A 1 164 ? 129.821 105.692 170.944 1.00 12790. ? 164 LYS A C     1 
ATOM   1020  O  O     . LYS A 1 164 ? 129.510 104.585 171.397 1.00 12781. ? 164 LYS A O     1 
ATOM   1021  C  CB    . LYS A 1 164 ? 130.550 105.726 168.543 1.00 12759. ? 164 LYS A CB    1 
ATOM   1022  C  CG    . LYS A 1 164 ? 131.577 106.820 168.358 1.00 12771. ? 164 LYS A CG    1 
ATOM   1023  C  CD    . LYS A 1 164 ? 132.624 106.410 167.335 1.00 12773. ? 164 LYS A CD    1 
ATOM   1024  C  CE    . LYS A 1 164 ? 132.978 104.935 167.458 1.00 12767. ? 164 LYS A CE    1 
ATOM   1025  N  NZ    . LYS A 1 164 ? 134.050 104.536 166.507 1.00 12756. ? 164 LYS A NZ    1 
ATOM   1026  N  N     . SER A 1 165 ? 130.498 106.585 171.661 1.00 13982. ? 165 SER A N     1 
ATOM   1027  C  CA    . SER A 1 165 ? 130.780 106.368 173.073 1.00 14035. ? 165 SER A CA    1 
ATOM   1028  C  C     . SER A 1 165 ? 131.094 107.706 173.724 1.00 14052. ? 165 SER A C     1 
ATOM   1029  O  O     . SER A 1 165 ? 131.353 108.705 173.049 1.00 14031. ? 165 SER A O     1 
ATOM   1030  C  CB    . SER A 1 165 ? 131.924 105.374 173.275 1.00 14060. ? 165 SER A CB    1 
ATOM   1031  O  OG    . SER A 1 165 ? 132.882 105.493 172.245 1.00 14063. ? 165 SER A OG    1 
ATOM   1032  N  N     . GLU A 1 166 ? 131.067 107.708 175.057 1.00 14836. ? 166 GLU A N     1 
ATOM   1033  C  CA    . GLU A 1 166 ? 131.220 108.950 175.807 1.00 14849. ? 166 GLU A CA    1 
ATOM   1034  C  C     . GLU A 1 166 ? 132.654 109.465 175.761 1.00 14837. ? 166 GLU A C     1 
ATOM   1035  O  O     . GLU A 1 166 ? 132.886 110.665 175.571 1.00 14817. ? 166 GLU A O     1 
ATOM   1036  C  CB    . GLU A 1 166 ? 130.771 108.739 177.253 1.00 14873. ? 166 GLU A CB    1 
ATOM   1037  C  CG    . GLU A 1 166 ? 131.153 109.862 178.207 1.00 14874. ? 166 GLU A CG    1 
ATOM   1038  C  CD    . GLU A 1 166 ? 130.352 111.131 177.985 1.00 14853. ? 166 GLU A CD    1 
ATOM   1039  O  OE1   . GLU A 1 166 ? 130.570 111.811 176.960 1.00 14829. ? 166 GLU A OE1   1 
ATOM   1040  O  OE2   . GLU A 1 166 ? 129.504 111.451 178.842 1.00 14847. ? 166 GLU A OE2   1 
ATOM   1041  N  N     . GLU A 1 167 ? 133.632 108.575 175.950 1.00 14897. ? 167 GLU A N     1 
ATOM   1042  C  CA    . GLU A 1 167 ? 135.014 109.029 176.083 1.00 14897. ? 167 GLU A CA    1 
ATOM   1043  C  C     . GLU A 1 167 ? 135.535 109.629 174.782 1.00 14862. ? 167 GLU A C     1 
ATOM   1044  O  O     . GLU A 1 167 ? 136.210 110.666 174.800 1.00 14851. ? 167 GLU A O     1 
ATOM   1045  C  CB    . GLU A 1 167 ? 135.912 107.884 176.565 1.00 14929. ? 167 GLU A CB    1 
ATOM   1046  C  CG    . GLU A 1 167 ? 136.157 106.749 175.579 1.00 14937. ? 167 GLU A CG    1 
ATOM   1047  C  CD    . GLU A 1 167 ? 134.920 105.920 175.298 1.00 14928. ? 167 GLU A CD    1 
ATOM   1048  O  OE1   . GLU A 1 167 ? 133.965 105.976 176.101 1.00 14924. ? 167 GLU A OE1   1 
ATOM   1049  O  OE2   . GLU A 1 167 ? 134.909 105.204 174.275 1.00 14929. ? 167 GLU A OE2   1 
ATOM   1050  N  N     . GLU A 1 168 ? 135.221 109.014 173.639 1.00 14144. ? 168 GLU A N     1 
ATOM   1051  C  CA    . GLU A 1 168 ? 135.650 109.607 172.378 1.00 14120. ? 168 GLU A CA    1 
ATOM   1052  C  C     . GLU A 1 168 ? 134.869 110.874 172.069 1.00 14068. ? 168 GLU A C     1 
ATOM   1053  O  O     . GLU A 1 168 ? 135.401 111.779 171.421 1.00 14067. ? 168 GLU A O     1 
ATOM   1054  C  CB    . GLU A 1 168 ? 135.526 108.608 171.232 1.00 14128. ? 168 GLU A CB    1 
ATOM   1055  C  CG    . GLU A 1 168 ? 135.687 107.162 171.638 1.00 14142. ? 168 GLU A CG    1 
ATOM   1056  C  CD    . GLU A 1 168 ? 135.136 106.214 170.598 1.00 14133. ? 168 GLU A CD    1 
ATOM   1057  O  OE1   . GLU A 1 168 ? 134.981 106.640 169.436 1.00 14131. ? 168 GLU A OE1   1 
ATOM   1058  O  OE2   . GLU A 1 168 ? 134.852 105.048 170.942 1.00 14136. ? 168 GLU A OE2   1 
ATOM   1059  N  N     . PHE A 1 169 ? 133.619 110.962 172.529 1.00 12849. ? 169 PHE A N     1 
ATOM   1060  C  CA    . PHE A 1 169 ? 132.878 112.214 172.416 1.00 12794. ? 169 PHE A CA    1 
ATOM   1061  C  C     . PHE A 1 169 ? 133.608 113.336 173.141 1.00 12780. ? 169 PHE A C     1 
ATOM   1062  O  O     . PHE A 1 169 ? 133.815 114.422 172.586 1.00 12774. ? 169 PHE A O     1 
ATOM   1063  C  CB    . PHE A 1 169 ? 131.467 112.036 172.978 1.00 12791. ? 169 PHE A CB    1 
ATOM   1064  C  CG    . PHE A 1 169 ? 130.694 113.317 173.100 1.00 12756. ? 169 PHE A CG    1 
ATOM   1065  C  CD1   . PHE A 1 169 ? 130.055 113.862 172.004 1.00 12746. ? 169 PHE A CD1   1 
ATOM   1066  C  CD2   . PHE A 1 169 ? 130.601 113.973 174.314 1.00 12768. ? 169 PHE A CD2   1 
ATOM   1067  C  CE1   . PHE A 1 169 ? 129.345 115.036 172.114 1.00 12744. ? 169 PHE A CE1   1 
ATOM   1068  C  CE2   . PHE A 1 169 ? 129.893 115.148 174.428 1.00 12760. ? 169 PHE A CE2   1 
ATOM   1069  C  CZ    . PHE A 1 169 ? 129.264 115.679 173.327 1.00 12746. ? 169 PHE A CZ    1 
ATOM   1070  N  N     . ILE A 1 170 ? 134.026 113.076 174.381 1.00 12800. ? 170 ILE A N     1 
ATOM   1071  C  CA    . ILE A 1 170 ? 134.751 114.080 175.153 1.00 12763. ? 170 ILE A CA    1 
ATOM   1072  C  C     . ILE A 1 170 ? 136.066 114.429 174.471 1.00 12767. ? 170 ILE A C     1 
ATOM   1073  O  O     . ILE A 1 170 ? 136.437 115.604 174.367 1.00 12758. ? 170 ILE A O     1 
ATOM   1074  C  CB    . ILE A 1 170 ? 134.977 113.584 176.593 1.00 12772. ? 170 ILE A CB    1 
ATOM   1075  C  CG1   . ILE A 1 170 ? 133.643 113.450 177.325 1.00 12789. ? 170 ILE A CG1   1 
ATOM   1076  C  CG2   . ILE A 1 170 ? 135.901 114.524 177.342 1.00 12753. ? 170 ILE A CG2   1 
ATOM   1077  C  CD1   . ILE A 1 170 ? 133.773 112.911 178.729 1.00 12783. ? 170 ILE A CD1   1 
ATOM   1078  N  N     . HIS A 1 171 ? 136.785 113.415 173.986 1.00 13137. ? 171 HIS A N     1 
ATOM   1079  C  CA    . HIS A 1 171 ? 138.070 113.653 173.338 1.00 13140. ? 171 HIS A CA    1 
ATOM   1080  C  C     . HIS A 1 171 ? 137.916 114.538 172.104 1.00 13134. ? 171 HIS A C     1 
ATOM   1081  O  O     . HIS A 1 171 ? 138.624 115.542 171.950 1.00 13142. ? 171 HIS A O     1 
ATOM   1082  C  CB    . HIS A 1 171 ? 138.712 112.315 172.971 1.00 13151. ? 171 HIS A CB    1 
ATOM   1083  C  CG    . HIS A 1 171 ? 140.084 112.437 172.390 1.00 13139. ? 171 HIS A CG    1 
ATOM   1084  N  ND1   . HIS A 1 171 ? 141.094 113.144 173.007 1.00 13141. ? 171 HIS A ND1   1 
ATOM   1085  C  CD2   . HIS A 1 171 ? 140.618 111.937 171.251 1.00 13148. ? 171 HIS A CD2   1 
ATOM   1086  C  CE1   . HIS A 1 171 ? 142.189 113.077 172.271 1.00 13163. ? 171 HIS A CE1   1 
ATOM   1087  N  NE2   . HIS A 1 171 ? 141.926 112.350 171.200 1.00 13171. ? 171 HIS A NE2   1 
ATOM   1088  N  N     . ILE A 1 172 ? 136.975 114.194 171.223 1.00 12789. ? 172 ILE A N     1 
ATOM   1089  C  CA    . ILE A 1 172 ? 136.822 114.944 169.982 1.00 12756. ? 172 ILE A CA    1 
ATOM   1090  C  C     . ILE A 1 172 ? 136.300 116.347 170.261 1.00 12752. ? 172 ILE A C     1 
ATOM   1091  O  O     . ILE A 1 172 ? 136.712 117.311 169.608 1.00 12762. ? 172 ILE A O     1 
ATOM   1092  C  CB    . ILE A 1 172 ? 135.926 114.178 168.988 1.00 12749. ? 172 ILE A CB    1 
ATOM   1093  C  CG1   . ILE A 1 172 ? 135.986 114.827 167.604 1.00 12751. ? 172 ILE A CG1   1 
ATOM   1094  C  CG2   . ILE A 1 172 ? 134.491 114.112 169.467 1.00 12763. ? 172 ILE A CG2   1 
ATOM   1095  C  CD1   . ILE A 1 172 ? 137.384 115.142 167.133 1.00 12755. ? 172 ILE A CD1   1 
ATOM   1096  N  N     . ASN A 1 173 ? 135.404 116.499 171.240 1.00 12758. ? 173 ASN A N     1 
ATOM   1097  C  CA    . ASN A 1 173 ? 134.892 117.831 171.530 1.00 12749. ? 173 ASN A CA    1 
ATOM   1098  C  C     . ASN A 1 173 ? 135.908 118.685 172.269 1.00 12746. ? 173 ASN A C     1 
ATOM   1099  O  O     . ASN A 1 173 ? 135.792 119.915 172.257 1.00 12742. ? 173 ASN A O     1 
ATOM   1100  C  CB    . ASN A 1 173 ? 133.594 117.731 172.324 1.00 12750. ? 173 ASN A CB    1 
ATOM   1101  C  CG    . ASN A 1 173 ? 132.437 117.266 171.472 1.00 12750. ? 173 ASN A CG    1 
ATOM   1102  O  OD1   . ASN A 1 173 ? 131.654 118.071 170.973 1.00 12746. ? 173 ASN A OD1   1 
ATOM   1103  N  ND2   . ASN A 1 173 ? 132.332 115.959 171.285 1.00 12763. ? 173 ASN A ND2   1 
ATOM   1104  N  N     . ASN A 1 174 ? 136.896 118.066 172.915 1.00 12750. ? 174 ASN A N     1 
ATOM   1105  C  CA    . ASN A 1 174 ? 138.013 118.829 173.451 1.00 12745. ? 174 ASN A CA    1 
ATOM   1106  C  C     . ASN A 1 174 ? 138.984 119.240 172.355 1.00 12738. ? 174 ASN A C     1 
ATOM   1107  O  O     . ASN A 1 174 ? 139.576 120.321 172.430 1.00 12753. ? 174 ASN A O     1 
ATOM   1108  C  CB    . ASN A 1 174 ? 138.740 118.015 174.521 1.00 12748. ? 174 ASN A CB    1 
ATOM   1109  C  CG    . ASN A 1 174 ? 138.435 118.495 175.921 1.00 12749. ? 174 ASN A CG    1 
ATOM   1110  O  OD1   . ASN A 1 174 ? 138.071 119.652 176.127 1.00 12756. ? 174 ASN A OD1   1 
ATOM   1111  N  ND2   . ASN A 1 174 ? 138.580 117.607 176.895 1.00 12748. ? 174 ASN A ND2   1 
ATOM   1112  N  N     . LYS A 1 175 ? 139.161 118.394 171.338 1.00 12726. ? 175 LYS A N     1 
ATOM   1113  C  CA    . LYS A 1 175 ? 140.073 118.733 170.250 1.00 12730. ? 175 LYS A CA    1 
ATOM   1114  C  C     . LYS A 1 175 ? 139.549 119.893 169.411 1.00 12732. ? 175 LYS A C     1 
ATOM   1115  O  O     . LYS A 1 175 ? 140.325 120.752 168.981 1.00 12740. ? 175 LYS A O     1 
ATOM   1116  C  CB    . LYS A 1 175 ? 140.312 117.509 169.368 1.00 12740. ? 175 LYS A CB    1 
ATOM   1117  C  CG    . LYS A 1 175 ? 141.357 116.556 169.906 1.00 12753. ? 175 LYS A CG    1 
ATOM   1118  C  CD    . LYS A 1 175 ? 141.240 115.189 169.259 1.00 12748. ? 175 LYS A CD    1 
ATOM   1119  C  CE    . LYS A 1 175 ? 141.242 115.293 167.748 1.00 12736. ? 175 LYS A CE    1 
ATOM   1120  N  NZ    . LYS A 1 175 ? 141.258 113.949 167.113 1.00 12746. ? 175 LYS A NZ    1 
ATOM   1121  N  N     . LEU A 1 176 ? 138.243 119.933 169.166 1.00 12741. ? 176 LEU A N     1 
ATOM   1122  C  CA    . LEU A 1 176 ? 137.690 120.853 168.181 1.00 12737. ? 176 LEU A CA    1 
ATOM   1123  C  C     . LEU A 1 176 ? 137.699 122.292 168.681 1.00 12738. ? 176 LEU A C     1 
ATOM   1124  O  O     . LEU A 1 176 ? 137.430 122.565 169.853 1.00 12748. ? 176 LEU A O     1 
ATOM   1125  C  CB    . LEU A 1 176 ? 136.265 120.444 167.818 1.00 12744. ? 176 LEU A CB    1 
ATOM   1126  C  CG    . LEU A 1 176 ? 136.124 119.116 167.077 1.00 12738. ? 176 LEU A CG    1 
ATOM   1127  C  CD1   . LEU A 1 176 ? 134.680 118.869 166.692 1.00 12743. ? 176 LEU A CD1   1 
ATOM   1128  C  CD2   . LEU A 1 176 ? 137.024 119.089 165.860 1.00 12753. ? 176 LEU A CD2   1 
ATOM   1129  N  N     . ARG A 1 177 ? 138.002 123.213 167.771 1.00 12743. ? 177 ARG A N     1 
ATOM   1130  C  CA    . ARG A 1 177 ? 137.931 124.645 168.014 1.00 12746. ? 177 ARG A CA    1 
ATOM   1131  C  C     . ARG A 1 177 ? 137.215 125.304 166.844 1.00 12753. ? 177 ARG A C     1 
ATOM   1132  O  O     . ARG A 1 177 ? 136.977 124.684 165.805 1.00 12778. ? 177 ARG A O     1 
ATOM   1133  C  CB    . ARG A 1 177 ? 139.324 125.260 168.200 1.00 12749. ? 177 ARG A CB    1 
ATOM   1134  C  CG    . ARG A 1 177 ? 140.019 124.850 169.481 1.00 12736. ? 177 ARG A CG    1 
ATOM   1135  C  CD    . ARG A 1 177 ? 139.349 125.464 170.689 1.00 12689. ? 177 ARG A CD    1 
ATOM   1136  N  NE    . ARG A 1 177 ? 140.111 125.223 171.908 1.00 12617. ? 177 ARG A NE    1 
ATOM   1137  C  CZ    . ARG A 1 177 ? 140.050 124.106 172.618 1.00 12674. ? 177 ARG A CZ    1 
ATOM   1138  N  NH1   . ARG A 1 177 ? 139.272 123.100 172.259 1.00 12730. ? 177 ARG A NH1   1 
ATOM   1139  N  NH2   . ARG A 1 177 ? 140.788 123.997 173.719 1.00 12632. ? 177 ARG A NH2   1 
ATOM   1140  N  N     . ARG A 1 178 ? 136.866 126.573 167.021 1.00 12712. ? 178 ARG A N     1 
ATOM   1141  C  CA    . ARG A 1 178 ? 136.195 127.311 165.960 1.00 12714. ? 178 ARG A CA    1 
ATOM   1142  C  C     . ARG A 1 178 ? 137.141 127.541 164.790 1.00 12729. ? 178 ARG A C     1 
ATOM   1143  O  O     . ARG A 1 178 ? 138.336 127.784 164.973 1.00 12729. ? 178 ARG A O     1 
ATOM   1144  C  CB    . ARG A 1 178 ? 135.677 128.645 166.486 1.00 12716. ? 178 ARG A CB    1 
ATOM   1145  C  CG    . ARG A 1 178 ? 134.417 128.536 167.316 1.00 12718. ? 178 ARG A CG    1 
ATOM   1146  C  CD    . ARG A 1 178 ? 133.649 129.838 167.292 1.00 12702. ? 178 ARG A CD    1 
ATOM   1147  N  NE    . ARG A 1 178 ? 134.522 130.967 167.005 1.00 12641. ? 178 ARG A NE    1 
ATOM   1148  C  CZ    . ARG A 1 178 ? 134.327 131.834 166.022 1.00 12669. ? 178 ARG A CZ    1 
ATOM   1149  N  NH1   . ARG A 1 178 ? 133.291 131.733 165.208 1.00 12748. ? 178 ARG A NH1   1 
ATOM   1150  N  NH2   . ARG A 1 178 ? 135.195 132.825 165.850 1.00 12648. ? 178 ARG A NH2   1 
ATOM   1151  N  N     . GLY A 1 179 ? 136.597 127.465 163.578 1.00 12743. ? 179 GLY A N     1 
ATOM   1152  C  CA    . GLY A 1 179 ? 137.377 127.629 162.374 1.00 12750. ? 179 GLY A CA    1 
ATOM   1153  C  C     . GLY A 1 179 ? 137.993 126.360 161.833 1.00 12748. ? 179 GLY A C     1 
ATOM   1154  O  O     . GLY A 1 179 ? 138.586 126.393 160.749 1.00 12759. ? 179 GLY A O     1 
ATOM   1155  N  N     . ASP A 1 180 ? 137.868 125.245 162.543 1.00 12736. ? 180 ASP A N     1 
ATOM   1156  C  CA    . ASP A 1 180 ? 138.450 123.992 162.090 1.00 12735. ? 180 ASP A CA    1 
ATOM   1157  C  C     . ASP A 1 180 ? 137.578 123.347 161.022 1.00 12738. ? 180 ASP A C     1 
ATOM   1158  O  O     . ASP A 1 180 ? 136.351 123.305 161.143 1.00 12752. ? 180 ASP A O     1 
ATOM   1159  C  CB    . ASP A 1 180 ? 138.626 123.033 163.266 1.00 12746. ? 180 ASP A CB    1 
ATOM   1160  C  CG    . ASP A 1 180 ? 139.730 123.465 164.210 1.00 12763. ? 180 ASP A CG    1 
ATOM   1161  O  OD1   . ASP A 1 180 ? 140.482 124.399 163.863 1.00 12768. ? 180 ASP A OD1   1 
ATOM   1162  O  OD2   . ASP A 1 180 ? 139.848 122.869 165.300 1.00 12768. ? 180 ASP A OD2   1 
ATOM   1163  N  N     . ILE A 1 181 ? 138.220 122.846 159.973 1.00 12739. ? 181 ILE A N     1 
ATOM   1164  C  CA    . ILE A 1 181 ? 137.529 122.071 158.948 1.00 12729. ? 181 ILE A CA    1 
ATOM   1165  C  C     . ILE A 1 181 ? 137.339 120.659 159.478 1.00 12741. ? 181 ILE A C     1 
ATOM   1166  O  O     . ILE A 1 181 ? 138.315 119.968 159.785 1.00 12770. ? 181 ILE A O     1 
ATOM   1167  C  CB    . ILE A 1 181 ? 138.317 122.060 157.632 1.00 12656. ? 181 ILE A CB    1 
ATOM   1168  C  CG1   . ILE A 1 181 ? 138.698 123.482 157.220 1.00 12565. ? 181 ILE A CG1   1 
ATOM   1169  C  CG2   . ILE A 1 181 ? 137.522 121.357 156.546 1.00 12645. ? 181 ILE A CG2   1 
ATOM   1170  C  CD1   . ILE A 1 181 ? 137.636 124.192 156.425 1.00 12653. ? 181 ILE A CD1   1 
ATOM   1171  N  N     . ILE A 1 182 ? 136.084 120.223 159.577 1.00 12730. ? 182 ILE A N     1 
ATOM   1172  C  CA    . ILE A 1 182 ? 135.753 118.932 160.156 1.00 12725. ? 182 ILE A CA    1 
ATOM   1173  C  C     . ILE A 1 182 ? 134.837 118.172 159.208 1.00 12716. ? 182 ILE A C     1 
ATOM   1174  O  O     . ILE A 1 182 ? 134.182 118.744 158.333 1.00 12740. ? 182 ILE A O     1 
ATOM   1175  C  CB    . ILE A 1 182 ? 135.087 119.066 161.541 1.00 12729. ? 182 ILE A CB    1 
ATOM   1176  C  CG1   . ILE A 1 182 ? 133.730 119.757 161.415 1.00 12733. ? 182 ILE A CG1   1 
ATOM   1177  C  CG2   . ILE A 1 182 ? 135.981 119.833 162.489 1.00 12750. ? 182 ILE A CG2   1 
ATOM   1178  C  CD1   . ILE A 1 182 ? 132.863 119.618 162.640 1.00 12736. ? 182 ILE A CD1   1 
ATOM   1179  N  N     . GLY A 1 183 ? 134.814 116.856 159.394 1.00 12720. ? 183 GLY A N     1 
ATOM   1180  C  CA    . GLY A 1 183 ? 133.919 115.984 158.667 1.00 12734. ? 183 GLY A CA    1 
ATOM   1181  C  C     . GLY A 1 183 ? 133.012 115.228 159.612 1.00 12730. ? 183 GLY A C     1 
ATOM   1182  O  O     . GLY A 1 183 ? 133.483 114.576 160.547 1.00 12748. ? 183 GLY A O     1 
ATOM   1183  N  N     . VAL A 1 184 ? 131.708 115.304 159.375 1.00 12729. ? 184 VAL A N     1 
ATOM   1184  C  CA    . VAL A 1 184 ? 130.700 114.802 160.297 1.00 12726. ? 184 VAL A CA    1 
ATOM   1185  C  C     . VAL A 1 184 ? 129.928 113.680 159.620 1.00 12734. ? 184 VAL A C     1 
ATOM   1186  O  O     . VAL A 1 184 ? 129.405 113.858 158.515 1.00 12765. ? 184 VAL A O     1 
ATOM   1187  C  CB    . VAL A 1 184 ? 129.746 115.923 160.747 1.00 12735. ? 184 VAL A CB    1 
ATOM   1188  C  CG1   . VAL A 1 184 ? 128.638 115.361 161.604 1.00 12745. ? 184 VAL A CG1   1 
ATOM   1189  C  CG2   . VAL A 1 184 ? 130.511 116.993 161.499 1.00 12749. ? 184 VAL A CG2   1 
ATOM   1190  N  N     . GLN A 1 185 ? 129.854 112.534 160.284 1.00 12734. ? 185 GLN A N     1 
ATOM   1191  C  CA    . GLN A 1 185 ? 129.030 111.416 159.846 1.00 12736. ? 185 GLN A CA    1 
ATOM   1192  C  C     . GLN A 1 185 ? 127.890 111.252 160.837 1.00 12732. ? 185 GLN A C     1 
ATOM   1193  O  O     . GLN A 1 185 ? 128.128 111.078 162.035 1.00 12750. ? 185 GLN A O     1 
ATOM   1194  C  CB    . GLN A 1 185 ? 129.847 110.130 159.754 1.00 12745. ? 185 GLN A CB    1 
ATOM   1195  C  CG    . GLN A 1 185 ? 129.020 108.905 159.430 1.00 12741. ? 185 GLN A CG    1 
ATOM   1196  C  CD    . GLN A 1 185 ? 129.775 107.619 159.668 1.00 12738. ? 185 GLN A CD    1 
ATOM   1197  O  OE1   . GLN A 1 185 ? 130.995 107.622 159.819 1.00 12738. ? 185 GLN A OE1   1 
ATOM   1198  N  NE2   . GLN A 1 185 ? 129.053 106.507 159.701 1.00 12742. ? 185 GLN A NE2   1 
ATOM   1199  N  N     . GLY A 1 186 ? 126.661 111.302 160.343 1.00 12730. ? 186 GLY A N     1 
ATOM   1200  C  CA    . GLY A 1 186 ? 125.535 111.217 161.246 1.00 12735. ? 186 GLY A CA    1 
ATOM   1201  C  C     . GLY A 1 186 ? 124.217 111.172 160.511 1.00 12741. ? 186 GLY A C     1 
ATOM   1202  O  O     . GLY A 1 186 ? 124.164 111.044 159.288 1.00 12767. ? 186 GLY A O     1 
ATOM   1203  N  N     . ASN A 1 187 ? 123.148 111.282 161.290 1.00 12733. ? 187 ASN A N     1 
ATOM   1204  C  CA    . ASN A 1 187 ? 121.786 111.201 160.789 1.00 12730. ? 187 ASN A CA    1 
ATOM   1205  C  C     . ASN A 1 187 ? 121.134 112.575 160.751 1.00 12739. ? 187 ASN A C     1 
ATOM   1206  O  O     . ASN A 1 187 ? 121.355 113.389 161.651 1.00 12761. ? 187 ASN A O     1 
ATOM   1207  C  CB    . ASN A 1 187 ? 120.934 110.275 161.662 1.00 12742. ? 187 ASN A CB    1 
ATOM   1208  C  CG    . ASN A 1 187 ? 121.643 108.989 162.012 1.00 12747. ? 187 ASN A CG    1 
ATOM   1209  O  OD1   . ASN A 1 187 ? 121.866 108.691 163.184 1.00 12758. ? 187 ASN A OD1   1 
ATOM   1210  N  ND2   . ASN A 1 187 ? 121.997 108.214 160.998 1.00 12759. ? 187 ASN A ND2   1 
ATOM   1211  N  N     . PRO A 1 188 ? 120.321 112.861 159.740 1.00 12730. ? 188 PRO A N     1 
ATOM   1212  C  CA    . PRO A 1 188 ? 119.585 114.127 159.732 1.00 12733. ? 188 PRO A CA    1 
ATOM   1213  C  C     . PRO A 1 188 ? 118.559 114.171 160.851 1.00 12734. ? 188 PRO A C     1 
ATOM   1214  O  O     . PRO A 1 188 ? 118.042 113.143 161.293 1.00 12757. ? 188 PRO A O     1 
ATOM   1215  C  CB    . PRO A 1 188 ? 118.909 114.136 158.358 1.00 12749. ? 188 PRO A CB    1 
ATOM   1216  C  CG    . PRO A 1 188 ? 118.809 112.704 157.984 1.00 12757. ? 188 PRO A CG    1 
ATOM   1217  C  CD    . PRO A 1 188 ? 120.019 112.039 158.558 1.00 12756. ? 188 PRO A CD    1 
ATOM   1218  N  N     . GLY A 1 189 ? 118.270 115.380 161.313 1.00 12729. ? 189 GLY A N     1 
ATOM   1219  C  CA    . GLY A 1 189 ? 117.260 115.546 162.340 1.00 12738. ? 189 GLY A CA    1 
ATOM   1220  C  C     . GLY A 1 189 ? 116.904 117.006 162.478 1.00 12737. ? 189 GLY A C     1 
ATOM   1221  O  O     . GLY A 1 189 ? 117.504 117.880 161.846 1.00 12754. ? 189 GLY A O     1 
ATOM   1222  N  N     . LYS A 1 190 ? 115.879 117.275 163.289 1.00 12739. ? 190 LYS A N     1 
ATOM   1223  C  CA    . LYS A 1 190 ? 115.455 118.680 163.522 1.00 12738. ? 190 LYS A CA    1 
ATOM   1224  C  C     . LYS A 1 190 ? 115.265 118.880 165.031 1.00 12741. ? 190 LYS A C     1 
ATOM   1225  O  O     . LYS A 1 190 ? 114.597 118.033 165.661 1.00 12756. ? 190 LYS A O     1 
ATOM   1226  C  CB    . LYS A 1 190 ? 114.181 119.004 162.736 1.00 12750. ? 190 LYS A CB    1 
ATOM   1227  C  CG    . LYS A 1 190 ? 113.786 120.471 162.772 1.00 12761. ? 190 LYS A CG    1 
ATOM   1228  C  CD    . LYS A 1 190 ? 113.159 120.942 161.466 1.00 12753. ? 190 LYS A CD    1 
ATOM   1229  C  CE    . LYS A 1 190 ? 114.035 120.638 160.292 1.00 12737. ? 190 LYS A CE    1 
ATOM   1230  N  NZ    . LYS A 1 190 ? 113.389 120.972 159.020 1.00 12744. ? 190 LYS A NZ    1 
ATOM   1231  N  N     . THR A 1 191 ? 115.833 119.955 165.583 1.00 12734. ? 191 THR A N     1 
ATOM   1232  C  CA    . THR A 1 191 ? 115.757 120.189 167.041 1.00 12684. ? 191 THR A CA    1 
ATOM   1233  C  C     . THR A 1 191 ? 114.340 120.557 167.425 1.00 12726. ? 191 THR A C     1 
ATOM   1234  O  O     . THR A 1 191 ? 113.562 120.942 166.525 1.00 12778. ? 191 THR A O     1 
ATOM   1235  C  CB    . THR A 1 191 ? 116.755 121.283 167.414 1.00 12640. ? 191 THR A CB    1 
ATOM   1236  O  OG1   . THR A 1 191 ? 116.266 122.462 166.783 1.00 12666. ? 191 THR A OG1   1 
ATOM   1237  C  CG2   . THR A 1 191 ? 118.159 120.965 166.933 1.00 12688. ? 191 THR A CG2   1 
ATOM   1238  N  N     . LYS A 1 192 ? 114.013 120.462 168.717 1.00 13229. ? 192 LYS A N     1 
ATOM   1239  C  CA    . LYS A 1 192 ? 112.645 120.781 169.200 1.00 13264. ? 192 LYS A CA    1 
ATOM   1240  C  C     . LYS A 1 192 ? 112.254 122.187 168.721 1.00 13293. ? 192 LYS A C     1 
ATOM   1241  O  O     . LYS A 1 192 ? 111.065 122.394 168.396 1.00 13321. ? 192 LYS A O     1 
ATOM   1242  C  CB    . LYS A 1 192 ? 112.598 120.715 170.730 1.00 13254. ? 192 LYS A CB    1 
ATOM   1243  C  CG    . LYS A 1 192 ? 112.790 119.333 171.338 1.00 13282. ? 192 LYS A CG    1 
ATOM   1244  C  CD    . LYS A 1 192 ? 112.633 119.339 172.854 1.00 13243. ? 192 LYS A CD    1 
ATOM   1245  C  CE    . LYS A 1 192 ? 112.700 117.974 173.462 1.00 13298. ? 192 LYS A CE    1 
ATOM   1246  N  NZ    . LYS A 1 192 ? 114.051 117.409 173.420 1.00 13317. ? 192 LYS A NZ    1 
ATOM   1247  N  N     . LYS A 1 193 ? 113.217 123.112 168.688 1.00 13225. ? 193 LYS A N     1 
ATOM   1248  C  CA    . LYS A 1 193 ? 112.942 124.500 168.234 1.00 13227. ? 193 LYS A CA    1 
ATOM   1249  C  C     . LYS A 1 193 ? 112.471 124.474 166.773 1.00 13211. ? 193 LYS A C     1 
ATOM   1250  O  O     . LYS A 1 193 ? 111.562 125.263 166.432 1.00 13195. ? 193 LYS A O     1 
ATOM   1251  C  CB    . LYS A 1 193 ? 114.203 125.360 168.366 1.00 13139. ? 193 LYS A CB    1 
ATOM   1252  C  CG    . LYS A 1 193 ? 114.918 125.257 169.705 1.00 13113. ? 193 LYS A CG    1 
ATOM   1253  C  CD    . LYS A 1 193 ? 114.040 125.622 170.895 1.00 13161. ? 193 LYS A CD    1 
ATOM   1254  C  CE    . LYS A 1 193 ? 114.723 125.350 172.196 1.00 13178. ? 193 LYS A CE    1 
ATOM   1255  N  NZ    . LYS A 1 193 ? 116.018 126.031 172.278 1.00 13072. ? 193 LYS A NZ    1 
ATOM   1256  N  N     . GLY A 1 194 ? 113.064 123.606 165.948 1.00 12779. ? 194 GLY A N     1 
ATOM   1257  C  CA    . GLY A 1 194 ? 112.715 123.551 164.515 1.00 12770. ? 194 GLY A CA    1 
ATOM   1258  C  C     . GLY A 1 194 ? 113.925 123.880 163.666 1.00 12755. ? 194 GLY A C     1 
ATOM   1259  O  O     . GLY A 1 194 ? 113.741 124.458 162.575 1.00 12759. ? 194 GLY A O     1 
ATOM   1260  N  N     . GLU A 1 195 ? 115.121 123.526 164.144 1.00 12725. ? 195 GLU A N     1 
ATOM   1261  C  CA    . GLU A 1 195 ? 116.350 123.835 163.424 1.00 12715. ? 195 GLU A CA    1 
ATOM   1262  C  C     . GLU A 1 195 ? 116.902 122.553 162.822 1.00 12726. ? 195 GLU A C     1 
ATOM   1263  O  O     . GLU A 1 195 ? 117.135 121.578 163.543 1.00 12735. ? 195 GLU A O     1 
ATOM   1264  C  CB    . GLU A 1 195 ? 117.381 124.484 164.347 1.00 12657. ? 195 GLU A CB    1 
ATOM   1265  C  CG    . GLU A 1 195 ? 118.745 124.666 163.710 1.00 12657. ? 195 GLU A CG    1 
ATOM   1266  C  CD    . GLU A 1 195 ? 118.905 126.020 163.057 1.00 12657. ? 195 GLU A CD    1 
ATOM   1267  O  OE1   . GLU A 1 195 ? 117.979 126.849 163.173 1.00 12640. ? 195 GLU A OE1   1 
ATOM   1268  O  OE2   . GLU A 1 195 ? 119.955 126.256 162.424 1.00 12706. ? 195 GLU A OE2   1 
ATOM   1269  N  N     . LEU A 1 196 ? 117.108 122.558 161.509 1.00 12737. ? 196 LEU A N     1 
ATOM   1270  C  CA    . LEU A 1 196 ? 117.700 121.409 160.842 1.00 12742. ? 196 LEU A CA    1 
ATOM   1271  C  C     . LEU A 1 196 ? 119.136 121.214 161.308 1.00 12741. ? 196 LEU A C     1 
ATOM   1272  O  O     . LEU A 1 196 ? 119.902 122.173 161.423 1.00 12752. ? 196 LEU A O     1 
ATOM   1273  C  CB    . LEU A 1 196 ? 117.662 121.597 159.327 1.00 12740. ? 196 LEU A CB    1 
ATOM   1274  C  CG    . LEU A 1 196 ? 118.179 120.438 158.475 1.00 12729. ? 196 LEU A CG    1 
ATOM   1275  C  CD1   . LEU A 1 196 ? 117.443 119.155 158.807 1.00 12741. ? 196 LEU A CD1   1 
ATOM   1276  C  CD2   . LEU A 1 196 ? 118.053 120.765 157.003 1.00 12750. ? 196 LEU A CD2   1 
ATOM   1277  N  N     . SER A 1 197 ? 119.502 119.963 161.568 1.00 12744. ? 197 SER A N     1 
ATOM   1278  C  CA    . SER A 1 197 ? 120.830 119.652 162.073 1.00 12739. ? 197 SER A CA    1 
ATOM   1279  C  C     . SER A 1 197 ? 121.165 118.219 161.697 1.00 12737. ? 197 SER A C     1 
ATOM   1280  O  O     . SER A 1 197 ? 120.306 117.452 161.259 1.00 12757. ? 197 SER A O     1 
ATOM   1281  C  CB    . SER A 1 197 ? 120.910 119.855 163.587 1.00 12748. ? 197 SER A CB    1 
ATOM   1282  O  OG    . SER A 1 197 ? 119.998 119.010 164.263 1.00 12746. ? 197 SER A OG    1 
ATOM   1283  N  N     . ILE A 1 198 ? 122.436 117.871 161.859 1.00 12730. ? 198 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 198 ? 122.905 116.505 161.679 1.00 12732. ? 198 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 198 ? 123.435 116.016 163.020 1.00 12737. ? 198 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 198 ? 124.373 116.599 163.576 1.00 12745. ? 198 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 198 ? 123.971 116.400 160.575 1.00 12733. ? 198 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 198 ? 124.575 114.996 160.545 1.00 12745. ? 198 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 198 ? 125.040 117.472 160.729 1.00 12754. ? 198 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 198 ? 125.190 114.630 159.221 1.00 12750. ? 198 ILE A CD1   1 
ATOM   1291  N  N     . ILE A 1 199 ? 122.818 114.966 163.548 1.00 12735. ? 199 ILE A N     1 
ATOM   1292  C  CA    . ILE A 1 199 ? 123.255 114.356 164.797 1.00 12728. ? 199 ILE A CA    1 
ATOM   1293  C  C     . ILE A 1 199 ? 124.410 113.423 164.463 1.00 12733. ? 199 ILE A C     1 
ATOM   1294  O  O     . ILE A 1 199 ? 124.214 112.431 163.746 1.00 12750. ? 199 ILE A O     1 
ATOM   1295  C  CB    . ILE A 1 199 ? 122.108 113.605 165.487 1.00 12734. ? 199 ILE A CB    1 
ATOM   1296  C  CG1   . ILE A 1 199 ? 121.045 114.589 165.972 1.00 12739. ? 199 ILE A CG1   1 
ATOM   1297  C  CG2   . ILE A 1 199 ? 122.635 112.784 166.641 1.00 12756. ? 199 ILE A CG2   1 
ATOM   1298  C  CD1   . ILE A 1 199 ? 119.840 114.670 165.071 1.00 12756. ? 199 ILE A CD1   1 
ATOM   1299  N  N     . PRO A 1 200 ? 125.619 113.695 164.951 1.00 12727. ? 200 PRO A N     1 
ATOM   1300  C  CA    . PRO A 1 200 ? 126.790 112.938 164.506 1.00 12735. ? 200 PRO A CA    1 
ATOM   1301  C  C     . PRO A 1 200 ? 127.002 111.643 165.271 1.00 12733. ? 200 PRO A C     1 
ATOM   1302  O  O     . PRO A 1 200 ? 126.835 111.566 166.489 1.00 12744. ? 200 PRO A O     1 
ATOM   1303  C  CB    . PRO A 1 200 ? 127.941 113.915 164.772 1.00 12743. ? 200 PRO A CB    1 
ATOM   1304  C  CG    . PRO A 1 200 ? 127.487 114.706 165.930 1.00 12745. ? 200 PRO A CG    1 
ATOM   1305  C  CD    . PRO A 1 200 ? 125.985 114.782 165.873 1.00 12746. ? 200 PRO A CD    1 
ATOM   1306  N  N     . TYR A 1 201 ? 127.371 110.609 164.521 1.00 12741. ? 201 TYR A N     1 
ATOM   1307  C  CA    . TYR A 1 201 ? 127.867 109.370 165.095 1.00 12732. ? 201 TYR A CA    1 
ATOM   1308  C  C     . TYR A 1 201 ? 129.383 109.354 165.217 1.00 12726. ? 201 TYR A C     1 
ATOM   1309  O  O     . TYR A 1 201 ? 129.918 108.588 166.025 1.00 12739. ? 201 TYR A O     1 
ATOM   1310  C  CB    . TYR A 1 201 ? 127.405 108.179 164.246 1.00 12742. ? 201 TYR A CB    1 
ATOM   1311  C  CG    . TYR A 1 201 ? 127.926 106.839 164.703 1.00 12728. ? 201 TYR A CG    1 
ATOM   1312  C  CD1   . TYR A 1 201 ? 127.347 106.177 165.774 1.00 12743. ? 201 TYR A CD1   1 
ATOM   1313  C  CD2   . TYR A 1 201 ? 128.992 106.231 164.056 1.00 12733. ? 201 TYR A CD2   1 
ATOM   1314  C  CE1   . TYR A 1 201 ? 127.818 104.952 166.192 1.00 12754. ? 201 TYR A CE1   1 
ATOM   1315  C  CE2   . TYR A 1 201 ? 129.470 105.007 164.467 1.00 12743. ? 201 TYR A CE2   1 
ATOM   1316  C  CZ    . TYR A 1 201 ? 128.879 104.371 165.535 1.00 12753. ? 201 TYR A CZ    1 
ATOM   1317  O  OH    . TYR A 1 201 ? 129.351 103.148 165.949 1.00 12752. ? 201 TYR A OH    1 
ATOM   1318  N  N     . GLU A 1 202 ? 130.066 110.189 164.462 1.00 12724. ? 202 GLU A N     1 
ATOM   1319  C  CA    . GLU A 1 202 ? 131.551 110.242 164.504 1.00 12738. ? 202 GLU A CA    1 
ATOM   1320  C  C     . GLU A 1 202 ? 132.036 111.535 163.832 1.00 12743. ? 202 GLU A C     1 
ATOM   1321  O  O     . GLU A 1 202 ? 131.669 111.765 162.658 1.00 12766. ? 202 GLU A O     1 
ATOM   1322  C  CB    . GLU A 1 202 ? 132.148 109.017 163.812 1.00 12745. ? 202 GLU A CB    1 
ATOM   1323  C  CG    . GLU A 1 202 ? 133.667 108.945 163.925 1.00 12750. ? 202 GLU A CG    1 
ATOM   1324  C  CD    . GLU A 1 202 ? 134.264 107.698 163.299 1.00 12751. ? 202 GLU A CD    1 
ATOM   1325  O  OE1   . GLU A 1 202 ? 133.489 106.875 162.769 1.00 12749. ? 202 GLU A OE1   1 
ATOM   1326  O  OE2   . GLU A 1 202 ? 135.504 107.551 163.343 1.00 12756. ? 202 GLU A OE2   1 
ATOM   1327  N  N     . ILE A 1 203 ? 132.814 112.336 164.518 1.00 12735. ? 203 ILE A N     1 
ATOM   1328  C  CA    . ILE A 1 203 ? 133.362 113.581 163.996 1.00 12727. ? 203 ILE A CA    1 
ATOM   1329  C  C     . ILE A 1 203 ? 134.868 113.421 163.877 1.00 12734. ? 203 ILE A C     1 
ATOM   1330  O  O     . ILE A 1 203 ? 135.530 113.009 164.837 1.00 12755. ? 203 ILE A O     1 
ATOM   1331  C  CB    . ILE A 1 203 ? 133.016 114.781 164.894 1.00 12724. ? 203 ILE A CB    1 
ATOM   1332  C  CG1   . ILE A 1 203 ? 131.505 114.890 165.086 1.00 12731. ? 203 ILE A CG1   1 
ATOM   1333  C  CG2   . ILE A 1 203 ? 133.570 116.064 164.303 1.00 12750. ? 203 ILE A CG2   1 
ATOM   1334  C  CD1   . ILE A 1 203 ? 131.092 116.043 165.963 1.00 12737. ? 203 ILE A CD1   1 
ATOM   1335  N  N     . THR A 1 204 ? 135.408 113.740 162.705 1.00 12726. ? 204 THR A N     1 
ATOM   1336  C  CA    . THR A 1 204 ? 136.839 113.665 162.453 1.00 12732. ? 204 THR A CA    1 
ATOM   1337  C  C     . THR A 1 204 ? 137.360 115.050 162.107 1.00 12735. ? 204 THR A C     1 
ATOM   1338  O  O     . THR A 1 204 ? 136.772 115.748 161.276 1.00 12761. ? 204 THR A O     1 
ATOM   1339  C  CB    . THR A 1 204 ? 137.157 112.691 161.318 1.00 12747. ? 204 THR A CB    1 
ATOM   1340  O  OG1   . THR A 1 204 ? 137.065 113.375 160.064 1.00 12753. ? 204 THR A OG1   1 
ATOM   1341  C  CG2   . THR A 1 204 ? 136.185 111.526 161.325 1.00 12751. ? 204 THR A CG2   1 
ATOM   1342  N  N     . LEU A 1 205 ? 138.458 115.444 162.744 1.00 12731. ? 205 LEU A N     1 
ATOM   1343  C  CA    . LEU A 1 205 ? 139.099 116.717 162.447 1.00 12724. ? 205 LEU A CA    1 
ATOM   1344  C  C     . LEU A 1 205 ? 139.888 116.587 161.152 1.00 12739. ? 205 LEU A C     1 
ATOM   1345  O  O     . LEU A 1 205 ? 140.803 115.763 161.058 1.00 12755. ? 205 LEU A O     1 
ATOM   1346  C  CB    . LEU A 1 205 ? 140.011 117.133 163.598 1.00 12732. ? 205 LEU A CB    1 
ATOM   1347  C  CG    . LEU A 1 205 ? 140.919 118.340 163.364 1.00 12734. ? 205 LEU A CG    1 
ATOM   1348  C  CD1   . LEU A 1 205 ? 140.102 119.562 163.002 1.00 12748. ? 205 LEU A CD1   1 
ATOM   1349  C  CD2   . LEU A 1 205 ? 141.768 118.610 164.590 1.00 12746. ? 205 LEU A CD2   1 
ATOM   1350  N  N     . LEU A 1 206 ? 139.533 117.391 160.152 1.00 12743. ? 206 LEU A N     1 
ATOM   1351  C  CA    . LEU A 1 206 ? 140.196 117.313 158.858 1.00 12695. ? 206 LEU A CA    1 
ATOM   1352  C  C     . LEU A 1 206 ? 141.331 118.318 158.724 1.00 12690. ? 206 LEU A C     1 
ATOM   1353  O  O     . LEU A 1 206 ? 142.390 117.985 158.183 1.00 12702. ? 206 LEU A O     1 
ATOM   1354  C  CB    . LEU A 1 206 ? 139.182 117.524 157.733 1.00 12682. ? 206 LEU A CB    1 
ATOM   1355  C  CG    . LEU A 1 206 ? 138.100 116.454 157.597 1.00 12694. ? 206 LEU A CG    1 
ATOM   1356  C  CD1   . LEU A 1 206 ? 137.252 116.710 156.370 1.00 12709. ? 206 LEU A CD1   1 
ATOM   1357  C  CD2   . LEU A 1 206 ? 138.723 115.076 157.535 1.00 12708. ? 206 LEU A CD2   1 
ATOM   1358  N  N     . SER A 1 207 ? 141.133 119.541 159.196 1.00 12716. ? 207 SER A N     1 
ATOM   1359  C  CA    . SER A 1 207 ? 142.180 120.551 159.120 1.00 12704. ? 207 SER A CA    1 
ATOM   1360  C  C     . SER A 1 207 ? 141.992 121.594 160.214 1.00 12714. ? 207 SER A C     1 
ATOM   1361  O  O     . SER A 1 207 ? 141.079 122.423 160.129 1.00 12729. ? 207 SER A O     1 
ATOM   1362  C  CB    . SER A 1 207 ? 142.185 121.214 157.743 1.00 12569. ? 207 SER A CB    1 
ATOM   1363  O  OG    . SER A 1 207 ? 143.411 121.880 157.502 1.00 12507. ? 207 SER A OG    1 
ATOM   1364  N  N     . PRO A 1 208 ? 142.826 121.586 161.249 1.00 12726. ? 208 PRO A N     1 
ATOM   1365  C  CA    . PRO A 1 208 ? 142.670 122.568 162.326 1.00 12733. ? 208 PRO A CA    1 
ATOM   1366  C  C     . PRO A 1 208 ? 143.031 123.974 161.877 1.00 12717. ? 208 PRO A C     1 
ATOM   1367  O  O     . PRO A 1 208 ? 143.832 124.177 160.961 1.00 12699. ? 208 PRO A O     1 
ATOM   1368  C  CB    . PRO A 1 208 ? 143.639 122.066 163.401 1.00 12735. ? 208 PRO A CB    1 
ATOM   1369  C  CG    . PRO A 1 208 ? 144.662 121.306 162.646 1.00 12732. ? 208 PRO A CG    1 
ATOM   1370  C  CD    . PRO A 1 208 ? 143.943 120.662 161.500 1.00 12741. ? 208 PRO A CD    1 
ATOM   1371  N  N     . CYS A 1 209 ? 142.426 124.954 162.542 1.00 12722. ? 209 CYS A N     1 
ATOM   1372  C  CA    . CYS A 1 209 ? 142.709 126.364 162.317 1.00 12688. ? 209 CYS A CA    1 
ATOM   1373  C  C     . CYS A 1 209 ? 143.550 126.888 163.471 1.00 12740. ? 209 CYS A C     1 
ATOM   1374  O  O     . CYS A 1 209 ? 143.177 126.726 164.637 1.00 12772. ? 209 CYS A O     1 
ATOM   1375  C  CB    . CYS A 1 209 ? 141.416 127.171 162.192 1.00 12732. ? 209 CYS A CB    1 
ATOM   1376  S  SG    . CYS A 1 209 ? 141.646 128.925 161.827 1.00 12728. ? 209 CYS A SG    1 
ATOM   1377  N  N     . LEU A 1 210 ? 144.681 127.513 163.148 1.00 12739. ? 210 LEU A N     1 
ATOM   1378  C  CA    . LEU A 1 210 ? 145.641 127.953 164.150 1.00 12738. ? 210 LEU A CA    1 
ATOM   1379  C  C     . LEU A 1 210 ? 145.554 129.443 164.453 1.00 12740. ? 210 LEU A C     1 
ATOM   1380  O  O     . LEU A 1 210 ? 146.454 129.981 165.101 1.00 12749. ? 210 LEU A O     1 
ATOM   1381  C  CB    . LEU A 1 210 ? 147.063 127.603 163.710 1.00 12729. ? 210 LEU A CB    1 
ATOM   1382  C  CG    . LEU A 1 210 ? 147.287 126.254 163.030 1.00 12731. ? 210 LEU A CG    1 
ATOM   1383  C  CD1   . LEU A 1 210 ? 148.664 126.213 162.398 1.00 12744. ? 210 LEU A CD1   1 
ATOM   1384  C  CD2   . LEU A 1 210 ? 147.120 125.117 164.016 1.00 12749. ? 210 LEU A CD2   1 
ATOM   1385  N  N     . HIS A 1 211 ? 144.503 130.120 164.004 1.00 12739. ? 211 HIS A N     1 
ATOM   1386  C  CA    . HIS A 1 211 ? 144.349 131.549 164.231 1.00 12736. ? 211 HIS A CA    1 
ATOM   1387  C  C     . HIS A 1 211 ? 142.961 131.838 164.780 1.00 12737. ? 211 HIS A C     1 
ATOM   1388  O  O     . HIS A 1 211 ? 142.022 131.067 164.569 1.00 12755. ? 211 HIS A O     1 
ATOM   1389  C  CB    . HIS A 1 211 ? 144.569 132.350 162.943 1.00 12704. ? 211 HIS A CB    1 
ATOM   1390  C  CG    . HIS A 1 211 ? 145.998 132.413 162.504 1.00 12699. ? 211 HIS A CG    1 
ATOM   1391  N  ND1   . HIS A 1 211 ? 146.900 133.308 163.035 1.00 12695. ? 211 HIS A ND1   1 
ATOM   1392  C  CD2   . HIS A 1 211 ? 146.678 131.698 161.578 1.00 12707. ? 211 HIS A CD2   1 
ATOM   1393  C  CE1   . HIS A 1 211 ? 148.077 133.138 162.459 1.00 12737. ? 211 HIS A CE1   1 
ATOM   1394  N  NE2   . HIS A 1 211 ? 147.968 132.168 161.570 1.00 12715. ? 211 HIS A NE2   1 
ATOM   1395  N  N     . MET A 1 212 ? 142.842 132.954 165.496 1.00 12729. ? 212 MET A N     1 
ATOM   1396  C  CA    . MET A 1 212 ? 141.537 133.395 165.967 1.00 12715. ? 212 MET A CA    1 
ATOM   1397  C  C     . MET A 1 212 ? 140.648 133.738 164.780 1.00 12715. ? 212 MET A C     1 
ATOM   1398  O  O     . MET A 1 212 ? 141.060 134.464 163.871 1.00 12701. ? 212 MET A O     1 
ATOM   1399  C  CB    . MET A 1 212 ? 141.672 134.607 166.885 1.00 12590. ? 212 MET A CB    1 
ATOM   1400  C  CG    . MET A 1 212 ? 142.294 134.320 168.236 1.00 12573. ? 212 MET A CG    1 
ATOM   1401  S  SD    . MET A 1 212 ? 142.288 135.781 169.289 1.00 12326. ? 212 MET A SD    1 
ATOM   1402  C  CE    . MET A 1 212 ? 143.339 135.243 170.630 1.00 12508. ? 212 MET A CE    1 
ATOM   1403  N  N     . LEU A 1 213 ? 139.426 133.212 164.791 1.00 12733. ? 213 LEU A N     1 
ATOM   1404  C  CA    . LEU A 1 213 ? 138.475 133.455 163.721 1.00 12743. ? 213 LEU A CA    1 
ATOM   1405  C  C     . LEU A 1 213 ? 137.472 134.501 164.173 1.00 12713. ? 213 LEU A C     1 
ATOM   1406  O  O     . LEU A 1 213 ? 136.782 134.282 165.181 1.00 12666. ? 213 LEU A O     1 
ATOM   1407  C  CB    . LEU A 1 213 ? 137.764 132.164 163.340 1.00 12735. ? 213 LEU A CB    1 
ATOM   1408  C  CG    . LEU A 1 213 ? 136.867 132.200 162.105 1.00 12734. ? 213 LEU A CG    1 
ATOM   1409  C  CD1   . LEU A 1 213 ? 137.660 131.809 160.874 1.00 12737. ? 213 LEU A CD1   1 
ATOM   1410  C  CD2   . LEU A 1 213 ? 135.679 131.277 162.291 1.00 12743. ? 213 LEU A CD2   1 
ATOM   1411  N  N     . PRO A 1 214 ? 137.364 135.641 163.493 1.00 12716. ? 214 PRO A N     1 
ATOM   1412  C  CA    . PRO A 1 214 ? 136.442 136.687 163.942 1.00 12679. ? 214 PRO A CA    1 
ATOM   1413  C  C     . PRO A 1 214 ? 134.995 136.222 163.912 1.00 12724. ? 214 PRO A C     1 
ATOM   1414  O  O     . PRO A 1 214 ? 134.590 135.396 163.092 1.00 12743. ? 214 PRO A O     1 
ATOM   1415  C  CB    . PRO A 1 214 ? 136.684 137.816 162.934 1.00 12630. ? 214 PRO A CB    1 
ATOM   1416  C  CG    . PRO A 1 214 ? 138.091 137.590 162.491 1.00 12608. ? 214 PRO A CG    1 
ATOM   1417  C  CD    . PRO A 1 214 ? 138.171 136.098 162.352 1.00 12732. ? 214 PRO A CD    1 
ATOM   1418  N  N     . HIS A 1 215 ? 134.208 136.812 164.820 1.00 12862. ? 215 HIS A N     1 
ATOM   1419  C  CA    . HIS A 1 215 ? 132.774 136.458 164.925 1.00 12888. ? 215 HIS A CA    1 
ATOM   1420  C  C     . HIS A 1 215 ? 132.028 137.084 163.758 1.00 12910. ? 215 HIS A C     1 
ATOM   1421  O  O     . HIS A 1 215 ? 132.337 138.212 163.378 1.00 12922. ? 215 HIS A O     1 
ATOM   1422  C  CB    . HIS A 1 215 ? 132.200 136.937 166.254 1.00 12810. ? 215 HIS A CB    1 
ATOM   1423  C  CG    . HIS A 1 215 ? 130.976 136.192 166.651 1.00 12803. ? 215 HIS A CG    1 
ATOM   1424  N  ND1   . HIS A 1 215 ? 129.706 136.633 166.365 1.00 12798. ? 215 HIS A ND1   1 
ATOM   1425  C  CD2   . HIS A 1 215 ? 130.827 135.040 167.304 1.00 12750. ? 215 HIS A CD2   1 
ATOM   1426  C  CE1   . HIS A 1 215 ? 128.828 135.764 166.832 1.00 12703. ? 215 HIS A CE1   1 
ATOM   1427  N  NE2   . HIS A 1 215 ? 129.489 134.788 167.406 1.00 12707. ? 215 HIS A NE2   1 
ATOM   1428  N  N     . LEU A 1 216 ? 131.045 136.383 163.225 1.00 12760. ? 216 LEU A N     1 
ATOM   1429  C  CA    . LEU A 1 216 ? 130.305 136.856 162.062 1.00 12745. ? 216 LEU A CA    1 
ATOM   1430  C  C     . LEU A 1 216 ? 129.450 138.080 162.356 1.00 12739. ? 216 LEU A C     1 
ATOM   1431  O  O     . LEU A 1 216 ? 129.066 138.779 161.413 1.00 12747. ? 216 LEU A O     1 
ATOM   1432  C  CB    . LEU A 1 216 ? 129.419 135.741 161.507 1.00 12744. ? 216 LEU A CB    1 
ATOM   1433  C  CG    . LEU A 1 216 ? 130.126 134.619 160.750 1.00 12743. ? 216 LEU A CG    1 
ATOM   1434  C  CD1   . LEU A 1 216 ? 129.199 133.434 160.576 1.00 12743. ? 216 LEU A CD1   1 
ATOM   1435  C  CD2   . LEU A 1 216 ? 130.614 135.114 159.404 1.00 12759. ? 216 LEU A CD2   1 
ATOM   1436  N  N     . HIS A 1 217 ? 129.239 138.416 163.618 1.00 12731. ? 217 HIS A N     1 
ATOM   1437  C  CA    . HIS A 1 217 ? 128.354 139.554 163.919 1.00 12732. ? 217 HIS A CA    1 
ATOM   1438  C  C     . HIS A 1 217 ? 129.099 140.847 163.641 1.00 12747. ? 217 HIS A C     1 
ATOM   1439  O  O     . HIS A 1 217 ? 128.448 141.863 163.373 1.00 12754. ? 217 HIS A O     1 
ATOM   1440  C  CB    . HIS A 1 217 ? 127.955 139.594 165.383 1.00 12594. ? 217 HIS A CB    1 
ATOM   1441  C  CG    . HIS A 1 217 ? 127.301 140.867 165.786 1.00 12568. ? 217 HIS A CG    1 
ATOM   1442  N  ND1   . HIS A 1 217 ? 125.964 141.112 165.578 1.00 12548. ? 217 HIS A ND1   1 
ATOM   1443  C  CD2   . HIS A 1 217 ? 127.794 141.970 166.343 1.00 12537. ? 217 HIS A CD2   1 
ATOM   1444  C  CE1   . HIS A 1 217 ? 125.673 142.324 166.016 1.00 12508. ? 217 HIS A CE1   1 
ATOM   1445  N  NE2   . HIS A 1 217 ? 126.770 142.859 166.489 1.00 12491. ? 217 HIS A NE2   1 
ATOM   1446  N  N     . PHE A 1 218 ? 130.426 140.821 163.724 1.00 12750. ? 218 PHE A N     1 
ATOM   1447  C  CA    . PHE A 1 218 ? 131.245 142.027 163.444 1.00 12698. ? 218 PHE A CA    1 
ATOM   1448  C  C     . PHE A 1 218 ? 131.892 141.840 162.096 1.00 12692. ? 218 PHE A C     1 
ATOM   1449  O  O     . PHE A 1 218 ? 131.930 142.796 161.331 1.00 12698. ? 218 PHE A O     1 
ATOM   1450  C  CB    . PHE A 1 218 ? 132.232 142.205 164.590 1.00 12601. ? 218 PHE A CB    1 
ATOM   1451  C  CG    . PHE A 1 218 ? 131.694 142.311 166.006 1.00 12633. ? 218 PHE A CG    1 
ATOM   1452  C  CD1   . PHE A 1 218 ? 131.224 143.518 166.501 1.00 12612. ? 218 PHE A CD1   1 
ATOM   1453  C  CD2   . PHE A 1 218 ? 131.731 141.222 166.860 1.00 12545. ? 218 PHE A CD2   1 
ATOM   1454  C  CE1   . PHE A 1 218 ? 130.758 143.616 167.797 1.00 12585. ? 218 PHE A CE1   1 
ATOM   1455  C  CE2   . PHE A 1 218 ? 131.274 141.332 168.158 1.00 12513. ? 218 PHE A CE2   1 
ATOM   1456  C  CZ    . PHE A 1 218 ? 130.786 142.524 168.622 1.00 12490. ? 218 PHE A CZ    1 
ATOM   1457  N  N     . GLY A 1 219 ? 132.396 140.643 161.804 1.00 13121. ? 219 GLY A N     1 
ATOM   1458  C  CA    . GLY A 1 219 ? 132.933 140.336 160.499 1.00 13131. ? 219 GLY A CA    1 
ATOM   1459  C  C     . GLY A 1 219 ? 134.205 141.099 160.189 1.00 13069. ? 219 GLY A C     1 
ATOM   1460  O  O     . GLY A 1 219 ? 134.866 141.670 161.059 1.00 12895. ? 219 GLY A O     1 
ATOM   1461  N  N     . LEU A 1 220 ? 134.548 141.098 158.906 1.00 12727. ? 220 LEU A N     1 
ATOM   1462  C  CA    . LEU A 1 220 ? 135.715 141.799 158.392 1.00 12700. ? 220 LEU A CA    1 
ATOM   1463  C  C     . LEU A 1 220 ? 135.239 143.017 157.614 1.00 12704. ? 220 LEU A C     1 
ATOM   1464  O  O     . LEU A 1 220 ? 134.478 142.882 156.651 1.00 12750. ? 220 LEU A O     1 
ATOM   1465  C  CB    . LEU A 1 220 ? 136.555 140.880 157.506 1.00 12744. ? 220 LEU A CB    1 
ATOM   1466  C  CG    . LEU A 1 220 ? 138.029 141.233 157.317 1.00 12724. ? 220 LEU A CG    1 
ATOM   1467  C  CD1   . LEU A 1 220 ? 138.716 141.386 158.658 1.00 12631. ? 220 LEU A CD1   1 
ATOM   1468  C  CD2   . LEU A 1 220 ? 138.717 140.170 156.485 1.00 12742. ? 220 LEU A CD2   1 
ATOM   1469  N  N     . LYS A 1 221 ? 135.681 144.201 158.033 1.00 12634. ? 221 LYS A N     1 
ATOM   1470  C  CA    . LYS A 1 221 ? 135.254 145.440 157.404 1.00 12681. ? 221 LYS A CA    1 
ATOM   1471  C  C     . LYS A 1 221 ? 136.404 146.356 157.016 1.00 12743. ? 221 LYS A C     1 
ATOM   1472  O  O     . LYS A 1 221 ? 136.157 147.409 156.420 1.00 12762. ? 221 LYS A O     1 
ATOM   1473  C  CB    . LYS A 1 221 ? 134.292 146.202 158.326 1.00 12674. ? 221 LYS A CB    1 
ATOM   1474  C  CG    . LYS A 1 221 ? 132.915 145.577 158.424 1.00 12709. ? 221 LYS A CG    1 
ATOM   1475  C  CD    . LYS A 1 221 ? 132.262 145.884 159.757 1.00 12660. ? 221 LYS A CD    1 
ATOM   1476  C  CE    . LYS A 1 221 ? 131.492 147.191 159.708 1.00 12669. ? 221 LYS A CE    1 
ATOM   1477  N  NZ    . LYS A 1 221 ? 132.375 148.368 159.933 1.00 12593. ? 221 LYS A NZ    1 
ATOM   1478  N  N     . ASP A 1 222 ? 137.644 145.995 157.332 1.00 13444. ? 222 ASP A N     1 
ATOM   1479  C  CA    . ASP A 1 222 ? 138.793 146.803 156.950 1.00 13481. ? 222 ASP A CA    1 
ATOM   1480  C  C     . ASP A 1 222 ? 139.162 146.487 155.507 1.00 13497. ? 222 ASP A C     1 
ATOM   1481  O  O     . ASP A 1 222 ? 139.421 145.327 155.170 1.00 13502. ? 222 ASP A O     1 
ATOM   1482  C  CB    . ASP A 1 222 ? 139.969 146.531 157.884 1.00 13452. ? 222 ASP A CB    1 
ATOM   1483  C  CG    . ASP A 1 222 ? 141.007 147.631 157.848 1.00 13508. ? 222 ASP A CG    1 
ATOM   1484  O  OD1   . ASP A 1 222 ? 140.776 148.689 158.469 1.00 13532. ? 222 ASP A OD1   1 
ATOM   1485  O  OD2   . ASP A 1 222 ? 142.057 147.439 157.200 1.00 13541. ? 222 ASP A OD2   1 
ATOM   1486  N  N     . LYS A 1 223 ? 139.183 147.515 154.656 1.00 12928. ? 223 LYS A N     1 
ATOM   1487  C  CA    . LYS A 1 223 ? 139.435 147.292 153.235 1.00 12913. ? 223 LYS A CA    1 
ATOM   1488  C  C     . LYS A 1 223 ? 140.822 146.710 153.000 1.00 12916. ? 223 LYS A C     1 
ATOM   1489  O  O     . LYS A 1 223 ? 140.986 145.789 152.190 1.00 12927. ? 223 LYS A O     1 
ATOM   1490  C  CB    . LYS A 1 223 ? 139.264 148.597 152.460 1.00 12893. ? 223 LYS A CB    1 
ATOM   1491  C  CG    . LYS A 1 223 ? 137.838 149.107 152.420 1.00 12900. ? 223 LYS A CG    1 
ATOM   1492  C  CD    . LYS A 1 223 ? 137.245 148.971 151.030 1.00 12906. ? 223 LYS A CD    1 
ATOM   1493  C  CE    . LYS A 1 223 ? 137.111 150.324 150.353 1.00 12801. ? 223 LYS A CE    1 
ATOM   1494  N  NZ    . LYS A 1 223 ? 136.515 150.203 148.995 1.00 12838. ? 223 LYS A NZ    1 
ATOM   1495  N  N     . GLU A 1 224 ? 141.834 147.235 153.693 1.00 13048. ? 224 GLU A N     1 
ATOM   1496  C  CA    . GLU A 1 224 ? 143.187 146.718 153.521 1.00 13053. ? 224 GLU A CA    1 
ATOM   1497  C  C     . GLU A 1 224 ? 143.284 145.266 153.965 1.00 13056. ? 224 GLU A C     1 
ATOM   1498  O  O     . GLU A 1 224 ? 143.901 144.440 153.283 1.00 13058. ? 224 GLU A O     1 
ATOM   1499  C  CB    . GLU A 1 224 ? 144.182 147.584 154.292 1.00 13029. ? 224 GLU A CB    1 
ATOM   1500  C  CG    . GLU A 1 224 ? 145.593 147.537 153.738 1.00 12947. ? 224 GLU A CG    1 
ATOM   1501  C  CD    . GLU A 1 224 ? 146.644 147.761 154.804 1.00 12971. ? 224 GLU A CD    1 
ATOM   1502  O  OE1   . GLU A 1 224 ? 146.272 148.126 155.938 1.00 13032. ? 224 GLU A OE1   1 
ATOM   1503  O  OE2   . GLU A 1 224 ? 147.842 147.573 154.508 1.00 12916. ? 224 GLU A OE2   1 
ATOM   1504  N  N     . THR A 1 225 ? 142.676 144.933 155.105 1.00 12755. ? 225 THR A N     1 
ATOM   1505  C  CA    . THR A 1 225 ? 142.689 143.552 155.574 1.00 12735. ? 225 THR A CA    1 
ATOM   1506  C  C     . THR A 1 225 ? 141.925 142.641 154.623 1.00 12743. ? 225 THR A C     1 
ATOM   1507  O  O     . THR A 1 225 ? 142.343 141.507 154.367 1.00 12761. ? 225 THR A O     1 
ATOM   1508  C  CB    . THR A 1 225 ? 142.099 143.468 156.980 1.00 12741. ? 225 THR A CB    1 
ATOM   1509  O  OG1   . THR A 1 225 ? 142.723 144.447 157.819 1.00 12721. ? 225 THR A OG1   1 
ATOM   1510  C  CG2   . THR A 1 225 ? 142.324 142.088 157.571 1.00 12725. ? 225 THR A CG2   1 
ATOM   1511  N  N     . ARG A 1 226 ? 140.798 143.120 154.095 1.00 12744. ? 226 ARG A N     1 
ATOM   1512  C  CA    . ARG A 1 226 ? 140.012 142.310 153.172 1.00 12739. ? 226 ARG A CA    1 
ATOM   1513  C  C     . ARG A 1 226 ? 140.771 142.045 151.879 1.00 12748. ? 226 ARG A C     1 
ATOM   1514  O  O     . ARG A 1 226 ? 140.699 140.941 151.327 1.00 12759. ? 226 ARG A O     1 
ATOM   1515  C  CB    . ARG A 1 226 ? 138.679 142.996 152.883 1.00 12740. ? 226 ARG A CB    1 
ATOM   1516  C  CG    . ARG A 1 226 ? 137.702 142.953 154.040 1.00 12757. ? 226 ARG A CG    1 
ATOM   1517  C  CD    . ARG A 1 226 ? 136.384 143.588 153.658 1.00 12766. ? 226 ARG A CD    1 
ATOM   1518  N  NE    . ARG A 1 226 ? 135.945 143.159 152.337 1.00 12764. ? 226 ARG A NE    1 
ATOM   1519  C  CZ    . ARG A 1 226 ? 135.225 143.904 151.511 1.00 12755. ? 226 ARG A CZ    1 
ATOM   1520  N  NH1   . ARG A 1 226 ? 134.841 145.125 151.840 1.00 12740. ? 226 ARG A NH1   1 
ATOM   1521  N  NH2   . ARG A 1 226 ? 134.882 143.410 150.325 1.00 12756. ? 226 ARG A NH2   1 
ATOM   1522  N  N     . TYR A 1 227 ? 141.497 143.043 151.375 1.00 12756. ? 227 TYR A N     1 
ATOM   1523  C  CA    . TYR A 1 227 ? 142.238 142.868 150.132 1.00 12746. ? 227 TYR A CA    1 
ATOM   1524  C  C     . TYR A 1 227 ? 143.514 142.061 150.327 1.00 12739. ? 227 TYR A C     1 
ATOM   1525  O  O     . TYR A 1 227 ? 143.918 141.324 149.422 1.00 12738. ? 227 TYR A O     1 
ATOM   1526  C  CB    . TYR A 1 227 ? 142.564 144.230 149.521 1.00 12747. ? 227 TYR A CB    1 
ATOM   1527  C  CG    . TYR A 1 227 ? 141.344 144.998 149.071 1.00 12750. ? 227 TYR A CG    1 
ATOM   1528  C  CD1   . TYR A 1 227 ? 140.173 144.338 148.730 1.00 12753. ? 227 TYR A CD1   1 
ATOM   1529  C  CD2   . TYR A 1 227 ? 141.361 146.382 148.991 1.00 12730. ? 227 TYR A CD2   1 
ATOM   1530  C  CE1   . TYR A 1 227 ? 139.057 145.033 148.321 1.00 12739. ? 227 TYR A CE1   1 
ATOM   1531  C  CE2   . TYR A 1 227 ? 140.248 147.086 148.584 1.00 12715. ? 227 TYR A CE2   1 
ATOM   1532  C  CZ    . TYR A 1 227 ? 139.099 146.406 148.250 1.00 12735. ? 227 TYR A CZ    1 
ATOM   1533  O  OH    . TYR A 1 227 ? 137.986 147.101 147.842 1.00 12746. ? 227 TYR A OH    1 
ATOM   1534  N  N     . ARG A 1 228 ? 144.163 142.184 151.488 1.00 12734. ? 228 ARG A N     1 
ATOM   1535  C  CA    . ARG A 1 228 ? 145.402 141.449 151.719 1.00 12736. ? 228 ARG A CA    1 
ATOM   1536  C  C     . ARG A 1 228 ? 145.135 139.970 151.963 1.00 12738. ? 228 ARG A C     1 
ATOM   1537  O  O     . ARG A 1 228 ? 145.895 139.113 151.500 1.00 12741. ? 228 ARG A O     1 
ATOM   1538  C  CB    . ARG A 1 228 ? 146.161 142.059 152.895 1.00 12738. ? 228 ARG A CB    1 
ATOM   1539  C  CG    . ARG A 1 228 ? 146.877 143.350 152.555 1.00 12755. ? 228 ARG A CG    1 
ATOM   1540  C  CD    . ARG A 1 228 ? 147.870 143.734 153.633 1.00 12771. ? 228 ARG A CD    1 
ATOM   1541  N  NE    . ARG A 1 228 ? 148.408 145.072 153.425 1.00 12756. ? 228 ARG A NE    1 
ATOM   1542  C  CZ    . ARG A 1 228 ? 149.383 145.363 152.576 1.00 12713. ? 228 ARG A CZ    1 
ATOM   1543  N  NH1   . ARG A 1 228 ? 149.952 144.430 151.833 1.00 12782. ? 228 ARG A NH1   1 
ATOM   1544  N  NH2   . ARG A 1 228 ? 149.799 146.621 152.473 1.00 12608. ? 228 ARG A NH2   1 
ATOM   1545  N  N     . GLN A 1 229 ? 144.067 139.650 152.687 1.00 12736. ? 229 GLN A N     1 
ATOM   1546  C  CA    . GLN A 1 229 ? 143.687 138.271 152.985 1.00 12741. ? 229 GLN A CA    1 
ATOM   1547  C  C     . GLN A 1 229 ? 142.310 138.030 152.378 1.00 12738. ? 229 GLN A C     1 
ATOM   1548  O  O     . GLN A 1 229 ? 141.288 138.195 153.047 1.00 12745. ? 229 GLN A O     1 
ATOM   1549  C  CB    . GLN A 1 229 ? 143.688 138.016 154.482 1.00 12738. ? 229 GLN A CB    1 
ATOM   1550  C  CG    . GLN A 1 229 ? 144.726 138.811 155.243 1.00 12734. ? 229 GLN A CG    1 
ATOM   1551  C  CD    . GLN A 1 229 ? 144.975 138.259 156.627 1.00 12721. ? 229 GLN A CD    1 
ATOM   1552  O  OE1   . GLN A 1 229 ? 144.904 137.051 156.848 1.00 12701. ? 229 GLN A OE1   1 
ATOM   1553  N  NE2   . GLN A 1 229 ? 145.267 139.143 157.572 1.00 12725. ? 229 GLN A NE2   1 
ATOM   1554  N  N     . ARG A 1 230 ? 142.287 137.633 151.105 1.00 12745. ? 230 ARG A N     1 
ATOM   1555  C  CA    . ARG A 1 230 ? 141.013 137.409 150.432 1.00 12741. ? 230 ARG A CA    1 
ATOM   1556  C  C     . ARG A 1 230 ? 140.324 136.146 150.931 1.00 12745. ? 230 ARG A C     1 
ATOM   1557  O  O     . ARG A 1 230 ? 139.091 136.064 150.905 1.00 12750. ? 230 ARG A O     1 
ATOM   1558  C  CB    . ARG A 1 230 ? 141.223 137.339 148.921 1.00 12749. ? 230 ARG A CB    1 
ATOM   1559  C  CG    . ARG A 1 230 ? 139.934 137.309 148.121 1.00 12739. ? 230 ARG A CG    1 
ATOM   1560  C  CD    . ARG A 1 230 ? 139.070 138.517 148.429 1.00 12742. ? 230 ARG A CD    1 
ATOM   1561  N  NE    . ARG A 1 230 ? 139.112 139.503 147.357 1.00 12738. ? 230 ARG A NE    1 
ATOM   1562  C  CZ    . ARG A 1 230 ? 138.520 140.687 147.405 1.00 12738. ? 230 ARG A CZ    1 
ATOM   1563  N  NH1   . ARG A 1 230 ? 137.835 141.075 148.468 1.00 12747. ? 230 ARG A NH1   1 
ATOM   1564  N  NH2   . ARG A 1 230 ? 138.617 141.503 146.361 1.00 12745. ? 230 ARG A NH2   1 
ATOM   1565  N  N     . TYR A 1 231 ? 141.095 135.154 151.378 1.00 12745. ? 231 TYR A N     1 
ATOM   1566  C  CA    . TYR A 1 231 ? 140.491 133.939 151.915 1.00 12738. ? 231 TYR A CA    1 
ATOM   1567  C  C     . TYR A 1 231 ? 139.673 134.241 153.163 1.00 12746. ? 231 TYR A C     1 
ATOM   1568  O  O     . TYR A 1 231 ? 138.565 133.718 153.331 1.00 12763. ? 231 TYR A O     1 
ATOM   1569  C  CB    . TYR A 1 231 ? 141.573 132.899 152.209 1.00 12748. ? 231 TYR A CB    1 
ATOM   1570  C  CG    . TYR A 1 231 ? 142.781 133.440 152.942 1.00 12743. ? 231 TYR A CG    1 
ATOM   1571  C  CD1   . TYR A 1 231 ? 143.856 133.973 152.248 1.00 12738. ? 231 TYR A CD1   1 
ATOM   1572  C  CD2   . TYR A 1 231 ? 142.848 133.408 154.327 1.00 12749. ? 231 TYR A CD2   1 
ATOM   1573  C  CE1   . TYR A 1 231 ? 144.957 134.467 152.913 1.00 12748. ? 231 TYR A CE1   1 
ATOM   1574  C  CE2   . TYR A 1 231 ? 143.944 133.898 154.998 1.00 12729. ? 231 TYR A CE2   1 
ATOM   1575  C  CZ    . TYR A 1 231 ? 144.996 134.426 154.288 1.00 12747. ? 231 TYR A CZ    1 
ATOM   1576  O  OH    . TYR A 1 231 ? 146.093 134.916 154.955 1.00 12756. ? 231 TYR A OH    1 
ATOM   1577  N  N     . LEU A 1 232 ? 140.196 135.092 154.046 1.00 12740. ? 232 LEU A N     1 
ATOM   1578  C  CA    . LEU A 1 232 ? 139.436 135.502 155.221 1.00 12741. ? 232 LEU A CA    1 
ATOM   1579  C  C     . LEU A 1 232 ? 138.198 136.294 154.823 1.00 12747. ? 232 LEU A C     1 
ATOM   1580  O  O     . LEU A 1 232 ? 137.143 136.170 155.455 1.00 12753. ? 232 LEU A O     1 
ATOM   1581  C  CB    . LEU A 1 232 ? 140.326 136.319 156.154 1.00 12741. ? 232 LEU A CB    1 
ATOM   1582  C  CG    . LEU A 1 232 ? 139.963 136.302 157.636 1.00 12719. ? 232 LEU A CG    1 
ATOM   1583  C  CD1   . LEU A 1 232 ? 140.065 134.894 158.186 1.00 12714. ? 232 LEU A CD1   1 
ATOM   1584  C  CD2   . LEU A 1 232 ? 140.866 137.243 158.408 1.00 12716. ? 232 LEU A CD2   1 
ATOM   1585  N  N     . ASP A 1 233 ? 138.313 137.116 153.778 1.00 12752. ? 233 ASP A N     1 
ATOM   1586  C  CA    . ASP A 1 233 ? 137.160 137.854 153.277 1.00 12745. ? 233 ASP A CA    1 
ATOM   1587  C  C     . ASP A 1 233 ? 136.065 136.908 152.801 1.00 12749. ? 233 ASP A C     1 
ATOM   1588  O  O     . ASP A 1 233 ? 134.882 137.123 153.084 1.00 12771. ? 233 ASP A O     1 
ATOM   1589  C  CB    . ASP A 1 233 ? 137.595 138.783 152.145 1.00 12750. ? 233 ASP A CB    1 
ATOM   1590  C  CG    . ASP A 1 233 ? 136.639 139.934 151.936 1.00 12739. ? 233 ASP A CG    1 
ATOM   1591  O  OD1   . ASP A 1 233 ? 135.813 140.192 152.834 1.00 12740. ? 233 ASP A OD1   1 
ATOM   1592  O  OD2   . ASP A 1 233 ? 136.714 140.583 150.872 1.00 12751. ? 233 ASP A OD2   1 
ATOM   1593  N  N     . LEU A 1 234 ? 136.442 135.854 152.075 1.00 12752. ? 234 LEU A N     1 
ATOM   1594  C  CA    . LEU A 1 234 ? 135.458 134.876 151.626 1.00 12742. ? 234 LEU A CA    1 
ATOM   1595  C  C     . LEU A 1 234 ? 134.869 134.105 152.799 1.00 12741. ? 234 LEU A C     1 
ATOM   1596  O  O     . LEU A 1 234 ? 133.678 133.775 152.797 1.00 12751. ? 234 LEU A O     1 
ATOM   1597  C  CB    . LEU A 1 234 ? 136.092 133.915 150.623 1.00 12751. ? 234 LEU A CB    1 
ATOM   1598  C  CG    . LEU A 1 234 ? 136.573 134.516 149.304 1.00 12740. ? 234 LEU A CG    1 
ATOM   1599  C  CD1   . LEU A 1 234 ? 137.597 133.605 148.657 1.00 12748. ? 234 LEU A CD1   1 
ATOM   1600  C  CD2   . LEU A 1 234 ? 135.403 134.753 148.372 1.00 12741. ? 234 LEU A CD2   1 
ATOM   1601  N  N     . ILE A 1 235 ? 135.692 133.795 153.801 1.00 12737. ? 235 ILE A N     1 
ATOM   1602  C  CA    . ILE A 1 235 ? 135.212 133.039 154.954 1.00 12724. ? 235 ILE A CA    1 
ATOM   1603  C  C     . ILE A 1 235 ? 134.178 133.844 155.731 1.00 12723. ? 235 ILE A C     1 
ATOM   1604  O  O     . ILE A 1 235 ? 133.118 133.331 156.107 1.00 12728. ? 235 ILE A O     1 
ATOM   1605  C  CB    . ILE A 1 235 ? 136.394 132.627 155.850 1.00 12737. ? 235 ILE A CB    1 
ATOM   1606  C  CG1   . ILE A 1 235 ? 137.154 131.460 155.225 1.00 12734. ? 235 ILE A CG1   1 
ATOM   1607  C  CG2   . ILE A 1 235 ? 135.909 132.263 157.239 1.00 12746. ? 235 ILE A CG2   1 
ATOM   1608  C  CD1   . ILE A 1 235 ? 138.364 131.037 156.016 1.00 12742. ? 235 ILE A CD1   1 
ATOM   1609  N  N     . LEU A 1 236 ? 134.464 135.122 155.974 1.00 12729. ? 236 LEU A N     1 
ATOM   1610  C  CA    . LEU A 1 236 ? 133.631 135.922 156.861 1.00 12737. ? 236 LEU A CA    1 
ATOM   1611  C  C     . LEU A 1 236 ? 132.507 136.661 156.150 1.00 12749. ? 236 LEU A C     1 
ATOM   1612  O  O     . LEU A 1 236 ? 131.489 136.960 156.782 1.00 12759. ? 236 LEU A O     1 
ATOM   1613  C  CB    . LEU A 1 236 ? 134.494 136.933 157.619 1.00 12747. ? 236 LEU A CB    1 
ATOM   1614  C  CG    . LEU A 1 236 ? 135.562 136.320 158.523 1.00 12743. ? 236 LEU A CG    1 
ATOM   1615  C  CD1   . LEU A 1 236 ? 136.369 137.405 159.209 1.00 12748. ? 236 LEU A CD1   1 
ATOM   1616  C  CD2   . LEU A 1 236 ? 134.921 135.396 159.542 1.00 12750. ? 236 LEU A CD2   1 
ATOM   1617  N  N     . ASN A 1 237 ? 132.658 136.966 154.865 1.00 12762. ? 237 ASN A N     1 
ATOM   1618  C  CA    . ASN A 1 237 ? 131.665 137.723 154.117 1.00 12760. ? 237 ASN A CA    1 
ATOM   1619  C  C     . ASN A 1 237 ? 131.074 136.853 153.018 1.00 12802. ? 237 ASN A C     1 
ATOM   1620  O  O     . ASN A 1 237 ? 131.801 136.157 152.304 1.00 12796. ? 237 ASN A O     1 
ATOM   1621  C  CB    . ASN A 1 237 ? 132.277 138.988 153.516 1.00 12759. ? 237 ASN A CB    1 
ATOM   1622  C  CG    . ASN A 1 237 ? 132.893 139.888 154.565 1.00 12746. ? 237 ASN A CG    1 
ATOM   1623  O  OD1   . ASN A 1 237 ? 132.232 140.290 155.520 1.00 12741. ? 237 ASN A OD1   1 
ATOM   1624  N  ND2   . ASN A 1 237 ? 134.169 140.205 154.396 1.00 12756. ? 237 ASN A ND2   1 
ATOM   1625  N  N     . ASP A 1 238 ? 129.749 136.897 152.887 1.00 14416. ? 238 ASP A N     1 
ATOM   1626  C  CA    . ASP A 1 238 ? 129.054 136.054 151.923 1.00 14463. ? 238 ASP A CA    1 
ATOM   1627  C  C     . ASP A 1 238 ? 128.844 136.735 150.578 1.00 14425. ? 238 ASP A C     1 
ATOM   1628  O  O     . ASP A 1 238 ? 128.733 136.047 149.557 1.00 14425. ? 238 ASP A O     1 
ATOM   1629  C  CB    . ASP A 1 238 ? 127.701 135.617 152.488 1.00 14494. ? 238 ASP A CB    1 
ATOM   1630  C  CG    . ASP A 1 238 ? 127.009 134.591 151.614 1.00 14503. ? 238 ASP A CG    1 
ATOM   1631  O  OD1   . ASP A 1 238 ? 127.713 133.804 150.949 1.00 14489. ? 238 ASP A OD1   1 
ATOM   1632  O  OD2   . ASP A 1 238 ? 125.761 134.573 151.591 1.00 14514. ? 238 ASP A OD2   1 
ATOM   1633  N  N     . PHE A 1 239 ? 128.787 138.067 150.547 1.00 12975. ? 239 PHE A N     1 
ATOM   1634  C  CA    . PHE A 1 239 ? 128.539 138.765 149.291 1.00 12932. ? 239 PHE A CA    1 
ATOM   1635  C  C     . PHE A 1 239 ? 129.729 138.705 148.342 1.00 12915. ? 239 PHE A C     1 
ATOM   1636  O  O     . PHE A 1 239 ? 129.544 138.860 147.132 1.00 12916. ? 239 PHE A O     1 
ATOM   1637  C  CB    . PHE A 1 239 ? 128.157 140.220 149.562 1.00 12923. ? 239 PHE A CB    1 
ATOM   1638  C  CG    . PHE A 1 239 ? 129.120 140.949 150.450 1.00 12912. ? 239 PHE A CG    1 
ATOM   1639  C  CD1   . PHE A 1 239 ? 130.204 141.622 149.914 1.00 12909. ? 239 PHE A CD1   1 
ATOM   1640  C  CD2   . PHE A 1 239 ? 128.934 140.975 151.820 1.00 12920. ? 239 PHE A CD2   1 
ATOM   1641  C  CE1   . PHE A 1 239 ? 131.088 142.299 150.728 1.00 12908. ? 239 PHE A CE1   1 
ATOM   1642  C  CE2   . PHE A 1 239 ? 129.817 141.649 152.639 1.00 12926. ? 239 PHE A CE2   1 
ATOM   1643  C  CZ    . PHE A 1 239 ? 130.894 142.312 152.092 1.00 12917. ? 239 PHE A CZ    1 
ATOM   1644  N  N     . VAL A 1 240 ? 130.940 138.488 148.859 1.00 12750. ? 240 VAL A N     1 
ATOM   1645  C  CA    . VAL A 1 240 ? 132.118 138.399 148.001 1.00 12739. ? 240 VAL A CA    1 
ATOM   1646  C  C     . VAL A 1 240 ? 132.034 137.184 147.083 1.00 12754. ? 240 VAL A C     1 
ATOM   1647  O  O     . VAL A 1 240 ? 132.328 137.272 145.877 1.00 12776. ? 240 VAL A O     1 
ATOM   1648  C  CB    . VAL A 1 240 ? 133.384 138.366 148.875 1.00 12735. ? 240 VAL A CB    1 
ATOM   1649  C  CG1   . VAL A 1 240 ? 134.623 138.518 148.028 1.00 12756. ? 240 VAL A CG1   1 
ATOM   1650  C  CG2   . VAL A 1 240 ? 133.321 139.452 149.932 1.00 12751. ? 240 VAL A CG2   1 
ATOM   1651  N  N     . ARG A 1 241 ? 131.634 136.037 147.633 1.00 12747. ? 241 ARG A N     1 
ATOM   1652  C  CA    . ARG A 1 241 ? 131.450 134.836 146.833 1.00 12749. ? 241 ARG A CA    1 
ATOM   1653  C  C     . ARG A 1 241 ? 130.405 135.036 145.748 1.00 12754. ? 241 ARG A C     1 
ATOM   1654  O  O     . ARG A 1 241 ? 130.616 134.600 144.611 1.00 12761. ? 241 ARG A O     1 
ATOM   1655  C  CB    . ARG A 1 241 ? 131.055 133.674 147.744 1.00 12750. ? 241 ARG A CB    1 
ATOM   1656  C  CG    . ARG A 1 241 ? 130.789 132.368 147.032 1.00 12747. ? 241 ARG A CG    1 
ATOM   1657  C  CD    . ARG A 1 241 ? 129.704 131.578 147.743 1.00 12753. ? 241 ARG A CD    1 
ATOM   1658  N  NE    . ARG A 1 241 ? 129.751 130.162 147.404 1.00 12709. ? 241 ARG A NE    1 
ATOM   1659  C  CZ    . ARG A 1 241 ? 130.665 129.313 147.855 1.00 12724. ? 241 ARG A CZ    1 
ATOM   1660  N  NH1   . ARG A 1 241 ? 131.608 129.697 148.699 1.00 12745. ? 241 ARG A NH1   1 
ATOM   1661  N  NH2   . ARG A 1 241 ? 130.627 128.047 147.453 1.00 12688. ? 241 ARG A NH2   1 
ATOM   1662  N  N     . GLN A 1 242 ? 129.297 135.700 146.068 1.00 12755. ? 242 GLN A N     1 
ATOM   1663  C  CA    . GLN A 1 242 ? 128.282 136.031 145.079 1.00 12747. ? 242 GLN A CA    1 
ATOM   1664  C  C     . GLN A 1 242 ? 128.813 136.971 144.006 1.00 12741. ? 242 GLN A C     1 
ATOM   1665  O  O     . GLN A 1 242 ? 128.473 136.816 142.831 1.00 12759. ? 242 GLN A O     1 
ATOM   1666  C  CB    . GLN A 1 242 ? 127.063 136.650 145.762 1.00 12746. ? 242 GLN A CB    1 
ATOM   1667  C  CG    . GLN A 1 242 ? 126.333 135.694 146.684 1.00 12760. ? 242 GLN A CG    1 
ATOM   1668  C  CD    . GLN A 1 242 ? 126.113 134.335 146.053 1.00 12752. ? 242 GLN A CD    1 
ATOM   1669  O  OE1   . GLN A 1 242 ? 125.614 134.230 144.933 1.00 12753. ? 242 GLN A OE1   1 
ATOM   1670  N  NE2   . GLN A 1 242 ? 126.485 133.283 146.771 1.00 12759. ? 242 GLN A NE2   1 
ATOM   1671  N  N     . LYS A 1 243 ? 129.644 137.943 144.386 1.00 12724. ? 243 LYS A N     1 
ATOM   1672  C  CA    . LYS A 1 243 ? 130.237 138.839 143.400 1.00 12730. ? 243 LYS A CA    1 
ATOM   1673  C  C     . LYS A 1 243 ? 131.080 138.064 142.397 1.00 12737. ? 243 LYS A C     1 
ATOM   1674  O  O     . LYS A 1 243 ? 130.992 138.284 141.181 1.00 12763. ? 243 LYS A O     1 
ATOM   1675  C  CB    . LYS A 1 243 ? 131.086 139.897 144.101 1.00 12737. ? 243 LYS A CB    1 
ATOM   1676  C  CG    . LYS A 1 243 ? 130.288 140.972 144.806 1.00 12745. ? 243 LYS A CG    1 
ATOM   1677  C  CD    . LYS A 1 243 ? 131.202 141.976 145.483 1.00 12747. ? 243 LYS A CD    1 
ATOM   1678  C  CE    . LYS A 1 243 ? 130.416 143.168 145.992 1.00 12750. ? 243 LYS A CE    1 
ATOM   1679  N  NZ    . LYS A 1 243 ? 131.282 144.361 146.179 1.00 12757. ? 243 LYS A NZ    1 
ATOM   1680  N  N     . PHE A 1 244 ? 131.902 137.140 142.890 1.00 12729. ? 244 PHE A N     1 
ATOM   1681  C  CA    . PHE A 1 244 ? 132.764 136.404 141.971 1.00 12729. ? 244 PHE A CA    1 
ATOM   1682  C  C     . PHE A 1 244 ? 131.978 135.394 141.142 1.00 12735. ? 244 PHE A C     1 
ATOM   1683  O  O     . PHE A 1 244 ? 132.306 135.165 139.968 1.00 12765. ? 244 PHE A O     1 
ATOM   1684  C  CB    . PHE A 1 244 ? 133.899 135.745 142.743 1.00 12741. ? 244 PHE A CB    1 
ATOM   1685  C  CG    . PHE A 1 244 ? 134.901 136.730 143.260 1.00 12739. ? 244 PHE A CG    1 
ATOM   1686  C  CD1   . PHE A 1 244 ? 135.526 137.608 142.393 1.00 12740. ? 244 PHE A CD1   1 
ATOM   1687  C  CD2   . PHE A 1 244 ? 135.197 136.803 144.605 1.00 12748. ? 244 PHE A CD2   1 
ATOM   1688  C  CE1   . PHE A 1 244 ? 136.437 138.527 142.856 1.00 12747. ? 244 PHE A CE1   1 
ATOM   1689  C  CE2   . PHE A 1 244 ? 136.112 137.722 145.072 1.00 12754. ? 244 PHE A CE2   1 
ATOM   1690  C  CZ    . PHE A 1 244 ? 136.730 138.585 144.197 1.00 12754. ? 244 PHE A CZ    1 
ATOM   1691  N  N     . ILE A 1 245 ? 130.922 134.809 141.711 1.00 12724. ? 245 ILE A N     1 
ATOM   1692  C  CA    . ILE A 1 245 ? 130.030 133.969 140.918 1.00 12736. ? 245 ILE A CA    1 
ATOM   1693  C  C     . ILE A 1 245 ? 129.388 134.785 139.803 1.00 12750. ? 245 ILE A C     1 
ATOM   1694  O  O     . ILE A 1 245 ? 129.258 134.317 138.666 1.00 12756. ? 245 ILE A O     1 
ATOM   1695  C  CB    . ILE A 1 245 ? 128.973 133.310 141.822 1.00 12735. ? 245 ILE A CB    1 
ATOM   1696  C  CG1   . ILE A 1 245 ? 129.616 132.237 142.698 1.00 12690. ? 245 ILE A CG1   1 
ATOM   1697  C  CG2   . ILE A 1 245 ? 127.860 132.701 140.992 1.00 12694. ? 245 ILE A CG2   1 
ATOM   1698  C  CD1   . ILE A 1 245 ? 128.749 131.803 143.852 1.00 12667. ? 245 ILE A CD1   1 
ATOM   1699  N  N     . ILE A 1 246 ? 128.982 136.019 140.109 1.00 12755. ? 246 ILE A N     1 
ATOM   1700  C  CA    . ILE A 1 246 ? 128.375 136.885 139.103 1.00 12738. ? 246 ILE A CA    1 
ATOM   1701  C  C     . ILE A 1 246 ? 129.369 137.194 137.992 1.00 12741. ? 246 ILE A C     1 
ATOM   1702  O  O     . ILE A 1 246 ? 129.016 137.199 136.808 1.00 12762. ? 246 ILE A O     1 
ATOM   1703  C  CB    . ILE A 1 246 ? 127.844 138.172 139.761 1.00 12732. ? 246 ILE A CB    1 
ATOM   1704  C  CG1   . ILE A 1 246 ? 126.523 137.900 140.477 1.00 12735. ? 246 ILE A CG1   1 
ATOM   1705  C  CG2   . ILE A 1 246 ? 127.663 139.270 138.731 1.00 12742. ? 246 ILE A CG2   1 
ATOM   1706  C  CD1   . ILE A 1 246 ? 126.106 139.009 141.409 1.00 12746. ? 246 ILE A CD1   1 
ATOM   1707  N  N     . ARG A 1 247 ? 130.621 137.476 138.354 1.00 12740. ? 247 ARG A N     1 
ATOM   1708  C  CA    . ARG A 1 247 ? 131.635 137.746 137.336 1.00 12733. ? 247 ARG A CA    1 
ATOM   1709  C  C     . ARG A 1 247 ? 131.846 136.538 136.428 1.00 12730. ? 247 ARG A C     1 
ATOM   1710  O  O     . ARG A 1 247 ? 131.928 136.672 135.194 1.00 12761. ? 247 ARG A O     1 
ATOM   1711  C  CB    . ARG A 1 247 ? 132.945 138.152 138.008 1.00 12743. ? 247 ARG A CB    1 
ATOM   1712  C  CG    . ARG A 1 247 ? 134.156 138.071 137.106 1.00 12745. ? 247 ARG A CG    1 
ATOM   1713  C  CD    . ARG A 1 247 ? 135.255 138.994 137.592 1.00 12739. ? 247 ARG A CD    1 
ATOM   1714  N  NE    . ARG A 1 247 ? 136.390 139.011 136.679 1.00 12732. ? 247 ARG A NE    1 
ATOM   1715  C  CZ    . ARG A 1 247 ? 137.160 140.067 136.464 1.00 12738. ? 247 ARG A CZ    1 
ATOM   1716  N  NH1   . ARG A 1 247 ? 136.950 141.213 137.088 1.00 12743. ? 247 ARG A NH1   1 
ATOM   1717  N  NH2   . ARG A 1 247 ? 138.166 139.971 135.600 1.00 12752. ? 247 ARG A NH2   1 
ATOM   1718  N  N     . SER A 1 248 ? 131.933 135.345 137.021 1.00 12723. ? 248 SER A N     1 
ATOM   1719  C  CA    . SER A 1 248 ? 132.078 134.136 136.218 1.00 12714. ? 248 SER A CA    1 
ATOM   1720  C  C     . SER A 1 248 ? 130.877 133.938 135.302 1.00 12688. ? 248 SER A C     1 
ATOM   1721  O  O     . SER A 1 248 ? 131.028 133.528 134.144 1.00 12702. ? 248 SER A O     1 
ATOM   1722  C  CB    . SER A 1 248 ? 132.267 132.925 137.127 1.00 12693. ? 248 SER A CB    1 
ATOM   1723  O  OG    . SER A 1 248 ? 131.914 131.729 136.459 1.00 12641. ? 248 SER A OG    1 
ATOM   1724  N  N     . LYS A 1 249 ? 129.674 134.223 135.805 1.00 12682. ? 249 LYS A N     1 
ATOM   1725  C  CA    . LYS A 1 249 ? 128.475 134.111 134.983 1.00 12674. ? 249 LYS A CA    1 
ATOM   1726  C  C     . LYS A 1 249 ? 128.510 135.095 133.822 1.00 12714. ? 249 LYS A C     1 
ATOM   1727  O  O     . LYS A 1 249 ? 128.087 134.767 132.710 1.00 12727. ? 249 LYS A O     1 
ATOM   1728  C  CB    . LYS A 1 249 ? 127.230 134.336 135.839 1.00 12710. ? 249 LYS A CB    1 
ATOM   1729  C  CG    . LYS A 1 249 ? 126.836 133.139 136.683 1.00 12658. ? 249 LYS A CG    1 
ATOM   1730  C  CD    . LYS A 1 249 ? 125.376 133.204 137.085 1.00 12675. ? 249 LYS A CD    1 
ATOM   1731  C  CE    . LYS A 1 249 ? 125.221 133.751 138.491 1.00 12729. ? 249 LYS A CE    1 
ATOM   1732  N  NZ    . LYS A 1 249 ? 123.799 133.785 138.925 1.00 12730. ? 249 LYS A NZ    1 
ATOM   1733  N  N     . ILE A 1 250 ? 129.005 136.309 134.068 1.00 12737. ? 250 ILE A N     1 
ATOM   1734  C  CA    . ILE A 1 250 ? 129.139 137.302 133.003 1.00 12731. ? 250 ILE A CA    1 
ATOM   1735  C  C     . ILE A 1 250 ? 130.028 136.763 131.893 1.00 12735. ? 250 ILE A C     1 
ATOM   1736  O  O     . ILE A 1 250 ? 129.672 136.798 130.705 1.00 12753. ? 250 ILE A O     1 
ATOM   1737  C  CB    . ILE A 1 250 ? 129.701 138.619 133.567 1.00 12739. ? 250 ILE A CB    1 
ATOM   1738  C  CG1   . ILE A 1 250 ? 128.641 139.381 134.355 1.00 12745. ? 250 ILE A CG1   1 
ATOM   1739  C  CG2   . ILE A 1 250 ? 130.254 139.487 132.452 1.00 12747. ? 250 ILE A CG2   1 
ATOM   1740  C  CD1   . ILE A 1 250 ? 129.213 140.450 135.246 1.00 12757. ? 250 ILE A CD1   1 
ATOM   1741  N  N     . ILE A 1 251 ? 131.202 136.252 132.268 1.00 12741. ? 251 ILE A N     1 
ATOM   1742  C  CA    . ILE A 1 251 ? 132.149 135.775 131.262 1.00 12734. ? 251 ILE A CA    1 
ATOM   1743  C  C     . ILE A 1 251 ? 131.574 134.583 130.503 1.00 12738. ? 251 ILE A C     1 
ATOM   1744  O  O     . ILE A 1 251 ? 131.691 134.494 129.272 1.00 12760. ? 251 ILE A O     1 
ATOM   1745  C  CB    . ILE A 1 251 ? 133.501 135.441 131.914 1.00 12734. ? 251 ILE A CB    1 
ATOM   1746  C  CG1   . ILE A 1 251 ? 134.173 136.722 132.407 1.00 12748. ? 251 ILE A CG1   1 
ATOM   1747  C  CG2   . ILE A 1 251 ? 134.401 134.724 130.932 1.00 12746. ? 251 ILE A CG2   1 
ATOM   1748  C  CD1   . ILE A 1 251 ? 135.513 136.497 133.055 1.00 12749. ? 251 ILE A CD1   1 
ATOM   1749  N  N     . THR A 1 252 ? 130.896 133.669 131.193 1.00 12731. ? 252 THR A N     1 
ATOM   1750  C  CA    . THR A 1 252 ? 130.290 132.507 130.504 1.00 12720. ? 252 THR A CA    1 
ATOM   1751  C  C     . THR A 1 252 ? 129.271 132.974 129.478 1.00 12719. ? 252 THR A C     1 
ATOM   1752  O  O     . THR A 1 252 ? 129.326 132.488 128.316 1.00 12724. ? 252 THR A O     1 
ATOM   1753  C  CB    . THR A 1 252 ? 129.667 131.570 131.535 1.00 12627. ? 252 THR A CB    1 
ATOM   1754  O  OG1   . THR A 1 252 ? 130.722 131.291 132.450 1.00 12632. ? 252 THR A OG1   1 
ATOM   1755  C  CG2   . THR A 1 252 ? 129.152 130.283 130.918 1.00 12628. ? 252 THR A CG2   1 
ATOM   1756  N  N     . TYR A 1 253 ? 128.382 133.896 129.861 1.00 12731. ? 253 TYR A N     1 
ATOM   1757  C  CA    . TYR A 1 253 ? 127.293 134.347 128.950 1.00 12729. ? 253 TYR A CA    1 
ATOM   1758  C  C     . TYR A 1 253 ? 127.884 134.884 127.656 1.00 12728. ? 253 TYR A C     1 
ATOM   1759  O  O     . TYR A 1 253 ? 127.412 134.494 126.570 1.00 12720. ? 253 TYR A O     1 
ATOM   1760  C  CB    . TYR A 1 253 ? 126.438 135.436 129.605 1.00 12736. ? 253 TYR A CB    1 
ATOM   1761  C  CG    . TYR A 1 253 ? 125.357 136.011 128.700 1.00 12714. ? 253 TYR A CG    1 
ATOM   1762  C  CD1   . TYR A 1 253 ? 125.619 137.087 127.861 1.00 12736. ? 253 TYR A CD1   1 
ATOM   1763  C  CD2   . TYR A 1 253 ? 124.075 135.477 128.686 1.00 12707. ? 253 TYR A CD2   1 
ATOM   1764  C  CE1   . TYR A 1 253 ? 124.643 137.609 127.029 1.00 12728. ? 253 TYR A CE1   1 
ATOM   1765  C  CE2   . TYR A 1 253 ? 123.088 135.994 127.864 1.00 12701. ? 253 TYR A CE2   1 
ATOM   1766  C  CZ    . TYR A 1 253 ? 123.374 137.062 127.032 1.00 12710. ? 253 TYR A CZ    1 
ATOM   1767  O  OH    . TYR A 1 253 ? 122.409 137.576 126.217 1.00 12726. ? 253 TYR A OH    1 
ATOM   1768  N  N     . ILE A 1 254 ? 128.872 135.773 127.761 1.00 12739. ? 254 ILE A N     1 
ATOM   1769  C  CA    . ILE A 1 254 ? 129.453 136.406 126.543 1.00 12727. ? 254 ILE A CA    1 
ATOM   1770  C  C     . ILE A 1 254 ? 129.964 135.288 125.627 1.00 12722. ? 254 ILE A C     1 
ATOM   1771  O  O     . ILE A 1 254 ? 129.584 135.275 124.433 1.00 12746. ? 254 ILE A O     1 
ATOM   1772  C  CB    . ILE A 1 254 ? 130.577 137.382 126.926 1.00 12735. ? 254 ILE A CB    1 
ATOM   1773  C  CG1   . ILE A 1 254 ? 130.090 138.429 127.919 1.00 12748. ? 254 ILE A CG1   1 
ATOM   1774  C  CG2   . ILE A 1 254 ? 131.188 138.025 125.682 1.00 12744. ? 254 ILE A CG2   1 
ATOM   1775  C  CD1   . ILE A 1 254 ? 131.204 139.250 128.538 1.00 12762. ? 254 ILE A CD1   1 
ATOM   1776  N  N     . ARG A 1 255 ? 130.755 134.369 126.184 1.00 12721. ? 255 ARG A N     1 
ATOM   1777  C  CA    . ARG A 1 255 ? 131.323 133.272 125.365 1.00 12726. ? 255 ARG A CA    1 
ATOM   1778  C  C     . ARG A 1 255 ? 130.165 132.564 124.660 1.00 12736. ? 255 ARG A C     1 
ATOM   1779  O  O     . ARG A 1 255 ? 130.188 132.506 123.428 1.00 12766. ? 255 ARG A O     1 
ATOM   1780  C  CB    . ARG A 1 255 ? 132.120 132.279 126.214 1.00 12738. ? 255 ARG A CB    1 
ATOM   1781  C  CG    . ARG A 1 255 ? 133.502 132.765 126.623 1.00 12747. ? 255 ARG A CG    1 
ATOM   1782  C  CD    . ARG A 1 255 ? 134.306 131.646 127.261 1.00 12743. ? 255 ARG A CD    1 
ATOM   1783  N  NE    . ARG A 1 255 ? 135.597 132.120 127.768 1.00 12739. ? 255 ARG A NE    1 
ATOM   1784  C  CZ    . ARG A 1 255 ? 135.962 132.049 129.040 1.00 12743. ? 255 ARG A CZ    1 
ATOM   1785  N  NH1   . ARG A 1 255 ? 135.179 131.447 129.915 1.00 12746. ? 255 ARG A NH1   1 
ATOM   1786  N  NH2   . ARG A 1 255 ? 137.105 132.582 129.431 1.00 12759. ? 255 ARG A NH2   1 
ATOM   1787  N  N     . SER A 1 256 ? 129.164 132.111 125.414 1.00 12729. ? 256 SER A N     1 
ATOM   1788  C  CA    . SER A 1 256 ? 128.040 131.357 124.804 1.00 12728. ? 256 SER A CA    1 
ATOM   1789  C  C     . SER A 1 256 ? 127.429 132.155 123.644 1.00 12725. ? 256 SER A C     1 
ATOM   1790  O  O     . SER A 1 256 ? 127.331 131.594 122.534 1.00 12733. ? 256 SER A O     1 
ATOM   1791  C  CB    . SER A 1 256 ? 126.999 131.029 125.834 1.00 12678. ? 256 SER A CB    1 
ATOM   1792  O  OG    . SER A 1 256 ? 125.882 130.390 125.234 1.00 12658. ? 256 SER A OG    1 
ATOM   1793  N  N     . PHE A 1 257 ? 127.064 133.416 123.881 1.00 12705. ? 257 PHE A N     1 
ATOM   1794  C  CA    . PHE A 1 257 ? 126.408 134.250 122.838 1.00 12687. ? 257 PHE A CA    1 
ATOM   1795  C  C     . PHE A 1 257 ? 127.276 134.297 121.591 1.00 12712. ? 257 PHE A C     1 
ATOM   1796  O  O     . PHE A 1 257 ? 126.800 133.963 120.473 1.00 12723. ? 257 PHE A O     1 
ATOM   1797  C  CB    . PHE A 1 257 ? 126.230 135.645 123.443 1.00 12703. ? 257 PHE A CB    1 
ATOM   1798  C  CG    . PHE A 1 257 ? 125.362 136.622 122.663 1.00 12681. ? 257 PHE A CG    1 
ATOM   1799  C  CD1   . PHE A 1 257 ? 125.907 137.424 121.667 1.00 12720. ? 257 PHE A CD1   1 
ATOM   1800  C  CD2   . PHE A 1 257 ? 124.009 136.758 122.948 1.00 12649. ? 257 PHE A CD2   1 
ATOM   1801  C  CE1   . PHE A 1 257 ? 125.116 138.320 120.967 1.00 12695. ? 257 PHE A CE1   1 
ATOM   1802  C  CE2   . PHE A 1 257 ? 123.223 137.655 122.244 1.00 12598. ? 257 PHE A CE2   1 
ATOM   1803  C  CZ    . PHE A 1 257 ? 123.778 138.434 121.257 1.00 12646. ? 257 PHE A CZ    1 
ATOM   1804  N  N     . LEU A 1 258 ? 128.543 134.671 121.766 1.00 12741. ? 258 LEU A N     1 
ATOM   1805  C  CA    . LEU A 1 258 ? 129.421 134.832 120.580 1.00 12731. ? 258 LEU A CA    1 
ATOM   1806  C  C     . LEU A 1 258 ? 129.535 133.491 119.839 1.00 12732. ? 258 LEU A C     1 
ATOM   1807  O  O     . LEU A 1 258 ? 129.427 133.509 118.606 1.00 12754. ? 258 LEU A O     1 
ATOM   1808  C  CB    . LEU A 1 258 ? 130.778 135.384 121.008 1.00 12745. ? 258 LEU A CB    1 
ATOM   1809  C  CG    . LEU A 1 258 ? 130.784 136.856 121.428 1.00 12728. ? 258 LEU A CG    1 
ATOM   1810  C  CD1   . LEU A 1 258 ? 132.151 137.290 121.916 1.00 12737. ? 258 LEU A CD1   1 
ATOM   1811  C  CD2   . LEU A 1 258 ? 130.324 137.732 120.277 1.00 12746. ? 258 LEU A CD2   1 
ATOM   1812  N  N     . ASP A 1 259 ? 129.701 132.383 120.564 1.00 12745. ? 259 ASP A N     1 
ATOM   1813  C  CA    . ASP A 1 259 ? 129.863 131.040 119.940 1.00 12753. ? 259 ASP A CA    1 
ATOM   1814  C  C     . ASP A 1 259 ? 128.616 130.681 119.131 1.00 12719. ? 259 ASP A C     1 
ATOM   1815  O  O     . ASP A 1 259 ? 128.780 130.137 118.012 1.00 12661. ? 259 ASP A O     1 
ATOM   1816  C  CB    . ASP A 1 259 ? 130.148 129.974 120.983 1.00 12727. ? 259 ASP A CB    1 
ATOM   1817  C  CG    . ASP A 1 259 ? 131.493 130.085 121.685 1.00 12712. ? 259 ASP A CG    1 
ATOM   1818  O  OD1   . ASP A 1 259 ? 132.248 131.019 121.353 1.00 12723. ? 259 ASP A OD1   1 
ATOM   1819  O  OD2   . ASP A 1 259 ? 131.773 129.237 122.557 1.00 12711. ? 259 ASP A OD2   1 
ATOM   1820  N  N     . GLU A 1 260 ? 127.429 130.948 119.684 1.00 12724. ? 260 GLU A N     1 
ATOM   1821  C  CA    . GLU A 1 260 ? 126.162 130.678 118.955 1.00 12679. ? 260 GLU A CA    1 
ATOM   1822  C  C     . GLU A 1 260 ? 126.139 131.530 117.681 1.00 12674. ? 260 GLU A C     1 
ATOM   1823  O  O     . GLU A 1 260 ? 125.804 130.982 116.615 1.00 12637. ? 260 GLU A O     1 
ATOM   1824  C  CB    . GLU A 1 260 ? 124.964 130.974 119.854 1.00 12668. ? 260 GLU A CB    1 
ATOM   1825  C  CG    . GLU A 1 260 ? 124.829 129.985 121.007 1.00 12669. ? 260 GLU A CG    1 
ATOM   1826  C  CD    . GLU A 1 260 ? 124.767 128.541 120.544 1.00 12684. ? 260 GLU A CD    1 
ATOM   1827  O  OE1   . GLU A 1 260 ? 123.838 128.205 119.780 1.00 12660. ? 260 GLU A OE1   1 
ATOM   1828  O  OE2   . GLU A 1 260 ? 125.648 127.752 120.945 1.00 12697. ? 260 GLU A OE2   1 
ATOM   1829  N  N     . LEU A 1 261 ? 126.555 132.797 117.777 1.00 12720. ? 261 LEU A N     1 
ATOM   1830  C  CA    . LEU A 1 261 ? 126.650 133.659 116.569 1.00 12716. ? 261 LEU A CA    1 
ATOM   1831  C  C     . LEU A 1 261 ? 127.595 132.997 115.554 1.00 12703. ? 261 LEU A C     1 
ATOM   1832  O  O     . LEU A 1 261 ? 127.405 133.218 114.338 1.00 12644. ? 261 LEU A O     1 
ATOM   1833  C  CB    . LEU A 1 261 ? 127.148 135.052 116.950 1.00 12728. ? 261 LEU A CB    1 
ATOM   1834  C  CG    . LEU A 1 261 ? 126.160 135.944 117.705 1.00 12662. ? 261 LEU A CG    1 
ATOM   1835  C  CD1   . LEU A 1 261 ? 126.828 137.258 118.068 1.00 12688. ? 261 LEU A CD1   1 
ATOM   1836  C  CD2   . LEU A 1 261 ? 124.932 136.191 116.848 1.00 12631. ? 261 LEU A CD2   1 
ATOM   1837  N  N     . GLY A 1 262 ? 128.574 132.224 116.036 1.00 12652. ? 262 GLY A N     1 
ATOM   1838  C  CA    . GLY A 1 262 ? 129.547 131.570 115.138 1.00 12568. ? 262 GLY A CA    1 
ATOM   1839  C  C     . GLY A 1 262 ? 130.933 132.171 115.286 1.00 12654. ? 262 GLY A C     1 
ATOM   1840  O  O     . GLY A 1 262 ? 131.718 132.085 114.318 1.00 12603. ? 262 GLY A O     1 
ATOM   1841  N  N     . PHE A 1 263 ? 131.227 132.765 116.447 1.00 12700. ? 263 PHE A N     1 
ATOM   1842  C  CA    . PHE A 1 263 ? 132.562 133.376 116.696 1.00 12711. ? 263 PHE A CA    1 
ATOM   1843  C  C     . PHE A 1 263 ? 133.540 132.298 117.165 1.00 12665. ? 263 PHE A C     1 
ATOM   1844  O  O     . PHE A 1 263 ? 133.149 131.432 117.978 1.00 12669. ? 263 PHE A O     1 
ATOM   1845  C  CB    . PHE A 1 263 ? 132.444 134.511 117.718 1.00 12737. ? 263 PHE A CB    1 
ATOM   1846  C  CG    . PHE A 1 263 ? 132.010 135.843 117.125 1.00 12741. ? 263 PHE A CG    1 
ATOM   1847  C  CD1   . PHE A 1 263 ? 130.663 136.154 116.977 1.00 12749. ? 263 PHE A CD1   1 
ATOM   1848  C  CD2   . PHE A 1 263 ? 132.950 136.783 116.722 1.00 12751. ? 263 PHE A CD2   1 
ATOM   1849  C  CE1   . PHE A 1 263 ? 130.272 137.367 116.435 1.00 12739. ? 263 PHE A CE1   1 
ATOM   1850  C  CE2   . PHE A 1 263 ? 132.554 137.993 116.179 1.00 12745. ? 263 PHE A CE2   1 
ATOM   1851  C  CZ    . PHE A 1 263 ? 131.217 138.284 116.039 1.00 12735. ? 263 PHE A CZ    1 
ATOM   1852  N  N     . LEU A 1 264 ? 134.781 132.354 116.672 1.00 12657. ? 264 LEU A N     1 
ATOM   1853  C  CA    . LEU A 1 264 ? 135.817 131.365 117.074 1.00 12657. ? 264 LEU A CA    1 
ATOM   1854  C  C     . LEU A 1 264 ? 136.713 131.989 118.155 1.00 12739. ? 264 LEU A C     1 
ATOM   1855  O  O     . LEU A 1 264 ? 137.088 133.172 118.001 1.00 12765. ? 264 LEU A O     1 
ATOM   1856  C  CB    . LEU A 1 264 ? 136.629 130.947 115.851 1.00 12615. ? 264 LEU A CB    1 
ATOM   1857  C  CG    . LEU A 1 264 ? 137.624 129.801 116.063 1.00 12642. ? 264 LEU A CG    1 
ATOM   1858  C  CD1   . LEU A 1 264 ? 136.911 128.554 116.558 1.00 12592. ? 264 LEU A CD1   1 
ATOM   1859  C  CD2   . LEU A 1 264 ? 138.381 129.507 114.780 1.00 12709. ? 264 LEU A CD2   1 
ATOM   1860  N  N     . GLU A 1 265 ? 137.042 131.224 119.200 1.00 12739. ? 265 GLU A N     1 
ATOM   1861  C  CA    . GLU A 1 265 ? 137.892 131.745 120.260 1.00 12739. ? 265 GLU A CA    1 
ATOM   1862  C  C     . GLU A 1 265 ? 139.357 131.558 119.890 1.00 12737. ? 265 GLU A C     1 
ATOM   1863  O  O     . GLU A 1 265 ? 139.752 130.497 119.398 1.00 12739. ? 265 GLU A O     1 
ATOM   1864  C  CB    . GLU A 1 265 ? 137.584 131.049 121.583 1.00 12739. ? 265 GLU A CB    1 
ATOM   1865  C  CG    . GLU A 1 265 ? 138.030 131.833 122.802 1.00 12752. ? 265 GLU A CG    1 
ATOM   1866  C  CD    . GLU A 1 265 ? 137.566 131.209 124.100 1.00 12759. ? 265 GLU A CD    1 
ATOM   1867  O  OE1   . GLU A 1 265 ? 136.928 130.137 124.052 1.00 12754. ? 265 GLU A OE1   1 
ATOM   1868  O  OE2   . GLU A 1 265 ? 137.838 131.793 125.170 1.00 12765. ? 265 GLU A OE2   1 
ATOM   1869  N  N     . ILE A 1 266 ? 140.164 132.588 120.135 1.00 12738. ? 266 ILE A N     1 
ATOM   1870  C  CA    . ILE A 1 266 ? 141.560 132.603 119.728 1.00 12719. ? 266 ILE A CA    1 
ATOM   1871  C  C     . ILE A 1 266 ? 142.428 133.011 120.910 1.00 12722. ? 266 ILE A C     1 
ATOM   1872  O  O     . ILE A 1 266 ? 141.961 133.601 121.886 1.00 12748. ? 266 ILE A O     1 
ATOM   1873  C  CB    . ILE A 1 266 ? 141.801 133.545 118.534 1.00 12703. ? 266 ILE A CB    1 
ATOM   1874  C  CG1   . ILE A 1 266 ? 141.240 134.931 118.843 1.00 12724. ? 266 ILE A CG1   1 
ATOM   1875  C  CG2   . ILE A 1 266 ? 141.179 132.977 117.273 1.00 12708. ? 266 ILE A CG2   1 
ATOM   1876  C  CD1   . ILE A 1 266 ? 141.453 135.934 117.747 1.00 12731. ? 266 ILE A CD1   1 
ATOM   1877  N  N     . GLU A 1 267 ? 143.714 132.683 120.807 1.00 12706. ? 267 GLU A N     1 
ATOM   1878  C  CA    . GLU A 1 267 ? 144.718 133.054 121.800 1.00 12719. ? 267 GLU A CA    1 
ATOM   1879  C  C     . GLU A 1 267 ? 145.866 133.748 121.079 1.00 12699. ? 267 GLU A C     1 
ATOM   1880  O  O     . GLU A 1 267 ? 146.659 133.095 120.394 1.00 12660. ? 267 GLU A O     1 
ATOM   1881  C  CB    . GLU A 1 267 ? 145.213 131.829 122.567 1.00 12752. ? 267 GLU A CB    1 
ATOM   1882  C  CG    . GLU A 1 267 ? 144.202 131.257 123.545 1.00 12762. ? 267 GLU A CG    1 
ATOM   1883  C  CD    . GLU A 1 267 ? 144.088 129.748 123.451 1.00 12761. ? 267 GLU A CD    1 
ATOM   1884  O  OE1   . GLU A 1 267 ? 144.999 129.049 123.940 1.00 12757. ? 267 GLU A OE1   1 
ATOM   1885  O  OE2   . GLU A 1 267 ? 143.085 129.260 122.887 1.00 12761. ? 267 GLU A OE2   1 
ATOM   1886  N  N     . THR A 1 268 ? 145.950 135.055 121.229 1.00 12724. ? 268 THR A N     1 
ATOM   1887  C  CA    . THR A 1 268 ? 146.996 135.870 120.637 1.00 12718. ? 268 THR A CA    1 
ATOM   1888  C  C     . THR A 1 268 ? 148.158 136.037 121.607 1.00 12748. ? 268 THR A C     1 
ATOM   1889  O  O     . THR A 1 268 ? 147.999 135.859 122.818 1.00 12763. ? 268 THR A O     1 
ATOM   1890  C  CB    . THR A 1 268 ? 146.435 137.241 120.244 1.00 12739. ? 268 THR A CB    1 
ATOM   1891  O  OG1   . THR A 1 268 ? 145.925 137.904 121.407 1.00 12759. ? 268 THR A OG1   1 
ATOM   1892  C  CG2   . THR A 1 268 ? 145.320 137.078 119.228 1.00 12689. ? 268 THR A CG2   1 
ATOM   1893  N  N     . PRO A 1 269 ? 149.352 136.364 121.108 1.00 12729. ? 269 PRO A N     1 
ATOM   1894  C  CA    . PRO A 1 269 ? 150.513 136.492 121.997 1.00 12735. ? 269 PRO A CA    1 
ATOM   1895  C  C     . PRO A 1 269 ? 150.316 137.563 123.060 1.00 12736. ? 269 PRO A C     1 
ATOM   1896  O  O     . PRO A 1 269 ? 149.680 138.591 122.825 1.00 12747. ? 269 PRO A O     1 
ATOM   1897  C  CB    . PRO A 1 269 ? 151.652 136.861 121.042 1.00 12707. ? 269 PRO A CB    1 
ATOM   1898  C  CG    . PRO A 1 269 ? 151.214 136.395 119.723 1.00 12592. ? 269 PRO A CG    1 
ATOM   1899  C  CD    . PRO A 1 269 ? 149.729 136.489 119.691 1.00 12599. ? 269 PRO A CD    1 
ATOM   1900  N  N     . MET A 1 270 ? 150.872 137.307 124.244 1.00 12735. ? 270 MET A N     1 
ATOM   1901  C  CA    . MET A 1 270 ? 150.824 138.252 125.347 1.00 12740. ? 270 MET A CA    1 
ATOM   1902  C  C     . MET A 1 270 ? 152.064 139.129 125.449 1.00 12743. ? 270 MET A C     1 
ATOM   1903  O  O     . MET A 1 270 ? 152.008 140.169 126.112 1.00 12753. ? 270 MET A O     1 
ATOM   1904  C  CB    . MET A 1 270 ? 150.619 137.512 126.675 1.00 12750. ? 270 MET A CB    1 
ATOM   1905  C  CG    . MET A 1 270 ? 149.204 137.017 126.890 1.00 12750. ? 270 MET A CG    1 
ATOM   1906  S  SD    . MET A 1 270 ? 148.718 137.060 128.621 1.00 12752. ? 270 MET A SD    1 
ATOM   1907  C  CE    . MET A 1 270 ? 146.941 136.959 128.468 1.00 12753. ? 270 MET A CE    1 
ATOM   1908  N  N     . MET A 1 271 ? 153.172 138.744 124.821 1.00 12732. ? 271 MET A N     1 
ATOM   1909  C  CA    . MET A 1 271 ? 154.340 139.605 124.730 1.00 12739. ? 271 MET A CA    1 
ATOM   1910  C  C     . MET A 1 271 ? 154.724 139.758 123.269 1.00 12737. ? 271 MET A C     1 
ATOM   1911  O  O     . MET A 1 271 ? 154.454 138.874 122.452 1.00 12741. ? 271 MET A O     1 
ATOM   1912  C  CB    . MET A 1 271 ? 155.546 139.063 125.508 1.00 12750. ? 271 MET A CB    1 
ATOM   1913  C  CG    . MET A 1 271 ? 155.257 138.627 126.923 1.00 12755. ? 271 MET A CG    1 
ATOM   1914  S  SD    . MET A 1 271 ? 156.237 137.195 127.403 1.00 12743. ? 271 MET A SD    1 
ATOM   1915  C  CE    . MET A 1 271 ? 155.978 136.121 126.001 1.00 12748. ? 271 MET A CE    1 
ATOM   1916  N  N     . ASN A 1 272 ? 155.355 140.882 122.949 1.00 12735. ? 272 ASN A N     1 
ATOM   1917  C  CA    . ASN A 1 272 ? 155.837 141.142 121.604 1.00 12725. ? 272 ASN A CA    1 
ATOM   1918  C  C     . ASN A 1 272 ? 157.229 141.746 121.692 1.00 12739. ? 272 ASN A C     1 
ATOM   1919  O  O     . ASN A 1 272 ? 157.607 142.348 122.699 1.00 12761. ? 272 ASN A O     1 
ATOM   1920  C  CB    . ASN A 1 272 ? 154.891 142.074 120.838 1.00 12736. ? 272 ASN A CB    1 
ATOM   1921  C  CG    . ASN A 1 272 ? 155.021 141.926 119.337 1.00 12755. ? 272 ASN A CG    1 
ATOM   1922  O  OD1   . ASN A 1 272 ? 155.755 141.067 118.848 1.00 12762. ? 272 ASN A OD1   1 
ATOM   1923  N  ND2   . ASN A 1 272 ? 154.310 142.766 118.596 1.00 12776. ? 272 ASN A ND2   1 
ATOM   1924  N  N     . ILE A 1 273 ? 158.000 141.573 120.618 1.00 12792. ? 273 ILE A N     1 
ATOM   1925  C  CA    . ILE A 1 273 ? 159.322 142.174 120.518 1.00 12804. ? 273 ILE A CA    1 
ATOM   1926  C  C     . ILE A 1 273 ? 159.265 143.611 120.033 1.00 12816. ? 273 ILE A C     1 
ATOM   1927  O  O     . ILE A 1 273 ? 160.309 144.271 119.949 1.00 12817. ? 273 ILE A O     1 
ATOM   1928  C  CB    . ILE A 1 273 ? 160.239 141.342 119.601 1.00 12801. ? 273 ILE A CB    1 
ATOM   1929  C  CG1   . ILE A 1 273 ? 159.730 141.387 118.162 1.00 12799. ? 273 ILE A CG1   1 
ATOM   1930  C  CG2   . ILE A 1 273 ? 160.314 139.907 120.085 1.00 12807. ? 273 ILE A CG2   1 
ATOM   1931  C  CD1   . ILE A 1 273 ? 160.629 140.676 117.178 1.00 12778. ? 273 ILE A CD1   1 
ATOM   1932  N  N     . ILE A 1 274 ? 158.079 144.117 119.714 1.00 12852. ? 274 ILE A N     1 
ATOM   1933  C  CA    . ILE A 1 274 ? 157.893 145.468 119.203 1.00 12875. ? 274 ILE A CA    1 
ATOM   1934  C  C     . ILE A 1 274 ? 157.140 146.265 120.258 1.00 12897. ? 274 ILE A C     1 
ATOM   1935  O  O     . ILE A 1 274 ? 156.079 145.827 120.705 1.00 12876. ? 274 ILE A O     1 
ATOM   1936  C  CB    . ILE A 1 274 ? 157.125 145.492 117.869 1.00 12877. ? 274 ILE A CB    1 
ATOM   1937  C  CG1   . ILE A 1 274 ? 157.904 144.757 116.774 1.00 12863. ? 274 ILE A CG1   1 
ATOM   1938  C  CG2   . ILE A 1 274 ? 156.833 146.921 117.446 1.00 12940. ? 274 ILE A CG2   1 
ATOM   1939  C  CD1   . ILE A 1 274 ? 159.404 144.953 116.834 1.00 12876. ? 274 ILE A CD1   1 
ATOM   1940  N  N     . PRO A 1 275 ? 157.652 147.418 120.695 1.00 13781. ? 275 PRO A N     1 
ATOM   1941  C  CA    . PRO A 1 275 ? 156.888 148.234 121.654 1.00 13804. ? 275 PRO A CA    1 
ATOM   1942  C  C     . PRO A 1 275 ? 155.535 148.674 121.127 1.00 13857. ? 275 PRO A C     1 
ATOM   1943  O  O     . PRO A 1 275 ? 154.579 148.789 121.903 1.00 13846. ? 275 PRO A O     1 
ATOM   1944  C  CB    . PRO A 1 275 ? 157.813 149.435 121.902 1.00 13839. ? 275 PRO A CB    1 
ATOM   1945  C  CG    . PRO A 1 275 ? 159.171 148.961 121.526 1.00 13843. ? 275 PRO A CG    1 
ATOM   1946  C  CD    . PRO A 1 275 ? 158.978 147.985 120.411 1.00 13835. ? 275 PRO A CD    1 
ATOM   1947  N  N     . GLY A 1 276 ? 155.426 148.923 119.826 1.00 15418. ? 276 GLY A N     1 
ATOM   1948  C  CA    . GLY A 1 276 ? 154.204 149.446 119.254 1.00 15476. ? 276 GLY A CA    1 
ATOM   1949  C  C     . GLY A 1 276 ? 154.124 150.954 119.356 1.00 15523. ? 276 GLY A C     1 
ATOM   1950  O  O     . GLY A 1 276 ? 154.945 151.624 119.988 1.00 15549. ? 276 GLY A O     1 
ATOM   1951  N  N     . GLY A 1 277 ? 153.096 151.502 118.710 1.00 15836. ? 277 GLY A N     1 
ATOM   1952  C  CA    . GLY A 1 277 ? 152.873 152.933 118.691 1.00 15859. ? 277 GLY A CA    1 
ATOM   1953  C  C     . GLY A 1 277 ? 151.833 153.449 119.658 1.00 15802. ? 277 GLY A C     1 
ATOM   1954  O  O     . GLY A 1 277 ? 151.494 154.638 119.598 1.00 15836. ? 277 GLY A O     1 
ATOM   1955  N  N     . ALA A 1 278 ? 151.309 152.611 120.547 1.00 15336. ? 278 ALA A N     1 
ATOM   1956  C  CA    . ALA A 1 278 ? 150.285 153.053 121.478 1.00 15295. ? 278 ALA A CA    1 
ATOM   1957  C  C     . ALA A 1 278 ? 150.864 154.033 122.493 1.00 15368. ? 278 ALA A C     1 
ATOM   1958  O  O     . ALA A 1 278 ? 152.037 153.965 122.868 1.00 15397. ? 278 ALA A O     1 
ATOM   1959  C  CB    . ALA A 1 278 ? 149.663 151.858 122.196 1.00 15235. ? 278 ALA A CB    1 
ATOM   1960  N  N     . VAL A 1 279 ? 150.016 154.961 122.936 1.00 14732. ? 279 VAL A N     1 
ATOM   1961  C  CA    . VAL A 1 279 ? 150.440 155.933 123.937 1.00 14745. ? 279 VAL A CA    1 
ATOM   1962  C  C     . VAL A 1 279 ? 150.597 155.278 125.304 1.00 14702. ? 279 VAL A C     1 
ATOM   1963  O  O     . VAL A 1 279 ? 151.445 155.694 126.101 1.00 14716. ? 279 VAL A O     1 
ATOM   1964  C  CB    . VAL A 1 279 ? 149.448 157.106 123.985 1.00 14625. ? 279 VAL A CB    1 
ATOM   1965  C  CG1   . VAL A 1 279 ? 149.940 158.189 124.932 1.00 14655. ? 279 VAL A CG1   1 
ATOM   1966  C  CG2   . VAL A 1 279 ? 149.233 157.670 122.592 1.00 14593. ? 279 VAL A CG2   1 
ATOM   1967  N  N     . ALA A 1 280 ? 149.797 154.253 125.596 1.00 13197. ? 280 ALA A N     1 
ATOM   1968  C  CA    . ALA A 1 280 ? 149.840 153.611 126.902 1.00 13168. ? 280 ALA A CA    1 
ATOM   1969  C  C     . ALA A 1 280 ? 151.214 153.011 127.167 1.00 13249. ? 280 ALA A C     1 
ATOM   1970  O  O     . ALA A 1 280 ? 151.795 152.341 126.310 1.00 13270. ? 280 ALA A O     1 
ATOM   1971  C  CB    . ALA A 1 280 ? 148.767 152.527 126.992 1.00 13120. ? 280 ALA A CB    1 
ATOM   1972  N  N     . LYS A 1 281 ? 151.732 153.262 128.361 1.00 12761. ? 281 LYS A N     1 
ATOM   1973  C  CA    . LYS A 1 281 ? 153.047 152.755 128.724 1.00 12745. ? 281 LYS A CA    1 
ATOM   1974  C  C     . LYS A 1 281 ? 152.985 151.244 128.910 1.00 12741. ? 281 LYS A C     1 
ATOM   1975  O  O     . LYS A 1 281 ? 152.072 150.744 129.577 1.00 12757. ? 281 LYS A O     1 
ATOM   1976  C  CB    . LYS A 1 281 ? 153.542 153.428 129.998 1.00 12747. ? 281 LYS A CB    1 
ATOM   1977  C  CG    . LYS A 1 281 ? 154.216 154.766 129.761 1.00 12747. ? 281 LYS A CG    1 
ATOM   1978  C  CD    . LYS A 1 281 ? 154.932 155.252 131.007 1.00 12743. ? 281 LYS A CD    1 
ATOM   1979  C  CE    . LYS A 1 281 ? 153.947 155.752 132.049 1.00 12749. ? 281 LYS A CE    1 
ATOM   1980  N  NZ    . LYS A 1 281 ? 152.991 156.739 131.477 1.00 12736. ? 281 LYS A NZ    1 
ATOM   1981  N  N     . PRO A 1 282 ? 153.919 150.490 128.345 1.00 12730. ? 282 PRO A N     1 
ATOM   1982  C  CA    . PRO A 1 282 ? 153.871 149.032 128.442 1.00 12738. ? 282 PRO A CA    1 
ATOM   1983  C  C     . PRO A 1 282 ? 154.638 148.511 129.653 1.00 12752. ? 282 PRO A C     1 
ATOM   1984  O  O     . PRO A 1 282 ? 155.317 149.252 130.365 1.00 12751. ? 282 PRO A O     1 
ATOM   1985  C  CB    . PRO A 1 282 ? 154.548 148.589 127.142 1.00 12743. ? 282 PRO A CB    1 
ATOM   1986  C  CG    . PRO A 1 282 ? 155.550 149.666 126.875 1.00 12742. ? 282 PRO A CG    1 
ATOM   1987  C  CD    . PRO A 1 282 ? 155.039 150.945 127.505 1.00 12742. ? 282 PRO A CD    1 
ATOM   1988  N  N     . PHE A 1 283 ? 154.509 147.207 129.871 1.00 12755. ? 283 PHE A N     1 
ATOM   1989  C  CA    . PHE A 1 283 ? 155.274 146.494 130.885 1.00 12742. ? 283 PHE A CA    1 
ATOM   1990  C  C     . PHE A 1 283 ? 156.470 145.847 130.196 1.00 12737. ? 283 PHE A C     1 
ATOM   1991  O  O     . PHE A 1 283 ? 156.314 144.866 129.464 1.00 12747. ? 283 PHE A O     1 
ATOM   1992  C  CB    . PHE A 1 283 ? 154.412 145.447 131.586 1.00 12741. ? 283 PHE A CB    1 
ATOM   1993  C  CG    . PHE A 1 283 ? 153.568 145.996 132.699 1.00 12740. ? 283 PHE A CG    1 
ATOM   1994  C  CD1   . PHE A 1 283 ? 154.054 146.051 133.992 1.00 12748. ? 283 PHE A CD1   1 
ATOM   1995  C  CD2   . PHE A 1 283 ? 152.284 146.446 132.456 1.00 12749. ? 283 PHE A CD2   1 
ATOM   1996  C  CE1   . PHE A 1 283 ? 153.278 146.550 135.016 1.00 12752. ? 283 PHE A CE1   1 
ATOM   1997  C  CE2   . PHE A 1 283 ? 151.505 146.945 133.478 1.00 12746. ? 283 PHE A CE2   1 
ATOM   1998  C  CZ    . PHE A 1 283 ? 152.002 146.997 134.758 1.00 12747. ? 283 PHE A CZ    1 
ATOM   1999  N  N     . ILE A 1 284 ? 157.656 146.395 130.424 1.00 12720. ? 284 ILE A N     1 
ATOM   2000  C  CA    . ILE A 1 284 ? 158.860 145.877 129.788 1.00 12716. ? 284 ILE A CA    1 
ATOM   2001  C  C     . ILE A 1 284 ? 159.293 144.600 130.495 1.00 12727. ? 284 ILE A C     1 
ATOM   2002  O  O     . ILE A 1 284 ? 159.015 144.391 131.680 1.00 12751. ? 284 ILE A O     1 
ATOM   2003  C  CB    . ILE A 1 284 ? 159.987 146.929 129.795 1.00 12732. ? 284 ILE A CB    1 
ATOM   2004  C  CG1   . ILE A 1 284 ? 159.414 148.344 129.721 1.00 12743. ? 284 ILE A CG1   1 
ATOM   2005  C  CG2   . ILE A 1 284 ? 160.937 146.693 128.636 1.00 12752. ? 284 ILE A CG2   1 
ATOM   2006  C  CD1   . ILE A 1 284 ? 158.745 148.671 128.415 1.00 12749. ? 284 ILE A CD1   1 
ATOM   2007  N  N     . THR A 1 285 ? 159.985 143.736 129.758 1.00 12737. ? 285 THR A N     1 
ATOM   2008  C  CA    . THR A 1 285 ? 160.448 142.463 130.281 1.00 12743. ? 285 THR A CA    1 
ATOM   2009  C  C     . THR A 1 285 ? 161.717 142.107 129.522 1.00 12758. ? 285 THR A C     1 
ATOM   2010  O  O     . THR A 1 285 ? 161.949 142.603 128.422 1.00 12773. ? 285 THR A O     1 
ATOM   2011  C  CB    . THR A 1 285 ? 159.366 141.386 130.116 1.00 12757. ? 285 THR A CB    1 
ATOM   2012  O  OG1   . THR A 1 285 ? 158.180 141.793 130.807 1.00 12760. ? 285 THR A OG1   1 
ATOM   2013  C  CG2   . THR A 1 285 ? 159.810 140.070 130.696 1.00 12763. ? 285 THR A CG2   1 
ATOM   2014  N  N     . TYR A 1 286 ? 162.547 141.253 130.109 1.00 13252. ? 286 TYR A N     1 
ATOM   2015  C  CA    . TYR A 1 286 ? 163.788 140.838 129.470 1.00 13277. ? 286 TYR A CA    1 
ATOM   2016  C  C     . TYR A 1 286 ? 163.782 139.335 129.231 1.00 13276. ? 286 TYR A C     1 
ATOM   2017  O  O     . TYR A 1 286 ? 163.369 138.561 130.097 1.00 13277. ? 286 TYR A O     1 
ATOM   2018  C  CB    . TYR A 1 286 ? 165.000 141.225 130.315 1.00 13287. ? 286 TYR A CB    1 
ATOM   2019  C  CG    . TYR A 1 286 ? 166.302 141.149 129.561 1.00 13290. ? 286 TYR A CG    1 
ATOM   2020  C  CD1   . TYR A 1 286 ? 166.735 142.208 128.780 1.00 13300. ? 286 TYR A CD1   1 
ATOM   2021  C  CD2   . TYR A 1 286 ? 167.098 140.017 129.628 1.00 13301. ? 286 TYR A CD2   1 
ATOM   2022  C  CE1   . TYR A 1 286 ? 167.924 142.142 128.087 1.00 13316. ? 286 TYR A CE1   1 
ATOM   2023  C  CE2   . TYR A 1 286 ? 168.288 139.941 128.939 1.00 13320. ? 286 TYR A CE2   1 
ATOM   2024  C  CZ    . TYR A 1 286 ? 168.696 141.006 128.171 1.00 13332. ? 286 TYR A CZ    1 
ATOM   2025  O  OH    . TYR A 1 286 ? 169.883 140.935 127.483 1.00 13349. ? 286 TYR A OH    1 
ATOM   2026  N  N     . HIS A 1 287 ? 164.243 138.930 128.050 1.00 13223. ? 287 HIS A N     1 
ATOM   2027  C  CA    . HIS A 1 287 ? 164.413 137.529 127.693 1.00 13230. ? 287 HIS A CA    1 
ATOM   2028  C  C     . HIS A 1 287 ? 165.902 137.260 127.532 1.00 13265. ? 287 HIS A C     1 
ATOM   2029  O  O     . HIS A 1 287 ? 166.555 137.861 126.669 1.00 13302. ? 287 HIS A O     1 
ATOM   2030  C  CB    . HIS A 1 287 ? 163.660 137.195 126.407 1.00 13239. ? 287 HIS A CB    1 
ATOM   2031  C  CG    . HIS A 1 287 ? 163.345 135.741 126.252 1.00 13221. ? 287 HIS A CG    1 
ATOM   2032  N  ND1   . HIS A 1 287 ? 164.241 134.840 125.720 1.00 13271. ? 287 HIS A ND1   1 
ATOM   2033  C  CD2   . HIS A 1 287 ? 162.234 135.032 126.556 1.00 13208. ? 287 HIS A CD2   1 
ATOM   2034  C  CE1   . HIS A 1 287 ? 163.695 133.637 125.705 1.00 13281. ? 287 HIS A CE1   1 
ATOM   2035  N  NE2   . HIS A 1 287 ? 162.478 133.726 126.207 1.00 13241. ? 287 HIS A NE2   1 
ATOM   2036  N  N     . ASN A 1 288 ? 166.405 136.411 128.424 1.00 13510. ? 288 ASN A N     1 
ATOM   2037  C  CA    . ASN A 1 288 ? 167.860 136.169 128.500 1.00 13523. ? 288 ASN A CA    1 
ATOM   2038  C  C     . ASN A 1 288 ? 168.320 135.362 127.294 1.00 13566. ? 288 ASN A C     1 
ATOM   2039  O  O     . ASN A 1 288 ? 169.432 135.606 126.819 1.00 13565. ? 288 ASN A O     1 
ATOM   2040  C  CB    . ASN A 1 288 ? 168.176 135.534 129.844 1.00 13514. ? 288 ASN A CB    1 
ATOM   2041  C  CG    . ASN A 1 288 ? 167.593 136.303 131.001 1.00 13510. ? 288 ASN A CG    1 
ATOM   2042  O  OD1   . ASN A 1 288 ? 166.687 135.810 131.677 1.00 13498. ? 288 ASN A OD1   1 
ATOM   2043  N  ND2   . ASN A 1 288 ? 168.088 137.505 131.239 1.00 13520. ? 288 ASN A ND2   1 
ATOM   2044  N  N     . GLU A 1 289 ? 167.516 134.422 126.836 1.00 15185. ? 289 GLU A N     1 
ATOM   2045  C  CA    . GLU A 1 289 ? 167.984 133.563 125.726 1.00 15242. ? 289 GLU A CA    1 
ATOM   2046  C  C     . GLU A 1 289 ? 168.044 134.383 124.439 1.00 15234. ? 289 GLU A C     1 
ATOM   2047  O  O     . GLU A 1 289 ? 169.053 134.277 123.732 1.00 15272. ? 289 GLU A O     1 
ATOM   2048  C  CB    . GLU A 1 289 ? 167.040 132.386 125.512 1.00 15268. ? 289 GLU A CB    1 
ATOM   2049  C  CG    . GLU A 1 289 ? 167.501 131.418 124.428 1.00 15284. ? 289 GLU A CG    1 
ATOM   2050  C  CD    . GLU A 1 289 ? 166.525 131.314 123.271 1.00 15270. ? 289 GLU A CD    1 
ATOM   2051  O  OE1   . GLU A 1 289 ? 165.527 132.057 123.286 1.00 15275. ? 289 GLU A OE1   1 
ATOM   2052  O  OE2   . GLU A 1 289 ? 166.752 130.487 122.366 1.00 15252. ? 289 GLU A OE2   1 
ATOM   2053  N  N     . LEU A 1 290 ? 166.988 135.153 124.159 1.00 14518. ? 290 LEU A N     1 
ATOM   2054  C  CA    . LEU A 1 290 ? 166.971 136.031 122.960 1.00 14515. ? 290 LEU A CA    1 
ATOM   2055  C  C     . LEU A 1 290 ? 167.852 137.256 123.240 1.00 14511. ? 290 LEU A C     1 
ATOM   2056  O  O     . LEU A 1 290 ? 168.105 138.031 122.292 1.00 14520. ? 290 LEU A O     1 
ATOM   2057  C  CB    . LEU A 1 290 ? 165.534 136.438 122.641 1.00 14510. ? 290 LEU A CB    1 
ATOM   2058  C  CG    . LEU A 1 290 ? 164.580 135.304 122.254 1.00 14499. ? 290 LEU A CG    1 
ATOM   2059  C  CD1   . LEU A 1 290 ? 163.177 135.850 122.058 1.00 14482. ? 290 LEU A CD1   1 
ATOM   2060  C  CD2   . LEU A 1 290 ? 165.061 134.604 120.995 1.00 14459. ? 290 LEU A CD2   1 
ATOM   2061  N  N     . ASP A 1 291 ? 168.287 137.421 124.494 1.00 14483. ? 291 ASP A N     1 
ATOM   2062  C  CA    . ASP A 1 291 ? 169.167 138.565 124.863 1.00 14484. ? 291 ASP A CA    1 
ATOM   2063  C  C     . ASP A 1 291 ? 168.488 139.867 124.424 1.00 14477. ? 291 ASP A C     1 
ATOM   2064  O  O     . ASP A 1 291 ? 169.161 140.692 123.767 1.00 14489. ? 291 ASP A O     1 
ATOM   2065  C  CB    . ASP A 1 291 ? 170.561 138.380 124.281 1.00 14498. ? 291 ASP A CB    1 
ATOM   2066  C  CG    . ASP A 1 291 ? 171.574 139.470 124.602 1.00 14499. ? 291 ASP A CG    1 
ATOM   2067  O  OD1   . ASP A 1 291 ? 171.919 139.621 125.791 1.00 14493. ? 291 ASP A OD1   1 
ATOM   2068  O  OD2   . ASP A 1 291 ? 172.009 140.160 123.656 1.00 14508. ? 291 ASP A OD2   1 
ATOM   2069  N  N     . MET A 1 292 ? 167.207 140.043 124.765 1.00 14411. ? 292 MET A N     1 
ATOM   2070  C  CA    . MET A 1 292 ? 166.458 141.245 124.310 1.00 14413. ? 292 MET A CA    1 
ATOM   2071  C  C     . MET A 1 292 ? 165.297 141.546 125.271 1.00 14367. ? 292 MET A C     1 
ATOM   2072  O  O     . MET A 1 292 ? 165.114 140.779 126.242 1.00 14371. ? 292 MET A O     1 
ATOM   2073  C  CB    . MET A 1 292 ? 165.883 141.030 122.907 1.00 14438. ? 292 MET A CB    1 
ATOM   2074  C  CG    . MET A 1 292 ? 164.816 139.955 122.840 1.00 14435. ? 292 MET A CG    1 
ATOM   2075  S  SD    . MET A 1 292 ? 164.220 139.704 121.157 1.00 14404. ? 292 MET A SD    1 
ATOM   2076  C  CE    . MET A 1 292 ? 165.797 139.479 120.324 1.00 14406. ? 292 MET A CE    1 
ATOM   2077  N  N     . ASN A 1 293 ? 164.547 142.620 125.002 1.00 12806. ? 293 ASN A N     1 
ATOM   2078  C  CA    . ASN A 1 293 ? 163.388 142.997 125.859 1.00 12758. ? 293 ASN A CA    1 
ATOM   2079  C  C     . ASN A 1 293 ? 162.081 142.590 125.169 1.00 12755. ? 293 ASN A C     1 
ATOM   2080  O  O     . ASN A 1 293 ? 162.034 142.634 123.920 1.00 12787. ? 293 ASN A O     1 
ATOM   2081  C  CB    . ASN A 1 293 ? 163.401 144.484 126.195 1.00 12743. ? 293 ASN A CB    1 
ATOM   2082  C  CG    . ASN A 1 293 ? 164.464 144.826 127.209 1.00 12756. ? 293 ASN A CG    1 
ATOM   2083  O  OD1   . ASN A 1 293 ? 164.422 144.337 128.344 1.00 12774. ? 293 ASN A OD1   1 
ATOM   2084  N  ND2   . ASN A 1 293 ? 165.416 145.665 126.828 1.00 12758. ? 293 ASN A ND2   1 
ATOM   2085  N  N     . LEU A 1 294 ? 161.062 142.217 125.952 1.00 12732. ? 294 LEU A N     1 
ATOM   2086  C  CA    . LEU A 1 294 ? 159.767 141.803 125.373 1.00 12734. ? 294 LEU A CA    1 
ATOM   2087  C  C     . LEU A 1 294 ? 158.754 142.757 125.997 1.00 12749. ? 294 LEU A C     1 
ATOM   2088  O  O     . LEU A 1 294 ? 158.950 143.121 127.148 1.00 12769. ? 294 LEU A O     1 
ATOM   2089  C  CB    . LEU A 1 294 ? 159.428 140.339 125.623 1.00 12732. ? 294 LEU A CB    1 
ATOM   2090  C  CG    . LEU A 1 294 ? 160.460 139.316 125.156 1.00 12734. ? 294 LEU A CG    1 
ATOM   2091  C  CD1   . LEU A 1 294 ? 159.909 137.936 125.418 1.00 12747. ? 294 LEU A CD1   1 
ATOM   2092  C  CD2   . LEU A 1 294 ? 160.685 139.525 123.680 1.00 12748. ? 294 LEU A CD2   1 
ATOM   2093  N  N     . TYR A 1 295 ? 157.753 143.181 125.253 1.00 12739. ? 295 TYR A N     1 
ATOM   2094  C  CA    . TYR A 1 295 ? 156.802 144.195 125.678 1.00 12731. ? 295 TYR A CA    1 
ATOM   2095  C  C     . TYR A 1 295 ? 155.435 143.554 125.848 1.00 12741. ? 295 TYR A C     1 
ATOM   2096  O  O     . TYR A 1 295 ? 154.979 142.814 124.971 1.00 12761. ? 295 TYR A O     1 
ATOM   2097  C  CB    . TYR A 1 295 ? 156.752 145.343 124.671 1.00 12745. ? 295 TYR A CB    1 
ATOM   2098  C  CG    . TYR A 1 295 ? 158.077 146.051 124.523 1.00 12747. ? 295 TYR A CG    1 
ATOM   2099  C  CD1   . TYR A 1 295 ? 159.066 145.547 123.694 1.00 12755. ? 295 TYR A CD1   1 
ATOM   2100  C  CD2   . TYR A 1 295 ? 158.345 147.214 125.223 1.00 12747. ? 295 TYR A CD2   1 
ATOM   2101  C  CE1   . TYR A 1 295 ? 160.280 146.185 123.561 1.00 12753. ? 295 TYR A CE1   1 
ATOM   2102  C  CE2   . TYR A 1 295 ? 159.556 147.860 125.096 1.00 12752. ? 295 TYR A CE2   1 
ATOM   2103  C  CZ    . TYR A 1 295 ? 160.519 147.341 124.264 1.00 12750. ? 295 TYR A CZ    1 
ATOM   2104  O  OH    . TYR A 1 295 ? 161.728 147.983 124.134 1.00 12752. ? 295 TYR A OH    1 
ATOM   2105  N  N     . MET A 1 296 ? 154.791 143.836 126.975 1.00 12748. ? 296 MET A N     1 
ATOM   2106  C  CA    . MET A 1 296 ? 153.517 143.209 127.283 1.00 12754. ? 296 MET A CA    1 
ATOM   2107  C  C     . MET A 1 296 ? 152.400 143.737 126.393 1.00 12754. ? 296 MET A C     1 
ATOM   2108  O  O     . MET A 1 296 ? 152.448 144.861 125.887 1.00 12768. ? 296 MET A O     1 
ATOM   2109  C  CB    . MET A 1 296 ? 153.162 143.411 128.754 1.00 12755. ? 296 MET A CB    1 
ATOM   2110  C  CG    . MET A 1 296 ? 152.702 142.133 129.412 1.00 12754. ? 296 MET A CG    1 
ATOM   2111  S  SD    . MET A 1 296 ? 153.964 140.856 129.457 1.00 12748. ? 296 MET A SD    1 
ATOM   2112  C  CE    . MET A 1 296 ? 152.920 139.405 129.394 1.00 12757. ? 296 MET A CE    1 
ATOM   2113  N  N     . ARG A 1 297 ? 151.385 142.900 126.211 1.00 12739. ? 297 ARG A N     1 
ATOM   2114  C  CA    . ARG A 1 297 ? 150.294 143.201 125.296 1.00 12725. ? 297 ARG A CA    1 
ATOM   2115  C  C     . ARG A 1 297 ? 149.406 144.307 125.851 1.00 12739. ? 297 ARG A C     1 
ATOM   2116  O  O     . ARG A 1 297 ? 148.970 144.252 127.004 1.00 12757. ? 297 ARG A O     1 
ATOM   2117  C  CB    . ARG A 1 297 ? 149.477 141.937 125.048 1.00 12737. ? 297 ARG A CB    1 
ATOM   2118  C  CG    . ARG A 1 297 ? 148.118 142.168 124.438 1.00 12754. ? 297 ARG A CG    1 
ATOM   2119  C  CD    . ARG A 1 297 ? 147.467 140.848 124.092 1.00 12737. ? 297 ARG A CD    1 
ATOM   2120  N  NE    . ARG A 1 297 ? 146.655 140.342 125.191 1.00 12720. ? 297 ARG A NE    1 
ATOM   2121  C  CZ    . ARG A 1 297 ? 145.987 139.199 125.160 1.00 12737. ? 297 ARG A CZ    1 
ATOM   2122  N  NH1   . ARG A 1 297 ? 146.013 138.413 124.098 1.00 12749. ? 297 ARG A NH1   1 
ATOM   2123  N  NH2   . ARG A 1 297 ? 145.276 138.835 126.222 1.00 12754. ? 297 ARG A NH2   1 
ATOM   2124  N  N     . ILE A 1 298 ? 149.133 145.308 125.022 1.00 12740. ? 298 ILE A N     1 
ATOM   2125  C  CA    . ILE A 1 298 ? 148.203 146.373 125.362 1.00 12731. ? 298 ILE A CA    1 
ATOM   2126  C  C     . ILE A 1 298 ? 146.816 146.103 124.795 1.00 12733. ? 298 ILE A C     1 
ATOM   2127  O  O     . ILE A 1 298 ? 145.812 146.303 125.480 1.00 12735. ? 298 ILE A O     1 
ATOM   2128  C  CB    . ILE A 1 298 ? 148.752 147.732 124.877 1.00 12732. ? 298 ILE A CB    1 
ATOM   2129  C  CG1   . ILE A 1 298 ? 149.875 148.207 125.798 1.00 12751. ? 298 ILE A CG1   1 
ATOM   2130  C  CG2   . ILE A 1 298 ? 147.651 148.771 124.814 1.00 12742. ? 298 ILE A CG2   1 
ATOM   2131  C  CD1   . ILE A 1 298 ? 150.823 149.182 125.149 1.00 12767. ? 298 ILE A CD1   1 
ATOM   2132  N  N     . ALA A 1 299 ? 146.745 145.634 123.547 1.00 12742. ? 299 ALA A N     1 
ATOM   2133  C  CA    . ALA A 1 299 ? 145.493 145.276 122.909 1.00 12725. ? 299 ALA A CA    1 
ATOM   2134  C  C     . ALA A 1 299 ? 145.777 144.253 121.821 1.00 12727. ? 299 ALA A C     1 
ATOM   2135  O  O     . ALA A 1 299 ? 146.798 144.366 121.128 1.00 12725. ? 299 ALA A O     1 
ATOM   2136  C  CB    . ALA A 1 299 ? 144.787 146.494 122.310 1.00 12683. ? 299 ALA A CB    1 
ATOM   2137  N  N     . PRO A 1 300 ? 144.913 143.254 121.649 1.00 12720. ? 300 PRO A N     1 
ATOM   2138  C  CA    . PRO A 1 300 ? 145.157 142.226 120.629 1.00 12731. ? 300 PRO A CA    1 
ATOM   2139  C  C     . PRO A 1 300 ? 144.606 142.581 119.255 1.00 12743. ? 300 PRO A C     1 
ATOM   2140  O  O     . PRO A 1 300 ? 144.423 141.694 118.417 1.00 12759. ? 300 PRO A O     1 
ATOM   2141  C  CB    . PRO A 1 300 ? 144.450 140.998 121.210 1.00 12747. ? 300 PRO A CB    1 
ATOM   2142  C  CG    . PRO A 1 300 ? 143.326 141.567 122.002 1.00 12751. ? 300 PRO A CG    1 
ATOM   2143  C  CD    . PRO A 1 300 ? 143.752 142.929 122.495 1.00 12746. ? 300 PRO A CD    1 
ATOM   2144  N  N     . GLU A 1 301 ? 144.330 143.867 119.020 1.00 12739. ? 301 GLU A N     1 
ATOM   2145  C  CA    . GLU A 1 301 ? 143.638 144.282 117.802 1.00 12735. ? 301 GLU A CA    1 
ATOM   2146  C  C     . GLU A 1 301 ? 144.380 143.840 116.546 1.00 12735. ? 301 GLU A C     1 
ATOM   2147  O  O     . GLU A 1 301 ? 143.772 143.315 115.605 1.00 12751. ? 301 GLU A O     1 
ATOM   2148  C  CB    . GLU A 1 301 ? 143.463 145.800 117.797 1.00 12740. ? 301 GLU A CB    1 
ATOM   2149  C  CG    . GLU A 1 301 ? 142.779 146.360 119.024 1.00 12721. ? 301 GLU A CG    1 
ATOM   2150  C  CD    . GLU A 1 301 ? 142.305 147.784 118.815 1.00 12685. ? 301 GLU A CD    1 
ATOM   2151  O  OE1   . GLU A 1 301 ? 141.691 148.058 117.762 1.00 12759. ? 301 GLU A OE1   1 
ATOM   2152  O  OE2   . GLU A 1 301 ? 142.553 148.631 119.698 1.00 12572. ? 301 GLU A OE2   1 
ATOM   2153  N  N     . LEU A 1 302 ? 145.695 144.059 116.507 1.00 12725. ? 302 LEU A N     1 
ATOM   2154  C  CA    . LEU A 1 302 ? 146.452 143.798 115.286 1.00 12727. ? 302 LEU A CA    1 
ATOM   2155  C  C     . LEU A 1 302 ? 146.424 142.321 114.916 1.00 12733. ? 302 LEU A C     1 
ATOM   2156  O  O     . LEU A 1 302 ? 146.248 141.970 113.743 1.00 12755. ? 302 LEU A O     1 
ATOM   2157  C  CB    . LEU A 1 302 ? 147.889 144.289 115.450 1.00 12744. ? 302 LEU A CB    1 
ATOM   2158  C  CG    . LEU A 1 302 ? 148.044 145.789 115.709 1.00 12741. ? 302 LEU A CG    1 
ATOM   2159  C  CD1   . LEU A 1 302 ? 149.491 146.215 115.560 1.00 12766. ? 302 LEU A CD1   1 
ATOM   2160  C  CD2   . LEU A 1 302 ? 147.154 146.593 114.779 1.00 12747. ? 302 LEU A CD2   1 
ATOM   2161  N  N     . TYR A 1 303 ? 146.590 141.439 115.900 1.00 12729. ? 303 TYR A N     1 
ATOM   2162  C  CA    . TYR A 1 303 ? 146.573 140.008 115.616 1.00 12676. ? 303 TYR A CA    1 
ATOM   2163  C  C     . TYR A 1 303 ? 145.189 139.544 115.179 1.00 12704. ? 303 TYR A C     1 
ATOM   2164  O  O     . TYR A 1 303 ? 145.066 138.698 114.287 1.00 12699. ? 303 TYR A O     1 
ATOM   2165  C  CB    . TYR A 1 303 ? 147.050 139.231 116.838 1.00 12649. ? 303 TYR A CB    1 
ATOM   2166  C  CG    . TYR A 1 303 ? 148.502 139.477 117.167 1.00 12620. ? 303 TYR A CG    1 
ATOM   2167  C  CD1   . TYR A 1 303 ? 149.508 138.995 116.345 1.00 12576. ? 303 TYR A CD1   1 
ATOM   2168  C  CD2   . TYR A 1 303 ? 148.866 140.198 118.293 1.00 12736. ? 303 TYR A CD2   1 
ATOM   2169  C  CE1   . TYR A 1 303 ? 150.834 139.219 116.636 1.00 12616. ? 303 TYR A CE1   1 
ATOM   2170  C  CE2   . TYR A 1 303 ? 150.191 140.427 118.592 1.00 12739. ? 303 TYR A CE2   1 
ATOM   2171  C  CZ    . TYR A 1 303 ? 151.171 139.935 117.760 1.00 12742. ? 303 TYR A CZ    1 
ATOM   2172  O  OH    . TYR A 1 303 ? 152.496 140.159 118.053 1.00 12745. ? 303 TYR A OH    1 
ATOM   2173  N  N     . HIS A 1 304 ? 144.136 140.086 115.794 1.00 12740. ? 304 HIS A N     1 
ATOM   2174  C  CA    . HIS A 1 304 ? 142.782 139.743 115.375 1.00 12746. ? 304 HIS A CA    1 
ATOM   2175  C  C     . HIS A 1 304 ? 142.531 140.167 113.934 1.00 12750. ? 304 HIS A C     1 
ATOM   2176  O  O     . HIS A 1 304 ? 141.937 139.416 113.149 1.00 12755. ? 304 HIS A O     1 
ATOM   2177  C  CB    . HIS A 1 304 ? 141.764 140.398 116.305 1.00 12760. ? 304 HIS A CB    1 
ATOM   2178  C  CG    . HIS A 1 304 ? 141.668 139.754 117.652 1.00 12742. ? 304 HIS A CG    1 
ATOM   2179  N  ND1   . HIS A 1 304 ? 140.469 139.580 118.307 1.00 12743. ? 304 HIS A ND1   1 
ATOM   2180  C  CD2   . HIS A 1 304 ? 142.620 139.249 118.470 1.00 12743. ? 304 HIS A CD2   1 
ATOM   2181  C  CE1   . HIS A 1 304 ? 140.686 138.993 119.470 1.00 12749. ? 304 HIS A CE1   1 
ATOM   2182  N  NE2   . HIS A 1 304 ? 141.983 138.781 119.593 1.00 12743. ? 304 HIS A NE2   1 
ATOM   2183  N  N     . LYS A 1 305 ? 142.979 141.367 113.566 1.00 12746. ? 305 LYS A N     1 
ATOM   2184  C  CA    . LYS A 1 305 ? 142.796 141.828 112.195 1.00 12738. ? 305 LYS A CA    1 
ATOM   2185  C  C     . LYS A 1 305 ? 143.616 140.997 111.217 1.00 12730. ? 305 LYS A C     1 
ATOM   2186  O  O     . LYS A 1 305 ? 143.166 140.724 110.099 1.00 12742. ? 305 LYS A O     1 
ATOM   2187  C  CB    . LYS A 1 305 ? 143.151 143.308 112.088 1.00 12748. ? 305 LYS A CB    1 
ATOM   2188  C  CG    . LYS A 1 305 ? 141.967 144.225 112.320 1.00 12746. ? 305 LYS A CG    1 
ATOM   2189  C  CD    . LYS A 1 305 ? 142.319 145.371 113.244 1.00 12746. ? 305 LYS A CD    1 
ATOM   2190  C  CE    . LYS A 1 305 ? 142.655 146.622 112.461 1.00 12743. ? 305 LYS A CE    1 
ATOM   2191  N  NZ    . LYS A 1 305 ? 142.892 147.779 113.365 1.00 12767. ? 305 LYS A NZ    1 
ATOM   2192  N  N     . MET A 1 306 ? 144.819 140.580 111.615 1.00 12734. ? 306 MET A N     1 
ATOM   2193  C  CA    . MET A 1 306 ? 145.605 139.695 110.760 1.00 12728. ? 306 MET A CA    1 
ATOM   2194  C  C     . MET A 1 306 ? 144.902 138.359 110.561 1.00 12726. ? 306 MET A C     1 
ATOM   2195  O  O     . MET A 1 306 ? 144.929 137.789 109.464 1.00 12743. ? 306 MET A O     1 
ATOM   2196  C  CB    . MET A 1 306 ? 146.998 139.489 111.350 1.00 12703. ? 306 MET A CB    1 
ATOM   2197  C  CG    . MET A 1 306 ? 147.952 140.636 111.078 1.00 12748. ? 306 MET A CG    1 
ATOM   2198  S  SD    . MET A 1 306 ? 149.680 140.169 111.261 1.00 12707. ? 306 MET A SD    1 
ATOM   2199  C  CE    . MET A 1 306 ? 149.874 140.288 113.032 1.00 12692. ? 306 MET A CE    1 
ATOM   2200  N  N     . LEU A 1 307 ? 144.272 137.839 111.613 1.00 12713. ? 307 LEU A N     1 
ATOM   2201  C  CA    . LEU A 1 307 ? 143.515 136.598 111.478 1.00 12735. ? 307 LEU A CA    1 
ATOM   2202  C  C     . LEU A 1 307 ? 142.324 136.773 110.547 1.00 12741. ? 307 LEU A C     1 
ATOM   2203  O  O     . LEU A 1 307 ? 142.020 135.883 109.745 1.00 12761. ? 307 LEU A O     1 
ATOM   2204  C  CB    . LEU A 1 307 ? 143.054 136.114 112.848 1.00 12742. ? 307 LEU A CB    1 
ATOM   2205  C  CG    . LEU A 1 307 ? 144.161 135.453 113.658 1.00 12671. ? 307 LEU A CG    1 
ATOM   2206  C  CD1   . LEU A 1 307 ? 143.806 135.449 115.123 1.00 12660. ? 307 LEU A CD1   1 
ATOM   2207  C  CD2   . LEU A 1 307 ? 144.389 134.049 113.149 1.00 12647. ? 307 LEU A CD2   1 
ATOM   2208  N  N     . VAL A 1 308 ? 141.629 137.907 110.648 1.00 12733. ? 308 VAL A N     1 
ATOM   2209  C  CA    . VAL A 1 308 ? 140.521 138.175 109.734 1.00 12729. ? 308 VAL A CA    1 
ATOM   2210  C  C     . VAL A 1 308 ? 141.029 138.266 108.300 1.00 12737. ? 308 VAL A C     1 
ATOM   2211  O  O     . VAL A 1 308 ? 140.359 137.828 107.358 1.00 12737. ? 308 VAL A O     1 
ATOM   2212  C  CB    . VAL A 1 308 ? 139.767 139.448 110.160 1.00 12732. ? 308 VAL A CB    1 
ATOM   2213  C  CG1   . VAL A 1 308 ? 138.717 139.813 109.133 1.00 12746. ? 308 VAL A CG1   1 
ATOM   2214  C  CG2   . VAL A 1 308 ? 139.120 139.243 111.514 1.00 12739. ? 308 VAL A CG2   1 
ATOM   2215  N  N     . VAL A 1 309 ? 142.222 138.834 108.113 1.00 12749. ? 309 VAL A N     1 
ATOM   2216  C  CA    . VAL A 1 309 ? 142.870 138.796 106.804 1.00 12734. ? 309 VAL A CA    1 
ATOM   2217  C  C     . VAL A 1 309 ? 143.086 137.354 106.367 1.00 12725. ? 309 VAL A C     1 
ATOM   2218  O  O     . VAL A 1 309 ? 142.917 137.011 105.191 1.00 12727. ? 309 VAL A O     1 
ATOM   2219  C  CB    . VAL A 1 309 ? 144.199 139.576 106.838 1.00 12738. ? 309 VAL A CB    1 
ATOM   2220  C  CG1   . VAL A 1 309 ? 145.022 139.283 105.598 1.00 12737. ? 309 VAL A CG1   1 
ATOM   2221  C  CG2   . VAL A 1 309 ? 143.945 141.058 106.959 1.00 12752. ? 309 VAL A CG2   1 
ATOM   2222  N  N     . GLY A 1 310 ? 143.456 136.486 107.310 1.00 12739. ? 310 GLY A N     1 
ATOM   2223  C  CA    . GLY A 1 310 ? 143.707 135.095 106.978 1.00 12748. ? 310 GLY A CA    1 
ATOM   2224  C  C     . GLY A 1 310 ? 142.499 134.378 106.410 1.00 12747. ? 310 GLY A C     1 
ATOM   2225  O  O     . GLY A 1 310 ? 142.639 133.510 105.546 1.00 12756. ? 310 GLY A O     1 
ATOM   2226  N  N     . GLY A 1 311 ? 141.305 134.719 106.882 1.00 12743. ? 311 GLY A N     1 
ATOM   2227  C  CA    . GLY A 1 311 ? 140.105 134.111 106.344 1.00 12737. ? 311 GLY A CA    1 
ATOM   2228  C  C     . GLY A 1 311 ? 139.117 133.642 107.389 1.00 12735. ? 311 GLY A C     1 
ATOM   2229  O  O     . GLY A 1 311 ? 138.148 132.949 107.065 1.00 12746. ? 311 GLY A O     1 
ATOM   2230  N  N     . ILE A 1 312 ? 139.348 134.005 108.644 1.00 12738. ? 312 ILE A N     1 
ATOM   2231  C  CA    . ILE A 1 312 ? 138.427 133.706 109.733 1.00 12737. ? 312 ILE A CA    1 
ATOM   2232  C  C     . ILE A 1 312 ? 137.559 134.939 109.936 1.00 12748. ? 312 ILE A C     1 
ATOM   2233  O  O     . ILE A 1 312 ? 138.026 135.965 110.441 1.00 12768. ? 312 ILE A O     1 
ATOM   2234  C  CB    . ILE A 1 312 ? 139.173 133.319 111.015 1.00 12728. ? 312 ILE A CB    1 
ATOM   2235  C  CG1   . ILE A 1 312 ? 140.421 132.508 110.668 1.00 12746. ? 312 ILE A CG1   1 
ATOM   2236  C  CG2   . ILE A 1 312 ? 138.267 132.521 111.930 1.00 12722. ? 312 ILE A CG2   1 
ATOM   2237  C  CD1   . ILE A 1 312 ? 141.140 131.947 111.868 1.00 12765. ? 312 ILE A CD1   1 
ATOM   2238  N  N     . ASP A 1 313 ? 136.290 134.839 109.540 1.00 12743. ? 313 ASP A N     1 
ATOM   2239  C  CA    . ASP A 1 313 ? 135.439 136.022 109.465 1.00 12739. ? 313 ASP A CA    1 
ATOM   2240  C  C     . ASP A 1 313 ? 135.114 136.578 110.845 1.00 12731. ? 313 ASP A C     1 
ATOM   2241  O  O     . ASP A 1 313 ? 135.120 137.797 111.043 1.00 12747. ? 313 ASP A O     1 
ATOM   2242  C  CB    . ASP A 1 313 ? 134.156 135.688 108.709 1.00 12729. ? 313 ASP A CB    1 
ATOM   2243  C  CG    . ASP A 1 313 ? 134.403 134.781 107.524 1.00 12743. ? 313 ASP A CG    1 
ATOM   2244  O  OD1   . ASP A 1 313 ? 134.793 135.290 106.452 1.00 12743. ? 313 ASP A OD1   1 
ATOM   2245  O  OD2   . ASP A 1 313 ? 134.213 133.556 107.666 1.00 12761. ? 313 ASP A OD2   1 
ATOM   2246  N  N     . ARG A 1 314 ? 134.821 135.709 111.807 1.00 12722. ? 314 ARG A N     1 
ATOM   2247  C  CA    . ARG A 1 314 ? 134.397 136.136 113.133 1.00 12725. ? 314 ARG A CA    1 
ATOM   2248  C  C     . ARG A 1 314 ? 135.308 135.505 114.172 1.00 12739. ? 314 ARG A C     1 
ATOM   2249  O  O     . ARG A 1 314 ? 135.379 134.277 114.273 1.00 12742. ? 314 ARG A O     1 
ATOM   2250  C  CB    . ARG A 1 314 ? 132.937 135.756 113.386 1.00 12741. ? 314 ARG A CB    1 
ATOM   2251  C  CG    . ARG A 1 314 ? 131.978 136.357 112.378 1.00 12735. ? 314 ARG A CG    1 
ATOM   2252  C  CD    . ARG A 1 314 ? 130.580 135.798 112.527 1.00 12719. ? 314 ARG A CD    1 
ATOM   2253  N  NE    . ARG A 1 314 ? 129.716 136.222 111.433 1.00 12589. ? 314 ARG A NE    1 
ATOM   2254  C  CZ    . ARG A 1 314 ? 128.410 136.006 111.384 1.00 12479. ? 314 ARG A CZ    1 
ATOM   2255  N  NH1   . ARG A 1 314 ? 127.778 135.372 112.356 1.00 12569. ? 314 ARG A NH1   1 
ATOM   2256  N  NH2   . ARG A 1 314 ? 127.721 136.436 110.332 1.00 12255. ? 314 ARG A NH2   1 
ATOM   2257  N  N     . VAL A 1 315 ? 135.999 136.345 114.943 1.00 12733. ? 315 VAL A N     1 
ATOM   2258  C  CA    . VAL A 1 315 ? 136.901 135.878 115.987 1.00 12728. ? 315 VAL A CA    1 
ATOM   2259  C  C     . VAL A 1 315 ? 136.618 136.659 117.260 1.00 12740. ? 315 VAL A C     1 
ATOM   2260  O  O     . VAL A 1 315 ? 136.076 137.763 117.229 1.00 12748. ? 315 VAL A O     1 
ATOM   2261  C  CB    . VAL A 1 315 ? 138.387 136.020 115.594 1.00 12729. ? 315 VAL A CB    1 
ATOM   2262  C  CG1   . VAL A 1 315 ? 138.744 135.040 114.495 1.00 12747. ? 315 VAL A CG1   1 
ATOM   2263  C  CG2   . VAL A 1 315 ? 138.690 137.443 115.167 1.00 12738. ? 315 VAL A CG2   1 
ATOM   2264  N  N     . TYR A 1 316 ? 136.990 136.068 118.393 1.00 12747. ? 316 TYR A N     1 
ATOM   2265  C  CA    . TYR A 1 316 ? 136.845 136.746 119.672 1.00 12737. ? 316 TYR A CA    1 
ATOM   2266  C  C     . TYR A 1 316 ? 137.857 136.191 120.660 1.00 12726. ? 316 TYR A C     1 
ATOM   2267  O  O     . TYR A 1 316 ? 138.390 135.093 120.486 1.00 12735. ? 316 TYR A O     1 
ATOM   2268  C  CB    . TYR A 1 316 ? 135.421 136.617 120.227 1.00 12744. ? 316 TYR A CB    1 
ATOM   2269  C  CG    . TYR A 1 316 ? 135.130 135.335 120.969 1.00 12736. ? 316 TYR A CG    1 
ATOM   2270  C  CD1   . TYR A 1 316 ? 134.817 134.173 120.285 1.00 12742. ? 316 TYR A CD1   1 
ATOM   2271  C  CD2   . TYR A 1 316 ? 135.140 135.294 122.355 1.00 12744. ? 316 TYR A CD2   1 
ATOM   2272  C  CE1   . TYR A 1 316 ? 134.538 133.007 120.956 1.00 12742. ? 316 TYR A CE1   1 
ATOM   2273  C  CE2   . TYR A 1 316 ? 134.863 134.131 123.034 1.00 12736. ? 316 TYR A CE2   1 
ATOM   2274  C  CZ    . TYR A 1 316 ? 134.564 132.991 122.329 1.00 12734. ? 316 TYR A CZ    1 
ATOM   2275  O  OH    . TYR A 1 316 ? 134.286 131.826 123.000 1.00 12767. ? 316 TYR A OH    1 
ATOM   2276  N  N     . GLU A 1 317 ? 138.115 136.974 121.703 1.00 12721. ? 317 GLU A N     1 
ATOM   2277  C  CA    . GLU A 1 317 ? 139.096 136.600 122.717 1.00 12728. ? 317 GLU A CA    1 
ATOM   2278  C  C     . GLU A 1 317 ? 138.804 137.376 123.988 1.00 12743. ? 317 GLU A C     1 
ATOM   2279  O  O     . GLU A 1 317 ? 138.680 138.604 123.948 1.00 12759. ? 317 GLU A O     1 
ATOM   2280  C  CB    . GLU A 1 317 ? 140.515 136.884 122.234 1.00 12744. ? 317 GLU A CB    1 
ATOM   2281  C  CG    . GLU A 1 317 ? 141.586 136.587 123.266 1.00 12756. ? 317 GLU A CG    1 
ATOM   2282  C  CD    . GLU A 1 317 ? 142.973 136.954 122.790 1.00 12755. ? 317 GLU A CD    1 
ATOM   2283  O  OE1   . GLU A 1 317 ? 143.103 137.420 121.641 1.00 12760. ? 317 GLU A OE1   1 
ATOM   2284  O  OE2   . GLU A 1 317 ? 143.935 136.776 123.565 1.00 12765. ? 317 GLU A OE2   1 
ATOM   2285  N  N     . ILE A 1 318 ? 138.690 136.668 125.106 1.00 12743. ? 318 ILE A N     1 
ATOM   2286  C  CA    . ILE A 1 318 ? 138.596 137.283 126.424 1.00 12741. ? 318 ILE A CA    1 
ATOM   2287  C  C     . ILE A 1 318 ? 139.920 137.049 127.131 1.00 12751. ? 318 ILE A C     1 
ATOM   2288  O  O     . ILE A 1 318 ? 140.332 135.900 127.330 1.00 12757. ? 318 ILE A O     1 
ATOM   2289  C  CB    . ILE A 1 318 ? 137.424 136.711 127.235 1.00 12733. ? 318 ILE A CB    1 
ATOM   2290  C  CG1   . ILE A 1 318 ? 136.217 136.470 126.332 1.00 12742. ? 318 ILE A CG1   1 
ATOM   2291  C  CG2   . ILE A 1 318 ? 137.063 137.643 128.378 1.00 12755. ? 318 ILE A CG2   1 
ATOM   2292  C  CD1   . ILE A 1 318 ? 134.987 136.024 127.076 1.00 12749. ? 318 ILE A CD1   1 
ATOM   2293  N  N     . GLY A 1 319 ? 140.592 138.131 127.509 1.00 12751. ? 319 GLY A N     1 
ATOM   2294  C  CA    . GLY A 1 319 ? 141.914 137.983 128.083 1.00 12739. ? 319 GLY A CA    1 
ATOM   2295  C  C     . GLY A 1 319 ? 142.391 139.253 128.748 1.00 12733. ? 319 GLY A C     1 
ATOM   2296  O  O     . GLY A 1 319 ? 141.698 140.272 128.772 1.00 12757. ? 319 GLY A O     1 
ATOM   2297  N  N     . ARG A 1 320 ? 143.606 139.176 129.280 1.00 12723. ? 320 ARG A N     1 
ATOM   2298  C  CA    . ARG A 1 320 ? 144.186 140.259 130.056 1.00 12733. ? 320 ARG A CA    1 
ATOM   2299  C  C     . ARG A 1 320 ? 144.947 141.236 129.172 1.00 12738. ? 320 ARG A C     1 
ATOM   2300  O  O     . ARG A 1 320 ? 145.625 140.851 128.217 1.00 12750. ? 320 ARG A O     1 
ATOM   2301  C  CB    . ARG A 1 320 ? 145.125 139.710 131.128 1.00 12746. ? 320 ARG A CB    1 
ATOM   2302  C  CG    . ARG A 1 320 ? 144.525 138.613 131.974 1.00 12744. ? 320 ARG A CG    1 
ATOM   2303  C  CD    . ARG A 1 320 ? 143.671 139.176 133.090 1.00 12746. ? 320 ARG A CD    1 
ATOM   2304  N  NE    . ARG A 1 320 ? 143.397 138.170 134.107 1.00 12748. ? 320 ARG A NE    1 
ATOM   2305  C  CZ    . ARG A 1 320 ? 144.277 137.757 135.007 1.00 12746. ? 320 ARG A CZ    1 
ATOM   2306  N  NH1   . ARG A 1 320 ? 145.497 138.264 135.065 1.00 12761. ? 320 ARG A NH1   1 
ATOM   2307  N  NH2   . ARG A 1 320 ? 143.924 136.812 135.873 1.00 12745. ? 320 ARG A NH2   1 
ATOM   2308  N  N     . GLN A 1 321 ? 144.821 142.513 129.510 1.00 12727. ? 321 GLN A N     1 
ATOM   2309  C  CA    . GLN A 1 321 ? 145.586 143.594 128.918 1.00 12733. ? 321 GLN A CA    1 
ATOM   2310  C  C     . GLN A 1 321 ? 146.363 144.285 130.027 1.00 12745. ? 321 GLN A C     1 
ATOM   2311  O  O     . GLN A 1 321 ? 145.853 144.454 131.142 1.00 12766. ? 321 GLN A O     1 
ATOM   2312  C  CB    . GLN A 1 321 ? 144.679 144.598 128.205 1.00 12747. ? 321 GLN A CB    1 
ATOM   2313  C  CG    . GLN A 1 321 ? 143.492 143.978 127.492 1.00 12758. ? 321 GLN A CG    1 
ATOM   2314  C  CD    . GLN A 1 321 ? 143.902 143.030 126.387 1.00 12749. ? 321 GLN A CD    1 
ATOM   2315  O  OE1   . GLN A 1 321 ? 144.852 143.291 125.652 1.00 12739. ? 321 GLN A OE1   1 
ATOM   2316  N  NE2   . GLN A 1 321 ? 143.183 141.922 126.260 1.00 12759. ? 321 GLN A NE2   1 
ATOM   2317  N  N     . PHE A 1 322 ? 147.599 144.674 129.718 1.00 12745. ? 322 PHE A N     1 
ATOM   2318  C  CA    . PHE A 1 322 ? 148.533 145.230 130.691 1.00 12738. ? 322 PHE A CA    1 
ATOM   2319  C  C     . PHE A 1 322 ? 148.938 146.627 130.244 1.00 12738. ? 322 PHE A C     1 
ATOM   2320  O  O     . PHE A 1 322 ? 149.607 146.784 129.217 1.00 12741. ? 322 PHE A O     1 
ATOM   2321  C  CB    . PHE A 1 322 ? 149.762 144.334 130.838 1.00 12743. ? 322 PHE A CB    1 
ATOM   2322  C  CG    . PHE A 1 322 ? 149.435 142.887 131.051 1.00 12736. ? 322 PHE A CG    1 
ATOM   2323  C  CD1   . PHE A 1 322 ? 149.258 142.385 132.326 1.00 12742. ? 322 PHE A CD1   1 
ATOM   2324  C  CD2   . PHE A 1 322 ? 149.299 142.028 129.975 1.00 12749. ? 322 PHE A CD2   1 
ATOM   2325  C  CE1   . PHE A 1 322 ? 148.957 141.057 132.524 1.00 12746. ? 322 PHE A CE1   1 
ATOM   2326  C  CE2   . PHE A 1 322 ? 148.998 140.700 130.168 1.00 12748. ? 322 PHE A CE2   1 
ATOM   2327  C  CZ    . PHE A 1 322 ? 148.826 140.214 131.443 1.00 12747. ? 322 PHE A CZ    1 
ATOM   2328  N  N     . ARG A 1 323 ? 148.519 147.629 131.028 1.00 12735. ? 323 ARG A N     1 
ATOM   2329  C  CA    . ARG A 1 323 ? 148.879 149.043 130.740 1.00 12731. ? 323 ARG A CA    1 
ATOM   2330  C  C     . ARG A 1 323 ? 149.555 149.622 131.991 1.00 12738. ? 323 ARG A C     1 
ATOM   2331  O  O     . ARG A 1 323 ? 148.909 149.628 133.059 1.00 12755. ? 323 ARG A O     1 
ATOM   2332  C  CB    . ARG A 1 323 ? 147.636 149.833 130.315 1.00 12728. ? 323 ARG A CB    1 
ATOM   2333  C  CG    . ARG A 1 323 ? 147.076 149.315 128.999 1.00 12736. ? 323 ARG A CG    1 
ATOM   2334  C  CD    . ARG A 1 323 ? 145.716 149.897 128.666 1.00 12720. ? 323 ARG A CD    1 
ATOM   2335  N  NE    . ARG A 1 323 ? 145.133 149.221 127.503 1.00 12750. ? 323 ARG A NE    1 
ATOM   2336  C  CZ    . ARG A 1 323 ? 143.928 149.478 127.017 1.00 12719. ? 323 ARG A CZ    1 
ATOM   2337  N  NH1   . ARG A 1 323 ? 143.143 150.345 127.630 1.00 12621. ? 323 ARG A NH1   1 
ATOM   2338  N  NH2   . ARG A 1 323 ? 143.508 148.861 125.927 1.00 12689. ? 323 ARG A NH2   1 
ATOM   2339  N  N     . ASN A 1 324 ? 150.794 150.094 131.862 1.00 12739. ? 324 ASN A N     1 
ATOM   2340  C  CA    . ASN A 1 324 ? 151.571 150.594 132.996 1.00 12736. ? 324 ASN A CA    1 
ATOM   2341  C  C     . ASN A 1 324 ? 151.156 152.032 133.311 1.00 12740. ? 324 ASN A C     1 
ATOM   2342  O  O     . ASN A 1 324 ? 151.915 152.990 133.155 1.00 12751. ? 324 ASN A O     1 
ATOM   2343  C  CB    . ASN A 1 324 ? 153.060 150.497 132.701 1.00 12744. ? 324 ASN A CB    1 
ATOM   2344  C  CG    . ASN A 1 324 ? 153.856 150.002 133.885 1.00 12739. ? 324 ASN A CG    1 
ATOM   2345  O  OD1   . ASN A 1 324 ? 153.346 149.923 135.000 1.00 12750. ? 324 ASN A OD1   1 
ATOM   2346  N  ND2   . ASN A 1 324 ? 155.118 149.670 133.652 1.00 12740. ? 324 ASN A ND2   1 
ATOM   2347  N  N     . GLU A 1 325 ? 149.915 152.170 133.775 1.00 12937. ? 325 GLU A N     1 
ATOM   2348  C  CA    . GLU A 1 325 ? 149.356 153.486 134.062 1.00 12934. ? 325 GLU A CA    1 
ATOM   2349  C  C     . GLU A 1 325 ? 148.807 153.562 135.481 1.00 12941. ? 325 GLU A C     1 
ATOM   2350  O  O     . GLU A 1 325 ? 149.030 152.656 136.289 1.00 12962. ? 325 GLU A O     1 
ATOM   2351  C  CB    . GLU A 1 325 ? 148.263 153.834 133.051 1.00 12874. ? 325 GLU A CB    1 
ATOM   2352  C  CG    . GLU A 1 325 ? 148.704 153.734 131.602 1.00 12871. ? 325 GLU A CG    1 
ATOM   2353  C  CD    . GLU A 1 325 ? 149.556 154.908 131.169 1.00 12828. ? 325 GLU A CD    1 
ATOM   2354  O  OE1   . GLU A 1 325 ? 149.580 155.927 131.888 1.00 12783. ? 325 GLU A OE1   1 
ATOM   2355  O  OE2   . GLU A 1 325 ? 150.204 154.813 130.107 1.00 12871. ? 325 GLU A OE2   1 
ATOM   2356  N  N     . GLY A 1 326 ? 148.089 154.638 135.788 1.00 12769. ? 326 GLY A N     1 
ATOM   2357  C  CA    . GLY A 1 326 ? 147.621 154.872 137.138 1.00 12775. ? 326 GLY A CA    1 
ATOM   2358  C  C     . GLY A 1 326 ? 146.520 153.919 137.564 1.00 12826. ? 326 GLY A C     1 
ATOM   2359  O  O     . GLY A 1 326 ? 145.924 153.192 136.769 1.00 12838. ? 326 GLY A O     1 
ATOM   2360  N  N     . ILE A 1 327 ? 146.252 153.929 138.868 1.00 12778. ? 327 ILE A N     1 
ATOM   2361  C  CA    . ILE A 1 327 ? 145.233 153.084 139.482 1.00 12791. ? 327 ILE A CA    1 
ATOM   2362  C  C     . ILE A 1 327 ? 144.234 153.983 140.194 1.00 12784. ? 327 ILE A C     1 
ATOM   2363  O  O     . ILE A 1 327 ? 144.622 154.832 141.006 1.00 12770. ? 327 ILE A O     1 
ATOM   2364  C  CB    . ILE A 1 327 ? 145.838 152.072 140.467 1.00 12782. ? 327 ILE A CB    1 
ATOM   2365  C  CG1   . ILE A 1 327 ? 147.119 151.461 139.903 1.00 12779. ? 327 ILE A CG1   1 
ATOM   2366  C  CG2   . ILE A 1 327 ? 144.831 150.986 140.796 1.00 12793. ? 327 ILE A CG2   1 
ATOM   2367  C  CD1   . ILE A 1 327 ? 147.815 150.527 140.863 1.00 12784. ? 327 ILE A CD1   1 
ATOM   2368  N  N     . ASP A 1 328 ? 142.951 153.797 139.892 1.00 12959. ? 328 ASP A N     1 
ATOM   2369  C  CA    . ASP A 1 328 ? 141.872 154.466 140.600 1.00 12954. ? 328 ASP A CA    1 
ATOM   2370  C  C     . ASP A 1 328 ? 140.678 153.522 140.659 1.00 12954. ? 328 ASP A C     1 
ATOM   2371  O  O     . ASP A 1 328 ? 140.797 152.321 140.403 1.00 12962. ? 328 ASP A O     1 
ATOM   2372  C  CB    . ASP A 1 328 ? 141.510 155.805 139.947 1.00 12966. ? 328 ASP A CB    1 
ATOM   2373  C  CG    . ASP A 1 328 ? 141.306 155.692 138.456 1.00 12974. ? 328 ASP A CG    1 
ATOM   2374  O  OD1   . ASP A 1 328 ? 142.294 155.431 137.741 1.00 12966. ? 328 ASP A OD1   1 
ATOM   2375  O  OD2   . ASP A 1 328 ? 140.158 155.869 137.996 1.00 12981. ? 328 ASP A OD2   1 
ATOM   2376  N  N     . LEU A 1 329 ? 139.515 154.079 141.008 1.00 12732. ? 329 LEU A N     1 
ATOM   2377  C  CA    . LEU A 1 329 ? 138.338 153.254 141.260 1.00 12744. ? 329 LEU A CA    1 
ATOM   2378  C  C     . LEU A 1 329 ? 137.915 152.459 140.032 1.00 12745. ? 329 LEU A C     1 
ATOM   2379  O  O     . LEU A 1 329 ? 137.351 151.368 140.169 1.00 12754. ? 329 LEU A O     1 
ATOM   2380  C  CB    . LEU A 1 329 ? 137.181 154.129 141.742 1.00 12718. ? 329 LEU A CB    1 
ATOM   2381  C  CG    . LEU A 1 329 ? 137.366 154.813 143.095 1.00 12606. ? 329 LEU A CG    1 
ATOM   2382  C  CD1   . LEU A 1 329 ? 136.087 155.505 143.523 1.00 12611. ? 329 LEU A CD1   1 
ATOM   2383  C  CD2   . LEU A 1 329 ? 137.799 153.805 144.138 1.00 12633. ? 329 LEU A CD2   1 
ATOM   2384  N  N     . THR A 1 330 ? 138.208 152.972 138.829 1.00 12746. ? 330 THR A N     1 
ATOM   2385  C  CA    . THR A 1 330 ? 137.724 152.298 137.596 1.00 12743. ? 330 THR A CA    1 
ATOM   2386  C  C     . THR A 1 330 ? 138.868 151.951 136.659 1.00 12748. ? 330 THR A C     1 
ATOM   2387  O  O     . THR A 1 330 ? 138.578 151.606 135.492 1.00 12752. ? 330 THR A O     1 
ATOM   2388  C  CB    . THR A 1 330 ? 136.699 153.193 136.900 1.00 12754. ? 330 THR A CB    1 
ATOM   2389  O  OG1   . THR A 1 330 ? 137.398 154.398 136.608 1.00 12761. ? 330 THR A OG1   1 
ATOM   2390  C  CG2   . THR A 1 330 ? 135.491 153.485 137.771 1.00 12761. ? 330 THR A CG2   1 
ATOM   2391  N  N     . HIS A 1 331 ? 140.118 152.027 137.124 1.00 12752. ? 331 HIS A N     1 
ATOM   2392  C  CA    . HIS A 1 331 ? 141.258 151.651 136.301 1.00 12744. ? 331 HIS A CA    1 
ATOM   2393  C  C     . HIS A 1 331 ? 142.155 150.693 137.066 1.00 12733. ? 331 HIS A C     1 
ATOM   2394  O  O     . HIS A 1 331 ? 142.381 150.871 138.266 1.00 12730. ? 331 HIS A O     1 
ATOM   2395  C  CB    . HIS A 1 331 ? 142.059 152.880 135.866 1.00 12745. ? 331 HIS A CB    1 
ATOM   2396  C  CG    . HIS A 1 331 ? 141.351 153.743 134.871 1.00 12695. ? 331 HIS A CG    1 
ATOM   2397  N  ND1   . HIS A 1 331 ? 140.664 154.883 135.229 1.00 12690. ? 331 HIS A ND1   1 
ATOM   2398  C  CD2   . HIS A 1 331 ? 141.225 153.634 133.528 1.00 12690. ? 331 HIS A CD2   1 
ATOM   2399  C  CE1   . HIS A 1 331 ? 140.146 155.439 134.149 1.00 12666. ? 331 HIS A CE1   1 
ATOM   2400  N  NE2   . HIS A 1 331 ? 140.470 154.700 133.104 1.00 12665. ? 331 HIS A NE2   1 
ATOM   2401  N  N     . ASN A 1 332 ? 142.656 149.679 136.367 1.00 12740. ? 332 ASN A N     1 
ATOM   2402  C  CA    . ASN A 1 332 ? 143.641 148.749 136.887 1.00 12747. ? 332 ASN A CA    1 
ATOM   2403  C  C     . ASN A 1 332 ? 144.720 148.534 135.835 1.00 12739. ? 332 ASN A C     1 
ATOM   2404  O  O     . ASN A 1 332 ? 144.413 148.480 134.638 1.00 12742. ? 332 ASN A O     1 
ATOM   2405  C  CB    . ASN A 1 332 ? 142.995 147.407 137.256 1.00 12761. ? 332 ASN A CB    1 
ATOM   2406  C  CG    . ASN A 1 332 ? 143.839 146.597 138.215 1.00 12758. ? 332 ASN A CG    1 
ATOM   2407  O  OD1   . ASN A 1 332 ? 144.170 147.056 139.307 1.00 12748. ? 332 ASN A OD1   1 
ATOM   2408  N  ND2   . ASN A 1 332 ? 144.190 145.383 137.814 1.00 12760. ? 332 ASN A ND2   1 
ATOM   2409  N  N     . PRO A 1 333 ? 145.989 148.435 136.240 1.00 12727. ? 333 PRO A N     1 
ATOM   2410  C  CA    . PRO A 1 333 ? 147.051 148.210 135.246 1.00 12736. ? 333 PRO A CA    1 
ATOM   2411  C  C     . PRO A 1 333 ? 146.872 146.939 134.435 1.00 12744. ? 333 PRO A C     1 
ATOM   2412  O  O     . PRO A 1 333 ? 147.178 146.927 133.237 1.00 12765. ? 333 PRO A O     1 
ATOM   2413  C  CB    . PRO A 1 333 ? 148.314 148.171 136.113 1.00 12749. ? 333 PRO A CB    1 
ATOM   2414  C  CG    . PRO A 1 333 ? 147.974 149.072 137.249 1.00 12748. ? 333 PRO A CG    1 
ATOM   2415  C  CD    . PRO A 1 333 ? 146.552 148.707 137.572 1.00 12741. ? 333 PRO A CD    1 
ATOM   2416  N  N     . GLU A 1 334 ? 146.408 145.877 135.052 1.00 12739. ? 334 GLU A N     1 
ATOM   2417  C  CA    . GLU A 1 334 ? 146.096 144.625 134.312 1.00 12741. ? 334 GLU A CA    1 
ATOM   2418  C  C     . GLU A 1 334 ? 144.578 144.422 134.427 1.00 12738. ? 334 GLU A C     1 
ATOM   2419  O  O     . GLU A 1 334 ? 144.050 144.573 135.546 1.00 12744. ? 334 GLU A O     1 
ATOM   2420  C  CB    . GLU A 1 334 ? 146.909 143.433 134.820 1.00 12744. ? 334 GLU A CB    1 
ATOM   2421  C  CG    . GLU A 1 334 ? 146.794 143.192 136.323 1.00 12747. ? 334 GLU A CG    1 
ATOM   2422  C  CD    . GLU A 1 334 ? 147.537 141.953 136.791 1.00 12744. ? 334 GLU A CD    1 
ATOM   2423  O  OE1   . GLU A 1 334 ? 148.144 141.270 135.939 1.00 12757. ? 334 GLU A OE1   1 
ATOM   2424  O  OE2   . GLU A 1 334 ? 147.512 141.670 138.007 1.00 12745. ? 334 GLU A OE2   1 
ATOM   2425  N  N     . PHE A 1 335 ? 143.900 144.100 133.351 1.00 12744. ? 335 PHE A N     1 
ATOM   2426  C  CA    . PHE A 1 335 ? 142.445 144.024 133.354 1.00 12745. ? 335 PHE A CA    1 
ATOM   2427  C  C     . PHE A 1 335 ? 141.963 143.086 132.260 1.00 12742. ? 335 PHE A C     1 
ATOM   2428  O  O     . PHE A 1 335 ? 142.597 142.954 131.215 1.00 12756. ? 335 PHE A O     1 
ATOM   2429  C  CB    . PHE A 1 335 ? 141.813 145.409 133.170 1.00 12756. ? 335 PHE A CB    1 
ATOM   2430  C  CG    . PHE A 1 335 ? 142.310 146.147 131.961 1.00 12749. ? 335 PHE A CG    1 
ATOM   2431  C  CD1   . PHE A 1 335 ? 143.476 146.888 132.014 1.00 12753. ? 335 PHE A CD1   1 
ATOM   2432  C  CD2   . PHE A 1 335 ? 141.608 146.104 130.772 1.00 12739. ? 335 PHE A CD2   1 
ATOM   2433  C  CE1   . PHE A 1 335 ? 143.931 147.565 130.906 1.00 12756. ? 335 PHE A CE1   1 
ATOM   2434  C  CE2   . PHE A 1 335 ? 142.060 146.780 129.661 1.00 12734. ? 335 PHE A CE2   1 
ATOM   2435  C  CZ    . PHE A 1 335 ? 143.222 147.512 129.729 1.00 12749. ? 335 PHE A CZ    1 
ATOM   2436  N  N     . THR A 1 336 ? 140.818 142.458 132.498 1.00 12721. ? 336 THR A N     1 
ATOM   2437  C  CA    . THR A 1 336 ? 140.228 141.522 131.551 1.00 12717. ? 336 THR A CA    1 
ATOM   2438  C  C     . THR A 1 336 ? 139.279 142.256 130.614 1.00 12732. ? 336 THR A C     1 
ATOM   2439  O  O     . THR A 1 336 ? 138.422 143.021 131.065 1.00 12750. ? 336 THR A O     1 
ATOM   2440  C  CB    . THR A 1 336 ? 139.476 140.407 132.276 1.00 12729. ? 336 THR A CB    1 
ATOM   2441  O  OG1   . THR A 1 336 ? 140.336 139.800 133.247 1.00 12746. ? 336 THR A OG1   1 
ATOM   2442  C  CG2   . THR A 1 336 ? 139.012 139.353 131.289 1.00 12741. ? 336 THR A CG2   1 
ATOM   2443  N  N     . THR A 1 337 ? 139.438 142.022 129.314 1.00 12746. ? 337 THR A N     1 
ATOM   2444  C  CA    . THR A 1 337 ? 138.531 142.553 128.309 1.00 12740. ? 337 THR A CA    1 
ATOM   2445  C  C     . THR A 1 337 ? 138.164 141.461 127.320 1.00 12742. ? 337 THR A C     1 
ATOM   2446  O  O     . THR A 1 337 ? 138.922 140.509 127.108 1.00 12761. ? 337 THR A O     1 
ATOM   2447  C  CB    . THR A 1 337 ? 139.132 143.731 127.535 1.00 12740. ? 337 THR A CB    1 
ATOM   2448  O  OG1   . THR A 1 337 ? 140.373 143.334 126.941 1.00 12750. ? 337 THR A OG1   1 
ATOM   2449  C  CG2   . THR A 1 337 ? 139.357 144.916 128.446 1.00 12759. ? 337 THR A CG2   1 
ATOM   2450  N  N     . CYS A 1 338 ? 136.995 141.617 126.710 1.00 12737. ? 338 CYS A N     1 
ATOM   2451  C  CA    . CYS A 1 338 ? 136.548 140.746 125.631 1.00 12739. ? 338 CYS A CA    1 
ATOM   2452  C  C     . CYS A 1 338 ? 136.533 141.549 124.340 1.00 12743. ? 338 CYS A C     1 
ATOM   2453  O  O     . CYS A 1 338 ? 135.843 142.567 124.251 1.00 12756. ? 338 CYS A O     1 
ATOM   2454  C  CB    . CYS A 1 338 ? 135.163 140.171 125.919 1.00 12743. ? 338 CYS A CB    1 
ATOM   2455  S  SG    . CYS A 1 338 ? 134.481 139.206 124.554 1.00 12757. ? 338 CYS A SG    1 
ATOM   2456  N  N     . GLU A 1 339 ? 137.286 141.093 123.345 1.00 12741. ? 339 GLU A N     1 
ATOM   2457  C  CA    . GLU A 1 339 ? 137.373 141.780 122.065 1.00 12734. ? 339 GLU A CA    1 
ATOM   2458  C  C     . GLU A 1 339 ? 137.024 140.809 120.951 1.00 12739. ? 339 GLU A C     1 
ATOM   2459  O  O     . GLU A 1 339 ? 137.565 139.701 120.903 1.00 12749. ? 339 GLU A O     1 
ATOM   2460  C  CB    . GLU A 1 339 ? 138.772 142.359 121.843 1.00 12737. ? 339 GLU A CB    1 
ATOM   2461  C  CG    . GLU A 1 339 ? 138.973 143.725 122.471 1.00 12748. ? 339 GLU A CG    1 
ATOM   2462  C  CD    . GLU A 1 339 ? 140.407 144.200 122.393 1.00 12743. ? 339 GLU A CD    1 
ATOM   2463  O  OE1   . GLU A 1 339 ? 140.963 144.233 121.276 1.00 12747. ? 339 GLU A OE1   1 
ATOM   2464  O  OE2   . GLU A 1 339 ? 140.977 144.546 123.449 1.00 12752. ? 339 GLU A OE2   1 
ATOM   2465  N  N     . PHE A 1 340 ? 136.129 141.222 120.057 1.00 12745. ? 340 PHE A N     1 
ATOM   2466  C  CA    . PHE A 1 340 ? 135.790 140.414 118.898 1.00 12742. ? 340 PHE A CA    1 
ATOM   2467  C  C     . PHE A 1 340 ? 135.884 141.250 117.630 1.00 12744. ? 340 PHE A C     1 
ATOM   2468  O  O     . PHE A 1 340 ? 135.841 142.483 117.657 1.00 12760. ? 340 PHE A O     1 
ATOM   2469  C  CB    . PHE A 1 340 ? 134.397 139.741 119.035 1.00 12747. ? 340 PHE A CB    1 
ATOM   2470  C  CG    . PHE A 1 340 ? 133.208 140.630 118.735 1.00 12738. ? 340 PHE A CG    1 
ATOM   2471  C  CD1   . PHE A 1 340 ? 132.909 141.038 117.444 1.00 12742. ? 340 PHE A CD1   1 
ATOM   2472  C  CD2   . PHE A 1 340 ? 132.335 140.981 119.744 1.00 12747. ? 340 PHE A CD2   1 
ATOM   2473  C  CE1   . PHE A 1 340 ? 131.810 141.824 117.183 1.00 12749. ? 340 PHE A CE1   1 
ATOM   2474  C  CE2   . PHE A 1 340 ? 131.229 141.761 119.483 1.00 12747. ? 340 PHE A CE2   1 
ATOM   2475  C  CZ    . PHE A 1 340 ? 130.969 142.184 118.204 1.00 12745. ? 340 PHE A CZ    1 
ATOM   2476  N  N     . TYR A 1 341 ? 136.034 140.544 116.515 1.00 12738. ? 341 TYR A N     1 
ATOM   2477  C  CA    . TYR A 1 341 ? 136.072 141.134 115.186 1.00 12733. ? 341 TYR A CA    1 
ATOM   2478  C  C     . TYR A 1 341 ? 135.141 140.348 114.281 1.00 12736. ? 341 TYR A C     1 
ATOM   2479  O  O     . TYR A 1 341 ? 135.141 139.111 114.306 1.00 12755. ? 341 TYR A O     1 
ATOM   2480  C  CB    . TYR A 1 341 ? 137.491 141.143 114.622 1.00 12736. ? 341 TYR A CB    1 
ATOM   2481  C  CG    . TYR A 1 341 ? 138.322 142.285 115.144 1.00 12726. ? 341 TYR A CG    1 
ATOM   2482  C  CD1   . TYR A 1 341 ? 138.804 142.279 116.442 1.00 12735. ? 341 TYR A CD1   1 
ATOM   2483  C  CD2   . TYR A 1 341 ? 138.612 143.375 114.344 1.00 12734. ? 341 TYR A CD2   1 
ATOM   2484  C  CE1   . TYR A 1 341 ? 139.555 143.320 116.925 1.00 12732. ? 341 TYR A CE1   1 
ATOM   2485  C  CE2   . TYR A 1 341 ? 139.361 144.421 114.819 1.00 12740. ? 341 TYR A CE2   1 
ATOM   2486  C  CZ    . TYR A 1 341 ? 139.831 144.389 116.109 1.00 12729. ? 341 TYR A CZ    1 
ATOM   2487  O  OH    . TYR A 1 341 ? 140.583 145.435 116.582 1.00 12753. ? 341 TYR A OH    1 
ATOM   2488  N  N     . MET A 1 342 ? 134.353 141.071 113.486 1.00 12732. ? 342 MET A N     1 
ATOM   2489  C  CA    . MET A 1 342 ? 133.316 140.489 112.645 1.00 12734. ? 342 MET A CA    1 
ATOM   2490  C  C     . MET A 1 342 ? 133.466 141.045 111.239 1.00 12741. ? 342 MET A C     1 
ATOM   2491  O  O     . MET A 1 342 ? 133.338 142.255 111.035 1.00 12760. ? 342 MET A O     1 
ATOM   2492  C  CB    . MET A 1 342 ? 131.929 140.812 113.205 1.00 12737. ? 342 MET A CB    1 
ATOM   2493  C  CG    . MET A 1 342 ? 130.785 140.072 112.552 1.00 12712. ? 342 MET A CG    1 
ATOM   2494  S  SD    . MET A 1 342 ? 129.239 140.386 113.420 1.00 12668. ? 342 MET A SD    1 
ATOM   2495  C  CE    . MET A 1 342 ? 128.516 138.753 113.451 1.00 12679. ? 342 MET A CE    1 
ATOM   2496  N  N     . ALA A 1 343 ? 133.744 140.170 110.279 1.00 12738. ? 343 ALA A N     1 
ATOM   2497  C  CA    . ALA A 1 343 ? 133.904 140.596 108.900 1.00 12733. ? 343 ALA A CA    1 
ATOM   2498  C  C     . ALA A 1 343 ? 132.550 140.903 108.268 1.00 12742. ? 343 ALA A C     1 
ATOM   2499  O  O     . ALA A 1 343 ? 131.509 140.390 108.685 1.00 12689. ? 343 ALA A O     1 
ATOM   2500  C  CB    . ALA A 1 343 ? 134.632 139.529 108.086 1.00 12737. ? 343 ALA A CB    1 
ATOM   2501  N  N     . TYR A 1 344 ? 132.582 141.755 107.241 1.00 12752. ? 344 TYR A N     1 
ATOM   2502  C  CA    . TYR A 1 344 ? 131.385 142.162 106.502 1.00 12742. ? 344 TYR A CA    1 
ATOM   2503  C  C     . TYR A 1 344 ? 130.342 142.779 107.428 1.00 12709. ? 344 TYR A C     1 
ATOM   2504  O  O     . TYR A 1 344 ? 129.142 142.537 107.295 1.00 12707. ? 344 TYR A O     1 
ATOM   2505  C  CB    . TYR A 1 344 ? 130.801 140.990 105.716 1.00 12701. ? 344 TYR A CB    1 
ATOM   2506  C  CG    . TYR A 1 344 ? 131.849 140.246 104.931 1.00 12692. ? 344 TYR A CG    1 
ATOM   2507  C  CD1   . TYR A 1 344 ? 132.554 140.872 103.917 1.00 12728. ? 344 TYR A CD1   1 
ATOM   2508  C  CD2   . TYR A 1 344 ? 132.149 138.924 105.217 1.00 12676. ? 344 TYR A CD2   1 
ATOM   2509  C  CE1   . TYR A 1 344 ? 133.519 140.202 103.203 1.00 12735. ? 344 TYR A CE1   1 
ATOM   2510  C  CE2   . TYR A 1 344 ? 133.112 138.246 104.509 1.00 12721. ? 344 TYR A CE2   1 
ATOM   2511  C  CZ    . TYR A 1 344 ? 133.795 138.889 103.503 1.00 12733. ? 344 TYR A CZ    1 
ATOM   2512  O  OH    . TYR A 1 344 ? 134.758 138.215 102.791 1.00 12746. ? 344 TYR A OH    1 
ATOM   2513  N  N     . ALA A 1 345 ? 130.810 143.588 108.374 1.00 12710. ? 345 ALA A N     1 
ATOM   2514  C  CA    . ALA A 1 345 ? 129.944 144.298 109.299 1.00 12703. ? 345 ALA A CA    1 
ATOM   2515  C  C     . ALA A 1 345 ? 130.470 145.712 109.483 1.00 12742. ? 345 ALA A C     1 
ATOM   2516  O  O     . ALA A 1 345 ? 131.648 145.994 109.253 1.00 12752. ? 345 ALA A O     1 
ATOM   2517  C  CB    . ALA A 1 345 ? 129.858 143.587 110.653 1.00 12686. ? 345 ALA A CB    1 
ATOM   2518  N  N     . ASP A 1 346 ? 129.578 146.604 109.888 1.00 12739. ? 346 ASP A N     1 
ATOM   2519  C  CA    . ASP A 1 346 ? 129.941 147.956 110.280 1.00 12731. ? 346 ASP A CA    1 
ATOM   2520  C  C     . ASP A 1 346 ? 129.474 148.187 111.715 1.00 12739. ? 346 ASP A C     1 
ATOM   2521  O  O     . ASP A 1 346 ? 128.860 147.317 112.335 1.00 12771. ? 346 ASP A O     1 
ATOM   2522  C  CB    . ASP A 1 346 ? 129.354 148.981 109.309 1.00 12741. ? 346 ASP A CB    1 
ATOM   2523  C  CG    . ASP A 1 346 ? 127.854 148.868 109.181 1.00 12751. ? 346 ASP A CG    1 
ATOM   2524  O  OD1   . ASP A 1 346 ? 127.291 147.852 109.635 1.00 12760. ? 346 ASP A OD1   1 
ATOM   2525  O  OD2   . ASP A 1 346 ? 127.234 149.799 108.626 1.00 12750. ? 346 ASP A OD2   1 
ATOM   2526  N  N     . TYR A 1 347 ? 129.767 149.372 112.244 1.00 12736. ? 347 TYR A N     1 
ATOM   2527  C  CA    . TYR A 1 347 ? 129.413 149.668 113.625 1.00 12736. ? 347 TYR A CA    1 
ATOM   2528  C  C     . TYR A 1 347 ? 127.910 149.763 113.847 1.00 12740. ? 347 TYR A C     1 
ATOM   2529  O  O     . TYR A 1 347 ? 127.468 149.683 114.996 1.00 12770. ? 347 TYR A O     1 
ATOM   2530  C  CB    . TYR A 1 347 ? 130.092 150.962 114.084 1.00 12743. ? 347 TYR A CB    1 
ATOM   2531  C  CG    . TYR A 1 347 ? 129.475 152.234 113.553 1.00 12734. ? 347 TYR A CG    1 
ATOM   2532  C  CD1   . TYR A 1 347 ? 129.359 152.460 112.192 1.00 12748. ? 347 TYR A CD1   1 
ATOM   2533  C  CD2   . TYR A 1 347 ? 129.023 153.217 114.420 1.00 12746. ? 347 TYR A CD2   1 
ATOM   2534  C  CE1   . TYR A 1 347 ? 128.800 153.622 111.708 1.00 12755. ? 347 TYR A CE1   1 
ATOM   2535  C  CE2   . TYR A 1 347 ? 128.464 154.383 113.945 1.00 12749. ? 347 TYR A CE2   1 
ATOM   2536  C  CZ    . TYR A 1 347 ? 128.357 154.580 112.590 1.00 12750. ? 347 TYR A CZ    1 
ATOM   2537  O  OH    . TYR A 1 347 ? 127.800 155.742 112.112 1.00 12759. ? 347 TYR A OH    1 
ATOM   2538  N  N     . HIS A 1 348 ? 127.116 149.919 112.788 1.00 12740. ? 348 HIS A N     1 
ATOM   2539  C  CA    . HIS A 1 348 ? 125.667 149.896 112.943 1.00 12732. ? 348 HIS A CA    1 
ATOM   2540  C  C     . HIS A 1 348 ? 125.157 148.525 113.368 1.00 12716. ? 348 HIS A C     1 
ATOM   2541  O  O     . HIS A 1 348 ? 124.262 148.438 114.216 1.00 12727. ? 348 HIS A O     1 
ATOM   2542  C  CB    . HIS A 1 348 ? 124.996 150.330 111.642 1.00 12716. ? 348 HIS A CB    1 
ATOM   2543  C  CG    . HIS A 1 348 ? 124.949 151.813 111.456 1.00 12728. ? 348 HIS A CG    1 
ATOM   2544  N  ND1   . HIS A 1 348 ? 124.625 152.680 112.478 1.00 12750. ? 348 HIS A ND1   1 
ATOM   2545  C  CD2   . HIS A 1 348 ? 125.189 152.585 110.371 1.00 12735. ? 348 HIS A CD2   1 
ATOM   2546  C  CE1   . HIS A 1 348 ? 124.665 153.921 112.028 1.00 12748. ? 348 HIS A CE1   1 
ATOM   2547  N  NE2   . HIS A 1 348 ? 125.005 153.891 110.753 1.00 12738. ? 348 HIS A NE2   1 
ATOM   2548  N  N     . ASP A 1 349 ? 125.698 147.453 112.789 1.00 12708. ? 349 ASP A N     1 
ATOM   2549  C  CA    . ASP A 1 349 ? 125.363 146.104 113.223 1.00 12685. ? 349 ASP A CA    1 
ATOM   2550  C  C     . ASP A 1 349 ? 125.874 145.808 114.624 1.00 12733. ? 349 ASP A C     1 
ATOM   2551  O  O     . ASP A 1 349 ? 125.175 145.151 115.407 1.00 12745. ? 349 ASP A O     1 
ATOM   2552  C  CB    . ASP A 1 349 ? 125.941 145.085 112.242 1.00 12670. ? 349 ASP A CB    1 
ATOM   2553  C  CG    . ASP A 1 349 ? 125.642 145.437 110.801 1.00 12655. ? 349 ASP A CG    1 
ATOM   2554  O  OD1   . ASP A 1 349 ? 124.947 146.447 110.568 1.00 12648. ? 349 ASP A OD1   1 
ATOM   2555  O  OD2   . ASP A 1 349 ? 126.108 144.710 109.899 1.00 12677. ? 349 ASP A OD2   1 
ATOM   2556  N  N     . LEU A 1 350 ? 127.073 146.279 114.953 1.00 12731. ? 350 LEU A N     1 
ATOM   2557  C  CA    . LEU A 1 350 ? 127.606 146.154 116.297 1.00 12734. ? 350 LEU A CA    1 
ATOM   2558  C  C     . LEU A 1 350 ? 126.771 146.899 117.324 1.00 12735. ? 350 LEU A C     1 
ATOM   2559  O  O     . LEU A 1 350 ? 126.699 146.458 118.470 1.00 12749. ? 350 LEU A O     1 
ATOM   2560  C  CB    . LEU A 1 350 ? 129.048 146.668 116.349 1.00 12740. ? 350 LEU A CB    1 
ATOM   2561  C  CG    . LEU A 1 350 ? 130.127 145.883 115.603 1.00 12746. ? 350 LEU A CG    1 
ATOM   2562  C  CD1   . LEU A 1 350 ? 131.483 146.150 116.227 1.00 12755. ? 350 LEU A CD1   1 
ATOM   2563  C  CD2   . LEU A 1 350 ? 129.822 144.397 115.571 1.00 12749. ? 350 LEU A CD2   1 
ATOM   2564  N  N     . MET A 1 351 ? 126.133 148.003 116.940 1.00 12737. ? 351 MET A N     1 
ATOM   2565  C  CA    . MET A 1 351 ? 125.265 148.746 117.841 1.00 12735. ? 351 MET A CA    1 
ATOM   2566  C  C     . MET A 1 351 ? 124.005 147.980 118.211 1.00 12735. ? 351 MET A C     1 
ATOM   2567  O  O     . MET A 1 351 ? 123.389 148.292 119.234 1.00 12757. ? 351 MET A O     1 
ATOM   2568  C  CB    . MET A 1 351 ? 124.893 150.094 117.214 1.00 12747. ? 351 MET A CB    1 
ATOM   2569  C  CG    . MET A 1 351 ? 125.900 151.187 117.517 1.00 12754. ? 351 MET A CG    1 
ATOM   2570  S  SD    . MET A 1 351 ? 125.520 152.797 116.815 1.00 12734. ? 351 MET A SD    1 
ATOM   2571  C  CE    . MET A 1 351 ? 123.870 153.018 117.449 1.00 12749. ? 351 MET A CE    1 
ATOM   2572  N  N     . GLU A 1 352 ? 123.603 146.996 117.407 1.00 12729. ? 352 GLU A N     1 
ATOM   2573  C  CA    . GLU A 1 352 ? 122.521 146.088 117.764 1.00 12732. ? 352 GLU A CA    1 
ATOM   2574  C  C     . GLU A 1 352 ? 123.011 144.844 118.482 1.00 12730. ? 352 GLU A C     1 
ATOM   2575  O  O     . GLU A 1 352 ? 122.354 144.376 119.421 1.00 12725. ? 352 GLU A O     1 
ATOM   2576  C  CB    . GLU A 1 352 ? 121.748 145.663 116.513 1.00 12745. ? 352 GLU A CB    1 
ATOM   2577  C  CG    . GLU A 1 352 ? 121.074 146.804 115.782 1.00 12743. ? 352 GLU A CG    1 
ATOM   2578  C  CD    . GLU A 1 352 ? 120.190 146.320 114.654 1.00 12683. ? 352 GLU A CD    1 
ATOM   2579  O  OE1   . GLU A 1 352 ? 120.073 145.089 114.479 1.00 12662. ? 352 GLU A OE1   1 
ATOM   2580  O  OE2   . GLU A 1 352 ? 119.612 147.167 113.944 1.00 12661. ? 352 GLU A OE2   1 
ATOM   2581  N  N     . ILE A 1 353 ? 124.152 144.302 118.057 1.00 12721. ? 353 ILE A N     1 
ATOM   2582  C  CA    . ILE A 1 353 ? 124.718 143.145 118.742 1.00 12703. ? 353 ILE A CA    1 
ATOM   2583  C  C     . ILE A 1 353 ? 125.053 143.490 120.188 1.00 12737. ? 353 ILE A C     1 
ATOM   2584  O  O     . ILE A 1 353 ? 124.814 142.691 121.098 1.00 12741. ? 353 ILE A O     1 
ATOM   2585  C  CB    . ILE A 1 353 ? 125.946 142.618 117.982 1.00 12719. ? 353 ILE A CB    1 
ATOM   2586  C  CG1   . ILE A 1 353 ? 125.561 142.243 116.553 1.00 12705. ? 353 ILE A CG1   1 
ATOM   2587  C  CG2   . ILE A 1 353 ? 126.538 141.419 118.692 1.00 12728. ? 353 ILE A CG2   1 
ATOM   2588  C  CD1   . ILE A 1 353 ? 126.728 141.798 115.710 1.00 12723. ? 353 ILE A CD1   1 
ATOM   2589  N  N     . THR A 1 354 ? 125.611 144.679 120.426 1.00 12742. ? 354 THR A N     1 
ATOM   2590  C  CA    . THR A 1 354 ? 125.926 145.104 121.785 1.00 12735. ? 354 THR A CA    1 
ATOM   2591  C  C     . THR A 1 354 ? 124.663 145.279 122.617 1.00 12737. ? 354 THR A C     1 
ATOM   2592  O  O     . THR A 1 354 ? 124.629 144.906 123.795 1.00 12759. ? 354 THR A O     1 
ATOM   2593  C  CB    . THR A 1 354 ? 126.728 146.404 121.747 1.00 12736. ? 354 THR A CB    1 
ATOM   2594  O  OG1   . THR A 1 354 ? 127.967 146.180 121.065 1.00 12743. ? 354 THR A OG1   1 
ATOM   2595  C  CG2   . THR A 1 354 ? 127.015 146.900 123.151 1.00 12745. ? 354 THR A CG2   1 
ATOM   2596  N  N     . GLU A 1 355 ? 123.619 145.860 122.024 1.00 12745. ? 355 GLU A N     1 
ATOM   2597  C  CA    . GLU A 1 355 ? 122.343 145.983 122.720 1.00 12744. ? 355 GLU A CA    1 
ATOM   2598  C  C     . GLU A 1 355 ? 121.840 144.619 123.163 1.00 12746. ? 355 GLU A C     1 
ATOM   2599  O  O     . GLU A 1 355 ? 121.471 144.422 124.328 1.00 12757. ? 355 GLU A O     1 
ATOM   2600  C  CB    . GLU A 1 355 ? 121.315 146.650 121.810 1.00 12743. ? 355 GLU A CB    1 
ATOM   2601  C  CG    . GLU A 1 355 ? 121.201 148.145 121.967 1.00 12749. ? 355 GLU A CG    1 
ATOM   2602  C  CD    . GLU A 1 355 ? 120.182 148.742 121.019 1.00 12743. ? 355 GLU A CD    1 
ATOM   2603  O  OE1   . GLU A 1 355 ? 119.487 147.967 120.330 1.00 12744. ? 355 GLU A OE1   1 
ATOM   2604  O  OE2   . GLU A 1 355 ? 120.078 149.984 120.958 1.00 12748. ? 355 GLU A OE2   1 
ATOM   2605  N  N     . LYS A 1 356 ? 121.824 143.660 122.236 1.00 12744. ? 356 LYS A N     1 
ATOM   2606  C  CA    . LYS A 1 356 ? 121.347 142.323 122.567 1.00 12736. ? 356 LYS A CA    1 
ATOM   2607  C  C     . LYS A 1 356 ? 122.214 141.688 123.646 1.00 12738. ? 356 LYS A C     1 
ATOM   2608  O  O     . LYS A 1 356 ? 121.698 141.134 124.622 1.00 12758. ? 356 LYS A O     1 
ATOM   2609  C  CB    . LYS A 1 356 ? 121.314 141.457 121.310 1.00 12702. ? 356 LYS A CB    1 
ATOM   2610  C  CG    . LYS A 1 356 ? 120.330 140.312 121.384 1.00 12636. ? 356 LYS A CG    1 
ATOM   2611  C  CD    . LYS A 1 356 ? 119.056 140.663 120.639 1.00 12643. ? 356 LYS A CD    1 
ATOM   2612  C  CE    . LYS A 1 356 ? 118.102 139.487 120.575 1.00 12575. ? 356 LYS A CE    1 
ATOM   2613  N  NZ    . LYS A 1 356 ? 116.682 139.933 120.558 1.00 12651. ? 356 LYS A NZ    1 
ATOM   2614  N  N     . MET A 1 357 ? 123.539 141.798 123.507 1.00 12740. ? 357 MET A N     1 
ATOM   2615  C  CA    . MET A 1 357 ? 124.453 141.234 124.496 1.00 12736. ? 357 MET A CA    1 
ATOM   2616  C  C     . MET A 1 357 ? 124.163 141.774 125.887 1.00 12740. ? 357 MET A C     1 
ATOM   2617  O  O     . MET A 1 357 ? 123.943 141.007 126.830 1.00 12764. ? 357 MET A O     1 
ATOM   2618  C  CB    . MET A 1 357 ? 125.900 141.560 124.123 1.00 12742. ? 357 MET A CB    1 
ATOM   2619  C  CG    . MET A 1 357 ? 126.937 140.848 124.982 1.00 12735. ? 357 MET A CG    1 
ATOM   2620  S  SD    . MET A 1 357 ? 128.482 140.437 124.145 1.00 12719. ? 357 MET A SD    1 
ATOM   2621  C  CE    . MET A 1 357 ? 127.929 140.114 122.481 1.00 12743. ? 357 MET A CE    1 
ATOM   2622  N  N     . VAL A 1 358 ? 124.145 143.098 126.028 1.00 12738. ? 358 VAL A N     1 
ATOM   2623  C  CA    . VAL A 1 358 ? 124.059 143.706 127.350 1.00 12725. ? 358 VAL A CA    1 
ATOM   2624  C  C     . VAL A 1 358 ? 122.686 143.461 127.963 1.00 12735. ? 358 VAL A C     1 
ATOM   2625  O  O     . VAL A 1 358 ? 122.574 143.081 129.136 1.00 12763. ? 358 VAL A O     1 
ATOM   2626  C  CB    . VAL A 1 358 ? 124.391 145.207 127.270 1.00 12732. ? 358 VAL A CB    1 
ATOM   2627  C  CG1   . VAL A 1 358 ? 124.065 145.895 128.576 1.00 12740. ? 358 VAL A CG1   1 
ATOM   2628  C  CG2   . VAL A 1 358 ? 125.855 145.402 126.925 1.00 12741. ? 358 VAL A CG2   1 
ATOM   2629  N  N     . SER A 1 359 ? 121.620 143.672 127.185 1.00 12736. ? 359 SER A N     1 
ATOM   2630  C  CA    . SER A 1 359 ? 120.281 143.461 127.723 1.00 12743. ? 359 SER A CA    1 
ATOM   2631  C  C     . SER A 1 359 ? 120.071 142.006 128.123 1.00 12743. ? 359 SER A C     1 
ATOM   2632  O  O     . SER A 1 359 ? 119.554 141.725 129.213 1.00 12754. ? 359 SER A O     1 
ATOM   2633  C  CB    . SER A 1 359 ? 119.233 143.903 126.704 1.00 12753. ? 359 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 359 ? 119.387 143.209 125.480 1.00 12759. ? 359 SER A OG    1 
ATOM   2635  N  N     . GLY A 1 360 ? 120.484 141.064 127.270 1.00 12747. ? 360 GLY A N     1 
ATOM   2636  C  CA    . GLY A 1 360 ? 120.319 139.663 127.603 1.00 12748. ? 360 GLY A CA    1 
ATOM   2637  C  C     . GLY A 1 360 ? 121.134 139.248 128.810 1.00 12749. ? 360 GLY A C     1 
ATOM   2638  O  O     . GLY A 1 360 ? 120.662 138.484 129.649 1.00 12765. ? 360 GLY A O     1 
ATOM   2639  N  N     . MET A 1 361 ? 122.366 139.752 128.920 1.00 12746. ? 361 MET A N     1 
ATOM   2640  C  CA    . MET A 1 361 ? 123.197 139.410 130.068 1.00 12739. ? 361 MET A CA    1 
ATOM   2641  C  C     . MET A 1 361 ? 122.596 139.938 131.362 1.00 12746. ? 361 MET A C     1 
ATOM   2642  O  O     . MET A 1 361 ? 122.530 139.217 132.366 1.00 12772. ? 361 MET A O     1 
ATOM   2643  C  CB    . MET A 1 361 ? 124.609 139.957 129.869 1.00 12746. ? 361 MET A CB    1 
ATOM   2644  C  CG    . MET A 1 361 ? 125.384 140.173 131.153 1.00 12748. ? 361 MET A CG    1 
ATOM   2645  S  SD    . MET A 1 361 ? 126.801 141.261 130.930 1.00 12747. ? 361 MET A SD    1 
ATOM   2646  C  CE    . MET A 1 361 ? 127.344 140.773 129.299 1.00 12747. ? 361 MET A CE    1 
ATOM   2647  N  N     . VAL A 1 362 ? 122.143 141.194 131.357 1.00 12739. ? 362 VAL A N     1 
ATOM   2648  C  CA    . VAL A 1 362 ? 121.558 141.769 132.564 1.00 12733. ? 362 VAL A CA    1 
ATOM   2649  C  C     . VAL A 1 362 ? 120.293 141.017 132.951 1.00 12732. ? 362 VAL A C     1 
ATOM   2650  O  O     . VAL A 1 362 ? 120.082 140.696 134.127 1.00 12759. ? 362 VAL A O     1 
ATOM   2651  C  CB    . VAL A 1 362 ? 121.292 143.271 132.368 1.00 12736. ? 362 VAL A CB    1 
ATOM   2652  C  CG1   . VAL A 1 362 ? 120.505 143.827 133.539 1.00 12751. ? 362 VAL A CG1   1 
ATOM   2653  C  CG2   . VAL A 1 362 ? 122.602 144.014 132.213 1.00 12742. ? 362 VAL A CG2   1 
ATOM   2654  N  N     . LYS A 1 363 ? 119.440 140.706 131.973 1.00 12722. ? 363 LYS A N     1 
ATOM   2655  C  CA    . LYS A 1 363 ? 118.218 139.969 132.279 1.00 12728. ? 363 LYS A CA    1 
ATOM   2656  C  C     . LYS A 1 363 ? 118.527 138.566 132.787 1.00 12724. ? 363 LYS A C     1 
ATOM   2657  O  O     . LYS A 1 363 ? 117.862 138.069 133.702 1.00 12740. ? 363 LYS A O     1 
ATOM   2658  C  CB    . LYS A 1 363 ? 117.321 139.908 131.045 1.00 12754. ? 363 LYS A CB    1 
ATOM   2659  C  CG    . LYS A 1 363 ? 115.999 139.206 131.279 1.00 12751. ? 363 LYS A CG    1 
ATOM   2660  C  CD    . LYS A 1 363 ? 114.898 140.201 131.586 1.00 12753. ? 363 LYS A CD    1 
ATOM   2661  C  CE    . LYS A 1 363 ? 113.540 139.524 131.610 1.00 12749. ? 363 LYS A CE    1 
ATOM   2662  N  NZ    . LYS A 1 363 ? 113.361 138.613 130.447 1.00 12751. ? 363 LYS A NZ    1 
ATOM   2663  N  N     . HIS A 1 364 ? 119.531 137.911 132.206 1.00 12721. ? 364 HIS A N     1 
ATOM   2664  C  CA    . HIS A 1 364 ? 119.862 136.547 132.599 1.00 12725. ? 364 HIS A CA    1 
ATOM   2665  C  C     . HIS A 1 364 ? 120.435 136.495 134.007 1.00 12742. ? 364 HIS A C     1 
ATOM   2666  O  O     . HIS A 1 364 ? 120.137 135.570 134.769 1.00 12754. ? 364 HIS A O     1 
ATOM   2667  C  CB    . HIS A 1 364 ? 120.849 135.950 131.597 1.00 12738. ? 364 HIS A CB    1 
ATOM   2668  C  CG    . HIS A 1 364 ? 121.087 134.485 131.779 1.00 12735. ? 364 HIS A CG    1 
ATOM   2669  N  ND1   . HIS A 1 364 ? 122.294 133.976 132.206 1.00 12716. ? 364 HIS A ND1   1 
ATOM   2670  C  CD2   . HIS A 1 364 ? 120.277 133.419 131.584 1.00 12717. ? 364 HIS A CD2   1 
ATOM   2671  C  CE1   . HIS A 1 364 ? 122.216 132.659 132.271 1.00 12654. ? 364 HIS A CE1   1 
ATOM   2672  N  NE2   . HIS A 1 364 ? 121.002 132.296 131.898 1.00 12642. ? 364 HIS A NE2   1 
ATOM   2673  N  N     . ILE A 1 365 ? 121.257 137.473 134.372 1.00 12751. ? 365 ILE A N     1 
ATOM   2674  C  CA    . ILE A 1 365 ? 121.961 137.418 135.648 1.00 12730. ? 365 ILE A CA    1 
ATOM   2675  C  C     . ILE A 1 365 ? 121.146 138.049 136.769 1.00 12736. ? 365 ILE A C     1 
ATOM   2676  O  O     . ILE A 1 365 ? 120.908 137.421 137.803 1.00 12749. ? 365 ILE A O     1 
ATOM   2677  C  CB    . ILE A 1 365 ? 123.343 138.081 135.506 1.00 12726. ? 365 ILE A CB    1 
ATOM   2678  C  CG1   . ILE A 1 365 ? 124.219 137.235 134.585 1.00 12734. ? 365 ILE A CG1   1 
ATOM   2679  C  CG2   . ILE A 1 365 ? 123.994 138.253 136.863 1.00 12739. ? 365 ILE A CG2   1 
ATOM   2680  C  CD1   . ILE A 1 365 ? 125.497 137.896 134.197 1.00 12753. ? 365 ILE A CD1   1 
ATOM   2681  N  N     . THR A 1 366 ? 120.702 139.293 136.596 1.00 12738. ? 366 THR A N     1 
ATOM   2682  C  CA    . THR A 1 366 ? 119.962 139.967 137.653 1.00 12738. ? 366 THR A CA    1 
ATOM   2683  C  C     . THR A 1 366 ? 118.485 139.602 137.677 1.00 12736. ? 366 THR A C     1 
ATOM   2684  O  O     . THR A 1 366 ? 117.801 139.933 138.651 1.00 12742. ? 366 THR A O     1 
ATOM   2685  C  CB    . THR A 1 366 ? 120.106 141.482 137.514 1.00 12742. ? 366 THR A CB    1 
ATOM   2686  O  OG1   . THR A 1 366 ? 119.094 141.979 136.630 1.00 12745. ? 366 THR A OG1   1 
ATOM   2687  C  CG2   . THR A 1 366 ? 121.475 141.833 136.960 1.00 12755. ? 366 THR A CG2   1 
ATOM   2688  N  N     . GLY A 1 367 ? 117.977 138.941 136.640 1.00 12734. ? 367 GLY A N     1 
ATOM   2689  C  CA    . GLY A 1 367 ? 116.589 138.540 136.595 1.00 12736. ? 367 GLY A CA    1 
ATOM   2690  C  C     . GLY A 1 367 ? 115.629 139.587 136.079 1.00 12736. ? 367 GLY A C     1 
ATOM   2691  O  O     . GLY A 1 367 ? 114.447 139.277 135.888 1.00 12740. ? 367 GLY A O     1 
ATOM   2692  N  N     . SER A 1 368 ? 116.089 140.812 135.846 1.00 12740. ? 368 SER A N     1 
ATOM   2693  C  CA    . SER A 1 368 ? 115.240 141.882 135.346 1.00 12743. ? 368 SER A CA    1 
ATOM   2694  C  C     . SER A 1 368 ? 116.093 142.798 134.478 1.00 12745. ? 368 SER A C     1 
ATOM   2695  O  O     . SER A 1 368 ? 117.270 142.526 134.222 1.00 12756. ? 368 SER A O     1 
ATOM   2696  C  CB    . SER A 1 368 ? 114.574 142.635 136.505 1.00 12750. ? 368 SER A CB    1 
ATOM   2697  O  OG    . SER A 1 368 ? 114.117 143.908 136.086 1.00 12750. ? 368 SER A OG    1 
ATOM   2698  N  N     . TYR A 1 369 ? 115.494 143.896 134.021 1.00 12735. ? 369 TYR A N     1 
ATOM   2699  C  CA    . TYR A 1 369 ? 116.200 144.866 133.198 1.00 12733. ? 369 TYR A CA    1 
ATOM   2700  C  C     . TYR A 1 369 ? 116.685 146.078 133.976 1.00 12745. ? 369 TYR A C     1 
ATOM   2701  O  O     . TYR A 1 369 ? 117.562 146.795 133.486 1.00 12765. ? 369 TYR A O     1 
ATOM   2702  C  CB    . TYR A 1 369 ? 115.304 145.341 132.051 1.00 12743. ? 369 TYR A CB    1 
ATOM   2703  C  CG    . TYR A 1 369 ? 115.351 144.450 130.837 1.00 12734. ? 369 TYR A CG    1 
ATOM   2704  C  CD1   . TYR A 1 369 ? 116.544 143.889 130.411 1.00 12735. ? 369 TYR A CD1   1 
ATOM   2705  C  CD2   . TYR A 1 369 ? 114.201 144.169 130.116 1.00 12741. ? 369 TYR A CD2   1 
ATOM   2706  C  CE1   . TYR A 1 369 ? 116.591 143.074 129.303 1.00 12744. ? 369 TYR A CE1   1 
ATOM   2707  C  CE2   . TYR A 1 369 ? 114.239 143.355 129.006 1.00 12746. ? 369 TYR A CE2   1 
ATOM   2708  C  CZ    . TYR A 1 369 ? 115.436 142.810 128.604 1.00 12750. ? 369 TYR A CZ    1 
ATOM   2709  O  OH    . TYR A 1 369 ? 115.477 141.998 127.496 1.00 12762. ? 369 TYR A OH    1 
ATOM   2710  N  N     . LYS A 1 370 ? 116.146 146.323 135.165 1.00 12740. ? 370 LYS A N     1 
ATOM   2711  C  CA    . LYS A 1 370 ? 116.499 147.486 135.966 1.00 12743. ? 370 LYS A CA    1 
ATOM   2712  C  C     . LYS A 1 370 ? 117.379 147.057 137.130 1.00 12741. ? 370 LYS A C     1 
ATOM   2713  O  O     . LYS A 1 370 ? 117.050 146.108 137.847 1.00 12753. ? 370 LYS A O     1 
ATOM   2714  C  CB    . LYS A 1 370 ? 115.246 148.192 136.485 1.00 12737. ? 370 LYS A CB    1 
ATOM   2715  C  CG    . LYS A 1 370 ? 114.061 148.110 135.543 1.00 12746. ? 370 LYS A CG    1 
ATOM   2716  C  CD    . LYS A 1 370 ? 112.916 148.977 136.030 1.00 12748. ? 370 LYS A CD    1 
ATOM   2717  C  CE    . LYS A 1 370 ? 113.247 150.452 135.891 1.00 12745. ? 370 LYS A CE    1 
ATOM   2718  N  NZ    . LYS A 1 370 ? 112.717 151.018 134.621 1.00 12755. ? 370 LYS A NZ    1 
ATOM   2719  N  N     . VAL A 1 371 ? 118.496 147.758 137.310 1.00 12742. ? 371 VAL A N     1 
ATOM   2720  C  CA    . VAL A 1 371 ? 119.406 147.510 138.418 1.00 12741. ? 371 VAL A CA    1 
ATOM   2721  C  C     . VAL A 1 371 ? 119.543 148.791 139.229 1.00 12756. ? 371 VAL A C     1 
ATOM   2722  O  O     . VAL A 1 371 ? 119.215 149.887 138.771 1.00 12787. ? 371 VAL A O     1 
ATOM   2723  C  CB    . VAL A 1 371 ? 120.789 147.012 137.949 1.00 12740. ? 371 VAL A CB    1 
ATOM   2724  C  CG1   . VAL A 1 371 ? 120.645 146.070 136.769 1.00 12747. ? 371 VAL A CG1   1 
ATOM   2725  C  CG2   . VAL A 1 371 ? 121.687 148.181 137.593 1.00 12755. ? 371 VAL A CG2   1 
ATOM   2726  N  N     . THR A 1 372 ? 120.016 148.636 140.460 1.00 12743. ? 372 THR A N     1 
ATOM   2727  C  CA    . THR A 1 372 ? 120.289 149.758 141.348 1.00 12745. ? 372 THR A CA    1 
ATOM   2728  C  C     . THR A 1 372 ? 121.790 149.829 141.579 1.00 12743. ? 372 THR A C     1 
ATOM   2729  O  O     . THR A 1 372 ? 122.412 148.828 141.950 1.00 12758. ? 372 THR A O     1 
ATOM   2730  C  CB    . THR A 1 372 ? 119.550 149.609 142.677 1.00 12753. ? 372 THR A CB    1 
ATOM   2731  O  OG1   . THR A 1 372 ? 120.018 148.436 143.353 1.00 12753. ? 372 THR A OG1   1 
ATOM   2732  C  CG2   . THR A 1 372 ? 118.056 149.487 142.442 1.00 12763. ? 372 THR A CG2   1 
ATOM   2733  N  N     . TYR A 1 373 ? 122.368 151.004 141.357 1.00 12737. ? 373 TYR A N     1 
ATOM   2734  C  CA    . TYR A 1 373 ? 123.799 151.213 141.513 1.00 12734. ? 373 TYR A CA    1 
ATOM   2735  C  C     . TYR A 1 373 ? 124.044 152.302 142.545 1.00 12762. ? 373 TYR A C     1 
ATOM   2736  O  O     . TYR A 1 373 ? 123.401 153.354 142.508 1.00 12772. ? 373 TYR A O     1 
ATOM   2737  C  CB    . TYR A 1 373 ? 124.449 151.588 140.181 1.00 12732. ? 373 TYR A CB    1 
ATOM   2738  C  CG    . TYR A 1 373 ? 125.956 151.603 140.233 1.00 12742. ? 373 TYR A CG    1 
ATOM   2739  C  CD1   . TYR A 1 373 ? 126.677 150.424 140.338 1.00 12751. ? 373 TYR A CD1   1 
ATOM   2740  C  CD2   . TYR A 1 373 ? 126.657 152.796 140.184 1.00 12763. ? 373 TYR A CD2   1 
ATOM   2741  C  CE1   . TYR A 1 373 ? 128.053 150.434 140.391 1.00 12750. ? 373 TYR A CE1   1 
ATOM   2742  C  CE2   . TYR A 1 373 ? 128.032 152.816 140.234 1.00 12769. ? 373 TYR A CE2   1 
ATOM   2743  C  CZ    . TYR A 1 373 ? 128.725 151.633 140.338 1.00 12753. ? 373 TYR A CZ    1 
ATOM   2744  O  OH    . TYR A 1 373 ? 130.098 151.651 140.389 1.00 12749. ? 373 TYR A OH    1 
ATOM   2745  N  N     . HIS A 1 374 ? 124.971 152.045 143.467 1.00 13019. ? 374 HIS A N     1 
ATOM   2746  C  CA    . HIS A 1 374 ? 125.363 153.033 144.459 1.00 13044. ? 374 HIS A CA    1 
ATOM   2747  C  C     . HIS A 1 374 ? 126.765 153.524 144.134 1.00 13060. ? 374 HIS A C     1 
ATOM   2748  O  O     . HIS A 1 374 ? 127.748 152.912 144.577 1.00 13064. ? 374 HIS A O     1 
ATOM   2749  C  CB    . HIS A 1 374 ? 125.315 152.438 145.868 1.00 13060. ? 374 HIS A CB    1 
ATOM   2750  C  CG    . HIS A 1 374 ? 123.938 152.073 146.323 1.00 13050. ? 374 HIS A CG    1 
ATOM   2751  N  ND1   . HIS A 1 374 ? 123.351 150.862 146.026 1.00 13003. ? 374 HIS A ND1   1 
ATOM   2752  C  CD2   . HIS A 1 374 ? 123.030 152.760 147.055 1.00 13083. ? 374 HIS A CD2   1 
ATOM   2753  C  CE1   . HIS A 1 374 ? 122.142 150.819 146.555 1.00 13006. ? 374 HIS A CE1   1 
ATOM   2754  N  NE2   . HIS A 1 374 ? 121.923 151.959 147.185 1.00 13040. ? 374 HIS A NE2   1 
ATOM   2755  N  N     . PRO A 1 375 ? 126.918 154.603 143.362 1.00 13241. ? 375 PRO A N     1 
ATOM   2756  C  CA    . PRO A 1 375 ? 128.268 155.073 143.021 1.00 13260. ? 375 PRO A CA    1 
ATOM   2757  C  C     . PRO A 1 375 ? 129.079 155.532 144.216 1.00 13307. ? 375 PRO A C     1 
ATOM   2758  O  O     . PRO A 1 375 ? 130.307 155.386 144.199 1.00 13274. ? 375 PRO A O     1 
ATOM   2759  C  CB    . PRO A 1 375 ? 127.990 156.231 142.055 1.00 13253. ? 375 PRO A CB    1 
ATOM   2760  C  CG    . PRO A 1 375 ? 126.666 156.748 142.507 1.00 13261. ? 375 PRO A CG    1 
ATOM   2761  C  CD    . PRO A 1 375 ? 125.882 155.504 142.831 1.00 13246. ? 375 PRO A CD    1 
ATOM   2762  N  N     . ASP A 1 376 ? 128.441 156.073 145.252 1.00 15072. ? 376 ASP A N     1 
ATOM   2763  C  CA    . ASP A 1 376 ? 129.146 156.603 146.407 1.00 15115. ? 376 ASP A CA    1 
ATOM   2764  C  C     . ASP A 1 376 ? 129.212 155.635 147.577 1.00 15131. ? 376 ASP A C     1 
ATOM   2765  O  O     . ASP A 1 376 ? 129.904 155.925 148.558 1.00 15158. ? 376 ASP A O     1 
ATOM   2766  C  CB    . ASP A 1 376 ? 128.486 157.908 146.875 1.00 15161. ? 376 ASP A CB    1 
ATOM   2767  C  CG    . ASP A 1 376 ? 128.286 158.897 145.746 1.00 15157. ? 376 ASP A CG    1 
ATOM   2768  O  OD1   . ASP A 1 376 ? 128.881 158.696 144.667 1.00 15146. ? 376 ASP A OD1   1 
ATOM   2769  O  OD2   . ASP A 1 376 ? 127.531 159.873 145.936 1.00 15166. ? 376 ASP A OD2   1 
ATOM   2770  N  N     . GLY A 1 377 ? 128.520 154.504 147.505 1.00 14807. ? 377 GLY A N     1 
ATOM   2771  C  CA    . GLY A 1 377 ? 128.491 153.563 148.597 1.00 14848. ? 377 GLY A CA    1 
ATOM   2772  C  C     . GLY A 1 377 ? 127.076 153.282 149.052 1.00 14880. ? 377 GLY A C     1 
ATOM   2773  O  O     . GLY A 1 377 ? 126.116 153.904 148.587 1.00 14861. ? 377 GLY A O     1 
ATOM   2774  N  N     . PRO A 1 378 ? 126.919 152.339 149.985 1.00 16310. ? 378 PRO A N     1 
ATOM   2775  C  CA    . PRO A 1 378 ? 125.574 151.959 150.442 1.00 16334. ? 378 PRO A CA    1 
ATOM   2776  C  C     . PRO A 1 378 ? 124.813 153.078 151.132 1.00 16368. ? 378 PRO A C     1 
ATOM   2777  O  O     . PRO A 1 378 ? 123.593 152.961 151.293 1.00 16364. ? 378 PRO A O     1 
ATOM   2778  C  CB    . PRO A 1 378 ? 125.855 150.805 151.418 1.00 16356. ? 378 PRO A CB    1 
ATOM   2779  C  CG    . PRO A 1 378 ? 127.203 150.291 151.014 1.00 16358. ? 378 PRO A CG    1 
ATOM   2780  C  CD    . PRO A 1 378 ? 127.961 151.517 150.618 1.00 16351. ? 378 PRO A CD    1 
ATOM   2781  N  N     . GLU A 1 379 ? 125.482 154.153 151.542 1.00 17280. ? 379 GLU A N     1 
ATOM   2782  C  CA    . GLU A 1 379 ? 124.826 155.268 152.205 1.00 17307. ? 379 GLU A CA    1 
ATOM   2783  C  C     . GLU A 1 379 ? 124.612 156.464 151.291 1.00 17294. ? 379 GLU A C     1 
ATOM   2784  O  O     . GLU A 1 379 ? 123.986 157.442 151.714 1.00 17315. ? 379 GLU A O     1 
ATOM   2785  C  CB    . GLU A 1 379 ? 125.637 155.708 153.432 1.00 17331. ? 379 GLU A CB    1 
ATOM   2786  C  CG    . GLU A 1 379 ? 126.873 156.534 153.097 1.00 17341. ? 379 GLU A CG    1 
ATOM   2787  C  CD    . GLU A 1 379 ? 128.012 155.703 152.532 1.00 17322. ? 379 GLU A CD    1 
ATOM   2788  O  OE1   . GLU A 1 379 ? 127.884 154.462 152.478 1.00 17311. ? 379 GLU A OE1   1 
ATOM   2789  O  OE2   . GLU A 1 379 ? 129.038 156.296 152.138 1.00 17326. ? 379 GLU A OE2   1 
ATOM   2790  N  N     . GLY A 1 380 ? 125.111 156.419 150.058 1.00 16133. ? 380 GLY A N     1 
ATOM   2791  C  CA    . GLY A 1 380 ? 124.972 157.518 149.128 1.00 16104. ? 380 GLY A CA    1 
ATOM   2792  C  C     . GLY A 1 380 ? 123.725 157.399 148.274 1.00 16070. ? 380 GLY A C     1 
ATOM   2793  O  O     . GLY A 1 380 ? 122.862 156.546 148.484 1.00 16061. ? 380 GLY A O     1 
ATOM   2794  N  N     . GLN A 1 381 ? 123.638 158.289 147.289 1.00 15134. ? 381 GLN A N     1 
ATOM   2795  C  CA    . GLN A 1 381 ? 122.509 158.286 146.371 1.00 15101. ? 381 GLN A CA    1 
ATOM   2796  C  C     . GLN A 1 381 ? 122.533 157.039 145.496 1.00 15060. ? 381 GLN A C     1 
ATOM   2797  O  O     . GLN A 1 381 ? 123.589 156.614 145.019 1.00 15049. ? 381 GLN A O     1 
ATOM   2798  C  CB    . GLN A 1 381 ? 122.534 159.545 145.505 1.00 15100. ? 381 GLN A CB    1 
ATOM   2799  C  CG    . GLN A 1 381 ? 121.724 159.445 144.224 1.00 15081. ? 381 GLN A CG    1 
ATOM   2800  C  CD    . GLN A 1 381 ? 120.484 160.313 144.250 1.00 15103. ? 381 GLN A CD    1 
ATOM   2801  O  OE1   . GLN A 1 381 ? 120.097 160.832 145.297 1.00 15117. ? 381 GLN A OE1   1 
ATOM   2802  N  NE2   . GLN A 1 381 ? 119.850 160.474 143.095 1.00 15088. ? 381 GLN A NE2   1 
ATOM   2803  N  N     . ALA A 1 382 ? 121.359 156.451 145.288 1.00 13771. ? 382 ALA A N     1 
ATOM   2804  C  CA    . ALA A 1 382 ? 121.210 155.264 144.461 1.00 13720. ? 382 ALA A CA    1 
ATOM   2805  C  C     . ALA A 1 382 ? 120.583 155.634 143.125 1.00 13697. ? 382 ALA A C     1 
ATOM   2806  O  O     . ALA A 1 382 ? 119.631 156.417 143.069 1.00 13716. ? 382 ALA A O     1 
ATOM   2807  C  CB    . ALA A 1 382 ? 120.353 154.212 145.166 1.00 13719. ? 382 ALA A CB    1 
ATOM   2808  N  N     . TYR A 1 383 ? 121.122 155.067 142.050 1.00 13022. ? 383 TYR A N     1 
ATOM   2809  C  CA    . TYR A 1 383 ? 120.649 155.322 140.700 1.00 13010. ? 383 TYR A CA    1 
ATOM   2810  C  C     . TYR A 1 383 ? 119.979 154.076 140.143 1.00 13029. ? 383 TYR A C     1 
ATOM   2811  O  O     . TYR A 1 383 ? 120.445 152.955 140.369 1.00 13024. ? 383 TYR A O     1 
ATOM   2812  C  CB    . TYR A 1 383 ? 121.798 155.738 139.780 1.00 12999. ? 383 TYR A CB    1 
ATOM   2813  C  CG    . TYR A 1 383 ? 122.363 157.105 140.072 1.00 12993. ? 383 TYR A CG    1 
ATOM   2814  C  CD1   . TYR A 1 383 ? 123.263 157.298 141.108 1.00 13015. ? 383 TYR A CD1   1 
ATOM   2815  C  CD2   . TYR A 1 383 ? 122.000 158.203 139.308 1.00 12988. ? 383 TYR A CD2   1 
ATOM   2816  C  CE1   . TYR A 1 383 ? 123.784 158.544 141.377 1.00 13018. ? 383 TYR A CE1   1 
ATOM   2817  C  CE2   . TYR A 1 383 ? 122.516 159.454 139.569 1.00 12995. ? 383 TYR A CE2   1 
ATOM   2818  C  CZ    . TYR A 1 383 ? 123.407 159.619 140.605 1.00 13002. ? 383 TYR A CZ    1 
ATOM   2819  O  OH    . TYR A 1 383 ? 123.925 160.865 140.871 1.00 13009. ? 383 TYR A OH    1 
ATOM   2820  N  N     . ASP A 1 384 ? 118.886 154.280 139.414 1.00 14117. ? 384 ASP A N     1 
ATOM   2821  C  CA    . ASP A 1 384 ? 118.162 153.201 138.755 1.00 14123. ? 384 ASP A CA    1 
ATOM   2822  C  C     . ASP A 1 384 ? 118.590 153.164 137.294 1.00 14101. ? 384 ASP A C     1 
ATOM   2823  O  O     . ASP A 1 384 ? 118.297 154.091 136.531 1.00 14127. ? 384 ASP A O     1 
ATOM   2824  C  CB    . ASP A 1 384 ? 116.654 153.402 138.881 1.00 14158. ? 384 ASP A CB    1 
ATOM   2825  C  CG    . ASP A 1 384 ? 116.081 152.738 140.114 1.00 14166. ? 384 ASP A CG    1 
ATOM   2826  O  OD1   . ASP A 1 384 ? 116.820 151.989 140.784 1.00 14156. ? 384 ASP A OD1   1 
ATOM   2827  O  OD2   . ASP A 1 384 ? 114.892 152.968 140.416 1.00 14177. ? 384 ASP A OD2   1 
ATOM   2828  N  N     . VAL A 1 385 ? 119.280 152.098 136.906 1.00 12787. ? 385 VAL A N     1 
ATOM   2829  C  CA    . VAL A 1 385 ? 119.775 151.931 135.547 1.00 12758. ? 385 VAL A CA    1 
ATOM   2830  C  C     . VAL A 1 385 ? 118.866 150.944 134.832 1.00 12748. ? 385 VAL A C     1 
ATOM   2831  O  O     . VAL A 1 385 ? 118.752 149.783 135.242 1.00 12763. ? 385 VAL A O     1 
ATOM   2832  C  CB    . VAL A 1 385 ? 121.232 151.447 135.538 1.00 12749. ? 385 VAL A CB    1 
ATOM   2833  C  CG1   . VAL A 1 385 ? 121.934 151.915 134.280 1.00 12769. ? 385 VAL A CG1   1 
ATOM   2834  C  CG2   . VAL A 1 385 ? 121.960 151.940 136.774 1.00 12758. ? 385 VAL A CG2   1 
ATOM   2835  N  N     . ASP A 1 386 ? 118.221 151.402 133.765 1.00 12738. ? 386 ASP A N     1 
ATOM   2836  C  CA    . ASP A 1 386 ? 117.320 150.580 132.971 1.00 12732. ? 386 ASP A CA    1 
ATOM   2837  C  C     . ASP A 1 386 ? 118.066 150.039 131.760 1.00 12734. ? 386 ASP A C     1 
ATOM   2838  O  O     . ASP A 1 386 ? 118.707 150.800 131.030 1.00 12749. ? 386 ASP A O     1 
ATOM   2839  C  CB    . ASP A 1 386 ? 116.101 151.386 132.525 1.00 12751. ? 386 ASP A CB    1 
ATOM   2840  C  CG    . ASP A 1 386 ? 114.940 150.508 132.107 1.00 12750. ? 386 ASP A CG    1 
ATOM   2841  O  OD1   . ASP A 1 386 ? 115.165 149.313 131.824 1.00 12747. ? 386 ASP A OD1   1 
ATOM   2842  O  OD2   . ASP A 1 386 ? 113.800 151.013 132.059 1.00 12753. ? 386 ASP A OD2   1 
ATOM   2843  N  N     . PHE A 1 387 ? 117.975 148.731 131.546 1.00 12734. ? 387 PHE A N     1 
ATOM   2844  C  CA    . PHE A 1 387 ? 118.674 148.057 130.459 1.00 12734. ? 387 PHE A CA    1 
ATOM   2845  C  C     . PHE A 1 387 ? 117.698 147.475 129.442 1.00 12746. ? 387 PHE A C     1 
ATOM   2846  O  O     . PHE A 1 387 ? 117.871 146.353 128.965 1.00 12750. ? 387 PHE A O     1 
ATOM   2847  C  CB    . PHE A 1 387 ? 119.585 146.960 131.000 1.00 12741. ? 387 PHE A CB    1 
ATOM   2848  C  CG    . PHE A 1 387 ? 120.855 147.471 131.608 1.00 12739. ? 387 PHE A CG    1 
ATOM   2849  C  CD1   . PHE A 1 387 ? 120.888 147.894 132.923 1.00 12753. ? 387 PHE A CD1   1 
ATOM   2850  C  CD2   . PHE A 1 387 ? 122.019 147.523 130.867 1.00 12746. ? 387 PHE A CD2   1 
ATOM   2851  C  CE1   . PHE A 1 387 ? 122.056 148.362 133.485 1.00 12746. ? 387 PHE A CE1   1 
ATOM   2852  C  CE2   . PHE A 1 387 ? 123.190 147.988 131.424 1.00 12742. ? 387 PHE A CE2   1 
ATOM   2853  C  CZ    . PHE A 1 387 ? 123.208 148.409 132.735 1.00 12732. ? 387 PHE A CZ    1 
ATOM   2854  N  N     . THR A 1 388 ? 116.658 148.233 129.103 1.00 12745. ? 388 THR A N     1 
ATOM   2855  C  CA    . THR A 1 388 ? 115.723 147.791 128.083 1.00 12730. ? 388 THR A CA    1 
ATOM   2856  C  C     . THR A 1 388 ? 116.448 147.672 126.742 1.00 12732. ? 388 THR A C     1 
ATOM   2857  O  O     . THR A 1 388 ? 117.444 148.361 126.511 1.00 12753. ? 388 THR A O     1 
ATOM   2858  C  CB    . THR A 1 388 ? 114.556 148.767 127.968 1.00 12735. ? 388 THR A CB    1 
ATOM   2859  O  OG1   . THR A 1 388 ? 115.049 150.111 128.027 1.00 12749. ? 388 THR A OG1   1 
ATOM   2860  C  CG2   . THR A 1 388 ? 113.568 148.546 129.098 1.00 12734. ? 388 THR A CG2   1 
ATOM   2861  N  N     . PRO A 1 389 ? 115.979 146.799 125.852 1.00 12725. ? 389 PRO A N     1 
ATOM   2862  C  CA    . PRO A 1 389 ? 116.721 146.504 124.615 1.00 12739. ? 389 PRO A CA    1 
ATOM   2863  C  C     . PRO A 1 389 ? 117.130 147.754 123.851 1.00 12742. ? 389 PRO A C     1 
ATOM   2864  O  O     . PRO A 1 389 ? 118.322 147.918 123.553 1.00 12763. ? 389 PRO A O     1 
ATOM   2865  C  CB    . PRO A 1 389 ? 115.734 145.645 123.812 1.00 12749. ? 389 PRO A CB    1 
ATOM   2866  C  CG    . PRO A 1 389 ? 114.947 144.944 124.857 1.00 12758. ? 389 PRO A CG    1 
ATOM   2867  C  CD    . PRO A 1 389 ? 114.813 145.910 126.011 1.00 12748. ? 389 PRO A CD    1 
ATOM   2868  N  N     . PRO A 1 390 ? 116.199 148.676 123.504 1.00 12730. ? 390 PRO A N     1 
ATOM   2869  C  CA    . PRO A 1 390 ? 116.610 149.813 122.668 1.00 12732. ? 390 PRO A CA    1 
ATOM   2870  C  C     . PRO A 1 390 ? 117.315 150.876 123.496 1.00 12737. ? 390 PRO A C     1 
ATOM   2871  O  O     . PRO A 1 390 ? 116.685 151.608 124.265 1.00 12743. ? 390 PRO A O     1 
ATOM   2872  C  CB    . PRO A 1 390 ? 115.280 150.318 122.092 1.00 12733. ? 390 PRO A CB    1 
ATOM   2873  C  CG    . PRO A 1 390 ? 114.245 149.904 123.070 1.00 12741. ? 390 PRO A CG    1 
ATOM   2874  C  CD    . PRO A 1 390 ? 114.815 148.856 123.985 1.00 12742. ? 390 PRO A CD    1 
ATOM   2875  N  N     . PHE A 1 391 ? 118.632 150.966 123.336 1.00 12740. ? 391 PHE A N     1 
ATOM   2876  C  CA    . PHE A 1 391 ? 119.406 151.960 124.059 1.00 12737. ? 391 PHE A CA    1 
ATOM   2877  C  C     . PHE A 1 391 ? 119.269 153.328 123.398 1.00 12741. ? 391 PHE A C     1 
ATOM   2878  O  O     . PHE A 1 391 ? 118.811 153.456 122.260 1.00 12747. ? 391 PHE A O     1 
ATOM   2879  C  CB    . PHE A 1 391 ? 120.883 151.568 124.121 1.00 12737. ? 391 PHE A CB    1 
ATOM   2880  C  CG    . PHE A 1 391 ? 121.162 150.365 124.976 1.00 12741. ? 391 PHE A CG    1 
ATOM   2881  C  CD1   . PHE A 1 391 ? 120.207 149.870 125.844 1.00 12747. ? 391 PHE A CD1   1 
ATOM   2882  C  CD2   . PHE A 1 391 ? 122.389 149.731 124.910 1.00 12751. ? 391 PHE A CD2   1 
ATOM   2883  C  CE1   . PHE A 1 391 ? 120.473 148.765 126.625 1.00 12747. ? 391 PHE A CE1   1 
ATOM   2884  C  CE2   . PHE A 1 391 ? 122.657 148.627 125.688 1.00 12744. ? 391 PHE A CE2   1 
ATOM   2885  C  CZ    . PHE A 1 391 ? 121.698 148.143 126.546 1.00 12742. ? 391 PHE A CZ    1 
ATOM   2886  N  N     . ARG A 1 392 ? 119.671 154.358 124.134 1.00 12741. ? 392 ARG A N     1 
ATOM   2887  C  CA    . ARG A 1 392 ? 119.679 155.713 123.605 1.00 12734. ? 392 ARG A CA    1 
ATOM   2888  C  C     . ARG A 1 392 ? 120.933 155.942 122.773 1.00 12737. ? 392 ARG A C     1 
ATOM   2889  O  O     . ARG A 1 392 ? 122.027 155.507 123.142 1.00 12754. ? 392 ARG A O     1 
ATOM   2890  C  CB    . ARG A 1 392 ? 119.609 156.730 124.742 1.00 12739. ? 392 ARG A CB    1 
ATOM   2891  C  CG    . ARG A 1 392 ? 119.659 158.175 124.292 1.00 12741. ? 392 ARG A CG    1 
ATOM   2892  C  CD    . ARG A 1 392 ? 119.007 159.090 125.311 1.00 12740. ? 392 ARG A CD    1 
ATOM   2893  N  NE    . ARG A 1 392 ? 119.829 160.260 125.592 1.00 12740. ? 392 ARG A NE    1 
ATOM   2894  C  CZ    . ARG A 1 392 ? 120.724 160.331 126.568 1.00 12747. ? 392 ARG A CZ    1 
ATOM   2895  N  NH1   . ARG A 1 392 ? 120.946 159.309 127.377 1.00 12745. ? 392 ARG A NH1   1 
ATOM   2896  N  NH2   . ARG A 1 392 ? 121.414 161.455 126.735 1.00 12763. ? 392 ARG A NH2   1 
ATOM   2897  N  N     . ARG A 1 393 ? 120.768 156.619 121.641 1.00 12730. ? 393 ARG A N     1 
ATOM   2898  C  CA    . ARG A 1 393 ? 121.870 156.936 120.744 1.00 12737. ? 393 ARG A CA    1 
ATOM   2899  C  C     . ARG A 1 393 ? 121.935 158.441 120.551 1.00 12737. ? 393 ARG A C     1 
ATOM   2900  O  O     . ARG A 1 393 ? 120.922 159.075 120.240 1.00 12744. ? 393 ARG A O     1 
ATOM   2901  C  CB    . ARG A 1 393 ? 121.698 156.234 119.398 1.00 12738. ? 393 ARG A CB    1 
ATOM   2902  C  CG    . ARG A 1 393 ? 121.513 154.739 119.524 1.00 12736. ? 393 ARG A CG    1 
ATOM   2903  C  CD    . ARG A 1 393 ? 120.315 154.264 118.727 1.00 12738. ? 393 ARG A CD    1 
ATOM   2904  N  NE    . ARG A 1 393 ? 120.280 152.813 118.605 1.00 12735. ? 393 ARG A NE    1 
ATOM   2905  C  CZ    . ARG A 1 393 ? 120.526 152.146 117.486 1.00 12741. ? 393 ARG A CZ    1 
ATOM   2906  N  NH1   . ARG A 1 393 ? 120.825 152.772 116.360 1.00 12748. ? 393 ARG A NH1   1 
ATOM   2907  N  NH2   . ARG A 1 393 ? 120.471 150.817 117.497 1.00 12748. ? 393 ARG A NH2   1 
ATOM   2908  N  N     . ILE A 1 394 ? 123.122 159.008 120.740 1.00 12738. ? 394 ILE A N     1 
ATOM   2909  C  CA    . ILE A 1 394 ? 123.347 160.437 120.580 1.00 12762. ? 394 ILE A CA    1 
ATOM   2910  C  C     . ILE A 1 394 ? 124.587 160.649 119.724 1.00 12801. ? 394 ILE A C     1 
ATOM   2911  O  O     . ILE A 1 394 ? 125.570 159.909 119.842 1.00 12803. ? 394 ILE A O     1 
ATOM   2912  C  CB    . ILE A 1 394 ? 123.491 161.151 121.942 1.00 12776. ? 394 ILE A CB    1 
ATOM   2913  C  CG1   . ILE A 1 394 ? 124.686 160.603 122.722 1.00 12766. ? 394 ILE A CG1   1 
ATOM   2914  C  CG2   . ILE A 1 394 ? 122.213 161.027 122.753 1.00 12779. ? 394 ILE A CG2   1 
ATOM   2915  C  CD1   . ILE A 1 394 ? 124.885 161.260 124.067 1.00 12768. ? 394 ILE A CD1   1 
ATOM   2916  N  N     . ASN A 1 395 ? 124.529 161.644 118.844 1.00 14122. ? 395 ASN A N     1 
ATOM   2917  C  CA    . ASN A 1 395 ? 125.687 162.063 118.069 1.00 14157. ? 395 ASN A CA    1 
ATOM   2918  C  C     . ASN A 1 395 ? 126.471 163.086 118.877 1.00 14200. ? 395 ASN A C     1 
ATOM   2919  O  O     . ASN A 1 395 ? 125.882 163.983 119.486 1.00 14245. ? 395 ASN A O     1 
ATOM   2920  C  CB    . ASN A 1 395 ? 125.260 162.653 116.726 1.00 14203. ? 395 ASN A CB    1 
ATOM   2921  C  CG    . ASN A 1 395 ? 124.828 161.593 115.737 1.00 14179. ? 395 ASN A CG    1 
ATOM   2922  O  OD1   . ASN A 1 395 ? 124.760 160.411 116.068 1.00 14153. ? 395 ASN A OD1   1 
ATOM   2923  N  ND2   . ASN A 1 395 ? 124.532 162.012 114.513 1.00 14193. ? 395 ASN A ND2   1 
ATOM   2924  N  N     . MET A 1 396 ? 127.797 162.943 118.889 1.00 14624. ? 396 MET A N     1 
ATOM   2925  C  CA    . MET A 1 396 ? 128.618 163.771 119.767 1.00 14654. ? 396 MET A CA    1 
ATOM   2926  C  C     . MET A 1 396 ? 128.515 165.249 119.416 1.00 14715. ? 396 MET A C     1 
ATOM   2927  O  O     . MET A 1 396 ? 128.324 166.091 120.299 1.00 14732. ? 396 MET A O     1 
ATOM   2928  C  CB    . MET A 1 396 ? 130.073 163.315 119.719 1.00 14645. ? 396 MET A CB    1 
ATOM   2929  C  CG    . MET A 1 396 ? 130.867 163.759 120.928 1.00 14653. ? 396 MET A CG    1 
ATOM   2930  S  SD    . MET A 1 396 ? 132.534 163.101 120.926 1.00 14629. ? 396 MET A SD    1 
ATOM   2931  C  CE    . MET A 1 396 ? 132.151 161.362 120.914 1.00 14610. ? 396 MET A CE    1 
ATOM   2932  N  N     . VAL A 1 397 ? 128.648 165.589 118.135 1.00 15843. ? 397 VAL A N     1 
ATOM   2933  C  CA    . VAL A 1 397 ? 128.753 166.996 117.758 1.00 15885. ? 397 VAL A CA    1 
ATOM   2934  C  C     . VAL A 1 397 ? 127.436 167.722 118.007 1.00 15933. ? 397 VAL A C     1 
ATOM   2935  O  O     . VAL A 1 397 ? 127.409 168.804 118.605 1.00 15952. ? 397 VAL A O     1 
ATOM   2936  C  CB    . VAL A 1 397 ? 129.205 167.126 116.294 1.00 15908. ? 397 VAL A CB    1 
ATOM   2937  C  CG1   . VAL A 1 397 ? 129.349 168.591 115.918 1.00 15935. ? 397 VAL A CG1   1 
ATOM   2938  C  CG2   . VAL A 1 397 ? 130.515 166.387 116.083 1.00 15888. ? 397 VAL A CG2   1 
ATOM   2939  N  N     . GLU A 1 398 ? 126.322 167.134 117.565 1.00 16690. ? 398 GLU A N     1 
ATOM   2940  C  CA    . GLU A 1 398 ? 125.030 167.796 117.713 1.00 16725. ? 398 GLU A CA    1 
ATOM   2941  C  C     . GLU A 1 398 ? 124.631 167.925 119.178 1.00 16716. ? 398 GLU A C     1 
ATOM   2942  O  O     . GLU A 1 398 ? 124.169 168.987 119.613 1.00 16744. ? 398 GLU A O     1 
ATOM   2943  C  CB    . GLU A 1 398 ? 123.961 167.036 116.931 1.00 16735. ? 398 GLU A CB    1 
ATOM   2944  C  CG    . GLU A 1 398 ? 124.170 167.047 115.426 1.00 16742. ? 398 GLU A CG    1 
ATOM   2945  C  CD    . GLU A 1 398 ? 125.066 165.920 114.950 1.00 16723. ? 398 GLU A CD    1 
ATOM   2946  O  OE1   . GLU A 1 398 ? 126.232 165.856 115.393 1.00 16707. ? 398 GLU A OE1   1 
ATOM   2947  O  OE2   . GLU A 1 398 ? 124.604 165.098 114.131 1.00 16730. ? 398 GLU A OE2   1 
ATOM   2948  N  N     . GLU A 1 399 ? 124.803 166.855 119.957 1.00 16259. ? 399 GLU A N     1 
ATOM   2949  C  CA    . GLU A 1 399 ? 124.449 166.914 121.370 1.00 16256. ? 399 GLU A CA    1 
ATOM   2950  C  C     . GLU A 1 399 ? 125.367 167.860 122.130 1.00 16251. ? 399 GLU A C     1 
ATOM   2951  O  O     . GLU A 1 399 ? 124.932 168.537 123.067 1.00 16274. ? 399 GLU A O     1 
ATOM   2952  C  CB    . GLU A 1 399 ? 124.485 165.516 121.980 1.00 16229. ? 399 GLU A CB    1 
ATOM   2953  C  CG    . GLU A 1 399 ? 123.243 164.700 121.696 1.00 16217. ? 399 GLU A CG    1 
ATOM   2954  C  CD    . GLU A 1 399 ? 122.015 165.250 122.392 1.00 16255. ? 399 GLU A CD    1 
ATOM   2955  O  OE1   . GLU A 1 399 ? 122.031 165.354 123.636 1.00 16254. ? 399 GLU A OE1   1 
ATOM   2956  O  OE2   . GLU A 1 399 ? 121.031 165.577 121.695 1.00 16271. ? 399 GLU A OE2   1 
ATOM   2957  N  N     . LEU A 1 400 ? 126.644 167.918 121.747 1.00 15831. ? 400 LEU A N     1 
ATOM   2958  C  CA    . LEU A 1 400 ? 127.554 168.870 122.371 1.00 15830. ? 400 LEU A CA    1 
ATOM   2959  C  C     . LEU A 1 400 ? 127.149 170.302 122.056 1.00 15890. ? 400 LEU A C     1 
ATOM   2960  O  O     . LEU A 1 400 ? 127.237 171.182 122.918 1.00 15890. ? 400 LEU A O     1 
ATOM   2961  C  CB    . LEU A 1 400 ? 128.987 168.604 121.919 1.00 15813. ? 400 LEU A CB    1 
ATOM   2962  C  CG    . LEU A 1 400 ? 130.068 169.097 122.881 1.00 15811. ? 400 LEU A CG    1 
ATOM   2963  C  CD1   . LEU A 1 400 ? 129.850 168.517 124.265 1.00 15796. ? 400 LEU A CD1   1 
ATOM   2964  C  CD2   . LEU A 1 400 ? 131.445 168.741 122.361 1.00 15809. ? 400 LEU A CD2   1 
ATOM   2965  N  N     . GLU A 1 401 ? 126.712 170.558 120.821 1.00 17575. ? 401 GLU A N     1 
ATOM   2966  C  CA    . GLU A 1 401 ? 126.207 171.883 120.480 1.00 17628. ? 401 GLU A CA    1 
ATOM   2967  C  C     . GLU A 1 401 ? 124.971 172.222 121.302 1.00 17614. ? 401 GLU A C     1 
ATOM   2968  O  O     . GLU A 1 401 ? 124.816 173.351 121.780 1.00 17651. ? 401 GLU A O     1 
ATOM   2969  C  CB    . GLU A 1 401 ? 125.894 171.961 118.985 1.00 17653. ? 401 GLU A CB    1 
ATOM   2970  C  CG    . GLU A 1 401 ? 127.115 171.933 118.085 1.00 17673. ? 401 GLU A CG    1 
ATOM   2971  C  CD    . GLU A 1 401 ? 126.750 171.983 116.614 1.00 17683. ? 401 GLU A CD    1 
ATOM   2972  O  OE1   . GLU A 1 401 ? 125.540 171.984 116.302 1.00 17676. ? 401 GLU A OE1   1 
ATOM   2973  O  OE2   . GLU A 1 401 ? 127.670 172.022 115.771 1.00 17697. ? 401 GLU A OE2   1 
ATOM   2974  N  N     . LYS A 1 402 ? 124.072 171.250 121.468 1.00 16601. ? 402 LYS A N     1 
ATOM   2975  C  CA    . LYS A 1 402 ? 122.863 171.485 122.253 1.00 16588. ? 402 LYS A CA    1 
ATOM   2976  C  C     . LYS A 1 402 ? 123.199 171.788 123.709 1.00 16587. ? 402 LYS A C     1 
ATOM   2977  O  O     . LYS A 1 402 ? 122.639 172.713 124.308 1.00 16590. ? 402 LYS A O     1 
ATOM   2978  C  CB    . LYS A 1 402 ? 121.933 170.277 122.158 1.00 16581. ? 402 LYS A CB    1 
ATOM   2979  C  CG    . LYS A 1 402 ? 121.302 170.085 120.791 1.00 16577. ? 402 LYS A CG    1 
ATOM   2980  C  CD    . LYS A 1 402 ? 120.444 168.831 120.751 1.00 16572. ? 402 LYS A CD    1 
ATOM   2981  C  CE    . LYS A 1 402 ? 119.546 168.733 121.974 1.00 16570. ? 402 LYS A CE    1 
ATOM   2982  N  NZ    . LYS A 1 402 ? 118.625 169.898 122.085 1.00 16570. ? 402 LYS A NZ    1 
ATOM   2983  N  N     . ALA A 1 403 ? 124.117 171.015 124.270 1.00 16537. ? 403 ALA A N     1 
ATOM   2984  C  CA    . ALA A 1 403 ? 124.499 171.235 125.678 1.00 16539. ? 403 ALA A CA    1 
ATOM   2985  C  C     . ALA A 1 403 ? 125.368 172.483 125.771 1.00 16555. ? 403 ALA A C     1 
ATOM   2986  O  O     . ALA A 1 403 ? 124.933 173.455 126.404 1.00 16553. ? 403 ALA A O     1 
ATOM   2987  C  CB    . ALA A 1 403 ? 125.219 170.038 126.209 1.00 16523. ? 403 ALA A CB    1 
ATOM   2988  N  N     . LEU A 1 404 ? 126.544 172.479 125.147 1.00 17145. ? 404 LEU A N     1 
ATOM   2989  C  CA    . LEU A 1 404 ? 127.460 173.637 125.308 1.00 17174. ? 404 LEU A CA    1 
ATOM   2990  C  C     . LEU A 1 404 ? 126.626 174.899 125.110 1.00 17221. ? 404 LEU A C     1 
ATOM   2991  O  O     . LEU A 1 404 ? 126.882 175.889 125.812 1.00 17219. ? 404 LEU A O     1 
ATOM   2992  C  CB    . LEU A 1 404 ? 128.639 173.593 124.344 1.00 17190. ? 404 LEU A CB    1 
ATOM   2993  C  CG    . LEU A 1 404 ? 129.855 172.808 124.833 1.00 17155. ? 404 LEU A CG    1 
ATOM   2994  C  CD1   . LEU A 1 404 ? 130.908 172.774 123.747 1.00 17166. ? 404 LEU A CD1   1 
ATOM   2995  C  CD2   . LEU A 1 404 ? 130.389 173.493 126.071 1.00 17170. ? 404 LEU A CD2   1 
ATOM   2996  N  N     . GLY A 1 405 ? 125.665 174.855 124.192 1.00 18979. ? 405 GLY A N     1 
ATOM   2997  C  CA    . GLY A 1 405 ? 124.751 175.996 124.022 1.00 19036. ? 405 GLY A CA    1 
ATOM   2998  C  C     . GLY A 1 405 ? 125.052 176.781 122.768 1.00 19074. ? 405 GLY A C     1 
ATOM   2999  O  O     . GLY A 1 405 ? 124.166 177.532 122.325 1.00 19074. ? 405 GLY A O     1 
ATOM   3000  N  N     . MET A 1 406 ? 126.241 176.614 122.195 1.00 20182. ? 406 MET A N     1 
ATOM   3001  C  CA    . MET A 1 406 ? 126.609 177.455 121.032 1.00 20211. ? 406 MET A CA    1 
ATOM   3002  C  C     . MET A 1 406 ? 126.805 176.580 119.793 1.00 20207. ? 406 MET A C     1 
ATOM   3003  O  O     . MET A 1 406 ? 126.463 175.388 119.850 1.00 20192. ? 406 MET A O     1 
ATOM   3004  C  CB    . MET A 1 406 ? 127.920 178.187 121.301 1.00 20220. ? 406 MET A CB    1 
ATOM   3005  C  CG    . MET A 1 406 ? 129.133 177.286 121.293 1.00 20219. ? 406 MET A CG    1 
ATOM   3006  S  SD    . MET A 1 406 ? 130.613 178.250 120.930 1.00 20222. ? 406 MET A SD    1 
ATOM   3007  C  CE    . MET A 1 406 ? 130.041 179.246 119.546 1.00 20229. ? 406 MET A CE    1 
ATOM   3008  N  N     . LYS A 1 407 ? 127.331 177.168 118.720 1.00 19785. ? 407 LYS A N     1 
ATOM   3009  C  CA    . LYS A 1 407 ? 127.550 176.402 117.472 1.00 19766. ? 407 LYS A CA    1 
ATOM   3010  C  C     . LYS A 1 407 ? 129.045 176.159 117.264 1.00 19756. ? 407 LYS A C     1 
ATOM   3011  O  O     . LYS A 1 407 ? 129.748 177.094 116.851 1.00 19770. ? 407 LYS A O     1 
ATOM   3012  C  CB    . LYS A 1 407 ? 126.993 177.157 116.266 1.00 19776. ? 407 LYS A CB    1 
ATOM   3013  C  CG    . LYS A 1 407 ? 125.538 176.869 115.940 1.00 19780. ? 407 LYS A CG    1 
ATOM   3014  C  CD    . LYS A 1 407 ? 125.308 175.407 115.580 1.00 19763. ? 407 LYS A CD    1 
ATOM   3015  C  CE    . LYS A 1 407 ? 126.166 174.969 114.437 1.00 19764. ? 407 LYS A CE    1 
ATOM   3016  N  NZ    . LYS A 1 407 ? 125.902 175.760 113.233 1.00 19776. ? 407 LYS A NZ    1 
ATOM   3017  N  N     . LEU A 1 408 ? 129.499 174.935 117.510 1.00 19129. ? 408 LEU A N     1 
ATOM   3018  C  CA    . LEU A 1 408 ? 130.919 174.605 117.261 1.00 19125. ? 408 LEU A CA    1 
ATOM   3019  C  C     . LEU A 1 408 ? 131.129 174.583 115.746 1.00 19126. ? 408 LEU A C     1 
ATOM   3020  O  O     . LEU A 1 408 ? 130.126 174.500 115.015 1.00 19123. ? 408 LEU A O     1 
ATOM   3021  C  CB    . LEU A 1 408 ? 131.258 173.266 117.907 1.00 19115. ? 408 LEU A CB    1 
ATOM   3022  C  CG    . LEU A 1 408 ? 131.270 173.241 119.437 1.00 19115. ? 408 LEU A CG    1 
ATOM   3023  C  CD1   . LEU A 1 408 ? 131.917 174.499 119.981 1.00 19123. ? 408 LEU A CD1   1 
ATOM   3024  C  CD2   . LEU A 1 408 ? 129.886 173.048 120.021 1.00 19105. ? 408 LEU A CD2   1 
ATOM   3025  N  N     . PRO A 1 409 ? 132.372 174.680 115.241 1.00 19493. ? 409 PRO A N     1 
ATOM   3026  C  CA    . PRO A 1 409 ? 132.589 174.743 113.806 1.00 19502. ? 409 PRO A CA    1 
ATOM   3027  C  C     . PRO A 1 409 ? 132.061 173.541 113.048 1.00 19500. ? 409 PRO A C     1 
ATOM   3028  O  O     . PRO A 1 409 ? 131.687 172.545 113.685 1.00 19495. ? 409 PRO A O     1 
ATOM   3029  C  CB    . PRO A 1 409 ? 134.110 174.798 113.766 1.00 19508. ? 409 PRO A CB    1 
ATOM   3030  C  CG    . PRO A 1 409 ? 134.488 175.484 115.048 1.00 19512. ? 409 PRO A CG    1 
ATOM   3031  C  CD    . PRO A 1 409 ? 133.584 174.777 116.028 1.00 19503. ? 409 PRO A CD    1 
ATOM   3032  N  N     . GLU A 1 410 ? 132.037 173.610 111.714 1.00 19411. ? 410 GLU A N     1 
ATOM   3033  C  CA    . GLU A 1 410 ? 131.642 172.446 110.935 1.00 19399. ? 410 GLU A CA    1 
ATOM   3034  C  C     . GLU A 1 410 ? 132.648 171.314 111.109 1.00 19379. ? 410 GLU A C     1 
ATOM   3035  O  O     . GLU A 1 410 ? 133.807 171.530 111.473 1.00 19391. ? 410 GLU A O     1 
ATOM   3036  C  CB    . GLU A 1 410 ? 131.506 172.814 109.459 1.00 19405. ? 410 GLU A CB    1 
ATOM   3037  C  CG    . GLU A 1 410 ? 130.345 173.746 109.172 1.00 19412. ? 410 GLU A CG    1 
ATOM   3038  C  CD    . GLU A 1 410 ? 129.052 173.272 109.804 1.00 19415. ? 410 GLU A CD    1 
ATOM   3039  O  OE1   . GLU A 1 410 ? 128.662 172.109 109.566 1.00 19417. ? 410 GLU A OE1   1 
ATOM   3040  O  OE2   . GLU A 1 410 ? 128.427 174.061 110.542 1.00 19418. ? 410 GLU A OE2   1 
ATOM   3041  N  N     . THR A 1 411 ? 132.188 170.093 110.834 1.00 18050. ? 411 THR A N     1 
ATOM   3042  C  CA    . THR A 1 411 ? 132.968 168.898 111.129 1.00 18026. ? 411 THR A CA    1 
ATOM   3043  C  C     . THR A 1 411 ? 134.257 168.807 110.323 1.00 18009. ? 411 THR A C     1 
ATOM   3044  O  O     . THR A 1 411 ? 135.138 168.022 110.689 1.00 17992. ? 411 THR A O     1 
ATOM   3045  C  CB    . THR A 1 411 ? 132.117 167.652 110.887 1.00 17943. ? 411 THR A CB    1 
ATOM   3046  O  OG1   . THR A 1 411 ? 131.581 167.688 109.558 1.00 17958. ? 411 THR A OG1   1 
ATOM   3047  C  CG2   . THR A 1 411 ? 130.976 167.589 111.884 1.00 17963. ? 411 THR A CG2   1 
ATOM   3048  N  N     . ASN A 1 412 ? 134.395 169.579 109.248 1.00 18819. ? 412 ASN A N     1 
ATOM   3049  C  CA    . ASN A 1 412 ? 135.622 169.559 108.463 1.00 18837. ? 412 ASN A CA    1 
ATOM   3050  C  C     . ASN A 1 412 ? 136.659 170.560 108.953 1.00 18868. ? 412 ASN A C     1 
ATOM   3051  O  O     . ASN A 1 412 ? 137.825 170.476 108.549 1.00 18871. ? 412 ASN A O     1 
ATOM   3052  C  CB    . ASN A 1 412 ? 135.311 169.826 106.989 1.00 18842. ? 412 ASN A CB    1 
ATOM   3053  C  CG    . ASN A 1 412 ? 134.405 171.024 106.793 1.00 18848. ? 412 ASN A CG    1 
ATOM   3054  O  OD1   . ASN A 1 412 ? 133.987 171.662 107.757 1.00 18854. ? 412 ASN A OD1   1 
ATOM   3055  N  ND2   . ASN A 1 412 ? 134.099 171.337 105.540 1.00 18849. ? 412 ASN A ND2   1 
ATOM   3056  N  N     . LEU A 1 413 ? 136.271 171.504 109.807 1.00 19227. ? 413 LEU A N     1 
ATOM   3057  C  CA    . LEU A 1 413 ? 137.165 172.567 110.248 1.00 19243. ? 413 LEU A CA    1 
ATOM   3058  C  C     . LEU A 1 413 ? 137.763 172.329 111.630 1.00 19258. ? 413 LEU A C     1 
ATOM   3059  O  O     . LEU A 1 413 ? 138.382 173.244 112.180 1.00 19274. ? 413 LEU A O     1 
ATOM   3060  C  CB    . LEU A 1 413 ? 136.437 173.915 110.234 1.00 19247. ? 413 LEU A CB    1 
ATOM   3061  C  CG    . LEU A 1 413 ? 135.499 174.225 109.069 1.00 19246. ? 413 LEU A CG    1 
ATOM   3062  C  CD1   . LEU A 1 413 ? 134.993 175.651 109.174 1.00 19252. ? 413 LEU A CD1   1 
ATOM   3063  C  CD2   . LEU A 1 413 ? 136.209 174.015 107.742 1.00 19249. ? 413 LEU A CD2   1 
ATOM   3064  N  N     . PHE A 1 414 ? 137.592 171.139 112.210 1.00 19263. ? 414 PHE A N     1 
ATOM   3065  C  CA    . PHE A 1 414 ? 138.165 170.888 113.530 1.00 19267. ? 414 PHE A CA    1 
ATOM   3066  C  C     . PHE A 1 414 ? 139.688 170.914 113.500 1.00 19270. ? 414 PHE A C     1 
ATOM   3067  O  O     . PHE A 1 414 ? 140.328 171.240 114.507 1.00 19268. ? 414 PHE A O     1 
ATOM   3068  C  CB    . PHE A 1 414 ? 137.664 169.560 114.097 1.00 19250. ? 414 PHE A CB    1 
ATOM   3069  C  CG    . PHE A 1 414 ? 136.265 169.619 114.634 1.00 19241. ? 414 PHE A CG    1 
ATOM   3070  C  CD1   . PHE A 1 414 ? 136.016 170.206 115.863 1.00 19246. ? 414 PHE A CD1   1 
ATOM   3071  C  CD2   . PHE A 1 414 ? 135.205 169.080 113.931 1.00 19237. ? 414 PHE A CD2   1 
ATOM   3072  C  CE1   . PHE A 1 414 ? 134.739 170.265 116.376 1.00 19248. ? 414 PHE A CE1   1 
ATOM   3073  C  CE2   . PHE A 1 414 ? 133.922 169.135 114.442 1.00 19237. ? 414 PHE A CE2   1 
ATOM   3074  C  CZ    . PHE A 1 414 ? 133.690 169.729 115.664 1.00 19242. ? 414 PHE A CZ    1 
ATOM   3075  N  N     . GLU A 1 415 ? 140.290 170.582 112.361 1.00 19320. ? 415 GLU A N     1 
ATOM   3076  C  CA    . GLU A 1 415 ? 141.745 170.498 112.310 1.00 19328. ? 415 GLU A CA    1 
ATOM   3077  C  C     . GLU A 1 415 ? 142.426 171.859 112.219 1.00 19341. ? 415 GLU A C     1 
ATOM   3078  O  O     . GLU A 1 415 ? 143.656 171.915 112.320 1.00 19335. ? 415 GLU A O     1 
ATOM   3079  C  CB    . GLU A 1 415 ? 142.174 169.622 111.133 1.00 19319. ? 415 GLU A CB    1 
ATOM   3080  C  CG    . GLU A 1 415 ? 141.946 168.138 111.367 1.00 19313. ? 415 GLU A CG    1 
ATOM   3081  C  CD    . GLU A 1 415 ? 142.870 167.267 110.540 1.00 19315. ? 415 GLU A CD    1 
ATOM   3082  O  OE1   . GLU A 1 415 ? 142.798 167.333 109.295 1.00 19324. ? 415 GLU A OE1   1 
ATOM   3083  O  OE2   . GLU A 1 415 ? 143.668 166.514 111.137 1.00 19311. ? 415 GLU A OE2   1 
ATOM   3084  N  N     . THR A 1 416 ? 141.631 172.922 112.113 1.00 20251. ? 416 THR A N     1 
ATOM   3085  C  CA    . THR A 1 416 ? 142.191 174.281 111.995 1.00 20277. ? 416 THR A CA    1 
ATOM   3086  C  C     . THR A 1 416 ? 142.482 174.816 113.369 1.00 20298. ? 416 THR A C     1 
ATOM   3087  O  O     . THR A 1 416 ? 141.793 174.407 114.324 1.00 20286. ? 416 THR A O     1 
ATOM   3088  C  CB    . THR A 1 416 ? 141.188 175.187 111.292 1.00 20288. ? 416 THR A CB    1 
ATOM   3089  O  OG1   . THR A 1 416 ? 140.190 175.440 112.276 1.00 20293. ? 416 THR A OG1   1 
ATOM   3090  C  CG2   . THR A 1 416 ? 140.582 174.538 110.061 1.00 20276. ? 416 THR A CG2   1 
ATOM   3091  N  N     . GLU A 1 417 ? 143.487 175.688 113.486 1.00 21013. ? 417 GLU A N     1 
ATOM   3092  C  CA    . GLU A 1 417 ? 143.879 176.235 114.812 1.00 21023. ? 417 GLU A CA    1 
ATOM   3093  C  C     . GLU A 1 417 ? 142.756 177.142 115.336 1.00 21024. ? 417 GLU A C     1 
ATOM   3094  O  O     . GLU A 1 417 ? 142.667 177.321 116.570 1.00 21022. ? 417 GLU A O     1 
ATOM   3095  C  CB    . GLU A 1 417 ? 145.210 176.980 114.710 1.00 21032. ? 417 GLU A CB    1 
ATOM   3096  C  CG    . GLU A 1 417 ? 146.370 176.065 114.329 1.00 21035. ? 417 GLU A CG    1 
ATOM   3097  C  CD    . GLU A 1 417 ? 146.501 174.860 115.242 1.00 21030. ? 417 GLU A CD    1 
ATOM   3098  O  OE1   . GLU A 1 417 ? 146.715 175.059 116.457 1.00 21025. ? 417 GLU A OE1   1 
ATOM   3099  O  OE2   . GLU A 1 417 ? 146.382 173.722 114.741 1.00 21028. ? 417 GLU A OE2   1 
ATOM   3100  N  N     . GLU A 1 418 ? 141.933 177.683 114.433 1.00 21148. ? 418 GLU A N     1 
ATOM   3101  C  CA    . GLU A 1 418 ? 140.790 178.533 114.856 1.00 21150. ? 418 GLU A CA    1 
ATOM   3102  C  C     . GLU A 1 418 ? 139.851 177.694 115.734 1.00 21128. ? 418 GLU A C     1 
ATOM   3103  O  O     . GLU A 1 418 ? 139.442 178.185 116.808 1.00 21126. ? 418 GLU A O     1 
ATOM   3104  C  CB    . GLU A 1 418 ? 140.052 179.089 113.638 1.00 21160. ? 418 GLU A CB    1 
ATOM   3105  C  CG    . GLU A 1 418 ? 138.795 179.873 114.004 1.00 21167. ? 418 GLU A CG    1 
ATOM   3106  C  CD    . GLU A 1 418 ? 139.025 180.973 115.025 1.00 21167. ? 418 GLU A CD    1 
ATOM   3107  O  OE1   . GLU A 1 418 ? 139.836 181.880 114.744 1.00 21171. ? 418 GLU A OE1   1 
ATOM   3108  O  OE2   . GLU A 1 418 ? 138.394 180.922 116.102 1.00 21161. ? 418 GLU A OE2   1 
ATOM   3109  N  N     . THR A 1 419 ? 139.542 176.469 115.299 1.00 20361. ? 419 THR A N     1 
ATOM   3110  C  CA    . THR A 1 419 ? 138.674 175.581 116.100 1.00 20346. ? 419 THR A CA    1 
ATOM   3111  C  C     . THR A 1 419 ? 139.339 175.331 117.435 1.00 20326. ? 419 THR A C     1 
ATOM   3112  O  O     . THR A 1 419 ? 138.655 175.450 118.469 1.00 20322. ? 419 THR A O     1 
ATOM   3113  C  CB    . THR A 1 419 ? 138.419 174.280 115.343 1.00 20333. ? 419 THR A CB    1 
ATOM   3114  O  OG1   . THR A 1 419 ? 137.763 174.678 114.144 1.00 20332. ? 419 THR A OG1   1 
ATOM   3115  C  CG2   . THR A 1 419 ? 137.542 173.320 116.126 1.00 20323. ? 419 THR A CG2   1 
ATOM   3116  N  N     . ARG A 1 420 ? 140.634 175.004 117.421 1.00 19696. ? 420 ARG A N     1 
ATOM   3117  C  CA    . ARG A 1 420 ? 141.381 174.794 118.688 1.00 19678. ? 420 ARG A CA    1 
ATOM   3118  C  C     . ARG A 1 420 ? 141.228 176.045 119.568 1.00 19689. ? 420 ARG A C     1 
ATOM   3119  O  O     . ARG A 1 420 ? 140.974 175.889 120.783 1.00 19676. ? 420 ARG A O     1 
ATOM   3120  C  CB    . ARG A 1 420 ? 142.855 174.491 118.397 1.00 19676. ? 420 ARG A CB    1 
ATOM   3121  C  CG    . ARG A 1 420 ? 143.673 174.160 119.637 1.00 19647. ? 420 ARG A CG    1 
ATOM   3122  C  CD    . ARG A 1 420 ? 145.051 173.629 119.280 1.00 19647. ? 420 ARG A CD    1 
ATOM   3123  N  NE    . ARG A 1 420 ? 145.863 173.359 120.471 1.00 19629. ? 420 ARG A NE    1 
ATOM   3124  C  CZ    . ARG A 1 420 ? 147.094 172.866 120.447 1.00 19641. ? 420 ARG A CZ    1 
ATOM   3125  N  NH1   . ARG A 1 420 ? 147.642 172.515 119.297 1.00 19658. ? 420 ARG A NH1   1 
ATOM   3126  N  NH2   . ARG A 1 420 ? 147.771 172.721 121.572 1.00 19621. ? 420 ARG A NH2   1 
ATOM   3127  N  N     . LYS A 1 421 ? 141.370 177.233 118.972 1.00 20414. ? 421 LYS A N     1 
ATOM   3128  C  CA    . LYS A 1 421 ? 141.268 178.498 119.748 1.00 20419. ? 421 LYS A CA    1 
ATOM   3129  C  C     . LYS A 1 421 ? 139.844 178.648 120.309 1.00 20405. ? 421 LYS A C     1 
ATOM   3130  O  O     . LYS A 1 421 ? 139.712 178.876 121.531 1.00 20411. ? 421 LYS A O     1 
ATOM   3131  C  CB    . LYS A 1 421 ? 141.625 179.710 118.881 1.00 20435. ? 421 LYS A CB    1 
ATOM   3132  C  CG    . LYS A 1 421 ? 141.536 181.036 119.620 1.00 20432. ? 421 LYS A CG    1 
ATOM   3133  C  CD    . LYS A 1 421 ? 142.446 181.078 120.842 1.00 20433. ? 421 LYS A CD    1 
ATOM   3134  C  CE    . LYS A 1 421 ? 141.877 181.900 121.954 1.00 20433. ? 421 LYS A CE    1 
ATOM   3135  N  NZ    . LYS A 1 421 ? 140.647 181.305 122.482 1.00 20428. ? 421 LYS A NZ    1 
ATOM   3136  N  N     . ILE A 1 422 ? 138.823 178.527 119.453 1.00 19728. ? 422 ILE A N     1 
ATOM   3137  C  CA    . ILE A 1 422 ? 137.421 178.738 119.928 1.00 19710. ? 422 ILE A CA    1 
ATOM   3138  C  C     . ILE A 1 422 ? 137.111 177.657 120.975 1.00 19696. ? 422 ILE A C     1 
ATOM   3139  O  O     . ILE A 1 422 ? 136.384 177.967 121.944 1.00 19691. ? 422 ILE A O     1 
ATOM   3140  C  CB    . ILE A 1 422 ? 136.411 178.753 118.763 1.00 19708. ? 422 ILE A CB    1 
ATOM   3141  C  CG1   . ILE A 1 422 ? 135.059 179.314 119.206 1.00 19697. ? 422 ILE A CG1   1 
ATOM   3142  C  CG2   . ILE A 1 422 ? 136.262 177.374 118.121 1.00 19710. ? 422 ILE A CG2   1 
ATOM   3143  C  CD1   . ILE A 1 422 ? 135.141 180.685 119.852 1.00 19698. ? 422 ILE A CD1   1 
ATOM   3144  N  N     . LEU A 1 423 ? 137.654 176.448 120.799 1.00 19232. ? 423 LEU A N     1 
ATOM   3145  C  CA    . LEU A 1 423 ? 137.465 175.413 121.808 1.00 19211. ? 423 LEU A CA    1 
ATOM   3146  C  C     . LEU A 1 423 ? 138.107 175.809 123.130 1.00 19225. ? 423 LEU A C     1 
ATOM   3147  O  O     . LEU A 1 423 ? 137.539 175.576 124.201 1.00 19202. ? 423 LEU A O     1 
ATOM   3148  C  CB    . LEU A 1 423 ? 138.027 174.084 121.309 1.00 19188. ? 423 LEU A CB    1 
ATOM   3149  C  CG    . LEU A 1 423 ? 137.148 173.353 120.296 1.00 19189. ? 423 LEU A CG    1 
ATOM   3150  C  CD1   . LEU A 1 423 ? 137.738 172.001 119.959 1.00 19150. ? 423 LEU A CD1   1 
ATOM   3151  C  CD2   . LEU A 1 423 ? 135.739 173.203 120.840 1.00 19178. ? 423 LEU A CD2   1 
ATOM   3152  N  N     . ASP A 1 424 ? 139.299 176.407 123.076 1.00 20169. ? 424 ASP A N     1 
ATOM   3153  C  CA    . ASP A 1 424 ? 139.952 176.866 124.295 1.00 20172. ? 424 ASP A CA    1 
ATOM   3154  C  C     . ASP A 1 424 ? 139.140 177.970 124.962 1.00 20182. ? 424 ASP A C     1 
ATOM   3155  O  O     . ASP A 1 424 ? 138.989 177.999 126.189 1.00 20175. ? 424 ASP A O     1 
ATOM   3156  C  CB    . ASP A 1 424 ? 141.368 177.348 123.979 1.00 20191. ? 424 ASP A CB    1 
ATOM   3157  C  CG    . ASP A 1 424 ? 141.952 178.199 125.086 1.00 20194. ? 424 ASP A CG    1 
ATOM   3158  O  OD1   . ASP A 1 424 ? 142.151 177.670 126.199 1.00 20178. ? 424 ASP A OD1   1 
ATOM   3159  O  OD2   . ASP A 1 424 ? 142.209 179.396 124.844 1.00 20205. ? 424 ASP A OD2   1 
ATOM   3160  N  N     . ASP A 1 425 ? 138.602 178.887 124.158 1.00 20088. ? 425 ASP A N     1 
ATOM   3161  C  CA    . ASP A 1 425 ? 137.770 179.960 124.686 1.00 20087. ? 425 ASP A CA    1 
ATOM   3162  C  C     . ASP A 1 425 ? 136.536 179.392 125.373 1.00 20064. ? 425 ASP A C     1 
ATOM   3163  O  O     . ASP A 1 425 ? 136.161 179.842 126.460 1.00 20060. ? 425 ASP A O     1 
ATOM   3164  C  CB    . ASP A 1 425 ? 137.361 180.920 123.569 1.00 20094. ? 425 ASP A CB    1 
ATOM   3165  C  CG    . ASP A 1 425 ? 136.188 181.796 123.957 1.00 20093. ? 425 ASP A CG    1 
ATOM   3166  O  OD1   . ASP A 1 425 ? 136.264 182.462 125.011 1.00 20092. ? 425 ASP A OD1   1 
ATOM   3167  O  OD2   . ASP A 1 425 ? 135.187 181.816 123.209 1.00 20091. ? 425 ASP A OD2   1 
ATOM   3168  N  N     . ILE A 1 426 ? 135.899 178.403 124.744 1.00 19499. ? 426 ILE A N     1 
ATOM   3169  C  CA    . ILE A 1 426 ? 134.709 177.796 125.332 1.00 19488. ? 426 ILE A CA    1 
ATOM   3170  C  C     . ILE A 1 426 ? 135.058 177.061 126.620 1.00 19471. ? 426 ILE A C     1 
ATOM   3171  O  O     . ILE A 1 426 ? 134.334 177.156 127.619 1.00 19460. ? 426 ILE A O     1 
ATOM   3172  C  CB    . ILE A 1 426 ? 134.022 176.873 124.310 1.00 19484. ? 426 ILE A CB    1 
ATOM   3173  C  CG1   . ILE A 1 426 ? 133.051 177.684 123.456 1.00 19488. ? 426 ILE A CG1   1 
ATOM   3174  C  CG2   . ILE A 1 426 ? 133.303 175.727 125.007 1.00 19452. ? 426 ILE A CG2   1 
ATOM   3175  C  CD1   . ILE A 1 426 ? 131.736 177.959 124.144 1.00 19483. ? 426 ILE A CD1   1 
ATOM   3176  N  N     . CYS A 1 427 ? 136.170 176.322 126.623 1.00 19324. ? 427 CYS A N     1 
ATOM   3177  C  CA    . CYS A 1 427 ? 136.582 175.603 127.824 1.00 19307. ? 427 CYS A CA    1 
ATOM   3178  C  C     . CYS A 1 427 ? 136.843 176.563 128.975 1.00 19300. ? 427 CYS A C     1 
ATOM   3179  O  O     . CYS A 1 427 ? 136.445 176.299 130.116 1.00 19292. ? 427 CYS A O     1 
ATOM   3180  C  CB    . CYS A 1 427 ? 137.829 174.768 127.534 1.00 19301. ? 427 CYS A CB    1 
ATOM   3181  S  SG    . CYS A 1 427 ? 137.509 173.020 127.223 1.00 19259. ? 427 CYS A SG    1 
ATOM   3182  N  N     . VAL A 1 428 ? 137.512 177.682 128.697 1.00 19074. ? 428 VAL A N     1 
ATOM   3183  C  CA    . VAL A 1 428 ? 137.766 178.669 129.742 1.00 19064. ? 428 VAL A CA    1 
ATOM   3184  C  C     . VAL A 1 428 ? 136.459 179.290 130.221 1.00 19055. ? 428 VAL A C     1 
ATOM   3185  O  O     . VAL A 1 428 ? 136.239 179.451 131.427 1.00 19055. ? 428 VAL A O     1 
ATOM   3186  C  CB    . VAL A 1 428 ? 138.755 179.734 129.235 1.00 19068. ? 428 VAL A CB    1 
ATOM   3187  C  CG1   . VAL A 1 428 ? 138.577 181.039 129.993 1.00 19063. ? 428 VAL A CG1   1 
ATOM   3188  C  CG2   . VAL A 1 428 ? 140.183 179.228 129.360 1.00 19067. ? 428 VAL A CG2   1 
ATOM   3189  N  N     . ALA A 1 429 ? 135.570 179.641 129.289 1.00 18684. ? 429 ALA A N     1 
ATOM   3190  C  CA    . ALA A 1 429 ? 134.317 180.288 129.664 1.00 18669. ? 429 ALA A CA    1 
ATOM   3191  C  C     . ALA A 1 429 ? 133.427 179.360 130.482 1.00 18669. ? 429 ALA A C     1 
ATOM   3192  O  O     . ALA A 1 429 ? 132.811 179.790 131.465 1.00 18667. ? 429 ALA A O     1 
ATOM   3193  C  CB    . ALA A 1 429 ? 133.582 180.770 128.414 1.00 18671. ? 429 ALA A CB    1 
ATOM   3194  N  N     . LYS A 1 430 ? 133.345 178.086 130.099 1.00 18840. ? 430 LYS A N     1 
ATOM   3195  C  CA    . LYS A 1 430 ? 132.482 177.126 130.775 1.00 18841. ? 430 LYS A CA    1 
ATOM   3196  C  C     . LYS A 1 430 ? 133.116 176.529 132.025 1.00 18836. ? 430 LYS A C     1 
ATOM   3197  O  O     . LYS A 1 430 ? 132.618 175.512 132.524 1.00 18835. ? 430 LYS A O     1 
ATOM   3198  C  CB    . LYS A 1 430 ? 132.077 176.009 129.811 1.00 18832. ? 430 LYS A CB    1 
ATOM   3199  C  CG    . LYS A 1 430 ? 130.980 176.397 128.832 1.00 18823. ? 430 LYS A CG    1 
ATOM   3200  C  CD    . LYS A 1 430 ? 129.953 177.310 129.481 1.00 18831. ? 430 LYS A CD    1 
ATOM   3201  C  CE    . LYS A 1 430 ? 128.796 177.598 128.540 1.00 18829. ? 430 LYS A CE    1 
ATOM   3202  N  NZ    . LYS A 1 430 ? 127.950 176.394 128.313 1.00 18811. ? 430 LYS A NZ    1 
ATOM   3203  N  N     . ALA A 1 431 ? 134.191 177.133 132.533 1.00 18635. ? 431 ALA A N     1 
ATOM   3204  C  CA    . ALA A 1 431 ? 134.854 176.690 133.760 1.00 18628. ? 431 ALA A CA    1 
ATOM   3205  C  C     . ALA A 1 431 ? 135.298 175.233 133.679 1.00 18624. ? 431 ALA A C     1 
ATOM   3206  O  O     . ALA A 1 431 ? 135.200 174.488 134.657 1.00 18622. ? 431 ALA A O     1 
ATOM   3207  C  CB    . ALA A 1 431 ? 133.961 176.908 134.984 1.00 18627. ? 431 ALA A CB    1 
ATOM   3208  N  N     . VAL A 1 432 ? 135.785 174.813 132.516 1.00 18509. ? 432 VAL A N     1 
ATOM   3209  C  CA    . VAL A 1 432 ? 136.322 173.471 132.323 1.00 18504. ? 432 VAL A CA    1 
ATOM   3210  C  C     . VAL A 1 432 ? 137.838 173.558 132.290 1.00 18510. ? 432 VAL A C     1 
ATOM   3211  O  O     . VAL A 1 432 ? 138.409 174.436 131.631 1.00 18515. ? 432 VAL A O     1 
ATOM   3212  C  CB    . VAL A 1 432 ? 135.776 172.828 131.035 1.00 18500. ? 432 VAL A CB    1 
ATOM   3213  C  CG1   . VAL A 1 432 ? 135.982 171.324 131.069 1.00 18468. ? 432 VAL A CG1   1 
ATOM   3214  C  CG2   . VAL A 1 432 ? 134.305 173.161 130.861 1.00 18473. ? 432 VAL A CG2   1 
ATOM   3215  N  N     . GLU A 1 433 ? 138.497 172.647 132.999 1.00 18676. ? 433 GLU A N     1 
ATOM   3216  C  CA    . GLU A 1 433 ? 139.946 172.654 133.133 1.00 18673. ? 433 GLU A CA    1 
ATOM   3217  C  C     . GLU A 1 433 ? 140.536 171.487 132.359 1.00 18666. ? 433 GLU A C     1 
ATOM   3218  O  O     . GLU A 1 433 ? 140.086 170.346 132.506 1.00 18641. ? 433 GLU A O     1 
ATOM   3219  C  CB    . GLU A 1 433 ? 140.364 172.577 134.604 1.00 18675. ? 433 GLU A CB    1 
ATOM   3220  C  CG    . GLU A 1 433 ? 141.860 172.711 134.824 1.00 18677. ? 433 GLU A CG    1 
ATOM   3221  C  CD    . GLU A 1 433 ? 142.492 173.738 133.905 1.00 18676. ? 433 GLU A CD    1 
ATOM   3222  O  OE1   . GLU A 1 433 ? 142.191 174.941 134.058 1.00 18679. ? 433 GLU A OE1   1 
ATOM   3223  O  OE2   . GLU A 1 433 ? 143.286 173.342 133.026 1.00 18674. ? 433 GLU A OE2   1 
ATOM   3224  N  N     . CYS A 1 434 ? 141.542 171.776 131.537 1.00 18401. ? 434 CYS A N     1 
ATOM   3225  C  CA    . CYS A 1 434 ? 142.250 170.758 130.769 1.00 18388. ? 434 CYS A CA    1 
ATOM   3226  C  C     . CYS A 1 434 ? 143.744 170.987 130.943 1.00 18388. ? 434 CYS A C     1 
ATOM   3227  O  O     . CYS A 1 434 ? 144.245 172.078 130.599 1.00 18388. ? 434 CYS A O     1 
ATOM   3228  C  CB    . CYS A 1 434 ? 141.858 170.804 129.290 1.00 18371. ? 434 CYS A CB    1 
ATOM   3229  S  SG    . CYS A 1 434 ? 142.882 169.768 128.221 1.00 18352. ? 434 CYS A SG    1 
ATOM   3230  N  N     . PRO A 1 435 ? 144.492 170.016 131.470 1.00 18179. ? 435 PRO A N     1 
ATOM   3231  C  CA    . PRO A 1 435 ? 145.931 170.205 131.614 1.00 18197. ? 435 PRO A CA    1 
ATOM   3232  C  C     . PRO A 1 435 ? 146.605 170.250 130.256 1.00 18191. ? 435 PRO A C     1 
ATOM   3233  O  O     . PRO A 1 435 ? 146.100 169.673 129.277 1.00 18168. ? 435 PRO A O     1 
ATOM   3234  C  CB    . PRO A 1 435 ? 146.370 168.970 132.420 1.00 18130. ? 435 PRO A CB    1 
ATOM   3235  C  CG    . PRO A 1 435 ? 145.350 167.940 132.087 1.00 18011. ? 435 PRO A CG    1 
ATOM   3236  C  CD    . PRO A 1 435 ? 144.056 168.690 131.939 1.00 18113. ? 435 PRO A CD    1 
ATOM   3237  N  N     . PRO A 1 436 ? 147.745 170.925 130.144 1.00 18325. ? 436 PRO A N     1 
ATOM   3238  C  CA    . PRO A 1 436 ? 148.434 171.016 128.852 1.00 18319. ? 436 PRO A CA    1 
ATOM   3239  C  C     . PRO A 1 436 ? 148.955 169.658 128.418 1.00 18314. ? 436 PRO A C     1 
ATOM   3240  O  O     . PRO A 1 436 ? 149.259 168.802 129.262 1.00 18323. ? 436 PRO A O     1 
ATOM   3241  C  CB    . PRO A 1 436 ? 149.585 171.994 129.132 1.00 18330. ? 436 PRO A CB    1 
ATOM   3242  C  CG    . PRO A 1 436 ? 149.787 171.932 130.606 1.00 18339. ? 436 PRO A CG    1 
ATOM   3243  C  CD    . PRO A 1 436 ? 148.431 171.695 131.194 1.00 18339. ? 436 PRO A CD    1 
ATOM   3244  N  N     . PRO A 1 437 ? 149.077 169.419 127.105 1.00 17782. ? 437 PRO A N     1 
ATOM   3245  C  CA    . PRO A 1 437 ? 148.812 170.339 125.989 1.00 17776. ? 437 PRO A CA    1 
ATOM   3246  C  C     . PRO A 1 437 ? 147.324 170.555 125.736 1.00 17763. ? 437 PRO A C     1 
ATOM   3247  O  O     . PRO A 1 437 ? 146.511 169.657 125.931 1.00 17761. ? 437 PRO A O     1 
ATOM   3248  C  CB    . PRO A 1 437 ? 149.495 169.639 124.811 1.00 17781. ? 437 PRO A CB    1 
ATOM   3249  C  CG    . PRO A 1 437 ? 149.331 168.182 125.122 1.00 17777. ? 437 PRO A CG    1 
ATOM   3250  C  CD    . PRO A 1 437 ? 149.476 168.084 126.623 1.00 17775. ? 437 PRO A CD    1 
ATOM   3251  N  N     . ARG A 1 438 ? 146.946 171.756 125.298 1.00 17282. ? 438 ARG A N     1 
ATOM   3252  C  CA    . ARG A 1 438 ? 145.546 172.092 125.051 1.00 17267. ? 438 ARG A CA    1 
ATOM   3253  C  C     . ARG A 1 438 ? 145.191 171.862 123.580 1.00 17271. ? 438 ARG A C     1 
ATOM   3254  O  O     . ARG A 1 438 ? 144.744 172.755 122.862 1.00 17285. ? 438 ARG A O     1 
ATOM   3255  C  CB    . ARG A 1 438 ? 145.274 173.529 125.471 1.00 17257. ? 438 ARG A CB    1 
ATOM   3256  C  CG    . ARG A 1 438 ? 145.885 173.901 126.806 1.00 17265. ? 438 ARG A CG    1 
ATOM   3257  C  CD    . ARG A 1 438 ? 144.831 173.981 127.891 1.00 17268. ? 438 ARG A CD    1 
ATOM   3258  N  NE    . ARG A 1 438 ? 143.837 175.008 127.607 1.00 17265. ? 438 ARG A NE    1 
ATOM   3259  C  CZ    . ARG A 1 438 ? 142.802 175.281 128.388 1.00 17273. ? 438 ARG A CZ    1 
ATOM   3260  N  NH1   . ARG A 1 438 ? 142.590 174.616 129.512 1.00 17283. ? 438 ARG A NH1   1 
ATOM   3261  N  NH2   . ARG A 1 438 ? 141.959 176.247 128.034 1.00 17310. ? 438 ARG A NH2   1 
ATOM   3262  N  N     . THR A 1 439 ? 145.401 170.625 123.140 1.00 17333. ? 439 THR A N     1 
ATOM   3263  C  CA    . THR A 1 439 ? 145.088 170.249 121.773 1.00 17339. ? 439 THR A CA    1 
ATOM   3264  C  C     . THR A 1 439 ? 143.576 170.167 121.577 1.00 17318. ? 439 THR A C     1 
ATOM   3265  O  O     . THR A 1 439 ? 142.797 170.147 122.533 1.00 17301. ? 439 THR A O     1 
ATOM   3266  C  CB    . THR A 1 439 ? 145.741 168.914 121.420 1.00 17326. ? 439 THR A CB    1 
ATOM   3267  O  OG1   . THR A 1 439 ? 145.068 167.855 122.109 1.00 17320. ? 439 THR A OG1   1 
ATOM   3268  C  CG2   . THR A 1 439 ? 147.203 168.918 121.822 1.00 17332. ? 439 THR A CG2   1 
ATOM   3269  N  N     . THR A 1 440 ? 143.162 170.131 120.309 1.00 17261. ? 440 THR A N     1 
ATOM   3270  C  CA    . THR A 1 440 ? 141.738 170.043 120.003 1.00 17258. ? 440 THR A CA    1 
ATOM   3271  C  C     . THR A 1 440 ? 141.139 168.749 120.536 1.00 17236. ? 440 THR A C     1 
ATOM   3272  O  O     . THR A 1 440 ? 140.037 168.754 121.095 1.00 17230. ? 440 THR A O     1 
ATOM   3273  C  CB    . THR A 1 440 ? 141.511 170.147 118.496 1.00 17274. ? 440 THR A CB    1 
ATOM   3274  O  OG1   . THR A 1 440 ? 141.878 171.453 118.044 1.00 17322. ? 440 THR A OG1   1 
ATOM   3275  C  CG2   . THR A 1 440 ? 140.051 169.920 118.168 1.00 17281. ? 440 THR A CG2   1 
ATOM   3276  N  N     . ALA A 1 441 ? 141.852 167.632 120.376 1.00 16607. ? 441 ALA A N     1 
ATOM   3277  C  CA    . ALA A 1 441 ? 141.329 166.352 120.840 1.00 16590. ? 441 ALA A CA    1 
ATOM   3278  C  C     . ALA A 1 441 ? 141.115 166.354 122.347 1.00 16586. ? 441 ALA A C     1 
ATOM   3279  O  O     . ALA A 1 441 ? 140.065 165.918 122.831 1.00 16571. ? 441 ALA A O     1 
ATOM   3280  C  CB    . ALA A 1 441 ? 142.275 165.223 120.435 1.00 16564. ? 441 ALA A CB    1 
ATOM   3281  N  N     . ARG A 1 442 ? 142.090 166.857 123.104 1.00 16906. ? 442 ARG A N     1 
ATOM   3282  C  CA    . ARG A 1 442 ? 141.984 166.843 124.558 1.00 16912. ? 442 ARG A CA    1 
ATOM   3283  C  C     . ARG A 1 442 ? 140.904 167.799 125.051 1.00 16884. ? 442 ARG A C     1 
ATOM   3284  O  O     . ARG A 1 442 ? 140.140 167.464 125.962 1.00 16870. ? 442 ARG A O     1 
ATOM   3285  C  CB    . ARG A 1 442 ? 143.338 167.180 125.182 1.00 16929. ? 442 ARG A CB    1 
ATOM   3286  C  CG    . ARG A 1 442 ? 144.350 166.052 125.066 1.00 16924. ? 442 ARG A CG    1 
ATOM   3287  C  CD    . ARG A 1 442 ? 145.765 166.544 125.307 1.00 16935. ? 442 ARG A CD    1 
ATOM   3288  N  NE    . ARG A 1 442 ? 145.920 167.156 126.621 1.00 16928. ? 442 ARG A NE    1 
ATOM   3289  C  CZ    . ARG A 1 442 ? 145.905 166.491 127.768 1.00 16897. ? 442 ARG A CZ    1 
ATOM   3290  N  NH1   . ARG A 1 442 ? 145.767 165.175 127.804 1.00 16824. ? 442 ARG A NH1   1 
ATOM   3291  N  NH2   . ARG A 1 442 ? 146.040 167.161 128.908 1.00 16883. ? 442 ARG A NH2   1 
ATOM   3292  N  N     . LEU A 1 443 ? 140.822 168.992 124.459 1.00 16312. ? 443 LEU A N     1 
ATOM   3293  C  CA    . LEU A 1 443 ? 139.767 169.927 124.837 1.00 16295. ? 443 LEU A CA    1 
ATOM   3294  C  C     . LEU A 1 443 ? 138.387 169.370 124.521 1.00 16268. ? 443 LEU A C     1 
ATOM   3295  O  O     . LEU A 1 443 ? 137.461 169.501 125.331 1.00 16255. ? 443 LEU A O     1 
ATOM   3296  C  CB    . LEU A 1 443 ? 139.971 171.264 124.127 1.00 16309. ? 443 LEU A CB    1 
ATOM   3297  C  CG    . LEU A 1 443 ? 141.156 172.109 124.589 1.00 16325. ? 443 LEU A CG    1 
ATOM   3298  C  CD1   . LEU A 1 443 ? 141.366 173.288 123.657 1.00 16352. ? 443 LEU A CD1   1 
ATOM   3299  C  CD2   . LEU A 1 443 ? 140.943 172.582 126.014 1.00 16333. ? 443 LEU A CD2   1 
ATOM   3300  N  N     . LEU A 1 444 ? 138.231 168.748 123.352 1.00 15824. ? 444 LEU A N     1 
ATOM   3301  C  CA    . LEU A 1 444 ? 136.950 168.155 122.991 1.00 15798. ? 444 LEU A CA    1 
ATOM   3302  C  C     . LEU A 1 444 ? 136.590 167.009 123.927 1.00 15775. ? 444 LEU A C     1 
ATOM   3303  O  O     . LEU A 1 444 ? 135.430 166.872 124.328 1.00 15755. ? 444 LEU A O     1 
ATOM   3304  C  CB    . LEU A 1 444 ? 136.989 167.675 121.543 1.00 15796. ? 444 LEU A CB    1 
ATOM   3305  C  CG    . LEU A 1 444 ? 136.242 168.523 120.516 1.00 15811. ? 444 LEU A CG    1 
ATOM   3306  C  CD1   . LEU A 1 444 ? 136.377 167.914 119.132 1.00 15805. ? 444 LEU A CD1   1 
ATOM   3307  C  CD2   . LEU A 1 444 ? 134.784 168.662 120.902 1.00 15793. ? 444 LEU A CD2   1 
ATOM   3308  N  N     . ASP A 1 445 ? 137.569 166.176 124.284 1.00 15794. ? 445 ASP A N     1 
ATOM   3309  C  CA    . ASP A 1 445 ? 137.308 165.091 125.222 1.00 15779. ? 445 ASP A CA    1 
ATOM   3310  C  C     . ASP A 1 445 ? 136.903 165.630 126.587 1.00 15765. ? 445 ASP A C     1 
ATOM   3311  O  O     . ASP A 1 445 ? 135.999 165.088 127.233 1.00 15753. ? 445 ASP A O     1 
ATOM   3312  C  CB    . ASP A 1 445 ? 138.539 164.195 125.341 1.00 15794. ? 445 ASP A CB    1 
ATOM   3313  C  CG    . ASP A 1 445 ? 138.315 163.019 126.268 1.00 15786. ? 445 ASP A CG    1 
ATOM   3314  O  OD1   . ASP A 1 445 ? 137.156 162.573 126.396 1.00 15777. ? 445 ASP A OD1   1 
ATOM   3315  O  OD2   . ASP A 1 445 ? 139.299 162.541 126.870 1.00 15786. ? 445 ASP A OD2   1 
ATOM   3316  N  N     . LYS A 1 446 ? 137.562 166.696 127.046 1.00 15641. ? 446 LYS A N     1 
ATOM   3317  C  CA    . LYS A 1 446 ? 137.196 167.297 128.324 1.00 15635. ? 446 LYS A CA    1 
ATOM   3318  C  C     . LYS A 1 446 ? 135.779 167.854 128.286 1.00 15614. ? 446 LYS A C     1 
ATOM   3319  O  O     . LYS A 1 446 ? 135.007 167.669 129.234 1.00 15612. ? 446 LYS A O     1 
ATOM   3320  C  CB    . LYS A 1 446 ? 138.194 168.394 128.692 1.00 15667. ? 446 LYS A CB    1 
ATOM   3321  C  CG    . LYS A 1 446 ? 139.185 167.994 129.770 1.00 15673. ? 446 LYS A CG    1 
ATOM   3322  C  CD    . LYS A 1 446 ? 139.815 166.646 129.466 1.00 15661. ? 446 LYS A CD    1 
ATOM   3323  C  CE    . LYS A 1 446 ? 141.097 166.444 130.253 1.00 15627. ? 446 LYS A CE    1 
ATOM   3324  N  NZ    . LYS A 1 446 ? 141.242 165.036 130.707 1.00 15555. ? 446 LYS A NZ    1 
ATOM   3325  N  N     . LEU A 1 447 ? 135.417 168.539 127.199 1.00 15159. ? 447 LEU A N     1 
ATOM   3326  C  CA    . LEU A 1 447 ? 134.061 169.067 127.081 1.00 15131. ? 447 LEU A CA    1 
ATOM   3327  C  C     . LEU A 1 447 ? 133.032 167.945 127.048 1.00 15106. ? 447 LEU A C     1 
ATOM   3328  O  O     . LEU A 1 447 ? 131.967 168.050 127.668 1.00 15116. ? 447 LEU A O     1 
ATOM   3329  C  CB    . LEU A 1 447 ? 133.937 169.939 125.834 1.00 15145. ? 447 LEU A CB    1 
ATOM   3330  C  CG    . LEU A 1 447 ? 134.637 171.295 125.875 1.00 15157. ? 447 LEU A CG    1 
ATOM   3331  C  CD1   . LEU A 1 447 ? 134.970 171.762 124.471 1.00 15187. ? 447 LEU A CD1   1 
ATOM   3332  C  CD2   . LEU A 1 447 ? 133.771 172.315 126.590 1.00 15198. ? 447 LEU A CD2   1 
ATOM   3333  N  N     . VAL A 1 448 ? 133.331 166.866 126.323 1.00 14332. ? 448 VAL A N     1 
ATOM   3334  C  CA    . VAL A 1 448 ? 132.415 165.733 126.259 1.00 14297. ? 448 VAL A CA    1 
ATOM   3335  C  C     . VAL A 1 448 ? 132.236 165.118 127.639 1.00 14310. ? 448 VAL A C     1 
ATOM   3336  O  O     . VAL A 1 448 ? 131.114 164.818 128.061 1.00 14321. ? 448 VAL A O     1 
ATOM   3337  C  CB    . VAL A 1 448 ? 132.920 164.699 125.237 1.00 14295. ? 448 VAL A CB    1 
ATOM   3338  C  CG1   . VAL A 1 448 ? 132.255 163.354 125.461 1.00 14284. ? 448 VAL A CG1   1 
ATOM   3339  C  CG2   . VAL A 1 448 ? 132.674 165.194 123.828 1.00 14312. ? 448 VAL A CG2   1 
ATOM   3340  N  N     . GLY A 1 449 ? 133.337 164.933 128.368 1.00 14524. ? 449 GLY A N     1 
ATOM   3341  C  CA    . GLY A 1 449 ? 133.242 164.379 129.707 1.00 14519. ? 449 GLY A CA    1 
ATOM   3342  C  C     . GLY A 1 449 ? 132.473 165.273 130.659 1.00 14539. ? 449 GLY A C     1 
ATOM   3343  O  O     . GLY A 1 449 ? 131.741 164.790 131.525 1.00 14528. ? 449 GLY A O     1 
ATOM   3344  N  N     . GLU A 1 450 ? 132.630 166.589 130.517 1.00 15728. ? 450 GLU A N     1 
ATOM   3345  C  CA    . GLU A 1 450 ? 131.972 167.510 131.434 1.00 15752. ? 450 GLU A CA    1 
ATOM   3346  C  C     . GLU A 1 450 ? 130.488 167.680 131.133 1.00 15739. ? 450 GLU A C     1 
ATOM   3347  O  O     . GLU A 1 450 ? 129.695 167.863 132.063 1.00 15755. ? 450 GLU A O     1 
ATOM   3348  C  CB    . GLU A 1 450 ? 132.666 168.871 131.398 1.00 15779. ? 450 GLU A CB    1 
ATOM   3349  C  CG    . GLU A 1 450 ? 132.760 169.548 132.754 1.00 15796. ? 450 GLU A CG    1 
ATOM   3350  C  CD    . GLU A 1 450 ? 131.567 170.433 133.047 1.00 15793. ? 450 GLU A CD    1 
ATOM   3351  O  OE1   . GLU A 1 450 ? 130.736 170.633 132.136 1.00 15786. ? 450 GLU A OE1   1 
ATOM   3352  O  OE2   . GLU A 1 450 ? 131.460 170.928 134.188 1.00 15798. ? 450 GLU A OE2   1 
ATOM   3353  N  N     . PHE A 1 451 ? 130.089 167.625 129.864 1.00 15230. ? 451 PHE A N     1 
ATOM   3354  C  CA    . PHE A 1 451 ? 128.716 167.933 129.477 1.00 15224. ? 451 PHE A CA    1 
ATOM   3355  C  C     . PHE A 1 451 ? 127.931 166.721 129.002 1.00 15202. ? 451 PHE A C     1 
ATOM   3356  O  O     . PHE A 1 451 ? 126.816 166.485 129.474 1.00 15199. ? 451 PHE A O     1 
ATOM   3357  C  CB    . PHE A 1 451 ? 128.714 169.010 128.385 1.00 15230. ? 451 PHE A CB    1 
ATOM   3358  C  CG    . PHE A 1 451 ? 129.075 170.375 128.886 1.00 15236. ? 451 PHE A CG    1 
ATOM   3359  C  CD1   . PHE A 1 451 ? 128.104 171.220 129.391 1.00 15240. ? 451 PHE A CD1   1 
ATOM   3360  C  CD2   . PHE A 1 451 ? 130.387 170.812 128.857 1.00 15244. ? 451 PHE A CD2   1 
ATOM   3361  C  CE1   . PHE A 1 451 ? 128.433 172.476 129.856 1.00 15245. ? 451 PHE A CE1   1 
ATOM   3362  C  CE2   . PHE A 1 451 ? 130.722 172.067 129.320 1.00 15258. ? 451 PHE A CE2   1 
ATOM   3363  C  CZ    . PHE A 1 451 ? 129.745 172.900 129.820 1.00 15277. ? 451 PHE A CZ    1 
ATOM   3364  N  N     . LEU A 1 452 ? 128.479 165.943 128.073 1.00 14633. ? 452 LEU A N     1 
ATOM   3365  C  CA    . LEU A 1 452 ? 127.752 164.819 127.499 1.00 14608. ? 452 LEU A CA    1 
ATOM   3366  C  C     . LEU A 1 452 ? 127.753 163.583 128.384 1.00 14596. ? 452 LEU A C     1 
ATOM   3367  O  O     . LEU A 1 452 ? 127.096 162.598 128.037 1.00 14591. ? 452 LEU A O     1 
ATOM   3368  C  CB    . LEU A 1 452 ? 128.339 164.450 126.135 1.00 14605. ? 452 LEU A CB    1 
ATOM   3369  C  CG    . LEU A 1 452 ? 127.953 165.332 124.953 1.00 14625. ? 452 LEU A CG    1 
ATOM   3370  C  CD1   . LEU A 1 452 ? 128.318 164.645 123.651 1.00 14614. ? 452 LEU A CD1   1 
ATOM   3371  C  CD2   . LEU A 1 452 ? 126.473 165.653 125.001 1.00 14642. ? 452 LEU A CD2   1 
ATOM   3372  N  N     . GLU A 1 453 ? 128.463 163.603 129.508 1.00 14362. ? 453 GLU A N     1 
ATOM   3373  C  CA    . GLU A 1 453 ? 128.729 162.381 130.246 1.00 14343. ? 453 GLU A CA    1 
ATOM   3374  C  C     . GLU A 1 453 ? 128.073 162.343 131.614 1.00 14337. ? 453 GLU A C     1 
ATOM   3375  O  O     . GLU A 1 453 ? 127.925 161.256 132.180 1.00 14315. ? 453 GLU A O     1 
ATOM   3376  C  CB    . GLU A 1 453 ? 130.242 162.197 130.406 1.00 14348. ? 453 GLU A CB    1 
ATOM   3377  C  CG    . GLU A 1 453 ? 130.916 161.839 129.104 1.00 14345. ? 453 GLU A CG    1 
ATOM   3378  C  CD    . GLU A 1 453 ? 130.760 160.400 128.707 1.00 14317. ? 453 GLU A CD    1 
ATOM   3379  O  OE1   . GLU A 1 453 ? 129.768 159.752 129.100 1.00 14303. ? 453 GLU A OE1   1 
ATOM   3380  O  OE2   . GLU A 1 453 ? 131.626 159.937 127.948 1.00 14314. ? 453 GLU A OE2   1 
ATOM   3381  N  N     . VAL A 1 454 ? 127.680 163.495 132.161 1.00 14659. ? 454 VAL A N     1 
ATOM   3382  C  CA    . VAL A 1 454 ? 126.923 163.508 133.408 1.00 14659. ? 454 VAL A CA    1 
ATOM   3383  C  C     . VAL A 1 454 ? 125.476 163.101 133.202 1.00 14648. ? 454 VAL A C     1 
ATOM   3384  O  O     . VAL A 1 454 ? 124.738 162.953 134.183 1.00 14649. ? 454 VAL A O     1 
ATOM   3385  C  CB    . VAL A 1 454 ? 126.994 164.899 134.062 1.00 14669. ? 454 VAL A CB    1 
ATOM   3386  C  CG1   . VAL A 1 454 ? 128.410 165.440 133.987 1.00 14684. ? 454 VAL A CG1   1 
ATOM   3387  C  CG2   . VAL A 1 454 ? 126.026 165.852 133.381 1.00 14678. ? 454 VAL A CG2   1 
ATOM   3388  N  N     . THR A 1 455 ? 125.051 162.910 131.954 1.00 14424. ? 455 THR A N     1 
ATOM   3389  C  CA    . THR A 1 455 ? 123.688 162.515 131.636 1.00 14412. ? 455 THR A CA    1 
ATOM   3390  C  C     . THR A 1 455 ? 123.579 161.069 131.175 1.00 14374. ? 455 THR A C     1 
ATOM   3391  O  O     . THR A 1 455 ? 122.488 160.640 130.787 1.00 14378. ? 455 THR A O     1 
ATOM   3392  C  CB    . THR A 1 455 ? 123.110 163.436 130.556 1.00 14417. ? 455 THR A CB    1 
ATOM   3393  O  OG1   . THR A 1 455 ? 123.603 163.032 129.272 1.00 14402. ? 455 THR A OG1   1 
ATOM   3394  C  CG2   . THR A 1 455 ? 123.516 164.876 130.814 1.00 14425. ? 455 THR A CG2   1 
ATOM   3395  N  N     . CYS A 1 456 ? 124.668 160.311 131.202 1.00 13313. ? 456 CYS A N     1 
ATOM   3396  C  CA    . CYS A 1 456 ? 124.658 158.925 130.738 1.00 13265. ? 456 CYS A CA    1 
ATOM   3397  C  C     . CYS A 1 456 ? 124.474 157.965 131.911 1.00 13235. ? 456 CYS A C     1 
ATOM   3398  O  O     . CYS A 1 456 ? 125.336 157.148 132.227 1.00 13225. ? 456 CYS A O     1 
ATOM   3399  C  CB    . CYS A 1 456 ? 125.937 158.617 129.966 1.00 13259. ? 456 CYS A CB    1 
ATOM   3400  S  SG    . CYS A 1 456 ? 126.010 159.360 128.323 1.00 13255. ? 456 CYS A SG    1 
ATOM   3401  N  N     . ILE A 1 457 ? 123.318 158.074 132.563 1.00 12776. ? 457 ILE A N     1 
ATOM   3402  C  CA    . ILE A 1 457 ? 122.969 157.129 133.620 1.00 12747. ? 457 ILE A CA    1 
ATOM   3403  C  C     . ILE A 1 457 ? 122.550 155.795 133.019 1.00 12731. ? 457 ILE A C     1 
ATOM   3404  O  O     . ILE A 1 457 ? 123.183 154.760 133.255 1.00 12740. ? 457 ILE A O     1 
ATOM   3405  C  CB    . ILE A 1 457 ? 121.866 157.710 134.521 1.00 12743. ? 457 ILE A CB    1 
ATOM   3406  C  CG1   . ILE A 1 457 ? 122.144 159.182 134.820 1.00 12760. ? 457 ILE A CG1   1 
ATOM   3407  C  CG2   . ILE A 1 457 ? 121.761 156.913 135.808 1.00 12752. ? 457 ILE A CG2   1 
ATOM   3408  C  CD1   . ILE A 1 457 ? 123.349 159.403 135.695 1.00 12765. ? 457 ILE A CD1   1 
ATOM   3409  N  N     . ASN A 1 458 ? 121.481 155.803 132.230 1.00 12731. ? 458 ASN A N     1 
ATOM   3410  C  CA    . ASN A 1 458 ? 121.106 154.620 131.481 1.00 12736. ? 458 ASN A CA    1 
ATOM   3411  C  C     . ASN A 1 458 ? 122.137 154.363 130.385 1.00 12744. ? 458 ASN A C     1 
ATOM   3412  O  O     . ASN A 1 458 ? 122.825 155.289 129.946 1.00 12763. ? 458 ASN A O     1 
ATOM   3413  C  CB    . ASN A 1 458 ? 119.723 154.793 130.864 1.00 12745. ? 458 ASN A CB    1 
ATOM   3414  C  CG    . ASN A 1 458 ? 118.688 155.231 131.874 1.00 12745. ? 458 ASN A CG    1 
ATOM   3415  O  OD1   . ASN A 1 458 ? 119.020 155.591 133.001 1.00 12751. ? 458 ASN A OD1   1 
ATOM   3416  N  ND2   . ASN A 1 458 ? 117.424 155.205 131.475 1.00 12746. ? 458 ASN A ND2   1 
ATOM   3417  N  N     . PRO A 1 459 ? 122.282 153.115 129.943 1.00 12732. ? 459 PRO A N     1 
ATOM   3418  C  CA    . PRO A 1 459 ? 123.228 152.828 128.857 1.00 12739. ? 459 PRO A CA    1 
ATOM   3419  C  C     . PRO A 1 459 ? 122.921 153.674 127.631 1.00 12741. ? 459 PRO A C     1 
ATOM   3420  O  O     . PRO A 1 459 ? 121.775 153.758 127.185 1.00 12757. ? 459 PRO A O     1 
ATOM   3421  C  CB    . PRO A 1 459 ? 123.022 151.333 128.584 1.00 12740. ? 459 PRO A CB    1 
ATOM   3422  C  CG    . PRO A 1 459 ? 121.825 150.924 129.385 1.00 12744. ? 459 PRO A CG    1 
ATOM   3423  C  CD    . PRO A 1 459 ? 121.693 151.891 130.502 1.00 12742. ? 459 PRO A CD    1 
ATOM   3424  N  N     . THR A 1 460 ? 123.958 154.309 127.093 1.00 12743. ? 460 THR A N     1 
ATOM   3425  C  CA    . THR A 1 460 ? 123.798 155.256 126.000 1.00 12737. ? 460 THR A CA    1 
ATOM   3426  C  C     . THR A 1 460 ? 124.939 155.099 125.010 1.00 12742. ? 460 THR A C     1 
ATOM   3427  O  O     . THR A 1 460 ? 126.096 154.937 125.406 1.00 12766. ? 460 THR A O     1 
ATOM   3428  C  CB    . THR A 1 460 ? 123.758 156.697 126.518 1.00 12747. ? 460 THR A CB    1 
ATOM   3429  O  OG1   . THR A 1 460 ? 122.875 156.776 127.642 1.00 12759. ? 460 THR A OG1   1 
ATOM   3430  C  CG2   . THR A 1 460 ? 123.269 157.641 125.435 1.00 12758. ? 460 THR A CG2   1 
ATOM   3431  N  N     . PHE A 1 461 ? 124.609 155.153 123.724 1.00 12739. ? 461 PHE A N     1 
ATOM   3432  C  CA    . PHE A 1 461 ? 125.608 155.123 122.667 1.00 12738. ? 461 PHE A CA    1 
ATOM   3433  C  C     . PHE A 1 461 ? 125.983 156.545 122.276 1.00 12738. ? 461 PHE A C     1 
ATOM   3434  O  O     . PHE A 1 461 ? 125.108 157.363 121.977 1.00 12754. ? 461 PHE A O     1 
ATOM   3435  C  CB    . PHE A 1 461 ? 125.086 154.373 121.442 1.00 12746. ? 461 PHE A CB    1 
ATOM   3436  C  CG    . PHE A 1 461 ? 124.961 152.894 121.638 1.00 12738. ? 461 PHE A CG    1 
ATOM   3437  C  CD1   . PHE A 1 461 ? 126.071 152.122 121.915 1.00 12742. ? 461 PHE A CD1   1 
ATOM   3438  C  CD2   . PHE A 1 461 ? 123.732 152.271 121.525 1.00 12745. ? 461 PHE A CD2   1 
ATOM   3439  C  CE1   . PHE A 1 461 ? 125.957 150.761 122.086 1.00 12749. ? 461 PHE A CE1   1 
ATOM   3440  C  CE2   . PHE A 1 461 ? 123.613 150.910 121.696 1.00 12744. ? 461 PHE A CE2   1 
ATOM   3441  C  CZ    . PHE A 1 461 ? 124.726 150.154 121.977 1.00 12745. ? 461 PHE A CZ    1 
ATOM   3442  N  N     . ILE A 1 462 ? 127.278 156.837 122.285 1.00 12738. ? 462 ILE A N     1 
ATOM   3443  C  CA    . ILE A 1 462 ? 127.810 158.088 121.758 1.00 12737. ? 462 ILE A CA    1 
ATOM   3444  C  C     . ILE A 1 462 ? 128.563 157.747 120.482 1.00 12743. ? 462 ILE A C     1 
ATOM   3445  O  O     . ILE A 1 462 ? 129.550 157.004 120.521 1.00 12768. ? 462 ILE A O     1 
ATOM   3446  C  CB    . ILE A 1 462 ? 128.718 158.794 122.772 1.00 12739. ? 462 ILE A CB    1 
ATOM   3447  C  CG1   . ILE A 1 462 ? 128.119 158.698 124.175 1.00 12742. ? 462 ILE A CG1   1 
ATOM   3448  C  CG2   . ILE A 1 462 ? 128.926 160.242 122.377 1.00 12770. ? 462 ILE A CG2   1 
ATOM   3449  C  CD1   . ILE A 1 462 ? 128.802 159.577 125.192 1.00 12771. ? 462 ILE A CD1   1 
ATOM   3450  N  N     . CYS A 1 463 ? 128.101 158.280 119.357 1.00 12740. ? 463 CYS A N     1 
ATOM   3451  C  CA    . CYS A 1 463 ? 128.567 157.854 118.047 1.00 12740. ? 463 CYS A CA    1 
ATOM   3452  C  C     . CYS A 1 463 ? 129.137 159.031 117.267 1.00 12761. ? 463 CYS A C     1 
ATOM   3453  O  O     . CYS A 1 463 ? 128.972 160.195 117.638 1.00 12813. ? 463 CYS A O     1 
ATOM   3454  C  CB    . CYS A 1 463 ? 127.432 157.201 117.249 1.00 12748. ? 463 CYS A CB    1 
ATOM   3455  S  SG    . CYS A 1 463 ? 126.366 156.114 118.215 1.00 12734. ? 463 CYS A SG    1 
ATOM   3456  N  N     . ASP A 1 464 ? 129.820 158.696 116.171 1.00 12961. ? 464 ASP A N     1 
ATOM   3457  C  CA    . ASP A 1 464 ? 130.344 159.667 115.211 1.00 12964. ? 464 ASP A CA    1 
ATOM   3458  C  C     . ASP A 1 464 ? 131.305 160.653 115.878 1.00 12969. ? 464 ASP A C     1 
ATOM   3459  O  O     . ASP A 1 464 ? 131.070 161.860 115.930 1.00 12998. ? 464 ASP A O     1 
ATOM   3460  C  CB    . ASP A 1 464 ? 129.203 160.402 114.502 1.00 12993. ? 464 ASP A CB    1 
ATOM   3461  C  CG    . ASP A 1 464 ? 128.170 159.455 113.930 1.00 13008. ? 464 ASP A CG    1 
ATOM   3462  O  OD1   . ASP A 1 464 ? 128.369 158.227 114.032 1.00 12996. ? 464 ASP A OD1   1 
ATOM   3463  O  OD2   . ASP A 1 464 ? 127.159 159.936 113.380 1.00 13028. ? 464 ASP A OD2   1 
ATOM   3464  N  N     . HIS A 1 465 ? 132.403 160.108 116.389 1.00 12761. ? 465 HIS A N     1 
ATOM   3465  C  CA    . HIS A 1 465 ? 133.452 160.940 116.947 1.00 12773. ? 465 HIS A CA    1 
ATOM   3466  C  C     . HIS A 1 465 ? 134.145 161.718 115.830 1.00 12774. ? 465 HIS A C     1 
ATOM   3467  O  O     . HIS A 1 465 ? 134.115 161.308 114.668 1.00 12798. ? 465 HIS A O     1 
ATOM   3468  C  CB    . HIS A 1 465 ? 134.482 160.090 117.686 1.00 12775. ? 465 HIS A CB    1 
ATOM   3469  C  CG    . HIS A 1 465 ? 133.933 159.338 118.859 1.00 12760. ? 465 HIS A CG    1 
ATOM   3470  N  ND1   . HIS A 1 465 ? 132.689 158.744 118.854 1.00 12768. ? 465 HIS A ND1   1 
ATOM   3471  C  CD2   . HIS A 1 465 ? 134.471 159.070 120.072 1.00 12766. ? 465 HIS A CD2   1 
ATOM   3472  C  CE1   . HIS A 1 465 ? 132.482 158.149 120.014 1.00 12763. ? 465 HIS A CE1   1 
ATOM   3473  N  NE2   . HIS A 1 465 ? 133.546 158.335 120.773 1.00 12759. ? 465 HIS A NE2   1 
ATOM   3474  N  N     . PRO A 1 466 ? 134.751 162.859 116.147 1.00 13317. ? 466 PRO A N     1 
ATOM   3475  C  CA    . PRO A 1 466 ? 135.626 163.511 115.169 1.00 13348. ? 466 PRO A CA    1 
ATOM   3476  C  C     . PRO A 1 466 ? 136.826 162.632 114.856 1.00 13408. ? 466 PRO A C     1 
ATOM   3477  O  O     . PRO A 1 466 ? 137.299 161.866 115.698 1.00 13423. ? 466 PRO A O     1 
ATOM   3478  C  CB    . PRO A 1 466 ? 136.040 164.808 115.870 1.00 13391. ? 466 PRO A CB    1 
ATOM   3479  C  CG    . PRO A 1 466 ? 134.949 165.060 116.852 1.00 13391. ? 466 PRO A CG    1 
ATOM   3480  C  CD    . PRO A 1 466 ? 134.523 163.705 117.328 1.00 13365. ? 466 PRO A CD    1 
ATOM   3481  N  N     . GLN A 1 467 ? 137.314 162.742 113.618 1.00 14565. ? 467 GLN A N     1 
ATOM   3482  C  CA    . GLN A 1 467 ? 138.401 161.876 113.173 1.00 14598. ? 467 GLN A CA    1 
ATOM   3483  C  C     . GLN A 1 467 ? 139.671 162.097 113.983 1.00 14642. ? 467 GLN A C     1 
ATOM   3484  O  O     . GLN A 1 467 ? 140.477 161.173 114.136 1.00 14659. ? 467 GLN A O     1 
ATOM   3485  C  CB    . GLN A 1 467 ? 138.677 162.100 111.688 1.00 14599. ? 467 GLN A CB    1 
ATOM   3486  C  CG    . GLN A 1 467 ? 139.318 160.911 110.992 1.00 14620. ? 467 GLN A CG    1 
ATOM   3487  C  CD    . GLN A 1 467 ? 138.714 160.636 109.629 1.00 14611. ? 467 GLN A CD    1 
ATOM   3488  O  OE1   . GLN A 1 467 ? 137.915 161.421 109.121 1.00 14597. ? 467 GLN A OE1   1 
ATOM   3489  N  NE2   . GLN A 1 467 ? 139.099 159.517 109.027 1.00 14596. ? 467 GLN A NE2   1 
ATOM   3490  N  N     . ILE A 1 468 ? 139.867 163.310 114.503 1.00 15220. ? 468 ILE A N     1 
ATOM   3491  C  CA    . ILE A 1 468 ? 141.064 163.605 115.283 1.00 15241. ? 468 ILE A CA    1 
ATOM   3492  C  C     . ILE A 1 468 ? 141.077 162.822 116.588 1.00 15259. ? 468 ILE A C     1 
ATOM   3493  O  O     . ILE A 1 468 ? 142.143 162.409 117.060 1.00 15273. ? 468 ILE A O     1 
ATOM   3494  C  CB    . ILE A 1 468 ? 141.164 165.118 115.535 1.00 15249. ? 468 ILE A CB    1 
ATOM   3495  C  CG1   . ILE A 1 468 ? 139.781 165.682 115.850 1.00 15241. ? 468 ILE A CG1   1 
ATOM   3496  C  CG2   . ILE A 1 468 ? 141.766 165.818 114.331 1.00 15287. ? 468 ILE A CG2   1 
ATOM   3497  C  CD1   . ILE A 1 468 ? 139.756 167.174 115.977 1.00 15306. ? 468 ILE A CD1   1 
ATOM   3498  N  N     . MET A 1 469 ? 139.925 162.739 117.252 1.00 15856. ? 469 MET A N     1 
ATOM   3499  C  CA    . MET A 1 469 ? 139.854 162.055 118.565 1.00 15888. ? 469 MET A CA    1 
ATOM   3500  C  C     . MET A 1 469 ? 140.076 160.556 118.394 1.00 15887. ? 469 MET A C     1 
ATOM   3501  O  O     . MET A 1 469 ? 140.210 159.880 119.415 1.00 15830. ? 469 MET A O     1 
ATOM   3502  C  CB    . MET A 1 469 ? 138.471 162.206 119.195 1.00 15878. ? 469 MET A CB    1 
ATOM   3503  C  CG    . MET A 1 469 ? 138.102 163.603 119.623 1.00 15898. ? 469 MET A CG    1 
ATOM   3504  S  SD    . MET A 1 469 ? 136.860 163.436 120.918 1.00 15891. ? 469 MET A SD    1 
ATOM   3505  C  CE    . MET A 1 469 ? 135.701 164.753 120.530 1.00 15899. ? 469 MET A CE    1 
ATOM   3506  N  N     . SER A 1 470 ? 140.114 160.050 117.166 1.00 15506. ? 470 SER A N     1 
ATOM   3507  C  CA    . SER A 1 470 ? 140.187 158.575 117.002 1.00 15502. ? 470 SER A CA    1 
ATOM   3508  C  C     . SER A 1 470 ? 140.828 158.158 115.684 1.00 15504. ? 470 SER A C     1 
ATOM   3509  O  O     . SER A 1 470 ? 140.312 158.549 114.638 1.00 15487. ? 470 SER A O     1 
ATOM   3510  C  CB    . SER A 1 470 ? 138.820 157.992 117.068 1.00 15479. ? 470 SER A CB    1 
ATOM   3511  O  OG    . SER A 1 470 ? 137.914 158.757 116.290 1.00 15453. ? 470 SER A OG    1 
ATOM   3512  N  N     . PRO A 1 471 ? 141.913 157.366 115.692 1.00 15361. ? 471 PRO A N     1 
ATOM   3513  C  CA    . PRO A 1 471 ? 142.462 156.837 114.462 1.00 15365. ? 471 PRO A CA    1 
ATOM   3514  C  C     . PRO A 1 471 ? 141.933 155.446 114.383 1.00 15351. ? 471 PRO A C     1 
ATOM   3515  O  O     . PRO A 1 471 ? 141.034 155.101 115.160 1.00 15352. ? 471 PRO A O     1 
ATOM   3516  C  CB    . PRO A 1 471 ? 143.915 156.826 114.844 1.00 15333. ? 471 PRO A CB    1 
ATOM   3517  C  CG    . PRO A 1 471 ? 143.905 156.336 116.269 1.00 15261. ? 471 PRO A CG    1 
ATOM   3518  C  CD    . PRO A 1 471 ? 142.683 157.010 116.872 1.00 15293. ? 471 PRO A CD    1 
ATOM   3519  N  N     . LEU A 1 472 ? 142.455 154.639 113.453 1.00 15230. ? 472 LEU A N     1 
ATOM   3520  C  CA    . LEU A 1 472 ? 142.077 153.200 113.353 1.00 15217. ? 472 LEU A CA    1 
ATOM   3521  C  C     . LEU A 1 472 ? 140.557 153.001 113.201 1.00 15189. ? 472 LEU A C     1 
ATOM   3522  O  O     . LEU A 1 472 ? 140.101 151.857 113.419 1.00 15181. ? 472 LEU A O     1 
ATOM   3523  C  CB    . LEU A 1 472 ? 142.618 152.429 114.559 1.00 15245. ? 472 LEU A CB    1 
ATOM   3524  C  CG    . LEU A 1 472 ? 144.074 151.960 114.465 1.00 15246. ? 472 LEU A CG    1 
ATOM   3525  C  CD1   . LEU A 1 472 ? 145.065 153.104 114.597 1.00 15148. ? 472 LEU A CD1   1 
ATOM   3526  C  CD2   . LEU A 1 472 ? 144.363 150.876 115.489 1.00 15193. ? 472 LEU A CD2   1 
ATOM   3527  N  N     . ALA A 1 473 ? 139.803 154.044 112.842 1.00 12880. ? 473 ALA A N     1 
ATOM   3528  C  CA    . ALA A 1 473 ? 138.367 153.859 112.585 1.00 12795. ? 473 ALA A CA    1 
ATOM   3529  C  C     . ALA A 1 473 ? 138.086 154.350 111.174 1.00 12760. ? 473 ALA A C     1 
ATOM   3530  O  O     . ALA A 1 473 ? 138.692 155.335 110.763 1.00 12780. ? 473 ALA A O     1 
ATOM   3531  C  CB    . ALA A 1 473 ? 137.620 154.614 113.612 1.00 12794. ? 473 ALA A CB    1 
ATOM   3532  N  N     . LYS A 1 474 ? 137.221 153.673 110.440 1.00 12731. ? 474 LYS A N     1 
ATOM   3533  C  CA    . LYS A 1 474 ? 137.053 154.088 109.040 1.00 12726. ? 474 LYS A CA    1 
ATOM   3534  C  C     . LYS A 1 474 ? 136.379 155.439 109.101 1.00 12739. ? 474 LYS A C     1 
ATOM   3535  O  O     . LYS A 1 474 ? 135.644 155.688 110.040 1.00 12770. ? 474 LYS A O     1 
ATOM   3536  C  CB    . LYS A 1 474 ? 136.268 153.065 108.224 1.00 12744. ? 474 LYS A CB    1 
ATOM   3537  C  CG    . LYS A 1 474 ? 136.667 152.960 106.775 1.00 12748. ? 474 LYS A CG    1 
ATOM   3538  C  CD    . LYS A 1 474 ? 136.023 151.725 106.172 1.00 12748. ? 474 LYS A CD    1 
ATOM   3539  C  CE    . LYS A 1 474 ? 136.432 151.481 104.769 1.00 12733. ? 474 LYS A CE    1 
ATOM   3540  N  NZ    . LYS A 1 474 ? 135.898 150.185 104.356 1.00 12744. ? 474 LYS A NZ    1 
ATOM   3541  N  N     . TRP A 1 475 ? 136.652 156.273 108.123 1.00 12732. ? 475 TRP A N     1 
ATOM   3542  C  CA    . TRP A 1 475 ? 136.017 157.592 108.082 1.00 12746. ? 475 TRP A CA    1 
ATOM   3543  C  C     . TRP A 1 475 ? 134.534 157.408 107.934 1.00 12745. ? 475 TRP A C     1 
ATOM   3544  O  O     . TRP A 1 475 ? 134.101 156.349 107.498 1.00 12758. ? 475 TRP A O     1 
ATOM   3545  C  CB    . TRP A 1 475 ? 136.585 158.374 106.903 1.00 12759. ? 475 TRP A CB    1 
ATOM   3546  C  CG    . TRP A 1 475 ? 136.438 157.680 105.576 1.00 12757. ? 475 TRP A CG    1 
ATOM   3547  C  CD1   . TRP A 1 475 ? 135.478 157.906 104.637 1.00 12754. ? 475 TRP A CD1   1 
ATOM   3548  C  CD2   . TRP A 1 475 ? 137.282 156.639 105.042 1.00 12758. ? 475 TRP A CD2   1 
ATOM   3549  N  NE1   . TRP A 1 475 ? 135.668 157.090 103.556 1.00 12748. ? 475 TRP A NE1   1 
ATOM   3550  C  CE2   . TRP A 1 475 ? 136.763 156.299 103.776 1.00 12753. ? 475 TRP A CE2   1 
ATOM   3551  C  CE3   . TRP A 1 475 ? 138.417 155.967 105.504 1.00 12760. ? 475 TRP A CE3   1 
ATOM   3552  C  CZ2   . TRP A 1 475 ? 137.339 155.319 102.975 1.00 12766. ? 475 TRP A CZ2   1 
ATOM   3553  C  CZ3   . TRP A 1 475 ? 138.987 154.999 104.710 1.00 12752. ? 475 TRP A CZ3   1 
ATOM   3554  C  CH2   . TRP A 1 475 ? 138.454 154.681 103.464 1.00 12756. ? 475 TRP A CH2   1 
ATOM   3555  N  N     . HIS A 1 476 ? 133.773 158.411 108.316 1.00 12754. ? 476 HIS A N     1 
ATOM   3556  C  CA    . HIS A 1 476 ? 132.331 158.379 108.121 1.00 12752. ? 476 HIS A CA    1 
ATOM   3557  C  C     . HIS A 1 476 ? 131.999 158.441 106.637 1.00 12751. ? 476 HIS A C     1 
ATOM   3558  O  O     . HIS A 1 476 ? 132.590 159.217 105.882 1.00 12759. ? 476 HIS A O     1 
ATOM   3559  C  CB    . HIS A 1 476 ? 131.673 159.541 108.861 1.00 12762. ? 476 HIS A CB    1 
ATOM   3560  C  CG    . HIS A 1 476 ? 130.253 159.281 109.253 1.00 12755. ? 476 HIS A CG    1 
ATOM   3561  N  ND1   . HIS A 1 476 ? 129.189 159.574 108.430 1.00 12774. ? 476 HIS A ND1   1 
ATOM   3562  C  CD2   . HIS A 1 476 ? 129.723 158.754 110.381 1.00 12753. ? 476 HIS A CD2   1 
ATOM   3563  C  CE1   . HIS A 1 476 ? 128.063 159.239 109.033 1.00 12768. ? 476 HIS A CE1   1 
ATOM   3564  N  NE2   . HIS A 1 476 ? 128.359 158.738 110.218 1.00 12754. ? 476 HIS A NE2   1 
ATOM   3565  N  N     . ARG A 1 477 ? 131.045 157.610 106.219 1.00 12746. ? 477 ARG A N     1 
ATOM   3566  C  CA    . ARG A 1 477 ? 130.704 157.531 104.805 1.00 12742. ? 477 ARG A CA    1 
ATOM   3567  C  C     . ARG A 1 477 ? 129.854 158.705 104.341 1.00 12746. ? 477 ARG A C     1 
ATOM   3568  O  O     . ARG A 1 477 ? 129.780 158.957 103.134 1.00 12749. ? 477 ARG A O     1 
ATOM   3569  C  CB    . ARG A 1 477 ? 129.979 156.219 104.515 1.00 12751. ? 477 ARG A CB    1 
ATOM   3570  C  CG    . ARG A 1 477 ? 128.571 156.153 105.069 1.00 12747. ? 477 ARG A CG    1 
ATOM   3571  C  CD    . ARG A 1 477 ? 128.042 154.733 105.046 1.00 12749. ? 477 ARG A CD    1 
ATOM   3572  N  NE    . ARG A 1 477 ? 128.668 153.902 106.066 1.00 12750. ? 477 ARG A NE    1 
ATOM   3573  C  CZ    . ARG A 1 477 ? 128.257 152.685 106.394 1.00 12739. ? 477 ARG A CZ    1 
ATOM   3574  N  NH1   . ARG A 1 477 ? 127.220 152.123 105.798 1.00 12740. ? 477 ARG A NH1   1 
ATOM   3575  N  NH2   . ARG A 1 477 ? 128.903 152.017 107.345 1.00 12744. ? 477 ARG A NH2   1 
ATOM   3576  N  N     . SER A 1 478 ? 129.216 159.428 105.260 1.00 12810. ? 478 SER A N     1 
ATOM   3577  C  CA    . SER A 1 478 ? 128.322 160.523 104.904 1.00 12811. ? 478 SER A CA    1 
ATOM   3578  C  C     . SER A 1 478 ? 128.848 161.874 105.370 1.00 12832. ? 478 SER A C     1 
ATOM   3579  O  O     . SER A 1 478 ? 128.994 162.794 104.561 1.00 12835. ? 478 SER A O     1 
ATOM   3580  C  CB    . SER A 1 478 ? 126.927 160.267 105.487 1.00 12813. ? 478 SER A CB    1 
ATOM   3581  O  OG    . SER A 1 478 ? 126.456 158.979 105.133 1.00 12804. ? 478 SER A OG    1 
ATOM   3582  N  N     . LYS A 1 479 ? 129.139 162.020 106.658 1.00 13776. ? 479 LYS A N     1 
ATOM   3583  C  CA    . LYS A 1 479 ? 129.561 163.296 107.220 1.00 13846. ? 479 LYS A CA    1 
ATOM   3584  C  C     . LYS A 1 479 ? 131.082 163.374 107.214 1.00 13897. ? 479 LYS A C     1 
ATOM   3585  O  O     . LYS A 1 479 ? 131.754 162.539 107.827 1.00 13851. ? 479 LYS A O     1 
ATOM   3586  C  CB    . LYS A 1 479 ? 129.020 163.460 108.639 1.00 13830. ? 479 LYS A CB    1 
ATOM   3587  C  CG    . LYS A 1 479 ? 127.622 162.901 108.831 1.00 13807. ? 479 LYS A CG    1 
ATOM   3588  C  CD    . LYS A 1 479 ? 127.328 162.648 110.298 1.00 13816. ? 479 LYS A CD    1 
ATOM   3589  C  CE    . LYS A 1 479 ? 126.062 161.830 110.471 1.00 13827. ? 479 LYS A CE    1 
ATOM   3590  N  NZ    . LYS A 1 479 ? 125.907 161.339 111.866 1.00 13834. ? 479 LYS A NZ    1 
ATOM   3591  N  N     . GLU A 1 480 ? 131.621 164.376 106.528 1.00 16030. ? 480 GLU A N     1 
ATOM   3592  C  CA    . GLU A 1 480 ? 133.064 164.544 106.464 1.00 16065. ? 480 GLU A CA    1 
ATOM   3593  C  C     . GLU A 1 480 ? 133.611 164.990 107.814 1.00 16052. ? 480 GLU A C     1 
ATOM   3594  O  O     . GLU A 1 480 ? 132.930 165.654 108.598 1.00 16083. ? 480 GLU A O     1 
ATOM   3595  C  CB    . GLU A 1 480 ? 133.436 165.558 105.381 1.00 16107. ? 480 GLU A CB    1 
ATOM   3596  C  CG    . GLU A 1 480 ? 133.348 167.013 105.818 1.00 16149. ? 480 GLU A CG    1 
ATOM   3597  C  CD    . GLU A 1 480 ? 131.920 167.511 105.940 1.00 16156. ? 480 GLU A CD    1 
ATOM   3598  O  OE1   . GLU A 1 480 ? 130.988 166.764 105.575 1.00 16113. ? 480 GLU A OE1   1 
ATOM   3599  O  OE2   . GLU A 1 480 ? 131.730 168.655 106.404 1.00 16191. ? 480 GLU A OE2   1 
ATOM   3600  N  N     . GLY A 1 481 ? 134.852 164.598 108.091 1.00 14202. ? 481 GLY A N     1 
ATOM   3601  C  CA    . GLY A 1 481 ? 135.517 164.980 109.316 1.00 14184. ? 481 GLY A CA    1 
ATOM   3602  C  C     . GLY A 1 481 ? 135.161 164.156 110.532 1.00 14114. ? 481 GLY A C     1 
ATOM   3603  O  O     . GLY A 1 481 ? 135.714 164.407 111.610 1.00 14120. ? 481 GLY A O     1 
ATOM   3604  N  N     . LEU A 1 482 ? 134.266 163.183 110.400 1.00 12934. ? 482 LEU A N     1 
ATOM   3605  C  CA    . LEU A 1 482 ? 133.875 162.314 111.496 1.00 12875. ? 482 LEU A CA    1 
ATOM   3606  C  C     . LEU A 1 482 ? 134.270 160.880 111.175 1.00 12853. ? 482 LEU A C     1 
ATOM   3607  O  O     . LEU A 1 482 ? 134.522 160.527 110.020 1.00 12856. ? 482 LEU A O     1 
ATOM   3608  C  CB    . LEU A 1 482 ? 132.368 162.395 111.766 1.00 12864. ? 482 LEU A CB    1 
ATOM   3609  C  CG    . LEU A 1 482 ? 131.813 163.773 112.122 1.00 12895. ? 482 LEU A CG    1 
ATOM   3610  C  CD1   . LEU A 1 482 ? 130.315 163.707 112.333 1.00 12872. ? 482 LEU A CD1   1 
ATOM   3611  C  CD2   . LEU A 1 482 ? 132.500 164.325 113.355 1.00 12893. ? 482 LEU A CD2   1 
ATOM   3612  N  N     . THR A 1 483 ? 134.329 160.055 112.210 1.00 12768. ? 483 THR A N     1 
ATOM   3613  C  CA    . THR A 1 483 ? 134.692 158.658 112.060 1.00 12735. ? 483 THR A CA    1 
ATOM   3614  C  C     . THR A 1 483 ? 133.465 157.777 112.285 1.00 12737. ? 483 THR A C     1 
ATOM   3615  O  O     . THR A 1 483 ? 132.340 158.264 112.429 1.00 12758. ? 483 THR A O     1 
ATOM   3616  C  CB    . THR A 1 483 ? 135.836 158.301 113.007 1.00 12767. ? 483 THR A CB    1 
ATOM   3617  O  OG1   . THR A 1 483 ? 136.209 156.935 112.804 1.00 12766. ? 483 THR A OG1   1 
ATOM   3618  C  CG2   . THR A 1 483 ? 135.415 158.489 114.440 1.00 12778. ? 483 THR A CG2   1 
ATOM   3619  N  N     . GLU A 1 484 ? 133.687 156.466 112.313 1.00 12734. ? 484 GLU A N     1 
ATOM   3620  C  CA    . GLU A 1 484 ? 132.593 155.505 112.306 1.00 12736. ? 484 GLU A CA    1 
ATOM   3621  C  C     . GLU A 1 484 ? 132.606 154.626 113.547 1.00 12740. ? 484 GLU A C     1 
ATOM   3622  O  O     . GLU A 1 484 ? 132.497 153.400 113.445 1.00 12750. ? 484 GLU A O     1 
ATOM   3623  C  CB    . GLU A 1 484 ? 132.657 154.638 111.050 1.00 12750. ? 484 GLU A CB    1 
ATOM   3624  C  CG    . GLU A 1 484 ? 131.828 155.167 109.897 1.00 12749. ? 484 GLU A CG    1 
ATOM   3625  C  CD    . GLU A 1 484 ? 131.213 154.062 109.069 1.00 12743. ? 484 GLU A CD    1 
ATOM   3626  O  OE1   . GLU A 1 484 ? 131.462 152.879 109.378 1.00 12742. ? 484 GLU A OE1   1 
ATOM   3627  O  OE2   . GLU A 1 484 ? 130.478 154.375 108.110 1.00 12755. ? 484 GLU A OE2   1 
ATOM   3628  N  N     . ARG A 1 485 ? 132.752 155.234 114.718 1.00 12735. ? 485 ARG A N     1 
ATOM   3629  C  CA    . ARG A 1 485 ? 132.838 154.507 115.973 1.00 12730. ? 485 ARG A CA    1 
ATOM   3630  C  C     . ARG A 1 485 ? 131.675 154.872 116.882 1.00 12725. ? 485 ARG A C     1 
ATOM   3631  O  O     . ARG A 1 485 ? 130.931 155.823 116.636 1.00 12751. ? 485 ARG A O     1 
ATOM   3632  C  CB    . ARG A 1 485 ? 134.152 154.809 116.691 1.00 12745. ? 485 ARG A CB    1 
ATOM   3633  C  CG    . ARG A 1 485 ? 134.367 156.275 116.949 1.00 12751. ? 485 ARG A CG    1 
ATOM   3634  C  CD    . ARG A 1 485 ? 135.609 156.501 117.772 1.00 12762. ? 485 ARG A CD    1 
ATOM   3635  N  NE    . ARG A 1 485 ? 135.696 155.570 118.888 1.00 12755. ? 485 ARG A NE    1 
ATOM   3636  C  CZ    . ARG A 1 485 ? 136.295 155.842 120.039 1.00 12762. ? 485 ARG A CZ    1 
ATOM   3637  N  NH1   . ARG A 1 485 ? 136.880 157.008 120.253 1.00 12772. ? 485 ARG A NH1   1 
ATOM   3638  N  NH2   . ARG A 1 485 ? 136.307 154.922 120.997 1.00 12758. ? 485 ARG A NH2   1 
ATOM   3639  N  N     . PHE A 1 486 ? 131.535 154.094 117.953 1.00 12714. ? 486 PHE A N     1 
ATOM   3640  C  CA    . PHE A 1 486 ? 130.590 154.406 119.012 1.00 12723. ? 486 PHE A CA    1 
ATOM   3641  C  C     . PHE A 1 486 ? 131.136 153.878 120.329 1.00 12735. ? 486 PHE A C     1 
ATOM   3642  O  O     . PHE A 1 486 ? 131.903 152.914 120.359 1.00 12755. ? 486 PHE A O     1 
ATOM   3643  C  CB    . PHE A 1 486 ? 129.200 153.820 118.732 1.00 12739. ? 486 PHE A CB    1 
ATOM   3644  C  CG    . PHE A 1 486 ? 129.134 152.322 118.823 1.00 12730. ? 486 PHE A CG    1 
ATOM   3645  C  CD1   . PHE A 1 486 ? 128.881 151.693 120.030 1.00 12736. ? 486 PHE A CD1   1 
ATOM   3646  C  CD2   . PHE A 1 486 ? 129.312 151.542 117.698 1.00 12745. ? 486 PHE A CD2   1 
ATOM   3647  C  CE1   . PHE A 1 486 ? 128.816 150.322 120.112 1.00 12742. ? 486 PHE A CE1   1 
ATOM   3648  C  CE2   . PHE A 1 486 ? 129.243 150.169 117.775 1.00 12746. ? 486 PHE A CE2   1 
ATOM   3649  C  CZ    . PHE A 1 486 ? 128.995 149.559 118.984 1.00 12742. ? 486 PHE A CZ    1 
ATOM   3650  N  N     . GLU A 1 487 ? 130.728 154.523 121.416 1.00 12738. ? 487 GLU A N     1 
ATOM   3651  C  CA    . GLU A 1 487 ? 131.089 154.115 122.766 1.00 12734. ? 487 GLU A CA    1 
ATOM   3652  C  C     . GLU A 1 487 ? 129.824 153.959 123.595 1.00 12732. ? 487 GLU A C     1 
ATOM   3653  O  O     . GLU A 1 487 ? 128.948 154.829 123.565 1.00 12753. ? 487 GLU A O     1 
ATOM   3654  C  CB    . GLU A 1 487 ? 132.025 155.130 123.421 1.00 12737. ? 487 GLU A CB    1 
ATOM   3655  C  CG    . GLU A 1 487 ? 133.198 155.533 122.557 1.00 12748. ? 487 GLU A CG    1 
ATOM   3656  C  CD    . GLU A 1 487 ? 134.274 156.250 123.340 1.00 12747. ? 487 GLU A CD    1 
ATOM   3657  O  OE1   . GLU A 1 487 ? 134.335 156.061 124.572 1.00 12747. ? 487 GLU A OE1   1 
ATOM   3658  O  OE2   . GLU A 1 487 ? 135.061 157.001 122.728 1.00 12759. ? 487 GLU A OE2   1 
ATOM   3659  N  N     . LEU A 1 488 ? 129.731 152.854 124.326 1.00 12727. ? 488 LEU A N     1 
ATOM   3660  C  CA    . LEU A 1 488 ? 128.604 152.595 125.210 1.00 12727. ? 488 LEU A CA    1 
ATOM   3661  C  C     . LEU A 1 488 ? 128.972 153.048 126.615 1.00 12740. ? 488 LEU A C     1 
ATOM   3662  O  O     . LEU A 1 488 ? 129.985 152.606 127.172 1.00 12771. ? 488 LEU A O     1 
ATOM   3663  C  CB    . LEU A 1 488 ? 128.220 151.117 125.204 1.00 12738. ? 488 LEU A CB    1 
ATOM   3664  C  CG    . LEU A 1 488 ? 127.037 150.758 126.102 1.00 12733. ? 488 LEU A CG    1 
ATOM   3665  C  CD1   . LEU A 1 488 ? 125.801 151.524 125.677 1.00 12760. ? 488 LEU A CD1   1 
ATOM   3666  C  CD2   . LEU A 1 488 ? 126.775 149.268 126.074 1.00 12743. ? 488 LEU A CD2   1 
ATOM   3667  N  N     . PHE A 1 489 ? 128.156 153.935 127.177 1.00 12739. ? 489 PHE A N     1 
ATOM   3668  C  CA    . PHE A 1 489 ? 128.388 154.498 128.497 1.00 12741. ? 489 PHE A CA    1 
ATOM   3669  C  C     . PHE A 1 489 ? 127.241 154.103 129.410 1.00 12746. ? 489 PHE A C     1 
ATOM   3670  O  O     . PHE A 1 489 ? 126.074 154.363 129.098 1.00 12766. ? 489 PHE A O     1 
ATOM   3671  C  CB    . PHE A 1 489 ? 128.530 156.018 128.427 1.00 12748. ? 489 PHE A CB    1 
ATOM   3672  C  CG    . PHE A 1 489 ? 129.913 156.467 128.086 1.00 12747. ? 489 PHE A CG    1 
ATOM   3673  C  CD1   . PHE A 1 489 ? 130.310 156.581 126.768 1.00 12764. ? 489 PHE A CD1   1 
ATOM   3674  C  CD2   . PHE A 1 489 ? 130.825 156.750 129.083 1.00 12757. ? 489 PHE A CD2   1 
ATOM   3675  C  CE1   . PHE A 1 489 ? 131.585 156.980 126.449 1.00 12772. ? 489 PHE A CE1   1 
ATOM   3676  C  CE2   . PHE A 1 489 ? 132.103 157.148 128.772 1.00 12775. ? 489 PHE A CE2   1 
ATOM   3677  C  CZ    . PHE A 1 489 ? 132.486 157.257 127.451 1.00 12773. ? 489 PHE A CZ    1 
ATOM   3678  N  N     . VAL A 1 490 ? 127.577 153.468 130.526 1.00 12744. ? 490 VAL A N     1 
ATOM   3679  C  CA    . VAL A 1 490 ? 126.627 153.128 131.574 1.00 12736. ? 490 VAL A CA    1 
ATOM   3680  C  C     . VAL A 1 490 ? 127.098 153.802 132.851 1.00 12733. ? 490 VAL A C     1 
ATOM   3681  O  O     . VAL A 1 490 ? 128.274 153.690 133.217 1.00 12744. ? 490 VAL A O     1 
ATOM   3682  C  CB    . VAL A 1 490 ? 126.510 151.606 131.767 1.00 12741. ? 490 VAL A CB    1 
ATOM   3683  C  CG1   . VAL A 1 490 ? 125.497 151.287 132.848 1.00 12757. ? 490 VAL A CG1   1 
ATOM   3684  C  CG2   . VAL A 1 490 ? 126.130 150.936 130.463 1.00 12751. ? 490 VAL A CG2   1 
ATOM   3685  N  N     . MET A 1 491 ? 126.189 154.515 133.510 1.00 12735. ? 491 MET A N     1 
ATOM   3686  C  CA    . MET A 1 491 ? 126.468 155.172 134.783 1.00 12742. ? 491 MET A CA    1 
ATOM   3687  C  C     . MET A 1 491 ? 127.719 156.045 134.674 1.00 12741. ? 491 MET A C     1 
ATOM   3688  O  O     . MET A 1 491 ? 128.633 155.988 135.499 1.00 12751. ? 491 MET A O     1 
ATOM   3689  C  CB    . MET A 1 491 ? 126.589 154.137 135.905 1.00 12740. ? 491 MET A CB    1 
ATOM   3690  C  CG    . MET A 1 491 ? 126.639 154.715 137.308 1.00 12742. ? 491 MET A CG    1 
ATOM   3691  S  SD    . MET A 1 491 ? 125.008 155.128 137.945 1.00 12718. ? 491 MET A SD    1 
ATOM   3692  C  CE    . MET A 1 491 ? 125.116 156.912 137.981 1.00 12756. ? 491 MET A CE    1 
ATOM   3693  N  N     . LYS A 1 492 ? 127.764 156.839 133.605 1.00 12751. ? 492 LYS A N     1 
ATOM   3694  C  CA    . LYS A 1 492 ? 128.833 157.799 133.338 1.00 12752. ? 492 LYS A CA    1 
ATOM   3695  C  C     . LYS A 1 492 ? 130.194 157.136 133.145 1.00 12745. ? 492 LYS A C     1 
ATOM   3696  O  O     . LYS A 1 492 ? 131.226 157.801 133.262 1.00 12746. ? 492 LYS A O     1 
ATOM   3697  C  CB    . LYS A 1 492 ? 128.923 158.856 134.445 1.00 12749. ? 492 LYS A CB    1 
ATOM   3698  C  CG    . LYS A 1 492 ? 127.584 159.403 134.899 1.00 12773. ? 492 LYS A CG    1 
ATOM   3699  C  CD    . LYS A 1 492 ? 127.767 160.636 135.762 1.00 12783. ? 492 LYS A CD    1 
ATOM   3700  C  CE    . LYS A 1 492 ? 126.546 160.897 136.621 1.00 12767. ? 492 LYS A CE    1 
ATOM   3701  N  NZ    . LYS A 1 492 ? 126.560 160.073 137.858 1.00 12749. ? 492 LYS A NZ    1 
ATOM   3702  N  N     . LYS A 1 493 ? 130.233 155.840 132.846 1.00 12742. ? 493 LYS A N     1 
ATOM   3703  C  CA    . LYS A 1 493 ? 131.491 155.140 132.633 1.00 12731. ? 493 LYS A CA    1 
ATOM   3704  C  C     . LYS A 1 493 ? 131.422 154.334 131.346 1.00 12743. ? 493 LYS A C     1 
ATOM   3705  O  O     . LYS A 1 493 ? 130.402 153.708 131.051 1.00 12765. ? 493 LYS A O     1 
ATOM   3706  C  CB    . LYS A 1 493 ? 131.824 154.217 133.808 1.00 12744. ? 493 LYS A CB    1 
ATOM   3707  C  CG    . LYS A 1 493 ? 132.181 154.946 135.090 1.00 12751. ? 493 LYS A CG    1 
ATOM   3708  C  CD    . LYS A 1 493 ? 133.349 155.891 134.879 1.00 12749. ? 493 LYS A CD    1 
ATOM   3709  C  CE    . LYS A 1 493 ? 133.758 156.563 136.176 1.00 12743. ? 493 LYS A CE    1 
ATOM   3710  N  NZ    . LYS A 1 493 ? 132.580 156.940 136.997 1.00 12752. ? 493 LYS A NZ    1 
ATOM   3711  N  N     . GLU A 1 494 ? 132.512 154.350 130.584 1.00 12743. ? 494 GLU A N     1 
ATOM   3712  C  CA    . GLU A 1 494 ? 132.572 153.626 129.322 1.00 12742. ? 494 GLU A CA    1 
ATOM   3713  C  C     . GLU A 1 494 ? 132.770 152.141 129.580 1.00 12739. ? 494 GLU A C     1 
ATOM   3714  O  O     . GLU A 1 494 ? 133.690 151.750 130.304 1.00 12756. ? 494 GLU A O     1 
ATOM   3715  C  CB    . GLU A 1 494 ? 133.710 154.162 128.457 1.00 12744. ? 494 GLU A CB    1 
ATOM   3716  C  CG    . GLU A 1 494 ? 133.778 153.561 127.070 1.00 12754. ? 494 GLU A CG    1 
ATOM   3717  C  CD    . GLU A 1 494 ? 135.193 153.512 126.531 1.00 12756. ? 494 GLU A CD    1 
ATOM   3718  O  OE1   . GLU A 1 494 ? 135.845 154.575 126.473 1.00 12755. ? 494 GLU A OE1   1 
ATOM   3719  O  OE2   . GLU A 1 494 ? 135.654 152.413 126.163 1.00 12756. ? 494 GLU A OE2   1 
ATOM   3720  N  N     . ILE A 1 495 ? 131.913 151.312 128.990 1.00 12734. ? 495 ILE A N     1 
ATOM   3721  C  CA    . ILE A 1 495 ? 132.062 149.869 129.111 1.00 12737. ? 495 ILE A CA    1 
ATOM   3722  C  C     . ILE A 1 495 ? 132.353 149.189 127.779 1.00 12746. ? 495 ILE A C     1 
ATOM   3723  O  O     . ILE A 1 495 ? 133.062 148.169 127.768 1.00 12758. ? 495 ILE A O     1 
ATOM   3724  C  CB    . ILE A 1 495 ? 130.827 149.229 129.778 1.00 12739. ? 495 ILE A CB    1 
ATOM   3725  C  CG1   . ILE A 1 495 ? 129.586 149.407 128.908 1.00 12750. ? 495 ILE A CG1   1 
ATOM   3726  C  CG2   . ILE A 1 495 ? 130.599 149.825 131.151 1.00 12749. ? 495 ILE A CG2   1 
ATOM   3727  C  CD1   . ILE A 1 495 ? 128.480 148.439 129.238 1.00 12755. ? 495 ILE A CD1   1 
ATOM   3728  N  N     . CYS A 1 496 ? 131.863 149.727 126.664 1.00 12750. ? 496 CYS A N     1 
ATOM   3729  C  CA    . CYS A 1 496 ? 132.074 149.142 125.350 1.00 12744. ? 496 CYS A CA    1 
ATOM   3730  C  C     . CYS A 1 496 ? 132.763 150.159 124.457 1.00 12738. ? 496 CYS A C     1 
ATOM   3731  O  O     . CYS A 1 496 ? 132.747 151.364 124.715 1.00 12749. ? 496 CYS A O     1 
ATOM   3732  C  CB    . CYS A 1 496 ? 130.760 148.701 124.693 1.00 12744. ? 496 CYS A CB    1 
ATOM   3733  S  SG    . CYS A 1 496 ? 129.829 147.440 125.568 1.00 12735. ? 496 CYS A SG    1 
ATOM   3734  N  N     . ASN A 1 497 ? 133.367 149.657 123.376 1.00 12734. ? 497 ASN A N     1 
ATOM   3735  C  CA    . ASN A 1 497 ? 134.070 150.545 122.411 1.00 12732. ? 497 ASN A CA    1 
ATOM   3736  C  C     . ASN A 1 497 ? 134.162 149.800 121.076 1.00 12740. ? 497 ASN A C     1 
ATOM   3737  O  O     . ASN A 1 497 ? 134.794 148.723 121.050 1.00 12759. ? 497 ASN A O     1 
ATOM   3738  C  CB    . ASN A 1 497 ? 135.438 150.961 122.938 1.00 12750. ? 497 ASN A CB    1 
ATOM   3739  C  CG    . ASN A 1 497 ? 136.099 152.006 122.072 1.00 12743. ? 497 ASN A CG    1 
ATOM   3740  O  OD1   . ASN A 1 497 ? 135.521 152.446 121.071 1.00 12737. ? 497 ASN A OD1   1 
ATOM   3741  N  ND2   . ASN A 1 497 ? 137.302 152.419 122.441 1.00 12741. ? 497 ASN A ND2   1 
ATOM   3742  N  N     . ALA A 1 498 ? 133.544 150.336 120.019 1.00 12741. ? 498 ALA A N     1 
ATOM   3743  C  CA    . ALA A 1 498 ? 133.524 149.614 118.723 1.00 12743. ? 498 ALA A CA    1 
ATOM   3744  C  C     . ALA A 1 498 ? 133.562 150.601 117.554 1.00 12736. ? 498 ALA A C     1 
ATOM   3745  O  O     . ALA A 1 498 ? 132.975 151.698 117.675 1.00 12751. ? 498 ALA A O     1 
ATOM   3746  C  CB    . ALA A 1 498 ? 132.298 148.734 118.654 1.00 12743. ? 498 ALA A CB    1 
ATOM   3747  N  N     . TYR A 1 499 ? 134.220 150.214 116.456 1.00 12725. ? 499 TYR A N     1 
ATOM   3748  C  CA    . TYR A 1 499 ? 134.295 151.089 115.252 1.00 12723. ? 499 TYR A CA    1 
ATOM   3749  C  C     . TYR A 1 499 ? 134.565 150.247 114.010 1.00 12730. ? 499 TYR A C     1 
ATOM   3750  O  O     . TYR A 1 499 ? 135.086 149.117 114.137 1.00 12752. ? 499 TYR A O     1 
ATOM   3751  C  CB    . TYR A 1 499 ? 135.383 152.160 115.384 1.00 12743. ? 499 TYR A CB    1 
ATOM   3752  C  CG    . TYR A 1 499 ? 136.617 151.794 116.198 1.00 12745. ? 499 TYR A CG    1 
ATOM   3753  C  CD1   . TYR A 1 499 ? 136.667 152.024 117.568 1.00 12748. ? 499 TYR A CD1   1 
ATOM   3754  C  CD2   . TYR A 1 499 ? 137.738 151.242 115.592 1.00 12753. ? 499 TYR A CD2   1 
ATOM   3755  C  CE1   . TYR A 1 499 ? 137.788 151.701 118.313 1.00 12760. ? 499 TYR A CE1   1 
ATOM   3756  C  CE2   . TYR A 1 499 ? 138.867 150.921 116.326 1.00 12756. ? 499 TYR A CE2   1 
ATOM   3757  C  CZ    . TYR A 1 499 ? 138.892 151.148 117.690 1.00 12758. ? 499 TYR A CZ    1 
ATOM   3758  O  OH    . TYR A 1 499 ? 140.001 150.827 118.418 1.00 12738. ? 499 TYR A OH    1 
ATOM   3759  N  N     . THR A 1 500 ? 134.223 150.783 112.834 1.00 12723. ? 500 THR A N     1 
ATOM   3760  C  CA    . THR A 1 500 ? 134.520 150.073 111.572 1.00 12735. ? 500 THR A CA    1 
ATOM   3761  C  C     . THR A 1 500 ? 136.018 150.097 111.370 1.00 12743. ? 500 THR A C     1 
ATOM   3762  O  O     . THR A 1 500 ? 136.597 151.204 111.410 1.00 12749. ? 500 THR A O     1 
ATOM   3763  C  CB    . THR A 1 500 ? 133.775 150.737 110.416 1.00 12738. ? 500 THR A CB    1 
ATOM   3764  O  OG1   . THR A 1 500 ? 132.407 150.748 110.812 1.00 12752. ? 500 THR A OG1   1 
ATOM   3765  C  CG2   . THR A 1 500 ? 133.933 149.980 109.110 1.00 12744. ? 500 THR A CG2   1 
ATOM   3766  N  N     . GLU A 1 501 ? 136.636 148.932 111.164 1.00 12743. ? 501 GLU A N     1 
ATOM   3767  C  CA    . GLU A 1 501 ? 138.085 148.869 111.050 1.00 12737. ? 501 GLU A CA    1 
ATOM   3768  C  C     . GLU A 1 501 ? 138.564 149.484 109.742 1.00 12740. ? 501 GLU A C     1 
ATOM   3769  O  O     . GLU A 1 501 ? 137.966 149.280 108.682 1.00 12748. ? 501 GLU A O     1 
ATOM   3770  C  CB    . GLU A 1 501 ? 138.557 147.424 111.157 1.00 12739. ? 501 GLU A CB    1 
ATOM   3771  C  CG    . GLU A 1 501 ? 138.237 146.786 112.492 1.00 12766. ? 501 GLU A CG    1 
ATOM   3772  C  CD    . GLU A 1 501 ? 138.723 147.616 113.663 1.00 12770. ? 501 GLU A CD    1 
ATOM   3773  O  OE1   . GLU A 1 501 ? 139.925 147.951 113.700 1.00 12767. ? 501 GLU A OE1   1 
ATOM   3774  O  OE2   . GLU A 1 501 ? 137.904 147.932 114.549 1.00 12771. ? 501 GLU A OE2   1 
ATOM   3775  N  N     . LEU A 1 502 ? 139.653 150.241 109.828 1.00 12749. ? 502 LEU A N     1 
ATOM   3776  C  CA    . LEU A 1 502 ? 140.255 150.854 108.652 1.00 12739. ? 502 LEU A CA    1 
ATOM   3777  C  C     . LEU A 1 502 ? 141.061 149.813 107.887 1.00 12732. ? 502 LEU A C     1 
ATOM   3778  O  O     . LEU A 1 502 ? 142.080 149.321 108.382 1.00 12751. ? 502 LEU A O     1 
ATOM   3779  C  CB    . LEU A 1 502 ? 141.143 152.021 109.074 1.00 12760. ? 502 LEU A CB    1 
ATOM   3780  C  CG    . LEU A 1 502 ? 141.906 152.770 107.983 1.00 12747. ? 502 LEU A CG    1 
ATOM   3781  C  CD1   . LEU A 1 502 ? 140.976 153.184 106.859 1.00 12739. ? 502 LEU A CD1   1 
ATOM   3782  C  CD2   . LEU A 1 502 ? 142.605 153.978 108.573 1.00 12786. ? 502 LEU A CD2   1 
ATOM   3783  N  N     . ASN A 1 503 ? 140.608 149.475 106.681 1.00 12733. ? 503 ASN A N     1 
ATOM   3784  C  CA    . ASN A 1 503 ? 141.254 148.454 105.868 1.00 12742. ? 503 ASN A CA    1 
ATOM   3785  C  C     . ASN A 1 503 ? 142.064 149.038 104.718 1.00 12741. ? 503 ASN A C     1 
ATOM   3786  O  O     . ASN A 1 503 ? 142.479 148.292 103.826 1.00 12746. ? 503 ASN A O     1 
ATOM   3787  C  CB    . ASN A 1 503 ? 140.216 147.468 105.329 1.00 12748. ? 503 ASN A CB    1 
ATOM   3788  C  CG    . ASN A 1 503 ? 139.078 148.156 104.616 1.00 12747. ? 503 ASN A CG    1 
ATOM   3789  O  OD1   . ASN A 1 503 ? 138.941 149.376 104.677 1.00 12758. ? 503 ASN A OD1   1 
ATOM   3790  N  ND2   . ASN A 1 503 ? 138.254 147.377 103.927 1.00 12745. ? 503 ASN A ND2   1 
ATOM   3791  N  N     . ASP A 1 504 ? 142.299 150.350 104.713 1.00 12738. ? 504 ASP A N     1 
ATOM   3792  C  CA    . ASP A 1 504 ? 143.094 150.979 103.668 1.00 12741. ? 504 ASP A CA    1 
ATOM   3793  C  C     . ASP A 1 504 ? 144.556 150.966 104.090 1.00 12754. ? 504 ASP A C     1 
ATOM   3794  O  O     . ASP A 1 504 ? 144.910 151.642 105.068 1.00 12782. ? 504 ASP A O     1 
ATOM   3795  C  CB    . ASP A 1 504 ? 142.624 152.404 103.422 1.00 12751. ? 504 ASP A CB    1 
ATOM   3796  C  CG    . ASP A 1 504 ? 143.221 153.009 102.169 1.00 12765. ? 504 ASP A CG    1 
ATOM   3797  O  OD1   . ASP A 1 504 ? 144.012 152.326 101.489 1.00 12775. ? 504 ASP A OD1   1 
ATOM   3798  O  OD2   . ASP A 1 504 ? 142.897 154.174 101.860 1.00 12765. ? 504 ASP A OD2   1 
ATOM   3799  N  N     . PRO A 1 505 ? 145.429 150.221 103.408 1.00 12747. ? 505 PRO A N     1 
ATOM   3800  C  CA    . PRO A 1 505 ? 146.834 150.166 103.847 1.00 12755. ? 505 PRO A CA    1 
ATOM   3801  C  C     . PRO A 1 505 ? 147.546 151.508 103.814 1.00 12781. ? 505 PRO A C     1 
ATOM   3802  O  O     . PRO A 1 505 ? 148.368 151.787 104.694 1.00 12814. ? 505 PRO A O     1 
ATOM   3803  C  CB    . PRO A 1 505 ? 147.448 149.156 102.868 1.00 12745. ? 505 PRO A CB    1 
ATOM   3804  C  CG    . PRO A 1 505 ? 146.585 149.259 101.659 1.00 12754. ? 505 PRO A CG    1 
ATOM   3805  C  CD    . PRO A 1 505 ? 145.204 149.385 102.219 1.00 12754. ? 505 PRO A CD    1 
ATOM   3806  N  N     . MET A 1 506 ? 147.250 152.355 102.827 1.00 13324. ? 506 MET A N     1 
ATOM   3807  C  CA    . MET A 1 506 ? 147.974 153.616 102.698 1.00 13345. ? 506 MET A CA    1 
ATOM   3808  C  C     . MET A 1 506 ? 147.635 154.571 103.835 1.00 13363. ? 506 MET A C     1 
ATOM   3809  O  O     . MET A 1 506 ? 148.530 155.143 104.471 1.00 13390. ? 506 MET A O     1 
ATOM   3810  C  CB    . MET A 1 506 ? 147.670 154.255 101.345 1.00 13370. ? 506 MET A CB    1 
ATOM   3811  C  CG    . MET A 1 506 ? 147.686 153.273 100.190 1.00 13373. ? 506 MET A CG    1 
ATOM   3812  S  SD    . MET A 1 506 ? 149.340 153.052 99.508  1.00 13372. ? 506 MET A SD    1 
ATOM   3813  C  CE    . MET A 1 506 ? 149.484 151.267 99.528  1.00 13370. ? 506 MET A CE    1 
ATOM   3814  N  N     . ARG A 1 507 ? 146.343 154.757 104.111 1.00 13132. ? 507 ARG A N     1 
ATOM   3815  C  CA    . ARG A 1 507 ? 145.953 155.657 105.189 1.00 13138. ? 507 ARG A CA    1 
ATOM   3816  C  C     . ARG A 1 507 ? 146.378 155.111 106.545 1.00 13167. ? 507 ARG A C     1 
ATOM   3817  O  O     . ARG A 1 507 ? 146.795 155.873 107.425 1.00 13198. ? 507 ARG A O     1 
ATOM   3818  C  CB    . ARG A 1 507 ? 144.447 155.906 105.154 1.00 13124. ? 507 ARG A CB    1 
ATOM   3819  C  CG    . ARG A 1 507 ? 144.018 157.125 105.949 1.00 13134. ? 507 ARG A CG    1 
ATOM   3820  C  CD    . ARG A 1 507 ? 142.610 157.557 105.587 1.00 13136. ? 507 ARG A CD    1 
ATOM   3821  N  NE    . ARG A 1 507 ? 142.342 157.390 104.164 1.00 13136. ? 507 ARG A NE    1 
ATOM   3822  C  CZ    . ARG A 1 507 ? 141.216 157.753 103.566 1.00 13136. ? 507 ARG A CZ    1 
ATOM   3823  N  NH1   . ARG A 1 507 ? 140.230 158.324 104.238 1.00 13131. ? 507 ARG A NH1   1 
ATOM   3824  N  NH2   . ARG A 1 507 ? 141.077 157.541 102.261 1.00 13139. ? 507 ARG A NH2   1 
ATOM   3825  N  N     . GLN A 1 508 ? 146.275 153.795 106.736 1.00 13382. ? 508 GLN A N     1 
ATOM   3826  C  CA    . GLN A 1 508 ? 146.725 153.199 107.988 1.00 13386. ? 508 GLN A CA    1 
ATOM   3827  C  C     . GLN A 1 508 ? 148.219 153.406 108.183 1.00 13421. ? 508 GLN A C     1 
ATOM   3828  O  O     . GLN A 1 508 ? 148.672 153.720 109.288 1.00 13460. ? 508 GLN A O     1 
ATOM   3829  C  CB    . GLN A 1 508 ? 146.382 151.712 108.021 1.00 13371. ? 508 GLN A CB    1 
ATOM   3830  C  CG    . GLN A 1 508 ? 146.779 151.036 109.317 1.00 13389. ? 508 GLN A CG    1 
ATOM   3831  C  CD    . GLN A 1 508 ? 145.687 151.099 110.360 1.00 13394. ? 508 GLN A CD    1 
ATOM   3832  O  OE1   . GLN A 1 508 ? 144.745 150.309 110.337 1.00 13394. ? 508 GLN A OE1   1 
ATOM   3833  N  NE2   . GLN A 1 508 ? 145.801 152.049 111.279 1.00 13415. ? 508 GLN A NE2   1 
ATOM   3834  N  N     . ARG A 1 509 ? 149.004 153.233 107.117 1.00 13891. ? 509 ARG A N     1 
ATOM   3835  C  CA    . ARG A 1 509 ? 150.437 153.482 107.210 1.00 13913. ? 509 ARG A CA    1 
ATOM   3836  C  C     . ARG A 1 509 ? 150.729 154.944 107.512 1.00 13960. ? 509 ARG A C     1 
ATOM   3837  O  O     . ARG A 1 509 ? 151.639 155.245 108.290 1.00 14009. ? 509 ARG A O     1 
ATOM   3838  C  CB    . ARG A 1 509 ? 151.128 153.054 105.917 1.00 13922. ? 509 ARG A CB    1 
ATOM   3839  C  CG    . ARG A 1 509 ? 152.641 153.040 106.005 1.00 13949. ? 509 ARG A CG    1 
ATOM   3840  C  CD    . ARG A 1 509 ? 153.267 152.647 104.678 1.00 13943. ? 509 ARG A CD    1 
ATOM   3841  N  NE    . ARG A 1 509 ? 153.111 151.227 104.388 1.00 13913. ? 509 ARG A NE    1 
ATOM   3842  C  CZ    . ARG A 1 509 ? 153.787 150.258 104.991 1.00 13923. ? 509 ARG A CZ    1 
ATOM   3843  N  NH1   . ARG A 1 509 ? 154.682 150.519 105.930 1.00 13952. ? 509 ARG A NH1   1 
ATOM   3844  N  NH2   . ARG A 1 509 ? 153.563 148.995 104.640 1.00 13918. ? 509 ARG A NH2   1 
ATOM   3845  N  N     . GLN A 1 510 ? 149.972 155.864 106.909 1.00 14296. ? 510 GLN A N     1 
ATOM   3846  C  CA    . GLN A 1 510 ? 150.164 157.283 107.197 1.00 14329. ? 510 GLN A CA    1 
ATOM   3847  C  C     . GLN A 1 510 ? 149.899 157.590 108.666 1.00 14345. ? 510 GLN A C     1 
ATOM   3848  O  O     . GLN A 1 510 ? 150.685 158.288 109.318 0.76 14376. ? 510 GLN A O     1 
ATOM   3849  C  CB    . GLN A 1 510 ? 149.256 158.126 106.304 1.00 14323. ? 510 GLN A CB    1 
ATOM   3850  C  CG    . GLN A 1 510 ? 149.789 158.351 104.903 1.00 14334. ? 510 GLN A CG    1 
ATOM   3851  C  CD    . GLN A 1 510 ? 148.817 159.126 104.038 1.00 14334. ? 510 GLN A CD    1 
ATOM   3852  O  OE1   . GLN A 1 510 ? 147.710 159.449 104.467 1.00 14320. ? 510 GLN A OE1   1 
ATOM   3853  N  NE2   . GLN A 1 510 ? 149.226 159.429 102.813 1.00 14341. ? 510 GLN A NE2   1 
ATOM   3854  N  N     . LEU A 1 511 ? 148.790 157.077 109.205 1.00 14274. ? 511 LEU A N     1 
ATOM   3855  C  CA    . LEU A 1 511 ? 148.479 157.320 110.611 1.00 14285. ? 511 LEU A CA    1 
ATOM   3856  C  C     . LEU A 1 511 ? 149.506 156.670 111.530 1.00 14319. ? 511 LEU A C     1 
ATOM   3857  O  O     . LEU A 1 511 ? 149.891 157.255 112.549 1.00 14373. ? 511 LEU A O     1 
ATOM   3858  C  CB    . LEU A 1 511 ? 147.070 156.828 110.940 1.00 14272. ? 511 LEU A CB    1 
ATOM   3859  C  CG    . LEU A 1 511 ? 145.945 157.370 110.058 1.00 14271. ? 511 LEU A CG    1 
ATOM   3860  C  CD1   . LEU A 1 511 ? 144.627 156.693 110.386 1.00 14287. ? 511 LEU A CD1   1 
ATOM   3861  C  CD2   . LEU A 1 511 ? 145.831 158.874 110.210 1.00 14280. ? 511 LEU A CD2   1 
ATOM   3862  N  N     . PHE A 1 512 ? 149.962 155.463 111.189 1.00 14284. ? 512 PHE A N     1 
ATOM   3863  C  CA    . PHE A 1 512 ? 150.985 154.804 111.992 1.00 14292. ? 512 PHE A CA    1 
ATOM   3864  C  C     . PHE A 1 512 ? 152.286 155.591 111.996 1.00 14359. ? 512 PHE A C     1 
ATOM   3865  O  O     . PHE A 1 512 ? 152.921 155.730 113.046 1.00 14389. ? 512 PHE A O     1 
ATOM   3866  C  CB    . PHE A 1 512 ? 151.226 153.387 111.475 1.00 14272. ? 512 PHE A CB    1 
ATOM   3867  C  CG    . PHE A 1 512 ? 150.351 152.352 112.116 1.00 14256. ? 512 PHE A CG    1 
ATOM   3868  C  CD1   . PHE A 1 512 ? 149.135 152.704 112.673 1.00 14242. ? 512 PHE A CD1   1 
ATOM   3869  C  CD2   . PHE A 1 512 ? 150.741 151.026 112.156 1.00 14266. ? 512 PHE A CD2   1 
ATOM   3870  C  CE1   . PHE A 1 512 ? 148.328 151.754 113.263 1.00 14196. ? 512 PHE A CE1   1 
ATOM   3871  C  CE2   . PHE A 1 512 ? 149.937 150.072 112.743 1.00 14234. ? 512 PHE A CE2   1 
ATOM   3872  C  CZ    . PHE A 1 512 ? 148.730 150.437 113.297 1.00 14197. ? 512 PHE A CZ    1 
ATOM   3873  N  N     . GLU A 1 513 ? 152.696 156.117 110.843 1.00 15976. ? 513 GLU A N     1 
ATOM   3874  C  CA    . GLU A 1 513 ? 153.898 156.934 110.770 1.00 16033. ? 513 GLU A CA    1 
ATOM   3875  C  C     . GLU A 1 513 ? 153.750 158.245 111.529 1.00 16053. ? 513 GLU A C     1 
ATOM   3876  O  O     . GLU A 1 513 ? 154.705 158.696 112.165 1.00 16104. ? 513 GLU A O     1 
ATOM   3877  C  CB    . GLU A 1 513 ? 154.264 157.205 109.310 1.00 16046. ? 513 GLU A CB    1 
ATOM   3878  C  CG    . GLU A 1 513 ? 154.993 156.048 108.648 1.00 16058. ? 513 GLU A CG    1 
ATOM   3879  C  CD    . GLU A 1 513 ? 154.877 156.064 107.138 1.00 16052. ? 513 GLU A CD    1 
ATOM   3880  O  OE1   . GLU A 1 513 ? 154.196 156.962 106.601 1.00 16044. ? 513 GLU A OE1   1 
ATOM   3881  O  OE2   . GLU A 1 513 ? 155.467 155.176 106.488 1.00 16052. ? 513 GLU A OE2   1 
ATOM   3882  N  N     . GLU A 1 514 ? 152.572 158.870 111.483 1.00 16007. ? 514 GLU A N     1 
ATOM   3883  C  CA    . GLU A 1 514 ? 152.352 160.074 112.280 1.00 16043. ? 514 GLU A CA    1 
ATOM   3884  C  C     . GLU A 1 514 ? 152.449 159.769 113.772 1.00 16075. ? 514 GLU A C     1 
ATOM   3885  O  O     . GLU A 1 514 ? 153.068 160.521 114.539 1.00 16102. ? 514 GLU A O     1 
ATOM   3886  C  CB    . GLU A 1 514 ? 150.994 160.687 111.936 1.00 16035. ? 514 GLU A CB    1 
ATOM   3887  C  CG    . GLU A 1 514 ? 150.668 161.955 112.705 1.00 16048. ? 514 GLU A CG    1 
ATOM   3888  C  CD    . GLU A 1 514 ? 149.836 161.693 113.947 1.00 16050. ? 514 GLU A CD    1 
ATOM   3889  O  OE1   . GLU A 1 514 ? 149.462 160.525 114.183 1.00 16015. ? 514 GLU A OE1   1 
ATOM   3890  O  OE2   . GLU A 1 514 ? 149.552 162.658 114.686 1.00 16031. ? 514 GLU A OE2   1 
ATOM   3891  N  N     . GLN A 1 515 ? 151.844 158.656 114.196 1.00 16611. ? 515 GLN A N     1 
ATOM   3892  C  CA    . GLN A 1 515 ? 151.928 158.228 115.588 1.00 16640. ? 515 GLN A CA    1 
ATOM   3893  C  C     . GLN A 1 515 ? 153.373 157.999 116.001 1.00 16680. ? 515 GLN A C     1 
ATOM   3894  O  O     . GLN A 1 515 ? 153.805 158.425 117.076 1.00 16711. ? 515 GLN A O     1 
ATOM   3895  C  CB    . GLN A 1 515 ? 151.124 156.945 115.793 1.00 16613. ? 515 GLN A CB    1 
ATOM   3896  C  CG    . GLN A 1 515 ? 149.633 157.129 115.882 1.00 16564. ? 515 GLN A CG    1 
ATOM   3897  C  CD    . GLN A 1 515 ? 148.981 156.011 116.658 1.00 16503. ? 515 GLN A CD    1 
ATOM   3898  O  OE1   . GLN A 1 515 ? 148.227 156.245 117.603 1.00 16409. ? 515 GLN A OE1   1 
ATOM   3899  N  NE2   . GLN A 1 515 ? 149.288 154.780 116.276 1.00 16493. ? 515 GLN A NE2   1 
ATOM   3900  N  N     . ALA A 1 516 ? 154.130 157.308 115.150 1.00 17476. ? 516 ALA A N     1 
ATOM   3901  C  CA    . ALA A 1 516 ? 155.523 157.003 115.451 1.00 17528. ? 516 ALA A CA    1 
ATOM   3902  C  C     . ALA A 1 516 ? 156.365 158.272 115.505 1.00 17550. ? 516 ALA A C     1 
ATOM   3903  O  O     . ALA A 1 516 ? 157.280 158.389 116.326 1.00 17592. ? 516 ALA A O     1 
ATOM   3904  C  CB    . ALA A 1 516 ? 156.067 156.020 114.413 1.00 17552. ? 516 ALA A CB    1 
ATOM   3905  N  N     . LYS A 1 517 ? 156.073 159.235 114.627 1.00 17475. ? 517 LYS A N     1 
ATOM   3906  C  CA    . LYS A 1 517 ? 156.762 160.519 114.652 1.00 17492. ? 517 LYS A CA    1 
ATOM   3907  C  C     . LYS A 1 517 ? 156.513 161.247 115.964 1.00 17499. ? 517 LYS A C     1 
ATOM   3908  O  O     . LYS A 1 517 ? 157.437 161.790 116.579 1.00 17518. ? 517 LYS A O     1 
ATOM   3909  C  CB    . LYS A 1 517 ? 156.308 161.381 113.470 1.00 17476. ? 517 LYS A CB    1 
ATOM   3910  C  CG    . LYS A 1 517 ? 156.712 162.843 113.583 1.00 17484. ? 517 LYS A CG    1 
ATOM   3911  C  CD    . LYS A 1 517 ? 155.805 163.726 112.751 1.00 17479. ? 517 LYS A CD    1 
ATOM   3912  C  CE    . LYS A 1 517 ? 154.356 163.574 113.176 1.00 17468. ? 517 LYS A CE    1 
ATOM   3913  N  NZ    . LYS A 1 517 ? 154.151 163.900 114.616 1.00 17473. ? 517 LYS A NZ    1 
ATOM   3914  N  N     . ALA A 1 518 ? 155.255 161.263 116.406 1.00 17818. ? 518 ALA A N     1 
ATOM   3915  C  CA    . ALA A 1 518 ? 154.938 161.917 117.672 1.00 17837. ? 518 ALA A CA    1 
ATOM   3916  C  C     . ALA A 1 518 ? 155.586 161.196 118.850 1.00 17855. ? 518 ALA A C     1 
ATOM   3917  O  O     . ALA A 1 518 ? 156.089 161.837 119.780 1.00 17862. ? 518 ALA A O     1 
ATOM   3918  C  CB    . ALA A 1 518 ? 153.424 161.996 117.856 1.00 17834. ? 518 ALA A CB    1 
ATOM   3919  N  N     . LYS A 1 519 ? 155.577 159.862 118.830 1.00 18252. ? 519 LYS A N     1 
ATOM   3920  C  CA    . LYS A 1 519 ? 156.034 159.087 119.980 1.00 18272. ? 519 LYS A CA    1 
ATOM   3921  C  C     . LYS A 1 519 ? 157.553 159.086 120.098 1.00 18306. ? 519 LYS A C     1 
ATOM   3922  O  O     . LYS A 1 519 ? 158.098 159.208 121.201 1.00 18305. ? 519 LYS A O     1 
ATOM   3923  C  CB    . LYS A 1 519 ? 155.507 157.655 119.879 1.00 18268. ? 519 LYS A CB    1 
ATOM   3924  C  CG    . LYS A 1 519 ? 155.938 156.746 121.015 1.00 18276. ? 519 LYS A CG    1 
ATOM   3925  C  CD    . LYS A 1 519 ? 155.256 155.394 120.922 1.00 18236. ? 519 LYS A CD    1 
ATOM   3926  C  CE    . LYS A 1 519 ? 155.638 154.507 122.091 1.00 18243. ? 519 LYS A CE    1 
ATOM   3927  N  NZ    . LYS A 1 519 ? 155.157 153.112 121.907 1.00 18198. ? 519 LYS A NZ    1 
ATOM   3928  N  N     . ALA A 1 520 ? 158.255 158.935 118.972 1.00 19854. ? 520 ALA A N     1 
ATOM   3929  C  CA    . ALA A 1 520 ? 159.689 158.668 119.013 1.00 19904. ? 520 ALA A CA    1 
ATOM   3930  C  C     . ALA A 1 520 ? 160.481 159.814 119.624 1.00 19940. ? 520 ALA A C     1 
ATOM   3931  O  O     . ALA A 1 520 ? 161.364 159.578 120.457 1.00 19954. ? 520 ALA A O     1 
ATOM   3932  C  CB    . ALA A 1 520 ? 160.204 158.371 117.604 1.00 19931. ? 520 ALA A CB    1 
ATOM   3933  N  N     . ALA A 1 521 ? 160.178 161.051 119.236 1.00 20716. ? 521 ALA A N     1 
ATOM   3934  C  CA    . ALA A 1 521 ? 160.945 162.224 119.654 1.00 20747. ? 521 ALA A CA    1 
ATOM   3935  C  C     . ALA A 1 521 ? 162.434 162.018 119.386 1.00 20771. ? 521 ALA A C     1 
ATOM   3936  O  O     . ALA A 1 521 ? 163.292 162.248 120.242 1.00 20771. ? 521 ALA A O     1 
ATOM   3937  C  CB    . ALA A 1 521 ? 160.689 162.555 121.124 1.00 20753. ? 521 ALA A CB    1 
ATOM   3938  N  N     . GLY A 1 522 ? 162.731 161.531 118.181 1.00 21502. ? 522 GLY A N     1 
ATOM   3939  C  CA    . GLY A 1 522 ? 164.127 161.216 117.833 1.00 21524. ? 522 GLY A CA    1 
ATOM   3940  C  C     . GLY A 1 522 ? 164.259 159.723 117.638 1.00 21536. ? 522 GLY A C     1 
ATOM   3941  O  O     . GLY A 1 522 ? 163.246 159.097 117.265 1.00 21532. ? 522 GLY A O     1 
ATOM   3942  N  N     . ASP A 1 523 ? 165.445 159.161 117.879 1.00 22347. ? 523 ASP A N     1 
ATOM   3943  C  CA    . ASP A 1 523 ? 165.624 157.684 117.797 1.00 22355. ? 523 ASP A CA    1 
ATOM   3944  C  C     . ASP A 1 523 ? 165.216 157.206 116.401 1.00 22346. ? 523 ASP A C     1 
ATOM   3945  O  O     . ASP A 1 523 ? 165.507 157.920 115.422 1.00 22353. ? 523 ASP A O     1 
ATOM   3946  C  CB    . ASP A 1 523 ? 164.848 156.987 118.903 1.00 22349. ? 523 ASP A CB    1 
ATOM   3947  C  CG    . ASP A 1 523 ? 165.158 155.512 119.110 1.00 22353. ? 523 ASP A CG    1 
ATOM   3948  O  OD1   . ASP A 1 523 ? 166.330 155.194 119.396 1.00 22370. ? 523 ASP A OD1   1 
ATOM   3949  O  OD2   . ASP A 1 523 ? 164.223 154.693 118.978 1.00 22333. ? 523 ASP A OD2   1 
ATOM   3950  N  N     . ASP A 1 524 ? 164.576 156.040 116.315 1.00 21561. ? 524 ASP A N     1 
ATOM   3951  C  CA    . ASP A 1 524 ? 164.080 155.539 115.007 1.00 21541. ? 524 ASP A CA    1 
ATOM   3952  C  C     . ASP A 1 524 ? 162.677 154.960 115.198 1.00 21504. ? 524 ASP A C     1 
ATOM   3953  O  O     . ASP A 1 524 ? 162.479 154.164 116.135 1.00 21492. ? 524 ASP A O     1 
ATOM   3954  C  CB    . ASP A 1 524 ? 165.043 154.539 114.395 1.00 21540. ? 524 ASP A CB    1 
ATOM   3955  C  CG    . ASP A 1 524 ? 165.490 153.408 115.310 1.00 21541. ? 524 ASP A CG    1 
ATOM   3956  O  OD1   . ASP A 1 524 ? 165.132 153.440 116.506 1.00 21540. ? 524 ASP A OD1   1 
ATOM   3957  O  OD2   . ASP A 1 524 ? 166.181 152.495 114.815 1.00 21534. ? 524 ASP A OD2   1 
ATOM   3958  N  N     . GLU A 1 525 ? 161.747 155.326 114.320 1.00 20299. ? 525 GLU A N     1 
ATOM   3959  C  CA    . GLU A 1 525 ? 160.358 154.825 114.425 1.00 20267. ? 525 GLU A CA    1 
ATOM   3960  C  C     . GLU A 1 525 ? 160.340 153.334 114.097 1.00 20237. ? 525 GLU A C     1 
ATOM   3961  O  O     . GLU A 1 525 ? 159.272 152.710 114.226 1.00 20212. ? 525 GLU A O     1 
ATOM   3962  C  CB    . GLU A 1 525 ? 159.468 155.540 113.416 1.00 20271. ? 525 GLU A CB    1 
ATOM   3963  C  CG    . GLU A 1 525 ? 159.889 155.319 111.967 1.00 20270. ? 525 GLU A CG    1 
ATOM   3964  C  CD    . GLU A 1 525 ? 161.059 156.170 111.506 1.00 20245. ? 525 GLU A CD    1 
ATOM   3965  O  OE1   . GLU A 1 525 ? 161.569 156.969 112.318 1.00 20231. ? 525 GLU A OE1   1 
ATOM   3966  O  OE2   . GLU A 1 525 ? 161.459 156.031 110.332 1.00 20221. ? 525 GLU A OE2   1 
ATOM   3967  N  N     . ALA A 1 526 ? 161.481 152.785 113.702 1.00 19683. ? 526 ALA A N     1 
ATOM   3968  C  CA    . ALA A 1 526 ? 161.519 151.373 113.278 1.00 19662. ? 526 ALA A CA    1 
ATOM   3969  C  C     . ALA A 1 526 ? 160.764 150.516 114.283 1.00 19635. ? 526 ALA A C     1 
ATOM   3970  O  O     . ALA A 1 526 ? 160.097 149.553 113.868 1.00 19621. ? 526 ALA A O     1 
ATOM   3971  C  CB    . ALA A 1 526 ? 162.955 150.938 113.186 1.00 19668. ? 526 ALA A CB    1 
ATOM   3972  N  N     . MET A 1 527 ? 160.878 150.847 115.564 1.00 19166. ? 527 MET A N     1 
ATOM   3973  C  CA    . MET A 1 527 ? 160.268 149.963 116.582 1.00 19122. ? 527 MET A CA    1 
ATOM   3974  C  C     . MET A 1 527 ? 158.934 150.542 117.056 1.00 19087. ? 527 MET A C     1 
ATOM   3975  O  O     . MET A 1 527 ? 158.351 149.969 117.980 1.00 19018. ? 527 MET A O     1 
ATOM   3976  C  CB    . MET A 1 527 ? 161.210 149.807 117.777 1.00 19135. ? 527 MET A CB    1 
ATOM   3977  C  CG    . MET A 1 527 ? 161.629 151.115 118.409 1.00 19150. ? 527 MET A CG    1 
ATOM   3978  S  SD    . MET A 1 527 ? 162.015 150.894 120.157 1.00 19203. ? 527 MET A SD    1 
ATOM   3979  C  CE    . MET A 1 527 ? 162.973 149.376 120.059 1.00 19197. ? 527 MET A CE    1 
ATOM   3980  N  N     . PHE A 1 528 ? 158.459 151.618 116.449 1.00 18448. ? 528 PHE A N     1 
ATOM   3981  C  CA    . PHE A 1 528 ? 157.125 152.101 116.868 1.00 18418. ? 528 PHE A CA    1 
ATOM   3982  C  C     . PHE A 1 528 ? 156.140 151.896 115.727 1.00 18392. ? 528 PHE A C     1 
ATOM   3983  O  O     . PHE A 1 528 ? 155.022 152.437 115.770 1.00 18387. ? 528 PHE A O     1 
ATOM   3984  C  CB    . PHE A 1 528 ? 157.270 153.552 117.317 1.00 18438. ? 528 PHE A CB    1 
ATOM   3985  C  CG    . PHE A 1 528 ? 158.419 153.819 118.276 1.00 18452. ? 528 PHE A CG    1 
ATOM   3986  C  CD1   . PHE A 1 528 ? 158.309 153.508 119.623 1.00 18430. ? 528 PHE A CD1   1 
ATOM   3987  C  CD2   . PHE A 1 528 ? 159.591 154.418 117.833 1.00 18489. ? 528 PHE A CD2   1 
ATOM   3988  C  CE1   . PHE A 1 528 ? 159.355 153.761 120.493 1.00 18445. ? 528 PHE A CE1   1 
ATOM   3989  C  CE2   . PHE A 1 528 ? 160.631 154.673 118.708 1.00 18486. ? 528 PHE A CE2   1 
ATOM   3990  C  CZ    . PHE A 1 528 ? 160.511 154.343 120.035 1.00 18460. ? 528 PHE A CZ    1 
ATOM   3991  N  N     . ILE A 1 529 ? 156.532 151.108 114.731 1.00 16994. ? 529 ILE A N     1 
ATOM   3992  C  CA    . ILE A 1 529 ? 155.620 150.817 113.590 1.00 16933. ? 529 ILE A CA    1 
ATOM   3993  C  C     . ILE A 1 529 ? 155.577 149.300 113.391 1.00 16885. ? 529 ILE A C     1 
ATOM   3994  O  O     . ILE A 1 529 ? 156.651 148.686 113.318 1.00 16903. ? 529 ILE A O     1 
ATOM   3995  C  CB    . ILE A 1 529 ? 156.071 151.548 112.316 1.00 16929. ? 529 ILE A CB    1 
ATOM   3996  C  CG1   . ILE A 1 529 ? 155.178 151.192 111.134 1.00 16889. ? 529 ILE A CG1   1 
ATOM   3997  C  CG2   . ILE A 1 529 ? 157.545 151.279 112.016 1.00 16952. ? 529 ILE A CG2   1 
ATOM   3998  C  CD1   . ILE A 1 529 ? 155.317 152.127 109.948 1.00 16880. ? 529 ILE A CD1   1 
ATOM   3999  N  N     . ASP A 1 530 ? 154.379 148.725 113.348 1.00 15636. ? 530 ASP A N     1 
ATOM   4000  C  CA    . ASP A 1 530 ? 154.279 147.274 113.075 1.00 15606. ? 530 ASP A CA    1 
ATOM   4001  C  C     . ASP A 1 530 ? 154.330 147.104 111.564 1.00 15567. ? 530 ASP A C     1 
ATOM   4002  O  O     . ASP A 1 530 ? 153.407 147.578 110.898 1.00 15543. ? 530 ASP A O     1 
ATOM   4003  C  CB    . ASP A 1 530 ? 153.060 146.651 113.721 1.00 15581. ? 530 ASP A CB    1 
ATOM   4004  C  CG    . ASP A 1 530 ? 153.120 145.136 113.841 1.00 15565. ? 530 ASP A CG    1 
ATOM   4005  O  OD1   . ASP A 1 530 ? 154.102 144.552 113.340 1.00 15576. ? 530 ASP A OD1   1 
ATOM   4006  O  OD2   . ASP A 1 530 ? 152.201 144.553 114.450 1.00 15554. ? 530 ASP A OD2   1 
ATOM   4007  N  N     . GLU A 1 531 ? 155.399 146.497 111.060 1.00 15471. ? 531 GLU A N     1 
ATOM   4008  C  CA    . GLU A 1 531 ? 155.548 146.296 109.626 1.00 15452. ? 531 GLU A CA    1 
ATOM   4009  C  C     . GLU A 1 531 ? 154.967 144.978 109.142 1.00 15393. ? 531 GLU A C     1 
ATOM   4010  O  O     . GLU A 1 531 ? 154.956 144.731 107.932 1.00 15406. ? 531 GLU A O     1 
ATOM   4011  C  CB    . GLU A 1 531 ? 157.025 146.386 109.229 1.00 15475. ? 531 GLU A CB    1 
ATOM   4012  C  CG    . GLU A 1 531 ? 157.667 147.727 109.537 1.00 15489. ? 531 GLU A CG    1 
ATOM   4013  C  CD    . GLU A 1 531 ? 157.405 148.762 108.460 1.00 15495. ? 531 GLU A CD    1 
ATOM   4014  O  OE1   . GLU A 1 531 ? 156.224 149.078 108.206 1.00 15484. ? 531 GLU A OE1   1 
ATOM   4015  O  OE2   . GLU A 1 531 ? 158.383 149.262 107.866 1.00 15496. ? 531 GLU A OE2   1 
ATOM   4016  N  N     . ASN A 1 532 ? 154.489 144.124 110.045 1.00 13822. ? 532 ASN A N     1 
ATOM   4017  C  CA    . ASN A 1 532 ? 153.771 142.924 109.645 1.00 13779. ? 532 ASN A CA    1 
ATOM   4018  C  C     . ASN A 1 532 ? 152.274 143.153 109.517 1.00 13747. ? 532 ASN A C     1 
ATOM   4019  O  O     . ASN A 1 532 ? 151.651 142.608 108.598 1.00 13737. ? 532 ASN A O     1 
ATOM   4020  C  CB    . ASN A 1 532 ? 154.029 141.792 110.646 1.00 13779. ? 532 ASN A CB    1 
ATOM   4021  C  CG    . ASN A 1 532 ? 153.777 140.423 110.052 1.00 13771. ? 532 ASN A CG    1 
ATOM   4022  O  OD1   . ASN A 1 532 ? 153.592 140.283 108.844 1.00 13765. ? 532 ASN A OD1   1 
ATOM   4023  N  ND2   . ASN A 1 532 ? 153.771 139.401 110.900 1.00 13777. ? 532 ASN A ND2   1 
ATOM   4024  N  N     . PHE A 1 533 ? 151.690 143.961 110.403 1.00 12851. ? 533 PHE A N     1 
ATOM   4025  C  CA    . PHE A 1 533 ? 150.288 144.331 110.269 1.00 12790. ? 533 PHE A CA    1 
ATOM   4026  C  C     . PHE A 1 533 ? 150.047 145.131 108.996 1.00 12785. ? 533 PHE A C     1 
ATOM   4027  O  O     . PHE A 1 533 ? 149.033 144.936 108.318 1.00 12782. ? 533 PHE A O     1 
ATOM   4028  C  CB    . PHE A 1 533 ? 149.843 145.122 111.497 1.00 12797. ? 533 PHE A CB    1 
ATOM   4029  C  CG    . PHE A 1 533 ? 148.485 145.735 111.361 1.00 12745. ? 533 PHE A CG    1 
ATOM   4030  C  CD1   . PHE A 1 533 ? 147.359 144.938 111.280 1.00 12741. ? 533 PHE A CD1   1 
ATOM   4031  C  CD2   . PHE A 1 533 ? 148.333 147.107 111.323 1.00 12765. ? 533 PHE A CD2   1 
ATOM   4032  C  CE1   . PHE A 1 533 ? 146.109 145.498 111.160 1.00 12747. ? 533 PHE A CE1   1 
ATOM   4033  C  CE2   . PHE A 1 533 ? 147.084 147.673 111.203 1.00 12767. ? 533 PHE A CE2   1 
ATOM   4034  C  CZ    . PHE A 1 533 ? 145.971 146.867 111.121 1.00 12753. ? 533 PHE A CZ    1 
ATOM   4035  N  N     . CYS A 1 534 ? 150.970 146.033 108.656 1.00 13176. ? 534 CYS A N     1 
ATOM   4036  C  CA    . CYS A 1 534 ? 150.847 146.785 107.413 1.00 13166. ? 534 CYS A CA    1 
ATOM   4037  C  C     . CYS A 1 534 ? 150.917 145.864 106.201 1.00 13138. ? 534 CYS A C     1 
ATOM   4038  O  O     . CYS A 1 534 ? 150.177 146.047 105.228 1.00 13142. ? 534 CYS A O     1 
ATOM   4039  C  CB    . CYS A 1 534 ? 151.934 147.855 107.342 1.00 13206. ? 534 CYS A CB    1 
ATOM   4040  S  SG    . CYS A 1 534 ? 151.780 149.148 108.592 1.00 13221. ? 534 CYS A SG    1 
ATOM   4041  N  N     . THR A 1 535 ? 151.807 144.871 106.238 1.00 12772. ? 535 THR A N     1 
ATOM   4042  C  CA    . THR A 1 535 ? 151.893 143.915 105.139 1.00 12755. ? 535 THR A CA    1 
ATOM   4043  C  C     . THR A 1 535 ? 150.613 143.096 105.019 1.00 12756. ? 535 THR A C     1 
ATOM   4044  O  O     . THR A 1 535 ? 150.133 142.834 103.910 1.00 12774. ? 535 THR A O     1 
ATOM   4045  C  CB    . THR A 1 535 ? 153.105 143.004 105.336 1.00 12763. ? 535 THR A CB    1 
ATOM   4046  O  OG1   . THR A 1 535 ? 154.304 143.777 105.211 1.00 12769. ? 535 THR A OG1   1 
ATOM   4047  C  CG2   . THR A 1 535 ? 153.122 141.897 104.296 1.00 12752. ? 535 THR A CG2   1 
ATOM   4048  N  N     . ALA A 1 536 ? 150.039 142.687 106.152 1.00 12752. ? 536 ALA A N     1 
ATOM   4049  C  CA    . ALA A 1 536 ? 148.763 141.979 106.111 1.00 12742. ? 536 ALA A CA    1 
ATOM   4050  C  C     . ALA A 1 536 ? 147.667 142.852 105.510 1.00 12747. ? 536 ALA A C     1 
ATOM   4051  O  O     . ALA A 1 536 ? 146.866 142.388 104.686 1.00 12775. ? 536 ALA A O     1 
ATOM   4052  C  CB    . ALA A 1 536 ? 148.375 141.519 107.514 1.00 12763. ? 536 ALA A CB    1 
ATOM   4053  N  N     . LEU A 1 537 ? 147.623 144.126 105.904 1.00 12752. ? 537 LEU A N     1 
ATOM   4054  C  CA    . LEU A 1 537 ? 146.628 145.039 105.350 1.00 12749. ? 537 LEU A CA    1 
ATOM   4055  C  C     . LEU A 1 537 ? 146.814 145.205 103.848 1.00 12749. ? 537 LEU A C     1 
ATOM   4056  O  O     . LEU A 1 537 ? 145.836 145.279 103.097 1.00 12748. ? 537 LEU A O     1 
ATOM   4057  C  CB    . LEU A 1 537 ? 146.710 146.389 106.056 1.00 12746. ? 537 LEU A CB    1 
ATOM   4058  C  CG    . LEU A 1 537 ? 145.611 146.676 107.074 1.00 12741. ? 537 LEU A CG    1 
ATOM   4059  C  CD1   . LEU A 1 537 ? 145.671 148.119 107.516 1.00 12748. ? 537 LEU A CD1   1 
ATOM   4060  C  CD2   . LEU A 1 537 ? 144.261 146.364 106.481 1.00 12751. ? 537 LEU A CD2   1 
ATOM   4061  N  N     . GLU A 1 538 ? 148.067 145.276 103.394 1.00 12751. ? 538 GLU A N     1 
ATOM   4062  C  CA    . GLU A 1 538 ? 148.340 145.310 101.962 1.00 12743. ? 538 GLU A CA    1 
ATOM   4063  C  C     . GLU A 1 538 ? 147.889 144.034 101.269 1.00 12729. ? 538 GLU A C     1 
ATOM   4064  O  O     . GLU A 1 538 ? 147.467 144.086 100.110 1.00 12745. ? 538 GLU A O     1 
ATOM   4065  C  CB    . GLU A 1 538 ? 149.829 145.536 101.714 1.00 12749. ? 538 GLU A CB    1 
ATOM   4066  C  CG    . GLU A 1 538 ? 150.216 146.995 101.600 1.00 12755. ? 538 GLU A CG    1 
ATOM   4067  C  CD    . GLU A 1 538 ? 151.697 147.221 101.808 1.00 12761. ? 538 GLU A CD    1 
ATOM   4068  O  OE1   . GLU A 1 538 ? 152.420 146.234 102.053 1.00 12759. ? 538 GLU A OE1   1 
ATOM   4069  O  OE2   . GLU A 1 538 ? 152.139 148.385 101.729 1.00 12770. ? 538 GLU A OE2   1 
ATOM   4070  N  N     . TYR A 1 539 ? 147.985 142.893 101.946 1.00 12727. ? 539 TYR A N     1 
ATOM   4071  C  CA    . TYR A 1 539 ? 147.456 141.649 101.402 1.00 12725. ? 539 TYR A CA    1 
ATOM   4072  C  C     . TYR A 1 539 ? 145.936 141.633 101.355 1.00 12731. ? 539 TYR A C     1 
ATOM   4073  O  O     . TYR A 1 539 ? 145.366 140.889 100.552 1.00 12733. ? 539 TYR A O     1 
ATOM   4074  C  CB    . TYR A 1 539 ? 147.960 140.455 102.211 1.00 12737. ? 539 TYR A CB    1 
ATOM   4075  C  CG    . TYR A 1 539 ? 149.223 139.852 101.650 1.00 12739. ? 539 TYR A CG    1 
ATOM   4076  C  CD1   . TYR A 1 539 ? 149.176 138.970 100.582 1.00 12745. ? 539 TYR A CD1   1 
ATOM   4077  C  CD2   . TYR A 1 539 ? 150.462 140.172 102.180 1.00 12746. ? 539 TYR A CD2   1 
ATOM   4078  C  CE1   . TYR A 1 539 ? 150.326 138.420 100.063 1.00 12755. ? 539 TYR A CE1   1 
ATOM   4079  C  CE2   . TYR A 1 539 ? 151.618 139.627 101.666 1.00 12746. ? 539 TYR A CE2   1 
ATOM   4080  C  CZ    . TYR A 1 539 ? 151.544 138.751 100.608 1.00 12749. ? 539 TYR A CZ    1 
ATOM   4081  O  OH    . TYR A 1 539 ? 152.695 138.203 100.093 1.00 12762. ? 539 TYR A OH    1 
ATOM   4082  N  N     . GLY A 1 540 ? 145.271 142.427 102.190 1.00 12749. ? 540 GLY A N     1 
ATOM   4083  C  CA    . GLY A 1 540 ? 143.846 142.641 102.021 1.00 12740. ? 540 GLY A CA    1 
ATOM   4084  C  C     . GLY A 1 540 ? 142.976 142.260 103.198 1.00 12737. ? 540 GLY A C     1 
ATOM   4085  O  O     . GLY A 1 540 ? 142.936 141.094 103.600 1.00 12750. ? 540 GLY A O     1 
ATOM   4086  N  N     . LEU A 1 541 ? 142.264 143.237 103.752 1.00 12726. ? 541 LEU A N     1 
ATOM   4087  C  CA    . LEU A 1 541 ? 141.352 143.011 104.859 1.00 12736. ? 541 LEU A CA    1 
ATOM   4088  C  C     . LEU A 1 541 ? 139.932 143.353 104.444 1.00 12746. ? 541 LEU A C     1 
ATOM   4089  O  O     . LEU A 1 541 ? 139.692 144.457 103.939 1.00 12766. ? 541 LEU A O     1 
ATOM   4090  C  CB    . LEU A 1 541 ? 141.759 143.853 106.071 1.00 12740. ? 541 LEU A CB    1 
ATOM   4091  C  CG    . LEU A 1 541 ? 140.820 143.885 107.275 1.00 12740. ? 541 LEU A CG    1 
ATOM   4092  C  CD1   . LEU A 1 541 ? 140.912 142.599 108.069 1.00 12755. ? 541 LEU A CD1   1 
ATOM   4093  C  CD2   . LEU A 1 541 ? 141.145 145.074 108.155 1.00 12751. ? 541 LEU A CD2   1 
ATOM   4094  N  N     . PRO A 1 542 ? 138.977 142.448 104.631 1.00 12729. ? 542 PRO A N     1 
ATOM   4095  C  CA    . PRO A 1 542 ? 137.590 142.738 104.262 1.00 12733. ? 542 PRO A CA    1 
ATOM   4096  C  C     . PRO A 1 542 ? 137.008 143.814 105.158 1.00 12738. ? 542 PRO A C     1 
ATOM   4097  O  O     . PRO A 1 542 ? 137.562 144.102 106.230 1.00 12765. ? 542 PRO A O     1 
ATOM   4098  C  CB    . PRO A 1 542 ? 136.877 141.393 104.476 1.00 12745. ? 542 PRO A CB    1 
ATOM   4099  C  CG    . PRO A 1 542 ? 137.961 140.377 104.584 1.00 12747. ? 542 PRO A CG    1 
ATOM   4100  C  CD    . PRO A 1 542 ? 139.135 141.086 105.159 1.00 12744. ? 542 PRO A CD    1 
ATOM   4101  N  N     . PRO A 1 543 ? 135.905 144.450 104.750 1.00 12713. ? 543 PRO A N     1 
ATOM   4102  C  CA    . PRO A 1 543 ? 135.232 145.395 105.650 1.00 12727. ? 543 PRO A CA    1 
ATOM   4103  C  C     . PRO A 1 543 ? 134.852 144.726 106.958 1.00 12740. ? 543 PRO A C     1 
ATOM   4104  O  O     . PRO A 1 543 ? 134.036 143.802 106.982 1.00 12767. ? 543 PRO A O     1 
ATOM   4105  C  CB    . PRO A 1 543 ? 133.998 145.834 104.852 1.00 12741. ? 543 PRO A CB    1 
ATOM   4106  C  CG    . PRO A 1 543 ? 133.863 144.844 103.745 1.00 12740. ? 543 PRO A CG    1 
ATOM   4107  C  CD    . PRO A 1 543 ? 135.238 144.365 103.443 1.00 12728. ? 543 PRO A CD    1 
ATOM   4108  N  N     . THR A 1 544 ? 135.448 145.183 108.053 1.00 12737. ? 544 THR A N     1 
ATOM   4109  C  CA    . THR A 1 544 ? 135.339 144.520 109.340 1.00 12739. ? 544 THR A CA    1 
ATOM   4110  C  C     . THR A 1 544 ? 134.864 145.516 110.386 1.00 12741. ? 544 THR A C     1 
ATOM   4111  O  O     . THR A 1 544 ? 135.034 146.728 110.243 1.00 12752. ? 544 THR A O     1 
ATOM   4112  C  CB    . THR A 1 544 ? 136.686 143.912 109.765 1.00 12747. ? 544 THR A CB    1 
ATOM   4113  O  OG1   . THR A 1 544 ? 137.367 143.411 108.609 1.00 12760. ? 544 THR A OG1   1 
ATOM   4114  C  CG2   . THR A 1 544 ? 136.489 142.778 110.749 1.00 12757. ? 544 THR A CG2   1 
ATOM   4115  N  N     . ALA A 1 545 ? 134.253 144.987 111.440 1.00 12737. ? 545 ALA A N     1 
ATOM   4116  C  CA    . ALA A 1 545 ? 133.857 145.773 112.596 1.00 12735. ? 545 ALA A CA    1 
ATOM   4117  C  C     . ALA A 1 545 ? 134.468 145.151 113.841 1.00 12740. ? 545 ALA A C     1 
ATOM   4118  O  O     . ALA A 1 545 ? 134.360 143.938 114.052 1.00 12751. ? 545 ALA A O     1 
ATOM   4119  C  CB    . ALA A 1 545 ? 132.337 145.843 112.719 1.00 12755. ? 545 ALA A CB    1 
ATOM   4120  N  N     . GLY A 1 546 ? 135.109 145.976 114.658 1.00 12753. ? 546 GLY A N     1 
ATOM   4121  C  CA    . GLY A 1 546 ? 135.778 145.521 115.868 1.00 12748. ? 546 GLY A CA    1 
ATOM   4122  C  C     . GLY A 1 546 ? 135.075 146.065 117.098 1.00 12741. ? 546 GLY A C     1 
ATOM   4123  O  O     . GLY A 1 546 ? 134.629 147.216 117.107 1.00 12760. ? 546 GLY A O     1 
ATOM   4124  N  N     . TRP A 1 547 ? 134.991 145.231 118.134 1.00 12736. ? 547 TRP A N     1 
ATOM   4125  C  CA    . TRP A 1 547 ? 134.276 145.556 119.358 1.00 12748. ? 547 TRP A CA    1 
ATOM   4126  C  C     . TRP A 1 547 ? 135.086 145.076 120.552 1.00 12743. ? 547 TRP A C     1 
ATOM   4127  O  O     . TRP A 1 547 ? 135.771 144.054 120.482 1.00 12755. ? 547 TRP A O     1 
ATOM   4128  C  CB    . TRP A 1 547 ? 132.890 144.910 119.352 1.00 12762. ? 547 TRP A CB    1 
ATOM   4129  C  CG    . TRP A 1 547 ? 132.007 145.219 120.518 1.00 12752. ? 547 TRP A CG    1 
ATOM   4130  C  CD1   . TRP A 1 547 ? 131.178 146.290 120.652 1.00 12758. ? 547 TRP A CD1   1 
ATOM   4131  C  CD2   . TRP A 1 547 ? 131.814 144.414 121.687 1.00 12732. ? 547 TRP A CD2   1 
ATOM   4132  N  NE1   . TRP A 1 547 ? 130.500 146.218 121.842 1.00 12739. ? 547 TRP A NE1   1 
ATOM   4133  C  CE2   . TRP A 1 547 ? 130.873 145.074 122.495 1.00 12738. ? 547 TRP A CE2   1 
ATOM   4134  C  CE3   . TRP A 1 547 ? 132.363 143.212 122.138 1.00 12735. ? 547 TRP A CE3   1 
ATOM   4135  C  CZ2   . TRP A 1 547 ? 130.463 144.567 123.722 1.00 12755. ? 547 TRP A CZ2   1 
ATOM   4136  C  CZ3   . TRP A 1 547 ? 131.951 142.709 123.349 1.00 12734. ? 547 TRP A CZ3   1 
ATOM   4137  C  CH2   . TRP A 1 547 ? 131.008 143.381 124.126 1.00 12748. ? 547 TRP A CH2   1 
ATOM   4138  N  N     . GLY A 1 548 ? 135.003 145.823 121.647 1.00 12741. ? 548 GLY A N     1 
ATOM   4139  C  CA    . GLY A 1 548 ? 135.755 145.517 122.846 1.00 12742. ? 548 GLY A CA    1 
ATOM   4140  C  C     . GLY A 1 548 ? 135.083 146.031 124.101 1.00 12730. ? 548 GLY A C     1 
ATOM   4141  O  O     . GLY A 1 548 ? 134.707 147.203 124.178 1.00 12746. ? 548 GLY A O     1 
ATOM   4142  N  N     . MET A 1 549 ? 134.935 145.162 125.094 1.00 12727. ? 549 MET A N     1 
ATOM   4143  C  CA    . MET A 1 549 ? 134.228 145.482 126.323 1.00 12742. ? 549 MET A CA    1 
ATOM   4144  C  C     . MET A 1 549 ? 135.102 145.191 127.528 1.00 12749. ? 549 MET A C     1 
ATOM   4145  O  O     . MET A 1 549 ? 135.857 144.212 127.552 1.00 12768. ? 549 MET A O     1 
ATOM   4146  C  CB    . MET A 1 549 ? 132.930 144.690 126.443 1.00 12760. ? 549 MET A CB    1 
ATOM   4147  C  CG    . MET A 1 549 ? 131.871 145.360 127.290 1.00 12755. ? 549 MET A CG    1 
ATOM   4148  S  SD    . MET A 1 549 ? 130.585 144.235 127.845 1.00 12726. ? 549 MET A SD    1 
ATOM   4149  C  CE    . MET A 1 549 ? 131.579 142.851 128.361 1.00 12743. ? 549 MET A CE    1 
ATOM   4150  N  N     . GLY A 1 550 ? 134.975 146.050 128.535 1.00 12732. ? 550 GLY A N     1 
ATOM   4151  C  CA    . GLY A 1 550 ? 135.670 145.852 129.791 1.00 12732. ? 550 GLY A CA    1 
ATOM   4152  C  C     . GLY A 1 550 ? 134.898 144.959 130.739 1.00 12739. ? 550 GLY A C     1 
ATOM   4153  O  O     . GLY A 1 550 ? 133.841 145.347 131.242 1.00 12755. ? 550 GLY A O     1 
ATOM   4154  N  N     . ILE A 1 551 ? 135.418 143.754 130.988 1.00 12733. ? 551 ILE A N     1 
ATOM   4155  C  CA    . ILE A 1 551 ? 134.736 142.805 131.864 1.00 12732. ? 551 ILE A CA    1 
ATOM   4156  C  C     . ILE A 1 551 ? 134.623 143.350 133.279 1.00 12742. ? 551 ILE A C     1 
ATOM   4157  O  O     . ILE A 1 551 ? 133.567 143.237 133.915 1.00 12754. ? 551 ILE A O     1 
ATOM   4158  C  CB    . ILE A 1 551 ? 135.467 141.448 131.856 1.00 12738. ? 551 ILE A CB    1 
ATOM   4159  C  CG1   . ILE A 1 551 ? 135.500 140.850 130.451 1.00 12736. ? 551 ILE A CG1   1 
ATOM   4160  C  CG2   . ILE A 1 551 ? 134.806 140.483 132.822 1.00 12742. ? 551 ILE A CG2   1 
ATOM   4161  C  CD1   . ILE A 1 551 ? 134.182 140.885 129.745 1.00 12739. ? 551 ILE A CD1   1 
ATOM   4162  N  N     . ASP A 1 552 ? 135.726 143.894 133.796 1.00 12732. ? 552 ASP A N     1 
ATOM   4163  C  CA    . ASP A 1 552 ? 135.736 144.357 135.212 1.00 12740. ? 552 ASP A CA    1 
ATOM   4164  C  C     . ASP A 1 552 ? 134.633 145.395 135.435 1.00 12742. ? 552 ASP A C     1 
ATOM   4165  O  O     . ASP A 1 552 ? 133.857 145.227 136.393 1.00 12770. ? 552 ASP A O     1 
ATOM   4166  C  CB    . ASP A 1 552 ? 137.116 144.858 135.608 1.00 12752. ? 552 ASP A CB    1 
ATOM   4167  C  CG    . ASP A 1 552 ? 138.276 143.949 135.224 1.00 12758. ? 552 ASP A CG    1 
ATOM   4168  O  OD1   . ASP A 1 552 ? 138.020 142.898 134.598 1.00 12755. ? 552 ASP A OD1   1 
ATOM   4169  O  OD2   . ASP A 1 552 ? 139.428 144.299 135.556 1.00 12769. ? 552 ASP A OD2   1 
ATOM   4170  N  N     . ARG A 1 553 ? 134.558 146.422 134.586 1.00 12733. ? 553 ARG A N     1 
ATOM   4171  C  CA    . ARG A 1 553 ? 133.582 147.485 134.790 1.00 12732. ? 553 ARG A CA    1 
ATOM   4172  C  C     . ARG A 1 553 ? 132.153 146.964 134.745 1.00 12737. ? 553 ARG A C     1 
ATOM   4173  O  O     . ARG A 1 553 ? 131.314 147.388 135.550 1.00 12763. ? 553 ARG A O     1 
ATOM   4174  C  CB    . ARG A 1 553 ? 133.788 148.583 133.748 1.00 12741. ? 553 ARG A CB    1 
ATOM   4175  C  CG    . ARG A 1 553 ? 135.164 149.215 133.820 1.00 12745. ? 553 ARG A CG    1 
ATOM   4176  C  CD    . ARG A 1 553 ? 135.232 150.531 133.076 1.00 12738. ? 553 ARG A CD    1 
ATOM   4177  N  NE    . ARG A 1 553 ? 136.575 151.094 133.121 1.00 12726. ? 553 ARG A NE    1 
ATOM   4178  C  CZ    . ARG A 1 553 ? 136.923 152.251 132.576 1.00 12727. ? 553 ARG A CZ    1 
ATOM   4179  N  NH1   . ARG A 1 553 ? 136.046 153.001 131.932 1.00 12737. ? 553 ARG A NH1   1 
ATOM   4180  N  NH2   . ARG A 1 553 ? 138.181 152.665 132.681 1.00 12739. ? 553 ARG A NH2   1 
ATOM   4181  N  N     . VAL A 1 554 ? 131.861 146.046 133.824 1.00 12734. ? 554 VAL A N     1 
ATOM   4182  C  CA    . VAL A 1 554 ? 130.545 145.417 133.787 1.00 12737. ? 554 VAL A CA    1 
ATOM   4183  C  C     . VAL A 1 554 ? 130.288 144.663 135.085 1.00 12744. ? 554 VAL A C     1 
ATOM   4184  O  O     . VAL A 1 554 ? 129.174 144.674 135.623 1.00 12763. ? 554 VAL A O     1 
ATOM   4185  C  CB    . VAL A 1 554 ? 130.432 144.493 132.562 1.00 12739. ? 554 VAL A CB    1 
ATOM   4186  C  CG1   . VAL A 1 554 ? 129.154 143.678 132.620 1.00 12744. ? 554 VAL A CG1   1 
ATOM   4187  C  CG2   . VAL A 1 554 ? 130.492 145.307 131.286 1.00 12755. ? 554 VAL A CG2   1 
ATOM   4188  N  N     . ALA A 1 555 ? 131.320 144.000 135.610 1.00 12739. ? 555 ALA A N     1 
ATOM   4189  C  CA    . ALA A 1 555 ? 131.177 143.275 136.868 1.00 12740. ? 555 ALA A CA    1 
ATOM   4190  C  C     . ALA A 1 555 ? 130.858 144.224 138.018 1.00 12745. ? 555 ALA A C     1 
ATOM   4191  O  O     . ALA A 1 555 ? 130.000 143.935 138.859 1.00 12750. ? 555 ALA A O     1 
ATOM   4192  C  CB    . ALA A 1 555 ? 132.448 142.476 137.154 1.00 12762. ? 555 ALA A CB    1 
ATOM   4193  N  N     . MET A 1 556 ? 131.545 145.364 138.074 1.00 12756. ? 556 MET A N     1 
ATOM   4194  C  CA    . MET A 1 556 ? 131.255 146.345 139.116 1.00 12747. ? 556 MET A CA    1 
ATOM   4195  C  C     . MET A 1 556 ? 129.832 146.865 138.986 1.00 12740. ? 556 MET A C     1 
ATOM   4196  O  O     . MET A 1 556 ? 129.144 147.060 139.991 1.00 12753. ? 556 MET A O     1 
ATOM   4197  C  CB    . MET A 1 556 ? 132.231 147.526 139.094 1.00 12746. ? 556 MET A CB    1 
ATOM   4198  C  CG    . MET A 1 556 ? 133.669 147.192 138.797 1.00 12755. ? 556 MET A CG    1 
ATOM   4199  S  SD    . MET A 1 556 ? 134.591 148.623 138.207 1.00 12743. ? 556 MET A SD    1 
ATOM   4200  C  CE    . MET A 1 556 ? 133.774 149.941 139.100 1.00 12754. ? 556 MET A CE    1 
ATOM   4201  N  N     . PHE A 1 557 ? 129.384 147.101 137.754 1.00 12748. ? 557 PHE A N     1 
ATOM   4202  C  CA    . PHE A 1 557 ? 128.041 147.638 137.571 1.00 12738. ? 557 PHE A CA    1 
ATOM   4203  C  C     . PHE A 1 557 ? 126.966 146.614 137.912 1.00 12733. ? 557 PHE A C     1 
ATOM   4204  O  O     . PHE A 1 557 ? 125.887 146.989 138.381 1.00 12739. ? 557 PHE A O     1 
ATOM   4205  C  CB    . PHE A 1 557 ? 127.872 148.148 136.143 1.00 12745. ? 557 PHE A CB    1 
ATOM   4206  C  CG    . PHE A 1 557 ? 128.573 149.446 135.890 1.00 12731. ? 557 PHE A CG    1 
ATOM   4207  C  CD1   . PHE A 1 557 ? 128.586 150.433 136.858 1.00 12736. ? 557 PHE A CD1   1 
ATOM   4208  C  CD2   . PHE A 1 557 ? 129.233 149.676 134.698 1.00 12738. ? 557 PHE A CD2   1 
ATOM   4209  C  CE1   . PHE A 1 557 ? 129.235 151.626 136.640 1.00 12747. ? 557 PHE A CE1   1 
ATOM   4210  C  CE2   . PHE A 1 557 ? 129.884 150.870 134.475 1.00 12741. ? 557 PHE A CE2   1 
ATOM   4211  C  CZ    . PHE A 1 557 ? 129.884 151.845 135.449 1.00 12745. ? 557 PHE A CZ    1 
ATOM   4212  N  N     . LEU A 1 558 ? 127.232 145.330 137.694 1.00 12737. ? 558 LEU A N     1 
ATOM   4213  C  CA    . LEU A 1 558 ? 126.259 144.294 138.016 1.00 12741. ? 558 LEU A CA    1 
ATOM   4214  C  C     . LEU A 1 558 ? 126.404 143.748 139.430 1.00 12749. ? 558 LEU A C     1 
ATOM   4215  O  O     . LEU A 1 558 ? 125.585 142.922 139.843 1.00 12752. ? 558 LEU A O     1 
ATOM   4216  C  CB    . LEU A 1 558 ? 126.352 143.142 137.013 1.00 12746. ? 558 LEU A CB    1 
ATOM   4217  C  CG    . LEU A 1 558 ? 125.927 143.473 135.583 1.00 12733. ? 558 LEU A CG    1 
ATOM   4218  C  CD1   . LEU A 1 558 ? 126.111 142.271 134.679 1.00 12737. ? 558 LEU A CD1   1 
ATOM   4219  C  CD2   . LEU A 1 558 ? 124.488 143.947 135.559 1.00 12740. ? 558 LEU A CD2   1 
ATOM   4220  N  N     . THR A 1 559 ? 127.418 144.178 140.180 1.00 12750. ? 559 THR A N     1 
ATOM   4221  C  CA    . THR A 1 559 ? 127.582 143.758 141.563 1.00 12737. ? 559 THR A CA    1 
ATOM   4222  C  C     . THR A 1 559 ? 127.426 144.897 142.559 1.00 12737. ? 559 THR A C     1 
ATOM   4223  O  O     . THR A 1 559 ? 127.637 144.679 143.757 1.00 12736. ? 559 THR A O     1 
ATOM   4224  C  CB    . THR A 1 559 ? 128.953 143.100 141.766 1.00 12745. ? 559 THR A CB    1 
ATOM   4225  O  OG1   . THR A 1 559 ? 129.964 143.899 141.143 1.00 12768. ? 559 THR A OG1   1 
ATOM   4226  C  CG2   . THR A 1 559 ? 128.972 141.714 141.158 1.00 12749. ? 559 THR A CG2   1 
ATOM   4227  N  N     . ASP A 1 560 ? 127.059 146.096 142.103 1.00 12753. ? 560 ASP A N     1 
ATOM   4228  C  CA    . ASP A 1 560 ? 126.927 147.273 142.963 1.00 12745. ? 560 ASP A CA    1 
ATOM   4229  C  C     . ASP A 1 560 ? 128.227 147.559 143.715 1.00 12737. ? 560 ASP A C     1 
ATOM   4230  O  O     . ASP A 1 560 ? 128.235 147.802 144.922 1.00 12745. ? 560 ASP A O     1 
ATOM   4231  C  CB    . ASP A 1 560 ? 125.752 147.122 143.931 1.00 12740. ? 560 ASP A CB    1 
ATOM   4232  C  CG    . ASP A 1 560 ? 125.246 148.455 144.445 1.00 12754. ? 560 ASP A CG    1 
ATOM   4233  O  OD1   . ASP A 1 560 ? 125.806 149.497 144.049 1.00 12769. ? 560 ASP A OD1   1 
ATOM   4234  O  OD2   . ASP A 1 560 ? 124.287 148.463 145.245 1.00 12757. ? 560 ASP A OD2   1 
ATOM   4235  N  N     . SER A 1 561 ? 129.336 147.528 142.983 1.00 12737. ? 561 SER A N     1 
ATOM   4236  C  CA    . SER A 1 561 ? 130.653 147.822 143.528 1.00 12735. ? 561 SER A CA    1 
ATOM   4237  C  C     . SER A 1 561 ? 131.190 149.087 142.877 1.00 12745. ? 561 SER A C     1 
ATOM   4238  O  O     . SER A 1 561 ? 131.190 149.203 141.648 1.00 12760. ? 561 SER A O     1 
ATOM   4239  C  CB    . SER A 1 561 ? 131.620 146.660 143.298 1.00 12744. ? 561 SER A CB    1 
ATOM   4240  O  OG    . SER A 1 561 ? 130.951 145.416 143.379 1.00 12755. ? 561 SER A OG    1 
ATOM   4241  N  N     . ASN A 1 562 ? 131.639 150.032 143.696 1.00 12741. ? 562 ASN A N     1 
ATOM   4242  C  CA    . ASN A 1 562 ? 132.200 151.279 143.198 1.00 12735. ? 562 ASN A CA    1 
ATOM   4243  C  C     . ASN A 1 562 ? 133.712 151.225 143.036 1.00 12733. ? 562 ASN A C     1 
ATOM   4244  O  O     . ASN A 1 562 ? 134.307 152.211 142.592 1.00 12749. ? 562 ASN A O     1 
ATOM   4245  C  CB    . ASN A 1 562 ? 131.826 152.436 144.126 1.00 12743. ? 562 ASN A CB    1 
ATOM   4246  C  CG    . ASN A 1 562 ? 132.347 152.244 145.532 1.00 12751. ? 562 ASN A CG    1 
ATOM   4247  O  OD1   . ASN A 1 562 ? 132.488 151.118 146.004 1.00 12750. ? 562 ASN A OD1   1 
ATOM   4248  N  ND2   . ASN A 1 562 ? 132.638 153.346 146.210 1.00 12775. ? 562 ASN A ND2   1 
ATOM   4249  N  N     . ASN A 1 563 ? 134.343 150.109 143.381 1.00 12733. ? 563 ASN A N     1 
ATOM   4250  C  CA    . ASN A 1 563 ? 135.783 149.945 143.266 1.00 12730. ? 563 ASN A CA    1 
ATOM   4251  C  C     . ASN A 1 563 ? 136.087 148.729 142.405 1.00 12730. ? 563 ASN A C     1 
ATOM   4252  O  O     . ASN A 1 563 ? 135.469 147.674 142.567 1.00 12763. ? 563 ASN A O     1 
ATOM   4253  C  CB    . ASN A 1 563 ? 136.433 149.786 144.641 1.00 12728. ? 563 ASN A CB    1 
ATOM   4254  C  CG    . ASN A 1 563 ? 137.881 150.220 144.654 1.00 12696. ? 563 ASN A CG    1 
ATOM   4255  O  OD1   . ASN A 1 563 ? 138.627 149.963 143.712 1.00 12726. ? 563 ASN A OD1   1 
ATOM   4256  N  ND2   . ASN A 1 563 ? 138.289 150.881 145.729 1.00 12642. ? 563 ASN A ND2   1 
ATOM   4257  N  N     . ILE A 1 564 ? 137.042 148.884 141.486 1.00 12727. ? 564 ILE A N     1 
ATOM   4258  C  CA    . ILE A 1 564 ? 137.408 147.771 140.619 1.00 12740. ? 564 ILE A CA    1 
ATOM   4259  C  C     . ILE A 1 564 ? 138.069 146.654 141.416 1.00 12753. ? 564 ILE A C     1 
ATOM   4260  O  O     . ILE A 1 564 ? 138.031 145.488 141.009 1.00 12765. ? 564 ILE A O     1 
ATOM   4261  C  CB    . ILE A 1 564 ? 138.308 148.261 139.469 1.00 12737. ? 564 ILE A CB    1 
ATOM   4262  C  CG1   . ILE A 1 564 ? 138.423 147.185 138.387 1.00 12730. ? 564 ILE A CG1   1 
ATOM   4263  C  CG2   . ILE A 1 564 ? 139.679 148.659 139.988 1.00 12762. ? 564 ILE A CG2   1 
ATOM   4264  C  CD1   . ILE A 1 564 ? 138.999 147.683 137.087 1.00 12753. ? 564 ILE A CD1   1 
ATOM   4265  N  N     . LYS A 1 565 ? 138.679 146.978 142.558 1.00 12745. ? 565 LYS A N     1 
ATOM   4266  C  CA    . LYS A 1 565 ? 139.309 145.951 143.378 1.00 12744. ? 565 LYS A CA    1 
ATOM   4267  C  C     . LYS A 1 565 ? 138.296 144.991 143.985 1.00 12739. ? 565 LYS A C     1 
ATOM   4268  O  O     . LYS A 1 565 ? 138.674 143.888 144.389 1.00 12749. ? 565 LYS A O     1 
ATOM   4269  C  CB    . LYS A 1 565 ? 140.136 146.595 144.489 1.00 12758. ? 565 LYS A CB    1 
ATOM   4270  C  CG    . LYS A 1 565 ? 141.371 147.331 144.007 1.00 12748. ? 565 LYS A CG    1 
ATOM   4271  C  CD    . LYS A 1 565 ? 142.084 148.008 145.165 1.00 12733. ? 565 LYS A CD    1 
ATOM   4272  C  CE    . LYS A 1 565 ? 143.274 148.821 144.689 1.00 12730. ? 565 LYS A CE    1 
ATOM   4273  N  NZ    . LYS A 1 565 ? 144.469 147.970 144.450 1.00 12754. ? 565 LYS A NZ    1 
ATOM   4274  N  N     . GLU A 1 566 ? 137.024 145.382 144.058 1.00 12730. ? 566 GLU A N     1 
ATOM   4275  C  CA    . GLU A 1 566 ? 136.007 144.506 144.624 1.00 12731. ? 566 GLU A CA    1 
ATOM   4276  C  C     . GLU A 1 566 ? 135.699 143.317 143.728 1.00 12736. ? 566 GLU A C     1 
ATOM   4277  O  O     . GLU A 1 566 ? 135.146 142.324 144.209 1.00 12756. ? 566 GLU A O     1 
ATOM   4278  C  CB    . GLU A 1 566 ? 134.728 145.293 144.897 1.00 12741. ? 566 GLU A CB    1 
ATOM   4279  C  CG    . GLU A 1 566 ? 134.939 146.542 145.728 1.00 12750. ? 566 GLU A CG    1 
ATOM   4280  C  CD    . GLU A 1 566 ? 134.712 146.301 147.206 1.00 12758. ? 566 GLU A CD    1 
ATOM   4281  O  OE1   . GLU A 1 566 ? 134.779 145.131 147.636 1.00 12749. ? 566 GLU A OE1   1 
ATOM   4282  O  OE2   . GLU A 1 566 ? 134.468 147.282 147.939 1.00 12773. ? 566 GLU A OE2   1 
ATOM   4283  N  N     . VAL A 1 567 ? 136.035 143.394 142.442 1.00 12739. ? 567 VAL A N     1 
ATOM   4284  C  CA    . VAL A 1 567 ? 135.807 142.289 141.517 1.00 12746. ? 567 VAL A CA    1 
ATOM   4285  C  C     . VAL A 1 567 ? 137.089 141.574 141.128 1.00 12744. ? 567 VAL A C     1 
ATOM   4286  O  O     . VAL A 1 567 ? 137.019 140.558 140.418 1.00 12750. ? 567 VAL A O     1 
ATOM   4287  C  CB    . VAL A 1 567 ? 135.057 142.754 140.252 1.00 12742. ? 567 VAL A CB    1 
ATOM   4288  C  CG1   . VAL A 1 567 ? 133.745 143.411 140.633 1.00 12747. ? 567 VAL A CG1   1 
ATOM   4289  C  CG2   . VAL A 1 567 ? 135.916 143.699 139.441 1.00 12757. ? 567 VAL A CG2   1 
ATOM   4290  N  N     . LEU A 1 568 ? 138.249 142.064 141.554 1.00 12727. ? 568 LEU A N     1 
ATOM   4291  C  CA    . LEU A 1 568 ? 139.502 141.347 141.378 1.00 12727. ? 568 LEU A CA    1 
ATOM   4292  C  C     . LEU A 1 568 ? 139.724 140.447 142.584 1.00 12737. ? 568 LEU A C     1 
ATOM   4293  O  O     . LEU A 1 568 ? 139.566 140.883 143.728 1.00 12746. ? 568 LEU A O     1 
ATOM   4294  C  CB    . LEU A 1 568 ? 140.672 142.316 141.218 1.00 12738. ? 568 LEU A CB    1 
ATOM   4295  C  CG    . LEU A 1 568 ? 140.502 143.433 140.190 1.00 12744. ? 568 LEU A CG    1 
ATOM   4296  C  CD1   . LEU A 1 568 ? 141.697 144.363 140.225 1.00 12753. ? 568 LEU A CD1   1 
ATOM   4297  C  CD2   . LEU A 1 568 ? 140.309 142.858 138.801 1.00 12753. ? 568 LEU A CD2   1 
ATOM   4298  N  N     . LEU A 1 569 ? 140.077 139.188 142.324 1.00 12752. ? 569 LEU A N     1 
ATOM   4299  C  CA    . LEU A 1 569 ? 140.234 138.230 143.412 1.00 12749. ? 569 LEU A CA    1 
ATOM   4300  C  C     . LEU A 1 569 ? 141.388 138.620 144.327 1.00 12749. ? 569 LEU A C     1 
ATOM   4301  O  O     . LEU A 1 569 ? 141.255 138.601 145.555 1.00 12754. ? 569 LEU A O     1 
ATOM   4302  C  CB    . LEU A 1 569 ? 140.440 136.828 142.845 1.00 12748. ? 569 LEU A CB    1 
ATOM   4303  C  CG    . LEU A 1 569 ? 139.164 136.008 142.668 1.00 12749. ? 569 LEU A CG    1 
ATOM   4304  C  CD1   . LEU A 1 569 ? 139.404 134.842 141.731 1.00 12758. ? 569 LEU A CD1   1 
ATOM   4305  C  CD2   . LEU A 1 569 ? 138.659 135.525 144.010 1.00 12765. ? 569 LEU A CD2   1 
ATOM   4306  N  N     . PHE A 1 570 ? 142.528 138.987 143.748 1.00 12740. ? 570 PHE A N     1 
ATOM   4307  C  CA    . PHE A 1 570 ? 143.725 139.343 144.508 1.00 12738. ? 570 PHE A CA    1 
ATOM   4308  C  C     . PHE A 1 570 ? 144.273 140.663 143.986 1.00 12728. ? 570 PHE A C     1 
ATOM   4309  O  O     . PHE A 1 570 ? 145.185 140.683 143.150 1.00 12740. ? 570 PHE A O     1 
ATOM   4310  C  CB    . PHE A 1 570 ? 144.778 138.238 144.430 1.00 12747. ? 570 PHE A CB    1 
ATOM   4311  C  CG    . PHE A 1 570 ? 144.285 136.897 144.887 1.00 12737. ? 570 PHE A CG    1 
ATOM   4312  C  CD1   . PHE A 1 570 ? 144.372 136.530 146.217 1.00 12747. ? 570 PHE A CD1   1 
ATOM   4313  C  CD2   . PHE A 1 570 ? 143.736 136.004 143.987 1.00 12745. ? 570 PHE A CD2   1 
ATOM   4314  C  CE1   . PHE A 1 570 ? 143.917 135.299 146.639 1.00 12751. ? 570 PHE A CE1   1 
ATOM   4315  C  CE2   . PHE A 1 570 ? 143.282 134.773 144.404 1.00 12741. ? 570 PHE A CE2   1 
ATOM   4316  C  CZ    . PHE A 1 570 ? 143.373 134.420 145.732 1.00 12738. ? 570 PHE A CZ    1 
ATOM   4317  N  N     . PRO A 1 571 ? 143.731 141.787 144.450 1.00 12711. ? 571 PRO A N     1 
ATOM   4318  C  CA    . PRO A 1 571 ? 144.283 143.086 144.050 1.00 12729. ? 571 PRO A CA    1 
ATOM   4319  C  C     . PRO A 1 571 ? 145.717 143.246 144.530 1.00 12748. ? 571 PRO A C     1 
ATOM   4320  O  O     . PRO A 1 571 ? 146.108 142.729 145.578 1.00 12768. ? 571 PRO A O     1 
ATOM   4321  C  CB    . PRO A 1 571 ? 143.347 144.097 144.723 1.00 12741. ? 571 PRO A CB    1 
ATOM   4322  C  CG    . PRO A 1 571 ? 142.668 143.342 145.806 1.00 12734. ? 571 PRO A CG    1 
ATOM   4323  C  CD    . PRO A 1 571 ? 142.574 141.925 145.349 1.00 12729. ? 571 PRO A CD    1 
ATOM   4324  N  N     . ALA A 1 572 ? 146.505 143.973 143.744 1.00 12744. ? 572 ALA A N     1 
ATOM   4325  C  CA    . ALA A 1 572 ? 147.921 144.143 144.045 1.00 12748. ? 572 ALA A CA    1 
ATOM   4326  C  C     . ALA A 1 572 ? 148.099 145.111 145.207 1.00 12757. ? 572 ALA A C     1 
ATOM   4327  O  O     . ALA A 1 572 ? 147.649 146.259 145.144 1.00 12739. ? 572 ALA A O     1 
ATOM   4328  C  CB    . ALA A 1 572 ? 148.667 144.644 142.813 1.00 12754. ? 572 ALA A CB    1 
ATOM   4329  N  N     . MET A 1 573 ? 148.737 144.633 146.281 1.00 13124. ? 573 MET A N     1 
ATOM   4330  C  CA    . MET A 1 573 ? 148.959 145.481 147.482 1.00 13106. ? 573 MET A CA    1 
ATOM   4331  C  C     . MET A 1 573 ? 150.455 145.466 147.832 1.00 13091. ? 573 MET A C     1 
ATOM   4332  O  O     . MET A 1 573 ? 151.011 144.359 148.002 1.00 13132. ? 573 MET A O     1 
ATOM   4333  C  CB    . MET A 1 573 ? 148.163 144.951 148.680 1.00 13112. ? 573 MET A CB    1 
ATOM   4334  C  CG    . MET A 1 573 ? 146.704 144.659 148.381 1.00 13125. ? 573 MET A CG    1 
ATOM   4335  S  SD    . MET A 1 573 ? 145.708 146.145 148.153 1.00 13074. ? 573 MET A SD    1 
ATOM   4336  C  CE    . MET A 1 573 ? 145.702 146.785 149.834 1.00 13035. ? 573 MET A CE    1 
ATOM   4337  N  N     . LYS A 1 574 ? 151.114 146.588 147.868 1.00 12641. ? 574 LYS A N     1 
ATOM   4338  C  CA    . LYS A 1 574 ? 152.554 146.630 148.228 1.00 12698. ? 574 LYS A CA    1 
ATOM   4339  C  C     . LYS A 1 574 ? 152.732 146.000 149.619 1.00 12699. ? 574 LYS A C     1 
ATOM   4340  O  O     . LYS A 1 574 ? 151.901 146.275 150.514 1.00 12661. ? 574 LYS A O     1 
ATOM   4341  C  CB    . LYS A 1 574 ? 153.078 148.070 148.185 1.00 12589. ? 574 LYS A CB    1 
ATOM   4342  C  CG    . LYS A 1 574 ? 152.851 148.783 146.859 1.00 12668. ? 574 LYS A CG    1 
ATOM   4343  C  CD    . LYS A 1 574 ? 153.706 150.030 146.673 1.00 12628. ? 574 LYS A CD    1 
ATOM   4344  C  CE    . LYS A 1 574 ? 155.163 149.706 146.561 1.00 12628. ? 574 LYS A CE    1 
ATOM   4345  N  NZ    . LYS A 1 574 ? 155.963 150.896 146.260 1.00 12706. ? 574 LYS A NZ    1 
ATOM   4346  N  N     . PRO A 1 575 ? 153.760 145.232 149.870 1.00 13689. ? 575 PRO A N     1 
ATOM   4347  C  CA    . PRO A 1 575 ? 153.944 144.519 151.128 1.00 13746. ? 575 PRO A CA    1 
ATOM   4348  C  C     . PRO A 1 575 ? 154.144 145.463 152.305 1.00 13762. ? 575 PRO A C     1 
ATOM   4349  O  O     . PRO A 1 575 ? 154.785 146.521 152.142 1.00 13665. ? 575 PRO A O     1 
ATOM   4350  C  CB    . PRO A 1 575 ? 155.186 143.651 150.860 1.00 13750. ? 575 PRO A CB    1 
ATOM   4351  C  CG    . PRO A 1 575 ? 155.912 144.381 149.754 1.00 13726. ? 575 PRO A CG    1 
ATOM   4352  C  CD    . PRO A 1 575 ? 154.806 144.970 148.897 1.00 13706. ? 575 PRO A CD    1 
ATOM   4353  N  N     . GLU A 1 576 ? 153.609 145.089 153.470 1.00 15792. ? 576 GLU A N     1 
ATOM   4354  C  CA    . GLU A 1 576 ? 153.735 145.942 154.682 1.00 15857. ? 576 GLU A CA    1 
ATOM   4355  C  C     . GLU A 1 576 ? 155.064 145.632 155.389 1.00 15977. ? 576 GLU A C     1 
ATOM   4356  O  O     . GLU A 1 576 ? 155.270 144.462 155.780 1.00 15992. ? 576 GLU A O     1 
ATOM   4357  C  CB    . GLU A 1 576 ? 152.511 145.743 155.577 1.00 15901. ? 576 GLU A CB    1 
ATOM   4358  C  CG    . GLU A 1 576 ? 152.026 144.298 155.626 1.00 15892. ? 576 GLU A CG    1 
ATOM   4359  C  CD    . GLU A 1 576 ? 150.597 144.149 156.113 1.00 15904. ? 576 GLU A CD    1 
ATOM   4360  O  OE1   . GLU A 1 576 ? 149.956 145.185 156.393 1.00 15901. ? 576 GLU A OE1   1 
ATOM   4361  O  OE2   . GLU A 1 576 ? 150.123 142.998 156.212 1.00 15918. ? 576 GLU A OE2   1 
ATOM   4362  N  N     . ASP A 1 577 ? 155.961 146.577 155.447 1.00 17513. ? 577 ASP A N     1 
ATOM   4363  C  CA    . ASP A 1 577 ? 157.275 146.377 156.114 1.00 17563. ? 577 ASP A CA    1 
ATOM   4364  C  C     . ASP A 1 577 ? 157.021 145.791 157.500 1.00 17632. ? 577 ASP A C     1 
ATOM   4365  O  O     . ASP A 1 577 ? 156.161 146.335 158.229 1.00 17617. ? 577 ASP A O     1 
ATOM   4366  C  CB    . ASP A 1 577 ? 158.063 147.675 156.171 1.00 17558. ? 577 ASP A CB    1 
ATOM   4367  C  CG    . ASP A 1 577 ? 158.609 148.170 154.839 1.00 17518. ? 577 ASP A CG    1 
ATOM   4368  O  OD1   . ASP A 1 577 ? 158.631 147.372 153.879 1.00 17405. ? 577 ASP A OD1   1 
ATOM   4369  O  OD2   . ASP A 1 577 ? 159.006 149.353 154.772 1.00 17551. ? 577 ASP A OD2   1 
ATOM   4370  N  N     . LYS A 1 578 ? 157.718 144.798 157.884 1.00 19951. ? 578 LYS A N     1 
ATOM   4371  C  CA    . LYS A 1 578 ? 157.529 144.063 159.124 1.00 19991. ? 578 LYS A CA    1 
ATOM   4372  C  C     . LYS A 1 578 ? 158.878 143.781 159.770 1.00 20018. ? 578 LYS A C     1 
ATOM   4373  O  O     . LYS A 1 578 ? 159.912 143.717 159.102 1.00 20020. ? 578 LYS A O     1 
ATOM   4374  C  CB    . LYS A 1 578 ? 156.778 142.746 158.882 1.00 20006. ? 578 LYS A CB    1 
ATOM   4375  C  CG    . LYS A 1 578 ? 157.233 142.000 157.638 1.00 20004. ? 578 LYS A CG    1 
ATOM   4376  C  CD    . LYS A 1 578 ? 156.168 141.034 157.148 1.00 20018. ? 578 LYS A CD    1 
ATOM   4377  C  CE    . LYS A 1 578 ? 156.441 140.592 155.720 1.00 20021. ? 578 LYS A CE    1 
ATOM   4378  N  NZ    . LYS A 1 578 ? 155.300 139.827 155.146 1.00 20005. ? 578 LYS A NZ    1 
ATOM   4379  N  N     . LYS A 1 579 ? 158.849 143.614 161.088 1.00 20247. ? 579 LYS A N     1 
ATOM   4380  C  CA    . LYS A 1 579 ? 160.052 143.310 161.853 1.00 20259. ? 579 LYS A CA    1 
ATOM   4381  C  C     . LYS A 1 579 ? 159.818 142.117 162.773 1.00 20259. ? 579 LYS A C     1 
ATOM   4382  O  O     . LYS A 1 579 ? 158.702 141.894 163.243 1.00 20259. ? 579 LYS A O     1 
ATOM   4383  C  CB    . LYS A 1 579 ? 160.494 144.527 162.668 1.00 20261. ? 579 LYS A CB    1 
ATOM   4384  C  CG    . LYS A 1 579 ? 160.814 145.754 161.830 1.00 20258. ? 579 LYS A CG    1 
ATOM   4385  C  CD    . LYS A 1 579 ? 161.096 146.962 162.706 1.00 20242. ? 579 LYS A CD    1 
ATOM   4386  C  CE    . LYS A 1 579 ? 161.246 148.223 161.872 1.00 20199. ? 579 LYS A CE    1 
ATOM   4387  N  NZ    . LYS A 1 579 ? 161.570 149.407 162.712 1.00 20033. ? 579 LYS A NZ    1 
ATOM   4388  N  N     . VAL B 1 71  ? 156.000 137.614 87.541  1.00 17042. ? 71  VAL B N     1 
ATOM   4389  C  CA    . VAL B 1 71  ? 156.995 138.668 87.393  1.00 17050. ? 71  VAL B CA    1 
ATOM   4390  C  C     . VAL B 1 71  ? 157.565 139.049 88.753  1.00 17038. ? 71  VAL B C     1 
ATOM   4391  O  O     . VAL B 1 71  ? 157.442 138.300 89.721  1.00 17026. ? 71  VAL B O     1 
ATOM   4392  C  CB    . VAL B 1 71  ? 156.400 139.899 86.689  1.00 17046. ? 71  VAL B CB    1 
ATOM   4393  C  CG1   . VAL B 1 71  ? 156.220 139.623 85.205  1.00 17045. ? 71  VAL B CG1   1 
ATOM   4394  C  CG2   . VAL B 1 71  ? 155.078 140.288 87.329  1.00 17034. ? 71  VAL B CG2   1 
ATOM   4395  N  N     . ASP B 1 72  ? 158.187 140.217 88.817  1.00 17154. ? 72  ASP B N     1 
ATOM   4396  C  CA    . ASP B 1 72  ? 158.777 140.694 90.061  1.00 17138. ? 72  ASP B CA    1 
ATOM   4397  C  C     . ASP B 1 72  ? 157.673 141.067 91.041  1.00 17090. ? 72  ASP B C     1 
ATOM   4398  O  O     . ASP B 1 72  ? 156.801 141.875 90.697  1.00 17081. ? 72  ASP B O     1 
ATOM   4399  C  CB    . ASP B 1 72  ? 159.677 141.896 89.782  1.00 17147. ? 72  ASP B CB    1 
ATOM   4400  C  CG    . ASP B 1 72  ? 160.480 142.327 90.996  1.00 17140. ? 72  ASP B CG    1 
ATOM   4401  O  OD1   . ASP B 1 72  ? 160.436 141.632 92.031  1.00 17138. ? 72  ASP B OD1   1 
ATOM   4402  O  OD2   . ASP B 1 72  ? 161.161 143.371 90.914  1.00 17144. ? 72  ASP B OD2   1 
ATOM   4403  N  N     . PRO B 1 73  ? 157.655 140.502 92.251  1.00 15923. ? 73  PRO B N     1 
ATOM   4404  C  CA    . PRO B 1 73  ? 156.639 140.907 93.233  1.00 15898. ? 73  PRO B CA    1 
ATOM   4405  C  C     . PRO B 1 73  ? 156.651 142.391 93.549  1.00 15881. ? 73  PRO B C     1 
ATOM   4406  O  O     . PRO B 1 73  ? 155.584 142.974 93.777  1.00 15837. ? 73  PRO B O     1 
ATOM   4407  C  CB    . PRO B 1 73  ? 157.002 140.066 94.462  1.00 15896. ? 73  PRO B CB    1 
ATOM   4408  C  CG    . PRO B 1 73  ? 157.625 138.846 93.885  1.00 15900. ? 73  PRO B CG    1 
ATOM   4409  C  CD    . PRO B 1 73  ? 158.430 139.339 92.715  1.00 15918. ? 73  PRO B CD    1 
ATOM   4410  N  N     . ASN B 1 74  ? 157.826 143.022 93.575  1.00 16026. ? 74  ASN B N     1 
ATOM   4411  C  CA    . ASN B 1 74  ? 157.893 144.457 93.827  1.00 16017. ? 74  ASN B CA    1 
ATOM   4412  C  C     . ASN B 1 74  ? 157.235 145.255 92.707  1.00 15978. ? 74  ASN B C     1 
ATOM   4413  O  O     . ASN B 1 74  ? 156.498 146.212 92.974  1.00 15934. ? 74  ASN B O     1 
ATOM   4414  C  CB    . ASN B 1 74  ? 159.346 144.889 94.009  1.00 16034. ? 74  ASN B CB    1 
ATOM   4415  C  CG    . ASN B 1 74  ? 159.959 144.340 95.279  1.00 16041. ? 74  ASN B CG    1 
ATOM   4416  O  OD1   . ASN B 1 74  ? 159.482 144.614 96.380  1.00 16034. ? 74  ASN B OD1   1 
ATOM   4417  N  ND2   . ASN B 1 74  ? 161.020 143.557 95.134  1.00 16046. ? 74  ASN B ND2   1 
ATOM   4418  N  N     . GLN B 1 75  ? 157.489 144.877 91.453  1.00 15706. ? 75  GLN B N     1 
ATOM   4419  C  CA    . GLN B 1 75  ? 156.840 145.553 90.335  1.00 15690. ? 75  GLN B CA    1 
ATOM   4420  C  C     . GLN B 1 75  ? 155.332 145.355 90.376  1.00 15607. ? 75  GLN B C     1 
ATOM   4421  O  O     . GLN B 1 75  ? 154.570 146.293 90.109  1.00 15573. ? 75  GLN B O     1 
ATOM   4422  C  CB    . GLN B 1 75  ? 157.411 145.049 89.012  1.00 15718. ? 75  GLN B CB    1 
ATOM   4423  C  CG    . GLN B 1 75  ? 158.836 145.490 88.758  1.00 15724. ? 75  GLN B CG    1 
ATOM   4424  C  CD    . GLN B 1 75  ? 158.972 146.997 88.720  1.00 15714. ? 75  GLN B CD    1 
ATOM   4425  O  OE1   . GLN B 1 75  ? 159.632 147.595 89.570  1.00 15712. ? 75  GLN B OE1   1 
ATOM   4426  N  NE2   . GLN B 1 75  ? 158.344 147.623 87.732  1.00 15701. ? 75  GLN B NE2   1 
ATOM   4427  N  N     . TYR B 1 76  ? 154.884 144.142 90.702  1.00 13847. ? 76  TYR B N     1 
ATOM   4428  C  CA    . TYR B 1 76  ? 153.453 143.886 90.818  1.00 13771. ? 76  TYR B CA    1 
ATOM   4429  C  C     . TYR B 1 76  ? 152.834 144.752 91.906  1.00 13733. ? 76  TYR B C     1 
ATOM   4430  O  O     . TYR B 1 76  ? 151.762 145.337 91.714  1.00 13738. ? 76  TYR B O     1 
ATOM   4431  C  CB    . TYR B 1 76  ? 153.213 142.404 91.101  1.00 13783. ? 76  TYR B CB    1 
ATOM   4432  C  CG    . TYR B 1 76  ? 151.759 141.995 91.083  1.00 13738. ? 76  TYR B CG    1 
ATOM   4433  C  CD1   . TYR B 1 76  ? 150.984 142.066 92.230  1.00 13731. ? 76  TYR B CD1   1 
ATOM   4434  C  CD2   . TYR B 1 76  ? 151.163 141.534 89.919  1.00 13742. ? 76  TYR B CD2   1 
ATOM   4435  C  CE1   . TYR B 1 76  ? 149.658 141.693 92.219  1.00 13729. ? 76  TYR B CE1   1 
ATOM   4436  C  CE2   . TYR B 1 76  ? 149.837 141.159 89.898  1.00 13733. ? 76  TYR B CE2   1 
ATOM   4437  C  CZ    . TYR B 1 76  ? 149.089 141.240 91.051  1.00 13732. ? 76  TYR B CZ    1 
ATOM   4438  O  OH    . TYR B 1 76  ? 147.766 140.866 91.038  1.00 13725. ? 76  TYR B OH    1 
ATOM   4439  N  N     . TYR B 1 77  ? 153.503 144.851 93.056  1.00 12863. ? 77  TYR B N     1 
ATOM   4440  C  CA    . TYR B 1 77  ? 152.988 145.677 94.141  1.00 12816. ? 77  TYR B CA    1 
ATOM   4441  C  C     . TYR B 1 77  ? 152.915 147.141 93.732  1.00 12823. ? 77  TYR B C     1 
ATOM   4442  O  O     . TYR B 1 77  ? 151.922 147.821 94.013  1.00 12814. ? 77  TYR B O     1 
ATOM   4443  C  CB    . TYR B 1 77  ? 153.858 145.511 95.385  1.00 12797. ? 77  TYR B CB    1 
ATOM   4444  C  CG    . TYR B 1 77  ? 153.555 146.507 96.479  1.00 12752. ? 77  TYR B CG    1 
ATOM   4445  C  CD1   . TYR B 1 77  ? 152.475 146.327 97.328  1.00 12750. ? 77  TYR B CD1   1 
ATOM   4446  C  CD2   . TYR B 1 77  ? 154.354 147.625 96.666  1.00 12750. ? 77  TYR B CD2   1 
ATOM   4447  C  CE1   . TYR B 1 77  ? 152.195 147.233 98.328  1.00 12755. ? 77  TYR B CE1   1 
ATOM   4448  C  CE2   . TYR B 1 77  ? 154.082 148.537 97.664  1.00 12743. ? 77  TYR B CE2   1 
ATOM   4449  C  CZ    . TYR B 1 77  ? 153.002 148.336 98.492  1.00 12748. ? 77  TYR B CZ    1 
ATOM   4450  O  OH    . TYR B 1 77  ? 152.726 149.241 99.489  1.00 12747. ? 77  TYR B OH    1 
ATOM   4451  N  N     . LYS B 1 78  ? 153.953 147.643 93.063  1.00 13379. ? 78  LYS B N     1 
ATOM   4452  C  CA    . LYS B 1 78  ? 153.954 149.039 92.638  1.00 13362. ? 78  LYS B CA    1 
ATOM   4453  C  C     . LYS B 1 78  ? 152.833 149.314 91.641  1.00 13359. ? 78  LYS B C     1 
ATOM   4454  O  O     . LYS B 1 78  ? 152.109 150.312 91.760  1.00 13374. ? 78  LYS B O     1 
ATOM   4455  C  CB    . LYS B 1 78  ? 155.312 149.398 92.038  1.00 13373. ? 78  LYS B CB    1 
ATOM   4456  C  CG    . LYS B 1 78  ? 155.499 150.876 91.760  1.00 13362. ? 78  LYS B CG    1 
ATOM   4457  C  CD    . LYS B 1 78  ? 156.570 151.102 90.709  1.00 13365. ? 78  LYS B CD    1 
ATOM   4458  C  CE    . LYS B 1 78  ? 156.203 150.432 89.396  1.00 13382. ? 78  LYS B CE    1 
ATOM   4459  N  NZ    . LYS B 1 78  ? 154.876 150.885 88.896  1.00 13378. ? 78  LYS B NZ    1 
ATOM   4460  N  N     . ILE B 1 79  ? 152.665 148.427 90.658  1.00 12928. ? 79  ILE B N     1 
ATOM   4461  C  CA    . ILE B 1 79  ? 151.635 148.627 89.642  1.00 12902. ? 79  ILE B CA    1 
ATOM   4462  C  C     . ILE B 1 79  ? 150.248 148.572 90.271  1.00 12911. ? 79  ILE B C     1 
ATOM   4463  O  O     . ILE B 1 79  ? 149.371 149.384 89.952  1.00 12912. ? 79  ILE B O     1 
ATOM   4464  C  CB    . ILE B 1 79  ? 151.786 147.592 88.514  1.00 12894. ? 79  ILE B CB    1 
ATOM   4465  C  CG1   . ILE B 1 79  ? 153.078 147.841 87.737  1.00 12894. ? 79  ILE B CG1   1 
ATOM   4466  C  CG2   . ILE B 1 79  ? 150.592 147.643 87.580  1.00 12892. ? 79  ILE B CG2   1 
ATOM   4467  C  CD1   . ILE B 1 79  ? 153.310 146.860 86.613  1.00 12889. ? 79  ILE B CD1   1 
ATOM   4468  N  N     . ARG B 1 80  ? 150.027 147.613 91.173  1.00 13265. ? 80  ARG B N     1 
ATOM   4469  C  CA    . ARG B 1 80  ? 148.718 147.499 91.806  1.00 13267. ? 80  ARG B CA    1 
ATOM   4470  C  C     . ARG B 1 80  ? 148.432 148.693 92.704  1.00 13271. ? 80  ARG B C     1 
ATOM   4471  O  O     . ARG B 1 80  ? 147.291 149.163 92.775  1.00 13291. ? 80  ARG B O     1 
ATOM   4472  C  CB    . ARG B 1 80  ? 148.622 146.194 92.591  1.00 13274. ? 80  ARG B CB    1 
ATOM   4473  C  CG    . ARG B 1 80  ? 148.199 145.015 91.738  1.00 13281. ? 80  ARG B CG    1 
ATOM   4474  C  CD    . ARG B 1 80  ? 146.762 145.162 91.270  1.00 13269. ? 80  ARG B CD    1 
ATOM   4475  N  NE    . ARG B 1 80  ? 145.806 144.695 92.266  1.00 13266. ? 80  ARG B NE    1 
ATOM   4476  C  CZ    . ARG B 1 80  ? 144.494 144.652 92.079  1.00 13276. ? 80  ARG B CZ    1 
ATOM   4477  N  NH1   . ARG B 1 80  ? 143.944 145.058 90.947  1.00 13286. ? 80  ARG B NH1   1 
ATOM   4478  N  NH2   . ARG B 1 80  ? 143.715 144.188 93.052  1.00 13270. ? 80  ARG B NH2   1 
ATOM   4479  N  N     . SER B 1 81  ? 149.451 149.200 93.402  1.00 13417. ? 81  SER B N     1 
ATOM   4480  C  CA    . SER B 1 81  ? 149.257 150.402 94.204  1.00 13439. ? 81  SER B CA    1 
ATOM   4481  C  C     . SER B 1 81  ? 148.883 151.587 93.326  1.00 13458. ? 81  SER B C     1 
ATOM   4482  O  O     . SER B 1 81  ? 147.985 152.365 93.671  1.00 13478. ? 81  SER B O     1 
ATOM   4483  C  CB    . SER B 1 81  ? 150.520 150.706 95.008  1.00 13453. ? 81  SER B CB    1 
ATOM   4484  O  OG    . SER B 1 81  ? 150.880 149.604 95.820  1.00 13443. ? 81  SER B OG    1 
ATOM   4485  N  N     . GLN B 1 82  ? 149.551 151.735 92.181  1.00 13775. ? 82  GLN B N     1 
ATOM   4486  C  CA    . GLN B 1 82  ? 149.210 152.813 91.259  1.00 13794. ? 82  GLN B CA    1 
ATOM   4487  C  C     . GLN B 1 82  ? 147.775 152.673 90.762  1.00 13779. ? 82  GLN B C     1 
ATOM   4488  O  O     . GLN B 1 82  ? 147.025 153.653 90.695  1.00 13797. ? 82  GLN B O     1 
ATOM   4489  C  CB    . GLN B 1 82  ? 150.189 152.825 90.085  1.00 13802. ? 82  GLN B CB    1 
ATOM   4490  C  CG    . GLN B 1 82  ? 150.670 154.210 89.703  1.00 13816. ? 82  GLN B CG    1 
ATOM   4491  C  CD    . GLN B 1 82  ? 151.422 154.888 90.828  1.00 13823. ? 82  GLN B CD    1 
ATOM   4492  O  OE1   . GLN B 1 82  ? 152.432 154.377 91.310  1.00 13824. ? 82  GLN B OE1   1 
ATOM   4493  N  NE2   . GLN B 1 82  ? 150.932 156.045 91.254  1.00 13832. ? 82  GLN B NE2   1 
ATOM   4494  N  N     . ALA B 1 83  ? 147.375 151.449 90.412  1.00 13189. ? 83  ALA B N     1 
ATOM   4495  C  CA    . ALA B 1 83  ? 146.028 151.203 89.913  1.00 13179. ? 83  ALA B CA    1 
ATOM   4496  C  C     . ALA B 1 83  ? 144.970 151.516 90.966  1.00 13178. ? 83  ALA B C     1 
ATOM   4497  O  O     . ALA B 1 83  ? 143.936 152.124 90.670  1.00 13207. ? 83  ALA B O     1 
ATOM   4498  C  CB    . ALA B 1 83  ? 145.907 149.751 89.444  1.00 13182. ? 83  ALA B CB    1 
ATOM   4499  N  N     . ILE B 1 84  ? 145.220 151.105 92.209  1.00 12799. ? 84  ILE B N     1 
ATOM   4500  C  CA    . ILE B 1 84  ? 144.255 151.354 93.275  1.00 12785. ? 84  ILE B CA    1 
ATOM   4501  C  C     . ILE B 1 84  ? 144.181 152.842 93.591  1.00 12833. ? 84  ILE B C     1 
ATOM   4502  O  O     . ILE B 1 84  ? 143.103 153.376 93.876  1.00 12832. ? 84  ILE B O     1 
ATOM   4503  C  CB    . ILE B 1 84  ? 144.601 150.515 94.517  1.00 12757. ? 84  ILE B CB    1 
ATOM   4504  C  CG1   . ILE B 1 84  ? 144.450 149.028 94.200  1.00 12752. ? 84  ILE B CG1   1 
ATOM   4505  C  CG2   . ILE B 1 84  ? 143.708 150.885 95.683  1.00 12769. ? 84  ILE B CG2   1 
ATOM   4506  C  CD1   . ILE B 1 84  ? 143.161 148.681 93.492  1.00 12751. ? 84  ILE B CD1   1 
ATOM   4507  N  N     . HIS B 1 85  ? 145.317 153.539 93.537  1.00 14086. ? 85  HIS B N     1 
ATOM   4508  C  CA    . HIS B 1 85  ? 145.287 154.986 93.719  1.00 14120. ? 85  HIS B CA    1 
ATOM   4509  C  C     . HIS B 1 85  ? 144.480 155.660 92.616  1.00 14128. ? 85  HIS B C     1 
ATOM   4510  O  O     . HIS B 1 85  ? 143.705 156.589 92.879  1.00 14141. ? 85  HIS B O     1 
ATOM   4511  C  CB    . HIS B 1 85  ? 146.708 155.541 93.760  1.00 14137. ? 85  HIS B CB    1 
ATOM   4512  C  CG    . HIS B 1 85  ? 146.770 157.017 93.990  1.00 14147. ? 85  HIS B CG    1 
ATOM   4513  N  ND1   . HIS B 1 85  ? 147.040 157.916 92.982  1.00 14154. ? 85  HIS B ND1   1 
ATOM   4514  C  CD2   . HIS B 1 85  ? 146.590 157.752 95.112  1.00 14159. ? 85  HIS B CD2   1 
ATOM   4515  C  CE1   . HIS B 1 85  ? 147.027 159.142 93.474  1.00 14163. ? 85  HIS B CE1   1 
ATOM   4516  N  NE2   . HIS B 1 85  ? 146.756 159.070 94.764  1.00 14162. ? 85  HIS B NE2   1 
ATOM   4517  N  N     . GLN B 1 86  ? 144.644 155.200 91.374  1.00 14172. ? 86  GLN B N     1 
ATOM   4518  C  CA    . GLN B 1 86  ? 143.852 155.743 90.276  1.00 14185. ? 86  GLN B CA    1 
ATOM   4519  C  C     . GLN B 1 86  ? 142.368 155.479 90.487  1.00 14180. ? 86  GLN B C     1 
ATOM   4520  O  O     . GLN B 1 86  ? 141.527 156.330 90.178  1.00 14215. ? 86  GLN B O     1 
ATOM   4521  C  CB    . GLN B 1 86  ? 144.320 155.154 88.947  1.00 14200. ? 86  GLN B CB    1 
ATOM   4522  C  CG    . GLN B 1 86  ? 145.594 155.781 88.419  1.00 14213. ? 86  GLN B CG    1 
ATOM   4523  C  CD    . GLN B 1 86  ? 145.492 157.287 88.309  1.00 14218. ? 86  GLN B CD    1 
ATOM   4524  O  OE1   . GLN B 1 86  ? 144.487 157.820 87.838  1.00 14225. ? 86  GLN B OE1   1 
ATOM   4525  N  NE2   . GLN B 1 86  ? 146.533 157.984 88.748  1.00 14216. ? 86  GLN B NE2   1 
ATOM   4526  N  N     . LEU B 1 87  ? 142.026 154.296 91.002  1.00 13362. ? 87  LEU B N     1 
ATOM   4527  C  CA    . LEU B 1 87  ? 140.634 154.015 91.337  1.00 13352. ? 87  LEU B CA    1 
ATOM   4528  C  C     . LEU B 1 87  ? 140.123 154.973 92.405  1.00 13394. ? 87  LEU B C     1 
ATOM   4529  O  O     . LEU B 1 87  ? 138.986 155.452 92.329  1.00 13426. ? 87  LEU B O     1 
ATOM   4530  C  CB    . LEU B 1 87  ? 140.484 152.570 91.807  1.00 13321. ? 87  LEU B CB    1 
ATOM   4531  C  CG    . LEU B 1 87  ? 140.431 151.486 90.733  1.00 13317. ? 87  LEU B CG    1 
ATOM   4532  C  CD1   . LEU B 1 87  ? 140.031 150.160 91.349  1.00 13308. ? 87  LEU B CD1   1 
ATOM   4533  C  CD2   . LEU B 1 87  ? 139.470 151.876 89.626  1.00 13350. ? 87  LEU B CD2   1 
ATOM   4534  N  N     . LYS B 1 88  ? 140.948 155.257 93.415  1.00 13838. ? 88  LYS B N     1 
ATOM   4535  C  CA    . LYS B 1 88  ? 140.539 156.173 94.475  1.00 13850. ? 88  LYS B CA    1 
ATOM   4536  C  C     . LYS B 1 88  ? 140.278 157.571 93.929  1.00 13880. ? 88  LYS B C     1 
ATOM   4537  O  O     . LYS B 1 88  ? 139.280 158.210 94.279  1.00 13889. ? 88  LYS B O     1 
ATOM   4538  C  CB    . LYS B 1 88  ? 141.603 156.230 95.571  1.00 13838. ? 88  LYS B CB    1 
ATOM   4539  C  CG    . LYS B 1 88  ? 141.798 154.944 96.345  1.00 13832. ? 88  LYS B CG    1 
ATOM   4540  C  CD    . LYS B 1 88  ? 142.828 155.143 97.443  1.00 13841. ? 88  LYS B CD    1 
ATOM   4541  C  CE    . LYS B 1 88  ? 143.153 153.842 98.149  1.00 13825. ? 88  LYS B CE    1 
ATOM   4542  N  NZ    . LYS B 1 88  ? 144.158 154.037 99.228  1.00 13825. ? 88  LYS B NZ    1 
ATOM   4543  N  N     . VAL B 1 89  ? 141.169 158.066 93.066  1.00 14449. ? 89  VAL B N     1 
ATOM   4544  C  CA    . VAL B 1 89  ? 141.033 159.443 92.598  1.00 14475. ? 89  VAL B CA    1 
ATOM   4545  C  C     . VAL B 1 89  ? 139.928 159.568 91.558  1.00 14490. ? 89  VAL B C     1 
ATOM   4546  O  O     . VAL B 1 89  ? 139.501 160.681 91.229  1.00 14501. ? 89  VAL B O     1 
ATOM   4547  C  CB    . VAL B 1 89  ? 142.376 159.968 92.053  1.00 14486. ? 89  VAL B CB    1 
ATOM   4548  C  CG1   . VAL B 1 89  ? 143.467 159.814 93.099  1.00 14480. ? 89  VAL B CG1   1 
ATOM   4549  C  CG2   . VAL B 1 89  ? 142.746 159.256 90.767  1.00 14494. ? 89  VAL B CG2   1 
ATOM   4550  N  N     . ASN B 1 90  ? 139.449 158.448 91.022  1.00 14957. ? 90  ASN B N     1 
ATOM   4551  C  CA    . ASN B 1 90  ? 138.397 158.480 90.013  1.00 14990. ? 90  ASN B CA    1 
ATOM   4552  C  C     . ASN B 1 90  ? 136.999 158.320 90.595  1.00 15005. ? 90  ASN B C     1 
ATOM   4553  O  O     . ASN B 1 90  ? 136.038 158.225 89.826  1.00 15029. ? 90  ASN B O     1 
ATOM   4554  C  CB    . ASN B 1 90  ? 138.639 157.396 88.961  1.00 14998. ? 90  ASN B CB    1 
ATOM   4555  C  CG    . ASN B 1 90  ? 139.812 157.714 88.059  1.00 15006. ? 90  ASN B CG    1 
ATOM   4556  O  OD1   . ASN B 1 90  ? 140.410 158.785 88.156  1.00 15011. ? 90  ASN B OD1   1 
ATOM   4557  N  ND2   . ASN B 1 90  ? 140.149 156.784 87.174  1.00 15008. ? 90  ASN B ND2   1 
ATOM   4558  N  N     . GLY B 1 91  ? 136.858 158.285 91.916  1.00 15097. ? 91  GLY B N     1 
ATOM   4559  C  CA    . GLY B 1 91  ? 135.548 158.119 92.514  1.00 15113. ? 91  GLY B CA    1 
ATOM   4560  C  C     . GLY B 1 91  ? 135.001 156.713 92.441  1.00 15118. ? 91  GLY B C     1 
ATOM   4561  O  O     . GLY B 1 91  ? 133.780 156.529 92.437  1.00 15131. ? 91  GLY B O     1 
ATOM   4562  N  N     . GLU B 1 92  ? 135.874 155.711 92.384  1.00 15167. ? 92  GLU B N     1 
ATOM   4563  C  CA    . GLU B 1 92  ? 135.460 154.315 92.332  1.00 15169. ? 92  GLU B CA    1 
ATOM   4564  C  C     . GLU B 1 92  ? 136.017 153.573 93.537  1.00 15150. ? 92  GLU B C     1 
ATOM   4565  O  O     . GLU B 1 92  ? 136.637 152.516 93.384  1.00 15132. ? 92  GLU B O     1 
ATOM   4566  C  CB    . GLU B 1 92  ? 135.927 153.654 91.036  1.00 15162. ? 92  GLU B CB    1 
ATOM   4567  C  CG    . GLU B 1 92  ? 136.029 154.598 89.854  1.00 15168. ? 92  GLU B CG    1 
ATOM   4568  C  CD    . GLU B 1 92  ? 136.373 153.877 88.568  1.00 15171. ? 92  GLU B CD    1 
ATOM   4569  O  OE1   . GLU B 1 92  ? 136.370 152.629 88.569  1.00 15165. ? 92  GLU B OE1   1 
ATOM   4570  O  OE2   . GLU B 1 92  ? 136.652 154.557 87.558  1.00 15182. ? 92  GLU B OE2   1 
ATOM   4571  N  N     . ASP B 1 93  ? 135.809 154.136 94.733  1.00 14678. ? 93  ASP B N     1 
ATOM   4572  C  CA    . ASP B 1 93  ? 136.416 153.723 95.995  1.00 14644. ? 93  ASP B CA    1 
ATOM   4573  C  C     . ASP B 1 93  ? 136.510 152.208 96.119  1.00 14588. ? 93  ASP B C     1 
ATOM   4574  O  O     . ASP B 1 93  ? 135.485 151.515 96.123  1.00 14611. ? 93  ASP B O     1 
ATOM   4575  C  CB    . ASP B 1 93  ? 135.608 154.287 97.165  1.00 14661. ? 93  ASP B CB    1 
ATOM   4576  C  CG    . ASP B 1 93  ? 136.322 154.144 98.496  1.00 14637. ? 93  ASP B CG    1 
ATOM   4577  O  OD1   . ASP B 1 93  ? 137.496 153.722 98.510  1.00 14613. ? 93  ASP B OD1   1 
ATOM   4578  O  OD2   . ASP B 1 93  ? 135.701 154.449 99.535  1.00 14638. ? 93  ASP B OD2   1 
ATOM   4579  N  N     . PRO B 1 94  ? 137.720 151.660 96.221  1.00 12916. ? 94  PRO B N     1 
ATOM   4580  C  CA    . PRO B 1 94  ? 137.889 150.210 96.378  1.00 12884. ? 94  PRO B CA    1 
ATOM   4581  C  C     . PRO B 1 94  ? 137.758 149.703 97.807  1.00 12869. ? 94  PRO B C     1 
ATOM   4582  O  O     . PRO B 1 94  ? 138.048 148.529 98.049  1.00 12860. ? 94  PRO B O     1 
ATOM   4583  C  CB    . PRO B 1 94  ? 139.318 149.997 95.867  1.00 12872. ? 94  PRO B CB    1 
ATOM   4584  C  CG    . PRO B 1 94  ? 140.018 151.246 96.252  1.00 12886. ? 94  PRO B CG    1 
ATOM   4585  C  CD    . PRO B 1 94  ? 139.013 152.354 96.090  1.00 12917. ? 94  PRO B CD    1 
ATOM   4586  N  N     . TYR B 1 95  ? 137.339 150.546 98.746  1.00 12787. ? 95  TYR B N     1 
ATOM   4587  C  CA    . TYR B 1 95  ? 137.133 150.145 100.138 1.00 12775. ? 95  TYR B CA    1 
ATOM   4588  C  C     . TYR B 1 95  ? 135.747 150.595 100.574 1.00 12768. ? 95  TYR B C     1 
ATOM   4589  O  O     . TYR B 1 95  ? 135.596 151.558 101.334 1.00 12778. ? 95  TYR B O     1 
ATOM   4590  C  CB    . TYR B 1 95  ? 138.221 150.730 101.040 1.00 12765. ? 95  TYR B CB    1 
ATOM   4591  C  CG    . TYR B 1 95  ? 139.622 150.354 100.618 1.00 12748. ? 95  TYR B CG    1 
ATOM   4592  C  CD1   . TYR B 1 95  ? 140.162 149.125 100.962 1.00 12748. ? 95  TYR B CD1   1 
ATOM   4593  C  CD2   . TYR B 1 95  ? 140.401 151.225 99.874  1.00 12753. ? 95  TYR B CD2   1 
ATOM   4594  C  CE1   . TYR B 1 95  ? 141.438 148.773 100.578 1.00 12744. ? 95  TYR B CE1   1 
ATOM   4595  C  CE2   . TYR B 1 95  ? 141.679 150.882 99.486  1.00 12752. ? 95  TYR B CE2   1 
ATOM   4596  C  CZ    . TYR B 1 95  ? 142.191 149.655 99.840  1.00 12746. ? 95  TYR B CZ    1 
ATOM   4597  O  OH    . TYR B 1 95  ? 143.464 149.308 99.456  1.00 12746. ? 95  TYR B OH    1 
ATOM   4598  N  N     . PRO B 1 96  ? 134.702 149.920 100.095 1.00 12743. ? 96  PRO B N     1 
ATOM   4599  C  CA    . PRO B 1 96  ? 133.345 150.289 100.504 1.00 12734. ? 96  PRO B CA    1 
ATOM   4600  C  C     . PRO B 1 96  ? 133.137 150.046 101.989 1.00 12742. ? 96  PRO B C     1 
ATOM   4601  O  O     . PRO B 1 96  ? 133.729 149.145 102.585 1.00 12754. ? 96  PRO B O     1 
ATOM   4602  C  CB    . PRO B 1 96  ? 132.456 149.375 99.654  1.00 12731. ? 96  PRO B CB    1 
ATOM   4603  C  CG    . PRO B 1 96  ? 133.321 148.221 99.319  1.00 12733. ? 96  PRO B CG    1 
ATOM   4604  C  CD    . PRO B 1 96  ? 134.706 148.767 99.181  1.00 12746. ? 96  PRO B CD    1 
ATOM   4605  N  N     . HIS B 1 97  ? 132.282 150.874 102.589 1.00 12742. ? 97  HIS B N     1 
ATOM   4606  C  CA    . HIS B 1 97  ? 132.078 150.796 104.029 1.00 12741. ? 97  HIS B CA    1 
ATOM   4607  C  C     . HIS B 1 97  ? 131.263 149.573 104.424 1.00 12737. ? 97  HIS B C     1 
ATOM   4608  O  O     . HIS B 1 97  ? 131.489 149.004 105.498 1.00 12737. ? 97  HIS B O     1 
ATOM   4609  C  CB    . HIS B 1 97  ? 131.403 152.070 104.527 1.00 12745. ? 97  HIS B CB    1 
ATOM   4610  C  CG    . HIS B 1 97  ? 132.335 153.232 104.655 1.00 12736. ? 97  HIS B CG    1 
ATOM   4611  N  ND1   . HIS B 1 97  ? 132.633 154.065 103.599 1.00 12727. ? 97  HIS B ND1   1 
ATOM   4612  C  CD2   . HIS B 1 97  ? 133.038 153.699 105.713 1.00 12746. ? 97  HIS B CD2   1 
ATOM   4613  C  CE1   . HIS B 1 97  ? 133.479 154.996 104.001 1.00 12739. ? 97  HIS B CE1   1 
ATOM   4614  N  NE2   . HIS B 1 97  ? 133.741 154.796 105.280 1.00 12747. ? 97  HIS B NE2   1 
ATOM   4615  N  N     . LYS B 1 98  ? 130.323 149.151 103.583 1.00 12740. ? 98  LYS B N     1 
ATOM   4616  C  CA    . LYS B 1 98  ? 129.424 148.067 103.945 1.00 12739. ? 98  LYS B CA    1 
ATOM   4617  C  C     . LYS B 1 98  ? 128.991 147.311 102.698 1.00 12739. ? 98  LYS B C     1 
ATOM   4618  O  O     . LYS B 1 98  ? 128.687 147.909 101.664 1.00 12754. ? 98  LYS B O     1 
ATOM   4619  C  CB    . LYS B 1 98  ? 128.197 148.597 104.696 1.00 12741. ? 98  LYS B CB    1 
ATOM   4620  C  CG    . LYS B 1 98  ? 127.079 147.586 104.870 1.00 12741. ? 98  LYS B CG    1 
ATOM   4621  C  CD    . LYS B 1 98  ? 127.393 146.599 105.978 1.00 12752. ? 98  LYS B CD    1 
ATOM   4622  C  CE    . LYS B 1 98  ? 126.260 145.611 106.168 1.00 12744. ? 98  LYS B CE    1 
ATOM   4623  N  NZ    . LYS B 1 98  ? 126.606 144.567 107.166 1.00 12724. ? 98  LYS B NZ    1 
ATOM   4624  N  N     . PHE B 1 99  ? 128.973 145.985 102.811 1.00 12722. ? 99  PHE B N     1 
ATOM   4625  C  CA    . PHE B 1 99  ? 128.401 145.111 101.795 1.00 12726. ? 99  PHE B CA    1 
ATOM   4626  C  C     . PHE B 1 99  ? 127.527 144.094 102.507 1.00 12749. ? 99  PHE B C     1 
ATOM   4627  O  O     . PHE B 1 99  ? 128.029 143.302 103.310 1.00 12771. ? 99  PHE B O     1 
ATOM   4628  C  CB    . PHE B 1 99  ? 129.488 144.413 100.977 1.00 12731. ? 99  PHE B CB    1 
ATOM   4629  C  CG    . PHE B 1 99  ? 128.956 143.472 99.934  1.00 12735. ? 99  PHE B CG    1 
ATOM   4630  C  CD1   . PHE B 1 99  ? 128.529 143.946 98.708  1.00 12740. ? 99  PHE B CD1   1 
ATOM   4631  C  CD2   . PHE B 1 99  ? 128.888 142.114 100.177 1.00 12750. ? 99  PHE B CD2   1 
ATOM   4632  C  CE1   . PHE B 1 99  ? 128.042 143.086 97.750  1.00 12743. ? 99  PHE B CE1   1 
ATOM   4633  C  CE2   . PHE B 1 99  ? 128.400 141.251 99.222  1.00 12751. ? 99  PHE B CE2   1 
ATOM   4634  C  CZ    . PHE B 1 99  ? 127.978 141.737 98.008  1.00 12749. ? 99  PHE B CZ    1 
ATOM   4635  N  N     . HIS B 1 100 ? 126.230 144.113 102.220 1.00 12749. ? 100 HIS B N     1 
ATOM   4636  C  CA    . HIS B 1 100 ? 125.275 143.275 102.940 1.00 12741. ? 100 HIS B CA    1 
ATOM   4637  C  C     . HIS B 1 100 ? 125.333 141.858 102.390 1.00 12738. ? 100 HIS B C     1 
ATOM   4638  O  O     . HIS B 1 100 ? 124.743 141.554 101.353 1.00 12751. ? 100 HIS B O     1 
ATOM   4639  C  CB    . HIS B 1 100 ? 123.868 143.848 102.832 1.00 12738. ? 100 HIS B CB    1 
ATOM   4640  C  CG    . HIS B 1 100 ? 122.908 143.267 103.822 1.00 12743. ? 100 HIS B CG    1 
ATOM   4641  N  ND1   . HIS B 1 100 ? 122.053 142.233 103.510 1.00 12745. ? 100 HIS B ND1   1 
ATOM   4642  C  CD2   . HIS B 1 100 ? 122.678 143.567 105.122 1.00 12750. ? 100 HIS B CD2   1 
ATOM   4643  C  CE1   . HIS B 1 100 ? 121.333 141.924 104.573 1.00 12736. ? 100 HIS B CE1   1 
ATOM   4644  N  NE2   . HIS B 1 100 ? 121.692 142.719 105.565 1.00 12699. ? 100 HIS B NE2   1 
ATOM   4645  N  N     . VAL B 1 101 ? 126.047 140.979 103.093 1.00 12728. ? 101 VAL B N     1 
ATOM   4646  C  CA    . VAL B 1 101 ? 126.079 139.572 102.721 1.00 12723. ? 101 VAL B CA    1 
ATOM   4647  C  C     . VAL B 1 101 ? 124.815 138.894 103.227 1.00 12695. ? 101 VAL B C     1 
ATOM   4648  O  O     . VAL B 1 101 ? 124.456 139.015 104.406 1.00 12652. ? 101 VAL B O     1 
ATOM   4649  C  CB    . VAL B 1 101 ? 127.338 138.896 103.281 1.00 12663. ? 101 VAL B CB    1 
ATOM   4650  C  CG1   . VAL B 1 101 ? 127.329 137.416 102.960 1.00 12628. ? 101 VAL B CG1   1 
ATOM   4651  C  CG2   . VAL B 1 101 ? 128.581 139.556 102.721 1.00 12714. ? 101 VAL B CG2   1 
ATOM   4652  N  N     . ASP B 1 102 ? 124.128 138.179 102.338 1.00 12722. ? 102 ASP B N     1 
ATOM   4653  C  CA    . ASP B 1 102 ? 122.871 137.534 102.696 1.00 12714. ? 102 ASP B CA    1 
ATOM   4654  C  C     . ASP B 1 102 ? 123.064 136.114 103.208 1.00 12675. ? 102 ASP B C     1 
ATOM   4655  O  O     . ASP B 1 102 ? 122.464 135.736 104.219 1.00 12671. ? 102 ASP B O     1 
ATOM   4656  C  CB    . ASP B 1 102 ? 121.924 137.519 101.494 1.00 12750. ? 102 ASP B CB    1 
ATOM   4657  C  CG    . ASP B 1 102 ? 121.454 138.905 101.106 1.00 12754. ? 102 ASP B CG    1 
ATOM   4658  O  OD1   . ASP B 1 102 ? 121.819 139.874 101.803 1.00 12754. ? 102 ASP B OD1   1 
ATOM   4659  O  OD2   . ASP B 1 102 ? 120.720 139.026 100.104 1.00 12758. ? 102 ASP B OD2   1 
ATOM   4660  N  N     . ILE B 1 103 ? 123.887 135.320 102.533 1.00 12707. ? 103 ILE B N     1 
ATOM   4661  C  CA    . ILE B 1 103 ? 124.087 133.922 102.884 1.00 12714. ? 103 ILE B CA    1 
ATOM   4662  C  C     . ILE B 1 103 ? 125.580 133.631 102.912 1.00 12684. ? 103 ILE B C     1 
ATOM   4663  O  O     . ILE B 1 103 ? 126.374 134.285 102.228 1.00 12718. ? 103 ILE B O     1 
ATOM   4664  C  CB    . ILE B 1 103 ? 123.353 132.982 101.900 1.00 12741. ? 103 ILE B CB    1 
ATOM   4665  C  CG1   . ILE B 1 103 ? 123.109 131.614 102.533 1.00 12754. ? 103 ILE B CG1   1 
ATOM   4666  C  CG2   . ILE B 1 103 ? 124.124 132.840 100.603 1.00 12753. ? 103 ILE B CG2   1 
ATOM   4667  C  CD1   . ILE B 1 103 ? 122.442 130.632 101.603 1.00 12754. ? 103 ILE B CD1   1 
ATOM   4668  N  N     . SER B 1 104 ? 125.963 132.659 103.730 1.00 12651. ? 104 SER B N     1 
ATOM   4669  C  CA    . SER B 1 104 ? 127.347 132.220 103.803 1.00 12702. ? 104 SER B CA    1 
ATOM   4670  C  C     . SER B 1 104 ? 127.631 131.205 102.705 1.00 12751. ? 104 SER B C     1 
ATOM   4671  O  O     . SER B 1 104 ? 126.716 130.607 102.135 1.00 12763. ? 104 SER B O     1 
ATOM   4672  C  CB    . SER B 1 104 ? 127.653 131.610 105.170 1.00 12676. ? 104 SER B CB    1 
ATOM   4673  O  OG    . SER B 1 104 ? 127.326 130.234 105.195 1.00 12732. ? 104 SER B OG    1 
ATOM   4674  N  N     . LEU B 1 105 ? 128.918 131.020 102.406 1.00 12745. ? 105 LEU B N     1 
ATOM   4675  C  CA    . LEU B 1 105 ? 129.295 130.096 101.342 1.00 12730. ? 105 LEU B CA    1 
ATOM   4676  C  C     . LEU B 1 105 ? 128.926 128.661 101.694 1.00 12744. ? 105 LEU B C     1 
ATOM   4677  O  O     . LEU B 1 105 ? 128.474 127.900 100.831 1.00 12753. ? 105 LEU B O     1 
ATOM   4678  C  CB    . LEU B 1 105 ? 130.789 130.212 101.044 1.00 12729. ? 105 LEU B CB    1 
ATOM   4679  C  CG    . LEU B 1 105 ? 131.212 131.484 100.310 1.00 12732. ? 105 LEU B CG    1 
ATOM   4680  C  CD1   . LEU B 1 105 ? 132.561 131.298 99.653  1.00 12759. ? 105 LEU B CD1   1 
ATOM   4681  C  CD2   . LEU B 1 105 ? 130.173 131.877 99.283  1.00 12743. ? 105 LEU B CD2   1 
ATOM   4682  N  N     . THR B 1 106 ? 129.118 128.269 102.955 1.00 12760. ? 106 THR B N     1 
ATOM   4683  C  CA    . THR B 1 106 ? 128.760 126.918 103.373 1.00 12744. ? 106 THR B CA    1 
ATOM   4684  C  C     . THR B 1 106 ? 127.266 126.672 103.203 1.00 12747. ? 106 THR B C     1 
ATOM   4685  O  O     . THR B 1 106 ? 126.848 125.622 102.698 1.00 12771. ? 106 THR B O     1 
ATOM   4686  C  CB    . THR B 1 106 ? 129.179 126.692 104.824 1.00 12740. ? 106 THR B CB    1 
ATOM   4687  O  OG1   . THR B 1 106 ? 130.533 127.121 105.002 1.00 12753. ? 106 THR B OG1   1 
ATOM   4688  C  CG2   . THR B 1 106 ? 129.069 125.223 105.182 1.00 12746. ? 106 THR B CG2   1 
ATOM   4689  N  N     . ASP B 1 107 ? 126.443 127.638 103.615 1.00 12788. ? 107 ASP B N     1 
ATOM   4690  C  CA    . ASP B 1 107 ? 125.002 127.507 103.436 1.00 12797. ? 107 ASP B CA    1 
ATOM   4691  C  C     . ASP B 1 107 ? 124.628 127.517 101.961 1.00 12793. ? 107 ASP B C     1 
ATOM   4692  O  O     . ASP B 1 107 ? 123.687 126.830 101.551 1.00 12825. ? 107 ASP B O     1 
ATOM   4693  C  CB    . ASP B 1 107 ? 124.275 128.623 104.181 1.00 12794. ? 107 ASP B CB    1 
ATOM   4694  C  CG    . ASP B 1 107 ? 124.612 128.654 105.654 1.00 12758. ? 107 ASP B CG    1 
ATOM   4695  O  OD1   . ASP B 1 107 ? 125.458 127.845 106.088 1.00 12757. ? 107 ASP B OD1   1 
ATOM   4696  O  OD2   . ASP B 1 107 ? 124.029 129.486 106.380 1.00 12702. ? 107 ASP B OD2   1 
ATOM   4697  N  N     . PHE B 1 108 ? 125.344 128.299 101.150 1.00 12736. ? 108 PHE B N     1 
ATOM   4698  C  CA    . PHE B 1 108 ? 125.091 128.298 99.714  1.00 12748. ? 108 PHE B CA    1 
ATOM   4699  C  C     . PHE B 1 108 ? 125.353 126.925 99.112  1.00 12763. ? 108 PHE B C     1 
ATOM   4700  O  O     . PHE B 1 108 ? 124.573 126.442 98.284  1.00 12795. ? 108 PHE B O     1 
ATOM   4701  C  CB    . PHE B 1 108 ? 125.957 129.353 99.027  1.00 12750. ? 108 PHE B CB    1 
ATOM   4702  C  CG    . PHE B 1 108 ? 125.477 129.731 97.657  1.00 12747. ? 108 PHE B CG    1 
ATOM   4703  C  CD1   . PHE B 1 108 ? 125.837 128.983 96.551  1.00 12746. ? 108 PHE B CD1   1 
ATOM   4704  C  CD2   . PHE B 1 108 ? 124.671 130.837 97.474  1.00 12754. ? 108 PHE B CD2   1 
ATOM   4705  C  CE1   . PHE B 1 108 ? 125.397 129.329 95.294  1.00 12751. ? 108 PHE B CE1   1 
ATOM   4706  C  CE2   . PHE B 1 108 ? 124.230 131.186 96.218  1.00 12749. ? 108 PHE B CE2   1 
ATOM   4707  C  CZ    . PHE B 1 108 ? 124.595 130.433 95.128  1.00 12749. ? 108 PHE B CZ    1 
ATOM   4708  N  N     . ILE B 1 109 ? 126.453 126.286 99.510  1.00 12759. ? 109 ILE B N     1 
ATOM   4709  C  CA    . ILE B 1 109 ? 126.754 124.948 99.010  1.00 12763. ? 109 ILE B CA    1 
ATOM   4710  C  C     . ILE B 1 109 ? 125.711 123.950 99.491  1.00 12799. ? 109 ILE B C     1 
ATOM   4711  O  O     . ILE B 1 109 ? 125.230 123.113 98.718  1.00 12807. ? 109 ILE B O     1 
ATOM   4712  C  CB    . ILE B 1 109 ? 128.173 124.523 99.429  1.00 12751. ? 109 ILE B CB    1 
ATOM   4713  C  CG1   . ILE B 1 109 ? 129.211 125.513 98.900  1.00 12745. ? 109 ILE B CG1   1 
ATOM   4714  C  CG2   . ILE B 1 109 ? 128.471 123.116 98.941  1.00 12756. ? 109 ILE B CG2   1 
ATOM   4715  C  CD1   . ILE B 1 109 ? 129.524 125.343 97.435  1.00 12754. ? 109 ILE B CD1   1 
ATOM   4716  N  N     . GLN B 1 110 ? 125.342 124.022 100.770 1.00 13780. ? 110 GLN B N     1 
ATOM   4717  C  CA    . GLN B 1 110 ? 124.423 123.043 101.339 1.00 13809. ? 110 GLN B CA    1 
ATOM   4718  C  C     . GLN B 1 110 ? 123.020 123.160 100.752 1.00 13813. ? 110 GLN B C     1 
ATOM   4719  O  O     . GLN B 1 110 ? 122.371 122.143 100.486 1.00 13838. ? 110 GLN B O     1 
ATOM   4720  C  CB    . GLN B 1 110 ? 124.385 123.199 102.859 1.00 13835. ? 110 GLN B CB    1 
ATOM   4721  C  CG    . GLN B 1 110 ? 123.046 122.893 103.495 1.00 13848. ? 110 GLN B CG    1 
ATOM   4722  C  CD    . GLN B 1 110 ? 122.816 123.694 104.758 1.00 13856. ? 110 GLN B CD    1 
ATOM   4723  O  OE1   . GLN B 1 110 ? 123.634 123.673 105.678 1.00 13859. ? 110 GLN B OE1   1 
ATOM   4724  N  NE2   . GLN B 1 110 ? 121.701 124.414 104.809 1.00 13854. ? 110 GLN B NE2   1 
ATOM   4725  N  N     . LYS B 1 111 ? 122.540 124.384 100.533 1.00 13234. ? 111 LYS B N     1 
ATOM   4726  C  CA    . LYS B 1 111 ? 121.156 124.588 100.128 1.00 13219. ? 111 LYS B CA    1 
ATOM   4727  C  C     . LYS B 1 111 ? 120.914 124.333 98.647  1.00 13215. ? 111 LYS B C     1 
ATOM   4728  O  O     . LYS B 1 111 ? 119.813 123.912 98.281  1.00 13236. ? 111 LYS B O     1 
ATOM   4729  C  CB    . LYS B 1 111 ? 120.715 126.011 100.476 1.00 13211. ? 111 LYS B CB    1 
ATOM   4730  C  CG    . LYS B 1 111 ? 119.213 126.225 100.417 1.00 13216. ? 111 LYS B CG    1 
ATOM   4731  C  CD    . LYS B 1 111 ? 118.847 127.685 100.618 1.00 13215. ? 111 LYS B CD    1 
ATOM   4732  C  CE    . LYS B 1 111 ? 119.581 128.282 101.806 1.00 13209. ? 111 LYS B CE    1 
ATOM   4733  N  NZ    . LYS B 1 111 ? 119.262 127.567 103.071 1.00 13219. ? 111 LYS B NZ    1 
ATOM   4734  N  N     . TYR B 1 112 ? 121.905 124.571 97.789  1.00 13091. ? 112 TYR B N     1 
ATOM   4735  C  CA    . TYR B 1 112 ? 121.696 124.505 96.348  1.00 13100. ? 112 TYR B CA    1 
ATOM   4736  C  C     . TYR B 1 112 ? 122.551 123.422 95.703  1.00 13146. ? 112 TYR B C     1 
ATOM   4737  O  O     . TYR B 1 112 ? 122.910 123.525 94.528  1.00 13136. ? 112 TYR B O     1 
ATOM   4738  C  CB    . TYR B 1 112 ? 121.964 125.861 95.699  1.00 13080. ? 112 TYR B CB    1 
ATOM   4739  C  CG    . TYR B 1 112 ? 121.025 126.942 96.176  1.00 13057. ? 112 TYR B CG    1 
ATOM   4740  C  CD1   . TYR B 1 112 ? 119.724 127.013 95.705  1.00 13072. ? 112 TYR B CD1   1 
ATOM   4741  C  CD2   . TYR B 1 112 ? 121.436 127.884 97.106  1.00 13056. ? 112 TYR B CD2   1 
ATOM   4742  C  CE1   . TYR B 1 112 ? 118.860 127.995 96.142  1.00 13058. ? 112 TYR B CE1   1 
ATOM   4743  C  CE2   . TYR B 1 112 ? 120.579 128.869 97.548  1.00 13059. ? 112 TYR B CE2   1 
ATOM   4744  C  CZ    . TYR B 1 112 ? 119.292 128.919 97.064  1.00 13054. ? 112 TYR B CZ    1 
ATOM   4745  O  OH    . TYR B 1 112 ? 118.433 129.899 97.501  1.00 13063. ? 112 TYR B OH    1 
ATOM   4746  N  N     . SER B 1 113 ? 122.884 122.374 96.456  1.00 14276. ? 113 SER B N     1 
ATOM   4747  C  CA    . SER B 1 113 ? 123.621 121.258 95.877  1.00 14304. ? 113 SER B CA    1 
ATOM   4748  C  C     . SER B 1 113 ? 122.700 120.273 95.172  1.00 14350. ? 113 SER B C     1 
ATOM   4749  O  O     . SER B 1 113 ? 123.180 119.344 94.514  1.00 14352. ? 113 SER B O     1 
ATOM   4750  C  CB    . SER B 1 113 ? 124.425 120.539 96.960  1.00 14316. ? 113 SER B CB    1 
ATOM   4751  O  OG    . SER B 1 113 ? 125.573 121.287 97.318  1.00 14308. ? 113 SER B OG    1 
ATOM   4752  N  N     . HIS B 1 114 ? 121.387 120.454 95.297  1.00 15286. ? 114 HIS B N     1 
ATOM   4753  C  CA    . HIS B 1 114 ? 120.425 119.540 94.694  1.00 15321. ? 114 HIS B CA    1 
ATOM   4754  C  C     . HIS B 1 114 ? 120.145 119.905 93.242  1.00 15335. ? 114 HIS B C     1 
ATOM   4755  O  O     . HIS B 1 114 ? 119.407 119.195 92.552  1.00 15361. ? 114 HIS B O     1 
ATOM   4756  C  CB    . HIS B 1 114 ? 119.122 119.538 95.493  1.00 15339. ? 114 HIS B CB    1 
ATOM   4757  C  CG    . HIS B 1 114 ? 118.398 120.848 95.467  1.00 15336. ? 114 HIS B CG    1 
ATOM   4758  N  ND1   . HIS B 1 114 ? 118.541 121.796 96.456  1.00 15324. ? 114 HIS B ND1   1 
ATOM   4759  C  CD2   . HIS B 1 114 ? 117.527 121.368 94.571  1.00 15348. ? 114 HIS B CD2   1 
ATOM   4760  C  CE1   . HIS B 1 114 ? 117.788 122.844 96.171  1.00 15323. ? 114 HIS B CE1   1 
ATOM   4761  N  NE2   . HIS B 1 114 ? 117.163 122.609 95.032  1.00 15342. ? 114 HIS B NE2   1 
ATOM   4762  N  N     . LEU B 1 115 ? 120.720 121.009 92.775  1.00 15280. ? 115 LEU B N     1 
ATOM   4763  C  CA    . LEU B 1 115 ? 120.445 121.482 91.426  1.00 15302. ? 115 LEU B CA    1 
ATOM   4764  C  C     . LEU B 1 115 ? 120.976 120.506 90.383  1.00 15330. ? 115 LEU B C     1 
ATOM   4765  O  O     . LEU B 1 115 ? 122.019 119.875 90.570  1.00 15318. ? 115 LEU B O     1 
ATOM   4766  C  CB    . LEU B 1 115 ? 121.063 122.861 91.209  1.00 15295. ? 115 LEU B CB    1 
ATOM   4767  C  CG    . LEU B 1 115 ? 120.540 123.982 92.104  1.00 15270. ? 115 LEU B CG    1 
ATOM   4768  C  CD1   . LEU B 1 115 ? 121.062 125.324 91.631  1.00 15236. ? 115 LEU B CD1   1 
ATOM   4769  C  CD2   . LEU B 1 115 ? 119.023 123.973 92.127  1.00 15283. ? 115 LEU B CD2   1 
ATOM   4770  N  N     . GLN B 1 116 ? 120.243 120.384 89.281  1.00 16378. ? 116 GLN B N     1 
ATOM   4771  C  CA    . GLN B 1 116 ? 120.672 119.548 88.177  1.00 16398. ? 116 GLN B CA    1 
ATOM   4772  C  C     . GLN B 1 116 ? 121.829 120.209 87.431  1.00 16393. ? 116 GLN B C     1 
ATOM   4773  O  O     . GLN B 1 116 ? 121.997 121.429 87.482  1.00 16391. ? 116 GLN B O     1 
ATOM   4774  C  CB    . GLN B 1 116 ? 119.504 119.287 87.230  1.00 16415. ? 116 GLN B CB    1 
ATOM   4775  C  CG    . GLN B 1 116 ? 118.463 118.330 87.787  1.00 16423. ? 116 GLN B CG    1 
ATOM   4776  C  CD    . GLN B 1 116 ? 119.085 117.131 88.477  1.00 16423. ? 116 GLN B CD    1 
ATOM   4777  O  OE1   . GLN B 1 116 ? 119.926 116.438 87.904  1.00 16424. ? 116 GLN B OE1   1 
ATOM   4778  N  NE2   . GLN B 1 116 ? 118.674 116.882 89.714  1.00 16423. ? 116 GLN B NE2   1 
ATOM   4779  N  N     . PRO B 1 117 ? 122.643 119.422 86.726  1.00 16360. ? 117 PRO B N     1 
ATOM   4780  C  CA    . PRO B 1 117 ? 123.797 120.005 86.028  1.00 16360. ? 117 PRO B CA    1 
ATOM   4781  C  C     . PRO B 1 117 ? 123.401 120.825 84.812  1.00 16352. ? 117 PRO B C     1 
ATOM   4782  O  O     . PRO B 1 117 ? 123.443 120.329 83.682  1.00 16363. ? 117 PRO B O     1 
ATOM   4783  C  CB    . PRO B 1 117 ? 124.629 118.781 85.624  1.00 16373. ? 117 PRO B CB    1 
ATOM   4784  C  CG    . PRO B 1 117 ? 123.704 117.629 85.686  1.00 16381. ? 117 PRO B CG    1 
ATOM   4785  C  CD    . PRO B 1 117 ? 122.642 117.951 86.683  1.00 16374. ? 117 PRO B CD    1 
ATOM   4786  N  N     . GLY B 1 118 ? 123.011 122.079 85.029  1.00 15741. ? 118 GLY B N     1 
ATOM   4787  C  CA    . GLY B 1 118 ? 122.698 122.963 83.925  1.00 15730. ? 118 GLY B CA    1 
ATOM   4788  C  C     . GLY B 1 118 ? 121.538 123.906 84.169  1.00 15725. ? 118 GLY B C     1 
ATOM   4789  O  O     . GLY B 1 118 ? 121.219 124.732 83.309  1.00 15722. ? 118 GLY B O     1 
ATOM   4790  N  N     . ASP B 1 119 ? 120.900 123.804 85.331  1.00 15918. ? 119 ASP B N     1 
ATOM   4791  C  CA    . ASP B 1 119 ? 119.772 124.671 85.629  1.00 15913. ? 119 ASP B CA    1 
ATOM   4792  C  C     . ASP B 1 119 ? 120.256 126.066 86.015  1.00 15881. ? 119 ASP B C     1 
ATOM   4793  O  O     . ASP B 1 119 ? 121.439 126.298 86.275  1.00 15874. ? 119 ASP B O     1 
ATOM   4794  C  CB    . ASP B 1 119 ? 118.913 124.077 86.742  1.00 15930. ? 119 ASP B CB    1 
ATOM   4795  C  CG    . ASP B 1 119 ? 119.738 123.473 87.854  1.00 15936. ? 119 ASP B CG    1 
ATOM   4796  O  OD1   . ASP B 1 119 ? 120.884 123.925 88.055  1.00 15919. ? 119 ASP B OD1   1 
ATOM   4797  O  OD2   . ASP B 1 119 ? 119.243 122.543 88.525  1.00 15943. ? 119 ASP B OD2   1 
ATOM   4798  N  N     . HIS B 1 120 ? 119.313 127.007 86.051  1.00 14813. ? 120 HIS B N     1 
ATOM   4799  C  CA    . HIS B 1 120 ? 119.629 128.403 86.349  1.00 14787. ? 120 HIS B CA    1 
ATOM   4800  C  C     . HIS B 1 120 ? 118.415 129.008 87.048  1.00 14779. ? 120 HIS B C     1 
ATOM   4801  O  O     . HIS B 1 120 ? 117.446 129.394 86.389  1.00 14782. ? 120 HIS B O     1 
ATOM   4802  C  CB    . HIS B 1 120 ? 119.982 129.162 85.077  1.00 14787. ? 120 HIS B CB    1 
ATOM   4803  C  CG    . HIS B 1 120 ? 120.425 130.571 85.313  1.00 14777. ? 120 HIS B CG    1 
ATOM   4804  N  ND1   . HIS B 1 120 ? 120.733 131.434 84.284  1.00 14781. ? 120 HIS B ND1   1 
ATOM   4805  C  CD2   . HIS B 1 120 ? 120.613 131.269 86.458  1.00 14752. ? 120 HIS B CD2   1 
ATOM   4806  C  CE1   . HIS B 1 120 ? 121.090 132.603 84.784  1.00 14770. ? 120 HIS B CE1   1 
ATOM   4807  N  NE2   . HIS B 1 120 ? 121.026 132.530 86.101  1.00 14752. ? 120 HIS B NE2   1 
ATOM   4808  N  N     . LEU B 1 121 ? 118.477 129.090 88.374  1.00 14577. ? 121 LEU B N     1 
ATOM   4809  C  CA    . LEU B 1 121 ? 117.385 129.648 89.167  1.00 14579. ? 121 LEU B CA    1 
ATOM   4810  C  C     . LEU B 1 121 ? 117.429 131.165 89.052  1.00 14594. ? 121 LEU B C     1 
ATOM   4811  O  O     . LEU B 1 121 ? 118.166 131.833 89.779  1.00 14564. ? 121 LEU B O     1 
ATOM   4812  C  CB    . LEU B 1 121 ? 117.493 129.203 90.620  1.00 14557. ? 121 LEU B CB    1 
ATOM   4813  C  CG    . LEU B 1 121 ? 117.580 127.699 90.864  1.00 14569. ? 121 LEU B CG    1 
ATOM   4814  C  CD1   . LEU B 1 121 ? 117.663 127.410 92.352  1.00 14569. ? 121 LEU B CD1   1 
ATOM   4815  C  CD2   . LEU B 1 121 ? 116.389 126.992 90.242  1.00 14580. ? 121 LEU B CD2   1 
ATOM   4816  N  N     . THR B 1 122 ? 116.630 131.717 88.143  1.00 15322. ? 122 THR B N     1 
ATOM   4817  C  CA    . THR B 1 122 ? 116.616 133.155 87.913  1.00 15329. ? 122 THR B CA    1 
ATOM   4818  C  C     . THR B 1 122 ? 115.711 133.908 88.878  1.00 15337. ? 122 THR B C     1 
ATOM   4819  O  O     . THR B 1 122 ? 115.692 135.142 88.845  1.00 15342. ? 122 THR B O     1 
ATOM   4820  C  CB    . THR B 1 122 ? 116.186 133.456 86.476  1.00 15362. ? 122 THR B CB    1 
ATOM   4821  O  OG1   . THR B 1 122 ? 115.215 132.490 86.055  1.00 15370. ? 122 THR B OG1   1 
ATOM   4822  C  CG2   . THR B 1 122 ? 117.383 133.403 85.541  1.00 15363. ? 122 THR B CG2   1 
ATOM   4823  N  N     . ASP B 1 123 ? 114.963 133.207 89.727  1.00 15313. ? 123 ASP B N     1 
ATOM   4824  C  CA    . ASP B 1 123 ? 114.062 133.850 90.671  1.00 15315. ? 123 ASP B CA    1 
ATOM   4825  C  C     . ASP B 1 123 ? 114.689 134.091 92.037  1.00 15295. ? 123 ASP B C     1 
ATOM   4826  O  O     . ASP B 1 123 ? 114.037 134.686 92.901  1.00 15313. ? 123 ASP B O     1 
ATOM   4827  C  CB    . ASP B 1 123 ? 112.790 133.013 90.841  1.00 15329. ? 123 ASP B CB    1 
ATOM   4828  C  CG    . ASP B 1 123 ? 113.072 131.526 90.865  1.00 15331. ? 123 ASP B CG    1 
ATOM   4829  O  OD1   . ASP B 1 123 ? 114.018 131.090 90.178  1.00 15334. ? 123 ASP B OD1   1 
ATOM   4830  O  OD2   . ASP B 1 123 ? 112.349 130.794 91.573  1.00 15332. ? 123 ASP B OD2   1 
ATOM   4831  N  N     . ILE B 1 124 ? 115.925 133.651 92.256  1.00 14210. ? 124 ILE B N     1 
ATOM   4832  C  CA    . ILE B 1 124 ? 116.610 133.808 93.534  1.00 14157. ? 124 ILE B CA    1 
ATOM   4833  C  C     . ILE B 1 124 ? 117.872 134.626 93.307  1.00 14113. ? 124 ILE B C     1 
ATOM   4834  O  O     . ILE B 1 124 ? 118.680 134.302 92.429  1.00 14121. ? 124 ILE B O     1 
ATOM   4835  C  CB    . ILE B 1 124 ? 116.946 132.448 94.168  1.00 14146. ? 124 ILE B CB    1 
ATOM   4836  C  CG1   . ILE B 1 124 ? 115.672 131.632 94.390  1.00 14173. ? 124 ILE B CG1   1 
ATOM   4837  C  CG2   . ILE B 1 124 ? 117.681 132.646 95.477  1.00 14126. ? 124 ILE B CG2   1 
ATOM   4838  C  CD1   . ILE B 1 124 ? 115.441 130.561 93.350  1.00 14193. ? 124 ILE B CD1   1 
ATOM   4839  N  N     . THR B 1 125 ? 118.042 135.681 94.100  1.00 12805. ? 125 THR B N     1 
ATOM   4840  C  CA    . THR B 1 125 ? 119.196 136.573 93.998  1.00 12768. ? 125 THR B CA    1 
ATOM   4841  C  C     . THR B 1 125 ? 119.838 136.679 95.378  1.00 12748. ? 125 THR B C     1 
ATOM   4842  O  O     . THR B 1 125 ? 119.259 137.269 96.294  1.00 12751. ? 125 THR B O     1 
ATOM   4843  C  CB    . THR B 1 125 ? 118.787 137.944 93.472  1.00 12761. ? 125 THR B CB    1 
ATOM   4844  O  OG1   . THR B 1 125 ? 118.161 137.798 92.192  1.00 12782. ? 125 THR B OG1   1 
ATOM   4845  C  CG2   . THR B 1 125 ? 120.002 138.843 93.335  1.00 12758. ? 125 THR B CG2   1 
ATOM   4846  N  N     . LEU B 1 126 ? 121.030 136.112 95.522  1.00 12742. ? 126 LEU B N     1 
ATOM   4847  C  CA    . LEU B 1 126 ? 121.748 136.095 96.785  1.00 12736. ? 126 LEU B CA    1 
ATOM   4848  C  C     . LEU B 1 126 ? 123.065 136.846 96.661  1.00 12744. ? 126 LEU B C     1 
ATOM   4849  O  O     . LEU B 1 126 ? 123.642 136.967 95.576  1.00 12757. ? 126 LEU B O     1 
ATOM   4850  C  CB    . LEU B 1 126 ? 122.013 134.659 97.246  1.00 12738. ? 126 LEU B CB    1 
ATOM   4851  C  CG    . LEU B 1 126 ? 120.777 133.807 97.517  1.00 12742. ? 126 LEU B CG    1 
ATOM   4852  C  CD1   . LEU B 1 126 ? 120.983 132.402 96.991  1.00 12755. ? 126 LEU B CD1   1 
ATOM   4853  C  CD2   . LEU B 1 126 ? 120.464 133.786 99.001  1.00 12752. ? 126 LEU B CD2   1 
ATOM   4854  N  N     . LYS B 1 127 ? 123.538 137.345 97.800  1.00 12739. ? 127 LYS B N     1 
ATOM   4855  C  CA    . LYS B 1 127 ? 124.786 138.092 97.889  1.00 12741. ? 127 LYS B CA    1 
ATOM   4856  C  C     . LYS B 1 127 ? 125.761 137.317 98.762  1.00 12741. ? 127 LYS B C     1 
ATOM   4857  O  O     . LYS B 1 127 ? 125.447 136.994 99.912  1.00 12748. ? 127 LYS B O     1 
ATOM   4858  C  CB    . LYS B 1 127 ? 124.547 139.489 98.462  1.00 12745. ? 127 LYS B CB    1 
ATOM   4859  C  CG    . LYS B 1 127 ? 123.423 140.246 97.785  1.00 12743. ? 127 LYS B CG    1 
ATOM   4860  C  CD    . LYS B 1 127 ? 123.073 141.515 98.538  1.00 12740. ? 127 LYS B CD    1 
ATOM   4861  C  CE    . LYS B 1 127 ? 124.118 142.590 98.325  1.00 12741. ? 127 LYS B CE    1 
ATOM   4862  N  NZ    . LYS B 1 127 ? 124.122 143.061 96.916  1.00 12741. ? 127 LYS B NZ    1 
ATOM   4863  N  N     . VAL B 1 128 ? 126.937 137.023 98.215  1.00 12745. ? 128 VAL B N     1 
ATOM   4864  C  CA    . VAL B 1 128 ? 128.003 136.344 98.936  1.00 12743. ? 128 VAL B CA    1 
ATOM   4865  C  C     . VAL B 1 128 ? 129.267 137.189 98.822  1.00 12746. ? 128 VAL B C     1 
ATOM   4866  O  O     . VAL B 1 128 ? 129.323 138.160 98.073  1.00 12758. ? 128 VAL B O     1 
ATOM   4867  C  CB    . VAL B 1 128 ? 128.248 134.917 98.413  1.00 12738. ? 128 VAL B CB    1 
ATOM   4868  C  CG1   . VAL B 1 128 ? 127.040 134.043 98.676  1.00 12748. ? 128 VAL B CG1   1 
ATOM   4869  C  CG2   . VAL B 1 128 ? 128.563 134.948 96.933  1.00 12745. ? 128 VAL B CG2   1 
ATOM   4870  N  N     . ALA B 1 129 ? 130.288 136.808 99.584  1.00 12746. ? 129 ALA B N     1 
ATOM   4871  C  CA    . ALA B 1 129 ? 131.549 137.533 99.561  1.00 12745. ? 129 ALA B CA    1 
ATOM   4872  C  C     . ALA B 1 129 ? 132.687 136.565 99.839  1.00 12746. ? 129 ALA B C     1 
ATOM   4873  O  O     . ALA B 1 129 ? 132.503 135.530 100.482 1.00 12750. ? 129 ALA B O     1 
ATOM   4874  C  CB    . ALA B 1 129 ? 131.560 138.676 100.580 1.00 12749. ? 129 ALA B CB    1 
ATOM   4875  N  N     . GLY B 1 130 ? 133.869 136.915 99.351  1.00 12750. ? 130 GLY B N     1 
ATOM   4876  C  CA    . GLY B 1 130 ? 135.021 136.066 99.577  1.00 12745. ? 130 GLY B CA    1 
ATOM   4877  C  C     . GLY B 1 130 ? 136.213 136.516 98.766  1.00 12751. ? 130 GLY B C     1 
ATOM   4878  O  O     . GLY B 1 130 ? 136.156 137.487 98.009  1.00 12768. ? 130 GLY B O     1 
ATOM   4879  N  N     . ARG B 1 131 ? 137.298 135.767 98.929  1.00 12741. ? 131 ARG B N     1 
ATOM   4880  C  CA    . ARG B 1 131 ? 138.571 136.064 98.290  1.00 12734. ? 131 ARG B CA    1 
ATOM   4881  C  C     . ARG B 1 131 ? 138.717 135.261 97.007  1.00 12737. ? 131 ARG B C     1 
ATOM   4882  O  O     . ARG B 1 131 ? 138.506 134.046 96.996  1.00 12752. ? 131 ARG B O     1 
ATOM   4883  C  CB    . ARG B 1 131 ? 139.732 135.749 99.233  1.00 12735. ? 131 ARG B CB    1 
ATOM   4884  C  CG    . ARG B 1 131 ? 141.051 136.372 98.831  1.00 12738. ? 131 ARG B CG    1 
ATOM   4885  C  CD    . ARG B 1 131 ? 142.154 135.970 99.785  1.00 12732. ? 131 ARG B CD    1 
ATOM   4886  N  NE    . ARG B 1 131 ? 142.109 136.745 101.018 1.00 12727. ? 131 ARG B NE    1 
ATOM   4887  C  CZ    . ARG B 1 131 ? 142.691 137.924 101.183 1.00 12736. ? 131 ARG B CZ    1 
ATOM   4888  N  NH1   . ARG B 1 131 ? 143.380 138.496 100.211 1.00 12751. ? 131 ARG B NH1   1 
ATOM   4889  N  NH2   . ARG B 1 131 ? 142.577 138.545 102.353 1.00 12743. ? 131 ARG B NH2   1 
ATOM   4890  N  N     . ILE B 1 132 ? 139.084 135.947 95.926  1.00 12740. ? 132 ILE B N     1 
ATOM   4891  C  CA    . ILE B 1 132 ? 139.295 135.272 94.652  1.00 12738. ? 132 ILE B CA    1 
ATOM   4892  C  C     . ILE B 1 132 ? 140.556 134.427 94.737  1.00 12746. ? 132 ILE B C     1 
ATOM   4893  O  O     . ILE B 1 132 ? 141.615 134.901 95.165  1.00 12768. ? 132 ILE B O     1 
ATOM   4894  C  CB    . ILE B 1 132 ? 139.391 136.290 93.508  1.00 12728. ? 132 ILE B CB    1 
ATOM   4895  C  CG1   . ILE B 1 132 ? 138.211 137.258 93.550  1.00 12739. ? 132 ILE B CG1   1 
ATOM   4896  C  CG2   . ILE B 1 132 ? 139.446 135.577 92.172  1.00 12747. ? 132 ILE B CG2   1 
ATOM   4897  C  CD1   . ILE B 1 132 ? 138.071 138.089 92.301  1.00 12756. ? 132 ILE B CD1   1 
ATOM   4898  N  N     . HIS B 1 133 ? 140.448 133.164 94.328  1.00 12741. ? 133 HIS B N     1 
ATOM   4899  C  CA    . HIS B 1 133 ? 141.585 132.258 94.334  1.00 12742. ? 133 HIS B CA    1 
ATOM   4900  C  C     . HIS B 1 133 ? 142.101 131.923 92.945  1.00 12739. ? 133 HIS B C     1 
ATOM   4901  O  O     . HIS B 1 133 ? 143.235 131.451 92.825  1.00 12790. ? 133 HIS B O     1 
ATOM   4902  C  CB    . HIS B 1 133 ? 141.223 130.955 95.058  1.00 12754. ? 133 HIS B CB    1 
ATOM   4903  C  CG    . HIS B 1 133 ? 142.410 130.184 95.544  1.00 12762. ? 133 HIS B CG    1 
ATOM   4904  N  ND1   . HIS B 1 133 ? 142.966 129.146 94.829  1.00 12762. ? 133 HIS B ND1   1 
ATOM   4905  C  CD2   . HIS B 1 133 ? 143.147 130.300 96.674  1.00 12751. ? 133 HIS B CD2   1 
ATOM   4906  C  CE1   . HIS B 1 133 ? 143.994 128.655 95.498  1.00 12775. ? 133 HIS B CE1   1 
ATOM   4907  N  NE2   . HIS B 1 133 ? 144.125 129.338 96.620  1.00 12768. ? 133 HIS B NE2   1 
ATOM   4908  N  N     . ALA B 1 134 ? 141.308 132.156 91.902  1.00 12741. ? 134 ALA B N     1 
ATOM   4909  C  CA    . ALA B 1 134 ? 141.735 131.889 90.536  1.00 12748. ? 134 ALA B CA    1 
ATOM   4910  C  C     . ALA B 1 134 ? 140.853 132.687 89.593  1.00 12765. ? 134 ALA B C     1 
ATOM   4911  O  O     . ALA B 1 134 ? 139.637 132.753 89.791  1.00 12777. ? 134 ALA B O     1 
ATOM   4912  C  CB    . ALA B 1 134 ? 141.654 130.394 90.211  1.00 12755. ? 134 ALA B CB    1 
ATOM   4913  N  N     . LYS B 1 135 ? 141.462 133.292 88.580  1.00 13211. ? 135 LYS B N     1 
ATOM   4914  C  CA    . LYS B 1 135 ? 140.751 134.076 87.575  1.00 13236. ? 135 LYS B CA    1 
ATOM   4915  C  C     . LYS B 1 135 ? 141.029 133.445 86.214  1.00 13285. ? 135 LYS B C     1 
ATOM   4916  O  O     . LYS B 1 135 ? 142.000 133.791 85.540  1.00 13286. ? 135 LYS B O     1 
ATOM   4917  C  CB    . LYS B 1 135 ? 141.180 135.538 87.613  1.00 13237. ? 135 LYS B CB    1 
ATOM   4918  C  CG    . LYS B 1 135 ? 140.466 136.418 86.602  1.00 13244. ? 135 LYS B CG    1 
ATOM   4919  C  CD    . LYS B 1 135 ? 140.689 137.890 86.895  1.00 13236. ? 135 LYS B CD    1 
ATOM   4920  C  CE    . LYS B 1 135 ? 140.170 138.762 85.766  1.00 13241. ? 135 LYS B CE    1 
ATOM   4921  N  NZ    . LYS B 1 135 ? 141.273 139.454 85.050  1.00 13250. ? 135 LYS B NZ    1 
ATOM   4922  N  N     . ARG B 1 136 ? 140.170 132.515 85.812  1.00 14793. ? 136 ARG B N     1 
ATOM   4923  C  CA    . ARG B 1 136 ? 140.307 131.824 84.540  1.00 14846. ? 136 ARG B CA    1 
ATOM   4924  C  C     . ARG B 1 136 ? 139.493 132.557 83.482  1.00 14869. ? 136 ARG B C     1 
ATOM   4925  O  O     . ARG B 1 136 ? 138.379 133.011 83.755  1.00 14840. ? 136 ARG B O     1 
ATOM   4926  C  CB    . ARG B 1 136 ? 139.849 130.371 84.663  1.00 14854. ? 136 ARG B CB    1 
ATOM   4927  C  CG    . ARG B 1 136 ? 139.867 129.591 83.363  1.00 14876. ? 136 ARG B CG    1 
ATOM   4928  C  CD    . ARG B 1 136 ? 139.999 128.102 83.628  1.00 14878. ? 136 ARG B CD    1 
ATOM   4929  N  NE    . ARG B 1 136 ? 138.832 127.560 84.313  1.00 14874. ? 136 ARG B NE    1 
ATOM   4930  C  CZ    . ARG B 1 136 ? 137.730 127.148 83.703  1.00 14859. ? 136 ARG B CZ    1 
ATOM   4931  N  NH1   . ARG B 1 136 ? 137.606 127.203 82.387  1.00 14856. ? 136 ARG B NH1   1 
ATOM   4932  N  NH2   . ARG B 1 136 ? 136.727 126.666 84.432  1.00 14849. ? 136 ARG B NH2   1 
ATOM   4933  N  N     . ALA B 1 137 ? 140.054 132.683 82.286  1.00 15968. ? 137 ALA B N     1 
ATOM   4934  C  CA    . ALA B 1 137 ? 139.396 133.371 81.188  1.00 15988. ? 137 ALA B CA    1 
ATOM   4935  C  C     . ALA B 1 137 ? 139.044 132.382 80.087  1.00 16019. ? 137 ALA B C     1 
ATOM   4936  O  O     . ALA B 1 137 ? 139.849 131.524 79.717  1.00 16026. ? 137 ALA B O     1 
ATOM   4937  C  CB    . ALA B 1 137 ? 140.281 134.485 80.624  1.00 16013. ? 137 ALA B CB    1 
ATOM   4938  N  N     . SER B 1 138 ? 137.824 132.511 79.565  1.00 16237. ? 138 SER B N     1 
ATOM   4939  C  CA    . SER B 1 138 ? 137.342 131.663 78.483  1.00 16252. ? 138 SER B CA    1 
ATOM   4940  C  C     . SER B 1 138 ? 136.802 132.504 77.334  1.00 16260. ? 138 SER B C     1 
ATOM   4941  O  O     . SER B 1 138 ? 135.849 132.108 76.658  1.00 16261. ? 138 SER B O     1 
ATOM   4942  C  CB    . SER B 1 138 ? 136.276 130.690 78.983  1.00 16235. ? 138 SER B CB    1 
ATOM   4943  O  OG    . SER B 1 138 ? 135.994 129.700 78.010  1.00 16253. ? 138 SER B OG    1 
ATOM   4944  N  N     . GLY B 1 139 ? 137.402 133.665 77.103  1.00 16701. ? 139 GLY B N     1 
ATOM   4945  C  CA    . GLY B 1 139 ? 136.960 134.596 76.090  1.00 16716. ? 139 GLY B CA    1 
ATOM   4946  C  C     . GLY B 1 139 ? 136.659 135.952 76.684  1.00 16718. ? 139 GLY B C     1 
ATOM   4947  O  O     . GLY B 1 139 ? 136.875 136.211 77.867  1.00 16701. ? 139 GLY B O     1 
ATOM   4948  N  N     . GLY B 1 140 ? 136.149 136.834 75.832  1.00 16791. ? 140 GLY B N     1 
ATOM   4949  C  CA    . GLY B 1 140 ? 135.796 138.166 76.269  1.00 16794. ? 140 GLY B CA    1 
ATOM   4950  C  C     . GLY B 1 140 ? 134.444 138.296 76.926  1.00 16775. ? 140 GLY B C     1 
ATOM   4951  O  O     . GLY B 1 140 ? 134.102 139.381 77.406  1.00 16773. ? 140 GLY B O     1 
ATOM   4952  N  N     . LYS B 1 141 ? 133.657 137.219 76.966  1.00 16269. ? 141 LYS B N     1 
ATOM   4953  C  CA    . LYS B 1 141 ? 132.307 137.271 77.511  1.00 16254. ? 141 LYS B CA    1 
ATOM   4954  C  C     . LYS B 1 141 ? 132.059 136.223 78.589  1.00 16210. ? 141 LYS B C     1 
ATOM   4955  O  O     . LYS B 1 141 ? 130.915 136.070 79.032  1.00 16205. ? 141 LYS B O     1 
ATOM   4956  C  CB    . LYS B 1 141 ? 131.271 137.113 76.391  1.00 16272. ? 141 LYS B CB    1 
ATOM   4957  C  CG    . LYS B 1 141 ? 131.578 137.925 75.135  1.00 16281. ? 141 LYS B CG    1 
ATOM   4958  C  CD    . LYS B 1 141 ? 130.367 138.130 74.211  1.00 16277. ? 141 LYS B CD    1 
ATOM   4959  C  CE    . LYS B 1 141 ? 129.381 136.954 74.132  1.00 16275. ? 141 LYS B CE    1 
ATOM   4960  N  NZ    . LYS B 1 141 ? 129.973 135.581 74.156  1.00 16278. ? 141 LYS B NZ    1 
ATOM   4961  N  N     . LEU B 1 142 ? 133.087 135.502 79.026  1.00 14646. ? 142 LEU B N     1 
ATOM   4962  C  CA    . LEU B 1 142 ? 132.918 134.465 80.039  1.00 14584. ? 142 LEU B CA    1 
ATOM   4963  C  C     . LEU B 1 142 ? 134.195 134.369 80.854  1.00 14573. ? 142 LEU B C     1 
ATOM   4964  O  O     . LEU B 1 142 ? 135.257 134.067 80.304  1.00 14610. ? 142 LEU B O     1 
ATOM   4965  C  CB    . LEU B 1 142 ? 132.588 133.119 79.393  1.00 14588. ? 142 LEU B CB    1 
ATOM   4966  C  CG    . LEU B 1 142 ? 132.320 131.944 80.334  1.00 14567. ? 142 LEU B CG    1 
ATOM   4967  C  CD1   . LEU B 1 142 ? 131.477 132.377 81.521  1.00 14556. ? 142 LEU B CD1   1 
ATOM   4968  C  CD2   . LEU B 1 142 ? 131.648 130.807 79.586  1.00 14570. ? 142 LEU B CD2   1 
ATOM   4969  N  N     . ILE B 1 143 ? 134.096 134.626 82.156  1.00 13932. ? 143 ILE B N     1 
ATOM   4970  C  CA    . ILE B 1 143 ? 135.248 134.546 83.048  1.00 13912. ? 143 ILE B CA    1 
ATOM   4971  C  C     . ILE B 1 143 ? 134.852 133.789 84.307  1.00 13884. ? 143 ILE B C     1 
ATOM   4972  O  O     . ILE B 1 143 ? 133.831 134.091 84.930  1.00 13894. ? 143 ILE B O     1 
ATOM   4973  C  CB    . ILE B 1 143 ? 135.798 135.944 83.397  1.00 13905. ? 143 ILE B CB    1 
ATOM   4974  C  CG1   . ILE B 1 143 ? 136.478 136.565 82.176  1.00 13936. ? 143 ILE B CG1   1 
ATOM   4975  C  CG2   . ILE B 1 143 ? 136.765 135.862 84.565  1.00 13895. ? 143 ILE B CG2   1 
ATOM   4976  C  CD1   . ILE B 1 143 ? 137.531 137.599 82.511  1.00 13928. ? 143 ILE B CD1   1 
ATOM   4977  N  N     . PHE B 1 144 ? 135.665 132.810 84.690  1.00 13425. ? 144 PHE B N     1 
ATOM   4978  C  CA    . PHE B 1 144 ? 135.420 132.013 85.883  1.00 13396. ? 144 PHE B CA    1 
ATOM   4979  C  C     . PHE B 1 144 ? 136.274 132.525 87.035  1.00 13382. ? 144 PHE B C     1 
ATOM   4980  O  O     . PHE B 1 144 ? 137.471 132.779 86.865  1.00 13408. ? 144 PHE B O     1 
ATOM   4981  C  CB    . PHE B 1 144 ? 135.721 130.538 85.622  1.00 13407. ? 144 PHE B CB    1 
ATOM   4982  C  CG    . PHE B 1 144 ? 134.836 129.915 84.586  1.00 13389. ? 144 PHE B CG    1 
ATOM   4983  C  CD1   . PHE B 1 144 ? 133.597 129.410 84.930  1.00 13389. ? 144 PHE B CD1   1 
ATOM   4984  C  CD2   . PHE B 1 144 ? 135.244 129.834 83.268  1.00 13413. ? 144 PHE B CD2   1 
ATOM   4985  C  CE1   . PHE B 1 144 ? 132.781 128.836 83.979  1.00 13399. ? 144 PHE B CE1   1 
ATOM   4986  C  CE2   . PHE B 1 144 ? 134.433 129.261 82.313  1.00 13417. ? 144 PHE B CE2   1 
ATOM   4987  C  CZ    . PHE B 1 144 ? 133.200 128.761 82.669  1.00 13413. ? 144 PHE B CZ    1 
ATOM   4988  N  N     . TYR B 1 145 ? 135.653 132.680 88.198  1.00 12772. ? 145 TYR B N     1 
ATOM   4989  C  CA    . TYR B 1 145 ? 136.338 133.046 89.425  1.00 12745. ? 145 TYR B CA    1 
ATOM   4990  C  C     . TYR B 1 145 ? 136.153 131.936 90.447  1.00 12754. ? 145 TYR B C     1 
ATOM   4991  O  O     . TYR B 1 145 ? 135.108 131.282 90.492  1.00 12771. ? 145 TYR B O     1 
ATOM   4992  C  CB    . TYR B 1 145 ? 135.799 134.358 90.001  1.00 12744. ? 145 TYR B CB    1 
ATOM   4993  C  CG    . TYR B 1 145 ? 136.121 135.583 89.183  1.00 12743. ? 145 TYR B CG    1 
ATOM   4994  C  CD1   . TYR B 1 145 ? 137.348 136.217 89.301  1.00 12751. ? 145 TYR B CD1   1 
ATOM   4995  C  CD2   . TYR B 1 145 ? 135.193 136.113 88.302  1.00 12761. ? 145 TYR B CD2   1 
ATOM   4996  C  CE1   . TYR B 1 145 ? 137.642 137.340 88.560  1.00 12750. ? 145 TYR B CE1   1 
ATOM   4997  C  CE2   . TYR B 1 145 ? 135.478 137.235 87.557  1.00 12763. ? 145 TYR B CE2   1 
ATOM   4998  C  CZ    . TYR B 1 145 ? 136.704 137.844 87.689  1.00 12754. ? 145 TYR B CZ    1 
ATOM   4999  O  OH    . TYR B 1 145 ? 136.991 138.964 86.947  1.00 12795. ? 145 TYR B OH    1 
ATOM   5000  N  N     . ASP B 1 146 ? 137.169 131.732 91.275  1.00 12939. ? 146 ASP B N     1 
ATOM   5001  C  CA    . ASP B 1 146 ? 137.137 130.720 92.326  1.00 12933. ? 146 ASP B CA    1 
ATOM   5002  C  C     . ASP B 1 146 ? 137.082 131.438 93.669  1.00 12923. ? 146 ASP B C     1 
ATOM   5003  O  O     . ASP B 1 146 ? 138.114 131.843 94.210  1.00 12943. ? 146 ASP B O     1 
ATOM   5004  C  CB    . ASP B 1 146 ? 138.346 129.798 92.232  1.00 12943. ? 146 ASP B CB    1 
ATOM   5005  C  CG    . ASP B 1 146 ? 138.114 128.464 92.909  1.00 12945. ? 146 ASP B CG    1 
ATOM   5006  O  OD1   . ASP B 1 146 ? 137.252 127.696 92.432  1.00 12951. ? 146 ASP B OD1   1 
ATOM   5007  O  OD2   . ASP B 1 146 ? 138.792 128.183 93.919  1.00 12954. ? 146 ASP B OD2   1 
ATOM   5008  N  N     . LEU B 1 147 ? 135.875 131.596 94.201  1.00 12733. ? 147 LEU B N     1 
ATOM   5009  C  CA    . LEU B 1 147 ? 135.683 132.241 95.489  1.00 12732. ? 147 LEU B CA    1 
ATOM   5010  C  C     . LEU B 1 147 ? 135.945 131.245 96.612  1.00 12743. ? 147 LEU B C     1 
ATOM   5011  O  O     . LEU B 1 147 ? 135.513 130.089 96.543  1.00 12757. ? 147 LEU B O     1 
ATOM   5012  C  CB    . LEU B 1 147 ? 134.263 132.793 95.588  1.00 12732. ? 147 LEU B CB    1 
ATOM   5013  C  CG    . LEU B 1 147 ? 134.071 134.093 96.363  1.00 12738. ? 147 LEU B CG    1 
ATOM   5014  C  CD1   . LEU B 1 147 ? 134.820 135.219 95.683  1.00 12755. ? 147 LEU B CD1   1 
ATOM   5015  C  CD2   . LEU B 1 147 ? 132.597 134.422 96.474  1.00 12743. ? 147 LEU B CD2   1 
ATOM   5016  N  N     . ARG B 1 148 ? 136.656 131.691 97.643  1.00 12737. ? 148 ARG B N     1 
ATOM   5017  C  CA    . ARG B 1 148 ? 136.963 130.871 98.806  1.00 12728. ? 148 ARG B CA    1 
ATOM   5018  C  C     . ARG B 1 148 ? 136.538 131.610 100.064 1.00 12735. ? 148 ARG B C     1 
ATOM   5019  O  O     . ARG B 1 148 ? 136.965 132.744 100.297 1.00 12738. ? 148 ARG B O     1 
ATOM   5020  C  CB    . ARG B 1 148 ? 138.452 130.534 98.862  1.00 12742. ? 148 ARG B CB    1 
ATOM   5021  C  CG    . ARG B 1 148 ? 138.841 129.304 98.064  1.00 12747. ? 148 ARG B CG    1 
ATOM   5022  C  CD    . ARG B 1 148 ? 140.320 129.013 98.220  1.00 12744. ? 148 ARG B CD    1 
ATOM   5023  N  NE    . ARG B 1 148 ? 140.660 127.625 97.931  1.00 12742. ? 148 ARG B NE    1 
ATOM   5024  C  CZ    . ARG B 1 148 ? 140.693 127.093 96.717  1.00 12751. ? 148 ARG B CZ    1 
ATOM   5025  N  NH1   . ARG B 1 148 ? 140.373 127.796 95.643  1.00 12756. ? 148 ARG B NH1   1 
ATOM   5026  N  NH2   . ARG B 1 148 ? 141.062 125.823 96.576  1.00 12760. ? 148 ARG B NH2   1 
ATOM   5027  N  N     . GLY B 1 149 ? 135.698 130.967 100.868 1.00 12977. ? 149 GLY B N     1 
ATOM   5028  C  CA    . GLY B 1 149 ? 135.166 131.587 102.064 1.00 13000. ? 149 GLY B CA    1 
ATOM   5029  C  C     . GLY B 1 149 ? 135.607 130.938 103.357 1.00 13013. ? 149 GLY B C     1 
ATOM   5030  O  O     . GLY B 1 149 ? 136.718 131.174 103.841 1.00 13007. ? 149 GLY B O     1 
ATOM   5031  N  N     . GLU B 1 150 ? 134.730 130.110 103.927 1.00 13610. ? 150 GLU B N     1 
ATOM   5032  C  CA    . GLU B 1 150 ? 134.944 129.493 105.229 1.00 13610. ? 150 GLU B CA    1 
ATOM   5033  C  C     . GLU B 1 150 ? 135.631 128.139 105.130 1.00 13604. ? 150 GLU B C     1 
ATOM   5034  O  O     . GLU B 1 150 ? 135.384 127.259 105.964 1.00 13618. ? 150 GLU B O     1 
ATOM   5035  C  CB    . GLU B 1 150 ? 133.611 129.353 105.963 1.00 13620. ? 150 GLU B CB    1 
ATOM   5036  C  CG    . GLU B 1 150 ? 133.209 130.575 106.764 1.00 13618. ? 150 GLU B CG    1 
ATOM   5037  C  CD    . GLU B 1 150 ? 132.088 131.353 106.108 1.00 13622. ? 150 GLU B CD    1 
ATOM   5038  O  OE1   . GLU B 1 150 ? 131.997 131.333 104.863 1.00 13631. ? 150 GLU B OE1   1 
ATOM   5039  O  OE2   . GLU B 1 150 ? 131.295 131.983 106.838 1.00 13529. ? 150 GLU B OE2   1 
ATOM   5040  N  N     . GLY B 1 151 ? 136.481 127.947 104.129 1.00 12781. ? 151 GLY B N     1 
ATOM   5041  C  CA    . GLY B 1 151 ? 137.078 126.658 103.869 1.00 12753. ? 151 GLY B CA    1 
ATOM   5042  C  C     . GLY B 1 151 ? 136.434 125.882 102.747 1.00 12744. ? 151 GLY B C     1 
ATOM   5043  O  O     . GLY B 1 151 ? 136.792 124.718 102.538 1.00 12750. ? 151 GLY B O     1 
ATOM   5044  N  N     . VAL B 1 152 ? 135.494 126.486 102.023 1.00 12736. ? 152 VAL B N     1 
ATOM   5045  C  CA    . VAL B 1 152 ? 134.816 125.826 100.916 1.00 12735. ? 152 VAL B CA    1 
ATOM   5046  C  C     . VAL B 1 152 ? 135.173 126.542 99.622  1.00 12736. ? 152 VAL B C     1 
ATOM   5047  O  O     . VAL B 1 152 ? 135.860 127.568 99.635  1.00 12740. ? 152 VAL B O     1 
ATOM   5048  C  CB    . VAL B 1 152 ? 133.294 125.801 101.133 1.00 12744. ? 152 VAL B CB    1 
ATOM   5049  C  CG1   . VAL B 1 152 ? 132.917 124.685 102.088 1.00 12749. ? 152 VAL B CG1   1 
ATOM   5050  C  CG2   . VAL B 1 152 ? 132.817 127.140 101.660 1.00 12765. ? 152 VAL B CG2   1 
ATOM   5051  N  N     . LYS B 1 153 ? 134.711 126.005 98.498  1.00 12734. ? 153 LYS B N     1 
ATOM   5052  C  CA    . LYS B 1 153 ? 134.980 126.563 97.182  1.00 12728. ? 153 LYS B CA    1 
ATOM   5053  C  C     . LYS B 1 153 ? 133.663 126.865 96.488  1.00 12744. ? 153 LYS B C     1 
ATOM   5054  O  O     . LYS B 1 153 ? 132.733 126.054 96.537  1.00 12764. ? 153 LYS B O     1 
ATOM   5055  C  CB    . LYS B 1 153 ? 135.804 125.595 96.333  1.00 12731. ? 153 LYS B CB    1 
ATOM   5056  C  CG    . LYS B 1 153 ? 137.284 125.907 96.280  1.00 12744. ? 153 LYS B CG    1 
ATOM   5057  C  CD    . LYS B 1 153 ? 138.092 124.635 96.091  1.00 12752. ? 153 LYS B CD    1 
ATOM   5058  C  CE    . LYS B 1 153 ? 137.897 123.678 97.256  1.00 12748. ? 153 LYS B CE    1 
ATOM   5059  N  NZ    . LYS B 1 153 ? 138.674 124.094 98.456  1.00 12750. ? 153 LYS B NZ    1 
ATOM   5060  N  N     . LEU B 1 154 ? 133.585 128.024 95.844  1.00 12745. ? 154 LEU B N     1 
ATOM   5061  C  CA    . LEU B 1 154 ? 132.440 128.382 95.025  1.00 12740. ? 154 LEU B CA    1 
ATOM   5062  C  C     . LEU B 1 154 ? 132.950 128.905 93.693  1.00 12751. ? 154 LEU B C     1 
ATOM   5063  O  O     . LEU B 1 154 ? 134.042 129.470 93.621  1.00 12777. ? 154 LEU B O     1 
ATOM   5064  C  CB    . LEU B 1 154 ? 131.565 129.430 95.717  1.00 12735. ? 154 LEU B CB    1 
ATOM   5065  C  CG    . LEU B 1 154 ? 130.201 129.703 95.088  1.00 12740. ? 154 LEU B CG    1 
ATOM   5066  C  CD1   . LEU B 1 154 ? 129.419 128.411 94.951  1.00 12761. ? 154 LEU B CD1   1 
ATOM   5067  C  CD2   . LEU B 1 154 ? 129.431 130.705 95.920  1.00 12741. ? 154 LEU B CD2   1 
ATOM   5068  N  N     . GLN B 1 155 ? 132.175 128.699 92.638  1.00 12750. ? 155 GLN B N     1 
ATOM   5069  C  CA    . GLN B 1 155 ? 132.555 129.155 91.312  1.00 12741. ? 155 GLN B CA    1 
ATOM   5070  C  C     . GLN B 1 155 ? 131.630 130.280 90.872  1.00 12744. ? 155 GLN B C     1 
ATOM   5071  O  O     . GLN B 1 155 ? 130.412 130.199 91.041  1.00 12756. ? 155 GLN B O     1 
ATOM   5072  C  CB    . GLN B 1 155 ? 132.511 128.005 90.306  1.00 12772. ? 155 GLN B CB    1 
ATOM   5073  C  CG    . GLN B 1 155 ? 132.429 128.446 88.860  1.00 12783. ? 155 GLN B CG    1 
ATOM   5074  C  CD    . GLN B 1 155 ? 132.755 127.330 87.895  1.00 12791. ? 155 GLN B CD    1 
ATOM   5075  O  OE1   . GLN B 1 155 ? 131.911 126.909 87.105  1.00 12822. ? 155 GLN B OE1   1 
ATOM   5076  N  NE2   . GLN B 1 155 ? 133.987 126.841 87.953  1.00 12780. ? 155 GLN B NE2   1 
ATOM   5077  N  N     . VAL B 1 156 ? 132.216 131.335 90.325  1.00 12744. ? 156 VAL B N     1 
ATOM   5078  C  CA    . VAL B 1 156 ? 131.471 132.485 89.829  1.00 12751. ? 156 VAL B CA    1 
ATOM   5079  C  C     . VAL B 1 156 ? 131.720 132.552 88.330  1.00 12792. ? 156 VAL B C     1 
ATOM   5080  O  O     . VAL B 1 156 ? 132.799 132.960 87.890  1.00 12802. ? 156 VAL B O     1 
ATOM   5081  C  CB    . VAL B 1 156 ? 131.891 133.783 90.525  1.00 12744. ? 156 VAL B CB    1 
ATOM   5082  C  CG1   . VAL B 1 156 ? 131.176 134.968 89.906  1.00 12759. ? 156 VAL B CG1   1 
ATOM   5083  C  CG2   . VAL B 1 156 ? 131.610 133.702 92.012  1.00 12755. ? 156 VAL B CG2   1 
ATOM   5084  N  N     . MET B 1 157 ? 130.738 132.137 87.536  1.00 14032. ? 157 MET B N     1 
ATOM   5085  C  CA    . MET B 1 157 ? 130.847 132.205 86.084  1.00 14078. ? 157 MET B CA    1 
ATOM   5086  C  C     . MET B 1 157 ? 130.220 133.513 85.604  1.00 14086. ? 157 MET B C     1 
ATOM   5087  O  O     . MET B 1 157 ? 129.006 133.605 85.404  1.00 14086. ? 157 MET B O     1 
ATOM   5088  C  CB    . MET B 1 157 ? 130.232 130.961 85.438  1.00 14086. ? 157 MET B CB    1 
ATOM   5089  C  CG    . MET B 1 157 ? 128.733 130.754 85.612  1.00 14084. ? 157 MET B CG    1 
ATOM   5090  S  SD    . MET B 1 157 ? 128.070 129.462 84.543  1.00 14096. ? 157 MET B SD    1 
ATOM   5091  C  CE    . MET B 1 157 ? 129.276 129.455 83.221  1.00 14122. ? 157 MET B CE    1 
ATOM   5092  N  N     . ALA B 1 158 ? 131.054 134.536 85.443  1.00 13925. ? 158 ALA B N     1 
ATOM   5093  C  CA    . ALA B 1 158 ? 130.608 135.858 85.016  1.00 13936. ? 158 ALA B CA    1 
ATOM   5094  C  C     . ALA B 1 158 ? 130.428 135.832 83.506  1.00 13964. ? 158 ALA B C     1 
ATOM   5095  O  O     . ALA B 1 158 ? 131.390 135.643 82.754  1.00 13986. ? 158 ALA B O     1 
ATOM   5096  C  CB    . ALA B 1 158 ? 131.606 136.924 85.449  1.00 13933. ? 158 ALA B CB    1 
ATOM   5097  N  N     . ASN B 1 159 ? 129.186 136.009 83.068  1.00 14558. ? 159 ASN B N     1 
ATOM   5098  C  CA    . ASN B 1 159 ? 128.826 136.050 81.658  1.00 14589. ? 159 ASN B CA    1 
ATOM   5099  C  C     . ASN B 1 159 ? 128.235 137.417 81.341  1.00 14613. ? 159 ASN B C     1 
ATOM   5100  O  O     . ASN B 1 159 ? 127.532 138.000 82.173  1.00 14604. ? 159 ASN B O     1 
ATOM   5101  C  CB    . ASN B 1 159 ? 127.827 134.944 81.321  1.00 14592. ? 159 ASN B CB    1 
ATOM   5102  C  CG    . ASN B 1 159 ? 127.741 134.668 79.835  1.00 14611. ? 159 ASN B CG    1 
ATOM   5103  O  OD1   . ASN B 1 159 ? 127.453 135.563 79.041  1.00 14637. ? 159 ASN B OD1   1 
ATOM   5104  N  ND2   . ASN B 1 159 ? 127.990 133.423 79.450  1.00 14604. ? 159 ASN B ND2   1 
ATOM   5105  N  N     . SER B 1 160 ? 128.524 137.925 80.142  1.00 15295. ? 160 SER B N     1 
ATOM   5106  C  CA    . SER B 1 160 ? 128.084 139.268 79.779  1.00 15311. ? 160 SER B CA    1 
ATOM   5107  C  C     . SER B 1 160 ? 126.564 139.367 79.730  1.00 15320. ? 160 SER B C     1 
ATOM   5108  O  O     . SER B 1 160 ? 125.982 140.365 80.170  1.00 15313. ? 160 SER B O     1 
ATOM   5109  C  CB    . SER B 1 160 ? 128.690 139.670 78.435  1.00 15346. ? 160 SER B CB    1 
ATOM   5110  O  OG    . SER B 1 160 ? 130.091 139.477 78.432  1.00 15351. ? 160 SER B OG    1 
ATOM   5111  N  N     . ARG B 1 161 ? 125.920 138.332 79.186  1.00 15909. ? 161 ARG B N     1 
ATOM   5112  C  CA    . ARG B 1 161 ? 124.440 138.335 79.074  1.00 15925. ? 161 ARG B CA    1 
ATOM   5113  C  C     . ARG B 1 161 ? 123.823 138.536 80.464  1.00 15905. ? 161 ARG B C     1 
ATOM   5114  O  O     . ARG B 1 161 ? 123.066 139.515 80.642  1.00 15931. ? 161 ARG B O     1 
ATOM   5115  C  CB    . ARG B 1 161 ? 123.941 137.002 78.511  1.00 15942. ? 161 ARG B CB    1 
ATOM   5116  C  CG    . ARG B 1 161 ? 124.686 136.486 77.289  1.00 15946. ? 161 ARG B CG    1 
ATOM   5117  C  CD    . ARG B 1 161 ? 124.444 134.994 77.135  1.00 15955. ? 161 ARG B CD    1 
ATOM   5118  N  NE    . ARG B 1 161 ? 124.930 134.263 78.311  1.00 15952. ? 161 ARG B NE    1 
ATOM   5119  C  CZ    . ARG B 1 161 ? 124.167 133.554 79.134  1.00 15958. ? 161 ARG B CZ    1 
ATOM   5120  N  NH1   . ARG B 1 161 ? 122.858 133.525 78.962  1.00 15960. ? 161 ARG B NH1   1 
ATOM   5121  N  NH2   . ARG B 1 161 ? 124.717 132.883 80.130  1.00 15960. ? 161 ARG B NH2   1 
ATOM   5122  N  N     . ASN B 1 162 ? 124.160 137.660 81.414  1.00 15179. ? 162 ASN B N     1 
ATOM   5123  C  CA    . ASN B 1 162 ? 123.542 137.720 82.769  1.00 15164. ? 162 ASN B CA    1 
ATOM   5124  C  C     . ASN B 1 162 ? 124.049 138.941 83.546  1.00 15136. ? 162 ASN B C     1 
ATOM   5125  O  O     . ASN B 1 162 ? 123.355 139.355 84.501  1.00 15129. ? 162 ASN B O     1 
ATOM   5126  C  CB    . ASN B 1 162 ? 123.789 136.426 83.535  1.00 15168. ? 162 ASN B CB    1 
ATOM   5127  C  CG    . ASN B 1 162 ? 123.506 135.209 82.686  1.00 15187. ? 162 ASN B CG    1 
ATOM   5128  O  OD1   . ASN B 1 162 ? 124.409 134.404 82.432  1.00 15186. ? 162 ASN B OD1   1 
ATOM   5129  N  ND2   . ASN B 1 162 ? 122.271 135.061 82.231  1.00 15195. ? 162 ASN B ND2   1 
ATOM   5130  N  N     . TYR B 1 163 ? 125.206 139.494 83.167  1.00 13901. ? 163 TYR B N     1 
ATOM   5131  C  CA    . TYR B 1 163 ? 125.779 140.627 83.949  1.00 13875. ? 163 TYR B CA    1 
ATOM   5132  C  C     . TYR B 1 163 ? 124.878 141.853 83.767  1.00 13894. ? 163 TYR B C     1 
ATOM   5133  O  O     . TYR B 1 163 ? 124.174 141.945 82.737  1.00 13892. ? 163 TYR B O     1 
ATOM   5134  C  CB    . TYR B 1 163 ? 127.236 140.930 83.582  1.00 13875. ? 163 TYR B CB    1 
ATOM   5135  C  CG    . TYR B 1 163 ? 127.963 141.718 84.664  1.00 13856. ? 163 TYR B CG    1 
ATOM   5136  C  CD1   . TYR B 1 163 ? 128.533 141.074 85.755  1.00 13817. ? 163 TYR B CD1   1 
ATOM   5137  C  CD2   . TYR B 1 163 ? 128.047 143.105 84.614  1.00 13877. ? 163 TYR B CD2   1 
ATOM   5138  C  CE1   . TYR B 1 163 ? 129.183 141.782 86.752  1.00 13796. ? 163 TYR B CE1   1 
ATOM   5139  C  CE2   . TYR B 1 163 ? 128.695 143.824 85.605  1.00 13863. ? 163 TYR B CE2   1 
ATOM   5140  C  CZ    . TYR B 1 163 ? 129.264 143.161 86.677  1.00 13815. ? 163 TYR B CZ    1 
ATOM   5141  O  OH    . TYR B 1 163 ? 129.904 143.861 87.658  1.00 13811. ? 163 TYR B OH    1 
ATOM   5142  N  N     . LYS B 1 164 ? 124.907 142.778 84.733  1.00 15006. ? 164 LYS B N     1 
ATOM   5143  C  CA    . LYS B 1 164 ? 124.018 143.969 84.678  1.00 15042. ? 164 LYS B CA    1 
ATOM   5144  C  C     . LYS B 1 164 ? 124.211 144.707 83.342  1.00 15080. ? 164 LYS B C     1 
ATOM   5145  O  O     . LYS B 1 164 ? 123.190 145.019 82.692  1.00 15081. ? 164 LYS B O     1 
ATOM   5146  C  CB    . LYS B 1 164 ? 124.305 144.892 85.868  1.00 15036. ? 164 LYS B CB    1 
ATOM   5147  C  CG    . LYS B 1 164 ? 123.322 146.039 86.046  1.00 15063. ? 164 LYS B CG    1 
ATOM   5148  C  CD    . LYS B 1 164 ? 123.308 146.594 87.465  1.00 15059. ? 164 LYS B CD    1 
ATOM   5149  C  CE    . LYS B 1 164 ? 124.595 147.247 87.846  1.00 15051. ? 164 LYS B CE    1 
ATOM   5150  N  NZ    . LYS B 1 164 ? 124.816 148.474 87.077  1.00 15074. ? 164 LYS B NZ    1 
ATOM   5151  N  N     . SER B 1 165 ? 125.463 144.970 82.951  1.00 15880. ? 165 SER B N     1 
ATOM   5152  C  CA    . SER B 1 165 ? 125.725 145.726 81.697  1.00 15907. ? 165 SER B CA    1 
ATOM   5153  C  C     . SER B 1 165 ? 127.049 145.273 81.065  1.00 15917. ? 165 SER B C     1 
ATOM   5154  O  O     . SER B 1 165 ? 127.956 144.865 81.822  1.00 15887. ? 165 SER B O     1 
ATOM   5155  C  CB    . SER B 1 165 ? 125.714 147.211 81.947  1.00 15921. ? 165 SER B CB    1 
ATOM   5156  O  OG    . SER B 1 165 ? 125.587 147.922 80.724  1.00 15935. ? 165 SER B OG    1 
ATOM   5157  N  N     . GLU B 1 166 ? 127.153 145.351 79.734  1.00 16691. ? 166 GLU B N     1 
ATOM   5158  C  CA    . GLU B 1 166 ? 128.376 144.887 79.026  1.00 16705. ? 166 GLU B CA    1 
ATOM   5159  C  C     . GLU B 1 166 ? 129.571 145.785 79.383  1.00 16694. ? 166 GLU B C     1 
ATOM   5160  O  O     . GLU B 1 166 ? 130.607 145.244 79.825  1.00 16675. ? 166 GLU B O     1 
ATOM   5161  C  CB    . GLU B 1 166 ? 128.159 144.902 77.513  1.00 16721. ? 166 GLU B CB    1 
ATOM   5162  C  CG    . GLU B 1 166 ? 129.411 144.518 76.730  1.00 16728. ? 166 GLU B CG    1 
ATOM   5163  C  CD    . GLU B 1 166 ? 129.818 143.069 76.917  1.00 16716. ? 166 GLU B CD    1 
ATOM   5164  O  OE1   . GLU B 1 166 ? 129.024 142.188 76.529  1.00 16726. ? 166 GLU B OE1   1 
ATOM   5165  O  OE2   . GLU B 1 166 ? 130.917 142.820 77.457  1.00 16697. ? 166 GLU B OE2   1 
ATOM   5166  N  N     . GLU B 1 167 ? 129.434 147.100 79.192  1.00 16445. ? 167 GLU B N     1 
ATOM   5167  C  CA    . GLU B 1 167 ? 130.572 148.020 79.460  1.00 16437. ? 167 GLU B CA    1 
ATOM   5168  C  C     . GLU B 1 167 ? 130.975 147.850 80.932  1.00 16401. ? 167 GLU B C     1 
ATOM   5169  O  O     . GLU B 1 167 ? 132.186 147.937 81.227  1.00 16391. ? 167 GLU B O     1 
ATOM   5170  C  CB    . GLU B 1 167 ? 130.230 149.471 79.110  1.00 16453. ? 167 GLU B CB    1 
ATOM   5171  C  CG    . GLU B 1 167 ? 129.350 150.174 80.140  1.00 16454. ? 167 GLU B CG    1 
ATOM   5172  C  CD    . GLU B 1 167 ? 127.879 149.803 80.107  1.00 16457. ? 167 GLU B CD    1 
ATOM   5173  O  OE1   . GLU B 1 167 ? 127.485 148.986 79.248  1.00 16460. ? 167 GLU B OE1   1 
ATOM   5174  O  OE2   . GLU B 1 167 ? 127.124 150.334 80.948  1.00 16453. ? 167 GLU B OE2   1 
ATOM   5175  N  N     . GLU B 1 168 ? 129.999 147.601 81.810  1.00 15653. ? 168 GLU B N     1 
ATOM   5176  C  CA    . GLU B 1 168 ? 130.307 147.366 83.214  1.00 15620. ? 168 GLU B CA    1 
ATOM   5177  C  C     . GLU B 1 168 ? 130.952 146.008 83.444  1.00 15574. ? 168 GLU B C     1 
ATOM   5178  O  O     . GLU B 1 168 ? 131.805 145.883 84.329  1.00 15558. ? 168 GLU B O     1 
ATOM   5179  C  CB    . GLU B 1 168 ? 129.041 147.492 84.062  1.00 15626. ? 168 GLU B CB    1 
ATOM   5180  C  CG    . GLU B 1 168 ? 128.291 148.791 83.844  1.00 15636. ? 168 GLU B CG    1 
ATOM   5181  C  CD    . GLU B 1 168 ? 127.256 149.051 84.917  1.00 15631. ? 168 GLU B CD    1 
ATOM   5182  O  OE1   . GLU B 1 168 ? 127.124 148.210 85.830  1.00 15624. ? 168 GLU B OE1   1 
ATOM   5183  O  OE2   . GLU B 1 168 ? 126.577 150.096 84.850  1.00 15635. ? 168 GLU B OE2   1 
ATOM   5184  N  N     . PHE B 1 169 ? 130.571 144.996 82.664  1.00 14769. ? 169 PHE B N     1 
ATOM   5185  C  CA    . PHE B 1 169 ? 131.241 143.701 82.732  1.00 14736. ? 169 PHE B CA    1 
ATOM   5186  C  C     . PHE B 1 169 ? 132.721 143.836 82.393  1.00 14716. ? 169 PHE B C     1 
ATOM   5187  O  O     . PHE B 1 169 ? 133.586 143.321 83.113  1.00 14706. ? 169 PHE B O     1 
ATOM   5188  C  CB    . PHE B 1 169 ? 130.548 142.724 81.783  1.00 14750. ? 169 PHE B CB    1 
ATOM   5189  C  CG    . PHE B 1 169 ? 131.130 141.346 81.786  1.00 14730. ? 169 PHE B CG    1 
ATOM   5190  C  CD1   . PHE B 1 169 ? 130.874 140.473 82.825  1.00 14713. ? 169 PHE B CD1   1 
ATOM   5191  C  CD2   . PHE B 1 169 ? 131.917 140.914 80.733  1.00 14748. ? 169 PHE B CD2   1 
ATOM   5192  C  CE1   . PHE B 1 169 ? 131.403 139.201 82.820  1.00 14720. ? 169 PHE B CE1   1 
ATOM   5193  C  CE2   . PHE B 1 169 ? 132.448 139.643 80.725  1.00 14757. ? 169 PHE B CE2   1 
ATOM   5194  C  CZ    . PHE B 1 169 ? 132.188 138.785 81.769  1.00 14732. ? 169 PHE B CZ    1 
ATOM   5195  N  N     . ILE B 1 170 ? 133.029 144.551 81.310  1.00 14592. ? 170 ILE B N     1 
ATOM   5196  C  CA    . ILE B 1 170 ? 134.420 144.783 80.934  1.00 14568. ? 170 ILE B CA    1 
ATOM   5197  C  C     . ILE B 1 170 ? 135.134 145.588 82.011  1.00 14561. ? 170 ILE B C     1 
ATOM   5198  O  O     . ILE B 1 170 ? 136.283 145.298 82.364  1.00 14560. ? 170 ILE B O     1 
ATOM   5199  C  CB    . ILE B 1 170 ? 134.493 145.486 79.566  1.00 14577. ? 170 ILE B CB    1 
ATOM   5200  C  CG1   . ILE B 1 170 ? 133.747 144.673 78.508  1.00 14588. ? 170 ILE B CG1   1 
ATOM   5201  C  CG2   . ILE B 1 170 ? 135.937 145.699 79.155  1.00 14568. ? 170 ILE B CG2   1 
ATOM   5202  C  CD1   . ILE B 1 170 ? 134.358 143.319 78.236  1.00 14587. ? 170 ILE B CD1   1 
ATOM   5203  N  N     . HIS B 1 171 ? 134.467 146.613 82.545  1.00 14631. ? 171 HIS B N     1 
ATOM   5204  C  CA    . HIS B 1 171 ? 135.094 147.465 83.548  1.00 14611. ? 171 HIS B CA    1 
ATOM   5205  C  C     . HIS B 1 171 ? 135.448 146.683 84.805  1.00 14574. ? 171 HIS B C     1 
ATOM   5206  O  O     . HIS B 1 171 ? 136.533 146.860 85.370  1.00 14578. ? 171 HIS B O     1 
ATOM   5207  C  CB    . HIS B 1 171 ? 134.171 148.634 83.888  1.00 14629. ? 171 HIS B CB    1 
ATOM   5208  C  CG    . HIS B 1 171 ? 134.819 149.689 84.727  1.00 14615. ? 171 HIS B CG    1 
ATOM   5209  N  ND1   . HIS B 1 171 ? 134.097 150.586 85.483  1.00 14626. ? 171 HIS B ND1   1 
ATOM   5210  C  CD2   . HIS B 1 171 ? 136.123 149.988 84.932  1.00 14617. ? 171 HIS B CD2   1 
ATOM   5211  C  CE1   . HIS B 1 171 ? 134.928 151.394 86.116  1.00 14634. ? 171 HIS B CE1   1 
ATOM   5212  N  NE2   . HIS B 1 171 ? 136.163 151.053 85.800  1.00 14628. ? 171 HIS B NE2   1 
ATOM   5213  N  N     . ILE B 1 172 ? 134.547 145.814 85.263  1.00 13199. ? 172 ILE B N     1 
ATOM   5214  C  CA    . ILE B 1 172 ? 134.819 145.069 86.485  1.00 13127. ? 172 ILE B CA    1 
ATOM   5215  C  C     . ILE B 1 172 ? 135.800 143.931 86.230  1.00 13143. ? 172 ILE B C     1 
ATOM   5216  O  O     . ILE B 1 172 ? 136.552 143.547 87.132  1.00 13129. ? 172 ILE B O     1 
ATOM   5217  C  CB    . ILE B 1 172 ? 133.511 144.558 87.112  1.00 13105. ? 172 ILE B CB    1 
ATOM   5218  C  CG1   . ILE B 1 172 ? 133.750 144.120 88.557  1.00 13079. ? 172 ILE B CG1   1 
ATOM   5219  C  CG2   . ILE B 1 172 ? 132.925 143.417 86.299  1.00 13144. ? 172 ILE B CG2   1 
ATOM   5220  C  CD1   . ILE B 1 172 ? 134.017 145.264 89.503  1.00 13074. ? 172 ILE B CD1   1 
ATOM   5221  N  N     . ASN B 1 173 ? 135.828 143.377 85.017  1.00 14120. ? 173 ASN B N     1 
ATOM   5222  C  CA    . ASN B 1 173 ? 136.759 142.295 84.733  1.00 14138. ? 173 ASN B CA    1 
ATOM   5223  C  C     . ASN B 1 173 ? 138.186 142.775 84.520  1.00 14138. ? 173 ASN B C     1 
ATOM   5224  O  O     . ASN B 1 173 ? 139.107 141.952 84.543  1.00 14130. ? 173 ASN B O     1 
ATOM   5225  C  CB    . ASN B 1 173 ? 136.298 141.509 83.507  1.00 14161. ? 173 ASN B CB    1 
ATOM   5226  C  CG    . ASN B 1 173 ? 135.335 140.402 83.861  1.00 14159. ? 173 ASN B CG    1 
ATOM   5227  O  OD1   . ASN B 1 173 ? 134.924 140.266 85.013  1.00 14152. ? 173 ASN B OD1   1 
ATOM   5228  N  ND2   . ASN B 1 173 ? 134.970 139.600 82.873  1.00 14176. ? 173 ASN B ND2   1 
ATOM   5229  N  N     . ASN B 1 174 ? 138.395 144.072 84.311  1.00 14162. ? 174 ASN B N     1 
ATOM   5230  C  CA    . ASN B 1 174 ? 139.727 144.624 84.118  1.00 14161. ? 174 ASN B CA    1 
ATOM   5231  C  C     . ASN B 1 174 ? 140.322 145.196 85.395  1.00 14136. ? 174 ASN B C     1 
ATOM   5232  O  O     . ASN B 1 174 ? 141.431 145.736 85.357  1.00 14172. ? 174 ASN B O     1 
ATOM   5233  C  CB    . ASN B 1 174 ? 139.696 145.706 83.036  1.00 14185. ? 174 ASN B CB    1 
ATOM   5234  C  CG    . ASN B 1 174 ? 139.327 145.155 81.676  1.00 14192. ? 174 ASN B CG    1 
ATOM   5235  O  OD1   . ASN B 1 174 ? 139.101 143.955 81.522  1.00 14197. ? 174 ASN B OD1   1 
ATOM   5236  N  ND2   . ASN B 1 174 ? 139.265 146.029 80.680  1.00 14192. ? 174 ASN B ND2   1 
ATOM   5237  N  N     . LYS B 1 175 ? 139.619 145.092 86.521  1.00 12815. ? 175 LYS B N     1 
ATOM   5238  C  CA    . LYS B 1 175 ? 140.117 145.592 87.791  1.00 12769. ? 175 LYS B CA    1 
ATOM   5239  C  C     . LYS B 1 175 ? 140.235 144.521 88.864  1.00 12751. ? 175 LYS B C     1 
ATOM   5240  O  O     . LYS B 1 175 ? 140.792 144.803 89.931  1.00 12755. ? 175 LYS B O     1 
ATOM   5241  C  CB    . LYS B 1 175 ? 139.218 146.726 88.309  1.00 12750. ? 175 LYS B CB    1 
ATOM   5242  C  CG    . LYS B 1 175 ? 138.093 146.266 89.216  1.00 12745. ? 175 LYS B CG    1 
ATOM   5243  C  CD    . LYS B 1 175 ? 137.501 147.418 90.006  1.00 12735. ? 175 LYS B CD    1 
ATOM   5244  C  CE    . LYS B 1 175 ? 136.921 148.476 89.091  1.00 12771. ? 175 LYS B CE    1 
ATOM   5245  N  NZ    . LYS B 1 175 ? 136.038 149.412 89.839  1.00 12783. ? 175 LYS B NZ    1 
ATOM   5246  N  N     . LEU B 1 176 ? 139.750 143.309 88.615  1.00 12763. ? 176 LEU B N     1 
ATOM   5247  C  CA    . LEU B 1 176 ? 139.780 142.234 89.596  1.00 12747. ? 176 LEU B CA    1 
ATOM   5248  C  C     . LEU B 1 176 ? 140.909 141.268 89.270  1.00 12749. ? 176 LEU B C     1 
ATOM   5249  O  O     . LEU B 1 176 ? 141.095 140.890 88.109  1.00 12758. ? 176 LEU B O     1 
ATOM   5250  C  CB    . LEU B 1 176 ? 138.449 141.485 89.630  1.00 12744. ? 176 LEU B CB    1 
ATOM   5251  C  CG    . LEU B 1 176 ? 137.225 142.281 90.077  1.00 12744. ? 176 LEU B CG    1 
ATOM   5252  C  CD1   . LEU B 1 176 ? 135.999 141.389 90.086  1.00 12749. ? 176 LEU B CD1   1 
ATOM   5253  C  CD2   . LEU B 1 176 ? 137.458 142.896 91.443  1.00 12761. ? 176 LEU B CD2   1 
ATOM   5254  N  N     . ARG B 1 177 ? 141.658 140.875 90.297  1.00 12748. ? 177 ARG B N     1 
ATOM   5255  C  CA    . ARG B 1 177 ? 142.737 139.911 90.157  1.00 12747. ? 177 ARG B CA    1 
ATOM   5256  C  C     . ARG B 1 177 ? 142.732 138.999 91.374  1.00 12744. ? 177 ARG B C     1 
ATOM   5257  O  O     . ARG B 1 177 ? 142.122 139.308 92.399  1.00 12750. ? 177 ARG B O     1 
ATOM   5258  C  CB    . ARG B 1 177 ? 144.092 140.609 89.988  1.00 12757. ? 177 ARG B CB    1 
ATOM   5259  C  CG    . ARG B 1 177 ? 144.301 141.147 88.586  1.00 12750. ? 177 ARG B CG    1 
ATOM   5260  C  CD    . ARG B 1 177 ? 145.425 142.160 88.513  1.00 12753. ? 177 ARG B CD    1 
ATOM   5261  N  NE    . ARG B 1 177 ? 145.576 142.699 87.166  1.00 12741. ? 177 ARG B NE    1 
ATOM   5262  C  CZ    . ARG B 1 177 ? 144.675 143.449 86.543  1.00 12744. ? 177 ARG B CZ    1 
ATOM   5263  N  NH1   . ARG B 1 177 ? 143.549 143.814 87.133  1.00 12756. ? 177 ARG B NH1   1 
ATOM   5264  N  NH2   . ARG B 1 177 ? 144.915 143.850 85.299  1.00 12745. ? 177 ARG B NH2   1 
ATOM   5265  N  N     . ARG B 1 178 ? 143.411 137.859 91.246  1.00 12743. ? 178 ARG B N     1 
ATOM   5266  C  CA    . ARG B 1 178 ? 143.363 136.841 92.287  1.00 12744. ? 178 ARG B CA    1 
ATOM   5267  C  C     . ARG B 1 178 ? 143.878 137.394 93.609  1.00 12731. ? 178 ARG B C     1 
ATOM   5268  O  O     . ARG B 1 178 ? 144.814 138.195 93.648  1.00 12737. ? 178 ARG B O     1 
ATOM   5269  C  CB    . ARG B 1 178 ? 144.167 135.607 91.868  1.00 12754. ? 178 ARG B CB    1 
ATOM   5270  C  CG    . ARG B 1 178 ? 145.671 135.747 91.977  1.00 12738. ? 178 ARG B CG    1 
ATOM   5271  C  CD    . ARG B 1 178 ? 146.359 134.414 91.736  1.00 12748. ? 178 ARG B CD    1 
ATOM   5272  N  NE    . ARG B 1 178 ? 146.032 133.436 92.766  1.00 12780. ? 178 ARG B NE    1 
ATOM   5273  C  CZ    . ARG B 1 178 ? 146.929 132.830 93.533  1.00 12812. ? 178 ARG B CZ    1 
ATOM   5274  N  NH1   . ARG B 1 178 ? 148.222 133.077 93.411  1.00 12887. ? 178 ARG B NH1   1 
ATOM   5275  N  NH2   . ARG B 1 178 ? 146.517 131.955 94.445  1.00 12810. ? 178 ARG B NH2   1 
ATOM   5276  N  N     . GLY B 1 179 ? 143.234 136.978 94.695  1.00 12745. ? 179 GLY B N     1 
ATOM   5277  C  CA    . GLY B 1 179 ? 143.517 137.482 96.015  1.00 12754. ? 179 GLY B CA    1 
ATOM   5278  C  C     . GLY B 1 179 ? 142.620 138.619 96.457  1.00 12744. ? 179 GLY B C     1 
ATOM   5279  O  O     . GLY B 1 179 ? 142.604 138.950 97.647  1.00 12762. ? 179 GLY B O     1 
ATOM   5280  N  N     . ASP B 1 180 ? 141.877 139.222 95.534  1.00 12734. ? 180 ASP B N     1 
ATOM   5281  C  CA    . ASP B 1 180 ? 140.996 140.325 95.885  1.00 12738. ? 180 ASP B CA    1 
ATOM   5282  C  C     . ASP B 1 180 ? 139.782 139.824 96.654  1.00 12734. ? 180 ASP B C     1 
ATOM   5283  O  O     . ASP B 1 180 ? 139.234 138.760 96.357  1.00 12743. ? 180 ASP B O     1 
ATOM   5284  C  CB    . ASP B 1 180 ? 140.542 141.063 94.628  1.00 12748. ? 180 ASP B CB    1 
ATOM   5285  C  CG    . ASP B 1 180 ? 141.633 141.923 94.031  1.00 12758. ? 180 ASP B CG    1 
ATOM   5286  O  OD1   . ASP B 1 180 ? 142.708 142.041 94.655  1.00 12770. ? 180 ASP B OD1   1 
ATOM   5287  O  OD2   . ASP B 1 180 ? 141.418 142.481 92.936  1.00 12761. ? 180 ASP B OD2   1 
ATOM   5288  N  N     . ILE B 1 181 ? 139.362 140.600 97.645  1.00 12732. ? 181 ILE B N     1 
ATOM   5289  C  CA    . ILE B 1 181 ? 138.136 140.329 98.384  1.00 12730. ? 181 ILE B CA    1 
ATOM   5290  C  C     . ILE B 1 181 ? 136.994 141.021 97.655  1.00 12737. ? 181 ILE B C     1 
ATOM   5291  O  O     . ILE B 1 181 ? 136.968 142.252 97.562  1.00 12753. ? 181 ILE B O     1 
ATOM   5292  C  CB    . ILE B 1 181 ? 138.238 140.819 99.835  1.00 12733. ? 181 ILE B CB    1 
ATOM   5293  C  CG1   . ILE B 1 181 ? 139.430 140.170 100.539 1.00 12740. ? 181 ILE B CG1   1 
ATOM   5294  C  CG2   . ILE B 1 181 ? 136.940 140.550 100.575 1.00 12751. ? 181 ILE B CG2   1 
ATOM   5295  C  CD1   . ILE B 1 181 ? 139.097 138.901 101.280 1.00 12745. ? 181 ILE B CD1   1 
ATOM   5296  N  N     . ILE B 1 182 ? 136.047 140.232 97.144  1.00 12741. ? 182 ILE B N     1 
ATOM   5297  C  CA    . ILE B 1 182 ? 134.960 140.741 96.323  1.00 12741. ? 182 ILE B CA    1 
ATOM   5298  C  C     . ILE B 1 182 ? 133.628 140.238 96.859  1.00 12737. ? 182 ILE B C     1 
ATOM   5299  O  O     . ILE B 1 182 ? 133.541 139.200 97.522  1.00 12749. ? 182 ILE B O     1 
ATOM   5300  C  CB    . ILE B 1 182 ? 135.107 140.339 94.841  1.00 12737. ? 182 ILE B CB    1 
ATOM   5301  C  CG1   . ILE B 1 182 ? 135.000 138.822 94.693  1.00 12739. ? 182 ILE B CG1   1 
ATOM   5302  C  CG2   . ILE B 1 182 ? 136.417 140.841 94.276  1.00 12759. ? 182 ILE B CG2   1 
ATOM   5303  C  CD1   . ILE B 1 182 ? 134.541 138.378 93.331  1.00 12747. ? 182 ILE B CD1   1 
ATOM   5304  N  N     . GLY B 1 183 ? 132.582 140.992 96.545  1.00 12738. ? 183 GLY B N     1 
ATOM   5305  C  CA    . GLY B 1 183 ? 131.210 140.602 96.828  1.00 12744. ? 183 GLY B CA    1 
ATOM   5306  C  C     . GLY B 1 183 ? 130.457 140.386 95.527  1.00 12747. ? 183 GLY B C     1 
ATOM   5307  O  O     . GLY B 1 183 ? 130.558 141.193 94.601  1.00 12769. ? 183 GLY B O     1 
ATOM   5308  N  N     . VAL B 1 184 ? 129.705 139.292 95.468  1.00 12729. ? 184 VAL B N     1 
ATOM   5309  C  CA    . VAL B 1 184 ? 128.985 138.878 94.271  1.00 12722. ? 184 VAL B CA    1 
ATOM   5310  C  C     . VAL B 1 184 ? 127.502 138.806 94.597  1.00 12733. ? 184 VAL B C     1 
ATOM   5311  O  O     . VAL B 1 184 ? 127.103 138.126 95.548  1.00 12756. ? 184 VAL B O     1 
ATOM   5312  C  CB    . VAL B 1 184 ? 129.486 137.518 93.754  1.00 12726. ? 184 VAL B CB    1 
ATOM   5313  C  CG1   . VAL B 1 184 ? 128.785 137.152 92.466  1.00 12744. ? 184 VAL B CG1   1 
ATOM   5314  C  CG2   . VAL B 1 184 ? 130.985 137.548 93.553  1.00 12748. ? 184 VAL B CG2   1 
ATOM   5315  N  N     . GLN B 1 185 ? 126.690 139.496 93.804  1.00 12740. ? 185 GLN B N     1 
ATOM   5316  C  CA    . GLN B 1 185 ? 125.239 139.396 93.875  1.00 12740. ? 185 GLN B CA    1 
ATOM   5317  C  C     . GLN B 1 185 ? 124.752 138.715 92.606  1.00 12749. ? 185 GLN B C     1 
ATOM   5318  O  O     . GLN B 1 185 ? 124.937 139.246 91.506  1.00 12781. ? 185 GLN B O     1 
ATOM   5319  C  CB    . GLN B 1 185 ? 124.599 140.774 94.029  1.00 12750. ? 185 GLN B CB    1 
ATOM   5320  C  CG    . GLN B 1 185 ? 123.103 140.734 94.258  1.00 12744. ? 185 GLN B CG    1 
ATOM   5321  C  CD    . GLN B 1 185 ? 122.384 141.890 93.605  1.00 12743. ? 185 GLN B CD    1 
ATOM   5322  O  OE1   . GLN B 1 185 ? 122.323 142.988 94.156  1.00 12745. ? 185 GLN B OE1   1 
ATOM   5323  N  NE2   . GLN B 1 185 ? 121.829 141.650 92.425  1.00 12756. ? 185 GLN B NE2   1 
ATOM   5324  N  N     . GLY B 1 186 ? 124.134 137.552 92.753  1.00 12738. ? 186 GLY B N     1 
ATOM   5325  C  CA    . GLY B 1 186 ? 123.767 136.797 91.575  1.00 12752. ? 186 GLY B CA    1 
ATOM   5326  C  C     . GLY B 1 186 ? 122.811 135.670 91.889  1.00 12752. ? 186 GLY B C     1 
ATOM   5327  O  O     . GLY B 1 186 ? 122.344 135.517 93.017  1.00 12762. ? 186 GLY B O     1 
ATOM   5328  N  N     . ASN B 1 187 ? 122.536 134.875 90.858  1.00 13018. ? 187 ASN B N     1 
ATOM   5329  C  CA    . ASN B 1 187 ? 121.568 133.785 90.908  1.00 13032. ? 187 ASN B CA    1 
ATOM   5330  C  C     . ASN B 1 187 ? 122.278 132.445 90.977  1.00 13025. ? 187 ASN B C     1 
ATOM   5331  O  O     . ASN B 1 187 ? 123.235 132.221 90.223  1.00 13042. ? 187 ASN B O     1 
ATOM   5332  C  CB    . ASN B 1 187 ? 120.663 133.817 89.681  1.00 13065. ? 187 ASN B CB    1 
ATOM   5333  C  CG    . ASN B 1 187 ? 120.061 135.183 89.435  1.00 13068. ? 187 ASN B CG    1 
ATOM   5334  O  OD1   . ASN B 1 187 ? 119.719 135.902 90.372  1.00 13061. ? 187 ASN B OD1   1 
ATOM   5335  N  ND2   . ASN B 1 187 ? 119.925 135.547 88.167  1.00 13088. ? 187 ASN B ND2   1 
ATOM   5336  N  N     . PRO B 1 188 ? 121.849 131.535 91.846  1.00 12747. ? 188 PRO B N     1 
ATOM   5337  C  CA    . PRO B 1 188 ? 122.471 130.209 91.887  1.00 12741. ? 188 PRO B CA    1 
ATOM   5338  C  C     . PRO B 1 188 ? 122.177 129.413 90.628  1.00 12770. ? 188 PRO B C     1 
ATOM   5339  O  O     . PRO B 1 188 ? 121.177 129.632 89.941  1.00 12814. ? 188 PRO B O     1 
ATOM   5340  C  CB    . PRO B 1 188 ? 121.831 129.555 93.116  1.00 12765. ? 188 PRO B CB    1 
ATOM   5341  C  CG    . PRO B 1 188 ? 120.546 130.272 93.296  1.00 12783. ? 188 PRO B CG    1 
ATOM   5342  C  CD    . PRO B 1 188 ? 120.783 131.680 92.848  1.00 12779. ? 188 PRO B CD    1 
ATOM   5343  N  N     . GLY B 1 189 ? 123.069 128.477 90.330  1.00 13132. ? 189 GLY B N     1 
ATOM   5344  C  CA    . GLY B 1 189 ? 122.893 127.630 89.169  1.00 13186. ? 189 GLY B CA    1 
ATOM   5345  C  C     . GLY B 1 189 ? 123.981 126.583 89.115  1.00 13213. ? 189 GLY B C     1 
ATOM   5346  O  O     . GLY B 1 189 ? 124.785 126.448 90.038  1.00 13194. ? 189 GLY B O     1 
ATOM   5347  N  N     . LYS B 1 190 ? 124.000 125.839 88.014  1.00 14714. ? 190 LYS B N     1 
ATOM   5348  C  CA    . LYS B 1 190 ? 125.004 124.808 87.813  1.00 14735. ? 190 LYS B CA    1 
ATOM   5349  C  C     . LYS B 1 190 ? 125.440 124.810 86.357  1.00 14778. ? 190 LYS B C     1 
ATOM   5350  O  O     . LYS B 1 190 ? 124.660 125.136 85.459  1.00 14780. ? 190 LYS B O     1 
ATOM   5351  C  CB    . LYS B 1 190 ? 124.476 123.424 88.209  1.00 14770. ? 190 LYS B CB    1 
ATOM   5352  C  CG    . LYS B 1 190 ? 125.436 122.627 89.069  1.00 14760. ? 190 LYS B CG    1 
ATOM   5353  C  CD    . LYS B 1 190 ? 124.841 121.296 89.487  1.00 14793. ? 190 LYS B CD    1 
ATOM   5354  C  CE    . LYS B 1 190 ? 125.150 120.993 90.942  1.00 14759. ? 190 LYS B CE    1 
ATOM   5355  N  NZ    . LYS B 1 190 ? 124.853 119.577 91.288  1.00 14766. ? 190 LYS B NZ    1 
ATOM   5356  N  N     . THR B 1 191 ? 126.698 124.449 86.134  1.00 15457. ? 191 THR B N     1 
ATOM   5357  C  CA    . THR B 1 191 ? 127.233 124.383 84.786  1.00 15494. ? 191 THR B CA    1 
ATOM   5358  C  C     . THR B 1 191 ? 126.917 123.031 84.154  1.00 15527. ? 191 THR B C     1 
ATOM   5359  O  O     . THR B 1 191 ? 126.393 122.118 84.797  1.00 15528. ? 191 THR B O     1 
ATOM   5360  C  CB    . THR B 1 191 ? 128.742 124.623 84.791  1.00 15494. ? 191 THR B CB    1 
ATOM   5361  O  OG1   . THR B 1 191 ? 129.423 123.379 84.993  1.00 15516. ? 191 THR B OG1   1 
ATOM   5362  C  CG2   . THR B 1 191 ? 129.122 125.585 85.900  1.00 15469. ? 191 THR B CG2   1 
ATOM   5363  N  N     . LYS B 1 192 ? 127.243 122.913 82.866  1.00 16462. ? 192 LYS B N     1 
ATOM   5364  C  CA    . LYS B 1 192 ? 127.035 121.657 82.158  1.00 16491. ? 192 LYS B CA    1 
ATOM   5365  C  C     . LYS B 1 192 ? 127.908 120.540 82.712  1.00 16500. ? 192 LYS B C     1 
ATOM   5366  O  O     . LYS B 1 192 ? 127.574 119.364 82.536  1.00 16511. ? 192 LYS B O     1 
ATOM   5367  C  CB    . LYS B 1 192 ? 127.295 121.794 80.645  1.00 16507. ? 192 LYS B CB    1 
ATOM   5368  C  CG    . LYS B 1 192 ? 127.056 120.574 79.712  1.00 16510. ? 192 LYS B CG    1 
ATOM   5369  C  CD    . LYS B 1 192 ? 127.285 120.782 78.214  1.00 16503. ? 192 LYS B CD    1 
ATOM   5370  C  CE    . LYS B 1 192 ? 127.039 119.502 77.423  1.00 16503. ? 192 LYS B CE    1 
ATOM   5371  N  NZ    . LYS B 1 192 ? 127.262 119.702 75.965  1.00 16494. ? 192 LYS B NZ    1 
ATOM   5372  N  N     . LYS B 1 193 ? 129.009 120.878 83.376  1.00 16696. ? 193 LYS B N     1 
ATOM   5373  C  CA    . LYS B 1 193 ? 129.888 119.893 83.987  1.00 16704. ? 193 LYS B CA    1 
ATOM   5374  C  C     . LYS B 1 193 ? 129.455 119.508 85.395  1.00 16699. ? 193 LYS B C     1 
ATOM   5375  O  O     . LYS B 1 193 ? 130.115 118.675 86.024  1.00 16714. ? 193 LYS B O     1 
ATOM   5376  C  CB    . LYS B 1 193 ? 131.328 120.414 84.015  1.00 16718. ? 193 LYS B CB    1 
ATOM   5377  C  CG    . LYS B 1 193 ? 131.957 120.560 82.640  1.00 16722. ? 193 LYS B CG    1 
ATOM   5378  C  CD    . LYS B 1 193 ? 133.372 121.102 82.736  1.00 16727. ? 193 LYS B CD    1 
ATOM   5379  C  CE    . LYS B 1 193 ? 134.011 121.226 81.363  1.00 16725. ? 193 LYS B CE    1 
ATOM   5380  N  NZ    . LYS B 1 193 ? 135.392 121.779 81.436  1.00 16723. ? 193 LYS B NZ    1 
ATOM   5381  N  N     . GLY B 1 194 ? 128.372 120.090 85.901  1.00 16023. ? 194 GLY B N     1 
ATOM   5382  C  CA    . GLY B 1 194 ? 127.862 119.733 87.209  1.00 16006. ? 194 GLY B CA    1 
ATOM   5383  C  C     . GLY B 1 194 ? 128.595 120.396 88.355  1.00 15978. ? 194 GLY B C     1 
ATOM   5384  O  O     . GLY B 1 194 ? 128.838 119.769 89.390  1.00 15987. ? 194 GLY B O     1 
ATOM   5385  N  N     . GLU B 1 195 ? 128.951 121.667 88.186  1.00 15279. ? 195 GLU B N     1 
ATOM   5386  C  CA    . GLU B 1 195 ? 129.632 122.440 89.215  1.00 15236. ? 195 GLU B CA    1 
ATOM   5387  C  C     . GLU B 1 195 ? 128.706 123.550 89.687  1.00 15176. ? 195 GLU B C     1 
ATOM   5388  O  O     . GLU B 1 195 ? 128.244 124.360 88.877  1.00 15189. ? 195 GLU B O     1 
ATOM   5389  C  CB    . GLU B 1 195 ? 130.944 123.023 88.687  1.00 15234. ? 195 GLU B CB    1 
ATOM   5390  C  CG    . GLU B 1 195 ? 131.568 124.062 89.598  1.00 15216. ? 195 GLU B CG    1 
ATOM   5391  C  CD    . GLU B 1 195 ? 133.078 124.106 89.481  1.00 15228. ? 195 GLU B CD    1 
ATOM   5392  O  OE1   . GLU B 1 195 ? 133.585 124.127 88.340  1.00 15224. ? 195 GLU B OE1   1 
ATOM   5393  O  OE2   . GLU B 1 195 ? 133.757 124.120 90.529  1.00 15243. ? 195 GLU B OE2   1 
ATOM   5394  N  N     . LEU B 1 196 ? 128.435 123.583 90.989  1.00 13374. ? 196 LEU B N     1 
ATOM   5395  C  CA    . LEU B 1 196 ? 127.593 124.630 91.551  1.00 13333. ? 196 LEU B CA    1 
ATOM   5396  C  C     . LEU B 1 196 ? 128.259 125.986 91.370  1.00 13303. ? 196 LEU B C     1 
ATOM   5397  O  O     . LEU B 1 196 ? 129.460 126.138 91.608  1.00 13317. ? 196 LEU B O     1 
ATOM   5398  C  CB    . LEU B 1 196 ? 127.330 124.360 93.031  1.00 13306. ? 196 LEU B CB    1 
ATOM   5399  C  CG    . LEU B 1 196 ? 126.566 125.444 93.790  1.00 13280. ? 196 LEU B CG    1 
ATOM   5400  C  CD1   . LEU B 1 196 ? 125.192 125.653 93.184  1.00 13292. ? 196 LEU B CD1   1 
ATOM   5401  C  CD2   . LEU B 1 196 ? 126.455 125.094 95.260  1.00 13286. ? 196 LEU B CD2   1 
ATOM   5402  N  N     . SER B 1 197 ? 127.475 126.976 90.948  1.00 12999. ? 197 SER B N     1 
ATOM   5403  C  CA    . SER B 1 197 ? 128.006 128.293 90.645  1.00 12969. ? 197 SER B CA    1 
ATOM   5404  C  C     . SER B 1 197 ? 126.960 129.340 90.985  1.00 12966. ? 197 SER B C     1 
ATOM   5405  O  O     . SER B 1 197 ? 125.781 129.031 91.172  1.00 12992. ? 197 SER B O     1 
ATOM   5406  C  CB    . SER B 1 197 ? 128.412 128.414 89.172  1.00 12990. ? 197 SER B CB    1 
ATOM   5407  O  OG    . SER B 1 197 ? 129.135 127.274 88.746  1.00 13035. ? 197 SER B OG    1 
ATOM   5408  N  N     . ILE B 1 198 ? 127.407 130.586 91.075  1.00 12752. ? 198 ILE B N     1 
ATOM   5409  C  CA    . ILE B 1 198 ? 126.523 131.726 91.276  1.00 12751. ? 198 ILE B CA    1 
ATOM   5410  C  C     . ILE B 1 198 ? 126.780 132.680 90.116  1.00 12745. ? 198 ILE B C     1 
ATOM   5411  O  O     . ILE B 1 198 ? 127.796 133.384 90.084  1.00 12760. ? 198 ILE B O     1 
ATOM   5412  C  CB    . ILE B 1 198 ? 126.741 132.402 92.636  1.00 12745. ? 198 ILE B CB    1 
ATOM   5413  C  CG1   . ILE B 1 198 ? 126.076 133.778 92.675  1.00 12748. ? 198 ILE B CG1   1 
ATOM   5414  C  CG2   . ILE B 1 198 ? 128.222 132.492 92.973  1.00 12747. ? 198 ILE B CG2   1 
ATOM   5415  C  CD1   . ILE B 1 198 ? 126.073 134.405 94.047  1.00 12756. ? 198 ILE B CD1   1 
ATOM   5416  N  N     . ILE B 1 199 ? 125.872 132.691 89.146  1.00 12744. ? 199 ILE B N     1 
ATOM   5417  C  CA    . ILE B 1 199 ? 126.014 133.566 87.989  1.00 12746. ? 199 ILE B CA    1 
ATOM   5418  C  C     . ILE B 1 199 ? 125.782 134.993 88.464  1.00 12748. ? 199 ILE B C     1 
ATOM   5419  O  O     . ILE B 1 199 ? 124.692 135.309 88.962  1.00 12761. ? 199 ILE B O     1 
ATOM   5420  C  CB    . ILE B 1 199 ? 125.040 133.179 86.869  1.00 12759. ? 199 ILE B CB    1 
ATOM   5421  C  CG1   . ILE B 1 199 ? 125.288 131.738 86.426  1.00 12773. ? 199 ILE B CG1   1 
ATOM   5422  C  CG2   . ILE B 1 199 ? 125.190 134.121 85.695  1.00 12786. ? 199 ILE B CG2   1 
ATOM   5423  C  CD1   . ILE B 1 199 ? 124.158 130.798 86.752  1.00 12807. ? 199 ILE B CD1   1 
ATOM   5424  N  N     . PRO B 1 200 ? 126.762 135.882 88.328  1.00 12749. ? 200 PRO B N     1 
ATOM   5425  C  CA    . PRO B 1 200 ? 126.656 137.199 88.959  1.00 12744. ? 200 PRO B CA    1 
ATOM   5426  C  C     . PRO B 1 200 ? 125.804 138.167 88.159  1.00 12766. ? 200 PRO B C     1 
ATOM   5427  O  O     . PRO B 1 200 ? 125.828 138.186 86.926  1.00 12790. ? 200 PRO B O     1 
ATOM   5428  C  CB    . PRO B 1 200 ? 128.112 137.673 89.015  1.00 12748. ? 200 PRO B CB    1 
ATOM   5429  C  CG    . PRO B 1 200 ? 128.738 137.027 87.847  1.00 12773. ? 200 PRO B CG    1 
ATOM   5430  C  CD    . PRO B 1 200 ? 128.070 135.687 87.684  1.00 12785. ? 200 PRO B CD    1 
ATOM   5431  N  N     . TYR B 1 201 ? 125.041 138.978 88.886  1.00 13295. ? 201 TYR B N     1 
ATOM   5432  C  CA    . TYR B 1 201 ? 124.384 140.146 88.322  1.00 13322. ? 201 TYR B CA    1 
ATOM   5433  C  C     . TYR B 1 201 ? 125.191 141.415 88.525  1.00 13336. ? 201 TYR B C     1 
ATOM   5434  O  O     . TYR B 1 201 ? 125.061 142.356 87.736  1.00 13374. ? 201 TYR B O     1 
ATOM   5435  C  CB    . TYR B 1 201 ? 122.994 140.323 88.943  1.00 13325. ? 201 TYR B CB    1 
ATOM   5436  C  CG    . TYR B 1 201 ? 122.260 141.557 88.476  1.00 13334. ? 201 TYR B CG    1 
ATOM   5437  C  CD1   . TYR B 1 201 ? 121.825 141.675 87.165  1.00 13347. ? 201 TYR B CD1   1 
ATOM   5438  C  CD2   . TYR B 1 201 ? 122.002 142.604 89.348  1.00 13335. ? 201 TYR B CD2   1 
ATOM   5439  C  CE1   . TYR B 1 201 ? 121.153 142.800 86.736  1.00 13350. ? 201 TYR B CE1   1 
ATOM   5440  C  CE2   . TYR B 1 201 ? 121.332 143.734 88.928  1.00 13345. ? 201 TYR B CE2   1 
ATOM   5441  C  CZ    . TYR B 1 201 ? 120.910 143.826 87.621  1.00 13352. ? 201 TYR B CZ    1 
ATOM   5442  O  OH    . TYR B 1 201 ? 120.241 144.950 87.197  1.00 13354. ? 201 TYR B OH    1 
ATOM   5443  N  N     . GLU B 1 202 ? 126.033 141.451 89.557  1.00 13532. ? 202 GLU B N     1 
ATOM   5444  C  CA    . GLU B 1 202 ? 126.885 142.599 89.833  1.00 13545. ? 202 GLU B CA    1 
ATOM   5445  C  C     . GLU B 1 202 ? 127.976 142.167 90.799  1.00 13524. ? 202 GLU B C     1 
ATOM   5446  O  O     . GLU B 1 202 ? 127.678 141.621 91.865  1.00 13529. ? 202 GLU B O     1 
ATOM   5447  C  CB    . GLU B 1 202 ? 126.077 143.757 90.423  1.00 13569. ? 202 GLU B CB    1 
ATOM   5448  C  CG    . GLU B 1 202 ? 126.918 144.794 91.137  1.00 13570. ? 202 GLU B CG    1 
ATOM   5449  C  CD    . GLU B 1 202 ? 126.384 146.197 90.950  1.00 13583. ? 202 GLU B CD    1 
ATOM   5450  O  OE1   . GLU B 1 202 ? 125.324 146.512 91.530  1.00 13581. ? 202 GLU B OE1   1 
ATOM   5451  O  OE2   . GLU B 1 202 ? 127.024 146.984 90.222  1.00 13599. ? 202 GLU B OE2   1 
ATOM   5452  N  N     . ILE B 1 203 ? 129.230 142.410 90.428  1.00 12775. ? 203 ILE B N     1 
ATOM   5453  C  CA    . ILE B 1 203 ? 130.384 142.081 91.256  1.00 12755. ? 203 ILE B CA    1 
ATOM   5454  C  C     . ILE B 1 203 ? 130.958 143.375 91.811  1.00 12754. ? 203 ILE B C     1 
ATOM   5455  O  O     . ILE B 1 203 ? 131.184 144.332 91.062  1.00 12765. ? 203 ILE B O     1 
ATOM   5456  C  CB    . ILE B 1 203 ? 131.449 141.304 90.465  1.00 12744. ? 203 ILE B CB    1 
ATOM   5457  C  CG1   . ILE B 1 203 ? 130.818 140.113 89.748  1.00 12754. ? 203 ILE B CG1   1 
ATOM   5458  C  CG2   . ILE B 1 203 ? 132.553 140.835 91.389  1.00 12756. ? 203 ILE B CG2   1 
ATOM   5459  C  CD1   . ILE B 1 203 ? 131.798 139.321 88.921  1.00 12750. ? 203 ILE B CD1   1 
ATOM   5460  N  N     . THR B 1 204 ? 131.192 143.404 93.119  1.00 12752. ? 204 THR B N     1 
ATOM   5461  C  CA    . THR B 1 204 ? 131.697 144.583 93.806  1.00 12737. ? 204 THR B CA    1 
ATOM   5462  C  C     . THR B 1 204 ? 133.041 144.259 94.440  1.00 12734. ? 204 THR B C     1 
ATOM   5463  O  O     . THR B 1 204 ? 133.170 143.256 95.148  1.00 12751. ? 204 THR B O     1 
ATOM   5464  C  CB    . THR B 1 204 ? 130.707 145.063 94.873  1.00 12749. ? 204 THR B CB    1 
ATOM   5465  O  OG1   . THR B 1 204 ? 129.538 145.592 94.237  1.00 12760. ? 204 THR B OG1   1 
ATOM   5466  C  CG2   . THR B 1 204 ? 131.331 146.139 95.742  1.00 12751. ? 204 THR B CG2   1 
ATOM   5467  N  N     . LEU B 1 205 ? 134.036 145.104 94.182  1.00 12729. ? 205 LEU B N     1 
ATOM   5468  C  CA    . LEU B 1 205 ? 135.353 144.939 94.783  1.00 12735. ? 205 LEU B CA    1 
ATOM   5469  C  C     . LEU B 1 205 ? 135.344 145.520 96.191  1.00 12739. ? 205 LEU B C     1 
ATOM   5470  O  O     . LEU B 1 205 ? 135.161 146.729 96.368  1.00 12753. ? 205 LEU B O     1 
ATOM   5471  C  CB    . LEU B 1 205 ? 136.419 145.617 93.928  1.00 12748. ? 205 LEU B CB    1 
ATOM   5472  C  CG    . LEU B 1 205 ? 137.793 145.779 94.579  1.00 12750. ? 205 LEU B CG    1 
ATOM   5473  C  CD1   . LEU B 1 205 ? 138.400 144.423 94.886  1.00 12753. ? 205 LEU B CD1   1 
ATOM   5474  C  CD2   . LEU B 1 205 ? 138.714 146.590 93.690  1.00 12756. ? 205 LEU B CD2   1 
ATOM   5475  N  N     . LEU B 1 206 ? 135.541 144.662 97.190  1.00 12742. ? 206 LEU B N     1 
ATOM   5476  C  CA    . LEU B 1 206 ? 135.513 145.096 98.581  1.00 12743. ? 206 LEU B CA    1 
ATOM   5477  C  C     . LEU B 1 206 ? 136.888 145.504 99.091  1.00 12747. ? 206 LEU B C     1 
ATOM   5478  O  O     . LEU B 1 206 ? 137.011 146.512 99.795  1.00 12752. ? 206 LEU B O     1 
ATOM   5479  C  CB    . LEU B 1 206 ? 134.944 143.988 99.467  1.00 12748. ? 206 LEU B CB    1 
ATOM   5480  C  CG    . LEU B 1 206 ? 133.562 143.469 99.079  1.00 12743. ? 206 LEU B CG    1 
ATOM   5481  C  CD1   . LEU B 1 206 ? 133.123 142.364 100.017 1.00 12748. ? 206 LEU B CD1   1 
ATOM   5482  C  CD2   . LEU B 1 206 ? 132.562 144.604 99.080  1.00 12755. ? 206 LEU B CD2   1 
ATOM   5483  N  N     . SER B 1 207 ? 137.919 144.736 98.765  1.00 12754. ? 207 SER B N     1 
ATOM   5484  C  CA    . SER B 1 207 ? 139.266 145.059 99.219  1.00 12749. ? 207 SER B CA    1 
ATOM   5485  C  C     . SER B 1 207 ? 140.304 144.449 98.287  1.00 12749. ? 207 SER B C     1 
ATOM   5486  O  O     . SER B 1 207 ? 140.430 143.221 98.219  1.00 12760. ? 207 SER B O     1 
ATOM   5487  C  CB    . SER B 1 207 ? 139.478 144.566 100.650 1.00 12756. ? 207 SER B CB    1 
ATOM   5488  O  OG    . SER B 1 207 ? 140.812 144.777 101.067 1.00 12769. ? 207 SER B OG    1 
ATOM   5489  N  N     . PRO B 1 208 ? 141.067 145.261 97.563  1.00 12733. ? 208 PRO B N     1 
ATOM   5490  C  CA    . PRO B 1 208 ? 142.064 144.711 96.642  1.00 12737. ? 208 PRO B CA    1 
ATOM   5491  C  C     . PRO B 1 208 ? 143.241 144.095 97.380  1.00 12745. ? 208 PRO B C     1 
ATOM   5492  O  O     . PRO B 1 208 ? 143.530 144.414 98.535  1.00 12764. ? 208 PRO B O     1 
ATOM   5493  C  CB    . PRO B 1 208 ? 142.501 145.930 95.827  1.00 12744. ? 208 PRO B CB    1 
ATOM   5494  C  CG    . PRO B 1 208 ? 142.263 147.079 96.734  1.00 12745. ? 208 PRO B CG    1 
ATOM   5495  C  CD    . PRO B 1 208 ? 141.042 146.733 97.535  1.00 12737. ? 208 PRO B CD    1 
ATOM   5496  N  N     . CYS B 1 209 ? 143.924 143.188 96.687  1.00 12739. ? 209 CYS B N     1 
ATOM   5497  C  CA    . CYS B 1 209 ? 145.145 142.559 97.178  1.00 12742. ? 209 CYS B CA    1 
ATOM   5498  C  C     . CYS B 1 209 ? 146.310 143.111 96.366  1.00 12746. ? 209 CYS B C     1 
ATOM   5499  O  O     . CYS B 1 209 ? 146.453 142.791 95.182  1.00 12762. ? 209 CYS B O     1 
ATOM   5500  C  CB    . CYS B 1 209 ? 145.063 141.039 97.067  1.00 12745. ? 209 CYS B CB    1 
ATOM   5501  S  SG    . CYS B 1 209 ? 146.590 140.170 97.469  1.00 12741. ? 209 CYS B SG    1 
ATOM   5502  N  N     . LEU B 1 210 ? 147.138 143.938 97.003  1.00 12745. ? 210 LEU B N     1 
ATOM   5503  C  CA    . LEU B 1 210 ? 148.211 144.627 96.300  1.00 12742. ? 210 LEU B CA    1 
ATOM   5504  C  C     . LEU B 1 210 ? 149.454 143.771 96.108  1.00 12746. ? 210 LEU B C     1 
ATOM   5505  O  O     . LEU B 1 210 ? 150.309 144.131 95.293  1.00 12771. ? 210 LEU B O     1 
ATOM   5506  C  CB    . LEU B 1 210 ? 148.589 145.905 97.048  1.00 12744. ? 210 LEU B CB    1 
ATOM   5507  C  CG    . LEU B 1 210 ? 147.424 146.698 97.634  1.00 12730. ? 210 LEU B CG    1 
ATOM   5508  C  CD1   . LEU B 1 210 ? 147.931 147.714 98.632  1.00 12746. ? 210 LEU B CD1   1 
ATOM   5509  C  CD2   . LEU B 1 210 ? 146.641 147.377 96.533  1.00 12752. ? 210 LEU B CD2   1 
ATOM   5510  N  N     . HIS B 1 211 ? 149.577 142.660 96.821  1.00 12745. ? 211 HIS B N     1 
ATOM   5511  C  CA    . HIS B 1 211 ? 150.740 141.794 96.722  1.00 12762. ? 211 HIS B CA    1 
ATOM   5512  C  C     . HIS B 1 211 ? 150.423 140.596 95.841  1.00 12792. ? 211 HIS B C     1 
ATOM   5513  O  O     . HIS B 1 211 ? 149.277 140.147 95.765  1.00 12783. ? 211 HIS B O     1 
ATOM   5514  C  CB    . HIS B 1 211 ? 151.190 141.318 98.105  1.00 12757. ? 211 HIS B CB    1 
ATOM   5515  C  CG    . HIS B 1 211 ? 152.036 142.310 98.838  1.00 12737. ? 211 HIS B CG    1 
ATOM   5516  N  ND1   . HIS B 1 211 ? 151.858 142.595 100.174 1.00 12735. ? 211 HIS B ND1   1 
ATOM   5517  C  CD2   . HIS B 1 211 ? 153.065 143.083 98.421  1.00 12743. ? 211 HIS B CD2   1 
ATOM   5518  C  CE1   . HIS B 1 211 ? 152.741 143.503 100.549 1.00 12737. ? 211 HIS B CE1   1 
ATOM   5519  N  NE2   . HIS B 1 211 ? 153.486 143.815 99.504  1.00 12729. ? 211 HIS B NE2   1 
ATOM   5520  N  N     . MET B 1 212 ? 151.448 140.081 95.172  1.00 14085. ? 212 MET B N     1 
ATOM   5521  C  CA    . MET B 1 212 ? 151.283 138.897 94.341  1.00 14116. ? 212 MET B CA    1 
ATOM   5522  C  C     . MET B 1 212 ? 151.271 137.662 95.230  1.00 14123. ? 212 MET B C     1 
ATOM   5523  O  O     . MET B 1 212 ? 152.261 137.367 95.907  1.00 14133. ? 212 MET B O     1 
ATOM   5524  C  CB    . MET B 1 212 ? 152.395 138.802 93.300  1.00 14142. ? 212 MET B CB    1 
ATOM   5525  C  CG    . MET B 1 212 ? 151.987 138.031 92.053  1.00 14146. ? 212 MET B CG    1 
ATOM   5526  S  SD    . MET B 1 212 ? 153.287 137.898 90.812  1.00 14154. ? 212 MET B SD    1 
ATOM   5527  C  CE    . MET B 1 212 ? 154.750 138.020 91.833  1.00 14212. ? 212 MET B CE    1 
ATOM   5528  N  N     . LEU B 1 213 ? 150.151 136.948 95.231  1.00 13822. ? 213 LEU B N     1 
ATOM   5529  C  CA    . LEU B 1 213 ? 150.042 135.740 96.026  1.00 13835. ? 213 LEU B CA    1 
ATOM   5530  C  C     . LEU B 1 213 ? 150.982 134.667 95.479  1.00 13878. ? 213 LEU B C     1 
ATOM   5531  O  O     . LEU B 1 213 ? 151.324 134.678 94.294  1.00 13875. ? 213 LEU B O     1 
ATOM   5532  C  CB    . LEU B 1 213 ? 148.604 135.229 96.020  1.00 13825. ? 213 LEU B CB    1 
ATOM   5533  C  CG    . LEU B 1 213 ? 147.660 135.824 97.063  1.00 13804. ? 213 LEU B CG    1 
ATOM   5534  C  CD1   . LEU B 1 213 ? 146.416 134.967 97.194  1.00 13799. ? 213 LEU B CD1   1 
ATOM   5535  C  CD2   . LEU B 1 213 ? 148.356 135.956 98.402  1.00 13807. ? 213 LEU B CD2   1 
ATOM   5536  N  N     . PRO B 1 214 ? 151.426 133.740 96.326  1.00 15527. ? 214 PRO B N     1 
ATOM   5537  C  CA    . PRO B 1 214 ? 152.319 132.678 95.852  1.00 15609. ? 214 PRO B CA    1 
ATOM   5538  C  C     . PRO B 1 214 ? 151.662 131.833 94.772  1.00 15686. ? 214 PRO B C     1 
ATOM   5539  O  O     . PRO B 1 214 ? 150.440 131.815 94.610  1.00 15637. ? 214 PRO B O     1 
ATOM   5540  C  CB    . PRO B 1 214 ? 152.594 131.855 97.115  1.00 15633. ? 214 PRO B CB    1 
ATOM   5541  C  CG    . PRO B 1 214 ? 152.372 132.810 98.233  1.00 15566. ? 214 PRO B CG    1 
ATOM   5542  C  CD    . PRO B 1 214 ? 151.251 133.697 97.787  1.00 15535. ? 214 PRO B CD    1 
ATOM   5543  N  N     . HIS B 1 215 ? 152.505 131.125 94.023  1.00 19883. ? 215 HIS B N     1 
ATOM   5544  C  CA    . HIS B 1 215 ? 152.036 130.364 92.874  1.00 19970. ? 215 HIS B CA    1 
ATOM   5545  C  C     . HIS B 1 215 ? 151.077 129.262 93.307  1.00 19997. ? 215 HIS B C     1 
ATOM   5546  O  O     . HIS B 1 215 ? 151.146 128.748 94.426  1.00 20010. ? 215 HIS B O     1 
ATOM   5547  C  CB    . HIS B 1 215 ? 153.221 129.763 92.121  1.00 20023. ? 215 HIS B CB    1 
ATOM   5548  C  CG    . HIS B 1 215 ? 153.087 129.832 90.633  1.00 20031. ? 215 HIS B CG    1 
ATOM   5549  N  ND1   . HIS B 1 215 ? 153.014 131.025 89.947  1.00 20025. ? 215 HIS B ND1   1 
ATOM   5550  C  CD2   . HIS B 1 215 ? 153.015 128.856 89.697  1.00 20044. ? 215 HIS B CD2   1 
ATOM   5551  C  CE1   . HIS B 1 215 ? 152.901 130.781 88.654  1.00 20025. ? 215 HIS B CE1   1 
ATOM   5552  N  NE2   . HIS B 1 215 ? 152.900 129.472 88.475  1.00 20034. ? 215 HIS B NE2   1 
ATOM   5553  N  N     . LEU B 1 216 ? 150.163 128.909 92.399  1.00 19914. ? 216 LEU B N     1 
ATOM   5554  C  CA    . LEU B 1 216 ? 149.141 127.917 92.717  1.00 19933. ? 216 LEU B CA    1 
ATOM   5555  C  C     . LEU B 1 216 ? 149.760 126.565 93.050  1.00 19971. ? 216 LEU B C     1 
ATOM   5556  O  O     . LEU B 1 216 ? 149.357 125.910 94.018  1.00 19947. ? 216 LEU B O     1 
ATOM   5557  C  CB    . LEU B 1 216 ? 148.161 127.781 91.551  1.00 19934. ? 216 LEU B CB    1 
ATOM   5558  C  CG    . LEU B 1 216 ? 146.994 128.771 91.480  1.00 19872. ? 216 LEU B CG    1 
ATOM   5559  C  CD1   . LEU B 1 216 ? 146.282 128.869 92.821  1.00 19813. ? 216 LEU B CD1   1 
ATOM   5560  C  CD2   . LEU B 1 216 ? 147.458 130.142 91.009  1.00 19845. ? 216 LEU B CD2   1 
ATOM   5561  N  N     . HIS B 1 217 ? 150.742 126.131 92.261  1.00 21754. ? 217 HIS B N     1 
ATOM   5562  C  CA    . HIS B 1 217 ? 151.386 124.845 92.492  1.00 21783. ? 217 HIS B CA    1 
ATOM   5563  C  C     . HIS B 1 217 ? 152.520 124.920 93.504  1.00 21783. ? 217 HIS B C     1 
ATOM   5564  O  O     . HIS B 1 217 ? 153.061 123.875 93.880  1.00 21798. ? 217 HIS B O     1 
ATOM   5565  C  CB    . HIS B 1 217 ? 151.920 124.279 91.174  1.00 21800. ? 217 HIS B CB    1 
ATOM   5566  C  CG    . HIS B 1 217 ? 150.862 124.056 90.139  1.00 21802. ? 217 HIS B CG    1 
ATOM   5567  N  ND1   . HIS B 1 217 ? 149.897 123.079 90.260  1.00 21797. ? 217 HIS B ND1   1 
ATOM   5568  C  CD2   . HIS B 1 217 ? 150.617 124.682 88.964  1.00 21811. ? 217 HIS B CD2   1 
ATOM   5569  C  CE1   . HIS B 1 217 ? 149.103 123.114 89.205  1.00 21807. ? 217 HIS B CE1   1 
ATOM   5570  N  NE2   . HIS B 1 217 ? 149.519 124.078 88.403  1.00 21814. ? 217 HIS B NE2   1 
ATOM   5571  N  N     . PHE B 1 218 ? 152.888 126.116 93.952  1.00 21410. ? 218 PHE B N     1 
ATOM   5572  C  CA    . PHE B 1 218 ? 154.005 126.325 94.867  1.00 21407. ? 218 PHE B CA    1 
ATOM   5573  C  C     . PHE B 1 218 ? 153.555 127.127 96.079  1.00 21365. ? 218 PHE B C     1 
ATOM   5574  O  O     . PHE B 1 218 ? 154.169 128.124 96.464  1.00 21356. ? 218 PHE B O     1 
ATOM   5575  C  CB    . PHE B 1 218 ? 155.167 127.014 94.158  1.00 21415. ? 218 PHE B CB    1 
ATOM   5576  C  CG    . PHE B 1 218 ? 155.523 126.393 92.838  1.00 21427. ? 218 PHE B CG    1 
ATOM   5577  C  CD1   . PHE B 1 218 ? 155.802 125.039 92.748  1.00 21433. ? 218 PHE B CD1   1 
ATOM   5578  C  CD2   . PHE B 1 218 ? 155.579 127.161 91.688  1.00 21423. ? 218 PHE B CD2   1 
ATOM   5579  C  CE1   . PHE B 1 218 ? 156.128 124.464 91.535  1.00 21434. ? 218 PHE B CE1   1 
ATOM   5580  C  CE2   . PHE B 1 218 ? 155.905 126.592 90.472  1.00 21425. ? 218 PHE B CE2   1 
ATOM   5581  C  CZ    . PHE B 1 218 ? 156.180 125.241 90.396  1.00 21431. ? 218 PHE B CZ    1 
ATOM   5582  N  N     . GLY B 1 219 ? 152.455 126.700 96.690  1.00 19209. ? 219 GLY B N     1 
ATOM   5583  C  CA    . GLY B 1 219 ? 151.943 127.364 97.873  1.00 19126. ? 219 GLY B CA    1 
ATOM   5584  C  C     . GLY B 1 219 ? 152.931 127.337 99.026  1.00 19050. ? 219 GLY B C     1 
ATOM   5585  O  O     . GLY B 1 219 ? 154.019 126.767 98.958  1.00 19082. ? 219 GLY B O     1 
ATOM   5586  N  N     . LEU B 1 220 ? 152.525 127.982 100.119 1.00 15371. ? 220 LEU B N     1 
ATOM   5587  C  CA    . LEU B 1 220 ? 153.387 128.134 101.285 1.00 15319. ? 220 LEU B CA    1 
ATOM   5588  C  C     . LEU B 1 220 ? 153.826 126.786 101.840 1.00 15325. ? 220 LEU B C     1 
ATOM   5589  O  O     . LEU B 1 220 ? 153.004 126.013 102.341 1.00 15301. ? 220 LEU B O     1 
ATOM   5590  C  CB    . LEU B 1 220 ? 152.679 128.943 102.372 1.00 15258. ? 220 LEU B CB    1 
ATOM   5591  C  CG    . LEU B 1 220 ? 153.041 130.426 102.458 1.00 15248. ? 220 LEU B CG    1 
ATOM   5592  C  CD1   . LEU B 1 220 ? 152.857 130.934 103.874 1.00 15200. ? 220 LEU B CD1   1 
ATOM   5593  C  CD2   . LEU B 1 220 ? 154.466 130.666 101.983 1.00 15282. ? 220 LEU B CD2   1 
ATOM   5594  N  N     . LYS B 1 221 ? 155.123 126.498 101.749 1.00 16522. ? 221 LYS B N     1 
ATOM   5595  C  CA    . LYS B 1 221 ? 155.690 125.274 102.298 1.00 16535. ? 221 LYS B CA    1 
ATOM   5596  C  C     . LYS B 1 221 ? 156.873 125.503 103.224 1.00 16521. ? 221 LYS B C     1 
ATOM   5597  O  O     . LYS B 1 221 ? 157.233 124.581 103.965 1.00 16534. ? 221 LYS B O     1 
ATOM   5598  C  CB    . LYS B 1 221 ? 156.126 124.327 101.170 1.00 16560. ? 221 LYS B CB    1 
ATOM   5599  C  CG    . LYS B 1 221 ? 154.991 123.515 100.575 1.00 16569. ? 221 LYS B CG    1 
ATOM   5600  C  CD    . LYS B 1 221 ? 154.425 122.534 101.587 1.00 16572. ? 221 LYS B CD    1 
ATOM   5601  C  CE    . LYS B 1 221 ? 155.502 121.603 102.120 1.00 16576. ? 221 LYS B CE    1 
ATOM   5602  N  NZ    . LYS B 1 221 ? 156.278 120.966 101.021 1.00 16577. ? 221 LYS B NZ    1 
ATOM   5603  N  N     . ASP B 1 222 ? 157.488 126.683 103.211 1.00 15847. ? 222 ASP B N     1 
ATOM   5604  C  CA    . ASP B 1 222 ? 158.586 126.972 104.124 1.00 15835. ? 222 ASP B CA    1 
ATOM   5605  C  C     . ASP B 1 222 ? 158.037 127.172 105.530 1.00 15788. ? 222 ASP B C     1 
ATOM   5606  O  O     . ASP B 1 222 ? 157.148 128.002 105.743 1.00 15769. ? 222 ASP B O     1 
ATOM   5607  C  CB    . ASP B 1 222 ? 159.346 128.210 103.659 1.00 15830. ? 222 ASP B CB    1 
ATOM   5608  C  CG    . ASP B 1 222 ? 160.526 128.537 104.549 1.00 15829. ? 222 ASP B CG    1 
ATOM   5609  O  OD1   . ASP B 1 222 ? 161.055 127.614 105.204 1.00 15833. ? 222 ASP B OD1   1 
ATOM   5610  O  OD2   . ASP B 1 222 ? 160.927 129.719 104.594 1.00 15835. ? 222 ASP B OD2   1 
ATOM   5611  N  N     . LYS B 1 223 ? 158.569 126.412 106.490 1.00 15030. ? 223 LYS B N     1 
ATOM   5612  C  CA    . LYS B 1 223 ? 158.053 126.476 107.853 1.00 15000. ? 223 LYS B CA    1 
ATOM   5613  C  C     . LYS B 1 223 ? 158.241 127.862 108.454 1.00 14981. ? 223 LYS B C     1 
ATOM   5614  O  O     . LYS B 1 223 ? 157.336 128.390 109.112 1.00 14945. ? 223 LYS B O     1 
ATOM   5615  C  CB    . LYS B 1 223 ? 158.734 125.419 108.720 1.00 14992. ? 223 LYS B CB    1 
ATOM   5616  C  CG    . LYS B 1 223 ? 158.390 123.991 108.340 1.00 14992. ? 223 LYS B CG    1 
ATOM   5617  C  CD    . LYS B 1 223 ? 156.969 123.642 108.746 1.00 14959. ? 223 LYS B CD    1 
ATOM   5618  C  CE    . LYS B 1 223 ? 156.839 122.168 109.089 1.00 14937. ? 223 LYS B CE    1 
ATOM   5619  N  NZ    . LYS B 1 223 ? 156.595 121.335 107.881 1.00 15004. ? 223 LYS B NZ    1 
ATOM   5620  N  N     . GLU B 1 224 ? 159.411 128.468 108.239 1.00 15648. ? 224 GLU B N     1 
ATOM   5621  C  CA    . GLU B 1 224 ? 159.664 129.796 108.787 1.00 15631. ? 224 GLU B CA    1 
ATOM   5622  C  C     . GLU B 1 224 ? 158.700 130.823 108.208 1.00 15602. ? 224 GLU B C     1 
ATOM   5623  O  O     . GLU B 1 224 ? 158.140 131.644 108.944 1.00 15578. ? 224 GLU B O     1 
ATOM   5624  C  CB    . GLU B 1 224 ? 161.111 130.204 108.518 1.00 15669. ? 224 GLU B CB    1 
ATOM   5625  C  CG    . GLU B 1 224 ? 161.512 131.526 109.145 1.00 15627. ? 224 GLU B CG    1 
ATOM   5626  C  CD    . GLU B 1 224 ? 162.251 131.346 110.457 1.00 15653. ? 224 GLU B CD    1 
ATOM   5627  O  OE1   . GLU B 1 224 ? 162.747 130.229 110.711 1.00 15676. ? 224 GLU B OE1   1 
ATOM   5628  O  OE2   . GLU B 1 224 ? 162.337 132.320 111.233 1.00 15587. ? 224 GLU B OE2   1 
ATOM   5629  N  N     . THR B 1 225 ? 158.486 130.784 106.891 1.00 14215. ? 225 THR B N     1 
ATOM   5630  C  CA    . THR B 1 225 ? 157.556 131.718 106.265 1.00 14164. ? 225 THR B CA    1 
ATOM   5631  C  C     . THR B 1 225 ? 156.134 131.493 106.759 1.00 14116. ? 225 THR B C     1 
ATOM   5632  O  O     . THR B 1 225 ? 155.394 132.453 107.001 1.00 14108. ? 225 THR B O     1 
ATOM   5633  C  CB    . THR B 1 225 ? 157.619 131.581 104.745 1.00 14167. ? 225 THR B CB    1 
ATOM   5634  O  OG1   . THR B 1 225 ? 158.985 131.630 104.316 1.00 14192. ? 225 THR B OG1   1 
ATOM   5635  C  CG2   . THR B 1 225 ? 156.845 132.705 104.080 1.00 14147. ? 225 THR B CG2   1 
ATOM   5636  N  N     . ARG B 1 226 ? 155.733 130.229 106.908 1.00 13268. ? 226 ARG B N     1 
ATOM   5637  C  CA    . ARG B 1 226 ? 154.388 129.928 107.384 1.00 13217. ? 226 ARG B CA    1 
ATOM   5638  C  C     . ARG B 1 226 ? 154.176 130.438 108.802 1.00 13207. ? 226 ARG B C     1 
ATOM   5639  O  O     . ARG B 1 226 ? 153.109 130.972 109.125 1.00 13195. ? 226 ARG B O     1 
ATOM   5640  C  CB    . ARG B 1 226 ? 154.134 128.425 107.318 1.00 13218. ? 226 ARG B CB    1 
ATOM   5641  C  CG    . ARG B 1 226 ? 153.981 127.874 105.916 1.00 13270. ? 226 ARG B CG    1 
ATOM   5642  C  CD    . ARG B 1 226 ? 153.418 126.471 105.970 1.00 13253. ? 226 ARG B CD    1 
ATOM   5643  N  NE    . ARG B 1 226 ? 152.675 126.257 107.204 1.00 13176. ? 226 ARG B NE    1 
ATOM   5644  C  CZ    . ARG B 1 226 ? 152.656 125.117 107.880 1.00 13133. ? 226 ARG B CZ    1 
ATOM   5645  N  NH1   . ARG B 1 226 ? 153.328 124.057 107.464 1.00 13147. ? 226 ARG B NH1   1 
ATOM   5646  N  NH2   . ARG B 1 226 ? 151.945 125.040 109.001 1.00 13096. ? 226 ARG B NH2   1 
ATOM   5647  N  N     . TYR B 1 227 ? 155.177 130.274 109.668 1.00 12897. ? 227 TYR B N     1 
ATOM   5648  C  CA    . TYR B 1 227 ? 155.020 130.701 111.054 1.00 12816. ? 227 TYR B CA    1 
ATOM   5649  C  C     . TYR B 1 227 ? 155.098 132.214 111.194 1.00 12845. ? 227 TYR B C     1 
ATOM   5650  O  O     . TYR B 1 227 ? 154.412 132.790 112.045 1.00 12761. ? 227 TYR B O     1 
ATOM   5651  C  CB    . TYR B 1 227 ? 156.071 130.028 111.935 1.00 12750. ? 227 TYR B CB    1 
ATOM   5652  C  CG    . TYR B 1 227 ? 155.996 128.520 111.926 1.00 12702. ? 227 TYR B CG    1 
ATOM   5653  C  CD1   . TYR B 1 227 ? 154.802 127.868 111.658 1.00 12715. ? 227 TYR B CD1   1 
ATOM   5654  C  CD2   . TYR B 1 227 ? 157.118 127.748 112.185 1.00 12715. ? 227 TYR B CD2   1 
ATOM   5655  C  CE1   . TYR B 1 227 ? 154.727 126.493 111.645 1.00 12636. ? 227 TYR B CE1   1 
ATOM   5656  C  CE2   . TYR B 1 227 ? 157.053 126.371 112.175 1.00 12715. ? 227 TYR B CE2   1 
ATOM   5657  C  CZ    . TYR B 1 227 ? 155.855 125.749 111.905 1.00 12593. ? 227 TYR B CZ    1 
ATOM   5658  O  OH    . TYR B 1 227 ? 155.783 124.377 111.894 1.00 12567. ? 227 TYR B OH    1 
ATOM   5659  N  N     . ARG B 1 228 ? 155.922 132.876 110.378 1.00 14191. ? 228 ARG B N     1 
ATOM   5660  C  CA    . ARG B 1 228 ? 156.040 134.326 110.483 1.00 14222. ? 228 ARG B CA    1 
ATOM   5661  C  C     . ARG B 1 228 ? 154.818 135.029 109.903 1.00 14199. ? 228 ARG B C     1 
ATOM   5662  O  O     . ARG B 1 228 ? 154.331 136.010 110.475 1.00 14228. ? 228 ARG B O     1 
ATOM   5663  C  CB    . ARG B 1 228 ? 157.315 134.799 109.789 1.00 14257. ? 228 ARG B CB    1 
ATOM   5664  C  CG    . ARG B 1 228 ? 158.583 134.371 110.502 1.00 14233. ? 228 ARG B CG    1 
ATOM   5665  C  CD    . ARG B 1 228 ? 159.791 135.138 110.004 1.00 14275. ? 228 ARG B CD    1 
ATOM   5666  N  NE    . ARG B 1 228 ? 161.007 134.730 110.696 1.00 14194. ? 228 ARG B NE    1 
ATOM   5667  C  CZ    . ARG B 1 228 ? 161.362 135.155 111.900 1.00 14108. ? 228 ARG B CZ    1 
ATOM   5668  N  NH1   . ARG B 1 228 ? 160.616 136.010 112.579 1.00 14115. ? 228 ARG B NH1   1 
ATOM   5669  N  NH2   . ARG B 1 228 ? 162.495 134.711 112.436 1.00 13986. ? 228 ARG B NH2   1 
ATOM   5670  N  N     . GLN B 1 229 ? 154.309 134.545 108.775 1.00 12823. ? 229 GLN B N     1 
ATOM   5671  C  CA    . GLN B 1 229 ? 153.136 135.117 108.117 1.00 12773. ? 229 GLN B CA    1 
ATOM   5672  C  C     . GLN B 1 229 ? 151.998 134.108 108.234 1.00 12769. ? 229 GLN B C     1 
ATOM   5673  O  O     . GLN B 1 229 ? 151.790 133.280 107.348 1.00 12779. ? 229 GLN B O     1 
ATOM   5674  C  CB    . GLN B 1 229 ? 153.437 135.455 106.664 1.00 12752. ? 229 GLN B CB    1 
ATOM   5675  C  CG    . GLN B 1 229 ? 154.165 136.770 106.474 1.00 12756. ? 229 GLN B CG    1 
ATOM   5676  C  CD    . GLN B 1 229 ? 154.708 136.935 105.072 1.00 12754. ? 229 GLN B CD    1 
ATOM   5677  O  OE1   . GLN B 1 229 ? 155.053 135.959 104.409 1.00 12760. ? 229 GLN B OE1   1 
ATOM   5678  N  NE2   . GLN B 1 229 ? 154.785 138.176 104.611 1.00 12762. ? 229 GLN B NE2   1 
ATOM   5679  N  N     . ARG B 1 230 ? 151.257 134.188 109.340 1.00 12760. ? 230 ARG B N     1 
ATOM   5680  C  CA    . ARG B 1 230 ? 150.179 133.234 109.572 1.00 12741. ? 230 ARG B CA    1 
ATOM   5681  C  C     . ARG B 1 230 ? 148.986 133.492 108.661 1.00 12740. ? 230 ARG B C     1 
ATOM   5682  O  O     . ARG B 1 230 ? 148.257 132.553 108.320 1.00 12752. ? 230 ARG B O     1 
ATOM   5683  C  CB    . ARG B 1 230 ? 149.749 133.276 111.037 1.00 12634. ? 230 ARG B CB    1 
ATOM   5684  C  CG    . ARG B 1 230 ? 148.848 132.126 111.454 1.00 12623. ? 230 ARG B CG    1 
ATOM   5685  C  CD    . ARG B 1 230 ? 149.484 130.783 111.144 1.00 12694. ? 230 ARG B CD    1 
ATOM   5686  N  NE    . ARG B 1 230 ? 149.997 130.132 112.343 1.00 12577. ? 230 ARG B NE    1 
ATOM   5687  C  CZ    . ARG B 1 230 ? 150.615 128.960 112.350 1.00 12581. ? 230 ARG B CZ    1 
ATOM   5688  N  NH1   . ARG B 1 230 ? 150.816 128.278 111.236 1.00 12702. ? 230 ARG B NH1   1 
ATOM   5689  N  NH2   . ARG B 1 230 ? 151.043 128.461 113.505 1.00 12363. ? 230 ARG B NH2   1 
ATOM   5690  N  N     . TYR B 1 231 ? 148.763 134.747 108.265 1.00 12733. ? 231 TYR B N     1 
ATOM   5691  C  CA    . TYR B 1 231 ? 147.641 135.048 107.381 1.00 12736. ? 231 TYR B CA    1 
ATOM   5692  C  C     . TYR B 1 231 ? 147.813 134.379 106.024 1.00 12751. ? 231 TYR B C     1 
ATOM   5693  O  O     . TYR B 1 231 ? 146.850 133.849 105.459 1.00 12781. ? 231 TYR B O     1 
ATOM   5694  C  CB    . TYR B 1 231 ? 147.479 136.560 107.224 1.00 12733. ? 231 TYR B CB    1 
ATOM   5695  C  CG    . TYR B 1 231 ? 148.767 137.317 107.000 1.00 12729. ? 231 TYR B CG    1 
ATOM   5696  C  CD1   . TYR B 1 231 ? 149.517 137.782 108.070 1.00 12741. ? 231 TYR B CD1   1 
ATOM   5697  C  CD2   . TYR B 1 231 ? 149.223 137.581 105.718 1.00 12748. ? 231 TYR B CD2   1 
ATOM   5698  C  CE1   . TYR B 1 231 ? 150.689 138.476 107.869 1.00 12754. ? 231 TYR B CE1   1 
ATOM   5699  C  CE2   . TYR B 1 231 ? 150.394 138.274 105.509 1.00 12753. ? 231 TYR B CE2   1 
ATOM   5700  C  CZ    . TYR B 1 231 ? 151.122 138.720 106.587 1.00 12749. ? 231 TYR B CZ    1 
ATOM   5701  O  OH    . TYR B 1 231 ? 152.291 139.413 106.382 1.00 12763. ? 231 TYR B OH    1 
ATOM   5702  N  N     . LEU B 1 232 ? 149.034 134.387 105.487 1.00 12743. ? 232 LEU B N     1 
ATOM   5703  C  CA    . LEU B 1 232 ? 149.294 133.679 104.238 1.00 12741. ? 232 LEU B CA    1 
ATOM   5704  C  C     . LEU B 1 232 ? 149.084 132.181 104.404 1.00 12748. ? 232 LEU B C     1 
ATOM   5705  O  O     . LEU B 1 232 ? 148.575 131.513 103.496 1.00 12772. ? 232 LEU B O     1 
ATOM   5706  C  CB    . LEU B 1 232 ? 150.712 133.968 103.755 1.00 12743. ? 232 LEU B CB    1 
ATOM   5707  C  CG    . LEU B 1 232 ? 150.888 135.231 102.918 1.00 12746. ? 232 LEU B CG    1 
ATOM   5708  C  CD1   . LEU B 1 232 ? 152.303 135.307 102.380 1.00 12759. ? 232 LEU B CD1   1 
ATOM   5709  C  CD2   . LEU B 1 232 ? 149.879 135.255 101.789 1.00 12762. ? 232 LEU B CD2   1 
ATOM   5710  N  N     . ASP B 1 233 ? 149.484 131.635 105.553 1.00 12741. ? 233 ASP B N     1 
ATOM   5711  C  CA    . ASP B 1 233 ? 149.260 130.220 105.820 1.00 12748. ? 233 ASP B CA    1 
ATOM   5712  C  C     . ASP B 1 233 ? 147.775 129.892 105.825 1.00 12753. ? 233 ASP B C     1 
ATOM   5713  O  O     . ASP B 1 233 ? 147.352 128.877 105.259 1.00 12763. ? 233 ASP B O     1 
ATOM   5714  C  CB    . ASP B 1 233 ? 149.897 129.836 107.154 1.00 12761. ? 233 ASP B CB    1 
ATOM   5715  C  CG    . ASP B 1 233 ? 150.193 128.358 107.252 1.00 12774. ? 233 ASP B CG    1 
ATOM   5716  O  OD1   . ASP B 1 233 ? 150.260 127.695 106.198 1.00 12789. ? 233 ASP B OD1   1 
ATOM   5717  O  OD2   . ASP B 1 233 ? 150.360 127.858 108.384 1.00 12783. ? 233 ASP B OD2   1 
ATOM   5718  N  N     . LEU B 1 234 ? 146.966 130.742 106.458 1.00 12751. ? 234 LEU B N     1 
ATOM   5719  C  CA    . LEU B 1 234 ? 145.523 130.529 106.463 1.00 12745. ? 234 LEU B CA    1 
ATOM   5720  C  C     . LEU B 1 234 ? 144.943 130.645 105.060 1.00 12757. ? 234 LEU B C     1 
ATOM   5721  O  O     . LEU B 1 234 ? 144.057 129.870 104.682 1.00 12775. ? 234 LEU B O     1 
ATOM   5722  C  CB    . LEU B 1 234 ? 144.851 131.525 107.405 1.00 12738. ? 234 LEU B CB    1 
ATOM   5723  C  CG    . LEU B 1 234 ? 145.062 131.287 108.898 1.00 12737. ? 234 LEU B CG    1 
ATOM   5724  C  CD1   . LEU B 1 234 ? 144.466 132.422 109.704 1.00 12752. ? 234 LEU B CD1   1 
ATOM   5725  C  CD2   . LEU B 1 234 ? 144.450 129.964 109.308 1.00 12745. ? 234 LEU B CD2   1 
ATOM   5726  N  N     . ILE B 1 235 ? 145.424 131.612 104.278 1.00 12752. ? 235 ILE B N     1 
ATOM   5727  C  CA    . ILE B 1 235 ? 144.890 131.825 102.935 1.00 12730. ? 235 ILE B CA    1 
ATOM   5728  C  C     . ILE B 1 235 ? 145.186 130.624 102.046 1.00 12740. ? 235 ILE B C     1 
ATOM   5729  O  O     . ILE B 1 235 ? 144.302 130.111 101.349 1.00 12751. ? 235 ILE B O     1 
ATOM   5730  C  CB    . ILE B 1 235 ? 145.460 133.121 102.333 1.00 12721. ? 235 ILE B CB    1 
ATOM   5731  C  CG1   . ILE B 1 235 ? 144.765 134.340 102.932 1.00 12728. ? 235 ILE B CG1   1 
ATOM   5732  C  CG2   . ILE B 1 235 ? 145.314 133.121 100.825 1.00 12746. ? 235 ILE B CG2   1 
ATOM   5733  C  CD1   . ILE B 1 235 ? 145.520 135.625 102.720 1.00 12747. ? 235 ILE B CD1   1 
ATOM   5734  N  N     . LEU B 1 236 ? 146.429 130.148 102.065 1.00 12740. ? 236 LEU B N     1 
ATOM   5735  C  CA    . LEU B 1 236 ? 146.853 129.126 101.115 1.00 12731. ? 236 LEU B CA    1 
ATOM   5736  C  C     . LEU B 1 236 ? 146.644 127.708 101.631 1.00 12760. ? 236 LEU B C     1 
ATOM   5737  O  O     . LEU B 1 236 ? 146.229 126.831 100.867 1.00 12755. ? 236 LEU B O     1 
ATOM   5738  C  CB    . LEU B 1 236 ? 148.323 129.334 100.750 1.00 12744. ? 236 LEU B CB    1 
ATOM   5739  C  CG    . LEU B 1 236 ? 148.634 130.669 100.076 1.00 12751. ? 236 LEU B CG    1 
ATOM   5740  C  CD1   . LEU B 1 236 ? 150.003 131.166 100.490 1.00 12797. ? 236 LEU B CD1   1 
ATOM   5741  C  CD2   . LEU B 1 236 ? 148.543 130.540 98.568  1.00 12785. ? 236 LEU B CD2   1 
ATOM   5742  N  N     . ASN B 1 237 ? 146.925 127.459 102.906 1.00 13138. ? 237 ASN B N     1 
ATOM   5743  C  CA    . ASN B 1 237 ? 146.807 126.129 103.487 1.00 13165. ? 237 ASN B CA    1 
ATOM   5744  C  C     . ASN B 1 237 ? 145.518 126.034 104.289 1.00 13193. ? 237 ASN B C     1 
ATOM   5745  O  O     . ASN B 1 237 ? 145.230 126.904 105.118 1.00 13171. ? 237 ASN B O     1 
ATOM   5746  C  CB    . ASN B 1 237 ? 148.013 125.815 104.372 1.00 13161. ? 237 ASN B CB    1 
ATOM   5747  C  CG    . ASN B 1 237 ? 149.329 125.990 103.642 1.00 13167. ? 237 ASN B CG    1 
ATOM   5748  O  OD1   . ASN B 1 237 ? 149.662 125.214 102.747 1.00 13170. ? 237 ASN B OD1   1 
ATOM   5749  N  ND2   . ASN B 1 237 ? 150.083 127.013 104.018 1.00 13185. ? 237 ASN B ND2   1 
ATOM   5750  N  N     . ASP B 1 238 ? 144.748 124.975 104.043 1.00 14542. ? 238 ASP B N     1 
ATOM   5751  C  CA    . ASP B 1 238 ? 143.435 124.822 104.657 1.00 14583. ? 238 ASP B CA    1 
ATOM   5752  C  C     . ASP B 1 238 ? 143.462 124.052 105.969 1.00 14544. ? 238 ASP B C     1 
ATOM   5753  O  O     . ASP B 1 238 ? 142.550 124.223 106.786 1.00 14543. ? 238 ASP B O     1 
ATOM   5754  C  CB    . ASP B 1 238 ? 142.483 124.120 103.685 1.00 14607. ? 238 ASP B CB    1 
ATOM   5755  C  CG    . ASP B 1 238 ? 143.159 123.004 102.916 1.00 14605. ? 238 ASP B CG    1 
ATOM   5756  O  OD1   . ASP B 1 238 ? 144.380 122.814 103.095 1.00 14594. ? 238 ASP B OD1   1 
ATOM   5757  O  OD2   . ASP B 1 238 ? 142.470 122.317 102.133 1.00 14619. ? 238 ASP B OD2   1 
ATOM   5758  N  N     . PHE B 1 239 ? 144.473 123.211 106.195 1.00 13257. ? 239 PHE B N     1 
ATOM   5759  C  CA    . PHE B 1 239 ? 144.515 122.417 107.416 1.00 13221. ? 239 PHE B CA    1 
ATOM   5760  C  C     . PHE B 1 239 ? 144.813 123.257 108.650 1.00 13190. ? 239 PHE B C     1 
ATOM   5761  O  O     . PHE B 1 239 ? 144.532 122.813 109.768 1.00 13199. ? 239 PHE B O     1 
ATOM   5762  C  CB    . PHE B 1 239 ? 145.552 121.301 107.283 1.00 13209. ? 239 PHE B CB    1 
ATOM   5763  C  CG    . PHE B 1 239 ? 146.907 121.777 106.845 1.00 13183. ? 239 PHE B CG    1 
ATOM   5764  C  CD1   . PHE B 1 239 ? 147.840 122.203 107.774 1.00 13176. ? 239 PHE B CD1   1 
ATOM   5765  C  CD2   . PHE B 1 239 ? 147.253 121.786 105.506 1.00 13197. ? 239 PHE B CD2   1 
ATOM   5766  C  CE1   . PHE B 1 239 ? 149.087 122.638 107.376 1.00 13195. ? 239 PHE B CE1   1 
ATOM   5767  C  CE2   . PHE B 1 239 ? 148.499 122.219 105.102 1.00 13199. ? 239 PHE B CE2   1 
ATOM   5768  C  CZ    . PHE B 1 239 ? 149.417 122.645 106.038 1.00 13202. ? 239 PHE B CZ    1 
ATOM   5769  N  N     . VAL B 1 240 ? 145.378 124.452 108.474 1.00 12779. ? 240 VAL B N     1 
ATOM   5770  C  CA    . VAL B 1 240 ? 145.685 125.315 109.611 1.00 12769. ? 240 VAL B CA    1 
ATOM   5771  C  C     . VAL B 1 240 ? 144.406 125.723 110.332 1.00 12753. ? 240 VAL B C     1 
ATOM   5772  O  O     . VAL B 1 240 ? 144.338 125.728 111.573 1.00 12762. ? 240 VAL B O     1 
ATOM   5773  C  CB    . VAL B 1 240 ? 146.485 126.539 109.131 1.00 12755. ? 240 VAL B CB    1 
ATOM   5774  C  CG1   . VAL B 1 240 ? 147.181 127.207 110.287 1.00 12754. ? 240 VAL B CG1   1 
ATOM   5775  C  CG2   . VAL B 1 240 ? 147.487 126.127 108.070 1.00 12771. ? 240 VAL B CG2   1 
ATOM   5776  N  N     . ARG B 1 241 ? 143.375 126.076 109.564 1.00 12734. ? 241 ARG B N     1 
ATOM   5777  C  CA    . ARG B 1 241 ? 142.094 126.432 110.157 1.00 12740. ? 241 ARG B CA    1 
ATOM   5778  C  C     . ARG B 1 241 ? 141.512 125.264 110.938 1.00 12754. ? 241 ARG B C     1 
ATOM   5779  O  O     . ARG B 1 241 ? 140.956 125.452 112.025 1.00 12777. ? 241 ARG B O     1 
ATOM   5780  C  CB    . ARG B 1 241 ? 141.126 126.889 109.067 1.00 12757. ? 241 ARG B CB    1 
ATOM   5781  C  CG    . ARG B 1 241 ? 139.750 127.260 109.575 1.00 12751. ? 241 ARG B CG    1 
ATOM   5782  C  CD    . ARG B 1 241 ? 138.748 127.330 108.440 1.00 12745. ? 241 ARG B CD    1 
ATOM   5783  N  NE    . ARG B 1 241 ? 137.899 128.508 108.548 1.00 12749. ? 241 ARG B NE    1 
ATOM   5784  C  CZ    . ARG B 1 241 ? 138.106 129.639 107.889 1.00 12760. ? 241 ARG B CZ    1 
ATOM   5785  N  NH1   . ARG B 1 241 ? 139.124 129.777 107.056 1.00 12746. ? 241 ARG B NH1   1 
ATOM   5786  N  NH2   . ARG B 1 241 ? 137.271 130.658 108.072 1.00 12761. ? 241 ARG B NH2   1 
ATOM   5787  N  N     . GLN B 1 242 ? 141.634 124.048 110.402 1.00 12748. ? 242 GLN B N     1 
ATOM   5788  C  CA    . GLN B 1 242 ? 141.151 122.875 111.120 1.00 12743. ? 242 GLN B CA    1 
ATOM   5789  C  C     . GLN B 1 242 ? 141.930 122.656 112.409 1.00 12745. ? 242 GLN B C     1 
ATOM   5790  O  O     . GLN B 1 242 ? 141.350 122.291 113.438 1.00 12761. ? 242 GLN B O     1 
ATOM   5791  C  CB    . GLN B 1 242 ? 141.231 121.641 110.224 1.00 12749. ? 242 GLN B CB    1 
ATOM   5792  C  CG    . GLN B 1 242 ? 140.467 121.784 108.923 1.00 12753. ? 242 GLN B CG    1 
ATOM   5793  C  CD    . GLN B 1 242 ? 139.014 122.154 109.140 1.00 12745. ? 242 GLN B CD    1 
ATOM   5794  O  OE1   . GLN B 1 242 ? 138.359 121.641 110.048 1.00 12754. ? 242 GLN B OE1   1 
ATOM   5795  N  NE2   . GLN B 1 242 ? 138.501 123.051 108.308 1.00 12745. ? 242 GLN B NE2   1 
ATOM   5796  N  N     . LYS B 1 243 ? 143.247 122.875 112.376 1.00 12736. ? 243 LYS B N     1 
ATOM   5797  C  CA    . LYS B 1 243 ? 144.053 122.738 113.585 1.00 12693. ? 243 LYS B CA    1 
ATOM   5798  C  C     . LYS B 1 243 ? 143.570 123.688 114.672 1.00 12723. ? 243 LYS B C     1 
ATOM   5799  O  O     . LYS B 1 243 ? 143.384 123.295 115.832 1.00 12740. ? 243 LYS B O     1 
ATOM   5800  C  CB    . LYS B 1 243 ? 145.524 123.005 113.267 1.00 12667. ? 243 LYS B CB    1 
ATOM   5801  C  CG    . LYS B 1 243 ? 146.229 121.883 112.531 1.00 12666. ? 243 LYS B CG    1 
ATOM   5802  C  CD    . LYS B 1 243 ? 147.735 122.058 112.595 1.00 12601. ? 243 LYS B CD    1 
ATOM   5803  C  CE    . LYS B 1 243 ? 148.447 121.147 111.613 1.00 12619. ? 243 LYS B CE    1 
ATOM   5804  N  NZ    . LYS B 1 243 ? 148.169 119.712 111.881 1.00 12524. ? 243 LYS B NZ    1 
ATOM   5805  N  N     . PHE B 1 244 ? 143.346 124.949 114.309 1.00 12734. ? 244 PHE B N     1 
ATOM   5806  C  CA    . PHE B 1 244 ? 142.948 125.917 115.326 1.00 12733. ? 244 PHE B CA    1 
ATOM   5807  C  C     . PHE B 1 244 ? 141.506 125.708 115.775 1.00 12731. ? 244 PHE B C     1 
ATOM   5808  O  O     . PHE B 1 244 ? 141.179 125.956 116.943 1.00 12751. ? 244 PHE B O     1 
ATOM   5809  C  CB    . PHE B 1 244 ? 143.191 127.329 114.810 1.00 12724. ? 244 PHE B CB    1 
ATOM   5810  C  CG    . PHE B 1 244 ? 144.646 127.667 114.706 1.00 12702. ? 244 PHE B CG    1 
ATOM   5811  C  CD1   . PHE B 1 244 ? 145.462 127.579 115.819 1.00 12585. ? 244 PHE B CD1   1 
ATOM   5812  C  CD2   . PHE B 1 244 ? 145.206 128.036 113.500 1.00 12702. ? 244 PHE B CD2   1 
ATOM   5813  C  CE1   . PHE B 1 244 ? 146.802 127.869 115.735 1.00 12426. ? 244 PHE B CE1   1 
ATOM   5814  C  CE2   . PHE B 1 244 ? 146.550 128.330 113.415 1.00 12613. ? 244 PHE B CE2   1 
ATOM   5815  C  CZ    . PHE B 1 244 ? 147.347 128.244 114.532 1.00 12410. ? 244 PHE B CZ    1 
ATOM   5816  N  N     . ILE B 1 245 ? 140.645 125.213 114.885 1.00 12731. ? 245 ILE B N     1 
ATOM   5817  C  CA    . ILE B 1 245 ? 139.293 124.839 115.289 1.00 12735. ? 245 ILE B CA    1 
ATOM   5818  C  C     . ILE B 1 245 ? 139.338 123.702 116.301 1.00 12745. ? 245 ILE B C     1 
ATOM   5819  O  O     . ILE B 1 245 ? 138.593 123.700 117.287 1.00 12761. ? 245 ILE B O     1 
ATOM   5820  C  CB    . ILE B 1 245 ? 138.454 124.468 114.053 1.00 12723. ? 245 ILE B CB    1 
ATOM   5821  C  CG1   . ILE B 1 245 ? 138.026 125.728 113.305 1.00 12670. ? 245 ILE B CG1   1 
ATOM   5822  C  CG2   . ILE B 1 245 ? 137.238 123.651 114.449 1.00 12709. ? 245 ILE B CG2   1 
ATOM   5823  C  CD1   . ILE B 1 245 ? 137.458 125.450 111.939 1.00 12674. ? 245 ILE B CD1   1 
ATOM   5824  N  N     . ILE B 1 246 ? 140.213 122.721 116.076 1.00 12740. ? 246 ILE B N     1 
ATOM   5825  C  CA    . ILE B 1 246 ? 140.344 121.610 117.014 1.00 12729. ? 246 ILE B CA    1 
ATOM   5826  C  C     . ILE B 1 246 ? 140.869 122.098 118.358 1.00 12725. ? 246 ILE B C     1 
ATOM   5827  O  O     . ILE B 1 246 ? 140.435 121.628 119.415 1.00 12752. ? 246 ILE B O     1 
ATOM   5828  C  CB    . ILE B 1 246 ? 141.240 120.512 116.415 1.00 12709. ? 246 ILE B CB    1 
ATOM   5829  C  CG1   . ILE B 1 246 ? 140.501 119.781 115.296 1.00 12726. ? 246 ILE B CG1   1 
ATOM   5830  C  CG2   . ILE B 1 246 ? 141.669 119.526 117.483 1.00 12633. ? 246 ILE B CG2   1 
ATOM   5831  C  CD1   . ILE B 1 246 ? 141.367 118.815 114.527 1.00 12674. ? 246 ILE B CD1   1 
ATOM   5832  N  N     . ARG B 1 247 ? 141.816 123.037 118.346 1.00 12725. ? 247 ARG B N     1 
ATOM   5833  C  CA    . ARG B 1 247 ? 142.310 123.596 119.604 1.00 12720. ? 247 ARG B CA    1 
ATOM   5834  C  C     . ARG B 1 247 ? 141.191 124.296 120.373 1.00 12742. ? 247 ARG B C     1 
ATOM   5835  O  O     . ARG B 1 247 ? 141.041 124.120 121.595 1.00 12771. ? 247 ARG B O     1 
ATOM   5836  C  CB    . ARG B 1 247 ? 143.461 124.560 119.326 1.00 12730. ? 247 ARG B CB    1 
ATOM   5837  C  CG    . ARG B 1 247 ? 144.078 125.160 120.570 1.00 12706. ? 247 ARG B CG    1 
ATOM   5838  C  CD    . ARG B 1 247 ? 145.057 126.260 120.217 1.00 12686. ? 247 ARG B CD    1 
ATOM   5839  N  NE    . ARG B 1 247 ? 145.410 127.059 121.383 1.00 12696. ? 247 ARG B NE    1 
ATOM   5840  C  CZ    . ARG B 1 247 ? 146.487 126.856 122.128 1.00 12672. ? 247 ARG B CZ    1 
ATOM   5841  N  NH1   . ARG B 1 247 ? 147.348 125.892 121.850 1.00 12505. ? 247 ARG B NH1   1 
ATOM   5842  N  NH2   . ARG B 1 247 ? 146.705 127.639 123.180 1.00 12667. ? 247 ARG B NH2   1 
ATOM   5843  N  N     . SER B 1 248 ? 140.387 125.095 119.665 1.00 12736. ? 248 SER B N     1 
ATOM   5844  C  CA    . SER B 1 248 ? 139.249 125.750 120.300 1.00 12709. ? 248 SER B CA    1 
ATOM   5845  C  C     . SER B 1 248 ? 138.266 124.728 120.855 1.00 12694. ? 248 SER B C     1 
ATOM   5846  O  O     . SER B 1 248 ? 137.717 124.911 121.948 1.00 12695. ? 248 SER B O     1 
ATOM   5847  C  CB    . SER B 1 248 ? 138.556 126.673 119.302 1.00 12693. ? 248 SER B CB    1 
ATOM   5848  O  OG    . SER B 1 248 ? 137.745 127.622 119.967 1.00 12685. ? 248 SER B OG    1 
ATOM   5849  N  N     . LYS B 1 249 ? 138.030 123.646 120.110 1.00 12696. ? 249 LYS B N     1 
ATOM   5850  C  CA    . LYS B 1 249 ? 137.146 122.588 120.584 1.00 12683. ? 249 LYS B CA    1 
ATOM   5851  C  C     . LYS B 1 249 ? 137.687 121.945 121.851 1.00 12726. ? 249 LYS B C     1 
ATOM   5852  O  O     . LYS B 1 249 ? 136.923 121.627 122.766 1.00 12745. ? 249 LYS B O     1 
ATOM   5853  C  CB    . LYS B 1 249 ? 136.960 121.532 119.497 1.00 12719. ? 249 LYS B CB    1 
ATOM   5854  C  CG    . LYS B 1 249 ? 135.904 121.864 118.465 1.00 12638. ? 249 LYS B CG    1 
ATOM   5855  C  CD    . LYS B 1 249 ? 135.928 120.851 117.339 1.00 12701. ? 249 LYS B CD    1 
ATOM   5856  C  CE    . LYS B 1 249 ? 134.672 120.925 116.498 1.00 12666. ? 249 LYS B CE    1 
ATOM   5857  N  NZ    . LYS B 1 249 ? 134.559 119.753 115.590 1.00 12723. ? 249 LYS B NZ    1 
ATOM   5858  N  N     . ILE B 1 250 ? 139.001 121.728 121.911 1.00 12753. ? 250 ILE B N     1 
ATOM   5859  C  CA    . ILE B 1 250 ? 139.616 121.149 123.104 1.00 12736. ? 250 ILE B CA    1 
ATOM   5860  C  C     . ILE B 1 250 ? 139.344 122.030 124.314 1.00 12736. ? 250 ILE B C     1 
ATOM   5861  O  O     . ILE B 1 250 ? 138.893 121.559 125.369 1.00 12755. ? 250 ILE B O     1 
ATOM   5862  C  CB    . ILE B 1 250 ? 141.129 120.960 122.887 1.00 12716. ? 250 ILE B CB    1 
ATOM   5863  C  CG1   . ILE B 1 250 ? 141.407 119.765 121.980 1.00 12687. ? 250 ILE B CG1   1 
ATOM   5864  C  CG2   . ILE B 1 250 ? 141.845 120.797 124.215 1.00 12672. ? 250 ILE B CG2   1 
ATOM   5865  C  CD1   . ILE B 1 250 ? 142.777 119.789 121.362 1.00 12548. ? 250 ILE B CD1   1 
ATOM   5866  N  N     . ILE B 1 251 ? 139.614 123.328 124.174 1.00 12744. ? 251 ILE B N     1 
ATOM   5867  C  CA    . ILE B 1 251 ? 139.433 124.230 125.309 1.00 12727. ? 251 ILE B CA    1 
ATOM   5868  C  C     . ILE B 1 251 ? 137.965 124.292 125.718 1.00 12734. ? 251 ILE B C     1 
ATOM   5869  O  O     . ILE B 1 251 ? 137.636 124.270 126.912 1.00 12753. ? 251 ILE B O     1 
ATOM   5870  C  CB    . ILE B 1 251 ? 139.998 125.622 124.983 1.00 12728. ? 251 ILE B CB    1 
ATOM   5871  C  CG1   . ILE B 1 251 ? 141.502 125.524 124.722 1.00 12706. ? 251 ILE B CG1   1 
ATOM   5872  C  CG2   . ILE B 1 251 ? 139.714 126.584 126.117 1.00 12733. ? 251 ILE B CG2   1 
ATOM   5873  C  CD1   . ILE B 1 251 ? 142.260 126.801 124.981 1.00 12720. ? 251 ILE B CD1   1 
ATOM   5874  N  N     . THR B 1 252 ? 137.060 124.362 124.739 1.00 12732. ? 252 THR B N     1 
ATOM   5875  C  CA    . THR B 1 252 ? 135.636 124.428 125.050 1.00 12713. ? 252 THR B CA    1 
ATOM   5876  C  C     . THR B 1 252 ? 135.156 123.157 125.737 1.00 12725. ? 252 THR B C     1 
ATOM   5877  O  O     . THR B 1 252 ? 134.333 123.215 126.657 1.00 12740. ? 252 THR B O     1 
ATOM   5878  C  CB    . THR B 1 252 ? 134.833 124.682 123.777 1.00 12622. ? 252 THR B CB    1 
ATOM   5879  O  OG1   . THR B 1 252 ? 135.508 125.658 122.976 1.00 12635. ? 252 THR B OG1   1 
ATOM   5880  C  CG2   . THR B 1 252 ? 133.448 125.190 124.120 1.00 12635. ? 252 THR B CG2   1 
ATOM   5881  N  N     . TYR B 1 253 ? 135.649 121.996 125.299 1.00 12728. ? 253 TYR B N     1 
ATOM   5882  C  CA    . TYR B 1 253 ? 135.273 120.744 125.944 1.00 12710. ? 253 TYR B CA    1 
ATOM   5883  C  C     . TYR B 1 253 ? 135.744 120.710 127.389 1.00 12728. ? 253 TYR B C     1 
ATOM   5884  O  O     . TYR B 1 253 ? 135.005 120.271 128.276 1.00 12734. ? 253 TYR B O     1 
ATOM   5885  C  CB    . TYR B 1 253 ? 135.846 119.556 125.173 1.00 12724. ? 253 TYR B CB    1 
ATOM   5886  C  CG    . TYR B 1 253 ? 135.455 118.214 125.748 1.00 12730. ? 253 TYR B CG    1 
ATOM   5887  C  CD1   . TYR B 1 253 ? 136.196 117.627 126.764 1.00 12744. ? 253 TYR B CD1   1 
ATOM   5888  C  CD2   . TYR B 1 253 ? 134.345 117.534 125.276 1.00 12668. ? 253 TYR B CD2   1 
ATOM   5889  C  CE1   . TYR B 1 253 ? 135.840 116.408 127.293 1.00 12747. ? 253 TYR B CE1   1 
ATOM   5890  C  CE2   . TYR B 1 253 ? 133.983 116.312 125.798 1.00 12617. ? 253 TYR B CE2   1 
ATOM   5891  C  CZ    . TYR B 1 253 ? 134.734 115.754 126.806 1.00 12662. ? 253 TYR B CZ    1 
ATOM   5892  O  OH    . TYR B 1 253 ? 134.376 114.535 127.330 1.00 12666. ? 253 TYR B OH    1 
ATOM   5893  N  N     . ILE B 1 254 ? 136.976 121.154 127.643 1.00 12740. ? 254 ILE B N     1 
ATOM   5894  C  CA    . ILE B 1 254 ? 137.475 121.176 129.017 1.00 12735. ? 254 ILE B CA    1 
ATOM   5895  C  C     . ILE B 1 254 ? 136.607 122.085 129.877 1.00 12731. ? 254 ILE B C     1 
ATOM   5896  O  O     . ILE B 1 254 ? 136.215 121.732 130.999 1.00 12754. ? 254 ILE B O     1 
ATOM   5897  C  CB    . ILE B 1 254 ? 138.949 121.614 129.049 1.00 12744. ? 254 ILE B CB    1 
ATOM   5898  C  CG1   . ILE B 1 254 ? 139.849 120.493 128.539 1.00 12741. ? 254 ILE B CG1   1 
ATOM   5899  C  CG2   . ILE B 1 254 ? 139.353 122.008 130.453 1.00 12751. ? 254 ILE B CG2   1 
ATOM   5900  C  CD1   . ILE B 1 254 ? 141.285 120.910 128.358 1.00 12675. ? 254 ILE B CD1   1 
ATOM   5901  N  N     . ARG B 1 255 ? 136.291 123.273 129.355 1.00 12728. ? 255 ARG B N     1 
ATOM   5902  C  CA    . ARG B 1 255 ? 135.479 124.219 130.112 1.00 12723. ? 255 ARG B CA    1 
ATOM   5903  C  C     . ARG B 1 255 ? 134.100 123.650 130.407 1.00 12740. ? 255 ARG B C     1 
ATOM   5904  O  O     . ARG B 1 255 ? 133.601 123.772 131.530 1.00 12756. ? 255 ARG B O     1 
ATOM   5905  C  CB    . ARG B 1 255 ? 135.362 125.534 129.348 1.00 12728. ? 255 ARG B CB    1 
ATOM   5906  C  CG    . ARG B 1 255 ? 136.158 126.664 129.956 1.00 12743. ? 255 ARG B CG    1 
ATOM   5907  C  CD    . ARG B 1 255 ? 135.889 127.970 129.246 1.00 12743. ? 255 ARG B CD    1 
ATOM   5908  N  NE    . ARG B 1 255 ? 137.123 128.670 128.920 1.00 12745. ? 255 ARG B NE    1 
ATOM   5909  C  CZ    . ARG B 1 255 ? 137.564 128.867 127.686 1.00 12743. ? 255 ARG B CZ    1 
ATOM   5910  N  NH1   . ARG B 1 255 ? 136.892 128.432 126.635 1.00 12745. ? 255 ARG B NH1   1 
ATOM   5911  N  NH2   . ARG B 1 255 ? 138.709 129.518 127.504 1.00 12755. ? 255 ARG B NH2   1 
ATOM   5912  N  N     . SER B 1 256 ? 133.473 123.018 129.414 1.00 12745. ? 256 SER B N     1 
ATOM   5913  C  CA    . SER B 1 256 ? 132.147 122.443 129.615 1.00 12736. ? 256 SER B CA    1 
ATOM   5914  C  C     . SER B 1 256 ? 132.181 121.303 130.624 1.00 12716. ? 256 SER B C     1 
ATOM   5915  O  O     . SER B 1 256 ? 131.299 121.201 131.484 1.00 12716. ? 256 SER B O     1 
ATOM   5916  C  CB    . SER B 1 256 ? 131.582 121.960 128.282 1.00 12685. ? 256 SER B CB    1 
ATOM   5917  O  OG    . SER B 1 256 ? 130.171 121.878 128.330 1.00 12682. ? 256 SER B OG    1 
ATOM   5918  N  N     . PHE B 1 257 ? 133.190 120.435 130.530 1.00 12690. ? 257 PHE B N     1 
ATOM   5919  C  CA    . PHE B 1 257 ? 133.326 119.331 131.474 1.00 12654. ? 257 PHE B CA    1 
ATOM   5920  C  C     . PHE B 1 257 ? 133.431 119.845 132.903 1.00 12672. ? 257 PHE B C     1 
ATOM   5921  O  O     . PHE B 1 257 ? 132.680 119.418 133.791 1.00 12674. ? 257 PHE B O     1 
ATOM   5922  C  CB    . PHE B 1 257 ? 134.555 118.498 131.102 1.00 12678. ? 257 PHE B CB    1 
ATOM   5923  C  CG    . PHE B 1 257 ? 134.657 117.189 131.829 1.00 12651. ? 257 PHE B CG    1 
ATOM   5924  C  CD1   . PHE B 1 257 ? 135.318 117.103 133.040 1.00 12708. ? 257 PHE B CD1   1 
ATOM   5925  C  CD2   . PHE B 1 257 ? 134.109 116.040 131.290 1.00 12638. ? 257 PHE B CD2   1 
ATOM   5926  C  CE1   . PHE B 1 257 ? 135.418 115.901 133.706 1.00 12685. ? 257 PHE B CE1   1 
ATOM   5927  C  CE2   . PHE B 1 257 ? 134.206 114.837 131.952 1.00 12635. ? 257 PHE B CE2   1 
ATOM   5928  C  CZ    . PHE B 1 257 ? 134.861 114.767 133.161 1.00 12666. ? 257 PHE B CZ    1 
ATOM   5929  N  N     . LEU B 1 258 ? 134.342 120.791 133.138 1.00 12719. ? 258 LEU B N     1 
ATOM   5930  C  CA    . LEU B 1 258 ? 134.528 121.286 134.496 1.00 12727. ? 258 LEU B CA    1 
ATOM   5931  C  C     . LEU B 1 258 ? 133.326 122.087 134.980 1.00 12742. ? 258 LEU B C     1 
ATOM   5932  O  O     . LEU B 1 258 ? 132.988 122.028 136.167 1.00 12767. ? 258 LEU B O     1 
ATOM   5933  C  CB    . LEU B 1 258 ? 135.803 122.119 134.582 1.00 12751. ? 258 LEU B CB    1 
ATOM   5934  C  CG    . LEU B 1 258 ? 137.077 121.274 134.563 1.00 12744. ? 258 LEU B CG    1 
ATOM   5935  C  CD1   . LEU B 1 258 ? 138.301 122.131 134.805 1.00 12758. ? 258 LEU B CD1   1 
ATOM   5936  C  CD2   . LEU B 1 258 ? 136.990 120.157 135.585 1.00 12755. ? 258 LEU B CD2   1 
ATOM   5937  N  N     . ASP B 1 259 ? 132.668 122.835 134.091 1.00 12739. ? 259 ASP B N     1 
ATOM   5938  C  CA    . ASP B 1 259 ? 131.480 123.580 134.487 1.00 12731. ? 259 ASP B CA    1 
ATOM   5939  C  C     . ASP B 1 259 ? 130.351 122.645 134.893 1.00 12706. ? 259 ASP B C     1 
ATOM   5940  O  O     . ASP B 1 259 ? 129.663 122.890 135.889 1.00 12661. ? 259 ASP B O     1 
ATOM   5941  C  CB    . ASP B 1 259 ? 131.031 124.492 133.348 1.00 12725. ? 259 ASP B CB    1 
ATOM   5942  C  CG    . ASP B 1 259 ? 131.782 125.804 133.322 1.00 12705. ? 259 ASP B CG    1 
ATOM   5943  O  OD1   . ASP B 1 259 ? 132.336 126.193 134.370 1.00 12714. ? 259 ASP B OD1   1 
ATOM   5944  O  OD2   . ASP B 1 259 ? 131.816 126.451 132.255 1.00 12717. ? 259 ASP B OD2   1 
ATOM   5945  N  N     . GLU B 1 260 ? 130.142 121.569 134.132 1.00 12738. ? 260 GLU B N     1 
ATOM   5946  C  CA    . GLU B 1 260 ? 129.096 120.618 134.486 1.00 12659. ? 260 GLU B CA    1 
ATOM   5947  C  C     . GLU B 1 260 ? 129.448 119.840 135.744 1.00 12673. ? 260 GLU B C     1 
ATOM   5948  O  O     . GLU B 1 260 ? 128.548 119.389 136.460 1.00 12645. ? 260 GLU B O     1 
ATOM   5949  C  CB    . GLU B 1 260 ? 128.840 119.661 133.326 1.00 12659. ? 260 GLU B CB    1 
ATOM   5950  C  CG    . GLU B 1 260 ? 127.371 119.397 133.047 1.00 12681. ? 260 GLU B CG    1 
ATOM   5951  C  CD    . GLU B 1 260 ? 126.685 120.566 132.367 1.00 12734. ? 260 GLU B CD    1 
ATOM   5952  O  OE1   . GLU B 1 260 ? 127.077 120.909 131.232 1.00 12767. ? 260 GLU B OE1   1 
ATOM   5953  O  OE2   . GLU B 1 260 ? 125.751 121.139 132.965 1.00 12687. ? 260 GLU B OE2   1 
ATOM   5954  N  N     . LEU B 1 261 ? 130.740 119.665 136.030 1.00 12696. ? 261 LEU B N     1 
ATOM   5955  C  CA    . LEU B 1 261 ? 131.125 119.009 137.275 1.00 12702. ? 261 LEU B CA    1 
ATOM   5956  C  C     . LEU B 1 261 ? 130.780 119.840 138.504 1.00 12706. ? 261 LEU B C     1 
ATOM   5957  O  O     . LEU B 1 261 ? 130.664 119.281 139.598 1.00 12633. ? 261 LEU B O     1 
ATOM   5958  C  CB    . LEU B 1 261 ? 132.620 118.698 137.272 1.00 12719. ? 261 LEU B CB    1 
ATOM   5959  C  CG    . LEU B 1 261 ? 132.991 117.230 137.075 1.00 12645. ? 261 LEU B CG    1 
ATOM   5960  C  CD1   . LEU B 1 261 ? 134.449 116.999 137.421 1.00 12714. ? 261 LEU B CD1   1 
ATOM   5961  C  CD2   . LEU B 1 261 ? 132.092 116.338 137.907 1.00 12655. ? 261 LEU B CD2   1 
ATOM   5962  N  N     . GLY B 1 262 ? 130.615 121.150 138.353 1.00 12684. ? 262 GLY B N     1 
ATOM   5963  C  CA    . GLY B 1 262 ? 130.336 122.028 139.468 1.00 12576. ? 262 GLY B CA    1 
ATOM   5964  C  C     . GLY B 1 262 ? 131.432 123.014 139.807 1.00 12640. ? 262 GLY B C     1 
ATOM   5965  O  O     . GLY B 1 262 ? 131.370 123.635 140.873 1.00 12606. ? 262 GLY B O     1 
ATOM   5966  N  N     . PHE B 1 263 ? 132.425 123.182 138.941 1.00 12731. ? 263 PHE B N     1 
ATOM   5967  C  CA    . PHE B 1 263 ? 133.539 124.072 139.213 1.00 12731. ? 263 PHE B CA    1 
ATOM   5968  C  C     . PHE B 1 263 ? 133.164 125.519 138.914 1.00 12693. ? 263 PHE B C     1 
ATOM   5969  O  O     . PHE B 1 263 ? 132.167 125.810 138.251 1.00 12674. ? 263 PHE B O     1 
ATOM   5970  C  CB    . PHE B 1 263 ? 134.758 123.672 138.385 1.00 12737. ? 263 PHE B CB    1 
ATOM   5971  C  CG    . PHE B 1 263 ? 135.444 122.437 138.878 1.00 12727. ? 263 PHE B CG    1 
ATOM   5972  C  CD1   . PHE B 1 263 ? 134.879 121.191 138.687 1.00 12739. ? 263 PHE B CD1   1 
ATOM   5973  C  CD2   . PHE B 1 263 ? 136.656 122.521 139.532 1.00 12737. ? 263 PHE B CD2   1 
ATOM   5974  C  CE1   . PHE B 1 263 ? 135.509 120.057 139.138 1.00 12751. ? 263 PHE B CE1   1 
ATOM   5975  C  CE2   . PHE B 1 263 ? 137.286 121.391 139.988 1.00 12756. ? 263 PHE B CE2   1 
ATOM   5976  C  CZ    . PHE B 1 263 ? 136.714 120.158 139.790 1.00 12759. ? 263 PHE B CZ    1 
ATOM   5977  N  N     . LEU B 1 264 ? 133.989 126.433 139.416 1.00 12699. ? 264 LEU B N     1 
ATOM   5978  C  CA    . LEU B 1 264 ? 133.824 127.863 139.191 1.00 12703. ? 264 LEU B CA    1 
ATOM   5979  C  C     . LEU B 1 264 ? 135.080 128.400 138.525 1.00 12731. ? 264 LEU B C     1 
ATOM   5980  O  O     . LEU B 1 264 ? 136.174 128.303 139.090 1.00 12745. ? 264 LEU B O     1 
ATOM   5981  C  CB    . LEU B 1 264 ? 133.561 128.599 140.505 1.00 12678. ? 264 LEU B CB    1 
ATOM   5982  C  CG    . LEU B 1 264 ? 133.458 130.121 140.414 1.00 12711. ? 264 LEU B CG    1 
ATOM   5983  C  CD1   . LEU B 1 264 ? 132.088 130.532 139.918 1.00 12659. ? 264 LEU B CD1   1 
ATOM   5984  C  CD2   . LEU B 1 264 ? 133.750 130.751 141.758 1.00 12721. ? 264 LEU B CD2   1 
ATOM   5985  N  N     . GLU B 1 265 ? 134.924 128.968 137.334 1.00 12729. ? 265 GLU B N     1 
ATOM   5986  C  CA    . GLU B 1 265 ? 136.061 129.545 136.633 1.00 12728. ? 265 GLU B CA    1 
ATOM   5987  C  C     . GLU B 1 265 ? 136.489 130.838 137.310 1.00 12722. ? 265 GLU B C     1 
ATOM   5988  O  O     . GLU B 1 265 ? 135.652 131.674 137.661 1.00 12739. ? 265 GLU B O     1 
ATOM   5989  C  CB    . GLU B 1 265 ? 135.709 129.805 135.172 1.00 12745. ? 265 GLU B CB    1 
ATOM   5990  C  CG    . GLU B 1 265 ? 136.919 129.972 134.273 1.00 12748. ? 265 GLU B CG    1 
ATOM   5991  C  CD    . GLU B 1 265 ? 136.561 130.536 132.917 1.00 12744. ? 265 GLU B CD    1 
ATOM   5992  O  OE1   . GLU B 1 265 ? 135.371 130.483 132.545 1.00 12744. ? 265 GLU B OE1   1 
ATOM   5993  O  OE2   . GLU B 1 265 ? 137.472 131.030 132.221 1.00 12755. ? 265 GLU B OE2   1 
ATOM   5994  N  N     . ILE B 1 266 ? 137.798 131.005 137.492 1.00 12714. ? 266 ILE B N     1 
ATOM   5995  C  CA    . ILE B 1 266 ? 138.352 132.159 138.183 1.00 12724. ? 266 ILE B CA    1 
ATOM   5996  C  C     . ILE B 1 266 ? 139.444 132.778 137.322 1.00 12730. ? 266 ILE B C     1 
ATOM   5997  O  O     . ILE B 1 266 ? 139.811 132.259 136.269 1.00 12738. ? 266 ILE B O     1 
ATOM   5998  C  CB    . ILE B 1 266 ? 138.911 131.797 139.572 1.00 12731. ? 266 ILE B CB    1 
ATOM   5999  C  CG1   . ILE B 1 266 ? 139.922 130.659 139.448 1.00 12753. ? 266 ILE B CG1   1 
ATOM   6000  C  CG2   . ILE B 1 266 ? 137.786 131.431 140.522 1.00 12745. ? 266 ILE B CG2   1 
ATOM   6001  C  CD1   . ILE B 1 266 ? 140.791 130.484 140.661 1.00 12760. ? 266 ILE B CD1   1 
ATOM   6002  N  N     . GLU B 1 267 ? 139.958 133.911 137.793 1.00 12737. ? 267 GLU B N     1 
ATOM   6003  C  CA    . GLU B 1 267 ? 141.072 134.595 137.150 1.00 12747. ? 267 GLU B CA    1 
ATOM   6004  C  C     . GLU B 1 267 ? 142.033 135.055 138.232 1.00 12749. ? 267 GLU B C     1 
ATOM   6005  O  O     . GLU B 1 267 ? 141.648 135.817 139.123 1.00 12756. ? 267 GLU B O     1 
ATOM   6006  C  CB    . GLU B 1 267 ? 140.592 135.783 136.316 1.00 12752. ? 267 GLU B CB    1 
ATOM   6007  C  CG    . GLU B 1 267 ? 140.175 135.411 134.911 1.00 12753. ? 267 GLU B CG    1 
ATOM   6008  C  CD    . GLU B 1 267 ? 139.475 136.543 134.195 1.00 12759. ? 267 GLU B CD    1 
ATOM   6009  O  OE1   . GLU B 1 267 ? 139.780 136.768 133.006 1.00 12761. ? 267 GLU B OE1   1 
ATOM   6010  O  OE2   . GLU B 1 267 ? 138.625 137.209 134.820 1.00 12765. ? 267 GLU B OE2   1 
ATOM   6011  N  N     . THR B 1 268 ? 143.272 134.600 138.152 1.00 12745. ? 268 THR B N     1 
ATOM   6012  C  CA    . THR B 1 268 ? 144.292 134.886 139.142 1.00 12739. ? 268 THR B CA    1 
ATOM   6013  C  C     . THR B 1 268 ? 145.312 135.871 138.586 1.00 12742. ? 268 THR B C     1 
ATOM   6014  O  O     . THR B 1 268 ? 145.500 135.962 137.369 1.00 12748. ? 268 THR B O     1 
ATOM   6015  C  CB    . THR B 1 268 ? 144.992 133.589 139.567 1.00 12748. ? 268 THR B CB    1 
ATOM   6016  O  OG1   . THR B 1 268 ? 145.181 132.754 138.420 1.00 12759. ? 268 THR B OG1   1 
ATOM   6017  C  CG2   . THR B 1 268 ? 144.132 132.846 140.566 1.00 12760. ? 268 THR B CG2   1 
ATOM   6018  N  N     . PRO B 1 269 ? 145.978 136.641 139.448 1.00 12731. ? 269 PRO B N     1 
ATOM   6019  C  CA    . PRO B 1 269 ? 146.898 137.672 138.955 1.00 12736. ? 269 PRO B CA    1 
ATOM   6020  C  C     . PRO B 1 269 ? 148.013 137.088 138.104 1.00 12744. ? 269 PRO B C     1 
ATOM   6021  O  O     . PRO B 1 269 ? 148.542 136.011 138.383 1.00 12756. ? 269 PRO B O     1 
ATOM   6022  C  CB    . PRO B 1 269 ? 147.452 138.288 140.243 1.00 12742. ? 269 PRO B CB    1 
ATOM   6023  C  CG    . PRO B 1 269 ? 146.375 138.064 141.232 1.00 12743. ? 269 PRO B CG    1 
ATOM   6024  C  CD    . PRO B 1 269 ? 145.863 136.691 140.915 1.00 12747. ? 269 PRO B CD    1 
ATOM   6025  N  N     . MET B 1 270 ? 148.368 137.822 137.051 1.00 12737. ? 270 MET B N     1 
ATOM   6026  C  CA    . MET B 1 270 ? 149.473 137.451 136.183 1.00 12733. ? 270 MET B CA    1 
ATOM   6027  C  C     . MET B 1 270 ? 150.792 138.076 136.609 1.00 12740. ? 270 MET B C     1 
ATOM   6028  O  O     . MET B 1 270 ? 151.838 137.712 136.065 1.00 12760. ? 270 MET B O     1 
ATOM   6029  C  CB    . MET B 1 270 ? 149.162 137.837 134.733 1.00 12743. ? 270 MET B CB    1 
ATOM   6030  C  CG    . MET B 1 270 ? 148.813 136.658 133.846 1.00 12747. ? 270 MET B CG    1 
ATOM   6031  S  SD    . MET B 1 270 ? 147.688 137.088 132.512 1.00 12754. ? 270 MET B SD    1 
ATOM   6032  C  CE    . MET B 1 270 ? 146.822 135.541 132.282 1.00 12756. ? 270 MET B CE    1 
ATOM   6033  N  N     . MET B 1 271 ? 150.738 139.014 137.559 1.00 12732. ? 271 MET B N     1 
ATOM   6034  C  CA    . MET B 1 271 ? 151.978 139.643 138.086 1.00 12742. ? 271 MET B CA    1 
ATOM   6035  C  C     . MET B 1 271 ? 152.085 139.314 139.582 1.00 12748. ? 271 MET B C     1 
ATOM   6036  O  O     . MET B 1 271 ? 151.195 139.748 140.345 1.00 12750. ? 271 MET B O     1 
ATOM   6037  C  CB    . MET B 1 271 ? 151.961 141.161 137.874 1.00 12741. ? 271 MET B CB    1 
ATOM   6038  C  CG    . MET B 1 271 ? 151.869 141.573 136.418 1.00 12741. ? 271 MET B CG    1 
ATOM   6039  S  SD    . MET B 1 271 ? 151.999 143.355 136.174 1.00 12716. ? 271 MET B SD    1 
ATOM   6040  C  CE    . MET B 1 271 ? 150.597 143.927 137.143 1.00 12752. ? 271 MET B CE    1 
ATOM   6041  N  N     . ASN B 1 272 ? 153.124 138.574 139.982 1.00 12815. ? 272 ASN B N     1 
ATOM   6042  C  CA    . ASN B 1 272 ? 153.243 138.137 141.401 1.00 12818. ? 272 ASN B CA    1 
ATOM   6043  C  C     . ASN B 1 272 ? 154.517 138.719 142.020 1.00 12826. ? 272 ASN B C     1 
ATOM   6044  O  O     . ASN B 1 272 ? 155.590 138.601 141.390 1.00 12830. ? 272 ASN B O     1 
ATOM   6045  C  CB    . ASN B 1 272 ? 153.214 136.617 141.510 1.00 12837. ? 272 ASN B CB    1 
ATOM   6046  C  CG    . ASN B 1 272 ? 152.237 136.000 140.537 1.00 12830. ? 272 ASN B CG    1 
ATOM   6047  O  OD1   . ASN B 1 272 ? 152.633 135.204 139.678 1.00 12829. ? 272 ASN B OD1   1 
ATOM   6048  N  ND2   . ASN B 1 272 ? 150.966 136.356 140.646 1.00 12828. ? 272 ASN B ND2   1 
ATOM   6049  N  N     . ILE B 1 273 ? 154.402 139.318 143.209 1.00 13214. ? 273 ILE B N     1 
ATOM   6050  C  CA    . ILE B 1 273 ? 155.600 139.868 143.914 1.00 13235. ? 273 ILE B CA    1 
ATOM   6051  C  C     . ILE B 1 273 ? 156.644 138.747 144.037 1.00 13265. ? 273 ILE B C     1 
ATOM   6052  O  O     . ILE B 1 273 ? 157.836 139.023 143.786 1.00 13249. ? 273 ILE B O     1 
ATOM   6053  C  CB    . ILE B 1 273 ? 155.212 140.446 145.287 1.00 13246. ? 273 ILE B CB    1 
ATOM   6054  C  CG1   . ILE B 1 273 ? 154.070 141.455 145.169 1.00 13246. ? 273 ILE B CG1   1 
ATOM   6055  C  CG2   . ILE B 1 273 ? 156.427 141.049 145.992 1.00 13260. ? 273 ILE B CG2   1 
ATOM   6056  C  CD1   . ILE B 1 273 ? 153.684 142.109 146.483 1.00 13252. ? 273 ILE B CD1   1 
ATOM   6057  N  N     . ILE B 1 274 ? 156.212 137.537 144.408 1.00 14030. ? 274 ILE B N     1 
ATOM   6058  C  CA    . ILE B 1 274 ? 157.136 136.411 144.493 1.00 14041. ? 274 ILE B CA    1 
ATOM   6059  C  C     . ILE B 1 274 ? 156.643 135.303 143.569 1.00 14041. ? 274 ILE B C     1 
ATOM   6060  O  O     . ILE B 1 274 ? 155.487 134.872 143.683 1.00 14056. ? 274 ILE B O     1 
ATOM   6061  C  CB    . ILE B 1 274 ? 157.271 135.913 145.941 1.00 14071. ? 274 ILE B CB    1 
ATOM   6062  C  CG1   . ILE B 1 274 ? 158.299 136.754 146.696 1.00 14075. ? 274 ILE B CG1   1 
ATOM   6063  C  CG2   . ILE B 1 274 ? 157.667 134.449 145.975 1.00 14109. ? 274 ILE B CG2   1 
ATOM   6064  C  CD1   . ILE B 1 274 ? 158.448 136.366 148.147 1.00 14096. ? 274 ILE B CD1   1 
ATOM   6065  N  N     . PRO B 1 275 ? 157.467 134.825 142.640 1.00 13615. ? 275 PRO B N     1 
ATOM   6066  C  CA    . PRO B 1 275 ? 157.034 133.726 141.772 1.00 13611. ? 275 PRO B CA    1 
ATOM   6067  C  C     . PRO B 1 275 ? 156.993 132.412 142.533 1.00 13626. ? 275 PRO B C     1 
ATOM   6068  O  O     . PRO B 1 275 ? 157.870 132.116 143.348 1.00 13677. ? 275 PRO B O     1 
ATOM   6069  C  CB    . PRO B 1 275 ? 158.103 133.707 140.676 1.00 13619. ? 275 PRO B CB    1 
ATOM   6070  C  CG    . PRO B 1 275 ? 159.324 134.197 141.375 1.00 13638. ? 275 PRO B CG    1 
ATOM   6071  C  CD    . PRO B 1 275 ? 158.837 135.264 142.324 1.00 13633. ? 275 PRO B CD    1 
ATOM   6072  N  N     . GLY B 1 276 ? 155.965 131.620 142.260 1.00 13483. ? 276 GLY B N     1 
ATOM   6073  C  CA    . GLY B 1 276 ? 155.816 130.347 142.933 1.00 13495. ? 276 GLY B CA    1 
ATOM   6074  C  C     . GLY B 1 276 ? 154.724 129.520 142.297 1.00 13489. ? 276 GLY B C     1 
ATOM   6075  O  O     . GLY B 1 276 ? 153.900 130.026 141.530 1.00 13482. ? 276 GLY B O     1 
ATOM   6076  N  N     . GLY B 1 277 ? 154.732 128.234 142.631 1.00 13616. ? 277 GLY B N     1 
ATOM   6077  C  CA    . GLY B 1 277 ? 153.736 127.318 142.119 1.00 13619. ? 277 GLY B CA    1 
ATOM   6078  C  C     . GLY B 1 277 ? 154.315 126.250 141.217 1.00 13631. ? 277 GLY B C     1 
ATOM   6079  O  O     . GLY B 1 277 ? 153.677 125.222 140.974 1.00 13547. ? 277 GLY B O     1 
ATOM   6080  N  N     . ALA B 1 278 ? 155.525 126.477 140.717 1.00 14289. ? 278 ALA B N     1 
ATOM   6081  C  CA    . ALA B 1 278 ? 156.179 125.528 139.826 1.00 14309. ? 278 ALA B CA    1 
ATOM   6082  C  C     . ALA B 1 278 ? 157.683 125.754 139.900 1.00 14339. ? 278 ALA B C     1 
ATOM   6083  O  O     . ALA B 1 278 ? 158.169 126.604 140.650 1.00 14337. ? 278 ALA B O     1 
ATOM   6084  C  CB    . ALA B 1 278 ? 155.661 125.665 138.392 1.00 14196. ? 278 ALA B CB    1 
ATOM   6085  N  N     . VAL B 1 279 ? 158.418 124.981 139.109 1.00 15364. ? 279 VAL B N     1 
ATOM   6086  C  CA    . VAL B 1 279 ? 159.871 125.062 139.038 1.00 15399. ? 279 VAL B CA    1 
ATOM   6087  C  C     . VAL B 1 279 ? 160.210 125.620 137.662 1.00 15406. ? 279 VAL B C     1 
ATOM   6088  O  O     . VAL B 1 279 ? 160.176 124.897 136.659 1.00 15400. ? 279 VAL B O     1 
ATOM   6089  C  CB    . VAL B 1 279 ? 160.532 123.701 139.279 1.00 15422. ? 279 VAL B CB    1 
ATOM   6090  C  CG1   . VAL B 1 279 ? 162.016 123.765 138.976 1.00 15462. ? 279 VAL B CG1   1 
ATOM   6091  C  CG2   . VAL B 1 279 ? 160.298 123.247 140.712 1.00 15422. ? 279 VAL B CG2   1 
ATOM   6092  N  N     . ALA B 1 280 ? 160.530 126.910 137.605 1.00 14541. ? 280 ALA B N     1 
ATOM   6093  C  CA    . ALA B 1 280 ? 160.803 127.570 136.338 1.00 14498. ? 280 ALA B CA    1 
ATOM   6094  C  C     . ALA B 1 280 ? 161.528 128.880 136.601 1.00 14462. ? 280 ALA B C     1 
ATOM   6095  O  O     . ALA B 1 280 ? 161.567 129.374 137.730 1.00 14473. ? 280 ALA B O     1 
ATOM   6096  C  CB    . ALA B 1 280 ? 159.514 127.821 135.552 1.00 14461. ? 280 ALA B CB    1 
ATOM   6097  N  N     . LYS B 1 281 ? 162.105 129.434 135.536 1.00 13187. ? 281 LYS B N     1 
ATOM   6098  C  CA    . LYS B 1 281 ? 162.742 130.745 135.605 1.00 13137. ? 281 LYS B CA    1 
ATOM   6099  C  C     . LYS B 1 281 ? 161.745 131.822 135.192 1.00 13127. ? 281 LYS B C     1 
ATOM   6100  O  O     . LYS B 1 281 ? 161.196 131.755 134.087 1.00 13149. ? 281 LYS B O     1 
ATOM   6101  C  CB    . LYS B 1 281 ? 163.967 130.802 134.708 1.00 13146. ? 281 LYS B CB    1 
ATOM   6102  C  CG    . LYS B 1 281 ? 164.888 131.969 135.007 1.00 13162. ? 281 LYS B CG    1 
ATOM   6103  C  CD    . LYS B 1 281 ? 165.843 132.232 133.858 1.00 13144. ? 281 LYS B CD    1 
ATOM   6104  C  CE    . LYS B 1 281 ? 166.730 133.429 134.152 1.00 13145. ? 281 LYS B CE    1 
ATOM   6105  N  NZ    . LYS B 1 281 ? 165.947 134.568 134.703 1.00 13133. ? 281 LYS B NZ    1 
ATOM   6106  N  N     . PRO B 1 282 ? 161.484 132.812 136.036 1.00 12753. ? 282 PRO B N     1 
ATOM   6107  C  CA    . PRO B 1 282 ? 160.402 133.761 135.774 1.00 12743. ? 282 PRO B CA    1 
ATOM   6108  C  C     . PRO B 1 282 ? 160.848 134.956 134.938 1.00 12741. ? 282 PRO B C     1 
ATOM   6109  O  O     . PRO B 1 282 ? 162.035 135.176 134.690 1.00 12758. ? 282 PRO B O     1 
ATOM   6110  C  CB    . PRO B 1 282 ? 159.994 134.220 137.186 1.00 12748. ? 282 PRO B CB    1 
ATOM   6111  C  CG    . PRO B 1 282 ? 160.878 133.443 138.150 1.00 12766. ? 282 PRO B CG    1 
ATOM   6112  C  CD    . PRO B 1 282 ? 162.068 133.027 137.364 1.00 12761. ? 282 PRO B CD    1 
ATOM   6113  N  N     . PHE B 1 283 ? 159.856 135.732 134.511 1.00 12737. ? 283 PHE B N     1 
ATOM   6114  C  CA    . PHE B 1 283 ? 160.059 137.013 133.850 1.00 12735. ? 283 PHE B CA    1 
ATOM   6115  C  C     . PHE B 1 283 ? 159.886 138.116 134.883 1.00 12744. ? 283 PHE B C     1 
ATOM   6116  O  O     . PHE B 1 283 ? 158.968 138.055 135.706 1.00 12755. ? 283 PHE B O     1 
ATOM   6117  C  CB    . PHE B 1 283 ? 159.057 137.216 132.712 1.00 12749. ? 283 PHE B CB    1 
ATOM   6118  C  CG    . PHE B 1 283 ? 159.356 136.423 131.473 1.00 12745. ? 283 PHE B CG    1 
ATOM   6119  C  CD1   . PHE B 1 283 ? 160.433 136.740 130.667 1.00 12750. ? 283 PHE B CD1   1 
ATOM   6120  C  CD2   . PHE B 1 283 ? 158.533 135.380 131.096 1.00 12758. ? 283 PHE B CD2   1 
ATOM   6121  C  CE1   . PHE B 1 283 ? 160.693 136.019 129.523 1.00 12769. ? 283 PHE B CE1   1 
ATOM   6122  C  CE2   . PHE B 1 283 ? 158.790 134.657 129.955 1.00 12765. ? 283 PHE B CE2   1 
ATOM   6123  C  CZ    . PHE B 1 283 ? 159.871 134.976 129.168 1.00 12770. ? 283 PHE B CZ    1 
ATOM   6124  N  N     . ILE B 1 284 ? 160.757 139.120 134.843 1.00 12739. ? 284 ILE B N     1 
ATOM   6125  C  CA    . ILE B 1 284 ? 160.712 140.233 135.784 1.00 12743. ? 284 ILE B CA    1 
ATOM   6126  C  C     . ILE B 1 284 ? 160.297 141.497 135.048 1.00 12738. ? 284 ILE B C     1 
ATOM   6127  O  O     . ILE B 1 284 ? 160.928 141.891 134.060 1.00 12749. ? 284 ILE B O     1 
ATOM   6128  C  CB    . ILE B 1 284 ? 162.062 140.435 136.498 1.00 12738. ? 284 ILE B CB    1 
ATOM   6129  C  CG1   . ILE B 1 284 ? 162.661 139.089 136.899 1.00 12755. ? 284 ILE B CG1   1 
ATOM   6130  C  CG2   . ILE B 1 284 ? 161.887 141.314 137.720 1.00 12743. ? 284 ILE B CG2   1 
ATOM   6131  C  CD1   . ILE B 1 284 ? 164.170 139.078 136.914 1.00 12755. ? 284 ILE B CD1   1 
ATOM   6132  N  N     . THR B 1 285 ? 159.231 142.133 135.536 1.00 12733. ? 285 THR B N     1 
ATOM   6133  C  CA    . THR B 1 285 ? 158.757 143.403 135.003 1.00 12729. ? 285 THR B CA    1 
ATOM   6134  C  C     . THR B 1 285 ? 158.823 144.463 136.093 1.00 12728. ? 285 THR B C     1 
ATOM   6135  O  O     . THR B 1 285 ? 159.055 144.138 137.259 1.00 12755. ? 285 THR B O     1 
ATOM   6136  C  CB    . THR B 1 285 ? 157.323 143.282 134.483 1.00 12740. ? 285 THR B CB    1 
ATOM   6137  O  OG1   . THR B 1 285 ? 156.411 143.354 135.585 1.00 12750. ? 285 THR B OG1   1 
ATOM   6138  C  CG2   . THR B 1 285 ? 157.122 141.959 133.773 1.00 12741. ? 285 THR B CG2   1 
ATOM   6139  N  N     . TYR B 1 286 ? 158.601 145.726 135.737 1.00 12723. ? 286 TYR B N     1 
ATOM   6140  C  CA    . TYR B 1 286 ? 158.646 146.819 136.701 1.00 12734. ? 286 TYR B CA    1 
ATOM   6141  C  C     . TYR B 1 286 ? 157.311 147.544 136.690 1.00 12734. ? 286 TYR B C     1 
ATOM   6142  O  O     . TYR B 1 286 ? 156.916 148.096 135.660 1.00 12750. ? 286 TYR B O     1 
ATOM   6143  C  CB    . TYR B 1 286 ? 159.784 147.789 136.378 1.00 12748. ? 286 TYR B CB    1 
ATOM   6144  C  CG    . TYR B 1 286 ? 159.744 149.068 137.178 1.00 12741. ? 286 TYR B CG    1 
ATOM   6145  C  CD1   . TYR B 1 286 ? 160.103 149.084 138.516 1.00 12760. ? 286 TYR B CD1   1 
ATOM   6146  C  CD2   . TYR B 1 286 ? 159.346 150.259 136.595 1.00 12738. ? 286 TYR B CD2   1 
ATOM   6147  C  CE1   . TYR B 1 286 ? 160.067 150.249 139.249 1.00 12760. ? 286 TYR B CE1   1 
ATOM   6148  C  CE2   . TYR B 1 286 ? 159.307 151.428 137.320 1.00 12738. ? 286 TYR B CE2   1 
ATOM   6149  C  CZ    . TYR B 1 286 ? 159.667 151.417 138.646 1.00 12751. ? 286 TYR B CZ    1 
ATOM   6150  O  OH    . TYR B 1 286 ? 159.629 152.584 139.369 1.00 12766. ? 286 TYR B OH    1 
ATOM   6151  N  N     . HIS B 1 287 ? 156.620 147.540 137.826 1.00 12736. ? 287 HIS B N     1 
ATOM   6152  C  CA    . HIS B 1 287 ? 155.373 148.276 137.956 1.00 12743. ? 287 HIS B CA    1 
ATOM   6153  C  C     . HIS B 1 287 ? 155.659 149.760 138.143 1.00 12745. ? 287 HIS B C     1 
ATOM   6154  O  O     . HIS B 1 287 ? 156.643 150.147 138.775 1.00 12763. ? 287 HIS B O     1 
ATOM   6155  C  CB    . HIS B 1 287 ? 154.560 147.743 139.132 1.00 12747. ? 287 HIS B CB    1 
ATOM   6156  C  CG    . HIS B 1 287 ? 153.080 147.866 138.953 1.00 12743. ? 287 HIS B CG    1 
ATOM   6157  N  ND1   . HIS B 1 287 ? 152.410 149.060 139.101 1.00 12754. ? 287 HIS B ND1   1 
ATOM   6158  C  CD2   . HIS B 1 287 ? 152.139 146.942 138.649 1.00 12742. ? 287 HIS B CD2   1 
ATOM   6159  C  CE1   . HIS B 1 287 ? 151.120 148.868 138.892 1.00 12752. ? 287 HIS B CE1   1 
ATOM   6160  N  NE2   . HIS B 1 287 ? 150.929 147.591 138.616 1.00 12742. ? 287 HIS B NE2   1 
ATOM   6161  N  N     . ASN B 1 288 ? 154.786 150.595 137.585 1.00 12745. ? 288 ASN B N     1 
ATOM   6162  C  CA    . ASN B 1 288 ? 155.005 152.036 137.628 1.00 12742. ? 288 ASN B CA    1 
ATOM   6163  C  C     . ASN B 1 288 ? 154.352 152.687 138.842 1.00 12772. ? 288 ASN B C     1 
ATOM   6164  O  O     . ASN B 1 288 ? 155.014 153.419 139.583 1.00 12774. ? 288 ASN B O     1 
ATOM   6165  C  CB    . ASN B 1 288 ? 154.493 152.684 136.340 1.00 12755. ? 288 ASN B CB    1 
ATOM   6166  C  CG    . ASN B 1 288 ? 155.580 152.842 135.300 1.00 12754. ? 288 ASN B CG    1 
ATOM   6167  O  OD1   . ASN B 1 288 ? 156.767 152.834 135.621 1.00 12743. ? 288 ASN B OD1   1 
ATOM   6168  N  ND2   . ASN B 1 288 ? 155.180 152.988 134.044 1.00 12766. ? 288 ASN B ND2   1 
ATOM   6169  N  N     . GLU B 1 289 ? 153.070 152.391 139.070 1.00 13765. ? 289 GLU B N     1 
ATOM   6170  C  CA    . GLU B 1 289 ? 152.400 152.913 140.290 1.00 13797. ? 289 GLU B CA    1 
ATOM   6171  C  C     . GLU B 1 289 ? 153.071 152.284 141.520 1.00 13781. ? 289 GLU B C     1 
ATOM   6172  O  O     . GLU B 1 289 ? 153.149 152.964 142.566 1.00 13808. ? 289 GLU B O     1 
ATOM   6173  C  CB    . GLU B 1 289 ? 150.904 152.606 140.266 1.00 13815. ? 289 GLU B CB    1 
ATOM   6174  C  CG    . GLU B 1 289 ? 150.182 153.296 139.115 1.00 13826. ? 289 GLU B CG    1 
ATOM   6175  C  CD    . GLU B 1 289 ? 150.424 154.793 139.060 1.00 13825. ? 289 GLU B CD    1 
ATOM   6176  O  OE1   . GLU B 1 289 ? 150.070 155.487 140.036 1.00 13839. ? 289 GLU B OE1   1 
ATOM   6177  O  OE2   . GLU B 1 289 ? 150.968 155.265 138.039 1.00 13778. ? 289 GLU B OE2   1 
ATOM   6178  N  N     . LEU B 1 290 ? 153.535 151.037 141.391 1.00 12777. ? 290 LEU B N     1 
ATOM   6179  C  CA    . LEU B 1 290 ? 154.224 150.351 142.514 1.00 12766. ? 290 LEU B CA    1 
ATOM   6180  C  C     . LEU B 1 290 ? 155.717 150.241 142.177 1.00 12785. ? 290 LEU B C     1 
ATOM   6181  O  O     . LEU B 1 290 ? 156.059 149.417 141.309 1.00 12789. ? 290 LEU B O     1 
ATOM   6182  C  CB    . LEU B 1 290 ? 153.601 148.973 142.730 1.00 12761. ? 290 LEU B CB    1 
ATOM   6183  C  CG    . LEU B 1 290 ? 152.075 148.894 142.617 1.00 12747. ? 290 LEU B CG    1 
ATOM   6184  C  CD1   . LEU B 1 290 ? 151.607 147.457 142.765 1.00 12754. ? 290 LEU B CD1   1 
ATOM   6185  C  CD2   . LEU B 1 290 ? 151.387 149.788 143.634 1.00 12751. ? 290 LEU B CD2   1 
ATOM   6186  N  N     . ASP B 1 291 ? 156.574 151.002 142.864 1.00 13425. ? 291 ASP B N     1 
ATOM   6187  C  CA    . ASP B 1 291 ? 158.029 151.010 142.539 1.00 13432. ? 291 ASP B CA    1 
ATOM   6188  C  C     . ASP B 1 291 ? 158.585 149.583 142.632 1.00 13424. ? 291 ASP B C     1 
ATOM   6189  O  O     . ASP B 1 291 ? 159.641 149.314 142.024 1.00 13457. ? 291 ASP B O     1 
ATOM   6190  C  CB    . ASP B 1 291 ? 158.780 151.999 143.418 1.00 13453. ? 291 ASP B CB    1 
ATOM   6191  C  CG    . ASP B 1 291 ? 160.094 152.522 142.854 1.00 13456. ? 291 ASP B CG    1 
ATOM   6192  O  OD1   . ASP B 1 291 ? 161.014 151.704 142.644 1.00 13452. ? 291 ASP B OD1   1 
ATOM   6193  O  OD2   . ASP B 1 291 ? 160.186 153.746 142.627 1.00 13459. ? 291 ASP B OD2   1 
ATOM   6194  N  N     . MET B 1 292 ? 157.904 148.703 143.369 1.00 13038. ? 292 MET B N     1 
ATOM   6195  C  CA    . MET B 1 292 ? 158.355 147.294 143.512 1.00 13049. ? 292 MET B CA    1 
ATOM   6196  C  C     . MET B 1 292 ? 158.321 146.588 142.146 1.00 13036. ? 292 MET B C     1 
ATOM   6197  O  O     . MET B 1 292 ? 157.426 146.905 141.331 1.00 13043. ? 292 MET B O     1 
ATOM   6198  C  CB    . MET B 1 292 ? 157.448 146.546 144.492 1.00 13050. ? 292 MET B CB    1 
ATOM   6199  C  CG    . MET B 1 292 ? 155.979 146.597 144.124 1.00 13044. ? 292 MET B CG    1 
ATOM   6200  S  SD    . MET B 1 292 ? 154.999 145.677 145.325 1.00 13026. ? 292 MET B SD    1 
ATOM   6201  C  CE    . MET B 1 292 ? 156.262 144.462 145.723 1.00 13053. ? 292 MET B CE    1 
ATOM   6202  N  N     . ASN B 1 293 ? 159.262 145.668 141.905 1.00 12754. ? 293 ASN B N     1 
ATOM   6203  C  CA    . ASN B 1 293 ? 159.267 144.887 140.635 1.00 12739. ? 293 ASN B CA    1 
ATOM   6204  C  C     . ASN B 1 293 ? 158.259 143.739 140.754 1.00 12733. ? 293 ASN B C     1 
ATOM   6205  O  O     . ASN B 1 293 ? 157.931 143.357 141.900 1.00 12739. ? 293 ASN B O     1 
ATOM   6206  C  CB    . ASN B 1 293 ? 160.662 144.376 140.295 1.00 12735. ? 293 ASN B CB    1 
ATOM   6207  C  CG    . ASN B 1 293 ? 161.605 145.497 139.933 1.00 12741. ? 293 ASN B CG    1 
ATOM   6208  O  OD1   . ASN B 1 293 ? 161.377 146.207 138.948 1.00 12754. ? 293 ASN B OD1   1 
ATOM   6209  N  ND2   . ASN B 1 293 ? 162.668 145.668 140.706 1.00 12748. ? 293 ASN B ND2   1 
ATOM   6210  N  N     . LEU B 1 294 ? 157.791 143.208 139.620 1.00 12737. ? 294 LEU B N     1 
ATOM   6211  C  CA    . LEU B 1 294 ? 156.760 142.135 139.654 1.00 12736. ? 294 LEU B CA    1 
ATOM   6212  C  C     . LEU B 1 294 ? 157.180 140.962 138.756 1.00 12740. ? 294 LEU B C     1 
ATOM   6213  O  O     . LEU B 1 294 ? 157.636 141.217 137.619 1.00 12757. ? 294 LEU B O     1 
ATOM   6214  C  CB    . LEU B 1 294 ? 155.400 142.699 139.244 1.00 12746. ? 294 LEU B CB    1 
ATOM   6215  C  CG    . LEU B 1 294 ? 154.701 143.572 140.291 1.00 12743. ? 294 LEU B CG    1 
ATOM   6216  C  CD1   . LEU B 1 294 ? 153.327 143.997 139.811 1.00 12749. ? 294 LEU B CD1   1 
ATOM   6217  C  CD2   . LEU B 1 294 ? 154.596 142.834 141.614 1.00 12758. ? 294 LEU B CD2   1 
ATOM   6218  N  N     . TYR B 1 295 ? 157.030 139.730 139.251 1.00 12737. ? 295 TYR B N     1 
ATOM   6219  C  CA    . TYR B 1 295 ? 157.365 138.548 138.474 1.00 12736. ? 295 TYR B CA    1 
ATOM   6220  C  C     . TYR B 1 295 ? 156.124 138.048 137.753 1.00 12735. ? 295 TYR B C     1 
ATOM   6221  O  O     . TYR B 1 295 ? 155.025 138.056 138.315 1.00 12757. ? 295 TYR B O     1 
ATOM   6222  C  CB    . TYR B 1 295 ? 157.927 137.441 139.365 1.00 12762. ? 295 TYR B CB    1 
ATOM   6223  C  CG    . TYR B 1 295 ? 159.261 137.769 139.990 1.00 12753. ? 295 TYR B CG    1 
ATOM   6224  C  CD1   . TYR B 1 295 ? 159.344 138.596 141.099 1.00 12769. ? 295 TYR B CD1   1 
ATOM   6225  C  CD2   . TYR B 1 295 ? 160.436 137.247 139.474 1.00 12752. ? 295 TYR B CD2   1 
ATOM   6226  C  CE1   . TYR B 1 295 ? 160.557 138.895 141.675 1.00 12750. ? 295 TYR B CE1   1 
ATOM   6227  C  CE2   . TYR B 1 295 ? 161.654 137.541 140.043 1.00 12752. ? 295 TYR B CE2   1 
ATOM   6228  C  CZ    . TYR B 1 295 ? 161.709 138.365 141.144 1.00 12743. ? 295 TYR B CZ    1 
ATOM   6229  O  OH    . TYR B 1 295 ? 162.924 138.661 141.716 1.00 12758. ? 295 TYR B OH    1 
ATOM   6230  N  N     . MET B 1 296 ? 156.296 137.623 136.507 1.00 12724. ? 296 MET B N     1 
ATOM   6231  C  CA    . MET B 1 296 ? 155.155 137.120 135.764 1.00 12737. ? 296 MET B CA    1 
ATOM   6232  C  C     . MET B 1 296 ? 154.783 135.722 136.240 1.00 12732. ? 296 MET B C     1 
ATOM   6233  O  O     . MET B 1 296 ? 155.576 135.012 136.863 1.00 12744. ? 296 MET B O     1 
ATOM   6234  C  CB    . MET B 1 296 ? 155.432 137.115 134.264 1.00 12755. ? 296 MET B CB    1 
ATOM   6235  C  CG    . MET B 1 296 ? 155.521 138.502 133.671 1.00 12756. ? 296 MET B CG    1 
ATOM   6236  S  SD    . MET B 1 296 ? 154.079 139.455 134.162 1.00 12744. ? 296 MET B SD    1 
ATOM   6237  C  CE    . MET B 1 296 ? 152.966 139.136 132.810 1.00 12762. ? 296 MET B CE    1 
ATOM   6238  N  N     . ARG B 1 297 ? 153.548 135.335 135.940 1.00 12729. ? 297 ARG B N     1 
ATOM   6239  C  CA    . ARG B 1 297 ? 153.000 134.091 136.458 1.00 12725. ? 297 ARG B CA    1 
ATOM   6240  C  C     . ARG B 1 297 ? 153.734 132.889 135.883 1.00 12732. ? 297 ARG B C     1 
ATOM   6241  O  O     . ARG B 1 297 ? 154.011 132.830 134.683 1.00 12754. ? 297 ARG B O     1 
ATOM   6242  C  CB    . ARG B 1 297 ? 151.514 133.995 136.128 1.00 12743. ? 297 ARG B CB    1 
ATOM   6243  C  CG    . ARG B 1 297 ? 150.765 133.006 136.986 1.00 12757. ? 297 ARG B CG    1 
ATOM   6244  C  CD    . ARG B 1 297 ? 149.271 133.214 136.877 1.00 12750. ? 297 ARG B CD    1 
ATOM   6245  N  NE    . ARG B 1 297 ? 148.776 132.901 135.544 1.00 12729. ? 297 ARG B NE    1 
ATOM   6246  C  CZ    . ARG B 1 297 ? 147.517 133.054 135.160 1.00 12731. ? 297 ARG B CZ    1 
ATOM   6247  N  NH1   . ARG B 1 297 ? 146.601 133.546 135.977 1.00 12747. ? 297 ARG B NH1   1 
ATOM   6248  N  NH2   . ARG B 1 297 ? 147.168 132.703 133.927 1.00 12752. ? 297 ARG B NH2   1 
ATOM   6249  N  N     . ILE B 1 298 ? 154.052 131.930 136.747 1.00 12735. ? 298 ILE B N     1 
ATOM   6250  C  CA    . ILE B 1 298 ? 154.513 130.623 136.306 1.00 12735. ? 298 ILE B CA    1 
ATOM   6251  C  C     . ILE B 1 298 ? 153.524 129.518 136.651 1.00 12735. ? 298 ILE B C     1 
ATOM   6252  O  O     . ILE B 1 298 ? 153.568 128.453 136.017 1.00 12731. ? 298 ILE B O     1 
ATOM   6253  C  CB    . ILE B 1 298 ? 155.906 130.293 136.879 1.00 12741. ? 298 ILE B CB    1 
ATOM   6254  C  CG1   . ILE B 1 298 ? 155.851 130.190 138.401 1.00 12777. ? 298 ILE B CG1   1 
ATOM   6255  C  CG2   . ILE B 1 298 ? 156.917 131.343 136.456 1.00 12741. ? 298 ILE B CG2   1 
ATOM   6256  C  CD1   . ILE B 1 298 ? 157.137 129.702 139.020 1.00 12805. ? 298 ILE B CD1   1 
ATOM   6257  N  N     . ALA B 1 299 ? 152.639 129.735 137.616 1.00 12731. ? 299 ALA B N     1 
ATOM   6258  C  CA    . ALA B 1 299 ? 151.584 128.796 137.971 1.00 12728. ? 299 ALA B CA    1 
ATOM   6259  C  C     . ALA B 1 299 ? 150.600 129.513 138.890 1.00 12749. ? 299 ALA B C     1 
ATOM   6260  O  O     . ALA B 1 299 ? 151.013 130.290 139.754 1.00 12746. ? 299 ALA B O     1 
ATOM   6261  C  CB    . ALA B 1 299 ? 152.150 127.546 138.660 1.00 12710. ? 299 ALA B CB    1 
ATOM   6262  N  N     . PRO B 1 300 ? 149.303 129.276 138.712 1.00 12759. ? 300 PRO B N     1 
ATOM   6263  C  CA    . PRO B 1 300 ? 148.306 129.898 139.593 1.00 12760. ? 300 PRO B CA    1 
ATOM   6264  C  C     . PRO B 1 300 ? 147.990 129.055 140.819 1.00 12767. ? 300 PRO B C     1 
ATOM   6265  O  O     . PRO B 1 300 ? 146.966 129.263 141.476 1.00 12777. ? 300 PRO B O     1 
ATOM   6266  C  CB    . PRO B 1 300 ? 147.087 130.039 138.677 1.00 12752. ? 300 PRO B CB    1 
ATOM   6267  C  CG    . PRO B 1 300 ? 147.239 128.928 137.665 1.00 12745. ? 300 PRO B CG    1 
ATOM   6268  C  CD    . PRO B 1 300 ? 148.672 128.445 137.675 1.00 12751. ? 300 PRO B CD    1 
ATOM   6269  N  N     . GLU B 1 301 ? 148.866 128.094 141.125 1.00 12758. ? 301 GLU B N     1 
ATOM   6270  C  CA    . GLU B 1 301 ? 148.579 127.099 142.155 1.00 12742. ? 301 GLU B CA    1 
ATOM   6271  C  C     . GLU B 1 301 ? 148.367 127.732 143.527 1.00 12742. ? 301 GLU B C     1 
ATOM   6272  O  O     . GLU B 1 301 ? 147.374 127.440 144.209 1.00 12757. ? 301 GLU B O     1 
ATOM   6273  C  CB    . GLU B 1 301 ? 149.719 126.084 142.205 1.00 12717. ? 301 GLU B CB    1 
ATOM   6274  C  CG    . GLU B 1 301 ? 149.845 125.343 143.516 1.00 12724. ? 301 GLU B CG    1 
ATOM   6275  C  CD    . GLU B 1 301 ? 150.569 124.024 143.363 1.00 12673. ? 301 GLU B CD    1 
ATOM   6276  O  OE1   . GLU B 1 301 ? 151.152 123.788 142.286 1.00 12622. ? 301 GLU B OE1   1 
ATOM   6277  O  OE2   . GLU B 1 301 ? 150.549 123.218 144.315 1.00 12723. ? 301 GLU B OE2   1 
ATOM   6278  N  N     . LEU B 1 302 ? 149.291 128.595 143.951 1.00 12737. ? 302 LEU B N     1 
ATOM   6279  C  CA    . LEU B 1 302 ? 149.245 129.165 145.291 1.00 12737. ? 302 LEU B CA    1 
ATOM   6280  C  C     . LEU B 1 302 ? 148.038 130.061 145.515 1.00 12740. ? 302 LEU B C     1 
ATOM   6281  O  O     . LEU B 1 302 ? 147.643 130.262 146.667 1.00 12752. ? 302 LEU B O     1 
ATOM   6282  C  CB    . LEU B 1 302 ? 150.527 129.952 145.570 1.00 12738. ? 302 LEU B CB    1 
ATOM   6283  C  CG    . LEU B 1 302 ? 151.836 129.160 145.520 1.00 12746. ? 302 LEU B CG    1 
ATOM   6284  C  CD1   . LEU B 1 302 ? 152.966 129.956 146.144 1.00 12770. ? 302 LEU B CD1   1 
ATOM   6285  C  CD2   . LEU B 1 302 ? 151.687 127.816 146.210 1.00 12746. ? 302 LEU B CD2   1 
ATOM   6286  N  N     . TYR B 1 303 ? 147.447 130.599 144.452 1.00 12731. ? 303 TYR B N     1 
ATOM   6287  C  CA    . TYR B 1 303 ? 146.227 131.384 144.556 1.00 12729. ? 303 TYR B CA    1 
ATOM   6288  C  C     . TYR B 1 303 ? 144.974 130.525 144.536 1.00 12747. ? 303 TYR B C     1 
ATOM   6289  O  O     . TYR B 1 303 ? 144.008 130.836 145.242 1.00 12764. ? 303 TYR B O     1 
ATOM   6290  C  CB    . TYR B 1 303 ? 146.163 132.401 143.417 1.00 12731. ? 303 TYR B CB    1 
ATOM   6291  C  CG    . TYR B 1 303 ? 147.148 133.534 143.559 1.00 12720. ? 303 TYR B CG    1 
ATOM   6292  C  CD1   . TYR B 1 303 ? 147.322 134.180 144.771 1.00 12732. ? 303 TYR B CD1   1 
ATOM   6293  C  CD2   . TYR B 1 303 ? 147.916 133.945 142.482 1.00 12735. ? 303 TYR B CD2   1 
ATOM   6294  C  CE1   . TYR B 1 303 ? 148.224 135.213 144.905 1.00 12744. ? 303 TYR B CE1   1 
ATOM   6295  C  CE2   . TYR B 1 303 ? 148.821 134.976 142.606 1.00 12742. ? 303 TYR B CE2   1 
ATOM   6296  C  CZ    . TYR B 1 303 ? 148.972 135.606 143.819 1.00 12742. ? 303 TYR B CZ    1 
ATOM   6297  O  OH    . TYR B 1 303 ? 149.875 136.635 143.944 1.00 12751. ? 303 TYR B OH    1 
ATOM   6298  N  N     . HIS B 1 304 ? 144.975 129.443 143.758 1.00 12742. ? 304 HIS B N     1 
ATOM   6299  C  CA    . HIS B 1 304 ? 143.862 128.503 143.795 1.00 12744. ? 304 HIS B CA    1 
ATOM   6300  C  C     . HIS B 1 304 ? 143.728 127.868 145.171 1.00 12754. ? 304 HIS B C     1 
ATOM   6301  O  O     . HIS B 1 304 ? 142.614 127.698 145.679 1.00 12775. ? 304 HIS B O     1 
ATOM   6302  C  CB    . HIS B 1 304 ? 144.049 127.423 142.734 1.00 12751. ? 304 HIS B CB    1 
ATOM   6303  C  CG    . HIS B 1 304 ? 143.806 127.894 141.335 1.00 12740. ? 304 HIS B CG    1 
ATOM   6304  N  ND1   . HIS B 1 304 ? 144.149 129.157 140.904 1.00 12737. ? 304 HIS B ND1   1 
ATOM   6305  C  CD2   . HIS B 1 304 ? 143.263 127.266 140.267 1.00 12753. ? 304 HIS B CD2   1 
ATOM   6306  C  CE1   . HIS B 1 304 ? 143.823 129.288 139.631 1.00 12749. ? 304 HIS B CE1   1 
ATOM   6307  N  NE2   . HIS B 1 304 ? 143.283 128.155 139.220 1.00 12756. ? 304 HIS B NE2   1 
ATOM   6308  N  N     . LYS B 1 305 ? 144.854 127.502 145.788 1.00 12749. ? 305 LYS B N     1 
ATOM   6309  C  CA    . LYS B 1 305 ? 144.788 126.928 147.128 1.00 12720. ? 305 LYS B CA    1 
ATOM   6310  C  C     . LYS B 1 305 ? 144.268 127.943 148.138 1.00 12721. ? 305 LYS B C     1 
ATOM   6311  O  O     . LYS B 1 305 ? 143.501 127.592 149.042 1.00 12743. ? 305 LYS B O     1 
ATOM   6312  C  CB    . LYS B 1 305 ? 146.159 126.398 147.538 1.00 12725. ? 305 LYS B CB    1 
ATOM   6313  C  CG    . LYS B 1 305 ? 146.473 125.044 146.938 1.00 12721. ? 305 LYS B CG    1 
ATOM   6314  C  CD    . LYS B 1 305 ? 147.628 124.374 147.645 1.00 12717. ? 305 LYS B CD    1 
ATOM   6315  C  CE    . LYS B 1 305 ? 148.910 124.536 146.859 1.00 12740. ? 305 LYS B CE    1 
ATOM   6316  N  NZ    . LYS B 1 305 ? 149.712 123.285 146.859 1.00 12722. ? 305 LYS B NZ    1 
ATOM   6317  N  N     . MET B 1 306 ? 144.667 129.208 147.998 1.00 12736. ? 306 MET B N     1 
ATOM   6318  C  CA    . MET B 1 306 ? 144.143 130.247 148.877 1.00 12732. ? 306 MET B CA    1 
ATOM   6319  C  C     . MET B 1 306 ? 142.640 130.411 148.696 1.00 12744. ? 306 MET B C     1 
ATOM   6320  O  O     . MET B 1 306 ? 141.906 130.616 149.669 1.00 12758. ? 306 MET B O     1 
ATOM   6321  C  CB    . MET B 1 306 ? 144.865 131.567 148.614 1.00 12740. ? 306 MET B CB    1 
ATOM   6322  C  CG    . MET B 1 306 ? 146.055 131.801 149.521 1.00 12749. ? 306 MET B CG    1 
ATOM   6323  S  SD    . MET B 1 306 ? 147.382 132.722 148.729 1.00 12739. ? 306 MET B SD    1 
ATOM   6324  C  CE    . MET B 1 306 ? 146.690 134.369 148.730 1.00 12748. ? 306 MET B CE    1 
ATOM   6325  N  N     . LEU B 1 307 ? 142.164 130.328 147.453 1.00 12753. ? 307 LEU B N     1 
ATOM   6326  C  CA    . LEU B 1 307 ? 140.727 130.407 147.210 1.00 12747. ? 307 LEU B CA    1 
ATOM   6327  C  C     . LEU B 1 307 ? 139.990 129.229 147.832 1.00 12754. ? 307 LEU B C     1 
ATOM   6328  O  O     . LEU B 1 307 ? 138.900 129.398 148.388 1.00 12765. ? 307 LEU B O     1 
ATOM   6329  C  CB    . LEU B 1 307 ? 140.445 130.476 145.713 1.00 12744. ? 307 LEU B CB    1 
ATOM   6330  C  CG    . LEU B 1 307 ? 140.610 131.856 145.089 1.00 12736. ? 307 LEU B CG    1 
ATOM   6331  C  CD1   . LEU B 1 307 ? 139.858 131.913 143.787 1.00 12749. ? 307 LEU B CD1   1 
ATOM   6332  C  CD2   . LEU B 1 307 ? 140.116 132.925 146.040 1.00 12744. ? 307 LEU B CD2   1 
ATOM   6333  N  N     . VAL B 1 308 ? 140.560 128.027 147.736 1.00 12758. ? 308 VAL B N     1 
ATOM   6334  C  CA    . VAL B 1 308 ? 139.931 126.863 148.356 1.00 12729. ? 308 VAL B CA    1 
ATOM   6335  C  C     . VAL B 1 308 ? 139.898 127.022 149.871 1.00 12699. ? 308 VAL B C     1 
ATOM   6336  O  O     . VAL B 1 308 ? 138.938 126.611 150.534 1.00 12677. ? 308 VAL B O     1 
ATOM   6337  C  CB    . VAL B 1 308 ? 140.651 125.570 147.933 1.00 12697. ? 308 VAL B CB    1 
ATOM   6338  C  CG1   . VAL B 1 308 ? 140.075 124.387 148.672 1.00 12625. ? 308 VAL B CG1   1 
ATOM   6339  C  CG2   . VAL B 1 308 ? 140.521 125.360 146.437 1.00 12751. ? 308 VAL B CG2   1 
ATOM   6340  N  N     . VAL B 1 309 ? 140.945 127.620 150.443 1.00 12704. ? 309 VAL B N     1 
ATOM   6341  C  CA    . VAL B 1 309 ? 140.906 127.995 151.855 1.00 12660. ? 309 VAL B CA    1 
ATOM   6342  C  C     . VAL B 1 309 ? 139.758 128.962 152.110 1.00 12714. ? 309 VAL B C     1 
ATOM   6343  O  O     . VAL B 1 309 ? 139.074 128.883 153.138 1.00 12724. ? 309 VAL B O     1 
ATOM   6344  C  CB    . VAL B 1 309 ? 142.255 128.598 152.289 1.00 12692. ? 309 VAL B CB    1 
ATOM   6345  C  CG1   . VAL B 1 309 ? 142.130 129.280 153.640 1.00 12697. ? 309 VAL B CG1   1 
ATOM   6346  C  CG2   . VAL B 1 309 ? 143.325 127.530 152.334 1.00 12600. ? 309 VAL B CG2   1 
ATOM   6347  N  N     . GLY B 1 310 ? 139.525 129.884 151.175 1.00 12736. ? 310 GLY B N     1 
ATOM   6348  C  CA    . GLY B 1 310 ? 138.462 130.859 151.353 1.00 12742. ? 310 GLY B CA    1 
ATOM   6349  C  C     . GLY B 1 310 ? 137.089 130.226 151.472 1.00 12742. ? 310 GLY B C     1 
ATOM   6350  O  O     . GLY B 1 310 ? 136.231 130.720 152.206 1.00 12748. ? 310 GLY B O     1 
ATOM   6351  N  N     . GLY B 1 311 ? 136.857 129.134 150.752 1.00 12743. ? 311 GLY B N     1 
ATOM   6352  C  CA    . GLY B 1 311 ? 135.591 128.440 150.870 1.00 12746. ? 311 GLY B CA    1 
ATOM   6353  C  C     . GLY B 1 311 ? 135.048 127.865 149.579 1.00 12751. ? 311 GLY B C     1 
ATOM   6354  O  O     . GLY B 1 311 ? 134.153 127.018 149.607 1.00 12765. ? 311 GLY B O     1 
ATOM   6355  N  N     . ILE B 1 312 ? 135.569 128.314 148.442 1.00 12734. ? 312 ILE B N     1 
ATOM   6356  C  CA    . ILE B 1 312 ? 135.127 127.800 147.150 1.00 12733. ? 312 ILE B CA    1 
ATOM   6357  C  C     . ILE B 1 312 ? 135.775 126.440 146.927 1.00 12733. ? 312 ILE B C     1 
ATOM   6358  O  O     . ILE B 1 312 ? 136.980 126.348 146.674 1.00 12742. ? 312 ILE B O     1 
ATOM   6359  C  CB    . ILE B 1 312 ? 135.473 128.775 146.018 1.00 12740. ? 312 ILE B CB    1 
ATOM   6360  C  CG1   . ILE B 1 312 ? 135.163 130.208 146.447 1.00 12747. ? 312 ILE B CG1   1 
ATOM   6361  C  CG2   . ILE B 1 312 ? 134.691 128.427 144.769 1.00 12737. ? 312 ILE B CG2   1 
ATOM   6362  C  CD1   . ILE B 1 312 ? 135.694 131.251 145.500 1.00 12757. ? 312 ILE B CD1   1 
ATOM   6363  N  N     . ASP B 1 313 ? 134.970 125.381 147.014 1.00 12721. ? 313 ASP B N     1 
ATOM   6364  C  CA    . ASP B 1 313 ? 135.514 124.029 147.069 1.00 12727. ? 313 ASP B CA    1 
ATOM   6365  C  C     . ASP B 1 313 ? 136.133 123.596 145.746 1.00 12738. ? 313 ASP B C     1 
ATOM   6366  O  O     . ASP B 1 313 ? 137.199 122.973 145.736 1.00 12744. ? 313 ASP B O     1 
ATOM   6367  C  CB    . ASP B 1 313 ? 134.422 123.048 147.491 1.00 12720. ? 313 ASP B CB    1 
ATOM   6368  C  CG    . ASP B 1 313 ? 134.015 123.224 148.938 1.00 12722. ? 313 ASP B CG    1 
ATOM   6369  O  OD1   . ASP B 1 313 ? 134.900 123.150 149.816 1.00 12737. ? 313 ASP B OD1   1 
ATOM   6370  O  OD2   . ASP B 1 313 ? 132.814 123.439 149.200 1.00 12727. ? 313 ASP B OD2   1 
ATOM   6371  N  N     . ARG B 1 314 ? 135.488 123.907 144.628 1.00 12741. ? 314 ARG B N     1 
ATOM   6372  C  CA    . ARG B 1 314 ? 135.952 123.485 143.310 1.00 12728. ? 314 ARG B CA    1 
ATOM   6373  C  C     . ARG B 1 314 ? 136.227 124.726 142.476 1.00 12730. ? 314 ARG B C     1 
ATOM   6374  O  O     . ARG B 1 314 ? 135.315 125.518 142.218 1.00 12745. ? 314 ARG B O     1 
ATOM   6375  C  CB    . ARG B 1 314 ? 134.922 122.582 142.637 1.00 12729. ? 314 ARG B CB    1 
ATOM   6376  C  CG    . ARG B 1 314 ? 134.635 121.322 143.419 1.00 12727. ? 314 ARG B CG    1 
ATOM   6377  C  CD    . ARG B 1 314 ? 133.672 120.413 142.695 1.00 12672. ? 314 ARG B CD    1 
ATOM   6378  N  NE    . ARG B 1 314 ? 133.270 119.297 143.540 1.00 12588. ? 314 ARG B NE    1 
ATOM   6379  C  CZ    . ARG B 1 314 ? 132.492 118.300 143.145 1.00 12538. ? 314 ARG B CZ    1 
ATOM   6380  N  NH1   . ARG B 1 314 ? 132.008 118.246 141.917 1.00 12584. ? 314 ARG B NH1   1 
ATOM   6381  N  NH2   . ARG B 1 314 ? 132.192 117.333 144.006 1.00 12245. ? 314 ARG B NH2   1 
ATOM   6382  N  N     . VAL B 1 315 ? 137.479 124.900 142.060 1.00 12724. ? 315 VAL B N     1 
ATOM   6383  C  CA    . VAL B 1 315 ? 137.860 126.042 141.240 1.00 12718. ? 315 VAL B CA    1 
ATOM   6384  C  C     . VAL B 1 315 ? 138.646 125.539 140.040 1.00 12732. ? 315 VAL B C     1 
ATOM   6385  O  O     . VAL B 1 315 ? 139.199 124.440 140.047 1.00 12755. ? 315 VAL B O     1 
ATOM   6386  C  CB    . VAL B 1 315 ? 138.684 127.082 142.024 1.00 12713. ? 315 VAL B CB    1 
ATOM   6387  C  CG1   . VAL B 1 315 ? 137.811 127.802 143.030 1.00 12732. ? 315 VAL B CG1   1 
ATOM   6388  C  CG2   . VAL B 1 315 ? 139.856 126.416 142.713 1.00 12741. ? 315 VAL B CG2   1 
ATOM   6389  N  N     . TYR B 1 316 ? 138.687 126.361 138.996 1.00 12730. ? 316 TYR B N     1 
ATOM   6390  C  CA    . TYR B 1 316 ? 139.500 126.041 137.832 1.00 12724. ? 316 TYR B CA    1 
ATOM   6391  C  C     . TYR B 1 316 ? 139.791 127.315 137.059 1.00 12722. ? 316 TYR B C     1 
ATOM   6392  O  O     . TYR B 1 316 ? 139.118 128.335 137.223 1.00 12746. ? 316 TYR B O     1 
ATOM   6393  C  CB    . TYR B 1 316 ? 138.827 124.995 136.938 1.00 12731. ? 316 TYR B CB    1 
ATOM   6394  C  CG    . TYR B 1 316 ? 137.870 125.542 135.907 1.00 12727. ? 316 TYR B CG    1 
ATOM   6395  C  CD1   . TYR B 1 316 ? 136.542 125.774 136.222 1.00 12759. ? 316 TYR B CD1   1 
ATOM   6396  C  CD2   . TYR B 1 316 ? 138.288 125.802 134.610 1.00 12731. ? 316 TYR B CD2   1 
ATOM   6397  C  CE1   . TYR B 1 316 ? 135.663 126.260 135.285 1.00 12767. ? 316 TYR B CE1   1 
ATOM   6398  C  CE2   . TYR B 1 316 ? 137.414 126.292 133.667 1.00 12747. ? 316 TYR B CE2   1 
ATOM   6399  C  CZ    . TYR B 1 316 ? 136.103 126.518 134.011 1.00 12751. ? 316 TYR B CZ    1 
ATOM   6400  O  OH    . TYR B 1 316 ? 135.221 127.007 133.078 1.00 12754. ? 316 TYR B OH    1 
ATOM   6401  N  N     . GLU B 1 317 ? 140.814 127.236 136.215 1.00 12716. ? 317 GLU B N     1 
ATOM   6402  C  CA    . GLU B 1 317 ? 141.275 128.381 135.444 1.00 12726. ? 317 GLU B CA    1 
ATOM   6403  C  C     . GLU B 1 317 ? 142.078 127.885 134.253 1.00 12738. ? 317 GLU B C     1 
ATOM   6404  O  O     . GLU B 1 317 ? 142.999 127.080 134.416 1.00 12758. ? 317 GLU B O     1 
ATOM   6405  C  CB    . GLU B 1 317 ? 142.126 129.315 136.308 1.00 12729. ? 317 GLU B CB    1 
ATOM   6406  C  CG    . GLU B 1 317 ? 143.204 130.061 135.548 1.00 12740. ? 317 GLU B CG    1 
ATOM   6407  C  CD    . GLU B 1 317 ? 143.444 131.450 136.093 1.00 12748. ? 317 GLU B CD    1 
ATOM   6408  O  OE1   . GLU B 1 317 ? 143.391 131.621 137.327 1.00 12755. ? 317 GLU B OE1   1 
ATOM   6409  O  OE2   . GLU B 1 317 ? 143.688 132.372 135.288 1.00 12757. ? 317 GLU B OE2   1 
ATOM   6410  N  N     . ILE B 1 318 ? 141.723 128.358 133.065 1.00 12735. ? 318 ILE B N     1 
ATOM   6411  C  CA    . ILE B 1 318 ? 142.490 128.113 131.851 1.00 12730. ? 318 ILE B CA    1 
ATOM   6412  C  C     . ILE B 1 318 ? 143.185 129.419 131.504 1.00 12734. ? 318 ILE B C     1 
ATOM   6413  O  O     . ILE B 1 318 ? 142.526 130.416 131.187 1.00 12734. ? 318 ILE B O     1 
ATOM   6414  C  CB    . ILE B 1 318 ? 141.606 127.625 130.696 1.00 12707. ? 318 ILE B CB    1 
ATOM   6415  C  CG1   . ILE B 1 318 ? 140.828 126.377 131.110 1.00 12719. ? 318 ILE B CG1   1 
ATOM   6416  C  CG2   . ILE B 1 318 ? 142.448 127.335 129.470 1.00 12721. ? 318 ILE B CG2   1 
ATOM   6417  C  CD1   . ILE B 1 318 ? 140.052 125.747 129.985 1.00 12726. ? 318 ILE B CD1   1 
ATOM   6418  N  N     . GLY B 1 319 ? 144.512 129.424 131.562 1.00 12735. ? 319 GLY B N     1 
ATOM   6419  C  CA    . GLY B 1 319 ? 145.233 130.671 131.414 1.00 12733. ? 319 GLY B CA    1 
ATOM   6420  C  C     . GLY B 1 319 ? 146.616 130.559 130.815 1.00 12737. ? 319 GLY B C     1 
ATOM   6421  O  O     . GLY B 1 319 ? 147.063 129.471 130.439 1.00 12753. ? 319 GLY B O     1 
ATOM   6422  N  N     . ARG B 1 320 ? 147.308 131.691 130.731 1.00 12728. ? 320 ARG B N     1 
ATOM   6423  C  CA    . ARG B 1 320 ? 148.626 131.777 130.121 1.00 12729. ? 320 ARG B CA    1 
ATOM   6424  C  C     . ARG B 1 320 ? 149.690 131.845 131.205 1.00 12733. ? 320 ARG B C     1 
ATOM   6425  O  O     . ARG B 1 320 ? 149.612 132.684 132.107 1.00 12753. ? 320 ARG B O     1 
ATOM   6426  C  CB    . ARG B 1 320 ? 148.727 133.003 129.212 1.00 12741. ? 320 ARG B CB    1 
ATOM   6427  C  CG    . ARG B 1 320 ? 149.604 132.799 127.993 1.00 12755. ? 320 ARG B CG    1 
ATOM   6428  C  CD    . ARG B 1 320 ? 148.802 132.265 126.821 1.00 12749. ? 320 ARG B CD    1 
ATOM   6429  N  NE    . ARG B 1 320 ? 147.690 133.143 126.481 1.00 12739. ? 320 ARG B NE    1 
ATOM   6430  C  CZ    . ARG B 1 320 ? 147.699 134.004 125.473 1.00 12747. ? 320 ARG B CZ    1 
ATOM   6431  N  NH1   . ARG B 1 320 ? 148.749 134.126 124.678 1.00 12755. ? 320 ARG B NH1   1 
ATOM   6432  N  NH2   . ARG B 1 320 ? 146.630 134.765 125.260 1.00 12751. ? 320 ARG B NH2   1 
ATOM   6433  N  N     . GLN B 1 321 ? 150.678 130.962 131.110 1.00 12728. ? 321 GLN B N     1 
ATOM   6434  C  CA    . GLN B 1 321 ? 151.828 130.944 131.995 1.00 12734. ? 321 GLN B CA    1 
ATOM   6435  C  C     . GLN B 1 321 ? 153.079 131.287 131.201 1.00 12745. ? 321 GLN B C     1 
ATOM   6436  O  O     . GLN B 1 321 ? 153.194 130.953 130.016 1.00 12775. ? 321 GLN B O     1 
ATOM   6437  C  CB    . GLN B 1 321 ? 151.989 129.578 132.664 1.00 12744. ? 321 GLN B CB    1 
ATOM   6438  C  CG    . GLN B 1 321 ? 150.685 128.835 132.875 1.00 12751. ? 321 GLN B CG    1 
ATOM   6439  C  CD    . GLN B 1 321 ? 149.806 129.470 133.933 1.00 12760. ? 321 GLN B CD    1 
ATOM   6440  O  OE1   . GLN B 1 321 ? 150.223 130.386 134.639 1.00 12768. ? 321 GLN B OE1   1 
ATOM   6441  N  NE2   . GLN B 1 321 ? 148.577 128.985 134.044 1.00 12762. ? 321 GLN B NE2   1 
ATOM   6442  N  N     . PHE B 1 322 ? 154.017 131.953 131.868 1.00 12742. ? 322 PHE B N     1 
ATOM   6443  C  CA    . PHE B 1 322 ? 155.209 132.497 131.239 1.00 12743. ? 322 PHE B CA    1 
ATOM   6444  C  C     . PHE B 1 322 ? 156.452 131.831 131.808 1.00 12765. ? 322 PHE B C     1 
ATOM   6445  O  O     . PHE B 1 322 ? 156.550 131.610 133.018 1.00 12774. ? 322 PHE B O     1 
ATOM   6446  C  CB    . PHE B 1 322 ? 155.286 134.010 131.446 1.00 12734. ? 322 PHE B CB    1 
ATOM   6447  C  CG    . PHE B 1 322 ? 154.010 134.728 131.123 1.00 12731. ? 322 PHE B CG    1 
ATOM   6448  C  CD1   . PHE B 1 322 ? 153.684 135.031 129.815 1.00 12745. ? 322 PHE B CD1   1 
ATOM   6449  C  CD2   . PHE B 1 322 ? 153.132 135.090 132.127 1.00 12741. ? 322 PHE B CD2   1 
ATOM   6450  C  CE1   . PHE B 1 322 ? 152.510 135.687 129.515 1.00 12747. ? 322 PHE B CE1   1 
ATOM   6451  C  CE2   . PHE B 1 322 ? 151.957 135.746 131.832 1.00 12742. ? 322 PHE B CE2   1 
ATOM   6452  C  CZ    . PHE B 1 322 ? 151.646 136.044 130.525 1.00 12740. ? 322 PHE B CZ    1 
ATOM   6453  N  N     . ARG B 1 323 ? 157.403 131.518 130.930 1.00 13361. ? 323 ARG B N     1 
ATOM   6454  C  CA    . ARG B 1 323 ? 158.642 130.860 131.321 1.00 13374. ? 323 ARG B CA    1 
ATOM   6455  C  C     . ARG B 1 323 ? 159.807 131.487 130.574 1.00 13377. ? 323 ARG B C     1 
ATOM   6456  O  O     . ARG B 1 323 ? 159.758 131.624 129.349 1.00 13402. ? 323 ARG B O     1 
ATOM   6457  C  CB    . ARG B 1 323 ? 158.579 129.358 131.039 1.00 13378. ? 323 ARG B CB    1 
ATOM   6458  C  CG    . ARG B 1 323 ? 158.357 128.519 132.277 1.00 13401. ? 323 ARG B CG    1 
ATOM   6459  C  CD    . ARG B 1 323 ? 157.885 127.121 131.926 1.00 13331. ? 323 ARG B CD    1 
ATOM   6460  N  NE    . ARG B 1 323 ? 157.547 126.327 133.103 1.00 13341. ? 323 ARG B NE    1 
ATOM   6461  C  CZ    . ARG B 1 323 ? 156.542 126.583 133.931 1.00 13359. ? 323 ARG B CZ    1 
ATOM   6462  N  NH1   . ARG B 1 323 ? 155.740 127.620 133.750 1.00 13402. ? 323 ARG B NH1   1 
ATOM   6463  N  NH2   . ARG B 1 323 ? 156.334 125.776 134.967 1.00 13342. ? 323 ARG B NH2   1 
ATOM   6464  N  N     . ASN B 1 324 ? 160.848 131.859 131.311 1.00 12777. ? 324 ASN B N     1 
ATOM   6465  C  CA    . ASN B 1 324 ? 162.027 132.497 130.727 1.00 12776. ? 324 ASN B CA    1 
ATOM   6466  C  C     . ASN B 1 324 ? 163.105 131.476 130.377 1.00 12829. ? 324 ASN B C     1 
ATOM   6467  O  O     . ASN B 1 324 ? 164.252 131.583 130.804 1.00 12816. ? 324 ASN B O     1 
ATOM   6468  C  CB    . ASN B 1 324 ? 162.566 133.554 131.681 1.00 12755. ? 324 ASN B CB    1 
ATOM   6469  C  CG    . ASN B 1 324 ? 163.438 134.575 130.986 1.00 12756. ? 324 ASN B CG    1 
ATOM   6470  O  OD1   . ASN B 1 324 ? 163.809 134.406 129.827 1.00 12783. ? 324 ASN B OD1   1 
ATOM   6471  N  ND2   . ASN B 1 324 ? 163.771 135.646 131.693 1.00 12770. ? 324 ASN B ND2   1 
ATOM   6472  N  N     . GLU B 1 325 ? 162.740 130.473 129.589 1.00 14986. ? 325 GLU B N     1 
ATOM   6473  C  CA    . GLU B 1 325 ? 163.669 129.457 129.127 1.00 15043. ? 325 GLU B CA    1 
ATOM   6474  C  C     . GLU B 1 325 ? 163.890 129.612 127.624 1.00 15057. ? 325 GLU B C     1 
ATOM   6475  O  O     . GLU B 1 325 ? 163.408 130.561 126.997 1.00 15053. ? 325 GLU B O     1 
ATOM   6476  C  CB    . GLU B 1 325 ? 163.153 128.063 129.488 1.00 15060. ? 325 GLU B CB    1 
ATOM   6477  C  CG    . GLU B 1 325 ? 161.663 127.877 129.278 1.00 15039. ? 325 GLU B CG    1 
ATOM   6478  C  CD    . GLU B 1 325 ? 161.198 126.475 129.618 1.00 15019. ? 325 GLU B CD    1 
ATOM   6479  O  OE1   . GLU B 1 325 ? 160.901 126.217 130.803 1.00 15021. ? 325 GLU B OE1   1 
ATOM   6480  O  OE2   . GLU B 1 325 ? 161.131 125.632 128.700 1.00 15019. ? 325 GLU B OE2   1 
ATOM   6481  N  N     . GLY B 1 326 ? 164.629 128.670 127.045 1.00 15116. ? 326 GLY B N     1 
ATOM   6482  C  CA    . GLY B 1 326 ? 164.933 128.746 125.630 1.00 15132. ? 326 GLY B CA    1 
ATOM   6483  C  C     . GLY B 1 326 ? 163.718 128.478 124.762 1.00 15128. ? 326 GLY B C     1 
ATOM   6484  O  O     . GLY B 1 326 ? 162.745 127.851 125.178 1.00 15131. ? 326 GLY B O     1 
ATOM   6485  N  N     . ILE B 1 327 ? 163.786 128.969 123.528 1.00 14939. ? 327 ILE B N     1 
ATOM   6486  C  CA    . ILE B 1 327 ? 162.726 128.792 122.542 1.00 14934. ? 327 ILE B CA    1 
ATOM   6487  C  C     . ILE B 1 327 ? 163.167 127.714 121.564 1.00 14911. ? 327 ILE B C     1 
ATOM   6488  O  O     . ILE B 1 327 ? 164.231 127.824 120.944 1.00 14897. ? 327 ILE B O     1 
ATOM   6489  C  CB    . ILE B 1 327 ? 162.416 130.106 121.809 1.00 14911. ? 327 ILE B CB    1 
ATOM   6490  C  CG1   . ILE B 1 327 ? 161.818 131.131 122.770 1.00 14894. ? 327 ILE B CG1   1 
ATOM   6491  C  CG2   . ILE B 1 327 ? 161.468 129.855 120.652 1.00 14833. ? 327 ILE B CG2   1 
ATOM   6492  C  CD1   . ILE B 1 327 ? 161.590 132.484 122.141 1.00 14859. ? 327 ILE B CD1   1 
ATOM   6493  N  N     . ASP B 1 328 ? 162.353 126.673 121.421 1.00 15371. ? 328 ASP B N     1 
ATOM   6494  C  CA    . ASP B 1 328 ? 162.669 125.560 120.538 1.00 15383. ? 328 ASP B CA    1 
ATOM   6495  C  C     . ASP B 1 328 ? 161.386 125.123 119.840 1.00 15338. ? 328 ASP B C     1 
ATOM   6496  O  O     . ASP B 1 328 ? 160.379 125.837 119.841 1.00 15303. ? 328 ASP B O     1 
ATOM   6497  C  CB    . ASP B 1 328 ? 163.331 124.416 121.318 1.00 15399. ? 328 ASP B CB    1 
ATOM   6498  C  CG    . ASP B 1 328 ? 162.549 124.023 122.556 1.00 15385. ? 328 ASP B CG    1 
ATOM   6499  O  OD1   . ASP B 1 328 ? 161.354 123.684 122.428 1.00 15362. ? 328 ASP B OD1   1 
ATOM   6500  O  OD2   . ASP B 1 328 ? 163.130 124.051 123.660 1.00 15401. ? 328 ASP B OD2   1 
ATOM   6501  N  N     . LEU B 1 329 ? 161.427 123.938 119.237 1.00 14802. ? 329 LEU B N     1 
ATOM   6502  C  CA    . LEU B 1 329 ? 160.279 123.393 118.527 1.00 14730. ? 329 LEU B CA    1 
ATOM   6503  C  C     . LEU B 1 329 ? 159.257 122.752 119.455 1.00 14668. ? 329 LEU B C     1 
ATOM   6504  O  O     . LEU B 1 329 ? 158.271 122.189 118.969 1.00 14486. ? 329 LEU B O     1 
ATOM   6505  C  CB    . LEU B 1 329 ? 160.744 122.369 117.488 1.00 14742. ? 329 LEU B CB    1 
ATOM   6506  C  CG    . LEU B 1 329 ? 161.316 122.934 116.186 1.00 14747. ? 329 LEU B CG    1 
ATOM   6507  C  CD1   . LEU B 1 329 ? 161.388 121.855 115.120 1.00 14752. ? 329 LEU B CD1   1 
ATOM   6508  C  CD2   . LEU B 1 329 ? 160.498 124.120 115.700 1.00 14660. ? 329 LEU B CD2   1 
ATOM   6509  N  N     . THR B 1 330 ? 159.468 122.809 120.769 1.00 14335. ? 330 THR B N     1 
ATOM   6510  C  CA    . THR B 1 330 ? 158.527 122.248 121.724 1.00 14330. ? 330 THR B CA    1 
ATOM   6511  C  C     . THR B 1 330 ? 158.230 123.178 122.893 1.00 14293. ? 330 THR B C     1 
ATOM   6512  O  O     . THR B 1 330 ? 157.290 122.908 123.649 1.00 14227. ? 330 THR B O     1 
ATOM   6513  C  CB    . THR B 1 330 ? 159.053 120.908 122.263 1.00 14384. ? 330 THR B CB    1 
ATOM   6514  O  OG1   . THR B 1 330 ? 159.665 120.178 121.194 1.00 14388. ? 330 THR B OG1   1 
ATOM   6515  C  CG2   . THR B 1 330 ? 157.918 120.065 122.829 1.00 14305. ? 330 THR B CG2   1 
ATOM   6516  N  N     . HIS B 1 331 ? 158.977 124.266 123.055 1.00 14607. ? 331 HIS B N     1 
ATOM   6517  C  CA    . HIS B 1 331 ? 158.808 125.178 124.176 1.00 14550. ? 331 HIS B CA    1 
ATOM   6518  C  C     . HIS B 1 331 ? 158.561 126.592 123.671 1.00 14537. ? 331 HIS B C     1 
ATOM   6519  O  O     . HIS B 1 331 ? 159.194 127.038 122.710 1.00 14627. ? 331 HIS B O     1 
ATOM   6520  C  CB    . HIS B 1 331 ? 160.036 125.153 125.087 1.00 14630. ? 331 HIS B CB    1 
ATOM   6521  C  CG    . HIS B 1 331 ? 160.213 123.861 125.822 1.00 14640. ? 331 HIS B CG    1 
ATOM   6522  N  ND1   . HIS B 1 331 ? 161.159 122.925 125.464 1.00 14719. ? 331 HIS B ND1   1 
ATOM   6523  C  CD2   . HIS B 1 331 ? 159.560 123.346 126.889 1.00 14540. ? 331 HIS B CD2   1 
ATOM   6524  C  CE1   . HIS B 1 331 ? 161.083 121.890 126.281 1.00 14715. ? 331 HIS B CE1   1 
ATOM   6525  N  NE2   . HIS B 1 331 ? 160.120 122.120 127.156 1.00 14648. ? 331 HIS B NE2   1 
ATOM   6526  N  N     . ASN B 1 332 ? 157.640 127.291 124.326 1.00 12678. ? 332 ASN B N     1 
ATOM   6527  C  CA    . ASN B 1 332 ? 157.308 128.670 124.013 1.00 12710. ? 332 ASN B CA    1 
ATOM   6528  C  C     . ASN B 1 332 ? 157.348 129.507 125.282 1.00 12709. ? 332 ASN B C     1 
ATOM   6529  O  O     . ASN B 1 332 ? 157.082 128.996 126.374 1.00 12668. ? 332 ASN B O     1 
ATOM   6530  C  CB    . ASN B 1 332 ? 155.917 128.776 123.375 1.00 12663. ? 332 ASN B CB    1 
ATOM   6531  C  CG    . ASN B 1 332 ? 155.860 129.806 122.269 1.00 12619. ? 332 ASN B CG    1 
ATOM   6532  O  OD1   . ASN B 1 332 ? 156.532 129.675 121.248 1.00 12540. ? 332 ASN B OD1   1 
ATOM   6533  N  ND2   . ASN B 1 332 ? 155.056 130.842 122.467 1.00 12590. ? 332 ASN B ND2   1 
ATOM   6534  N  N     . PRO B 1 333 ? 157.690 130.794 125.171 1.00 12737. ? 333 PRO B N     1 
ATOM   6535  C  CA    . PRO B 1 333 ? 157.711 131.643 126.375 1.00 12735. ? 333 PRO B CA    1 
ATOM   6536  C  C     . PRO B 1 333 ? 156.377 131.711 127.095 1.00 12750. ? 333 PRO B C     1 
ATOM   6537  O  O     . PRO B 1 333 ? 156.350 131.739 128.330 1.00 12770. ? 333 PRO B O     1 
ATOM   6538  C  CB    . PRO B 1 333 ? 158.132 133.013 125.827 1.00 12739. ? 333 PRO B CB    1 
ATOM   6539  C  CG    . PRO B 1 333 ? 158.857 132.716 124.573 1.00 12726. ? 333 PRO B CG    1 
ATOM   6540  C  CD    . PRO B 1 333 ? 158.231 131.489 123.992 1.00 12750. ? 333 PRO B CD    1 
ATOM   6541  N  N     . GLU B 1 334 ? 155.267 131.735 126.364 1.00 12742. ? 334 GLU B N     1 
ATOM   6542  C  CA    . GLU B 1 334 ? 153.937 131.790 126.954 1.00 12744. ? 334 GLU B CA    1 
ATOM   6543  C  C     . GLU B 1 334 ? 153.121 130.616 126.440 1.00 12741. ? 334 GLU B C     1 
ATOM   6544  O  O     . GLU B 1 334 ? 153.087 130.362 125.233 1.00 12738. ? 334 GLU B O     1 
ATOM   6545  C  CB    . GLU B 1 334 ? 153.238 133.109 126.623 1.00 12735. ? 334 GLU B CB    1 
ATOM   6546  C  CG    . GLU B 1 334 ? 153.587 133.664 125.258 1.00 12746. ? 334 GLU B CG    1 
ATOM   6547  C  CD    . GLU B 1 334 ? 152.652 134.772 124.826 1.00 12755. ? 334 GLU B CD    1 
ATOM   6548  O  OE1   . GLU B 1 334 ? 151.457 134.717 125.182 1.00 12749. ? 334 GLU B OE1   1 
ATOM   6549  O  OE2   . GLU B 1 334 ? 153.111 135.701 124.129 1.00 12771. ? 334 GLU B OE2   1 
ATOM   6550  N  N     . PHE B 1 335 ? 152.465 129.906 127.353 1.00 12736. ? 335 PHE B N     1 
ATOM   6551  C  CA    . PHE B 1 335 ? 151.719 128.712 126.987 1.00 12668. ? 335 PHE B CA    1 
ATOM   6552  C  C     . PHE B 1 335 ? 150.464 128.601 127.837 1.00 12684. ? 335 PHE B C     1 
ATOM   6553  O  O     . PHE B 1 335 ? 150.411 129.100 128.961 1.00 12740. ? 335 PHE B O     1 
ATOM   6554  C  CB    . PHE B 1 335 ? 152.576 127.448 127.134 1.00 12601. ? 335 PHE B CB    1 
ATOM   6555  C  CG    . PHE B 1 335 ? 153.191 127.286 128.492 1.00 12595. ? 335 PHE B CG    1 
ATOM   6556  C  CD1   . PHE B 1 335 ? 154.339 127.977 128.835 1.00 12608. ? 335 PHE B CD1   1 
ATOM   6557  C  CD2   . PHE B 1 335 ? 152.628 126.436 129.422 1.00 12603. ? 335 PHE B CD2   1 
ATOM   6558  C  CE1   . PHE B 1 335 ? 154.903 127.830 130.078 1.00 12623. ? 335 PHE B CE1   1 
ATOM   6559  C  CE2   . PHE B 1 335 ? 153.190 126.284 130.668 1.00 12635. ? 335 PHE B CE2   1 
ATOM   6560  C  CZ    . PHE B 1 335 ? 154.328 126.982 130.995 1.00 12635. ? 335 PHE B CZ    1 
ATOM   6561  N  N     . THR B 1 336 ? 149.456 127.926 127.296 1.00 12650. ? 336 THR B N     1 
ATOM   6562  C  CA    . THR B 1 336 ? 148.149 127.825 127.930 1.00 12665. ? 336 THR B CA    1 
ATOM   6563  C  C     . THR B 1 336 ? 148.053 126.535 128.732 1.00 12596. ? 336 THR B C     1 
ATOM   6564  O  O     . THR B 1 336 ? 148.386 125.458 128.228 1.00 12424. ? 336 THR B O     1 
ATOM   6565  C  CB    . THR B 1 336 ? 147.034 127.876 126.885 1.00 12653. ? 336 THR B CB    1 
ATOM   6566  O  OG1   . THR B 1 336 ? 147.300 128.932 125.955 1.00 12702. ? 336 THR B OG1   1 
ATOM   6567  C  CG2   . THR B 1 336 ? 145.694 128.128 127.549 1.00 12710. ? 336 THR B CG2   1 
ATOM   6568  N  N     . THR B 1 337 ? 147.605 126.651 129.981 1.00 12673. ? 337 THR B N     1 
ATOM   6569  C  CA    . THR B 1 337 ? 147.408 125.499 130.848 1.00 12575. ? 337 THR B CA    1 
ATOM   6570  C  C     . THR B 1 337 ? 146.065 125.611 131.553 1.00 12643. ? 337 THR B C     1 
ATOM   6571  O  O     . THR B 1 337 ? 145.550 126.706 131.790 1.00 12710. ? 337 THR B O     1 
ATOM   6572  C  CB    . THR B 1 337 ? 148.513 125.359 131.905 1.00 12664. ? 337 THR B CB    1 
ATOM   6573  O  OG1   . THR B 1 337 ? 148.458 126.469 132.809 1.00 12741. ? 337 THR B OG1   1 
ATOM   6574  C  CG2   . THR B 1 337 ? 149.881 125.297 131.261 1.00 12649. ? 337 THR B CG2   1 
ATOM   6575  N  N     . CYS B 1 338 ? 145.513 124.454 131.901 1.00 12583. ? 338 CYS B N     1 
ATOM   6576  C  CA    . CYS B 1 338 ? 144.290 124.359 132.684 1.00 12647. ? 338 CYS B CA    1 
ATOM   6577  C  C     . CYS B 1 338 ? 144.619 123.805 134.061 1.00 12608. ? 338 CYS B C     1 
ATOM   6578  O  O     . CYS B 1 338 ? 145.192 122.719 134.175 1.00 12423. ? 338 CYS B O     1 
ATOM   6579  C  CB    . CYS B 1 338 ? 143.260 123.465 131.994 1.00 12606. ? 338 CYS B CB    1 
ATOM   6580  S  SG    . CYS B 1 338 ? 141.702 123.318 132.890 1.00 12648. ? 338 CYS B SG    1 
ATOM   6581  N  N     . GLU B 1 339 ? 144.205 124.512 135.117 1.00 12709. ? 339 GLU B N     1 
ATOM   6582  C  CA    . GLU B 1 339 ? 144.425 123.988 136.493 1.00 12634. ? 339 GLU B CA    1 
ATOM   6583  C  C     . GLU B 1 339 ? 143.107 124.003 137.285 1.00 12680. ? 339 GLU B C     1 
ATOM   6584  O  O     . GLU B 1 339 ? 142.614 125.113 137.580 1.00 12748. ? 339 GLU B O     1 
ATOM   6585  C  CB    . GLU B 1 339 ? 145.490 124.795 137.237 1.00 12710. ? 339 GLU B CB    1 
ATOM   6586  C  CG    . GLU B 1 339 ? 146.882 124.668 136.625 1.00 12679. ? 339 GLU B CG    1 
ATOM   6587  C  CD    . GLU B 1 339 ? 148.009 125.011 137.580 1.00 12616. ? 339 GLU B CD    1 
ATOM   6588  O  OE1   . GLU B 1 339 ? 147.722 125.314 138.758 1.00 12645. ? 339 GLU B OE1   1 
ATOM   6589  O  OE2   . GLU B 1 339 ? 149.178 124.980 137.142 1.00 12592. ? 339 GLU B OE2   1 
ATOM   6590  N  N     . PHE B 1 340 ? 142.571 122.824 137.625 1.00 12594. ? 340 PHE B N     1 
ATOM   6591  C  CA    . PHE B 1 340 ? 141.347 122.773 138.475 1.00 12655. ? 340 PHE B CA    1 
ATOM   6592  C  C     . PHE B 1 340 ? 141.743 122.287 139.873 1.00 12600. ? 340 PHE B C     1 
ATOM   6593  O  O     . PHE B 1 340 ? 142.738 121.539 140.002 1.00 12495. ? 340 PHE B O     1 
ATOM   6594  C  CB    . PHE B 1 340 ? 140.204 121.923 137.902 1.00 12684. ? 340 PHE B CB    1 
ATOM   6595  C  CG    . PHE B 1 340 ? 140.298 120.409 138.044 1.00 12605. ? 340 PHE B CG    1 
ATOM   6596  C  CD1   . PHE B 1 340 ? 140.065 119.784 139.264 1.00 12665. ? 340 PHE B CD1   1 
ATOM   6597  C  CD2   . PHE B 1 340 ? 140.543 119.605 136.938 1.00 12559. ? 340 PHE B CD2   1 
ATOM   6598  C  CE1   . PHE B 1 340 ? 140.133 118.406 139.384 1.00 12694. ? 340 PHE B CE1   1 
ATOM   6599  C  CE2   . PHE B 1 340 ? 140.606 118.225 137.062 1.00 12573. ? 340 PHE B CE2   1 
ATOM   6600  C  CZ    . PHE B 1 340 ? 140.401 117.629 138.283 1.00 12652. ? 340 PHE B CZ    1 
ATOM   6601  N  N     . TYR B 1 341 ? 140.982 122.700 140.892 1.00 12700. ? 341 TYR B N     1 
ATOM   6602  C  CA    . TYR B 1 341 ? 141.292 122.301 142.294 1.00 12646. ? 341 TYR B CA    1 
ATOM   6603  C  C     . TYR B 1 341 ? 140.011 121.818 142.972 1.00 12685. ? 341 TYR B C     1 
ATOM   6604  O  O     . TYR B 1 341 ? 139.040 122.599 143.058 1.00 12739. ? 341 TYR B O     1 
ATOM   6605  C  CB    . TYR B 1 341 ? 141.994 123.470 142.994 1.00 12699. ? 341 TYR B CB    1 
ATOM   6606  C  CG    . TYR B 1 341 ? 143.460 123.599 142.605 1.00 12658. ? 341 TYR B CG    1 
ATOM   6607  C  CD1   . TYR B 1 341 ? 143.836 124.249 141.435 1.00 12725. ? 341 TYR B CD1   1 
ATOM   6608  C  CD2   . TYR B 1 341 ? 144.467 123.072 143.404 1.00 12613. ? 341 TYR B CD2   1 
ATOM   6609  C  CE1   . TYR B 1 341 ? 145.166 124.365 141.068 1.00 12664. ? 341 TYR B CE1   1 
ATOM   6610  C  CE2   . TYR B 1 341 ? 145.801 123.186 143.050 1.00 12610. ? 341 TYR B CE2   1 
ATOM   6611  C  CZ    . TYR B 1 341 ? 146.151 123.834 141.879 1.00 12615. ? 341 TYR B CZ    1 
ATOM   6612  O  OH    . TYR B 1 341 ? 147.460 123.951 141.517 1.00 12611. ? 341 TYR B OH    1 
ATOM   6613  N  N     . MET B 1 342 ? 140.007 120.565 143.436 1.00 12627. ? 342 MET B N     1 
ATOM   6614  C  CA    . MET B 1 342 ? 138.841 119.983 144.076 1.00 12674. ? 342 MET B CA    1 
ATOM   6615  C  C     . MET B 1 342 ? 139.089 119.870 145.573 1.00 12592. ? 342 MET B C     1 
ATOM   6616  O  O     . MET B 1 342 ? 140.215 119.631 146.016 1.00 12449. ? 342 MET B O     1 
ATOM   6617  C  CB    . MET B 1 342 ? 138.545 118.599 143.498 1.00 12698. ? 342 MET B CB    1 
ATOM   6618  C  CG    . MET B 1 342 ? 137.084 118.290 143.259 1.00 12686. ? 342 MET B CG    1 
ATOM   6619  S  SD    . MET B 1 342 ? 136.895 116.739 142.362 1.00 12596. ? 342 MET B SD    1 
ATOM   6620  C  CE    . MET B 1 342 ? 135.481 117.098 141.330 1.00 12693. ? 342 MET B CE    1 
ATOM   6621  N  N     . ALA B 1 343 ? 138.030 120.046 146.351 1.00 12680. ? 343 ALA B N     1 
ATOM   6622  C  CA    . ALA B 1 343 ? 138.090 119.861 147.791 1.00 12612. ? 343 ALA B CA    1 
ATOM   6623  C  C     . ALA B 1 343 ? 137.517 118.501 148.168 1.00 12632. ? 343 ALA B C     1 
ATOM   6624  O  O     . ALA B 1 343 ? 136.671 117.942 147.467 1.00 12641. ? 343 ALA B O     1 
ATOM   6625  C  CB    . ALA B 1 343 ? 137.335 120.974 148.517 1.00 12677. ? 343 ALA B CB    1 
ATOM   6626  N  N     . TYR B 1 344 ? 137.999 117.973 149.293 1.00 12558. ? 344 TYR B N     1 
ATOM   6627  C  CA    . TYR B 1 344 ? 137.590 116.660 149.790 1.00 12632. ? 344 TYR B CA    1 
ATOM   6628  C  C     . TYR B 1 344 ? 137.856 115.569 148.761 1.00 12650. ? 344 TYR B C     1 
ATOM   6629  O  O     . TYR B 1 344 ? 137.071 114.631 148.612 1.00 12688. ? 344 TYR B O     1 
ATOM   6630  C  CB    . TYR B 1 344 ? 136.121 116.667 150.214 1.00 12672. ? 344 TYR B CB    1 
ATOM   6631  C  CG    . TYR B 1 344 ? 135.788 117.842 151.096 1.00 12670. ? 344 TYR B CG    1 
ATOM   6632  C  CD1   . TYR B 1 344 ? 136.448 118.037 152.298 1.00 12635. ? 344 TYR B CD1   1 
ATOM   6633  C  CD2   . TYR B 1 344 ? 134.836 118.772 150.714 1.00 12673. ? 344 TYR B CD2   1 
ATOM   6634  C  CE1   . TYR B 1 344 ? 136.157 119.116 153.102 1.00 12652. ? 344 TYR B CE1   1 
ATOM   6635  C  CE2   . TYR B 1 344 ? 134.540 119.855 151.511 1.00 12702. ? 344 TYR B CE2   1 
ATOM   6636  C  CZ    . TYR B 1 344 ? 135.203 120.022 152.704 1.00 12698. ? 344 TYR B CZ    1 
ATOM   6637  O  OH    . TYR B 1 344 ? 134.909 121.101 153.503 1.00 12716. ? 344 TYR B OH    1 
ATOM   6638  N  N     . ALA B 1 345 ? 138.970 115.691 148.047 1.00 12568. ? 345 ALA B N     1 
ATOM   6639  C  CA    . ALA B 1 345 ? 139.380 114.734 147.035 1.00 12632. ? 345 ALA B CA    1 
ATOM   6640  C  C     . ALA B 1 345 ? 140.842 114.374 147.248 1.00 12586. ? 345 ALA B C     1 
ATOM   6641  O  O     . ALA B 1 345 ? 141.573 115.044 147.981 1.00 12498. ? 345 ALA B O     1 
ATOM   6642  C  CB    . ALA B 1 345 ? 139.173 115.291 145.621 1.00 12635. ? 345 ALA B CB    1 
ATOM   6643  N  N     . ASP B 1 346 ? 141.264 113.295 146.598 1.00 12698. ? 346 ASP B N     1 
ATOM   6644  C  CA    . ASP B 1 346 ? 142.661 112.893 146.598 1.00 12708. ? 346 ASP B CA    1 
ATOM   6645  C  C     . ASP B 1 346 ? 143.048 112.545 145.170 1.00 12712. ? 346 ASP B C     1 
ATOM   6646  O  O     . ASP B 1 346 ? 142.214 112.551 144.263 1.00 12736. ? 346 ASP B O     1 
ATOM   6647  C  CB    . ASP B 1 346 ? 142.916 111.724 147.557 1.00 12741. ? 346 ASP B CB    1 
ATOM   6648  C  CG    . ASP B 1 346 ? 142.154 110.473 147.172 1.00 12745. ? 346 ASP B CG    1 
ATOM   6649  O  OD1   . ASP B 1 346 ? 141.178 110.577 146.402 1.00 12759. ? 346 ASP B OD1   1 
ATOM   6650  O  OD2   . ASP B 1 346 ? 142.528 109.380 147.646 1.00 12742. ? 346 ASP B OD2   1 
ATOM   6651  N  N     . TYR B 1 347 ? 144.333 112.244 144.972 1.00 12711. ? 347 TYR B N     1 
ATOM   6652  C  CA    . TYR B 1 347 ? 144.814 111.976 143.621 1.00 12722. ? 347 TYR B CA    1 
ATOM   6653  C  C     . TYR B 1 347 ? 144.188 110.717 143.036 1.00 12743. ? 347 TYR B C     1 
ATOM   6654  O  O     . TYR B 1 347 ? 144.147 110.558 141.812 1.00 12763. ? 347 TYR B O     1 
ATOM   6655  C  CB    . TYR B 1 347 ? 146.340 111.879 143.611 1.00 12754. ? 347 TYR B CB    1 
ATOM   6656  C  CG    . TYR B 1 347 ? 146.908 110.585 144.145 1.00 12745. ? 347 TYR B CG    1 
ATOM   6657  C  CD1   . TYR B 1 347 ? 146.590 110.132 145.415 1.00 12745. ? 347 TYR B CD1   1 
ATOM   6658  C  CD2   . TYR B 1 347 ? 147.780 109.826 143.380 1.00 12741. ? 347 TYR B CD2   1 
ATOM   6659  C  CE1   . TYR B 1 347 ? 147.115 108.955 145.902 1.00 12738. ? 347 TYR B CE1   1 
ATOM   6660  C  CE2   . TYR B 1 347 ? 148.310 108.651 143.859 1.00 12736. ? 347 TYR B CE2   1 
ATOM   6661  C  CZ    . TYR B 1 347 ? 147.975 108.220 145.119 1.00 12732. ? 347 TYR B CZ    1 
ATOM   6662  O  OH    . TYR B 1 347 ? 148.503 107.045 145.598 1.00 12747. ? 347 TYR B OH    1 
ATOM   6663  N  N     . HIS B 1 348 ? 143.678 109.822 143.882 1.00 12740. ? 348 HIS B N     1 
ATOM   6664  C  CA    . HIS B 1 348 ? 142.985 108.641 143.385 1.00 12734. ? 348 HIS B CA    1 
ATOM   6665  C  C     . HIS B 1 348 ? 141.655 108.972 142.725 1.00 12726. ? 348 HIS B C     1 
ATOM   6666  O  O     . HIS B 1 348 ? 141.174 108.178 141.911 1.00 12714. ? 348 HIS B O     1 
ATOM   6667  C  CB    . HIS B 1 348 ? 142.763 107.648 144.525 1.00 12741. ? 348 HIS B CB    1 
ATOM   6668  C  CG    . HIS B 1 348 ? 143.941 106.766 144.793 1.00 12733. ? 348 HIS B CG    1 
ATOM   6669  N  ND1   . HIS B 1 348 ? 144.770 106.309 143.792 1.00 12745. ? 348 HIS B ND1   1 
ATOM   6670  C  CD2   . HIS B 1 348 ? 144.431 106.260 145.948 1.00 12739. ? 348 HIS B CD2   1 
ATOM   6671  C  CE1   . HIS B 1 348 ? 145.719 105.557 144.319 1.00 12745. ? 348 HIS B CE1   1 
ATOM   6672  N  NE2   . HIS B 1 348 ? 145.536 105.511 145.626 1.00 12737. ? 348 HIS B NE2   1 
ATOM   6673  N  N     . ASP B 1 349 ? 141.050 110.112 143.057 1.00 12723. ? 349 ASP B N     1 
ATOM   6674  C  CA    . ASP B 1 349 ? 139.827 110.567 142.406 1.00 12716. ? 349 ASP B CA    1 
ATOM   6675  C  C     . ASP B 1 349 ? 140.136 111.345 141.133 1.00 12754. ? 349 ASP B C     1 
ATOM   6676  O  O     . ASP B 1 349 ? 139.456 111.182 140.111 1.00 12767. ? 349 ASP B O     1 
ATOM   6677  C  CB    . ASP B 1 349 ? 139.014 111.437 143.367 1.00 12687. ? 349 ASP B CB    1 
ATOM   6678  C  CG    . ASP B 1 349 ? 138.598 110.692 144.617 1.00 12659. ? 349 ASP B CG    1 
ATOM   6679  O  OD1   . ASP B 1 349 ? 138.982 109.515 144.765 1.00 12689. ? 349 ASP B OD1   1 
ATOM   6680  O  OD2   . ASP B 1 349 ? 137.888 111.285 145.454 1.00 12681. ? 349 ASP B OD2   1 
ATOM   6681  N  N     . LEU B 1 350 ? 141.155 112.202 141.188 1.00 12755. ? 350 LEU B N     1 
ATOM   6682  C  CA    . LEU B 1 350 ? 141.620 112.884 139.993 1.00 12742. ? 350 LEU B CA    1 
ATOM   6683  C  C     . LEU B 1 350 ? 142.113 111.915 138.937 1.00 12745. ? 350 LEU B C     1 
ATOM   6684  O  O     . LEU B 1 350 ? 141.993 112.214 137.749 1.00 12736. ? 350 LEU B O     1 
ATOM   6685  C  CB    . LEU B 1 350 ? 142.737 113.865 140.335 1.00 12699. ? 350 LEU B CB    1 
ATOM   6686  C  CG    . LEU B 1 350 ? 142.441 114.956 141.359 1.00 12601. ? 350 LEU B CG    1 
ATOM   6687  C  CD1   . LEU B 1 350 ? 143.451 116.069 141.205 1.00 12437. ? 350 LEU B CD1   1 
ATOM   6688  C  CD2   . LEU B 1 350 ? 141.030 115.490 141.206 1.00 12683. ? 350 LEU B CD2   1 
ATOM   6689  N  N     . MET B 1 351 ? 142.653 110.768 139.332 1.00 12749. ? 351 MET B N     1 
ATOM   6690  C  CA    . MET B 1 351 ? 143.103 109.774 138.374 1.00 12739. ? 351 MET B CA    1 
ATOM   6691  C  C     . MET B 1 351 ? 141.954 109.175 137.576 1.00 12734. ? 351 MET B C     1 
ATOM   6692  O  O     . MET B 1 351 ? 142.146 108.832 136.406 1.00 12757. ? 351 MET B O     1 
ATOM   6693  C  CB    . MET B 1 351 ? 143.883 108.674 139.101 1.00 12749. ? 351 MET B CB    1 
ATOM   6694  C  CG    . MET B 1 351 ? 144.341 107.528 138.231 1.00 12760. ? 351 MET B CG    1 
ATOM   6695  S  SD    . MET B 1 351 ? 145.458 106.411 139.100 1.00 12739. ? 351 MET B SD    1 
ATOM   6696  C  CE    . MET B 1 351 ? 146.317 107.555 140.175 1.00 12749. ? 351 MET B CE    1 
ATOM   6697  N  N     . GLU B 1 352 ? 140.767 109.055 138.169 1.00 12725. ? 352 GLU B N     1 
ATOM   6698  C  CA    . GLU B 1 352 ? 139.568 108.649 137.447 1.00 12728. ? 352 GLU B CA    1 
ATOM   6699  C  C     . GLU B 1 352 ? 138.953 109.777 136.635 1.00 12729. ? 352 GLU B C     1 
ATOM   6700  O  O     . GLU B 1 352 ? 138.519 109.550 135.498 1.00 12737. ? 352 GLU B O     1 
ATOM   6701  C  CB    . GLU B 1 352 ? 138.517 108.115 138.426 1.00 12727. ? 352 GLU B CB    1 
ATOM   6702  C  CG    . GLU B 1 352 ? 138.766 106.695 138.895 1.00 12726. ? 352 GLU B CG    1 
ATOM   6703  C  CD    . GLU B 1 352 ? 138.242 105.659 137.922 1.00 12740. ? 352 GLU B CD    1 
ATOM   6704  O  OE1   . GLU B 1 352 ? 137.691 106.050 136.871 1.00 12748. ? 352 GLU B OE1   1 
ATOM   6705  O  OE2   . GLU B 1 352 ? 138.381 104.451 138.207 1.00 12747. ? 352 GLU B OE2   1 
ATOM   6706  N  N     . ILE B 1 353 ? 138.911 110.986 137.196 1.00 12740. ? 353 ILE B N     1 
ATOM   6707  C  CA    . ILE B 1 353 ? 138.355 112.125 136.471 1.00 12715. ? 353 ILE B CA    1 
ATOM   6708  C  C     . ILE B 1 353 ? 139.177 112.427 135.223 1.00 12743. ? 353 ILE B C     1 
ATOM   6709  O  O     . ILE B 1 353 ? 138.622 112.724 134.159 1.00 12765. ? 353 ILE B O     1 
ATOM   6710  C  CB    . ILE B 1 353 ? 138.257 113.347 137.401 1.00 12714. ? 353 ILE B CB    1 
ATOM   6711  C  CG1   . ILE B 1 353 ? 137.145 113.141 138.429 1.00 12710. ? 353 ILE B CG1   1 
ATOM   6712  C  CG2   . ILE B 1 353 ? 138.013 114.613 136.605 1.00 12722. ? 353 ILE B CG2   1 
ATOM   6713  C  CD1   . ILE B 1 353 ? 137.037 114.257 139.436 1.00 12702. ? 353 ILE B CD1   1 
ATOM   6714  N  N     . THR B 1 354 ? 140.506 112.361 135.331 1.00 12741. ? 354 THR B N     1 
ATOM   6715  C  CA    . THR B 1 354 ? 141.368 112.604 134.181 1.00 12715. ? 354 THR B CA    1 
ATOM   6716  C  C     . THR B 1 354 ? 141.161 111.549 133.104 1.00 12736. ? 354 THR B C     1 
ATOM   6717  O  O     . THR B 1 354 ? 141.091 111.874 131.915 1.00 12760. ? 354 THR B O     1 
ATOM   6718  C  CB    . THR B 1 354 ? 142.830 112.637 134.626 1.00 12683. ? 354 THR B CB    1 
ATOM   6719  O  OG1   . THR B 1 354 ? 143.049 113.780 135.461 1.00 12592. ? 354 THR B OG1   1 
ATOM   6720  C  CG2   . THR B 1 354 ? 143.751 112.718 133.427 1.00 12673. ? 354 THR B CG2   1 
ATOM   6721  N  N     . GLU B 1 355 ? 141.062 110.278 133.502 1.00 12738. ? 355 GLU B N     1 
ATOM   6722  C  CA    . GLU B 1 355 ? 140.745 109.225 132.544 1.00 12736. ? 355 GLU B CA    1 
ATOM   6723  C  C     . GLU B 1 355 ? 139.461 109.549 131.798 1.00 12741. ? 355 GLU B C     1 
ATOM   6724  O  O     . GLU B 1 355 ? 139.429 109.564 130.559 1.00 12764. ? 355 GLU B O     1 
ATOM   6725  C  CB    . GLU B 1 355 ? 140.604 107.886 133.265 1.00 12747. ? 355 GLU B CB    1 
ATOM   6726  C  CG    . GLU B 1 355 ? 141.906 107.207 133.616 1.00 12758. ? 355 GLU B CG    1 
ATOM   6727  C  CD    . GLU B 1 355 ? 141.694 105.840 134.232 1.00 12749. ? 355 GLU B CD    1 
ATOM   6728  O  OE1   . GLU B 1 355 ? 140.534 105.381 134.277 1.00 12747. ? 355 GLU B OE1   1 
ATOM   6729  O  OE2   . GLU B 1 355 ? 142.686 105.223 134.674 1.00 12742. ? 355 GLU B OE2   1 
ATOM   6730  N  N     . LYS B 1 356 ? 138.396 109.841 132.549 1.00 12742. ? 356 LYS B N     1 
ATOM   6731  C  CA    . LYS B 1 356 ? 137.101 110.107 131.935 1.00 12739. ? 356 LYS B CA    1 
ATOM   6732  C  C     . LYS B 1 356 ? 137.182 111.276 130.966 1.00 12734. ? 356 LYS B C     1 
ATOM   6733  O  O     . LYS B 1 356 ? 136.744 111.173 129.816 1.00 12748. ? 356 LYS B O     1 
ATOM   6734  C  CB    . LYS B 1 356 ? 136.055 110.379 133.015 1.00 12708. ? 356 LYS B CB    1 
ATOM   6735  C  CG    . LYS B 1 356 ? 134.671 109.860 132.677 1.00 12630. ? 356 LYS B CG    1 
ATOM   6736  C  CD    . LYS B 1 356 ? 134.540 108.385 133.005 1.00 12676. ? 356 LYS B CD    1 
ATOM   6737  C  CE    . LYS B 1 356 ? 133.092 107.935 132.940 1.00 12647. ? 356 LYS B CE    1 
ATOM   6738  N  NZ    . LYS B 1 356 ? 132.641 107.739 131.536 1.00 12651. ? 356 LYS B NZ    1 
ATOM   6739  N  N     . MET B 1 357 ? 137.777 112.388 131.399 1.00 12729. ? 357 MET B N     1 
ATOM   6740  C  CA    . MET B 1 357 ? 137.733 113.594 130.583 1.00 12727. ? 357 MET B CA    1 
ATOM   6741  C  C     . MET B 1 357 ? 138.648 113.492 129.370 1.00 12733. ? 357 MET B C     1 
ATOM   6742  O  O     . MET B 1 357 ? 138.279 113.937 128.281 1.00 12757. ? 357 MET B O     1 
ATOM   6743  C  CB    . MET B 1 357 ? 138.073 114.818 131.428 1.00 12736. ? 357 MET B CB    1 
ATOM   6744  C  CG    . MET B 1 357 ? 138.941 115.845 130.739 1.00 12724. ? 357 MET B CG    1 
ATOM   6745  S  SD    . MET B 1 357 ? 139.144 117.293 131.783 1.00 12675. ? 357 MET B SD    1 
ATOM   6746  C  CE    . MET B 1 357 ? 140.441 116.717 132.863 1.00 12592. ? 357 MET B CE    1 
ATOM   6747  N  N     . VAL B 1 358 ? 139.834 112.898 129.520 1.00 12739. ? 358 VAL B N     1 
ATOM   6748  C  CA    . VAL B 1 358 ? 140.734 112.762 128.379 1.00 12733. ? 358 VAL B CA    1 
ATOM   6749  C  C     . VAL B 1 358 ? 140.143 111.816 127.341 1.00 12730. ? 358 VAL B C     1 
ATOM   6750  O  O     . VAL B 1 358 ? 140.131 112.117 126.139 1.00 12750. ? 358 VAL B O     1 
ATOM   6751  C  CB    . VAL B 1 358 ? 142.125 112.299 128.844 1.00 12739. ? 358 VAL B CB    1 
ATOM   6752  C  CG1   . VAL B 1 358 ? 142.956 111.848 127.659 1.00 12748. ? 358 VAL B CG1   1 
ATOM   6753  C  CG2   . VAL B 1 358 ? 142.827 113.419 129.586 1.00 12723. ? 358 VAL B CG2   1 
ATOM   6754  N  N     . SER B 1 359 ? 139.633 110.661 127.783 1.00 12728. ? 359 SER B N     1 
ATOM   6755  C  CA    . SER B 1 359 ? 139.020 109.737 126.837 1.00 12733. ? 359 SER B CA    1 
ATOM   6756  C  C     . SER B 1 359 ? 137.803 110.362 126.168 1.00 12743. ? 359 SER B C     1 
ATOM   6757  O  O     . SER B 1 359 ? 137.605 110.209 124.956 1.00 12758. ? 359 SER B O     1 
ATOM   6758  C  CB    . SER B 1 359 ? 138.640 108.438 127.544 1.00 12749. ? 359 SER B CB    1 
ATOM   6759  O  OG    . SER B 1 359 ? 137.987 108.701 128.772 1.00 12755. ? 359 SER B OG    1 
ATOM   6760  N  N     . GLY B 1 360 ? 136.981 111.082 126.936 1.00 12747. ? 360 GLY B N     1 
ATOM   6761  C  CA    . GLY B 1 360 ? 135.814 111.718 126.355 1.00 12749. ? 360 GLY B CA    1 
ATOM   6762  C  C     . GLY B 1 360 ? 136.170 112.794 125.352 1.00 12740. ? 360 GLY B C     1 
ATOM   6763  O  O     . GLY B 1 360 ? 135.528 112.913 124.309 1.00 12758. ? 360 GLY B O     1 
ATOM   6764  N  N     . MET B 1 361 ? 137.192 113.597 125.653 1.00 12730. ? 361 MET B N     1 
ATOM   6765  C  CA    . MET B 1 361 ? 137.629 114.623 124.715 1.00 12731. ? 361 MET B CA    1 
ATOM   6766  C  C     . MET B 1 361 ? 138.138 114.002 123.425 1.00 12740. ? 361 MET B C     1 
ATOM   6767  O  O     . MET B 1 361 ? 137.803 114.466 122.327 1.00 12747. ? 361 MET B O     1 
ATOM   6768  C  CB    . MET B 1 361 ? 138.714 115.484 125.356 1.00 12736. ? 361 MET B CB    1 
ATOM   6769  C  CG    . MET B 1 361 ? 139.709 116.063 124.373 1.00 12723. ? 361 MET B CG    1 
ATOM   6770  S  SD    . MET B 1 361 ? 141.211 116.630 125.184 1.00 12684. ? 361 MET B SD    1 
ATOM   6771  C  CE    . MET B 1 361 ? 140.521 117.685 126.448 1.00 12694. ? 361 MET B CE    1 
ATOM   6772  N  N     . VAL B 1 362 ? 138.944 112.944 123.536 1.00 12733. ? 362 VAL B N     1 
ATOM   6773  C  CA    . VAL B 1 362 ? 139.462 112.290 122.339 1.00 12690. ? 362 VAL B CA    1 
ATOM   6774  C  C     . VAL B 1 362 ? 138.320 111.721 121.509 1.00 12728. ? 362 VAL B C     1 
ATOM   6775  O  O     . VAL B 1 362 ? 138.281 111.888 120.285 1.00 12753. ? 362 VAL B O     1 
ATOM   6776  C  CB    . VAL B 1 362 ? 140.485 111.207 122.723 1.00 12716. ? 362 VAL B CB    1 
ATOM   6777  C  CG1   . VAL B 1 362 ? 140.758 110.293 121.546 1.00 12718. ? 362 VAL B CG1   1 
ATOM   6778  C  CG2   . VAL B 1 362 ? 141.766 111.851 123.208 1.00 12701. ? 362 VAL B CG2   1 
ATOM   6779  N  N     . LYS B 1 363 ? 137.361 111.059 122.159 1.00 12734. ? 363 LYS B N     1 
ATOM   6780  C  CA    . LYS B 1 363 ? 136.240 110.477 121.427 1.00 12739. ? 363 LYS B CA    1 
ATOM   6781  C  C     . LYS B 1 363 ? 135.363 111.553 120.798 1.00 12737. ? 363 LYS B C     1 
ATOM   6782  O  O     . LYS B 1 363 ? 134.855 111.376 119.686 1.00 12750. ? 363 LYS B O     1 
ATOM   6783  C  CB    . LYS B 1 363 ? 135.418 109.589 122.358 1.00 12743. ? 363 LYS B CB    1 
ATOM   6784  C  CG    . LYS B 1 363 ? 134.091 109.140 121.785 1.00 12743. ? 363 LYS B CG    1 
ATOM   6785  C  CD    . LYS B 1 363 ? 134.279 107.998 120.809 1.00 12754. ? 363 LYS B CD    1 
ATOM   6786  C  CE    . LYS B 1 363 ? 133.750 106.696 121.380 1.00 12760. ? 363 LYS B CE    1 
ATOM   6787  N  NZ    . LYS B 1 363 ? 133.813 105.592 120.385 1.00 12765. ? 363 LYS B NZ    1 
ATOM   6788  N  N     . HIS B 1 364 ? 135.175 112.675 121.491 1.00 12732. ? 364 HIS B N     1 
ATOM   6789  C  CA    . HIS B 1 364 ? 134.290 113.726 121.010 1.00 12734. ? 364 HIS B CA    1 
ATOM   6790  C  C     . HIS B 1 364 ? 134.906 114.522 119.869 1.00 12738. ? 364 HIS B C     1 
ATOM   6791  O  O     . HIS B 1 364 ? 134.178 115.006 118.997 1.00 12758. ? 364 HIS B O     1 
ATOM   6792  C  CB    . HIS B 1 364 ? 133.920 114.652 122.170 1.00 12737. ? 364 HIS B CB    1 
ATOM   6793  C  CG    . HIS B 1 364 ? 133.370 115.977 121.743 1.00 12698. ? 364 HIS B CG    1 
ATOM   6794  N  ND1   . HIS B 1 364 ? 134.161 117.093 121.582 1.00 12719. ? 364 HIS B ND1   1 
ATOM   6795  C  CD2   . HIS B 1 364 ? 132.106 116.367 121.459 1.00 12687. ? 364 HIS B CD2   1 
ATOM   6796  C  CE1   . HIS B 1 364 ? 133.410 118.113 121.209 1.00 12684. ? 364 HIS B CE1   1 
ATOM   6797  N  NE2   . HIS B 1 364 ? 132.158 117.699 121.127 1.00 12668. ? 364 HIS B NE2   1 
ATOM   6798  N  N     . ILE B 1 365 ? 136.226 114.666 119.848 1.00 12739. ? 365 ILE B N     1 
ATOM   6799  C  CA    . ILE B 1 365 ? 136.873 115.449 118.799 1.00 12736. ? 365 ILE B CA    1 
ATOM   6800  C  C     . ILE B 1 365 ? 137.297 114.574 117.629 1.00 12744. ? 365 ILE B C     1 
ATOM   6801  O  O     . ILE B 1 365 ? 136.958 114.853 116.476 1.00 12747. ? 365 ILE B O     1 
ATOM   6802  C  CB    . ILE B 1 365 ? 138.064 116.227 119.391 1.00 12713. ? 365 ILE B CB    1 
ATOM   6803  C  CG1   . ILE B 1 365 ? 137.552 117.430 120.178 1.00 12720. ? 365 ILE B CG1   1 
ATOM   6804  C  CG2   . ILE B 1 365 ? 139.006 116.677 118.293 1.00 12722. ? 365 ILE B CG2   1 
ATOM   6805  C  CD1   . ILE B 1 365 ? 138.522 117.950 121.187 1.00 12731. ? 365 ILE B CD1   1 
ATOM   6806  N  N     . THR B 1 366 ? 138.042 113.500 117.896 1.00 12750. ? 366 THR B N     1 
ATOM   6807  C  CA    . THR B 1 366 ? 138.515 112.643 116.815 1.00 12736. ? 366 THR B CA    1 
ATOM   6808  C  C     . THR B 1 366 ? 137.396 111.778 116.250 1.00 12734. ? 366 THR B C     1 
ATOM   6809  O  O     . THR B 1 366 ? 137.450 111.382 115.081 1.00 12742. ? 366 THR B O     1 
ATOM   6810  C  CB    . THR B 1 366 ? 139.664 111.768 117.313 1.00 12737. ? 366 THR B CB    1 
ATOM   6811  O  OG1   . THR B 1 366 ? 140.595 112.575 118.043 1.00 12702. ? 366 THR B OG1   1 
ATOM   6812  C  CG2   . THR B 1 366 ? 140.387 111.112 116.149 1.00 12748. ? 366 THR B CG2   1 
ATOM   6813  N  N     . GLY B 1 367 ? 136.374 111.486 117.049 1.00 12730. ? 367 GLY B N     1 
ATOM   6814  C  CA    . GLY B 1 367 ? 135.327 110.574 116.651 1.00 12731. ? 367 GLY B CA    1 
ATOM   6815  C  C     . GLY B 1 367 ? 135.570 109.131 117.031 1.00 12734. ? 367 GLY B C     1 
ATOM   6816  O  O     . GLY B 1 367 ? 134.674 108.299 116.846 1.00 12731. ? 367 GLY B O     1 
ATOM   6817  N  N     . SER B 1 368 ? 136.748 108.809 117.557 1.00 12851. ? 368 SER B N     1 
ATOM   6818  C  CA    . SER B 1 368 ? 137.073 107.457 117.981 1.00 12857. ? 368 SER B CA    1 
ATOM   6819  C  C     . SER B 1 368 ? 138.042 107.542 119.152 1.00 12854. ? 368 SER B C     1 
ATOM   6820  O  O     . SER B 1 368 ? 138.473 108.627 119.550 1.00 12856. ? 368 SER B O     1 
ATOM   6821  C  CB    . SER B 1 368 ? 137.660 106.641 116.827 1.00 12864. ? 368 SER B CB    1 
ATOM   6822  O  OG    . SER B 1 368 ? 137.796 105.278 117.183 1.00 12871. ? 368 SER B OG    1 
ATOM   6823  N  N     . TYR B 1 369 ? 138.381 106.382 119.709 1.00 12753. ? 369 TYR B N     1 
ATOM   6824  C  CA    . TYR B 1 369 ? 139.335 106.321 120.806 1.00 12752. ? 369 TYR B CA    1 
ATOM   6825  C  C     . TYR B 1 369 ? 140.770 106.145 120.337 1.00 12750. ? 369 TYR B C     1 
ATOM   6826  O  O     . TYR B 1 369 ? 141.694 106.511 121.070 1.00 12766. ? 369 TYR B O     1 
ATOM   6827  C  CB    . TYR B 1 369 ? 138.976 105.179 121.758 1.00 12762. ? 369 TYR B CB    1 
ATOM   6828  C  CG    . TYR B 1 369 ? 137.939 105.551 122.789 1.00 12741. ? 369 TYR B CG    1 
ATOM   6829  C  CD1   . TYR B 1 369 ? 137.952 106.798 123.392 1.00 12743. ? 369 TYR B CD1   1 
ATOM   6830  C  CD2   . TYR B 1 369 ? 136.949 104.656 123.158 1.00 12731. ? 369 TYR B CD2   1 
ATOM   6831  C  CE1   . TYR B 1 369 ? 137.008 107.143 124.333 1.00 12740. ? 369 TYR B CE1   1 
ATOM   6832  C  CE2   . TYR B 1 369 ? 136.001 104.992 124.099 1.00 12737. ? 369 TYR B CE2   1 
ATOM   6833  C  CZ    . TYR B 1 369 ? 136.035 106.237 124.683 1.00 12743. ? 369 TYR B CZ    1 
ATOM   6834  O  OH    . TYR B 1 369 ? 135.091 106.578 125.623 1.00 12761. ? 369 TYR B OH    1 
ATOM   6835  N  N     . LYS B 1 370 ? 140.978 105.605 119.141 1.00 12738. ? 370 LYS B N     1 
ATOM   6836  C  CA    . LYS B 1 370 ? 142.311 105.359 118.611 1.00 12736. ? 370 LYS B CA    1 
ATOM   6837  C  C     . LYS B 1 370 ? 142.717 106.499 117.689 1.00 12741. ? 370 LYS B C     1 
ATOM   6838  O  O     . LYS B 1 370 ? 141.963 106.872 116.786 1.00 12752. ? 370 LYS B O     1 
ATOM   6839  C  CB    . LYS B 1 370 ? 142.358 104.031 117.857 1.00 12740. ? 370 LYS B CB    1 
ATOM   6840  C  CG    . LYS B 1 370 ? 142.171 102.814 118.740 1.00 12745. ? 370 LYS B CG    1 
ATOM   6841  C  CD    . LYS B 1 370 ? 142.205 101.536 117.922 1.00 12752. ? 370 LYS B CD    1 
ATOM   6842  C  CE    . LYS B 1 370 ? 142.043 100.314 118.805 1.00 12750. ? 370 LYS B CE    1 
ATOM   6843  N  NZ    . LYS B 1 370 ? 142.050 99.056  118.010 1.00 12759. ? 370 LYS B NZ    1 
ATOM   6844  N  N     . VAL B 1 371 ? 143.908 107.046 117.920 1.00 12740. ? 371 VAL B N     1 
ATOM   6845  C  CA    . VAL B 1 371 ? 144.460 108.101 117.083 1.00 12743. ? 371 VAL B CA    1 
ATOM   6846  C  C     . VAL B 1 371 ? 145.800 107.630 116.538 1.00 12775. ? 371 VAL B C     1 
ATOM   6847  O  O     . VAL B 1 371 ? 146.414 106.692 117.050 1.00 12819. ? 371 VAL B O     1 
ATOM   6848  C  CB    . VAL B 1 371 ? 144.618 109.435 117.841 1.00 12731. ? 371 VAL B CB    1 
ATOM   6849  C  CG1   . VAL B 1 371 ? 143.431 109.674 118.755 1.00 12726. ? 371 VAL B CG1   1 
ATOM   6850  C  CG2   . VAL B 1 371 ? 145.911 109.450 118.631 1.00 12738. ? 371 VAL B CG2   1 
ATOM   6851  N  N     . THR B 1 372 ? 146.243 108.282 115.468 1.00 13263. ? 372 THR B N     1 
ATOM   6852  C  CA    . THR B 1 372 ? 147.527 107.990 114.848 1.00 13284. ? 372 THR B CA    1 
ATOM   6853  C  C     . THR B 1 372 ? 148.407 109.226 114.936 1.00 13227. ? 372 THR B C     1 
ATOM   6854  O  O     . THR B 1 372 ? 147.998 110.313 114.516 1.00 13198. ? 372 THR B O     1 
ATOM   6855  C  CB    . THR B 1 372 ? 147.358 107.562 113.390 1.00 13296. ? 372 THR B CB    1 
ATOM   6856  O  OG1   . THR B 1 372 ? 146.592 106.353 113.333 1.00 13312. ? 372 THR B OG1   1 
ATOM   6857  C  CG2   . THR B 1 372 ? 148.713 107.326 112.748 1.00 13326. ? 372 THR B CG2   1 
ATOM   6858  N  N     . TYR B 1 373 ? 149.608 109.058 115.477 1.00 12741. ? 373 TYR B N     1 
ATOM   6859  C  CA    . TYR B 1 373 ? 150.537 110.158 115.676 1.00 12713. ? 373 TYR B CA    1 
ATOM   6860  C  C     . TYR B 1 373 ? 151.833 109.884 114.931 1.00 12771. ? 373 TYR B C     1 
ATOM   6861  O  O     . TYR B 1 373 ? 152.326 108.752 114.918 1.00 12871. ? 373 TYR B O     1 
ATOM   6862  C  CB    . TYR B 1 373 ? 150.829 110.373 117.159 1.00 12746. ? 373 TYR B CB    1 
ATOM   6863  C  CG    . TYR B 1 373 ? 151.602 111.637 117.444 1.00 12709. ? 373 TYR B CG    1 
ATOM   6864  C  CD1   . TYR B 1 373 ? 151.000 112.879 117.330 1.00 12450. ? 373 TYR B CD1   1 
ATOM   6865  C  CD2   . TYR B 1 373 ? 152.934 111.588 117.820 1.00 12743. ? 373 TYR B CD2   1 
ATOM   6866  C  CE1   . TYR B 1 373 ? 151.702 114.036 117.588 1.00 12366. ? 373 TYR B CE1   1 
ATOM   6867  C  CE2   . TYR B 1 373 ? 153.644 112.739 118.079 1.00 12718. ? 373 TYR B CE2   1 
ATOM   6868  C  CZ    . TYR B 1 373 ? 153.022 113.960 117.960 1.00 12526. ? 373 TYR B CZ    1 
ATOM   6869  O  OH    . TYR B 1 373 ? 153.725 115.112 118.216 1.00 12461. ? 373 TYR B OH    1 
ATOM   6870  N  N     . HIS B 1 374 ? 152.378 110.925 114.311 1.00 13577. ? 374 HIS B N     1 
ATOM   6871  C  CA    . HIS B 1 374 ? 153.655 110.844 113.603 1.00 13661. ? 374 HIS B CA    1 
ATOM   6872  C  C     . HIS B 1 374 ? 154.662 111.724 114.324 1.00 13669. ? 374 HIS B C     1 
ATOM   6873  O  O     . HIS B 1 374 ? 154.688 112.949 114.109 1.00 13586. ? 374 HIS B O     1 
ATOM   6874  C  CB    . HIS B 1 374 ? 153.502 111.280 112.148 1.00 13658. ? 374 HIS B CB    1 
ATOM   6875  C  CG    . HIS B 1 374 ? 152.692 110.336 111.317 1.00 13659. ? 374 HIS B CG    1 
ATOM   6876  N  ND1   . HIS B 1 374 ? 151.315 110.372 111.280 1.00 13598. ? 374 HIS B ND1   1 
ATOM   6877  C  CD2   . HIS B 1 374 ? 153.064 109.330 110.492 1.00 13752. ? 374 HIS B CD2   1 
ATOM   6878  C  CE1   . HIS B 1 374 ? 150.874 109.429 110.467 1.00 13630. ? 374 HIS B CE1   1 
ATOM   6879  N  NE2   . HIS B 1 374 ? 151.915 108.782 109.976 1.00 13723. ? 374 HIS B NE2   1 
ATOM   6880  N  N     . PRO B 1 375 ? 155.504 111.158 115.192 1.00 14144. ? 375 PRO B N     1 
ATOM   6881  C  CA    . PRO B 1 375 ? 156.430 111.995 115.970 1.00 14118. ? 375 PRO B CA    1 
ATOM   6882  C  C     . PRO B 1 375 ? 157.491 112.687 115.133 1.00 14149. ? 375 PRO B C     1 
ATOM   6883  O  O     . PRO B 1 375 ? 158.083 113.663 115.609 1.00 14080. ? 375 PRO B O     1 
ATOM   6884  C  CB    . PRO B 1 375 ? 157.060 111.001 116.954 1.00 14171. ? 375 PRO B CB    1 
ATOM   6885  C  CG    . PRO B 1 375 ? 156.907 109.673 116.302 1.00 14190. ? 375 PRO B CG    1 
ATOM   6886  C  CD    . PRO B 1 375 ? 155.631 109.729 115.521 1.00 14161. ? 375 PRO B CD    1 
ATOM   6887  N  N     . ASP B 1 376 ? 157.755 112.225 113.915 1.00 16092. ? 376 ASP B N     1 
ATOM   6888  C  CA    . ASP B 1 376 ? 158.809 112.784 113.073 1.00 16157. ? 376 ASP B CA    1 
ATOM   6889  C  C     . ASP B 1 376 ? 158.294 113.028 111.662 1.00 16187. ? 376 ASP B C     1 
ATOM   6890  O  O     . ASP B 1 376 ? 158.941 112.696 110.667 1.00 16255. ? 376 ASP B O     1 
ATOM   6891  C  CB    . ASP B 1 376 ? 160.029 111.868 113.057 1.00 16222. ? 376 ASP B CB    1 
ATOM   6892  C  CG    . ASP B 1 376 ? 159.690 110.457 112.628 1.00 16249. ? 376 ASP B CG    1 
ATOM   6893  O  OD1   . ASP B 1 376 ? 158.594 109.975 112.982 1.00 16241. ? 376 ASP B OD1   1 
ATOM   6894  O  OD2   . ASP B 1 376 ? 160.520 109.829 111.938 1.00 16266. ? 376 ASP B OD2   1 
ATOM   6895  N  N     . GLY B 1 377 ? 157.109 113.622 111.559 1.00 15880. ? 377 GLY B N     1 
ATOM   6896  C  CA    . GLY B 1 377 ? 156.547 113.975 110.279 1.00 15951. ? 377 GLY B CA    1 
ATOM   6897  C  C     . GLY B 1 377 ? 155.803 112.827 109.632 1.00 16019. ? 377 GLY B C     1 
ATOM   6898  O  O     . GLY B 1 377 ? 155.905 111.671 110.053 1.00 16003. ? 377 GLY B O     1 
ATOM   6899  N  N     . PRO B 1 378 ? 155.038 113.129 108.580 1.00 17043. ? 378 PRO B N     1 
ATOM   6900  C  CA    . PRO B 1 378 ? 154.245 112.079 107.922 1.00 17047. ? 378 PRO B CA    1 
ATOM   6901  C  C     . PRO B 1 378 ? 155.085 110.998 107.268 1.00 17080. ? 378 PRO B C     1 
ATOM   6902  O  O     . PRO B 1 378 ? 154.565 109.906 107.007 1.00 17079. ? 378 PRO B O     1 
ATOM   6903  C  CB    . PRO B 1 378 ? 153.428 112.857 106.883 1.00 17081. ? 378 PRO B CB    1 
ATOM   6904  C  CG    . PRO B 1 378 ? 154.231 114.085 106.620 1.00 17082. ? 378 PRO B CG    1 
ATOM   6905  C  CD    . PRO B 1 378 ? 154.885 114.437 107.922 1.00 17074. ? 378 PRO B CD    1 
ATOM   6906  N  N     . GLU B 1 379 ? 156.359 111.263 106.990 1.00 17764. ? 379 GLU B N     1 
ATOM   6907  C  CA    . GLU B 1 379 ? 157.223 110.265 106.375 1.00 17783. ? 379 GLU B CA    1 
ATOM   6908  C  C     . GLU B 1 379 ? 157.846 109.313 107.386 1.00 17775. ? 379 GLU B C     1 
ATOM   6909  O  O     . GLU B 1 379 ? 158.486 108.338 106.979 1.00 17795. ? 379 GLU B O     1 
ATOM   6910  C  CB    . GLU B 1 379 ? 158.329 110.954 105.572 1.00 17800. ? 379 GLU B CB    1 
ATOM   6911  C  CG    . GLU B 1 379 ? 159.407 111.596 106.428 1.00 17803. ? 379 GLU B CG    1 
ATOM   6912  C  CD    . GLU B 1 379 ? 158.969 112.918 107.028 1.00 17789. ? 379 GLU B CD    1 
ATOM   6913  O  OE1   . GLU B 1 379 ? 157.922 113.449 106.602 1.00 17789. ? 379 GLU B OE1   1 
ATOM   6914  O  OE2   . GLU B 1 379 ? 159.670 113.425 107.928 1.00 17791. ? 379 GLU B OE2   1 
ATOM   6915  N  N     . GLY B 1 380 ? 157.677 109.567 108.682 1.00 16948. ? 380 GLY B N     1 
ATOM   6916  C  CA    . GLY B 1 380 ? 158.244 108.727 109.714 1.00 16936. ? 380 GLY B CA    1 
ATOM   6917  C  C     . GLY B 1 380 ? 157.304 107.615 110.139 1.00 16925. ? 380 GLY B C     1 
ATOM   6918  O  O     . GLY B 1 380 ? 156.304 107.313 109.485 1.00 16923. ? 380 GLY B O     1 
ATOM   6919  N  N     . GLN B 1 381 ? 157.646 106.995 111.264 1.00 16751. ? 381 GLN B N     1 
ATOM   6920  C  CA    . GLN B 1 381 ? 156.838 105.912 111.802 1.00 16737. ? 381 GLN B CA    1 
ATOM   6921  C  C     . GLN B 1 381 ? 155.528 106.450 112.365 1.00 16692. ? 381 GLN B C     1 
ATOM   6922  O  O     . GLN B 1 381 ? 155.460 107.564 112.891 1.00 16664. ? 381 GLN B O     1 
ATOM   6923  C  CB    . GLN B 1 381 ? 157.591 105.145 112.896 1.00 16736. ? 381 GLN B CB    1 
ATOM   6924  C  CG    . GLN B 1 381 ? 158.286 105.967 114.006 1.00 16725. ? 381 GLN B CG    1 
ATOM   6925  C  CD    . GLN B 1 381 ? 159.421 106.875 113.537 1.00 16747. ? 381 GLN B CD    1 
ATOM   6926  O  OE1   . GLN B 1 381 ? 159.579 107.146 112.347 1.00 16754. ? 381 GLN B OE1   1 
ATOM   6927  N  NE2   . GLN B 1 381 ? 160.215 107.352 114.488 1.00 16749. ? 381 GLN B NE2   1 
ATOM   6928  N  N     . ALA B 1 382 ? 154.481 105.640 112.253 1.00 15662. ? 382 ALA B N     1 
ATOM   6929  C  CA    . ALA B 1 382 ? 153.156 105.986 112.747 1.00 15611. ? 382 ALA B CA    1 
ATOM   6930  C  C     . ALA B 1 382 ? 152.861 105.178 114.002 1.00 15601. ? 382 ALA B C     1 
ATOM   6931  O  O     . ALA B 1 382 ? 153.039 103.956 114.014 1.00 15619. ? 382 ALA B O     1 
ATOM   6932  C  CB    . ALA B 1 382 ? 152.088 105.726 111.684 1.00 15618. ? 382 ALA B CB    1 
ATOM   6933  N  N     . TYR B 1 383 ? 152.412 105.860 115.049 1.00 14710. ? 383 TYR B N     1 
ATOM   6934  C  CA    . TYR B 1 383 ? 152.112 105.238 116.330 1.00 14695. ? 383 TYR B CA    1 
ATOM   6935  C  C     . TYR B 1 383 ? 150.614 105.293 116.585 1.00 14665. ? 383 TYR B C     1 
ATOM   6936  O  O     . TYR B 1 383 ? 150.004 106.363 116.496 1.00 14638. ? 383 TYR B O     1 
ATOM   6937  C  CB    . TYR B 1 383 ? 152.870 105.930 117.463 1.00 14673. ? 383 TYR B CB    1 
ATOM   6938  C  CG    . TYR B 1 383 ? 154.326 105.543 117.542 1.00 14675. ? 383 TYR B CG    1 
ATOM   6939  C  CD1   . TYR B 1 383 ? 154.715 104.215 117.458 1.00 14693. ? 383 TYR B CD1   1 
ATOM   6940  C  CD2   . TYR B 1 383 ? 155.311 106.503 117.707 1.00 14676. ? 383 TYR B CD2   1 
ATOM   6941  C  CE1   . TYR B 1 383 ? 156.044 103.856 117.533 1.00 14699. ? 383 TYR B CE1   1 
ATOM   6942  C  CE2   . TYR B 1 383 ? 156.641 106.155 117.783 1.00 14679. ? 383 TYR B CE2   1 
ATOM   6943  C  CZ    . TYR B 1 383 ? 157.004 104.831 117.695 1.00 14691. ? 383 TYR B CZ    1 
ATOM   6944  O  OH    . TYR B 1 383 ? 158.331 104.481 117.771 1.00 14700. ? 383 TYR B OH    1 
ATOM   6945  N  N     . ASP B 1 384 ? 150.029 104.139 116.897 1.00 14539. ? 384 ASP B N     1 
ATOM   6946  C  CA    . ASP B 1 384 ? 148.604 104.035 117.191 1.00 14512. ? 384 ASP B CA    1 
ATOM   6947  C  C     . ASP B 1 384 ? 148.406 104.164 118.696 1.00 14477. ? 384 ASP B C     1 
ATOM   6948  O  O     . ASP B 1 384 ? 148.761 103.258 119.456 1.00 14493. ? 384 ASP B O     1 
ATOM   6949  C  CB    . ASP B 1 384 ? 148.045 102.713 116.676 1.00 14541. ? 384 ASP B CB    1 
ATOM   6950  C  CG    . ASP B 1 384 ? 147.733 102.750 115.195 1.00 14548. ? 384 ASP B CG    1 
ATOM   6951  O  OD1   . ASP B 1 384 ? 147.811 103.843 114.597 1.00 14540. ? 384 ASP B OD1   1 
ATOM   6952  O  OD2   . ASP B 1 384 ? 147.411 101.685 114.628 1.00 14555. ? 384 ASP B OD2   1 
ATOM   6953  N  N     . VAL B 1 385 ? 147.838 105.285 119.126 1.00 12813. ? 385 VAL B N     1 
ATOM   6954  C  CA    . VAL B 1 385 ? 147.595 105.556 120.536 1.00 12765. ? 385 VAL B CA    1 
ATOM   6955  C  C     . VAL B 1 385 ? 146.136 105.248 120.834 1.00 12761. ? 385 VAL B C     1 
ATOM   6956  O  O     . VAL B 1 385 ? 145.233 105.793 120.187 1.00 12785. ? 385 VAL B O     1 
ATOM   6957  C  CB    . VAL B 1 385 ? 147.935 107.009 120.895 1.00 12755. ? 385 VAL B CB    1 
ATOM   6958  C  CG1   . VAL B 1 385 ? 148.094 107.154 122.393 1.00 12764. ? 385 VAL B CG1   1 
ATOM   6959  C  CG2   . VAL B 1 385 ? 149.196 107.451 120.174 1.00 12771. ? 385 VAL B CG2   1 
ATOM   6960  N  N     . ASP B 1 386 ? 145.894 104.370 121.810 1.00 12749. ? 386 ASP B N     1 
ATOM   6961  C  CA    . ASP B 1 386 ? 144.493 104.048 122.201 1.00 12744. ? 386 ASP B CA    1 
ATOM   6962  C  C     . ASP B 1 386 ? 144.124 104.859 123.448 1.00 12742. ? 386 ASP B C     1 
ATOM   6963  O  O     . ASP B 1 386 ? 144.926 104.868 124.404 1.00 12751. ? 386 ASP B O     1 
ATOM   6964  C  CB    . ASP B 1 386 ? 144.287 102.554 122.389 1.00 12749. ? 386 ASP B CB    1 
ATOM   6965  C  CG    . ASP B 1 386 ? 142.836 102.108 122.507 1.00 12753. ? 386 ASP B CG    1 
ATOM   6966  O  OD1   . ASP B 1 386 ? 141.944 102.979 122.426 1.00 12752. ? 386 ASP B OD1   1 
ATOM   6967  O  OD2   . ASP B 1 386 ? 142.610 100.892 122.679 1.00 12759. ? 386 ASP B OD2   1 
ATOM   6968  N  N     . PHE B 1 387 ? 142.953 105.503 123.437 1.00 12745. ? 387 PHE B N     1 
ATOM   6969  C  CA    . PHE B 1 387 ? 142.535 106.356 124.584 1.00 12732. ? 387 PHE B CA    1 
ATOM   6970  C  C     . PHE B 1 387 ? 141.344 105.715 125.291 1.00 12745. ? 387 PHE B C     1 
ATOM   6971  O  O     . PHE B 1 387 ? 140.437 106.452 125.734 1.00 12749. ? 387 PHE B O     1 
ATOM   6972  C  CB    . PHE B 1 387 ? 142.226 107.776 124.100 1.00 12726. ? 387 PHE B CB    1 
ATOM   6973  C  CG    . PHE B 1 387 ? 143.466 108.567 123.710 1.00 12728. ? 387 PHE B CG    1 
ATOM   6974  C  CD1   . PHE B 1 387 ? 143.953 108.536 122.408 1.00 12744. ? 387 PHE B CD1   1 
ATOM   6975  C  CD2   . PHE B 1 387 ? 144.148 109.331 124.650 1.00 12741. ? 387 PHE B CD2   1 
ATOM   6976  C  CE1   . PHE B 1 387 ? 145.083 109.256 122.059 1.00 12750. ? 387 PHE B CE1   1 
ATOM   6977  C  CE2   . PHE B 1 387 ? 145.278 110.048 124.294 1.00 12744. ? 387 PHE B CE2   1 
ATOM   6978  C  CZ    . PHE B 1 387 ? 145.743 110.010 123.001 1.00 12743. ? 387 PHE B CZ    1 
ATOM   6979  N  N     . THR B 1 388 ? 141.341 104.383 125.399 1.00 12754. ? 388 THR B N     1 
ATOM   6980  C  CA    . THR B 1 388 ? 140.265 103.702 126.150 1.00 12749. ? 388 THR B CA    1 
ATOM   6981  C  C     . THR B 1 388 ? 140.204 104.324 127.527 1.00 12756. ? 388 THR B C     1 
ATOM   6982  O  O     . THR B 1 388 ? 141.274 104.449 128.158 1.00 12773. ? 388 THR B O     1 
ATOM   6983  C  CB    . THR B 1 388 ? 140.560 102.205 126.206 1.00 12747. ? 388 THR B CB    1 
ATOM   6984  O  OG1   . THR B 1 388 ? 140.718 101.809 124.847 1.00 12743. ? 388 THR B OG1   1 
ATOM   6985  C  CG2   . THR B 1 388 ? 139.438 101.407 126.846 1.00 12750. ? 388 THR B CG2   1 
ATOM   6986  N  N     . PRO B 1 389 ? 139.018 104.714 128.045 1.00 12894. ? 389 PRO B N     1 
ATOM   6987  C  CA    . PRO B 1 389 ? 138.944 105.416 129.322 1.00 12906. ? 389 PRO B CA    1 
ATOM   6988  C  C     . PRO B 1 389 ? 139.939 104.944 130.392 1.00 12912. ? 389 PRO B C     1 
ATOM   6989  O  O     . PRO B 1 389 ? 140.692 105.805 130.885 1.00 12936. ? 389 PRO B O     1 
ATOM   6990  C  CB    . PRO B 1 389 ? 137.471 105.209 129.731 1.00 12916. ? 389 PRO B CB    1 
ATOM   6991  C  CG    . PRO B 1 389 ? 136.741 105.140 128.408 1.00 12916. ? 389 PRO B CG    1 
ATOM   6992  C  CD    . PRO B 1 389 ? 137.719 104.512 127.424 1.00 12912. ? 389 PRO B CD    1 
ATOM   6993  N  N     . PRO B 1 390 ? 140.016 103.647 130.775 1.00 12747. ? 390 PRO B N     1 
ATOM   6994  C  CA    . PRO B 1 390 ? 141.013 103.224 131.749 1.00 12735. ? 390 PRO B CA    1 
ATOM   6995  C  C     . PRO B 1 390 ? 142.421 103.396 131.193 1.00 12742. ? 390 PRO B C     1 
ATOM   6996  O  O     . PRO B 1 390 ? 142.727 102.844 130.117 1.00 12755. ? 390 PRO B O     1 
ATOM   6997  C  CB    . PRO B 1 390 ? 140.664 101.752 132.018 1.00 12736. ? 390 PRO B CB    1 
ATOM   6998  C  CG    . PRO B 1 390 ? 139.927 101.315 130.772 1.00 12749. ? 390 PRO B CG    1 
ATOM   6999  C  CD    . PRO B 1 390 ? 139.174 102.551 130.314 1.00 12743. ? 390 PRO B CD    1 
ATOM   7000  N  N     . PHE B 1 391 ? 143.265 104.144 131.911 1.00 12737. ? 391 PHE B N     1 
ATOM   7001  C  CA    . PHE B 1 391 ? 144.662 104.376 131.453 1.00 12729. ? 391 PHE B CA    1 
ATOM   7002  C  C     . PHE B 1 391 ? 145.611 103.522 132.293 1.00 12737. ? 391 PHE B C     1 
ATOM   7003  O  O     . PHE B 1 391 ? 145.347 103.328 133.501 1.00 12756. ? 391 PHE B O     1 
ATOM   7004  C  CB    . PHE B 1 391 ? 145.033 105.862 131.520 1.00 12743. ? 391 PHE B CB    1 
ATOM   7005  C  CG    . PHE B 1 391 ? 144.205 106.774 130.625 1.00 12746. ? 391 PHE B CG    1 
ATOM   7006  C  CD1   . PHE B 1 391 ? 143.625 106.294 129.456 1.00 12745. ? 391 PHE B CD1   1 
ATOM   7007  C  CD2   . PHE B 1 391 ? 144.021 108.113 130.947 1.00 12757. ? 391 PHE B CD2   1 
ATOM   7008  C  CE1   . PHE B 1 391 ? 142.873 107.128 128.643 1.00 12755. ? 391 PHE B CE1   1 
ATOM   7009  C  CE2   . PHE B 1 391 ? 143.269 108.942 130.129 1.00 12750. ? 391 PHE B CE2   1 
ATOM   7010  C  CZ    . PHE B 1 391 ? 142.696 108.448 128.981 1.00 12751. ? 391 PHE B CZ    1 
ATOM   7011  N  N     . ARG B 1 392 ? 146.687 103.025 131.675 1.00 12731. ? 392 ARG B N     1 
ATOM   7012  C  CA    . ARG B 1 392 ? 147.681 102.182 132.392 1.00 12733. ? 392 ARG B CA    1 
ATOM   7013  C  C     . ARG B 1 392 ? 148.245 102.957 133.595 1.00 12743. ? 392 ARG B C     1 
ATOM   7014  O  O     . ARG B 1 392 ? 148.306 104.202 133.525 1.00 12751. ? 392 ARG B O     1 
ATOM   7015  C  CB    . ARG B 1 392 ? 148.773 101.769 131.399 1.00 12738. ? 392 ARG B CB    1 
ATOM   7016  C  CG    . ARG B 1 392 ? 149.984 101.043 131.964 1.00 12743. ? 392 ARG B CG    1 
ATOM   7017  C  CD    . ARG B 1 392 ? 150.968 100.703 130.854 1.00 12743. ? 392 ARG B CD    1 
ATOM   7018  N  NE    . ARG B 1 392 ? 152.327 100.450 131.344 1.00 12747. ? 392 ARG B NE    1 
ATOM   7019  C  CZ    . ARG B 1 392 ? 153.400 101.134 130.964 1.00 12754. ? 392 ARG B CZ    1 
ATOM   7020  N  NH1   . ARG B 1 392 ? 153.291 102.082 130.050 1.00 12765. ? 392 ARG B NH1   1 
ATOM   7021  N  NH2   . ARG B 1 392 ? 154.579 100.865 131.495 1.00 12766. ? 392 ARG B NH2   1 
ATOM   7022  N  N     . ARG B 1 393 ? 148.635 102.244 134.657 1.00 12840. ? 393 ARG B N     1 
ATOM   7023  C  CA    . ARG B 1 393 ? 149.201 102.903 135.865 1.00 12847. ? 393 ARG B CA    1 
ATOM   7024  C  C     . ARG B 1 393 ? 150.506 102.195 136.260 1.00 12850. ? 393 ARG B C     1 
ATOM   7025  O  O     . ARG B 1 393 ? 150.508 100.945 136.297 1.00 12852. ? 393 ARG B O     1 
ATOM   7026  C  CB    . ARG B 1 393 ? 148.224 102.825 137.041 1.00 12845. ? 393 ARG B CB    1 
ATOM   7027  C  CG    . ARG B 1 393 ? 146.857 103.461 136.838 1.00 12851. ? 393 ARG B CG    1 
ATOM   7028  C  CD    . ARG B 1 393 ? 145.929 103.030 137.963 1.00 12851. ? 393 ARG B CD    1 
ATOM   7029  N  NE    . ARG B 1 393 ? 144.658 103.760 138.019 1.00 12839. ? 393 ARG B NE    1 
ATOM   7030  C  CZ    . ARG B 1 393 ? 143.712 103.755 137.088 1.00 12849. ? 393 ARG B CZ    1 
ATOM   7031  N  NH1   . ARG B 1 393 ? 143.814 102.965 136.033 1.00 12845. ? 393 ARG B NH1   1 
ATOM   7032  N  NH2   . ARG B 1 393 ? 142.658 104.539 137.221 1.00 12865. ? 393 ARG B NH2   1 
ATOM   7033  N  N     . ILE B 1 394 ? 151.562 102.960 136.555 1.00 12757. ? 394 ILE B N     1 
ATOM   7034  C  CA    . ILE B 1 394 ? 152.864 102.360 136.985 1.00 12762. ? 394 ILE B CA    1 
ATOM   7035  C  C     . ILE B 1 394 ? 153.441 103.177 138.153 1.00 12784. ? 394 ILE B C     1 
ATOM   7036  O  O     . ILE B 1 394 ? 152.991 104.327 138.350 1.00 12783. ? 394 ILE B O     1 
ATOM   7037  C  CB    . ILE B 1 394 ? 153.859 102.282 135.810 1.00 12771. ? 394 ILE B CB    1 
ATOM   7038  C  CG1   . ILE B 1 394 ? 154.145 103.660 135.215 1.00 12770. ? 394 ILE B CG1   1 
ATOM   7039  C  CG2   . ILE B 1 394 ? 153.381 101.295 134.744 1.00 12775. ? 394 ILE B CG2   1 
ATOM   7040  C  CD1   . ILE B 1 394 ? 155.118 103.638 134.051 1.00 12773. ? 394 ILE B CD1   1 
ATOM   7041  N  N     . ASN B 1 395 ? 154.392 102.600 138.895 1.00 13496. ? 395 ASN B N     1 
ATOM   7042  C  CA    . ASN B 1 395 ? 155.029 103.308 139.997 1.00 13514. ? 395 ASN B CA    1 
ATOM   7043  C  C     . ASN B 1 395 ? 156.457 103.668 139.614 1.00 13532. ? 395 ASN B C     1 
ATOM   7044  O  O     . ASN B 1 395 ? 157.158 102.869 138.987 1.00 13573. ? 395 ASN B O     1 
ATOM   7045  C  CB    . ASN B 1 395 ? 155.034 102.459 141.269 1.00 13545. ? 395 ASN B CB    1 
ATOM   7046  C  CG    . ASN B 1 395 ? 153.656 102.309 141.872 1.00 13532. ? 395 ASN B CG    1 
ATOM   7047  O  OD1   . ASN B 1 395 ? 153.367 102.859 142.932 1.00 13535. ? 395 ASN B OD1   1 
ATOM   7048  N  ND2   . ASN B 1 395 ? 152.798 101.551 141.202 1.00 13528. ? 395 ASN B ND2   1 
ATOM   7049  N  N     . MET B 1 396 ? 156.884 104.875 139.992 1.00 13042. ? 396 MET B N     1 
ATOM   7050  C  CA    . MET B 1 396 ? 158.222 105.333 139.628 1.00 13043. ? 396 MET B CA    1 
ATOM   7051  C  C     . MET B 1 396 ? 159.306 104.423 140.186 1.00 13106. ? 396 MET B C     1 
ATOM   7052  O  O     . MET B 1 396 ? 160.169 103.946 139.443 1.00 13129. ? 396 MET B O     1 
ATOM   7053  C  CB    . MET B 1 396 ? 158.440 106.767 140.106 1.00 13027. ? 396 MET B CB    1 
ATOM   7054  C  CG    . MET B 1 396 ? 159.666 107.428 139.493 1.00 13033. ? 396 MET B CG    1 
ATOM   7055  S  SD    . MET B 1 396 ? 159.507 109.197 139.226 1.00 13023. ? 396 MET B SD    1 
ATOM   7056  C  CE    . MET B 1 396 ? 157.739 109.328 139.108 1.00 13027. ? 396 MET B CE    1 
ATOM   7057  N  N     . VAL B 1 397 ? 159.281 104.166 141.493 1.00 14104. ? 397 VAL B N     1 
ATOM   7058  C  CA    . VAL B 1 397 ? 160.391 103.454 142.118 1.00 14130. ? 397 VAL B CA    1 
ATOM   7059  C  C     . VAL B 1 397 ? 160.433 102.004 141.652 1.00 14184. ? 397 VAL B C     1 
ATOM   7060  O  O     . VAL B 1 397 ? 161.489 101.493 141.264 1.00 14189. ? 397 VAL B O     1 
ATOM   7061  C  CB    . VAL B 1 397 ? 160.299 103.558 143.650 1.00 14147. ? 397 VAL B CB    1 
ATOM   7062  C  CG1   . VAL B 1 397 ? 161.419 102.766 144.297 1.00 14162. ? 397 VAL B CG1   1 
ATOM   7063  C  CG2   . VAL B 1 397 ? 160.357 105.013 144.078 1.00 14124. ? 397 VAL B CG2   1 
ATOM   7064  N  N     . GLU B 1 398 ? 159.284 101.326 141.663 1.00 15589. ? 398 GLU B N     1 
ATOM   7065  C  CA    . GLU B 1 398 ? 159.258 99.907  141.318 1.00 15635. ? 398 GLU B CA    1 
ATOM   7066  C  C     . GLU B 1 398 ? 159.613 99.682  139.853 1.00 15634. ? 398 GLU B C     1 
ATOM   7067  O  O     . GLU B 1 398 ? 160.436 98.817  139.527 1.00 15666. ? 398 GLU B O     1 
ATOM   7068  C  CB    . GLU B 1 398 ? 157.883 99.321  141.635 1.00 15669. ? 398 GLU B CB    1 
ATOM   7069  C  CG    . GLU B 1 398 ? 157.727 98.854  143.070 1.00 15681. ? 398 GLU B CG    1 
ATOM   7070  C  CD    . GLU B 1 398 ? 157.104 99.910  143.961 1.00 15672. ? 398 GLU B CD    1 
ATOM   7071  O  OE1   . GLU B 1 398 ? 156.983 101.069 143.514 1.00 15646. ? 398 GLU B OE1   1 
ATOM   7072  O  OE2   . GLU B 1 398 ? 156.734 99.582  145.107 1.00 15685. ? 398 GLU B OE2   1 
ATOM   7073  N  N     . GLU B 1 399 ? 159.005 100.453 138.952 1.00 15084. ? 399 GLU B N     1 
ATOM   7074  C  CA    . GLU B 1 399 ? 159.295 100.280 137.534 1.00 15085. ? 399 GLU B CA    1 
ATOM   7075  C  C     . GLU B 1 399 ? 160.702 100.744 137.186 1.00 15072. ? 399 GLU B C     1 
ATOM   7076  O  O     . GLU B 1 399 ? 161.335 100.170 136.296 1.00 15103. ? 399 GLU B O     1 
ATOM   7077  C  CB    . GLU B 1 399 ? 158.262 101.020 136.689 1.00 15071. ? 399 GLU B CB    1 
ATOM   7078  C  CG    . GLU B 1 399 ? 156.909 100.341 136.660 1.00 15070. ? 399 GLU B CG    1 
ATOM   7079  C  CD    . GLU B 1 399 ? 156.915 99.069  135.837 1.00 15105. ? 399 GLU B CD    1 
ATOM   7080  O  OE1   . GLU B 1 399 ? 157.667 99.007  134.843 1.00 15109. ? 399 GLU B OE1   1 
ATOM   7081  O  OE2   . GLU B 1 399 ? 156.170 98.130  136.188 1.00 15110. ? 399 GLU B OE2   1 
ATOM   7082  N  N     . LEU B 1 400 ? 161.205 101.777 137.863 1.00 14205. ? 400 LEU B N     1 
ATOM   7083  C  CA    . LEU B 1 400 ? 162.584 102.196 137.646 1.00 14188. ? 400 LEU B CA    1 
ATOM   7084  C  C     . LEU B 1 400 ? 163.557 101.116 138.096 1.00 14248. ? 400 LEU B C     1 
ATOM   7085  O  O     . LEU B 1 400 ? 164.568 100.865 137.431 1.00 14250. ? 400 LEU B O     1 
ATOM   7086  C  CB    . LEU B 1 400 ? 162.852 103.508 138.380 1.00 14167. ? 400 LEU B CB    1 
ATOM   7087  C  CG    . LEU B 1 400 ? 164.162 104.225 138.059 1.00 14162. ? 400 LEU B CG    1 
ATOM   7088  C  CD1   . LEU B 1 400 ? 164.355 104.330 136.561 1.00 14159. ? 400 LEU B CD1   1 
ATOM   7089  C  CD2   . LEU B 1 400 ? 164.179 105.601 138.699 1.00 14156. ? 400 LEU B CD2   1 
ATOM   7090  N  N     . GLU B 1 401 ? 163.270 100.468 139.227 1.00 15617. ? 401 GLU B N     1 
ATOM   7091  C  CA    . GLU B 1 401 ? 164.098 99.355  139.674 1.00 15659. ? 401 GLU B CA    1 
ATOM   7092  C  C     . GLU B 1 401 ? 164.052 98.205  138.680 1.00 15663. ? 401 GLU B C     1 
ATOM   7093  O  O     . GLU B 1 401 ? 165.084 97.594  138.376 1.00 15690. ? 401 GLU B O     1 
ATOM   7094  C  CB    . GLU B 1 401 ? 163.639 98.884  141.052 1.00 15678. ? 401 GLU B CB    1 
ATOM   7095  C  CG    . GLU B 1 401 ? 164.409 99.488  142.207 1.00 15691. ? 401 GLU B CG    1 
ATOM   7096  C  CD    . GLU B 1 401 ? 163.638 99.431  143.509 1.00 15693. ? 401 GLU B CD    1 
ATOM   7097  O  OE1   . GLU B 1 401 ? 162.400 99.277  143.461 1.00 15683. ? 401 GLU B OE1   1 
ATOM   7098  O  OE2   . GLU B 1 401 ? 164.269 99.540  144.581 1.00 15704. ? 401 GLU B OE2   1 
ATOM   7099  N  N     . LYS B 1 402 ? 162.861 97.889  138.168 1.00 15448. ? 402 LYS B N     1 
ATOM   7100  C  CA    . LYS B 1 402 ? 162.737 96.803  137.201 1.00 15453. ? 402 LYS B CA    1 
ATOM   7101  C  C     . LYS B 1 402 ? 163.497 97.114  135.917 1.00 15457. ? 402 LYS B C     1 
ATOM   7102  O  O     . LYS B 1 402 ? 164.181 96.244  135.365 1.00 15463. ? 402 LYS B O     1 
ATOM   7103  C  CB    . LYS B 1 402 ? 161.263 96.536  136.901 1.00 15455. ? 402 LYS B CB    1 
ATOM   7104  C  CG    . LYS B 1 402 ? 161.028 95.551  135.770 1.00 15459. ? 402 LYS B CG    1 
ATOM   7105  C  CD    . LYS B 1 402 ? 159.545 95.367  135.496 1.00 15462. ? 402 LYS B CD    1 
ATOM   7106  C  CE    . LYS B 1 402 ? 158.775 95.091  136.778 1.00 15465. ? 402 LYS B CE    1 
ATOM   7107  N  NZ    . LYS B 1 402 ? 159.306 93.903  137.500 1.00 15465. ? 402 LYS B NZ    1 
ATOM   7108  N  N     . ALA B 1 403 ? 163.388 98.349  135.425 1.00 15344. ? 403 ALA B N     1 
ATOM   7109  C  CA    . ALA B 1 403 ? 164.079 98.728  134.197 1.00 15343. ? 403 ALA B CA    1 
ATOM   7110  C  C     . ALA B 1 403 ? 165.589 98.735  134.394 1.00 15357. ? 403 ALA B C     1 
ATOM   7111  O  O     . ALA B 1 403 ? 166.340 98.268  133.530 1.00 15362. ? 403 ALA B O     1 
ATOM   7112  C  CB    . ALA B 1 403 ? 163.591 100.096 133.723 1.00 15334. ? 403 ALA B CB    1 
ATOM   7113  N  N     . LEU B 1 404 ? 166.054 99.264  135.524 1.00 15673. ? 404 LEU B N     1 
ATOM   7114  C  CA    . LEU B 1 404 ? 167.484 99.329  135.796 1.00 15681. ? 404 LEU B CA    1 
ATOM   7115  C  C     . LEU B 1 404 ? 168.086 97.973  136.135 1.00 15698. ? 404 LEU B C     1 
ATOM   7116  O  O     . LEU B 1 404 ? 169.315 97.859  136.173 1.00 15702. ? 404 LEU B O     1 
ATOM   7117  C  CB    . LEU B 1 404 ? 167.754 100.312 136.935 1.00 15688. ? 404 LEU B CB    1 
ATOM   7118  C  CG    . LEU B 1 404 ? 167.651 101.795 136.581 1.00 15670. ? 404 LEU B CG    1 
ATOM   7119  C  CD1   . LEU B 1 404 ? 167.517 102.635 137.839 1.00 15664. ? 404 LEU B CD1   1 
ATOM   7120  C  CD2   . LEU B 1 404 ? 168.852 102.238 135.768 1.00 15674. ? 404 LEU B CD2   1 
ATOM   7121  N  N     . GLY B 1 405 ? 167.264 96.954  136.376 1.00 16154. ? 405 GLY B N     1 
ATOM   7122  C  CA    . GLY B 1 405 ? 167.765 95.642  136.734 1.00 16172. ? 405 GLY B CA    1 
ATOM   7123  C  C     . GLY B 1 405 ? 168.527 95.644  138.042 1.00 16192. ? 405 GLY B C     1 
ATOM   7124  O  O     . GLY B 1 405 ? 169.586 95.020  138.154 1.00 16198. ? 405 GLY B O     1 
ATOM   7125  N  N     . MET B 1 406 ? 167.989 96.342  139.041 1.00 16786. ? 406 MET B N     1 
ATOM   7126  C  CA    . MET B 1 406 ? 168.664 96.501  140.323 1.00 16807. ? 406 MET B CA    1 
ATOM   7127  C  C     . MET B 1 406 ? 167.701 97.041  141.371 1.00 16799. ? 406 MET B C     1 
ATOM   7128  O  O     . MET B 1 406 ? 166.524 97.270  141.076 1.00 16795. ? 406 MET B O     1 
ATOM   7129  C  CB    . MET B 1 406 ? 169.869 97.427  140.167 1.00 16809. ? 406 MET B CB    1 
ATOM   7130  C  CG    . MET B 1 406 ? 169.518 98.901  140.158 1.00 16804. ? 406 MET B CG    1 
ATOM   7131  S  SD    . MET B 1 406 ? 170.997 99.916  140.134 1.00 16811. ? 406 MET B SD    1 
ATOM   7132  C  CE    . MET B 1 406 ? 171.674 99.429  138.549 1.00 16819. ? 406 MET B CE    1 
ATOM   7133  N  N     . LYS B 1 407 ? 168.185 97.249  142.593 1.00 16248. ? 407 LYS B N     1 
ATOM   7134  C  CA    . LYS B 1 407 ? 167.364 97.754  143.686 1.00 16233. ? 407 LYS B CA    1 
ATOM   7135  C  C     . LYS B 1 407 ? 167.927 99.087  144.154 1.00 16224. ? 407 LYS B C     1 
ATOM   7136  O  O     . LYS B 1 407 ? 169.079 99.159  144.595 1.00 16226. ? 407 LYS B O     1 
ATOM   7137  C  CB    . LYS B 1 407 ? 167.312 96.754  144.842 1.00 16233. ? 407 LYS B CB    1 
ATOM   7138  C  CG    . LYS B 1 407 ? 165.977 96.719  145.564 1.00 16234. ? 407 LYS B CG    1 
ATOM   7139  C  CD    . LYS B 1 407 ? 166.144 96.314  147.017 1.00 16238. ? 407 LYS B CD    1 
ATOM   7140  C  CE    . LYS B 1 407 ? 166.519 97.506  147.880 1.00 16241. ? 407 LYS B CE    1 
ATOM   7141  N  NZ    . LYS B 1 407 ? 165.722 98.712  147.527 1.00 16242. ? 407 LYS B NZ    1 
ATOM   7142  N  N     . LEU B 1 408 ? 167.116 100.133 144.058 1.00 15961. ? 408 LEU B N     1 
ATOM   7143  C  CA    . LEU B 1 408 ? 167.486 101.456 144.532 1.00 15961. ? 408 LEU B CA    1 
ATOM   7144  C  C     . LEU B 1 408 ? 167.421 101.496 146.054 1.00 15978. ? 408 LEU B C     1 
ATOM   7145  O  O     . LEU B 1 408 ? 166.794 100.641 146.683 1.00 15976. ? 408 LEU B O     1 
ATOM   7146  C  CB    . LEU B 1 408 ? 166.563 102.502 143.911 1.00 15959. ? 408 LEU B CB    1 
ATOM   7147  C  CG    . LEU B 1 408 ? 166.963 103.092 142.556 1.00 15956. ? 408 LEU B CG    1 
ATOM   7148  C  CD1   . LEU B 1 408 ? 168.388 103.616 142.593 1.00 15962. ? 408 LEU B CD1   1 
ATOM   7149  C  CD2   . LEU B 1 408 ? 166.797 102.078 141.439 1.00 15954. ? 408 LEU B CD2   1 
ATOM   7150  N  N     . PRO B 1 409 ? 168.076 102.473 146.683 1.00 16525. ? 409 PRO B N     1 
ATOM   7151  C  CA    . PRO B 1 409 ? 167.978 102.600 148.140 1.00 16533. ? 409 PRO B CA    1 
ATOM   7152  C  C     . PRO B 1 409 ? 166.543 102.837 148.586 1.00 16527. ? 409 PRO B C     1 
ATOM   7153  O  O     . PRO B 1 409 ? 165.679 103.246 147.807 1.00 16522. ? 409 PRO B O     1 
ATOM   7154  C  CB    . PRO B 1 409 ? 168.865 103.811 148.452 1.00 16541. ? 409 PRO B CB    1 
ATOM   7155  C  CG    . PRO B 1 409 ? 169.830 103.855 147.327 1.00 16541. ? 409 PRO B CG    1 
ATOM   7156  C  CD    . PRO B 1 409 ? 169.052 103.422 146.121 1.00 16536. ? 409 PRO B CD    1 
ATOM   7157  N  N     . GLU B 1 410 ? 166.297 102.562 149.864 1.00 16526. ? 410 GLU B N     1 
ATOM   7158  C  CA    . GLU B 1 410 ? 164.952 102.679 150.410 1.00 16505. ? 410 GLU B CA    1 
ATOM   7159  C  C     . GLU B 1 410 ? 164.448 104.112 150.297 1.00 16465. ? 410 GLU B C     1 
ATOM   7160  O  O     . GLU B 1 410 ? 165.205 105.077 150.431 1.00 16469. ? 410 GLU B O     1 
ATOM   7161  C  CB    . GLU B 1 410 ? 164.929 102.226 151.869 1.00 16512. ? 410 GLU B CB    1 
ATOM   7162  C  CG    . GLU B 1 410 ? 165.114 100.731 152.045 1.00 16534. ? 410 GLU B CG    1 
ATOM   7163  C  CD    . GLU B 1 410 ? 164.254 99.925  151.092 1.00 16535. ? 410 GLU B CD    1 
ATOM   7164  O  OE1   . GLU B 1 410 ? 163.015 100.071 151.139 1.00 16539. ? 410 GLU B OE1   1 
ATOM   7165  O  OE2   . GLU B 1 410 ? 164.817 99.147  150.295 1.00 16535. ? 410 GLU B OE2   1 
ATOM   7166  N  N     . THR B 1 411 ? 163.145 104.242 150.044 1.00 14825. ? 411 THR B N     1 
ATOM   7167  C  CA    . THR B 1 411 ? 162.544 105.540 149.771 1.00 14791. ? 411 THR B CA    1 
ATOM   7168  C  C     . THR B 1 411 ? 162.594 106.486 150.962 1.00 14775. ? 411 THR B C     1 
ATOM   7169  O  O     . THR B 1 411 ? 162.391 107.690 150.778 1.00 14765. ? 411 THR B O     1 
ATOM   7170  C  CB    . THR B 1 411 ? 161.096 105.358 149.317 1.00 14749. ? 411 THR B CB    1 
ATOM   7171  O  OG1   . THR B 1 411 ? 160.397 104.543 150.265 1.00 14742. ? 411 THR B OG1   1 
ATOM   7172  C  CG2   . THR B 1 411 ? 161.052 104.688 147.955 1.00 14760. ? 411 THR B CG2   1 
ATOM   7173  N  N     . ASN B 1 412 ? 162.856 105.984 152.166 1.00 15046. ? 412 ASN B N     1 
ATOM   7174  C  CA    . ASN B 1 412 ? 162.991 106.852 153.327 1.00 15039. ? 412 ASN B CA    1 
ATOM   7175  C  C     . ASN B 1 412 ? 164.386 107.448 153.463 1.00 15071. ? 412 ASN B C     1 
ATOM   7176  O  O     . ASN B 1 412 ? 164.606 108.263 154.365 1.00 15063. ? 412 ASN B O     1 
ATOM   7177  C  CB    . ASN B 1 412 ? 162.630 106.084 154.600 1.00 15036. ? 412 ASN B CB    1 
ATOM   7178  C  CG    . ASN B 1 412 ? 163.061 104.635 154.546 1.00 15057. ? 412 ASN B CG    1 
ATOM   7179  O  OD1   . ASN B 1 412 ? 162.640 103.884 153.667 1.00 15070. ? 412 ASN B OD1   1 
ATOM   7180  N  ND2   . ASN B 1 412 ? 163.900 104.231 155.490 1.00 15060. ? 412 ASN B ND2   1 
ATOM   7181  N  N     . LEU B 1 413 ? 165.323 107.070 152.599 1.00 15665. ? 413 LEU B N     1 
ATOM   7182  C  CA    . LEU B 1 413 ? 166.692 107.570 152.633 1.00 15685. ? 413 LEU B CA    1 
ATOM   7183  C  C     . LEU B 1 413 ? 167.036 108.302 151.343 1.00 15698. ? 413 LEU B C     1 
ATOM   7184  O  O     . LEU B 1 413 ? 168.148 108.195 150.826 1.00 15724. ? 413 LEU B O     1 
ATOM   7185  C  CB    . LEU B 1 413 ? 167.682 106.433 152.874 1.00 15698. ? 413 LEU B CB    1 
ATOM   7186  C  CG    . LEU B 1 413 ? 167.196 105.236 153.688 1.00 15692. ? 413 LEU B CG    1 
ATOM   7187  C  CD1   . LEU B 1 413 ? 168.218 104.116 153.635 1.00 15700. ? 413 LEU B CD1   1 
ATOM   7188  C  CD2   . LEU B 1 413 ? 166.929 105.645 155.126 1.00 15690. ? 413 LEU B CD2   1 
ATOM   7189  N  N     . PHE B 1 414 ? 166.080 109.057 150.804 1.00 15512. ? 414 PHE B N     1 
ATOM   7190  C  CA    . PHE B 1 414 ? 166.279 109.741 149.533 1.00 15515. ? 414 PHE B CA    1 
ATOM   7191  C  C     . PHE B 1 414 ? 166.793 111.165 149.682 1.00 15525. ? 414 PHE B C     1 
ATOM   7192  O  O     . PHE B 1 414 ? 167.260 111.741 148.694 1.00 15506. ? 414 PHE B O     1 
ATOM   7193  C  CB    . PHE B 1 414 ? 164.971 109.760 148.734 1.00 15483. ? 414 PHE B CB    1 
ATOM   7194  C  CG    . PHE B 1 414 ? 164.871 108.661 147.717 1.00 15484. ? 414 PHE B CG    1 
ATOM   7195  C  CD1   . PHE B 1 414 ? 165.037 107.341 148.090 1.00 15497. ? 414 PHE B CD1   1 
ATOM   7196  C  CD2   . PHE B 1 414 ? 164.611 108.947 146.390 1.00 15465. ? 414 PHE B CD2   1 
ATOM   7197  C  CE1   . PHE B 1 414 ? 164.947 106.327 147.160 1.00 15506. ? 414 PHE B CE1   1 
ATOM   7198  C  CE2   . PHE B 1 414 ? 164.519 107.936 145.457 1.00 15471. ? 414 PHE B CE2   1 
ATOM   7199  C  CZ    . PHE B 1 414 ? 164.688 106.625 145.842 1.00 15490. ? 414 PHE B CZ    1 
ATOM   7200  N  N     . GLU B 1 415 ? 166.725 111.744 150.880 1.00 16582. ? 415 GLU B N     1 
ATOM   7201  C  CA    . GLU B 1 415 ? 167.204 113.098 151.127 1.00 16608. ? 415 GLU B CA    1 
ATOM   7202  C  C     . GLU B 1 415 ? 168.616 113.110 151.700 1.00 16633. ? 415 GLU B C     1 
ATOM   7203  O  O     . GLU B 1 415 ? 169.010 114.073 152.366 1.00 16633. ? 415 GLU B O     1 
ATOM   7204  C  CB    . GLU B 1 415 ? 166.245 113.837 152.059 1.00 16617. ? 415 GLU B CB    1 
ATOM   7205  C  CG    . GLU B 1 415 ? 164.813 113.908 151.553 1.00 16619. ? 415 GLU B CG    1 
ATOM   7206  C  CD    . GLU B 1 415 ? 164.168 115.257 151.809 1.00 16619. ? 415 GLU B CD    1 
ATOM   7207  O  OE1   . GLU B 1 415 ? 164.841 116.137 152.384 1.00 16620. ? 415 GLU B OE1   1 
ATOM   7208  O  OE2   . GLU B 1 415 ? 162.990 115.437 151.437 1.00 16590. ? 415 GLU B OE2   1 
ATOM   7209  N  N     . THR B 1 416 ? 169.386 112.058 151.452 1.00 17008. ? 416 THR B N     1 
ATOM   7210  C  CA    . THR B 1 416 ? 170.722 111.897 152.000 1.00 17040. ? 416 THR B CA    1 
ATOM   7211  C  C     . THR B 1 416 ? 171.765 112.011 150.892 1.00 17062. ? 416 THR B C     1 
ATOM   7212  O  O     . THR B 1 416 ? 171.455 112.316 149.737 1.00 17042. ? 416 THR B O     1 
ATOM   7213  C  CB    . THR B 1 416 ? 170.839 110.560 152.733 1.00 17048. ? 416 THR B CB    1 
ATOM   7214  O  OG1   . THR B 1 416 ? 170.716 109.488 151.792 1.00 17045. ? 416 THR B OG1   1 
ATOM   7215  C  CG2   . THR B 1 416 ? 169.750 110.431 153.784 1.00 17034. ? 416 THR B CG2   1 
ATOM   7216  N  N     . GLU B 1 417 ? 173.022 111.765 151.261 1.00 17989. ? 417 GLU B N     1 
ATOM   7217  C  CA    . GLU B 1 417 ? 174.139 111.928 150.338 1.00 18009. ? 417 GLU B CA    1 
ATOM   7218  C  C     . GLU B 1 417 ? 174.550 110.621 149.670 1.00 18009. ? 417 GLU B C     1 
ATOM   7219  O  O     . GLU B 1 417 ? 174.903 110.620 148.485 1.00 18003. ? 417 GLU B O     1 
ATOM   7220  C  CB    . GLU B 1 417 ? 175.338 112.536 151.071 1.00 18025. ? 417 GLU B CB    1 
ATOM   7221  C  CG    . GLU B 1 417 ? 176.603 112.633 150.233 1.00 18029. ? 417 GLU B CG    1 
ATOM   7222  C  CD    . GLU B 1 417 ? 176.410 113.467 148.982 1.00 18023. ? 417 GLU B CD    1 
ATOM   7223  O  OE1   . GLU B 1 417 ? 175.975 114.631 149.105 1.00 18024. ? 417 GLU B OE1   1 
ATOM   7224  O  OE2   . GLU B 1 417 ? 176.694 112.960 147.876 1.00 18010. ? 417 GLU B OE2   1 
ATOM   7225  N  N     . GLU B 1 418 ? 174.521 109.502 150.398 1.00 18260. ? 418 GLU B N     1 
ATOM   7226  C  CA    . GLU B 1 418 ? 174.907 108.235 149.786 1.00 18272. ? 418 GLU B CA    1 
ATOM   7227  C  C     . GLU B 1 418 ? 173.938 107.829 148.684 1.00 18235. ? 418 GLU B C     1 
ATOM   7228  O  O     . GLU B 1 418 ? 174.355 107.238 147.682 1.00 18228. ? 418 GLU B O     1 
ATOM   7229  C  CB    . GLU B 1 418 ? 175.024 107.117 150.830 1.00 18289. ? 418 GLU B CB    1 
ATOM   7230  C  CG    . GLU B 1 418 ? 173.800 106.784 151.707 1.00 18289. ? 418 GLU B CG    1 
ATOM   7231  C  CD    . GLU B 1 418 ? 173.216 107.943 152.510 1.00 18283. ? 418 GLU B CD    1 
ATOM   7232  O  OE1   . GLU B 1 418 ? 173.667 109.099 152.373 1.00 18276. ? 418 GLU B OE1   1 
ATOM   7233  O  OE2   . GLU B 1 418 ? 172.291 107.681 153.308 1.00 18281. ? 418 GLU B OE2   1 
ATOM   7234  N  N     . THR B 1 419 ? 172.648 108.134 148.841 1.00 17189. ? 419 THR B N     1 
ATOM   7235  C  CA    . THR B 1 419 ? 171.712 107.880 147.752 1.00 17158. ? 419 THR B CA    1 
ATOM   7236  C  C     . THR B 1 419 ? 172.031 108.745 146.537 1.00 17139. ? 419 THR B C     1 
ATOM   7237  O  O     . THR B 1 419 ? 171.895 108.289 145.397 1.00 17131. ? 419 THR B O     1 
ATOM   7238  C  CB    . THR B 1 419 ? 170.270 108.103 148.217 1.00 17143. ? 419 THR B CB    1 
ATOM   7239  O  OG1   . THR B 1 419 ? 169.366 107.773 147.156 1.00 17125. ? 419 THR B OG1   1 
ATOM   7240  C  CG2   . THR B 1 419 ? 170.042 109.545 148.637 1.00 17132. ? 419 THR B CG2   1 
ATOM   7241  N  N     . ARG B 1 420 ? 172.472 109.987 146.759 1.00 16719. ? 420 ARG B N     1 
ATOM   7242  C  CA    . ARG B 1 420 ? 172.892 110.834 145.649 1.00 16701. ? 420 ARG B CA    1 
ATOM   7243  C  C     . ARG B 1 420 ? 174.101 110.239 144.943 1.00 16703. ? 420 ARG B C     1 
ATOM   7244  O  O     . ARG B 1 420 ? 174.182 110.246 143.710 1.00 16693. ? 420 ARG B O     1 
ATOM   7245  C  CB    . ARG B 1 420 ? 173.205 112.244 146.148 1.00 16699. ? 420 ARG B CB    1 
ATOM   7246  C  CG    . ARG B 1 420 ? 173.197 113.295 145.053 1.00 16673. ? 420 ARG B CG    1 
ATOM   7247  C  CD    . ARG B 1 420 ? 174.046 114.496 145.437 1.00 16684. ? 420 ARG B CD    1 
ATOM   7248  N  NE    . ARG B 1 420 ? 175.445 114.136 145.640 1.00 16700. ? 420 ARG B NE    1 
ATOM   7249  C  CZ    . ARG B 1 420 ? 176.274 113.750 144.680 1.00 16695. ? 420 ARG B CZ    1 
ATOM   7250  N  NH1   . ARG B 1 420 ? 175.891 113.691 143.415 1.00 16685. ? 420 ARG B NH1   1 
ATOM   7251  N  NH2   . ARG B 1 420 ? 177.524 113.423 144.996 1.00 16701. ? 420 ARG B NH2   1 
ATOM   7252  N  N     . LYS B 1 421 ? 175.060 109.726 145.715 1.00 17037. ? 421 LYS B N     1 
ATOM   7253  C  CA    . LYS B 1 421 ? 176.234 109.099 145.117 1.00 17039. ? 421 LYS B CA    1 
ATOM   7254  C  C     . LYS B 1 421 ? 175.848 107.866 144.310 1.00 17024. ? 421 LYS B C     1 
ATOM   7255  O  O     . LYS B 1 421 ? 176.367 107.641 143.211 1.00 17031. ? 421 LYS B O     1 
ATOM   7256  C  CB    . LYS B 1 421 ? 177.248 108.736 146.202 1.00 17053. ? 421 LYS B CB    1 
ATOM   7257  C  CG    . LYS B 1 421 ? 178.322 109.788 146.421 1.00 17051. ? 421 LYS B CG    1 
ATOM   7258  C  CD    . LYS B 1 421 ? 179.133 110.032 145.156 1.00 17050. ? 421 LYS B CD    1 
ATOM   7259  C  CE    . LYS B 1 421 ? 179.751 108.746 144.626 1.00 17047. ? 421 LYS B CE    1 
ATOM   7260  N  NZ    . LYS B 1 421 ? 180.543 108.038 145.668 1.00 17046. ? 421 LYS B NZ    1 
ATOM   7261  N  N     . ILE B 1 422 ? 174.936 107.051 144.845 1.00 16486. ? 422 ILE B N     1 
ATOM   7262  C  CA    . ILE B 1 422 ? 174.470 105.876 144.115 1.00 16477. ? 422 ILE B CA    1 
ATOM   7263  C  C     . ILE B 1 422 ? 173.790 106.282 142.818 1.00 16472. ? 422 ILE B C     1 
ATOM   7264  O  O     . ILE B 1 422 ? 174.033 105.682 141.764 1.00 16462. ? 422 ILE B O     1 
ATOM   7265  C  CB    . ILE B 1 422 ? 173.534 105.027 145.000 1.00 16472. ? 422 ILE B CB    1 
ATOM   7266  C  CG1   . ILE B 1 422 ? 174.306 104.440 146.182 1.00 16472. ? 422 ILE B CG1   1 
ATOM   7267  C  CG2   . ILE B 1 422 ? 172.891 103.918 144.186 1.00 16461. ? 422 ILE B CG2   1 
ATOM   7268  C  CD1   . ILE B 1 422 ? 173.508 103.446 146.996 1.00 16468. ? 422 ILE B CD1   1 
ATOM   7269  N  N     . LEU B 1 423 ? 172.935 107.305 142.865 1.00 16385. ? 423 LEU B N     1 
ATOM   7270  C  CA    . LEU B 1 423 ? 172.251 107.758 141.658 1.00 16371. ? 423 LEU B CA    1 
ATOM   7271  C  C     . LEU B 1 423 ? 173.241 108.299 140.634 1.00 16367. ? 423 LEU B C     1 
ATOM   7272  O  O     . LEU B 1 423 ? 173.095 108.066 139.430 1.00 16357. ? 423 LEU B O     1 
ATOM   7273  C  CB    . LEU B 1 423 ? 171.204 108.814 142.011 1.00 16362. ? 423 LEU B CB    1 
ATOM   7274  C  CG    . LEU B 1 423 ? 169.894 108.274 142.583 1.00 16364. ? 423 LEU B CG    1 
ATOM   7275  C  CD1   . LEU B 1 423 ? 168.840 109.361 142.602 1.00 16325. ? 423 LEU B CD1   1 
ATOM   7276  C  CD2   . LEU B 1 423 ? 169.413 107.074 141.785 1.00 16358. ? 423 LEU B CD2   1 
ATOM   7277  N  N     . ASP B 1 424 ? 174.255 109.031 141.094 1.00 16539. ? 424 ASP B N     1 
ATOM   7278  C  CA    . ASP B 1 424 ? 175.279 109.558 140.201 1.00 16538. ? 424 ASP B CA    1 
ATOM   7279  C  C     . ASP B 1 424 ? 176.046 108.426 139.532 1.00 16549. ? 424 ASP B C     1 
ATOM   7280  O  O     . ASP B 1 424 ? 176.305 108.469 138.324 1.00 16547. ? 424 ASP B O     1 
ATOM   7281  C  CB    . ASP B 1 424 ? 176.237 110.469 140.967 1.00 16549. ? 424 ASP B CB    1 
ATOM   7282  C  CG    . ASP B 1 424 ? 176.884 111.510 140.080 1.00 16543. ? 424 ASP B CG    1 
ATOM   7283  O  OD1   . ASP B 1 424 ? 176.482 111.621 138.904 1.00 16532. ? 424 ASP B OD1   1 
ATOM   7284  O  OD2   . ASP B 1 424 ? 177.795 112.218 140.558 1.00 16548. ? 424 ASP B OD2   1 
ATOM   7285  N  N     . ASP B 1 425 ? 176.406 107.406 140.312 1.00 16989. ? 425 ASP B N     1 
ATOM   7286  C  CA    . ASP B 1 425 ? 177.114 106.262 139.749 1.00 17002. ? 425 ASP B CA    1 
ATOM   7287  C  C     . ASP B 1 425 ? 176.251 105.528 138.733 1.00 16979. ? 425 ASP B C     1 
ATOM   7288  O  O     . ASP B 1 425 ? 176.748 105.079 137.694 1.00 16985. ? 425 ASP B O     1 
ATOM   7289  C  CB    . ASP B 1 425 ? 177.556 105.316 140.863 1.00 17018. ? 425 ASP B CB    1 
ATOM   7290  C  CG    . ASP B 1 425 ? 178.521 105.969 141.832 1.00 17019. ? 425 ASP B CG    1 
ATOM   7291  O  OD1   . ASP B 1 425 ? 178.883 107.143 141.609 1.00 17020. ? 425 ASP B OD1   1 
ATOM   7292  O  OD2   . ASP B 1 425 ? 178.916 105.310 142.816 1.00 17022. ? 425 ASP B OD2   1 
ATOM   7293  N  N     . ILE B 1 426 ? 174.954 105.392 139.017 1.00 16280. ? 426 ILE B N     1 
ATOM   7294  C  CA    . ILE B 1 426 ? 174.065 104.703 138.086 1.00 16268. ? 426 ILE B CA    1 
ATOM   7295  C  C     . ILE B 1 426 ? 173.916 105.504 136.799 1.00 16257. ? 426 ILE B C     1 
ATOM   7296  O  O     . ILE B 1 426 ? 173.925 104.944 135.696 1.00 16252. ? 426 ILE B O     1 
ATOM   7297  C  CB    . ILE B 1 426 ? 172.703 104.428 138.747 1.00 16261. ? 426 ILE B CB    1 
ATOM   7298  C  CG1   . ILE B 1 426 ? 172.883 103.467 139.920 1.00 16267. ? 426 ILE B CG1   1 
ATOM   7299  C  CG2   . ILE B 1 426 ? 171.725 103.852 137.741 1.00 16255. ? 426 ILE B CG2   1 
ATOM   7300  C  CD1   . ILE B 1 426 ? 173.629 102.210 139.558 1.00 16269. ? 426 ILE B CD1   1 
ATOM   7301  N  N     . CYS B 1 427 ? 173.782 106.826 136.918 1.00 15835. ? 427 CYS B N     1 
ATOM   7302  C  CA    . CYS B 1 427 ? 173.682 107.670 135.733 1.00 15818. ? 427 CYS B CA    1 
ATOM   7303  C  C     . CYS B 1 427 ? 174.949 107.590 134.894 1.00 15834. ? 427 CYS B C     1 
ATOM   7304  O  O     . CYS B 1 427 ? 174.885 107.539 133.661 1.00 15824. ? 427 CYS B O     1 
ATOM   7305  C  CB    . CYS B 1 427 ? 173.401 109.116 136.141 1.00 15814. ? 427 CYS B CB    1 
ATOM   7306  S  SG    . CYS B 1 427 ? 171.669 109.472 136.502 1.00 15765. ? 427 CYS B SG    1 
ATOM   7307  N  N     . VAL B 1 428 ? 176.113 107.581 135.546 1.00 16351. ? 428 VAL B N     1 
ATOM   7308  C  CA    . VAL B 1 428 ? 177.370 107.458 134.815 1.00 16355. ? 428 VAL B CA    1 
ATOM   7309  C  C     . VAL B 1 428 ? 177.455 106.106 134.117 1.00 16350. ? 428 VAL B C     1 
ATOM   7310  O  O     . VAL B 1 428 ? 177.842 106.020 132.946 1.00 16353. ? 428 VAL B O     1 
ATOM   7311  C  CB    . VAL B 1 428 ? 178.560 107.685 135.765 1.00 16362. ? 428 VAL B CB    1 
ATOM   7312  C  CG1   . VAL B 1 428 ? 179.820 107.037 135.214 1.00 16366. ? 428 VAL B CG1   1 
ATOM   7313  C  CG2   . VAL B 1 428 ? 178.775 109.173 135.993 1.00 16360. ? 428 VAL B CG2   1 
ATOM   7314  N  N     . ALA B 1 429 ? 177.090 105.031 134.820 1.00 16090. ? 429 ALA B N     1 
ATOM   7315  C  CA    . ALA B 1 429 ? 177.166 103.698 134.230 1.00 16082. ? 429 ALA B CA    1 
ATOM   7316  C  C     . ALA B 1 429 ? 176.205 103.551 133.058 1.00 16070. ? 429 ALA B C     1 
ATOM   7317  O  O     . ALA B 1 429 ? 176.551 102.953 132.033 1.00 16067. ? 429 ALA B O     1 
ATOM   7318  C  CB    . ALA B 1 429 ? 176.881 102.638 135.293 1.00 16089. ? 429 ALA B CB    1 
ATOM   7319  N  N     . LYS B 1 430 ? 174.996 104.092 133.187 1.00 15871. ? 430 LYS B N     1 
ATOM   7320  C  CA    . LYS B 1 430 ? 173.977 103.975 132.154 1.00 15863. ? 430 LYS B CA    1 
ATOM   7321  C  C     . LYS B 1 430 ? 174.064 105.082 131.110 1.00 15860. ? 430 LYS B C     1 
ATOM   7322  O  O     . LYS B 1 430 ? 173.178 105.179 130.255 1.00 15857. ? 430 LYS B O     1 
ATOM   7323  C  CB    . LYS B 1 430 ? 172.584 103.962 132.787 1.00 15856. ? 430 LYS B CB    1 
ATOM   7324  C  CG    . LYS B 1 430 ? 172.270 102.682 133.542 1.00 15858. ? 430 LYS B CG    1 
ATOM   7325  C  CD    . LYS B 1 430 ? 172.565 101.460 132.687 1.00 15858. ? 430 LYS B CD    1 
ATOM   7326  C  CE    . LYS B 1 430 ? 172.044 100.189 133.335 1.00 15862. ? 430 LYS B CE    1 
ATOM   7327  N  NZ    . LYS B 1 430 ? 170.599 100.286 133.667 1.00 15857. ? 430 LYS B NZ    1 
ATOM   7328  N  N     . ALA B 1 431 ? 175.101 105.920 131.174 1.00 15806. ? 431 ALA B N     1 
ATOM   7329  C  CA    . ALA B 1 431 ? 175.351 106.967 130.184 1.00 15803. ? 431 ALA B CA    1 
ATOM   7330  C  C     . ALA B 1 431 ? 174.209 107.976 130.109 1.00 15813. ? 431 ALA B C     1 
ATOM   7331  O  O     . ALA B 1 431 ? 173.962 108.573 129.059 1.00 15823. ? 431 ALA B O     1 
ATOM   7332  C  CB    . ALA B 1 431 ? 175.629 106.373 128.800 1.00 15803. ? 431 ALA B CB    1 
ATOM   7333  N  N     . VAL B 1 432 ? 173.504 108.175 131.216 1.00 16067. ? 432 VAL B N     1 
ATOM   7334  C  CA    . VAL B 1 432 ? 172.492 109.220 131.294 1.00 16084. ? 432 VAL B CA    1 
ATOM   7335  C  C     . VAL B 1 432 ? 173.180 110.555 131.533 1.00 16133. ? 432 VAL B C     1 
ATOM   7336  O  O     . VAL B 1 432 ? 174.069 110.670 132.385 1.00 16123. ? 432 VAL B O     1 
ATOM   7337  C  CB    . VAL B 1 432 ? 171.471 108.907 132.400 1.00 16068. ? 432 VAL B CB    1 
ATOM   7338  C  CG1   . VAL B 1 432 ? 170.253 109.799 132.262 1.00 16047. ? 432 VAL B CG1   1 
ATOM   7339  C  CG2   . VAL B 1 432 ? 171.072 107.443 132.346 1.00 16053. ? 432 VAL B CG2   1 
ATOM   7340  N  N     . GLU B 1 433 ? 172.775 111.571 130.779 1.00 18165. ? 433 GLU B N     1 
ATOM   7341  C  CA    . GLU B 1 433 ? 173.410 112.880 130.815 1.00 18202. ? 433 GLU B CA    1 
ATOM   7342  C  C     . GLU B 1 433 ? 172.604 113.823 131.696 1.00 18202. ? 433 GLU B C     1 
ATOM   7343  O  O     . GLU B 1 433 ? 171.382 113.927 131.547 1.00 18188. ? 433 GLU B O     1 
ATOM   7344  C  CB    . GLU B 1 433 ? 173.545 113.460 129.406 1.00 18220. ? 433 GLU B CB    1 
ATOM   7345  C  CG    . GLU B 1 433 ? 174.647 114.496 129.265 1.00 18231. ? 433 GLU B CG    1 
ATOM   7346  C  CD    . GLU B 1 433 ? 176.031 113.877 129.231 1.00 18235. ? 433 GLU B CD    1 
ATOM   7347  O  OE1   . GLU B 1 433 ? 176.130 112.646 129.047 1.00 18228. ? 433 GLU B OE1   1 
ATOM   7348  O  OE2   . GLU B 1 433 ? 177.020 114.622 129.390 1.00 18244. ? 433 GLU B OE2   1 
ATOM   7349  N  N     . CYS B 1 434 ? 173.289 114.504 132.609 1.00 18105. ? 434 CYS B N     1 
ATOM   7350  C  CA    . CYS B 1 434 ? 172.651 115.477 133.484 1.00 18095. ? 434 CYS B CA    1 
ATOM   7351  C  C     . CYS B 1 434 ? 173.623 116.607 133.798 1.00 18095. ? 434 CYS B C     1 
ATOM   7352  O  O     . CYS B 1 434 ? 174.615 116.395 134.507 1.00 18090. ? 434 CYS B O     1 
ATOM   7353  C  CB    . CYS B 1 434 ? 172.167 114.813 134.774 1.00 18081. ? 434 CYS B CB    1 
ATOM   7354  S  SG    . CYS B 1 434 ? 171.522 115.968 136.003 1.00 18051. ? 434 CYS B SG    1 
ATOM   7355  N  N     . PRO B 1 435 ? 173.381 117.810 133.289 1.00 17648. ? 435 PRO B N     1 
ATOM   7356  C  CA    . PRO B 1 435 ? 174.281 118.933 133.567 1.00 17634. ? 435 PRO B CA    1 
ATOM   7357  C  C     . PRO B 1 435 ? 174.204 119.342 135.025 1.00 17610. ? 435 PRO B C     1 
ATOM   7358  O  O     . PRO B 1 435 ? 173.187 119.102 135.693 1.00 17604. ? 435 PRO B O     1 
ATOM   7359  C  CB    . PRO B 1 435 ? 173.756 120.043 132.645 1.00 17635. ? 435 PRO B CB    1 
ATOM   7360  C  CG    . PRO B 1 435 ? 172.329 119.699 132.418 1.00 17634. ? 435 PRO B CG    1 
ATOM   7361  C  CD    . PRO B 1 435 ? 172.251 118.200 132.429 1.00 17639. ? 435 PRO B CD    1 
ATOM   7362  N  N     . PRO B 1 436 ? 175.261 119.953 135.558 1.00 17041. ? 436 PRO B N     1 
ATOM   7363  C  CA    . PRO B 1 436 ? 175.237 120.352 136.961 1.00 17030. ? 436 PRO B CA    1 
ATOM   7364  C  C     . PRO B 1 436 ? 174.184 121.414 137.197 1.00 17016. ? 436 PRO B C     1 
ATOM   7365  O  O     . PRO B 1 436 ? 173.838 122.186 136.283 1.00 17023. ? 436 PRO B O     1 
ATOM   7366  C  CB    . PRO B 1 436 ? 176.653 120.898 137.196 1.00 17033. ? 436 PRO B CB    1 
ATOM   7367  C  CG    . PRO B 1 436 ? 177.485 120.275 136.128 1.00 17038. ? 436 PRO B CG    1 
ATOM   7368  C  CD    . PRO B 1 436 ? 176.581 120.164 134.943 1.00 17043. ? 436 PRO B CD    1 
ATOM   7369  N  N     . PRO B 1 437 ? 173.640 121.495 138.420 1.00 16619. ? 437 PRO B N     1 
ATOM   7370  C  CA    . PRO B 1 437 ? 173.974 120.687 139.600 1.00 16618. ? 437 PRO B CA    1 
ATOM   7371  C  C     . PRO B 1 437 ? 173.368 119.289 139.543 1.00 16604. ? 437 PRO B C     1 
ATOM   7372  O  O     . PRO B 1 437 ? 172.240 119.105 139.100 1.00 16599. ? 437 PRO B O     1 
ATOM   7373  C  CB    . PRO B 1 437 ? 173.401 121.518 140.753 1.00 16619. ? 437 PRO B CB    1 
ATOM   7374  C  CG    . PRO B 1 437 ? 172.259 122.305 140.153 1.00 16632. ? 437 PRO B CG    1 
ATOM   7375  C  CD    . PRO B 1 437 ? 172.458 122.342 138.653 1.00 16613. ? 437 PRO B CD    1 
ATOM   7376  N  N     . ARG B 1 438 ? 174.111 118.282 139.996 1.00 16141. ? 438 ARG B N     1 
ATOM   7377  C  CA    . ARG B 1 438 ? 173.659 116.893 139.932 1.00 16125. ? 438 ARG B CA    1 
ATOM   7378  C  C     . ARG B 1 438 ? 172.988 116.485 141.244 1.00 16103. ? 438 ARG B C     1 
ATOM   7379  O  O     . ARG B 1 438 ? 173.419 115.572 141.947 1.00 16113. ? 438 ARG B O     1 
ATOM   7380  C  CB    . ARG B 1 438 ? 174.827 115.974 139.596 1.00 16119. ? 438 ARG B CB    1 
ATOM   7381  C  CG    . ARG B 1 438 ? 175.152 115.908 138.116 1.00 16138. ? 438 ARG B CG    1 
ATOM   7382  C  CD    . ARG B 1 438 ? 176.516 115.286 137.879 1.00 16121. ? 438 ARG B CD    1 
ATOM   7383  N  NE    . ARG B 1 438 ? 176.424 113.859 137.595 1.00 16123. ? 438 ARG B NE    1 
ATOM   7384  C  CZ    . ARG B 1 438 ? 176.016 113.348 136.441 1.00 16137. ? 438 ARG B CZ    1 
ATOM   7385  N  NH1   . ARG B 1 438 ? 175.655 114.122 135.431 1.00 16159. ? 438 ARG B NH1   1 
ATOM   7386  N  NH2   . ARG B 1 438 ? 175.972 112.027 136.297 1.00 16130. ? 438 ARG B NH2   1 
ATOM   7387  N  N     . THR B 1 439 ? 171.907 117.189 141.564 1.00 15577. ? 439 THR B N     1 
ATOM   7388  C  CA    . THR B 1 439 ? 171.151 116.879 142.765 1.00 15558. ? 439 THR B CA    1 
ATOM   7389  C  C     . THR B 1 439 ? 170.331 115.606 142.560 1.00 15527. ? 439 THR B C     1 
ATOM   7390  O  O     . THR B 1 439 ? 170.197 115.088 141.448 1.00 15527. ? 439 THR B O     1 
ATOM   7391  C  CB    . THR B 1 439 ? 170.241 118.046 143.145 1.00 15555. ? 439 THR B CB    1 
ATOM   7392  O  OG1   . THR B 1 439 ? 169.419 117.669 144.256 1.00 15543. ? 439 THR B OG1   1 
ATOM   7393  C  CG2   . THR B 1 439 ? 169.355 118.429 141.978 1.00 15551. ? 439 THR B CG2   1 
ATOM   7394  N  N     . THR B 1 440 ? 169.785 115.096 143.665 1.00 14759. ? 440 THR B N     1 
ATOM   7395  C  CA    . THR B 1 440 ? 169.027 113.850 143.613 1.00 14730. ? 440 THR B CA    1 
ATOM   7396  C  C     . THR B 1 440 ? 167.782 113.989 142.745 1.00 14717. ? 440 THR B C     1 
ATOM   7397  O  O     . THR B 1 440 ? 167.453 113.082 141.971 1.00 14711. ? 440 THR B O     1 
ATOM   7398  C  CB    . THR B 1 440 ? 168.644 113.412 145.025 1.00 14728. ? 440 THR B CB    1 
ATOM   7399  O  OG1   . THR B 1 440 ? 169.726 113.689 145.922 1.00 14754. ? 440 THR B OG1   1 
ATOM   7400  C  CG2   . THR B 1 440 ? 168.339 111.927 145.056 1.00 14741. ? 440 THR B CG2   1 
ATOM   7401  N  N     . ALA B 1 441 ? 167.076 115.114 142.863 1.00 14510. ? 441 ALA B N     1 
ATOM   7402  C  CA    . ALA B 1 441 ? 165.846 115.302 142.100 1.00 14496. ? 441 ALA B CA    1 
ATOM   7403  C  C     . ALA B 1 441 ? 166.122 115.309 140.602 1.00 14510. ? 441 ALA B C     1 
ATOM   7404  O  O     . ALA B 1 441 ? 165.417 114.653 139.825 1.00 14485. ? 441 ALA B O     1 
ATOM   7405  C  CB    . ALA B 1 441 ? 165.159 116.598 142.528 1.00 14484. ? 441 ALA B CB    1 
ATOM   7406  N  N     . ARG B 1 442 ? 167.153 116.041 140.177 1.00 15309. ? 442 ARG B N     1 
ATOM   7407  C  CA    . ARG B 1 442 ? 167.470 116.113 138.755 1.00 15318. ? 442 ARG B CA    1 
ATOM   7408  C  C     . ARG B 1 442 ? 167.952 114.769 138.226 1.00 15293. ? 442 ARG B C     1 
ATOM   7409  O  O     . ARG B 1 442 ? 167.606 114.377 137.106 1.00 15282. ? 442 ARG B O     1 
ATOM   7410  C  CB    . ARG B 1 442 ? 168.514 117.199 138.507 1.00 15345. ? 442 ARG B CB    1 
ATOM   7411  C  CG    . ARG B 1 442 ? 167.961 118.609 138.610 1.00 15349. ? 442 ARG B CG    1 
ATOM   7412  C  CD    . ARG B 1 442 ? 169.060 119.646 138.488 1.00 15365. ? 442 ARG B CD    1 
ATOM   7413  N  NE    . ARG B 1 442 ? 169.860 119.442 137.288 1.00 15383. ? 442 ARG B NE    1 
ATOM   7414  C  CZ    . ARG B 1 442 ? 169.608 120.010 136.117 1.00 15380. ? 442 ARG B CZ    1 
ATOM   7415  N  NH1   . ARG B 1 442 ? 168.582 120.829 135.953 1.00 15353. ? 442 ARG B NH1   1 
ATOM   7416  N  NH2   . ARG B 1 442 ? 170.405 119.751 135.085 1.00 15406. ? 442 ARG B NH2   1 
ATOM   7417  N  N     . LEU B 1 443 ? 168.752 114.051 139.016 1.00 14643. ? 443 LEU B N     1 
ATOM   7418  C  CA    . LEU B 1 443 ? 169.205 112.730 138.598 1.00 14620. ? 443 LEU B CA    1 
ATOM   7419  C  C     . LEU B 1 443 ? 168.031 111.776 138.435 1.00 14589. ? 443 LEU B C     1 
ATOM   7420  O  O     . LEU B 1 443 ? 167.968 111.014 137.462 1.00 14579. ? 443 LEU B O     1 
ATOM   7421  C  CB    . LEU B 1 443 ? 170.205 112.177 139.612 1.00 14633. ? 443 LEU B CB    1 
ATOM   7422  C  CG    . LEU B 1 443 ? 171.690 112.304 139.279 1.00 14658. ? 443 LEU B CG    1 
ATOM   7423  C  CD1   . LEU B 1 443 ? 172.022 113.712 138.829 1.00 14682. ? 443 LEU B CD1   1 
ATOM   7424  C  CD2   . LEU B 1 443 ? 172.526 111.923 140.484 1.00 14689. ? 443 LEU B CD2   1 
ATOM   7425  N  N     . LEU B 1 444 ? 167.087 111.807 139.378 1.00 14088. ? 444 LEU B N     1 
ATOM   7426  C  CA    . LEU B 1 444 ? 165.903 110.962 139.267 1.00 14062. ? 444 LEU B CA    1 
ATOM   7427  C  C     . LEU B 1 444 ? 165.074 111.336 138.047 1.00 14040. ? 444 LEU B C     1 
ATOM   7428  O  O     . LEU B 1 444 ? 164.563 110.458 137.344 1.00 14030. ? 444 LEU B O     1 
ATOM   7429  C  CB    . LEU B 1 444 ? 165.064 111.067 140.537 1.00 14060. ? 444 LEU B CB    1 
ATOM   7430  C  CG    . LEU B 1 444 ? 165.247 109.943 141.554 1.00 14061. ? 444 LEU B CG    1 
ATOM   7431  C  CD1   . LEU B 1 444 ? 164.777 110.397 142.923 1.00 14057. ? 444 LEU B CD1   1 
ATOM   7432  C  CD2   . LEU B 1 444 ? 164.503 108.696 141.113 1.00 14054. ? 444 LEU B CD2   1 
ATOM   7433  N  N     . ASP B 1 445 ? 164.925 112.636 137.784 1.00 13784. ? 445 ASP B N     1 
ATOM   7434  C  CA    . ASP B 1 445 ? 164.173 113.074 136.613 1.00 13765. ? 445 ASP B CA    1 
ATOM   7435  C  C     . ASP B 1 445 ? 164.819 112.574 135.328 1.00 13758. ? 445 ASP B C     1 
ATOM   7436  O  O     . ASP B 1 445 ? 164.132 112.087 134.423 1.00 13755. ? 445 ASP B O     1 
ATOM   7437  C  CB    . ASP B 1 445 ? 164.065 114.597 136.601 1.00 13769. ? 445 ASP B CB    1 
ATOM   7438  C  CG    . ASP B 1 445 ? 163.213 115.111 135.462 1.00 13751. ? 445 ASP B CG    1 
ATOM   7439  O  OD1   . ASP B 1 445 ? 162.689 114.281 134.690 1.00 13753. ? 445 ASP B OD1   1 
ATOM   7440  O  OD2   . ASP B 1 445 ? 163.063 116.344 135.338 1.00 13747. ? 445 ASP B OD2   1 
ATOM   7441  N  N     . LYS B 1 446 ? 166.145 112.688 135.229 1.00 13803. ? 446 LYS B N     1 
ATOM   7442  C  CA    . LYS B 1 446 ? 166.837 112.223 134.032 1.00 13792. ? 446 LYS B CA    1 
ATOM   7443  C  C     . LYS B 1 446 ? 166.707 110.714 133.871 1.00 13788. ? 446 LYS B C     1 
ATOM   7444  O  O     . LYS B 1 446 ? 166.466 110.220 132.763 1.00 13810. ? 446 LYS B O     1 
ATOM   7445  C  CB    . LYS B 1 446 ? 168.307 112.634 134.077 1.00 13825. ? 446 LYS B CB    1 
ATOM   7446  C  CG    . LYS B 1 446 ? 168.523 114.133 134.013 1.00 13860. ? 446 LYS B CG    1 
ATOM   7447  C  CD    . LYS B 1 446 ? 168.134 114.688 132.657 1.00 13839. ? 446 LYS B CD    1 
ATOM   7448  C  CE    . LYS B 1 446 ? 168.043 116.202 132.693 1.00 13842. ? 446 LYS B CE    1 
ATOM   7449  N  NZ    . LYS B 1 446 ? 167.101 116.669 133.746 1.00 13814. ? 446 LYS B NZ    1 
ATOM   7450  N  N     . LEU B 1 447 ? 166.853 109.967 134.967 1.00 13337. ? 447 LEU B N     1 
ATOM   7451  C  CA    . LEU B 1 447 ? 166.716 108.516 134.895 1.00 13325. ? 447 LEU B CA    1 
ATOM   7452  C  C     . LEU B 1 447 ? 165.314 108.115 134.456 1.00 13333. ? 447 LEU B C     1 
ATOM   7453  O  O     . LEU B 1 447 ? 165.147 107.208 133.631 1.00 13349. ? 447 LEU B O     1 
ATOM   7454  C  CB    . LEU B 1 447 ? 167.048 107.893 136.249 1.00 13316. ? 447 LEU B CB    1 
ATOM   7455  C  CG    . LEU B 1 447 ? 168.513 107.544 136.500 1.00 13305. ? 447 LEU B CG    1 
ATOM   7456  C  CD1   . LEU B 1 447 ? 168.676 106.909 137.867 1.00 13333. ? 447 LEU B CD1   1 
ATOM   7457  C  CD2   . LEU B 1 447 ? 169.030 106.619 135.416 1.00 13342. ? 447 LEU B CD2   1 
ATOM   7458  N  N     . VAL B 1 448 ? 164.294 108.781 134.997 1.00 13262. ? 448 VAL B N     1 
ATOM   7459  C  CA    . VAL B 1 448 ? 162.917 108.465 134.634 1.00 13249. ? 448 VAL B CA    1 
ATOM   7460  C  C     . VAL B 1 448 ? 162.659 108.797 133.172 1.00 13277. ? 448 VAL B C     1 
ATOM   7461  O  O     . VAL B 1 448 ? 162.050 108.007 132.441 1.00 13292. ? 448 VAL B O     1 
ATOM   7462  C  CB    . VAL B 1 448 ? 161.948 109.207 135.569 1.00 13232. ? 448 VAL B CB    1 
ATOM   7463  C  CG1   . VAL B 1 448 ? 160.542 109.198 135.002 1.00 13242. ? 448 VAL B CG1   1 
ATOM   7464  C  CG2   . VAL B 1 448 ? 161.984 108.579 136.938 1.00 13241. ? 448 VAL B CG2   1 
ATOM   7465  N  N     . GLY B 1 449 ? 163.120 109.963 132.718 1.00 13741. ? 449 GLY B N     1 
ATOM   7466  C  CA    . GLY B 1 449 ? 162.929 110.325 131.326 1.00 13759. ? 449 GLY B CA    1 
ATOM   7467  C  C     . GLY B 1 449 ? 163.633 109.378 130.375 1.00 13783. ? 449 GLY B C     1 
ATOM   7468  O  O     . GLY B 1 449 ? 163.134 109.093 129.285 1.00 13789. ? 449 GLY B O     1 
ATOM   7469  N  N     . GLU B 1 450 ? 164.800 108.874 130.775 1.00 14822. ? 450 GLU B N     1 
ATOM   7470  C  CA    . GLU B 1 450 ? 165.549 107.983 129.901 1.00 14858. ? 450 GLU B CA    1 
ATOM   7471  C  C     . GLU B 1 450 ? 165.028 106.552 129.937 1.00 14853. ? 450 GLU B C     1 
ATOM   7472  O  O     . GLU B 1 450 ? 165.209 105.812 128.964 1.00 14872. ? 450 GLU B O     1 
ATOM   7473  C  CB    . GLU B 1 450 ? 167.030 108.008 130.277 1.00 14881. ? 450 GLU B CB    1 
ATOM   7474  C  CG    . GLU B 1 450 ? 167.957 107.595 129.153 1.00 14903. ? 450 GLU B CG    1 
ATOM   7475  C  CD    . GLU B 1 450 ? 168.377 106.145 129.254 1.00 14904. ? 450 GLU B CD    1 
ATOM   7476  O  OE1   . GLU B 1 450 ? 169.085 105.799 130.222 1.00 14917. ? 450 GLU B OE1   1 
ATOM   7477  O  OE2   . GLU B 1 450 ? 168.000 105.352 128.367 1.00 14900. ? 450 GLU B OE2   1 
ATOM   7478  N  N     . PHE B 1 451 ? 164.385 106.141 131.028 1.00 14535. ? 451 PHE B N     1 
ATOM   7479  C  CA    . PHE B 1 451 ? 163.992 104.748 131.193 1.00 14534. ? 451 PHE B CA    1 
ATOM   7480  C  C     . PHE B 1 451 ? 162.493 104.520 131.299 1.00 14514. ? 451 PHE B C     1 
ATOM   7481  O  O     . PHE B 1 451 ? 162.014 103.484 130.835 1.00 14525. ? 451 PHE B O     1 
ATOM   7482  C  CB    . PHE B 1 451 ? 164.662 104.152 132.440 1.00 14550. ? 451 PHE B CB    1 
ATOM   7483  C  CG    . PHE B 1 451 ? 166.013 103.563 132.175 1.00 14562. ? 451 PHE B CG    1 
ATOM   7484  C  CD1   . PHE B 1 451 ? 166.139 102.370 131.487 1.00 14570. ? 451 PHE B CD1   1 
ATOM   7485  C  CD2   . PHE B 1 451 ? 167.158 104.203 132.612 1.00 14561. ? 451 PHE B CD2   1 
ATOM   7486  C  CE1   . PHE B 1 451 ? 167.382 101.826 131.240 1.00 14571. ? 451 PHE B CE1   1 
ATOM   7487  C  CE2   . PHE B 1 451 ? 168.403 103.663 132.369 1.00 14578. ? 451 PHE B CE2   1 
ATOM   7488  C  CZ    . PHE B 1 451 ? 168.516 102.473 131.682 1.00 14581. ? 451 PHE B CZ    1 
ATOM   7489  N  N     . LEU B 1 452 ? 161.741 105.444 131.893 1.00 13506. ? 452 LEU B N     1 
ATOM   7490  C  CA    . LEU B 1 452 ? 160.330 105.199 132.165 1.00 13470. ? 452 LEU B CA    1 
ATOM   7491  C  C     . LEU B 1 452 ? 159.418 105.741 131.070 1.00 13490. ? 452 LEU B C     1 
ATOM   7492  O  O     . LEU B 1 452 ? 158.534 105.028 130.588 1.00 13504. ? 452 LEU B O     1 
ATOM   7493  C  CB    . LEU B 1 452 ? 159.943 105.810 133.515 1.00 13450. ? 452 LEU B CB    1 
ATOM   7494  C  CG    . LEU B 1 452 ? 160.036 104.892 134.733 1.00 13463. ? 452 LEU B CG    1 
ATOM   7495  C  CD1   . LEU B 1 452 ? 159.246 105.472 135.890 1.00 13453. ? 452 LEU B CD1   1 
ATOM   7496  C  CD2   . LEU B 1 452 ? 159.543 103.502 134.388 1.00 13482. ? 452 LEU B CD2   1 
ATOM   7497  N  N     . GLU B 1 453 ? 159.617 106.994 130.668 1.00 13972. ? 453 GLU B N     1 
ATOM   7498  C  CA    . GLU B 1 453 ? 158.702 107.642 129.739 1.00 13974. ? 453 GLU B CA    1 
ATOM   7499  C  C     . GLU B 1 453 ? 158.908 107.216 128.293 1.00 13978. ? 453 GLU B C     1 
ATOM   7500  O  O     . GLU B 1 453 ? 158.084 107.565 127.443 1.00 13981. ? 453 GLU B O     1 
ATOM   7501  C  CB    . GLU B 1 453 ? 158.838 109.161 129.847 1.00 13965. ? 453 GLU B CB    1 
ATOM   7502  C  CG    . GLU B 1 453 ? 158.940 109.667 131.274 1.00 13963. ? 453 GLU B CG    1 
ATOM   7503  C  CD    . GLU B 1 453 ? 159.587 111.036 131.362 1.00 13977. ? 453 GLU B CD    1 
ATOM   7504  O  OE1   . GLU B 1 453 ? 159.855 111.638 130.302 1.00 13986. ? 453 GLU B OE1   1 
ATOM   7505  O  OE2   . GLU B 1 453 ? 159.830 111.510 132.492 1.00 13977. ? 453 GLU B OE2   1 
ATOM   7506  N  N     . VAL B 1 454 ? 159.977 106.473 127.988 1.00 14018. ? 454 VAL B N     1 
ATOM   7507  C  CA    . VAL B 1 454 ? 160.231 106.055 126.610 1.00 14016. ? 454 VAL B CA    1 
ATOM   7508  C  C     . VAL B 1 454 ? 159.403 104.852 126.196 1.00 14031. ? 454 VAL B C     1 
ATOM   7509  O  O     . VAL B 1 454 ? 159.477 104.437 125.032 1.00 14027. ? 454 VAL B O     1 
ATOM   7510  C  CB    . VAL B 1 454 ? 161.721 105.731 126.387 1.00 14023. ? 454 VAL B CB    1 
ATOM   7511  C  CG1   . VAL B 1 454 ? 162.542 107.009 126.378 1.00 14028. ? 454 VAL B CG1   1 
ATOM   7512  C  CG2   . VAL B 1 454 ? 162.220 104.773 127.453 1.00 14036. ? 454 VAL B CG2   1 
ATOM   7513  N  N     . THR B 1 455 ? 158.620 104.275 127.106 1.00 14618. ? 455 THR B N     1 
ATOM   7514  C  CA    . THR B 1 455 ? 157.748 103.156 126.776 1.00 14637. ? 455 THR B CA    1 
ATOM   7515  C  C     . THR B 1 455 ? 156.277 103.475 127.011 1.00 14627. ? 455 THR B C     1 
ATOM   7516  O  O     . THR B 1 455 ? 155.433 102.580 126.894 1.00 14635. ? 455 THR B O     1 
ATOM   7517  C  CB    . THR B 1 455 ? 158.143 101.910 127.574 1.00 14658. ? 455 THR B CB    1 
ATOM   7518  O  OG1   . THR B 1 455 ? 157.116 100.918 127.451 1.00 14670. ? 455 THR B OG1   1 
ATOM   7519  C  CG2   . THR B 1 455 ? 158.331 102.254 129.039 1.00 14652. ? 455 THR B CG2   1 
ATOM   7520  N  N     . CYS B 1 456 ? 155.947 104.725 127.336 1.00 14006. ? 456 CYS B N     1 
ATOM   7521  C  CA    . CYS B 1 456 ? 154.565 105.132 127.572 1.00 13975. ? 456 CYS B CA    1 
ATOM   7522  C  C     . CYS B 1 456 ? 154.006 105.715 126.277 1.00 13939. ? 456 CYS B C     1 
ATOM   7523  O  O     . CYS B 1 456 ? 153.876 106.927 126.109 1.00 13937. ? 456 CYS B O     1 
ATOM   7524  C  CB    . CYS B 1 456 ? 154.484 106.129 128.724 1.00 13966. ? 456 CYS B CB    1 
ATOM   7525  S  SG    . CYS B 1 456 ? 155.150 105.520 130.287 1.00 13964. ? 456 CYS B SG    1 
ATOM   7526  N  N     . ILE B 1 457 ? 153.674 104.823 125.346 1.00 12806. ? 457 ILE B N     1 
ATOM   7527  C  CA    . ILE B 1 457 ? 153.034 105.245 124.104 1.00 12766. ? 457 ILE B CA    1 
ATOM   7528  C  C     . ILE B 1 457 ? 151.565 105.560 124.346 1.00 12755. ? 457 ILE B C     1 
ATOM   7529  O  O     . ILE B 1 457 ? 151.114 106.695 124.156 1.00 12758. ? 457 ILE B O     1 
ATOM   7530  C  CB    . ILE B 1 457 ? 153.205 104.168 123.018 1.00 12742. ? 457 ILE B CB    1 
ATOM   7531  C  CG1   . ILE B 1 457 ? 154.668 103.736 122.924 1.00 12762. ? 457 ILE B CG1   1 
ATOM   7532  C  CG2   . ILE B 1 457 ? 152.689 104.675 121.682 1.00 12759. ? 457 ILE B CG2   1 
ATOM   7533  C  CD1   . ILE B 1 457 ? 155.495 104.572 121.980 1.00 12775. ? 457 ILE B CD1   1 
ATOM   7534  N  N     . ASN B 1 458 ? 150.800 104.558 124.772 1.00 12749. ? 458 ASN B N     1 
ATOM   7535  C  CA    . ASN B 1 458 ? 149.437 104.786 125.204 1.00 12742. ? 458 ASN B CA    1 
ATOM   7536  C  C     . ASN B 1 458 ? 149.445 105.578 126.507 1.00 12744. ? 458 ASN B C     1 
ATOM   7537  O  O     . ASN B 1 458 ? 150.430 105.554 127.247 1.00 12765. ? 458 ASN B O     1 
ATOM   7538  C  CB    . ASN B 1 458 ? 148.710 103.458 125.396 1.00 12735. ? 458 ASN B CB    1 
ATOM   7539  C  CG    . ASN B 1 458 ? 148.751 102.590 124.160 1.00 12735. ? 458 ASN B CG    1 
ATOM   7540  O  OD1   . ASN B 1 458 ? 149.645 102.720 123.327 1.00 12741. ? 458 ASN B OD1   1 
ATOM   7541  N  ND2   . ASN B 1 458 ? 147.781 101.695 124.034 1.00 12743. ? 458 ASN B ND2   1 
ATOM   7542  N  N     . PRO B 1 459 ? 148.368 106.306 126.801 1.00 12732. ? 459 PRO B N     1 
ATOM   7543  C  CA    . PRO B 1 459 ? 148.334 107.088 128.043 1.00 12738. ? 459 PRO B CA    1 
ATOM   7544  C  C     . PRO B 1 459 ? 148.565 106.200 129.256 1.00 12745. ? 459 PRO B C     1 
ATOM   7545  O  O     . PRO B 1 459 ? 148.004 105.108 129.365 1.00 12769. ? 459 PRO B O     1 
ATOM   7546  C  CB    . PRO B 1 459 ? 146.929 107.703 128.041 1.00 12743. ? 459 PRO B CB    1 
ATOM   7547  C  CG    . PRO B 1 459 ? 146.164 106.948 127.009 1.00 12746. ? 459 PRO B CG    1 
ATOM   7548  C  CD    . PRO B 1 459 ? 147.157 106.512 125.994 1.00 12748. ? 459 PRO B CD    1 
ATOM   7549  N  N     . THR B 1 460 ? 149.407 106.679 130.168 1.00 12735. ? 460 THR B N     1 
ATOM   7550  C  CA    . THR B 1 460 ? 149.845 105.886 131.305 1.00 12732. ? 460 THR B CA    1 
ATOM   7551  C  C     . THR B 1 460 ? 150.054 106.808 132.495 1.00 12742. ? 460 THR B C     1 
ATOM   7552  O  O     . THR B 1 460 ? 150.468 107.956 132.330 1.00 12760. ? 460 THR B O     1 
ATOM   7553  C  CB    . THR B 1 460 ? 151.139 105.129 130.981 1.00 12750. ? 460 THR B CB    1 
ATOM   7554  O  OG1   . THR B 1 460 ? 150.958 104.366 129.782 1.00 12763. ? 460 THR B OG1   1 
ATOM   7555  C  CG2   . THR B 1 460 ? 151.519 104.190 132.110 1.00 12762. ? 460 THR B CG2   1 
ATOM   7556  N  N     . PHE B 1 461 ? 149.766 106.302 133.689 1.00 12741. ? 461 PHE B N     1 
ATOM   7557  C  CA    . PHE B 1 461 ? 149.950 107.056 134.921 1.00 12742. ? 461 PHE B CA    1 
ATOM   7558  C  C     . PHE B 1 461 ? 151.243 106.612 135.590 1.00 12746. ? 461 PHE B C     1 
ATOM   7559  O  O     . PHE B 1 461 ? 151.432 105.421 135.857 1.00 12756. ? 461 PHE B O     1 
ATOM   7560  C  CB    . PHE B 1 461 ? 148.770 106.853 135.869 1.00 12750. ? 461 PHE B CB    1 
ATOM   7561  C  CG    . PHE B 1 461 ? 147.506 107.516 135.418 1.00 12731. ? 461 PHE B CG    1 
ATOM   7562  C  CD1   . PHE B 1 461 ? 147.433 108.889 135.302 1.00 12731. ? 461 PHE B CD1   1 
ATOM   7563  C  CD2   . PHE B 1 461 ? 146.387 106.764 135.117 1.00 12745. ? 461 PHE B CD2   1 
ATOM   7564  C  CE1   . PHE B 1 461 ? 146.270 109.499 134.893 1.00 12739. ? 461 PHE B CE1   1 
ATOM   7565  C  CE2   . PHE B 1 461 ? 145.224 107.370 134.708 1.00 12746. ? 461 PHE B CE2   1 
ATOM   7566  C  CZ    . PHE B 1 461 ? 145.166 108.739 134.596 1.00 12746. ? 461 PHE B CZ    1 
ATOM   7567  N  N     . ILE B 1 462 ? 152.127 107.567 135.856 1.00 12741. ? 462 ILE B N     1 
ATOM   7568  C  CA    . ILE B 1 462 ? 153.336 107.335 136.637 1.00 12734. ? 462 ILE B CA    1 
ATOM   7569  C  C     . ILE B 1 462 ? 153.134 108.043 137.967 1.00 12744. ? 462 ILE B C     1 
ATOM   7570  O  O     . ILE B 1 462 ? 153.093 109.276 138.017 1.00 12761. ? 462 ILE B O     1 
ATOM   7571  C  CB    . ILE B 1 462 ? 154.591 107.844 135.917 1.00 12727. ? 462 ILE B CB    1 
ATOM   7572  C  CG1   . ILE B 1 462 ? 154.624 107.327 134.480 1.00 12742. ? 462 ILE B CG1   1 
ATOM   7573  C  CG2   . ILE B 1 462 ? 155.836 107.407 136.659 1.00 12747. ? 462 ILE B CG2   1 
ATOM   7574  C  CD1   . ILE B 1 462 ? 155.917 107.615 133.760 1.00 12758. ? 462 ILE B CD1   1 
ATOM   7575  N  N     . CYS B 1 463 ? 152.999 107.277 139.042 1.00 12747. ? 463 CYS B N     1 
ATOM   7576  C  CA    . CYS B 1 463 ? 152.573 107.822 140.322 1.00 12744. ? 463 CYS B CA    1 
ATOM   7577  C  C     . CYS B 1 463 ? 153.600 107.520 141.409 1.00 12745. ? 463 CYS B C     1 
ATOM   7578  O  O     . CYS B 1 463 ? 154.613 106.857 141.177 1.00 12766. ? 463 CYS B O     1 
ATOM   7579  C  CB    . CYS B 1 463 ? 151.195 107.276 140.710 1.00 12753. ? 463 CYS B CB    1 
ATOM   7580  S  SG    . CYS B 1 463 ? 151.073 105.478 140.741 1.00 12743. ? 463 CYS B SG    1 
ATOM   7581  N  N     . ASP B 1 464 ? 153.317 108.032 142.608 1.00 12740. ? 464 ASP B N     1 
ATOM   7582  C  CA    . ASP B 1 464 ? 154.147 107.832 143.795 1.00 12741. ? 464 ASP B CA    1 
ATOM   7583  C  C     . ASP B 1 464 ? 155.568 108.353 143.573 1.00 12741. ? 464 ASP B C     1 
ATOM   7584  O  O     . ASP B 1 464 ? 156.545 107.603 143.571 1.00 12757. ? 464 ASP B O     1 
ATOM   7585  C  CB    . ASP B 1 464 ? 154.154 106.359 144.214 1.00 12759. ? 464 ASP B CB    1 
ATOM   7586  C  CG    . ASP B 1 464 ? 152.773 105.850 144.568 1.00 12753. ? 464 ASP B CG    1 
ATOM   7587  O  OD1   . ASP B 1 464 ? 151.804 106.627 144.450 1.00 12748. ? 464 ASP B OD1   1 
ATOM   7588  O  OD2   . ASP B 1 464 ? 152.655 104.674 144.970 1.00 12763. ? 464 ASP B OD2   1 
ATOM   7589  N  N     . HIS B 1 465 ? 155.664 109.665 143.379 1.00 12743. ? 465 HIS B N     1 
ATOM   7590  C  CA    . HIS B 1 465 ? 156.962 110.295 143.215 1.00 12749. ? 465 HIS B CA    1 
ATOM   7591  C  C     . HIS B 1 465 ? 157.591 110.571 144.579 1.00 12755. ? 465 HIS B C     1 
ATOM   7592  O  O     . HIS B 1 465 ? 156.881 110.771 145.567 1.00 12780. ? 465 HIS B O     1 
ATOM   7593  C  CB    . HIS B 1 465 ? 156.841 111.610 142.450 1.00 12756. ? 465 HIS B CB    1 
ATOM   7594  C  CG    . HIS B 1 465 ? 156.137 111.502 141.132 1.00 12739. ? 465 HIS B CG    1 
ATOM   7595  N  ND1   . HIS B 1 465 ? 156.306 112.430 140.129 1.00 12736. ? 465 HIS B ND1   1 
ATOM   7596  C  CD2   . HIS B 1 465 ? 155.223 110.615 140.671 1.00 12749. ? 465 HIS B CD2   1 
ATOM   7597  C  CE1   . HIS B 1 465 ? 155.557 112.100 139.093 1.00 12744. ? 465 HIS B CE1   1 
ATOM   7598  N  NE2   . HIS B 1 465 ? 154.890 111.002 139.396 1.00 12758. ? 465 HIS B NE2   1 
ATOM   7599  N  N     . PRO B 1 466 ? 158.917 110.591 144.659 1.00 12734. ? 466 PRO B N     1 
ATOM   7600  C  CA    . PRO B 1 466 ? 159.573 111.002 145.903 1.00 12735. ? 466 PRO B CA    1 
ATOM   7601  C  C     . PRO B 1 466 ? 159.316 112.471 146.198 1.00 12741. ? 466 PRO B C     1 
ATOM   7602  O  O     . PRO B 1 466 ? 159.099 113.286 145.300 1.00 12761. ? 466 PRO B O     1 
ATOM   7603  C  CB    . PRO B 1 466 ? 161.057 110.742 145.629 1.00 12761. ? 466 PRO B CB    1 
ATOM   7604  C  CG    . PRO B 1 466 ? 161.073 109.777 144.492 1.00 12771. ? 466 PRO B CG    1 
ATOM   7605  C  CD    . PRO B 1 466 ? 159.884 110.115 143.660 1.00 12745. ? 466 PRO B CD    1 
ATOM   7606  N  N     . GLN B 1 467 ? 159.340 112.807 147.487 1.00 12732. ? 467 GLN B N     1 
ATOM   7607  C  CA    . GLN B 1 467 ? 159.061 114.178 147.897 1.00 12743. ? 467 GLN B CA    1 
ATOM   7608  C  C     . GLN B 1 467 ? 160.168 115.153 147.520 1.00 12754. ? 467 GLN B C     1 
ATOM   7609  O  O     . GLN B 1 467 ? 159.930 116.366 147.527 1.00 12754. ? 467 GLN B O     1 
ATOM   7610  C  CB    . GLN B 1 467 ? 158.811 114.246 149.405 1.00 12757. ? 467 GLN B CB    1 
ATOM   7611  C  CG    . GLN B 1 467 ? 158.058 115.495 149.836 1.00 12751. ? 467 GLN B CG    1 
ATOM   7612  C  CD    . GLN B 1 467 ? 156.985 115.211 150.859 1.00 12747. ? 467 GLN B CD    1 
ATOM   7613  O  OE1   . GLN B 1 467 ? 156.942 114.131 151.446 1.00 12747. ? 467 GLN B OE1   1 
ATOM   7614  N  NE2   . GLN B 1 467 ? 156.103 116.179 151.073 1.00 12744. ? 467 GLN B NE2   1 
ATOM   7615  N  N     . ILE B 1 468 ? 161.366 114.666 147.192 1.00 12774. ? 468 ILE B N     1 
ATOM   7616  C  CA    . ILE B 1 468 ? 162.401 115.557 146.689 1.00 12773. ? 468 ILE B CA    1 
ATOM   7617  C  C     . ILE B 1 468 ? 162.029 116.128 145.330 1.00 12779. ? 468 ILE B C     1 
ATOM   7618  O  O     . ILE B 1 468 ? 162.538 117.185 144.943 1.00 12776. ? 468 ILE B O     1 
ATOM   7619  C  CB    . ILE B 1 468 ? 163.753 114.827 146.618 1.00 12774. ? 468 ILE B CB    1 
ATOM   7620  C  CG1   . ILE B 1 468 ? 163.623 113.554 145.783 1.00 12796. ? 468 ILE B CG1   1 
ATOM   7621  C  CG2   . ILE B 1 468 ? 164.248 114.501 148.010 1.00 12844. ? 468 ILE B CG2   1 
ATOM   7622  C  CD1   . ILE B 1 468 ? 164.819 112.644 145.874 1.00 12839. ? 468 ILE B CD1   1 
ATOM   7623  N  N     . MET B 1 469 ? 161.150 115.452 144.592 1.00 13149. ? 469 MET B N     1 
ATOM   7624  C  CA    . MET B 1 469 ? 160.707 115.905 143.282 1.00 13157. ? 469 MET B CA    1 
ATOM   7625  C  C     . MET B 1 469 ? 159.399 116.678 143.328 1.00 13158. ? 469 MET B C     1 
ATOM   7626  O  O     . MET B 1 469 ? 158.957 117.178 142.289 1.00 13173. ? 469 MET B O     1 
ATOM   7627  C  CB    . MET B 1 469 ? 160.562 114.708 142.337 1.00 13162. ? 469 MET B CB    1 
ATOM   7628  C  CG    . MET B 1 469 ? 161.614 113.636 142.538 1.00 13172. ? 469 MET B CG    1 
ATOM   7629  S  SD    . MET B 1 469 ? 161.570 112.387 141.245 1.00 13168. ? 469 MET B SD    1 
ATOM   7630  C  CE    . MET B 1 469 ? 161.505 113.423 139.790 1.00 13202. ? 469 MET B CE    1 
ATOM   7631  N  N     . SER B 1 470 ? 158.771 116.796 144.493 1.00 12763. ? 470 SER B N     1 
ATOM   7632  C  CA    . SER B 1 470 ? 157.483 117.479 144.619 1.00 12752. ? 470 SER B CA    1 
ATOM   7633  C  C     . SER B 1 470 ? 157.425 118.149 145.981 1.00 12738. ? 470 SER B C     1 
ATOM   7634  O  O     . SER B 1 470 ? 157.115 117.501 146.992 1.00 12752. ? 470 SER B O     1 
ATOM   7635  C  CB    . SER B 1 470 ? 156.316 116.514 144.434 1.00 12768. ? 470 SER B CB    1 
ATOM   7636  O  OG    . SER B 1 470 ? 156.299 115.537 145.458 1.00 12765. ? 470 SER B OG    1 
ATOM   7637  N  N     . PRO B 1 471 ? 157.716 119.446 146.055 1.00 12728. ? 471 PRO B N     1 
ATOM   7638  C  CA    . PRO B 1 471 ? 157.688 120.157 147.338 1.00 12739. ? 471 PRO B CA    1 
ATOM   7639  C  C     . PRO B 1 471 ? 156.327 120.700 147.742 1.00 12740. ? 471 PRO B C     1 
ATOM   7640  O  O     . PRO B 1 471 ? 156.252 121.444 148.726 1.00 12744. ? 471 PRO B O     1 
ATOM   7641  C  CB    . PRO B 1 471 ? 158.671 121.307 147.088 1.00 12776. ? 471 PRO B CB    1 
ATOM   7642  C  CG    . PRO B 1 471 ? 158.504 121.609 145.645 1.00 12790. ? 471 PRO B CG    1 
ATOM   7643  C  CD    . PRO B 1 471 ? 158.170 120.311 144.953 1.00 12757. ? 471 PRO B CD    1 
ATOM   7644  N  N     . LEU B 1 472 ? 155.260 120.360 147.020 1.00 12732. ? 472 LEU B N     1 
ATOM   7645  C  CA    . LEU B 1 472 ? 153.925 120.842 147.349 1.00 12726. ? 472 LEU B CA    1 
ATOM   7646  C  C     . LEU B 1 472 ? 152.903 119.717 147.436 1.00 12729. ? 472 LEU B C     1 
ATOM   7647  O  O     . LEU B 1 472 ? 151.710 119.994 147.604 1.00 12746. ? 472 LEU B O     1 
ATOM   7648  C  CB    . LEU B 1 472 ? 153.465 121.883 146.323 1.00 12743. ? 472 LEU B CB    1 
ATOM   7649  C  CG    . LEU B 1 472 ? 154.080 123.277 146.443 1.00 12766. ? 472 LEU B CG    1 
ATOM   7650  C  CD1   . LEU B 1 472 ? 154.070 123.979 145.100 1.00 12781. ? 472 LEU B CD1   1 
ATOM   7651  C  CD2   . LEU B 1 472 ? 153.339 124.101 147.477 1.00 12767. ? 472 LEU B CD2   1 
ATOM   7652  N  N     . ALA B 1 473 ? 153.331 118.464 147.333 1.00 12725. ? 473 ALA B N     1 
ATOM   7653  C  CA    . ALA B 1 473 ? 152.432 117.322 147.367 1.00 12726. ? 473 ALA B CA    1 
ATOM   7654  C  C     . ALA B 1 473 ? 152.449 116.673 148.744 1.00 12728. ? 473 ALA B C     1 
ATOM   7655  O  O     . ALA B 1 473 ? 153.474 116.649 149.429 1.00 12748. ? 473 ALA B O     1 
ATOM   7656  C  CB    . ALA B 1 473 ? 152.819 116.293 146.304 1.00 12749. ? 473 ALA B CB    1 
ATOM   7657  N  N     . LYS B 1 474 ? 151.297 116.147 149.144 1.00 12730. ? 474 LYS B N     1 
ATOM   7658  C  CA    . LYS B 1 474 ? 151.170 115.515 150.445 1.00 12729. ? 474 LYS B CA    1 
ATOM   7659  C  C     . LYS B 1 474 ? 151.867 114.161 150.454 1.00 12731. ? 474 LYS B C     1 
ATOM   7660  O  O     . LYS B 1 474 ? 151.939 113.468 149.437 1.00 12742. ? 474 LYS B O     1 
ATOM   7661  C  CB    . LYS B 1 474 ? 149.700 115.348 150.821 1.00 12743. ? 474 LYS B CB    1 
ATOM   7662  C  CG    . LYS B 1 474 ? 149.423 115.528 152.297 1.00 12744. ? 474 LYS B CG    1 
ATOM   7663  C  CD    . LYS B 1 474 ? 147.938 115.560 152.578 1.00 12743. ? 474 LYS B CD    1 
ATOM   7664  C  CE    . LYS B 1 474 ? 147.660 115.418 154.059 1.00 12741. ? 474 LYS B CE    1 
ATOM   7665  N  NZ    . LYS B 1 474 ? 146.302 115.912 154.399 1.00 12741. ? 474 LYS B NZ    1 
ATOM   7666  N  N     . TRP B 1 475 ? 152.385 113.792 151.621 1.00 12741. ? 475 TRP B N     1 
ATOM   7667  C  CA    . TRP B 1 475 ? 153.111 112.541 151.760 1.00 12733. ? 475 TRP B CA    1 
ATOM   7668  C  C     . TRP B 1 475 ? 152.179 111.351 151.568 1.00 12738. ? 475 TRP B C     1 
ATOM   7669  O  O     . TRP B 1 475 ? 150.986 111.410 151.871 1.00 12762. ? 475 TRP B O     1 
ATOM   7670  C  CB    . TRP B 1 475 ? 153.785 112.467 153.130 1.00 12739. ? 475 TRP B CB    1 
ATOM   7671  C  CG    . TRP B 1 475 ? 152.825 112.402 154.277 1.00 12738. ? 475 TRP B CG    1 
ATOM   7672  C  CD1   . TRP B 1 475 ? 152.448 111.288 154.965 1.00 12750. ? 475 TRP B CD1   1 
ATOM   7673  C  CD2   . TRP B 1 475 ? 152.121 113.498 154.871 1.00 12734. ? 475 TRP B CD2   1 
ATOM   7674  N  NE1   . TRP B 1 475 ? 151.552 111.621 155.949 1.00 12752. ? 475 TRP B NE1   1 
ATOM   7675  C  CE2   . TRP B 1 475 ? 151.335 112.972 155.912 1.00 12744. ? 475 TRP B CE2   1 
ATOM   7676  C  CE3   . TRP B 1 475 ? 152.079 114.871 154.624 1.00 12746. ? 475 TRP B CE3   1 
ATOM   7677  C  CZ2   . TRP B 1 475 ? 150.517 113.771 156.704 1.00 12752. ? 475 TRP B CZ2   1 
ATOM   7678  C  CZ3   . TRP B 1 475 ? 151.267 115.661 155.410 1.00 12741. ? 475 TRP B CZ3   1 
ATOM   7679  C  CH2   . TRP B 1 475 ? 150.497 115.110 156.437 1.00 12739. ? 475 TRP B CH2   1 
ATOM   7680  N  N     . HIS B 1 476 ? 152.738 110.264 151.047 1.00 12743. ? 476 HIS B N     1 
ATOM   7681  C  CA    . HIS B 1 476 ? 151.961 109.057 150.818 1.00 12749. ? 476 HIS B CA    1 
ATOM   7682  C  C     . HIS B 1 476 ? 151.523 108.438 152.139 1.00 12740. ? 476 HIS B C     1 
ATOM   7683  O  O     . HIS B 1 476 ? 152.205 108.550 153.161 1.00 12751. ? 476 HIS B O     1 
ATOM   7684  C  CB    . HIS B 1 476 ? 152.775 108.048 150.012 1.00 12757. ? 476 HIS B CB    1 
ATOM   7685  C  CG    . HIS B 1 476 ? 151.940 107.034 149.295 1.00 12736. ? 476 HIS B CG    1 
ATOM   7686  N  ND1   . HIS B 1 476 ? 152.358 105.738 149.091 1.00 12742. ? 476 HIS B ND1   1 
ATOM   7687  C  CD2   . HIS B 1 476 ? 150.714 107.127 148.731 1.00 12733. ? 476 HIS B CD2   1 
ATOM   7688  C  CE1   . HIS B 1 476 ? 151.424 105.074 148.436 1.00 12744. ? 476 HIS B CE1   1 
ATOM   7689  N  NE2   . HIS B 1 476 ? 150.416 105.894 148.206 1.00 12731. ? 476 HIS B NE2   1 
ATOM   7690  N  N     . ARG B 1 477 ? 150.363 107.782 152.110 1.00 12728. ? 477 ARG B N     1 
ATOM   7691  C  CA    . ARG B 1 477 ? 149.813 107.192 153.326 1.00 12731. ? 477 ARG B CA    1 
ATOM   7692  C  C     . ARG B 1 477 ? 150.665 106.030 153.820 1.00 12736. ? 477 ARG B C     1 
ATOM   7693  O  O     . ARG B 1 477 ? 151.020 105.967 155.002 1.00 12750. ? 477 ARG B O     1 
ATOM   7694  C  CB    . ARG B 1 477 ? 148.380 106.723 153.081 1.00 12742. ? 477 ARG B CB    1 
ATOM   7695  C  CG    . ARG B 1 477 ? 147.485 107.748 152.430 1.00 12750. ? 477 ARG B CG    1 
ATOM   7696  C  CD    . ARG B 1 477 ? 146.264 107.083 151.825 1.00 12750. ? 477 ARG B CD    1 
ATOM   7697  N  NE    . ARG B 1 477 ? 145.819 107.762 150.615 1.00 12741. ? 477 ARG B NE    1 
ATOM   7698  C  CZ    . ARG B 1 477 ? 144.640 108.351 150.481 1.00 12741. ? 477 ARG B CZ    1 
ATOM   7699  N  NH1   . ARG B 1 477 ? 143.754 108.353 151.462 1.00 12751. ? 477 ARG B NH1   1 
ATOM   7700  N  NH2   . ARG B 1 477 ? 144.342 108.952 149.333 1.00 12748. ? 477 ARG B NH2   1 
ATOM   7701  N  N     . SER B 1 478 ? 151.004 105.100 152.931 1.00 12736. ? 478 SER B N     1 
ATOM   7702  C  CA    . SER B 1 478 ? 151.632 103.849 153.336 1.00 12742. ? 478 SER B CA    1 
ATOM   7703  C  C     . SER B 1 478 ? 153.127 103.794 153.068 1.00 12745. ? 478 SER B C     1 
ATOM   7704  O  O     . SER B 1 478 ? 153.852 103.138 153.822 1.00 12747. ? 478 SER B O     1 
ATOM   7705  C  CB    . SER B 1 478 ? 150.956 102.668 152.632 1.00 12745. ? 478 SER B CB    1 
ATOM   7706  O  OG    . SER B 1 478 ? 150.510 103.036 151.339 1.00 12748. ? 478 SER B OG    1 
ATOM   7707  N  N     . LYS B 1 479 ? 153.611 104.457 152.023 1.00 12749. ? 479 LYS B N     1 
ATOM   7708  C  CA    . LYS B 1 479 ? 155.019 104.408 151.657 1.00 12755. ? 479 LYS B CA    1 
ATOM   7709  C  C     . LYS B 1 479 ? 155.710 105.689 152.100 1.00 12784. ? 479 LYS B C     1 
ATOM   7710  O  O     . LYS B 1 479 ? 155.285 106.789 151.731 1.00 12789. ? 479 LYS B O     1 
ATOM   7711  C  CB    . LYS B 1 479 ? 155.181 104.209 150.151 1.00 12753. ? 479 LYS B CB    1 
ATOM   7712  C  CG    . LYS B 1 479 ? 154.296 103.118 149.578 1.00 12754. ? 479 LYS B CG    1 
ATOM   7713  C  CD    . LYS B 1 479 ? 154.367 103.094 148.064 1.00 12751. ? 479 LYS B CD    1 
ATOM   7714  C  CE    . LYS B 1 479 ? 153.313 102.174 147.477 1.00 12756. ? 479 LYS B CE    1 
ATOM   7715  N  NZ    . LYS B 1 479 ? 153.292 102.243 145.991 1.00 12768. ? 479 LYS B NZ    1 
ATOM   7716  N  N     . GLU B 1 480 ? 156.770 105.543 152.887 1.00 13789. ? 480 GLU B N     1 
ATOM   7717  C  CA    . GLU B 1 480 ? 157.508 106.691 153.387 1.00 13798. ? 480 GLU B CA    1 
ATOM   7718  C  C     . GLU B 1 480 ? 158.436 107.246 152.316 1.00 13788. ? 480 GLU B C     1 
ATOM   7719  O  O     . GLU B 1 480 ? 159.014 106.506 151.517 1.00 13814. ? 480 GLU B O     1 
ATOM   7720  C  CB    . GLU B 1 480 ? 158.318 106.312 154.626 1.00 13825. ? 480 GLU B CB    1 
ATOM   7721  C  CG    . GLU B 1 480 ? 158.370 107.398 155.681 1.00 13828. ? 480 GLU B CG    1 
ATOM   7722  C  CD    . GLU B 1 480 ? 159.378 107.101 156.772 1.00 13847. ? 480 GLU B CD    1 
ATOM   7723  O  OE1   . GLU B 1 480 ? 159.434 105.942 157.232 1.00 13848. ? 480 GLU B OE1   1 
ATOM   7724  O  OE2   . GLU B 1 480 ? 160.116 108.028 157.168 1.00 13855. ? 480 GLU B OE2   1 
ATOM   7725  N  N     . GLY B 1 481 ? 158.573 108.570 152.306 1.00 12782. ? 481 GLY B N     1 
ATOM   7726  C  CA    . GLY B 1 481 ? 159.439 109.249 151.374 1.00 12778. ? 481 GLY B CA    1 
ATOM   7727  C  C     . GLY B 1 481 ? 158.822 109.543 150.025 1.00 12754. ? 481 GLY B C     1 
ATOM   7728  O  O     . GLY B 1 481 ? 159.442 110.240 149.216 1.00 12755. ? 481 GLY B O     1 
ATOM   7729  N  N     . LEU B 1 482 ? 157.623 109.038 149.759 1.00 12736. ? 482 LEU B N     1 
ATOM   7730  C  CA    . LEU B 1 482 ? 156.929 109.274 148.504 1.00 12736. ? 482 LEU B CA    1 
ATOM   7731  C  C     . LEU B 1 482 ? 155.766 110.231 148.720 1.00 12741. ? 482 LEU B C     1 
ATOM   7732  O  O     . LEU B 1 482 ? 155.317 110.457 149.845 1.00 12749. ? 482 LEU B O     1 
ATOM   7733  C  CB    . LEU B 1 482 ? 156.422 107.962 147.898 1.00 12739. ? 482 LEU B CB    1 
ATOM   7734  C  CG    . LEU B 1 482 ? 157.472 106.876 147.672 1.00 12757. ? 482 LEU B CG    1 
ATOM   7735  C  CD1   . LEU B 1 482 ? 156.830 105.624 147.111 1.00 12762. ? 482 LEU B CD1   1 
ATOM   7736  C  CD2   . LEU B 1 482 ? 158.567 107.373 146.750 1.00 12770. ? 482 LEU B CD2   1 
ATOM   7737  N  N     . THR B 1 483 ? 155.286 110.796 147.620 1.00 12739. ? 483 THR B N     1 
ATOM   7738  C  CA    . THR B 1 483 ? 154.165 111.720 147.636 1.00 12731. ? 483 THR B CA    1 
ATOM   7739  C  C     . THR B 1 483 ? 152.960 111.091 146.954 1.00 12737. ? 483 THR B C     1 
ATOM   7740  O  O     . THR B 1 483 ? 153.046 110.041 146.314 1.00 12741. ? 483 THR B O     1 
ATOM   7741  C  CB    . THR B 1 483 ? 154.527 113.038 146.947 1.00 12731. ? 483 THR B CB    1 
ATOM   7742  O  OG1   . THR B 1 483 ? 155.279 112.767 145.761 1.00 12739. ? 483 THR B OG1   1 
ATOM   7743  C  CG2   . THR B 1 483 ? 155.349 113.906 147.872 1.00 12756. ? 483 THR B CG2   1 
ATOM   7744  N  N     . GLU B 1 484 ? 151.818 111.755 147.111 1.00 12746. ? 484 GLU B N     1 
ATOM   7745  C  CA    . GLU B 1 484 ? 150.567 111.311 146.508 1.00 12744. ? 484 GLU B CA    1 
ATOM   7746  C  C     . GLU B 1 484 ? 150.337 112.128 145.242 1.00 12744. ? 484 GLU B C     1 
ATOM   7747  O  O     . GLU B 1 484 ? 149.562 113.081 145.216 1.00 12763. ? 484 GLU B O     1 
ATOM   7748  C  CB    . GLU B 1 484 ? 149.419 111.457 147.498 1.00 12751. ? 484 GLU B CB    1 
ATOM   7749  C  CG    . GLU B 1 484 ? 149.263 110.280 148.436 1.00 12754. ? 484 GLU B CG    1 
ATOM   7750  C  CD    . GLU B 1 484 ? 147.936 110.287 149.153 1.00 12747. ? 484 GLU B CD    1 
ATOM   7751  O  OE1   . GLU B 1 484 ? 147.309 111.364 149.230 1.00 12761. ? 484 GLU B OE1   1 
ATOM   7752  O  OE2   . GLU B 1 484 ? 147.514 109.217 149.633 1.00 12747. ? 484 GLU B OE2   1 
ATOM   7753  N  N     . ARG B 1 485 ? 151.032 111.742 144.175 1.00 12732. ? 485 ARG B N     1 
ATOM   7754  C  CA    . ARG B 1 485 ? 150.925 112.435 142.901 1.00 12729. ? 485 ARG B CA    1 
ATOM   7755  C  C     . ARG B 1 485 ? 151.022 111.436 141.762 1.00 12726. ? 485 ARG B C     1 
ATOM   7756  O  O     . ARG B 1 485 ? 151.426 110.286 141.943 1.00 12738. ? 485 ARG B O     1 
ATOM   7757  C  CB    . ARG B 1 485 ? 152.003 113.509 142.740 1.00 12737. ? 485 ARG B CB    1 
ATOM   7758  C  CG    . ARG B 1 485 ? 153.363 112.997 142.379 1.00 12750. ? 485 ARG B CG    1 
ATOM   7759  C  CD    . ARG B 1 485 ? 154.353 114.140 142.330 1.00 12751. ? 485 ARG B CD    1 
ATOM   7760  N  NE    . ARG B 1 485 ? 154.137 115.009 141.181 1.00 12730. ? 485 ARG B NE    1 
ATOM   7761  C  CZ    . ARG B 1 485 ? 155.078 115.766 140.633 1.00 12741. ? 485 ARG B CZ    1 
ATOM   7762  N  NH1   . ARG B 1 485 ? 156.311 115.787 141.108 1.00 12758. ? 485 ARG B NH1   1 
ATOM   7763  N  NH2   . ARG B 1 485 ? 154.774 116.520 139.582 1.00 12750. ? 485 ARG B NH2   1 
ATOM   7764  N  N     . PHE B 1 486 ? 150.635 111.895 140.574 1.00 12729. ? 486 PHE B N     1 
ATOM   7765  C  CA    . PHE B 1 486 ? 150.743 111.102 139.362 1.00 12732. ? 486 PHE B CA    1 
ATOM   7766  C  C     . PHE B 1 486 ? 150.932 112.036 138.178 1.00 12738. ? 486 PHE B C     1 
ATOM   7767  O  O     . PHE B 1 486 ? 150.581 113.216 138.227 1.00 12757. ? 486 PHE B O     1 
ATOM   7768  C  CB    . PHE B 1 486 ? 149.513 110.210 139.153 1.00 12746. ? 486 PHE B CB    1 
ATOM   7769  C  CG    . PHE B 1 486 ? 148.241 110.972 138.910 1.00 12757. ? 486 PHE B CG    1 
ATOM   7770  C  CD1   . PHE B 1 486 ? 147.439 111.358 139.966 1.00 12762. ? 486 PHE B CD1   1 
ATOM   7771  C  CD2   . PHE B 1 486 ? 147.840 111.290 137.625 1.00 12754. ? 486 PHE B CD2   1 
ATOM   7772  C  CE1   . PHE B 1 486 ? 146.271 112.054 139.746 1.00 12754. ? 486 PHE B CE1   1 
ATOM   7773  C  CE2   . PHE B 1 486 ? 146.673 111.986 137.401 1.00 12725. ? 486 PHE B CE2   1 
ATOM   7774  C  CZ    . PHE B 1 486 ? 145.888 112.365 138.461 1.00 12727. ? 486 PHE B CZ    1 
ATOM   7775  N  N     . GLU B 1 487 ? 151.501 111.487 137.113 1.00 12730. ? 487 GLU B N     1 
ATOM   7776  C  CA    . GLU B 1 487 ? 151.687 112.193 135.857 1.00 12732. ? 487 GLU B CA    1 
ATOM   7777  C  C     . GLU B 1 487 ? 151.134 111.341 134.728 1.00 12736. ? 487 GLU B C     1 
ATOM   7778  O  O     . GLU B 1 487 ? 151.339 110.124 134.702 1.00 12749. ? 487 GLU B O     1 
ATOM   7779  C  CB    . GLU B 1 487 ? 153.163 112.505 135.601 1.00 12746. ? 487 GLU B CB    1 
ATOM   7780  C  CG    . GLU B 1 487 ? 153.584 113.896 136.033 1.00 12750. ? 487 GLU B CG    1 
ATOM   7781  C  CD    . GLU B 1 487 ? 155.088 114.069 136.051 1.00 12754. ? 487 GLU B CD    1 
ATOM   7782  O  OE1   . GLU B 1 487 ? 155.804 113.048 136.087 1.00 12765. ? 487 GLU B OE1   1 
ATOM   7783  O  OE2   . GLU B 1 487 ? 155.555 115.226 136.028 1.00 12753. ? 487 GLU B OE2   1 
ATOM   7784  N  N     . LEU B 1 488 ? 150.430 111.983 133.801 1.00 12741. ? 488 LEU B N     1 
ATOM   7785  C  CA    . LEU B 1 488 ? 149.858 111.307 132.646 1.00 12740. ? 488 LEU B CA    1 
ATOM   7786  C  C     . LEU B 1 488 ? 150.803 111.468 131.465 1.00 12734. ? 488 LEU B C     1 
ATOM   7787  O  O     . LEU B 1 488 ? 151.129 112.595 131.071 1.00 12756. ? 488 LEU B O     1 
ATOM   7788  C  CB    . LEU B 1 488 ? 148.476 111.861 132.308 1.00 12745. ? 488 LEU B CB    1 
ATOM   7789  C  CG    . LEU B 1 488 ? 147.715 111.090 131.229 1.00 12738. ? 488 LEU B CG    1 
ATOM   7790  C  CD1   . LEU B 1 488 ? 147.660 109.610 131.560 1.00 12759. ? 488 LEU B CD1   1 
ATOM   7791  C  CD2   . LEU B 1 488 ? 146.321 111.652 131.055 1.00 12741. ? 488 LEU B CD2   1 
ATOM   7792  N  N     . PHE B 1 489 ? 151.250 110.343 130.915 1.00 12723. ? 489 PHE B N     1 
ATOM   7793  C  CA    . PHE B 1 489 ? 152.198 110.316 129.813 1.00 12729. ? 489 PHE B CA    1 
ATOM   7794  C  C     . PHE B 1 489 ? 151.537 109.661 128.613 1.00 12742. ? 489 PHE B C     1 
ATOM   7795  O  O     . PHE B 1 489 ? 151.125 108.498 128.683 1.00 12758. ? 489 PHE B O     1 
ATOM   7796  C  CB    . PHE B 1 489 ? 153.470 109.564 130.201 1.00 12745. ? 489 PHE B CB    1 
ATOM   7797  C  CG    . PHE B 1 489 ? 154.471 110.411 130.920 1.00 12751. ? 489 PHE B CG    1 
ATOM   7798  C  CD1   . PHE B 1 489 ? 155.423 111.123 130.219 1.00 12767. ? 489 PHE B CD1   1 
ATOM   7799  C  CD2   . PHE B 1 489 ? 154.451 110.506 132.298 1.00 12755. ? 489 PHE B CD2   1 
ATOM   7800  C  CE1   . PHE B 1 489 ? 156.339 111.907 130.878 1.00 12767. ? 489 PHE B CE1   1 
ATOM   7801  C  CE2   . PHE B 1 489 ? 155.366 111.288 132.962 1.00 12761. ? 489 PHE B CE2   1 
ATOM   7802  C  CZ    . PHE B 1 489 ? 156.312 111.989 132.252 1.00 12763. ? 489 PHE B CZ    1 
ATOM   7803  N  N     . VAL B 1 490 ? 151.436 110.408 127.523 1.00 12747. ? 490 VAL B N     1 
ATOM   7804  C  CA    . VAL B 1 490 ? 150.945 109.899 126.253 1.00 12752. ? 490 VAL B CA    1 
ATOM   7805  C  C     . VAL B 1 490 ? 151.961 110.270 125.185 1.00 12724. ? 490 VAL B C     1 
ATOM   7806  O  O     . VAL B 1 490 ? 152.525 111.370 125.209 1.00 12687. ? 490 VAL B O     1 
ATOM   7807  C  CB    . VAL B 1 490 ? 149.544 110.451 125.914 1.00 12720. ? 490 VAL B CB    1 
ATOM   7808  C  CG1   . VAL B 1 490 ? 149.564 111.962 125.835 1.00 12661. ? 490 VAL B CG1   1 
ATOM   7809  C  CG2   . VAL B 1 490 ? 149.037 109.857 124.617 1.00 12750. ? 490 VAL B CG2   1 
ATOM   7810  N  N     . MET B 1 491 ? 152.229 109.333 124.277 1.00 13162. ? 491 MET B N     1 
ATOM   7811  C  CA    . MET B 1 491 ? 153.203 109.538 123.207 1.00 13177. ? 491 MET B CA    1 
ATOM   7812  C  C     . MET B 1 491 ? 154.557 109.955 123.774 1.00 13173. ? 491 MET B C     1 
ATOM   7813  O  O     . MET B 1 491 ? 155.248 110.814 123.224 1.00 13153. ? 491 MET B O     1 
ATOM   7814  C  CB    . MET B 1 491 ? 152.692 110.560 122.191 1.00 13077. ? 491 MET B CB    1 
ATOM   7815  C  CG    . MET B 1 491 ? 152.172 109.943 120.909 1.00 13156. ? 491 MET B CG    1 
ATOM   7816  S  SD    . MET B 1 491 ? 153.013 108.399 120.524 1.00 13201. ? 491 MET B SD    1 
ATOM   7817  C  CE    . MET B 1 491 ? 154.547 109.029 119.854 1.00 13216. ? 491 MET B CE    1 
ATOM   7818  N  N     . LYS B 1 492 ? 154.926 109.343 124.899 1.00 12763. ? 492 LYS B N     1 
ATOM   7819  C  CA    . LYS B 1 492 ? 156.194 109.579 125.585 1.00 12754. ? 492 LYS B CA    1 
ATOM   7820  C  C     . LYS B 1 492 ? 156.341 111.016 126.073 1.00 12741. ? 492 LYS B C     1 
ATOM   7821  O  O     . LYS B 1 492 ? 157.459 111.478 126.312 1.00 12742. ? 492 LYS B O     1 
ATOM   7822  C  CB    . LYS B 1 492 ? 157.385 109.200 124.698 1.00 12758. ? 492 LYS B CB    1 
ATOM   7823  C  CG    . LYS B 1 492 ? 157.216 107.881 123.968 1.00 12772. ? 492 LYS B CG    1 
ATOM   7824  C  CD    . LYS B 1 492 ? 158.533 107.393 123.403 1.00 12764. ? 492 LYS B CD    1 
ATOM   7825  C  CE    . LYS B 1 492 ? 158.361 106.857 121.995 1.00 12759. ? 492 LYS B CE    1 
ATOM   7826  N  NZ    . LYS B 1 492 ? 159.644 106.864 121.244 1.00 12767. ? 492 LYS B NZ    1 
ATOM   7827  N  N     . LYS B 1 493 ? 155.236 111.742 126.230 1.00 12739. ? 493 LYS B N     1 
ATOM   7828  C  CA    . LYS B 1 493 ? 155.277 113.116 126.708 1.00 12703. ? 493 LYS B CA    1 
ATOM   7829  C  C     . LYS B 1 493 ? 154.238 113.312 127.801 1.00 12715. ? 493 LYS B C     1 
ATOM   7830  O  O     . LYS B 1 493 ? 153.151 112.731 127.757 1.00 12727. ? 493 LYS B O     1 
ATOM   7831  C  CB    . LYS B 1 493 ? 155.033 114.119 125.574 1.00 12633. ? 493 LYS B CB    1 
ATOM   7832  C  CG    . LYS B 1 493 ? 155.922 113.920 124.359 1.00 12678. ? 493 LYS B CG    1 
ATOM   7833  C  CD    . LYS B 1 493 ? 157.317 114.464 124.596 1.00 12709. ? 493 LYS B CD    1 
ATOM   7834  C  CE    . LYS B 1 493 ? 157.631 115.607 123.649 1.00 12690. ? 493 LYS B CE    1 
ATOM   7835  N  NZ    . LYS B 1 493 ? 158.883 116.314 124.033 1.00 12700. ? 493 LYS B NZ    1 
ATOM   7836  N  N     . GLU B 1 494 ? 154.581 114.143 128.780 1.00 12712. ? 494 GLU B N     1 
ATOM   7837  C  CA    . GLU B 1 494 ? 153.691 114.414 129.900 1.00 12733. ? 494 GLU B CA    1 
ATOM   7838  C  C     . GLU B 1 494 ? 152.681 115.485 129.517 1.00 12706. ? 494 GLU B C     1 
ATOM   7839  O  O     . GLU B 1 494 ? 153.042 116.504 128.923 1.00 12606. ? 494 GLU B O     1 
ATOM   7840  C  CB    . GLU B 1 494 ? 154.492 114.862 131.120 1.00 12741. ? 494 GLU B CB    1 
ATOM   7841  C  CG    . GLU B 1 494 ? 153.645 115.195 132.332 1.00 12750. ? 494 GLU B CG    1 
ATOM   7842  C  CD    . GLU B 1 494 ? 154.065 116.489 132.998 1.00 12708. ? 494 GLU B CD    1 
ATOM   7843  O  OE1   . GLU B 1 494 ? 155.206 116.560 133.498 1.00 12721. ? 494 GLU B OE1   1 
ATOM   7844  O  OE2   . GLU B 1 494 ? 153.252 117.437 133.023 1.00 12672. ? 494 GLU B OE2   1 
ATOM   7845  N  N     . ILE B 1 495 ? 151.415 115.259 129.862 1.00 12742. ? 495 ILE B N     1 
ATOM   7846  C  CA    . ILE B 1 495 ? 150.375 116.231 129.545 1.00 12685. ? 495 ILE B CA    1 
ATOM   7847  C  C     . ILE B 1 495 ? 149.710 116.735 130.819 1.00 12610. ? 495 ILE B C     1 
ATOM   7848  O  O     . ILE B 1 495 ? 149.216 117.870 130.867 1.00 12451. ? 495 ILE B O     1 
ATOM   7849  C  CB    . ILE B 1 495 ? 149.334 115.633 128.582 1.00 12693. ? 495 ILE B CB    1 
ATOM   7850  C  CG1   . ILE B 1 495 ? 148.757 114.340 129.153 1.00 12735. ? 495 ILE B CG1   1 
ATOM   7851  C  CG2   . ILE B 1 495 ? 149.956 115.382 127.222 1.00 12602. ? 495 ILE B CG2   1 
ATOM   7852  C  CD1   . ILE B 1 495 ? 147.648 113.752 128.321 1.00 12710. ? 495 ILE B CD1   1 
ATOM   7853  N  N     . CYS B 1 496 ? 149.708 115.905 131.860 1.00 12695. ? 496 CYS B N     1 
ATOM   7854  C  CA    . CYS B 1 496 ? 148.989 116.187 133.093 1.00 12611. ? 496 CYS B CA    1 
ATOM   7855  C  C     . CYS B 1 496 ? 149.910 116.015 134.291 1.00 12691. ? 496 CYS B C     1 
ATOM   7856  O  O     . CYS B 1 496 ? 150.920 115.310 134.235 1.00 12742. ? 496 CYS B O     1 
ATOM   7857  C  CB    . CYS B 1 496 ? 147.768 115.274 133.258 1.00 12583. ? 496 CYS B CB    1 
ATOM   7858  S  SG    . CYS B 1 496 ? 146.387 115.657 132.169 1.00 12507. ? 496 CYS B SG    1 
ATOM   7859  N  N     . ASN B 1 497 ? 149.539 116.677 135.383 1.00 12631. ? 497 ASN B N     1 
ATOM   7860  C  CA    . ASN B 1 497 ? 150.286 116.599 136.635 1.00 12677. ? 497 ASN B CA    1 
ATOM   7861  C  C     . ASN B 1 497 ? 149.322 116.917 137.764 1.00 12565. ? 497 ASN B C     1 
ATOM   7862  O  O     . ASN B 1 497 ? 148.753 118.011 137.794 1.00 12375. ? 497 ASN B O     1 
ATOM   7863  C  CB    . ASN B 1 497 ? 151.460 117.574 136.629 1.00 12682. ? 497 ASN B CB    1 
ATOM   7864  C  CG    . ASN B 1 497 ? 152.352 117.419 137.838 1.00 12692. ? 497 ASN B CG    1 
ATOM   7865  O  OD1   . ASN B 1 497 ? 152.900 116.346 138.085 1.00 12757. ? 497 ASN B OD1   1 
ATOM   7866  N  ND2   . ASN B 1 497 ? 152.508 118.493 138.599 1.00 12627. ? 497 ASN B ND2   1 
ATOM   7867  N  N     . ALA B 1 498 ? 149.126 115.974 138.680 1.00 12642. ? 498 ALA B N     1 
ATOM   7868  C  CA    . ALA B 1 498 ? 148.142 116.164 139.734 1.00 12510. ? 498 ALA B CA    1 
ATOM   7869  C  C     . ALA B 1 498 ? 148.641 115.539 141.025 1.00 12681. ? 498 ALA B C     1 
ATOM   7870  O  O     . ALA B 1 498 ? 149.362 114.540 141.007 1.00 12733. ? 498 ALA B O     1 
ATOM   7871  C  CB    . ALA B 1 498 ? 146.792 115.559 139.346 1.00 12508. ? 498 ALA B CB    1 
ATOM   7872  N  N     . TYR B 1 499 ? 148.237 116.131 142.146 1.00 12605. ? 499 TYR B N     1 
ATOM   7873  C  CA    . TYR B 1 499 ? 148.577 115.558 143.441 1.00 12704. ? 499 TYR B CA    1 
ATOM   7874  C  C     . TYR B 1 499 ? 147.597 116.017 144.505 1.00 12611. ? 499 TYR B C     1 
ATOM   7875  O  O     . TYR B 1 499 ? 146.884 117.009 144.340 1.00 12495. ? 499 TYR B O     1 
ATOM   7876  C  CB    . TYR B 1 499 ? 150.000 115.917 143.881 1.00 12737. ? 499 TYR B CB    1 
ATOM   7877  C  CG    . TYR B 1 499 ? 150.480 117.305 143.545 1.00 12675. ? 499 TYR B CG    1 
ATOM   7878  C  CD1   . TYR B 1 499 ? 150.143 118.387 144.342 1.00 12698. ? 499 TYR B CD1   1 
ATOM   7879  C  CD2   . TYR B 1 499 ? 151.319 117.525 142.464 1.00 12689. ? 499 TYR B CD2   1 
ATOM   7880  C  CE1   . TYR B 1 499 ? 150.597 119.653 144.051 1.00 12679. ? 499 TYR B CE1   1 
ATOM   7881  C  CE2   . TYR B 1 499 ? 151.780 118.786 142.166 1.00 12649. ? 499 TYR B CE2   1 
ATOM   7882  C  CZ    . TYR B 1 499 ? 151.417 119.847 142.963 1.00 12636. ? 499 TYR B CZ    1 
ATOM   7883  O  OH    . TYR B 1 499 ? 151.873 121.111 142.669 1.00 12624. ? 499 TYR B OH    1 
ATOM   7884  N  N     . THR B 1 500 ? 147.592 115.283 145.614 1.00 12644. ? 500 THR B N     1 
ATOM   7885  C  CA    . THR B 1 500 ? 146.894 115.716 146.814 1.00 12602. ? 500 THR B CA    1 
ATOM   7886  C  C     . THR B 1 500 ? 147.667 116.865 147.444 1.00 12669. ? 500 THR B C     1 
ATOM   7887  O  O     . THR B 1 500 ? 148.863 116.740 147.720 1.00 12734. ? 500 THR B O     1 
ATOM   7888  C  CB    . THR B 1 500 ? 146.761 114.562 147.806 1.00 12705. ? 500 THR B CB    1 
ATOM   7889  O  OG1   . THR B 1 500 ? 146.214 113.419 147.141 1.00 12708. ? 500 THR B OG1   1 
ATOM   7890  C  CG2   . THR B 1 500 ? 145.852 114.951 148.953 1.00 12671. ? 500 THR B CG2   1 
ATOM   7891  N  N     . GLU B 1 501 ? 146.988 117.986 147.660 1.00 12553. ? 501 GLU B N     1 
ATOM   7892  C  CA    . GLU B 1 501 ? 147.662 119.179 148.148 1.00 12657. ? 501 GLU B CA    1 
ATOM   7893  C  C     . GLU B 1 501 ? 148.126 118.999 149.588 1.00 12704. ? 501 GLU B C     1 
ATOM   7894  O  O     . GLU B 1 501 ? 147.494 118.309 150.391 1.00 12718. ? 501 GLU B O     1 
ATOM   7895  C  CB    . GLU B 1 501 ? 146.740 120.392 148.043 1.00 12585. ? 501 GLU B CB    1 
ATOM   7896  C  CG    . GLU B 1 501 ? 146.317 120.723 146.626 1.00 12516. ? 501 GLU B CG    1 
ATOM   7897  C  CD    . GLU B 1 501 ? 147.487 120.769 145.665 1.00 12625. ? 501 GLU B CD    1 
ATOM   7898  O  OE1   . GLU B 1 501 ? 148.435 121.540 145.914 1.00 12708. ? 501 GLU B OE1   1 
ATOM   7899  O  OE2   . GLU B 1 501 ? 147.458 120.037 144.656 1.00 12545. ? 501 GLU B OE2   1 
ATOM   7900  N  N     . LEU B 1 502 ? 149.249 119.635 149.909 1.00 12744. ? 502 LEU B N     1 
ATOM   7901  C  CA    . LEU B 1 502 ? 149.799 119.597 151.258 1.00 12730. ? 502 LEU B CA    1 
ATOM   7902  C  C     . LEU B 1 502 ? 149.160 120.699 152.093 1.00 12704. ? 502 LEU B C     1 
ATOM   7903  O  O     . LEU B 1 502 ? 149.360 121.886 151.819 1.00 12708. ? 502 LEU B O     1 
ATOM   7904  C  CB    . LEU B 1 502 ? 151.316 119.760 151.212 1.00 12739. ? 502 LEU B CB    1 
ATOM   7905  C  CG    . LEU B 1 502 ? 152.071 119.738 152.539 1.00 12737. ? 502 LEU B CG    1 
ATOM   7906  C  CD1   . LEU B 1 502 ? 151.780 118.463 153.299 1.00 12740. ? 502 LEU B CD1   1 
ATOM   7907  C  CD2   . LEU B 1 502 ? 153.558 119.879 152.293 1.00 12757. ? 502 LEU B CD2   1 
ATOM   7908  N  N     . ASN B 1 503 ? 148.391 120.309 153.108 1.00 12705. ? 503 ASN B N     1 
ATOM   7909  C  CA    . ASN B 1 503 ? 147.659 121.257 153.937 1.00 12655. ? 503 ASN B CA    1 
ATOM   7910  C  C     . ASN B 1 503 ? 148.281 121.448 155.314 1.00 12748. ? 503 ASN B C     1 
ATOM   7911  O  O     . ASN B 1 503 ? 147.698 122.143 156.152 1.00 12723. ? 503 ASN B O     1 
ATOM   7912  C  CB    . ASN B 1 503 ? 146.201 120.816 154.080 1.00 12549. ? 503 ASN B CB    1 
ATOM   7913  C  CG    . ASN B 1 503 ? 146.058 119.318 154.222 1.00 12608. ? 503 ASN B CG    1 
ATOM   7914  O  OD1   . ASN B 1 503 ? 147.026 118.577 154.080 1.00 12735. ? 503 ASN B OD1   1 
ATOM   7915  N  ND2   . ASN B 1 503 ? 144.845 118.864 154.507 1.00 12517. ? 503 ASN B ND2   1 
ATOM   7916  N  N     . ASP B 1 504 ? 149.447 120.856 155.571 1.00 12751. ? 504 ASP B N     1 
ATOM   7917  C  CA    . ASP B 1 504 ? 150.108 121.003 156.860 1.00 12741. ? 504 ASP B CA    1 
ATOM   7918  C  C     . ASP B 1 504 ? 151.052 122.195 156.797 1.00 12749. ? 504 ASP B C     1 
ATOM   7919  O  O     . ASP B 1 504 ? 152.021 122.161 156.025 1.00 12770. ? 504 ASP B O     1 
ATOM   7920  C  CB    . ASP B 1 504 ? 150.872 119.738 157.216 1.00 12743. ? 504 ASP B CB    1 
ATOM   7921  C  CG    . ASP B 1 504 ? 151.250 119.675 158.682 1.00 12754. ? 504 ASP B CG    1 
ATOM   7922  O  OD1   . ASP B 1 504 ? 151.159 120.711 159.370 1.00 12764. ? 504 ASP B OD1   1 
ATOM   7923  O  OD2   . ASP B 1 504 ? 151.641 118.586 159.148 1.00 12758. ? 504 ASP B OD2   1 
ATOM   7924  N  N     . PRO B 1 505 ? 150.813 123.262 157.564 1.00 12743. ? 505 PRO B N     1 
ATOM   7925  C  CA    . PRO B 1 505 ? 151.713 124.426 157.490 1.00 12750. ? 505 PRO B CA    1 
ATOM   7926  C  C     . PRO B 1 505 ? 153.147 124.122 157.886 1.00 12783. ? 505 PRO B C     1 
ATOM   7927  O  O     . PRO B 1 505 ? 154.075 124.676 157.286 1.00 12779. ? 505 PRO B O     1 
ATOM   7928  C  CB    . PRO B 1 505 ? 151.061 125.431 158.451 1.00 12751. ? 505 PRO B CB    1 
ATOM   7929  C  CG    . PRO B 1 505 ? 149.656 124.967 158.614 1.00 12748. ? 505 PRO B CG    1 
ATOM   7930  C  CD    . PRO B 1 505 ? 149.698 123.482 158.496 1.00 12756. ? 505 PRO B CD    1 
ATOM   7931  N  N     . MET B 1 506 ? 153.362 123.254 158.875 1.00 13789. ? 506 MET B N     1 
ATOM   7932  C  CA    . MET B 1 506 ? 154.718 122.999 159.351 1.00 13813. ? 506 MET B CA    1 
ATOM   7933  C  C     . MET B 1 506 ? 155.537 122.241 158.314 1.00 13780. ? 506 MET B C     1 
ATOM   7934  O  O     . MET B 1 506 ? 156.682 122.606 158.022 1.00 13803. ? 506 MET B O     1 
ATOM   7935  C  CB    . MET B 1 506 ? 154.675 122.230 160.670 1.00 13839. ? 506 MET B CB    1 
ATOM   7936  C  CG    . MET B 1 506 ? 154.078 123.016 161.821 1.00 13859. ? 506 MET B CG    1 
ATOM   7937  S  SD    . MET B 1 506 ? 154.133 124.797 161.547 1.00 13847. ? 506 MET B SD    1 
ATOM   7938  C  CE    . MET B 1 506 ? 152.827 125.352 162.640 1.00 13857. ? 506 MET B CE    1 
ATOM   7939  N  N     . ARG B 1 507 ? 154.968 121.177 157.746 1.00 12771. ? 507 ARG B N     1 
ATOM   7940  C  CA    . ARG B 1 507 ? 155.688 120.421 156.728 1.00 12761. ? 507 ARG B CA    1 
ATOM   7941  C  C     . ARG B 1 507 ? 155.891 121.253 155.470 1.00 12770. ? 507 ARG B C     1 
ATOM   7942  O  O     . ARG B 1 507 ? 156.942 121.168 154.823 1.00 12788. ? 507 ARG B O     1 
ATOM   7943  C  CB    . ARG B 1 507 ? 154.942 119.128 156.412 1.00 12750. ? 507 ARG B CB    1 
ATOM   7944  C  CG    . ARG B 1 507 ? 154.551 118.340 157.647 1.00 12749. ? 507 ARG B CG    1 
ATOM   7945  C  CD    . ARG B 1 507 ? 154.079 116.945 157.292 1.00 12746. ? 507 ARG B CD    1 
ATOM   7946  N  NE    . ARG B 1 507 ? 155.119 116.166 156.632 1.00 12746. ? 507 ARG B NE    1 
ATOM   7947  C  CZ    . ARG B 1 507 ? 155.289 114.862 156.792 1.00 12749. ? 507 ARG B CZ    1 
ATOM   7948  N  NH1   . ARG B 1 507 ? 154.508 114.156 157.592 1.00 12747. ? 507 ARG B NH1   1 
ATOM   7949  N  NH2   . ARG B 1 507 ? 156.268 114.250 156.133 1.00 12754. ? 507 ARG B NH2   1 
ATOM   7950  N  N     . GLN B 1 508 ? 154.898 122.068 155.110 1.00 12757. ? 508 GLN B N     1 
ATOM   7951  C  CA    . GLN B 1 508 ? 155.053 122.948 153.958 1.00 12749. ? 508 GLN B CA    1 
ATOM   7952  C  C     . GLN B 1 508 ? 156.170 123.956 154.188 1.00 12763. ? 508 GLN B C     1 
ATOM   7953  O  O     . GLN B 1 508 ? 156.957 124.241 153.279 1.00 12788. ? 508 GLN B O     1 
ATOM   7954  C  CB    . GLN B 1 508 ? 153.736 123.662 153.660 1.00 12751. ? 508 GLN B CB    1 
ATOM   7955  C  CG    . GLN B 1 508 ? 153.792 124.551 152.436 1.00 12745. ? 508 GLN B CG    1 
ATOM   7956  C  CD    . GLN B 1 508 ? 154.049 123.769 151.167 1.00 12740. ? 508 GLN B CD    1 
ATOM   7957  O  OE1   . GLN B 1 508 ? 153.295 122.864 150.818 1.00 12746. ? 508 GLN B OE1   1 
ATOM   7958  N  NE2   . GLN B 1 508 ? 155.129 124.106 150.475 1.00 12747. ? 508 GLN B NE2   1 
ATOM   7959  N  N     . ARG B 1 509 ? 156.257 124.505 155.401 1.00 12761. ? 509 ARG B N     1 
ATOM   7960  C  CA    . ARG B 1 509 ? 157.346 125.418 155.724 1.00 12753. ? 509 ARG B CA    1 
ATOM   7961  C  C     . ARG B 1 509 ? 158.693 124.711 155.666 1.00 12763. ? 509 ARG B C     1 
ATOM   7962  O  O     . ARG B 1 509 ? 159.676 125.276 155.178 1.00 12787. ? 509 ARG B O     1 
ATOM   7963  C  CB    . ARG B 1 509 ? 157.119 126.034 157.102 1.00 12760. ? 509 ARG B CB    1 
ATOM   7964  C  CG    . ARG B 1 509 ? 156.366 127.346 157.065 1.00 12754. ? 509 ARG B CG    1 
ATOM   7965  C  CD    . ARG B 1 509 ? 156.833 128.286 158.155 1.00 12753. ? 509 ARG B CD    1 
ATOM   7966  N  NE    . ARG B 1 509 ? 156.141 129.567 158.090 1.00 12761. ? 509 ARG B NE    1 
ATOM   7967  C  CZ    . ARG B 1 509 ? 154.888 129.764 158.477 1.00 12756. ? 509 ARG B CZ    1 
ATOM   7968  N  NH1   . ARG B 1 509 ? 154.158 128.783 158.982 1.00 12754. ? 509 ARG B NH1   1 
ATOM   7969  N  NH2   . ARG B 1 509 ? 154.355 130.976 158.356 1.00 12766. ? 509 ARG B NH2   1 
ATOM   7970  N  N     . GLN B 1 510 ? 158.762 123.477 156.165 1.00 12827. ? 510 GLN B N     1 
ATOM   7971  C  CA    . GLN B 1 510 ? 160.017 122.736 156.088 1.00 12822. ? 510 GLN B CA    1 
ATOM   7972  C  C     . GLN B 1 510 ? 160.441 122.525 154.640 1.00 12846. ? 510 GLN B C     1 
ATOM   7973  O  O     . GLN B 1 510 ? 161.618 122.691 154.297 1.00 12878. ? 510 GLN B O     1 
ATOM   7974  C  CB    . GLN B 1 510 ? 159.885 121.398 156.812 1.00 12825. ? 510 GLN B CB    1 
ATOM   7975  C  CG    . GLN B 1 510 ? 159.827 121.515 158.324 1.00 12826. ? 510 GLN B CG    1 
ATOM   7976  C  CD    . GLN B 1 510 ? 159.340 120.243 158.988 1.00 12839. ? 510 GLN B CD    1 
ATOM   7977  O  OE1   . GLN B 1 510 ? 159.214 119.202 158.343 1.00 12834. ? 510 GLN B OE1   1 
ATOM   7978  N  NE2   . GLN B 1 510 ? 159.057 120.322 160.282 1.00 12846. ? 510 GLN B NE2   1 
ATOM   7979  N  N     . LEU B 1 511 ? 159.478 122.156 153.789 1.00 12763. ? 511 LEU B N     1 
ATOM   7980  C  CA    . LEU B 1 511 ? 159.783 121.916 152.353 1.00 12762. ? 511 LEU B CA    1 
ATOM   7981  C  C     . LEU B 1 511 ? 160.246 123.231 151.707 1.00 12785. ? 511 LEU B C     1 
ATOM   7982  O  O     . LEU B 1 511 ? 161.280 123.214 151.004 1.00 12815. ? 511 LEU B O     1 
ATOM   7983  C  CB    . LEU B 1 511 ? 158.560 121.340 151.643 1.00 12751. ? 511 LEU B CB    1 
ATOM   7984  C  CG    . LEU B 1 511 ? 158.180 119.908 152.031 1.00 12742. ? 511 LEU B CG    1 
ATOM   7985  C  CD1   . LEU B 1 511 ? 156.995 119.421 151.219 1.00 12748. ? 511 LEU B CD1   1 
ATOM   7986  C  CD2   . LEU B 1 511 ? 159.365 118.974 151.861 1.00 12765. ? 511 LEU B CD2   1 
ATOM   7987  N  N     . PHE B 1 512 ? 159.511 124.321 151.945 1.00 12956. ? 512 PHE B N     1 
ATOM   7988  C  CA    . PHE B 1 512 ? 159.897 125.644 151.382 1.00 12963. ? 512 PHE B CA    1 
ATOM   7989  C  C     . PHE B 1 512 ? 161.307 125.986 151.855 1.00 13006. ? 512 PHE B C     1 
ATOM   7990  O  O     . PHE B 1 512 ? 162.130 126.457 151.040 1.00 13037. ? 512 PHE B O     1 
ATOM   7991  C  CB    . PHE B 1 512 ? 158.893 126.721 151.801 1.00 12963. ? 512 PHE B CB    1 
ATOM   7992  C  CG    . PHE B 1 512 ? 157.703 126.883 150.864 1.00 12948. ? 512 PHE B CG    1 
ATOM   7993  C  CD1   . PHE B 1 512 ? 157.817 126.585 149.511 1.00 12948. ? 512 PHE B CD1   1 
ATOM   7994  C  CD2   . PHE B 1 512 ? 156.480 127.344 151.335 1.00 12971. ? 512 PHE B CD2   1 
ATOM   7995  C  CE1   . PHE B 1 512 ? 156.735 126.737 148.658 1.00 12966. ? 512 PHE B CE1   1 
ATOM   7996  C  CE2   . PHE B 1 512 ? 155.401 127.495 150.478 1.00 12979. ? 512 PHE B CE2   1 
ATOM   7997  C  CZ    . PHE B 1 512 ? 155.531 127.192 149.143 1.00 12961. ? 512 PHE B CZ    1 
ATOM   7998  N  N     . GLU B 1 513 ? 161.582 125.749 153.141 1.00 13602. ? 513 GLU B N     1 
ATOM   7999  C  CA    . GLU B 1 513 ? 162.930 126.037 153.699 1.00 13628. ? 513 GLU B CA    1 
ATOM   8000  C  C     . GLU B 1 513 ? 163.985 125.241 152.911 1.00 13667. ? 513 GLU B C     1 
ATOM   8001  O  O     . GLU B 1 513 ? 165.028 125.834 152.560 1.00 13712. ? 513 GLU B O     1 
ATOM   8002  C  CB    . GLU B 1 513 ? 162.972 125.730 155.196 1.00 13630. ? 513 GLU B CB    1 
ATOM   8003  C  CG    . GLU B 1 513 ? 162.099 126.661 156.034 1.00 13641. ? 513 GLU B CG    1 
ATOM   8004  C  CD    . GLU B 1 513 ? 162.023 126.388 157.527 1.00 13627. ? 513 GLU B CD    1 
ATOM   8005  O  OE1   . GLU B 1 513 ? 162.516 125.319 157.945 1.00 13628. ? 513 GLU B OE1   1 
ATOM   8006  O  OE2   . GLU B 1 513 ? 161.490 127.233 158.277 1.00 13628. ? 513 GLU B OE2   1 
ATOM   8007  N  N     . GLU B 1 514 ? 163.725 123.956 152.646 1.00 14396. ? 514 GLU B N     1 
ATOM   8008  C  CA    . GLU B 1 514 ? 164.740 123.130 151.950 1.00 14434. ? 514 GLU B CA    1 
ATOM   8009  C  C     . GLU B 1 514 ? 165.000 123.726 150.567 1.00 14453. ? 514 GLU B C     1 
ATOM   8010  O  O     . GLU B 1 514 ? 166.162 123.758 150.146 1.00 14478. ? 514 GLU B O     1 
ATOM   8011  C  CB    . GLU B 1 514 ? 164.291 121.684 151.799 1.00 14441. ? 514 GLU B CB    1 
ATOM   8012  C  CG    . GLU B 1 514 ? 164.127 120.960 153.130 1.00 14452. ? 514 GLU B CG    1 
ATOM   8013  C  CD    . GLU B 1 514 ? 163.495 119.595 152.949 1.00 14469. ? 514 GLU B CD    1 
ATOM   8014  O  OE1   . GLU B 1 514 ? 163.194 119.243 151.790 1.00 14465. ? 514 GLU B OE1   1 
ATOM   8015  O  OE2   . GLU B 1 514 ? 163.299 118.889 153.958 1.00 14478. ? 514 GLU B OE2   1 
ATOM   8016  N  N     . GLN B 1 515 ? 163.960 124.180 149.888 1.00 14319. ? 515 GLN B N     1 
ATOM   8017  C  CA    . GLN B 1 515 ? 164.152 124.690 148.515 1.00 14341. ? 515 GLN B CA    1 
ATOM   8018  C  C     . GLN B 1 515 ? 165.078 125.902 148.601 1.00 14377. ? 515 GLN B C     1 
ATOM   8019  O  O     . GLN B 1 515 ? 166.000 125.988 147.790 1.00 14416. ? 515 GLN B O     1 
ATOM   8020  C  CB    . GLN B 1 515 ? 162.819 125.025 147.855 1.00 14344. ? 515 GLN B CB    1 
ATOM   8021  C  CG    . GLN B 1 515 ? 161.913 123.826 147.618 1.00 14322. ? 515 GLN B CG    1 
ATOM   8022  C  CD    . GLN B 1 515 ? 162.443 122.894 146.556 1.00 14334. ? 515 GLN B CD    1 
ATOM   8023  O  OE1   . GLN B 1 515 ? 162.617 123.274 145.395 1.00 14354. ? 515 GLN B OE1   1 
ATOM   8024  N  NE2   . GLN B 1 515 ? 162.703 121.657 146.946 1.00 14328. ? 515 GLN B NE2   1 
ATOM   8025  N  N     . ALA B 1 516 ? 164.857 126.785 149.568 1.00 14735. ? 516 ALA B N     1 
ATOM   8026  C  CA    . ALA B 1 516 ? 165.688 127.998 149.730 1.00 14758. ? 516 ALA B CA    1 
ATOM   8027  C  C     . ALA B 1 516 ? 167.141 127.604 149.937 1.00 14805. ? 516 ALA B C     1 
ATOM   8028  O  O     . ALA B 1 516 ? 168.028 128.242 149.367 1.00 14841. ? 516 ALA B O     1 
ATOM   8029  C  CB    . ALA B 1 516 ? 165.213 128.780 150.910 1.00 14750. ? 516 ALA B CB    1 
ATOM   8030  N  N     . LYS B 1 517 ? 167.379 126.591 150.750 1.00 15330. ? 517 LYS B N     1 
ATOM   8031  C  CA    . LYS B 1 517 ? 168.771 126.132 150.919 1.00 15353. ? 517 LYS B CA    1 
ATOM   8032  C  C     . LYS B 1 517 ? 169.368 125.930 149.529 1.00 15392. ? 517 LYS B C     1 
ATOM   8033  O  O     . LYS B 1 517 ? 170.425 126.514 149.252 1.00 15419. ? 517 LYS B O     1 
ATOM   8034  C  CB    . LYS B 1 517 ? 168.863 124.824 151.702 1.00 15352. ? 517 LYS B CB    1 
ATOM   8035  C  CG    . LYS B 1 517 ? 168.353 124.932 153.126 1.00 15363. ? 517 LYS B CG    1 
ATOM   8036  C  CD    . LYS B 1 517 ? 168.969 126.110 153.868 1.00 15356. ? 517 LYS B CD    1 
ATOM   8037  C  CE    . LYS B 1 517 ? 167.998 126.764 154.799 1.00 15345. ? 517 LYS B CE    1 
ATOM   8038  N  NZ    . LYS B 1 517 ? 166.901 127.407 154.072 1.00 15354. ? 517 LYS B NZ    1 
ATOM   8039  N  N     . ALA B 1 518 ? 168.712 125.142 148.688 1.00 16204. ? 518 ALA B N     1 
ATOM   8040  C  CA    . ALA B 1 518 ? 169.287 124.858 147.357 1.00 16245. ? 518 ALA B CA    1 
ATOM   8041  C  C     . ALA B 1 518 ? 169.418 126.153 146.561 1.00 16286. ? 518 ALA B C     1 
ATOM   8042  O  O     . ALA B 1 518 ? 170.528 126.468 146.117 1.00 16330. ? 518 ALA B O     1 
ATOM   8043  C  CB    . ALA B 1 518 ? 168.427 123.870 146.628 1.00 16247. ? 518 ALA B CB    1 
ATOM   8044  N  N     . LYS B 1 519 ? 168.336 126.909 146.418 1.00 16459. ? 519 LYS B N     1 
ATOM   8045  C  CA    . LYS B 1 519 ? 168.407 128.110 145.556 1.00 16481. ? 519 LYS B CA    1 
ATOM   8046  C  C     . LYS B 1 519 ? 169.672 128.842 145.964 1.00 16491. ? 519 LYS B C     1 
ATOM   8047  O  O     . LYS B 1 519 ? 170.438 129.272 145.092 1.00 16513. ? 519 LYS B O     1 
ATOM   8048  C  CB    . LYS B 1 519 ? 167.227 129.064 145.726 1.00 16471. ? 519 LYS B CB    1 
ATOM   8049  C  CG    . LYS B 1 519 ? 167.358 130.392 145.008 1.00 16489. ? 519 LYS B CG    1 
ATOM   8050  C  CD    . LYS B 1 519 ? 166.137 131.279 145.210 1.00 16477. ? 519 LYS B CD    1 
ATOM   8051  C  CE    . LYS B 1 519 ? 164.916 130.696 144.586 1.00 16478. ? 519 LYS B CE    1 
ATOM   8052  N  NZ    . LYS B 1 519 ? 165.094 130.516 143.144 1.00 16503. ? 519 LYS B NZ    1 
ATOM   8053  N  N     . ALA B 1 520 ? 169.890 128.989 147.274 1.00 16718. ? 520 ALA B N     1 
ATOM   8054  C  CA    . ALA B 1 520 ? 171.071 129.740 147.767 1.00 16737. ? 520 ALA B CA    1 
ATOM   8055  C  C     . ALA B 1 520 ? 172.329 129.284 147.023 1.00 16762. ? 520 ALA B C     1 
ATOM   8056  O  O     . ALA B 1 520 ? 173.077 130.151 146.520 1.00 16763. ? 520 ALA B O     1 
ATOM   8057  C  CB    . ALA B 1 520 ? 171.215 129.565 149.263 1.00 16732. ? 520 ALA B CB    1 
ATOM   8058  N  N     . ALA B 1 521 ? 172.558 127.968 146.955 1.00 17780. ? 521 ALA B N     1 
ATOM   8059  C  CA    . ALA B 1 521 ? 173.770 127.434 146.287 1.00 17814. ? 521 ALA B CA    1 
ATOM   8060  C  C     . ALA B 1 521 ? 173.381 126.728 144.987 1.00 17831. ? 521 ALA B C     1 
ATOM   8061  O  O     . ALA B 1 521 ? 173.089 125.512 145.025 1.00 17841. ? 521 ALA B O     1 
ATOM   8062  C  CB    . ALA B 1 521 ? 174.502 126.501 147.226 1.00 17825. ? 521 ALA B CB    1 
ATOM   8063  N  N     . GLY B 1 522 ? 173.375 127.465 143.871 1.00 18240. ? 522 GLY B N     1 
ATOM   8064  C  CA    . GLY B 1 522 ? 173.018 126.876 142.565 1.00 18264. ? 522 GLY B CA    1 
ATOM   8065  C  C     . GLY B 1 522 ? 171.539 126.550 142.495 1.00 18274. ? 522 GLY B C     1 
ATOM   8066  O  O     . GLY B 1 522 ? 170.774 127.103 143.310 1.00 18278. ? 522 GLY B O     1 
ATOM   8067  N  N     . ASP B 1 523 ? 171.140 125.700 141.544 1.00 18379. ? 523 ASP B N     1 
ATOM   8068  C  CA    . ASP B 1 523 ? 169.714 125.283 141.428 1.00 18386. ? 523 ASP B CA    1 
ATOM   8069  C  C     . ASP B 1 523 ? 168.819 126.515 141.600 1.00 18389. ? 523 ASP B C     1 
ATOM   8070  O  O     . ASP B 1 523 ? 167.952 126.499 142.499 1.00 18375. ? 523 ASP B O     1 
ATOM   8071  C  CB    . ASP B 1 523 ? 169.385 124.163 142.404 1.00 18380. ? 523 ASP B CB    1 
ATOM   8072  C  CG    . ASP B 1 523 ? 168.060 123.455 142.164 1.00 18387. ? 523 ASP B CG    1 
ATOM   8073  O  OD1   . ASP B 1 523 ? 167.885 122.897 141.061 1.00 18394. ? 523 ASP B OD1   1 
ATOM   8074  O  OD2   . ASP B 1 523 ? 167.215 123.466 143.084 1.00 18389. ? 523 ASP B OD2   1 
ATOM   8075  N  N     . ASP B 1 524 ? 169.024 127.544 140.772 1.00 18748. ? 524 ASP B N     1 
ATOM   8076  C  CA    . ASP B 1 524 ? 168.217 128.793 140.869 1.00 18754. ? 524 ASP B CA    1 
ATOM   8077  C  C     . ASP B 1 524 ? 166.750 128.473 140.562 1.00 18731. ? 524 ASP B C     1 
ATOM   8078  O  O     . ASP B 1 524 ? 165.868 129.213 141.048 1.00 18730. ? 524 ASP B O     1 
ATOM   8079  C  CB    . ASP B 1 524 ? 168.773 129.882 139.966 1.00 18766. ? 524 ASP B CB    1 
ATOM   8080  C  CG    . ASP B 1 524 ? 168.003 131.195 139.982 1.00 18760. ? 524 ASP B CG    1 
ATOM   8081  O  OD1   . ASP B 1 524 ? 167.901 131.801 141.069 1.00 18758. ? 524 ASP B OD1   1 
ATOM   8082  O  OD2   . ASP B 1 524 ? 167.507 131.596 138.908 1.00 18736. ? 524 ASP B OD2   1 
ATOM   8083  N  N     . GLU B 1 525 ? 166.501 127.406 139.797 1.00 17982. ? 525 GLU B N     1 
ATOM   8084  C  CA    . GLU B 1 525 ? 165.113 127.022 139.426 1.00 17947. ? 525 GLU B CA    1 
ATOM   8085  C  C     . GLU B 1 525 ? 164.314 126.683 140.695 1.00 17920. ? 525 GLU B C     1 
ATOM   8086  O  O     . GLU B 1 525 ? 163.065 126.674 140.618 1.00 17891. ? 525 GLU B O     1 
ATOM   8087  C  CB    . GLU B 1 525 ? 165.141 125.842 138.454 1.00 17934. ? 525 GLU B CB    1 
ATOM   8088  C  CG    . GLU B 1 525 ? 166.013 126.094 137.227 1.00 17923. ? 525 GLU B CG    1 
ATOM   8089  C  CD    . GLU B 1 525 ? 165.471 127.105 136.232 1.00 17927. ? 525 GLU B CD    1 
ATOM   8090  O  OE1   . GLU B 1 525 ? 164.352 127.618 136.441 1.00 17945. ? 525 GLU B OE1   1 
ATOM   8091  O  OE2   . GLU B 1 525 ? 166.178 127.382 135.240 1.00 17919. ? 525 GLU B OE2   1 
ATOM   8092  N  N     . ALA B 1 526 ? 165.006 126.446 141.816 1.00 16917. ? 526 ALA B N     1 
ATOM   8093  C  CA    . ALA B 1 526 ? 164.329 126.083 143.087 1.00 16864. ? 526 ALA B CA    1 
ATOM   8094  C  C     . ALA B 1 526 ? 163.157 127.029 143.358 1.00 16841. ? 526 ALA B C     1 
ATOM   8095  O  O     . ALA B 1 526 ? 163.270 128.241 143.063 1.00 16856. ? 526 ALA B O     1 
ATOM   8096  C  CB    . ALA B 1 526 ? 165.321 126.102 144.229 1.00 16850. ? 526 ALA B CB    1 
ATOM   8097  N  N     . MET B 1 527 ? 162.073 126.498 143.931 1.00 15870. ? 527 MET B N     1 
ATOM   8098  C  CA    . MET B 1 527 ? 160.868 127.323 144.208 1.00 15859. ? 527 MET B CA    1 
ATOM   8099  C  C     . MET B 1 527 ? 161.205 128.417 145.233 1.00 15857. ? 527 MET B C     1 
ATOM   8100  O  O     . MET B 1 527 ? 162.095 128.186 146.082 1.00 15843. ? 527 MET B O     1 
ATOM   8101  C  CB    . MET B 1 527 ? 159.722 126.459 144.746 1.00 15841. ? 527 MET B CB    1 
ATOM   8102  C  CG    . MET B 1 527 ? 159.185 125.461 143.742 1.00 15832. ? 527 MET B CG    1 
ATOM   8103  S  SD    . MET B 1 527 ? 157.577 124.820 144.247 1.00 15789. ? 527 MET B SD    1 
ATOM   8104  C  CE    . MET B 1 527 ? 156.743 126.374 144.596 1.00 15794. ? 527 MET B CE    1 
ATOM   8105  N  N     . PHE B 1 528 ? 160.511 129.557 145.156 1.00 16088. ? 528 PHE B N     1 
ATOM   8106  C  CA    . PHE B 1 528 ? 160.764 130.689 146.089 1.00 16082. ? 528 PHE B CA    1 
ATOM   8107  C  C     . PHE B 1 528 ? 159.954 130.486 147.370 1.00 16077. ? 528 PHE B C     1 
ATOM   8108  O  O     . PHE B 1 528 ? 159.087 129.585 147.411 1.00 16048. ? 528 PHE B O     1 
ATOM   8109  C  CB    . PHE B 1 528 ? 160.410 131.993 145.370 1.00 16077. ? 528 PHE B CB    1 
ATOM   8110  C  CG    . PHE B 1 528 ? 161.342 132.355 144.221 1.00 16082. ? 528 PHE B CG    1 
ATOM   8111  C  CD1   . PHE B 1 528 ? 161.198 131.765 142.970 1.00 16081. ? 528 PHE B CD1   1 
ATOM   8112  C  CD2   . PHE B 1 528 ? 162.345 133.303 144.388 1.00 16090. ? 528 PHE B CD2   1 
ATOM   8113  C  CE1   . PHE B 1 528 ? 162.046 132.099 141.926 1.00 16085. ? 528 PHE B CE1   1 
ATOM   8114  C  CE2   . PHE B 1 528 ? 163.186 133.637 143.339 1.00 16093. ? 528 PHE B CE2   1 
ATOM   8115  C  CZ    . PHE B 1 528 ? 163.035 133.036 142.111 1.00 16089. ? 528 PHE B CZ    1 
ATOM   8116  N  N     . ILE B 1 529 ? 160.226 131.304 148.392 1.00 15238. ? 529 ILE B N     1 
ATOM   8117  C  CA    . ILE B 1 529 ? 159.502 131.191 149.695 1.00 15200. ? 529 ILE B CA    1 
ATOM   8118  C  C     . ILE B 1 529 ? 158.347 132.206 149.712 1.00 15201. ? 529 ILE B C     1 
ATOM   8119  O  O     . ILE B 1 529 ? 158.550 133.335 149.218 1.00 15202. ? 529 ILE B O     1 
ATOM   8120  C  CB    . ILE B 1 529 ? 160.478 131.405 150.868 1.00 15204. ? 529 ILE B CB    1 
ATOM   8121  C  CG1   . ILE B 1 529 ? 159.752 131.520 152.209 1.00 15199. ? 529 ILE B CG1   1 
ATOM   8122  C  CG2   . ILE B 1 529 ? 161.380 132.614 150.614 1.00 15213. ? 529 ILE B CG2   1 
ATOM   8123  C  CD1   . ILE B 1 529 ? 159.083 130.237 152.667 1.00 15182. ? 529 ILE B CD1   1 
ATOM   8124  N  N     . ASP B 1 530 ? 157.185 131.816 150.245 1.00 15010. ? 530 ASP B N     1 
ATOM   8125  C  CA    . ASP B 1 530 ? 156.049 132.725 150.333 1.00 15001. ? 530 ASP B CA    1 
ATOM   8126  C  C     . ASP B 1 530 ? 155.486 132.686 151.747 1.00 14984. ? 530 ASP B C     1 
ATOM   8127  O  O     . ASP B 1 530 ? 155.081 131.623 152.229 1.00 14960. ? 530 ASP B O     1 
ATOM   8128  C  CB    . ASP B 1 530 ? 154.970 132.352 149.317 1.00 14987. ? 530 ASP B CB    1 
ATOM   8129  C  CG    . ASP B 1 530 ? 154.046 133.511 148.995 1.00 14981. ? 530 ASP B CG    1 
ATOM   8130  O  OD1   . ASP B 1 530 ? 153.760 134.318 149.904 1.00 14974. ? 530 ASP B OD1   1 
ATOM   8131  O  OD2   . ASP B 1 530 ? 153.603 133.615 147.833 1.00 14998. ? 530 ASP B OD2   1 
ATOM   8132  N  N     . GLU B 1 531 ? 155.460 133.844 152.405 1.00 14964. ? 531 GLU B N     1 
ATOM   8133  C  CA    . GLU B 1 531 ? 154.866 133.929 153.733 1.00 14942. ? 531 GLU B CA    1 
ATOM   8134  C  C     . GLU B 1 531 ? 153.345 133.938 153.668 1.00 14894. ? 531 GLU B C     1 
ATOM   8135  O  O     . GLU B 1 531 ? 152.681 133.386 154.552 1.00 14878. ? 531 GLU B O     1 
ATOM   8136  C  CB    . GLU B 1 531 ? 155.370 135.178 154.456 1.00 14969. ? 531 GLU B CB    1 
ATOM   8137  C  CG    . GLU B 1 531 ? 156.785 135.071 155.000 1.00 14984. ? 531 GLU B CG    1 
ATOM   8138  C  CD    . GLU B 1 531 ? 157.182 133.646 155.330 1.00 14981. ? 531 GLU B CD    1 
ATOM   8139  O  OE1   . GLU B 1 531 ? 156.860 133.181 156.443 1.00 14972. ? 531 GLU B OE1   1 
ATOM   8140  O  OE2   . GLU B 1 531 ? 157.825 132.995 154.482 1.00 14990. ? 531 GLU B OE2   1 
ATOM   8141  N  N     . ASN B 1 532 ? 152.779 134.568 152.636 1.00 13853. ? 532 ASN B N     1 
ATOM   8142  C  CA    . ASN B 1 532 ? 151.328 134.686 152.545 1.00 13818. ? 532 ASN B CA    1 
ATOM   8143  C  C     . ASN B 1 532 ? 150.668 133.326 152.371 1.00 13777. ? 532 ASN B C     1 
ATOM   8144  O  O     . ASN B 1 532 ? 149.623 133.054 152.973 1.00 13757. ? 532 ASN B O     1 
ATOM   8145  C  CB    . ASN B 1 532 ? 150.951 135.618 151.396 1.00 13825. ? 532 ASN B CB    1 
ATOM   8146  C  CG    . ASN B 1 532 ? 151.606 136.976 151.514 1.00 13827. ? 532 ASN B CG    1 
ATOM   8147  O  OD1   . ASN B 1 532 ? 151.894 137.444 152.615 1.00 13841. ? 532 ASN B OD1   1 
ATOM   8148  N  ND2   . ASN B 1 532 ? 151.847 137.618 150.378 1.00 13828. ? 532 ASN B ND2   1 
ATOM   8149  N  N     . PHE B 1 533 ? 151.258 132.458 151.548 1.00 12846. ? 533 PHE B N     1 
ATOM   8150  C  CA    . PHE B 1 533 ? 150.677 131.136 151.346 1.00 12786. ? 533 PHE B CA    1 
ATOM   8151  C  C     . PHE B 1 533 ? 150.718 130.310 152.626 1.00 12773. ? 533 PHE B C     1 
ATOM   8152  O  O     . PHE B 1 533 ? 149.754 129.607 152.947 1.00 12767. ? 533 PHE B O     1 
ATOM   8153  C  CB    . PHE B 1 533 ? 151.397 130.408 150.214 1.00 12782. ? 533 PHE B CB    1 
ATOM   8154  C  CG    . PHE B 1 533 ? 150.910 129.009 149.999 1.00 12748. ? 533 PHE B CG    1 
ATOM   8155  C  CD1   . PHE B 1 533 ? 149.566 128.757 149.800 1.00 12746. ? 533 PHE B CD1   1 
ATOM   8156  C  CD2   . PHE B 1 533 ? 151.792 127.945 150.007 1.00 12751. ? 533 PHE B CD2   1 
ATOM   8157  C  CE1   . PHE B 1 533 ? 149.112 127.473 149.608 1.00 12749. ? 533 PHE B CE1   1 
ATOM   8158  C  CE2   . PHE B 1 533 ? 151.342 126.659 149.815 1.00 12755. ? 533 PHE B CE2   1 
ATOM   8159  C  CZ    . PHE B 1 533 ? 150.001 126.422 149.616 1.00 12750. ? 533 PHE B CZ    1 
ATOM   8160  N  N     . CYS B 1 534 ? 151.823 130.378 153.370 1.00 12850. ? 534 CYS B N     1 
ATOM   8161  C  CA    . CYS B 1 534 ? 151.903 129.650 154.632 1.00 12825. ? 534 CYS B CA    1 
ATOM   8162  C  C     . CYS B 1 534 ? 150.919 130.208 155.653 1.00 12829. ? 534 CYS B C     1 
ATOM   8163  O  O     . CYS B 1 534 ? 150.293 129.448 156.404 1.00 12843. ? 534 CYS B O     1 
ATOM   8164  C  CB    . CYS B 1 534 ? 153.330 129.694 155.172 1.00 12834. ? 534 CYS B CB    1 
ATOM   8165  S  SG    . CYS B 1 534 ? 154.553 128.936 154.079 1.00 12840. ? 534 CYS B SG    1 
ATOM   8166  N  N     . THR B 1 535 ? 150.761 131.531 155.691 1.00 12761. ? 535 THR B N     1 
ATOM   8167  C  CA    . THR B 1 535 ? 149.777 132.128 156.587 1.00 12745. ? 535 THR B CA    1 
ATOM   8168  C  C     . THR B 1 535 ? 148.368 131.673 156.232 1.00 12750. ? 535 THR B C     1 
ATOM   8169  O  O     . THR B 1 535 ? 147.559 131.381 157.119 1.00 12756. ? 535 THR B O     1 
ATOM   8170  C  CB    . THR B 1 535 ? 149.882 133.651 156.539 1.00 12754. ? 535 THR B CB    1 
ATOM   8171  O  OG1   . THR B 1 535 ? 151.130 134.059 157.109 1.00 12761. ? 535 THR B OG1   1 
ATOM   8172  C  CG2   . THR B 1 535 ? 148.746 134.291 157.317 1.00 12752. ? 535 THR B CG2   1 
ATOM   8173  N  N     . ALA B 1 536 ? 148.057 131.604 154.936 1.00 12761. ? 536 ALA B N     1 
ATOM   8174  C  CA    . ALA B 1 536 ? 146.756 131.096 154.515 1.00 12755. ? 536 ALA B CA    1 
ATOM   8175  C  C     . ALA B 1 536 ? 146.579 129.637 154.911 1.00 12727. ? 536 ALA B C     1 
ATOM   8176  O  O     . ALA B 1 536 ? 145.497 129.232 155.347 1.00 12702. ? 536 ALA B O     1 
ATOM   8177  C  CB    . ALA B 1 536 ? 146.590 131.266 153.008 1.00 12766. ? 536 ALA B CB    1 
ATOM   8178  N  N     . LEU B 1 537 ? 147.630 128.830 154.754 1.00 12744. ? 537 LEU B N     1 
ATOM   8179  C  CA    . LEU B 1 537 ? 147.562 127.434 155.170 1.00 12720. ? 537 LEU B CA    1 
ATOM   8180  C  C     . LEU B 1 537 ? 147.309 127.314 156.663 1.00 12703. ? 537 LEU B C     1 
ATOM   8181  O  O     . LEU B 1 537 ? 146.655 126.366 157.110 1.00 12649. ? 537 LEU B O     1 
ATOM   8182  C  CB    . LEU B 1 537 ? 148.853 126.710 154.796 1.00 12736. ? 537 LEU B CB    1 
ATOM   8183  C  CG    . LEU B 1 537 ? 148.988 126.235 153.352 1.00 12742. ? 537 LEU B CG    1 
ATOM   8184  C  CD1   . LEU B 1 537 ? 150.062 125.172 153.253 1.00 12746. ? 537 LEU B CD1   1 
ATOM   8185  C  CD2   . LEU B 1 537 ? 147.665 125.710 152.833 1.00 12669. ? 537 LEU B CD2   1 
ATOM   8186  N  N     . GLU B 1 538 ? 147.821 128.261 157.448 1.00 12720. ? 538 GLU B N     1 
ATOM   8187  C  CA    . GLU B 1 538 ? 147.585 128.259 158.886 1.00 12718. ? 538 GLU B CA    1 
ATOM   8188  C  C     . GLU B 1 538 ? 146.123 128.485 159.248 1.00 12692. ? 538 GLU B C     1 
ATOM   8189  O  O     . GLU B 1 538 ? 145.752 128.267 160.405 1.00 12728. ? 538 GLU B O     1 
ATOM   8190  C  CB    . GLU B 1 538 ? 148.450 129.320 159.563 1.00 12743. ? 538 GLU B CB    1 
ATOM   8191  C  CG    . GLU B 1 538 ? 149.928 128.988 159.577 1.00 12751. ? 538 GLU B CG    1 
ATOM   8192  C  CD    . GLU B 1 538 ? 150.775 130.131 160.091 1.00 12751. ? 538 GLU B CD    1 
ATOM   8193  O  OE1   . GLU B 1 538 ? 150.201 131.159 160.501 1.00 12745. ? 538 GLU B OE1   1 
ATOM   8194  O  OE2   . GLU B 1 538 ? 152.017 130.002 160.084 1.00 12757. ? 538 GLU B OE2   1 
ATOM   8195  N  N     . TYR B 1 539 ? 145.292 128.920 158.305 1.00 12666. ? 539 TYR B N     1 
ATOM   8196  C  CA    . TYR B 1 539 ? 143.874 129.135 158.557 1.00 12626. ? 539 TYR B CA    1 
ATOM   8197  C  C     . TYR B 1 539 ? 143.023 127.906 158.273 1.00 12466. ? 539 TYR B C     1 
ATOM   8198  O  O     . TYR B 1 539 ? 141.810 127.948 158.491 1.00 12580. ? 539 TYR B O     1 
ATOM   8199  C  CB    . TYR B 1 539 ? 143.363 130.314 157.728 1.00 12679. ? 539 TYR B CB    1 
ATOM   8200  C  CG    . TYR B 1 539 ? 143.493 131.640 158.434 1.00 12655. ? 539 TYR B CG    1 
ATOM   8201  C  CD1   . TYR B 1 539 ? 142.541 132.052 159.353 1.00 12661. ? 539 TYR B CD1   1 
ATOM   8202  C  CD2   . TYR B 1 539 ? 144.572 132.475 158.189 1.00 12661. ? 539 TYR B CD2   1 
ATOM   8203  C  CE1   . TYR B 1 539 ? 142.658 133.259 160.004 1.00 12554. ? 539 TYR B CE1   1 
ATOM   8204  C  CE2   . TYR B 1 539 ? 144.697 133.684 158.836 1.00 12558. ? 539 TYR B CE2   1 
ATOM   8205  C  CZ    . TYR B 1 539 ? 143.738 134.071 159.742 1.00 93.42  ? 539 TYR B CZ    1 
ATOM   8206  O  OH    . TYR B 1 539 ? 143.858 135.277 160.389 1.00 91.81  ? 539 TYR B OH    1 
ATOM   8207  N  N     . GLY B 1 540 ? 143.620 126.822 157.787 1.00 76.17  ? 540 GLY B N     1 
ATOM   8208  C  CA    . GLY B 1 540 ? 142.888 125.593 157.566 1.00 74.82  ? 540 GLY B CA    1 
ATOM   8209  C  C     . GLY B 1 540 ? 142.529 125.340 156.117 1.00 78.65  ? 540 GLY B C     1 
ATOM   8210  O  O     . GLY B 1 540 ? 141.565 125.909 155.600 1.00 83.88  ? 540 GLY B O     1 
ATOM   8211  N  N     . LEU B 1 541 ? 143.302 124.485 155.451 1.00 81.46  ? 541 LEU B N     1 
ATOM   8212  C  CA    . LEU B 1 541 ? 142.994 124.065 154.095 1.00 76.63  ? 541 LEU B CA    1 
ATOM   8213  C  C     . LEU B 1 541 ? 142.419 122.660 154.132 1.00 76.96  ? 541 LEU B C     1 
ATOM   8214  O  O     . LEU B 1 541 ? 143.076 121.751 154.661 1.00 80.97  ? 541 LEU B O     1 
ATOM   8215  C  CB    . LEU B 1 541 ? 144.241 124.103 153.220 1.00 72.95  ? 541 LEU B CB    1 
ATOM   8216  C  CG    . LEU B 1 541 ? 144.141 123.409 151.860 1.00 78.92  ? 541 LEU B CG    1 
ATOM   8217  C  CD1   . LEU B 1 541 ? 143.319 124.232 150.888 1.00 79.69  ? 541 LEU B CD1   1 
ATOM   8218  C  CD2   . LEU B 1 541 ? 145.520 123.135 151.287 1.00 86.68  ? 541 LEU B CD2   1 
ATOM   8219  N  N     . PRO B 1 542 ? 141.218 122.432 153.608 1.00 67.25  ? 542 PRO B N     1 
ATOM   8220  C  CA    . PRO B 1 542 ? 140.625 121.092 153.652 1.00 66.74  ? 542 PRO B CA    1 
ATOM   8221  C  C     . PRO B 1 542 ? 141.458 120.106 152.858 1.00 65.72  ? 542 PRO B C     1 
ATOM   8222  O  O     . PRO B 1 542 ? 142.343 120.509 152.089 1.00 65.16  ? 542 PRO B O     1 
ATOM   8223  C  CB    . PRO B 1 542 ? 139.243 121.294 153.009 1.00 67.46  ? 542 PRO B CB    1 
ATOM   8224  C  CG    . PRO B 1 542 ? 139.006 122.758 153.025 1.00 67.86  ? 542 PRO B CG    1 
ATOM   8225  C  CD    . PRO B 1 542 ? 140.341 123.405 152.942 1.00 79.86  ? 542 PRO B CD    1 
ATOM   8226  N  N     . PRO B 1 543 ? 141.231 118.804 153.032 1.00 62.79  ? 543 PRO B N     1 
ATOM   8227  C  CA    . PRO B 1 543 ? 141.878 117.831 152.145 1.00 67.56  ? 543 PRO B CA    1 
ATOM   8228  C  C     . PRO B 1 543 ? 141.499 118.093 150.699 1.00 80.29  ? 543 PRO B C     1 
ATOM   8229  O  O     . PRO B 1 543 ? 140.331 117.958 150.330 1.00 91.58  ? 543 PRO B O     1 
ATOM   8230  C  CB    . PRO B 1 543 ? 141.339 116.484 152.640 1.00 69.61  ? 543 PRO B CB    1 
ATOM   8231  C  CG    . PRO B 1 543 ? 140.906 116.736 154.036 1.00 66.06  ? 543 PRO B CG    1 
ATOM   8232  C  CD    . PRO B 1 543 ? 140.427 118.151 154.078 1.00 73.80  ? 543 PRO B CD    1 
ATOM   8233  N  N     . THR B 1 544 ? 142.463 118.482 149.873 1.00 78.15  ? 544 THR B N     1 
ATOM   8234  C  CA    . THR B 1 544 ? 142.182 118.891 148.508 1.00 71.01  ? 544 THR B CA    1 
ATOM   8235  C  C     . THR B 1 544 ? 143.125 118.193 147.544 1.00 77.82  ? 544 THR B C     1 
ATOM   8236  O  O     . THR B 1 544 ? 144.183 117.689 147.924 1.00 84.69  ? 544 THR B O     1 
ATOM   8237  C  CB    . THR B 1 544 ? 142.306 120.408 148.329 1.00 61.84  ? 544 THR B CB    1 
ATOM   8238  O  OG1   . THR B 1 544 ? 143.611 120.834 148.735 1.00 74.10  ? 544 THR B OG1   1 
ATOM   8239  C  CG2   . THR B 1 544 ? 141.269 121.120 149.160 1.00 74.67  ? 544 THR B CG2   1 
ATOM   8240  N  N     . ALA B 1 545 ? 142.716 118.171 146.282 1.00 77.70  ? 545 ALA B N     1 
ATOM   8241  C  CA    . ALA B 1 545 ? 143.531 117.633 145.209 1.00 73.74  ? 545 ALA B CA    1 
ATOM   8242  C  C     . ALA B 1 545 ? 143.583 118.632 144.064 1.00 75.54  ? 545 ALA B C     1 
ATOM   8243  O  O     . ALA B 1 545 ? 142.570 119.223 143.683 1.00 82.30  ? 545 ALA B O     1 
ATOM   8244  C  CB    . ALA B 1 545 ? 142.988 116.293 144.716 1.00 89.53  ? 545 ALA B CB    1 
ATOM   8245  N  N     . GLY B 1 546 ? 144.778 118.808 143.507 1.00 79.02  ? 546 GLY B N     1 
ATOM   8246  C  CA    . GLY B 1 546 ? 144.970 119.725 142.411 1.00 81.56  ? 546 GLY B CA    1 
ATOM   8247  C  C     . GLY B 1 546 ? 145.456 118.985 141.182 1.00 71.77  ? 546 GLY B C     1 
ATOM   8248  O  O     . GLY B 1 546 ? 146.125 117.956 141.270 1.00 84.38  ? 546 GLY B O     1 
ATOM   8249  N  N     . TRP B 1 547 ? 145.107 119.538 140.024 1.00 66.01  ? 547 TRP B N     1 
ATOM   8250  C  CA    . TRP B 1 547 ? 145.397 118.916 138.745 1.00 73.71  ? 547 TRP B CA    1 
ATOM   8251  C  C     . TRP B 1 547 ? 145.695 120.009 137.733 1.00 79.89  ? 547 TRP B C     1 
ATOM   8252  O  O     . TRP B 1 547 ? 145.087 121.080 137.760 1.00 89.20  ? 547 TRP B O     1 
ATOM   8253  C  CB    . TRP B 1 547 ? 144.216 118.044 138.306 1.00 71.43  ? 547 TRP B CB    1 
ATOM   8254  C  CG    . TRP B 1 547 ? 144.257 117.498 136.919 1.00 72.60  ? 547 TRP B CG    1 
ATOM   8255  C  CD1   . TRP B 1 547 ? 144.656 116.253 136.547 1.00 79.94  ? 547 TRP B CD1   1 
ATOM   8256  C  CD2   . TRP B 1 547 ? 143.820 118.152 135.724 1.00 76.44  ? 547 TRP B CD2   1 
ATOM   8257  N  NE1   . TRP B 1 547 ? 144.522 116.097 135.191 1.00 63.27  ? 547 TRP B NE1   1 
ATOM   8258  C  CE2   . TRP B 1 547 ? 144.010 117.251 134.663 1.00 61.43  ? 547 TRP B CE2   1 
ATOM   8259  C  CE3   . TRP B 1 547 ? 143.307 119.420 135.445 1.00 85.98  ? 547 TRP B CE3   1 
ATOM   8260  C  CZ2   . TRP B 1 547 ? 143.700 117.575 133.350 1.00 69.97  ? 547 TRP B CZ2   1 
ATOM   8261  C  CZ3   . TRP B 1 547 ? 142.994 119.737 134.143 1.00 66.57  ? 547 TRP B CZ3   1 
ATOM   8262  C  CH2   . TRP B 1 547 ? 143.189 118.819 133.113 1.00 69.82  ? 547 TRP B CH2   1 
ATOM   8263  N  N     . GLY B 1 548 ? 146.651 119.740 136.853 1.00 72.96  ? 548 GLY B N     1 
ATOM   8264  C  CA    . GLY B 1 548 ? 147.024 120.708 135.846 1.00 71.79  ? 548 GLY B CA    1 
ATOM   8265  C  C     . GLY B 1 548 ? 147.462 120.055 134.555 1.00 69.38  ? 548 GLY B C     1 
ATOM   8266  O  O     . GLY B 1 548 ? 148.310 119.161 134.557 1.00 78.32  ? 548 GLY B O     1 
ATOM   8267  N  N     . MET B 1 549 ? 146.886 120.498 133.444 1.00 76.62  ? 549 MET B N     1 
ATOM   8268  C  CA    . MET B 1 549 ? 147.199 119.971 132.125 1.00 86.68  ? 549 MET B CA    1 
ATOM   8269  C  C     . MET B 1 549 ? 147.756 121.085 131.260 1.00 87.21  ? 549 MET B C     1 
ATOM   8270  O  O     . MET B 1 549 ? 147.211 122.193 131.236 1.00 91.60  ? 549 MET B O     1 
ATOM   8271  C  CB    . MET B 1 549 ? 145.964 119.369 131.461 1.00 87.97  ? 549 MET B CB    1 
ATOM   8272  C  CG    . MET B 1 549 ? 146.108 119.094 129.980 1.00 78.20  ? 549 MET B CG    1 
ATOM   8273  S  SD    . MET B 1 549 ? 144.519 118.747 129.206 1.00 48.85  ? 549 MET B SD    1 
ATOM   8274  C  CE    . MET B 1 549 ? 144.391 116.984 129.471 1.00 79.68  ? 549 MET B CE    1 
ATOM   8275  N  N     . GLY B 1 550 ? 148.835 120.790 130.550 1.00 91.81  ? 550 GLY B N     1 
ATOM   8276  C  CA    . GLY B 1 550 ? 149.361 121.753 129.606 1.00 83.98  ? 550 GLY B CA    1 
ATOM   8277  C  C     . GLY B 1 550 ? 148.652 121.654 128.274 1.00 78.09  ? 550 GLY B C     1 
ATOM   8278  O  O     . GLY B 1 550 ? 148.887 120.703 127.524 1.00 76.49  ? 550 GLY B O     1 
ATOM   8279  N  N     . ILE B 1 551 ? 147.780 122.612 127.956 1.00 89.64  ? 551 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 551 ? 147.048 122.513 126.701 1.00 83.37  ? 551 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 551 ? 147.868 123.160 125.599 1.00 87.38  ? 551 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 551 ? 147.529 124.240 125.106 1.00 95.01  ? 551 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 551 ? 145.670 123.191 126.799 1.00 90.43  ? 551 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 551 ? 145.097 123.057 128.207 1.00 99.69  ? 551 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 551 ? 144.721 122.618 125.763 1.00 95.53  ? 551 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 551 ? 143.811 123.820 128.401 1.00 99.31  ? 551 ILE B CD1   1 
ATOM   8287  N  N     . ASP B 1 552 ? 148.945 122.494 125.201 1.00 97.53  ? 552 ASP B N     1 
ATOM   8288  C  CA    . ASP B 1 552 ? 149.592 122.725 123.921 1.00 96.19  ? 552 ASP B CA    1 
ATOM   8289  C  C     . ASP B 1 552 ? 149.911 121.366 123.324 1.00 96.07  ? 552 ASP B C     1 
ATOM   8290  O  O     . ASP B 1 552 ? 149.799 121.159 122.114 1.00 100.82 ? 552 ASP B O     1 
ATOM   8291  C  CB    . ASP B 1 552 ? 150.845 123.584 124.085 1.00 100.58 ? 552 ASP B CB    1 
ATOM   8292  C  CG    . ASP B 1 552 ? 150.541 124.950 124.670 1.00 100.87 ? 552 ASP B CG    1 
ATOM   8293  O  OD1   . ASP B 1 552 ? 150.260 125.885 123.892 1.00 96.21  ? 552 ASP B OD1   1 
ATOM   8294  O  OD2   . ASP B 1 552 ? 150.578 125.087 125.910 1.00 102.99 ? 552 ASP B OD2   1 
ATOM   8295  N  N     . ARG B 1 553 ? 150.299 120.429 124.194 1.00 91.40  ? 553 ARG B N     1 
ATOM   8296  C  CA    . ARG B 1 553 ? 150.644 119.084 123.756 1.00 90.21  ? 553 ARG B CA    1 
ATOM   8297  C  C     . ARG B 1 553 ? 149.408 118.276 123.402 1.00 91.78  ? 553 ARG B C     1 
ATOM   8298  O  O     . ARG B 1 553 ? 149.461 117.424 122.509 1.00 99.49  ? 553 ARG B O     1 
ATOM   8299  C  CB    . ARG B 1 553 ? 151.441 118.367 124.841 1.00 89.73  ? 553 ARG B CB    1 
ATOM   8300  C  CG    . ARG B 1 553 ? 152.798 118.972 125.126 1.00 93.57  ? 553 ARG B CG    1 
ATOM   8301  C  CD    . ARG B 1 553 ? 153.291 118.538 126.489 1.00 97.95  ? 553 ARG B CD    1 
ATOM   8302  N  NE    . ARG B 1 553 ? 154.591 119.108 126.817 1.00 98.61  ? 553 ARG B NE    1 
ATOM   8303  C  CZ    . ARG B 1 553 ? 155.752 118.528 126.551 1.00 97.43  ? 553 ARG B CZ    1 
ATOM   8304  N  NH1   . ARG B 1 553 ? 155.815 117.353 125.947 1.00 96.52  ? 553 ARG B NH1   1 
ATOM   8305  N  NH2   . ARG B 1 553 ? 156.878 119.141 126.902 1.00 98.45  ? 553 ARG B NH2   1 
ATOM   8306  N  N     . VAL B 1 554 ? 148.295 118.513 124.097 1.00 74.95  ? 554 VAL B N     1 
ATOM   8307  C  CA    . VAL B 1 554 ? 147.046 117.853 123.735 1.00 71.54  ? 554 VAL B CA    1 
ATOM   8308  C  C     . VAL B 1 554 ? 146.642 118.245 122.323 1.00 77.53  ? 554 VAL B C     1 
ATOM   8309  O  O     . VAL B 1 554 ? 146.212 117.403 121.525 1.00 85.96  ? 554 VAL B O     1 
ATOM   8310  C  CB    . VAL B 1 554 ? 145.948 118.192 124.757 1.00 77.19  ? 554 VAL B CB    1 
ATOM   8311  C  CG1   . VAL B 1 554 ? 144.691 117.402 124.461 1.00 85.40  ? 554 VAL B CG1   1 
ATOM   8312  C  CG2   . VAL B 1 554 ? 146.438 117.916 126.165 1.00 88.24  ? 554 VAL B CG2   1 
ATOM   8313  N  N     . ALA B 1 555 ? 146.782 119.529 121.990 1.00 77.96  ? 555 ALA B N     1 
ATOM   8314  C  CA    . ALA B 1 555 ? 146.507 119.981 120.632 1.00 77.92  ? 555 ALA B CA    1 
ATOM   8315  C  C     . ALA B 1 555 ? 147.463 119.345 119.632 1.00 76.82  ? 555 ALA B C     1 
ATOM   8316  O  O     . ALA B 1 555 ? 147.051 118.951 118.536 1.00 87.40  ? 555 ALA B O     1 
ATOM   8317  C  CB    . ALA B 1 555 ? 146.588 121.504 120.563 1.00 82.86  ? 555 ALA B CB    1 
ATOM   8318  N  N     . MET B 1 556 ? 148.746 119.236 119.987 1.00 84.36  ? 556 MET B N     1 
ATOM   8319  C  CA    . MET B 1 556 ? 149.710 118.622 119.080 1.00 85.57  ? 556 MET B CA    1 
ATOM   8320  C  C     . MET B 1 556 ? 149.363 117.167 118.803 1.00 81.01  ? 556 MET B C     1 
ATOM   8321  O  O     . MET B 1 556 ? 149.452 116.706 117.660 1.00 95.43  ? 556 MET B O     1 
ATOM   8322  C  CB    . MET B 1 556 ? 151.123 118.731 119.652 1.00 82.06  ? 556 MET B CB    1 
ATOM   8323  C  CG    . MET B 1 556 ? 151.623 120.151 119.821 1.00 80.50  ? 556 MET B CG    1 
ATOM   8324  S  SD    . MET B 1 556 ? 153.083 120.249 120.869 1.00 50.01  ? 556 MET B SD    1 
ATOM   8325  C  CE    . MET B 1 556 ? 154.087 118.950 120.160 1.00 83.22  ? 556 MET B CE    1 
ATOM   8326  N  N     . PHE B 1 557 ? 148.968 116.424 119.836 1.00 76.15  ? 557 PHE B N     1 
ATOM   8327  C  CA    . PHE B 1 557 ? 148.648 115.015 119.642 1.00 85.27  ? 557 PHE B CA    1 
ATOM   8328  C  C     . PHE B 1 557 ? 147.332 114.842 118.897 1.00 85.31  ? 557 PHE B C     1 
ATOM   8329  O  O     . PHE B 1 557 ? 147.196 113.935 118.069 1.00 85.88  ? 557 PHE B O     1 
ATOM   8330  C  CB    . PHE B 1 557 ? 148.606 114.296 120.989 1.00 94.68  ? 557 PHE B CB    1 
ATOM   8331  C  CG    . PHE B 1 557 ? 149.896 114.370 121.753 1.00 92.41  ? 557 PHE B CG    1 
ATOM   8332  C  CD1   . PHE B 1 557 ? 151.109 114.393 121.088 1.00 93.43  ? 557 PHE B CD1   1 
ATOM   8333  C  CD2   . PHE B 1 557 ? 149.896 114.419 123.135 1.00 93.43  ? 557 PHE B CD2   1 
ATOM   8334  C  CE1   . PHE B 1 557 ? 152.297 114.463 121.786 1.00 95.00  ? 557 PHE B CE1   1 
ATOM   8335  C  CE2   . PHE B 1 557 ? 151.081 114.490 123.838 1.00 95.29  ? 557 PHE B CE2   1 
ATOM   8336  C  CZ    . PHE B 1 557 ? 152.283 114.512 123.162 1.00 95.06  ? 557 PHE B CZ    1 
ATOM   8337  N  N     . LEU B 1 558 ? 146.349 115.700 119.176 1.00 83.02  ? 558 LEU B N     1 
ATOM   8338  C  CA    . LEU B 1 558 ? 145.050 115.572 118.527 1.00 81.29  ? 558 LEU B CA    1 
ATOM   8339  C  C     . LEU B 1 558 ? 145.067 116.076 117.090 1.00 83.46  ? 558 LEU B C     1 
ATOM   8340  O  O     . LEU B 1 558 ? 144.323 115.557 116.251 1.00 76.82  ? 558 LEU B O     1 
ATOM   8341  C  CB    . LEU B 1 558 ? 143.986 116.312 119.338 1.00 80.06  ? 558 LEU B CB    1 
ATOM   8342  C  CG    . LEU B 1 558 ? 143.535 115.600 120.616 1.00 82.07  ? 558 LEU B CG    1 
ATOM   8343  C  CD1   . LEU B 1 558 ? 142.242 116.191 121.140 1.00 88.55  ? 558 LEU B CD1   1 
ATOM   8344  C  CD2   . LEU B 1 558 ? 143.380 114.108 120.377 1.00 87.30  ? 558 LEU B CD2   1 
ATOM   8345  N  N     . THR B 1 559 ? 145.891 117.074 116.784 1.00 84.40  ? 559 THR B N     1 
ATOM   8346  C  CA    . THR B 1 559 ? 146.005 117.592 115.427 1.00 70.28  ? 559 THR B CA    1 
ATOM   8347  C  C     . THR B 1 559 ? 147.128 116.940 114.632 1.00 72.52  ? 559 THR B C     1 
ATOM   8348  O  O     . THR B 1 559 ? 147.336 117.311 113.473 1.00 74.97  ? 559 THR B O     1 
ATOM   8349  C  CB    . THR B 1 559 ? 146.219 119.107 115.448 1.00 69.77  ? 559 THR B CB    1 
ATOM   8350  O  OG1   . THR B 1 559 ? 147.432 119.408 116.146 1.00 78.22  ? 559 THR B OG1   1 
ATOM   8351  C  CG2   . THR B 1 559 ? 145.061 119.798 116.138 1.00 80.59  ? 559 THR B CG2   1 
ATOM   8352  N  N     . ASP B 1 560 ? 147.849 115.986 115.222 1.00 94.57  ? 560 ASP B N     1 
ATOM   8353  C  CA    . ASP B 1 560 ? 148.937 115.270 114.556 1.00 89.99  ? 560 ASP B CA    1 
ATOM   8354  C  C     . ASP B 1 560 ? 150.006 116.240 114.046 1.00 92.29  ? 560 ASP B C     1 
ATOM   8355  O  O     . ASP B 1 560 ? 150.287 116.332 112.851 1.00 102.21 ? 560 ASP B O     1 
ATOM   8356  C  CB    . ASP B 1 560 ? 148.400 114.392 113.421 1.00 92.29  ? 560 ASP B CB    1 
ATOM   8357  C  CG    . ASP B 1 560 ? 149.370 113.298 113.020 1.00 99.99  ? 560 ASP B CG    1 
ATOM   8358  O  OD1   . ASP B 1 560 ? 150.542 113.354 113.443 1.00 101.49 ? 560 ASP B OD1   1 
ATOM   8359  O  OD2   . ASP B 1 560 ? 148.960 112.382 112.279 1.00 106.42 ? 560 ASP B OD2   1 
ATOM   8360  N  N     . SER B 1 561 ? 150.605 116.966 114.986 1.00 85.70  ? 561 SER B N     1 
ATOM   8361  C  CA    . SER B 1 561 ? 151.656 117.926 114.672 1.00 82.54  ? 561 SER B CA    1 
ATOM   8362  C  C     . SER B 1 561 ? 152.766 117.785 115.700 1.00 86.74  ? 561 SER B C     1 
ATOM   8363  O  O     . SER B 1 561 ? 152.524 117.946 116.899 1.00 95.99  ? 561 SER B O     1 
ATOM   8364  C  CB    . SER B 1 561 ? 151.112 119.356 114.658 1.00 82.64  ? 561 SER B CB    1 
ATOM   8365  O  OG    . SER B 1 561 ? 150.864 119.819 115.973 1.00 80.24  ? 561 SER B OG    1 
ATOM   8366  N  N     . ASN B 1 562 ? 153.975 117.489 115.235 1.00 101.58 ? 562 ASN B N     1 
ATOM   8367  C  CA    . ASN B 1 562 ? 155.128 117.329 116.119 1.00 97.25  ? 562 ASN B CA    1 
ATOM   8368  C  C     . ASN B 1 562 ? 155.876 118.645 116.300 1.00 93.69  ? 562 ASN B C     1 
ATOM   8369  O  O     . ASN B 1 562 ? 157.093 118.722 116.153 1.00 101.84 ? 562 ASN B O     1 
ATOM   8370  C  CB    . ASN B 1 562 ? 156.051 116.249 115.571 1.00 103.43 ? 562 ASN B CB    1 
ATOM   8371  C  CG    . ASN B 1 562 ? 156.466 116.515 114.141 1.00 103.75 ? 562 ASN B CG    1 
ATOM   8372  O  OD1   . ASN B 1 562 ? 155.883 117.359 113.461 1.00 103.64 ? 562 ASN B OD1   1 
ATOM   8373  N  ND2   . ASN B 1 562 ? 157.480 115.799 113.676 1.00 106.50 ? 562 ASN B ND2   1 
ATOM   8374  N  N     . ASN B 1 563 ? 155.132 119.693 116.640 1.00 86.65  ? 563 ASN B N     1 
ATOM   8375  C  CA    . ASN B 1 563 ? 155.694 121.030 116.768 1.00 90.18  ? 563 ASN B CA    1 
ATOM   8376  C  C     . ASN B 1 563 ? 154.701 121.940 117.474 1.00 88.61  ? 563 ASN B C     1 
ATOM   8377  O  O     . ASN B 1 563 ? 153.530 121.997 117.088 1.00 94.54  ? 563 ASN B O     1 
ATOM   8378  C  CB    . ASN B 1 563 ? 156.050 121.590 115.390 1.00 97.31  ? 563 ASN B CB    1 
ATOM   8379  C  CG    . ASN B 1 563 ? 157.080 122.689 115.455 1.00 100.84 ? 563 ASN B CG    1 
ATOM   8380  O  OD1   . ASN B 1 563 ? 157.369 123.222 116.524 1.00 103.75 ? 563 ASN B OD1   1 
ATOM   8381  N  ND2   . ASN B 1 563 ? 157.640 123.041 114.305 1.00 102.47 ? 563 ASN B ND2   1 
ATOM   8382  N  N     . ILE B 1 564 ? 155.147 122.649 118.510 1.00 89.24  ? 564 ILE B N     1 
ATOM   8383  C  CA    . ILE B 1 564 ? 154.240 123.559 119.199 1.00 86.42  ? 564 ILE B CA    1 
ATOM   8384  C  C     . ILE B 1 564 ? 153.846 124.712 118.286 1.00 89.42  ? 564 ILE B C     1 
ATOM   8385  O  O     . ILE B 1 564 ? 152.700 125.178 118.321 1.00 97.49  ? 564 ILE B O     1 
ATOM   8386  C  CB    . ILE B 1 564 ? 154.868 124.051 120.517 1.00 88.97  ? 564 ILE B CB    1 
ATOM   8387  C  CG1   . ILE B 1 564 ? 153.856 124.873 121.316 1.00 87.13  ? 564 ILE B CG1   1 
ATOM   8388  C  CG2   . ILE B 1 564 ? 156.139 124.842 120.260 1.00 96.24  ? 564 ILE B CG2   1 
ATOM   8389  C  CD1   . ILE B 1 564 ? 154.325 125.236 122.701 1.00 92.18  ? 564 ILE B CD1   1 
ATOM   8390  N  N     . LYS B 1 565 ? 154.767 125.167 117.433 1.00 88.53  ? 565 LYS B N     1 
ATOM   8391  C  CA    . LYS B 1 565 ? 154.486 126.275 116.529 1.00 82.50  ? 565 LYS B CA    1 
ATOM   8392  C  C     . LYS B 1 565 ? 153.328 125.979 115.589 1.00 81.62  ? 565 LYS B C     1 
ATOM   8393  O  O     . LYS B 1 565 ? 152.703 126.917 115.083 1.00 85.21  ? 565 LYS B O     1 
ATOM   8394  C  CB    . LYS B 1 565 ? 155.735 126.615 115.718 1.00 88.79  ? 565 LYS B CB    1 
ATOM   8395  C  CG    . LYS B 1 565 ? 156.867 127.192 116.545 1.00 85.87  ? 565 LYS B CG    1 
ATOM   8396  C  CD    . LYS B 1 565 ? 158.126 127.354 115.717 1.00 88.15  ? 565 LYS B CD    1 
ATOM   8397  C  CE    . LYS B 1 565 ? 159.241 127.983 116.531 1.00 87.76  ? 565 LYS B CE    1 
ATOM   8398  N  NZ    . LYS B 1 565 ? 158.719 128.672 117.741 1.00 91.56  ? 565 LYS B NZ    1 
ATOM   8399  N  N     . GLU B 1 566 ? 153.029 124.704 115.343 1.00 90.55  ? 566 GLU B N     1 
ATOM   8400  C  CA    . GLU B 1 566 ? 151.897 124.365 114.490 1.00 91.69  ? 566 GLU B CA    1 
ATOM   8401  C  C     . GLU B 1 566 ? 150.574 124.703 115.163 1.00 89.60  ? 566 GLU B C     1 
ATOM   8402  O  O     . GLU B 1 566 ? 149.619 125.109 114.492 1.00 93.15  ? 566 GLU B O     1 
ATOM   8403  C  CB    . GLU B 1 566 ? 151.944 122.886 114.118 1.00 89.99  ? 566 GLU B CB    1 
ATOM   8404  C  CG    . GLU B 1 566 ? 153.184 122.490 113.345 1.00 86.17  ? 566 GLU B CG    1 
ATOM   8405  C  CD    . GLU B 1 566 ? 153.010 122.646 111.849 1.00 95.42  ? 566 GLU B CD    1 
ATOM   8406  O  OE1   . GLU B 1 566 ? 153.124 123.785 111.352 1.00 104.54 ? 566 GLU B OE1   1 
ATOM   8407  O  OE2   . GLU B 1 566 ? 152.763 121.629 111.169 1.00 98.07  ? 566 GLU B OE2   1 
ATOM   8408  N  N     . VAL B 1 567 ? 150.494 124.545 116.484 1.00 80.27  ? 567 VAL B N     1 
ATOM   8409  C  CA    . VAL B 1 567 ? 149.247 124.766 117.206 1.00 79.00  ? 567 VAL B CA    1 
ATOM   8410  C  C     . VAL B 1 567 ? 149.221 126.124 117.896 1.00 85.00  ? 567 VAL B C     1 
ATOM   8411  O  O     . VAL B 1 567 ? 148.382 126.354 118.771 1.00 89.05  ? 567 VAL B O     1 
ATOM   8412  C  CB    . VAL B 1 567 ? 148.978 123.635 118.211 1.00 76.95  ? 567 VAL B CB    1 
ATOM   8413  C  CG1   . VAL B 1 567 ? 148.892 122.301 117.490 1.00 79.85  ? 567 VAL B CG1   1 
ATOM   8414  C  CG2   . VAL B 1 567 ? 150.056 123.603 119.276 1.00 78.50  ? 567 VAL B CG2   1 
ATOM   8415  N  N     . LEU B 1 568 ? 150.120 127.026 117.524 1.00 78.42  ? 568 LEU B N     1 
ATOM   8416  C  CA    . LEU B 1 568 ? 150.150 128.381 118.054 1.00 74.64  ? 568 LEU B CA    1 
ATOM   8417  C  C     . LEU B 1 568 ? 149.855 129.355 116.923 1.00 84.31  ? 568 LEU B C     1 
ATOM   8418  O  O     . LEU B 1 568 ? 150.435 129.243 115.838 1.00 92.22  ? 568 LEU B O     1 
ATOM   8419  C  CB    . LEU B 1 568 ? 151.506 128.690 118.688 1.00 71.79  ? 568 LEU B CB    1 
ATOM   8420  C  CG    . LEU B 1 568 ? 151.640 128.371 120.175 1.00 72.54  ? 568 LEU B CG    1 
ATOM   8421  C  CD1   . LEU B 1 568 ? 153.093 128.410 120.593 1.00 78.96  ? 568 LEU B CD1   1 
ATOM   8422  C  CD2   . LEU B 1 568 ? 150.820 129.337 121.005 1.00 81.63  ? 568 LEU B CD2   1 
ATOM   8423  N  N     . LEU B 1 569 ? 148.949 130.300 117.176 1.00 86.96  ? 569 LEU B N     1 
ATOM   8424  C  CA    . LEU B 1 569 ? 148.560 131.246 116.136 1.00 83.54  ? 569 LEU B CA    1 
ATOM   8425  C  C     . LEU B 1 569 ? 149.751 132.077 115.680 1.00 79.16  ? 569 LEU B C     1 
ATOM   8426  O  O     . LEU B 1 569 ? 150.047 132.156 114.483 1.00 88.63  ? 569 LEU B O     1 
ATOM   8427  C  CB    . LEU B 1 569 ? 147.439 132.147 116.649 1.00 81.67  ? 569 LEU B CB    1 
ATOM   8428  C  CG    . LEU B 1 569 ? 146.015 131.620 116.487 1.00 75.31  ? 569 LEU B CG    1 
ATOM   8429  C  CD1   . LEU B 1 569 ? 145.023 132.619 117.037 1.00 80.26  ? 569 LEU B CD1   1 
ATOM   8430  C  CD2   . LEU B 1 569 ? 145.723 131.328 115.033 1.00 86.70  ? 569 LEU B CD2   1 
ATOM   8431  N  N     . PHE B 1 570 ? 150.451 132.698 116.624 1.00 63.00  ? 570 PHE B N     1 
ATOM   8432  C  CA    . PHE B 1 570 ? 151.630 133.513 116.340 1.00 69.19  ? 570 PHE B CA    1 
ATOM   8433  C  C     . PHE B 1 570 ? 152.739 133.080 117.286 1.00 78.48  ? 570 PHE B C     1 
ATOM   8434  O  O     . PHE B 1 570 ? 152.998 133.738 118.302 1.00 79.86  ? 570 PHE B O     1 
ATOM   8435  C  CB    . PHE B 1 570 ? 151.322 135.003 116.482 1.00 78.67  ? 570 PHE B CB    1 
ATOM   8436  C  CG    . PHE B 1 570 ? 150.152 135.462 115.663 1.00 81.04  ? 570 PHE B CG    1 
ATOM   8437  C  CD1   . PHE B 1 570 ? 150.327 135.890 114.359 1.00 87.44  ? 570 PHE B CD1   1 
ATOM   8438  C  CD2   . PHE B 1 570 ? 148.876 135.469 116.197 1.00 80.97  ? 570 PHE B CD2   1 
ATOM   8439  C  CE1   . PHE B 1 570 ? 149.254 136.311 113.605 1.00 82.38  ? 570 PHE B CE1   1 
ATOM   8440  C  CE2   . PHE B 1 570 ? 147.800 135.889 115.447 1.00 83.26  ? 570 PHE B CE2   1 
ATOM   8441  C  CZ    . PHE B 1 570 ? 147.989 136.311 114.150 1.00 74.98  ? 570 PHE B CZ    1 
ATOM   8442  N  N     . PRO B 1 571 ? 153.407 131.969 116.990 1.00 77.55  ? 571 PRO B N     1 
ATOM   8443  C  CA    . PRO B 1 571 ? 154.472 131.495 117.876 1.00 70.92  ? 571 PRO B CA    1 
ATOM   8444  C  C     . PRO B 1 571 ? 155.655 132.446 117.889 1.00 78.49  ? 571 PRO B C     1 
ATOM   8445  O  O     . PRO B 1 571 ? 155.939 133.138 116.909 1.00 84.76  ? 571 PRO B O     1 
ATOM   8446  C  CB    . PRO B 1 571 ? 154.856 130.143 117.271 1.00 71.40  ? 571 PRO B CB    1 
ATOM   8447  C  CG    . PRO B 1 571 ? 154.497 130.270 115.836 1.00 74.08  ? 571 PRO B CG    1 
ATOM   8448  C  CD    . PRO B 1 571 ? 153.271 131.130 115.789 1.00 83.22  ? 571 PRO B CD    1 
ATOM   8449  N  N     . ALA B 1 572 ? 156.347 132.477 119.024 1.00 96.82  ? 572 ALA B N     1 
ATOM   8450  C  CA    . ALA B 1 572 ? 157.536 133.306 119.150 1.00 93.77  ? 572 ALA B CA    1 
ATOM   8451  C  C     . ALA B 1 572 ? 158.657 132.738 118.290 1.00 96.04  ? 572 ALA B C     1 
ATOM   8452  O  O     . ALA B 1 572 ? 158.952 131.541 118.348 1.00 101.20 ? 572 ALA B O     1 
ATOM   8453  C  CB    . ALA B 1 572 ? 157.976 133.391 120.609 1.00 98.32  ? 572 ALA B CB    1 
ATOM   8454  N  N     . MET B 1 573 ? 159.281 133.600 117.494 1.00 112.31 ? 573 MET B N     1 
ATOM   8455  C  CA    . MET B 1 573 ? 160.330 133.191 116.574 1.00 110.59 ? 573 MET B CA    1 
ATOM   8456  C  C     . MET B 1 573 ? 161.576 134.028 116.813 1.00 113.83 ? 573 MET B C     1 
ATOM   8457  O  O     . MET B 1 573 ? 161.497 135.179 117.249 1.00 113.55 ? 573 MET B O     1 
ATOM   8458  C  CB    . MET B 1 573 ? 159.886 133.333 115.111 1.00 114.10 ? 573 MET B CB    1 
ATOM   8459  C  CG    . MET B 1 573 ? 158.469 132.864 114.839 1.00 114.83 ? 573 MET B CG    1 
ATOM   8460  S  SD    . MET B 1 573 ? 158.388 131.101 114.490 1.00 115.10 ? 573 MET B SD    1 
ATOM   8461  C  CE    . MET B 1 573 ? 159.636 130.958 113.216 1.00 120.01 ? 573 MET B CE    1 
ATOM   8462  N  N     . LYS B 1 574 ? 162.727 133.432 116.532 1.00 125.37 ? 574 LYS B N     1 
ATOM   8463  C  CA    . LYS B 1 574 ? 163.983 134.160 116.637 1.00 126.28 ? 574 LYS B CA    1 
ATOM   8464  C  C     . LYS B 1 574 ? 164.016 135.272 115.595 1.00 129.39 ? 574 LYS B C     1 
ATOM   8465  O  O     . LYS B 1 574 ? 163.680 135.030 114.430 1.00 134.27 ? 574 LYS B O     1 
ATOM   8466  C  CB    . LYS B 1 574 ? 165.166 133.216 116.441 1.00 127.06 ? 574 LYS B CB    1 
ATOM   8467  C  CG    . LYS B 1 574 ? 164.943 131.822 116.998 1.00 125.79 ? 574 LYS B CG    1 
ATOM   8468  C  CD    . LYS B 1 574 ? 166.178 131.313 117.718 1.00 125.67 ? 574 LYS B CD    1 
ATOM   8469  C  CE    . LYS B 1 574 ? 165.851 130.114 118.590 1.00 130.50 ? 574 LYS B CE    1 
ATOM   8470  N  NZ    . LYS B 1 574 ? 165.850 128.847 117.809 1.00 129.84 ? 574 LYS B NZ    1 
ATOM   8471  N  N     . PRO B 1 575 ? 164.391 136.493 115.970 1.00 136.63 ? 575 PRO B N     1 
ATOM   8472  C  CA    . PRO B 1 575 ? 164.431 137.583 114.989 1.00 136.78 ? 575 PRO B CA    1 
ATOM   8473  C  C     . PRO B 1 575 ? 165.412 137.285 113.866 1.00 138.23 ? 575 PRO B C     1 
ATOM   8474  O  O     . PRO B 1 575 ? 166.463 136.676 114.077 1.00 136.62 ? 575 PRO B O     1 
ATOM   8475  C  CB    . PRO B 1 575 ? 164.873 138.791 115.821 1.00 135.80 ? 575 PRO B CB    1 
ATOM   8476  C  CG    . PRO B 1 575 ? 164.488 138.439 117.220 1.00 138.94 ? 575 PRO B CG    1 
ATOM   8477  C  CD    . PRO B 1 575 ? 164.706 136.963 117.327 1.00 139.10 ? 575 PRO B CD    1 
ATOM   8478  N  N     . GLU B 1 576 ? 165.056 137.721 112.663 1.00 155.48 ? 576 GLU B N     1 
ATOM   8479  C  CA    . GLU B 1 576 ? 165.838 137.462 111.466 1.00 154.74 ? 576 GLU B CA    1 
ATOM   8480  C  C     . GLU B 1 576 ? 166.544 138.733 111.012 1.00 154.28 ? 576 GLU B C     1 
ATOM   8481  O  O     . GLU B 1 576 ? 166.058 139.846 111.229 1.00 152.95 ? 576 GLU B O     1 
ATOM   8482  C  CB    . GLU B 1 576 ? 164.951 136.928 110.338 1.00 153.48 ? 576 GLU B CB    1 
ATOM   8483  C  CG    . GLU B 1 576 ? 165.610 135.865 109.478 1.00 155.56 ? 576 GLU B CG    1 
ATOM   8484  C  CD    . GLU B 1 576 ? 164.659 135.274 108.458 1.00 154.97 ? 576 GLU B CD    1 
ATOM   8485  O  OE1   . GLU B 1 576 ? 163.509 135.753 108.368 1.00 155.04 ? 576 GLU B OE1   1 
ATOM   8486  O  OE2   . GLU B 1 576 ? 165.060 134.329 107.746 1.00 154.82 ? 576 GLU B OE2   1 
ATOM   8487  N  N     . ASP B 1 577 ? 167.698 138.554 110.379 1.00 161.52 ? 577 ASP B N     1 
ATOM   8488  C  CA    . ASP B 1 577 ? 168.485 139.678 109.886 1.00 160.29 ? 577 ASP B CA    1 
ATOM   8489  C  C     . ASP B 1 577 ? 168.054 140.074 108.478 1.00 161.89 ? 577 ASP B C     1 
ATOM   8490  O  O     . ASP B 1 577 ? 168.240 141.216 108.060 1.00 162.42 ? 577 ASP B O     1 
ATOM   8491  C  CB    . ASP B 1 577 ? 169.976 139.338 109.905 1.00 162.17 ? 577 ASP B CB    1 
ATOM   8492  C  CG    . ASP B 1 577 ? 170.478 138.999 111.294 1.00 163.53 ? 577 ASP B CG    1 
ATOM   8493  O  OD1   . ASP B 1 577 ? 169.674 139.052 112.248 1.00 163.82 ? 577 ASP B OD1   1 
ATOM   8494  O  OD2   . ASP B 1 577 ? 171.678 138.679 111.432 1.00 163.17 ? 577 ASP B OD2   1 
ATOM   8495  P  P     . G   C 2 1   ? 156.180 159.655 142.493 1.00 76.88  ? 1   G   C P     1 
ATOM   8496  O  OP1   . G   C 2 1   ? 157.668 159.762 142.240 1.00 78.59  ? 1   G   C OP1   1 
ATOM   8497  O  OP2   . G   C 2 1   ? 155.837 159.636 143.968 1.00 75.20  ? 1   G   C OP2   1 
ATOM   8498  O  "O5'" . G   C 2 1   ? 155.544 161.016 141.912 1.00 78.76  ? 1   G   C "O5'" 1 
ATOM   8499  C  "C5'" . G   C 2 1   ? 156.402 161.927 141.186 1.00 77.93  ? 1   G   C "C5'" 1 
ATOM   8500  C  "C4'" . G   C 2 1   ? 155.619 163.166 140.834 1.00 78.66  ? 1   G   C "C4'" 1 
ATOM   8501  O  "O4'" . G   C 2 1   ? 154.646 162.844 139.810 1.00 79.49  ? 1   G   C "O4'" 1 
ATOM   8502  C  "C3'" . G   C 2 1   ? 154.804 163.775 141.975 1.00 78.23  ? 1   G   C "C3'" 1 
ATOM   8503  O  "O3'" . G   C 2 1   ? 155.597 164.683 142.724 1.00 77.17  ? 1   G   C "O3'" 1 
ATOM   8504  C  "C2'" . G   C 2 1   ? 153.687 164.489 141.216 1.00 79.34  ? 1   G   C "C2'" 1 
ATOM   8505  O  "O2'" . G   C 2 1   ? 154.085 165.758 140.752 1.00 79.34  ? 1   G   C "O2'" 1 
ATOM   8506  C  "C1'" . G   C 2 1   ? 153.451 163.556 140.034 1.00 78.22  ? 1   G   C "C1'" 1 
ATOM   8507  N  N9    . G   C 2 1   ? 152.373 162.595 140.227 1.00 20.00  ? 1   G   C N9    1 
ATOM   8508  C  C8    . G   C 2 1   ? 152.507 161.242 140.400 1.00 20.00  ? 1   G   C C8    1 
ATOM   8509  N  N7    . G   C 2 1   ? 151.360 160.619 140.509 1.00 20.00  ? 1   G   C N7    1 
ATOM   8510  C  C5    . G   C 2 1   ? 150.412 161.623 140.375 1.00 20.00  ? 1   G   C C5    1 
ATOM   8511  C  C6    . G   C 2 1   ? 149.000 161.549 140.408 1.00 20.00  ? 1   G   C C6    1 
ATOM   8512  O  O6    . G   C 2 1   ? 148.289 160.549 140.571 1.00 20.00  ? 1   G   C O6    1 
ATOM   8513  N  N1    . G   C 2 1   ? 148.422 162.804 140.232 1.00 20.00  ? 1   G   C N1    1 
ATOM   8514  C  C2    . G   C 2 1   ? 149.112 163.975 140.051 1.00 20.00  ? 1   G   C C2    1 
ATOM   8515  N  N2    . G   C 2 1   ? 148.380 165.085 139.901 1.00 20.00  ? 1   G   C N2    1 
ATOM   8516  N  N3    . G   C 2 1   ? 150.440 164.051 140.020 1.00 20.00  ? 1   G   C N3    1 
ATOM   8517  C  C4    . G   C 2 1   ? 151.022 162.840 140.176 1.00 20.00  ? 1   G   C C4    1 
ATOM   8518  P  P     . C   C 2 2   ? 155.250 165.021 144.254 1.00 116.37 ? 2   C   C P     1 
ATOM   8519  O  OP1   . C   C 2 2   ? 156.246 165.978 144.866 1.00 117.69 ? 2   C   C OP1   1 
ATOM   8520  O  OP2   . C   C 2 2   ? 155.009 163.777 145.081 1.00 127.23 ? 2   C   C OP2   1 
ATOM   8521  O  "O5'" . C   C 2 2   ? 153.853 165.806 144.166 1.00 121.51 ? 2   C   C "O5'" 1 
ATOM   8522  C  "C5'" . C   C 2 2   ? 153.831 167.115 143.558 1.00 123.77 ? 2   C   C "C5'" 1 
ATOM   8523  C  "C4'" . C   C 2 2   ? 152.416 167.624 143.587 1.00 120.18 ? 2   C   C "C4'" 1 
ATOM   8524  O  "O4'" . C   C 2 2   ? 151.593 166.856 142.675 1.00 119.53 ? 2   C   C "O4'" 1 
ATOM   8525  C  "C3'" . C   C 2 2   ? 151.699 167.466 144.929 1.00 119.76 ? 2   C   C "C3'" 1 
ATOM   8526  O  "O3'" . C   C 2 2   ? 152.081 168.483 145.845 1.00 120.96 ? 2   C   C "O3'" 1 
ATOM   8527  C  "C2'" . C   C 2 2   ? 150.243 167.575 144.481 1.00 122.15 ? 2   C   C "C2'" 1 
ATOM   8528  O  "O2'" . C   C 2 2   ? 149.872 168.896 144.158 1.00 128.99 ? 2   C   C "O2'" 1 
ATOM   8529  C  "C1'" . C   C 2 2   ? 150.278 166.773 143.180 1.00 119.68 ? 2   C   C "C1'" 1 
ATOM   8530  N  N1    . C   C 2 2   ? 149.929 165.344 143.373 1.00 118.51 ? 2   C   C N1    1 
ATOM   8531  C  C2    . C   C 2 2   ? 148.580 164.997 143.371 1.00 121.72 ? 2   C   C C2    1 
ATOM   8532  O  O2    . C   C 2 2   ? 147.735 165.893 143.241 1.00 124.17 ? 2   C   C O2    1 
ATOM   8533  N  N3    . C   C 2 2   ? 148.239 163.701 143.536 1.00 124.55 ? 2   C   C N3    1 
ATOM   8534  C  C4    . C   C 2 2   ? 149.183 162.768 143.682 1.00 124.76 ? 2   C   C C4    1 
ATOM   8535  N  N4    . C   C 2 2   ? 148.790 161.515 143.835 1.00 124.86 ? 2   C   C N4    1 
ATOM   8536  C  C5    . C   C 2 2   ? 150.561 163.101 143.672 1.00 127.23 ? 2   C   C C5    1 
ATOM   8537  C  C6    . C   C 2 2   ? 150.888 164.390 143.510 1.00 125.38 ? 2   C   C C6    1 
ATOM   8538  P  P     . C   C 2 3   ? 151.845 168.310 147.424 1.00 106.18 ? 3   C   C P     1 
ATOM   8539  O  OP1   . C   C 2 3   ? 152.351 169.500 148.211 1.00 117.60 ? 3   C   C OP1   1 
ATOM   8540  O  OP2   . C   C 2 3   ? 152.353 166.976 147.928 1.00 109.73 ? 3   C   C OP2   1 
ATOM   8541  O  "O5'" . C   C 2 3   ? 150.247 168.290 147.587 1.00 118.56 ? 3   C   C "O5'" 1 
ATOM   8542  C  "C5'" . C   C 2 3   ? 149.497 169.484 147.265 1.00 114.76 ? 3   C   C "C5'" 1 
ATOM   8543  C  "C4'" . C   C 2 3   ? 148.030 169.192 147.443 1.00 113.75 ? 3   C   C "C4'" 1 
ATOM   8544  O  "O4'" . C   C 2 3   ? 147.611 168.174 146.498 1.00 111.39 ? 3   C   C "O4'" 1 
ATOM   8545  C  "C3'" . C   C 2 3   ? 147.637 168.611 148.804 1.00 118.13 ? 3   C   C "C3'" 1 
ATOM   8546  O  "O3'" . C   C 2 3   ? 147.528 169.633 149.785 1.00 110.26 ? 3   C   C "O3'" 1 
ATOM   8547  C  "C2'" . C   C 2 3   ? 146.301 167.949 148.463 1.00 116.37 ? 3   C   C "C2'" 1 
ATOM   8548  O  "O2'" . C   C 2 3   ? 145.247 168.875 148.325 1.00 116.61 ? 3   C   C "O2'" 1 
ATOM   8549  C  "C1'" . C   C 2 3   ? 146.602 167.374 147.077 1.00 109.36 ? 3   C   C "C1'" 1 
ATOM   8550  N  N1    . C   C 2 3   ? 147.072 165.965 147.118 1.00 109.87 ? 3   C   C N1    1 
ATOM   8551  C  C2    . C   C 2 3   ? 146.109 164.959 147.178 1.00 113.27 ? 3   C   C C2    1 
ATOM   8552  O  O2    . C   C 2 3   ? 144.915 165.285 147.230 1.00 112.32 ? 3   C   C O2    1 
ATOM   8553  N  N3    . C   C 2 3   ? 146.509 163.668 147.201 1.00 114.95 ? 3   C   C N3    1 
ATOM   8554  C  C4    . C   C 2 3   ? 147.810 163.364 147.147 1.00 111.44 ? 3   C   C C4    1 
ATOM   8555  N  N4    . C   C 2 3   ? 148.145 162.084 147.170 1.00 113.25 ? 3   C   C N4    1 
ATOM   8556  C  C5    . C   C 2 3   ? 148.804 164.375 147.071 1.00 112.65 ? 3   C   C C5    1 
ATOM   8557  C  C6    . C   C 2 3   ? 148.395 165.651 147.052 1.00 113.58 ? 3   C   C C6    1 
ATOM   8558  P  P     . C   C 2 4   ? 147.683 169.290 151.346 1.00 95.42  ? 4   C   C P     1 
ATOM   8559  O  OP1   . C   C 2 4   ? 147.658 170.527 152.214 1.00 109.09 ? 4   C   C OP1   1 
ATOM   8560  O  OP2   . C   C 2 4   ? 148.865 168.380 151.604 1.00 108.65 ? 4   C   C OP2   1 
ATOM   8561  O  "O5'" . C   C 2 4   ? 146.359 168.448 151.695 1.00 100.66 ? 4   C   C "O5'" 1 
ATOM   8562  C  "C5'" . C   C 2 4   ? 145.076 169.107 151.595 1.00 106.40 ? 4   C   C "C5'" 1 
ATOM   8563  C  "C4'" . C   C 2 4   ? 143.991 168.097 151.861 1.00 104.08 ? 4   C   C "C4'" 1 
ATOM   8564  O  "O4'" . C   C 2 4   ? 144.002 167.076 150.833 1.00 106.00 ? 4   C   C "O4'" 1 
ATOM   8565  C  "C3'" . C   C 2 4   ? 144.141 167.299 153.158 1.00 102.39 ? 4   C   C "C3'" 1 
ATOM   8566  O  "O3'" . C   C 2 4   ? 143.719 168.080 154.268 1.00 114.04 ? 4   C   C "O3'" 1 
ATOM   8567  C  "C2'" . C   C 2 4   ? 143.245 166.093 152.861 1.00 99.20  ? 4   C   C "C2'" 1 
ATOM   8568  O  "O2'" . C   C 2 4   ? 141.875 166.383 153.026 1.00 107.30 ? 4   C   C "O2'" 1 
ATOM   8569  C  "C1'" . C   C 2 4   ? 143.518 165.864 151.371 1.00 99.64  ? 4   C   C "C1'" 1 
ATOM   8570  N  N1    . C   C 2 4   ? 144.522 164.798 151.124 1.00 99.04  ? 4   C   C N1    1 
ATOM   8571  C  C2    . C   C 2 4   ? 144.071 163.481 151.064 1.00 101.48 ? 4   C   C C2    1 
ATOM   8572  O  O2    . C   C 2 4   ? 142.862 163.262 151.231 1.00 97.73  ? 4   C   C O2    1 
ATOM   8573  N  N3    . C   C 2 4   ? 144.963 162.490 150.840 1.00 106.57 ? 4   C   C N3    1 
ATOM   8574  C  C4    . C   C 2 4   ? 146.257 162.776 150.667 1.00 104.06 ? 4   C   C C4    1 
ATOM   8575  N  N4    . C   C 2 4   ? 147.086 161.769 150.447 1.00 106.82 ? 4   C   C N4    1 
ATOM   8576  C  C5    . C   C 2 4   ? 146.733 164.113 150.717 1.00 106.42 ? 4   C   C C5    1 
ATOM   8577  C  C6    . C   C 2 4   ? 145.840 165.086 150.941 1.00 108.40 ? 4   C   C C6    1 
ATOM   8578  P  P     . G   C 2 5   ? 144.167 167.698 155.761 1.00 81.59  ? 5   G   C P     1 
ATOM   8579  O  OP1   . G   C 2 5   ? 143.777 168.752 156.774 1.00 99.60  ? 5   G   C OP1   1 
ATOM   8580  O  OP2   . G   C 2 5   ? 145.618 167.274 155.839 1.00 86.70  ? 5   G   C OP2   1 
ATOM   8581  O  "O5'" . G   C 2 5   ? 143.278 166.393 156.058 1.00 90.00  ? 5   G   C "O5'" 1 
ATOM   8582  C  "C5'" . G   C 2 5   ? 143.948 165.161 156.402 1.00 96.47  ? 5   G   C "C5'" 1 
ATOM   8583  C  "C4'" . G   C 2 5   ? 142.943 164.039 156.394 1.00 96.10  ? 5   G   C "C4'" 1 
ATOM   8584  O  "O4'" . G   C 2 5   ? 142.842 163.495 155.053 1.00 94.73  ? 5   G   C "O4'" 1 
ATOM   8585  C  "C3'" . G   C 2 5   ? 143.289 162.838 157.279 1.00 98.90  ? 5   G   C "C3'" 1 
ATOM   8586  O  "O3'" . G   C 2 5   ? 142.820 163.029 158.606 1.00 95.45  ? 5   G   C "O3'" 1 
ATOM   8587  C  "C2'" . G   C 2 5   ? 142.564 161.710 156.548 1.00 100.01 ? 5   G   C "C2'" 1 
ATOM   8588  O  "O2'" . G   C 2 5   ? 141.174 161.704 156.785 1.00 98.48  ? 5   G   C "O2'" 1 
ATOM   8589  C  "C1'" . G   C 2 5   ? 142.863 162.087 155.105 1.00 88.48  ? 5   G   C "C1'" 1 
ATOM   8590  N  N9    . G   C 2 5   ? 144.163 161.627 154.643 1.00 79.31  ? 5   G   C N9    1 
ATOM   8591  C  C8    . G   C 2 5   ? 145.263 162.399 154.372 1.00 91.38  ? 5   G   C C8    1 
ATOM   8592  N  N7    . G   C 2 5   ? 146.290 161.704 153.954 1.00 93.07  ? 5   G   C N7    1 
ATOM   8593  C  C5    . G   C 2 5   ? 145.829 160.395 153.932 1.00 85.83  ? 5   G   C C5    1 
ATOM   8594  C  C6    . G   C 2 5   ? 146.496 159.205 153.560 1.00 93.39  ? 5   G   C C6    1 
ATOM   8595  O  O6    . G   C 2 5   ? 147.661 159.072 153.162 1.00 97.51  ? 5   G   C O6    1 
ATOM   8596  N  N1    . G   C 2 5   ? 145.661 158.096 153.688 1.00 98.04  ? 5   G   C N1    1 
ATOM   8597  C  C2    . G   C 2 5   ? 144.357 158.129 154.114 1.00 95.90  ? 5   G   C C2    1 
ATOM   8598  N  N2    . G   C 2 5   ? 143.711 156.958 154.171 1.00 95.43  ? 5   G   C N2    1 
ATOM   8599  N  N3    . G   C 2 5   ? 143.726 159.247 154.462 1.00 91.73  ? 5   G   C N3    1 
ATOM   8600  C  C4    . G   C 2 5   ? 144.516 160.337 154.335 1.00 81.97  ? 5   G   C C4    1 
ATOM   8601  P  P     . G   C 2 6   ? 143.624 162.413 159.851 1.00 83.01  ? 6   G   C P     1 
ATOM   8602  O  OP1   . G   C 2 6   ? 142.969 162.738 161.173 1.00 100.75 ? 6   G   C OP1   1 
ATOM   8603  O  OP2   . G   C 2 6   ? 145.097 162.746 159.797 1.00 84.97  ? 6   G   C OP2   1 
ATOM   8604  O  "O5'" . G   C 2 6   ? 143.494 160.826 159.636 1.00 92.77  ? 6   G   C "O5'" 1 
ATOM   8605  C  "C5'" . G   C 2 6   ? 142.190 160.222 159.775 1.00 88.00  ? 6   G   C "C5'" 1 
ATOM   8606  C  "C4'" . G   C 2 6   ? 142.301 158.746 159.499 1.00 89.17  ? 6   G   C "C4'" 1 
ATOM   8607  O  "O4'" . G   C 2 6   ? 142.854 158.543 158.176 1.00 91.37  ? 6   G   C "O4'" 1 
ATOM   8608  C  "C3'" . G   C 2 6   ? 143.249 157.961 160.406 1.00 100.08 ? 6   G   C "C3'" 1 
ATOM   8609  O  "O3'" . G   C 2 6   ? 142.637 157.616 161.639 1.00 87.39  ? 6   G   C "O3'" 1 
ATOM   8610  C  "C2'" . G   C 2 6   ? 143.508 156.725 159.547 1.00 99.48  ? 6   G   C "C2'" 1 
ATOM   8611  O  "O2'" . G   C 2 6   ? 142.461 155.785 159.626 1.00 103.50 ? 6   G   C "O2'" 1 
ATOM   8612  C  "C1'" . G   C 2 6   ? 143.558 157.322 158.146 1.00 86.12  ? 6   G   C "C1'" 1 
ATOM   8613  N  N9    . G   C 2 6   ? 144.904 157.569 157.648 1.00 80.78  ? 6   G   C N9    1 
ATOM   8614  C  C8    . G   C 2 6   ? 145.525 158.781 157.500 1.00 89.08  ? 6   G   C C8    1 
ATOM   8615  N  N7    . G   C 2 6   ? 146.727 158.685 156.988 1.00 95.10  ? 6   G   C N7    1 
ATOM   8616  C  C5    . G   C 2 6   ? 146.895 157.325 156.764 1.00 91.68  ? 6   G   C C5    1 
ATOM   8617  C  C6    . G   C 2 6   ? 147.995 156.618 156.222 1.00 86.65  ? 6   G   C C6    1 
ATOM   8618  O  O6    . G   C 2 6   ? 149.076 157.070 155.823 1.00 91.85  ? 6   G   C O6    1 
ATOM   8619  N  N1    . G   C 2 6   ? 147.749 155.248 156.179 1.00 80.03  ? 6   G   C N1    1 
ATOM   8620  C  C2    . G   C 2 6   ? 146.596 154.637 156.599 1.00 86.70  ? 6   G   C C2    1 
ATOM   8621  N  N2    . G   C 2 6   ? 146.542 153.305 156.473 1.00 86.74  ? 6   G   C N2    1 
ATOM   8622  N  N3    . G   C 2 6   ? 145.557 155.295 157.106 1.00 94.65  ? 6   G   C N3    1 
ATOM   8623  C  C4    . G   C 2 6   ? 145.773 156.630 157.150 1.00 89.75  ? 6   G   C C4    1 
ATOM   8624  P  P     . A   C 2 7   ? 143.529 157.321 162.939 1.00 61.24  ? 7   A   C P     1 
ATOM   8625  O  OP1   . A   C 2 7   ? 142.692 157.073 164.170 1.00 87.81  ? 7   A   C OP1   1 
ATOM   8626  O  OP2   . A   C 2 7   ? 144.591 158.381 163.123 1.00 95.21  ? 7   A   C OP2   1 
ATOM   8627  O  "O5'" . A   C 2 7   ? 144.294 155.949 162.615 1.00 89.99  ? 7   A   C "O5'" 1 
ATOM   8628  C  "C5'" . A   C 2 7   ? 143.533 154.721 162.548 1.00 99.24  ? 7   A   C "C5'" 1 
ATOM   8629  C  "C4'" . A   C 2 7   ? 144.417 153.640 161.982 1.00 93.45  ? 7   A   C "C4'" 1 
ATOM   8630  O  "O4'" . A   C 2 7   ? 145.153 154.193 160.863 1.00 82.54  ? 7   A   C "O4'" 1 
ATOM   8631  C  "C3'" . A   C 2 7   ? 145.472 153.070 162.939 1.00 97.63  ? 7   A   C "C3'" 1 
ATOM   8632  O  "O3'" . A   C 2 7   ? 145.592 151.659 162.831 1.00 88.03  ? 7   A   C "O3'" 1 
ATOM   8633  C  "C2'" . A   C 2 7   ? 146.774 153.731 162.488 1.00 91.89  ? 7   A   C "C2'" 1 
ATOM   8634  O  "O2'" . A   C 2 7   ? 147.893 152.901 162.704 1.00 104.79 ? 7   A   C "O2'" 1 
ATOM   8635  C  "C1'" . A   C 2 7   ? 146.530 153.947 161.002 1.00 83.13  ? 7   A   C "C1'" 1 
ATOM   8636  N  N9    . A   C 2 7   ? 147.262 155.096 160.493 1.00 88.24  ? 7   A   C N9    1 
ATOM   8637  C  C8    . A   C 2 7   ? 146.956 156.417 160.692 1.00 91.71  ? 7   A   C C8    1 
ATOM   8638  N  N7    . A   C 2 7   ? 147.825 157.237 160.160 1.00 94.37  ? 7   A   C N7    1 
ATOM   8639  C  C5    . A   C 2 7   ? 148.774 156.404 159.591 1.00 97.50  ? 7   A   C C5    1 
ATOM   8640  C  C6    . A   C 2 7   ? 149.954 156.668 158.875 1.00 99.22  ? 7   A   C C6    1 
ATOM   8641  N  N6    . A   C 2 7   ? 150.387 157.891 158.588 1.00 97.81  ? 7   A   C N6    1 
ATOM   8642  N  N1    . A   C 2 7   ? 150.672 155.605 158.447 1.00 94.70  ? 7   A   C N1    1 
ATOM   8643  C  C2    . A   C 2 7   ? 150.228 154.375 158.729 1.00 92.40  ? 7   A   C C2    1 
ATOM   8644  N  N3    . A   C 2 7   ? 149.138 154.008 159.393 1.00 95.09  ? 7   A   C N3    1 
ATOM   8645  C  C4    . A   C 2 7   ? 148.449 155.081 159.808 1.00 95.70  ? 7   A   C C4    1 
ATOM   8646  P  P     . U   C 2 8   ? 144.675 150.686 163.715 1.00 48.52  ? 8   U   C P     1 
ATOM   8647  O  OP1   . U   C 2 8   ? 145.130 149.254 163.602 1.00 86.47  ? 8   U   C OP1   1 
ATOM   8648  O  OP2   . U   C 2 8   ? 143.198 150.879 163.474 1.00 71.78  ? 8   U   C OP2   1 
ATOM   8649  O  "O5'" . U   C 2 8   ? 144.966 151.155 165.224 1.00 80.99  ? 8   U   C "O5'" 1 
ATOM   8650  C  "C5'" . U   C 2 8   ? 146.302 151.018 165.762 1.00 85.58  ? 8   U   C "C5'" 1 
ATOM   8651  C  "C4'" . U   C 2 8   ? 146.213 150.898 167.263 1.00 83.62  ? 8   U   C "C4'" 1 
ATOM   8652  O  "O4'" . U   C 2 8   ? 145.711 152.131 167.843 1.00 82.52  ? 8   U   C "O4'" 1 
ATOM   8653  C  "C3'" . U   C 2 8   ? 145.225 149.850 167.782 1.00 87.56  ? 8   U   C "C3'" 1 
ATOM   8654  O  "O3'" . U   C 2 8   ? 145.721 148.524 167.702 1.00 82.55  ? 8   U   C "O3'" 1 
ATOM   8655  C  "C2'" . U   C 2 8   ? 145.055 150.331 169.222 1.00 90.52  ? 8   U   C "C2'" 1 
ATOM   8656  O  "O2'" . U   C 2 8   ? 146.204 150.098 170.006 1.00 90.03  ? 8   U   C "O2'" 1 
ATOM   8657  C  "C1'" . U   C 2 8   ? 144.915 151.829 168.972 1.00 82.97  ? 8   U   C "C1'" 1 
ATOM   8658  N  N1    . U   C 2 8   ? 143.521 152.218 168.691 1.00 85.49  ? 8   U   C N1    1 
ATOM   8659  C  C2    . U   C 2 8   ? 142.705 152.462 169.777 1.00 93.34  ? 8   U   C C2    1 
ATOM   8660  O  O2    . U   C 2 8   ? 143.089 152.356 170.932 1.00 84.38  ? 8   U   C O2    1 
ATOM   8661  N  N3    . U   C 2 8   ? 141.423 152.824 169.462 1.00 97.26  ? 8   U   C N3    1 
ATOM   8662  C  C4    . U   C 2 8   ? 140.883 152.970 168.201 1.00 87.83  ? 8   U   C C4    1 
ATOM   8663  O  O4    . U   C 2 8   ? 139.704 153.302 168.083 1.00 80.82  ? 8   U   C O4    1 
ATOM   8664  C  C5    . U   C 2 8   ? 141.793 152.705 167.128 1.00 83.71  ? 8   U   C C5    1 
ATOM   8665  C  C6    . U   C 2 8   ? 143.055 152.351 167.406 1.00 83.74  ? 8   U   C C6    1 
ATOM   8666  P  P     . A   C 2 9   ? 144.699 147.294 167.799 1.00 12.25  ? 9   A   C P     1 
ATOM   8667  O  OP1   . A   C 2 9   ? 144.893 146.312 166.672 1.00 63.62  ? 9   A   C OP1   1 
ATOM   8668  O  OP2   . A   C 2 9   ? 143.270 147.743 167.980 1.00 62.47  ? 9   A   C OP2   1 
ATOM   8669  O  "O5'" . A   C 2 9   ? 145.152 146.567 169.156 1.00 86.18  ? 9   A   C "O5'" 1 
ATOM   8670  C  "C5'" . A   C 2 9   ? 146.368 145.785 169.156 1.00 88.80  ? 9   A   C "C5'" 1 
ATOM   8671  C  "C4'" . A   C 2 9   ? 146.073 144.443 169.774 1.00 85.16  ? 9   A   C "C4'" 1 
ATOM   8672  O  "O4'" . A   C 2 9   ? 145.480 144.655 171.080 1.00 68.77  ? 9   A   C "O4'" 1 
ATOM   8673  C  "C3'" . A   C 2 9   ? 145.083 143.560 169.004 1.00 77.93  ? 9   A   C "C3'" 1 
ATOM   8674  O  "O3'" . A   C 2 9   ? 145.492 142.201 168.980 1.00 71.68  ? 9   A   C "O3'" 1 
ATOM   8675  C  "C2'" . A   C 2 9   ? 143.787 143.711 169.803 1.00 69.84  ? 9   A   C "C2'" 1 
ATOM   8676  O  "O2'" . A   C 2 9   ? 142.941 142.592 169.691 1.00 78.20  ? 9   A   C "O2'" 1 
ATOM   8677  C  "C1'" . A   C 2 9   ? 144.321 143.873 171.218 1.00 63.72  ? 9   A   C "C1'" 1 
ATOM   8678  N  N9    . A   C 2 9   ? 143.396 144.578 172.091 1.00 77.15  ? 9   A   C N9    1 
ATOM   8679  C  C8    . A   C 2 9   ? 142.230 145.188 171.709 1.00 81.90  ? 9   A   C C8    1 
ATOM   8680  N  N7    . A   C 2 9   ? 141.575 145.724 172.705 1.00 71.95  ? 9   A   C N7    1 
ATOM   8681  C  C5    . A   C 2 9   ? 142.348 145.438 173.818 1.00 74.83  ? 9   A   C C5    1 
ATOM   8682  C  C6    . A   C 2 9   ? 142.184 145.738 175.181 1.00 75.29  ? 9   A   C C6    1 
ATOM   8683  N  N6    . A   C 2 9   ? 141.153 146.421 175.666 1.00 77.93  ? 9   A   C N6    1 
ATOM   8684  N  N1    . A   C 2 9   ? 143.141 145.307 176.033 1.00 81.93  ? 9   A   C N1    1 
ATOM   8685  C  C2    . A   C 2 9   ? 144.175 144.622 175.534 1.00 91.29  ? 9   A   C C2    1 
ATOM   8686  N  N3    . A   C 2 9   ? 144.432 144.280 174.276 1.00 84.31  ? 9   A   C N3    1 
ATOM   8687  C  C4    . A   C 2 9   ? 143.462 144.710 173.456 1.00 76.54  ? 9   A   C C4    1 
HETATM 8688  P  P     . 2MG C 2 10  ? 146.820 141.734 168.207 1.00 35.94  ? 10  2MG C P     1 
HETATM 8689  O  OP1   . 2MG C 2 10  ? 147.715 140.923 169.114 1.00 77.20  ? 10  2MG C OP1   1 
HETATM 8690  O  OP2   . 2MG C 2 10  ? 147.542 142.835 167.471 1.00 70.51  ? 10  2MG C OP2   1 
HETATM 8691  O  "O5'" . 2MG C 2 10  ? 146.260 140.732 167.084 1.00 75.01  ? 10  2MG C "O5'" 1 
HETATM 8692  C  "C5'" . 2MG C 2 10  ? 145.294 141.230 166.130 1.00 88.84  ? 10  2MG C "C5'" 1 
HETATM 8693  C  "C4'" . 2MG C 2 10  ? 144.579 140.068 165.487 1.00 85.71  ? 10  2MG C "C4'" 1 
HETATM 8694  O  "O4'" . 2MG C 2 10  ? 144.575 138.949 166.408 1.00 89.42  ? 10  2MG C "O4'" 1 
HETATM 8695  C  "C3'" . 2MG C 2 10  ? 143.112 140.315 165.114 1.00 80.52  ? 10  2MG C "C3'" 1 
HETATM 8696  O  "O3'" . 2MG C 2 10  ? 143.014 140.615 163.727 1.00 84.47  ? 10  2MG C "O3'" 1 
HETATM 8697  C  "C2'" . 2MG C 2 10  ? 142.419 139.001 165.490 1.00 86.55  ? 10  2MG C "C2'" 1 
HETATM 8698  O  "O2'" . 2MG C 2 10  ? 142.419 138.062 164.439 1.00 88.88  ? 10  2MG C "O2'" 1 
HETATM 8699  C  "C1'" . 2MG C 2 10  ? 143.262 138.511 166.663 1.00 83.10  ? 10  2MG C "C1'" 1 
HETATM 8700  N  N9    . 2MG C 2 10  ? 142.855 139.036 167.962 1.00 72.18  ? 10  2MG C N9    1 
HETATM 8701  C  C8    . 2MG C 2 10  ? 143.694 139.522 168.930 1.00 84.76  ? 10  2MG C C8    1 
HETATM 8702  N  N7    . 2MG C 2 10  ? 143.067 139.950 169.996 1.00 91.33  ? 10  2MG C N7    1 
HETATM 8703  C  C5    . 2MG C 2 10  ? 141.727 139.737 169.712 1.00 78.00  ? 10  2MG C C5    1 
HETATM 8704  C  C6    . 2MG C 2 10  ? 140.578 140.006 170.496 1.00 85.45  ? 10  2MG C C6    1 
HETATM 8705  O  O6    . 2MG C 2 10  ? 140.526 140.499 171.630 1.00 82.35  ? 10  2MG C O6    1 
HETATM 8706  N  N1    . 2MG C 2 10  ? 139.407 139.636 169.835 1.00 90.60  ? 10  2MG C N1    1 
HETATM 8707  C  C2    . 2MG C 2 10  ? 139.362 139.083 168.584 1.00 82.80  ? 10  2MG C C2    1 
HETATM 8708  N  N2    . 2MG C 2 10  ? 138.151 138.787 168.093 1.00 73.37  ? 10  2MG C N2    1 
HETATM 8709  C  CM2   . 2MG C 2 10  ? 138.009 137.972 166.904 1.00 87.57  ? 10  2MG C CM2   1 
HETATM 8710  N  N3    . 2MG C 2 10  ? 140.427 138.832 167.850 1.00 90.10  ? 10  2MG C N3    1 
HETATM 8711  C  C4    . 2MG C 2 10  ? 141.581 139.189 168.457 1.00 78.26  ? 10  2MG C C4    1 
ATOM   8712  P  P     . C   C 2 11  ? 142.731 142.112 163.217 1.00 61.79  ? 11  C   C P     1 
ATOM   8713  O  OP1   . C   C 2 11  ? 143.230 142.367 161.817 1.00 102.71 ? 11  C   C OP1   1 
ATOM   8714  O  OP2   . C   C 2 11  ? 143.143 143.164 164.216 1.00 73.38  ? 11  C   C OP2   1 
ATOM   8715  O  "O5'" . C   C 2 11  ? 141.131 142.145 163.157 1.00 92.36  ? 11  C   C "O5'" 1 
ATOM   8716  C  "C5'" . C   C 2 11  ? 140.442 141.142 162.374 1.00 91.58  ? 11  C   C "C5'" 1 
ATOM   8717  C  "C4'" . C   C 2 11  ? 138.995 141.141 162.788 1.00 86.80  ? 11  C   C "C4'" 1 
ATOM   8718  O  "O4'" . C   C 2 11  ? 138.870 140.515 164.090 1.00 79.19  ? 11  C   C "O4'" 1 
ATOM   8719  C  "C3'" . C   C 2 11  ? 138.371 142.528 162.971 1.00 89.84  ? 11  C   C "C3'" 1 
ATOM   8720  O  "O3'" . C   C 2 11  ? 137.894 143.044 161.737 1.00 75.14  ? 11  C   C "O3'" 1 
ATOM   8721  C  "C2'" . C   C 2 11  ? 137.237 142.227 163.950 1.00 97.52  ? 11  C   C "C2'" 1 
ATOM   8722  O  "O2'" . C   C 2 11  ? 136.137 141.606 163.324 1.00 108.08 ? 11  C   C "O2'" 1 
ATOM   8723  C  "C1'" . C   C 2 11  ? 137.893 141.185 164.856 1.00 95.19  ? 11  C   C "C1'" 1 
ATOM   8724  N  N1    . C   C 2 11  ? 138.544 141.765 166.061 1.00 90.39  ? 11  C   C N1    1 
ATOM   8725  C  C2    . C   C 2 11  ? 137.733 142.110 167.141 1.00 94.65  ? 11  C   C C2    1 
ATOM   8726  O  O2    . C   C 2 11  ? 136.507 141.965 167.032 1.00 97.89  ? 11  C   C O2    1 
ATOM   8727  N  N3    . C   C 2 11  ? 138.304 142.616 168.256 1.00 95.47  ? 11  C   C N3    1 
ATOM   8728  C  C4    . C   C 2 11  ? 139.630 142.758 168.330 1.00 84.70  ? 11  C   C C4    1 
ATOM   8729  N  N4    . C   C 2 11  ? 140.133 143.261 169.446 1.00 93.23  ? 11  C   C N4    1 
ATOM   8730  C  C5    . C   C 2 11  ? 140.474 142.390 167.250 1.00 86.47  ? 11  C   C C5    1 
ATOM   8731  C  C6    . C   C 2 11  ? 139.896 141.893 166.149 1.00 95.05  ? 11  C   C C6    1 
ATOM   8732  P  P     . U   C 2 12  ? 137.753 144.625 161.511 1.00 20.70  ? 12  U   C P     1 
ATOM   8733  O  OP1   . U   C 2 12  ? 137.218 144.949 160.141 1.00 90.80  ? 12  U   C OP1   1 
ATOM   8734  O  OP2   . U   C 2 12  ? 139.015 145.372 161.866 1.00 80.17  ? 12  U   C OP2   1 
ATOM   8735  O  "O5'" . U   C 2 12  ? 136.631 145.081 162.561 1.00 82.16  ? 12  U   C "O5'" 1 
ATOM   8736  C  "C5'" . U   C 2 12  ? 135.264 144.675 162.333 1.00 103.31 ? 12  U   C "C5'" 1 
ATOM   8737  C  "C4'" . U   C 2 12  ? 134.400 145.277 163.409 1.00 97.92  ? 12  U   C "C4'" 1 
ATOM   8738  O  "O4'" . U   C 2 12  ? 134.690 144.653 164.685 1.00 79.76  ? 12  U   C "O4'" 1 
ATOM   8739  C  "C3'" . U   C 2 12  ? 134.641 146.761 163.688 1.00 85.84  ? 12  U   C "C3'" 1 
ATOM   8740  O  "O3'" . U   C 2 12  ? 134.042 147.610 162.720 1.00 71.25  ? 12  U   C "O3'" 1 
ATOM   8741  C  "C2'" . U   C 2 12  ? 133.999 146.887 165.069 1.00 90.13  ? 12  U   C "C2'" 1 
ATOM   8742  O  "O2'" . U   C 2 12  ? 132.590 146.888 165.012 1.00 92.65  ? 12  U   C "O2'" 1 
ATOM   8743  C  "C1'" . U   C 2 12  ? 134.477 145.591 165.720 1.00 84.34  ? 12  U   C "C1'" 1 
ATOM   8744  N  N1    . U   C 2 12  ? 135.728 145.770 166.477 1.00 82.85  ? 12  U   C N1    1 
ATOM   8745  C  C2    . U   C 2 12  ? 135.609 146.244 167.767 1.00 88.17  ? 12  U   C C2    1 
ATOM   8746  O  O2    . U   C 2 12  ? 134.534 146.528 168.273 1.00 89.52  ? 12  U   C O2    1 
ATOM   8747  N  N3    . U   C 2 12  ? 136.793 146.394 168.435 1.00 82.08  ? 12  U   C N3    1 
ATOM   8748  C  C4    . U   C 2 12  ? 138.056 146.111 167.966 1.00 82.61  ? 12  U   C C4    1 
ATOM   8749  O  O4    . U   C 2 12  ? 139.024 146.297 168.701 1.00 91.00  ? 12  U   C O4    1 
ATOM   8750  C  C5    . U   C 2 12  ? 138.098 145.618 166.621 1.00 86.96  ? 12  U   C C5    1 
ATOM   8751  C  C6    . U   C 2 12  ? 136.954 145.465 165.939 1.00 86.88  ? 12  U   C C6    1 
ATOM   8752  P  P     . C   C 2 13  ? 134.514 149.139 162.601 1.00 37.18  ? 13  C   C P     1 
ATOM   8753  O  OP1   . C   C 2 13  ? 133.698 149.936 161.613 1.00 89.42  ? 13  C   C OP1   1 
ATOM   8754  O  OP2   . C   C 2 13  ? 136.008 149.276 162.425 1.00 77.68  ? 13  C   C OP2   1 
ATOM   8755  O  "O5'" . C   C 2 13  ? 134.166 149.697 164.064 1.00 75.87  ? 13  C   C "O5'" 1 
ATOM   8756  C  "C5'" . C   C 2 13  ? 134.990 150.738 164.631 1.00 86.09  ? 13  C   C "C5'" 1 
ATOM   8757  C  "C4'" . C   C 2 13  ? 134.689 150.848 166.103 1.00 87.09  ? 13  C   C "C4'" 1 
ATOM   8758  O  "O4'" . C   C 2 13  ? 135.338 149.771 166.825 1.00 96.40  ? 13  C   C "O4'" 1 
ATOM   8759  C  "C3'" . C   C 2 13  ? 135.211 152.108 166.798 1.00 88.37  ? 13  C   C "C3'" 1 
ATOM   8760  O  "O3'" . C   C 2 13  ? 134.352 153.212 166.555 1.00 85.04  ? 13  C   C "O3'" 1 
ATOM   8761  C  "C2'" . C   C 2 13  ? 135.198 151.660 168.260 1.00 91.78  ? 13  C   C "C2'" 1 
ATOM   8762  O  "O2'" . C   C 2 13  ? 133.907 151.707 168.827 1.00 88.71  ? 13  C   C "O2'" 1 
ATOM   8763  C  "C1'" . C   C 2 13  ? 135.629 150.195 168.140 1.00 80.94  ? 13  C   C "C1'" 1 
ATOM   8764  N  N1    . C   C 2 13  ? 137.078 149.990 168.407 1.00 72.57  ? 13  C   C N1    1 
ATOM   8765  C  C2    . C   C 2 13  ? 137.544 150.188 169.708 1.00 90.64  ? 13  C   C C2    1 
ATOM   8766  O  O2    . C   C 2 13  ? 136.741 150.554 170.577 1.00 102.24 ? 13  C   C O2    1 
ATOM   8767  N  N3    . C   C 2 13  ? 138.858 150.005 169.972 1.00 97.15  ? 13  C   C N3    1 
ATOM   8768  C  C4    . C   C 2 13  ? 139.694 149.620 169.004 1.00 88.02  ? 13  C   C C4    1 
ATOM   8769  N  N4    . C   C 2 13  ? 140.967 149.446 169.321 1.00 72.96  ? 13  C   C N4    1 
ATOM   8770  C  C5    . C   C 2 13  ? 139.236 149.396 167.679 1.00 92.11  ? 13  C   C C5    1 
ATOM   8771  C  C6    . C   C 2 13  ? 137.933 149.586 167.427 1.00 90.10  ? 13  C   C C6    1 
ATOM   8772  P  P     . A   C 2 14  ? 134.790 154.702 166.961 1.00 48.87  ? 14  A   C P     1 
ATOM   8773  O  OP1   . A   C 2 14  ? 133.738 155.721 166.587 1.00 79.16  ? 14  A   C OP1   1 
ATOM   8774  O  OP2   . A   C 2 14  ? 136.182 155.051 166.486 1.00 89.33  ? 14  A   C OP2   1 
ATOM   8775  O  "O5'" . A   C 2 14  ? 134.837 154.650 168.567 1.00 80.93  ? 14  A   C "O5'" 1 
ATOM   8776  C  "C5'" . A   C 2 14  ? 135.863 155.400 169.252 1.00 97.44  ? 14  A   C "C5'" 1 
ATOM   8777  C  "C4'" . A   C 2 14  ? 135.543 155.453 170.724 1.00 96.05  ? 14  A   C "C4'" 1 
ATOM   8778  O  "O4'" . A   C 2 14  ? 135.907 154.196 171.350 1.00 86.97  ? 14  A   C "O4'" 1 
ATOM   8779  C  "C3'" . A   C 2 14  ? 136.304 156.514 171.520 1.00 93.98  ? 14  A   C "C3'" 1 
ATOM   8780  O  "O3'" . A   C 2 14  ? 135.649 157.774 171.472 1.00 82.15  ? 14  A   C "O3'" 1 
ATOM   8781  C  "C2'" . A   C 2 14  ? 136.280 155.914 172.924 1.00 90.36  ? 14  A   C "C2'" 1 
ATOM   8782  O  "O2'" . A   C 2 14  ? 135.053 156.135 173.581 1.00 84.10  ? 14  A   C "O2'" 1 
ATOM   8783  C  "C1'" . A   C 2 14  ? 136.482 154.436 172.615 1.00 84.66  ? 14  A   C "C1'" 1 
ATOM   8784  N  N9    . A   C 2 14  ? 137.878 154.019 172.577 1.00 84.35  ? 14  A   C N9    1 
ATOM   8785  C  C8    . A   C 2 14  ? 138.582 153.627 171.468 1.00 81.35  ? 14  A   C C8    1 
ATOM   8786  N  N7    . A   C 2 14  ? 139.809 153.262 171.738 1.00 91.72  ? 14  A   C N7    1 
ATOM   8787  C  C5    . A   C 2 14  ? 139.917 153.405 173.111 1.00 91.97  ? 14  A   C C5    1 
ATOM   8788  C  C6    . A   C 2 14  ? 140.979 153.174 174.003 1.00 95.46  ? 14  A   C C6    1 
ATOM   8789  N  N6    . A   C 2 14  ? 142.179 152.746 173.625 1.00 92.93  ? 14  A   C N6    1 
ATOM   8790  N  N1    . A   C 2 14  ? 140.756 153.418 175.314 1.00 97.30  ? 14  A   C N1    1 
ATOM   8791  C  C2    . A   C 2 14  ? 139.549 153.859 175.684 1.00 94.24  ? 14  A   C C2    1 
ATOM   8792  N  N3    . A   C 2 14  ? 138.479 154.108 174.937 1.00 93.79  ? 14  A   C N3    1 
ATOM   8793  C  C4    . A   C 2 14  ? 138.726 153.851 173.644 1.00 90.30  ? 14  A   C C4    1 
ATOM   8794  P  P     . G   C 2 15  ? 136.498 159.124 171.298 1.00 50.22  ? 15  G   C P     1 
ATOM   8795  O  OP1   . G   C 2 15  ? 135.703 160.358 171.659 1.00 89.92  ? 15  G   C OP1   1 
ATOM   8796  O  OP2   . G   C 2 15  ? 137.188 159.202 169.955 1.00 78.96  ? 15  G   C OP2   1 
ATOM   8797  O  "O5'" . G   C 2 15  ? 137.646 158.968 172.413 1.00 95.49  ? 15  G   C "O5'" 1 
ATOM   8798  C  "C5'" . G   C 2 15  ? 137.276 159.056 173.807 1.00 98.62  ? 15  G   C "C5'" 1 
ATOM   8799  C  "C4'" . G   C 2 15  ? 138.494 158.790 174.651 1.00 90.89  ? 15  G   C "C4'" 1 
ATOM   8800  O  "O4'" . G   C 2 15  ? 138.927 157.417 174.479 1.00 87.46  ? 15  G   C "O4'" 1 
ATOM   8801  C  "C3'" . G   C 2 15  ? 139.746 159.592 174.292 1.00 94.19  ? 15  G   C "C3'" 1 
ATOM   8802  O  "O3'" . G   C 2 15  ? 139.713 160.937 174.748 1.00 95.82  ? 15  G   C "O3'" 1 
ATOM   8803  C  "C2'" . G   C 2 15  ? 140.796 158.747 175.009 1.00 94.13  ? 15  G   C "C2'" 1 
ATOM   8804  O  "O2'" . G   C 2 15  ? 140.751 158.912 176.408 1.00 100.42 ? 15  G   C "O2'" 1 
ATOM   8805  C  "C1'" . G   C 2 15  ? 140.331 157.354 174.606 1.00 85.51  ? 15  G   C "C1'" 1 
ATOM   8806  N  N9    . G   C 2 15  ? 140.903 156.912 173.343 1.00 88.47  ? 15  G   C N9    1 
ATOM   8807  C  C8    . G   C 2 15  ? 140.317 156.965 172.105 1.00 90.56  ? 15  G   C C8    1 
ATOM   8808  N  N7    . G   C 2 15  ? 141.081 156.486 171.154 1.00 88.39  ? 15  G   C N7    1 
ATOM   8809  C  C5    . G   C 2 15  ? 142.238 156.090 171.811 1.00 92.69  ? 15  G   C C5    1 
ATOM   8810  C  C6    . G   C 2 15  ? 143.417 155.500 171.299 1.00 91.14  ? 15  G   C C6    1 
ATOM   8811  O  O6    . G   C 2 15  ? 143.679 155.205 170.127 1.00 95.61  ? 15  G   C O6    1 
ATOM   8812  N  N1    . G   C 2 15  ? 144.345 155.256 172.310 1.00 87.80  ? 15  G   C N1    1 
ATOM   8813  C  C2    . G   C 2 15  ? 144.160 155.543 173.638 1.00 97.05  ? 15  G   C C2    1 
ATOM   8814  N  N2    . G   C 2 15  ? 145.167 155.234 174.463 1.00 105.25 ? 15  G   C N2    1 
ATOM   8815  N  N3    . G   C 2 15  ? 143.054 156.099 174.125 1.00 100.85 ? 15  G   C N3    1 
ATOM   8816  C  C4    . G   C 2 15  ? 142.136 156.335 173.160 1.00 95.45  ? 15  G   C C4    1 
HETATM 8817  P  P     . H2U C 2 16  ? 140.858 161.967 174.295 1.00 148.64 ? 16  H2U C P     1 
HETATM 8818  O  OP1   . H2U C 2 16  ? 141.586 161.487 173.057 1.00 155.67 ? 16  H2U C OP1   1 
HETATM 8819  O  OP2   . H2U C 2 16  ? 141.778 162.373 175.426 1.00 156.19 ? 16  H2U C OP2   1 
HETATM 8820  O  "O5'" . H2U C 2 16  ? 140.011 163.270 173.866 1.00 157.83 ? 16  H2U C "O5'" 1 
HETATM 8821  C  "C5'" . H2U C 2 16  ? 138.666 163.427 174.381 1.00 157.52 ? 16  H2U C "C5'" 1 
HETATM 8822  C  "C4'" . H2U C 2 16  ? 138.554 164.740 175.117 1.00 158.74 ? 16  H2U C "C4'" 1 
HETATM 8823  O  "O4'" . H2U C 2 16  ? 138.002 164.492 176.434 1.00 160.27 ? 16  H2U C "O4'" 1 
HETATM 8824  C  "C3'" . H2U C 2 16  ? 139.868 165.503 175.338 1.00 162.08 ? 16  H2U C "C3'" 1 
HETATM 8825  O  "O3'" . H2U C 2 16  ? 139.652 166.904 175.238 1.00 160.22 ? 16  H2U C "O3'" 1 
HETATM 8826  C  "C1'" . H2U C 2 16  ? 138.911 164.879 177.439 1.00 158.03 ? 16  H2U C "C1'" 1 
HETATM 8827  C  "C2'" . H2U C 2 16  ? 140.258 165.083 176.752 1.00 159.10 ? 16  H2U C "C2'" 1 
HETATM 8828  O  "O2'" . H2U C 2 16  ? 141.041 166.067 177.411 1.00 157.14 ? 16  H2U C "O2'" 1 
HETATM 8829  N  N1    . H2U C 2 16  ? 138.960 163.821 178.491 1.00 156.45 ? 16  H2U C N1    1 
HETATM 8830  C  C2    . H2U C 2 16  ? 138.770 162.519 178.169 1.00 157.10 ? 16  H2U C C2    1 
HETATM 8831  O  O2    . H2U C 2 16  ? 139.174 162.048 177.113 1.00 157.08 ? 16  H2U C O2    1 
HETATM 8832  N  N3    . H2U C 2 16  ? 138.117 161.771 179.070 1.00 157.80 ? 16  H2U C N3    1 
HETATM 8833  C  C4    . H2U C 2 16  ? 138.190 162.063 180.411 1.00 158.13 ? 16  H2U C C4    1 
HETATM 8834  O  O4    . H2U C 2 16  ? 137.415 161.561 181.206 1.00 157.94 ? 16  H2U C O4    1 
HETATM 8835  C  C5    . H2U C 2 16  ? 139.238 163.054 180.805 1.00 158.73 ? 16  H2U C C5    1 
HETATM 8836  C  C6    . H2U C 2 16  ? 139.185 164.260 179.873 1.00 157.50 ? 16  H2U C C6    1 
ATOM   8837  P  P     . C   C 2 17  ? 140.637 167.865 174.405 1.00 175.13 ? 17  C   C P     1 
ATOM   8838  O  OP1   . C   C 2 17  ? 140.001 169.215 174.139 1.00 178.09 ? 17  C   C OP1   1 
ATOM   8839  O  OP2   . C   C 2 17  ? 141.231 167.218 173.166 1.00 178.84 ? 17  C   C OP2   1 
ATOM   8840  O  "O5'" . C   C 2 17  ? 141.856 168.127 175.425 1.00 179.64 ? 17  C   C "O5'" 1 
ATOM   8841  C  "C5'" . C   C 2 17  ? 142.847 169.124 175.079 1.00 180.07 ? 17  C   C "C5'" 1 
ATOM   8842  C  "C4'" . C   C 2 17  ? 143.481 169.639 176.347 1.00 181.32 ? 17  C   C "C4'" 1 
ATOM   8843  O  "O4'" . C   C 2 17  ? 142.526 170.478 177.046 1.00 180.93 ? 17  C   C "O4'" 1 
ATOM   8844  C  "C3'" . C   C 2 17  ? 143.905 168.565 177.359 1.00 179.63 ? 17  C   C "C3'" 1 
ATOM   8845  O  "O3'" . C   C 2 17  ? 145.264 168.183 177.183 1.00 176.03 ? 17  C   C "O3'" 1 
ATOM   8846  C  "C2'" . C   C 2 17  ? 143.718 169.259 178.713 1.00 178.36 ? 17  C   C "C2'" 1 
ATOM   8847  O  "O2'" . C   C 2 17  ? 144.862 169.982 179.115 1.00 179.54 ? 17  C   C "O2'" 1 
ATOM   8848  C  "C1'" . C   C 2 17  ? 142.577 170.245 178.437 1.00 179.06 ? 17  C   C "C1'" 1 
ATOM   8849  N  N1    . C   C 2 17  ? 141.249 169.744 178.886 1.00 177.36 ? 17  C   C N1    1 
ATOM   8850  C  C2    . C   C 2 17  ? 140.862 169.988 180.206 1.00 177.58 ? 17  C   C C2    1 
ATOM   8851  O  O2    . C   C 2 17  ? 141.643 170.595 180.955 1.00 178.66 ? 17  C   C O2    1 
ATOM   8852  N  N3    . C   C 2 17  ? 139.653 169.542 180.628 1.00 179.26 ? 17  C   C N3    1 
ATOM   8853  C  C4    . C   C 2 17  ? 138.840 168.889 179.788 1.00 179.98 ? 17  C   C C4    1 
ATOM   8854  N  N4    . C   C 2 17  ? 137.669 168.479 180.254 1.00 179.79 ? 17  C   C N4    1 
ATOM   8855  C  C5    . C   C 2 17  ? 139.214 168.642 178.439 1.00 180.94 ? 17  C   C C5    1 
ATOM   8856  C  C6    . C   C 2 17  ? 140.412 169.086 178.033 1.00 180.20 ? 17  C   C C6    1 
ATOM   8857  P  P     . G   C 2 18  ? 145.718 167.177 176.015 1.00 130.70 ? 18  G   C P     1 
ATOM   8858  O  OP1   . G   C 2 18  ? 145.634 167.766 174.620 1.00 137.99 ? 18  G   C OP1   1 
ATOM   8859  O  OP2   . G   C 2 18  ? 145.084 165.805 176.144 1.00 140.84 ? 18  G   C OP2   1 
ATOM   8860  O  "O5'" . G   C 2 18  ? 147.289 167.018 176.344 1.00 139.62 ? 18  G   C "O5'" 1 
ATOM   8861  C  "C5'" . G   C 2 18  ? 148.072 166.053 175.599 1.00 140.65 ? 18  G   C "C5'" 1 
ATOM   8862  C  "C4'" . G   C 2 18  ? 148.320 164.837 176.456 1.00 139.15 ? 18  G   C "C4'" 1 
ATOM   8863  O  "O4'" . G   C 2 18  ? 149.748 164.623 176.569 1.00 138.11 ? 18  G   C "O4'" 1 
ATOM   8864  C  "C3'" . G   C 2 18  ? 147.840 164.921 177.907 1.00 136.04 ? 18  G   C "C3'" 1 
ATOM   8865  O  "O3'" . G   C 2 18  ? 147.675 163.624 178.463 1.00 128.37 ? 18  G   C "O3'" 1 
ATOM   8866  C  "C2'" . G   C 2 18  ? 149.008 165.654 178.571 1.00 133.82 ? 18  G   C "C2'" 1 
ATOM   8867  O  "O2'" . G   C 2 18  ? 149.092 165.417 179.959 1.00 137.91 ? 18  G   C "O2'" 1 
ATOM   8868  C  "C1'" . G   C 2 18  ? 150.208 165.077 177.822 1.00 133.31 ? 18  G   C "C1'" 1 
ATOM   8869  N  N9    . G   C 2 18  ? 151.265 166.051 177.586 1.00 131.83 ? 18  G   C N9    1 
ATOM   8870  C  C8    . G   C 2 18  ? 151.108 167.404 177.421 1.00 135.30 ? 18  G   C C8    1 
ATOM   8871  N  N7    . G   C 2 18  ? 152.239 168.035 177.222 1.00 135.06 ? 18  G   C N7    1 
ATOM   8872  C  C5    . G   C 2 18  ? 153.200 167.032 177.254 1.00 134.75 ? 18  G   C C5    1 
ATOM   8873  C  C6    . G   C 2 18  ? 154.605 167.117 177.104 1.00 137.76 ? 18  G   C C6    1 
ATOM   8874  O  O6    . G   C 2 18  ? 155.294 168.125 176.897 1.00 138.91 ? 18  G   C O6    1 
ATOM   8875  N  N1    . G   C 2 18  ? 155.203 165.861 177.209 1.00 138.46 ? 18  G   C N1    1 
ATOM   8876  C  C2    . G   C 2 18  ? 154.535 164.682 177.436 1.00 139.76 ? 18  G   C C2    1 
ATOM   8877  N  N2    . G   C 2 18  ? 155.284 163.575 177.504 1.00 141.84 ? 18  G   C N2    1 
ATOM   8878  N  N3    . G   C 2 18  ? 153.214 164.597 177.580 1.00 140.99 ? 18  G   C N3    1 
ATOM   8879  C  C4    . G   C 2 18  ? 152.613 165.806 177.477 1.00 136.70 ? 18  G   C C4    1 
ATOM   8880  P  P     . G   C 2 19  ? 146.471 163.271 179.470 1.00 127.45 ? 19  G   C P     1 
ATOM   8881  O  OP1   . G   C 2 19  ? 145.355 162.603 178.694 1.00 134.69 ? 19  G   C OP1   1 
ATOM   8882  O  OP2   . G   C 2 19  ? 146.016 164.411 180.355 1.00 142.18 ? 19  G   C OP2   1 
ATOM   8883  O  "O5'" . G   C 2 19  ? 147.118 162.158 180.434 1.00 137.16 ? 19  G   C "O5'" 1 
ATOM   8884  C  "C5'" . G   C 2 19  ? 148.351 162.486 181.116 1.00 139.97 ? 19  G   C "C5'" 1 
ATOM   8885  C  "C4'" . G   C 2 19  ? 148.674 161.415 182.125 1.00 137.70 ? 19  G   C "C4'" 1 
ATOM   8886  O  "O4'" . G   C 2 19  ? 149.932 161.741 182.761 1.00 137.40 ? 19  G   C "O4'" 1 
ATOM   8887  C  "C3'" . G   C 2 19  ? 147.691 161.266 183.288 1.00 136.43 ? 19  G   C "C3'" 1 
ATOM   8888  O  "O3'" . G   C 2 19  ? 147.752 159.961 183.843 1.00 134.51 ? 19  G   C "O3'" 1 
ATOM   8889  C  "C2'" . G   C 2 19  ? 148.202 162.304 184.288 1.00 136.95 ? 19  G   C "C2'" 1 
ATOM   8890  O  "O2'" . G   C 2 19  ? 147.922 161.945 185.623 1.00 138.25 ? 19  G   C "O2'" 1 
ATOM   8891  C  "C1'" . G   C 2 19  ? 149.706 162.319 184.027 1.00 136.00 ? 19  G   C "C1'" 1 
ATOM   8892  N  N9    . G   C 2 19  ? 150.260 163.665 184.009 1.00 134.27 ? 19  G   C N9    1 
ATOM   8893  C  C8    . G   C 2 19  ? 149.578 164.823 183.738 1.00 133.87 ? 19  G   C C8    1 
ATOM   8894  N  N7    . G   C 2 19  ? 150.332 165.892 183.804 1.00 133.23 ? 19  G   C N7    1 
ATOM   8895  C  C5    . G   C 2 19  ? 151.585 165.405 184.148 1.00 133.37 ? 19  G   C C5    1 
ATOM   8896  C  C6    . G   C 2 19  ? 152.800 166.097 184.357 1.00 136.74 ? 19  G   C C6    1 
ATOM   8897  O  O6    . G   C 2 19  ? 153.007 167.315 184.280 1.00 137.48 ? 19  G   C O6    1 
ATOM   8898  N  N1    . G   C 2 19  ? 153.834 165.222 184.688 1.00 139.66 ? 19  G   C N1    1 
ATOM   8899  C  C2    . G   C 2 19  ? 153.711 163.859 184.800 1.00 139.69 ? 19  G   C C2    1 
ATOM   8900  N  N2    . G   C 2 19  ? 154.818 163.181 185.128 1.00 140.20 ? 19  G   C N2    1 
ATOM   8901  N  N3    . G   C 2 19  ? 152.571 163.202 184.601 1.00 136.29 ? 19  G   C N3    1 
ATOM   8902  C  C4    . G   C 2 19  ? 151.554 164.036 184.284 1.00 134.26 ? 19  G   C C4    1 
HETATM 8903  P  P     . H2U C 2 20  ? 146.941 158.744 183.181 1.00 131.79 ? 20  H2U C P     1 
HETATM 8904  O  OP1   . H2U C 2 20  ? 146.630 158.953 181.713 1.00 144.24 ? 20  H2U C OP1   1 
HETATM 8905  O  OP2   . H2U C 2 20  ? 145.744 158.346 184.015 1.00 146.26 ? 20  H2U C OP2   1 
HETATM 8906  O  "O5'" . H2U C 2 20  ? 147.995 157.537 183.278 1.00 142.60 ? 20  H2U C "O5'" 1 
HETATM 8907  C  "C5'" . H2U C 2 20  ? 149.333 157.741 182.770 1.00 149.95 ? 20  H2U C "C5'" 1 
HETATM 8908  C  "C4'" . H2U C 2 20  ? 150.109 156.462 182.945 1.00 148.54 ? 20  H2U C "C4'" 1 
HETATM 8909  O  "O4'" . H2U C 2 20  ? 150.071 156.091 184.345 1.00 146.21 ? 20  H2U C "O4'" 1 
HETATM 8910  C  "C3'" . H2U C 2 20  ? 149.574 155.258 182.160 1.00 149.62 ? 20  H2U C "C3'" 1 
HETATM 8911  O  "O3'" . H2U C 2 20  ? 150.274 155.152 180.927 1.00 150.13 ? 20  H2U C "O3'" 1 
HETATM 8912  C  "C1'" . H2U C 2 20  ? 150.000 154.693 184.497 1.00 146.21 ? 20  H2U C "C1'" 1 
HETATM 8913  C  "C2'" . H2U C 2 20  ? 149.811 154.082 183.110 1.00 147.80 ? 20  H2U C "C2'" 1 
HETATM 8914  O  "O2'" . H2U C 2 20  ? 150.950 153.316 182.750 1.00 148.03 ? 20  H2U C "O2'" 1 
HETATM 8915  N  N1    . H2U C 2 20  ? 148.864 154.380 185.406 1.00 147.40 ? 20  H2U C N1    1 
HETATM 8916  C  C2    . H2U C 2 20  ? 148.932 153.308 186.211 1.00 149.81 ? 20  H2U C C2    1 
HETATM 8917  O  O2    . H2U C 2 20  ? 149.607 152.330 185.909 1.00 153.08 ? 20  H2U C O2    1 
HETATM 8918  N  N3    . H2U C 2 20  ? 148.248 153.370 187.370 1.00 151.08 ? 20  H2U C N3    1 
HETATM 8919  C  C4    . H2U C 2 20  ? 147.377 154.383 187.710 1.00 150.49 ? 20  H2U C C4    1 
HETATM 8920  O  O4    . H2U C 2 20  ? 146.554 154.222 188.593 1.00 148.69 ? 20  H2U C O4    1 
HETATM 8921  C  C5    . H2U C 2 20  ? 147.460 155.647 186.914 1.00 152.20 ? 20  H2U C C5    1 
HETATM 8922  C  C6    . H2U C 2 20  ? 147.705 155.274 185.461 1.00 151.81 ? 20  H2U C C6    1 
ATOM   8923  P  P     . A   C 2 21  ? 149.905 154.021 179.850 1.00 89.76  ? 21  A   C P     1 
ATOM   8924  O  OP1   . A   C 2 21  ? 150.229 152.614 180.308 1.00 101.07 ? 21  A   C OP1   1 
ATOM   8925  O  OP2   . A   C 2 21  ? 150.438 154.352 178.471 1.00 102.29 ? 21  A   C OP2   1 
ATOM   8926  O  "O5'" . A   C 2 21  ? 148.307 154.110 179.760 1.00 96.40  ? 21  A   C "O5'" 1 
ATOM   8927  C  "C5'" . A   C 2 21  ? 147.565 152.877 179.847 1.00 95.00  ? 21  A   C "C5'" 1 
ATOM   8928  C  "C4'" . A   C 2 21  ? 146.148 153.112 179.395 1.00 96.17  ? 21  A   C "C4'" 1 
ATOM   8929  O  "O4'" . A   C 2 21  ? 146.164 153.616 178.038 1.00 99.77  ? 21  A   C "O4'" 1 
ATOM   8930  C  "C3'" . A   C 2 21  ? 145.259 151.865 179.381 1.00 98.71  ? 21  A   C "C3'" 1 
ATOM   8931  O  "O3'" . A   C 2 21  ? 144.488 151.900 180.573 1.00 96.01  ? 21  A   C "O3'" 1 
ATOM   8932  C  "C2'" . A   C 2 21  ? 144.443 152.016 178.095 1.00 103.82 ? 21  A   C "C2'" 1 
ATOM   8933  O  "O2'" . A   C 2 21  ? 143.255 152.748 178.290 1.00 101.91 ? 21  A   C "O2'" 1 
ATOM   8934  C  "C1'" . A   C 2 21  ? 145.384 152.804 177.193 1.00 101.97 ? 21  A   C "C1'" 1 
ATOM   8935  N  N9    . A   C 2 21  ? 146.291 151.996 176.387 1.00 97.13  ? 21  A   C N9    1 
ATOM   8936  C  C8    . A   C 2 21  ? 147.480 151.440 176.782 1.00 99.38  ? 21  A   C C8    1 
ATOM   8937  N  N7    . A   C 2 21  ? 148.085 150.778 175.831 1.00 95.94  ? 21  A   C N7    1 
ATOM   8938  C  C5    . A   C 2 21  ? 147.245 150.905 174.738 1.00 100.06 ? 21  A   C C5    1 
ATOM   8939  C  C6    . A   C 2 21  ? 147.333 150.426 173.420 1.00 100.17 ? 21  A   C C6    1 
ATOM   8940  N  N6    . A   C 2 21  ? 148.343 149.692 172.966 1.00 95.19  ? 21  A   C N6    1 
ATOM   8941  N  N1    . A   C 2 21  ? 146.320 150.732 172.579 1.00 99.71  ? 21  A   C N1    1 
ATOM   8942  C  C2    . A   C 2 21  ? 145.305 151.468 173.043 1.00 104.25 ? 21  A   C C2    1 
ATOM   8943  N  N3    . A   C 2 21  ? 145.119 151.976 174.255 1.00 99.50  ? 21  A   C N3    1 
ATOM   8944  C  C4    . A   C 2 21  ? 146.131 151.647 175.070 1.00 97.28  ? 21  A   C C4    1 
ATOM   8945  P  P     . G   C 2 22  ? 143.802 150.573 181.159 1.00 76.99  ? 22  G   C P     1 
ATOM   8946  O  OP1   . G   C 2 22  ? 143.388 150.705 182.609 1.00 93.40  ? 22  G   C OP1   1 
ATOM   8947  O  OP2   . G   C 2 22  ? 144.591 149.319 180.851 1.00 94.47  ? 22  G   C OP2   1 
ATOM   8948  O  "O5'" . G   C 2 22  ? 142.454 150.511 180.296 1.00 93.62  ? 22  G   C "O5'" 1 
ATOM   8949  C  "C5'" . G   C 2 22  ? 141.463 151.548 180.483 1.00 99.49  ? 22  G   C "C5'" 1 
ATOM   8950  C  "C4'" . G   C 2 22  ? 140.190 151.114 179.808 1.00 99.42  ? 22  G   C "C4'" 1 
ATOM   8951  O  "O4'" . G   C 2 22  ? 140.354 151.194 178.368 1.00 93.10  ? 22  G   C "O4'" 1 
ATOM   8952  C  "C3'" . G   C 2 22  ? 139.764 149.669 180.095 1.00 96.55  ? 22  G   C "C3'" 1 
ATOM   8953  O  "O3'" . G   C 2 22  ? 138.348 149.587 180.133 1.00 90.46  ? 22  G   C "O3'" 1 
ATOM   8954  C  "C2'" . G   C 2 22  ? 140.324 148.924 178.884 1.00 95.11  ? 22  G   C "C2'" 1 
ATOM   8955  O  "O2'" . G   C 2 22  ? 139.692 147.688 178.637 1.00 94.77  ? 22  G   C "O2'" 1 
ATOM   8956  C  "C1'" . G   C 2 22  ? 140.011 149.951 177.806 1.00 86.98  ? 22  G   C "C1'" 1 
ATOM   8957  N  N9    . G   C 2 22  ? 140.723 149.756 176.552 1.00 81.78  ? 22  G   C N9    1 
ATOM   8958  C  C8    . G   C 2 22  ? 142.038 149.415 176.370 1.00 94.58  ? 22  G   C C8    1 
ATOM   8959  N  N7    . G   C 2 22  ? 142.372 149.309 175.107 1.00 97.20  ? 22  G   C N7    1 
ATOM   8960  C  C5    . G   C 2 22  ? 141.206 149.614 174.418 1.00 94.40  ? 22  G   C C5    1 
ATOM   8961  C  C6    . G   C 2 22  ? 140.952 149.666 173.027 1.00 91.37  ? 22  G   C C6    1 
ATOM   8962  O  O6    . G   C 2 22  ? 141.736 149.448 172.095 1.00 96.67  ? 22  G   C O6    1 
ATOM   8963  N  N1    . G   C 2 22  ? 139.629 150.016 172.763 1.00 81.31  ? 22  G   C N1    1 
ATOM   8964  C  C2    . G   C 2 22  ? 138.677 150.285 173.714 1.00 87.65  ? 22  G   C C2    1 
ATOM   8965  N  N2    . G   C 2 22  ? 137.457 150.612 173.272 1.00 93.93  ? 22  G   C N2    1 
ATOM   8966  N  N3    . G   C 2 22  ? 138.909 150.237 175.021 1.00 96.66  ? 22  G   C N3    1 
ATOM   8967  C  C4    . G   C 2 22  ? 140.191 149.906 175.297 1.00 90.46  ? 22  G   C C4    1 
ATOM   8968  P  P     . A   C 2 23  ? 137.593 148.543 181.090 1.00 90.10  ? 23  A   C P     1 
ATOM   8969  O  OP1   . A   C 2 23  ? 137.123 149.166 182.385 1.00 95.77  ? 23  A   C OP1   1 
ATOM   8970  O  OP2   . A   C 2 23  ? 138.348 147.244 181.263 1.00 95.11  ? 23  A   C OP2   1 
ATOM   8971  O  "O5'" . A   C 2 23  ? 136.284 148.221 180.217 1.00 99.18  ? 23  A   C "O5'" 1 
ATOM   8972  C  "C5'" . A   C 2 23  ? 136.468 147.573 178.940 1.00 96.74  ? 23  A   C "C5'" 1 
ATOM   8973  C  "C4'" . A   C 2 23  ? 135.204 147.689 178.131 1.00 91.37  ? 23  A   C "C4'" 1 
ATOM   8974  O  "O4'" . A   C 2 23  ? 135.438 148.599 177.027 1.00 77.28  ? 23  A   C "O4'" 1 
ATOM   8975  C  "C3'" . A   C 2 23  ? 134.712 146.383 177.498 1.00 92.19  ? 23  A   C "C3'" 1 
ATOM   8976  O  "O3'" . A   C 2 23  ? 133.765 145.758 178.352 1.00 82.13  ? 23  A   C "O3'" 1 
ATOM   8977  C  "C2'" . A   C 2 23  ? 134.086 146.862 176.189 1.00 99.64  ? 23  A   C "C2'" 1 
ATOM   8978  O  "O2'" . A   C 2 23  ? 132.754 147.293 176.352 1.00 106.89 ? 23  A   C "O2'" 1 
ATOM   8979  C  "C1'" . A   C 2 23  ? 134.996 148.028 175.819 1.00 86.69  ? 23  A   C "C1'" 1 
ATOM   8980  N  N9    . A   C 2 23  ? 136.162 147.646 175.034 1.00 90.88  ? 23  A   C N9    1 
ATOM   8981  C  C8    . A   C 2 23  ? 137.426 147.392 175.500 1.00 102.59 ? 23  A   C C8    1 
ATOM   8982  N  N7    . A   C 2 23  ? 138.275 147.088 174.552 1.00 97.32  ? 23  A   C N7    1 
ATOM   8983  C  C5    . A   C 2 23  ? 137.530 147.158 173.387 1.00 77.95  ? 23  A   C C5    1 
ATOM   8984  C  C6    . A   C 2 23  ? 137.860 146.945 172.037 1.00 90.92  ? 23  A   C C6    1 
ATOM   8985  N  N6    . A   C 2 23  ? 139.072 146.600 171.614 1.00 105.10 ? 23  A   C N6    1 
ATOM   8986  N  N1    . A   C 2 23  ? 136.876 147.099 171.125 1.00 95.40  ? 23  A   C N1    1 
ATOM   8987  C  C2    . A   C 2 23  ? 135.656 147.441 171.550 1.00 97.19  ? 23  A   C C2    1 
ATOM   8988  N  N3    . A   C 2 23  ? 135.231 147.665 172.788 1.00 92.78  ? 23  A   C N3    1 
ATOM   8989  C  C4    . A   C 2 23  ? 136.228 147.513 173.671 1.00 80.77  ? 23  A   C C4    1 
ATOM   8990  P  P     . G   C 2 24  ? 133.641 144.160 178.425 1.00 54.42  ? 24  G   C P     1 
ATOM   8991  O  OP1   . G   C 2 24  ? 132.653 143.715 179.477 1.00 96.11  ? 24  G   C OP1   1 
ATOM   8992  O  OP2   . G   C 2 24  ? 134.988 143.480 178.522 1.00 89.93  ? 24  G   C OP2   1 
ATOM   8993  O  "O5'" . G   C 2 24  ? 133.013 143.757 177.003 1.00 98.22  ? 24  G   C "O5'" 1 
ATOM   8994  C  "C5'" . G   C 2 24  ? 131.624 144.073 176.751 1.00 99.54  ? 24  G   C "C5'" 1 
ATOM   8995  C  "C4'" . G   C 2 24  ? 131.303 143.775 175.309 1.00 99.47  ? 24  G   C "C4'" 1 
ATOM   8996  O  "O4'" . G   C 2 24  ? 132.036 144.686 174.451 1.00 93.46  ? 24  G   C "O4'" 1 
ATOM   8997  C  "C3'" . G   C 2 24  ? 131.705 142.389 174.799 1.00 90.41  ? 24  G   C "C3'" 1 
ATOM   8998  O  "O3'" . G   C 2 24  ? 130.771 141.378 175.153 1.00 90.06  ? 24  G   C "O3'" 1 
ATOM   8999  C  "C2'" . G   C 2 24  ? 131.725 142.650 173.294 1.00 94.66  ? 24  G   C "C2'" 1 
ATOM   9000  O  "O2'" . G   C 2 24  ? 130.434 142.647 172.728 1.00 100.31 ? 24  G   C "O2'" 1 
ATOM   9001  C  "C1'" . G   C 2 24  ? 132.363 144.035 173.244 1.00 87.77  ? 24  G   C "C1'" 1 
ATOM   9002  N  N9    . G   C 2 24  ? 133.812 143.981 173.106 1.00 83.59  ? 24  G   C N9    1 
ATOM   9003  C  C8    . G   C 2 24  ? 134.751 144.091 174.099 1.00 98.72  ? 24  G   C C8    1 
ATOM   9004  N  N7    . G   C 2 24  ? 135.980 143.992 173.656 1.00 102.53 ? 24  G   C N7    1 
ATOM   9005  C  C5    . G   C 2 24  ? 135.839 143.806 172.288 1.00 102.72 ? 24  G   C C5    1 
ATOM   9006  C  C6    . G   C 2 24  ? 136.821 143.634 171.283 1.00 106.31 ? 24  G   C C6    1 
ATOM   9007  O  O6    . G   C 2 24  ? 138.052 143.615 171.408 1.00 102.74 ? 24  G   C O6    1 
ATOM   9008  N  N1    . G   C 2 24  ? 136.241 143.476 170.025 1.00 104.58 ? 24  G   C N1    1 
ATOM   9009  C  C2    . G   C 2 24  ? 134.894 143.484 169.769 1.00 97.54  ? 24  G   C C2    1 
ATOM   9010  N  N2    . G   C 2 24  ? 134.525 143.320 168.493 1.00 100.18 ? 24  G   C N2    1 
ATOM   9011  N  N3    . G   C 2 24  ? 133.967 143.645 170.708 1.00 99.98  ? 24  G   C N3    1 
ATOM   9012  C  C4    . G   C 2 24  ? 134.510 143.809 171.936 1.00 97.73  ? 24  G   C C4    1 
ATOM   9013  P  P     . C   C 2 25  ? 131.245 139.858 175.364 1.00 86.09  ? 25  C   C P     1 
ATOM   9014  O  OP1   . C   C 2 25  ? 130.079 138.932 175.618 1.00 97.82  ? 25  C   C OP1   1 
ATOM   9015  O  OP2   . C   C 2 25  ? 132.345 139.742 176.394 1.00 101.21 ? 25  C   C OP2   1 
ATOM   9016  O  "O5'" . C   C 2 25  ? 131.880 139.416 173.953 1.00 91.22  ? 25  C   C "O5'" 1 
ATOM   9017  C  "C5'" . C   C 2 25  ? 130.994 139.186 172.834 1.00 96.14  ? 25  C   C "C5'" 1 
ATOM   9018  C  "C4'" . C   C 2 25  ? 131.806 139.071 171.569 1.00 96.97  ? 25  C   C "C4'" 1 
ATOM   9019  O  "O4'" . C   C 2 25  ? 132.665 140.231 171.426 1.00 100.82 ? 25  C   C "O4'" 1 
ATOM   9020  C  "C3'" . C   C 2 25  ? 132.774 137.887 171.490 1.00 95.15  ? 25  C   C "C3'" 1 
ATOM   9021  O  "O3'" . C   C 2 25  ? 132.131 136.690 171.081 1.00 102.59 ? 25  C   C "O3'" 1 
ATOM   9022  C  "C2'" . C   C 2 25  ? 133.734 138.376 170.406 1.00 101.88 ? 25  C   C "C2'" 1 
ATOM   9023  O  "O2'" . C   C 2 25  ? 133.184 138.263 169.113 1.00 109.41 ? 25  C   C "O2'" 1 
ATOM   9024  C  "C1'" . C   C 2 25  ? 133.850 139.860 170.757 1.00 97.88  ? 25  C   C "C1'" 1 
ATOM   9025  N  N1    . C   C 2 25  ? 135.010 140.149 171.637 1.00 89.61  ? 25  C   C N1    1 
ATOM   9026  C  C2    . C   C 2 25  ? 136.272 140.214 171.049 1.00 94.65  ? 25  C   C C2    1 
ATOM   9027  O  O2    . C   C 2 25  ? 136.373 140.003 169.833 1.00 99.06  ? 25  C   C O2    1 
ATOM   9028  N  N3    . C   C 2 25  ? 137.344 140.475 171.829 1.00 99.02  ? 25  C   C N3    1 
ATOM   9029  C  C4    . C   C 2 25  ? 137.188 140.695 173.138 1.00 93.12  ? 25  C   C C4    1 
ATOM   9030  N  N4    . C   C 2 25  ? 138.272 140.960 173.850 1.00 101.94 ? 25  C   C N4    1 
ATOM   9031  C  C5    . C   C 2 25  ? 135.908 140.648 173.750 1.00 95.66  ? 25  C   C C5    1 
ATOM   9032  C  C6    . C   C 2 25  ? 134.853 140.380 172.969 1.00 101.23 ? 25  C   C C6    1 
ATOM   9033  P  P     . A   C 2 26  ? 132.728 135.255 171.480 1.00 78.62  ? 26  A   C P     1 
ATOM   9034  O  OP1   . A   C 2 26  ? 132.042 134.115 170.765 1.00 86.95  ? 26  A   C OP1   1 
ATOM   9035  O  OP2   . A   C 2 26  ? 132.788 135.085 172.978 1.00 89.87  ? 26  A   C OP2   1 
ATOM   9036  O  "O5'" . A   C 2 26  ? 134.247 135.276 170.956 1.00 82.25  ? 26  A   C "O5'" 1 
ATOM   9037  C  "C5'" . A   C 2 26  ? 134.510 135.161 169.538 1.00 82.88  ? 26  A   C "C5'" 1 
ATOM   9038  C  "C4'" . A   C 2 26  ? 136.001 135.201 169.323 1.00 89.81  ? 26  A   C "C4'" 1 
ATOM   9039  O  "O4'" . A   C 2 26  ? 136.515 136.490 169.742 1.00 90.53  ? 26  A   C "O4'" 1 
ATOM   9040  C  "C3'" . A   C 2 26  ? 136.813 134.196 170.141 1.00 93.90  ? 26  A   C "C3'" 1 
ATOM   9041  O  "O3'" . A   C 2 26  ? 136.881 132.922 169.518 1.00 81.53  ? 26  A   C "O3'" 1 
ATOM   9042  C  "C2'" . A   C 2 26  ? 138.179 134.879 170.176 1.00 89.52  ? 26  A   C "C2'" 1 
ATOM   9043  O  "O2'" . A   C 2 26  ? 138.897 134.712 168.975 1.00 91.38  ? 26  A   C "O2'" 1 
ATOM   9044  C  "C1'" . A   C 2 26  ? 137.774 136.334 170.357 1.00 86.79  ? 26  A   C "C1'" 1 
ATOM   9045  N  N9    . A   C 2 26  ? 137.664 136.743 171.750 1.00 80.76  ? 26  A   C N9    1 
ATOM   9046  C  C8    . A   C 2 26  ? 136.514 136.852 172.486 1.00 88.42  ? 26  A   C C8    1 
ATOM   9047  N  N7    . A   C 2 26  ? 136.719 137.263 173.710 1.00 87.72  ? 26  A   C N7    1 
ATOM   9048  C  C5    . A   C 2 26  ? 138.090 137.454 173.782 1.00 83.23  ? 26  A   C C5    1 
ATOM   9049  C  C6    . A   C 2 26  ? 138.930 137.889 174.823 1.00 88.55  ? 26  A   C C6    1 
ATOM   9050  N  N6    . A   C 2 26  ? 138.493 138.219 176.033 1.00 92.09  ? 26  A   C N6    1 
ATOM   9051  N  N1    . A   C 2 26  ? 140.255 137.967 174.565 1.00 87.38  ? 26  A   C N1    1 
ATOM   9052  C  C2    . A   C 2 26  ? 140.687 137.629 173.345 1.00 89.93  ? 26  A   C C2    1 
ATOM   9053  N  N3    . A   C 2 26  ? 139.993 137.210 172.293 1.00 95.42  ? 26  A   C N3    1 
ATOM   9054  C  C4    . A   C 2 26  ? 138.683 137.149 172.575 1.00 83.59  ? 26  A   C C4    1 
HETATM 9055  N  N1    . PSU C 2 27  ? 137.665 134.262 174.702 1.00 83.29  ? 27  PSU C N1    1 
HETATM 9056  C  C2    . PSU C 2 27  ? 137.892 134.785 175.943 1.00 85.99  ? 27  PSU C C2    1 
HETATM 9057  N  N3    . PSU C 2 27  ? 139.204 134.871 176.317 1.00 81.11  ? 27  PSU C N3    1 
HETATM 9058  C  C4    . PSU C 2 27  ? 140.263 134.479 175.538 1.00 78.37  ? 27  PSU C C4    1 
HETATM 9059  C  C5    . PSU C 2 27  ? 139.981 133.940 174.275 1.00 82.42  ? 27  PSU C C5    1 
HETATM 9060  C  C6    . PSU C 2 27  ? 138.656 133.848 173.875 1.00 87.03  ? 27  PSU C C6    1 
HETATM 9061  O  O2    . PSU C 2 27  ? 136.985 135.154 176.676 1.00 93.39  ? 27  PSU C O2    1 
HETATM 9062  O  O4    . PSU C 2 27  ? 141.405 134.609 175.989 1.00 93.90  ? 27  PSU C O4    1 
HETATM 9063  C  "C1'" . PSU C 2 27  ? 141.096 133.491 173.371 1.00 83.52  ? 27  PSU C "C1'" 1 
HETATM 9064  C  "C2'" . PSU C 2 27  ? 141.637 132.092 173.676 1.00 79.88  ? 27  PSU C "C2'" 1 
HETATM 9065  O  "O2'" . PSU C 2 27  ? 143.004 131.996 173.336 1.00 76.40  ? 27  PSU C "O2'" 1 
HETATM 9066  C  "C3'" . PSU C 2 27  ? 140.732 131.216 172.808 1.00 79.67  ? 27  PSU C "C3'" 1 
HETATM 9067  C  "C4'" . PSU C 2 27  ? 140.735 132.058 171.533 1.00 88.06  ? 27  PSU C "C4'" 1 
HETATM 9068  O  "O3'" . PSU C 2 27  ? 141.314 129.938 172.596 1.00 77.73  ? 27  PSU C "O3'" 1 
HETATM 9069  O  "O4'" . PSU C 2 27  ? 140.642 133.420 172.010 1.00 84.86  ? 27  PSU C "O4'" 1 
HETATM 9070  C  "C5'" . PSU C 2 27  ? 139.626 131.777 170.552 1.00 102.11 ? 27  PSU C "C5'" 1 
HETATM 9071  O  "O5'" . PSU C 2 27  ? 138.356 131.815 171.248 1.00 82.40  ? 27  PSU C "O5'" 1 
HETATM 9072  P  P     . PSU C 2 27  ? 137.001 131.595 170.410 1.00 0.99   ? 27  PSU C P     1 
HETATM 9073  O  OP1   . PSU C 2 27  ? 137.187 130.345 169.588 1.00 72.49  ? 27  PSU C OP1   1 
HETATM 9074  O  OP2   . PSU C 2 27  ? 135.877 131.509 171.414 1.00 77.13  ? 27  PSU C OP2   1 
ATOM   9075  P  P     . C   C 2 28  ? 140.829 128.671 173.451 1.00 33.63  ? 28  C   C P     1 
ATOM   9076  O  OP1   . C   C 2 28  ? 141.531 127.390 173.066 1.00 76.04  ? 28  C   C OP1   1 
ATOM   9077  O  OP2   . C   C 2 28  ? 139.326 128.554 173.499 1.00 68.48  ? 28  C   C OP2   1 
ATOM   9078  O  "O5'" . C   C 2 28  ? 141.315 129.051 174.932 1.00 79.89  ? 28  C   C "O5'" 1 
ATOM   9079  C  "C5'" . C   C 2 28  ? 142.734 129.131 175.198 1.00 90.25  ? 28  C   C "C5'" 1 
ATOM   9080  C  "C4'" . C   C 2 28  ? 142.938 129.364 176.672 1.00 79.58  ? 28  C   C "C4'" 1 
ATOM   9081  O  "O4'" . C   C 2 28  ? 142.551 130.715 177.024 1.00 79.05  ? 28  C   C "O4'" 1 
ATOM   9082  C  "C3'" . C   C 2 28  ? 142.068 128.517 177.603 1.00 77.51  ? 28  C   C "C3'" 1 
ATOM   9083  O  "O3'" . C   C 2 28  ? 142.516 127.175 177.716 1.00 73.24  ? 28  C   C "O3'" 1 
ATOM   9084  C  "C2'" . C   C 2 28  ? 142.225 129.305 178.904 1.00 85.01  ? 28  C   C "C2'" 1 
ATOM   9085  O  "O2'" . C   C 2 28  ? 143.490 129.130 179.501 1.00 82.42  ? 28  C   C "O2'" 1 
ATOM   9086  C  "C1'" . C   C 2 28  ? 142.148 130.740 178.378 1.00 79.51  ? 28  C   C "C1'" 1 
ATOM   9087  N  N1    . C   C 2 28  ? 140.779 131.309 178.474 1.00 69.45  ? 28  C   C N1    1 
ATOM   9088  C  C2    . C   C 2 28  ? 140.394 131.849 179.700 1.00 69.27  ? 28  C   C C2    1 
ATOM   9089  O  O2    . C   C 2 28  ? 141.199 131.809 180.641 1.00 77.69  ? 28  C   C O2    1 
ATOM   9090  N  N3    . C   C 2 28  ? 139.157 132.378 179.826 1.00 76.16  ? 28  C   C N3    1 
ATOM   9091  C  C4    . C   C 2 28  ? 138.323 132.393 178.783 1.00 89.52  ? 28  C   C C4    1 
ATOM   9092  N  N4    . C   C 2 28  ? 137.125 132.929 178.961 1.00 99.63  ? 28  C   C N4    1 
ATOM   9093  C  C5    . C   C 2 28  ? 138.702 131.852 177.524 1.00 76.36  ? 28  C   C C5    1 
ATOM   9094  C  C6    . C   C 2 28  ? 139.932 131.331 177.410 1.00 78.94  ? 28  C   C C6    1 
ATOM   9095  P  P     . A   C 2 29  ? 141.491 126.019 178.150 1.00 61.81  ? 29  A   C P     1 
ATOM   9096  O  OP1   . A   C 2 29  ? 142.152 124.662 178.207 1.00 93.09  ? 29  A   C OP1   1 
ATOM   9097  O  OP2   . A   C 2 29  ? 140.223 126.049 177.329 1.00 72.83  ? 29  A   C OP2   1 
ATOM   9098  O  "O5'" . A   C 2 29  ? 141.080 126.401 179.654 1.00 87.81  ? 29  A   C "O5'" 1 
ATOM   9099  C  "C5'" . A   C 2 29  ? 142.074 126.273 180.694 1.00 93.81  ? 29  A   C "C5'" 1 
ATOM   9100  C  "C4'" . A   C 2 29  ? 141.434 126.571 182.025 1.00 87.77  ? 29  A   C "C4'" 1 
ATOM   9101  O  "O4'" . A   C 2 29  ? 141.108 127.981 182.117 1.00 87.00  ? 29  A   C "O4'" 1 
ATOM   9102  C  "C3'" . A   C 2 29  ? 140.087 125.897 182.296 1.00 81.59  ? 29  A   C "C3'" 1 
ATOM   9103  O  "O3'" . A   C 2 29  ? 140.184 124.521 182.632 1.00 76.78  ? 29  A   C "O3'" 1 
ATOM   9104  C  "C2'" . A   C 2 29  ? 139.613 126.756 183.467 1.00 87.44  ? 29  A   C "C2'" 1 
ATOM   9105  O  "O2'" . A   C 2 29  ? 140.289 126.467 184.669 1.00 87.45  ? 29  A   C "O2'" 1 
ATOM   9106  C  "C1'" . A   C 2 29  ? 139.979 128.141 182.949 1.00 85.66  ? 29  A   C "C1'" 1 
ATOM   9107  N  N9    . A   C 2 29  ? 138.901 128.752 182.186 1.00 83.70  ? 29  A   C N9    1 
ATOM   9108  C  C8    . A   C 2 29  ? 138.724 128.738 180.827 1.00 82.79  ? 29  A   C C8    1 
ATOM   9109  N  N7    . A   C 2 29  ? 137.650 129.378 180.441 1.00 82.74  ? 29  A   C N7    1 
ATOM   9110  C  C5    . A   C 2 29  ? 137.083 129.842 181.618 1.00 76.80  ? 29  A   C C5    1 
ATOM   9111  C  C6    . A   C 2 29  ? 135.926 130.595 181.881 1.00 78.36  ? 29  A   C C6    1 
ATOM   9112  N  N6    . A   C 2 29  ? 135.097 131.032 180.939 1.00 89.47  ? 29  A   C N6    1 
ATOM   9113  N  N1    . A   C 2 29  ? 135.651 130.883 183.172 1.00 78.51  ? 29  A   C N1    1 
ATOM   9114  C  C2    . A   C 2 29  ? 136.486 130.445 184.119 1.00 81.79  ? 29  A   C C2    1 
ATOM   9115  N  N3    . A   C 2 29  ? 137.599 129.733 183.991 1.00 86.09  ? 29  A   C N3    1 
ATOM   9116  C  C4    . A   C 2 29  ? 137.850 129.467 182.701 1.00 83.97  ? 29  A   C C4    1 
ATOM   9117  P  P     . G   C 2 30  ? 138.951 123.536 182.333 1.00 64.33  ? 30  G   C P     1 
ATOM   9118  O  OP1   . G   C 2 30  ? 139.212 122.125 182.809 1.00 93.10  ? 30  G   C OP1   1 
ATOM   9119  O  OP2   . G   C 2 30  ? 138.497 123.625 180.892 1.00 99.71  ? 30  G   C OP2   1 
ATOM   9120  O  "O5'" . G   C 2 30  ? 137.755 124.122 183.234 1.00 88.99  ? 30  G   C "O5'" 1 
ATOM   9121  C  "C5'" . G   C 2 30  ? 137.905 124.095 184.670 1.00 101.10 ? 30  G   C "C5'" 1 
ATOM   9122  C  "C4'" . G   C 2 30  ? 136.700 124.727 185.317 1.00 99.15  ? 30  G   C "C4'" 1 
ATOM   9123  O  "O4'" . G   C 2 30  ? 136.554 126.106 184.892 1.00 89.48  ? 30  G   C "O4'" 1 
ATOM   9124  C  "C3'" . G   C 2 30  ? 135.342 124.129 184.953 1.00 99.22  ? 30  G   C "C3'" 1 
ATOM   9125  O  "O3'" . G   C 2 30  ? 135.111 122.869 185.567 1.00 101.11 ? 30  G   C "O3'" 1 
ATOM   9126  C  "C2'" . G   C 2 30  ? 134.433 125.239 185.478 1.00 98.87  ? 30  G   C "C2'" 1 
ATOM   9127  O  "O2'" . G   C 2 30  ? 134.295 125.208 186.881 1.00 110.25 ? 30  G   C "O2'" 1 
ATOM   9128  C  "C1'" . G   C 2 30  ? 135.199 126.479 185.026 1.00 84.05  ? 30  G   C "C1'" 1 
ATOM   9129  N  N9    . G   C 2 30  ? 134.709 127.013 183.763 1.00 85.62  ? 30  G   C N9    1 
ATOM   9130  C  C8    . G   C 2 30  ? 135.206 126.791 182.506 1.00 99.55  ? 30  G   C C8    1 
ATOM   9131  N  N7    . G   C 2 30  ? 134.534 127.415 181.569 1.00 101.61 ? 30  G   C N7    1 
ATOM   9132  C  C5    . G   C 2 30  ? 133.533 128.088 182.256 1.00 96.43  ? 30  G   C C5    1 
ATOM   9133  C  C6    . G   C 2 30  ? 132.500 128.929 181.775 1.00 92.93  ? 30  G   C C6    1 
ATOM   9134  O  O6    . G   C 2 30  ? 132.261 129.257 180.605 1.00 86.17  ? 30  G   C O6    1 
ATOM   9135  N  N1    . G   C 2 30  ? 131.704 129.404 182.816 1.00 92.32  ? 30  G   C N1    1 
ATOM   9136  C  C2    . G   C 2 30  ? 131.879 129.108 184.144 1.00 95.81  ? 30  G   C C2    1 
ATOM   9137  N  N2    . G   C 2 30  ? 131.014 129.656 185.006 1.00 95.35  ? 30  G   C N2    1 
ATOM   9138  N  N3    . G   C 2 30  ? 132.846 128.320 184.601 1.00 100.67 ? 30  G   C N3    1 
ATOM   9139  C  C4    . G   C 2 30  ? 133.635 127.854 183.606 1.00 96.10  ? 30  G   C C4    1 
ATOM   9140  P  P     . A   C 2 31  ? 133.854 121.975 185.122 1.00 87.59  ? 31  A   C P     1 
ATOM   9141  O  OP1   . A   C 2 31  ? 133.819 120.619 185.788 1.00 102.21 ? 31  A   C OP1   1 
ATOM   9142  O  OP2   . A   C 2 31  ? 133.676 121.930 183.620 1.00 98.33  ? 31  A   C OP2   1 
ATOM   9143  O  "O5'" . A   C 2 31  ? 132.626 122.823 185.707 1.00 107.09 ? 31  A   C "O5'" 1 
ATOM   9144  C  "C5'" . A   C 2 31  ? 131.328 122.633 185.115 1.00 114.45 ? 31  A   C "C5'" 1 
ATOM   9145  C  "C4'" . A   C 2 31  ? 130.324 123.502 185.825 1.00 109.09 ? 31  A   C "C4'" 1 
ATOM   9146  O  "O4'" . A   C 2 31  ? 130.686 124.897 185.655 1.00 99.09  ? 31  A   C "O4'" 1 
ATOM   9147  C  "C3'" . A   C 2 31  ? 128.886 123.378 185.311 1.00 103.96 ? 31  A   C "C3'" 1 
ATOM   9148  O  "O3'" . A   C 2 31  ? 128.199 122.391 186.069 1.00 98.44  ? 31  A   C "O3'" 1 
ATOM   9149  C  "C2'" . A   C 2 31  ? 128.342 124.795 185.490 1.00 107.42 ? 31  A   C "C2'" 1 
ATOM   9150  O  "O2'" . A   C 2 31  ? 127.885 125.040 186.801 1.00 103.79 ? 31  A   C "O2'" 1 
ATOM   9151  C  "C1'" . A   C 2 31  ? 129.580 125.628 185.179 1.00 102.70 ? 31  A   C "C1'" 1 
ATOM   9152  N  N9    . A   C 2 31  ? 129.789 125.893 183.761 1.00 98.46  ? 31  A   C N9    1 
ATOM   9153  C  C8    . A   C 2 31  ? 130.794 125.390 182.976 1.00 101.04 ? 31  A   C C8    1 
ATOM   9154  N  N7    . A   C 2 31  ? 130.758 125.825 181.744 1.00 109.04 ? 31  A   C N7    1 
ATOM   9155  C  C5    . A   C 2 31  ? 129.674 126.687 181.718 1.00 104.37 ? 31  A   C C5    1 
ATOM   9156  C  C6    . A   C 2 31  ? 129.114 127.468 180.692 1.00 105.04 ? 31  A   C C6    1 
ATOM   9157  N  N6    . A   C 2 31  ? 129.587 127.502 179.450 1.00 106.85 ? 31  A   C N6    1 
ATOM   9158  N  N1    . A   C 2 31  ? 128.032 128.218 180.998 1.00 101.05 ? 31  A   C N1    1 
ATOM   9159  C  C2    . A   C 2 31  ? 127.559 128.174 182.249 1.00 101.10 ? 31  A   C C2    1 
ATOM   9160  N  N3    . A   C 2 31  ? 128.003 127.481 183.292 1.00 104.56 ? 31  A   C N3    1 
ATOM   9161  C  C4    . A   C 2 31  ? 129.082 126.755 182.962 1.00 101.47 ? 31  A   C C4    1 
ATOM   9162  P  P     . C   C 2 32  ? 127.883 120.949 185.437 1.00 104.30 ? 32  C   C P     1 
ATOM   9163  O  OP1   . C   C 2 32  ? 127.503 119.911 186.468 1.00 116.53 ? 32  C   C OP1   1 
ATOM   9164  O  OP2   . C   C 2 32  ? 128.912 120.479 184.434 1.00 114.71 ? 32  C   C OP2   1 
ATOM   9165  O  "O5'" . C   C 2 32  ? 126.554 121.301 184.612 1.00 115.34 ? 32  C   C "O5'" 1 
ATOM   9166  C  "C5'" . C   C 2 32  ? 125.411 121.791 185.348 1.00 120.97 ? 32  C   C "C5'" 1 
ATOM   9167  C  "C4'" . C   C 2 32  ? 124.606 122.705 184.461 1.00 116.48 ? 32  C   C "C4'" 1 
ATOM   9168  O  "O4'" . C   C 2 32  ? 125.404 123.855 184.075 1.00 112.05 ? 32  C   C "O4'" 1 
ATOM   9169  C  "C3'" . C   C 2 32  ? 124.160 122.123 183.115 1.00 115.42 ? 32  C   C "C3'" 1 
ATOM   9170  O  "O3'" . C   C 2 32  ? 123.069 121.221 183.245 1.00 112.36 ? 32  C   C "O3'" 1 
ATOM   9171  C  "C2'" . C   C 2 32  ? 123.802 123.418 182.384 1.00 117.19 ? 32  C   C "C2'" 1 
ATOM   9172  O  "O2'" . C   C 2 32  ? 122.594 123.982 182.844 1.00 118.29 ? 32  C   C "O2'" 1 
ATOM   9173  C  "C1'" . C   C 2 32  ? 124.973 124.309 182.810 1.00 112.13 ? 32  C   C "C1'" 1 
ATOM   9174  N  N1    . C   C 2 32  ? 126.101 124.232 181.847 1.00 112.36 ? 32  C   C N1    1 
ATOM   9175  C  C2    . C   C 2 32  ? 126.036 125.046 180.717 1.00 117.10 ? 32  C   C C2    1 
ATOM   9176  O  O2    . C   C 2 32  ? 125.053 125.790 180.580 1.00 121.61 ? 32  C   C O2    1 
ATOM   9177  N  N3    . C   C 2 32  ? 127.028 124.977 179.802 1.00 116.24 ? 32  C   C N3    1 
ATOM   9178  C  C4    . C   C 2 32  ? 128.062 124.150 179.988 1.00 117.60 ? 32  C   C C4    1 
ATOM   9179  N  N4    . C   C 2 32  ? 129.013 124.137 179.068 1.00 122.69 ? 32  C   C N4    1 
ATOM   9180  C  C5    . C   C 2 32  ? 128.149 123.320 181.137 1.00 119.68 ? 32  C   C C5    1 
ATOM   9181  C  C6    . C   C 2 32  ? 127.156 123.391 182.035 1.00 117.90 ? 32  C   C C6    1 
ATOM   9182  P  P     . U   C 2 33  ? 123.238 119.668 182.870 1.00 113.29 ? 33  U   C P     1 
ATOM   9183  O  OP1   . U   C 2 33  ? 122.452 118.758 183.787 1.00 117.21 ? 33  U   C OP1   1 
ATOM   9184  O  OP2   . U   C 2 33  ? 124.695 119.288 182.742 1.00 115.36 ? 33  U   C OP2   1 
ATOM   9185  O  "O5'" . U   C 2 33  ? 122.599 119.519 181.399 1.00 124.11 ? 33  U   C "O5'" 1 
ATOM   9186  C  "C5'" . U   C 2 33  ? 123.291 120.114 180.275 1.00 121.84 ? 33  U   C "C5'" 1 
ATOM   9187  C  "C4'" . U   C 2 33  ? 122.465 119.963 179.019 1.00 122.28 ? 33  U   C "C4'" 1 
ATOM   9188  O  "O4'" . U   C 2 33  ? 122.847 118.754 178.309 1.00 118.08 ? 33  U   C "O4'" 1 
ATOM   9189  C  "C3'" . U   C 2 33  ? 120.944 119.866 179.211 1.00 119.10 ? 33  U   C "C3'" 1 
ATOM   9190  O  "O3'" . U   C 2 33  ? 120.325 120.573 178.145 1.00 115.59 ? 33  U   C "O3'" 1 
ATOM   9191  C  "C2'" . U   C 2 33  ? 120.703 118.352 179.183 1.00 113.97 ? 33  U   C "C2'" 1 
ATOM   9192  O  "O2'" . U   C 2 33  ? 119.411 117.989 178.747 1.00 116.85 ? 33  U   C "O2'" 1 
ATOM   9193  C  "C1'" . U   C 2 33  ? 121.714 117.935 178.121 1.00 115.71 ? 33  U   C "C1'" 1 
ATOM   9194  N  N1    . U   C 2 33  ? 122.137 116.527 178.221 1.00 114.98 ? 33  U   C N1    1 
ATOM   9195  C  C2    . U   C 2 33  ? 122.369 115.863 177.033 1.00 118.98 ? 33  U   C C2    1 
ATOM   9196  O  O2    . U   C 2 33  ? 122.184 116.379 175.941 1.00 125.00 ? 33  U   C O2    1 
ATOM   9197  N  N3    . U   C 2 33  ? 122.783 114.565 177.168 1.00 119.44 ? 33  U   C N3    1 
ATOM   9198  C  C4    . U   C 2 33  ? 123.010 113.887 178.348 1.00 121.14 ? 33  U   C C4    1 
ATOM   9199  O  O4    . U   C 2 33  ? 123.382 112.716 178.304 1.00 122.58 ? 33  U   C O4    1 
ATOM   9200  C  C5    . U   C 2 33  ? 122.770 114.651 179.537 1.00 120.63 ? 33  U   C C5    1 
ATOM   9201  C  C6    . U   C 2 33  ? 122.358 115.923 179.434 1.00 118.60 ? 33  U   C C6    1 
HETATM 9202  N  N1    . 70U C 2 34  ? 117.526 120.770 172.499 1.00 115.71 ? 34  70U C N1    1 
HETATM 9203  C  C2    . 70U C 2 34  ? 116.685 120.551 171.448 1.00 120.35 ? 34  70U C C2    1 
HETATM 9204  S  S2    . 70U C 2 34  ? 115.972 121.830 170.675 1.00 129.23 ? 34  70U C S2    1 
HETATM 9205  N  N3    . 70U C 2 34  ? 116.446 119.273 171.073 1.00 122.48 ? 34  70U C N3    1 
HETATM 9206  C  C4    . 70U C 2 34  ? 117.058 118.209 171.722 1.00 122.33 ? 34  70U C C4    1 
HETATM 9207  O  O4    . 70U C 2 34  ? 116.615 117.077 171.532 1.00 124.21 ? 34  70U C O4    1 
HETATM 9208  C  C5    . 70U C 2 34  ? 118.136 118.487 172.528 1.00 122.48 ? 34  70U C C5    1 
HETATM 9209  C  C6    . 70U C 2 34  ? 118.360 119.782 172.932 1.00 124.09 ? 34  70U C C6    1 
HETATM 9210  C  C5M   . 70U C 2 34  ? 119.069 117.395 172.981 1.00 121.06 ? 34  70U C C5M   1 
HETATM 9211  C  C8    . 70U C 2 34  ? 118.729 116.763 174.306 1.00 118.16 ? 34  70U C C8    1 
HETATM 9212  O  O8    . 70U C 2 34  ? 119.338 115.865 174.815 1.00 120.38 ? 34  70U C O8    1 
HETATM 9213  O  O9    . 70U C 2 34  ? 117.658 117.335 174.852 1.00 120.30 ? 34  70U C O9    1 
HETATM 9214  C  C9    . 70U C 2 34  ? 117.278 116.843 176.158 1.00 121.23 ? 34  70U C C9    1 
HETATM 9215  C  "C1'" . 70U C 2 34  ? 117.435 122.094 173.167 1.00 116.07 ? 34  70U C "C1'" 1 
HETATM 9216  O  "O2'" . 70U C 2 34  ? 115.180 122.195 174.066 1.00 118.50 ? 34  70U C "O2'" 1 
HETATM 9217  C  "C2'" . 70U C 2 34  ? 116.547 122.030 174.402 1.00 119.62 ? 34  70U C "C2'" 1 
HETATM 9218  O  "O3'" . 70U C 2 34  ? 116.564 124.412 174.774 1.00 110.56 ? 34  70U C "O3'" 1 
HETATM 9219  C  "C3'" . 70U C 2 34  ? 117.108 123.179 175.226 1.00 120.83 ? 34  70U C "C3'" 1 
HETATM 9220  C  "C4'" . 70U C 2 34  ? 118.611 123.036 174.955 1.00 117.39 ? 34  70U C "C4'" 1 
HETATM 9221  O  "O4'" . 70U C 2 34  ? 118.710 122.456 173.632 1.00 113.56 ? 34  70U C "O4'" 1 
HETATM 9222  C  "C5'" . 70U C 2 34  ? 119.360 122.151 175.916 1.00 116.91 ? 34  70U C "C5'" 1 
HETATM 9223  O  "O5'" . 70U C 2 34  ? 118.728 122.228 177.212 1.00 117.53 ? 34  70U C "O5'" 1 
HETATM 9224  P  P     . 70U C 2 34  ? 118.761 120.931 178.156 1.00 105.79 ? 34  70U C P     1 
HETATM 9225  O  OP1   . 70U C 2 34  ? 118.249 121.356 179.514 1.00 113.33 ? 34  70U C OP1   1 
HETATM 9226  O  OP2   . 70U C 2 34  ? 117.913 119.876 177.482 1.00 122.73 ? 34  70U C OP2   1 
ATOM   9227  P  P     . U   C 2 35  ? 117.058 125.818 175.371 1.00 72.85  ? 35  U   C P     1 
ATOM   9228  O  OP1   . U   C 2 35  ? 117.509 125.710 176.811 1.00 97.66  ? 35  U   C OP1   1 
ATOM   9229  O  OP2   . U   C 2 35  ? 116.064 126.931 175.123 1.00 92.70  ? 35  U   C OP2   1 
ATOM   9230  O  "O5'" . U   C 2 35  ? 118.358 126.150 174.482 1.00 107.20 ? 35  U   C "O5'" 1 
ATOM   9231  C  "C5'" . U   C 2 35  ? 119.447 126.873 175.101 1.00 105.79 ? 35  U   C "C5'" 1 
ATOM   9232  C  "C4'" . U   C 2 35  ? 120.496 127.184 174.066 1.00 96.09  ? 35  U   C "C4'" 1 
ATOM   9233  O  "O4'" . U   C 2 35  ? 120.809 126.003 173.286 1.00 97.12  ? 35  U   C "O4'" 1 
ATOM   9234  C  "C3'" . U   C 2 35  ? 120.100 128.199 172.992 1.00 95.37  ? 35  U   C "C3'" 1 
ATOM   9235  O  "O3'" . U   C 2 35  ? 120.129 129.532 173.478 1.00 91.50  ? 35  U   C "O3'" 1 
ATOM   9236  C  "C2'" . U   C 2 35  ? 121.189 127.927 171.953 1.00 96.96  ? 35  U   C "C2'" 1 
ATOM   9237  O  "O2'" . U   C 2 35  ? 122.440 128.464 172.316 1.00 103.01 ? 35  U   C "O2'" 1 
ATOM   9238  C  "C1'" . U   C 2 35  ? 121.296 126.406 172.022 1.00 92.73  ? 35  U   C "C1'" 1 
ATOM   9239  N  N1    . U   C 2 35  ? 120.512 125.756 170.962 1.00 93.37  ? 35  U   C N1    1 
ATOM   9240  C  C2    . U   C 2 35  ? 121.113 125.652 169.724 1.00 103.53 ? 35  U   C C2    1 
ATOM   9241  O  O2    . U   C 2 35  ? 122.232 126.089 169.493 1.00 108.47 ? 35  U   C O2    1 
ATOM   9242  N  N3    . U   C 2 35  ? 120.351 125.043 168.764 1.00 103.94 ? 35  U   C N3    1 
ATOM   9243  C  C4    . U   C 2 35  ? 119.083 124.524 168.918 1.00 100.59 ? 35  U   C C4    1 
ATOM   9244  O  O4    . U   C 2 35  ? 118.529 124.001 167.954 1.00 105.87 ? 35  U   C O4    1 
ATOM   9245  C  C5    . U   C 2 35  ? 118.531 124.664 170.232 1.00 102.66 ? 35  U   C C5    1 
ATOM   9246  C  C6    . U   C 2 35  ? 119.252 125.262 171.191 1.00 101.95 ? 35  U   C C6    1 
ATOM   9247  P  P     . U   C 2 36  ? 119.767 130.764 172.515 1.00 94.17  ? 36  U   C P     1 
ATOM   9248  O  OP1   . U   C 2 36  ? 119.758 132.090 173.237 1.00 104.65 ? 36  U   C OP1   1 
ATOM   9249  O  OP2   . U   C 2 36  ? 118.522 130.505 171.702 1.00 103.44 ? 36  U   C OP2   1 
ATOM   9250  O  "O5'" . U   C 2 36  ? 120.995 130.807 171.483 1.00 111.60 ? 36  U   C "O5'" 1 
ATOM   9251  C  "C5'" . U   C 2 36  ? 121.024 131.855 170.499 1.00 109.00 ? 36  U   C "C5'" 1 
ATOM   9252  C  "C4'" . U   C 2 36  ? 121.780 131.380 169.286 1.00 102.59 ? 36  U   C "C4'" 1 
ATOM   9253  O  "O4'" . U   C 2 36  ? 121.615 129.948 169.133 1.00 99.33  ? 36  U   C "O4'" 1 
ATOM   9254  C  "C3'" . U   C 2 36  ? 121.302 131.981 167.962 1.00 103.71 ? 36  U   C "C3'" 1 
ATOM   9255  O  "O3'" . U   C 2 36  ? 122.015 133.176 167.695 1.00 102.46 ? 36  U   C "O3'" 1 
ATOM   9256  C  "C2'" . U   C 2 36  ? 121.650 130.891 166.948 1.00 104.49 ? 36  U   C "C2'" 1 
ATOM   9257  O  "O2'" . U   C 2 36  ? 122.995 130.955 166.526 1.00 108.54 ? 36  U   C "O2'" 1 
ATOM   9258  C  "C1'" . U   C 2 36  ? 121.451 129.618 167.770 1.00 101.06 ? 36  U   C "C1'" 1 
ATOM   9259  N  N1    . U   C 2 36  ? 120.119 129.009 167.590 1.00 100.88 ? 36  U   C N1    1 
ATOM   9260  C  C2    . U   C 2 36  ? 119.885 128.343 166.403 1.00 106.19 ? 36  U   C C2    1 
ATOM   9261  O  O2    . U   C 2 36  ? 120.706 128.287 165.498 1.00 107.21 ? 36  U   C O2    1 
ATOM   9262  N  N3    . U   C 2 36  ? 118.641 127.783 166.293 1.00 104.46 ? 36  U   C N3    1 
ATOM   9263  C  C4    . U   C 2 36  ? 117.639 127.789 167.241 1.00 102.78 ? 36  U   C C4    1 
ATOM   9264  O  O4    . U   C 2 36  ? 116.573 127.229 166.993 1.00 111.52 ? 36  U   C O4    1 
ATOM   9265  C  C5    . U   C 2 36  ? 117.968 128.474 168.456 1.00 95.88  ? 36  U   C C5    1 
ATOM   9266  C  C6    . U   C 2 36  ? 119.176 129.041 168.588 1.00 96.03  ? 36  U   C C6    1 
HETATM 9267  P  P     . 12A C 2 37  ? 121.455 134.266 166.651 1.00 20.00  ? 37  12A C P     1 
HETATM 9268  O  OP1   . 12A C 2 37  ? 120.509 135.243 167.323 1.00 20.00  ? 37  12A C OP1   1 
HETATM 9269  O  OP2   . 12A C 2 37  ? 120.900 133.664 165.372 1.00 20.00  ? 37  12A C OP2   1 
HETATM 9270  O  "O5'" . 12A C 2 37  ? 122.758 135.114 166.222 1.00 20.00  ? 37  12A C "O5'" 1 
HETATM 9271  C  "C5'" . 12A C 2 37  ? 123.859 134.427 165.572 1.00 20.00  ? 37  12A C "C5'" 1 
HETATM 9272  C  "C4'" . 12A C 2 37  ? 125.116 134.585 166.393 1.00 20.00  ? 37  12A C "C4'" 1 
HETATM 9273  O  "O4'" . 12A C 2 37  ? 125.336 135.992 166.671 1.00 20.00  ? 37  12A C "O4'" 1 
HETATM 9274  C  "C3'" . 12A C 2 37  ? 125.113 133.911 167.771 1.00 20.00  ? 37  12A C "C3'" 1 
HETATM 9275  O  "O3'" . 12A C 2 37  ? 126.446 133.611 168.161 1.00 20.00  ? 37  12A C "O3'" 1 
HETATM 9276  C  "C2'" . 12A C 2 37  ? 124.514 135.013 168.646 1.00 20.00  ? 37  12A C "C2'" 1 
HETATM 9277  O  "O2'" . 12A C 2 37  ? 124.781 134.866 170.023 1.00 20.00  ? 37  12A C "O2'" 1 
HETATM 9278  C  "C1'" . 12A C 2 37  ? 125.239 136.218 168.060 1.00 20.00  ? 37  12A C "C1'" 1 
HETATM 9279  N  N9    . 12A C 2 37  ? 124.583 137.500 168.280 1.00 20.00  ? 37  12A C N9    1 
HETATM 9280  C  C8    . 12A C 2 37  ? 123.260 137.824 168.109 1.00 20.00  ? 37  12A C C8    1 
HETATM 9281  N  N7    . 12A C 2 37  ? 123.000 139.084 168.361 1.00 20.00  ? 37  12A C N7    1 
HETATM 9282  C  C5    . 12A C 2 37  ? 124.230 139.630 168.701 1.00 20.00  ? 37  12A C C5    1 
HETATM 9283  C  C6    . 12A C 2 37  ? 124.625 140.925 169.074 1.00 20.00  ? 37  12A C C6    1 
HETATM 9284  N  N6    . 12A C 2 37  ? 123.742 142.009 169.177 1.00 20.00  ? 37  12A C N6    1 
HETATM 9285  N  N1    . 12A C 2 37  ? 125.924 141.144 169.347 1.00 20.00  ? 37  12A C N1    1 
HETATM 9286  C  C2    . 12A C 2 37  ? 126.790 140.106 169.252 1.00 20.00  ? 37  12A C C2    1 
HETATM 9287  N  N3    . 12A C 2 37  ? 126.510 138.858 168.909 1.00 20.00  ? 37  12A C N3    1 
HETATM 9288  C  C4    . 12A C 2 37  ? 125.214 138.665 168.630 1.00 20.00  ? 37  12A C C4    1 
HETATM 9289  S  S2    . 12A C 2 37  ? 128.503 140.354 169.608 1.00 20.00  ? 37  12A C S2    1 
HETATM 9290  C  C2M   . 12A C 2 37  ? 129.325 138.797 169.188 1.00 20.00  ? 37  12A C C2M   1 
HETATM 9291  C  CC    . 12A C 2 37  ? 124.044 143.287 169.547 1.00 20.00  ? 37  12A C CC    1 
HETATM 9292  O  OO    . 12A C 2 37  ? 123.256 144.232 169.447 1.00 20.00  ? 37  12A C OO    1 
HETATM 9293  N  N     . 12A C 2 37  ? 125.287 143.429 170.039 1.00 20.00  ? 37  12A C N     1 
HETATM 9294  C  CA    . 12A C 2 37  ? 125.922 144.706 170.304 1.00 20.00  ? 37  12A C CA    1 
HETATM 9295  C  C     . 12A C 2 37  ? 127.191 144.872 169.451 1.00 20.00  ? 37  12A C C     1 
HETATM 9296  O  O     . 12A C 2 37  ? 127.672 146.018 169.355 1.00 20.00  ? 37  12A C O     1 
HETATM 9297  O  OXT   . 12A C 2 37  ? 127.655 143.849 168.911 1.00 20.00  ? 37  12A C OXT   1 
HETATM 9298  C  CB    . 12A C 2 37  ? 126.267 144.829 171.800 1.00 20.00  ? 37  12A C CB    1 
HETATM 9299  O  OG1   . 12A C 2 37  ? 126.959 146.059 172.019 1.00 20.00  ? 37  12A C OG1   1 
HETATM 9300  C  CG2   . 12A C 2 37  ? 127.110 143.672 172.290 1.00 20.00  ? 37  12A C CG2   1 
ATOM   9301  P  P     . A   C 2 38  ? 126.785 132.416 169.182 1.00 58.45  ? 38  A   C P     1 
ATOM   9302  O  OP1   . A   C 2 38  ? 128.227 132.469 169.622 1.00 97.08  ? 38  A   C OP1   1 
ATOM   9303  O  OP2   . A   C 2 38  ? 126.360 131.078 168.636 1.00 97.50  ? 38  A   C OP2   1 
ATOM   9304  O  "O5'" . A   C 2 38  ? 125.882 132.724 170.475 1.00 90.52  ? 38  A   C "O5'" 1 
ATOM   9305  C  "C5'" . A   C 2 38  ? 125.812 131.736 171.525 1.00 101.14 ? 38  A   C "C5'" 1 
ATOM   9306  C  "C4'" . A   C 2 38  ? 124.610 132.022 172.388 1.00 96.53  ? 38  A   C "C4'" 1 
ATOM   9307  O  "O4'" . A   C 2 38  ? 123.968 130.770 172.737 1.00 90.99  ? 38  A   C "O4'" 1 
ATOM   9308  C  "C3'" . A   C 2 38  ? 124.893 132.704 173.729 1.00 94.13  ? 38  A   C "C3'" 1 
ATOM   9309  O  "O3'" . A   C 2 38  ? 124.900 134.121 173.634 1.00 95.14  ? 38  A   C "O3'" 1 
ATOM   9310  C  "C2'" . A   C 2 38  ? 123.701 132.240 174.564 1.00 94.86  ? 38  A   C "C2'" 1 
ATOM   9311  O  "O2'" . A   C 2 38  ? 122.541 133.003 174.320 1.00 97.34  ? 38  A   C "O2'" 1 
ATOM   9312  C  "C1'" . A   C 2 38  ? 123.521 130.810 174.072 1.00 93.38  ? 38  A   C "C1'" 1 
ATOM   9313  N  N9    . A   C 2 38  ? 124.271 129.827 174.840 1.00 97.14  ? 38  A   C N9    1 
ATOM   9314  C  C8    . A   C 2 38  ? 125.437 129.209 174.470 1.00 99.12  ? 38  A   C C8    1 
ATOM   9315  N  N7    . A   C 2 38  ? 125.869 128.349 175.356 1.00 102.86 ? 38  A   C N7    1 
ATOM   9316  C  C5    . A   C 2 38  ? 124.920 128.389 176.365 1.00 98.90  ? 38  A   C C5    1 
ATOM   9317  C  C6    . A   C 2 38  ? 124.811 127.703 177.587 1.00 101.03 ? 38  A   C C6    1 
ATOM   9318  N  N6    . A   C 2 38  ? 125.698 126.811 178.013 1.00 107.67 ? 38  A   C N6    1 
ATOM   9319  N  N1    . A   C 2 38  ? 123.739 127.978 178.364 1.00 94.36  ? 38  A   C N1    1 
ATOM   9320  C  C2    . A   C 2 38  ? 122.851 128.879 177.929 1.00 94.97  ? 38  A   C C2    1 
ATOM   9321  N  N3    . A   C 2 38  ? 122.851 129.585 176.803 1.00 99.05  ? 38  A   C N3    1 
ATOM   9322  C  C4    . A   C 2 38  ? 123.919 129.284 176.050 1.00 99.06  ? 38  A   C C4    1 
HETATM 9323  N  N1    . PSU C 2 39  ? 127.032 131.096 177.141 1.00 94.87  ? 39  PSU C N1    1 
HETATM 9324  C  C2    . PSU C 2 39  ? 127.557 130.152 177.976 1.00 97.28  ? 39  PSU C C2    1 
HETATM 9325  N  N3    . PSU C 2 39  ? 126.884 129.961 179.151 1.00 103.20 ? 39  PSU C N3    1 
HETATM 9326  C  C4    . PSU C 2 39  ? 125.747 130.638 179.522 1.00 104.21 ? 39  PSU C C4    1 
HETATM 9327  C  C5    . PSU C 2 39  ? 125.254 131.609 178.638 1.00 100.61 ? 39  PSU C C5    1 
HETATM 9328  C  C6    . PSU C 2 39  ? 125.918 131.809 177.436 1.00 103.36 ? 39  PSU C C6    1 
HETATM 9329  O  O2    . PSU C 2 39  ? 128.564 129.515 177.695 1.00 99.49  ? 39  PSU C O2    1 
HETATM 9330  O  O4    . PSU C 2 39  ? 125.228 130.377 180.615 1.00 107.92 ? 39  PSU C O4    1 
HETATM 9331  C  "C1'" . PSU C 2 39  ? 124.004 132.379 178.971 1.00 96.81  ? 39  PSU C "C1'" 1 
HETATM 9332  C  "C2'" . PSU C 2 39  ? 124.193 133.529 179.964 1.00 94.37  ? 39  PSU C "C2'" 1 
HETATM 9333  O  "O2'" . PSU C 2 39  ? 123.022 133.734 180.725 1.00 94.92  ? 39  PSU C "O2'" 1 
HETATM 9334  C  "C3'" . PSU C 2 39  ? 124.523 134.699 179.036 1.00 92.46  ? 39  PSU C "C3'" 1 
HETATM 9335  C  "C4'" . PSU C 2 39  ? 123.522 134.435 177.911 1.00 97.77  ? 39  PSU C "C4'" 1 
HETATM 9336  O  "O3'" . PSU C 2 39  ? 124.252 135.934 179.685 1.00 96.42  ? 39  PSU C "O3'" 1 
HETATM 9337  O  "O4'" . PSU C 2 39  ? 123.469 132.994 177.790 1.00 101.10 ? 39  PSU C "O4'" 1 
HETATM 9338  C  "C5'" . PSU C 2 39  ? 123.856 135.046 176.573 1.00 101.47 ? 39  PSU C "C5'" 1 
HETATM 9339  O  "O5'" . PSU C 2 39  ? 125.157 134.578 176.150 1.00 95.33  ? 39  PSU C "O5'" 1 
HETATM 9340  P  P     . PSU C 2 39  ? 125.706 135.010 174.702 1.00 86.04  ? 39  PSU C P     1 
HETATM 9341  O  OP1   . PSU C 2 39  ? 125.411 136.486 174.565 1.00 99.96  ? 39  PSU C OP1   1 
HETATM 9342  O  OP2   . PSU C 2 39  ? 127.180 134.680 174.681 1.00 94.28  ? 39  PSU C OP2   1 
ATOM   9343  P  P     . C   C 2 40  ? 125.422 136.744 180.427 1.00 76.37  ? 40  C   C P     1 
ATOM   9344  O  OP1   . C   C 2 40  ? 124.943 138.045 181.032 1.00 99.66  ? 40  C   C OP1   1 
ATOM   9345  O  OP2   . C   C 2 40  ? 126.648 136.888 179.553 1.00 94.96  ? 40  C   C OP2   1 
ATOM   9346  O  "O5'" . C   C 2 40  ? 125.831 135.783 181.647 1.00 101.98 ? 40  C   C "O5'" 1 
ATOM   9347  C  "C5'" . C   C 2 40  ? 124.902 135.613 182.741 1.00 104.05 ? 40  C   C "C5'" 1 
ATOM   9348  C  "C4'" . C   C 2 40  ? 125.519 134.685 183.753 1.00 100.75 ? 40  C   C "C4'" 1 
ATOM   9349  O  "O4'" . C   C 2 40  ? 125.676 133.364 183.177 1.00 105.98 ? 40  C   C "O4'" 1 
ATOM   9350  C  "C3'" . C   C 2 40  ? 126.938 135.045 184.200 1.00 101.29 ? 40  C   C "C3'" 1 
ATOM   9351  O  "O3'" . C   C 2 40  ? 126.951 136.086 185.167 1.00 99.78  ? 40  C   C "O3'" 1 
ATOM   9352  C  "C2'" . C   C 2 40  ? 127.401 133.703 184.766 1.00 104.82 ? 40  C   C "C2'" 1 
ATOM   9353  O  "O2'" . C   C 2 40  ? 126.813 133.406 186.012 1.00 110.46 ? 40  C   C "O2'" 1 
ATOM   9354  C  "C1'" . C   C 2 40  ? 126.817 132.742 183.729 1.00 96.02  ? 40  C   C "C1'" 1 
ATOM   9355  N  N1    . C   C 2 40  ? 127.773 132.423 182.638 1.00 90.39  ? 40  C   C N1    1 
ATOM   9356  C  C2    . C   C 2 40  ? 128.720 131.431 182.884 1.00 101.60 ? 40  C   C C2    1 
ATOM   9357  O  O2    . C   C 2 40  ? 128.733 130.891 183.999 1.00 103.65 ? 40  C   C O2    1 
ATOM   9358  N  N3    . C   C 2 40  ? 129.603 131.111 181.912 1.00 108.78 ? 40  C   C N3    1 
ATOM   9359  C  C4    . C   C 2 40  ? 129.550 131.721 180.724 1.00 101.68 ? 40  C   C C4    1 
ATOM   9360  N  N4    . C   C 2 40  ? 130.436 131.363 179.807 1.00 100.96 ? 40  C   C N4    1 
ATOM   9361  C  C5    . C   C 2 40  ? 128.581 132.723 180.451 1.00 100.41 ? 40  C   C C5    1 
ATOM   9362  C  C6    . C   C 2 40  ? 127.714 133.037 181.424 1.00 103.41 ? 40  C   C C6    1 
ATOM   9363  P  P     . U   C 2 41  ? 128.260 136.995 185.359 1.00 78.65  ? 41  U   C P     1 
ATOM   9364  O  OP1   . U   C 2 41  ? 128.055 138.119 186.349 1.00 93.52  ? 41  U   C OP1   1 
ATOM   9365  O  OP2   . U   C 2 41  ? 128.820 137.443 184.027 1.00 93.06  ? 41  U   C OP2   1 
ATOM   9366  O  "O5'" . U   C 2 41  ? 129.336 135.991 186.003 1.00 93.13  ? 41  U   C "O5'" 1 
ATOM   9367  C  "C5'" . U   C 2 41  ? 129.093 135.472 187.331 1.00 98.89  ? 41  U   C "C5'" 1 
ATOM   9368  C  "C4'" . U   C 2 41  ? 130.297 134.676 187.763 1.00 94.04  ? 41  U   C "C4'" 1 
ATOM   9369  O  "O4'" . U   C 2 41  ? 130.375 133.441 187.007 1.00 99.31  ? 41  U   C "O4'" 1 
ATOM   9370  C  "C3'" . U   C 2 41  ? 131.652 135.338 187.497 1.00 94.71  ? 41  U   C "C3'" 1 
ATOM   9371  O  "O3'" . U   C 2 41  ? 131.949 136.343 188.457 1.00 86.83  ? 41  U   C "O3'" 1 
ATOM   9372  C  "C2'" . U   C 2 41  ? 132.572 134.119 187.571 1.00 103.52 ? 41  U   C "C2'" 1 
ATOM   9373  O  "O2'" . U   C 2 41  ? 132.765 133.661 188.891 1.00 98.84  ? 41  U   C "O2'" 1 
ATOM   9374  C  "C1'" . U   C 2 41  ? 131.731 133.091 186.817 1.00 101.23 ? 41  U   C "C1'" 1 
ATOM   9375  N  N1    . U   C 2 41  ? 132.021 133.075 185.373 1.00 92.55  ? 41  U   C N1    1 
ATOM   9376  C  C2    . U   C 2 41  ? 133.077 132.290 184.958 1.00 87.53  ? 41  U   C C2    1 
ATOM   9377  O  O2    . U   C 2 41  ? 133.767 131.639 185.730 1.00 92.32  ? 41  U   C O2    1 
ATOM   9378  N  N3    . U   C 2 41  ? 133.308 132.304 183.610 1.00 84.83  ? 41  U   C N3    1 
ATOM   9379  C  C4    . U   C 2 41  ? 132.601 132.997 182.652 1.00 94.44  ? 41  U   C C4    1 
ATOM   9380  O  O4    . U   C 2 41  ? 132.935 132.900 181.473 1.00 105.31 ? 41  U   C O4    1 
ATOM   9381  C  C5    . U   C 2 41  ? 131.516 133.783 183.159 1.00 94.04  ? 41  U   C C5    1 
ATOM   9382  C  C6    . U   C 2 41  ? 131.267 133.790 184.476 1.00 94.48  ? 41  U   C C6    1 
ATOM   9383  P  P     . G   C 2 42  ? 132.873 137.594 188.058 1.00 40.61  ? 42  G   C P     1 
ATOM   9384  O  OP1   . G   C 2 42  ? 133.003 138.602 189.177 1.00 80.13  ? 42  G   C OP1   1 
ATOM   9385  O  OP2   . G   C 2 42  ? 132.481 138.196 186.727 1.00 90.30  ? 42  G   C OP2   1 
ATOM   9386  O  "O5'" . G   C 2 42  ? 134.319 136.928 187.854 1.00 86.37  ? 42  G   C "O5'" 1 
ATOM   9387  C  "C5'" . G   C 2 42  ? 135.037 136.475 189.022 1.00 98.78  ? 42  G   C "C5'" 1 
ATOM   9388  C  "C4'" . G   C 2 42  ? 136.252 135.703 188.580 1.00 95.31  ? 42  G   C "C4'" 1 
ATOM   9389  O  "O4'" . G   C 2 42  ? 135.838 134.620 187.709 1.00 95.42  ? 42  G   C "O4'" 1 
ATOM   9390  C  "C3'" . G   C 2 42  ? 137.274 136.466 187.733 1.00 92.53  ? 42  G   C "C3'" 1 
ATOM   9391  O  "O3'" . G   C 2 42  ? 138.154 137.291 188.483 1.00 79.43  ? 42  G   C "O3'" 1 
ATOM   9392  C  "C2'" . G   C 2 42  ? 138.016 135.291 187.100 1.00 96.23  ? 42  G   C "C2'" 1 
ATOM   9393  O  "O2'" . G   C 2 42  ? 138.886 134.644 188.001 1.00 100.32 ? 42  G   C "O2'" 1 
ATOM   9394  C  "C1'" . G   C 2 42  ? 136.842 134.389 186.746 1.00 85.88  ? 42  G   C "C1'" 1 
ATOM   9395  N  N9    . G   C 2 42  ? 136.310 134.652 185.417 1.00 78.10  ? 42  G   C N9    1 
ATOM   9396  C  C8    . G   C 2 42  ? 135.174 135.335 185.070 1.00 90.40  ? 42  G   C C8    1 
ATOM   9397  N  N7    . G   C 2 42  ? 134.975 135.376 183.774 1.00 90.36  ? 42  G   C N7    1 
ATOM   9398  C  C5    . G   C 2 42  ? 136.044 134.669 183.241 1.00 92.37  ? 42  G   C C5    1 
ATOM   9399  C  C6    . G   C 2 42  ? 136.369 134.375 181.896 1.00 90.76  ? 42  G   C C6    1 
ATOM   9400  O  O6    . G   C 2 42  ? 135.756 134.694 180.870 1.00 83.13  ? 42  G   C O6    1 
ATOM   9401  N  N1    . G   C 2 42  ? 137.546 133.630 181.810 1.00 87.56  ? 42  G   C N1    1 
ATOM   9402  C  C2    . G   C 2 42  ? 138.307 133.222 182.877 1.00 93.26  ? 42  G   C C2    1 
ATOM   9403  N  N2    . G   C 2 42  ? 139.408 132.513 182.605 1.00 93.38  ? 42  G   C N2    1 
ATOM   9404  N  N3    . G   C 2 42  ? 138.005 133.494 184.141 1.00 92.85  ? 42  G   C N3    1 
ATOM   9405  C  C4    . G   C 2 42  ? 136.861 134.207 184.245 1.00 90.24  ? 42  G   C C4    1 
ATOM   9406  P  P     . A   C 2 43  ? 138.944 138.491 187.766 1.00 47.94  ? 43  A   C P     1 
ATOM   9407  O  OP1   . A   C 2 43  ? 139.787 139.279 188.741 1.00 68.41  ? 43  A   C OP1   1 
ATOM   9408  O  OP2   . A   C 2 43  ? 138.005 139.343 186.942 1.00 84.10  ? 43  A   C OP2   1 
ATOM   9409  O  "O5'" . A   C 2 43  ? 139.956 137.789 186.728 1.00 92.33  ? 43  A   C "O5'" 1 
ATOM   9410  C  "C5'" . A   C 2 43  ? 141.059 137.008 187.247 1.00 92.69  ? 43  A   C "C5'" 1 
ATOM   9411  C  "C4'" . A   C 2 43  ? 141.922 136.548 186.100 1.00 85.32  ? 43  A   C "C4'" 1 
ATOM   9412  O  "O4'" . A   C 2 43  ? 141.135 135.742 185.190 1.00 75.11  ? 43  A   C "O4'" 1 
ATOM   9413  C  "C3'" . A   C 2 43  ? 142.491 137.650 185.204 1.00 88.07  ? 43  A   C "C3'" 1 
ATOM   9414  O  "O3'" . A   C 2 43  ? 143.643 138.245 185.786 1.00 80.18  ? 43  A   C "O3'" 1 
ATOM   9415  C  "C2'" . A   C 2 43  ? 142.805 136.858 183.934 1.00 87.94  ? 43  A   C "C2'" 1 
ATOM   9416  O  "O2'" . A   C 2 43  ? 144.035 136.174 184.009 1.00 91.64  ? 43  A   C "O2'" 1 
ATOM   9417  C  "C1'" . A   C 2 43  ? 141.653 135.859 183.883 1.00 79.76  ? 43  A   C "C1'" 1 
ATOM   9418  N  N9    . A   C 2 43  ? 140.577 136.253 182.983 1.00 85.84  ? 43  A   C N9    1 
ATOM   9419  C  C8    . A   C 2 43  ? 139.426 136.920 183.312 1.00 89.92  ? 43  A   C C8    1 
ATOM   9420  N  N7    . A   C 2 43  ? 138.637 137.126 182.290 1.00 85.00  ? 43  A   C N7    1 
ATOM   9421  C  C5    . A   C 2 43  ? 139.306 136.555 181.219 1.00 83.46  ? 43  A   C C5    1 
ATOM   9422  C  C6    . A   C 2 43  ? 138.985 136.442 179.856 1.00 84.12  ? 43  A   C C6    1 
ATOM   9423  N  N6    . A   C 2 43  ? 137.868 136.922 179.319 1.00 86.91  ? 43  A   C N6    1 
ATOM   9424  N  N1    . A   C 2 43  ? 139.873 135.810 179.055 1.00 85.65  ? 43  A   C N1    1 
ATOM   9425  C  C2    . A   C 2 43  ? 140.996 135.333 179.601 1.00 87.55  ? 43  A   C C2    1 
ATOM   9426  N  N3    . A   C 2 43  ? 141.402 135.380 180.865 1.00 87.39  ? 43  A   C N3    1 
ATOM   9427  C  C4    . A   C 2 43  ? 140.500 136.005 181.635 1.00 86.01  ? 43  A   C C4    1 
ATOM   9428  P  P     . G   C 2 44  ? 144.162 139.686 185.303 1.00 66.65  ? 44  G   C P     1 
ATOM   9429  O  OP1   . G   C 2 44  ? 145.185 140.279 186.245 1.00 80.01  ? 44  G   C OP1   1 
ATOM   9430  O  OP2   . G   C 2 44  ? 143.012 140.614 184.985 1.00 89.76  ? 44  G   C OP2   1 
ATOM   9431  O  "O5'" . G   C 2 44  ? 144.921 139.380 183.921 1.00 93.27  ? 44  G   C "O5'" 1 
ATOM   9432  C  "C5'" . G   C 2 44  ? 146.144 138.611 183.961 1.00 91.12  ? 44  G   C "C5'" 1 
ATOM   9433  C  "C4'" . G   C 2 44  ? 146.530 138.243 182.552 1.00 79.18  ? 44  G   C "C4'" 1 
ATOM   9434  O  "O4'" . G   C 2 44  ? 145.440 137.513 181.940 1.00 73.84  ? 44  G   C "O4'" 1 
ATOM   9435  C  "C3'" . G   C 2 44  ? 146.781 139.416 181.604 1.00 80.64  ? 44  G   C "C3'" 1 
ATOM   9436  O  "O3'" . G   C 2 44  ? 148.121 139.872 181.733 1.00 77.08  ? 44  G   C "O3'" 1 
ATOM   9437  C  "C2'" . G   C 2 44  ? 146.504 138.777 180.242 1.00 86.44  ? 44  G   C "C2'" 1 
ATOM   9438  O  "O2'" . G   C 2 44  ? 147.619 138.088 179.726 1.00 103.31 ? 44  G   C "O2'" 1 
ATOM   9439  C  "C1'" . G   C 2 44  ? 145.386 137.789 180.559 1.00 76.57  ? 44  G   C "C1'" 1 
ATOM   9440  N  N9    . G   C 2 44  ? 144.052 138.278 180.236 1.00 72.78  ? 44  G   C N9    1 
ATOM   9441  C  C8    . G   C 2 44  ? 143.177 138.909 181.081 1.00 85.76  ? 44  G   C C8    1 
ATOM   9442  N  N7    . G   C 2 44  ? 142.040 139.215 180.510 1.00 87.87  ? 44  G   C N7    1 
ATOM   9443  C  C5    . G   C 2 44  ? 142.176 138.753 179.209 1.00 72.06  ? 44  G   C C5    1 
ATOM   9444  C  C6    . G   C 2 44  ? 141.267 138.804 178.127 1.00 70.66  ? 44  G   C C6    1 
ATOM   9445  O  O6    . G   C 2 44  ? 140.129 139.289 178.107 1.00 70.41  ? 44  G   C O6    1 
ATOM   9446  N  N1    . G   C 2 44  ? 141.803 138.217 176.983 1.00 80.22  ? 44  G   C N1    1 
ATOM   9447  C  C2    . G   C 2 44  ? 143.052 137.657 176.892 1.00 88.57  ? 44  G   C C2    1 
ATOM   9448  N  N2    . G   C 2 44  ? 143.391 137.136 175.706 1.00 89.29  ? 44  G   C N2    1 
ATOM   9449  N  N3    . G   C 2 44  ? 143.911 137.607 177.906 1.00 93.01  ? 44  G   C N3    1 
ATOM   9450  C  C4    . G   C 2 44  ? 143.406 138.167 179.029 1.00 80.80  ? 44  G   C C4    1 
ATOM   9451  P  P     . G   C 2 45  ? 148.556 141.353 181.276 1.00 71.40  ? 45  G   C P     1 
ATOM   9452  O  OP1   . G   C 2 45  ? 150.029 141.600 181.535 1.00 87.82  ? 45  G   C OP1   1 
ATOM   9453  O  OP2   . G   C 2 45  ? 147.653 142.432 181.847 1.00 95.93  ? 45  G   C OP2   1 
ATOM   9454  O  "O5'" . G   C 2 45  ? 148.366 141.387 179.671 1.00 90.41  ? 45  G   C "O5'" 1 
ATOM   9455  C  "C5'" . G   C 2 45  ? 149.270 140.607 178.849 1.00 94.18  ? 45  G   C "C5'" 1 
ATOM   9456  C  "C4'" . G   C 2 45  ? 148.732 140.523 177.441 1.00 94.79  ? 45  G   C "C4'" 1 
ATOM   9457  O  "O4'" . G   C 2 45  ? 147.304 140.278 177.484 1.00 93.45  ? 45  G   C "O4'" 1 
ATOM   9458  C  "C3'" . G   C 2 45  ? 148.921 141.775 176.569 1.00 95.40  ? 45  G   C "C3'" 1 
ATOM   9459  O  "O3'" . G   C 2 45  ? 149.706 141.443 175.430 1.00 90.22  ? 45  G   C "O3'" 1 
ATOM   9460  C  "C2'" . G   C 2 45  ? 147.498 142.210 176.195 1.00 98.19  ? 45  G   C "C2'" 1 
ATOM   9461  O  "O2'" . G   C 2 45  ? 147.396 142.683 174.869 1.00 99.38  ? 45  G   C "O2'" 1 
ATOM   9462  C  "C1'" . G   C 2 45  ? 146.704 140.923 176.389 1.00 99.84  ? 45  G   C "C1'" 1 
ATOM   9463  N  N9    . G   C 2 45  ? 145.293 141.136 176.683 1.00 92.26  ? 45  G   C N9    1 
ATOM   9464  C  C8    . G   C 2 45  ? 144.728 141.345 177.915 1.00 94.61  ? 45  G   C C8    1 
ATOM   9465  N  N7    . G   C 2 45  ? 143.428 141.509 177.866 1.00 89.76  ? 45  G   C N7    1 
ATOM   9466  C  C5    . G   C 2 45  ? 143.119 141.401 176.516 1.00 87.67  ? 45  G   C C5    1 
ATOM   9467  C  C6    . G   C 2 45  ? 141.868 141.492 175.857 1.00 96.92  ? 45  G   C C6    1 
ATOM   9468  O  O6    . G   C 2 45  ? 140.752 141.691 176.355 1.00 105.69 ? 45  G   C O6    1 
ATOM   9469  N  N1    . G   C 2 45  ? 142.005 141.323 174.479 1.00 92.73  ? 45  G   C N1    1 
ATOM   9470  C  C2    . G   C 2 45  ? 143.190 141.097 173.822 1.00 89.64  ? 45  G   C C2    1 
ATOM   9471  N  N2    . G   C 2 45  ? 143.121 140.960 172.491 1.00 86.43  ? 45  G   C N2    1 
ATOM   9472  N  N3    . G   C 2 45  ? 144.369 141.011 174.436 1.00 90.69  ? 45  G   C N3    1 
ATOM   9473  C  C4    . G   C 2 45  ? 144.258 141.171 175.777 1.00 87.43  ? 45  G   C C4    1 
HETATM 9474  P  P     . 7MG C 2 46  ? 150.928 142.378 174.968 1.00 90.17  ? 46  7MG C P     1 
HETATM 9475  O  OP1   . 7MG C 2 46  ? 152.019 141.593 174.265 1.00 97.40  ? 46  7MG C OP1   1 
HETATM 9476  O  OP2   . 7MG C 2 46  ? 151.434 143.252 176.100 1.00 91.76  ? 46  7MG C OP2   1 
HETATM 9477  O  "O5'" . 7MG C 2 46  ? 150.276 143.362 173.871 1.00 97.86  ? 46  7MG C "O5'" 1 
HETATM 9478  C  "C5'" . 7MG C 2 46  ? 149.952 142.827 172.564 1.00 97.46  ? 46  7MG C "C5'" 1 
HETATM 9479  C  "C4'" . 7MG C 2 46  ? 149.581 143.957 171.635 1.00 95.26  ? 46  7MG C "C4'" 1 
HETATM 9480  O  "O4'" . 7MG C 2 46  ? 148.409 144.635 172.158 1.00 86.95  ? 46  7MG C "O4'" 1 
HETATM 9481  C  "C3'" . 7MG C 2 46  ? 150.644 145.051 171.443 1.00 93.58  ? 46  7MG C "C3'" 1 
HETATM 9482  O  "O3'" . 7MG C 2 46  ? 150.680 145.484 170.090 1.00 97.69  ? 46  7MG C "O3'" 1 
HETATM 9483  C  "C2'" . 7MG C 2 46  ? 150.211 146.143 172.397 1.00 91.74  ? 46  7MG C "C2'" 1 
HETATM 9484  O  "O2'" . 7MG C 2 46  ? 150.542 147.436 171.933 1.00 98.80  ? 46  7MG C "O2'" 1 
HETATM 9485  C  "C1'" . 7MG C 2 46  ? 148.691 146.009 172.333 1.00 87.98  ? 46  7MG C "C1'" 1 
HETATM 9486  N  N9    . 7MG C 2 46  ? 148.031 146.494 173.541 1.00 91.01  ? 46  7MG C N9    1 
HETATM 9487  C  C8    . 7MG C 2 46  ? 148.633 146.447 174.872 1.00 88.86  ? 46  7MG C C8    1 
HETATM 9488  N  N7    . 7MG C 2 46  ? 147.597 147.054 175.697 1.00 91.53  ? 46  7MG C N7    1 
HETATM 9489  C  C5    . 7MG C 2 46  ? 146.499 147.409 174.908 1.00 99.39  ? 46  7MG C C5    1 
HETATM 9490  C  C6    . 7MG C 2 46  ? 145.289 148.010 175.257 1.00 94.00  ? 46  7MG C C6    1 
HETATM 9491  O  O6    . 7MG C 2 46  ? 144.908 148.372 176.366 1.00 87.16  ? 46  7MG C O6    1 
HETATM 9492  N  N1    . 7MG C 2 46  ? 144.482 148.177 174.132 1.00 92.13  ? 46  7MG C N1    1 
HETATM 9493  C  C2    . 7MG C 2 46  ? 144.808 147.811 172.854 1.00 90.77  ? 46  7MG C C2    1 
HETATM 9494  N  N2    . 7MG C 2 46  ? 143.899 148.055 171.905 1.00 94.04  ? 46  7MG C N2    1 
HETATM 9495  N  N3    . 7MG C 2 46  ? 145.957 147.245 172.538 1.00 97.95  ? 46  7MG C N3    1 
HETATM 9496  C  C4    . 7MG C 2 46  ? 146.773 147.054 173.590 1.00 99.31  ? 46  7MG C C4    1 
HETATM 9497  C  CM7   . 7MG C 2 46  ? 147.729 147.239 177.132 1.00 92.76  ? 46  7MG C CM7   1 
HETATM 9498  P  P     . H2U C 2 47  ? 151.773 144.934 169.046 1.00 127.79 ? 47  H2U C P     1 
HETATM 9499  O  OP1   . H2U C 2 47  ? 151.376 145.350 167.647 1.00 125.36 ? 47  H2U C OP1   1 
HETATM 9500  O  OP2   . H2U C 2 47  ? 152.060 143.456 169.188 1.00 125.02 ? 47  H2U C OP2   1 
HETATM 9501  O  "O5'" . H2U C 2 47  ? 153.135 145.711 169.399 1.00 132.81 ? 47  H2U C "O5'" 1 
HETATM 9502  C  "C5'" . H2U C 2 47  ? 153.158 147.155 169.295 1.00 129.27 ? 47  H2U C "C5'" 1 
HETATM 9503  C  "C4'" . H2U C 2 47  ? 154.206 147.693 170.235 1.00 127.35 ? 47  H2U C "C4'" 1 
HETATM 9504  O  "O4'" . H2U C 2 47  ? 155.491 147.133 169.880 1.00 128.35 ? 47  H2U C "O4'" 1 
HETATM 9505  C  "C3'" . H2U C 2 47  ? 154.417 149.212 170.223 1.00 125.45 ? 47  H2U C "C3'" 1 
HETATM 9506  O  "O3'" . H2U C 2 47  ? 153.592 149.833 171.200 1.00 118.54 ? 47  H2U C "O3'" 1 
HETATM 9507  C  "C1'" . H2U C 2 47  ? 156.507 147.942 170.419 1.00 126.98 ? 47  H2U C "C1'" 1 
HETATM 9508  C  "C2'" . H2U C 2 47  ? 155.915 149.346 170.526 1.00 129.10 ? 47  H2U C "C2'" 1 
HETATM 9509  O  "O2'" . H2U C 2 47  ? 156.159 149.876 171.819 1.00 134.83 ? 47  H2U C "O2'" 1 
HETATM 9510  N  N1    . H2U C 2 47  ? 157.686 147.894 169.516 1.00 125.20 ? 47  H2U C N1    1 
HETATM 9511  C  C2    . H2U C 2 47  ? 158.573 146.900 169.723 1.00 130.79 ? 47  H2U C C2    1 
HETATM 9512  O  O2    . H2U C 2 47  ? 158.689 146.379 170.826 1.00 130.71 ? 47  H2U C O2    1 
HETATM 9513  N  N3    . H2U C 2 47  ? 159.300 146.498 168.669 1.00 132.67 ? 47  H2U C N3    1 
HETATM 9514  C  C4    . H2U C 2 47  ? 159.402 147.272 167.538 1.00 132.06 ? 47  H2U C C4    1 
HETATM 9515  O  O4    . H2U C 2 47  ? 159.660 146.773 166.457 1.00 125.96 ? 47  H2U C O4    1 
HETATM 9516  C  C5    . H2U C 2 47  ? 159.129 148.730 167.718 1.00 132.99 ? 47  H2U C C5    1 
HETATM 9517  C  C6    . H2U C 2 47  ? 157.816 148.913 168.467 1.00 126.17 ? 47  H2U C C6    1 
HETATM 9518  P  P     . 5MC C 2 48  ? 153.259 151.407 171.159 1.00 42.92  ? 48  5MC C P     1 
HETATM 9519  O  OP1   . 5MC C 2 48  ? 154.050 152.204 170.135 1.00 81.85  ? 48  5MC C OP1   1 
HETATM 9520  O  OP2   . 5MC C 2 48  ? 153.292 152.010 172.551 1.00 95.13  ? 48  5MC C OP2   1 
HETATM 9521  O  "O5'" . 5MC C 2 48  ? 151.719 151.450 170.682 1.00 73.08  ? 48  5MC C "O5'" 1 
HETATM 9522  C  "C5'" . 5MC C 2 48  ? 151.320 150.692 169.513 1.00 91.74  ? 48  5MC C "C5'" 1 
HETATM 9523  C  "C4'" . 5MC C 2 48  ? 149.976 151.188 169.042 1.00 90.11  ? 48  5MC C "C4'" 1 
HETATM 9524  O  "O4'" . 5MC C 2 48  ? 149.102 151.348 170.189 1.00 86.34  ? 48  5MC C "O4'" 1 
HETATM 9525  C  "C3'" . 5MC C 2 48  ? 149.994 152.537 168.303 1.00 90.96  ? 48  5MC C "C3'" 1 
HETATM 9526  O  "O3'" . 5MC C 2 48  ? 149.368 152.408 167.031 1.00 83.00  ? 48  5MC C "O3'" 1 
HETATM 9527  C  "C2'" . 5MC C 2 48  ? 149.275 153.519 169.243 1.00 90.58  ? 48  5MC C "C2'" 1 
HETATM 9528  O  "O2'" . 5MC C 2 48  ? 148.372 154.373 168.571 1.00 97.50  ? 48  5MC C "O2'" 1 
HETATM 9529  C  "C1'" . 5MC C 2 48  ? 148.468 152.606 170.170 1.00 78.01  ? 48  5MC C "C1'" 1 
HETATM 9530  N  N1    . 5MC C 2 48  ? 148.427 153.120 171.562 1.00 76.93  ? 48  5MC C N1    1 
HETATM 9531  C  C2    . 5MC C 2 48  ? 147.334 153.889 171.960 1.00 85.91  ? 48  5MC C C2    1 
HETATM 9532  O  O2    . 5MC C 2 48  ? 146.423 154.100 171.144 1.00 95.88  ? 48  5MC C O2    1 
HETATM 9533  N  N3    . 5MC C 2 48  ? 147.298 154.362 173.229 1.00 85.46  ? 48  5MC C N3    1 
HETATM 9534  C  C4    . 5MC C 2 48  ? 148.303 154.108 174.079 1.00 83.46  ? 48  5MC C C4    1 
HETATM 9535  N  N4    . 5MC C 2 48  ? 148.199 154.612 175.319 1.00 87.27  ? 48  5MC C N4    1 
HETATM 9536  C  C5    . 5MC C 2 48  ? 149.424 153.340 173.688 1.00 84.49  ? 48  5MC C C5    1 
HETATM 9537  C  C6    . 5MC C 2 48  ? 149.447 152.874 172.432 1.00 87.18  ? 48  5MC C C6    1 
HETATM 9538  C  CM5   . 5MC C 2 48  ? 150.537 153.066 174.657 1.00 89.62  ? 48  5MC C CM5   1 
HETATM 9539  P  P     . 5MC C 2 49  ? 149.724 153.416 165.832 1.00 49.90  ? 49  5MC C P     1 
HETATM 9540  O  OP1   . 5MC C 2 49  ? 151.172 153.866 165.858 1.00 84.32  ? 49  5MC C OP1   1 
HETATM 9541  O  OP2   . 5MC C 2 49  ? 148.730 154.557 165.728 1.00 89.74  ? 49  5MC C OP2   1 
HETATM 9542  O  "O5'" . 5MC C 2 49  ? 149.519 152.499 164.520 1.00 83.29  ? 49  5MC C "O5'" 1 
HETATM 9543  C  "C5'" . 5MC C 2 49  ? 150.005 151.132 164.532 1.00 97.47  ? 49  5MC C "C5'" 1 
HETATM 9544  C  "C4'" . 5MC C 2 49  ? 151.207 151.005 163.627 1.00 96.17  ? 49  5MC C "C4'" 1 
HETATM 9545  O  "O4'" . 5MC C 2 49  ? 151.006 151.795 162.426 1.00 95.94  ? 49  5MC C "O4'" 1 
HETATM 9546  C  "C3'" . 5MC C 2 49  ? 152.537 151.521 164.190 1.00 91.67  ? 49  5MC C "C3'" 1 
HETATM 9547  O  "O3'" . 5MC C 2 49  ? 153.144 150.559 165.045 1.00 86.19  ? 49  5MC C "O3'" 1 
HETATM 9548  C  "C2'" . 5MC C 2 49  ? 153.339 151.759 162.906 1.00 90.80  ? 49  5MC C "C2'" 1 
HETATM 9549  O  "O2'" . 5MC C 2 49  ? 153.924 150.580 162.396 1.00 87.96  ? 49  5MC C "O2'" 1 
HETATM 9550  C  "C1'" . 5MC C 2 49  ? 152.254 152.234 161.932 1.00 94.15  ? 49  5MC C "C1'" 1 
HETATM 9551  N  N1    . 5MC C 2 49  ? 152.220 153.712 161.782 1.00 84.64  ? 49  5MC C N1    1 
HETATM 9552  C  C2    . 5MC C 2 49  ? 153.079 154.309 160.858 1.00 93.65  ? 49  5MC C C2    1 
HETATM 9553  O  O2    . 5MC C 2 49  ? 153.855 153.590 160.210 1.00 96.33  ? 49  5MC C O2    1 
HETATM 9554  N  N3    . 5MC C 2 49  ? 153.051 155.655 160.715 1.00 96.27  ? 49  5MC C N3    1 
HETATM 9555  C  C4    . 5MC C 2 49  ? 152.200 156.397 161.440 1.00 90.40  ? 49  5MC C C4    1 
HETATM 9556  N  N4    . 5MC C 2 49  ? 152.226 157.724 161.239 1.00 90.46  ? 49  5MC C N4    1 
HETATM 9557  C  C5    . 5MC C 2 49  ? 151.314 155.808 162.371 1.00 90.25  ? 49  5MC C C5    1 
HETATM 9558  C  C6    . 5MC C 2 49  ? 151.354 154.476 162.507 1.00 88.81  ? 49  5MC C C6    1 
HETATM 9559  C  CM5   . 5MC C 2 49  ? 150.370 156.658 163.171 1.00 99.88  ? 49  5MC C CM5   1 
ATOM   9560  P  P     . A   C 2 50  ? 154.346 150.946 166.043 1.00 73.66  ? 50  A   C P     1 
ATOM   9561  O  OP1   . A   C 2 50  ? 154.728 149.756 166.891 1.00 113.12 ? 50  A   C OP1   1 
ATOM   9562  O  OP2   . A   C 2 50  ? 154.068 152.196 166.846 1.00 95.80  ? 50  A   C OP2   1 
ATOM   9563  O  "O5'" . A   C 2 50  ? 155.614 151.278 165.114 1.00 112.89 ? 50  A   C "O5'" 1 
ATOM   9564  C  "C5'" . A   C 2 50  ? 156.377 150.184 164.554 1.00 120.08 ? 50  A   C "C5'" 1 
ATOM   9565  C  "C4'" . A   C 2 50  ? 157.535 150.744 163.769 1.00 119.23 ? 50  A   C "C4'" 1 
ATOM   9566  O  "O4'" . A   C 2 50  ? 157.025 151.487 162.632 1.00 113.92 ? 50  A   C "O4'" 1 
ATOM   9567  C  "C3'" . A   C 2 50  ? 158.429 151.746 164.507 1.00 115.73 ? 50  A   C "C3'" 1 
ATOM   9568  O  "O3'" . A   C 2 50  ? 159.456 151.130 165.271 1.00 105.90 ? 50  A   C "O3'" 1 
ATOM   9569  C  "C2'" . A   C 2 50  ? 159.022 152.525 163.335 1.00 115.90 ? 50  A   C "C2'" 1 
ATOM   9570  O  "O2'" . A   C 2 50  ? 160.064 151.826 162.693 1.00 121.72 ? 50  A   C "O2'" 1 
ATOM   9571  C  "C1'" . A   C 2 50  ? 157.807 152.642 162.425 1.00 109.04 ? 50  A   C "C1'" 1 
ATOM   9572  N  N9    . A   C 2 50  ? 156.999 153.820 162.701 1.00 104.03 ? 50  A   C N9    1 
ATOM   9573  C  C8    . A   C 2 50  ? 155.835 153.887 163.423 1.00 114.11 ? 50  A   C C8    1 
ATOM   9574  N  N7    . A   C 2 50  ? 155.332 155.093 163.483 1.00 111.89 ? 50  A   C N7    1 
ATOM   9575  C  C5    . A   C 2 50  ? 156.214 155.868 162.747 1.00 104.83 ? 50  A   C C5    1 
ATOM   9576  C  C6    . A   C 2 50  ? 156.237 157.238 162.434 1.00 111.22 ? 50  A   C C6    1 
ATOM   9577  N  N6    . A   C 2 50  ? 155.315 158.106 162.836 1.00 114.49 ? 50  A   C N6    1 
ATOM   9578  N  N1    . A   C 2 50  ? 157.264 157.684 161.677 1.00 117.87 ? 50  A   C N1    1 
ATOM   9579  C  C2    . A   C 2 50  ? 158.194 156.812 161.275 1.00 118.70 ? 50  A   C C2    1 
ATOM   9580  N  N3    . A   C 2 50  ? 158.274 155.507 161.507 1.00 112.21 ? 50  A   C N3    1 
ATOM   9581  C  C4    . A   C 2 50  ? 157.240 155.091 162.251 1.00 102.85 ? 50  A   C C4    1 
ATOM   9582  P  P     . G   C 2 51  ? 160.231 151.952 166.412 1.00 105.01 ? 51  G   C P     1 
ATOM   9583  O  OP1   . G   C 2 51  ? 161.287 151.110 167.090 1.00 125.46 ? 51  G   C OP1   1 
ATOM   9584  O  OP2   . G   C 2 51  ? 159.272 152.620 167.373 1.00 115.53 ? 51  G   C OP2   1 
ATOM   9585  O  "O5'" . G   C 2 51  ? 161.009 153.139 165.653 1.00 119.71 ? 51  G   C "O5'" 1 
ATOM   9586  C  "C5'" . G   C 2 51  ? 162.194 152.817 164.892 1.00 123.03 ? 51  G   C "C5'" 1 
ATOM   9587  C  "C4'" . G   C 2 51  ? 162.797 154.089 164.355 1.00 119.06 ? 51  G   C "C4'" 1 
ATOM   9588  O  "O4'" . G   C 2 51  ? 161.876 154.726 163.434 1.00 115.98 ? 51  G   C "O4'" 1 
ATOM   9589  C  "C3'" . G   C 2 51  ? 163.073 155.195 165.375 1.00 117.50 ? 51  G   C "C3'" 1 
ATOM   9590  O  "O3'" . G   C 2 51  ? 164.241 154.998 166.157 1.00 121.86 ? 51  G   C "O3'" 1 
ATOM   9591  C  "C2'" . G   C 2 51  ? 163.242 156.383 164.430 1.00 121.10 ? 51  G   C "C2'" 1 
ATOM   9592  O  "O2'" . G   C 2 51  ? 164.500 156.399 163.795 1.00 123.83 ? 51  G   C "O2'" 1 
ATOM   9593  C  "C1'" . G   C 2 51  ? 162.114 156.118 163.439 1.00 119.26 ? 51  G   C "C1'" 1 
ATOM   9594  N  N9    . G   C 2 51  ? 160.892 156.822 163.798 1.00 119.10 ? 51  G   C N9    1 
ATOM   9595  C  C8    . G   C 2 51  ? 159.786 156.318 164.430 1.00 124.48 ? 51  G   C C8    1 
ATOM   9596  N  N7    . G   C 2 51  ? 158.849 157.215 164.618 1.00 122.65 ? 51  G   C N7    1 
ATOM   9597  C  C5    . G   C 2 51  ? 159.373 158.378 164.071 1.00 119.79 ? 51  G   C C5    1 
ATOM   9598  C  C6    . G   C 2 51  ? 158.815 159.674 163.975 1.00 123.46 ? 51  G   C C6    1 
ATOM   9599  O  O6    . G   C 2 51  ? 157.708 160.060 164.374 1.00 125.40 ? 51  G   C O6    1 
ATOM   9600  N  N1    . G   C 2 51  ? 159.689 160.561 163.347 1.00 126.48 ? 51  G   C N1    1 
ATOM   9601  C  C2    . G   C 2 51  ? 160.935 160.240 162.869 1.00 126.03 ? 51  G   C C2    1 
ATOM   9602  N  N2    . G   C 2 51  ? 161.633 161.225 162.291 1.00 120.41 ? 51  G   C N2    1 
ATOM   9603  N  N3    . G   C 2 51  ? 161.462 159.023 162.954 1.00 126.02 ? 51  G   C N3    1 
ATOM   9604  C  C4    . G   C 2 51  ? 160.626 158.146 163.554 1.00 120.20 ? 51  G   C C4    1 
ATOM   9605  P  P     . G   C 2 52  ? 164.419 155.798 167.538 1.00 132.70 ? 52  G   C P     1 
ATOM   9606  O  OP1   . G   C 2 52  ? 165.743 155.508 168.205 1.00 137.14 ? 52  G   C OP1   1 
ATOM   9607  O  OP2   . G   C 2 52  ? 163.212 155.616 168.427 1.00 138.19 ? 52  G   C OP2   1 
ATOM   9608  O  "O5'" . G   C 2 52  ? 164.452 157.352 167.139 1.00 141.14 ? 52  G   C "O5'" 1 
ATOM   9609  C  "C5'" . G   C 2 52  ? 165.659 157.884 166.554 1.00 137.26 ? 52  G   C "C5'" 1 
ATOM   9610  C  "C4'" . G   C 2 52  ? 165.473 159.358 166.307 1.00 133.92 ? 52  G   C "C4'" 1 
ATOM   9611  O  "O4'" . G   C 2 52  ? 164.357 159.566 165.405 1.00 131.14 ? 52  G   C "O4'" 1 
ATOM   9612  C  "C3'" . G   C 2 52  ? 165.108 160.210 167.526 1.00 133.98 ? 52  G   C "C3'" 1 
ATOM   9613  O  "O3'" . G   C 2 52  ? 166.223 160.503 168.357 1.00 132.59 ? 52  G   C "O3'" 1 
ATOM   9614  C  "C2'" . G   C 2 52  ? 164.567 161.448 166.814 1.00 131.32 ? 52  G   C "C2'" 1 
ATOM   9615  O  "O2'" . G   C 2 52  ? 165.586 162.265 166.282 1.00 132.71 ? 52  G   C "O2'" 1 
ATOM   9616  C  "C1'" . G   C 2 52  ? 163.744 160.800 165.707 1.00 129.39 ? 52  G   C "C1'" 1 
ATOM   9617  N  N9    . G   C 2 52  ? 162.368 160.571 166.118 1.00 131.17 ? 52  G   C N9    1 
ATOM   9618  C  C8    . G   C 2 52  ? 161.799 159.401 166.549 1.00 134.54 ? 52  G   C C8    1 
ATOM   9619  N  N7    . G   C 2 52  ? 160.535 159.533 166.869 1.00 135.46 ? 52  G   C N7    1 
ATOM   9620  C  C5    . G   C 2 52  ? 160.261 160.874 166.634 1.00 133.34 ? 52  G   C C5    1 
ATOM   9621  C  C6    . G   C 2 52  ? 159.058 161.601 166.795 1.00 133.35 ? 52  G   C C6    1 
ATOM   9622  O  O6    . G   C 2 52  ? 157.960 161.188 167.188 1.00 134.66 ? 52  G   C O6    1 
ATOM   9623  N  N1    . G   C 2 52  ? 159.219 162.939 166.437 1.00 131.79 ? 52  G   C N1    1 
ATOM   9624  C  C2    . G   C 2 52  ? 160.385 163.501 165.984 1.00 132.22 ? 52  G   C C2    1 
ATOM   9625  N  N2    . G   C 2 52  ? 160.349 164.805 165.687 1.00 134.74 ? 52  G   C N2    1 
ATOM   9626  N  N3    . G   C 2 52  ? 161.518 162.823 165.828 1.00 132.41 ? 52  G   C N3    1 
ATOM   9627  C  C4    . G   C 2 52  ? 161.378 161.519 166.159 1.00 131.06 ? 52  G   C C4    1 
ATOM   9628  P  P     . G   C 2 53  ? 166.025 160.965 169.884 1.00 130.75 ? 53  G   C P     1 
ATOM   9629  O  OP1   . G   C 2 53  ? 167.347 161.292 170.540 1.00 134.85 ? 53  G   C OP1   1 
ATOM   9630  O  OP2   . G   C 2 53  ? 165.179 160.007 170.689 1.00 140.08 ? 53  G   C OP2   1 
ATOM   9631  O  "O5'" . G   C 2 53  ? 165.205 162.347 169.798 1.00 135.80 ? 53  G   C "O5'" 1 
ATOM   9632  C  "C5'" . G   C 2 53  ? 165.898 163.524 169.325 1.00 134.21 ? 53  G   C "C5'" 1 
ATOM   9633  C  "C4'" . G   C 2 53  ? 164.903 164.632 169.090 1.00 135.30 ? 53  G   C "C4'" 1 
ATOM   9634  O  "O4'" . G   C 2 53  ? 163.744 164.105 168.401 1.00 134.77 ? 53  G   C "O4'" 1 
ATOM   9635  C  "C3'" . G   C 2 53  ? 164.310 165.290 170.337 1.00 134.60 ? 53  G   C "C3'" 1 
ATOM   9636  O  "O3'" . G   C 2 53  ? 165.177 166.285 170.860 1.00 137.41 ? 53  G   C "O3'" 1 
ATOM   9637  C  "C2'" . G   C 2 53  ? 163.040 165.916 169.762 1.00 132.35 ? 53  G   C "C2'" 1 
ATOM   9638  O  "O2'" . G   C 2 53  ? 163.286 167.174 169.176 1.00 133.13 ? 53  G   C "O2'" 1 
ATOM   9639  C  "C1'" . G   C 2 53  ? 162.621 164.903 168.700 1.00 133.01 ? 53  G   C "C1'" 1 
ATOM   9640  N  N9    . G   C 2 53  ? 161.528 164.041 169.126 1.00 131.28 ? 53  G   C N9    1 
ATOM   9641  C  C8    . G   C 2 53  ? 161.560 162.684 169.322 1.00 134.30 ? 53  G   C C8    1 
ATOM   9642  N  N7    . G   C 2 53  ? 160.405 162.194 169.700 1.00 134.42 ? 53  G   C N7    1 
ATOM   9643  C  C5    . G   C 2 53  ? 159.562 163.296 169.748 1.00 131.79 ? 53  G   C C5    1 
ATOM   9644  C  C6    . G   C 2 53  ? 158.191 163.384 170.092 1.00 134.20 ? 53  G   C C6    1 
ATOM   9645  O  O6    . G   C 2 53  ? 157.428 162.471 170.432 1.00 132.37 ? 53  G   C O6    1 
ATOM   9646  N  N1    . G   C 2 53  ? 157.729 164.698 170.010 1.00 135.38 ? 53  G   C N1    1 
ATOM   9647  C  C2    . G   C 2 53  ? 158.487 165.782 169.646 1.00 135.93 ? 53  G   C C2    1 
ATOM   9648  N  N2    . G   C 2 53  ? 157.871 166.970 169.623 1.00 136.46 ? 53  G   C N2    1 
ATOM   9649  N  N3    . G   C 2 53  ? 159.773 165.704 169.317 1.00 134.52 ? 53  G   C N3    1 
ATOM   9650  C  C4    . G   C 2 53  ? 160.240 164.436 169.386 1.00 130.59 ? 53  G   C C4    1 
HETATM 9651  N  N1    . 2MU C 2 54  ? 159.610 166.958 172.832 1.00 136.21 ? 54  2MU C N1    1 
HETATM 9652  C  C2    . 2MU C 2 54  ? 158.323 166.615 173.173 1.00 135.30 ? 54  2MU C C2    1 
HETATM 9653  N  N3    . 2MU C 2 54  ? 158.118 165.275 173.375 1.00 136.32 ? 54  2MU C N3    1 
HETATM 9654  C  C4    . 2MU C 2 54  ? 159.051 164.263 173.260 1.00 137.42 ? 54  2MU C C4    1 
HETATM 9655  C  C5    . 2MU C 2 54  ? 160.381 164.688 172.888 1.00 138.39 ? 54  2MU C C5    1 
HETATM 9656  C  C5M   . 2MU C 2 54  ? 161.456 163.654 172.748 1.00 138.85 ? 54  2MU C C5M   1 
HETATM 9657  C  C6    . 2MU C 2 54  ? 160.597 165.997 172.692 1.00 139.70 ? 54  2MU C C6    1 
HETATM 9658  O  O2    . 2MU C 2 54  ? 157.426 167.436 173.298 1.00 136.14 ? 54  2MU C O2    1 
HETATM 9659  O  O4    . 2MU C 2 54  ? 158.715 163.098 173.471 1.00 140.32 ? 54  2MU C O4    1 
HETATM 9660  C  "C1'" . 2MU C 2 54  ? 159.894 168.387 172.595 1.00 135.54 ? 54  2MU C "C1'" 1 
HETATM 9661  C  "C2'" . 2MU C 2 54  ? 160.235 169.163 173.870 1.00 135.25 ? 54  2MU C "C2'" 1 
HETATM 9662  O  "O2'" . 2MU C 2 54  ? 159.801 170.512 173.761 1.00 136.63 ? 54  2MU C "O2'" 1 
HETATM 9663  C  "C3'" . 2MU C 2 54  ? 161.756 169.075 173.881 1.00 134.74 ? 54  2MU C "C3'" 1 
HETATM 9664  C  "C4'" . 2MU C 2 54  ? 162.068 169.235 172.391 1.00 135.89 ? 54  2MU C "C4'" 1 
HETATM 9665  O  "O3'" . 2MU C 2 54  ? 162.366 170.108 174.643 1.00 135.25 ? 54  2MU C "O3'" 1 
HETATM 9666  O  "O4'" . 2MU C 2 54  ? 161.010 168.493 171.734 1.00 138.38 ? 54  2MU C "O4'" 1 
HETATM 9667  C  "C5'" . 2MU C 2 54  ? 163.415 168.721 171.954 1.00 135.80 ? 54  2MU C "C5'" 1 
HETATM 9668  O  "O5'" . 2MU C 2 54  ? 163.634 167.421 172.546 1.00 130.87 ? 54  2MU C "O5'" 1 
HETATM 9669  C  "C6'" . 2MU C 2 54  ? 158.412 170.629 173.482 1.00 139.74 ? 54  2MU C "C6'" 1 
HETATM 9670  P  P     . 2MU C 2 54  ? 165.083 166.743 172.396 1.00 128.01 ? 54  2MU C P     1 
HETATM 9671  O  OP1   . 2MU C 2 54  ? 166.096 167.817 172.729 1.00 135.27 ? 54  2MU C OP1   1 
HETATM 9672  O  OP2   . 2MU C 2 54  ? 165.117 165.560 173.340 1.00 137.87 ? 54  2MU C OP2   1 
HETATM 9673  N  N1    . PSU C 2 55  ? 161.338 165.564 176.313 1.00 145.35 ? 55  PSU C N1    1 
HETATM 9674  C  C2    . PSU C 2 55  ? 160.930 164.263 176.359 1.00 142.10 ? 55  PSU C C2    1 
HETATM 9675  N  N3    . PSU C 2 55  ? 159.653 164.054 176.805 1.00 144.13 ? 55  PSU C N3    1 
HETATM 9676  C  C4    . PSU C 2 55  ? 158.788 165.048 177.195 1.00 144.34 ? 55  PSU C C4    1 
HETATM 9677  C  C5    . PSU C 2 55  ? 159.253 166.370 177.125 1.00 143.38 ? 55  PSU C C5    1 
HETATM 9678  C  C6    . PSU C 2 55  ? 160.546 166.597 176.677 1.00 146.54 ? 55  PSU C C6    1 
HETATM 9679  O  O2    . PSU C 2 55  ? 161.657 163.341 176.016 1.00 141.89 ? 55  PSU C O2    1 
HETATM 9680  O  O4    . PSU C 2 55  ? 157.656 164.736 177.587 1.00 145.62 ? 55  PSU C O4    1 
HETATM 9681  C  "C1'" . PSU C 2 55  ? 158.373 167.508 177.563 1.00 142.91 ? 55  PSU C "C1'" 1 
HETATM 9682  C  "C2'" . PSU C 2 55  ? 158.500 167.847 179.051 1.00 141.90 ? 55  PSU C "C2'" 1 
HETATM 9683  O  "O2'" . PSU C 2 55  ? 157.327 168.460 179.545 1.00 142.97 ? 55  PSU C "O2'" 1 
HETATM 9684  C  "C3'" . PSU C 2 55  ? 159.717 168.774 179.034 1.00 143.57 ? 55  PSU C "C3'" 1 
HETATM 9685  C  "C4'" . PSU C 2 55  ? 159.373 169.630 177.812 1.00 147.62 ? 55  PSU C "C4'" 1 
HETATM 9686  O  "O3'" . PSU C 2 55  ? 159.785 169.558 180.218 1.00 142.45 ? 55  PSU C "O3'" 1 
HETATM 9687  O  "O4'" . PSU C 2 55  ? 158.737 168.719 176.883 1.00 147.25 ? 55  PSU C "O4'" 1 
HETATM 9688  C  "C5'" . PSU C 2 55  ? 160.532 170.323 177.139 1.00 146.96 ? 55  PSU C "C5'" 1 
HETATM 9689  O  "O5'" . PSU C 2 55  ? 161.603 169.369 176.945 1.00 144.75 ? 55  PSU C "O5'" 1 
HETATM 9690  P  P     . PSU C 2 55  ? 162.910 169.824 176.127 1.00 139.59 ? 55  PSU C P     1 
HETATM 9691  O  OP1   . PSU C 2 55  ? 163.433 171.076 176.798 1.00 143.75 ? 55  PSU C OP1   1 
HETATM 9692  O  OP2   . PSU C 2 55  ? 163.875 168.656 176.161 1.00 144.34 ? 55  PSU C OP2   1 
ATOM   9693  P  P     . C   C 2 56  ? 161.107 169.543 181.129 1.00 143.50 ? 56  C   C P     1 
ATOM   9694  O  OP1   . C   C 2 56  ? 161.121 170.633 182.178 1.00 144.85 ? 56  C   C OP1   1 
ATOM   9695  O  OP2   . C   C 2 56  ? 162.376 169.458 180.304 1.00 144.77 ? 56  C   C OP2   1 
ATOM   9696  O  "O5'" . C   C 2 56  ? 160.973 168.145 181.905 1.00 150.13 ? 56  C   C "O5'" 1 
ATOM   9697  C  "C5'" . C   C 2 56  ? 161.918 167.830 182.955 1.00 147.64 ? 56  C   C "C5'" 1 
ATOM   9698  C  "C4'" . C   C 2 56  ? 161.474 166.540 183.594 1.00 146.20 ? 56  C   C "C4'" 1 
ATOM   9699  O  "O4'" . C   C 2 56  ? 160.507 166.826 184.637 1.00 142.34 ? 56  C   C "O4'" 1 
ATOM   9700  C  "C3'" . C   C 2 56  ? 160.781 165.571 182.628 1.00 146.07 ? 56  C   C "C3'" 1 
ATOM   9701  O  "O3'" . C   C 2 56  ? 161.731 164.648 182.113 1.00 143.49 ? 56  C   C "O3'" 1 
ATOM   9702  C  "C2'" . C   C 2 56  ? 159.719 164.896 183.499 1.00 144.26 ? 56  C   C "C2'" 1 
ATOM   9703  O  "O2'" . C   C 2 56  ? 160.225 163.778 184.196 1.00 145.90 ? 56  C   C "O2'" 1 
ATOM   9704  C  "C1'" . C   C 2 56  ? 159.374 165.998 184.503 1.00 143.51 ? 56  C   C "C1'" 1 
ATOM   9705  N  N1    . C   C 2 56  ? 158.219 166.838 184.086 1.00 145.95 ? 56  C   C N1    1 
ATOM   9706  C  C2    . C   C 2 56  ? 156.933 166.339 184.299 1.00 144.81 ? 56  C   C C2    1 
ATOM   9707  O  O2    . C   C 2 56  ? 156.807 165.204 184.781 1.00 147.15 ? 56  C   C O2    1 
ATOM   9708  N  N3    . C   C 2 56  ? 155.870 167.094 183.940 1.00 140.40 ? 56  C   C N3    1 
ATOM   9709  C  C4    . C   C 2 56  ? 156.049 168.314 183.420 1.00 143.40 ? 56  C   C C4    1 
ATOM   9710  N  N4    . C   C 2 56  ? 154.971 169.010 183.091 1.00 145.13 ? 56  C   C N4    1 
ATOM   9711  C  C5    . C   C 2 56  ? 157.350 168.848 183.220 1.00 147.14 ? 56  C   C C5    1 
ATOM   9712  C  C6    . C   C 2 56  ? 158.396 168.088 183.574 1.00 147.35 ? 56  C   C C6    1 
ATOM   9713  P  P     . A   C 2 57  ? 161.427 163.823 180.770 1.00 127.93 ? 57  A   C P     1 
ATOM   9714  O  OP1   . A   C 2 57  ? 162.489 162.790 180.468 1.00 137.98 ? 57  A   C OP1   1 
ATOM   9715  O  OP2   . A   C 2 57  ? 161.082 164.721 179.602 1.00 136.95 ? 57  A   C OP2   1 
ATOM   9716  O  "O5'" . A   C 2 57  ? 160.096 163.018 181.161 1.00 133.61 ? 57  A   C "O5'" 1 
ATOM   9717  C  "C5'" . A   C 2 57  ? 159.123 162.739 180.133 1.00 137.87 ? 57  A   C "C5'" 1 
ATOM   9718  C  "C4'" . A   C 2 57  ? 157.876 162.208 180.790 1.00 134.50 ? 57  A   C "C4'" 1 
ATOM   9719  O  "O4'" . A   C 2 57  ? 157.411 163.162 181.774 1.00 136.26 ? 57  A   C "O4'" 1 
ATOM   9720  C  "C3'" . A   C 2 57  ? 156.669 161.998 179.875 1.00 132.67 ? 57  A   C "C3'" 1 
ATOM   9721  O  "O3'" . A   C 2 57  ? 156.769 160.744 179.219 1.00 126.72 ? 57  A   C "O3'" 1 
ATOM   9722  C  "C2'" . A   C 2 57  ? 155.517 162.076 180.875 1.00 139.28 ? 57  A   C "C2'" 1 
ATOM   9723  O  "O2'" . A   C 2 57  ? 155.335 160.866 181.575 1.00 142.23 ? 57  A   C "O2'" 1 
ATOM   9724  C  "C1'" . A   C 2 57  ? 156.002 163.187 181.802 1.00 137.72 ? 57  A   C "C1'" 1 
ATOM   9725  N  N9    . A   C 2 57  ? 155.563 164.513 181.393 1.00 136.11 ? 57  A   C N9    1 
ATOM   9726  C  C8    . A   C 2 57  ? 156.362 165.590 181.108 1.00 136.43 ? 57  A   C C8    1 
ATOM   9727  N  N7    . A   C 2 57  ? 155.689 166.654 180.753 1.00 137.62 ? 57  A   C N7    1 
ATOM   9728  C  C5    . A   C 2 57  ? 154.363 166.252 180.795 1.00 136.74 ? 57  A   C C5    1 
ATOM   9729  C  C6    . A   C 2 57  ? 153.161 166.930 180.525 1.00 138.32 ? 57  A   C C6    1 
ATOM   9730  N  N6    . A   C 2 57  ? 153.101 168.203 180.146 1.00 138.86 ? 57  A   C N6    1 
ATOM   9731  N  N1    . A   C 2 57  ? 152.008 166.235 180.660 1.00 140.77 ? 57  A   C N1    1 
ATOM   9732  C  C2    . A   C 2 57  ? 152.077 164.953 181.037 1.00 138.86 ? 57  A   C C2    1 
ATOM   9733  N  N3    . A   C 2 57  ? 153.145 164.218 181.324 1.00 132.77 ? 57  A   C N3    1 
ATOM   9734  C  C4    . A   C 2 57  ? 154.273 164.929 181.173 1.00 134.18 ? 57  A   C C4    1 
HETATM 9735  P  P     . 1MA C 2 58  ? 157.022 160.696 177.637 1.00 100.94 ? 58  1MA C P     1 
HETATM 9736  O  OP1   . 1MA C 2 58  ? 157.437 159.337 177.121 1.00 127.25 ? 58  1MA C OP1   1 
HETATM 9737  O  OP2   . 1MA C 2 58  ? 157.893 161.837 177.168 1.00 122.59 ? 58  1MA C OP2   1 
HETATM 9738  O  "O5'" . 1MA C 2 58  ? 155.554 161.006 177.073 1.00 125.17 ? 58  1MA C "O5'" 1 
HETATM 9739  C  "C5'" . 1MA C 2 58  ? 154.472 160.110 177.414 1.00 128.69 ? 58  1MA C "C5'" 1 
HETATM 9740  C  "C4'" . 1MA C 2 58  ? 153.513 160.052 176.253 1.00 126.88 ? 58  1MA C "C4'" 1 
HETATM 9741  O  "O4'" . 1MA C 2 58  ? 153.184 161.408 175.856 1.00 125.25 ? 58  1MA C "O4'" 1 
HETATM 9742  C  "C3'" . 1MA C 2 58  ? 154.045 159.362 174.991 1.00 122.13 ? 58  1MA C "C3'" 1 
HETATM 9743  O  "O3'" . 1MA C 2 58  ? 153.008 158.703 174.278 1.00 122.36 ? 58  1MA C "O3'" 1 
HETATM 9744  C  "C2'" . 1MA C 2 58  ? 154.573 160.537 174.172 1.00 122.96 ? 58  1MA C "C2'" 1 
HETATM 9745  O  "O2'" . 1MA C 2 58  ? 154.589 160.270 172.789 1.00 126.60 ? 58  1MA C "O2'" 1 
HETATM 9746  C  "C1'" . 1MA C 2 58  ? 153.527 161.610 174.508 1.00 120.80 ? 58  1MA C "C1'" 1 
HETATM 9747  N  N9    . 1MA C 2 58  ? 154.033 162.977 174.375 1.00 117.66 ? 58  1MA C N9    1 
HETATM 9748  C  C8    . 1MA C 2 58  ? 155.346 163.356 174.369 1.00 125.47 ? 58  1MA C C8    1 
HETATM 9749  N  N7    . 1MA C 2 58  ? 155.497 164.652 174.215 1.00 125.00 ? 58  1MA C N7    1 
HETATM 9750  C  C5    . 1MA C 2 58  ? 154.207 165.143 174.100 1.00 123.73 ? 58  1MA C C5    1 
HETATM 9751  C  C6    . 1MA C 2 58  ? 153.759 166.456 173.914 1.00 127.50 ? 58  1MA C C6    1 
HETATM 9752  N  N6    . 1MA C 2 58  ? 154.431 167.519 173.733 1.00 130.13 ? 58  1MA C N6    1 
HETATM 9753  N  N1    . 1MA C 2 58  ? 152.359 166.548 173.947 1.00 124.39 ? 58  1MA C N1    1 
HETATM 9754  C  CM1   . 1MA C 2 58  ? 151.738 167.880 173.914 1.00 125.20 ? 58  1MA C CM1   1 
HETATM 9755  C  C2    . 1MA C 2 58  ? 151.552 165.448 174.006 1.00 124.43 ? 58  1MA C C2    1 
HETATM 9756  N  N3    . 1MA C 2 58  ? 151.960 164.222 174.122 1.00 124.82 ? 58  1MA C N3    1 
HETATM 9757  C  C4    . 1MA C 2 58  ? 153.306 164.109 174.187 1.00 120.80 ? 58  1MA C C4    1 
ATOM   9758  P  P     . G   C 2 59  ? 152.346 157.347 174.821 1.00 84.09  ? 59  G   C P     1 
ATOM   9759  O  OP1   . G   C 2 59  ? 151.671 157.489 176.165 1.00 95.18  ? 59  G   C OP1   1 
ATOM   9760  O  OP2   . G   C 2 59  ? 153.295 156.177 174.729 1.00 99.73  ? 59  G   C OP2   1 
ATOM   9761  O  "O5'" . G   C 2 59  ? 151.192 157.087 173.736 1.00 104.74 ? 59  G   C "O5'" 1 
ATOM   9762  C  "C5'" . G   C 2 59  ? 151.570 156.614 172.423 1.00 105.10 ? 59  G   C "C5'" 1 
ATOM   9763  C  "C4'" . G   C 2 59  ? 150.477 156.960 171.445 1.00 104.43 ? 59  G   C "C4'" 1 
ATOM   9764  O  "O4'" . G   C 2 59  ? 149.216 156.451 171.945 1.00 109.24 ? 59  G   C "O4'" 1 
ATOM   9765  C  "C3'" . G   C 2 59  ? 150.237 158.455 171.218 1.00 103.00 ? 59  G   C "C3'" 1 
ATOM   9766  O  "O3'" . G   C 2 59  ? 151.050 158.947 170.162 1.00 94.82  ? 59  G   C "O3'" 1 
ATOM   9767  C  "C2'" . G   C 2 59  ? 148.763 158.482 170.817 1.00 108.08 ? 59  G   C "C2'" 1 
ATOM   9768  O  "O2'" . G   C 2 59  ? 148.575 158.219 169.445 1.00 107.53 ? 59  G   C "O2'" 1 
ATOM   9769  C  "C1'" . G   C 2 59  ? 148.172 157.350 171.649 1.00 103.11 ? 59  G   C "C1'" 1 
ATOM   9770  N  N9    . G   C 2 59  ? 147.561 157.785 172.898 1.00 103.85 ? 59  G   C N9    1 
ATOM   9771  C  C8    . G   C 2 59  ? 148.052 157.601 174.164 1.00 104.47 ? 59  G   C C8    1 
ATOM   9772  N  N7    . G   C 2 59  ? 147.267 158.074 175.099 1.00 103.44 ? 59  G   C N7    1 
ATOM   9773  C  C5    . G   C 2 59  ? 146.179 158.582 174.404 1.00 97.46  ? 59  G   C C5    1 
ATOM   9774  C  C6    . G   C 2 59  ? 145.011 159.218 174.886 1.00 91.85  ? 59  G   C C6    1 
ATOM   9775  O  O6    . G   C 2 59  ? 144.703 159.466 176.059 1.00 92.44  ? 59  G   C O6    1 
ATOM   9776  N  N1    . G   C 2 59  ? 144.160 159.578 173.842 1.00 92.08  ? 59  G   C N1    1 
ATOM   9777  C  C2    . G   C 2 59  ? 144.404 159.356 172.511 1.00 95.39  ? 59  G   C C2    1 
ATOM   9778  N  N2    . G   C 2 59  ? 143.464 159.769 171.652 1.00 101.40 ? 59  G   C N2    1 
ATOM   9779  N  N3    . G   C 2 59  ? 145.502 158.759 172.052 1.00 96.48  ? 59  G   C N3    1 
ATOM   9780  C  C4    . G   C 2 59  ? 146.337 158.391 173.051 1.00 100.67 ? 59  G   C C4    1 
ATOM   9781  P  P     . U   C 2 60  ? 151.743 160.398 170.221 1.00 84.50  ? 60  U   C P     1 
ATOM   9782  O  OP1   . U   C 2 60  ? 152.268 160.811 168.860 1.00 103.63 ? 60  U   C OP1   1 
ATOM   9783  O  OP2   . U   C 2 60  ? 152.781 160.485 171.316 1.00 114.13 ? 60  U   C OP2   1 
ATOM   9784  O  "O5'" . U   C 2 60  ? 150.587 161.459 170.604 1.00 103.80 ? 60  U   C "O5'" 1 
ATOM   9785  C  "C5'" . U   C 2 60  ? 149.553 161.759 169.635 1.00 107.81 ? 60  U   C "C5'" 1 
ATOM   9786  C  "C4'" . U   C 2 60  ? 148.367 162.347 170.359 1.00 107.38 ? 60  U   C "C4'" 1 
ATOM   9787  O  "O4'" . U   C 2 60  ? 148.069 161.516 171.508 1.00 106.52 ? 60  U   C "O4'" 1 
ATOM   9788  C  "C3'" . U   C 2 60  ? 148.551 163.779 170.889 1.00 110.31 ? 60  U   C "C3'" 1 
ATOM   9789  O  "O3'" . U   C 2 60  ? 147.628 164.674 170.278 1.00 107.69 ? 60  U   C "O3'" 1 
ATOM   9790  C  "C2'" . U   C 2 60  ? 148.313 163.697 172.405 1.00 114.39 ? 60  U   C "C2'" 1 
ATOM   9791  O  "O2'" . U   C 2 60  ? 147.374 164.652 172.850 1.00 120.44 ? 60  U   C "O2'" 1 
ATOM   9792  C  "C1'" . U   C 2 60  ? 147.717 162.306 172.620 1.00 108.44 ? 60  U   C "C1'" 1 
ATOM   9793  N  N1    . U   C 2 60  ? 148.256 161.657 173.829 1.00 109.10 ? 60  U   C N1    1 
ATOM   9794  C  C2    . U   C 2 60  ? 147.521 161.777 174.994 1.00 109.84 ? 60  U   C C2    1 
ATOM   9795  O  O2    . U   C 2 60  ? 146.451 162.368 175.047 1.00 105.70 ? 60  U   C O2    1 
ATOM   9796  N  N3    . U   C 2 60  ? 148.076 161.163 176.088 1.00 113.40 ? 60  U   C N3    1 
ATOM   9797  C  C4    . U   C 2 60  ? 149.270 160.471 176.138 1.00 108.74 ? 60  U   C C4    1 
ATOM   9798  O  O4    . U   C 2 60  ? 149.635 159.974 177.203 1.00 112.61 ? 60  U   C O4    1 
ATOM   9799  C  C5    . U   C 2 60  ? 149.977 160.402 174.893 1.00 104.53 ? 60  U   C C5    1 
ATOM   9800  C  C6    . U   C 2 60  ? 149.458 160.991 173.805 1.00 107.60 ? 60  U   C C6    1 
ATOM   9801  P  P     . C   C 2 61  ? 147.883 165.262 168.804 1.00 108.68 ? 61  C   C P     1 
ATOM   9802  O  OP1   . C   C 2 61  ? 146.786 166.223 168.387 1.00 121.98 ? 61  C   C OP1   1 
ATOM   9803  O  OP2   . C   C 2 61  ? 148.187 164.199 167.765 1.00 122.76 ? 61  C   C OP2   1 
ATOM   9804  O  "O5'" . C   C 2 61  ? 149.223 166.141 168.984 1.00 119.45 ? 61  C   C "O5'" 1 
ATOM   9805  C  "C5'" . C   C 2 61  ? 149.125 167.441 169.620 1.00 124.44 ? 61  C   C "C5'" 1 
ATOM   9806  C  "C4'" . C   C 2 61  ? 150.476 168.110 169.581 1.00 123.47 ? 61  C   C "C4'" 1 
ATOM   9807  O  "O4'" . C   C 2 61  ? 151.306 167.596 170.652 1.00 121.22 ? 61  C   C "O4'" 1 
ATOM   9808  C  "C3'" . C   C 2 61  ? 151.299 167.866 168.310 1.00 125.83 ? 61  C   C "C3'" 1 
ATOM   9809  O  "O3'" . C   C 2 61  ? 150.915 168.750 167.260 1.00 125.76 ? 61  C   C "O3'" 1 
ATOM   9810  C  "C2'" . C   C 2 61  ? 152.732 168.097 168.810 1.00 127.89 ? 61  C   C "C2'" 1 
ATOM   9811  O  "O2'" . C   C 2 61  ? 153.095 169.461 168.832 1.00 124.68 ? 61  C   C "O2'" 1 
ATOM   9812  C  "C1'" . C   C 2 61  ? 152.661 167.585 170.254 1.00 124.40 ? 61  C   C "C1'" 1 
ATOM   9813  N  N1    . C   C 2 61  ? 153.190 166.204 170.416 1.00 121.01 ? 61  C   C N1    1 
ATOM   9814  C  C2    . C   C 2 61  ? 154.554 166.041 170.669 1.00 120.66 ? 61  C   C C2    1 
ATOM   9815  O  O2    . C   C 2 61  ? 155.274 167.050 170.736 1.00 122.73 ? 61  C   C O2    1 
ATOM   9816  N  N3    . C   C 2 61  ? 155.047 164.789 170.828 1.00 119.99 ? 61  C   C N3    1 
ATOM   9817  C  C4    . C   C 2 61  ? 154.237 163.727 170.749 1.00 123.76 ? 61  C   C C4    1 
ATOM   9818  N  N4    . C   C 2 61  ? 154.772 162.526 170.912 1.00 127.38 ? 61  C   C N4    1 
ATOM   9819  C  C5    . C   C 2 61  ? 152.845 163.875 170.499 1.00 125.42 ? 61  C   C C5    1 
ATOM   9820  C  C6    . C   C 2 61  ? 152.367 165.119 170.344 1.00 123.38 ? 61  C   C C6    1 
ATOM   9821  P  P     . C   C 2 62  ? 151.244 168.416 165.720 1.00 126.20 ? 62  C   C P     1 
ATOM   9822  O  OP1   . C   C 2 62  ? 150.555 169.331 164.732 1.00 126.82 ? 62  C   C OP1   1 
ATOM   9823  O  OP2   . C   C 2 62  ? 151.016 166.944 165.449 1.00 135.75 ? 62  C   C OP2   1 
ATOM   9824  O  "O5'" . C   C 2 62  ? 152.826 168.675 165.580 1.00 136.79 ? 62  C   C "O5'" 1 
ATOM   9825  C  "C5'" . C   C 2 62  ? 153.326 170.031 165.665 1.00 138.46 ? 62  C   C "C5'" 1 
ATOM   9826  C  "C4'" . C   C 2 62  ? 154.822 169.998 165.490 1.00 138.84 ? 62  C   C "C4'" 1 
ATOM   9827  O  "O4'" . C   C 2 62  ? 155.423 169.297 166.607 1.00 136.37 ? 62  C   C "O4'" 1 
ATOM   9828  C  "C3'" . C   C 2 62  ? 155.319 169.240 164.253 1.00 138.99 ? 62  C   C "C3'" 1 
ATOM   9829  O  "O3'" . C   C 2 62  ? 155.324 170.066 163.097 1.00 135.24 ? 62  C   C "O3'" 1 
ATOM   9830  C  "C2'" . C   C 2 62  ? 156.735 168.849 164.677 1.00 135.64 ? 62  C   C "C2'" 1 
ATOM   9831  O  "O2'" . C   C 2 62  ? 157.653 169.912 164.544 1.00 135.37 ? 62  C   C "O2'" 1 
ATOM   9832  C  "C1'" . C   C 2 62  ? 156.539 168.553 166.166 1.00 134.51 ? 62  C   C "C1'" 1 
ATOM   9833  N  N1    . C   C 2 62  ? 156.303 167.111 166.442 1.00 133.99 ? 62  C   C N1    1 
ATOM   9834  C  C2    . C   C 2 62  ? 157.422 166.291 166.579 1.00 134.33 ? 62  C   C C2    1 
ATOM   9835  O  O2    . C   C 2 62  ? 158.545 166.799 166.448 1.00 135.69 ? 62  C   C O2    1 
ATOM   9836  N  N3    . C   C 2 62  ? 157.244 164.976 166.838 1.00 132.66 ? 62  C   C N3    1 
ATOM   9837  C  C4    . C   C 2 62  ? 156.012 164.476 166.973 1.00 134.11 ? 62  C   C C4    1 
ATOM   9838  N  N4    . C   C 2 62  ? 155.896 163.183 167.228 1.00 136.27 ? 62  C   C N4    1 
ATOM   9839  C  C5    . C   C 2 62  ? 154.861 165.299 166.847 1.00 136.29 ? 62  C   C C5    1 
ATOM   9840  C  C6    . C   C 2 62  ? 155.049 166.600 166.588 1.00 137.24 ? 62  C   C C6    1 
ATOM   9841  P  P     . C   C 2 63  ? 155.222 169.424 161.629 1.00 129.60 ? 63  C   C P     1 
ATOM   9842  O  OP1   . C   C 2 63  ? 155.305 170.466 160.534 1.00 138.76 ? 63  C   C OP1   1 
ATOM   9843  O  OP2   . C   C 2 63  ? 154.024 168.507 161.508 1.00 136.07 ? 63  C   C OP2   1 
ATOM   9844  O  "O5'" . C   C 2 63  ? 156.535 168.502 161.493 1.00 135.37 ? 63  C   C "O5'" 1 
ATOM   9845  C  "C5'" . C   C 2 63  ? 157.824 169.144 161.356 1.00 139.45 ? 63  C   C "C5'" 1 
ATOM   9846  C  "C4'" . C   C 2 63  ? 158.884 168.081 161.216 1.00 139.80 ? 63  C   C "C4'" 1 
ATOM   9847  O  "O4'" . C   C 2 63  ? 158.973 167.306 162.438 1.00 140.72 ? 63  C   C "O4'" 1 
ATOM   9848  C  "C3'" . C   C 2 63  ? 158.627 167.023 160.139 1.00 135.39 ? 63  C   C "C3'" 1 
ATOM   9849  O  "O3'" . C   C 2 63  ? 158.941 167.515 158.843 1.00 132.25 ? 63  C   C "O3'" 1 
ATOM   9850  C  "C2'" . C   C 2 63  ? 159.557 165.901 160.610 1.00 137.69 ? 63  C   C "C2'" 1 
ATOM   9851  O  "O2'" . C   C 2 63  ? 160.908 166.133 160.276 1.00 141.08 ? 63  C   C "O2'" 1 
ATOM   9852  C  "C1'" . C   C 2 63  ? 159.399 165.995 162.131 1.00 135.93 ? 63  C   C "C1'" 1 
ATOM   9853  N  N1    . C   C 2 63  ? 158.401 165.026 162.656 1.00 134.94 ? 63  C   C N1    1 
ATOM   9854  C  C2    . C   C 2 63  ? 158.844 163.738 162.950 1.00 136.91 ? 63  C   C C2    1 
ATOM   9855  O  O2    . C   C 2 63  ? 160.037 163.464 162.757 1.00 137.94 ? 63  C   C O2    1 
ATOM   9856  N  N3    . C   C 2 63  ? 157.960 162.832 163.423 1.00 138.65 ? 63  C   C N3    1 
ATOM   9857  C  C4    . C   C 2 63  ? 156.680 163.172 163.610 1.00 137.73 ? 63  C   C C4    1 
ATOM   9858  N  N4    . C   C 2 63  ? 155.860 162.245 164.079 1.00 139.07 ? 63  C   C N4    1 
ATOM   9859  C  C5    . C   C 2 63  ? 156.213 164.482 163.321 1.00 138.19 ? 63  C   C C5    1 
ATOM   9860  C  C6    . C   C 2 63  ? 157.099 165.372 162.852 1.00 137.76 ? 63  C   C C6    1 
ATOM   9861  P  P     . U   C 2 64  ? 158.586 166.663 157.529 1.00 126.21 ? 64  U   C P     1 
ATOM   9862  O  OP1   . U   C 2 64  ? 158.808 167.439 156.249 1.00 132.94 ? 64  U   C OP1   1 
ATOM   9863  O  OP2   . U   C 2 64  ? 157.229 166.001 157.613 1.00 130.34 ? 64  U   C OP2   1 
ATOM   9864  O  "O5'" . U   C 2 64  ? 159.683 165.489 157.557 1.00 130.05 ? 64  U   C "O5'" 1 
ATOM   9865  C  "C5'" . U   C 2 64  ? 159.493 164.335 156.709 1.00 127.77 ? 64  U   C "C5'" 1 
ATOM   9866  C  "C4'" . U   C 2 64  ? 160.564 163.323 157.023 1.00 128.46 ? 64  U   C "C4'" 1 
ATOM   9867  O  "O4'" . U   C 2 64  ? 160.781 163.280 158.459 1.00 128.41 ? 64  U   C "O4'" 1 
ATOM   9868  C  "C3'" . U   C 2 64  ? 160.253 161.869 156.650 1.00 132.56 ? 64  U   C "C3'" 1 
ATOM   9869  O  "O3'" . U   C 2 64  ? 160.557 161.548 155.300 1.00 129.29 ? 64  U   C "O3'" 1 
ATOM   9870  C  "C2'" . U   C 2 64  ? 161.158 161.127 157.633 1.00 133.60 ? 64  U   C "C2'" 1 
ATOM   9871  O  "O2'" . U   C 2 64  ? 162.525 161.241 157.305 1.00 131.86 ? 64  U   C "O2'" 1 
ATOM   9872  C  "C1'" . U   C 2 64  ? 160.870 161.939 158.892 1.00 128.37 ? 64  U   C "C1'" 1 
ATOM   9873  N  N1    . U   C 2 64  ? 159.591 161.566 159.528 1.00 129.59 ? 64  U   C N1    1 
ATOM   9874  C  C2    . U   C 2 64  ? 159.423 160.247 159.913 1.00 129.25 ? 64  U   C C2    1 
ATOM   9875  O  O2    . U   C 2 64  ? 160.285 159.389 159.784 1.00 127.62 ? 64  U   C O2    1 
ATOM   9876  N  N3    . U   C 2 64  ? 158.214 159.968 160.489 1.00 129.41 ? 64  U   C N3    1 
ATOM   9877  C  C4    . U   C 2 64  ? 157.168 160.839 160.703 1.00 128.86 ? 64  U   C C4    1 
ATOM   9878  O  O4    . U   C 2 64  ? 156.140 160.423 161.235 1.00 128.46 ? 64  U   C O4    1 
ATOM   9879  C  C5    . U   C 2 64  ? 157.408 162.181 160.261 1.00 128.50 ? 64  U   C C5    1 
ATOM   9880  C  C6    . U   C 2 64  ? 158.586 162.489 159.700 1.00 129.73 ? 64  U   C C6    1 
ATOM   9881  P  P     . G   C 2 65  ? 159.550 161.945 154.115 1.00 102.28 ? 65  G   C P     1 
ATOM   9882  O  OP1   . G   C 2 65  ? 160.085 163.064 153.248 1.00 117.54 ? 65  G   C OP1   1 
ATOM   9883  O  OP2   . G   C 2 65  ? 158.134 162.172 154.597 1.00 115.56 ? 65  G   C OP2   1 
ATOM   9884  O  "O5'" . G   C 2 65  ? 159.523 160.615 153.211 1.00 114.00 ? 65  G   C "O5'" 1 
ATOM   9885  C  "C5'" . G   C 2 65  ? 158.707 159.498 153.641 1.00 119.67 ? 65  G   C "C5'" 1 
ATOM   9886  C  "C4'" . G   C 2 65  ? 159.565 158.477 154.345 1.00 116.87 ? 65  G   C "C4'" 1 
ATOM   9887  O  "O4'" . G   C 2 65  ? 159.781 158.896 155.715 1.00 120.14 ? 65  G   C "O4'" 1 
ATOM   9888  C  "C3'" . G   C 2 65  ? 158.969 157.069 154.439 1.00 115.26 ? 65  G   C "C3'" 1 
ATOM   9889  O  "O3'" . G   C 2 65  ? 159.486 156.279 153.379 1.00 111.87 ? 65  G   C "O3'" 1 
ATOM   9890  C  "C2'" . G   C 2 65  ? 159.439 156.575 155.807 1.00 118.82 ? 65  G   C "C2'" 1 
ATOM   9891  O  "O2'" . G   C 2 65  ? 160.720 155.992 155.743 1.00 115.05 ? 65  G   C "O2'" 1 
ATOM   9892  C  "C1'" . G   C 2 65  ? 159.453 157.866 156.618 1.00 118.20 ? 65  G   C "C1'" 1 
ATOM   9893  N  N9    . G   C 2 65  ? 158.178 158.207 157.238 1.00 113.40 ? 65  G   C N9    1 
ATOM   9894  C  C8    . G   C 2 65  ? 157.615 159.457 157.247 1.00 119.05 ? 65  G   C C8    1 
ATOM   9895  N  N7    . G   C 2 65  ? 156.459 159.503 157.858 1.00 118.32 ? 65  G   C N7    1 
ATOM   9896  C  C5    . G   C 2 65  ? 156.243 158.196 158.270 1.00 117.30 ? 65  G   C C5    1 
ATOM   9897  C  C6    . G   C 2 65  ? 155.151 157.646 158.983 1.00 121.08 ? 65  G   C C6    1 
ATOM   9898  O  O6    . G   C 2 65  ? 154.141 158.229 159.396 1.00 120.00 ? 65  G   C O6    1 
ATOM   9899  N  N1    . G   C 2 65  ? 155.319 156.279 159.201 1.00 122.19 ? 65  G   C N1    1 
ATOM   9900  C  C2    . G   C 2 65  ? 156.397 155.540 158.782 1.00 122.65 ? 65  G   C C2    1 
ATOM   9901  N  N2    . G   C 2 65  ? 156.376 154.236 159.087 1.00 123.12 ? 65  G   C N2    1 
ATOM   9902  N  N3    . G   C 2 65  ? 157.430 156.054 158.114 1.00 120.87 ? 65  G   C N3    1 
ATOM   9903  C  C4    . G   C 2 65  ? 157.283 157.381 157.881 1.00 114.92 ? 65  G   C C4    1 
ATOM   9904  P  P     . U   C 2 66  ? 158.534 155.806 152.179 1.00 61.71  ? 66  U   C P     1 
ATOM   9905  O  OP1   . U   C 2 66  ? 159.276 155.136 151.045 1.00 93.83  ? 66  U   C OP1   1 
ATOM   9906  O  OP2   . U   C 2 66  ? 157.558 156.874 151.739 1.00 89.18  ? 66  U   C OP2   1 
ATOM   9907  O  "O5'" . U   C 2 66  ? 157.692 154.668 152.932 1.00 96.95  ? 66  U   C "O5'" 1 
ATOM   9908  C  "C5'" . U   C 2 66  ? 158.414 153.625 153.623 1.00 105.97 ? 66  U   C "C5'" 1 
ATOM   9909  C  "C4'" . U   C 2 66  ? 157.415 152.739 154.318 1.00 97.64  ? 66  U   C "C4'" 1 
ATOM   9910  O  "O4'" . U   C 2 66  ? 156.976 153.355 155.553 1.00 85.72  ? 66  U   C "O4'" 1 
ATOM   9911  C  "C3'" . U   C 2 66  ? 156.111 152.511 153.554 1.00 99.93  ? 66  U   C "C3'" 1 
ATOM   9912  O  "O3'" . U   C 2 66  ? 156.303 151.548 152.528 1.00 101.84 ? 66  U   C "O3'" 1 
ATOM   9913  C  "C2'" . U   C 2 66  ? 155.197 152.047 154.689 1.00 99.91  ? 66  U   C "C2'" 1 
ATOM   9914  O  "O2'" . U   C 2 66  ? 155.440 150.709 155.064 1.00 97.33  ? 66  U   C "O2'" 1 
ATOM   9915  C  "C1'" . U   C 2 66  ? 155.655 152.942 155.839 1.00 89.29  ? 66  U   C "C1'" 1 
ATOM   9916  N  N1    . U   C 2 66  ? 154.820 154.143 156.026 1.00 94.21  ? 66  U   C N1    1 
ATOM   9917  C  C2    . U   C 2 66  ? 153.671 154.007 156.785 1.00 102.97 ? 66  U   C C2    1 
ATOM   9918  O  O2    . U   C 2 66  ? 153.304 152.943 157.263 1.00 109.78 ? 66  U   C O2    1 
ATOM   9919  N  N3    . U   C 2 66  ? 152.951 155.159 156.947 1.00 99.16  ? 66  U   C N3    1 
ATOM   9920  C  C4    . U   C 2 66  ? 153.261 156.410 156.459 1.00 97.27  ? 66  U   C C4    1 
ATOM   9921  O  O4    . U   C 2 66  ? 152.503 157.350 156.694 1.00 109.41 ? 66  U   C O4    1 
ATOM   9922  C  C5    . U   C 2 66  ? 154.474 156.474 155.699 1.00 96.52  ? 66  U   C C5    1 
ATOM   9923  C  C6    . U   C 2 66  ? 155.200 155.361 155.519 1.00 101.94 ? 66  U   C C6    1 
ATOM   9924  P  P     . U   C 2 67  ? 155.407 151.573 151.197 1.00 73.74  ? 67  U   C P     1 
ATOM   9925  O  OP1   . U   C 2 67  ? 155.836 150.546 150.179 1.00 92.71  ? 67  U   C OP1   1 
ATOM   9926  O  OP2   . U   C 2 67  ? 155.262 152.970 150.646 1.00 88.18  ? 67  U   C OP2   1 
ATOM   9927  O  "O5'" . U   C 2 67  ? 153.960 151.132 151.715 1.00 102.76 ? 67  U   C "O5'" 1 
ATOM   9928  C  "C5'" . U   C 2 67  ? 153.800 149.840 152.339 1.00 106.28 ? 67  U   C "C5'" 1 
ATOM   9929  C  "C4'" . U   C 2 67  ? 152.452 149.822 153.008 1.00 102.11 ? 67  U   C "C4'" 1 
ATOM   9930  O  "O4'" . U   C 2 67  ? 152.446 150.746 154.125 1.00 95.30  ? 67  U   C "O4'" 1 
ATOM   9931  C  "C3'" . U   C 2 67  ? 151.298 150.316 152.133 1.00 94.82  ? 67  U   C "C3'" 1 
ATOM   9932  O  "O3'" . U   C 2 67  ? 150.882 149.303 151.228 1.00 91.43  ? 67  U   C "O3'" 1 
ATOM   9933  C  "C2'" . U   C 2 67  ? 150.272 150.701 153.202 1.00 98.57  ? 67  U   C "C2'" 1 
ATOM   9934  O  "O2'" . U   C 2 67  ? 149.645 149.584 153.792 1.00 106.95 ? 67  U   C "O2'" 1 
ATOM   9935  C  "C1'" . U   C 2 67  ? 151.177 151.355 154.242 1.00 86.49  ? 67  U   C "C1'" 1 
ATOM   9936  N  N1    . U   C 2 67  ? 151.318 152.808 154.040 1.00 78.67  ? 67  U   C N1    1 
ATOM   9937  C  C2    . U   C 2 67  ? 150.399 153.615 154.678 1.00 87.83  ? 67  U   C C2    1 
ATOM   9938  O  O2    . U   C 2 67  ? 149.502 153.168 155.375 1.00 100.44 ? 67  U   C O2    1 
ATOM   9939  N  N3    . U   C 2 67  ? 150.564 154.958 154.468 1.00 91.65  ? 67  U   C N3    1 
ATOM   9940  C  C4    . U   C 2 67  ? 151.538 155.563 153.702 1.00 89.14  ? 67  U   C C4    1 
ATOM   9941  O  O4    . U   C 2 67  ? 151.554 156.789 153.609 1.00 105.32 ? 67  U   C O4    1 
ATOM   9942  C  C5    . U   C 2 67  ? 152.456 154.660 153.074 1.00 83.22  ? 67  U   C C5    1 
ATOM   9943  C  C6    . U   C 2 67  ? 152.315 153.341 153.262 1.00 89.24  ? 67  U   C C6    1 
ATOM   9944  P  P     . C   C 2 68  ? 149.737 149.614 150.150 1.00 62.60  ? 68  C   C P     1 
ATOM   9945  O  OP1   . C   C 2 68  ? 149.527 148.538 149.114 1.00 102.97 ? 68  C   C OP1   1 
ATOM   9946  O  OP2   . C   C 2 68  ? 149.847 151.010 149.587 1.00 89.97  ? 68  C   C OP2   1 
ATOM   9947  O  "O5'" . C   C 2 68  ? 148.462 149.596 151.113 1.00 79.81  ? 68  C   C "O5'" 1 
ATOM   9948  C  "C5'" . C   C 2 68  ? 147.204 150.022 150.575 1.00 95.76  ? 68  C   C "C5'" 1 
ATOM   9949  C  "C4'" . C   C 2 68  ? 146.407 150.715 151.648 1.00 91.80  ? 68  C   C "C4'" 1 
ATOM   9950  O  "O4'" . C   C 2 68  ? 147.263 151.555 152.459 1.00 81.23  ? 68  C   C "O4'" 1 
ATOM   9951  C  "C3'" . C   C 2 68  ? 145.346 151.676 151.114 1.00 89.81  ? 68  C   C "C3'" 1 
ATOM   9952  O  "O3'" . C   C 2 68  ? 144.220 150.910 150.716 1.00 85.99  ? 68  C   C "O3'" 1 
ATOM   9953  C  "C2'" . C   C 2 68  ? 145.129 152.598 152.314 1.00 85.20  ? 68  C   C "C2'" 1 
ATOM   9954  O  "O2'" . C   C 2 68  ? 144.284 152.027 153.288 1.00 86.64  ? 68  C   C "O2'" 1 
ATOM   9955  C  "C1'" . C   C 2 68  ? 146.544 152.689 152.893 1.00 74.68  ? 68  C   C "C1'" 1 
ATOM   9956  N  N1    . C   C 2 68  ? 147.285 153.903 152.463 1.00 73.47  ? 68  C   C N1    1 
ATOM   9957  C  C2    . C   C 2 68  ? 146.887 155.138 152.974 1.00 88.34  ? 68  C   C C2    1 
ATOM   9958  O  O2    . C   C 2 68  ? 145.901 155.186 153.722 1.00 91.06  ? 68  C   C O2    1 
ATOM   9959  N  N3    . C   C 2 68  ? 147.559 156.249 152.602 1.00 97.35  ? 68  C   C N3    1 
ATOM   9960  C  C4    . C   C 2 68  ? 148.611 156.161 151.784 1.00 90.86  ? 68  C   C C4    1 
ATOM   9961  N  N4    . C   C 2 68  ? 149.235 157.284 151.467 1.00 81.87  ? 68  C   C N4    1 
ATOM   9962  C  C5    . C   C 2 68  ? 149.047 154.911 151.274 1.00 92.68  ? 68  C   C C5    1 
ATOM   9963  C  C6    . C   C 2 68  ? 148.369 153.815 151.644 1.00 88.77  ? 68  C   C C6    1 
ATOM   9964  P  P     . G   C 2 69  ? 143.421 151.299 149.383 1.00 60.18  ? 69  G   C P     1 
ATOM   9965  O  OP1   . G   C 2 69  ? 142.537 150.196 148.850 1.00 80.98  ? 69  G   C OP1   1 
ATOM   9966  O  OP2   . G   C 2 69  ? 144.334 151.924 148.352 1.00 86.26  ? 69  G   C OP2   1 
ATOM   9967  O  "O5'" . G   C 2 69  ? 142.469 152.455 149.953 1.00 82.57  ? 69  G   C "O5'" 1 
ATOM   9968  C  "C5'" . G   C 2 69  ? 141.567 152.129 151.035 1.00 99.45  ? 69  G   C "C5'" 1 
ATOM   9969  C  "C4'" . G   C 2 69  ? 140.690 153.323 151.297 1.00 81.14  ? 69  G   C "C4'" 1 
ATOM   9970  O  "O4'" . G   C 2 69  ? 141.418 154.294 152.086 1.00 73.42  ? 69  G   C "O4'" 1 
ATOM   9971  C  "C3'" . G   C 2 69  ? 140.253 154.089 150.049 1.00 83.74  ? 69  G   C "C3'" 1 
ATOM   9972  O  "O3'" . G   C 2 69  ? 139.087 153.490 149.501 1.00 97.77  ? 69  G   C "O3'" 1 
ATOM   9973  C  "C2'" . G   C 2 69  ? 140.005 155.489 150.609 1.00 93.04  ? 69  G   C "C2'" 1 
ATOM   9974  O  "O2'" . G   C 2 69  ? 138.721 155.620 151.177 1.00 93.11  ? 69  G   C "O2'" 1 
ATOM   9975  C  "C1'" . G   C 2 69  ? 141.088 155.602 151.677 1.00 86.22  ? 69  G   C "C1'" 1 
ATOM   9976  N  N9    . G   C 2 69  ? 142.309 156.263 151.233 1.00 84.94  ? 69  G   C N9    1 
ATOM   9977  C  C8    . G   C 2 69  ? 143.453 155.660 150.778 1.00 85.49  ? 69  G   C C8    1 
ATOM   9978  N  N7    . G   C 2 69  ? 144.404 156.512 150.485 1.00 76.40  ? 69  G   C N7    1 
ATOM   9979  C  C5    . G   C 2 69  ? 143.855 157.752 150.781 1.00 75.75  ? 69  G   C C5    1 
ATOM   9980  C  C6    . G   C 2 69  ? 144.417 159.045 150.667 1.00 87.73  ? 69  G   C C6    1 
ATOM   9981  O  O6    . G   C 2 69  ? 145.544 159.358 150.261 1.00 84.13  ? 69  G   C O6    1 
ATOM   9982  N  N1    . G   C 2 69  ? 143.515 160.029 151.071 1.00 104.80 ? 69  G   C N1    1 
ATOM   9983  C  C2    . G   C 2 69  ? 142.243 159.796 151.529 1.00 93.80  ? 69  G   C C2    1 
ATOM   9984  N  N2    . G   C 2 69  ? 141.523 160.868 151.879 1.00 79.40  ? 69  G   C N2    1 
ATOM   9985  N  N3    . G   C 2 69  ? 141.711 158.582 151.639 1.00 89.37  ? 69  G   C N3    1 
ATOM   9986  C  C4    . G   C 2 69  ? 142.569 157.611 151.248 1.00 87.24  ? 69  G   C C4    1 
ATOM   9987  P  P     . G   C 2 70  ? 138.723 153.663 147.949 1.00 67.36  ? 70  G   C P     1 
ATOM   9988  O  OP1   . G   C 2 70  ? 137.533 152.825 147.544 1.00 85.05  ? 70  G   C OP1   1 
ATOM   9989  O  OP2   . G   C 2 70  ? 139.936 153.480 147.066 1.00 94.50  ? 70  G   C OP2   1 
ATOM   9990  O  "O5'" . G   C 2 70  ? 138.282 155.202 147.837 1.00 91.49  ? 70  G   C "O5'" 1 
ATOM   9991  C  "C5'" . G   C 2 70  ? 139.196 156.139 147.230 1.00 100.02 ? 70  G   C "C5'" 1 
ATOM   9992  C  "C4'" . G   C 2 70  ? 138.733 157.538 147.537 1.00 91.05  ? 70  G   C "C4'" 1 
ATOM   9993  O  "O4'" . G   C 2 70  ? 139.532 158.074 148.623 1.00 80.48  ? 70  G   C "O4'" 1 
ATOM   9994  C  "C3'" . G   C 2 70  ? 138.888 158.550 146.398 1.00 97.36  ? 70  G   C "C3'" 1 
ATOM   9995  O  "O3'" . G   C 2 70  ? 137.745 158.566 145.555 1.00 95.82  ? 70  G   C "O3'" 1 
ATOM   9996  C  "C2'" . G   C 2 70  ? 139.048 159.856 147.173 1.00 94.85  ? 70  G   C "C2'" 1 
ATOM   9997  O  "O2'" . G   C 2 70  ? 137.826 160.363 147.658 1.00 100.13 ? 70  G   C "O2'" 1 
ATOM   9998  C  "C1'" . G   C 2 70  ? 139.936 159.388 148.315 1.00 79.98  ? 70  G   C "C1'" 1 
ATOM   9999  N  N9    . G   C 2 70  ? 141.351 159.376 147.978 1.00 78.49  ? 70  G   C N9    1 
ATOM   10000 C  C8    . G   C 2 70  ? 142.141 158.284 147.725 1.00 94.43  ? 70  G   C C8    1 
ATOM   10001 N  N7    . G   C 2 70  ? 143.387 158.598 147.475 1.00 99.22  ? 70  G   C N7    1 
ATOM   10002 C  C5    . G   C 2 70  ? 143.420 159.982 147.585 1.00 93.93  ? 70  G   C C5    1 
ATOM   10003 C  C6    . G   C 2 70  ? 144.497 160.884 147.424 1.00 93.50  ? 70  G   C C6    1 
ATOM   10004 O  O6    . G   C 2 70  ? 145.673 160.627 147.138 1.00 92.65  ? 70  G   C O6    1 
ATOM   10005 N  N1    . G   C 2 70  ? 144.089 162.202 147.622 1.00 93.49  ? 70  G   C N1    1 
ATOM   10006 C  C2    . G   C 2 70  ? 142.813 162.598 147.936 1.00 91.18  ? 70  G   C C2    1 
ATOM   10007 N  N2    . G   C 2 70  ? 142.609 163.912 148.094 1.00 97.16  ? 70  G   C N2    1 
ATOM   10008 N  N3    . G   C 2 70  ? 141.799 161.754 148.093 1.00 88.21  ? 70  G   C N3    1 
ATOM   10009 C  C4    . G   C 2 70  ? 142.177 160.469 147.911 1.00 85.11  ? 70  G   C C4    1 
ATOM   10010 P  P     . G   C 2 71  ? 137.884 158.945 144.002 1.00 87.24  ? 71  G   C P     1 
ATOM   10011 O  OP1   . G   C 2 71  ? 136.549 158.966 143.294 1.00 102.38 ? 71  G   C OP1   1 
ATOM   10012 O  OP2   . G   C 2 71  ? 138.940 158.117 143.302 1.00 106.31 ? 71  G   C OP2   1 
ATOM   10013 O  "O5'" . G   C 2 71  ? 138.419 160.457 144.027 1.00 105.71 ? 71  G   C "O5'" 1 
ATOM   10014 C  "C5'" . G   C 2 71  ? 137.529 161.494 144.491 1.00 109.39 ? 71  G   C "C5'" 1 
ATOM   10015 C  "C4'" . G   C 2 71  ? 138.213 162.825 144.322 1.00 110.88 ? 71  G   C "C4'" 1 
ATOM   10016 O  "O4'" . G   C 2 71  ? 139.312 162.933 145.260 1.00 106.84 ? 71  G   C "O4'" 1 
ATOM   10017 C  "C3'" . G   C 2 71  ? 138.869 163.068 142.960 1.00 113.56 ? 71  G   C "C3'" 1 
ATOM   10018 O  "O3'" . G   C 2 71  ? 137.935 163.465 141.965 1.00 110.49 ? 71  G   C "O3'" 1 
ATOM   10019 C  "C2'" . G   C 2 71  ? 139.859 164.172 143.329 1.00 112.84 ? 71  G   C "C2'" 1 
ATOM   10020 O  "O2'" . G   C 2 71  ? 139.242 165.431 143.472 1.00 115.94 ? 71  G   C "O2'" 1 
ATOM   10021 C  "C1'" . G   C 2 71  ? 140.372 163.647 144.664 1.00 103.79 ? 71  G   C "C1'" 1 
ATOM   10022 N  N9    . G   C 2 71  ? 141.518 162.760 144.519 1.00 98.27  ? 71  G   C N9    1 
ATOM   10023 C  C8    . G   C 2 71  ? 141.524 161.390 144.496 1.00 106.50 ? 71  G   C C8    1 
ATOM   10024 N  N7    . G   C 2 71  ? 142.723 160.883 144.348 1.00 110.83 ? 71  G   C N7    1 
ATOM   10025 C  C5    . G   C 2 71  ? 143.556 161.991 144.273 1.00 106.68 ? 71  G   C C5    1 
ATOM   10026 C  C6    . G   C 2 71  ? 144.960 162.070 144.110 1.00 113.86 ? 71  G   C C6    1 
ATOM   10027 O  O6    . G   C 2 71  ? 145.771 161.142 144.000 1.00 118.50 ? 71  G   C O6    1 
ATOM   10028 N  N1    . G   C 2 71  ? 145.396 163.395 144.083 1.00 114.38 ? 71  G   C N1    1 
ATOM   10029 C  C2    . G   C 2 71  ? 144.586 164.496 144.196 1.00 110.65 ? 71  G   C C2    1 
ATOM   10030 N  N2    . G   C 2 71  ? 145.183 165.693 144.150 1.00 109.15 ? 71  G   C N2    1 
ATOM   10031 N  N3    . G   C 2 71  ? 143.267 164.428 144.352 1.00 109.80 ? 71  G   C N3    1 
ATOM   10032 C  C4    . G   C 2 71  ? 142.826 163.150 144.388 1.00 105.19 ? 71  G   C C4    1 
ATOM   10033 P  P     . C   C 2 72  ? 138.340 163.438 140.412 1.00 107.46 ? 72  C   C P     1 
ATOM   10034 O  OP1   . C   C 2 72  ? 137.168 163.758 139.514 1.00 121.19 ? 72  C   C OP1   1 
ATOM   10035 O  OP2   . C   C 2 72  ? 139.083 162.175 140.035 1.00 120.02 ? 72  C   C OP2   1 
ATOM   10036 O  "O5'" . C   C 2 72  ? 139.386 164.650 140.282 1.00 114.74 ? 72  C   C "O5'" 1 
ATOM   10037 C  "C5'" . C   C 2 72  ? 140.185 164.757 139.082 1.00 122.75 ? 72  C   C "C5'" 1 
ATOM   10038 C  "C4'" . C   C 2 72  ? 141.299 165.742 139.330 1.00 120.94 ? 72  C   C "C4'" 1 
ATOM   10039 O  "O4'" . C   C 2 72  ? 141.880 165.481 140.635 1.00 115.06 ? 72  C   C "O4'" 1 
ATOM   10040 C  "C3'" . C   C 2 72  ? 142.486 165.677 138.359 1.00 124.59 ? 72  C   C "C3'" 1 
ATOM   10041 O  "O3'" . C   C 2 72  ? 142.332 166.481 137.196 1.00 122.45 ? 72  C   C "O3'" 1 
ATOM   10042 C  "C2'" . C   C 2 72  ? 143.625 166.189 139.241 1.00 125.50 ? 72  C   C "C2'" 1 
ATOM   10043 O  "O2'" . C   C 2 72  ? 143.570 167.582 139.456 1.00 119.81 ? 72  C   C "O2'" 1 
ATOM   10044 C  "C1'" . C   C 2 72  ? 143.288 165.480 140.551 1.00 122.51 ? 72  C   C "C1'" 1 
ATOM   10045 N  N1    . C   C 2 72  ? 143.764 164.072 140.595 1.00 120.34 ? 72  C   C N1    1 
ATOM   10046 C  C2    . C   C 2 72  ? 145.131 163.815 140.465 1.00 120.40 ? 72  C   C C2    1 
ATOM   10047 O  O2    . C   C 2 72  ? 145.913 164.766 140.330 1.00 125.35 ? 72  C   C O2    1 
ATOM   10048 N  N3    . C   C 2 72  ? 145.567 162.537 140.508 1.00 116.89 ? 72  C   C N3    1 
ATOM   10049 C  C4    . C   C 2 72  ? 144.703 161.530 140.670 1.00 115.42 ? 72  C   C C4    1 
ATOM   10050 N  N4    . C   C 2 72  ? 145.192 160.300 140.700 1.00 120.98 ? 72  C   C N4    1 
ATOM   10051 C  C5    . C   C 2 72  ? 143.309 161.768 140.796 1.00 115.86 ? 72  C   C C5    1 
ATOM   10052 C  C6    . C   C 2 72  ? 142.888 163.040 140.757 1.00 119.57 ? 72  C   C C6    1 
ATOM   10053 P  P     . G   C 2 73  ? 141.548 165.936 135.904 1.00 118.67 ? 73  G   C P     1 
ATOM   10054 O  OP1   . G   C 2 73  ? 141.994 166.644 134.642 1.00 130.93 ? 73  G   C OP1   1 
ATOM   10055 O  OP2   . G   C 2 73  ? 140.046 165.914 136.087 1.00 127.41 ? 73  G   C OP2   1 
ATOM   10056 O  "O5'" . G   C 2 73  ? 142.031 164.401 135.779 1.00 127.13 ? 73  G   C "O5'" 1 
ATOM   10057 C  "C5'" . G   C 2 73  ? 143.038 164.051 134.794 1.00 133.68 ? 73  G   C "C5'" 1 
ATOM   10058 C  "C4'" . G   C 2 73  ? 144.377 164.612 135.205 1.00 133.69 ? 73  G   C "C4'" 1 
ATOM   10059 O  "O4'" . G   C 2 73  ? 144.580 164.366 136.619 1.00 131.91 ? 73  G   C "O4'" 1 
ATOM   10060 C  "C3'" . G   C 2 73  ? 145.603 164.001 134.519 1.00 134.37 ? 73  G   C "C3'" 1 
ATOM   10061 O  "O3'" . G   C 2 73  ? 145.933 164.705 133.329 1.00 132.39 ? 73  G   C "O3'" 1 
ATOM   10062 C  "C2'" . G   C 2 73  ? 146.677 164.134 135.600 1.00 131.80 ? 73  G   C "C2'" 1 
ATOM   10063 O  "O2'" . G   C 2 73  ? 147.240 165.425 135.650 1.00 133.72 ? 73  G   C "O2'" 1 
ATOM   10064 C  "C1'" . G   C 2 73  ? 145.865 163.843 136.857 1.00 128.93 ? 73  G   C "C1'" 1 
ATOM   10065 N  N9    . G   C 2 73  ? 145.719 162.424 137.154 1.00 128.36 ? 73  G   C N9    1 
ATOM   10066 C  C8    . G   C 2 73  ? 144.542 161.782 137.440 1.00 130.88 ? 73  G   C C8    1 
ATOM   10067 N  N7    . G   C 2 73  ? 144.691 160.499 137.653 1.00 133.34 ? 73  G   C N7    1 
ATOM   10068 C  C5    . G   C 2 73  ? 146.050 160.280 137.480 1.00 131.89 ? 73  G   C C5    1 
ATOM   10069 C  C6    . G   C 2 73  ? 146.794 159.081 137.582 1.00 132.87 ? 73  G   C C6    1 
ATOM   10070 O  O6    . G   C 2 73  ? 146.380 157.946 137.856 1.00 138.03 ? 73  G   C O6    1 
ATOM   10071 N  N1    . G   C 2 73  ? 148.147 159.298 137.326 1.00 128.35 ? 73  G   C N1    1 
ATOM   10072 C  C2    . G   C 2 73  ? 148.708 160.511 137.015 1.00 130.41 ? 73  G   C C2    1 
ATOM   10073 N  N2    . G   C 2 73  ? 150.030 160.523 136.806 1.00 131.95 ? 73  G   C N2    1 
ATOM   10074 N  N3    . G   C 2 73  ? 148.013 161.644 136.921 1.00 133.44 ? 73  G   C N3    1 
ATOM   10075 C  C4    . G   C 2 73  ? 146.692 161.453 137.151 1.00 131.69 ? 73  G   C C4    1 
ATOM   10076 P  P     . C   C 2 74  ? 145.586 164.082 131.891 1.00 122.39 ? 74  C   C P     1 
ATOM   10077 O  OP1   . C   C 2 74  ? 146.188 164.872 130.750 1.00 135.07 ? 74  C   C OP1   1 
ATOM   10078 O  OP2   . C   C 2 74  ? 144.122 163.746 131.705 1.00 133.92 ? 74  C   C OP2   1 
ATOM   10079 O  "O5'" . C   C 2 74  ? 146.383 162.689 131.967 1.00 126.89 ? 74  C   C "O5'" 1 
ATOM   10080 C  "C5'" . C   C 2 74  ? 147.817 162.722 132.162 1.00 133.03 ? 74  C   C "C5'" 1 
ATOM   10081 C  "C4'" . C   C 2 74  ? 148.328 161.306 132.178 1.00 131.61 ? 74  C   C "C4'" 1 
ATOM   10082 O  "O4'" . C   C 2 74  ? 147.992 160.677 133.438 1.00 129.82 ? 74  C   C "O4'" 1 
ATOM   10083 C  "C3'" . C   C 2 74  ? 147.710 160.383 131.124 1.00 132.79 ? 74  C   C "C3'" 1 
ATOM   10084 O  "O3'" . C   C 2 74  ? 148.358 160.565 129.872 1.00 132.13 ? 74  C   C "O3'" 1 
ATOM   10085 C  "C2'" . C   C 2 74  ? 147.945 159.001 131.744 1.00 134.04 ? 74  C   C "C2'" 1 
ATOM   10086 O  "O2'" . C   C 2 74  ? 149.236 158.500 131.475 1.00 132.86 ? 74  C   C "O2'" 1 
ATOM   10087 C  "C1'" . C   C 2 74  ? 147.821 159.290 133.244 1.00 132.54 ? 74  C   C "C1'" 1 
ATOM   10088 N  N1    . C   C 2 74  ? 146.501 158.893 133.797 1.00 132.06 ? 74  C   C N1    1 
ATOM   10089 C  C2    . C   C 2 74  ? 146.337 157.569 134.207 1.00 133.73 ? 74  C   C C2    1 
ATOM   10090 O  O2    . C   C 2 74  ? 147.289 156.786 134.081 1.00 131.18 ? 74  C   C O2    1 
ATOM   10091 N  N3    . C   C 2 74  ? 145.144 157.182 134.713 1.00 133.61 ? 74  C   C N3    1 
ATOM   10092 C  C4    . C   C 2 74  ? 144.144 158.063 134.830 1.00 132.51 ? 74  C   C C4    1 
ATOM   10093 N  N4    . C   C 2 74  ? 143.000 157.631 135.336 1.00 135.74 ? 74  C   C N4    1 
ATOM   10094 C  C5    . C   C 2 74  ? 144.298 159.418 134.427 1.00 133.25 ? 74  C   C C5    1 
ATOM   10095 C  C6    . C   C 2 74  ? 145.483 159.789 133.922 1.00 131.12 ? 74  C   C C6    1 
ATOM   10096 P  P     . C   C 2 75  ? 147.724 159.983 128.516 1.00 131.40 ? 75  C   C P     1 
ATOM   10097 O  OP1   . C   C 2 75  ? 148.540 160.350 127.296 1.00 134.08 ? 75  C   C OP1   1 
ATOM   10098 O  OP2   . C   C 2 75  ? 146.250 160.302 128.384 1.00 128.39 ? 75  C   C OP2   1 
ATOM   10099 O  "O5'" . C   C 2 75  ? 147.847 158.389 128.715 1.00 130.75 ? 75  C   C "O5'" 1 
ATOM   10100 C  "C5'" . C   C 2 75  ? 147.251 157.515 127.730 1.00 133.57 ? 75  C   C "C5'" 1 
ATOM   10101 C  "C4'" . C   C 2 75  ? 146.876 156.212 128.388 1.00 131.28 ? 75  C   C "C4'" 1 
ATOM   10102 O  "O4'" . C   C 2 75  ? 146.662 156.439 129.806 1.00 133.67 ? 75  C   C "O4'" 1 
ATOM   10103 C  "C3'" . C   C 2 75  ? 145.595 155.545 127.865 1.00 128.53 ? 75  C   C "C3'" 1 
ATOM   10104 O  "O3'" . C   C 2 75  ? 145.913 154.555 126.895 1.00 130.76 ? 75  C   C "O3'" 1 
ATOM   10105 C  "C2'" . C   C 2 75  ? 144.979 154.910 129.115 1.00 124.19 ? 75  C   C "C2'" 1 
ATOM   10106 O  "O2'" . C   C 2 75  ? 145.470 153.613 129.372 1.00 128.22 ? 75  C   C "O2'" 1 
ATOM   10107 C  "C1'" . C   C 2 75  ? 145.458 155.841 130.233 1.00 129.56 ? 75  C   C "C1'" 1 
ATOM   10108 N  N1    . C   C 2 75  ? 144.481 156.913 130.565 1.00 127.04 ? 75  C   C N1    1 
ATOM   10109 C  C2    . C   C 2 75  ? 143.382 156.581 131.359 1.00 129.08 ? 75  C   C C2    1 
ATOM   10110 O  O2    . C   C 2 75  ? 143.245 155.405 131.725 1.00 136.44 ? 75  C   C O2    1 
ATOM   10111 N  N3    . C   C 2 75  ? 142.481 157.544 131.667 1.00 124.95 ? 75  C   C N3    1 
ATOM   10112 C  C4    . C   C 2 75  ? 142.663 158.800 131.246 1.00 126.93 ? 75  C   C C4    1 
ATOM   10113 N  N4    . C   C 2 75  ? 141.760 159.705 131.591 1.00 127.34 ? 75  C   C N4    1 
ATOM   10114 C  C5    . C   C 2 75  ? 143.789 159.161 130.459 1.00 127.83 ? 75  C   C C5    1 
ATOM   10115 C  C6    . C   C 2 75  ? 144.669 158.198 130.153 1.00 125.94 ? 75  C   C C6    1 
ATOM   10116 P  P     A A   C 2 76  ? 145.678 154.820 125.328 0.44 120.65 ? 76  A   C P     1 
ATOM   10117 P  P     B A   C 2 76  ? 145.644 154.773 125.324 0.56 118.44 ? 76  A   C P     1 
ATOM   10118 O  OP1   A A   C 2 76  ? 146.677 155.809 124.770 0.44 127.37 ? 76  A   C OP1   1 
ATOM   10119 O  OP1   B A   C 2 76  ? 144.188 154.520 124.991 0.56 125.12 ? 76  A   C OP1   1 
ATOM   10120 O  OP2   A A   C 2 76  ? 144.231 155.171 125.047 0.44 123.32 ? 76  A   C OP2   1 
ATOM   10121 O  OP2   B A   C 2 76  ? 146.611 153.958 124.489 0.56 124.93 ? 76  A   C OP2   1 
ATOM   10122 O  "O5'" A A   C 2 76  ? 145.999 153.379 124.671 0.44 124.58 ? 76  A   C "O5'" 1 
ATOM   10123 O  "O5'" B A   C 2 76  ? 145.935 156.328 124.994 0.56 123.04 ? 76  A   C "O5'" 1 
ATOM   10124 C  "C5'" A A   C 2 76  ? 145.861 153.209 123.236 0.44 126.55 ? 76  A   C "C5'" 1 
ATOM   10125 C  "C5'" B A   C 2 76  ? 144.890 157.308 125.228 0.56 125.43 ? 76  A   C "C5'" 1 
ATOM   10126 C  "C4'" A A   C 2 76  ? 144.417 152.954 122.884 0.44 126.01 ? 76  A   C "C4'" 1 
ATOM   10127 C  "C4'" B A   C 2 76  ? 145.429 158.693 124.972 0.56 127.36 ? 76  A   C "C4'" 1 
ATOM   10128 O  "O4'" A A   C 2 76  ? 144.309 152.750 121.455 0.44 126.57 ? 76  A   C "O4'" 1 
ATOM   10129 O  "O4'" B A   C 2 76  ? 146.085 158.720 123.678 0.56 128.29 ? 76  A   C "O4'" 1 
ATOM   10130 C  "C3'" A A   C 2 76  ? 143.777 151.707 123.504 0.44 127.78 ? 76  A   C "C3'" 1 
ATOM   10131 C  "C3'" B A   C 2 76  ? 144.385 159.816 124.930 0.56 127.08 ? 76  A   C "C3'" 1 
ATOM   10132 O  "O3'" A A   C 2 76  ? 142.377 151.888 123.666 0.44 129.84 ? 76  A   C "O3'" 1 
ATOM   10133 O  "O3'" B A   C 2 76  ? 144.906 161.023 125.470 0.56 127.85 ? 76  A   C "O3'" 1 
ATOM   10134 C  "C2'" A A   C 2 76  ? 144.090 150.613 122.478 0.44 128.77 ? 76  A   C "C2'" 1 
ATOM   10135 C  "C2'" B A   C 2 76  ? 144.103 159.946 123.432 0.56 124.99 ? 76  A   C "C2'" 1 
ATOM   10136 O  "O2'" A A   C 2 76  ? 143.084 149.625 122.418 0.44 132.28 ? 76  A   C "O2'" 1 
ATOM   10137 O  "O2'" B A   C 2 76  ? 143.601 161.214 123.070 0.56 126.53 ? 76  A   C "O2'" 1 
ATOM   10138 C  "C1'" A A   C 2 76  ? 144.182 151.377 121.157 0.44 127.56 ? 76  A   C "C1'" 1 
ATOM   10139 C  "C1'" B A   C 2 76  ? 145.495 159.703 122.860 0.56 125.13 ? 76  A   C "C1'" 1 
ATOM   10140 N  N9    A A   C 2 76  ? 145.322 150.975 120.341 0.44 128.46 ? 76  A   C N9    1 
ATOM   10141 N  N9    B A   C 2 76  ? 145.491 159.222 121.484 0.56 123.00 ? 76  A   C N9    1 
ATOM   10142 C  C8    A A   C 2 76  ? 145.892 149.727 120.305 0.44 127.14 ? 76  A   C C8    1 
ATOM   10143 C  C8    B A   C 2 76  ? 144.523 158.457 120.885 0.56 125.91 ? 76  A   C C8    1 
ATOM   10144 N  N7    A A   C 2 76  ? 146.906 149.642 119.483 0.44 127.11 ? 76  A   C N7    1 
ATOM   10145 N  N7    B A   C 2 76  ? 144.788 158.171 119.635 0.56 129.79 ? 76  A   C N7    1 
ATOM   10146 C  C5    A A   C 2 76  ? 147.016 150.913 118.940 0.44 127.47 ? 76  A   C C5    1 
ATOM   10147 C  C5    B A   C 2 76  ? 146.009 158.783 119.394 0.56 127.87 ? 76  A   C C5    1 
ATOM   10148 C  C6    A A   C 2 76  ? 147.905 151.464 117.997 0.44 128.56 ? 76  A   C C6    1 
ATOM   10149 C  C6    B A   C 2 76  ? 146.823 158.850 118.248 0.56 129.88 ? 76  A   C C6    1 
ATOM   10150 N  N6    A A   C 2 76  ? 148.886 150.778 117.417 0.44 128.29 ? 76  A   C N6    1 
ATOM   10151 N  N6    B A   C 2 76  ? 146.520 158.270 117.091 0.56 131.12 ? 76  A   C N6    1 
ATOM   10152 N  N1    A A   C 2 76  ? 147.742 152.767 117.672 0.44 130.05 ? 76  A   C N1    1 
ATOM   10153 N  N1    B A   C 2 76  ? 147.982 159.543 118.344 0.56 130.63 ? 76  A   C N1    1 
ATOM   10154 C  C2    A A   C 2 76  ? 146.753 153.452 118.259 0.44 130.77 ? 76  A   C C2    1 
ATOM   10155 C  C2    B A   C 2 76  ? 148.283 160.123 119.513 0.56 128.36 ? 76  A   C C2    1 
ATOM   10156 N  N3    A A   C 2 76  ? 145.861 153.040 119.154 0.44 129.83 ? 76  A   C N3    1 
ATOM   10157 N  N3    B A   C 2 76  ? 147.595 160.130 120.651 0.56 126.58 ? 76  A   C N3    1 
ATOM   10158 C  C4    A A   C 2 76  ? 146.044 151.745 119.459 0.44 127.95 ? 76  A   C C4    1 
ATOM   10159 C  C4    B A   C 2 76  ? 146.455 159.432 120.528 0.56 124.90 ? 76  A   C C4    1 
ATOM   10160 N  N     . MET D 3 1   ? 132.582 106.142 145.417 1.00 128.49 ? 1   MET D N     1 
ATOM   10161 C  CA    . MET D 3 1   ? 133.846 106.857 145.258 1.00 129.18 ? 1   MET D CA    1 
ATOM   10162 C  C     . MET D 3 1   ? 133.737 108.139 144.415 1.00 125.86 ? 1   MET D C     1 
ATOM   10163 O  O     . MET D 3 1   ? 134.432 109.110 144.710 1.00 127.70 ? 1   MET D O     1 
ATOM   10164 C  CB    . MET D 3 1   ? 134.912 105.935 144.655 1.00 128.47 ? 1   MET D CB    1 
ATOM   10165 C  CG    . MET D 3 1   ? 136.331 106.476 144.773 1.00 129.85 ? 1   MET D CG    1 
ATOM   10166 S  SD    . MET D 3 1   ? 136.864 107.427 143.335 1.00 131.16 ? 1   MET D SD    1 
ATOM   10167 C  CE    . MET D 3 1   ? 137.975 106.264 142.551 1.00 129.90 ? 1   MET D CE    1 
ATOM   10168 N  N     . PRO D 3 2   ? 132.892 108.150 143.351 1.00 112.77 ? 2   PRO D N     1 
ATOM   10169 C  CA    . PRO D 3 2   ? 132.661 109.413 142.638 1.00 112.98 ? 2   PRO D CA    1 
ATOM   10170 C  C     . PRO D 3 2   ? 132.291 110.544 143.580 1.00 110.31 ? 2   PRO D C     1 
ATOM   10171 O  O     . PRO D 3 2   ? 131.492 110.358 144.502 1.00 113.99 ? 2   PRO D O     1 
ATOM   10172 C  CB    . PRO D 3 2   ? 131.505 109.068 141.695 1.00 115.91 ? 2   PRO D CB    1 
ATOM   10173 C  CG    . PRO D 3 2   ? 131.748 107.654 141.351 1.00 114.82 ? 2   PRO D CG    1 
ATOM   10174 C  CD    . PRO D 3 2   ? 132.383 107.007 142.567 1.00 117.06 ? 2   PRO D CD    1 
ATOM   10175 N  N     . MET D 3 3   ? 132.879 111.715 143.359 1.00 80.24  ? 3   MET D N     1 
ATOM   10176 C  CA    . MET D 3 3   ? 132.731 112.816 144.296 1.00 80.81  ? 3   MET D CA    1 
ATOM   10177 C  C     . MET D 3 3   ? 131.280 113.272 144.373 1.00 80.00  ? 3   MET D C     1 
ATOM   10178 O  O     . MET D 3 3   ? 130.514 113.150 143.414 1.00 83.60  ? 3   MET D O     1 
ATOM   10179 C  CB    . MET D 3 3   ? 133.632 113.978 143.888 1.00 86.49  ? 3   MET D CB    1 
ATOM   10180 C  CG    . MET D 3 3   ? 135.108 113.642 143.939 1.00 84.50  ? 3   MET D CG    1 
ATOM   10181 S  SD    . MET D 3 3   ? 135.850 114.069 145.520 1.00 72.16  ? 3   MET D SD    1 
ATOM   10182 C  CE    . MET D 3 3   ? 134.904 115.523 145.953 1.00 89.98  ? 3   MET D CE    1 
ATOM   10183 N  N     . TYR D 3 4   ? 130.904 113.787 145.544 1.00 68.77  ? 4   TYR D N     1 
ATOM   10184 C  CA    . TYR D 3 4   ? 129.552 114.271 145.787 1.00 60.58  ? 4   TYR D CA    1 
ATOM   10185 C  C     . TYR D 3 4   ? 129.165 115.311 144.745 1.00 71.52  ? 4   TYR D C     1 
ATOM   10186 O  O     . TYR D 3 4   ? 130.022 116.042 144.241 1.00 83.34  ? 4   TYR D O     1 
ATOM   10187 C  CB    . TYR D 3 4   ? 129.433 114.849 147.198 1.00 68.93  ? 4   TYR D CB    1 
ATOM   10188 C  CG    . TYR D 3 4   ? 130.263 116.088 147.433 1.00 67.93  ? 4   TYR D CG    1 
ATOM   10189 C  CD1   . TYR D 3 4   ? 131.628 116.004 147.649 1.00 68.38  ? 4   TYR D CD1   1 
ATOM   10190 C  CD2   . TYR D 3 4   ? 129.677 117.342 147.445 1.00 77.14  ? 4   TYR D CD2   1 
ATOM   10191 C  CE1   . TYR D 3 4   ? 132.384 117.131 147.863 1.00 66.34  ? 4   TYR D CE1   1 
ATOM   10192 C  CE2   . TYR D 3 4   ? 130.426 118.475 147.661 1.00 74.60  ? 4   TYR D CE2   1 
ATOM   10193 C  CZ    . TYR D 3 4   ? 131.779 118.364 147.868 1.00 70.01  ? 4   TYR D CZ    1 
ATOM   10194 O  OH    . TYR D 3 4   ? 132.531 119.495 148.082 1.00 74.54  ? 4   TYR D OH    1 
ATOM   10195 N  N     . GLN D 3 5   ? 127.881 115.380 144.415 1.00 87.81  ? 5   GLN D N     1 
ATOM   10196 C  CA    . GLN D 3 5   ? 127.406 116.198 143.309 1.00 83.71  ? 5   GLN D CA    1 
ATOM   10197 C  C     . GLN D 3 5   ? 127.260 117.646 143.758 1.00 84.98  ? 5   GLN D C     1 
ATOM   10198 O  O     . GLN D 3 5   ? 126.628 117.924 144.782 1.00 90.45  ? 5   GLN D O     1 
ATOM   10199 C  CB    . GLN D 3 5   ? 126.077 115.662 142.783 1.00 76.88  ? 5   GLN D CB    1 
ATOM   10200 C  CG    . GLN D 3 5   ? 126.209 114.361 142.018 1.00 83.14  ? 5   GLN D CG    1 
ATOM   10201 C  CD    . GLN D 3 5   ? 125.198 114.240 140.899 1.00 79.05  ? 5   GLN D CD    1 
ATOM   10202 O  OE1   . GLN D 3 5   ? 124.380 115.134 140.687 1.00 83.75  ? 5   GLN D OE1   1 
ATOM   10203 N  NE2   . GLN D 3 5   ? 125.248 113.129 140.176 1.00 82.48  ? 5   GLN D NE2   1 
ATOM   10204 N  N     . VAL D 3 6   ? 127.846 118.557 142.994 1.00 78.03  ? 6   VAL D N     1 
ATOM   10205 C  CA    . VAL D 3 6   ? 127.705 119.990 143.212 1.00 74.26  ? 6   VAL D CA    1 
ATOM   10206 C  C     . VAL D 3 6   ? 126.991 120.583 142.006 1.00 81.95  ? 6   VAL D C     1 
ATOM   10207 O  O     . VAL D 3 6   ? 127.346 120.313 140.854 1.00 81.45  ? 6   VAL D O     1 
ATOM   10208 C  CB    . VAL D 3 6   ? 129.074 120.663 143.446 1.00 75.79  ? 6   VAL D CB    1 
ATOM   10209 C  CG1   . VAL D 3 6   ? 129.047 122.114 143.002 1.00 86.18  ? 6   VAL D CG1   1 
ATOM   10210 C  CG2   . VAL D 3 6   ? 129.471 120.561 144.905 1.00 76.48  ? 6   VAL D CG2   1 
ATOM   10211 N  N     . LYS D 3 7   ? 125.960 121.383 142.271 1.00 98.73  ? 7   LYS D N     1 
ATOM   10212 C  CA    . LYS D 3 7   ? 125.183 121.932 141.166 1.00 94.87  ? 7   LYS D CA    1 
ATOM   10213 C  C     . LYS D 3 7   ? 126.004 122.953 140.384 1.00 91.10  ? 7   LYS D C     1 
ATOM   10214 O  O     . LYS D 3 7   ? 126.740 123.744 140.980 1.00 87.63  ? 7   LYS D O     1 
ATOM   10215 C  CB    . LYS D 3 7   ? 123.908 122.592 141.679 1.00 101.50 ? 7   LYS D CB    1 
ATOM   10216 C  CG    . LYS D 3 7   ? 122.858 121.613 142.180 1.00 100.50 ? 7   LYS D CG    1 
ATOM   10217 C  CD    . LYS D 3 7   ? 122.875 120.313 141.388 1.00 91.24  ? 7   LYS D CD    1 
ATOM   10218 C  CE    . LYS D 3 7   ? 122.992 119.110 142.310 1.00 93.50  ? 7   LYS D CE    1 
ATOM   10219 N  NZ    . LYS D 3 7   ? 123.079 117.834 141.553 1.00 99.17  ? 7   LYS D NZ    1 
ATOM   10220 N  N     . PRO D 3 8   ? 125.896 122.942 139.056 1.00 97.50  ? 8   PRO D N     1 
ATOM   10221 C  CA    . PRO D 3 8   ? 126.626 123.927 138.248 1.00 100.93 ? 8   PRO D CA    1 
ATOM   10222 C  C     . PRO D 3 8   ? 126.194 125.345 138.585 1.00 103.47 ? 8   PRO D C     1 
ATOM   10223 O  O     . PRO D 3 8   ? 125.014 125.618 138.810 1.00 110.36 ? 8   PRO D O     1 
ATOM   10224 C  CB    . PRO D 3 8   ? 126.253 123.549 136.810 1.00 100.19 ? 8   PRO D CB    1 
ATOM   10225 C  CG    . PRO D 3 8   ? 125.847 122.117 136.893 1.00 100.12 ? 8   PRO D CG    1 
ATOM   10226 C  CD    . PRO D 3 8   ? 125.166 121.978 138.218 1.00 101.22 ? 8   PRO D CD    1 
ATOM   10227 N  N     . TYR D 3 9   ? 127.169 126.254 138.616 1.00 104.95 ? 9   TYR D N     1 
ATOM   10228 C  CA    . TYR D 3 9   ? 126.869 127.646 138.930 1.00 103.25 ? 9   TYR D CA    1 
ATOM   10229 C  C     . TYR D 3 9   ? 126.090 128.310 137.804 1.00 99.83  ? 9   TYR D C     1 
ATOM   10230 O  O     . TYR D 3 9   ? 125.188 129.117 138.055 1.00 106.23 ? 9   TYR D O     1 
ATOM   10231 C  CB    . TYR D 3 9   ? 128.161 128.408 139.209 1.00 104.19 ? 9   TYR D CB    1 
ATOM   10232 C  CG    . TYR D 3 9   ? 128.761 128.108 140.561 1.00 103.07 ? 9   TYR D CG    1 
ATOM   10233 C  CD1   . TYR D 3 9   ? 128.184 128.602 141.722 1.00 104.82 ? 9   TYR D CD1   1 
ATOM   10234 C  CD2   . TYR D 3 9   ? 129.899 127.326 140.677 1.00 106.39 ? 9   TYR D CD2   1 
ATOM   10235 C  CE1   . TYR D 3 9   ? 128.728 128.329 142.959 1.00 103.53 ? 9   TYR D CE1   1 
ATOM   10236 C  CE2   . TYR D 3 9   ? 130.450 127.047 141.911 1.00 106.70 ? 9   TYR D CE2   1 
ATOM   10237 C  CZ    . TYR D 3 9   ? 129.861 127.552 143.048 1.00 105.04 ? 9   TYR D CZ    1 
ATOM   10238 O  OH    . TYR D 3 9   ? 130.405 127.278 144.281 1.00 115.31 ? 9   TYR D OH    1 
ATOM   10239 N  N     . HIS D 3 10  ? 126.423 127.982 136.557 1.00 94.25  ? 10  HIS D N     1 
ATOM   10240 C  CA    . HIS D 3 10  ? 125.838 128.637 135.390 1.00 100.33 ? 10  HIS D CA    1 
ATOM   10241 C  C     . HIS D 3 10  ? 124.548 127.933 134.968 1.00 102.49 ? 10  HIS D C     1 
ATOM   10242 O  O     . HIS D 3 10  ? 124.407 127.420 133.859 1.00 105.93 ? 10  HIS D O     1 
ATOM   10243 C  CB    . HIS D 3 10  ? 126.858 128.671 134.262 1.00 103.75 ? 10  HIS D CB    1 
ATOM   10244 C  CG    . HIS D 3 10  ? 128.171 129.264 134.666 1.00 104.42 ? 10  HIS D CG    1 
ATOM   10245 N  ND1   . HIS D 3 10  ? 129.365 128.589 134.534 1.00 105.79 ? 10  HIS D ND1   1 
ATOM   10246 C  CD2   . HIS D 3 10  ? 128.476 130.465 135.210 1.00 108.37 ? 10  HIS D CD2   1 
ATOM   10247 C  CE1   . HIS D 3 10  ? 130.349 129.351 134.976 1.00 102.99 ? 10  HIS D CE1   1 
ATOM   10248 N  NE2   . HIS D 3 10  ? 129.837 130.495 135.391 1.00 107.03 ? 10  HIS D NE2   1 
ATOM   10249 N  N     . GLY D 3 11  ? 123.595 127.910 135.895 1.00 127.62 ? 11  GLY D N     1 
ATOM   10250 C  CA    . GLY D 3 11  ? 122.311 127.289 135.642 1.00 129.13 ? 11  GLY D CA    1 
ATOM   10251 C  C     . GLY D 3 11  ? 122.376 125.777 135.659 1.00 124.65 ? 11  GLY D C     1 
ATOM   10252 O  O     . GLY D 3 11  ? 121.825 125.134 136.557 1.00 122.31 ? 11  GLY D O     1 
ATOM   10253 N  N     . GLY D 3 12  ? 123.055 125.199 134.671 1.00 148.86 ? 12  GLY D N     1 
ATOM   10254 C  CA    . GLY D 3 12  ? 123.201 123.763 134.575 1.00 150.34 ? 12  GLY D CA    1 
ATOM   10255 C  C     . GLY D 3 12  ? 122.120 123.053 133.794 1.00 151.21 ? 12  GLY D C     1 
ATOM   10256 O  O     . GLY D 3 12  ? 122.257 121.850 133.536 1.00 151.94 ? 12  GLY D O     1 
ATOM   10257 N  N     . GLY D 3 13  ? 121.054 123.748 133.408 1.00 163.59 ? 13  GLY D N     1 
ATOM   10258 C  CA    . GLY D 3 13  ? 120.011 123.154 132.596 1.00 163.67 ? 13  GLY D CA    1 
ATOM   10259 C  C     . GLY D 3 13  ? 119.952 123.781 131.221 1.00 162.65 ? 13  GLY D C     1 
ATOM   10260 O  O     . GLY D 3 13  ? 118.866 124.017 130.681 1.00 162.47 ? 13  GLY D O     1 
ATOM   10261 N  N     . ALA D 3 14  ? 121.127 124.046 130.645 1.00 161.04 ? 14  ALA D N     1 
ATOM   10262 C  CA    . ALA D 3 14  ? 121.284 124.796 129.404 1.00 161.43 ? 14  ALA D CA    1 
ATOM   10263 C  C     . ALA D 3 14  ? 120.505 126.106 129.466 1.00 162.70 ? 14  ALA D C     1 
ATOM   10264 O  O     . ALA D 3 14  ? 119.651 126.358 128.606 1.00 162.78 ? 14  ALA D O     1 
ATOM   10265 C  CB    . ALA D 3 14  ? 120.832 123.962 128.204 1.00 162.40 ? 14  ALA D CB    1 
ATOM   10266 N  N     . PRO D 3 15  ? 120.761 126.964 130.459 1.00 154.03 ? 15  PRO D N     1 
ATOM   10267 C  CA    . PRO D 3 15  ? 119.978 128.203 130.553 1.00 153.73 ? 15  PRO D CA    1 
ATOM   10268 C  C     . PRO D 3 15  ? 120.387 129.243 129.529 1.00 154.68 ? 15  PRO D C     1 
ATOM   10269 O  O     . PRO D 3 15  ? 119.628 130.189 129.287 1.00 155.08 ? 15  PRO D O     1 
ATOM   10270 C  CB    . PRO D 3 15  ? 120.264 128.677 131.982 1.00 153.65 ? 15  PRO D CB    1 
ATOM   10271 C  CG    . PRO D 3 15  ? 121.672 128.246 132.203 1.00 151.99 ? 15  PRO D CG    1 
ATOM   10272 C  CD    . PRO D 3 15  ? 121.820 126.919 131.486 1.00 152.83 ? 15  PRO D CD    1 
ATOM   10273 N  N     . LEU D 3 16  ? 121.560 129.095 128.918 1.00 144.63 ? 16  LEU D N     1 
ATOM   10274 C  CA    . LEU D 3 16  ? 122.074 130.108 128.008 1.00 142.34 ? 16  LEU D CA    1 
ATOM   10275 C  C     . LEU D 3 16  ? 121.529 129.914 126.599 1.00 139.68 ? 16  LEU D C     1 
ATOM   10276 O  O     . LEU D 3 16  ? 122.295 129.865 125.632 1.00 141.55 ? 16  LEU D O     1 
ATOM   10277 C  CB    . LEU D 3 16  ? 123.604 130.081 127.996 1.00 141.57 ? 16  LEU D CB    1 
ATOM   10278 C  CG    . LEU D 3 16  ? 124.277 130.343 129.345 1.00 142.10 ? 16  LEU D CG    1 
ATOM   10279 C  CD1   . LEU D 3 16  ? 125.451 129.399 129.560 1.00 142.52 ? 16  LEU D CD1   1 
ATOM   10280 C  CD2   . LEU D 3 16  ? 124.720 131.787 129.456 1.00 145.61 ? 16  LEU D CD2   1 
ATOM   10281 N  N     . ARG D 3 17  ? 120.206 129.805 126.473 1.00 142.12 ? 17  ARG D N     1 
ATOM   10282 C  CA    . ARG D 3 17  ? 119.575 129.817 125.161 1.00 145.43 ? 17  ARG D CA    1 
ATOM   10283 C  C     . ARG D 3 17  ? 119.479 131.264 124.697 1.00 145.21 ? 17  ARG D C     1 
ATOM   10284 O  O     . ARG D 3 17  ? 118.398 131.860 124.702 1.00 145.36 ? 17  ARG D O     1 
ATOM   10285 C  CB    . ARG D 3 17  ? 118.197 129.156 125.207 1.00 146.31 ? 17  ARG D CB    1 
ATOM   10286 C  CG    . ARG D 3 17  ? 117.559 128.928 123.842 1.00 146.17 ? 17  ARG D CG    1 
ATOM   10287 C  CD    . ARG D 3 17  ? 118.284 127.845 123.053 1.00 146.43 ? 17  ARG D CD    1 
ATOM   10288 N  NE    . ARG D 3 17  ? 119.313 128.389 122.174 1.00 145.42 ? 17  ARG D NE    1 
ATOM   10289 C  CZ    . ARG D 3 17  ? 120.595 128.053 122.222 1.00 145.25 ? 17  ARG D CZ    1 
ATOM   10290 N  NH1   . ARG D 3 17  ? 121.047 127.173 123.100 1.00 146.60 ? 17  ARG D NH1   1 
ATOM   10291 N  NH2   . ARG D 3 17  ? 121.444 128.613 121.365 1.00 144.40 ? 17  ARG D NH2   1 
ATOM   10292 N  N     . VAL D 3 18  ? 120.621 131.833 124.308 1.00 133.81 ? 18  VAL D N     1 
ATOM   10293 C  CA    . VAL D 3 18  ? 120.703 133.266 124.066 1.00 133.63 ? 18  VAL D CA    1 
ATOM   10294 C  C     . VAL D 3 18  ? 119.876 133.649 122.848 1.00 135.13 ? 18  VAL D C     1 
ATOM   10295 O  O     . VAL D 3 18  ? 119.861 132.945 121.829 1.00 137.09 ? 18  VAL D O     1 
ATOM   10296 C  CB    . VAL D 3 18  ? 122.171 133.689 123.894 1.00 135.84 ? 18  VAL D CB    1 
ATOM   10297 C  CG1   . VAL D 3 18  ? 122.863 133.749 125.243 1.00 138.18 ? 18  VAL D CG1   1 
ATOM   10298 C  CG2   . VAL D 3 18  ? 122.892 132.723 122.970 1.00 138.87 ? 18  VAL D CG2   1 
ATOM   10299 N  N     . GLU D 3 19  ? 119.171 134.773 122.956 1.00 140.05 ? 19  GLU D N     1 
ATOM   10300 C  CA    . GLU D 3 19  ? 118.474 135.358 121.817 1.00 137.98 ? 19  GLU D CA    1 
ATOM   10301 C  C     . GLU D 3 19  ? 119.493 136.126 120.986 1.00 136.29 ? 19  GLU D C     1 
ATOM   10302 O  O     . GLU D 3 19  ? 120.069 137.113 121.454 1.00 137.15 ? 19  GLU D O     1 
ATOM   10303 C  CB    . GLU D 3 19  ? 117.341 136.265 122.287 1.00 138.36 ? 19  GLU D CB    1 
ATOM   10304 C  CG    . GLU D 3 19  ? 116.136 135.516 122.832 1.00 137.86 ? 19  GLU D CG    1 
ATOM   10305 C  CD    . GLU D 3 19  ? 114.976 136.437 123.156 1.00 137.18 ? 19  GLU D CD    1 
ATOM   10306 O  OE1   . GLU D 3 19  ? 115.142 137.669 123.039 1.00 136.17 ? 19  GLU D OE1   1 
ATOM   10307 O  OE2   . GLU D 3 19  ? 113.898 135.928 123.526 1.00 138.57 ? 19  GLU D OE2   1 
ATOM   10308 N  N     . LEU D 3 20  ? 119.724 135.674 119.767 1.00 125.00 ? 20  LEU D N     1 
ATOM   10309 C  CA    . LEU D 3 20  ? 120.779 136.214 118.931 1.00 126.46 ? 20  LEU D CA    1 
ATOM   10310 C  C     . LEU D 3 20  ? 120.219 137.204 117.921 1.00 124.63 ? 20  LEU D C     1 
ATOM   10311 O  O     . LEU D 3 20  ? 119.053 137.115 117.525 1.00 127.62 ? 20  LEU D O     1 
ATOM   10312 C  CB    . LEU D 3 20  ? 121.503 135.078 118.201 1.00 126.63 ? 20  LEU D CB    1 
ATOM   10313 C  CG    . LEU D 3 20  ? 122.049 133.977 119.112 1.00 127.87 ? 20  LEU D CG    1 
ATOM   10314 C  CD1   . LEU D 3 20  ? 122.164 132.660 118.360 1.00 128.37 ? 20  LEU D CD1   1 
ATOM   10315 C  CD2   . LEU D 3 20  ? 123.385 134.381 119.716 1.00 132.55 ? 20  LEU D CD2   1 
ATOM   10316 N  N     . PRO D 3 21  ? 121.031 138.181 117.486 1.00 118.56 ? 21  PRO D N     1 
ATOM   10317 C  CA    . PRO D 3 21  ? 120.628 139.166 116.476 1.00 120.20 ? 21  PRO D CA    1 
ATOM   10318 C  C     . PRO D 3 21  ? 120.240 138.527 115.145 1.00 116.26 ? 21  PRO D C     1 
ATOM   10319 O  O     . PRO D 3 21  ? 119.840 139.246 114.229 1.00 117.07 ? 21  PRO D O     1 
ATOM   10320 C  CB    . PRO D 3 21  ? 121.884 140.027 116.318 1.00 120.09 ? 21  PRO D CB    1 
ATOM   10321 C  CG    . PRO D 3 21  ? 122.559 139.921 117.640 1.00 121.50 ? 21  PRO D CG    1 
ATOM   10322 C  CD    . PRO D 3 21  ? 122.364 138.488 118.032 1.00 123.32 ? 21  PRO D CD    1 
ATOM   10323 N  N     . MET E 3 1   ? 119.871 144.154 108.310 1.00 128.49 ? 1   MET E N     1 
ATOM   10324 C  CA    . MET E 3 1   ? 120.975 144.389 109.281 1.00 129.18 ? 1   MET E CA    1 
ATOM   10325 C  C     . MET E 3 1   ? 121.344 143.081 110.010 1.00 125.86 ? 1   MET E C     1 
ATOM   10326 O  O     . MET E 3 1   ? 122.559 142.837 110.171 1.00 127.70 ? 1   MET E O     1 
ATOM   10327 C  CB    . MET E 3 1   ? 120.610 145.478 110.297 1.00 128.47 ? 1   MET E CB    1 
ATOM   10328 C  CG    . MET E 3 1   ? 121.729 145.805 111.267 1.00 129.85 ? 1   MET E CG    1 
ATOM   10329 S  SD    . MET E 3 1   ? 121.856 147.569 111.623 1.00 131.16 ? 1   MET E SD    1 
ATOM   10330 C  CE    . MET E 3 1   ? 122.102 148.225 109.968 1.00 129.90 ? 1   MET E CE    1 
ATOM   10331 N  N     . PRO E 3 2   ? 120.397 142.229 110.465 1.00 112.77 ? 2   PRO E N     1 
ATOM   10332 C  CA    . PRO E 3 2   ? 120.781 140.975 111.091 1.00 112.98 ? 2   PRO E CA    1 
ATOM   10333 C  C     . PRO E 3 2   ? 121.890 140.360 110.267 1.00 110.31 ? 2   PRO E C     1 
ATOM   10334 O  O     . PRO E 3 2   ? 121.705 140.135 109.057 1.00 113.99 ? 2   PRO E O     1 
ATOM   10335 C  CB    . PRO E 3 2   ? 119.493 140.156 111.042 1.00 115.91 ? 2   PRO E CB    1 
ATOM   10336 C  CG    . PRO E 3 2   ? 118.405 141.197 111.154 1.00 114.82 ? 2   PRO E CG    1 
ATOM   10337 C  CD    . PRO E 3 2   ? 118.953 142.430 110.452 1.00 117.06 ? 2   PRO E CD    1 
ATOM   10338 N  N     . MET E 3 3   ? 123.025 140.088 110.907 1.00 80.24  ? 3   MET E N     1 
ATOM   10339 C  CA    . MET E 3 3   ? 124.190 139.520 110.186 1.00 80.81  ? 3   MET E CA    1 
ATOM   10340 C  C     . MET E 3 3   ? 123.837 138.125 109.661 1.00 80.00  ? 3   MET E C     1 
ATOM   10341 O  O     . MET E 3 3   ? 123.021 137.439 110.304 1.00 83.60  ? 3   MET E O     1 
ATOM   10342 C  CB    . MET E 3 3   ? 125.397 139.425 111.122 1.00 86.49  ? 3   MET E CB    1 
ATOM   10343 C  CG    . MET E 3 3   ? 126.046 140.759 111.417 1.00 84.50  ? 3   MET E CG    1 
ATOM   10344 S  SD    . MET E 3 3   ? 126.838 141.427 109.942 1.00 72.16  ? 3   MET E SD    1 
ATOM   10345 C  CE    . MET E 3 3   ? 127.989 140.100 109.560 1.00 89.98  ? 3   MET E CE    1 
ATOM   10346 N  N     . TYR E 3 4   ? 124.433 137.732 108.535 1.00 68.77  ? 4   TYR E N     1 
ATOM   10347 C  CA    . TYR E 3 4   ? 124.203 136.373 107.981 1.00 60.58  ? 4   TYR E CA    1 
ATOM   10348 C  C     . TYR E 3 4   ? 124.530 135.356 109.061 1.00 71.52  ? 4   TYR E C     1 
ATOM   10349 O  O     . TYR E 3 4   ? 125.345 135.652 109.956 1.00 83.34  ? 4   TYR E O     1 
ATOM   10350 C  CB    . TYR E 3 4   ? 125.031 136.193 106.706 1.00 68.93  ? 4   TYR E CB    1 
ATOM   10351 C  CG    . TYR E 3 4   ? 126.544 136.260 106.853 1.00 67.93  ? 4   TYR E CG    1 
ATOM   10352 C  CD1   . TYR E 3 4   ? 127.210 137.479 106.875 1.00 68.38  ? 4   TYR E CD1   1 
ATOM   10353 C  CD2   . TYR E 3 4   ? 127.309 135.103 106.920 1.00 77.14  ? 4   TYR E CD2   1 
ATOM   10354 C  CE1   . TYR E 3 4   ? 128.587 137.546 106.994 1.00 66.34  ? 4   TYR E CE1   1 
ATOM   10355 C  CE2   . TYR E 3 4   ? 128.687 135.157 107.034 1.00 74.60  ? 4   TYR E CE2   1 
ATOM   10356 C  CZ    . TYR E 3 4   ? 129.327 136.381 107.073 1.00 70.01  ? 4   TYR E CZ    1 
ATOM   10357 O  OH    . TYR E 3 4   ? 130.685 136.439 107.188 1.00 74.54  ? 4   TYR E OH    1 
ATOM   10358 N  N     . GLN E 3 5   ? 123.932 134.170 108.976 1.00 87.81  ? 5   GLN E N     1 
ATOM   10359 C  CA    . GLN E 3 5   ? 124.127 133.168 110.033 1.00 83.71  ? 5   GLN E CA    1 
ATOM   10360 C  C     . GLN E 3 5   ? 125.254 132.223 109.678 1.00 84.98  ? 5   GLN E C     1 
ATOM   10361 O  O     . GLN E 3 5   ? 125.158 131.587 108.631 1.00 90.45  ? 5   GLN E O     1 
ATOM   10362 C  CB    . GLN E 3 5   ? 122.925 132.246 110.077 1.00 76.88  ? 5   GLN E CB    1 
ATOM   10363 C  CG    . GLN E 3 5   ? 121.678 132.862 110.696 1.00 83.14  ? 5   GLN E CG    1 
ATOM   10364 C  CD    . GLN E 3 5   ? 120.595 131.832 110.918 1.00 79.05  ? 5   GLN E CD    1 
ATOM   10365 O  OE1   . GLN E 3 5   ? 120.764 130.649 110.606 1.00 83.75  ? 5   GLN E OE1   1 
ATOM   10366 N  NE2   . GLN E 3 5   ? 119.470 132.275 111.460 1.00 82.48  ? 5   GLN E NE2   1 
ATOM   10367 N  N     . VAL E 3 6   ? 126.264 132.121 110.531 1.00 78.03  ? 6   VAL E N     1 
ATOM   10368 C  CA    . VAL E 3 6   ? 127.339 131.119 110.333 1.00 74.26  ? 6   VAL E CA    1 
ATOM   10369 C  C     . VAL E 3 6   ? 127.052 130.048 111.386 1.00 81.95  ? 6   VAL E C     1 
ATOM   10370 O  O     . VAL E 3 6   ? 126.471 130.405 112.413 1.00 81.45  ? 6   VAL E O     1 
ATOM   10371 C  CB    . VAL E 3 6   ? 128.725 131.745 110.508 1.00 75.79  ? 6   VAL E CB    1 
ATOM   10372 C  CG1   . VAL E 3 6   ? 129.834 130.774 110.139 1.00 86.18  ? 6   VAL E CG1   1 
ATOM   10373 C  CG2   . VAL E 3 6   ? 128.872 133.023 109.704 1.00 76.48  ? 6   VAL E CG2   1 
ATOM   10374 N  N     . LYS E 3 7   ? 127.391 128.789 111.138 1.00 98.73  ? 7   LYS E N     1 
ATOM   10375 C  CA    . LYS E 3 7   ? 127.020 127.714 112.086 1.00 94.87  ? 7   LYS E CA    1 
ATOM   10376 C  C     . LYS E 3 7   ? 128.058 127.579 113.195 1.00 91.10  ? 7   LYS E C     1 
ATOM   10377 O  O     . LYS E 3 7   ? 129.248 127.616 112.878 1.00 87.63  ? 7   LYS E O     1 
ATOM   10378 C  CB    . LYS E 3 7   ? 126.907 126.430 111.275 1.00 101.50 ? 7   LYS E CB    1 
ATOM   10379 C  CG    . LYS E 3 7   ? 125.802 126.512 110.236 1.00 100.50 ? 7   LYS E CG    1 
ATOM   10380 C  CD    . LYS E 3 7   ? 124.542 127.145 110.816 1.00 91.24  ? 7   LYS E CD    1 
ATOM   10381 C  CE    . LYS E 3 7   ? 123.794 127.984 109.827 1.00 93.50  ? 7   LYS E CE    1 
ATOM   10382 N  NZ    . LYS E 3 7   ? 122.806 128.847 110.480 1.00 99.17  ? 7   LYS E NZ    1 
ATOM   10383 N  N     . PRO E 3 8   ? 127.679 127.396 114.480 1.00 97.50  ? 8   PRO E N     1 
ATOM   10384 C  CA    . PRO E 3 8   ? 128.658 127.354 115.549 1.00 100.93 ? 8   PRO E CA    1 
ATOM   10385 C  C     . PRO E 3 8   ? 129.636 126.231 115.328 1.00 103.47 ? 8   PRO E C     1 
ATOM   10386 O  O     . PRO E 3 8   ? 129.217 125.141 114.928 1.00 110.36 ? 8   PRO E O     1 
ATOM   10387 C  CB    . PRO E 3 8   ? 127.827 127.153 116.794 1.00 100.19 ? 8   PRO E CB    1 
ATOM   10388 C  CG    . PRO E 3 8   ? 126.487 127.710 116.421 1.00 100.12 ? 8   PRO E CG    1 
ATOM   10389 C  CD    . PRO E 3 8   ? 126.321 127.247 114.991 1.00 101.22 ? 8   PRO E CD    1 
ATOM   10390 N  N     . TYR E 3 9   ? 130.918 126.493 115.570 1.00 104.95 ? 9   TYR E N     1 
ATOM   10391 C  CA    . TYR E 3 9   ? 131.973 125.487 115.317 1.00 103.25 ? 9   TYR E CA    1 
ATOM   10392 C  C     . TYR E 3 9   ? 131.905 124.455 116.362 1.00 99.83  ? 9   TYR E C     1 
ATOM   10393 O  O     . TYR E 3 9   ? 131.942 123.265 116.051 1.00 106.23 ? 9   TYR E O     1 
ATOM   10394 C  CB    . TYR E 3 9   ? 133.349 126.117 115.530 1.00 104.19 ? 9   TYR E CB    1 
ATOM   10395 C  CG    . TYR E 3 9   ? 133.761 127.256 114.617 1.00 103.07 ? 9   TYR E CG    1 
ATOM   10396 C  CD1   . TYR E 3 9   ? 134.343 127.011 113.381 1.00 104.82 ? 9   TYR E CD1   1 
ATOM   10397 C  CD2   . TYR E 3 9   ? 133.619 128.575 115.017 1.00 106.39 ? 9   TYR E CD2   1 
ATOM   10398 C  CE1   . TYR E 3 9   ? 134.742 128.045 112.554 1.00 103.53 ? 9   TYR E CE1   1 
ATOM   10399 C  CE2   . TYR E 3 9   ? 134.013 129.618 114.200 1.00 106.70 ? 9   TYR E CE2   1 
ATOM   10400 C  CZ    . TYR E 3 9   ? 134.579 129.353 112.967 1.00 105.04 ? 9   TYR E CZ    1 
ATOM   10401 O  OH    . TYR E 3 9   ? 134.962 130.385 112.167 1.00 115.31 ? 9   TYR E OH    1 
ATOM   10402 N  N     . HIS E 3 10  ? 131.785 124.900 117.602 1.00 94.25  ? 10  HIS E N     1 
ATOM   10403 C  CA    . HIS E 3 10  ? 131.847 123.953 118.736 1.00 100.33 ? 10  HIS E CA    1 
ATOM   10404 C  C     . HIS E 3 10  ? 130.498 123.255 118.800 1.00 102.49 ? 10  HIS E C     1 
ATOM   10405 O  O     . HIS E 3 10  ? 129.858 123.233 119.863 1.00 105.93 ? 10  HIS E O     1 
ATOM   10406 C  CB    . HIS E 3 10  ? 132.268 124.693 120.010 1.00 103.75 ? 10  HIS E CB    1 
ATOM   10407 C  CG    . HIS E 3 10  ? 133.392 125.652 119.859 1.00 104.42 ? 10  HIS E CG    1 
ATOM   10408 N  ND1   . HIS E 3 10  ? 133.185 127.012 119.832 1.00 105.79 ? 10  HIS E ND1   1 
ATOM   10409 C  CD2   . HIS E 3 10  ? 134.708 125.476 119.789 1.00 108.37 ? 10  HIS E CD2   1 
ATOM   10410 C  CE1   . HIS E 3 10  ? 134.349 127.629 119.714 1.00 102.99 ? 10  HIS E CE1   1 
ATOM   10411 N  NE2   . HIS E 3 10  ? 135.285 126.712 119.682 1.00 107.03 ? 10  HIS E NE2   1 
ATOM   10412 N  N     . GLY E 3 11  ? 130.079 122.705 117.666 1.00 127.62 ? 11  GLY E N     1 
ATOM   10413 C  CA    . GLY E 3 11  ? 128.762 122.059 117.604 1.00 129.13 ? 11  GLY E CA    1 
ATOM   10414 C  C     . GLY E 3 11  ? 127.712 122.956 118.222 1.00 124.65 ? 11  GLY E C     1 
ATOM   10415 O  O     . GLY E 3 11  ? 127.928 124.181 118.288 1.00 122.31 ? 11  GLY E O     1 
ATOM   10416 N  N     . GLY E 3 12  ? 126.603 122.377 118.671 1.00 148.86 ? 12  GLY E N     1 
ATOM   10417 C  CA    . GLY E 3 12  ? 125.499 123.189 119.212 1.00 150.34 ? 12  GLY E CA    1 
ATOM   10418 C  C     . GLY E 3 12  ? 124.491 122.312 119.922 1.00 151.21 ? 12  GLY E C     1 
ATOM   10419 O  O     . GLY E 3 12  ? 124.643 121.070 119.853 1.00 151.94 ? 12  GLY E O     1 
ATOM   10420 N  N     . GLY E 3 13  ? 123.514 122.916 120.608 1.00 163.59 ? 13  GLY E N     1 
ATOM   10421 C  CA    . GLY E 3 13  ? 122.568 122.113 121.407 1.00 163.67 ? 13  GLY E CA    1 
ATOM   10422 C  C     . GLY E 3 13  ? 123.345 121.171 122.300 1.00 162.65 ? 13  GLY E C     1 
ATOM   10423 O  O     . GLY E 3 13  ? 123.020 119.966 122.308 1.00 162.47 ? 13  GLY E O     1 
ATOM   10424 N  N     . ALA E 3 14  ? 124.353 121.695 123.004 1.00 161.04 ? 14  ALA E N     1 
ATOM   10425 C  CA    . ALA E 3 14  ? 125.230 120.839 123.835 1.00 161.43 ? 14  ALA E CA    1 
ATOM   10426 C  C     . ALA E 3 14  ? 125.681 119.639 123.000 1.00 162.70 ? 14  ALA E C     1 
ATOM   10427 O  O     . ALA E 3 14  ? 125.265 118.498 123.293 1.00 162.78 ? 14  ALA E O     1 
ATOM   10428 C  CB    . ALA E 3 14  ? 124.513 120.413 125.094 1.00 162.40 ? 14  ALA E CB    1 
ATOM   10429 N  N     . PRO E 3 15  ? 126.613 119.787 122.024 1.00 154.03 ? 15  PRO E N     1 
ATOM   10430 C  CA    . PRO E 3 15  ? 127.087 118.633 121.273 1.00 153.73 ? 15  PRO E CA    1 
ATOM   10431 C  C     . PRO E 3 15  ? 127.930 117.731 122.162 1.00 154.68 ? 15  PRO E C     1 
ATOM   10432 O  O     . PRO E 3 15  ? 127.764 116.496 122.108 1.00 155.08 ? 15  PRO E O     1 
ATOM   10433 C  CB    . PRO E 3 15  ? 127.907 119.266 120.143 1.00 153.65 ? 15  PRO E CB    1 
ATOM   10434 C  CG    . PRO E 3 15  ? 128.454 120.524 120.768 1.00 151.99 ? 15  PRO E CG    1 
ATOM   10435 C  CD    . PRO E 3 15  ? 127.311 121.022 121.634 1.00 152.83 ? 15  PRO E CD    1 
ATOM   10436 N  N     . LEU E 3 16  ? 128.813 118.330 122.965 1.00 144.63 ? 16  LEU E N     1 
ATOM   10437 C  CA    . LEU E 3 16  ? 129.683 117.545 123.879 1.00 142.34 ? 16  LEU E CA    1 
ATOM   10438 C  C     . LEU E 3 16  ? 128.867 117.121 125.109 1.00 139.68 ? 16  LEU E C     1 
ATOM   10439 O  O     . LEU E 3 16  ? 128.359 118.013 125.823 1.00 141.55 ? 16  LEU E O     1 
ATOM   10440 C  CB    . LEU E 3 16  ? 130.911 118.369 124.266 1.00 141.57 ? 16  LEU E CB    1 
ATOM   10441 C  CG    . LEU E 3 16  ? 130.640 119.670 125.031 1.00 142.10 ? 16  LEU E CG    1 
ATOM   10442 C  CD1   . LEU E 3 16  ? 130.381 119.434 126.509 1.00 142.52 ? 16  LEU E CD1   1 
ATOM   10443 C  CD2   . LEU E 3 16  ? 131.766 120.668 124.836 1.00 145.61 ? 16  LEU E CD2   1 
ATOM   10444 N  N     . ARG E 3 17  ? 128.681 115.810 125.290 1.00 142.12 ? 17  ARG E N     1 
ATOM   10445 C  CA    . ARG E 3 17  ? 127.986 115.305 126.502 1.00 145.43 ? 17  ARG E CA    1 
ATOM   10446 C  C     . ARG E 3 17  ? 129.086 114.908 127.495 1.00 145.21 ? 17  ARG E C     1 
ATOM   10447 O  O     . ARG E 3 17  ? 129.336 113.692 127.658 1.00 145.36 ? 17  ARG E O     1 
ATOM   10448 C  CB    . ARG E 3 17  ? 127.042 114.145 126.168 1.00 146.31 ? 17  ARG E CB    1 
ATOM   10449 C  CG    . ARG E 3 17  ? 126.201 113.704 127.357 1.00 146.17 ? 17  ARG E CG    1 
ATOM   10450 C  CD    . ARG E 3 17  ? 125.594 114.900 128.073 1.00 146.43 ? 17  ARG E CD    1 
ATOM   10451 N  NE    . ARG E 3 17  ? 124.939 114.526 129.331 1.00 145.42 ? 17  ARG E NE    1 
ATOM   10452 C  CZ    . ARG E 3 17  ? 124.360 115.386 130.158 1.00 145.25 ? 17  ARG E CZ    1 
ATOM   10453 N  NH1   . ARG E 3 17  ? 124.381 116.679 129.888 1.00 146.60 ? 17  ARG E NH1   1 
ATOM   10454 N  NH2   . ARG E 3 17  ? 123.764 114.951 131.254 1.00 144.40 ? 17  ARG E NH2   1 
ATOM   10455 N  N     . VAL E 3 18  ? 129.729 115.900 128.112 1.00 133.81 ? 18  VAL E N     1 
ATOM   10456 C  CA    . VAL E 3 18  ? 130.874 115.615 129.026 1.00 133.63 ? 18  VAL E CA    1 
ATOM   10457 C  C     . VAL E 3 18  ? 130.469 114.528 130.035 1.00 135.13 ? 18  VAL E C     1 
ATOM   10458 O  O     . VAL E 3 18  ? 129.404 114.671 130.676 1.00 137.09 ? 18  VAL E O     1 
ATOM   10459 C  CB    . VAL E 3 18  ? 131.314 116.931 129.694 1.00 135.84 ? 18  VAL E CB    1 
ATOM   10460 C  CG1   . VAL E 3 18  ? 131.922 117.879 128.667 1.00 138.18 ? 18  VAL E CG1   1 
ATOM   10461 C  CG2   . VAL E 3 18  ? 130.164 117.618 130.422 1.00 138.87 ? 18  VAL E CG2   1 
ATOM   10462 N  N     . GLU E 3 19  ? 131.284 113.476 130.155 1.00 140.05 ? 19  GLU E N     1 
ATOM   10463 C  CA    . GLU E 3 19  ? 130.949 112.345 131.060 1.00 137.98 ? 19  GLU E CA    1 
ATOM   10464 C  C     . GLU E 3 19  ? 131.486 112.640 132.468 1.00 136.29 ? 19  GLU E C     1 
ATOM   10465 O  O     . GLU E 3 19  ? 132.634 112.247 132.760 1.00 137.15 ? 19  GLU E O     1 
ATOM   10466 C  CB    . GLU E 3 19  ? 131.548 111.051 130.512 1.00 138.36 ? 19  GLU E CB    1 
ATOM   10467 C  CG    . GLU E 3 19  ? 131.118 110.750 129.080 1.00 137.86 ? 19  GLU E CG    1 
ATOM   10468 C  CD    . GLU E 3 19  ? 131.853 109.581 128.450 1.00 137.18 ? 19  GLU E CD    1 
ATOM   10469 O  OE1   . GLU E 3 19  ? 132.726 108.998 129.126 1.00 136.17 ? 19  GLU E OE1   1 
ATOM   10470 O  OE2   . GLU E 3 19  ? 131.551 109.254 127.283 1.00 138.57 ? 19  GLU E OE2   1 
ATOM   10471 N  N     . LEU E 3 20  ? 130.678 113.298 133.303 1.00 125.00 ? 20  LEU E N     1 
ATOM   10472 C  CA    . LEU E 3 20  ? 131.109 113.626 134.686 1.00 126.46 ? 20  LEU E CA    1 
ATOM   10473 C  C     . LEU E 3 20  ? 131.361 112.317 135.450 1.00 124.63 ? 20  LEU E C     1 
ATOM   10474 O  O     . LEU E 3 20  ? 130.432 111.484 135.524 1.00 127.62 ? 20  LEU E O     1 
ATOM   10475 C  CB    . LEU E 3 20  ? 130.031 114.476 135.351 1.00 126.63 ? 20  LEU E CB    1 
ATOM   10476 C  CG    . LEU E 3 20  ? 129.524 115.660 134.523 1.00 127.87 ? 20  LEU E CG    1 
ATOM   10477 C  CD1   . LEU E 3 20  ? 128.436 116.406 135.270 1.00 128.37 ? 20  LEU E CD1   1 
ATOM   10478 C  CD2   . LEU E 3 20  ? 130.666 116.590 134.149 1.00 132.55 ? 20  LEU E CD2   1 
ATOM   10479 N  N     . PRO E 3 21  ? 132.569 112.100 136.014 1.00 118.56 ? 21  PRO E N     1 
ATOM   10480 C  CA    . PRO E 3 21  ? 132.879 110.854 136.701 1.00 120.20 ? 21  PRO E CA    1 
ATOM   10481 C  C     . PRO E 3 21  ? 132.161 110.766 138.042 1.00 116.26 ? 21  PRO E C     1 
ATOM   10482 O  O     . PRO E 3 21  ? 132.653 111.405 138.994 1.00 117.07 ? 21  PRO E O     1 
ATOM   10483 C  CB    . PRO E 3 21  ? 134.409 110.911 136.859 1.00 120.09 ? 21  PRO E CB    1 
ATOM   10484 C  CG    . PRO E 3 21  ? 134.836 112.050 135.958 1.00 121.50 ? 21  PRO E CG    1 
ATOM   10485 C  CD    . PRO E 3 21  ? 133.680 113.029 135.994 1.00 123.32 ? 21  PRO E CD    1 
HETATM 10486 N  N     . LYS F 4 .   ? 140.871 147.926 121.904 1.00 12688. ? 601 LYS A N     1 
HETATM 10487 C  CA    . LYS F 4 .   ? 139.703 148.301 121.115 1.00 12721. ? 601 LYS A CA    1 
HETATM 10488 C  C     . LYS F 4 .   ? 138.847 149.319 121.856 1.00 12723. ? 601 LYS A C     1 
HETATM 10489 O  O     . LYS F 4 .   ? 138.773 150.485 121.470 1.00 12724. ? 601 LYS A O     1 
HETATM 10490 C  CB    . LYS F 4 .   ? 138.872 147.066 120.774 1.00 12749. ? 601 LYS A CB    1 
HETATM 10491 C  CG    . LYS F 4 .   ? 137.508 147.382 120.193 1.00 12744. ? 601 LYS A CG    1 
HETATM 10492 C  CD    . LYS F 4 .   ? 137.627 148.070 118.854 1.00 12759. ? 601 LYS A CD    1 
HETATM 10493 C  CE    . LYS F 4 .   ? 138.294 147.167 117.839 1.00 12757. ? 601 LYS A CE    1 
HETATM 10494 N  NZ    . LYS F 4 .   ? 139.136 147.922 116.871 1.00 12755. ? 601 LYS A NZ    1 
HETATM 10495 O  OXT   . LYS F 4 .   ? 138.214 149.000 122.861 1.00 12748. ? 601 LYS A OXT   1 
HETATM 10496 P  P     . AMP G 5 .   ? 140.211 149.981 125.213 1.00 12666. ? 602 AMP A P     1 
HETATM 10497 O  O1P   . AMP G 5 .   ? 141.290 150.775 125.904 1.00 12641. ? 602 AMP A O1P   1 
HETATM 10498 O  O2P   . AMP G 5 .   ? 139.026 150.832 124.839 1.00 12706. ? 602 AMP A O2P   1 
HETATM 10499 O  O3P   . AMP G 5 .   ? 140.746 149.165 124.069 1.00 12683. ? 602 AMP A O3P   1 
HETATM 10500 O  "O5'" . AMP G 5 .   ? 139.679 148.908 126.289 1.00 12750. ? 602 AMP A "O5'" 1 
HETATM 10501 C  "C5'" . AMP G 5 .   ? 138.364 148.322 126.130 1.00 12754. ? 602 AMP A "C5'" 1 
HETATM 10502 C  "C4'" . AMP G 5 .   ? 137.580 148.567 127.394 1.00 12751. ? 602 AMP A "C4'" 1 
HETATM 10503 O  "O4'" . AMP G 5 .   ? 138.391 148.199 128.533 1.00 12762. ? 602 AMP A "O4'" 1 
HETATM 10504 C  "C3'" . AMP G 5 .   ? 137.188 150.019 127.661 1.00 12748. ? 602 AMP A "C3'" 1 
HETATM 10505 O  "O3'" . AMP G 5 .   ? 135.930 150.310 127.076 1.00 12761. ? 602 AMP A "O3'" 1 
HETATM 10506 C  "C2'" . AMP G 5 .   ? 137.085 150.072 129.183 1.00 12751. ? 602 AMP A "C2'" 1 
HETATM 10507 O  "O2'" . AMP G 5 .   ? 135.790 149.717 129.601 1.00 12764. ? 602 AMP A "O2'" 1 
HETATM 10508 C  "C1'" . AMP G 5 .   ? 138.105 149.031 129.634 1.00 12751. ? 602 AMP A "C1'" 1 
HETATM 10509 N  N9    . AMP G 5 .   ? 139.353 149.603 130.125 1.00 12742. ? 602 AMP A N9    1 
HETATM 10510 C  C8    . AMP G 5 .   ? 140.190 150.457 129.458 1.00 12750. ? 602 AMP A C8    1 
HETATM 10511 N  N7    . AMP G 5 .   ? 141.234 150.811 130.161 1.00 12743. ? 602 AMP A N7    1 
HETATM 10512 C  C5    . AMP G 5 .   ? 141.070 150.157 131.370 1.00 12739. ? 602 AMP A C5    1 
HETATM 10513 C  C6    . AMP G 5 .   ? 141.845 150.129 132.542 1.00 12744. ? 602 AMP A C6    1 
HETATM 10514 N  N6    . AMP G 5 .   ? 142.984 150.797 132.687 1.00 12749. ? 602 AMP A N6    1 
HETATM 10515 N  N1    . AMP G 5 .   ? 141.397 149.375 133.569 1.00 12738. ? 602 AMP A N1    1 
HETATM 10516 C  C2    . AMP G 5 .   ? 140.253 148.704 133.415 1.00 12739. ? 602 AMP A C2    1 
HETATM 10517 N  N3    . AMP G 5 .   ? 139.445 148.654 132.364 1.00 12734. ? 602 AMP A N3    1 
HETATM 10518 C  C4    . AMP G 5 .   ? 139.912 149.414 131.363 1.00 12737. ? 602 AMP A C4    1 
HETATM 10519 N  N     . LYS H 4 .   ? 150.974 124.104 138.842 1.00 104.34 ? 601 LYS B N     1 
HETATM 10520 C  CA    . LYS H 4 .   ? 151.639 122.827 138.616 1.00 102.06 ? 601 LYS B CA    1 
HETATM 10521 C  C     . LYS H 4 .   ? 152.513 122.869 137.371 1.00 101.33 ? 601 LYS B C     1 
HETATM 10522 O  O     . LYS H 4 .   ? 152.360 123.740 136.516 1.00 97.44  ? 601 LYS B O     1 
HETATM 10523 C  CB    . LYS H 4 .   ? 150.612 121.703 138.494 1.00 97.46  ? 601 LYS B CB    1 
HETATM 10524 C  CG    . LYS H 4 .   ? 149.500 121.780 139.515 1.00 94.71  ? 601 LYS B CG    1 
HETATM 10525 C  CD    . LYS H 4 .   ? 149.315 120.451 140.209 1.00 99.63  ? 601 LYS B CD    1 
HETATM 10526 C  CE    . LYS H 4 .   ? 148.377 120.582 141.387 1.00 105.95 ? 601 LYS B CE    1 
HETATM 10527 N  NZ    . LYS H 4 .   ? 148.730 121.732 142.256 1.00 111.17 ? 601 LYS B NZ    1 
HETATM 10528 O  OXT   . LYS H 4 .   ? 153.393 122.029 137.193 1.00 106.81 ? 601 LYS B OXT   1 
HETATM 10529 P  P     . AMP I 5 .   ? 155.076 121.802 134.207 1.00 119.00 ? 602 AMP B P     1 
HETATM 10530 O  O1P   . AMP I 5 .   ? 154.717 120.358 134.486 1.00 129.00 ? 602 AMP B O1P   1 
HETATM 10531 O  O2P   . AMP I 5 .   ? 155.977 122.387 135.274 1.00 127.50 ? 602 AMP B O2P   1 
HETATM 10532 O  O3P   . AMP I 5 .   ? 153.868 122.673 133.924 1.00 131.78 ? 602 AMP B O3P   1 
HETATM 10533 O  "O5'" . AMP I 5 .   ? 155.960 121.783 132.857 1.00 134.09 ? 602 AMP B "O5'" 1 
HETATM 10534 C  "C5'" . AMP I 5 .   ? 155.630 120.836 131.809 1.00 136.53 ? 602 AMP B "C5'" 1 
HETATM 10535 C  "C4'" . AMP I 5 .   ? 154.242 121.119 131.293 1.00 133.48 ? 602 AMP B "C4'" 1 
HETATM 10536 O  "O4'" . AMP I 5 .   ? 154.131 122.532 130.989 1.00 132.54 ? 602 AMP B "O4'" 1 
HETATM 10537 C  "C3'" . AMP I 5 .   ? 153.861 120.418 129.986 1.00 130.78 ? 602 AMP B "C3'" 1 
HETATM 10538 O  "O3'" . AMP I 5 .   ? 152.451 120.301 129.852 1.00 130.76 ? 602 AMP B "O3'" 1 
HETATM 10539 C  "C2'" . AMP I 5 .   ? 154.452 121.375 128.948 1.00 131.00 ? 602 AMP B "C2'" 1 
HETATM 10540 O  "O2'" . AMP I 5 .   ? 153.798 121.332 127.699 1.00 131.88 ? 602 AMP B "O2'" 1 
HETATM 10541 C  "C1'" . AMP I 5 .   ? 154.257 122.739 129.602 1.00 132.65 ? 602 AMP B "C1'" 1 
HETATM 10542 N  N9    . AMP I 5 .   ? 155.372 123.646 129.372 1.00 139.58 ? 602 AMP B N9    1 
HETATM 10543 C  C8    . AMP I 5 .   ? 156.419 123.898 130.220 1.00 136.82 ? 602 AMP B C8    1 
HETATM 10544 N  N7    . AMP I 5 .   ? 157.285 124.750 129.735 1.00 137.88 ? 602 AMP B N7    1 
HETATM 10545 C  C5    . AMP I 5 .   ? 156.785 125.070 128.483 1.00 136.99 ? 602 AMP B C5    1 
HETATM 10546 C  C6    . AMP I 5 .   ? 157.251 125.928 127.472 1.00 137.38 ? 602 AMP B C6    1 
HETATM 10547 N  N6    . AMP I 5 .   ? 158.367 126.641 127.571 1.00 137.86 ? 602 AMP B N6    1 
HETATM 10548 N  N1    . AMP I 5 .   ? 156.510 126.020 126.343 1.00 139.89 ? 602 AMP B N1    1 
HETATM 10549 C  C2    . AMP I 5 .   ? 155.392 125.292 126.250 1.00 139.96 ? 602 AMP B C2    1 
HETATM 10550 N  N3    . AMP I 5 .   ? 154.859 124.455 127.133 1.00 138.83 ? 602 AMP B N3    1 
HETATM 10551 C  C4    . AMP I 5 .   ? 155.611 124.387 128.242 1.00 137.58 ? 602 AMP B C4    1 
HETATM 10552 NA NA    . NA  J 6 .   ? 141.166 143.888 180.036 1.00 91.45  ? 101 NA  C NA    1 
HETATM 10553 NA NA    . NA  K 6 .   ? 141.952 147.231 163.785 1.00 50.03  ? 102 NA  C NA    1 
HETATM 10554 MG MG    . MG  L 7 .   ? 135.292 128.353 177.553 1.00 78.72  ? 103 MG  C MG    1 
HETATM 10555 MG MG    . MG  M 7 .   ? 150.489 159.823 155.112 1.00 80.57  ? 104 MG  C MG    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 14  ? 328.9722 328.9722 328.9722 0.0000 0.0000 0.0000 14  SER A N   
2    C CA  . SER A 14  ? 328.9972 328.9972 328.9972 0.0000 0.0000 0.0000 14  SER A CA  
3    C C   . SER A 14  ? 329.1004 329.1004 329.1004 0.0000 0.0000 0.0000 14  SER A C   
4    O O   . SER A 14  ? 329.0930 329.0930 329.0930 0.0000 0.0000 0.0000 14  SER A O   
5    C CB  . SER A 14  ? 328.9877 328.9877 328.9877 0.0000 0.0000 0.0000 14  SER A CB  
6    O OG  . SER A 14  ? 328.9423 328.9423 328.9423 0.0000 0.0000 0.0000 14  SER A OG  
7    N N   . GLU A 15  ? 335.3520 335.3520 335.3520 0.0000 0.0000 0.0000 15  GLU A N   
8    C CA  . GLU A 15  ? 335.3518 335.3518 335.3518 0.0000 0.0000 0.0000 15  GLU A CA  
9    C C   . GLU A 15  ? 335.2255 335.2255 335.2255 0.0000 0.0000 0.0000 15  GLU A C   
10   O O   . GLU A 15  ? 335.0907 335.0907 335.0907 0.0000 0.0000 0.0000 15  GLU A O   
11   C CB  . GLU A 15  ? 335.1697 335.1697 335.1697 0.0000 0.0000 0.0000 15  GLU A CB  
12   C CG  . GLU A 15  ? 335.3150 335.3150 335.3150 0.0000 0.0000 0.0000 15  GLU A CG  
13   C CD  . GLU A 15  ? 335.3252 335.3252 335.3252 0.0000 0.0000 0.0000 15  GLU A CD  
14   O OE1 . GLU A 15  ? 335.2093 335.2093 335.2093 0.0000 0.0000 0.0000 15  GLU A OE1 
15   O OE2 . GLU A 15  ? 335.4568 335.4568 335.4568 0.0000 0.0000 0.0000 15  GLU A OE2 
16   N N   . PRO A 16  ? 337.1041 337.1041 337.1041 0.0000 0.0000 0.0000 16  PRO A N   
17   C CA  . PRO A 16  ? 337.0540 337.0540 337.0540 0.0000 0.0000 0.0000 16  PRO A CA  
18   C C   . PRO A 16  ? 336.6417 336.6417 336.6417 0.0000 0.0000 0.0000 16  PRO A C   
19   O O   . PRO A 16  ? 336.7055 336.7055 336.7055 0.0000 0.0000 0.0000 16  PRO A O   
20   C CB  . PRO A 16  ? 337.1763 337.1763 337.1763 0.0000 0.0000 0.0000 16  PRO A CB  
21   C CG  . PRO A 16  ? 337.2429 337.2429 337.2429 0.0000 0.0000 0.0000 16  PRO A CG  
22   C CD  . PRO A 16  ? 337.2500 337.2500 337.2500 0.0000 0.0000 0.0000 16  PRO A CD  
23   N N   . LYS A 17  ? 314.9710 314.9710 314.9710 0.0000 0.0000 0.0000 17  LYS A N   
24   C CA  . LYS A 17  ? 314.6626 314.6626 314.6626 0.0000 0.0000 0.0000 17  LYS A CA  
25   C C   . LYS A 17  ? 313.9793 313.9793 313.9793 0.0000 0.0000 0.0000 17  LYS A C   
26   O O   . LYS A 17  ? 313.6217 313.6217 313.6217 0.0000 0.0000 0.0000 17  LYS A O   
27   C CB  . LYS A 17  ? 314.5502 314.5502 314.5502 0.0000 0.0000 0.0000 17  LYS A CB  
28   C CG  . LYS A 17  ? 314.6615 314.6615 314.6615 0.0000 0.0000 0.0000 17  LYS A CG  
29   C CD  . LYS A 17  ? 314.6129 314.6129 314.6129 0.0000 0.0000 0.0000 17  LYS A CD  
30   C CE  . LYS A 17  ? 314.6536 314.6536 314.6536 0.0000 0.0000 0.0000 17  LYS A CE  
31   N NZ  . LYS A 17  ? 314.7562 314.7562 314.7562 0.0000 0.0000 0.0000 17  LYS A NZ  
32   N N   . LEU A 18  ? 299.9833 299.9833 299.9833 0.0000 0.0000 0.0000 18  LEU A N   
33   C CA  . LEU A 18  ? 299.4265 299.4265 299.4265 0.0000 0.0000 0.0000 18  LEU A CA  
34   C C   . LEU A 18  ? 298.7284 298.7284 298.7284 0.0000 0.0000 0.0000 18  LEU A C   
35   O O   . LEU A 18  ? 299.1648 299.1648 299.1648 0.0000 0.0000 0.0000 18  LEU A O   
36   C CB  . LEU A 18  ? 298.8368 298.8368 298.8368 0.0000 0.0000 0.0000 18  LEU A CB  
37   C CG  . LEU A 18  ? 299.2081 299.2081 299.2081 0.0000 0.0000 0.0000 18  LEU A CG  
38   C CD1 . LEU A 18  ? 299.4011 299.4011 299.4011 0.0000 0.0000 0.0000 18  LEU A CD1 
39   C CD2 . LEU A 18  ? 298.9408 298.9408 298.9408 0.0000 0.0000 0.0000 18  LEU A CD2 
40   N N   . SER A 19  ? 254.7261 254.7261 254.7261 0.0000 0.0000 0.0000 19  SER A N   
41   C CA  . SER A 19  ? 252.9720 252.9720 252.9720 0.0000 0.0000 0.0000 19  SER A CA  
42   C C   . SER A 19  ? 252.9018 252.9018 252.9018 0.0000 0.0000 0.0000 19  SER A C   
43   O O   . SER A 19  ? 253.4126 253.4126 253.4126 0.0000 0.0000 0.0000 19  SER A O   
44   C CB  . SER A 19  ? 250.7058 250.7058 250.7058 0.0000 0.0000 0.0000 19  SER A CB  
45   O OG  . SER A 19  ? 251.2915 251.2915 251.2915 0.0000 0.0000 0.0000 19  SER A OG  
46   N N   . LYS A 20  ? 248.7622 248.7622 248.7622 0.0000 0.0000 0.0000 20  LYS A N   
47   C CA  . LYS A 20  ? 249.0490 249.0490 249.0490 0.0000 0.0000 0.0000 20  LYS A CA  
48   C C   . LYS A 20  ? 249.4247 249.4247 249.4247 0.0000 0.0000 0.0000 20  LYS A C   
49   O O   . LYS A 20  ? 249.6480 249.6480 249.6480 0.0000 0.0000 0.0000 20  LYS A O   
50   C CB  . LYS A 20  ? 248.1448 248.1448 248.1448 0.0000 0.0000 0.0000 20  LYS A CB  
51   C CG  . LYS A 20  ? 248.7447 248.7447 248.7447 0.0000 0.0000 0.0000 20  LYS A CG  
52   C CD  . LYS A 20  ? 249.3276 249.3276 249.3276 0.0000 0.0000 0.0000 20  LYS A CD  
53   C CE  . LYS A 20  ? 249.2570 249.2570 249.2570 0.0000 0.0000 0.0000 20  LYS A CE  
54   N NZ  . LYS A 20  ? 249.7301 249.7301 249.7301 0.0000 0.0000 0.0000 20  LYS A NZ  
55   N N   . ASN A 21  ? 246.5328 246.5328 246.5328 0.0000 0.0000 0.0000 21  ASN A N   
56   C CA  . ASN A 21  ? 246.3929 246.3929 246.3929 0.0000 0.0000 0.0000 21  ASN A CA  
57   C C   . ASN A 21  ? 246.8661 246.8661 246.8661 0.0000 0.0000 0.0000 21  ASN A C   
58   O O   . ASN A 21  ? 246.8099 246.8099 246.8099 0.0000 0.0000 0.0000 21  ASN A O   
59   C CB  . ASN A 21  ? 245.7739 245.7739 245.7739 0.0000 0.0000 0.0000 21  ASN A CB  
60   C CG  . ASN A 21  ? 244.0423 244.0423 244.0423 0.0000 0.0000 0.0000 21  ASN A CG  
61   O OD1 . ASN A 21  ? 241.4618 241.4618 241.4618 0.0000 0.0000 0.0000 21  ASN A OD1 
62   N ND2 . ASN A 21  ? 244.0277 244.0277 244.0277 0.0000 0.0000 0.0000 21  ASN A ND2 
63   N N   . GLU A 22  ? 250.1378 250.1378 250.1378 0.0000 0.0000 0.0000 22  GLU A N   
64   C CA  . GLU A 22  ? 250.4442 250.4442 250.4442 0.0000 0.0000 0.0000 22  GLU A CA  
65   C C   . GLU A 22  ? 250.4972 250.4972 250.4972 0.0000 0.0000 0.0000 22  GLU A C   
66   O O   . GLU A 22  ? 250.5126 250.5126 250.5126 0.0000 0.0000 0.0000 22  GLU A O   
67   C CB  . GLU A 22  ? 250.5543 250.5543 250.5543 0.0000 0.0000 0.0000 22  GLU A CB  
68   C CG  . GLU A 22  ? 250.2201 250.2201 250.2201 0.0000 0.0000 0.0000 22  GLU A CG  
69   C CD  . GLU A 22  ? 249.1435 249.1435 249.1435 0.0000 0.0000 0.0000 22  GLU A CD  
70   O OE1 . GLU A 22  ? 248.5741 248.5741 248.5741 0.0000 0.0000 0.0000 22  GLU A OE1 
71   O OE2 . GLU A 22  ? 248.1815 248.1815 248.1815 0.0000 0.0000 0.0000 22  GLU A OE2 
72   N N   . LEU A 23  ? 250.3901 250.3901 250.3901 0.0000 0.0000 0.0000 23  LEU A N   
73   C CA  . LEU A 23  ? 250.3904 250.3904 250.3904 0.0000 0.0000 0.0000 23  LEU A CA  
74   C C   . LEU A 23  ? 250.3367 250.3367 250.3367 0.0000 0.0000 0.0000 23  LEU A C   
75   O O   . LEU A 23  ? 250.4002 250.4002 250.4002 0.0000 0.0000 0.0000 23  LEU A O   
76   C CB  . LEU A 23  ? 250.4556 250.4556 250.4556 0.0000 0.0000 0.0000 23  LEU A CB  
77   C CG  . LEU A 23  ? 250.6300 250.6300 250.6300 0.0000 0.0000 0.0000 23  LEU A CG  
78   C CD1 . LEU A 23  ? 250.6571 250.6571 250.6571 0.0000 0.0000 0.0000 23  LEU A CD1 
79   C CD2 . LEU A 23  ? 250.7099 250.7099 250.7099 0.0000 0.0000 0.0000 23  LEU A CD2 
80   N N   . LYS A 24  ? 246.0367 246.0367 246.0367 0.0000 0.0000 0.0000 24  LYS A N   
81   C CA  . LYS A 24  ? 245.9891 245.9891 245.9891 0.0000 0.0000 0.0000 24  LYS A CA  
82   C C   . LYS A 24  ? 246.0777 246.0777 246.0777 0.0000 0.0000 0.0000 24  LYS A C   
83   O O   . LYS A 24  ? 246.0827 246.0827 246.0827 0.0000 0.0000 0.0000 24  LYS A O   
84   C CB  . LYS A 24  ? 245.6738 245.6738 245.6738 0.0000 0.0000 0.0000 24  LYS A CB  
85   C CG  . LYS A 24  ? 245.1723 245.1723 245.1723 0.0000 0.0000 0.0000 24  LYS A CG  
86   C CD  . LYS A 24  ? 244.6057 244.6057 244.6057 0.0000 0.0000 0.0000 24  LYS A CD  
87   C CE  . LYS A 24  ? 243.2359 243.2359 243.2359 0.0000 0.0000 0.0000 24  LYS A CE  
88   N NZ  . LYS A 24  ? 241.2194 241.2194 241.2194 0.0000 0.0000 0.0000 24  LYS A NZ  
89   N N   . ARG A 25  ? 248.3404 248.3404 248.3404 0.0000 0.0000 0.0000 25  ARG A N   
90   C CA  . ARG A 25  ? 248.3937 248.3937 248.3937 0.0000 0.0000 0.0000 25  ARG A CA  
91   C C   . ARG A 25  ? 248.5333 248.5333 248.5333 0.0000 0.0000 0.0000 25  ARG A C   
92   O O   . ARG A 25  ? 248.4770 248.4770 248.4770 0.0000 0.0000 0.0000 25  ARG A O   
93   C CB  . ARG A 25  ? 248.3682 248.3682 248.3682 0.0000 0.0000 0.0000 25  ARG A CB  
94   C CG  . ARG A 25  ? 248.3142 248.3142 248.3142 0.0000 0.0000 0.0000 25  ARG A CG  
95   C CD  . ARG A 25  ? 248.3132 248.3132 248.3132 0.0000 0.0000 0.0000 25  ARG A CD  
96   N NE  . ARG A 25  ? 247.9605 247.9605 247.9605 0.0000 0.0000 0.0000 25  ARG A NE  
97   C CZ  . ARG A 25  ? 245.6086 245.6086 245.6086 0.0000 0.0000 0.0000 25  ARG A CZ  
98   N NH1 . ARG A 25  ? 244.1353 244.1353 244.1353 0.0000 0.0000 0.0000 25  ARG A NH1 
99   N NH2 . ARG A 25  ? 244.9664 244.9664 244.9664 0.0000 0.0000 0.0000 25  ARG A NH2 
100  N N   . ARG A 26  ? 256.1960 256.1960 256.1960 0.0000 0.0000 0.0000 26  ARG A N   
101  C CA  . ARG A 26  ? 256.3829 256.3829 256.3829 0.0000 0.0000 0.0000 26  ARG A CA  
102  C C   . ARG A 26  ? 256.3193 256.3193 256.3193 0.0000 0.0000 0.0000 26  ARG A C   
103  O O   . ARG A 26  ? 256.4112 256.4112 256.4112 0.0000 0.0000 0.0000 26  ARG A O   
104  C CB  . ARG A 26  ? 256.5093 256.5093 256.5093 0.0000 0.0000 0.0000 26  ARG A CB  
105  C CG  . ARG A 26  ? 256.5648 256.5648 256.5648 0.0000 0.0000 0.0000 26  ARG A CG  
106  C CD  . ARG A 26  ? 256.5741 256.5741 256.5741 0.0000 0.0000 0.0000 26  ARG A CD  
107  N NE  . ARG A 26  ? 256.5914 256.5914 256.5914 0.0000 0.0000 0.0000 26  ARG A NE  
108  C CZ  . ARG A 26  ? 256.5044 256.5044 256.5044 0.0000 0.0000 0.0000 26  ARG A CZ  
109  N NH1 . ARG A 26  ? 256.5109 256.5109 256.5109 0.0000 0.0000 0.0000 26  ARG A NH1 
110  N NH2 . ARG A 26  ? 256.4235 256.4235 256.4235 0.0000 0.0000 0.0000 26  ARG A NH2 
111  N N   . LEU A 27  ? 251.6970 251.6970 251.6970 0.0000 0.0000 0.0000 27  LEU A N   
112  C CA  . LEU A 27  ? 251.6925 251.6925 251.6925 0.0000 0.0000 0.0000 27  LEU A CA  
113  C C   . LEU A 27  ? 251.6657 251.6657 251.6657 0.0000 0.0000 0.0000 27  LEU A C   
114  O O   . LEU A 27  ? 251.6505 251.6505 251.6505 0.0000 0.0000 0.0000 27  LEU A O   
115  C CB  . LEU A 27  ? 251.6806 251.6806 251.6806 0.0000 0.0000 0.0000 27  LEU A CB  
116  C CG  . LEU A 27  ? 251.6627 251.6627 251.6627 0.0000 0.0000 0.0000 27  LEU A CG  
117  C CD1 . LEU A 27  ? 251.7020 251.7020 251.7020 0.0000 0.0000 0.0000 27  LEU A CD1 
118  C CD2 . LEU A 27  ? 251.6776 251.6776 251.6776 0.0000 0.0000 0.0000 27  LEU A CD2 
119  N N   . LYS A 28  ? 251.0531 251.0531 251.0531 0.0000 0.0000 0.0000 28  LYS A N   
120  C CA  . LYS A 28  ? 251.0517 251.0517 251.0517 0.0000 0.0000 0.0000 28  LYS A CA  
121  C C   . LYS A 28  ? 251.0753 251.0753 251.0753 0.0000 0.0000 0.0000 28  LYS A C   
122  O O   . LYS A 28  ? 251.0687 251.0687 251.0687 0.0000 0.0000 0.0000 28  LYS A O   
123  C CB  . LYS A 28  ? 251.0207 251.0207 251.0207 0.0000 0.0000 0.0000 28  LYS A CB  
124  C CG  . LYS A 28  ? 251.0442 251.0442 251.0442 0.0000 0.0000 0.0000 28  LYS A CG  
125  C CD  . LYS A 28  ? 251.0436 251.0436 251.0436 0.0000 0.0000 0.0000 28  LYS A CD  
126  C CE  . LYS A 28  ? 251.0594 251.0594 251.0594 0.0000 0.0000 0.0000 28  LYS A CE  
127  N NZ  . LYS A 28  ? 250.8198 250.8198 250.8198 0.0000 0.0000 0.0000 28  LYS A NZ  
128  N N   . ALA A 29  ? 250.8732 250.8732 250.8732 0.0000 0.0000 0.0000 29  ALA A N   
129  C CA  . ALA A 29  ? 250.8493 250.8493 250.8493 0.0000 0.0000 0.0000 29  ALA A CA  
130  C C   . ALA A 29  ? 250.9840 250.9840 250.9840 0.0000 0.0000 0.0000 29  ALA A C   
131  O O   . ALA A 29  ? 250.9879 250.9879 250.9879 0.0000 0.0000 0.0000 29  ALA A O   
132  C CB  . ALA A 29  ? 250.8331 250.8331 250.8331 0.0000 0.0000 0.0000 29  ALA A CB  
133  N N   . GLU A 30  ? 255.1599 255.1599 255.1599 0.0000 0.0000 0.0000 30  GLU A N   
134  C CA  . GLU A 30  ? 255.2606 255.2606 255.2606 0.0000 0.0000 0.0000 30  GLU A CA  
135  C C   . GLU A 30  ? 255.2650 255.2650 255.2650 0.0000 0.0000 0.0000 30  GLU A C   
136  O O   . GLU A 30  ? 255.3582 255.3582 255.3582 0.0000 0.0000 0.0000 30  GLU A O   
137  C CB  . GLU A 30  ? 255.3165 255.3165 255.3165 0.0000 0.0000 0.0000 30  GLU A CB  
138  C CG  . GLU A 30  ? 255.3633 255.3633 255.3633 0.0000 0.0000 0.0000 30  GLU A CG  
139  C CD  . GLU A 30  ? 255.3556 255.3556 255.3556 0.0000 0.0000 0.0000 30  GLU A CD  
140  O OE1 . GLU A 30  ? 255.3168 255.3168 255.3168 0.0000 0.0000 0.0000 30  GLU A OE1 
141  O OE2 . GLU A 30  ? 255.4101 255.4101 255.4101 0.0000 0.0000 0.0000 30  GLU A OE2 
142  N N   . LYS A 31  ? 254.3898 254.3898 254.3898 0.0000 0.0000 0.0000 31  LYS A N   
143  C CA  . LYS A 31  ? 254.4647 254.4647 254.4647 0.0000 0.0000 0.0000 31  LYS A CA  
144  C C   . LYS A 31  ? 254.5563 254.5563 254.5563 0.0000 0.0000 0.0000 31  LYS A C   
145  O O   . LYS A 31  ? 254.7040 254.7040 254.7040 0.0000 0.0000 0.0000 31  LYS A O   
146  C CB  . LYS A 31  ? 254.4690 254.4690 254.4690 0.0000 0.0000 0.0000 31  LYS A CB  
147  C CG  . LYS A 31  ? 254.5495 254.5495 254.5495 0.0000 0.0000 0.0000 31  LYS A CG  
148  C CD  . LYS A 31  ? 254.5868 254.5868 254.5868 0.0000 0.0000 0.0000 31  LYS A CD  
149  C CE  . LYS A 31  ? 254.3779 254.3779 254.3779 0.0000 0.0000 0.0000 31  LYS A CE  
150  N NZ  . LYS A 31  ? 254.0844 254.0844 254.0844 0.0000 0.0000 0.0000 31  LYS A NZ  
151  N N   . LYS A 32  ? 251.6937 251.6937 251.6937 0.0000 0.0000 0.0000 32  LYS A N   
152  C CA  . LYS A 32  ? 251.7267 251.7267 251.7267 0.0000 0.0000 0.0000 32  LYS A CA  
153  C C   . LYS A 32  ? 251.9592 251.9592 251.9592 0.0000 0.0000 0.0000 32  LYS A C   
154  O O   . LYS A 32  ? 252.0491 252.0491 252.0491 0.0000 0.0000 0.0000 32  LYS A O   
155  C CB  . LYS A 32  ? 251.5573 251.5573 251.5573 0.0000 0.0000 0.0000 32  LYS A CB  
156  C CG  . LYS A 32  ? 251.5488 251.5488 251.5488 0.0000 0.0000 0.0000 32  LYS A CG  
157  C CD  . LYS A 32  ? 251.5158 251.5158 251.5158 0.0000 0.0000 0.0000 32  LYS A CD  
158  C CE  . LYS A 32  ? 251.5427 251.5427 251.5427 0.0000 0.0000 0.0000 32  LYS A CE  
159  N NZ  . LYS A 32  ? 251.5460 251.5460 251.5460 0.0000 0.0000 0.0000 32  LYS A NZ  
160  N N   . VAL A 33  ? 258.9330 258.9330 258.9330 0.0000 0.0000 0.0000 33  VAL A N   
161  C CA  . VAL A 33  ? 259.1420 259.1420 259.1420 0.0000 0.0000 0.0000 33  VAL A CA  
162  C C   . VAL A 33  ? 259.3805 259.3805 259.3805 0.0000 0.0000 0.0000 33  VAL A C   
163  O O   . VAL A 33  ? 259.6458 259.6458 259.6458 0.0000 0.0000 0.0000 33  VAL A O   
164  C CB  . VAL A 33  ? 259.1732 259.1732 259.1732 0.0000 0.0000 0.0000 33  VAL A CB  
165  C CG1 . VAL A 33  ? 259.1513 259.1513 259.1513 0.0000 0.0000 0.0000 33  VAL A CG1 
166  C CG2 . VAL A 33  ? 259.2078 259.2078 259.2078 0.0000 0.0000 0.0000 33  VAL A CG2 
167  N N   . ALA A 34  ? 263.0317 263.0317 263.0317 0.0000 0.0000 0.0000 34  ALA A N   
168  C CA  . ALA A 34  ? 263.2726 263.2726 263.2726 0.0000 0.0000 0.0000 34  ALA A CA  
169  C C   . ALA A 34  ? 263.5128 263.5128 263.5128 0.0000 0.0000 0.0000 34  ALA A C   
170  O O   . ALA A 34  ? 263.6466 263.6466 263.6466 0.0000 0.0000 0.0000 34  ALA A O   
171  C CB  . ALA A 34  ? 263.1797 263.1797 263.1797 0.0000 0.0000 0.0000 34  ALA A CB  
172  N N   . GLU A 35  ? 271.9108 271.9108 271.9108 0.0000 0.0000 0.0000 35  GLU A N   
173  C CA  . GLU A 35  ? 272.1526 272.1526 272.1526 0.0000 0.0000 0.0000 35  GLU A CA  
174  C C   . GLU A 35  ? 272.0995 272.0995 272.0995 0.0000 0.0000 0.0000 35  GLU A C   
175  O O   . GLU A 35  ? 272.3024 272.3024 272.3024 0.0000 0.0000 0.0000 35  GLU A O   
176  C CB  . GLU A 35  ? 272.1857 272.1857 272.1857 0.0000 0.0000 0.0000 35  GLU A CB  
177  C CG  . GLU A 35  ? 272.3714 272.3714 272.3714 0.0000 0.0000 0.0000 35  GLU A CG  
178  C CD  . GLU A 35  ? 272.4292 272.4292 272.4292 0.0000 0.0000 0.0000 35  GLU A CD  
179  O OE1 . GLU A 35  ? 272.4085 272.4085 272.4085 0.0000 0.0000 0.0000 35  GLU A OE1 
180  O OE2 . GLU A 35  ? 272.4291 272.4291 272.4291 0.0000 0.0000 0.0000 35  GLU A OE2 
181  N N   . LYS A 36  ? 263.5800 263.5800 263.5800 0.0000 0.0000 0.0000 36  LYS A N   
182  C CA  . LYS A 36  ? 263.5947 263.5947 263.5947 0.0000 0.0000 0.0000 36  LYS A CA  
183  C C   . LYS A 36  ? 263.9503 263.9503 263.9503 0.0000 0.0000 0.0000 36  LYS A C   
184  O O   . LYS A 36  ? 264.0991 264.0991 264.0991 0.0000 0.0000 0.0000 36  LYS A O   
185  C CB  . LYS A 36  ? 263.3955 263.3955 263.3955 0.0000 0.0000 0.0000 36  LYS A CB  
186  C CG  . LYS A 36  ? 263.4069 263.4069 263.4069 0.0000 0.0000 0.0000 36  LYS A CG  
187  C CD  . LYS A 36  ? 263.1846 263.1846 263.1846 0.0000 0.0000 0.0000 36  LYS A CD  
188  C CE  . LYS A 36  ? 262.5185 262.5185 262.5185 0.0000 0.0000 0.0000 36  LYS A CE  
189  N NZ  . LYS A 36  ? 261.8616 261.8616 261.8616 0.0000 0.0000 0.0000 36  LYS A NZ  
190  N N   . GLU A 37  ? 277.8323 277.8323 277.8323 0.0000 0.0000 0.0000 37  GLU A N   
191  C CA  . GLU A 37  ? 278.1404 278.1404 278.1404 0.0000 0.0000 0.0000 37  GLU A CA  
192  C C   . GLU A 37  ? 278.1827 278.1827 278.1827 0.0000 0.0000 0.0000 37  GLU A C   
193  O O   . GLU A 37  ? 278.3490 278.3490 278.3490 0.0000 0.0000 0.0000 37  GLU A O   
194  C CB  . GLU A 37  ? 278.2105 278.2105 278.2105 0.0000 0.0000 0.0000 37  GLU A CB  
195  C CG  . GLU A 37  ? 278.1705 278.1705 278.1705 0.0000 0.0000 0.0000 37  GLU A CG  
196  C CD  . GLU A 37  ? 278.3110 278.3110 278.3110 0.0000 0.0000 0.0000 37  GLU A CD  
197  O OE1 . GLU A 37  ? 278.4174 278.4174 278.4174 0.0000 0.0000 0.0000 37  GLU A OE1 
198  O OE2 . GLU A 37  ? 278.2939 278.2939 278.2939 0.0000 0.0000 0.0000 37  GLU A OE2 
199  N N   . ALA A 38  ? 275.9009 275.9009 275.9009 0.0000 0.0000 0.0000 38  ALA A N   
200  C CA  . ALA A 38  ? 275.9397 275.9397 275.9397 0.0000 0.0000 0.0000 38  ALA A CA  
201  C C   . ALA A 38  ? 275.9912 275.9912 275.9912 0.0000 0.0000 0.0000 38  ALA A C   
202  O O   . ALA A 38  ? 276.0800 276.0800 276.0800 0.0000 0.0000 0.0000 38  ALA A O   
203  C CB  . ALA A 38  ? 275.9239 275.9239 275.9239 0.0000 0.0000 0.0000 38  ALA A CB  
204  N N   . LYS A 39  ? 273.8518 273.8518 273.8518 0.0000 0.0000 0.0000 39  LYS A N   
205  C CA  . LYS A 39  ? 273.8680 273.8680 273.8680 0.0000 0.0000 0.0000 39  LYS A CA  
206  C C   . LYS A 39  ? 274.1242 274.1242 274.1242 0.0000 0.0000 0.0000 39  LYS A C   
207  O O   . LYS A 39  ? 274.2632 274.2632 274.2632 0.0000 0.0000 0.0000 39  LYS A O   
208  C CB  . LYS A 39  ? 273.7313 273.7313 273.7313 0.0000 0.0000 0.0000 39  LYS A CB  
209  C CG  . LYS A 39  ? 273.7525 273.7525 273.7525 0.0000 0.0000 0.0000 39  LYS A CG  
210  C CD  . LYS A 39  ? 273.7453 273.7453 273.7453 0.0000 0.0000 0.0000 39  LYS A CD  
211  C CE  . LYS A 39  ? 273.6757 273.6757 273.6757 0.0000 0.0000 0.0000 39  LYS A CE  
212  N NZ  . LYS A 39  ? 273.0876 273.0876 273.0876 0.0000 0.0000 0.0000 39  LYS A NZ  
213  N N   . GLN A 40  ? 286.0794 286.0794 286.0794 0.0000 0.0000 0.0000 40  GLN A N   
214  C CA  . GLN A 40  ? 286.4206 286.4206 286.4206 0.0000 0.0000 0.0000 40  GLN A CA  
215  C C   . GLN A 40  ? 286.5766 286.5766 286.5766 0.0000 0.0000 0.0000 40  GLN A C   
216  O O   . GLN A 40  ? 286.7091 286.7091 286.7091 0.0000 0.0000 0.0000 40  GLN A O   
217  C CB  . GLN A 40  ? 286.4747 286.4747 286.4747 0.0000 0.0000 0.0000 40  GLN A CB  
218  C CG  . GLN A 40  ? 286.4979 286.4979 286.4979 0.0000 0.0000 0.0000 40  GLN A CG  
219  C CD  . GLN A 40  ? 286.6405 286.6405 286.6405 0.0000 0.0000 0.0000 40  GLN A CD  
220  O OE1 . GLN A 40  ? 286.7019 286.7019 286.7019 0.0000 0.0000 0.0000 40  GLN A OE1 
221  N NE2 . GLN A 40  ? 286.6208 286.6208 286.6208 0.0000 0.0000 0.0000 40  GLN A NE2 
222  N N   . LYS A 41  ? 285.0463 285.0463 285.0463 0.0000 0.0000 0.0000 41  LYS A N   
223  C CA  . LYS A 41  ? 285.1539 285.1539 285.1539 0.0000 0.0000 0.0000 41  LYS A CA  
224  C C   . LYS A 41  ? 285.2691 285.2691 285.2691 0.0000 0.0000 0.0000 41  LYS A C   
225  O O   . LYS A 41  ? 285.2552 285.2552 285.2552 0.0000 0.0000 0.0000 41  LYS A O   
226  C CB  . LYS A 41  ? 285.1362 285.1362 285.1362 0.0000 0.0000 0.0000 41  LYS A CB  
227  C CG  . LYS A 41  ? 285.1489 285.1489 285.1489 0.0000 0.0000 0.0000 41  LYS A CG  
228  C CD  . LYS A 41  ? 285.1519 285.1519 285.1519 0.0000 0.0000 0.0000 41  LYS A CD  
229  C CE  . LYS A 41  ? 285.1527 285.1527 285.1527 0.0000 0.0000 0.0000 41  LYS A CE  
230  N NZ  . LYS A 41  ? 285.1350 285.1350 285.1350 0.0000 0.0000 0.0000 41  LYS A NZ  
231  N N   . GLU A 42  ? 292.1135 292.1135 292.1135 0.0000 0.0000 0.0000 42  GLU A N   
232  C CA  . GLU A 42  ? 292.3201 292.3201 292.3201 0.0000 0.0000 0.0000 42  GLU A CA  
233  C C   . GLU A 42  ? 292.4865 292.4865 292.4865 0.0000 0.0000 0.0000 42  GLU A C   
234  O O   . GLU A 42  ? 292.5342 292.5342 292.5342 0.0000 0.0000 0.0000 42  GLU A O   
235  C CB  . GLU A 42  ? 292.2714 292.2714 292.2714 0.0000 0.0000 0.0000 42  GLU A CB  
236  C CG  . GLU A 42  ? 292.4446 292.4446 292.4446 0.0000 0.0000 0.0000 42  GLU A CG  
237  C CD  . GLU A 42  ? 292.5296 292.5296 292.5296 0.0000 0.0000 0.0000 42  GLU A CD  
238  O OE1 . GLU A 42  ? 292.5213 292.5213 292.5213 0.0000 0.0000 0.0000 42  GLU A OE1 
239  O OE2 . GLU A 42  ? 292.5658 292.5658 292.5658 0.0000 0.0000 0.0000 42  GLU A OE2 
240  N N   . LEU A 43  ? 296.9041 296.9041 296.9041 0.0000 0.0000 0.0000 43  LEU A N   
241  C CA  . LEU A 43  ? 297.0942 297.0942 297.0942 0.0000 0.0000 0.0000 43  LEU A CA  
242  C C   . LEU A 43  ? 297.1573 297.1573 297.1573 0.0000 0.0000 0.0000 43  LEU A C   
243  O O   . LEU A 43  ? 297.0977 297.0977 297.0977 0.0000 0.0000 0.0000 43  LEU A O   
244  C CB  . LEU A 43  ? 297.1158 297.1158 297.1158 0.0000 0.0000 0.0000 43  LEU A CB  
245  C CG  . LEU A 43  ? 297.1705 297.1705 297.1705 0.0000 0.0000 0.0000 43  LEU A CG  
246  C CD1 . LEU A 43  ? 297.2397 297.2397 297.2397 0.0000 0.0000 0.0000 43  LEU A CD1 
247  C CD2 . LEU A 43  ? 297.0979 297.0979 297.0979 0.0000 0.0000 0.0000 43  LEU A CD2 
248  N N   . GLU A 69  ? 263.7085 263.7085 263.7085 0.0000 0.0000 0.0000 69  GLU A N   
249  C CA  . GLU A 69  ? 263.6100 263.6100 263.6100 0.0000 0.0000 0.0000 69  GLU A CA  
250  C C   . GLU A 69  ? 263.0556 263.0556 263.0556 0.0000 0.0000 0.0000 69  GLU A C   
251  O O   . GLU A 69  ? 263.0893 263.0893 263.0893 0.0000 0.0000 0.0000 69  GLU A O   
252  C CB  . GLU A 69  ? 263.7141 263.7141 263.7141 0.0000 0.0000 0.0000 69  GLU A CB  
253  C CG  . GLU A 69  ? 263.6122 263.6122 263.6122 0.0000 0.0000 0.0000 69  GLU A CG  
254  C CD  . GLU A 69  ? 263.6308 263.6308 263.6308 0.0000 0.0000 0.0000 69  GLU A CD  
255  O OE1 . GLU A 69  ? 263.8224 263.8224 263.8224 0.0000 0.0000 0.0000 69  GLU A OE1 
256  O OE2 . GLU A 69  ? 263.4514 263.4514 263.4514 0.0000 0.0000 0.0000 69  GLU A OE2 
257  N N   . SER A 70  ? 240.6660 240.6660 240.6660 0.0000 0.0000 0.0000 70  SER A N   
258  C CA  . SER A 70  ? 240.0182 240.0182 240.0182 0.0000 0.0000 0.0000 70  SER A CA  
259  C C   . SER A 70  ? 239.2894 239.2894 239.2894 0.0000 0.0000 0.0000 70  SER A C   
260  O O   . SER A 70  ? 239.4988 239.4988 239.4988 0.0000 0.0000 0.0000 70  SER A O   
261  C CB  . SER A 70  ? 240.0886 240.0886 240.0886 0.0000 0.0000 0.0000 70  SER A CB  
262  O OG  . SER A 70  ? 240.2236 240.2236 240.2236 0.0000 0.0000 0.0000 70  SER A OG  
263  N N   . VAL A 71  ? 201.4898 201.4898 201.4898 0.0000 0.0000 0.0000 71  VAL A N   
264  C CA  . VAL A 71  ? 200.3889 200.3889 200.3889 0.0000 0.0000 0.0000 71  VAL A CA  
265  C C   . VAL A 71  ? 199.4885 199.4885 199.4885 0.0000 0.0000 0.0000 71  VAL A C   
266  O O   . VAL A 71  ? 199.7355 199.7355 199.7355 0.0000 0.0000 0.0000 71  VAL A O   
267  C CB  . VAL A 71  ? 199.9564 199.9564 199.9564 0.0000 0.0000 0.0000 71  VAL A CB  
268  C CG1 . VAL A 71  ? 199.2433 199.2433 199.2433 0.0000 0.0000 0.0000 71  VAL A CG1 
269  C CG2 . VAL A 71  ? 200.1255 200.1255 200.1255 0.0000 0.0000 0.0000 71  VAL A CG2 
270  N N   . ASP A 72  ? 180.4188 180.4188 180.4188 0.0000 0.0000 0.0000 72  ASP A N   
271  C CA  . ASP A 72  ? 179.4880 179.4880 179.4880 0.0000 0.0000 0.0000 72  ASP A CA  
272  C C   . ASP A 72  ? 179.0586 179.0586 179.0586 0.0000 0.0000 0.0000 72  ASP A C   
273  O O   . ASP A 72  ? 179.1999 179.1999 179.1999 0.0000 0.0000 0.0000 72  ASP A O   
274  C CB  . ASP A 72  ? 179.2026 179.2026 179.2026 0.0000 0.0000 0.0000 72  ASP A CB  
275  C CG  . ASP A 72  ? 179.5154 179.5154 179.5154 0.0000 0.0000 0.0000 72  ASP A CG  
276  O OD1 . ASP A 72  ? 179.7774 179.7774 179.7774 0.0000 0.0000 0.0000 72  ASP A OD1 
277  O OD2 . ASP A 72  ? 179.7002 179.7002 179.7002 0.0000 0.0000 0.0000 72  ASP A OD2 
278  N N   . PRO A 73  ? 161.7338 161.7338 161.7338 0.0000 0.0000 0.0000 73  PRO A N   
279  C CA  . PRO A 73  ? 159.9931 159.9931 159.9931 0.0000 0.0000 0.0000 73  PRO A CA  
280  C C   . PRO A 73  ? 159.8203 159.8203 159.8203 0.0000 0.0000 0.0000 73  PRO A C   
281  O O   . PRO A 73  ? 159.2234 159.2234 159.2234 0.0000 0.0000 0.0000 73  PRO A O   
282  C CB  . PRO A 73  ? 157.7022 157.7022 157.7022 0.0000 0.0000 0.0000 73  PRO A CB  
283  C CG  . PRO A 73  ? 158.9055 158.9055 158.9055 0.0000 0.0000 0.0000 73  PRO A CG  
284  C CD  . PRO A 73  ? 160.2201 160.2201 160.2201 0.0000 0.0000 0.0000 73  PRO A CD  
285  N N   . ASN A 74  ? 160.7896 160.7896 160.7896 0.0000 0.0000 0.0000 74  ASN A N   
286  C CA  . ASN A 74  ? 160.9440 160.9440 160.9440 0.0000 0.0000 0.0000 74  ASN A CA  
287  C C   . ASN A 74  ? 161.4825 161.4825 161.4825 0.0000 0.0000 0.0000 74  ASN A C   
288  O O   . ASN A 74  ? 161.4847 161.4847 161.4847 0.0000 0.0000 0.0000 74  ASN A O   
289  C CB  . ASN A 74  ? 159.3803 159.3803 159.3803 0.0000 0.0000 0.0000 74  ASN A CB  
290  C CG  . ASN A 74  ? 160.1286 160.1286 160.1286 0.0000 0.0000 0.0000 74  ASN A CG  
291  O OD1 . ASN A 74  ? 161.5576 161.5576 161.5576 0.0000 0.0000 0.0000 74  ASN A OD1 
292  N ND2 . ASN A 74  ? 158.1380 158.1380 158.1380 0.0000 0.0000 0.0000 74  ASN A ND2 
293  N N   . GLN A 75  ? 161.5424 161.5424 161.5424 0.0000 0.0000 0.0000 75  GLN A N   
294  C CA  . GLN A 75  ? 161.4568 161.4568 161.4568 0.0000 0.0000 0.0000 75  GLN A CA  
295  C C   . GLN A 75  ? 161.3000 161.3000 161.3000 0.0000 0.0000 0.0000 75  GLN A C   
296  O O   . GLN A 75  ? 161.3845 161.3845 161.3845 0.0000 0.0000 0.0000 75  GLN A O   
297  C CB  . GLN A 75  ? 161.5359 161.5359 161.5359 0.0000 0.0000 0.0000 75  GLN A CB  
298  C CG  . GLN A 75  ? 161.8505 161.8505 161.8505 0.0000 0.0000 0.0000 75  GLN A CG  
299  C CD  . GLN A 75  ? 161.4751 161.4751 161.4751 0.0000 0.0000 0.0000 75  GLN A CD  
300  O OE1 . GLN A 75  ? 161.4327 161.4327 161.4327 0.0000 0.0000 0.0000 75  GLN A OE1 
301  N NE2 . GLN A 75  ? 161.2657 161.2657 161.2657 0.0000 0.0000 0.0000 75  GLN A NE2 
302  N N   . TYR A 76  ? 161.1882 161.1882 161.1882 0.0000 0.0000 0.0000 76  TYR A N   
303  C CA  . TYR A 76  ? 161.0588 161.0588 161.0588 0.0000 0.0000 0.0000 76  TYR A CA  
304  C C   . TYR A 76  ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 76  TYR A C   
305  O O   . TYR A 76  ? 161.6062 161.6062 161.6062 0.0000 0.0000 0.0000 76  TYR A O   
306  C CB  . TYR A 76  ? 160.7726 160.7726 160.7726 0.0000 0.0000 0.0000 76  TYR A CB  
307  C CG  . TYR A 76  ? 159.9386 159.9386 159.9386 0.0000 0.0000 0.0000 76  TYR A CG  
308  C CD1 . TYR A 76  ? 158.8769 158.8769 158.8769 0.0000 0.0000 0.0000 76  TYR A CD1 
309  C CD2 . TYR A 76  ? 161.4023 161.4023 161.4023 0.0000 0.0000 0.0000 76  TYR A CD2 
310  C CE1 . TYR A 76  ? 159.3657 159.3657 159.3657 0.0000 0.0000 0.0000 76  TYR A CE1 
311  C CE2 . TYR A 76  ? 161.4364 161.4364 161.4364 0.0000 0.0000 0.0000 76  TYR A CE2 
312  C CZ  . TYR A 76  ? 160.5335 160.5335 160.5335 0.0000 0.0000 0.0000 76  TYR A CZ  
313  O OH  . TYR A 76  ? 161.2608 161.2608 161.2608 0.0000 0.0000 0.0000 76  TYR A OH  
314  N N   . TYR A 77  ? 161.3082 161.3082 161.3082 0.0000 0.0000 0.0000 77  TYR A N   
315  C CA  . TYR A 77  ? 161.3252 161.3252 161.3252 0.0000 0.0000 0.0000 77  TYR A CA  
316  C C   . TYR A 77  ? 161.3946 161.3946 161.3946 0.0000 0.0000 0.0000 77  TYR A C   
317  O O   . TYR A 77  ? 161.5208 161.5208 161.5208 0.0000 0.0000 0.0000 77  TYR A O   
318  C CB  . TYR A 77  ? 161.3111 161.3111 161.3111 0.0000 0.0000 0.0000 77  TYR A CB  
319  C CG  . TYR A 77  ? 161.3139 161.3139 161.3139 0.0000 0.0000 0.0000 77  TYR A CG  
320  C CD1 . TYR A 77  ? 161.5513 161.5513 161.5513 0.0000 0.0000 0.0000 77  TYR A CD1 
321  C CD2 . TYR A 77  ? 161.4684 161.4684 161.4684 0.0000 0.0000 0.0000 77  TYR A CD2 
322  C CE1 . TYR A 77  ? 161.6030 161.6030 161.6030 0.0000 0.0000 0.0000 77  TYR A CE1 
323  C CE2 . TYR A 77  ? 161.4988 161.4988 161.4988 0.0000 0.0000 0.0000 77  TYR A CE2 
324  C CZ  . TYR A 77  ? 161.4881 161.4881 161.4881 0.0000 0.0000 0.0000 77  TYR A CZ  
325  O OH  . TYR A 77  ? 161.6227 161.6227 161.6227 0.0000 0.0000 0.0000 77  TYR A OH  
326  N N   . LYS A 78  ? 161.3516 161.3516 161.3516 0.0000 0.0000 0.0000 78  LYS A N   
327  C CA  . LYS A 78  ? 161.3429 161.3429 161.3429 0.0000 0.0000 0.0000 78  LYS A CA  
328  C C   . LYS A 78  ? 161.3686 161.3686 161.3686 0.0000 0.0000 0.0000 78  LYS A C   
329  O O   . LYS A 78  ? 161.5603 161.5603 161.5603 0.0000 0.0000 0.0000 78  LYS A O   
330  C CB  . LYS A 78  ? 161.4942 161.4942 161.4942 0.0000 0.0000 0.0000 78  LYS A CB  
331  C CG  . LYS A 78  ? 161.4572 161.4572 161.4572 0.0000 0.0000 0.0000 78  LYS A CG  
332  C CD  . LYS A 78  ? 161.6010 161.6010 161.6010 0.0000 0.0000 0.0000 78  LYS A CD  
333  C CE  . LYS A 78  ? 161.5731 161.5731 161.5731 0.0000 0.0000 0.0000 78  LYS A CE  
334  N NZ  . LYS A 78  ? 161.5189 161.5189 161.5189 0.0000 0.0000 0.0000 78  LYS A NZ  
335  N N   . ILE A 79  ? 161.3020 161.3020 161.3020 0.0000 0.0000 0.0000 79  ILE A N   
336  C CA  . ILE A 79  ? 161.2559 161.2559 161.2559 0.0000 0.0000 0.0000 79  ILE A CA  
337  C C   . ILE A 79  ? 161.2829 161.2829 161.2829 0.0000 0.0000 0.0000 79  ILE A C   
338  O O   . ILE A 79  ? 161.3951 161.3951 161.3951 0.0000 0.0000 0.0000 79  ILE A O   
339  C CB  . ILE A 79  ? 161.3530 161.3530 161.3530 0.0000 0.0000 0.0000 79  ILE A CB  
340  C CG1 . ILE A 79  ? 161.7133 161.7133 161.7133 0.0000 0.0000 0.0000 79  ILE A CG1 
341  C CG2 . ILE A 79  ? 161.4552 161.4552 161.4552 0.0000 0.0000 0.0000 79  ILE A CG2 
342  C CD1 . ILE A 79  ? 161.1783 161.1783 161.1783 0.0000 0.0000 0.0000 79  ILE A CD1 
343  N N   . ARG A 80  ? 161.3351 161.3351 161.3351 0.0000 0.0000 0.0000 80  ARG A N   
344  C CA  . ARG A 80  ? 161.3349 161.3349 161.3349 0.0000 0.0000 0.0000 80  ARG A CA  
345  C C   . ARG A 80  ? 161.3941 161.3941 161.3941 0.0000 0.0000 0.0000 80  ARG A C   
346  O O   . ARG A 80  ? 161.5842 161.5842 161.5842 0.0000 0.0000 0.0000 80  ARG A O   
347  C CB  . ARG A 80  ? 161.4571 161.4571 161.4571 0.0000 0.0000 0.0000 80  ARG A CB  
348  C CG  . ARG A 80  ? 161.4786 161.4786 161.4786 0.0000 0.0000 0.0000 80  ARG A CG  
349  C CD  . ARG A 80  ? 161.3179 161.3179 161.3179 0.0000 0.0000 0.0000 80  ARG A CD  
350  N NE  . ARG A 80  ? 161.1997 161.1997 161.1997 0.0000 0.0000 0.0000 80  ARG A NE  
351  C CZ  . ARG A 80  ? 161.2200 161.2200 161.2200 0.0000 0.0000 0.0000 80  ARG A CZ  
352  N NH1 . ARG A 80  ? 161.3069 161.3069 161.3069 0.0000 0.0000 0.0000 80  ARG A NH1 
353  N NH2 . ARG A 80  ? 161.4258 161.4258 161.4258 0.0000 0.0000 0.0000 80  ARG A NH2 
354  N N   . SER A 81  ? 161.3805 161.3805 161.3805 0.0000 0.0000 0.0000 81  SER A N   
355  C CA  . SER A 81  ? 161.3492 161.3492 161.3492 0.0000 0.0000 0.0000 81  SER A CA  
356  C C   . SER A 81  ? 161.3353 161.3353 161.3353 0.0000 0.0000 0.0000 81  SER A C   
357  O O   . SER A 81  ? 161.4266 161.4266 161.4266 0.0000 0.0000 0.0000 81  SER A O   
358  C CB  . SER A 81  ? 161.4066 161.4066 161.4066 0.0000 0.0000 0.0000 81  SER A CB  
359  O OG  . SER A 81  ? 161.4566 161.4566 161.4566 0.0000 0.0000 0.0000 81  SER A OG  
360  N N   . GLN A 82  ? 161.2616 161.2616 161.2616 0.0000 0.0000 0.0000 82  GLN A N   
361  C CA  . GLN A 82  ? 161.1965 161.1965 161.1965 0.0000 0.0000 0.0000 82  GLN A CA  
362  C C   . GLN A 82  ? 161.1858 161.1858 161.1858 0.0000 0.0000 0.0000 82  GLN A C   
363  O O   . GLN A 82  ? 161.4038 161.4038 161.4038 0.0000 0.0000 0.0000 82  GLN A O   
364  C CB  . GLN A 82  ? 161.3705 161.3705 161.3705 0.0000 0.0000 0.0000 82  GLN A CB  
365  C CG  . GLN A 82  ? 161.4070 161.4070 161.4070 0.0000 0.0000 0.0000 82  GLN A CG  
366  C CD  . GLN A 82  ? 161.4432 161.4432 161.4432 0.0000 0.0000 0.0000 82  GLN A CD  
367  O OE1 . GLN A 82  ? 161.5734 161.5734 161.5734 0.0000 0.0000 0.0000 82  GLN A OE1 
368  N NE2 . GLN A 82  ? 161.5944 161.5944 161.5944 0.0000 0.0000 0.0000 82  GLN A NE2 
369  N N   . ALA A 83  ? 161.1334 161.1334 161.1334 0.0000 0.0000 0.0000 83  ALA A N   
370  C CA  . ALA A 83  ? 161.2697 161.2697 161.2697 0.0000 0.0000 0.0000 83  ALA A CA  
371  C C   . ALA A 83  ? 161.4487 161.4487 161.4487 0.0000 0.0000 0.0000 83  ALA A C   
372  O O   . ALA A 83  ? 161.6445 161.6445 161.6445 0.0000 0.0000 0.0000 83  ALA A O   
373  C CB  . ALA A 83  ? 161.4221 161.4221 161.4221 0.0000 0.0000 0.0000 83  ALA A CB  
374  N N   . ILE A 84  ? 161.4446 161.4446 161.4446 0.0000 0.0000 0.0000 84  ILE A N   
375  C CA  . ILE A 84  ? 161.3525 161.3525 161.3525 0.0000 0.0000 0.0000 84  ILE A CA  
376  C C   . ILE A 84  ? 161.4367 161.4367 161.4367 0.0000 0.0000 0.0000 84  ILE A C   
377  O O   . ILE A 84  ? 161.6126 161.6126 161.6126 0.0000 0.0000 0.0000 84  ILE A O   
378  C CB  . ILE A 84  ? 161.3828 161.3828 161.3828 0.0000 0.0000 0.0000 84  ILE A CB  
379  C CG1 . ILE A 84  ? 161.5113 161.5113 161.5113 0.0000 0.0000 0.0000 84  ILE A CG1 
380  C CG2 . ILE A 84  ? 161.4882 161.4882 161.4882 0.0000 0.0000 0.0000 84  ILE A CG2 
381  C CD1 . ILE A 84  ? 161.6033 161.6033 161.6033 0.0000 0.0000 0.0000 84  ILE A CD1 
382  N N   . HIS A 85  ? 161.4564 161.4564 161.4564 0.0000 0.0000 0.0000 85  HIS A N   
383  C CA  . HIS A 85  ? 161.3734 161.3734 161.3734 0.0000 0.0000 0.0000 85  HIS A CA  
384  C C   . HIS A 85  ? 161.4361 161.4361 161.4361 0.0000 0.0000 0.0000 85  HIS A C   
385  O O   . HIS A 85  ? 161.5900 161.5900 161.5900 0.0000 0.0000 0.0000 85  HIS A O   
386  C CB  . HIS A 85  ? 161.2994 161.2994 161.2994 0.0000 0.0000 0.0000 85  HIS A CB  
387  C CG  . HIS A 85  ? 161.3065 161.3065 161.3065 0.0000 0.0000 0.0000 85  HIS A CG  
388  N ND1 . HIS A 85  ? 161.3959 161.3959 161.3959 0.0000 0.0000 0.0000 85  HIS A ND1 
389  C CD2 . HIS A 85  ? 161.4434 161.4434 161.4434 0.0000 0.0000 0.0000 85  HIS A CD2 
390  C CE1 . HIS A 85  ? 161.5053 161.5053 161.5053 0.0000 0.0000 0.0000 85  HIS A CE1 
391  N NE2 . HIS A 85  ? 161.5122 161.5122 161.5122 0.0000 0.0000 0.0000 85  HIS A NE2 
392  N N   . GLN A 86  ? 161.4221 161.4221 161.4221 0.0000 0.0000 0.0000 86  GLN A N   
393  C CA  . GLN A 86  ? 161.4616 161.4616 161.4616 0.0000 0.0000 0.0000 86  GLN A CA  
394  C C   . GLN A 86  ? 161.6198 161.6198 161.6198 0.0000 0.0000 0.0000 86  GLN A C   
395  O O   . GLN A 86  ? 162.0281 162.0281 162.0281 0.0000 0.0000 0.0000 86  GLN A O   
396  C CB  . GLN A 86  ? 161.4726 161.4726 161.4726 0.0000 0.0000 0.0000 86  GLN A CB  
397  C CG  . GLN A 86  ? 161.4540 161.4540 161.4540 0.0000 0.0000 0.0000 86  GLN A CG  
398  C CD  . GLN A 86  ? 161.4432 161.4432 161.4432 0.0000 0.0000 0.0000 86  GLN A CD  
399  O OE1 . GLN A 86  ? 161.3757 161.3757 161.3757 0.0000 0.0000 0.0000 86  GLN A OE1 
400  N NE2 . GLN A 86  ? 161.4946 161.4946 161.4946 0.0000 0.0000 0.0000 86  GLN A NE2 
401  N N   . LEU A 87  ? 161.4600 161.4600 161.4600 0.0000 0.0000 0.0000 87  LEU A N   
402  C CA  . LEU A 87  ? 161.8693 161.8693 161.8693 0.0000 0.0000 0.0000 87  LEU A CA  
403  C C   . LEU A 87  ? 162.0225 162.0225 162.0225 0.0000 0.0000 0.0000 87  LEU A C   
404  O O   . LEU A 87  ? 162.7048 162.7048 162.7048 0.0000 0.0000 0.0000 87  LEU A O   
405  C CB  . LEU A 87  ? 161.7290 161.7290 161.7290 0.0000 0.0000 0.0000 87  LEU A CB  
406  C CG  . LEU A 87  ? 161.5344 161.5344 161.5344 0.0000 0.0000 0.0000 87  LEU A CG  
407  C CD1 . LEU A 87  ? 161.4064 161.4064 161.4064 0.0000 0.0000 0.0000 87  LEU A CD1 
408  C CD2 . LEU A 87  ? 161.8839 161.8839 161.8839 0.0000 0.0000 0.0000 87  LEU A CD2 
409  N N   . LYS A 88  ? 161.6624 161.6624 161.6624 0.0000 0.0000 0.0000 88  LYS A N   
410  C CA  . LYS A 88  ? 161.6931 161.6931 161.6931 0.0000 0.0000 0.0000 88  LYS A CA  
411  C C   . LYS A 88  ? 161.9085 161.9085 161.9085 0.0000 0.0000 0.0000 88  LYS A C   
412  O O   . LYS A 88  ? 161.9959 161.9959 161.9959 0.0000 0.0000 0.0000 88  LYS A O   
413  C CB  . LYS A 88  ? 161.5491 161.5491 161.5491 0.0000 0.0000 0.0000 88  LYS A CB  
414  C CG  . LYS A 88  ? 161.5544 161.5544 161.5544 0.0000 0.0000 0.0000 88  LYS A CG  
415  C CD  . LYS A 88  ? 161.3497 161.3497 161.3497 0.0000 0.0000 0.0000 88  LYS A CD  
416  C CE  . LYS A 88  ? 161.2433 161.2433 161.2433 0.0000 0.0000 0.0000 88  LYS A CE  
417  N NZ  . LYS A 88  ? 161.2907 161.2907 161.2907 0.0000 0.0000 0.0000 88  LYS A NZ  
418  N N   . VAL A 89  ? 167.5125 167.5125 167.5125 0.0000 0.0000 0.0000 89  VAL A N   
419  C CA  . VAL A 89  ? 167.6778 167.6778 167.6778 0.0000 0.0000 0.0000 89  VAL A CA  
420  C C   . VAL A 89  ? 167.9384 167.9384 167.9384 0.0000 0.0000 0.0000 89  VAL A C   
421  O O   . VAL A 89  ? 167.9874 167.9874 167.9874 0.0000 0.0000 0.0000 89  VAL A O   
422  C CB  . VAL A 89  ? 167.5140 167.5140 167.5140 0.0000 0.0000 0.0000 89  VAL A CB  
423  C CG1 . VAL A 89  ? 167.4726 167.4726 167.4726 0.0000 0.0000 0.0000 89  VAL A CG1 
424  C CG2 . VAL A 89  ? 167.7116 167.7116 167.7116 0.0000 0.0000 0.0000 89  VAL A CG2 
425  N N   . ASN A 90  ? 178.7993 178.7993 178.7993 0.0000 0.0000 0.0000 90  ASN A N   
426  C CA  . ASN A 90  ? 179.2988 179.2988 179.2988 0.0000 0.0000 0.0000 90  ASN A CA  
427  C C   . ASN A 90  ? 179.4720 179.4720 179.4720 0.0000 0.0000 0.0000 90  ASN A C   
428  O O   . ASN A 90  ? 179.8298 179.8298 179.8298 0.0000 0.0000 0.0000 90  ASN A O   
429  C CB  . ASN A 90  ? 179.6159 179.6159 179.6159 0.0000 0.0000 0.0000 90  ASN A CB  
430  C CG  . ASN A 90  ? 179.6367 179.6367 179.6367 0.0000 0.0000 0.0000 90  ASN A CG  
431  O OD1 . ASN A 90  ? 179.4372 179.4372 179.4372 0.0000 0.0000 0.0000 90  ASN A OD1 
432  N ND2 . ASN A 90  ? 179.6979 179.6979 179.6979 0.0000 0.0000 0.0000 90  ASN A ND2 
433  N N   . GLY A 91  ? 175.4381 175.4381 175.4381 0.0000 0.0000 0.0000 91  GLY A N   
434  C CA  . GLY A 91  ? 175.4936 175.4936 175.4936 0.0000 0.0000 0.0000 91  GLY A CA  
435  C C   . GLY A 91  ? 175.6339 175.6339 175.6339 0.0000 0.0000 0.0000 91  GLY A C   
436  O O   . GLY A 91  ? 175.4365 175.4365 175.4365 0.0000 0.0000 0.0000 91  GLY A O   
437  N N   . GLU A 92  ? 186.8119 186.8119 186.8119 0.0000 0.0000 0.0000 92  GLU A N   
438  C CA  . GLU A 92  ? 186.9796 186.9796 186.9796 0.0000 0.0000 0.0000 92  GLU A CA  
439  C C   . GLU A 92  ? 186.4270 186.4270 186.4270 0.0000 0.0000 0.0000 92  GLU A C   
440  O O   . GLU A 92  ? 186.4782 186.4782 186.4782 0.0000 0.0000 0.0000 92  GLU A O   
441  C CB  . GLU A 92  ? 187.1692 187.1692 187.1692 0.0000 0.0000 0.0000 92  GLU A CB  
442  C CG  . GLU A 92  ? 187.4236 187.4236 187.4236 0.0000 0.0000 0.0000 92  GLU A CG  
443  C CD  . GLU A 92  ? 187.4445 187.4445 187.4445 0.0000 0.0000 0.0000 92  GLU A CD  
444  O OE1 . GLU A 92  ? 187.2347 187.2347 187.2347 0.0000 0.0000 0.0000 92  GLU A OE1 
445  O OE2 . GLU A 92  ? 187.5002 187.5002 187.5002 0.0000 0.0000 0.0000 92  GLU A OE2 
446  N N   . ASP A 93  ? 164.1804 164.1804 164.1804 0.0000 0.0000 0.0000 93  ASP A N   
447  C CA  . ASP A 93  ? 163.6138 163.6138 163.6138 0.0000 0.0000 0.0000 93  ASP A CA  
448  C C   . ASP A 93  ? 163.3047 163.3047 163.3047 0.0000 0.0000 0.0000 93  ASP A C   
449  O O   . ASP A 93  ? 163.2657 163.2657 163.2657 0.0000 0.0000 0.0000 93  ASP A O   
450  C CB  . ASP A 93  ? 163.4048 163.4048 163.4048 0.0000 0.0000 0.0000 93  ASP A CB  
451  C CG  . ASP A 93  ? 163.2219 163.2219 163.2219 0.0000 0.0000 0.0000 93  ASP A CG  
452  O OD1 . ASP A 93  ? 163.0579 163.0579 163.0579 0.0000 0.0000 0.0000 93  ASP A OD1 
453  O OD2 . ASP A 93  ? 163.2171 163.2171 163.2171 0.0000 0.0000 0.0000 93  ASP A OD2 
454  N N   . PRO A 94  ? 161.4995 161.4995 161.4995 0.0000 0.0000 0.0000 94  PRO A N   
455  C CA  . PRO A 94  ? 161.4124 161.4124 161.4124 0.0000 0.0000 0.0000 94  PRO A CA  
456  C C   . PRO A 94  ? 161.5136 161.5136 161.5136 0.0000 0.0000 0.0000 94  PRO A C   
457  O O   . PRO A 94  ? 161.8286 161.8286 161.8286 0.0000 0.0000 0.0000 94  PRO A O   
458  C CB  . PRO A 94  ? 161.5061 161.5061 161.5061 0.0000 0.0000 0.0000 94  PRO A CB  
459  C CG  . PRO A 94  ? 161.5286 161.5286 161.5286 0.0000 0.0000 0.0000 94  PRO A CG  
460  C CD  . PRO A 94  ? 161.6305 161.6305 161.6305 0.0000 0.0000 0.0000 94  PRO A CD  
461  N N   . TYR A 95  ? 161.5569 161.5569 161.5569 0.0000 0.0000 0.0000 95  TYR A N   
462  C CA  . TYR A 95  ? 161.4316 161.4316 161.4316 0.0000 0.0000 0.0000 95  TYR A CA  
463  C C   . TYR A 95  ? 161.2982 161.2982 161.2982 0.0000 0.0000 0.0000 95  TYR A C   
464  O O   . TYR A 95  ? 161.5500 161.5500 161.5500 0.0000 0.0000 0.0000 95  TYR A O   
465  C CB  . TYR A 95  ? 161.3957 161.3957 161.3957 0.0000 0.0000 0.0000 95  TYR A CB  
466  C CG  . TYR A 95  ? 161.2595 161.2595 161.2595 0.0000 0.0000 0.0000 95  TYR A CG  
467  C CD1 . TYR A 95  ? 161.2767 161.2767 161.2767 0.0000 0.0000 0.0000 95  TYR A CD1 
468  C CD2 . TYR A 95  ? 161.4522 161.4522 161.4522 0.0000 0.0000 0.0000 95  TYR A CD2 
469  C CE1 . TYR A 95  ? 161.1976 161.1976 161.1976 0.0000 0.0000 0.0000 95  TYR A CE1 
470  C CE2 . TYR A 95  ? 161.4840 161.4840 161.4840 0.0000 0.0000 0.0000 95  TYR A CE2 
471  C CZ  . TYR A 95  ? 161.2841 161.2841 161.2841 0.0000 0.0000 0.0000 95  TYR A CZ  
472  O OH  . TYR A 95  ? 161.5497 161.5497 161.5497 0.0000 0.0000 0.0000 95  TYR A OH  
473  N N   . PRO A 96  ? 160.9959 160.9959 160.9959 0.0000 0.0000 0.0000 96  PRO A N   
474  C CA  . PRO A 96  ? 161.0667 161.0667 161.0667 0.0000 0.0000 0.0000 96  PRO A CA  
475  C C   . PRO A 96  ? 160.9653 160.9653 160.9653 0.0000 0.0000 0.0000 96  PRO A C   
476  O O   . PRO A 96  ? 160.5257 160.5257 160.5257 0.0000 0.0000 0.0000 96  PRO A O   
477  C CB  . PRO A 96  ? 161.3695 161.3695 161.3695 0.0000 0.0000 0.0000 96  PRO A CB  
478  C CG  . PRO A 96  ? 161.4610 161.4610 161.4610 0.0000 0.0000 0.0000 96  PRO A CG  
479  C CD  . PRO A 96  ? 161.3651 161.3651 161.3651 0.0000 0.0000 0.0000 96  PRO A CD  
480  N N   . HIS A 97  ? 161.3343 161.3343 161.3343 0.0000 0.0000 0.0000 97  HIS A N   
481  C CA  . HIS A 97  ? 161.4096 161.4096 161.4096 0.0000 0.0000 0.0000 97  HIS A CA  
482  C C   . HIS A 97  ? 161.0290 161.0290 161.0290 0.0000 0.0000 0.0000 97  HIS A C   
483  O O   . HIS A 97  ? 160.3909 160.3909 160.3909 0.0000 0.0000 0.0000 97  HIS A O   
484  C CB  . HIS A 97  ? 161.4355 161.4355 161.4355 0.0000 0.0000 0.0000 97  HIS A CB  
485  C CG  . HIS A 97  ? 161.2302 161.2302 161.2302 0.0000 0.0000 0.0000 97  HIS A CG  
486  N ND1 . HIS A 97  ? 161.1506 161.1506 161.1506 0.0000 0.0000 0.0000 97  HIS A ND1 
487  C CD2 . HIS A 97  ? 161.3919 161.3919 161.3919 0.0000 0.0000 0.0000 97  HIS A CD2 
488  C CE1 . HIS A 97  ? 161.4601 161.4601 161.4601 0.0000 0.0000 0.0000 97  HIS A CE1 
489  N NE2 . HIS A 97  ? 161.5115 161.5115 161.5115 0.0000 0.0000 0.0000 97  HIS A NE2 
490  N N   . LYS A 98  ? 161.2087 161.2087 161.2087 0.0000 0.0000 0.0000 98  LYS A N   
491  C CA  . LYS A 98  ? 161.2761 161.2761 161.2761 0.0000 0.0000 0.0000 98  LYS A CA  
492  C C   . LYS A 98  ? 161.3153 161.3153 161.3153 0.0000 0.0000 0.0000 98  LYS A C   
493  O O   . LYS A 98  ? 161.4134 161.4134 161.4134 0.0000 0.0000 0.0000 98  LYS A O   
494  C CB  . LYS A 98  ? 161.3768 161.3768 161.3768 0.0000 0.0000 0.0000 98  LYS A CB  
495  C CG  . LYS A 98  ? 161.4124 161.4124 161.4124 0.0000 0.0000 0.0000 98  LYS A CG  
496  C CD  . LYS A 98  ? 161.4959 161.4959 161.4959 0.0000 0.0000 0.0000 98  LYS A CD  
497  C CE  . LYS A 98  ? 161.4395 161.4395 161.4395 0.0000 0.0000 0.0000 98  LYS A CE  
498  N NZ  . LYS A 98  ? 161.2307 161.2307 161.2307 0.0000 0.0000 0.0000 98  LYS A NZ  
499  N N   . PHE A 99  ? 161.3489 161.3489 161.3489 0.0000 0.0000 0.0000 99  PHE A N   
500  C CA  . PHE A 99  ? 161.3546 161.3546 161.3546 0.0000 0.0000 0.0000 99  PHE A CA  
501  C C   . PHE A 99  ? 161.4270 161.4270 161.4270 0.0000 0.0000 0.0000 99  PHE A C   
502  O O   . PHE A 99  ? 161.6476 161.6476 161.6476 0.0000 0.0000 0.0000 99  PHE A O   
503  C CB  . PHE A 99  ? 161.3681 161.3681 161.3681 0.0000 0.0000 0.0000 99  PHE A CB  
504  C CG  . PHE A 99  ? 161.3485 161.3485 161.3485 0.0000 0.0000 0.0000 99  PHE A CG  
505  C CD1 . PHE A 99  ? 161.4292 161.4292 161.4292 0.0000 0.0000 0.0000 99  PHE A CD1 
506  C CD2 . PHE A 99  ? 161.4679 161.4679 161.4679 0.0000 0.0000 0.0000 99  PHE A CD2 
507  C CE1 . PHE A 99  ? 161.4471 161.4471 161.4471 0.0000 0.0000 0.0000 99  PHE A CE1 
508  C CE2 . PHE A 99  ? 161.4489 161.4489 161.4489 0.0000 0.0000 0.0000 99  PHE A CE2 
509  C CZ  . PHE A 99  ? 161.4226 161.4226 161.4226 0.0000 0.0000 0.0000 99  PHE A CZ  
510  N N   . HIS A 100 ? 161.3032 161.3032 161.3032 0.0000 0.0000 0.0000 100 HIS A N   
511  C CA  . HIS A 100 ? 161.3946 161.3946 161.3946 0.0000 0.0000 0.0000 100 HIS A CA  
512  C C   . HIS A 100 ? 161.4336 161.4336 161.4336 0.0000 0.0000 0.0000 100 HIS A C   
513  O O   . HIS A 100 ? 161.5673 161.5673 161.5673 0.0000 0.0000 0.0000 100 HIS A O   
514  C CB  . HIS A 100 ? 161.3571 161.3571 161.3571 0.0000 0.0000 0.0000 100 HIS A CB  
515  C CG  . HIS A 100 ? 161.3662 161.3662 161.3662 0.0000 0.0000 0.0000 100 HIS A CG  
516  N ND1 . HIS A 100 ? 160.8163 160.8163 160.8163 0.0000 0.0000 0.0000 100 HIS A ND1 
517  C CD2 . HIS A 100 ? 161.4378 161.4378 161.4378 0.0000 0.0000 0.0000 100 HIS A CD2 
518  C CE1 . HIS A 100 ? 160.5235 160.5235 160.5235 0.0000 0.0000 0.0000 100 HIS A CE1 
519  N NE2 . HIS A 100 ? 161.1080 161.1080 161.1080 0.0000 0.0000 0.0000 100 HIS A NE2 
520  N N   . VAL A 101 ? 161.3459 161.3459 161.3459 0.0000 0.0000 0.0000 101 VAL A N   
521  C CA  . VAL A 101 ? 161.0365 161.0365 161.0365 0.0000 0.0000 0.0000 101 VAL A CA  
522  C C   . VAL A 101 ? 160.5854 160.5854 160.5854 0.0000 0.0000 0.0000 101 VAL A C   
523  O O   . VAL A 101 ? 159.9232 159.9232 159.9232 0.0000 0.0000 0.0000 101 VAL A O   
524  C CB  . VAL A 101 ? 159.9683 159.9683 159.9683 0.0000 0.0000 0.0000 101 VAL A CB  
525  C CG1 . VAL A 101 ? 159.6035 159.6035 159.6035 0.0000 0.0000 0.0000 101 VAL A CG1 
526  C CG2 . VAL A 101 ? 160.8617 160.8617 160.8617 0.0000 0.0000 0.0000 101 VAL A CG2 
527  N N   . ASP A 102 ? 161.0878 161.0878 161.0878 0.0000 0.0000 0.0000 102 ASP A N   
528  C CA  . ASP A 102 ? 161.0431 161.0431 161.0431 0.0000 0.0000 0.0000 102 ASP A CA  
529  C C   . ASP A 102 ? 160.7773 160.7773 160.7773 0.0000 0.0000 0.0000 102 ASP A C   
530  O O   . ASP A 102 ? 160.7503 160.7503 160.7503 0.0000 0.0000 0.0000 102 ASP A O   
531  C CB  . ASP A 102 ? 161.4316 161.4316 161.4316 0.0000 0.0000 0.0000 102 ASP A CB  
532  C CG  . ASP A 102 ? 161.5554 161.5554 161.5554 0.0000 0.0000 0.0000 102 ASP A CG  
533  O OD1 . ASP A 102 ? 161.7059 161.7059 161.7059 0.0000 0.0000 0.0000 102 ASP A OD1 
534  O OD2 . ASP A 102 ? 161.6249 161.6249 161.6249 0.0000 0.0000 0.0000 102 ASP A OD2 
535  N N   . ILE A 103 ? 160.8434 160.8434 160.8434 0.0000 0.0000 0.0000 103 ILE A N   
536  C CA  . ILE A 103 ? 160.5705 160.5705 160.5705 0.0000 0.0000 0.0000 103 ILE A CA  
537  C C   . ILE A 103 ? 160.6146 160.6146 160.6146 0.0000 0.0000 0.0000 103 ILE A C   
538  O O   . ILE A 103 ? 161.0111 161.0111 161.0111 0.0000 0.0000 0.0000 103 ILE A O   
539  C CB  . ILE A 103 ? 161.2825 161.2825 161.2825 0.0000 0.0000 0.0000 103 ILE A CB  
540  C CG1 . ILE A 103 ? 161.4165 161.4165 161.4165 0.0000 0.0000 0.0000 103 ILE A CG1 
541  C CG2 . ILE A 103 ? 161.5358 161.5358 161.5358 0.0000 0.0000 0.0000 103 ILE A CG2 
542  C CD1 . ILE A 103 ? 161.4637 161.4637 161.4637 0.0000 0.0000 0.0000 103 ILE A CD1 
543  N N   . SER A 104 ? 160.0964 160.0964 160.0964 0.0000 0.0000 0.0000 104 SER A N   
544  C CA  . SER A 104 ? 160.5236 160.5236 160.5236 0.0000 0.0000 0.0000 104 SER A CA  
545  C C   . SER A 104 ? 161.4774 161.4774 161.4774 0.0000 0.0000 0.0000 104 SER A C   
546  O O   . SER A 104 ? 161.7295 161.7295 161.7295 0.0000 0.0000 0.0000 104 SER A O   
547  C CB  . SER A 104 ? 159.9864 159.9864 159.9864 0.0000 0.0000 0.0000 104 SER A CB  
548  O OG  . SER A 104 ? 160.9163 160.9163 160.9163 0.0000 0.0000 0.0000 104 SER A OG  
549  N N   . LEU A 105 ? 161.4412 161.4412 161.4412 0.0000 0.0000 0.0000 105 LEU A N   
550  C CA  . LEU A 105 ? 161.3951 161.3951 161.3951 0.0000 0.0000 0.0000 105 LEU A CA  
551  C C   . LEU A 105 ? 161.3879 161.3879 161.3879 0.0000 0.0000 0.0000 105 LEU A C   
552  O O   . LEU A 105 ? 161.5031 161.5031 161.5031 0.0000 0.0000 0.0000 105 LEU A O   
553  C CB  . LEU A 105 ? 161.4714 161.4714 161.4714 0.0000 0.0000 0.0000 105 LEU A CB  
554  C CG  . LEU A 105 ? 161.4694 161.4694 161.4694 0.0000 0.0000 0.0000 105 LEU A CG  
555  C CD1 . LEU A 105 ? 161.3743 161.3743 161.3743 0.0000 0.0000 0.0000 105 LEU A CD1 
556  C CD2 . LEU A 105 ? 161.6089 161.6089 161.6089 0.0000 0.0000 0.0000 105 LEU A CD2 
557  N N   . THR A 106 ? 161.3609 161.3609 161.3609 0.0000 0.0000 0.0000 106 THR A N   
558  C CA  . THR A 106 ? 161.2925 161.2925 161.2925 0.0000 0.0000 0.0000 106 THR A CA  
559  C C   . THR A 106 ? 161.3651 161.3651 161.3651 0.0000 0.0000 0.0000 106 THR A C   
560  O O   . THR A 106 ? 161.4940 161.4940 161.4940 0.0000 0.0000 0.0000 106 THR A O   
561  C CB  . THR A 106 ? 161.3068 161.3068 161.3068 0.0000 0.0000 0.0000 106 THR A CB  
562  O OG1 . THR A 106 ? 161.2086 161.2086 161.2086 0.0000 0.0000 0.0000 106 THR A OG1 
563  C CG2 . THR A 106 ? 161.4562 161.4562 161.4562 0.0000 0.0000 0.0000 106 THR A CG2 
564  N N   . ASP A 107 ? 161.4009 161.4009 161.4009 0.0000 0.0000 0.0000 107 ASP A N   
565  C CA  . ASP A 107 ? 161.3345 161.3345 161.3345 0.0000 0.0000 0.0000 107 ASP A CA  
566  C C   . ASP A 107 ? 161.3229 161.3229 161.3229 0.0000 0.0000 0.0000 107 ASP A C   
567  O O   . ASP A 107 ? 161.6621 161.6621 161.6621 0.0000 0.0000 0.0000 107 ASP A O   
568  C CB  . ASP A 107 ? 161.4597 161.4597 161.4597 0.0000 0.0000 0.0000 107 ASP A CB  
569  C CG  . ASP A 107 ? 161.0787 161.0787 161.0787 0.0000 0.0000 0.0000 107 ASP A CG  
570  O OD1 . ASP A 107 ? 160.5155 160.5155 160.5155 0.0000 0.0000 0.0000 107 ASP A OD1 
571  O OD2 . ASP A 107 ? 160.6350 160.6350 160.6350 0.0000 0.0000 0.0000 107 ASP A OD2 
572  N N   . PHE A 108 ? 161.2680 161.2680 161.2680 0.0000 0.0000 0.0000 108 PHE A N   
573  C CA  . PHE A 108 ? 161.4090 161.4090 161.4090 0.0000 0.0000 0.0000 108 PHE A CA  
574  C C   . PHE A 108 ? 161.5845 161.5845 161.5845 0.0000 0.0000 0.0000 108 PHE A C   
575  O O   . PHE A 108 ? 161.7581 161.7581 161.7581 0.0000 0.0000 0.0000 108 PHE A O   
576  C CB  . PHE A 108 ? 161.3559 161.3559 161.3559 0.0000 0.0000 0.0000 108 PHE A CB  
577  C CG  . PHE A 108 ? 161.2729 161.2729 161.2729 0.0000 0.0000 0.0000 108 PHE A CG  
578  C CD1 . PHE A 108 ? 161.3413 161.3413 161.3413 0.0000 0.0000 0.0000 108 PHE A CD1 
579  C CD2 . PHE A 108 ? 161.3508 161.3508 161.3508 0.0000 0.0000 0.0000 108 PHE A CD2 
580  C CE1 . PHE A 108 ? 161.4072 161.4072 161.4072 0.0000 0.0000 0.0000 108 PHE A CE1 
581  C CE2 . PHE A 108 ? 161.4890 161.4890 161.4890 0.0000 0.0000 0.0000 108 PHE A CE2 
582  C CZ  . PHE A 108 ? 161.5557 161.5557 161.5557 0.0000 0.0000 0.0000 108 PHE A CZ  
583  N N   . ILE A 109 ? 161.5349 161.5349 161.5349 0.0000 0.0000 0.0000 109 ILE A N   
584  C CA  . ILE A 109 ? 161.3063 161.3063 161.3063 0.0000 0.0000 0.0000 109 ILE A CA  
585  C C   . ILE A 109 ? 161.3429 161.3429 161.3429 0.0000 0.0000 0.0000 109 ILE A C   
586  O O   . ILE A 109 ? 161.4974 161.4974 161.4974 0.0000 0.0000 0.0000 109 ILE A O   
587  C CB  . ILE A 109 ? 161.1715 161.1715 161.1715 0.0000 0.0000 0.0000 109 ILE A CB  
588  C CG1 . ILE A 109 ? 161.2806 161.2806 161.2806 0.0000 0.0000 0.0000 109 ILE A CG1 
589  C CG2 . ILE A 109 ? 161.3969 161.3969 161.3969 0.0000 0.0000 0.0000 109 ILE A CG2 
590  C CD1 . ILE A 109 ? 161.6431 161.6431 161.6431 0.0000 0.0000 0.0000 109 ILE A CD1 
591  N N   . GLN A 110 ? 161.3391 161.3391 161.3391 0.0000 0.0000 0.0000 110 GLN A N   
592  C CA  . GLN A 110 ? 161.2567 161.2567 161.2567 0.0000 0.0000 0.0000 110 GLN A CA  
593  C C   . GLN A 110 ? 161.2839 161.2839 161.2839 0.0000 0.0000 0.0000 110 GLN A C   
594  O O   . GLN A 110 ? 161.3932 161.3932 161.3932 0.0000 0.0000 0.0000 110 GLN A O   
595  C CB  . GLN A 110 ? 161.3441 161.3441 161.3441 0.0000 0.0000 0.0000 110 GLN A CB  
596  C CG  . GLN A 110 ? 161.4899 161.4899 161.4899 0.0000 0.0000 0.0000 110 GLN A CG  
597  C CD  . GLN A 110 ? 161.5096 161.5096 161.5096 0.0000 0.0000 0.0000 110 GLN A CD  
598  O OE1 . GLN A 110 ? 161.4472 161.4472 161.4472 0.0000 0.0000 0.0000 110 GLN A OE1 
599  N NE2 . GLN A 110 ? 161.5486 161.5486 161.5486 0.0000 0.0000 0.0000 110 GLN A NE2 
600  N N   . LYS A 111 ? 161.3498 161.3498 161.3498 0.0000 0.0000 0.0000 111 LYS A N   
601  C CA  . LYS A 111 ? 161.3623 161.3623 161.3623 0.0000 0.0000 0.0000 111 LYS A CA  
602  C C   . LYS A 111 ? 161.3485 161.3485 161.3485 0.0000 0.0000 0.0000 111 LYS A C   
603  O O   . LYS A 111 ? 161.4310 161.4310 161.4310 0.0000 0.0000 0.0000 111 LYS A O   
604  C CB  . LYS A 111 ? 161.4100 161.4100 161.4100 0.0000 0.0000 0.0000 111 LYS A CB  
605  C CG  . LYS A 111 ? 161.4082 161.4082 161.4082 0.0000 0.0000 0.0000 111 LYS A CG  
606  C CD  . LYS A 111 ? 161.3733 161.3733 161.3733 0.0000 0.0000 0.0000 111 LYS A CD  
607  C CE  . LYS A 111 ? 161.4038 161.4038 161.4038 0.0000 0.0000 0.0000 111 LYS A CE  
608  N NZ  . LYS A 111 ? 161.5133 161.5133 161.5133 0.0000 0.0000 0.0000 111 LYS A NZ  
609  N N   . TYR A 112 ? 161.3049 161.3049 161.3049 0.0000 0.0000 0.0000 112 TYR A N   
610  C CA  . TYR A 112 ? 161.3434 161.3434 161.3434 0.0000 0.0000 0.0000 112 TYR A CA  
611  C C   . TYR A 112 ? 161.3727 161.3727 161.3727 0.0000 0.0000 0.0000 112 TYR A C   
612  O O   . TYR A 112 ? 161.4509 161.4509 161.4509 0.0000 0.0000 0.0000 112 TYR A O   
613  C CB  . TYR A 112 ? 161.5043 161.5043 161.5043 0.0000 0.0000 0.0000 112 TYR A CB  
614  C CG  . TYR A 112 ? 161.3298 161.3298 161.3298 0.0000 0.0000 0.0000 112 TYR A CG  
615  C CD1 . TYR A 112 ? 161.3597 161.3597 161.3597 0.0000 0.0000 0.0000 112 TYR A CD1 
616  C CD2 . TYR A 112 ? 161.3885 161.3885 161.3885 0.0000 0.0000 0.0000 112 TYR A CD2 
617  C CE1 . TYR A 112 ? 161.3998 161.3998 161.3998 0.0000 0.0000 0.0000 112 TYR A CE1 
618  C CE2 . TYR A 112 ? 161.4112 161.4112 161.4112 0.0000 0.0000 0.0000 112 TYR A CE2 
619  C CZ  . TYR A 112 ? 161.4146 161.4146 161.4146 0.0000 0.0000 0.0000 112 TYR A CZ  
620  O OH  . TYR A 112 ? 161.5987 161.5987 161.5987 0.0000 0.0000 0.0000 112 TYR A OH  
621  N N   . SER A 113 ? 161.3381 161.3381 161.3381 0.0000 0.0000 0.0000 113 SER A N   
622  C CA  . SER A 113 ? 161.2783 161.2783 161.2783 0.0000 0.0000 0.0000 113 SER A CA  
623  C C   . SER A 113 ? 161.3468 161.3468 161.3468 0.0000 0.0000 0.0000 113 SER A C   
624  O O   . SER A 113 ? 161.5503 161.5503 161.5503 0.0000 0.0000 0.0000 113 SER A O   
625  C CB  . SER A 113 ? 161.4353 161.4353 161.4353 0.0000 0.0000 0.0000 113 SER A CB  
626  O OG  . SER A 113 ? 161.5355 161.5355 161.5355 0.0000 0.0000 0.0000 113 SER A OG  
627  N N   . HIS A 114 ? 161.3654 161.3654 161.3654 0.0000 0.0000 0.0000 114 HIS A N   
628  C CA  . HIS A 114 ? 161.4699 161.4699 161.4699 0.0000 0.0000 0.0000 114 HIS A CA  
629  C C   . HIS A 114 ? 161.4509 161.4509 161.4509 0.0000 0.0000 0.0000 114 HIS A C   
630  O O   . HIS A 114 ? 161.5532 161.5532 161.5532 0.0000 0.0000 0.0000 114 HIS A O   
631  C CB  . HIS A 114 ? 161.5251 161.5251 161.5251 0.0000 0.0000 0.0000 114 HIS A CB  
632  C CG  . HIS A 114 ? 161.4093 161.4093 161.4093 0.0000 0.0000 0.0000 114 HIS A CG  
633  N ND1 . HIS A 114 ? 161.3966 161.3966 161.3966 0.0000 0.0000 0.0000 114 HIS A ND1 
634  C CD2 . HIS A 114 ? 161.4049 161.4049 161.4049 0.0000 0.0000 0.0000 114 HIS A CD2 
635  C CE1 . HIS A 114 ? 161.3853 161.3853 161.3853 0.0000 0.0000 0.0000 114 HIS A CE1 
636  N NE2 . HIS A 114 ? 161.3812 161.3812 161.3812 0.0000 0.0000 0.0000 114 HIS A NE2 
637  N N   . LEU A 115 ? 161.5174 161.5174 161.5174 0.0000 0.0000 0.0000 115 LEU A N   
638  C CA  . LEU A 115 ? 161.6092 161.6092 161.6092 0.0000 0.0000 0.0000 115 LEU A CA  
639  C C   . LEU A 115 ? 161.6890 161.6890 161.6890 0.0000 0.0000 0.0000 115 LEU A C   
640  O O   . LEU A 115 ? 161.6109 161.6109 161.6109 0.0000 0.0000 0.0000 115 LEU A O   
641  C CB  . LEU A 115 ? 161.5848 161.5848 161.5848 0.0000 0.0000 0.0000 115 LEU A CB  
642  C CG  . LEU A 115 ? 161.3875 161.3875 161.3875 0.0000 0.0000 0.0000 115 LEU A CG  
643  C CD1 . LEU A 115 ? 161.4744 161.4744 161.4744 0.0000 0.0000 0.0000 115 LEU A CD1 
644  C CD2 . LEU A 115 ? 161.4768 161.4768 161.4768 0.0000 0.0000 0.0000 115 LEU A CD2 
645  N N   . GLN A 116 ? 163.5653 163.5653 163.5653 0.0000 0.0000 0.0000 116 GLN A N   
646  C CA  . GLN A 116 ? 163.5968 163.5968 163.5968 0.0000 0.0000 0.0000 116 GLN A CA  
647  C C   . GLN A 116 ? 163.7169 163.7169 163.7169 0.0000 0.0000 0.0000 116 GLN A C   
648  O O   . GLN A 116 ? 163.8968 163.8968 163.8968 0.0000 0.0000 0.0000 116 GLN A O   
649  C CB  . GLN A 116 ? 163.6434 163.6434 163.6434 0.0000 0.0000 0.0000 116 GLN A CB  
650  C CG  . GLN A 116 ? 163.5841 163.5841 163.5841 0.0000 0.0000 0.0000 116 GLN A CG  
651  C CD  . GLN A 116 ? 163.5122 163.5122 163.5122 0.0000 0.0000 0.0000 116 GLN A CD  
652  O OE1 . GLN A 116 ? 163.5869 163.5869 163.5869 0.0000 0.0000 0.0000 116 GLN A OE1 
653  N NE2 . GLN A 116 ? 163.4911 163.4911 163.4911 0.0000 0.0000 0.0000 116 GLN A NE2 
654  N N   . PRO A 117 ? 166.0313 166.0313 166.0313 0.0000 0.0000 0.0000 117 PRO A N   
655  C CA  . PRO A 117 ? 166.1017 166.1017 166.1017 0.0000 0.0000 0.0000 117 PRO A CA  
656  C C   . PRO A 117 ? 166.1285 166.1285 166.1285 0.0000 0.0000 0.0000 117 PRO A C   
657  O O   . PRO A 117 ? 166.2287 166.2287 166.2287 0.0000 0.0000 0.0000 117 PRO A O   
658  C CB  . PRO A 117 ? 166.1943 166.1943 166.1943 0.0000 0.0000 0.0000 117 PRO A CB  
659  C CG  . PRO A 117 ? 166.2289 166.2289 166.2289 0.0000 0.0000 0.0000 117 PRO A CG  
660  C CD  . PRO A 117 ? 166.1613 166.1613 166.1613 0.0000 0.0000 0.0000 117 PRO A CD  
661  N N   . GLY A 118 ? 161.8543 161.8543 161.8543 0.0000 0.0000 0.0000 118 GLY A N   
662  C CA  . GLY A 118 ? 161.7540 161.7540 161.7540 0.0000 0.0000 0.0000 118 GLY A CA  
663  C C   . GLY A 118 ? 161.7342 161.7342 161.7342 0.0000 0.0000 0.0000 118 GLY A C   
664  O O   . GLY A 118 ? 161.6853 161.6853 161.6853 0.0000 0.0000 0.0000 118 GLY A O   
665  N N   . ASP A 119 ? 171.4451 171.4451 171.4451 0.0000 0.0000 0.0000 119 ASP A N   
666  C CA  . ASP A 119 ? 171.7391 171.7391 171.7391 0.0000 0.0000 0.0000 119 ASP A CA  
667  C C   . ASP A 119 ? 171.5588 171.5588 171.5588 0.0000 0.0000 0.0000 119 ASP A C   
668  O O   . ASP A 119 ? 171.6863 171.6863 171.6863 0.0000 0.0000 0.0000 119 ASP A O   
669  C CB  . ASP A 119 ? 171.9157 171.9157 171.9157 0.0000 0.0000 0.0000 119 ASP A CB  
670  C CG  . ASP A 119 ? 172.1022 172.1022 172.1022 0.0000 0.0000 0.0000 119 ASP A CG  
671  O OD1 . ASP A 119 ? 172.2524 172.2524 172.2524 0.0000 0.0000 0.0000 119 ASP A OD1 
672  O OD2 . ASP A 119 ? 172.0446 172.0446 172.0446 0.0000 0.0000 0.0000 119 ASP A OD2 
673  N N   . HIS A 120 ? 161.6936 161.6936 161.6936 0.0000 0.0000 0.0000 120 HIS A N   
674  C CA  . HIS A 120 ? 161.4925 161.4925 161.4925 0.0000 0.0000 0.0000 120 HIS A CA  
675  C C   . HIS A 120 ? 161.5251 161.5251 161.5251 0.0000 0.0000 0.0000 120 HIS A C   
676  O O   . HIS A 120 ? 161.6997 161.6997 161.6997 0.0000 0.0000 0.0000 120 HIS A O   
677  C CB  . HIS A 120 ? 161.5652 161.5652 161.5652 0.0000 0.0000 0.0000 120 HIS A CB  
678  C CG  . HIS A 120 ? 161.5195 161.5195 161.5195 0.0000 0.0000 0.0000 120 HIS A CG  
679  N ND1 . HIS A 120 ? 161.4454 161.4454 161.4454 0.0000 0.0000 0.0000 120 HIS A ND1 
680  C CD2 . HIS A 120 ? 161.6122 161.6122 161.6122 0.0000 0.0000 0.0000 120 HIS A CD2 
681  C CE1 . HIS A 120 ? 161.4509 161.4509 161.4509 0.0000 0.0000 0.0000 120 HIS A CE1 
682  N NE2 . HIS A 120 ? 161.5351 161.5351 161.5351 0.0000 0.0000 0.0000 120 HIS A NE2 
683  N N   . LEU A 121 ? 161.4375 161.4375 161.4375 0.0000 0.0000 0.0000 121 LEU A N   
684  C CA  . LEU A 121 ? 161.5150 161.5150 161.5150 0.0000 0.0000 0.0000 121 LEU A CA  
685  C C   . LEU A 121 ? 161.9447 161.9447 161.9447 0.0000 0.0000 0.0000 121 LEU A C   
686  O O   . LEU A 121 ? 161.9657 161.9657 161.9657 0.0000 0.0000 0.0000 121 LEU A O   
687  C CB  . LEU A 121 ? 161.4467 161.4467 161.4467 0.0000 0.0000 0.0000 121 LEU A CB  
688  C CG  . LEU A 121 ? 161.3957 161.3957 161.3957 0.0000 0.0000 0.0000 121 LEU A CG  
689  C CD1 . LEU A 121 ? 161.3901 161.3901 161.3901 0.0000 0.0000 0.0000 121 LEU A CD1 
690  C CD2 . LEU A 121 ? 161.5378 161.5378 161.5378 0.0000 0.0000 0.0000 121 LEU A CD2 
691  N N   . THR A 122 ? 172.3632 172.3632 172.3632 0.0000 0.0000 0.0000 122 THR A N   
692  C CA  . THR A 122 ? 172.6516 172.6516 172.6516 0.0000 0.0000 0.0000 122 THR A CA  
693  C C   . THR A 122 ? 172.9327 172.9327 172.9327 0.0000 0.0000 0.0000 122 THR A C   
694  O O   . THR A 122 ? 173.0695 173.0695 173.0695 0.0000 0.0000 0.0000 122 THR A O   
695  C CB  . THR A 122 ? 172.9736 172.9736 172.9736 0.0000 0.0000 0.0000 122 THR A CB  
696  O OG1 . THR A 122 ? 173.1149 173.1149 173.1149 0.0000 0.0000 0.0000 122 THR A OG1 
697  C CG2 . THR A 122 ? 172.9054 172.9054 172.9054 0.0000 0.0000 0.0000 122 THR A CG2 
698  N N   . ASP A 123 ? 176.0585 176.0585 176.0585 0.0000 0.0000 0.0000 123 ASP A N   
699  C CA  . ASP A 123 ? 176.2076 176.2076 176.2076 0.0000 0.0000 0.0000 123 ASP A CA  
700  C C   . ASP A 123 ? 175.9457 175.9457 175.9457 0.0000 0.0000 0.0000 123 ASP A C   
701  O O   . ASP A 123 ? 176.1706 176.1706 176.1706 0.0000 0.0000 0.0000 123 ASP A O   
702  C CB  . ASP A 123 ? 176.3797 176.3797 176.3797 0.0000 0.0000 0.0000 123 ASP A CB  
703  C CG  . ASP A 123 ? 176.3925 176.3925 176.3925 0.0000 0.0000 0.0000 123 ASP A CG  
704  O OD1 . ASP A 123 ? 176.3628 176.3628 176.3628 0.0000 0.0000 0.0000 123 ASP A OD1 
705  O OD2 . ASP A 123 ? 176.5264 176.5264 176.5264 0.0000 0.0000 0.0000 123 ASP A OD2 
706  N N   . ILE A 124 ? 164.2659 164.2659 164.2659 0.0000 0.0000 0.0000 124 ILE A N   
707  C CA  . ILE A 124 ? 163.7894 163.7894 163.7894 0.0000 0.0000 0.0000 124 ILE A CA  
708  C C   . ILE A 124 ? 163.6178 163.6178 163.6178 0.0000 0.0000 0.0000 124 ILE A C   
709  O O   . ILE A 124 ? 163.8366 163.8366 163.8366 0.0000 0.0000 0.0000 124 ILE A O   
710  C CB  . ILE A 124 ? 163.6342 163.6342 163.6342 0.0000 0.0000 0.0000 124 ILE A CB  
711  C CG1 . ILE A 124 ? 163.7434 163.7434 163.7434 0.0000 0.0000 0.0000 124 ILE A CG1 
712  C CG2 . ILE A 124 ? 163.5281 163.5281 163.5281 0.0000 0.0000 0.0000 124 ILE A CG2 
713  C CD1 . ILE A 124 ? 163.7484 163.7484 163.7484 0.0000 0.0000 0.0000 124 ILE A CD1 
714  N N   . THR A 125 ? 161.4225 161.4225 161.4225 0.0000 0.0000 0.0000 125 THR A N   
715  C CA  . THR A 125 ? 161.3720 161.3720 161.3720 0.0000 0.0000 0.0000 125 THR A CA  
716  C C   . THR A 125 ? 161.3195 161.3195 161.3195 0.0000 0.0000 0.0000 125 THR A C   
717  O O   . THR A 125 ? 161.4825 161.4825 161.4825 0.0000 0.0000 0.0000 125 THR A O   
718  C CB  . THR A 125 ? 161.4562 161.4562 161.4562 0.0000 0.0000 0.0000 125 THR A CB  
719  O OG1 . THR A 125 ? 161.6246 161.6246 161.6246 0.0000 0.0000 0.0000 125 THR A OG1 
720  C CG2 . THR A 125 ? 161.5458 161.5458 161.5458 0.0000 0.0000 0.0000 125 THR A CG2 
721  N N   . LEU A 126 ? 161.2044 161.2044 161.2044 0.0000 0.0000 0.0000 126 LEU A N   
722  C CA  . LEU A 126 ? 161.2052 161.2052 161.2052 0.0000 0.0000 0.0000 126 LEU A CA  
723  C C   . LEU A 126 ? 161.2772 161.2772 161.2772 0.0000 0.0000 0.0000 126 LEU A C   
724  O O   . LEU A 126 ? 161.4723 161.4723 161.4723 0.0000 0.0000 0.0000 126 LEU A O   
725  C CB  . LEU A 126 ? 161.3820 161.3820 161.3820 0.0000 0.0000 0.0000 126 LEU A CB  
726  C CG  . LEU A 126 ? 161.4820 161.4820 161.4820 0.0000 0.0000 0.0000 126 LEU A CG  
727  C CD1 . LEU A 126 ? 161.5117 161.5117 161.5117 0.0000 0.0000 0.0000 126 LEU A CD1 
728  C CD2 . LEU A 126 ? 161.5524 161.5524 161.5524 0.0000 0.0000 0.0000 126 LEU A CD2 
729  N N   . LYS A 127 ? 161.3689 161.3689 161.3689 0.0000 0.0000 0.0000 127 LYS A N   
730  C CA  . LYS A 127 ? 161.3689 161.3689 161.3689 0.0000 0.0000 0.0000 127 LYS A CA  
731  C C   . LYS A 127 ? 161.2568 161.2568 161.2568 0.0000 0.0000 0.0000 127 LYS A C   
732  O O   . LYS A 127 ? 161.4720 161.4720 161.4720 0.0000 0.0000 0.0000 127 LYS A O   
733  C CB  . LYS A 127 ? 161.4658 161.4658 161.4658 0.0000 0.0000 0.0000 127 LYS A CB  
734  C CG  . LYS A 127 ? 161.3854 161.3854 161.3854 0.0000 0.0000 0.0000 127 LYS A CG  
735  C CD  . LYS A 127 ? 161.3393 161.3393 161.3393 0.0000 0.0000 0.0000 127 LYS A CD  
736  C CE  . LYS A 127 ? 161.3736 161.3736 161.3736 0.0000 0.0000 0.0000 127 LYS A CE  
737  N NZ  . LYS A 127 ? 161.5316 161.5316 161.5316 0.0000 0.0000 0.0000 127 LYS A NZ  
738  N N   . VAL A 128 ? 161.1379 161.1379 161.1379 0.0000 0.0000 0.0000 128 VAL A N   
739  C CA  . VAL A 128 ? 161.1853 161.1853 161.1853 0.0000 0.0000 0.0000 128 VAL A CA  
740  C C   . VAL A 128 ? 161.3314 161.3314 161.3314 0.0000 0.0000 0.0000 128 VAL A C   
741  O O   . VAL A 128 ? 161.5708 161.5708 161.5708 0.0000 0.0000 0.0000 128 VAL A O   
742  C CB  . VAL A 128 ? 161.2478 161.2478 161.2478 0.0000 0.0000 0.0000 128 VAL A CB  
743  C CG1 . VAL A 128 ? 161.4709 161.4709 161.4709 0.0000 0.0000 0.0000 128 VAL A CG1 
744  C CG2 . VAL A 128 ? 161.3591 161.3591 161.3591 0.0000 0.0000 0.0000 128 VAL A CG2 
745  N N   . ALA A 129 ? 161.3104 161.3104 161.3104 0.0000 0.0000 0.0000 129 ALA A N   
746  C CA  . ALA A 129 ? 161.3487 161.3487 161.3487 0.0000 0.0000 0.0000 129 ALA A CA  
747  C C   . ALA A 129 ? 161.3239 161.3239 161.3239 0.0000 0.0000 0.0000 129 ALA A C   
748  O O   . ALA A 129 ? 161.4277 161.4277 161.4277 0.0000 0.0000 0.0000 129 ALA A O   
749  C CB  . ALA A 129 ? 161.5450 161.5450 161.5450 0.0000 0.0000 0.0000 129 ALA A CB  
750  N N   . GLY A 130 ? 161.3596 161.3596 161.3596 0.0000 0.0000 0.0000 130 GLY A N   
751  C CA  . GLY A 130 ? 161.2704 161.2704 161.2704 0.0000 0.0000 0.0000 130 GLY A CA  
752  C C   . GLY A 130 ? 161.1662 161.1662 161.1662 0.0000 0.0000 0.0000 130 GLY A C   
753  O O   . GLY A 130 ? 161.5217 161.5217 161.5217 0.0000 0.0000 0.0000 130 GLY A O   
754  N N   . ARG A 131 ? 161.0258 161.0258 161.0258 0.0000 0.0000 0.0000 131 ARG A N   
755  C CA  . ARG A 131 ? 161.1528 161.1528 161.1528 0.0000 0.0000 0.0000 131 ARG A CA  
756  C C   . ARG A 131 ? 161.2195 161.2195 161.2195 0.0000 0.0000 0.0000 131 ARG A C   
757  O O   . ARG A 131 ? 161.7217 161.7217 161.7217 0.0000 0.0000 0.0000 131 ARG A O   
758  C CB  . ARG A 131 ? 161.3152 161.3152 161.3152 0.0000 0.0000 0.0000 131 ARG A CB  
759  C CG  . ARG A 131 ? 161.4633 161.4633 161.4633 0.0000 0.0000 0.0000 131 ARG A CG  
760  C CD  . ARG A 131 ? 161.2702 161.2702 161.2702 0.0000 0.0000 0.0000 131 ARG A CD  
761  N NE  . ARG A 131 ? 161.0298 161.0298 161.0298 0.0000 0.0000 0.0000 131 ARG A NE  
762  C CZ  . ARG A 131 ? 160.4620 160.4620 160.4620 0.0000 0.0000 0.0000 131 ARG A CZ  
763  N NH1 . ARG A 131 ? 160.3366 160.3366 160.3366 0.0000 0.0000 0.0000 131 ARG A NH1 
764  N NH2 . ARG A 131 ? 160.1816 160.1816 160.1816 0.0000 0.0000 0.0000 131 ARG A NH2 
765  N N   . ILE A 132 ? 161.1223 161.1223 161.1223 0.0000 0.0000 0.0000 132 ILE A N   
766  C CA  . ILE A 132 ? 161.0897 161.0897 161.0897 0.0000 0.0000 0.0000 132 ILE A CA  
767  C C   . ILE A 132 ? 161.1742 161.1742 161.1742 0.0000 0.0000 0.0000 132 ILE A C   
768  O O   . ILE A 132 ? 161.4304 161.4304 161.4304 0.0000 0.0000 0.0000 132 ILE A O   
769  C CB  . ILE A 132 ? 161.2910 161.2910 161.2910 0.0000 0.0000 0.0000 132 ILE A CB  
770  C CG1 . ILE A 132 ? 161.5709 161.5709 161.5709 0.0000 0.0000 0.0000 132 ILE A CG1 
771  C CG2 . ILE A 132 ? 161.5360 161.5360 161.5360 0.0000 0.0000 0.0000 132 ILE A CG2 
772  C CD1 . ILE A 132 ? 161.7850 161.7850 161.7850 0.0000 0.0000 0.0000 132 ILE A CD1 
773  N N   . HIS A 133 ? 161.2159 161.2159 161.2159 0.0000 0.0000 0.0000 133 HIS A N   
774  C CA  . HIS A 133 ? 161.2701 161.2701 161.2701 0.0000 0.0000 0.0000 133 HIS A CA  
775  C C   . HIS A 133 ? 161.3264 161.3264 161.3264 0.0000 0.0000 0.0000 133 HIS A C   
776  O O   . HIS A 133 ? 161.5242 161.5242 161.5242 0.0000 0.0000 0.0000 133 HIS A O   
777  C CB  . HIS A 133 ? 161.4292 161.4292 161.4292 0.0000 0.0000 0.0000 133 HIS A CB  
778  C CG  . HIS A 133 ? 161.3026 161.3026 161.3026 0.0000 0.0000 0.0000 133 HIS A CG  
779  N ND1 . HIS A 133 ? 161.3971 161.3971 161.3971 0.0000 0.0000 0.0000 133 HIS A ND1 
780  C CD2 . HIS A 133 ? 161.3830 161.3830 161.3830 0.0000 0.0000 0.0000 133 HIS A CD2 
781  C CE1 . HIS A 133 ? 161.4434 161.4434 161.4434 0.0000 0.0000 0.0000 133 HIS A CE1 
782  N NE2 . HIS A 133 ? 161.4652 161.4652 161.4652 0.0000 0.0000 0.0000 133 HIS A NE2 
783  N N   . ALA A 134 ? 161.1374 161.1374 161.1374 0.0000 0.0000 0.0000 134 ALA A N   
784  C CA  . ALA A 134 ? 161.1190 161.1190 161.1190 0.0000 0.0000 0.0000 134 ALA A CA  
785  C C   . ALA A 134 ? 161.2088 161.2088 161.2088 0.0000 0.0000 0.0000 134 ALA A C   
786  O O   . ALA A 134 ? 161.2707 161.2707 161.2707 0.0000 0.0000 0.0000 134 ALA A O   
787  C CB  . ALA A 134 ? 160.8162 160.8162 160.8162 0.0000 0.0000 0.0000 134 ALA A CB  
788  N N   . LYS A 135 ? 161.3551 161.3551 161.3551 0.0000 0.0000 0.0000 135 LYS A N   
789  C CA  . LYS A 135 ? 161.4096 161.4096 161.4096 0.0000 0.0000 0.0000 135 LYS A CA  
790  C C   . LYS A 135 ? 161.3097 161.3097 161.3097 0.0000 0.0000 0.0000 135 LYS A C   
791  O O   . LYS A 135 ? 161.3749 161.3749 161.3749 0.0000 0.0000 0.0000 135 LYS A O   
792  C CB  . LYS A 135 ? 161.5229 161.5229 161.5229 0.0000 0.0000 0.0000 135 LYS A CB  
793  C CG  . LYS A 135 ? 161.3905 161.3905 161.3905 0.0000 0.0000 0.0000 135 LYS A CG  
794  C CD  . LYS A 135 ? 161.4213 161.4213 161.4213 0.0000 0.0000 0.0000 135 LYS A CD  
795  C CE  . LYS A 135 ? 161.5057 161.5057 161.5057 0.0000 0.0000 0.0000 135 LYS A CE  
796  N NZ  . LYS A 135 ? 161.4961 161.4961 161.4961 0.0000 0.0000 0.0000 135 LYS A NZ  
797  N N   . ARG A 136 ? 161.3045 161.3045 161.3045 0.0000 0.0000 0.0000 136 ARG A N   
798  C CA  . ARG A 136 ? 160.8706 160.8706 160.8706 0.0000 0.0000 0.0000 136 ARG A CA  
799  C C   . ARG A 136 ? 160.9218 160.9218 160.9218 0.0000 0.0000 0.0000 136 ARG A C   
800  O O   . ARG A 136 ? 161.3978 161.3978 161.3978 0.0000 0.0000 0.0000 136 ARG A O   
801  C CB  . ARG A 136 ? 159.7957 159.7957 159.7957 0.0000 0.0000 0.0000 136 ARG A CB  
802  C CG  . ARG A 136 ? 158.9912 158.9912 158.9912 0.0000 0.0000 0.0000 136 ARG A CG  
803  C CD  . ARG A 136 ? 156.8596 156.8596 156.8596 0.0000 0.0000 0.0000 136 ARG A CD  
804  N NE  . ARG A 136 ? 157.4995 157.4995 157.4995 0.0000 0.0000 0.0000 136 ARG A NE  
805  C CZ  . ARG A 136 ? 159.0785 159.0785 159.0785 0.0000 0.0000 0.0000 136 ARG A CZ  
806  N NH1 . ARG A 136 ? 159.6207 159.6207 159.6207 0.0000 0.0000 0.0000 136 ARG A NH1 
807  N NH2 . ARG A 136 ? 159.4386 159.4386 159.4386 0.0000 0.0000 0.0000 136 ARG A NH2 
808  N N   . ALA A 137 ? 160.7579 160.7579 160.7579 0.0000 0.0000 0.0000 137 ALA A N   
809  C CA  . ALA A 137 ? 160.9120 160.9120 160.9120 0.0000 0.0000 0.0000 137 ALA A CA  
810  C C   . ALA A 137 ? 159.6981 159.6981 159.6981 0.0000 0.0000 0.0000 137 ALA A C   
811  O O   . ALA A 137 ? 158.0378 158.0378 158.0378 0.0000 0.0000 0.0000 137 ALA A O   
812  C CB  . ALA A 137 ? 161.0535 161.0535 161.0535 0.0000 0.0000 0.0000 137 ALA A CB  
813  N N   . SER A 138 ? 160.0859 160.0859 160.0859 0.0000 0.0000 0.0000 138 SER A N   
814  C CA  . SER A 138 ? 159.5168 159.5168 159.5168 0.0000 0.0000 0.0000 138 SER A CA  
815  C C   . SER A 138 ? 158.9063 158.9063 158.9063 0.0000 0.0000 0.0000 138 SER A C   
816  O O   . SER A 138 ? 157.7853 157.7853 157.7853 0.0000 0.0000 0.0000 138 SER A O   
817  C CB  . SER A 138 ? 160.5076 160.5076 160.5076 0.0000 0.0000 0.0000 138 SER A CB  
818  O OG  . SER A 138 ? 158.9966 158.9966 158.9966 0.0000 0.0000 0.0000 138 SER A OG  
819  N N   . GLY A 139 ? 161.7366 161.7366 161.7366 0.0000 0.0000 0.0000 139 GLY A N   
820  C CA  . GLY A 139 ? 161.6010 161.6010 161.6010 0.0000 0.0000 0.0000 139 GLY A CA  
821  C C   . GLY A 139 ? 162.9705 162.9705 162.9705 0.0000 0.0000 0.0000 139 GLY A C   
822  O O   . GLY A 139 ? 163.6173 163.6173 163.6173 0.0000 0.0000 0.0000 139 GLY A O   
823  N N   . GLY A 140 ? 165.9669 165.9669 165.9669 0.0000 0.0000 0.0000 140 GLY A N   
824  C CA  . GLY A 140 ? 166.9540 166.9540 166.9540 0.0000 0.0000 0.0000 140 GLY A CA  
825  C C   . GLY A 140 ? 167.2983 167.2983 167.2983 0.0000 0.0000 0.0000 140 GLY A C   
826  O O   . GLY A 140 ? 167.2755 167.2755 167.2755 0.0000 0.0000 0.0000 140 GLY A O   
827  N N   . LYS A 141 ? 166.5275 166.5275 166.5275 0.0000 0.0000 0.0000 141 LYS A N   
828  C CA  . LYS A 141 ? 166.3275 166.3275 166.3275 0.0000 0.0000 0.0000 141 LYS A CA  
829  C C   . LYS A 141 ? 165.6411 165.6411 165.6411 0.0000 0.0000 0.0000 141 LYS A C   
830  O O   . LYS A 141 ? 165.5380 165.5380 165.5380 0.0000 0.0000 0.0000 141 LYS A O   
831  C CB  . LYS A 141 ? 165.4852 165.4852 165.4852 0.0000 0.0000 0.0000 141 LYS A CB  
832  C CG  . LYS A 141 ? 166.3829 166.3829 166.3829 0.0000 0.0000 0.0000 141 LYS A CG  
833  C CD  . LYS A 141 ? 166.1521 166.1521 166.1521 0.0000 0.0000 0.0000 141 LYS A CD  
834  C CE  . LYS A 141 ? 165.9660 165.9660 165.9660 0.0000 0.0000 0.0000 141 LYS A CE  
835  N NZ  . LYS A 141 ? 166.0955 166.0955 166.0955 0.0000 0.0000 0.0000 141 LYS A NZ  
836  N N   . LEU A 142 ? 161.3025 161.3025 161.3025 0.0000 0.0000 0.0000 142 LEU A N   
837  C CA  . LEU A 142 ? 161.1433 161.1433 161.1433 0.0000 0.0000 0.0000 142 LEU A CA  
838  C C   . LEU A 142 ? 161.4188 161.4188 161.4188 0.0000 0.0000 0.0000 142 LEU A C   
839  O O   . LEU A 142 ? 161.5836 161.5836 161.5836 0.0000 0.0000 0.0000 142 LEU A O   
840  C CB  . LEU A 142 ? 160.1963 160.1963 160.1963 0.0000 0.0000 0.0000 142 LEU A CB  
841  C CG  . LEU A 142 ? 160.2900 160.2900 160.2900 0.0000 0.0000 0.0000 142 LEU A CG  
842  C CD1 . LEU A 142 ? 160.9994 160.9994 160.9994 0.0000 0.0000 0.0000 142 LEU A CD1 
843  C CD2 . LEU A 142 ? 157.8686 157.8686 157.8686 0.0000 0.0000 0.0000 142 LEU A CD2 
844  N N   . ILE A 143 ? 161.3462 161.3462 161.3462 0.0000 0.0000 0.0000 143 ILE A N   
845  C CA  . ILE A 143 ? 161.3332 161.3332 161.3332 0.0000 0.0000 0.0000 143 ILE A CA  
846  C C   . ILE A 143 ? 161.6519 161.6519 161.6519 0.0000 0.0000 0.0000 143 ILE A C   
847  O O   . ILE A 143 ? 161.8721 161.8721 161.8721 0.0000 0.0000 0.0000 143 ILE A O   
848  C CB  . ILE A 143 ? 161.1893 161.1893 161.1893 0.0000 0.0000 0.0000 143 ILE A CB  
849  C CG1 . ILE A 143 ? 161.3890 161.3890 161.3890 0.0000 0.0000 0.0000 143 ILE A CG1 
850  C CG2 . ILE A 143 ? 161.3963 161.3963 161.3963 0.0000 0.0000 0.0000 143 ILE A CG2 
851  C CD1 . ILE A 143 ? 161.7027 161.7027 161.7027 0.0000 0.0000 0.0000 143 ILE A CD1 
852  N N   . PHE A 144 ? 161.5762 161.5762 161.5762 0.0000 0.0000 0.0000 144 PHE A N   
853  C CA  . PHE A 144 ? 161.0673 161.0673 161.0673 0.0000 0.0000 0.0000 144 PHE A CA  
854  C C   . PHE A 144 ? 161.2108 161.2108 161.2108 0.0000 0.0000 0.0000 144 PHE A C   
855  O O   . PHE A 144 ? 161.4083 161.4083 161.4083 0.0000 0.0000 0.0000 144 PHE A O   
856  C CB  . PHE A 144 ? 160.6461 160.6461 160.6461 0.0000 0.0000 0.0000 144 PHE A CB  
857  C CG  . PHE A 144 ? 159.9956 159.9956 159.9956 0.0000 0.0000 0.0000 144 PHE A CG  
858  C CD1 . PHE A 144 ? 159.9440 159.9440 159.9440 0.0000 0.0000 0.0000 144 PHE A CD1 
859  C CD2 . PHE A 144 ? 159.5927 159.5927 159.5927 0.0000 0.0000 0.0000 144 PHE A CD2 
860  C CE1 . PHE A 144 ? 159.4048 159.4048 159.4048 0.0000 0.0000 0.0000 144 PHE A CE1 
861  C CE2 . PHE A 144 ? 158.9934 158.9934 158.9934 0.0000 0.0000 0.0000 144 PHE A CE2 
862  C CZ  . PHE A 144 ? 158.4096 158.4096 158.4096 0.0000 0.0000 0.0000 144 PHE A CZ  
863  N N   . TYR A 145 ? 161.2099 161.2099 161.2099 0.0000 0.0000 0.0000 145 TYR A N   
864  C CA  . TYR A 145 ? 161.3595 161.3595 161.3595 0.0000 0.0000 0.0000 145 TYR A CA  
865  C C   . TYR A 145 ? 161.5688 161.5688 161.5688 0.0000 0.0000 0.0000 145 TYR A C   
866  O O   . TYR A 145 ? 161.8228 161.8228 161.8228 0.0000 0.0000 0.0000 145 TYR A O   
867  C CB  . TYR A 145 ? 161.3377 161.3377 161.3377 0.0000 0.0000 0.0000 145 TYR A CB  
868  C CG  . TYR A 145 ? 161.2641 161.2641 161.2641 0.0000 0.0000 0.0000 145 TYR A CG  
869  C CD1 . TYR A 145 ? 161.4376 161.4376 161.4376 0.0000 0.0000 0.0000 145 TYR A CD1 
870  C CD2 . TYR A 145 ? 161.4668 161.4668 161.4668 0.0000 0.0000 0.0000 145 TYR A CD2 
871  C CE1 . TYR A 145 ? 161.4017 161.4017 161.4017 0.0000 0.0000 0.0000 145 TYR A CE1 
872  C CE2 . TYR A 145 ? 161.5909 161.5909 161.5909 0.0000 0.0000 0.0000 145 TYR A CE2 
873  C CZ  . TYR A 145 ? 161.4879 161.4879 161.4879 0.0000 0.0000 0.0000 145 TYR A CZ  
874  O OH  . TYR A 145 ? 161.4703 161.4703 161.4703 0.0000 0.0000 0.0000 145 TYR A OH  
875  N N   . ASP A 146 ? 161.4550 161.4550 161.4550 0.0000 0.0000 0.0000 146 ASP A N   
876  C CA  . ASP A 146 ? 161.3160 161.3160 161.3160 0.0000 0.0000 0.0000 146 ASP A CA  
877  C C   . ASP A 146 ? 161.2500 161.2500 161.2500 0.0000 0.0000 0.0000 146 ASP A C   
878  O O   . ASP A 146 ? 161.4825 161.4825 161.4825 0.0000 0.0000 0.0000 146 ASP A O   
879  C CB  . ASP A 146 ? 161.4823 161.4823 161.4823 0.0000 0.0000 0.0000 146 ASP A CB  
880  C CG  . ASP A 146 ? 161.4351 161.4351 161.4351 0.0000 0.0000 0.0000 146 ASP A CG  
881  O OD1 . ASP A 146 ? 161.2911 161.2911 161.2911 0.0000 0.0000 0.0000 146 ASP A OD1 
882  O OD2 . ASP A 146 ? 161.2573 161.2573 161.2573 0.0000 0.0000 0.0000 146 ASP A OD2 
883  N N   . LEU A 147 ? 161.1964 161.1964 161.1964 0.0000 0.0000 0.0000 147 LEU A N   
884  C CA  . LEU A 147 ? 161.3153 161.3153 161.3153 0.0000 0.0000 0.0000 147 LEU A CA  
885  C C   . LEU A 147 ? 161.2776 161.2776 161.2776 0.0000 0.0000 0.0000 147 LEU A C   
886  O O   . LEU A 147 ? 161.5465 161.5465 161.5465 0.0000 0.0000 0.0000 147 LEU A O   
887  C CB  . LEU A 147 ? 161.3970 161.3970 161.3970 0.0000 0.0000 0.0000 147 LEU A CB  
888  C CG  . LEU A 147 ? 161.3331 161.3331 161.3331 0.0000 0.0000 0.0000 147 LEU A CG  
889  C CD1 . LEU A 147 ? 161.3552 161.3552 161.3552 0.0000 0.0000 0.0000 147 LEU A CD1 
890  C CD2 . LEU A 147 ? 161.5069 161.5069 161.5069 0.0000 0.0000 0.0000 147 LEU A CD2 
891  N N   . ARG A 148 ? 161.1897 161.1897 161.1897 0.0000 0.0000 0.0000 148 ARG A N   
892  C CA  . ARG A 148 ? 161.2159 161.2159 161.2159 0.0000 0.0000 0.0000 148 ARG A CA  
893  C C   . ARG A 148 ? 161.3287 161.3287 161.3287 0.0000 0.0000 0.0000 148 ARG A C   
894  O O   . ARG A 148 ? 161.5140 161.5140 161.5140 0.0000 0.0000 0.0000 148 ARG A O   
895  C CB  . ARG A 148 ? 161.4505 161.4505 161.4505 0.0000 0.0000 0.0000 148 ARG A CB  
896  C CG  . ARG A 148 ? 161.5018 161.5018 161.5018 0.0000 0.0000 0.0000 148 ARG A CG  
897  C CD  . ARG A 148 ? 161.5157 161.5157 161.5157 0.0000 0.0000 0.0000 148 ARG A CD  
898  N NE  . ARG A 148 ? 161.3368 161.3368 161.3368 0.0000 0.0000 0.0000 148 ARG A NE  
899  C CZ  . ARG A 148 ? 161.4345 161.4345 161.4345 0.0000 0.0000 0.0000 148 ARG A CZ  
900  N NH1 . ARG A 148 ? 161.4411 161.4411 161.4411 0.0000 0.0000 0.0000 148 ARG A NH1 
901  N NH2 . ARG A 148 ? 161.6672 161.6672 161.6672 0.0000 0.0000 0.0000 148 ARG A NH2 
902  N N   . GLY A 149 ? 161.4372 161.4372 161.4372 0.0000 0.0000 0.0000 149 GLY A N   
903  C CA  . GLY A 149 ? 161.5009 161.5009 161.5009 0.0000 0.0000 0.0000 149 GLY A CA  
904  C C   . GLY A 149 ? 161.5733 161.5733 161.5733 0.0000 0.0000 0.0000 149 GLY A C   
905  O O   . GLY A 149 ? 161.8313 161.8313 161.8313 0.0000 0.0000 0.0000 149 GLY A O   
906  N N   . GLU A 150 ? 162.1372 162.1372 162.1372 0.0000 0.0000 0.0000 150 GLU A N   
907  C CA  . GLU A 150 ? 162.0419 162.0419 162.0419 0.0000 0.0000 0.0000 150 GLU A CA  
908  C C   . GLU A 150 ? 162.0897 162.0897 162.0897 0.0000 0.0000 0.0000 150 GLU A C   
909  O O   . GLU A 150 ? 162.1829 162.1829 162.1829 0.0000 0.0000 0.0000 150 GLU A O   
910  C CB  . GLU A 150 ? 162.2268 162.2268 162.2268 0.0000 0.0000 0.0000 150 GLU A CB  
911  C CG  . GLU A 150 ? 162.3492 162.3492 162.3492 0.0000 0.0000 0.0000 150 GLU A CG  
912  C CD  . GLU A 150 ? 162.3973 162.3973 162.3973 0.0000 0.0000 0.0000 150 GLU A CD  
913  O OE1 . GLU A 150 ? 162.5141 162.5141 162.5141 0.0000 0.0000 0.0000 150 GLU A OE1 
914  O OE2 . GLU A 150 ? 161.3695 161.3695 161.3695 0.0000 0.0000 0.0000 150 GLU A OE2 
915  N N   . GLY A 151 ? 161.3569 161.3569 161.3569 0.0000 0.0000 0.0000 151 GLY A N   
916  C CA  . GLY A 151 ? 161.4245 161.4245 161.4245 0.0000 0.0000 0.0000 151 GLY A CA  
917  C C   . GLY A 151 ? 161.4420 161.4420 161.4420 0.0000 0.0000 0.0000 151 GLY A C   
918  O O   . GLY A 151 ? 161.6423 161.6423 161.6423 0.0000 0.0000 0.0000 151 GLY A O   
919  N N   . VAL A 152 ? 161.4259 161.4259 161.4259 0.0000 0.0000 0.0000 152 VAL A N   
920  C CA  . VAL A 152 ? 161.3120 161.3120 161.3120 0.0000 0.0000 0.0000 152 VAL A CA  
921  C C   . VAL A 152 ? 161.3552 161.3552 161.3552 0.0000 0.0000 0.0000 152 VAL A C   
922  O O   . VAL A 152 ? 161.5599 161.5599 161.5599 0.0000 0.0000 0.0000 152 VAL A O   
923  C CB  . VAL A 152 ? 161.3665 161.3665 161.3665 0.0000 0.0000 0.0000 152 VAL A CB  
924  C CG1 . VAL A 152 ? 161.5721 161.5721 161.5721 0.0000 0.0000 0.0000 152 VAL A CG1 
925  C CG2 . VAL A 152 ? 161.4626 161.4626 161.4626 0.0000 0.0000 0.0000 152 VAL A CG2 
926  N N   . LYS A 153 ? 161.3780 161.3780 161.3780 0.0000 0.0000 0.0000 153 LYS A N   
927  C CA  . LYS A 153 ? 161.3727 161.3727 161.3727 0.0000 0.0000 0.0000 153 LYS A CA  
928  C C   . LYS A 153 ? 161.3583 161.3583 161.3583 0.0000 0.0000 0.0000 153 LYS A C   
929  O O   . LYS A 153 ? 161.5670 161.5670 161.5670 0.0000 0.0000 0.0000 153 LYS A O   
930  C CB  . LYS A 153 ? 161.3205 161.3205 161.3205 0.0000 0.0000 0.0000 153 LYS A CB  
931  C CG  . LYS A 153 ? 161.3276 161.3276 161.3276 0.0000 0.0000 0.0000 153 LYS A CG  
932  C CD  . LYS A 153 ? 161.3092 161.3092 161.3092 0.0000 0.0000 0.0000 153 LYS A CD  
933  C CE  . LYS A 153 ? 161.2407 161.2407 161.2407 0.0000 0.0000 0.0000 153 LYS A CE  
934  N NZ  . LYS A 153 ? 161.3062 161.3062 161.3062 0.0000 0.0000 0.0000 153 LYS A NZ  
935  N N   . LEU A 154 ? 161.3892 161.3892 161.3892 0.0000 0.0000 0.0000 154 LEU A N   
936  C CA  . LEU A 154 ? 161.2950 161.2950 161.2950 0.0000 0.0000 0.0000 154 LEU A CA  
937  C C   . LEU A 154 ? 161.3123 161.3123 161.3123 0.0000 0.0000 0.0000 154 LEU A C   
938  O O   . LEU A 154 ? 161.4905 161.4905 161.4905 0.0000 0.0000 0.0000 154 LEU A O   
939  C CB  . LEU A 154 ? 161.3114 161.3114 161.3114 0.0000 0.0000 0.0000 154 LEU A CB  
940  C CG  . LEU A 154 ? 161.3460 161.3460 161.3460 0.0000 0.0000 0.0000 154 LEU A CG  
941  C CD1 . LEU A 154 ? 161.5704 161.5704 161.5704 0.0000 0.0000 0.0000 154 LEU A CD1 
942  C CD2 . LEU A 154 ? 161.5027 161.5027 161.5027 0.0000 0.0000 0.0000 154 LEU A CD2 
943  N N   . GLN A 155 ? 161.4068 161.4068 161.4068 0.0000 0.0000 0.0000 155 GLN A N   
944  C CA  . GLN A 155 ? 161.3809 161.3809 161.3809 0.0000 0.0000 0.0000 155 GLN A CA  
945  C C   . GLN A 155 ? 161.4634 161.4634 161.4634 0.0000 0.0000 0.0000 155 GLN A C   
946  O O   . GLN A 155 ? 161.7418 161.7418 161.7418 0.0000 0.0000 0.0000 155 GLN A O   
947  C CB  . GLN A 155 ? 161.4007 161.4007 161.4007 0.0000 0.0000 0.0000 155 GLN A CB  
948  C CG  . GLN A 155 ? 161.1017 161.1017 161.1017 0.0000 0.0000 0.0000 155 GLN A CG  
949  C CD  . GLN A 155 ? 160.0108 160.0108 160.0108 0.0000 0.0000 0.0000 155 GLN A CD  
950  O OE1 . GLN A 155 ? 158.5651 158.5651 158.5651 0.0000 0.0000 0.0000 155 GLN A OE1 
951  N NE2 . GLN A 155 ? 160.4278 160.4278 160.4278 0.0000 0.0000 0.0000 155 GLN A NE2 
952  N N   . VAL A 156 ? 161.3245 161.3245 161.3245 0.0000 0.0000 0.0000 156 VAL A N   
953  C CA  . VAL A 156 ? 161.2219 161.2219 161.2219 0.0000 0.0000 0.0000 156 VAL A CA  
954  C C   . VAL A 156 ? 161.2997 161.2997 161.2997 0.0000 0.0000 0.0000 156 VAL A C   
955  O O   . VAL A 156 ? 161.4560 161.4560 161.4560 0.0000 0.0000 0.0000 156 VAL A O   
956  C CB  . VAL A 156 ? 161.3352 161.3352 161.3352 0.0000 0.0000 0.0000 156 VAL A CB  
957  C CG1 . VAL A 156 ? 161.5033 161.5033 161.5033 0.0000 0.0000 0.0000 156 VAL A CG1 
958  C CG2 . VAL A 156 ? 161.5536 161.5536 161.5536 0.0000 0.0000 0.0000 156 VAL A CG2 
959  N N   . MET A 157 ? 161.3280 161.3280 161.3280 0.0000 0.0000 0.0000 157 MET A N   
960  C CA  . MET A 157 ? 161.3632 161.3632 161.3632 0.0000 0.0000 0.0000 157 MET A CA  
961  C C   . MET A 157 ? 161.4480 161.4480 161.4480 0.0000 0.0000 0.0000 157 MET A C   
962  O O   . MET A 157 ? 161.5061 161.5061 161.5061 0.0000 0.0000 0.0000 157 MET A O   
963  C CB  . MET A 157 ? 161.3556 161.3556 161.3556 0.0000 0.0000 0.0000 157 MET A CB  
964  C CG  . MET A 157 ? 161.4000 161.4000 161.4000 0.0000 0.0000 0.0000 157 MET A CG  
965  S SD  . MET A 157 ? 160.1596 160.1596 160.1596 0.0000 0.0000 0.0000 157 MET A SD  
966  C CE  . MET A 157 ? 160.6300 160.6300 160.6300 0.0000 0.0000 0.0000 157 MET A CE  
967  N N   . ALA A 158 ? 161.4421 161.4421 161.4421 0.0000 0.0000 0.0000 158 ALA A N   
968  C CA  . ALA A 158 ? 161.3442 161.3442 161.3442 0.0000 0.0000 0.0000 158 ALA A CA  
969  C C   . ALA A 158 ? 161.4064 161.4064 161.4064 0.0000 0.0000 0.0000 158 ALA A C   
970  O O   . ALA A 158 ? 161.6408 161.6408 161.6408 0.0000 0.0000 0.0000 158 ALA A O   
971  C CB  . ALA A 158 ? 161.4568 161.4568 161.4568 0.0000 0.0000 0.0000 158 ALA A CB  
972  N N   . ASN A 159 ? 163.5441 163.5441 163.5441 0.0000 0.0000 0.0000 159 ASN A N   
973  C CA  . ASN A 159 ? 163.8504 163.8504 163.8504 0.0000 0.0000 0.0000 159 ASN A CA  
974  C C   . ASN A 159 ? 163.9073 163.9073 163.9073 0.0000 0.0000 0.0000 159 ASN A C   
975  O O   . ASN A 159 ? 163.9260 163.9260 163.9260 0.0000 0.0000 0.0000 159 ASN A O   
976  C CB  . ASN A 159 ? 163.6671 163.6671 163.6671 0.0000 0.0000 0.0000 159 ASN A CB  
977  C CG  . ASN A 159 ? 162.8506 162.8506 162.8506 0.0000 0.0000 0.0000 159 ASN A CG  
978  O OD1 . ASN A 159 ? 162.4202 162.4202 162.4202 0.0000 0.0000 0.0000 159 ASN A OD1 
979  N ND2 . ASN A 159 ? 162.1082 162.1082 162.1082 0.0000 0.0000 0.0000 159 ASN A ND2 
980  N N   . SER A 160 ? 161.7670 161.7670 161.7670 0.0000 0.0000 0.0000 160 SER A N   
981  C CA  . SER A 160 ? 161.6840 161.6840 161.6840 0.0000 0.0000 0.0000 160 SER A CA  
982  C C   . SER A 160 ? 161.6330 161.6330 161.6330 0.0000 0.0000 0.0000 160 SER A C   
983  O O   . SER A 160 ? 161.8298 161.8298 161.8298 0.0000 0.0000 0.0000 160 SER A O   
984  C CB  . SER A 160 ? 162.0190 162.0190 162.0190 0.0000 0.0000 0.0000 160 SER A CB  
985  O OG  . SER A 160 ? 161.8846 161.8846 161.8846 0.0000 0.0000 0.0000 160 SER A OG  
986  N N   . ARG A 161 ? 166.9170 166.9170 166.9170 0.0000 0.0000 0.0000 161 ARG A N   
987  C CA  . ARG A 161 ? 167.1528 167.1528 167.1528 0.0000 0.0000 0.0000 161 ARG A CA  
988  C C   . ARG A 161 ? 167.0497 167.0497 167.0497 0.0000 0.0000 0.0000 161 ARG A C   
989  O O   . ARG A 161 ? 167.1829 167.1829 167.1829 0.0000 0.0000 0.0000 161 ARG A O   
990  C CB  . ARG A 161 ? 167.1097 167.1097 167.1097 0.0000 0.0000 0.0000 161 ARG A CB  
991  C CG  . ARG A 161 ? 167.4259 167.4259 167.4259 0.0000 0.0000 0.0000 161 ARG A CG  
992  C CD  . ARG A 161 ? 167.4397 167.4397 167.4397 0.0000 0.0000 0.0000 161 ARG A CD  
993  N NE  . ARG A 161 ? 166.8045 166.8045 166.8045 0.0000 0.0000 0.0000 161 ARG A NE  
994  C CZ  . ARG A 161 ? 166.2189 166.2189 166.2189 0.0000 0.0000 0.0000 161 ARG A CZ  
995  N NH1 . ARG A 161 ? 165.9404 165.9404 165.9404 0.0000 0.0000 0.0000 161 ARG A NH1 
996  N NH2 . ARG A 161 ? 165.3283 165.3283 165.3283 0.0000 0.0000 0.0000 161 ARG A NH2 
997  N N   . ASN A 162 ? 161.6709 161.6709 161.6709 0.0000 0.0000 0.0000 162 ASN A N   
998  C CA  . ASN A 162 ? 161.5954 161.5954 161.5954 0.0000 0.0000 0.0000 162 ASN A CA  
999  C C   . ASN A 162 ? 161.5953 161.5953 161.5953 0.0000 0.0000 0.0000 162 ASN A C   
1000 O O   . ASN A 162 ? 161.6974 161.6974 161.6974 0.0000 0.0000 0.0000 162 ASN A O   
1001 C CB  . ASN A 162 ? 161.5085 161.5085 161.5085 0.0000 0.0000 0.0000 162 ASN A CB  
1002 C CG  . ASN A 162 ? 161.4550 161.4550 161.4550 0.0000 0.0000 0.0000 162 ASN A CG  
1003 O OD1 . ASN A 162 ? 161.3973 161.3973 161.3973 0.0000 0.0000 0.0000 162 ASN A OD1 
1004 N ND2 . ASN A 162 ? 161.4889 161.4889 161.4889 0.0000 0.0000 0.0000 162 ASN A ND2 
1005 N N   . TYR A 163 ? 161.4612 161.4612 161.4612 0.0000 0.0000 0.0000 163 TYR A N   
1006 C CA  . TYR A 163 ? 161.4568 161.4568 161.4568 0.0000 0.0000 0.0000 163 TYR A CA  
1007 C C   . TYR A 163 ? 161.4826 161.4826 161.4826 0.0000 0.0000 0.0000 163 TYR A C   
1008 O O   . TYR A 163 ? 161.6486 161.6486 161.6486 0.0000 0.0000 0.0000 163 TYR A O   
1009 C CB  . TYR A 163 ? 161.5511 161.5511 161.5511 0.0000 0.0000 0.0000 163 TYR A CB  
1010 C CG  . TYR A 163 ? 161.5391 161.5391 161.5391 0.0000 0.0000 0.0000 163 TYR A CG  
1011 C CD1 . TYR A 163 ? 161.5044 161.5044 161.5044 0.0000 0.0000 0.0000 163 TYR A CD1 
1012 C CD2 . TYR A 163 ? 161.7200 161.7200 161.7200 0.0000 0.0000 0.0000 163 TYR A CD2 
1013 C CE1 . TYR A 163 ? 161.4114 161.4114 161.4114 0.0000 0.0000 0.0000 163 TYR A CE1 
1014 C CE2 . TYR A 163 ? 161.6833 161.6833 161.6833 0.0000 0.0000 0.0000 163 TYR A CE2 
1015 C CZ  . TYR A 163 ? 161.4214 161.4214 161.4214 0.0000 0.0000 0.0000 163 TYR A CZ  
1016 O OH  . TYR A 163 ? 161.5487 161.5487 161.5487 0.0000 0.0000 0.0000 163 TYR A OH  
1017 N N   . LYS A 164 ? 161.4280 161.4280 161.4280 0.0000 0.0000 0.0000 164 LYS A N   
1018 C CA  . LYS A 164 ? 161.5756 161.5756 161.5756 0.0000 0.0000 0.0000 164 LYS A CA  
1019 C C   . LYS A 164 ? 161.9897 161.9897 161.9897 0.0000 0.0000 0.0000 164 LYS A C   
1020 O O   . LYS A 164 ? 161.8802 161.8802 161.8802 0.0000 0.0000 0.0000 164 LYS A O   
1021 C CB  . LYS A 164 ? 161.5984 161.5984 161.5984 0.0000 0.0000 0.0000 164 LYS A CB  
1022 C CG  . LYS A 164 ? 161.7495 161.7495 161.7495 0.0000 0.0000 0.0000 164 LYS A CG  
1023 C CD  . LYS A 164 ? 161.7828 161.7828 161.7828 0.0000 0.0000 0.0000 164 LYS A CD  
1024 C CE  . LYS A 164 ? 161.7069 161.7069 161.7069 0.0000 0.0000 0.0000 164 LYS A CE  
1025 N NZ  . LYS A 164 ? 161.5622 161.5622 161.5622 0.0000 0.0000 0.0000 164 LYS A NZ  
1026 N N   . SER A 165 ? 177.0863 177.0863 177.0863 0.0000 0.0000 0.0000 165 SER A N   
1027 C CA  . SER A 165 ? 177.7575 177.7575 177.7575 0.0000 0.0000 0.0000 165 SER A CA  
1028 C C   . SER A 165 ? 177.9756 177.9756 177.9756 0.0000 0.0000 0.0000 165 SER A C   
1029 O O   . SER A 165 ? 177.7149 177.7149 177.7149 0.0000 0.0000 0.0000 165 SER A O   
1030 C CB  . SER A 165 ? 178.0755 178.0755 178.0755 0.0000 0.0000 0.0000 165 SER A CB  
1031 O OG  . SER A 165 ? 178.1195 178.1195 178.1195 0.0000 0.0000 0.0000 165 SER A OG  
1032 N N   . GLU A 166 ? 187.9126 187.9126 187.9126 0.0000 0.0000 0.0000 166 GLU A N   
1033 C CA  . GLU A 166 ? 188.0732 188.0732 188.0732 0.0000 0.0000 0.0000 166 GLU A CA  
1034 C C   . GLU A 166 ? 187.9237 187.9237 187.9237 0.0000 0.0000 0.0000 166 GLU A C   
1035 O O   . GLU A 166 ? 187.6694 187.6694 187.6694 0.0000 0.0000 0.0000 166 GLU A O   
1036 C CB  . GLU A 166 ? 188.3740 188.3740 188.3740 0.0000 0.0000 0.0000 166 GLU A CB  
1037 C CG  . GLU A 166 ? 188.3890 188.3890 188.3890 0.0000 0.0000 0.0000 166 GLU A CG  
1038 C CD  . GLU A 166 ? 188.1269 188.1269 188.1269 0.0000 0.0000 0.0000 166 GLU A CD  
1039 O OE1 . GLU A 166 ? 187.8184 187.8184 187.8184 0.0000 0.0000 0.0000 166 GLU A OE1 
1040 O OE2 . GLU A 166 ? 188.0438 188.0438 188.0438 0.0000 0.0000 0.0000 166 GLU A OE2 
1041 N N   . GLU A 167 ? 188.6787 188.6787 188.6787 0.0000 0.0000 0.0000 167 GLU A N   
1042 C CA  . GLU A 167 ? 188.6783 188.6783 188.6783 0.0000 0.0000 0.0000 167 GLU A CA  
1043 C C   . GLU A 167 ? 188.2350 188.2350 188.2350 0.0000 0.0000 0.0000 167 GLU A C   
1044 O O   . GLU A 167 ? 188.1018 188.1018 188.1018 0.0000 0.0000 0.0000 167 GLU A O   
1045 C CB  . GLU A 167 ? 189.0813 189.0813 189.0813 0.0000 0.0000 0.0000 167 GLU A CB  
1046 C CG  . GLU A 167 ? 189.1886 189.1886 189.1886 0.0000 0.0000 0.0000 167 GLU A CG  
1047 C CD  . GLU A 167 ? 189.0717 189.0717 189.0717 0.0000 0.0000 0.0000 167 GLU A CD  
1048 O OE1 . GLU A 167 ? 189.0263 189.0263 189.0263 0.0000 0.0000 0.0000 167 GLU A OE1 
1049 O OE2 . GLU A 167 ? 189.0877 189.0877 189.0877 0.0000 0.0000 0.0000 167 GLU A OE2 
1050 N N   . GLU A 168 ? 179.1457 179.1457 179.1457 0.0000 0.0000 0.0000 168 GLU A N   
1051 C CA  . GLU A 168 ? 178.8433 178.8433 178.8433 0.0000 0.0000 0.0000 168 GLU A CA  
1052 C C   . GLU A 168 ? 178.1797 178.1797 178.1797 0.0000 0.0000 0.0000 168 GLU A C   
1053 O O   . GLU A 168 ? 178.1667 178.1667 178.1667 0.0000 0.0000 0.0000 168 GLU A O   
1054 C CB  . GLU A 168 ? 178.9375 178.9375 178.9375 0.0000 0.0000 0.0000 168 GLU A CB  
1055 C CG  . GLU A 168 ? 179.1135 179.1135 179.1135 0.0000 0.0000 0.0000 168 GLU A CG  
1056 C CD  . GLU A 168 ? 178.9997 178.9997 178.9997 0.0000 0.0000 0.0000 168 GLU A CD  
1057 O OE1 . GLU A 168 ? 178.9783 178.9783 178.9783 0.0000 0.0000 0.0000 168 GLU A OE1 
1058 O OE2 . GLU A 168 ? 179.0414 179.0414 179.0414 0.0000 0.0000 0.0000 168 GLU A OE2 
1059 N N   . PHE A 169 ? 162.7444 162.7444 162.7444 0.0000 0.0000 0.0000 169 PHE A N   
1060 C CA  . PHE A 169 ? 162.0415 162.0415 162.0415 0.0000 0.0000 0.0000 169 PHE A CA  
1061 C C   . PHE A 169 ? 161.8726 161.8726 161.8726 0.0000 0.0000 0.0000 169 PHE A C   
1062 O O   . PHE A 169 ? 161.7865 161.7865 161.7865 0.0000 0.0000 0.0000 169 PHE A O   
1063 C CB  . PHE A 169 ? 162.0060 162.0060 162.0060 0.0000 0.0000 0.0000 169 PHE A CB  
1064 C CG  . PHE A 169 ? 161.5582 161.5582 161.5582 0.0000 0.0000 0.0000 169 PHE A CG  
1065 C CD1 . PHE A 169 ? 161.4399 161.4399 161.4399 0.0000 0.0000 0.0000 169 PHE A CD1 
1066 C CD2 . PHE A 169 ? 161.7209 161.7209 161.7209 0.0000 0.0000 0.0000 169 PHE A CD2 
1067 C CE1 . PHE A 169 ? 161.4167 161.4167 161.4167 0.0000 0.0000 0.0000 169 PHE A CE1 
1068 C CE2 . PHE A 169 ? 161.6079 161.6079 161.6079 0.0000 0.0000 0.0000 169 PHE A CE2 
1069 C CZ  . PHE A 169 ? 161.4392 161.4392 161.4392 0.0000 0.0000 0.0000 169 PHE A CZ  
1070 N N   . ILE A 170 ? 162.1142 162.1142 162.1142 0.0000 0.0000 0.0000 170 ILE A N   
1071 C CA  . ILE A 170 ? 161.6538 161.6538 161.6538 0.0000 0.0000 0.0000 170 ILE A CA  
1072 C C   . ILE A 170 ? 161.6980 161.6980 161.6980 0.0000 0.0000 0.0000 170 ILE A C   
1073 O O   . ILE A 170 ? 161.5879 161.5879 161.5879 0.0000 0.0000 0.0000 170 ILE A O   
1074 C CB  . ILE A 170 ? 161.7625 161.7625 161.7625 0.0000 0.0000 0.0000 170 ILE A CB  
1075 C CG1 . ILE A 170 ? 161.9846 161.9846 161.9846 0.0000 0.0000 0.0000 170 ILE A CG1 
1076 C CG2 . ILE A 170 ? 161.5260 161.5260 161.5260 0.0000 0.0000 0.0000 170 ILE A CG2 
1077 C CD1 . ILE A 170 ? 161.9043 161.9043 161.9043 0.0000 0.0000 0.0000 170 ILE A CD1 
1078 N N   . HIS A 171 ? 166.3863 166.3863 166.3863 0.0000 0.0000 0.0000 171 HIS A N   
1079 C CA  . HIS A 171 ? 166.4245 166.4245 166.4245 0.0000 0.0000 0.0000 171 HIS A CA  
1080 C C   . HIS A 171 ? 166.3558 166.3558 166.3558 0.0000 0.0000 0.0000 171 HIS A C   
1081 O O   . HIS A 171 ? 166.4501 166.4501 166.4501 0.0000 0.0000 0.0000 171 HIS A O   
1082 C CB  . HIS A 171 ? 166.5622 166.5622 166.5622 0.0000 0.0000 0.0000 171 HIS A CB  
1083 C CG  . HIS A 171 ? 166.4184 166.4184 166.4184 0.0000 0.0000 0.0000 171 HIS A CG  
1084 N ND1 . HIS A 171 ? 166.4353 166.4353 166.4353 0.0000 0.0000 0.0000 171 HIS A ND1 
1085 C CD2 . HIS A 171 ? 166.5297 166.5297 166.5297 0.0000 0.0000 0.0000 171 HIS A CD2 
1086 C CE1 . HIS A 171 ? 166.7190 166.7190 166.7190 0.0000 0.0000 0.0000 171 HIS A CE1 
1087 N NE2 . HIS A 171 ? 166.8142 166.8142 166.8142 0.0000 0.0000 0.0000 171 HIS A NE2 
1088 N N   . ILE A 172 ? 161.9818 161.9818 161.9818 0.0000 0.0000 0.0000 172 ILE A N   
1089 C CA  . ILE A 172 ? 161.5634 161.5634 161.5634 0.0000 0.0000 0.0000 172 ILE A CA  
1090 C C   . ILE A 172 ? 161.5185 161.5185 161.5185 0.0000 0.0000 0.0000 172 ILE A C   
1091 O O   . ILE A 172 ? 161.6405 161.6405 161.6405 0.0000 0.0000 0.0000 172 ILE A O   
1092 C CB  . ILE A 172 ? 161.4735 161.4735 161.4735 0.0000 0.0000 0.0000 172 ILE A CB  
1093 C CG1 . ILE A 172 ? 161.5049 161.5049 161.5049 0.0000 0.0000 0.0000 172 ILE A CG1 
1094 C CG2 . ILE A 172 ? 161.6478 161.6478 161.6478 0.0000 0.0000 0.0000 172 ILE A CG2 
1095 C CD1 . ILE A 172 ? 161.5472 161.5472 161.5472 0.0000 0.0000 0.0000 172 ILE A CD1 
1096 N N   . ASN A 173 ? 161.5896 161.5896 161.5896 0.0000 0.0000 0.0000 173 ASN A N   
1097 C CA  . ASN A 173 ? 161.4714 161.4714 161.4714 0.0000 0.0000 0.0000 173 ASN A CA  
1098 C C   . ASN A 173 ? 161.4342 161.4342 161.4342 0.0000 0.0000 0.0000 173 ASN A C   
1099 O O   . ASN A 173 ? 161.3916 161.3916 161.3916 0.0000 0.0000 0.0000 173 ASN A O   
1100 C CB  . ASN A 173 ? 161.4875 161.4875 161.4875 0.0000 0.0000 0.0000 173 ASN A CB  
1101 C CG  . ASN A 173 ? 161.4882 161.4882 161.4882 0.0000 0.0000 0.0000 173 ASN A CG  
1102 O OD1 . ASN A 173 ? 161.4336 161.4336 161.4336 0.0000 0.0000 0.0000 173 ASN A OD1 
1103 N ND2 . ASN A 173 ? 161.6488 161.6488 161.6488 0.0000 0.0000 0.0000 173 ASN A ND2 
1104 N N   . ASN A 174 ? 161.4894 161.4894 161.4894 0.0000 0.0000 0.0000 174 ASN A N   
1105 C CA  . ASN A 174 ? 161.4229 161.4229 161.4229 0.0000 0.0000 0.0000 174 ASN A CA  
1106 C C   . ASN A 174 ? 161.3367 161.3367 161.3367 0.0000 0.0000 0.0000 174 ASN A C   
1107 O O   . ASN A 174 ? 161.5208 161.5208 161.5208 0.0000 0.0000 0.0000 174 ASN A O   
1108 C CB  . ASN A 174 ? 161.4626 161.4626 161.4626 0.0000 0.0000 0.0000 174 ASN A CB  
1109 C CG  . ASN A 174 ? 161.4706 161.4706 161.4706 0.0000 0.0000 0.0000 174 ASN A CG  
1110 O OD1 . ASN A 174 ? 161.5592 161.5592 161.5592 0.0000 0.0000 0.0000 174 ASN A OD1 
1111 N ND2 . ASN A 174 ? 161.4588 161.4588 161.4588 0.0000 0.0000 0.0000 174 ASN A ND2 
1112 N N   . LYS A 175 ? 161.1854 161.1854 161.1854 0.0000 0.0000 0.0000 175 LYS A N   
1113 C CA  . LYS A 175 ? 161.2286 161.2286 161.2286 0.0000 0.0000 0.0000 175 LYS A CA  
1114 C C   . LYS A 175 ? 161.2587 161.2587 161.2587 0.0000 0.0000 0.0000 175 LYS A C   
1115 O O   . LYS A 175 ? 161.3607 161.3607 161.3607 0.0000 0.0000 0.0000 175 LYS A O   
1116 C CB  . LYS A 175 ? 161.3588 161.3588 161.3588 0.0000 0.0000 0.0000 175 LYS A CB  
1117 C CG  . LYS A 175 ? 161.5219 161.5219 161.5219 0.0000 0.0000 0.0000 175 LYS A CG  
1118 C CD  . LYS A 175 ? 161.4611 161.4611 161.4611 0.0000 0.0000 0.0000 175 LYS A CD  
1119 C CE  . LYS A 175 ? 161.3116 161.3116 161.3116 0.0000 0.0000 0.0000 175 LYS A CE  
1120 N NZ  . LYS A 175 ? 161.4373 161.4373 161.4373 0.0000 0.0000 0.0000 175 LYS A NZ  
1121 N N   . LEU A 176 ? 161.3763 161.3763 161.3763 0.0000 0.0000 0.0000 176 LEU A N   
1122 C CA  . LEU A 176 ? 161.3205 161.3205 161.3205 0.0000 0.0000 0.0000 176 LEU A CA  
1123 C C   . LEU A 176 ? 161.3304 161.3304 161.3304 0.0000 0.0000 0.0000 176 LEU A C   
1124 O O   . LEU A 176 ? 161.4643 161.4643 161.4643 0.0000 0.0000 0.0000 176 LEU A O   
1125 C CB  . LEU A 176 ? 161.4157 161.4157 161.4157 0.0000 0.0000 0.0000 176 LEU A CB  
1126 C CG  . LEU A 176 ? 161.3292 161.3292 161.3292 0.0000 0.0000 0.0000 176 LEU A CG  
1127 C CD1 . LEU A 176 ? 161.4017 161.4017 161.4017 0.0000 0.0000 0.0000 176 LEU A CD1 
1128 C CD2 . LEU A 176 ? 161.5307 161.5307 161.5307 0.0000 0.0000 0.0000 176 LEU A CD2 
1129 N N   . ARG A 177 ? 161.3999 161.3999 161.3999 0.0000 0.0000 0.0000 177 ARG A N   
1130 C CA  . ARG A 177 ? 161.4356 161.4356 161.4356 0.0000 0.0000 0.0000 177 ARG A CA  
1131 C C   . ARG A 177 ? 161.5212 161.5212 161.5212 0.0000 0.0000 0.0000 177 ARG A C   
1132 O O   . ARG A 177 ? 161.8446 161.8446 161.8446 0.0000 0.0000 0.0000 177 ARG A O   
1133 C CB  . ARG A 177 ? 161.4799 161.4799 161.4799 0.0000 0.0000 0.0000 177 ARG A CB  
1134 C CG  . ARG A 177 ? 161.3036 161.3036 161.3036 0.0000 0.0000 0.0000 177 ARG A CG  
1135 C CD  . ARG A 177 ? 160.7081 160.7081 160.7081 0.0000 0.0000 0.0000 177 ARG A CD  
1136 N NE  . ARG A 177 ? 159.8034 159.8034 159.8034 0.0000 0.0000 0.0000 177 ARG A NE  
1137 C CZ  . ARG A 177 ? 160.5303 160.5303 160.5303 0.0000 0.0000 0.0000 177 ARG A CZ  
1138 N NH1 . ARG A 177 ? 161.2377 161.2377 161.2377 0.0000 0.0000 0.0000 177 ARG A NH1 
1139 N NH2 . ARG A 177 ? 159.9967 159.9967 159.9967 0.0000 0.0000 0.0000 177 ARG A NH2 
1140 N N   . ARG A 178 ? 161.0025 161.0025 161.0025 0.0000 0.0000 0.0000 178 ARG A N   
1141 C CA  . ARG A 178 ? 161.0271 161.0271 161.0271 0.0000 0.0000 0.0000 178 ARG A CA  
1142 C C   . ARG A 178 ? 161.2229 161.2229 161.2229 0.0000 0.0000 0.0000 178 ARG A C   
1143 O O   . ARG A 178 ? 161.2201 161.2201 161.2201 0.0000 0.0000 0.0000 178 ARG A O   
1144 C CB  . ARG A 178 ? 161.0591 161.0591 161.0591 0.0000 0.0000 0.0000 178 ARG A CB  
1145 C CG  . ARG A 178 ? 161.0757 161.0757 161.0757 0.0000 0.0000 0.0000 178 ARG A CG  
1146 C CD  . ARG A 178 ? 160.8758 160.8758 160.8758 0.0000 0.0000 0.0000 178 ARG A CD  
1147 N NE  . ARG A 178 ? 160.1078 160.1078 160.1078 0.0000 0.0000 0.0000 178 ARG A NE  
1148 C CZ  . ARG A 178 ? 160.4644 160.4644 160.4644 0.0000 0.0000 0.0000 178 ARG A CZ  
1149 N NH1 . ARG A 178 ? 161.4640 161.4640 161.4640 0.0000 0.0000 0.0000 178 ARG A NH1 
1150 N NH2 . ARG A 178 ? 160.1893 160.1893 160.1893 0.0000 0.0000 0.0000 178 ARG A NH2 
1151 N N   . GLY A 179 ? 161.4003 161.4003 161.4003 0.0000 0.0000 0.0000 179 GLY A N   
1152 C CA  . GLY A 179 ? 161.4880 161.4880 161.4880 0.0000 0.0000 0.0000 179 GLY A CA  
1153 C C   . GLY A 179 ? 161.4632 161.4632 161.4632 0.0000 0.0000 0.0000 179 GLY A C   
1154 O O   . GLY A 179 ? 161.5975 161.5975 161.5975 0.0000 0.0000 0.0000 179 GLY A O   
1155 N N   . ASP A 180 ? 161.3077 161.3077 161.3077 0.0000 0.0000 0.0000 180 ASP A N   
1156 C CA  . ASP A 180 ? 161.2980 161.2980 161.2980 0.0000 0.0000 0.0000 180 ASP A CA  
1157 C C   . ASP A 180 ? 161.3368 161.3368 161.3368 0.0000 0.0000 0.0000 180 ASP A C   
1158 O O   . ASP A 180 ? 161.5104 161.5104 161.5104 0.0000 0.0000 0.0000 180 ASP A O   
1159 C CB  . ASP A 180 ? 161.4312 161.4312 161.4312 0.0000 0.0000 0.0000 180 ASP A CB  
1160 C CG  . ASP A 180 ? 161.6507 161.6507 161.6507 0.0000 0.0000 0.0000 180 ASP A CG  
1161 O OD1 . ASP A 180 ? 161.7173 161.7173 161.7173 0.0000 0.0000 0.0000 180 ASP A OD1 
1162 O OD2 . ASP A 180 ? 161.7179 161.7179 161.7179 0.0000 0.0000 0.0000 180 ASP A OD2 
1163 N N   . ILE A 181 ? 161.3495 161.3495 161.3495 0.0000 0.0000 0.0000 181 ILE A N   
1164 C CA  . ILE A 181 ? 161.2190 161.2190 161.2190 0.0000 0.0000 0.0000 181 ILE A CA  
1165 C C   . ILE A 181 ? 161.3703 161.3703 161.3703 0.0000 0.0000 0.0000 181 ILE A C   
1166 O O   . ILE A 181 ? 161.7407 161.7407 161.7407 0.0000 0.0000 0.0000 181 ILE A O   
1167 C CB  . ILE A 181 ? 160.2930 160.2930 160.2930 0.0000 0.0000 0.0000 181 ILE A CB  
1168 C CG1 . ILE A 181 ? 159.1485 159.1485 159.1485 0.0000 0.0000 0.0000 181 ILE A CG1 
1169 C CG2 . ILE A 181 ? 160.1600 160.1600 160.1600 0.0000 0.0000 0.0000 181 ILE A CG2 
1170 C CD1 . ILE A 181 ? 160.2635 160.2635 160.2635 0.0000 0.0000 0.0000 181 ILE A CD1 
1171 N N   . ILE A 182 ? 161.2360 161.2360 161.2360 0.0000 0.0000 0.0000 182 ILE A N   
1172 C CA  . ILE A 182 ? 161.1724 161.1724 161.1724 0.0000 0.0000 0.0000 182 ILE A CA  
1173 C C   . ILE A 182 ? 161.0560 161.0560 161.0560 0.0000 0.0000 0.0000 182 ILE A C   
1174 O O   . ILE A 182 ? 161.3649 161.3649 161.3649 0.0000 0.0000 0.0000 182 ILE A O   
1175 C CB  . ILE A 182 ? 161.2252 161.2252 161.2252 0.0000 0.0000 0.0000 182 ILE A CB  
1176 C CG1 . ILE A 182 ? 161.2717 161.2717 161.2717 0.0000 0.0000 0.0000 182 ILE A CG1 
1177 C CG2 . ILE A 182 ? 161.4932 161.4932 161.4932 0.0000 0.0000 0.0000 182 ILE A CG2 
1178 C CD1 . ILE A 182 ? 161.3147 161.3147 161.3147 0.0000 0.0000 0.0000 182 ILE A CD1 
1179 N N   . GLY A 183 ? 161.1021 161.1021 161.1021 0.0000 0.0000 0.0000 183 GLY A N   
1180 C CA  . GLY A 183 ? 161.2904 161.2904 161.2904 0.0000 0.0000 0.0000 183 GLY A CA  
1181 C C   . GLY A 183 ? 161.2283 161.2283 161.2283 0.0000 0.0000 0.0000 183 GLY A C   
1182 O O   . GLY A 183 ? 161.4573 161.4573 161.4573 0.0000 0.0000 0.0000 183 GLY A O   
1183 N N   . VAL A 184 ? 161.2156 161.2156 161.2156 0.0000 0.0000 0.0000 184 VAL A N   
1184 C CA  . VAL A 184 ? 161.1864 161.1864 161.1864 0.0000 0.0000 0.0000 184 VAL A CA  
1185 C C   . VAL A 184 ? 161.2784 161.2784 161.2784 0.0000 0.0000 0.0000 184 VAL A C   
1186 O O   . VAL A 184 ? 161.6768 161.6768 161.6768 0.0000 0.0000 0.0000 184 VAL A O   
1187 C CB  . VAL A 184 ? 161.2912 161.2912 161.2912 0.0000 0.0000 0.0000 184 VAL A CB  
1188 C CG1 . VAL A 184 ? 161.4293 161.4293 161.4293 0.0000 0.0000 0.0000 184 VAL A CG1 
1189 C CG2 . VAL A 184 ? 161.4760 161.4760 161.4760 0.0000 0.0000 0.0000 184 VAL A CG2 
1190 N N   . GLN A 185 ? 161.2826 161.2826 161.2826 0.0000 0.0000 0.0000 185 GLN A N   
1191 C CA  . GLN A 185 ? 161.3116 161.3116 161.3116 0.0000 0.0000 0.0000 185 GLN A CA  
1192 C C   . GLN A 185 ? 161.2563 161.2563 161.2563 0.0000 0.0000 0.0000 185 GLN A C   
1193 O O   . GLN A 185 ? 161.4887 161.4887 161.4887 0.0000 0.0000 0.0000 185 GLN A O   
1194 C CB  . GLN A 185 ? 161.4185 161.4185 161.4185 0.0000 0.0000 0.0000 185 GLN A CB  
1195 C CG  . GLN A 185 ? 161.3774 161.3774 161.3774 0.0000 0.0000 0.0000 185 GLN A CG  
1196 C CD  . GLN A 185 ? 161.3309 161.3309 161.3309 0.0000 0.0000 0.0000 185 GLN A CD  
1197 O OE1 . GLN A 185 ? 161.3310 161.3310 161.3310 0.0000 0.0000 0.0000 185 GLN A OE1 
1198 N NE2 . GLN A 185 ? 161.3879 161.3879 161.3879 0.0000 0.0000 0.0000 185 GLN A NE2 
1199 N N   . GLY A 186 ? 161.2312 161.2312 161.2312 0.0000 0.0000 0.0000 186 GLY A N   
1200 C CA  . GLY A 186 ? 161.2973 161.2973 161.2973 0.0000 0.0000 0.0000 186 GLY A CA  
1201 C C   . GLY A 186 ? 161.3761 161.3761 161.3761 0.0000 0.0000 0.0000 186 GLY A C   
1202 O O   . GLY A 186 ? 161.6974 161.6974 161.6974 0.0000 0.0000 0.0000 186 GLY A O   
1203 N N   . ASN A 187 ? 161.2779 161.2779 161.2779 0.0000 0.0000 0.0000 187 ASN A N   
1204 C CA  . ASN A 187 ? 161.2394 161.2394 161.2394 0.0000 0.0000 0.0000 187 ASN A CA  
1205 C C   . ASN A 187 ? 161.3495 161.3495 161.3495 0.0000 0.0000 0.0000 187 ASN A C   
1206 O O   . ASN A 187 ? 161.6299 161.6299 161.6299 0.0000 0.0000 0.0000 187 ASN A O   
1207 C CB  . ASN A 187 ? 161.3905 161.3905 161.3905 0.0000 0.0000 0.0000 187 ASN A CB  
1208 C CG  . ASN A 187 ? 161.4519 161.4519 161.4519 0.0000 0.0000 0.0000 187 ASN A CG  
1209 O OD1 . ASN A 187 ? 161.5839 161.5839 161.5839 0.0000 0.0000 0.0000 187 ASN A OD1 
1210 N ND2 . ASN A 187 ? 161.6017 161.6017 161.6017 0.0000 0.0000 0.0000 187 ASN A ND2 
1211 N N   . PRO A 188 ? 161.2354 161.2354 161.2354 0.0000 0.0000 0.0000 188 PRO A N   
1212 C CA  . PRO A 188 ? 161.2738 161.2738 161.2738 0.0000 0.0000 0.0000 188 PRO A CA  
1213 C C   . PRO A 188 ? 161.2813 161.2813 161.2813 0.0000 0.0000 0.0000 188 PRO A C   
1214 O O   . PRO A 188 ? 161.5699 161.5699 161.5699 0.0000 0.0000 0.0000 188 PRO A O   
1215 C CB  . PRO A 188 ? 161.4697 161.4697 161.4697 0.0000 0.0000 0.0000 188 PRO A CB  
1216 C CG  . PRO A 188 ? 161.5740 161.5740 161.5740 0.0000 0.0000 0.0000 188 PRO A CG  
1217 C CD  . PRO A 188 ? 161.5578 161.5578 161.5578 0.0000 0.0000 0.0000 188 PRO A CD  
1218 N N   . GLY A 189 ? 161.2152 161.2152 161.2152 0.0000 0.0000 0.0000 189 GLY A N   
1219 C CA  . GLY A 189 ? 161.3397 161.3397 161.3397 0.0000 0.0000 0.0000 189 GLY A CA  
1220 C C   . GLY A 189 ? 161.3241 161.3241 161.3241 0.0000 0.0000 0.0000 189 GLY A C   
1221 O O   . GLY A 189 ? 161.5375 161.5375 161.5375 0.0000 0.0000 0.0000 189 GLY A O   
1222 N N   . LYS A 190 ? 161.3467 161.3467 161.3467 0.0000 0.0000 0.0000 190 LYS A N   
1223 C CA  . LYS A 190 ? 161.3377 161.3377 161.3377 0.0000 0.0000 0.0000 190 LYS A CA  
1224 C C   . LYS A 190 ? 161.3668 161.3668 161.3668 0.0000 0.0000 0.0000 190 LYS A C   
1225 O O   . LYS A 190 ? 161.5632 161.5632 161.5632 0.0000 0.0000 0.0000 190 LYS A O   
1226 C CB  . LYS A 190 ? 161.4843 161.4843 161.4843 0.0000 0.0000 0.0000 190 LYS A CB  
1227 C CG  . LYS A 190 ? 161.6293 161.6293 161.6293 0.0000 0.0000 0.0000 190 LYS A CG  
1228 C CD  . LYS A 190 ? 161.5206 161.5206 161.5206 0.0000 0.0000 0.0000 190 LYS A CD  
1229 C CE  . LYS A 190 ? 161.3170 161.3170 161.3170 0.0000 0.0000 0.0000 190 LYS A CE  
1230 N NZ  . LYS A 190 ? 161.4158 161.4158 161.4158 0.0000 0.0000 0.0000 190 LYS A NZ  
1231 N N   . THR A 191 ? 161.2833 161.2833 161.2833 0.0000 0.0000 0.0000 191 THR A N   
1232 C CA  . THR A 191 ? 160.6510 160.6510 160.6510 0.0000 0.0000 0.0000 191 THR A CA  
1233 C C   . THR A 191 ? 161.1766 161.1766 161.1766 0.0000 0.0000 0.0000 191 THR A C   
1234 O O   . THR A 191 ? 161.8467 161.8467 161.8467 0.0000 0.0000 0.0000 191 THR A O   
1235 C CB  . THR A 191 ? 160.0944 160.0944 160.0944 0.0000 0.0000 0.0000 191 THR A CB  
1236 O OG1 . THR A 191 ? 160.4277 160.4277 160.4277 0.0000 0.0000 0.0000 191 THR A OG1 
1237 C CG2 . THR A 191 ? 160.7052 160.7052 160.7052 0.0000 0.0000 0.0000 191 THR A CG2 
1238 N N   . LYS A 192 ? 167.5591 167.5591 167.5591 0.0000 0.0000 0.0000 192 LYS A N   
1239 C CA  . LYS A 192 ? 168.0025 168.0025 168.0025 0.0000 0.0000 0.0000 192 LYS A CA  
1240 C C   . LYS A 192 ? 168.3647 168.3647 168.3647 0.0000 0.0000 0.0000 192 LYS A C   
1241 O O   . LYS A 192 ? 168.7249 168.7249 168.7249 0.0000 0.0000 0.0000 192 LYS A O   
1242 C CB  . LYS A 192 ? 167.8695 167.8695 167.8695 0.0000 0.0000 0.0000 192 LYS A CB  
1243 C CG  . LYS A 192 ? 168.2285 168.2285 168.2285 0.0000 0.0000 0.0000 192 LYS A CG  
1244 C CD  . LYS A 192 ? 167.7253 167.7253 167.7253 0.0000 0.0000 0.0000 192 LYS A CD  
1245 C CE  . LYS A 192 ? 168.4300 168.4300 168.4300 0.0000 0.0000 0.0000 192 LYS A CE  
1246 N NZ  . LYS A 192 ? 168.6723 168.6723 168.6723 0.0000 0.0000 0.0000 192 LYS A NZ  
1247 N N   . LYS A 193 ? 167.4966 167.4966 167.4966 0.0000 0.0000 0.0000 193 LYS A N   
1248 C CA  . LYS A 193 ? 167.5257 167.5257 167.5257 0.0000 0.0000 0.0000 193 LYS A CA  
1249 C C   . LYS A 193 ? 167.3310 167.3310 167.3310 0.0000 0.0000 0.0000 193 LYS A C   
1250 O O   . LYS A 193 ? 167.1247 167.1247 167.1247 0.0000 0.0000 0.0000 193 LYS A O   
1251 C CB  . LYS A 193 ? 166.4149 166.4149 166.4149 0.0000 0.0000 0.0000 193 LYS A CB  
1252 C CG  . LYS A 193 ? 166.0851 166.0851 166.0851 0.0000 0.0000 0.0000 193 LYS A CG  
1253 C CD  . LYS A 193 ? 166.6913 166.6913 166.6913 0.0000 0.0000 0.0000 193 LYS A CD  
1254 C CE  . LYS A 193 ? 166.9117 166.9117 166.9117 0.0000 0.0000 0.0000 193 LYS A CE  
1255 N NZ  . LYS A 193 ? 165.5622 165.5622 165.5622 0.0000 0.0000 0.0000 193 LYS A NZ  
1256 N N   . GLY A 194 ? 161.8566 161.8566 161.8566 0.0000 0.0000 0.0000 194 GLY A N   
1257 C CA  . GLY A 194 ? 161.7425 161.7425 161.7425 0.0000 0.0000 0.0000 194 GLY A CA  
1258 C C   . GLY A 194 ? 161.5497 161.5497 161.5497 0.0000 0.0000 0.0000 194 GLY A C   
1259 O O   . GLY A 194 ? 161.6023 161.6023 161.6023 0.0000 0.0000 0.0000 194 GLY A O   
1260 N N   . GLU A 195 ? 161.1740 161.1740 161.1740 0.0000 0.0000 0.0000 195 GLU A N   
1261 C CA  . GLU A 195 ? 161.0426 161.0426 161.0426 0.0000 0.0000 0.0000 195 GLU A CA  
1262 C C   . GLU A 195 ? 161.1830 161.1830 161.1830 0.0000 0.0000 0.0000 195 GLU A C   
1263 O O   . GLU A 195 ? 161.2973 161.2973 161.2973 0.0000 0.0000 0.0000 195 GLU A O   
1264 C CB  . GLU A 195 ? 160.3055 160.3055 160.3055 0.0000 0.0000 0.0000 195 GLU A CB  
1265 C CG  . GLU A 195 ? 160.3150 160.3150 160.3150 0.0000 0.0000 0.0000 195 GLU A CG  
1266 C CD  . GLU A 195 ? 160.3095 160.3095 160.3095 0.0000 0.0000 0.0000 195 GLU A CD  
1267 O OE1 . GLU A 195 ? 160.0884 160.0884 160.0884 0.0000 0.0000 0.0000 195 GLU A OE1 
1268 O OE2 . GLU A 195 ? 160.9287 160.9287 160.9287 0.0000 0.0000 0.0000 195 GLU A OE2 
1269 N N   . LEU A 196 ? 161.3245 161.3245 161.3245 0.0000 0.0000 0.0000 196 LEU A N   
1270 C CA  . LEU A 196 ? 161.3910 161.3910 161.3910 0.0000 0.0000 0.0000 196 LEU A CA  
1271 C C   . LEU A 196 ? 161.3698 161.3698 161.3698 0.0000 0.0000 0.0000 196 LEU A C   
1272 O O   . LEU A 196 ? 161.5109 161.5109 161.5109 0.0000 0.0000 0.0000 196 LEU A O   
1273 C CB  . LEU A 196 ? 161.3572 161.3572 161.3572 0.0000 0.0000 0.0000 196 LEU A CB  
1274 C CG  . LEU A 196 ? 161.2186 161.2186 161.2186 0.0000 0.0000 0.0000 196 LEU A CG  
1275 C CD1 . LEU A 196 ? 161.3696 161.3696 161.3696 0.0000 0.0000 0.0000 196 LEU A CD1 
1276 C CD2 . LEU A 196 ? 161.4806 161.4806 161.4806 0.0000 0.0000 0.0000 196 LEU A CD2 
1277 N N   . SER A 197 ? 161.4155 161.4155 161.4155 0.0000 0.0000 0.0000 197 SER A N   
1278 C CA  . SER A 197 ? 161.3465 161.3465 161.3465 0.0000 0.0000 0.0000 197 SER A CA  
1279 C C   . SER A 197 ? 161.3194 161.3194 161.3194 0.0000 0.0000 0.0000 197 SER A C   
1280 O O   . SER A 197 ? 161.5790 161.5790 161.5790 0.0000 0.0000 0.0000 197 SER A O   
1281 C CB  . SER A 197 ? 161.4637 161.4637 161.4637 0.0000 0.0000 0.0000 197 SER A CB  
1282 O OG  . SER A 197 ? 161.4302 161.4302 161.4302 0.0000 0.0000 0.0000 197 SER A OG  
1283 N N   . ILE A 198 ? 161.2299 161.2299 161.2299 0.0000 0.0000 0.0000 198 ILE A N   
1284 C CA  . ILE A 198 ? 161.2573 161.2573 161.2573 0.0000 0.0000 0.0000 198 ILE A CA  
1285 C C   . ILE A 198 ? 161.3208 161.3208 161.3208 0.0000 0.0000 0.0000 198 ILE A C   
1286 O O   . ILE A 198 ? 161.4244 161.4244 161.4244 0.0000 0.0000 0.0000 198 ILE A O   
1287 C CB  . ILE A 198 ? 161.2655 161.2655 161.2655 0.0000 0.0000 0.0000 198 ILE A CB  
1288 C CG1 . ILE A 198 ? 161.4224 161.4224 161.4224 0.0000 0.0000 0.0000 198 ILE A CG1 
1289 C CG2 . ILE A 198 ? 161.5395 161.5395 161.5395 0.0000 0.0000 0.0000 198 ILE A CG2 
1290 C CD1 . ILE A 198 ? 161.4909 161.4909 161.4909 0.0000 0.0000 0.0000 198 ILE A CD1 
1291 N N   . ILE A 199 ? 161.2917 161.2917 161.2917 0.0000 0.0000 0.0000 199 ILE A N   
1292 C CA  . ILE A 199 ? 161.2049 161.2049 161.2049 0.0000 0.0000 0.0000 199 ILE A CA  
1293 C C   . ILE A 199 ? 161.2733 161.2733 161.2733 0.0000 0.0000 0.0000 199 ILE A C   
1294 O O   . ILE A 199 ? 161.4828 161.4828 161.4828 0.0000 0.0000 0.0000 199 ILE A O   
1295 C CB  . ILE A 199 ? 161.2816 161.2816 161.2816 0.0000 0.0000 0.0000 199 ILE A CB  
1296 C CG1 . ILE A 199 ? 161.3427 161.3427 161.3427 0.0000 0.0000 0.0000 199 ILE A CG1 
1297 C CG2 . ILE A 199 ? 161.5662 161.5662 161.5662 0.0000 0.0000 0.0000 199 ILE A CG2 
1298 C CD1 . ILE A 199 ? 161.5681 161.5681 161.5681 0.0000 0.0000 0.0000 199 ILE A CD1 
1299 N N   . PRO A 200 ? 161.1994 161.1994 161.1994 0.0000 0.0000 0.0000 200 PRO A N   
1300 C CA  . PRO A 200 ? 161.2973 161.2973 161.2973 0.0000 0.0000 0.0000 200 PRO A CA  
1301 C C   . PRO A 200 ? 161.2755 161.2755 161.2755 0.0000 0.0000 0.0000 200 PRO A C   
1302 O O   . PRO A 200 ? 161.4110 161.4110 161.4110 0.0000 0.0000 0.0000 200 PRO A O   
1303 C CB  . PRO A 200 ? 161.3966 161.3966 161.3966 0.0000 0.0000 0.0000 200 PRO A CB  
1304 C CG  . PRO A 200 ? 161.4259 161.4259 161.4259 0.0000 0.0000 0.0000 200 PRO A CG  
1305 C CD  . PRO A 200 ? 161.4411 161.4411 161.4411 0.0000 0.0000 0.0000 200 PRO A CD  
1306 N N   . TYR A 201 ? 161.3765 161.3765 161.3765 0.0000 0.0000 0.0000 201 TYR A N   
1307 C CA  . TYR A 201 ? 161.2643 161.2643 161.2643 0.0000 0.0000 0.0000 201 TYR A CA  
1308 C C   . TYR A 201 ? 161.1771 161.1771 161.1771 0.0000 0.0000 0.0000 201 TYR A C   
1309 O O   . TYR A 201 ? 161.3482 161.3482 161.3482 0.0000 0.0000 0.0000 201 TYR A O   
1310 C CB  . TYR A 201 ? 161.3837 161.3837 161.3837 0.0000 0.0000 0.0000 201 TYR A CB  
1311 C CG  . TYR A 201 ? 161.2145 161.2145 161.2145 0.0000 0.0000 0.0000 201 TYR A CG  
1312 C CD1 . TYR A 201 ? 161.3981 161.3981 161.3981 0.0000 0.0000 0.0000 201 TYR A CD1 
1313 C CD2 . TYR A 201 ? 161.2769 161.2769 161.2769 0.0000 0.0000 0.0000 201 TYR A CD2 
1314 C CE1 . TYR A 201 ? 161.5338 161.5338 161.5338 0.0000 0.0000 0.0000 201 TYR A CE1 
1315 C CE2 . TYR A 201 ? 161.3928 161.3928 161.3928 0.0000 0.0000 0.0000 201 TYR A CE2 
1316 C CZ  . TYR A 201 ? 161.5307 161.5307 161.5307 0.0000 0.0000 0.0000 201 TYR A CZ  
1317 O OH  . TYR A 201 ? 161.5100 161.5100 161.5100 0.0000 0.0000 0.0000 201 TYR A OH  
1318 N N   . GLU A 202 ? 161.1521 161.1521 161.1521 0.0000 0.0000 0.0000 202 GLU A N   
1319 C CA  . GLU A 202 ? 161.3401 161.3401 161.3401 0.0000 0.0000 0.0000 202 GLU A CA  
1320 C C   . GLU A 202 ? 161.3920 161.3920 161.3920 0.0000 0.0000 0.0000 202 GLU A C   
1321 O O   . GLU A 202 ? 161.6871 161.6871 161.6871 0.0000 0.0000 0.0000 202 GLU A O   
1322 C CB  . GLU A 202 ? 161.4194 161.4194 161.4194 0.0000 0.0000 0.0000 202 GLU A CB  
1323 C CG  . GLU A 202 ? 161.4917 161.4917 161.4917 0.0000 0.0000 0.0000 202 GLU A CG  
1324 C CD  . GLU A 202 ? 161.5041 161.5041 161.5041 0.0000 0.0000 0.0000 202 GLU A CD  
1325 O OE1 . GLU A 202 ? 161.4722 161.4722 161.4722 0.0000 0.0000 0.0000 202 GLU A OE1 
1326 O OE2 . GLU A 202 ? 161.5643 161.5643 161.5643 0.0000 0.0000 0.0000 202 GLU A OE2 
1327 N N   . ILE A 203 ? 161.3015 161.3015 161.3015 0.0000 0.0000 0.0000 203 ILE A N   
1328 C CA  . ILE A 203 ? 161.1922 161.1922 161.1922 0.0000 0.0000 0.0000 203 ILE A CA  
1329 C C   . ILE A 203 ? 161.2829 161.2829 161.2829 0.0000 0.0000 0.0000 203 ILE A C   
1330 O O   . ILE A 203 ? 161.5530 161.5530 161.5530 0.0000 0.0000 0.0000 203 ILE A O   
1331 C CB  . ILE A 203 ? 161.1620 161.1620 161.1620 0.0000 0.0000 0.0000 203 ILE A CB  
1332 C CG1 . ILE A 203 ? 161.2506 161.2506 161.2506 0.0000 0.0000 0.0000 203 ILE A CG1 
1333 C CG2 . ILE A 203 ? 161.4833 161.4833 161.4833 0.0000 0.0000 0.0000 203 ILE A CG2 
1334 C CD1 . ILE A 203 ? 161.3202 161.3202 161.3202 0.0000 0.0000 0.0000 203 ILE A CD1 
1335 N N   . THR A 204 ? 161.1853 161.1853 161.1853 0.0000 0.0000 0.0000 204 THR A N   
1336 C CA  . THR A 204 ? 161.2586 161.2586 161.2586 0.0000 0.0000 0.0000 204 THR A CA  
1337 C C   . THR A 204 ? 161.2962 161.2962 161.2962 0.0000 0.0000 0.0000 204 THR A C   
1338 O O   . THR A 204 ? 161.6247 161.6247 161.6247 0.0000 0.0000 0.0000 204 THR A O   
1339 C CB  . THR A 204 ? 161.4436 161.4436 161.4436 0.0000 0.0000 0.0000 204 THR A CB  
1340 O OG1 . THR A 204 ? 161.5224 161.5224 161.5224 0.0000 0.0000 0.0000 204 THR A OG1 
1341 C CG2 . THR A 204 ? 161.4945 161.4945 161.4945 0.0000 0.0000 0.0000 204 THR A CG2 
1342 N N   . LEU A 205 ? 161.2411 161.2411 161.2411 0.0000 0.0000 0.0000 205 LEU A N   
1343 C CA  . LEU A 205 ? 161.1555 161.1555 161.1555 0.0000 0.0000 0.0000 205 LEU A CA  
1344 C C   . LEU A 205 ? 161.3428 161.3428 161.3428 0.0000 0.0000 0.0000 205 LEU A C   
1345 O O   . LEU A 205 ? 161.5513 161.5513 161.5513 0.0000 0.0000 0.0000 205 LEU A O   
1346 C CB  . LEU A 205 ? 161.2538 161.2538 161.2538 0.0000 0.0000 0.0000 205 LEU A CB  
1347 C CG  . LEU A 205 ? 161.2848 161.2848 161.2848 0.0000 0.0000 0.0000 205 LEU A CG  
1348 C CD1 . LEU A 205 ? 161.4646 161.4646 161.4646 0.0000 0.0000 0.0000 205 LEU A CD1 
1349 C CD2 . LEU A 205 ? 161.4349 161.4349 161.4349 0.0000 0.0000 0.0000 205 LEU A CD2 
1350 N N   . LEU A 206 ? 161.3974 161.3974 161.3974 0.0000 0.0000 0.0000 206 LEU A N   
1351 C CA  . LEU A 206 ? 160.7879 160.7879 160.7879 0.0000 0.0000 0.0000 206 LEU A CA  
1352 C C   . LEU A 206 ? 160.7228 160.7228 160.7228 0.0000 0.0000 0.0000 206 LEU A C   
1353 O O   . LEU A 206 ? 160.8746 160.8746 160.8746 0.0000 0.0000 0.0000 206 LEU A O   
1354 C CB  . LEU A 206 ? 160.6244 160.6244 160.6244 0.0000 0.0000 0.0000 206 LEU A CB  
1355 C CG  . LEU A 206 ? 160.7811 160.7811 160.7811 0.0000 0.0000 0.0000 206 LEU A CG  
1356 C CD1 . LEU A 206 ? 160.9719 160.9719 160.9719 0.0000 0.0000 0.0000 206 LEU A CD1 
1357 C CD2 . LEU A 206 ? 160.9548 160.9548 160.9548 0.0000 0.0000 0.0000 206 LEU A CD2 
1358 N N   . SER A 207 ? 161.0590 161.0590 161.0590 0.0000 0.0000 0.0000 207 SER A N   
1359 C CA  . SER A 207 ? 160.8999 160.8999 160.8999 0.0000 0.0000 0.0000 207 SER A CA  
1360 C C   . SER A 207 ? 161.0289 161.0289 161.0289 0.0000 0.0000 0.0000 207 SER A C   
1361 O O   . SER A 207 ? 161.2225 161.2225 161.2225 0.0000 0.0000 0.0000 207 SER A O   
1362 C CB  . SER A 207 ? 159.1960 159.1960 159.1960 0.0000 0.0000 0.0000 207 SER A CB  
1363 O OG  . SER A 207 ? 158.4096 158.4096 158.4096 0.0000 0.0000 0.0000 207 SER A OG  
1364 N N   . PRO A 208 ? 161.1781 161.1781 161.1781 0.0000 0.0000 0.0000 208 PRO A N   
1365 C CA  . PRO A 208 ? 161.2684 161.2684 161.2684 0.0000 0.0000 0.0000 208 PRO A CA  
1366 C C   . PRO A 208 ? 161.0711 161.0711 161.0711 0.0000 0.0000 0.0000 208 PRO A C   
1367 O O   . PRO A 208 ? 160.8428 160.8428 160.8428 0.0000 0.0000 0.0000 208 PRO A O   
1368 C CB  . PRO A 208 ? 161.2926 161.2926 161.2926 0.0000 0.0000 0.0000 208 PRO A CB  
1369 C CG  . PRO A 208 ? 161.2585 161.2585 161.2585 0.0000 0.0000 0.0000 208 PRO A CG  
1370 C CD  . PRO A 208 ? 161.3755 161.3755 161.3755 0.0000 0.0000 0.0000 208 PRO A CD  
1371 N N   . CYS A 209 ? 161.1326 161.1326 161.1326 0.0000 0.0000 0.0000 209 CYS A N   
1372 C CA  . CYS A 209 ? 160.7010 160.7010 160.7010 0.0000 0.0000 0.0000 209 CYS A CA  
1373 C C   . CYS A 209 ? 161.3577 161.3577 161.3577 0.0000 0.0000 0.0000 209 CYS A C   
1374 O O   . CYS A 209 ? 161.7593 161.7593 161.7593 0.0000 0.0000 0.0000 209 CYS A O   
1375 C CB  . CYS A 209 ? 161.2594 161.2594 161.2594 0.0000 0.0000 0.0000 209 CYS A CB  
1376 S SG  . CYS A 209 ? 161.2044 161.2044 161.2044 0.0000 0.0000 0.0000 209 CYS A SG  
1377 N N   . LEU A 210 ? 161.3494 161.3494 161.3494 0.0000 0.0000 0.0000 210 LEU A N   
1378 C CA  . LEU A 210 ? 161.3301 161.3301 161.3301 0.0000 0.0000 0.0000 210 LEU A CA  
1379 C C   . LEU A 210 ? 161.3661 161.3661 161.3661 0.0000 0.0000 0.0000 210 LEU A C   
1380 O O   . LEU A 210 ? 161.4779 161.4779 161.4779 0.0000 0.0000 0.0000 210 LEU A O   
1381 C CB  . LEU A 210 ? 161.2251 161.2251 161.2251 0.0000 0.0000 0.0000 210 LEU A CB  
1382 C CG  . LEU A 210 ? 161.2405 161.2405 161.2405 0.0000 0.0000 0.0000 210 LEU A CG  
1383 C CD1 . LEU A 210 ? 161.4056 161.4056 161.4056 0.0000 0.0000 0.0000 210 LEU A CD1 
1384 C CD2 . LEU A 210 ? 161.4710 161.4710 161.4710 0.0000 0.0000 0.0000 210 LEU A CD2 
1385 N N   . HIS A 211 ? 161.3415 161.3415 161.3415 0.0000 0.0000 0.0000 211 HIS A N   
1386 C CA  . HIS A 211 ? 161.3046 161.3046 161.3046 0.0000 0.0000 0.0000 211 HIS A CA  
1387 C C   . HIS A 211 ? 161.3241 161.3241 161.3241 0.0000 0.0000 0.0000 211 HIS A C   
1388 O O   . HIS A 211 ? 161.5560 161.5560 161.5560 0.0000 0.0000 0.0000 211 HIS A O   
1389 C CB  . HIS A 211 ? 160.9079 160.9079 160.9079 0.0000 0.0000 0.0000 211 HIS A CB  
1390 C CG  . HIS A 211 ? 160.8385 160.8385 160.8385 0.0000 0.0000 0.0000 211 HIS A CG  
1391 N ND1 . HIS A 211 ? 160.7889 160.7889 160.7889 0.0000 0.0000 0.0000 211 HIS A ND1 
1392 C CD2 . HIS A 211 ? 160.9411 160.9411 160.9411 0.0000 0.0000 0.0000 211 HIS A CD2 
1393 C CE1 . HIS A 211 ? 161.3169 161.3169 161.3169 0.0000 0.0000 0.0000 211 HIS A CE1 
1394 N NE2 . HIS A 211 ? 161.0438 161.0438 161.0438 0.0000 0.0000 0.0000 211 HIS A NE2 
1395 N N   . MET A 212 ? 161.2272 161.2272 161.2272 0.0000 0.0000 0.0000 212 MET A N   
1396 C CA  . MET A 212 ? 161.0425 161.0425 161.0425 0.0000 0.0000 0.0000 212 MET A CA  
1397 C C   . MET A 212 ? 161.0490 161.0490 161.0490 0.0000 0.0000 0.0000 212 MET A C   
1398 O O   . MET A 212 ? 160.8694 160.8694 160.8694 0.0000 0.0000 0.0000 212 MET A O   
1399 C CB  . MET A 212 ? 159.4624 159.4624 159.4624 0.0000 0.0000 0.0000 212 MET A CB  
1400 C CG  . MET A 212 ? 159.2393 159.2393 159.2393 0.0000 0.0000 0.0000 212 MET A CG  
1401 S SD  . MET A 212 ? 156.1133 156.1133 156.1133 0.0000 0.0000 0.0000 212 MET A SD  
1402 C CE  . MET A 212 ? 158.4160 158.4160 158.4160 0.0000 0.0000 0.0000 212 MET A CE  
1403 N N   . LEU A 213 ? 161.2680 161.2680 161.2680 0.0000 0.0000 0.0000 213 LEU A N   
1404 C CA  . LEU A 213 ? 161.3967 161.3967 161.3967 0.0000 0.0000 0.0000 213 LEU A CA  
1405 C C   . LEU A 213 ? 161.0203 161.0203 161.0203 0.0000 0.0000 0.0000 213 LEU A C   
1406 O O   . LEU A 213 ? 160.4236 160.4236 160.4236 0.0000 0.0000 0.0000 213 LEU A O   
1407 C CB  . LEU A 213 ? 161.3010 161.3010 161.3010 0.0000 0.0000 0.0000 213 LEU A CB  
1408 C CG  . LEU A 213 ? 161.2829 161.2829 161.2829 0.0000 0.0000 0.0000 213 LEU A CG  
1409 C CD1 . LEU A 213 ? 161.3197 161.3197 161.3197 0.0000 0.0000 0.0000 213 LEU A CD1 
1410 C CD2 . LEU A 213 ? 161.4013 161.4013 161.4013 0.0000 0.0000 0.0000 213 LEU A CD2 
1411 N N   . PRO A 214 ? 161.0538 161.0538 161.0538 0.0000 0.0000 0.0000 214 PRO A N   
1412 C CA  . PRO A 214 ? 160.5888 160.5888 160.5888 0.0000 0.0000 0.0000 214 PRO A CA  
1413 C C   . PRO A 214 ? 161.1596 161.1596 161.1596 0.0000 0.0000 0.0000 214 PRO A C   
1414 O O   . PRO A 214 ? 161.3967 161.3967 161.3967 0.0000 0.0000 0.0000 214 PRO A O   
1415 C CB  . PRO A 214 ? 159.9666 159.9666 159.9666 0.0000 0.0000 0.0000 214 PRO A CB  
1416 C CG  . PRO A 214 ? 159.6943 159.6943 159.6943 0.0000 0.0000 0.0000 214 PRO A CG  
1417 C CD  . PRO A 214 ? 161.2580 161.2580 161.2580 0.0000 0.0000 0.0000 214 PRO A CD  
1418 N N   . HIS A 215 ? 162.9109 162.9109 162.9109 0.0000 0.0000 0.0000 215 HIS A N   
1419 C CA  . HIS A 215 ? 163.2295 163.2295 163.2295 0.0000 0.0000 0.0000 215 HIS A CA  
1420 C C   . HIS A 215 ? 163.5166 163.5166 163.5166 0.0000 0.0000 0.0000 215 HIS A C   
1421 O O   . HIS A 215 ? 163.6711 163.6711 163.6711 0.0000 0.0000 0.0000 215 HIS A O   
1422 C CB  . HIS A 215 ? 162.2414 162.2414 162.2414 0.0000 0.0000 0.0000 215 HIS A CB  
1423 C CG  . HIS A 215 ? 162.1603 162.1603 162.1603 0.0000 0.0000 0.0000 215 HIS A CG  
1424 N ND1 . HIS A 215 ? 162.0996 162.0996 162.0996 0.0000 0.0000 0.0000 215 HIS A ND1 
1425 C CD2 . HIS A 215 ? 161.4929 161.4929 161.4929 0.0000 0.0000 0.0000 215 HIS A CD2 
1426 C CE1 . HIS A 215 ? 160.8885 160.8885 160.8885 0.0000 0.0000 0.0000 215 HIS A CE1 
1427 N NE2 . HIS A 215 ? 160.9455 160.9455 160.9455 0.0000 0.0000 0.0000 215 HIS A NE2 
1428 N N   . LEU A 216 ? 161.6095 161.6095 161.6095 0.0000 0.0000 0.0000 216 LEU A N   
1429 C CA  . LEU A 216 ? 161.4279 161.4279 161.4279 0.0000 0.0000 0.0000 216 LEU A CA  
1430 C C   . LEU A 216 ? 161.3537 161.3537 161.3537 0.0000 0.0000 0.0000 216 LEU A C   
1431 O O   . LEU A 216 ? 161.4451 161.4451 161.4451 0.0000 0.0000 0.0000 216 LEU A O   
1432 C CB  . LEU A 216 ? 161.4059 161.4059 161.4059 0.0000 0.0000 0.0000 216 LEU A CB  
1433 C CG  . LEU A 216 ? 161.4028 161.4028 161.4028 0.0000 0.0000 0.0000 216 LEU A CG  
1434 C CD1 . LEU A 216 ? 161.4012 161.4012 161.4012 0.0000 0.0000 0.0000 216 LEU A CD1 
1435 C CD2 . LEU A 216 ? 161.6071 161.6071 161.6071 0.0000 0.0000 0.0000 216 LEU A CD2 
1436 N N   . HIS A 217 ? 161.2487 161.2487 161.2487 0.0000 0.0000 0.0000 217 HIS A N   
1437 C CA  . HIS A 217 ? 161.2632 161.2632 161.2632 0.0000 0.0000 0.0000 217 HIS A CA  
1438 C C   . HIS A 217 ? 161.4493 161.4493 161.4493 0.0000 0.0000 0.0000 217 HIS A C   
1439 O O   . HIS A 217 ? 161.5367 161.5367 161.5367 0.0000 0.0000 0.0000 217 HIS A O   
1440 C CB  . HIS A 217 ? 159.5099 159.5099 159.5099 0.0000 0.0000 0.0000 217 HIS A CB  
1441 C CG  . HIS A 217 ? 159.1836 159.1836 159.1836 0.0000 0.0000 0.0000 217 HIS A CG  
1442 N ND1 . HIS A 217 ? 158.9285 158.9285 158.9285 0.0000 0.0000 0.0000 217 HIS A ND1 
1443 C CD2 . HIS A 217 ? 158.7944 158.7944 158.7944 0.0000 0.0000 0.0000 217 HIS A CD2 
1444 C CE1 . HIS A 217 ? 158.4174 158.4174 158.4174 0.0000 0.0000 0.0000 217 HIS A CE1 
1445 N NE2 . HIS A 217 ? 158.2101 158.2101 158.2101 0.0000 0.0000 0.0000 217 HIS A NE2 
1446 N N   . PHE A 218 ? 161.4870 161.4870 161.4870 0.0000 0.0000 0.0000 218 PHE A N   
1447 C CA  . PHE A 218 ? 160.8323 160.8323 160.8323 0.0000 0.0000 0.0000 218 PHE A CA  
1448 C C   . PHE A 218 ? 160.7478 160.7478 160.7478 0.0000 0.0000 0.0000 218 PHE A C   
1449 O O   . PHE A 218 ? 160.8287 160.8287 160.8287 0.0000 0.0000 0.0000 218 PHE A O   
1450 C CB  . PHE A 218 ? 159.6019 159.6019 159.6019 0.0000 0.0000 0.0000 218 PHE A CB  
1451 C CG  . PHE A 218 ? 160.0067 160.0067 160.0067 0.0000 0.0000 0.0000 218 PHE A CG  
1452 C CD1 . PHE A 218 ? 159.7409 159.7409 159.7409 0.0000 0.0000 0.0000 218 PHE A CD1 
1453 C CD2 . PHE A 218 ? 158.8940 158.8940 158.8940 0.0000 0.0000 0.0000 218 PHE A CD2 
1454 C CE1 . PHE A 218 ? 159.3962 159.3962 159.3962 0.0000 0.0000 0.0000 218 PHE A CE1 
1455 C CE2 . PHE A 218 ? 158.4811 158.4811 158.4811 0.0000 0.0000 0.0000 218 PHE A CE2 
1456 C CZ  . PHE A 218 ? 158.1935 158.1935 158.1935 0.0000 0.0000 0.0000 218 PHE A CZ  
1457 N N   . GLY A 219 ? 166.1830 166.1830 166.1830 0.0000 0.0000 0.0000 219 GLY A N   
1458 C CA  . GLY A 219 ? 166.3074 166.3074 166.3074 0.0000 0.0000 0.0000 219 GLY A CA  
1459 C C   . GLY A 219 ? 165.5219 165.5219 165.5219 0.0000 0.0000 0.0000 219 GLY A C   
1460 O O   . GLY A 219 ? 163.3229 163.3229 163.3229 0.0000 0.0000 0.0000 219 GLY A O   
1461 N N   . LEU A 220 ? 161.1915 161.1915 161.1915 0.0000 0.0000 0.0000 220 LEU A N   
1462 C CA  . LEU A 220 ? 160.8506 160.8506 160.8506 0.0000 0.0000 0.0000 220 LEU A CA  
1463 C C   . LEU A 220 ? 160.9034 160.9034 160.9034 0.0000 0.0000 0.0000 220 LEU A C   
1464 O O   . LEU A 220 ? 161.4851 161.4851 161.4851 0.0000 0.0000 0.0000 220 LEU A O   
1465 C CB  . LEU A 220 ? 161.4086 161.4086 161.4086 0.0000 0.0000 0.0000 220 LEU A CB  
1466 C CG  . LEU A 220 ? 161.1606 161.1606 161.1606 0.0000 0.0000 0.0000 220 LEU A CG  
1467 C CD1 . LEU A 220 ? 159.9752 159.9752 159.9752 0.0000 0.0000 0.0000 220 LEU A CD1 
1468 C CD2 . LEU A 220 ? 161.3855 161.3855 161.3855 0.0000 0.0000 0.0000 220 LEU A CD2 
1469 N N   . LYS A 221 ? 160.0188 160.0188 160.0188 0.0000 0.0000 0.0000 221 LYS A N   
1470 C CA  . LYS A 221 ? 160.6075 160.6075 160.6075 0.0000 0.0000 0.0000 221 LYS A CA  
1471 C C   . LYS A 221 ? 161.3990 161.3990 161.3990 0.0000 0.0000 0.0000 221 LYS A C   
1472 O O   . LYS A 221 ? 161.6424 161.6424 161.6424 0.0000 0.0000 0.0000 221 LYS A O   
1473 C CB  . LYS A 221 ? 160.5225 160.5225 160.5225 0.0000 0.0000 0.0000 221 LYS A CB  
1474 C CG  . LYS A 221 ? 160.9645 160.9645 160.9645 0.0000 0.0000 0.0000 221 LYS A CG  
1475 C CD  . LYS A 221 ? 160.3447 160.3447 160.3447 0.0000 0.0000 0.0000 221 LYS A CD  
1476 C CE  . LYS A 221 ? 160.4625 160.4625 160.4625 0.0000 0.0000 0.0000 221 LYS A CE  
1477 N NZ  . LYS A 221 ? 159.4924 159.4924 159.4924 0.0000 0.0000 0.0000 221 LYS A NZ  
1478 N N   . ASP A 222 ? 170.2725 170.2725 170.2725 0.0000 0.0000 0.0000 222 ASP A N   
1479 C CA  . ASP A 222 ? 170.7511 170.7511 170.7511 0.0000 0.0000 0.0000 222 ASP A CA  
1480 C C   . ASP A 222 ? 170.9419 170.9419 170.9419 0.0000 0.0000 0.0000 222 ASP A C   
1481 O O   . ASP A 222 ? 171.0100 171.0100 171.0100 0.0000 0.0000 0.0000 222 ASP A O   
1482 C CB  . ASP A 222 ? 170.3791 170.3791 170.3791 0.0000 0.0000 0.0000 222 ASP A CB  
1483 C CG  . ASP A 222 ? 171.0868 171.0868 171.0868 0.0000 0.0000 0.0000 222 ASP A CG  
1484 O OD1 . ASP A 222 ? 171.3967 171.3967 171.3967 0.0000 0.0000 0.0000 222 ASP A OD1 
1485 O OD2 . ASP A 222 ? 171.5025 171.5025 171.5025 0.0000 0.0000 0.0000 222 ASP A OD2 
1486 N N   . LYS A 223 ? 163.7397 163.7397 163.7397 0.0000 0.0000 0.0000 223 LYS A N   
1487 C CA  . LYS A 223 ? 163.5513 163.5513 163.5513 0.0000 0.0000 0.0000 223 LYS A CA  
1488 C C   . LYS A 223 ? 163.5878 163.5878 163.5878 0.0000 0.0000 0.0000 223 LYS A C   
1489 O O   . LYS A 223 ? 163.7330 163.7330 163.7330 0.0000 0.0000 0.0000 223 LYS A O   
1490 C CB  . LYS A 223 ? 163.3007 163.3007 163.3007 0.0000 0.0000 0.0000 223 LYS A CB  
1491 C CG  . LYS A 223 ? 163.3819 163.3819 163.3819 0.0000 0.0000 0.0000 223 LYS A CG  
1492 C CD  . LYS A 223 ? 163.4603 163.4603 163.4603 0.0000 0.0000 0.0000 223 LYS A CD  
1493 C CE  . LYS A 223 ? 162.1370 162.1370 162.1370 0.0000 0.0000 0.0000 223 LYS A CE  
1494 N NZ  . LYS A 223 ? 162.6062 162.6062 162.6062 0.0000 0.0000 0.0000 223 LYS A NZ  
1495 N N   . GLU A 224 ? 165.2659 165.2659 165.2659 0.0000 0.0000 0.0000 224 GLU A N   
1496 C CA  . GLU A 224 ? 165.3222 165.3222 165.3222 0.0000 0.0000 0.0000 224 GLU A CA  
1497 C C   . GLU A 224 ? 165.3579 165.3579 165.3579 0.0000 0.0000 0.0000 224 GLU A C   
1498 O O   . GLU A 224 ? 165.3865 165.3865 165.3865 0.0000 0.0000 0.0000 224 GLU A O   
1499 C CB  . GLU A 224 ? 165.0192 165.0192 165.0192 0.0000 0.0000 0.0000 224 GLU A CB  
1500 C CG  . GLU A 224 ? 163.9846 163.9846 163.9846 0.0000 0.0000 0.0000 224 GLU A CG  
1501 C CD  . GLU A 224 ? 164.2851 164.2851 164.2851 0.0000 0.0000 0.0000 224 GLU A CD  
1502 O OE1 . GLU A 224 ? 165.0601 165.0601 165.0601 0.0000 0.0000 0.0000 224 GLU A OE1 
1503 O OE2 . GLU A 224 ? 163.5887 163.5887 163.5887 0.0000 0.0000 0.0000 224 GLU A OE2 
1504 N N   . THR A 225 ? 161.5545 161.5545 161.5545 0.0000 0.0000 0.0000 225 THR A N   
1505 C CA  . THR A 225 ? 161.2973 161.2973 161.2973 0.0000 0.0000 0.0000 225 THR A CA  
1506 C C   . THR A 225 ? 161.3984 161.3984 161.3984 0.0000 0.0000 0.0000 225 THR A C   
1507 O O   . THR A 225 ? 161.6287 161.6287 161.6287 0.0000 0.0000 0.0000 225 THR A O   
1508 C CB  . THR A 225 ? 161.3751 161.3751 161.3751 0.0000 0.0000 0.0000 225 THR A CB  
1509 O OG1 . THR A 225 ? 161.1204 161.1204 161.1204 0.0000 0.0000 0.0000 225 THR A OG1 
1510 C CG2 . THR A 225 ? 161.1748 161.1748 161.1748 0.0000 0.0000 0.0000 225 THR A CG2 
1511 N N   . ARG A 226 ? 161.4168 161.4168 161.4168 0.0000 0.0000 0.0000 226 ARG A N   
1512 C CA  . ARG A 226 ? 161.3435 161.3435 161.3435 0.0000 0.0000 0.0000 226 ARG A CA  
1513 C C   . ARG A 226 ? 161.4564 161.4564 161.4564 0.0000 0.0000 0.0000 226 ARG A C   
1514 O O   . ARG A 226 ? 161.6001 161.6001 161.6001 0.0000 0.0000 0.0000 226 ARG A O   
1515 C CB  . ARG A 226 ? 161.3580 161.3580 161.3580 0.0000 0.0000 0.0000 226 ARG A CB  
1516 C CG  . ARG A 226 ? 161.5792 161.5792 161.5792 0.0000 0.0000 0.0000 226 ARG A CG  
1517 C CD  . ARG A 226 ? 161.6949 161.6949 161.6949 0.0000 0.0000 0.0000 226 ARG A CD  
1518 N NE  . ARG A 226 ? 161.6685 161.6685 161.6685 0.0000 0.0000 0.0000 226 ARG A NE  
1519 C CZ  . ARG A 226 ? 161.5479 161.5479 161.5479 0.0000 0.0000 0.0000 226 ARG A CZ  
1520 N NH1 . ARG A 226 ? 161.3629 161.3629 161.3629 0.0000 0.0000 0.0000 226 ARG A NH1 
1521 N NH2 . ARG A 226 ? 161.5604 161.5604 161.5604 0.0000 0.0000 0.0000 226 ARG A NH2 
1522 N N   . TYR A 227 ? 161.5654 161.5654 161.5654 0.0000 0.0000 0.0000 227 TYR A N   
1523 C CA  . TYR A 227 ? 161.4413 161.4413 161.4413 0.0000 0.0000 0.0000 227 TYR A CA  
1524 C C   . TYR A 227 ? 161.3442 161.3442 161.3442 0.0000 0.0000 0.0000 227 TYR A C   
1525 O O   . TYR A 227 ? 161.3332 161.3332 161.3332 0.0000 0.0000 0.0000 227 TYR A O   
1526 C CB  . TYR A 227 ? 161.4496 161.4496 161.4496 0.0000 0.0000 0.0000 227 TYR A CB  
1527 C CG  . TYR A 227 ? 161.4932 161.4932 161.4932 0.0000 0.0000 0.0000 227 TYR A CG  
1528 C CD1 . TYR A 227 ? 161.5234 161.5234 161.5234 0.0000 0.0000 0.0000 227 TYR A CD1 
1529 C CD2 . TYR A 227 ? 161.2338 161.2338 161.2338 0.0000 0.0000 0.0000 227 TYR A CD2 
1530 C CE1 . TYR A 227 ? 161.3470 161.3470 161.3470 0.0000 0.0000 0.0000 227 TYR A CE1 
1531 C CE2 . TYR A 227 ? 161.0384 161.0384 161.0384 0.0000 0.0000 0.0000 227 TYR A CE2 
1532 C CZ  . TYR A 227 ? 161.3019 161.3019 161.3019 0.0000 0.0000 0.0000 227 TYR A CZ  
1533 O OH  . TYR A 227 ? 161.4378 161.4378 161.4378 0.0000 0.0000 0.0000 227 TYR A OH  
1534 N N   . ARG A 228 ? 161.2863 161.2863 161.2863 0.0000 0.0000 0.0000 228 ARG A N   
1535 C CA  . ARG A 228 ? 161.3111 161.3111 161.3111 0.0000 0.0000 0.0000 228 ARG A CA  
1536 C C   . ARG A 228 ? 161.3287 161.3287 161.3287 0.0000 0.0000 0.0000 228 ARG A C   
1537 O O   . ARG A 228 ? 161.3701 161.3701 161.3701 0.0000 0.0000 0.0000 228 ARG A O   
1538 C CB  . ARG A 228 ? 161.3345 161.3345 161.3345 0.0000 0.0000 0.0000 228 ARG A CB  
1539 C CG  . ARG A 228 ? 161.5497 161.5497 161.5497 0.0000 0.0000 0.0000 228 ARG A CG  
1540 C CD  . ARG A 228 ? 161.7569 161.7569 161.7569 0.0000 0.0000 0.0000 228 ARG A CD  
1541 N NE  . ARG A 228 ? 161.5669 161.5669 161.5669 0.0000 0.0000 0.0000 228 ARG A NE  
1542 C CZ  . ARG A 228 ? 161.0161 161.0161 161.0161 0.0000 0.0000 0.0000 228 ARG A CZ  
1543 N NH1 . ARG A 228 ? 161.8931 161.8931 161.8931 0.0000 0.0000 0.0000 228 ARG A NH1 
1544 N NH2 . ARG A 228 ? 159.6822 159.6822 159.6822 0.0000 0.0000 0.0000 228 ARG A NH2 
1545 N N   . GLN A 229 ? 161.3083 161.3083 161.3083 0.0000 0.0000 0.0000 229 GLN A N   
1546 C CA  . GLN A 229 ? 161.3704 161.3704 161.3704 0.0000 0.0000 0.0000 229 GLN A CA  
1547 C C   . GLN A 229 ? 161.3333 161.3333 161.3333 0.0000 0.0000 0.0000 229 GLN A C   
1548 O O   . GLN A 229 ? 161.4272 161.4272 161.4272 0.0000 0.0000 0.0000 229 GLN A O   
1549 C CB  . GLN A 229 ? 161.3346 161.3346 161.3346 0.0000 0.0000 0.0000 229 GLN A CB  
1550 C CG  . GLN A 229 ? 161.2905 161.2905 161.2905 0.0000 0.0000 0.0000 229 GLN A CG  
1551 C CD  . GLN A 229 ? 161.1234 161.1234 161.1234 0.0000 0.0000 0.0000 229 GLN A CD  
1552 O OE1 . GLN A 229 ? 160.8604 160.8604 160.8604 0.0000 0.0000 0.0000 229 GLN A OE1 
1553 N NE2 . GLN A 229 ? 161.1711 161.1711 161.1711 0.0000 0.0000 0.0000 229 GLN A NE2 
1554 N N   . ARG A 230 ? 161.4219 161.4219 161.4219 0.0000 0.0000 0.0000 230 ARG A N   
1555 C CA  . ARG A 230 ? 161.3713 161.3713 161.3713 0.0000 0.0000 0.0000 230 ARG A CA  
1556 C C   . ARG A 230 ? 161.4198 161.4198 161.4198 0.0000 0.0000 0.0000 230 ARG A C   
1557 O O   . ARG A 230 ? 161.4876 161.4876 161.4876 0.0000 0.0000 0.0000 230 ARG A O   
1558 C CB  . ARG A 230 ? 161.4765 161.4765 161.4765 0.0000 0.0000 0.0000 230 ARG A CB  
1559 C CG  . ARG A 230 ? 161.3427 161.3427 161.3427 0.0000 0.0000 0.0000 230 ARG A CG  
1560 C CD  . ARG A 230 ? 161.3917 161.3917 161.3917 0.0000 0.0000 0.0000 230 ARG A CD  
1561 N NE  . ARG A 230 ? 161.3334 161.3334 161.3334 0.0000 0.0000 0.0000 230 ARG A NE  
1562 C CZ  . ARG A 230 ? 161.3405 161.3405 161.3405 0.0000 0.0000 0.0000 230 ARG A CZ  
1563 N NH1 . ARG A 230 ? 161.4520 161.4520 161.4520 0.0000 0.0000 0.0000 230 ARG A NH1 
1564 N NH2 . ARG A 230 ? 161.4283 161.4283 161.4283 0.0000 0.0000 0.0000 230 ARG A NH2 
1565 N N   . TYR A 231 ? 161.4250 161.4250 161.4250 0.0000 0.0000 0.0000 231 TYR A N   
1566 C CA  . TYR A 231 ? 161.3402 161.3402 161.3402 0.0000 0.0000 0.0000 231 TYR A CA  
1567 C C   . TYR A 231 ? 161.4414 161.4414 161.4414 0.0000 0.0000 0.0000 231 TYR A C   
1568 O O   . TYR A 231 ? 161.6558 161.6558 161.6558 0.0000 0.0000 0.0000 231 TYR A O   
1569 C CB  . TYR A 231 ? 161.4565 161.4565 161.4565 0.0000 0.0000 0.0000 231 TYR A CB  
1570 C CG  . TYR A 231 ? 161.3929 161.3929 161.3929 0.0000 0.0000 0.0000 231 TYR A CG  
1571 C CD1 . TYR A 231 ? 161.3334 161.3334 161.3334 0.0000 0.0000 0.0000 231 TYR A CD1 
1572 C CD2 . TYR A 231 ? 161.4735 161.4735 161.4735 0.0000 0.0000 0.0000 231 TYR A CD2 
1573 C CE1 . TYR A 231 ? 161.4653 161.4653 161.4653 0.0000 0.0000 0.0000 231 TYR A CE1 
1574 C CE2 . TYR A 231 ? 161.2237 161.2237 161.2237 0.0000 0.0000 0.0000 231 TYR A CE2 
1575 C CZ  . TYR A 231 ? 161.4465 161.4465 161.4465 0.0000 0.0000 0.0000 231 TYR A CZ  
1576 O OH  . TYR A 231 ? 161.5631 161.5631 161.5631 0.0000 0.0000 0.0000 231 TYR A OH  
1577 N N   . LEU A 232 ? 161.3589 161.3589 161.3589 0.0000 0.0000 0.0000 232 LEU A N   
1578 C CA  . LEU A 232 ? 161.3779 161.3779 161.3779 0.0000 0.0000 0.0000 232 LEU A CA  
1579 C C   . LEU A 232 ? 161.4551 161.4551 161.4551 0.0000 0.0000 0.0000 232 LEU A C   
1580 O O   . LEU A 232 ? 161.5232 161.5232 161.5232 0.0000 0.0000 0.0000 232 LEU A O   
1581 C CB  . LEU A 232 ? 161.3710 161.3710 161.3710 0.0000 0.0000 0.0000 232 LEU A CB  
1582 C CG  . LEU A 232 ? 161.0984 161.0984 161.0984 0.0000 0.0000 0.0000 232 LEU A CG  
1583 C CD1 . LEU A 232 ? 161.0346 161.0346 161.0346 0.0000 0.0000 0.0000 232 LEU A CD1 
1584 C CD2 . LEU A 232 ? 161.0614 161.0614 161.0614 0.0000 0.0000 0.0000 232 LEU A CD2 
1585 N N   . ASP A 233 ? 161.5154 161.5154 161.5154 0.0000 0.0000 0.0000 233 ASP A N   
1586 C CA  . ASP A 233 ? 161.4264 161.4264 161.4264 0.0000 0.0000 0.0000 233 ASP A CA  
1587 C C   . ASP A 233 ? 161.4796 161.4796 161.4796 0.0000 0.0000 0.0000 233 ASP A C   
1588 O O   . ASP A 233 ? 161.7588 161.7588 161.7588 0.0000 0.0000 0.0000 233 ASP A O   
1589 C CB  . ASP A 233 ? 161.4850 161.4850 161.4850 0.0000 0.0000 0.0000 233 ASP A CB  
1590 C CG  . ASP A 233 ? 161.3494 161.3494 161.3494 0.0000 0.0000 0.0000 233 ASP A CG  
1591 O OD1 . ASP A 233 ? 161.3651 161.3651 161.3651 0.0000 0.0000 0.0000 233 ASP A OD1 
1592 O OD2 . ASP A 233 ? 161.5011 161.5011 161.5011 0.0000 0.0000 0.0000 233 ASP A OD2 
1593 N N   . LEU A 234 ? 161.5099 161.5099 161.5099 0.0000 0.0000 0.0000 234 LEU A N   
1594 C CA  . LEU A 234 ? 161.3917 161.3917 161.3917 0.0000 0.0000 0.0000 234 LEU A CA  
1595 C C   . LEU A 234 ? 161.3677 161.3677 161.3677 0.0000 0.0000 0.0000 234 LEU A C   
1596 O O   . LEU A 234 ? 161.4944 161.4944 161.4944 0.0000 0.0000 0.0000 234 LEU A O   
1597 C CB  . LEU A 234 ? 161.5052 161.5052 161.5052 0.0000 0.0000 0.0000 234 LEU A CB  
1598 C CG  . LEU A 234 ? 161.3594 161.3594 161.3594 0.0000 0.0000 0.0000 234 LEU A CG  
1599 C CD1 . LEU A 234 ? 161.4621 161.4621 161.4621 0.0000 0.0000 0.0000 234 LEU A CD1 
1600 C CD2 . LEU A 234 ? 161.3722 161.3722 161.3722 0.0000 0.0000 0.0000 234 LEU A CD2 
1601 N N   . ILE A 235 ? 161.3268 161.3268 161.3268 0.0000 0.0000 0.0000 235 ILE A N   
1602 C CA  . ILE A 235 ? 161.1587 161.1587 161.1587 0.0000 0.0000 0.0000 235 ILE A CA  
1603 C C   . ILE A 235 ? 161.1433 161.1433 161.1433 0.0000 0.0000 0.0000 235 ILE A C   
1604 O O   . ILE A 235 ? 161.2025 161.2025 161.2025 0.0000 0.0000 0.0000 235 ILE A O   
1605 C CB  . ILE A 235 ? 161.3168 161.3168 161.3168 0.0000 0.0000 0.0000 235 ILE A CB  
1606 C CG1 . ILE A 235 ? 161.2851 161.2851 161.2851 0.0000 0.0000 0.0000 235 ILE A CG1 
1607 C CG2 . ILE A 235 ? 161.4314 161.4314 161.4314 0.0000 0.0000 0.0000 235 ILE A CG2 
1608 C CD1 . ILE A 235 ? 161.3899 161.3899 161.3899 0.0000 0.0000 0.0000 235 ILE A CD1 
1609 N N   . LEU A 236 ? 161.2163 161.2163 161.2163 0.0000 0.0000 0.0000 236 LEU A N   
1610 C CA  . LEU A 236 ? 161.3168 161.3168 161.3168 0.0000 0.0000 0.0000 236 LEU A CA  
1611 C C   . LEU A 236 ? 161.4804 161.4804 161.4804 0.0000 0.0000 0.0000 236 LEU A C   
1612 O O   . LEU A 236 ? 161.5959 161.5959 161.5959 0.0000 0.0000 0.0000 236 LEU A O   
1613 C CB  . LEU A 236 ? 161.4441 161.4441 161.4441 0.0000 0.0000 0.0000 236 LEU A CB  
1614 C CG  . LEU A 236 ? 161.4013 161.4013 161.4013 0.0000 0.0000 0.0000 236 LEU A CG  
1615 C CD1 . LEU A 236 ? 161.4654 161.4654 161.4654 0.0000 0.0000 0.0000 236 LEU A CD1 
1616 C CD2 . LEU A 236 ? 161.4864 161.4864 161.4864 0.0000 0.0000 0.0000 236 LEU A CD2 
1617 N N   . ASN A 237 ? 161.6370 161.6370 161.6370 0.0000 0.0000 0.0000 237 ASN A N   
1618 C CA  . ASN A 237 ? 161.6154 161.6154 161.6154 0.0000 0.0000 0.0000 237 ASN A CA  
1619 C C   . ASN A 237 ? 162.1442 162.1442 162.1442 0.0000 0.0000 0.0000 237 ASN A C   
1620 O O   . ASN A 237 ? 162.0739 162.0739 162.0739 0.0000 0.0000 0.0000 237 ASN A O   
1621 C CB  . ASN A 237 ? 161.5995 161.5995 161.5995 0.0000 0.0000 0.0000 237 ASN A CB  
1622 C CG  . ASN A 237 ? 161.4386 161.4386 161.4386 0.0000 0.0000 0.0000 237 ASN A CG  
1623 O OD1 . ASN A 237 ? 161.3684 161.3684 161.3684 0.0000 0.0000 0.0000 237 ASN A OD1 
1624 N ND2 . ASN A 237 ? 161.5649 161.5649 161.5649 0.0000 0.0000 0.0000 237 ASN A ND2 
1625 N N   . ASP A 238 ? 182.5837 182.5837 182.5837 0.0000 0.0000 0.0000 238 ASP A N   
1626 C CA  . ASP A 238 ? 183.1784 183.1784 183.1784 0.0000 0.0000 0.0000 238 ASP A CA  
1627 C C   . ASP A 238 ? 182.7010 182.7010 182.7010 0.0000 0.0000 0.0000 238 ASP A C   
1628 O O   . ASP A 238 ? 182.7017 182.7017 182.7017 0.0000 0.0000 0.0000 238 ASP A O   
1629 C CB  . ASP A 238 ? 183.5707 183.5707 183.5707 0.0000 0.0000 0.0000 238 ASP A CB  
1630 C CG  . ASP A 238 ? 183.6949 183.6949 183.6949 0.0000 0.0000 0.0000 238 ASP A CG  
1631 O OD1 . ASP A 238 ? 183.5176 183.5176 183.5176 0.0000 0.0000 0.0000 238 ASP A OD1 
1632 O OD2 . ASP A 238 ? 183.8292 183.8292 183.8292 0.0000 0.0000 0.0000 238 ASP A OD2 
1633 N N   . PHE A 239 ? 164.3387 164.3387 164.3387 0.0000 0.0000 0.0000 239 PHE A N   
1634 C CA  . PHE A 239 ? 163.7947 163.7947 163.7947 0.0000 0.0000 0.0000 239 PHE A CA  
1635 C C   . PHE A 239 ? 163.5784 163.5784 163.5784 0.0000 0.0000 0.0000 239 PHE A C   
1636 O O   . PHE A 239 ? 163.5881 163.5881 163.5881 0.0000 0.0000 0.0000 239 PHE A O   
1637 C CB  . PHE A 239 ? 163.6765 163.6765 163.6765 0.0000 0.0000 0.0000 239 PHE A CB  
1638 C CG  . PHE A 239 ? 163.5397 163.5397 163.5397 0.0000 0.0000 0.0000 239 PHE A CG  
1639 C CD1 . PHE A 239 ? 163.4949 163.4949 163.4949 0.0000 0.0000 0.0000 239 PHE A CD1 
1640 C CD2 . PHE A 239 ? 163.6358 163.6358 163.6358 0.0000 0.0000 0.0000 239 PHE A CD2 
1641 C CE1 . PHE A 239 ? 163.4885 163.4885 163.4885 0.0000 0.0000 0.0000 239 PHE A CE1 
1642 C CE2 . PHE A 239 ? 163.7115 163.7115 163.7115 0.0000 0.0000 0.0000 239 PHE A CE2 
1643 C CZ  . PHE A 239 ? 163.5987 163.5987 163.5987 0.0000 0.0000 0.0000 239 PHE A CZ  
1644 N N   . VAL A 240 ? 161.4824 161.4824 161.4824 0.0000 0.0000 0.0000 240 VAL A N   
1645 C CA  . VAL A 240 ? 161.3464 161.3464 161.3464 0.0000 0.0000 0.0000 240 VAL A CA  
1646 C C   . VAL A 240 ? 161.5387 161.5387 161.5387 0.0000 0.0000 0.0000 240 VAL A C   
1647 O O   . VAL A 240 ? 161.8220 161.8220 161.8220 0.0000 0.0000 0.0000 240 VAL A O   
1648 C CB  . VAL A 240 ? 161.2932 161.2932 161.2932 0.0000 0.0000 0.0000 240 VAL A CB  
1649 C CG1 . VAL A 240 ? 161.5648 161.5648 161.5648 0.0000 0.0000 0.0000 240 VAL A CG1 
1650 C CG2 . VAL A 240 ? 161.4982 161.4982 161.4982 0.0000 0.0000 0.0000 240 VAL A CG2 
1651 N N   . ARG A 241 ? 161.4498 161.4498 161.4498 0.0000 0.0000 0.0000 241 ARG A N   
1652 C CA  . ARG A 241 ? 161.4743 161.4743 161.4743 0.0000 0.0000 0.0000 241 ARG A CA  
1653 C C   . ARG A 241 ? 161.5411 161.5411 161.5411 0.0000 0.0000 0.0000 241 ARG A C   
1654 O O   . ARG A 241 ? 161.6297 161.6297 161.6297 0.0000 0.0000 0.0000 241 ARG A O   
1655 C CB  . ARG A 241 ? 161.4864 161.4864 161.4864 0.0000 0.0000 0.0000 241 ARG A CB  
1656 C CG  . ARG A 241 ? 161.4533 161.4533 161.4533 0.0000 0.0000 0.0000 241 ARG A CG  
1657 C CD  . ARG A 241 ? 161.5199 161.5199 161.5199 0.0000 0.0000 0.0000 241 ARG A CD  
1658 N NE  . ARG A 241 ? 160.9679 160.9679 160.9679 0.0000 0.0000 0.0000 241 ARG A NE  
1659 C CZ  . ARG A 241 ? 161.1545 161.1545 161.1545 0.0000 0.0000 0.0000 241 ARG A CZ  
1660 N NH1 . ARG A 241 ? 161.4285 161.4285 161.4285 0.0000 0.0000 0.0000 241 ARG A NH1 
1661 N NH2 . ARG A 241 ? 160.6993 160.6993 160.6993 0.0000 0.0000 0.0000 241 ARG A NH2 
1662 N N   . GLN A 242 ? 161.5443 161.5443 161.5443 0.0000 0.0000 0.0000 242 GLN A N   
1663 C CA  . GLN A 242 ? 161.4438 161.4438 161.4438 0.0000 0.0000 0.0000 242 GLN A CA  
1664 C C   . GLN A 242 ? 161.3714 161.3714 161.3714 0.0000 0.0000 0.0000 242 GLN A C   
1665 O O   . GLN A 242 ? 161.6058 161.6058 161.6058 0.0000 0.0000 0.0000 242 GLN A O   
1666 C CB  . GLN A 242 ? 161.4381 161.4381 161.4381 0.0000 0.0000 0.0000 242 GLN A CB  
1667 C CG  . GLN A 242 ? 161.6097 161.6097 161.6097 0.0000 0.0000 0.0000 242 GLN A CG  
1668 C CD  . GLN A 242 ? 161.5077 161.5077 161.5077 0.0000 0.0000 0.0000 242 GLN A CD  
1669 O OE1 . GLN A 242 ? 161.5306 161.5306 161.5306 0.0000 0.0000 0.0000 242 GLN A OE1 
1670 N NE2 . GLN A 242 ? 161.6062 161.6062 161.6062 0.0000 0.0000 0.0000 242 GLN A NE2 
1671 N N   . LYS A 243 ? 161.1535 161.1535 161.1535 0.0000 0.0000 0.0000 243 LYS A N   
1672 C CA  . LYS A 243 ? 161.2366 161.2366 161.2366 0.0000 0.0000 0.0000 243 LYS A CA  
1673 C C   . LYS A 243 ? 161.3197 161.3197 161.3197 0.0000 0.0000 0.0000 243 LYS A C   
1674 O O   . LYS A 243 ? 161.6550 161.6550 161.6550 0.0000 0.0000 0.0000 243 LYS A O   
1675 C CB  . LYS A 243 ? 161.3182 161.3182 161.3182 0.0000 0.0000 0.0000 243 LYS A CB  
1676 C CG  . LYS A 243 ? 161.4194 161.4194 161.4194 0.0000 0.0000 0.0000 243 LYS A CG  
1677 C CD  . LYS A 243 ? 161.4490 161.4490 161.4490 0.0000 0.0000 0.0000 243 LYS A CD  
1678 C CE  . LYS A 243 ? 161.4889 161.4889 161.4889 0.0000 0.0000 0.0000 243 LYS A CE  
1679 N NZ  . LYS A 243 ? 161.5704 161.5704 161.5704 0.0000 0.0000 0.0000 243 LYS A NZ  
1680 N N   . PHE A 244 ? 161.2192 161.2192 161.2192 0.0000 0.0000 0.0000 244 PHE A N   
1681 C CA  . PHE A 244 ? 161.2257 161.2257 161.2257 0.0000 0.0000 0.0000 244 PHE A CA  
1682 C C   . PHE A 244 ? 161.2977 161.2977 161.2977 0.0000 0.0000 0.0000 244 PHE A C   
1683 O O   . PHE A 244 ? 161.6722 161.6722 161.6722 0.0000 0.0000 0.0000 244 PHE A O   
1684 C CB  . PHE A 244 ? 161.3683 161.3683 161.3683 0.0000 0.0000 0.0000 244 PHE A CB  
1685 C CG  . PHE A 244 ? 161.3531 161.3531 161.3531 0.0000 0.0000 0.0000 244 PHE A CG  
1686 C CD1 . PHE A 244 ? 161.3582 161.3582 161.3582 0.0000 0.0000 0.0000 244 PHE A CD1 
1687 C CD2 . PHE A 244 ? 161.4585 161.4585 161.4585 0.0000 0.0000 0.0000 244 PHE A CD2 
1688 C CE1 . PHE A 244 ? 161.4460 161.4460 161.4460 0.0000 0.0000 0.0000 244 PHE A CE1 
1689 C CE2 . PHE A 244 ? 161.5353 161.5353 161.5353 0.0000 0.0000 0.0000 244 PHE A CE2 
1690 C CZ  . PHE A 244 ? 161.5315 161.5315 161.5315 0.0000 0.0000 0.0000 244 PHE A CZ  
1691 N N   . ILE A 245 ? 161.1614 161.1614 161.1614 0.0000 0.0000 0.0000 245 ILE A N   
1692 C CA  . ILE A 245 ? 161.3035 161.3035 161.3035 0.0000 0.0000 0.0000 245 ILE A CA  
1693 C C   . ILE A 245 ? 161.4878 161.4878 161.4878 0.0000 0.0000 0.0000 245 ILE A C   
1694 O O   . ILE A 245 ? 161.5591 161.5591 161.5591 0.0000 0.0000 0.0000 245 ILE A O   
1695 C CB  . ILE A 245 ? 161.2945 161.2945 161.2945 0.0000 0.0000 0.0000 245 ILE A CB  
1696 C CG1 . ILE A 245 ? 160.7255 160.7255 160.7255 0.0000 0.0000 0.0000 245 ILE A CG1 
1697 C CG2 . ILE A 245 ? 160.7737 160.7737 160.7737 0.0000 0.0000 0.0000 245 ILE A CG2 
1698 C CD1 . ILE A 245 ? 160.4375 160.4375 160.4375 0.0000 0.0000 0.0000 245 ILE A CD1 
1699 N N   . ILE A 246 ? 161.5501 161.5501 161.5501 0.0000 0.0000 0.0000 246 ILE A N   
1700 C CA  . ILE A 246 ? 161.3305 161.3305 161.3305 0.0000 0.0000 0.0000 246 ILE A CA  
1701 C C   . ILE A 246 ? 161.3785 161.3785 161.3785 0.0000 0.0000 0.0000 246 ILE A C   
1702 O O   . ILE A 246 ? 161.6379 161.6379 161.6379 0.0000 0.0000 0.0000 246 ILE A O   
1703 C CB  . ILE A 246 ? 161.2548 161.2548 161.2548 0.0000 0.0000 0.0000 246 ILE A CB  
1704 C CG1 . ILE A 246 ? 161.2907 161.2907 161.2907 0.0000 0.0000 0.0000 246 ILE A CG1 
1705 C CG2 . ILE A 246 ? 161.3826 161.3826 161.3826 0.0000 0.0000 0.0000 246 ILE A CG2 
1706 C CD1 . ILE A 246 ? 161.4412 161.4412 161.4412 0.0000 0.0000 0.0000 246 ILE A CD1 
1707 N N   . ARG A 247 ? 161.3585 161.3585 161.3585 0.0000 0.0000 0.0000 247 ARG A N   
1708 C CA  . ARG A 247 ? 161.2666 161.2666 161.2666 0.0000 0.0000 0.0000 247 ARG A CA  
1709 C C   . ARG A 247 ? 161.2379 161.2379 161.2379 0.0000 0.0000 0.0000 247 ARG A C   
1710 O O   . ARG A 247 ? 161.6242 161.6242 161.6242 0.0000 0.0000 0.0000 247 ARG A O   
1711 C CB  . ARG A 247 ? 161.3983 161.3983 161.3983 0.0000 0.0000 0.0000 247 ARG A CB  
1712 C CG  . ARG A 247 ? 161.4182 161.4182 161.4182 0.0000 0.0000 0.0000 247 ARG A CG  
1713 C CD  . ARG A 247 ? 161.3441 161.3441 161.3441 0.0000 0.0000 0.0000 247 ARG A CD  
1714 N NE  . ARG A 247 ? 161.2617 161.2617 161.2617 0.0000 0.0000 0.0000 247 ARG A NE  
1715 C CZ  . ARG A 247 ? 161.3300 161.3300 161.3300 0.0000 0.0000 0.0000 247 ARG A CZ  
1716 N NH1 . ARG A 247 ? 161.3996 161.3996 161.3996 0.0000 0.0000 0.0000 247 ARG A NH1 
1717 N NH2 . ARG A 247 ? 161.5076 161.5076 161.5076 0.0000 0.0000 0.0000 247 ARG A NH2 
1718 N N   . SER A 248 ? 161.1495 161.1495 161.1495 0.0000 0.0000 0.0000 248 SER A N   
1719 C CA  . SER A 248 ? 161.0302 161.0302 161.0302 0.0000 0.0000 0.0000 248 SER A CA  
1720 C C   . SER A 248 ? 160.6960 160.6960 160.6960 0.0000 0.0000 0.0000 248 SER A C   
1721 O O   . SER A 248 ? 160.8822 160.8822 160.8822 0.0000 0.0000 0.0000 248 SER A O   
1722 C CB  . SER A 248 ? 160.7651 160.7651 160.7651 0.0000 0.0000 0.0000 248 SER A CB  
1723 O OG  . SER A 248 ? 160.1057 160.1057 160.1057 0.0000 0.0000 0.0000 248 SER A OG  
1724 N N   . LYS A 249 ? 160.6309 160.6309 160.6309 0.0000 0.0000 0.0000 249 LYS A N   
1725 C CA  . LYS A 249 ? 160.5246 160.5246 160.5246 0.0000 0.0000 0.0000 249 LYS A CA  
1726 C C   . LYS A 249 ? 161.0324 161.0324 161.0324 0.0000 0.0000 0.0000 249 LYS A C   
1727 O O   . LYS A 249 ? 161.1915 161.1915 161.1915 0.0000 0.0000 0.0000 249 LYS A O   
1728 C CB  . LYS A 249 ? 160.9838 160.9838 160.9838 0.0000 0.0000 0.0000 249 LYS A CB  
1729 C CG  . LYS A 249 ? 160.3274 160.3274 160.3274 0.0000 0.0000 0.0000 249 LYS A CG  
1730 C CD  . LYS A 249 ? 160.5378 160.5378 160.5378 0.0000 0.0000 0.0000 249 LYS A CD  
1731 C CE  . LYS A 249 ? 161.2229 161.2229 161.2229 0.0000 0.0000 0.0000 249 LYS A CE  
1732 N NZ  . LYS A 249 ? 161.2278 161.2278 161.2278 0.0000 0.0000 0.0000 249 LYS A NZ  
1733 N N   . ILE A 250 ? 161.3160 161.3160 161.3160 0.0000 0.0000 0.0000 250 ILE A N   
1734 C CA  . ILE A 250 ? 161.2516 161.2516 161.2516 0.0000 0.0000 0.0000 250 ILE A CA  
1735 C C   . ILE A 250 ? 161.3020 161.3020 161.3020 0.0000 0.0000 0.0000 250 ILE A C   
1736 O O   . ILE A 250 ? 161.5238 161.5238 161.5238 0.0000 0.0000 0.0000 250 ILE A O   
1737 C CB  . ILE A 250 ? 161.3453 161.3453 161.3453 0.0000 0.0000 0.0000 250 ILE A CB  
1738 C CG1 . ILE A 250 ? 161.4249 161.4249 161.4249 0.0000 0.0000 0.0000 250 ILE A CG1 
1739 C CG2 . ILE A 250 ? 161.4523 161.4523 161.4523 0.0000 0.0000 0.0000 250 ILE A CG2 
1740 C CD1 . ILE A 250 ? 161.5721 161.5721 161.5721 0.0000 0.0000 0.0000 250 ILE A CD1 
1741 N N   . ILE A 251 ? 161.3709 161.3709 161.3709 0.0000 0.0000 0.0000 251 ILE A N   
1742 C CA  . ILE A 251 ? 161.2858 161.2858 161.2858 0.0000 0.0000 0.0000 251 ILE A CA  
1743 C C   . ILE A 251 ? 161.3291 161.3291 161.3291 0.0000 0.0000 0.0000 251 ILE A C   
1744 O O   . ILE A 251 ? 161.6167 161.6167 161.6167 0.0000 0.0000 0.0000 251 ILE A O   
1745 C CB  . ILE A 251 ? 161.2846 161.2846 161.2846 0.0000 0.0000 0.0000 251 ILE A CB  
1746 C CG1 . ILE A 251 ? 161.4569 161.4569 161.4569 0.0000 0.0000 0.0000 251 ILE A CG1 
1747 C CG2 . ILE A 251 ? 161.4348 161.4348 161.4348 0.0000 0.0000 0.0000 251 ILE A CG2 
1748 C CD1 . ILE A 251 ? 161.4703 161.4703 161.4703 0.0000 0.0000 0.0000 251 ILE A CD1 
1749 N N   . THR A 252 ? 161.2496 161.2496 161.2496 0.0000 0.0000 0.0000 252 THR A N   
1750 C CA  . THR A 252 ? 161.1072 161.1072 161.1072 0.0000 0.0000 0.0000 252 THR A CA  
1751 C C   . THR A 252 ? 161.0978 161.0978 161.0978 0.0000 0.0000 0.0000 252 THR A C   
1752 O O   . THR A 252 ? 161.1635 161.1635 161.1635 0.0000 0.0000 0.0000 252 THR A O   
1753 C CB  . THR A 252 ? 159.9286 159.9286 159.9286 0.0000 0.0000 0.0000 252 THR A CB  
1754 O OG1 . THR A 252 ? 159.9932 159.9932 159.9932 0.0000 0.0000 0.0000 252 THR A OG1 
1755 C CG2 . THR A 252 ? 159.9406 159.9406 159.9406 0.0000 0.0000 0.0000 252 THR A CG2 
1756 N N   . TYR A 253 ? 161.2500 161.2500 161.2500 0.0000 0.0000 0.0000 253 TYR A N   
1757 C CA  . TYR A 253 ? 161.2147 161.2147 161.2147 0.0000 0.0000 0.0000 253 TYR A CA  
1758 C C   . TYR A 253 ? 161.2042 161.2042 161.2042 0.0000 0.0000 0.0000 253 TYR A C   
1759 O O   . TYR A 253 ? 161.1043 161.1043 161.1043 0.0000 0.0000 0.0000 253 TYR A O   
1760 C CB  . TYR A 253 ? 161.3128 161.3128 161.3128 0.0000 0.0000 0.0000 253 TYR A CB  
1761 C CG  . TYR A 253 ? 161.0329 161.0329 161.0329 0.0000 0.0000 0.0000 253 TYR A CG  
1762 C CD1 . TYR A 253 ? 161.3140 161.3140 161.3140 0.0000 0.0000 0.0000 253 TYR A CD1 
1763 C CD2 . TYR A 253 ? 160.9435 160.9435 160.9435 0.0000 0.0000 0.0000 253 TYR A CD2 
1764 C CE1 . TYR A 253 ? 161.2136 161.2136 161.2136 0.0000 0.0000 0.0000 253 TYR A CE1 
1765 C CE2 . TYR A 253 ? 160.8634 160.8634 160.8634 0.0000 0.0000 0.0000 253 TYR A CE2 
1766 C CZ  . TYR A 253 ? 160.9752 160.9752 160.9752 0.0000 0.0000 0.0000 253 TYR A CZ  
1767 O OH  . TYR A 253 ? 161.1833 161.1833 161.1833 0.0000 0.0000 0.0000 253 TYR A OH  
1768 N N   . ILE A 254 ? 161.3475 161.3475 161.3475 0.0000 0.0000 0.0000 254 ILE A N   
1769 C CA  . ILE A 254 ? 161.1914 161.1914 161.1914 0.0000 0.0000 0.0000 254 ILE A CA  
1770 C C   . ILE A 254 ? 161.1314 161.1314 161.1314 0.0000 0.0000 0.0000 254 ILE A C   
1771 O O   . ILE A 254 ? 161.4322 161.4322 161.4322 0.0000 0.0000 0.0000 254 ILE A O   
1772 C CB  . ILE A 254 ? 161.2920 161.2920 161.2920 0.0000 0.0000 0.0000 254 ILE A CB  
1773 C CG1 . ILE A 254 ? 161.4582 161.4582 161.4582 0.0000 0.0000 0.0000 254 ILE A CG1 
1774 C CG2 . ILE A 254 ? 161.4133 161.4133 161.4133 0.0000 0.0000 0.0000 254 ILE A CG2 
1775 C CD1 . ILE A 254 ? 161.6451 161.6451 161.6451 0.0000 0.0000 0.0000 254 ILE A CD1 
1776 N N   . ARG A 255 ? 161.1135 161.1135 161.1135 0.0000 0.0000 0.0000 255 ARG A N   
1777 C CA  . ARG A 255 ? 161.1790 161.1790 161.1790 0.0000 0.0000 0.0000 255 ARG A CA  
1778 C C   . ARG A 255 ? 161.3141 161.3141 161.3141 0.0000 0.0000 0.0000 255 ARG A C   
1779 O O   . ARG A 255 ? 161.6860 161.6860 161.6860 0.0000 0.0000 0.0000 255 ARG A O   
1780 C CB  . ARG A 255 ? 161.3361 161.3361 161.3361 0.0000 0.0000 0.0000 255 ARG A CB  
1781 C CG  . ARG A 255 ? 161.4451 161.4451 161.4451 0.0000 0.0000 0.0000 255 ARG A CG  
1782 C CD  . ARG A 255 ? 161.3972 161.3972 161.3972 0.0000 0.0000 0.0000 255 ARG A CD  
1783 N NE  . ARG A 255 ? 161.3459 161.3459 161.3459 0.0000 0.0000 0.0000 255 ARG A NE  
1784 C CZ  . ARG A 255 ? 161.3937 161.3937 161.3937 0.0000 0.0000 0.0000 255 ARG A CZ  
1785 N NH1 . ARG A 255 ? 161.4347 161.4347 161.4347 0.0000 0.0000 0.0000 255 ARG A NH1 
1786 N NH2 . ARG A 255 ? 161.6025 161.6025 161.6025 0.0000 0.0000 0.0000 255 ARG A NH2 
1787 N N   . SER A 256 ? 161.2264 161.2264 161.2264 0.0000 0.0000 0.0000 256 SER A N   
1788 C CA  . SER A 256 ? 161.2138 161.2138 161.2138 0.0000 0.0000 0.0000 256 SER A CA  
1789 C C   . SER A 256 ? 161.1755 161.1755 161.1755 0.0000 0.0000 0.0000 256 SER A C   
1790 O O   . SER A 256 ? 161.2723 161.2723 161.2723 0.0000 0.0000 0.0000 256 SER A O   
1791 C CB  . SER A 256 ? 160.5701 160.5701 160.5701 0.0000 0.0000 0.0000 256 SER A CB  
1792 O OG  . SER A 256 ? 160.3173 160.3173 160.3173 0.0000 0.0000 0.0000 256 SER A OG  
1793 N N   . PHE A 257 ? 160.9202 160.9202 160.9202 0.0000 0.0000 0.0000 257 PHE A N   
1794 C CA  . PHE A 257 ? 160.6828 160.6828 160.6828 0.0000 0.0000 0.0000 257 PHE A CA  
1795 C C   . PHE A 257 ? 161.0067 161.0067 161.0067 0.0000 0.0000 0.0000 257 PHE A C   
1796 O O   . PHE A 257 ? 161.1510 161.1510 161.1510 0.0000 0.0000 0.0000 257 PHE A O   
1797 C CB  . PHE A 257 ? 160.8942 160.8942 160.8942 0.0000 0.0000 0.0000 257 PHE A CB  
1798 C CG  . PHE A 257 ? 160.6141 160.6141 160.6141 0.0000 0.0000 0.0000 257 PHE A CG  
1799 C CD1 . PHE A 257 ? 161.1108 161.1108 161.1108 0.0000 0.0000 0.0000 257 PHE A CD1 
1800 C CD2 . PHE A 257 ? 160.2078 160.2078 160.2078 0.0000 0.0000 0.0000 257 PHE A CD2 
1801 C CE1 . PHE A 257 ? 160.7929 160.7929 160.7929 0.0000 0.0000 0.0000 257 PHE A CE1 
1802 C CE2 . PHE A 257 ? 159.5660 159.5660 159.5660 0.0000 0.0000 0.0000 257 PHE A CE2 
1803 C CZ  . PHE A 257 ? 160.1679 160.1679 160.1679 0.0000 0.0000 0.0000 257 PHE A CZ  
1804 N N   . LEU A 258 ? 161.3695 161.3695 161.3695 0.0000 0.0000 0.0000 258 LEU A N   
1805 C CA  . LEU A 258 ? 161.2429 161.2429 161.2429 0.0000 0.0000 0.0000 258 LEU A CA  
1806 C C   . LEU A 258 ? 161.2580 161.2580 161.2580 0.0000 0.0000 0.0000 258 LEU A C   
1807 O O   . LEU A 258 ? 161.5383 161.5383 161.5383 0.0000 0.0000 0.0000 258 LEU A O   
1808 C CB  . LEU A 258 ? 161.4212 161.4212 161.4212 0.0000 0.0000 0.0000 258 LEU A CB  
1809 C CG  . LEU A 258 ? 161.2110 161.2110 161.2110 0.0000 0.0000 0.0000 258 LEU A CG  
1810 C CD1 . LEU A 258 ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 258 LEU A CD1 
1811 C CD2 . LEU A 258 ? 161.4396 161.4396 161.4396 0.0000 0.0000 0.0000 258 LEU A CD2 
1812 N N   . ASP A 259 ? 161.4225 161.4225 161.4225 0.0000 0.0000 0.0000 259 ASP A N   
1813 C CA  . ASP A 259 ? 161.5289 161.5289 161.5289 0.0000 0.0000 0.0000 259 ASP A CA  
1814 C C   . ASP A 259 ? 161.0949 161.0949 161.0949 0.0000 0.0000 0.0000 259 ASP A C   
1815 O O   . ASP A 259 ? 160.3636 160.3636 160.3636 0.0000 0.0000 0.0000 259 ASP A O   
1816 C CB  . ASP A 259 ? 161.1944 161.1944 161.1944 0.0000 0.0000 0.0000 259 ASP A CB  
1817 C CG  . ASP A 259 ? 161.0097 161.0097 161.0097 0.0000 0.0000 0.0000 259 ASP A CG  
1818 O OD1 . ASP A 259 ? 161.1491 161.1491 161.1491 0.0000 0.0000 0.0000 259 ASP A OD1 
1819 O OD2 . ASP A 259 ? 160.9950 160.9950 160.9950 0.0000 0.0000 0.0000 259 ASP A OD2 
1820 N N   . GLU A 260 ? 161.1586 161.1586 161.1586 0.0000 0.0000 0.0000 260 GLU A N   
1821 C CA  . GLU A 260 ? 160.5896 160.5896 160.5896 0.0000 0.0000 0.0000 260 GLU A CA  
1822 C C   . GLU A 260 ? 160.5300 160.5300 160.5300 0.0000 0.0000 0.0000 260 GLU A C   
1823 O O   . GLU A 260 ? 160.0591 160.0591 160.0591 0.0000 0.0000 0.0000 260 GLU A O   
1824 C CB  . GLU A 260 ? 160.4524 160.4524 160.4524 0.0000 0.0000 0.0000 260 GLU A CB  
1825 C CG  . GLU A 260 ? 160.4556 160.4556 160.4556 0.0000 0.0000 0.0000 260 GLU A CG  
1826 C CD  . GLU A 260 ? 160.6502 160.6502 160.6502 0.0000 0.0000 0.0000 260 GLU A CD  
1827 O OE1 . GLU A 260 ? 160.3500 160.3500 160.3500 0.0000 0.0000 0.0000 260 GLU A OE1 
1828 O OE2 . GLU A 260 ? 160.8109 160.8109 160.8109 0.0000 0.0000 0.0000 260 GLU A OE2 
1829 N N   . LEU A 261 ? 161.1059 161.1059 161.1059 0.0000 0.0000 0.0000 261 LEU A N   
1830 C CA  . LEU A 261 ? 161.0521 161.0521 161.0521 0.0000 0.0000 0.0000 261 LEU A CA  
1831 C C   . LEU A 261 ? 160.8969 160.8969 160.8969 0.0000 0.0000 0.0000 261 LEU A C   
1832 O O   . LEU A 261 ? 160.1394 160.1394 160.1394 0.0000 0.0000 0.0000 261 LEU A O   
1833 C CB  . LEU A 261 ? 161.2126 161.2126 161.2126 0.0000 0.0000 0.0000 261 LEU A CB  
1834 C CG  . LEU A 261 ? 160.3712 160.3712 160.3712 0.0000 0.0000 0.0000 261 LEU A CG  
1835 C CD1 . LEU A 261 ? 160.7006 160.7006 160.7006 0.0000 0.0000 0.0000 261 LEU A CD1 
1836 C CD2 . LEU A 261 ? 159.9828 159.9828 159.9828 0.0000 0.0000 0.0000 261 LEU A CD2 
1837 N N   . GLY A 262 ? 160.2396 160.2396 160.2396 0.0000 0.0000 0.0000 262 GLY A N   
1838 C CA  . GLY A 262 ? 159.1861 159.1861 159.1861 0.0000 0.0000 0.0000 262 GLY A CA  
1839 C C   . GLY A 262 ? 160.2754 160.2754 160.2754 0.0000 0.0000 0.0000 262 GLY A C   
1840 O O   . GLY A 262 ? 159.6202 159.6202 159.6202 0.0000 0.0000 0.0000 262 GLY A O   
1841 N N   . PHE A 263 ? 160.8496 160.8496 160.8496 0.0000 0.0000 0.0000 263 PHE A N   
1842 C CA  . PHE A 263 ? 160.9908 160.9908 160.9908 0.0000 0.0000 0.0000 263 PHE A CA  
1843 C C   . PHE A 263 ? 160.4071 160.4071 160.4071 0.0000 0.0000 0.0000 263 PHE A C   
1844 O O   . PHE A 263 ? 160.4574 160.4574 160.4574 0.0000 0.0000 0.0000 263 PHE A O   
1845 C CB  . PHE A 263 ? 161.3214 161.3214 161.3214 0.0000 0.0000 0.0000 263 PHE A CB  
1846 C CG  . PHE A 263 ? 161.3742 161.3742 161.3742 0.0000 0.0000 0.0000 263 PHE A CG  
1847 C CD1 . PHE A 263 ? 161.4721 161.4721 161.4721 0.0000 0.0000 0.0000 263 PHE A CD1 
1848 C CD2 . PHE A 263 ? 161.5001 161.5001 161.5001 0.0000 0.0000 0.0000 263 PHE A CD2 
1849 C CE1 . PHE A 263 ? 161.3445 161.3445 161.3445 0.0000 0.0000 0.0000 263 PHE A CE1 
1850 C CE2 . PHE A 263 ? 161.4197 161.4197 161.4197 0.0000 0.0000 0.0000 263 PHE A CE2 
1851 C CZ  . PHE A 263 ? 161.2920 161.2920 161.2920 0.0000 0.0000 0.0000 263 PHE A CZ  
1852 N N   . LEU A 264 ? 160.3046 160.3046 160.3046 0.0000 0.0000 0.0000 264 LEU A N   
1853 C CA  . LEU A 264 ? 160.3091 160.3091 160.3091 0.0000 0.0000 0.0000 264 LEU A CA  
1854 C C   . LEU A 264 ? 161.3493 161.3493 161.3493 0.0000 0.0000 0.0000 264 LEU A C   
1855 O O   . LEU A 264 ? 161.6710 161.6710 161.6710 0.0000 0.0000 0.0000 264 LEU A O   
1856 C CB  . LEU A 264 ? 159.7830 159.7830 159.7830 0.0000 0.0000 0.0000 264 LEU A CB  
1857 C CG  . LEU A 264 ? 160.1155 160.1155 160.1155 0.0000 0.0000 0.0000 264 LEU A CG  
1858 C CD1 . LEU A 264 ? 159.4840 159.4840 159.4840 0.0000 0.0000 0.0000 264 LEU A CD1 
1859 C CD2 . LEU A 264 ? 160.9717 160.9717 160.9717 0.0000 0.0000 0.0000 264 LEU A CD2 
1860 N N   . GLU A 265 ? 161.3494 161.3494 161.3494 0.0000 0.0000 0.0000 265 GLU A N   
1861 C CA  . GLU A 265 ? 161.3512 161.3512 161.3512 0.0000 0.0000 0.0000 265 GLU A CA  
1862 C C   . GLU A 265 ? 161.3232 161.3232 161.3232 0.0000 0.0000 0.0000 265 GLU A C   
1863 O O   . GLU A 265 ? 161.3507 161.3507 161.3507 0.0000 0.0000 0.0000 265 GLU A O   
1864 C CB  . GLU A 265 ? 161.3457 161.3457 161.3457 0.0000 0.0000 0.0000 265 GLU A CB  
1865 C CG  . GLU A 265 ? 161.5141 161.5141 161.5141 0.0000 0.0000 0.0000 265 GLU A CG  
1866 C CD  . GLU A 265 ? 161.6034 161.6034 161.6034 0.0000 0.0000 0.0000 265 GLU A CD  
1867 O OE1 . GLU A 265 ? 161.5409 161.5409 161.5409 0.0000 0.0000 0.0000 265 GLU A OE1 
1868 O OE2 . GLU A 265 ? 161.6795 161.6795 161.6795 0.0000 0.0000 0.0000 265 GLU A OE2 
1869 N N   . ILE A 266 ? 161.3410 161.3410 161.3410 0.0000 0.0000 0.0000 266 ILE A N   
1870 C CA  . ILE A 266 ? 161.0925 161.0925 161.0925 0.0000 0.0000 0.0000 266 ILE A CA  
1871 C C   . ILE A 266 ? 161.1326 161.1326 161.1326 0.0000 0.0000 0.0000 266 ILE A C   
1872 O O   . ILE A 266 ? 161.4646 161.4646 161.4646 0.0000 0.0000 0.0000 266 ILE A O   
1873 C CB  . ILE A 266 ? 160.8938 160.8938 160.8938 0.0000 0.0000 0.0000 266 ILE A CB  
1874 C CG1 . ILE A 266 ? 161.1571 161.1571 161.1571 0.0000 0.0000 0.0000 266 ILE A CG1 
1875 C CG2 . ILE A 266 ? 160.9586 160.9586 160.9586 0.0000 0.0000 0.0000 266 ILE A CG2 
1876 C CD1 . ILE A 266 ? 161.2525 161.2525 161.2525 0.0000 0.0000 0.0000 266 ILE A CD1 
1877 N N   . GLU A 267 ? 160.9337 160.9337 160.9337 0.0000 0.0000 0.0000 267 GLU A N   
1878 C CA  . GLU A 267 ? 161.0971 161.0971 161.0971 0.0000 0.0000 0.0000 267 GLU A CA  
1879 C C   . GLU A 267 ? 160.8436 160.8436 160.8436 0.0000 0.0000 0.0000 267 GLU A C   
1880 O O   . GLU A 267 ? 160.3508 160.3508 160.3508 0.0000 0.0000 0.0000 267 GLU A O   
1881 C CB  . GLU A 267 ? 161.5171 161.5171 161.5171 0.0000 0.0000 0.0000 267 GLU A CB  
1882 C CG  . GLU A 267 ? 161.6440 161.6440 161.6440 0.0000 0.0000 0.0000 267 GLU A CG  
1883 C CD  . GLU A 267 ? 161.6296 161.6296 161.6296 0.0000 0.0000 0.0000 267 GLU A CD  
1884 O OE1 . GLU A 267 ? 161.5809 161.5809 161.5809 0.0000 0.0000 0.0000 267 GLU A OE1 
1885 O OE2 . GLU A 267 ? 161.6220 161.6220 161.6220 0.0000 0.0000 0.0000 267 GLU A OE2 
1886 N N   . THR A 268 ? 161.1582 161.1582 161.1582 0.0000 0.0000 0.0000 268 THR A N   
1887 C CA  . THR A 268 ? 161.0779 161.0779 161.0779 0.0000 0.0000 0.0000 268 THR A CA  
1888 C C   . THR A 268 ? 161.4652 161.4652 161.4652 0.0000 0.0000 0.0000 268 THR A C   
1889 O O   . THR A 268 ? 161.6511 161.6511 161.6511 0.0000 0.0000 0.0000 268 THR A O   
1890 C CB  . THR A 268 ? 161.3518 161.3518 161.3518 0.0000 0.0000 0.0000 268 THR A CB  
1891 O OG1 . THR A 268 ? 161.5986 161.5986 161.5986 0.0000 0.0000 0.0000 268 THR A OG1 
1892 C CG2 . THR A 268 ? 160.7142 160.7142 160.7142 0.0000 0.0000 0.0000 268 THR A CG2 
1893 N N   . PRO A 269 ? 161.2229 161.2229 161.2229 0.0000 0.0000 0.0000 269 PRO A N   
1894 C CA  . PRO A 269 ? 161.2995 161.2995 161.2995 0.0000 0.0000 0.0000 269 PRO A CA  
1895 C C   . PRO A 269 ? 161.3044 161.3044 161.3044 0.0000 0.0000 0.0000 269 PRO A C   
1896 O O   . PRO A 269 ? 161.4509 161.4509 161.4509 0.0000 0.0000 0.0000 269 PRO A O   
1897 C CB  . PRO A 269 ? 160.9459 160.9459 160.9459 0.0000 0.0000 0.0000 269 PRO A CB  
1898 C CG  . PRO A 269 ? 159.4795 159.4795 159.4795 0.0000 0.0000 0.0000 269 PRO A CG  
1899 C CD  . PRO A 269 ? 159.5712 159.5712 159.5712 0.0000 0.0000 0.0000 269 PRO A CD  
1900 N N   . MET A 270 ? 161.2935 161.2935 161.2935 0.0000 0.0000 0.0000 270 MET A N   
1901 C CA  . MET A 270 ? 161.3652 161.3652 161.3652 0.0000 0.0000 0.0000 270 MET A CA  
1902 C C   . MET A 270 ? 161.4031 161.4031 161.4031 0.0000 0.0000 0.0000 270 MET A C   
1903 O O   . MET A 270 ? 161.5305 161.5305 161.5305 0.0000 0.0000 0.0000 270 MET A O   
1904 C CB  . MET A 270 ? 161.4825 161.4825 161.4825 0.0000 0.0000 0.0000 270 MET A CB  
1905 C CG  . MET A 270 ? 161.4859 161.4859 161.4859 0.0000 0.0000 0.0000 270 MET A CG  
1906 S SD  . MET A 270 ? 161.5139 161.5139 161.5139 0.0000 0.0000 0.0000 270 MET A SD  
1907 C CE  . MET A 270 ? 161.5189 161.5189 161.5189 0.0000 0.0000 0.0000 270 MET A CE  
1908 N N   . MET A 271 ? 161.2623 161.2623 161.2623 0.0000 0.0000 0.0000 271 MET A N   
1909 C CA  . MET A 271 ? 161.3455 161.3455 161.3455 0.0000 0.0000 0.0000 271 MET A CA  
1910 C C   . MET A 271 ? 161.3181 161.3181 161.3181 0.0000 0.0000 0.0000 271 MET A C   
1911 O O   . MET A 271 ? 161.3685 161.3685 161.3685 0.0000 0.0000 0.0000 271 MET A O   
1912 C CB  . MET A 271 ? 161.4889 161.4889 161.4889 0.0000 0.0000 0.0000 271 MET A CB  
1913 C CG  . MET A 271 ? 161.5468 161.5468 161.5468 0.0000 0.0000 0.0000 271 MET A CG  
1914 S SD  . MET A 271 ? 161.4034 161.4034 161.4034 0.0000 0.0000 0.0000 271 MET A SD  
1915 C CE  . MET A 271 ? 161.4677 161.4677 161.4677 0.0000 0.0000 0.0000 271 MET A CE  
1916 N N   . ASN A 272 ? 161.3024 161.3024 161.3024 0.0000 0.0000 0.0000 272 ASN A N   
1917 C CA  . ASN A 272 ? 161.1755 161.1755 161.1755 0.0000 0.0000 0.0000 272 ASN A CA  
1918 C C   . ASN A 272 ? 161.3522 161.3522 161.3522 0.0000 0.0000 0.0000 272 ASN A C   
1919 O O   . ASN A 272 ? 161.6213 161.6213 161.6213 0.0000 0.0000 0.0000 272 ASN A O   
1920 C CB  . ASN A 272 ? 161.3101 161.3101 161.3101 0.0000 0.0000 0.0000 272 ASN A CB  
1921 C CG  . ASN A 272 ? 161.5471 161.5471 161.5471 0.0000 0.0000 0.0000 272 ASN A CG  
1922 O OD1 . ASN A 272 ? 161.6400 161.6400 161.6400 0.0000 0.0000 0.0000 272 ASN A OD1 
1923 N ND2 . ASN A 272 ? 161.8113 161.8113 161.8113 0.0000 0.0000 0.0000 272 ASN A ND2 
1924 N N   . ILE A 273 ? 162.0208 162.0208 162.0208 0.0000 0.0000 0.0000 273 ILE A N   
1925 C CA  . ILE A 273 ? 162.1753 162.1753 162.1753 0.0000 0.0000 0.0000 273 ILE A CA  
1926 C C   . ILE A 273 ? 162.3254 162.3254 162.3254 0.0000 0.0000 0.0000 273 ILE A C   
1927 O O   . ILE A 273 ? 162.3334 162.3334 162.3334 0.0000 0.0000 0.0000 273 ILE A O   
1928 C CB  . ILE A 273 ? 162.1382 162.1382 162.1382 0.0000 0.0000 0.0000 273 ILE A CB  
1929 C CG1 . ILE A 273 ? 162.1083 162.1083 162.1083 0.0000 0.0000 0.0000 273 ILE A CG1 
1930 C CG2 . ILE A 273 ? 162.2052 162.2052 162.2052 0.0000 0.0000 0.0000 273 ILE A CG2 
1931 C CD1 . ILE A 273 ? 161.8443 161.8443 161.8443 0.0000 0.0000 0.0000 273 ILE A CD1 
1932 N N   . ILE A 274 ? 162.7748 162.7748 162.7748 0.0000 0.0000 0.0000 274 ILE A N   
1933 C CA  . ILE A 274 ? 163.0705 163.0705 163.0705 0.0000 0.0000 0.0000 274 ILE A CA  
1934 C C   . ILE A 274 ? 163.3447 163.3447 163.3447 0.0000 0.0000 0.0000 274 ILE A C   
1935 O O   . ILE A 274 ? 163.0882 163.0882 163.0882 0.0000 0.0000 0.0000 274 ILE A O   
1936 C CB  . ILE A 274 ? 163.0914 163.0914 163.0914 0.0000 0.0000 0.0000 274 ILE A CB  
1937 C CG1 . ILE A 274 ? 162.9241 162.9241 162.9241 0.0000 0.0000 0.0000 274 ILE A CG1 
1938 C CG2 . ILE A 274 ? 163.8982 163.8982 163.8982 0.0000 0.0000 0.0000 274 ILE A CG2 
1939 C CD1 . ILE A 274 ? 163.0851 163.0851 163.0851 0.0000 0.0000 0.0000 274 ILE A CD1 
1940 N N   . PRO A 275 ? 174.5408 174.5408 174.5408 0.0000 0.0000 0.0000 275 PRO A N   
1941 C CA  . PRO A 275 ? 174.8318 174.8318 174.8318 0.0000 0.0000 0.0000 275 PRO A CA  
1942 C C   . PRO A 275 ? 175.5085 175.5085 175.5085 0.0000 0.0000 0.0000 275 PRO A C   
1943 O O   . PRO A 275 ? 175.3659 175.3659 175.3659 0.0000 0.0000 0.0000 275 PRO A O   
1944 C CB  . PRO A 275 ? 175.2809 175.2809 175.2809 0.0000 0.0000 0.0000 275 PRO A CB  
1945 C CG  . PRO A 275 ? 175.3255 175.3255 175.3255 0.0000 0.0000 0.0000 275 PRO A CG  
1946 C CD  . PRO A 275 ? 175.2336 175.2336 175.2336 0.0000 0.0000 0.0000 275 PRO A CD  
1947 N N   . GLY A 276 ? 195.2769 195.2769 195.2769 0.0000 0.0000 0.0000 276 GLY A N   
1948 C CA  . GLY A 276 ? 196.0155 196.0155 196.0155 0.0000 0.0000 0.0000 276 GLY A CA  
1949 C C   . GLY A 276 ? 196.6136 196.6136 196.6136 0.0000 0.0000 0.0000 276 GLY A C   
1950 O O   . GLY A 276 ? 196.9380 196.9380 196.9380 0.0000 0.0000 0.0000 276 GLY A O   
1951 N N   . GLY A 277 ? 200.5730 200.5730 200.5730 0.0000 0.0000 0.0000 277 GLY A N   
1952 C CA  . GLY A 277 ? 200.8607 200.8607 200.8607 0.0000 0.0000 0.0000 277 GLY A CA  
1953 C C   . GLY A 277 ? 200.1357 200.1357 200.1357 0.0000 0.0000 0.0000 277 GLY A C   
1954 O O   . GLY A 277 ? 200.5685 200.5685 200.5685 0.0000 0.0000 0.0000 277 GLY A O   
1955 N N   . ALA A 278 ? 194.2339 194.2339 194.2339 0.0000 0.0000 0.0000 278 ALA A N   
1956 C CA  . ALA A 278 ? 193.7223 193.7223 193.7223 0.0000 0.0000 0.0000 278 ALA A CA  
1957 C C   . ALA A 278 ? 194.6462 194.6462 194.6462 0.0000 0.0000 0.0000 278 ALA A C   
1958 O O   . ALA A 278 ? 195.0055 195.0055 195.0055 0.0000 0.0000 0.0000 278 ALA A O   
1959 C CB  . ALA A 278 ? 192.9630 192.9630 192.9630 0.0000 0.0000 0.0000 278 ALA A CB  
1960 N N   . VAL A 279 ? 186.5849 186.5849 186.5849 0.0000 0.0000 0.0000 279 VAL A N   
1961 C CA  . VAL A 279 ? 186.7589 186.7589 186.7589 0.0000 0.0000 0.0000 279 VAL A CA  
1962 C C   . VAL A 279 ? 186.2036 186.2036 186.2036 0.0000 0.0000 0.0000 279 VAL A C   
1963 O O   . VAL A 279 ? 186.3809 186.3809 186.3809 0.0000 0.0000 0.0000 279 VAL A O   
1964 C CB  . VAL A 279 ? 185.2327 185.2327 185.2327 0.0000 0.0000 0.0000 279 VAL A CB  
1965 C CG1 . VAL A 279 ? 185.6193 185.6193 185.6193 0.0000 0.0000 0.0000 279 VAL A CG1 
1966 C CG2 . VAL A 279 ? 184.8229 184.8229 184.8229 0.0000 0.0000 0.0000 279 VAL A CG2 
1967 N N   . ALA A 280 ? 167.1516 167.1516 167.1516 0.0000 0.0000 0.0000 280 ALA A N   
1968 C CA  . ALA A 280 ? 166.7821 166.7821 166.7821 0.0000 0.0000 0.0000 280 ALA A CA  
1969 C C   . ALA A 280 ? 167.8031 167.8031 167.8031 0.0000 0.0000 0.0000 280 ALA A C   
1970 O O   . ALA A 280 ? 168.0690 168.0690 168.0690 0.0000 0.0000 0.0000 280 ALA A O   
1971 C CB  . ALA A 280 ? 166.1729 166.1729 166.1729 0.0000 0.0000 0.0000 280 ALA A CB  
1972 N N   . LYS A 281 ? 161.6270 161.6270 161.6270 0.0000 0.0000 0.0000 281 LYS A N   
1973 C CA  . LYS A 281 ? 161.4252 161.4252 161.4252 0.0000 0.0000 0.0000 281 LYS A CA  
1974 C C   . LYS A 281 ? 161.3721 161.3721 161.3721 0.0000 0.0000 0.0000 281 LYS A C   
1975 O O   . LYS A 281 ? 161.5794 161.5794 161.5794 0.0000 0.0000 0.0000 281 LYS A O   
1976 C CB  . LYS A 281 ? 161.4514 161.4514 161.4514 0.0000 0.0000 0.0000 281 LYS A CB  
1977 C CG  . LYS A 281 ? 161.4480 161.4480 161.4480 0.0000 0.0000 0.0000 281 LYS A CG  
1978 C CD  . LYS A 281 ? 161.3963 161.3963 161.3963 0.0000 0.0000 0.0000 281 LYS A CD  
1979 C CE  . LYS A 281 ? 161.4722 161.4722 161.4722 0.0000 0.0000 0.0000 281 LYS A CE  
1980 N NZ  . LYS A 281 ? 161.3086 161.3086 161.3086 0.0000 0.0000 0.0000 281 LYS A NZ  
1981 N N   . PRO A 282 ? 161.2312 161.2312 161.2312 0.0000 0.0000 0.0000 282 PRO A N   
1982 C CA  . PRO A 282 ? 161.3366 161.3366 161.3366 0.0000 0.0000 0.0000 282 PRO A CA  
1983 C C   . PRO A 282 ? 161.5099 161.5099 161.5099 0.0000 0.0000 0.0000 282 PRO A C   
1984 O O   . PRO A 282 ? 161.4995 161.4995 161.4995 0.0000 0.0000 0.0000 282 PRO A O   
1985 C CB  . PRO A 282 ? 161.3966 161.3966 161.3966 0.0000 0.0000 0.0000 282 PRO A CB  
1986 C CG  . PRO A 282 ? 161.3796 161.3796 161.3796 0.0000 0.0000 0.0000 282 PRO A CG  
1987 C CD  . PRO A 282 ? 161.3805 161.3805 161.3805 0.0000 0.0000 0.0000 282 PRO A CD  
1988 N N   . PHE A 283 ? 161.5519 161.5519 161.5519 0.0000 0.0000 0.0000 283 PHE A N   
1989 C CA  . PHE A 283 ? 161.3798 161.3798 161.3798 0.0000 0.0000 0.0000 283 PHE A CA  
1990 C C   . PHE A 283 ? 161.3262 161.3262 161.3262 0.0000 0.0000 0.0000 283 PHE A C   
1991 O O   . PHE A 283 ? 161.4533 161.4533 161.4533 0.0000 0.0000 0.0000 283 PHE A O   
1992 C CB  . PHE A 283 ? 161.3765 161.3765 161.3765 0.0000 0.0000 0.0000 283 PHE A CB  
1993 C CG  . PHE A 283 ? 161.3645 161.3645 161.3645 0.0000 0.0000 0.0000 283 PHE A CG  
1994 C CD1 . PHE A 283 ? 161.4616 161.4616 161.4616 0.0000 0.0000 0.0000 283 PHE A CD1 
1995 C CD2 . PHE A 283 ? 161.4769 161.4769 161.4769 0.0000 0.0000 0.0000 283 PHE A CD2 
1996 C CE1 . PHE A 283 ? 161.5087 161.5087 161.5087 0.0000 0.0000 0.0000 283 PHE A CE1 
1997 C CE2 . PHE A 283 ? 161.4383 161.4383 161.4383 0.0000 0.0000 0.0000 283 PHE A CE2 
1998 C CZ  . PHE A 283 ? 161.4475 161.4475 161.4475 0.0000 0.0000 0.0000 283 PHE A CZ  
1999 N N   . ILE A 284 ? 161.1028 161.1028 161.1028 0.0000 0.0000 0.0000 284 ILE A N   
2000 C CA  . ILE A 284 ? 161.0621 161.0621 161.0621 0.0000 0.0000 0.0000 284 ILE A CA  
2001 C C   . ILE A 284 ? 161.1996 161.1996 161.1996 0.0000 0.0000 0.0000 284 ILE A C   
2002 O O   . ILE A 284 ? 161.5016 161.5016 161.5016 0.0000 0.0000 0.0000 284 ILE A O   
2003 C CB  . ILE A 284 ? 161.2622 161.2622 161.2622 0.0000 0.0000 0.0000 284 ILE A CB  
2004 C CG1 . ILE A 284 ? 161.3987 161.3987 161.3987 0.0000 0.0000 0.0000 284 ILE A CG1 
2005 C CG2 . ILE A 284 ? 161.5151 161.5151 161.5151 0.0000 0.0000 0.0000 284 ILE A CG2 
2006 C CD1 . ILE A 284 ? 161.4685 161.4685 161.4685 0.0000 0.0000 0.0000 284 ILE A CD1 
2007 N N   . THR A 285 ? 161.3161 161.3161 161.3161 0.0000 0.0000 0.0000 285 THR A N   
2008 C CA  . THR A 285 ? 161.4011 161.4011 161.4011 0.0000 0.0000 0.0000 285 THR A CA  
2009 C C   . THR A 285 ? 161.5858 161.5858 161.5858 0.0000 0.0000 0.0000 285 THR A C   
2010 O O   . THR A 285 ? 161.7814 161.7814 161.7814 0.0000 0.0000 0.0000 285 THR A O   
2011 C CB  . THR A 285 ? 161.5708 161.5708 161.5708 0.0000 0.0000 0.0000 285 THR A CB  
2012 O OG1 . THR A 285 ? 161.6185 161.6185 161.6185 0.0000 0.0000 0.0000 285 THR A OG1 
2013 C CG2 . THR A 285 ? 161.6535 161.6535 161.6535 0.0000 0.0000 0.0000 285 THR A CG2 
2014 N N   . TYR A 286 ? 167.8410 167.8410 167.8410 0.0000 0.0000 0.0000 286 TYR A N   
2015 C CA  . TYR A 286 ? 168.1601 168.1601 168.1601 0.0000 0.0000 0.0000 286 TYR A CA  
2016 C C   . TYR A 286 ? 168.1478 168.1478 168.1478 0.0000 0.0000 0.0000 286 TYR A C   
2017 O O   . TYR A 286 ? 168.1668 168.1668 168.1668 0.0000 0.0000 0.0000 286 TYR A O   
2018 C CB  . TYR A 286 ? 168.2937 168.2937 168.2937 0.0000 0.0000 0.0000 286 TYR A CB  
2019 C CG  . TYR A 286 ? 168.3282 168.3282 168.3282 0.0000 0.0000 0.0000 286 TYR A CG  
2020 C CD1 . TYR A 286 ? 168.4472 168.4472 168.4472 0.0000 0.0000 0.0000 286 TYR A CD1 
2021 C CD2 . TYR A 286 ? 168.4677 168.4677 168.4677 0.0000 0.0000 0.0000 286 TYR A CD2 
2022 C CE1 . TYR A 286 ? 168.6495 168.6495 168.6495 0.0000 0.0000 0.0000 286 TYR A CE1 
2023 C CE2 . TYR A 286 ? 168.7076 168.7076 168.7076 0.0000 0.0000 0.0000 286 TYR A CE2 
2024 C CZ  . TYR A 286 ? 168.8621 168.8621 168.8621 0.0000 0.0000 0.0000 286 TYR A CZ  
2025 O OH  . TYR A 286 ? 169.0737 169.0737 169.0737 0.0000 0.0000 0.0000 286 TYR A OH  
2026 N N   . HIS A 287 ? 167.4725 167.4725 167.4725 0.0000 0.0000 0.0000 287 HIS A N   
2027 C CA  . HIS A 287 ? 167.5641 167.5641 167.5641 0.0000 0.0000 0.0000 287 HIS A CA  
2028 C C   . HIS A 287 ? 168.0110 168.0110 168.0110 0.0000 0.0000 0.0000 287 HIS A C   
2029 O O   . HIS A 287 ? 168.4811 168.4811 168.4811 0.0000 0.0000 0.0000 287 HIS A O   
2030 C CB  . HIS A 287 ? 167.6755 167.6755 167.6755 0.0000 0.0000 0.0000 287 HIS A CB  
2031 C CG  . HIS A 287 ? 167.4505 167.4505 167.4505 0.0000 0.0000 0.0000 287 HIS A CG  
2032 N ND1 . HIS A 287 ? 168.0834 168.0834 168.0834 0.0000 0.0000 0.0000 287 HIS A ND1 
2033 C CD2 . HIS A 287 ? 167.2929 167.2929 167.2929 0.0000 0.0000 0.0000 287 HIS A CD2 
2034 C CE1 . HIS A 287 ? 168.2059 168.2059 168.2059 0.0000 0.0000 0.0000 287 HIS A CE1 
2035 N NE2 . HIS A 287 ? 167.7089 167.7089 167.7089 0.0000 0.0000 0.0000 287 HIS A NE2 
2036 N N   . ASN A 288 ? 171.1184 171.1184 171.1184 0.0000 0.0000 0.0000 288 ASN A N   
2037 C CA  . ASN A 288 ? 171.2717 171.2717 171.2717 0.0000 0.0000 0.0000 288 ASN A CA  
2038 C C   . ASN A 288 ? 171.8237 171.8237 171.8237 0.0000 0.0000 0.0000 288 ASN A C   
2039 O O   . ASN A 288 ? 171.8112 171.8112 171.8112 0.0000 0.0000 0.0000 288 ASN A O   
2040 C CB  . ASN A 288 ? 171.1678 171.1678 171.1678 0.0000 0.0000 0.0000 288 ASN A CB  
2041 C CG  . ASN A 288 ? 171.1147 171.1147 171.1147 0.0000 0.0000 0.0000 288 ASN A CG  
2042 O OD1 . ASN A 288 ? 170.9606 170.9606 170.9606 0.0000 0.0000 0.0000 288 ASN A OD1 
2043 N ND2 . ASN A 288 ? 171.2444 171.2444 171.2444 0.0000 0.0000 0.0000 288 ASN A ND2 
2044 N N   . GLU A 289 ? 192.3211 192.3211 192.3211 0.0000 0.0000 0.0000 289 GLU A N   
2045 C CA  . GLU A 289 ? 193.0424 193.0424 193.0424 0.0000 0.0000 0.0000 289 GLU A CA  
2046 C C   . GLU A 289 ? 192.9519 192.9519 192.9519 0.0000 0.0000 0.0000 289 GLU A C   
2047 O O   . GLU A 289 ? 193.4254 193.4254 193.4254 0.0000 0.0000 0.0000 289 GLU A O   
2048 C CB  . GLU A 289 ? 193.3730 193.3730 193.3730 0.0000 0.0000 0.0000 289 GLU A CB  
2049 C CG  . GLU A 289 ? 193.5764 193.5764 193.5764 0.0000 0.0000 0.0000 289 GLU A CG  
2050 C CD  . GLU A 289 ? 193.4006 193.4006 193.4006 0.0000 0.0000 0.0000 289 GLU A CD  
2051 O OE1 . GLU A 289 ? 193.4674 193.4674 193.4674 0.0000 0.0000 0.0000 289 GLU A OE1 
2052 O OE2 . GLU A 289 ? 193.1746 193.1746 193.1746 0.0000 0.0000 0.0000 289 GLU A OE2 
2053 N N   . LEU A 290 ? 183.8835 183.8835 183.8835 0.0000 0.0000 0.0000 290 LEU A N   
2054 C CA  . LEU A 290 ? 183.8469 183.8469 183.8469 0.0000 0.0000 0.0000 290 LEU A CA  
2055 C C   . LEU A 290 ? 183.7858 183.7858 183.7858 0.0000 0.0000 0.0000 290 LEU A C   
2056 O O   . LEU A 290 ? 183.9009 183.9009 183.9009 0.0000 0.0000 0.0000 290 LEU A O   
2057 C CB  . LEU A 290 ? 183.7767 183.7767 183.7767 0.0000 0.0000 0.0000 290 LEU A CB  
2058 C CG  . LEU A 290 ? 183.6409 183.6409 183.6409 0.0000 0.0000 0.0000 290 LEU A CG  
2059 C CD1 . LEU A 290 ? 183.4285 183.4285 183.4285 0.0000 0.0000 0.0000 290 LEU A CD1 
2060 C CD2 . LEU A 290 ? 183.1354 183.1354 183.1354 0.0000 0.0000 0.0000 290 LEU A CD2 
2061 N N   . ASP A 291 ? 183.4417 183.4417 183.4417 0.0000 0.0000 0.0000 291 ASP A N   
2062 C CA  . ASP A 291 ? 183.4474 183.4474 183.4474 0.0000 0.0000 0.0000 291 ASP A CA  
2063 C C   . ASP A 291 ? 183.3647 183.3647 183.3647 0.0000 0.0000 0.0000 291 ASP A C   
2064 O O   . ASP A 291 ? 183.5126 183.5126 183.5126 0.0000 0.0000 0.0000 291 ASP A O   
2065 C CB  . ASP A 291 ? 183.6270 183.6270 183.6270 0.0000 0.0000 0.0000 291 ASP A CB  
2066 C CG  . ASP A 291 ? 183.6371 183.6371 183.6371 0.0000 0.0000 0.0000 291 ASP A CG  
2067 O OD1 . ASP A 291 ? 183.5636 183.5636 183.5636 0.0000 0.0000 0.0000 291 ASP A OD1 
2068 O OD2 . ASP A 291 ? 183.7555 183.7555 183.7555 0.0000 0.0000 0.0000 291 ASP A OD2 
2069 N N   . MET A 292 ? 182.5288 182.5288 182.5288 0.0000 0.0000 0.0000 292 MET A N   
2070 C CA  . MET A 292 ? 182.5501 182.5501 182.5501 0.0000 0.0000 0.0000 292 MET A CA  
2071 C C   . MET A 292 ? 181.9627 181.9627 181.9627 0.0000 0.0000 0.0000 292 MET A C   
2072 O O   . MET A 292 ? 182.0179 182.0179 182.0179 0.0000 0.0000 0.0000 292 MET A O   
2073 C CB  . MET A 292 ? 182.8644 182.8644 182.8644 0.0000 0.0000 0.0000 292 MET A CB  
2074 C CG  . MET A 292 ? 182.8294 182.8294 182.8294 0.0000 0.0000 0.0000 292 MET A CG  
2075 S SD  . MET A 292 ? 182.4413 182.4413 182.4413 0.0000 0.0000 0.0000 292 MET A SD  
2076 C CE  . MET A 292 ? 182.4604 182.4604 182.4604 0.0000 0.0000 0.0000 292 MET A CE  
2077 N N   . ASN A 293 ? 162.1910 162.1910 162.1910 0.0000 0.0000 0.0000 293 ASN A N   
2078 C CA  . ASN A 293 ? 161.5913 161.5913 161.5913 0.0000 0.0000 0.0000 293 ASN A CA  
2079 C C   . ASN A 293 ? 161.5557 161.5557 161.5557 0.0000 0.0000 0.0000 293 ASN A C   
2080 O O   . ASN A 293 ? 161.9502 161.9502 161.9502 0.0000 0.0000 0.0000 293 ASN A O   
2081 C CB  . ASN A 293 ? 161.3941 161.3941 161.3941 0.0000 0.0000 0.0000 293 ASN A CB  
2082 C CG  . ASN A 293 ? 161.5620 161.5620 161.5620 0.0000 0.0000 0.0000 293 ASN A CG  
2083 O OD1 . ASN A 293 ? 161.7910 161.7910 161.7910 0.0000 0.0000 0.0000 293 ASN A OD1 
2084 N ND2 . ASN A 293 ? 161.5909 161.5909 161.5909 0.0000 0.0000 0.0000 293 ASN A ND2 
2085 N N   . LEU A 294 ? 161.2626 161.2626 161.2626 0.0000 0.0000 0.0000 294 LEU A N   
2086 C CA  . LEU A 294 ? 161.2871 161.2871 161.2871 0.0000 0.0000 0.0000 294 LEU A CA  
2087 C C   . LEU A 294 ? 161.4746 161.4746 161.4746 0.0000 0.0000 0.0000 294 LEU A C   
2088 O O   . LEU A 294 ? 161.7258 161.7258 161.7258 0.0000 0.0000 0.0000 294 LEU A O   
2089 C CB  . LEU A 294 ? 161.2637 161.2637 161.2637 0.0000 0.0000 0.0000 294 LEU A CB  
2090 C CG  . LEU A 294 ? 161.2899 161.2899 161.2899 0.0000 0.0000 0.0000 294 LEU A CG  
2091 C CD1 . LEU A 294 ? 161.4459 161.4459 161.4459 0.0000 0.0000 0.0000 294 LEU A CD1 
2092 C CD2 . LEU A 294 ? 161.4643 161.4643 161.4643 0.0000 0.0000 0.0000 294 LEU A CD2 
2093 N N   . TYR A 295 ? 161.3434 161.3434 161.3434 0.0000 0.0000 0.0000 295 TYR A N   
2094 C CA  . TYR A 295 ? 161.2520 161.2520 161.2520 0.0000 0.0000 0.0000 295 TYR A CA  
2095 C C   . TYR A 295 ? 161.3775 161.3775 161.3775 0.0000 0.0000 0.0000 295 TYR A C   
2096 O O   . TYR A 295 ? 161.6212 161.6212 161.6212 0.0000 0.0000 0.0000 295 TYR A O   
2097 C CB  . TYR A 295 ? 161.4270 161.4270 161.4270 0.0000 0.0000 0.0000 295 TYR A CB  
2098 C CG  . TYR A 295 ? 161.4427 161.4427 161.4427 0.0000 0.0000 0.0000 295 TYR A CG  
2099 C CD1 . TYR A 295 ? 161.5443 161.5443 161.5443 0.0000 0.0000 0.0000 295 TYR A CD1 
2100 C CD2 . TYR A 295 ? 161.4501 161.4501 161.4501 0.0000 0.0000 0.0000 295 TYR A CD2 
2101 C CE1 . TYR A 295 ? 161.5208 161.5208 161.5208 0.0000 0.0000 0.0000 295 TYR A CE1 
2102 C CE2 . TYR A 295 ? 161.5105 161.5105 161.5105 0.0000 0.0000 0.0000 295 TYR A CE2 
2103 C CZ  . TYR A 295 ? 161.4846 161.4846 161.4846 0.0000 0.0000 0.0000 295 TYR A CZ  
2104 O OH  . TYR A 295 ? 161.5093 161.5093 161.5093 0.0000 0.0000 0.0000 295 TYR A OH  
2105 N N   . MET A 296 ? 161.4658 161.4658 161.4658 0.0000 0.0000 0.0000 296 MET A N   
2106 C CA  . MET A 296 ? 161.5390 161.5390 161.5390 0.0000 0.0000 0.0000 296 MET A CA  
2107 C C   . MET A 296 ? 161.5434 161.5434 161.5434 0.0000 0.0000 0.0000 296 MET A C   
2108 O O   . MET A 296 ? 161.7179 161.7179 161.7179 0.0000 0.0000 0.0000 296 MET A O   
2109 C CB  . MET A 296 ? 161.5500 161.5500 161.5500 0.0000 0.0000 0.0000 296 MET A CB  
2110 C CG  . MET A 296 ? 161.5438 161.5438 161.5438 0.0000 0.0000 0.0000 296 MET A CG  
2111 S SD  . MET A 296 ? 161.4559 161.4559 161.4559 0.0000 0.0000 0.0000 296 MET A SD  
2112 C CE  . MET A 296 ? 161.5745 161.5745 161.5745 0.0000 0.0000 0.0000 296 MET A CE  
2113 N N   . ARG A 297 ? 161.3475 161.3475 161.3475 0.0000 0.0000 0.0000 297 ARG A N   
2114 C CA  . ARG A 297 ? 161.1756 161.1756 161.1756 0.0000 0.0000 0.0000 297 ARG A CA  
2115 C C   . ARG A 297 ? 161.3453 161.3453 161.3453 0.0000 0.0000 0.0000 297 ARG A C   
2116 O O   . ARG A 297 ? 161.5801 161.5801 161.5801 0.0000 0.0000 0.0000 297 ARG A O   
2117 C CB  . ARG A 297 ? 161.3167 161.3167 161.3167 0.0000 0.0000 0.0000 297 ARG A CB  
2118 C CG  . ARG A 297 ? 161.5346 161.5346 161.5346 0.0000 0.0000 0.0000 297 ARG A CG  
2119 C CD  . ARG A 297 ? 161.3261 161.3261 161.3261 0.0000 0.0000 0.0000 297 ARG A CD  
2120 N NE  . ARG A 297 ? 161.1039 161.1039 161.1039 0.0000 0.0000 0.0000 297 ARG A NE  
2121 C CZ  . ARG A 297 ? 161.3217 161.3217 161.3217 0.0000 0.0000 0.0000 297 ARG A CZ  
2122 N NH1 . ARG A 297 ? 161.4799 161.4799 161.4799 0.0000 0.0000 0.0000 297 ARG A NH1 
2123 N NH2 . ARG A 297 ? 161.5433 161.5433 161.5433 0.0000 0.0000 0.0000 297 ARG A NH2 
2124 N N   . ILE A 298 ? 161.3552 161.3552 161.3552 0.0000 0.0000 0.0000 298 ILE A N   
2125 C CA  . ILE A 298 ? 161.2460 161.2460 161.2460 0.0000 0.0000 0.0000 298 ILE A CA  
2126 C C   . ILE A 298 ? 161.2673 161.2673 161.2673 0.0000 0.0000 0.0000 298 ILE A C   
2127 O O   . ILE A 298 ? 161.2915 161.2915 161.2915 0.0000 0.0000 0.0000 298 ILE A O   
2128 C CB  . ILE A 298 ? 161.2609 161.2609 161.2609 0.0000 0.0000 0.0000 298 ILE A CB  
2129 C CG1 . ILE A 298 ? 161.4966 161.4966 161.4966 0.0000 0.0000 0.0000 298 ILE A CG1 
2130 C CG2 . ILE A 298 ? 161.3882 161.3882 161.3882 0.0000 0.0000 0.0000 298 ILE A CG2 
2131 C CD1 . ILE A 298 ? 161.6988 161.6988 161.6988 0.0000 0.0000 0.0000 298 ILE A CD1 
2132 N N   . ALA A 299 ? 161.3804 161.3804 161.3804 0.0000 0.0000 0.0000 299 ALA A N   
2133 C CA  . ALA A 299 ? 161.1648 161.1648 161.1648 0.0000 0.0000 0.0000 299 ALA A CA  
2134 C C   . ALA A 299 ? 161.2017 161.2017 161.2017 0.0000 0.0000 0.0000 299 ALA A C   
2135 O O   . ALA A 299 ? 161.1702 161.1702 161.1702 0.0000 0.0000 0.0000 299 ALA A O   
2136 C CB  . ALA A 299 ? 160.6368 160.6368 160.6368 0.0000 0.0000 0.0000 299 ALA A CB  
2137 N N   . PRO A 300 ? 161.1120 161.1120 161.1120 0.0000 0.0000 0.0000 300 PRO A N   
2138 C CA  . PRO A 300 ? 161.2450 161.2450 161.2450 0.0000 0.0000 0.0000 300 PRO A CA  
2139 C C   . PRO A 300 ? 161.3995 161.3995 161.3995 0.0000 0.0000 0.0000 300 PRO A C   
2140 O O   . PRO A 300 ? 161.6030 161.6030 161.6030 0.0000 0.0000 0.0000 300 PRO A O   
2141 C CB  . PRO A 300 ? 161.4511 161.4511 161.4511 0.0000 0.0000 0.0000 300 PRO A CB  
2142 C CG  . PRO A 300 ? 161.5007 161.5007 161.5007 0.0000 0.0000 0.0000 300 PRO A CG  
2143 C CD  . PRO A 300 ? 161.4389 161.4389 161.4389 0.0000 0.0000 0.0000 300 PRO A CD  
2144 N N   . GLU A 301 ? 161.3449 161.3449 161.3449 0.0000 0.0000 0.0000 301 GLU A N   
2145 C CA  . GLU A 301 ? 161.2970 161.2970 161.2970 0.0000 0.0000 0.0000 301 GLU A CA  
2146 C C   . GLU A 301 ? 161.2988 161.2988 161.2988 0.0000 0.0000 0.0000 301 GLU A C   
2147 O O   . GLU A 301 ? 161.5021 161.5021 161.5021 0.0000 0.0000 0.0000 301 GLU A O   
2148 C CB  . GLU A 301 ? 161.3560 161.3560 161.3560 0.0000 0.0000 0.0000 301 GLU A CB  
2149 C CG  . GLU A 301 ? 161.1198 161.1198 161.1198 0.0000 0.0000 0.0000 301 GLU A CG  
2150 C CD  . GLU A 301 ? 160.6638 160.6638 160.6638 0.0000 0.0000 0.0000 301 GLU A CD  
2151 O OE1 . GLU A 301 ? 161.6036 161.6036 161.6036 0.0000 0.0000 0.0000 301 GLU A OE1 
2152 O OE2 . GLU A 301 ? 159.2298 159.2298 159.2298 0.0000 0.0000 0.0000 301 GLU A OE2 
2153 N N   . LEU A 302 ? 161.1727 161.1727 161.1727 0.0000 0.0000 0.0000 302 LEU A N   
2154 C CA  . LEU A 302 ? 161.2003 161.2003 161.2003 0.0000 0.0000 0.0000 302 LEU A CA  
2155 C C   . LEU A 302 ? 161.2743 161.2743 161.2743 0.0000 0.0000 0.0000 302 LEU A C   
2156 O O   . LEU A 302 ? 161.5442 161.5442 161.5442 0.0000 0.0000 0.0000 302 LEU A O   
2157 C CB  . LEU A 302 ? 161.4068 161.4068 161.4068 0.0000 0.0000 0.0000 302 LEU A CB  
2158 C CG  . LEU A 302 ? 161.3699 161.3699 161.3699 0.0000 0.0000 0.0000 302 LEU A CG  
2159 C CD1 . LEU A 302 ? 161.6949 161.6949 161.6949 0.0000 0.0000 0.0000 302 LEU A CD1 
2160 C CD2 . LEU A 302 ? 161.4477 161.4477 161.4477 0.0000 0.0000 0.0000 302 LEU A CD2 
2161 N N   . TYR A 303 ? 161.2251 161.2251 161.2251 0.0000 0.0000 0.0000 303 TYR A N   
2162 C CA  . TYR A 303 ? 160.5543 160.5543 160.5543 0.0000 0.0000 0.0000 303 TYR A CA  
2163 C C   . TYR A 303 ? 160.9049 160.9049 160.9049 0.0000 0.0000 0.0000 303 TYR A C   
2164 O O   . TYR A 303 ? 160.8358 160.8358 160.8358 0.0000 0.0000 0.0000 303 TYR A O   
2165 C CB  . TYR A 303 ? 160.2024 160.2024 160.2024 0.0000 0.0000 0.0000 303 TYR A CB  
2166 C CG  . TYR A 303 ? 159.8346 159.8346 159.8346 0.0000 0.0000 0.0000 303 TYR A CG  
2167 C CD1 . TYR A 303 ? 159.2769 159.2769 159.2769 0.0000 0.0000 0.0000 303 TYR A CD1 
2168 C CD2 . TYR A 303 ? 161.3039 161.3039 161.3039 0.0000 0.0000 0.0000 303 TYR A CD2 
2169 C CE1 . TYR A 303 ? 159.7880 159.7880 159.7880 0.0000 0.0000 0.0000 303 TYR A CE1 
2170 C CE2 . TYR A 303 ? 161.3482 161.3482 161.3482 0.0000 0.0000 0.0000 303 TYR A CE2 
2171 C CZ  . TYR A 303 ? 161.3906 161.3906 161.3906 0.0000 0.0000 0.0000 303 TYR A CZ  
2172 O OH  . TYR A 303 ? 161.4205 161.4205 161.4205 0.0000 0.0000 0.0000 303 TYR A OH  
2173 N N   . HIS A 304 ? 161.3600 161.3600 161.3600 0.0000 0.0000 0.0000 304 HIS A N   
2174 C CA  . HIS A 304 ? 161.4396 161.4396 161.4396 0.0000 0.0000 0.0000 304 HIS A CA  
2175 C C   . HIS A 304 ? 161.4851 161.4851 161.4851 0.0000 0.0000 0.0000 304 HIS A C   
2176 O O   . HIS A 304 ? 161.5555 161.5555 161.5555 0.0000 0.0000 0.0000 304 HIS A O   
2177 C CB  . HIS A 304 ? 161.6106 161.6106 161.6106 0.0000 0.0000 0.0000 304 HIS A CB  
2178 C CG  . HIS A 304 ? 161.3864 161.3864 161.3864 0.0000 0.0000 0.0000 304 HIS A CG  
2179 N ND1 . HIS A 304 ? 161.4023 161.4023 161.4023 0.0000 0.0000 0.0000 304 HIS A ND1 
2180 C CD2 . HIS A 304 ? 161.3960 161.3960 161.3960 0.0000 0.0000 0.0000 304 HIS A CD2 
2181 C CE1 . HIS A 304 ? 161.4747 161.4747 161.4747 0.0000 0.0000 0.0000 304 HIS A CE1 
2182 N NE2 . HIS A 304 ? 161.4005 161.4005 161.4005 0.0000 0.0000 0.0000 304 HIS A NE2 
2183 N N   . LYS A 305 ? 161.4361 161.4361 161.4361 0.0000 0.0000 0.0000 305 LYS A N   
2184 C CA  . LYS A 305 ? 161.3384 161.3384 161.3384 0.0000 0.0000 0.0000 305 LYS A CA  
2185 C C   . LYS A 305 ? 161.2325 161.2325 161.2325 0.0000 0.0000 0.0000 305 LYS A C   
2186 O O   . LYS A 305 ? 161.3904 161.3904 161.3904 0.0000 0.0000 0.0000 305 LYS A O   
2187 C CB  . LYS A 305 ? 161.4561 161.4561 161.4561 0.0000 0.0000 0.0000 305 LYS A CB  
2188 C CG  . LYS A 305 ? 161.4337 161.4337 161.4337 0.0000 0.0000 0.0000 305 LYS A CG  
2189 C CD  . LYS A 305 ? 161.4353 161.4353 161.4353 0.0000 0.0000 0.0000 305 LYS A CD  
2190 C CE  . LYS A 305 ? 161.3960 161.3960 161.3960 0.0000 0.0000 0.0000 305 LYS A CE  
2191 N NZ  . LYS A 305 ? 161.7079 161.7079 161.7079 0.0000 0.0000 0.0000 305 LYS A NZ  
2192 N N   . MET A 306 ? 161.2875 161.2875 161.2875 0.0000 0.0000 0.0000 306 MET A N   
2193 C CA  . MET A 306 ? 161.2096 161.2096 161.2096 0.0000 0.0000 0.0000 306 MET A CA  
2194 C C   . MET A 306 ? 161.1778 161.1778 161.1778 0.0000 0.0000 0.0000 306 MET A C   
2195 O O   . MET A 306 ? 161.3956 161.3956 161.3956 0.0000 0.0000 0.0000 306 MET A O   
2196 C CB  . MET A 306 ? 160.8948 160.8948 160.8948 0.0000 0.0000 0.0000 306 MET A CB  
2197 C CG  . MET A 306 ? 161.4576 161.4576 161.4576 0.0000 0.0000 0.0000 306 MET A CG  
2198 S SD  . MET A 306 ? 160.9382 160.9382 160.9382 0.0000 0.0000 0.0000 306 MET A SD  
2199 C CE  . MET A 306 ? 160.7503 160.7503 160.7503 0.0000 0.0000 0.0000 306 MET A CE  
2200 N N   . LEU A 307 ? 161.0180 161.0180 161.0180 0.0000 0.0000 0.0000 307 LEU A N   
2201 C CA  . LEU A 307 ? 161.2929 161.2929 161.2929 0.0000 0.0000 0.0000 307 LEU A CA  
2202 C C   . LEU A 307 ? 161.3742 161.3742 161.3742 0.0000 0.0000 0.0000 307 LEU A C   
2203 O O   . LEU A 307 ? 161.6316 161.6316 161.6316 0.0000 0.0000 0.0000 307 LEU A O   
2204 C CB  . LEU A 307 ? 161.3891 161.3891 161.3891 0.0000 0.0000 0.0000 307 LEU A CB  
2205 C CG  . LEU A 307 ? 160.4858 160.4858 160.4858 0.0000 0.0000 0.0000 307 LEU A CG  
2206 C CD1 . LEU A 307 ? 160.3476 160.3476 160.3476 0.0000 0.0000 0.0000 307 LEU A CD1 
2207 C CD2 . LEU A 307 ? 160.1834 160.1834 160.1834 0.0000 0.0000 0.0000 307 LEU A CD2 
2208 N N   . VAL A 308 ? 161.2733 161.2733 161.2733 0.0000 0.0000 0.0000 308 VAL A N   
2209 C CA  . VAL A 308 ? 161.2254 161.2254 161.2254 0.0000 0.0000 0.0000 308 VAL A CA  
2210 C C   . VAL A 308 ? 161.3188 161.3188 161.3188 0.0000 0.0000 0.0000 308 VAL A C   
2211 O O   . VAL A 308 ? 161.3264 161.3264 161.3264 0.0000 0.0000 0.0000 308 VAL A O   
2212 C CB  . VAL A 308 ? 161.2540 161.2540 161.2540 0.0000 0.0000 0.0000 308 VAL A CB  
2213 C CG1 . VAL A 308 ? 161.4346 161.4346 161.4346 0.0000 0.0000 0.0000 308 VAL A CG1 
2214 C CG2 . VAL A 308 ? 161.3489 161.3489 161.3489 0.0000 0.0000 0.0000 308 VAL A CG2 
2215 N N   . VAL A 309 ? 161.4684 161.4684 161.4684 0.0000 0.0000 0.0000 309 VAL A N   
2216 C CA  . VAL A 309 ? 161.2873 161.2873 161.2873 0.0000 0.0000 0.0000 309 VAL A CA  
2217 C C   . VAL A 309 ? 161.1640 161.1640 161.1640 0.0000 0.0000 0.0000 309 VAL A C   
2218 O O   . VAL A 309 ? 161.1993 161.1993 161.1993 0.0000 0.0000 0.0000 309 VAL A O   
2219 C CB  . VAL A 309 ? 161.3393 161.3393 161.3393 0.0000 0.0000 0.0000 309 VAL A CB  
2220 C CG1 . VAL A 309 ? 161.3173 161.3173 161.3173 0.0000 0.0000 0.0000 309 VAL A CG1 
2221 C CG2 . VAL A 309 ? 161.5110 161.5110 161.5110 0.0000 0.0000 0.0000 309 VAL A CG2 
2222 N N   . GLY A 310 ? 161.3476 161.3476 161.3476 0.0000 0.0000 0.0000 310 GLY A N   
2223 C CA  . GLY A 310 ? 161.4619 161.4619 161.4619 0.0000 0.0000 0.0000 310 GLY A CA  
2224 C C   . GLY A 310 ? 161.4440 161.4440 161.4440 0.0000 0.0000 0.0000 310 GLY A C   
2225 O O   . GLY A 310 ? 161.5679 161.5679 161.5679 0.0000 0.0000 0.0000 310 GLY A O   
2226 N N   . GLY A 311 ? 161.4020 161.4020 161.4020 0.0000 0.0000 0.0000 311 GLY A N   
2227 C CA  . GLY A 311 ? 161.3203 161.3203 161.3203 0.0000 0.0000 0.0000 311 GLY A CA  
2228 C C   . GLY A 311 ? 161.3029 161.3029 161.3029 0.0000 0.0000 0.0000 311 GLY A C   
2229 O O   . GLY A 311 ? 161.4411 161.4411 161.4411 0.0000 0.0000 0.0000 311 GLY A O   
2230 N N   . ILE A 312 ? 161.3398 161.3398 161.3398 0.0000 0.0000 0.0000 312 ILE A N   
2231 C CA  . ILE A 312 ? 161.3238 161.3238 161.3238 0.0000 0.0000 0.0000 312 ILE A CA  
2232 C C   . ILE A 312 ? 161.4616 161.4616 161.4616 0.0000 0.0000 0.0000 312 ILE A C   
2233 O O   . ILE A 312 ? 161.7199 161.7199 161.7199 0.0000 0.0000 0.0000 312 ILE A O   
2234 C CB  . ILE A 312 ? 161.2106 161.2106 161.2106 0.0000 0.0000 0.0000 312 ILE A CB  
2235 C CG1 . ILE A 312 ? 161.4307 161.4307 161.4307 0.0000 0.0000 0.0000 312 ILE A CG1 
2236 C CG2 . ILE A 312 ? 161.1300 161.1300 161.1300 0.0000 0.0000 0.0000 312 ILE A CG2 
2237 C CD1 . ILE A 312 ? 161.6737 161.6737 161.6737 0.0000 0.0000 0.0000 312 ILE A CD1 
2238 N N   . ASP A 313 ? 161.3981 161.3981 161.3981 0.0000 0.0000 0.0000 313 ASP A N   
2239 C CA  . ASP A 313 ? 161.3423 161.3423 161.3423 0.0000 0.0000 0.0000 313 ASP A CA  
2240 C C   . ASP A 313 ? 161.2521 161.2521 161.2521 0.0000 0.0000 0.0000 313 ASP A C   
2241 O O   . ASP A 313 ? 161.4439 161.4439 161.4439 0.0000 0.0000 0.0000 313 ASP A O   
2242 C CB  . ASP A 313 ? 161.2223 161.2223 161.2223 0.0000 0.0000 0.0000 313 ASP A CB  
2243 C CG  . ASP A 313 ? 161.3997 161.3997 161.3997 0.0000 0.0000 0.0000 313 ASP A CG  
2244 O OD1 . ASP A 313 ? 161.3979 161.3979 161.3979 0.0000 0.0000 0.0000 313 ASP A OD1 
2245 O OD2 . ASP A 313 ? 161.6251 161.6251 161.6251 0.0000 0.0000 0.0000 313 ASP A OD2 
2246 N N   . ARG A 314 ? 161.1350 161.1350 161.1350 0.0000 0.0000 0.0000 314 ARG A N   
2247 C CA  . ARG A 314 ? 161.1754 161.1754 161.1754 0.0000 0.0000 0.0000 314 ARG A CA  
2248 C C   . ARG A 314 ? 161.3470 161.3470 161.3470 0.0000 0.0000 0.0000 314 ARG A C   
2249 O O   . ARG A 314 ? 161.3867 161.3867 161.3867 0.0000 0.0000 0.0000 314 ARG A O   
2250 C CB  . ARG A 314 ? 161.3717 161.3717 161.3717 0.0000 0.0000 0.0000 314 ARG A CB  
2251 C CG  . ARG A 314 ? 161.2975 161.2975 161.2975 0.0000 0.0000 0.0000 314 ARG A CG  
2252 C CD  . ARG A 314 ? 161.0970 161.0970 161.0970 0.0000 0.0000 0.0000 314 ARG A CD  
2253 N NE  . ARG A 314 ? 159.4537 159.4537 159.4537 0.0000 0.0000 0.0000 314 ARG A NE  
2254 C CZ  . ARG A 314 ? 158.0570 158.0570 158.0570 0.0000 0.0000 0.0000 314 ARG A CZ  
2255 N NH1 . ARG A 314 ? 159.1962 159.1962 159.1962 0.0000 0.0000 0.0000 314 ARG A NH1 
2256 N NH2 . ARG A 314 ? 155.2210 155.2210 155.2210 0.0000 0.0000 0.0000 314 ARG A NH2 
2257 N N   . VAL A 315 ? 161.2722 161.2722 161.2722 0.0000 0.0000 0.0000 315 VAL A N   
2258 C CA  . VAL A 315 ? 161.2058 161.2058 161.2058 0.0000 0.0000 0.0000 315 VAL A CA  
2259 C C   . VAL A 315 ? 161.3628 161.3628 161.3628 0.0000 0.0000 0.0000 315 VAL A C   
2260 O O   . VAL A 315 ? 161.4631 161.4631 161.4631 0.0000 0.0000 0.0000 315 VAL A O   
2261 C CB  . VAL A 315 ? 161.2180 161.2180 161.2180 0.0000 0.0000 0.0000 315 VAL A CB  
2262 C CG1 . VAL A 315 ? 161.4488 161.4488 161.4488 0.0000 0.0000 0.0000 315 VAL A CG1 
2263 C CG2 . VAL A 315 ? 161.3294 161.3294 161.3294 0.0000 0.0000 0.0000 315 VAL A CG2 
2264 N N   . TYR A 316 ? 161.4542 161.4542 161.4542 0.0000 0.0000 0.0000 316 TYR A N   
2265 C CA  . TYR A 316 ? 161.3251 161.3251 161.3251 0.0000 0.0000 0.0000 316 TYR A CA  
2266 C C   . TYR A 316 ? 161.1860 161.1860 161.1860 0.0000 0.0000 0.0000 316 TYR A C   
2267 O O   . TYR A 316 ? 161.2967 161.2967 161.2967 0.0000 0.0000 0.0000 316 TYR A O   
2268 C CB  . TYR A 316 ? 161.4170 161.4170 161.4170 0.0000 0.0000 0.0000 316 TYR A CB  
2269 C CG  . TYR A 316 ? 161.3099 161.3099 161.3099 0.0000 0.0000 0.0000 316 TYR A CG  
2270 C CD1 . TYR A 316 ? 161.3900 161.3900 161.3900 0.0000 0.0000 0.0000 316 TYR A CD1 
2271 C CD2 . TYR A 316 ? 161.4113 161.4113 161.4113 0.0000 0.0000 0.0000 316 TYR A CD2 
2272 C CE1 . TYR A 316 ? 161.3841 161.3841 161.3841 0.0000 0.0000 0.0000 316 TYR A CE1 
2273 C CE2 . TYR A 316 ? 161.3158 161.3158 161.3158 0.0000 0.0000 0.0000 316 TYR A CE2 
2274 C CZ  . TYR A 316 ? 161.2866 161.2866 161.2866 0.0000 0.0000 0.0000 316 TYR A CZ  
2275 O OH  . TYR A 316 ? 161.7004 161.7004 161.7004 0.0000 0.0000 0.0000 316 TYR A OH  
2276 N N   . GLU A 317 ? 161.1163 161.1163 161.1163 0.0000 0.0000 0.0000 317 GLU A N   
2277 C CA  . GLU A 317 ? 161.2139 161.2139 161.2139 0.0000 0.0000 0.0000 317 GLU A CA  
2278 C C   . GLU A 317 ? 161.3934 161.3934 161.3934 0.0000 0.0000 0.0000 317 GLU A C   
2279 O O   . GLU A 317 ? 161.5964 161.5964 161.5964 0.0000 0.0000 0.0000 317 GLU A O   
2280 C CB  . GLU A 317 ? 161.4060 161.4060 161.4060 0.0000 0.0000 0.0000 317 GLU A CB  
2281 C CG  . GLU A 317 ? 161.5642 161.5642 161.5642 0.0000 0.0000 0.0000 317 GLU A CG  
2282 C CD  . GLU A 317 ? 161.5523 161.5523 161.5523 0.0000 0.0000 0.0000 317 GLU A CD  
2283 O OE1 . GLU A 317 ? 161.6083 161.6083 161.6083 0.0000 0.0000 0.0000 317 GLU A OE1 
2284 O OE2 . GLU A 317 ? 161.6717 161.6717 161.6717 0.0000 0.0000 0.0000 317 GLU A OE2 
2285 N N   . ILE A 318 ? 161.3982 161.3982 161.3982 0.0000 0.0000 0.0000 318 ILE A N   
2286 C CA  . ILE A 318 ? 161.3757 161.3757 161.3757 0.0000 0.0000 0.0000 318 ILE A CA  
2287 C C   . ILE A 318 ? 161.4990 161.4990 161.4990 0.0000 0.0000 0.0000 318 ILE A C   
2288 O O   . ILE A 318 ? 161.5777 161.5777 161.5777 0.0000 0.0000 0.0000 318 ILE A O   
2289 C CB  . ILE A 318 ? 161.2760 161.2760 161.2760 0.0000 0.0000 0.0000 318 ILE A CB  
2290 C CG1 . ILE A 318 ? 161.3828 161.3828 161.3828 0.0000 0.0000 0.0000 318 ILE A CG1 
2291 C CG2 . ILE A 318 ? 161.5520 161.5520 161.5520 0.0000 0.0000 0.0000 318 ILE A CG2 
2292 C CD1 . ILE A 318 ? 161.4710 161.4710 161.4710 0.0000 0.0000 0.0000 318 ILE A CD1 
2293 N N   . GLY A 319 ? 161.5014 161.5014 161.5014 0.0000 0.0000 0.0000 319 GLY A N   
2294 C CA  . GLY A 319 ? 161.3421 161.3421 161.3421 0.0000 0.0000 0.0000 319 GLY A CA  
2295 C C   . GLY A 319 ? 161.2762 161.2762 161.2762 0.0000 0.0000 0.0000 319 GLY A C   
2296 O O   . GLY A 319 ? 161.5808 161.5808 161.5808 0.0000 0.0000 0.0000 319 GLY A O   
2297 N N   . ARG A 320 ? 161.1395 161.1395 161.1395 0.0000 0.0000 0.0000 320 ARG A N   
2298 C CA  . ARG A 320 ? 161.2724 161.2724 161.2724 0.0000 0.0000 0.0000 320 ARG A CA  
2299 C C   . ARG A 320 ? 161.3410 161.3410 161.3410 0.0000 0.0000 0.0000 320 ARG A C   
2300 O O   . ARG A 320 ? 161.4895 161.4895 161.4895 0.0000 0.0000 0.0000 320 ARG A O   
2301 C CB  . ARG A 320 ? 161.4358 161.4358 161.4358 0.0000 0.0000 0.0000 320 ARG A CB  
2302 C CG  . ARG A 320 ? 161.4049 161.4049 161.4049 0.0000 0.0000 0.0000 320 ARG A CG  
2303 C CD  . ARG A 320 ? 161.4354 161.4354 161.4354 0.0000 0.0000 0.0000 320 ARG A CD  
2304 N NE  . ARG A 320 ? 161.4620 161.4620 161.4620 0.0000 0.0000 0.0000 320 ARG A NE  
2305 C CZ  . ARG A 320 ? 161.4404 161.4404 161.4404 0.0000 0.0000 0.0000 320 ARG A CZ  
2306 N NH1 . ARG A 320 ? 161.6260 161.6260 161.6260 0.0000 0.0000 0.0000 320 ARG A NH1 
2307 N NH2 . ARG A 320 ? 161.4291 161.4291 161.4291 0.0000 0.0000 0.0000 320 ARG A NH2 
2308 N N   . GLN A 321 ? 161.1949 161.1949 161.1949 0.0000 0.0000 0.0000 321 GLN A N   
2309 C CA  . GLN A 321 ? 161.2655 161.2655 161.2655 0.0000 0.0000 0.0000 321 GLN A CA  
2310 C C   . GLN A 321 ? 161.4286 161.4286 161.4286 0.0000 0.0000 0.0000 321 GLN A C   
2311 O O   . GLN A 321 ? 161.6944 161.6944 161.6944 0.0000 0.0000 0.0000 321 GLN A O   
2312 C CB  . GLN A 321 ? 161.4490 161.4490 161.4490 0.0000 0.0000 0.0000 321 GLN A CB  
2313 C CG  . GLN A 321 ? 161.5908 161.5908 161.5908 0.0000 0.0000 0.0000 321 GLN A CG  
2314 C CD  . GLN A 321 ? 161.4771 161.4771 161.4771 0.0000 0.0000 0.0000 321 GLN A CD  
2315 O OE1 . GLN A 321 ? 161.3432 161.3432 161.3432 0.0000 0.0000 0.0000 321 GLN A OE1 
2316 N NE2 . GLN A 321 ? 161.6007 161.6007 161.6007 0.0000 0.0000 0.0000 321 GLN A NE2 
2317 N N   . PHE A 322 ? 161.4211 161.4211 161.4211 0.0000 0.0000 0.0000 322 PHE A N   
2318 C CA  . PHE A 322 ? 161.3355 161.3355 161.3355 0.0000 0.0000 0.0000 322 PHE A CA  
2319 C C   . PHE A 322 ? 161.3313 161.3313 161.3313 0.0000 0.0000 0.0000 322 PHE A C   
2320 O O   . PHE A 322 ? 161.3671 161.3671 161.3671 0.0000 0.0000 0.0000 322 PHE A O   
2321 C CB  . PHE A 322 ? 161.4000 161.4000 161.4000 0.0000 0.0000 0.0000 322 PHE A CB  
2322 C CG  . PHE A 322 ? 161.3054 161.3054 161.3054 0.0000 0.0000 0.0000 322 PHE A CG  
2323 C CD1 . PHE A 322 ? 161.3837 161.3837 161.3837 0.0000 0.0000 0.0000 322 PHE A CD1 
2324 C CD2 . PHE A 322 ? 161.4798 161.4798 161.4798 0.0000 0.0000 0.0000 322 PHE A CD2 
2325 C CE1 . PHE A 322 ? 161.4330 161.4330 161.4330 0.0000 0.0000 0.0000 322 PHE A CE1 
2326 C CE2 . PHE A 322 ? 161.4590 161.4590 161.4590 0.0000 0.0000 0.0000 322 PHE A CE2 
2327 C CZ  . PHE A 322 ? 161.4502 161.4502 161.4502 0.0000 0.0000 0.0000 322 PHE A CZ  
2328 N N   . ARG A 323 ? 161.3028 161.3028 161.3028 0.0000 0.0000 0.0000 323 ARG A N   
2329 C CA  . ARG A 323 ? 161.2445 161.2445 161.2445 0.0000 0.0000 0.0000 323 ARG A CA  
2330 C C   . ARG A 323 ? 161.3398 161.3398 161.3398 0.0000 0.0000 0.0000 323 ARG A C   
2331 O O   . ARG A 323 ? 161.5553 161.5553 161.5553 0.0000 0.0000 0.0000 323 ARG A O   
2332 C CB  . ARG A 323 ? 161.2063 161.2063 161.2063 0.0000 0.0000 0.0000 323 ARG A CB  
2333 C CG  . ARG A 323 ? 161.3049 161.3049 161.3049 0.0000 0.0000 0.0000 323 ARG A CG  
2334 C CD  . ARG A 323 ? 161.1079 161.1079 161.1079 0.0000 0.0000 0.0000 323 ARG A CD  
2335 N NE  . ARG A 323 ? 161.4808 161.4808 161.4808 0.0000 0.0000 0.0000 323 ARG A NE  
2336 C CZ  . ARG A 323 ? 161.0917 161.0917 161.0917 0.0000 0.0000 0.0000 323 ARG A CZ  
2337 N NH1 . ARG A 323 ? 159.8550 159.8550 159.8550 0.0000 0.0000 0.0000 323 ARG A NH1 
2338 N NH2 . ARG A 323 ? 160.7085 160.7085 160.7085 0.0000 0.0000 0.0000 323 ARG A NH2 
2339 N N   . ASN A 324 ? 161.3511 161.3511 161.3511 0.0000 0.0000 0.0000 324 ASN A N   
2340 C CA  . ASN A 324 ? 161.3105 161.3105 161.3105 0.0000 0.0000 0.0000 324 ASN A CA  
2341 C C   . ASN A 324 ? 161.3645 161.3645 161.3645 0.0000 0.0000 0.0000 324 ASN A C   
2342 O O   . ASN A 324 ? 161.4952 161.4952 161.4952 0.0000 0.0000 0.0000 324 ASN A O   
2343 C CB  . ASN A 324 ? 161.4049 161.4049 161.4049 0.0000 0.0000 0.0000 324 ASN A CB  
2344 C CG  . ASN A 324 ? 161.3487 161.3487 161.3487 0.0000 0.0000 0.0000 324 ASN A CG  
2345 O OD1 . ASN A 324 ? 161.4903 161.4903 161.4903 0.0000 0.0000 0.0000 324 ASN A OD1 
2346 N ND2 . ASN A 324 ? 161.3579 161.3579 161.3579 0.0000 0.0000 0.0000 324 ASN A ND2 
2347 N N   . GLU A 325 ? 163.8578 163.8578 163.8578 0.0000 0.0000 0.0000 325 GLU A N   
2348 C CA  . GLU A 325 ? 163.8165 163.8165 163.8165 0.0000 0.0000 0.0000 325 GLU A CA  
2349 C C   . GLU A 325 ? 163.9094 163.9094 163.9094 0.0000 0.0000 0.0000 325 GLU A C   
2350 O O   . GLU A 325 ? 164.1773 164.1773 164.1773 0.0000 0.0000 0.0000 325 GLU A O   
2351 C CB  . GLU A 325 ? 163.0614 163.0614 163.0614 0.0000 0.0000 0.0000 325 GLU A CB  
2352 C CG  . GLU A 325 ? 163.0240 163.0240 163.0240 0.0000 0.0000 0.0000 325 GLU A CG  
2353 C CD  . GLU A 325 ? 162.4772 162.4772 162.4772 0.0000 0.0000 0.0000 325 GLU A CD  
2354 O OE1 . GLU A 325 ? 161.9001 161.9001 161.9001 0.0000 0.0000 0.0000 325 GLU A OE1 
2355 O OE2 . GLU A 325 ? 163.0217 163.0217 163.0217 0.0000 0.0000 0.0000 325 GLU A OE2 
2356 N N   . GLY A 326 ? 161.7326 161.7326 161.7326 0.0000 0.0000 0.0000 326 GLY A N   
2357 C CA  . GLY A 326 ? 161.8007 161.8007 161.8007 0.0000 0.0000 0.0000 326 GLY A CA  
2358 C C   . GLY A 326 ? 162.4556 162.4556 162.4556 0.0000 0.0000 0.0000 326 GLY A C   
2359 O O   . GLY A 326 ? 162.6065 162.6065 162.6065 0.0000 0.0000 0.0000 326 GLY A O   
2360 N N   . ILE A 327 ? 161.8468 161.8468 161.8468 0.0000 0.0000 0.0000 327 ILE A N   
2361 C CA  . ILE A 327 ? 162.0084 162.0084 162.0084 0.0000 0.0000 0.0000 327 ILE A CA  
2362 C C   . ILE A 327 ? 161.9206 161.9206 161.9206 0.0000 0.0000 0.0000 327 ILE A C   
2363 O O   . ILE A 327 ? 161.7410 161.7410 161.7410 0.0000 0.0000 0.0000 327 ILE A O   
2364 C CB  . ILE A 327 ? 161.8981 161.8981 161.8981 0.0000 0.0000 0.0000 327 ILE A CB  
2365 C CG1 . ILE A 327 ? 161.8544 161.8544 161.8544 0.0000 0.0000 0.0000 327 ILE A CG1 
2366 C CG2 . ILE A 327 ? 162.0309 162.0309 162.0309 0.0000 0.0000 0.0000 327 ILE A CG2 
2367 C CD1 . ILE A 327 ? 161.9219 161.9219 161.9219 0.0000 0.0000 0.0000 327 ILE A CD1 
2368 N N   . ASP A 328 ? 164.1287 164.1287 164.1287 0.0000 0.0000 0.0000 328 ASP A N   
2369 C CA  . ASP A 328 ? 164.0748 164.0748 164.0748 0.0000 0.0000 0.0000 328 ASP A CA  
2370 C C   . ASP A 328 ? 164.0762 164.0762 164.0762 0.0000 0.0000 0.0000 328 ASP A C   
2371 O O   . ASP A 328 ? 164.1676 164.1676 164.1676 0.0000 0.0000 0.0000 328 ASP A O   
2372 C CB  . ASP A 328 ? 164.2277 164.2277 164.2277 0.0000 0.0000 0.0000 328 ASP A CB  
2373 C CG  . ASP A 328 ? 164.3184 164.3184 164.3184 0.0000 0.0000 0.0000 328 ASP A CG  
2374 O OD1 . ASP A 328 ? 164.2281 164.2281 164.2281 0.0000 0.0000 0.0000 328 ASP A OD1 
2375 O OD2 . ASP A 328 ? 164.4064 164.4064 164.4064 0.0000 0.0000 0.0000 328 ASP A OD2 
2376 N N   . LEU A 329 ? 161.2586 161.2586 161.2586 0.0000 0.0000 0.0000 329 LEU A N   
2377 C CA  . LEU A 329 ? 161.4157 161.4157 161.4157 0.0000 0.0000 0.0000 329 LEU A CA  
2378 C C   . LEU A 329 ? 161.4278 161.4278 161.4278 0.0000 0.0000 0.0000 329 LEU A C   
2379 O O   . LEU A 329 ? 161.5343 161.5343 161.5343 0.0000 0.0000 0.0000 329 LEU A O   
2380 C CB  . LEU A 329 ? 161.0834 161.0834 161.0834 0.0000 0.0000 0.0000 329 LEU A CB  
2381 C CG  . LEU A 329 ? 159.6633 159.6633 159.6633 0.0000 0.0000 0.0000 329 LEU A CG  
2382 C CD1 . LEU A 329 ? 159.7221 159.7221 159.7221 0.0000 0.0000 0.0000 329 LEU A CD1 
2383 C CD2 . LEU A 329 ? 160.0051 160.0051 160.0051 0.0000 0.0000 0.0000 329 LEU A CD2 
2384 N N   . THR A 330 ? 161.4317 161.4317 161.4317 0.0000 0.0000 0.0000 330 THR A N   
2385 C CA  . THR A 330 ? 161.3955 161.3955 161.3955 0.0000 0.0000 0.0000 330 THR A CA  
2386 C C   . THR A 330 ? 161.4669 161.4669 161.4669 0.0000 0.0000 0.0000 330 THR A C   
2387 O O   . THR A 330 ? 161.5137 161.5137 161.5137 0.0000 0.0000 0.0000 330 THR A O   
2388 C CB  . THR A 330 ? 161.5425 161.5425 161.5425 0.0000 0.0000 0.0000 330 THR A CB  
2389 O OG1 . THR A 330 ? 161.6270 161.6270 161.6270 0.0000 0.0000 0.0000 330 THR A OG1 
2390 C CG2 . THR A 330 ? 161.6289 161.6289 161.6289 0.0000 0.0000 0.0000 330 THR A CG2 
2391 N N   . HIS A 331 ? 161.5082 161.5082 161.5082 0.0000 0.0000 0.0000 331 HIS A N   
2392 C CA  . HIS A 331 ? 161.4108 161.4108 161.4108 0.0000 0.0000 0.0000 331 HIS A CA  
2393 C C   . HIS A 331 ? 161.2676 161.2676 161.2676 0.0000 0.0000 0.0000 331 HIS A C   
2394 O O   . HIS A 331 ? 161.2294 161.2294 161.2294 0.0000 0.0000 0.0000 331 HIS A O   
2395 C CB  . HIS A 331 ? 161.4205 161.4205 161.4205 0.0000 0.0000 0.0000 331 HIS A CB  
2396 C CG  . HIS A 331 ? 160.7899 160.7899 160.7899 0.0000 0.0000 0.0000 331 HIS A CG  
2397 N ND1 . HIS A 331 ? 160.7274 160.7274 160.7274 0.0000 0.0000 0.0000 331 HIS A ND1 
2398 C CD2 . HIS A 331 ? 160.7324 160.7324 160.7324 0.0000 0.0000 0.0000 331 HIS A CD2 
2399 C CE1 . HIS A 331 ? 160.4244 160.4244 160.4244 0.0000 0.0000 0.0000 331 HIS A CE1 
2400 N NE2 . HIS A 331 ? 160.4100 160.4100 160.4100 0.0000 0.0000 0.0000 331 HIS A NE2 
2401 N N   . ASN A 332 ? 161.3611 161.3611 161.3611 0.0000 0.0000 0.0000 332 ASN A N   
2402 C CA  . ASN A 332 ? 161.4467 161.4467 161.4467 0.0000 0.0000 0.0000 332 ASN A CA  
2403 C C   . ASN A 332 ? 161.3524 161.3524 161.3524 0.0000 0.0000 0.0000 332 ASN A C   
2404 O O   . ASN A 332 ? 161.3800 161.3800 161.3800 0.0000 0.0000 0.0000 332 ASN A O   
2405 C CB  . ASN A 332 ? 161.6307 161.6307 161.6307 0.0000 0.0000 0.0000 332 ASN A CB  
2406 C CG  . ASN A 332 ? 161.5834 161.5834 161.5834 0.0000 0.0000 0.0000 332 ASN A CG  
2407 O OD1 . ASN A 332 ? 161.4645 161.4645 161.4645 0.0000 0.0000 0.0000 332 ASN A OD1 
2408 N ND2 . ASN A 332 ? 161.6156 161.6156 161.6156 0.0000 0.0000 0.0000 332 ASN A ND2 
2409 N N   . PRO A 333 ? 161.1938 161.1938 161.1938 0.0000 0.0000 0.0000 333 PRO A N   
2410 C CA  . PRO A 333 ? 161.3037 161.3037 161.3037 0.0000 0.0000 0.0000 333 PRO A CA  
2411 C C   . PRO A 333 ? 161.4073 161.4073 161.4073 0.0000 0.0000 0.0000 333 PRO A C   
2412 O O   . PRO A 333 ? 161.6726 161.6726 161.6726 0.0000 0.0000 0.0000 333 PRO A O   
2413 C CB  . PRO A 333 ? 161.4781 161.4781 161.4781 0.0000 0.0000 0.0000 333 PRO A CB  
2414 C CG  . PRO A 333 ? 161.4566 161.4566 161.4566 0.0000 0.0000 0.0000 333 PRO A CG  
2415 C CD  . PRO A 333 ? 161.3692 161.3692 161.3692 0.0000 0.0000 0.0000 333 PRO A CD  
2416 N N   . GLU A 334 ? 161.3462 161.3462 161.3462 0.0000 0.0000 0.0000 334 GLU A N   
2417 C CA  . GLU A 334 ? 161.3787 161.3787 161.3787 0.0000 0.0000 0.0000 334 GLU A CA  
2418 C C   . GLU A 334 ? 161.3353 161.3353 161.3353 0.0000 0.0000 0.0000 334 GLU A C   
2419 O O   . GLU A 334 ? 161.4071 161.4071 161.4071 0.0000 0.0000 0.0000 334 GLU A O   
2420 C CB  . GLU A 334 ? 161.4053 161.4053 161.4053 0.0000 0.0000 0.0000 334 GLU A CB  
2421 C CG  . GLU A 334 ? 161.4537 161.4537 161.4537 0.0000 0.0000 0.0000 334 GLU A CG  
2422 C CD  . GLU A 334 ? 161.4140 161.4140 161.4140 0.0000 0.0000 0.0000 334 GLU A CD  
2423 O OE1 . GLU A 334 ? 161.5755 161.5755 161.5755 0.0000 0.0000 0.0000 334 GLU A OE1 
2424 O OE2 . GLU A 334 ? 161.4176 161.4176 161.4176 0.0000 0.0000 0.0000 334 GLU A OE2 
2425 N N   . PHE A 335 ? 161.4150 161.4150 161.4150 0.0000 0.0000 0.0000 335 PHE A N   
2426 C CA  . PHE A 335 ? 161.4186 161.4186 161.4186 0.0000 0.0000 0.0000 335 PHE A CA  
2427 C C   . PHE A 335 ? 161.3917 161.3917 161.3917 0.0000 0.0000 0.0000 335 PHE A C   
2428 O O   . PHE A 335 ? 161.5612 161.5612 161.5612 0.0000 0.0000 0.0000 335 PHE A O   
2429 C CB  . PHE A 335 ? 161.5650 161.5650 161.5650 0.0000 0.0000 0.0000 335 PHE A CB  
2430 C CG  . PHE A 335 ? 161.4787 161.4787 161.4787 0.0000 0.0000 0.0000 335 PHE A CG  
2431 C CD1 . PHE A 335 ? 161.5269 161.5269 161.5269 0.0000 0.0000 0.0000 335 PHE A CD1 
2432 C CD2 . PHE A 335 ? 161.3436 161.3436 161.3436 0.0000 0.0000 0.0000 335 PHE A CD2 
2433 C CE1 . PHE A 335 ? 161.5592 161.5592 161.5592 0.0000 0.0000 0.0000 335 PHE A CE1 
2434 C CE2 . PHE A 335 ? 161.2848 161.2848 161.2848 0.0000 0.0000 0.0000 335 PHE A CE2 
2435 C CZ  . PHE A 335 ? 161.4768 161.4768 161.4768 0.0000 0.0000 0.0000 335 PHE A CZ  
2436 N N   . THR A 336 ? 161.1190 161.1190 161.1190 0.0000 0.0000 0.0000 336 THR A N   
2437 C CA  . THR A 336 ? 161.0657 161.0657 161.0657 0.0000 0.0000 0.0000 336 THR A CA  
2438 C C   . THR A 336 ? 161.2637 161.2637 161.2637 0.0000 0.0000 0.0000 336 THR A C   
2439 O O   . THR A 336 ? 161.4829 161.4829 161.4829 0.0000 0.0000 0.0000 336 THR A O   
2440 C CB  . THR A 336 ? 161.2225 161.2225 161.2225 0.0000 0.0000 0.0000 336 THR A CB  
2441 O OG1 . THR A 336 ? 161.4300 161.4300 161.4300 0.0000 0.0000 0.0000 336 THR A OG1 
2442 C CG2 . THR A 336 ? 161.3764 161.3764 161.3764 0.0000 0.0000 0.0000 336 THR A CG2 
2443 N N   . THR A 337 ? 161.4359 161.4359 161.4359 0.0000 0.0000 0.0000 337 THR A N   
2444 C CA  . THR A 337 ? 161.3576 161.3576 161.3576 0.0000 0.0000 0.0000 337 THR A CA  
2445 C C   . THR A 337 ? 161.3798 161.3798 161.3798 0.0000 0.0000 0.0000 337 THR A C   
2446 O O   . THR A 337 ? 161.6323 161.6323 161.6323 0.0000 0.0000 0.0000 337 THR A O   
2447 C CB  . THR A 337 ? 161.3578 161.3578 161.3578 0.0000 0.0000 0.0000 337 THR A CB  
2448 O OG1 . THR A 337 ? 161.4834 161.4834 161.4834 0.0000 0.0000 0.0000 337 THR A OG1 
2449 C CG2 . THR A 337 ? 161.6033 161.6033 161.6033 0.0000 0.0000 0.0000 337 THR A CG2 
2450 N N   . CYS A 338 ? 161.3278 161.3278 161.3278 0.0000 0.0000 0.0000 338 CYS A N   
2451 C CA  . CYS A 338 ? 161.3440 161.3440 161.3440 0.0000 0.0000 0.0000 338 CYS A CA  
2452 C C   . CYS A 338 ? 161.4018 161.4018 161.4018 0.0000 0.0000 0.0000 338 CYS A C   
2453 O O   . CYS A 338 ? 161.5636 161.5636 161.5636 0.0000 0.0000 0.0000 338 CYS A O   
2454 C CB  . CYS A 338 ? 161.4040 161.4040 161.4040 0.0000 0.0000 0.0000 338 CYS A CB  
2455 S SG  . CYS A 338 ? 161.5699 161.5699 161.5699 0.0000 0.0000 0.0000 338 CYS A SG  
2456 N N   . GLU A 339 ? 161.3773 161.3773 161.3773 0.0000 0.0000 0.0000 339 GLU A N   
2457 C CA  . GLU A 339 ? 161.2835 161.2835 161.2835 0.0000 0.0000 0.0000 339 GLU A CA  
2458 C C   . GLU A 339 ? 161.3526 161.3526 161.3526 0.0000 0.0000 0.0000 339 GLU A C   
2459 O O   . GLU A 339 ? 161.4747 161.4747 161.4747 0.0000 0.0000 0.0000 339 GLU A O   
2460 C CB  . GLU A 339 ? 161.3228 161.3228 161.3228 0.0000 0.0000 0.0000 339 GLU A CB  
2461 C CG  . GLU A 339 ? 161.4654 161.4654 161.4654 0.0000 0.0000 0.0000 339 GLU A CG  
2462 C CD  . GLU A 339 ? 161.3934 161.3934 161.3934 0.0000 0.0000 0.0000 339 GLU A CD  
2463 O OE1 . GLU A 339 ? 161.4471 161.4471 161.4471 0.0000 0.0000 0.0000 339 GLU A OE1 
2464 O OE2 . GLU A 339 ? 161.5080 161.5080 161.5080 0.0000 0.0000 0.0000 339 GLU A OE2 
2465 N N   . PHE A 340 ? 161.4268 161.4268 161.4268 0.0000 0.0000 0.0000 340 PHE A N   
2466 C CA  . PHE A 340 ? 161.3916 161.3916 161.3916 0.0000 0.0000 0.0000 340 PHE A CA  
2467 C C   . PHE A 340 ? 161.4050 161.4050 161.4050 0.0000 0.0000 0.0000 340 PHE A C   
2468 O O   . PHE A 340 ? 161.6103 161.6103 161.6103 0.0000 0.0000 0.0000 340 PHE A O   
2469 C CB  . PHE A 340 ? 161.4473 161.4473 161.4473 0.0000 0.0000 0.0000 340 PHE A CB  
2470 C CG  . PHE A 340 ? 161.3313 161.3313 161.3313 0.0000 0.0000 0.0000 340 PHE A CG  
2471 C CD1 . PHE A 340 ? 161.3913 161.3913 161.3913 0.0000 0.0000 0.0000 340 PHE A CD1 
2472 C CD2 . PHE A 340 ? 161.4505 161.4505 161.4505 0.0000 0.0000 0.0000 340 PHE A CD2 
2473 C CE1 . PHE A 340 ? 161.4764 161.4764 161.4764 0.0000 0.0000 0.0000 340 PHE A CE1 
2474 C CE2 . PHE A 340 ? 161.4438 161.4438 161.4438 0.0000 0.0000 0.0000 340 PHE A CE2 
2475 C CZ  . PHE A 340 ? 161.4213 161.4213 161.4213 0.0000 0.0000 0.0000 340 PHE A CZ  
2476 N N   . TYR A 341 ? 161.3316 161.3316 161.3316 0.0000 0.0000 0.0000 341 TYR A N   
2477 C CA  . TYR A 341 ? 161.2768 161.2768 161.2768 0.0000 0.0000 0.0000 341 TYR A CA  
2478 C C   . TYR A 341 ? 161.3056 161.3056 161.3056 0.0000 0.0000 0.0000 341 TYR A C   
2479 O O   . TYR A 341 ? 161.5538 161.5538 161.5538 0.0000 0.0000 0.0000 341 TYR A O   
2480 C CB  . TYR A 341 ? 161.3101 161.3101 161.3101 0.0000 0.0000 0.0000 341 TYR A CB  
2481 C CG  . TYR A 341 ? 161.1838 161.1838 161.1838 0.0000 0.0000 0.0000 341 TYR A CG  
2482 C CD1 . TYR A 341 ? 161.2982 161.2982 161.2982 0.0000 0.0000 0.0000 341 TYR A CD1 
2483 C CD2 . TYR A 341 ? 161.2872 161.2872 161.2872 0.0000 0.0000 0.0000 341 TYR A CD2 
2484 C CE1 . TYR A 341 ? 161.2631 161.2631 161.2631 0.0000 0.0000 0.0000 341 TYR A CE1 
2485 C CE2 . TYR A 341 ? 161.3616 161.3616 161.3616 0.0000 0.0000 0.0000 341 TYR A CE2 
2486 C CZ  . TYR A 341 ? 161.2222 161.2222 161.2222 0.0000 0.0000 0.0000 341 TYR A CZ  
2487 O OH  . TYR A 341 ? 161.5199 161.5199 161.5199 0.0000 0.0000 0.0000 341 TYR A OH  
2488 N N   . MET A 342 ? 161.2572 161.2572 161.2572 0.0000 0.0000 0.0000 342 MET A N   
2489 C CA  . MET A 342 ? 161.2854 161.2854 161.2854 0.0000 0.0000 0.0000 342 MET A CA  
2490 C C   . MET A 342 ? 161.3776 161.3776 161.3776 0.0000 0.0000 0.0000 342 MET A C   
2491 O O   . MET A 342 ? 161.6166 161.6166 161.6166 0.0000 0.0000 0.0000 342 MET A O   
2492 C CB  . MET A 342 ? 161.3230 161.3230 161.3230 0.0000 0.0000 0.0000 342 MET A CB  
2493 C CG  . MET A 342 ? 161.0073 161.0073 161.0073 0.0000 0.0000 0.0000 342 MET A CG  
2494 S SD  . MET A 342 ? 160.4481 160.4481 160.4481 0.0000 0.0000 0.0000 342 MET A SD  
2495 C CE  . MET A 342 ? 160.5878 160.5878 160.5878 0.0000 0.0000 0.0000 342 MET A CE  
2496 N N   . ALA A 343 ? 161.3302 161.3302 161.3302 0.0000 0.0000 0.0000 343 ALA A N   
2497 C CA  . ALA A 343 ? 161.2712 161.2712 161.2712 0.0000 0.0000 0.0000 343 ALA A CA  
2498 C C   . ALA A 343 ? 161.3798 161.3798 161.3798 0.0000 0.0000 0.0000 343 ALA A C   
2499 O O   . ALA A 343 ? 160.7159 160.7159 160.7159 0.0000 0.0000 0.0000 343 ALA A O   
2500 C CB  . ALA A 343 ? 161.3194 161.3194 161.3194 0.0000 0.0000 0.0000 343 ALA A CB  
2501 N N   . TYR A 344 ? 161.5084 161.5084 161.5084 0.0000 0.0000 0.0000 344 TYR A N   
2502 C CA  . TYR A 344 ? 161.3912 161.3912 161.3912 0.0000 0.0000 0.0000 344 TYR A CA  
2503 C C   . TYR A 344 ? 160.9681 160.9681 160.9681 0.0000 0.0000 0.0000 344 TYR A C   
2504 O O   . TYR A 344 ? 160.9378 160.9378 160.9378 0.0000 0.0000 0.0000 344 TYR A O   
2505 C CB  . TYR A 344 ? 160.8666 160.8666 160.8666 0.0000 0.0000 0.0000 344 TYR A CB  
2506 C CG  . TYR A 344 ? 160.7484 160.7484 160.7484 0.0000 0.0000 0.0000 344 TYR A CG  
2507 C CD1 . TYR A 344 ? 161.2119 161.2119 161.2119 0.0000 0.0000 0.0000 344 TYR A CD1 
2508 C CD2 . TYR A 344 ? 160.5534 160.5534 160.5534 0.0000 0.0000 0.0000 344 TYR A CD2 
2509 C CE1 . TYR A 344 ? 161.2930 161.2930 161.2930 0.0000 0.0000 0.0000 344 TYR A CE1 
2510 C CE2 . TYR A 344 ? 161.1162 161.1162 161.1162 0.0000 0.0000 0.0000 344 TYR A CE2 
2511 C CZ  . TYR A 344 ? 161.2769 161.2769 161.2769 0.0000 0.0000 0.0000 344 TYR A CZ  
2512 O OH  . TYR A 344 ? 161.4397 161.4397 161.4397 0.0000 0.0000 0.0000 344 TYR A OH  
2513 N N   . ALA A 345 ? 160.9860 160.9860 160.9860 0.0000 0.0000 0.0000 345 ALA A N   
2514 C CA  . ALA A 345 ? 160.8963 160.8963 160.8963 0.0000 0.0000 0.0000 345 ALA A CA  
2515 C C   . ALA A 345 ? 161.3851 161.3851 161.3851 0.0000 0.0000 0.0000 345 ALA A C   
2516 O O   . ALA A 345 ? 161.5122 161.5122 161.5122 0.0000 0.0000 0.0000 345 ALA A O   
2517 C CB  . ALA A 345 ? 160.6731 160.6731 160.6731 0.0000 0.0000 0.0000 345 ALA A CB  
2518 N N   . ASP A 346 ? 161.3530 161.3530 161.3530 0.0000 0.0000 0.0000 346 ASP A N   
2519 C CA  . ASP A 346 ? 161.2452 161.2452 161.2452 0.0000 0.0000 0.0000 346 ASP A CA  
2520 C C   . ASP A 346 ? 161.3523 161.3523 161.3523 0.0000 0.0000 0.0000 346 ASP A C   
2521 O O   . ASP A 346 ? 161.7498 161.7498 161.7498 0.0000 0.0000 0.0000 346 ASP A O   
2522 C CB  . ASP A 346 ? 161.3668 161.3668 161.3668 0.0000 0.0000 0.0000 346 ASP A CB  
2523 C CG  . ASP A 346 ? 161.5011 161.5011 161.5011 0.0000 0.0000 0.0000 346 ASP A CG  
2524 O OD1 . ASP A 346 ? 161.6139 161.6139 161.6139 0.0000 0.0000 0.0000 346 ASP A OD1 
2525 O OD2 . ASP A 346 ? 161.4875 161.4875 161.4875 0.0000 0.0000 0.0000 346 ASP A OD2 
2526 N N   . TYR A 347 ? 161.3151 161.3151 161.3151 0.0000 0.0000 0.0000 347 TYR A N   
2527 C CA  . TYR A 347 ? 161.3143 161.3143 161.3143 0.0000 0.0000 0.0000 347 TYR A CA  
2528 C C   . TYR A 347 ? 161.3647 161.3647 161.3647 0.0000 0.0000 0.0000 347 TYR A C   
2529 O O   . TYR A 347 ? 161.7379 161.7379 161.7379 0.0000 0.0000 0.0000 347 TYR A O   
2530 C CB  . TYR A 347 ? 161.4032 161.4032 161.4032 0.0000 0.0000 0.0000 347 TYR A CB  
2531 C CG  . TYR A 347 ? 161.2866 161.2866 161.2866 0.0000 0.0000 0.0000 347 TYR A CG  
2532 C CD1 . TYR A 347 ? 161.4678 161.4678 161.4678 0.0000 0.0000 0.0000 347 TYR A CD1 
2533 C CD2 . TYR A 347 ? 161.4355 161.4355 161.4355 0.0000 0.0000 0.0000 347 TYR A CD2 
2534 C CE1 . TYR A 347 ? 161.5465 161.5465 161.5465 0.0000 0.0000 0.0000 347 TYR A CE1 
2535 C CE2 . TYR A 347 ? 161.4787 161.4787 161.4787 0.0000 0.0000 0.0000 347 TYR A CE2 
2536 C CZ  . TYR A 347 ? 161.4809 161.4809 161.4809 0.0000 0.0000 0.0000 347 TYR A CZ  
2537 O OH  . TYR A 347 ? 161.5960 161.5960 161.5960 0.0000 0.0000 0.0000 347 TYR A OH  
2538 N N   . HIS A 348 ? 161.3597 161.3597 161.3597 0.0000 0.0000 0.0000 348 HIS A N   
2539 C CA  . HIS A 348 ? 161.2600 161.2600 161.2600 0.0000 0.0000 0.0000 348 HIS A CA  
2540 C C   . HIS A 348 ? 161.0595 161.0595 161.0595 0.0000 0.0000 0.0000 348 HIS A C   
2541 O O   . HIS A 348 ? 161.1954 161.1954 161.1954 0.0000 0.0000 0.0000 348 HIS A O   
2542 C CB  . HIS A 348 ? 161.0592 161.0592 161.0592 0.0000 0.0000 0.0000 348 HIS A CB  
2543 C CG  . HIS A 348 ? 161.2081 161.2081 161.2081 0.0000 0.0000 0.0000 348 HIS A CG  
2544 N ND1 . HIS A 348 ? 161.4891 161.4891 161.4891 0.0000 0.0000 0.0000 348 HIS A ND1 
2545 C CD2 . HIS A 348 ? 161.3029 161.3029 161.3029 0.0000 0.0000 0.0000 348 HIS A CD2 
2546 C CE1 . HIS A 348 ? 161.4618 161.4618 161.4618 0.0000 0.0000 0.0000 348 HIS A CE1 
2547 N NE2 . HIS A 348 ? 161.3288 161.3288 161.3288 0.0000 0.0000 0.0000 348 HIS A NE2 
2548 N N   . ASP A 349 ? 160.9574 160.9574 160.9574 0.0000 0.0000 0.0000 349 ASP A N   
2549 C CA  . ASP A 349 ? 160.6690 160.6690 160.6690 0.0000 0.0000 0.0000 349 ASP A CA  
2550 C C   . ASP A 349 ? 161.2676 161.2676 161.2676 0.0000 0.0000 0.0000 349 ASP A C   
2551 O O   . ASP A 349 ? 161.4188 161.4188 161.4188 0.0000 0.0000 0.0000 349 ASP A O   
2552 C CB  . ASP A 349 ? 160.4779 160.4779 160.4779 0.0000 0.0000 0.0000 349 ASP A CB  
2553 C CG  . ASP A 349 ? 160.2840 160.2840 160.2840 0.0000 0.0000 0.0000 349 ASP A CG  
2554 O OD1 . ASP A 349 ? 160.2012 160.2012 160.2012 0.0000 0.0000 0.0000 349 ASP A OD1 
2555 O OD2 . ASP A 349 ? 160.5565 160.5565 160.5565 0.0000 0.0000 0.0000 349 ASP A OD2 
2556 N N   . LEU A 350 ? 161.2522 161.2522 161.2522 0.0000 0.0000 0.0000 350 LEU A N   
2557 C CA  . LEU A 350 ? 161.2874 161.2874 161.2874 0.0000 0.0000 0.0000 350 LEU A CA  
2558 C C   . LEU A 350 ? 161.2998 161.2998 161.2998 0.0000 0.0000 0.0000 350 LEU A C   
2559 O O   . LEU A 350 ? 161.4781 161.4781 161.4781 0.0000 0.0000 0.0000 350 LEU A O   
2560 C CB  . LEU A 350 ? 161.3661 161.3661 161.3661 0.0000 0.0000 0.0000 350 LEU A CB  
2561 C CG  . LEU A 350 ? 161.4382 161.4382 161.4382 0.0000 0.0000 0.0000 350 LEU A CG  
2562 C CD1 . LEU A 350 ? 161.5475 161.5475 161.5475 0.0000 0.0000 0.0000 350 LEU A CD1 
2563 C CD2 . LEU A 350 ? 161.4690 161.4690 161.4690 0.0000 0.0000 0.0000 350 LEU A CD2 
2564 N N   . MET A 351 ? 161.3265 161.3265 161.3265 0.0000 0.0000 0.0000 351 MET A N   
2565 C CA  . MET A 351 ? 161.2975 161.2975 161.2975 0.0000 0.0000 0.0000 351 MET A CA  
2566 C C   . MET A 351 ? 161.2978 161.2978 161.2978 0.0000 0.0000 0.0000 351 MET A C   
2567 O O   . MET A 351 ? 161.5791 161.5791 161.5791 0.0000 0.0000 0.0000 351 MET A O   
2568 C CB  . MET A 351 ? 161.4519 161.4519 161.4519 0.0000 0.0000 0.0000 351 MET A CB  
2569 C CG  . MET A 351 ? 161.5319 161.5319 161.5319 0.0000 0.0000 0.0000 351 MET A CG  
2570 S SD  . MET A 351 ? 161.2879 161.2879 161.2879 0.0000 0.0000 0.0000 351 MET A SD  
2571 C CE  . MET A 351 ? 161.4685 161.4685 161.4685 0.0000 0.0000 0.0000 351 MET A CE  
2572 N N   . GLU A 352 ? 161.2248 161.2248 161.2248 0.0000 0.0000 0.0000 352 GLU A N   
2573 C CA  . GLU A 352 ? 161.2623 161.2623 161.2623 0.0000 0.0000 0.0000 352 GLU A CA  
2574 C C   . GLU A 352 ? 161.2379 161.2379 161.2379 0.0000 0.0000 0.0000 352 GLU A C   
2575 O O   . GLU A 352 ? 161.1646 161.1646 161.1646 0.0000 0.0000 0.0000 352 GLU A O   
2576 C CB  . GLU A 352 ? 161.4224 161.4224 161.4224 0.0000 0.0000 0.0000 352 GLU A CB  
2577 C CG  . GLU A 352 ? 161.3957 161.3957 161.3957 0.0000 0.0000 0.0000 352 GLU A CG  
2578 C CD  . GLU A 352 ? 160.6436 160.6436 160.6436 0.0000 0.0000 0.0000 352 GLU A CD  
2579 O OE1 . GLU A 352 ? 160.3765 160.3765 160.3765 0.0000 0.0000 0.0000 352 GLU A OE1 
2580 O OE2 . GLU A 352 ? 160.3543 160.3543 160.3543 0.0000 0.0000 0.0000 352 GLU A OE2 
2581 N N   . ILE A 353 ? 161.1133 161.1133 161.1133 0.0000 0.0000 0.0000 353 ILE A N   
2582 C CA  . ILE A 353 ? 160.8978 160.8978 160.8978 0.0000 0.0000 0.0000 353 ILE A CA  
2583 C C   . ILE A 353 ? 161.3210 161.3210 161.3210 0.0000 0.0000 0.0000 353 ILE A C   
2584 O O   . ILE A 353 ? 161.3787 161.3787 161.3787 0.0000 0.0000 0.0000 353 ILE A O   
2585 C CB  . ILE A 353 ? 161.0910 161.0910 161.0910 0.0000 0.0000 0.0000 353 ILE A CB  
2586 C CG1 . ILE A 353 ? 160.9185 160.9185 160.9185 0.0000 0.0000 0.0000 353 ILE A CG1 
2587 C CG2 . ILE A 353 ? 161.2064 161.2064 161.2064 0.0000 0.0000 0.0000 353 ILE A CG2 
2588 C CD1 . ILE A 353 ? 161.1443 161.1443 161.1443 0.0000 0.0000 0.0000 353 ILE A CD1 
2589 N N   . THR A 354 ? 161.3846 161.3846 161.3846 0.0000 0.0000 0.0000 354 THR A N   
2590 C CA  . THR A 354 ? 161.2955 161.2955 161.2955 0.0000 0.0000 0.0000 354 THR A CA  
2591 C C   . THR A 354 ? 161.3265 161.3265 161.3265 0.0000 0.0000 0.0000 354 THR A C   
2592 O O   . THR A 354 ? 161.6048 161.6048 161.6048 0.0000 0.0000 0.0000 354 THR A O   
2593 C CB  . THR A 354 ? 161.3127 161.3127 161.3127 0.0000 0.0000 0.0000 354 THR A CB  
2594 O OG1 . THR A 354 ? 161.3970 161.3970 161.3970 0.0000 0.0000 0.0000 354 THR A OG1 
2595 C CG2 . THR A 354 ? 161.4209 161.4209 161.4209 0.0000 0.0000 0.0000 354 THR A CG2 
2596 N N   . GLU A 355 ? 161.4204 161.4204 161.4204 0.0000 0.0000 0.0000 355 GLU A N   
2597 C CA  . GLU A 355 ? 161.4112 161.4112 161.4112 0.0000 0.0000 0.0000 355 GLU A CA  
2598 C C   . GLU A 355 ? 161.4377 161.4377 161.4377 0.0000 0.0000 0.0000 355 GLU A C   
2599 O O   . GLU A 355 ? 161.5800 161.5800 161.5800 0.0000 0.0000 0.0000 355 GLU A O   
2600 C CB  . GLU A 355 ? 161.4034 161.4034 161.4034 0.0000 0.0000 0.0000 355 GLU A CB  
2601 C CG  . GLU A 355 ? 161.4702 161.4702 161.4702 0.0000 0.0000 0.0000 355 GLU A CG  
2602 C CD  . GLU A 355 ? 161.3942 161.3942 161.3942 0.0000 0.0000 0.0000 355 GLU A CD  
2603 O OE1 . GLU A 355 ? 161.4172 161.4172 161.4172 0.0000 0.0000 0.0000 355 GLU A OE1 
2604 O OE2 . GLU A 355 ? 161.4673 161.4673 161.4673 0.0000 0.0000 0.0000 355 GLU A OE2 
2605 N N   . LYS A 356 ? 161.4086 161.4086 161.4086 0.0000 0.0000 0.0000 356 LYS A N   
2606 C CA  . LYS A 356 ? 161.3088 161.3088 161.3088 0.0000 0.0000 0.0000 356 LYS A CA  
2607 C C   . LYS A 356 ? 161.3312 161.3312 161.3312 0.0000 0.0000 0.0000 356 LYS A C   
2608 O O   . LYS A 356 ? 161.5847 161.5847 161.5847 0.0000 0.0000 0.0000 356 LYS A O   
2609 C CB  . LYS A 356 ? 160.8759 160.8759 160.8759 0.0000 0.0000 0.0000 356 LYS A CB  
2610 C CG  . LYS A 356 ? 160.0487 160.0487 160.0487 0.0000 0.0000 0.0000 356 LYS A CG  
2611 C CD  . LYS A 356 ? 160.1373 160.1373 160.1373 0.0000 0.0000 0.0000 356 LYS A CD  
2612 C CE  . LYS A 356 ? 159.2728 159.2728 159.2728 0.0000 0.0000 0.0000 356 LYS A CE  
2613 N NZ  . LYS A 356 ? 160.2332 160.2332 160.2332 0.0000 0.0000 0.0000 356 LYS A NZ  
2614 N N   . MET A 357 ? 161.3664 161.3664 161.3664 0.0000 0.0000 0.0000 357 MET A N   
2615 C CA  . MET A 357 ? 161.3154 161.3154 161.3154 0.0000 0.0000 0.0000 357 MET A CA  
2616 C C   . MET A 357 ? 161.3659 161.3659 161.3659 0.0000 0.0000 0.0000 357 MET A C   
2617 O O   . MET A 357 ? 161.6671 161.6671 161.6671 0.0000 0.0000 0.0000 357 MET A O   
2618 C CB  . MET A 357 ? 161.3804 161.3804 161.3804 0.0000 0.0000 0.0000 357 MET A CB  
2619 C CG  . MET A 357 ? 161.2974 161.2974 161.2974 0.0000 0.0000 0.0000 357 MET A CG  
2620 S SD  . MET A 357 ? 161.0916 161.0916 161.0916 0.0000 0.0000 0.0000 357 MET A SD  
2621 C CE  . MET A 357 ? 161.4015 161.4015 161.4015 0.0000 0.0000 0.0000 357 MET A CE  
2622 N N   . VAL A 358 ? 161.3370 161.3370 161.3370 0.0000 0.0000 0.0000 358 VAL A N   
2623 C CA  . VAL A 358 ? 161.1741 161.1741 161.1741 0.0000 0.0000 0.0000 358 VAL A CA  
2624 C C   . VAL A 358 ? 161.2974 161.2974 161.2974 0.0000 0.0000 0.0000 358 VAL A C   
2625 O O   . VAL A 358 ? 161.6579 161.6579 161.6579 0.0000 0.0000 0.0000 358 VAL A O   
2626 C CB  . VAL A 358 ? 161.2575 161.2575 161.2575 0.0000 0.0000 0.0000 358 VAL A CB  
2627 C CG1 . VAL A 358 ? 161.3633 161.3633 161.3633 0.0000 0.0000 0.0000 358 VAL A CG1 
2628 C CG2 . VAL A 358 ? 161.3746 161.3746 161.3746 0.0000 0.0000 0.0000 358 VAL A CG2 
2629 N N   . SER A 359 ? 161.3154 161.3154 161.3154 0.0000 0.0000 0.0000 359 SER A N   
2630 C CA  . SER A 359 ? 161.4009 161.4009 161.4009 0.0000 0.0000 0.0000 359 SER A CA  
2631 C C   . SER A 359 ? 161.4045 161.4045 161.4045 0.0000 0.0000 0.0000 359 SER A C   
2632 O O   . SER A 359 ? 161.5405 161.5405 161.5405 0.0000 0.0000 0.0000 359 SER A O   
2633 C CB  . SER A 359 ? 161.5209 161.5209 161.5209 0.0000 0.0000 0.0000 359 SER A CB  
2634 O OG  . SER A 359 ? 161.5970 161.5970 161.5970 0.0000 0.0000 0.0000 359 SER A OG  
2635 N N   . GLY A 360 ? 161.4545 161.4545 161.4545 0.0000 0.0000 0.0000 360 GLY A N   
2636 C CA  . GLY A 360 ? 161.4631 161.4631 161.4631 0.0000 0.0000 0.0000 360 GLY A CA  
2637 C C   . GLY A 360 ? 161.4759 161.4759 161.4759 0.0000 0.0000 0.0000 360 GLY A C   
2638 O O   . GLY A 360 ? 161.6824 161.6824 161.6824 0.0000 0.0000 0.0000 360 GLY A O   
2639 N N   . MET A 361 ? 161.4412 161.4412 161.4412 0.0000 0.0000 0.0000 361 MET A N   
2640 C CA  . MET A 361 ? 161.3434 161.3434 161.3434 0.0000 0.0000 0.0000 361 MET A CA  
2641 C C   . MET A 361 ? 161.4356 161.4356 161.4356 0.0000 0.0000 0.0000 361 MET A C   
2642 O O   . MET A 361 ? 161.7689 161.7689 161.7689 0.0000 0.0000 0.0000 361 MET A O   
2643 C CB  . MET A 361 ? 161.4410 161.4410 161.4410 0.0000 0.0000 0.0000 361 MET A CB  
2644 C CG  . MET A 361 ? 161.4626 161.4626 161.4626 0.0000 0.0000 0.0000 361 MET A CG  
2645 S SD  . MET A 361 ? 161.4436 161.4436 161.4436 0.0000 0.0000 0.0000 361 MET A SD  
2646 C CE  . MET A 361 ? 161.4484 161.4484 161.4484 0.0000 0.0000 0.0000 361 MET A CE  
2647 N N   . VAL A 362 ? 161.3509 161.3509 161.3509 0.0000 0.0000 0.0000 362 VAL A N   
2648 C CA  . VAL A 362 ? 161.2690 161.2690 161.2690 0.0000 0.0000 0.0000 362 VAL A CA  
2649 C C   . VAL A 362 ? 161.2570 161.2570 161.2570 0.0000 0.0000 0.0000 362 VAL A C   
2650 O O   . VAL A 362 ? 161.6011 161.6011 161.6011 0.0000 0.0000 0.0000 362 VAL A O   
2651 C CB  . VAL A 362 ? 161.3039 161.3039 161.3039 0.0000 0.0000 0.0000 362 VAL A CB  
2652 C CG1 . VAL A 362 ? 161.4963 161.4963 161.4963 0.0000 0.0000 0.0000 362 VAL A CG1 
2653 C CG2 . VAL A 362 ? 161.3833 161.3833 161.3833 0.0000 0.0000 0.0000 362 VAL A CG2 
2654 N N   . LYS A 363 ? 161.1318 161.1318 161.1318 0.0000 0.0000 0.0000 363 LYS A N   
2655 C CA  . LYS A 363 ? 161.2043 161.2043 161.2043 0.0000 0.0000 0.0000 363 LYS A CA  
2656 C C   . LYS A 363 ? 161.1553 161.1553 161.1553 0.0000 0.0000 0.0000 363 LYS A C   
2657 O O   . LYS A 363 ? 161.3658 161.3658 161.3658 0.0000 0.0000 0.0000 363 LYS A O   
2658 C CB  . LYS A 363 ? 161.5411 161.5411 161.5411 0.0000 0.0000 0.0000 363 LYS A CB  
2659 C CG  . LYS A 363 ? 161.5004 161.5004 161.5004 0.0000 0.0000 0.0000 363 LYS A CG  
2660 C CD  . LYS A 363 ? 161.5274 161.5274 161.5274 0.0000 0.0000 0.0000 363 LYS A CD  
2661 C CE  . LYS A 363 ? 161.4790 161.4790 161.4790 0.0000 0.0000 0.0000 363 LYS A CE  
2662 N NZ  . LYS A 363 ? 161.4974 161.4974 161.4974 0.0000 0.0000 0.0000 363 LYS A NZ  
2663 N N   . HIS A 364 ? 161.1259 161.1259 161.1259 0.0000 0.0000 0.0000 364 HIS A N   
2664 C CA  . HIS A 364 ? 161.1698 161.1698 161.1698 0.0000 0.0000 0.0000 364 HIS A CA  
2665 C C   . HIS A 364 ? 161.3914 161.3914 161.3914 0.0000 0.0000 0.0000 364 HIS A C   
2666 O O   . HIS A 364 ? 161.5394 161.5394 161.5394 0.0000 0.0000 0.0000 364 HIS A O   
2667 C CB  . HIS A 364 ? 161.3394 161.3394 161.3394 0.0000 0.0000 0.0000 364 HIS A CB  
2668 C CG  . HIS A 364 ? 161.2908 161.2908 161.2908 0.0000 0.0000 0.0000 364 HIS A CG  
2669 N ND1 . HIS A 364 ? 161.0597 161.0597 161.0597 0.0000 0.0000 0.0000 364 HIS A ND1 
2670 C CD2 . HIS A 364 ? 161.0748 161.0748 161.0748 0.0000 0.0000 0.0000 364 HIS A CD2 
2671 C CE1 . HIS A 364 ? 160.2723 160.2723 160.2723 0.0000 0.0000 0.0000 364 HIS A CE1 
2672 N NE2 . HIS A 364 ? 160.1176 160.1176 160.1176 0.0000 0.0000 0.0000 364 HIS A NE2 
2673 N N   . ILE A 365 ? 161.4977 161.4977 161.4977 0.0000 0.0000 0.0000 365 ILE A N   
2674 C CA  . ILE A 365 ? 161.2347 161.2347 161.2347 0.0000 0.0000 0.0000 365 ILE A CA  
2675 C C   . ILE A 365 ? 161.3157 161.3157 161.3157 0.0000 0.0000 0.0000 365 ILE A C   
2676 O O   . ILE A 365 ? 161.4681 161.4681 161.4681 0.0000 0.0000 0.0000 365 ILE A O   
2677 C CB  . ILE A 365 ? 161.1808 161.1808 161.1808 0.0000 0.0000 0.0000 365 ILE A CB  
2678 C CG1 . ILE A 365 ? 161.2895 161.2895 161.2895 0.0000 0.0000 0.0000 365 ILE A CG1 
2679 C CG2 . ILE A 365 ? 161.3441 161.3441 161.3441 0.0000 0.0000 0.0000 365 ILE A CG2 
2680 C CD1 . ILE A 365 ? 161.5253 161.5253 161.5253 0.0000 0.0000 0.0000 365 ILE A CD1 
2681 N N   . THR A 366 ? 161.3301 161.3301 161.3301 0.0000 0.0000 0.0000 366 THR A N   
2682 C CA  . THR A 366 ? 161.3302 161.3302 161.3302 0.0000 0.0000 0.0000 366 THR A CA  
2683 C C   . THR A 366 ? 161.3068 161.3068 161.3068 0.0000 0.0000 0.0000 366 THR A C   
2684 O O   . THR A 366 ? 161.3836 161.3836 161.3836 0.0000 0.0000 0.0000 366 THR A O   
2685 C CB  . THR A 366 ? 161.3866 161.3866 161.3866 0.0000 0.0000 0.0000 366 THR A CB  
2686 O OG1 . THR A 366 ? 161.4235 161.4235 161.4235 0.0000 0.0000 0.0000 366 THR A OG1 
2687 C CG2 . THR A 366 ? 161.5459 161.5459 161.5459 0.0000 0.0000 0.0000 366 THR A CG2 
2688 N N   . GLY A 367 ? 161.2822 161.2822 161.2822 0.0000 0.0000 0.0000 367 GLY A N   
2689 C CA  . GLY A 367 ? 161.3039 161.3039 161.3039 0.0000 0.0000 0.0000 367 GLY A CA  
2690 C C   . GLY A 367 ? 161.3045 161.3045 161.3045 0.0000 0.0000 0.0000 367 GLY A C   
2691 O O   . GLY A 367 ? 161.3545 161.3545 161.3545 0.0000 0.0000 0.0000 367 GLY A O   
2692 N N   . SER A 368 ? 161.3602 161.3602 161.3602 0.0000 0.0000 0.0000 368 SER A N   
2693 C CA  . SER A 368 ? 161.3944 161.3944 161.3944 0.0000 0.0000 0.0000 368 SER A CA  
2694 C C   . SER A 368 ? 161.4244 161.4244 161.4244 0.0000 0.0000 0.0000 368 SER A C   
2695 O O   . SER A 368 ? 161.5680 161.5680 161.5680 0.0000 0.0000 0.0000 368 SER A O   
2696 C CB  . SER A 368 ? 161.4882 161.4882 161.4882 0.0000 0.0000 0.0000 368 SER A CB  
2697 O OG  . SER A 368 ? 161.4880 161.4880 161.4880 0.0000 0.0000 0.0000 368 SER A OG  
2698 N N   . TYR A 369 ? 161.2941 161.2941 161.2941 0.0000 0.0000 0.0000 369 TYR A N   
2699 C CA  . TYR A 369 ? 161.2679 161.2679 161.2679 0.0000 0.0000 0.0000 369 TYR A CA  
2700 C C   . TYR A 369 ? 161.4210 161.4210 161.4210 0.0000 0.0000 0.0000 369 TYR A C   
2701 O O   . TYR A 369 ? 161.6766 161.6766 161.6766 0.0000 0.0000 0.0000 369 TYR A O   
2702 C CB  . TYR A 369 ? 161.3927 161.3927 161.3927 0.0000 0.0000 0.0000 369 TYR A CB  
2703 C CG  . TYR A 369 ? 161.2853 161.2853 161.2853 0.0000 0.0000 0.0000 369 TYR A CG  
2704 C CD1 . TYR A 369 ? 161.3001 161.3001 161.3001 0.0000 0.0000 0.0000 369 TYR A CD1 
2705 C CD2 . TYR A 369 ? 161.3747 161.3747 161.3747 0.0000 0.0000 0.0000 369 TYR A CD2 
2706 C CE1 . TYR A 369 ? 161.4057 161.4057 161.4057 0.0000 0.0000 0.0000 369 TYR A CE1 
2707 C CE2 . TYR A 369 ? 161.4387 161.4387 161.4387 0.0000 0.0000 0.0000 369 TYR A CE2 
2708 C CZ  . TYR A 369 ? 161.4836 161.4836 161.4836 0.0000 0.0000 0.0000 369 TYR A CZ  
2709 O OH  . TYR A 369 ? 161.6396 161.6396 161.6396 0.0000 0.0000 0.0000 369 TYR A OH  
2710 N N   . LYS A 370 ? 161.3657 161.3657 161.3657 0.0000 0.0000 0.0000 370 LYS A N   
2711 C CA  . LYS A 370 ? 161.3998 161.3998 161.3998 0.0000 0.0000 0.0000 370 LYS A CA  
2712 C C   . LYS A 370 ? 161.3733 161.3733 161.3733 0.0000 0.0000 0.0000 370 LYS A C   
2713 O O   . LYS A 370 ? 161.5215 161.5215 161.5215 0.0000 0.0000 0.0000 370 LYS A O   
2714 C CB  . LYS A 370 ? 161.3239 161.3239 161.3239 0.0000 0.0000 0.0000 370 LYS A CB  
2715 C CG  . LYS A 370 ? 161.4362 161.4362 161.4362 0.0000 0.0000 0.0000 370 LYS A CG  
2716 C CD  . LYS A 370 ? 161.4612 161.4612 161.4612 0.0000 0.0000 0.0000 370 LYS A CD  
2717 C CE  . LYS A 370 ? 161.4282 161.4282 161.4282 0.0000 0.0000 0.0000 370 LYS A CE  
2718 N NZ  . LYS A 370 ? 161.5528 161.5528 161.5528 0.0000 0.0000 0.0000 370 LYS A NZ  
2719 N N   . VAL A 371 ? 161.3864 161.3864 161.3864 0.0000 0.0000 0.0000 371 VAL A N   
2720 C CA  . VAL A 371 ? 161.3733 161.3733 161.3733 0.0000 0.0000 0.0000 371 VAL A CA  
2721 C C   . VAL A 371 ? 161.5685 161.5685 161.5685 0.0000 0.0000 0.0000 371 VAL A C   
2722 O O   . VAL A 371 ? 161.9570 161.9570 161.9570 0.0000 0.0000 0.0000 371 VAL A O   
2723 C CB  . VAL A 371 ? 161.3544 161.3544 161.3544 0.0000 0.0000 0.0000 371 VAL A CB  
2724 C CG1 . VAL A 371 ? 161.4444 161.4444 161.4444 0.0000 0.0000 0.0000 371 VAL A CG1 
2725 C CG2 . VAL A 371 ? 161.5459 161.5459 161.5459 0.0000 0.0000 0.0000 371 VAL A CG2 
2726 N N   . THR A 372 ? 161.3954 161.3954 161.3954 0.0000 0.0000 0.0000 372 THR A N   
2727 C CA  . THR A 372 ? 161.4234 161.4234 161.4234 0.0000 0.0000 0.0000 372 THR A CA  
2728 C C   . THR A 372 ? 161.3998 161.3998 161.3998 0.0000 0.0000 0.0000 372 THR A C   
2729 O O   . THR A 372 ? 161.5933 161.5933 161.5933 0.0000 0.0000 0.0000 372 THR A O   
2730 C CB  . THR A 372 ? 161.5211 161.5211 161.5211 0.0000 0.0000 0.0000 372 THR A CB  
2731 O OG1 . THR A 372 ? 161.5217 161.5217 161.5217 0.0000 0.0000 0.0000 372 THR A OG1 
2732 C CG2 . THR A 372 ? 161.6546 161.6546 161.6546 0.0000 0.0000 0.0000 372 THR A CG2 
2733 N N   . TYR A 373 ? 161.3285 161.3285 161.3285 0.0000 0.0000 0.0000 373 TYR A N   
2734 C CA  . TYR A 373 ? 161.2827 161.2827 161.2827 0.0000 0.0000 0.0000 373 TYR A CA  
2735 C C   . TYR A 373 ? 161.6342 161.6342 161.6342 0.0000 0.0000 0.0000 373 TYR A C   
2736 O O   . TYR A 373 ? 161.7602 161.7602 161.7602 0.0000 0.0000 0.0000 373 TYR A O   
2737 C CB  . TYR A 373 ? 161.2553 161.2553 161.2553 0.0000 0.0000 0.0000 373 TYR A CB  
2738 C CG  . TYR A 373 ? 161.3810 161.3810 161.3810 0.0000 0.0000 0.0000 373 TYR A CG  
2739 C CD1 . TYR A 373 ? 161.4959 161.4959 161.4959 0.0000 0.0000 0.0000 373 TYR A CD1 
2740 C CD2 . TYR A 373 ? 161.6466 161.6466 161.6466 0.0000 0.0000 0.0000 373 TYR A CD2 
2741 C CE1 . TYR A 373 ? 161.4904 161.4904 161.4904 0.0000 0.0000 0.0000 373 TYR A CE1 
2742 C CE2 . TYR A 373 ? 161.7308 161.7308 161.7308 0.0000 0.0000 0.0000 373 TYR A CE2 
2743 C CZ  . TYR A 373 ? 161.5247 161.5247 161.5247 0.0000 0.0000 0.0000 373 TYR A CZ  
2744 O OH  . TYR A 373 ? 161.4695 161.4695 161.4695 0.0000 0.0000 0.0000 373 TYR A OH  
2745 N N   . HIS A 374 ? 164.8977 164.8977 164.8977 0.0000 0.0000 0.0000 374 HIS A N   
2746 C CA  . HIS A 374 ? 165.2163 165.2163 165.2163 0.0000 0.0000 0.0000 374 HIS A CA  
2747 C C   . HIS A 374 ? 165.4087 165.4087 165.4087 0.0000 0.0000 0.0000 374 HIS A C   
2748 O O   . HIS A 374 ? 165.4668 165.4668 165.4668 0.0000 0.0000 0.0000 374 HIS A O   
2749 C CB  . HIS A 374 ? 165.4169 165.4169 165.4169 0.0000 0.0000 0.0000 374 HIS A CB  
2750 C CG  . HIS A 374 ? 165.2869 165.2869 165.2869 0.0000 0.0000 0.0000 374 HIS A CG  
2751 N ND1 . HIS A 374 ? 164.6945 164.6945 164.6945 0.0000 0.0000 0.0000 374 HIS A ND1 
2752 C CD2 . HIS A 374 ? 165.7018 165.7018 165.7018 0.0000 0.0000 0.0000 374 HIS A CD2 
2753 C CE1 . HIS A 374 ? 164.7231 164.7231 164.7231 0.0000 0.0000 0.0000 374 HIS A CE1 
2754 N NE2 . HIS A 374 ? 165.1632 165.1632 165.1632 0.0000 0.0000 0.0000 374 HIS A NE2 
2755 N N   . PRO A 375 ? 167.7044 167.7044 167.7044 0.0000 0.0000 0.0000 375 PRO A N   
2756 C CA  . PRO A 375 ? 167.9515 167.9515 167.9515 0.0000 0.0000 0.0000 375 PRO A CA  
2757 C C   . PRO A 375 ? 168.5375 168.5375 168.5375 0.0000 0.0000 0.0000 375 PRO A C   
2758 O O   . PRO A 375 ? 168.1217 168.1217 168.1217 0.0000 0.0000 0.0000 375 PRO A O   
2759 C CB  . PRO A 375 ? 167.8556 167.8556 167.8556 0.0000 0.0000 0.0000 375 PRO A CB  
2760 C CG  . PRO A 375 ? 167.9573 167.9573 167.9573 0.0000 0.0000 0.0000 375 PRO A CG  
2761 C CD  . PRO A 375 ? 167.7638 167.7638 167.7638 0.0000 0.0000 0.0000 375 PRO A CD  
2762 N N   . ASP A 376 ? 190.8904 190.8904 190.8904 0.0000 0.0000 0.0000 376 ASP A N   
2763 C CA  . ASP A 376 ? 191.4365 191.4365 191.4365 0.0000 0.0000 0.0000 376 ASP A CA  
2764 C C   . ASP A 376 ? 191.6442 191.6442 191.6442 0.0000 0.0000 0.0000 376 ASP A C   
2765 O O   . ASP A 376 ? 191.9810 191.9810 191.9810 0.0000 0.0000 0.0000 376 ASP A O   
2766 C CB  . ASP A 376 ? 192.0242 192.0242 192.0242 0.0000 0.0000 0.0000 376 ASP A CB  
2767 C CG  . ASP A 376 ? 191.9760 191.9760 191.9760 0.0000 0.0000 0.0000 376 ASP A CG  
2768 O OD1 . ASP A 376 ? 191.8327 191.8327 191.8327 0.0000 0.0000 0.0000 376 ASP A OD1 
2769 O OD2 . ASP A 376 ? 192.0835 192.0835 192.0835 0.0000 0.0000 0.0000 376 ASP A OD2 
2770 N N   . GLY A 377 ? 187.5389 187.5389 187.5389 0.0000 0.0000 0.0000 377 GLY A N   
2771 C CA  . GLY A 377 ? 188.0588 188.0588 188.0588 0.0000 0.0000 0.0000 377 GLY A CA  
2772 C C   . GLY A 377 ? 188.4581 188.4581 188.4581 0.0000 0.0000 0.0000 377 GLY A C   
2773 O O   . GLY A 377 ? 188.2274 188.2274 188.2274 0.0000 0.0000 0.0000 377 GLY A O   
2774 N N   . PRO A 378 ? 206.5798 206.5798 206.5798 0.0000 0.0000 0.0000 378 PRO A N   
2775 C CA  . PRO A 378 ? 206.8785 206.8785 206.8785 0.0000 0.0000 0.0000 378 PRO A CA  
2776 C C   . PRO A 378 ? 207.3119 207.3119 207.3119 0.0000 0.0000 0.0000 378 PRO A C   
2777 O O   . PRO A 378 ? 207.2569 207.2569 207.2569 0.0000 0.0000 0.0000 378 PRO A O   
2778 C CB  . PRO A 378 ? 207.1603 207.1603 207.1603 0.0000 0.0000 0.0000 378 PRO A CB  
2779 C CG  . PRO A 378 ? 207.1854 207.1854 207.1854 0.0000 0.0000 0.0000 378 PRO A CG  
2780 C CD  . PRO A 378 ? 207.0982 207.0982 207.0982 0.0000 0.0000 0.0000 378 PRO A CD  
2781 N N   . GLU A 379 ? 218.8652 218.8652 218.8652 0.0000 0.0000 0.0000 379 GLU A N   
2782 C CA  . GLU A 379 ? 219.2055 219.2055 219.2055 0.0000 0.0000 0.0000 379 GLU A CA  
2783 C C   . GLU A 379 ? 219.0412 219.0412 219.0412 0.0000 0.0000 0.0000 379 GLU A C   
2784 O O   . GLU A 379 ? 219.2994 219.2994 219.2994 0.0000 0.0000 0.0000 379 GLU A O   
2785 C CB  . GLU A 379 ? 219.5030 219.5030 219.5030 0.0000 0.0000 0.0000 379 GLU A CB  
2786 C CG  . GLU A 379 ? 219.6368 219.6368 219.6368 0.0000 0.0000 0.0000 379 GLU A CG  
2787 C CD  . GLU A 379 ? 219.3955 219.3955 219.3955 0.0000 0.0000 0.0000 379 GLU A CD  
2788 O OE1 . GLU A 379 ? 219.2507 219.2507 219.2507 0.0000 0.0000 0.0000 379 GLU A OE1 
2789 O OE2 . GLU A 379 ? 219.4450 219.4450 219.4450 0.0000 0.0000 0.0000 379 GLU A OE2 
2790 N N   . GLY A 380 ? 204.3311 204.3311 204.3311 0.0000 0.0000 0.0000 380 GLY A N   
2791 C CA  . GLY A 380 ? 203.9640 203.9640 203.9640 0.0000 0.0000 0.0000 380 GLY A CA  
2792 C C   . GLY A 380 ? 203.5318 203.5318 203.5318 0.0000 0.0000 0.0000 380 GLY A C   
2793 O O   . GLY A 380 ? 203.4228 203.4228 203.4228 0.0000 0.0000 0.0000 380 GLY A O   
2794 N N   . GLN A 381 ? 191.6790 191.6790 191.6790 0.0000 0.0000 0.0000 381 GLN A N   
2795 C CA  . GLN A 381 ? 191.2651 191.2651 191.2651 0.0000 0.0000 0.0000 381 GLN A CA  
2796 C C   . GLN A 381 ? 190.7471 190.7471 190.7471 0.0000 0.0000 0.0000 381 GLN A C   
2797 O O   . GLN A 381 ? 190.6028 190.6028 190.6028 0.0000 0.0000 0.0000 381 GLN A O   
2798 C CB  . GLN A 381 ? 191.2554 191.2554 191.2554 0.0000 0.0000 0.0000 381 GLN A CB  
2799 C CG  . GLN A 381 ? 191.0151 191.0151 191.0151 0.0000 0.0000 0.0000 381 GLN A CG  
2800 C CD  . GLN A 381 ? 191.2831 191.2831 191.2831 0.0000 0.0000 0.0000 381 GLN A CD  
2801 O OE1 . GLN A 381 ? 191.4709 191.4709 191.4709 0.0000 0.0000 0.0000 381 GLN A OE1 
2802 N NE2 . GLN A 381 ? 191.0979 191.0979 191.0979 0.0000 0.0000 0.0000 381 GLN A NE2 
2803 N N   . ALA A 382 ? 174.4183 174.4183 174.4183 0.0000 0.0000 0.0000 382 ALA A N   
2804 C CA  . ALA A 382 ? 173.7693 173.7693 173.7693 0.0000 0.0000 0.0000 382 ALA A CA  
2805 C C   . ALA A 382 ? 173.4808 173.4808 173.4808 0.0000 0.0000 0.0000 382 ALA A C   
2806 O O   . ALA A 382 ? 173.7207 173.7207 173.7207 0.0000 0.0000 0.0000 382 ALA A O   
2807 C CB  . ALA A 382 ? 173.7543 173.7543 173.7543 0.0000 0.0000 0.0000 382 ALA A CB  
2808 N N   . TYR A 383 ? 164.9358 164.9358 164.9358 0.0000 0.0000 0.0000 383 TYR A N   
2809 C CA  . TYR A 383 ? 164.7800 164.7800 164.7800 0.0000 0.0000 0.0000 383 TYR A CA  
2810 C C   . TYR A 383 ? 165.0212 165.0212 165.0212 0.0000 0.0000 0.0000 383 TYR A C   
2811 O O   . TYR A 383 ? 164.9564 164.9564 164.9564 0.0000 0.0000 0.0000 383 TYR A O   
2812 C CB  . TYR A 383 ? 164.6369 164.6369 164.6369 0.0000 0.0000 0.0000 383 TYR A CB  
2813 C CG  . TYR A 383 ? 164.5595 164.5595 164.5595 0.0000 0.0000 0.0000 383 TYR A CG  
2814 C CD1 . TYR A 383 ? 164.8466 164.8466 164.8466 0.0000 0.0000 0.0000 383 TYR A CD1 
2815 C CD2 . TYR A 383 ? 164.5043 164.5043 164.5043 0.0000 0.0000 0.0000 383 TYR A CD2 
2816 C CE1 . TYR A 383 ? 164.8763 164.8763 164.8763 0.0000 0.0000 0.0000 383 TYR A CE1 
2817 C CE2 . TYR A 383 ? 164.5863 164.5863 164.5863 0.0000 0.0000 0.0000 383 TYR A CE2 
2818 C CZ  . TYR A 383 ? 164.6831 164.6831 164.6831 0.0000 0.0000 0.0000 383 TYR A CZ  
2819 O OH  . TYR A 383 ? 164.7713 164.7713 164.7713 0.0000 0.0000 0.0000 383 TYR A OH  
2820 N N   . ASP A 384 ? 178.8050 178.8050 178.8050 0.0000 0.0000 0.0000 384 ASP A N   
2821 C CA  . ASP A 384 ? 178.8815 178.8815 178.8815 0.0000 0.0000 0.0000 384 ASP A CA  
2822 C C   . ASP A 384 ? 178.5964 178.5964 178.5964 0.0000 0.0000 0.0000 384 ASP A C   
2823 O O   . ASP A 384 ? 178.9284 178.9284 178.9284 0.0000 0.0000 0.0000 384 ASP A O   
2824 C CB  . ASP A 384 ? 179.3252 179.3252 179.3252 0.0000 0.0000 0.0000 384 ASP A CB  
2825 C CG  . ASP A 384 ? 179.4260 179.4260 179.4260 0.0000 0.0000 0.0000 384 ASP A CG  
2826 O OD1 . ASP A 384 ? 179.2979 179.2979 179.2979 0.0000 0.0000 0.0000 384 ASP A OD1 
2827 O OD2 . ASP A 384 ? 179.5645 179.5645 179.5645 0.0000 0.0000 0.0000 384 ASP A OD2 
2828 N N   . VAL A 385 ? 161.9575 161.9575 161.9575 0.0000 0.0000 0.0000 385 VAL A N   
2829 C CA  . VAL A 385 ? 161.5846 161.5846 161.5846 0.0000 0.0000 0.0000 385 VAL A CA  
2830 C C   . VAL A 385 ? 161.4581 161.4581 161.4581 0.0000 0.0000 0.0000 385 VAL A C   
2831 O O   . VAL A 385 ? 161.6471 161.6471 161.6471 0.0000 0.0000 0.0000 385 VAL A O   
2832 C CB  . VAL A 385 ? 161.4721 161.4721 161.4721 0.0000 0.0000 0.0000 385 VAL A CB  
2833 C CG1 . VAL A 385 ? 161.7223 161.7223 161.7223 0.0000 0.0000 0.0000 385 VAL A CG1 
2834 C CG2 . VAL A 385 ? 161.5917 161.5917 161.5917 0.0000 0.0000 0.0000 385 VAL A CG2 
2835 N N   . ASP A 386 ? 161.3380 161.3380 161.3380 0.0000 0.0000 0.0000 386 ASP A N   
2836 C CA  . ASP A 386 ? 161.2542 161.2542 161.2542 0.0000 0.0000 0.0000 386 ASP A CA  
2837 C C   . ASP A 386 ? 161.2787 161.2787 161.2787 0.0000 0.0000 0.0000 386 ASP A C   
2838 O O   . ASP A 386 ? 161.4725 161.4725 161.4725 0.0000 0.0000 0.0000 386 ASP A O   
2839 C CB  . ASP A 386 ? 161.4947 161.4947 161.4947 0.0000 0.0000 0.0000 386 ASP A CB  
2840 C CG  . ASP A 386 ? 161.4917 161.4917 161.4917 0.0000 0.0000 0.0000 386 ASP A CG  
2841 O OD1 . ASP A 386 ? 161.4474 161.4474 161.4474 0.0000 0.0000 0.0000 386 ASP A OD1 
2842 O OD2 . ASP A 386 ? 161.5295 161.5295 161.5295 0.0000 0.0000 0.0000 386 ASP A OD2 
2843 N N   . PHE A 387 ? 161.2787 161.2787 161.2787 0.0000 0.0000 0.0000 387 PHE A N   
2844 C CA  . PHE A 387 ? 161.2781 161.2781 161.2781 0.0000 0.0000 0.0000 387 PHE A CA  
2845 C C   . PHE A 387 ? 161.4401 161.4401 161.4401 0.0000 0.0000 0.0000 387 PHE A C   
2846 O O   . PHE A 387 ? 161.4912 161.4912 161.4912 0.0000 0.0000 0.0000 387 PHE A O   
2847 C CB  . PHE A 387 ? 161.3718 161.3718 161.3718 0.0000 0.0000 0.0000 387 PHE A CB  
2848 C CG  . PHE A 387 ? 161.3475 161.3475 161.3475 0.0000 0.0000 0.0000 387 PHE A CG  
2849 C CD1 . PHE A 387 ? 161.5243 161.5243 161.5243 0.0000 0.0000 0.0000 387 PHE A CD1 
2850 C CD2 . PHE A 387 ? 161.4320 161.4320 161.4320 0.0000 0.0000 0.0000 387 PHE A CD2 
2851 C CE1 . PHE A 387 ? 161.4408 161.4408 161.4408 0.0000 0.0000 0.0000 387 PHE A CE1 
2852 C CE2 . PHE A 387 ? 161.3848 161.3848 161.3848 0.0000 0.0000 0.0000 387 PHE A CE2 
2853 C CZ  . PHE A 387 ? 161.2627 161.2627 161.2627 0.0000 0.0000 0.0000 387 PHE A CZ  
2854 N N   . THR A 388 ? 161.4250 161.4250 161.4250 0.0000 0.0000 0.0000 388 THR A N   
2855 C CA  . THR A 388 ? 161.2364 161.2364 161.2364 0.0000 0.0000 0.0000 388 THR A CA  
2856 C C   . THR A 388 ? 161.2645 161.2645 161.2645 0.0000 0.0000 0.0000 388 THR A C   
2857 O O   . THR A 388 ? 161.5311 161.5311 161.5311 0.0000 0.0000 0.0000 388 THR A O   
2858 C CB  . THR A 388 ? 161.2914 161.2914 161.2914 0.0000 0.0000 0.0000 388 THR A CB  
2859 O OG1 . THR A 388 ? 161.4716 161.4716 161.4716 0.0000 0.0000 0.0000 388 THR A OG1 
2860 C CG2 . THR A 388 ? 161.2888 161.2888 161.2888 0.0000 0.0000 0.0000 388 THR A CG2 
2861 N N   . PRO A 389 ? 161.1754 161.1754 161.1754 0.0000 0.0000 0.0000 389 PRO A N   
2862 C CA  . PRO A 389 ? 161.3425 161.3425 161.3425 0.0000 0.0000 0.0000 389 PRO A CA  
2863 C C   . PRO A 389 ? 161.3910 161.3910 161.3910 0.0000 0.0000 0.0000 389 PRO A C   
2864 O O   . PRO A 389 ? 161.6517 161.6517 161.6517 0.0000 0.0000 0.0000 389 PRO A O   
2865 C CB  . PRO A 389 ? 161.4784 161.4784 161.4784 0.0000 0.0000 0.0000 389 PRO A CB  
2866 C CG  . PRO A 389 ? 161.5861 161.5861 161.5861 0.0000 0.0000 0.0000 389 PRO A CG  
2867 C CD  . PRO A 389 ? 161.4616 161.4616 161.4616 0.0000 0.0000 0.0000 389 PRO A CD  
2868 N N   . PRO A 390 ? 161.2310 161.2310 161.2310 0.0000 0.0000 0.0000 390 PRO A N   
2869 C CA  . PRO A 390 ? 161.2602 161.2602 161.2602 0.0000 0.0000 0.0000 390 PRO A CA  
2870 C C   . PRO A 390 ? 161.3192 161.3192 161.3192 0.0000 0.0000 0.0000 390 PRO A C   
2871 O O   . PRO A 390 ? 161.3945 161.3945 161.3945 0.0000 0.0000 0.0000 390 PRO A O   
2872 C CB  . PRO A 390 ? 161.2720 161.2720 161.2720 0.0000 0.0000 0.0000 390 PRO A CB  
2873 C CG  . PRO A 390 ? 161.3790 161.3790 161.3790 0.0000 0.0000 0.0000 390 PRO A CG  
2874 C CD  . PRO A 390 ? 161.3899 161.3899 161.3899 0.0000 0.0000 0.0000 390 PRO A CD  
2875 N N   . PHE A 391 ? 161.3644 161.3644 161.3644 0.0000 0.0000 0.0000 391 PHE A N   
2876 C CA  . PHE A 391 ? 161.3199 161.3199 161.3199 0.0000 0.0000 0.0000 391 PHE A CA  
2877 C C   . PHE A 391 ? 161.3777 161.3777 161.3777 0.0000 0.0000 0.0000 391 PHE A C   
2878 O O   . PHE A 391 ? 161.4483 161.4483 161.4483 0.0000 0.0000 0.0000 391 PHE A O   
2879 C CB  . PHE A 391 ? 161.3230 161.3230 161.3230 0.0000 0.0000 0.0000 391 PHE A CB  
2880 C CG  . PHE A 391 ? 161.3761 161.3761 161.3761 0.0000 0.0000 0.0000 391 PHE A CG  
2881 C CD1 . PHE A 391 ? 161.4500 161.4500 161.4500 0.0000 0.0000 0.0000 391 PHE A CD1 
2882 C CD2 . PHE A 391 ? 161.4972 161.4972 161.4972 0.0000 0.0000 0.0000 391 PHE A CD2 
2883 C CE1 . PHE A 391 ? 161.4544 161.4544 161.4544 0.0000 0.0000 0.0000 391 PHE A CE1 
2884 C CE2 . PHE A 391 ? 161.4166 161.4166 161.4166 0.0000 0.0000 0.0000 391 PHE A CE2 
2885 C CZ  . PHE A 391 ? 161.3808 161.3808 161.3808 0.0000 0.0000 0.0000 391 PHE A CZ  
2886 N N   . ARG A 392 ? 161.3712 161.3712 161.3712 0.0000 0.0000 0.0000 392 ARG A N   
2887 C CA  . ARG A 392 ? 161.2842 161.2842 161.2842 0.0000 0.0000 0.0000 392 ARG A CA  
2888 C C   . ARG A 392 ? 161.3223 161.3223 161.3223 0.0000 0.0000 0.0000 392 ARG A C   
2889 O O   . ARG A 392 ? 161.5343 161.5343 161.5343 0.0000 0.0000 0.0000 392 ARG A O   
2890 C CB  . ARG A 392 ? 161.3502 161.3502 161.3502 0.0000 0.0000 0.0000 392 ARG A CB  
2891 C CG  . ARG A 392 ? 161.3682 161.3682 161.3682 0.0000 0.0000 0.0000 392 ARG A CG  
2892 C CD  . ARG A 392 ? 161.3622 161.3622 161.3622 0.0000 0.0000 0.0000 392 ARG A CD  
2893 N NE  . ARG A 392 ? 161.3574 161.3574 161.3574 0.0000 0.0000 0.0000 392 ARG A NE  
2894 C CZ  . ARG A 392 ? 161.4545 161.4545 161.4545 0.0000 0.0000 0.0000 392 ARG A CZ  
2895 N NH1 . ARG A 392 ? 161.4184 161.4184 161.4184 0.0000 0.0000 0.0000 392 ARG A NH1 
2896 N NH2 . ARG A 392 ? 161.6510 161.6510 161.6510 0.0000 0.0000 0.0000 392 ARG A NH2 
2897 N N   . ARG A 393 ? 161.2369 161.2369 161.2369 0.0000 0.0000 0.0000 393 ARG A N   
2898 C CA  . ARG A 393 ? 161.3269 161.3269 161.3269 0.0000 0.0000 0.0000 393 ARG A CA  
2899 C C   . ARG A 393 ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 393 ARG A C   
2900 O O   . ARG A 393 ? 161.4142 161.4142 161.4142 0.0000 0.0000 0.0000 393 ARG A O   
2901 C CB  . ARG A 393 ? 161.3327 161.3327 161.3327 0.0000 0.0000 0.0000 393 ARG A CB  
2902 C CG  . ARG A 393 ? 161.3034 161.3034 161.3034 0.0000 0.0000 0.0000 393 ARG A CG  
2903 C CD  . ARG A 393 ? 161.3367 161.3367 161.3367 0.0000 0.0000 0.0000 393 ARG A CD  
2904 N NE  . ARG A 393 ? 161.3022 161.3022 161.3022 0.0000 0.0000 0.0000 393 ARG A NE  
2905 C CZ  . ARG A 393 ? 161.3669 161.3669 161.3669 0.0000 0.0000 0.0000 393 ARG A CZ  
2906 N NH1 . ARG A 393 ? 161.4673 161.4673 161.4673 0.0000 0.0000 0.0000 393 ARG A NH1 
2907 N NH2 . ARG A 393 ? 161.4589 161.4589 161.4589 0.0000 0.0000 0.0000 393 ARG A NH2 
2908 N N   . ILE A 394 ? 161.3336 161.3336 161.3336 0.0000 0.0000 0.0000 394 ILE A N   
2909 C CA  . ILE A 394 ? 161.6418 161.6418 161.6418 0.0000 0.0000 0.0000 394 ILE A CA  
2910 C C   . ILE A 394 ? 162.1389 162.1389 162.1389 0.0000 0.0000 0.0000 394 ILE A C   
2911 O O   . ILE A 394 ? 162.1536 162.1536 162.1536 0.0000 0.0000 0.0000 394 ILE A O   
2912 C CB  . ILE A 394 ? 161.8219 161.8219 161.8219 0.0000 0.0000 0.0000 394 ILE A CB  
2913 C CG1 . ILE A 394 ? 161.6855 161.6855 161.6855 0.0000 0.0000 0.0000 394 ILE A CG1 
2914 C CG2 . ILE A 394 ? 161.8513 161.8513 161.8513 0.0000 0.0000 0.0000 394 ILE A CG2 
2915 C CD1 . ILE A 394 ? 161.7194 161.7194 161.7194 0.0000 0.0000 0.0000 394 ILE A CD1 
2916 N N   . ASN A 395 ? 178.8623 178.8623 178.8623 0.0000 0.0000 0.0000 395 ASN A N   
2917 C CA  . ASN A 395 ? 179.3113 179.3113 179.3113 0.0000 0.0000 0.0000 395 ASN A CA  
2918 C C   . ASN A 395 ? 179.8499 179.8499 179.8499 0.0000 0.0000 0.0000 395 ASN A C   
2919 O O   . ASN A 395 ? 180.4156 180.4156 180.4156 0.0000 0.0000 0.0000 395 ASN A O   
2920 C CB  . ASN A 395 ? 179.8941 179.8941 179.8941 0.0000 0.0000 0.0000 395 ASN A CB  
2921 C CG  . ASN A 395 ? 179.5862 179.5862 179.5862 0.0000 0.0000 0.0000 395 ASN A CG  
2922 O OD1 . ASN A 395 ? 179.2516 179.2516 179.2516 0.0000 0.0000 0.0000 395 ASN A OD1 
2923 N ND2 . ASN A 395 ? 179.7569 179.7569 179.7569 0.0000 0.0000 0.0000 395 ASN A ND2 
2924 N N   . MET A 396 ? 185.2195 185.2195 185.2195 0.0000 0.0000 0.0000 396 MET A N   
2925 C CA  . MET A 396 ? 185.5999 185.5999 185.5999 0.0000 0.0000 0.0000 396 MET A CA  
2926 C C   . MET A 396 ? 186.3776 186.3776 186.3776 0.0000 0.0000 0.0000 396 MET A C   
2927 O O   . MET A 396 ? 186.5861 186.5861 186.5861 0.0000 0.0000 0.0000 396 MET A O   
2928 C CB  . MET A 396 ? 185.4934 185.4934 185.4934 0.0000 0.0000 0.0000 396 MET A CB  
2929 C CG  . MET A 396 ? 185.5905 185.5905 185.5905 0.0000 0.0000 0.0000 396 MET A CG  
2930 S SD  . MET A 396 ? 185.2832 185.2832 185.2832 0.0000 0.0000 0.0000 396 MET A SD  
2931 C CE  . MET A 396 ? 185.0386 185.0386 185.0386 0.0000 0.0000 0.0000 396 MET A CE  
2932 N N   . VAL A 397 ? 200.6609 200.6609 200.6609 0.0000 0.0000 0.0000 397 VAL A N   
2933 C CA  . VAL A 397 ? 201.1885 201.1885 201.1885 0.0000 0.0000 0.0000 397 VAL A CA  
2934 C C   . VAL A 397 ? 201.7978 201.7978 201.7978 0.0000 0.0000 0.0000 397 VAL A C   
2935 O O   . VAL A 397 ? 202.0415 202.0415 202.0415 0.0000 0.0000 0.0000 397 VAL A O   
2936 C CB  . VAL A 397 ? 201.4845 201.4845 201.4845 0.0000 0.0000 0.0000 397 VAL A CB  
2937 C CG1 . VAL A 397 ? 201.8196 201.8196 201.8196 0.0000 0.0000 0.0000 397 VAL A CG1 
2938 C CG2 . VAL A 397 ? 201.2243 201.2243 201.2243 0.0000 0.0000 0.0000 397 VAL A CG2 
2939 N N   . GLU A 398 ? 211.3855 211.3855 211.3855 0.0000 0.0000 0.0000 398 GLU A N   
2940 C CA  . GLU A 398 ? 211.8265 211.8265 211.8265 0.0000 0.0000 0.0000 398 GLU A CA  
2941 C C   . GLU A 398 ? 211.7174 211.7174 211.7174 0.0000 0.0000 0.0000 398 GLU A C   
2942 O O   . GLU A 398 ? 212.0748 212.0748 212.0748 0.0000 0.0000 0.0000 398 GLU A O   
2943 C CB  . GLU A 398 ? 211.9570 211.9570 211.9570 0.0000 0.0000 0.0000 398 GLU A CB  
2944 C CG  . GLU A 398 ? 212.0508 212.0508 212.0508 0.0000 0.0000 0.0000 398 GLU A CG  
2945 C CD  . GLU A 398 ? 211.8063 211.8063 211.8063 0.0000 0.0000 0.0000 398 GLU A CD  
2946 O OE1 . GLU A 398 ? 211.5982 211.5982 211.5982 0.0000 0.0000 0.0000 398 GLU A OE1 
2947 O OE2 . GLU A 398 ? 211.8910 211.8910 211.8910 0.0000 0.0000 0.0000 398 GLU A OE2 
2948 N N   . GLU A 399 ? 205.9301 205.9301 205.9301 0.0000 0.0000 0.0000 399 GLU A N   
2949 C CA  . GLU A 399 ? 205.8904 205.8904 205.8904 0.0000 0.0000 0.0000 399 GLU A CA  
2950 C C   . GLU A 399 ? 205.8235 205.8235 205.8235 0.0000 0.0000 0.0000 399 GLU A C   
2951 O O   . GLU A 399 ? 206.1247 206.1247 206.1247 0.0000 0.0000 0.0000 399 GLU A O   
2952 C CB  . GLU A 399 ? 205.5518 205.5518 205.5518 0.0000 0.0000 0.0000 399 GLU A CB  
2953 C CG  . GLU A 399 ? 205.4009 205.4009 205.4009 0.0000 0.0000 0.0000 399 GLU A CG  
2954 C CD  . GLU A 399 ? 205.8835 205.8835 205.8835 0.0000 0.0000 0.0000 399 GLU A CD  
2955 O OE1 . GLU A 399 ? 205.8647 205.8647 205.8647 0.0000 0.0000 0.0000 399 GLU A OE1 
2956 O OE2 . GLU A 399 ? 206.0833 206.0833 206.0833 0.0000 0.0000 0.0000 399 GLU A OE2 
2957 N N   . LEU A 400 ? 200.5041 200.5041 200.5041 0.0000 0.0000 0.0000 400 LEU A N   
2958 C CA  . LEU A 400 ? 200.4952 200.4952 200.4952 0.0000 0.0000 0.0000 400 LEU A CA  
2959 C C   . LEU A 400 ? 201.2526 201.2526 201.2526 0.0000 0.0000 0.0000 400 LEU A C   
2960 O O   . LEU A 400 ? 201.2602 201.2602 201.2602 0.0000 0.0000 0.0000 400 LEU A O   
2961 C CB  . LEU A 400 ? 200.2850 200.2850 200.2850 0.0000 0.0000 0.0000 400 LEU A CB  
2962 C CG  . LEU A 400 ? 200.2555 200.2555 200.2555 0.0000 0.0000 0.0000 400 LEU A CG  
2963 C CD1 . LEU A 400 ? 200.0698 200.0698 200.0698 0.0000 0.0000 0.0000 400 LEU A CD1 
2964 C CD2 . LEU A 400 ? 200.2248 200.2248 200.2248 0.0000 0.0000 0.0000 400 LEU A CD2 
2965 N N   . GLU A 401 ? 222.5994 222.5994 222.5994 0.0000 0.0000 0.0000 401 GLU A N   
2966 C CA  . GLU A 401 ? 223.2638 223.2638 223.2638 0.0000 0.0000 0.0000 401 GLU A CA  
2967 C C   . GLU A 401 ? 223.0881 223.0881 223.0881 0.0000 0.0000 0.0000 401 GLU A C   
2968 O O   . GLU A 401 ? 223.5584 223.5584 223.5584 0.0000 0.0000 0.0000 401 GLU A O   
2969 C CB  . GLU A 401 ? 223.5789 223.5789 223.5789 0.0000 0.0000 0.0000 401 GLU A CB  
2970 C CG  . GLU A 401 ? 223.8420 223.8420 223.8420 0.0000 0.0000 0.0000 401 GLU A CG  
2971 C CD  . GLU A 401 ? 223.9590 223.9590 223.9590 0.0000 0.0000 0.0000 401 GLU A CD  
2972 O OE1 . GLU A 401 ? 223.8769 223.8769 223.8769 0.0000 0.0000 0.0000 401 GLU A OE1 
2973 O OE2 . GLU A 401 ? 224.1407 224.1407 224.1407 0.0000 0.0000 0.0000 401 GLU A OE2 
2974 N N   . LYS A 402 ? 210.2626 210.2626 210.2626 0.0000 0.0000 0.0000 402 LYS A N   
2975 C CA  . LYS A 402 ? 210.0982 210.0982 210.0982 0.0000 0.0000 0.0000 402 LYS A CA  
2976 C C   . LYS A 402 ? 210.0890 210.0890 210.0890 0.0000 0.0000 0.0000 402 LYS A C   
2977 O O   . LYS A 402 ? 210.1220 210.1220 210.1220 0.0000 0.0000 0.0000 402 LYS A O   
2978 C CB  . LYS A 402 ? 210.0098 210.0098 210.0098 0.0000 0.0000 0.0000 402 LYS A CB  
2979 C CG  . LYS A 402 ? 209.9533 209.9533 209.9533 0.0000 0.0000 0.0000 402 LYS A CG  
2980 C CD  . LYS A 402 ? 209.8980 209.8980 209.8980 0.0000 0.0000 0.0000 402 LYS A CD  
2981 C CE  . LYS A 402 ? 209.8688 209.8688 209.8688 0.0000 0.0000 0.0000 402 LYS A CE  
2982 N NZ  . LYS A 402 ? 209.8634 209.8634 209.8634 0.0000 0.0000 0.0000 402 LYS A NZ  
2983 N N   . ALA A 403 ? 209.4530 209.4530 209.4530 0.0000 0.0000 0.0000 403 ALA A N   
2984 C CA  . ALA A 403 ? 209.4705 209.4705 209.4705 0.0000 0.0000 0.0000 403 ALA A CA  
2985 C C   . ALA A 403 ? 209.6792 209.6792 209.6792 0.0000 0.0000 0.0000 403 ALA A C   
2986 O O   . ALA A 403 ? 209.6581 209.6581 209.6581 0.0000 0.0000 0.0000 403 ALA A O   
2987 C CB  . ALA A 403 ? 209.2667 209.2667 209.2667 0.0000 0.0000 0.0000 403 ALA A CB  
2988 N N   . LEU A 404 ? 217.1452 217.1452 217.1452 0.0000 0.0000 0.0000 404 LEU A N   
2989 C CA  . LEU A 404 ? 217.5177 217.5177 217.5177 0.0000 0.0000 0.0000 404 LEU A CA  
2990 C C   . LEU A 404 ? 218.1081 218.1081 218.1081 0.0000 0.0000 0.0000 404 LEU A C   
2991 O O   . LEU A 404 ? 218.0926 218.0926 218.0926 0.0000 0.0000 0.0000 404 LEU A O   
2992 C CB  . LEU A 404 ? 217.7156 217.7156 217.7156 0.0000 0.0000 0.0000 404 LEU A CB  
2993 C CG  . LEU A 404 ? 217.2787 217.2787 217.2787 0.0000 0.0000 0.0000 404 LEU A CG  
2994 C CD1 . LEU A 404 ? 217.4192 217.4192 217.4192 0.0000 0.0000 0.0000 404 LEU A CD1 
2995 C CD2 . LEU A 404 ? 217.4655 217.4655 217.4655 0.0000 0.0000 0.0000 404 LEU A CD2 
2996 N N   . GLY A 405 ? 240.3718 240.3718 240.3718 0.0000 0.0000 0.0000 405 GLY A N   
2997 C CA  . GLY A 405 ? 241.0952 241.0952 241.0952 0.0000 0.0000 0.0000 405 GLY A CA  
2998 C C   . GLY A 405 ? 241.5860 241.5860 241.5860 0.0000 0.0000 0.0000 405 GLY A C   
2999 O O   . GLY A 405 ? 241.5859 241.5859 241.5859 0.0000 0.0000 0.0000 405 GLY A O   
3000 N N   . MET A 406 ? 255.6151 255.6151 255.6151 0.0000 0.0000 0.0000 406 MET A N   
3001 C CA  . MET A 406 ? 255.9834 255.9834 255.9834 0.0000 0.0000 0.0000 406 MET A CA  
3002 C C   . MET A 406 ? 255.9361 255.9361 255.9361 0.0000 0.0000 0.0000 406 MET A C   
3003 O O   . MET A 406 ? 255.7450 255.7450 255.7450 0.0000 0.0000 0.0000 406 MET A O   
3004 C CB  . MET A 406 ? 256.0910 256.0910 256.0910 0.0000 0.0000 0.0000 406 MET A CB  
3005 C CG  . MET A 406 ? 256.0841 256.0841 256.0841 0.0000 0.0000 0.0000 406 MET A CG  
3006 S SD  . MET A 406 ? 256.1221 256.1221 256.1221 0.0000 0.0000 0.0000 406 MET A SD  
3007 C CE  . MET A 406 ? 256.2048 256.2048 256.2048 0.0000 0.0000 0.0000 406 MET A CE  
3008 N N   . LYS A 407 ? 250.5892 250.5892 250.5892 0.0000 0.0000 0.0000 407 LYS A N   
3009 C CA  . LYS A 407 ? 250.3413 250.3413 250.3413 0.0000 0.0000 0.0000 407 LYS A CA  
3010 C C   . LYS A 407 ? 250.2219 250.2219 250.2219 0.0000 0.0000 0.0000 407 LYS A C   
3011 O O   . LYS A 407 ? 250.3992 250.3992 250.3992 0.0000 0.0000 0.0000 407 LYS A O   
3012 C CB  . LYS A 407 ? 250.4740 250.4740 250.4740 0.0000 0.0000 0.0000 407 LYS A CB  
3013 C CG  . LYS A 407 ? 250.5192 250.5192 250.5192 0.0000 0.0000 0.0000 407 LYS A CG  
3014 C CD  . LYS A 407 ? 250.3051 250.3051 250.3051 0.0000 0.0000 0.0000 407 LYS A CD  
3015 C CE  . LYS A 407 ? 250.3158 250.3158 250.3158 0.0000 0.0000 0.0000 407 LYS A CE  
3016 N NZ  . LYS A 407 ? 250.4782 250.4782 250.4782 0.0000 0.0000 0.0000 407 LYS A NZ  
3017 N N   . LEU A 408 ? 242.2794 242.2794 242.2794 0.0000 0.0000 0.0000 408 LEU A N   
3018 C CA  . LEU A 408 ? 242.2242 242.2242 242.2242 0.0000 0.0000 0.0000 408 LEU A CA  
3019 C C   . LEU A 408 ? 242.2337 242.2337 242.2337 0.0000 0.0000 0.0000 408 LEU A C   
3020 O O   . LEU A 408 ? 242.2016 242.2016 242.2016 0.0000 0.0000 0.0000 408 LEU A O   
3021 C CB  . LEU A 408 ? 242.1066 242.1066 242.1066 0.0000 0.0000 0.0000 408 LEU A CB  
3022 C CG  . LEU A 408 ? 242.1016 242.1016 242.1016 0.0000 0.0000 0.0000 408 LEU A CG  
3023 C CD1 . LEU A 408 ? 242.2028 242.2028 242.2028 0.0000 0.0000 0.0000 408 LEU A CD1 
3024 C CD2 . LEU A 408 ? 241.9766 241.9766 241.9766 0.0000 0.0000 0.0000 408 LEU A CD2 
3025 N N   . PRO A 409 ? 246.8940 246.8940 246.8940 0.0000 0.0000 0.0000 409 PRO A N   
3026 C CA  . PRO A 409 ? 246.9984 246.9984 246.9984 0.0000 0.0000 0.0000 409 PRO A CA  
3027 C C   . PRO A 409 ? 246.9797 246.9797 246.9797 0.0000 0.0000 0.0000 409 PRO A C   
3028 O O   . PRO A 409 ? 246.9134 246.9134 246.9134 0.0000 0.0000 0.0000 409 PRO A O   
3029 C CB  . PRO A 409 ? 247.0753 247.0753 247.0753 0.0000 0.0000 0.0000 409 PRO A CB  
3030 C CG  . PRO A 409 ? 247.1238 247.1238 247.1238 0.0000 0.0000 0.0000 409 PRO A CG  
3031 C CD  . PRO A 409 ? 247.0121 247.0121 247.0121 0.0000 0.0000 0.0000 409 PRO A CD  
3032 N N   . GLU A 410 ? 245.8544 245.8544 245.8544 0.0000 0.0000 0.0000 410 GLU A N   
3033 C CA  . GLU A 410 ? 245.6998 245.6998 245.6998 0.0000 0.0000 0.0000 410 GLU A CA  
3034 C C   . GLU A 410 ? 245.4413 245.4413 245.4413 0.0000 0.0000 0.0000 410 GLU A C   
3035 O O   . GLU A 410 ? 245.6012 245.6012 245.6012 0.0000 0.0000 0.0000 410 GLU A O   
3036 C CB  . GLU A 410 ? 245.7764 245.7764 245.7764 0.0000 0.0000 0.0000 410 GLU A CB  
3037 C CG  . GLU A 410 ? 245.8580 245.8580 245.8580 0.0000 0.0000 0.0000 410 GLU A CG  
3038 C CD  . GLU A 410 ? 245.8961 245.8961 245.8961 0.0000 0.0000 0.0000 410 GLU A CD  
3039 O OE1 . GLU A 410 ? 245.9276 245.9276 245.9276 0.0000 0.0000 0.0000 410 GLU A OE1 
3040 O OE2 . GLU A 410 ? 245.9410 245.9410 245.9410 0.0000 0.0000 0.0000 410 GLU A OE2 
3041 N N   . THR A 411 ? 228.6111 228.6111 228.6111 0.0000 0.0000 0.0000 411 THR A N   
3042 C CA  . THR A 411 ? 228.3088 228.3088 228.3088 0.0000 0.0000 0.0000 411 THR A CA  
3043 C C   . THR A 411 ? 228.0986 228.0986 228.0986 0.0000 0.0000 0.0000 411 THR A C   
3044 O O   . THR A 411 ? 227.8734 227.8734 227.8734 0.0000 0.0000 0.0000 411 THR A O   
3045 C CB  . THR A 411 ? 227.2516 227.2516 227.2516 0.0000 0.0000 0.0000 411 THR A CB  
3046 O OG1 . THR A 411 ? 227.4432 227.4432 227.4432 0.0000 0.0000 0.0000 411 THR A OG1 
3047 C CG2 . THR A 411 ? 227.5095 227.5095 227.5095 0.0000 0.0000 0.0000 411 THR A CG2 
3048 N N   . ASN A 412 ? 238.3472 238.3472 238.3472 0.0000 0.0000 0.0000 412 ASN A N   
3049 C CA  . ASN A 412 ? 238.5779 238.5779 238.5779 0.0000 0.0000 0.0000 412 ASN A CA  
3050 C C   . ASN A 412 ? 238.9696 238.9696 238.9696 0.0000 0.0000 0.0000 412 ASN A C   
3051 O O   . ASN A 412 ? 239.0135 239.0135 239.0135 0.0000 0.0000 0.0000 412 ASN A O   
3052 C CB  . ASN A 412 ? 238.6398 238.6398 238.6398 0.0000 0.0000 0.0000 412 ASN A CB  
3053 C CG  . ASN A 412 ? 238.7174 238.7174 238.7174 0.0000 0.0000 0.0000 412 ASN A CG  
3054 O OD1 . ASN A 412 ? 238.7965 238.7965 238.7965 0.0000 0.0000 0.0000 412 ASN A OD1 
3055 N ND2 . ASN A 412 ? 238.7286 238.7286 238.7286 0.0000 0.0000 0.0000 412 ASN A ND2 
3056 N N   . LEU A 413 ? 243.5229 243.5229 243.5229 0.0000 0.0000 0.0000 413 LEU A N   
3057 C CA  . LEU A 413 ? 243.7219 243.7219 243.7219 0.0000 0.0000 0.0000 413 LEU A CA  
3058 C C   . LEU A 413 ? 243.9111 243.9111 243.9111 0.0000 0.0000 0.0000 413 LEU A C   
3059 O O   . LEU A 413 ? 244.1096 244.1096 244.1096 0.0000 0.0000 0.0000 413 LEU A O   
3060 C CB  . LEU A 413 ? 243.7770 243.7770 243.7770 0.0000 0.0000 0.0000 413 LEU A CB  
3061 C CG  . LEU A 413 ? 243.7566 243.7566 243.7566 0.0000 0.0000 0.0000 413 LEU A CG  
3062 C CD1 . LEU A 413 ? 243.8380 243.8380 243.8380 0.0000 0.0000 0.0000 413 LEU A CD1 
3063 C CD2 . LEU A 413 ? 243.7984 243.7984 243.7984 0.0000 0.0000 0.0000 413 LEU A CD2 
3064 N N   . PHE A 414 ? 243.9733 243.9733 243.9733 0.0000 0.0000 0.0000 414 PHE A N   
3065 C CA  . PHE A 414 ? 244.0208 244.0208 244.0208 0.0000 0.0000 0.0000 414 PHE A CA  
3066 C C   . PHE A 414 ? 244.0647 244.0647 244.0647 0.0000 0.0000 0.0000 414 PHE A C   
3067 O O   . PHE A 414 ? 244.0372 244.0372 244.0372 0.0000 0.0000 0.0000 414 PHE A O   
3068 C CB  . PHE A 414 ? 243.8163 243.8163 243.8163 0.0000 0.0000 0.0000 414 PHE A CB  
3069 C CG  . PHE A 414 ? 243.6971 243.6971 243.6971 0.0000 0.0000 0.0000 414 PHE A CG  
3070 C CD1 . PHE A 414 ? 243.7573 243.7573 243.7573 0.0000 0.0000 0.0000 414 PHE A CD1 
3071 C CD2 . PHE A 414 ? 243.6498 243.6498 243.6498 0.0000 0.0000 0.0000 414 PHE A CD2 
3072 C CE1 . PHE A 414 ? 243.7826 243.7826 243.7826 0.0000 0.0000 0.0000 414 PHE A CE1 
3073 C CE2 . PHE A 414 ? 243.6469 243.6469 243.6469 0.0000 0.0000 0.0000 414 PHE A CE2 
3074 C CZ  . PHE A 414 ? 243.7043 243.7043 243.7043 0.0000 0.0000 0.0000 414 PHE A CZ  
3075 N N   . GLU A 415 ? 244.7011 244.7011 244.7011 0.0000 0.0000 0.0000 415 GLU A N   
3076 C CA  . GLU A 415 ? 244.7948 244.7948 244.7948 0.0000 0.0000 0.0000 415 GLU A CA  
3077 C C   . GLU A 415 ? 244.9637 244.9637 244.9637 0.0000 0.0000 0.0000 415 GLU A C   
3078 O O   . GLU A 415 ? 244.8842 244.8842 244.8842 0.0000 0.0000 0.0000 415 GLU A O   
3079 C CB  . GLU A 415 ? 244.6784 244.6784 244.6784 0.0000 0.0000 0.0000 415 GLU A CB  
3080 C CG  . GLU A 415 ? 244.6123 244.6123 244.6123 0.0000 0.0000 0.0000 415 GLU A CG  
3081 C CD  . GLU A 415 ? 244.6290 244.6290 244.6290 0.0000 0.0000 0.0000 415 GLU A CD  
3082 O OE1 . GLU A 415 ? 244.7504 244.7504 244.7504 0.0000 0.0000 0.0000 415 GLU A OE1 
3083 O OE2 . GLU A 415 ? 244.5768 244.5768 244.5768 0.0000 0.0000 0.0000 415 GLU A OE2 
3084 N N   . THR A 416 ? 256.4824 256.4824 256.4824 0.0000 0.0000 0.0000 416 THR A N   
3085 C CA  . THR A 416 ? 256.8123 256.8123 256.8123 0.0000 0.0000 0.0000 416 THR A CA  
3086 C C   . THR A 416 ? 257.0859 257.0859 257.0859 0.0000 0.0000 0.0000 416 THR A C   
3087 O O   . THR A 416 ? 256.9263 256.9263 256.9263 0.0000 0.0000 0.0000 416 THR A O   
3088 C CB  . THR A 416 ? 256.9568 256.9568 256.9568 0.0000 0.0000 0.0000 416 THR A CB  
3089 O OG1 . THR A 416 ? 257.0208 257.0208 257.0208 0.0000 0.0000 0.0000 416 THR A OG1 
3090 C CG2 . THR A 416 ? 256.8029 256.8029 256.8029 0.0000 0.0000 0.0000 416 THR A CG2 
3091 N N   . GLU A 417 ? 266.1335 266.1335 266.1335 0.0000 0.0000 0.0000 417 GLU A N   
3092 C CA  . GLU A 417 ? 266.2675 266.2675 266.2675 0.0000 0.0000 0.0000 417 GLU A CA  
3093 C C   . GLU A 417 ? 266.2790 266.2790 266.2790 0.0000 0.0000 0.0000 417 GLU A C   
3094 O O   . GLU A 417 ? 266.2569 266.2569 266.2569 0.0000 0.0000 0.0000 417 GLU A O   
3095 C CB  . GLU A 417 ? 266.3819 266.3819 266.3819 0.0000 0.0000 0.0000 417 GLU A CB  
3096 C CG  . GLU A 417 ? 266.4115 266.4115 266.4115 0.0000 0.0000 0.0000 417 GLU A CG  
3097 C CD  . GLU A 417 ? 266.3561 266.3561 266.3561 0.0000 0.0000 0.0000 417 GLU A CD  
3098 O OE1 . GLU A 417 ? 266.2969 266.2969 266.2969 0.0000 0.0000 0.0000 417 GLU A OE1 
3099 O OE2 . GLU A 417 ? 266.3298 266.3298 266.3298 0.0000 0.0000 0.0000 417 GLU A OE2 
3100 N N   . GLU A 418 ? 267.8426 267.8426 267.8426 0.0000 0.0000 0.0000 418 GLU A N   
3101 C CA  . GLU A 418 ? 267.8739 267.8739 267.8739 0.0000 0.0000 0.0000 418 GLU A CA  
3102 C C   . GLU A 418 ? 267.5911 267.5911 267.5911 0.0000 0.0000 0.0000 418 GLU A C   
3103 O O   . GLU A 418 ? 267.5661 267.5661 267.5661 0.0000 0.0000 0.0000 418 GLU A O   
3104 C CB  . GLU A 418 ? 268.0025 268.0025 268.0025 0.0000 0.0000 0.0000 418 GLU A CB  
3105 C CG  . GLU A 418 ? 268.0939 268.0939 268.0939 0.0000 0.0000 0.0000 418 GLU A CG  
3106 C CD  . GLU A 418 ? 268.0930 268.0930 268.0930 0.0000 0.0000 0.0000 418 GLU A CD  
3107 O OE1 . GLU A 418 ? 268.1365 268.1365 268.1365 0.0000 0.0000 0.0000 418 GLU A OE1 
3108 O OE2 . GLU A 418 ? 268.0169 268.0169 268.0169 0.0000 0.0000 0.0000 418 GLU A OE2 
3109 N N   . THR A 419 ? 257.8868 257.8868 257.8868 0.0000 0.0000 0.0000 419 THR A N   
3110 C CA  . THR A 419 ? 257.6891 257.6891 257.6891 0.0000 0.0000 0.0000 419 THR A CA  
3111 C C   . THR A 419 ? 257.4434 257.4434 257.4434 0.0000 0.0000 0.0000 419 THR A C   
3112 O O   . THR A 419 ? 257.3937 257.3937 257.3937 0.0000 0.0000 0.0000 419 THR A O   
3113 C CB  . THR A 419 ? 257.5235 257.5235 257.5235 0.0000 0.0000 0.0000 419 THR A CB  
3114 O OG1 . THR A 419 ? 257.5193 257.5193 257.5193 0.0000 0.0000 0.0000 419 THR A OG1 
3115 C CG2 . THR A 419 ? 257.3981 257.3981 257.3981 0.0000 0.0000 0.0000 419 THR A CG2 
3116 N N   . ARG A 420 ? 249.4635 249.4635 249.4635 0.0000 0.0000 0.0000 420 ARG A N   
3117 C CA  . ARG A 420 ? 249.2267 249.2267 249.2267 0.0000 0.0000 0.0000 420 ARG A CA  
3118 C C   . ARG A 420 ? 249.3670 249.3670 249.3670 0.0000 0.0000 0.0000 420 ARG A C   
3119 O O   . ARG A 420 ? 249.2105 249.2105 249.2105 0.0000 0.0000 0.0000 420 ARG A O   
3120 C CB  . ARG A 420 ? 249.2084 249.2084 249.2084 0.0000 0.0000 0.0000 420 ARG A CB  
3121 C CG  . ARG A 420 ? 248.8425 248.8425 248.8425 0.0000 0.0000 0.0000 420 ARG A CG  
3122 C CD  . ARG A 420 ? 248.8396 248.8396 248.8396 0.0000 0.0000 0.0000 420 ARG A CD  
3123 N NE  . ARG A 420 ? 248.6059 248.6059 248.6059 0.0000 0.0000 0.0000 420 ARG A NE  
3124 C CZ  . ARG A 420 ? 248.7627 248.7627 248.7627 0.0000 0.0000 0.0000 420 ARG A CZ  
3125 N NH1 . ARG A 420 ? 248.9731 248.9731 248.9731 0.0000 0.0000 0.0000 420 ARG A NH1 
3126 N NH2 . ARG A 420 ? 248.5135 248.5135 248.5135 0.0000 0.0000 0.0000 420 ARG A NH2 
3127 N N   . LYS A 421 ? 258.5541 258.5541 258.5541 0.0000 0.0000 0.0000 421 LYS A N   
3128 C CA  . LYS A 421 ? 258.6183 258.6183 258.6183 0.0000 0.0000 0.0000 421 LYS A CA  
3129 C C   . LYS A 421 ? 258.4356 258.4356 258.4356 0.0000 0.0000 0.0000 421 LYS A C   
3130 O O   . LYS A 421 ? 258.5139 258.5139 258.5139 0.0000 0.0000 0.0000 421 LYS A O   
3131 C CB  . LYS A 421 ? 258.8192 258.8192 258.8192 0.0000 0.0000 0.0000 421 LYS A CB  
3132 C CG  . LYS A 421 ? 258.7769 258.7769 258.7769 0.0000 0.0000 0.0000 421 LYS A CG  
3133 C CD  . LYS A 421 ? 258.7879 258.7879 258.7879 0.0000 0.0000 0.0000 421 LYS A CD  
3134 C CE  . LYS A 421 ? 258.7885 258.7885 258.7885 0.0000 0.0000 0.0000 421 LYS A CE  
3135 N NZ  . LYS A 421 ? 258.7317 258.7317 258.7317 0.0000 0.0000 0.0000 421 LYS A NZ  
3136 N N   . ILE A 422 ? 249.8701 249.8701 249.8701 0.0000 0.0000 0.0000 422 ILE A N   
3137 C CA  . ILE A 422 ? 249.6364 249.6364 249.6364 0.0000 0.0000 0.0000 422 ILE A CA  
3138 C C   . ILE A 422 ? 249.4590 249.4590 249.4590 0.0000 0.0000 0.0000 422 ILE A C   
3139 O O   . ILE A 422 ? 249.3999 249.3999 249.3999 0.0000 0.0000 0.0000 422 ILE A O   
3140 C CB  . ILE A 422 ? 249.6112 249.6112 249.6112 0.0000 0.0000 0.0000 422 ILE A CB  
3141 C CG1 . ILE A 422 ? 249.4738 249.4738 249.4738 0.0000 0.0000 0.0000 422 ILE A CG1 
3142 C CG2 . ILE A 422 ? 249.6312 249.6312 249.6312 0.0000 0.0000 0.0000 422 ILE A CG2 
3143 C CD1 . ILE A 422 ? 249.4801 249.4801 249.4801 0.0000 0.0000 0.0000 422 ILE A CD1 
3144 N N   . LEU A 423 ? 243.5866 243.5866 243.5866 0.0000 0.0000 0.0000 423 LEU A N   
3145 C CA  . LEU A 423 ? 243.3204 243.3204 243.3204 0.0000 0.0000 0.0000 423 LEU A CA  
3146 C C   . LEU A 423 ? 243.4952 243.4952 243.4952 0.0000 0.0000 0.0000 423 LEU A C   
3147 O O   . LEU A 423 ? 243.1983 243.1983 243.1983 0.0000 0.0000 0.0000 423 LEU A O   
3148 C CB  . LEU A 423 ? 243.0310 243.0310 243.0310 0.0000 0.0000 0.0000 423 LEU A CB  
3149 C CG  . LEU A 423 ? 243.0435 243.0435 243.0435 0.0000 0.0000 0.0000 423 LEU A CG  
3150 C CD1 . LEU A 423 ? 242.5433 242.5433 242.5433 0.0000 0.0000 0.0000 423 LEU A CD1 
3151 C CD2 . LEU A 423 ? 242.9027 242.9027 242.9027 0.0000 0.0000 0.0000 423 LEU A CD2 
3152 N N   . ASP A 424 ? 255.4549 255.4549 255.4549 0.0000 0.0000 0.0000 424 ASP A N   
3153 C CA  . ASP A 424 ? 255.4909 255.4909 255.4909 0.0000 0.0000 0.0000 424 ASP A CA  
3154 C C   . ASP A 424 ? 255.6185 255.6185 255.6185 0.0000 0.0000 0.0000 424 ASP A C   
3155 O O   . ASP A 424 ? 255.5299 255.5299 255.5299 0.0000 0.0000 0.0000 424 ASP A O   
3156 C CB  . ASP A 424 ? 255.7316 255.7316 255.7316 0.0000 0.0000 0.0000 424 ASP A CB  
3157 C CG  . ASP A 424 ? 255.7608 255.7608 255.7608 0.0000 0.0000 0.0000 424 ASP A CG  
3158 O OD1 . ASP A 424 ? 255.5679 255.5679 255.5679 0.0000 0.0000 0.0000 424 ASP A OD1 
3159 O OD2 . ASP A 424 ? 255.9084 255.9084 255.9084 0.0000 0.0000 0.0000 424 ASP A OD2 
3160 N N   . ASP A 425 ? 254.4203 254.4203 254.4203 0.0000 0.0000 0.0000 425 ASP A N   
3161 C CA  . ASP A 425 ? 254.4068 254.4068 254.4068 0.0000 0.0000 0.0000 425 ASP A CA  
3162 C C   . ASP A 425 ? 254.1228 254.1228 254.1228 0.0000 0.0000 0.0000 425 ASP A C   
3163 O O   . ASP A 425 ? 254.0691 254.0691 254.0691 0.0000 0.0000 0.0000 425 ASP A O   
3164 C CB  . ASP A 425 ? 254.4984 254.4984 254.4984 0.0000 0.0000 0.0000 425 ASP A CB  
3165 C CG  . ASP A 425 ? 254.4899 254.4899 254.4899 0.0000 0.0000 0.0000 425 ASP A CG  
3166 O OD1 . ASP A 425 ? 254.4803 254.4803 254.4803 0.0000 0.0000 0.0000 425 ASP A OD1 
3167 O OD2 . ASP A 425 ? 254.4583 254.4583 254.4583 0.0000 0.0000 0.0000 425 ASP A OD2 
3168 N N   . ILE A 426 ? 246.9670 246.9670 246.9670 0.0000 0.0000 0.0000 426 ILE A N   
3169 C CA  . ILE A 426 ? 246.8217 246.8217 246.8217 0.0000 0.0000 0.0000 426 ILE A CA  
3170 C C   . ILE A 426 ? 246.6094 246.6094 246.6094 0.0000 0.0000 0.0000 426 ILE A C   
3171 O O   . ILE A 426 ? 246.4713 246.4713 246.4713 0.0000 0.0000 0.0000 426 ILE A O   
3172 C CB  . ILE A 426 ? 246.7717 246.7717 246.7717 0.0000 0.0000 0.0000 426 ILE A CB  
3173 C CG1 . ILE A 426 ? 246.8200 246.8200 246.8200 0.0000 0.0000 0.0000 426 ILE A CG1 
3174 C CG2 . ILE A 426 ? 246.3642 246.3642 246.3642 0.0000 0.0000 0.0000 426 ILE A CG2 
3175 C CD1 . ILE A 426 ? 246.7617 246.7617 246.7617 0.0000 0.0000 0.0000 426 ILE A CD1 
3176 N N   . CYS A 427 ? 244.7536 244.7536 244.7536 0.0000 0.0000 0.0000 427 CYS A N   
3177 C CA  . CYS A 427 ? 244.5281 244.5281 244.5281 0.0000 0.0000 0.0000 427 CYS A CA  
3178 C C   . CYS A 427 ? 244.4486 244.4486 244.4486 0.0000 0.0000 0.0000 427 CYS A C   
3179 O O   . CYS A 427 ? 244.3426 244.3426 244.3426 0.0000 0.0000 0.0000 427 CYS A O   
3180 C CB  . CYS A 427 ? 244.4524 244.4524 244.4524 0.0000 0.0000 0.0000 427 CYS A CB  
3181 S SG  . CYS A 427 ? 243.9270 243.9270 243.9270 0.0000 0.0000 0.0000 427 CYS A SG  
3182 N N   . VAL A 428 ? 241.5781 241.5781 241.5781 0.0000 0.0000 0.0000 428 VAL A N   
3183 C CA  . VAL A 428 ? 241.4484 241.4484 241.4484 0.0000 0.0000 0.0000 428 VAL A CA  
3184 C C   . VAL A 428 ? 241.3465 241.3465 241.3465 0.0000 0.0000 0.0000 428 VAL A C   
3185 O O   . VAL A 428 ? 241.3346 241.3346 241.3346 0.0000 0.0000 0.0000 428 VAL A O   
3186 C CB  . VAL A 428 ? 241.4991 241.4991 241.4991 0.0000 0.0000 0.0000 428 VAL A CB  
3187 C CG1 . VAL A 428 ? 241.4374 241.4374 241.4374 0.0000 0.0000 0.0000 428 VAL A CG1 
3188 C CG2 . VAL A 428 ? 241.4898 241.4898 241.4898 0.0000 0.0000 0.0000 428 VAL A CG2 
3189 N N   . ALA A 429 ? 236.6433 236.6433 236.6433 0.0000 0.0000 0.0000 429 ALA A N   
3190 C CA  . ALA A 429 ? 236.4520 236.4520 236.4520 0.0000 0.0000 0.0000 429 ALA A CA  
3191 C C   . ALA A 429 ? 236.4501 236.4501 236.4501 0.0000 0.0000 0.0000 429 ALA A C   
3192 O O   . ALA A 429 ? 236.4226 236.4226 236.4226 0.0000 0.0000 0.0000 429 ALA A O   
3193 C CB  . ALA A 429 ? 236.4781 236.4781 236.4781 0.0000 0.0000 0.0000 429 ALA A CB  
3194 N N   . LYS A 430 ? 238.6135 238.6135 238.6135 0.0000 0.0000 0.0000 430 LYS A N   
3195 C CA  . LYS A 430 ? 238.6295 238.6295 238.6295 0.0000 0.0000 0.0000 430 LYS A CA  
3196 C C   . LYS A 430 ? 238.5709 238.5709 238.5709 0.0000 0.0000 0.0000 430 LYS A C   
3197 O O   . LYS A 430 ? 238.5532 238.5532 238.5532 0.0000 0.0000 0.0000 430 LYS A O   
3198 C CB  . LYS A 430 ? 238.5111 238.5111 238.5111 0.0000 0.0000 0.0000 430 LYS A CB  
3199 C CG  . LYS A 430 ? 238.3980 238.3980 238.3980 0.0000 0.0000 0.0000 430 LYS A CG  
3200 C CD  . LYS A 430 ? 238.5071 238.5071 238.5071 0.0000 0.0000 0.0000 430 LYS A CD  
3201 C CE  . LYS A 430 ? 238.4831 238.4831 238.4831 0.0000 0.0000 0.0000 430 LYS A CE  
3202 N NZ  . LYS A 430 ? 238.2550 238.2550 238.2550 0.0000 0.0000 0.0000 430 LYS A NZ  
3203 N N   . ALA A 431 ? 236.0205 236.0205 236.0205 0.0000 0.0000 0.0000 431 ALA A N   
3204 C CA  . ALA A 431 ? 235.9328 235.9328 235.9328 0.0000 0.0000 0.0000 431 ALA A CA  
3205 C C   . ALA A 431 ? 235.8815 235.8815 235.8815 0.0000 0.0000 0.0000 431 ALA A C   
3206 O O   . ALA A 431 ? 235.8531 235.8531 235.8531 0.0000 0.0000 0.0000 431 ALA A O   
3207 C CB  . ALA A 431 ? 235.9243 235.9243 235.9243 0.0000 0.0000 0.0000 431 ALA A CB  
3208 N N   . VAL A 432 ? 234.4253 234.4253 234.4253 0.0000 0.0000 0.0000 432 VAL A N   
3209 C CA  . VAL A 432 ? 234.3670 234.3670 234.3670 0.0000 0.0000 0.0000 432 VAL A CA  
3210 C C   . VAL A 432 ? 234.4407 234.4407 234.4407 0.0000 0.0000 0.0000 432 VAL A C   
3211 O O   . VAL A 432 ? 234.5056 234.5056 234.5056 0.0000 0.0000 0.0000 432 VAL A O   
3212 C CB  . VAL A 432 ? 234.3081 234.3081 234.3081 0.0000 0.0000 0.0000 432 VAL A CB  
3213 C CG1 . VAL A 432 ? 233.9079 233.9079 233.9079 0.0000 0.0000 0.0000 432 VAL A CG1 
3214 C CG2 . VAL A 432 ? 233.9732 233.9732 233.9732 0.0000 0.0000 0.0000 432 VAL A CG2 
3215 N N   . GLU A 433 ? 236.5353 236.5353 236.5353 0.0000 0.0000 0.0000 433 GLU A N   
3216 C CA  . GLU A 433 ? 236.5009 236.5009 236.5009 0.0000 0.0000 0.0000 433 GLU A CA  
3217 C C   . GLU A 433 ? 236.4109 236.4109 236.4109 0.0000 0.0000 0.0000 433 GLU A C   
3218 O O   . GLU A 433 ? 236.1024 236.1024 236.1024 0.0000 0.0000 0.0000 433 GLU A O   
3219 C CB  . GLU A 433 ? 236.5257 236.5257 236.5257 0.0000 0.0000 0.0000 433 GLU A CB  
3220 C CG  . GLU A 433 ? 236.5471 236.5471 236.5471 0.0000 0.0000 0.0000 433 GLU A CG  
3221 C CD  . GLU A 433 ? 236.5381 236.5381 236.5381 0.0000 0.0000 0.0000 433 GLU A CD  
3222 O OE1 . GLU A 433 ? 236.5737 236.5737 236.5737 0.0000 0.0000 0.0000 433 GLU A OE1 
3223 O OE2 . GLU A 433 ? 236.5138 236.5138 236.5138 0.0000 0.0000 0.0000 433 GLU A OE2 
3224 N N   . CYS A 434 ? 233.0559 233.0559 233.0559 0.0000 0.0000 0.0000 434 CYS A N   
3225 C CA  . CYS A 434 ? 232.8889 232.8889 232.8889 0.0000 0.0000 0.0000 434 CYS A CA  
3226 C C   . CYS A 434 ? 232.8916 232.8916 232.8916 0.0000 0.0000 0.0000 434 CYS A C   
3227 O O   . CYS A 434 ? 232.8938 232.8938 232.8938 0.0000 0.0000 0.0000 434 CYS A O   
3228 C CB  . CYS A 434 ? 232.6715 232.6715 232.6715 0.0000 0.0000 0.0000 434 CYS A CB  
3229 S SG  . CYS A 434 ? 232.4318 232.4318 232.4318 0.0000 0.0000 0.0000 434 CYS A SG  
3230 N N   . PRO A 435 ? 230.2418 230.2418 230.2418 0.0000 0.0000 0.0000 435 PRO A N   
3231 C CA  . PRO A 435 ? 230.4765 230.4765 230.4765 0.0000 0.0000 0.0000 435 PRO A CA  
3232 C C   . PRO A 435 ? 230.3965 230.3965 230.3965 0.0000 0.0000 0.0000 435 PRO A C   
3233 O O   . PRO A 435 ? 230.1108 230.1108 230.1108 0.0000 0.0000 0.0000 435 PRO A O   
3234 C CB  . PRO A 435 ? 229.6270 229.6270 229.6270 0.0000 0.0000 0.0000 435 PRO A CB  
3235 C CG  . PRO A 435 ? 228.1159 228.1159 228.1159 0.0000 0.0000 0.0000 435 PRO A CG  
3236 C CD  . PRO A 435 ? 229.4076 229.4076 229.4076 0.0000 0.0000 0.0000 435 PRO A CD  
3237 N N   . PRO A 436 ? 232.1011 232.1011 232.1011 0.0000 0.0000 0.0000 436 PRO A N   
3238 C CA  . PRO A 436 ? 232.0162 232.0162 232.0162 0.0000 0.0000 0.0000 436 PRO A CA  
3239 C C   . PRO A 436 ? 231.9520 231.9520 231.9520 0.0000 0.0000 0.0000 436 PRO A C   
3240 O O   . PRO A 436 ? 232.0658 232.0658 232.0658 0.0000 0.0000 0.0000 436 PRO A O   
3241 C CB  . PRO A 436 ? 232.1565 232.1565 232.1565 0.0000 0.0000 0.0000 436 PRO A CB  
3242 C CG  . PRO A 436 ? 232.2781 232.2781 232.2781 0.0000 0.0000 0.0000 436 PRO A CG  
3243 C CD  . PRO A 436 ? 232.2754 232.2754 232.2754 0.0000 0.0000 0.0000 436 PRO A CD  
3244 N N   . PRO A 437 ? 225.2124 225.2124 225.2124 0.0000 0.0000 0.0000 437 PRO A N   
3245 C CA  . PRO A 437 ? 225.1439 225.1439 225.1439 0.0000 0.0000 0.0000 437 PRO A CA  
3246 C C   . PRO A 437 ? 224.9820 224.9820 224.9820 0.0000 0.0000 0.0000 437 PRO A C   
3247 O O   . PRO A 437 ? 224.9534 224.9534 224.9534 0.0000 0.0000 0.0000 437 PRO A O   
3248 C CB  . PRO A 437 ? 225.2035 225.2035 225.2035 0.0000 0.0000 0.0000 437 PRO A CB  
3249 C CG  . PRO A 437 ? 225.1598 225.1598 225.1598 0.0000 0.0000 0.0000 437 PRO A CG  
3250 C CD  . PRO A 437 ? 225.1237 225.1237 225.1237 0.0000 0.0000 0.0000 437 PRO A CD  
3251 N N   . ARG A 438 ? 218.8904 218.8904 218.8904 0.0000 0.0000 0.0000 438 ARG A N   
3252 C CA  . ARG A 438 ? 218.6935 218.6935 218.6935 0.0000 0.0000 0.0000 438 ARG A CA  
3253 C C   . ARG A 438 ? 218.7466 218.7466 218.7466 0.0000 0.0000 0.0000 438 ARG A C   
3254 O O   . ARG A 438 ? 218.9275 218.9275 218.9275 0.0000 0.0000 0.0000 438 ARG A O   
3255 C CB  . ARG A 438 ? 218.5690 218.5690 218.5690 0.0000 0.0000 0.0000 438 ARG A CB  
3256 C CG  . ARG A 438 ? 218.6695 218.6695 218.6695 0.0000 0.0000 0.0000 438 ARG A CG  
3257 C CD  . ARG A 438 ? 218.7093 218.7093 218.7093 0.0000 0.0000 0.0000 438 ARG A CD  
3258 N NE  . ARG A 438 ? 218.6734 218.6734 218.6734 0.0000 0.0000 0.0000 438 ARG A NE  
3259 C CZ  . ARG A 438 ? 218.7669 218.7669 218.7669 0.0000 0.0000 0.0000 438 ARG A CZ  
3260 N NH1 . ARG A 438 ? 218.8933 218.8933 218.8933 0.0000 0.0000 0.0000 438 ARG A NH1 
3261 N NH2 . ARG A 438 ? 219.2347 219.2347 219.2347 0.0000 0.0000 0.0000 438 ARG A NH2 
3262 N N   . THR A 439 ? 219.5284 219.5284 219.5284 0.0000 0.0000 0.0000 439 THR A N   
3263 C CA  . THR A 439 ? 219.6122 219.6122 219.6122 0.0000 0.0000 0.0000 439 THR A CA  
3264 C C   . THR A 439 ? 219.3470 219.3470 219.3470 0.0000 0.0000 0.0000 439 THR A C   
3265 O O   . THR A 439 ? 219.1320 219.1320 219.1320 0.0000 0.0000 0.0000 439 THR A O   
3266 C CB  . THR A 439 ? 219.4425 219.4425 219.4425 0.0000 0.0000 0.0000 439 THR A CB  
3267 O OG1 . THR A 439 ? 219.3659 219.3659 219.3659 0.0000 0.0000 0.0000 439 THR A OG1 
3268 C CG2 . THR A 439 ? 219.5183 219.5183 219.5183 0.0000 0.0000 0.0000 439 THR A CG2 
3269 N N   . THR A 440 ? 218.6235 218.6235 218.6235 0.0000 0.0000 0.0000 440 THR A N   
3270 C CA  . THR A 440 ? 218.5866 218.5866 218.5866 0.0000 0.0000 0.0000 440 THR A CA  
3271 C C   . THR A 440 ? 218.3073 218.3073 218.3073 0.0000 0.0000 0.0000 440 THR A C   
3272 O O   . THR A 440 ? 218.2314 218.2314 218.2314 0.0000 0.0000 0.0000 440 THR A O   
3273 C CB  . THR A 440 ? 218.7796 218.7796 218.7796 0.0000 0.0000 0.0000 440 THR A CB  
3274 O OG1 . THR A 440 ? 219.3887 219.3887 219.3887 0.0000 0.0000 0.0000 440 THR A OG1 
3275 C CG2 . THR A 440 ? 218.8739 218.8739 218.8739 0.0000 0.0000 0.0000 440 THR A CG2 
3276 N N   . ALA A 441 ? 210.3360 210.3360 210.3360 0.0000 0.0000 0.0000 441 ALA A N   
3277 C CA  . ALA A 441 ? 210.1272 210.1272 210.1272 0.0000 0.0000 0.0000 441 ALA A CA  
3278 C C   . ALA A 441 ? 210.0754 210.0754 210.0754 0.0000 0.0000 0.0000 441 ALA A C   
3279 O O   . ALA A 441 ? 209.8783 209.8783 209.8783 0.0000 0.0000 0.0000 441 ALA A O   
3280 C CB  . ALA A 441 ? 209.7897 209.7897 209.7897 0.0000 0.0000 0.0000 441 ALA A CB  
3281 N N   . ARG A 442 ? 214.1222 214.1222 214.1222 0.0000 0.0000 0.0000 442 ARG A N   
3282 C CA  . ARG A 442 ? 214.2005 214.2005 214.2005 0.0000 0.0000 0.0000 442 ARG A CA  
3283 C C   . ARG A 442 ? 213.8459 213.8459 213.8459 0.0000 0.0000 0.0000 442 ARG A C   
3284 O O   . ARG A 442 ? 213.6724 213.6724 213.6724 0.0000 0.0000 0.0000 442 ARG A O   
3285 C CB  . ARG A 442 ? 214.4110 214.4110 214.4110 0.0000 0.0000 0.0000 442 ARG A CB  
3286 C CG  . ARG A 442 ? 214.3511 214.3511 214.3511 0.0000 0.0000 0.0000 442 ARG A CG  
3287 C CD  . ARG A 442 ? 214.4935 214.4935 214.4935 0.0000 0.0000 0.0000 442 ARG A CD  
3288 N NE  . ARG A 442 ? 214.3979 214.3979 214.3979 0.0000 0.0000 0.0000 442 ARG A NE  
3289 C CZ  . ARG A 442 ? 214.0049 214.0049 214.0049 0.0000 0.0000 0.0000 442 ARG A CZ  
3290 N NH1 . ARG A 442 ? 213.0895 213.0895 213.0895 0.0000 0.0000 0.0000 442 ARG A NH1 
3291 N NH2 . ARG A 442 ? 213.8258 213.8258 213.8258 0.0000 0.0000 0.0000 442 ARG A NH2 
3292 N N   . LEU A 443 ? 206.5986 206.5986 206.5986 0.0000 0.0000 0.0000 443 LEU A N   
3293 C CA  . LEU A 443 ? 206.3905 206.3905 206.3905 0.0000 0.0000 0.0000 443 LEU A CA  
3294 C C   . LEU A 443 ? 206.0431 206.0431 206.0431 0.0000 0.0000 0.0000 443 LEU A C   
3295 O O   . LEU A 443 ? 205.8725 205.8725 205.8725 0.0000 0.0000 0.0000 443 LEU A O   
3296 C CB  . LEU A 443 ? 206.5605 206.5605 206.5605 0.0000 0.0000 0.0000 443 LEU A CB  
3297 C CG  . LEU A 443 ? 206.7603 206.7603 206.7603 0.0000 0.0000 0.0000 443 LEU A CG  
3298 C CD1 . LEU A 443 ? 207.1081 207.1081 207.1081 0.0000 0.0000 0.0000 443 LEU A CD1 
3299 C CD2 . LEU A 443 ? 206.8630 206.8630 206.8630 0.0000 0.0000 0.0000 443 LEU A CD2 
3300 N N   . LEU A 444 ? 200.4174 200.4174 200.4174 0.0000 0.0000 0.0000 444 LEU A N   
3301 C CA  . LEU A 444 ? 200.0921 200.0921 200.0921 0.0000 0.0000 0.0000 444 LEU A CA  
3302 C C   . LEU A 444 ? 199.7979 199.7979 199.7979 0.0000 0.0000 0.0000 444 LEU A C   
3303 O O   . LEU A 444 ? 199.5440 199.5440 199.5440 0.0000 0.0000 0.0000 444 LEU A O   
3304 C CB  . LEU A 444 ? 200.0631 200.0631 200.0631 0.0000 0.0000 0.0000 444 LEU A CB  
3305 C CG  . LEU A 444 ? 200.2555 200.2555 200.2555 0.0000 0.0000 0.0000 444 LEU A CG  
3306 C CD1 . LEU A 444 ? 200.1794 200.1794 200.1794 0.0000 0.0000 0.0000 444 LEU A CD1 
3307 C CD2 . LEU A 444 ? 200.0239 200.0239 200.0239 0.0000 0.0000 0.0000 444 LEU A CD2 
3308 N N   . ASP A 445 ? 200.0414 200.0414 200.0414 0.0000 0.0000 0.0000 445 ASP A N   
3309 C CA  . ASP A 445 ? 199.8493 199.8493 199.8493 0.0000 0.0000 0.0000 445 ASP A CA  
3310 C C   . ASP A 445 ? 199.6702 199.6702 199.6702 0.0000 0.0000 0.0000 445 ASP A C   
3311 O O   . ASP A 445 ? 199.5191 199.5191 199.5191 0.0000 0.0000 0.0000 445 ASP A O   
3312 C CB  . ASP A 445 ? 200.0370 200.0370 200.0370 0.0000 0.0000 0.0000 445 ASP A CB  
3313 C CG  . ASP A 445 ? 199.9333 199.9333 199.9333 0.0000 0.0000 0.0000 445 ASP A CG  
3314 O OD1 . ASP A 445 ? 199.8184 199.8184 199.8184 0.0000 0.0000 0.0000 445 ASP A OD1 
3315 O OD2 . ASP A 445 ? 199.9379 199.9379 199.9379 0.0000 0.0000 0.0000 445 ASP A OD2 
3316 N N   . LYS A 446 ? 198.1079 198.1079 198.1079 0.0000 0.0000 0.0000 446 LYS A N   
3317 C CA  . LYS A 446 ? 198.0203 198.0203 198.0203 0.0000 0.0000 0.0000 446 LYS A CA  
3318 C C   . LYS A 446 ? 197.7600 197.7600 197.7600 0.0000 0.0000 0.0000 446 LYS A C   
3319 O O   . LYS A 446 ? 197.7397 197.7397 197.7397 0.0000 0.0000 0.0000 446 LYS A O   
3320 C CB  . LYS A 446 ? 198.4267 198.4267 198.4267 0.0000 0.0000 0.0000 446 LYS A CB  
3321 C CG  . LYS A 446 ? 198.5083 198.5083 198.5083 0.0000 0.0000 0.0000 446 LYS A CG  
3322 C CD  . LYS A 446 ? 198.3541 198.3541 198.3541 0.0000 0.0000 0.0000 446 LYS A CD  
3323 C CE  . LYS A 446 ? 197.9217 197.9217 197.9217 0.0000 0.0000 0.0000 446 LYS A CE  
3324 N NZ  . LYS A 446 ? 197.0155 197.0155 197.0155 0.0000 0.0000 0.0000 446 LYS A NZ  
3325 N N   . LEU A 447 ? 191.9914 191.9914 191.9914 0.0000 0.0000 0.0000 447 LEU A N   
3326 C CA  . LEU A 447 ? 191.6392 191.6392 191.6392 0.0000 0.0000 0.0000 447 LEU A CA  
3327 C C   . LEU A 447 ? 191.3213 191.3213 191.3213 0.0000 0.0000 0.0000 447 LEU A C   
3328 O O   . LEU A 447 ? 191.4576 191.4576 191.4576 0.0000 0.0000 0.0000 447 LEU A O   
3329 C CB  . LEU A 447 ? 191.8173 191.8173 191.8173 0.0000 0.0000 0.0000 447 LEU A CB  
3330 C CG  . LEU A 447 ? 191.9759 191.9759 191.9759 0.0000 0.0000 0.0000 447 LEU A CG  
3331 C CD1 . LEU A 447 ? 192.3520 192.3520 192.3520 0.0000 0.0000 0.0000 447 LEU A CD1 
3332 C CD2 . LEU A 447 ? 192.4922 192.4922 192.4922 0.0000 0.0000 0.0000 447 LEU A CD2 
3333 N N   . VAL A 448 ? 181.5260 181.5260 181.5260 0.0000 0.0000 0.0000 448 VAL A N   
3334 C CA  . VAL A 448 ? 181.0816 181.0816 181.0816 0.0000 0.0000 0.0000 448 VAL A CA  
3335 C C   . VAL A 448 ? 181.2443 181.2443 181.2443 0.0000 0.0000 0.0000 448 VAL A C   
3336 O O   . VAL A 448 ? 181.3886 181.3886 181.3886 0.0000 0.0000 0.0000 448 VAL A O   
3337 C CB  . VAL A 448 ? 181.0605 181.0605 181.0605 0.0000 0.0000 0.0000 448 VAL A CB  
3338 C CG1 . VAL A 448 ? 180.9128 180.9128 180.9128 0.0000 0.0000 0.0000 448 VAL A CG1 
3339 C CG2 . VAL A 448 ? 181.2681 181.2681 181.2681 0.0000 0.0000 0.0000 448 VAL A CG2 
3340 N N   . GLY A 449 ? 183.9599 183.9599 183.9599 0.0000 0.0000 0.0000 449 GLY A N   
3341 C CA  . GLY A 449 ? 183.8955 183.8955 183.8955 0.0000 0.0000 0.0000 449 GLY A CA  
3342 C C   . GLY A 449 ? 184.1406 184.1406 184.1406 0.0000 0.0000 0.0000 449 GLY A C   
3343 O O   . GLY A 449 ? 184.0002 184.0002 184.0002 0.0000 0.0000 0.0000 449 GLY A O   
3344 N N   . GLU A 450 ? 199.1978 199.1978 199.1978 0.0000 0.0000 0.0000 450 GLU A N   
3345 C CA  . GLU A 450 ? 199.5059 199.5059 199.5059 0.0000 0.0000 0.0000 450 GLU A CA  
3346 C C   . GLU A 450 ? 199.3399 199.3399 199.3399 0.0000 0.0000 0.0000 450 GLU A C   
3347 O O   . GLU A 450 ? 199.5456 199.5456 199.5456 0.0000 0.0000 0.0000 450 GLU A O   
3348 C CB  . GLU A 450 ? 199.8507 199.8507 199.8507 0.0000 0.0000 0.0000 450 GLU A CB  
3349 C CG  . GLU A 450 ? 200.0606 200.0606 200.0606 0.0000 0.0000 0.0000 450 GLU A CG  
3350 C CD  . GLU A 450 ? 200.0250 200.0250 200.0250 0.0000 0.0000 0.0000 450 GLU A CD  
3351 O OE1 . GLU A 450 ? 199.9363 199.9363 199.9363 0.0000 0.0000 0.0000 450 GLU A OE1 
3352 O OE2 . GLU A 450 ? 200.0950 200.0950 200.0950 0.0000 0.0000 0.0000 450 GLU A OE2 
3353 N N   . PHE A 451 ? 192.8902 192.8902 192.8902 0.0000 0.0000 0.0000 451 PHE A N   
3354 C CA  . PHE A 451 ? 192.8206 192.8206 192.8206 0.0000 0.0000 0.0000 451 PHE A CA  
3355 C C   . PHE A 451 ? 192.5462 192.5462 192.5462 0.0000 0.0000 0.0000 451 PHE A C   
3356 O O   . PHE A 451 ? 192.5008 192.5008 192.5008 0.0000 0.0000 0.0000 451 PHE A O   
3357 C CB  . PHE A 451 ? 192.8992 192.8992 192.8992 0.0000 0.0000 0.0000 451 PHE A CB  
3358 C CG  . PHE A 451 ? 192.9768 192.9768 192.9768 0.0000 0.0000 0.0000 451 PHE A CG  
3359 C CD1 . PHE A 451 ? 193.0289 193.0289 193.0289 0.0000 0.0000 0.0000 451 PHE A CD1 
3360 C CD2 . PHE A 451 ? 193.0780 193.0780 193.0780 0.0000 0.0000 0.0000 451 PHE A CD2 
3361 C CE1 . PHE A 451 ? 193.0843 193.0843 193.0843 0.0000 0.0000 0.0000 451 PHE A CE1 
3362 C CE2 . PHE A 451 ? 193.2503 193.2503 193.2503 0.0000 0.0000 0.0000 451 PHE A CE2 
3363 C CZ  . PHE A 451 ? 193.4868 193.4868 193.4868 0.0000 0.0000 0.0000 451 PHE A CZ  
3364 N N   . LEU A 452 ? 185.3335 185.3335 185.3335 0.0000 0.0000 0.0000 452 LEU A N   
3365 C CA  . LEU A 452 ? 185.0142 185.0142 185.0142 0.0000 0.0000 0.0000 452 LEU A CA  
3366 C C   . LEU A 452 ? 184.8719 184.8719 184.8719 0.0000 0.0000 0.0000 452 LEU A C   
3367 O O   . LEU A 452 ? 184.8090 184.8090 184.8090 0.0000 0.0000 0.0000 452 LEU A O   
3368 C CB  . LEU A 452 ? 184.9837 184.9837 184.9837 0.0000 0.0000 0.0000 452 LEU A CB  
3369 C CG  . LEU A 452 ? 185.2351 185.2351 185.2351 0.0000 0.0000 0.0000 452 LEU A CG  
3370 C CD1 . LEU A 452 ? 185.0931 185.0931 185.0931 0.0000 0.0000 0.0000 452 LEU A CD1 
3371 C CD2 . LEU A 452 ? 185.4460 185.4460 185.4460 0.0000 0.0000 0.0000 452 LEU A CD2 
3372 N N   . GLU A 453 ? 181.9049 181.9049 181.9049 0.0000 0.0000 0.0000 453 GLU A N   
3373 C CA  . GLU A 453 ? 181.6577 181.6577 181.6577 0.0000 0.0000 0.0000 453 GLU A CA  
3374 C C   . GLU A 453 ? 181.5903 181.5903 181.5903 0.0000 0.0000 0.0000 453 GLU A C   
3375 O O   . GLU A 453 ? 181.3121 181.3121 181.3121 0.0000 0.0000 0.0000 453 GLU A O   
3376 C CB  . GLU A 453 ? 181.7235 181.7235 181.7235 0.0000 0.0000 0.0000 453 GLU A CB  
3377 C CG  . GLU A 453 ? 181.6913 181.6913 181.6913 0.0000 0.0000 0.0000 453 GLU A CG  
3378 C CD  . GLU A 453 ? 181.3304 181.3304 181.3304 0.0000 0.0000 0.0000 453 GLU A CD  
3379 O OE1 . GLU A 453 ? 181.1598 181.1598 181.1598 0.0000 0.0000 0.0000 453 GLU A OE1 
3380 O OE2 . GLU A 453 ? 181.2910 181.2910 181.2910 0.0000 0.0000 0.0000 453 GLU A OE2 
3381 N N   . VAL A 454 ? 185.6657 185.6657 185.6657 0.0000 0.0000 0.0000 454 VAL A N   
3382 C CA  . VAL A 454 ? 185.6603 185.6603 185.6603 0.0000 0.0000 0.0000 454 VAL A CA  
3383 C C   . VAL A 454 ? 185.5305 185.5305 185.5305 0.0000 0.0000 0.0000 454 VAL A C   
3384 O O   . VAL A 454 ? 185.5397 185.5397 185.5397 0.0000 0.0000 0.0000 454 VAL A O   
3385 C CB  . VAL A 454 ? 185.7973 185.7973 185.7973 0.0000 0.0000 0.0000 454 VAL A CB  
3386 C CG1 . VAL A 454 ? 185.9815 185.9815 185.9815 0.0000 0.0000 0.0000 454 VAL A CG1 
3387 C CG2 . VAL A 454 ? 185.9019 185.9019 185.9019 0.0000 0.0000 0.0000 454 VAL A CG2 
3388 N N   . THR A 455 ? 182.6914 182.6914 182.6914 0.0000 0.0000 0.0000 455 THR A N   
3389 C CA  . THR A 455 ? 182.5316 182.5316 182.5316 0.0000 0.0000 0.0000 455 THR A CA  
3390 C C   . THR A 455 ? 182.0547 182.0547 182.0547 0.0000 0.0000 0.0000 455 THR A C   
3391 O O   . THR A 455 ? 182.1017 182.1017 182.1017 0.0000 0.0000 0.0000 455 THR A O   
3392 C CB  . THR A 455 ? 182.6033 182.6033 182.6033 0.0000 0.0000 0.0000 455 THR A CB  
3393 O OG1 . THR A 455 ? 182.4122 182.4122 182.4122 0.0000 0.0000 0.0000 455 THR A OG1 
3394 C CG2 . THR A 455 ? 182.7014 182.7014 182.7014 0.0000 0.0000 0.0000 455 THR A CG2 
3395 N N   . CYS A 456 ? 168.6204 168.6204 168.6204 0.0000 0.0000 0.0000 456 CYS A N   
3396 C CA  . CYS A 456 ? 168.0092 168.0092 168.0092 0.0000 0.0000 0.0000 456 CYS A CA  
3397 C C   . CYS A 456 ? 167.6256 167.6256 167.6256 0.0000 0.0000 0.0000 456 CYS A C   
3398 O O   . CYS A 456 ? 167.5053 167.5053 167.5053 0.0000 0.0000 0.0000 456 CYS A O   
3399 C CB  . CYS A 456 ? 167.9344 167.9344 167.9344 0.0000 0.0000 0.0000 456 CYS A CB  
3400 S SG  . CYS A 456 ? 167.8780 167.8780 167.8780 0.0000 0.0000 0.0000 456 CYS A SG  
3401 N N   . ILE A 457 ? 161.8186 161.8186 161.8186 0.0000 0.0000 0.0000 457 ILE A N   
3402 C CA  . ILE A 457 ? 161.4540 161.4540 161.4540 0.0000 0.0000 0.0000 457 ILE A CA  
3403 C C   . ILE A 457 ? 161.2455 161.2455 161.2455 0.0000 0.0000 0.0000 457 ILE A C   
3404 O O   . ILE A 457 ? 161.3603 161.3603 161.3603 0.0000 0.0000 0.0000 457 ILE A O   
3405 C CB  . ILE A 457 ? 161.3991 161.3991 161.3991 0.0000 0.0000 0.0000 457 ILE A CB  
3406 C CG1 . ILE A 457 ? 161.6171 161.6171 161.6171 0.0000 0.0000 0.0000 457 ILE A CG1 
3407 C CG2 . ILE A 457 ? 161.5120 161.5120 161.5120 0.0000 0.0000 0.0000 457 ILE A CG2 
3408 C CD1 . ILE A 457 ? 161.6784 161.6784 161.6784 0.0000 0.0000 0.0000 457 ILE A CD1 
3409 N N   . ASN A 458 ? 161.2448 161.2448 161.2448 0.0000 0.0000 0.0000 458 ASN A N   
3410 C CA  . ASN A 458 ? 161.3137 161.3137 161.3137 0.0000 0.0000 0.0000 458 ASN A CA  
3411 C C   . ASN A 458 ? 161.4102 161.4102 161.4102 0.0000 0.0000 0.0000 458 ASN A C   
3412 O O   . ASN A 458 ? 161.6488 161.6488 161.6488 0.0000 0.0000 0.0000 458 ASN A O   
3413 C CB  . ASN A 458 ? 161.4292 161.4292 161.4292 0.0000 0.0000 0.0000 458 ASN A CB  
3414 C CG  . ASN A 458 ? 161.4234 161.4234 161.4234 0.0000 0.0000 0.0000 458 ASN A CG  
3415 O OD1 . ASN A 458 ? 161.5053 161.5053 161.5053 0.0000 0.0000 0.0000 458 ASN A OD1 
3416 N ND2 . ASN A 458 ? 161.4378 161.4378 161.4378 0.0000 0.0000 0.0000 458 ASN A ND2 
3417 N N   . PRO A 459 ? 161.2580 161.2580 161.2580 0.0000 0.0000 0.0000 459 PRO A N   
3418 C CA  . PRO A 459 ? 161.3437 161.3437 161.3437 0.0000 0.0000 0.0000 459 PRO A CA  
3419 C C   . PRO A 459 ? 161.3716 161.3716 161.3716 0.0000 0.0000 0.0000 459 PRO A C   
3420 O O   . PRO A 459 ? 161.5787 161.5787 161.5787 0.0000 0.0000 0.0000 459 PRO A O   
3421 C CB  . PRO A 459 ? 161.3551 161.3551 161.3551 0.0000 0.0000 0.0000 459 PRO A CB  
3422 C CG  . PRO A 459 ? 161.4170 161.4170 161.4170 0.0000 0.0000 0.0000 459 PRO A CG  
3423 C CD  . PRO A 459 ? 161.3829 161.3829 161.3829 0.0000 0.0000 0.0000 459 PRO A CD  
3424 N N   . THR A 460 ? 161.4000 161.4000 161.4000 0.0000 0.0000 0.0000 460 THR A N   
3425 C CA  . THR A 460 ? 161.3190 161.3190 161.3190 0.0000 0.0000 0.0000 460 THR A CA  
3426 C C   . THR A 460 ? 161.3902 161.3902 161.3902 0.0000 0.0000 0.0000 460 THR A C   
3427 O O   . THR A 460 ? 161.6941 161.6941 161.6941 0.0000 0.0000 0.0000 460 THR A O   
3428 C CB  . THR A 460 ? 161.4449 161.4449 161.4449 0.0000 0.0000 0.0000 460 THR A CB  
3429 O OG1 . THR A 460 ? 161.6004 161.6004 161.6004 0.0000 0.0000 0.0000 460 THR A OG1 
3430 C CG2 . THR A 460 ? 161.5820 161.5820 161.5820 0.0000 0.0000 0.0000 460 THR A CG2 
3431 N N   . PHE A 461 ? 161.3490 161.3490 161.3490 0.0000 0.0000 0.0000 461 PHE A N   
3432 C CA  . PHE A 461 ? 161.3407 161.3407 161.3407 0.0000 0.0000 0.0000 461 PHE A CA  
3433 C C   . PHE A 461 ? 161.3303 161.3303 161.3303 0.0000 0.0000 0.0000 461 PHE A C   
3434 O O   . PHE A 461 ? 161.5377 161.5377 161.5377 0.0000 0.0000 0.0000 461 PHE A O   
3435 C CB  . PHE A 461 ? 161.4414 161.4414 161.4414 0.0000 0.0000 0.0000 461 PHE A CB  
3436 C CG  . PHE A 461 ? 161.3358 161.3358 161.3358 0.0000 0.0000 0.0000 461 PHE A CG  
3437 C CD1 . PHE A 461 ? 161.3860 161.3860 161.3860 0.0000 0.0000 0.0000 461 PHE A CD1 
3438 C CD2 . PHE A 461 ? 161.4283 161.4283 161.4283 0.0000 0.0000 0.0000 461 PHE A CD2 
3439 C CE1 . PHE A 461 ? 161.4799 161.4799 161.4799 0.0000 0.0000 0.0000 461 PHE A CE1 
3440 C CE2 . PHE A 461 ? 161.4166 161.4166 161.4166 0.0000 0.0000 0.0000 461 PHE A CE2 
3441 C CZ  . PHE A 461 ? 161.4274 161.4274 161.4274 0.0000 0.0000 0.0000 461 PHE A CZ  
3442 N N   . ILE A 462 ? 161.3327 161.3327 161.3327 0.0000 0.0000 0.0000 462 ILE A N   
3443 C CA  . ILE A 462 ? 161.3248 161.3248 161.3248 0.0000 0.0000 0.0000 462 ILE A CA  
3444 C C   . ILE A 462 ? 161.3946 161.3946 161.3946 0.0000 0.0000 0.0000 462 ILE A C   
3445 O O   . ILE A 462 ? 161.7088 161.7088 161.7088 0.0000 0.0000 0.0000 462 ILE A O   
3446 C CB  . ILE A 462 ? 161.3491 161.3491 161.3491 0.0000 0.0000 0.0000 462 ILE A CB  
3447 C CG1 . ILE A 462 ? 161.3832 161.3832 161.3832 0.0000 0.0000 0.0000 462 ILE A CG1 
3448 C CG2 . ILE A 462 ? 161.7437 161.7437 161.7437 0.0000 0.0000 0.0000 462 ILE A CG2 
3449 C CD1 . ILE A 462 ? 161.7560 161.7560 161.7560 0.0000 0.0000 0.0000 462 ILE A CD1 
3450 N N   . CYS A 463 ? 161.3652 161.3652 161.3652 0.0000 0.0000 0.0000 463 CYS A N   
3451 C CA  . CYS A 463 ? 161.3599 161.3599 161.3599 0.0000 0.0000 0.0000 463 CYS A CA  
3452 C C   . CYS A 463 ? 161.6296 161.6296 161.6296 0.0000 0.0000 0.0000 463 CYS A C   
3453 O O   . CYS A 463 ? 162.2840 162.2840 162.2840 0.0000 0.0000 0.0000 463 CYS A O   
3454 C CB  . CYS A 463 ? 161.4657 161.4657 161.4657 0.0000 0.0000 0.0000 463 CYS A CB  
3455 S SG  . CYS A 463 ? 161.2840 161.2840 161.2840 0.0000 0.0000 0.0000 463 CYS A SG  
3456 N N   . ASP A 464 ? 164.1609 164.1609 164.1609 0.0000 0.0000 0.0000 464 ASP A N   
3457 C CA  . ASP A 464 ? 164.2019 164.2019 164.2019 0.0000 0.0000 0.0000 464 ASP A CA  
3458 C C   . ASP A 464 ? 164.2602 164.2602 164.2602 0.0000 0.0000 0.0000 464 ASP A C   
3459 O O   . ASP A 464 ? 164.6312 164.6312 164.6312 0.0000 0.0000 0.0000 464 ASP A O   
3460 C CB  . ASP A 464 ? 164.5653 164.5653 164.5653 0.0000 0.0000 0.0000 464 ASP A CB  
3461 C CG  . ASP A 464 ? 164.7512 164.7512 164.7512 0.0000 0.0000 0.0000 464 ASP A CG  
3462 O OD1 . ASP A 464 ? 164.5967 164.5967 164.5967 0.0000 0.0000 0.0000 464 ASP A OD1 
3463 O OD2 . ASP A 464 ? 165.0043 165.0043 165.0043 0.0000 0.0000 0.0000 464 ASP A OD2 
3464 N N   . HIS A 465 ? 161.6322 161.6322 161.6322 0.0000 0.0000 0.0000 465 HIS A N   
3465 C CA  . HIS A 465 ? 161.7834 161.7834 161.7834 0.0000 0.0000 0.0000 465 HIS A CA  
3466 C C   . HIS A 465 ? 161.7931 161.7931 161.7931 0.0000 0.0000 0.0000 465 HIS A C   
3467 O O   . HIS A 465 ? 162.0983 162.0983 162.0983 0.0000 0.0000 0.0000 465 HIS A O   
3468 C CB  . HIS A 465 ? 161.8068 161.8068 161.8068 0.0000 0.0000 0.0000 465 HIS A CB  
3469 C CG  . HIS A 465 ? 161.6188 161.6188 161.6188 0.0000 0.0000 0.0000 465 HIS A CG  
3470 N ND1 . HIS A 465 ? 161.7149 161.7149 161.7149 0.0000 0.0000 0.0000 465 HIS A ND1 
3471 C CD2 . HIS A 465 ? 161.6836 161.6836 161.6836 0.0000 0.0000 0.0000 465 HIS A CD2 
3472 C CE1 . HIS A 465 ? 161.6529 161.6529 161.6529 0.0000 0.0000 0.0000 465 HIS A CE1 
3473 N NE2 . HIS A 465 ? 161.6039 161.6039 161.6039 0.0000 0.0000 0.0000 465 HIS A NE2 
3474 N N   . PRO A 466 ? 168.6665 168.6665 168.6665 0.0000 0.0000 0.0000 466 PRO A N   
3475 C CA  . PRO A 466 ? 169.0572 169.0572 169.0572 0.0000 0.0000 0.0000 466 PRO A CA  
3476 C C   . PRO A 466 ? 169.8144 169.8144 169.8144 0.0000 0.0000 0.0000 466 PRO A C   
3477 O O   . PRO A 466 ? 170.0099 170.0099 170.0099 0.0000 0.0000 0.0000 466 PRO A O   
3478 C CB  . PRO A 466 ? 169.6097 169.6097 169.6097 0.0000 0.0000 0.0000 466 PRO A CB  
3479 C CG  . PRO A 466 ? 169.6033 169.6033 169.6033 0.0000 0.0000 0.0000 466 PRO A CG  
3480 C CD  . PRO A 466 ? 169.2741 169.2741 169.2741 0.0000 0.0000 0.0000 466 PRO A CD  
3481 N N   . GLN A 467 ? 184.4719 184.4719 184.4719 0.0000 0.0000 0.0000 467 GLN A N   
3482 C CA  . GLN A 467 ? 184.8870 184.8870 184.8870 0.0000 0.0000 0.0000 467 GLN A CA  
3483 C C   . GLN A 467 ? 185.4554 185.4554 185.4554 0.0000 0.0000 0.0000 467 GLN A C   
3484 O O   . GLN A 467 ? 185.6593 185.6593 185.6593 0.0000 0.0000 0.0000 467 GLN A O   
3485 C CB  . GLN A 467 ? 184.9080 184.9080 184.9080 0.0000 0.0000 0.0000 467 GLN A CB  
3486 C CG  . GLN A 467 ? 185.1716 185.1716 185.1716 0.0000 0.0000 0.0000 467 GLN A CG  
3487 C CD  . GLN A 467 ? 185.0584 185.0584 185.0584 0.0000 0.0000 0.0000 467 GLN A CD  
3488 O OE1 . GLN A 467 ? 184.8837 184.8837 184.8837 0.0000 0.0000 0.0000 467 GLN A OE1 
3489 N NE2 . GLN A 467 ? 184.8665 184.8665 184.8665 0.0000 0.0000 0.0000 467 GLN A NE2 
3490 N N   . ILE A 468 ? 192.7675 192.7675 192.7675 0.0000 0.0000 0.0000 468 ILE A N   
3491 C CA  . ILE A 468 ? 193.0333 193.0333 193.0333 0.0000 0.0000 0.0000 468 ILE A CA  
3492 C C   . ILE A 468 ? 193.2694 193.2694 193.2694 0.0000 0.0000 0.0000 468 ILE A C   
3493 O O   . ILE A 468 ? 193.4437 193.4437 193.4437 0.0000 0.0000 0.0000 468 ILE A O   
3494 C CB  . ILE A 468 ? 193.1311 193.1311 193.1311 0.0000 0.0000 0.0000 468 ILE A CB  
3495 C CG1 . ILE A 468 ? 193.0313 193.0313 193.0313 0.0000 0.0000 0.0000 468 ILE A CG1 
3496 C CG2 . ILE A 468 ? 193.6242 193.6242 193.6242 0.0000 0.0000 0.0000 468 ILE A CG2 
3497 C CD1 . ILE A 468 ? 193.8558 193.8558 193.8558 0.0000 0.0000 0.0000 468 ILE A CD1 
3498 N N   . MET A 469 ? 200.8207 200.8207 200.8207 0.0000 0.0000 0.0000 469 MET A N   
3499 C CA  . MET A 469 ? 201.2251 201.2251 201.2251 0.0000 0.0000 0.0000 469 MET A CA  
3500 C C   . MET A 469 ? 201.2190 201.2190 201.2190 0.0000 0.0000 0.0000 469 MET A C   
3501 O O   . MET A 469 ? 200.4950 200.4950 200.4950 0.0000 0.0000 0.0000 469 MET A O   
3502 C CB  . MET A 469 ? 201.0996 201.0996 201.0996 0.0000 0.0000 0.0000 469 MET A CB  
3503 C CG  . MET A 469 ? 201.3597 201.3597 201.3597 0.0000 0.0000 0.0000 469 MET A CG  
3504 S SD  . MET A 469 ? 201.2707 201.2707 201.2707 0.0000 0.0000 0.0000 469 MET A SD  
3505 C CE  . MET A 469 ? 201.3739 201.3739 201.3739 0.0000 0.0000 0.0000 469 MET A CE  
3506 N N   . SER A 470 ? 196.3955 196.3955 196.3955 0.0000 0.0000 0.0000 470 SER A N   
3507 C CA  . SER A 470 ? 196.3423 196.3423 196.3423 0.0000 0.0000 0.0000 470 SER A CA  
3508 C C   . SER A 470 ? 196.3651 196.3651 196.3651 0.0000 0.0000 0.0000 470 SER A C   
3509 O O   . SER A 470 ? 196.1565 196.1565 196.1565 0.0000 0.0000 0.0000 470 SER A O   
3510 C CB  . SER A 470 ? 196.0557 196.0557 196.0557 0.0000 0.0000 0.0000 470 SER A CB  
3511 O OG  . SER A 470 ? 195.7146 195.7146 195.7146 0.0000 0.0000 0.0000 470 SER A OG  
3512 N N   . PRO A 471 ? 194.5580 194.5580 194.5580 0.0000 0.0000 0.0000 471 PRO A N   
3513 C CA  . PRO A 471 ? 194.6125 194.6125 194.6125 0.0000 0.0000 0.0000 471 PRO A CA  
3514 C C   . PRO A 471 ? 194.4302 194.4302 194.4302 0.0000 0.0000 0.0000 471 PRO A C   
3515 O O   . PRO A 471 ? 194.4432 194.4432 194.4432 0.0000 0.0000 0.0000 471 PRO A O   
3516 C CB  . PRO A 471 ? 194.2059 194.2059 194.2059 0.0000 0.0000 0.0000 471 PRO A CB  
3517 C CG  . PRO A 471 ? 193.2899 193.2899 193.2899 0.0000 0.0000 0.0000 471 PRO A CG  
3518 C CD  . PRO A 471 ? 193.6986 193.6986 193.6986 0.0000 0.0000 0.0000 471 PRO A CD  
3519 N N   . LEU A 472 ? 192.9024 192.9024 192.9024 0.0000 0.0000 0.0000 472 LEU A N   
3520 C CA  . LEU A 472 ? 192.7262 192.7262 192.7262 0.0000 0.0000 0.0000 472 LEU A CA  
3521 C C   . LEU A 472 ? 192.3814 192.3814 192.3814 0.0000 0.0000 0.0000 472 LEU A C   
3522 O O   . LEU A 472 ? 192.2764 192.2764 192.2764 0.0000 0.0000 0.0000 472 LEU A O   
3523 C CB  . LEU A 472 ? 193.0826 193.0826 193.0826 0.0000 0.0000 0.0000 472 LEU A CB  
3524 C CG  . LEU A 472 ? 193.0959 193.0959 193.0959 0.0000 0.0000 0.0000 472 LEU A CG  
3525 C CD1 . LEU A 472 ? 191.8622 191.8622 191.8622 0.0000 0.0000 0.0000 472 LEU A CD1 
3526 C CD2 . LEU A 472 ? 192.4301 192.4301 192.4301 0.0000 0.0000 0.0000 472 LEU A CD2 
3527 N N   . ALA A 473 ? 163.1306 163.1306 163.1306 0.0000 0.0000 0.0000 473 ALA A N   
3528 C CA  . ALA A 473 ? 162.0529 162.0529 162.0529 0.0000 0.0000 0.0000 473 ALA A CA  
3529 C C   . ALA A 473 ? 161.6159 161.6159 161.6159 0.0000 0.0000 0.0000 473 ALA A C   
3530 O O   . ALA A 473 ? 161.8652 161.8652 161.8652 0.0000 0.0000 0.0000 473 ALA A O   
3531 C CB  . ALA A 473 ? 162.0386 162.0386 162.0386 0.0000 0.0000 0.0000 473 ALA A CB  
3532 N N   . LYS A 474 ? 161.2472 161.2472 161.2472 0.0000 0.0000 0.0000 474 LYS A N   
3533 C CA  . LYS A 474 ? 161.1783 161.1783 161.1783 0.0000 0.0000 0.0000 474 LYS A CA  
3534 C C   . LYS A 474 ? 161.3464 161.3464 161.3464 0.0000 0.0000 0.0000 474 LYS A C   
3535 O O   . LYS A 474 ? 161.7458 161.7458 161.7458 0.0000 0.0000 0.0000 474 LYS A O   
3536 C CB  . LYS A 474 ? 161.4170 161.4170 161.4170 0.0000 0.0000 0.0000 474 LYS A CB  
3537 C CG  . LYS A 474 ? 161.4644 161.4644 161.4644 0.0000 0.0000 0.0000 474 LYS A CG  
3538 C CD  . LYS A 474 ? 161.4667 161.4667 161.4667 0.0000 0.0000 0.0000 474 LYS A CD  
3539 C CE  . LYS A 474 ? 161.2678 161.2678 161.2678 0.0000 0.0000 0.0000 474 LYS A CE  
3540 N NZ  . LYS A 474 ? 161.4097 161.4097 161.4097 0.0000 0.0000 0.0000 474 LYS A NZ  
3541 N N   . TRP A 475 ? 161.2569 161.2569 161.2569 0.0000 0.0000 0.0000 475 TRP A N   
3542 C CA  . TRP A 475 ? 161.4330 161.4330 161.4330 0.0000 0.0000 0.0000 475 TRP A CA  
3543 C C   . TRP A 475 ? 161.4289 161.4289 161.4289 0.0000 0.0000 0.0000 475 TRP A C   
3544 O O   . TRP A 475 ? 161.5911 161.5911 161.5911 0.0000 0.0000 0.0000 475 TRP A O   
3545 C CB  . TRP A 475 ? 161.5971 161.5971 161.5971 0.0000 0.0000 0.0000 475 TRP A CB  
3546 C CG  . TRP A 475 ? 161.5718 161.5718 161.5718 0.0000 0.0000 0.0000 475 TRP A CG  
3547 C CD1 . TRP A 475 ? 161.5356 161.5356 161.5356 0.0000 0.0000 0.0000 475 TRP A CD1 
3548 C CD2 . TRP A 475 ? 161.5873 161.5873 161.5873 0.0000 0.0000 0.0000 475 TRP A CD2 
3549 N NE1 . TRP A 475 ? 161.4660 161.4660 161.4660 0.0000 0.0000 0.0000 475 TRP A NE1 
3550 C CE2 . TRP A 475 ? 161.5241 161.5241 161.5241 0.0000 0.0000 0.0000 475 TRP A CE2 
3551 C CE3 . TRP A 475 ? 161.6116 161.6116 161.6116 0.0000 0.0000 0.0000 475 TRP A CE3 
3552 C CZ2 . TRP A 475 ? 161.6852 161.6852 161.6852 0.0000 0.0000 0.0000 475 TRP A CZ2 
3553 C CZ3 . TRP A 475 ? 161.5112 161.5112 161.5112 0.0000 0.0000 0.0000 475 TRP A CZ3 
3554 C CH2 . TRP A 475 ? 161.5671 161.5671 161.5671 0.0000 0.0000 0.0000 475 TRP A CH2 
3555 N N   . HIS A 476 ? 161.5415 161.5415 161.5415 0.0000 0.0000 0.0000 476 HIS A N   
3556 C CA  . HIS A 476 ? 161.5140 161.5140 161.5140 0.0000 0.0000 0.0000 476 HIS A CA  
3557 C C   . HIS A 476 ? 161.5029 161.5029 161.5029 0.0000 0.0000 0.0000 476 HIS A C   
3558 O O   . HIS A 476 ? 161.6021 161.6021 161.6021 0.0000 0.0000 0.0000 476 HIS A O   
3559 C CB  . HIS A 476 ? 161.6376 161.6376 161.6376 0.0000 0.0000 0.0000 476 HIS A CB  
3560 C CG  . HIS A 476 ? 161.5553 161.5553 161.5553 0.0000 0.0000 0.0000 476 HIS A CG  
3561 N ND1 . HIS A 476 ? 161.7910 161.7910 161.7910 0.0000 0.0000 0.0000 476 HIS A ND1 
3562 C CD2 . HIS A 476 ? 161.5205 161.5205 161.5205 0.0000 0.0000 0.0000 476 HIS A CD2 
3563 C CE1 . HIS A 476 ? 161.7115 161.7115 161.7115 0.0000 0.0000 0.0000 476 HIS A CE1 
3564 N NE2 . HIS A 476 ? 161.5346 161.5346 161.5346 0.0000 0.0000 0.0000 476 HIS A NE2 
3565 N N   . ARG A 477 ? 161.4354 161.4354 161.4354 0.0000 0.0000 0.0000 477 ARG A N   
3566 C CA  . ARG A 477 ? 161.3849 161.3849 161.3849 0.0000 0.0000 0.0000 477 ARG A CA  
3567 C C   . ARG A 477 ? 161.4369 161.4369 161.4369 0.0000 0.0000 0.0000 477 ARG A C   
3568 O O   . ARG A 477 ? 161.4724 161.4724 161.4724 0.0000 0.0000 0.0000 477 ARG A O   
3569 C CB  . ARG A 477 ? 161.5037 161.5037 161.5037 0.0000 0.0000 0.0000 477 ARG A CB  
3570 C CG  . ARG A 477 ? 161.4538 161.4538 161.4538 0.0000 0.0000 0.0000 477 ARG A CG  
3571 C CD  . ARG A 477 ? 161.4727 161.4727 161.4727 0.0000 0.0000 0.0000 477 ARG A CD  
3572 N NE  . ARG A 477 ? 161.4852 161.4852 161.4852 0.0000 0.0000 0.0000 477 ARG A NE  
3573 C CZ  . ARG A 477 ? 161.3534 161.3534 161.3534 0.0000 0.0000 0.0000 477 ARG A CZ  
3574 N NH1 . ARG A 477 ? 161.3614 161.3614 161.3614 0.0000 0.0000 0.0000 477 ARG A NH1 
3575 N NH2 . ARG A 477 ? 161.4058 161.4058 161.4058 0.0000 0.0000 0.0000 477 ARG A NH2 
3576 N N   . SER A 478 ? 162.2434 162.2434 162.2434 0.0000 0.0000 0.0000 478 SER A N   
3577 C CA  . SER A 478 ? 162.2545 162.2545 162.2545 0.0000 0.0000 0.0000 478 SER A CA  
3578 C C   . SER A 478 ? 162.5226 162.5226 162.5226 0.0000 0.0000 0.0000 478 SER A C   
3579 O O   . SER A 478 ? 162.5620 162.5620 162.5620 0.0000 0.0000 0.0000 478 SER A O   
3580 C CB  . SER A 478 ? 162.2872 162.2872 162.2872 0.0000 0.0000 0.0000 478 SER A CB  
3581 O OG  . SER A 478 ? 162.1762 162.1762 162.1762 0.0000 0.0000 0.0000 478 SER A OG  
3582 N N   . LYS A 479 ? 174.4790 174.4790 174.4790 0.0000 0.0000 0.0000 479 LYS A N   
3583 C CA  . LYS A 479 ? 175.3647 175.3647 175.3647 0.0000 0.0000 0.0000 479 LYS A CA  
3584 C C   . LYS A 479 ? 176.0147 176.0147 176.0147 0.0000 0.0000 0.0000 479 LYS A C   
3585 O O   . LYS A 479 ? 175.4258 175.4258 175.4258 0.0000 0.0000 0.0000 479 LYS A O   
3586 C CB  . LYS A 479 ? 175.1654 175.1654 175.1654 0.0000 0.0000 0.0000 479 LYS A CB  
3587 C CG  . LYS A 479 ? 174.8761 174.8761 174.8761 0.0000 0.0000 0.0000 479 LYS A CG  
3588 C CD  . LYS A 479 ? 174.9864 174.9864 174.9864 0.0000 0.0000 0.0000 479 LYS A CD  
3589 C CE  . LYS A 479 ? 175.1320 175.1320 175.1320 0.0000 0.0000 0.0000 479 LYS A CE  
3590 N NZ  . LYS A 479 ? 175.2204 175.2204 175.2204 0.0000 0.0000 0.0000 479 LYS A NZ  
3591 N N   . GLU A 480 ? 203.0236 203.0236 203.0236 0.0000 0.0000 0.0000 480 GLU A N   
3592 C CA  . GLU A 480 ? 203.4766 203.4766 203.4766 0.0000 0.0000 0.0000 480 GLU A CA  
3593 C C   . GLU A 480 ? 203.3093 203.3093 203.3093 0.0000 0.0000 0.0000 480 GLU A C   
3594 O O   . GLU A 480 ? 203.6940 203.6940 203.6940 0.0000 0.0000 0.0000 480 GLU A O   
3595 C CB  . GLU A 480 ? 203.9984 203.9984 203.9984 0.0000 0.0000 0.0000 480 GLU A CB  
3596 C CG  . GLU A 480 ? 204.5305 204.5305 204.5305 0.0000 0.0000 0.0000 480 GLU A CG  
3597 C CD  . GLU A 480 ? 204.6230 204.6230 204.6230 0.0000 0.0000 0.0000 480 GLU A CD  
3598 O OE1 . GLU A 480 ? 204.0826 204.0826 204.0826 0.0000 0.0000 0.0000 480 GLU A OE1 
3599 O OE2 . GLU A 480 ? 205.0666 205.0666 205.0666 0.0000 0.0000 0.0000 480 GLU A OE2 
3600 N N   . GLY A 481 ? 179.8756 179.8756 179.8756 0.0000 0.0000 0.0000 481 GLY A N   
3601 C CA  . GLY A 481 ? 179.6460 179.6460 179.6460 0.0000 0.0000 0.0000 481 GLY A CA  
3602 C C   . GLY A 481 ? 178.7657 178.7657 178.7657 0.0000 0.0000 0.0000 481 GLY A C   
3603 O O   . GLY A 481 ? 178.8415 178.8415 178.8415 0.0000 0.0000 0.0000 481 GLY A O   
3604 N N   . LEU A 482 ? 163.8119 163.8119 163.8119 0.0000 0.0000 0.0000 482 LEU A N   
3605 C CA  . LEU A 482 ? 163.0734 163.0734 163.0734 0.0000 0.0000 0.0000 482 LEU A CA  
3606 C C   . LEU A 482 ? 162.7942 162.7942 162.7942 0.0000 0.0000 0.0000 482 LEU A C   
3607 O O   . LEU A 482 ? 162.8239 162.8239 162.8239 0.0000 0.0000 0.0000 482 LEU A O   
3608 C CB  . LEU A 482 ? 162.9289 162.9289 162.9289 0.0000 0.0000 0.0000 482 LEU A CB  
3609 C CG  . LEU A 482 ? 163.3258 163.3258 163.3258 0.0000 0.0000 0.0000 482 LEU A CG  
3610 C CD1 . LEU A 482 ? 163.0281 163.0281 163.0281 0.0000 0.0000 0.0000 482 LEU A CD1 
3611 C CD2 . LEU A 482 ? 163.2931 163.2931 163.2931 0.0000 0.0000 0.0000 482 LEU A CD2 
3612 N N   . THR A 483 ? 161.7105 161.7105 161.7105 0.0000 0.0000 0.0000 483 THR A N   
3613 C CA  . THR A 483 ? 161.2935 161.2935 161.2935 0.0000 0.0000 0.0000 483 THR A CA  
3614 C C   . THR A 483 ? 161.3242 161.3242 161.3242 0.0000 0.0000 0.0000 483 THR A C   
3615 O O   . THR A 483 ? 161.5848 161.5848 161.5848 0.0000 0.0000 0.0000 483 THR A O   
3616 C CB  . THR A 483 ? 161.6986 161.6986 161.6986 0.0000 0.0000 0.0000 483 THR A CB  
3617 O OG1 . THR A 483 ? 161.6833 161.6833 161.6833 0.0000 0.0000 0.0000 483 THR A OG1 
3618 C CG2 . THR A 483 ? 161.8454 161.8454 161.8454 0.0000 0.0000 0.0000 483 THR A CG2 
3619 N N   . GLU A 484 ? 161.2807 161.2807 161.2807 0.0000 0.0000 0.0000 484 GLU A N   
3620 C CA  . GLU A 484 ? 161.3151 161.3151 161.3151 0.0000 0.0000 0.0000 484 GLU A CA  
3621 C C   . GLU A 484 ? 161.3572 161.3572 161.3572 0.0000 0.0000 0.0000 484 GLU A C   
3622 O O   . GLU A 484 ? 161.4832 161.4832 161.4832 0.0000 0.0000 0.0000 484 GLU A O   
3623 C CB  . GLU A 484 ? 161.4843 161.4843 161.4843 0.0000 0.0000 0.0000 484 GLU A CB  
3624 C CG  . GLU A 484 ? 161.4757 161.4757 161.4757 0.0000 0.0000 0.0000 484 GLU A CG  
3625 C CD  . GLU A 484 ? 161.4040 161.4040 161.4040 0.0000 0.0000 0.0000 484 GLU A CD  
3626 O OE1 . GLU A 484 ? 161.3804 161.3804 161.3804 0.0000 0.0000 0.0000 484 GLU A OE1 
3627 O OE2 . GLU A 484 ? 161.5441 161.5441 161.5441 0.0000 0.0000 0.0000 484 GLU A OE2 
3628 N N   . ARG A 485 ? 161.3026 161.3026 161.3026 0.0000 0.0000 0.0000 485 ARG A N   
3629 C CA  . ARG A 485 ? 161.2311 161.2311 161.2311 0.0000 0.0000 0.0000 485 ARG A CA  
3630 C C   . ARG A 485 ? 161.1655 161.1655 161.1655 0.0000 0.0000 0.0000 485 ARG A C   
3631 O O   . ARG A 485 ? 161.5032 161.5032 161.5032 0.0000 0.0000 0.0000 485 ARG A O   
3632 C CB  . ARG A 485 ? 161.4173 161.4173 161.4173 0.0000 0.0000 0.0000 485 ARG A CB  
3633 C CG  . ARG A 485 ? 161.5010 161.5010 161.5010 0.0000 0.0000 0.0000 485 ARG A CG  
3634 C CD  . ARG A 485 ? 161.6395 161.6395 161.6395 0.0000 0.0000 0.0000 485 ARG A CD  
3635 N NE  . ARG A 485 ? 161.5441 161.5441 161.5441 0.0000 0.0000 0.0000 485 ARG A NE  
3636 C CZ  . ARG A 485 ? 161.6365 161.6365 161.6365 0.0000 0.0000 0.0000 485 ARG A CZ  
3637 N NH1 . ARG A 485 ? 161.7712 161.7712 161.7712 0.0000 0.0000 0.0000 485 ARG A NH1 
3638 N NH2 . ARG A 485 ? 161.5904 161.5904 161.5904 0.0000 0.0000 0.0000 485 ARG A NH2 
3639 N N   . PHE A 486 ? 161.0247 161.0247 161.0247 0.0000 0.0000 0.0000 486 PHE A N   
3640 C CA  . PHE A 486 ? 161.1456 161.1456 161.1456 0.0000 0.0000 0.0000 486 PHE A CA  
3641 C C   . PHE A 486 ? 161.3014 161.3014 161.3014 0.0000 0.0000 0.0000 486 PHE A C   
3642 O O   . PHE A 486 ? 161.5563 161.5563 161.5563 0.0000 0.0000 0.0000 486 PHE A O   
3643 C CB  . PHE A 486 ? 161.3482 161.3482 161.3482 0.0000 0.0000 0.0000 486 PHE A CB  
3644 C CG  . PHE A 486 ? 161.2382 161.2382 161.2382 0.0000 0.0000 0.0000 486 PHE A CG  
3645 C CD1 . PHE A 486 ? 161.3078 161.3078 161.3078 0.0000 0.0000 0.0000 486 PHE A CD1 
3646 C CD2 . PHE A 486 ? 161.4194 161.4194 161.4194 0.0000 0.0000 0.0000 486 PHE A CD2 
3647 C CE1 . PHE A 486 ? 161.3832 161.3832 161.3832 0.0000 0.0000 0.0000 486 PHE A CE1 
3648 C CE2 . PHE A 486 ? 161.4336 161.4336 161.4336 0.0000 0.0000 0.0000 486 PHE A CE2 
3649 C CZ  . PHE A 486 ? 161.3916 161.3916 161.3916 0.0000 0.0000 0.0000 486 PHE A CZ  
3650 N N   . GLU A 487 ? 161.3302 161.3302 161.3302 0.0000 0.0000 0.0000 487 GLU A N   
3651 C CA  . GLU A 487 ? 161.2820 161.2820 161.2820 0.0000 0.0000 0.0000 487 GLU A CA  
3652 C C   . GLU A 487 ? 161.2614 161.2614 161.2614 0.0000 0.0000 0.0000 487 GLU A C   
3653 O O   . GLU A 487 ? 161.5190 161.5190 161.5190 0.0000 0.0000 0.0000 487 GLU A O   
3654 C CB  . GLU A 487 ? 161.3229 161.3229 161.3229 0.0000 0.0000 0.0000 487 GLU A CB  
3655 C CG  . GLU A 487 ? 161.4599 161.4599 161.4599 0.0000 0.0000 0.0000 487 GLU A CG  
3656 C CD  . GLU A 487 ? 161.4548 161.4548 161.4548 0.0000 0.0000 0.0000 487 GLU A CD  
3657 O OE1 . GLU A 487 ? 161.4530 161.4530 161.4530 0.0000 0.0000 0.0000 487 GLU A OE1 
3658 O OE2 . GLU A 487 ? 161.6053 161.6053 161.6053 0.0000 0.0000 0.0000 487 GLU A OE2 
3659 N N   . LEU A 488 ? 161.1906 161.1906 161.1906 0.0000 0.0000 0.0000 488 LEU A N   
3660 C CA  . LEU A 488 ? 161.1912 161.1912 161.1912 0.0000 0.0000 0.0000 488 LEU A CA  
3661 C C   . LEU A 488 ? 161.3660 161.3660 161.3660 0.0000 0.0000 0.0000 488 LEU A C   
3662 O O   . LEU A 488 ? 161.7483 161.7483 161.7483 0.0000 0.0000 0.0000 488 LEU A O   
3663 C CB  . LEU A 488 ? 161.3384 161.3384 161.3384 0.0000 0.0000 0.0000 488 LEU A CB  
3664 C CG  . LEU A 488 ? 161.2774 161.2774 161.2774 0.0000 0.0000 0.0000 488 LEU A CG  
3665 C CD1 . LEU A 488 ? 161.6112 161.6112 161.6112 0.0000 0.0000 0.0000 488 LEU A CD1 
3666 C CD2 . LEU A 488 ? 161.3977 161.3977 161.3977 0.0000 0.0000 0.0000 488 LEU A CD2 
3667 N N   . PHE A 489 ? 161.3470 161.3470 161.3470 0.0000 0.0000 0.0000 489 PHE A N   
3668 C CA  . PHE A 489 ? 161.3768 161.3768 161.3768 0.0000 0.0000 0.0000 489 PHE A CA  
3669 C C   . PHE A 489 ? 161.4408 161.4408 161.4408 0.0000 0.0000 0.0000 489 PHE A C   
3670 O O   . PHE A 489 ? 161.6871 161.6871 161.6871 0.0000 0.0000 0.0000 489 PHE A O   
3671 C CB  . PHE A 489 ? 161.4630 161.4630 161.4630 0.0000 0.0000 0.0000 489 PHE A CB  
3672 C CG  . PHE A 489 ? 161.4539 161.4539 161.4539 0.0000 0.0000 0.0000 489 PHE A CG  
3673 C CD1 . PHE A 489 ? 161.6638 161.6638 161.6638 0.0000 0.0000 0.0000 489 PHE A CD1 
3674 C CD2 . PHE A 489 ? 161.5753 161.5753 161.5753 0.0000 0.0000 0.0000 489 PHE A CD2 
3675 C CE1 . PHE A 489 ? 161.7623 161.7623 161.7623 0.0000 0.0000 0.0000 489 PHE A CE1 
3676 C CE2 . PHE A 489 ? 161.8071 161.8071 161.8071 0.0000 0.0000 0.0000 489 PHE A CE2 
3677 C CZ  . PHE A 489 ? 161.7768 161.7768 161.7768 0.0000 0.0000 0.0000 489 PHE A CZ  
3678 N N   . VAL A 490 ? 161.4134 161.4134 161.4134 0.0000 0.0000 0.0000 490 VAL A N   
3679 C CA  . VAL A 490 ? 161.3064 161.3064 161.3064 0.0000 0.0000 0.0000 490 VAL A CA  
3680 C C   . VAL A 490 ? 161.2727 161.2727 161.2727 0.0000 0.0000 0.0000 490 VAL A C   
3681 O O   . VAL A 490 ? 161.4054 161.4054 161.4054 0.0000 0.0000 0.0000 490 VAL A O   
3682 C CB  . VAL A 490 ? 161.3788 161.3788 161.3788 0.0000 0.0000 0.0000 490 VAL A CB  
3683 C CG1 . VAL A 490 ? 161.5726 161.5726 161.5726 0.0000 0.0000 0.0000 490 VAL A CG1 
3684 C CG2 . VAL A 490 ? 161.4947 161.4947 161.4947 0.0000 0.0000 0.0000 490 VAL A CG2 
3685 N N   . MET A 491 ? 161.2906 161.2906 161.2906 0.0000 0.0000 0.0000 491 MET A N   
3686 C CA  . MET A 491 ? 161.3811 161.3811 161.3811 0.0000 0.0000 0.0000 491 MET A CA  
3687 C C   . MET A 491 ? 161.3725 161.3725 161.3725 0.0000 0.0000 0.0000 491 MET A C   
3688 O O   . MET A 491 ? 161.4950 161.4950 161.4950 0.0000 0.0000 0.0000 491 MET A O   
3689 C CB  . MET A 491 ? 161.3543 161.3543 161.3543 0.0000 0.0000 0.0000 491 MET A CB  
3690 C CG  . MET A 491 ? 161.3856 161.3856 161.3856 0.0000 0.0000 0.0000 491 MET A CG  
3691 S SD  . MET A 491 ? 161.0786 161.0786 161.0786 0.0000 0.0000 0.0000 491 MET A SD  
3692 C CE  . MET A 491 ? 161.5660 161.5660 161.5660 0.0000 0.0000 0.0000 491 MET A CE  
3693 N N   . LYS A 492 ? 161.4946 161.4946 161.4946 0.0000 0.0000 0.0000 492 LYS A N   
3694 C CA  . LYS A 492 ? 161.5091 161.5091 161.5091 0.0000 0.0000 0.0000 492 LYS A CA  
3695 C C   . LYS A 492 ? 161.4280 161.4280 161.4280 0.0000 0.0000 0.0000 492 LYS A C   
3696 O O   . LYS A 492 ? 161.4388 161.4388 161.4388 0.0000 0.0000 0.0000 492 LYS A O   
3697 C CB  . LYS A 492 ? 161.4723 161.4723 161.4723 0.0000 0.0000 0.0000 492 LYS A CB  
3698 C CG  . LYS A 492 ? 161.7832 161.7832 161.7832 0.0000 0.0000 0.0000 492 LYS A CG  
3699 C CD  . LYS A 492 ? 161.9081 161.9081 161.9081 0.0000 0.0000 0.0000 492 LYS A CD  
3700 C CE  . LYS A 492 ? 161.7039 161.7039 161.7039 0.0000 0.0000 0.0000 492 LYS A CE  
3701 N NZ  . LYS A 492 ? 161.4721 161.4721 161.4721 0.0000 0.0000 0.0000 492 LYS A NZ  
3702 N N   . LYS A 493 ? 161.3812 161.3812 161.3812 0.0000 0.0000 0.0000 493 LYS A N   
3703 C CA  . LYS A 493 ? 161.2493 161.2493 161.2493 0.0000 0.0000 0.0000 493 LYS A CA  
3704 C C   . LYS A 493 ? 161.3943 161.3943 161.3943 0.0000 0.0000 0.0000 493 LYS A C   
3705 O O   . LYS A 493 ? 161.6735 161.6735 161.6735 0.0000 0.0000 0.0000 493 LYS A O   
3706 C CB  . LYS A 493 ? 161.4161 161.4161 161.4161 0.0000 0.0000 0.0000 493 LYS A CB  
3707 C CG  . LYS A 493 ? 161.4976 161.4976 161.4976 0.0000 0.0000 0.0000 493 LYS A CG  
3708 C CD  . LYS A 493 ? 161.4709 161.4709 161.4709 0.0000 0.0000 0.0000 493 LYS A CD  
3709 C CE  . LYS A 493 ? 161.3996 161.3996 161.3996 0.0000 0.0000 0.0000 493 LYS A CE  
3710 N NZ  . LYS A 493 ? 161.5182 161.5182 161.5182 0.0000 0.0000 0.0000 493 LYS A NZ  
3711 N N   . GLU A 494 ? 161.4021 161.4021 161.4021 0.0000 0.0000 0.0000 494 GLU A N   
3712 C CA  . GLU A 494 ? 161.3873 161.3873 161.3873 0.0000 0.0000 0.0000 494 GLU A CA  
3713 C C   . GLU A 494 ? 161.3420 161.3420 161.3420 0.0000 0.0000 0.0000 494 GLU A C   
3714 O O   . GLU A 494 ? 161.5650 161.5650 161.5650 0.0000 0.0000 0.0000 494 GLU A O   
3715 C CB  . GLU A 494 ? 161.4105 161.4105 161.4105 0.0000 0.0000 0.0000 494 GLU A CB  
3716 C CG  . GLU A 494 ? 161.5336 161.5336 161.5336 0.0000 0.0000 0.0000 494 GLU A CG  
3717 C CD  . GLU A 494 ? 161.5567 161.5567 161.5567 0.0000 0.0000 0.0000 494 GLU A CD  
3718 O OE1 . GLU A 494 ? 161.5505 161.5505 161.5505 0.0000 0.0000 0.0000 494 GLU A OE1 
3719 O OE2 . GLU A 494 ? 161.5566 161.5566 161.5566 0.0000 0.0000 0.0000 494 GLU A OE2 
3720 N N   . ILE A 495 ? 161.2793 161.2793 161.2793 0.0000 0.0000 0.0000 495 ILE A N   
3721 C CA  . ILE A 495 ? 161.3243 161.3243 161.3243 0.0000 0.0000 0.0000 495 ILE A CA  
3722 C C   . ILE A 495 ? 161.4362 161.4362 161.4362 0.0000 0.0000 0.0000 495 ILE A C   
3723 O O   . ILE A 495 ? 161.5898 161.5898 161.5898 0.0000 0.0000 0.0000 495 ILE A O   
3724 C CB  . ILE A 495 ? 161.3536 161.3536 161.3536 0.0000 0.0000 0.0000 495 ILE A CB  
3725 C CG1 . ILE A 495 ? 161.4917 161.4917 161.4917 0.0000 0.0000 0.0000 495 ILE A CG1 
3726 C CG2 . ILE A 495 ? 161.4695 161.4695 161.4695 0.0000 0.0000 0.0000 495 ILE A CG2 
3727 C CD1 . ILE A 495 ? 161.5552 161.5552 161.5552 0.0000 0.0000 0.0000 495 ILE A CD1 
3728 N N   . CYS A 496 ? 161.4923 161.4923 161.4923 0.0000 0.0000 0.0000 496 CYS A N   
3729 C CA  . CYS A 496 ? 161.4171 161.4171 161.4171 0.0000 0.0000 0.0000 496 CYS A CA  
3730 C C   . CYS A 496 ? 161.3392 161.3392 161.3392 0.0000 0.0000 0.0000 496 CYS A C   
3731 O O   . CYS A 496 ? 161.4691 161.4691 161.4691 0.0000 0.0000 0.0000 496 CYS A O   
3732 C CB  . CYS A 496 ? 161.4104 161.4104 161.4104 0.0000 0.0000 0.0000 496 CYS A CB  
3733 S SG  . CYS A 496 ? 161.3026 161.3026 161.3026 0.0000 0.0000 0.0000 496 CYS A SG  
3734 N N   . ASN A 497 ? 161.2825 161.2825 161.2825 0.0000 0.0000 0.0000 497 ASN A N   
3735 C CA  . ASN A 497 ? 161.2571 161.2571 161.2571 0.0000 0.0000 0.0000 497 ASN A CA  
3736 C C   . ASN A 497 ? 161.3555 161.3555 161.3555 0.0000 0.0000 0.0000 497 ASN A C   
3737 O O   . ASN A 497 ? 161.6038 161.6038 161.6038 0.0000 0.0000 0.0000 497 ASN A O   
3738 C CB  . ASN A 497 ? 161.4818 161.4818 161.4818 0.0000 0.0000 0.0000 497 ASN A CB  
3739 C CG  . ASN A 497 ? 161.3978 161.3978 161.3978 0.0000 0.0000 0.0000 497 ASN A CG  
3740 O OD1 . ASN A 497 ? 161.3224 161.3224 161.3224 0.0000 0.0000 0.0000 497 ASN A OD1 
3741 N ND2 . ASN A 497 ? 161.3773 161.3773 161.3773 0.0000 0.0000 0.0000 497 ASN A ND2 
3742 N N   . ALA A 498 ? 161.3698 161.3698 161.3698 0.0000 0.0000 0.0000 498 ALA A N   
3743 C CA  . ALA A 498 ? 161.3994 161.3994 161.3994 0.0000 0.0000 0.0000 498 ALA A CA  
3744 C C   . ALA A 498 ? 161.3153 161.3153 161.3153 0.0000 0.0000 0.0000 498 ALA A C   
3745 O O   . ALA A 498 ? 161.4999 161.4999 161.4999 0.0000 0.0000 0.0000 498 ALA A O   
3746 C CB  . ALA A 498 ? 161.4043 161.4043 161.4043 0.0000 0.0000 0.0000 498 ALA A CB  
3747 N N   . TYR A 499 ? 161.1749 161.1749 161.1749 0.0000 0.0000 0.0000 499 TYR A N   
3748 C CA  . TYR A 499 ? 161.1499 161.1499 161.1499 0.0000 0.0000 0.0000 499 TYR A CA  
3749 C C   . TYR A 499 ? 161.2378 161.2378 161.2378 0.0000 0.0000 0.0000 499 TYR A C   
3750 O O   . TYR A 499 ? 161.5176 161.5176 161.5176 0.0000 0.0000 0.0000 499 TYR A O   
3751 C CB  . TYR A 499 ? 161.4043 161.4043 161.4043 0.0000 0.0000 0.0000 499 TYR A CB  
3752 C CG  . TYR A 499 ? 161.4283 161.4283 161.4283 0.0000 0.0000 0.0000 499 TYR A CG  
3753 C CD1 . TYR A 499 ? 161.4610 161.4610 161.4610 0.0000 0.0000 0.0000 499 TYR A CD1 
3754 C CD2 . TYR A 499 ? 161.5263 161.5263 161.5263 0.0000 0.0000 0.0000 499 TYR A CD2 
3755 C CE1 . TYR A 499 ? 161.6104 161.6104 161.6104 0.0000 0.0000 0.0000 499 TYR A CE1 
3756 C CE2 . TYR A 499 ? 161.5642 161.5642 161.5642 0.0000 0.0000 0.0000 499 TYR A CE2 
3757 C CZ  . TYR A 499 ? 161.5893 161.5893 161.5893 0.0000 0.0000 0.0000 499 TYR A CZ  
3758 O OH  . TYR A 499 ? 161.3365 161.3365 161.3365 0.0000 0.0000 0.0000 499 TYR A OH  
3759 N N   . THR A 500 ? 161.1393 161.1393 161.1393 0.0000 0.0000 0.0000 500 THR A N   
3760 C CA  . THR A 500 ? 161.2927 161.2927 161.2927 0.0000 0.0000 0.0000 500 THR A CA  
3761 C C   . THR A 500 ? 161.3992 161.3992 161.3992 0.0000 0.0000 0.0000 500 THR A C   
3762 O O   . THR A 500 ? 161.4778 161.4778 161.4778 0.0000 0.0000 0.0000 500 THR A O   
3763 C CB  . THR A 500 ? 161.3290 161.3290 161.3290 0.0000 0.0000 0.0000 500 THR A CB  
3764 O OG1 . THR A 500 ? 161.5134 161.5134 161.5134 0.0000 0.0000 0.0000 500 THR A OG1 
3765 C CG2 . THR A 500 ? 161.4146 161.4146 161.4146 0.0000 0.0000 0.0000 500 THR A CG2 
3766 N N   . GLU A 501 ? 161.4010 161.4010 161.4010 0.0000 0.0000 0.0000 501 GLU A N   
3767 C CA  . GLU A 501 ? 161.3260 161.3260 161.3260 0.0000 0.0000 0.0000 501 GLU A CA  
3768 C C   . GLU A 501 ? 161.3583 161.3583 161.3583 0.0000 0.0000 0.0000 501 GLU A C   
3769 O O   . GLU A 501 ? 161.4593 161.4593 161.4593 0.0000 0.0000 0.0000 501 GLU A O   
3770 C CB  . GLU A 501 ? 161.3498 161.3498 161.3498 0.0000 0.0000 0.0000 501 GLU A CB  
3771 C CG  . GLU A 501 ? 161.6917 161.6917 161.6917 0.0000 0.0000 0.0000 501 GLU A CG  
3772 C CD  . GLU A 501 ? 161.7413 161.7413 161.7413 0.0000 0.0000 0.0000 501 GLU A CD  
3773 O OE1 . GLU A 501 ? 161.6996 161.6996 161.6996 0.0000 0.0000 0.0000 501 GLU A OE1 
3774 O OE2 . GLU A 501 ? 161.7556 161.7556 161.7556 0.0000 0.0000 0.0000 501 GLU A OE2 
3775 N N   . LEU A 502 ? 161.4691 161.4691 161.4691 0.0000 0.0000 0.0000 502 LEU A N   
3776 C CA  . LEU A 502 ? 161.3415 161.3415 161.3415 0.0000 0.0000 0.0000 502 LEU A CA  
3777 C C   . LEU A 502 ? 161.2601 161.2601 161.2601 0.0000 0.0000 0.0000 502 LEU A C   
3778 O O   . LEU A 502 ? 161.5052 161.5052 161.5052 0.0000 0.0000 0.0000 502 LEU A O   
3779 C CB  . LEU A 502 ? 161.6134 161.6134 161.6134 0.0000 0.0000 0.0000 502 LEU A CB  
3780 C CG  . LEU A 502 ? 161.4469 161.4469 161.4469 0.0000 0.0000 0.0000 502 LEU A CG  
3781 C CD1 . LEU A 502 ? 161.3450 161.3450 161.3450 0.0000 0.0000 0.0000 502 LEU A CD1 
3782 C CD2 . LEU A 502 ? 161.9399 161.9399 161.9399 0.0000 0.0000 0.0000 502 LEU A CD2 
3783 N N   . ASN A 503 ? 161.2743 161.2743 161.2743 0.0000 0.0000 0.0000 503 ASN A N   
3784 C CA  . ASN A 503 ? 161.3832 161.3832 161.3832 0.0000 0.0000 0.0000 503 ASN A CA  
3785 C C   . ASN A 503 ? 161.3768 161.3768 161.3768 0.0000 0.0000 0.0000 503 ASN A C   
3786 O O   . ASN A 503 ? 161.4323 161.4323 161.4323 0.0000 0.0000 0.0000 503 ASN A O   
3787 C CB  . ASN A 503 ? 161.4561 161.4561 161.4561 0.0000 0.0000 0.0000 503 ASN A CB  
3788 C CG  . ASN A 503 ? 161.4430 161.4430 161.4430 0.0000 0.0000 0.0000 503 ASN A CG  
3789 O OD1 . ASN A 503 ? 161.5875 161.5875 161.5875 0.0000 0.0000 0.0000 503 ASN A OD1 
3790 N ND2 . ASN A 503 ? 161.4295 161.4295 161.4295 0.0000 0.0000 0.0000 503 ASN A ND2 
3791 N N   . ASP A 504 ? 161.3300 161.3300 161.3300 0.0000 0.0000 0.0000 504 ASP A N   
3792 C CA  . ASP A 504 ? 161.3733 161.3733 161.3733 0.0000 0.0000 0.0000 504 ASP A CA  
3793 C C   . ASP A 504 ? 161.5321 161.5321 161.5321 0.0000 0.0000 0.0000 504 ASP A C   
3794 O O   . ASP A 504 ? 161.8896 161.8896 161.8896 0.0000 0.0000 0.0000 504 ASP A O   
3795 C CB  . ASP A 504 ? 161.4999 161.4999 161.4999 0.0000 0.0000 0.0000 504 ASP A CB  
3796 C CG  . ASP A 504 ? 161.6737 161.6737 161.6737 0.0000 0.0000 0.0000 504 ASP A CG  
3797 O OD1 . ASP A 504 ? 161.8054 161.8054 161.8054 0.0000 0.0000 0.0000 504 ASP A OD1 
3798 O OD2 . ASP A 504 ? 161.6825 161.6825 161.6825 0.0000 0.0000 0.0000 504 ASP A OD2 
3799 N N   . PRO A 505 ? 161.4527 161.4527 161.4527 0.0000 0.0000 0.0000 505 PRO A N   
3800 C CA  . PRO A 505 ? 161.5467 161.5467 161.5467 0.0000 0.0000 0.0000 505 PRO A CA  
3801 C C   . PRO A 505 ? 161.8838 161.8838 161.8838 0.0000 0.0000 0.0000 505 PRO A C   
3802 O O   . PRO A 505 ? 162.2984 162.2984 162.2984 0.0000 0.0000 0.0000 505 PRO A O   
3803 C CB  . PRO A 505 ? 161.4229 161.4229 161.4229 0.0000 0.0000 0.0000 505 PRO A CB  
3804 C CG  . PRO A 505 ? 161.5390 161.5390 161.5390 0.0000 0.0000 0.0000 505 PRO A CG  
3805 C CD  . PRO A 505 ? 161.5366 161.5366 161.5366 0.0000 0.0000 0.0000 505 PRO A CD  
3806 N N   . MET A 506 ? 168.7559 168.7559 168.7559 0.0000 0.0000 0.0000 506 MET A N   
3807 C CA  . MET A 506 ? 169.0281 169.0281 169.0281 0.0000 0.0000 0.0000 506 MET A CA  
3808 C C   . MET A 506 ? 169.2542 169.2542 169.2542 0.0000 0.0000 0.0000 506 MET A C   
3809 O O   . MET A 506 ? 169.5951 169.5951 169.5951 0.0000 0.0000 0.0000 506 MET A O   
3810 C CB  . MET A 506 ? 169.3367 169.3367 169.3367 0.0000 0.0000 0.0000 506 MET A CB  
3811 C CG  . MET A 506 ? 169.3711 169.3711 169.3711 0.0000 0.0000 0.0000 506 MET A CG  
3812 S SD  . MET A 506 ? 169.3659 169.3659 169.3659 0.0000 0.0000 0.0000 506 MET A SD  
3813 C CE  . MET A 506 ? 169.3336 169.3336 169.3336 0.0000 0.0000 0.0000 506 MET A CE  
3814 N N   . ARG A 507 ? 166.3273 166.3273 166.3273 0.0000 0.0000 0.0000 507 ARG A N   
3815 C CA  . ARG A 507 ? 166.4046 166.4046 166.4046 0.0000 0.0000 0.0000 507 ARG A CA  
3816 C C   . ARG A 507 ? 166.7652 166.7652 166.7652 0.0000 0.0000 0.0000 507 ARG A C   
3817 O O   . ARG A 507 ? 167.1605 167.1605 167.1605 0.0000 0.0000 0.0000 507 ARG A O   
3818 C CB  . ARG A 507 ? 166.2179 166.2179 166.2179 0.0000 0.0000 0.0000 507 ARG A CB  
3819 C CG  . ARG A 507 ? 166.3527 166.3527 166.3527 0.0000 0.0000 0.0000 507 ARG A CG  
3820 C CD  . ARG A 507 ? 166.3708 166.3708 166.3708 0.0000 0.0000 0.0000 507 ARG A CD  
3821 N NE  . ARG A 507 ? 166.3800 166.3800 166.3800 0.0000 0.0000 0.0000 507 ARG A NE  
3822 C CZ  . ARG A 507 ? 166.3784 166.3784 166.3784 0.0000 0.0000 0.0000 507 ARG A CZ  
3823 N NH1 . ARG A 507 ? 166.3168 166.3168 166.3168 0.0000 0.0000 0.0000 507 ARG A NH1 
3824 N NH2 . ARG A 507 ? 166.4179 166.4179 166.4179 0.0000 0.0000 0.0000 507 ARG A NH2 
3825 N N   . GLN A 508 ? 169.4874 169.4874 169.4874 0.0000 0.0000 0.0000 508 GLN A N   
3826 C CA  . GLN A 508 ? 169.5425 169.5425 169.5425 0.0000 0.0000 0.0000 508 GLN A CA  
3827 C C   . GLN A 508 ? 169.9862 169.9862 169.9862 0.0000 0.0000 0.0000 508 GLN A C   
3828 O O   . GLN A 508 ? 170.4750 170.4750 170.4750 0.0000 0.0000 0.0000 508 GLN A O   
3829 C CB  . GLN A 508 ? 169.3508 169.3508 169.3508 0.0000 0.0000 0.0000 508 GLN A CB  
3830 C CG  . GLN A 508 ? 169.5766 169.5766 169.5766 0.0000 0.0000 0.0000 508 GLN A CG  
3831 C CD  . GLN A 508 ? 169.6425 169.6425 169.6425 0.0000 0.0000 0.0000 508 GLN A CD  
3832 O OE1 . GLN A 508 ? 169.6474 169.6474 169.6474 0.0000 0.0000 0.0000 508 GLN A OE1 
3833 N NE2 . GLN A 508 ? 169.9065 169.9065 169.9065 0.0000 0.0000 0.0000 508 GLN A NE2 
3834 N N   . ARG A 509 ? 175.9369 175.9369 175.9369 0.0000 0.0000 0.0000 509 ARG A N   
3835 C CA  . ARG A 509 ? 176.2165 176.2165 176.2165 0.0000 0.0000 0.0000 509 ARG A CA  
3836 C C   . ARG A 509 ? 176.8119 176.8119 176.8119 0.0000 0.0000 0.0000 509 ARG A C   
3837 O O   . ARG A 509 ? 177.4324 177.4324 177.4324 0.0000 0.0000 0.0000 509 ARG A O   
3838 C CB  . ARG A 509 ? 176.3338 176.3338 176.3338 0.0000 0.0000 0.0000 509 ARG A CB  
3839 C CG  . ARG A 509 ? 176.6671 176.6671 176.6671 0.0000 0.0000 0.0000 509 ARG A CG  
3840 C CD  . ARG A 509 ? 176.6024 176.6024 176.6024 0.0000 0.0000 0.0000 509 ARG A CD  
3841 N NE  . ARG A 509 ? 176.2148 176.2148 176.2148 0.0000 0.0000 0.0000 509 ARG A NE  
3842 C CZ  . ARG A 509 ? 176.3431 176.3431 176.3431 0.0000 0.0000 0.0000 509 ARG A CZ  
3843 N NH1 . ARG A 509 ? 176.7082 176.7082 176.7082 0.0000 0.0000 0.0000 509 ARG A NH1 
3844 N NH2 . ARG A 509 ? 176.2783 176.2783 176.2783 0.0000 0.0000 0.0000 509 ARG A NH2 
3845 N N   . GLN A 510 ? 181.0704 181.0704 181.0704 0.0000 0.0000 0.0000 510 GLN A N   
3846 C CA  . GLN A 510 ? 181.4845 181.4845 181.4845 0.0000 0.0000 0.0000 510 GLN A CA  
3847 C C   . GLN A 510 ? 181.6822 181.6822 181.6822 0.0000 0.0000 0.0000 510 GLN A C   
3848 O O   . GLN A 510 ? 182.0790 182.0790 182.0790 0.0000 0.0000 0.0000 510 GLN A O   
3849 C CB  . GLN A 510 ? 181.4144 181.4144 181.4144 0.0000 0.0000 0.0000 510 GLN A CB  
3850 C CG  . GLN A 510 ? 181.5481 181.5481 181.5481 0.0000 0.0000 0.0000 510 GLN A CG  
3851 C CD  . GLN A 510 ? 181.5530 181.5530 181.5530 0.0000 0.0000 0.0000 510 GLN A CD  
3852 O OE1 . GLN A 510 ? 181.3748 181.3748 181.3748 0.0000 0.0000 0.0000 510 GLN A OE1 
3853 N NE2 . GLN A 510 ? 181.6327 181.6327 181.6327 0.0000 0.0000 0.0000 510 GLN A NE2 
3854 N N   . LEU A 511 ? 180.7913 180.7913 180.7913 0.0000 0.0000 0.0000 511 LEU A N   
3855 C CA  . LEU A 511 ? 180.9296 180.9296 180.9296 0.0000 0.0000 0.0000 511 LEU A CA  
3856 C C   . LEU A 511 ? 181.3603 181.3603 181.3603 0.0000 0.0000 0.0000 511 LEU A C   
3857 O O   . LEU A 511 ? 182.0409 182.0409 182.0409 0.0000 0.0000 0.0000 511 LEU A O   
3858 C CB  . LEU A 511 ? 180.7669 180.7669 180.7669 0.0000 0.0000 0.0000 511 LEU A CB  
3859 C CG  . LEU A 511 ? 180.7550 180.7550 180.7550 0.0000 0.0000 0.0000 511 LEU A CG  
3860 C CD1 . LEU A 511 ? 180.9474 180.9474 180.9474 0.0000 0.0000 0.0000 511 LEU A CD1 
3861 C CD2 . LEU A 511 ? 180.8706 180.8706 180.8706 0.0000 0.0000 0.0000 511 LEU A CD2 
3862 N N   . PHE A 512 ? 180.9169 180.9169 180.9169 0.0000 0.0000 0.0000 512 PHE A N   
3863 C CA  . PHE A 512 ? 181.0118 181.0118 181.0118 0.0000 0.0000 0.0000 512 PHE A CA  
3864 C C   . PHE A 512 ? 181.8629 181.8629 181.8629 0.0000 0.0000 0.0000 512 PHE A C   
3865 O O   . PHE A 512 ? 182.2426 182.2426 182.2426 0.0000 0.0000 0.0000 512 PHE A O   
3866 C CB  . PHE A 512 ? 180.7611 180.7611 180.7611 0.0000 0.0000 0.0000 512 PHE A CB  
3867 C CG  . PHE A 512 ? 180.5666 180.5666 180.5666 0.0000 0.0000 0.0000 512 PHE A CG  
3868 C CD1 . PHE A 512 ? 180.3894 180.3894 180.3894 0.0000 0.0000 0.0000 512 PHE A CD1 
3869 C CD2 . PHE A 512 ? 180.6838 180.6838 180.6838 0.0000 0.0000 0.0000 512 PHE A CD2 
3870 C CE1 . PHE A 512 ? 179.7989 179.7989 179.7989 0.0000 0.0000 0.0000 512 PHE A CE1 
3871 C CE2 . PHE A 512 ? 180.2858 180.2858 180.2858 0.0000 0.0000 0.0000 512 PHE A CE2 
3872 C CZ  . PHE A 512 ? 179.8173 179.8173 179.8173 0.0000 0.0000 0.0000 512 PHE A CZ  
3873 N N   . GLU A 513 ? 202.3400 202.3400 202.3400 0.0000 0.0000 0.0000 513 GLU A N   
3874 C CA  . GLU A 513 ? 203.0647 203.0647 203.0647 0.0000 0.0000 0.0000 513 GLU A CA  
3875 C C   . GLU A 513 ? 203.3223 203.3223 203.3223 0.0000 0.0000 0.0000 513 GLU A C   
3876 O O   . GLU A 513 ? 203.9668 203.9668 203.9668 0.0000 0.0000 0.0000 513 GLU A O   
3877 C CB  . GLU A 513 ? 203.2323 203.2323 203.2323 0.0000 0.0000 0.0000 513 GLU A CB  
3878 C CG  . GLU A 513 ? 203.3868 203.3868 203.3868 0.0000 0.0000 0.0000 513 GLU A CG  
3879 C CD  . GLU A 513 ? 203.3088 203.3088 203.3088 0.0000 0.0000 0.0000 513 GLU A CD  
3880 O OE1 . GLU A 513 ? 203.1997 203.1997 203.1997 0.0000 0.0000 0.0000 513 GLU A OE1 
3881 O OE2 . GLU A 513 ? 203.3076 203.3076 203.3076 0.0000 0.0000 0.0000 513 GLU A OE2 
3882 N N   . GLU A 514 ? 202.7430 202.7430 202.7430 0.0000 0.0000 0.0000 514 GLU A N   
3883 C CA  . GLU A 514 ? 203.1904 203.1904 203.1904 0.0000 0.0000 0.0000 514 GLU A CA  
3884 C C   . GLU A 514 ? 203.6004 203.6004 203.6004 0.0000 0.0000 0.0000 514 GLU A C   
3885 O O   . GLU A 514 ? 203.9402 203.9402 203.9402 0.0000 0.0000 0.0000 514 GLU A O   
3886 C CB  . GLU A 514 ? 203.0927 203.0927 203.0927 0.0000 0.0000 0.0000 514 GLU A CB  
3887 C CG  . GLU A 514 ? 203.2554 203.2554 203.2554 0.0000 0.0000 0.0000 514 GLU A CG  
3888 C CD  . GLU A 514 ? 203.2796 203.2796 203.2796 0.0000 0.0000 0.0000 514 GLU A CD  
3889 O OE1 . GLU A 514 ? 202.8349 202.8349 202.8349 0.0000 0.0000 0.0000 514 GLU A OE1 
3890 O OE2 . GLU A 514 ? 203.0465 203.0465 203.0465 0.0000 0.0000 0.0000 514 GLU A OE2 
3891 N N   . GLN A 515 ? 210.3848 210.3848 210.3848 0.0000 0.0000 0.0000 515 GLN A N   
3892 C CA  . GLN A 515 ? 210.7552 210.7552 210.7552 0.0000 0.0000 0.0000 515 GLN A CA  
3893 C C   . GLN A 515 ? 211.2553 211.2553 211.2553 0.0000 0.0000 0.0000 515 GLN A C   
3894 O O   . GLN A 515 ? 211.6526 211.6526 211.6526 0.0000 0.0000 0.0000 515 GLN A O   
3895 C CB  . GLN A 515 ? 210.4093 210.4093 210.4093 0.0000 0.0000 0.0000 515 GLN A CB  
3896 C CG  . GLN A 515 ? 209.7960 209.7960 209.7960 0.0000 0.0000 0.0000 515 GLN A CG  
3897 C CD  . GLN A 515 ? 209.0153 209.0153 209.0153 0.0000 0.0000 0.0000 515 GLN A CD  
3898 O OE1 . GLN A 515 ? 207.8291 207.8291 207.8291 0.0000 0.0000 0.0000 515 GLN A OE1 
3899 N NE2 . GLN A 515 ? 208.8917 208.8917 208.8917 0.0000 0.0000 0.0000 515 GLN A NE2 
3900 N N   . ALA A 516 ? 221.3395 221.3395 221.3395 0.0000 0.0000 0.0000 516 ALA A N   
3901 C CA  . ALA A 516 ? 222.0051 222.0051 222.0051 0.0000 0.0000 0.0000 516 ALA A CA  
3902 C C   . ALA A 516 ? 222.2827 222.2827 222.2827 0.0000 0.0000 0.0000 516 ALA A C   
3903 O O   . ALA A 516 ? 222.8133 222.8133 222.8133 0.0000 0.0000 0.0000 516 ALA A O   
3904 C CB  . ALA A 516 ? 222.3040 222.3040 222.3040 0.0000 0.0000 0.0000 516 ALA A CB  
3905 N N   . LYS A 517 ? 221.3295 221.3295 221.3295 0.0000 0.0000 0.0000 517 LYS A N   
3906 C CA  . LYS A 517 ? 221.5419 221.5419 221.5419 0.0000 0.0000 0.0000 517 LYS A CA  
3907 C C   . LYS A 517 ? 221.6278 221.6278 221.6278 0.0000 0.0000 0.0000 517 LYS A C   
3908 O O   . LYS A 517 ? 221.8787 221.8787 221.8787 0.0000 0.0000 0.0000 517 LYS A O   
3909 C CB  . LYS A 517 ? 221.3435 221.3435 221.3435 0.0000 0.0000 0.0000 517 LYS A CB  
3910 C CG  . LYS A 517 ? 221.4422 221.4422 221.4422 0.0000 0.0000 0.0000 517 LYS A CG  
3911 C CD  . LYS A 517 ? 221.3864 221.3864 221.3864 0.0000 0.0000 0.0000 517 LYS A CD  
3912 C CE  . LYS A 517 ? 221.2365 221.2365 221.2365 0.0000 0.0000 0.0000 517 LYS A CE  
3913 N NZ  . LYS A 517 ? 221.3064 221.3064 221.3064 0.0000 0.0000 0.0000 517 LYS A NZ  
3914 N N   . ALA A 518 ? 225.6681 225.6681 225.6681 0.0000 0.0000 0.0000 518 ALA A N   
3915 C CA  . ALA A 518 ? 225.9196 225.9196 225.9196 0.0000 0.0000 0.0000 518 ALA A CA  
3916 C C   . ALA A 518 ? 226.1407 226.1407 226.1407 0.0000 0.0000 0.0000 518 ALA A C   
3917 O O   . ALA A 518 ? 226.2257 226.2257 226.2257 0.0000 0.0000 0.0000 518 ALA A O   
3918 C CB  . ALA A 518 ? 225.8749 225.8749 225.8749 0.0000 0.0000 0.0000 518 ALA A CB  
3919 N N   . LYS A 519 ? 231.1699 231.1699 231.1699 0.0000 0.0000 0.0000 519 LYS A N   
3920 C CA  . LYS A 519 ? 231.4278 231.4278 231.4278 0.0000 0.0000 0.0000 519 LYS A CA  
3921 C C   . LYS A 519 ? 231.8566 231.8566 231.8566 0.0000 0.0000 0.0000 519 LYS A C   
3922 O O   . LYS A 519 ? 231.8438 231.8438 231.8438 0.0000 0.0000 0.0000 519 LYS A O   
3923 C CB  . LYS A 519 ? 231.3755 231.3755 231.3755 0.0000 0.0000 0.0000 519 LYS A CB  
3924 C CG  . LYS A 519 ? 231.4799 231.4799 231.4799 0.0000 0.0000 0.0000 519 LYS A CG  
3925 C CD  . LYS A 519 ? 230.9719 230.9719 230.9719 0.0000 0.0000 0.0000 519 LYS A CD  
3926 C CE  . LYS A 519 ? 231.0534 231.0534 231.0534 0.0000 0.0000 0.0000 519 LYS A CE  
3927 N NZ  . LYS A 519 ? 230.4873 230.4873 230.4873 0.0000 0.0000 0.0000 519 LYS A NZ  
3928 N N   . ALA A 520 ? 251.4547 251.4547 251.4547 0.0000 0.0000 0.0000 520 ALA A N   
3929 C CA  . ALA A 520 ? 252.0898 252.0898 252.0898 0.0000 0.0000 0.0000 520 ALA A CA  
3930 C C   . ALA A 520 ? 252.5471 252.5471 252.5471 0.0000 0.0000 0.0000 520 ALA A C   
3931 O O   . ALA A 520 ? 252.7236 252.7236 252.7236 0.0000 0.0000 0.0000 520 ALA A O   
3932 C CB  . ALA A 520 ? 252.4334 252.4334 252.4334 0.0000 0.0000 0.0000 520 ALA A CB  
3933 N N   . ALA A 521 ? 262.3781 262.3781 262.3781 0.0000 0.0000 0.0000 521 ALA A N   
3934 C CA  . ALA A 521 ? 262.7744 262.7744 262.7744 0.0000 0.0000 0.0000 521 ALA A CA  
3935 C C   . ALA A 521 ? 263.0705 263.0705 263.0705 0.0000 0.0000 0.0000 521 ALA A C   
3936 O O   . ALA A 521 ? 263.0724 263.0724 263.0724 0.0000 0.0000 0.0000 521 ALA A O   
3937 C CB  . ALA A 521 ? 262.8508 262.8508 262.8508 0.0000 0.0000 0.0000 521 ALA A CB  
3938 N N   . GLY A 522 ? 272.3355 272.3355 272.3355 0.0000 0.0000 0.0000 522 GLY A N   
3939 C CA  . GLY A 522 ? 272.6055 272.6055 272.6055 0.0000 0.0000 0.0000 522 GLY A CA  
3940 C C   . GLY A 522 ? 272.7568 272.7568 272.7568 0.0000 0.0000 0.0000 522 GLY A C   
3941 O O   . GLY A 522 ? 272.7071 272.7071 272.7071 0.0000 0.0000 0.0000 522 GLY A O   
3942 N N   . ASP A 523 ? 283.0293 283.0293 283.0293 0.0000 0.0000 0.0000 523 ASP A N   
3943 C CA  . ASP A 523 ? 283.1300 283.1300 283.1300 0.0000 0.0000 0.0000 523 ASP A CA  
3944 C C   . ASP A 523 ? 283.0238 283.0238 283.0238 0.0000 0.0000 0.0000 523 ASP A C   
3945 O O   . ASP A 523 ? 283.1126 283.1126 283.1126 0.0000 0.0000 0.0000 523 ASP A O   
3946 C CB  . ASP A 523 ? 283.0584 283.0584 283.0584 0.0000 0.0000 0.0000 523 ASP A CB  
3947 C CG  . ASP A 523 ? 283.1157 283.1157 283.1157 0.0000 0.0000 0.0000 523 ASP A CG  
3948 O OD1 . ASP A 523 ? 283.3209 283.3209 283.3209 0.0000 0.0000 0.0000 523 ASP A OD1 
3949 O OD2 . ASP A 523 ? 282.8632 282.8632 282.8632 0.0000 0.0000 0.0000 523 ASP A OD2 
3950 N N   . ASP A 524 ? 273.0813 273.0813 273.0813 0.0000 0.0000 0.0000 524 ASP A N   
3951 C CA  . ASP A 524 ? 272.8274 272.8274 272.8274 0.0000 0.0000 0.0000 524 ASP A CA  
3952 C C   . ASP A 524 ? 272.3590 272.3590 272.3590 0.0000 0.0000 0.0000 524 ASP A C   
3953 O O   . ASP A 524 ? 272.2095 272.2095 272.2095 0.0000 0.0000 0.0000 524 ASP A O   
3954 C CB  . ASP A 524 ? 272.8132 272.8132 272.8132 0.0000 0.0000 0.0000 524 ASP A CB  
3955 C CG  . ASP A 524 ? 272.8237 272.8237 272.8237 0.0000 0.0000 0.0000 524 ASP A CG  
3956 O OD1 . ASP A 524 ? 272.8181 272.8181 272.8181 0.0000 0.0000 0.0000 524 ASP A OD1 
3957 O OD2 . ASP A 524 ? 272.7348 272.7348 272.7348 0.0000 0.0000 0.0000 524 ASP A OD2 
3958 N N   . GLU A 525 ? 257.0961 257.0961 257.0961 0.0000 0.0000 0.0000 525 GLU A N   
3959 C CA  . GLU A 525 ? 256.6910 256.6910 256.6910 0.0000 0.0000 0.0000 525 GLU A CA  
3960 C C   . GLU A 525 ? 256.3070 256.3070 256.3070 0.0000 0.0000 0.0000 525 GLU A C   
3961 O O   . GLU A 525 ? 255.9953 255.9953 255.9953 0.0000 0.0000 0.0000 525 GLU A O   
3962 C CB  . GLU A 525 ? 256.7353 256.7353 256.7353 0.0000 0.0000 0.0000 525 GLU A CB  
3963 C CG  . GLU A 525 ? 256.7291 256.7291 256.7291 0.0000 0.0000 0.0000 525 GLU A CG  
3964 C CD  . GLU A 525 ? 256.4176 256.4176 256.4176 0.0000 0.0000 0.0000 525 GLU A CD  
3965 O OE1 . GLU A 525 ? 256.2392 256.2392 256.2392 0.0000 0.0000 0.0000 525 GLU A OE1 
3966 O OE2 . GLU A 525 ? 256.1065 256.1065 256.1065 0.0000 0.0000 0.0000 525 GLU A OE2 
3967 N N   . ALA A 526 ? 249.2977 249.2977 249.2977 0.0000 0.0000 0.0000 526 ALA A N   
3968 C CA  . ALA A 526 ? 249.0340 249.0340 249.0340 0.0000 0.0000 0.0000 526 ALA A CA  
3969 C C   . ALA A 526 ? 248.6865 248.6865 248.6865 0.0000 0.0000 0.0000 526 ALA A C   
3970 O O   . ALA A 526 ? 248.5144 248.5144 248.5144 0.0000 0.0000 0.0000 526 ALA A O   
3971 C CB  . ALA A 526 ? 249.1051 249.1051 249.1051 0.0000 0.0000 0.0000 526 ALA A CB  
3972 N N   . MET A 527 ? 242.7521 242.7521 242.7521 0.0000 0.0000 0.0000 527 MET A N   
3973 C CA  . MET A 527 ? 242.1859 242.1859 242.1859 0.0000 0.0000 0.0000 527 MET A CA  
3974 C C   . MET A 527 ? 241.7490 241.7490 241.7490 0.0000 0.0000 0.0000 527 MET A C   
3975 O O   . MET A 527 ? 240.8755 240.8755 240.8755 0.0000 0.0000 0.0000 527 MET A O   
3976 C CB  . MET A 527 ? 242.3547 242.3547 242.3547 0.0000 0.0000 0.0000 527 MET A CB  
3977 C CG  . MET A 527 ? 242.5389 242.5389 242.5389 0.0000 0.0000 0.0000 527 MET A CG  
3978 S SD  . MET A 527 ? 243.2090 243.2090 243.2090 0.0000 0.0000 0.0000 527 MET A SD  
3979 C CE  . MET A 527 ? 243.1413 243.1413 243.1413 0.0000 0.0000 0.0000 527 MET A CE  
3980 N N   . PHE A 528 ? 233.6572 233.6572 233.6572 0.0000 0.0000 0.0000 528 PHE A N   
3981 C CA  . PHE A 528 ? 233.2717 233.2717 233.2717 0.0000 0.0000 0.0000 528 PHE A CA  
3982 C C   . PHE A 528 ? 232.9410 232.9410 232.9410 0.0000 0.0000 0.0000 528 PHE A C   
3983 O O   . PHE A 528 ? 232.8761 232.8761 232.8761 0.0000 0.0000 0.0000 528 PHE A O   
3984 C CB  . PHE A 528 ? 233.5236 233.5236 233.5236 0.0000 0.0000 0.0000 528 PHE A CB  
3985 C CG  . PHE A 528 ? 233.7069 233.7069 233.7069 0.0000 0.0000 0.0000 528 PHE A CG  
3986 C CD1 . PHE A 528 ? 233.4202 233.4202 233.4202 0.0000 0.0000 0.0000 528 PHE A CD1 
3987 C CD2 . PHE A 528 ? 234.1784 234.1784 234.1784 0.0000 0.0000 0.0000 528 PHE A CD2 
3988 C CE1 . PHE A 528 ? 233.6141 233.6141 233.6141 0.0000 0.0000 0.0000 528 PHE A CE1 
3989 C CE2 . PHE A 528 ? 234.1322 234.1322 234.1322 0.0000 0.0000 0.0000 528 PHE A CE2 
3990 C CZ  . PHE A 528 ? 233.8063 233.8063 233.8063 0.0000 0.0000 0.0000 528 PHE A CZ  
3991 N N   . ILE A 529 ? 215.2354 215.2354 215.2354 0.0000 0.0000 0.0000 529 ILE A N   
3992 C CA  . ILE A 529 ? 214.4589 214.4589 214.4589 0.0000 0.0000 0.0000 529 ILE A CA  
3993 C C   . ILE A 529 ? 213.8591 213.8591 213.8591 0.0000 0.0000 0.0000 529 ILE A C   
3994 O O   . ILE A 529 ? 214.0818 214.0818 214.0818 0.0000 0.0000 0.0000 529 ILE A O   
3995 C CB  . ILE A 529 ? 214.4096 214.4096 214.4096 0.0000 0.0000 0.0000 529 ILE A CB  
3996 C CG1 . ILE A 529 ? 213.9067 213.9067 213.9067 0.0000 0.0000 0.0000 529 ILE A CG1 
3997 C CG2 . ILE A 529 ? 214.7047 214.7047 214.7047 0.0000 0.0000 0.0000 529 ILE A CG2 
3998 C CD1 . ILE A 529 ? 213.7928 213.7928 213.7928 0.0000 0.0000 0.0000 529 ILE A CD1 
3999 N N   . ASP A 530 ? 198.0328 198.0328 198.0328 0.0000 0.0000 0.0000 530 ASP A N   
4000 C CA  . ASP A 530 ? 197.6643 197.6643 197.6643 0.0000 0.0000 0.0000 530 ASP A CA  
4001 C C   . ASP A 530 ? 197.1644 197.1644 197.1644 0.0000 0.0000 0.0000 530 ASP A C   
4002 O O   . ASP A 530 ? 196.8552 196.8552 196.8552 0.0000 0.0000 0.0000 530 ASP A O   
4003 C CB  . ASP A 530 ? 197.3365 197.3365 197.3365 0.0000 0.0000 0.0000 530 ASP A CB  
4004 C CG  . ASP A 530 ? 197.1422 197.1422 197.1422 0.0000 0.0000 0.0000 530 ASP A CG  
4005 O OD1 . ASP A 530 ? 197.2824 197.2824 197.2824 0.0000 0.0000 0.0000 530 ASP A OD1 
4006 O OD2 . ASP A 530 ? 197.0024 197.0024 197.0024 0.0000 0.0000 0.0000 530 ASP A OD2 
4007 N N   . GLU A 531 ? 195.9505 195.9505 195.9505 0.0000 0.0000 0.0000 531 GLU A N   
4008 C CA  . GLU A 531 ? 195.7119 195.7119 195.7119 0.0000 0.0000 0.0000 531 GLU A CA  
4009 C C   . GLU A 531 ? 194.9624 194.9624 194.9624 0.0000 0.0000 0.0000 531 GLU A C   
4010 O O   . GLU A 531 ? 195.1212 195.1212 195.1212 0.0000 0.0000 0.0000 531 GLU A O   
4011 C CB  . GLU A 531 ? 195.9990 195.9990 195.9990 0.0000 0.0000 0.0000 531 GLU A CB  
4012 C CG  . GLU A 531 ? 196.1801 196.1801 196.1801 0.0000 0.0000 0.0000 531 GLU A CG  
4013 C CD  . GLU A 531 ? 196.2498 196.2498 196.2498 0.0000 0.0000 0.0000 531 GLU A CD  
4014 O OE1 . GLU A 531 ? 196.1132 196.1132 196.1132 0.0000 0.0000 0.0000 531 GLU A OE1 
4015 O OE2 . GLU A 531 ? 196.2622 196.2622 196.2622 0.0000 0.0000 0.0000 531 GLU A OE2 
4016 N N   . ASN A 532 ? 175.0697 175.0697 175.0697 0.0000 0.0000 0.0000 532 ASN A N   
4017 C CA  . ASN A 532 ? 174.5248 174.5248 174.5248 0.0000 0.0000 0.0000 532 ASN A CA  
4018 C C   . ASN A 532 ? 174.1111 174.1111 174.1111 0.0000 0.0000 0.0000 532 ASN A C   
4019 O O   . ASN A 532 ? 173.9834 173.9834 173.9834 0.0000 0.0000 0.0000 532 ASN A O   
4020 C CB  . ASN A 532 ? 174.5224 174.5224 174.5224 0.0000 0.0000 0.0000 532 ASN A CB  
4021 C CG  . ASN A 532 ? 174.4185 174.4185 174.4185 0.0000 0.0000 0.0000 532 ASN A CG  
4022 O OD1 . ASN A 532 ? 174.3419 174.3419 174.3419 0.0000 0.0000 0.0000 532 ASN A OD1 
4023 N ND2 . ASN A 532 ? 174.4902 174.4902 174.4902 0.0000 0.0000 0.0000 532 ASN A ND2 
4024 N N   . PHE A 533 ? 162.7701 162.7701 162.7701 0.0000 0.0000 0.0000 533 PHE A N   
4025 C CA  . PHE A 533 ? 161.9885 161.9885 161.9885 0.0000 0.0000 0.0000 533 PHE A CA  
4026 C C   . PHE A 533 ? 161.9258 161.9258 161.9258 0.0000 0.0000 0.0000 533 PHE A C   
4027 O O   . PHE A 533 ? 161.8877 161.8877 161.8877 0.0000 0.0000 0.0000 533 PHE A O   
4028 C CB  . PHE A 533 ? 162.0790 162.0790 162.0790 0.0000 0.0000 0.0000 533 PHE A CB  
4029 C CG  . PHE A 533 ? 161.4288 161.4288 161.4288 0.0000 0.0000 0.0000 533 PHE A CG  
4030 C CD1 . PHE A 533 ? 161.3784 161.3784 161.3784 0.0000 0.0000 0.0000 533 PHE A CD1 
4031 C CD2 . PHE A 533 ? 161.6736 161.6736 161.6736 0.0000 0.0000 0.0000 533 PHE A CD2 
4032 C CE1 . PHE A 533 ? 161.4453 161.4453 161.4453 0.0000 0.0000 0.0000 533 PHE A CE1 
4033 C CE2 . PHE A 533 ? 161.7011 161.7011 161.7011 0.0000 0.0000 0.0000 533 PHE A CE2 
4034 C CZ  . PHE A 533 ? 161.5198 161.5198 161.5198 0.0000 0.0000 0.0000 533 PHE A CZ  
4035 N N   . CYS A 534 ? 166.8812 166.8812 166.8812 0.0000 0.0000 0.0000 534 CYS A N   
4036 C CA  . CYS A 534 ? 166.7577 166.7577 166.7577 0.0000 0.0000 0.0000 534 CYS A CA  
4037 C C   . CYS A 534 ? 166.4001 166.4001 166.4001 0.0000 0.0000 0.0000 534 CYS A C   
4038 O O   . CYS A 534 ? 166.4491 166.4491 166.4491 0.0000 0.0000 0.0000 534 CYS A O   
4039 C CB  . CYS A 534 ? 167.2578 167.2578 167.2578 0.0000 0.0000 0.0000 534 CYS A CB  
4040 S SG  . CYS A 534 ? 167.4527 167.4527 167.4527 0.0000 0.0000 0.0000 534 CYS A SG  
4041 N N   . THR A 535 ? 161.7660 161.7660 161.7660 0.0000 0.0000 0.0000 535 THR A N   
4042 C CA  . THR A 535 ? 161.5491 161.5491 161.5491 0.0000 0.0000 0.0000 535 THR A CA  
4043 C C   . THR A 535 ? 161.5605 161.5605 161.5605 0.0000 0.0000 0.0000 535 THR A C   
4044 O O   . THR A 535 ? 161.7930 161.7930 161.7930 0.0000 0.0000 0.0000 535 THR A O   
4045 C CB  . THR A 535 ? 161.6558 161.6558 161.6558 0.0000 0.0000 0.0000 535 THR A CB  
4046 O OG1 . THR A 535 ? 161.7245 161.7245 161.7245 0.0000 0.0000 0.0000 535 THR A OG1 
4047 C CG2 . THR A 535 ? 161.5088 161.5088 161.5088 0.0000 0.0000 0.0000 535 THR A CG2 
4048 N N   . ALA A 536 ? 161.5140 161.5140 161.5140 0.0000 0.0000 0.0000 536 ALA A N   
4049 C CA  . ALA A 536 ? 161.3899 161.3899 161.3899 0.0000 0.0000 0.0000 536 ALA A CA  
4050 C C   . ALA A 536 ? 161.4511 161.4511 161.4511 0.0000 0.0000 0.0000 536 ALA A C   
4051 O O   . ALA A 536 ? 161.8040 161.8040 161.8040 0.0000 0.0000 0.0000 536 ALA A O   
4052 C CB  . ALA A 536 ? 161.6521 161.6521 161.6521 0.0000 0.0000 0.0000 536 ALA A CB  
4053 N N   . LEU A 537 ? 161.5068 161.5068 161.5068 0.0000 0.0000 0.0000 537 LEU A N   
4054 C CA  . LEU A 537 ? 161.4755 161.4755 161.4755 0.0000 0.0000 0.0000 537 LEU A CA  
4055 C C   . LEU A 537 ? 161.4703 161.4703 161.4703 0.0000 0.0000 0.0000 537 LEU A C   
4056 O O   . LEU A 537 ? 161.4622 161.4622 161.4622 0.0000 0.0000 0.0000 537 LEU A O   
4057 C CB  . LEU A 537 ? 161.4400 161.4400 161.4400 0.0000 0.0000 0.0000 537 LEU A CB  
4058 C CG  . LEU A 537 ? 161.3721 161.3721 161.3721 0.0000 0.0000 0.0000 537 LEU A CG  
4059 C CD1 . LEU A 537 ? 161.4604 161.4604 161.4604 0.0000 0.0000 0.0000 537 LEU A CD1 
4060 C CD2 . LEU A 537 ? 161.4991 161.4991 161.4991 0.0000 0.0000 0.0000 537 LEU A CD2 
4061 N N   . GLU A 538 ? 161.5045 161.5045 161.5045 0.0000 0.0000 0.0000 538 GLU A N   
4062 C CA  . GLU A 538 ? 161.4025 161.4025 161.4025 0.0000 0.0000 0.0000 538 GLU A CA  
4063 C C   . GLU A 538 ? 161.2259 161.2259 161.2259 0.0000 0.0000 0.0000 538 GLU A C   
4064 O O   . GLU A 538 ? 161.4280 161.4280 161.4280 0.0000 0.0000 0.0000 538 GLU A O   
4065 C CB  . GLU A 538 ? 161.4749 161.4749 161.4749 0.0000 0.0000 0.0000 538 GLU A CB  
4066 C CG  . GLU A 538 ? 161.5494 161.5494 161.5494 0.0000 0.0000 0.0000 538 GLU A CG  
4067 C CD  . GLU A 538 ? 161.6297 161.6297 161.6297 0.0000 0.0000 0.0000 538 GLU A CD  
4068 O OE1 . GLU A 538 ? 161.5983 161.5983 161.5983 0.0000 0.0000 0.0000 538 GLU A OE1 
4069 O OE2 . GLU A 538 ? 161.7430 161.7430 161.7430 0.0000 0.0000 0.0000 538 GLU A OE2 
4070 N N   . TYR A 539 ? 161.1949 161.1949 161.1949 0.0000 0.0000 0.0000 539 TYR A N   
4071 C CA  . TYR A 539 ? 161.1644 161.1644 161.1644 0.0000 0.0000 0.0000 539 TYR A CA  
4072 C C   . TYR A 539 ? 161.2523 161.2523 161.2523 0.0000 0.0000 0.0000 539 TYR A C   
4073 O O   . TYR A 539 ? 161.2766 161.2766 161.2766 0.0000 0.0000 0.0000 539 TYR A O   
4074 C CB  . TYR A 539 ? 161.3188 161.3188 161.3188 0.0000 0.0000 0.0000 539 TYR A CB  
4075 C CG  . TYR A 539 ? 161.3487 161.3487 161.3487 0.0000 0.0000 0.0000 539 TYR A CG  
4076 C CD1 . TYR A 539 ? 161.4243 161.4243 161.4243 0.0000 0.0000 0.0000 539 TYR A CD1 
4077 C CD2 . TYR A 539 ? 161.4328 161.4328 161.4328 0.0000 0.0000 0.0000 539 TYR A CD2 
4078 C CE1 . TYR A 539 ? 161.5504 161.5504 161.5504 0.0000 0.0000 0.0000 539 TYR A CE1 
4079 C CE2 . TYR A 539 ? 161.4314 161.4314 161.4314 0.0000 0.0000 0.0000 539 TYR A CE2 
4080 C CZ  . TYR A 539 ? 161.4790 161.4790 161.4790 0.0000 0.0000 0.0000 539 TYR A CZ  
4081 O OH  . TYR A 539 ? 161.6443 161.6443 161.6443 0.0000 0.0000 0.0000 539 TYR A OH  
4082 N N   . GLY A 540 ? 161.4729 161.4729 161.4729 0.0000 0.0000 0.0000 540 GLY A N   
4083 C CA  . GLY A 540 ? 161.3625 161.3625 161.3625 0.0000 0.0000 0.0000 540 GLY A CA  
4084 C C   . GLY A 540 ? 161.3182 161.3182 161.3182 0.0000 0.0000 0.0000 540 GLY A C   
4085 O O   . GLY A 540 ? 161.4886 161.4886 161.4886 0.0000 0.0000 0.0000 540 GLY A O   
4086 N N   . LEU A 541 ? 161.1827 161.1827 161.1827 0.0000 0.0000 0.0000 541 LEU A N   
4087 C CA  . LEU A 541 ? 161.3102 161.3102 161.3102 0.0000 0.0000 0.0000 541 LEU A CA  
4088 C C   . LEU A 541 ? 161.4389 161.4389 161.4389 0.0000 0.0000 0.0000 541 LEU A C   
4089 O O   . LEU A 541 ? 161.6861 161.6861 161.6861 0.0000 0.0000 0.0000 541 LEU A O   
4090 C CB  . LEU A 541 ? 161.3572 161.3572 161.3572 0.0000 0.0000 0.0000 541 LEU A CB  
4091 C CG  . LEU A 541 ? 161.3572 161.3572 161.3572 0.0000 0.0000 0.0000 541 LEU A CG  
4092 C CD1 . LEU A 541 ? 161.5526 161.5526 161.5526 0.0000 0.0000 0.0000 541 LEU A CD1 
4093 C CD2 . LEU A 541 ? 161.4936 161.4936 161.4936 0.0000 0.0000 0.0000 541 LEU A CD2 
4094 N N   . PRO A 542 ? 161.2156 161.2156 161.2156 0.0000 0.0000 0.0000 542 PRO A N   
4095 C CA  . PRO A 542 ? 161.2735 161.2735 161.2735 0.0000 0.0000 0.0000 542 PRO A CA  
4096 C C   . PRO A 542 ? 161.3333 161.3333 161.3333 0.0000 0.0000 0.0000 542 PRO A C   
4097 O O   . PRO A 542 ? 161.6804 161.6804 161.6804 0.0000 0.0000 0.0000 542 PRO A O   
4098 C CB  . PRO A 542 ? 161.4184 161.4184 161.4184 0.0000 0.0000 0.0000 542 PRO A CB  
4099 C CG  . PRO A 542 ? 161.4511 161.4511 161.4511 0.0000 0.0000 0.0000 542 PRO A CG  
4100 C CD  . PRO A 542 ? 161.4119 161.4119 161.4119 0.0000 0.0000 0.0000 542 PRO A CD  
4101 N N   . PRO A 543 ? 161.0204 161.0204 161.0204 0.0000 0.0000 0.0000 543 PRO A N   
4102 C CA  . PRO A 543 ? 161.1959 161.1959 161.1959 0.0000 0.0000 0.0000 543 PRO A CA  
4103 C C   . PRO A 543 ? 161.3649 161.3649 161.3649 0.0000 0.0000 0.0000 543 PRO A C   
4104 O O   . PRO A 543 ? 161.6970 161.6970 161.6970 0.0000 0.0000 0.0000 543 PRO A O   
4105 C CB  . PRO A 543 ? 161.3789 161.3789 161.3789 0.0000 0.0000 0.0000 543 PRO A CB  
4106 C CG  . PRO A 543 ? 161.3569 161.3569 161.3569 0.0000 0.0000 0.0000 543 PRO A CG  
4107 C CD  . PRO A 543 ? 161.2083 161.2083 161.2083 0.0000 0.0000 0.0000 543 PRO A CD  
4108 N N   . THR A 544 ? 161.3200 161.3200 161.3200 0.0000 0.0000 0.0000 544 THR A N   
4109 C CA  . THR A 544 ? 161.3527 161.3527 161.3527 0.0000 0.0000 0.0000 544 THR A CA  
4110 C C   . THR A 544 ? 161.3702 161.3702 161.3702 0.0000 0.0000 0.0000 544 THR A C   
4111 O O   . THR A 544 ? 161.5144 161.5144 161.5144 0.0000 0.0000 0.0000 544 THR A O   
4112 C CB  . THR A 544 ? 161.4449 161.4449 161.4449 0.0000 0.0000 0.0000 544 THR A CB  
4113 O OG1 . THR A 544 ? 161.6142 161.6142 161.6142 0.0000 0.0000 0.0000 544 THR A OG1 
4114 C CG2 . THR A 544 ? 161.5818 161.5818 161.5818 0.0000 0.0000 0.0000 544 THR A CG2 
4115 N N   . ALA A 545 ? 161.3234 161.3234 161.3234 0.0000 0.0000 0.0000 545 ALA A N   
4116 C CA  . ALA A 545 ? 161.2976 161.2976 161.2976 0.0000 0.0000 0.0000 545 ALA A CA  
4117 C C   . ALA A 545 ? 161.3549 161.3549 161.3549 0.0000 0.0000 0.0000 545 ALA A C   
4118 O O   . ALA A 545 ? 161.4987 161.4987 161.4987 0.0000 0.0000 0.0000 545 ALA A O   
4119 C CB  . ALA A 545 ? 161.5506 161.5506 161.5506 0.0000 0.0000 0.0000 545 ALA A CB  
4120 N N   . GLY A 546 ? 161.5277 161.5277 161.5277 0.0000 0.0000 0.0000 546 GLY A N   
4121 C CA  . GLY A 546 ? 161.4631 161.4631 161.4631 0.0000 0.0000 0.0000 546 GLY A CA  
4122 C C   . GLY A 546 ? 161.3723 161.3723 161.3723 0.0000 0.0000 0.0000 546 GLY A C   
4123 O O   . GLY A 546 ? 161.6182 161.6182 161.6182 0.0000 0.0000 0.0000 546 GLY A O   
4124 N N   . TRP A 547 ? 161.3081 161.3081 161.3081 0.0000 0.0000 0.0000 547 TRP A N   
4125 C CA  . TRP A 547 ? 161.4560 161.4560 161.4560 0.0000 0.0000 0.0000 547 TRP A CA  
4126 C C   . TRP A 547 ? 161.4014 161.4014 161.4014 0.0000 0.0000 0.0000 547 TRP A C   
4127 O O   . TRP A 547 ? 161.5480 161.5480 161.5480 0.0000 0.0000 0.0000 547 TRP A O   
4128 C CB  . TRP A 547 ? 161.6438 161.6438 161.6438 0.0000 0.0000 0.0000 547 TRP A CB  
4129 C CG  . TRP A 547 ? 161.5176 161.5176 161.5176 0.0000 0.0000 0.0000 547 TRP A CG  
4130 C CD1 . TRP A 547 ? 161.5903 161.5903 161.5903 0.0000 0.0000 0.0000 547 TRP A CD1 
4131 C CD2 . TRP A 547 ? 161.2622 161.2622 161.2622 0.0000 0.0000 0.0000 547 TRP A CD2 
4132 N NE1 . TRP A 547 ? 161.3438 161.3438 161.3438 0.0000 0.0000 0.0000 547 TRP A NE1 
4133 C CE2 . TRP A 547 ? 161.3322 161.3322 161.3322 0.0000 0.0000 0.0000 547 TRP A CE2 
4134 C CE3 . TRP A 547 ? 161.2917 161.2917 161.2917 0.0000 0.0000 0.0000 547 TRP A CE3 
4135 C CZ2 . TRP A 547 ? 161.5474 161.5474 161.5474 0.0000 0.0000 0.0000 547 TRP A CZ2 
4136 C CZ3 . TRP A 547 ? 161.2785 161.2785 161.2785 0.0000 0.0000 0.0000 547 TRP A CZ3 
4137 C CH2 . TRP A 547 ? 161.4570 161.4570 161.4570 0.0000 0.0000 0.0000 547 TRP A CH2 
4138 N N   . GLY A 548 ? 161.3775 161.3775 161.3775 0.0000 0.0000 0.0000 548 GLY A N   
4139 C CA  . GLY A 548 ? 161.3900 161.3900 161.3900 0.0000 0.0000 0.0000 548 GLY A CA  
4140 C C   . GLY A 548 ? 161.2276 161.2276 161.2276 0.0000 0.0000 0.0000 548 GLY A C   
4141 O O   . GLY A 548 ? 161.4306 161.4306 161.4306 0.0000 0.0000 0.0000 548 GLY A O   
4142 N N   . MET A 549 ? 161.1979 161.1979 161.1979 0.0000 0.0000 0.0000 549 MET A N   
4143 C CA  . MET A 549 ? 161.3919 161.3919 161.3919 0.0000 0.0000 0.0000 549 MET A CA  
4144 C C   . MET A 549 ? 161.4796 161.4796 161.4796 0.0000 0.0000 0.0000 549 MET A C   
4145 O O   . MET A 549 ? 161.7137 161.7137 161.7137 0.0000 0.0000 0.0000 549 MET A O   
4146 C CB  . MET A 549 ? 161.6076 161.6076 161.6076 0.0000 0.0000 0.0000 549 MET A CB  
4147 C CG  . MET A 549 ? 161.5502 161.5502 161.5502 0.0000 0.0000 0.0000 549 MET A CG  
4148 S SD  . MET A 549 ? 161.1784 161.1784 161.1784 0.0000 0.0000 0.0000 549 MET A SD  
4149 C CE  . MET A 549 ? 161.4009 161.4009 161.4009 0.0000 0.0000 0.0000 549 MET A CE  
4150 N N   . GLY A 550 ? 161.2652 161.2652 161.2652 0.0000 0.0000 0.0000 550 GLY A N   
4151 C CA  . GLY A 550 ? 161.2593 161.2593 161.2593 0.0000 0.0000 0.0000 550 GLY A CA  
4152 C C   . GLY A 550 ? 161.3435 161.3435 161.3435 0.0000 0.0000 0.0000 550 GLY A C   
4153 O O   . GLY A 550 ? 161.5462 161.5462 161.5462 0.0000 0.0000 0.0000 550 GLY A O   
4154 N N   . ILE A 551 ? 161.2711 161.2711 161.2711 0.0000 0.0000 0.0000 551 ILE A N   
4155 C CA  . ILE A 551 ? 161.2589 161.2589 161.2589 0.0000 0.0000 0.0000 551 ILE A CA  
4156 C C   . ILE A 551 ? 161.3803 161.3803 161.3803 0.0000 0.0000 0.0000 551 ILE A C   
4157 O O   . ILE A 551 ? 161.5434 161.5434 161.5434 0.0000 0.0000 0.0000 551 ILE A O   
4158 C CB  . ILE A 551 ? 161.3381 161.3381 161.3381 0.0000 0.0000 0.0000 551 ILE A CB  
4159 C CG1 . ILE A 551 ? 161.3127 161.3127 161.3127 0.0000 0.0000 0.0000 551 ILE A CG1 
4160 C CG2 . ILE A 551 ? 161.3905 161.3905 161.3905 0.0000 0.0000 0.0000 551 ILE A CG2 
4161 C CD1 . ILE A 551 ? 161.3502 161.3502 161.3502 0.0000 0.0000 0.0000 551 ILE A CD1 
4162 N N   . ASP A 552 ? 161.2611 161.2611 161.2611 0.0000 0.0000 0.0000 552 ASP A N   
4163 C CA  . ASP A 552 ? 161.3559 161.3559 161.3559 0.0000 0.0000 0.0000 552 ASP A CA  
4164 C C   . ASP A 552 ? 161.3910 161.3910 161.3910 0.0000 0.0000 0.0000 552 ASP A C   
4165 O O   . ASP A 552 ? 161.7379 161.7379 161.7379 0.0000 0.0000 0.0000 552 ASP A O   
4166 C CB  . ASP A 552 ? 161.5104 161.5104 161.5104 0.0000 0.0000 0.0000 552 ASP A CB  
4167 C CG  . ASP A 552 ? 161.5872 161.5872 161.5872 0.0000 0.0000 0.0000 552 ASP A CG  
4168 O OD1 . ASP A 552 ? 161.5508 161.5508 161.5508 0.0000 0.0000 0.0000 552 ASP A OD1 
4169 O OD2 . ASP A 552 ? 161.7278 161.7278 161.7278 0.0000 0.0000 0.0000 552 ASP A OD2 
4170 N N   . ARG A 553 ? 161.2762 161.2762 161.2762 0.0000 0.0000 0.0000 553 ARG A N   
4171 C CA  . ARG A 553 ? 161.2650 161.2650 161.2650 0.0000 0.0000 0.0000 553 ARG A CA  
4172 C C   . ARG A 553 ? 161.3229 161.3229 161.3229 0.0000 0.0000 0.0000 553 ARG A C   
4173 O O   . ARG A 553 ? 161.6510 161.6510 161.6510 0.0000 0.0000 0.0000 553 ARG A O   
4174 C CB  . ARG A 553 ? 161.3764 161.3764 161.3764 0.0000 0.0000 0.0000 553 ARG A CB  
4175 C CG  . ARG A 553 ? 161.4274 161.4274 161.4274 0.0000 0.0000 0.0000 553 ARG A CG  
4176 C CD  . ARG A 553 ? 161.3327 161.3327 161.3327 0.0000 0.0000 0.0000 553 ARG A CD  
4177 N NE  . ARG A 553 ? 161.1813 161.1813 161.1813 0.0000 0.0000 0.0000 553 ARG A NE  
4178 C CZ  . ARG A 553 ? 161.1992 161.1992 161.1992 0.0000 0.0000 0.0000 553 ARG A CZ  
4179 N NH1 . ARG A 553 ? 161.3212 161.3212 161.3212 0.0000 0.0000 0.0000 553 ARG A NH1 
4180 N NH2 . ARG A 553 ? 161.3435 161.3435 161.3435 0.0000 0.0000 0.0000 553 ARG A NH2 
4181 N N   . VAL A 554 ? 161.2852 161.2852 161.2852 0.0000 0.0000 0.0000 554 VAL A N   
4182 C CA  . VAL A 554 ? 161.3162 161.3162 161.3162 0.0000 0.0000 0.0000 554 VAL A CA  
4183 C C   . VAL A 554 ? 161.4124 161.4124 161.4124 0.0000 0.0000 0.0000 554 VAL A C   
4184 O O   . VAL A 554 ? 161.6564 161.6564 161.6564 0.0000 0.0000 0.0000 554 VAL A O   
4185 C CB  . VAL A 554 ? 161.3502 161.3502 161.3502 0.0000 0.0000 0.0000 554 VAL A CB  
4186 C CG1 . VAL A 554 ? 161.4134 161.4134 161.4134 0.0000 0.0000 0.0000 554 VAL A CG1 
4187 C CG2 . VAL A 554 ? 161.5505 161.5505 161.5505 0.0000 0.0000 0.0000 554 VAL A CG2 
4188 N N   . ALA A 555 ? 161.3454 161.3454 161.3454 0.0000 0.0000 0.0000 555 ALA A N   
4189 C CA  . ALA A 555 ? 161.3577 161.3577 161.3577 0.0000 0.0000 0.0000 555 ALA A CA  
4190 C C   . ALA A 555 ? 161.4175 161.4175 161.4175 0.0000 0.0000 0.0000 555 ALA A C   
4191 O O   . ALA A 555 ? 161.4871 161.4871 161.4871 0.0000 0.0000 0.0000 555 ALA A O   
4192 C CB  . ALA A 555 ? 161.6429 161.6429 161.6429 0.0000 0.0000 0.0000 555 ALA A CB  
4193 N N   . MET A 556 ? 161.5665 161.5665 161.5665 0.0000 0.0000 0.0000 556 MET A N   
4194 C CA  . MET A 556 ? 161.4550 161.4550 161.4550 0.0000 0.0000 0.0000 556 MET A CA  
4195 C C   . MET A 556 ? 161.3623 161.3623 161.3623 0.0000 0.0000 0.0000 556 MET A C   
4196 O O   . MET A 556 ? 161.5312 161.5312 161.5312 0.0000 0.0000 0.0000 556 MET A O   
4197 C CB  . MET A 556 ? 161.4370 161.4370 161.4370 0.0000 0.0000 0.0000 556 MET A CB  
4198 C CG  . MET A 556 ? 161.5465 161.5465 161.5465 0.0000 0.0000 0.0000 556 MET A CG  
4199 S SD  . MET A 556 ? 161.4014 161.4014 161.4014 0.0000 0.0000 0.0000 556 MET A SD  
4200 C CE  . MET A 556 ? 161.5349 161.5349 161.5349 0.0000 0.0000 0.0000 556 MET A CE  
4201 N N   . PHE A 557 ? 161.4580 161.4580 161.4580 0.0000 0.0000 0.0000 557 PHE A N   
4202 C CA  . PHE A 557 ? 161.3289 161.3289 161.3289 0.0000 0.0000 0.0000 557 PHE A CA  
4203 C C   . PHE A 557 ? 161.2659 161.2659 161.2659 0.0000 0.0000 0.0000 557 PHE A C   
4204 O O   . PHE A 557 ? 161.3446 161.3446 161.3446 0.0000 0.0000 0.0000 557 PHE A O   
4205 C CB  . PHE A 557 ? 161.4217 161.4217 161.4217 0.0000 0.0000 0.0000 557 PHE A CB  
4206 C CG  . PHE A 557 ? 161.2446 161.2446 161.2446 0.0000 0.0000 0.0000 557 PHE A CG  
4207 C CD1 . PHE A 557 ? 161.3111 161.3111 161.3111 0.0000 0.0000 0.0000 557 PHE A CD1 
4208 C CD2 . PHE A 557 ? 161.3383 161.3383 161.3383 0.0000 0.0000 0.0000 557 PHE A CD2 
4209 C CE1 . PHE A 557 ? 161.4483 161.4483 161.4483 0.0000 0.0000 0.0000 557 PHE A CE1 
4210 C CE2 . PHE A 557 ? 161.3790 161.3790 161.3790 0.0000 0.0000 0.0000 557 PHE A CE2 
4211 C CZ  . PHE A 557 ? 161.4236 161.4236 161.4236 0.0000 0.0000 0.0000 557 PHE A CZ  
4212 N N   . LEU A 558 ? 161.3235 161.3235 161.3235 0.0000 0.0000 0.0000 558 LEU A N   
4213 C CA  . LEU A 558 ? 161.3770 161.3770 161.3770 0.0000 0.0000 0.0000 558 LEU A CA  
4214 C C   . LEU A 558 ? 161.4690 161.4690 161.4690 0.0000 0.0000 0.0000 558 LEU A C   
4215 O O   . LEU A 558 ? 161.5163 161.5163 161.5163 0.0000 0.0000 0.0000 558 LEU A O   
4216 C CB  . LEU A 558 ? 161.4418 161.4418 161.4418 0.0000 0.0000 0.0000 558 LEU A CB  
4217 C CG  . LEU A 558 ? 161.2672 161.2672 161.2672 0.0000 0.0000 0.0000 558 LEU A CG  
4218 C CD1 . LEU A 558 ? 161.3246 161.3246 161.3246 0.0000 0.0000 0.0000 558 LEU A CD1 
4219 C CD2 . LEU A 558 ? 161.3625 161.3625 161.3625 0.0000 0.0000 0.0000 558 LEU A CD2 
4220 N N   . THR A 559 ? 161.4912 161.4912 161.4912 0.0000 0.0000 0.0000 559 THR A N   
4221 C CA  . THR A 559 ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 559 THR A CA  
4222 C C   . THR A 559 ? 161.3250 161.3250 161.3250 0.0000 0.0000 0.0000 559 THR A C   
4223 O O   . THR A 559 ? 161.3079 161.3079 161.3079 0.0000 0.0000 0.0000 559 THR A O   
4224 C CB  . THR A 559 ? 161.4209 161.4209 161.4209 0.0000 0.0000 0.0000 559 THR A CB  
4225 O OG1 . THR A 559 ? 161.7189 161.7189 161.7189 0.0000 0.0000 0.0000 559 THR A OG1 
4226 C CG2 . THR A 559 ? 161.4772 161.4772 161.4772 0.0000 0.0000 0.0000 559 THR A CG2 
4227 N N   . ASP A 560 ? 161.5202 161.5202 161.5202 0.0000 0.0000 0.0000 560 ASP A N   
4228 C CA  . ASP A 560 ? 161.4254 161.4254 161.4254 0.0000 0.0000 0.0000 560 ASP A CA  
4229 C C   . ASP A 560 ? 161.3243 161.3243 161.3243 0.0000 0.0000 0.0000 560 ASP A C   
4230 O O   . ASP A 560 ? 161.4200 161.4200 161.4200 0.0000 0.0000 0.0000 560 ASP A O   
4231 C CB  . ASP A 560 ? 161.3542 161.3542 161.3542 0.0000 0.0000 0.0000 560 ASP A CB  
4232 C CG  . ASP A 560 ? 161.5386 161.5386 161.5386 0.0000 0.0000 0.0000 560 ASP A CG  
4233 O OD1 . ASP A 560 ? 161.7279 161.7279 161.7279 0.0000 0.0000 0.0000 560 ASP A OD1 
4234 O OD2 . ASP A 560 ? 161.5813 161.5813 161.5813 0.0000 0.0000 0.0000 560 ASP A OD2 
4235 N N   . SER A 561 ? 161.3264 161.3264 161.3264 0.0000 0.0000 0.0000 561 SER A N   
4236 C CA  . SER A 561 ? 161.3030 161.3030 161.3030 0.0000 0.0000 0.0000 561 SER A CA  
4237 C C   . SER A 561 ? 161.4198 161.4198 161.4198 0.0000 0.0000 0.0000 561 SER A C   
4238 O O   . SER A 561 ? 161.6157 161.6157 161.6157 0.0000 0.0000 0.0000 561 SER A O   
4239 C CB  . SER A 561 ? 161.4078 161.4078 161.4078 0.0000 0.0000 0.0000 561 SER A CB  
4240 O OG  . SER A 561 ? 161.5458 161.5458 161.5458 0.0000 0.0000 0.0000 561 SER A OG  
4241 N N   . ASN A 562 ? 161.3673 161.3673 161.3673 0.0000 0.0000 0.0000 562 ASN A N   
4242 C CA  . ASN A 562 ? 161.2958 161.2958 161.2958 0.0000 0.0000 0.0000 562 ASN A CA  
4243 C C   . ASN A 562 ? 161.2767 161.2767 161.2767 0.0000 0.0000 0.0000 562 ASN A C   
4244 O O   . ASN A 562 ? 161.4754 161.4754 161.4754 0.0000 0.0000 0.0000 562 ASN A O   
4245 C CB  . ASN A 562 ? 161.3946 161.3946 161.3946 0.0000 0.0000 0.0000 562 ASN A CB  
4246 C CG  . ASN A 562 ? 161.5002 161.5002 161.5002 0.0000 0.0000 0.0000 562 ASN A CG  
4247 O OD1 . ASN A 562 ? 161.4894 161.4894 161.4894 0.0000 0.0000 0.0000 562 ASN A OD1 
4248 N ND2 . ASN A 562 ? 161.7988 161.7988 161.7988 0.0000 0.0000 0.0000 562 ASN A ND2 
4249 N N   . ASN A 563 ? 161.2726 161.2726 161.2726 0.0000 0.0000 0.0000 563 ASN A N   
4250 C CA  . ASN A 563 ? 161.2351 161.2351 161.2351 0.0000 0.0000 0.0000 563 ASN A CA  
4251 C C   . ASN A 563 ? 161.2366 161.2366 161.2366 0.0000 0.0000 0.0000 563 ASN A C   
4252 O O   . ASN A 563 ? 161.6458 161.6458 161.6458 0.0000 0.0000 0.0000 563 ASN A O   
4253 C CB  . ASN A 563 ? 161.2055 161.2055 161.2055 0.0000 0.0000 0.0000 563 ASN A CB  
4254 C CG  . ASN A 563 ? 160.8037 160.8037 160.8037 0.0000 0.0000 0.0000 563 ASN A CG  
4255 O OD1 . ASN A 563 ? 161.1845 161.1845 161.1845 0.0000 0.0000 0.0000 563 ASN A OD1 
4256 N ND2 . ASN A 563 ? 160.1252 160.1252 160.1252 0.0000 0.0000 0.0000 563 ASN A ND2 
4257 N N   . ILE A 564 ? 161.1925 161.1925 161.1925 0.0000 0.0000 0.0000 564 ILE A N   
4258 C CA  . ILE A 564 ? 161.3622 161.3622 161.3622 0.0000 0.0000 0.0000 564 ILE A CA  
4259 C C   . ILE A 564 ? 161.5262 161.5262 161.5262 0.0000 0.0000 0.0000 564 ILE A C   
4260 O O   . ILE A 564 ? 161.6792 161.6792 161.6792 0.0000 0.0000 0.0000 564 ILE A O   
4261 C CB  . ILE A 564 ? 161.3246 161.3246 161.3246 0.0000 0.0000 0.0000 564 ILE A CB  
4262 C CG1 . ILE A 564 ? 161.2336 161.2336 161.2336 0.0000 0.0000 0.0000 564 ILE A CG1 
4263 C CG2 . ILE A 564 ? 161.6352 161.6352 161.6352 0.0000 0.0000 0.0000 564 ILE A CG2 
4264 C CD1 . ILE A 564 ? 161.5197 161.5197 161.5197 0.0000 0.0000 0.0000 564 ILE A CD1 
4265 N N   . LYS A 565 ? 161.4194 161.4194 161.4194 0.0000 0.0000 0.0000 565 LYS A N   
4266 C CA  . LYS A 565 ? 161.4064 161.4064 161.4064 0.0000 0.0000 0.0000 565 LYS A CA  
4267 C C   . LYS A 565 ? 161.3462 161.3462 161.3462 0.0000 0.0000 0.0000 565 LYS A C   
4268 O O   . LYS A 565 ? 161.4710 161.4710 161.4710 0.0000 0.0000 0.0000 565 LYS A O   
4269 C CB  . LYS A 565 ? 161.5822 161.5822 161.5822 0.0000 0.0000 0.0000 565 LYS A CB  
4270 C CG  . LYS A 565 ? 161.4598 161.4598 161.4598 0.0000 0.0000 0.0000 565 LYS A CG  
4271 C CD  . LYS A 565 ? 161.2740 161.2740 161.2740 0.0000 0.0000 0.0000 565 LYS A CD  
4272 C CE  . LYS A 565 ? 161.2346 161.2346 161.2346 0.0000 0.0000 0.0000 565 LYS A CE  
4273 N NZ  . LYS A 565 ? 161.5340 161.5340 161.5340 0.0000 0.0000 0.0000 565 LYS A NZ  
4274 N N   . GLU A 566 ? 161.2379 161.2379 161.2379 0.0000 0.0000 0.0000 566 GLU A N   
4275 C CA  . GLU A 566 ? 161.2439 161.2439 161.2439 0.0000 0.0000 0.0000 566 GLU A CA  
4276 C C   . GLU A 566 ? 161.3078 161.3078 161.3078 0.0000 0.0000 0.0000 566 GLU A C   
4277 O O   . GLU A 566 ? 161.5583 161.5583 161.5583 0.0000 0.0000 0.0000 566 GLU A O   
4278 C CB  . GLU A 566 ? 161.3673 161.3673 161.3673 0.0000 0.0000 0.0000 566 GLU A CB  
4279 C CG  . GLU A 566 ? 161.4863 161.4863 161.4863 0.0000 0.0000 0.0000 566 GLU A CG  
4280 C CD  . GLU A 566 ? 161.5866 161.5866 161.5866 0.0000 0.0000 0.0000 566 GLU A CD  
4281 O OE1 . GLU A 566 ? 161.4728 161.4728 161.4728 0.0000 0.0000 0.0000 566 GLU A OE1 
4282 O OE2 . GLU A 566 ? 161.7831 161.7831 161.7831 0.0000 0.0000 0.0000 566 GLU A OE2 
4283 N N   . VAL A 567 ? 161.3537 161.3537 161.3537 0.0000 0.0000 0.0000 567 VAL A N   
4284 C CA  . VAL A 567 ? 161.4314 161.4314 161.4314 0.0000 0.0000 0.0000 567 VAL A CA  
4285 C C   . VAL A 567 ? 161.4065 161.4065 161.4065 0.0000 0.0000 0.0000 567 VAL A C   
4286 O O   . VAL A 567 ? 161.4845 161.4845 161.4845 0.0000 0.0000 0.0000 567 VAL A O   
4287 C CB  . VAL A 567 ? 161.3886 161.3886 161.3886 0.0000 0.0000 0.0000 567 VAL A CB  
4288 C CG1 . VAL A 567 ? 161.4509 161.4509 161.4509 0.0000 0.0000 0.0000 567 VAL A CG1 
4289 C CG2 . VAL A 567 ? 161.5715 161.5715 161.5715 0.0000 0.0000 0.0000 567 VAL A CG2 
4290 N N   . LEU A 568 ? 161.2013 161.2013 161.2013 0.0000 0.0000 0.0000 568 LEU A N   
4291 C CA  . LEU A 568 ? 161.1913 161.1913 161.1913 0.0000 0.0000 0.0000 568 LEU A CA  
4292 C C   . LEU A 568 ? 161.3177 161.3177 161.3177 0.0000 0.0000 0.0000 568 LEU A C   
4293 O O   . LEU A 568 ? 161.4390 161.4390 161.4390 0.0000 0.0000 0.0000 568 LEU A O   
4294 C CB  . LEU A 568 ? 161.3398 161.3398 161.3398 0.0000 0.0000 0.0000 568 LEU A CB  
4295 C CG  . LEU A 568 ? 161.4121 161.4121 161.4121 0.0000 0.0000 0.0000 568 LEU A CG  
4296 C CD1 . LEU A 568 ? 161.5244 161.5244 161.5244 0.0000 0.0000 0.0000 568 LEU A CD1 
4297 C CD2 . LEU A 568 ? 161.5188 161.5188 161.5188 0.0000 0.0000 0.0000 568 LEU A CD2 
4298 N N   . LEU A 569 ? 161.5156 161.5156 161.5156 0.0000 0.0000 0.0000 569 LEU A N   
4299 C CA  . LEU A 569 ? 161.4703 161.4703 161.4703 0.0000 0.0000 0.0000 569 LEU A CA  
4300 C C   . LEU A 569 ? 161.4710 161.4710 161.4710 0.0000 0.0000 0.0000 569 LEU A C   
4301 O O   . LEU A 569 ? 161.5356 161.5356 161.5356 0.0000 0.0000 0.0000 569 LEU A O   
4302 C CB  . LEU A 569 ? 161.4662 161.4662 161.4662 0.0000 0.0000 0.0000 569 LEU A CB  
4303 C CG  . LEU A 569 ? 161.4695 161.4695 161.4695 0.0000 0.0000 0.0000 569 LEU A CG  
4304 C CD1 . LEU A 569 ? 161.5877 161.5877 161.5877 0.0000 0.0000 0.0000 569 LEU A CD1 
4305 C CD2 . LEU A 569 ? 161.6815 161.6815 161.6815 0.0000 0.0000 0.0000 569 LEU A CD2 
4306 N N   . PHE A 570 ? 161.3605 161.3605 161.3605 0.0000 0.0000 0.0000 570 PHE A N   
4307 C CA  . PHE A 570 ? 161.3326 161.3326 161.3326 0.0000 0.0000 0.0000 570 PHE A CA  
4308 C C   . PHE A 570 ? 161.2071 161.2071 161.2071 0.0000 0.0000 0.0000 570 PHE A C   
4309 O O   . PHE A 570 ? 161.3615 161.3615 161.3615 0.0000 0.0000 0.0000 570 PHE A O   
4310 C CB  . PHE A 570 ? 161.4470 161.4470 161.4470 0.0000 0.0000 0.0000 570 PHE A CB  
4311 C CG  . PHE A 570 ? 161.3162 161.3162 161.3162 0.0000 0.0000 0.0000 570 PHE A CG  
4312 C CD1 . PHE A 570 ? 161.4497 161.4497 161.4497 0.0000 0.0000 0.0000 570 PHE A CD1 
4313 C CD2 . PHE A 570 ? 161.4244 161.4244 161.4244 0.0000 0.0000 0.0000 570 PHE A CD2 
4314 C CE1 . PHE A 570 ? 161.4946 161.4946 161.4946 0.0000 0.0000 0.0000 570 PHE A CE1 
4315 C CE2 . PHE A 570 ? 161.3737 161.3737 161.3737 0.0000 0.0000 0.0000 570 PHE A CE2 
4316 C CZ  . PHE A 570 ? 161.3287 161.3287 161.3287 0.0000 0.0000 0.0000 570 PHE A CZ  
4317 N N   . PRO A 571 ? 160.9906 160.9906 160.9906 0.0000 0.0000 0.0000 571 PRO A N   
4318 C CA  . PRO A 571 ? 161.2268 161.2268 161.2268 0.0000 0.0000 0.0000 571 PRO A CA  
4319 C C   . PRO A 571 ? 161.4670 161.4670 161.4670 0.0000 0.0000 0.0000 571 PRO A C   
4320 O O   . PRO A 571 ? 161.7115 161.7115 161.7115 0.0000 0.0000 0.0000 571 PRO A O   
4321 C CB  . PRO A 571 ? 161.3756 161.3756 161.3756 0.0000 0.0000 0.0000 571 PRO A CB  
4322 C CG  . PRO A 571 ? 161.2818 161.2818 161.2818 0.0000 0.0000 0.0000 571 PRO A CG  
4323 C CD  . PRO A 571 ? 161.2239 161.2239 161.2239 0.0000 0.0000 0.0000 571 PRO A CD  
4324 N N   . ALA A 572 ? 161.4154 161.4154 161.4154 0.0000 0.0000 0.0000 572 ALA A N   
4325 C CA  . ALA A 572 ? 161.4588 161.4588 161.4588 0.0000 0.0000 0.0000 572 ALA A CA  
4326 C C   . ALA A 572 ? 161.5775 161.5775 161.5775 0.0000 0.0000 0.0000 572 ALA A C   
4327 O O   . ALA A 572 ? 161.3538 161.3538 161.3538 0.0000 0.0000 0.0000 572 ALA A O   
4328 C CB  . ALA A 572 ? 161.5339 161.5339 161.5339 0.0000 0.0000 0.0000 572 ALA A CB  
4329 N N   . MET A 573 ? 166.2248 166.2248 166.2248 0.0000 0.0000 0.0000 573 MET A N   
4330 C CA  . MET A 573 ? 165.9934 165.9934 165.9934 0.0000 0.0000 0.0000 573 MET A CA  
4331 C C   . MET A 573 ? 165.8012 165.8012 165.8012 0.0000 0.0000 0.0000 573 MET A C   
4332 O O   . MET A 573 ? 166.3219 166.3219 166.3219 0.0000 0.0000 0.0000 573 MET A O   
4333 C CB  . MET A 573 ? 166.0655 166.0655 166.0655 0.0000 0.0000 0.0000 573 MET A CB  
4334 C CG  . MET A 573 ? 166.2350 166.2350 166.2350 0.0000 0.0000 0.0000 573 MET A CG  
4335 S SD  . MET A 573 ? 165.5964 165.5964 165.5964 0.0000 0.0000 0.0000 573 MET A SD  
4336 C CE  . MET A 573 ? 165.1025 165.1025 165.1025 0.0000 0.0000 0.0000 573 MET A CE  
4337 N N   . LYS A 574 ? 160.1015 160.1015 160.1015 0.0000 0.0000 0.0000 574 LYS A N   
4338 C CA  . LYS A 574 ? 160.8286 160.8286 160.8286 0.0000 0.0000 0.0000 574 LYS A CA  
4339 C C   . LYS A 574 ? 160.8471 160.8471 160.8471 0.0000 0.0000 0.0000 574 LYS A C   
4340 O O   . LYS A 574 ? 160.3586 160.3586 160.3586 0.0000 0.0000 0.0000 574 LYS A O   
4341 C CB  . LYS A 574 ? 159.4432 159.4432 159.4432 0.0000 0.0000 0.0000 574 LYS A CB  
4342 C CG  . LYS A 574 ? 160.4519 160.4519 160.4519 0.0000 0.0000 0.0000 574 LYS A CG  
4343 C CD  . LYS A 574 ? 159.9393 159.9393 159.9393 0.0000 0.0000 0.0000 574 LYS A CD  
4344 C CE  . LYS A 574 ? 159.9437 159.9437 159.9437 0.0000 0.0000 0.0000 574 LYS A CE  
4345 N NZ  . LYS A 574 ? 160.9298 160.9298 160.9298 0.0000 0.0000 0.0000 574 LYS A NZ  
4346 N N   . PRO A 575 ? 173.3825 173.3825 173.3825 0.0000 0.0000 0.0000 575 PRO A N   
4347 C CA  . PRO A 575 ? 174.1062 174.1062 174.1062 0.0000 0.0000 0.0000 575 PRO A CA  
4348 C C   . PRO A 575 ? 174.3046 174.3046 174.3046 0.0000 0.0000 0.0000 575 PRO A C   
4349 O O   . PRO A 575 ? 173.0806 173.0806 173.0806 0.0000 0.0000 0.0000 575 PRO A O   
4350 C CB  . PRO A 575 ? 174.1550 174.1550 174.1550 0.0000 0.0000 0.0000 575 PRO A CB  
4351 C CG  . PRO A 575 ? 173.8451 173.8451 173.8451 0.0000 0.0000 0.0000 575 PRO A CG  
4352 C CD  . PRO A 575 ? 173.5955 173.5955 173.5955 0.0000 0.0000 0.0000 575 PRO A CD  
4353 N N   . GLU A 576 ? 200.0124 200.0124 200.0124 0.0000 0.0000 0.0000 576 GLU A N   
4354 C CA  . GLU A 576 ? 200.8316 200.8316 200.8316 0.0000 0.0000 0.0000 576 GLU A CA  
4355 C C   . GLU A 576 ? 202.3634 202.3634 202.3634 0.0000 0.0000 0.0000 576 GLU A C   
4356 O O   . GLU A 576 ? 202.5429 202.5429 202.5429 0.0000 0.0000 0.0000 576 GLU A O   
4357 C CB  . GLU A 576 ? 201.3911 201.3911 201.3911 0.0000 0.0000 0.0000 576 GLU A CB  
4358 C CG  . GLU A 576 ? 201.2855 201.2855 201.2855 0.0000 0.0000 0.0000 576 GLU A CG  
4359 C CD  . GLU A 576 ? 201.4340 201.4340 201.4340 0.0000 0.0000 0.0000 576 GLU A CD  
4360 O OE1 . GLU A 576 ? 201.3995 201.3995 201.3995 0.0000 0.0000 0.0000 576 GLU A OE1 
4361 O OE2 . GLU A 576 ? 201.6130 201.6130 201.6130 0.0000 0.0000 0.0000 576 GLU A OE2 
4362 N N   . ASP A 577 ? 221.8105 221.8105 221.8105 0.0000 0.0000 0.0000 577 ASP A N   
4363 C CA  . ASP A 577 ? 222.4402 222.4402 222.4402 0.0000 0.0000 0.0000 577 ASP A CA  
4364 C C   . ASP A 577 ? 223.3158 223.3158 223.3158 0.0000 0.0000 0.0000 577 ASP A C   
4365 O O   . ASP A 577 ? 223.1247 223.1247 223.1247 0.0000 0.0000 0.0000 577 ASP A O   
4366 C CB  . ASP A 577 ? 222.3770 222.3770 222.3770 0.0000 0.0000 0.0000 577 ASP A CB  
4367 C CG  . ASP A 577 ? 221.8761 221.8761 221.8761 0.0000 0.0000 0.0000 577 ASP A CG  
4368 O OD1 . ASP A 577 ? 220.4387 220.4387 220.4387 0.0000 0.0000 0.0000 577 ASP A OD1 
4369 O OD2 . ASP A 577 ? 222.2866 222.2866 222.2866 0.0000 0.0000 0.0000 577 ASP A OD2 
4370 N N   . LYS A 578 ? 252.6949 252.6949 252.6949 0.0000 0.0000 0.0000 578 LYS A N   
4371 C CA  . LYS A 578 ? 253.1949 253.1949 253.1949 0.0000 0.0000 0.0000 578 LYS A CA  
4372 C C   . LYS A 578 ? 253.5397 253.5397 253.5397 0.0000 0.0000 0.0000 578 LYS A C   
4373 O O   . LYS A 578 ? 253.5642 253.5642 253.5642 0.0000 0.0000 0.0000 578 LYS A O   
4374 C CB  . LYS A 578 ? 253.3863 253.3863 253.3863 0.0000 0.0000 0.0000 578 LYS A CB  
4375 C CG  . LYS A 578 ? 253.3640 253.3640 253.3640 0.0000 0.0000 0.0000 578 LYS A CG  
4376 C CD  . LYS A 578 ? 253.5432 253.5432 253.5432 0.0000 0.0000 0.0000 578 LYS A CD  
4377 C CE  . LYS A 578 ? 253.5720 253.5720 253.5720 0.0000 0.0000 0.0000 578 LYS A CE  
4378 N NZ  . LYS A 578 ? 253.3680 253.3680 253.3680 0.0000 0.0000 0.0000 578 LYS A NZ  
4379 N N   . LYS A 579 ? 256.4336 256.4336 256.4336 0.0000 0.0000 0.0000 579 LYS A N   
4380 C CA  . LYS A 579 ? 256.5895 256.5895 256.5895 0.0000 0.0000 0.0000 579 LYS A CA  
4381 C C   . LYS A 579 ? 256.5895 256.5895 256.5895 0.0000 0.0000 0.0000 579 LYS A C   
4382 O O   . LYS A 579 ? 256.5903 256.5903 256.5903 0.0000 0.0000 0.0000 579 LYS A O   
4383 C CB  . LYS A 579 ? 256.6118 256.6118 256.6118 0.0000 0.0000 0.0000 579 LYS A CB  
4384 C CG  . LYS A 579 ? 256.5783 256.5783 256.5783 0.0000 0.0000 0.0000 579 LYS A CG  
4385 C CD  . LYS A 579 ? 256.3765 256.3765 256.3765 0.0000 0.0000 0.0000 579 LYS A CD  
4386 C CE  . LYS A 579 ? 255.8347 255.8347 255.8347 0.0000 0.0000 0.0000 579 LYS A CE  
4387 N NZ  . LYS A 579 ? 253.7270 253.7270 253.7270 0.0000 0.0000 0.0000 579 LYS A NZ  
4388 N N   . VAL B 71  ? 197.2444 197.2444 197.2444 0.0000 0.0000 0.0000 71  VAL B N   
4389 C CA  . VAL B 71  ? 199.0784 199.0784 199.0784 0.0000 0.0000 0.0000 71  VAL B CA  
4390 C C   . VAL B 71  ? 199.1590 199.1590 199.1590 0.0000 0.0000 0.0000 71  VAL B C   
4391 O O   . VAL B 71  ? 199.0275 199.0275 199.0275 0.0000 0.0000 0.0000 71  VAL B O   
4392 C CB  . VAL B 71  ? 199.0062 199.0062 199.0062 0.0000 0.0000 0.0000 71  VAL B CB  
4393 C CG1 . VAL B 71  ? 198.8643 198.8643 198.8643 0.0000 0.0000 0.0000 71  VAL B CG1 
4394 C CG2 . VAL B 71  ? 175.3748 175.3748 175.3748 0.0000 0.0000 0.0000 71  VAL B CG2 
4395 N N   . ASP B 72  ? 174.4186 174.4186 174.4186 0.0000 0.0000 0.0000 72  ASP B N   
4396 C CA  . ASP B 72  ? 173.9343 173.9343 173.9343 0.0000 0.0000 0.0000 72  ASP B CA  
4397 C C   . ASP B 72  ? 174.0053 174.0053 174.0053 0.0000 0.0000 0.0000 72  ASP B C   
4398 O O   . ASP B 72  ? 174.5686 174.5686 174.5686 0.0000 0.0000 0.0000 72  ASP B O   
4399 C CB  . ASP B 72  ? 174.0042 174.0042 174.0042 0.0000 0.0000 0.0000 72  ASP B CB  
4400 C CG  . ASP B 72  ? 173.9081 173.9081 173.9081 0.0000 0.0000 0.0000 72  ASP B CG  
4401 O OD1 . ASP B 72  ? 174.0466 174.0466 174.0466 0.0000 0.0000 0.0000 72  ASP B OD1 
4402 O OD2 . ASP B 72  ? 173.8906 173.8906 173.8906 0.0000 0.0000 0.0000 72  ASP B OD2 
4403 N N   . PRO B 73  ? 173.9389 173.9389 173.9389 0.0000 0.0000 0.0000 73  PRO B N   
4404 C CA  . PRO B 73  ? 173.9222 173.9222 173.9222 0.0000 0.0000 0.0000 73  PRO B CA  
4405 C C   . PRO B 73  ? 173.8330 173.8330 173.8330 0.0000 0.0000 0.0000 73  PRO B C   
4406 O O   . PRO B 73  ? 162.9136 162.9136 162.9136 0.0000 0.0000 0.0000 73  PRO B O   
4407 C CB  . PRO B 73  ? 162.3238 162.3238 162.3238 0.0000 0.0000 0.0000 73  PRO B CB  
4408 C CG  . PRO B 73  ? 162.4129 162.4129 162.4129 0.0000 0.0000 0.0000 73  PRO B CG  
4409 C CD  . PRO B 73  ? 162.2993 162.2993 162.2993 0.0000 0.0000 0.0000 73  PRO B CD  
4410 N N   . ASN B 74  ? 162.0829 162.0829 162.0829 0.0000 0.0000 0.0000 74  ASN B N   
4411 C CA  . ASN B 74  ? 161.5162 161.5162 161.5162 0.0000 0.0000 0.0000 74  ASN B CA  
4412 C C   . ASN B 74  ? 161.4889 161.4889 161.4889 0.0000 0.0000 0.0000 74  ASN B C   
4413 O O   . ASN B 74  ? 161.4880 161.4880 161.4880 0.0000 0.0000 0.0000 74  ASN B O   
4414 C CB  . ASN B 74  ? 161.5549 161.5549 161.5549 0.0000 0.0000 0.0000 74  ASN B CB  
4415 C CG  . ASN B 74  ? 161.3967 161.3967 161.3967 0.0000 0.0000 0.0000 74  ASN B CG  
4416 O OD1 . ASN B 74  ? 161.4619 161.4619 161.4619 0.0000 0.0000 0.0000 74  ASN B OD1 
4417 N ND2 . ASN B 74  ? 161.4535 161.4535 161.4535 0.0000 0.0000 0.0000 74  ASN B ND2 
4418 N N   . GLN B 75  ? 169.4503 169.4503 169.4503 0.0000 0.0000 0.0000 75  GLN B N   
4419 C CA  . GLN B 75  ? 169.2333 169.2333 169.2333 0.0000 0.0000 0.0000 75  GLN B CA  
4420 C C   . GLN B 75  ? 169.1998 169.1998 169.1998 0.0000 0.0000 0.0000 75  GLN B C   
4421 O O   . GLN B 75  ? 169.3962 169.3962 169.3962 0.0000 0.0000 0.0000 75  GLN B O   
4422 C CB  . GLN B 75  ? 169.3784 169.3784 169.3784 0.0000 0.0000 0.0000 75  GLN B CB  
4423 C CG  . GLN B 75  ? 169.2373 169.2373 169.2373 0.0000 0.0000 0.0000 75  GLN B CG  
4424 C CD  . GLN B 75  ? 169.2765 169.2765 169.2765 0.0000 0.0000 0.0000 75  GLN B CD  
4425 O OE1 . GLN B 75  ? 169.4889 169.4889 169.4889 0.0000 0.0000 0.0000 75  GLN B OE1 
4426 N NE2 . GLN B 75  ? 169.4390 169.4390 169.4390 0.0000 0.0000 0.0000 75  GLN B NE2 
4427 N N   . TYR B 76  ? 163.7444 163.7444 163.7444 0.0000 0.0000 0.0000 76  TYR B N   
4428 C CA  . TYR B 76  ? 163.4150 163.4150 163.4150 0.0000 0.0000 0.0000 76  TYR B CA  
4429 C C   . TYR B 76  ? 163.5249 163.5249 163.5249 0.0000 0.0000 0.0000 76  TYR B C   
4430 O O   . TYR B 76  ? 163.5348 163.5348 163.5348 0.0000 0.0000 0.0000 76  TYR B O   
4431 C CB  . TYR B 76  ? 163.3156 163.3156 163.3156 0.0000 0.0000 0.0000 76  TYR B CB  
4432 C CG  . TYR B 76  ? 163.3128 163.3128 163.3128 0.0000 0.0000 0.0000 76  TYR B CG  
4433 C CD1 . TYR B 76  ? 163.2911 163.2911 163.2911 0.0000 0.0000 0.0000 76  TYR B CD1 
4434 C CD2 . TYR B 76  ? 163.2442 163.2442 163.2442 0.0000 0.0000 0.0000 76  TYR B CD2 
4435 C CE1 . TYR B 76  ? 168.0063 168.0063 168.0063 0.0000 0.0000 0.0000 76  TYR B CE1 
4436 C CE2 . TYR B 76  ? 168.0370 168.0370 168.0370 0.0000 0.0000 0.0000 76  TYR B CE2 
4437 C CZ  . TYR B 76  ? 168.0910 168.0910 168.0910 0.0000 0.0000 0.0000 76  TYR B CZ  
4438 O OH  . TYR B 76  ? 168.3391 168.3391 168.3391 0.0000 0.0000 0.0000 76  TYR B OH  
4439 N N   . TYR B 77  ? 168.1196 168.1196 168.1196 0.0000 0.0000 0.0000 77  TYR B N   
4440 C CA  . TYR B 77  ? 168.2183 168.2183 168.2183 0.0000 0.0000 0.0000 77  TYR B CA  
4441 C C   . TYR B 77  ? 168.0551 168.0551 168.0551 0.0000 0.0000 0.0000 77  TYR B C   
4442 O O   . TYR B 77  ? 168.0237 168.0237 168.0237 0.0000 0.0000 0.0000 77  TYR B O   
4443 C CB  . TYR B 77  ? 168.1426 168.1426 168.1426 0.0000 0.0000 0.0000 77  TYR B CB  
4444 C CG  . TYR B 77  ? 168.2788 168.2788 168.2788 0.0000 0.0000 0.0000 77  TYR B CG  
4445 C CD1 . TYR B 77  ? 168.0750 168.0750 168.0750 0.0000 0.0000 0.0000 77  TYR B CD1 
4446 C CD2 . TYR B 77  ? 169.9371 169.9371 169.9371 0.0000 0.0000 0.0000 77  TYR B CD2 
4447 C CE1 . TYR B 77  ? 170.2132 170.2132 170.2132 0.0000 0.0000 0.0000 77  TYR B CE1 
4448 C CE2 . TYR B 77  ? 170.4537 170.4537 170.4537 0.0000 0.0000 0.0000 77  TYR B CE2 
4449 C CZ  . TYR B 77  ? 170.7021 170.7021 170.7021 0.0000 0.0000 0.0000 77  TYR B CZ  
4450 O OH  . TYR B 77  ? 170.3878 170.3878 170.3878 0.0000 0.0000 0.0000 77  TYR B OH  
4451 N N   . LYS B 78  ? 170.2595 170.2595 170.2595 0.0000 0.0000 0.0000 78  LYS B N   
4452 C CA  . LYS B 78  ? 174.4639 174.4639 174.4639 0.0000 0.0000 0.0000 78  LYS B CA  
4453 C C   . LYS B 78  ? 174.7129 174.7129 174.7129 0.0000 0.0000 0.0000 78  LYS B C   
4454 O O   . LYS B 78  ? 174.5200 174.5200 174.5200 0.0000 0.0000 0.0000 78  LYS B O   
4455 C CB  . LYS B 78  ? 174.7467 174.7467 174.7467 0.0000 0.0000 0.0000 78  LYS B CB  
4456 C CG  . LYS B 78  ? 174.8083 174.8083 174.8083 0.0000 0.0000 0.0000 78  LYS B CG  
4457 C CD  . LYS B 78  ? 174.9934 174.9934 174.9934 0.0000 0.0000 0.0000 78  LYS B CD  
4458 C CE  . LYS B 78  ? 175.0781 175.0781 175.0781 0.0000 0.0000 0.0000 78  LYS B CE  
4459 N NZ  . LYS B 78  ? 175.0894 175.0894 175.0894 0.0000 0.0000 0.0000 78  LYS B NZ  
4460 N N   . ILE B 79  ? 175.1941 175.1941 175.1941 0.0000 0.0000 0.0000 79  ILE B N   
4461 C CA  . ILE B 79  ? 167.0509 167.0509 167.0509 0.0000 0.0000 0.0000 79  ILE B CA  
4462 C C   . ILE B 79  ? 166.9216 166.9216 166.9216 0.0000 0.0000 0.0000 79  ILE B C   
4463 O O   . ILE B 79  ? 166.9116 166.9116 166.9116 0.0000 0.0000 0.0000 79  ILE B O   
4464 C CB  . ILE B 79  ? 167.2695 167.2695 167.2695 0.0000 0.0000 0.0000 79  ILE B CB  
4465 C CG1 . ILE B 79  ? 166.9542 166.9542 166.9542 0.0000 0.0000 0.0000 79  ILE B CG1 
4466 C CG2 . ILE B 79  ? 162.1123 162.1123 162.1123 0.0000 0.0000 0.0000 79  ILE B CG2 
4467 C CD1 . ILE B 79  ? 161.9348 161.9348 161.9348 0.0000 0.0000 0.0000 79  ILE B CD1 
4468 N N   . ARG B 80  ? 162.5416 162.5416 162.5416 0.0000 0.0000 0.0000 80  ARG B N   
4469 C CA  . ARG B 80  ? 162.5237 162.5237 162.5237 0.0000 0.0000 0.0000 80  ARG B CA  
4470 C C   . ARG B 80  ? 161.5762 161.5762 161.5762 0.0000 0.0000 0.0000 80  ARG B C   
4471 O O   . ARG B 80  ? 161.5160 161.5160 161.5160 0.0000 0.0000 0.0000 80  ARG B O   
4472 C CB  . ARG B 80  ? 161.7215 161.7215 161.7215 0.0000 0.0000 0.0000 80  ARG B CB  
4473 C CG  . ARG B 80  ? 161.5042 161.5042 161.5042 0.0000 0.0000 0.0000 80  ARG B CG  
4474 C CD  . ARG B 80  ? 178.4068 178.4068 178.4068 0.0000 0.0000 0.0000 80  ARG B CD  
4475 N NE  . ARG B 80  ? 178.8344 178.8344 178.8344 0.0000 0.0000 0.0000 80  ARG B NE  
4476 C CZ  . ARG B 80  ? 178.9380 178.9380 178.9380 0.0000 0.0000 0.0000 80  ARG B CZ  
4477 N NH1 . ARG B 80  ? 179.1067 179.1067 179.1067 0.0000 0.0000 0.0000 80  ARG B NH1 
4478 N NH2 . ARG B 80  ? 179.0513 179.0513 179.0513 0.0000 0.0000 0.0000 80  ARG B NH2 
4479 N N   . SER B 81  ? 179.1861 179.1861 179.1861 0.0000 0.0000 0.0000 81  SER B N   
4480 C CA  . SER B 81  ? 179.2646 179.2646 179.2646 0.0000 0.0000 0.0000 81  SER B CA  
4481 C C   . SER B 81  ? 179.3260 179.3260 179.3260 0.0000 0.0000 0.0000 81  SER B C   
4482 O O   . SER B 81  ? 179.3871 179.3871 179.3871 0.0000 0.0000 0.0000 81  SER B O   
4483 C CB  . SER B 81  ? 179.3667 179.3667 179.3667 0.0000 0.0000 0.0000 81  SER B CB  
4484 O OG  . SER B 81  ? 179.4918 179.4918 179.4918 0.0000 0.0000 0.0000 81  SER B OG  
4485 N N   . GLN B 82  ? 179.6652 179.6652 179.6652 0.0000 0.0000 0.0000 82  GLN B N   
4486 C CA  . GLN B 82  ? 179.5977 179.5977 179.5977 0.0000 0.0000 0.0000 82  GLN B CA  
4487 C C   . GLN B 82  ? 180.0360 180.0360 180.0360 0.0000 0.0000 0.0000 82  GLN B C   
4488 O O   . GLN B 82  ? 179.8464 179.8464 179.8464 0.0000 0.0000 0.0000 82  GLN B O   
4489 C CB  . GLN B 82  ? 180.0184 180.0184 180.0184 0.0000 0.0000 0.0000 82  GLN B CB  
4490 C CG  . GLN B 82  ? 180.0750 180.0750 180.0750 0.0000 0.0000 0.0000 82  GLN B CG  
4491 C CD  . GLN B 82  ? 180.1742 180.1742 180.1742 0.0000 0.0000 0.0000 82  GLN B CD  
4492 O OE1 . GLN B 82  ? 180.0587 180.0587 180.0587 0.0000 0.0000 0.0000 82  GLN B OE1 
4493 N NE2 . GLN B 82  ? 169.2413 169.2413 169.2413 0.0000 0.0000 0.0000 82  GLN B NE2 
4494 N N   . ALA B 83  ? 169.1157 169.1157 169.1157 0.0000 0.0000 0.0000 83  ALA B N   
4495 C CA  . ALA B 83  ? 169.6450 169.6450 169.6450 0.0000 0.0000 0.0000 83  ALA B CA  
4496 C C   . ALA B 83  ? 170.0475 170.0475 170.0475 0.0000 0.0000 0.0000 83  ALA B C   
4497 O O   . ALA B 83  ? 168.7245 168.7245 168.7245 0.0000 0.0000 0.0000 83  ALA B O   
4498 C CB  . ALA B 83  ? 168.6661 168.6661 168.6661 0.0000 0.0000 0.0000 83  ALA B CB  
4499 N N   . ILE B 84  ? 168.5508 168.5508 168.5508 0.0000 0.0000 0.0000 84  ILE B N   
4500 C CA  . ILE B 84  ? 169.0807 169.0807 169.0807 0.0000 0.0000 0.0000 84  ILE B CA  
4501 C C   . ILE B 84  ? 175.2656 175.2656 175.2656 0.0000 0.0000 0.0000 84  ILE B C   
4502 O O   . ILE B 84  ? 175.4161 175.4161 175.4161 0.0000 0.0000 0.0000 84  ILE B O   
4503 C CB  . ILE B 84  ? 175.7938 175.7938 175.7938 0.0000 0.0000 0.0000 84  ILE B CB  
4504 C CG1 . ILE B 84  ? 175.9068 175.9068 175.9068 0.0000 0.0000 0.0000 84  ILE B CG1 
4505 C CG2 . ILE B 84  ? 175.2654 175.2654 175.2654 0.0000 0.0000 0.0000 84  ILE B CG2 
4506 C CD1 . ILE B 84  ? 175.1969 175.1969 175.1969 0.0000 0.0000 0.0000 84  ILE B CD1 
4507 N N   . HIS B 85  ? 175.3035 175.3035 175.3035 0.0000 0.0000 0.0000 85  HIS B N   
4508 C CA  . HIS B 85  ? 175.0998 175.0998 175.0998 0.0000 0.0000 0.0000 85  HIS B CA  
4509 C C   . HIS B 85  ? 175.0997 175.0997 175.0997 0.0000 0.0000 0.0000 85  HIS B C   
4510 O O   . HIS B 85  ? 183.0028 183.0028 183.0028 0.0000 0.0000 0.0000 85  HIS B O   
4511 C CB  . HIS B 85  ? 183.3344 183.3344 183.3344 0.0000 0.0000 0.0000 85  HIS B CB  
4512 C CG  . HIS B 85  ? 183.5256 183.5256 183.5256 0.0000 0.0000 0.0000 85  HIS B CG  
4513 N ND1 . HIS B 85  ? 183.6666 183.6666 183.6666 0.0000 0.0000 0.0000 85  HIS B ND1 
4514 C CD2 . HIS B 85  ? 183.4749 183.4749 183.4749 0.0000 0.0000 0.0000 85  HIS B CD2 
4515 C CE1 . HIS B 85  ? 183.4034 183.4034 183.4034 0.0000 0.0000 0.0000 85  HIS B CE1 
4516 N NE2 . HIS B 85  ? 183.5740 183.5740 183.5740 0.0000 0.0000 0.0000 85  HIS B NE2 
4517 N N   . GLN B 86  ? 189.4429 189.4429 189.4429 0.0000 0.0000 0.0000 86  GLN B N   
4518 C CA  . GLN B 86  ? 189.8535 189.8535 189.8535 0.0000 0.0000 0.0000 86  GLN B CA  
4519 C C   . GLN B 86  ? 190.0514 190.0514 190.0514 0.0000 0.0000 0.0000 86  GLN B C   
4520 O O   . GLN B 86  ? 190.3524 190.3524 190.3524 0.0000 0.0000 0.0000 86  GLN B O   
4521 C CB  . GLN B 86  ? 189.9607 189.9607 189.9607 0.0000 0.0000 0.0000 86  GLN B CB  
4522 C CG  . GLN B 86  ? 190.0595 190.0595 190.0595 0.0000 0.0000 0.0000 86  GLN B CG  
4523 C CD  . GLN B 86  ? 190.1173 190.1173 190.1173 0.0000 0.0000 0.0000 86  GLN B CD  
4524 O OE1 . GLN B 86  ? 190.0862 190.0862 190.0862 0.0000 0.0000 0.0000 86  GLN B OE1 
4525 N NE2 . GLN B 86  ? 191.2172 191.2172 191.2172 0.0000 0.0000 0.0000 86  GLN B NE2 
4526 N N   . LEU B 87  ? 191.4122 191.4122 191.4122 0.0000 0.0000 0.0000 87  LEU B N   
4527 C CA  . LEU B 87  ? 191.4824 191.4824 191.4824 0.0000 0.0000 0.0000 87  LEU B CA  
4528 C C   . LEU B 87  ? 191.6403 191.6403 191.6403 0.0000 0.0000 0.0000 87  LEU B C   
4529 O O   . LEU B 87  ? 192.0951 192.0951 192.0951 0.0000 0.0000 0.0000 87  LEU B O   
4530 C CB  . LEU B 87  ? 192.1257 192.1257 192.1257 0.0000 0.0000 0.0000 87  LEU B CB  
4531 C CG  . LEU B 87  ? 191.8859 191.8859 191.8859 0.0000 0.0000 0.0000 87  LEU B CG  
4532 C CD1 . LEU B 87  ? 191.6514 191.6514 191.6514 0.0000 0.0000 0.0000 87  LEU B CD1 
4533 C CD2 . LEU B 87  ? 192.0326 192.0326 192.0326 0.0000 0.0000 0.0000 87  LEU B CD2 
4534 N N   . LYS B 88  ? 192.1078 192.1078 192.1078 0.0000 0.0000 0.0000 88  LYS B N   
4535 C CA  . LYS B 88  ? 192.1448 192.1448 192.1448 0.0000 0.0000 0.0000 88  LYS B CA  
4536 C C   . LYS B 88  ? 192.0772 192.0772 192.0772 0.0000 0.0000 0.0000 88  LYS B C   
4537 O O   . LYS B 88  ? 192.2841 192.2841 192.2841 0.0000 0.0000 0.0000 88  LYS B O   
4538 C CB  . LYS B 88  ? 185.9113 185.9113 185.9113 0.0000 0.0000 0.0000 88  LYS B CB  
4539 C CG  . LYS B 88  ? 185.4729 185.4729 185.4729 0.0000 0.0000 0.0000 88  LYS B CG  
4540 C CD  . LYS B 88  ? 184.7593 184.7593 184.7593 0.0000 0.0000 0.0000 88  LYS B CD  
4541 C CE  . LYS B 88  ? 185.0583 185.0583 185.0583 0.0000 0.0000 0.0000 88  LYS B CE  
4542 N NZ  . LYS B 88  ? 185.6885 185.6885 185.6885 0.0000 0.0000 0.0000 88  LYS B NZ  
4543 N N   . VAL B 89  ? 185.3835 185.3835 185.3835 0.0000 0.0000 0.0000 89  VAL B N   
4544 C CA  . VAL B 89  ? 185.0760 185.0760 185.0760 0.0000 0.0000 0.0000 89  VAL B CA  
4545 C C   . VAL B 89  ? 185.3930 185.3930 185.3930 0.0000 0.0000 0.0000 89  VAL B C   
4546 O O   . VAL B 89  ? 163.5866 163.5866 163.5866 0.0000 0.0000 0.0000 89  VAL B O   
4547 C CB  . VAL B 89  ? 163.1819 163.1819 163.1819 0.0000 0.0000 0.0000 89  VAL B CB  
4548 C CG1 . VAL B 89  ? 162.9941 162.9941 162.9941 0.0000 0.0000 0.0000 89  VAL B CG1 
4549 C CG2 . VAL B 89  ? 162.8738 162.8738 162.8738 0.0000 0.0000 0.0000 89  VAL B CG2 
4550 N N   . ASN B 90  ? 163.0356 163.0356 163.0356 0.0000 0.0000 0.0000 90  ASN B N   
4551 C CA  . ASN B 90  ? 163.2145 163.2145 163.2145 0.0000 0.0000 0.0000 90  ASN B CA  
4552 C C   . ASN B 90  ? 163.6003 163.6003 163.6003 0.0000 0.0000 0.0000 90  ASN B C   
4553 O O   . ASN B 90  ? 161.9512 161.9512 161.9512 0.0000 0.0000 0.0000 90  ASN B O   
4554 C CB  . ASN B 90  ? 161.8008 161.8008 161.8008 0.0000 0.0000 0.0000 90  ASN B CB  
4555 C CG  . ASN B 90  ? 161.7173 161.7173 161.7173 0.0000 0.0000 0.0000 90  ASN B CG  
4556 O OD1 . ASN B 90  ? 161.8460 161.8460 161.8460 0.0000 0.0000 0.0000 90  ASN B OD1 
4557 N ND2 . ASN B 90  ? 161.6778 161.6778 161.6778 0.0000 0.0000 0.0000 90  ASN B ND2 
4558 N N   . GLY B 91  ? 161.4584 161.4584 161.4584 0.0000 0.0000 0.0000 91  GLY B N   
4559 C CA  . GLY B 91  ? 161.4630 161.4630 161.4630 0.0000 0.0000 0.0000 91  GLY B CA  
4560 C C   . GLY B 91  ? 161.5221 161.5221 161.5221 0.0000 0.0000 0.0000 91  GLY B C   
4561 O O   . GLY B 91  ? 161.4070 161.4070 161.4070 0.0000 0.0000 0.0000 91  GLY B O   
4562 N N   . GLU B 92  ? 161.5112 161.5112 161.5112 0.0000 0.0000 0.0000 92  GLU B N   
4563 C CA  . GLU B 92  ? 161.4328 161.4328 161.4328 0.0000 0.0000 0.0000 92  GLU B CA  
4564 C C   . GLU B 92  ? 161.4423 161.4423 161.4423 0.0000 0.0000 0.0000 92  GLU B C   
4565 O O   . GLU B 92  ? 161.3927 161.3927 161.3927 0.0000 0.0000 0.0000 92  GLU B O   
4566 C CB  . GLU B 92  ? 161.2870 161.2870 161.2870 0.0000 0.0000 0.0000 92  GLU B CB  
4567 C CG  . GLU B 92  ? 161.3897 161.3897 161.3897 0.0000 0.0000 0.0000 92  GLU B CG  
4568 C CD  . GLU B 92  ? 161.5369 161.5369 161.5369 0.0000 0.0000 0.0000 92  GLU B CD  
4569 O OE1 . GLU B 92  ? 161.2417 161.2417 161.2417 0.0000 0.0000 0.0000 92  GLU B OE1 
4570 O OE2 . GLU B 92  ? 161.2727 161.2727 161.2727 0.0000 0.0000 0.0000 92  GLU B OE2 
4571 N N   . ASP B 93  ? 161.4329 161.4329 161.4329 0.0000 0.0000 0.0000 93  ASP B N   
4572 C CA  . ASP B 93  ? 161.3882 161.3882 161.3882 0.0000 0.0000 0.0000 93  ASP B CA  
4573 C C   . ASP B 93  ? 161.3754 161.3754 161.3754 0.0000 0.0000 0.0000 93  ASP B C   
4574 O O   . ASP B 93  ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 93  ASP B O   
4575 C CB  . ASP B 93  ? 161.3185 161.3185 161.3185 0.0000 0.0000 0.0000 93  ASP B CB  
4576 C CG  . ASP B 93  ? 161.4222 161.4222 161.4222 0.0000 0.0000 0.0000 93  ASP B CG  
4577 O OD1 . ASP B 93  ? 161.3079 161.3079 161.3079 0.0000 0.0000 0.0000 93  ASP B OD1 
4578 O OD2 . ASP B 93  ? 161.1919 161.1919 161.1919 0.0000 0.0000 0.0000 93  ASP B OD2 
4579 N N   . PRO B 94  ? 161.4365 161.4365 161.4365 0.0000 0.0000 0.0000 94  PRO B N   
4580 C CA  . PRO B 94  ? 161.3417 161.3417 161.3417 0.0000 0.0000 0.0000 94  PRO B CA  
4581 C C   . PRO B 94  ? 161.4501 161.4501 161.4501 0.0000 0.0000 0.0000 94  PRO B C   
4582 O O   . PRO B 94  ? 161.3643 161.3643 161.3643 0.0000 0.0000 0.0000 94  PRO B O   
4583 C CB  . PRO B 94  ? 161.3455 161.3455 161.3455 0.0000 0.0000 0.0000 94  PRO B CB  
4584 C CG  . PRO B 94  ? 161.3515 161.3515 161.3515 0.0000 0.0000 0.0000 94  PRO B CG  
4585 C CD  . PRO B 94  ? 161.5407 161.5407 161.5407 0.0000 0.0000 0.0000 94  PRO B CD  
4586 N N   . TYR B 95  ? 161.3728 161.3728 161.3728 0.0000 0.0000 0.0000 95  TYR B N   
4587 C CA  . TYR B 95  ? 161.3747 161.3747 161.3747 0.0000 0.0000 0.0000 95  TYR B CA  
4588 C C   . TYR B 95  ? 161.5160 161.5160 161.5160 0.0000 0.0000 0.0000 95  TYR B C   
4589 O O   . TYR B 95  ? 161.4108 161.4108 161.4108 0.0000 0.0000 0.0000 95  TYR B O   
4590 C CB  . TYR B 95  ? 161.1537 161.1537 161.1537 0.0000 0.0000 0.0000 95  TYR B CB  
4591 C CG  . TYR B 95  ? 161.1303 161.1303 161.1303 0.0000 0.0000 0.0000 95  TYR B CG  
4592 C CD1 . TYR B 95  ? 161.1812 161.1812 161.1812 0.0000 0.0000 0.0000 95  TYR B CD1 
4593 C CD2 . TYR B 95  ? 161.4743 161.4743 161.4743 0.0000 0.0000 0.0000 95  TYR B CD2 
4594 C CE1 . TYR B 95  ? 161.7528 161.7528 161.7528 0.0000 0.0000 0.0000 95  TYR B CE1 
4595 C CE2 . TYR B 95  ? 161.2511 161.2511 161.2511 0.0000 0.0000 0.0000 95  TYR B CE2 
4596 C CZ  . TYR B 95  ? 161.3032 161.3032 161.3032 0.0000 0.0000 0.0000 95  TYR B CZ  
4597 O OH  . TYR B 95  ? 161.3655 161.3655 161.3655 0.0000 0.0000 0.0000 95  TYR B OH  
4598 N N   . PRO B 96  ? 161.4863 161.4863 161.4863 0.0000 0.0000 0.0000 96  PRO B N   
4599 C CA  . PRO B 96  ? 161.3976 161.3976 161.3976 0.0000 0.0000 0.0000 96  PRO B CA  
4600 C C   . PRO B 96  ? 161.5005 161.5005 161.5005 0.0000 0.0000 0.0000 96  PRO B C   
4601 O O   . PRO B 96  ? 161.4690 161.4690 161.4690 0.0000 0.0000 0.0000 96  PRO B O   
4602 C CB  . PRO B 96  ? 161.4730 161.4730 161.4730 0.0000 0.0000 0.0000 96  PRO B CB  
4603 C CG  . PRO B 96  ? 161.3676 161.3676 161.3676 0.0000 0.0000 0.0000 96  PRO B CG  
4604 C CD  . PRO B 96  ? 161.3289 161.3289 161.3289 0.0000 0.0000 0.0000 96  PRO B CD  
4605 N N   . HIS B 97  ? 161.5028 161.5028 161.5028 0.0000 0.0000 0.0000 97  HIS B N   
4606 C CA  . HIS B 97  ? 161.3407 161.3407 161.3407 0.0000 0.0000 0.0000 97  HIS B CA  
4607 C C   . HIS B 97  ? 161.3977 161.3977 161.3977 0.0000 0.0000 0.0000 97  HIS B C   
4608 O O   . HIS B 97  ? 161.4257 161.4257 161.4257 0.0000 0.0000 0.0000 97  HIS B O   
4609 C CB  . HIS B 97  ? 161.4841 161.4841 161.4841 0.0000 0.0000 0.0000 97  HIS B CB  
4610 C CG  . HIS B 97  ? 161.3041 161.3041 161.3041 0.0000 0.0000 0.0000 97  HIS B CG  
4611 N ND1 . HIS B 97  ? 160.8347 160.8347 160.8347 0.0000 0.0000 0.0000 97  HIS B ND1 
4612 C CD2 . HIS B 97  ? 161.2121 161.2121 161.2121 0.0000 0.0000 0.0000 97  HIS B CD2 
4613 C CE1 . HIS B 97  ? 161.1436 161.1436 161.1436 0.0000 0.0000 0.0000 97  HIS B CE1 
4614 N NE2 . HIS B 97  ? 160.7923 160.7923 160.7923 0.0000 0.0000 0.0000 97  HIS B NE2 
4615 N N   . LYS B 98  ? 160.2471 160.2471 160.2471 0.0000 0.0000 0.0000 98  LYS B N   
4616 C CA  . LYS B 98  ? 160.3831 160.3831 160.3831 0.0000 0.0000 0.0000 98  LYS B CA  
4617 C C   . LYS B 98  ? 159.9428 159.9428 159.9428 0.0000 0.0000 0.0000 98  LYS B C   
4618 O O   . LYS B 98  ? 161.0277 161.0277 161.0277 0.0000 0.0000 0.0000 98  LYS B O   
4619 C CB  . LYS B 98  ? 161.1348 161.1348 161.1348 0.0000 0.0000 0.0000 98  LYS B CB  
4620 C CG  . LYS B 98  ? 161.0334 161.0334 161.0334 0.0000 0.0000 0.0000 98  LYS B CG  
4621 C CD  . LYS B 98  ? 160.5322 160.5322 160.5322 0.0000 0.0000 0.0000 98  LYS B CD  
4622 C CE  . LYS B 98  ? 160.4825 160.4825 160.4825 0.0000 0.0000 0.0000 98  LYS B CE  
4623 N NZ  . LYS B 98  ? 161.4858 161.4858 161.4858 0.0000 0.0000 0.0000 98  LYS B NZ  
4624 N N   . PHE B 99  ? 161.5409 161.5409 161.5409 0.0000 0.0000 0.0000 99  PHE B N   
4625 C CA  . PHE B 99  ? 161.5408 161.5408 161.5408 0.0000 0.0000 0.0000 99  PHE B CA  
4626 C C   . PHE B 99  ? 161.5933 161.5933 161.5933 0.0000 0.0000 0.0000 99  PHE B C   
4627 O O   . PHE B 99  ? 160.9449 160.9449 160.9449 0.0000 0.0000 0.0000 99  PHE B O   
4628 C CB  . PHE B 99  ? 161.0313 161.0313 161.0313 0.0000 0.0000 0.0000 99  PHE B CB  
4629 C CG  . PHE B 99  ? 160.6482 160.6482 160.6482 0.0000 0.0000 0.0000 99  PHE B CG  
4630 C CD1 . PHE B 99  ? 161.0807 161.0807 161.0807 0.0000 0.0000 0.0000 99  PHE B CD1 
4631 C CD2 . PHE B 99  ? 161.3715 161.3715 161.3715 0.0000 0.0000 0.0000 99  PHE B CD2 
4632 C CE1 . PHE B 99  ? 161.5355 161.5355 161.5355 0.0000 0.0000 0.0000 99  PHE B CE1 
4633 C CE2 . PHE B 99  ? 161.5229 161.5229 161.5229 0.0000 0.0000 0.0000 99  PHE B CE2 
4634 C CZ  . PHE B 99  ? 161.5358 161.5358 161.5358 0.0000 0.0000 0.0000 99  PHE B CZ  
4635 N N   . HIS B 100 ? 160.2369 160.2369 160.2369 0.0000 0.0000 0.0000 100 HIS B N   
4636 C CA  . HIS B 100 ? 160.8827 160.8827 160.8827 0.0000 0.0000 0.0000 100 HIS B CA  
4637 C C   . HIS B 100 ? 161.4994 161.4994 161.4994 0.0000 0.0000 0.0000 100 HIS B C   
4638 O O   . HIS B 100 ? 161.6488 161.6488 161.6488 0.0000 0.0000 0.0000 100 HIS B O   
4639 C CB  . HIS B 100 ? 160.5557 160.5557 160.5557 0.0000 0.0000 0.0000 100 HIS B CB  
4640 C CG  . HIS B 100 ? 161.2644 161.2644 161.2644 0.0000 0.0000 0.0000 100 HIS B CG  
4641 N ND1 . HIS B 100 ? 161.4232 161.4232 161.4232 0.0000 0.0000 0.0000 100 HIS B ND1 
4642 C CD2 . HIS B 100 ? 161.2285 161.2285 161.2285 0.0000 0.0000 0.0000 100 HIS B CD2 
4643 C CE1 . HIS B 100 ? 161.4154 161.4154 161.4154 0.0000 0.0000 0.0000 100 HIS B CE1 
4644 N NE2 . HIS B 100 ? 161.5199 161.5199 161.5199 0.0000 0.0000 0.0000 100 HIS B NE2 
4645 N N   . VAL B 101 ? 161.2249 161.2249 161.2249 0.0000 0.0000 0.0000 101 VAL B N   
4646 C CA  . VAL B 101 ? 161.2593 161.2593 161.2593 0.0000 0.0000 0.0000 101 VAL B CA  
4647 C C   . VAL B 101 ? 161.6048 161.6048 161.6048 0.0000 0.0000 0.0000 101 VAL B C   
4648 O O   . VAL B 101 ? 161.4015 161.4015 161.4015 0.0000 0.0000 0.0000 101 VAL B O   
4649 C CB  . VAL B 101 ? 161.6079 161.6079 161.6079 0.0000 0.0000 0.0000 101 VAL B CB  
4650 C CG1 . VAL B 101 ? 161.4169 161.4169 161.4169 0.0000 0.0000 0.0000 101 VAL B CG1 
4651 C CG2 . VAL B 101 ? 161.4500 161.4500 161.4500 0.0000 0.0000 0.0000 101 VAL B CG2 
4652 N N   . ASP B 102 ? 161.7572 161.7572 161.7572 0.0000 0.0000 0.0000 102 ASP B N   
4653 C CA  . ASP B 102 ? 161.3577 161.3577 161.3577 0.0000 0.0000 0.0000 102 ASP B CA  
4654 C C   . ASP B 102 ? 161.5308 161.5308 161.5308 0.0000 0.0000 0.0000 102 ASP B C   
4655 O O   . ASP B 102 ? 161.4300 161.4300 161.4300 0.0000 0.0000 0.0000 102 ASP B O   
4656 C CB  . ASP B 102 ? 161.9684 161.9684 161.9684 0.0000 0.0000 0.0000 102 ASP B CB  
4657 C CG  . ASP B 102 ? 162.0784 162.0784 162.0784 0.0000 0.0000 0.0000 102 ASP B CG  
4658 O OD1 . ASP B 102 ? 162.0300 162.0300 162.0300 0.0000 0.0000 0.0000 102 ASP B OD1 
4659 O OD2 . ASP B 102 ? 162.4357 162.4357 162.4357 0.0000 0.0000 0.0000 102 ASP B OD2 
4660 N N   . ILE B 103 ? 162.0430 162.0430 162.0430 0.0000 0.0000 0.0000 103 ILE B N   
4661 C CA  . ILE B 103 ? 161.5866 161.5866 161.5866 0.0000 0.0000 0.0000 103 ILE B CA  
4662 C C   . ILE B 103 ? 161.5698 161.5698 161.5698 0.0000 0.0000 0.0000 103 ILE B C   
4663 O O   . ILE B 103 ? 160.8769 160.8769 160.8769 0.0000 0.0000 0.0000 103 ILE B O   
4664 C CB  . ILE B 103 ? 161.3087 161.3087 161.3087 0.0000 0.0000 0.0000 103 ILE B CB  
4665 C CG1 . ILE B 103 ? 161.4679 161.4679 161.4679 0.0000 0.0000 0.0000 103 ILE B CG1 
4666 C CG2 . ILE B 103 ? 161.6550 161.6550 161.6550 0.0000 0.0000 0.0000 103 ILE B CG2 
4667 C CD1 . ILE B 103 ? 162.0605 162.0605 162.0605 0.0000 0.0000 0.0000 103 ILE B CD1 
4668 N N   . SER B 104 ? 161.4864 161.4864 161.4864 0.0000 0.0000 0.0000 104 SER B N   
4669 C CA  . SER B 104 ? 161.4463 161.4463 161.4463 0.0000 0.0000 0.0000 104 SER B CA  
4670 C C   . SER B 104 ? 161.4374 161.4374 161.4374 0.0000 0.0000 0.0000 104 SER B C   
4671 O O   . SER B 104 ? 161.5414 161.5414 161.5414 0.0000 0.0000 0.0000 104 SER B O   
4672 C CB  . SER B 104 ? 161.5022 161.5022 161.5022 0.0000 0.0000 0.0000 104 SER B CB  
4673 O OG  . SER B 104 ? 161.4768 161.4768 161.4768 0.0000 0.0000 0.0000 104 SER B OG  
4674 N N   . LEU B 105 ? 161.4725 161.4725 161.4725 0.0000 0.0000 0.0000 105 LEU B N   
4675 C CA  . LEU B 105 ? 161.5964 161.5964 161.5964 0.0000 0.0000 0.0000 105 LEU B CA  
4676 C C   . LEU B 105 ? 161.6489 161.6489 161.6489 0.0000 0.0000 0.0000 105 LEU B C   
4677 O O   . LEU B 105 ? 162.1064 162.1064 162.1064 0.0000 0.0000 0.0000 105 LEU B O   
4678 C CB  . LEU B 105 ? 162.2135 162.2135 162.2135 0.0000 0.0000 0.0000 105 LEU B CB  
4679 C CG  . LEU B 105 ? 161.5009 161.5009 161.5009 0.0000 0.0000 0.0000 105 LEU B CG  
4680 C CD1 . LEU B 105 ? 161.4271 161.4271 161.4271 0.0000 0.0000 0.0000 105 LEU B CD1 
4681 C CD2 . LEU B 105 ? 161.5669 161.5669 161.5669 0.0000 0.0000 0.0000 105 LEU B CD2 
4682 N N   . THR B 106 ? 161.5389 161.5389 161.5389 0.0000 0.0000 0.0000 106 THR B N   
4683 C CA  . THR B 106 ? 174.5258 174.5258 174.5258 0.0000 0.0000 0.0000 106 THR B CA  
4684 C C   . THR B 106 ? 174.8984 174.8984 174.8984 0.0000 0.0000 0.0000 106 THR B C   
4685 O O   . THR B 106 ? 174.9547 174.9547 174.9547 0.0000 0.0000 0.0000 106 THR B O   
4686 C CB  . THR B 106 ? 175.2715 175.2715 175.2715 0.0000 0.0000 0.0000 106 THR B CB  
4687 O OG1 . THR B 106 ? 175.2334 175.2334 175.2334 0.0000 0.0000 0.0000 106 THR B OG1 
4688 C CG2 . THR B 106 ? 175.3906 175.3906 175.3906 0.0000 0.0000 0.0000 106 THR B CG2 
4689 N N   . ASP B 107 ? 175.4917 175.4917 175.4917 0.0000 0.0000 0.0000 107 ASP B N   
4690 C CA  . ASP B 107 ? 175.5344 175.5344 175.5344 0.0000 0.0000 0.0000 107 ASP B CA  
4691 C C   . ASP B 107 ? 175.4648 175.4648 175.4648 0.0000 0.0000 0.0000 107 ASP B C   
4692 O O   . ASP B 107 ? 167.6206 167.6206 167.6206 0.0000 0.0000 0.0000 107 ASP B O   
4693 C CB  . ASP B 107 ? 167.4325 167.4325 167.4325 0.0000 0.0000 0.0000 107 ASP B CB  
4694 C CG  . ASP B 107 ? 167.3788 167.3788 167.3788 0.0000 0.0000 0.0000 107 ASP B CG  
4695 O OD1 . ASP B 107 ? 167.6425 167.6425 167.6425 0.0000 0.0000 0.0000 107 ASP B OD1 
4696 O OD2 . ASP B 107 ? 167.3274 167.3274 167.3274 0.0000 0.0000 0.0000 107 ASP B OD2 
4697 N N   . PHE B 108 ? 167.3852 167.3852 167.3852 0.0000 0.0000 0.0000 108 PHE B N   
4698 C CA  . PHE B 108 ? 167.3806 167.3806 167.3806 0.0000 0.0000 0.0000 108 PHE B CA  
4699 C C   . PHE B 108 ? 167.2989 167.2989 167.2989 0.0000 0.0000 0.0000 108 PHE B C   
4700 O O   . PHE B 108 ? 167.4219 167.4219 167.4219 0.0000 0.0000 0.0000 108 PHE B O   
4701 C CB  . PHE B 108 ? 165.8034 165.8034 165.8034 0.0000 0.0000 0.0000 108 PHE B CB  
4702 C CG  . PHE B 108 ? 165.9219 165.9219 165.9219 0.0000 0.0000 0.0000 108 PHE B CG  
4703 C CD1 . PHE B 108 ? 166.5068 166.5068 166.5068 0.0000 0.0000 0.0000 108 PHE B CD1 
4704 C CD2 . PHE B 108 ? 166.3710 166.3710 166.3710 0.0000 0.0000 0.0000 108 PHE B CD2 
4705 C CE1 . PHE B 108 ? 165.6619 165.6619 165.6619 0.0000 0.0000 0.0000 108 PHE B CE1 
4706 C CE2 . PHE B 108 ? 165.3767 165.3767 165.3767 0.0000 0.0000 0.0000 108 PHE B CE2 
4707 C CZ  . PHE B 108 ? 165.5693 165.5693 165.5693 0.0000 0.0000 0.0000 108 PHE B CZ  
4708 N N   . ILE B 109 ? 165.3617 165.3617 165.3617 0.0000 0.0000 0.0000 109 ILE B N   
4709 C CA  . ILE B 109 ? 165.3870 165.3870 165.3870 0.0000 0.0000 0.0000 109 ILE B CA  
4710 C C   . ILE B 109 ? 165.3942 165.3942 165.3942 0.0000 0.0000 0.0000 109 ILE B C   
4711 O O   . ILE B 109 ? 165.3427 165.3427 165.3427 0.0000 0.0000 0.0000 109 ILE B O   
4712 C CB  . ILE B 109 ? 165.4569 165.4569 165.4569 0.0000 0.0000 0.0000 109 ILE B CB  
4713 C CG1 . ILE B 109 ? 180.8185 180.8185 180.8185 0.0000 0.0000 0.0000 109 ILE B CG1 
4714 C CG2 . ILE B 109 ? 181.1741 181.1741 181.1741 0.0000 0.0000 0.0000 109 ILE B CG2 
4715 C CD1 . ILE B 109 ? 181.7477 181.7477 181.7477 0.0000 0.0000 0.0000 109 ILE B CD1 
4716 N N   . GLN B 110 ? 181.7826 181.7826 181.7826 0.0000 0.0000 0.0000 110 GLN B N   
4717 C CA  . GLN B 110 ? 181.3219 181.3219 181.3219 0.0000 0.0000 0.0000 110 GLN B CA  
4718 C C   . GLN B 110 ? 181.2205 181.2205 181.2205 0.0000 0.0000 0.0000 110 GLN B C   
4719 O O   . GLN B 110 ? 193.6104 193.6104 193.6104 0.0000 0.0000 0.0000 110 GLN B O   
4720 C CB  . GLN B 110 ? 194.0446 194.0446 194.0446 0.0000 0.0000 0.0000 110 GLN B CB  
4721 C CG  . GLN B 110 ? 194.2247 194.2247 194.2247 0.0000 0.0000 0.0000 110 GLN B CG  
4722 C CD  . GLN B 110 ? 194.5543 194.5543 194.5543 0.0000 0.0000 0.0000 110 GLN B CD  
4723 O OE1 . GLN B 110 ? 194.2801 194.2801 194.2801 0.0000 0.0000 0.0000 110 GLN B OE1 
4724 N NE2 . GLN B 110 ? 194.2395 194.2395 194.2395 0.0000 0.0000 0.0000 110 GLN B NE2 
4725 N N   . LYS B 111 ? 194.0886 194.0886 194.0886 0.0000 0.0000 0.0000 111 LYS B N   
4726 C CA  . LYS B 111 ? 194.3969 194.3969 194.3969 0.0000 0.0000 0.0000 111 LYS B CA  
4727 C C   . LYS B 111 ? 194.0770 194.0770 194.0770 0.0000 0.0000 0.0000 111 LYS B C   
4728 O O   . LYS B 111 ? 194.3201 194.3201 194.3201 0.0000 0.0000 0.0000 111 LYS B O   
4729 C CB  . LYS B 111 ? 193.5259 193.5259 193.5259 0.0000 0.0000 0.0000 111 LYS B CB  
4730 C CG  . LYS B 111 ? 193.8021 193.8021 193.8021 0.0000 0.0000 0.0000 111 LYS B CG  
4731 C CD  . LYS B 111 ? 194.1646 194.1646 194.1646 0.0000 0.0000 0.0000 111 LYS B CD  
4732 C CE  . LYS B 111 ? 194.0130 194.0130 194.0130 0.0000 0.0000 0.0000 111 LYS B CE  
4733 N NZ  . LYS B 111 ? 193.7196 193.7196 193.7196 0.0000 0.0000 0.0000 111 LYS B NZ  
4734 N N   . TYR B 112 ? 193.4051 193.4051 193.4051 0.0000 0.0000 0.0000 112 TYR B N   
4735 C CA  . TYR B 112 ? 192.9716 192.9716 192.9716 0.0000 0.0000 0.0000 112 TYR B CA  
4736 C C   . TYR B 112 ? 193.5704 193.5704 193.5704 0.0000 0.0000 0.0000 112 TYR B C   
4737 O O   . TYR B 112 ? 207.4407 207.4407 207.4407 0.0000 0.0000 0.0000 112 TYR B O   
4738 C CB  . TYR B 112 ? 207.6882 207.6882 207.6882 0.0000 0.0000 0.0000 112 TYR B CB  
4739 C CG  . TYR B 112 ? 207.6283 207.6283 207.6283 0.0000 0.0000 0.0000 112 TYR B CG  
4740 C CD1 . TYR B 112 ? 207.6032 207.6032 207.6032 0.0000 0.0000 0.0000 112 TYR B CD1 
4741 C CD2 . TYR B 112 ? 207.9042 207.9042 207.9042 0.0000 0.0000 0.0000 112 TYR B CD2 
4742 C CE1 . TYR B 112 ? 207.9998 207.9998 207.9998 0.0000 0.0000 0.0000 112 TYR B CE1 
4743 C CE2 . TYR B 112 ? 208.0108 208.0108 208.0108 0.0000 0.0000 0.0000 112 TYR B CE2 
4744 C CZ  . TYR B 112 ? 208.0198 208.0198 208.0198 0.0000 0.0000 0.0000 112 TYR B CZ  
4745 O OH  . TYR B 112 ? 208.0026 208.0026 208.0026 0.0000 0.0000 0.0000 112 TYR B OH  
4746 N N   . SER B 113 ? 207.2025 207.2025 207.2025 0.0000 0.0000 0.0000 113 SER B N   
4747 C CA  . SER B 113 ? 207.2042 207.2042 207.2042 0.0000 0.0000 0.0000 113 SER B CA  
4748 C C   . SER B 113 ? 207.1128 207.1128 207.1128 0.0000 0.0000 0.0000 113 SER B C   
4749 O O   . SER B 113 ? 207.2523 207.2523 207.2523 0.0000 0.0000 0.0000 113 SER B O   
4750 C CB  . SER B 113 ? 207.3756 207.3756 207.3756 0.0000 0.0000 0.0000 113 SER B CB  
4751 O OG  . SER B 113 ? 207.4780 207.4780 207.4780 0.0000 0.0000 0.0000 113 SER B OG  
4752 N N   . HIS B 114 ? 207.3860 207.3860 207.3860 0.0000 0.0000 0.0000 114 HIS B N   
4753 C CA  . HIS B 114 ? 199.3641 199.3641 199.3641 0.0000 0.0000 0.0000 114 HIS B CA  
4754 C C   . HIS B 114 ? 199.2312 199.2312 199.2312 0.0000 0.0000 0.0000 114 HIS B C   
4755 O O   . HIS B 114 ? 199.1654 199.1654 199.1654 0.0000 0.0000 0.0000 114 HIS B O   
4756 C CB  . HIS B 114 ? 199.1269 199.1269 199.1269 0.0000 0.0000 0.0000 114 HIS B CB  
4757 C CG  . HIS B 114 ? 201.6042 201.6042 201.6042 0.0000 0.0000 0.0000 114 HIS B CG  
4758 N ND1 . HIS B 114 ? 201.5500 201.5500 201.5500 0.0000 0.0000 0.0000 114 HIS B ND1 
4759 C CD2 . HIS B 114 ? 201.1439 201.1439 201.1439 0.0000 0.0000 0.0000 114 HIS B CD2 
4760 C CE1 . HIS B 114 ? 201.0526 201.0526 201.0526 0.0000 0.0000 0.0000 114 HIS B CE1 
4761 N NE2 . HIS B 114 ? 201.7633 201.7633 201.7633 0.0000 0.0000 0.0000 114 HIS B NE2 
4762 N N   . LEU B 115 ? 201.8384 201.8384 201.8384 0.0000 0.0000 0.0000 115 LEU B N   
4763 C CA  . LEU B 115 ? 201.6256 201.6256 201.6256 0.0000 0.0000 0.0000 115 LEU B CA  
4764 C C   . LEU B 115 ? 201.9305 201.9305 201.9305 0.0000 0.0000 0.0000 115 LEU B C   
4765 O O   . LEU B 115 ? 187.6214 187.6214 187.6214 0.0000 0.0000 0.0000 115 LEU B O   
4766 C CB  . LEU B 115 ? 187.2882 187.2882 187.2882 0.0000 0.0000 0.0000 115 LEU B CB  
4767 C CG  . LEU B 115 ? 187.1790 187.1790 187.1790 0.0000 0.0000 0.0000 115 LEU B CG  
4768 C CD1 . LEU B 115 ? 187.2179 187.2179 187.2179 0.0000 0.0000 0.0000 115 LEU B CD1 
4769 C CD2 . LEU B 115 ? 187.2919 187.2919 187.2919 0.0000 0.0000 0.0000 115 LEU B CD2 
4770 N N   . GLN B 116 ? 187.1560 187.1560 187.1560 0.0000 0.0000 0.0000 116 GLN B N   
4771 C CA  . GLN B 116 ? 187.2125 187.2125 187.2125 0.0000 0.0000 0.0000 116 GLN B CA  
4772 C C   . GLN B 116 ? 186.8462 186.8462 186.8462 0.0000 0.0000 0.0000 116 GLN B C   
4773 O O   . GLN B 116 ? 187.0653 187.0653 187.0653 0.0000 0.0000 0.0000 116 GLN B O   
4774 C CB  . GLN B 116 ? 186.8377 186.8377 186.8377 0.0000 0.0000 0.0000 116 GLN B CB  
4775 C CG  . GLN B 116 ? 184.6224 184.6224 184.6224 0.0000 0.0000 0.0000 116 GLN B CG  
4776 C CD  . GLN B 116 ? 184.6522 184.6522 184.6522 0.0000 0.0000 0.0000 116 GLN B CD  
4777 O OE1 . GLN B 116 ? 184.8464 184.8464 184.8464 0.0000 0.0000 0.0000 116 GLN B OE1 
4778 N NE2 . GLN B 116 ? 184.4633 184.4633 184.4633 0.0000 0.0000 0.0000 116 GLN B NE2 
4779 N N   . PRO B 117 ? 184.3702 184.3702 184.3702 0.0000 0.0000 0.0000 117 PRO B N   
4780 C CA  . PRO B 117 ? 184.5254 184.5254 184.5254 0.0000 0.0000 0.0000 117 PRO B CA  
4781 C C   . PRO B 117 ? 184.5255 184.5255 184.5255 0.0000 0.0000 0.0000 117 PRO B C   
4782 O O   . PRO B 117 ? 184.6604 184.6604 184.6604 0.0000 0.0000 0.0000 117 PRO B O   
4783 C CB  . PRO B 117 ? 194.0665 194.0665 194.0665 0.0000 0.0000 0.0000 117 PRO B CB  
4784 C CG  . PRO B 117 ? 194.1441 194.1441 194.1441 0.0000 0.0000 0.0000 117 PRO B CG  
4785 C CD  . PRO B 117 ? 194.2466 194.2466 194.2466 0.0000 0.0000 0.0000 117 PRO B CD  
4786 N N   . GLY B 118 ? 194.3105 194.3105 194.3105 0.0000 0.0000 0.0000 118 GLY B N   
4787 C CA  . GLY B 118 ? 194.5646 194.5646 194.5646 0.0000 0.0000 0.0000 118 GLY B CA  
4788 C C   . GLY B 118 ? 194.6733 194.6733 194.6733 0.0000 0.0000 0.0000 118 GLY B C   
4789 O O   . GLY B 118 ? 194.5790 194.5790 194.5790 0.0000 0.0000 0.0000 118 GLY B O   
4790 N N   . ASP B 119 ? 193.9454 193.9454 193.9454 0.0000 0.0000 0.0000 119 ASP B N   
4791 C CA  . ASP B 119 ? 193.9712 193.9712 193.9712 0.0000 0.0000 0.0000 119 ASP B CA  
4792 C C   . ASP B 119 ? 193.7215 193.7215 193.7215 0.0000 0.0000 0.0000 119 ASP B C   
4793 O O   . ASP B 119 ? 193.9506 193.9506 193.9506 0.0000 0.0000 0.0000 119 ASP B O   
4794 C CB  . ASP B 119 ? 194.1476 194.1476 194.1476 0.0000 0.0000 0.0000 119 ASP B CB  
4795 C CG  . ASP B 119 ? 194.1725 194.1725 194.1725 0.0000 0.0000 0.0000 119 ASP B CG  
4796 O OD1 . ASP B 119 ? 194.2083 194.2083 194.2083 0.0000 0.0000 0.0000 119 ASP B OD1 
4797 O OD2 . ASP B 119 ? 194.1937 194.1937 194.1937 0.0000 0.0000 0.0000 119 ASP B OD2 
4798 N N   . HIS B 120 ? 179.9719 179.9719 179.9719 0.0000 0.0000 0.0000 120 HIS B N   
4799 C CA  . HIS B 120 ? 179.3122 179.3122 179.3122 0.0000 0.0000 0.0000 120 HIS B CA  
4800 C C   . HIS B 120 ? 178.7490 178.7490 178.7490 0.0000 0.0000 0.0000 120 HIS B C   
4801 O O   . HIS B 120 ? 178.8451 178.8451 178.8451 0.0000 0.0000 0.0000 120 HIS B O   
4802 C CB  . HIS B 120 ? 179.1731 179.1731 179.1731 0.0000 0.0000 0.0000 120 HIS B CB  
4803 C CG  . HIS B 120 ? 179.5156 179.5156 179.5156 0.0000 0.0000 0.0000 120 HIS B CG  
4804 N ND1 . HIS B 120 ? 178.9164 178.9164 178.9164 0.0000 0.0000 0.0000 120 HIS B ND1 
4805 C CD2 . HIS B 120 ? 179.7679 179.7679 179.7679 0.0000 0.0000 0.0000 120 HIS B CD2 
4806 C CE1 . HIS B 120 ? 162.1832 162.1832 162.1832 0.0000 0.0000 0.0000 120 HIS B CE1 
4807 N NE2 . HIS B 120 ? 161.7191 161.7191 161.7191 0.0000 0.0000 0.0000 120 HIS B NE2 
4808 N N   . LEU B 121 ? 161.4572 161.4572 161.4572 0.0000 0.0000 0.0000 121 LEU B N   
4809 C CA  . LEU B 121 ? 161.4976 161.4976 161.4976 0.0000 0.0000 0.0000 121 LEU B CA  
4810 C C   . LEU B 121 ? 161.6236 161.6236 161.6236 0.0000 0.0000 0.0000 121 LEU B C   
4811 O O   . LEU B 121 ? 161.8871 161.8871 161.8871 0.0000 0.0000 0.0000 121 LEU B O   
4812 C CB  . LEU B 121 ? 161.5934 161.5934 161.5934 0.0000 0.0000 0.0000 121 LEU B CB  
4813 C CG  . LEU B 121 ? 161.3888 161.3888 161.3888 0.0000 0.0000 0.0000 121 LEU B CG  
4814 C CD1 . LEU B 121 ? 161.3101 161.3101 161.3101 0.0000 0.0000 0.0000 121 LEU B CD1 
4815 C CD2 . LEU B 121 ? 161.4140 161.4140 161.4140 0.0000 0.0000 0.0000 121 LEU B CD2 
4816 N N   . THR B 122 ? 161.5701 161.5701 161.5701 0.0000 0.0000 0.0000 122 THR B N   
4817 C CA  . THR B 122 ? 161.3380 161.3380 161.3380 0.0000 0.0000 0.0000 122 THR B CA  
4818 C C   . THR B 122 ? 161.3915 161.3915 161.3915 0.0000 0.0000 0.0000 122 THR B C   
4819 O O   . THR B 122 ? 161.5508 161.5508 161.5508 0.0000 0.0000 0.0000 122 THR B O   
4820 C CB  . THR B 122 ? 161.5068 161.5068 161.5068 0.0000 0.0000 0.0000 122 THR B CB  
4821 O OG1 . THR B 122 ? 161.3428 161.3428 161.3428 0.0000 0.0000 0.0000 122 THR B OG1 
4822 C CG2 . THR B 122 ? 161.3678 161.3678 161.3678 0.0000 0.0000 0.0000 122 THR B CG2 
4823 N N   . ASP B 123 ? 161.3762 161.3762 161.3762 0.0000 0.0000 0.0000 123 ASP B N   
4824 C CA  . ASP B 123 ? 161.4663 161.4663 161.4663 0.0000 0.0000 0.0000 123 ASP B CA  
4825 C C   . ASP B 123 ? 161.4198 161.4198 161.4198 0.0000 0.0000 0.0000 123 ASP B C   
4826 O O   . ASP B 123 ? 161.3955 161.3955 161.3955 0.0000 0.0000 0.0000 123 ASP B O   
4827 C CB  . ASP B 123 ? 161.3646 161.3646 161.3646 0.0000 0.0000 0.0000 123 ASP B CB  
4828 C CG  . ASP B 123 ? 161.3679 161.3679 161.3679 0.0000 0.0000 0.0000 123 ASP B CG  
4829 O OD1 . ASP B 123 ? 161.3673 161.3673 161.3673 0.0000 0.0000 0.0000 123 ASP B OD1 
4830 O OD2 . ASP B 123 ? 161.4288 161.4288 161.4288 0.0000 0.0000 0.0000 123 ASP B OD2 
4831 N N   . ILE B 124 ? 161.4043 161.4043 161.4043 0.0000 0.0000 0.0000 124 ILE B N   
4832 C CA  . ILE B 124 ? 161.4393 161.4393 161.4393 0.0000 0.0000 0.0000 124 ILE B CA  
4833 C C   . ILE B 124 ? 161.5891 161.5891 161.5891 0.0000 0.0000 0.0000 124 ILE B C   
4834 O O   . ILE B 124 ? 161.3328 161.3328 161.3328 0.0000 0.0000 0.0000 124 ILE B O   
4835 C CB  . ILE B 124 ? 161.4636 161.4636 161.4636 0.0000 0.0000 0.0000 124 ILE B CB  
4836 C CG1 . ILE B 124 ? 161.4223 161.4223 161.4223 0.0000 0.0000 0.0000 124 ILE B CG1 
4837 C CG2 . ILE B 124 ? 161.4341 161.4341 161.4341 0.0000 0.0000 0.0000 124 ILE B CG2 
4838 C CD1 . ILE B 124 ? 161.4244 161.4244 161.4244 0.0000 0.0000 0.0000 124 ILE B CD1 
4839 N N   . THR B 125 ? 161.4313 161.4313 161.4313 0.0000 0.0000 0.0000 125 THR B N   
4840 C CA  . THR B 125 ? 161.4925 161.4925 161.4925 0.0000 0.0000 0.0000 125 THR B CA  
4841 C C   . THR B 125 ? 161.4706 161.4706 161.4706 0.0000 0.0000 0.0000 125 THR B C   
4842 O O   . THR B 125 ? 161.4881 161.4881 161.4881 0.0000 0.0000 0.0000 125 THR B O   
4843 C CB  . THR B 125 ? 161.4192 161.4192 161.4192 0.0000 0.0000 0.0000 125 THR B CB  
4844 O OG1 . THR B 125 ? 161.4982 161.4982 161.4982 0.0000 0.0000 0.0000 125 THR B OG1 
4845 C CG2 . THR B 125 ? 161.7147 161.7147 161.7147 0.0000 0.0000 0.0000 125 THR B CG2 
4846 N N   . LEU B 126 ? 161.3741 161.3741 161.3741 0.0000 0.0000 0.0000 126 LEU B N   
4847 C CA  . LEU B 126 ? 161.2868 161.2868 161.2868 0.0000 0.0000 0.0000 126 LEU B CA  
4848 C C   . LEU B 126 ? 161.3188 161.3188 161.3188 0.0000 0.0000 0.0000 126 LEU B C   
4849 O O   . LEU B 126 ? 161.5145 161.5145 161.5145 0.0000 0.0000 0.0000 126 LEU B O   
4850 C CB  . LEU B 126 ? 161.2958 161.2958 161.2958 0.0000 0.0000 0.0000 126 LEU B CB  
4851 C CG  . LEU B 126 ? 161.3295 161.3295 161.3295 0.0000 0.0000 0.0000 126 LEU B CG  
4852 C CD1 . LEU B 126 ? 161.2569 161.2569 161.2569 0.0000 0.0000 0.0000 126 LEU B CD1 
4853 C CD2 . LEU B 126 ? 161.1962 161.1962 161.1962 0.0000 0.0000 0.0000 126 LEU B CD2 
4854 N N   . LYS B 127 ? 161.3064 161.3064 161.3064 0.0000 0.0000 0.0000 127 LYS B N   
4855 C CA  . LYS B 127 ? 161.4957 161.4957 161.4957 0.0000 0.0000 0.0000 127 LYS B CA  
4856 C C   . LYS B 127 ? 161.3982 161.3982 161.3982 0.0000 0.0000 0.0000 127 LYS B C   
4857 O O   . LYS B 127 ? 161.3647 161.3647 161.3647 0.0000 0.0000 0.0000 127 LYS B O   
4858 C CB  . LYS B 127 ? 161.3382 161.3382 161.3382 0.0000 0.0000 0.0000 127 LYS B CB  
4859 C CG  . LYS B 127 ? 161.4325 161.4325 161.4325 0.0000 0.0000 0.0000 127 LYS B CG  
4860 C CD  . LYS B 127 ? 161.7147 161.7147 161.7147 0.0000 0.0000 0.0000 127 LYS B CD  
4861 C CE  . LYS B 127 ? 161.2041 161.2041 161.2041 0.0000 0.0000 0.0000 127 LYS B CE  
4862 N NZ  . LYS B 127 ? 161.3531 161.3531 161.3531 0.0000 0.0000 0.0000 127 LYS B NZ  
4863 N N   . VAL B 128 ? 161.4536 161.4536 161.4536 0.0000 0.0000 0.0000 128 VAL B N   
4864 C CA  . VAL B 128 ? 161.5576 161.5576 161.5576 0.0000 0.0000 0.0000 128 VAL B CA  
4865 C C   . VAL B 128 ? 161.3761 161.3761 161.3761 0.0000 0.0000 0.0000 128 VAL B C   
4866 O O   . VAL B 128 ? 161.3806 161.3806 161.3806 0.0000 0.0000 0.0000 128 VAL B O   
4867 C CB  . VAL B 128 ? 161.3512 161.3512 161.3512 0.0000 0.0000 0.0000 128 VAL B CB  
4868 C CG1 . VAL B 128 ? 161.9922 161.9922 161.9922 0.0000 0.0000 0.0000 128 VAL B CG1 
4869 C CG2 . VAL B 128 ? 161.5437 161.5437 161.5437 0.0000 0.0000 0.0000 128 VAL B CG2 
4870 N N   . ALA B 129 ? 161.6337 161.6337 161.6337 0.0000 0.0000 0.0000 129 ALA B N   
4871 C CA  . ALA B 129 ? 161.6329 161.6329 161.6329 0.0000 0.0000 0.0000 129 ALA B CA  
4872 C C   . ALA B 129 ? 161.5012 161.5012 161.5012 0.0000 0.0000 0.0000 129 ALA B C   
4873 O O   . ALA B 129 ? 161.8082 161.8082 161.8082 0.0000 0.0000 0.0000 129 ALA B O   
4874 C CB  . ALA B 129 ? 161.7175 161.7175 161.7175 0.0000 0.0000 0.0000 129 ALA B CB  
4875 N N   . GLY B 130 ? 161.3668 161.3668 161.3668 0.0000 0.0000 0.0000 130 GLY B N   
4876 C CA  . GLY B 130 ? 161.4613 161.4613 161.4613 0.0000 0.0000 0.0000 130 GLY B CA  
4877 C C   . GLY B 130 ? 161.6804 161.6804 161.6804 0.0000 0.0000 0.0000 130 GLY B C   
4878 O O   . GLY B 130 ? 161.8323 161.8323 161.8323 0.0000 0.0000 0.0000 130 GLY B O   
4879 N N   . ARG B 131 ? 161.5500 161.5500 161.5500 0.0000 0.0000 0.0000 131 ARG B N   
4880 C CA  . ARG B 131 ? 167.3199 167.3199 167.3199 0.0000 0.0000 0.0000 131 ARG B CA  
4881 C C   . ARG B 131 ? 167.6404 167.6404 167.6404 0.0000 0.0000 0.0000 131 ARG B C   
4882 O O   . ARG B 131 ? 168.2663 168.2663 168.2663 0.0000 0.0000 0.0000 131 ARG B O   
4883 C CB  . ARG B 131 ? 168.2692 168.2692 168.2692 0.0000 0.0000 0.0000 131 ARG B CB  
4884 C CG  . ARG B 131 ? 167.6586 167.6586 167.6586 0.0000 0.0000 0.0000 131 ARG B CG  
4885 C CD  . ARG B 131 ? 167.7397 167.7397 167.7397 0.0000 0.0000 0.0000 131 ARG B CD  
4886 N NE  . ARG B 131 ? 167.6459 167.6459 167.6459 0.0000 0.0000 0.0000 131 ARG B NE  
4887 C CZ  . ARG B 131 ? 167.7106 167.7106 167.7106 0.0000 0.0000 0.0000 131 ARG B CZ  
4888 N NH1 . ARG B 131 ? 167.8184 167.8184 167.8184 0.0000 0.0000 0.0000 131 ARG B NH1 
4889 N NH2 . ARG B 131 ? 187.3583 187.3583 187.3583 0.0000 0.0000 0.0000 131 ARG B NH2 
4890 N N   . ILE B 132 ? 188.0364 188.0364 188.0364 0.0000 0.0000 0.0000 132 ILE B N   
4891 C CA  . ILE B 132 ? 188.3225 188.3225 188.3225 0.0000 0.0000 0.0000 132 ILE B CA  
4892 C C   . ILE B 132 ? 187.9589 187.9589 187.9589 0.0000 0.0000 0.0000 132 ILE B C   
4893 O O   . ILE B 132 ? 188.1400 188.1400 188.1400 0.0000 0.0000 0.0000 132 ILE B O   
4894 C CB  . ILE B 132 ? 188.4075 188.4075 188.4075 0.0000 0.0000 0.0000 132 ILE B CB  
4895 C CG1 . ILE B 132 ? 188.4437 188.4437 188.4437 0.0000 0.0000 0.0000 132 ILE B CG1 
4896 C CG2 . ILE B 132 ? 188.3850 188.3850 188.3850 0.0000 0.0000 0.0000 132 ILE B CG2 
4897 C CD1 . ILE B 132 ? 188.1937 188.1937 188.1937 0.0000 0.0000 0.0000 132 ILE B CD1 
4898 N N   . HIS B 133 ? 188.1536 188.1536 188.1536 0.0000 0.0000 0.0000 133 HIS B N   
4899 C CA  . HIS B 133 ? 188.0687 188.0687 188.0687 0.0000 0.0000 0.0000 133 HIS B CA  
4900 C C   . HIS B 133 ? 202.2378 202.2378 202.2378 0.0000 0.0000 0.0000 133 HIS B C   
4901 O O   . HIS B 133 ? 202.4923 202.4923 202.4923 0.0000 0.0000 0.0000 133 HIS B O   
4902 C CB  . HIS B 133 ? 202.8918 202.8918 202.8918 0.0000 0.0000 0.0000 133 HIS B CB  
4903 C CG  . HIS B 133 ? 202.9723 202.9723 202.9723 0.0000 0.0000 0.0000 133 HIS B CG  
4904 N ND1 . HIS B 133 ? 202.8120 202.8120 202.8120 0.0000 0.0000 0.0000 133 HIS B ND1 
4905 C CD2 . HIS B 133 ? 205.6505 205.6505 205.6505 0.0000 0.0000 0.0000 133 HIS B CD2 
4906 C CE1 . HIS B 133 ? 205.8382 205.8382 205.8382 0.0000 0.0000 0.0000 133 HIS B CE1 
4907 N NE2 . HIS B 133 ? 205.9404 205.9404 205.9404 0.0000 0.0000 0.0000 133 HIS B NE2 
4908 N N   . ALA B 134 ? 205.9580 205.9580 205.9580 0.0000 0.0000 0.0000 134 ALA B N   
4909 C CA  . ALA B 134 ? 205.6226 205.6226 205.6226 0.0000 0.0000 0.0000 134 ALA B CA  
4910 C C   . ALA B 134 ? 205.8529 205.8529 205.8529 0.0000 0.0000 0.0000 134 ALA B C   
4911 O O   . ALA B 134 ? 211.5314 211.5314 211.5314 0.0000 0.0000 0.0000 134 ALA B O   
4912 C CB  . ALA B 134 ? 211.7124 211.7124 211.7124 0.0000 0.0000 0.0000 134 ALA B CB  
4913 N N   . LYS B 135 ? 211.7380 211.7380 211.7380 0.0000 0.0000 0.0000 135 LYS B N   
4914 C CA  . LYS B 135 ? 211.5241 211.5241 211.5241 0.0000 0.0000 0.0000 135 LYS B CA  
4915 C C   . LYS B 135 ? 212.6702 212.6702 212.6702 0.0000 0.0000 0.0000 135 LYS B C   
4916 O O   . LYS B 135 ? 212.7092 212.7092 212.7092 0.0000 0.0000 0.0000 135 LYS B O   
4917 C CB  . LYS B 135 ? 212.4638 212.4638 212.4638 0.0000 0.0000 0.0000 135 LYS B CB  
4918 C CG  . LYS B 135 ? 212.4390 212.4390 212.4390 0.0000 0.0000 0.0000 135 LYS B CG  
4919 C CD  . LYS B 135 ? 206.0513 206.0513 206.0513 0.0000 0.0000 0.0000 135 LYS B CD  
4920 C CE  . LYS B 135 ? 205.8682 205.8682 205.8682 0.0000 0.0000 0.0000 135 LYS B CE  
4921 N NZ  . LYS B 135 ? 205.3110 205.3110 205.3110 0.0000 0.0000 0.0000 135 LYS B NZ  
4922 N N   . ARG B 136 ? 205.2424 205.2424 205.2424 0.0000 0.0000 0.0000 136 ARG B N   
4923 C CA  . ARG B 136 ? 206.0951 206.0951 206.0951 0.0000 0.0000 0.0000 136 ARG B CA  
4924 C C   . ARG B 136 ? 206.2093 206.2093 206.2093 0.0000 0.0000 0.0000 136 ARG B C   
4925 O O   . ARG B 136 ? 206.1611 206.1611 206.1611 0.0000 0.0000 0.0000 136 ARG B O   
4926 C CB  . ARG B 136 ? 206.1274 206.1274 206.1274 0.0000 0.0000 0.0000 136 ARG B CB  
4927 C CG  . ARG B 136 ? 206.1725 206.1725 206.1725 0.0000 0.0000 0.0000 136 ARG B CG  
4928 C CD  . ARG B 136 ? 185.4970 185.4970 185.4970 0.0000 0.0000 0.0000 136 ARG B CD  
4929 N NE  . ARG B 136 ? 184.7205 184.7205 184.7205 0.0000 0.0000 0.0000 136 ARG B NE  
4930 C CZ  . ARG B 136 ? 184.5704 184.5704 184.5704 0.0000 0.0000 0.0000 136 ARG B CZ  
4931 N NH1 . ARG B 136 ? 185.0418 185.0418 185.0418 0.0000 0.0000 0.0000 136 ARG B NH1 
4932 N NH2 . ARG B 136 ? 184.7645 184.7645 184.7645 0.0000 0.0000 0.0000 136 ARG B NH2 
4933 N N   . ALA B 137 ? 184.5019 184.5019 184.5019 0.0000 0.0000 0.0000 137 ALA B N   
4934 C CA  . ALA B 137 ? 184.3563 184.3563 184.3563 0.0000 0.0000 0.0000 137 ALA B CA  
4935 C C   . ALA B 137 ? 184.5432 184.5432 184.5432 0.0000 0.0000 0.0000 137 ALA B C   
4936 O O   . ALA B 137 ? 176.4589 176.4589 176.4589 0.0000 0.0000 0.0000 137 ALA B O   
4937 C CB  . ALA B 137 ? 176.2016 176.2016 176.2016 0.0000 0.0000 0.0000 137 ALA B CB  
4938 N N   . SER B 138 ? 175.8486 175.8486 175.8486 0.0000 0.0000 0.0000 138 SER B N   
4939 C CA  . SER B 138 ? 175.9697 175.9697 175.9697 0.0000 0.0000 0.0000 138 SER B CA  
4940 C C   . SER B 138 ? 176.1107 176.1107 176.1107 0.0000 0.0000 0.0000 138 SER B C   
4941 O O   . SER B 138 ? 176.5073 176.5073 176.5073 0.0000 0.0000 0.0000 138 SER B O   
4942 C CB  . SER B 138 ? 175.9824 175.9824 175.9824 0.0000 0.0000 0.0000 138 SER B CB  
4943 O OG  . SER B 138 ? 176.4045 176.4045 176.4045 0.0000 0.0000 0.0000 138 SER B OG  
4944 N N   . GLY B 139 ? 170.0334 170.0334 170.0334 0.0000 0.0000 0.0000 139 GLY B N   
4945 C CA  . GLY B 139 ? 169.6626 169.6626 169.6626 0.0000 0.0000 0.0000 139 GLY B CA  
4946 C C   . GLY B 139 ? 169.4932 169.4932 169.4932 0.0000 0.0000 0.0000 139 GLY B C   
4947 O O   . GLY B 139 ? 169.8174 169.8174 169.8174 0.0000 0.0000 0.0000 139 GLY B O   
4948 N N   . GLY B 140 ? 169.8129 169.8129 169.8129 0.0000 0.0000 0.0000 140 GLY B N   
4949 C CA  . GLY B 140 ? 169.5844 169.5844 169.5844 0.0000 0.0000 0.0000 140 GLY B CA  
4950 C C   . GLY B 140 ? 169.5850 169.5850 169.5850 0.0000 0.0000 0.0000 140 GLY B C   
4951 O O   . GLY B 140 ? 169.8791 169.8791 169.8791 0.0000 0.0000 0.0000 140 GLY B O   
4952 N N   . LYS B 141 ? 169.7098 169.7098 169.7098 0.0000 0.0000 0.0000 141 LYS B N   
4953 C CA  . LYS B 141 ? 169.9315 169.9315 169.9315 0.0000 0.0000 0.0000 141 LYS B CA  
4954 C C   . LYS B 141 ? 169.8822 169.8822 169.8822 0.0000 0.0000 0.0000 141 LYS B C   
4955 O O   . LYS B 141 ? 161.7656 161.7656 161.7656 0.0000 0.0000 0.0000 141 LYS B O   
4956 C CB  . LYS B 141 ? 161.4238 161.4238 161.4238 0.0000 0.0000 0.0000 141 LYS B CB  
4957 C CG  . LYS B 141 ? 161.5348 161.5348 161.5348 0.0000 0.0000 0.0000 141 LYS B CG  
4958 C CD  . LYS B 141 ? 161.7556 161.7556 161.7556 0.0000 0.0000 0.0000 141 LYS B CD  
4959 C CE  . LYS B 141 ? 161.4156 161.4156 161.4156 0.0000 0.0000 0.0000 141 LYS B CE  
4960 N NZ  . LYS B 141 ? 161.4022 161.4022 161.4022 0.0000 0.0000 0.0000 141 LYS B NZ  
4961 N N   . LEU B 142 ? 161.4979 161.4979 161.4979 0.0000 0.0000 0.0000 142 LEU B N   
4962 C CA  . LEU B 142 ? 161.6224 161.6224 161.6224 0.0000 0.0000 0.0000 142 LEU B CA  
4963 C C   . LEU B 142 ? 161.4854 161.4854 161.4854 0.0000 0.0000 0.0000 142 LEU B C   
4964 O O   . LEU B 142 ? 161.6484 161.6484 161.6484 0.0000 0.0000 0.0000 142 LEU B O   
4965 C CB  . LEU B 142 ? 161.5414 161.5414 161.5414 0.0000 0.0000 0.0000 142 LEU B CB  
4966 C CG  . LEU B 142 ? 162.0567 162.0567 162.0567 0.0000 0.0000 0.0000 142 LEU B CG  
4967 C CD1 . LEU B 142 ? 163.8852 163.8852 163.8852 0.0000 0.0000 0.0000 142 LEU B CD1 
4968 C CD2 . LEU B 142 ? 163.8068 163.8068 163.8068 0.0000 0.0000 0.0000 142 LEU B CD2 
4969 N N   . ILE B 143 ? 163.6805 163.6805 163.6805 0.0000 0.0000 0.0000 143 ILE B N   
4970 C CA  . ILE B 143 ? 163.9350 163.9350 163.9350 0.0000 0.0000 0.0000 143 ILE B CA  
4971 C C   . ILE B 143 ? 163.9360 163.9360 163.9360 0.0000 0.0000 0.0000 143 ILE B C   
4972 O O   . ILE B 143 ? 163.9592 163.9592 163.9592 0.0000 0.0000 0.0000 143 ILE B O   
4973 C CB  . ILE B 143 ? 164.0360 164.0360 164.0360 0.0000 0.0000 0.0000 143 ILE B CB  
4974 C CG1 . ILE B 143 ? 164.0729 164.0729 164.0729 0.0000 0.0000 0.0000 143 ILE B CG1 
4975 C CG2 . ILE B 143 ? 161.2660 161.2660 161.2660 0.0000 0.0000 0.0000 143 ILE B CG2 
4976 C CD1 . ILE B 143 ? 161.2623 161.2623 161.2623 0.0000 0.0000 0.0000 143 ILE B CD1 
4977 N N   . PHE B 144 ? 161.4003 161.4003 161.4003 0.0000 0.0000 0.0000 144 PHE B N   
4978 C CA  . PHE B 144 ? 161.5713 161.5713 161.5713 0.0000 0.0000 0.0000 144 PHE B CA  
4979 C C   . PHE B 144 ? 161.2628 161.2628 161.2628 0.0000 0.0000 0.0000 144 PHE B C   
4980 O O   . PHE B 144 ? 161.3328 161.3328 161.3328 0.0000 0.0000 0.0000 144 PHE B O   
4981 C CB  . PHE B 144 ? 161.5451 161.5451 161.5451 0.0000 0.0000 0.0000 144 PHE B CB  
4982 C CG  . PHE B 144 ? 161.3977 161.3977 161.3977 0.0000 0.0000 0.0000 144 PHE B CG  
4983 C CD1 . PHE B 144 ? 161.3232 161.3232 161.3232 0.0000 0.0000 0.0000 144 PHE B CD1 
4984 C CD2 . PHE B 144 ? 161.2139 161.2139 161.2139 0.0000 0.0000 0.0000 144 PHE B CD2 
4985 C CE1 . PHE B 144 ? 161.2919 161.2919 161.2919 0.0000 0.0000 0.0000 144 PHE B CE1 
4986 C CE2 . PHE B 144 ? 161.3400 161.3400 161.3400 0.0000 0.0000 0.0000 144 PHE B CE2 
4987 C CZ  . PHE B 144 ? 161.3865 161.3865 161.3865 0.0000 0.0000 0.0000 144 PHE B CZ  
4988 N N   . TYR B 145 ? 161.4472 161.4472 161.4472 0.0000 0.0000 0.0000 145 TYR B N   
4989 C CA  . TYR B 145 ? 161.4132 161.4132 161.4132 0.0000 0.0000 0.0000 145 TYR B CA  
4990 C C   . TYR B 145 ? 161.3828 161.3828 161.3828 0.0000 0.0000 0.0000 145 TYR B C   
4991 O O   . TYR B 145 ? 161.5029 161.5029 161.5029 0.0000 0.0000 0.0000 145 TYR B O   
4992 C CB  . TYR B 145 ? 161.5658 161.5658 161.5658 0.0000 0.0000 0.0000 145 TYR B CB  
4993 C CG  . TYR B 145 ? 161.6106 161.6106 161.6106 0.0000 0.0000 0.0000 145 TYR B CG  
4994 C CD1 . TYR B 145 ? 164.3655 164.3655 164.3655 0.0000 0.0000 0.0000 145 TYR B CD1 
4995 C CD2 . TYR B 145 ? 164.6535 164.6535 164.6535 0.0000 0.0000 0.0000 145 TYR B CD2 
4996 C CE1 . TYR B 145 ? 164.8224 164.8224 164.8224 0.0000 0.0000 0.0000 145 TYR B CE1 
4997 C CE2 . TYR B 145 ? 164.7400 164.7400 164.7400 0.0000 0.0000 0.0000 145 TYR B CE2 
4998 C CZ  . TYR B 145 ? 172.3768 172.3768 172.3768 0.0000 0.0000 0.0000 145 TYR B CZ  
4999 O OH  . TYR B 145 ? 172.3776 172.3776 172.3776 0.0000 0.0000 0.0000 145 TYR B OH  
5000 N N   . ASP B 146 ? 172.3004 172.3004 172.3004 0.0000 0.0000 0.0000 146 ASP B N   
5001 C CA  . ASP B 146 ? 172.4791 172.4791 172.4791 0.0000 0.0000 0.0000 146 ASP B CA  
5002 C C   . ASP B 146 ? 172.5110 172.5110 172.5110 0.0000 0.0000 0.0000 146 ASP B C   
5003 O O   . ASP B 146 ? 172.4860 172.4860 172.4860 0.0000 0.0000 0.0000 146 ASP B O   
5004 C CB  . ASP B 146 ? 172.5248 172.5248 172.5248 0.0000 0.0000 0.0000 146 ASP B CB  
5005 C CG  . ASP B 146 ? 172.6505 172.6505 172.6505 0.0000 0.0000 0.0000 146 ASP B CG  
5006 O OD1 . ASP B 146 ? 171.3555 171.3555 171.3555 0.0000 0.0000 0.0000 146 ASP B OD1 
5007 O OD2 . ASP B 146 ? 161.8809 161.8809 161.8809 0.0000 0.0000 0.0000 146 ASP B OD2 
5008 N N   . LEU B 147 ? 161.5289 161.5289 161.5289 0.0000 0.0000 0.0000 147 LEU B N   
5009 C CA  . LEU B 147 ? 161.4110 161.4110 161.4110 0.0000 0.0000 0.0000 147 LEU B CA  
5010 C C   . LEU B 147 ? 161.4849 161.4849 161.4849 0.0000 0.0000 0.0000 147 LEU B C   
5011 O O   . LEU B 147 ? 161.3108 161.3108 161.3108 0.0000 0.0000 0.0000 147 LEU B O   
5012 C CB  . LEU B 147 ? 161.3022 161.3022 161.3022 0.0000 0.0000 0.0000 147 LEU B CB  
5013 C CG  . LEU B 147 ? 161.3080 161.3080 161.3080 0.0000 0.0000 0.0000 147 LEU B CG  
5014 C CD1 . LEU B 147 ? 161.3661 161.3661 161.3661 0.0000 0.0000 0.0000 147 LEU B CD1 
5015 C CD2 . LEU B 147 ? 161.4154 161.4154 161.4154 0.0000 0.0000 0.0000 147 LEU B CD2 
5016 N N   . ARG B 148 ? 161.4788 161.4788 161.4788 0.0000 0.0000 0.0000 148 ARG B N   
5017 C CA  . ARG B 148 ? 161.6714 161.6714 161.6714 0.0000 0.0000 0.0000 148 ARG B CA  
5018 C C   . ARG B 148 ? 161.2829 161.2829 161.2829 0.0000 0.0000 0.0000 148 ARG B C   
5019 O O   . ARG B 148 ? 161.2097 161.2097 161.2097 0.0000 0.0000 0.0000 148 ARG B O   
5020 C CB  . ARG B 148 ? 161.4123 161.4123 161.4123 0.0000 0.0000 0.0000 148 ARG B CB  
5021 C CG  . ARG B 148 ? 161.6633 161.6633 161.6633 0.0000 0.0000 0.0000 148 ARG B CG  
5022 C CD  . ARG B 148 ? 161.2469 161.2469 161.2469 0.0000 0.0000 0.0000 148 ARG B CD  
5023 N NE  . ARG B 148 ? 161.4089 161.4089 161.4089 0.0000 0.0000 0.0000 148 ARG B NE  
5024 C CZ  . ARG B 148 ? 161.5146 161.5146 161.5146 0.0000 0.0000 0.0000 148 ARG B CZ  
5025 N NH1 . ARG B 148 ? 161.4584 161.4584 161.4584 0.0000 0.0000 0.0000 148 ARG B NH1 
5026 N NH2 . ARG B 148 ? 161.4808 161.4808 161.4808 0.0000 0.0000 0.0000 148 ARG B NH2 
5027 N N   . GLY B 149 ? 161.4191 161.4191 161.4191 0.0000 0.0000 0.0000 149 GLY B N   
5028 C CA  . GLY B 149 ? 161.3601 161.3601 161.3601 0.0000 0.0000 0.0000 149 GLY B CA  
5029 C C   . GLY B 149 ? 161.5042 161.5042 161.5042 0.0000 0.0000 0.0000 149 GLY B C   
5030 O O   . GLY B 149 ? 161.8251 161.8251 161.8251 0.0000 0.0000 0.0000 149 GLY B O   
5031 N N   . GLU B 150 ? 161.2990 161.2990 161.2990 0.0000 0.0000 0.0000 150 GLU B N   
5032 C CA  . GLU B 150 ? 161.3587 161.3587 161.3587 0.0000 0.0000 0.0000 150 GLU B CA  
5033 C C   . GLU B 150 ? 161.6225 161.6225 161.6225 0.0000 0.0000 0.0000 150 GLU B C   
5034 O O   . GLU B 150 ? 161.3746 161.3746 161.3746 0.0000 0.0000 0.0000 150 GLU B O   
5035 C CB  . GLU B 150 ? 161.4913 161.4913 161.4913 0.0000 0.0000 0.0000 150 GLU B CB  
5036 C CG  . GLU B 150 ? 161.3726 161.3726 161.3726 0.0000 0.0000 0.0000 150 GLU B CG  
5037 C CD  . GLU B 150 ? 161.4095 161.4095 161.4095 0.0000 0.0000 0.0000 150 GLU B CD  
5038 O OE1 . GLU B 150 ? 161.5579 161.5579 161.5579 0.0000 0.0000 0.0000 150 GLU B OE1 
5039 O OE2 . GLU B 150 ? 161.7651 161.7651 161.7651 0.0000 0.0000 0.0000 150 GLU B OE2 
5040 N N   . GLY B 151 ? 161.9023 161.9023 161.9023 0.0000 0.0000 0.0000 151 GLY B N   
5041 C CA  . GLY B 151 ? 162.0047 162.0047 162.0047 0.0000 0.0000 0.0000 151 GLY B CA  
5042 C C   . GLY B 151 ? 162.4048 162.4048 162.4048 0.0000 0.0000 0.0000 151 GLY B C   
5043 O O   . GLY B 151 ? 161.8656 161.8656 161.8656 0.0000 0.0000 0.0000 151 GLY B O   
5044 N N   . VAL B 152 ? 161.4112 161.4112 161.4112 0.0000 0.0000 0.0000 152 VAL B N   
5045 C CA  . VAL B 152 ? 161.4964 161.4964 161.4964 0.0000 0.0000 0.0000 152 VAL B CA  
5046 C C   . VAL B 152 ? 162.0136 162.0136 162.0136 0.0000 0.0000 0.0000 152 VAL B C   
5047 O O   . VAL B 152 ? 162.1421 162.1421 162.1421 0.0000 0.0000 0.0000 152 VAL B O   
5048 C CB  . VAL B 152 ? 161.4157 161.4157 161.4157 0.0000 0.0000 0.0000 152 VAL B CB  
5049 C CG1 . VAL B 152 ? 161.6055 161.6055 161.6055 0.0000 0.0000 0.0000 152 VAL B CG1 
5050 C CG2 . VAL B 152 ? 161.5560 161.5560 161.5560 0.0000 0.0000 0.0000 152 VAL B CG2 
5051 N N   . LYS B 153 ? 177.7220 177.7220 177.7220 0.0000 0.0000 0.0000 153 LYS B N   
5052 C CA  . LYS B 153 ? 178.3005 178.3005 178.3005 0.0000 0.0000 0.0000 153 LYS B CA  
5053 C C   . LYS B 153 ? 178.4066 178.4066 178.4066 0.0000 0.0000 0.0000 153 LYS B C   
5054 O O   . LYS B 153 ? 178.4039 178.4039 178.4039 0.0000 0.0000 0.0000 153 LYS B O   
5055 C CB  . LYS B 153 ? 178.4035 178.4035 178.4035 0.0000 0.0000 0.0000 153 LYS B CB  
5056 C CG  . LYS B 153 ? 178.3843 178.3843 178.3843 0.0000 0.0000 0.0000 153 LYS B CG  
5057 C CD  . LYS B 153 ? 178.5362 178.5362 178.5362 0.0000 0.0000 0.0000 153 LYS B CD  
5058 C CE  . LYS B 153 ? 178.8617 178.8617 178.8617 0.0000 0.0000 0.0000 153 LYS B CE  
5059 N NZ  . LYS B 153 ? 176.3635 176.3635 176.3635 0.0000 0.0000 0.0000 153 LYS B NZ  
5060 N N   . LEU B 154 ? 176.5043 176.5043 176.5043 0.0000 0.0000 0.0000 154 LEU B N   
5061 C CA  . LEU B 154 ? 176.8601 176.8601 176.8601 0.0000 0.0000 0.0000 154 LEU B CA  
5062 C C   . LEU B 154 ? 177.1415 177.1415 177.1415 0.0000 0.0000 0.0000 154 LEU B C   
5063 O O   . LEU B 154 ? 176.4643 176.4643 176.4643 0.0000 0.0000 0.0000 154 LEU B O   
5064 C CB  . LEU B 154 ? 184.3842 184.3842 184.3842 0.0000 0.0000 0.0000 154 LEU B CB  
5065 C CG  . LEU B 154 ? 184.7828 184.7828 184.7828 0.0000 0.0000 0.0000 154 LEU B CG  
5066 C CD1 . LEU B 154 ? 185.0839 185.0839 185.0839 0.0000 0.0000 0.0000 154 LEU B CD1 
5067 C CD2 . LEU B 154 ? 184.9731 184.9731 184.9731 0.0000 0.0000 0.0000 154 LEU B CD2 
5068 N N   . GLN B 155 ? 184.8103 184.8103 184.8103 0.0000 0.0000 0.0000 155 GLN B N   
5069 C CA  . GLN B 155 ? 185.0603 185.0603 185.0603 0.0000 0.0000 0.0000 155 GLN B CA  
5070 C C   . GLN B 155 ? 185.3801 185.3801 185.3801 0.0000 0.0000 0.0000 155 GLN B C   
5071 O O   . GLN B 155 ? 184.9657 184.9657 184.9657 0.0000 0.0000 0.0000 155 GLN B O   
5072 C CB  . GLN B 155 ? 193.7197 193.7197 193.7197 0.0000 0.0000 0.0000 155 GLN B CB  
5073 C CG  . GLN B 155 ? 193.9226 193.9226 193.9226 0.0000 0.0000 0.0000 155 GLN B CG  
5074 C CD  . GLN B 155 ? 194.0329 194.0329 194.0329 0.0000 0.0000 0.0000 155 GLN B CD  
5075 O OE1 . GLN B 155 ? 193.9503 193.9503 193.9503 0.0000 0.0000 0.0000 155 GLN B OE1 
5076 N NE2 . GLN B 155 ? 194.3616 194.3616 194.3616 0.0000 0.0000 0.0000 155 GLN B NE2 
5077 N N   . VAL B 156 ? 194.4289 194.4289 194.4289 0.0000 0.0000 0.0000 156 VAL B N   
5078 C CA  . VAL B 156 ? 201.4961 201.4961 201.4961 0.0000 0.0000 0.0000 156 VAL B CA  
5079 C C   . VAL B 156 ? 201.6990 201.6990 201.6990 0.0000 0.0000 0.0000 156 VAL B C   
5080 O O   . VAL B 156 ? 201.4445 201.4445 201.4445 0.0000 0.0000 0.0000 156 VAL B O   
5081 C CB  . VAL B 156 ? 201.7753 201.7753 201.7753 0.0000 0.0000 0.0000 156 VAL B CB  
5082 C CG1 . VAL B 156 ? 201.9112 201.9112 201.9112 0.0000 0.0000 0.0000 156 VAL B CG1 
5083 C CG2 . VAL B 156 ? 201.9698 201.9698 201.9698 0.0000 0.0000 0.0000 156 VAL B CG2 
5084 N N   . MET B 157 ? 202.0749 202.0749 202.0749 0.0000 0.0000 0.0000 157 MET B N   
5085 C CA  . MET B 157 ? 202.0363 202.0363 202.0363 0.0000 0.0000 0.0000 157 MET B CA  
5086 C C   . MET B 157 ? 202.1112 202.1112 202.1112 0.0000 0.0000 0.0000 157 MET B C   
5087 O O   . MET B 157 ? 202.1426 202.1426 202.1426 0.0000 0.0000 0.0000 157 MET B O   
5088 C CB  . MET B 157 ? 202.1457 202.1457 202.1457 0.0000 0.0000 0.0000 157 MET B CB  
5089 C CG  . MET B 157 ? 192.2491 192.2491 192.2491 0.0000 0.0000 0.0000 157 MET B CG  
5090 S SD  . MET B 157 ? 192.0595 192.0595 192.0595 0.0000 0.0000 0.0000 157 MET B SD  
5091 C CE  . MET B 157 ? 191.7044 191.7044 191.7044 0.0000 0.0000 0.0000 157 MET B CE  
5092 N N   . ALA B 158 ? 191.6229 191.6229 191.6229 0.0000 0.0000 0.0000 158 ALA B N   
5093 C CA  . ALA B 158 ? 192.1137 192.1137 192.1137 0.0000 0.0000 0.0000 158 ALA B CA  
5094 C C   . ALA B 158 ? 192.3476 192.3476 192.3476 0.0000 0.0000 0.0000 158 ALA B C   
5095 O O   . ALA B 158 ? 192.3427 192.3427 192.3427 0.0000 0.0000 0.0000 158 ALA B O   
5096 C CB  . ALA B 158 ? 192.4495 192.4495 192.4495 0.0000 0.0000 0.0000 158 ALA B CB  
5097 N N   . ASN B 159 ? 176.0701 176.0701 176.0701 0.0000 0.0000 0.0000 159 ASN B N   
5098 C CA  . ASN B 159 ? 175.7322 175.7322 175.7322 0.0000 0.0000 0.0000 159 ASN B CA  
5099 C C   . ASN B 159 ? 175.9711 175.9711 175.9711 0.0000 0.0000 0.0000 159 ASN B C   
5100 O O   . ASN B 159 ? 175.9514 175.9514 175.9514 0.0000 0.0000 0.0000 159 ASN B O   
5101 C CB  . ASN B 159 ? 175.7341 175.7341 175.7341 0.0000 0.0000 0.0000 159 ASN B CB  
5102 C CG  . ASN B 159 ? 175.4973 175.4973 175.4973 0.0000 0.0000 0.0000 159 ASN B CG  
5103 O OD1 . ASN B 159 ? 175.7626 175.7626 175.7626 0.0000 0.0000 0.0000 159 ASN B OD1 
5104 N ND2 . ASN B 159 ? 175.0069 175.0069 175.0069 0.0000 0.0000 0.0000 159 ASN B ND2 
5105 N N   . SER B 160 ? 175.5791 175.5791 175.5791 0.0000 0.0000 0.0000 160 SER B N   
5106 C CA  . SER B 160 ? 174.7350 174.7350 174.7350 0.0000 0.0000 0.0000 160 SER B CA  
5107 C C   . SER B 160 ? 174.9697 174.9697 174.9697 0.0000 0.0000 0.0000 160 SER B C   
5108 O O   . SER B 160 ? 174.9254 174.9254 174.9254 0.0000 0.0000 0.0000 160 SER B O   
5109 C CB  . SER B 160 ? 190.0621 190.0621 190.0621 0.0000 0.0000 0.0000 160 SER B CB  
5110 O OG  . SER B 160 ? 190.5158 190.5158 190.5158 0.0000 0.0000 0.0000 160 SER B OG  
5111 N N   . ARG B 161 ? 190.9975 190.9975 190.9975 0.0000 0.0000 0.0000 161 ARG B N   
5112 C CA  . ARG B 161 ? 191.0098 191.0098 191.0098 0.0000 0.0000 0.0000 161 ARG B CA  
5113 C C   . ARG B 161 ? 190.4397 190.4397 190.4397 0.0000 0.0000 0.0000 161 ARG B C   
5114 O O   . ARG B 161 ? 190.7855 190.7855 190.7855 0.0000 0.0000 0.0000 161 ARG B O   
5115 C CB  . ARG B 161 ? 190.7326 190.7326 190.7326 0.0000 0.0000 0.0000 161 ARG B CB  
5116 C CG  . ARG B 161 ? 190.6258 190.6258 190.6258 0.0000 0.0000 0.0000 161 ARG B CG  
5117 C CD  . ARG B 161 ? 190.9263 190.9263 190.9263 0.0000 0.0000 0.0000 161 ARG B CD  
5118 N NE  . ARG B 161 ? 201.1293 201.1293 201.1293 0.0000 0.0000 0.0000 161 ARG B NE  
5119 C CZ  . ARG B 161 ? 201.4724 201.4724 201.4724 0.0000 0.0000 0.0000 161 ARG B CZ  
5120 N NH1 . ARG B 161 ? 201.5947 201.5947 201.5947 0.0000 0.0000 0.0000 161 ARG B NH1 
5121 N NH2 . ARG B 161 ? 201.2186 201.2186 201.2186 0.0000 0.0000 0.0000 161 ARG B NH2 
5122 N N   . ASN B 162 ? 201.6534 201.6534 201.6534 0.0000 0.0000 0.0000 162 ASN B N   
5123 C CA  . ASN B 162 ? 201.8262 201.8262 201.8262 0.0000 0.0000 0.0000 162 ASN B CA  
5124 C C   . ASN B 162 ? 211.4026 211.4026 211.4026 0.0000 0.0000 0.0000 162 ASN B C   
5125 O O   . ASN B 162 ? 211.5815 211.5815 211.5815 0.0000 0.0000 0.0000 162 ASN B O   
5126 C CB  . ASN B 162 ? 211.4352 211.4352 211.4352 0.0000 0.0000 0.0000 162 ASN B CB  
5127 C CG  . ASN B 162 ? 211.1969 211.1969 211.1969 0.0000 0.0000 0.0000 162 ASN B CG  
5128 O OD1 . ASN B 162 ? 211.7765 211.7765 211.7765 0.0000 0.0000 0.0000 162 ASN B OD1 
5129 N ND2 . ASN B 162 ? 211.8683 211.8683 211.8683 0.0000 0.0000 0.0000 162 ASN B ND2 
5130 N N   . TYR B 163 ? 211.7230 211.7230 211.7230 0.0000 0.0000 0.0000 163 TYR B N   
5131 C CA  . TYR B 163 ? 211.8380 211.8380 211.8380 0.0000 0.0000 0.0000 163 TYR B CA  
5132 C C   . TYR B 163 ? 211.4820 211.4820 211.4820 0.0000 0.0000 0.0000 163 TYR B C   
5133 O O   . TYR B 163 ? 208.2892 208.2892 208.2892 0.0000 0.0000 0.0000 163 TYR B O   
5134 C CB  . TYR B 163 ? 208.1886 208.1886 208.1886 0.0000 0.0000 0.0000 163 TYR B CB  
5135 C CG  . TYR B 163 ? 207.7293 207.7293 207.7293 0.0000 0.0000 0.0000 163 TYR B CG  
5136 C CD1 . TYR B 163 ? 208.3908 208.3908 208.3908 0.0000 0.0000 0.0000 163 TYR B CD1 
5137 C CD2 . TYR B 163 ? 207.6045 207.6045 207.6045 0.0000 0.0000 0.0000 163 TYR B CD2 
5138 C CE1 . TYR B 163 ? 208.4419 208.4419 208.4419 0.0000 0.0000 0.0000 163 TYR B CE1 
5139 C CE2 . TYR B 163 ? 208.4038 208.4038 208.4038 0.0000 0.0000 0.0000 163 TYR B CE2 
5140 C CZ  . TYR B 163 ? 208.4696 208.4696 208.4696 0.0000 0.0000 0.0000 163 TYR B CZ  
5141 O OH  . TYR B 163 ? 208.3881 208.3881 208.3881 0.0000 0.0000 0.0000 163 TYR B OH  
5142 N N   . LYS B 164 ? 198.2560 198.2560 198.2560 0.0000 0.0000 0.0000 164 LYS B N   
5143 C CA  . LYS B 164 ? 197.8373 197.8373 197.8373 0.0000 0.0000 0.0000 164 LYS B CA  
5144 C C   . LYS B 164 ? 197.2582 197.2582 197.2582 0.0000 0.0000 0.0000 164 LYS B C   
5145 O O   . LYS B 164 ? 197.0504 197.0504 197.0504 0.0000 0.0000 0.0000 164 LYS B O   
5146 C CB  . LYS B 164 ? 197.9119 197.9119 197.9119 0.0000 0.0000 0.0000 164 LYS B CB  
5147 C CG  . LYS B 164 ? 198.0343 198.0343 198.0343 0.0000 0.0000 0.0000 164 LYS B CG  
5148 C CD  . LYS B 164 ? 197.9808 197.9808 197.9808 0.0000 0.0000 0.0000 164 LYS B CD  
5149 C CE  . LYS B 164 ? 197.8880 197.8880 197.8880 0.0000 0.0000 0.0000 164 LYS B CE  
5150 N NZ  . LYS B 164 ? 198.0315 198.0315 198.0315 0.0000 0.0000 0.0000 164 LYS B NZ  
5151 N N   . SER B 165 ? 187.0641 187.0641 187.0641 0.0000 0.0000 0.0000 165 SER B N   
5152 C CA  . SER B 165 ? 186.6422 186.6422 186.6422 0.0000 0.0000 0.0000 165 SER B CA  
5153 C C   . SER B 165 ? 186.3858 186.3858 186.3858 0.0000 0.0000 0.0000 165 SER B C   
5154 O O   . SER B 165 ? 186.2619 186.2619 186.2619 0.0000 0.0000 0.0000 165 SER B O   
5155 C CB  . SER B 165 ? 186.8155 186.8155 186.8155 0.0000 0.0000 0.0000 165 SER B CB  
5156 O OG  . SER B 165 ? 186.5674 186.5674 186.5674 0.0000 0.0000 0.0000 165 SER B OG  
5157 N N   . GLU B 166 ? 186.3514 186.3514 186.3514 0.0000 0.0000 0.0000 166 GLU B N   
5158 C CA  . GLU B 166 ? 186.7953 186.7953 186.7953 0.0000 0.0000 0.0000 166 GLU B CA  
5159 C C   . GLU B 166 ? 186.4310 186.4310 186.4310 0.0000 0.0000 0.0000 166 GLU B C   
5160 O O   . GLU B 166 ? 186.9091 186.9091 186.9091 0.0000 0.0000 0.0000 166 GLU B O   
5161 C CB  . GLU B 166 ? 186.5867 186.5867 186.5867 0.0000 0.0000 0.0000 166 GLU B CB  
5162 C CG  . GLU B 166 ? 184.8217 184.8217 184.8217 0.0000 0.0000 0.0000 166 GLU B CG  
5163 C CD  . GLU B 166 ? 184.5100 184.5100 184.5100 0.0000 0.0000 0.0000 166 GLU B CD  
5164 O OE1 . GLU B 166 ? 184.4215 184.4215 184.4215 0.0000 0.0000 0.0000 166 GLU B OE1 
5165 O OE2 . GLU B 166 ? 184.4160 184.4160 184.4160 0.0000 0.0000 0.0000 166 GLU B OE2 
5166 N N   . GLU B 167 ? 184.6274 184.6274 184.6274 0.0000 0.0000 0.0000 167 GLU B N   
5167 C CA  . GLU B 167 ? 184.7704 184.7704 184.7704 0.0000 0.0000 0.0000 167 GLU B CA  
5168 C C   . GLU B 167 ? 184.5158 184.5158 184.5158 0.0000 0.0000 0.0000 167 GLU B C   
5169 O O   . GLU B 167 ? 184.7505 184.7505 184.7505 0.0000 0.0000 0.0000 167 GLU B O   
5170 C CB  . GLU B 167 ? 185.3070 185.3070 185.3070 0.0000 0.0000 0.0000 167 GLU B CB  
5171 C CG  . GLU B 167 ? 185.0626 185.0626 185.0626 0.0000 0.0000 0.0000 167 GLU B CG  
5172 C CD  . GLU B 167 ? 184.5851 184.5851 184.5851 0.0000 0.0000 0.0000 167 GLU B CD  
5173 O OE1 . GLU B 167 ? 184.6411 184.6411 184.6411 0.0000 0.0000 0.0000 167 GLU B OE1 
5174 O OE2 . GLU B 167 ? 185.2889 185.2889 185.2889 0.0000 0.0000 0.0000 167 GLU B OE2 
5175 N N   . GLU B 168 ? 185.1112 185.1112 185.1112 0.0000 0.0000 0.0000 168 GLU B N   
5176 C CA  . GLU B 168 ? 185.2434 185.2434 185.2434 0.0000 0.0000 0.0000 168 GLU B CA  
5177 C C   . GLU B 168 ? 185.1354 185.1354 185.1354 0.0000 0.0000 0.0000 168 GLU B C   
5178 O O   . GLU B 168 ? 185.3536 185.3536 185.3536 0.0000 0.0000 0.0000 168 GLU B O   
5179 C CB  . GLU B 168 ? 185.2746 185.2746 185.2746 0.0000 0.0000 0.0000 168 GLU B CB  
5180 C CG  . GLU B 168 ? 167.1773 167.1773 167.1773 0.0000 0.0000 0.0000 168 GLU B CG  
5181 C CD  . GLU B 168 ? 166.2659 166.2659 166.2659 0.0000 0.0000 0.0000 168 GLU B CD  
5182 O OE1 . GLU B 168 ? 166.4643 166.4643 166.4643 0.0000 0.0000 0.0000 168 GLU B OE1 
5183 O OE2 . GLU B 168 ? 166.2912 166.2912 166.2912 0.0000 0.0000 0.0000 168 GLU B OE2 
5184 N N   . PHE B 169 ? 165.9867 165.9867 165.9867 0.0000 0.0000 0.0000 169 PHE B N   
5185 C CA  . PHE B 169 ? 165.6597 165.6597 165.6597 0.0000 0.0000 0.0000 169 PHE B CA  
5186 C C   . PHE B 169 ? 166.4794 166.4794 166.4794 0.0000 0.0000 0.0000 169 PHE B C   
5187 O O   . PHE B 169 ? 165.5922 165.5922 165.5922 0.0000 0.0000 0.0000 169 PHE B O   
5188 C CB  . PHE B 169 ? 178.8437 178.8437 178.8437 0.0000 0.0000 0.0000 169 PHE B CB  
5189 C CG  . PHE B 169 ? 179.0711 179.0711 179.0711 0.0000 0.0000 0.0000 169 PHE B CG  
5190 C CD1 . PHE B 169 ? 179.0652 179.0652 179.0652 0.0000 0.0000 0.0000 169 PHE B CD1 
5191 C CD2 . PHE B 169 ? 178.9693 178.9693 178.9693 0.0000 0.0000 0.0000 169 PHE B CD2 
5192 C CE1 . PHE B 169 ? 179.3516 179.3516 179.3516 0.0000 0.0000 0.0000 169 PHE B CE1 
5193 C CE2 . PHE B 169 ? 179.3281 179.3281 179.3281 0.0000 0.0000 0.0000 169 PHE B CE2 
5194 C CZ  . PHE B 169 ? 179.2446 179.2446 179.2446 0.0000 0.0000 0.0000 169 PHE B CZ  
5195 N N   . ILE B 170 ? 179.5421 179.5421 179.5421 0.0000 0.0000 0.0000 170 ILE B N   
5196 C CA  . ILE B 170 ? 179.3730 179.3730 179.3730 0.0000 0.0000 0.0000 170 ILE B CA  
5197 C C   . ILE B 170 ? 179.3583 179.3583 179.3583 0.0000 0.0000 0.0000 170 ILE B C   
5198 O O   . ILE B 170 ? 179.0352 179.0352 179.0352 0.0000 0.0000 0.0000 170 ILE B O   
5199 C CB  . ILE B 170 ? 179.4992 179.4992 179.4992 0.0000 0.0000 0.0000 170 ILE B CB  
5200 C CG1 . ILE B 170 ? 179.6568 179.6568 179.6568 0.0000 0.0000 0.0000 170 ILE B CG1 
5201 C CG2 . ILE B 170 ? 179.7467 179.7467 179.7467 0.0000 0.0000 0.0000 170 ILE B CG2 
5202 C CD1 . ILE B 170 ? 179.8097 179.8097 179.8097 0.0000 0.0000 0.0000 170 ILE B CD1 
5203 N N   . HIS B 171 ? 179.7519 179.7519 179.7519 0.0000 0.0000 0.0000 171 HIS B N   
5204 C CA  . HIS B 171 ? 162.3158 162.3158 162.3158 0.0000 0.0000 0.0000 171 HIS B CA  
5205 C C   . HIS B 171 ? 161.7219 161.7219 161.7219 0.0000 0.0000 0.0000 171 HIS B C   
5206 O O   . HIS B 171 ? 161.4982 161.4982 161.4982 0.0000 0.0000 0.0000 171 HIS B O   
5207 C CB  . HIS B 171 ? 161.5540 161.5540 161.5540 0.0000 0.0000 0.0000 171 HIS B CB  
5208 C CG  . HIS B 171 ? 161.4904 161.4904 161.4904 0.0000 0.0000 0.0000 171 HIS B CG  
5209 N ND1 . HIS B 171 ? 161.4265 161.4265 161.4265 0.0000 0.0000 0.0000 171 HIS B ND1 
5210 C CD2 . HIS B 171 ? 161.3024 161.3024 161.3024 0.0000 0.0000 0.0000 171 HIS B CD2 
5211 C CE1 . HIS B 171 ? 161.7551 161.7551 161.7551 0.0000 0.0000 0.0000 171 HIS B CE1 
5212 N NE2 . HIS B 171 ? 161.8994 161.8994 161.8994 0.0000 0.0000 0.0000 171 HIS B NE2 
5213 N N   . ILE B 172 ? 161.6495 161.6495 161.6495 0.0000 0.0000 0.0000 172 ILE B N   
5214 C CA  . ILE B 172 ? 161.4482 161.4482 161.4482 0.0000 0.0000 0.0000 172 ILE B CA  
5215 C C   . ILE B 172 ? 161.4782 161.4782 161.4782 0.0000 0.0000 0.0000 172 ILE B C   
5216 O O   . ILE B 172 ? 161.5893 161.5893 161.5893 0.0000 0.0000 0.0000 172 ILE B O   
5217 C CB  . ILE B 172 ? 161.4068 161.4068 161.4068 0.0000 0.0000 0.0000 172 ILE B CB  
5218 C CG1 . ILE B 172 ? 161.4048 161.4048 161.4048 0.0000 0.0000 0.0000 172 ILE B CG1 
5219 C CG2 . ILE B 172 ? 161.4757 161.4757 161.4757 0.0000 0.0000 0.0000 172 ILE B CG2 
5220 C CD1 . ILE B 172 ? 161.6275 161.6275 161.6275 0.0000 0.0000 0.0000 172 ILE B CD1 
5221 N N   . ASN B 173 ? 161.4561 161.4561 161.4561 0.0000 0.0000 0.0000 173 ASN B N   
5222 C CA  . ASN B 173 ? 161.4459 161.4459 161.4459 0.0000 0.0000 0.0000 173 ASN B CA  
5223 C C   . ASN B 173 ? 161.4080 161.4080 161.4080 0.0000 0.0000 0.0000 173 ASN B C   
5224 O O   . ASN B 173 ? 161.4913 161.4913 161.4913 0.0000 0.0000 0.0000 173 ASN B O   
5225 C CB  . ASN B 173 ? 161.5789 161.5789 161.5789 0.0000 0.0000 0.0000 173 ASN B CB  
5226 C CG  . ASN B 173 ? 161.4840 161.4840 161.4840 0.0000 0.0000 0.0000 173 ASN B CG  
5227 O OD1 . ASN B 173 ? 161.5235 161.5235 161.5235 0.0000 0.0000 0.0000 173 ASN B OD1 
5228 N ND2 . ASN B 173 ? 161.3705 161.3705 161.3705 0.0000 0.0000 0.0000 173 ASN B ND2 
5229 N N   . ASN B 174 ? 161.4135 161.4135 161.4135 0.0000 0.0000 0.0000 174 ASN B N   
5230 C CA  . ASN B 174 ? 161.5689 161.5689 161.5689 0.0000 0.0000 0.0000 174 ASN B CA  
5231 C C   . ASN B 174 ? 161.4204 161.4204 161.4204 0.0000 0.0000 0.0000 174 ASN B C   
5232 O O   . ASN B 174 ? 161.4021 161.4021 161.4021 0.0000 0.0000 0.0000 174 ASN B O   
5233 C CB  . ASN B 174 ? 161.4113 161.4113 161.4113 0.0000 0.0000 0.0000 174 ASN B CB  
5234 C CG  . ASN B 174 ? 161.2512 161.2512 161.2512 0.0000 0.0000 0.0000 174 ASN B CG  
5235 O OD1 . ASN B 174 ? 161.3189 161.3189 161.3189 0.0000 0.0000 0.0000 174 ASN B OD1 
5236 N ND2 . ASN B 174 ? 161.5425 161.5425 161.5425 0.0000 0.0000 0.0000 174 ASN B ND2 
5237 N N   . LYS B 175 ? 161.3370 161.3370 161.3370 0.0000 0.0000 0.0000 175 LYS B N   
5238 C CA  . LYS B 175 ? 161.4600 161.4600 161.4600 0.0000 0.0000 0.0000 175 LYS B CA  
5239 C C   . LYS B 175 ? 161.8609 161.8609 161.8609 0.0000 0.0000 0.0000 175 LYS B C   
5240 O O   . LYS B 175 ? 162.2732 162.2732 162.2732 0.0000 0.0000 0.0000 175 LYS B O   
5241 C CB  . LYS B 175 ? 163.2161 163.2161 163.2161 0.0000 0.0000 0.0000 175 LYS B CB  
5242 C CG  . LYS B 175 ? 162.2430 162.2430 162.2430 0.0000 0.0000 0.0000 175 LYS B CG  
5243 C CD  . LYS B 175 ? 161.4210 161.4210 161.4210 0.0000 0.0000 0.0000 175 LYS B CD  
5244 C CE  . LYS B 175 ? 161.5380 161.5380 161.5380 0.0000 0.0000 0.0000 175 LYS B CE  
5245 N NZ  . LYS B 175 ? 161.4084 161.4084 161.4084 0.0000 0.0000 0.0000 175 LYS B NZ  
5246 N N   . LEU B 176 ? 161.6362 161.6362 161.6362 0.0000 0.0000 0.0000 176 LEU B N   
5247 C CA  . LEU B 176 ? 161.2820 161.2820 161.2820 0.0000 0.0000 0.0000 176 LEU B CA  
5248 C C   . LEU B 176 ? 161.3315 161.3315 161.3315 0.0000 0.0000 0.0000 176 LEU B C   
5249 O O   . LEU B 176 ? 161.2875 161.2875 161.2875 0.0000 0.0000 0.0000 176 LEU B O   
5250 C CB  . LEU B 176 ? 161.4006 161.4006 161.4006 0.0000 0.0000 0.0000 176 LEU B CB  
5251 C CG  . LEU B 176 ? 161.4597 161.4597 161.4597 0.0000 0.0000 0.0000 176 LEU B CG  
5252 C CD1 . LEU B 176 ? 161.5906 161.5906 161.5906 0.0000 0.0000 0.0000 176 LEU B CD1 
5253 C CD2 . LEU B 176 ? 161.7447 161.7447 161.7447 0.0000 0.0000 0.0000 176 LEU B CD2 
5254 N N   . ARG B 177 ? 161.6230 161.6230 161.6230 0.0000 0.0000 0.0000 177 ARG B N   
5255 C CA  . ARG B 177 ? 161.2623 161.2623 161.2623 0.0000 0.0000 0.0000 177 ARG B CA  
5256 C C   . ARG B 177 ? 161.2354 161.2354 161.2354 0.0000 0.0000 0.0000 177 ARG B C   
5257 O O   . ARG B 177 ? 161.3196 161.3196 161.3196 0.0000 0.0000 0.0000 177 ARG B O   
5258 C CB  . ARG B 177 ? 161.5277 161.5277 161.5277 0.0000 0.0000 0.0000 177 ARG B CB  
5259 C CG  . ARG B 177 ? 161.2736 161.2736 161.2736 0.0000 0.0000 0.0000 177 ARG B CG  
5260 C CD  . ARG B 177 ? 161.3611 161.3611 161.3611 0.0000 0.0000 0.0000 177 ARG B CD  
5261 N NE  . ARG B 177 ? 161.5002 161.5002 161.5002 0.0000 0.0000 0.0000 177 ARG B NE  
5262 C CZ  . ARG B 177 ? 161.4183 161.4183 161.4183 0.0000 0.0000 0.0000 177 ARG B CZ  
5263 N NH1 . ARG B 177 ? 161.3669 161.3669 161.3669 0.0000 0.0000 0.0000 177 ARG B NH1 
5264 N NH2 . ARG B 177 ? 161.3708 161.3708 161.3708 0.0000 0.0000 0.0000 177 ARG B NH2 
5265 N N   . ARG B 178 ? 161.3250 161.3250 161.3250 0.0000 0.0000 0.0000 178 ARG B N   
5266 C CA  . ARG B 178 ? 161.4725 161.4725 161.4725 0.0000 0.0000 0.0000 178 ARG B CA  
5267 C C   . ARG B 178 ? 161.3265 161.3265 161.3265 0.0000 0.0000 0.0000 178 ARG B C   
5268 O O   . ARG B 178 ? 161.3451 161.3451 161.3451 0.0000 0.0000 0.0000 178 ARG B O   
5269 C CB  . ARG B 178 ? 161.5985 161.5985 161.5985 0.0000 0.0000 0.0000 178 ARG B CB  
5270 C CG  . ARG B 178 ? 161.4488 161.4488 161.4488 0.0000 0.0000 0.0000 178 ARG B CG  
5271 C CD  . ARG B 178 ? 161.3403 161.3403 161.3403 0.0000 0.0000 0.0000 178 ARG B CD  
5272 N NE  . ARG B 178 ? 161.4135 161.4135 161.4135 0.0000 0.0000 0.0000 178 ARG B NE  
5273 C CZ  . ARG B 178 ? 161.4433 161.4433 161.4433 0.0000 0.0000 0.0000 178 ARG B CZ  
5274 N NH1 . ARG B 178 ? 161.7292 161.7292 161.7292 0.0000 0.0000 0.0000 178 ARG B NH1 
5275 N NH2 . ARG B 178 ? 161.2147 161.2147 161.2147 0.0000 0.0000 0.0000 178 ARG B NH2 
5276 N N   . GLY B 179 ? 161.1329 161.1329 161.1329 0.0000 0.0000 0.0000 179 GLY B N   
5277 C CA  . GLY B 179 ? 161.2758 161.2758 161.2758 0.0000 0.0000 0.0000 179 GLY B CA  
5278 C C   . GLY B 179 ? 161.5625 161.5625 161.5625 0.0000 0.0000 0.0000 179 GLY B C   
5279 O O   . GLY B 179 ? 161.1867 161.1867 161.1867 0.0000 0.0000 0.0000 179 GLY B O   
5280 N N   . ASP B 180 ? 161.4144 161.4144 161.4144 0.0000 0.0000 0.0000 180 ASP B N   
5281 C CA  . ASP B 180 ? 161.4630 161.4630 161.4630 0.0000 0.0000 0.0000 180 ASP B CA  
5282 C C   . ASP B 180 ? 161.3646 161.3646 161.3646 0.0000 0.0000 0.0000 180 ASP B C   
5283 O O   . ASP B 180 ? 161.3633 161.3633 161.3633 0.0000 0.0000 0.0000 180 ASP B O   
5284 C CB  . ASP B 180 ? 161.4721 161.4721 161.4721 0.0000 0.0000 0.0000 180 ASP B CB  
5285 C CG  . ASP B 180 ? 161.8785 161.8785 161.8785 0.0000 0.0000 0.0000 180 ASP B CG  
5286 O OD1 . ASP B 180 ? 161.4888 161.4888 161.4888 0.0000 0.0000 0.0000 180 ASP B OD1 
5287 O OD2 . ASP B 180 ? 161.4087 161.4087 161.4087 0.0000 0.0000 0.0000 180 ASP B OD2 
5288 N N   . ILE B 181 ? 161.4012 161.4012 161.4012 0.0000 0.0000 0.0000 181 ILE B N   
5289 C CA  . ILE B 181 ? 161.4273 161.4273 161.4273 0.0000 0.0000 0.0000 181 ILE B CA  
5290 C C   . ILE B 181 ? 161.5670 161.5670 161.5670 0.0000 0.0000 0.0000 181 ILE B C   
5291 O O   . ILE B 181 ? 161.3399 161.3399 161.3399 0.0000 0.0000 0.0000 181 ILE B O   
5292 C CB  . ILE B 181 ? 161.5175 161.5175 161.5175 0.0000 0.0000 0.0000 181 ILE B CB  
5293 C CG1 . ILE B 181 ? 161.5156 161.5156 161.5156 0.0000 0.0000 0.0000 181 ILE B CG1 
5294 C CG2 . ILE B 181 ? 161.6381 161.6381 161.6381 0.0000 0.0000 0.0000 181 ILE B CG2 
5295 C CD1 . ILE B 181 ? 164.8799 164.8799 164.8799 0.0000 0.0000 0.0000 181 ILE B CD1 
5296 N N   . ILE B 182 ? 165.0622 165.0622 165.0622 0.0000 0.0000 0.0000 182 ILE B N   
5297 C CA  . ILE B 182 ? 164.9751 164.9751 164.9751 0.0000 0.0000 0.0000 182 ILE B CA  
5298 C C   . ILE B 182 ? 165.1810 165.1810 165.1810 0.0000 0.0000 0.0000 182 ILE B C   
5299 O O   . ILE B 182 ? 165.4756 165.4756 165.4756 0.0000 0.0000 0.0000 182 ILE B O   
5300 C CB  . ILE B 182 ? 165.5201 165.5201 165.5201 0.0000 0.0000 0.0000 182 ILE B CB  
5301 C CG1 . ILE B 182 ? 165.4304 165.4304 165.4304 0.0000 0.0000 0.0000 182 ILE B CG1 
5302 C CG2 . ILE B 182 ? 165.7703 165.7703 165.7703 0.0000 0.0000 0.0000 182 ILE B CG2 
5303 C CD1 . ILE B 182 ? 161.4510 161.4510 161.4510 0.0000 0.0000 0.0000 182 ILE B CD1 
5304 N N   . GLY B 183 ? 161.3699 161.3699 161.3699 0.0000 0.0000 0.0000 183 GLY B N   
5305 C CA  . GLY B 183 ? 161.7440 161.7440 161.7440 0.0000 0.0000 0.0000 183 GLY B CA  
5306 C C   . GLY B 183 ? 162.2921 162.2921 162.2921 0.0000 0.0000 0.0000 183 GLY B C   
5307 O O   . GLY B 183 ? 161.6777 161.6777 161.6777 0.0000 0.0000 0.0000 183 GLY B O   
5308 N N   . VAL B 184 ? 161.9000 161.9000 161.9000 0.0000 0.0000 0.0000 184 VAL B N   
5309 C CA  . VAL B 184 ? 161.8485 161.8485 161.8485 0.0000 0.0000 0.0000 184 VAL B CA  
5310 C C   . VAL B 184 ? 166.3231 166.3231 166.3231 0.0000 0.0000 0.0000 184 VAL B C   
5311 O O   . VAL B 184 ? 167.0042 167.0042 167.0042 0.0000 0.0000 0.0000 184 VAL B O   
5312 C CB  . VAL B 184 ? 167.3547 167.3547 167.3547 0.0000 0.0000 0.0000 184 VAL B CB  
5313 C CG1 . VAL B 184 ? 167.1127 167.1127 167.1127 0.0000 0.0000 0.0000 184 VAL B CG1 
5314 C CG2 . VAL B 184 ? 186.3605 186.3605 186.3605 0.0000 0.0000 0.0000 184 VAL B CG2 
5315 N N   . GLN B 185 ? 186.6229 186.6229 186.6229 0.0000 0.0000 0.0000 185 GLN B N   
5316 C CA  . GLN B 185 ? 187.1724 187.1724 187.1724 0.0000 0.0000 0.0000 185 GLN B CA  
5317 C C   . GLN B 185 ? 187.1943 187.1943 187.1943 0.0000 0.0000 0.0000 185 GLN B C   
5318 O O   . GLN B 185 ? 187.0690 187.0690 187.0690 0.0000 0.0000 0.0000 185 GLN B O   
5319 C CB  . GLN B 185 ? 186.9465 186.9465 186.9465 0.0000 0.0000 0.0000 185 GLN B CB  
5320 C CG  . GLN B 185 ? 187.3611 187.3611 187.3611 0.0000 0.0000 0.0000 185 GLN B CG  
5321 C CD  . GLN B 185 ? 186.9324 186.9324 186.9324 0.0000 0.0000 0.0000 185 GLN B CD  
5322 O OE1 . GLN B 185 ? 187.0136 187.0136 187.0136 0.0000 0.0000 0.0000 185 GLN B OE1 
5323 N NE2 . GLN B 185 ? 195.7763 195.7763 195.7763 0.0000 0.0000 0.0000 185 GLN B NE2 
5324 N N   . GLY B 186 ? 196.2419 196.2419 196.2419 0.0000 0.0000 0.0000 186 GLY B N   
5325 C CA  . GLY B 186 ? 196.6576 196.6576 196.6576 0.0000 0.0000 0.0000 186 GLY B CA  
5326 C C   . GLY B 186 ? 196.6672 196.6672 196.6672 0.0000 0.0000 0.0000 186 GLY B C   
5327 O O   . GLY B 186 ? 196.2359 196.2359 196.2359 0.0000 0.0000 0.0000 186 GLY B O   
5328 N N   . ASN B 187 ? 196.5219 196.5219 196.5219 0.0000 0.0000 0.0000 187 ASN B N   
5329 C CA  . ASN B 187 ? 195.9217 195.9217 195.9217 0.0000 0.0000 0.0000 187 ASN B CA  
5330 C C   . ASN B 187 ? 208.4955 208.4955 208.4955 0.0000 0.0000 0.0000 187 ASN B C   
5331 O O   . ASN B 187 ? 208.8687 208.8687 208.8687 0.0000 0.0000 0.0000 187 ASN B O   
5332 C CB  . ASN B 187 ? 208.9769 208.9769 208.9769 0.0000 0.0000 0.0000 187 ASN B CB  
5333 C CG  . ASN B 187 ? 209.1260 209.1260 209.1260 0.0000 0.0000 0.0000 187 ASN B CG  
5334 O OD1 . ASN B 187 ? 209.0694 209.0694 209.0694 0.0000 0.0000 0.0000 187 ASN B OD1 
5335 N ND2 . ASN B 187 ? 209.1053 209.1053 209.1053 0.0000 0.0000 0.0000 187 ASN B ND2 
5336 N N   . PRO B 188 ? 209.0241 209.0241 209.0241 0.0000 0.0000 0.0000 188 PRO B N   
5337 C CA  . PRO B 188 ? 209.0200 209.0200 209.0200 0.0000 0.0000 0.0000 188 PRO B CA  
5338 C C   . PRO B 188 ? 208.9107 208.9107 208.9107 0.0000 0.0000 0.0000 188 PRO B C   
5339 O O   . PRO B 188 ? 211.4590 211.4590 211.4590 0.0000 0.0000 0.0000 188 PRO B O   
5340 C CB  . PRO B 188 ? 211.5625 211.5625 211.5625 0.0000 0.0000 0.0000 188 PRO B CB  
5341 C CG  . PRO B 188 ? 211.4953 211.4953 211.4953 0.0000 0.0000 0.0000 188 PRO B CG  
5342 C CD  . PRO B 188 ? 211.6881 211.6881 211.6881 0.0000 0.0000 0.0000 188 PRO B CD  
5343 N N   . GLY B 189 ? 211.7391 211.7391 211.7391 0.0000 0.0000 0.0000 189 GLY B N   
5344 C CA  . GLY B 189 ? 211.7921 211.7921 211.7921 0.0000 0.0000 0.0000 189 GLY B CA  
5345 C C   . GLY B 189 ? 211.8613 211.8613 211.8613 0.0000 0.0000 0.0000 189 GLY B C   
5346 O O   . GLY B 189 ? 211.8347 211.8347 211.8347 0.0000 0.0000 0.0000 189 GLY B O   
5347 N N   . LYS B 190 ? 211.8081 211.8081 211.8081 0.0000 0.0000 0.0000 190 LYS B N   
5348 C CA  . LYS B 190 ? 202.9433 202.9433 202.9433 0.0000 0.0000 0.0000 190 LYS B CA  
5349 C C   . LYS B 190 ? 202.7188 202.7188 202.7188 0.0000 0.0000 0.0000 190 LYS B C   
5350 O O   . LYS B 190 ? 202.3674 202.3674 202.3674 0.0000 0.0000 0.0000 190 LYS B O   
5351 C CB  . LYS B 190 ? 202.4783 202.4783 202.4783 0.0000 0.0000 0.0000 190 LYS B CB  
5352 C CG  . LYS B 190 ? 193.5214 193.5214 193.5214 0.0000 0.0000 0.0000 190 LYS B CG  
5353 C CD  . LYS B 190 ? 192.9715 192.9715 192.9715 0.0000 0.0000 0.0000 190 LYS B CD  
5354 C CE  . LYS B 190 ? 192.2181 192.2181 192.2181 0.0000 0.0000 0.0000 190 LYS B CE  
5355 N NZ  . LYS B 190 ? 192.3817 192.3817 192.3817 0.0000 0.0000 0.0000 190 LYS B NZ  
5356 N N   . THR B 191 ? 192.9410 192.9410 192.9410 0.0000 0.0000 0.0000 191 THR B N   
5357 C CA  . THR B 191 ? 192.7129 192.7129 192.7129 0.0000 0.0000 0.0000 191 THR B CA  
5358 C C   . THR B 191 ? 192.8674 192.8674 192.8674 0.0000 0.0000 0.0000 191 THR B C   
5359 O O   . THR B 191 ? 192.8174 192.8174 192.8174 0.0000 0.0000 0.0000 191 THR B O   
5360 C CB  . THR B 191 ? 193.0657 193.0657 193.0657 0.0000 0.0000 0.0000 191 THR B CB  
5361 O OG1 . THR B 191 ? 169.3843 169.3843 169.3843 0.0000 0.0000 0.0000 191 THR B OG1 
5362 C CG2 . THR B 191 ? 168.8751 168.8751 168.8751 0.0000 0.0000 0.0000 191 THR B CG2 
5363 N N   . LYS B 192 ? 168.4888 168.4888 168.4888 0.0000 0.0000 0.0000 192 LYS B N   
5364 C CA  . LYS B 192 ? 168.6693 168.6693 168.6693 0.0000 0.0000 0.0000 192 LYS B CA  
5365 C C   . LYS B 192 ? 168.5336 168.5336 168.5336 0.0000 0.0000 0.0000 192 LYS B C   
5366 O O   . LYS B 192 ? 168.1994 168.1994 168.1994 0.0000 0.0000 0.0000 192 LYS B O   
5367 C CB  . LYS B 192 ? 168.3557 168.3557 168.3557 0.0000 0.0000 0.0000 192 LYS B CB  
5368 C CG  . LYS B 192 ? 168.2708 168.2708 168.2708 0.0000 0.0000 0.0000 192 LYS B CG  
5369 C CD  . LYS B 192 ? 164.6407 164.6407 164.6407 0.0000 0.0000 0.0000 192 LYS B CD  
5370 C CE  . LYS B 192 ? 164.2545 164.2545 164.2545 0.0000 0.0000 0.0000 192 LYS B CE  
5371 N NZ  . LYS B 192 ? 164.2173 164.2173 164.2173 0.0000 0.0000 0.0000 192 LYS B NZ  
5372 N N   . LYS B 193 ? 164.5577 164.5577 164.5577 0.0000 0.0000 0.0000 193 LYS B N   
5373 C CA  . LYS B 193 ? 164.5268 164.5268 164.5268 0.0000 0.0000 0.0000 193 LYS B CA  
5374 C C   . LYS B 193 ? 165.0945 165.0945 165.0945 0.0000 0.0000 0.0000 193 LYS B C   
5375 O O   . LYS B 193 ? 161.5072 161.5072 161.5072 0.0000 0.0000 0.0000 193 LYS B O   
5376 C CB  . LYS B 193 ? 161.4996 161.4996 161.4996 0.0000 0.0000 0.0000 193 LYS B CB  
5377 C CG  . LYS B 193 ? 161.4216 161.4216 161.4216 0.0000 0.0000 0.0000 193 LYS B CG  
5378 C CD  . LYS B 193 ? 161.6090 161.6090 161.6090 0.0000 0.0000 0.0000 193 LYS B CD  
5379 C CE  . LYS B 193 ? 161.4176 161.4176 161.4176 0.0000 0.0000 0.0000 193 LYS B CE  
5380 N NZ  . LYS B 193 ? 161.4574 161.4574 161.4574 0.0000 0.0000 0.0000 193 LYS B NZ  
5381 N N   . GLY B 194 ? 161.4459 161.4459 161.4459 0.0000 0.0000 0.0000 194 GLY B N   
5382 C CA  . GLY B 194 ? 161.5593 161.5593 161.5593 0.0000 0.0000 0.0000 194 GLY B CA  
5383 C C   . GLY B 194 ? 161.4150 161.4150 161.4150 0.0000 0.0000 0.0000 194 GLY B C   
5384 O O   . GLY B 194 ? 161.4304 161.4304 161.4304 0.0000 0.0000 0.0000 194 GLY B O   
5385 N N   . GLU B 195 ? 161.4601 161.4601 161.4601 0.0000 0.0000 0.0000 195 GLU B N   
5386 C CA  . GLU B 195 ? 161.6216 161.6216 161.6216 0.0000 0.0000 0.0000 195 GLU B CA  
5387 C C   . GLU B 195 ? 161.5999 161.5999 161.5999 0.0000 0.0000 0.0000 195 GLU B C   
5388 O O   . GLU B 195 ? 161.7779 161.7779 161.7779 0.0000 0.0000 0.0000 195 GLU B O   
5389 C CB  . GLU B 195 ? 161.9410 161.9410 161.9410 0.0000 0.0000 0.0000 195 GLU B CB  
5390 C CG  . GLU B 195 ? 162.2047 162.2047 162.2047 0.0000 0.0000 0.0000 195 GLU B CG  
5391 C CD  . GLU B 195 ? 161.4693 161.4693 161.4693 0.0000 0.0000 0.0000 195 GLU B CD  
5392 O OE1 . GLU B 195 ? 161.4103 161.4103 161.4103 0.0000 0.0000 0.0000 195 GLU B OE1 
5393 O OE2 . GLU B 195 ? 161.6842 161.6842 161.6842 0.0000 0.0000 0.0000 195 GLU B OE2 
5394 N N   . LEU B 196 ? 161.9985 161.9985 161.9985 0.0000 0.0000 0.0000 196 LEU B N   
5395 C CA  . LEU B 196 ? 161.4614 161.4614 161.4614 0.0000 0.0000 0.0000 196 LEU B CA  
5396 C C   . LEU B 196 ? 161.7844 161.7844 161.7844 0.0000 0.0000 0.0000 196 LEU B C   
5397 O O   . LEU B 196 ? 161.9239 161.9239 161.9239 0.0000 0.0000 0.0000 196 LEU B O   
5398 C CB  . LEU B 196 ? 168.3890 168.3890 168.3890 0.0000 0.0000 0.0000 196 LEU B CB  
5399 C CG  . LEU B 196 ? 168.7337 168.7337 168.7337 0.0000 0.0000 0.0000 196 LEU B CG  
5400 C CD1 . LEU B 196 ? 168.9062 168.9062 168.9062 0.0000 0.0000 0.0000 196 LEU B CD1 
5401 C CD2 . LEU B 196 ? 169.3863 169.3863 169.3863 0.0000 0.0000 0.0000 196 LEU B CD2 
5402 N N   . SER B 197 ? 168.7717 168.7717 168.7717 0.0000 0.0000 0.0000 197 SER B N   
5403 C CA  . SER B 197 ? 168.8771 168.8771 168.8771 0.0000 0.0000 0.0000 197 SER B CA  
5404 C C   . SER B 197 ? 169.0521 169.0521 169.0521 0.0000 0.0000 0.0000 197 SER B C   
5405 O O   . SER B 197 ? 168.8931 168.8931 168.8931 0.0000 0.0000 0.0000 197 SER B O   
5406 C CB  . SER B 197 ? 169.0902 169.0902 169.0902 0.0000 0.0000 0.0000 197 SER B CB  
5407 O OG  . SER B 197 ? 169.0273 169.0273 169.0273 0.0000 0.0000 0.0000 197 SER B OG  
5408 N N   . ILE B 198 ? 169.1134 169.1134 169.1134 0.0000 0.0000 0.0000 198 ILE B N   
5409 C CA  . ILE B 198 ? 169.1407 169.1407 169.1407 0.0000 0.0000 0.0000 198 ILE B CA  
5410 C C   . ILE B 198 ? 171.3928 171.3928 171.3928 0.0000 0.0000 0.0000 198 ILE B C   
5411 O O   . ILE B 198 ? 171.5533 171.5533 171.5533 0.0000 0.0000 0.0000 198 ILE B O   
5412 C CB  . ILE B 198 ? 171.2886 171.2886 171.2886 0.0000 0.0000 0.0000 198 ILE B CB  
5413 C CG1 . ILE B 198 ? 171.3576 171.3576 171.3576 0.0000 0.0000 0.0000 198 ILE B CG1 
5414 C CG2 . ILE B 198 ? 171.8566 171.8566 171.8566 0.0000 0.0000 0.0000 198 ILE B CG2 
5415 C CD1 . ILE B 198 ? 171.8728 171.8728 171.8728 0.0000 0.0000 0.0000 198 ILE B CD1 
5416 N N   . ILE B 199 ? 172.0407 172.0407 172.0407 0.0000 0.0000 0.0000 199 ILE B N   
5417 C CA  . ILE B 199 ? 172.0130 172.0130 172.0130 0.0000 0.0000 0.0000 199 ILE B CA  
5418 C C   . ILE B 199 ? 172.2421 172.2421 172.2421 0.0000 0.0000 0.0000 199 ILE B C   
5419 O O   . ILE B 199 ? 161.7989 161.7989 161.7989 0.0000 0.0000 0.0000 199 ILE B O   
5420 C CB  . ILE B 199 ? 161.5492 161.5492 161.5492 0.0000 0.0000 0.0000 199 ILE B CB  
5421 C CG1 . ILE B 199 ? 161.5355 161.5355 161.5355 0.0000 0.0000 0.0000 199 ILE B CG1 
5422 C CG2 . ILE B 199 ? 161.6725 161.6725 161.6725 0.0000 0.0000 0.0000 199 ILE B CG2 
5423 C CD1 . ILE B 199 ? 161.4129 161.4129 161.4129 0.0000 0.0000 0.0000 199 ILE B CD1 
5424 N N   . PRO B 200 ? 161.5411 161.5411 161.5411 0.0000 0.0000 0.0000 200 PRO B N   
5425 C CA  . PRO B 200 ? 161.5640 161.5640 161.5640 0.0000 0.0000 0.0000 200 PRO B CA  
5426 C C   . PRO B 200 ? 161.4820 161.4820 161.4820 0.0000 0.0000 0.0000 200 PRO B C   
5427 O O   . PRO B 200 ? 161.5136 161.5136 161.5136 0.0000 0.0000 0.0000 200 PRO B O   
5428 C CB  . PRO B 200 ? 161.3180 161.3180 161.3180 0.0000 0.0000 0.0000 200 PRO B CB  
5429 C CG  . PRO B 200 ? 161.2851 161.2851 161.2851 0.0000 0.0000 0.0000 200 PRO B CG  
5430 C CD  . PRO B 200 ? 161.5025 161.5025 161.5025 0.0000 0.0000 0.0000 200 PRO B CD  
5431 N N   . TYR B 201 ? 161.4739 161.4739 161.4739 0.0000 0.0000 0.0000 201 TYR B N   
5432 C CA  . TYR B 201 ? 161.6142 161.6142 161.6142 0.0000 0.0000 0.0000 201 TYR B CA  
5433 C C   . TYR B 201 ? 161.5026 161.5026 161.5026 0.0000 0.0000 0.0000 201 TYR B C   
5434 O O   . TYR B 201 ? 161.2267 161.2267 161.2267 0.0000 0.0000 0.0000 201 TYR B O   
5435 C CB  . TYR B 201 ? 161.3023 161.3023 161.3023 0.0000 0.0000 0.0000 201 TYR B CB  
5436 C CG  . TYR B 201 ? 161.3444 161.3444 161.3444 0.0000 0.0000 0.0000 201 TYR B CG  
5437 C CD1 . TYR B 201 ? 161.5271 161.5271 161.5271 0.0000 0.0000 0.0000 201 TYR B CD1 
5438 C CD2 . TYR B 201 ? 161.4607 161.4607 161.4607 0.0000 0.0000 0.0000 201 TYR B CD2 
5439 C CE1 . TYR B 201 ? 161.4885 161.4885 161.4885 0.0000 0.0000 0.0000 201 TYR B CE1 
5440 C CE2 . TYR B 201 ? 161.5250 161.5250 161.5250 0.0000 0.0000 0.0000 201 TYR B CE2 
5441 C CZ  . TYR B 201 ? 161.5626 161.5626 161.5626 0.0000 0.0000 0.0000 201 TYR B CZ  
5442 O OH  . TYR B 201 ? 161.3818 161.3818 161.3818 0.0000 0.0000 0.0000 201 TYR B OH  
5443 N N   . GLU B 202 ? 161.3943 161.3943 161.3943 0.0000 0.0000 0.0000 202 GLU B N   
5444 C CA  . GLU B 202 ? 161.4434 161.4434 161.4434 0.0000 0.0000 0.0000 202 GLU B CA  
5445 C C   . GLU B 202 ? 161.5136 161.5136 161.5136 0.0000 0.0000 0.0000 202 GLU B C   
5446 O O   . GLU B 202 ? 161.4626 161.4626 161.4626 0.0000 0.0000 0.0000 202 GLU B O   
5447 C CB  . GLU B 202 ? 161.3995 161.3995 161.3995 0.0000 0.0000 0.0000 202 GLU B CB  
5448 C CG  . GLU B 202 ? 161.4620 161.4620 161.4620 0.0000 0.0000 0.0000 202 GLU B CG  
5449 C CD  . GLU B 202 ? 161.5550 161.5550 161.5550 0.0000 0.0000 0.0000 202 GLU B CD  
5450 O OE1 . GLU B 202 ? 161.5401 161.5401 161.5401 0.0000 0.0000 0.0000 202 GLU B OE1 
5451 O OE2 . GLU B 202 ? 161.4694 161.4694 161.4694 0.0000 0.0000 0.0000 202 GLU B OE2 
5452 N N   . ILE B 203 ? 161.4727 161.4727 161.4727 0.0000 0.0000 0.0000 203 ILE B N   
5453 C CA  . ILE B 203 ? 161.6152 161.6152 161.6152 0.0000 0.0000 0.0000 203 ILE B CA  
5454 C C   . ILE B 203 ? 161.5626 161.5626 161.5626 0.0000 0.0000 0.0000 203 ILE B C   
5455 O O   . ILE B 203 ? 161.7212 161.7212 161.7212 0.0000 0.0000 0.0000 203 ILE B O   
5456 C CB  . ILE B 203 ? 161.2745 161.2745 161.2745 0.0000 0.0000 0.0000 203 ILE B CB  
5457 C CG1 . ILE B 203 ? 161.3184 161.3184 161.3184 0.0000 0.0000 0.0000 203 ILE B CG1 
5458 C CG2 . ILE B 203 ? 161.4259 161.4259 161.4259 0.0000 0.0000 0.0000 203 ILE B CG2 
5459 C CD1 . ILE B 203 ? 161.6660 161.6660 161.6660 0.0000 0.0000 0.0000 203 ILE B CD1 
5460 N N   . THR B 204 ? 161.4085 161.4085 161.4085 0.0000 0.0000 0.0000 204 THR B N   
5461 C CA  . THR B 204 ? 161.4239 161.4239 161.4239 0.0000 0.0000 0.0000 204 THR B CA  
5462 C C   . THR B 204 ? 161.3271 161.3271 161.3271 0.0000 0.0000 0.0000 204 THR B C   
5463 O O   . THR B 204 ? 161.3531 161.3531 161.3531 0.0000 0.0000 0.0000 204 THR B O   
5464 C CB  . THR B 204 ? 161.3803 161.3803 161.3803 0.0000 0.0000 0.0000 204 THR B CB  
5465 O OG1 . THR B 204 ? 161.4392 161.4392 161.4392 0.0000 0.0000 0.0000 204 THR B OG1 
5466 C CG2 . THR B 204 ? 161.6392 161.6392 161.6392 0.0000 0.0000 0.0000 204 THR B CG2 
5467 N N   . LEU B 205 ? 161.4176 161.4176 161.4176 0.0000 0.0000 0.0000 205 LEU B N   
5468 C CA  . LEU B 205 ? 161.3720 161.3720 161.3720 0.0000 0.0000 0.0000 205 LEU B CA  
5469 C C   . LEU B 205 ? 161.4195 161.4195 161.4195 0.0000 0.0000 0.0000 205 LEU B C   
5470 O O   . LEU B 205 ? 161.3813 161.3813 161.3813 0.0000 0.0000 0.0000 205 LEU B O   
5471 C CB  . LEU B 205 ? 161.4386 161.4386 161.4386 0.0000 0.0000 0.0000 205 LEU B CB  
5472 C CG  . LEU B 205 ? 161.7590 161.7590 161.7590 0.0000 0.0000 0.0000 205 LEU B CG  
5473 C CD1 . LEU B 205 ? 161.4079 161.4079 161.4079 0.0000 0.0000 0.0000 205 LEU B CD1 
5474 C CD2 . LEU B 205 ? 161.2366 161.2366 161.2366 0.0000 0.0000 0.0000 205 LEU B CD2 
5475 N N   . LEU B 206 ? 161.4351 161.4351 161.4351 0.0000 0.0000 0.0000 206 LEU B N   
5476 C CA  . LEU B 206 ? 161.5094 161.5094 161.5094 0.0000 0.0000 0.0000 206 LEU B CA  
5477 C C   . LEU B 206 ? 161.4206 161.4206 161.4206 0.0000 0.0000 0.0000 206 LEU B C   
5478 O O   . LEU B 206 ? 161.6330 161.6330 161.6330 0.0000 0.0000 0.0000 206 LEU B O   
5479 C CB  . LEU B 206 ? 162.0186 162.0186 162.0186 0.0000 0.0000 0.0000 206 LEU B CB  
5480 C CG  . LEU B 206 ? 161.8994 161.8994 161.8994 0.0000 0.0000 0.0000 206 LEU B CG  
5481 C CD1 . LEU B 206 ? 161.5719 161.5719 161.5719 0.0000 0.0000 0.0000 206 LEU B CD1 
5482 C CD2 . LEU B 206 ? 161.3274 161.3274 161.3274 0.0000 0.0000 0.0000 206 LEU B CD2 
5483 N N   . SER B 207 ? 161.2996 161.2996 161.2996 0.0000 0.0000 0.0000 207 SER B N   
5484 C CA  . SER B 207 ? 161.3940 161.3940 161.3940 0.0000 0.0000 0.0000 207 SER B CA  
5485 C C   . SER B 207 ? 161.3188 161.3188 161.3188 0.0000 0.0000 0.0000 207 SER B C   
5486 O O   . SER B 207 ? 161.2265 161.2265 161.2265 0.0000 0.0000 0.0000 207 SER B O   
5487 C CB  . SER B 207 ? 178.3971 178.3971 178.3971 0.0000 0.0000 0.0000 207 SER B CB  
5488 O OG  . SER B 207 ? 178.7825 178.7825 178.7825 0.0000 0.0000 0.0000 207 SER B OG  
5489 N N   . PRO B 208 ? 178.8803 178.8803 178.8803 0.0000 0.0000 0.0000 208 PRO B N   
5490 C CA  . PRO B 208 ? 178.9995 178.9995 178.9995 0.0000 0.0000 0.0000 208 PRO B CA  
5491 C C   . PRO B 208 ? 179.1180 179.1180 179.1180 0.0000 0.0000 0.0000 208 PRO B C   
5492 O O   . PRO B 208 ? 179.1644 179.1644 179.1644 0.0000 0.0000 0.0000 208 PRO B O   
5493 C CB  . PRO B 208 ? 179.2738 179.2738 179.2738 0.0000 0.0000 0.0000 208 PRO B CB  
5494 C CG  . PRO B 208 ? 180.0060 180.0060 180.0060 0.0000 0.0000 0.0000 208 PRO B CG  
5495 C CD  . PRO B 208 ? 175.0623 175.0623 175.0623 0.0000 0.0000 0.0000 208 PRO B CD  
5496 N N   . CYS B 209 ? 175.2265 175.2265 175.2265 0.0000 0.0000 0.0000 209 CYS B N   
5497 C CA  . CYS B 209 ? 175.7755 175.7755 175.7755 0.0000 0.0000 0.0000 209 CYS B CA  
5498 C C   . CYS B 209 ? 175.7383 175.7383 175.7383 0.0000 0.0000 0.0000 209 CYS B C   
5499 O O   . CYS B 209 ? 175.1070 175.1070 175.1070 0.0000 0.0000 0.0000 209 CYS B O   
5500 C CB  . CYS B 209 ? 174.8400 174.8400 174.8400 0.0000 0.0000 0.0000 209 CYS B CB  
5501 S SG  . CYS B 209 ? 174.7671 174.7671 174.7671 0.0000 0.0000 0.0000 209 CYS B SG  
5502 N N   . LEU B 210 ? 174.8709 174.8709 174.8709 0.0000 0.0000 0.0000 210 LEU B N   
5503 C CA  . LEU B 210 ? 196.6577 196.6577 196.6577 0.0000 0.0000 0.0000 210 LEU B CA  
5504 C C   . LEU B 210 ? 197.7028 197.7028 197.7028 0.0000 0.0000 0.0000 210 LEU B C   
5505 O O   . LEU B 210 ? 198.6734 198.6734 198.6734 0.0000 0.0000 0.0000 210 LEU B O   
5506 C CB  . LEU B 210 ? 198.0525 198.0525 198.0525 0.0000 0.0000 0.0000 210 LEU B CB  
5507 C CG  . LEU B 210 ? 197.9997 197.9997 197.9997 0.0000 0.0000 0.0000 210 LEU B CG  
5508 C CD1 . LEU B 210 ? 197.1498 197.1498 197.1498 0.0000 0.0000 0.0000 210 LEU B CD1 
5509 C CD2 . LEU B 210 ? 196.7647 196.7647 196.7647 0.0000 0.0000 0.0000 210 LEU B CD2 
5510 N N   . HIS B 211 ? 251.8333 251.8333 251.8333 0.0000 0.0000 0.0000 211 HIS B N   
5511 C CA  . HIS B 211 ? 252.9306 252.9306 252.9306 0.0000 0.0000 0.0000 211 HIS B CA  
5512 C C   . HIS B 211 ? 253.2739 253.2739 253.2739 0.0000 0.0000 0.0000 211 HIS B C   
5513 O O   . HIS B 211 ? 253.4387 253.4387 253.4387 0.0000 0.0000 0.0000 211 HIS B O   
5514 C CB  . HIS B 211 ? 253.6019 253.6019 253.6019 0.0000 0.0000 0.0000 211 HIS B CB  
5515 C CG  . HIS B 211 ? 253.7034 253.7034 253.7034 0.0000 0.0000 0.0000 211 HIS B CG  
5516 N ND1 . HIS B 211 ? 253.6305 253.6305 253.6305 0.0000 0.0000 0.0000 211 HIS B ND1 
5517 C CD2 . HIS B 211 ? 253.8713 253.8713 253.8713 0.0000 0.0000 0.0000 211 HIS B CD2 
5518 C CE1 . HIS B 211 ? 253.6287 253.6287 253.6287 0.0000 0.0000 0.0000 211 HIS B CE1 
5519 N NE2 . HIS B 211 ? 253.7390 253.7390 253.7390 0.0000 0.0000 0.0000 211 HIS B NE2 
5520 N N   . MET B 212 ? 252.2145 252.2145 252.2145 0.0000 0.0000 0.0000 212 MET B N   
5521 C CA  . MET B 212 ? 252.4546 252.4546 252.4546 0.0000 0.0000 0.0000 212 MET B CA  
5522 C C   . MET B 212 ? 252.9399 252.9399 252.9399 0.0000 0.0000 0.0000 212 MET B C   
5523 O O   . MET B 212 ? 252.6384 252.6384 252.6384 0.0000 0.0000 0.0000 212 MET B O   
5524 C CB  . MET B 212 ? 252.4731 252.4731 252.4731 0.0000 0.0000 0.0000 212 MET B CB  
5525 C CG  . MET B 212 ? 251.6912 251.6912 251.6912 0.0000 0.0000 0.0000 212 MET B CG  
5526 S SD  . MET B 212 ? 250.9379 250.9379 250.9379 0.0000 0.0000 0.0000 212 MET B SD  
5527 C CE  . MET B 212 ? 251.3456 251.3456 251.3456 0.0000 0.0000 0.0000 212 MET B CE  
5528 N N   . LEU B 213 ? 275.5223 275.5223 275.5223 0.0000 0.0000 0.0000 213 LEU B N   
5529 C CA  . LEU B 213 ? 275.8851 275.8851 275.8851 0.0000 0.0000 0.0000 213 LEU B CA  
5530 C C   . LEU B 213 ? 275.8868 275.8868 275.8868 0.0000 0.0000 0.0000 213 LEU B C   
5531 O O   . LEU B 213 ? 276.0842 276.0842 276.0842 0.0000 0.0000 0.0000 213 LEU B O   
5532 C CB  . LEU B 213 ? 276.1097 276.1097 276.1097 0.0000 0.0000 0.0000 213 LEU B CB  
5533 C CG  . LEU B 213 ? 276.1306 276.1306 276.1306 0.0000 0.0000 0.0000 213 LEU B CG  
5534 C CD1 . LEU B 213 ? 276.0721 276.0721 276.0721 0.0000 0.0000 0.0000 213 LEU B CD1 
5535 C CD2 . LEU B 213 ? 276.2473 276.2473 276.2473 0.0000 0.0000 0.0000 213 LEU B CD2 
5536 N N   . PRO B 214 ? 276.1981 276.1981 276.1981 0.0000 0.0000 0.0000 214 PRO B N   
5537 C CA  . PRO B 214 ? 276.2833 276.2833 276.2833 0.0000 0.0000 0.0000 214 PRO B CA  
5538 C C   . PRO B 214 ? 271.1714 271.1714 271.1714 0.0000 0.0000 0.0000 214 PRO B C   
5539 O O   . PRO B 214 ? 271.1246 271.1246 271.1246 0.0000 0.0000 0.0000 214 PRO B O   
5540 C CB  . PRO B 214 ? 270.5922 270.5922 270.5922 0.0000 0.0000 0.0000 214 PRO B CB  
5541 C CG  . PRO B 214 ? 270.4804 270.4804 270.4804 0.0000 0.0000 0.0000 214 PRO B CG  
5542 C CD  . PRO B 214 ? 271.2315 271.2315 271.2315 0.0000 0.0000 0.0000 214 PRO B CD  
5543 N N   . HIS B 215 ? 271.3829 271.3829 271.3829 0.0000 0.0000 0.0000 215 HIS B N   
5544 C CA  . HIS B 215 ? 271.4593 271.4593 271.4593 0.0000 0.0000 0.0000 215 HIS B CA  
5545 C C   . HIS B 215 ? 271.3344 271.3344 271.3344 0.0000 0.0000 0.0000 215 HIS B C   
5546 O O   . HIS B 215 ? 271.4681 271.4681 271.4681 0.0000 0.0000 0.0000 215 HIS B O   
5547 C CB  . HIS B 215 ? 271.3529 271.3529 271.3529 0.0000 0.0000 0.0000 215 HIS B CB  
5548 C CG  . HIS B 215 ? 271.4383 271.4383 271.4383 0.0000 0.0000 0.0000 215 HIS B CG  
5549 N ND1 . HIS B 215 ? 243.2959 243.2959 243.2959 0.0000 0.0000 0.0000 215 HIS B ND1 
5550 C CD2 . HIS B 215 ? 242.2384 242.2384 242.2384 0.0000 0.0000 0.0000 215 HIS B CD2 
5551 C CE1 . HIS B 215 ? 241.2739 241.2739 241.2739 0.0000 0.0000 0.0000 215 HIS B CE1 
5552 N NE2 . HIS B 215 ? 241.6865 241.6865 241.6865 0.0000 0.0000 0.0000 215 HIS B NE2 
5553 N N   . LEU B 216 ? 194.6769 194.6769 194.6769 0.0000 0.0000 0.0000 216 LEU B N   
5554 C CA  . LEU B 216 ? 194.0279 194.0279 194.0279 0.0000 0.0000 0.0000 216 LEU B CA  
5555 C C   . LEU B 216 ? 194.0941 194.0941 194.0941 0.0000 0.0000 0.0000 216 LEU B C   
5556 O O   . LEU B 216 ? 193.7945 193.7945 193.7945 0.0000 0.0000 0.0000 216 LEU B O   
5557 C CB  . LEU B 216 ? 193.2506 193.2506 193.2506 0.0000 0.0000 0.0000 216 LEU B CB  
5558 C CG  . LEU B 216 ? 193.1193 193.1193 193.1193 0.0000 0.0000 0.0000 216 LEU B CG  
5559 C CD1 . LEU B 216 ? 192.5121 192.5121 192.5121 0.0000 0.0000 0.0000 216 LEU B CD1 
5560 C CD2 . LEU B 216 ? 193.5606 193.5606 193.5606 0.0000 0.0000 0.0000 216 LEU B CD2 
5561 N N   . HIS B 217 ? 209.2585 209.2585 209.2585 0.0000 0.0000 0.0000 217 HIS B N   
5562 C CA  . HIS B 217 ? 209.4291 209.4291 209.4291 0.0000 0.0000 0.0000 217 HIS B CA  
5563 C C   . HIS B 217 ? 209.2440 209.2440 209.2440 0.0000 0.0000 0.0000 217 HIS B C   
5564 O O   . HIS B 217 ? 209.4165 209.4165 209.4165 0.0000 0.0000 0.0000 217 HIS B O   
5565 C CB  . HIS B 217 ? 209.7465 209.7465 209.7465 0.0000 0.0000 0.0000 217 HIS B CB  
5566 C CG  . HIS B 217 ? 209.8569 209.8569 209.8569 0.0000 0.0000 0.0000 217 HIS B CG  
5567 N ND1 . HIS B 217 ? 209.8966 209.8966 209.8966 0.0000 0.0000 0.0000 217 HIS B ND1 
5568 C CD2 . HIS B 217 ? 209.9420 209.9420 209.9420 0.0000 0.0000 0.0000 217 HIS B CD2 
5569 C CE1 . HIS B 217 ? 209.9553 209.9553 209.9553 0.0000 0.0000 0.0000 217 HIS B CE1 
5570 N NE2 . HIS B 217 ? 200.7116 200.7116 200.7116 0.0000 0.0000 0.0000 217 HIS B NE2 
5571 N N   . PHE B 218 ? 200.5548 200.5548 200.5548 0.0000 0.0000 0.0000 218 PHE B N   
5572 C CA  . PHE B 218 ? 199.9612 199.9612 199.9612 0.0000 0.0000 0.0000 218 PHE B CA  
5573 C C   . PHE B 218 ? 199.7283 199.7283 199.7283 0.0000 0.0000 0.0000 218 PHE B C   
5574 O O   . PHE B 218 ? 200.4916 200.4916 200.4916 0.0000 0.0000 0.0000 218 PHE B O   
5575 C CB  . PHE B 218 ? 200.4837 200.4837 200.4837 0.0000 0.0000 0.0000 218 PHE B CB  
5576 C CG  . PHE B 218 ? 200.5333 200.5333 200.5333 0.0000 0.0000 0.0000 218 PHE B CG  
5577 C CD1 . PHE B 218 ? 200.5621 200.5621 200.5621 0.0000 0.0000 0.0000 218 PHE B CD1 
5578 C CD2 . PHE B 218 ? 190.3596 190.3596 190.3596 0.0000 0.0000 0.0000 218 PHE B CD2 
5579 C CE1 . PHE B 218 ? 189.9823 189.9823 189.9823 0.0000 0.0000 0.0000 218 PHE B CE1 
5580 C CE2 . PHE B 218 ? 189.7407 189.7407 189.7407 0.0000 0.0000 0.0000 218 PHE B CE2 
5581 C CZ  . PHE B 218 ? 189.2814 189.2814 189.2814 0.0000 0.0000 0.0000 218 PHE B CZ  
5582 N N   . GLY B 219 ? 189.8857 189.8857 189.8857 0.0000 0.0000 0.0000 219 GLY B N   
5583 C CA  . GLY B 219 ? 189.8785 189.8785 189.8785 0.0000 0.0000 0.0000 219 GLY B CA  
5584 C C   . GLY B 219 ? 189.4663 189.4663 189.4663 0.0000 0.0000 0.0000 219 GLY B C   
5585 O O   . GLY B 219 ? 189.1906 189.1906 189.1906 0.0000 0.0000 0.0000 219 GLY B O   
5586 N N   . LEU B 220 ? 190.0393 190.0393 190.0393 0.0000 0.0000 0.0000 220 LEU B N   
5587 C CA  . LEU B 220 ? 198.1875 198.1875 198.1875 0.0000 0.0000 0.0000 220 LEU B CA  
5588 C C   . LEU B 220 ? 197.9698 197.9698 197.9698 0.0000 0.0000 0.0000 220 LEU B C   
5589 O O   . LEU B 220 ? 197.6034 197.6034 197.6034 0.0000 0.0000 0.0000 220 LEU B O   
5590 C CB  . LEU B 220 ? 197.2996 197.2996 197.2996 0.0000 0.0000 0.0000 220 LEU B CB  
5591 C CG  . LEU B 220 ? 198.4534 198.4534 198.4534 0.0000 0.0000 0.0000 220 LEU B CG  
5592 C CD1 . LEU B 220 ? 197.9188 197.9188 197.9188 0.0000 0.0000 0.0000 220 LEU B CD1 
5593 C CD2 . LEU B 220 ? 198.2561 198.2561 198.2561 0.0000 0.0000 0.0000 220 LEU B CD2 
5594 N N   . LYS B 221 ? 198.5423 198.5423 198.5423 0.0000 0.0000 0.0000 221 LYS B N   
5595 C CA  . LYS B 221 ? 197.4169 197.4169 197.4169 0.0000 0.0000 0.0000 221 LYS B CA  
5596 C C   . LYS B 221 ? 180.0402 180.0402 180.0402 0.0000 0.0000 0.0000 221 LYS B C   
5597 O O   . LYS B 221 ? 179.3919 179.3919 179.3919 0.0000 0.0000 0.0000 221 LYS B O   
5598 C CB  . LYS B 221 ? 178.7843 178.7843 178.7843 0.0000 0.0000 0.0000 221 LYS B CB  
5599 C CG  . LYS B 221 ? 178.6856 178.6856 178.6856 0.0000 0.0000 0.0000 221 LYS B CG  
5600 C CD  . LYS B 221 ? 179.4319 179.4319 179.4319 0.0000 0.0000 0.0000 221 LYS B CD  
5601 C CE  . LYS B 221 ? 179.7464 179.7464 179.7464 0.0000 0.0000 0.0000 221 LYS B CE  
5602 N NZ  . LYS B 221 ? 179.1850 179.1850 179.1850 0.0000 0.0000 0.0000 221 LYS B NZ  
5603 N N   . ASP B 222 ? 168.0477 168.0477 168.0477 0.0000 0.0000 0.0000 222 ASP B N   
5604 C CA  . ASP B 222 ? 167.4067 167.4067 167.4067 0.0000 0.0000 0.0000 222 ASP B CA  
5605 C C   . ASP B 222 ? 167.2791 167.2791 167.2791 0.0000 0.0000 0.0000 222 ASP B C   
5606 O O   . ASP B 222 ? 167.1232 167.1232 167.1232 0.0000 0.0000 0.0000 222 ASP B O   
5607 C CB  . ASP B 222 ? 167.4106 167.4106 167.4106 0.0000 0.0000 0.0000 222 ASP B CB  
5608 C CG  . ASP B 222 ? 168.0764 168.0764 168.0764 0.0000 0.0000 0.0000 222 ASP B CG  
5609 O OD1 . ASP B 222 ? 167.8627 167.8627 167.8627 0.0000 0.0000 0.0000 222 ASP B OD1 
5610 O OD2 . ASP B 222 ? 166.8761 166.8761 166.8761 0.0000 0.0000 0.0000 222 ASP B OD2 
5611 N N   . LYS B 223 ? 166.3399 166.3399 166.3399 0.0000 0.0000 0.0000 223 LYS B N   
5612 C CA  . LYS B 223 ? 166.5148 166.5148 166.5148 0.0000 0.0000 0.0000 223 LYS B CA  
5613 C C   . LYS B 223 ? 165.8656 165.8656 165.8656 0.0000 0.0000 0.0000 223 LYS B C   
5614 O O   . LYS B 223 ? 163.3503 163.3503 163.3503 0.0000 0.0000 0.0000 223 LYS B O   
5615 C CB  . LYS B 223 ? 162.3245 162.3245 162.3245 0.0000 0.0000 0.0000 223 LYS B CB  
5616 C CG  . LYS B 223 ? 162.6961 162.6961 162.6961 0.0000 0.0000 0.0000 223 LYS B CG  
5617 C CD  . LYS B 223 ? 161.6211 161.6211 161.6211 0.0000 0.0000 0.0000 223 LYS B CD  
5618 C CE  . LYS B 223 ? 161.4878 161.4878 161.4878 0.0000 0.0000 0.0000 223 LYS B CE  
5619 N NZ  . LYS B 223 ? 160.8831 160.8831 160.8831 0.0000 0.0000 0.0000 223 LYS B NZ  
5620 N N   . GLU B 224 ? 161.0442 161.0442 161.0442 0.0000 0.0000 0.0000 224 GLU B N   
5621 C CA  . GLU B 224 ? 161.0457 161.0457 161.0457 0.0000 0.0000 0.0000 224 GLU B CA  
5622 C C   . GLU B 224 ? 160.0422 160.0422 160.0422 0.0000 0.0000 0.0000 224 GLU B C   
5623 O O   . GLU B 224 ? 161.0437 161.0437 161.0437 0.0000 0.0000 0.0000 224 GLU B O   
5624 C CB  . GLU B 224 ? 159.4942 159.4942 159.4942 0.0000 0.0000 0.0000 224 GLU B CB  
5625 C CG  . GLU B 224 ? 159.1662 159.1662 159.1662 0.0000 0.0000 0.0000 224 GLU B CG  
5626 C CD  . GLU B 224 ? 179.7311 179.7311 179.7311 0.0000 0.0000 0.0000 224 GLU B CD  
5627 O OE1 . GLU B 224 ? 180.1249 180.1249 180.1249 0.0000 0.0000 0.0000 224 GLU B OE1 
5628 O OE2 . GLU B 224 ? 179.8428 179.8428 179.8428 0.0000 0.0000 0.0000 224 GLU B OE2 
5629 N N   . THR B 225 ? 180.2015 180.2015 180.2015 0.0000 0.0000 0.0000 225 THR B N   
5630 C CA  . THR B 225 ? 180.5681 180.5681 180.5681 0.0000 0.0000 0.0000 225 THR B CA  
5631 C C   . THR B 225 ? 180.2728 180.2728 180.2728 0.0000 0.0000 0.0000 225 THR B C   
5632 O O   . THR B 225 ? 180.7989 180.7989 180.7989 0.0000 0.0000 0.0000 225 THR B O   
5633 C CB  . THR B 225 ? 179.7726 179.7726 179.7726 0.0000 0.0000 0.0000 225 THR B CB  
5634 O OG1 . THR B 225 ? 178.6843 178.6843 178.6843 0.0000 0.0000 0.0000 225 THR B OG1 
5635 C CG2 . THR B 225 ? 178.7704 178.7704 178.7704 0.0000 0.0000 0.0000 225 THR B CG2 
5636 N N   . ARG B 226 ? 177.1410 177.1410 177.1410 0.0000 0.0000 0.0000 226 ARG B N   
5637 C CA  . ARG B 226 ? 162.4112 162.4112 162.4112 0.0000 0.0000 0.0000 226 ARG B CA  
5638 C C   . ARG B 226 ? 161.7816 161.7816 161.7816 0.0000 0.0000 0.0000 226 ARG B C   
5639 O O   . ARG B 226 ? 161.7265 161.7265 161.7265 0.0000 0.0000 0.0000 226 ARG B O   
5640 C CB  . ARG B 226 ? 161.8494 161.8494 161.8494 0.0000 0.0000 0.0000 226 ARG B CB  
5641 C CG  . ARG B 226 ? 161.5163 161.5163 161.5163 0.0000 0.0000 0.0000 226 ARG B CG  
5642 C CD  . ARG B 226 ? 161.5576 161.5576 161.5576 0.0000 0.0000 0.0000 226 ARG B CD  
5643 N NE  . ARG B 226 ? 161.5380 161.5380 161.5380 0.0000 0.0000 0.0000 226 ARG B NE  
5644 C CZ  . ARG B 226 ? 161.6154 161.6154 161.6154 0.0000 0.0000 0.0000 226 ARG B CZ  
5645 N NH1 . ARG B 226 ? 161.6447 161.6447 161.6447 0.0000 0.0000 0.0000 226 ARG B NH1 
5646 N NH2 . ARG B 226 ? 161.6082 161.6082 161.6082 0.0000 0.0000 0.0000 226 ARG B NH2 
5647 N N   . TYR B 227 ? 161.3791 161.3791 161.3791 0.0000 0.0000 0.0000 227 TYR B N   
5648 C CA  . TYR B 227 ? 161.3568 161.3568 161.3568 0.0000 0.0000 0.0000 227 TYR B CA  
5649 C C   . TYR B 227 ? 161.5088 161.5088 161.5088 0.0000 0.0000 0.0000 227 TYR B C   
5650 O O   . TYR B 227 ? 160.0179 160.0179 160.0179 0.0000 0.0000 0.0000 227 TYR B O   
5651 C CB  . TYR B 227 ? 159.8770 159.8770 159.8770 0.0000 0.0000 0.0000 227 TYR B CB  
5652 C CG  . TYR B 227 ? 160.7728 160.7728 160.7728 0.0000 0.0000 0.0000 227 TYR B CG  
5653 C CD1 . TYR B 227 ? 159.2949 159.2949 159.2949 0.0000 0.0000 0.0000 227 TYR B CD1 
5654 C CD2 . TYR B 227 ? 159.3468 159.3468 159.3468 0.0000 0.0000 0.0000 227 TYR B CD2 
5655 C CE1 . TYR B 227 ? 160.8802 160.8802 160.8802 0.0000 0.0000 0.0000 227 TYR B CE1 
5656 C CE2 . TYR B 227 ? 156.5804 156.5804 156.5804 0.0000 0.0000 0.0000 227 TYR B CE2 
5657 C CZ  . TYR B 227 ? 161.2689 161.2689 161.2689 0.0000 0.0000 0.0000 227 TYR B CZ  
5658 O OH  . TYR B 227 ? 161.3045 161.3045 161.3045 0.0000 0.0000 0.0000 227 TYR B OH  
5659 N N   . ARG B 228 ? 161.5048 161.5048 161.5048 0.0000 0.0000 0.0000 228 ARG B N   
5660 C CA  . ARG B 228 ? 161.8825 161.8825 161.8825 0.0000 0.0000 0.0000 228 ARG B CA  
5661 C C   . ARG B 228 ? 161.2720 161.2720 161.2720 0.0000 0.0000 0.0000 228 ARG B C   
5662 O O   . ARG B 228 ? 161.2214 161.2214 161.2214 0.0000 0.0000 0.0000 228 ARG B O   
5663 C CB  . ARG B 228 ? 161.3769 161.3769 161.3769 0.0000 0.0000 0.0000 228 ARG B CB  
5664 C CG  . ARG B 228 ? 161.4597 161.4597 161.4597 0.0000 0.0000 0.0000 228 ARG B CG  
5665 C CD  . ARG B 228 ? 161.5432 161.5432 161.5432 0.0000 0.0000 0.0000 228 ARG B CD  
5666 N NE  . ARG B 228 ? 161.5237 161.5237 161.5237 0.0000 0.0000 0.0000 228 ARG B NE  
5667 C CZ  . ARG B 228 ? 161.4714 161.4714 161.4714 0.0000 0.0000 0.0000 228 ARG B CZ  
5668 N NH1 . ARG B 228 ? 161.6459 161.6459 161.6459 0.0000 0.0000 0.0000 228 ARG B NH1 
5669 N NH2 . ARG B 228 ? 161.3990 161.3990 161.3990 0.0000 0.0000 0.0000 228 ARG B NH2 
5670 N N   . GLN B 229 ? 161.3709 161.3709 161.3709 0.0000 0.0000 0.0000 229 GLN B N   
5671 C CA  . GLN B 229 ? 161.4643 161.4643 161.4643 0.0000 0.0000 0.0000 229 GLN B CA  
5672 C C   . GLN B 229 ? 161.7689 161.7689 161.7689 0.0000 0.0000 0.0000 229 GLN B C   
5673 O O   . GLN B 229 ? 161.3988 161.3988 161.3988 0.0000 0.0000 0.0000 229 GLN B O   
5674 C CB  . GLN B 229 ? 161.4379 161.4379 161.4379 0.0000 0.0000 0.0000 229 GLN B CB  
5675 C CG  . GLN B 229 ? 161.6053 161.6053 161.6053 0.0000 0.0000 0.0000 229 GLN B CG  
5676 C CD  . GLN B 229 ? 161.6405 161.6405 161.6405 0.0000 0.0000 0.0000 229 GLN B CD  
5677 O OE1 . GLN B 229 ? 161.3695 161.3695 161.3695 0.0000 0.0000 0.0000 229 GLN B OE1 
5678 N NE2 . GLN B 229 ? 161.4636 161.4636 161.4636 0.0000 0.0000 0.0000 229 GLN B NE2 
5679 N N   . ARG B 230 ? 161.5303 161.5303 161.5303 0.0000 0.0000 0.0000 230 ARG B N   
5680 C CA  . ARG B 230 ? 161.6555 161.6555 161.6555 0.0000 0.0000 0.0000 230 ARG B CA  
5681 C C   . ARG B 230 ? 161.6313 161.6313 161.6313 0.0000 0.0000 0.0000 230 ARG B C   
5682 O O   . ARG B 230 ? 161.7867 161.7867 161.7867 0.0000 0.0000 0.0000 230 ARG B O   
5683 C CB  . ARG B 230 ? 161.9848 161.9848 161.9848 0.0000 0.0000 0.0000 230 ARG B CB  
5684 C CG  . ARG B 230 ? 161.9047 161.9047 161.9047 0.0000 0.0000 0.0000 230 ARG B CG  
5685 C CD  . ARG B 230 ? 161.5044 161.5044 161.5044 0.0000 0.0000 0.0000 230 ARG B CD  
5686 N NE  . ARG B 230 ? 161.4213 161.4213 161.4213 0.0000 0.0000 0.0000 230 ARG B NE  
5687 C CZ  . ARG B 230 ? 161.5700 161.5700 161.5700 0.0000 0.0000 0.0000 230 ARG B CZ  
5688 N NH1 . ARG B 230 ? 161.7995 161.7995 161.7995 0.0000 0.0000 0.0000 230 ARG B NH1 
5689 N NH2 . ARG B 230 ? 161.3288 161.3288 161.3288 0.0000 0.0000 0.0000 230 ARG B NH2 
5690 N N   . TYR B 231 ? 161.3215 161.3215 161.3215 0.0000 0.0000 0.0000 231 TYR B N   
5691 C CA  . TYR B 231 ? 161.5118 161.5118 161.5118 0.0000 0.0000 0.0000 231 TYR B CA  
5692 C C   . TYR B 231 ? 161.4188 161.4188 161.4188 0.0000 0.0000 0.0000 231 TYR B C   
5693 O O   . TYR B 231 ? 161.5122 161.5122 161.5122 0.0000 0.0000 0.0000 231 TYR B O   
5694 C CB  . TYR B 231 ? 161.2348 161.2348 161.2348 0.0000 0.0000 0.0000 231 TYR B CB  
5695 C CG  . TYR B 231 ? 161.3653 161.3653 161.3653 0.0000 0.0000 0.0000 231 TYR B CG  
5696 C CD1 . TYR B 231 ? 161.4971 161.4971 161.4971 0.0000 0.0000 0.0000 231 TYR B CD1 
5697 C CD2 . TYR B 231 ? 161.1234 161.1234 161.1234 0.0000 0.0000 0.0000 231 TYR B CD2 
5698 C CE1 . TYR B 231 ? 161.2137 161.2137 161.2137 0.0000 0.0000 0.0000 231 TYR B CE1 
5699 C CE2 . TYR B 231 ? 161.4358 161.4358 161.4358 0.0000 0.0000 0.0000 231 TYR B CE2 
5700 C CZ  . TYR B 231 ? 161.4440 161.4440 161.4440 0.0000 0.0000 0.0000 231 TYR B CZ  
5701 O OH  . TYR B 231 ? 161.3570 161.3570 161.3570 0.0000 0.0000 0.0000 231 TYR B OH  
5702 N N   . LEU B 232 ? 161.2510 161.2510 161.2510 0.0000 0.0000 0.0000 232 LEU B N   
5703 C CA  . LEU B 232 ? 161.6093 161.6093 161.6093 0.0000 0.0000 0.0000 232 LEU B CA  
5704 C C   . LEU B 232 ? 161.5522 161.5522 161.5522 0.0000 0.0000 0.0000 232 LEU B C   
5705 O O   . LEU B 232 ? 161.4115 161.4115 161.4115 0.0000 0.0000 0.0000 232 LEU B O   
5706 C CB  . LEU B 232 ? 161.5023 161.5023 161.5023 0.0000 0.0000 0.0000 232 LEU B CB  
5707 C CG  . LEU B 232 ? 162.0793 162.0793 162.0793 0.0000 0.0000 0.0000 232 LEU B CG  
5708 C CD1 . LEU B 232 ? 161.9273 161.9273 161.9273 0.0000 0.0000 0.0000 232 LEU B CD1 
5709 C CD2 . LEU B 232 ? 166.3977 166.3977 166.3977 0.0000 0.0000 0.0000 232 LEU B CD2 
5710 N N   . ASP B 233 ? 166.7410 166.7410 166.7410 0.0000 0.0000 0.0000 233 ASP B N   
5711 C CA  . ASP B 233 ? 167.0940 167.0940 167.0940 0.0000 0.0000 0.0000 233 ASP B CA  
5712 C C   . ASP B 233 ? 166.8182 166.8182 166.8182 0.0000 0.0000 0.0000 233 ASP B C   
5713 O O   . ASP B 233 ? 166.6962 166.6962 166.6962 0.0000 0.0000 0.0000 233 ASP B O   
5714 C CB  . ASP B 233 ? 166.7641 166.7641 166.7641 0.0000 0.0000 0.0000 233 ASP B CB  
5715 C CG  . ASP B 233 ? 166.8062 166.8062 166.8062 0.0000 0.0000 0.0000 233 ASP B CG  
5716 O OD1 . ASP B 233 ? 167.0019 167.0019 167.0019 0.0000 0.0000 0.0000 233 ASP B OD1 
5717 O OD2 . ASP B 233 ? 184.1818 184.1818 184.1818 0.0000 0.0000 0.0000 233 ASP B OD2 
5718 N N   . LEU B 234 ? 184.7046 184.7046 184.7046 0.0000 0.0000 0.0000 234 LEU B N   
5719 C CA  . LEU B 234 ? 184.2027 184.2027 184.2027 0.0000 0.0000 0.0000 234 LEU B CA  
5720 C C   . LEU B 234 ? 184.1977 184.1977 184.1977 0.0000 0.0000 0.0000 234 LEU B C   
5721 O O   . LEU B 234 ? 185.0072 185.0072 185.0072 0.0000 0.0000 0.0000 234 LEU B O   
5722 C CB  . LEU B 234 ? 184.9861 184.9861 184.9861 0.0000 0.0000 0.0000 234 LEU B CB  
5723 C CG  . LEU B 234 ? 184.8408 184.8408 184.8408 0.0000 0.0000 0.0000 234 LEU B CG  
5724 C CD1 . LEU B 234 ? 185.1561 185.1561 185.1561 0.0000 0.0000 0.0000 234 LEU B CD1 
5725 C CD2 . LEU B 234 ? 167.9039 167.9039 167.9039 0.0000 0.0000 0.0000 234 LEU B CD2 
5726 N N   . ILE B 235 ? 167.4486 167.4486 167.4486 0.0000 0.0000 0.0000 235 ILE B N   
5727 C CA  . ILE B 235 ? 167.0560 167.0560 167.0560 0.0000 0.0000 0.0000 235 ILE B CA  
5728 C C   . ILE B 235 ? 167.1695 167.1695 167.1695 0.0000 0.0000 0.0000 235 ILE B C   
5729 O O   . ILE B 235 ? 167.2960 167.2960 167.2960 0.0000 0.0000 0.0000 235 ILE B O   
5730 C CB  . ILE B 235 ? 166.9680 166.9680 166.9680 0.0000 0.0000 0.0000 235 ILE B CB  
5731 C CG1 . ILE B 235 ? 166.8875 166.8875 166.8875 0.0000 0.0000 0.0000 235 ILE B CG1 
5732 C CG2 . ILE B 235 ? 167.1465 167.1465 167.1465 0.0000 0.0000 0.0000 235 ILE B CG2 
5733 C CD1 . ILE B 235 ? 167.1230 167.1230 167.1230 0.0000 0.0000 0.0000 235 ILE B CD1 
5734 N N   . LEU B 236 ? 167.1790 167.1790 167.1790 0.0000 0.0000 0.0000 236 LEU B N   
5735 C CA  . LEU B 236 ? 167.2127 167.2127 167.2127 0.0000 0.0000 0.0000 236 LEU B CA  
5736 C C   . LEU B 236 ? 161.8573 161.8573 161.8573 0.0000 0.0000 0.0000 236 LEU B C   
5737 O O   . LEU B 236 ? 161.7228 161.7228 161.7228 0.0000 0.0000 0.0000 236 LEU B O   
5738 C CB  . LEU B 236 ? 161.5267 161.5267 161.5267 0.0000 0.0000 0.0000 236 LEU B CB  
5739 C CG  . LEU B 236 ? 161.6384 161.6384 161.6384 0.0000 0.0000 0.0000 236 LEU B CG  
5740 C CD1 . LEU B 236 ? 161.5546 161.5546 161.5546 0.0000 0.0000 0.0000 236 LEU B CD1 
5741 C CD2 . LEU B 236 ? 161.5357 161.5357 161.5357 0.0000 0.0000 0.0000 236 LEU B CD2 
5742 N N   . ASN B 237 ? 161.7552 161.7552 161.7552 0.0000 0.0000 0.0000 237 ASN B N   
5743 C CA  . ASN B 237 ? 161.2815 161.2815 161.2815 0.0000 0.0000 0.0000 237 ASN B CA  
5744 C C   . ASN B 237 ? 161.3562 161.3562 161.3562 0.0000 0.0000 0.0000 237 ASN B C   
5745 O O   . ASN B 237 ? 161.5374 161.5374 161.5374 0.0000 0.0000 0.0000 237 ASN B O   
5746 C CB  . ASN B 237 ? 161.8330 161.8330 161.8330 0.0000 0.0000 0.0000 237 ASN B CB  
5747 C CG  . ASN B 237 ? 161.5770 161.5770 161.5770 0.0000 0.0000 0.0000 237 ASN B CG  
5748 O OD1 . ASN B 237 ? 161.4947 161.4947 161.4947 0.0000 0.0000 0.0000 237 ASN B OD1 
5749 N ND2 . ASN B 237 ? 161.4254 161.4254 161.4254 0.0000 0.0000 0.0000 237 ASN B ND2 
5750 N N   . ASP B 238 ? 161.4701 161.4701 161.4701 0.0000 0.0000 0.0000 238 ASP B N   
5751 C CA  . ASP B 238 ? 161.6179 161.6179 161.6179 0.0000 0.0000 0.0000 238 ASP B CA  
5752 C C   . ASP B 238 ? 161.4322 161.4322 161.4322 0.0000 0.0000 0.0000 238 ASP B C   
5753 O O   . ASP B 238 ? 161.6304 161.6304 161.6304 0.0000 0.0000 0.0000 238 ASP B O   
5754 C CB  . ASP B 238 ? 161.4616 161.4616 161.4616 0.0000 0.0000 0.0000 238 ASP B CB  
5755 C CG  . ASP B 238 ? 161.4015 161.4015 161.4015 0.0000 0.0000 0.0000 238 ASP B CG  
5756 O OD1 . ASP B 238 ? 161.4196 161.4196 161.4196 0.0000 0.0000 0.0000 238 ASP B OD1 
5757 O OD2 . ASP B 238 ? 161.6243 161.6243 161.6243 0.0000 0.0000 0.0000 238 ASP B OD2 
5758 N N   . PHE B 239 ? 161.4708 161.4708 161.4708 0.0000 0.0000 0.0000 239 PHE B N   
5759 C CA  . PHE B 239 ? 161.5270 161.5270 161.5270 0.0000 0.0000 0.0000 239 PHE B CA  
5760 C C   . PHE B 239 ? 161.4200 161.4200 161.4200 0.0000 0.0000 0.0000 239 PHE B C   
5761 O O   . PHE B 239 ? 161.5330 161.5330 161.5330 0.0000 0.0000 0.0000 239 PHE B O   
5762 C CB  . PHE B 239 ? 161.4218 161.4218 161.4218 0.0000 0.0000 0.0000 239 PHE B CB  
5763 C CG  . PHE B 239 ? 161.3145 161.3145 161.3145 0.0000 0.0000 0.0000 239 PHE B CG  
5764 C CD1 . PHE B 239 ? 160.7623 160.7623 160.7623 0.0000 0.0000 0.0000 239 PHE B CD1 
5765 C CD2 . PHE B 239 ? 161.1431 161.1431 161.1431 0.0000 0.0000 0.0000 239 PHE B CD2 
5766 C CE1 . PHE B 239 ? 161.3571 161.3571 161.3571 0.0000 0.0000 0.0000 239 PHE B CE1 
5767 C CE2 . PHE B 239 ? 160.4347 160.4347 160.4347 0.0000 0.0000 0.0000 239 PHE B CE2 
5768 C CZ  . PHE B 239 ? 160.4183 160.4183 160.4183 0.0000 0.0000 0.0000 239 PHE B CZ  
5769 N N   . VAL B 240 ? 159.6001 159.6001 159.6001 0.0000 0.0000 0.0000 240 VAL B N   
5770 C CA  . VAL B 240 ? 159.8313 159.8313 159.8313 0.0000 0.0000 0.0000 240 VAL B CA  
5771 C C   . VAL B 240 ? 158.6196 158.6196 158.6196 0.0000 0.0000 0.0000 240 VAL B C   
5772 O O   . VAL B 240 ? 161.2785 161.2785 161.2785 0.0000 0.0000 0.0000 240 VAL B O   
5773 C CB  . VAL B 240 ? 161.2770 161.2770 161.2770 0.0000 0.0000 0.0000 240 VAL B CB  
5774 C CG1 . VAL B 240 ? 161.2505 161.2505 161.2505 0.0000 0.0000 0.0000 240 VAL B CG1 
5775 C CG2 . VAL B 240 ? 161.4953 161.4953 161.4953 0.0000 0.0000 0.0000 240 VAL B CG2 
5776 N N   . ARG B 241 ? 161.1633 161.1633 161.1633 0.0000 0.0000 0.0000 241 ARG B N   
5777 C CA  . ARG B 241 ? 160.8839 160.8839 160.8839 0.0000 0.0000 0.0000 241 ARG B CA  
5778 C C   . ARG B 241 ? 159.4004 159.4004 159.4004 0.0000 0.0000 0.0000 241 ARG B C   
5779 O O   . ARG B 241 ? 160.8789 160.8789 160.8789 0.0000 0.0000 0.0000 241 ARG B O   
5780 C CB  . ARG B 241 ? 157.3835 157.3835 157.3835 0.0000 0.0000 0.0000 241 ARG B CB  
5781 C CG  . ARG B 241 ? 159.7470 159.7470 159.7470 0.0000 0.0000 0.0000 241 ARG B CG  
5782 C CD  . ARG B 241 ? 157.1797 157.1797 157.1797 0.0000 0.0000 0.0000 241 ARG B CD  
5783 N NE  . ARG B 241 ? 161.2510 161.2510 161.2510 0.0000 0.0000 0.0000 241 ARG B NE  
5784 C CZ  . ARG B 241 ? 161.2967 161.2967 161.2967 0.0000 0.0000 0.0000 241 ARG B CZ  
5785 N NH1 . ARG B 241 ? 161.4246 161.4246 161.4246 0.0000 0.0000 0.0000 241 ARG B NH1 
5786 N NH2 . ARG B 241 ? 161.6267 161.6267 161.6267 0.0000 0.0000 0.0000 241 ARG B NH2 
5787 N N   . GLN B 242 ? 161.1421 161.1421 161.1421 0.0000 0.0000 0.0000 242 GLN B N   
5788 C CA  . GLN B 242 ? 160.4707 160.4707 160.4707 0.0000 0.0000 0.0000 242 GLN B CA  
5789 C C   . GLN B 242 ? 160.9631 160.9631 160.9631 0.0000 0.0000 0.0000 242 GLN B C   
5790 O O   . GLN B 242 ? 160.5301 160.5301 160.5301 0.0000 0.0000 0.0000 242 GLN B O   
5791 C CB  . GLN B 242 ? 161.3547 161.3547 161.3547 0.0000 0.0000 0.0000 242 GLN B CB  
5792 C CG  . GLN B 242 ? 161.2268 161.2268 161.2268 0.0000 0.0000 0.0000 242 GLN B CG  
5793 C CD  . GLN B 242 ? 161.1746 161.1746 161.1746 0.0000 0.0000 0.0000 242 GLN B CD  
5794 O OE1 . GLN B 242 ? 161.5087 161.5087 161.5087 0.0000 0.0000 0.0000 242 GLN B OE1 
5795 N NE2 . GLN B 242 ? 160.9648 160.9648 160.9648 0.0000 0.0000 0.0000 242 GLN B NE2 
5796 N N   . LYS B 243 ? 161.1886 161.1886 161.1886 0.0000 0.0000 0.0000 243 LYS B N   
5797 C CA  . LYS B 243 ? 159.9988 159.9988 159.9988 0.0000 0.0000 0.0000 243 LYS B CA  
5798 C C   . LYS B 243 ? 160.5293 160.5293 160.5293 0.0000 0.0000 0.0000 243 LYS B C   
5799 O O   . LYS B 243 ? 161.1718 161.1718 161.1718 0.0000 0.0000 0.0000 243 LYS B O   
5800 C CB  . LYS B 243 ? 161.1049 161.1049 161.1049 0.0000 0.0000 0.0000 243 LYS B CB  
5801 C CG  . LYS B 243 ? 161.3848 161.3848 161.3848 0.0000 0.0000 0.0000 243 LYS B CG  
5802 C CD  . LYS B 243 ? 161.7576 161.7576 161.7576 0.0000 0.0000 0.0000 243 LYS B CD  
5803 C CE  . LYS B 243 ? 161.2325 161.2325 161.2325 0.0000 0.0000 0.0000 243 LYS B CE  
5804 N NZ  . LYS B 243 ? 160.9238 160.9238 160.9238 0.0000 0.0000 0.0000 243 LYS B NZ  
5805 N N   . PHE B 244 ? 160.6754 160.6754 160.6754 0.0000 0.0000 0.0000 244 PHE B N   
5806 C CA  . PHE B 244 ? 160.8015 160.8015 160.8015 0.0000 0.0000 0.0000 244 PHE B CA  
5807 C C   . PHE B 244 ? 160.4944 160.4944 160.4944 0.0000 0.0000 0.0000 244 PHE B C   
5808 O O   . PHE B 244 ? 158.3790 158.3790 158.3790 0.0000 0.0000 0.0000 244 PHE B O   
5809 C CB  . PHE B 244 ? 160.4369 160.4369 160.4369 0.0000 0.0000 0.0000 244 PHE B CB  
5810 C CG  . PHE B 244 ? 161.3110 161.3110 161.3110 0.0000 0.0000 0.0000 244 PHE B CG  
5811 C CD1 . PHE B 244 ? 160.9682 160.9682 160.9682 0.0000 0.0000 0.0000 244 PHE B CD1 
5812 C CD2 . PHE B 244 ? 160.7784 160.7784 160.7784 0.0000 0.0000 0.0000 244 PHE B CD2 
5813 C CE1 . PHE B 244 ? 160.7941 160.7941 160.7941 0.0000 0.0000 0.0000 244 PHE B CE1 
5814 C CE2 . PHE B 244 ? 160.7588 160.7588 160.7588 0.0000 0.0000 0.0000 244 PHE B CE2 
5815 C CZ  . PHE B 244 ? 160.6636 160.6636 160.6636 0.0000 0.0000 0.0000 244 PHE B CZ  
5816 N N   . ILE B 245 ? 160.8000 160.8000 160.8000 0.0000 0.0000 0.0000 245 ILE B N   
5817 C CA  . ILE B 245 ? 160.6394 160.6394 160.6394 0.0000 0.0000 0.0000 245 ILE B CA  
5818 C C   . ILE B 245 ? 161.1872 161.1872 161.1872 0.0000 0.0000 0.0000 245 ILE B C   
5819 O O   . ILE B 245 ? 161.4267 161.4267 161.4267 0.0000 0.0000 0.0000 245 ILE B O   
5820 C CB  . ILE B 245 ? 161.0886 161.0886 161.0886 0.0000 0.0000 0.0000 245 ILE B CB  
5821 C CG1 . ILE B 245 ? 160.0721 160.0721 160.0721 0.0000 0.0000 0.0000 245 ILE B CG1 
5822 C CG2 . ILE B 245 ? 160.8649 160.8649 160.8649 0.0000 0.0000 0.0000 245 ILE B CG2 
5823 C CD1 . ILE B 245 ? 160.4210 160.4210 160.4210 0.0000 0.0000 0.0000 245 ILE B CD1 
5824 N N   . ILE B 246 ? 161.1503 161.1503 161.1503 0.0000 0.0000 0.0000 246 ILE B N   
5825 C CA  . ILE B 246 ? 161.5249 161.5249 161.5249 0.0000 0.0000 0.0000 246 ILE B CA  
5826 C C   . ILE B 246 ? 161.3082 161.3082 161.3082 0.0000 0.0000 0.0000 246 ILE B C   
5827 O O   . ILE B 246 ? 161.3101 161.3101 161.3101 0.0000 0.0000 0.0000 246 ILE B O   
5828 C CB  . ILE B 246 ? 161.5483 161.5483 161.5483 0.0000 0.0000 0.0000 246 ILE B CB  
5829 C CG1 . ILE B 246 ? 161.0571 161.0571 161.0571 0.0000 0.0000 0.0000 246 ILE B CG1 
5830 C CG2 . ILE B 246 ? 160.6833 160.6833 160.6833 0.0000 0.0000 0.0000 246 ILE B CG2 
5831 C CD1 . ILE B 246 ? 160.5038 160.5038 160.5038 0.0000 0.0000 0.0000 246 ILE B CD1 
5832 N N   . ARG B 247 ? 158.9236 158.9236 158.9236 0.0000 0.0000 0.0000 247 ARG B N   
5833 C CA  . ARG B 247 ? 161.4167 161.4167 161.4167 0.0000 0.0000 0.0000 247 ARG B CA  
5834 C C   . ARG B 247 ? 161.2008 161.2008 161.2008 0.0000 0.0000 0.0000 247 ARG B C   
5835 O O   . ARG B 247 ? 161.2835 161.2835 161.2835 0.0000 0.0000 0.0000 247 ARG B O   
5836 C CB  . ARG B 247 ? 161.5285 161.5285 161.5285 0.0000 0.0000 0.0000 247 ARG B CB  
5837 C CG  . ARG B 247 ? 161.2129 161.2129 161.2129 0.0000 0.0000 0.0000 247 ARG B CG  
5838 C CD  . ARG B 247 ? 160.9267 160.9267 160.9267 0.0000 0.0000 0.0000 247 ARG B CD  
5839 N NE  . ARG B 247 ? 161.2698 161.2698 161.2698 0.0000 0.0000 0.0000 247 ARG B NE  
5840 C CZ  . ARG B 247 ? 161.1133 161.1133 161.1133 0.0000 0.0000 0.0000 247 ARG B CZ  
5841 N NH1 . ARG B 247 ? 161.2531 161.2531 161.2531 0.0000 0.0000 0.0000 247 ARG B NH1 
5842 N NH2 . ARG B 247 ? 161.0235 161.0235 161.0235 0.0000 0.0000 0.0000 247 ARG B NH2 
5843 N N   . SER B 248 ? 161.1704 161.1704 161.1704 0.0000 0.0000 0.0000 248 SER B N   
5844 C CA  . SER B 248 ? 161.3620 161.3620 161.3620 0.0000 0.0000 0.0000 248 SER B CA  
5845 C C   . SER B 248 ? 159.8605 159.8605 159.8605 0.0000 0.0000 0.0000 248 SER B C   
5846 O O   . SER B 248 ? 160.0328 160.0328 160.0328 0.0000 0.0000 0.0000 248 SER B O   
5847 C CB  . SER B 248 ? 160.0265 160.0265 160.0265 0.0000 0.0000 0.0000 248 SER B CB  
5848 O OG  . SER B 248 ? 161.2102 161.2102 161.2102 0.0000 0.0000 0.0000 248 SER B OG  
5849 N N   . LYS B 249 ? 160.9803 160.9803 160.9803 0.0000 0.0000 0.0000 249 LYS B N   
5850 C CA  . LYS B 249 ? 161.2036 161.2036 161.2036 0.0000 0.0000 0.0000 249 LYS B CA  
5851 C C   . LYS B 249 ? 161.2819 161.2819 161.2819 0.0000 0.0000 0.0000 249 LYS B C   
5852 O O   . LYS B 249 ? 161.1531 161.1531 161.1531 0.0000 0.0000 0.0000 249 LYS B O   
5853 C CB  . LYS B 249 ? 161.2313 161.2313 161.2313 0.0000 0.0000 0.0000 249 LYS B CB  
5854 C CG  . LYS B 249 ? 161.4096 161.4096 161.4096 0.0000 0.0000 0.0000 249 LYS B CG  
5855 C CD  . LYS B 249 ? 160.4541 160.4541 160.4541 0.0000 0.0000 0.0000 249 LYS B CD  
5856 C CE  . LYS B 249 ? 161.4515 161.4515 161.4515 0.0000 0.0000 0.0000 249 LYS B CE  
5857 N NZ  . LYS B 249 ? 159.7988 159.7988 159.7988 0.0000 0.0000 0.0000 249 LYS B NZ  
5858 N N   . ILE B 250 ? 160.3668 160.3668 160.3668 0.0000 0.0000 0.0000 250 ILE B N   
5859 C CA  . ILE B 250 ? 160.4246 160.4246 160.4246 0.0000 0.0000 0.0000 250 ILE B CA  
5860 C C   . ILE B 250 ? 161.3584 161.3584 161.3584 0.0000 0.0000 0.0000 250 ILE B C   
5861 O O   . ILE B 250 ? 161.3001 161.3001 161.3001 0.0000 0.0000 0.0000 250 ILE B O   
5862 C CB  . ILE B 250 ? 161.2496 161.2496 161.2496 0.0000 0.0000 0.0000 250 ILE B CB  
5863 C CG1 . ILE B 250 ? 161.5406 161.5406 161.5406 0.0000 0.0000 0.0000 250 ILE B CG1 
5864 C CG2 . ILE B 250 ? 161.4077 161.4077 161.4077 0.0000 0.0000 0.0000 250 ILE B CG2 
5865 C CD1 . ILE B 250 ? 161.3750 161.3750 161.3750 0.0000 0.0000 0.0000 250 ILE B CD1 
5866 N N   . ILE B 251 ? 161.5006 161.5006 161.5006 0.0000 0.0000 0.0000 251 ILE B N   
5867 C CA  . ILE B 251 ? 160.5418 160.5418 160.5418 0.0000 0.0000 0.0000 251 ILE B CA  
5868 C C   . ILE B 251 ? 161.2101 161.2101 161.2101 0.0000 0.0000 0.0000 251 ILE B C   
5869 O O   . ILE B 251 ? 161.1494 161.1494 161.1494 0.0000 0.0000 0.0000 251 ILE B O   
5870 C CB  . ILE B 251 ? 161.3591 161.3591 161.3591 0.0000 0.0000 0.0000 251 ILE B CB  
5871 C CG1 . ILE B 251 ? 161.5610 161.5610 161.5610 0.0000 0.0000 0.0000 251 ILE B CG1 
5872 C CG2 . ILE B 251 ? 161.2136 161.2136 161.2136 0.0000 0.0000 0.0000 251 ILE B CG2 
5873 C CD1 . ILE B 251 ? 161.3930 161.3930 161.3930 0.0000 0.0000 0.0000 251 ILE B CD1 
5874 N N   . THR B 252 ? 161.3935 161.3935 161.3935 0.0000 0.0000 0.0000 252 THR B N   
5875 C CA  . THR B 252 ? 161.4175 161.4175 161.4175 0.0000 0.0000 0.0000 252 THR B CA  
5876 C C   . THR B 252 ? 161.4034 161.4034 161.4034 0.0000 0.0000 0.0000 252 THR B C   
5877 O O   . THR B 252 ? 161.4225 161.4225 161.4225 0.0000 0.0000 0.0000 252 THR B O   
5878 C CB  . THR B 252 ? 161.5486 161.5486 161.5486 0.0000 0.0000 0.0000 252 THR B CB  
5879 O OG1 . THR B 252 ? 161.4289 161.4289 161.4289 0.0000 0.0000 0.0000 252 THR B OG1 
5880 C CG2 . THR B 252 ? 161.3122 161.3122 161.3122 0.0000 0.0000 0.0000 252 THR B CG2 
5881 N N   . TYR B 253 ? 161.0512 161.0512 161.0512 0.0000 0.0000 0.0000 253 TYR B N   
5882 C CA  . TYR B 253 ? 161.0547 161.0547 161.0547 0.0000 0.0000 0.0000 253 TYR B CA  
5883 C C   . TYR B 253 ? 160.6645 160.6645 160.6645 0.0000 0.0000 0.0000 253 TYR B C   
5884 O O   . TYR B 253 ? 160.6204 160.6204 160.6204 0.0000 0.0000 0.0000 253 TYR B O   
5885 C CB  . TYR B 253 ? 160.7236 160.7236 160.7236 0.0000 0.0000 0.0000 253 TYR B CB  
5886 C CG  . TYR B 253 ? 160.2742 160.2742 160.2742 0.0000 0.0000 0.0000 253 TYR B CG  
5887 C CD1 . TYR B 253 ? 160.5000 160.5000 160.5000 0.0000 0.0000 0.0000 253 TYR B CD1 
5888 C CD2 . TYR B 253 ? 160.5268 160.5268 160.5268 0.0000 0.0000 0.0000 253 TYR B CD2 
5889 C CE1 . TYR B 253 ? 160.5705 160.5705 160.5705 0.0000 0.0000 0.0000 253 TYR B CE1 
5890 C CE2 . TYR B 253 ? 160.2318 160.2318 160.2318 0.0000 0.0000 0.0000 253 TYR B CE2 
5891 C CZ  . TYR B 253 ? 160.9593 160.9593 160.9593 0.0000 0.0000 0.0000 253 TYR B CZ  
5892 O OH  . TYR B 253 ? 160.0661 160.0661 160.0661 0.0000 0.0000 0.0000 253 TYR B OH  
5893 N N   . ILE B 254 ? 160.6607 160.6607 160.6607 0.0000 0.0000 0.0000 254 ILE B N   
5894 C CA  . ILE B 254 ? 160.0325 160.0325 160.0325 0.0000 0.0000 0.0000 254 ILE B CA  
5895 C C   . ILE B 254 ? 160.4199 160.4199 160.4199 0.0000 0.0000 0.0000 254 ILE B C   
5896 O O   . ILE B 254 ? 161.0950 161.0950 161.0950 0.0000 0.0000 0.0000 254 ILE B O   
5897 C CB  . ILE B 254 ? 161.1922 161.1922 161.1922 0.0000 0.0000 0.0000 254 ILE B CB  
5898 C CG1 . ILE B 254 ? 161.3847 161.3847 161.3847 0.0000 0.0000 0.0000 254 ILE B CG1 
5899 C CG2 . ILE B 254 ? 161.7011 161.7011 161.7011 0.0000 0.0000 0.0000 254 ILE B CG2 
5900 C CD1 . ILE B 254 ? 161.4956 161.4956 161.4956 0.0000 0.0000 0.0000 254 ILE B CD1 
5901 N N   . ARG B 255 ? 161.4118 161.4118 161.4118 0.0000 0.0000 0.0000 255 ARG B N   
5902 C CA  . ARG B 255 ? 161.5896 161.5896 161.5896 0.0000 0.0000 0.0000 255 ARG B CA  
5903 C C   . ARG B 255 ? 161.5501 161.5501 161.5501 0.0000 0.0000 0.0000 255 ARG B C   
5904 O O   . ARG B 255 ? 161.3454 161.3454 161.3454 0.0000 0.0000 0.0000 255 ARG B O   
5905 C CB  . ARG B 255 ? 161.2433 161.2433 161.2433 0.0000 0.0000 0.0000 255 ARG B CB  
5906 C CG  . ARG B 255 ? 160.9278 160.9278 160.9278 0.0000 0.0000 0.0000 255 ARG B CG  
5907 C CD  . ARG B 255 ? 160.3581 160.3581 160.3581 0.0000 0.0000 0.0000 255 ARG B CD  
5908 N NE  . ARG B 255 ? 161.1645 161.1645 161.1645 0.0000 0.0000 0.0000 255 ARG B NE  
5909 C CZ  . ARG B 255 ? 160.9222 160.9222 160.9222 0.0000 0.0000 0.0000 255 ARG B CZ  
5910 N NH1 . ARG B 255 ? 161.0344 161.0344 161.0344 0.0000 0.0000 0.0000 255 ARG B NH1 
5911 N NH2 . ARG B 255 ? 161.0718 161.0718 161.0718 0.0000 0.0000 0.0000 255 ARG B NH2 
5912 N N   . SER B 256 ? 161.3293 161.3293 161.3293 0.0000 0.0000 0.0000 256 SER B N   
5913 C CA  . SER B 256 ? 160.3288 160.3288 160.3288 0.0000 0.0000 0.0000 256 SER B CA  
5914 C C   . SER B 256 ? 160.5077 160.5077 160.5077 0.0000 0.0000 0.0000 256 SER B C   
5915 O O   . SER B 256 ? 160.1596 160.1596 160.1596 0.0000 0.0000 0.0000 256 SER B O   
5916 C CB  . SER B 256 ? 160.3382 160.3382 160.3382 0.0000 0.0000 0.0000 256 SER B CB  
5917 O OG  . SER B 256 ? 160.6078 160.6078 160.6078 0.0000 0.0000 0.0000 256 SER B OG  
5918 N N   . PHE B 257 ? 161.2852 161.2852 161.2852 0.0000 0.0000 0.0000 257 PHE B N   
5919 C CA  . PHE B 257 ? 161.7060 161.7060 161.7060 0.0000 0.0000 0.0000 257 PHE B CA  
5920 C C   . PHE B 257 ? 160.6894 160.6894 160.6894 0.0000 0.0000 0.0000 257 PHE B C   
5921 O O   . PHE B 257 ? 160.8015 160.8015 160.8015 0.0000 0.0000 0.0000 257 PHE B O   
5922 C CB  . PHE B 257 ? 160.8763 160.8763 160.8763 0.0000 0.0000 0.0000 257 PHE B CB  
5923 C CG  . PHE B 257 ? 160.9353 160.9353 160.9353 0.0000 0.0000 0.0000 257 PHE B CG  
5924 C CD1 . PHE B 257 ? 160.0041 160.0041 160.0041 0.0000 0.0000 0.0000 257 PHE B CD1 
5925 C CD2 . PHE B 257 ? 161.0907 161.0907 161.0907 0.0000 0.0000 0.0000 257 PHE B CD2 
5926 C CE1 . PHE B 257 ? 160.1560 160.1560 160.1560 0.0000 0.0000 0.0000 257 PHE B CE1 
5927 C CE2 . PHE B 257 ? 161.0284 161.0284 161.0284 0.0000 0.0000 0.0000 257 PHE B CE2 
5928 C CZ  . PHE B 257 ? 160.2799 160.2799 160.2799 0.0000 0.0000 0.0000 257 PHE B CZ  
5929 N N   . LEU B 258 ? 160.6540 160.6540 160.6540 0.0000 0.0000 0.0000 258 LEU B N   
5930 C CA  . LEU B 258 ? 159.2815 159.2815 159.2815 0.0000 0.0000 0.0000 258 LEU B CA  
5931 C C   . LEU B 258 ? 160.0958 160.0958 160.0958 0.0000 0.0000 0.0000 258 LEU B C   
5932 O O   . LEU B 258 ? 159.6584 159.6584 159.6584 0.0000 0.0000 0.0000 258 LEU B O   
5933 C CB  . LEU B 258 ? 161.2418 161.2418 161.2418 0.0000 0.0000 0.0000 258 LEU B CB  
5934 C CG  . LEU B 258 ? 161.2500 161.2500 161.2500 0.0000 0.0000 0.0000 258 LEU B CG  
5935 C CD1 . LEU B 258 ? 160.7588 160.7588 160.7588 0.0000 0.0000 0.0000 258 LEU B CD1 
5936 C CD2 . LEU B 258 ? 160.5288 160.5288 160.5288 0.0000 0.0000 0.0000 258 LEU B CD2 
5937 N N   . ASP B 259 ? 161.3239 161.3239 161.3239 0.0000 0.0000 0.0000 259 ASP B N   
5938 C CA  . ASP B 259 ? 161.1907 161.1907 161.1907 0.0000 0.0000 0.0000 259 ASP B CA  
5939 C C   . ASP B 259 ? 161.3437 161.3437 161.3437 0.0000 0.0000 0.0000 259 ASP B C   
5940 O O   . ASP B 259 ? 161.3282 161.3282 161.3282 0.0000 0.0000 0.0000 259 ASP B O   
5941 C CB  . ASP B 259 ? 161.4997 161.4997 161.4997 0.0000 0.0000 0.0000 259 ASP B CB  
5942 C CG  . ASP B 259 ? 161.5692 161.5692 161.5692 0.0000 0.0000 0.0000 259 ASP B CG  
5943 O OD1 . ASP B 259 ? 161.6044 161.6044 161.6044 0.0000 0.0000 0.0000 259 ASP B OD1 
5944 O OD2 . ASP B 259 ? 160.8451 160.8451 160.8451 0.0000 0.0000 0.0000 259 ASP B OD2 
5945 N N   . GLU B 260 ? 160.8960 160.8960 160.8960 0.0000 0.0000 0.0000 260 GLU B N   
5946 C CA  . GLU B 260 ? 161.2420 161.2420 161.2420 0.0000 0.0000 0.0000 260 GLU B CA  
5947 C C   . GLU B 260 ? 161.4238 161.4238 161.4238 0.0000 0.0000 0.0000 260 GLU B C   
5948 O O   . GLU B 260 ? 160.5688 160.5688 160.5688 0.0000 0.0000 0.0000 260 GLU B O   
5949 C CB  . GLU B 260 ? 160.9926 160.9926 160.9926 0.0000 0.0000 0.0000 260 GLU B CB  
5950 C CG  . GLU B 260 ? 160.3320 160.3320 160.3320 0.0000 0.0000 0.0000 260 GLU B CG  
5951 C CD  . GLU B 260 ? 161.1247 161.1247 161.1247 0.0000 0.0000 0.0000 260 GLU B CD  
5952 O OE1 . GLU B 260 ? 161.2195 161.2195 161.2195 0.0000 0.0000 0.0000 260 GLU B OE1 
5953 O OE2 . GLU B 260 ? 161.2120 161.2120 161.2120 0.0000 0.0000 0.0000 260 GLU B OE2 
5954 N N   . LEU B 261 ? 161.1367 161.1367 161.1367 0.0000 0.0000 0.0000 261 LEU B N   
5955 C CA  . LEU B 261 ? 161.3462 161.3462 161.3462 0.0000 0.0000 0.0000 261 LEU B CA  
5956 C C   . LEU B 261 ? 161.4291 161.4291 161.4291 0.0000 0.0000 0.0000 261 LEU B C   
5957 O O   . LEU B 261 ? 161.4606 161.4606 161.4606 0.0000 0.0000 0.0000 261 LEU B O   
5958 C CB  . LEU B 261 ? 161.4147 161.4147 161.4147 0.0000 0.0000 0.0000 261 LEU B CB  
5959 C CG  . LEU B 261 ? 161.4059 161.4059 161.4059 0.0000 0.0000 0.0000 261 LEU B CG  
5960 C CD1 . LEU B 261 ? 161.5439 161.5439 161.5439 0.0000 0.0000 0.0000 261 LEU B CD1 
5961 C CD2 . LEU B 261 ? 161.0352 161.0352 161.0352 0.0000 0.0000 0.0000 261 LEU B CD2 
5962 N N   . GLY B 262 ? 161.1596 161.1596 161.1596 0.0000 0.0000 0.0000 262 GLY B N   
5963 C CA  . GLY B 262 ? 161.2371 161.2371 161.2371 0.0000 0.0000 0.0000 262 GLY B CA  
5964 C C   . GLY B 262 ? 161.3378 161.3378 161.3378 0.0000 0.0000 0.0000 262 GLY B C   
5965 O O   . GLY B 262 ? 161.2482 161.2482 161.2482 0.0000 0.0000 0.0000 262 GLY B O   
5966 N N   . PHE B 263 ? 161.5216 161.5216 161.5216 0.0000 0.0000 0.0000 263 PHE B N   
5967 C CA  . PHE B 263 ? 161.4225 161.4225 161.4225 0.0000 0.0000 0.0000 263 PHE B CA  
5968 C C   . PHE B 263 ? 161.6089 161.6089 161.6089 0.0000 0.0000 0.0000 263 PHE B C   
5969 O O   . PHE B 263 ? 161.3235 161.3235 161.3235 0.0000 0.0000 0.0000 263 PHE B O   
5970 C CB  . PHE B 263 ? 161.4470 161.4470 161.4470 0.0000 0.0000 0.0000 263 PHE B CB  
5971 C CG  . PHE B 263 ? 161.4775 161.4775 161.4775 0.0000 0.0000 0.0000 263 PHE B CG  
5972 C CD1 . PHE B 263 ? 161.5678 161.5678 161.5678 0.0000 0.0000 0.0000 263 PHE B CD1 
5973 C CD2 . PHE B 263 ? 161.5107 161.5107 161.5107 0.0000 0.0000 0.0000 263 PHE B CD2 
5974 C CE1 . PHE B 263 ? 161.5304 161.5304 161.5304 0.0000 0.0000 0.0000 263 PHE B CE1 
5975 C CE2 . PHE B 263 ? 161.5989 161.5989 161.5989 0.0000 0.0000 0.0000 263 PHE B CE2 
5976 C CZ  . PHE B 263 ? 161.6216 161.6216 161.6216 0.0000 0.0000 0.0000 263 PHE B CZ  
5977 N N   . LEU B 264 ? 161.6786 161.6786 161.6786 0.0000 0.0000 0.0000 264 LEU B N   
5978 C CA  . LEU B 264 ? 161.4257 161.4257 161.4257 0.0000 0.0000 0.0000 264 LEU B CA  
5979 C C   . LEU B 264 ? 161.3451 161.3451 161.3451 0.0000 0.0000 0.0000 264 LEU B C   
5980 O O   . LEU B 264 ? 161.3824 161.3824 161.3824 0.0000 0.0000 0.0000 264 LEU B O   
5981 C CB  . LEU B 264 ? 161.4653 161.4653 161.4653 0.0000 0.0000 0.0000 264 LEU B CB  
5982 C CG  . LEU B 264 ? 161.4577 161.4577 161.4577 0.0000 0.0000 0.0000 264 LEU B CG  
5983 C CD1 . LEU B 264 ? 161.6025 161.6025 161.6025 0.0000 0.0000 0.0000 264 LEU B CD1 
5984 C CD2 . LEU B 264 ? 161.6126 161.6126 161.6126 0.0000 0.0000 0.0000 264 LEU B CD2 
5985 N N   . GLU B 265 ? 161.2526 161.2526 161.2526 0.0000 0.0000 0.0000 265 GLU B N   
5986 C CA  . GLU B 265 ? 161.3120 161.3120 161.3120 0.0000 0.0000 0.0000 265 GLU B CA  
5987 C C   . GLU B 265 ? 161.4098 161.4098 161.4098 0.0000 0.0000 0.0000 265 GLU B C   
5988 O O   . GLU B 265 ? 161.5681 161.5681 161.5681 0.0000 0.0000 0.0000 265 GLU B O   
5989 C CB  . GLU B 265 ? 161.3903 161.3903 161.3903 0.0000 0.0000 0.0000 265 GLU B CB  
5990 C CG  . GLU B 265 ? 161.3949 161.3949 161.3949 0.0000 0.0000 0.0000 265 GLU B CG  
5991 C CD  . GLU B 265 ? 161.4531 161.4531 161.4531 0.0000 0.0000 0.0000 265 GLU B CD  
5992 O OE1 . GLU B 265 ? 161.3179 161.3179 161.3179 0.0000 0.0000 0.0000 265 GLU B OE1 
5993 O OE2 . GLU B 265 ? 161.2742 161.2742 161.2742 0.0000 0.0000 0.0000 265 GLU B OE2 
5994 N N   . ILE B 266 ? 161.3558 161.3558 161.3558 0.0000 0.0000 0.0000 266 ILE B N   
5995 C CA  . ILE B 266 ? 161.6191 161.6191 161.6191 0.0000 0.0000 0.0000 266 ILE B CA  
5996 C C   . ILE B 266 ? 161.3924 161.3924 161.3924 0.0000 0.0000 0.0000 266 ILE B C   
5997 O O   . ILE B 266 ? 161.4476 161.4476 161.4476 0.0000 0.0000 0.0000 266 ILE B O   
5998 C CB  . ILE B 266 ? 161.5361 161.5361 161.5361 0.0000 0.0000 0.0000 266 ILE B CB  
5999 C CG1 . ILE B 266 ? 161.5600 161.5600 161.5600 0.0000 0.0000 0.0000 266 ILE B CG1 
6000 C CG2 . ILE B 266 ? 161.2621 161.2621 161.2621 0.0000 0.0000 0.0000 266 ILE B CG2 
6001 C CD1 . ILE B 266 ? 161.3857 161.3857 161.3857 0.0000 0.0000 0.0000 266 ILE B CD1 
6002 N N   . GLU B 267 ? 161.4556 161.4556 161.4556 0.0000 0.0000 0.0000 267 GLU B N   
6003 C CA  . GLU B 267 ? 161.4866 161.4866 161.4866 0.0000 0.0000 0.0000 267 GLU B CA  
6004 C C   . GLU B 267 ? 161.3708 161.3708 161.3708 0.0000 0.0000 0.0000 267 GLU B C   
6005 O O   . GLU B 267 ? 161.3788 161.3788 161.3788 0.0000 0.0000 0.0000 267 GLU B O   
6006 C CB  . GLU B 267 ? 161.0586 161.0586 161.0586 0.0000 0.0000 0.0000 267 GLU B CB  
6007 C CG  . GLU B 267 ? 161.5143 161.5143 161.5143 0.0000 0.0000 0.0000 267 GLU B CG  
6008 C CD  . GLU B 267 ? 162.3154 162.3154 162.3154 0.0000 0.0000 0.0000 267 GLU B CD  
6009 O OE1 . GLU B 267 ? 162.3496 162.3496 162.3496 0.0000 0.0000 0.0000 267 GLU B OE1 
6010 O OE2 . GLU B 267 ? 162.4558 162.4558 162.4558 0.0000 0.0000 0.0000 267 GLU B OE2 
6011 N N   . THR B 268 ? 162.4984 162.4984 162.4984 0.0000 0.0000 0.0000 268 THR B N   
6012 C CA  . THR B 268 ? 162.5850 162.5850 162.5850 0.0000 0.0000 0.0000 268 THR B CA  
6013 C C   . THR B 268 ? 162.5012 162.5012 162.5012 0.0000 0.0000 0.0000 268 THR B C   
6014 O O   . THR B 268 ? 162.4862 162.4862 162.4862 0.0000 0.0000 0.0000 268 THR B O   
6015 C CB  . THR B 268 ? 162.4788 162.4788 162.4788 0.0000 0.0000 0.0000 268 THR B CB  
6016 O OG1 . THR B 268 ? 167.3689 167.3689 167.3689 0.0000 0.0000 0.0000 268 THR B OG1 
6017 C CG2 . THR B 268 ? 167.6272 167.6272 167.6272 0.0000 0.0000 0.0000 268 THR B CG2 
6018 N N   . PRO B 269 ? 168.0039 168.0039 168.0039 0.0000 0.0000 0.0000 269 PRO B N   
6019 C CA  . PRO B 269 ? 167.8068 167.8068 167.8068 0.0000 0.0000 0.0000 269 PRO B CA  
6020 C C   . PRO B 269 ? 167.7671 167.7671 167.7671 0.0000 0.0000 0.0000 269 PRO B C   
6021 O O   . PRO B 269 ? 167.7730 167.7730 167.7730 0.0000 0.0000 0.0000 269 PRO B O   
6022 C CB  . PRO B 269 ? 167.9459 167.9459 167.9459 0.0000 0.0000 0.0000 269 PRO B CB  
6023 C CG  . PRO B 269 ? 167.8448 167.8448 167.8448 0.0000 0.0000 0.0000 269 PRO B CG  
6024 C CD  . PRO B 269 ? 177.7030 177.7030 177.7030 0.0000 0.0000 0.0000 269 PRO B CD  
6025 N N   . MET B 270 ? 177.8357 177.8357 177.8357 0.0000 0.0000 0.0000 270 MET B N   
6026 C CA  . MET B 270 ? 177.8320 177.8320 177.8320 0.0000 0.0000 0.0000 270 MET B CA  
6027 C C   . MET B 270 ? 178.0241 178.0241 178.0241 0.0000 0.0000 0.0000 270 MET B C   
6028 O O   . MET B 270 ? 178.2161 178.2161 178.2161 0.0000 0.0000 0.0000 270 MET B O   
6029 C CB  . MET B 270 ? 178.2659 178.2659 178.2659 0.0000 0.0000 0.0000 270 MET B CB  
6030 C CG  . MET B 270 ? 178.6986 178.6986 178.6986 0.0000 0.0000 0.0000 270 MET B CG  
6031 S SD  . MET B 270 ? 178.5339 178.5339 178.5339 0.0000 0.0000 0.0000 270 MET B SD  
6032 C CE  . MET B 270 ? 172.4467 172.4467 172.4467 0.0000 0.0000 0.0000 270 MET B CE  
6033 N N   . MET B 271 ? 172.3975 172.3975 172.3975 0.0000 0.0000 0.0000 271 MET B N   
6034 C CA  . MET B 271 ? 172.5831 172.5831 172.5831 0.0000 0.0000 0.0000 271 MET B CA  
6035 C C   . MET B 271 ? 173.2268 173.2268 173.2268 0.0000 0.0000 0.0000 271 MET B C   
6036 O O   . MET B 271 ? 172.4880 172.4880 172.4880 0.0000 0.0000 0.0000 271 MET B O   
6037 C CB  . MET B 271 ? 172.7379 172.7379 172.7379 0.0000 0.0000 0.0000 271 MET B CB  
6038 C CG  . MET B 271 ? 172.6711 172.6711 172.6711 0.0000 0.0000 0.0000 271 MET B CG  
6039 S SD  . MET B 271 ? 170.7676 170.7676 170.7676 0.0000 0.0000 0.0000 271 MET B SD  
6040 C CE  . MET B 271 ? 170.9170 170.9170 170.9170 0.0000 0.0000 0.0000 271 MET B CE  
6041 N N   . ASN B 272 ? 170.8436 170.8436 170.8436 0.0000 0.0000 0.0000 272 ASN B N   
6042 C CA  . ASN B 272 ? 170.7569 170.7569 170.7569 0.0000 0.0000 0.0000 272 ASN B CA  
6043 C C   . ASN B 272 ? 172.4568 172.4568 172.4568 0.0000 0.0000 0.0000 272 ASN B C   
6044 O O   . ASN B 272 ? 172.4990 172.4990 172.4990 0.0000 0.0000 0.0000 272 ASN B O   
6045 C CB  . ASN B 272 ? 172.6412 172.6412 172.6412 0.0000 0.0000 0.0000 272 ASN B CB  
6046 C CG  . ASN B 272 ? 171.5773 171.5773 171.5773 0.0000 0.0000 0.0000 272 ASN B CG  
6047 O OD1 . ASN B 272 ? 180.9826 180.9826 180.9826 0.0000 0.0000 0.0000 272 ASN B OD1 
6048 N ND2 . ASN B 272 ? 181.2302 181.2302 181.2302 0.0000 0.0000 0.0000 272 ASN B ND2 
6049 N N   . ILE B 273 ? 181.6167 181.6167 181.6167 0.0000 0.0000 0.0000 273 ILE B N   
6050 C CA  . ILE B 273 ? 181.5913 181.5913 181.5913 0.0000 0.0000 0.0000 273 ILE B CA  
6051 C C   . ILE B 273 ? 179.8043 179.8043 179.8043 0.0000 0.0000 0.0000 273 ILE B C   
6052 O O   . ILE B 273 ? 194.5883 194.5883 194.5883 0.0000 0.0000 0.0000 273 ILE B O   
6053 C CB  . ILE B 273 ? 195.0422 195.0422 195.0422 0.0000 0.0000 0.0000 273 ILE B CB  
6054 C CG1 . ILE B 273 ? 195.1232 195.1232 195.1232 0.0000 0.0000 0.0000 273 ILE B CG1 
6055 C CG2 . ILE B 273 ? 195.0520 195.0520 195.0520 0.0000 0.0000 0.0000 273 ILE B CG2 
6056 C CD1 . ILE B 273 ? 195.3250 195.3250 195.3250 0.0000 0.0000 0.0000 273 ILE B CD1 
6057 N N   . ILE B 274 ? 195.8286 195.8286 195.8286 0.0000 0.0000 0.0000 274 ILE B N   
6058 C CA  . ILE B 274 ? 195.3318 195.3318 195.3318 0.0000 0.0000 0.0000 274 ILE B CA  
6059 C C   . ILE B 274 ? 184.1676 184.1676 184.1676 0.0000 0.0000 0.0000 274 ILE B C   
6060 O O   . ILE B 274 ? 183.6235 183.6235 183.6235 0.0000 0.0000 0.0000 274 ILE B O   
6061 C CB  . ILE B 274 ? 183.1687 183.1687 183.1687 0.0000 0.0000 0.0000 274 ILE B CB  
6062 C CG1 . ILE B 274 ? 183.3126 183.3126 183.3126 0.0000 0.0000 0.0000 274 ILE B CG1 
6063 C CG2 . ILE B 274 ? 183.1543 183.1543 183.1543 0.0000 0.0000 0.0000 274 ILE B CG2 
6064 C CD1 . ILE B 274 ? 167.0198 167.0198 167.0198 0.0000 0.0000 0.0000 274 ILE B CD1 
6065 N N   . PRO B 275 ? 166.3882 166.3882 166.3882 0.0000 0.0000 0.0000 275 PRO B N   
6066 C CA  . PRO B 275 ? 166.2559 166.2559 166.2559 0.0000 0.0000 0.0000 275 PRO B CA  
6067 C C   . PRO B 275 ? 166.5368 166.5368 166.5368 0.0000 0.0000 0.0000 275 PRO B C   
6068 O O   . PRO B 275 ? 166.5076 166.5076 166.5076 0.0000 0.0000 0.0000 275 PRO B O   
6069 C CB  . PRO B 275 ? 166.7017 166.7017 166.7017 0.0000 0.0000 0.0000 275 PRO B CB  
6070 C CG  . PRO B 275 ? 166.4830 166.4830 166.4830 0.0000 0.0000 0.0000 275 PRO B CG  
6071 C CD  . PRO B 275 ? 166.4936 166.4936 166.4936 0.0000 0.0000 0.0000 275 PRO B CD  
6072 N N   . GLY B 276 ? 166.3393 166.3393 166.3393 0.0000 0.0000 0.0000 276 GLY B N   
6073 C CA  . GLY B 276 ? 161.5280 161.5280 161.5280 0.0000 0.0000 0.0000 276 GLY B CA  
6074 C C   . GLY B 276 ? 161.3972 161.3972 161.3972 0.0000 0.0000 0.0000 276 GLY B C   
6075 O O   . GLY B 276 ? 161.3709 161.3709 161.3709 0.0000 0.0000 0.0000 276 GLY B O   
6076 N N   . GLY B 277 ? 161.5865 161.5865 161.5865 0.0000 0.0000 0.0000 277 GLY B N   
6077 C CA  . GLY B 277 ? 161.4636 161.4636 161.4636 0.0000 0.0000 0.0000 277 GLY B CA  
6078 C C   . GLY B 277 ? 161.6922 161.6922 161.6922 0.0000 0.0000 0.0000 277 GLY B C   
6079 O O   . GLY B 277 ? 161.6236 161.6236 161.6236 0.0000 0.0000 0.0000 277 GLY B O   
6080 N N   . ALA B 278 ? 161.3224 161.3224 161.3224 0.0000 0.0000 0.0000 278 ALA B N   
6081 C CA  . ALA B 278 ? 161.3031 161.3031 161.3031 0.0000 0.0000 0.0000 278 ALA B CA  
6082 C C   . ALA B 278 ? 161.4171 161.4171 161.4171 0.0000 0.0000 0.0000 278 ALA B C   
6083 O O   . ALA B 278 ? 161.5543 161.5543 161.5543 0.0000 0.0000 0.0000 278 ALA B O   
6084 C CB  . ALA B 278 ? 161.4680 161.4680 161.4680 0.0000 0.0000 0.0000 278 ALA B CB  
6085 N N   . VAL B 279 ? 161.4292 161.4292 161.4292 0.0000 0.0000 0.0000 279 VAL B N   
6086 C CA  . VAL B 279 ? 161.4876 161.4876 161.4876 0.0000 0.0000 0.0000 279 VAL B CA  
6087 C C   . VAL B 279 ? 161.5868 161.5868 161.5868 0.0000 0.0000 0.0000 279 VAL B C   
6088 O O   . VAL B 279 ? 161.7223 161.7223 161.7223 0.0000 0.0000 0.0000 279 VAL B O   
6089 C CB  . VAL B 279 ? 161.6821 161.6821 161.6821 0.0000 0.0000 0.0000 279 VAL B CB  
6090 C CG1 . VAL B 279 ? 161.7370 161.7370 161.7370 0.0000 0.0000 0.0000 279 VAL B CG1 
6091 C CG2 . VAL B 279 ? 161.3446 161.3446 161.3446 0.0000 0.0000 0.0000 279 VAL B CG2 
6092 N N   . ALA B 280 ? 161.3945 161.3945 161.3945 0.0000 0.0000 0.0000 280 ALA B N   
6093 C CA  . ALA B 280 ? 161.3309 161.3309 161.3309 0.0000 0.0000 0.0000 280 ALA B CA  
6094 C C   . ALA B 280 ? 161.4696 161.4696 161.4696 0.0000 0.0000 0.0000 280 ALA B C   
6095 O O   . ALA B 280 ? 161.3316 161.3316 161.3316 0.0000 0.0000 0.0000 280 ALA B O   
6096 C CB  . ALA B 280 ? 161.5466 161.5466 161.5466 0.0000 0.0000 0.0000 280 ALA B CB  
6097 N N   . LYS B 281 ? 161.3926 161.3926 161.3926 0.0000 0.0000 0.0000 281 LYS B N   
6098 C CA  . LYS B 281 ? 161.5451 161.5451 161.5451 0.0000 0.0000 0.0000 281 LYS B CA  
6099 C C   . LYS B 281 ? 161.2734 161.2734 161.2734 0.0000 0.0000 0.0000 281 LYS B C   
6100 O O   . LYS B 281 ? 161.2251 161.2251 161.2251 0.0000 0.0000 0.0000 281 LYS B O   
6101 C CB  . LYS B 281 ? 161.2107 161.2107 161.2107 0.0000 0.0000 0.0000 281 LYS B CB  
6102 C CG  . LYS B 281 ? 161.5547 161.5547 161.5547 0.0000 0.0000 0.0000 281 LYS B CG  
6103 C CD  . LYS B 281 ? 161.3610 161.3610 161.3610 0.0000 0.0000 0.0000 281 LYS B CD  
6104 C CE  . LYS B 281 ? 161.4893 161.4893 161.4893 0.0000 0.0000 0.0000 281 LYS B CE  
6105 N NZ  . LYS B 281 ? 161.3776 161.3776 161.3776 0.0000 0.0000 0.0000 281 LYS B NZ  
6106 N N   . PRO B 282 ? 161.1509 161.1509 161.1509 0.0000 0.0000 0.0000 282 PRO B N   
6107 C CA  . PRO B 282 ? 161.2896 161.2896 161.2896 0.0000 0.0000 0.0000 282 PRO B CA  
6108 C C   . PRO B 282 ? 161.2854 161.2854 161.2854 0.0000 0.0000 0.0000 282 PRO B C   
6109 O O   . PRO B 282 ? 161.4923 161.4923 161.4923 0.0000 0.0000 0.0000 282 PRO B O   
6110 C CB  . PRO B 282 ? 161.4617 161.4617 161.4617 0.0000 0.0000 0.0000 282 PRO B CB  
6111 C CG  . PRO B 282 ? 161.3708 161.3708 161.3708 0.0000 0.0000 0.0000 282 PRO B CG  
6112 C CD  . PRO B 282 ? 161.6089 161.6089 161.6089 0.0000 0.0000 0.0000 282 PRO B CD  
6113 N N   . PHE B 283 ? 161.3367 161.3367 161.3367 0.0000 0.0000 0.0000 283 PHE B N   
6114 C CA  . PHE B 283 ? 161.6155 161.6155 161.6155 0.0000 0.0000 0.0000 283 PHE B CA  
6115 C C   . PHE B 283 ? 161.3392 161.3392 161.3392 0.0000 0.0000 0.0000 283 PHE B C   
6116 O O   . PHE B 283 ? 161.4992 161.4992 161.4992 0.0000 0.0000 0.0000 283 PHE B O   
6117 C CB  . PHE B 283 ? 161.6854 161.6854 161.6854 0.0000 0.0000 0.0000 283 PHE B CB  
6118 C CG  . PHE B 283 ? 161.3048 161.3048 161.3048 0.0000 0.0000 0.0000 283 PHE B CG  
6119 C CD1 . PHE B 283 ? 161.4035 161.4035 161.4035 0.0000 0.0000 0.0000 283 PHE B CD1 
6120 C CD2 . PHE B 283 ? 161.4183 161.4183 161.4183 0.0000 0.0000 0.0000 283 PHE B CD2 
6121 C CE1 . PHE B 283 ? 161.6490 161.6490 161.6490 0.0000 0.0000 0.0000 283 PHE B CE1 
6122 C CE2 . PHE B 283 ? 161.4507 161.4507 161.4507 0.0000 0.0000 0.0000 283 PHE B CE2 
6123 C CZ  . PHE B 283 ? 161.3995 161.3995 161.3995 0.0000 0.0000 0.0000 283 PHE B CZ  
6124 N N   . ILE B 284 ? 161.5353 161.5353 161.5353 0.0000 0.0000 0.0000 284 ILE B N   
6125 C CA  . ILE B 284 ? 161.3883 161.3883 161.3883 0.0000 0.0000 0.0000 284 ILE B CA  
6126 C C   . ILE B 284 ? 161.5173 161.5173 161.5173 0.0000 0.0000 0.0000 284 ILE B C   
6127 O O   . ILE B 284 ? 161.3870 161.3870 161.3870 0.0000 0.0000 0.0000 284 ILE B O   
6128 C CB  . ILE B 284 ? 161.4273 161.4273 161.4273 0.0000 0.0000 0.0000 284 ILE B CB  
6129 C CG1 . ILE B 284 ? 161.3910 161.3910 161.3910 0.0000 0.0000 0.0000 284 ILE B CG1 
6130 C CG2 . ILE B 284 ? 161.7634 161.7634 161.7634 0.0000 0.0000 0.0000 284 ILE B CG2 
6131 C CD1 . ILE B 284 ? 161.7917 161.7917 161.7917 0.0000 0.0000 0.0000 284 ILE B CD1 
6132 N N   . THR B 285 ? 161.5527 161.5527 161.5527 0.0000 0.0000 0.0000 285 THR B N   
6133 C CA  . THR B 285 ? 161.5319 161.5319 161.5319 0.0000 0.0000 0.0000 285 THR B CA  
6134 C C   . THR B 285 ? 161.4016 161.4016 161.4016 0.0000 0.0000 0.0000 285 THR B C   
6135 O O   . THR B 285 ? 161.6837 161.6837 161.6837 0.0000 0.0000 0.0000 285 THR B O   
6136 C CB  . THR B 285 ? 174.3474 174.3474 174.3474 0.0000 0.0000 0.0000 285 THR B CB  
6137 O OG1 . THR B 285 ? 174.7464 174.7464 174.7464 0.0000 0.0000 0.0000 285 THR B OG1 
6138 C CG2 . THR B 285 ? 174.5404 174.5404 174.5404 0.0000 0.0000 0.0000 285 THR B CG2 
6139 N N   . TYR B 286 ? 174.8871 174.8871 174.8871 0.0000 0.0000 0.0000 286 TYR B N   
6140 C CA  . TYR B 286 ? 174.9812 174.9812 174.9812 0.0000 0.0000 0.0000 286 TYR B CA  
6141 C C   . TYR B 286 ? 175.1168 175.1168 175.1168 0.0000 0.0000 0.0000 286 TYR B C   
6142 O O   . TYR B 286 ? 175.1076 175.1076 175.1076 0.0000 0.0000 0.0000 286 TYR B O   
6143 C CB  . TYR B 286 ? 175.2740 175.2740 175.2740 0.0000 0.0000 0.0000 286 TYR B CB  
6144 C CG  . TYR B 286 ? 174.5117 174.5117 174.5117 0.0000 0.0000 0.0000 286 TYR B CG  
6145 C CD1 . TYR B 286 ? 161.8313 161.8313 161.8313 0.0000 0.0000 0.0000 286 TYR B CD1 
6146 C CD2 . TYR B 286 ? 161.6842 161.6842 161.6842 0.0000 0.0000 0.0000 286 TYR B CD2 
6147 C CE1 . TYR B 286 ? 161.9344 161.9344 161.9344 0.0000 0.0000 0.0000 286 TYR B CE1 
6148 C CE2 . TYR B 286 ? 161.9861 161.9861 161.9861 0.0000 0.0000 0.0000 286 TYR B CE2 
6149 C CZ  . TYR B 286 ? 161.6277 161.6277 161.6277 0.0000 0.0000 0.0000 286 TYR B CZ  
6150 O OH  . TYR B 286 ? 161.4479 161.4479 161.4479 0.0000 0.0000 0.0000 286 TYR B OH  
6151 N N   . HIS B 287 ? 161.5385 161.5385 161.5385 0.0000 0.0000 0.0000 287 HIS B N   
6152 C CA  . HIS B 287 ? 161.4983 161.4983 161.4983 0.0000 0.0000 0.0000 287 HIS B CA  
6153 C C   . HIS B 287 ? 170.0413 170.0413 170.0413 0.0000 0.0000 0.0000 287 HIS B C   
6154 O O   . HIS B 287 ? 170.1228 170.1228 170.1228 0.0000 0.0000 0.0000 287 HIS B O   
6155 C CB  . HIS B 287 ? 170.0255 170.0255 170.0255 0.0000 0.0000 0.0000 287 HIS B CB  
6156 C CG  . HIS B 287 ? 170.4411 170.4411 170.4411 0.0000 0.0000 0.0000 287 HIS B CG  
6157 N ND1 . HIS B 287 ? 170.3846 170.3846 170.3846 0.0000 0.0000 0.0000 287 HIS B ND1 
6158 C CD2 . HIS B 287 ? 170.4250 170.4250 170.4250 0.0000 0.0000 0.0000 287 HIS B CD2 
6159 C CE1 . HIS B 287 ? 170.3750 170.3750 170.3750 0.0000 0.0000 0.0000 287 HIS B CE1 
6160 N NE2 . HIS B 287 ? 170.4686 170.4686 170.4686 0.0000 0.0000 0.0000 287 HIS B NE2 
6161 N N   . ASN B 288 ? 165.1319 165.1319 165.1319 0.0000 0.0000 0.0000 288 ASN B N   
6162 C CA  . ASN B 288 ? 165.2676 165.2676 165.2676 0.0000 0.0000 0.0000 288 ASN B CA  
6163 C C   . ASN B 288 ? 165.1103 165.1103 165.1103 0.0000 0.0000 0.0000 288 ASN B C   
6164 O O   . ASN B 288 ? 165.1915 165.1915 165.1915 0.0000 0.0000 0.0000 288 ASN B O   
6165 C CB  . ASN B 288 ? 165.2815 165.2815 165.2815 0.0000 0.0000 0.0000 288 ASN B CB  
6166 C CG  . ASN B 288 ? 165.2110 165.2110 165.2110 0.0000 0.0000 0.0000 288 ASN B CG  
6167 O OD1 . ASN B 288 ? 164.9876 164.9876 164.9876 0.0000 0.0000 0.0000 288 ASN B OD1 
6168 N ND2 . ASN B 288 ? 165.3188 165.3188 165.3188 0.0000 0.0000 0.0000 288 ASN B ND2 
6169 N N   . GLU B 289 ? 161.5425 161.5425 161.5425 0.0000 0.0000 0.0000 289 GLU B N   
6170 C CA  . GLU B 289 ? 161.3510 161.3510 161.3510 0.0000 0.0000 0.0000 289 GLU B CA  
6171 C C   . GLU B 289 ? 161.2726 161.2726 161.2726 0.0000 0.0000 0.0000 289 GLU B C   
6172 O O   . GLU B 289 ? 161.3469 161.3469 161.3469 0.0000 0.0000 0.0000 289 GLU B O   
6173 C CB  . GLU B 289 ? 161.2971 161.2971 161.2971 0.0000 0.0000 0.0000 289 GLU B CB  
6174 C CG  . GLU B 289 ? 161.3681 161.3681 161.3681 0.0000 0.0000 0.0000 289 GLU B CG  
6175 C CD  . GLU B 289 ? 161.5323 161.5323 161.5323 0.0000 0.0000 0.0000 289 GLU B CD  
6176 O OE1 . GLU B 289 ? 161.4601 161.4601 161.4601 0.0000 0.0000 0.0000 289 GLU B OE1 
6177 O OE2 . GLU B 289 ? 161.3276 161.3276 161.3276 0.0000 0.0000 0.0000 289 GLU B OE2 
6178 N N   . LEU B 290 ? 161.3073 161.3073 161.3073 0.0000 0.0000 0.0000 290 LEU B N   
6179 C CA  . LEU B 290 ? 161.3543 161.3543 161.3543 0.0000 0.0000 0.0000 290 LEU B CA  
6180 C C   . LEU B 290 ? 161.5711 161.5711 161.5711 0.0000 0.0000 0.0000 290 LEU B C   
6181 O O   . LEU B 290 ? 161.4381 161.4381 161.4381 0.0000 0.0000 0.0000 290 LEU B O   
6182 C CB  . LEU B 290 ? 161.4005 161.4005 161.4005 0.0000 0.0000 0.0000 290 LEU B CB  
6183 C CG  . LEU B 290 ? 161.4699 161.4699 161.4699 0.0000 0.0000 0.0000 290 LEU B CG  
6184 C CD1 . LEU B 290 ? 161.5909 161.5909 161.5909 0.0000 0.0000 0.0000 290 LEU B CD1 
6185 C CD2 . LEU B 290 ? 161.3161 161.3161 161.3161 0.0000 0.0000 0.0000 290 LEU B CD2 
6186 N N   . ASP B 291 ? 161.3120 161.3120 161.3120 0.0000 0.0000 0.0000 291 ASP B N   
6187 C CA  . ASP B 291 ? 161.2965 161.2965 161.2965 0.0000 0.0000 0.0000 291 ASP B CA  
6188 C C   . ASP B 291 ? 161.5746 161.5746 161.5746 0.0000 0.0000 0.0000 291 ASP B C   
6189 O O   . ASP B 291 ? 161.6373 161.6373 161.6373 0.0000 0.0000 0.0000 291 ASP B O   
6190 C CB  . ASP B 291 ? 161.5286 161.5286 161.5286 0.0000 0.0000 0.0000 291 ASP B CB  
6191 C CG  . ASP B 291 ? 161.7306 161.7306 161.7306 0.0000 0.0000 0.0000 291 ASP B CG  
6192 O OD1 . ASP B 291 ? 161.5067 161.5067 161.5067 0.0000 0.0000 0.0000 291 ASP B OD1 
6193 O OD2 . ASP B 291 ? 161.4825 161.4825 161.4825 0.0000 0.0000 0.0000 291 ASP B OD2 
6194 N N   . MET B 292 ? 161.5110 161.5110 161.5110 0.0000 0.0000 0.0000 292 MET B N   
6195 C CA  . MET B 292 ? 161.3943 161.3943 161.3943 0.0000 0.0000 0.0000 292 MET B CA  
6196 C C   . MET B 292 ? 161.5853 161.5853 161.5853 0.0000 0.0000 0.0000 292 MET B C   
6197 O O   . MET B 292 ? 161.1616 161.1616 161.1616 0.0000 0.0000 0.0000 292 MET B O   
6198 C CB  . MET B 292 ? 161.3213 161.3213 161.3213 0.0000 0.0000 0.0000 292 MET B CB  
6199 C CG  . MET B 292 ? 161.2618 161.2618 161.2618 0.0000 0.0000 0.0000 292 MET B CG  
6200 S SD  . MET B 292 ? 161.4141 161.4141 161.4141 0.0000 0.0000 0.0000 292 MET B SD  
6201 C CE  . MET B 292 ? 161.5539 161.5539 161.5539 0.0000 0.0000 0.0000 292 MET B CE  
6202 N N   . ASN B 293 ? 161.5574 161.5574 161.5574 0.0000 0.0000 0.0000 293 ASN B N   
6203 C CA  . ASN B 293 ? 161.4092 161.4092 161.4092 0.0000 0.0000 0.0000 293 ASN B CA  
6204 C C   . ASN B 293 ? 161.6376 161.6376 161.6376 0.0000 0.0000 0.0000 293 ASN B C   
6205 O O   . ASN B 293 ? 161.2176 161.2176 161.2176 0.0000 0.0000 0.0000 293 ASN B O   
6206 C CB  . ASN B 293 ? 161.1737 161.1737 161.1737 0.0000 0.0000 0.0000 293 ASN B CB  
6207 C CG  . ASN B 293 ? 161.2528 161.2528 161.2528 0.0000 0.0000 0.0000 293 ASN B CG  
6208 O OD1 . ASN B 293 ? 161.5366 161.5366 161.5366 0.0000 0.0000 0.0000 293 ASN B OD1 
6209 N ND2 . ASN B 293 ? 161.3964 161.3964 161.3964 0.0000 0.0000 0.0000 293 ASN B ND2 
6210 N N   . LEU B 294 ? 161.5789 161.5789 161.5789 0.0000 0.0000 0.0000 294 LEU B N   
6211 C CA  . LEU B 294 ? 161.4857 161.4857 161.4857 0.0000 0.0000 0.0000 294 LEU B CA  
6212 C C   . LEU B 294 ? 161.2216 161.2216 161.2216 0.0000 0.0000 0.0000 294 LEU B C   
6213 O O   . LEU B 294 ? 161.2435 161.2435 161.2435 0.0000 0.0000 0.0000 294 LEU B O   
6214 C CB  . LEU B 294 ? 161.4455 161.4455 161.4455 0.0000 0.0000 0.0000 294 LEU B CB  
6215 C CG  . LEU B 294 ? 161.5080 161.5080 161.5080 0.0000 0.0000 0.0000 294 LEU B CG  
6216 C CD1 . LEU B 294 ? 161.2960 161.2960 161.2960 0.0000 0.0000 0.0000 294 LEU B CD1 
6217 C CD2 . LEU B 294 ? 161.2925 161.2925 161.2925 0.0000 0.0000 0.0000 294 LEU B CD2 
6218 N N   . TYR B 295 ? 161.3014 161.3014 161.3014 0.0000 0.0000 0.0000 295 TYR B N   
6219 C CA  . TYR B 295 ? 161.2429 161.2429 161.2429 0.0000 0.0000 0.0000 295 TYR B CA  
6220 C C   . TYR B 295 ? 161.3710 161.3710 161.3710 0.0000 0.0000 0.0000 295 TYR B C   
6221 O O   . TYR B 295 ? 161.8239 161.8239 161.8239 0.0000 0.0000 0.0000 295 TYR B O   
6222 C CB  . TYR B 295 ? 161.3759 161.3759 161.3759 0.0000 0.0000 0.0000 295 TYR B CB  
6223 C CG  . TYR B 295 ? 162.1877 162.1877 162.1877 0.0000 0.0000 0.0000 295 TYR B CG  
6224 C CD1 . TYR B 295 ? 161.2434 161.2434 161.2434 0.0000 0.0000 0.0000 295 TYR B CD1 
6225 C CD2 . TYR B 295 ? 161.2114 161.2114 161.2114 0.0000 0.0000 0.0000 295 TYR B CD2 
6226 C CE1 . TYR B 295 ? 161.4711 161.4711 161.4711 0.0000 0.0000 0.0000 295 TYR B CE1 
6227 C CE2 . TYR B 295 ? 161.4395 161.4395 161.4395 0.0000 0.0000 0.0000 295 TYR B CE2 
6228 C CZ  . TYR B 295 ? 160.9812 160.9812 160.9812 0.0000 0.0000 0.0000 295 TYR B CZ  
6229 O OH  . TYR B 295 ? 161.6024 161.6024 161.6024 0.0000 0.0000 0.0000 295 TYR B OH  
6230 N N   . MET B 296 ? 161.6122 161.6122 161.6122 0.0000 0.0000 0.0000 296 MET B N   
6231 C CA  . MET B 296 ? 161.6997 161.6997 161.6997 0.0000 0.0000 0.0000 296 MET B CA  
6232 C C   . MET B 296 ? 161.8295 161.8295 161.8295 0.0000 0.0000 0.0000 296 MET B C   
6233 O O   . MET B 296 ? 161.5070 161.5070 161.5070 0.0000 0.0000 0.0000 296 MET B O   
6234 C CB  . MET B 296 ? 161.4237 161.4237 161.4237 0.0000 0.0000 0.0000 296 MET B CB  
6235 C CG  . MET B 296 ? 161.5029 161.5029 161.5029 0.0000 0.0000 0.0000 296 MET B CG  
6236 S SD  . MET B 296 ? 161.5844 161.5844 161.5844 0.0000 0.0000 0.0000 296 MET B SD  
6237 C CE  . MET B 296 ? 161.3828 161.3828 161.3828 0.0000 0.0000 0.0000 296 MET B CE  
6238 N N   . ARG B 297 ? 161.3879 161.3879 161.3879 0.0000 0.0000 0.0000 297 ARG B N   
6239 C CA  . ARG B 297 ? 161.5816 161.5816 161.5816 0.0000 0.0000 0.0000 297 ARG B CA  
6240 C C   . ARG B 297 ? 161.0706 161.0706 161.0706 0.0000 0.0000 0.0000 297 ARG B C   
6241 O O   . ARG B 297 ? 161.1538 161.1538 161.1538 0.0000 0.0000 0.0000 297 ARG B O   
6242 C CB  . ARG B 297 ? 160.5098 160.5098 160.5098 0.0000 0.0000 0.0000 297 ARG B CB  
6243 C CG  . ARG B 297 ? 159.8689 159.8689 159.8689 0.0000 0.0000 0.0000 297 ARG B CG  
6244 C CD  . ARG B 297 ? 161.1414 161.1414 161.1414 0.0000 0.0000 0.0000 297 ARG B CD  
6245 N NE  . ARG B 297 ? 161.3201 161.3201 161.3201 0.0000 0.0000 0.0000 297 ARG B NE  
6246 C CZ  . ARG B 297 ? 161.3220 161.3220 161.3220 0.0000 0.0000 0.0000 297 ARG B CZ  
6247 N NH1 . ARG B 297 ? 161.3587 161.3587 161.3587 0.0000 0.0000 0.0000 297 ARG B NH1 
6248 N NH2 . ARG B 297 ? 161.5132 161.5132 161.5132 0.0000 0.0000 0.0000 297 ARG B NH2 
6249 N N   . ILE B 298 ? 161.3339 161.3339 161.3339 0.0000 0.0000 0.0000 298 ILE B N   
6250 C CA  . ILE B 298 ? 161.4324 161.4324 161.4324 0.0000 0.0000 0.0000 298 ILE B CA  
6251 C C   . ILE B 298 ? 161.7426 161.7426 161.7426 0.0000 0.0000 0.0000 298 ILE B C   
6252 O O   . ILE B 298 ? 161.4323 161.4323 161.4323 0.0000 0.0000 0.0000 298 ILE B O   
6253 C CB  . ILE B 298 ? 161.2473 161.2473 161.2473 0.0000 0.0000 0.0000 298 ILE B CB  
6254 C CG1 . ILE B 298 ? 161.2259 161.2259 161.2259 0.0000 0.0000 0.0000 298 ILE B CG1 
6255 C CG2 . ILE B 298 ? 161.4448 161.4448 161.4448 0.0000 0.0000 0.0000 298 ILE B CG2 
6256 C CD1 . ILE B 298 ? 161.6692 161.6692 161.6692 0.0000 0.0000 0.0000 298 ILE B CD1 
6257 N N   . ALA B 299 ? 161.2469 161.2469 161.2469 0.0000 0.0000 0.0000 299 ALA B N   
6258 C CA  . ALA B 299 ? 161.1049 161.1049 161.1049 0.0000 0.0000 0.0000 299 ALA B CA  
6259 C C   . ALA B 299 ? 161.2563 161.2563 161.2563 0.0000 0.0000 0.0000 299 ALA B C   
6260 O O   . ALA B 299 ? 161.2989 161.2989 161.2989 0.0000 0.0000 0.0000 299 ALA B O   
6261 C CB  . ALA B 299 ? 161.4134 161.4134 161.4134 0.0000 0.0000 0.0000 299 ALA B CB  
6262 N N   . PRO B 300 ? 161.3918 161.3918 161.3918 0.0000 0.0000 0.0000 300 PRO B N   
6263 C CA  . PRO B 300 ? 161.3799 161.3799 161.3799 0.0000 0.0000 0.0000 300 PRO B CA  
6264 C C   . PRO B 300 ? 161.5031 161.5031 161.5031 0.0000 0.0000 0.0000 300 PRO B C   
6265 O O   . PRO B 300 ? 161.3803 161.3803 161.3803 0.0000 0.0000 0.0000 300 PRO B O   
6266 C CB  . PRO B 300 ? 161.4093 161.4093 161.4093 0.0000 0.0000 0.0000 300 PRO B CB  
6267 C CG  . PRO B 300 ? 161.5420 161.5420 161.5420 0.0000 0.0000 0.0000 300 PRO B CG  
6268 C CD  . PRO B 300 ? 161.8015 161.8015 161.8015 0.0000 0.0000 0.0000 300 PRO B CD  
6269 N N   . GLU B 301 ? 161.4999 161.4999 161.4999 0.0000 0.0000 0.0000 301 GLU B N   
6270 C CA  . GLU B 301 ? 161.3615 161.3615 161.3615 0.0000 0.0000 0.0000 301 GLU B CA  
6271 C C   . GLU B 301 ? 161.3201 161.3201 161.3201 0.0000 0.0000 0.0000 301 GLU B C   
6272 O O   . GLU B 301 ? 161.5261 161.5261 161.5261 0.0000 0.0000 0.0000 301 GLU B O   
6273 C CB  . GLU B 301 ? 161.4734 161.4734 161.4734 0.0000 0.0000 0.0000 301 GLU B CB  
6274 C CG  . GLU B 301 ? 161.5686 161.5686 161.5686 0.0000 0.0000 0.0000 301 GLU B CG  
6275 C CD  . GLU B 301 ? 161.4739 161.4739 161.4739 0.0000 0.0000 0.0000 301 GLU B CD  
6276 O OE1 . GLU B 301 ? 161.1027 161.1027 161.1027 0.0000 0.0000 0.0000 301 GLU B OE1 
6277 O OE2 . GLU B 301 ? 161.1232 161.1232 161.1232 0.0000 0.0000 0.0000 301 GLU B OE2 
6278 N N   . LEU B 302 ? 161.4010 161.4010 161.4010 0.0000 0.0000 0.0000 302 LEU B N   
6279 C CA  . LEU B 302 ? 161.1729 161.1729 161.1729 0.0000 0.0000 0.0000 302 LEU B CA  
6280 C C   . LEU B 302 ? 161.1257 161.1257 161.1257 0.0000 0.0000 0.0000 302 LEU B C   
6281 O O   . LEU B 302 ? 161.0713 161.0713 161.0713 0.0000 0.0000 0.0000 302 LEU B O   
6282 C CB  . LEU B 302 ? 161.3551 161.3551 161.3551 0.0000 0.0000 0.0000 302 LEU B CB  
6283 C CG  . LEU B 302 ? 161.1369 161.1369 161.1369 0.0000 0.0000 0.0000 302 LEU B CG  
6284 C CD1 . LEU B 302 ? 161.3054 161.3054 161.3054 0.0000 0.0000 0.0000 302 LEU B CD1 
6285 C CD2 . LEU B 302 ? 161.2537 161.2537 161.2537 0.0000 0.0000 0.0000 302 LEU B CD2 
6286 N N   . TYR B 303 ? 161.4084 161.4084 161.4084 0.0000 0.0000 0.0000 303 TYR B N   
6287 C CA  . TYR B 303 ? 161.5911 161.5911 161.5911 0.0000 0.0000 0.0000 303 TYR B CA  
6288 C C   . TYR B 303 ? 161.3587 161.3587 161.3587 0.0000 0.0000 0.0000 303 TYR B C   
6289 O O   . TYR B 303 ? 161.4745 161.4745 161.4745 0.0000 0.0000 0.0000 303 TYR B O   
6290 C CB  . TYR B 303 ? 161.3531 161.3531 161.3531 0.0000 0.0000 0.0000 303 TYR B CB  
6291 C CG  . TYR B 303 ? 161.4589 161.4589 161.4589 0.0000 0.0000 0.0000 303 TYR B CG  
6292 C CD1 . TYR B 303 ? 161.5249 161.5249 161.5249 0.0000 0.0000 0.0000 303 TYR B CD1 
6293 C CD2 . TYR B 303 ? 161.4496 161.4496 161.4496 0.0000 0.0000 0.0000 303 TYR B CD2 
6294 C CE1 . TYR B 303 ? 161.5384 161.5384 161.5384 0.0000 0.0000 0.0000 303 TYR B CE1 
6295 C CE2 . TYR B 303 ? 161.6730 161.6730 161.6730 0.0000 0.0000 0.0000 303 TYR B CE2 
6296 C CZ  . TYR B 303 ? 161.4164 161.4164 161.4164 0.0000 0.0000 0.0000 303 TYR B CZ  
6297 O OH  . TYR B 303 ? 161.3143 161.3143 161.3143 0.0000 0.0000 0.0000 303 TYR B OH  
6298 N N   . HIS B 304 ? 161.4798 161.4798 161.4798 0.0000 0.0000 0.0000 304 HIS B N   
6299 C CA  . HIS B 304 ? 161.4105 161.4105 161.4105 0.0000 0.0000 0.0000 304 HIS B CA  
6300 C C   . HIS B 304 ? 161.5903 161.5903 161.5903 0.0000 0.0000 0.0000 304 HIS B C   
6301 O O   . HIS B 304 ? 161.2189 161.2189 161.2189 0.0000 0.0000 0.0000 304 HIS B O   
6302 C CB  . HIS B 304 ? 160.8351 160.8351 160.8351 0.0000 0.0000 0.0000 304 HIS B CB  
6303 C CG  . HIS B 304 ? 160.5580 160.5580 160.5580 0.0000 0.0000 0.0000 304 HIS B CG  
6304 N ND1 . HIS B 304 ? 160.8179 160.8179 160.8179 0.0000 0.0000 0.0000 304 HIS B ND1 
6305 C CD2 . HIS B 304 ? 159.9036 159.9036 159.9036 0.0000 0.0000 0.0000 304 HIS B CD2 
6306 C CE1 . HIS B 304 ? 161.4936 161.4936 161.4936 0.0000 0.0000 0.0000 304 HIS B CE1 
6307 N NE2 . HIS B 304 ? 160.9076 160.9076 160.9076 0.0000 0.0000 0.0000 304 HIS B NE2 
6308 N N   . LYS B 305 ? 160.3499 160.3499 160.3499 0.0000 0.0000 0.0000 305 LYS B N   
6309 C CA  . LYS B 305 ? 161.0372 161.0372 161.0372 0.0000 0.0000 0.0000 305 LYS B CA  
6310 C C   . LYS B 305 ? 161.1558 161.1558 161.1558 0.0000 0.0000 0.0000 305 LYS B C   
6311 O O   . LYS B 305 ? 160.7532 160.7532 160.7532 0.0000 0.0000 0.0000 305 LYS B O   
6312 C CB  . LYS B 305 ? 160.8190 160.8190 160.8190 0.0000 0.0000 0.0000 305 LYS B CB  
6313 C CG  . LYS B 305 ? 159.5874 159.5874 159.5874 0.0000 0.0000 0.0000 305 LYS B CG  
6314 C CD  . LYS B 305 ? 161.3049 161.3049 161.3049 0.0000 0.0000 0.0000 305 LYS B CD  
6315 C CE  . LYS B 305 ? 161.3856 161.3856 161.3856 0.0000 0.0000 0.0000 305 LYS B CE  
6316 N NZ  . LYS B 305 ? 161.3905 161.3905 161.3905 0.0000 0.0000 0.0000 305 LYS B NZ  
6317 N N   . MET B 306 ? 161.4612 161.4612 161.4612 0.0000 0.0000 0.0000 306 MET B N   
6318 C CA  . MET B 306 ? 161.4023 161.4023 161.4023 0.0000 0.0000 0.0000 306 MET B CA  
6319 C C   . MET B 306 ? 161.4387 161.4387 161.4387 0.0000 0.0000 0.0000 306 MET B C   
6320 O O   . MET B 306 ? 161.4941 161.4941 161.4941 0.0000 0.0000 0.0000 306 MET B O   
6321 C CB  . MET B 306 ? 161.6725 161.6725 161.6725 0.0000 0.0000 0.0000 306 MET B CB  
6322 C CG  . MET B 306 ? 161.2797 161.2797 161.2797 0.0000 0.0000 0.0000 306 MET B CG  
6323 S SD  . MET B 306 ? 161.2769 161.2769 161.2769 0.0000 0.0000 0.0000 306 MET B SD  
6324 C CE  . MET B 306 ? 161.2656 161.2656 161.2656 0.0000 0.0000 0.0000 306 MET B CE  
6325 N N   . LEU B 307 ? 161.3911 161.3911 161.3911 0.0000 0.0000 0.0000 307 LEU B N   
6326 C CA  . LEU B 307 ? 161.3632 161.3632 161.3632 0.0000 0.0000 0.0000 307 LEU B CA  
6327 C C   . LEU B 307 ? 161.4486 161.4486 161.4486 0.0000 0.0000 0.0000 307 LEU B C   
6328 O O   . LEU B 307 ? 161.3283 161.3283 161.3283 0.0000 0.0000 0.0000 307 LEU B O   
6329 C CB  . LEU B 307 ? 161.5750 161.5750 161.5750 0.0000 0.0000 0.0000 307 LEU B CB  
6330 C CG  . LEU B 307 ? 161.1234 161.1234 161.1234 0.0000 0.0000 0.0000 307 LEU B CG  
6331 C CD1 . LEU B 307 ? 161.2008 161.2008 161.2008 0.0000 0.0000 0.0000 307 LEU B CD1 
6332 C CD2 . LEU B 307 ? 161.3398 161.3398 161.3398 0.0000 0.0000 0.0000 307 LEU B CD2 
6333 N N   . VAL B 308 ? 161.4107 161.4107 161.4107 0.0000 0.0000 0.0000 308 VAL B N   
6334 C CA  . VAL B 308 ? 161.1021 161.1021 161.1021 0.0000 0.0000 0.0000 308 VAL B CA  
6335 C C   . VAL B 308 ? 161.1327 161.1327 161.1327 0.0000 0.0000 0.0000 308 VAL B C   
6336 O O   . VAL B 308 ? 161.3248 161.3248 161.3248 0.0000 0.0000 0.0000 308 VAL B O   
6337 C CB  . VAL B 308 ? 161.1950 161.1950 161.1950 0.0000 0.0000 0.0000 308 VAL B CB  
6338 C CG1 . VAL B 308 ? 161.3683 161.3683 161.3683 0.0000 0.0000 0.0000 308 VAL B CG1 
6339 C CG2 . VAL B 308 ? 161.2056 161.2056 161.2056 0.0000 0.0000 0.0000 308 VAL B CG2 
6340 N N   . VAL B 309 ? 161.2283 161.2283 161.2283 0.0000 0.0000 0.0000 309 VAL B N   
6341 C CA  . VAL B 309 ? 161.4184 161.4184 161.4184 0.0000 0.0000 0.0000 309 VAL B CA  
6342 C C   . VAL B 309 ? 161.2224 161.2224 161.2224 0.0000 0.0000 0.0000 309 VAL B C   
6343 O O   . VAL B 309 ? 161.1930 161.1930 161.1930 0.0000 0.0000 0.0000 309 VAL B O   
6344 C CB  . VAL B 309 ? 160.4961 160.4961 160.4961 0.0000 0.0000 0.0000 309 VAL B CB  
6345 C CG1 . VAL B 309 ? 159.4301 159.4301 159.4301 0.0000 0.0000 0.0000 309 VAL B CG1 
6346 C CG2 . VAL B 309 ? 158.7976 158.7976 158.7976 0.0000 0.0000 0.0000 309 VAL B CG2 
6347 N N   . GLY B 310 ? 159.3822 159.3822 159.3822 0.0000 0.0000 0.0000 310 GLY B N   
6348 C CA  . GLY B 310 ? 155.0900 155.0900 155.0900 0.0000 0.0000 0.0000 310 GLY B CA  
6349 C C   . GLY B 310 ? 161.1597 161.1597 161.1597 0.0000 0.0000 0.0000 310 GLY B C   
6350 O O   . GLY B 310 ? 161.0873 161.0873 161.0873 0.0000 0.0000 0.0000 310 GLY B O   
6351 N N   . GLY B 311 ? 161.2581 161.2581 161.2581 0.0000 0.0000 0.0000 311 GLY B N   
6352 C CA  . GLY B 311 ? 161.5471 161.5471 161.5471 0.0000 0.0000 0.0000 311 GLY B CA  
6353 C C   . GLY B 311 ? 161.0158 161.0158 161.0158 0.0000 0.0000 0.0000 311 GLY B C   
6354 O O   . GLY B 311 ? 161.2629 161.2629 161.2629 0.0000 0.0000 0.0000 311 GLY B O   
6355 N N   . ILE B 312 ? 161.3703 161.3703 161.3703 0.0000 0.0000 0.0000 312 ILE B N   
6356 C CA  . ILE B 312 ? 161.2396 161.2396 161.2396 0.0000 0.0000 0.0000 312 ILE B CA  
6357 C C   . ILE B 312 ? 161.1638 161.1638 161.1638 0.0000 0.0000 0.0000 312 ILE B C   
6358 O O   . ILE B 312 ? 161.1382 161.1382 161.1382 0.0000 0.0000 0.0000 312 ILE B O   
6359 C CB  . ILE B 312 ? 161.4344 161.4344 161.4344 0.0000 0.0000 0.0000 312 ILE B CB  
6360 C CG1 . ILE B 312 ? 161.2475 161.2475 161.2475 0.0000 0.0000 0.0000 312 ILE B CG1 
6361 C CG2 . ILE B 312 ? 161.2018 161.2018 161.2018 0.0000 0.0000 0.0000 312 ILE B CG2 
6362 C CD1 . ILE B 312 ? 161.6017 161.6017 161.6017 0.0000 0.0000 0.0000 312 ILE B CD1 
6363 N N   . ASP B 313 ? 161.2503 161.2503 161.2503 0.0000 0.0000 0.0000 313 ASP B N   
6364 C CA  . ASP B 313 ? 161.6998 161.6998 161.6998 0.0000 0.0000 0.0000 313 ASP B CA  
6365 C C   . ASP B 313 ? 161.4439 161.4439 161.4439 0.0000 0.0000 0.0000 313 ASP B C   
6366 O O   . ASP B 313 ? 161.5019 161.5019 161.5019 0.0000 0.0000 0.0000 313 ASP B O   
6367 C CB  . ASP B 313 ? 161.5337 161.5337 161.5337 0.0000 0.0000 0.0000 313 ASP B CB  
6368 C CG  . ASP B 313 ? 161.0508 161.0508 161.0508 0.0000 0.0000 0.0000 313 ASP B CG  
6369 O OD1 . ASP B 313 ? 161.1818 161.1818 161.1818 0.0000 0.0000 0.0000 313 ASP B OD1 
6370 O OD2 . ASP B 313 ? 161.3307 161.3307 161.3307 0.0000 0.0000 0.0000 313 ASP B OD2 
6371 N N   . ARG B 314 ? 161.5858 161.5858 161.5858 0.0000 0.0000 0.0000 314 ARG B N   
6372 C CA  . ARG B 314 ? 161.2157 161.2157 161.2157 0.0000 0.0000 0.0000 314 ARG B CA  
6373 C C   . ARG B 314 ? 161.3656 161.3656 161.3656 0.0000 0.0000 0.0000 314 ARG B C   
6374 O O   . ARG B 314 ? 161.4667 161.4667 161.4667 0.0000 0.0000 0.0000 314 ARG B O   
6375 C CB  . ARG B 314 ? 161.5476 161.5476 161.5476 0.0000 0.0000 0.0000 314 ARG B CB  
6376 C CG  . ARG B 314 ? 161.5792 161.5792 161.5792 0.0000 0.0000 0.0000 314 ARG B CG  
6377 C CD  . ARG B 314 ? 161.3007 161.3007 161.3007 0.0000 0.0000 0.0000 314 ARG B CD  
6378 N NE  . ARG B 314 ? 161.2349 161.2349 161.2349 0.0000 0.0000 0.0000 314 ARG B NE  
6379 C CZ  . ARG B 314 ? 161.2790 161.2790 161.2790 0.0000 0.0000 0.0000 314 ARG B CZ  
6380 N NH1 . ARG B 314 ? 161.2788 161.2788 161.2788 0.0000 0.0000 0.0000 314 ARG B NH1 
6381 N NH2 . ARG B 314 ? 160.9367 160.9367 160.9367 0.0000 0.0000 0.0000 314 ARG B NH2 
6382 N N   . VAL B 315 ? 161.0991 161.0991 161.0991 0.0000 0.0000 0.0000 315 VAL B N   
6383 C CA  . VAL B 315 ? 161.1137 161.1137 161.1137 0.0000 0.0000 0.0000 315 VAL B CA  
6384 C C   . VAL B 315 ? 161.1871 161.1871 161.1871 0.0000 0.0000 0.0000 315 VAL B C   
6385 O O   . VAL B 315 ? 161.3011 161.3011 161.3011 0.0000 0.0000 0.0000 315 VAL B O   
6386 C CB  . VAL B 315 ? 161.2773 161.2773 161.2773 0.0000 0.0000 0.0000 315 VAL B CB  
6387 C CG1 . VAL B 315 ? 161.3260 161.3260 161.3260 0.0000 0.0000 0.0000 315 VAL B CG1 
6388 C CG2 . VAL B 315 ? 161.5249 161.5249 161.5249 0.0000 0.0000 0.0000 315 VAL B CG2 
6389 N N   . TYR B 316 ? 161.2043 161.2043 161.2043 0.0000 0.0000 0.0000 316 TYR B N   
6390 C CA  . TYR B 316 ? 161.2148 161.2148 161.2148 0.0000 0.0000 0.0000 316 TYR B CA  
6391 C C   . TYR B 316 ? 161.2773 161.2773 161.2773 0.0000 0.0000 0.0000 316 TYR B C   
6392 O O   . TYR B 316 ? 161.5228 161.5228 161.5228 0.0000 0.0000 0.0000 316 TYR B O   
6393 C CB  . TYR B 316 ? 161.3787 161.3787 161.3787 0.0000 0.0000 0.0000 316 TYR B CB  
6394 C CG  . TYR B 316 ? 161.5447 161.5447 161.5447 0.0000 0.0000 0.0000 316 TYR B CG  
6395 C CD1 . TYR B 316 ? 161.4686 161.4686 161.4686 0.0000 0.0000 0.0000 316 TYR B CD1 
6396 C CD2 . TYR B 316 ? 161.3518 161.3518 161.3518 0.0000 0.0000 0.0000 316 TYR B CD2 
6397 C CE1 . TYR B 316 ? 161.4534 161.4534 161.4534 0.0000 0.0000 0.0000 316 TYR B CE1 
6398 C CE2 . TYR B 316 ? 161.5527 161.5527 161.5527 0.0000 0.0000 0.0000 316 TYR B CE2 
6399 C CZ  . TYR B 316 ? 161.4972 161.4972 161.4972 0.0000 0.0000 0.0000 316 TYR B CZ  
6400 O OH  . TYR B 316 ? 161.2121 161.2121 161.2121 0.0000 0.0000 0.0000 316 TYR B OH  
6401 N N   . GLU B 317 ? 161.2819 161.2819 161.2819 0.0000 0.0000 0.0000 317 GLU B N   
6402 C CA  . GLU B 317 ? 161.4286 161.4286 161.4286 0.0000 0.0000 0.0000 317 GLU B CA  
6403 C C   . GLU B 317 ? 161.8004 161.8004 161.8004 0.0000 0.0000 0.0000 317 GLU B C   
6404 O O   . GLU B 317 ? 161.4143 161.4143 161.4143 0.0000 0.0000 0.0000 317 GLU B O   
6405 C CB  . GLU B 317 ? 161.5031 161.5031 161.5031 0.0000 0.0000 0.0000 317 GLU B CB  
6406 C CG  . GLU B 317 ? 161.6163 161.6163 161.6163 0.0000 0.0000 0.0000 317 GLU B CG  
6407 C CD  . GLU B 317 ? 161.7186 161.7186 161.7186 0.0000 0.0000 0.0000 317 GLU B CD  
6408 O OE1 . GLU B 317 ? 161.6392 161.6392 161.6392 0.0000 0.0000 0.0000 317 GLU B OE1 
6409 O OE2 . GLU B 317 ? 161.3872 161.3872 161.3872 0.0000 0.0000 0.0000 317 GLU B OE2 
6410 N N   . ILE B 318 ? 161.3957 161.3957 161.3957 0.0000 0.0000 0.0000 318 ILE B N   
6411 C CA  . ILE B 318 ? 161.6759 161.6759 161.6759 0.0000 0.0000 0.0000 318 ILE B CA  
6412 C C   . ILE B 318 ? 161.7857 161.7857 161.7857 0.0000 0.0000 0.0000 318 ILE B C   
6413 O O   . ILE B 318 ? 161.2883 161.2883 161.2883 0.0000 0.0000 0.0000 318 ILE B O   
6414 C CB  . ILE B 318 ? 161.2401 161.2401 161.2401 0.0000 0.0000 0.0000 318 ILE B CB  
6415 C CG1 . ILE B 318 ? 161.4292 161.4292 161.4292 0.0000 0.0000 0.0000 318 ILE B CG1 
6416 C CG2 . ILE B 318 ? 161.3750 161.3750 161.3750 0.0000 0.0000 0.0000 318 ILE B CG2 
6417 C CD1 . ILE B 318 ? 161.4436 161.4436 161.4436 0.0000 0.0000 0.0000 318 ILE B CD1 
6418 N N   . GLY B 319 ? 161.3888 161.3888 161.3888 0.0000 0.0000 0.0000 319 GLY B N   
6419 C CA  . GLY B 319 ? 161.3616 161.3616 161.3616 0.0000 0.0000 0.0000 319 GLY B CA  
6420 C C   . GLY B 319 ? 169.2222 169.2222 169.2222 0.0000 0.0000 0.0000 319 GLY B C   
6421 O O   . GLY B 319 ? 169.3899 169.3899 169.3899 0.0000 0.0000 0.0000 319 GLY B O   
6422 N N   . ARG B 320 ? 169.4222 169.4222 169.4222 0.0000 0.0000 0.0000 320 ARG B N   
6423 C CA  . ARG B 320 ? 169.7449 169.7449 169.7449 0.0000 0.0000 0.0000 320 ARG B CA  
6424 C C   . ARG B 320 ? 169.4422 169.4422 169.4422 0.0000 0.0000 0.0000 320 ARG B C   
6425 O O   . ARG B 320 ? 169.7268 169.7268 169.7268 0.0000 0.0000 0.0000 320 ARG B O   
6426 C CB  . ARG B 320 ? 168.8452 168.8452 168.8452 0.0000 0.0000 0.0000 320 ARG B CB  
6427 C CG  . ARG B 320 ? 168.9720 168.9720 168.9720 0.0000 0.0000 0.0000 320 ARG B CG  
6428 C CD  . ARG B 320 ? 169.2040 169.2040 169.2040 0.0000 0.0000 0.0000 320 ARG B CD  
6429 N NE  . ARG B 320 ? 169.7500 169.7500 169.7500 0.0000 0.0000 0.0000 320 ARG B NE  
6430 C CZ  . ARG B 320 ? 168.9895 168.9895 168.9895 0.0000 0.0000 0.0000 320 ARG B CZ  
6431 N NH1 . ARG B 320 ? 161.8348 161.8348 161.8348 0.0000 0.0000 0.0000 320 ARG B NH1 
6432 N NH2 . ARG B 320 ? 161.8135 161.8135 161.8135 0.0000 0.0000 0.0000 320 ARG B NH2 
6433 N N   . GLN B 321 ? 162.4877 162.4877 162.4877 0.0000 0.0000 0.0000 321 GLN B N   
6434 C CA  . GLN B 321 ? 162.3289 162.3289 162.3289 0.0000 0.0000 0.0000 321 GLN B CA  
6435 C C   . GLN B 321 ? 161.5444 161.5444 161.5444 0.0000 0.0000 0.0000 321 GLN B C   
6436 O O   . GLN B 321 ? 161.5669 161.5669 161.5669 0.0000 0.0000 0.0000 321 GLN B O   
6437 C CB  . GLN B 321 ? 161.9027 161.9027 161.9027 0.0000 0.0000 0.0000 321 GLN B CB  
6438 C CG  . GLN B 321 ? 161.7465 161.7465 161.7465 0.0000 0.0000 0.0000 321 GLN B CG  
6439 C CD  . GLN B 321 ? 189.8057 189.8057 189.8057 0.0000 0.0000 0.0000 321 GLN B CD  
6440 O OE1 . GLN B 321 ? 190.5310 190.5310 190.5310 0.0000 0.0000 0.0000 321 GLN B OE1 
6441 N NE2 . GLN B 321 ? 190.7106 190.7106 190.7106 0.0000 0.0000 0.0000 321 GLN B NE2 
6442 N N   . PHE B 322 ? 190.6562 190.6562 190.6562 0.0000 0.0000 0.0000 322 PHE B N   
6443 C CA  . PHE B 322 ? 190.7405 190.7405 190.7405 0.0000 0.0000 0.0000 322 PHE B CA  
6444 C C   . PHE B 322 ? 190.4810 190.4810 190.4810 0.0000 0.0000 0.0000 322 PHE B C   
6445 O O   . PHE B 322 ? 190.2273 190.2273 190.2273 0.0000 0.0000 0.0000 322 PHE B O   
6446 C CB  . PHE B 322 ? 190.2522 190.2522 190.2522 0.0000 0.0000 0.0000 322 PHE B CB  
6447 C CG  . PHE B 322 ? 190.2211 190.2211 190.2211 0.0000 0.0000 0.0000 322 PHE B CG  
6448 C CD1 . PHE B 322 ? 191.4504 191.4504 191.4504 0.0000 0.0000 0.0000 322 PHE B CD1 
6449 C CD2 . PHE B 322 ? 191.6591 191.6591 191.6591 0.0000 0.0000 0.0000 322 PHE B CD2 
6450 C CE1 . PHE B 322 ? 191.6090 191.6090 191.6090 0.0000 0.0000 0.0000 322 PHE B CE1 
6451 C CE2 . PHE B 322 ? 191.6467 191.6467 191.6467 0.0000 0.0000 0.0000 322 PHE B CE2 
6452 C CZ  . PHE B 322 ? 189.2076 189.2076 189.2076 0.0000 0.0000 0.0000 322 PHE B CZ  
6453 N N   . ARG B 323 ? 189.1427 189.1427 189.1427 0.0000 0.0000 0.0000 323 ARG B N   
6454 C CA  . ARG B 323 ? 188.8556 188.8556 188.8556 0.0000 0.0000 0.0000 323 ARG B CA  
6455 C C   . ARG B 323 ? 188.6753 188.6753 188.6753 0.0000 0.0000 0.0000 323 ARG B C   
6456 O O   . ARG B 323 ? 188.8541 188.8541 188.8541 0.0000 0.0000 0.0000 323 ARG B O   
6457 C CB  . ARG B 323 ? 188.6441 188.6441 188.6441 0.0000 0.0000 0.0000 323 ARG B CB  
6458 C CG  . ARG B 323 ? 187.8638 187.8638 187.8638 0.0000 0.0000 0.0000 323 ARG B CG  
6459 C CD  . ARG B 323 ? 188.1953 188.1953 188.1953 0.0000 0.0000 0.0000 323 ARG B CD  
6460 N NE  . ARG B 323 ? 194.6830 194.6830 194.6830 0.0000 0.0000 0.0000 323 ARG B NE  
6461 C CZ  . ARG B 323 ? 194.8347 194.8347 194.8347 0.0000 0.0000 0.0000 323 ARG B CZ  
6462 N NH1 . ARG B 323 ? 194.2604 194.2604 194.2604 0.0000 0.0000 0.0000 323 ARG B NH1 
6463 N NH2 . ARG B 323 ? 193.8157 193.8157 193.8157 0.0000 0.0000 0.0000 323 ARG B NH2 
6464 N N   . ASN B 324 ? 195.0396 195.0396 195.0396 0.0000 0.0000 0.0000 324 ASN B N   
6465 C CA  . ASN B 324 ? 194.8587 194.8587 194.8587 0.0000 0.0000 0.0000 324 ASN B CA  
6466 C C   . ASN B 324 ? 194.5738 194.5738 194.5738 0.0000 0.0000 0.0000 324 ASN B C   
6467 O O   . ASN B 324 ? 195.0599 195.0599 195.0599 0.0000 0.0000 0.0000 324 ASN B O   
6468 C CB  . ASN B 324 ? 187.4715 187.4715 187.4715 0.0000 0.0000 0.0000 324 ASN B CB  
6469 C CG  . ASN B 324 ? 186.5620 186.5620 186.5620 0.0000 0.0000 0.0000 324 ASN B CG  
6470 O OD1 . ASN B 324 ? 185.7741 185.7741 185.7741 0.0000 0.0000 0.0000 324 ASN B OD1 
6471 N ND2 . ASN B 324 ? 183.4796 183.4796 183.4796 0.0000 0.0000 0.0000 324 ASN B ND2 
6472 N N   . GLU B 325 ? 186.7161 186.7161 186.7161 0.0000 0.0000 0.0000 325 GLU B N   
6473 C CA  . GLU B 325 ? 186.7780 186.7780 186.7780 0.0000 0.0000 0.0000 325 GLU B CA  
6474 C C   . GLU B 325 ? 186.8401 186.8401 186.8401 0.0000 0.0000 0.0000 325 GLU B C   
6475 O O   . GLU B 325 ? 185.6801 185.6801 185.6801 0.0000 0.0000 0.0000 325 GLU B O   
6476 C CB  . GLU B 325 ? 181.5608 181.5608 181.5608 0.0000 0.0000 0.0000 325 GLU B CB  
6477 C CG  . GLU B 325 ? 181.4940 181.4940 181.4940 0.0000 0.0000 0.0000 325 GLU B CG  
6478 C CD  . GLU B 325 ? 181.0306 181.0306 181.0306 0.0000 0.0000 0.0000 325 GLU B CD  
6479 O OE1 . GLU B 325 ? 180.1927 180.1927 180.1927 0.0000 0.0000 0.0000 325 GLU B OE1 
6480 O OE2 . GLU B 325 ? 182.1805 182.1805 182.1805 0.0000 0.0000 0.0000 325 GLU B OE2 
6481 N N   . GLY B 326 ? 182.2294 182.2294 182.2294 0.0000 0.0000 0.0000 326 GLY B N   
6482 C CA  . GLY B 326 ? 181.1827 181.1827 181.1827 0.0000 0.0000 0.0000 326 GLY B CA  
6483 C C   . GLY B 326 ? 185.0060 185.0060 185.0060 0.0000 0.0000 0.0000 326 GLY B C   
6484 O O   . GLY B 326 ? 184.2821 184.2821 184.2821 0.0000 0.0000 0.0000 326 GLY B O   
6485 N N   . ILE B 327 ? 184.1251 184.1251 184.1251 0.0000 0.0000 0.0000 327 ILE B N   
6486 C CA  . ILE B 327 ? 185.2572 185.2572 185.2572 0.0000 0.0000 0.0000 327 ILE B CA  
6487 C C   . ILE B 327 ? 185.2929 185.2929 185.2929 0.0000 0.0000 0.0000 327 ILE B C   
6488 O O   . ILE B 327 ? 185.4256 185.4256 185.4256 0.0000 0.0000 0.0000 327 ILE B O   
6489 C CB  . ILE B 327 ? 186.4300 186.4300 186.4300 0.0000 0.0000 0.0000 327 ILE B CB  
6490 C CG1 . ILE B 327 ? 184.1549 184.1549 184.1549 0.0000 0.0000 0.0000 327 ILE B CG1 
6491 C CG2 . ILE B 327 ? 186.3730 186.3730 186.3730 0.0000 0.0000 0.0000 327 ILE B CG2 
6492 C CD1 . ILE B 327 ? 185.5223 185.5223 185.5223 0.0000 0.0000 0.0000 327 ILE B CD1 
6493 N N   . ASP B 328 ? 160.5729 160.5729 160.5729 0.0000 0.0000 0.0000 328 ASP B N   
6494 C CA  . ASP B 328 ? 160.9748 160.9748 160.9748 0.0000 0.0000 0.0000 328 ASP B CA  
6495 C C   . ASP B 328 ? 160.9709 160.9709 160.9709 0.0000 0.0000 0.0000 328 ASP B C   
6496 O O   . ASP B 328 ? 160.4533 160.4533 160.4533 0.0000 0.0000 0.0000 328 ASP B O   
6497 C CB  . ASP B 328 ? 160.3874 160.3874 160.3874 0.0000 0.0000 0.0000 328 ASP B CB  
6498 C CG  . ASP B 328 ? 159.8273 159.8273 159.8273 0.0000 0.0000 0.0000 328 ASP B CG  
6499 O OD1 . ASP B 328 ? 158.8237 158.8237 158.8237 0.0000 0.0000 0.0000 328 ASP B OD1 
6500 O OD2 . ASP B 328 ? 159.4660 159.4660 159.4660 0.0000 0.0000 0.0000 328 ASP B OD2 
6501 N N   . LEU B 329 ? 161.3240 161.3240 161.3240 0.0000 0.0000 0.0000 329 LEU B N   
6502 C CA  . LEU B 329 ? 161.2910 161.2910 161.2910 0.0000 0.0000 0.0000 329 LEU B CA  
6503 C C   . LEU B 329 ? 161.4874 161.4874 161.4874 0.0000 0.0000 0.0000 329 LEU B C   
6504 O O   . LEU B 329 ? 161.7396 161.7396 161.7396 0.0000 0.0000 0.0000 329 LEU B O   
6505 C CB  . LEU B 329 ? 161.3491 161.3491 161.3491 0.0000 0.0000 0.0000 329 LEU B CB  
6506 C CG  . LEU B 329 ? 161.1887 161.1887 161.1887 0.0000 0.0000 0.0000 329 LEU B CG  
6507 C CD1 . LEU B 329 ? 161.4916 161.4916 161.4916 0.0000 0.0000 0.0000 329 LEU B CD1 
6508 C CD2 . LEU B 329 ? 161.3867 161.3867 161.3867 0.0000 0.0000 0.0000 329 LEU B CD2 
6509 N N   . THR B 330 ? 161.4166 161.4166 161.4166 0.0000 0.0000 0.0000 330 THR B N   
6510 C CA  . THR B 330 ? 161.3746 161.3746 161.3746 0.0000 0.0000 0.0000 330 THR B CA  
6511 C C   . THR B 330 ? 161.3397 161.3397 161.3397 0.0000 0.0000 0.0000 330 THR B C   
6512 O O   . THR B 330 ? 161.2971 161.2971 161.2971 0.0000 0.0000 0.0000 330 THR B O   
6513 C CB  . THR B 330 ? 161.4407 161.4407 161.4407 0.0000 0.0000 0.0000 330 THR B CB  
6514 O OG1 . THR B 330 ? 161.5540 161.5540 161.5540 0.0000 0.0000 0.0000 330 THR B OG1 
6515 C CG2 . THR B 330 ? 161.4709 161.4709 161.4709 0.0000 0.0000 0.0000 330 THR B CG2 
6516 N N   . HIS B 331 ? 161.7555 161.7555 161.7555 0.0000 0.0000 0.0000 331 HIS B N   
6517 C CA  . HIS B 331 ? 161.3150 161.3150 161.3150 0.0000 0.0000 0.0000 331 HIS B CA  
6518 C C   . HIS B 331 ? 160.4447 160.4447 160.4447 0.0000 0.0000 0.0000 331 HIS B C   
6519 O O   . HIS B 331 ? 160.6457 160.6457 160.6457 0.0000 0.0000 0.0000 331 HIS B O   
6520 C CB  . HIS B 331 ? 161.3631 161.3631 161.3631 0.0000 0.0000 0.0000 331 HIS B CB  
6521 C CG  . HIS B 331 ? 159.6016 159.6016 159.6016 0.0000 0.0000 0.0000 331 HIS B CG  
6522 N ND1 . HIS B 331 ? 159.5297 159.5297 159.5297 0.0000 0.0000 0.0000 331 HIS B ND1 
6523 C CD2 . HIS B 331 ? 159.6871 159.6871 159.6871 0.0000 0.0000 0.0000 331 HIS B CD2 
6524 C CE1 . HIS B 331 ? 159.6276 159.6276 159.6276 0.0000 0.0000 0.0000 331 HIS B CE1 
6525 N NE2 . HIS B 331 ? 159.8753 159.8753 159.8753 0.0000 0.0000 0.0000 331 HIS B NE2 
6526 N N   . ASN B 332 ? 160.0300 160.0300 160.0300 0.0000 0.0000 0.0000 332 ASN B N   
6527 C CA  . ASN B 332 ? 160.0356 160.0356 160.0356 0.0000 0.0000 0.0000 332 ASN B CA  
6528 C C   . ASN B 332 ? 160.2159 160.2159 160.2159 0.0000 0.0000 0.0000 332 ASN B C   
6529 O O   . ASN B 332 ? 160.4109 160.4109 160.4109 0.0000 0.0000 0.0000 332 ASN B O   
6530 C CB  . ASN B 332 ? 159.5419 159.5419 159.5419 0.0000 0.0000 0.0000 332 ASN B CB  
6531 C CG  . ASN B 332 ? 157.3524 157.3524 157.3524 0.0000 0.0000 0.0000 332 ASN B CG  
6532 O OD1 . ASN B 332 ? 160.2586 160.2586 160.2586 0.0000 0.0000 0.0000 332 ASN B OD1 
6533 N ND2 . ASN B 332 ? 160.8774 160.8774 160.8774 0.0000 0.0000 0.0000 332 ASN B ND2 
6534 N N   . PRO B 333 ? 160.9803 160.9803 160.9803 0.0000 0.0000 0.0000 333 PRO B N   
6535 C CA  . PRO B 333 ? 160.5086 160.5086 160.5086 0.0000 0.0000 0.0000 333 PRO B CA  
6536 C C   . PRO B 333 ? 159.2724 159.2724 159.2724 0.0000 0.0000 0.0000 333 PRO B C   
6537 O O   . PRO B 333 ? 160.1282 160.1282 160.1282 0.0000 0.0000 0.0000 333 PRO B O   
6538 C CB  . PRO B 333 ? 160.9771 160.9771 160.9771 0.0000 0.0000 0.0000 333 PRO B CB  
6539 C CG  . PRO B 333 ? 160.3919 160.3919 160.3919 0.0000 0.0000 0.0000 333 PRO B CG  
6540 C CD  . PRO B 333 ? 161.3705 161.3705 161.3705 0.0000 0.0000 0.0000 333 PRO B CD  
6541 N N   . GLU B 334 ? 160.2108 160.2108 160.2108 0.0000 0.0000 0.0000 334 GLU B N   
6542 C CA  . GLU B 334 ? 159.3754 159.3754 159.3754 0.0000 0.0000 0.0000 334 GLU B CA  
6543 C C   . GLU B 334 ? 160.1841 160.1841 160.1841 0.0000 0.0000 0.0000 334 GLU B C   
6544 O O   . GLU B 334 ? 159.6882 159.6882 159.6882 0.0000 0.0000 0.0000 334 GLU B O   
6545 C CB  . GLU B 334 ? 157.3428 157.3428 157.3428 0.0000 0.0000 0.0000 334 GLU B CB  
6546 C CG  . GLU B 334 ? 159.6661 159.6661 159.6661 0.0000 0.0000 0.0000 334 GLU B CG  
6547 C CD  . GLU B 334 ? 160.1933 160.1933 160.1933 0.0000 0.0000 0.0000 334 GLU B CD  
6548 O OE1 . GLU B 334 ? 160.9634 160.9634 160.9634 0.0000 0.0000 0.0000 334 GLU B OE1 
6549 O OE2 . GLU B 334 ? 160.0216 160.0216 160.0216 0.0000 0.0000 0.0000 334 GLU B OE2 
6550 N N   . PHE B 335 ? 160.6054 160.6054 160.6054 0.0000 0.0000 0.0000 335 PHE B N   
6551 C CA  . PHE B 335 ? 161.4652 161.4652 161.4652 0.0000 0.0000 0.0000 335 PHE B CA  
6552 C C   . PHE B 335 ? 160.9794 160.9794 160.9794 0.0000 0.0000 0.0000 335 PHE B C   
6553 O O   . PHE B 335 ? 160.5919 160.5919 160.5919 0.0000 0.0000 0.0000 335 PHE B O   
6554 C CB  . PHE B 335 ? 159.7880 159.7880 159.7880 0.0000 0.0000 0.0000 335 PHE B CB  
6555 C CG  . PHE B 335 ? 160.1511 160.1511 160.1511 0.0000 0.0000 0.0000 335 PHE B CG  
6556 C CD1 . PHE B 335 ? 159.4836 159.4836 159.4836 0.0000 0.0000 0.0000 335 PHE B CD1 
6557 C CD2 . PHE B 335 ? 159.5168 159.5168 159.5168 0.0000 0.0000 0.0000 335 PHE B CD2 
6558 C CE1 . PHE B 335 ? 160.2842 160.2842 160.2842 0.0000 0.0000 0.0000 335 PHE B CE1 
6559 C CE2 . PHE B 335 ? 159.5829 159.5829 159.5829 0.0000 0.0000 0.0000 335 PHE B CE2 
6560 C CZ  . PHE B 335 ? 158.2544 158.2544 158.2544 0.0000 0.0000 0.0000 335 PHE B CZ  
6561 N N   . THR B 336 ? 160.6480 160.6480 160.6480 0.0000 0.0000 0.0000 336 THR B N   
6562 C CA  . THR B 336 ? 159.6512 159.6512 159.6512 0.0000 0.0000 0.0000 336 THR B CA  
6563 C C   . THR B 336 ? 160.4070 160.4070 160.4070 0.0000 0.0000 0.0000 336 THR B C   
6564 O O   . THR B 336 ? 159.0654 159.0654 159.0654 0.0000 0.0000 0.0000 336 THR B O   
6565 C CB  . THR B 336 ? 160.7767 160.7767 160.7767 0.0000 0.0000 0.0000 336 THR B CB  
6566 O OG1 . THR B 336 ? 159.2459 159.2459 159.2459 0.0000 0.0000 0.0000 336 THR B OG1 
6567 C CG2 . THR B 336 ? 160.2401 160.2401 160.2401 0.0000 0.0000 0.0000 336 THR B CG2 
6568 N N   . THR B 337 ? 160.8561 160.8561 160.8561 0.0000 0.0000 0.0000 337 THR B N   
6569 C CA  . THR B 337 ? 160.1696 160.1696 160.1696 0.0000 0.0000 0.0000 337 THR B CA  
6570 C C   . THR B 337 ? 160.6629 160.6629 160.6629 0.0000 0.0000 0.0000 337 THR B C   
6571 O O   . THR B 337 ? 161.3494 161.3494 161.3494 0.0000 0.0000 0.0000 337 THR B O   
6572 C CB  . THR B 337 ? 160.8439 160.8439 160.8439 0.0000 0.0000 0.0000 337 THR B CB  
6573 O OG1 . THR B 337 ? 160.3245 160.3245 160.3245 0.0000 0.0000 0.0000 337 THR B OG1 
6574 C CG2 . THR B 337 ? 161.1739 161.1739 161.1739 0.0000 0.0000 0.0000 337 THR B CG2 
6575 N N   . CYS B 338 ? 159.7558 159.7558 159.7558 0.0000 0.0000 0.0000 338 CYS B N   
6576 C CA  . CYS B 338 ? 160.3923 160.3923 160.3923 0.0000 0.0000 0.0000 338 CYS B CA  
6577 C C   . CYS B 338 ? 159.7097 159.7097 159.7097 0.0000 0.0000 0.0000 338 CYS B C   
6578 O O   . CYS B 338 ? 159.7781 159.7781 159.7781 0.0000 0.0000 0.0000 338 CYS B O   
6579 C CB  . CYS B 338 ? 159.7202 159.7202 159.7202 0.0000 0.0000 0.0000 338 CYS B CB  
6580 S SG  . CYS B 338 ? 159.9293 159.9293 159.9293 0.0000 0.0000 0.0000 338 CYS B SG  
6581 N N   . GLU B 339 ? 160.5290 160.5290 160.5290 0.0000 0.0000 0.0000 339 GLU B N   
6582 C CA  . GLU B 339 ? 159.4918 159.4918 159.4918 0.0000 0.0000 0.0000 339 GLU B CA  
6583 C C   . GLU B 339 ? 157.6700 157.6700 157.6700 0.0000 0.0000 0.0000 339 GLU B C   
6584 O O   . GLU B 339 ? 160.8262 160.8262 160.8262 0.0000 0.0000 0.0000 339 GLU B O   
6585 C CB  . GLU B 339 ? 160.6734 160.6734 160.6734 0.0000 0.0000 0.0000 339 GLU B CB  
6586 C CG  . GLU B 339 ? 159.5382 159.5382 159.5382 0.0000 0.0000 0.0000 339 GLU B CG  
6587 C CD  . GLU B 339 ? 160.7645 160.7645 160.7645 0.0000 0.0000 0.0000 339 GLU B CD  
6588 O OE1 . GLU B 339 ? 160.6053 160.6053 160.6053 0.0000 0.0000 0.0000 339 GLU B OE1 
6589 O OE2 . GLU B 339 ? 159.7445 159.7445 159.7445 0.0000 0.0000 0.0000 339 GLU B OE2 
6590 N N   . PHE B 340 ? 159.9981 159.9981 159.9981 0.0000 0.0000 0.0000 340 PHE B N   
6591 C CA  . PHE B 340 ? 160.1074 160.1074 160.1074 0.0000 0.0000 0.0000 340 PHE B CA  
6592 C C   . PHE B 340 ? 160.5597 160.5597 160.5597 0.0000 0.0000 0.0000 340 PHE B C   
6593 O O   . PHE B 340 ? 159.0503 159.0503 159.0503 0.0000 0.0000 0.0000 340 PHE B O   
6594 C CB  . PHE B 340 ? 159.9862 159.9862 159.9862 0.0000 0.0000 0.0000 340 PHE B CB  
6595 C CG  . PHE B 340 ? 160.2223 160.2223 160.2223 0.0000 0.0000 0.0000 340 PHE B CG  
6596 C CD1 . PHE B 340 ? 160.6955 160.6955 160.6955 0.0000 0.0000 0.0000 340 PHE B CD1 
6597 C CD2 . PHE B 340 ? 160.5045 160.5045 160.5045 0.0000 0.0000 0.0000 340 PHE B CD2 
6598 C CE1 . PHE B 340 ? 160.4708 160.4708 160.4708 0.0000 0.0000 0.0000 340 PHE B CE1 
6599 C CE2 . PHE B 340 ? 160.0270 160.0270 160.0270 0.0000 0.0000 0.0000 340 PHE B CE2 
6600 C CZ  . PHE B 340 ? 160.5062 160.5062 160.5062 0.0000 0.0000 0.0000 340 PHE B CZ  
6601 N N   . TYR B 341 ? 160.2453 160.2453 160.2453 0.0000 0.0000 0.0000 341 TYR B N   
6602 C CA  . TYR B 341 ? 160.8818 160.8818 160.8818 0.0000 0.0000 0.0000 341 TYR B CA  
6603 C C   . TYR B 341 ? 160.8251 160.8251 160.8251 0.0000 0.0000 0.0000 341 TYR B C   
6604 O O   . TYR B 341 ? 161.0605 161.0605 161.0605 0.0000 0.0000 0.0000 341 TYR B O   
6605 C CB  . TYR B 341 ? 159.1834 159.1834 159.1834 0.0000 0.0000 0.0000 341 TYR B CB  
6606 C CG  . TYR B 341 ? 159.9957 159.9957 159.9957 0.0000 0.0000 0.0000 341 TYR B CG  
6607 C CD1 . TYR B 341 ? 159.4041 159.4041 159.4041 0.0000 0.0000 0.0000 341 TYR B CD1 
6608 C CD2 . TYR B 341 ? 158.2982 158.2982 158.2982 0.0000 0.0000 0.0000 341 TYR B CD2 
6609 C CE1 . TYR B 341 ? 160.0255 160.0255 160.0255 0.0000 0.0000 0.0000 341 TYR B CE1 
6610 C CE2 . TYR B 341 ? 160.8327 160.8327 160.8327 0.0000 0.0000 0.0000 341 TYR B CE2 
6611 C CZ  . TYR B 341 ? 160.9563 160.9563 160.9563 0.0000 0.0000 0.0000 341 TYR B CZ  
6612 O OH  . TYR B 341 ? 161.0063 161.0063 161.0063 0.0000 0.0000 0.0000 341 TYR B OH  
6613 N N   . MET B 342 ? 161.3058 161.3058 161.3058 0.0000 0.0000 0.0000 342 MET B N   
6614 C CA  . MET B 342 ? 161.3747 161.3747 161.3747 0.0000 0.0000 0.0000 342 MET B CA  
6615 C C   . MET B 342 ? 161.4260 161.4260 161.4260 0.0000 0.0000 0.0000 342 MET B C   
6616 O O   . MET B 342 ? 161.5957 161.5957 161.5957 0.0000 0.0000 0.0000 342 MET B O   
6617 C CB  . MET B 342 ? 161.3885 161.3885 161.3885 0.0000 0.0000 0.0000 342 MET B CB  
6618 C CG  . MET B 342 ? 160.9928 160.9928 160.9928 0.0000 0.0000 0.0000 342 MET B CG  
6619 S SD  . MET B 342 ? 161.1261 161.1261 161.1261 0.0000 0.0000 0.0000 342 MET B SD  
6620 C CE  . MET B 342 ? 161.4030 161.4030 161.4030 0.0000 0.0000 0.0000 342 MET B CE  
6621 N N   . ALA B 343 ? 161.6462 161.6462 161.6462 0.0000 0.0000 0.0000 343 ALA B N   
6622 C CA  . ALA B 343 ? 161.5374 161.5374 161.5374 0.0000 0.0000 0.0000 343 ALA B CA  
6623 C C   . ALA B 343 ? 161.4186 161.4186 161.4186 0.0000 0.0000 0.0000 343 ALA B C   
6624 O O   . ALA B 343 ? 161.4273 161.4273 161.4273 0.0000 0.0000 0.0000 343 ALA B O   
6625 C CB  . ALA B 343 ? 161.3779 161.3779 161.3779 0.0000 0.0000 0.0000 343 ALA B CB  
6626 N N   . TYR B 344 ? 161.3359 161.3359 161.3359 0.0000 0.0000 0.0000 344 TYR B N   
6627 C CA  . TYR B 344 ? 161.3062 161.3062 161.3062 0.0000 0.0000 0.0000 344 TYR B CA  
6628 C C   . TYR B 344 ? 161.2538 161.2538 161.2538 0.0000 0.0000 0.0000 344 TYR B C   
6629 O O   . TYR B 344 ? 161.4502 161.4502 161.4502 0.0000 0.0000 0.0000 344 TYR B O   
6630 C CB  . TYR B 344 ? 161.3606 161.3606 161.3606 0.0000 0.0000 0.0000 344 TYR B CB  
6631 C CG  . TYR B 344 ? 161.2853 161.2853 161.2853 0.0000 0.0000 0.0000 344 TYR B CG  
6632 C CD1 . TYR B 344 ? 161.1890 161.1890 161.1890 0.0000 0.0000 0.0000 344 TYR B CD1 
6633 C CD2 . TYR B 344 ? 161.0304 161.0304 161.0304 0.0000 0.0000 0.0000 344 TYR B CD2 
6634 C CE1 . TYR B 344 ? 161.3726 161.3726 161.3726 0.0000 0.0000 0.0000 344 TYR B CE1 
6635 C CE2 . TYR B 344 ? 161.2666 161.2666 161.2666 0.0000 0.0000 0.0000 344 TYR B CE2 
6636 C CZ  . TYR B 344 ? 161.4248 161.4248 161.4248 0.0000 0.0000 0.0000 344 TYR B CZ  
6637 O OH  . TYR B 344 ? 161.3473 161.3473 161.3473 0.0000 0.0000 0.0000 344 TYR B OH  
6638 N N   . ALA B 345 ? 161.4192 161.4192 161.4192 0.0000 0.0000 0.0000 345 ALA B N   
6639 C CA  . ALA B 345 ? 161.3219 161.3219 161.3219 0.0000 0.0000 0.0000 345 ALA B CA  
6640 C C   . ALA B 345 ? 161.1416 161.1416 161.1416 0.0000 0.0000 0.0000 345 ALA B C   
6641 O O   . ALA B 345 ? 161.0569 161.0569 161.0569 0.0000 0.0000 0.0000 345 ALA B O   
6642 C CB  . ALA B 345 ? 161.5393 161.5393 161.5393 0.0000 0.0000 0.0000 345 ALA B CB  
6643 N N   . ASP B 346 ? 161.7078 161.7078 161.7078 0.0000 0.0000 0.0000 346 ASP B N   
6644 C CA  . ASP B 346 ? 160.6953 160.6953 160.6953 0.0000 0.0000 0.0000 346 ASP B CA  
6645 C C   . ASP B 346 ? 160.3370 160.3370 160.3370 0.0000 0.0000 0.0000 346 ASP B C   
6646 O O   . ASP B 346 ? 160.7087 160.7087 160.7087 0.0000 0.0000 0.0000 346 ASP B O   
6647 C CB  . ASP B 346 ? 160.6159 160.6159 160.6159 0.0000 0.0000 0.0000 346 ASP B CB  
6648 C CG  . ASP B 346 ? 161.5525 161.5525 161.5525 0.0000 0.0000 0.0000 346 ASP B CG  
6649 O OD1 . ASP B 346 ? 161.3883 161.3883 161.3883 0.0000 0.0000 0.0000 346 ASP B OD1 
6650 O OD2 . ASP B 346 ? 161.4241 161.4241 161.4241 0.0000 0.0000 0.0000 346 ASP B OD2 
6651 N N   . TYR B 347 ? 161.3126 161.3126 161.3126 0.0000 0.0000 0.0000 347 TYR B N   
6652 C CA  . TYR B 347 ? 160.8385 160.8385 160.8385 0.0000 0.0000 0.0000 347 TYR B CA  
6653 C C   . TYR B 347 ? 159.5958 159.5958 159.5958 0.0000 0.0000 0.0000 347 TYR B C   
6654 O O   . TYR B 347 ? 157.5216 157.5216 157.5216 0.0000 0.0000 0.0000 347 TYR B O   
6655 C CB  . TYR B 347 ? 160.6367 160.6367 160.6367 0.0000 0.0000 0.0000 347 TYR B CB  
6656 C CG  . TYR B 347 ? 161.4701 161.4701 161.4701 0.0000 0.0000 0.0000 347 TYR B CG  
6657 C CD1 . TYR B 347 ? 161.3508 161.3508 161.3508 0.0000 0.0000 0.0000 347 TYR B CD1 
6658 C CD2 . TYR B 347 ? 161.2786 161.2786 161.2786 0.0000 0.0000 0.0000 347 TYR B CD2 
6659 C CE1 . TYR B 347 ? 161.5816 161.5816 161.5816 0.0000 0.0000 0.0000 347 TYR B CE1 
6660 C CE2 . TYR B 347 ? 161.4736 161.4736 161.4736 0.0000 0.0000 0.0000 347 TYR B CE2 
6661 C CZ  . TYR B 347 ? 161.6153 161.6153 161.6153 0.0000 0.0000 0.0000 347 TYR B CZ  
6662 O OH  . TYR B 347 ? 161.3442 161.3442 161.3442 0.0000 0.0000 0.0000 347 TYR B OH  
6663 N N   . HIS B 348 ? 161.4696 161.4696 161.4696 0.0000 0.0000 0.0000 348 HIS B N   
6664 C CA  . HIS B 348 ? 161.1649 161.1649 161.1649 0.0000 0.0000 0.0000 348 HIS B CA  
6665 C C   . HIS B 348 ? 161.2085 161.2085 161.2085 0.0000 0.0000 0.0000 348 HIS B C   
6666 O O   . HIS B 348 ? 161.2218 161.2218 161.2218 0.0000 0.0000 0.0000 348 HIS B O   
6667 C CB  . HIS B 348 ? 161.3239 161.3239 161.3239 0.0000 0.0000 0.0000 348 HIS B CB  
6668 C CG  . HIS B 348 ? 161.1905 161.1905 161.1905 0.0000 0.0000 0.0000 348 HIS B CG  
6669 N ND1 . HIS B 348 ? 161.1804 161.1804 161.1804 0.0000 0.0000 0.0000 348 HIS B ND1 
6670 C CD2 . HIS B 348 ? 161.3630 161.3630 161.3630 0.0000 0.0000 0.0000 348 HIS B CD2 
6671 C CE1 . HIS B 348 ? 161.4561 161.4561 161.4561 0.0000 0.0000 0.0000 348 HIS B CE1 
6672 N NE2 . HIS B 348 ? 161.4428 161.4428 161.4428 0.0000 0.0000 0.0000 348 HIS B NE2 
6673 N N   . ASP B 349 ? 161.3620 161.3620 161.3620 0.0000 0.0000 0.0000 349 ASP B N   
6674 C CA  . ASP B 349 ? 161.0490 161.0490 161.0490 0.0000 0.0000 0.0000 349 ASP B CA  
6675 C C   . ASP B 349 ? 161.4004 161.4004 161.4004 0.0000 0.0000 0.0000 349 ASP B C   
6676 O O   . ASP B 349 ? 161.6797 161.6797 161.6797 0.0000 0.0000 0.0000 349 ASP B O   
6677 C CB  . ASP B 349 ? 161.0287 161.0287 161.0287 0.0000 0.0000 0.0000 349 ASP B CB  
6678 C CG  . ASP B 349 ? 160.9855 160.9855 160.9855 0.0000 0.0000 0.0000 349 ASP B CG  
6679 O OD1 . ASP B 349 ? 161.1335 161.1335 161.1335 0.0000 0.0000 0.0000 349 ASP B OD1 
6680 O OD2 . ASP B 349 ? 160.8781 160.8781 160.8781 0.0000 0.0000 0.0000 349 ASP B OD2 
6681 N N   . LEU B 350 ? 161.3735 161.3735 161.3735 0.0000 0.0000 0.0000 350 LEU B N   
6682 C CA  . LEU B 350 ? 161.0378 161.0378 161.0378 0.0000 0.0000 0.0000 350 LEU B CA  
6683 C C   . LEU B 350 ? 161.3072 161.3072 161.3072 0.0000 0.0000 0.0000 350 LEU B C   
6684 O O   . LEU B 350 ? 161.6186 161.6186 161.6186 0.0000 0.0000 0.0000 350 LEU B O   
6685 C CB  . LEU B 350 ? 160.6352 160.6352 160.6352 0.0000 0.0000 0.0000 350 LEU B CB  
6686 C CG  . LEU B 350 ? 159.4818 159.4818 159.4818 0.0000 0.0000 0.0000 350 LEU B CG  
6687 C CD1 . LEU B 350 ? 160.5087 160.5087 160.5087 0.0000 0.0000 0.0000 350 LEU B CD1 
6688 C CD2 . LEU B 350 ? 161.3387 161.3387 161.3387 0.0000 0.0000 0.0000 350 LEU B CD2 
6689 N N   . MET B 351 ? 161.3061 161.3061 161.3061 0.0000 0.0000 0.0000 351 MET B N   
6690 C CA  . MET B 351 ? 161.3699 161.3699 161.3699 0.0000 0.0000 0.0000 351 MET B CA  
6691 C C   . MET B 351 ? 161.6691 161.6691 161.6691 0.0000 0.0000 0.0000 351 MET B C   
6692 O O   . MET B 351 ? 161.4547 161.4547 161.4547 0.0000 0.0000 0.0000 351 MET B O   
6693 C CB  . MET B 351 ? 161.5869 161.5869 161.5869 0.0000 0.0000 0.0000 351 MET B CB  
6694 C CG  . MET B 351 ? 161.4771 161.4771 161.4771 0.0000 0.0000 0.0000 351 MET B CG  
6695 S SD  . MET B 351 ? 161.4529 161.4529 161.4529 0.0000 0.0000 0.0000 351 MET B SD  
6696 C CE  . MET B 351 ? 161.3915 161.3915 161.3915 0.0000 0.0000 0.0000 351 MET B CE  
6697 N N   . GLU B 352 ? 161.3813 161.3813 161.3813 0.0000 0.0000 0.0000 352 GLU B N   
6698 C CA  . GLU B 352 ? 161.3526 161.3526 161.3526 0.0000 0.0000 0.0000 352 GLU B CA  
6699 C C   . GLU B 352 ? 161.2810 161.2810 161.2810 0.0000 0.0000 0.0000 352 GLU B C   
6700 O O   . GLU B 352 ? 161.4567 161.4567 161.4567 0.0000 0.0000 0.0000 352 GLU B O   
6701 C CB  . GLU B 352 ? 160.9518 160.9518 160.9518 0.0000 0.0000 0.0000 352 GLU B CB  
6702 C CG  . GLU B 352 ? 159.9624 159.9624 159.9624 0.0000 0.0000 0.0000 352 GLU B CG  
6703 C CD  . GLU B 352 ? 160.5505 160.5505 160.5505 0.0000 0.0000 0.0000 352 GLU B CD  
6704 O OE1 . GLU B 352 ? 160.1791 160.1791 160.1791 0.0000 0.0000 0.0000 352 GLU B OE1 
6705 O OE2 . GLU B 352 ? 160.2370 160.2370 160.2370 0.0000 0.0000 0.0000 352 GLU B OE2 
6706 N N   . ILE B 353 ? 161.2199 161.2199 161.2199 0.0000 0.0000 0.0000 353 ILE B N   
6707 C CA  . ILE B 353 ? 161.1941 161.1941 161.1941 0.0000 0.0000 0.0000 353 ILE B CA  
6708 C C   . ILE B 353 ? 161.2708 161.2708 161.2708 0.0000 0.0000 0.0000 353 ILE B C   
6709 O O   . ILE B 353 ? 161.5717 161.5717 161.5717 0.0000 0.0000 0.0000 353 ILE B O   
6710 C CB  . ILE B 353 ? 161.3152 161.3152 161.3152 0.0000 0.0000 0.0000 353 ILE B CB  
6711 C CG1 . ILE B 353 ? 161.1514 161.1514 161.1514 0.0000 0.0000 0.0000 353 ILE B CG1 
6712 C CG2 . ILE B 353 ? 160.5387 160.5387 160.5387 0.0000 0.0000 0.0000 353 ILE B CG2 
6713 C CD1 . ILE B 353 ? 159.4859 159.4859 159.4859 0.0000 0.0000 0.0000 353 ILE B CD1 
6714 N N   . THR B 354 ? 161.3502 161.3502 161.3502 0.0000 0.0000 0.0000 354 THR B N   
6715 C CA  . THR B 354 ? 161.2736 161.2736 161.2736 0.0000 0.0000 0.0000 354 THR B CA  
6716 C C   . THR B 354 ? 161.2294 161.2294 161.2294 0.0000 0.0000 0.0000 354 THR B C   
6717 O O   . THR B 354 ? 161.4880 161.4880 161.4880 0.0000 0.0000 0.0000 354 THR B O   
6718 C CB  . THR B 354 ? 161.3448 161.3448 161.3448 0.0000 0.0000 0.0000 354 THR B CB  
6719 O OG1 . THR B 354 ? 161.4624 161.4624 161.4624 0.0000 0.0000 0.0000 354 THR B OG1 
6720 C CG2 . THR B 354 ? 161.1461 161.1461 161.1461 0.0000 0.0000 0.0000 354 THR B CG2 
6721 N N   . GLU B 355 ? 161.2030 161.2030 161.2030 0.0000 0.0000 0.0000 355 GLU B N   
6722 C CA  . GLU B 355 ? 161.2659 161.2659 161.2659 0.0000 0.0000 0.0000 355 GLU B CA  
6723 C C   . GLU B 355 ? 161.3978 161.3978 161.3978 0.0000 0.0000 0.0000 355 GLU B C   
6724 O O   . GLU B 355 ? 161.5884 161.5884 161.5884 0.0000 0.0000 0.0000 355 GLU B O   
6725 C CB  . GLU B 355 ? 161.4721 161.4721 161.4721 0.0000 0.0000 0.0000 355 GLU B CB  
6726 C CG  . GLU B 355 ? 161.5478 161.5478 161.5478 0.0000 0.0000 0.0000 355 GLU B CG  
6727 C CD  . GLU B 355 ? 161.4431 161.4431 161.4431 0.0000 0.0000 0.0000 355 GLU B CD  
6728 O OE1 . GLU B 355 ? 161.4771 161.4771 161.4771 0.0000 0.0000 0.0000 355 GLU B OE1 
6729 O OE2 . GLU B 355 ? 161.3664 161.3664 161.3664 0.0000 0.0000 0.0000 355 GLU B OE2 
6730 N N   . LYS B 356 ? 161.5888 161.5888 161.5888 0.0000 0.0000 0.0000 356 LYS B N   
6731 C CA  . LYS B 356 ? 161.2304 161.2304 161.2304 0.0000 0.0000 0.0000 356 LYS B CA  
6732 C C   . LYS B 356 ? 161.2418 161.2418 161.2418 0.0000 0.0000 0.0000 356 LYS B C   
6733 O O   . LYS B 356 ? 161.3583 161.3583 161.3583 0.0000 0.0000 0.0000 356 LYS B O   
6734 C CB  . LYS B 356 ? 161.4454 161.4454 161.4454 0.0000 0.0000 0.0000 356 LYS B CB  
6735 C CG  . LYS B 356 ? 161.3141 161.3141 161.3141 0.0000 0.0000 0.0000 356 LYS B CG  
6736 C CD  . LYS B 356 ? 161.1423 161.1423 161.1423 0.0000 0.0000 0.0000 356 LYS B CD  
6737 C CE  . LYS B 356 ? 160.6536 160.6536 160.6536 0.0000 0.0000 0.0000 356 LYS B CE  
6738 N NZ  . LYS B 356 ? 160.7837 160.7837 160.7837 0.0000 0.0000 0.0000 356 LYS B NZ  
6739 N N   . MET B 357 ? 161.2758 161.2758 161.2758 0.0000 0.0000 0.0000 357 MET B N   
6740 C CA  . MET B 357 ? 160.7289 160.7289 160.7289 0.0000 0.0000 0.0000 357 MET B CA  
6741 C C   . MET B 357 ? 161.2091 161.2091 161.2091 0.0000 0.0000 0.0000 357 MET B C   
6742 O O   . MET B 357 ? 161.5281 161.5281 161.5281 0.0000 0.0000 0.0000 357 MET B O   
6743 C CB  . MET B 357 ? 161.0557 161.0557 161.0557 0.0000 0.0000 0.0000 357 MET B CB  
6744 C CG  . MET B 357 ? 161.0821 161.0821 161.0821 0.0000 0.0000 0.0000 357 MET B CG  
6745 S SD  . MET B 357 ? 160.8699 160.8699 160.8699 0.0000 0.0000 0.0000 357 MET B SD  
6746 C CE  . MET B 357 ? 161.2853 161.2853 161.2853 0.0000 0.0000 0.0000 357 MET B CE  
6747 N N   . VAL B 358 ? 161.3470 161.3470 161.3470 0.0000 0.0000 0.0000 358 VAL B N   
6748 C CA  . VAL B 358 ? 161.3250 161.3250 161.3250 0.0000 0.0000 0.0000 358 VAL B CA  
6749 C C   . VAL B 358 ? 161.4828 161.4828 161.4828 0.0000 0.0000 0.0000 358 VAL B C   
6750 O O   . VAL B 358 ? 161.4030 161.4030 161.4030 0.0000 0.0000 0.0000 358 VAL B O   
6751 C CB  . VAL B 358 ? 161.3936 161.3936 161.3936 0.0000 0.0000 0.0000 358 VAL B CB  
6752 C CG1 . VAL B 358 ? 161.5364 161.5364 161.5364 0.0000 0.0000 0.0000 358 VAL B CG1 
6753 C CG2 . VAL B 358 ? 161.6138 161.6138 161.6138 0.0000 0.0000 0.0000 358 VAL B CG2 
6754 N N   . SER B 359 ? 161.6821 161.6821 161.6821 0.0000 0.0000 0.0000 359 SER B N   
6755 C CA  . SER B 359 ? 161.2588 161.2588 161.2588 0.0000 0.0000 0.0000 359 SER B CA  
6756 C C   . SER B 359 ? 161.2799 161.2799 161.2799 0.0000 0.0000 0.0000 359 SER B C   
6757 O O   . SER B 359 ? 161.3359 161.3359 161.3359 0.0000 0.0000 0.0000 359 SER B O   
6758 C CB  . SER B 359 ? 161.5933 161.5933 161.5933 0.0000 0.0000 0.0000 359 SER B CB  
6759 O OG  . SER B 359 ? 161.3171 161.3171 161.3171 0.0000 0.0000 0.0000 359 SER B OG  
6760 N N   . GLY B 360 ? 160.8341 160.8341 160.8341 0.0000 0.0000 0.0000 360 GLY B N   
6761 C CA  . GLY B 360 ? 161.0911 161.0911 161.0911 0.0000 0.0000 0.0000 360 GLY B CA  
6762 C C   . GLY B 360 ? 160.6846 160.6846 160.6846 0.0000 0.0000 0.0000 360 GLY B C   
6763 O O   . GLY B 360 ? 160.6558 160.6558 160.6558 0.0000 0.0000 0.0000 360 GLY B O   
6764 N N   . MET B 361 ? 160.4480 160.4480 160.4480 0.0000 0.0000 0.0000 361 MET B N   
6765 C CA  . MET B 361 ? 161.3504 161.3504 161.3504 0.0000 0.0000 0.0000 361 MET B CA  
6766 C C   . MET B 361 ? 161.3127 161.3127 161.3127 0.0000 0.0000 0.0000 361 MET B C   
6767 O O   . MET B 361 ? 161.4168 161.4168 161.4168 0.0000 0.0000 0.0000 361 MET B O   
6768 C CB  . MET B 361 ? 161.4494 161.4494 161.4494 0.0000 0.0000 0.0000 361 MET B CB  
6769 C CG  . MET B 361 ? 161.0233 161.0233 161.0233 0.0000 0.0000 0.0000 361 MET B CG  
6770 S SD  . MET B 361 ? 161.1107 161.1107 161.1107 0.0000 0.0000 0.0000 361 MET B SD  
6771 C CE  . MET B 361 ? 161.1360 161.1360 161.1360 0.0000 0.0000 0.0000 361 MET B CE  
6772 N N   . VAL B 362 ? 161.2462 161.2462 161.2462 0.0000 0.0000 0.0000 362 VAL B N   
6773 C CA  . VAL B 362 ? 161.4909 161.4909 161.4909 0.0000 0.0000 0.0000 362 VAL B CA  
6774 C C   . VAL B 362 ? 161.3120 161.3120 161.3120 0.0000 0.0000 0.0000 362 VAL B C   
6775 O O   . VAL B 362 ? 161.2852 161.2852 161.2852 0.0000 0.0000 0.0000 362 VAL B O   
6776 C CB  . VAL B 362 ? 161.3852 161.3852 161.3852 0.0000 0.0000 0.0000 362 VAL B CB  
6777 C CG1 . VAL B 362 ? 161.3211 161.3211 161.3211 0.0000 0.0000 0.0000 362 VAL B CG1 
6778 C CG2 . VAL B 362 ? 160.8778 160.8778 160.8778 0.0000 0.0000 0.0000 362 VAL B CG2 
6779 N N   . LYS B 363 ? 161.4559 161.4559 161.4559 0.0000 0.0000 0.0000 363 LYS B N   
6780 C CA  . LYS B 363 ? 161.2397 161.2397 161.2397 0.0000 0.0000 0.0000 363 LYS B CA  
6781 C C   . LYS B 363 ? 161.2496 161.2496 161.2496 0.0000 0.0000 0.0000 363 LYS B C   
6782 O O   . LYS B 363 ? 161.2843 161.2843 161.2843 0.0000 0.0000 0.0000 363 LYS B O   
6783 C CB  . LYS B 363 ? 161.2506 161.2506 161.2506 0.0000 0.0000 0.0000 363 LYS B CB  
6784 C CG  . LYS B 363 ? 162.7617 162.7617 162.7617 0.0000 0.0000 0.0000 363 LYS B CG  
6785 C CD  . LYS B 363 ? 162.8382 162.8382 162.8382 0.0000 0.0000 0.0000 363 LYS B CD  
6786 C CE  . LYS B 363 ? 162.8042 162.8042 162.8042 0.0000 0.0000 0.0000 363 LYS B CE  
6787 N NZ  . LYS B 363 ? 162.8247 162.8247 162.8247 0.0000 0.0000 0.0000 363 LYS B NZ  
6788 N N   . HIS B 364 ? 162.9257 162.9257 162.9257 0.0000 0.0000 0.0000 364 HIS B N   
6789 C CA  . HIS B 364 ? 163.0210 163.0210 163.0210 0.0000 0.0000 0.0000 364 HIS B CA  
6790 C C   . HIS B 364 ? 161.5204 161.5204 161.5204 0.0000 0.0000 0.0000 364 HIS B C   
6791 O O   . HIS B 364 ? 161.5110 161.5110 161.5110 0.0000 0.0000 0.0000 364 HIS B O   
6792 C CB  . HIS B 364 ? 161.4902 161.4902 161.4902 0.0000 0.0000 0.0000 364 HIS B CB  
6793 C CG  . HIS B 364 ? 161.6858 161.6858 161.6858 0.0000 0.0000 0.0000 364 HIS B CG  
6794 N ND1 . HIS B 364 ? 161.6352 161.6352 161.6352 0.0000 0.0000 0.0000 364 HIS B ND1 
6795 C CD2 . HIS B 364 ? 161.3717 161.3717 161.3717 0.0000 0.0000 0.0000 364 HIS B CD2 
6796 C CE1 . HIS B 364 ? 161.3962 161.3962 161.3962 0.0000 0.0000 0.0000 364 HIS B CE1 
6797 N NE2 . HIS B 364 ? 161.2405 161.2405 161.2405 0.0000 0.0000 0.0000 364 HIS B NE2 
6798 N N   . ILE B 365 ? 161.3625 161.3625 161.3625 0.0000 0.0000 0.0000 365 ILE B N   
6799 C CA  . ILE B 365 ? 161.3228 161.3228 161.3228 0.0000 0.0000 0.0000 365 ILE B CA  
6800 C C   . ILE B 365 ? 161.3926 161.3926 161.3926 0.0000 0.0000 0.0000 365 ILE B C   
6801 O O   . ILE B 365 ? 161.6279 161.6279 161.6279 0.0000 0.0000 0.0000 365 ILE B O   
6802 C CB  . ILE B 365 ? 161.3299 161.3299 161.3299 0.0000 0.0000 0.0000 365 ILE B CB  
6803 C CG1 . ILE B 365 ? 161.3120 161.3120 161.3120 0.0000 0.0000 0.0000 365 ILE B CG1 
6804 C CG2 . ILE B 365 ? 161.3680 161.3680 161.3680 0.0000 0.0000 0.0000 365 ILE B CG2 
6805 C CD1 . ILE B 365 ? 161.5064 161.5064 161.5064 0.0000 0.0000 0.0000 365 ILE B CD1 
6806 N N   . THR B 366 ? 161.3601 161.3601 161.3601 0.0000 0.0000 0.0000 366 THR B N   
6807 C CA  . THR B 366 ? 161.4270 161.4270 161.4270 0.0000 0.0000 0.0000 366 THR B CA  
6808 C C   . THR B 366 ? 161.5148 161.5148 161.5148 0.0000 0.0000 0.0000 366 THR B C   
6809 O O   . THR B 366 ? 161.4832 161.4832 161.4832 0.0000 0.0000 0.0000 366 THR B O   
6810 C CB  . THR B 366 ? 161.6046 161.6046 161.6046 0.0000 0.0000 0.0000 366 THR B CB  
6811 O OG1 . THR B 366 ? 161.3625 161.3625 161.3625 0.0000 0.0000 0.0000 366 THR B OG1 
6812 C CG2 . THR B 366 ? 161.3939 161.3939 161.3939 0.0000 0.0000 0.0000 366 THR B CG2 
6813 N N   . GLY B 367 ? 161.8013 161.8013 161.8013 0.0000 0.0000 0.0000 367 GLY B N   
6814 C CA  . GLY B 367 ? 162.3601 162.3601 162.3601 0.0000 0.0000 0.0000 367 GLY B CA  
6815 C C   . GLY B 367 ? 161.2493 161.2493 161.2493 0.0000 0.0000 0.0000 367 GLY B C   
6816 O O   . GLY B 367 ? 161.1805 161.1805 161.1805 0.0000 0.0000 0.0000 367 GLY B O   
6817 N N   . SER B 368 ? 161.3326 161.3326 161.3326 0.0000 0.0000 0.0000 368 SER B N   
6818 C CA  . SER B 368 ? 167.9883 167.9883 167.9883 0.0000 0.0000 0.0000 368 SER B CA  
6819 C C   . SER B 368 ? 168.2528 168.2528 168.2528 0.0000 0.0000 0.0000 368 SER B C   
6820 O O   . SER B 368 ? 167.5328 167.5328 167.5328 0.0000 0.0000 0.0000 368 SER B O   
6821 C CB  . SER B 368 ? 167.1594 167.1594 167.1594 0.0000 0.0000 0.0000 368 SER B CB  
6822 O OG  . SER B 368 ? 168.4010 168.4010 168.4010 0.0000 0.0000 0.0000 368 SER B OG  
6823 N N   . TYR B 369 ? 168.6084 168.6084 168.6084 0.0000 0.0000 0.0000 369 TYR B N   
6824 C CA  . TYR B 369 ? 168.7770 168.7770 168.7770 0.0000 0.0000 0.0000 369 TYR B CA  
6825 C C   . TYR B 369 ? 161.3779 161.3779 161.3779 0.0000 0.0000 0.0000 369 TYR B C   
6826 O O   . TYR B 369 ? 161.0242 161.0242 161.0242 0.0000 0.0000 0.0000 369 TYR B O   
6827 C CB  . TYR B 369 ? 161.7573 161.7573 161.7573 0.0000 0.0000 0.0000 369 TYR B CB  
6828 C CG  . TYR B 369 ? 163.0244 163.0244 163.0244 0.0000 0.0000 0.0000 369 TYR B CG  
6829 C CD1 . TYR B 369 ? 161.4402 161.4402 161.4402 0.0000 0.0000 0.0000 369 TYR B CD1 
6830 C CD2 . TYR B 369 ? 160.9677 160.9677 160.9677 0.0000 0.0000 0.0000 369 TYR B CD2 
6831 C CE1 . TYR B 369 ? 157.6811 157.6811 157.6811 0.0000 0.0000 0.0000 369 TYR B CE1 
6832 C CE2 . TYR B 369 ? 161.3970 161.3970 161.3970 0.0000 0.0000 0.0000 369 TYR B CE2 
6833 C CZ  . TYR B 369 ? 156.6285 156.6285 156.6285 0.0000 0.0000 0.0000 369 TYR B CZ  
6834 O OH  . TYR B 369 ? 161.0774 161.0774 161.0774 0.0000 0.0000 0.0000 369 TYR B OH  
6835 N N   . LYS B 370 ? 158.6502 158.6502 158.6502 0.0000 0.0000 0.0000 370 LYS B N   
6836 C CA  . LYS B 370 ? 157.8239 157.8239 157.8239 0.0000 0.0000 0.0000 370 LYS B CA  
6837 C C   . LYS B 370 ? 171.9604 171.9604 171.9604 0.0000 0.0000 0.0000 370 LYS B C   
6838 O O   . LYS B 370 ? 173.0190 173.0190 173.0190 0.0000 0.0000 0.0000 370 LYS B O   
6839 C CB  . LYS B 370 ? 173.1257 173.1257 173.1257 0.0000 0.0000 0.0000 370 LYS B CB  
6840 C CG  . LYS B 370 ? 172.0770 172.0770 172.0770 0.0000 0.0000 0.0000 370 LYS B CG  
6841 C CD  . LYS B 370 ? 172.9877 172.9877 172.9877 0.0000 0.0000 0.0000 370 LYS B CD  
6842 C CE  . LYS B 370 ? 172.9941 172.9941 172.9941 0.0000 0.0000 0.0000 370 LYS B CE  
6843 N NZ  . LYS B 370 ? 172.2298 172.2298 172.2298 0.0000 0.0000 0.0000 370 LYS B NZ  
6844 N N   . VAL B 371 ? 174.1733 174.1733 174.1733 0.0000 0.0000 0.0000 371 VAL B N   
6845 C CA  . VAL B 371 ? 172.6378 172.6378 172.6378 0.0000 0.0000 0.0000 371 VAL B CA  
6846 C C   . VAL B 371 ? 173.8109 173.8109 173.8109 0.0000 0.0000 0.0000 371 VAL B C   
6847 O O   . VAL B 371 ? 179.1418 179.1418 179.1418 0.0000 0.0000 0.0000 371 VAL B O   
6848 C CB  . VAL B 371 ? 178.8148 178.8148 178.8148 0.0000 0.0000 0.0000 371 VAL B CB  
6849 C CG1 . VAL B 371 ? 179.2106 179.2106 179.2106 0.0000 0.0000 0.0000 371 VAL B CG1 
6850 C CG2 . VAL B 371 ? 178.3270 178.3270 178.3270 0.0000 0.0000 0.0000 371 VAL B CG2 
6851 N N   . THR B 372 ? 179.4779 179.4779 179.4779 0.0000 0.0000 0.0000 372 THR B N   
6852 C CA  . THR B 372 ? 179.7269 179.7269 179.7269 0.0000 0.0000 0.0000 372 THR B CA  
6853 C C   . THR B 372 ? 179.3605 179.3605 179.3605 0.0000 0.0000 0.0000 372 THR B C   
6854 O O   . THR B 372 ? 203.8200 203.8200 203.8200 0.0000 0.0000 0.0000 372 THR B O   
6855 C CB  . THR B 372 ? 204.6346 204.6346 204.6346 0.0000 0.0000 0.0000 372 THR B CB  
6856 O OG1 . THR B 372 ? 205.0169 205.0169 205.0169 0.0000 0.0000 0.0000 372 THR B OG1 
6857 C CG2 . THR B 372 ? 205.8821 205.8821 205.8821 0.0000 0.0000 0.0000 372 THR B CG2 
6858 N N   . TYR B 373 ? 205.4565 205.4565 205.4565 0.0000 0.0000 0.0000 373 TYR B N   
6859 C CA  . TYR B 373 ? 205.7995 205.7995 205.7995 0.0000 0.0000 0.0000 373 TYR B CA  
6860 C C   . TYR B 373 ? 205.7027 205.7027 205.7027 0.0000 0.0000 0.0000 373 TYR B C   
6861 O O   . TYR B 373 ? 206.0212 206.0212 206.0212 0.0000 0.0000 0.0000 373 TYR B O   
6862 C CB  . TYR B 373 ? 201.1319 201.1319 201.1319 0.0000 0.0000 0.0000 373 TYR B CB  
6863 C CG  . TYR B 373 ? 202.0222 202.0222 202.0222 0.0000 0.0000 0.0000 373 TYR B CG  
6864 C CD1 . TYR B 373 ? 202.8940 202.8940 202.8940 0.0000 0.0000 0.0000 373 TYR B CD1 
6865 C CD2 . TYR B 373 ? 202.6825 202.6825 202.6825 0.0000 0.0000 0.0000 373 TYR B CD2 
6866 C CE1 . TYR B 373 ? 215.8608 215.8608 215.8608 0.0000 0.0000 0.0000 373 TYR B CE1 
6867 C CE2 . TYR B 373 ? 215.9027 215.9027 215.9027 0.0000 0.0000 0.0000 373 TYR B CE2 
6868 C CZ  . TYR B 373 ? 216.3268 216.3268 216.3268 0.0000 0.0000 0.0000 373 TYR B CZ  
6869 O OH  . TYR B 373 ? 216.3176 216.3176 216.3176 0.0000 0.0000 0.0000 373 TYR B OH  
6870 N N   . HIS B 374 ? 216.3405 216.3405 216.3405 0.0000 0.0000 0.0000 374 HIS B N   
6871 C CA  . HIS B 374 ? 216.3587 216.3587 216.3587 0.0000 0.0000 0.0000 374 HIS B CA  
6872 C C   . HIS B 374 ? 216.2461 216.2461 216.2461 0.0000 0.0000 0.0000 374 HIS B C   
6873 O O   . HIS B 374 ? 224.9922 224.9922 224.9922 0.0000 0.0000 0.0000 374 HIS B O   
6874 C CB  . HIS B 374 ? 225.2359 225.2359 225.2359 0.0000 0.0000 0.0000 374 HIS B CB  
6875 C CG  . HIS B 374 ? 225.1316 225.1316 225.1316 0.0000 0.0000 0.0000 374 HIS B CG  
6876 N ND1 . HIS B 374 ? 225.3830 225.3830 225.3830 0.0000 0.0000 0.0000 374 HIS B ND1 
6877 C CD2 . HIS B 374 ? 225.4458 225.4458 225.4458 0.0000 0.0000 0.0000 374 HIS B CD2 
6878 C CE1 . HIS B 374 ? 225.4818 225.4818 225.4818 0.0000 0.0000 0.0000 374 HIS B CE1 
6879 N NE2 . HIS B 374 ? 225.3069 225.3069 225.3069 0.0000 0.0000 0.0000 374 HIS B NE2 
6880 N N   . PRO B 375 ? 225.3074 225.3074 225.3074 0.0000 0.0000 0.0000 375 PRO B N   
6881 C CA  . PRO B 375 ? 225.3275 225.3275 225.3275 0.0000 0.0000 0.0000 375 PRO B CA  
6882 C C   . PRO B 375 ? 214.6531 214.6531 214.6531 0.0000 0.0000 0.0000 375 PRO B C   
6883 O O   . PRO B 375 ? 214.5057 214.5057 214.5057 0.0000 0.0000 0.0000 375 PRO B O   
6884 C CB  . PRO B 375 ? 214.3578 214.3578 214.3578 0.0000 0.0000 0.0000 375 PRO B CB  
6885 C CG  . PRO B 375 ? 214.3411 214.3411 214.3411 0.0000 0.0000 0.0000 375 PRO B CG  
6886 C CD  . PRO B 375 ? 212.1566 212.1566 212.1566 0.0000 0.0000 0.0000 375 PRO B CD  
6887 N N   . ASP B 376 ? 211.9856 211.9856 211.9856 0.0000 0.0000 0.0000 376 ASP B N   
6888 C CA  . ASP B 376 ? 211.4081 211.4081 211.4081 0.0000 0.0000 0.0000 376 ASP B CA  
6889 C C   . ASP B 376 ? 211.0584 211.0584 211.0584 0.0000 0.0000 0.0000 376 ASP B C   
6890 O O   . ASP B 376 ? 211.9754 211.9754 211.9754 0.0000 0.0000 0.0000 376 ASP B O   
6891 C CB  . ASP B 376 ? 211.8306 211.8306 211.8306 0.0000 0.0000 0.0000 376 ASP B CB  
6892 C CG  . ASP B 376 ? 212.1064 212.1064 212.1064 0.0000 0.0000 0.0000 376 ASP B CG  
6893 O OD1 . ASP B 376 ? 212.1921 212.1921 212.1921 0.0000 0.0000 0.0000 376 ASP B OD1 
6894 O OD2 . ASP B 376 ? 212.1295 212.1295 212.1295 0.0000 0.0000 0.0000 376 ASP B OD2 
6895 N N   . GLY B 377 ? 198.3671 198.3671 198.3671 0.0000 0.0000 0.0000 377 GLY B N   
6896 C CA  . GLY B 377 ? 197.7241 197.7241 197.7241 0.0000 0.0000 0.0000 377 GLY B CA  
6897 C C   . GLY B 377 ? 197.6010 197.6010 197.6010 0.0000 0.0000 0.0000 377 GLY B C   
6898 O O   . GLY B 377 ? 197.8258 197.8258 197.8258 0.0000 0.0000 0.0000 377 GLY B O   
6899 N N   . PRO B 378 ? 197.8153 197.8153 197.8153 0.0000 0.0000 0.0000 378 PRO B N   
6900 C CA  . PRO B 378 ? 186.3168 186.3168 186.3168 0.0000 0.0000 0.0000 378 PRO B CA  
6901 C C   . PRO B 378 ? 186.1185 186.1185 186.1185 0.0000 0.0000 0.0000 378 PRO B C   
6902 O O   . PRO B 378 ? 185.7437 185.7437 185.7437 0.0000 0.0000 0.0000 378 PRO B O   
6903 C CB  . PRO B 378 ? 185.4005 185.4005 185.4005 0.0000 0.0000 0.0000 378 PRO B CB  
6904 C CG  . PRO B 378 ? 185.8434 185.8434 185.8434 0.0000 0.0000 0.0000 378 PRO B CG  
6905 C CD  . PRO B 378 ? 185.8717 185.8717 185.8717 0.0000 0.0000 0.0000 378 PRO B CD  
6906 N N   . GLU B 379 ? 186.0904 186.0904 186.0904 0.0000 0.0000 0.0000 379 GLU B N   
6907 C CA  . GLU B 379 ? 185.8843 185.8843 185.8843 0.0000 0.0000 0.0000 379 GLU B CA  
6908 C C   . GLU B 379 ? 186.1706 186.1706 186.1706 0.0000 0.0000 0.0000 379 GLU B C   
6909 O O   . GLU B 379 ? 185.9119 185.9119 185.9119 0.0000 0.0000 0.0000 379 GLU B O   
6910 C CB  . GLU B 379 ? 186.0651 186.0651 186.0651 0.0000 0.0000 0.0000 379 GLU B CB  
6911 C CG  . GLU B 379 ? 186.1820 186.1820 186.1820 0.0000 0.0000 0.0000 379 GLU B CG  
6912 C CD  . GLU B 379 ? 184.1435 184.1435 184.1435 0.0000 0.0000 0.0000 379 GLU B CD  
6913 O OE1 . GLU B 379 ? 183.8053 183.8053 183.8053 0.0000 0.0000 0.0000 379 GLU B OE1 
6914 O OE2 . GLU B 379 ? 183.3655 183.3655 183.3655 0.0000 0.0000 0.0000 379 GLU B OE2 
6915 N N   . GLY B 380 ? 183.5678 183.5678 183.5678 0.0000 0.0000 0.0000 380 GLY B N   
6916 C CA  . GLY B 380 ? 184.1651 184.1651 184.1651 0.0000 0.0000 0.0000 380 GLY B CA  
6917 C C   . GLY B 380 ? 184.2549 184.2549 184.2549 0.0000 0.0000 0.0000 380 GLY B C   
6918 O O   . GLY B 380 ? 184.1529 184.1529 184.1529 0.0000 0.0000 0.0000 380 GLY B O   
6919 N N   . GLN B 381 ? 184.3483 184.3483 184.3483 0.0000 0.0000 0.0000 381 GLN B N   
6920 C CA  . GLN B 381 ? 162.2864 162.2864 162.2864 0.0000 0.0000 0.0000 381 GLN B CA  
6921 C C   . GLN B 381 ? 161.6776 161.6776 161.6776 0.0000 0.0000 0.0000 381 GLN B C   
6922 O O   . GLN B 381 ? 161.6217 161.6217 161.6217 0.0000 0.0000 0.0000 381 GLN B O   
6923 C CB  . GLN B 381 ? 161.9333 161.9333 161.9333 0.0000 0.0000 0.0000 381 GLN B CB  
6924 C CG  . GLN B 381 ? 161.5564 161.5564 161.5564 0.0000 0.0000 0.0000 381 GLN B CG  
6925 C CD  . GLN B 381 ? 161.6655 161.6655 161.6655 0.0000 0.0000 0.0000 381 GLN B CD  
6926 O OE1 . GLN B 381 ? 161.7561 161.7561 161.7561 0.0000 0.0000 0.0000 381 GLN B OE1 
6927 N NE2 . GLN B 381 ? 161.4791 161.4791 161.4791 0.0000 0.0000 0.0000 381 GLN B NE2 
6928 N N   . ALA B 382 ? 161.4116 161.4116 161.4116 0.0000 0.0000 0.0000 382 ALA B N   
6929 C CA  . ALA B 382 ? 161.3794 161.3794 161.3794 0.0000 0.0000 0.0000 382 ALA B CA  
6930 C C   . ALA B 382 ? 161.4967 161.4967 161.4967 0.0000 0.0000 0.0000 382 ALA B C   
6931 O O   . ALA B 382 ? 161.4800 161.4800 161.4800 0.0000 0.0000 0.0000 382 ALA B O   
6932 C CB  . ALA B 382 ? 161.5268 161.5268 161.5268 0.0000 0.0000 0.0000 382 ALA B CB  
6933 N N   . TYR B 383 ? 161.5121 161.5121 161.5121 0.0000 0.0000 0.0000 383 TYR B N   
6934 C CA  . TYR B 383 ? 161.5946 161.5946 161.5946 0.0000 0.0000 0.0000 383 TYR B CA  
6935 C C   . TYR B 383 ? 161.4275 161.4275 161.4275 0.0000 0.0000 0.0000 383 TYR B C   
6936 O O   . TYR B 383 ? 161.2595 161.2595 161.2595 0.0000 0.0000 0.0000 383 TYR B O   
6937 C CB  . TYR B 383 ? 161.4260 161.4260 161.4260 0.0000 0.0000 0.0000 383 TYR B CB  
6938 C CG  . TYR B 383 ? 161.4777 161.4777 161.4777 0.0000 0.0000 0.0000 383 TYR B CG  
6939 C CD1 . TYR B 383 ? 161.1884 161.1884 161.1884 0.0000 0.0000 0.0000 383 TYR B CD1 
6940 C CD2 . TYR B 383 ? 161.2054 161.2054 161.2054 0.0000 0.0000 0.0000 383 TYR B CD2 
6941 C CE1 . TYR B 383 ? 161.4162 161.4162 161.4162 0.0000 0.0000 0.0000 383 TYR B CE1 
6942 C CE2 . TYR B 383 ? 161.3684 161.3684 161.3684 0.0000 0.0000 0.0000 383 TYR B CE2 
6943 C CZ  . TYR B 383 ? 161.4896 161.4896 161.4896 0.0000 0.0000 0.0000 383 TYR B CZ  
6944 O OH  . TYR B 383 ? 161.4140 161.4140 161.4140 0.0000 0.0000 0.0000 383 TYR B OH  
6945 N N   . ASP B 384 ? 161.4030 161.4030 161.4030 0.0000 0.0000 0.0000 384 ASP B N   
6946 C CA  . ASP B 384 ? 161.5365 161.5365 161.5365 0.0000 0.0000 0.0000 384 ASP B CA  
6947 C C   . ASP B 384 ? 161.4766 161.4766 161.4766 0.0000 0.0000 0.0000 384 ASP B C   
6948 O O   . ASP B 384 ? 161.5638 161.5638 161.5638 0.0000 0.0000 0.0000 384 ASP B O   
6949 C CB  . ASP B 384 ? 161.7789 161.7789 161.7789 0.0000 0.0000 0.0000 384 ASP B CB  
6950 C CG  . ASP B 384 ? 161.4471 161.4471 161.4471 0.0000 0.0000 0.0000 384 ASP B CG  
6951 O OD1 . ASP B 384 ? 161.3963 161.3963 161.3963 0.0000 0.0000 0.0000 384 ASP B OD1 
6952 O OD2 . ASP B 384 ? 161.4818 161.4818 161.4818 0.0000 0.0000 0.0000 384 ASP B OD2 
6953 N N   . VAL B 385 ? 163.3114 163.3114 163.3114 0.0000 0.0000 0.0000 385 VAL B N   
6954 C CA  . VAL B 385 ? 163.4656 163.4656 163.4656 0.0000 0.0000 0.0000 385 VAL B CA  
6955 C C   . VAL B 385 ? 163.5347 163.5347 163.5347 0.0000 0.0000 0.0000 385 VAL B C   
6956 O O   . VAL B 385 ? 163.8431 163.8431 163.8431 0.0000 0.0000 0.0000 385 VAL B O   
6957 C CB  . VAL B 385 ? 163.5831 163.5831 163.5831 0.0000 0.0000 0.0000 385 VAL B CB  
6958 C CG1 . VAL B 385 ? 163.5939 163.5939 163.5939 0.0000 0.0000 0.0000 385 VAL B CG1 
6959 C CG2 . VAL B 385 ? 163.5368 163.5368 163.5368 0.0000 0.0000 0.0000 385 VAL B CG2 
6960 N N   . ASP B 386 ? 161.4435 161.4435 161.4435 0.0000 0.0000 0.0000 386 ASP B N   
6961 C CA  . ASP B 386 ? 161.2917 161.2917 161.2917 0.0000 0.0000 0.0000 386 ASP B CA  
6962 C C   . ASP B 386 ? 161.3907 161.3907 161.3907 0.0000 0.0000 0.0000 386 ASP B C   
6963 O O   . ASP B 386 ? 161.5549 161.5549 161.5549 0.0000 0.0000 0.0000 386 ASP B O   
6964 C CB  . ASP B 386 ? 161.3145 161.3145 161.3145 0.0000 0.0000 0.0000 386 ASP B CB  
6965 C CG  . ASP B 386 ? 161.4794 161.4794 161.4794 0.0000 0.0000 0.0000 386 ASP B CG  
6966 O OD1 . ASP B 386 ? 161.4046 161.4046 161.4046 0.0000 0.0000 0.0000 386 ASP B OD1 
6967 O OD2 . ASP B 386 ? 161.3222 161.3222 161.3222 0.0000 0.0000 0.0000 386 ASP B OD2 
6968 N N   . PHE B 387 ? 161.2185 161.2185 161.2185 0.0000 0.0000 0.0000 387 PHE B N   
6969 C CA  . PHE B 387 ? 161.3191 161.3191 161.3191 0.0000 0.0000 0.0000 387 PHE B CA  
6970 C C   . PHE B 387 ? 161.5629 161.5629 161.5629 0.0000 0.0000 0.0000 387 PHE B C   
6971 O O   . PHE B 387 ? 161.3953 161.3953 161.3953 0.0000 0.0000 0.0000 387 PHE B O   
6972 C CB  . PHE B 387 ? 161.4311 161.4311 161.4311 0.0000 0.0000 0.0000 387 PHE B CB  
6973 C CG  . PHE B 387 ? 161.4253 161.4253 161.4253 0.0000 0.0000 0.0000 387 PHE B CG  
6974 C CD1 . PHE B 387 ? 161.5758 161.5758 161.5758 0.0000 0.0000 0.0000 387 PHE B CD1 
6975 C CD2 . PHE B 387 ? 161.5457 161.5457 161.5457 0.0000 0.0000 0.0000 387 PHE B CD2 
6976 C CE1 . PHE B 387 ? 161.4831 161.4831 161.4831 0.0000 0.0000 0.0000 387 PHE B CE1 
6977 C CE2 . PHE B 387 ? 161.4974 161.4974 161.4974 0.0000 0.0000 0.0000 387 PHE B CE2 
6978 C CZ  . PHE B 387 ? 161.2512 161.2512 161.2512 0.0000 0.0000 0.0000 387 PHE B CZ  
6979 N N   . THR B 388 ? 161.2741 161.2741 161.2741 0.0000 0.0000 0.0000 388 THR B N   
6980 C CA  . THR B 388 ? 161.3970 161.3970 161.3970 0.0000 0.0000 0.0000 388 THR B CA  
6981 C C   . THR B 388 ? 161.4933 161.4933 161.4933 0.0000 0.0000 0.0000 388 THR B C   
6982 O O   . THR B 388 ? 161.3290 161.3290 161.3290 0.0000 0.0000 0.0000 388 THR B O   
6983 C CB  . THR B 388 ? 161.4028 161.4028 161.4028 0.0000 0.0000 0.0000 388 THR B CB  
6984 O OG1 . THR B 388 ? 161.3936 161.3936 161.3936 0.0000 0.0000 0.0000 388 THR B OG1 
6985 C CG2 . THR B 388 ? 161.4527 161.4527 161.4527 0.0000 0.0000 0.0000 388 THR B CG2 
6986 N N   . PRO B 389 ? 161.5365 161.5365 161.5365 0.0000 0.0000 0.0000 389 PRO B N   
6987 C CA  . PRO B 389 ? 161.6779 161.6779 161.6779 0.0000 0.0000 0.0000 389 PRO B CA  
6988 C C   . PRO B 389 ? 161.6847 161.6847 161.6847 0.0000 0.0000 0.0000 389 PRO B C   
6989 O O   . PRO B 389 ? 162.6307 162.6307 162.6307 0.0000 0.0000 0.0000 389 PRO B O   
6990 C CB  . PRO B 389 ? 162.7197 162.7197 162.7197 0.0000 0.0000 0.0000 389 PRO B CB  
6991 C CG  . PRO B 389 ? 162.7505 162.7505 162.7505 0.0000 0.0000 0.0000 389 PRO B CG  
6992 C CD  . PRO B 389 ? 162.7827 162.7827 162.7827 0.0000 0.0000 0.0000 389 PRO B CD  
6993 N N   . PRO B 390 ? 162.6946 162.6946 162.6946 0.0000 0.0000 0.0000 390 PRO B N   
6994 C CA  . PRO B 390 ? 162.7712 162.7712 162.7712 0.0000 0.0000 0.0000 390 PRO B CA  
6995 C C   . PRO B 390 ? 162.7609 162.7609 162.7609 0.0000 0.0000 0.0000 390 PRO B C   
6996 O O   . PRO B 390 ? 162.6097 162.6097 162.6097 0.0000 0.0000 0.0000 390 PRO B O   
6997 C CB  . PRO B 390 ? 162.7372 162.7372 162.7372 0.0000 0.0000 0.0000 390 PRO B CB  
6998 C CG  . PRO B 390 ? 162.6923 162.6923 162.6923 0.0000 0.0000 0.0000 390 PRO B CG  
6999 C CD  . PRO B 390 ? 162.9497 162.9497 162.9497 0.0000 0.0000 0.0000 390 PRO B CD  
7000 N N   . PHE B 391 ? 161.5800 161.5800 161.5800 0.0000 0.0000 0.0000 391 PHE B N   
7001 C CA  . PHE B 391 ? 161.6372 161.6372 161.6372 0.0000 0.0000 0.0000 391 PHE B CA  
7002 C C   . PHE B 391 ? 161.9153 161.9153 161.9153 0.0000 0.0000 0.0000 391 PHE B C   
7003 O O   . PHE B 391 ? 161.9041 161.9041 161.9041 0.0000 0.0000 0.0000 391 PHE B O   
7004 C CB  . PHE B 391 ? 161.7475 161.7475 161.7475 0.0000 0.0000 0.0000 391 PHE B CB  
7005 C CG  . PHE B 391 ? 161.7432 161.7432 161.7432 0.0000 0.0000 0.0000 391 PHE B CG  
7006 C CD1 . PHE B 391 ? 161.8064 161.8064 161.8064 0.0000 0.0000 0.0000 391 PHE B CD1 
7007 C CD2 . PHE B 391 ? 161.7831 161.7831 161.7831 0.0000 0.0000 0.0000 391 PHE B CD2 
7008 C CE1 . PHE B 391 ? 170.9402 170.9402 170.9402 0.0000 0.0000 0.0000 391 PHE B CE1 
7009 C CE2 . PHE B 391 ? 171.1649 171.1649 171.1649 0.0000 0.0000 0.0000 391 PHE B CE2 
7010 C CZ  . PHE B 391 ? 171.3942 171.3942 171.3942 0.0000 0.0000 0.0000 391 PHE B CZ  
7011 N N   . ARG B 392 ? 171.9113 171.9113 171.9113 0.0000 0.0000 0.0000 392 ARG B N   
7012 C CA  . ARG B 392 ? 171.5564 171.5564 171.5564 0.0000 0.0000 0.0000 392 ARG B CA  
7013 C C   . ARG B 392 ? 171.3872 171.3872 171.3872 0.0000 0.0000 0.0000 392 ARG B C   
7014 O O   . ARG B 392 ? 171.4319 171.4319 171.4319 0.0000 0.0000 0.0000 392 ARG B O   
7015 C CB  . ARG B 392 ? 171.3446 171.3446 171.3446 0.0000 0.0000 0.0000 392 ARG B CB  
7016 C CG  . ARG B 392 ? 165.1860 165.1860 165.1860 0.0000 0.0000 0.0000 392 ARG B CG  
7017 C CD  . ARG B 392 ? 165.2022 165.2022 165.2022 0.0000 0.0000 0.0000 392 ARG B CD  
7018 N NE  . ARG B 392 ? 165.9951 165.9951 165.9951 0.0000 0.0000 0.0000 392 ARG B NE  
7019 C CZ  . ARG B 392 ? 166.2874 166.2874 166.2874 0.0000 0.0000 0.0000 392 ARG B CZ  
7020 N NH1 . ARG B 392 ? 164.9967 164.9967 164.9967 0.0000 0.0000 0.0000 392 ARG B NH1 
7021 N NH2 . ARG B 392 ? 165.0704 165.0704 165.0704 0.0000 0.0000 0.0000 392 ARG B NH2 
7022 N N   . ARG B 393 ? 164.9418 164.9418 164.9418 0.0000 0.0000 0.0000 393 ARG B N   
7023 C CA  . ARG B 393 ? 164.9898 164.9898 164.9898 0.0000 0.0000 0.0000 393 ARG B CA  
7024 C C   . ARG B 393 ? 178.6337 178.6337 178.6337 0.0000 0.0000 0.0000 393 ARG B C   
7025 O O   . ARG B 393 ? 178.9700 178.9700 178.9700 0.0000 0.0000 0.0000 393 ARG B O   
7026 C CB  . ARG B 393 ? 179.6471 179.6471 179.6471 0.0000 0.0000 0.0000 393 ARG B CB  
7027 C CG  . ARG B 393 ? 179.7167 179.7167 179.7167 0.0000 0.0000 0.0000 393 ARG B CG  
7028 C CD  . ARG B 393 ? 179.1851 179.1851 179.1851 0.0000 0.0000 0.0000 393 ARG B CD  
7029 N NE  . ARG B 393 ? 179.3665 179.3665 179.3665 0.0000 0.0000 0.0000 393 ARG B NE  
7030 C CZ  . ARG B 393 ? 178.8878 178.8878 178.8878 0.0000 0.0000 0.0000 393 ARG B CZ  
7031 N NH1 . ARG B 393 ? 197.4450 197.4450 197.4450 0.0000 0.0000 0.0000 393 ARG B NH1 
7032 N NH2 . ARG B 393 ? 198.0302 198.0302 198.0302 0.0000 0.0000 0.0000 393 ARG B NH2 
7033 N N   . ILE B 394 ? 198.0140 198.0140 198.0140 0.0000 0.0000 0.0000 394 ILE B N   
7034 C CA  . ILE B 394 ? 198.4138 198.4138 198.4138 0.0000 0.0000 0.0000 394 ILE B CA  
7035 C C   . ILE B 394 ? 198.4537 198.4537 198.4537 0.0000 0.0000 0.0000 394 ILE B C   
7036 O O   . ILE B 394 ? 198.6138 198.6138 198.6138 0.0000 0.0000 0.0000 394 ILE B O   
7037 C CB  . ILE B 394 ? 198.4926 198.4926 198.4926 0.0000 0.0000 0.0000 394 ILE B CB  
7038 C CG1 . ILE B 394 ? 198.1625 198.1625 198.1625 0.0000 0.0000 0.0000 394 ILE B CG1 
7039 C CG2 . ILE B 394 ? 198.6623 198.6623 198.6623 0.0000 0.0000 0.0000 394 ILE B CG2 
7040 C CD1 . ILE B 394 ? 191.0480 191.0480 191.0480 0.0000 0.0000 0.0000 394 ILE B CD1 
7041 N N   . ASN B 395 ? 191.0602 191.0602 191.0602 0.0000 0.0000 0.0000 395 ASN B N   
7042 C CA  . ASN B 395 ? 190.8898 190.8898 190.8898 0.0000 0.0000 0.0000 395 ASN B CA  
7043 C C   . ASN B 395 ? 191.2824 191.2824 191.2824 0.0000 0.0000 0.0000 395 ASN B C   
7044 O O   . ASN B 395 ? 190.8841 190.8841 190.8841 0.0000 0.0000 0.0000 395 ASN B O   
7045 C CB  . ASN B 395 ? 190.8700 190.8700 190.8700 0.0000 0.0000 0.0000 395 ASN B CB  
7046 C CG  . ASN B 395 ? 191.3196 191.3196 191.3196 0.0000 0.0000 0.0000 395 ASN B CG  
7047 O OD1 . ASN B 395 ? 191.3583 191.3583 191.3583 0.0000 0.0000 0.0000 395 ASN B OD1 
7048 N ND2 . ASN B 395 ? 191.3792 191.3792 191.3792 0.0000 0.0000 0.0000 395 ASN B ND2 
7049 N N   . MET B 396 ? 179.9148 179.9148 179.9148 0.0000 0.0000 0.0000 396 MET B N   
7050 C CA  . MET B 396 ? 179.6994 179.6994 179.6994 0.0000 0.0000 0.0000 396 MET B CA  
7051 C C   . MET B 396 ? 180.4611 180.4611 180.4611 0.0000 0.0000 0.0000 396 MET B C   
7052 O O   . MET B 396 ? 180.4822 180.4822 180.4822 0.0000 0.0000 0.0000 396 MET B O   
7053 C CB  . MET B 396 ? 179.4313 179.4313 179.4313 0.0000 0.0000 0.0000 396 MET B CB  
7054 C CG  . MET B 396 ? 179.3720 179.3720 179.3720 0.0000 0.0000 0.0000 396 MET B CG  
7055 S SD  . MET B 396 ? 179.3346 179.3346 179.3346 0.0000 0.0000 0.0000 396 MET B SD  
7056 C CE  . MET B 396 ? 179.2931 179.2931 179.2931 0.0000 0.0000 0.0000 396 MET B CE  
7057 N N   . VAL B 397 ? 197.8034 197.8034 197.8034 0.0000 0.0000 0.0000 397 VAL B N   
7058 C CA  . VAL B 397 ? 198.3275 198.3275 198.3275 0.0000 0.0000 0.0000 397 VAL B CA  
7059 C C   . VAL B 397 ? 198.3788 198.3788 198.3788 0.0000 0.0000 0.0000 397 VAL B C   
7060 O O   . VAL B 397 ? 198.7178 198.7178 198.7178 0.0000 0.0000 0.0000 397 VAL B O   
7061 C CB  . VAL B 397 ? 198.5711 198.5711 198.5711 0.0000 0.0000 0.0000 397 VAL B CB  
7062 C CG1 . VAL B 397 ? 198.7344 198.7344 198.7344 0.0000 0.0000 0.0000 397 VAL B CG1 
7063 C CG2 . VAL B 397 ? 198.7629 198.7629 198.7629 0.0000 0.0000 0.0000 397 VAL B CG2 
7064 N N   . GLU B 398 ? 198.6295 198.6295 198.6295 0.0000 0.0000 0.0000 398 GLU B N   
7065 C CA  . GLU B 398 ? 198.9047 198.9047 198.9047 0.0000 0.0000 0.0000 398 GLU B CA  
7066 C C   . GLU B 398 ? 195.6620 195.6620 195.6620 0.0000 0.0000 0.0000 398 GLU B C   
7067 O O   . GLU B 398 ? 195.7194 195.7194 195.7194 0.0000 0.0000 0.0000 398 GLU B O   
7068 C CB  . GLU B 398 ? 195.7677 195.7677 195.7677 0.0000 0.0000 0.0000 398 GLU B CB  
7069 C CG  . GLU B 398 ? 195.8513 195.8513 195.8513 0.0000 0.0000 0.0000 398 GLU B CG  
7070 C CD  . GLU B 398 ? 195.7501 195.7501 195.7501 0.0000 0.0000 0.0000 398 GLU B CD  
7071 O OE1 . GLU B 398 ? 195.7983 195.7983 195.7983 0.0000 0.0000 0.0000 398 GLU B OE1 
7072 O OE2 . GLU B 398 ? 195.8401 195.8401 195.8401 0.0000 0.0000 0.0000 398 GLU B OE2 
7073 N N   . GLU B 399 ? 195.8777 195.8777 195.8777 0.0000 0.0000 0.0000 399 GLU B N   
7074 C CA  . GLU B 399 ? 195.8715 195.8715 195.8715 0.0000 0.0000 0.0000 399 GLU B CA  
7075 C C   . GLU B 399 ? 194.3382 194.3382 194.3382 0.0000 0.0000 0.0000 399 GLU B C   
7076 O O   . GLU B 399 ? 194.3289 194.3289 194.3289 0.0000 0.0000 0.0000 399 GLU B O   
7077 C CB  . GLU B 399 ? 194.5027 194.5027 194.5027 0.0000 0.0000 0.0000 399 GLU B CB  
7078 C CG  . GLU B 399 ? 194.5628 194.5628 194.5628 0.0000 0.0000 0.0000 399 GLU B CG  
7079 C CD  . GLU B 399 ? 194.2191 194.2191 194.2191 0.0000 0.0000 0.0000 399 GLU B CD  
7080 O OE1 . GLU B 399 ? 198.5072 198.5072 198.5072 0.0000 0.0000 0.0000 399 GLU B OE1 
7081 O OE2 . GLU B 399 ? 198.6140 198.6140 198.6140 0.0000 0.0000 0.0000 399 GLU B OE2 
7082 N N   . LEU B 400 ? 198.8281 198.8281 198.8281 0.0000 0.0000 0.0000 400 LEU B N   
7083 C CA  . LEU B 400 ? 198.8768 198.8768 198.8768 0.0000 0.0000 0.0000 400 LEU B CA  
7084 C C   . LEU B 400 ? 198.6994 198.6994 198.6994 0.0000 0.0000 0.0000 400 LEU B C   
7085 O O   . LEU B 400 ? 198.4724 198.4724 198.4724 0.0000 0.0000 0.0000 400 LEU B O   
7086 C CB  . LEU B 400 ? 198.3987 198.3987 198.3987 0.0000 0.0000 0.0000 400 LEU B CB  
7087 C CG  . LEU B 400 ? 198.5251 198.5251 198.5251 0.0000 0.0000 0.0000 400 LEU B CG  
7088 C CD1 . LEU B 400 ? 204.5968 204.5968 204.5968 0.0000 0.0000 0.0000 400 LEU B CD1 
7089 C CD2 . LEU B 400 ? 204.8303 204.8303 204.8303 0.0000 0.0000 0.0000 400 LEU B CD2 
7090 N N   . GLU B 401 ? 205.0760 205.0760 205.0760 0.0000 0.0000 0.0000 401 GLU B N   
7091 C CA  . GLU B 401 ? 205.1595 205.1595 205.1595 0.0000 0.0000 0.0000 401 GLU B CA  
7092 C C   . GLU B 401 ? 212.6090 212.6090 212.6090 0.0000 0.0000 0.0000 401 GLU B C   
7093 O O   . GLU B 401 ? 212.8655 212.8655 212.8655 0.0000 0.0000 0.0000 401 GLU B O   
7094 C CB  . GLU B 401 ? 212.7648 212.7648 212.7648 0.0000 0.0000 0.0000 401 GLU B CB  
7095 C CG  . GLU B 401 ? 212.7223 212.7223 212.7223 0.0000 0.0000 0.0000 401 GLU B CG  
7096 C CD  . GLU B 401 ? 212.8895 212.8895 212.8895 0.0000 0.0000 0.0000 401 GLU B CD  
7097 O OE1 . GLU B 401 ? 212.8254 212.8254 212.8254 0.0000 0.0000 0.0000 401 GLU B OE1 
7098 O OE2 . GLU B 401 ? 212.9178 212.9178 212.9178 0.0000 0.0000 0.0000 401 GLU B OE2 
7099 N N   . LYS B 402 ? 213.0206 213.0206 213.0206 0.0000 0.0000 0.0000 402 LYS B N   
7100 C CA  . LYS B 402 ? 205.7950 205.7950 205.7950 0.0000 0.0000 0.0000 402 LYS B CA  
7101 C C   . LYS B 402 ? 205.5968 205.5968 205.5968 0.0000 0.0000 0.0000 402 LYS B C   
7102 O O   . LYS B 402 ? 205.4877 205.4877 205.4877 0.0000 0.0000 0.0000 402 LYS B O   
7103 C CB  . LYS B 402 ? 205.5170 205.5170 205.5170 0.0000 0.0000 0.0000 402 LYS B CB  
7104 C CG  . LYS B 402 ? 205.5986 205.5986 205.5986 0.0000 0.0000 0.0000 402 LYS B CG  
7105 C CD  . LYS B 402 ? 205.6167 205.6167 205.6167 0.0000 0.0000 0.0000 402 LYS B CD  
7106 C CE  . LYS B 402 ? 205.6676 205.6676 205.6676 0.0000 0.0000 0.0000 402 LYS B CE  
7107 N NZ  . LYS B 402 ? 205.7054 205.7054 205.7054 0.0000 0.0000 0.0000 402 LYS B NZ  
7108 N N   . ALA B 403 ? 205.7199 205.7199 205.7199 0.0000 0.0000 0.0000 403 ALA B N   
7109 C CA  . ALA B 403 ? 202.1542 202.1542 202.1542 0.0000 0.0000 0.0000 403 ALA B CA  
7110 C C   . ALA B 403 ? 202.1574 202.1574 202.1574 0.0000 0.0000 0.0000 403 ALA B C   
7111 O O   . ALA B 403 ? 202.3654 202.3654 202.3654 0.0000 0.0000 0.0000 403 ALA B O   
7112 C CB  . ALA B 403 ? 202.3417 202.3417 202.3417 0.0000 0.0000 0.0000 403 ALA B CB  
7113 N N   . LEU B 404 ? 202.1308 202.1308 202.1308 0.0000 0.0000 0.0000 404 LEU B N   
7114 C CA  . LEU B 404 ? 202.0882 202.0882 202.0882 0.0000 0.0000 0.0000 404 LEU B CA  
7115 C C   . LEU B 404 ? 202.1622 202.1622 202.1622 0.0000 0.0000 0.0000 404 LEU B C   
7116 O O   . LEU B 404 ? 202.0650 202.0650 202.0650 0.0000 0.0000 0.0000 404 LEU B O   
7117 C CB  . LEU B 404 ? 209.2955 209.2955 209.2955 0.0000 0.0000 0.0000 404 LEU B CB  
7118 C CG  . LEU B 404 ? 209.3957 209.3957 209.3957 0.0000 0.0000 0.0000 404 LEU B CG  
7119 C CD1 . LEU B 404 ? 209.3291 209.3291 209.3291 0.0000 0.0000 0.0000 404 LEU B CD1 
7120 C CD2 . LEU B 404 ? 209.2631 209.2631 209.2631 0.0000 0.0000 0.0000 404 LEU B CD2 
7121 N N   . GLY B 405 ? 209.4964 209.4964 209.4964 0.0000 0.0000 0.0000 405 GLY B N   
7122 C CA  . GLY B 405 ? 209.4977 209.4977 209.4977 0.0000 0.0000 0.0000 405 GLY B CA  
7123 C C   . GLY B 405 ? 209.4320 209.4320 209.4320 0.0000 0.0000 0.0000 405 GLY B C   
7124 O O   . GLY B 405 ? 209.3044 209.3044 209.3044 0.0000 0.0000 0.0000 405 GLY B O   
7125 N N   . MET B 406 ? 209.0422 209.0422 209.0422 0.0000 0.0000 0.0000 406 MET B N   
7126 C CA  . MET B 406 ? 208.5389 208.5389 208.5389 0.0000 0.0000 0.0000 406 MET B CA  
7127 C C   . MET B 406 ? 208.5911 208.5911 208.5911 0.0000 0.0000 0.0000 406 MET B C   
7128 O O   . MET B 406 ? 209.1369 209.1369 209.1369 0.0000 0.0000 0.0000 406 MET B O   
7129 C CB  . MET B 406 ? 209.4077 209.4077 209.4077 0.0000 0.0000 0.0000 406 MET B CB  
7130 C CG  . MET B 406 ? 209.4241 209.4241 209.4241 0.0000 0.0000 0.0000 406 MET B CG  
7131 S SD  . MET B 406 ? 209.4729 209.4729 209.4729 0.0000 0.0000 0.0000 406 MET B SD  
7132 C CE  . MET B 406 ? 209.4227 209.4227 209.4227 0.0000 0.0000 0.0000 406 MET B CE  
7133 N N   . LYS B 407 ? 187.7684 187.7684 187.7684 0.0000 0.0000 0.0000 407 LYS B N   
7134 C CA  . LYS B 407 ? 187.3313 187.3313 187.3313 0.0000 0.0000 0.0000 407 LYS B CA  
7135 C C   . LYS B 407 ? 187.1354 187.1354 187.1354 0.0000 0.0000 0.0000 407 LYS B C   
7136 O O   . LYS B 407 ? 187.0117 187.0117 187.0117 0.0000 0.0000 0.0000 407 LYS B O   
7137 C CB  . LYS B 407 ? 186.8031 186.8031 186.8031 0.0000 0.0000 0.0000 407 LYS B CB  
7138 C CG  . LYS B 407 ? 186.7160 186.7160 186.7160 0.0000 0.0000 0.0000 407 LYS B CG  
7139 C CD  . LYS B 407 ? 186.9497 186.9497 186.9497 0.0000 0.0000 0.0000 407 LYS B CD  
7140 C CE  . LYS B 407 ? 190.5686 190.5686 190.5686 0.0000 0.0000 0.0000 407 LYS B CE  
7141 N NZ  . LYS B 407 ? 190.4764 190.4764 190.4764 0.0000 0.0000 0.0000 407 LYS B NZ  
7142 N N   . LEU B 408 ? 190.8865 190.8865 190.8865 0.0000 0.0000 0.0000 408 LEU B N   
7143 C CA  . LEU B 408 ? 190.7854 190.7854 190.7854 0.0000 0.0000 0.0000 408 LEU B CA  
7144 C C   . LEU B 408 ? 190.4363 190.4363 190.4363 0.0000 0.0000 0.0000 408 LEU B C   
7145 O O   . LEU B 408 ? 190.7056 190.7056 190.7056 0.0000 0.0000 0.0000 408 LEU B O   
7146 C CB  . LEU B 408 ? 190.8697 190.8697 190.8697 0.0000 0.0000 0.0000 408 LEU B CB  
7147 C CG  . LEU B 408 ? 190.7469 190.7469 190.7469 0.0000 0.0000 0.0000 408 LEU B CG  
7148 C CD1 . LEU B 408 ? 198.4092 198.4092 198.4092 0.0000 0.0000 0.0000 408 LEU B CD1 
7149 C CD2 . LEU B 408 ? 198.6573 198.6573 198.6573 0.0000 0.0000 0.0000 408 LEU B CD2 
7150 N N   . PRO B 409 ? 198.8271 198.8271 198.8271 0.0000 0.0000 0.0000 409 PRO B N   
7151 C CA  . PRO B 409 ? 199.1481 199.1481 199.1481 0.0000 0.0000 0.0000 409 PRO B CA  
7152 C C   . PRO B 409 ? 198.8187 198.8187 198.8187 0.0000 0.0000 0.0000 409 PRO B C   
7153 O O   . PRO B 409 ? 198.7456 198.7456 198.7456 0.0000 0.0000 0.0000 409 PRO B O   
7154 C CB  . PRO B 409 ? 198.8502 198.8502 198.8502 0.0000 0.0000 0.0000 409 PRO B CB  
7155 C CG  . PRO B 409 ? 198.7223 198.7223 198.7223 0.0000 0.0000 0.0000 409 PRO B CG  
7156 C CD  . PRO B 409 ? 196.4717 196.4717 196.4717 0.0000 0.0000 0.0000 409 PRO B CD  
7157 N N   . GLU B 410 ? 196.5074 196.5074 196.5074 0.0000 0.0000 0.0000 410 GLU B N   
7158 C CA  . GLU B 410 ? 196.6294 196.6294 196.6294 0.0000 0.0000 0.0000 410 GLU B CA  
7159 C C   . GLU B 410 ? 196.3899 196.3899 196.3899 0.0000 0.0000 0.0000 410 GLU B C   
7160 O O   . GLU B 410 ? 196.1066 196.1066 196.1066 0.0000 0.0000 0.0000 410 GLU B O   
7161 C CB  . GLU B 410 ? 196.1111 196.1111 196.1111 0.0000 0.0000 0.0000 410 GLU B CB  
7162 C CG  . GLU B 410 ? 196.2730 196.2730 196.2730 0.0000 0.0000 0.0000 410 GLU B CG  
7163 C CD  . GLU B 410 ? 195.8739 195.8739 195.8739 0.0000 0.0000 0.0000 410 GLU B CD  
7164 O OE1 . GLU B 410 ? 196.3898 196.3898 196.3898 0.0000 0.0000 0.0000 410 GLU B OE1 
7165 O OE2 . GLU B 410 ? 195.9488 195.9488 195.9488 0.0000 0.0000 0.0000 410 GLU B OE2 
7166 N N   . THR B 411 ? 196.1858 196.1858 196.1858 0.0000 0.0000 0.0000 411 THR B N   
7167 C CA  . THR B 411 ? 210.0167 210.0167 210.0167 0.0000 0.0000 0.0000 411 THR B CA  
7168 C C   . THR B 411 ? 210.3480 210.3480 210.3480 0.0000 0.0000 0.0000 411 THR B C   
7169 O O   . THR B 411 ? 210.6645 210.6645 210.6645 0.0000 0.0000 0.0000 411 THR B O   
7170 C CB  . THR B 411 ? 210.6714 210.6714 210.6714 0.0000 0.0000 0.0000 411 THR B CB  
7171 O OG1 . THR B 411 ? 210.4615 210.4615 210.4615 0.0000 0.0000 0.0000 411 THR B OG1 
7172 C CG2 . THR B 411 ? 210.4821 210.4821 210.4821 0.0000 0.0000 0.0000 411 THR B CG2 
7173 N N   . ASN B 412 ? 210.4889 210.4889 210.4889 0.0000 0.0000 0.0000 412 ASN B N   
7174 C CA  . ASN B 412 ? 210.4949 210.4949 210.4949 0.0000 0.0000 0.0000 412 ASN B CA  
7175 C C   . ASN B 412 ? 210.1257 210.1257 210.1257 0.0000 0.0000 0.0000 412 ASN B C   
7176 O O   . ASN B 412 ? 215.4145 215.4145 215.4145 0.0000 0.0000 0.0000 412 ASN B O   
7177 C CB  . ASN B 412 ? 215.8167 215.8167 215.8167 0.0000 0.0000 0.0000 412 ASN B CB  
7178 C CG  . ASN B 412 ? 216.1017 216.1017 216.1017 0.0000 0.0000 0.0000 412 ASN B CG  
7179 O OD1 . ASN B 412 ? 215.8450 215.8450 215.8450 0.0000 0.0000 0.0000 412 ASN B OD1 
7180 N ND2 . ASN B 412 ? 215.9195 215.9195 215.9195 0.0000 0.0000 0.0000 412 ASN B ND2 
7181 N N   . LEU B 413 ? 215.8866 215.8866 215.8866 0.0000 0.0000 0.0000 413 LEU B N   
7182 C CA  . LEU B 413 ? 215.7397 215.7397 215.7397 0.0000 0.0000 0.0000 413 LEU B CA  
7183 C C   . LEU B 413 ? 227.8459 227.8459 227.8459 0.0000 0.0000 0.0000 413 LEU B C   
7184 O O   . LEU B 413 ? 228.0867 228.0867 228.0867 0.0000 0.0000 0.0000 413 LEU B O   
7185 C CB  . LEU B 413 ? 228.0931 228.0931 228.0931 0.0000 0.0000 0.0000 413 LEU B CB  
7186 C CG  . LEU B 413 ? 228.0183 228.0183 228.0183 0.0000 0.0000 0.0000 413 LEU B CG  
7187 C CD1 . LEU B 413 ? 228.2969 228.2969 228.2969 0.0000 0.0000 0.0000 413 LEU B CD1 
7188 C CD2 . LEU B 413 ? 228.3512 228.3512 228.3512 0.0000 0.0000 0.0000 413 LEU B CD2 
7189 N N   . PHE B 414 ? 228.2716 228.2716 228.2716 0.0000 0.0000 0.0000 414 PHE B N   
7190 C CA  . PHE B 414 ? 228.2883 228.2883 228.2883 0.0000 0.0000 0.0000 414 PHE B CA  
7191 C C   . PHE B 414 ? 228.1113 228.1113 228.1113 0.0000 0.0000 0.0000 414 PHE B C   
7192 O O   . PHE B 414 ? 231.2729 231.2729 231.2729 0.0000 0.0000 0.0000 414 PHE B O   
7193 C CB  . PHE B 414 ? 231.4210 231.4210 231.4210 0.0000 0.0000 0.0000 414 PHE B CB  
7194 C CG  . PHE B 414 ? 230.9534 230.9534 230.9534 0.0000 0.0000 0.0000 414 PHE B CG  
7195 C CD1 . PHE B 414 ? 230.8686 230.8686 230.8686 0.0000 0.0000 0.0000 414 PHE B CD1 
7196 C CD2 . PHE B 414 ? 231.6448 231.6448 231.6448 0.0000 0.0000 0.0000 414 PHE B CD2 
7197 C CE1 . PHE B 414 ? 231.6372 231.6372 231.6372 0.0000 0.0000 0.0000 414 PHE B CE1 
7198 C CE2 . PHE B 414 ? 231.5676 231.5676 231.5676 0.0000 0.0000 0.0000 414 PHE B CE2 
7199 C CZ  . PHE B 414 ? 231.4784 231.4784 231.4784 0.0000 0.0000 0.0000 414 PHE B CZ  
7200 N N   . GLU B 415 ? 231.5353 231.5353 231.5353 0.0000 0.0000 0.0000 415 GLU B N   
7201 C CA  . GLU B 415 ? 217.7016 217.7016 217.7016 0.0000 0.0000 0.0000 415 GLU B CA  
7202 C C   . GLU B 415 ? 217.3180 217.3180 217.3180 0.0000 0.0000 0.0000 415 GLU B C   
7203 O O   . GLU B 415 ? 217.0795 217.0795 217.0795 0.0000 0.0000 0.0000 415 GLU B O   
7204 C CB  . GLU B 415 ? 216.9704 216.9704 216.9704 0.0000 0.0000 0.0000 415 GLU B CB  
7205 C CG  . GLU B 415 ? 217.1294 217.1294 217.1294 0.0000 0.0000 0.0000 415 GLU B CG  
7206 C CD  . GLU B 415 ? 216.8986 216.8986 216.8986 0.0000 0.0000 0.0000 415 GLU B CD  
7207 O OE1 . GLU B 415 ? 216.9858 216.9858 216.9858 0.0000 0.0000 0.0000 415 GLU B OE1 
7208 O OE2 . GLU B 415 ? 211.7502 211.7502 211.7502 0.0000 0.0000 0.0000 415 GLU B OE2 
7209 N N   . THR B 416 ? 211.5306 211.5306 211.5306 0.0000 0.0000 0.0000 416 THR B N   
7210 C CA  . THR B 416 ? 211.5527 211.5527 211.5527 0.0000 0.0000 0.0000 416 THR B CA  
7211 C C   . THR B 416 ? 211.4289 211.4289 211.4289 0.0000 0.0000 0.0000 416 THR B C   
7212 O O   . THR B 416 ? 211.5062 211.5062 211.5062 0.0000 0.0000 0.0000 416 THR B O   
7213 C CB  . THR B 416 ? 211.1733 211.1733 211.1733 0.0000 0.0000 0.0000 416 THR B CB  
7214 O OG1 . THR B 416 ? 211.3118 211.3118 211.3118 0.0000 0.0000 0.0000 416 THR B OG1 
7215 C CG2 . THR B 416 ? 211.5108 211.5108 211.5108 0.0000 0.0000 0.0000 416 THR B CG2 
7216 N N   . GLU B 417 ? 211.4476 211.4476 211.4476 0.0000 0.0000 0.0000 417 GLU B N   
7217 C CA  . GLU B 417 ? 211.3258 211.3258 211.3258 0.0000 0.0000 0.0000 417 GLU B CA  
7218 C C   . GLU B 417 ? 211.5306 211.5306 211.5306 0.0000 0.0000 0.0000 417 GLU B C   
7219 O O   . GLU B 417 ? 215.7861 215.7861 215.7861 0.0000 0.0000 0.0000 417 GLU B O   
7220 C CB  . GLU B 417 ? 215.8126 215.8126 215.8126 0.0000 0.0000 0.0000 417 GLU B CB  
7221 C CG  . GLU B 417 ? 215.6184 215.6184 215.6184 0.0000 0.0000 0.0000 417 GLU B CG  
7222 C CD  . GLU B 417 ? 215.7033 215.7033 215.7033 0.0000 0.0000 0.0000 417 GLU B CD  
7223 O OE1 . GLU B 417 ? 215.9823 215.9823 215.9823 0.0000 0.0000 0.0000 417 GLU B OE1 
7224 O OE2 . GLU B 417 ? 215.9620 215.9620 215.9620 0.0000 0.0000 0.0000 417 GLU B OE2 
7225 N N   . GLU B 418 ? 215.9471 215.9471 215.9471 0.0000 0.0000 0.0000 418 GLU B N   
7226 C CA  . GLU B 418 ? 215.9154 215.9154 215.9154 0.0000 0.0000 0.0000 418 GLU B CA  
7227 C C   . GLU B 418 ? 215.9020 215.9020 215.9020 0.0000 0.0000 0.0000 418 GLU B C   
7228 O O   . GLU B 418 ? 208.8007 208.8007 208.8007 0.0000 0.0000 0.0000 418 GLU B O   
7229 C CB  . GLU B 418 ? 208.6916 208.6916 208.6916 0.0000 0.0000 0.0000 418 GLU B CB  
7230 C CG  . GLU B 418 ? 208.6235 208.6235 208.6235 0.0000 0.0000 0.0000 418 GLU B CG  
7231 C CD  . GLU B 418 ? 208.4942 208.4942 208.4942 0.0000 0.0000 0.0000 418 GLU B CD  
7232 O OE1 . GLU B 418 ? 208.6323 208.6323 208.6323 0.0000 0.0000 0.0000 418 GLU B OE1 
7233 O OE2 . GLU B 418 ? 208.6208 208.6208 208.6208 0.0000 0.0000 0.0000 418 GLU B OE2 
7234 N N   . THR B 419 ? 208.4915 208.4915 208.4915 0.0000 0.0000 0.0000 419 THR B N   
7235 C CA  . THR B 419 ? 208.5697 208.5697 208.5697 0.0000 0.0000 0.0000 419 THR B CA  
7236 C C   . THR B 419 ? 207.5234 207.5234 207.5234 0.0000 0.0000 0.0000 419 THR B C   
7237 O O   . THR B 419 ? 207.3432 207.3432 207.3432 0.0000 0.0000 0.0000 419 THR B O   
7238 C CB  . THR B 419 ? 207.2965 207.2965 207.2965 0.0000 0.0000 0.0000 419 THR B CB  
7239 O OG1 . THR B 419 ? 207.1698 207.1698 207.1698 0.0000 0.0000 0.0000 419 THR B OG1 
7240 C CG2 . THR B 419 ? 207.2326 207.2326 207.2326 0.0000 0.0000 0.0000 419 THR B CG2 
7241 N N   . ARG B 420 ? 207.2578 207.2578 207.2578 0.0000 0.0000 0.0000 420 ARG B N   
7242 C CA  . ARG B 420 ? 206.7701 206.7701 206.7701 0.0000 0.0000 0.0000 420 ARG B CA  
7243 C C   . ARG B 420 ? 207.1836 207.1836 207.1836 0.0000 0.0000 0.0000 420 ARG B C   
7244 O O   . ARG B 420 ? 209.4810 209.4810 209.4810 0.0000 0.0000 0.0000 420 ARG B O   
7245 C CB  . ARG B 420 ? 209.4633 209.4633 209.4633 0.0000 0.0000 0.0000 420 ARG B CB  
7246 C CG  . ARG B 420 ? 209.5962 209.5962 209.5962 0.0000 0.0000 0.0000 420 ARG B CG  
7247 C CD  . ARG B 420 ? 209.5710 209.5710 209.5710 0.0000 0.0000 0.0000 420 ARG B CD  
7248 N NE  . ARG B 420 ? 209.6067 209.6067 209.6067 0.0000 0.0000 0.0000 420 ARG B NE  
7249 C CZ  . ARG B 420 ? 209.5292 209.5292 209.5292 0.0000 0.0000 0.0000 420 ARG B CZ  
7250 N NH1 . ARG B 420 ? 209.3844 209.3844 209.3844 0.0000 0.0000 0.0000 420 ARG B NH1 
7251 N NH2 . ARG B 420 ? 209.5944 209.5944 209.5944 0.0000 0.0000 0.0000 420 ARG B NH2 
7252 N N   . LYS B 421 ? 215.1712 215.1712 215.1712 0.0000 0.0000 0.0000 421 LYS B N   
7253 C CA  . LYS B 421 ? 215.3437 215.3437 215.3437 0.0000 0.0000 0.0000 421 LYS B CA  
7254 C C   . LYS B 421 ? 215.0455 215.0455 215.0455 0.0000 0.0000 0.0000 421 LYS B C   
7255 O O   . LYS B 421 ? 215.1228 215.1228 215.1228 0.0000 0.0000 0.0000 421 LYS B O   
7256 C CB  . LYS B 421 ? 215.5367 215.5367 215.5367 0.0000 0.0000 0.0000 421 LYS B CB  
7257 C CG  . LYS B 421 ? 215.5582 215.5582 215.5582 0.0000 0.0000 0.0000 421 LYS B CG  
7258 C CD  . LYS B 421 ? 215.5659 215.5659 215.5659 0.0000 0.0000 0.0000 421 LYS B CD  
7259 C CE  . LYS B 421 ? 215.5940 215.5940 215.5940 0.0000 0.0000 0.0000 421 LYS B CE  
7260 N NZ  . LYS B 421 ? 206.1906 206.1906 206.1906 0.0000 0.0000 0.0000 421 LYS B NZ  
7261 N N   . ILE B 422 ? 206.0411 206.0411 206.0411 0.0000 0.0000 0.0000 422 ILE B N   
7262 C CA  . ILE B 422 ? 205.8990 205.8990 205.8990 0.0000 0.0000 0.0000 422 ILE B CA  
7263 C C   . ILE B 422 ? 205.8387 205.8387 205.8387 0.0000 0.0000 0.0000 422 ILE B C   
7264 O O   . ILE B 422 ? 205.9600 205.9600 205.9600 0.0000 0.0000 0.0000 422 ILE B O   
7265 C CB  . ILE B 422 ? 206.0292 206.0292 206.0292 0.0000 0.0000 0.0000 422 ILE B CB  
7266 C CG1 . ILE B 422 ? 205.8767 205.8767 205.8767 0.0000 0.0000 0.0000 422 ILE B CG1 
7267 C CG2 . ILE B 422 ? 206.0566 206.0566 206.0566 0.0000 0.0000 0.0000 422 ILE B CG2 
7268 C CD1 . ILE B 422 ? 200.5547 200.5547 200.5547 0.0000 0.0000 0.0000 422 ILE B CD1 
7269 N N   . LEU B 423 ? 200.3464 200.3464 200.3464 0.0000 0.0000 0.0000 423 LEU B N   
7270 C CA  . LEU B 423 ? 200.5451 200.5451 200.5451 0.0000 0.0000 0.0000 423 LEU B CA  
7271 C C   . LEU B 423 ? 200.4231 200.4231 200.4231 0.0000 0.0000 0.0000 423 LEU B C   
7272 O O   . LEU B 423 ? 200.2868 200.2868 200.2868 0.0000 0.0000 0.0000 423 LEU B O   
7273 C CB  . LEU B 423 ? 199.6668 199.6668 199.6668 0.0000 0.0000 0.0000 423 LEU B CB  
7274 C CG  . LEU B 423 ? 207.0991 207.0991 207.0991 0.0000 0.0000 0.0000 423 LEU B CG  
7275 C CD1 . LEU B 423 ? 207.1423 207.1423 207.1423 0.0000 0.0000 0.0000 423 LEU B CD1 
7276 C CD2 . LEU B 423 ? 207.0769 207.0769 207.0769 0.0000 0.0000 0.0000 423 LEU B CD2 
7277 N N   . ASP B 424 ? 207.1189 207.1189 207.1189 0.0000 0.0000 0.0000 424 ASP B N   
7278 C CA  . ASP B 424 ? 207.2287 207.2287 207.2287 0.0000 0.0000 0.0000 424 ASP B CA  
7279 C C   . ASP B 424 ? 207.2845 207.2845 207.2845 0.0000 0.0000 0.0000 424 ASP B C   
7280 O O   . ASP B 424 ? 207.2106 207.2106 207.2106 0.0000 0.0000 0.0000 424 ASP B O   
7281 C CB  . ASP B 424 ? 203.7927 203.7927 203.7927 0.0000 0.0000 0.0000 424 ASP B CB  
7282 C CG  . ASP B 424 ? 203.6881 203.6881 203.6881 0.0000 0.0000 0.0000 424 ASP B CG  
7283 O OD1 . ASP B 424 ? 203.5362 203.5362 203.5362 0.0000 0.0000 0.0000 424 ASP B OD1 
7284 O OD2 . ASP B 424 ? 203.5032 203.5032 203.5032 0.0000 0.0000 0.0000 424 ASP B OD2 
7285 N N   . ASP B 425 ? 203.7814 203.7814 203.7814 0.0000 0.0000 0.0000 425 ASP B N   
7286 C CA  . ASP B 425 ? 201.0158 201.0158 201.0158 0.0000 0.0000 0.0000 425 ASP B CA  
7287 C C   . ASP B 425 ? 200.9139 200.9139 200.9139 0.0000 0.0000 0.0000 425 ASP B C   
7288 O O   . ASP B 425 ? 200.8746 200.8746 200.8746 0.0000 0.0000 0.0000 425 ASP B O   
7289 C CB  . ASP B 425 ? 200.8357 200.8357 200.8357 0.0000 0.0000 0.0000 425 ASP B CB  
7290 C CG  . ASP B 425 ? 200.8198 200.8198 200.8198 0.0000 0.0000 0.0000 425 ASP B CG  
7291 O OD1 . ASP B 425 ? 200.8442 200.8442 200.8442 0.0000 0.0000 0.0000 425 ASP B OD1 
7292 O OD2 . ASP B 425 ? 200.8505 200.8505 200.8505 0.0000 0.0000 0.0000 425 ASP B OD2 
7293 N N   . ILE B 426 ? 200.9009 200.9009 200.9009 0.0000 0.0000 0.0000 426 ILE B N   
7294 C CA  . ILE B 426 ? 200.8417 200.8417 200.8417 0.0000 0.0000 0.0000 426 ILE B CA  
7295 C C   . ILE B 426 ? 200.1935 200.1935 200.1935 0.0000 0.0000 0.0000 426 ILE B C   
7296 O O   . ILE B 426 ? 200.1561 200.1561 200.1561 0.0000 0.0000 0.0000 426 ILE B O   
7297 C CB  . ILE B 426 ? 200.2767 200.2767 200.2767 0.0000 0.0000 0.0000 426 ILE B CB  
7298 C CG1 . ILE B 426 ? 200.4108 200.4108 200.4108 0.0000 0.0000 0.0000 426 ILE B CG1 
7299 C CG2 . ILE B 426 ? 200.1544 200.1544 200.1544 0.0000 0.0000 0.0000 426 ILE B CG2 
7300 C CD1 . ILE B 426 ? 203.4943 203.4943 203.4943 0.0000 0.0000 0.0000 426 ILE B CD1 
7301 N N   . CYS B 427 ? 203.7083 203.7083 203.7083 0.0000 0.0000 0.0000 427 CYS B N   
7302 C CA  . CYS B 427 ? 204.3268 204.3268 204.3268 0.0000 0.0000 0.0000 427 CYS B CA  
7303 C C   . CYS B 427 ? 204.2053 204.2053 204.2053 0.0000 0.0000 0.0000 427 CYS B C   
7304 O O   . CYS B 427 ? 203.5036 203.5036 203.5036 0.0000 0.0000 0.0000 427 CYS B O   
7305 C CB  . CYS B 427 ? 203.2471 203.2471 203.2471 0.0000 0.0000 0.0000 427 CYS B CB  
7306 S SG  . CYS B 427 ? 203.3186 203.3186 203.3186 0.0000 0.0000 0.0000 427 CYS B SG  
7307 N N   . VAL B 428 ? 230.0676 230.0676 230.0676 0.0000 0.0000 0.0000 428 VAL B N   
7308 C CA  . VAL B 428 ? 230.5363 230.5363 230.5363 0.0000 0.0000 0.0000 428 VAL B CA  
7309 C C   . VAL B 428 ? 230.5347 230.5347 230.5347 0.0000 0.0000 0.0000 428 VAL B C   
7310 O O   . VAL B 428 ? 230.3642 230.3642 230.3642 0.0000 0.0000 0.0000 428 VAL B O   
7311 C CB  . VAL B 428 ? 230.7699 230.7699 230.7699 0.0000 0.0000 0.0000 428 VAL B CB  
7312 C CG1 . VAL B 428 ? 230.9075 230.9075 230.9075 0.0000 0.0000 0.0000 428 VAL B CG1 
7313 C CG2 . VAL B 428 ? 230.9519 230.9519 230.9519 0.0000 0.0000 0.0000 428 VAL B CG2 
7314 N N   . ALA B 429 ? 230.8653 230.8653 230.8653 0.0000 0.0000 0.0000 429 ALA B N   
7315 C CA  . ALA B 429 ? 231.0700 231.0700 231.0700 0.0000 0.0000 0.0000 429 ALA B CA  
7316 C C   . ALA B 429 ? 229.3151 229.3151 229.3151 0.0000 0.0000 0.0000 429 ALA B C   
7317 O O   . ALA B 429 ? 229.1771 229.1771 229.1771 0.0000 0.0000 0.0000 429 ALA B O   
7318 C CB  . ALA B 429 ? 229.1864 229.1864 229.1864 0.0000 0.0000 0.0000 429 ALA B CB  
7319 N N   . LYS B 430 ? 229.1154 229.1154 229.1154 0.0000 0.0000 0.0000 430 LYS B N   
7320 C CA  . LYS B 430 ? 229.0025 229.0025 229.0025 0.0000 0.0000 0.0000 430 LYS B CA  
7321 C C   . LYS B 430 ? 228.6297 228.6297 228.6297 0.0000 0.0000 0.0000 430 LYS B C   
7322 O O   . LYS B 430 ? 223.5179 223.5179 223.5179 0.0000 0.0000 0.0000 430 LYS B O   
7323 C CB  . LYS B 430 ? 223.3458 223.3458 223.3458 0.0000 0.0000 0.0000 430 LYS B CB  
7324 C CG  . LYS B 430 ? 223.0451 223.0451 223.0451 0.0000 0.0000 0.0000 430 LYS B CG  
7325 C CD  . LYS B 430 ? 222.9680 222.9680 222.9680 0.0000 0.0000 0.0000 430 LYS B CD  
7326 C CE  . LYS B 430 ? 223.3528 223.3528 223.3528 0.0000 0.0000 0.0000 430 LYS B CE  
7327 N NZ  . LYS B 430 ? 223.3396 223.3396 223.3396 0.0000 0.0000 0.0000 430 LYS B NZ  
7328 N N   . ALA B 431 ? 223.4103 223.4103 223.4103 0.0000 0.0000 0.0000 431 ALA B N   
7329 C CA  . ALA B 431 ? 215.8343 215.8343 215.8343 0.0000 0.0000 0.0000 431 ALA B CA  
7330 C C   . ALA B 431 ? 215.6890 215.6890 215.6890 0.0000 0.0000 0.0000 431 ALA B C   
7331 O O   . ALA B 431 ? 215.5114 215.5114 215.5114 0.0000 0.0000 0.0000 431 ALA B O   
7332 C CB  . ALA B 431 ? 215.5995 215.5995 215.5995 0.0000 0.0000 0.0000 431 ALA B CB  
7333 N N   . VAL B 432 ? 215.7335 215.7335 215.7335 0.0000 0.0000 0.0000 432 VAL B N   
7334 C CA  . VAL B 432 ? 215.8003 215.8003 215.8003 0.0000 0.0000 0.0000 432 VAL B CA  
7335 C C   . VAL B 432 ? 215.8536 215.8536 215.8536 0.0000 0.0000 0.0000 432 VAL B C   
7336 O O   . VAL B 432 ? 210.4923 210.4923 210.4923 0.0000 0.0000 0.0000 432 VAL B O   
7337 C CB  . VAL B 432 ? 210.4816 210.4816 210.4816 0.0000 0.0000 0.0000 432 VAL B CB  
7338 C CG1 . VAL B 432 ? 210.2988 210.2988 210.2988 0.0000 0.0000 0.0000 432 VAL B CG1 
7339 C CG2 . VAL B 432 ? 210.2299 210.2299 210.2299 0.0000 0.0000 0.0000 432 VAL B CG2 
7340 N N   . GLU B 433 ? 210.4931 210.4931 210.4931 0.0000 0.0000 0.0000 433 GLU B N   
7341 C CA  . GLU B 433 ? 210.6546 210.6546 210.6546 0.0000 0.0000 0.0000 433 GLU B CA  
7342 C C   . GLU B 433 ? 210.4156 210.4156 210.4156 0.0000 0.0000 0.0000 433 GLU B C   
7343 O O   . GLU B 433 ? 204.4332 204.4332 204.4332 0.0000 0.0000 0.0000 433 GLU B O   
7344 C CB  . GLU B 433 ? 204.2306 204.2306 204.2306 0.0000 0.0000 0.0000 433 GLU B CB  
7345 C CG  . GLU B 433 ? 203.9482 203.9482 203.9482 0.0000 0.0000 0.0000 433 GLU B CG  
7346 C CD  . GLU B 433 ? 204.0795 204.0795 204.0795 0.0000 0.0000 0.0000 433 GLU B CD  
7347 O OE1 . GLU B 433 ? 204.1552 204.1552 204.1552 0.0000 0.0000 0.0000 433 GLU B OE1 
7348 O OE2 . GLU B 433 ? 204.3942 204.3942 204.3942 0.0000 0.0000 0.0000 433 GLU B OE2 
7349 N N   . CYS B 434 ? 204.1794 204.1794 204.1794 0.0000 0.0000 0.0000 434 CYS B N   
7350 C CA  . CYS B 434 ? 204.2093 204.2093 204.2093 0.0000 0.0000 0.0000 434 CYS B CA  
7351 C C   . CYS B 434 ? 204.3884 204.3884 204.3884 0.0000 0.0000 0.0000 434 CYS B C   
7352 O O   . CYS B 434 ? 204.6607 204.6607 204.6607 0.0000 0.0000 0.0000 434 CYS B O   
7353 C CB  . CYS B 434 ? 204.2909 204.2909 204.2909 0.0000 0.0000 0.0000 434 CYS B CB  
7354 S SG  . CYS B 434 ? 197.2867 197.2867 197.2867 0.0000 0.0000 0.0000 434 CYS B SG  
7355 N N   . PRO B 435 ? 197.0504 197.0504 197.0504 0.0000 0.0000 0.0000 435 PRO B N   
7356 C CA  . PRO B 435 ? 196.6529 196.6529 196.6529 0.0000 0.0000 0.0000 435 PRO B CA  
7357 C C   . PRO B 435 ? 196.6578 196.6578 196.6578 0.0000 0.0000 0.0000 435 PRO B C   
7358 O O   . PRO B 435 ? 197.0074 197.0074 197.0074 0.0000 0.0000 0.0000 435 PRO B O   
7359 C CB  . PRO B 435 ? 196.8569 196.8569 196.8569 0.0000 0.0000 0.0000 435 PRO B CB  
7360 C CG  . PRO B 435 ? 196.9578 196.9578 196.9578 0.0000 0.0000 0.0000 435 PRO B CG  
7361 C CD  . PRO B 435 ? 186.9309 186.9309 186.9309 0.0000 0.0000 0.0000 435 PRO B CD  
7362 N N   . PRO B 436 ? 186.5647 186.5647 186.5647 0.0000 0.0000 0.0000 436 PRO B N   
7363 C CA  . PRO B 436 ? 186.3955 186.3955 186.3955 0.0000 0.0000 0.0000 436 PRO B CA  
7364 C C   . PRO B 436 ? 186.3211 186.3211 186.3211 0.0000 0.0000 0.0000 436 PRO B C   
7365 O O   . PRO B 436 ? 186.5411 186.5411 186.5411 0.0000 0.0000 0.0000 436 PRO B O   
7366 C CB  . PRO B 436 ? 186.8620 186.8620 186.8620 0.0000 0.0000 0.0000 436 PRO B CB  
7367 C CG  . PRO B 436 ? 186.7056 186.7056 186.7056 0.0000 0.0000 0.0000 436 PRO B CG  
7368 C CD  . PRO B 436 ? 183.7808 183.7808 183.7808 0.0000 0.0000 0.0000 436 PRO B CD  
7369 N N   . PRO B 437 ? 183.6055 183.6055 183.6055 0.0000 0.0000 0.0000 437 PRO B N   
7370 C CA  . PRO B 437 ? 183.7837 183.7837 183.7837 0.0000 0.0000 0.0000 437 PRO B CA  
7371 C C   . PRO B 437 ? 183.4580 183.4580 183.4580 0.0000 0.0000 0.0000 437 PRO B C   
7372 O O   . PRO B 437 ? 183.4444 183.4444 183.4444 0.0000 0.0000 0.0000 437 PRO B O   
7373 C CB  . PRO B 437 ? 193.8985 193.8985 193.8985 0.0000 0.0000 0.0000 437 PRO B CB  
7374 C CG  . PRO B 437 ? 194.0105 194.0105 194.0105 0.0000 0.0000 0.0000 437 PRO B CG  
7375 C CD  . PRO B 437 ? 193.6945 193.6945 193.6945 0.0000 0.0000 0.0000 437 PRO B CD  
7376 N N   . ARG B 438 ? 193.5524 193.5524 193.5524 0.0000 0.0000 0.0000 438 ARG B N   
7377 C CA  . ARG B 438 ? 194.3542 194.3542 194.3542 0.0000 0.0000 0.0000 438 ARG B CA  
7378 C C   . ARG B 438 ? 194.4084 194.4084 194.4084 0.0000 0.0000 0.0000 438 ARG B C   
7379 O O   . ARG B 438 ? 194.6005 194.6005 194.6005 0.0000 0.0000 0.0000 438 ARG B O   
7380 C CB  . ARG B 438 ? 194.8319 194.8319 194.8319 0.0000 0.0000 0.0000 438 ARG B CB  
7381 C CG  . ARG B 438 ? 194.7941 194.7941 194.7941 0.0000 0.0000 0.0000 438 ARG B CG  
7382 C CD  . ARG B 438 ? 194.4585 194.4585 194.4585 0.0000 0.0000 0.0000 438 ARG B CD  
7383 N NE  . ARG B 438 ? 195.1310 195.1310 195.1310 0.0000 0.0000 0.0000 438 ARG B NE  
7384 C CZ  . ARG B 438 ? 185.4609 185.4609 185.4609 0.0000 0.0000 0.0000 438 ARG B CZ  
7385 N NH1 . ARG B 438 ? 185.1739 185.1739 185.1739 0.0000 0.0000 0.0000 438 ARG B NH1 
7386 N NH2 . ARG B 438 ? 184.7800 184.7800 184.7800 0.0000 0.0000 0.0000 438 ARG B NH2 
7387 N N   . THR B 439 ? 184.6547 184.6547 184.6547 0.0000 0.0000 0.0000 439 THR B N   
7388 C CA  . THR B 439 ? 185.3312 185.3312 185.3312 0.0000 0.0000 0.0000 439 THR B CA  
7389 C C   . THR B 439 ? 185.6489 185.6489 185.6489 0.0000 0.0000 0.0000 439 THR B C   
7390 O O   . THR B 439 ? 185.9505 185.9505 185.9505 0.0000 0.0000 0.0000 439 THR B O   
7391 C CB  . THR B 439 ? 186.0416 186.0416 186.0416 0.0000 0.0000 0.0000 439 THR B CB  
7392 O OG1 . THR B 439 ? 178.4365 178.4365 178.4365 0.0000 0.0000 0.0000 439 THR B OG1 
7393 C CG2 . THR B 439 ? 178.1053 178.1053 178.1053 0.0000 0.0000 0.0000 439 THR B CG2 
7394 N N   . THR B 440 ? 177.8269 177.8269 177.8269 0.0000 0.0000 0.0000 440 THR B N   
7395 C CA  . THR B 440 ? 177.6995 177.6995 177.6995 0.0000 0.0000 0.0000 440 THR B CA  
7396 C C   . THR B 440 ? 178.0740 178.0740 178.0740 0.0000 0.0000 0.0000 440 THR B C   
7397 O O   . THR B 440 ? 178.0965 178.0965 178.0965 0.0000 0.0000 0.0000 440 THR B O   
7398 C CB  . THR B 440 ? 178.0379 178.0379 178.0379 0.0000 0.0000 0.0000 440 THR B CB  
7399 O OG1 . THR B 440 ? 177.9995 177.9995 177.9995 0.0000 0.0000 0.0000 440 THR B OG1 
7400 C CG2 . THR B 440 ? 174.5842 174.5842 174.5842 0.0000 0.0000 0.0000 440 THR B CG2 
7401 N N   . ALA B 441 ? 174.3389 174.3389 174.3389 0.0000 0.0000 0.0000 441 ALA B N   
7402 C CA  . ALA B 441 ? 174.2532 174.2532 174.2532 0.0000 0.0000 0.0000 441 ALA B CA  
7403 C C   . ALA B 441 ? 174.2177 174.2177 174.2177 0.0000 0.0000 0.0000 441 ALA B C   
7404 O O   . ALA B 441 ? 174.3913 174.3913 174.3913 0.0000 0.0000 0.0000 441 ALA B O   
7405 C CB  . ALA B 441 ? 174.1670 174.1670 174.1670 0.0000 0.0000 0.0000 441 ALA B CB  
7406 N N   . ARG B 442 ? 174.1857 174.1857 174.1857 0.0000 0.0000 0.0000 442 ARG B N   
7407 C CA  . ARG B 442 ? 174.1078 174.1078 174.1078 0.0000 0.0000 0.0000 442 ARG B CA  
7408 C C   . ARG B 442 ? 174.8221 174.8221 174.8221 0.0000 0.0000 0.0000 442 ARG B C   
7409 O O   . ARG B 442 ? 174.6902 174.6902 174.6902 0.0000 0.0000 0.0000 442 ARG B O   
7410 C CB  . ARG B 442 ? 174.6395 174.6395 174.6395 0.0000 0.0000 0.0000 442 ARG B CB  
7411 C CG  . ARG B 442 ? 174.9124 174.9124 174.9124 0.0000 0.0000 0.0000 442 ARG B CG  
7412 C CD  . ARG B 442 ? 175.1050 175.1050 175.1050 0.0000 0.0000 0.0000 442 ARG B CD  
7413 N NE  . ARG B 442 ? 175.5408 175.5408 175.5408 0.0000 0.0000 0.0000 442 ARG B NE  
7414 C CZ  . ARG B 442 ? 175.2838 175.2838 175.2838 0.0000 0.0000 0.0000 442 ARG B CZ  
7415 N NH1 . ARG B 442 ? 175.3152 175.3152 175.3152 0.0000 0.0000 0.0000 442 ARG B NH1 
7416 N NH2 . ARG B 442 ? 174.9613 174.9613 174.9613 0.0000 0.0000 0.0000 442 ARG B NH2 
7417 N N   . LEU B 443 ? 168.9241 168.9241 168.9241 0.0000 0.0000 0.0000 443 LEU B N   
7418 C CA  . LEU B 443 ? 168.7690 168.7690 168.7690 0.0000 0.0000 0.0000 443 LEU B CA  
7419 C C   . LEU B 443 ? 168.8660 168.8660 168.8660 0.0000 0.0000 0.0000 443 LEU B C   
7420 O O   . LEU B 443 ? 169.0687 169.0687 169.0687 0.0000 0.0000 0.0000 443 LEU B O   
7421 C CB  . LEU B 443 ? 168.6610 168.6610 168.6610 0.0000 0.0000 0.0000 443 LEU B CB  
7422 C CG  . LEU B 443 ? 168.5196 168.5196 168.5196 0.0000 0.0000 0.0000 443 LEU B CG  
7423 C CD1 . LEU B 443 ? 168.8652 168.8652 168.8652 0.0000 0.0000 0.0000 443 LEU B CD1 
7424 C CD2 . LEU B 443 ? 168.9880 168.9880 168.9880 0.0000 0.0000 0.0000 443 LEU B CD2 
7425 N N   . LEU B 444 ? 167.9769 167.9769 167.9769 0.0000 0.0000 0.0000 444 LEU B N   
7426 C CA  . LEU B 444 ? 167.8082 167.8082 167.8082 0.0000 0.0000 0.0000 444 LEU B CA  
7427 C C   . LEU B 444 ? 168.1670 168.1670 168.1670 0.0000 0.0000 0.0000 444 LEU B C   
7428 O O   . LEU B 444 ? 168.3567 168.3567 168.3567 0.0000 0.0000 0.0000 444 LEU B O   
7429 C CB  . LEU B 444 ? 167.5861 167.5861 167.5861 0.0000 0.0000 0.0000 444 LEU B CB  
7430 C CG  . LEU B 444 ? 167.7175 167.7175 167.7175 0.0000 0.0000 0.0000 444 LEU B CG  
7431 C CD1 . LEU B 444 ? 167.7064 167.7064 167.7064 0.0000 0.0000 0.0000 444 LEU B CD1 
7432 C CD2 . LEU B 444 ? 174.0334 174.0334 174.0334 0.0000 0.0000 0.0000 444 LEU B CD2 
7433 N N   . ASP B 445 ? 174.2721 174.2721 174.2721 0.0000 0.0000 0.0000 445 ASP B N   
7434 C CA  . ASP B 445 ? 174.5651 174.5651 174.5651 0.0000 0.0000 0.0000 445 ASP B CA  
7435 C C   . ASP B 445 ? 174.6432 174.6432 174.6432 0.0000 0.0000 0.0000 445 ASP B C   
7436 O O   . ASP B 445 ? 187.7302 187.7302 187.7302 0.0000 0.0000 0.0000 445 ASP B O   
7437 C CB  . ASP B 445 ? 188.1791 188.1791 188.1791 0.0000 0.0000 0.0000 445 ASP B CB  
7438 C CG  . ASP B 445 ? 188.1188 188.1188 188.1188 0.0000 0.0000 0.0000 445 ASP B CG  
7439 O OD1 . ASP B 445 ? 188.3652 188.3652 188.3652 0.0000 0.0000 0.0000 445 ASP B OD1 
7440 O OD2 . ASP B 445 ? 188.4815 188.4815 188.4815 0.0000 0.0000 0.0000 445 ASP B OD2 
7441 N N   . LYS B 446 ? 188.7608 188.7608 188.7608 0.0000 0.0000 0.0000 446 LYS B N   
7442 C CA  . LYS B 446 ? 188.7662 188.7662 188.7662 0.0000 0.0000 0.0000 446 LYS B CA  
7443 C C   . LYS B 446 ? 188.9341 188.9341 188.9341 0.0000 0.0000 0.0000 446 LYS B C   
7444 O O   . LYS B 446 ? 188.7175 188.7175 188.7175 0.0000 0.0000 0.0000 446 LYS B O   
7445 C CB  . LYS B 446 ? 184.0898 184.0898 184.0898 0.0000 0.0000 0.0000 446 LYS B CB  
7446 C CG  . LYS B 446 ? 184.0819 184.0819 184.0819 0.0000 0.0000 0.0000 446 LYS B CG  
7447 C CD  . LYS B 446 ? 183.8305 183.8305 183.8305 0.0000 0.0000 0.0000 446 LYS B CD  
7448 C CE  . LYS B 446 ? 183.9654 183.9654 183.9654 0.0000 0.0000 0.0000 446 LYS B CE  
7449 N NZ  . LYS B 446 ? 184.2859 184.2859 184.2859 0.0000 0.0000 0.0000 446 LYS B NZ  
7450 N N   . LEU B 447 ? 184.4423 184.4423 184.4423 0.0000 0.0000 0.0000 447 LEU B N   
7451 C CA  . LEU B 447 ? 184.5345 184.5345 184.5345 0.0000 0.0000 0.0000 447 LEU B CA  
7452 C C   . LEU B 447 ? 184.4252 184.4252 184.4252 0.0000 0.0000 0.0000 447 LEU B C   
7453 O O   . LEU B 447 ? 184.5466 184.5466 184.5466 0.0000 0.0000 0.0000 447 LEU B O   
7454 C CB  . LEU B 447 ? 184.6419 184.6419 184.6419 0.0000 0.0000 0.0000 447 LEU B CB  
7455 C CG  . LEU B 447 ? 184.6807 184.6807 184.6807 0.0000 0.0000 0.0000 447 LEU B CG  
7456 C CD1 . LEU B 447 ? 171.0660 171.0660 171.0660 0.0000 0.0000 0.0000 447 LEU B CD1 
7457 C CD2 . LEU B 447 ? 170.6077 170.6077 170.6077 0.0000 0.0000 0.0000 447 LEU B CD2 
7458 N N   . VAL B 448 ? 170.8619 170.8619 170.8619 0.0000 0.0000 0.0000 448 VAL B N   
7459 C CA  . VAL B 448 ? 171.0392 171.0392 171.0392 0.0000 0.0000 0.0000 448 VAL B CA  
7460 C C   . VAL B 448 ? 170.3544 170.3544 170.3544 0.0000 0.0000 0.0000 448 VAL B C   
7461 O O   . VAL B 448 ? 170.5113 170.5113 170.5113 0.0000 0.0000 0.0000 448 VAL B O   
7462 C CB  . VAL B 448 ? 170.3856 170.3856 170.3856 0.0000 0.0000 0.0000 448 VAL B CB  
7463 C CG1 . VAL B 448 ? 170.7580 170.7580 170.7580 0.0000 0.0000 0.0000 448 VAL B CG1 
7464 C CG2 . VAL B 448 ? 176.9697 176.9697 176.9697 0.0000 0.0000 0.0000 448 VAL B CG2 
7465 N N   . GLY B 449 ? 176.9863 176.9863 176.9863 0.0000 0.0000 0.0000 449 GLY B N   
7466 C CA  . GLY B 449 ? 177.0451 177.0451 177.0451 0.0000 0.0000 0.0000 449 GLY B CA  
7467 C C   . GLY B 449 ? 177.0826 177.0826 177.0826 0.0000 0.0000 0.0000 449 GLY B C   
7468 O O   . GLY B 449 ? 176.8712 176.8712 176.8712 0.0000 0.0000 0.0000 449 GLY B O   
7469 N N   . GLU B 450 ? 176.8549 176.8549 176.8549 0.0000 0.0000 0.0000 450 GLU B N   
7470 C CA  . GLU B 450 ? 177.0230 177.0230 177.0230 0.0000 0.0000 0.0000 450 GLU B CA  
7471 C C   . GLU B 450 ? 177.1392 177.1392 177.1392 0.0000 0.0000 0.0000 450 GLU B C   
7472 O O   . GLU B 450 ? 177.0255 177.0255 177.0255 0.0000 0.0000 0.0000 450 GLU B O   
7473 C CB  . GLU B 450 ? 177.5481 177.5481 177.5481 0.0000 0.0000 0.0000 450 GLU B CB  
7474 C CG  . GLU B 450 ? 177.5211 177.5211 177.5211 0.0000 0.0000 0.0000 450 GLU B CG  
7475 C CD  . GLU B 450 ? 177.7084 177.7084 177.7084 0.0000 0.0000 0.0000 450 GLU B CD  
7476 O OE1 . GLU B 450 ? 177.6582 177.6582 177.6582 0.0000 0.0000 0.0000 450 GLU B OE1 
7477 O OE2 . GLU B 450 ? 177.6073 177.6073 177.6073 0.0000 0.0000 0.0000 450 GLU B OE2 
7478 N N   . PHE B 451 ? 177.6765 177.6765 177.6765 0.0000 0.0000 0.0000 451 PHE B N   
7479 C CA  . PHE B 451 ? 177.7805 177.7805 177.7805 0.0000 0.0000 0.0000 451 PHE B CA  
7480 C C   . PHE B 451 ? 185.1517 185.1517 185.1517 0.0000 0.0000 0.0000 451 PHE B C   
7481 O O   . PHE B 451 ? 185.3849 185.3849 185.3849 0.0000 0.0000 0.0000 451 PHE B O   
7482 C CB  . PHE B 451 ? 185.2539 185.2539 185.2539 0.0000 0.0000 0.0000 451 PHE B CB  
7483 C CG  . PHE B 451 ? 185.3656 185.3656 185.3656 0.0000 0.0000 0.0000 451 PHE B CG  
7484 C CD1 . PHE B 451 ? 185.6574 185.6574 185.6574 0.0000 0.0000 0.0000 451 PHE B CD1 
7485 C CD2 . PHE B 451 ? 185.8075 185.8075 185.8075 0.0000 0.0000 0.0000 451 PHE B CD2 
7486 C CE1 . PHE B 451 ? 185.5722 185.5722 185.5722 0.0000 0.0000 0.0000 451 PHE B CE1 
7487 C CE2 . PHE B 451 ? 177.3910 177.3910 177.3910 0.0000 0.0000 0.0000 451 PHE B CE2 
7488 C CZ  . PHE B 451 ? 176.9968 176.9968 176.9968 0.0000 0.0000 0.0000 451 PHE B CZ  
7489 N N   . LEU B 452 ? 176.5430 176.5430 176.5430 0.0000 0.0000 0.0000 452 LEU B N   
7490 C CA  . LEU B 452 ? 176.5260 176.5260 176.5260 0.0000 0.0000 0.0000 452 LEU B CA  
7491 C C   . LEU B 452 ? 176.8917 176.8917 176.8917 0.0000 0.0000 0.0000 452 LEU B C   
7492 O O   . LEU B 452 ? 176.8569 176.8569 176.8569 0.0000 0.0000 0.0000 452 LEU B O   
7493 C CB  . LEU B 452 ? 162.1964 162.1964 162.1964 0.0000 0.0000 0.0000 452 LEU B CB  
7494 C CG  . LEU B 452 ? 161.6954 161.6954 161.6954 0.0000 0.0000 0.0000 452 LEU B CG  
7495 C CD1 . LEU B 452 ? 161.5469 161.5469 161.5469 0.0000 0.0000 0.0000 452 LEU B CD1 
7496 C CD2 . LEU B 452 ? 161.5848 161.5848 161.5848 0.0000 0.0000 0.0000 452 LEU B CD2 
7497 N N   . GLU B 453 ? 161.3883 161.3883 161.3883 0.0000 0.0000 0.0000 453 GLU B N   
7498 C CA  . GLU B 453 ? 161.6383 161.6383 161.6383 0.0000 0.0000 0.0000 453 GLU B CA  
7499 C C   . GLU B 453 ? 161.6056 161.6056 161.6056 0.0000 0.0000 0.0000 453 GLU B C   
7500 O O   . GLU B 453 ? 161.8062 161.8062 161.8062 0.0000 0.0000 0.0000 453 GLU B O   
7501 C CB  . GLU B 453 ? 161.4794 161.4794 161.4794 0.0000 0.0000 0.0000 453 GLU B CB  
7502 C CG  . GLU B 453 ? 161.3824 161.3824 161.3824 0.0000 0.0000 0.0000 453 GLU B CG  
7503 C CD  . GLU B 453 ? 161.4161 161.4161 161.4161 0.0000 0.0000 0.0000 453 GLU B CD  
7504 O OE1 . GLU B 453 ? 161.6774 161.6774 161.6774 0.0000 0.0000 0.0000 453 GLU B OE1 
7505 O OE2 . GLU B 453 ? 161.2986 161.2986 161.2986 0.0000 0.0000 0.0000 453 GLU B OE2 
7506 N N   . VAL B 454 ? 161.2915 161.2915 161.2915 0.0000 0.0000 0.0000 454 VAL B N   
7507 C CA  . VAL B 454 ? 161.3736 161.3736 161.3736 0.0000 0.0000 0.0000 454 VAL B CA  
7508 C C   . VAL B 454 ? 161.3979 161.3979 161.3979 0.0000 0.0000 0.0000 454 VAL B C   
7509 O O   . VAL B 454 ? 161.2588 161.2588 161.2588 0.0000 0.0000 0.0000 454 VAL B O   
7510 C CB  . VAL B 454 ? 161.3377 161.3377 161.3377 0.0000 0.0000 0.0000 454 VAL B CB  
7511 C CG1 . VAL B 454 ? 161.4226 161.4226 161.4226 0.0000 0.0000 0.0000 454 VAL B CG1 
7512 C CG2 . VAL B 454 ? 161.7264 161.7264 161.7264 0.0000 0.0000 0.0000 454 VAL B CG2 
7513 N N   . THR B 455 ? 161.3998 161.3998 161.3998 0.0000 0.0000 0.0000 455 THR B N   
7514 C CA  . THR B 455 ? 161.4316 161.4316 161.4316 0.0000 0.0000 0.0000 455 THR B CA  
7515 C C   . THR B 455 ? 161.4653 161.4653 161.4653 0.0000 0.0000 0.0000 455 THR B C   
7516 O O   . THR B 455 ? 161.3021 161.3021 161.3021 0.0000 0.0000 0.0000 455 THR B O   
7517 C CB  . THR B 455 ? 161.2539 161.2539 161.2539 0.0000 0.0000 0.0000 455 THR B CB  
7518 O OG1 . THR B 455 ? 161.3857 161.3857 161.3857 0.0000 0.0000 0.0000 455 THR B OG1 
7519 C CG2 . THR B 455 ? 161.6100 161.6100 161.6100 0.0000 0.0000 0.0000 455 THR B CG2 
7520 N N   . CYS B 456 ? 161.4923 161.4923 161.4923 0.0000 0.0000 0.0000 456 CYS B N   
7521 C CA  . CYS B 456 ? 161.6541 161.6541 161.6541 0.0000 0.0000 0.0000 456 CYS B CA  
7522 C C   . CYS B 456 ? 161.6415 161.6415 161.6415 0.0000 0.0000 0.0000 456 CYS B C   
7523 O O   . CYS B 456 ? 161.3703 161.3703 161.3703 0.0000 0.0000 0.0000 456 CYS B O   
7524 C CB  . CYS B 456 ? 161.3811 161.3811 161.3811 0.0000 0.0000 0.0000 456 CYS B CB  
7525 S SG  . CYS B 456 ? 161.4343 161.4343 161.4343 0.0000 0.0000 0.0000 456 CYS B SG  
7526 N N   . ILE B 457 ? 161.5657 161.5657 161.5657 0.0000 0.0000 0.0000 457 ILE B N   
7527 C CA  . ILE B 457 ? 161.4808 161.4808 161.4808 0.0000 0.0000 0.0000 457 ILE B CA  
7528 C C   . ILE B 457 ? 161.2470 161.2470 161.2470 0.0000 0.0000 0.0000 457 ILE B C   
7529 O O   . ILE B 457 ? 161.2471 161.2471 161.2471 0.0000 0.0000 0.0000 457 ILE B O   
7530 C CB  . ILE B 457 ? 161.4173 161.4173 161.4173 0.0000 0.0000 0.0000 457 ILE B CB  
7531 C CG1 . ILE B 457 ? 161.3537 161.3537 161.3537 0.0000 0.0000 0.0000 457 ILE B CG1 
7532 C CG2 . ILE B 457 ? 161.4352 161.4352 161.4352 0.0000 0.0000 0.0000 457 ILE B CG2 
7533 C CD1 . ILE B 457 ? 161.4425 161.4425 161.4425 0.0000 0.0000 0.0000 457 ILE B CD1 
7534 N N   . ASN B 458 ? 161.3730 161.3730 161.3730 0.0000 0.0000 0.0000 458 ASN B N   
7535 C CA  . ASN B 458 ? 161.2876 161.2876 161.2876 0.0000 0.0000 0.0000 458 ASN B CA  
7536 C C   . ASN B 458 ? 161.4075 161.4075 161.4075 0.0000 0.0000 0.0000 458 ASN B C   
7537 O O   . ASN B 458 ? 161.6235 161.6235 161.6235 0.0000 0.0000 0.0000 458 ASN B O   
7538 C CB  . ASN B 458 ? 161.1979 161.1979 161.1979 0.0000 0.0000 0.0000 458 ASN B CB  
7539 C CG  . ASN B 458 ? 161.3854 161.3854 161.3854 0.0000 0.0000 0.0000 458 ASN B CG  
7540 O OD1 . ASN B 458 ? 161.4539 161.4539 161.4539 0.0000 0.0000 0.0000 458 ASN B OD1 
7541 N ND2 . ASN B 458 ? 161.5898 161.5898 161.5898 0.0000 0.0000 0.0000 458 ASN B ND2 
7542 N N   . PRO B 459 ? 161.4433 161.4433 161.4433 0.0000 0.0000 0.0000 459 PRO B N   
7543 C CA  . PRO B 459 ? 161.4170 161.4170 161.4170 0.0000 0.0000 0.0000 459 PRO B CA  
7544 C C   . PRO B 459 ? 161.4249 161.4249 161.4249 0.0000 0.0000 0.0000 459 PRO B C   
7545 O O   . PRO B 459 ? 161.6883 161.6883 161.6883 0.0000 0.0000 0.0000 459 PRO B O   
7546 C CB  . PRO B 459 ? 161.5214 161.5214 161.5214 0.0000 0.0000 0.0000 459 PRO B CB  
7547 C CG  . PRO B 459 ? 161.3999 161.3999 161.3999 0.0000 0.0000 0.0000 459 PRO B CG  
7548 C CD  . PRO B 459 ? 161.3606 161.3606 161.3606 0.0000 0.0000 0.0000 459 PRO B CD  
7549 N N   . THR B 460 ? 161.3779 161.3779 161.3779 0.0000 0.0000 0.0000 460 THR B N   
7550 C CA  . THR B 460 ? 161.3782 161.3782 161.3782 0.0000 0.0000 0.0000 460 THR B CA  
7551 C C   . THR B 460 ? 161.5695 161.5695 161.5695 0.0000 0.0000 0.0000 460 THR B C   
7552 O O   . THR B 460 ? 161.6001 161.6001 161.6001 0.0000 0.0000 0.0000 460 THR B O   
7553 C CB  . THR B 460 ? 161.5257 161.5257 161.5257 0.0000 0.0000 0.0000 460 THR B CB  
7554 O OG1 . THR B 460 ? 161.4582 161.4582 161.4582 0.0000 0.0000 0.0000 460 THR B OG1 
7555 C CG2 . THR B 460 ? 161.6544 161.6544 161.6544 0.0000 0.0000 0.0000 460 THR B CG2 
7556 N N   . PHE B 461 ? 161.4022 161.4022 161.4022 0.0000 0.0000 0.0000 461 PHE B N   
7557 C CA  . PHE B 461 ? 161.4684 161.4684 161.4684 0.0000 0.0000 0.0000 461 PHE B CA  
7558 C C   . PHE B 461 ? 161.5498 161.5498 161.5498 0.0000 0.0000 0.0000 461 PHE B C   
7559 O O   . PHE B 461 ? 161.8676 161.8676 161.8676 0.0000 0.0000 0.0000 461 PHE B O   
7560 C CB  . PHE B 461 ? 161.5598 161.5598 161.5598 0.0000 0.0000 0.0000 461 PHE B CB  
7561 C CG  . PHE B 461 ? 161.3538 161.3538 161.3538 0.0000 0.0000 0.0000 461 PHE B CG  
7562 C CD1 . PHE B 461 ? 161.3100 161.3100 161.3100 0.0000 0.0000 0.0000 461 PHE B CD1 
7563 C CD2 . PHE B 461 ? 161.4706 161.4706 161.4706 0.0000 0.0000 0.0000 461 PHE B CD2 
7564 C CE1 . PHE B 461 ? 161.4172 161.4172 161.4172 0.0000 0.0000 0.0000 461 PHE B CE1 
7565 C CE2 . PHE B 461 ? 161.5918 161.5918 161.5918 0.0000 0.0000 0.0000 461 PHE B CE2 
7566 C CZ  . PHE B 461 ? 161.2883 161.2883 161.2883 0.0000 0.0000 0.0000 461 PHE B CZ  
7567 N N   . ILE B 462 ? 161.2960 161.2960 161.2960 0.0000 0.0000 0.0000 462 ILE B N   
7568 C CA  . ILE B 462 ? 161.3682 161.3682 161.3682 0.0000 0.0000 0.0000 462 ILE B CA  
7569 C C   . ILE B 462 ? 161.6314 161.6314 161.6314 0.0000 0.0000 0.0000 462 ILE B C   
7570 O O   . ILE B 462 ? 161.6271 161.6271 161.6271 0.0000 0.0000 0.0000 462 ILE B O   
7571 C CB  . ILE B 462 ? 161.7545 161.7545 161.7545 0.0000 0.0000 0.0000 462 ILE B CB  
7572 C CG1 . ILE B 462 ? 161.4223 161.4223 161.4223 0.0000 0.0000 0.0000 462 ILE B CG1 
7573 C CG2 . ILE B 462 ? 161.2607 161.2607 161.2607 0.0000 0.0000 0.0000 462 ILE B CG2 
7574 C CD1 . ILE B 462 ? 161.3997 161.3997 161.3997 0.0000 0.0000 0.0000 462 ILE B CD1 
7575 N N   . CYS B 463 ? 161.5377 161.5377 161.5377 0.0000 0.0000 0.0000 463 CYS B N   
7576 C CA  . CYS B 463 ? 161.5397 161.5397 161.5397 0.0000 0.0000 0.0000 463 CYS B CA  
7577 C C   . CYS B 463 ? 161.5712 161.5712 161.5712 0.0000 0.0000 0.0000 463 CYS B C   
7578 O O   . CYS B 463 ? 161.5009 161.5009 161.5009 0.0000 0.0000 0.0000 463 CYS B O   
7579 C CB  . CYS B 463 ? 161.4434 161.4434 161.4434 0.0000 0.0000 0.0000 463 CYS B CB  
7580 S SG  . CYS B 463 ? 161.4478 161.4478 161.4478 0.0000 0.0000 0.0000 463 CYS B SG  
7581 N N   . ASP B 464 ? 161.4073 161.4073 161.4073 0.0000 0.0000 0.0000 464 ASP B N   
7582 C CA  . ASP B 464 ? 161.7887 161.7887 161.7887 0.0000 0.0000 0.0000 464 ASP B CA  
7583 C C   . ASP B 464 ? 161.7759 161.7759 161.7759 0.0000 0.0000 0.0000 464 ASP B C   
7584 O O   . ASP B 464 ? 161.8498 161.8498 161.8498 0.0000 0.0000 0.0000 464 ASP B O   
7585 C CB  . ASP B 464 ? 161.8137 161.8137 161.8137 0.0000 0.0000 0.0000 464 ASP B CB  
7586 C CG  . ASP B 464 ? 161.7855 161.7855 161.7855 0.0000 0.0000 0.0000 464 ASP B CG  
7587 O OD1 . ASP B 464 ? 162.0639 162.0639 162.0639 0.0000 0.0000 0.0000 464 ASP B OD1 
7588 O OD2 . ASP B 464 ? 162.6762 162.6762 162.6762 0.0000 0.0000 0.0000 464 ASP B OD2 
7589 N N   . HIS B 465 ? 162.6200 162.6200 162.6200 0.0000 0.0000 0.0000 465 HIS B N   
7590 C CA  . HIS B 465 ? 166.5453 166.5453 166.5453 0.0000 0.0000 0.0000 465 HIS B CA  
7591 C C   . HIS B 465 ? 166.6397 166.6397 166.6397 0.0000 0.0000 0.0000 465 HIS B C   
7592 O O   . HIS B 465 ? 166.6519 166.6519 166.6519 0.0000 0.0000 0.0000 465 HIS B O   
7593 C CB  . HIS B 465 ? 166.8425 166.8425 166.8425 0.0000 0.0000 0.0000 465 HIS B CB  
7594 C CG  . HIS B 465 ? 166.7050 166.7050 166.7050 0.0000 0.0000 0.0000 465 HIS B CG  
7595 N ND1 . HIS B 465 ? 166.8305 166.8305 166.8305 0.0000 0.0000 0.0000 465 HIS B ND1 
7596 C CD2 . HIS B 465 ? 166.7859 166.7859 166.7859 0.0000 0.0000 0.0000 465 HIS B CD2 
7597 C CE1 . HIS B 465 ? 167.2146 167.2146 167.2146 0.0000 0.0000 0.0000 465 HIS B CE1 
7598 N NE2 . HIS B 465 ? 161.6483 161.6483 161.6483 0.0000 0.0000 0.0000 465 HIS B NE2 
7599 N N   . PRO B 466 ? 161.5070 161.5070 161.5070 0.0000 0.0000 0.0000 466 PRO B N   
7600 C CA  . PRO B 466 ? 161.3365 161.3365 161.3365 0.0000 0.0000 0.0000 466 PRO B CA  
7601 C C   . PRO B 466 ? 161.5160 161.5160 161.5160 0.0000 0.0000 0.0000 466 PRO B C   
7602 O O   . PRO B 466 ? 161.7116 161.7116 161.7116 0.0000 0.0000 0.0000 466 PRO B O   
7603 C CB  . PRO B 466 ? 161.6711 161.6711 161.6711 0.0000 0.0000 0.0000 466 PRO B CB  
7604 C CG  . PRO B 466 ? 161.2070 161.2070 161.2070 0.0000 0.0000 0.0000 466 PRO B CG  
7605 C CD  . PRO B 466 ? 161.3506 161.3506 161.3506 0.0000 0.0000 0.0000 466 PRO B CD  
7606 N N   . GLN B 467 ? 161.3556 161.3556 161.3556 0.0000 0.0000 0.0000 467 GLN B N   
7607 C CA  . GLN B 467 ? 161.4060 161.4060 161.4060 0.0000 0.0000 0.0000 467 GLN B CA  
7608 C C   . GLN B 467 ? 161.8211 161.8211 161.8211 0.0000 0.0000 0.0000 467 GLN B C   
7609 O O   . GLN B 467 ? 161.9974 161.9974 161.9974 0.0000 0.0000 0.0000 467 GLN B O   
7610 C CB  . GLN B 467 ? 161.5794 161.5794 161.5794 0.0000 0.0000 0.0000 467 GLN B CB  
7611 C CG  . GLN B 467 ? 161.2534 161.2534 161.2534 0.0000 0.0000 0.0000 467 GLN B CG  
7612 C CD  . GLN B 467 ? 161.1857 161.1857 161.1857 0.0000 0.0000 0.0000 467 GLN B CD  
7613 O OE1 . GLN B 467 ? 161.2270 161.2270 161.2270 0.0000 0.0000 0.0000 467 GLN B OE1 
7614 N NE2 . GLN B 467 ? 161.4383 161.4383 161.4383 0.0000 0.0000 0.0000 467 GLN B NE2 
7615 N N   . ILE B 468 ? 161.4007 161.4007 161.4007 0.0000 0.0000 0.0000 468 ILE B N   
7616 C CA  . ILE B 468 ? 161.6844 161.6844 161.6844 0.0000 0.0000 0.0000 468 ILE B CA  
7617 C C   . ILE B 468 ? 161.8820 161.8820 161.8820 0.0000 0.0000 0.0000 468 ILE B C   
7618 O O   . ILE B 468 ? 161.7043 161.7043 161.7043 0.0000 0.0000 0.0000 468 ILE B O   
7619 C CB  . ILE B 468 ? 161.1764 161.1764 161.1764 0.0000 0.0000 0.0000 468 ILE B CB  
7620 C CG1 . ILE B 468 ? 161.1875 161.1875 161.1875 0.0000 0.0000 0.0000 468 ILE B CG1 
7621 C CG2 . ILE B 468 ? 161.2102 161.2102 161.2102 0.0000 0.0000 0.0000 468 ILE B CG2 
7622 C CD1 . ILE B 468 ? 161.4626 161.4626 161.4626 0.0000 0.0000 0.0000 468 ILE B CD1 
7623 N N   . MET B 469 ? 161.4804 161.4804 161.4804 0.0000 0.0000 0.0000 469 MET B N   
7624 C CA  . MET B 469 ? 161.2368 161.2368 161.2368 0.0000 0.0000 0.0000 469 MET B CA  
7625 C C   . MET B 469 ? 161.2151 161.2151 161.2151 0.0000 0.0000 0.0000 469 MET B C   
7626 O O   . MET B 469 ? 161.2507 161.2507 161.2507 0.0000 0.0000 0.0000 469 MET B O   
7627 C CB  . MET B 469 ? 161.3876 161.3876 161.3876 0.0000 0.0000 0.0000 469 MET B CB  
7628 C CG  . MET B 469 ? 161.3930 161.3930 161.3930 0.0000 0.0000 0.0000 469 MET B CG  
7629 S SD  . MET B 469 ? 161.4133 161.4133 161.4133 0.0000 0.0000 0.0000 469 MET B SD  
7630 C CE  . MET B 469 ? 161.3982 161.3982 161.3982 0.0000 0.0000 0.0000 469 MET B CE  
7631 N N   . SER B 470 ? 161.3778 161.3778 161.3778 0.0000 0.0000 0.0000 470 SER B N   
7632 C CA  . SER B 470 ? 161.3774 161.3774 161.3774 0.0000 0.0000 0.0000 470 SER B CA  
7633 C C   . SER B 470 ? 161.3684 161.3684 161.3684 0.0000 0.0000 0.0000 470 SER B C   
7634 O O   . SER B 470 ? 161.2707 161.2707 161.2707 0.0000 0.0000 0.0000 470 SER B O   
7635 C CB  . SER B 470 ? 161.3366 161.3366 161.3366 0.0000 0.0000 0.0000 470 SER B CB  
7636 O OG  . SER B 470 ? 161.6389 161.6389 161.6389 0.0000 0.0000 0.0000 470 SER B OG  
7637 N N   . PRO B 471 ? 161.3520 161.3520 161.3520 0.0000 0.0000 0.0000 471 PRO B N   
7638 C CA  . PRO B 471 ? 161.3329 161.3329 161.3329 0.0000 0.0000 0.0000 471 PRO B CA  
7639 C C   . PRO B 471 ? 161.4828 161.4828 161.4828 0.0000 0.0000 0.0000 471 PRO B C   
7640 O O   . PRO B 471 ? 161.2833 161.2833 161.2833 0.0000 0.0000 0.0000 471 PRO B O   
7641 C CB  . PRO B 471 ? 161.5114 161.5114 161.5114 0.0000 0.0000 0.0000 471 PRO B CB  
7642 C CG  . PRO B 471 ? 161.4053 161.4053 161.4053 0.0000 0.0000 0.0000 471 PRO B CG  
7643 C CD  . PRO B 471 ? 161.4382 161.4382 161.4382 0.0000 0.0000 0.0000 471 PRO B CD  
7644 N N   . LEU B 472 ? 161.5118 161.5118 161.5118 0.0000 0.0000 0.0000 472 LEU B N   
7645 C CA  . LEU B 472 ? 161.3667 161.3667 161.3667 0.0000 0.0000 0.0000 472 LEU B CA  
7646 C C   . LEU B 472 ? 161.3495 161.3495 161.3495 0.0000 0.0000 0.0000 472 LEU B C   
7647 O O   . LEU B 472 ? 161.4008 161.4008 161.4008 0.0000 0.0000 0.0000 472 LEU B O   
7648 C CB  . LEU B 472 ? 161.4774 161.4774 161.4774 0.0000 0.0000 0.0000 472 LEU B CB  
7649 C CG  . LEU B 472 ? 161.3552 161.3552 161.3552 0.0000 0.0000 0.0000 472 LEU B CG  
7650 C CD1 . LEU B 472 ? 161.4979 161.4979 161.4979 0.0000 0.0000 0.0000 472 LEU B CD1 
7651 C CD2 . LEU B 472 ? 161.5812 161.5812 161.5812 0.0000 0.0000 0.0000 472 LEU B CD2 
7652 N N   . ALA B 473 ? 161.3151 161.3151 161.3151 0.0000 0.0000 0.0000 473 ALA B N   
7653 C CA  . ALA B 473 ? 161.3906 161.3906 161.3906 0.0000 0.0000 0.0000 473 ALA B CA  
7654 C C   . ALA B 473 ? 161.2685 161.2685 161.2685 0.0000 0.0000 0.0000 473 ALA B C   
7655 O O   . ALA B 473 ? 161.4103 161.4103 161.4103 0.0000 0.0000 0.0000 473 ALA B O   
7656 C CB  . ALA B 473 ? 161.2447 161.2447 161.2447 0.0000 0.0000 0.0000 473 ALA B CB  
7657 N N   . LYS B 474 ? 161.2133 161.2133 161.2133 0.0000 0.0000 0.0000 474 LYS B N   
7658 C CA  . LYS B 474 ? 161.2416 161.2416 161.2416 0.0000 0.0000 0.0000 474 LYS B CA  
7659 C C   . LYS B 474 ? 161.3149 161.3149 161.3149 0.0000 0.0000 0.0000 474 LYS B C   
7660 O O   . LYS B 474 ? 161.4812 161.4812 161.4812 0.0000 0.0000 0.0000 474 LYS B O   
7661 C CB  . LYS B 474 ? 161.3798 161.3798 161.3798 0.0000 0.0000 0.0000 474 LYS B CB  
7662 C CG  . LYS B 474 ? 161.4817 161.4817 161.4817 0.0000 0.0000 0.0000 474 LYS B CG  
7663 C CD  . LYS B 474 ? 161.4866 161.4866 161.4866 0.0000 0.0000 0.0000 474 LYS B CD  
7664 C CE  . LYS B 474 ? 161.3693 161.3693 161.3693 0.0000 0.0000 0.0000 474 LYS B CE  
7665 N NZ  . LYS B 474 ? 161.3762 161.3762 161.3762 0.0000 0.0000 0.0000 474 LYS B NZ  
7666 N N   . TRP B 475 ? 161.5003 161.5003 161.5003 0.0000 0.0000 0.0000 475 TRP B N   
7667 C CA  . TRP B 475 ? 161.4557 161.4557 161.4557 0.0000 0.0000 0.0000 475 TRP B CA  
7668 C C   . TRP B 475 ? 161.3124 161.3124 161.3124 0.0000 0.0000 0.0000 475 TRP B C   
7669 O O   . TRP B 475 ? 161.3822 161.3822 161.3822 0.0000 0.0000 0.0000 475 TRP B O   
7670 C CB  . TRP B 475 ? 161.4229 161.4229 161.4229 0.0000 0.0000 0.0000 475 TRP B CB  
7671 C CG  . TRP B 475 ? 161.4454 161.4454 161.4454 0.0000 0.0000 0.0000 475 TRP B CG  
7672 C CD1 . TRP B 475 ? 161.4260 161.4260 161.4260 0.0000 0.0000 0.0000 475 TRP B CD1 
7673 C CD2 . TRP B 475 ? 161.4599 161.4599 161.4599 0.0000 0.0000 0.0000 475 TRP B CD2 
7674 N NE1 . TRP B 475 ? 161.4711 161.4711 161.4711 0.0000 0.0000 0.0000 475 TRP B NE1 
7675 C CE2 . TRP B 475 ? 161.5501 161.5501 161.5501 0.0000 0.0000 0.0000 475 TRP B CE2 
7676 C CE3 . TRP B 475 ? 161.9151 161.9151 161.9151 0.0000 0.0000 0.0000 475 TRP B CE3 
7677 C CZ2 . TRP B 475 ? 161.9803 161.9803 161.9803 0.0000 0.0000 0.0000 475 TRP B CZ2 
7678 C CZ3 . TRP B 475 ? 161.5280 161.5280 161.5280 0.0000 0.0000 0.0000 475 TRP B CZ3 
7679 C CH2 . TRP B 475 ? 161.5358 161.5358 161.5358 0.0000 0.0000 0.0000 475 TRP B CH2 
7680 N N   . HIS B 476 ? 161.5028 161.5028 161.5028 0.0000 0.0000 0.0000 476 HIS B N   
7681 C CA  . HIS B 476 ? 161.5645 161.5645 161.5645 0.0000 0.0000 0.0000 476 HIS B CA  
7682 C C   . HIS B 476 ? 161.7148 161.7148 161.7148 0.0000 0.0000 0.0000 476 HIS B C   
7683 O O   . HIS B 476 ? 174.6443 174.6443 174.6443 0.0000 0.0000 0.0000 476 HIS B O   
7684 C CB  . HIS B 476 ? 174.7601 174.7601 174.7601 0.0000 0.0000 0.0000 476 HIS B CB  
7685 C CG  . HIS B 476 ? 174.6274 174.6274 174.6274 0.0000 0.0000 0.0000 476 HIS B CG  
7686 N ND1 . HIS B 476 ? 174.9685 174.9685 174.9685 0.0000 0.0000 0.0000 476 HIS B ND1 
7687 C CD2 . HIS B 476 ? 175.1013 175.1013 175.1013 0.0000 0.0000 0.0000 476 HIS B CD2 
7688 C CE1 . HIS B 476 ? 175.1340 175.1340 175.1340 0.0000 0.0000 0.0000 476 HIS B CE1 
7689 N NE2 . HIS B 476 ? 175.3772 175.3772 175.3772 0.0000 0.0000 0.0000 476 HIS B NE2 
7690 N N   . ARG B 477 ? 175.3899 175.3899 175.3899 0.0000 0.0000 0.0000 477 ARG B N   
7691 C CA  . ARG B 477 ? 175.4821 175.4821 175.4821 0.0000 0.0000 0.0000 477 ARG B CA  
7692 C C   . ARG B 477 ? 161.8860 161.8860 161.8860 0.0000 0.0000 0.0000 477 ARG B C   
7693 O O   . ARG B 477 ? 161.8354 161.8354 161.8354 0.0000 0.0000 0.0000 477 ARG B O   
7694 C CB  . ARG B 477 ? 161.5397 161.5397 161.5397 0.0000 0.0000 0.0000 477 ARG B CB  
7695 C CG  . ARG B 477 ? 161.5539 161.5539 161.5539 0.0000 0.0000 0.0000 477 ARG B CG  
7696 C CD  . ARG B 477 ? 161.3128 161.3128 161.3128 0.0000 0.0000 0.0000 477 ARG B CD  
7697 N NE  . ARG B 477 ? 161.3082 161.3082 161.3082 0.0000 0.0000 0.0000 477 ARG B NE  
7698 C CZ  . ARG B 477 ? 161.3670 161.3670 161.3670 0.0000 0.0000 0.0000 477 ARG B CZ  
7699 N NH1 . ARG B 477 ? 161.4751 161.4751 161.4751 0.0000 0.0000 0.0000 477 ARG B NH1 
7700 N NH2 . ARG B 477 ? 161.3500 161.3500 161.3500 0.0000 0.0000 0.0000 477 ARG B NH2 
7701 N N   . SER B 478 ? 161.5813 161.5813 161.5813 0.0000 0.0000 0.0000 478 SER B N   
7702 C CA  . SER B 478 ? 161.6435 161.6435 161.6435 0.0000 0.0000 0.0000 478 SER B CA  
7703 C C   . SER B 478 ? 161.7348 161.7348 161.7348 0.0000 0.0000 0.0000 478 SER B C   
7704 O O   . SER B 478 ? 161.3430 161.3430 161.3430 0.0000 0.0000 0.0000 478 SER B O   
7705 C CB  . SER B 478 ? 161.2496 161.2496 161.2496 0.0000 0.0000 0.0000 478 SER B CB  
7706 O OG  . SER B 478 ? 161.3257 161.3257 161.3257 0.0000 0.0000 0.0000 478 SER B OG  
7707 N N   . LYS B 479 ? 161.3746 161.3746 161.3746 0.0000 0.0000 0.0000 479 LYS B N   
7708 C CA  . LYS B 479 ? 161.2526 161.2526 161.2526 0.0000 0.0000 0.0000 479 LYS B CA  
7709 C C   . LYS B 479 ? 161.3527 161.3527 161.3527 0.0000 0.0000 0.0000 479 LYS B C   
7710 O O   . LYS B 479 ? 161.5652 161.5652 161.5652 0.0000 0.0000 0.0000 479 LYS B O   
7711 C CB  . LYS B 479 ? 161.4312 161.4312 161.4312 0.0000 0.0000 0.0000 479 LYS B CB  
7712 C CG  . LYS B 479 ? 161.4110 161.4110 161.4110 0.0000 0.0000 0.0000 479 LYS B CG  
7713 C CD  . LYS B 479 ? 161.4170 161.4170 161.4170 0.0000 0.0000 0.0000 479 LYS B CD  
7714 C CE  . LYS B 479 ? 161.6560 161.6560 161.6560 0.0000 0.0000 0.0000 479 LYS B CE  
7715 N NZ  . LYS B 479 ? 161.5038 161.5038 161.5038 0.0000 0.0000 0.0000 479 LYS B NZ  
7716 N N   . GLU B 480 ? 161.5320 161.5320 161.5320 0.0000 0.0000 0.0000 480 GLU B N   
7717 C CA  . GLU B 480 ? 161.4450 161.4450 161.4450 0.0000 0.0000 0.0000 480 GLU B CA  
7718 C C   . GLU B 480 ? 161.6325 161.6325 161.6325 0.0000 0.0000 0.0000 480 GLU B C   
7719 O O   . GLU B 480 ? 161.4488 161.4488 161.4488 0.0000 0.0000 0.0000 480 GLU B O   
7720 C CB  . GLU B 480 ? 161.2644 161.2644 161.2644 0.0000 0.0000 0.0000 480 GLU B CB  
7721 C CG  . GLU B 480 ? 161.2150 161.2150 161.2150 0.0000 0.0000 0.0000 480 GLU B CG  
7722 C CD  . GLU B 480 ? 161.1831 161.1831 161.1831 0.0000 0.0000 0.0000 480 GLU B CD  
7723 O OE1 . GLU B 480 ? 161.3409 161.3409 161.3409 0.0000 0.0000 0.0000 480 GLU B OE1 
7724 O OE2 . GLU B 480 ? 161.3181 161.3181 161.3181 0.0000 0.0000 0.0000 480 GLU B OE2 
7725 N N   . GLY B 481 ? 161.4920 161.4920 161.4920 0.0000 0.0000 0.0000 481 GLY B N   
7726 C CA  . GLY B 481 ? 161.5039 161.5039 161.5039 0.0000 0.0000 0.0000 481 GLY B CA  
7727 C C   . GLY B 481 ? 161.2370 161.2370 161.2370 0.0000 0.0000 0.0000 481 GLY B C   
7728 O O   . GLY B 481 ? 161.3684 161.3684 161.3684 0.0000 0.0000 0.0000 481 GLY B O   
7729 N N   . LEU B 482 ? 161.5840 161.5840 161.5840 0.0000 0.0000 0.0000 482 LEU B N   
7730 C CA  . LEU B 482 ? 161.4885 161.4885 161.4885 0.0000 0.0000 0.0000 482 LEU B CA  
7731 C C   . LEU B 482 ? 161.2258 161.2258 161.2258 0.0000 0.0000 0.0000 482 LEU B C   
7732 O O   . LEU B 482 ? 161.2616 161.2616 161.2616 0.0000 0.0000 0.0000 482 LEU B O   
7733 C CB  . LEU B 482 ? 161.3365 161.3365 161.3365 0.0000 0.0000 0.0000 482 LEU B CB  
7734 C CG  . LEU B 482 ? 161.5720 161.5720 161.5720 0.0000 0.0000 0.0000 482 LEU B CG  
7735 C CD1 . LEU B 482 ? 161.4349 161.4349 161.4349 0.0000 0.0000 0.0000 482 LEU B CD1 
7736 C CD2 . LEU B 482 ? 161.5741 161.5741 161.5741 0.0000 0.0000 0.0000 482 LEU B CD2 
7737 N N   . THR B 483 ? 161.6379 161.6379 161.6379 0.0000 0.0000 0.0000 483 THR B N   
7738 C CA  . THR B 483 ? 161.5368 161.5368 161.5368 0.0000 0.0000 0.0000 483 THR B CA  
7739 C C   . THR B 483 ? 161.5344 161.5344 161.5344 0.0000 0.0000 0.0000 483 THR B C   
7740 O O   . THR B 483 ? 161.1747 161.1747 161.1747 0.0000 0.0000 0.0000 483 THR B O   
7741 C CB  . THR B 483 ? 161.1973 161.1973 161.1973 0.0000 0.0000 0.0000 483 THR B CB  
7742 O OG1 . THR B 483 ? 161.2342 161.2342 161.2342 0.0000 0.0000 0.0000 483 THR B OG1 
7743 C CG2 . THR B 483 ? 161.2552 161.2552 161.2552 0.0000 0.0000 0.0000 483 THR B CG2 
7744 N N   . GLU B 484 ? 161.3048 161.3048 161.3048 0.0000 0.0000 0.0000 484 GLU B N   
7745 C CA  . GLU B 484 ? 161.4781 161.4781 161.4781 0.0000 0.0000 0.0000 484 GLU B CA  
7746 C C   . GLU B 484 ? 161.4378 161.4378 161.4378 0.0000 0.0000 0.0000 484 GLU B C   
7747 O O   . GLU B 484 ? 161.4832 161.4832 161.4832 0.0000 0.0000 0.0000 484 GLU B O   
7748 C CB  . GLU B 484 ? 161.5366 161.5366 161.5366 0.0000 0.0000 0.0000 484 GLU B CB  
7749 C CG  . GLU B 484 ? 161.6736 161.6736 161.6736 0.0000 0.0000 0.0000 484 GLU B CG  
7750 C CD  . GLU B 484 ? 161.5304 161.5304 161.5304 0.0000 0.0000 0.0000 484 GLU B CD  
7751 O OE1 . GLU B 484 ? 161.3765 161.3765 161.3765 0.0000 0.0000 0.0000 484 GLU B OE1 
7752 O OE2 . GLU B 484 ? 161.3666 161.3666 161.3666 0.0000 0.0000 0.0000 484 GLU B OE2 
7753 N N   . ARG B 485 ? 161.2784 161.2784 161.2784 0.0000 0.0000 0.0000 485 ARG B N   
7754 C CA  . ARG B 485 ? 161.5605 161.5605 161.5605 0.0000 0.0000 0.0000 485 ARG B CA  
7755 C C   . ARG B 485 ? 161.4194 161.4194 161.4194 0.0000 0.0000 0.0000 485 ARG B C   
7756 O O   . ARG B 485 ? 161.3401 161.3401 161.3401 0.0000 0.0000 0.0000 485 ARG B O   
7757 C CB  . ARG B 485 ? 161.6064 161.6064 161.6064 0.0000 0.0000 0.0000 485 ARG B CB  
7758 C CG  . ARG B 485 ? 161.3702 161.3702 161.3702 0.0000 0.0000 0.0000 485 ARG B CG  
7759 C CD  . ARG B 485 ? 161.1457 161.1457 161.1457 0.0000 0.0000 0.0000 485 ARG B CD  
7760 N NE  . ARG B 485 ? 161.2265 161.2265 161.2265 0.0000 0.0000 0.0000 485 ARG B NE  
7761 C CZ  . ARG B 485 ? 161.3823 161.3823 161.3823 0.0000 0.0000 0.0000 485 ARG B CZ  
7762 N NH1 . ARG B 485 ? 161.5834 161.5834 161.5834 0.0000 0.0000 0.0000 485 ARG B NH1 
7763 N NH2 . ARG B 485 ? 161.4178 161.4178 161.4178 0.0000 0.0000 0.0000 485 ARG B NH2 
7764 N N   . PHE B 486 ? 161.4976 161.4976 161.4976 0.0000 0.0000 0.0000 486 PHE B N   
7765 C CA  . PHE B 486 ? 161.7074 161.7074 161.7074 0.0000 0.0000 0.0000 486 PHE B CA  
7766 C C   . PHE B 486 ? 161.5512 161.5512 161.5512 0.0000 0.0000 0.0000 486 PHE B C   
7767 O O   . PHE B 486 ? 161.7034 161.7034 161.7034 0.0000 0.0000 0.0000 486 PHE B O   
7768 C CB  . PHE B 486 ? 161.6309 161.6309 161.6309 0.0000 0.0000 0.0000 486 PHE B CB  
7769 C CG  . PHE B 486 ? 161.6522 161.6522 161.6522 0.0000 0.0000 0.0000 486 PHE B CG  
7770 C CD1 . PHE B 486 ? 161.4445 161.4445 161.4445 0.0000 0.0000 0.0000 486 PHE B CD1 
7771 C CD2 . PHE B 486 ? 161.5068 161.5068 161.5068 0.0000 0.0000 0.0000 486 PHE B CD2 
7772 C CE1 . PHE B 486 ? 161.1574 161.1574 161.1574 0.0000 0.0000 0.0000 486 PHE B CE1 
7773 C CE2 . PHE B 486 ? 160.6838 160.6838 160.6838 0.0000 0.0000 0.0000 486 PHE B CE2 
7774 C CZ  . PHE B 486 ? 161.1063 161.1063 161.1063 0.0000 0.0000 0.0000 486 PHE B CZ  
7775 N N   . GLU B 487 ? 160.3631 160.3631 160.3631 0.0000 0.0000 0.0000 487 GLU B N   
7776 C CA  . GLU B 487 ? 161.4844 161.4844 161.4844 0.0000 0.0000 0.0000 487 GLU B CA  
7777 C C   . GLU B 487 ? 166.7087 166.7087 166.7087 0.0000 0.0000 0.0000 487 GLU B C   
7778 O O   . GLU B 487 ? 166.8947 166.8947 166.8947 0.0000 0.0000 0.0000 487 GLU B O   
7779 C CB  . GLU B 487 ? 166.8389 166.8389 166.8389 0.0000 0.0000 0.0000 487 GLU B CB  
7780 C CG  . GLU B 487 ? 166.5894 166.5894 166.5894 0.0000 0.0000 0.0000 487 GLU B CG  
7781 C CD  . GLU B 487 ? 165.6264 165.6264 165.6264 0.0000 0.0000 0.0000 487 GLU B CD  
7782 O OE1 . GLU B 487 ? 166.6249 166.6249 166.6249 0.0000 0.0000 0.0000 487 GLU B OE1 
7783 O OE2 . GLU B 487 ? 167.2016 167.2016 167.2016 0.0000 0.0000 0.0000 487 GLU B OE2 
7784 N N   . LEU B 488 ? 167.3942 167.3942 167.3942 0.0000 0.0000 0.0000 488 LEU B N   
7785 C CA  . LEU B 488 ? 161.6516 161.6516 161.6516 0.0000 0.0000 0.0000 488 LEU B CA  
7786 C C   . LEU B 488 ? 161.5358 161.5358 161.5358 0.0000 0.0000 0.0000 488 LEU B C   
7787 O O   . LEU B 488 ? 161.3692 161.3692 161.3692 0.0000 0.0000 0.0000 488 LEU B O   
7788 C CB  . LEU B 488 ? 161.3904 161.3904 161.3904 0.0000 0.0000 0.0000 488 LEU B CB  
7789 C CG  . LEU B 488 ? 161.5939 161.5939 161.5939 0.0000 0.0000 0.0000 488 LEU B CG  
7790 C CD1 . LEU B 488 ? 161.7658 161.7658 161.7658 0.0000 0.0000 0.0000 488 LEU B CD1 
7791 C CD2 . LEU B 488 ? 161.6688 161.6688 161.6688 0.0000 0.0000 0.0000 488 LEU B CD2 
7792 N N   . PHE B 489 ? 161.6003 161.6003 161.6003 0.0000 0.0000 0.0000 489 PHE B N   
7793 C CA  . PHE B 489 ? 161.7013 161.7013 161.7013 0.0000 0.0000 0.0000 489 PHE B CA  
7794 C C   . PHE B 489 ? 161.3494 161.3494 161.3494 0.0000 0.0000 0.0000 489 PHE B C   
7795 O O   . PHE B 489 ? 160.8927 160.8927 160.8927 0.0000 0.0000 0.0000 489 PHE B O   
7796 C CB  . PHE B 489 ? 161.0427 161.0427 161.0427 0.0000 0.0000 0.0000 489 PHE B CB  
7797 C CG  . PHE B 489 ? 161.1964 161.1964 161.1964 0.0000 0.0000 0.0000 489 PHE B CG  
7798 C CD1 . PHE B 489 ? 160.0108 160.0108 160.0108 0.0000 0.0000 0.0000 489 PHE B CD1 
7799 C CD2 . PHE B 489 ? 160.5712 160.5712 160.5712 0.0000 0.0000 0.0000 489 PHE B CD2 
7800 C CE1 . PHE B 489 ? 160.9678 160.9678 160.9678 0.0000 0.0000 0.0000 489 PHE B CE1 
7801 C CE2 . PHE B 489 ? 160.7299 160.7299 160.7299 0.0000 0.0000 0.0000 489 PHE B CE2 
7802 C CZ  . PHE B 489 ? 160.8563 160.8563 160.8563 0.0000 0.0000 0.0000 489 PHE B CZ  
7803 N N   . VAL B 490 ? 161.0077 161.0077 161.0077 0.0000 0.0000 0.0000 490 VAL B N   
7804 C CA  . VAL B 490 ? 161.2722 161.2722 161.2722 0.0000 0.0000 0.0000 490 VAL B CA  
7805 C C   . VAL B 490 ? 160.9336 160.9336 160.9336 0.0000 0.0000 0.0000 490 VAL B C   
7806 O O   . VAL B 490 ? 159.6597 159.6597 159.6597 0.0000 0.0000 0.0000 490 VAL B O   
7807 C CB  . VAL B 490 ? 161.3675 161.3675 161.3675 0.0000 0.0000 0.0000 490 VAL B CB  
7808 C CG1 . VAL B 490 ? 161.4926 161.4926 161.4926 0.0000 0.0000 0.0000 490 VAL B CG1 
7809 C CG2 . VAL B 490 ? 160.9510 160.9510 160.9510 0.0000 0.0000 0.0000 490 VAL B CG2 
7810 N N   . MET B 491 ? 161.1145 161.1145 161.1145 0.0000 0.0000 0.0000 491 MET B N   
7811 C CA  . MET B 491 ? 160.4992 160.4992 160.4992 0.0000 0.0000 0.0000 491 MET B CA  
7812 C C   . MET B 491 ? 161.3889 161.3889 161.3889 0.0000 0.0000 0.0000 491 MET B C   
7813 O O   . MET B 491 ? 160.6644 160.6644 160.6644 0.0000 0.0000 0.0000 491 MET B O   
7814 C CB  . MET B 491 ? 159.7150 159.7150 159.7150 0.0000 0.0000 0.0000 491 MET B CB  
7815 C CG  . MET B 491 ? 157.6993 157.6993 157.6993 0.0000 0.0000 0.0000 491 MET B CG  
7816 S SD  . MET B 491 ? 160.7620 160.7620 160.7620 0.0000 0.0000 0.0000 491 MET B SD  
7817 C CE  . MET B 491 ? 161.3024 161.3024 161.3024 0.0000 0.0000 0.0000 491 MET B CE  
7818 N N   . LYS B 492 ? 159.6151 159.6151 159.6151 0.0000 0.0000 0.0000 492 LYS B N   
7819 C CA  . LYS B 492 ? 160.9834 160.9834 160.9834 0.0000 0.0000 0.0000 492 LYS B CA  
7820 C C   . LYS B 492 ? 160.7922 160.7922 160.7922 0.0000 0.0000 0.0000 492 LYS B C   
7821 O O   . LYS B 492 ? 159.7213 159.7213 159.7213 0.0000 0.0000 0.0000 492 LYS B O   
7822 C CB  . LYS B 492 ? 160.7390 160.7390 160.7390 0.0000 0.0000 0.0000 492 LYS B CB  
7823 C CG  . LYS B 492 ? 161.3883 161.3883 161.3883 0.0000 0.0000 0.0000 492 LYS B CG  
7824 C CD  . LYS B 492 ? 159.3713 159.3713 159.3713 0.0000 0.0000 0.0000 492 LYS B CD  
7825 C CE  . LYS B 492 ? 158.4041 158.4041 158.4041 0.0000 0.0000 0.0000 492 LYS B CE  
7826 N NZ  . LYS B 492 ? 159.9849 159.9849 159.9849 0.0000 0.0000 0.0000 492 LYS B NZ  
7827 N N   . LYS B 493 ? 160.5627 160.5627 160.5627 0.0000 0.0000 0.0000 493 LYS B N   
7828 C CA  . LYS B 493 ? 159.1411 159.1411 159.1411 0.0000 0.0000 0.0000 493 LYS B CA  
7829 C C   . LYS B 493 ? 156.7390 156.7390 156.7390 0.0000 0.0000 0.0000 493 LYS B C   
7830 O O   . LYS B 493 ? 160.6243 160.6243 160.6243 0.0000 0.0000 0.0000 493 LYS B O   
7831 C CB  . LYS B 493 ? 160.7546 160.7546 160.7546 0.0000 0.0000 0.0000 493 LYS B CB  
7832 C CG  . LYS B 493 ? 161.5768 161.5768 161.5768 0.0000 0.0000 0.0000 493 LYS B CG  
7833 C CD  . LYS B 493 ? 159.9237 159.9237 159.9237 0.0000 0.0000 0.0000 493 LYS B CD  
7834 C CE  . LYS B 493 ? 160.1157 160.1157 160.1157 0.0000 0.0000 0.0000 493 LYS B CE  
7835 N NZ  . LYS B 493 ? 158.4422 158.4422 158.4422 0.0000 0.0000 0.0000 493 LYS B NZ  
7836 N N   . GLU B 494 ? 160.6166 160.6166 160.6166 0.0000 0.0000 0.0000 494 GLU B N   
7837 C CA  . GLU B 494 ? 161.2679 161.2679 161.2679 0.0000 0.0000 0.0000 494 GLU B CA  
7838 C C   . GLU B 494 ? 158.4268 158.4268 158.4268 0.0000 0.0000 0.0000 494 GLU B C   
7839 O O   . GLU B 494 ? 159.6487 159.6487 159.6487 0.0000 0.0000 0.0000 494 GLU B O   
7840 C CB  . GLU B 494 ? 160.9013 160.9013 160.9013 0.0000 0.0000 0.0000 494 GLU B CB  
7841 C CG  . GLU B 494 ? 159.7318 159.7318 159.7318 0.0000 0.0000 0.0000 494 GLU B CG  
7842 C CD  . GLU B 494 ? 158.2629 158.2629 158.2629 0.0000 0.0000 0.0000 494 GLU B CD  
7843 O OE1 . GLU B 494 ? 161.3267 161.3267 161.3267 0.0000 0.0000 0.0000 494 GLU B OE1 
7844 O OE2 . GLU B 494 ? 160.5380 160.5380 160.5380 0.0000 0.0000 0.0000 494 GLU B OE2 
7845 N N   . ILE B 495 ? 160.8303 160.8303 160.8303 0.0000 0.0000 0.0000 495 ILE B N   
7846 C CA  . ILE B 495 ? 160.7148 160.7148 160.7148 0.0000 0.0000 0.0000 495 ILE B CA  
7847 C C   . ILE B 495 ? 160.5841 160.5841 160.5841 0.0000 0.0000 0.0000 495 ILE B C   
7848 O O   . ILE B 495 ? 160.2124 160.2124 160.2124 0.0000 0.0000 0.0000 495 ILE B O   
7849 C CB  . ILE B 495 ? 160.0429 160.0429 160.0429 0.0000 0.0000 0.0000 495 ILE B CB  
7850 C CG1 . ILE B 495 ? 159.8902 159.8902 159.8902 0.0000 0.0000 0.0000 495 ILE B CG1 
7851 C CG2 . ILE B 495 ? 160.1494 160.1494 160.1494 0.0000 0.0000 0.0000 495 ILE B CG2 
7852 C CD1 . ILE B 495 ? 159.6072 159.6072 159.6072 0.0000 0.0000 0.0000 495 ILE B CD1 
7853 N N   . CYS B 496 ? 160.4583 160.4583 160.4583 0.0000 0.0000 0.0000 496 CYS B N   
7854 C CA  . CYS B 496 ? 161.2854 161.2854 161.2854 0.0000 0.0000 0.0000 496 CYS B CA  
7855 C C   . CYS B 496 ? 160.9157 160.9157 160.9157 0.0000 0.0000 0.0000 496 CYS B C   
7856 O O   . CYS B 496 ? 160.9551 160.9551 160.9551 0.0000 0.0000 0.0000 496 CYS B O   
7857 C CB  . CYS B 496 ? 160.4880 160.4880 160.4880 0.0000 0.0000 0.0000 496 CYS B CB  
7858 S SG  . CYS B 496 ? 158.9877 158.9877 158.9877 0.0000 0.0000 0.0000 496 CYS B SG  
7859 N N   . ASN B 497 ? 160.3093 160.3093 160.3093 0.0000 0.0000 0.0000 497 ASN B N   
7860 C CA  . ASN B 497 ? 160.9102 160.9102 160.9102 0.0000 0.0000 0.0000 497 ASN B CA  
7861 C C   . ASN B 497 ? 161.0844 161.0844 161.0844 0.0000 0.0000 0.0000 497 ASN B C   
7862 O O   . ASN B 497 ? 159.3923 159.3923 159.3923 0.0000 0.0000 0.0000 497 ASN B O   
7863 C CB  . ASN B 497 ? 158.5273 158.5273 158.5273 0.0000 0.0000 0.0000 497 ASN B CB  
7864 C CG  . ASN B 497 ? 159.9026 159.9026 159.9026 0.0000 0.0000 0.0000 497 ASN B CG  
7865 O OD1 . ASN B 497 ? 160.9577 160.9577 160.9577 0.0000 0.0000 0.0000 497 ASN B OD1 
7866 N ND2 . ASN B 497 ? 158.8929 158.8929 158.8929 0.0000 0.0000 0.0000 497 ASN B ND2 
7867 N N   . ALA B 498 ? 161.4093 161.4093 161.4093 0.0000 0.0000 0.0000 498 ALA B N   
7868 C CA  . ALA B 498 ? 161.2303 161.2303 161.2303 0.0000 0.0000 0.0000 498 ALA B CA  
7869 C C   . ALA B 498 ? 160.9015 160.9015 160.9015 0.0000 0.0000 0.0000 498 ALA B C   
7870 O O   . ALA B 498 ? 160.9552 160.9552 160.9552 0.0000 0.0000 0.0000 498 ALA B O   
7871 C CB  . ALA B 498 ? 161.3431 161.3431 161.3431 0.0000 0.0000 0.0000 498 ALA B CB  
7872 N N   . TYR B 499 ? 161.3265 161.3265 161.3265 0.0000 0.0000 0.0000 499 TYR B N   
7873 C CA  . TYR B 499 ? 161.3639 161.3639 161.3639 0.0000 0.0000 0.0000 499 TYR B CA  
7874 C C   . TYR B 499 ? 161.5744 161.5744 161.5744 0.0000 0.0000 0.0000 499 TYR B C   
7875 O O   . TYR B 499 ? 160.9149 160.9149 160.9149 0.0000 0.0000 0.0000 499 TYR B O   
7876 C CB  . TYR B 499 ? 160.2809 160.2809 160.2809 0.0000 0.0000 0.0000 499 TYR B CB  
7877 C CG  . TYR B 499 ? 161.4643 161.4643 161.4643 0.0000 0.0000 0.0000 499 TYR B CG  
7878 C CD1 . TYR B 499 ? 161.1481 161.1481 161.1481 0.0000 0.0000 0.0000 499 TYR B CD1 
7879 C CD2 . TYR B 499 ? 158.9430 158.9430 158.9430 0.0000 0.0000 0.0000 499 TYR B CD2 
7880 C CE1 . TYR B 499 ? 159.6925 159.6925 159.6925 0.0000 0.0000 0.0000 499 TYR B CE1 
7881 C CE2 . TYR B 499 ? 161.2943 161.2943 161.2943 0.0000 0.0000 0.0000 499 TYR B CE2 
7882 C CZ  . TYR B 499 ? 158.5399 158.5399 158.5399 0.0000 0.0000 0.0000 499 TYR B CZ  
7883 O OH  . TYR B 499 ? 161.5028 161.5028 161.5028 0.0000 0.0000 0.0000 499 TYR B OH  
7884 N N   . THR B 500 ? 161.3771 161.3771 161.3771 0.0000 0.0000 0.0000 500 THR B N   
7885 C CA  . THR B 500 ? 161.4695 161.4695 161.4695 0.0000 0.0000 0.0000 500 THR B CA  
7886 C C   . THR B 500 ? 161.7395 161.7395 161.7395 0.0000 0.0000 0.0000 500 THR B C   
7887 O O   . THR B 500 ? 161.3977 161.3977 161.3977 0.0000 0.0000 0.0000 500 THR B O   
7888 C CB  . THR B 500 ? 161.5359 161.5359 161.5359 0.0000 0.0000 0.0000 500 THR B CB  
7889 O OG1 . THR B 500 ? 161.6687 161.6687 161.6687 0.0000 0.0000 0.0000 500 THR B OG1 
7890 C CG2 . THR B 500 ? 161.5829 161.5829 161.5829 0.0000 0.0000 0.0000 500 THR B CG2 
7891 N N   . GLU B 501 ? 161.3983 161.3983 161.3983 0.0000 0.0000 0.0000 501 GLU B N   
7892 C CA  . GLU B 501 ? 161.4827 161.4827 161.4827 0.0000 0.0000 0.0000 501 GLU B CA  
7893 C C   . GLU B 501 ? 161.9076 161.9076 161.9076 0.0000 0.0000 0.0000 501 GLU B C   
7894 O O   . GLU B 501 ? 161.8572 161.8572 161.8572 0.0000 0.0000 0.0000 501 GLU B O   
7895 C CB  . GLU B 501 ? 161.5000 161.5000 161.5000 0.0000 0.0000 0.0000 501 GLU B CB  
7896 C CG  . GLU B 501 ? 161.4635 161.4635 161.4635 0.0000 0.0000 0.0000 501 GLU B CG  
7897 C CD  . GLU B 501 ? 161.5597 161.5597 161.5597 0.0000 0.0000 0.0000 501 GLU B CD  
7898 O OE1 . GLU B 501 ? 174.6428 174.6428 174.6428 0.0000 0.0000 0.0000 501 GLU B OE1 
7899 O OE2 . GLU B 501 ? 174.9512 174.9512 174.9512 0.0000 0.0000 0.0000 501 GLU B OE2 
7900 N N   . LEU B 502 ? 174.5334 174.5334 174.5334 0.0000 0.0000 0.0000 502 LEU B N   
7901 C CA  . LEU B 502 ? 174.8238 174.8238 174.8238 0.0000 0.0000 0.0000 502 LEU B CA  
7902 C C   . LEU B 502 ? 175.2793 175.2793 175.2793 0.0000 0.0000 0.0000 502 LEU B C   
7903 O O   . LEU B 502 ? 175.5379 175.5379 175.5379 0.0000 0.0000 0.0000 502 LEU B O   
7904 C CB  . LEU B 502 ? 175.3792 175.3792 175.3792 0.0000 0.0000 0.0000 502 LEU B CB  
7905 C CG  . LEU B 502 ? 175.5114 175.5114 175.5114 0.0000 0.0000 0.0000 502 LEU B CG  
7906 C CD1 . LEU B 502 ? 161.7545 161.7545 161.7545 0.0000 0.0000 0.0000 502 LEU B CD1 
7907 C CD2 . LEU B 502 ? 161.6290 161.6290 161.6290 0.0000 0.0000 0.0000 502 LEU B CD2 
7908 N N   . ASN B 503 ? 161.7452 161.7452 161.7452 0.0000 0.0000 0.0000 503 ASN B N   
7909 C CA  . ASN B 503 ? 161.9692 161.9692 161.9692 0.0000 0.0000 0.0000 503 ASN B CA  
7910 C C   . ASN B 503 ? 161.4824 161.4824 161.4824 0.0000 0.0000 0.0000 503 ASN B C   
7911 O O   . ASN B 503 ? 161.4694 161.4694 161.4694 0.0000 0.0000 0.0000 503 ASN B O   
7912 C CB  . ASN B 503 ? 161.4341 161.4341 161.4341 0.0000 0.0000 0.0000 503 ASN B CB  
7913 C CG  . ASN B 503 ? 161.4393 161.4393 161.4393 0.0000 0.0000 0.0000 503 ASN B CG  
7914 O OD1 . ASN B 503 ? 161.4802 161.4802 161.4802 0.0000 0.0000 0.0000 503 ASN B OD1 
7915 N ND2 . ASN B 503 ? 161.4427 161.4427 161.4427 0.0000 0.0000 0.0000 503 ASN B ND2 
7916 N N   . ASP B 504 ? 161.5421 161.5421 161.5421 0.0000 0.0000 0.0000 504 ASP B N   
7917 C CA  . ASP B 504 ? 161.5792 161.5792 161.5792 0.0000 0.0000 0.0000 504 ASP B CA  
7918 C C   . ASP B 504 ? 161.4685 161.4685 161.4685 0.0000 0.0000 0.0000 504 ASP B C   
7919 O O   . ASP B 504 ? 161.6510 161.6510 161.6510 0.0000 0.0000 0.0000 504 ASP B O   
7920 C CB  . ASP B 504 ? 161.9706 161.9706 161.9706 0.0000 0.0000 0.0000 504 ASP B CB  
7921 C CG  . ASP B 504 ? 161.4963 161.4963 161.4963 0.0000 0.0000 0.0000 504 ASP B CG  
7922 O OD1 . ASP B 504 ? 161.4287 161.4287 161.4287 0.0000 0.0000 0.0000 504 ASP B OD1 
7923 O OD2 . ASP B 504 ? 161.3543 161.3543 161.3543 0.0000 0.0000 0.0000 504 ASP B OD2 
7924 N N   . PRO B 505 ? 161.4412 161.4412 161.4412 0.0000 0.0000 0.0000 505 PRO B N   
7925 C CA  . PRO B 505 ? 161.4516 161.4516 161.4516 0.0000 0.0000 0.0000 505 PRO B CA  
7926 C C   . PRO B 505 ? 161.6308 161.6308 161.6308 0.0000 0.0000 0.0000 505 PRO B C   
7927 O O   . PRO B 505 ? 161.5227 161.5227 161.5227 0.0000 0.0000 0.0000 505 PRO B O   
7928 C CB  . PRO B 505 ? 161.6524 161.6524 161.6524 0.0000 0.0000 0.0000 505 PRO B CB  
7929 C CG  . PRO B 505 ? 161.9590 161.9590 161.9590 0.0000 0.0000 0.0000 505 PRO B CG  
7930 C CD  . PRO B 505 ? 161.6094 161.6094 161.6094 0.0000 0.0000 0.0000 505 PRO B CD  
7931 N N   . MET B 506 ? 161.5404 161.5404 161.5404 0.0000 0.0000 0.0000 506 MET B N   
7932 C CA  . MET B 506 ? 161.5187 161.5187 161.5187 0.0000 0.0000 0.0000 506 MET B CA  
7933 C C   . MET B 506 ? 161.6325 161.6325 161.6325 0.0000 0.0000 0.0000 506 MET B C   
7934 O O   . MET B 506 ? 161.5691 161.5691 161.5691 0.0000 0.0000 0.0000 506 MET B O   
7935 C CB  . MET B 506 ? 161.5391 161.5391 161.5391 0.0000 0.0000 0.0000 506 MET B CB  
7936 C CG  . MET B 506 ? 161.6952 161.6952 161.6952 0.0000 0.0000 0.0000 506 MET B CG  
7937 S SD  . MET B 506 ? 162.4681 162.4681 162.4681 0.0000 0.0000 0.0000 506 MET B SD  
7938 C CE  . MET B 506 ? 162.3989 162.3989 162.3989 0.0000 0.0000 0.0000 506 MET B CE  
7939 N N   . ARG B 507 ? 162.7017 162.7017 162.7017 0.0000 0.0000 0.0000 507 ARG B N   
7940 C CA  . ARG B 507 ? 163.1062 163.1062 163.1062 0.0000 0.0000 0.0000 507 ARG B CA  
7941 C C   . ARG B 507 ? 162.4334 162.4334 162.4334 0.0000 0.0000 0.0000 507 ARG B C   
7942 O O   . ARG B 507 ? 162.4546 162.4546 162.4546 0.0000 0.0000 0.0000 507 ARG B O   
7943 C CB  . ARG B 507 ? 162.6144 162.6144 162.6144 0.0000 0.0000 0.0000 507 ARG B CB  
7944 C CG  . ARG B 507 ? 162.5493 162.5493 162.5493 0.0000 0.0000 0.0000 507 ARG B CG  
7945 C CD  . ARG B 507 ? 162.6989 162.6989 162.6989 0.0000 0.0000 0.0000 507 ARG B CD  
7946 N NE  . ARG B 507 ? 161.6539 161.6539 161.6539 0.0000 0.0000 0.0000 507 ARG B NE  
7947 C CZ  . ARG B 507 ? 161.6336 161.6336 161.6336 0.0000 0.0000 0.0000 507 ARG B CZ  
7948 N NH1 . ARG B 507 ? 161.9250 161.9250 161.9250 0.0000 0.0000 0.0000 507 ARG B NH1 
7949 N NH2 . ARG B 507 ? 162.3154 162.3154 162.3154 0.0000 0.0000 0.0000 507 ARG B NH2 
7950 N N   . GLN B 508 ? 161.4970 161.4970 161.4970 0.0000 0.0000 0.0000 508 GLN B N   
7951 C CA  . GLN B 508 ? 161.3798 161.3798 161.3798 0.0000 0.0000 0.0000 508 GLN B CA  
7952 C C   . GLN B 508 ? 161.4629 161.4629 161.4629 0.0000 0.0000 0.0000 508 GLN B C   
7953 O O   . GLN B 508 ? 161.6827 161.6827 161.6827 0.0000 0.0000 0.0000 508 GLN B O   
7954 C CB  . GLN B 508 ? 164.0932 164.0932 164.0932 0.0000 0.0000 0.0000 508 GLN B CB  
7955 C CG  . GLN B 508 ? 164.1823 164.1823 164.1823 0.0000 0.0000 0.0000 508 GLN B CG  
7956 C CD  . GLN B 508 ? 164.7286 164.7286 164.7286 0.0000 0.0000 0.0000 508 GLN B CD  
7957 O OE1 . GLN B 508 ? 165.1252 165.1252 165.1252 0.0000 0.0000 0.0000 508 GLN B OE1 
7958 N NE2 . GLN B 508 ? 164.1883 164.1883 164.1883 0.0000 0.0000 0.0000 508 GLN B NE2 
7959 N N   . ARG B 509 ? 163.9906 163.9906 163.9906 0.0000 0.0000 0.0000 509 ARG B N   
7960 C CA  . ARG B 509 ? 163.9999 163.9999 163.9999 0.0000 0.0000 0.0000 509 ARG B CA  
7961 C C   . ARG B 509 ? 164.2839 164.2839 164.2839 0.0000 0.0000 0.0000 509 ARG B C   
7962 O O   . ARG B 509 ? 164.2174 164.2174 164.2174 0.0000 0.0000 0.0000 509 ARG B O   
7963 C CB  . ARG B 509 ? 164.3855 164.3855 164.3855 0.0000 0.0000 0.0000 509 ARG B CB  
7964 C CG  . ARG B 509 ? 164.1581 164.1581 164.1581 0.0000 0.0000 0.0000 509 ARG B CG  
7965 C CD  . ARG B 509 ? 172.2762 172.2762 172.2762 0.0000 0.0000 0.0000 509 ARG B CD  
7966 N NE  . ARG B 509 ? 172.6125 172.6125 172.6125 0.0000 0.0000 0.0000 509 ARG B NE  
7967 C CZ  . ARG B 509 ? 173.1044 173.1044 173.1044 0.0000 0.0000 0.0000 509 ARG B CZ  
7968 N NH1 . ARG B 509 ? 173.6684 173.6684 173.6684 0.0000 0.0000 0.0000 509 ARG B NH1 
7969 N NH2 . ARG B 509 ? 172.6270 172.6270 172.6270 0.0000 0.0000 0.0000 509 ARG B NH2 
7970 N N   . GLN B 510 ? 172.7701 172.7701 172.7701 0.0000 0.0000 0.0000 510 GLN B N   
7971 C CA  . GLN B 510 ? 172.5894 172.5894 172.5894 0.0000 0.0000 0.0000 510 GLN B CA  
7972 C C   . GLN B 510 ? 172.6115 172.6115 172.6115 0.0000 0.0000 0.0000 510 GLN B C   
7973 O O   . GLN B 510 ? 172.6073 172.6073 172.6073 0.0000 0.0000 0.0000 510 GLN B O   
7974 C CB  . GLN B 510 ? 182.3293 182.3293 182.3293 0.0000 0.0000 0.0000 510 GLN B CB  
7975 C CG  . GLN B 510 ? 182.8137 182.8137 182.8137 0.0000 0.0000 0.0000 510 GLN B CG  
7976 C CD  . GLN B 510 ? 183.0601 183.0601 183.0601 0.0000 0.0000 0.0000 510 GLN B CD  
7977 O OE1 . GLN B 510 ? 183.3779 183.3779 183.3779 0.0000 0.0000 0.0000 510 GLN B OE1 
7978 N NE2 . GLN B 510 ? 182.8992 182.8992 182.8992 0.0000 0.0000 0.0000 510 GLN B NE2 
7979 N N   . LEU B 511 ? 183.0493 183.0493 183.0493 0.0000 0.0000 0.0000 511 LEU B N   
7980 C CA  . LEU B 511 ? 183.2598 183.2598 183.2598 0.0000 0.0000 0.0000 511 LEU B CA  
7981 C C   . LEU B 511 ? 183.2022 183.2022 183.2022 0.0000 0.0000 0.0000 511 LEU B C   
7982 O O   . LEU B 511 ? 183.3703 183.3703 183.3703 0.0000 0.0000 0.0000 511 LEU B O   
7983 C CB  . LEU B 511 ? 181.3616 181.3616 181.3616 0.0000 0.0000 0.0000 511 LEU B CB  
7984 C CG  . LEU B 511 ? 181.6414 181.6414 181.6414 0.0000 0.0000 0.0000 511 LEU B CG  
7985 C CD1 . LEU B 511 ? 182.0891 182.0891 182.0891 0.0000 0.0000 0.0000 511 LEU B CD1 
7986 C CD2 . LEU B 511 ? 182.5852 182.5852 182.5852 0.0000 0.0000 0.0000 511 LEU B CD2 
7987 N N   . PHE B 512 ? 181.6768 181.6768 181.6768 0.0000 0.0000 0.0000 512 PHE B N   
7988 C CA  . PHE B 512 ? 181.4012 181.4012 181.4012 0.0000 0.0000 0.0000 512 PHE B CA  
7989 C C   . PHE B 512 ? 181.5428 181.5428 181.5428 0.0000 0.0000 0.0000 512 PHE B C   
7990 O O   . PHE B 512 ? 181.8021 181.8021 181.8021 0.0000 0.0000 0.0000 512 PHE B O   
7991 C CB  . PHE B 512 ? 181.4667 181.4667 181.4667 0.0000 0.0000 0.0000 512 PHE B CB  
7992 C CG  . PHE B 512 ? 186.6235 186.6235 186.6235 0.0000 0.0000 0.0000 512 PHE B CG  
7993 C CD1 . PHE B 512 ? 186.9155 186.9155 186.9155 0.0000 0.0000 0.0000 512 PHE B CD1 
7994 C CD2 . PHE B 512 ? 187.5190 187.5190 187.5190 0.0000 0.0000 0.0000 512 PHE B CD2 
7995 C CE1 . PHE B 512 ? 187.9681 187.9681 187.9681 0.0000 0.0000 0.0000 512 PHE B CE1 
7996 C CE2 . PHE B 512 ? 186.8156 186.8156 186.8156 0.0000 0.0000 0.0000 512 PHE B CE2 
7997 C CZ  . PHE B 512 ? 194.1602 194.1602 194.1602 0.0000 0.0000 0.0000 512 PHE B CZ  
7998 N N   . GLU B 513 ? 194.4590 194.4590 194.4590 0.0000 0.0000 0.0000 513 GLU B N   
7999 C CA  . GLU B 513 ? 194.9505 194.9505 194.9505 0.0000 0.0000 0.0000 513 GLU B CA  
8000 C C   . GLU B 513 ? 195.2897 195.2897 195.2897 0.0000 0.0000 0.0000 513 GLU B C   
8001 O O   . GLU B 513 ? 194.4386 194.4386 194.4386 0.0000 0.0000 0.0000 513 GLU B O   
8002 C CB  . GLU B 513 ? 194.5853 194.5853 194.5853 0.0000 0.0000 0.0000 513 GLU B CB  
8003 C CG  . GLU B 513 ? 194.4960 194.4960 194.4960 0.0000 0.0000 0.0000 513 GLU B CG  
8004 C CD  . GLU B 513 ? 194.3501 194.3501 194.3501 0.0000 0.0000 0.0000 513 GLU B CD  
8005 O OE1 . GLU B 513 ? 194.4637 194.4637 194.4637 0.0000 0.0000 0.0000 513 GLU B OE1 
8006 O OE2 . GLU B 513 ? 205.2336 205.2336 205.2336 0.0000 0.0000 0.0000 513 GLU B OE2 
8007 N N   . GLU B 514 ? 205.7478 205.7478 205.7478 0.0000 0.0000 0.0000 514 GLU B N   
8008 C CA  . GLU B 514 ? 206.2758 206.2758 206.2758 0.0000 0.0000 0.0000 514 GLU B CA  
8009 C C   . GLU B 514 ? 206.8224 206.8224 206.8224 0.0000 0.0000 0.0000 514 GLU B C   
8010 O O   . GLU B 514 ? 205.7714 205.7714 205.7714 0.0000 0.0000 0.0000 514 GLU B O   
8011 C CB  . GLU B 514 ? 208.4584 208.4584 208.4584 0.0000 0.0000 0.0000 514 GLU B CB  
8012 C CG  . GLU B 514 ? 208.7423 208.7423 208.7423 0.0000 0.0000 0.0000 514 GLU B CG  
8013 C CD  . GLU B 514 ? 208.8646 208.8646 208.8646 0.0000 0.0000 0.0000 514 GLU B CD  
8014 O OE1 . GLU B 514 ? 209.1403 209.1403 209.1403 0.0000 0.0000 0.0000 514 GLU B OE1 
8015 O OE2 . GLU B 514 ? 208.6082 208.6082 208.6082 0.0000 0.0000 0.0000 514 GLU B OE2 
8016 N N   . GLN B 515 ? 208.8472 208.8472 208.8472 0.0000 0.0000 0.0000 515 GLN B N   
8017 C CA  . GLN B 515 ? 208.6936 208.6936 208.6936 0.0000 0.0000 0.0000 515 GLN B CA  
8018 C C   . GLN B 515 ? 208.6989 208.6989 208.6989 0.0000 0.0000 0.0000 515 GLN B C   
8019 O O   . GLN B 515 ? 209.0162 209.0162 209.0162 0.0000 0.0000 0.0000 515 GLN B O   
8020 C CB  . GLN B 515 ? 211.7422 211.7422 211.7422 0.0000 0.0000 0.0000 515 GLN B CB  
8021 C CG  . GLN B 515 ? 211.9792 211.9792 211.9792 0.0000 0.0000 0.0000 515 GLN B CG  
8022 C CD  . GLN B 515 ? 212.2957 212.2957 212.2957 0.0000 0.0000 0.0000 515 GLN B CD  
8023 O OE1 . GLN B 515 ? 212.3162 212.3162 212.3162 0.0000 0.0000 0.0000 515 GLN B OE1 
8024 N NE2 . GLN B 515 ? 211.9151 211.9151 211.9151 0.0000 0.0000 0.0000 515 GLN B NE2 
8025 N N   . ALA B 516 ? 225.1911 225.1911 225.1911 0.0000 0.0000 0.0000 516 ALA B N   
8026 C CA  . ALA B 516 ? 225.6289 225.6289 225.6289 0.0000 0.0000 0.0000 516 ALA B CA  
8027 C C   . ALA B 516 ? 225.8362 225.8362 225.8362 0.0000 0.0000 0.0000 516 ALA B C   
8028 O O   . ALA B 516 ? 225.9643 225.9643 225.9643 0.0000 0.0000 0.0000 516 ALA B O   
8029 C CB  . ALA B 516 ? 225.7636 225.7636 225.7636 0.0000 0.0000 0.0000 516 ALA B CB  
8030 N N   . LYS B 517 ? 231.0129 231.0129 231.0129 0.0000 0.0000 0.0000 517 LYS B N   
8031 C CA  . LYS B 517 ? 231.3242 231.3242 231.3242 0.0000 0.0000 0.0000 517 LYS B CA  
8032 C C   . LYS B 517 ? 231.4552 231.4552 231.4552 0.0000 0.0000 0.0000 517 LYS B C   
8033 O O   . LYS B 517 ? 231.4953 231.4953 231.4953 0.0000 0.0000 0.0000 517 LYS B O   
8034 C CB  . LYS B 517 ? 232.7779 232.7779 232.7779 0.0000 0.0000 0.0000 517 LYS B CB  
8035 C CG  . LYS B 517 ? 232.8725 232.8725 232.8725 0.0000 0.0000 0.0000 517 LYS B CG  
8036 C CD  . LYS B 517 ? 232.9019 232.9019 232.9019 0.0000 0.0000 0.0000 517 LYS B CD  
8037 C CE  . LYS B 517 ? 232.7233 232.7233 232.7233 0.0000 0.0000 0.0000 517 LYS B CE  
8038 N NZ  . LYS B 517 ? 232.7961 232.7961 232.7961 0.0000 0.0000 0.0000 517 LYS B NZ  
8039 N N   . ALA B 518 ? 232.8794 232.8794 232.8794 0.0000 0.0000 0.0000 518 ALA B N   
8040 C CA  . ALA B 518 ? 232.9633 232.9633 232.9633 0.0000 0.0000 0.0000 518 ALA B CA  
8041 C C   . ALA B 518 ? 232.9007 232.9007 232.9007 0.0000 0.0000 0.0000 518 ALA B C   
8042 O O   . ALA B 518 ? 237.4552 237.4552 237.4552 0.0000 0.0000 0.0000 518 ALA B O   
8043 C CB  . ALA B 518 ? 237.5259 237.5259 237.5259 0.0000 0.0000 0.0000 518 ALA B CB  
8044 N N   . LYS B 519 ? 237.2331 237.2331 237.2331 0.0000 0.0000 0.0000 519 LYS B N   
8045 C CA  . LYS B 519 ? 237.2220 237.2220 237.2220 0.0000 0.0000 0.0000 519 LYS B CA  
8046 C C   . LYS B 519 ? 237.6827 237.6827 237.6827 0.0000 0.0000 0.0000 519 LYS B C   
8047 O O   . LYS B 519 ? 237.6069 237.6069 237.6069 0.0000 0.0000 0.0000 519 LYS B O   
8048 C CB  . LYS B 519 ? 237.5837 237.5837 237.5837 0.0000 0.0000 0.0000 519 LYS B CB  
8049 C CG  . LYS B 519 ? 237.3055 237.3055 237.3055 0.0000 0.0000 0.0000 519 LYS B CG  
8050 C CD  . LYS B 519 ? 227.7467 227.7467 227.7467 0.0000 0.0000 0.0000 519 LYS B CD  
8051 C CE  . LYS B 519 ? 227.3095 227.3095 227.3095 0.0000 0.0000 0.0000 519 LYS B CE  
8052 N NZ  . LYS B 519 ? 226.9628 226.9628 226.9628 0.0000 0.0000 0.0000 519 LYS B NZ  
8053 N N   . ALA B 520 ? 226.5922 226.5922 226.5922 0.0000 0.0000 0.0000 520 ALA B N   
8054 C CA  . ALA B 520 ? 227.1388 227.1388 227.1388 0.0000 0.0000 0.0000 520 ALA B CA  
8055 C C   . ALA B 520 ? 227.0040 227.0040 227.0040 0.0000 0.0000 0.0000 520 ALA B C   
8056 O O   . ALA B 520 ? 227.0483 227.0483 227.0483 0.0000 0.0000 0.0000 520 ALA B O   
8057 C CB  . ALA B 520 ? 227.2871 227.2871 227.2871 0.0000 0.0000 0.0000 520 ALA B CB  
8058 N N   . ALA B 521 ? 226.9590 226.9590 226.9590 0.0000 0.0000 0.0000 521 ALA B N   
8059 C CA  . ALA B 521 ? 214.2658 214.2658 214.2658 0.0000 0.0000 0.0000 521 ALA B CA  
8060 C C   . ALA B 521 ? 213.5901 213.5901 213.5901 0.0000 0.0000 0.0000 521 ALA B C   
8061 O O   . ALA B 521 ? 213.3021 213.3021 213.3021 0.0000 0.0000 0.0000 521 ALA B O   
8062 C CB  . ALA B 521 ? 213.4866 213.4866 213.4866 0.0000 0.0000 0.0000 521 ALA B CB  
8063 N N   . GLY B 522 ? 213.4150 213.4150 213.4150 0.0000 0.0000 0.0000 522 GLY B N   
8064 C CA  . GLY B 522 ? 201.0002 201.0002 201.0002 0.0000 0.0000 0.0000 522 GLY B CA  
8065 C C   . GLY B 522 ? 200.8629 200.8629 200.8629 0.0000 0.0000 0.0000 522 GLY B C   
8066 O O   . GLY B 522 ? 200.8349 200.8349 200.8349 0.0000 0.0000 0.0000 522 GLY B O   
8067 N N   . ASP B 523 ? 200.6577 200.6577 200.6577 0.0000 0.0000 0.0000 523 ASP B N   
8068 C CA  . ASP B 523 ? 200.6365 200.6365 200.6365 0.0000 0.0000 0.0000 523 ASP B CA  
8069 C C   . ASP B 523 ? 200.5192 200.5192 200.5192 0.0000 0.0000 0.0000 523 ASP B C   
8070 O O   . ASP B 523 ? 199.9704 199.9704 199.9704 0.0000 0.0000 0.0000 523 ASP B O   
8071 C CB  . ASP B 523 ? 200.0354 200.0354 200.0354 0.0000 0.0000 0.0000 523 ASP B CB  
8072 C CG  . ASP B 523 ? 203.7632 203.7632 203.7632 0.0000 0.0000 0.0000 523 ASP B CG  
8073 O OD1 . ASP B 523 ? 203.6812 203.6812 203.6812 0.0000 0.0000 0.0000 523 ASP B OD1 
8074 O OD2 . ASP B 523 ? 203.6265 203.6265 203.6265 0.0000 0.0000 0.0000 523 ASP B OD2 
8075 N N   . ASP B 524 ? 203.2574 203.2574 203.2574 0.0000 0.0000 0.0000 524 ASP B N   
8076 C CA  . ASP B 524 ? 203.6221 203.6221 203.6221 0.0000 0.0000 0.0000 524 ASP B CA  
8077 C C   . ASP B 524 ? 203.6872 203.6872 203.6872 0.0000 0.0000 0.0000 524 ASP B C   
8078 O O   . ASP B 524 ? 203.6705 203.6705 203.6705 0.0000 0.0000 0.0000 524 ASP B O   
8079 C CB  . ASP B 524 ? 203.7831 203.7831 203.7831 0.0000 0.0000 0.0000 524 ASP B CB  
8080 C CG  . ASP B 524 ? 203.7229 203.7229 203.7229 0.0000 0.0000 0.0000 524 ASP B CG  
8081 O OD1 . ASP B 524 ? 203.8275 203.8275 203.8275 0.0000 0.0000 0.0000 524 ASP B OD1 
8082 O OD2 . ASP B 524 ? 203.7719 203.7719 203.7719 0.0000 0.0000 0.0000 524 ASP B OD2 
8083 N N   . GLU B 525 ? 192.9949 192.9949 192.9949 0.0000 0.0000 0.0000 525 GLU B N   
8084 C CA  . GLU B 525 ? 192.5116 192.5116 192.5116 0.0000 0.0000 0.0000 525 GLU B CA  
8085 C C   . GLU B 525 ? 192.5264 192.5264 192.5264 0.0000 0.0000 0.0000 525 GLU B C   
8086 O O   . GLU B 525 ? 192.5425 192.5425 192.5425 0.0000 0.0000 0.0000 525 GLU B O   
8087 C CB  . GLU B 525 ? 192.5617 192.5617 192.5617 0.0000 0.0000 0.0000 525 GLU B CB  
8088 C CG  . GLU B 525 ? 192.5086 192.5086 192.5086 0.0000 0.0000 0.0000 525 GLU B CG  
8089 C CD  . GLU B 525 ? 192.6869 192.6869 192.6869 0.0000 0.0000 0.0000 525 GLU B CD  
8090 O OE1 . GLU B 525 ? 192.2871 192.2871 192.2871 0.0000 0.0000 0.0000 525 GLU B OE1 
8091 O OE2 . GLU B 525 ? 190.1070 190.1070 190.1070 0.0000 0.0000 0.0000 525 GLU B OE2 
8092 N N   . ALA B 526 ? 189.9983 189.9983 189.9983 0.0000 0.0000 0.0000 526 ALA B N   
8093 C CA  . ALA B 526 ? 189.7789 189.7789 189.7789 0.0000 0.0000 0.0000 526 ALA B CA  
8094 C C   . ALA B 526 ? 189.4760 189.4760 189.4760 0.0000 0.0000 0.0000 526 ALA B C   
8095 O O   . ALA B 526 ? 189.8159 189.8159 189.8159 0.0000 0.0000 0.0000 526 ALA B O   
8096 C CB  . ALA B 526 ? 189.7402 189.7402 189.7402 0.0000 0.0000 0.0000 526 ALA B CB  
8097 N N   . MET B 527 ? 189.6572 189.6572 189.6572 0.0000 0.0000 0.0000 527 MET B N   
8098 C CA  . MET B 527 ? 189.9557 189.9557 189.9557 0.0000 0.0000 0.0000 527 MET B CA  
8099 C C   . MET B 527 ? 189.5295 189.5295 189.5295 0.0000 0.0000 0.0000 527 MET B C   
8100 O O   . MET B 527 ? 189.2524 189.2524 189.2524 0.0000 0.0000 0.0000 527 MET B O   
8101 C CB  . MET B 527 ? 188.6405 188.6405 188.6405 0.0000 0.0000 0.0000 527 MET B CB  
8102 C CG  . MET B 527 ? 188.4412 188.4412 188.4412 0.0000 0.0000 0.0000 527 MET B CG  
8103 S SD  . MET B 527 ? 189.5860 189.5860 189.5860 0.0000 0.0000 0.0000 527 MET B SD  
8104 C CE  . MET B 527 ? 189.7747 189.7747 189.7747 0.0000 0.0000 0.0000 527 MET B CE  
8105 N N   . PHE B 528 ? 189.7417 189.7417 189.7417 0.0000 0.0000 0.0000 528 PHE B N   
8106 C CA  . PHE B 528 ? 189.6339 189.6339 189.6339 0.0000 0.0000 0.0000 528 PHE B CA  
8107 C C   . PHE B 528 ? 189.8575 189.8575 189.8575 0.0000 0.0000 0.0000 528 PHE B C   
8108 O O   . PHE B 528 ? 175.4614 175.4614 175.4614 0.0000 0.0000 0.0000 528 PHE B O   
8109 C CB  . PHE B 528 ? 175.0079 175.0079 175.0079 0.0000 0.0000 0.0000 528 PHE B CB  
8110 C CG  . PHE B 528 ? 174.4938 174.4938 174.4938 0.0000 0.0000 0.0000 528 PHE B CG  
8111 C CD1 . PHE B 528 ? 174.2371 174.2371 174.2371 0.0000 0.0000 0.0000 528 PHE B CD1 
8112 C CD2 . PHE B 528 ? 175.0969 175.0969 175.0969 0.0000 0.0000 0.0000 528 PHE B CD2 
8113 C CE1 . PHE B 528 ? 175.1241 175.1241 175.1241 0.0000 0.0000 0.0000 528 PHE B CE1 
8114 C CE2 . PHE B 528 ? 175.3011 175.3011 175.3011 0.0000 0.0000 0.0000 528 PHE B CE2 
8115 C CZ  . PHE B 528 ? 175.1366 175.1366 175.1366 0.0000 0.0000 0.0000 528 PHE B CZ  
8116 N N   . ILE B 529 ? 162.7019 162.7019 162.7019 0.0000 0.0000 0.0000 529 ILE B N   
8117 C CA  . ILE B 529 ? 161.9470 161.9470 161.9470 0.0000 0.0000 0.0000 529 ILE B CA  
8118 C C   . ILE B 529 ? 161.7788 161.7788 161.7788 0.0000 0.0000 0.0000 529 ILE B C   
8119 O O   . ILE B 529 ? 161.6971 161.6971 161.6971 0.0000 0.0000 0.0000 529 ILE B O   
8120 C CB  . ILE B 529 ? 161.8911 161.8911 161.8911 0.0000 0.0000 0.0000 529 ILE B CB  
8121 C CG1 . ILE B 529 ? 161.4614 161.4614 161.4614 0.0000 0.0000 0.0000 529 ILE B CG1 
8122 C CG2 . ILE B 529 ? 161.4370 161.4370 161.4370 0.0000 0.0000 0.0000 529 ILE B CG2 
8123 C CD1 . ILE B 529 ? 161.5043 161.5043 161.5043 0.0000 0.0000 0.0000 529 ILE B CD1 
8124 N N   . ASP B 530 ? 161.4788 161.4788 161.4788 0.0000 0.0000 0.0000 530 ASP B N   
8125 C CA  . ASP B 530 ? 161.5509 161.5509 161.5509 0.0000 0.0000 0.0000 530 ASP B CA  
8126 C C   . ASP B 530 ? 161.4870 161.4870 161.4870 0.0000 0.0000 0.0000 530 ASP B C   
8127 O O   . ASP B 530 ? 162.7569 162.7569 162.7569 0.0000 0.0000 0.0000 530 ASP B O   
8128 C CB  . ASP B 530 ? 162.4424 162.4424 162.4424 0.0000 0.0000 0.0000 530 ASP B CB  
8129 C CG  . ASP B 530 ? 162.4937 162.4937 162.4937 0.0000 0.0000 0.0000 530 ASP B CG  
8130 O OD1 . ASP B 530 ? 162.6666 162.6666 162.6666 0.0000 0.0000 0.0000 530 ASP B OD1 
8131 O OD2 . ASP B 530 ? 162.5533 162.5533 162.5533 0.0000 0.0000 0.0000 530 ASP B OD2 
8132 N N   . GLU B 531 ? 162.6274 162.6274 162.6274 0.0000 0.0000 0.0000 531 GLU B N   
8133 C CA  . GLU B 531 ? 161.6303 161.6303 161.6303 0.0000 0.0000 0.0000 531 GLU B CA  
8134 C C   . GLU B 531 ? 161.4240 161.4240 161.4240 0.0000 0.0000 0.0000 531 GLU B C   
8135 O O   . GLU B 531 ? 161.4912 161.4912 161.4912 0.0000 0.0000 0.0000 531 GLU B O   
8136 C CB  . GLU B 531 ? 161.5599 161.5599 161.5599 0.0000 0.0000 0.0000 531 GLU B CB  
8137 C CG  . GLU B 531 ? 161.5313 161.5313 161.5313 0.0000 0.0000 0.0000 531 GLU B CG  
8138 C CD  . GLU B 531 ? 161.6247 161.6247 161.6247 0.0000 0.0000 0.0000 531 GLU B CD  
8139 O OE1 . GLU B 531 ? 161.5129 161.5129 161.5129 0.0000 0.0000 0.0000 531 GLU B OE1 
8140 O OE2 . GLU B 531 ? 161.6272 161.6272 161.6272 0.0000 0.0000 0.0000 531 GLU B OE2 
8141 N N   . ASN B 532 ? 161.5519 161.5519 161.5519 0.0000 0.0000 0.0000 532 ASN B N   
8142 C CA  . ASN B 532 ? 161.1993 161.1993 161.1993 0.0000 0.0000 0.0000 532 ASN B CA  
8143 C C   . ASN B 532 ? 160.8766 160.8766 160.8766 0.0000 0.0000 0.0000 532 ASN B C   
8144 O O   . ASN B 532 ? 161.6841 161.6841 161.6841 0.0000 0.0000 0.0000 532 ASN B O   
8145 C CB  . ASN B 532 ? 161.4145 161.4145 161.4145 0.0000 0.0000 0.0000 532 ASN B CB  
8146 C CG  . ASN B 532 ? 161.1100 161.1100 161.1100 0.0000 0.0000 0.0000 532 ASN B CG  
8147 O OD1 . ASN B 532 ? 160.8872 160.8872 160.8872 0.0000 0.0000 0.0000 532 ASN B OD1 
8148 N ND2 . ASN B 532 ? 160.2046 160.2046 160.2046 0.0000 0.0000 0.0000 532 ASN B ND2 
8149 N N   . PHE B 533 ? 161.3111 161.3111 161.3111 0.0000 0.0000 0.0000 533 PHE B N   
8150 C CA  . PHE B 533 ? 161.3796 161.3796 161.3796 0.0000 0.0000 0.0000 533 PHE B CA  
8151 C C   . PHE B 533 ? 161.4419 161.4419 161.4419 0.0000 0.0000 0.0000 533 PHE B C   
8152 O O   . PHE B 533 ? 160.4673 160.4673 160.4673 0.0000 0.0000 0.0000 533 PHE B O   
8153 C CB  . PHE B 533 ? 161.1132 161.1132 161.1132 0.0000 0.0000 0.0000 533 PHE B CB  
8154 C CG  . PHE B 533 ? 161.0771 161.0771 161.0771 0.0000 0.0000 0.0000 533 PHE B CG  
8155 C CD1 . PHE B 533 ? 160.7534 160.7534 160.7534 0.0000 0.0000 0.0000 533 PHE B CD1 
8156 C CD2 . PHE B 533 ? 161.2087 161.2087 161.2087 0.0000 0.0000 0.0000 533 PHE B CD2 
8157 C CE1 . PHE B 533 ? 161.3933 161.3933 161.3933 0.0000 0.0000 0.0000 533 PHE B CE1 
8158 C CE2 . PHE B 533 ? 161.4974 161.4974 161.4974 0.0000 0.0000 0.0000 533 PHE B CE2 
8159 C CZ  . PHE B 533 ? 161.4987 161.4987 161.4987 0.0000 0.0000 0.0000 533 PHE B CZ  
8160 N N   . CYS B 534 ? 161.4275 161.4275 161.4275 0.0000 0.0000 0.0000 534 CYS B N   
8161 C CA  . CYS B 534 ? 161.5780 161.5780 161.5780 0.0000 0.0000 0.0000 534 CYS B CA  
8162 C C   . CYS B 534 ? 160.4272 160.4272 160.4272 0.0000 0.0000 0.0000 534 CYS B C   
8163 O O   . CYS B 534 ? 159.9121 159.9121 159.9121 0.0000 0.0000 0.0000 534 CYS B O   
8164 C CB  . CYS B 534 ? 157.8920 157.8920 157.8920 0.0000 0.0000 0.0000 534 CYS B CB  
8165 S SG  . CYS B 534 ? 159.3383 159.3383 159.3383 0.0000 0.0000 0.0000 534 CYS B SG  
8166 N N   . THR B 535 ? 160.5917 160.5917 160.5917 0.0000 0.0000 0.0000 535 THR B N   
8167 C CA  . THR B 535 ? 160.2807 160.2807 160.2807 0.0000 0.0000 0.0000 535 THR B CA  
8168 C C   . THR B 535 ? 160.3569 160.3569 160.3569 0.0000 0.0000 0.0000 535 THR B C   
8169 O O   . THR B 535 ? 160.3615 160.3615 160.3615 0.0000 0.0000 0.0000 535 THR B O   
8170 C CB  . THR B 535 ? 159.0035 159.0035 159.0035 0.0000 0.0000 0.0000 535 THR B CB  
8171 O OG1 . THR B 535 ? 159.0523 159.0523 159.0523 0.0000 0.0000 0.0000 535 THR B OG1 
8172 C CG2 . THR B 535 ? 160.7007 160.7007 160.7007 0.0000 0.0000 0.0000 535 THR B CG2 
8173 N N   . ALA B 536 ? 161.1140 161.1140 161.1140 0.0000 0.0000 0.0000 536 ALA B N   
8174 C CA  . ALA B 536 ? 161.1459 161.1459 161.1459 0.0000 0.0000 0.0000 536 ALA B CA  
8175 C C   . ALA B 536 ? 161.1585 161.1585 161.1585 0.0000 0.0000 0.0000 536 ALA B C   
8176 O O   . ALA B 536 ? 161.4729 161.4729 161.4729 0.0000 0.0000 0.0000 536 ALA B O   
8177 C CB  . ALA B 536 ? 161.4130 161.4130 161.4130 0.0000 0.0000 0.0000 536 ALA B CB  
8178 N N   . LEU B 537 ? 161.5992 161.5992 161.5992 0.0000 0.0000 0.0000 537 LEU B N   
8179 C CA  . LEU B 537 ? 161.5716 161.5716 161.5716 0.0000 0.0000 0.0000 537 LEU B CA  
8180 C C   . LEU B 537 ? 161.5547 161.5547 161.5547 0.0000 0.0000 0.0000 537 LEU B C   
8181 O O   . LEU B 537 ? 161.4669 161.4669 161.4669 0.0000 0.0000 0.0000 537 LEU B O   
8182 C CB  . LEU B 537 ? 160.4210 160.4210 160.4210 0.0000 0.0000 0.0000 537 LEU B CB  
8183 C CG  . LEU B 537 ? 160.1102 160.1102 160.1102 0.0000 0.0000 0.0000 537 LEU B CG  
8184 C CD1 . LEU B 537 ? 160.9345 160.9345 160.9345 0.0000 0.0000 0.0000 537 LEU B CD1 
8185 C CD2 . LEU B 537 ? 160.6390 160.6390 160.6390 0.0000 0.0000 0.0000 537 LEU B CD2 
8186 N N   . GLU B 538 ? 161.4812 161.4812 161.4812 0.0000 0.0000 0.0000 538 GLU B N   
8187 C CA  . GLU B 538 ? 161.5417 161.5417 161.5417 0.0000 0.0000 0.0000 538 GLU B CA  
8188 C C   . GLU B 538 ? 161.4956 161.4956 161.4956 0.0000 0.0000 0.0000 538 GLU B C   
8189 O O   . GLU B 538 ? 161.6365 161.6365 161.6365 0.0000 0.0000 0.0000 538 GLU B O   
8190 C CB  . GLU B 538 ? 161.4560 161.4560 161.4560 0.0000 0.0000 0.0000 538 GLU B CB  
8191 C CG  . GLU B 538 ? 161.6224 161.6224 161.6224 0.0000 0.0000 0.0000 538 GLU B CG  
8192 C CD  . GLU B 538 ? 161.5009 161.5009 161.5009 0.0000 0.0000 0.0000 538 GLU B CD  
8193 O OE1 . GLU B 538 ? 161.6643 161.6643 161.6643 0.0000 0.0000 0.0000 538 GLU B OE1 
8194 O OE2 . GLU B 538 ? 161.5016 161.5016 161.5016 0.0000 0.0000 0.0000 538 GLU B OE2 
8195 N N   . TYR B 539 ? 161.3908 161.3908 161.3908 0.0000 0.0000 0.0000 539 TYR B N   
8196 C CA  . TYR B 539 ? 161.4815 161.4815 161.4815 0.0000 0.0000 0.0000 539 TYR B CA  
8197 C C   . TYR B 539 ? 161.3988 161.3988 161.3988 0.0000 0.0000 0.0000 539 TYR B C   
8198 O O   . TYR B 539 ? 161.3456 161.3456 161.3456 0.0000 0.0000 0.0000 539 TYR B O   
8199 C CB  . TYR B 539 ? 161.4067 161.4067 161.4067 0.0000 0.0000 0.0000 539 TYR B CB  
8200 C CG  . TYR B 539 ? 161.4703 161.4703 161.4703 0.0000 0.0000 0.0000 539 TYR B CG  
8201 C CD1 . TYR B 539 ? 161.3373 161.3373 161.3373 0.0000 0.0000 0.0000 539 TYR B CD1 
8202 C CD2 . TYR B 539 ? 161.3447 161.3447 161.3447 0.0000 0.0000 0.0000 539 TYR B CD2 
8203 C CE1 . TYR B 539 ? 161.2854 161.2854 161.2854 0.0000 0.0000 0.0000 539 TYR B CE1 
8204 C CE2 . TYR B 539 ? 161.3172 161.3172 161.3172 0.0000 0.0000 0.0000 539 TYR B CE2 
8205 C CZ  . TYR B 539 ? 215.8440 215.8440 215.8440 0.0000 0.0000 0.0000 539 TYR B CZ  
8206 O OH  . TYR B 539 ? 215.9472 215.9472 215.9472 0.0000 0.0000 0.0000 539 TYR B OH  
8207 N N   . GLY B 540 ? 215.7980 215.7980 215.7980 0.0000 0.0000 0.0000 540 GLY B N   
8208 C CA  . GLY B 540 ? 215.6477 215.6477 215.6477 0.0000 0.0000 0.0000 540 GLY B CA  
8209 C C   . GLY B 540 ? 215.8951 215.8951 215.8951 0.0000 0.0000 0.0000 540 GLY B C   
8210 O O   . GLY B 540 ? 215.8899 215.8899 215.8899 0.0000 0.0000 0.0000 540 GLY B O   
8211 N N   . LEU B 541 ? 215.7468 215.7468 215.7468 0.0000 0.0000 0.0000 541 LEU B N   
8212 C CA  . LEU B 541 ? 217.2595 217.2595 217.2595 0.0000 0.0000 0.0000 541 LEU B CA  
8213 C C   . LEU B 541 ? 217.0661 217.0661 217.0661 0.0000 0.0000 0.0000 541 LEU B C   
8214 O O   . LEU B 541 ? 216.4531 216.4531 216.4531 0.0000 0.0000 0.0000 541 LEU B O   
8215 C CB  . LEU B 541 ? 216.3384 216.3384 216.3384 0.0000 0.0000 0.0000 541 LEU B CB  
8216 C CG  . LEU B 541 ? 217.1737 217.1737 217.1737 0.0000 0.0000 0.0000 541 LEU B CG  
8217 C CD1 . LEU B 541 ? 217.0920 217.0920 217.0920 0.0000 0.0000 0.0000 541 LEU B CD1 
8218 C CD2 . LEU B 541 ? 217.0665 217.0665 217.0665 0.0000 0.0000 0.0000 541 LEU B CD2 
8219 N N   . PRO B 542 ? 217.1410 217.1410 217.1410 0.0000 0.0000 0.0000 542 PRO B N   
8220 C CA  . PRO B 542 ? 201.6672 201.6672 201.6672 0.0000 0.0000 0.0000 542 PRO B CA  
8221 C C   . PRO B 542 ? 201.3611 201.3611 201.3611 0.0000 0.0000 0.0000 542 PRO B C   
8222 O O   . PRO B 542 ? 201.1353 201.1353 201.1353 0.0000 0.0000 0.0000 542 PRO B O   
8223 C CB  . PRO B 542 ? 200.5878 200.5878 200.5878 0.0000 0.0000 0.0000 542 PRO B CB  
8224 C CG  . PRO B 542 ? 201.3313 201.3313 201.3313 0.0000 0.0000 0.0000 542 PRO B CG  
8225 C CD  . PRO B 542 ? 201.3824 201.3824 201.3824 0.0000 0.0000 0.0000 542 PRO B CD  
8226 N N   . PRO B 543 ? 201.6075 201.6075 201.6075 0.0000 0.0000 0.0000 543 PRO B N   
8227 C CA  . PRO B 543 ? 202.9759 202.9759 202.9759 0.0000 0.0000 0.0000 543 PRO B CA  
8228 C C   . PRO B 543 ? 202.8588 202.8588 202.8588 0.0000 0.0000 0.0000 543 PRO B C   
8229 O O   . PRO B 543 ? 202.3747 202.3747 202.3747 0.0000 0.0000 0.0000 543 PRO B O   
8230 C CB  . PRO B 543 ? 201.8079 201.8079 201.8079 0.0000 0.0000 0.0000 543 PRO B CB  
8231 C CG  . PRO B 543 ? 203.0846 203.0846 203.0846 0.0000 0.0000 0.0000 543 PRO B CG  
8232 C CD  . PRO B 543 ? 203.1658 203.1658 203.1658 0.0000 0.0000 0.0000 543 PRO B CD  
8233 N N   . THR B 544 ? 203.0741 203.0741 203.0741 0.0000 0.0000 0.0000 544 THR B N   
8234 C CA  . THR B 544 ? 203.2280 203.2280 203.2280 0.0000 0.0000 0.0000 544 THR B CA  
8235 C C   . THR B 544 ? 198.9227 198.9227 198.9227 0.0000 0.0000 0.0000 544 THR B C   
8236 O O   . THR B 544 ? 198.7228 198.7228 198.7228 0.0000 0.0000 0.0000 544 THR B O   
8237 C CB  . THR B 544 ? 197.6670 197.6670 197.6670 0.0000 0.0000 0.0000 544 THR B CB  
# 
